http://togogenome.org/gene/9606:TLX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43763                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||Pro residues|||T-cell leukemia homeobox protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049336
http://togogenome.org/gene/9606:SUCO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV04|||http://purl.uniprot.org/uniprot/B4DYM4|||http://purl.uniprot.org/uniprot/Q9UBS9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||SUN|||SUN domain-containing ossification factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000065707|||http://purl.uniprot.org/annotation/PRO_5014567694|||http://purl.uniprot.org/annotation/VSP_027921|||http://purl.uniprot.org/annotation/VSP_027922|||http://purl.uniprot.org/annotation/VSP_027923
http://togogenome.org/gene/9606:TUBB4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04350                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||In DYT4.|||In HLD6.|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-4A chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048252|||http://purl.uniprot.org/annotation/VAR_026044|||http://purl.uniprot.org/annotation/VAR_052673|||http://purl.uniprot.org/annotation/VAR_069798|||http://purl.uniprot.org/annotation/VAR_069799
http://togogenome.org/gene/9606:AP3M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRN6|||http://purl.uniprot.org/uniprot/Q9Y2T2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  AP-3 complex subunit mu-1|||MHD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193781
http://togogenome.org/gene/9606:SKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WV1|||http://purl.uniprot.org/uniprot/V9HW03                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes FYB1-dependent activation of ITGAL clustering.|||Abolishes homodimerization, interaction with FYB1 and activation of the MAP kinase pathway.|||Abolishes interaction with PTPRC, translocation to cell membrane upon T-cell stimulation and activation of the MAP kinase pathway. No effect on interaction with FYN or GRB2.|||Acidic residues|||Disordered|||Impairs interaction with FYB1.|||Impairs interaction with PTPRC. No effect on interaction with FYN or GRB2.|||In isoform 2.|||Interaction with FYB1|||No effect on interaction with PTPRC and translocation to cell membrane upon T-cell stimulation. Abolishes interaction with FYN and GRB2 and activation of the MAP kinase pathway.|||PH|||Phosphotyrosine|||Phosphotyrosine; by FYN|||SH3|||Src kinase-associated phosphoprotein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270173|||http://purl.uniprot.org/annotation/VAR_029811|||http://purl.uniprot.org/annotation/VAR_035343|||http://purl.uniprot.org/annotation/VSP_022179
http://togogenome.org/gene/9606:CCDC169                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNP5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 169|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341366|||http://purl.uniprot.org/annotation/VAR_057811|||http://purl.uniprot.org/annotation/VSP_035636|||http://purl.uniprot.org/annotation/VSP_035637|||http://purl.uniprot.org/annotation/VSP_040479|||http://purl.uniprot.org/annotation/VSP_040480|||http://purl.uniprot.org/annotation/VSP_043810|||http://purl.uniprot.org/annotation/VSP_043811
http://togogenome.org/gene/9606:MMS22L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRQ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished interaction with RAD51.|||Does not affect interaction with RAD51.|||Protein MMS22-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260216|||http://purl.uniprot.org/annotation/VAR_029013|||http://purl.uniprot.org/annotation/VAR_029014|||http://purl.uniprot.org/annotation/VAR_029015|||http://purl.uniprot.org/annotation/VAR_029016
http://togogenome.org/gene/9606:H3C10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:TAGLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTL2|||http://purl.uniprot.org/uniprot/P37802                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||Calponin-like|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed|||Transgelin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204786|||http://purl.uniprot.org/annotation/VAR_047903|||http://purl.uniprot.org/annotation/VSP_055311
http://togogenome.org/gene/9606:DHX32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L7V1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAH box|||Disordered|||Helicase ATP-binding|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292663|||http://purl.uniprot.org/annotation/VAR_035843|||http://purl.uniprot.org/annotation/VAR_052181|||http://purl.uniprot.org/annotation/VAR_052182|||http://purl.uniprot.org/annotation/VAR_052183|||http://purl.uniprot.org/annotation/VSP_026427
http://togogenome.org/gene/9606:CYP27C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0S4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Cytochrome P450 27C1|||Disordered|||In isoform 1.|||Mitochondrion|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293732|||http://purl.uniprot.org/annotation/VAR_033120|||http://purl.uniprot.org/annotation/VSP_060866
http://togogenome.org/gene/9606:IL11RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14626|||http://purl.uniprot.org/uniprot/Q5VZ79                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreases proteolyisis by ADAM10.|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like C2-type|||In CRSDA.|||In CRSDA; renders the receptor unable to mediate the IL11 signal.|||In isoform HCR2.|||Interleukin-11 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Soluble interleukin-11 receptor subunit alpha|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010913|||http://purl.uniprot.org/annotation/PRO_0000450688|||http://purl.uniprot.org/annotation/PRO_5014310174|||http://purl.uniprot.org/annotation/VAR_019821|||http://purl.uniprot.org/annotation/VAR_019822|||http://purl.uniprot.org/annotation/VAR_066666|||http://purl.uniprot.org/annotation/VAR_066667|||http://purl.uniprot.org/annotation/VAR_066668|||http://purl.uniprot.org/annotation/VAR_066669|||http://purl.uniprot.org/annotation/VSP_011879
http://togogenome.org/gene/9606:EEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13639                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosyldiphthamide|||Cleavage|||Confers resistance to diphtheria toxin.|||Diphthamide|||Elongation factor 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||In SCA26; compromises the mechanics of translocation.|||N6,N6,N6-trimethyllysine; by EEF2KMT|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Phosphothreonine; by EEF2K|||Phosphotyrosine; by CSK|||Removed|||Strongly reduced phosphorylation at Thr-57.|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091000|||http://purl.uniprot.org/annotation/VAR_070792
http://togogenome.org/gene/9606:ZDHHC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PI61|||http://purl.uniprot.org/uniprot/E9PLR9|||http://purl.uniprot.org/uniprot/Q6UX98                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Extracellular|||Helical|||Palmitoyltransferase DHHC|||Probable palmitoyltransferase ZDHHC24|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233710
http://togogenome.org/gene/9606:HES5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Orange|||Pro residues|||Transcription factor HES-5|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269175
http://togogenome.org/gene/9606:REP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6BDI9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-myristoyl glycine|||Rab15 effector protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323587|||http://purl.uniprot.org/annotation/VAR_039548|||http://purl.uniprot.org/annotation/VAR_039549
http://togogenome.org/gene/9606:NME9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XW9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||NDK|||Thioredoxin|||Thioredoxin domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120161|||http://purl.uniprot.org/annotation/VSP_010375|||http://purl.uniprot.org/annotation/VSP_010376|||http://purl.uniprot.org/annotation/VSP_010377|||http://purl.uniprot.org/annotation/VSP_010378
http://togogenome.org/gene/9606:IQUB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA54                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with spermatogenic failure with radial spoke defects; binding to RSPH3 and calmodulin is abrogated.|||IQ|||IQ and ubiquitin-like domain-containing protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274601|||http://purl.uniprot.org/annotation/VAR_030332|||http://purl.uniprot.org/annotation/VAR_030333|||http://purl.uniprot.org/annotation/VAR_030334|||http://purl.uniprot.org/annotation/VAR_036291|||http://purl.uniprot.org/annotation/VAR_087798|||http://purl.uniprot.org/annotation/VSP_022830|||http://purl.uniprot.org/annotation/VSP_022831
http://togogenome.org/gene/9606:KMT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMN6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||Abolishes interaction with S-adenosyl-L-methionine.|||Basic and acidic residues|||Basic residues|||C2HC pre-PHD-type|||CXXC-type|||Disordered|||FYR C-terminal|||FYR N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase 2B|||In DYT28.|||In DYT28; unknown pathological significance.|||In MRD68.|||Menin-binding motif (MBM)|||N-acetylalanine|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||Removed|||SET|||WDR5 interaction motif (WIN)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124881|||http://purl.uniprot.org/annotation/VAR_046563|||http://purl.uniprot.org/annotation/VAR_046564|||http://purl.uniprot.org/annotation/VAR_046565|||http://purl.uniprot.org/annotation/VAR_052653|||http://purl.uniprot.org/annotation/VAR_052654|||http://purl.uniprot.org/annotation/VAR_052655|||http://purl.uniprot.org/annotation/VAR_061913|||http://purl.uniprot.org/annotation/VAR_080233|||http://purl.uniprot.org/annotation/VAR_080234|||http://purl.uniprot.org/annotation/VAR_080235|||http://purl.uniprot.org/annotation/VAR_080236|||http://purl.uniprot.org/annotation/VAR_080237|||http://purl.uniprot.org/annotation/VAR_080238|||http://purl.uniprot.org/annotation/VAR_080239|||http://purl.uniprot.org/annotation/VAR_080240|||http://purl.uniprot.org/annotation/VAR_080241|||http://purl.uniprot.org/annotation/VAR_080242|||http://purl.uniprot.org/annotation/VAR_080243|||http://purl.uniprot.org/annotation/VAR_081649|||http://purl.uniprot.org/annotation/VAR_087544|||http://purl.uniprot.org/annotation/VAR_087545|||http://purl.uniprot.org/annotation/VAR_087546|||http://purl.uniprot.org/annotation/VAR_087547|||http://purl.uniprot.org/annotation/VAR_087548
http://togogenome.org/gene/9606:ITGB1BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQY5|||http://purl.uniprot.org/uniprot/O14713                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes ITGB1 binding.|||Abolishes KRIT1 binding; when associated with A-93.|||Abolishes KRIT1 binding; when associated with A-96.|||Abolishes nuclear import and transcriptional activity.|||Changes in cell spreading.|||Disordered|||In isoform 2.|||Integrin beta-1-binding protein 1|||Interaction with ITGB1|||Interaction with KRIT1|||No effect on ITGB1 binding.|||Nuclear localization signal|||PID|||Phosphoserine|||Phosphothreonine; by CaMK2|||Polar residues|||Reduces ITGB1 binding.|||Reduces KRIT1 and ITGB1 binding.|||Reduces KRIT1 binding. No effect on ITGB1 binding.|||Stimulates cell spreading on fibronectin to a similar extent as inhibition of CaMKII.|||Strong defect in cell spreading.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084264|||http://purl.uniprot.org/annotation/VSP_003898
http://togogenome.org/gene/9606:SNURF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63162|||http://purl.uniprot.org/uniprot/Q9Y675                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Pro residues|||Repeat-rich region|||SNRPN upstream reading frame protein|||Sm|||Small nuclear ribonucleoprotein-associated protein N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125523|||http://purl.uniprot.org/annotation/PRO_0000312993|||http://purl.uniprot.org/annotation/VSP_056488
http://togogenome.org/gene/9606:LAMP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJQ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell surface localization.|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Lysosome-associated membrane glycoprotein 5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021031|||http://purl.uniprot.org/annotation/VAR_014401|||http://purl.uniprot.org/annotation/VAR_014402|||http://purl.uniprot.org/annotation/VAR_014403|||http://purl.uniprot.org/annotation/VAR_014404|||http://purl.uniprot.org/annotation/VSP_037186
http://togogenome.org/gene/9606:PSMB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL30|||http://purl.uniprot.org/uniprot/Q99436                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Nucleophile|||Proteasome beta subunit C-terminal|||Proteasome subunit beta type-7|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026645|||http://purl.uniprot.org/annotation/PRO_0000026646|||http://purl.uniprot.org/annotation/VAR_013292|||http://purl.uniprot.org/annotation/VSP_056573|||http://purl.uniprot.org/annotation/VSP_056574
http://togogenome.org/gene/9606:STARD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92502                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||No effect on cell morphology when overexpressed.|||Phosphoserine|||Polar residues|||Rho-GAP|||START|||StAR-related lipid transfer protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220676|||http://purl.uniprot.org/annotation/VAR_036588|||http://purl.uniprot.org/annotation/VAR_036589|||http://purl.uniprot.org/annotation/VAR_061816|||http://purl.uniprot.org/annotation/VSP_032984
http://togogenome.org/gene/9606:SEPSECS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4F3|||http://purl.uniprot.org/uniprot/Q9HD40                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PCH2D.|||In PCH2D; abrogates enzyme activity.|||In isoform 2.|||In isoform 3.|||Inactive in vivo.|||Indistinguishable from wild-type.|||Loss of activity.|||May act as a substrate filter by repelling compounds with a negatively charged alpha-carboxylate|||N6-(pyridoxal phosphate)lysine|||O-phosphoseryl-tRNA(Sec) selenium transferase|||Phosphate loop (P-loop)|||Phosphoserine|||SLA/LP epitope|||Tetramerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219875|||http://purl.uniprot.org/annotation/VAR_065585|||http://purl.uniprot.org/annotation/VAR_065586|||http://purl.uniprot.org/annotation/VAR_074163|||http://purl.uniprot.org/annotation/VSP_038078|||http://purl.uniprot.org/annotation/VSP_038079|||http://purl.uniprot.org/annotation/VSP_038080
http://togogenome.org/gene/9606:AK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCS8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Adenylate kinase 1|||Adenylate kinase 2|||Adenylate kinase 3|||Adenylate kinase 9|||Basic and acidic residues|||Disordered|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||LID 1|||LID 2|||LID 3|||NMP 1|||NMP 2|||NMPbind 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304138|||http://purl.uniprot.org/annotation/VSP_028008|||http://purl.uniprot.org/annotation/VSP_028009|||http://purl.uniprot.org/annotation/VSP_028010|||http://purl.uniprot.org/annotation/VSP_028011|||http://purl.uniprot.org/annotation/VSP_039638|||http://purl.uniprot.org/annotation/VSP_039639|||http://purl.uniprot.org/annotation/VSP_039640|||http://purl.uniprot.org/annotation/VSP_039641|||http://purl.uniprot.org/annotation/VSP_039642|||http://purl.uniprot.org/annotation/VSP_039643|||http://purl.uniprot.org/annotation/VSP_039644
http://togogenome.org/gene/9606:FKBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75344                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In SPGF77.|||In isoform 2.|||In isoform 3.|||Inactive peptidyl-prolyl cis-trans isomerase FKBP6|||PPIase FKBP-type|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075329|||http://purl.uniprot.org/annotation/VAR_070840|||http://purl.uniprot.org/annotation/VAR_087742|||http://purl.uniprot.org/annotation/VAR_087743|||http://purl.uniprot.org/annotation/VSP_042038|||http://purl.uniprot.org/annotation/VSP_054251
http://togogenome.org/gene/9606:CFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7H8|||http://purl.uniprot.org/uniprot/P00751                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C3/C5 convertase|||Charge relay system|||Complement factor B|||Complement factor B Ba fragment|||Complement factor B Bb fragment|||Decreases binding to the pro-C3-convertase complex. Does not affect Complement C3 beta chain binding.|||In AHUS4.|||In AHUS4; benign variant.|||In AHUS4; gain-of-function mutation that results in enhanced formation of the C3bBb.|||In allele FA.|||In allele FA; requires 2 nucleotide substitutions.|||In allele S.|||In allele S; may be associated with a reduced risk for age-related macular degeneration.|||In isoform 2.|||May be associated with a reduced risk for age-related macular degeneration.|||N-linked (Glc) (glycation) lysine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027545|||http://purl.uniprot.org/annotation/PRO_0000027546|||http://purl.uniprot.org/annotation/PRO_0000027547|||http://purl.uniprot.org/annotation/PRO_5014275538|||http://purl.uniprot.org/annotation/VAR_006492|||http://purl.uniprot.org/annotation/VAR_006493|||http://purl.uniprot.org/annotation/VAR_006494|||http://purl.uniprot.org/annotation/VAR_006495|||http://purl.uniprot.org/annotation/VAR_016274|||http://purl.uniprot.org/annotation/VAR_016275|||http://purl.uniprot.org/annotation/VAR_016276|||http://purl.uniprot.org/annotation/VAR_016277|||http://purl.uniprot.org/annotation/VAR_016278|||http://purl.uniprot.org/annotation/VAR_063221|||http://purl.uniprot.org/annotation/VAR_063222|||http://purl.uniprot.org/annotation/VAR_063659|||http://purl.uniprot.org/annotation/VAR_063660|||http://purl.uniprot.org/annotation/VAR_063661|||http://purl.uniprot.org/annotation/VAR_063662|||http://purl.uniprot.org/annotation/VAR_063663|||http://purl.uniprot.org/annotation/VAR_063664|||http://purl.uniprot.org/annotation/VSP_005380|||http://purl.uniprot.org/annotation/VSP_005381
http://togogenome.org/gene/9606:MUC5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC84                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  11 X approximate tandem repeats, Ser/Thr-rich|||17 X approximate tandem repeats, Ser/Thr-rich|||23 X approximate tandem repeats, Ser/Thr-rich|||7 X Cys-rich subdomain repeats|||C-linked (Man) tryptophan|||CTCK|||Cys-rich subdomain 1|||Cys-rich subdomain 2|||Cys-rich subdomain 3|||Cys-rich subdomain 4|||Cys-rich subdomain 5|||Cys-rich subdomain 6|||Cys-rich subdomain 7|||Disordered|||HAT 1|||HAT 2|||HAT 3|||Mucin-5B|||N-linked (GlcNAc...) asparagine|||Polar residues|||Poorly secreted.|||TIL 1|||TIL 2|||TIL 3|||VWFC 1|||VWFC 2|||VWFC 3|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019283|||http://purl.uniprot.org/annotation/VAR_014123|||http://purl.uniprot.org/annotation/VAR_056588|||http://purl.uniprot.org/annotation/VAR_059538|||http://purl.uniprot.org/annotation/VAR_059539|||http://purl.uniprot.org/annotation/VAR_059540|||http://purl.uniprot.org/annotation/VAR_059541|||http://purl.uniprot.org/annotation/VAR_063616|||http://purl.uniprot.org/annotation/VAR_063617|||http://purl.uniprot.org/annotation/VAR_063618|||http://purl.uniprot.org/annotation/VAR_063619|||http://purl.uniprot.org/annotation/VAR_063620|||http://purl.uniprot.org/annotation/VAR_063621|||http://purl.uniprot.org/annotation/VAR_063622|||http://purl.uniprot.org/annotation/VAR_063623|||http://purl.uniprot.org/annotation/VAR_063624|||http://purl.uniprot.org/annotation/VAR_063625|||http://purl.uniprot.org/annotation/VAR_063626|||http://purl.uniprot.org/annotation/VAR_063627|||http://purl.uniprot.org/annotation/VAR_063628|||http://purl.uniprot.org/annotation/VAR_063629|||http://purl.uniprot.org/annotation/VAR_063630|||http://purl.uniprot.org/annotation/VAR_063631|||http://purl.uniprot.org/annotation/VAR_063632
http://togogenome.org/gene/9606:UGP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE1|||http://purl.uniprot.org/uniprot/Q16851                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes oligomerization and significantly increases enzymatic activity.|||Critical for end-to-end subunit interaction|||In DEE83; the nucleotide substitution also alters the translation of other alternatively spliced products of the gene globally reducing functional enzyme levels and causing reduced synthesis of UDP-glucose and decreased glycogen biosynthetic process; no effect on protein localization; no effect on UTP:glucose-1-phosphate uridylyltransferase activity.|||In isoform 2.|||Loss of activity; possibly due to folding defect.|||N-acetylserine|||N6-acetyllysine|||No significant loss of activity.|||Oligomerization|||Phosphoserine|||Phosphothreonine|||Removed|||UTP--glucose-1-phosphate uridylyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185752|||http://purl.uniprot.org/annotation/VAR_033042|||http://purl.uniprot.org/annotation/VAR_083746|||http://purl.uniprot.org/annotation/VSP_012834
http://togogenome.org/gene/9606:CREG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUH2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||N-linked (GlcNAc...) asparagine|||Protein CREG2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006206|||http://purl.uniprot.org/annotation/VAR_021252
http://togogenome.org/gene/9606:RNF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination.|||Disordered|||Loss of GGA1-binding.|||Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1.|||Loss of UBE2N-binding. No gain of UBE2L3-binding.|||Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding.|||Loss of phosphorylation and of 14-3-3-binding.|||N-myristoyl glycine|||No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1.|||No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99.|||No effect on UBE2N-binding. Gain of UBE2L3-binding.|||No effect on UBE2N-binding. No gain of UBE2L3-binding.|||No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128.|||No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128.|||PPxY motif|||Phosphoserine|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Pro residues|||RING finger protein 11|||RING-type|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056050|||http://purl.uniprot.org/annotation/VAR_058272
http://togogenome.org/gene/9606:GRHL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL28|||http://purl.uniprot.org/uniprot/Q6ISB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Grainyhead-like protein 2 homolog|||Grh/CP2 DB|||Important for activation of transcription|||In ECTDS.|||In ECTDS; reduced expression; altered cell morphology; impaired tight junctions; adhesion defects; cytoplasmic translocation.|||In isoform 2.|||Loss of activity as transcriptional activator.|||Polar residues|||Transcription activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227994|||http://purl.uniprot.org/annotation/VAR_049293|||http://purl.uniprot.org/annotation/VAR_071989|||http://purl.uniprot.org/annotation/VAR_071990|||http://purl.uniprot.org/annotation/VSP_017642
http://togogenome.org/gene/9606:RETREG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HHX5|||http://purl.uniprot.org/uniprot/Q9H6L5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with ATG8 family proteins and reduces endoplasmic reticulum branching.|||Abolishes interaction with ATG8 family proteins.|||Abolishes phosphorylation and reduces self-association.|||Acidic residues|||Cytoplasmic|||Disordered|||Found in a patient with HSAN2B; uncertain pathological significance; dramatically enhances homooligomerization which results in aberrant endoplasmic reticulum scission and excessive reticulophagy; induces sensory neuron death in vitro.|||Helical|||In isoform 2.|||LIR motif|||Lumenal|||Mildly weakened binding to GABARAP.|||Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-149 and D-151.|||Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-149 and D-153.|||Phosphomimetic mutant which enhances self-association. Enhanced membrane scission activity; when associated with D-151 and D-153.|||Phosphoserine|||Phosphoserine; by CAMK2B|||Polar residues|||Pro residues|||Reduces self-association.|||Reticulon homology domain|||Reticulophagy regulator 1|||Severely impaired binding to GABARAP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288466|||http://purl.uniprot.org/annotation/VAR_032422|||http://purl.uniprot.org/annotation/VAR_068477|||http://purl.uniprot.org/annotation/VSP_025685|||http://purl.uniprot.org/annotation/VSP_025686
http://togogenome.org/gene/9606:NUMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14980|||http://purl.uniprot.org/uniprot/Q3SYK8|||http://purl.uniprot.org/uniprot/Q4LE64                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4.1-binding domain|||Abolishes association with the mitotic spindle.|||Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2015 and A-2055.|||Abolishes association with the mitotic spindle. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2055 and A-2087.|||Abolishes interaction with GPSM2.|||Abolishes nuclear localization.|||Absence of cell membrane association even in anaphase. Increased localization at spindle poles and chromosome congression defects. Does not localize to the cortex in either metaphase or anaphase. Increased randomization of spindle orientation.|||Basic and acidic residues|||Disordered|||GPSM2-binding domain|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head (Globular)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increases localization at the spindle poles. Decreases localization at the cell cortex.|||Increases premature accumulation at the cell membrane of the polar cortical region in prophase and metaphase. Reduces association with the mitotic spindle. Increased randomization of spindle orientation. Increases premature accumulation at the cell cortex during metaphase; when associated with A-2015 and A-2087.|||Membrane-binding domain 1|||Membrane-binding domain 2|||N6-acetyllysine|||No effect on nuclear localization.|||Nuclear localization signal|||Nuclear mitotic apparatus protein 1|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by PLK1|||Phosphotyrosine|||Polar residues|||Tail (Globular)|||Tankyrase-binding domain|||Tubulin-binding domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057998|||http://purl.uniprot.org/annotation/VAR_031679|||http://purl.uniprot.org/annotation/VAR_031680|||http://purl.uniprot.org/annotation/VAR_031681|||http://purl.uniprot.org/annotation/VAR_031682|||http://purl.uniprot.org/annotation/VAR_031683|||http://purl.uniprot.org/annotation/VAR_051248|||http://purl.uniprot.org/annotation/VSP_012910|||http://purl.uniprot.org/annotation/VSP_044378|||http://purl.uniprot.org/annotation/VSP_044379|||http://purl.uniprot.org/annotation/VSP_054146
http://togogenome.org/gene/9606:NUP37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFH4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  In MCPH24; reduced mutant protein levels; impairs assembly of nuclear pore complex as indicated by lower number of nuclear pores in patient fibroblasts.|||Nucleoporin Nup37|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051109|||http://purl.uniprot.org/annotation/VAR_081367
http://togogenome.org/gene/9606:PPP4R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||Phosphoserine|||Serine/threonine-protein phosphatase 4 regulatory subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071527|||http://purl.uniprot.org/annotation/VAR_017807|||http://purl.uniprot.org/annotation/VAR_017808|||http://purl.uniprot.org/annotation/VAR_017809|||http://purl.uniprot.org/annotation/VAR_051748|||http://purl.uniprot.org/annotation/VSP_009469
http://togogenome.org/gene/9606:TMEM202                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITB0|||http://purl.uniprot.org/uniprot/A6NGA9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 202                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317201|||http://purl.uniprot.org/annotation/VAR_051434
http://togogenome.org/gene/9606:USP32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFA0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||DUSP|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||Nucleophile|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||Removed in mature form|||S-farnesyl cysteine|||USP|||Ubiquitin carboxyl-terminal hydrolase 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080663|||http://purl.uniprot.org/annotation/PRO_0000396658|||http://purl.uniprot.org/annotation/VAR_051536|||http://purl.uniprot.org/annotation/VAR_051537|||http://purl.uniprot.org/annotation/VAR_051538|||http://purl.uniprot.org/annotation/VAR_051539|||http://purl.uniprot.org/annotation/VSP_056307|||http://purl.uniprot.org/annotation/VSP_056308
http://togogenome.org/gene/9606:CRADD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJT6|||http://purl.uniprot.org/uniprot/F5H7C2|||http://purl.uniprot.org/uniprot/F8VV49|||http://purl.uniprot.org/uniprot/F8VVY5|||http://purl.uniprot.org/uniprot/P78560|||http://purl.uniprot.org/uniprot/Q53XL1|||http://purl.uniprot.org/uniprot/Q8IY43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CARD|||Death|||Death domain-containing protein CRADD|||Disordered|||In MRT34.|||In isoform 2.|||Loss of interaction with CASP2.|||Loss of interaction with PIDD1.|||Loss of interaction with PIDD1. Decreased PIDDosome assembly. Decreased CASP2 activation.|||Loss of interaction with PIDD1. Loss of PIDDosome assembly. Loss of CASP2 activation.|||No effect on interaction with PIDD1.|||Partial loss of interaction with PIDD1.|||Partial loss of interaction with PIDD1. Decreased PIDDosome assembly. Decreased CASP2 activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079326|||http://purl.uniprot.org/annotation/VAR_067536|||http://purl.uniprot.org/annotation/VSP_056892
http://togogenome.org/gene/9606:ARSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4A0|||http://purl.uniprot.org/uniprot/P15848                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase B|||In MPS6.|||In MPS6; intermediate form.|||In MPS6; intermediate form; severe reduction of activity.|||In MPS6; mild form.|||In MPS6; mild form; severe reduction of activity.|||In MPS6; mild/intermediate.|||In MPS6; mild/severe form.|||In MPS6; severe form.|||In MPS6; severe form; loss of activity.|||In MPS6; severe form; low protein levels and activity.|||In MPS6; severe form; severe reduction of activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Or 38|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033421|||http://purl.uniprot.org/annotation/PRO_5002722144|||http://purl.uniprot.org/annotation/VAR_007294|||http://purl.uniprot.org/annotation/VAR_007295|||http://purl.uniprot.org/annotation/VAR_007296|||http://purl.uniprot.org/annotation/VAR_007297|||http://purl.uniprot.org/annotation/VAR_007298|||http://purl.uniprot.org/annotation/VAR_007299|||http://purl.uniprot.org/annotation/VAR_007300|||http://purl.uniprot.org/annotation/VAR_007301|||http://purl.uniprot.org/annotation/VAR_007302|||http://purl.uniprot.org/annotation/VAR_007303|||http://purl.uniprot.org/annotation/VAR_007304|||http://purl.uniprot.org/annotation/VAR_007305|||http://purl.uniprot.org/annotation/VAR_007306|||http://purl.uniprot.org/annotation/VAR_016061|||http://purl.uniprot.org/annotation/VAR_019017|||http://purl.uniprot.org/annotation/VAR_019018|||http://purl.uniprot.org/annotation/VAR_019019|||http://purl.uniprot.org/annotation/VAR_019020|||http://purl.uniprot.org/annotation/VAR_019021|||http://purl.uniprot.org/annotation/VAR_019022|||http://purl.uniprot.org/annotation/VAR_019023|||http://purl.uniprot.org/annotation/VAR_019024|||http://purl.uniprot.org/annotation/VAR_019025|||http://purl.uniprot.org/annotation/VAR_019026|||http://purl.uniprot.org/annotation/VAR_019027|||http://purl.uniprot.org/annotation/VAR_019028|||http://purl.uniprot.org/annotation/VAR_019029|||http://purl.uniprot.org/annotation/VAR_019030|||http://purl.uniprot.org/annotation/VAR_019031|||http://purl.uniprot.org/annotation/VAR_019032|||http://purl.uniprot.org/annotation/VAR_019033|||http://purl.uniprot.org/annotation/VAR_019034|||http://purl.uniprot.org/annotation/VAR_061883|||http://purl.uniprot.org/annotation/VAR_080270|||http://purl.uniprot.org/annotation/VSP_042721
http://togogenome.org/gene/9606:KIAA1191                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT18|||http://purl.uniprot.org/uniprot/Q96A73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Flavin-containing monooxygenase motif|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Putative monooxygenase p33MONOX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307730|||http://purl.uniprot.org/annotation/VSP_028800|||http://purl.uniprot.org/annotation/VSP_028801
http://togogenome.org/gene/9606:CDC25A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30304                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphatase activity.|||Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation.|||Abrogates 14-3-3 protein binding; increases binding to cyclin B1.|||Abrogates binding to CCNB1; when associated with L-514.|||Abrogates binding to CCNB1; when associated with L-520.|||Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination.|||Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293.|||Basic and acidic residues|||Disordered|||In isoform 2.|||Increased stability following IR treatment.|||Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279.|||Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293.|||Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding.|||KEN box|||M-phase inducer phosphatase 1|||Mimicks phosphorylation state, leading to promote degradation following IR treatment.|||Phosphodegron|||Phosphoserine|||Phosphoserine; by CHEK1|||Phosphoserine; by CHEK1 and CHEK2|||Phosphoserine; by NEK11|||Phosphoserine; by PLK3|||Phosphothreonine; by CHEK1|||Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex.|||Rhodanese                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198641|||http://purl.uniprot.org/annotation/VAR_020932|||http://purl.uniprot.org/annotation/VAR_023532|||http://purl.uniprot.org/annotation/VAR_023533|||http://purl.uniprot.org/annotation/VSP_000860
http://togogenome.org/gene/9606:METTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRN9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In METTL5-3A; abolished methyltransferase activity.|||Unknown pathological significance; found in patients with intellectual disability and microcephaly; impaired interaction with TRMT112.|||rRNA N6-adenosine-methyltransferase METTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251919|||http://purl.uniprot.org/annotation/VAR_051507|||http://purl.uniprot.org/annotation/VAR_086154
http://togogenome.org/gene/9606:MRPL53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EL3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL53|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261664|||http://purl.uniprot.org/annotation/VAR_029475
http://togogenome.org/gene/9606:TARS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RTX5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||TGS|||Threonine--tRNA ligase 2, cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333828|||http://purl.uniprot.org/annotation/VSP_033562
http://togogenome.org/gene/9606:UBE2U                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY9|||http://purl.uniprot.org/uniprot/Q5VVX9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||In isoform 2.|||UBC core|||Ubiquitin-conjugating enzyme E2 U                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082512|||http://purl.uniprot.org/annotation/VAR_057323|||http://purl.uniprot.org/annotation/VSP_016003
http://togogenome.org/gene/9606:FN3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H479                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue                                                                                  ^@                                                                                  Fructosamine-3-kinase|||N-acetylmethionine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216337
http://togogenome.org/gene/9606:SLC14A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFJ8|||http://purl.uniprot.org/uniprot/B4DHU3|||http://purl.uniprot.org/uniprot/F5GWS2|||http://purl.uniprot.org/uniprot/G0W2N5|||http://purl.uniprot.org/uniprot/Q13336                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||Important for channel permeability|||In Jk(b).|||In Jk(null).|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Urea transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065737|||http://purl.uniprot.org/annotation/VAR_005669|||http://purl.uniprot.org/annotation/VAR_013752|||http://purl.uniprot.org/annotation/VAR_022319|||http://purl.uniprot.org/annotation/VAR_051483|||http://purl.uniprot.org/annotation/VAR_051484|||http://purl.uniprot.org/annotation/VAR_065466|||http://purl.uniprot.org/annotation/VAR_065467|||http://purl.uniprot.org/annotation/VAR_065468|||http://purl.uniprot.org/annotation/VSP_041573
http://togogenome.org/gene/9606:PDCD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEG3|||http://purl.uniprot.org/uniprot/Q8N8D1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Pro residues|||Programmed cell death protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058269
http://togogenome.org/gene/9606:LYNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP58                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated cysteine|||In isoform 2.|||Ly-6/neurotoxin-like protein 1|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036154|||http://purl.uniprot.org/annotation/PRO_0000440641|||http://purl.uniprot.org/annotation/VSP_058978
http://togogenome.org/gene/9606:RNF181                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0P0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF181|||Phosphothreonine|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295174|||http://purl.uniprot.org/annotation/VAR_033323
http://togogenome.org/gene/9606:RBMXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||RNA binding motif protein, X-linked-like-1|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000408005
http://togogenome.org/gene/9606:NUDT22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity with UDP-galactose.|||Disordered|||In isoform 2.|||In isoform 3.|||Nudix box|||Nudix hydrolase|||Uridine diphosphate glucose pyrophosphatase NUDT22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263731|||http://purl.uniprot.org/annotation/VAR_029616|||http://purl.uniprot.org/annotation/VAR_029617|||http://purl.uniprot.org/annotation/VAR_029618|||http://purl.uniprot.org/annotation/VAR_050414|||http://purl.uniprot.org/annotation/VSP_021884|||http://purl.uniprot.org/annotation/VSP_053790
http://togogenome.org/gene/9606:ANKRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9E1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat family A protein 2|||Decreased affinity for HDAC4.|||Loss of interaction with CCDC8. Decreased affinity for HDAC4.|||No effect on interaction with CCDC8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066895
http://togogenome.org/gene/9606:DDX20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4N4|||http://purl.uniprot.org/uniprot/Q9UHI6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable ATP-dependent RNA helicase DDX20|||Q motif|||SMN interacting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055025|||http://purl.uniprot.org/annotation/VAR_057231|||http://purl.uniprot.org/annotation/VAR_057232|||http://purl.uniprot.org/annotation/VAR_057233|||http://purl.uniprot.org/annotation/VSP_056505|||http://purl.uniprot.org/annotation/VSP_056506
http://togogenome.org/gene/9606:MMP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPA2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Lipid Binding|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Cysteine switch|||Disordered|||GPI-anchor amidated alanine|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-25|||Pro residues|||Removed in mature form|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028852|||http://purl.uniprot.org/annotation/PRO_0000028853|||http://purl.uniprot.org/annotation/PRO_0000028854
http://togogenome.org/gene/9606:BTLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6A9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B- and T-lymphocyte attenuator|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-257.|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-282.|||No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-257 and/or F-282.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014523|||http://purl.uniprot.org/annotation/VAR_027607|||http://purl.uniprot.org/annotation/VAR_027608|||http://purl.uniprot.org/annotation/VAR_056027|||http://purl.uniprot.org/annotation/VSP_040305
http://togogenome.org/gene/9606:GSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2LYG3|||http://purl.uniprot.org/uniprot/Q9BZM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||GS homeobox 2|||Homeobox|||In DMJDS2; decreased protein abundance; decreased nuclear localization; increased localization to the cytoplasm; changed regulation of gene expression.|||In DMJDS2; loss of protein expression.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048896|||http://purl.uniprot.org/annotation/VAR_049580|||http://purl.uniprot.org/annotation/VAR_083532|||http://purl.uniprot.org/annotation/VAR_083533
http://togogenome.org/gene/9606:SRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12931                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In THC6; increased protein tyrosine kinase activity; increased autophosphorylation at Y-419; causes defective megakaryopoiesis associated with increased overall tyrosine phosphorylation in megakaryocytes.|||In isoform 2.|||In isoform 3.|||Kinase active. Interacts with PDLIM4; when associated with E-302 and F-419.|||Kinase active. Interacts with PDLIM4; when associated with E-307 and F-419.|||Kinase inactive. Abolishes ubiquitination promoted by CBLC.|||Loss of kinase activity. Loss of interaction with PDLIM4.|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphotyrosine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by FAK2|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proto-oncogene tyrosine-protein kinase Src|||Proton acceptor|||Removed|||SH2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088141|||http://purl.uniprot.org/annotation/VAR_041830|||http://purl.uniprot.org/annotation/VAR_051699|||http://purl.uniprot.org/annotation/VAR_076919|||http://purl.uniprot.org/annotation/VSP_012134|||http://purl.uniprot.org/annotation/VSP_061494
http://togogenome.org/gene/9606:AP1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61966                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP-1 complex subunit sigma-1A|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193797|||http://purl.uniprot.org/annotation/VSP_000171
http://togogenome.org/gene/9606:ISY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 1.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor ISY1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235813|||http://purl.uniprot.org/annotation/VSP_039410|||http://purl.uniprot.org/annotation/VSP_039411
http://togogenome.org/gene/9606:BCL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWW9|||http://purl.uniprot.org/uniprot/A2TDT2|||http://purl.uniprot.org/uniprot/O95999                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished homomultimerization and formation of a CBM complex, abolished ability to activate NF-kappa-B.|||Abolished homomultimerization and formation of a CBM complex.|||Abolishes MALT1-mediated cleavage.|||Abolishes NF-kappa-B activation and homo/heterodimerization.|||Abolishes NF-kappa-B activation.|||Abolishes cell death-inducing capability.|||B-cell lymphoma/leukemia 10|||CARD|||Cleavage; by MALT1|||Complete loss of IKBKB/IKKB-mediated phosphorylation.|||Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-31 and R-63.|||Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-31. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-31.|||Decreased ubiquitination and ability to bind NEMO; when associated with 63-R--R-67. Decreased ubiquitination and ability to bind NEMO, impaired ability to activate NF-kappa-B; when associated with R-63. Decreased linear ubiquitination and impaired ability to activate NF-kappa-B; when associated with R-17 and R-63.|||Decreased ubiquitination and ability to bind NEMO; when associated with R-31.|||Disordered|||Does not affect ubiquitination and ability to bind NEMO.|||Found in a MALT lymphoma sample; unknown pathological significance.|||Found in a follicular lymphoma sample; unknown pathological significance.|||Found in a germ cell tumor and other cancer cell lines; unknown pathological significance.|||Found in a germ cell tumor sample; unknown pathological significance.|||Found in a mesothelioma sample; unknown pathological significance.|||Found in a testicular teratoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Promotes NF-kappa-B activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144074|||http://purl.uniprot.org/annotation/VAR_013208|||http://purl.uniprot.org/annotation/VAR_013209|||http://purl.uniprot.org/annotation/VAR_013210|||http://purl.uniprot.org/annotation/VAR_013211|||http://purl.uniprot.org/annotation/VAR_013212|||http://purl.uniprot.org/annotation/VAR_013213|||http://purl.uniprot.org/annotation/VAR_013214|||http://purl.uniprot.org/annotation/VAR_013215|||http://purl.uniprot.org/annotation/VAR_013216|||http://purl.uniprot.org/annotation/VAR_013217|||http://purl.uniprot.org/annotation/VAR_013218|||http://purl.uniprot.org/annotation/VAR_013219|||http://purl.uniprot.org/annotation/VAR_013220|||http://purl.uniprot.org/annotation/VAR_013221|||http://purl.uniprot.org/annotation/VAR_013222|||http://purl.uniprot.org/annotation/VAR_013223|||http://purl.uniprot.org/annotation/VAR_013224|||http://purl.uniprot.org/annotation/VAR_013225|||http://purl.uniprot.org/annotation/VAR_013226|||http://purl.uniprot.org/annotation/VAR_077898
http://togogenome.org/gene/9606:KCNJ9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92806                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 3|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||PDZ-binding|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154950|||http://purl.uniprot.org/annotation/VAR_023568
http://togogenome.org/gene/9606:FOXE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A1EII5|||http://purl.uniprot.org/uniprot/Q13461                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein E3|||In AAT11.|||In ASGD2; complete loss of DNA binding; significant reduction of sequence-specific DNA binding transcription factor activity.|||In ASGD2; significant reduction of sequence-specific DNA binding transcription factor activity.|||In ASGD2; unknown pathological significance.|||In CTRCT34; decreases DNAJB1 expression.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091829|||http://purl.uniprot.org/annotation/VAR_026234|||http://purl.uniprot.org/annotation/VAR_026235|||http://purl.uniprot.org/annotation/VAR_062582|||http://purl.uniprot.org/annotation/VAR_062583|||http://purl.uniprot.org/annotation/VAR_062584|||http://purl.uniprot.org/annotation/VAR_072783|||http://purl.uniprot.org/annotation/VAR_078112|||http://purl.uniprot.org/annotation/VAR_078113|||http://purl.uniprot.org/annotation/VAR_078114|||http://purl.uniprot.org/annotation/VAR_078115
http://togogenome.org/gene/9606:EYA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99504                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eyes absent homolog 3|||Fails to form damage-dependent nuclear foci or interact with H2AX.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Loss of tyrosine phosphatase activity toward H2AX.|||N-acetylmethionine|||Nucleophile|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218648|||http://purl.uniprot.org/annotation/VSP_001493|||http://purl.uniprot.org/annotation/VSP_054518|||http://purl.uniprot.org/annotation/VSP_054519|||http://purl.uniprot.org/annotation/VSP_054530
http://togogenome.org/gene/9606:KCTD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD8|||Basic and acidic residues|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251481|||http://purl.uniprot.org/annotation/VAR_027692
http://togogenome.org/gene/9606:ANAPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Anaphase-promoting complex subunit 2|||Cullin homology|||Disordered|||Impairs UBE2S-mediated polyubiquitination, decreasing substrate affinity, does not affect UBE2C-mediated multiubiquitination; when associated with K-350.|||Impairs UBE2S-mediated polyubiquitination, decreasing substrate affinity, does not affect UBE2C-mediated multiubiquitination; when associated with K-353.|||In isoform 2.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119811|||http://purl.uniprot.org/annotation/VSP_008463
http://togogenome.org/gene/9606:CHD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GWX5|||http://purl.uniprot.org/uniprot/Q14839                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Chromo|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 4|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In SIHIWES.|||In SIHIWES; no effect on interaction with HDAC1; no effect on nuclear localization.|||In SIHIWES; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine; alternate|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with PCNT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080228|||http://purl.uniprot.org/annotation/VAR_031674|||http://purl.uniprot.org/annotation/VAR_031675|||http://purl.uniprot.org/annotation/VAR_031676|||http://purl.uniprot.org/annotation/VAR_077146|||http://purl.uniprot.org/annotation/VAR_077147|||http://purl.uniprot.org/annotation/VAR_077148|||http://purl.uniprot.org/annotation/VAR_077149|||http://purl.uniprot.org/annotation/VAR_077150|||http://purl.uniprot.org/annotation/VAR_077151|||http://purl.uniprot.org/annotation/VAR_077152|||http://purl.uniprot.org/annotation/VSP_011416
http://togogenome.org/gene/9606:HAPSTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0TBJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||HUWE1-associated protein modifying stress responses 2|||Loss of homodimerization. Loss of heterodimerization with HAPSTR1. No effect on interaction with HUWE1.|||Nuclear localization signal|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000457925
http://togogenome.org/gene/9606:ROR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01974                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical|||Ig-like C2-type|||In RRS1.|||In a colorectal adenocarcinoma sample; somatic mutation.|||Kringle|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Slight increase in kinase activity.|||Sulfoserine; partial|||Tyrosine-protein kinase transmembrane receptor ROR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024460|||http://purl.uniprot.org/annotation/VAR_010768|||http://purl.uniprot.org/annotation/VAR_010769|||http://purl.uniprot.org/annotation/VAR_010770|||http://purl.uniprot.org/annotation/VAR_010771|||http://purl.uniprot.org/annotation/VAR_010911|||http://purl.uniprot.org/annotation/VAR_010912|||http://purl.uniprot.org/annotation/VAR_010913|||http://purl.uniprot.org/annotation/VAR_041787|||http://purl.uniprot.org/annotation/VAR_041788|||http://purl.uniprot.org/annotation/VAR_041789|||http://purl.uniprot.org/annotation/VAR_041790|||http://purl.uniprot.org/annotation/VAR_041791|||http://purl.uniprot.org/annotation/VAR_041792|||http://purl.uniprot.org/annotation/VAR_041793|||http://purl.uniprot.org/annotation/VAR_041794|||http://purl.uniprot.org/annotation/VAR_041795|||http://purl.uniprot.org/annotation/VAR_041796|||http://purl.uniprot.org/annotation/VAR_041797|||http://purl.uniprot.org/annotation/VAR_041798|||http://purl.uniprot.org/annotation/VAR_041799
http://togogenome.org/gene/9606:OR4C12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R67                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150533|||http://purl.uniprot.org/annotation/VAR_034192
http://togogenome.org/gene/9606:VWA5B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF13|||http://purl.uniprot.org/uniprot/E9PF42|||http://purl.uniprot.org/uniprot/Q8N398|||http://purl.uniprot.org/uniprot/Q9BVH8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339302|||http://purl.uniprot.org/annotation/VAR_043939
http://togogenome.org/gene/9606:KRTAP10-12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60413                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||19 X 5 AA repeats of C-C-X(3)|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185220|||http://purl.uniprot.org/annotation/VAR_053465|||http://purl.uniprot.org/annotation/VAR_053466
http://togogenome.org/gene/9606:ABI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG21|||http://purl.uniprot.org/uniprot/A0A7D9NKC8|||http://purl.uniprot.org/uniprot/B7Z836|||http://purl.uniprot.org/uniprot/Q9NYB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abl interactor 2|||Acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a consanguineous family with intellectual disability.|||SH3|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191790|||http://purl.uniprot.org/annotation/VAR_080776|||http://purl.uniprot.org/annotation/VSP_010759|||http://purl.uniprot.org/annotation/VSP_010760|||http://purl.uniprot.org/annotation/VSP_010761|||http://purl.uniprot.org/annotation/VSP_010762|||http://purl.uniprot.org/annotation/VSP_010763
http://togogenome.org/gene/9606:CSRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBB5|||http://purl.uniprot.org/uniprot/Q16527                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif                                                                                  ^@                                                                                  Cysteine and glycine-rich protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075721
http://togogenome.org/gene/9606:NRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54845                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||Disordered|||Found in a patient with atypical retinitis pigmentosa and a patient with cone dysfunction; unknown pathological significance; no effect on phosphorylation; no effect on subcellular localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In RDCP; alters phosphorylation; no effect on subcellular localization; loss of transcriptional coactivator activity.|||In RDCP; unknown pathological significance; alters phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity.|||In RP27.|||In RP27; autosomal dominant; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity.|||In RP27; decreases phosphorylation; no effect on subcellular localization; increased transactivational activity; increased transcriptional coactivator activity.|||In RP27; decreases phosphorylation; no effect on subcellular localization; increased transcriptional coactivator activity.|||In RP27; increased transactivational activity.|||In RP27; no effect on phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity.|||In RP27; unknown pathological significance; alters phosphorylation; no effect on subcellular localization; no effect on transcriptional coactivator activity.|||In isoform 2.|||Leucine-zipper|||Minimal transactivation domain (MTD)|||Neural retina-specific leucine zipper protein|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076633|||http://purl.uniprot.org/annotation/VAR_009268|||http://purl.uniprot.org/annotation/VAR_064977|||http://purl.uniprot.org/annotation/VAR_068364|||http://purl.uniprot.org/annotation/VAR_079382|||http://purl.uniprot.org/annotation/VAR_079383|||http://purl.uniprot.org/annotation/VAR_079384|||http://purl.uniprot.org/annotation/VAR_079385|||http://purl.uniprot.org/annotation/VAR_079386|||http://purl.uniprot.org/annotation/VAR_079387|||http://purl.uniprot.org/annotation/VAR_079388|||http://purl.uniprot.org/annotation/VAR_079389|||http://purl.uniprot.org/annotation/VAR_079390|||http://purl.uniprot.org/annotation/VAR_079391|||http://purl.uniprot.org/annotation/VSP_055567
http://togogenome.org/gene/9606:CYB5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384ME44|||http://purl.uniprot.org/uniprot/P00167                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b5|||Cytochrome b5 heme-binding|||Helical|||In METAG.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166010|||http://purl.uniprot.org/annotation/VAR_080833|||http://purl.uniprot.org/annotation/VAR_080834|||http://purl.uniprot.org/annotation/VSP_001240|||http://purl.uniprot.org/annotation/VSP_001241|||http://purl.uniprot.org/annotation/VSP_045367
http://togogenome.org/gene/9606:OR2B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58173                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2B6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150462|||http://purl.uniprot.org/annotation/VAR_024090|||http://purl.uniprot.org/annotation/VAR_053131
http://togogenome.org/gene/9606:NSUN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8I8|||http://purl.uniprot.org/uniprot/Q96CB9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  5-methylcytosine rRNA methyltransferase NSUN4|||Disrupts complex with MTERFD2; when associated with A-136, R-139 and A-141.|||Disrupts complex with MTERFD2; when associated with R-65, A-136 and R-139.|||Disrupts complex with MTERFD2; when associated with R-65, A-136, and A-141.|||Disrupts complex with MTERFD2; when associated with R-65, R-139 and A-141.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||Nucleophile|||Phosphoserine|||SAM-dependent MTase RsmB/NOP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289234|||http://purl.uniprot.org/annotation/VAR_032606|||http://purl.uniprot.org/annotation/VAR_032607|||http://purl.uniprot.org/annotation/VAR_032608|||http://purl.uniprot.org/annotation/VAR_032609|||http://purl.uniprot.org/annotation/VSP_025971|||http://purl.uniprot.org/annotation/VSP_025972|||http://purl.uniprot.org/annotation/VSP_025973|||http://purl.uniprot.org/annotation/VSP_045053
http://togogenome.org/gene/9606:TSPAN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X235|||http://purl.uniprot.org/uniprot/F1T0E7|||http://purl.uniprot.org/uniprot/F1T0E8|||http://purl.uniprot.org/uniprot/Q6PJ65|||http://purl.uniprot.org/uniprot/Q9H1Z9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Tetraspanin-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219255|||http://purl.uniprot.org/annotation/VAR_057277|||http://purl.uniprot.org/annotation/VAR_061849
http://togogenome.org/gene/9606:ANKRD26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ESJ3|||http://purl.uniprot.org/uniprot/Q9UPS8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 26|||Basic and acidic residues|||CCDC144C-like coiled-coil|||DUF3496|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240843|||http://purl.uniprot.org/annotation/VAR_026833|||http://purl.uniprot.org/annotation/VAR_026834|||http://purl.uniprot.org/annotation/VAR_026835|||http://purl.uniprot.org/annotation/VAR_055513|||http://purl.uniprot.org/annotation/VAR_055514|||http://purl.uniprot.org/annotation/VAR_080646|||http://purl.uniprot.org/annotation/VSP_019434|||http://purl.uniprot.org/annotation/VSP_019435
http://togogenome.org/gene/9606:PIH1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWB5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PIH1 domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307334|||http://purl.uniprot.org/annotation/VAR_035415|||http://purl.uniprot.org/annotation/VSP_054022|||http://purl.uniprot.org/annotation/VSP_054023|||http://purl.uniprot.org/annotation/VSP_054024|||http://purl.uniprot.org/annotation/VSP_054025
http://togogenome.org/gene/9606:MCM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z662|||http://purl.uniprot.org/uniprot/Q9NXL9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA helicase MCM9|||Disordered|||In isoform 4.|||In isoform M.|||In isoform S.|||Loss of helicase activity and DNA mismatch repair function but does not affect the interaction with MCM8, MSH2 or chromatin; when associated with A-358.|||Loss of helicase activity and DNA mismatch repair function but does not affect the interaction with MCM8, MSH2 or chromatin; when associated with A-482.|||MCM|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089513|||http://purl.uniprot.org/annotation/VSP_028013|||http://purl.uniprot.org/annotation/VSP_028014|||http://purl.uniprot.org/annotation/VSP_044180|||http://purl.uniprot.org/annotation/VSP_044181|||http://purl.uniprot.org/annotation/VSP_047462|||http://purl.uniprot.org/annotation/VSP_047463
http://togogenome.org/gene/9606:SMU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0MNN4|||http://purl.uniprot.org/uniprot/Q2TAY7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  CTLH|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||LisH|||N-acetylmethionine|||N-acetylserine; in WD40 repeat-containing protein SMU1, N-terminally processed|||Removed; alternate|||Required for interaction with IK and with influenza A virus RNA polymerase|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD40 repeat-containing protein SMU1|||WD40 repeat-containing protein SMU1, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237590|||http://purl.uniprot.org/annotation/PRO_0000424520|||http://purl.uniprot.org/annotation/VSP_056394
http://togogenome.org/gene/9606:CCDC69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI79|||http://purl.uniprot.org/uniprot/Q7L2X4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 69|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328962|||http://purl.uniprot.org/annotation/VAR_042584
http://togogenome.org/gene/9606:CA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3D0|||http://purl.uniprot.org/uniprot/Q16790                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Alpha-carbonic anhydrase|||Basic and acidic residues|||Carbonic anhydrase|||Carbonic anhydrase 9|||Catalytic|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||O-linked (GlcNAc...) threonine|||Phosphotyrosine|||Proteoglycan-like (PG)|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004243|||http://purl.uniprot.org/annotation/PRO_5006608191|||http://purl.uniprot.org/annotation/VAR_010787|||http://purl.uniprot.org/annotation/VAR_020049
http://togogenome.org/gene/9606:PIWIL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG8|||http://purl.uniprot.org/uniprot/Q7Z3Z4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||PAZ|||Piwi|||Piwi-like protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234572|||http://purl.uniprot.org/annotation/VAR_026291|||http://purl.uniprot.org/annotation/VAR_028367|||http://purl.uniprot.org/annotation/VAR_055533|||http://purl.uniprot.org/annotation/VAR_061025|||http://purl.uniprot.org/annotation/VSP_021031|||http://purl.uniprot.org/annotation/VSP_021032|||http://purl.uniprot.org/annotation/VSP_021033|||http://purl.uniprot.org/annotation/VSP_036665
http://togogenome.org/gene/9606:GLI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNF7|||http://purl.uniprot.org/uniprot/P08151                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In PAPA8.|||In PAPA8; decreased transcriptional activity; reduced expression of the GLI1 target PTCH1 observed in patient fibroblasts after chemical induction of the hedgehog pathway.|||In PPD1; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with DNA|||Interaction with SUFU|||N6-acetyllysine|||Polar residues|||Pro residues|||SNAG domain|||Zinc finger protein GLI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047197|||http://purl.uniprot.org/annotation/VAR_015114|||http://purl.uniprot.org/annotation/VAR_015115|||http://purl.uniprot.org/annotation/VAR_015116|||http://purl.uniprot.org/annotation/VAR_035557|||http://purl.uniprot.org/annotation/VAR_035558|||http://purl.uniprot.org/annotation/VAR_035559|||http://purl.uniprot.org/annotation/VAR_052723|||http://purl.uniprot.org/annotation/VAR_081480|||http://purl.uniprot.org/annotation/VAR_081481|||http://purl.uniprot.org/annotation/VAR_081482|||http://purl.uniprot.org/annotation/VAR_082590|||http://purl.uniprot.org/annotation/VSP_042215|||http://purl.uniprot.org/annotation/VSP_054829
http://togogenome.org/gene/9606:RGS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14921                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  RGS|||Regulator of G-protein signaling 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204215|||http://purl.uniprot.org/annotation/VAR_034453
http://togogenome.org/gene/9606:RGS9BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS82                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Anchor for type IV membrane protein|||Regulator of G-protein signaling 9-binding protein|||SNARE-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287586|||http://purl.uniprot.org/annotation/VAR_032333
http://togogenome.org/gene/9606:SPDYE6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CI01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Speedy protein E6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000399478
http://togogenome.org/gene/9606:HOXB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPJ1|||http://purl.uniprot.org/uniprot/P17482                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein Hox-B9|||Hox9 N-terminal activation|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200155
http://togogenome.org/gene/9606:FECH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22830                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decreased activity.|||Ferrochelatase, mitochondrial|||Greatly reduced activity.|||In EPP1.|||In EPP1; enzyme almost inactive.|||In EPP1; enzyme retains 12% of activity.|||In EPP1; enzyme retains 18% of activity.|||In EPP1; enzyme retains 19% of activity.|||In EPP1; enzyme retains 37% of activity.|||In EPP1; enzyme retains 52% of activity.|||In EPP1; enzyme retains 72% of activity.|||In EPP1; enzyme totally inactive.|||In EPP1; loss of activity.|||In EPP1; no detectable enzymatic activity.|||In EPP1; reduced activity.|||In EPP1; unchanged activity; but increased thermolability.|||In isoform 2.|||Increases activity inhibition upon interaction with PGRMC1.|||Loss of activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008873|||http://purl.uniprot.org/annotation/VAR_002383|||http://purl.uniprot.org/annotation/VAR_002384|||http://purl.uniprot.org/annotation/VAR_002385|||http://purl.uniprot.org/annotation/VAR_002386|||http://purl.uniprot.org/annotation/VAR_002387|||http://purl.uniprot.org/annotation/VAR_012028|||http://purl.uniprot.org/annotation/VAR_030553|||http://purl.uniprot.org/annotation/VAR_030554|||http://purl.uniprot.org/annotation/VAR_030555|||http://purl.uniprot.org/annotation/VAR_030556|||http://purl.uniprot.org/annotation/VAR_030557|||http://purl.uniprot.org/annotation/VAR_030558|||http://purl.uniprot.org/annotation/VAR_030559|||http://purl.uniprot.org/annotation/VAR_030560|||http://purl.uniprot.org/annotation/VAR_030561|||http://purl.uniprot.org/annotation/VAR_030562|||http://purl.uniprot.org/annotation/VAR_030563|||http://purl.uniprot.org/annotation/VAR_030564|||http://purl.uniprot.org/annotation/VAR_030565|||http://purl.uniprot.org/annotation/VAR_030566|||http://purl.uniprot.org/annotation/VAR_030567|||http://purl.uniprot.org/annotation/VAR_030568|||http://purl.uniprot.org/annotation/VAR_030569|||http://purl.uniprot.org/annotation/VAR_030570|||http://purl.uniprot.org/annotation/VAR_030571|||http://purl.uniprot.org/annotation/VAR_054629|||http://purl.uniprot.org/annotation/VSP_041208
http://togogenome.org/gene/9606:ACTN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3G9|||http://purl.uniprot.org/uniprot/H7C144|||http://purl.uniprot.org/uniprot/O43707                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Alpha-actinin-4|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||EF-hand|||EF-hand 1|||EF-hand 2|||In FSGS1.|||In FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity.|||In FSGS1; unknown pathological significance.|||In isoform 3.|||In isoform ACTN4ISO.|||Interaction with VCL|||LXXLL motif|||Mediates interaction with MICALL2|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polyphosphoinositide (PIP2)-binding|||Rare variant found in patients with IgA nephropathy; unknown pathological significance.|||Reduced interaction with RARA. Loss of the transcriptional coac tivator activity toward RARA.|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073440|||http://purl.uniprot.org/annotation/VAR_010378|||http://purl.uniprot.org/annotation/VAR_010379|||http://purl.uniprot.org/annotation/VAR_010380|||http://purl.uniprot.org/annotation/VAR_072115|||http://purl.uniprot.org/annotation/VAR_072116|||http://purl.uniprot.org/annotation/VAR_072117|||http://purl.uniprot.org/annotation/VAR_072118|||http://purl.uniprot.org/annotation/VAR_072119|||http://purl.uniprot.org/annotation/VAR_072120|||http://purl.uniprot.org/annotation/VAR_072121|||http://purl.uniprot.org/annotation/VAR_072122|||http://purl.uniprot.org/annotation/VAR_072123|||http://purl.uniprot.org/annotation/VAR_072124|||http://purl.uniprot.org/annotation/VAR_079797|||http://purl.uniprot.org/annotation/VAR_079798|||http://purl.uniprot.org/annotation/VAR_079799|||http://purl.uniprot.org/annotation/VAR_079800|||http://purl.uniprot.org/annotation/VSP_047733|||http://purl.uniprot.org/annotation/VSP_053401
http://togogenome.org/gene/9606:RIPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13546                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolished GlcNAcylation by E.coli NleB1.|||Abolished cleavage by S.flexneri OspD3.|||Abolishes RIP-mediated NF-Kappa-B activation.|||Abolishes cleavage by caspase-8.|||Abolishes kinase activity.|||Basic and acidic residues|||Blocks homodimerization, necroptosis and apoptosis.|||Cleavage; by CASP8|||Death|||Decreases RIPK1 kinase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In AIEFL; prevents cleavage by CASP8; changed inflammatory response.|||In AIEFL; prevents cleavage by CASP8; increased kinase activity; increased inflammatory response.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with SQSTM1|||No effect on RIPK1 autophosphorylation.|||Phophomimetic mutant. Significant loss of kinase activity.|||Phosphoserine|||Phosphoserine; by IKKA and IKKB|||Phosphoserine; by MAP3K7|||Phosphoserine; by RIPK3 and autocatalysis|||Phosphoserine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||RIP homotypic interaction motif (RHIM)|||Receptor-interacting serine/threonine-protein kinase 1|||Strongly reduced homodimerization and interaction with RIPK3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086606|||http://purl.uniprot.org/annotation/VAR_021109|||http://purl.uniprot.org/annotation/VAR_041039|||http://purl.uniprot.org/annotation/VAR_041040|||http://purl.uniprot.org/annotation/VAR_041041|||http://purl.uniprot.org/annotation/VAR_041042|||http://purl.uniprot.org/annotation/VAR_041043|||http://purl.uniprot.org/annotation/VAR_041044|||http://purl.uniprot.org/annotation/VAR_058285|||http://purl.uniprot.org/annotation/VAR_083518|||http://purl.uniprot.org/annotation/VAR_083519|||http://purl.uniprot.org/annotation/VAR_083520|||http://purl.uniprot.org/annotation/VAR_084135|||http://purl.uniprot.org/annotation/VSP_037690
http://togogenome.org/gene/9606:FAM98A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT23|||http://purl.uniprot.org/uniprot/I6L9E8|||http://purl.uniprot.org/uniprot/Q8NCA5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Protein FAM98A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187184
http://togogenome.org/gene/9606:GPR107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E994|||http://purl.uniprot.org/uniprot/Q5VW38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||Loss of furin cleavage.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein GPR107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021340|||http://purl.uniprot.org/annotation/PRO_5014571897|||http://purl.uniprot.org/annotation/VAR_030863|||http://purl.uniprot.org/annotation/VSP_014434|||http://purl.uniprot.org/annotation/VSP_014435|||http://purl.uniprot.org/annotation/VSP_014436
http://togogenome.org/gene/9606:RNASE6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IB39|||http://purl.uniprot.org/uniprot/Q93091                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Critical for catalytic activity|||Facilitates cleavage of polynucleotide substrates|||Important for bactericidal activity, bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS)|||Moderately impairs bactericidal activity, bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS).|||N-linked (GlcNAc...) asparagine|||No significant effect on activity towards dinucleotides UpA and CpA. Reduced activity towards polymeric substrates poly(U) and poly(U):poly(A). Significantly reduced activity towards poly(U) and poly(U):poly(A); when associated with A-38.|||Proton acceptor|||Proton donor|||Ribonuclease A-domain|||Ribonuclease K6|||Significantly reduced activity towards dinucleotides UpA and CpA. Slightly reduced activity towards polymeric substrates poly(U) and poly(U):poly(A). No effect on bactericidal activity. Significantly reduced activity towards poly(U) and poly(U):poly(A); when associated with R-59.|||Strongly impairs bactericidal activity, bacterial agglutination activity and binding to bacterial lipopolysaccharide (LPS).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030892|||http://purl.uniprot.org/annotation/PRO_5014205944|||http://purl.uniprot.org/annotation/VAR_012048
http://togogenome.org/gene/9606:OR10V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGI7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10V1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150718|||http://purl.uniprot.org/annotation/VAR_034296|||http://purl.uniprot.org/annotation/VAR_048065
http://togogenome.org/gene/9606:NEUROG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2A3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Neurogenin-2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127400
http://togogenome.org/gene/9606:ZNF280D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6N043                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||Zinc finger protein 280D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227977|||http://purl.uniprot.org/annotation/VAR_054314|||http://purl.uniprot.org/annotation/VAR_054315|||http://purl.uniprot.org/annotation/VAR_054316|||http://purl.uniprot.org/annotation/VAR_054317|||http://purl.uniprot.org/annotation/VSP_017622|||http://purl.uniprot.org/annotation/VSP_017623|||http://purl.uniprot.org/annotation/VSP_017624|||http://purl.uniprot.org/annotation/VSP_017625|||http://purl.uniprot.org/annotation/VSP_017626|||http://purl.uniprot.org/annotation/VSP_017627|||http://purl.uniprot.org/annotation/VSP_017628|||http://purl.uniprot.org/annotation/VSP_054317|||http://purl.uniprot.org/annotation/VSP_054318
http://togogenome.org/gene/9606:PCLAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15004                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  D-box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||Inhibits chain initiation by APC/C.|||Initiation motif|||KEN box|||Loss of binding to PCNA.|||Loss of monoubiquitination; when associated with R-15.|||Loss of monoubiquitination; when associated with R-24.|||N6-acetyllysine; alternate|||No effect on chain initiation by APC/C.|||PCNA-associated factor|||PIP-box|||Phosphoserine|||Polar residues|||Stabilizes the protein in G1 by preventing association with the APC/C complex and degradation by the proteasome.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096684|||http://purl.uniprot.org/annotation/VAR_051262|||http://purl.uniprot.org/annotation/VSP_045659
http://togogenome.org/gene/9606:CTHRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CG8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Collagen triple helix repeat-containing protein 1|||Collagen-like|||Disordered|||Found in patients with Barrett esophagus.|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021038|||http://purl.uniprot.org/annotation/VAR_066589|||http://purl.uniprot.org/annotation/VSP_013622|||http://purl.uniprot.org/annotation/VSP_013623
http://togogenome.org/gene/9606:UEVLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIA9|||http://purl.uniprot.org/uniprot/Q8IX04                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||UEV|||Ubiquitin-conjugating enzyme E2 variant 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278651|||http://purl.uniprot.org/annotation/VSP_023346|||http://purl.uniprot.org/annotation/VSP_023347|||http://purl.uniprot.org/annotation/VSP_023348|||http://purl.uniprot.org/annotation/VSP_023349|||http://purl.uniprot.org/annotation/VSP_023350|||http://purl.uniprot.org/annotation/VSP_023351|||http://purl.uniprot.org/annotation/VSP_045986|||http://purl.uniprot.org/annotation/VSP_045987|||http://purl.uniprot.org/annotation/VSP_045988
http://togogenome.org/gene/9606:ARHGEF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes its exchange activity on RHOA.|||DH|||Disordered|||Important for binding to Rho GTPases|||In isoform 2.|||In isoform 3.|||PH|||Polar residues|||Reduces exchange activity mediated by GNAQ activation; in truncated construct.|||Rho guanine nucleotide exchange factor 25|||Sufficient to bind activated GNAQ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322132|||http://purl.uniprot.org/annotation/VAR_039402|||http://purl.uniprot.org/annotation/VAR_039403|||http://purl.uniprot.org/annotation/VAR_039404|||http://purl.uniprot.org/annotation/VSP_031875|||http://purl.uniprot.org/annotation/VSP_047254
http://togogenome.org/gene/9606:SHD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||SH2|||SH2 domain-containing adapter protein D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246773|||http://purl.uniprot.org/annotation/VAR_027043|||http://purl.uniprot.org/annotation/VAR_027044
http://togogenome.org/gene/9606:PFKFB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I1Z9G4|||http://purl.uniprot.org/uniprot/P16118                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1|||Fructose-2,6-bisphosphatase|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKA|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179960|||http://purl.uniprot.org/annotation/VSP_054795
http://togogenome.org/gene/9606:ZNF557                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N988                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 557                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047647|||http://purl.uniprot.org/annotation/VSP_014515
http://togogenome.org/gene/9606:DVL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92997                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT1; alternate|||Basic and acidic residues|||Basic residues|||DEP|||DIX|||Dimethylated arginine; alternate|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Localizes to plasma membranes.|||No effect on subcellular location.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Segment polarity protein dishevelled homolog DVL-3|||Symmetric dimethylarginine; by PRMT7|||Symmetric dimethylarginine; by PRMT7; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145749|||http://purl.uniprot.org/annotation/VAR_025519|||http://purl.uniprot.org/annotation/VAR_036116|||http://purl.uniprot.org/annotation/VSP_053371
http://togogenome.org/gene/9606:C1QBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07021                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  C1q binding|||Complement component 1 Q subcomponent-binding protein, mitochondrial|||Disordered|||Impairs HIVRNA splicing in mouse cells.|||In COXPD33.|||In COXPD33; unknown pathological significance.|||Interaction with MAVS|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018590|||http://purl.uniprot.org/annotation/VAR_080391|||http://purl.uniprot.org/annotation/VAR_080392|||http://purl.uniprot.org/annotation/VAR_080393|||http://purl.uniprot.org/annotation/VAR_080394|||http://purl.uniprot.org/annotation/VAR_080395|||http://purl.uniprot.org/annotation/VAR_080396
http://togogenome.org/gene/9606:LRRC4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4JIV9|||http://purl.uniprot.org/uniprot/Q4JIW0|||http://purl.uniprot.org/uniprot/Q9HCJ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Ig-like|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 4C|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015108|||http://purl.uniprot.org/annotation/PRO_5004239102|||http://purl.uniprot.org/annotation/PRO_5004239235
http://togogenome.org/gene/9606:SHROOM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULL8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ASD2|||Acidic residues|||Basic and acidic residues|||Disordered|||Found in a family with Stocco dos Santos-type X-linked syndromic intellectual developmental disorder; unknown pathological significance.|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||In isoform 2.|||PDZ|||Phosphoserine|||Polar residues|||Protein Shroom4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287077|||http://purl.uniprot.org/annotation/VAR_032257|||http://purl.uniprot.org/annotation/VAR_032258|||http://purl.uniprot.org/annotation/VAR_057770|||http://purl.uniprot.org/annotation/VAR_057771|||http://purl.uniprot.org/annotation/VAR_074639|||http://purl.uniprot.org/annotation/VAR_075207|||http://purl.uniprot.org/annotation/VAR_079036|||http://purl.uniprot.org/annotation/VSP_025290
http://togogenome.org/gene/9606:SATB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPQ9|||http://purl.uniprot.org/uniprot/Q59FT3|||http://purl.uniprot.org/uniprot/Q9UPW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CUT|||CUT 1|||CUT 2|||CUTL|||DNA-binding protein SATB2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced sumoylation, impaired nuclear localization, but enhanced transcription factor activity.|||ULD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202400|||http://purl.uniprot.org/annotation/VAR_059320|||http://purl.uniprot.org/annotation/VSP_054416
http://togogenome.org/gene/9606:TMEM217                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C081|||http://purl.uniprot.org/uniprot/Q8N7C4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 217                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089528|||http://purl.uniprot.org/annotation/VSP_014386|||http://purl.uniprot.org/annotation/VSP_014387
http://togogenome.org/gene/9606:MTMR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3D5|||http://purl.uniprot.org/uniprot/F8WA39|||http://purl.uniprot.org/uniprot/Q13613|||http://purl.uniprot.org/uniprot/Q8NEC6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity with phosphatidylinositol 3-phosphate. Reduces activity with phosphatidylinositol (3,5)-bisphosphate.|||Abolishes enzyme activity.|||Disordered|||GRAM|||In isoform 1A.|||Myotubularin phosphatase|||Myotubularin-related protein 1|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Required for dimerization|||Tyrosine specific protein phosphatases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094932|||http://purl.uniprot.org/annotation/VSP_005169|||http://purl.uniprot.org/annotation/VSP_005170
http://togogenome.org/gene/9606:BRIX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Brix|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Ribosome biogenesis protein BRX1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120230
http://togogenome.org/gene/9606:RTBDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ESG0|||http://purl.uniprot.org/uniprot/Q8N210|||http://purl.uniprot.org/uniprot/Q9BSG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Folate receptor-like|||In isoform 2.|||In isoform 3.|||Polar residues|||Retbindin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043174|||http://purl.uniprot.org/annotation/VAR_049053|||http://purl.uniprot.org/annotation/VSP_037666|||http://purl.uniprot.org/annotation/VSP_046903
http://togogenome.org/gene/9606:C2CD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLK1|||http://purl.uniprot.org/uniprot/Q86YS7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 domain-containing protein 5|||Disordered|||Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion.|||Phosphoserine|||Phosphoserine; by PKB/AKT2|||Phosphothreonine|||Polar residues|||Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-78.|||Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-84.|||Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-78 and A-84.|||Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-76; A-78 and A-84.|||Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-26; A-76; A-78 and A-84.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247450|||http://purl.uniprot.org/annotation/VSP_028255|||http://purl.uniprot.org/annotation/VSP_028256|||http://purl.uniprot.org/annotation/VSP_055638|||http://purl.uniprot.org/annotation/VSP_055639|||http://purl.uniprot.org/annotation/VSP_055640
http://togogenome.org/gene/9606:STK32A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9H7|||http://purl.uniprot.org/uniprot/Q8WU08                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Localizes to cytoplasm.|||N-myristoyl glycine|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 32A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232411|||http://purl.uniprot.org/annotation/VAR_041163|||http://purl.uniprot.org/annotation/VAR_041164|||http://purl.uniprot.org/annotation/VAR_041165|||http://purl.uniprot.org/annotation/VSP_051992|||http://purl.uniprot.org/annotation/VSP_051993|||http://purl.uniprot.org/annotation/VSP_051994|||http://purl.uniprot.org/annotation/VSP_051995
http://togogenome.org/gene/9606:TNFSF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X228|||http://purl.uniprot.org/uniprot/P32971|||http://purl.uniprot.org/uniprot/Q52M88                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185499
http://togogenome.org/gene/9606:ARID4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LE39                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 4B|||Acidic residues|||Antigenic epitope|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282863|||http://purl.uniprot.org/annotation/VSP_024230|||http://purl.uniprot.org/annotation/VSP_024231|||http://purl.uniprot.org/annotation/VSP_024232|||http://purl.uniprot.org/annotation/VSP_024233|||http://purl.uniprot.org/annotation/VSP_024234|||http://purl.uniprot.org/annotation/VSP_024235
http://togogenome.org/gene/9606:ZNF528                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIS6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 528                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280418|||http://purl.uniprot.org/annotation/VAR_052858|||http://purl.uniprot.org/annotation/VSP_023662
http://togogenome.org/gene/9606:GPR157                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5UAW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 157|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070339
http://togogenome.org/gene/9606:UGT2B11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75310                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 2B11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036035
http://togogenome.org/gene/9606:SLC28A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased uridine transport. Normal localization to the cell membrane.|||Disordered|||Extracellular|||Helical; Name=HP1|||Helical; Name=HP2|||Helical; Name=TM1|||Helical; Name=TM10|||Helical; Name=TM11|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||Helical; Name=TM6|||Helical; Name=TM7|||Helical; Name=TM8|||Helical; Name=TM9|||In isoform 2.|||Lower concentrative capacity and altered sodium binding capacity.|||Polar residues|||Reduced transport of inosine and thymidine.|||Solute carrier family 28 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324146|||http://purl.uniprot.org/annotation/VAR_039665|||http://purl.uniprot.org/annotation/VAR_039666|||http://purl.uniprot.org/annotation/VAR_039667|||http://purl.uniprot.org/annotation/VAR_039668|||http://purl.uniprot.org/annotation/VAR_039669|||http://purl.uniprot.org/annotation/VAR_039670|||http://purl.uniprot.org/annotation/VAR_039671|||http://purl.uniprot.org/annotation/VAR_039672|||http://purl.uniprot.org/annotation/VAR_039673|||http://purl.uniprot.org/annotation/VAR_039674|||http://purl.uniprot.org/annotation/VAR_039675|||http://purl.uniprot.org/annotation/VAR_039676|||http://purl.uniprot.org/annotation/VAR_039677|||http://purl.uniprot.org/annotation/VAR_039678|||http://purl.uniprot.org/annotation/VAR_070606|||http://purl.uniprot.org/annotation/VSP_053848
http://togogenome.org/gene/9606:FUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19526                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Found in individuals with Bombay phenotype.|||Found in individuals with para-Bombay phenotype.|||Found in individuals with para-Bombay phenotype; allele H3.|||Found in individuals with para-Bombay phenotype; allele H4.|||Found in individuals with para-Bombay phenotype; allele H5.|||Galactoside alpha-(1,2)-fucosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149095|||http://purl.uniprot.org/annotation/VAR_003417|||http://purl.uniprot.org/annotation/VAR_003418|||http://purl.uniprot.org/annotation/VAR_003419|||http://purl.uniprot.org/annotation/VAR_003420|||http://purl.uniprot.org/annotation/VAR_003421|||http://purl.uniprot.org/annotation/VAR_009708|||http://purl.uniprot.org/annotation/VAR_009709|||http://purl.uniprot.org/annotation/VAR_020536|||http://purl.uniprot.org/annotation/VAR_020537|||http://purl.uniprot.org/annotation/VAR_020538|||http://purl.uniprot.org/annotation/VAR_020539|||http://purl.uniprot.org/annotation/VAR_022268
http://togogenome.org/gene/9606:CEP126                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2H0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 126 kDa|||Disordered|||May be associated with susceptibility to monomelic amyotrophy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248831|||http://purl.uniprot.org/annotation/VAR_027363|||http://purl.uniprot.org/annotation/VAR_027364|||http://purl.uniprot.org/annotation/VAR_027365|||http://purl.uniprot.org/annotation/VAR_027366|||http://purl.uniprot.org/annotation/VAR_027367|||http://purl.uniprot.org/annotation/VAR_027368|||http://purl.uniprot.org/annotation/VAR_027369|||http://purl.uniprot.org/annotation/VAR_027370|||http://purl.uniprot.org/annotation/VAR_068173
http://togogenome.org/gene/9606:ABCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X609|||http://purl.uniprot.org/uniprot/Q2L6I2|||http://purl.uniprot.org/uniprot/Q8NE71                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 1|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not inhibit ribosome binding.|||Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-342. Shows a reduced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664.|||Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-664. Shows an enhanced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664.|||Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477.|||Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-109. Does not inhibits interaction with EIF2; when associated with S-109. Does not inhibit association with ribosomes; when associated with S-109. Reduces EIF2 interaction with ribosomes; when associated with S-109. Does not inhibit protein synthesis; when associated with A-109.|||Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-140. Does not inhibit interaction with EIF2; when associated with S-140. Does not inhibit association with ribosomes; when associated with S-140. Reduces EIF2 interaction with ribosomes; when associated with S-140. Does not inhibit protein synthesis; when associated with A-140.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093318|||http://purl.uniprot.org/annotation/VAR_048136|||http://purl.uniprot.org/annotation/VSP_012078
http://togogenome.org/gene/9606:HIKESHI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FT3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases nuclear import activity of HSPA8. Does not affect the dimer formation. Decreases binding to HSPA8.|||Decreases nuclear import activity of HSPA8. Does not affect the dimer formation. Impairs binding to HSPA8.|||Decreases nuclear import activity of HSPA8. Does not affect the dimer formation. Markedly decreases binding to HSPA8.|||Flexible linker region involved in nuclear import of HSP70 proteins|||Impairs the nuclear migrating activity.|||In HLD13.|||Increases the nuclear migrating activity.|||Protein Hikeshi|||Reduces the nuclear migrating activity.|||Required for F-X-F-G repeats-nucleoporins recognition and nuclear import                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245262|||http://purl.uniprot.org/annotation/VAR_026968|||http://purl.uniprot.org/annotation/VAR_076411
http://togogenome.org/gene/9606:CNKSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y622|||http://purl.uniprot.org/uniprot/A0A2R8Y700|||http://purl.uniprot.org/uniprot/A0A2R8Y7A1|||http://purl.uniprot.org/uniprot/A0A2U3TZH5|||http://purl.uniprot.org/uniprot/B3KPN2|||http://purl.uniprot.org/uniprot/Q8WXI2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||CRIC|||Connector enhancer of kinase suppressor of ras 2|||DUF1170|||Disordered|||In MRXSHG.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||PDZ|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089970|||http://purl.uniprot.org/annotation/VAR_035681|||http://purl.uniprot.org/annotation/VAR_080600|||http://purl.uniprot.org/annotation/VSP_010887|||http://purl.uniprot.org/annotation/VSP_043168|||http://purl.uniprot.org/annotation/VSP_043169
http://togogenome.org/gene/9606:TRABD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Metalloprotease TIKI2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346436
http://togogenome.org/gene/9606:EFR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Induces localization to the cytosol.|||Phosphoserine|||Protein EFR3 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312295|||http://purl.uniprot.org/annotation/VSP_029806|||http://purl.uniprot.org/annotation/VSP_029807
http://togogenome.org/gene/9606:SLC35D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9Y0|||http://purl.uniprot.org/uniprot/Q5M8T2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Solute carrier family 35 member D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307727
http://togogenome.org/gene/9606:PLK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q496M5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Inactive serine/threonine-protein kinase PLK5|||POLO box|||Protein kinase; truncated                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280397|||http://purl.uniprot.org/annotation/VSP_023654
http://togogenome.org/gene/9606:TCF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Ribosome quality control complex subunit TCF25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087265
http://togogenome.org/gene/9606:RSPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYR4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In CILD24.|||In isoform 2.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||Radial spoke head 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065662|||http://purl.uniprot.org/annotation/VAR_070564|||http://purl.uniprot.org/annotation/VSP_055743
http://togogenome.org/gene/9606:EPB41L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DH22|||http://purl.uniprot.org/uniprot/B7Z653|||http://purl.uniprot.org/uniprot/Q9H4G0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 4.1-like protein 1|||Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||In MRD11; results in a 50% reduction of interaction of 4.1N protein to GRIA1 compared to wild-type.|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Spectrin--actin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219395|||http://purl.uniprot.org/annotation/VAR_066600|||http://purl.uniprot.org/annotation/VSP_023958|||http://purl.uniprot.org/annotation/VSP_023959|||http://purl.uniprot.org/annotation/VSP_023960|||http://purl.uniprot.org/annotation/VSP_023961|||http://purl.uniprot.org/annotation/VSP_023962|||http://purl.uniprot.org/annotation/VSP_023963
http://togogenome.org/gene/9606:ZNF704                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||CR1|||CR2|||Disordered|||Phosphoserine|||Polar residues|||Sufficient for binding to RE2 sequence motifs|||Zinc finger protein 704                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288824|||http://purl.uniprot.org/annotation/VAR_032506
http://togogenome.org/gene/9606:CBLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW01                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Cerebellin-3|||Interchain|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with CBLN3, and homotrimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003554
http://togogenome.org/gene/9606:STMND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BQB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Polar residues|||Removed|||SLD|||Stathmin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421693
http://togogenome.org/gene/9606:PABPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DU9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Polyadenylate-binding protein 5|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081705|||http://purl.uniprot.org/annotation/VAR_054049|||http://purl.uniprot.org/annotation/VSP_047456
http://togogenome.org/gene/9606:PWWP3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNX4|||http://purl.uniprot.org/uniprot/Q2TAK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PWWP|||PWWP domain-containing DNA repair factor 3A|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295046|||http://purl.uniprot.org/annotation/VAR_033195|||http://purl.uniprot.org/annotation/VAR_033196|||http://purl.uniprot.org/annotation/VSP_026684|||http://purl.uniprot.org/annotation/VSP_026685|||http://purl.uniprot.org/annotation/VSP_053986
http://togogenome.org/gene/9606:DCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07585|||http://purl.uniprot.org/uniprot/Q6FH10                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Decorin|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032709|||http://purl.uniprot.org/annotation/PRO_0000032710|||http://purl.uniprot.org/annotation/PRO_5014205939|||http://purl.uniprot.org/annotation/VAR_011975|||http://purl.uniprot.org/annotation/VAR_014351|||http://purl.uniprot.org/annotation/VSP_006172|||http://purl.uniprot.org/annotation/VSP_006173|||http://purl.uniprot.org/annotation/VSP_006174|||http://purl.uniprot.org/annotation/VSP_006175|||http://purl.uniprot.org/annotation/VSP_006176
http://togogenome.org/gene/9606:OR1L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFP2|||http://purl.uniprot.org/uniprot/Q8NGR2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1L6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150445|||http://purl.uniprot.org/annotation/VAR_055056|||http://purl.uniprot.org/annotation/VAR_055057|||http://purl.uniprot.org/annotation/VAR_055058|||http://purl.uniprot.org/annotation/VAR_055059
http://togogenome.org/gene/9606:EXOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV70                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exocyst complex component 1|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118913|||http://purl.uniprot.org/annotation/VSP_001481
http://togogenome.org/gene/9606:ZSCAN31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTA4|||http://purl.uniprot.org/uniprot/Q96LW9|||http://purl.uniprot.org/uniprot/Q96QL1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||SCAN box|||Zinc finger and SCAN domain-containing protein 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047532|||http://purl.uniprot.org/annotation/VAR_019981|||http://purl.uniprot.org/annotation/VAR_024209|||http://purl.uniprot.org/annotation/VAR_052809|||http://purl.uniprot.org/annotation/VAR_052810|||http://purl.uniprot.org/annotation/VAR_059911|||http://purl.uniprot.org/annotation/VSP_047105
http://togogenome.org/gene/9606:LY75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60449|||http://purl.uniprot.org/uniprot/Q59H44                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin 1|||C-type lectin 10|||C-type lectin 2|||C-type lectin 3|||C-type lectin 4|||C-type lectin 5|||C-type lectin 6|||C-type lectin 7|||C-type lectin 8|||C-type lectin 9|||Cytoplasmic|||Extracellular|||Fibronectin type-II|||Helical|||In isoform 2.|||In isoform 3.|||Lymphocyte antigen 75|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017552|||http://purl.uniprot.org/annotation/VAR_024522|||http://purl.uniprot.org/annotation/VAR_027824|||http://purl.uniprot.org/annotation/VAR_027825|||http://purl.uniprot.org/annotation/VAR_027826|||http://purl.uniprot.org/annotation/VAR_027827|||http://purl.uniprot.org/annotation/VAR_027828|||http://purl.uniprot.org/annotation/VAR_027829|||http://purl.uniprot.org/annotation/VAR_027830|||http://purl.uniprot.org/annotation/VAR_027831|||http://purl.uniprot.org/annotation/VAR_056156|||http://purl.uniprot.org/annotation/VAR_056157|||http://purl.uniprot.org/annotation/VAR_056158|||http://purl.uniprot.org/annotation/VSP_020908|||http://purl.uniprot.org/annotation/VSP_020909
http://togogenome.org/gene/9606:FUT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y231                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9|||Almost complete loss of alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-62. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-101.|||Cytoplasmic|||Does not affect glycosylation. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity. Affects subcellular location.|||Does not affect glycosylation; when associated with A-3. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with A-3. Does not affect subcellular location; when associated with A-3.|||Does not affect glycosylation; when associated with A-5. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with A-5. Does not affect subcellular location; when associated with A-5.|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Significantly decrease alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-62. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-153. Loss of catalytic efficiency.|||Weakly decreases alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-101. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-153. Loss of catalytic efficiency.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221118|||http://purl.uniprot.org/annotation/VAR_024465|||http://purl.uniprot.org/annotation/VAR_030575
http://togogenome.org/gene/9606:CLC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05315                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-10|||N-acetylserine|||Not glycosylated|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076960|||http://purl.uniprot.org/annotation/VAR_014765
http://togogenome.org/gene/9606:KCTD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L273                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD9|||Impaired interaction with CUL3.|||KHA|||Pentapeptide repeat 1|||Pentapeptide repeat 2|||Pentapeptide repeat 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191293
http://togogenome.org/gene/9606:PHACTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PFA8|||http://purl.uniprot.org/uniprot/A0A6Q8PG87|||http://purl.uniprot.org/uniprot/A0A6Q8PGC2|||http://purl.uniprot.org/uniprot/A0A8I5QJF9|||http://purl.uniprot.org/uniprot/B4DHU0|||http://purl.uniprot.org/uniprot/Q9C0D0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In DEE70; loss of interaction with PP1 complex.|||In DEE70; severely impaired interaction with actin.|||In isoform 2.|||Nuclear localization signal|||Phosphatase and actin regulator 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||RPEL|||RPEL 1|||RPEL 2|||RPEL 3|||RPEL 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126634|||http://purl.uniprot.org/annotation/VAR_053645|||http://purl.uniprot.org/annotation/VAR_069379|||http://purl.uniprot.org/annotation/VAR_081810|||http://purl.uniprot.org/annotation/VAR_081811|||http://purl.uniprot.org/annotation/VSP_018529|||http://purl.uniprot.org/annotation/VSP_018530
http://togogenome.org/gene/9606:MAPRE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15555                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  APC-binding|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||In CSCSC2; enhances binding to microtubules.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Microtubule-associated protein RP/EB family member 2|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213424|||http://purl.uniprot.org/annotation/VAR_050018|||http://purl.uniprot.org/annotation/VAR_076540|||http://purl.uniprot.org/annotation/VAR_076541|||http://purl.uniprot.org/annotation/VAR_076542|||http://purl.uniprot.org/annotation/VSP_012944|||http://purl.uniprot.org/annotation/VSP_012945|||http://purl.uniprot.org/annotation/VSP_045710|||http://purl.uniprot.org/annotation/VSP_046041|||http://purl.uniprot.org/annotation/VSP_055671
http://togogenome.org/gene/9606:TBC1D22B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NU19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of ACBD3-binding.|||Disordered|||N-acetylalanine|||No effect on ACBD3-binding.|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||Removed|||TBC1 domain family member 22B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208054
http://togogenome.org/gene/9606:MICU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z6V5|||http://purl.uniprot.org/uniprot/Q8IYU8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes mitochondrial Ca(2+) uptake; when associated with A-185 and A-375.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-185 and A-386.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-375 and A-386.|||Calcium uptake protein 2, mitochondrial|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interchain (with C-463 in MICU1)|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251217|||http://purl.uniprot.org/annotation/VAR_027662
http://togogenome.org/gene/9606:CLEC18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8T8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 18 member A|||EGF-like|||Has a mild effect on polysaccharides binding.|||In allele CLEC18A-1.|||In allele CLEC18A-1; abolishes binding to polysaccharides.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324316|||http://purl.uniprot.org/annotation/VAR_059449|||http://purl.uniprot.org/annotation/VAR_074610|||http://purl.uniprot.org/annotation/VAR_074611|||http://purl.uniprot.org/annotation/VSP_032204|||http://purl.uniprot.org/annotation/VSP_032205
http://togogenome.org/gene/9606:TPD52L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH0|||http://purl.uniprot.org/uniprot/Q96J77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Tumor protein D55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295856|||http://purl.uniprot.org/annotation/VAR_033372|||http://purl.uniprot.org/annotation/VSP_027113|||http://purl.uniprot.org/annotation/VSP_027114
http://togogenome.org/gene/9606:AGAP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 9|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2.|||PH|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284677|||http://purl.uniprot.org/annotation/VSP_044549|||http://purl.uniprot.org/annotation/VSP_044550|||http://purl.uniprot.org/annotation/VSP_044551
http://togogenome.org/gene/9606:SEC24A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E205|||http://purl.uniprot.org/uniprot/O95486                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased ability to interact with and package the SNARESEC22B cargo into COPII vesicles. Has no effect on other cargos packaging.|||Disordered|||Gelsolin-like|||In isoform 2.|||Polar residues|||Pro residues|||Protein transport protein Sec24A|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type|||Zinc finger-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205153|||http://purl.uniprot.org/annotation/VAR_037253|||http://purl.uniprot.org/annotation/VAR_037254|||http://purl.uniprot.org/annotation/VAR_037255|||http://purl.uniprot.org/annotation/VSP_029571|||http://purl.uniprot.org/annotation/VSP_029572
http://togogenome.org/gene/9606:RPL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27635|||http://purl.uniprot.org/uniprot/X5D2T3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Citrulline|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In AUTSX5; associated with disease susceptibility; no effect on function; rescues embryonic brain development when expressed in a zebrafish heterologous system.|||In MRXS35; increased the formation of actively translating ribosomes when expressed in a yeast heterologous system.|||In MRXS35; loss of function; fails to rescue embryonic brain development when expressed in a zebrafish heterologous system.|||In MRXS35; unknown pathological significance.|||Large ribosomal subunit protein uL16|||Removed|||Rescues embryonic brain development when expressed in a zebrafish heterologous system.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147105|||http://purl.uniprot.org/annotation/VAR_006922|||http://purl.uniprot.org/annotation/VAR_027795|||http://purl.uniprot.org/annotation/VAR_027796|||http://purl.uniprot.org/annotation/VAR_079288|||http://purl.uniprot.org/annotation/VAR_079289|||http://purl.uniprot.org/annotation/VAR_079290
http://togogenome.org/gene/9606:PCDHB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H00|||http://purl.uniprot.org/uniprot/Q9Y5E1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003930|||http://purl.uniprot.org/annotation/VAR_059186|||http://purl.uniprot.org/annotation/VAR_059187|||http://purl.uniprot.org/annotation/VAR_061064|||http://purl.uniprot.org/annotation/VAR_061065|||http://purl.uniprot.org/annotation/VAR_061066|||http://purl.uniprot.org/annotation/VAR_061067
http://togogenome.org/gene/9606:SELENOF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60613                                                                                  ^@                                                                                  Chain|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non standard residue|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mass|||Mutagenesis Site|||Non standard residue|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Does not affect protein folding and binding to UGGT1 or UGGT2.|||In isoform 2.|||Selenocysteine|||Selenoprotein F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022307|||http://purl.uniprot.org/annotation/VSP_014695|||http://purl.uniprot.org/annotation/VSP_014696
http://togogenome.org/gene/9606:TRIR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ELS0|||http://purl.uniprot.org/uniprot/K7EN60|||http://purl.uniprot.org/uniprot/Q9BQ61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N6-acetyllysine|||Polar residues|||Telomerase RNA component interacting RNase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280762
http://togogenome.org/gene/9606:C8orf76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K31                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Uncharacterized protein C8orf76                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225635
http://togogenome.org/gene/9606:HNRNPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14103                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein D0|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-acetylserine|||N6-acetyllysine|||N6-methyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081849|||http://purl.uniprot.org/annotation/VSP_005834|||http://purl.uniprot.org/annotation/VSP_005835
http://togogenome.org/gene/9606:DCTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75935                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Dynactin subunit 3|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225603|||http://purl.uniprot.org/annotation/VSP_051961|||http://purl.uniprot.org/annotation/VSP_051964
http://togogenome.org/gene/9606:VPS29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR19|||http://purl.uniprot.org/uniprot/F8VXU5|||http://purl.uniprot.org/uniprot/Q9UBQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcineurin-like phosphoesterase|||Decreases interaction with VPS35.|||Disrupts interaction with TBC1D5.|||Disrupts interaction with VPS35.|||In isoform 2.|||Loss of in vitro protein phosphatase activity.|||N6-acetyllysine|||No effect on in vitro protein phosphatase activity.|||Vacuolar protein sorting-associated protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065894|||http://purl.uniprot.org/annotation/VSP_004073
http://togogenome.org/gene/9606:ATP6V1G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75348                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylalanine|||Removed|||V-type proton ATPase subunit G 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192897
http://togogenome.org/gene/9606:NDUFS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KRK5|||http://purl.uniprot.org/uniprot/P28331                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||4Fe-4S His(Cys)3-ligated-type|||4Fe-4S Mo/W bis-MGD-type|||In MC1DN5; also found in a patient with muscular hypotonia; loss of catalytic activity.|||In MC1DN5; loss of catalytic activity.|||In MC1DN5; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitochondrion|||N6-acetyllysine|||NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019968|||http://purl.uniprot.org/annotation/VAR_018463|||http://purl.uniprot.org/annotation/VAR_019532|||http://purl.uniprot.org/annotation/VAR_019533|||http://purl.uniprot.org/annotation/VAR_025511|||http://purl.uniprot.org/annotation/VAR_069506|||http://purl.uniprot.org/annotation/VAR_084177|||http://purl.uniprot.org/annotation/VSP_042682|||http://purl.uniprot.org/annotation/VSP_043727|||http://purl.uniprot.org/annotation/VSP_043728|||http://purl.uniprot.org/annotation/VSP_043729|||http://purl.uniprot.org/annotation/VSP_045864
http://togogenome.org/gene/9606:NANOS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60321                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC 1|||C2HC 2|||Disordered|||Nanos homolog 2|||Nanos-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207687|||http://purl.uniprot.org/annotation/VAR_065246
http://togogenome.org/gene/9606:HTR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2D3FAF9|||http://purl.uniprot.org/uniprot/Q13639                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 4|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a patient with diffuse leukoencephalopathy with spheroids; unknown pathological significance.|||In isoform 5-HT4(A).|||In isoform 5-HT4(C).|||In isoform 5-HT4(D).|||In isoform 5-HT4(E).|||In isoform 5-HT4(F).|||In isoform 5-HT4(G).|||In isoform 5-HT4(I).|||In isoform 5-HT4c1.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068965|||http://purl.uniprot.org/annotation/VAR_049364|||http://purl.uniprot.org/annotation/VAR_067412|||http://purl.uniprot.org/annotation/VSP_001845|||http://purl.uniprot.org/annotation/VSP_001846|||http://purl.uniprot.org/annotation/VSP_001847|||http://purl.uniprot.org/annotation/VSP_001848|||http://purl.uniprot.org/annotation/VSP_001849|||http://purl.uniprot.org/annotation/VSP_001850|||http://purl.uniprot.org/annotation/VSP_043316|||http://purl.uniprot.org/annotation/VSP_047862
http://togogenome.org/gene/9606:ZNF385B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q569K4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with p53/TP53|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Matrin-type 4|||Polar residues|||Required for induction of apoptosis|||Zinc finger protein 385B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191812|||http://purl.uniprot.org/annotation/VAR_053765|||http://purl.uniprot.org/annotation/VAR_076447|||http://purl.uniprot.org/annotation/VSP_015972|||http://purl.uniprot.org/annotation/VSP_015973|||http://purl.uniprot.org/annotation/VSP_015974|||http://purl.uniprot.org/annotation/VSP_015975|||http://purl.uniprot.org/annotation/VSP_015976|||http://purl.uniprot.org/annotation/VSP_015977|||http://purl.uniprot.org/annotation/VSP_015978|||http://purl.uniprot.org/annotation/VSP_015979|||http://purl.uniprot.org/annotation/VSP_015980
http://togogenome.org/gene/9606:H2AC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R5B6|||http://purl.uniprot.org/uniprot/P20671                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1-D|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055234
http://togogenome.org/gene/9606:GALNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14435                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In HFTC1.|||In isoform 2.|||Loss of ability to glycosylate FGF23.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 3|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059106|||http://purl.uniprot.org/annotation/VAR_080832|||http://purl.uniprot.org/annotation/VSP_011202|||http://purl.uniprot.org/annotation/VSP_011203
http://togogenome.org/gene/9606:SMIM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DI80                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000412225
http://togogenome.org/gene/9606:KDELR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24390                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased binding to the sequence motif K-D-E-L.|||ER lumen protein-retaining receptor 1|||Helical|||Important for recycling of cargo proteins with the sequence motif K-D-E-L from the Golgi to the endoplasmic reticulum|||In isoform 2.|||Inhibits coatomer/ARF-GAP recruitment, receptor redistribution, and intracellular retention of KDEL ligands.|||Interaction with the K-D-E-L motif on target proteins|||Loss of recycling together with cargo proteins containing the sequence motif K-D-E-L from the Golgi to the endoplasmic reticulum.|||Lumenal|||Phosphoserine; by PKA|||Redistribution to the ER is not affected upon PKA inactivation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194153|||http://purl.uniprot.org/annotation/VSP_055484
http://togogenome.org/gene/9606:PPM1N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N819                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PPM-type phosphatase|||Probable protein phosphatase 1N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349231|||http://purl.uniprot.org/annotation/VSP_035233|||http://purl.uniprot.org/annotation/VSP_035234|||http://purl.uniprot.org/annotation/VSP_035235
http://togogenome.org/gene/9606:UBC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG48                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosylthreonine|||ADP-ribosylglycine|||Abolishes CteC-catalyzed ADP-ribosylation.|||Abolishes HLTF-mediated polyubiquitination of PCNA.|||Essential for function|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interacts with activating enzyme|||Loss of ADP-ribosylation.|||Loss of DTX3L-mediated polyubiquitination of histone H3 and H4.|||No effect on ADP-ribosylation, when associated with K-72.|||No effect on ADP-ribosylation, when associated with K-74.|||No effect on ADP-ribosylation.|||No effect on HLTF-mediated polyubiquitination of PCNA.|||Phosphomimetic mutant that binds and activates PRKN.|||Phosphoserine; by PINK1|||Prevents phosphorylation in case of mitophagy. Decreased localization of PRKN to mitochondria.|||Ubiquitin|||Ubiquitin-like 1|||Ubiquitin-like 2|||Ubiquitin-like 3|||Ubiquitin-like 4|||Ubiquitin-like 5|||Ubiquitin-like 6|||Ubiquitin-like 7|||Ubiquitin-like 8|||Ubiquitin-like 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000396178|||http://purl.uniprot.org/annotation/PRO_0000396179|||http://purl.uniprot.org/annotation/PRO_0000396180|||http://purl.uniprot.org/annotation/PRO_0000396181|||http://purl.uniprot.org/annotation/PRO_0000396182|||http://purl.uniprot.org/annotation/PRO_0000396183|||http://purl.uniprot.org/annotation/PRO_0000396184|||http://purl.uniprot.org/annotation/PRO_0000396185|||http://purl.uniprot.org/annotation/PRO_0000396186|||http://purl.uniprot.org/annotation/PRO_0000396187
http://togogenome.org/gene/9606:CXorf51A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTR3|||http://purl.uniprot.org/uniprot/P0DPH9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Uncharacterized protein CXorf51A|||Uncharacterized protein CXorf51B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444693|||http://purl.uniprot.org/annotation/PRO_0000444694
http://togogenome.org/gene/9606:ABTB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6QL63|||http://purl.uniprot.org/uniprot/B3KVD0|||http://purl.uniprot.org/uniprot/B3KXB0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat and BTB/POZ domain-containing protein 3|||BTB|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328827|||http://purl.uniprot.org/annotation/VAR_042534|||http://purl.uniprot.org/annotation/VAR_042535|||http://purl.uniprot.org/annotation/VAR_055560|||http://purl.uniprot.org/annotation/VSP_032801|||http://purl.uniprot.org/annotation/VSP_032802|||http://purl.uniprot.org/annotation/VSP_032803|||http://purl.uniprot.org/annotation/VSP_045802|||http://purl.uniprot.org/annotation/VSP_045803
http://togogenome.org/gene/9606:COTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTY2|||http://purl.uniprot.org/uniprot/Q14019                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H|||Abolishes 5LO-binding activity.|||Abolishes actin-binding activity.|||Coactosin-like protein|||Flexible and important for F-actin binding|||N-acetylalanine|||N6-acetyllysine|||No effect on 5LO-binding activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214954
http://togogenome.org/gene/9606:GLB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6Q5|||http://purl.uniprot.org/uniprot/P16278                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-galactosidase|||Beta-galactosidase jelly roll|||Disordered|||Glycoside hydrolase 35 catalytic|||In GM1-gangliosidosis; unclassified clinical type.|||In GM1G1 and GM1G2; also in a patient with a slowly progressive GM1-gangliosidosis form; 36.2% of wild-type galactosidase activity.|||In GM1G1 and GM1G2; decrease in galactosidase activity.|||In GM1G1 and GM1G2; loss of galactosidase activity.|||In GM1G1 and GM1G2; loss of galactosidase activity; severe mutation.|||In GM1G1 and GM1G2; no effect on intrinsic catalytic activity; decreased protein stability; 8.4% of wild-type galactosidase activity; activity severely reduced in transfection with variant F-436.|||In GM1G1 and GM1G3.|||In GM1G1.|||In GM1G1; 2.1% of wild-type galactosidase activity.|||In GM1G1; 2.3% of wild-type galactosidase activity.|||In GM1G1; 2.4% of wild-type galactosidase activity.|||In GM1G1; 3.4% of wild-type galactosidase activity.|||In GM1G1; 4.3% of wild-type galactosidase activity.|||In GM1G1; 5.0% of wild-type galactosidase activity.|||In GM1G1; complete lack of protein; loss of galactosidase activity.|||In GM1G1; decrease in galactosidase activity.|||In GM1G1; loss of galactosidase activity.|||In GM1G1; loss of galactosidase activity; severe mutation.|||In GM1G1; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor.|||In GM1G1; mild phenotype; unknown pathological significance; reduction of galactosidase activity.|||In GM1G1; unknown pathological significance.|||In GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation.|||In GM1G1; with cardiac involvement in some patients; loss of galactosidase activity; severe mutation; causes a rapid degradation of the protein precursor.|||In GM1G2 and GM1G1; loss of galactosidase activity.|||In GM1G2 and GM1G3; 6.7% of wild-type galactosidase activity.|||In GM1G2.|||In GM1G2; 3.0% of wild-type galactosidase activity; the mutant protein is localized in the lysosomal-endosomal compartment.|||In GM1G2; 7.4% of wild-type galactosidase activity.|||In GM1G2; decrease in galactosidase activity.|||In GM1G2; unknown pathological significance.|||In GM1G3 and GM1G2.|||In GM1G3 and MPS4B; mild form; 5.7% of wild-type galactosidase activity.|||In GM1G3.|||In GM1G3; decrease in galactosidase activity.|||In GM1G3; mild phenotype.|||In GM1G3; no effect on catalytic activity; decreased protein stability.|||In GM1G3; originally classified as Morquio syndrome.|||In MPS4B and GM1G1; severe decrease in galactosidase activity.|||In MPS4B; 1.1% of wild-type galactosidase activity.|||In MPS4B; 17.4% of wild-type galactosidase activity.|||In MPS4B; 2-5% of wild-type galactosidase activity.|||In MPS4B; 2.0% of wild-type galactosidase activity.|||In MPS4B; 24.0% of wild-type galactosidase activity.|||In MPS4B; also in a patient with a slowly progressive form of GM1-gangliosidosis; loss of galactosidase activity.|||In MPS4B; decrease in galactosidase activity.|||In MPS4B; decreased galactosidase activity.|||In MPS4B; loss of galactosidase activity.|||In MPS4B; mild form; 2.1% of wild-type galactosidase activity.|||In MPS4B; mild form; fibroblasts from MPS4B compound heterozygotes for K-484 and A-500 have 1.9% of wild-type galactosidase activity.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Reduction of galactosidase activity.|||Results in near-normal activity corresponding to 60%-100% of the wild-type depending on the expression system.|||Seems to have a modulating action in the expression of the severity of other mutations.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012185|||http://purl.uniprot.org/annotation/PRO_0000012186|||http://purl.uniprot.org/annotation/PRO_5002863977|||http://purl.uniprot.org/annotation/VAR_003329|||http://purl.uniprot.org/annotation/VAR_003330|||http://purl.uniprot.org/annotation/VAR_003331|||http://purl.uniprot.org/annotation/VAR_003332|||http://purl.uniprot.org/annotation/VAR_003333|||http://purl.uniprot.org/annotation/VAR_003334|||http://purl.uniprot.org/annotation/VAR_003335|||http://purl.uniprot.org/annotation/VAR_003336|||http://purl.uniprot.org/annotation/VAR_003337|||http://purl.uniprot.org/annotation/VAR_008671|||http://purl.uniprot.org/annotation/VAR_008672|||http://purl.uniprot.org/annotation/VAR_008673|||http://purl.uniprot.org/annotation/VAR_008674|||http://purl.uniprot.org/annotation/VAR_008675|||http://purl.uniprot.org/annotation/VAR_008676|||http://purl.uniprot.org/annotation/VAR_008677|||http://purl.uniprot.org/annotation/VAR_008678|||http://purl.uniprot.org/annotation/VAR_008679|||http://purl.uniprot.org/annotation/VAR_008680|||http://purl.uniprot.org/annotation/VAR_008681|||http://purl.uniprot.org/annotation/VAR_008682|||http://purl.uniprot.org/annotation/VAR_008683|||http://purl.uniprot.org/annotation/VAR_008684|||http://purl.uniprot.org/annotation/VAR_008685|||http://purl.uniprot.org/annotation/VAR_008686|||http://purl.uniprot.org/annotation/VAR_013541|||http://purl.uniprot.org/annotation/VAR_013542|||http://purl.uniprot.org/annotation/VAR_013543|||http://purl.uniprot.org/annotation/VAR_013544|||http://purl.uniprot.org/annotation/VAR_013545|||http://purl.uniprot.org/annotation/VAR_013546|||http://purl.uniprot.org/annotation/VAR_013547|||http://purl.uniprot.org/annotation/VAR_013548|||http://purl.uniprot.org/annotation/VAR_013549|||http://purl.uniprot.org/annotation/VAR_013550|||http://purl.uniprot.org/annotation/VAR_013551|||http://purl.uniprot.org/annotation/VAR_013552|||http://purl.uniprot.org/annotation/VAR_013553|||http://purl.uniprot.org/annotation/VAR_013554|||http://purl.uniprot.org/annotation/VAR_013555|||http://purl.uniprot.org/annotation/VAR_026129|||http://purl.uniprot.org/annotation/VAR_026130|||http://purl.uniprot.org/annotation/VAR_026131|||http://purl.uniprot.org/annotation/VAR_026132|||http://purl.uniprot.org/annotation/VAR_026133|||http://purl.uniprot.org/annotation/VAR_037937|||http://purl.uniprot.org/annotation/VAR_037938|||http://purl.uniprot.org/annotation/VAR_037939|||http://purl.uniprot.org/annotation/VAR_037940|||http://purl.uniprot.org/annotation/VAR_037941|||http://purl.uniprot.org/annotation/VAR_037942|||http://purl.uniprot.org/annotation/VAR_037943|||http://purl.uniprot.org/annotation/VAR_037944|||http://purl.uniprot.org/annotation/VAR_037945|||http://purl.uniprot.org/annotation/VAR_037946|||http://purl.uniprot.org/annotation/VAR_037947|||http://purl.uniprot.org/annotation/VAR_038346|||http://purl.uniprot.org/annotation/VAR_053875|||http://purl.uniprot.org/annotation/VAR_062340|||http://purl.uniprot.org/annotation/VAR_062341|||http://purl.uniprot.org/annotation/VAR_062342|||http://purl.uniprot.org/annotation/VAR_062343|||http://purl.uniprot.org/annotation/VAR_062344|||http://purl.uniprot.org/annotation/VAR_062345|||http://purl.uniprot.org/annotation/VAR_062346|||http://purl.uniprot.org/annotation/VAR_062347|||http://purl.uniprot.org/annotation/VAR_062348|||http://purl.uniprot.org/annotation/VAR_062349|||http://purl.uniprot.org/annotation/VAR_062350|||http://purl.uniprot.org/annotation/VAR_062351|||http://purl.uniprot.org/annotation/VAR_062352|||http://purl.uniprot.org/annotation/VAR_062353|||http://purl.uniprot.org/annotation/VAR_062354|||http://purl.uniprot.org/annotation/VAR_062355|||http://purl.uniprot.org/annotation/VAR_062356|||http://purl.uniprot.org/annotation/VAR_062357|||http://purl.uniprot.org/annotation/VAR_062358|||http://purl.uniprot.org/annotation/VAR_062359|||http://purl.uniprot.org/annotation/VAR_062360|||http://purl.uniprot.org/annotation/VAR_062361|||http://purl.uniprot.org/annotation/VAR_062362|||http://purl.uniprot.org/annotation/VAR_062363|||http://purl.uniprot.org/annotation/VAR_062364|||http://purl.uniprot.org/annotation/VAR_062365|||http://purl.uniprot.org/annotation/VAR_062366|||http://purl.uniprot.org/annotation/VAR_062367|||http://purl.uniprot.org/annotation/VAR_062368|||http://purl.uniprot.org/annotation/VAR_062369|||http://purl.uniprot.org/annotation/VAR_062370|||http://purl.uniprot.org/annotation/VAR_074054|||http://purl.uniprot.org/annotation/VAR_074055|||http://purl.uniprot.org/annotation/VAR_074056|||http://purl.uniprot.org/annotation/VAR_074057|||http://purl.uniprot.org/annotation/VAR_074058|||http://purl.uniprot.org/annotation/VAR_074059|||http://purl.uniprot.org/annotation/VAR_074060|||http://purl.uniprot.org/annotation/VAR_074061|||http://purl.uniprot.org/annotation/VAR_074062|||http://purl.uniprot.org/annotation/VAR_074063|||http://purl.uniprot.org/annotation/VAR_074064|||http://purl.uniprot.org/annotation/VAR_074065|||http://purl.uniprot.org/annotation/VAR_074066|||http://purl.uniprot.org/annotation/VSP_031241|||http://purl.uniprot.org/annotation/VSP_039974
http://togogenome.org/gene/9606:FAM135A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RCC7|||http://purl.uniprot.org/uniprot/Q9P2D6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DUF676|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein FAM135A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314168|||http://purl.uniprot.org/annotation/VAR_037854|||http://purl.uniprot.org/annotation/VAR_037855|||http://purl.uniprot.org/annotation/VAR_037856|||http://purl.uniprot.org/annotation/VSP_030225|||http://purl.uniprot.org/annotation/VSP_030226|||http://purl.uniprot.org/annotation/VSP_030227|||http://purl.uniprot.org/annotation/VSP_030230
http://togogenome.org/gene/9606:CD300A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QKQ4|||http://purl.uniprot.org/uniprot/Q9UGN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CMRF35-like molecule 8|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014682|||http://purl.uniprot.org/annotation/VAR_030797|||http://purl.uniprot.org/annotation/VSP_010558|||http://purl.uniprot.org/annotation/VSP_010559|||http://purl.uniprot.org/annotation/VSP_041246
http://togogenome.org/gene/9606:TARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2JGV3|||http://purl.uniprot.org/uniprot/Q0VGM3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||T-cell receptor gamma alternate reading frame protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000457484
http://togogenome.org/gene/9606:MKRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13064                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||In CPPB2.|||In a colorectal cancer sample; somatic mutation.|||Makorin-type Cys-His|||Probable E3 ubiquitin-protein ligase makorin-3|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055959|||http://purl.uniprot.org/annotation/VAR_035955|||http://purl.uniprot.org/annotation/VAR_035956|||http://purl.uniprot.org/annotation/VAR_070103|||http://purl.uniprot.org/annotation/VAR_073023|||http://purl.uniprot.org/annotation/VAR_073024|||http://purl.uniprot.org/annotation/VAR_073025
http://togogenome.org/gene/9606:SPATA24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W54                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Required for interaction with CBX5 and TBPL1|||Spermatogenesis-associated protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328979|||http://purl.uniprot.org/annotation/VSP_032867
http://togogenome.org/gene/9606:CCDC30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVM6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 30|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336044|||http://purl.uniprot.org/annotation/VAR_043472|||http://purl.uniprot.org/annotation/VSP_033791|||http://purl.uniprot.org/annotation/VSP_033792
http://togogenome.org/gene/9606:CCDC38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q502W7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 38|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234490|||http://purl.uniprot.org/annotation/VAR_056778|||http://purl.uniprot.org/annotation/VAR_056779
http://togogenome.org/gene/9606:NCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4M6|||http://purl.uniprot.org/uniprot/E7ERP6|||http://purl.uniprot.org/uniprot/O43639                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with DOCK1.|||Cytoplasmic protein NCK2|||Disordered|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||SH2|||SH3|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096767
http://togogenome.org/gene/9606:RAB11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62491                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolishes SH3BP5-mediated guanine nucleotide exchange.|||Constitutively active mutant. Decreases GTPase activity. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells.|||Cysteine methyl ester|||Decreases SH3BP5-mediated guanine nucleotide exchange.|||Disordered|||Dominant-negative mutant. Induces increased number of binucleated cells, indicating defects in cytokinesis. Inhibits the transport of NPC1L1 to the plama membrane. Disrupts the trafficking of CDH1 to the plasma membrane and promotes accumulation of CDH1 in RAB11A endosomes in nonpolarized cells. Promotes mistargeting of CDH1 to the apical membrane in polarized cells. Increased interaction with ATP9A. Loss of interaction with WDR44, decreased WDR44-positive tubules and loss of E-cadherin export.|||Effector region|||Impairs protein folding and decreases affinity for guanine nucleotides.|||Impairs protein folding.|||In isoform 2.|||Mildly decreases SH3BP5-mediated guanine nucleotide exchange.|||N-acetylglycine|||Nearly abolishes SH3BP5-mediated guanine nucleotide exchange.|||Ras-related protein Rab-11A|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121151|||http://purl.uniprot.org/annotation/PRO_0000370807|||http://purl.uniprot.org/annotation/VSP_046755
http://togogenome.org/gene/9606:NIPSNAP3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFN0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N6-acetyllysine|||Protein NipSnap homolog 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221152|||http://purl.uniprot.org/annotation/VAR_020442
http://togogenome.org/gene/9606:MCM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L590                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD80; cell cycle defect and replication stress in patient-derived cells; loss of nuclear localization.|||In IMD80; no effect on the formation of the replisome.|||In isoform 2.|||N-terminal domain|||OB-fold domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein MCM10 homolog|||Zinc finger-like 1|||Zinc finger-like 2|||Zinc finger-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278320|||http://purl.uniprot.org/annotation/VAR_030771|||http://purl.uniprot.org/annotation/VAR_030772|||http://purl.uniprot.org/annotation/VAR_030773|||http://purl.uniprot.org/annotation/VAR_053836|||http://purl.uniprot.org/annotation/VAR_053837|||http://purl.uniprot.org/annotation/VAR_085769|||http://purl.uniprot.org/annotation/VAR_085770|||http://purl.uniprot.org/annotation/VSP_029951
http://togogenome.org/gene/9606:COX6B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YFQ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase subunit 6B2|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194921
http://togogenome.org/gene/9606:TMTC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z639|||http://purl.uniprot.org/uniprot/F8VSH2|||http://purl.uniprot.org/uniprot/Q8N394                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  DUF1736|||Helical|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase TMTC2|||TPR|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||dolichyl-phosphate-mannose--protein mannosyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280290|||http://purl.uniprot.org/annotation/PRO_5003379333|||http://purl.uniprot.org/annotation/VAR_031113|||http://purl.uniprot.org/annotation/VAR_031114|||http://purl.uniprot.org/annotation/VAR_053852
http://togogenome.org/gene/9606:ZNF181                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM69|||http://purl.uniprot.org/uniprot/Q2M3W8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 181                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230666|||http://purl.uniprot.org/annotation/VSP_017824|||http://purl.uniprot.org/annotation/VSP_043416
http://togogenome.org/gene/9606:INTS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVH2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Integrator complex subunit 7|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259549|||http://purl.uniprot.org/annotation/VAR_028963|||http://purl.uniprot.org/annotation/VSP_021463|||http://purl.uniprot.org/annotation/VSP_021464|||http://purl.uniprot.org/annotation/VSP_043201
http://togogenome.org/gene/9606:NEK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SG6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In NPHP9; a full-length mouse NEK8 construct containing the mutation shows a defect in ciliary localization with no apparent effect on ciliation, mitosis or centriole number.|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||Serine/threonine-protein kinase Nek8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086432|||http://purl.uniprot.org/annotation/VAR_065769|||http://purl.uniprot.org/annotation/VAR_065770|||http://purl.uniprot.org/annotation/VAR_065771
http://togogenome.org/gene/9606:MRS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQX2|||http://purl.uniprot.org/uniprot/B4DSN2|||http://purl.uniprot.org/uniprot/Q9HD23                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Magnesium transporter MRS2 homolog, mitochondrial|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042837|||http://purl.uniprot.org/annotation/VAR_023782|||http://purl.uniprot.org/annotation/VAR_061129|||http://purl.uniprot.org/annotation/VSP_016207|||http://purl.uniprot.org/annotation/VSP_016208|||http://purl.uniprot.org/annotation/VSP_016209|||http://purl.uniprot.org/annotation/VSP_016210|||http://purl.uniprot.org/annotation/VSP_055287
http://togogenome.org/gene/9606:DMRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05C20|||http://purl.uniprot.org/uniprot/Q5HYK2|||http://purl.uniprot.org/uniprot/Q9Y5R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DM|||Disordered|||Doublesex- and mab-3-related transcription factor 2|||Helical|||In isoform 2.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207048|||http://purl.uniprot.org/annotation/VAR_067719|||http://purl.uniprot.org/annotation/VAR_067720|||http://purl.uniprot.org/annotation/VSP_041247|||http://purl.uniprot.org/annotation/VSP_041248|||http://purl.uniprot.org/annotation/VSP_041249
http://togogenome.org/gene/9606:OR7E24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IFN5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7E24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281642|||http://purl.uniprot.org/annotation/VAR_053236|||http://purl.uniprot.org/annotation/VAR_053237
http://togogenome.org/gene/9606:LIMK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53667                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation by ROCK1.|||Abolishes kinase activity.|||Abrogates kinase activity.|||Disordered|||Enhances actin aggregation.|||Enhances kinase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LIM domain kinase 1|||LIM zinc-binding 1|||LIM zinc-binding 2|||PDZ|||Phosphomimetic mutant; enhances kinase activity.|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Phosphothreonine; by ROCK1 and PAK1|||Polar residues|||Protein kinase|||Reduces actin aggregation.|||Reduces kinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075803|||http://purl.uniprot.org/annotation/VAR_042246|||http://purl.uniprot.org/annotation/VAR_042247|||http://purl.uniprot.org/annotation/VAR_042248|||http://purl.uniprot.org/annotation/VAR_050148|||http://purl.uniprot.org/annotation/VSP_003125|||http://purl.uniprot.org/annotation/VSP_003126|||http://purl.uniprot.org/annotation/VSP_003127|||http://purl.uniprot.org/annotation/VSP_043331
http://togogenome.org/gene/9606:PDGFD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZP0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage into active form; when associated with A-247.|||Abolishes cleavage into active form; when associated with A-249.|||CUB|||Cleavage|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor D, latent form|||Platelet-derived growth factor D, receptor-binding form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250188|||http://purl.uniprot.org/annotation/PRO_0000250189|||http://purl.uniprot.org/annotation/VAR_036418|||http://purl.uniprot.org/annotation/VAR_051563|||http://purl.uniprot.org/annotation/VSP_020615
http://togogenome.org/gene/9606:ADAMTS20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59510                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 20|||Disintegrin|||GON|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 10|||TSP type-1 11|||TSP type-1 12|||TSP type-1 13|||TSP type-1 14|||TSP type-1 15|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029206|||http://purl.uniprot.org/annotation/PRO_0000029207|||http://purl.uniprot.org/annotation/VAR_057088|||http://purl.uniprot.org/annotation/VAR_057089|||http://purl.uniprot.org/annotation/VAR_057090|||http://purl.uniprot.org/annotation/VSP_007106|||http://purl.uniprot.org/annotation/VSP_007107|||http://purl.uniprot.org/annotation/VSP_007108|||http://purl.uniprot.org/annotation/VSP_047084
http://togogenome.org/gene/9606:PDE4DIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU43                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein|||Disordered|||In isoform 13.|||In isoform 2 and isoform 13.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 12.|||In isoform 3.|||In isoform 4.|||In isoform 7.|||In isoform 8 and isoform 11.|||In isoform 8 and isoform 9.|||In isoform 9, isoform 10 and isoform 12.|||Myomegalin|||Olduvai|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307690|||http://purl.uniprot.org/annotation/VAR_036627|||http://purl.uniprot.org/annotation/VAR_036628|||http://purl.uniprot.org/annotation/VAR_036629|||http://purl.uniprot.org/annotation/VAR_036630|||http://purl.uniprot.org/annotation/VAR_051204|||http://purl.uniprot.org/annotation/VAR_051205|||http://purl.uniprot.org/annotation/VAR_051206|||http://purl.uniprot.org/annotation/VAR_051207|||http://purl.uniprot.org/annotation/VAR_051208|||http://purl.uniprot.org/annotation/VAR_051209|||http://purl.uniprot.org/annotation/VAR_051210|||http://purl.uniprot.org/annotation/VAR_051211|||http://purl.uniprot.org/annotation/VAR_051212|||http://purl.uniprot.org/annotation/VAR_051213|||http://purl.uniprot.org/annotation/VAR_051214|||http://purl.uniprot.org/annotation/VAR_056951|||http://purl.uniprot.org/annotation/VAR_056952|||http://purl.uniprot.org/annotation/VAR_080232|||http://purl.uniprot.org/annotation/VSP_028772|||http://purl.uniprot.org/annotation/VSP_028773|||http://purl.uniprot.org/annotation/VSP_028774|||http://purl.uniprot.org/annotation/VSP_028775|||http://purl.uniprot.org/annotation/VSP_028776|||http://purl.uniprot.org/annotation/VSP_028777|||http://purl.uniprot.org/annotation/VSP_028778|||http://purl.uniprot.org/annotation/VSP_028779|||http://purl.uniprot.org/annotation/VSP_028780|||http://purl.uniprot.org/annotation/VSP_028781|||http://purl.uniprot.org/annotation/VSP_028782|||http://purl.uniprot.org/annotation/VSP_028783|||http://purl.uniprot.org/annotation/VSP_059333|||http://purl.uniprot.org/annotation/VSP_059334
http://togogenome.org/gene/9606:KCNK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57789                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform B.|||In isoform C.|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101758|||http://purl.uniprot.org/annotation/VAR_052428|||http://purl.uniprot.org/annotation/VAR_060216|||http://purl.uniprot.org/annotation/VSP_006697|||http://purl.uniprot.org/annotation/VSP_006698
http://togogenome.org/gene/9606:USP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35125                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not restore GAP activity in yeast complementation assay.|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||Nucleophile|||Polar residues|||Proton acceptor|||Rab-GAP TBC|||USP|||Ubiquitin carboxyl-terminal hydrolase 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080625|||http://purl.uniprot.org/annotation/VAR_051522|||http://purl.uniprot.org/annotation/VAR_051523|||http://purl.uniprot.org/annotation/VAR_059749|||http://purl.uniprot.org/annotation/VSP_010878|||http://purl.uniprot.org/annotation/VSP_010879|||http://purl.uniprot.org/annotation/VSP_010880|||http://purl.uniprot.org/annotation/VSP_010881
http://togogenome.org/gene/9606:AVL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBF6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Late secretory pathway protein AVL9 homolog|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247178|||http://purl.uniprot.org/annotation/VAR_027083|||http://purl.uniprot.org/annotation/VSP_019943
http://togogenome.org/gene/9606:SLC9A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14940|||http://purl.uniprot.org/uniprot/Q9NSW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with A-702; A-709; A-711 and A-712.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with A-702; A-709; A-711 and A-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with A-702; A-709; A-712 and A-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with A-702; A-711; A-712 and A-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with A-709; A-711; A-712 and A-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with D-702; D-709; D-711 and D-712.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with D-702; D-709; D-711 and D-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with D-702; D-709; D-712 and D-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with D-702; D-711; D-712 and D-714.|||Abolishes SLC9A5 phosphorylation by CSNK2A1 and abolishes CSNK2A1-mediated binding of ARRB2; when associated with D-709; D-711; D-712 and D-714.|||Acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Does not disrupt the binding of ARRB2. Does not affect endocytosis of SLC9A5.|||Does not disrupt the binding of ARRB2. Impaired endocytosis of SLC9A5.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for interaction with ARRB2|||Sodium/hydrogen exchanger 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052360
http://togogenome.org/gene/9606:ATF6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X796|||http://purl.uniprot.org/uniprot/Q6AZW6|||http://purl.uniprot.org/uniprot/Q99941                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BZIP|||Basic motif|||Cleavage; by MBTPS1|||Cyclic AMP-dependent transcription factor ATF-6 beta|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Important for cleavage by MBTPS2|||In isoform 1.|||Leucine-zipper|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Processed cyclic AMP-dependent transcription factor ATF-6 beta|||Removed|||Transcription activation|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076590|||http://purl.uniprot.org/annotation/PRO_0000296201|||http://purl.uniprot.org/annotation/VSP_000593
http://togogenome.org/gene/9606:PIAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNI3|||http://purl.uniprot.org/uniprot/Q9Y6X2                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 SUMO-protein ligase PIAS3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CCAR2|||LXXLL motif|||PINIT|||SAP|||SP-RING-type|||SUMO1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218979|||http://purl.uniprot.org/annotation/VAR_050535
http://togogenome.org/gene/9606:KATNAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EIJ8|||http://purl.uniprot.org/uniprot/Q8IYT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||Disordered|||In isoform 2.|||Katanin p60 ATPase-containing subunit A-like 2|||LisH|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333792|||http://purl.uniprot.org/annotation/VAR_043160|||http://purl.uniprot.org/annotation/VSP_033523
http://togogenome.org/gene/9606:ETF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7P8|||http://purl.uniprot.org/uniprot/P62495                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxylysine|||Abolishes methylation by N6AMT1.|||Eukaryotic peptide chain release factor subunit 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In AAQ mutant; abolished ability to mediate translation termination. Can recognize stop codons in ribosomal A-site, but is unable to catalyze peptidyl-tRNA hydrolysis, promoting ribosome collisions.|||In isoform 2.|||Loss of hydroxylation.|||N-acetylalanine|||N5-methylglutamine|||NIKS motif; plays an important role in translational termination|||Phosphothreonine|||Removed|||eRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143138|||http://purl.uniprot.org/annotation/VSP_056189
http://togogenome.org/gene/9606:PLA2G10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15496                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Group 10 secretory phospholipase A2|||Loss of PLA2 activity toward PAF. Impairs anti-adenoviral activity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022764|||http://purl.uniprot.org/annotation/PRO_0000022765
http://togogenome.org/gene/9606:ZNF775                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BV0                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 775                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280441|||http://purl.uniprot.org/annotation/VAR_059937
http://togogenome.org/gene/9606:GYPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06028                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycophorin-B|||Helical|||In M(v) antigen.|||In Mit antigen.|||In S antigen and Mit antigen.|||In isoform 2.|||In s(D) antigen.|||Not glycosylated|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012136|||http://purl.uniprot.org/annotation/VAR_003192|||http://purl.uniprot.org/annotation/VAR_030785|||http://purl.uniprot.org/annotation/VAR_047948|||http://purl.uniprot.org/annotation/VAR_047949|||http://purl.uniprot.org/annotation/VAR_047950|||http://purl.uniprot.org/annotation/VSP_047824
http://togogenome.org/gene/9606:CWC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXE8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Pre-mRNA-splicing factor CWC25 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288865|||http://purl.uniprot.org/annotation/VSP_025797
http://togogenome.org/gene/9606:STMN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW2|||http://purl.uniprot.org/uniprot/P16949                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphoserine; by CDK1, MAPK1 and MAPK3|||Phosphoserine; by PKA|||Removed|||SLD|||Stathmin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182389|||http://purl.uniprot.org/annotation/VSP_041377
http://togogenome.org/gene/9606:CR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20023                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complement receptor type 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform B.|||In isoform C and isoform D.|||In isoform D.|||N-linked (GlcNAc...) asparagine|||No effect on affinity for C3.|||Reduced affinity for C3.|||Strongly reduced affinity for C3.|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006010|||http://purl.uniprot.org/annotation/VAR_016164|||http://purl.uniprot.org/annotation/VAR_016165|||http://purl.uniprot.org/annotation/VAR_016166|||http://purl.uniprot.org/annotation/VSP_001208|||http://purl.uniprot.org/annotation/VSP_001209|||http://purl.uniprot.org/annotation/VSP_001210|||http://purl.uniprot.org/annotation/VSP_001211
http://togogenome.org/gene/9606:PTGR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G1C4|||http://purl.uniprot.org/uniprot/Q8N4Q0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Enoyl reductase (ER)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Prostaglandin reductase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223467|||http://purl.uniprot.org/annotation/VAR_048202|||http://purl.uniprot.org/annotation/VSP_055796
http://togogenome.org/gene/9606:XKR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Polar residues|||XK-related protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190782|||http://purl.uniprot.org/annotation/VSP_059371|||http://purl.uniprot.org/annotation/VSP_059372
http://togogenome.org/gene/9606:CHRFAM7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYA8|||http://purl.uniprot.org/uniprot/P36544|||http://purl.uniprot.org/uniprot/Q494W8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  115-fold more potently inhibited by the alpha-conotoxin ImI; but no change in inhibition by the alpha-conotoxin ImII.|||Associated with receptor activation|||CHRNA7-FAM7A fusion protein|||Cytoplasmic|||Essential for TMEM35A/NACHO-mediated proper subunit assembly and trafficking to cell membrane|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-7|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000366|||http://purl.uniprot.org/annotation/PRO_0000232101|||http://purl.uniprot.org/annotation/VSP_043019|||http://purl.uniprot.org/annotation/VSP_058107|||http://purl.uniprot.org/annotation/VSP_058108
http://togogenome.org/gene/9606:GCHFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30047                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Splice Variant|||Strand                                                                                  ^@                                                                                  GTP cyclohydrolase 1 feedback regulatory protein|||In isoform 2.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189675|||http://purl.uniprot.org/annotation/VSP_055592
http://togogenome.org/gene/9606:CNTFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26992                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Propeptide|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Ciliary neurotrophic factor receptor subunit alpha|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||GPI-anchor amidated serine|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010991|||http://purl.uniprot.org/annotation/PRO_0000010992
http://togogenome.org/gene/9606:NELL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXR2|||http://purl.uniprot.org/uniprot/F5H6I3|||http://purl.uniprot.org/uniprot/J3KNC5|||http://purl.uniprot.org/uniprot/K9UUD5|||http://purl.uniprot.org/uniprot/Q92832                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protein kinase C-binding protein NELL1|||VWFC|||VWFC 1|||VWFC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007664|||http://purl.uniprot.org/annotation/PRO_5002790203|||http://purl.uniprot.org/annotation/PRO_5003327275|||http://purl.uniprot.org/annotation/PRO_5014098590|||http://purl.uniprot.org/annotation/VAR_020167|||http://purl.uniprot.org/annotation/VAR_035834|||http://purl.uniprot.org/annotation/VAR_047828|||http://purl.uniprot.org/annotation/VAR_047829|||http://purl.uniprot.org/annotation/VAR_047830|||http://purl.uniprot.org/annotation/VSP_039954
http://togogenome.org/gene/9606:SMIM10L2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMW4|||http://purl.uniprot.org/uniprot/P0DMW5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Small integral membrane protein 10-like protein 2A|||Small integral membrane protein 10-like protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433232|||http://purl.uniprot.org/annotation/PRO_0000433233
http://togogenome.org/gene/9606:MPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E325|||http://purl.uniprot.org/uniprot/Q00013                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  55 kDa erythrocyte membrane protein|||Guanylate kinase-like|||In isoform 2.|||In isoform 3.|||Interaction with PALS1|||N-acetylthreonine|||PDZ|||Phosphoserine|||Phosphothreonine|||Removed|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094565|||http://purl.uniprot.org/annotation/VAR_011914|||http://purl.uniprot.org/annotation/VSP_042675|||http://purl.uniprot.org/annotation/VSP_044634
http://togogenome.org/gene/9606:RPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04844                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022244|||http://purl.uniprot.org/annotation/VAR_054040|||http://purl.uniprot.org/annotation/VSP_043051|||http://purl.uniprot.org/annotation/VSP_043052
http://togogenome.org/gene/9606:HEPHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZM0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Ferroxidase HEPHL1|||Helical|||In HJDD; due to a nucleotide substitution that affects a canonical splice site; patient cells contain normally spliced transcripts corresponding to protein variant T-355 but also transcripts lacking exon 5 and corresponding to protein variant 271-L--A-355 del.|||In HJDD; due to a nucleotide substitution that affects a canonical splice site; patient cells contain transcripts lacking exon 5 and corresponding to protein variant 271-L--A-355 del but also normally spliced transcripts corresponding to protein variant T-355; loss of ferroxidase activity.|||In HJDD; loss of ferroxidase activity.|||N-linked (GlcNAc...) asparagine|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||type 1 copper site|||type 2 copper site|||type 3 copper site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346771|||http://purl.uniprot.org/annotation/VAR_045903|||http://purl.uniprot.org/annotation/VAR_045904|||http://purl.uniprot.org/annotation/VAR_082699|||http://purl.uniprot.org/annotation/VAR_082700|||http://purl.uniprot.org/annotation/VAR_082701
http://togogenome.org/gene/9606:OR51S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWN3|||http://purl.uniprot.org/uniprot/Q8NGJ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150762|||http://purl.uniprot.org/annotation/VAR_024145|||http://purl.uniprot.org/annotation/VAR_034329|||http://purl.uniprot.org/annotation/VAR_034330|||http://purl.uniprot.org/annotation/VAR_053331
http://togogenome.org/gene/9606:PPIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PCH14.|||In PCH14; reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells.|||In PCH14; strongly reduced interaction with SNW1; slightly reduced protein levels compared to wild-type, after transfection in HEK293T cell line, reduced thermal stability and increased aggregation propensity in vitro; in transgenic knockin mice, produces a pontocerebellar hypoplasia-like phenotype.|||In PCH14; strongly reduced interaction with SNW1; strongly reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells; in transgenic knockin mice, produces a pontocerebellar hypoplasia-like phenotype.|||In PCH14; unknown pathological significance.|||In PCH14; unknown pathological significance; reduced interaction with SNW1; no effect on protein expression level, but shows reduced thermal stability and increased aggregation propensity in vitro.|||In PCH14; unknown pathological significance; strongly reduced protein levels compared to wild-type after transfection in HEK293T cell line.|||Loss of isomerase activity. Can rescue splicing defects when transfected in knockout cells.|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase-like 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064164|||http://purl.uniprot.org/annotation/VAR_051772|||http://purl.uniprot.org/annotation/VAR_085506|||http://purl.uniprot.org/annotation/VAR_085507|||http://purl.uniprot.org/annotation/VAR_085508|||http://purl.uniprot.org/annotation/VAR_085509|||http://purl.uniprot.org/annotation/VAR_085510|||http://purl.uniprot.org/annotation/VAR_085511|||http://purl.uniprot.org/annotation/VAR_085512|||http://purl.uniprot.org/annotation/VAR_085513|||http://purl.uniprot.org/annotation/VAR_085514
http://togogenome.org/gene/9606:ZSWIM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2V4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SWIM-type|||Zinc finger SWIM domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311802|||http://purl.uniprot.org/annotation/VSP_029586|||http://purl.uniprot.org/annotation/VSP_029587|||http://purl.uniprot.org/annotation/VSP_029590|||http://purl.uniprot.org/annotation/VSP_029591
http://togogenome.org/gene/9606:RAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2V3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In MCOPS16; does not affect nuclear localization; reduces DNA binding activity.|||In MCOPS16; unknown pathological significance.|||In isoform 2.|||Nuclear localization signal|||OAR|||Octapeptide motif|||Polar residues|||Pro residues|||Retinal homeobox protein Rx                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049276|||http://purl.uniprot.org/annotation/VAR_020150|||http://purl.uniprot.org/annotation/VAR_034905|||http://purl.uniprot.org/annotation/VAR_075630|||http://purl.uniprot.org/annotation/VAR_075631|||http://purl.uniprot.org/annotation/VAR_075632|||http://purl.uniprot.org/annotation/VSP_053558|||http://purl.uniprot.org/annotation/VSP_053559
http://togogenome.org/gene/9606:CCN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95388                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CCN family member 4|||CTCK|||IGFBP N-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||TSP type-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014406|||http://purl.uniprot.org/annotation/VAR_061265|||http://purl.uniprot.org/annotation/VSP_008008|||http://purl.uniprot.org/annotation/VSP_008009|||http://purl.uniprot.org/annotation/VSP_042010|||http://purl.uniprot.org/annotation/VSP_045958|||http://purl.uniprot.org/annotation/VSP_045959|||http://purl.uniprot.org/annotation/VSP_047706|||http://purl.uniprot.org/annotation/VSP_047707
http://togogenome.org/gene/9606:TECPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15040                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||TECPR 1|||TECPR 2|||TECPR 3|||TECPR 4|||TECPR 5|||TECPR 6|||Tectonin beta-propeller repeat-containing protein 2|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050747|||http://purl.uniprot.org/annotation/VAR_046529|||http://purl.uniprot.org/annotation/VAR_046530|||http://purl.uniprot.org/annotation/VAR_046531|||http://purl.uniprot.org/annotation/VAR_046532|||http://purl.uniprot.org/annotation/VSP_044793|||http://purl.uniprot.org/annotation/VSP_044794
http://togogenome.org/gene/9606:CYYR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine and tyrosine-rich protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021054|||http://purl.uniprot.org/annotation/VAR_044042|||http://purl.uniprot.org/annotation/VAR_044043|||http://purl.uniprot.org/annotation/VSP_034245|||http://purl.uniprot.org/annotation/VSP_057143|||http://purl.uniprot.org/annotation/VSP_057144|||http://purl.uniprot.org/annotation/VSP_057145|||http://purl.uniprot.org/annotation/VSP_057146|||http://purl.uniprot.org/annotation/VSP_057147|||http://purl.uniprot.org/annotation/VSP_057148|||http://purl.uniprot.org/annotation/VSP_057149|||http://purl.uniprot.org/annotation/VSP_057150
http://togogenome.org/gene/9606:BCL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5B0A5|||http://purl.uniprot.org/uniprot/P41182                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished ubiquitination by the SCF(FBXL17) complex.|||Abolishes DNA-binding and transcriptional repression activity, no effect on nuclear localization and interaction with HDAC5.|||Abolishes DNA-binding and transcriptional repression activity, perturbs nuclear localization. No effect on interaction with HDAC5.|||Abolishes acetylation. No effect on interaction with MTA3, NCOR1 and NCOR2.|||Abolishes interaction with HDAC2 and MTA3 as well as transcriptional repressor and transforming activities. Abolishes interaction with NCOR2 and HDAC2, no effect on interaction with CTBP1 and transcriptional autoinhibition; when associated with K-21 and A-116.|||Abolishes interaction with NCOR2 and HDAC2, no effect on interaction with CTBP1 and transcriptional autoinhibition; when associated with A-116 and 376-Q--Q-379.|||Abolishes interaction with NCOR2 and HDAC2, no effect on interaction with CTBP1 and transcriptional autoinhibition; when associated with K-21 and 376-Q--Q-379.|||B-cell lymphoma 6 protein|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Decrease in phosphorylation by MAPK1.|||Disordered|||In isoform 2.|||N6-acetyllysine|||No effect on DNA-binding, nuclear localization, transcriptional repression activity and interaction with HDAC5.|||No effect on acetylation.|||No effect on interaction with PIN1.|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||Required for interaction with NuRD complex and for transcriptional repressor activity|||Strongly reduces interaction with PIN1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047098|||http://purl.uniprot.org/annotation/VAR_014825|||http://purl.uniprot.org/annotation/VAR_019970|||http://purl.uniprot.org/annotation/VAR_052709|||http://purl.uniprot.org/annotation/VSP_042709
http://togogenome.org/gene/9606:LCTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWM7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Lactase-like protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042251|||http://purl.uniprot.org/annotation/VAR_023586|||http://purl.uniprot.org/annotation/VAR_049297|||http://purl.uniprot.org/annotation/VSP_054596
http://togogenome.org/gene/9606:OR2M5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KFT3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2M5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293719|||http://purl.uniprot.org/annotation/VAR_064739
http://togogenome.org/gene/9606:GOLGA8H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CJ92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8H|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000405257
http://togogenome.org/gene/9606:SLPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03973                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Antileukoproteinase|||Elastase inhibitory domain|||Increases inhibition of chymotrypsin.|||No significant effect on inhibition of elastase, trypsin and chymotrypsin.|||Reactive bond for chymotrypsin, trypsin and elastase|||Reduced inhibition of elastase. Strongly reduced inhibition of chymotrypsin and trypsin.|||Strongly reduced inhibition of elastase. Abolishes inhibition of trypsin.|||WAP 1|||WAP 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041355
http://togogenome.org/gene/9606:POLR3H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y535                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase III subunit RPC8|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073994|||http://purl.uniprot.org/annotation/VSP_007067
http://togogenome.org/gene/9606:MEIOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Meiosis-specific coiled-coil domain-containing protein MEIOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325800|||http://purl.uniprot.org/annotation/VAR_039917|||http://purl.uniprot.org/annotation/VAR_039918|||http://purl.uniprot.org/annotation/VSP_038971|||http://purl.uniprot.org/annotation/VSP_038972|||http://purl.uniprot.org/annotation/VSP_038973
http://togogenome.org/gene/9606:CFAP45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL16                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 45|||Disordered|||In HTX11; loss of panaxonemal expression in respiratory cilia and in sperm flagella.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089410|||http://purl.uniprot.org/annotation/VAR_059600|||http://purl.uniprot.org/annotation/VAR_085330|||http://purl.uniprot.org/annotation/VAR_085331|||http://purl.uniprot.org/annotation/VSP_056614
http://togogenome.org/gene/9606:CAMK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16566                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase type IV|||Calmodulin-binding|||Disordered|||Fully active Ca2+/CaM-independent kinase; when associated with 309-A--A-312. Loss of interaction with PPP2CA/PPP2CB.|||Fully active Ca2+/CaM-independent kinase; when associated with 320-A-A-321.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||Increases phosphorylation of CREB1 2-fold. Decreases total O-linked glycosylation 2-fold. Increases ATP-binding affinity.|||Loss of activation by CaMKK1 or CaMKK2.|||Loss of activity.|||Loss of activity; dominant negative form.|||Loss of phosphorylation of CREB1.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PP2A-binding|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by CaMKK1 and CaMKK2|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086106|||http://purl.uniprot.org/annotation/VAR_040604|||http://purl.uniprot.org/annotation/VAR_040605|||http://purl.uniprot.org/annotation/VAR_040606|||http://purl.uniprot.org/annotation/VAR_040607
http://togogenome.org/gene/9606:SYT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8C5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Helical|||Synaptotagmin-13|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183975
http://togogenome.org/gene/9606:RAMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60895                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Receptor activity-modifying protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030172|||http://purl.uniprot.org/annotation/VSP_055838
http://togogenome.org/gene/9606:HYCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hyccin|||In HLD5; induces misfolding and degradation, leading to destabilization of the PI4K complex.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080005|||http://purl.uniprot.org/annotation/VAR_030647|||http://purl.uniprot.org/annotation/VAR_075100|||http://purl.uniprot.org/annotation/VAR_079751|||http://purl.uniprot.org/annotation/VSP_023126|||http://purl.uniprot.org/annotation/VSP_058128|||http://purl.uniprot.org/annotation/VSP_058129
http://togogenome.org/gene/9606:DSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02413                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein repeat 3|||Desmoglein repeat 4|||Desmoglein repeat 5|||Desmoglein-1|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003837|||http://purl.uniprot.org/annotation/PRO_0000003838|||http://purl.uniprot.org/annotation/VAR_020364|||http://purl.uniprot.org/annotation/VAR_024385|||http://purl.uniprot.org/annotation/VAR_024386|||http://purl.uniprot.org/annotation/VAR_055573|||http://purl.uniprot.org/annotation/VAR_055574|||http://purl.uniprot.org/annotation/VAR_055575|||http://purl.uniprot.org/annotation/VAR_055576|||http://purl.uniprot.org/annotation/VAR_055577|||http://purl.uniprot.org/annotation/VAR_060248|||http://purl.uniprot.org/annotation/VAR_060249|||http://purl.uniprot.org/annotation/VSP_055930
http://togogenome.org/gene/9606:ZNF721                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF20                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20; degenerate|||C2H2-type 21; degenerate|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24; degenerate|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 30|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Zinc finger protein 721                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306879|||http://purl.uniprot.org/annotation/VSP_040879
http://togogenome.org/gene/9606:RASA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14644                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||C2 1|||C2 2|||In isoform 2.|||N-acetylalanine|||No binding to IP4 and loss of plasma membrane localization.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Ras GTPase-activating protein 3|||Ras-GAP|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056642|||http://purl.uniprot.org/annotation/VSP_056141
http://togogenome.org/gene/9606:NPIPB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VUA1                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:IL22RA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6P7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Interleukin-22 receptor subunit alpha-1|||Loss of response to IL22.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Strongly reduced response to IL22.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324320|||http://purl.uniprot.org/annotation/VAR_039699|||http://purl.uniprot.org/annotation/VAR_039700|||http://purl.uniprot.org/annotation/VAR_039701|||http://purl.uniprot.org/annotation/VAR_039702|||http://purl.uniprot.org/annotation/VAR_039703|||http://purl.uniprot.org/annotation/VAR_039704
http://togogenome.org/gene/9606:OR5M3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGP4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150605|||http://purl.uniprot.org/annotation/VAR_057549|||http://purl.uniprot.org/annotation/VAR_057550
http://togogenome.org/gene/9606:POP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F88|||http://purl.uniprot.org/uniprot/Q99575                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ANXD2.|||In a breast cancer sample; somatic mutation.|||POPLD|||Phosphoserine|||Polar residues|||Pop1 N-terminal|||Ribonucleases P/MRP protein subunit POP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058513|||http://purl.uniprot.org/annotation/VAR_036232|||http://purl.uniprot.org/annotation/VAR_057746|||http://purl.uniprot.org/annotation/VAR_057747|||http://purl.uniprot.org/annotation/VAR_057748|||http://purl.uniprot.org/annotation/VAR_057749|||http://purl.uniprot.org/annotation/VAR_067755|||http://purl.uniprot.org/annotation/VAR_078770|||http://purl.uniprot.org/annotation/VAR_078771
http://togogenome.org/gene/9606:COL18A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39060                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cell attachment site|||Collagen alpha-1(XVIII) chain|||Disordered|||Endostatin|||FZ|||In GLCC; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Laminin G-like|||May be associated with increased risk for prostate cancer; results in decreased affinity for laminin.|||N-linked (GlcNAc...) asparagine|||Non-collagenous domain 1|||Non-collagenous domain 1 association domain|||Non-collagenous domain 1 hinge region|||Nonhelical region 1 (NC1)|||Nonhelical region 10 (NC10)|||Nonhelical region 11 (NC11)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Nonhelical region 4 (NC4)|||Nonhelical region 5 (NC5)|||Nonhelical region 6 (NC6)|||Nonhelical region 7 (NC7)|||Nonhelical region 8 (NC8)|||Nonhelical region 9 (NC9)|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphothreonine|||Polar residues|||Pro residues|||Triple-helical region 1 (COL1)|||Triple-helical region 10 (COL10)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)|||Triple-helical region 4 (COL4)|||Triple-helical region 5 (COL5)|||Triple-helical region 6 (COL6)|||Triple-helical region 7 (COL7)|||Triple-helical region 8 (COL8)|||Triple-helical region 9 (COL9)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000150|||http://purl.uniprot.org/annotation/PRO_0000005793|||http://purl.uniprot.org/annotation/PRO_0000005794|||http://purl.uniprot.org/annotation/PRO_0000441861|||http://purl.uniprot.org/annotation/VAR_012709|||http://purl.uniprot.org/annotation/VAR_018053|||http://purl.uniprot.org/annotation/VAR_018054|||http://purl.uniprot.org/annotation/VAR_018055|||http://purl.uniprot.org/annotation/VAR_018056|||http://purl.uniprot.org/annotation/VAR_059232|||http://purl.uniprot.org/annotation/VAR_059233|||http://purl.uniprot.org/annotation/VAR_061115|||http://purl.uniprot.org/annotation/VAR_084282|||http://purl.uniprot.org/annotation/VSP_023130|||http://purl.uniprot.org/annotation/VSP_023131|||http://purl.uniprot.org/annotation/VSP_023132
http://togogenome.org/gene/9606:ZBTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N680                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047709
http://togogenome.org/gene/9606:SCD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SK9|||http://purl.uniprot.org/uniprot/Q86UC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In DFNA79; unknown pathological significance.|||In isoform 2.|||Lumenal|||Stearoyl-CoA desaturase 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312653|||http://purl.uniprot.org/annotation/VAR_085092|||http://purl.uniprot.org/annotation/VSP_029883
http://togogenome.org/gene/9606:ADGRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14514                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage and production of vasculostatin-120.|||Abolishes processing of vasculostatin-40.|||Adhesion G protein-coupled receptor B1|||Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||Does not affect processing of vasculostatin-40.|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increased levels of vasculostatin-120 and decreased levels of vasculostatin-40.|||Indispensable for interaction with MAGI1|||Involved in interaction with MAGI1|||N-linked (GlcNAc...) asparagine|||N-terminal stalk following vasculostatin-120 cleavage which is not required for signaling activity|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||Vasculostatin-120|||Vasculostatin-40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012863|||http://purl.uniprot.org/annotation/PRO_0000441804|||http://purl.uniprot.org/annotation/PRO_0000441805
http://togogenome.org/gene/9606:P2RY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41231                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070013|||http://purl.uniprot.org/annotation/VAR_054870|||http://purl.uniprot.org/annotation/VAR_054871|||http://purl.uniprot.org/annotation/VAR_054872
http://togogenome.org/gene/9606:ZFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPR6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DZF|||Disordered|||In isoform 2.|||In isoform 3.|||Pro residues|||Zinc finger RNA-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308958|||http://purl.uniprot.org/annotation/VAR_036886|||http://purl.uniprot.org/annotation/VAR_036887|||http://purl.uniprot.org/annotation/VAR_036888|||http://purl.uniprot.org/annotation/VAR_036889|||http://purl.uniprot.org/annotation/VAR_036890|||http://purl.uniprot.org/annotation/VAR_036891|||http://purl.uniprot.org/annotation/VAR_061730|||http://purl.uniprot.org/annotation/VSP_040635|||http://purl.uniprot.org/annotation/VSP_040636|||http://purl.uniprot.org/annotation/VSP_057301|||http://purl.uniprot.org/annotation/VSP_057302
http://togogenome.org/gene/9606:CDX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47902                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein CDX-1|||In isoform 2.|||Interaction with 5-mCpG DNA|||Interaction with DNA|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048846|||http://purl.uniprot.org/annotation/VAR_020149|||http://purl.uniprot.org/annotation/VSP_021030
http://togogenome.org/gene/9606:DGLUCY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVU6|||http://purl.uniprot.org/uniprot/Q4LE40|||http://purl.uniprot.org/uniprot/Q7Z3D6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  D-glutamate cyclase, mitochondrial|||D-glutamate cyclase-like C-terminal|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036292|||http://purl.uniprot.org/annotation/VAR_018738|||http://purl.uniprot.org/annotation/VAR_018739|||http://purl.uniprot.org/annotation/VAR_052599|||http://purl.uniprot.org/annotation/VAR_052600|||http://purl.uniprot.org/annotation/VAR_052601|||http://purl.uniprot.org/annotation/VAR_052602|||http://purl.uniprot.org/annotation/VSP_010505|||http://purl.uniprot.org/annotation/VSP_010506|||http://purl.uniprot.org/annotation/VSP_010507|||http://purl.uniprot.org/annotation/VSP_010508|||http://purl.uniprot.org/annotation/VSP_010509|||http://purl.uniprot.org/annotation/VSP_010510|||http://purl.uniprot.org/annotation/VSP_010511
http://togogenome.org/gene/9606:TMEM35B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCS4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 35B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411096
http://togogenome.org/gene/9606:PRM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NNZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Protamine-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261158|||http://purl.uniprot.org/annotation/VAR_034414
http://togogenome.org/gene/9606:PRAMEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95521                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156975|||http://purl.uniprot.org/annotation/VAR_034396|||http://purl.uniprot.org/annotation/VAR_034397|||http://purl.uniprot.org/annotation/VAR_053604|||http://purl.uniprot.org/annotation/VAR_053605|||http://purl.uniprot.org/annotation/VAR_060091|||http://purl.uniprot.org/annotation/VAR_060092|||http://purl.uniprot.org/annotation/VAR_062138
http://togogenome.org/gene/9606:TEX101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY14                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Testis-expressed protein 101|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247621|||http://purl.uniprot.org/annotation/PRO_0000247622|||http://purl.uniprot.org/annotation/VAR_059883|||http://purl.uniprot.org/annotation/VAR_082931|||http://purl.uniprot.org/annotation/VSP_020029
http://togogenome.org/gene/9606:MID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X255|||http://purl.uniprot.org/uniprot/A0A8I5KPE0|||http://purl.uniprot.org/uniprot/A0A8I5KR14|||http://purl.uniprot.org/uniprot/O15344                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B box-type 1|||B box-type 2|||B30.2/SPRY|||Basic and acidic residues|||COS|||Disordered|||E3 ubiquitin-protein ligase Midline-1|||Fibronectin type-III|||Helical|||In GBBB.|||In isoform 2.|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056227|||http://purl.uniprot.org/annotation/VAR_013758|||http://purl.uniprot.org/annotation/VAR_013759|||http://purl.uniprot.org/annotation/VAR_013760|||http://purl.uniprot.org/annotation/VAR_013761|||http://purl.uniprot.org/annotation/VAR_013762|||http://purl.uniprot.org/annotation/VAR_025495|||http://purl.uniprot.org/annotation/VAR_025496|||http://purl.uniprot.org/annotation/VSP_005735
http://togogenome.org/gene/9606:RIMKLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  ATP-grasp|||Beta-citrylglutamate synthase B|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282571|||http://purl.uniprot.org/annotation/VSP_024198|||http://purl.uniprot.org/annotation/VSP_024199
http://togogenome.org/gene/9606:CRYBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05813                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Beta-crystallin A3|||Beta-crystallin A3, isoform A1, Delta4 form|||Beta-crystallin A3, isoform A1, Delta7 form|||Beta-crystallin A3, isoform A1, Delta8 form|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Disordered|||In CTRCT10.|||In isoform A1.|||N-acetylalanine|||N-acetylmethionine|||N-terminal arm|||Polar residues|||Removed|||S-glutathionyl cysteine; alternate|||S-methylcysteine|||S-methylcysteine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006331|||http://purl.uniprot.org/annotation/PRO_0000226692|||http://purl.uniprot.org/annotation/PRO_0000226693|||http://purl.uniprot.org/annotation/PRO_0000226694|||http://purl.uniprot.org/annotation/VAR_084782|||http://purl.uniprot.org/annotation/VSP_018710
http://togogenome.org/gene/9606:NPRL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z220|||http://purl.uniprot.org/uniprot/B7Z6Q0|||http://purl.uniprot.org/uniprot/Q12980|||http://purl.uniprot.org/uniprot/Q9BTE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||GATOR1 complex protein NPRL3|||In FFEVF3; unknown pathological significance.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220638|||http://purl.uniprot.org/annotation/VAR_077126|||http://purl.uniprot.org/annotation/VAR_077127
http://togogenome.org/gene/9606:BFSP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13515                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Head|||IF rod|||In CTRCT12.|||In CTRCT12; unknown pathological significance.|||N-acetylserine|||Phakinin|||Phosphoserine|||Polar residues|||Removed|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063851|||http://purl.uniprot.org/annotation/VAR_012163|||http://purl.uniprot.org/annotation/VAR_012164|||http://purl.uniprot.org/annotation/VAR_084817
http://togogenome.org/gene/9606:MPPED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15777                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Metallophosphoesterase MPPED2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053405|||http://purl.uniprot.org/annotation/VAR_052487|||http://purl.uniprot.org/annotation/VSP_045627
http://togogenome.org/gene/9606:TLCD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0W5|||http://purl.uniprot.org/uniprot/Q6ZRR5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||TLC|||TLC domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285583|||http://purl.uniprot.org/annotation/PRO_5002722701|||http://purl.uniprot.org/annotation/VSP_024871|||http://purl.uniprot.org/annotation/VSP_039853
http://togogenome.org/gene/9606:TPPP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||Removed|||Tubulin polymerization-promoting protein family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221138
http://togogenome.org/gene/9606:DSEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZU8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Dermatan-sulfate epimerase-like protein|||Helical|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278288|||http://purl.uniprot.org/annotation/VAR_030833|||http://purl.uniprot.org/annotation/VAR_030834|||http://purl.uniprot.org/annotation/VAR_036528|||http://purl.uniprot.org/annotation/VAR_057759
http://togogenome.org/gene/9606:TRMT44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYL2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Probable tRNA (uracil-O(2)-)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249894|||http://purl.uniprot.org/annotation/VAR_027515|||http://purl.uniprot.org/annotation/VAR_066601|||http://purl.uniprot.org/annotation/VAR_066602|||http://purl.uniprot.org/annotation/VAR_066603|||http://purl.uniprot.org/annotation/VSP_020589|||http://purl.uniprot.org/annotation/VSP_020590|||http://purl.uniprot.org/annotation/VSP_020591|||http://purl.uniprot.org/annotation/VSP_020592|||http://purl.uniprot.org/annotation/VSP_039538
http://togogenome.org/gene/9606:AMIGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SJ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amphoterin-induced protein 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014509
http://togogenome.org/gene/9606:SGCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4P8|||http://purl.uniprot.org/uniprot/A0A0S2Z4Q1|||http://purl.uniprot.org/uniprot/Q16586                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-sarcoglycan|||Cytoplasmic|||Dystroglycan-type cadherin-like|||Extracellular|||Helical|||In LGMDR3.|||In LGMDR3; associated with G-137.|||In LGMDR3; associated with P-G-A-Q-P-136 ins.|||In isoform SGCA-2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031673|||http://purl.uniprot.org/annotation/PRO_5006608268|||http://purl.uniprot.org/annotation/PRO_5014239286|||http://purl.uniprot.org/annotation/VAR_010387|||http://purl.uniprot.org/annotation/VAR_010388|||http://purl.uniprot.org/annotation/VAR_010389|||http://purl.uniprot.org/annotation/VAR_010390|||http://purl.uniprot.org/annotation/VAR_010402|||http://purl.uniprot.org/annotation/VAR_010403|||http://purl.uniprot.org/annotation/VAR_010404|||http://purl.uniprot.org/annotation/VAR_010405|||http://purl.uniprot.org/annotation/VAR_010406|||http://purl.uniprot.org/annotation/VAR_010407|||http://purl.uniprot.org/annotation/VAR_010408|||http://purl.uniprot.org/annotation/VAR_010409|||http://purl.uniprot.org/annotation/VAR_010410|||http://purl.uniprot.org/annotation/VAR_010411|||http://purl.uniprot.org/annotation/VAR_010412|||http://purl.uniprot.org/annotation/VAR_010413|||http://purl.uniprot.org/annotation/VAR_010414|||http://purl.uniprot.org/annotation/VAR_010415|||http://purl.uniprot.org/annotation/VAR_010416|||http://purl.uniprot.org/annotation/VAR_010417|||http://purl.uniprot.org/annotation/VAR_010418|||http://purl.uniprot.org/annotation/VAR_010419|||http://purl.uniprot.org/annotation/VAR_010420|||http://purl.uniprot.org/annotation/VAR_010431|||http://purl.uniprot.org/annotation/VAR_010432|||http://purl.uniprot.org/annotation/VAR_010433|||http://purl.uniprot.org/annotation/VAR_037965|||http://purl.uniprot.org/annotation/VAR_037966|||http://purl.uniprot.org/annotation/VAR_081098|||http://purl.uniprot.org/annotation/VAR_081099|||http://purl.uniprot.org/annotation/VSP_006017
http://togogenome.org/gene/9606:CCL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13236                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-C motif chemokine 4|||MIP-1-beta(3-69)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005164|||http://purl.uniprot.org/annotation/PRO_0000005165|||http://purl.uniprot.org/annotation/VAR_048702|||http://purl.uniprot.org/annotation/VAR_048703|||http://purl.uniprot.org/annotation/VAR_059211
http://togogenome.org/gene/9606:GRTP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0Y1|||http://purl.uniprot.org/uniprot/Q5TC63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Growth hormone-regulated TBC protein 1|||In isoform 2 and isoform 3.|||In isoform 2.|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288708|||http://purl.uniprot.org/annotation/VSP_025754|||http://purl.uniprot.org/annotation/VSP_025755
http://togogenome.org/gene/9606:TUBB2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEE3|||http://purl.uniprot.org/uniprot/Q9BVA1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Acidic residues|||Disordered|||Found in a patient with cerebellar ataxia intellectual disability and dysequilibrium syndrome; unknown pathological significance; no effect on protein folding; no effect on tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on cytoskeleton subcellular location.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CDCBM7.|||In CDCBM7; affects microtubules assembly.|||In CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance.|||In CDCBM7; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize.|||MREI motif|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta-2B chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262651|||http://purl.uniprot.org/annotation/VAR_063389|||http://purl.uniprot.org/annotation/VAR_063390|||http://purl.uniprot.org/annotation/VAR_063391|||http://purl.uniprot.org/annotation/VAR_063392|||http://purl.uniprot.org/annotation/VAR_063393|||http://purl.uniprot.org/annotation/VAR_063394|||http://purl.uniprot.org/annotation/VAR_078186|||http://purl.uniprot.org/annotation/VAR_078187|||http://purl.uniprot.org/annotation/VAR_078188|||http://purl.uniprot.org/annotation/VAR_078189|||http://purl.uniprot.org/annotation/VAR_078190|||http://purl.uniprot.org/annotation/VAR_078191
http://togogenome.org/gene/9606:EGFL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7N9|||http://purl.uniprot.org/uniprot/Q99944                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EMI|||Epidermal growth factor-like protein 8|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007531|||http://purl.uniprot.org/annotation/PRO_5014275539|||http://purl.uniprot.org/annotation/VAR_019792|||http://purl.uniprot.org/annotation/VAR_019793|||http://purl.uniprot.org/annotation/VAR_048983
http://togogenome.org/gene/9606:SP140L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BYP4|||http://purl.uniprot.org/uniprot/Q9H930|||http://purl.uniprot.org/uniprot/U5Y3L1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HSR|||In isoform 1.|||In isoform 2.|||In isoform 3.|||Nuclear body protein SP140-like protein|||PHD-type|||Phosphoserine|||Polar residues|||SAND                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321936|||http://purl.uniprot.org/annotation/VAR_059144|||http://purl.uniprot.org/annotation/VAR_059145|||http://purl.uniprot.org/annotation/VAR_059146|||http://purl.uniprot.org/annotation/VSP_031830|||http://purl.uniprot.org/annotation/VSP_031831|||http://purl.uniprot.org/annotation/VSP_031832|||http://purl.uniprot.org/annotation/VSP_031833|||http://purl.uniprot.org/annotation/VSP_040889
http://togogenome.org/gene/9606:CIR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X95                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Corepressor interacting with RBPJ 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RBPJ|||Interaction with RP9|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247984|||http://purl.uniprot.org/annotation/VSP_020091|||http://purl.uniprot.org/annotation/VSP_020092
http://togogenome.org/gene/9606:SH3D19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Interaction with SH3GL1|||Phosphoserine|||Polar residues|||Pro residues|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 domain-containing protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318197|||http://purl.uniprot.org/annotation/VSP_031182|||http://purl.uniprot.org/annotation/VSP_031183|||http://purl.uniprot.org/annotation/VSP_031184
http://togogenome.org/gene/9606:INSC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1MX18                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with GPSM2 and GPSM1; when associated with R-89.|||Abolishes interaction with GPSM2.|||Important for interaction with GPSM2|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||PDZ-binding|||Protein inscuteable homolog|||Strongly reduces interaction with GPSM2. Abolishes interaction with GPSM2 and GPSM1; when associated with D-97.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252405|||http://purl.uniprot.org/annotation/VAR_027852|||http://purl.uniprot.org/annotation/VAR_051073|||http://purl.uniprot.org/annotation/VSP_020946|||http://purl.uniprot.org/annotation/VSP_020947|||http://purl.uniprot.org/annotation/VSP_020948|||http://purl.uniprot.org/annotation/VSP_020949|||http://purl.uniprot.org/annotation/VSP_020950|||http://purl.uniprot.org/annotation/VSP_054159
http://togogenome.org/gene/9606:PEX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Y5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In PBD8B.|||In isoform 2.|||Interaction with PEX19|||Peroxisomal|||Peroxisomal membrane protein PEX16|||Required for peroxisomal location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058330|||http://purl.uniprot.org/annotation/VAR_034145|||http://purl.uniprot.org/annotation/VAR_051272|||http://purl.uniprot.org/annotation/VAR_061841|||http://purl.uniprot.org/annotation/VAR_069208|||http://purl.uniprot.org/annotation/VAR_069209|||http://purl.uniprot.org/annotation/VAR_069210|||http://purl.uniprot.org/annotation/VSP_036593
http://togogenome.org/gene/9606:FOXN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H901|||http://purl.uniprot.org/uniprot/Q96NZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein N4|||In isoform 2.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091870|||http://purl.uniprot.org/annotation/VAR_059300|||http://purl.uniprot.org/annotation/VSP_017227|||http://purl.uniprot.org/annotation/VSP_017228|||http://purl.uniprot.org/annotation/VSP_017229|||http://purl.uniprot.org/annotation/VSP_054325
http://togogenome.org/gene/9606:LPCAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5N7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EF-hand 1|||EF-hand 2|||EGTC motif|||HXXXXD motif|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Lysophosphatidylcholine acyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247058|||http://purl.uniprot.org/annotation/VAR_027058|||http://purl.uniprot.org/annotation/VSP_019912
http://togogenome.org/gene/9606:DUSP26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV47                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 26|||In isoform 2.|||Loss of activity.|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292219|||http://purl.uniprot.org/annotation/VSP_026406
http://togogenome.org/gene/9606:SPATA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDM6|||http://purl.uniprot.org/uniprot/B4DMC2|||http://purl.uniprot.org/uniprot/E9PFR9|||http://purl.uniprot.org/uniprot/Q96N96                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ABR (APC-binding region) domain|||C-terminal tail|||DH|||Disordered|||Found in two consanguineous families with intellectual disability; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PH|||Phosphoserine|||SH3|||Spermatogenesis-associated protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278448|||http://purl.uniprot.org/annotation/VAR_030776|||http://purl.uniprot.org/annotation/VAR_080767|||http://purl.uniprot.org/annotation/VSP_041030|||http://purl.uniprot.org/annotation/VSP_041031|||http://purl.uniprot.org/annotation/VSP_041032|||http://purl.uniprot.org/annotation/VSP_041033|||http://purl.uniprot.org/annotation/VSP_041034|||http://purl.uniprot.org/annotation/VSP_054112
http://togogenome.org/gene/9606:PPP1R14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein phosphatase 1 regulatory subunit 14B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071490
http://togogenome.org/gene/9606:PRMT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2P2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  8-fold increase in MMA production and almost complete elimination of sDMA production.|||Abolishes enzymatic activity.|||In isoform 2.|||Loss of interaction with SF3B2; Abolishes enzymatic activity.|||Protein arginine N-methyltransferase 9|||SAM-dependent MTase PRMT-type 1|||SAM-dependent MTase PRMT-type 2|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325929|||http://purl.uniprot.org/annotation/VAR_039954|||http://purl.uniprot.org/annotation/VAR_039955|||http://purl.uniprot.org/annotation/VSP_053972
http://togogenome.org/gene/9606:AMACR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHK6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-methylacyl-CoA racemase|||In AMACRD and CBAS4; inactive enzyme.|||In CBAS4; inactive enzyme.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194705|||http://purl.uniprot.org/annotation/VAR_010660|||http://purl.uniprot.org/annotation/VAR_010661|||http://purl.uniprot.org/annotation/VAR_010662|||http://purl.uniprot.org/annotation/VAR_010663|||http://purl.uniprot.org/annotation/VAR_010664|||http://purl.uniprot.org/annotation/VAR_010665|||http://purl.uniprot.org/annotation/VAR_055616|||http://purl.uniprot.org/annotation/VAR_055617|||http://purl.uniprot.org/annotation/VAR_055618|||http://purl.uniprot.org/annotation/VAR_055619|||http://purl.uniprot.org/annotation/VAR_055620|||http://purl.uniprot.org/annotation/VSP_037321|||http://purl.uniprot.org/annotation/VSP_037323|||http://purl.uniprot.org/annotation/VSP_037324|||http://purl.uniprot.org/annotation/VSP_037326|||http://purl.uniprot.org/annotation/VSP_044875
http://togogenome.org/gene/9606:EID3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI9|||http://purl.uniprot.org/uniprot/Q8N140                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  EP300-interacting inhibitor of differentiation 3|||Non-structural maintenance of chromosome element 4 C-terminal|||Nse4/EID protein Nse3/MAGE-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315905
http://togogenome.org/gene/9606:HSD11B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28845|||http://purl.uniprot.org/uniprot/X5D2L1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  11-beta-hydroxysteroid dehydrogenase 1|||Complete loss of activity.|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||Inverted topology. No effect on activity.|||Inverted topology. Reduced Vmax.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on activity.|||No effect on topology or activity.|||No effect on topology. Increased Km for corticosterone.|||No effect on topology. Reduced Vmax.|||Predominantly inverted topology. No effect on activity.|||Proton acceptor|||Reduced Vmax.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054619|||http://purl.uniprot.org/annotation/VAR_035845
http://togogenome.org/gene/9606:CCER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Coiled-coil domain-containing glutamate-rich protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288857|||http://purl.uniprot.org/annotation/VAR_032512|||http://purl.uniprot.org/annotation/VAR_059617
http://togogenome.org/gene/9606:FBXL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3WK56|||http://purl.uniprot.org/uniprot/Q8N1P0|||http://purl.uniprot.org/uniprot/Q8NEE6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box and leucine-rich repeat protein 13|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119859|||http://purl.uniprot.org/annotation/VAR_021480|||http://purl.uniprot.org/annotation/VAR_031426|||http://purl.uniprot.org/annotation/VAR_031427|||http://purl.uniprot.org/annotation/VAR_031428|||http://purl.uniprot.org/annotation/VAR_031429|||http://purl.uniprot.org/annotation/VSP_013003|||http://purl.uniprot.org/annotation/VSP_013004|||http://purl.uniprot.org/annotation/VSP_013005
http://togogenome.org/gene/9606:MYO9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0I1T6|||http://purl.uniprot.org/uniprot/Q13459|||http://purl.uniprot.org/uniprot/Q4LE74|||http://purl.uniprot.org/uniprot/Q8WVD2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Decreases interaction with RHOA. Decreases stimulation of RHOAGTPase activity.|||Decreases interaction with RHOA. Strongly decreases stimulation of RHOAGTPase activity.|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||In isoform Short.|||Interaction with RHOA|||Myosin motor|||N-acetylserine|||Neck or regulatory domain|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras-associating|||Removed|||Rho-GAP|||Strongly decreases interaction with RHOA. Strongly decreases stimulation of RHOAGTPase activity.|||Tail|||Unconventional myosin-IXb                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123469|||http://purl.uniprot.org/annotation/VSP_003361|||http://purl.uniprot.org/annotation/VSP_003362
http://togogenome.org/gene/9606:ZNF335                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW09|||http://purl.uniprot.org/uniprot/Q9H4Z2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MCPH10; hypomorphic mutation; may cause altered transcript but some full-length protein is still formed.|||In isoform 2.|||Involved in the interaction with CCAR2|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 335                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047538|||http://purl.uniprot.org/annotation/VAR_024211|||http://purl.uniprot.org/annotation/VAR_047560|||http://purl.uniprot.org/annotation/VAR_047561|||http://purl.uniprot.org/annotation/VAR_047562|||http://purl.uniprot.org/annotation/VAR_069469|||http://purl.uniprot.org/annotation/VSP_035791|||http://purl.uniprot.org/annotation/VSP_035792
http://togogenome.org/gene/9606:YARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4R1|||http://purl.uniprot.org/uniprot/P54577                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Abolished localization to the nucleus. Abolished tyrosine--tRNA ligase activity. Abolished ability to activate PARP1.|||Disordered|||Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance.|||Found in a patient with proximal-predominant motor neuropathy; probable disease-associated variant; loss of function.|||In CMTDIC.|||In CMTDIC; partial loss of activity.|||In IMNEPD2; hypomorphic variant in yeast complementation assays; decreased homodimerization; does not affect localization to the cytoplasm.|||In IMNEPD2; unknown pathological significance.|||N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Reduced tyrosine--tRNA ligase activity.|||Removed; alternate|||Slightly reduced tyrosine--tRNA ligase activity.|||TRNA-binding|||Tyrosine--tRNA ligase, cytoplasmic|||Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed|||tRNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055673|||http://purl.uniprot.org/annotation/PRO_0000423285|||http://purl.uniprot.org/annotation/VAR_026681|||http://purl.uniprot.org/annotation/VAR_026682|||http://purl.uniprot.org/annotation/VAR_026683|||http://purl.uniprot.org/annotation/VAR_026684|||http://purl.uniprot.org/annotation/VAR_073292|||http://purl.uniprot.org/annotation/VAR_086001|||http://purl.uniprot.org/annotation/VAR_086002|||http://purl.uniprot.org/annotation/VAR_086003|||http://purl.uniprot.org/annotation/VAR_086004|||http://purl.uniprot.org/annotation/VAR_087701
http://togogenome.org/gene/9606:PAICS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22234                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AIR carboxylase domain|||Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase|||In PAICSD; unknown pathological significance; no effect on protein abundance; decreased phosphoribosylaminoimidazole carboxylase activity; decreased phosphoribosylaminoimidazolesuccinocarboxamide synthase activity.|||In isoform 2.|||Linker|||Loss of phosphoribosylaminoimidazole carboxylase activity.|||N-acetylalanine|||N6-acetyllysine|||No effect on phosphoribosylaminoimidazole carboxylase activity.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||SAICAR synthetase domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075030|||http://purl.uniprot.org/annotation/VAR_051884|||http://purl.uniprot.org/annotation/VAR_085931|||http://purl.uniprot.org/annotation/VSP_041265
http://togogenome.org/gene/9606:GOLM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNK9|||http://purl.uniprot.org/uniprot/Q8NBJ4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Golgi membrane protein 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021356|||http://purl.uniprot.org/annotation/VAR_053922|||http://purl.uniprot.org/annotation/VSP_018782
http://togogenome.org/gene/9606:FAM174A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane protein FAM174A|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263650
http://togogenome.org/gene/9606:CEMIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G8|||GG-type lectin 1|||GG-type lectin 2|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Inactive cell surface hyaluronidase CEMIP2|||N-linked (GlcNAc...) asparagine|||PbH1 1|||PbH1 2|||PbH1 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289972|||http://purl.uniprot.org/annotation/VAR_032669|||http://purl.uniprot.org/annotation/VAR_032670|||http://purl.uniprot.org/annotation/VAR_032671|||http://purl.uniprot.org/annotation/VAR_032672|||http://purl.uniprot.org/annotation/VAR_032673|||http://purl.uniprot.org/annotation/VAR_032674|||http://purl.uniprot.org/annotation/VAR_032675|||http://purl.uniprot.org/annotation/VAR_062197|||http://purl.uniprot.org/annotation/VAR_062198|||http://purl.uniprot.org/annotation/VSP_041401
http://togogenome.org/gene/9606:ABCC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T3U5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 10|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253576|||http://purl.uniprot.org/annotation/VAR_028391|||http://purl.uniprot.org/annotation/VSP_021078|||http://purl.uniprot.org/annotation/VSP_021079|||http://purl.uniprot.org/annotation/VSP_021080
http://togogenome.org/gene/9606:CDY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chromo|||Disordered|||In isoform 2.|||Polar residues|||Testis-specific chromodomain protein Y 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080219|||http://purl.uniprot.org/annotation/VSP_001079
http://togogenome.org/gene/9606:OLFM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX06                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Abolishes secretion. No effect on multimer formation.|||N-linked (GlcNAc...) asparagine|||No effect on secretion. Affects multimer formation.|||Olfactomedin-4|||Olfactomedin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311398|||http://purl.uniprot.org/annotation/VAR_037246
http://togogenome.org/gene/9606:MYLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1R3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||In CMH.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||Myosin light chain kinase 2, skeletal/cardiac muscle|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086408|||http://purl.uniprot.org/annotation/VAR_014197|||http://purl.uniprot.org/annotation/VAR_014198|||http://purl.uniprot.org/annotation/VAR_040860|||http://purl.uniprot.org/annotation/VAR_040861|||http://purl.uniprot.org/annotation/VAR_040862|||http://purl.uniprot.org/annotation/VAR_040863
http://togogenome.org/gene/9606:RFTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LD8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Raftlin-2|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089338
http://togogenome.org/gene/9606:CSNK1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48730                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory|||Basic and acidic residues|||Casein kinase I isoform delta|||Centrosomal localization signal (CLS)|||Disordered|||Impaired kinase activity and abnormal subcellular localization with exclusive accumulation to the nucleus.|||In FASPS2; strongly reduces kinase activity.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192833|||http://purl.uniprot.org/annotation/VAR_029075|||http://purl.uniprot.org/annotation/VAR_036451|||http://purl.uniprot.org/annotation/VAR_042081|||http://purl.uniprot.org/annotation/VAR_069801|||http://purl.uniprot.org/annotation/VSP_010253
http://togogenome.org/gene/9606:UBE2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW00|||http://purl.uniprot.org/uniprot/P51668                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Decrease in autoubiquitination.|||Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082460
http://togogenome.org/gene/9606:ARFGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53F62|||http://purl.uniprot.org/uniprot/Q8N6T3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosylation factor GTPase-activating protein 1|||Arf-GAP|||C4-type|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074190|||http://purl.uniprot.org/annotation/VAR_015187|||http://purl.uniprot.org/annotation/VSP_000298|||http://purl.uniprot.org/annotation/VSP_000299|||http://purl.uniprot.org/annotation/VSP_021818|||http://purl.uniprot.org/annotation/VSP_055379|||http://purl.uniprot.org/annotation/VSP_055380|||http://purl.uniprot.org/annotation/VSP_055739
http://togogenome.org/gene/9606:NDUFA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0J0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Important for inducing cell death|||In MC1DN28; reduced NDUFA13 protein level resulting in complex I instability.|||In a Hurthle cell variant of papillary carcinoma sample.|||In isoform 2.|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118804|||http://purl.uniprot.org/annotation/VAR_045984|||http://purl.uniprot.org/annotation/VAR_045985|||http://purl.uniprot.org/annotation/VAR_078938|||http://purl.uniprot.org/annotation/VSP_056644
http://togogenome.org/gene/9606:LIN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y322|||http://purl.uniprot.org/uniprot/Q5TKA1|||http://purl.uniprot.org/uniprot/Q6P142                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DIRP|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein lin-9 homolog|||Removed|||Sufficient for interaction with RB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249546|||http://purl.uniprot.org/annotation/VSP_020509|||http://purl.uniprot.org/annotation/VSP_020510
http://togogenome.org/gene/9606:TMEM200B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YZ2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 200B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317154
http://togogenome.org/gene/9606:TRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20396                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Peptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro-thyrotropin-releasing hormone|||Proline amide|||Thyrotropin-releasing hormone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022509|||http://purl.uniprot.org/annotation/PRO_0000022510|||http://purl.uniprot.org/annotation/PRO_0000022511|||http://purl.uniprot.org/annotation/PRO_0000022512|||http://purl.uniprot.org/annotation/PRO_0000022513|||http://purl.uniprot.org/annotation/PRO_0000022514|||http://purl.uniprot.org/annotation/PRO_0000022515|||http://purl.uniprot.org/annotation/VAR_014787
http://togogenome.org/gene/9606:NDUFS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z433|||http://purl.uniprot.org/uniprot/O43181                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In MC1DN1.|||In MC1DN1; loss of mitochondrial respiratory complex I; altered nonsense mediated mRNA decay.|||Loss of phosphorylation.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial|||Phosphoserine; by PKA|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020038|||http://purl.uniprot.org/annotation/VAR_012037|||http://purl.uniprot.org/annotation/VAR_078943|||http://purl.uniprot.org/annotation/VAR_078944|||http://purl.uniprot.org/annotation/VAR_078945|||http://purl.uniprot.org/annotation/VAR_078946
http://togogenome.org/gene/9606:DNM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ16                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dynamin-3|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206573|||http://purl.uniprot.org/annotation/VSP_034053|||http://purl.uniprot.org/annotation/VSP_034054|||http://purl.uniprot.org/annotation/VSP_054546|||http://purl.uniprot.org/annotation/VSP_054547
http://togogenome.org/gene/9606:SERINC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NH21                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Serine incorporator 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333871|||http://purl.uniprot.org/annotation/VSP_033584|||http://purl.uniprot.org/annotation/VSP_033585
http://togogenome.org/gene/9606:SEC14L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43304                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  CRAL-TRIO|||Disordered|||GOLD|||PRELI/MSF1|||SEC14-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333865
http://togogenome.org/gene/9606:ATP8B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PG43|||http://purl.uniprot.org/uniprot/Q8TF62                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic residues|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||P-type ATPase C-terminal|||Probable phospholipid-transporting ATPase IM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046368|||http://purl.uniprot.org/annotation/VAR_046962|||http://purl.uniprot.org/annotation/VAR_046963|||http://purl.uniprot.org/annotation/VAR_046964|||http://purl.uniprot.org/annotation/VAR_046965
http://togogenome.org/gene/9606:HS3ST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14792                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Heparan sulfate glucosamine 3-O-sulfotransferase 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033451|||http://purl.uniprot.org/annotation/VAR_021515|||http://purl.uniprot.org/annotation/VAR_052529
http://togogenome.org/gene/9606:C17orf99                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX52                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Protein IL-40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272654|||http://purl.uniprot.org/annotation/VAR_067466
http://togogenome.org/gene/9606:ST8SIA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9U8|||http://purl.uniprot.org/uniprot/C6G488|||http://purl.uniprot.org/uniprot/Q4VAY9|||http://purl.uniprot.org/uniprot/Q92186                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-2,8-sialyltransferase 8B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149285|||http://purl.uniprot.org/annotation/PRO_5004245513|||http://purl.uniprot.org/annotation/PRO_5014086434|||http://purl.uniprot.org/annotation/PRO_5014298297
http://togogenome.org/gene/9606:MAGEB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||MAGE|||Melanoma-associated antigen B10|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156718|||http://purl.uniprot.org/annotation/VAR_026773|||http://purl.uniprot.org/annotation/VAR_054500
http://togogenome.org/gene/9606:AMY1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTE7|||http://purl.uniprot.org/uniprot/P0DTE8|||http://purl.uniprot.org/uniprot/P0DUB6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-amylase 1A|||Alpha-amylase 1B|||Alpha-amylase 1C|||Deamidated asparagine; partial|||Deamidated asparagine; partial; alternate|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001401|||http://purl.uniprot.org/annotation/PRO_0000450820|||http://purl.uniprot.org/annotation/PRO_0000450821
http://togogenome.org/gene/9606:LGALS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00214                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to cytoplasmic vesicles in case of infection by S.typhimurium.|||Critical for binding to sialylated and sulfated oligosaccharides|||Does not affect localization to cytoplasmic vesicles in case of infection by S.typhimurium.|||Galectin 1|||Galectin 2|||Galectin-8|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076943|||http://purl.uniprot.org/annotation/VAR_009710|||http://purl.uniprot.org/annotation/VAR_012990|||http://purl.uniprot.org/annotation/VAR_012991|||http://purl.uniprot.org/annotation/VAR_063506|||http://purl.uniprot.org/annotation/VSP_003094
http://togogenome.org/gene/9606:FPR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25089|||http://purl.uniprot.org/uniprot/Q6L5J4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-formyl peptide receptor 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069457
http://togogenome.org/gene/9606:PRR20C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86478|||http://purl.uniprot.org/uniprot/P86479|||http://purl.uniprot.org/uniprot/P86480|||http://purl.uniprot.org/uniprot/P86481|||http://purl.uniprot.org/uniprot/P86496                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 20A|||Proline-rich protein 20B|||Proline-rich protein 20C|||Proline-rich protein 20D|||Proline-rich protein 20E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336092|||http://purl.uniprot.org/annotation/PRO_0000393890|||http://purl.uniprot.org/annotation/PRO_0000393891|||http://purl.uniprot.org/annotation/PRO_0000393892|||http://purl.uniprot.org/annotation/PRO_0000393893
http://togogenome.org/gene/9606:PRAME                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78395                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Impaired formation of the CRL2(PRAME) complex.|||LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of interaction with RARA and defective in repressing RARA signaling.|||Mediates interaction with RARA|||Melanoma antigen preferentially expressed in tumors|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156973|||http://purl.uniprot.org/annotation/VAR_021258|||http://purl.uniprot.org/annotation/VAR_062137
http://togogenome.org/gene/9606:FAM53C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM53C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189546|||http://purl.uniprot.org/annotation/VAR_053089
http://togogenome.org/gene/9606:CDCA7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8X5|||http://purl.uniprot.org/uniprot/Q96GN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cell division cycle-associated 7-like protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Integrase domain-binding motif 1 (IBM1)|||Integrase domain-binding motif 2 (IBM2)|||MYC-binding|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-21, D-77 and D-79.|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-21, D-77 and D-81.|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-21, D-79 and D-81.|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-77, D-79 and D-81.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Significant loss of interaction with PSIP1; when associated with A-16. Complete loss of interaction with PSIP1; when associated with A-16, A-72 and A-73.|||Significant loss of interaction with PSIP1; when associated with A-17. Complete loss of interaction with PSIP1; when associated with A-17, A-72 and A-73.|||Significant loss of interaction with PSIP1; when associated with A-72. Complete loss of interaction with PSIP1; when associated with A-16, A-17 and A-72.|||Significant loss of interaction with PSIP1; when associated with A-73. Complete loss of interaction with PSIP1; when associated with A-16, A-17 and A-73.|||Zinc-finger                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249313|||http://purl.uniprot.org/annotation/VAR_050776|||http://purl.uniprot.org/annotation/VAR_083475|||http://purl.uniprot.org/annotation/VSP_020398|||http://purl.uniprot.org/annotation/VSP_043806|||http://purl.uniprot.org/annotation/VSP_046270
http://togogenome.org/gene/9606:TICRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2Z1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Treslin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296623|||http://purl.uniprot.org/annotation/VAR_034631|||http://purl.uniprot.org/annotation/VAR_050886|||http://purl.uniprot.org/annotation/VAR_050887|||http://purl.uniprot.org/annotation/VAR_050888|||http://purl.uniprot.org/annotation/VAR_050889|||http://purl.uniprot.org/annotation/VAR_050890|||http://purl.uniprot.org/annotation/VAR_050891|||http://purl.uniprot.org/annotation/VAR_050892|||http://purl.uniprot.org/annotation/VSP_039218
http://togogenome.org/gene/9606:RECK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9D8|||http://purl.uniprot.org/uniprot/O95980|||http://purl.uniprot.org/uniprot/Q6P9E2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  5 X Knot repeats|||Abolished interaction with WNT7A.|||GPI-anchor amidated serine|||Kazal-like|||Kazal-like 1|||Kazal-like 2|||Kazal-like 3|||Knot 1|||Knot 2|||Knot 3|||Knot 4|||Knot 5|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Reversion-inducing cysteine-rich protein with Kazal motifs                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016583|||http://purl.uniprot.org/annotation/PRO_0000016584|||http://purl.uniprot.org/annotation/PRO_5002725579|||http://purl.uniprot.org/annotation/PRO_5004278890|||http://purl.uniprot.org/annotation/VAR_034021
http://togogenome.org/gene/9606:FSIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5CZC0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibrous sheath-interacting protein 2|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331750|||http://purl.uniprot.org/annotation/VAR_042938|||http://purl.uniprot.org/annotation/VAR_075707|||http://purl.uniprot.org/annotation/VAR_075708|||http://purl.uniprot.org/annotation/VSP_039412|||http://purl.uniprot.org/annotation/VSP_039413
http://togogenome.org/gene/9606:DAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQ75|||http://purl.uniprot.org/uniprot/P51397                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Death-associated protein 1|||Disordered|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by MTOR|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079782
http://togogenome.org/gene/9606:MPIG6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0V023|||http://purl.uniprot.org/uniprot/O95866                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes the inhibitory effect against ligand-induced activation of PLCG2 by CLEC1B and GP6:FCER1G; when associated with F-237.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||In THAMY; increased protein degradation; decreased enhancement of hematopoietic lineage differentiation.|||In isoform A.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||In isoform G.|||Loss of tyrosine phosphorylation and loss of interaction with PTPN6 and PTPN11.|||Megakaryocyte and platelet inhibitory receptor G6b|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Reduced level of tyrosine phosphorylation and interaction with PTPN6 and PTPN11.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021312|||http://purl.uniprot.org/annotation/PRO_5014298131|||http://purl.uniprot.org/annotation/VAR_051004|||http://purl.uniprot.org/annotation/VAR_078570|||http://purl.uniprot.org/annotation/VSP_014172|||http://purl.uniprot.org/annotation/VSP_014173|||http://purl.uniprot.org/annotation/VSP_014174|||http://purl.uniprot.org/annotation/VSP_014175|||http://purl.uniprot.org/annotation/VSP_014176|||http://purl.uniprot.org/annotation/VSP_014177
http://togogenome.org/gene/9606:FAM167A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KS9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein FAM167A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221433|||http://purl.uniprot.org/annotation/VAR_062205|||http://purl.uniprot.org/annotation/VAR_062206
http://togogenome.org/gene/9606:SRP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYR0|||http://purl.uniprot.org/uniprot/P09132                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Signal recognition particle 19 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135197|||http://purl.uniprot.org/annotation/VAR_027800|||http://purl.uniprot.org/annotation/VSP_042540|||http://purl.uniprot.org/annotation/VSP_044524
http://togogenome.org/gene/9606:MTX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75431                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Metaxin-2|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220995|||http://purl.uniprot.org/annotation/VSP_054468
http://togogenome.org/gene/9606:CREB3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D60|||http://purl.uniprot.org/uniprot/Q70SY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic motif|||Cyclic AMP-responsive element-binding protein 3-like protein 2|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Processed cyclic AMP-responsive element-binding protein 3-like protein 2|||S1P recognition|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288067|||http://purl.uniprot.org/annotation/PRO_0000296209|||http://purl.uniprot.org/annotation/VAR_062385|||http://purl.uniprot.org/annotation/VAR_062386|||http://purl.uniprot.org/annotation/VSP_025634|||http://purl.uniprot.org/annotation/VSP_025635|||http://purl.uniprot.org/annotation/VSP_025636
http://togogenome.org/gene/9606:TUBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJT1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Tubulin delta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048484|||http://purl.uniprot.org/annotation/VAR_030000|||http://purl.uniprot.org/annotation/VSP_006680|||http://purl.uniprot.org/annotation/VSP_006681|||http://purl.uniprot.org/annotation/VSP_045196|||http://purl.uniprot.org/annotation/VSP_046949|||http://purl.uniprot.org/annotation/VSP_046950
http://togogenome.org/gene/9606:AP4M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JC87|||http://purl.uniprot.org/uniprot/O00189                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  AP-4 complex subunit mu-1|||Abolishes interaction with APP.|||MHD|||Strongly reduced interaction with APP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193787
http://togogenome.org/gene/9606:STK38L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2H1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Decreased kinase activity.|||Decreased kinase activity. Reduced binding of S100B.|||In a aLLTEL/AML1+ sample; somatic mutation.|||In isoform 2.|||Loss of autophosphorylation and kinase activity.|||N-acetylalanine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by STK24/MST3|||Protein kinase|||Proton acceptor|||Removed|||S100B binding|||Serine/threonine-protein kinase 38-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086720|||http://purl.uniprot.org/annotation/VAR_041199|||http://purl.uniprot.org/annotation/VSP_056233|||http://purl.uniprot.org/annotation/VSP_056234
http://togogenome.org/gene/9606:IL13RA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14627                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Interleukin-13 receptor subunit alpha-2|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010942|||http://purl.uniprot.org/annotation/VAR_021256
http://togogenome.org/gene/9606:DNMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L9H2|||http://purl.uniprot.org/uniprot/P26358|||http://purl.uniprot.org/uniprot/Q59FP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6 X 2 AA tandem repeats of K-G|||6; approximate|||Abolishes interaction with PCNA.|||Autoinhibitory linker|||BAH|||BAH 1|||BAH 2|||Basic and acidic residues|||CXXC-type|||Catalytic|||DMAP1-binding|||DNA (cytosine-5)-methyltransferase 1|||DNA replication foci-targeting sequence|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homodimerization|||Important for activity|||In ADCADN.|||In HSN1E; unstable protein with decreased enzymatic activity and impaired heterochromatin binding ability after the S phase.|||In isoform 2.|||In isoform 3.|||Interaction with DMAP1|||Interaction with DNMT3A|||Interaction with DNMT3B|||Interaction with PCNA|||Interaction with the PRC2/EED-EZH2 complex|||Loss of activity.|||Loss of interaction with L3MBTL3 and DCAF5. Loss of ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex.|||N6,N6-dimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-acetyllysine; by EHMT2|||N6-methyllysine; by SETD7|||No loss of interaction with PCNA.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Polar residues|||Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-667.|||Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-664 and G-670.|||Reduces activity about 10-fold; when associated with G-653; G-656; G-659; G-667 and G-670.|||Reduces activity about 10-fold; when associated with G-653; G-656; G-664; G-667 and G-670.|||Reduces activity about 10-fold; when associated with G-653; G-659; G-664; G-667 and G-670.|||Reduces activity about 10-fold; when associated with G-656; G-659; G-664; G-667 and G-670.|||Required for activity|||SAM-dependent MTase C5-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088034|||http://purl.uniprot.org/annotation/VAR_024605|||http://purl.uniprot.org/annotation/VAR_051960|||http://purl.uniprot.org/annotation/VAR_065965|||http://purl.uniprot.org/annotation/VAR_065966|||http://purl.uniprot.org/annotation/VAR_070055|||http://purl.uniprot.org/annotation/VAR_070056|||http://purl.uniprot.org/annotation/VAR_070057|||http://purl.uniprot.org/annotation/VSP_005617|||http://purl.uniprot.org/annotation/VSP_005618
http://togogenome.org/gene/9606:ZDHHC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULC8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Omega-N-methylarginine|||Palmitoyltransferase ZDHHC8|||Phosphoserine|||Polar residues|||Pro residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212877|||http://purl.uniprot.org/annotation/VSP_012572|||http://purl.uniprot.org/annotation/VSP_012573
http://togogenome.org/gene/9606:BRWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo 1|||Bromo 2|||Bromodomain and WD repeat-containing protein 1|||Disordered|||In isoform B.|||In isoform C.|||In isoform D.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050888|||http://purl.uniprot.org/annotation/VAR_026435|||http://purl.uniprot.org/annotation/VAR_026436|||http://purl.uniprot.org/annotation/VAR_026437|||http://purl.uniprot.org/annotation/VAR_057584|||http://purl.uniprot.org/annotation/VSP_018526|||http://purl.uniprot.org/annotation/VSP_018527|||http://purl.uniprot.org/annotation/VSP_018528|||http://purl.uniprot.org/annotation/VSP_044245|||http://purl.uniprot.org/annotation/VSP_044246
http://togogenome.org/gene/9606:HIGD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y241                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  HIG1|||HIG1 domain family member 1A, mitochondrial|||Helical|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215770|||http://purl.uniprot.org/annotation/VSP_041211
http://togogenome.org/gene/9606:S100A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26447                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||N-acetylalanine|||N6-acetyllysine|||Protein S100-A4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143977
http://togogenome.org/gene/9606:BLTP3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6BDS2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Bridge-like lipid transfer protein family member 3A|||Chorein N-terminal|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065723|||http://purl.uniprot.org/annotation/VAR_051474|||http://purl.uniprot.org/annotation/VAR_051475|||http://purl.uniprot.org/annotation/VAR_051476|||http://purl.uniprot.org/annotation/VAR_051477|||http://purl.uniprot.org/annotation/VAR_051478
http://togogenome.org/gene/9606:C8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07357                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Complement component C8 alpha chain|||Disordered|||EGF-like|||In allele C8A*B.|||Interchain (with C-60 in C8-gamma chain)|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||TSP type-1 1|||TSP type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023585|||http://purl.uniprot.org/annotation/PRO_0000023586|||http://purl.uniprot.org/annotation/VAR_011889|||http://purl.uniprot.org/annotation/VAR_011890|||http://purl.uniprot.org/annotation/VAR_011891|||http://purl.uniprot.org/annotation/VAR_011892|||http://purl.uniprot.org/annotation/VAR_033800|||http://purl.uniprot.org/annotation/VAR_033801
http://togogenome.org/gene/9606:RPH3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2J0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||RabBD|||Rabphilin-3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190227|||http://purl.uniprot.org/annotation/VSP_021016
http://togogenome.org/gene/9606:HBG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZU9|||http://purl.uniprot.org/uniprot/P69892                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit gamma-2|||In Albaicin.|||In Auckland.|||In Austell.|||In Bonheiden; causes severe hereditary hemolytic anemia.|||In Bron.|||In Brooklyn.|||In Calabria.|||In Caltech.|||In Carlton.|||In Catalonia.|||In Clamart.|||In Clarke.|||In Coigneres.|||In Columbus-Ga.|||In Cosenza.|||In Emirates.|||In Fuchu.|||In Granada.|||In Heather.|||In Kennestone.|||In Kingston.|||In La Grange.|||In LesVos/Waynesboro/Charlotte.|||In Lodz.|||In Macedonia-II.|||In Malaysia.|||In Malta-1.|||In Marietta.|||In Meinohama.|||In Melbourne.|||In Minoo.|||In Oakland.|||In Onoda; O(2) affinity up.|||In Ouled Rabah.|||In Poole; unstable.|||In Port-Royal.|||In Sacromonte.|||In Saskatoon.|||In Shanghai.|||In TNCY; hemoglobin Cincinnati.|||In TNCY; hemoglobin F-Brugine/Feldkirch; lowered affinity for oxygen.|||In TNCY; hemoglobin Fort Ripley.|||In TNCY; hemoglobin M-Circleville.|||In TNCY; hemoglobin Osaka; the presence of a tyrosine causes the formation of a covalent link with heme iron, so that the iron is stabilized in the ferric form; when this occurs methemoglobin is formed, oxygen can no longer bind to heme and cyanosis occurs.|||In TNCY; hemoglobin Toms River; the side chain of methionine decreases both the affinity of oxygen for binding to the mutant hemoglobin subunit via steric hindrance and the rate at which it does so; the mutant methionine is converted to aspartic acid post-translationally.|||In Tokyo.|||In Urumqi.|||In Veleta.|||N-acetylglycine; in form Hb F1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||S-nitrosocysteine|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053254|||http://purl.uniprot.org/annotation/VAR_003123|||http://purl.uniprot.org/annotation/VAR_003126|||http://purl.uniprot.org/annotation/VAR_003129|||http://purl.uniprot.org/annotation/VAR_003131|||http://purl.uniprot.org/annotation/VAR_003132|||http://purl.uniprot.org/annotation/VAR_003133|||http://purl.uniprot.org/annotation/VAR_003134|||http://purl.uniprot.org/annotation/VAR_003136|||http://purl.uniprot.org/annotation/VAR_003137|||http://purl.uniprot.org/annotation/VAR_003139|||http://purl.uniprot.org/annotation/VAR_003140|||http://purl.uniprot.org/annotation/VAR_003144|||http://purl.uniprot.org/annotation/VAR_003146|||http://purl.uniprot.org/annotation/VAR_003148|||http://purl.uniprot.org/annotation/VAR_003150|||http://purl.uniprot.org/annotation/VAR_003151|||http://purl.uniprot.org/annotation/VAR_003152|||http://purl.uniprot.org/annotation/VAR_003154|||http://purl.uniprot.org/annotation/VAR_003155|||http://purl.uniprot.org/annotation/VAR_003156|||http://purl.uniprot.org/annotation/VAR_003157|||http://purl.uniprot.org/annotation/VAR_003162|||http://purl.uniprot.org/annotation/VAR_003166|||http://purl.uniprot.org/annotation/VAR_003167|||http://purl.uniprot.org/annotation/VAR_003169|||http://purl.uniprot.org/annotation/VAR_003170|||http://purl.uniprot.org/annotation/VAR_003171|||http://purl.uniprot.org/annotation/VAR_003172|||http://purl.uniprot.org/annotation/VAR_003174|||http://purl.uniprot.org/annotation/VAR_003176|||http://purl.uniprot.org/annotation/VAR_003179|||http://purl.uniprot.org/annotation/VAR_015740|||http://purl.uniprot.org/annotation/VAR_020643|||http://purl.uniprot.org/annotation/VAR_020644|||http://purl.uniprot.org/annotation/VAR_020645|||http://purl.uniprot.org/annotation/VAR_020646|||http://purl.uniprot.org/annotation/VAR_020647|||http://purl.uniprot.org/annotation/VAR_020648|||http://purl.uniprot.org/annotation/VAR_020649|||http://purl.uniprot.org/annotation/VAR_020650|||http://purl.uniprot.org/annotation/VAR_020651|||http://purl.uniprot.org/annotation/VAR_020652|||http://purl.uniprot.org/annotation/VAR_020653|||http://purl.uniprot.org/annotation/VAR_025336|||http://purl.uniprot.org/annotation/VAR_030496|||http://purl.uniprot.org/annotation/VAR_030497|||http://purl.uniprot.org/annotation/VAR_030498|||http://purl.uniprot.org/annotation/VAR_065950|||http://purl.uniprot.org/annotation/VAR_073159
http://togogenome.org/gene/9606:LARGE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP69|||http://purl.uniprot.org/uniprot/E9PIZ2|||http://purl.uniprot.org/uniprot/Q8N3Y3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glucuronyltransferase activity|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyl- and glucuronyltransferase LARGE2|||Xylosyltransferase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226811|||http://purl.uniprot.org/annotation/PRO_5002790274|||http://purl.uniprot.org/annotation/PRO_5003244089|||http://purl.uniprot.org/annotation/VAR_025518|||http://purl.uniprot.org/annotation/VAR_031854|||http://purl.uniprot.org/annotation/VAR_031855
http://togogenome.org/gene/9606:SNX13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XC4|||http://purl.uniprot.org/uniprot/Q9Y5W8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||PX|||PXA|||RGS|||Sorting nexin-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213860|||http://purl.uniprot.org/annotation/VAR_057333|||http://purl.uniprot.org/annotation/VSP_006192
http://togogenome.org/gene/9606:PSMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK42|||http://purl.uniprot.org/uniprot/P17980                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  26S proteasome regulatory subunit 6A|||AAA+ ATPase|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084698
http://togogenome.org/gene/9606:CYP11A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3R3|||http://purl.uniprot.org/uniprot/P05108                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cholesterol side-chain cleavage enzyme, mitochondrial|||In AICSR; complete loss of activity.|||In AICSR; loss of activity.|||In AICSR; markedly reduced activity.|||In AICSR; no loss of activity.|||In AICSR; reduced activity.|||In isoform 2.|||Mitochondrion|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003585|||http://purl.uniprot.org/annotation/VAR_013944|||http://purl.uniprot.org/annotation/VAR_016949|||http://purl.uniprot.org/annotation/VAR_016950|||http://purl.uniprot.org/annotation/VAR_016951|||http://purl.uniprot.org/annotation/VAR_065241|||http://purl.uniprot.org/annotation/VAR_065242|||http://purl.uniprot.org/annotation/VAR_065243|||http://purl.uniprot.org/annotation/VAR_065244|||http://purl.uniprot.org/annotation/VSP_045695
http://togogenome.org/gene/9606:USP17L10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JJH3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421086
http://togogenome.org/gene/9606:FLCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5Y7|||http://purl.uniprot.org/uniprot/Q8NFG4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished GTPase activation (GAP) activity.|||Disordered|||Does not assemble into a stable folliculin complex (LFC), preventing localization to the lysosomal membrane upon amino acid starvation.|||Essential for GTPase activation (GAP) activity|||Essential for interaction with LDHA|||Folliculin|||Found in a colorectal cell line; impaired protein stability.|||Impaired ability to regulate autophagy; when associated with A-406 and A-537.|||Impaired ability to regulate autophagy; when associated with A-406 and A-542.|||Impaired ability to regulate autophagy; when associated with A-537 and A-542.|||In BHD.|||In BHD; does not impair protein stability, growth suppression activity or intracellular localization of folliculin.|||In PSP and BHD; impaired protein stability.|||In PSP.|||In RCC; impaired protein stability.|||In a primary clear-cell renal cell carcinoma; somatic mutation.|||In a primary colorectal cancer.|||In a primary colorectal cancer; somatic mutation.|||In a renal cell carcinoma cell line.|||In a sporadic colorectal carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by ULK1|||Polar residues|||UDENN FLCN/SMCR8-type|||cDENN FLCN/SMCR8-type|||dDENN FLCN/SMCR8-type|||uDENN FLCN/SMCR8-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223940|||http://purl.uniprot.org/annotation/VAR_025356|||http://purl.uniprot.org/annotation/VAR_025357|||http://purl.uniprot.org/annotation/VAR_025358|||http://purl.uniprot.org/annotation/VAR_025359|||http://purl.uniprot.org/annotation/VAR_025360|||http://purl.uniprot.org/annotation/VAR_025361|||http://purl.uniprot.org/annotation/VAR_066023|||http://purl.uniprot.org/annotation/VAR_066024|||http://purl.uniprot.org/annotation/VAR_066025|||http://purl.uniprot.org/annotation/VAR_066026|||http://purl.uniprot.org/annotation/VAR_066027|||http://purl.uniprot.org/annotation/VAR_066028|||http://purl.uniprot.org/annotation/VAR_066029|||http://purl.uniprot.org/annotation/VAR_083268|||http://purl.uniprot.org/annotation/VAR_083269|||http://purl.uniprot.org/annotation/VAR_083270|||http://purl.uniprot.org/annotation/VAR_083271|||http://purl.uniprot.org/annotation/VAR_083272|||http://purl.uniprot.org/annotation/VAR_083273|||http://purl.uniprot.org/annotation/VAR_083274|||http://purl.uniprot.org/annotation/VAR_083275|||http://purl.uniprot.org/annotation/VAR_083276|||http://purl.uniprot.org/annotation/VSP_017312|||http://purl.uniprot.org/annotation/VSP_017313|||http://purl.uniprot.org/annotation/VSP_017314|||http://purl.uniprot.org/annotation/VSP_017315
http://togogenome.org/gene/9606:CFL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q549N0|||http://purl.uniprot.org/uniprot/Q9Y281                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H|||Cofilin-2|||In NEM7; protein is less soluble when expressed in Escherichia coli.|||In NEM7; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||Interaction with CSRP3|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214907|||http://purl.uniprot.org/annotation/VAR_031989|||http://purl.uniprot.org/annotation/VAR_036458|||http://purl.uniprot.org/annotation/VAR_075983|||http://purl.uniprot.org/annotation/VSP_046831
http://togogenome.org/gene/9606:MVB12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EY5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with CD2AP and CIN85/SH3KBP1.|||In isoform 2.|||In isoform 3.|||Interaction with TSG101, VPS37B and VPS28|||MABP|||Mimics constitutively phosphorylated form and has the ability to interact with CD2AP and CIN85/SH3KBP1 without EGF treatment.|||Multivesicular body subunit 12A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SH3-binding|||UMA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249069|||http://purl.uniprot.org/annotation/VAR_049018|||http://purl.uniprot.org/annotation/VSP_020629|||http://purl.uniprot.org/annotation/VSP_020630
http://togogenome.org/gene/9606:ULK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||Polar residues|||Protein kinase|||Serine/threonine-protein kinase ULK4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260154|||http://purl.uniprot.org/annotation/VAR_029005|||http://purl.uniprot.org/annotation/VAR_029006|||http://purl.uniprot.org/annotation/VAR_029007|||http://purl.uniprot.org/annotation/VAR_029008|||http://purl.uniprot.org/annotation/VAR_029009|||http://purl.uniprot.org/annotation/VAR_041286|||http://purl.uniprot.org/annotation/VAR_041287|||http://purl.uniprot.org/annotation/VAR_041288|||http://purl.uniprot.org/annotation/VAR_041289|||http://purl.uniprot.org/annotation/VAR_041290|||http://purl.uniprot.org/annotation/VAR_041291|||http://purl.uniprot.org/annotation/VAR_041292|||http://purl.uniprot.org/annotation/VAR_051679|||http://purl.uniprot.org/annotation/VAR_051680|||http://purl.uniprot.org/annotation/VAR_059772
http://togogenome.org/gene/9606:DARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW5|||http://purl.uniprot.org/uniprot/P14868                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminoacyl-transfer RNA synthetases class-II family profile|||Aspartate|||Aspartate--tRNA ligase, cytoplasmic|||Binding site for the 3'-end of tRNA|||In HBSL.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111010|||http://purl.uniprot.org/annotation/VAR_027611|||http://purl.uniprot.org/annotation/VAR_070038|||http://purl.uniprot.org/annotation/VAR_070039|||http://purl.uniprot.org/annotation/VAR_070040|||http://purl.uniprot.org/annotation/VAR_070041|||http://purl.uniprot.org/annotation/VAR_070042|||http://purl.uniprot.org/annotation/VAR_070043|||http://purl.uniprot.org/annotation/VAR_070044|||http://purl.uniprot.org/annotation/VAR_070045|||http://purl.uniprot.org/annotation/VSP_056192
http://togogenome.org/gene/9606:ZNF407                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0G0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In SIMHA.|||In SIMHA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Zinc finger protein 407                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047568|||http://purl.uniprot.org/annotation/VAR_036694|||http://purl.uniprot.org/annotation/VAR_052820|||http://purl.uniprot.org/annotation/VAR_052821|||http://purl.uniprot.org/annotation/VAR_052822|||http://purl.uniprot.org/annotation/VAR_061945|||http://purl.uniprot.org/annotation/VAR_086433|||http://purl.uniprot.org/annotation/VAR_086434|||http://purl.uniprot.org/annotation/VAR_086435|||http://purl.uniprot.org/annotation/VAR_086436|||http://purl.uniprot.org/annotation/VAR_086437|||http://purl.uniprot.org/annotation/VSP_028843|||http://purl.uniprot.org/annotation/VSP_028844|||http://purl.uniprot.org/annotation/VSP_028845|||http://purl.uniprot.org/annotation/VSP_028846
http://togogenome.org/gene/9606:SNX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5X2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||PX|||Phosphoserine|||Phosphothreonine|||Sorting nexin-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213851|||http://purl.uniprot.org/annotation/VAR_036259
http://togogenome.org/gene/9606:RFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35251                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Replication factor C subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121772|||http://purl.uniprot.org/annotation/VAR_014860|||http://purl.uniprot.org/annotation/VAR_016986|||http://purl.uniprot.org/annotation/VAR_020657|||http://purl.uniprot.org/annotation/VAR_020658|||http://purl.uniprot.org/annotation/VAR_020659|||http://purl.uniprot.org/annotation/VSP_008443
http://togogenome.org/gene/9606:GRID2IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2P6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Delphilin|||Disordered|||FH2|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331624|||http://purl.uniprot.org/annotation/VAR_042909
http://togogenome.org/gene/9606:NUP155                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLT2|||http://purl.uniprot.org/uniprot/E9PF10|||http://purl.uniprot.org/uniprot/O75694                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ATFB15; fails to accumulate at various foci of the nuclear envelope and is diffusely distributed in the cytoplasm; shows significantly reduced permeability of the nuclear envelope compared to wild-type.|||In isoform 2.|||Nuclear pore complex protein Nup155|||Nucleoporin Nup133/Nup155-like C-terminal|||Nucleoporin Nup133/Nup155-like N-terminal|||O-linked (GlcNAc) serine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204844|||http://purl.uniprot.org/annotation/VAR_071762|||http://purl.uniprot.org/annotation/VSP_014437
http://togogenome.org/gene/9606:BMP8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5Y6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Bone morphogenetic protein 8A|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227896|||http://purl.uniprot.org/annotation/PRO_0000227897|||http://purl.uniprot.org/annotation/VAR_052571|||http://purl.uniprot.org/annotation/VAR_059859
http://togogenome.org/gene/9606:ZNF462                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HJ5|||http://purl.uniprot.org/uniprot/Q96JM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18; degenerate|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In WSKA.|||In isoform 2.|||In isoform 3.|||Interaction with PBX1|||N6-methyllysine|||O-linked (GlcNAc6P) serine|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 462                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047601|||http://purl.uniprot.org/annotation/VAR_058301|||http://purl.uniprot.org/annotation/VAR_058302|||http://purl.uniprot.org/annotation/VAR_058303|||http://purl.uniprot.org/annotation/VAR_058304|||http://purl.uniprot.org/annotation/VAR_058305|||http://purl.uniprot.org/annotation/VAR_083319|||http://purl.uniprot.org/annotation/VAR_083320|||http://purl.uniprot.org/annotation/VAR_083321|||http://purl.uniprot.org/annotation/VAR_083322|||http://purl.uniprot.org/annotation/VAR_083323|||http://purl.uniprot.org/annotation/VAR_083324|||http://purl.uniprot.org/annotation/VAR_083325|||http://purl.uniprot.org/annotation/VSP_037407|||http://purl.uniprot.org/annotation/VSP_037408|||http://purl.uniprot.org/annotation/VSP_037409
http://togogenome.org/gene/9606:NXT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKK6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  57% reduction in mRNA export activity and loss of nuclear rim staining.|||70% reduction in mRNA export activity.|||N-acetylalanine|||NTF2|||NTF2-related export protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194793
http://togogenome.org/gene/9606:CACNA1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUN6|||http://purl.uniprot.org/uniprot/Q01668|||http://purl.uniprot.org/uniprot/Q59GD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Binding to the beta subunit|||Cytoplasmic|||Dihydropyridine binding|||Disordered|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density and impaired channel inactivation.|||In PASNA; the mutant channel is activated at less depolarized potentials; results in increased current density.|||In SANDD; the mutant channels are unable to conduct calcium ions currents and have abnormal voltage-dependent gating.|||In a NIDDM patient.|||In isoform 3.|||In isoform 4.|||In isoform Beta-cell-type.|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Polar residues|||Probable disease-associated variant found in a patient with autism spectrum disorder; gain of function; increases channel activity; the mutant channel is activated at less depolarized potentials with an increased current density and impaired channel inactivation.|||Voltage-dependent L-type calcium channel subunit alpha-1D|||Voltage-dependent calcium channel alpha-1 subunit IQ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053933|||http://purl.uniprot.org/annotation/VAR_001497|||http://purl.uniprot.org/annotation/VAR_061103|||http://purl.uniprot.org/annotation/VAR_069170|||http://purl.uniprot.org/annotation/VAR_070868|||http://purl.uniprot.org/annotation/VAR_070869|||http://purl.uniprot.org/annotation/VAR_079531|||http://purl.uniprot.org/annotation/VAR_079532|||http://purl.uniprot.org/annotation/VAR_079533|||http://purl.uniprot.org/annotation/VSP_000913|||http://purl.uniprot.org/annotation/VSP_000914|||http://purl.uniprot.org/annotation/VSP_046743|||http://purl.uniprot.org/annotation/VSP_046744|||http://purl.uniprot.org/annotation/VSP_047921|||http://purl.uniprot.org/annotation/VSP_047922
http://togogenome.org/gene/9606:SURF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75683                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Surfeit locus protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220969|||http://purl.uniprot.org/annotation/VAR_014532|||http://purl.uniprot.org/annotation/VAR_014533|||http://purl.uniprot.org/annotation/VAR_014534|||http://purl.uniprot.org/annotation/VAR_052199|||http://purl.uniprot.org/annotation/VAR_052200
http://togogenome.org/gene/9606:CYBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT46|||http://purl.uniprot.org/uniprot/H3BNP7|||http://purl.uniprot.org/uniprot/P13498                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b-245 light chain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In CGD4.|||Loss of interaction with NOXO1.|||Phosphoserine|||Phosphothreonine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144907|||http://purl.uniprot.org/annotation/VAR_005122|||http://purl.uniprot.org/annotation/VAR_005123|||http://purl.uniprot.org/annotation/VAR_005124|||http://purl.uniprot.org/annotation/VAR_005125|||http://purl.uniprot.org/annotation/VAR_005126|||http://purl.uniprot.org/annotation/VAR_012755|||http://purl.uniprot.org/annotation/VAR_054801|||http://purl.uniprot.org/annotation/VAR_060576|||http://purl.uniprot.org/annotation/VAR_060577|||http://purl.uniprot.org/annotation/VAR_060578|||http://purl.uniprot.org/annotation/VAR_060579|||http://purl.uniprot.org/annotation/VAR_060580|||http://purl.uniprot.org/annotation/VAR_060581|||http://purl.uniprot.org/annotation/VAR_060582|||http://purl.uniprot.org/annotation/VAR_060583|||http://purl.uniprot.org/annotation/VAR_071860
http://togogenome.org/gene/9606:ARSI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FYB1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase I|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No arylsulfatase activity in the media of retinal epithelium cell.|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042216|||http://purl.uniprot.org/annotation/VSP_036022
http://togogenome.org/gene/9606:KIAA1586                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIC2|||http://purl.uniprot.org/uniprot/F5H2N6|||http://purl.uniprot.org/uniprot/Q9HCI6                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||E3 SUMO-protein ligase KIAA1586|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with SUMO2 1|||Interaction with SUMO2 2|||PSRP|||Sufficient for E3 SUMO-protein ligase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320680|||http://purl.uniprot.org/annotation/VAR_039276|||http://purl.uniprot.org/annotation/VAR_039277|||http://purl.uniprot.org/annotation/VSP_031740
http://togogenome.org/gene/9606:PGLYRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interaction with murein|||N-acetylmuramoyl-L-alanine amidase 1|||N-acetylmuramoyl-L-alanine amidase 2|||N-linked (GlcNAc...) asparagine|||Peptidoglycan recognition protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023923|||http://purl.uniprot.org/annotation/VAR_024561|||http://purl.uniprot.org/annotation/VAR_061515
http://togogenome.org/gene/9606:LRCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUJ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat and calponin homology domain-containing protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253482|||http://purl.uniprot.org/annotation/VSP_044969
http://togogenome.org/gene/9606:MFN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95140                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes the targeting to mitochondrial outer membrane.|||Cytoplasmic|||Diminishes interaction with PRKN in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PRKN in presence of PINK1; when associated with Ala-111.|||Diminishes interaction with PRKN in presence of PINK1. Abolishes phosphorylation by PINK1 and interaction with PRKN in presence of PINK1; when associated with Ala-442.|||Does not affect its ability to cluster mitochondria; when overexpressed.|||Does not affect the targeting to mitochondrial outer membrane.|||Dynamin-type G|||Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance.|||Found in a patient with hereditary motor neuropathy; unknown pathological significance.|||Found in a patient with intermediate Charcot-Marie-Tooth disease; unknown pathological significance.|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Helical; Name=1|||Helical; Name=2|||In CMT2A2A and CMT2A2B; decreased function in mitochondrial fusion; reduced homo-oligomerization; no effect on hetero-oligomerization with MFN1.|||In CMT2A2A, CMT2A2B and HMSN6A.|||In CMT2A2A.|||In CMT2A2A; also found in patients with an unclassified form of Charcot-Marie-Tooth disease; unknown pathological significance.|||In CMT2A2A; requires 2 nucleotide substitutions.|||In CMT2A2A; unknown pathological significance.|||In CMT2A2B.|||In CMT2A2B; unknown pathological significance.|||In HMSN6A and CMT2A2A.|||In HMSN6A.|||In HMSN6A; severely reduced homo-oligomerization; no effect on hetero-oligomerization with MFN1.|||In isoform 2.|||Interacts with PRKN in absence of PINK1; when associated with Glu-111.|||Interacts with PRKN in absence of PINK1; when associated with Glu-442.|||Loss of function in promoting mitochondrial fusion.|||Mitochondrial intermembrane|||Mitofusin-2|||Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions|||Phosphoserine; by PINK1|||Phosphothreonine; by PINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127675|||http://purl.uniprot.org/annotation/VAR_018607|||http://purl.uniprot.org/annotation/VAR_018608|||http://purl.uniprot.org/annotation/VAR_018609|||http://purl.uniprot.org/annotation/VAR_018610|||http://purl.uniprot.org/annotation/VAR_018611|||http://purl.uniprot.org/annotation/VAR_018612|||http://purl.uniprot.org/annotation/VAR_022464|||http://purl.uniprot.org/annotation/VAR_029876|||http://purl.uniprot.org/annotation/VAR_029877|||http://purl.uniprot.org/annotation/VAR_029878|||http://purl.uniprot.org/annotation/VAR_029879|||http://purl.uniprot.org/annotation/VAR_029880|||http://purl.uniprot.org/annotation/VAR_067088|||http://purl.uniprot.org/annotation/VAR_067089|||http://purl.uniprot.org/annotation/VAR_073291|||http://purl.uniprot.org/annotation/VAR_076895|||http://purl.uniprot.org/annotation/VAR_076896|||http://purl.uniprot.org/annotation/VAR_076897|||http://purl.uniprot.org/annotation/VAR_078437|||http://purl.uniprot.org/annotation/VAR_078438|||http://purl.uniprot.org/annotation/VAR_078439|||http://purl.uniprot.org/annotation/VAR_078440|||http://purl.uniprot.org/annotation/VAR_078441|||http://purl.uniprot.org/annotation/VAR_078442|||http://purl.uniprot.org/annotation/VAR_078443|||http://purl.uniprot.org/annotation/VAR_078444|||http://purl.uniprot.org/annotation/VAR_080339|||http://purl.uniprot.org/annotation/VAR_080340|||http://purl.uniprot.org/annotation/VAR_080341|||http://purl.uniprot.org/annotation/VAR_087590|||http://purl.uniprot.org/annotation/VSP_015159|||http://purl.uniprot.org/annotation/VSP_015160|||http://purl.uniprot.org/annotation/VSP_015161
http://togogenome.org/gene/9606:FLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RSL3|||http://purl.uniprot.org/uniprot/P17948                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity. Abolishes interaction with PLCG.|||Abolishes proteolytic cleavage by PSEN1.|||Cleavage; by PSEN1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In a bladder transitional cell carcinoma sample; somatic mutation.|||In a glioma low grade oligodendroglioma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of phosphorylation site.|||Loss of phosphorylation site. Abolishes interaction with CBL.|||Loss of phosphorylation site. Abolishes interaction with PIK3R1.|||Loss of phosphorylation site. Abolishes interaction with PLCG.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces phosphorylation at other tyrosine residues.|||Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells.|||Vascular endothelial growth factor receptor 1|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016768|||http://purl.uniprot.org/annotation/PRO_5003983118|||http://purl.uniprot.org/annotation/VAR_042045|||http://purl.uniprot.org/annotation/VAR_042046|||http://purl.uniprot.org/annotation/VAR_042047|||http://purl.uniprot.org/annotation/VAR_042048|||http://purl.uniprot.org/annotation/VAR_042049|||http://purl.uniprot.org/annotation/VAR_042050|||http://purl.uniprot.org/annotation/VAR_042051|||http://purl.uniprot.org/annotation/VAR_042052|||http://purl.uniprot.org/annotation/VAR_049719|||http://purl.uniprot.org/annotation/VSP_002955|||http://purl.uniprot.org/annotation/VSP_002956|||http://purl.uniprot.org/annotation/VSP_041927|||http://purl.uniprot.org/annotation/VSP_041928|||http://purl.uniprot.org/annotation/VSP_041929|||http://purl.uniprot.org/annotation/VSP_041930|||http://purl.uniprot.org/annotation/VSP_041983|||http://purl.uniprot.org/annotation/VSP_041984|||http://purl.uniprot.org/annotation/VSP_041985|||http://purl.uniprot.org/annotation/VSP_047759|||http://purl.uniprot.org/annotation/VSP_047760
http://togogenome.org/gene/9606:CGNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VF96                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cingulin-like protein 1|||Disordered|||Head|||In isoform 2.|||Phosphoserine|||Polar residues|||Tail|||ZIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312875|||http://purl.uniprot.org/annotation/VAR_037606|||http://purl.uniprot.org/annotation/VAR_037607|||http://purl.uniprot.org/annotation/VAR_037608|||http://purl.uniprot.org/annotation/VAR_037609|||http://purl.uniprot.org/annotation/VAR_037610|||http://purl.uniprot.org/annotation/VSP_029946
http://togogenome.org/gene/9606:TMEM45B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B21                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Transmembrane protein 45B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271199|||http://purl.uniprot.org/annotation/VAR_029866
http://togogenome.org/gene/9606:PRAMEF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SWL8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290167
http://togogenome.org/gene/9606:SLC16A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCK7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Monocarboxylate transporter 11|||Risk factor for T2D when associated with G-127, S-340 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with G-127, S-340 and T-443.|||Risk factor for T2D when associated with I-113, G-127 and S-340; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, G-127 and S-340.|||Risk factor for T2D when associated with I-113, G-127 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, G-127 and T-443.|||Risk factor for T2D when associated with I-113, S-340 and T-443; reduced pyruvate transmembrane transporter activity, loss of interaction with BSG and decreased localization to plasma membrane when associated with I-113, S-340 and T-443.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286673|||http://purl.uniprot.org/annotation/VAR_032157|||http://purl.uniprot.org/annotation/VAR_070544|||http://purl.uniprot.org/annotation/VAR_070545|||http://purl.uniprot.org/annotation/VAR_070546
http://togogenome.org/gene/9606:EFCAB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY85                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||EF-hand calcium-binding domain-containing protein 13|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281110|||http://purl.uniprot.org/annotation/VAR_031228|||http://purl.uniprot.org/annotation/VAR_031229|||http://purl.uniprot.org/annotation/VAR_035465|||http://purl.uniprot.org/annotation/VAR_061091|||http://purl.uniprot.org/annotation/VSP_047187|||http://purl.uniprot.org/annotation/VSP_047188|||http://purl.uniprot.org/annotation/VSP_047189
http://togogenome.org/gene/9606:PDE2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00408|||http://purl.uniprot.org/uniprot/Q8IW54                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased 3',5'-cyclic-AMP phosphodiesterase activity. Decreased 3',5'-cyclic-GMP phosphodiesterase activity.|||Decreased 3',5'-cyclic-AMP phosphodiesterase activity. Increased 3',5'-cyclic-GMP phosphodiesterase activity.|||Decreased 3',5'-cyclic-AMP phosphodiesterase activity. Loss of 3',5'-cyclic-GMP phosphodiesterase activity.|||Decreased 3',5'-cyclic-AMP phosphodiesterase activity. No effect on 3',5'-cyclic-GMP phosphodiesterase activity.|||Disordered|||GAF 1|||GAF 2|||In IDDPADS.|||In IDDPADS; unknown pathological significance.|||In IDDPADS; unknown pathological significance; loss of 3',5'-cyclic-AMP phosphodiesterase activity; loss of 3',5'-cyclic-GMP phosphodiesterase activity.|||In isoform 5.|||In isoform 6.|||In isoform PDE2A1 and isoform 6.|||In isoform PDE2A2 and isoform 5.|||In isoform PDE2A4.|||Loss of 3',5'-cyclic-AMP phosphodiesterase activity. Decreased 3',5'-cyclic-GMP phosphodiesterase activity.|||Loss of 3',5'-cyclic-AMP phosphodiesterase activity. Loss of 3',5'-cyclic-GMP phosphodiesterase activity.|||N-myristoyl glycine|||No effect on 3',5'-cyclic-AMP phosphodiesterase activity. Decreased 3',5'-cyclic-GMP phosphodiesterase activity.|||PDEase|||Proton donor|||Removed|||S-palmitoyl cysteine|||cGMP-dependent 3',5'-cyclic phosphodiesterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198796|||http://purl.uniprot.org/annotation/VAR_024170|||http://purl.uniprot.org/annotation/VAR_085242|||http://purl.uniprot.org/annotation/VAR_085243|||http://purl.uniprot.org/annotation/VAR_085244|||http://purl.uniprot.org/annotation/VSP_055315|||http://purl.uniprot.org/annotation/VSP_055316|||http://purl.uniprot.org/annotation/VSP_055317|||http://purl.uniprot.org/annotation/VSP_055318|||http://purl.uniprot.org/annotation/VSP_055319|||http://purl.uniprot.org/annotation/VSP_055320
http://togogenome.org/gene/9606:LYRM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JRX8|||http://purl.uniprot.org/uniprot/C9JY28|||http://purl.uniprot.org/uniprot/F5H189|||http://purl.uniprot.org/uniprot/Q9HD34                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Complex 1 LYR protein|||Disordered|||In COXPD19; can form a normal complex with NFS1 but the desulfurase enzymatic activity of this complex is severely decreased compared to control.|||LYR motif-containing protein 4|||N6-succinyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174308|||http://purl.uniprot.org/annotation/VAR_024551|||http://purl.uniprot.org/annotation/VAR_070943
http://togogenome.org/gene/9606:RNF38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0F5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||E3 ubiquitin-protein ligase RNF38|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056078|||http://purl.uniprot.org/annotation/VAR_055400|||http://purl.uniprot.org/annotation/VSP_012243|||http://purl.uniprot.org/annotation/VSP_037337|||http://purl.uniprot.org/annotation/VSP_053845|||http://purl.uniprot.org/annotation/VSP_053846|||http://purl.uniprot.org/annotation/VSP_053847
http://togogenome.org/gene/9606:RCOR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2K3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||REST corepressor 3|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226781|||http://purl.uniprot.org/annotation/VAR_025517|||http://purl.uniprot.org/annotation/VSP_017460|||http://purl.uniprot.org/annotation/VSP_017461|||http://purl.uniprot.org/annotation/VSP_017462|||http://purl.uniprot.org/annotation/VSP_041465|||http://purl.uniprot.org/annotation/VSP_041466
http://togogenome.org/gene/9606:MRAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14807|||http://purl.uniprot.org/uniprot/Q6FGP0|||http://purl.uniprot.org/uniprot/Q8WVM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In NS11.|||In NS11; constitutively active form; increased GTPase activity.|||In isoform 2.|||Ras-related protein M-Ras|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082654|||http://purl.uniprot.org/annotation/PRO_0000281304|||http://purl.uniprot.org/annotation/VAR_083112|||http://purl.uniprot.org/annotation/VAR_083113|||http://purl.uniprot.org/annotation/VAR_083114|||http://purl.uniprot.org/annotation/VSP_044792
http://togogenome.org/gene/9606:ANKRD27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NW4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 27|||Disordered|||Disrupts interaction with RAB32.|||Disrupts interaction with VAMP7.|||Disrupts interaction with VPS29; when associated with A-432.|||Disrupts interaction with VPS29; when associated with A-434.|||Disrupts interaction with VPS29; when associated with A-712.|||Disrupts interaction with VPS29; when associated with A-714.|||Impairs interaction with RAB32.|||Interaction with RAB32|||Interaction with RAB38|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with VAMP7|||Sufficient for GEF activity towards RAB21|||Sufficient for interaction with VPS29|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274556|||http://purl.uniprot.org/annotation/VAR_030317|||http://purl.uniprot.org/annotation/VAR_030318
http://togogenome.org/gene/9606:SAPCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8I8|||http://purl.uniprot.org/uniprot/Q5SSQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Suppressor APC domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244082|||http://purl.uniprot.org/annotation/VAR_056889|||http://purl.uniprot.org/annotation/VAR_056890|||http://purl.uniprot.org/annotation/VSP_040223
http://togogenome.org/gene/9606:BTN3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4B5|||http://purl.uniprot.org/uniprot/P78410                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Butyrophilin subfamily 3 member A2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014533|||http://purl.uniprot.org/annotation/PRO_5002725439|||http://purl.uniprot.org/annotation/VAR_026211|||http://purl.uniprot.org/annotation/VAR_049833|||http://purl.uniprot.org/annotation/VAR_049834|||http://purl.uniprot.org/annotation/VAR_049835|||http://purl.uniprot.org/annotation/VAR_049836|||http://purl.uniprot.org/annotation/VSP_045906|||http://purl.uniprot.org/annotation/VSP_045907
http://togogenome.org/gene/9606:SREBF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12772                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished transactivation activity.|||Cleavage; by MBTPS1|||Cleavage; by MBTPS2|||Cleavage; by caspase-3 and caspase-7|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with LMNA|||Leucine-zipper|||Loss of cleavage by S2P.|||Loss of proteolytic processing in response to low sterol.|||Lumenal|||No effect on cleavage by S2P.|||No effect on proteolytic processing in response to low sterol.|||Phosphoserine|||Polar residues|||Processed sterol regulatory element-binding protein 2|||Reduced cleavage by S2P.|||Restores cleavage by S2P; when associated with F-495 and L-496. No effect on site of cleavage by S2P.|||Sterol regulatory element-binding protein 2|||Transcriptional activation (acidic)|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127452|||http://purl.uniprot.org/annotation/PRO_0000314033|||http://purl.uniprot.org/annotation/VAR_028440|||http://purl.uniprot.org/annotation/VAR_028441|||http://purl.uniprot.org/annotation/VAR_036394|||http://purl.uniprot.org/annotation/VAR_036395|||http://purl.uniprot.org/annotation/VAR_049550|||http://purl.uniprot.org/annotation/VAR_049551|||http://purl.uniprot.org/annotation/VSP_054283|||http://purl.uniprot.org/annotation/VSP_054284|||http://purl.uniprot.org/annotation/VSP_054285
http://togogenome.org/gene/9606:BCS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R445|||http://purl.uniprot.org/uniprot/A8JZZ8|||http://purl.uniprot.org/uniprot/Q9Y276                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AAA+ ATPase|||BCS1 N-terminal|||Helical|||In BJS.|||In BJS; with mild mitochondrial complex III deficiency.|||In GRACILE.|||In MC3DN1 and BJS; with mild mitochondrial complex III deficiency; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III.|||In MC3DN1.|||In MC3DN1; abolishes interaction with LETM1.|||In MC3DN1; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III.|||Mitochondrial chaperone BCS1|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084772|||http://purl.uniprot.org/annotation/VAR_018149|||http://purl.uniprot.org/annotation/VAR_018159|||http://purl.uniprot.org/annotation/VAR_018160|||http://purl.uniprot.org/annotation/VAR_018161|||http://purl.uniprot.org/annotation/VAR_018162|||http://purl.uniprot.org/annotation/VAR_018163|||http://purl.uniprot.org/annotation/VAR_018164|||http://purl.uniprot.org/annotation/VAR_032086|||http://purl.uniprot.org/annotation/VAR_032087|||http://purl.uniprot.org/annotation/VAR_032088|||http://purl.uniprot.org/annotation/VAR_032089|||http://purl.uniprot.org/annotation/VAR_032090|||http://purl.uniprot.org/annotation/VAR_032091|||http://purl.uniprot.org/annotation/VAR_032092|||http://purl.uniprot.org/annotation/VAR_064615|||http://purl.uniprot.org/annotation/VAR_064616|||http://purl.uniprot.org/annotation/VAR_064617|||http://purl.uniprot.org/annotation/VAR_064618|||http://purl.uniprot.org/annotation/VAR_072243|||http://purl.uniprot.org/annotation/VAR_072244
http://togogenome.org/gene/9606:HEBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5THN1|||http://purl.uniprot.org/uniprot/Q9Y5Z4                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Heme-binding protein 2|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116900|||http://purl.uniprot.org/annotation/VAR_053364|||http://purl.uniprot.org/annotation/VAR_053365|||http://purl.uniprot.org/annotation/VSP_017057
http://togogenome.org/gene/9606:DEFB131B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LNP1                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 131B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000441044
http://togogenome.org/gene/9606:DPP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27487                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Dipeptidyl peptidase 4 membrane form|||Dipeptidyl peptidase 4 soluble form|||Does not inhibit dipeptidyl peptidase activity, interaction with ADA and homodimer formation.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Inhibits dipeptidyl peptidase activity.|||Inhibits strongly homodimerization, dipeptidyl peptidase activity, interaction with CARD11 and T-cell costimulation activity.|||Inhibits weakly homodimerization and dipeptidyl peptidase activity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027213|||http://purl.uniprot.org/annotation/PRO_0000027214|||http://purl.uniprot.org/annotation/VAR_084545
http://togogenome.org/gene/9606:SLC45A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A076YGN1|||http://purl.uniprot.org/uniprot/A0A076YIB8|||http://purl.uniprot.org/uniprot/D6RGY6|||http://purl.uniprot.org/uniprot/Q9UMX9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with variability of hair, eye and skin pigmentation; in Caucasians associated with dark hair, skin and eye color; strong protective effect for melanoma risk.|||Associated with variability of hair, eye and skin pigmentation; in Caucasians associated with dark hair, skin and eye color; strong protective effect for melanoma risk; decreased protein stability; no effect on subcellular location.|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In OCA4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Membrane-associated transporter protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122517|||http://purl.uniprot.org/annotation/VAR_012162|||http://purl.uniprot.org/annotation/VAR_022710|||http://purl.uniprot.org/annotation/VAR_022711|||http://purl.uniprot.org/annotation/VAR_022712|||http://purl.uniprot.org/annotation/VAR_022713|||http://purl.uniprot.org/annotation/VAR_022714|||http://purl.uniprot.org/annotation/VAR_022715|||http://purl.uniprot.org/annotation/VAR_022716|||http://purl.uniprot.org/annotation/VAR_022717|||http://purl.uniprot.org/annotation/VAR_022718|||http://purl.uniprot.org/annotation/VAR_022719|||http://purl.uniprot.org/annotation/VAR_022720|||http://purl.uniprot.org/annotation/VAR_022721|||http://purl.uniprot.org/annotation/VAR_022722|||http://purl.uniprot.org/annotation/VAR_067071|||http://purl.uniprot.org/annotation/VAR_067072|||http://purl.uniprot.org/annotation/VAR_067073|||http://purl.uniprot.org/annotation/VAR_067074|||http://purl.uniprot.org/annotation/VAR_072602|||http://purl.uniprot.org/annotation/VAR_073166|||http://purl.uniprot.org/annotation/VAR_073167|||http://purl.uniprot.org/annotation/VAR_073168|||http://purl.uniprot.org/annotation/VAR_073169|||http://purl.uniprot.org/annotation/VAR_073170|||http://purl.uniprot.org/annotation/VAR_073171|||http://purl.uniprot.org/annotation/VAR_073172|||http://purl.uniprot.org/annotation/VSP_006296|||http://purl.uniprot.org/annotation/VSP_006297|||http://purl.uniprot.org/annotation/VSP_006298|||http://purl.uniprot.org/annotation/VSP_006299|||http://purl.uniprot.org/annotation/VSP_041220|||http://purl.uniprot.org/annotation/VSP_041221
http://togogenome.org/gene/9606:HNRNPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHY1|||http://purl.uniprot.org/uniprot/P31942|||http://purl.uniprot.org/uniprot/Q53F48                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein H3|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5 and isoform 6.|||In isoform 6.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081861|||http://purl.uniprot.org/annotation/VAR_020333|||http://purl.uniprot.org/annotation/VAR_052226|||http://purl.uniprot.org/annotation/VSP_005838|||http://purl.uniprot.org/annotation/VSP_005839|||http://purl.uniprot.org/annotation/VSP_005840|||http://purl.uniprot.org/annotation/VSP_005841|||http://purl.uniprot.org/annotation/VSP_005842|||http://purl.uniprot.org/annotation/VSP_005843|||http://purl.uniprot.org/annotation/VSP_005844
http://togogenome.org/gene/9606:FOXRED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXM1|||http://purl.uniprot.org/uniprot/Q96CU9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  FAD dependent oxidoreductase|||FAD-dependent oxidoreductase domain-containing protein 1|||Helical|||In MC1DN19.|||In MC1DN19; hypomorphic variant in vitro.|||In isoform 2.|||In isoform 3.|||No effect. Able to restore complex I assembly when expressed in cells lacking FOXRED1.|||Not able to restore complex I assembly when expressed in cells lacking FOXRED1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274142|||http://purl.uniprot.org/annotation/VAR_030192|||http://purl.uniprot.org/annotation/VAR_033856|||http://purl.uniprot.org/annotation/VAR_051003|||http://purl.uniprot.org/annotation/VAR_064571|||http://purl.uniprot.org/annotation/VAR_073273|||http://purl.uniprot.org/annotation/VAR_081414|||http://purl.uniprot.org/annotation/VSP_022629|||http://purl.uniprot.org/annotation/VSP_039003
http://togogenome.org/gene/9606:FAAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00519|||http://purl.uniprot.org/uniprot/Q9UG55                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-ester intermediate|||Amidase|||Associated with susceptibility to drug abuse; the mutant enzyme is more sensitive to proteolytic degradation; displays reduced cellular expression probably due to a post-translational mechanism preceding productive folding.|||Charge relay system|||Cytoplasmic|||Fatty-acid amide hydrolase 1|||Helical|||In a breast cancer sample; somatic mutation.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105264|||http://purl.uniprot.org/annotation/VAR_013563|||http://purl.uniprot.org/annotation/VAR_035704
http://togogenome.org/gene/9606:JAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y219                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||DSL|||Disordered|||EGF-like 1|||EGF-like 10; atypical|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13|||EGF-like 14|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 2; atypical|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8|||EGF-like 9|||Extracellular|||Helical|||In LGMDR27.|||In LGMDR27; unknown pathological significance.|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein jagged-2|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007629|||http://purl.uniprot.org/annotation/VAR_028113|||http://purl.uniprot.org/annotation/VAR_048986|||http://purl.uniprot.org/annotation/VAR_086389|||http://purl.uniprot.org/annotation/VAR_086390|||http://purl.uniprot.org/annotation/VAR_086391|||http://purl.uniprot.org/annotation/VAR_086392|||http://purl.uniprot.org/annotation/VAR_086393|||http://purl.uniprot.org/annotation/VAR_086394|||http://purl.uniprot.org/annotation/VAR_086395|||http://purl.uniprot.org/annotation/VAR_086396|||http://purl.uniprot.org/annotation/VAR_086397|||http://purl.uniprot.org/annotation/VAR_086398|||http://purl.uniprot.org/annotation/VAR_086399|||http://purl.uniprot.org/annotation/VAR_086400|||http://purl.uniprot.org/annotation/VSP_001395
http://togogenome.org/gene/9606:ERCC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4Q3|||http://purl.uniprot.org/uniprot/P0DP91|||http://purl.uniprot.org/uniprot/Q03468|||http://purl.uniprot.org/uniprot/Q59FF6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Chimeric ERCC6-PGBD3 protein|||DEAH box|||DNA excision repair protein ERCC-6|||Disordered|||Essential for its interaction with RNA polymerase II, transcription-coupled nucleotide excision repair activity, association with chromatin after UV irradiation and for mediating the UV-induced translocation of ERRC8 to the nuclear matrix|||Fails to bind polyubiquitin chains.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Helicase ATP-binding|||Helicase C-terminal|||In COFS1.|||In CSB.|||In CSB; DNA-dependent ATPase-dead mutant; loss of chromatin remodeling activity; loss of its ability to inhibit non-homologous end joining-mediated repair and promote homologous recombination-mediated repair of DNA double-strand breaks; loss of its ability to suppress premature exit from G2/M checkpoint; abrogation of its UV-induced chromatin association.|||In POF11; weaker cellular response to DNA damage as indicated by delayed recruitment of mutant protein to DNA damaged sites, compared to ERCC6 isoform 1; no effect on interaction with RNA polymerase II either after UV or H(2)O(2) damage.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Interchain|||Loss of interaction with RIF1; when associated with G-1470 and G-1486.|||Loss of interaction with RIF1; when associated with G-1470 and G-1488.|||Loss of interaction with RIF1; when associated with G-1486 and G-1488.|||Loss of sumoylation and defects in transcription-coupled nucleotide excision repair.|||N-terminal domain; essential for its chromatin remodeling activity|||N6-methylated lysine; by EHMT2|||No loss of sumoylation; when associated with R-1457 and R-1487. No loss of sumoylation; when associated with R-1487.|||No loss of sumoylation; when associated with R-1457 and R-1489. No loss of sumoylation; when associated with R-1489.|||No loss of sumoylation; when associated with R-1487 and R-1489.|||Non-phosphorylatable by ATM. Loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain.|||Non-phosphorylatable by CDK2. Loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain.|||Phosphomimetic mutant. No loss of chromatin remodeling activity and its ability to promote the intramolecular interaction of the N-terminal domain with the helicase ATP-binding domain.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by CDK2|||PiggyBac transposable element-derived protein|||Polar residues|||Ubiquitin-binding domain (UBD)|||Winged-helix domain (WHD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074314|||http://purl.uniprot.org/annotation/PRO_0000441747|||http://purl.uniprot.org/annotation/VAR_001216|||http://purl.uniprot.org/annotation/VAR_001217|||http://purl.uniprot.org/annotation/VAR_001218|||http://purl.uniprot.org/annotation/VAR_001219|||http://purl.uniprot.org/annotation/VAR_001220|||http://purl.uniprot.org/annotation/VAR_001221|||http://purl.uniprot.org/annotation/VAR_001222|||http://purl.uniprot.org/annotation/VAR_001223|||http://purl.uniprot.org/annotation/VAR_001224|||http://purl.uniprot.org/annotation/VAR_001225|||http://purl.uniprot.org/annotation/VAR_016301|||http://purl.uniprot.org/annotation/VAR_016302|||http://purl.uniprot.org/annotation/VAR_016303|||http://purl.uniprot.org/annotation/VAR_016304|||http://purl.uniprot.org/annotation/VAR_016305|||http://purl.uniprot.org/annotation/VAR_016306|||http://purl.uniprot.org/annotation/VAR_016307|||http://purl.uniprot.org/annotation/VAR_016308|||http://purl.uniprot.org/annotation/VAR_016309|||http://purl.uniprot.org/annotation/VAR_016310|||http://purl.uniprot.org/annotation/VAR_016311|||http://purl.uniprot.org/annotation/VAR_036021|||http://purl.uniprot.org/annotation/VAR_036022|||http://purl.uniprot.org/annotation/VAR_036023|||http://purl.uniprot.org/annotation/VAR_036024|||http://purl.uniprot.org/annotation/VAR_036025|||http://purl.uniprot.org/annotation/VAR_037436|||http://purl.uniprot.org/annotation/VAR_037437|||http://purl.uniprot.org/annotation/VAR_054153|||http://purl.uniprot.org/annotation/VAR_063511|||http://purl.uniprot.org/annotation/VAR_063512|||http://purl.uniprot.org/annotation/VAR_063513|||http://purl.uniprot.org/annotation/VAR_063514|||http://purl.uniprot.org/annotation/VAR_063515|||http://purl.uniprot.org/annotation/VAR_079009|||http://purl.uniprot.org/annotation/VAR_079010|||http://purl.uniprot.org/annotation/VAR_079011
http://togogenome.org/gene/9606:PIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V86                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086533
http://togogenome.org/gene/9606:TMEM33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57088                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-acetylalanine|||Removed|||Transmembrane protein 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220899
http://togogenome.org/gene/9606:RPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27694                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In PFBMFT6; results in shortened telomeres and impaired hematopoiesis when expressed in iPSC-derived hematopoietic cells; increased single-stranded DNA binding; increased telomeric DNA binding; has no effect on the formation of canonical replication protein A complex.|||In PFBMFT6; unknown pathological significance; has DNA-binding properties similar to the wild-type; has no effect on the formation of canonical replication protein A complex.|||In PFBMFT6; unknown pathological significance; increased single-stranded DNA binding; increased telomeric DNA binding; has no effect on the formation of canonical replication protein A complex.|||Loss of HELB-binding; when associated with E-41.|||Loss of HELB-binding; when associated with E-43.|||Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-500.|||Loss of function in DNA replication and mismatch repair without effect on DNA-binding activity; when associated with S-503.|||N-acetylmethionine|||N6-acetyllysine; alternate|||OB|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed; alternate|||Replication protein A 70 kDa DNA-binding subunit|||Replication protein A 70 kDa DNA-binding subunit, N-terminally processed|||Significant reduction of sumoylation. Loss of sumoylation; when associated with R-577.|||Slight sumoylation decrease. Loss of sumoylation; when associated with R-449.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097260|||http://purl.uniprot.org/annotation/PRO_0000423231|||http://purl.uniprot.org/annotation/VAR_019236|||http://purl.uniprot.org/annotation/VAR_086965|||http://purl.uniprot.org/annotation/VAR_086966|||http://purl.uniprot.org/annotation/VAR_086967
http://togogenome.org/gene/9606:HS6ST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MM7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan-sulfate 6-O-sulfotransferase 2|||In MRXSPM; unknown pathological significance; reduced sulfotransferase activity; no effect on protein levels.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190805|||http://purl.uniprot.org/annotation/VAR_061828|||http://purl.uniprot.org/annotation/VAR_082055|||http://purl.uniprot.org/annotation/VSP_015846|||http://purl.uniprot.org/annotation/VSP_015847
http://togogenome.org/gene/9606:OR4C46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHA9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310456|||http://purl.uniprot.org/annotation/VAR_037045|||http://purl.uniprot.org/annotation/VAR_037046|||http://purl.uniprot.org/annotation/VAR_037047
http://togogenome.org/gene/9606:WARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23381                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Disordered|||In HMN9; decreased tryptophan-tRNA ligase activity; dominant negative effect; decreased general protein synthesis; decreased cell viability; no effect on homodimerization.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N6-succinyllysine|||Phosphoserine|||Removed|||T1-TrpRS|||T2-TrpRS|||Tryptophan--tRNA ligase, cytoplasmic|||WHEP-TRS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136738|||http://purl.uniprot.org/annotation/PRO_0000386461|||http://purl.uniprot.org/annotation/PRO_0000386462|||http://purl.uniprot.org/annotation/VAR_036466|||http://purl.uniprot.org/annotation/VAR_052406|||http://purl.uniprot.org/annotation/VAR_080407|||http://purl.uniprot.org/annotation/VAR_080408|||http://purl.uniprot.org/annotation/VSP_038221
http://togogenome.org/gene/9606:ERVW-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0EYG5|||http://purl.uniprot.org/uniprot/Q9UQF0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CX6CC|||CXXC|||Cleavage|||Complete loss of cleavage between SU and TM. Loss of fusiogenic function.|||Cytoplasmic|||Disordered|||Essential for the fusiogenic function|||Extracellular|||Fusion peptide|||Helical|||Immunosuppression|||Interchain (between SU and TM chains, or C-189 with C-405); in linked form|||Loss of fusiogenic function. No effect on cleavage between SU and TM.|||N-linked (GlcNAc...) asparagine|||Surface protein|||Syncytin-1|||Transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008485|||http://purl.uniprot.org/annotation/PRO_0000008486|||http://purl.uniprot.org/annotation/PRO_0000008487|||http://purl.uniprot.org/annotation/PRO_5003008230|||http://purl.uniprot.org/annotation/VAR_018638|||http://purl.uniprot.org/annotation/VAR_018639|||http://purl.uniprot.org/annotation/VAR_018640|||http://purl.uniprot.org/annotation/VAR_018641
http://togogenome.org/gene/9606:ZNF845                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IR2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 845                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349878
http://togogenome.org/gene/9606:CCDC57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAC2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal targeting domain|||Coiled-coil domain-containing protein 57|||Disordered|||In isoform 2.|||Microtubule binding domain|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288871|||http://purl.uniprot.org/annotation/VAR_032516|||http://purl.uniprot.org/annotation/VAR_032517|||http://purl.uniprot.org/annotation/VAR_032518|||http://purl.uniprot.org/annotation/VAR_032519|||http://purl.uniprot.org/annotation/VAR_032520|||http://purl.uniprot.org/annotation/VAR_032521|||http://purl.uniprot.org/annotation/VAR_032522|||http://purl.uniprot.org/annotation/VAR_032523|||http://purl.uniprot.org/annotation/VSP_025802|||http://purl.uniprot.org/annotation/VSP_025803
http://togogenome.org/gene/9606:SLC5A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3M2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium/glucose cotransporter 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333805|||http://purl.uniprot.org/annotation/VAR_043166|||http://purl.uniprot.org/annotation/VAR_043167|||http://purl.uniprot.org/annotation/VAR_043168|||http://purl.uniprot.org/annotation/VAR_068963|||http://purl.uniprot.org/annotation/VSP_044577|||http://purl.uniprot.org/annotation/VSP_057168
http://togogenome.org/gene/9606:OR2S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQN1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2S2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150495|||http://purl.uniprot.org/annotation/VAR_059994|||http://purl.uniprot.org/annotation/VAR_059995|||http://purl.uniprot.org/annotation/VAR_059996|||http://purl.uniprot.org/annotation/VAR_059997|||http://purl.uniprot.org/annotation/VAR_059998|||http://purl.uniprot.org/annotation/VAR_059999|||http://purl.uniprot.org/annotation/VAR_060000
http://togogenome.org/gene/9606:NTNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKF0|||http://purl.uniprot.org/uniprot/Q5IEC3|||http://purl.uniprot.org/uniprot/Q5IEC8|||http://purl.uniprot.org/uniprot/Q9Y2I2|||http://purl.uniprot.org/uniprot/X5DNW2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EGF-like|||GPI-anchor amidated serine|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||NGL discriminant loop I|||NGL discriminant loop II|||NGL discriminant loop III|||Netrin-G1|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017091|||http://purl.uniprot.org/annotation/PRO_0000017092|||http://purl.uniprot.org/annotation/PRO_5002800844|||http://purl.uniprot.org/annotation/PRO_5004954502|||http://purl.uniprot.org/annotation/VSP_010429|||http://purl.uniprot.org/annotation/VSP_010430|||http://purl.uniprot.org/annotation/VSP_012574|||http://purl.uniprot.org/annotation/VSP_012575|||http://purl.uniprot.org/annotation/VSP_012576|||http://purl.uniprot.org/annotation/VSP_012577|||http://purl.uniprot.org/annotation/VSP_012578|||http://purl.uniprot.org/annotation/VSP_012579|||http://purl.uniprot.org/annotation/VSP_012580
http://togogenome.org/gene/9606:SYNGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43759                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In a patient affected by schizophrenia.|||In isoform 1B and isoform 1C.|||In isoform 1C.|||Lumenal|||MARVEL|||N-acetylmethionine|||Polar residues|||Synaptogyrin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183990|||http://purl.uniprot.org/annotation/VAR_060489|||http://purl.uniprot.org/annotation/VAR_060490|||http://purl.uniprot.org/annotation/VSP_006331|||http://purl.uniprot.org/annotation/VSP_006332
http://togogenome.org/gene/9606:MAP1LC3B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCE7                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Site                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Propeptide|||Site                                                                                  ^@                                                                                  Cleavage; by ATG4B|||Microtubule-associated proteins 1A/1B light chain 3 beta 2|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343732|||http://purl.uniprot.org/annotation/PRO_0000343733
http://togogenome.org/gene/9606:GAMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14353|||http://purl.uniprot.org/uniprot/V9HWB2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disrupts enzymatic activity.|||Guanidinoacetate N-methyltransferase|||In CCDS2.|||In CCDS2; loss of activity.|||In CCDS2; retains no significant activity.|||In isoform 2.|||N-acetylserine|||No effect on activity.|||No effect on enzymatic activity.|||RMT2|||Removed|||S-adenosyl-L-methionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087430|||http://purl.uniprot.org/annotation/VAR_025723|||http://purl.uniprot.org/annotation/VAR_058102|||http://purl.uniprot.org/annotation/VAR_058103|||http://purl.uniprot.org/annotation/VAR_058104|||http://purl.uniprot.org/annotation/VAR_058105|||http://purl.uniprot.org/annotation/VAR_058106|||http://purl.uniprot.org/annotation/VAR_058107|||http://purl.uniprot.org/annotation/VAR_071775|||http://purl.uniprot.org/annotation/VAR_071776|||http://purl.uniprot.org/annotation/VAR_071777|||http://purl.uniprot.org/annotation/VAR_071778|||http://purl.uniprot.org/annotation/VAR_071779|||http://purl.uniprot.org/annotation/VAR_071780|||http://purl.uniprot.org/annotation/VAR_071781|||http://purl.uniprot.org/annotation/VAR_071782|||http://purl.uniprot.org/annotation/VAR_071783|||http://purl.uniprot.org/annotation/VAR_071784|||http://purl.uniprot.org/annotation/VAR_071785|||http://purl.uniprot.org/annotation/VAR_071786|||http://purl.uniprot.org/annotation/VAR_071787|||http://purl.uniprot.org/annotation/VAR_071788|||http://purl.uniprot.org/annotation/VAR_075290|||http://purl.uniprot.org/annotation/VAR_075291|||http://purl.uniprot.org/annotation/VAR_075292|||http://purl.uniprot.org/annotation/VAR_075293|||http://purl.uniprot.org/annotation/VAR_075294|||http://purl.uniprot.org/annotation/VAR_075295|||http://purl.uniprot.org/annotation/VAR_075296|||http://purl.uniprot.org/annotation/VAR_075297|||http://purl.uniprot.org/annotation/VAR_075298|||http://purl.uniprot.org/annotation/VAR_075299|||http://purl.uniprot.org/annotation/VAR_075300|||http://purl.uniprot.org/annotation/VAR_075301|||http://purl.uniprot.org/annotation/VAR_075302|||http://purl.uniprot.org/annotation/VAR_075303|||http://purl.uniprot.org/annotation/VSP_042722
http://togogenome.org/gene/9606:LCN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62502                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Epididymal-specific lipocalin-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017914
http://togogenome.org/gene/9606:CLTCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53675                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Binding site for the uncoating ATPase, involved in lattice disassembly|||CHCR 1|||CHCR 2|||CHCR 3|||CHCR 4|||CHCR 5|||CHCR 6|||CHCR 7|||Clathrin heavy chain 2|||Distal segment|||Flexible linker|||Globular terminal domain|||Heavy chain arm|||In isoform 2.|||Involved in binding clathrin light chain|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proximal segment|||Removed|||Trimerization|||WD40-like repeat 1|||WD40-like repeat 2|||WD40-like repeat 3|||WD40-like repeat 4|||WD40-like repeat 5|||WD40-like repeat 6|||WD40-like repeat 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205786|||http://purl.uniprot.org/annotation/VAR_055653|||http://purl.uniprot.org/annotation/VAR_055654|||http://purl.uniprot.org/annotation/VAR_055655|||http://purl.uniprot.org/annotation/VAR_055656|||http://purl.uniprot.org/annotation/VAR_055657|||http://purl.uniprot.org/annotation/VAR_055658|||http://purl.uniprot.org/annotation/VAR_055659|||http://purl.uniprot.org/annotation/VAR_059214|||http://purl.uniprot.org/annotation/VAR_059215|||http://purl.uniprot.org/annotation/VAR_059216|||http://purl.uniprot.org/annotation/VAR_059217|||http://purl.uniprot.org/annotation/VAR_059218|||http://purl.uniprot.org/annotation/VSP_001100
http://togogenome.org/gene/9606:NDUFAF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L188                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||In MC1DN34; unknown pathological significance.|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299480|||http://purl.uniprot.org/annotation/VAR_083800
http://togogenome.org/gene/9606:AGXT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21549                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.|||Alanine--glyoxylate aminotransferase|||Associated with hyperoxaluria.|||In HP1.|||In HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding.|||In HP1; loss of alanine--glyoxylate aminotransferase activity.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization but improved dimerization in the presence of pyridoxal phosphate; decreased protein stability.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability.|||In HP1; loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; loss of dimerization.|||In HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting.|||In HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability.|||In HP1; unknown pathological significance.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of protein stability; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; partial mitochondrial mistargeting; intraperoxisomal protein aggregation seen.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight decrease in alanine--glyoxylate aminotransferase activity; loss of dimerization; partial loss of protein stability but protein stability increases in the presence of pyridoxal phosphate; causes protein aggregation.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting.|||In HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; reduced expression levels; reduced pyridoxal phosphate binding; reduced dimerization; reduced thermostability; increased propensity to aggregation; increased susceptibility to proteolytic degradation within the N-terminal region; mitochondrial mistargeting; exposure to pyridoxine can rescue the functionality by partially preventing aggregation and degradation and by redirecting all the protein to the peroxisome.|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No loss of alanine--glyoxylate aminotransferase activity.|||Phosphothreonine|||Reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150237|||http://purl.uniprot.org/annotation/VAR_000587|||http://purl.uniprot.org/annotation/VAR_000588|||http://purl.uniprot.org/annotation/VAR_000589|||http://purl.uniprot.org/annotation/VAR_000590|||http://purl.uniprot.org/annotation/VAR_000591|||http://purl.uniprot.org/annotation/VAR_000592|||http://purl.uniprot.org/annotation/VAR_000593|||http://purl.uniprot.org/annotation/VAR_008878|||http://purl.uniprot.org/annotation/VAR_008879|||http://purl.uniprot.org/annotation/VAR_008880|||http://purl.uniprot.org/annotation/VAR_008881|||http://purl.uniprot.org/annotation/VAR_010969|||http://purl.uniprot.org/annotation/VAR_010970|||http://purl.uniprot.org/annotation/VAR_010971|||http://purl.uniprot.org/annotation/VAR_010972|||http://purl.uniprot.org/annotation/VAR_010973|||http://purl.uniprot.org/annotation/VAR_048236|||http://purl.uniprot.org/annotation/VAR_048237|||http://purl.uniprot.org/annotation/VAR_060547|||http://purl.uniprot.org/annotation/VAR_060548|||http://purl.uniprot.org/annotation/VAR_060549|||http://purl.uniprot.org/annotation/VAR_060550|||http://purl.uniprot.org/annotation/VAR_060551|||http://purl.uniprot.org/annotation/VAR_060552|||http://purl.uniprot.org/annotation/VAR_060553|||http://purl.uniprot.org/annotation/VAR_060554|||http://purl.uniprot.org/annotation/VAR_060555|||http://purl.uniprot.org/annotation/VAR_060556|||http://purl.uniprot.org/annotation/VAR_060557|||http://purl.uniprot.org/annotation/VAR_060558|||http://purl.uniprot.org/annotation/VAR_060559|||http://purl.uniprot.org/annotation/VAR_060560|||http://purl.uniprot.org/annotation/VAR_060561|||http://purl.uniprot.org/annotation/VAR_060562|||http://purl.uniprot.org/annotation/VAR_060563|||http://purl.uniprot.org/annotation/VAR_060564|||http://purl.uniprot.org/annotation/VAR_060565|||http://purl.uniprot.org/annotation/VAR_060566|||http://purl.uniprot.org/annotation/VAR_060567|||http://purl.uniprot.org/annotation/VAR_060568|||http://purl.uniprot.org/annotation/VAR_060569|||http://purl.uniprot.org/annotation/VAR_060570|||http://purl.uniprot.org/annotation/VAR_060571|||http://purl.uniprot.org/annotation/VAR_060572|||http://purl.uniprot.org/annotation/VAR_074582|||http://purl.uniprot.org/annotation/VAR_074583|||http://purl.uniprot.org/annotation/VAR_074584|||http://purl.uniprot.org/annotation/VAR_074585|||http://purl.uniprot.org/annotation/VAR_074586|||http://purl.uniprot.org/annotation/VAR_074587|||http://purl.uniprot.org/annotation/VAR_074588|||http://purl.uniprot.org/annotation/VAR_074589
http://togogenome.org/gene/9606:HPGDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5J0|||http://purl.uniprot.org/uniprot/O60760                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Hematopoietic prostaglandin D synthase|||Increases PGD2 synthesis. Loss of activation by calcium or magnesium ions.|||Loss of activation by calcium or magnesium ions.|||Reduces PGD2 synthesis by 99%. Loss of activation by calcium or magnesium ions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185934
http://togogenome.org/gene/9606:SNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AK66|||http://purl.uniprot.org/uniprot/Q8TAD8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes sumoylation.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NEDHCS.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Smad nuclear-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072009|||http://purl.uniprot.org/annotation/VAR_067542
http://togogenome.org/gene/9606:CCDC88B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC98|||http://purl.uniprot.org/uniprot/B2RTU8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 88B|||Disordered|||HOOK N-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317454|||http://purl.uniprot.org/annotation/PRO_5014298363|||http://purl.uniprot.org/annotation/VAR_038523|||http://purl.uniprot.org/annotation/VAR_038524|||http://purl.uniprot.org/annotation/VAR_038525|||http://purl.uniprot.org/annotation/VSP_030956|||http://purl.uniprot.org/annotation/VSP_030957|||http://purl.uniprot.org/annotation/VSP_030958|||http://purl.uniprot.org/annotation/VSP_030959|||http://purl.uniprot.org/annotation/VSP_030960|||http://purl.uniprot.org/annotation/VSP_030961|||http://purl.uniprot.org/annotation/VSP_030962|||http://purl.uniprot.org/annotation/VSP_030963|||http://purl.uniprot.org/annotation/VSP_030964|||http://purl.uniprot.org/annotation/VSP_030965|||http://purl.uniprot.org/annotation/VSP_035405|||http://purl.uniprot.org/annotation/VSP_035406
http://togogenome.org/gene/9606:TMEM170A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT46|||http://purl.uniprot.org/uniprot/H3BRD7|||http://purl.uniprot.org/uniprot/H3BS26|||http://purl.uniprot.org/uniprot/Q8WVE7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 170A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291759|||http://purl.uniprot.org/annotation/VSP_026229
http://togogenome.org/gene/9606:TMPRSS11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR82|||http://purl.uniprot.org/uniprot/A8KA85|||http://purl.uniprot.org/uniprot/Q6ZMR5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 1.|||May be a susceptibility factor for developing esophageal cancer especially in smoking population.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 11A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000095974|||http://purl.uniprot.org/annotation/VAR_034797|||http://purl.uniprot.org/annotation/VSP_061449
http://togogenome.org/gene/9606:IGSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6C5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||Immunoglobulin superfamily member 1|||In CHTE; impairs IGSF1 trafficking to the plasma membrane.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318512|||http://purl.uniprot.org/annotation/VAR_054960|||http://purl.uniprot.org/annotation/VAR_069268|||http://purl.uniprot.org/annotation/VAR_069269|||http://purl.uniprot.org/annotation/VAR_069270|||http://purl.uniprot.org/annotation/VAR_069271|||http://purl.uniprot.org/annotation/VAR_076256|||http://purl.uniprot.org/annotation/VSP_031195|||http://purl.uniprot.org/annotation/VSP_031196|||http://purl.uniprot.org/annotation/VSP_031197|||http://purl.uniprot.org/annotation/VSP_044554
http://togogenome.org/gene/9606:ADAM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14672                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abrogates APP cleavage. Reduces Notch signaling. Loss of proteolytic activity.|||Cleavage; by furin and PCSK7|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 10|||Disordered|||Extracellular|||Helical|||In AD18; associated with disease susceptibility; significantly attenuates alpha-secretase activity of the enzyme; shifts APP processing toward beta-secretase-mediated cleavage resulting in enhanced amyloid-beta plaque load and reactive gliosis.|||In RAK.|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Interaction with AP2A1, AP2A2 and AP2M1|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphothreonine; by FAM20C|||Pro residues|||SH3-binding|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029066|||http://purl.uniprot.org/annotation/PRO_0000029067|||http://purl.uniprot.org/annotation/VAR_066309|||http://purl.uniprot.org/annotation/VAR_070907|||http://purl.uniprot.org/annotation/VAR_070908|||http://purl.uniprot.org/annotation/VAR_070909|||http://purl.uniprot.org/annotation/VAR_070910|||http://purl.uniprot.org/annotation/VSP_056401
http://togogenome.org/gene/9606:HDAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13547|||http://purl.uniprot.org/uniprot/Q6IT96                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolished histone deacetylase and decrotonylase activities.|||Abolishes histone deacetylase and decrotonylase activities.|||Abolishes interaction with CHFR; when associated with I-297.|||Abolishes interaction with CHFR; when associated with Y-287.|||Basic and acidic residues|||Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.|||Decreases deacetylase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone deacetylase|||Histone deacetylase 1|||Impaired protein deacetylase activity without affecting the protein decrotonylase activity.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methylated lysine; by EHMT2|||No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.|||Phosphoserine|||Phosphoserine; by CK2|||Proton acceptor|||S-nitrosocysteine|||Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.|||Slightly decreases deacetylase activity.|||Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114687
http://togogenome.org/gene/9606:CABLES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7K6Y5|||http://purl.uniprot.org/uniprot/Q8TDN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CDK5 and ABL1 enzyme substrate 1|||Cyclin N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CDK3|||Interaction with TDRD7|||Phosphoserine|||Phosphoserine; by CDK2 and CDK3|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080510|||http://purl.uniprot.org/annotation/VSP_012695|||http://purl.uniprot.org/annotation/VSP_012696|||http://purl.uniprot.org/annotation/VSP_012697|||http://purl.uniprot.org/annotation/VSP_045014
http://togogenome.org/gene/9606:RGS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15539                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||RGS|||Regulator of G-protein signaling 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204188|||http://purl.uniprot.org/annotation/VSP_043094|||http://purl.uniprot.org/annotation/VSP_045086
http://togogenome.org/gene/9606:HSD17B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14756                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase type 6|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303211
http://togogenome.org/gene/9606:LAMA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24043|||http://purl.uniprot.org/uniprot/Q59H37                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Domain II and I|||In LGMDR23.|||In LGMDR23; decreased protein abundance in patient cells.|||In MDC1A.|||In MDC1A; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 14; first part|||Laminin EGF-like 14; second part|||Laminin EGF-like 15|||Laminin EGF-like 16|||Laminin EGF-like 17|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; first part|||Laminin EGF-like 5; second part|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin IV type A|||Laminin IV type A 1|||Laminin IV type A 2|||Laminin N-terminal|||Laminin subunit alpha-2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017056|||http://purl.uniprot.org/annotation/VAR_004165|||http://purl.uniprot.org/annotation/VAR_004166|||http://purl.uniprot.org/annotation/VAR_004167|||http://purl.uniprot.org/annotation/VAR_004168|||http://purl.uniprot.org/annotation/VAR_004169|||http://purl.uniprot.org/annotation/VAR_015743|||http://purl.uniprot.org/annotation/VAR_015744|||http://purl.uniprot.org/annotation/VAR_015745|||http://purl.uniprot.org/annotation/VAR_035819|||http://purl.uniprot.org/annotation/VAR_047713|||http://purl.uniprot.org/annotation/VAR_047714|||http://purl.uniprot.org/annotation/VAR_047715|||http://purl.uniprot.org/annotation/VAR_047716|||http://purl.uniprot.org/annotation/VAR_047717|||http://purl.uniprot.org/annotation/VAR_047718|||http://purl.uniprot.org/annotation/VAR_047719|||http://purl.uniprot.org/annotation/VAR_047720|||http://purl.uniprot.org/annotation/VAR_047721|||http://purl.uniprot.org/annotation/VAR_047722|||http://purl.uniprot.org/annotation/VAR_076560|||http://purl.uniprot.org/annotation/VAR_081607|||http://purl.uniprot.org/annotation/VAR_081608|||http://purl.uniprot.org/annotation/VAR_081609|||http://purl.uniprot.org/annotation/VAR_081610|||http://purl.uniprot.org/annotation/VAR_081611|||http://purl.uniprot.org/annotation/VAR_081612|||http://purl.uniprot.org/annotation/VAR_081613|||http://purl.uniprot.org/annotation/VAR_081614|||http://purl.uniprot.org/annotation/VAR_081615|||http://purl.uniprot.org/annotation/VAR_081616|||http://purl.uniprot.org/annotation/VAR_081617|||http://purl.uniprot.org/annotation/VAR_081618|||http://purl.uniprot.org/annotation/VAR_081619|||http://purl.uniprot.org/annotation/VAR_081620|||http://purl.uniprot.org/annotation/VAR_081621|||http://purl.uniprot.org/annotation/VAR_081622|||http://purl.uniprot.org/annotation/VAR_081623|||http://purl.uniprot.org/annotation/VAR_081624|||http://purl.uniprot.org/annotation/VAR_081625|||http://purl.uniprot.org/annotation/VAR_081626|||http://purl.uniprot.org/annotation/VAR_081627|||http://purl.uniprot.org/annotation/VAR_081628|||http://purl.uniprot.org/annotation/VAR_081629|||http://purl.uniprot.org/annotation/VAR_081630|||http://purl.uniprot.org/annotation/VAR_081631|||http://purl.uniprot.org/annotation/VAR_081632|||http://purl.uniprot.org/annotation/VAR_081633|||http://purl.uniprot.org/annotation/VAR_081634|||http://purl.uniprot.org/annotation/VAR_081635|||http://purl.uniprot.org/annotation/VAR_081636
http://togogenome.org/gene/9606:NVL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF43|||http://purl.uniprot.org/uniprot/O15381                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to MTREX.|||Basic and acidic residues|||Decreased nuclear localization when associated with 218-A--A-220. Complete loss of nuclear localization; when associated with 85-A-A-86 and 218-A--A-220.|||Decreased nuclear localization. Complete loss of nuclear localization; when associated with 218-A--A-220 and 230-A--A-232.|||Decreased nuclear localization; when associated with 230-A--A-232. Complete loss of nuclear localization; when associated with 85-A-A-86 and 230-A--A-232.|||Decreases 60S ribosomes synthesis. Strongly decreases 60S ribosomal subunit synthesis, enhances interaction with WDR74 and increases association of WDR74 and MTREX as well as induces partial migration of WDR74 to the nucleoplasm; when associated with Q-365.|||Decreases 60S ribosomes synthesis. Strongly decreases 60S ribosomal subunit synthesis, enhances interaction with WDR74 and increases association of WDR74 and MTREX as well as induces partial migration of WDR74 to the nucleoplasm; when associated with Q-682.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs binding to MTREX.|||Impairs the binding of MTREX.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||Interaction with RPL5|||Interaction with WDR74|||Loss of ATP-binding. No effect on interaction with TERT, MTREX and RPL5 and on telomerase activity. Significant reduction in the level of the 60S ribosomal subunit.|||Loss of ATP-binding. Significant reduction in interaction with TERT and in telomerase activity. Loss of interaction with MTREX.|||Loss of nucleolar localization and interaction with RPL5.|||N6-acetyllysine|||NVL2 nucleolin binding|||Nuclear localization signal|||Nuclear valosin-containing protein-like|||Nucleolar localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084588|||http://purl.uniprot.org/annotation/VAR_015890|||http://purl.uniprot.org/annotation/VAR_048109|||http://purl.uniprot.org/annotation/VAR_048110|||http://purl.uniprot.org/annotation/VSP_007771|||http://purl.uniprot.org/annotation/VSP_007772|||http://purl.uniprot.org/annotation/VSP_045334|||http://purl.uniprot.org/annotation/VSP_045335
http://togogenome.org/gene/9606:HOXC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00444                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-C5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200169
http://togogenome.org/gene/9606:SLC6A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7Y7|||http://purl.uniprot.org/uniprot/P31645                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Disrupts chloride ion dependence of serotonin transport. Results in larger serotonin-induced currents independent of the chloride ion gradient. Increases serotonin transport rate; when associated with C-336. Decreases expression at the cell surface.|||Extracellular|||Found in 15 autistic individuals, decreased expression at the cell surface; increased affinity for serotonin; increased serotonin transport capacity; loss of regulation through cGMP and MAP kinases pathways; hypoplasia of the enteric nervous system and decreased gastrointestinal peristaltic reflexes shown by a mouse knockin model of the mutation.|||Found in 2 autistic individuals; increased affinity for serotonin; increased serotonin transport rate.|||Found in 2 autistic individuals; increased expression at the cell surface; increased affinity for serotonin.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Impairs serotonin transport. Results in chloride ion-independent serotonin transport; when associated with A-101 or C-101.|||In isoform 2.|||Interaction with RAB4A|||Linked with susceptibility to obsessive-compulsive disorder; increased serotonin transport capacity.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKG|||Phosphotyrosine|||Polar residues|||Sodium-dependent serotonin transporter|||Sodium:neurotransmitter symporter serotonin N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214757|||http://purl.uniprot.org/annotation/VAR_014181|||http://purl.uniprot.org/annotation/VAR_014182|||http://purl.uniprot.org/annotation/VAR_026751|||http://purl.uniprot.org/annotation/VAR_029158|||http://purl.uniprot.org/annotation/VAR_036788|||http://purl.uniprot.org/annotation/VAR_036789|||http://purl.uniprot.org/annotation/VAR_036790|||http://purl.uniprot.org/annotation/VSP_046553
http://togogenome.org/gene/9606:POGLUT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXM5|||http://purl.uniprot.org/uniprot/Q6UW63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Filamin|||Glycosyl transferase CAP10|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247163|||http://purl.uniprot.org/annotation/PRO_5040469714|||http://purl.uniprot.org/annotation/VAR_027080
http://togogenome.org/gene/9606:FASLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48023|||http://purl.uniprot.org/uniprot/Q53ZZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ADAM10-processed FasL form|||Abolishes binding to TNRFSF6 and cytotoxicity.|||Cleavage; by ADAM10|||Cleavage; by SPPL2A|||Cytoplasmic|||Disordered|||Extracellular|||FasL intracellular domain|||Helical|||Helical; Signal-anchor for type II membrane protein|||In ALPS1B; significant reduction in cytotoxicity and apoptosis and inhibition of the shedding of the soluble form.|||In isoform 2.|||Lowers binding to TNFRSF6 and abolishes cytotoxicity.|||Lowers binding to TNFRSF6 and reduces cytotoxicity more than 100-fold.|||N-linked (GlcNAc...) asparagine|||Pro residues|||TNF family profile|||Tumor necrosis factor ligand superfamily member 6, membrane form|||Tumor necrosis factor ligand superfamily member 6, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034500|||http://purl.uniprot.org/annotation/PRO_0000034501|||http://purl.uniprot.org/annotation/PRO_0000416842|||http://purl.uniprot.org/annotation/PRO_0000417152|||http://purl.uniprot.org/annotation/VAR_052583|||http://purl.uniprot.org/annotation/VAR_075568|||http://purl.uniprot.org/annotation/VSP_006443|||http://purl.uniprot.org/annotation/VSP_006444
http://togogenome.org/gene/9606:IRF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02556                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  IRF tryptophan pentad repeat|||In IMD32A; impairs transcriptional activity by disrupting the interaction between IRF8 and DNA.|||In IMD32B; in resting macrophages, no effect on cytoplasmic subcellular localization; loss of nuclear subcellular localization upon IFN-gamma induction; decreased protein abundance; increased proteasome-dependent degradation; increased ubiquitination and sumoylation; loss of transcriptional repressor activity; loss of IRF1-dependent transcriptional repressor activity; loss of IRF1-dependent transcriptional activator activity; impairs transcriptional activity by disrupting the interaction between IRF8 and DNA.|||In a breast cancer sample; somatic mutation.|||In resting macrophages, no effect on cytoplasmic subcellular localization. Decreased nuclear subcellular localization upon IFN-gamma induction. Partial loss of IRF1-dependent transcriptional activator activity.|||In resting macrophages, no effect on cytoplasmic subcellular localization. Loss of nuclear subcellular localization upon IFN-gamma induction. Loss of IRF1-dependent transcriptional activator activity.|||In resting macrophages, no effect on cytoplasmic subcellular localization. No effect on nuclear subcellular localization upon IFN-gamma induction. No effect on transcriptional activator activity. No effect on IRF1-dependent transcriptional activator activity.|||Interferon regulatory factor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154564|||http://purl.uniprot.org/annotation/VAR_036490|||http://purl.uniprot.org/annotation/VAR_036491|||http://purl.uniprot.org/annotation/VAR_070084|||http://purl.uniprot.org/annotation/VAR_070085
http://togogenome.org/gene/9606:ENKUR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUX1|||http://purl.uniprot.org/uniprot/Q8TC29                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Enkurin|||IQ|||Interaction with TRPC proteins|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086975
http://togogenome.org/gene/9606:TNNI3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H18                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||In CCDD; the mutation results in decreased protein solubility; causes abnormal aggregation; markedly reduced protein expression is observed in the sarcoplasm and nuclei of patient cardiomyocytes.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a head & Neck squamous cell carcinoma sample; somatic mutation.|||In isoform 1, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of autophosphorylation activity.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TNNI3K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086757|||http://purl.uniprot.org/annotation/VAR_035639|||http://purl.uniprot.org/annotation/VAR_038821|||http://purl.uniprot.org/annotation/VAR_038822|||http://purl.uniprot.org/annotation/VAR_041223|||http://purl.uniprot.org/annotation/VAR_041224|||http://purl.uniprot.org/annotation/VAR_041225|||http://purl.uniprot.org/annotation/VAR_041226|||http://purl.uniprot.org/annotation/VAR_041227|||http://purl.uniprot.org/annotation/VAR_041228|||http://purl.uniprot.org/annotation/VAR_041229|||http://purl.uniprot.org/annotation/VAR_041230|||http://purl.uniprot.org/annotation/VAR_072650|||http://purl.uniprot.org/annotation/VSP_039403|||http://purl.uniprot.org/annotation/VSP_051882|||http://purl.uniprot.org/annotation/VSP_051883|||http://purl.uniprot.org/annotation/VSP_051884|||http://purl.uniprot.org/annotation/VSP_051885
http://togogenome.org/gene/9606:DNAJC30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSU4|||http://purl.uniprot.org/uniprot/Q96LL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 30, mitochondrial|||Helical|||In LHONAR; results in reduced turnover of N-module subunits of the respiratory chain complex I and reduced complex I activity in homozygous patient-derived cells.|||J|||Mitochondrion|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071137|||http://purl.uniprot.org/annotation/PRO_5002790097|||http://purl.uniprot.org/annotation/VAR_024433|||http://purl.uniprot.org/annotation/VAR_048915|||http://purl.uniprot.org/annotation/VAR_085951|||http://purl.uniprot.org/annotation/VAR_085952|||http://purl.uniprot.org/annotation/VAR_085953
http://togogenome.org/gene/9606:TGFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EPT6|||http://purl.uniprot.org/uniprot/F8VNR3|||http://purl.uniprot.org/uniprot/P01135                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||Extracellular|||Helical|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||N-linked (GlcNAc...) asparagine|||Protransforming growth factor alpha|||Removed in mature form|||S-palmitoyl cysteine|||Transforming growth factor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007752|||http://purl.uniprot.org/annotation/PRO_0000007753|||http://purl.uniprot.org/annotation/PRO_0000007754|||http://purl.uniprot.org/annotation/PRO_0000302744|||http://purl.uniprot.org/annotation/PRO_5003217483|||http://purl.uniprot.org/annotation/PRO_5003379224|||http://purl.uniprot.org/annotation/VAR_024271|||http://purl.uniprot.org/annotation/VSP_038369|||http://purl.uniprot.org/annotation/VSP_038370|||http://purl.uniprot.org/annotation/VSP_038371
http://togogenome.org/gene/9606:PCNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12004                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination. No effect on interaction with SHPRH.|||Alters chromatin-associated PCNA stability and its function in DNA replication and repair.|||Complete loss of interaction with UHRF2.|||Decrease in POLD3-binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In ATLD2; a hypomorphic mutation affecting DNA repair in response to UV; results in significantly decreased interaction with FEN1, LIG1 and ERCC5.|||Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-20 and R-77.|||Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-20 and R-80.|||Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-14; R-77 and R-80.|||Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-13; R-20; R-77 and R-80.|||Inhibits acetylation, recruitment to DNA damage sites, inducible ubiquitination and protein degradation, DNA replication and repair synthesis efficiencies, but homotrimer formation, nuclear recruitment to DNA damage sites, interactions with CREBBP, EP300 and POLD1 are similar as the wild-type; in association with R-14; R-20; R-77 and R-80.|||Inhibits recruitment to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-77.|||Inhibits recruitment to DNA damage sites, but nuclear localization is similar as the wild-type; in association with A-80.|||Interaction with NUDT15|||N6-acetyllysine|||No effect on POLD3-binding. Impairs binding to ALKBH2.|||No effect on POLD3-binding. No effect on ALKBH2-binding.|||Phosphotyrosine; by EGFR|||Proliferating cell nuclear antigen|||Strong decrease in POLD3-binding. Impairs binding to ALKBH2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149158|||http://purl.uniprot.org/annotation/VAR_071871
http://togogenome.org/gene/9606:ZNF286A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A525|||http://purl.uniprot.org/uniprot/B2RCD9|||http://purl.uniprot.org/uniprot/Q9HBT8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Phosphoserine|||Polar residues|||Zinc finger protein 286A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047510|||http://purl.uniprot.org/annotation/VAR_021892|||http://purl.uniprot.org/annotation/VSP_056673
http://togogenome.org/gene/9606:RPL10L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L21                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In SPGF63; reduced protein expression.|||Ribosomal protein uL16-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147106|||http://purl.uniprot.org/annotation/VAR_085860
http://togogenome.org/gene/9606:RAE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78406                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||mRNA export factor RAE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051181
http://togogenome.org/gene/9606:NOS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJJ7|||http://purl.uniprot.org/uniprot/B3VK56|||http://purl.uniprot.org/uniprot/B4DG68|||http://purl.uniprot.org/uniprot/P29475                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||FAD-binding FR-type|||Flavodoxin-like|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with DYNLL1/PIN|||Interaction with NOSIP|||Nitric oxide synthase 1|||PDZ|||Phosphoserine|||Polar residues|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170921|||http://purl.uniprot.org/annotation/VAR_018948|||http://purl.uniprot.org/annotation/VAR_018949|||http://purl.uniprot.org/annotation/VAR_018950|||http://purl.uniprot.org/annotation/VAR_018951|||http://purl.uniprot.org/annotation/VAR_018952|||http://purl.uniprot.org/annotation/VSP_003571|||http://purl.uniprot.org/annotation/VSP_003572|||http://purl.uniprot.org/annotation/VSP_003573|||http://purl.uniprot.org/annotation/VSP_003574|||http://purl.uniprot.org/annotation/VSP_044916
http://togogenome.org/gene/9606:KRTAP9-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 5 AA repeats of C-C-[RQVGE]-[SPTN]-[TASPF]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185190|||http://purl.uniprot.org/annotation/VAR_060242
http://togogenome.org/gene/9606:CNOT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDX7|||http://purl.uniprot.org/uniprot/B3KTL6|||http://purl.uniprot.org/uniprot/F8VV52|||http://purl.uniprot.org/uniprot/Q9NZN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 2|||Disordered|||In IDNADFS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||NOT2/NOT3/NOT5 C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Repressor domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198331|||http://purl.uniprot.org/annotation/VAR_048750|||http://purl.uniprot.org/annotation/VAR_083417|||http://purl.uniprot.org/annotation/VSP_009912|||http://purl.uniprot.org/annotation/VSP_009913|||http://purl.uniprot.org/annotation/VSP_009914|||http://purl.uniprot.org/annotation/VSP_009915|||http://purl.uniprot.org/annotation/VSP_009916
http://togogenome.org/gene/9606:ALAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22557                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-fold increased enzyme activity with a lower specificity for glycine and higher for succinyl-CoA.|||5-aminolevulinate synthase, erythroid-specific, mitochondrial|||In SIDBA1.|||In SIDBA1; 12% to 25% activity of wild-type.|||In SIDBA1; 15% to 35% activity of wild-type.|||In SIDBA1; associated in cis with L-520 in a patient.|||In SIDBA1; does not affect activity.|||In SIDBA1; likely benign variant; associated in cis with H-560 in a patient.|||In SIDBA1; significantly increased thermosensitivity.|||In SIDBA1; significantly reduced activity.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||Rare variant found in a congenital erythropoietic porphyria patient that also carries UROS mutations R-73 and Q-248; increased enzyme activity.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001223|||http://purl.uniprot.org/annotation/VAR_000562|||http://purl.uniprot.org/annotation/VAR_000563|||http://purl.uniprot.org/annotation/VAR_000564|||http://purl.uniprot.org/annotation/VAR_012334|||http://purl.uniprot.org/annotation/VAR_012335|||http://purl.uniprot.org/annotation/VAR_012336|||http://purl.uniprot.org/annotation/VAR_012337|||http://purl.uniprot.org/annotation/VAR_018604|||http://purl.uniprot.org/annotation/VAR_018605|||http://purl.uniprot.org/annotation/VAR_066232|||http://purl.uniprot.org/annotation/VAR_066233|||http://purl.uniprot.org/annotation/VAR_066234|||http://purl.uniprot.org/annotation/VAR_066235|||http://purl.uniprot.org/annotation/VAR_066236|||http://purl.uniprot.org/annotation/VAR_066237|||http://purl.uniprot.org/annotation/VAR_066238|||http://purl.uniprot.org/annotation/VAR_066239|||http://purl.uniprot.org/annotation/VAR_066240|||http://purl.uniprot.org/annotation/VAR_066241|||http://purl.uniprot.org/annotation/VAR_066242|||http://purl.uniprot.org/annotation/VAR_066243|||http://purl.uniprot.org/annotation/VAR_066244|||http://purl.uniprot.org/annotation/VAR_072328|||http://purl.uniprot.org/annotation/VAR_072329|||http://purl.uniprot.org/annotation/VAR_072330|||http://purl.uniprot.org/annotation/VAR_072331|||http://purl.uniprot.org/annotation/VSP_042851|||http://purl.uniprot.org/annotation/VSP_042852|||http://purl.uniprot.org/annotation/VSP_042853|||http://purl.uniprot.org/annotation/VSP_047330
http://togogenome.org/gene/9606:USP9Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00507                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform Short.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Probable ubiquitin carboxyl-terminal hydrolase FAF-Y|||Proton acceptor|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080690|||http://purl.uniprot.org/annotation/VAR_016194|||http://purl.uniprot.org/annotation/VAR_029328|||http://purl.uniprot.org/annotation/VAR_055350|||http://purl.uniprot.org/annotation/VAR_055351|||http://purl.uniprot.org/annotation/VAR_055352|||http://purl.uniprot.org/annotation/VSP_005272
http://togogenome.org/gene/9606:PLEKHH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVE3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||In isoform 2.|||In isoform 3.|||MyTH4|||PH 1|||PH 2|||Pleckstrin homology domain-containing family H member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307121|||http://purl.uniprot.org/annotation/VAR_035344|||http://purl.uniprot.org/annotation/VAR_035345|||http://purl.uniprot.org/annotation/VAR_035346|||http://purl.uniprot.org/annotation/VAR_055542|||http://purl.uniprot.org/annotation/VSP_028573|||http://purl.uniprot.org/annotation/VSP_028574|||http://purl.uniprot.org/annotation/VSP_028575
http://togogenome.org/gene/9606:MTMR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y217                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GRAM|||In isoform 2.|||Interaction with RAB1B|||Myotubularin phosphatase|||Myotubularin-related protein 6|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094939|||http://purl.uniprot.org/annotation/VAR_024583|||http://purl.uniprot.org/annotation/VAR_057143|||http://purl.uniprot.org/annotation/VSP_036614|||http://purl.uniprot.org/annotation/VSP_036615
http://togogenome.org/gene/9606:TMEM221                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGB7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 221                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332134
http://togogenome.org/gene/9606:RTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZR62                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Retrotransposon Gag-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257494|||http://purl.uniprot.org/annotation/VAR_028917|||http://purl.uniprot.org/annotation/VAR_053756
http://togogenome.org/gene/9606:FEZF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG3|||http://purl.uniprot.org/uniprot/Q8TBJ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Engrailed homology 1 repressor|||Fez family zinc finger protein 2|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295119|||http://purl.uniprot.org/annotation/VAR_033213|||http://purl.uniprot.org/annotation/VAR_033214|||http://purl.uniprot.org/annotation/VAR_065740|||http://purl.uniprot.org/annotation/VSP_026734|||http://purl.uniprot.org/annotation/VSP_026735
http://togogenome.org/gene/9606:OR13C9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150736|||http://purl.uniprot.org/annotation/VAR_024136|||http://purl.uniprot.org/annotation/VAR_034308|||http://purl.uniprot.org/annotation/VAR_053301
http://togogenome.org/gene/9606:POFUT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G5|||http://purl.uniprot.org/uniprot/S6FW71                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Essential for catalytic activity|||GDP-fucose protein O-fucosyltransferase 2|||In isoform A.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||No enhanced secretion of ADASMTS13; when associated with A-396.|||Proton acceptor|||Reduces enzyme activity.|||Reduces enzyme activity. No enhanced secretion of ADASMTS13; when associated with A-396.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012154|||http://purl.uniprot.org/annotation/PRO_5014594117|||http://purl.uniprot.org/annotation/VSP_003832|||http://purl.uniprot.org/annotation/VSP_003833|||http://purl.uniprot.org/annotation/VSP_003834
http://togogenome.org/gene/9606:PMVK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15126|||http://purl.uniprot.org/uniprot/Q6FGV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost no change in KM and Vmax for MgATP and R-MVP.|||Approximately 10-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in KM for MgATP and 50-fold increase in KM for R-MVP.|||Approximately 100000-fold decrease in Vmax for MgATP.|||Approximately 1400-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in KM for MgATP and R-MVP.|||Approximately 15-fold decrease in Vmax for MgATP and R-MVP. Approximately 50-fold increase in KM for MgATP and approximately 7-fold in KM for R-MVP.|||Approximately 20000-fold decrease in Vmax for MgATP.|||Approximately 3-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in KM for MgATP and no change in KM for R-MVP.|||Approximately 3000-fold decrease in Vmax for MgATP and R-MVP. No change in KM for MgATP and approximately 3-fold increase in KM for R-MVP.|||Approximately 4-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in KM for MgATP and R-MVP.|||Approximately 500-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in KM for MgATP and R-MVP.|||Approximately 65-fold decrease in Vmax for MgATP and R-MVP. Approximately 8-fold increase in KM for MgATP and 60-fold increase in KM for R-MVP.|||Approximately 7-fold decrease in Vmax for MgATP and R-MVP. Approximately 10-fold increase in KM for MgATP and 5-fold increase in KM for R-MVP.|||Approximately 8-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in KM for MgATP and R-MVP.|||Approximately 85-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in KM for MgATP and R-MVP.|||Approximately 9-fold decrease in Vmax for MgATP and R-MVP. Approximately 10-fold increase in KM for MgATP and R-MVP.|||In POROK1; results in reduced expression and solubility; disturbs subcellular localization with punctate rather than diffuse cytoplasmic distribution.|||In POROK1; unknown pathological significance.|||Phosphomevalonate kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058472|||http://purl.uniprot.org/annotation/VAR_051283|||http://purl.uniprot.org/annotation/VAR_075051|||http://purl.uniprot.org/annotation/VAR_080138
http://togogenome.org/gene/9606:UGT2B7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PBP8|||http://purl.uniprot.org/uniprot/P16662                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished androsterone glucuronosyltransferase activity; no change in hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.|||Abolished androsterone glucuronosyltransferase activity; reduced hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.|||Abolished androsterone, hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.|||Helical|||In allele UGT2B7*1.|||N-linked (GlcNAc...) asparagine|||Reduced androsterone and tetrachlorocatechol glucuronosyltransferase activities; abolished hyodeoxycholic acid glucuronosyltransferase activity.|||Reduced androsterone, hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.|||UDP-glucuronosyltransferase 2B7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036031|||http://purl.uniprot.org/annotation/PRO_5003245095|||http://purl.uniprot.org/annotation/VAR_012342|||http://purl.uniprot.org/annotation/VAR_057327|||http://purl.uniprot.org/annotation/VAR_057328
http://togogenome.org/gene/9606:SLC2A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X018|||http://purl.uniprot.org/uniprot/B7Z6F0|||http://purl.uniprot.org/uniprot/Q6PJ99|||http://purl.uniprot.org/uniprot/Q9BYW1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050380|||http://purl.uniprot.org/annotation/VAR_046704|||http://purl.uniprot.org/annotation/VAR_046705|||http://purl.uniprot.org/annotation/VAR_046706|||http://purl.uniprot.org/annotation/VAR_061881|||http://purl.uniprot.org/annotation/VAR_061882|||http://purl.uniprot.org/annotation/VSP_006293|||http://purl.uniprot.org/annotation/VSP_006294|||http://purl.uniprot.org/annotation/VSP_006295|||http://purl.uniprot.org/annotation/VSP_045650
http://togogenome.org/gene/9606:ERICH6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0A0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glutamate-rich protein 6B|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326050|||http://purl.uniprot.org/annotation/VAR_039969|||http://purl.uniprot.org/annotation/VAR_039970|||http://purl.uniprot.org/annotation/VAR_039971|||http://purl.uniprot.org/annotation/VAR_039972|||http://purl.uniprot.org/annotation/VAR_039973|||http://purl.uniprot.org/annotation/VAR_039974|||http://purl.uniprot.org/annotation/VAR_039975|||http://purl.uniprot.org/annotation/VAR_039976|||http://purl.uniprot.org/annotation/VAR_039977|||http://purl.uniprot.org/annotation/VAR_039978|||http://purl.uniprot.org/annotation/VSP_032523
http://togogenome.org/gene/9606:GJA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IBU3|||http://purl.uniprot.org/uniprot/P17302                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with hidrotic ectodermal dysplasia, abortive features of oculodentodigital dysplasia and extensive hyperkeratosis of the skin; unknown pathological significance; the patient also carries GJB2 variant H-127.|||Gap junction alpha-1 protein|||Gap junction protein cysteine-rich|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||In CMDR.|||In EKVP3; loss of localization to the plasma membrane, retention in the Golgi apparatus.|||In HLHS1; unknown pathological significance; associated with Q-362; abolishes phosphorylation by PKA and PKC.|||In HLHS1; unknown pathological significance; associated with Q-376; abolishes phosphorylation by PKA and PKC.|||In HSS; overlapping features with oculodentodigital dysplasia.|||In ODDD.|||In ODDD; atypical form of ODDD characterized by the predominance of the ocular involvement and by the absence of hand and/or foot syndactyly and absence of any neurologic signs.|||In ODDD; de novo mutation found in a sporadic case.|||In PPKCA1; can form functional gap junctions; results in enhanced hemichannel activity that causes increased cell death.|||In SDTY3.|||In congenital heart malformations.|||In heart malformations.|||In heart malformations; shows abnormalities in the regulation of cell-cell communication as compared with cells expressing normal GJA1.|||Interaction with NOV|||Interaction with UBQLN4|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by PKC/PRKCG and PKC/PRKCD|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057801|||http://purl.uniprot.org/annotation/VAR_014095|||http://purl.uniprot.org/annotation/VAR_014096|||http://purl.uniprot.org/annotation/VAR_014100|||http://purl.uniprot.org/annotation/VAR_014101|||http://purl.uniprot.org/annotation/VAR_014102|||http://purl.uniprot.org/annotation/VAR_015747|||http://purl.uniprot.org/annotation/VAR_015748|||http://purl.uniprot.org/annotation/VAR_015749|||http://purl.uniprot.org/annotation/VAR_015750|||http://purl.uniprot.org/annotation/VAR_015751|||http://purl.uniprot.org/annotation/VAR_015752|||http://purl.uniprot.org/annotation/VAR_015753|||http://purl.uniprot.org/annotation/VAR_015754|||http://purl.uniprot.org/annotation/VAR_015755|||http://purl.uniprot.org/annotation/VAR_015756|||http://purl.uniprot.org/annotation/VAR_015757|||http://purl.uniprot.org/annotation/VAR_015758|||http://purl.uniprot.org/annotation/VAR_015759|||http://purl.uniprot.org/annotation/VAR_015760|||http://purl.uniprot.org/annotation/VAR_015761|||http://purl.uniprot.org/annotation/VAR_015762|||http://purl.uniprot.org/annotation/VAR_015763|||http://purl.uniprot.org/annotation/VAR_015764|||http://purl.uniprot.org/annotation/VAR_032924|||http://purl.uniprot.org/annotation/VAR_032925|||http://purl.uniprot.org/annotation/VAR_038356|||http://purl.uniprot.org/annotation/VAR_038357|||http://purl.uniprot.org/annotation/VAR_038358|||http://purl.uniprot.org/annotation/VAR_038359|||http://purl.uniprot.org/annotation/VAR_038360|||http://purl.uniprot.org/annotation/VAR_038361|||http://purl.uniprot.org/annotation/VAR_058990|||http://purl.uniprot.org/annotation/VAR_058991|||http://purl.uniprot.org/annotation/VAR_058992|||http://purl.uniprot.org/annotation/VAR_058993|||http://purl.uniprot.org/annotation/VAR_058994|||http://purl.uniprot.org/annotation/VAR_058995|||http://purl.uniprot.org/annotation/VAR_058996|||http://purl.uniprot.org/annotation/VAR_058997|||http://purl.uniprot.org/annotation/VAR_058998|||http://purl.uniprot.org/annotation/VAR_058999|||http://purl.uniprot.org/annotation/VAR_059000|||http://purl.uniprot.org/annotation/VAR_059001|||http://purl.uniprot.org/annotation/VAR_059002|||http://purl.uniprot.org/annotation/VAR_059003|||http://purl.uniprot.org/annotation/VAR_059004|||http://purl.uniprot.org/annotation/VAR_059005|||http://purl.uniprot.org/annotation/VAR_059006|||http://purl.uniprot.org/annotation/VAR_059007|||http://purl.uniprot.org/annotation/VAR_059008|||http://purl.uniprot.org/annotation/VAR_059009|||http://purl.uniprot.org/annotation/VAR_059010|||http://purl.uniprot.org/annotation/VAR_059011|||http://purl.uniprot.org/annotation/VAR_059012|||http://purl.uniprot.org/annotation/VAR_059013|||http://purl.uniprot.org/annotation/VAR_059014|||http://purl.uniprot.org/annotation/VAR_059015|||http://purl.uniprot.org/annotation/VAR_059016|||http://purl.uniprot.org/annotation/VAR_059017|||http://purl.uniprot.org/annotation/VAR_070439|||http://purl.uniprot.org/annotation/VAR_070440|||http://purl.uniprot.org/annotation/VAR_070441|||http://purl.uniprot.org/annotation/VAR_071009|||http://purl.uniprot.org/annotation/VAR_071010|||http://purl.uniprot.org/annotation/VAR_071011|||http://purl.uniprot.org/annotation/VAR_075754|||http://purl.uniprot.org/annotation/VAR_075755|||http://purl.uniprot.org/annotation/VAR_075756|||http://purl.uniprot.org/annotation/VAR_078238
http://togogenome.org/gene/9606:KDM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSN4|||http://purl.uniprot.org/uniprot/Q8NHM5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CXXC-type|||Decreased ininteraction with UBB.|||Disordered|||F-box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increased interaction with UBB.|||JmjC|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Lysine-specific demethylase 2B|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119853|||http://purl.uniprot.org/annotation/VSP_011340|||http://purl.uniprot.org/annotation/VSP_011341|||http://purl.uniprot.org/annotation/VSP_017475|||http://purl.uniprot.org/annotation/VSP_017476|||http://purl.uniprot.org/annotation/VSP_043146|||http://purl.uniprot.org/annotation/VSP_043147|||http://purl.uniprot.org/annotation/VSP_043148|||http://purl.uniprot.org/annotation/VSP_057394|||http://purl.uniprot.org/annotation/VSP_057395|||http://purl.uniprot.org/annotation/VSP_057396
http://togogenome.org/gene/9606:SLC35G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKP0|||http://purl.uniprot.org/uniprot/Q2M3R5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA|||EamA 1|||EamA 2|||Helical|||In isoform 2.|||Solute carrier family 35 member G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244463|||http://purl.uniprot.org/annotation/VSP_019566
http://togogenome.org/gene/9606:PLPBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94903                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In EPVB6D.|||In EPVB6D; decreased expression at the mRNA level; undetectable at the protein level in patient's fibroblasts.|||N6-(pyridoxal phosphate)lysine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Pyridoxal phosphate homeostasis protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163210|||http://purl.uniprot.org/annotation/VAR_052476|||http://purl.uniprot.org/annotation/VAR_078004|||http://purl.uniprot.org/annotation/VAR_078005|||http://purl.uniprot.org/annotation/VAR_078006|||http://purl.uniprot.org/annotation/VAR_078007|||http://purl.uniprot.org/annotation/VAR_078008
http://togogenome.org/gene/9606:TEAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28347|||http://purl.uniprot.org/uniprot/Q59EF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Important loss of interaction with YAP1.|||In SCRA; loss of interaction with YAP1 and also activation by YAP1.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||TEA|||Transcriptional activation|||Transcriptional enhancer factor TEF-1|||YAP binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205930|||http://purl.uniprot.org/annotation/VAR_031530|||http://purl.uniprot.org/annotation/VSP_056275|||http://purl.uniprot.org/annotation/VSP_056276|||http://purl.uniprot.org/annotation/VSP_056277
http://togogenome.org/gene/9606:PSMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 3|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||PCI|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173816|||http://purl.uniprot.org/annotation/VSP_056362|||http://purl.uniprot.org/annotation/VSP_056363
http://togogenome.org/gene/9606:TIGD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6B0B8                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent                                                                                  ^@                                                                                  DDE-1|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Tigger transposable element-derived protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271090
http://togogenome.org/gene/9606:EPB42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16452                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Band 3 binding|||In SPH5; Komatsu.|||In SPH5; Nippon/Fukuoka.|||In SPH5; Shiga.|||In SPH5; Tozeur.|||In isoform 3.|||In isoform Long.|||N-myristoyl glycine|||Phosphoserine; by PKA|||Protein 4.2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213720|||http://purl.uniprot.org/annotation/VAR_007482|||http://purl.uniprot.org/annotation/VAR_012268|||http://purl.uniprot.org/annotation/VAR_058099|||http://purl.uniprot.org/annotation/VAR_058100|||http://purl.uniprot.org/annotation/VSP_006416|||http://purl.uniprot.org/annotation/VSP_055340
http://togogenome.org/gene/9606:ZNF706                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5V0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Polar residues|||Zinc finger protein 706                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047703
http://togogenome.org/gene/9606:CBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14781                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  A.T hook|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Chromo|||Chromobox protein homolog 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In SRXY5.|||In isoform 2.|||Involved in the interaction with H3C15 and H3C1|||Nuclear localization signal|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Reduced interaction with H3C15 and H3C1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080201|||http://purl.uniprot.org/annotation/VAR_063751|||http://purl.uniprot.org/annotation/VAR_063752|||http://purl.uniprot.org/annotation/VSP_015816|||http://purl.uniprot.org/annotation/VSP_015817
http://togogenome.org/gene/9606:STOML3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAV4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Phosphoserine|||Stomatin-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094033|||http://purl.uniprot.org/annotation/VSP_042937
http://togogenome.org/gene/9606:PXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ8|||http://purl.uniprot.org/uniprot/P49023                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 4.|||In isoform Alpha and isoform 4.|||In isoform Gamma.|||LD motif 1|||LD motif 2|||LD motif 3|||LD motif 4|||LD motif 5|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Loss of interaction with PDCD10.|||N-acetylmethionine|||N-acetylserine|||Paxillin|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by SLK|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by PTK6|||Polar residues|||Removed|||Required for binding to PARVA and ILK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075853|||http://purl.uniprot.org/annotation/VAR_065099|||http://purl.uniprot.org/annotation/VSP_003114|||http://purl.uniprot.org/annotation/VSP_003115|||http://purl.uniprot.org/annotation/VSP_040483
http://togogenome.org/gene/9606:ZBTB42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXF5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In LCCS6; loss of function mutation.|||Zinc finger and BTB domain-containing protein 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343711|||http://purl.uniprot.org/annotation/VAR_073265
http://togogenome.org/gene/9606:LRPPRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KNY5|||http://purl.uniprot.org/uniprot/P42704                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  In MC4DN5.|||In MC4DN5; unknown pathological significance.|||Leucine-rich PPR motif-containing protein, mitochondrial|||Mitochondrion|||N6-acetyllysine|||PPR|||PPR 1|||PPR 10|||PPR 11|||PPR 12|||PPR 13|||PPR 14|||PPR 15|||PPR 16|||PPR 17|||PPR 18|||PPR 19|||PPR 2|||PPR 20|||PPR 3|||PPR 4|||PPR 5|||PPR 6|||PPR 7|||PPR 8|||PPR 9|||Pentacotripeptide-repeat region of PRORP|||Phosphoserine|||Phosphothreonine|||RNA-binding|||Reduces binding to EIF4E.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084467|||http://purl.uniprot.org/annotation/VAR_018656|||http://purl.uniprot.org/annotation/VAR_052935|||http://purl.uniprot.org/annotation/VAR_075428|||http://purl.uniprot.org/annotation/VAR_075429
http://togogenome.org/gene/9606:KLHL34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N239                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  Acidic residues|||BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274597
http://togogenome.org/gene/9606:FXYD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00168                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phospholemman|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKA and PKC|||Phosphothreonine|||Phosphothreonine; by PKC|||S-glutathionyl cysteine; alternate|||S-palmitoyl cysteine|||S-palmitoyl cysteine; alternate|||Significantly reduced half-life; when associated with S-60.|||Significantly reduced half-life; when associated with S-62.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010359
http://togogenome.org/gene/9606:CLCN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51793                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes translocation of protons and chloride ions.|||CBS 1|||CBS 2|||Cytoplasmic|||H(+)/Cl(-) exchange transporter 4|||Helical|||In MRXSRC; also in patients with complex congenital diaphragmatic hernia; unknown pathological significance; no reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane.|||In MRXSRC; has normal localization to structures resembling endoplasmic reticulum membranes; almost abolishes the outwardly-rectifying currents.|||In MRXSRC; marked reduction in outwardly-rectifying currents.|||In MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum membrane.|||In MRXSRC; marked reduction in outwardly-rectifying currents; does not affect its localization in endoplasmic reticulum.|||In isoform 2.|||Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport|||Mediates proton transfer from the protein to the inner aqueous phase|||Note=Loop between two helices|||Required for localization in the endoplasmic reticulum|||Restores chloride translocation, but not proton transport; when associated with A-281.|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094443|||http://purl.uniprot.org/annotation/VAR_077819|||http://purl.uniprot.org/annotation/VAR_077820|||http://purl.uniprot.org/annotation/VAR_077821|||http://purl.uniprot.org/annotation/VAR_077822|||http://purl.uniprot.org/annotation/VAR_077823|||http://purl.uniprot.org/annotation/VAR_083577|||http://purl.uniprot.org/annotation/VAR_083578|||http://purl.uniprot.org/annotation/VAR_083579|||http://purl.uniprot.org/annotation/VAR_083580|||http://purl.uniprot.org/annotation/VAR_083581|||http://purl.uniprot.org/annotation/VAR_083582|||http://purl.uniprot.org/annotation/VAR_083583|||http://purl.uniprot.org/annotation/VSP_054658
http://togogenome.org/gene/9606:NKAPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein NKAPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274244|||http://purl.uniprot.org/annotation/VSP_022685|||http://purl.uniprot.org/annotation/VSP_022686
http://togogenome.org/gene/9606:KDM7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||JmjC|||Linker|||Lysine-specific demethylase 7A|||PHD-type|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226771|||http://purl.uniprot.org/annotation/VAR_049653|||http://purl.uniprot.org/annotation/VSP_017458|||http://purl.uniprot.org/annotation/VSP_017459
http://togogenome.org/gene/9606:OR4D9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP8|||http://purl.uniprot.org/uniprot/Q8NGE8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150541|||http://purl.uniprot.org/annotation/VAR_053170
http://togogenome.org/gene/9606:KRTAP5-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8H4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184099
http://togogenome.org/gene/9606:SMR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02814|||http://purl.uniprot.org/uniprot/Q504X8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Peptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Peptide D1A|||Peptide P-A|||Pro residues|||Pyrrolidone carboxylic acid|||Submaxillary gland androgen-regulated protein 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022112|||http://purl.uniprot.org/annotation/PRO_0000022113|||http://purl.uniprot.org/annotation/PRO_0000022114|||http://purl.uniprot.org/annotation/PRO_5004247542
http://togogenome.org/gene/9606:CLEC2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UVW9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 2 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on affinity for KLRF2.|||Reduces affinity for KLRF2 360-fold.|||Reduces affinity for KLRF2 40-fold.|||Reduces affinity for KLRF2 550-fold.|||Reduces affinity for KLRF2 over 10'000-fold.|||Slightly reduces affinity for KLRF2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264240|||http://purl.uniprot.org/annotation/VAR_029629|||http://purl.uniprot.org/annotation/VSP_035643
http://togogenome.org/gene/9606:TPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1I0|||http://purl.uniprot.org/uniprot/B7Z722|||http://purl.uniprot.org/uniprot/D9YZV4|||http://purl.uniprot.org/uniprot/D9YZV5|||http://purl.uniprot.org/uniprot/D9YZV7|||http://purl.uniprot.org/uniprot/F5H7S3|||http://purl.uniprot.org/uniprot/H0YK48|||http://purl.uniprot.org/uniprot/H7BYY1|||http://purl.uniprot.org/uniprot/O15513|||http://purl.uniprot.org/uniprot/P09493                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Impairs interaction with LMOD2 and TMOD1.|||In CMD1Y.|||In CMH3.|||In CMH3; no change in homodimerization; decreased in hom odimer thermal stability; decreased in actin binding; increased calcium-dependent regulation of myosin binding to actin filaments; dominant effect in the homodimer.|||In CMH3; no change in homodimerization; no change in homodimer thermal stability; decreased actin binding; recessive effect in the homodimer; increased calcium-dependent regulation of myosin binding to actin filaments; dominant effect in the homodimer.|||In LVNC9.|||In isoform 10.|||In isoform 2, isoform 3, isoform 7, isoform 8 and isoform 9.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8 and isoform 10.|||In isoform 8.|||Increased formation of actin stress fibers.|||Loss of phosphorylation and decreased formation of actin stress fibers.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by DAPK1|||Phosphotyrosine|||The measured range is 1-284.|||Tropomyosin alpha-1 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205620|||http://purl.uniprot.org/annotation/VAR_007601|||http://purl.uniprot.org/annotation/VAR_007602|||http://purl.uniprot.org/annotation/VAR_013135|||http://purl.uniprot.org/annotation/VAR_029452|||http://purl.uniprot.org/annotation/VAR_043986|||http://purl.uniprot.org/annotation/VAR_043987|||http://purl.uniprot.org/annotation/VAR_070121|||http://purl.uniprot.org/annotation/VAR_070122|||http://purl.uniprot.org/annotation/VSP_006576|||http://purl.uniprot.org/annotation/VSP_006577|||http://purl.uniprot.org/annotation/VSP_006578|||http://purl.uniprot.org/annotation/VSP_006579|||http://purl.uniprot.org/annotation/VSP_017498|||http://purl.uniprot.org/annotation/VSP_017499|||http://purl.uniprot.org/annotation/VSP_036064|||http://purl.uniprot.org/annotation/VSP_047297|||http://purl.uniprot.org/annotation/VSP_047298|||http://purl.uniprot.org/annotation/VSP_047299|||http://purl.uniprot.org/annotation/VSP_047300|||http://purl.uniprot.org/annotation/VSP_047301
http://togogenome.org/gene/9606:RPS6KA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDW3|||http://purl.uniprot.org/uniprot/B1AXG1|||http://purl.uniprot.org/uniprot/B4DG22|||http://purl.uniprot.org/uniprot/B7ZB17|||http://purl.uniprot.org/uniprot/P51812                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||In CLS.|||In XLID19.|||In XLID19; kinase activity is decreased but not abolished.|||In a breast cancer sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||Phosphoserine|||Phosphoserine; by PDPK1|||Phosphoserine; by autocatalysis and MAPKAPK2|||Phosphothreonine|||Phosphotyrosine; by FGFR3|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086203|||http://purl.uniprot.org/annotation/VAR_006188|||http://purl.uniprot.org/annotation/VAR_006189|||http://purl.uniprot.org/annotation/VAR_006190|||http://purl.uniprot.org/annotation/VAR_006191|||http://purl.uniprot.org/annotation/VAR_006192|||http://purl.uniprot.org/annotation/VAR_006193|||http://purl.uniprot.org/annotation/VAR_006194|||http://purl.uniprot.org/annotation/VAR_006195|||http://purl.uniprot.org/annotation/VAR_006196|||http://purl.uniprot.org/annotation/VAR_006197|||http://purl.uniprot.org/annotation/VAR_035627|||http://purl.uniprot.org/annotation/VAR_040629|||http://purl.uniprot.org/annotation/VAR_040630|||http://purl.uniprot.org/annotation/VAR_040631|||http://purl.uniprot.org/annotation/VAR_065892|||http://purl.uniprot.org/annotation/VAR_065893|||http://purl.uniprot.org/annotation/VAR_065894|||http://purl.uniprot.org/annotation/VAR_065895|||http://purl.uniprot.org/annotation/VAR_065896|||http://purl.uniprot.org/annotation/VAR_065897|||http://purl.uniprot.org/annotation/VAR_065898
http://togogenome.org/gene/9606:SEC61A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KME8|||http://purl.uniprot.org/uniprot/B3KNF6|||http://purl.uniprot.org/uniprot/P61619                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In ADTKD5; decreases in protein stability; partly confers novel Golgi subcellular location.|||In isoform 3.|||Lumenal|||Probable disease-associated variant found in a family with hypogammaglobulinemia; decreased function in cotranslational protein targeting to endoplasmic reticulum.|||Protein transport protein Sec61 subunit alpha isoform 1|||Reduces cotranslational translocation of APLN precursor/preproapelin.|||Translocon Sec61/SecY plug                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131791|||http://purl.uniprot.org/annotation/VAR_077059|||http://purl.uniprot.org/annotation/VAR_077060|||http://purl.uniprot.org/annotation/VAR_080231|||http://purl.uniprot.org/annotation/VSP_013747
http://togogenome.org/gene/9606:AGK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1U5|||http://purl.uniprot.org/uniprot/Q53H12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes lipid kinase activity. Does not affect ability to associate with the TIM22 complex and mediate import of transmembrane proteins into the mitochondrial inner membrane.|||Acylglycerol kinase, mitochondrial|||DAGKc|||Disordered|||Hydrophobic|||In MTDPS10.|||In isoform 2.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252380|||http://purl.uniprot.org/annotation/VAR_027848|||http://purl.uniprot.org/annotation/VAR_079050|||http://purl.uniprot.org/annotation/VAR_079051|||http://purl.uniprot.org/annotation/VAR_079052|||http://purl.uniprot.org/annotation/VSP_020925|||http://purl.uniprot.org/annotation/VSP_020926
http://togogenome.org/gene/9606:OR5T3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGG3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5T3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150615|||http://purl.uniprot.org/annotation/VAR_047836
http://togogenome.org/gene/9606:ASAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR71                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Decreased ceramide hydrolase activity.|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of ceramide hydrolase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Neutral ceramidase|||Neutral ceramidase soluble form|||No effect on ceramide hydrolase activity.|||Nucleophile|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Required for correct folding and localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247099|||http://purl.uniprot.org/annotation/PRO_0000247100|||http://purl.uniprot.org/annotation/VAR_027064|||http://purl.uniprot.org/annotation/VAR_027065|||http://purl.uniprot.org/annotation/VSP_019928
http://togogenome.org/gene/9606:PCDHGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003952|||http://purl.uniprot.org/annotation/VAR_055588|||http://purl.uniprot.org/annotation/VAR_055589|||http://purl.uniprot.org/annotation/VAR_059190|||http://purl.uniprot.org/annotation/VSP_008663|||http://purl.uniprot.org/annotation/VSP_008664
http://togogenome.org/gene/9606:TBC1D13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNG3|||http://purl.uniprot.org/uniprot/B4DHM6|||http://purl.uniprot.org/uniprot/Q9NVG8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Rab-GAP TBC|||TBC1 domain family member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208038|||http://purl.uniprot.org/annotation/VAR_070804|||http://purl.uniprot.org/annotation/VSP_039845|||http://purl.uniprot.org/annotation/VSP_053994
http://togogenome.org/gene/9606:DCUN1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PH85                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DCN1-like protein 2|||DCUN1|||In isoform 2.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and A-241. Does not affect both nucleus and cytoplasm localization; when associated with A-211 and A-241.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and R-235. Does not affect both nucleus and cytoplasm localization; when associated with A-211 and R-235.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with R-235 and A-241. Does not affect both nucleus and cytoplasm localization; when associated with R-235 and A-241.|||Phosphoserine|||UBA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129501|||http://purl.uniprot.org/annotation/VSP_015315|||http://purl.uniprot.org/annotation/VSP_015316
http://togogenome.org/gene/9606:VPS37A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEZ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SPG53; found in patients with complex hereditary spastic paraparesis; hypomorphic mutation; does not affect interaction with TSG101 and VPS28.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287198|||http://purl.uniprot.org/annotation/VAR_032287|||http://purl.uniprot.org/annotation/VAR_032288|||http://purl.uniprot.org/annotation/VAR_068424|||http://purl.uniprot.org/annotation/VSP_025367|||http://purl.uniprot.org/annotation/VSP_025368|||http://purl.uniprot.org/annotation/VSP_025369
http://togogenome.org/gene/9606:ATP8A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z880|||http://purl.uniprot.org/uniprot/Q6ZU25|||http://purl.uniprot.org/uniprot/Q9NTI2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Abolishes ATPase activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CAMRQ4; abolishes ATPase activity. No effect on interaction with TMEM30A.|||In CAMRQ4; unknown pathological significance.|||In CAMRQ4; unknown pathological significance; abolishes ATPase activity and results in protein misfolding and proteasomal degradation. No effect on interaction with TMEM30A.|||In CAMRQ4; unknown pathological significance; abolishes ATPase activity. No effect on interaction with TMEM30A.|||In CAMRQ4; unknown pathological significance; results in protein misfolding and proteasomal degradation.|||In isoform 1 and isoform 2.|||In isoform 2.|||Involved in the recognition of the lipid substrate on the exoplasmic side|||Involved in the release of the transported lipid into the cytosolic leaflet|||No effect on flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase IB|||Phosphothreonine|||Reduced flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046362|||http://purl.uniprot.org/annotation/VAR_055543|||http://purl.uniprot.org/annotation/VAR_069928|||http://purl.uniprot.org/annotation/VAR_084370|||http://purl.uniprot.org/annotation/VAR_084371|||http://purl.uniprot.org/annotation/VAR_084372|||http://purl.uniprot.org/annotation/VAR_084373|||http://purl.uniprot.org/annotation/VAR_084374|||http://purl.uniprot.org/annotation/VAR_084375|||http://purl.uniprot.org/annotation/VAR_084376|||http://purl.uniprot.org/annotation/VAR_084377|||http://purl.uniprot.org/annotation/VSP_059718|||http://purl.uniprot.org/annotation/VSP_059719|||http://purl.uniprot.org/annotation/VSP_059720
http://togogenome.org/gene/9606:NEK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6U4U2|||http://purl.uniprot.org/uniprot/P51955                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CEP85|||Interaction with PCNT|||Interaction with SAV1 and STK3/MST2|||Kinase activity decreased by two fold.|||Kinase activity increased by two fold.|||Leucine-zipper|||Loss of autophosphorylation.|||Loss of kinase activity and of ability to activate NEK11. Loss of phosphorylation of CCDC102B.|||Loss of kinase activity.|||Necessary for interaction with MAD1L1|||No effect on kinase activity.|||Phosphoserine|||Phosphoserine; by STK3/MST2|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Required for microtubule binding and for localization to the centrosomes|||Serine/threonine-protein kinase Nek2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086421|||http://purl.uniprot.org/annotation/VAR_019990|||http://purl.uniprot.org/annotation/VAR_040907|||http://purl.uniprot.org/annotation/VSP_015576|||http://purl.uniprot.org/annotation/VSP_015577|||http://purl.uniprot.org/annotation/VSP_015578|||http://purl.uniprot.org/annotation/VSP_015579|||http://purl.uniprot.org/annotation/VSP_041758
http://togogenome.org/gene/9606:GPR63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1C4|||http://purl.uniprot.org/uniprot/Q9BZJ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 63                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069581|||http://purl.uniprot.org/annotation/VAR_049396
http://togogenome.org/gene/9606:RCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZU3|||http://purl.uniprot.org/uniprot/Q9Y2P8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||RNA 3'-terminal phosphate cyclase|||RNA 3'-terminal phosphate cyclase insert|||RNA 3'-terminal phosphate cyclase-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156438|||http://purl.uniprot.org/annotation/VSP_056452|||http://purl.uniprot.org/annotation/VSP_056453
http://togogenome.org/gene/9606:SLC1A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUF9|||http://purl.uniprot.org/uniprot/F1T0D3|||http://purl.uniprot.org/uniprot/F1T0D4|||http://purl.uniprot.org/uniprot/G1CT06|||http://purl.uniprot.org/uniprot/O00341                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Excitatory amino acid transporter 5|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202073|||http://purl.uniprot.org/annotation/VAR_035707|||http://purl.uniprot.org/annotation/VAR_052488|||http://purl.uniprot.org/annotation/VSP_056560|||http://purl.uniprot.org/annotation/VSP_056561
http://togogenome.org/gene/9606:CCR10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46092                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 10|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069293
http://togogenome.org/gene/9606:UBE2R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q712K3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2.|||Acidic residues|||Disordered|||Glycyl thioester intermediate|||Loss of function.|||Phosphoserine; by CK2|||UBC core|||Ubiquitin-conjugating enzyme E2 R2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280513
http://togogenome.org/gene/9606:CPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSY5|||http://purl.uniprot.org/uniprot/Q96IY4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase B2|||Cleavage; by thrombin|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004377|||http://purl.uniprot.org/annotation/PRO_0000004378|||http://purl.uniprot.org/annotation/PRO_5001831887|||http://purl.uniprot.org/annotation/VAR_022258|||http://purl.uniprot.org/annotation/VAR_032565|||http://purl.uniprot.org/annotation/VSP_013446|||http://purl.uniprot.org/annotation/VSP_013447
http://togogenome.org/gene/9606:TPRX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2CFI5|||http://purl.uniprot.org/uniprot/Q8N7U7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2.|||Pro residues|||Tetra-peptide repeat homeobox protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285591|||http://purl.uniprot.org/annotation/VSP_027444
http://togogenome.org/gene/9606:NCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQZ0|||http://purl.uniprot.org/uniprot/A0A0A0MR94|||http://purl.uniprot.org/uniprot/A0A0A0MTU0|||http://purl.uniprot.org/uniprot/O76036                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like 1|||Ig-like 2|||Immunoglobulin subtype|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Natural cytotoxicity triggering receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015027|||http://purl.uniprot.org/annotation/PRO_5014015972|||http://purl.uniprot.org/annotation/PRO_5014015973|||http://purl.uniprot.org/annotation/PRO_5014015975|||http://purl.uniprot.org/annotation/VAR_018633|||http://purl.uniprot.org/annotation/VAR_035527|||http://purl.uniprot.org/annotation/VSP_010406|||http://purl.uniprot.org/annotation/VSP_010407|||http://purl.uniprot.org/annotation/VSP_010408|||http://purl.uniprot.org/annotation/VSP_038384
http://togogenome.org/gene/9606:CPNE7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-7|||In isoform 2.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144848|||http://purl.uniprot.org/annotation/VAR_021955|||http://purl.uniprot.org/annotation/VAR_021956|||http://purl.uniprot.org/annotation/VAR_033822|||http://purl.uniprot.org/annotation/VAR_048849|||http://purl.uniprot.org/annotation/VSP_001215
http://togogenome.org/gene/9606:BNIPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z465                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein|||CRAL-TRIO|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210770|||http://purl.uniprot.org/annotation/VAR_051917|||http://purl.uniprot.org/annotation/VAR_051918|||http://purl.uniprot.org/annotation/VSP_012448|||http://purl.uniprot.org/annotation/VSP_012449
http://togogenome.org/gene/9606:SEH1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EE3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform B.|||Nucleoporin SEH1|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051213|||http://purl.uniprot.org/annotation/VAR_053417|||http://purl.uniprot.org/annotation/VSP_037954
http://togogenome.org/gene/9606:FAM149A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein FAM149A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319930|||http://purl.uniprot.org/annotation/VAR_039050|||http://purl.uniprot.org/annotation/VAR_039051|||http://purl.uniprot.org/annotation/VAR_039052|||http://purl.uniprot.org/annotation/VAR_039053|||http://purl.uniprot.org/annotation/VAR_039054|||http://purl.uniprot.org/annotation/VAR_039055|||http://purl.uniprot.org/annotation/VSP_031530|||http://purl.uniprot.org/annotation/VSP_031531|||http://purl.uniprot.org/annotation/VSP_031532
http://togogenome.org/gene/9606:CD300LG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMRF35-like molecule 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306112|||http://purl.uniprot.org/annotation/VAR_035261|||http://purl.uniprot.org/annotation/VAR_035262|||http://purl.uniprot.org/annotation/VSP_028410|||http://purl.uniprot.org/annotation/VSP_028411|||http://purl.uniprot.org/annotation/VSP_028412|||http://purl.uniprot.org/annotation/VSP_045362
http://togogenome.org/gene/9606:TASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6P5                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  0.1% enzymatic activity; no intramolecular processing.|||Complete loss of enzymatic activity; no intramolecular processing.|||Disordered|||In SULEHS.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Threonine aspartase subunit alpha|||Threonine aspartase subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002350|||http://purl.uniprot.org/annotation/PRO_0000002351|||http://purl.uniprot.org/annotation/VAR_084461|||http://purl.uniprot.org/annotation/VAR_084462|||http://purl.uniprot.org/annotation/VSP_056327|||http://purl.uniprot.org/annotation/VSP_056328|||http://purl.uniprot.org/annotation/VSP_056533|||http://purl.uniprot.org/annotation/VSP_056534
http://togogenome.org/gene/9606:CCND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24385|||http://purl.uniprot.org/uniprot/Q6FI00                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-D1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphothreonine|||Reduced interaction with the DCX(AMBRA1) complex, and subsequent ubiquitination and degradation by the proteasome.|||Reduced interaction with the DCX(AMBRA1) complex, and subsequent ubiquitination and degradation by the proteasome. Abolished ubiquitination and subsequent degradation following DNA damage.|||Reduced ubiquitination and subsequent degradation by the proteasome.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080430
http://togogenome.org/gene/9606:SPEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4L4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Spermatid maturation protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307806
http://togogenome.org/gene/9606:CCDC88A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14997|||http://purl.uniprot.org/uniprot/Q3V6T2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes binding to phosphorylated EGFR.|||Abolishes interaction with GNAI3.|||Abolishes interaction with and activation of GNAI3 and also abolishes recruitment of GNAI3 to EGFR. Reduced EGFR autophosphorylation and SH2 adapter recruitment, reduced localization of EGFR at the cell membrane following ligand stimulation with increased endosomal localization, reduced cell migration and increased cell proliferation. Abolishes enhancement of AKT signaling. Abolishes interaction with GNAS.|||Abolishes phosphorylation and leads to reduced AKT phosphorylation, impaired formation of actin stress fibers and impaired cell migration abolishes interaction with PIK3R1 and activation of PI3K, reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3; when associated with F-1799.|||Abolishes phosphorylation and leads to reduced AKT phosphorylation, impaired formation of actin stress fibers and impaired cell migration, abolishes interaction with PIK3R1 and activation of PI3K activity, reduces phosphorylation of Ser-1417 but does not affect interaction with or activation of GNAI3; when associated with F-1765.|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Does not affect binding to phosphorylated EGFR.|||GBA|||Girdin|||HOOK N-terminal|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||Increases binding to phosphorylated EGFR.|||No effect on guanine nucleotide exchange factor activity.|||Phosphoinositide-binding|||Phosphomimetic mutant which abolishes interaction with GNAI3, inhibits guanine nucleotide exchange factor activity, inhibits cell migration and triggers cell proliferation. Retains ability to bind to GNAS. Increased inhibition of GNAS; when associated with D-1675.|||Phosphomimetic mutant which has no effect on tyrosine phosphorylation.|||Phosphomimetic mutant which results in slight increase in binding to GNAI3 and GNAS. Increased inhibition of GNAS; when associated with D-1690.|||Phosphorylation-deficient mutant which disrupts actin organization, cell migration and lamellipodia formation but has no effect on tyrosine phosphorylation.|||Phosphorylation-deficient mutant which disrupts binding to GNAI3 and GNAS.|||Phosphorylation-deficient mutant which retains the ability to bind GNAI3.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH2-like; required for interaction with growth factor receptors                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287429|||http://purl.uniprot.org/annotation/VSP_040129|||http://purl.uniprot.org/annotation/VSP_044943|||http://purl.uniprot.org/annotation/VSP_052409
http://togogenome.org/gene/9606:HOMER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSB8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homer protein homolog 2|||In DFNA68.|||In isoform 2.|||Polar residues|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191008|||http://purl.uniprot.org/annotation/VAR_053366|||http://purl.uniprot.org/annotation/VAR_053367|||http://purl.uniprot.org/annotation/VAR_075751|||http://purl.uniprot.org/annotation/VSP_041731
http://togogenome.org/gene/9606:ACSM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7M7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A synthetase ACSM4, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339384|||http://purl.uniprot.org/annotation/VAR_061010
http://togogenome.org/gene/9606:DNAAF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0IIP3|||http://purl.uniprot.org/uniprot/Q5TEA3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal assembly factor 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236042|||http://purl.uniprot.org/annotation/VAR_050923|||http://purl.uniprot.org/annotation/VAR_050924|||http://purl.uniprot.org/annotation/VAR_059637|||http://purl.uniprot.org/annotation/VAR_065913
http://togogenome.org/gene/9606:PCED1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HM7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||PC-esterase domain-containing protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331356|||http://purl.uniprot.org/annotation/VAR_042761
http://togogenome.org/gene/9606:GIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Gypsy retrotransposon integrase-like protein 1|||In isoform 2.|||In isoform 3.|||Integrase catalytic|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333016|||http://purl.uniprot.org/annotation/VAR_043041|||http://purl.uniprot.org/annotation/VAR_043042|||http://purl.uniprot.org/annotation/VSP_033438|||http://purl.uniprot.org/annotation/VSP_033439|||http://purl.uniprot.org/annotation/VSP_038518|||http://purl.uniprot.org/annotation/VSP_038519
http://togogenome.org/gene/9606:RAB11FIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YS3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes Rab11-binding.|||Disordered|||EF-hand|||FIP-RBD|||In isoform 2.|||Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerization|||Polar residues|||Rab11 family-interacting protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073880|||http://purl.uniprot.org/annotation/VSP_013724|||http://purl.uniprot.org/annotation/VSP_013725
http://togogenome.org/gene/9606:REM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75628                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||GTP-binding protein REM 1|||No endothelial cell sprouting.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122481|||http://purl.uniprot.org/annotation/VAR_049498|||http://purl.uniprot.org/annotation/VAR_049499|||http://purl.uniprot.org/annotation/VAR_061232
http://togogenome.org/gene/9606:MEAK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5C2|||http://purl.uniprot.org/uniprot/Q6P9B6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Abolishes lysosomal location.|||MTOR-associated protein MEAK7|||N-myristoyl glycine|||Removed|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313640|||http://purl.uniprot.org/annotation/VAR_037675|||http://purl.uniprot.org/annotation/VAR_037676|||http://purl.uniprot.org/annotation/VAR_037677|||http://purl.uniprot.org/annotation/VAR_037678|||http://purl.uniprot.org/annotation/VAR_037679|||http://purl.uniprot.org/annotation/VAR_037680|||http://purl.uniprot.org/annotation/VAR_037681
http://togogenome.org/gene/9606:ZDHHC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUH4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Cytoplasmic|||DHHC|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylmethionine|||Palmitoyltransferase ZDHHC13|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212887|||http://purl.uniprot.org/annotation/VAR_023835|||http://purl.uniprot.org/annotation/VAR_057490|||http://purl.uniprot.org/annotation/VSP_010028|||http://purl.uniprot.org/annotation/VSP_010029
http://togogenome.org/gene/9606:BRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95696|||http://purl.uniprot.org/uniprot/Q59G93                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo|||Bromodomain-containing protein 1|||C2HC pre-PHD-type|||Decreased interaction with free histones.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired interaction with KAT7/HBO1.|||In isoform 2.|||Interaction with KAT7/HBO1 and histones|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PWWP|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211177|||http://purl.uniprot.org/annotation/VAR_048424|||http://purl.uniprot.org/annotation/VAR_048425|||http://purl.uniprot.org/annotation/VAR_048426|||http://purl.uniprot.org/annotation/VAR_079184|||http://purl.uniprot.org/annotation/VSP_040262
http://togogenome.org/gene/9606:COLEC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5KU26                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collectin-12|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318681|||http://purl.uniprot.org/annotation/VAR_038853|||http://purl.uniprot.org/annotation/VAR_038854|||http://purl.uniprot.org/annotation/VAR_038855|||http://purl.uniprot.org/annotation/VAR_038856
http://togogenome.org/gene/9606:SPMAP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Sperm microtubule associated protein 2-like|||THEG 1|||THEG 2|||THEG 3|||THEG 4|||THEG 5|||THEG 6|||THEG 7|||THEG 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416826
http://togogenome.org/gene/9606:PPP1R1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13522                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1000-fold reduction in activity, inhibits equally PP1 and PP2A.|||Basic and acidic residues|||Disordered|||Essential for activity|||Interaction with PPP1R15A|||N-acetylmethionine|||No activity.|||Phosphoserine|||Phosphothreonine; by PKA|||Polar residues|||Protein phosphatase 1 regulatory subunit 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071477|||http://purl.uniprot.org/annotation/VAR_053898|||http://purl.uniprot.org/annotation/VAR_053899
http://togogenome.org/gene/9606:UBTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ubiquitin domain-containing protein 1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242674
http://togogenome.org/gene/9606:ZNF195                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14628                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 4 and isoform 7.|||In isoform 5 and isoform 6.|||In isoform 6, isoform 7 and isoform 8.|||In isoform 8.|||KRAB|||N6-acetyllysine|||Spacer|||Zinc finger protein 195                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047447|||http://purl.uniprot.org/annotation/VSP_036879|||http://purl.uniprot.org/annotation/VSP_036880|||http://purl.uniprot.org/annotation/VSP_036881|||http://purl.uniprot.org/annotation/VSP_045071|||http://purl.uniprot.org/annotation/VSP_045072
http://togogenome.org/gene/9606:IRF2BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5L9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Cys-rich|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CVID14; increased protein abundance in patient-derived B lymphocytes; impairs immature B cell differentiation.|||In isoform 2.|||In isoform 3.|||Interferon regulatory factor 2-binding protein 2|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues|||RING-type; degenerate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328734|||http://purl.uniprot.org/annotation/VAR_042503|||http://purl.uniprot.org/annotation/VAR_080578|||http://purl.uniprot.org/annotation/VSP_032769|||http://purl.uniprot.org/annotation/VSP_032770
http://togogenome.org/gene/9606:FAM177A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N128                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein FAM177A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089885|||http://purl.uniprot.org/annotation/VSP_038223
http://togogenome.org/gene/9606:CD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4Y5UGE4|||http://purl.uniprot.org/uniprot/B0AZV7|||http://purl.uniprot.org/uniprot/B4DT49|||http://purl.uniprot.org/uniprot/P01730                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished interaction with SPG21 and induced T-cell activation.|||About 75% loss of internalization.|||Abrogates the interaction with MHCII and T cell activation.|||CD4 extracellular|||Cytoplasmic|||Extracellular|||HIV-1 Vpu-susceptibility domain|||Has no effect on the interaction with MHCII. Impairs recognition by OKT4 antibody.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||Immunoglobulin C2-set|||In OKT4-negative populations.|||Increases the affinity for MHCII; when associated with W-70; R-85 and R-88.|||Increases the affinity for MHCII; when associated with Y-65; R-85 and R-88.|||Increases the affinity for MHCII; when associated with Y-65; W-70 and R-85.|||Increases the affinity for MHCII; when associated with Y-65; W-70 and R-88.|||Loss of Nef-induced CD4 down-modulation.|||Loss of homodimerization; when associated with A-445.|||Loss of homodimerization; when associated with A-447.|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine|||S-palmitoyl cysteine|||T cell CD4 receptor C-terminal region|||T-cell surface glycoprotein CD4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000053|||http://purl.uniprot.org/annotation/CAR_000054|||http://purl.uniprot.org/annotation/PRO_0000014621|||http://purl.uniprot.org/annotation/PRO_5021371852|||http://purl.uniprot.org/annotation/VAR_003906|||http://purl.uniprot.org/annotation/VAR_023459|||http://purl.uniprot.org/annotation/VAR_023460
http://togogenome.org/gene/9606:TGFBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TMH4|||http://purl.uniprot.org/uniprot/B4DXN7|||http://purl.uniprot.org/uniprot/P36897|||http://purl.uniprot.org/uniprot/Q5T7S2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Constitutive activation.|||Cytoplasmic|||Extracellular|||FKBP1A-binding|||GS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||In LDS1.|||In MSSE; hypomorphic variant.|||In a patient with Marfan syndrome.|||In allele TGFBR1*10A.|||In allele TGFBR1*6A; could be a tumor susceptibility allele.|||In isoform 2.|||In isoform 3.|||Loss of interaction with FKBP1A.|||Loss of phosphorylation on threonine residues. Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with A-187; A-189 and A-191.|||Loss of phosphorylation. Loss of response to TGF-beta.|||Loss of response to TGF-beta.|||Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-189.|||Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-191.|||Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-189 and A-191.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by TGFBR2|||Phosphothreonine; by TGFBR2|||Protein kinase|||Proton acceptor|||Reduced phosphorylation. Reduced response to TGF-beta.|||TGF-beta receptor type-1|||receptor protein serine/threonine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024423|||http://purl.uniprot.org/annotation/PRO_5002801077|||http://purl.uniprot.org/annotation/PRO_5014309963|||http://purl.uniprot.org/annotation/VAR_022342|||http://purl.uniprot.org/annotation/VAR_022343|||http://purl.uniprot.org/annotation/VAR_022344|||http://purl.uniprot.org/annotation/VAR_022345|||http://purl.uniprot.org/annotation/VAR_022346|||http://purl.uniprot.org/annotation/VAR_022347|||http://purl.uniprot.org/annotation/VAR_029481|||http://purl.uniprot.org/annotation/VAR_029482|||http://purl.uniprot.org/annotation/VAR_029483|||http://purl.uniprot.org/annotation/VAR_029484|||http://purl.uniprot.org/annotation/VAR_029485|||http://purl.uniprot.org/annotation/VAR_041412|||http://purl.uniprot.org/annotation/VAR_041413|||http://purl.uniprot.org/annotation/VAR_054160|||http://purl.uniprot.org/annotation/VAR_065826|||http://purl.uniprot.org/annotation/VAR_065827|||http://purl.uniprot.org/annotation/VAR_065828|||http://purl.uniprot.org/annotation/VAR_065829|||http://purl.uniprot.org/annotation/VAR_066720|||http://purl.uniprot.org/annotation/VAR_066721|||http://purl.uniprot.org/annotation/VAR_066722|||http://purl.uniprot.org/annotation/VSP_041326|||http://purl.uniprot.org/annotation/VSP_041327
http://togogenome.org/gene/9606:FBXO42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3S6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 42|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119942|||http://purl.uniprot.org/annotation/VAR_024447
http://togogenome.org/gene/9606:OR8B12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWS7|||http://purl.uniprot.org/uniprot/Q8NGG6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8B12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150658
http://togogenome.org/gene/9606:DMXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWN7|||http://purl.uniprot.org/uniprot/F1T0K4|||http://purl.uniprot.org/uniprot/F5H269|||http://purl.uniprot.org/uniprot/Q9Y485                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||DmX-like protein 1|||Phosphoserine|||RAVE complex protein Rav1 C-terminal|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 14|||WD 15|||WD 16|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223322|||http://purl.uniprot.org/annotation/VAR_057589|||http://purl.uniprot.org/annotation/VAR_057590|||http://purl.uniprot.org/annotation/VAR_057591|||http://purl.uniprot.org/annotation/VAR_057592
http://togogenome.org/gene/9606:LIN54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZP7|||http://purl.uniprot.org/uniprot/Q7Z3G2                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DNA-binding to the CDK1 promoter; when associated with Y-525.|||Abolishes DNA-binding to the CDK1 promoter; when associated with Y-527.|||CRC|||Critical for interaction with target DNA|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with DNA|||Linker|||Loss of DNA-binding.|||N6-acetyllysine|||Phosphoserine|||Protein lin-54 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341389|||http://purl.uniprot.org/annotation/VSP_034272|||http://purl.uniprot.org/annotation/VSP_034273|||http://purl.uniprot.org/annotation/VSP_034274|||http://purl.uniprot.org/annotation/VSP_034275|||http://purl.uniprot.org/annotation/VSP_034276
http://togogenome.org/gene/9606:PDXP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R1I3|||http://purl.uniprot.org/uniprot/Q96GD0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes protein phosphatase activity.|||Chronophin|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068837
http://togogenome.org/gene/9606:PDPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  29kDa cytosolic podoplanin intracellular domain|||Cleavage; by gamma-secretase|||Cytoplasmic|||Disordered|||Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively. Does not significant change RHOA activation. No effect on interaction with CD44. Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not change localization at invadopodium. Fails to assemble into rings. Fails invadopodia-mediated ECM degradation.|||Eliminates induction of platelet aggregation.|||Extracellular|||Helical|||Highly decreases interaction with the EZR and MSN. Induces an intermediate phenotype between epithelial and mesenchymal. Does not affect localization at cell surface protrusions. Induces reorganization of the actin cytoskeleton oncomitantly with the induced morphological changes. Increases cell migration individually. Increases invasiveness. Enhances RHOA activity. Colocalizes at cell-surface protrusions with RHOA and RAC1.|||Impairs interaction with the EZR and MSN. Impairs epithelial to mesenchymal transition. Does not affect localization at cell surface protrusions. Does not induce reorganization of the actin cytoskeleton. Increases cell migration collectively.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Podoplanin|||Prevents self-assembly and association to lipid rafts. Reduces the recruitment to invadopodium. Disrupts assembly into adhesion rings. Fails invadopodia-mediated ECM degradation.|||Requires for dimerization and lipid rafts association|||Requires for interaction with MSN and EZR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223875|||http://purl.uniprot.org/annotation/PRO_0000442187|||http://purl.uniprot.org/annotation/VAR_028015|||http://purl.uniprot.org/annotation/VAR_028016|||http://purl.uniprot.org/annotation/VSP_035753|||http://purl.uniprot.org/annotation/VSP_035754|||http://purl.uniprot.org/annotation/VSP_046799|||http://purl.uniprot.org/annotation/VSP_046800|||http://purl.uniprot.org/annotation/VSP_051949|||http://purl.uniprot.org/annotation/VSP_051950|||http://purl.uniprot.org/annotation/VSP_051951
http://togogenome.org/gene/9606:THRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10827|||http://purl.uniprot.org/uniprot/Q6FH41                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In CHNG6) (Ref.26.|||In CHNG6, decreases transcriptional activity, decreases T3 binding) (Ref.25.|||In CHNG6, reduces T3 binding, impairs thyroid hormone-dependent transcriptional activation, no effect on DNA-binding) (Ref.24.|||In CHNG6; atypical phenotype; weak reduction in transcriptional activation.|||In CHNG6; no effect on T3 binding; no effect on thyroid hormone-dependent transcriptional activation.|||In isoform Alpha-1.|||In isoform Alpha-3.|||In isoform Alpha-4.|||Modulating|||NR C4-type|||NR LBD|||No effect on thyroid hormone binding.|||Nuclear receptor|||Thyroid hormone receptor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053424|||http://purl.uniprot.org/annotation/VAR_074559|||http://purl.uniprot.org/annotation/VAR_074560|||http://purl.uniprot.org/annotation/VAR_082873|||http://purl.uniprot.org/annotation/VAR_082874|||http://purl.uniprot.org/annotation/VAR_082875|||http://purl.uniprot.org/annotation/VAR_082876|||http://purl.uniprot.org/annotation/VSP_003621|||http://purl.uniprot.org/annotation/VSP_003622|||http://purl.uniprot.org/annotation/VSP_003623
http://togogenome.org/gene/9606:RNF19A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV58                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-132.|||Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-135.|||Disordered|||E3 ubiquitin-protein ligase RNF19A|||Helical|||IBR-type|||In isoform 2.|||In isoform 3.|||Interaction with CASR|||Phosphoserine|||Polar residues|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056061|||http://purl.uniprot.org/annotation/VAR_028045|||http://purl.uniprot.org/annotation/VSP_021010|||http://purl.uniprot.org/annotation/VSP_021011|||http://purl.uniprot.org/annotation/VSP_028631
http://togogenome.org/gene/9606:AXL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R0W6|||http://purl.uniprot.org/uniprot/P30530                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytically inactive mutant.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform Short.|||Interaction with GAS6|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced affinity for GAS6.|||Slightly reduced affinity for GAS6.|||Tyrosine-protein kinase receptor UFO                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024481|||http://purl.uniprot.org/annotation/VAR_041877|||http://purl.uniprot.org/annotation/VAR_041878|||http://purl.uniprot.org/annotation/VAR_045596|||http://purl.uniprot.org/annotation/VAR_045597|||http://purl.uniprot.org/annotation/VAR_057990|||http://purl.uniprot.org/annotation/VSP_005017
http://togogenome.org/gene/9606:METAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53582                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C6H2-type|||Methionine aminopeptidase 1|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148967
http://togogenome.org/gene/9606:GRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L2P9|||http://purl.uniprot.org/uniprot/Q13588                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||GRB2-related adapter protein|||In DFNB114.|||Polar residues|||SH2|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088206|||http://purl.uniprot.org/annotation/VAR_082111
http://togogenome.org/gene/9606:TTC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DKK2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Cleavage; by PARL|||Mitochondrion|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||Tetratricopeptide repeat protein 19, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106407
http://togogenome.org/gene/9606:ANO9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5B4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin-9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289329|||http://purl.uniprot.org/annotation/VAR_032617|||http://purl.uniprot.org/annotation/VAR_032618|||http://purl.uniprot.org/annotation/VAR_054621|||http://purl.uniprot.org/annotation/VSP_036489|||http://purl.uniprot.org/annotation/VSP_036490|||http://purl.uniprot.org/annotation/VSP_036491|||http://purl.uniprot.org/annotation/VSP_036492
http://togogenome.org/gene/9606:SIDT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBJ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||SID1 transmembrane family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032578|||http://purl.uniprot.org/annotation/VAR_034493|||http://purl.uniprot.org/annotation/VAR_034494|||http://purl.uniprot.org/annotation/VSP_013523|||http://purl.uniprot.org/annotation/VSP_013524
http://togogenome.org/gene/9606:CFAP107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1D5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247260
http://togogenome.org/gene/9606:ZNF792                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KQV3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Phosphoserine|||Zinc finger protein 792                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293698|||http://purl.uniprot.org/annotation/VAR_033106|||http://purl.uniprot.org/annotation/VAR_047354
http://togogenome.org/gene/9606:STRADB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0K7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Protein kinase|||STE20-related kinase adapter protein beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085617|||http://purl.uniprot.org/annotation/VAR_041335|||http://purl.uniprot.org/annotation/VAR_041336|||http://purl.uniprot.org/annotation/VSP_016623|||http://purl.uniprot.org/annotation/VSP_016624|||http://purl.uniprot.org/annotation/VSP_016625
http://togogenome.org/gene/9606:CYCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P99999                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome c|||Decreased covalent heme attachment.|||In THC4; increases the pro-apoptotic function by triggering caspase activation more efficiently than wild-type; does not affect the redox function.|||Loss of covalent heme attachment.|||N-acetylglycine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on covalent heme attachment.|||Phosphotyrosine|||Removed|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000108218|||http://purl.uniprot.org/annotation/VAR_002204|||http://purl.uniprot.org/annotation/VAR_044450|||http://purl.uniprot.org/annotation/VAR_048850
http://togogenome.org/gene/9606:CREG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75629                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Protein CREG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006203
http://togogenome.org/gene/9606:SCIMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Inhibits interaction with BLNK. Inhibits activation of several downstream signaling pathways.|||Inhibits interaction with CSK. Stimulates activation of several downstream signaling pathways.|||Inhibits interaction with GRB2.|||Inhibits interaction with LYN.|||Interaction with TLR4|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Proline-rich region necessary for constitutive interaction with LYN|||S-palmitoyl cysteine|||SLP adapter and CSK-interacting membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295237|||http://purl.uniprot.org/annotation/VSP_026853|||http://purl.uniprot.org/annotation/VSP_026854|||http://purl.uniprot.org/annotation/VSP_026855
http://togogenome.org/gene/9606:EBAG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00559                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Receptor-binding cancer antigen expressed on SiSo cells                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097195|||http://purl.uniprot.org/annotation/VSP_055503
http://togogenome.org/gene/9606:GSTM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21266|||http://purl.uniprot.org/uniprot/Q6FGJ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||No effect.|||Strongly increased catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185822|||http://purl.uniprot.org/annotation/VAR_014498
http://togogenome.org/gene/9606:SLC35B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Mediates endoplasmic reticulum retention|||Nucleotide sugar transporter SLC35B4|||Results in loss of ER retention signal and relocalization at the Golgi apparatus.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213385|||http://purl.uniprot.org/annotation/VSP_016197|||http://purl.uniprot.org/annotation/VSP_016198|||http://purl.uniprot.org/annotation/VSP_016199|||http://purl.uniprot.org/annotation/VSP_016200
http://togogenome.org/gene/9606:ZNF324B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AW86                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 324B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280405|||http://purl.uniprot.org/annotation/VAR_052811|||http://purl.uniprot.org/annotation/VSP_023658
http://togogenome.org/gene/9606:XPNPEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6H7|||http://purl.uniprot.org/uniprot/Q9NQW7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Creatinase N-terminal|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interferes with dimerization and reduces activity by 94%.|||N6-acetyllysine|||Peptidase M24|||Peptidase M24 C-terminal|||Reduces activity by 10%.|||Removed|||Xaa-Pro aminopeptidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185083|||http://purl.uniprot.org/annotation/VSP_045250|||http://purl.uniprot.org/annotation/VSP_051752
http://togogenome.org/gene/9606:PRSS54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC3|||http://purl.uniprot.org/uniprot/F5H6C6|||http://purl.uniprot.org/uniprot/Q6PEW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Inactive serine protease 54|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288801|||http://purl.uniprot.org/annotation/PRO_5007491757|||http://purl.uniprot.org/annotation/VAR_032497|||http://purl.uniprot.org/annotation/VAR_032498|||http://purl.uniprot.org/annotation/VAR_032499
http://togogenome.org/gene/9606:RBBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLF8|||http://purl.uniprot.org/uniprot/Q15291                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with ASH2L|||Interaction with WDR5|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1|||Polar residues|||Reduced ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L.|||Retinoblastoma-binding protein 5|||Significant reduction in its ability to stimulate KMT2A methyltransferase activity in association with WDR5 and ASH2L.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051194|||http://purl.uniprot.org/annotation/VSP_035583
http://togogenome.org/gene/9606:ZSWIM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCJ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In AFND.|||In NEDMAGA.|||SWIM-type|||Zinc finger SWIM domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223105|||http://purl.uniprot.org/annotation/VAR_071802|||http://purl.uniprot.org/annotation/VAR_076431|||http://purl.uniprot.org/annotation/VAR_080756
http://togogenome.org/gene/9606:DGAT2L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZPD8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Diacylglycerol O-acyltransferase 2-like protein 6|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249054
http://togogenome.org/gene/9606:FGF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JW12|||http://purl.uniprot.org/uniprot/P08620                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fibroblast growth factor|||Fibroblast growth factor 4|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008953|||http://purl.uniprot.org/annotation/PRO_5034192521|||http://purl.uniprot.org/annotation/VSP_053541
http://togogenome.org/gene/9606:CES3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFY7|||http://purl.uniprot.org/uniprot/Q6UWW8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acyl-ester intermediate|||Carboxylesterase 3|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305191|||http://purl.uniprot.org/annotation/PRO_5014203187|||http://purl.uniprot.org/annotation/VAR_060699|||http://purl.uniprot.org/annotation/VAR_060700|||http://purl.uniprot.org/annotation/VAR_060701|||http://purl.uniprot.org/annotation/VAR_060702|||http://purl.uniprot.org/annotation/VAR_060703|||http://purl.uniprot.org/annotation/VAR_060704|||http://purl.uniprot.org/annotation/VAR_060705|||http://purl.uniprot.org/annotation/VAR_060706|||http://purl.uniprot.org/annotation/VSP_044994
http://togogenome.org/gene/9606:MTFR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3G8|||http://purl.uniprot.org/uniprot/Q15390                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondrial fission regulator 1|||Mitochondrion|||Necessary and sufficient to promote mitochondrial fission|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096622|||http://purl.uniprot.org/annotation/VSP_046765
http://togogenome.org/gene/9606:SPATA25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR10                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Spermatogenesis-associated protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079478|||http://purl.uniprot.org/annotation/VAR_015146
http://togogenome.org/gene/9606:TTC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPL4|||http://purl.uniprot.org/uniprot/Q8NBP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||Tetratricopeptide repeat protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106398|||http://purl.uniprot.org/annotation/VSP_011644|||http://purl.uniprot.org/annotation/VSP_035660
http://togogenome.org/gene/9606:HEATR5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H619|||http://purl.uniprot.org/uniprot/Q86XA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT repeat-containing protein 5A|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311990|||http://purl.uniprot.org/annotation/VSP_029685|||http://purl.uniprot.org/annotation/VSP_029686
http://togogenome.org/gene/9606:ZXDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98168                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Required for interaction with ZXDC|||Required for transcriptional activation|||Zinc finger X-linked protein ZXDA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047776|||http://purl.uniprot.org/annotation/VAR_033002|||http://purl.uniprot.org/annotation/VAR_076439
http://togogenome.org/gene/9606:CCNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14635                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Does not affect phosphorylation by PLK1.|||G2/mitotic-specific cyclin-B1|||In isoform 2.|||Interaction with CDK2|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Strongly impairs phosphorylation by PLK1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080350|||http://purl.uniprot.org/annotation/VSP_053892
http://togogenome.org/gene/9606:TEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10587                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||In isoform 2.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Thyrotroph embryonic factor|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076512|||http://purl.uniprot.org/annotation/VSP_041376
http://togogenome.org/gene/9606:EVA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVM1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphothreonine|||Protein eva-1 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271112
http://togogenome.org/gene/9606:NOL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Nucleolar protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271207
http://togogenome.org/gene/9606:MARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56192                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Found in a patient with spastic paraplegia; unknown pathological significance.|||GST C-terminal|||In CMT2U.|||In CMT2U; loss of function mutation.|||In ILLD.|||In ILLD; may act as a disease modifier aggravating the phenotype; found in patients that carried additional mutations C-344 and/or L-567; when assayed in yeast, does not exhibit any phenotype; when assayed in yeast in association with L-567, increases L-567-induced growth retardation and reduction in methionine incorporation.|||In ILLD; when assayed in yeast, induces a slight growth retardation and reduction in methionine incorporation; may interfere with efficient substrate binding.|||In ILLD; when assayed in yeast, reduces methionine incorporation; when assayed in yeast in association with T-393, induces growth retardation and strong reduction in methionine incorporation; may interfere with efficient substrate binding.|||In TTD9; unknown pathological significance; homozygous patient cells show decreased methionyl-tRNA aminoacylation; decreased protein abundance in homozygous patient cells.|||In isoform 2.|||Loss of interaction with EEF1E1.|||Methionine--tRNA ligase, cytoplasmic|||No effect on enzyme activity.|||Phosphoserine|||Phosphothreonine|||Slightly decreased enzyme activity.|||Strongly decreased affinity for tRNA.|||WHEP-TRS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139262|||http://purl.uniprot.org/annotation/VAR_020459|||http://purl.uniprot.org/annotation/VAR_070872|||http://purl.uniprot.org/annotation/VAR_070873|||http://purl.uniprot.org/annotation/VAR_073377|||http://purl.uniprot.org/annotation/VAR_073378|||http://purl.uniprot.org/annotation/VAR_075360|||http://purl.uniprot.org/annotation/VAR_075361|||http://purl.uniprot.org/annotation/VAR_075362|||http://purl.uniprot.org/annotation/VAR_075363|||http://purl.uniprot.org/annotation/VAR_075364|||http://purl.uniprot.org/annotation/VAR_075365|||http://purl.uniprot.org/annotation/VAR_077848|||http://purl.uniprot.org/annotation/VAR_077849|||http://purl.uniprot.org/annotation/VAR_086779|||http://purl.uniprot.org/annotation/VSP_056563|||http://purl.uniprot.org/annotation/VSP_056564
http://togogenome.org/gene/9606:GOLGA8O                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCC3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8O|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342409|||http://purl.uniprot.org/annotation/VSP_044760|||http://purl.uniprot.org/annotation/VSP_044761|||http://purl.uniprot.org/annotation/VSP_044762
http://togogenome.org/gene/9606:TRIM68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AZZ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM68|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249437|||http://purl.uniprot.org/annotation/VAR_027415|||http://purl.uniprot.org/annotation/VAR_063007|||http://purl.uniprot.org/annotation/VAR_063008|||http://purl.uniprot.org/annotation/VSP_055444|||http://purl.uniprot.org/annotation/VSP_055445
http://togogenome.org/gene/9606:ARL4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49703                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 4D|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207464|||http://purl.uniprot.org/annotation/VAR_028205
http://togogenome.org/gene/9606:MAP3K19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56UN5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 7.|||Mitogen-activated protein kinase kinase kinase 19|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232640|||http://purl.uniprot.org/annotation/VAR_041334|||http://purl.uniprot.org/annotation/VAR_051687|||http://purl.uniprot.org/annotation/VAR_051688|||http://purl.uniprot.org/annotation/VAR_051689|||http://purl.uniprot.org/annotation/VSP_017924|||http://purl.uniprot.org/annotation/VSP_017925|||http://purl.uniprot.org/annotation/VSP_017926|||http://purl.uniprot.org/annotation/VSP_055367
http://togogenome.org/gene/9606:SGCZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AT0|||http://purl.uniprot.org/uniprot/Q96LD1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Zeta-sarcoglycan                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175251|||http://purl.uniprot.org/annotation/VSP_037410
http://togogenome.org/gene/9606:HYPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX55                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NAA10 and NAA15.|||Basic and acidic residues|||Disordered|||Huntingtin-interacting protein K|||In isoform 3.|||Phosphoserine|||Reduces ability to inhibit NAA10-NAA15 complex-mediated N-terminal acetylation, which results in increased N-terminal acetylation.|||Reduces ability to inhibit NAA10-NAA15 complex-mediated N-terminal acetylation, which results in increased N-terminal acetylation; when associated with A-35.|||Reduces ability to inhibit NAA10-NAA15 complex-mediated N-terminal acetylation, which results in increased N-terminal acetylation; when associated with A-38.|||Required for association with the NAA10-NAA15 complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274605|||http://purl.uniprot.org/annotation/VAR_030335|||http://purl.uniprot.org/annotation/VSP_040677|||http://purl.uniprot.org/annotation/VSP_040678
http://togogenome.org/gene/9606:DSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKX6|||http://purl.uniprot.org/uniprot/P15924|||http://purl.uniprot.org/uniprot/Q4LE79                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4.5 X 38 AA tandem repeats (Domain A)|||4.5 X 38 AA tandem repeats (Domain B)|||4.5 X 38 AA tandem repeats (Domain C)|||6 X 4 AA tandem repeats of G-S-R-[SR]|||Central fibrous rod domain|||Desmoplakin|||Disordered|||Globular 1|||Globular 2|||In ARVD8.|||In ARVD8; unknown pathological significance.|||In DCWHKTA.|||In SFWHS.|||In a case of recessive arrhythmogenic right ventricular cardiomyopathy with skin abnormalities and woolly hair.|||In isoform DPII.|||In isoform DSPIa.|||Interaction with PKP1, JUP, PKP2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Plectin 1|||Plectin 10|||Plectin 11|||Plectin 12|||Plectin 13|||Plectin 14|||Plectin 15|||Plectin 16|||Plectin 17|||Plectin 2|||Plectin 3|||Plectin 4|||Plectin 5|||Plectin 6|||Plectin 7|||Plectin 8|||Plectin 9|||Polar residues|||SH3|||Spectrin 1|||Spectrin 2|||Spectrin 3a|||Spectrin 3b|||Spectrin 4|||Spectrin 5|||Spectrin 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078144|||http://purl.uniprot.org/annotation/VAR_015402|||http://purl.uniprot.org/annotation/VAR_015569|||http://purl.uniprot.org/annotation/VAR_015570|||http://purl.uniprot.org/annotation/VAR_018158|||http://purl.uniprot.org/annotation/VAR_020468|||http://purl.uniprot.org/annotation/VAR_023814|||http://purl.uniprot.org/annotation/VAR_023815|||http://purl.uniprot.org/annotation/VAR_023816|||http://purl.uniprot.org/annotation/VAR_033862|||http://purl.uniprot.org/annotation/VAR_065693|||http://purl.uniprot.org/annotation/VAR_065694|||http://purl.uniprot.org/annotation/VAR_065695|||http://purl.uniprot.org/annotation/VAR_065696|||http://purl.uniprot.org/annotation/VAR_065697|||http://purl.uniprot.org/annotation/VAR_072432|||http://purl.uniprot.org/annotation/VAR_072433|||http://purl.uniprot.org/annotation/VSP_005070|||http://purl.uniprot.org/annotation/VSP_053769
http://togogenome.org/gene/9606:GCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01275                                                                                  ^@                                                                                  Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Arginine amide|||Cleavage; by PCSK1|||Cleavage; by PCSK1 and PCSK2|||Cleavage; by PCSK2|||Disordered|||Glicentin|||Glicentin-related polypeptide|||Glucagon|||Glucagon-like peptide 1|||Glucagon-like peptide 1(7-36)|||Glucagon-like peptide 1(7-37)|||Glucagon-like peptide 2|||Oxyntomodulin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011253|||http://purl.uniprot.org/annotation/PRO_0000011254|||http://purl.uniprot.org/annotation/PRO_0000011255|||http://purl.uniprot.org/annotation/PRO_0000011256|||http://purl.uniprot.org/annotation/PRO_0000011257|||http://purl.uniprot.org/annotation/PRO_0000011258|||http://purl.uniprot.org/annotation/PRO_0000011259|||http://purl.uniprot.org/annotation/PRO_0000011260|||http://purl.uniprot.org/annotation/PRO_0000011261|||http://purl.uniprot.org/annotation/PRO_0000011262|||http://purl.uniprot.org/annotation/VAR_014596
http://togogenome.org/gene/9606:SOX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H0I3|||http://purl.uniprot.org/uniprot/P35711|||http://purl.uniprot.org/uniprot/T2CYZ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||HMG box|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor SOX-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048726|||http://purl.uniprot.org/annotation/VAR_065754|||http://purl.uniprot.org/annotation/VSP_007261|||http://purl.uniprot.org/annotation/VSP_007262|||http://purl.uniprot.org/annotation/VSP_007263|||http://purl.uniprot.org/annotation/VSP_007264|||http://purl.uniprot.org/annotation/VSP_045997
http://togogenome.org/gene/9606:ATF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D7V5|||http://purl.uniprot.org/uniprot/P15336                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BZIP|||Basic and acidic residues|||Basic motif|||C2H2-type|||Cyclic AMP-dependent transcription factor ATF-2|||Disordered|||Essential for its histone acetyltransferase activity|||Impairs phosphorylation by PLK3. Weak histone acetyltransferase activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6 and isoform 8.|||In isoform 7.|||Leucine-zipper|||N6-acetyllysine|||Nuclear export signal 1 (N-NES)|||Nuclear export signal 2 (C-NES)|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by PKC/PRKCA and PKC/PRKCB|||Phosphoserine; by VRK1|||Phosphothreonine|||Phosphothreonine; by MAPK1, MAPK3, MAPK11, MAPK12, MAPK14 and PLK3|||Phosphothreonine; by MAPK11 and MAPK14|||Phosphothreonine; by PKC/PRKCH|||Phosphothreonine; by VRK1|||Polar residues|||Reduced phosphorylation and repression of c-Jun-mediated activation of transcription.|||Weak histone acetyltransferase activity.|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076577|||http://purl.uniprot.org/annotation/VAR_035999|||http://purl.uniprot.org/annotation/VSP_000587|||http://purl.uniprot.org/annotation/VSP_000588|||http://purl.uniprot.org/annotation/VSP_045161|||http://purl.uniprot.org/annotation/VSP_046959|||http://purl.uniprot.org/annotation/VSP_046960|||http://purl.uniprot.org/annotation/VSP_047593|||http://purl.uniprot.org/annotation/VSP_047594|||http://purl.uniprot.org/annotation/VSP_047595
http://togogenome.org/gene/9606:KNOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1ED39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with ZNF106|||Lysine-rich nucleolar protein 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321938|||http://purl.uniprot.org/annotation/VAR_039387|||http://purl.uniprot.org/annotation/VAR_061716|||http://purl.uniprot.org/annotation/VAR_061717
http://togogenome.org/gene/9606:FARP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0TVY0|||http://purl.uniprot.org/uniprot/C9JME2|||http://purl.uniprot.org/uniprot/Q9Y4F1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||FERM|||FERM, ARHGEF and pleckstrin domain-containing protein 1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232753|||http://purl.uniprot.org/annotation/VAR_035851|||http://purl.uniprot.org/annotation/VAR_048362|||http://purl.uniprot.org/annotation/VSP_017976|||http://purl.uniprot.org/annotation/VSP_040989|||http://purl.uniprot.org/annotation/VSP_040990
http://togogenome.org/gene/9606:POSTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALD9|||http://purl.uniprot.org/uniprot/Q15063                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EMI|||FAS1|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 7.|||In isoform 6 and isoform 7.|||Loss of homodimerization.|||N-linked (GlcNAc...) asparagine|||No effect on homodimerization.|||Periostin|||S-cysteinyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008789|||http://purl.uniprot.org/annotation/PRO_5002761412|||http://purl.uniprot.org/annotation/VAR_049115|||http://purl.uniprot.org/annotation/VAR_049116|||http://purl.uniprot.org/annotation/VSP_050005|||http://purl.uniprot.org/annotation/VSP_050669|||http://purl.uniprot.org/annotation/VSP_050670|||http://purl.uniprot.org/annotation/VSP_055183
http://togogenome.org/gene/9606:ZC3H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPT8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234068|||http://purl.uniprot.org/annotation/VAR_052964|||http://purl.uniprot.org/annotation/VAR_052965|||http://purl.uniprot.org/annotation/VAR_052966
http://togogenome.org/gene/9606:RBM39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NQ03|||http://purl.uniprot.org/uniprot/B4DRA0|||http://purl.uniprot.org/uniprot/Q14498                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activating domain|||Associated with resistance to anticancer indisulam.|||Associated with resistance to anticancer indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam.|||Associated with resistance to anticancer indisulam; decreased interaction with the DCX(DCAF15) complex in presence of indisulam; abolished degradation by the DCX(DCAF15) complex in presence of indisulam.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with ESR1 and ESR2|||Interaction with JUN|||Interaction with NCOA6|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RNA-binding protein 39|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081814|||http://purl.uniprot.org/annotation/VAR_015228|||http://purl.uniprot.org/annotation/VAR_083212|||http://purl.uniprot.org/annotation/VAR_083213|||http://purl.uniprot.org/annotation/VAR_083214|||http://purl.uniprot.org/annotation/VAR_083215|||http://purl.uniprot.org/annotation/VAR_083216|||http://purl.uniprot.org/annotation/VAR_083217|||http://purl.uniprot.org/annotation/VAR_083218|||http://purl.uniprot.org/annotation/VAR_083219|||http://purl.uniprot.org/annotation/VSP_005820|||http://purl.uniprot.org/annotation/VSP_043375
http://togogenome.org/gene/9606:ZRANB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95218                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RanBP2-type 1|||RanBP2-type 2|||Required for nuclear targeting|||Zinc finger Ran-binding domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066585|||http://purl.uniprot.org/annotation/VAR_030783|||http://purl.uniprot.org/annotation/VSP_024945
http://togogenome.org/gene/9606:UBE2N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61088|||http://purl.uniprot.org/uniprot/V9HW41                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Glycyl thioester intermediate|||Interchain (with C-78 in ISG15)|||Loss of polyubiquitination of PCNA. Impairs interaction with SHPRH.|||N6-acetyllysine|||No ISGylation.|||No effect on ISGylation.|||UBC core|||Ubiquitin-conjugating enzyme E2 N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082502
http://togogenome.org/gene/9606:TMEM53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TDE2|||http://purl.uniprot.org/uniprot/Q6P2H8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284118|||http://purl.uniprot.org/annotation/VSP_024446
http://togogenome.org/gene/9606:NKX2-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95096                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-2.2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048929
http://togogenome.org/gene/9606:CORO2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ03                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coronin-2B|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050930|||http://purl.uniprot.org/annotation/VAR_035878|||http://purl.uniprot.org/annotation/VAR_058323|||http://purl.uniprot.org/annotation/VSP_037706
http://togogenome.org/gene/9606:INTS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N11                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Integrator complex subunit 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089582|||http://purl.uniprot.org/annotation/VAR_061593|||http://purl.uniprot.org/annotation/VSP_007907|||http://purl.uniprot.org/annotation/VSP_007908
http://togogenome.org/gene/9606:MIEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C03                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In COXPD49; patient cells have reduced MIEF2 protein levels and show elongated mitochondria and increased mitochondrial fusion events.|||In isoform 2.|||In isoform 3.|||Mitochondrial dynamics protein MID49|||Mitochondrial intermembrane|||Phosphoserine|||Unable to associate with DNM1L into filaments forming the tubular structures that wrap around the scission site.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310445|||http://purl.uniprot.org/annotation/VAR_037038|||http://purl.uniprot.org/annotation/VAR_037039|||http://purl.uniprot.org/annotation/VAR_081553|||http://purl.uniprot.org/annotation/VSP_029358|||http://purl.uniprot.org/annotation/VSP_029359|||http://purl.uniprot.org/annotation/VSP_047650
http://togogenome.org/gene/9606:CRYBG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPT0|||http://purl.uniprot.org/uniprot/Q9Y4K1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 10|||Beta/gamma crystallin 'Greek key' 11|||Beta/gamma crystallin 'Greek key' 12|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Beta/gamma crystallin 'Greek key' 5|||Beta/gamma crystallin 'Greek key' 6|||Beta/gamma crystallin 'Greek key' 7|||Beta/gamma crystallin 'Greek key' 8|||Beta/gamma crystallin 'Greek key' 9|||Beta/gamma crystallin domain-containing protein 1|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057609|||http://purl.uniprot.org/annotation/VAR_055687|||http://purl.uniprot.org/annotation/VAR_055688|||http://purl.uniprot.org/annotation/VAR_055689|||http://purl.uniprot.org/annotation/VAR_055690|||http://purl.uniprot.org/annotation/VAR_055691|||http://purl.uniprot.org/annotation/VAR_055692|||http://purl.uniprot.org/annotation/VAR_055693|||http://purl.uniprot.org/annotation/VSP_056580|||http://purl.uniprot.org/annotation/VSP_056581
http://togogenome.org/gene/9606:NPTX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47972                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Neuronal pentraxin-2|||Pentraxin (PTX)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023551
http://togogenome.org/gene/9606:LRRC59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AG4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 59|||Leucine-rich repeat-containing protein 59, N-terminally processed|||Lumenal|||N-acetylmethionine|||N-acetylthreonine; in Leucine-rich repeat-containing protein 59, N-terminally processed|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235159|||http://purl.uniprot.org/annotation/PRO_0000441739
http://togogenome.org/gene/9606:STARD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R789|||http://purl.uniprot.org/uniprot/B3KRK6|||http://purl.uniprot.org/uniprot/Q9Y3M8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of RhoGAP activity.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Rho-GAP|||SAM|||START|||StAR-related lipid transfer protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220679|||http://purl.uniprot.org/annotation/VAR_022098|||http://purl.uniprot.org/annotation/VAR_037494|||http://purl.uniprot.org/annotation/VAR_037495|||http://purl.uniprot.org/annotation/VAR_037496|||http://purl.uniprot.org/annotation/VSP_017353|||http://purl.uniprot.org/annotation/VSP_017354|||http://purl.uniprot.org/annotation/VSP_017355|||http://purl.uniprot.org/annotation/VSP_017356|||http://purl.uniprot.org/annotation/VSP_017357
http://togogenome.org/gene/9606:TRNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q11                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolished homodimerization and disulfide bond formation.|||CCA tRNA nucleotidyltransferase 1, mitochondrial|||Decreased CCA tRNA nucleotidyltransferase activity; abolished homodimerization and disulfide bond formation.|||In RPEM.|||In SIFD.|||In SIFD; decreased CCA tRNA nucleotidyltransferase activity; abolished homodimerization and disulfide bond formation.|||In SIFD; loss of CCA tRNA nucleotidyltransferase activity.|||In SIFD; loss of CCA tRNA nucleotidyltransferase activity; decreased stability.|||In SIFD; reduced CCA tRNA nucleotidyltransferasevactivity; decreased stability.|||In SIFD; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interchain|||Involved in nucleotide selection|||May assist in discriminating ATP from CTP|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004782|||http://purl.uniprot.org/annotation/VAR_048698|||http://purl.uniprot.org/annotation/VAR_072421|||http://purl.uniprot.org/annotation/VAR_072422|||http://purl.uniprot.org/annotation/VAR_072423|||http://purl.uniprot.org/annotation/VAR_072424|||http://purl.uniprot.org/annotation/VAR_072425|||http://purl.uniprot.org/annotation/VAR_072426|||http://purl.uniprot.org/annotation/VAR_072427|||http://purl.uniprot.org/annotation/VAR_076924|||http://purl.uniprot.org/annotation/VAR_088001|||http://purl.uniprot.org/annotation/VAR_088002|||http://purl.uniprot.org/annotation/VAR_088003|||http://purl.uniprot.org/annotation/VAR_088004|||http://purl.uniprot.org/annotation/VAR_088005|||http://purl.uniprot.org/annotation/VAR_088006|||http://purl.uniprot.org/annotation/VAR_088007|||http://purl.uniprot.org/annotation/VAR_088008|||http://purl.uniprot.org/annotation/VAR_088009|||http://purl.uniprot.org/annotation/VAR_088010|||http://purl.uniprot.org/annotation/VAR_088011|||http://purl.uniprot.org/annotation/VAR_088012|||http://purl.uniprot.org/annotation/VAR_088013|||http://purl.uniprot.org/annotation/VAR_088014|||http://purl.uniprot.org/annotation/VAR_088015|||http://purl.uniprot.org/annotation/VSP_008440|||http://purl.uniprot.org/annotation/VSP_008441|||http://purl.uniprot.org/annotation/VSP_008442
http://togogenome.org/gene/9606:AMPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01432                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP deaminase 3|||Disordered|||In AMPDDE.|||In AMPDDE; enzyme inactive.|||In isoform 1A and isoform 2.|||In isoform 1A.|||In isoform 1C and isoform 3.|||In isoform 1C.|||In isoform 4.|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194410|||http://purl.uniprot.org/annotation/VAR_009881|||http://purl.uniprot.org/annotation/VAR_033499|||http://purl.uniprot.org/annotation/VAR_042606|||http://purl.uniprot.org/annotation/VAR_042607|||http://purl.uniprot.org/annotation/VAR_042608|||http://purl.uniprot.org/annotation/VAR_042609|||http://purl.uniprot.org/annotation/VAR_042610|||http://purl.uniprot.org/annotation/VAR_042611|||http://purl.uniprot.org/annotation/VAR_042612|||http://purl.uniprot.org/annotation/VAR_042613|||http://purl.uniprot.org/annotation/VAR_042614|||http://purl.uniprot.org/annotation/VAR_042615|||http://purl.uniprot.org/annotation/VSP_001275|||http://purl.uniprot.org/annotation/VSP_001276|||http://purl.uniprot.org/annotation/VSP_001277|||http://purl.uniprot.org/annotation/VSP_001278|||http://purl.uniprot.org/annotation/VSP_044230
http://togogenome.org/gene/9606:LMO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61968                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  LIM domain transcription factor LMO4|||LIM zinc-binding 1|||LIM zinc-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075820
http://togogenome.org/gene/9606:LIPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8L5|||http://purl.uniprot.org/uniprot/P11150                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Essential for determining substrate specificity|||Hepatic triacylglycerol lipase|||In HL deficiency.|||Increased triglyceride hydrolase and reduced phospholipase activity.|||Loss of triglyceride hydrolase and phospholipase activity.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017769|||http://purl.uniprot.org/annotation/PRO_5002698104|||http://purl.uniprot.org/annotation/VAR_004206|||http://purl.uniprot.org/annotation/VAR_004207|||http://purl.uniprot.org/annotation/VAR_004208|||http://purl.uniprot.org/annotation/VAR_004209|||http://purl.uniprot.org/annotation/VAR_004210|||http://purl.uniprot.org/annotation/VAR_014179|||http://purl.uniprot.org/annotation/VAR_017024|||http://purl.uniprot.org/annotation/VAR_017025|||http://purl.uniprot.org/annotation/VAR_017026
http://togogenome.org/gene/9606:BNC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z885|||http://purl.uniprot.org/uniprot/F5GY04|||http://purl.uniprot.org/uniprot/Q01954                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Hydrophobic|||In POF16; unknown pathological significance; affects nuclear localization; the mutant exhibits a punctate localization in the nucleus.|||No effect on phosphorylation, no effect on subcellular location.|||No effect on phosphorylation. Abolishes phosphorylation and induces nuclear restriction; when associated with A-541.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Reduces phosphorylation and induces partial relocation into the cytoplasm.|||Strongly reduces phosphorylation and induces partial relocation into the cytoplasm.|||Strongly reduces phosphorylation. Abolishes phosphorylation and induces nuclear restriction; when associated with A-537.|||Zinc finger protein basonuclin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046932|||http://purl.uniprot.org/annotation/PRO_5002866266|||http://purl.uniprot.org/annotation/PRO_5003322980|||http://purl.uniprot.org/annotation/VAR_083487
http://togogenome.org/gene/9606:FRMD4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW91|||http://purl.uniprot.org/uniprot/Q9P2Q2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||FERM domain-containing protein 4A|||Necessary for interaction with CYTH1|||Necessary for tight junction and adherens junction localization; Requires for interaction with PARD3|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219444|||http://purl.uniprot.org/annotation/VAR_048367
http://togogenome.org/gene/9606:TMED8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PL24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||GOLD|||N6-acetyllysine|||Protein TMED8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055638|||http://purl.uniprot.org/annotation/VAR_049112
http://togogenome.org/gene/9606:INSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01101                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Inhibits weakly translational repression activity. Inhibits interaction with CCND1 and cell cycle arrest.|||Insulinoma-associated protein 1|||Necessary for interaction with CCND1|||Pro residues|||Required and sufficient for interaction with KDM1A|||SNAG domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047268
http://togogenome.org/gene/9606:SH3PXD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPL1|||http://purl.uniprot.org/uniprot/Q5TCZ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2).|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 and PX domain-containing protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278488|||http://purl.uniprot.org/annotation/VAR_030781|||http://purl.uniprot.org/annotation/VAR_030782|||http://purl.uniprot.org/annotation/VAR_056993|||http://purl.uniprot.org/annotation/VSP_023312|||http://purl.uniprot.org/annotation/VSP_023313
http://togogenome.org/gene/9606:PEX5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||PEX5-related protein|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106317|||http://purl.uniprot.org/annotation/VAR_035865|||http://purl.uniprot.org/annotation/VSP_010435|||http://purl.uniprot.org/annotation/VSP_010436|||http://purl.uniprot.org/annotation/VSP_044743|||http://purl.uniprot.org/annotation/VSP_045136|||http://purl.uniprot.org/annotation/VSP_046976|||http://purl.uniprot.org/annotation/VSP_046977|||http://purl.uniprot.org/annotation/VSP_046978
http://togogenome.org/gene/9606:OPN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6U736                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Opsin-5|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197817
http://togogenome.org/gene/9606:PRAMEF33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JMD5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440971
http://togogenome.org/gene/9606:MINDY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBR6                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||No effect on binding to 'Lys-48'- or 'Lys-63'-tetraubiquitin chains.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||Strongly decreased binding to 'Lys-48' or 'Lys-63'-tetraubiquitin chains.|||Ubiquitin carboxyl-terminal hydrolase MINDY-2|||Ubiquitin-binding|||Ubiquitin-binding domain (UBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344042|||http://purl.uniprot.org/annotation/VSP_034719
http://togogenome.org/gene/9606:GUCA1ANB-GUCA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9P6|||http://purl.uniprot.org/uniprot/P43080                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Deamidated asparagine|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Found in a family with autosomal dominant macular dystrophy; unknown pathological significance.|||Found in autosomal dominant macular dystrophy; unknown pathological significance; affects guanylate cyclase regulator activity resulting in a constitutively active form at physiologic calcium concentrations; no change of affinity for calcium ions; increased affinity for magnesium ions.|||Guanylyl cyclase-activating protein 1|||In COD3 and CORD14.|||In COD3.|||In COD3; constitutive activation of GUCY2D.|||In COD3; exhibits an about 18-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal.|||In COD3; exhibits an about 28-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal.|||In COD3; exhibits an about 6-fold shift of ionic calcium concentration at which the guanylate cyclase activity is halfmaximal.|||In COD3; likely benign variant.|||In COD3; results in impaired guanylate cyclase regulator activity leading to increased GUCY2D activity.|||In COD3; results in impaired guanylate cyclase regulator activity; at high calcium ion concentrations the mutant protein stimulates GUCY2D activity while the wild-type inhibits it.|||In COD3; results in impaired guanylate cyclase regulator activity; at low calcium concentrations the mutant protein stimulates GUCY2D less efficiently than the wild-type but it remains active at high calcium concentrations causing persistent GUCY2D stimulation.|||In COD3; some subjects may present a moderately severe cone-rod dystrophy; unknown pathological significance; causes a decrease in the number of bound calcium ions from 3 to 2, without changing the activity profile.|||In COD3; unknown pathological significance.|||In CORD14.|||In CORD14; affects guanylate cyclase regulator activity resulting in constitutive activation of GUCY2D at physiologic calcium concentrations; 10-fold lower affinity for calcium ions.|||In CORD14; affects guanylate cyclase regulator activity resulting in constitutive activation of GUCY2D at physiologic calcium concentrations; altered tertiary structure; no change of affinity for calcium ions; increased affinity for magnesium ions.|||In CORD14; results in impaired guanylate cyclase regulator activity; at low calcium concentrations the mutant protein stimulates GUCY2D as the wild-type while at high calcium concentrations it does not fully inhibit GUCY2D; decreased affinity for calcium ions.|||In CORD14; results in impaired guanylate cyclase regulator activity; interferes with GCAP1 calcium-dependent transition from activator to inhibitor of GUCY2D; the mutant protein remains active at high calcium concentrations causing persistent GUCY2D stimulation.|||In a patient with an atypical form of retinitis pigmentosa; unknown pathological significance.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073803|||http://purl.uniprot.org/annotation/VAR_001372|||http://purl.uniprot.org/annotation/VAR_010648|||http://purl.uniprot.org/annotation/VAR_012987|||http://purl.uniprot.org/annotation/VAR_060802|||http://purl.uniprot.org/annotation/VAR_060803|||http://purl.uniprot.org/annotation/VAR_060804|||http://purl.uniprot.org/annotation/VAR_060805|||http://purl.uniprot.org/annotation/VAR_060806|||http://purl.uniprot.org/annotation/VAR_060807|||http://purl.uniprot.org/annotation/VAR_083669|||http://purl.uniprot.org/annotation/VAR_083670|||http://purl.uniprot.org/annotation/VAR_083671|||http://purl.uniprot.org/annotation/VAR_083672|||http://purl.uniprot.org/annotation/VAR_083673|||http://purl.uniprot.org/annotation/VAR_083674|||http://purl.uniprot.org/annotation/VAR_083675|||http://purl.uniprot.org/annotation/VAR_083676|||http://purl.uniprot.org/annotation/VAR_083677|||http://purl.uniprot.org/annotation/VAR_083678|||http://purl.uniprot.org/annotation/VAR_083679|||http://purl.uniprot.org/annotation/VAR_083680|||http://purl.uniprot.org/annotation/VAR_083681|||http://purl.uniprot.org/annotation/VAR_083682|||http://purl.uniprot.org/annotation/VAR_083683|||http://purl.uniprot.org/annotation/VAR_083684|||http://purl.uniprot.org/annotation/VAR_083685
http://togogenome.org/gene/9606:GPR148                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDV2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 148                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069625|||http://purl.uniprot.org/annotation/VAR_049403
http://togogenome.org/gene/9606:DUSP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16828|||http://purl.uniprot.org/uniprot/Q53GP9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dual specificity protein phosphatase 6|||In HH19.|||In HH19; rare variant associated with susceptibility to disease; the patient carries a second mutation in the HH-associated gene FGFR1.|||In HH19; rare variant associated with susceptibility to disease; the patient carries a second variant in the HH-associated gene SPRY4.|||In isoform 2.|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094804|||http://purl.uniprot.org/annotation/VAR_015113|||http://purl.uniprot.org/annotation/VAR_051750|||http://purl.uniprot.org/annotation/VAR_051751|||http://purl.uniprot.org/annotation/VAR_069943|||http://purl.uniprot.org/annotation/VAR_069944|||http://purl.uniprot.org/annotation/VAR_069945|||http://purl.uniprot.org/annotation/VAR_069946|||http://purl.uniprot.org/annotation/VSP_005137
http://togogenome.org/gene/9606:SPATA22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV9|||http://purl.uniprot.org/uniprot/B4DHW8|||http://purl.uniprot.org/uniprot/F5GWB9|||http://purl.uniprot.org/uniprot/Q8NHS9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Spermatogenesis-associated protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251605|||http://purl.uniprot.org/annotation/VAR_027693|||http://purl.uniprot.org/annotation/VAR_027694|||http://purl.uniprot.org/annotation/VAR_027695|||http://purl.uniprot.org/annotation/VAR_027696|||http://purl.uniprot.org/annotation/VSP_020763|||http://purl.uniprot.org/annotation/VSP_044858
http://togogenome.org/gene/9606:PRODH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43272                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In HYRPRO1 and SCZD4; associated with disease susceptibility; mild decrease of enzymatic activity.|||In HYRPRO1 and SCZD4; may be associated with disease susceptibility; enhanced enzymatic activity.|||In HYRPRO1 and SCZD4; may be associated with disease susceptibility; moderate reduction of enzymatic activity.|||In HYRPRO1 and SCZD4; may be associated with disease susceptibility; strongly reduced enzymatic activity.|||In HYRPRO1; mild decrease of enzymatic activity.|||In HYRPRO1; moderate reduction of enzymatic activity.|||In SCZD4; may be associated with disease susceptibility; strongly reduced affinity for FAD; strongly reduced enzymatic activity.|||In SCZD4; may be associated with disease susceptibility; strongly reduced enzymatic activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||May be a risk factor for schizophrenia; moderate reduction of enzymatic activity.|||Mild decrease of enzymatic activity.|||Mitochondrion|||Moderate reduction of enzymatic activity.|||N6-acetyllysine|||Proline dehydrogenase 1, mitochondrial|||Strongly reduced enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025800|||http://purl.uniprot.org/annotation/VAR_029563|||http://purl.uniprot.org/annotation/VAR_029564|||http://purl.uniprot.org/annotation/VAR_029565|||http://purl.uniprot.org/annotation/VAR_029566|||http://purl.uniprot.org/annotation/VAR_029567|||http://purl.uniprot.org/annotation/VAR_029568|||http://purl.uniprot.org/annotation/VAR_029569|||http://purl.uniprot.org/annotation/VAR_029570|||http://purl.uniprot.org/annotation/VAR_029571|||http://purl.uniprot.org/annotation/VAR_029572|||http://purl.uniprot.org/annotation/VAR_029573|||http://purl.uniprot.org/annotation/VAR_029574|||http://purl.uniprot.org/annotation/VAR_029575|||http://purl.uniprot.org/annotation/VAR_029576|||http://purl.uniprot.org/annotation/VAR_029577|||http://purl.uniprot.org/annotation/VAR_029874|||http://purl.uniprot.org/annotation/VAR_029875|||http://purl.uniprot.org/annotation/VAR_036566|||http://purl.uniprot.org/annotation/VAR_064883|||http://purl.uniprot.org/annotation/VAR_064884|||http://purl.uniprot.org/annotation/VAR_064885|||http://purl.uniprot.org/annotation/VAR_064886|||http://purl.uniprot.org/annotation/VSP_021848|||http://purl.uniprot.org/annotation/VSP_040848|||http://purl.uniprot.org/annotation/VSP_040849
http://togogenome.org/gene/9606:DBNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUF9|||http://purl.uniprot.org/uniprot/Q9UJU6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H|||Abolishes cleavage by caspase-3.|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Drebrin-like protein|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079793|||http://purl.uniprot.org/annotation/VSP_011398|||http://purl.uniprot.org/annotation/VSP_011399|||http://purl.uniprot.org/annotation/VSP_054779|||http://purl.uniprot.org/annotation/VSP_054780|||http://purl.uniprot.org/annotation/VSP_057346
http://togogenome.org/gene/9606:VCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXA2|||http://purl.uniprot.org/uniprot/P18206|||http://purl.uniprot.org/uniprot/V9HWK2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 112 AA tandem repeats|||C-terminal tail|||Disordered|||Facilitates phospholipid membrane insertion|||In CMD1W.|||In CMD1W; significantly alters metavinculin-mediated cross-linking of actin filaments.|||In CMH15.|||In isoform 1.|||In isoform 3.|||Interaction with ACTN4|||Linker (Pro-rich)|||N-terminal globular head|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by SRC-type Tyr-kinases|||Pro residues|||Talin-interaction|||Vinculin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064252|||http://purl.uniprot.org/annotation/VAR_035101|||http://purl.uniprot.org/annotation/VAR_035102|||http://purl.uniprot.org/annotation/VAR_035103|||http://purl.uniprot.org/annotation/VAR_035104|||http://purl.uniprot.org/annotation/VAR_035105|||http://purl.uniprot.org/annotation/VAR_037667|||http://purl.uniprot.org/annotation/VSP_006731|||http://purl.uniprot.org/annotation/VSP_011857|||http://purl.uniprot.org/annotation/VSP_011858|||http://purl.uniprot.org/annotation/VSP_011859
http://togogenome.org/gene/9606:CSDE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75534                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CSD 1|||CSD 2; truncated|||CSD 3|||CSD 4; truncated|||CSD 5|||CSD 6|||CSD 7|||CSD 8|||CSD 9|||Cold shock domain-containing protein E1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SUZ-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100348|||http://purl.uniprot.org/annotation/VSP_001138|||http://purl.uniprot.org/annotation/VSP_045615
http://togogenome.org/gene/9606:FBXL19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BVB1|||http://purl.uniprot.org/uniprot/Q6PCT2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CXXC-type|||Disordered|||F-box|||F-box/LRR-repeat protein 19|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||PHD-type|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119868|||http://purl.uniprot.org/annotation/VSP_013015|||http://purl.uniprot.org/annotation/VSP_040503
http://togogenome.org/gene/9606:CDC42EP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00587                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 7 AA tandem repeats of [PT]-[AT]-A-[ENT]-[PT]-[PTS]-[AG]|||Basic and acidic residues|||CRIB|||Cdc42 effector protein 1|||Disordered|||In isoform 2.|||No binding with CDC42.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212657|||http://purl.uniprot.org/annotation/VSP_004325
http://togogenome.org/gene/9606:ZNF385D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YG37|||http://purl.uniprot.org/uniprot/A0A994J5P6|||http://purl.uniprot.org/uniprot/Q9H6B1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Polar residues|||Zinc finger protein 385D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191819|||http://purl.uniprot.org/annotation/VAR_036058|||http://purl.uniprot.org/annotation/VAR_036059
http://togogenome.org/gene/9606:YWHAQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27348                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Sequence Conflict|||Site                                                                                  ^@                                                                                  14-3-3 protein theta|||3'-nitrotyrosine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058636
http://togogenome.org/gene/9606:NTAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AB6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  3-fold reduction in catalytic activity.|||Abolishes catalytic activity.|||Essential for catalytic activity|||Protein N-terminal asparagine amidohydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057971|||http://purl.uniprot.org/annotation/VAR_051244|||http://purl.uniprot.org/annotation/VAR_051245
http://togogenome.org/gene/9606:GPATCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRR8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||G patch domain-containing protein 1|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287457|||http://purl.uniprot.org/annotation/VAR_032303|||http://purl.uniprot.org/annotation/VAR_032304|||http://purl.uniprot.org/annotation/VAR_032305|||http://purl.uniprot.org/annotation/VAR_032306|||http://purl.uniprot.org/annotation/VAR_051014|||http://purl.uniprot.org/annotation/VAR_059657
http://togogenome.org/gene/9606:KCNJ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63252                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not significantly alter affinity for PIP2, but mutant channels do not open despite binding PIP2.|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In ATFB9; has a gain-of-function effect on the channels.|||In LQT7.|||In LQT7; loss of function and dominant-negative effect in current.|||In LQT7; loss of function mutation acting in a dominant-negative manner.|||In LQT7; there is loss of function when the mutant is expressed alone and a dominant-negative effect when expressed with wild-type channels; channel trafficking and assembly are not affected.|||In SQT3; gain of function.|||Inward rectifier potassium channel 2|||N-myristoyl glycine|||PDZ-binding|||Pore-forming|||Removed|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||S-nitrosocysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154923|||http://purl.uniprot.org/annotation/VAR_017851|||http://purl.uniprot.org/annotation/VAR_017852|||http://purl.uniprot.org/annotation/VAR_017853|||http://purl.uniprot.org/annotation/VAR_017854|||http://purl.uniprot.org/annotation/VAR_017855|||http://purl.uniprot.org/annotation/VAR_017856|||http://purl.uniprot.org/annotation/VAR_017857|||http://purl.uniprot.org/annotation/VAR_017858|||http://purl.uniprot.org/annotation/VAR_017859|||http://purl.uniprot.org/annotation/VAR_023842|||http://purl.uniprot.org/annotation/VAR_065861|||http://purl.uniprot.org/annotation/VAR_065862|||http://purl.uniprot.org/annotation/VAR_065863|||http://purl.uniprot.org/annotation/VAR_065864
http://togogenome.org/gene/9606:ELK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41970                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CTBP-binding motif|||Disordered|||ETS|||ETS domain-containing protein Elk-3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204097|||http://purl.uniprot.org/annotation/VAR_048946
http://togogenome.org/gene/9606:CENPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8C8KX99|||http://purl.uniprot.org/uniprot/B4DZL4|||http://purl.uniprot.org/uniprot/Q92674                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere protein I|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087354|||http://purl.uniprot.org/annotation/VSP_015797
http://togogenome.org/gene/9606:SLC15A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N697                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolished localization to the lysosome membrane and promotes relocalization to the plasma membrane; when associated with 14-A-A-15.|||Abolished localization to the lysosome membrane and promotes relocalization to the plasma membrane; when associated with 318-A-A-319. Does not affect interaction with TASL.|||Abolished transmembrane transporter activity. Abolished interaction with TASL.|||Does not affect interaction with TASL.|||Helical|||In isoform 2.|||Phosphoserine|||Solute carrier family 15 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338599|||http://purl.uniprot.org/annotation/VAR_051611|||http://purl.uniprot.org/annotation/VSP_034052
http://togogenome.org/gene/9606:RIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4T0|||http://purl.uniprot.org/uniprot/Q8WYP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras and Rab interactor 2|||Ras-associating|||SH2|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191320|||http://purl.uniprot.org/annotation/VAR_024694|||http://purl.uniprot.org/annotation/VAR_052945|||http://purl.uniprot.org/annotation/VSP_015145
http://togogenome.org/gene/9606:ABCC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2Q2|||http://purl.uniprot.org/uniprot/O15439                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  10% reduced expression level compared to wild-type; transport properties comparable to wild-type.|||20% reduced expression level compared to wild-type; significant lower activity in 6-mercaptopurine transport than wild-type.|||40% reduced expression level compared to wild-type; higher transport of 9-(2-phosphonyl-methoxyethyl) adenine than wild-type.|||ABC transmembrane type-1|||ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 4|||Disordered|||Does not affect plasma membrane localization; 1.5 fold increase in PEG2 transport; does not affect estradiol 17-beta-D-glucuronide transport.|||Does not affect plasma membrane localization; PEG2 transport is decreased by 50%; does not affect estradiol 17-beta-D-glucuronide transport.|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Transport properties comparable to wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093362|||http://purl.uniprot.org/annotation/VAR_020241|||http://purl.uniprot.org/annotation/VAR_020242|||http://purl.uniprot.org/annotation/VAR_020243|||http://purl.uniprot.org/annotation/VAR_020244|||http://purl.uniprot.org/annotation/VAR_020245|||http://purl.uniprot.org/annotation/VAR_020246|||http://purl.uniprot.org/annotation/VAR_022072|||http://purl.uniprot.org/annotation/VAR_022073|||http://purl.uniprot.org/annotation/VAR_029121|||http://purl.uniprot.org/annotation/VAR_029122|||http://purl.uniprot.org/annotation/VAR_029123|||http://purl.uniprot.org/annotation/VAR_029124|||http://purl.uniprot.org/annotation/VAR_029125|||http://purl.uniprot.org/annotation/VAR_029126|||http://purl.uniprot.org/annotation/VAR_045684|||http://purl.uniprot.org/annotation/VAR_045685|||http://purl.uniprot.org/annotation/VAR_045686|||http://purl.uniprot.org/annotation/VAR_045687|||http://purl.uniprot.org/annotation/VAR_045688|||http://purl.uniprot.org/annotation/VAR_046445|||http://purl.uniprot.org/annotation/VAR_046446|||http://purl.uniprot.org/annotation/VAR_046447|||http://purl.uniprot.org/annotation/VAR_046448|||http://purl.uniprot.org/annotation/VSP_035426|||http://purl.uniprot.org/annotation/VSP_043283|||http://purl.uniprot.org/annotation/VSP_043284|||http://purl.uniprot.org/annotation/VSP_057413
http://togogenome.org/gene/9606:OMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99983                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||Osteomodulin|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032754|||http://purl.uniprot.org/annotation/VAR_052014|||http://purl.uniprot.org/annotation/VAR_052015|||http://purl.uniprot.org/annotation/VAR_052016|||http://purl.uniprot.org/annotation/VAR_052017|||http://purl.uniprot.org/annotation/VAR_052018
http://togogenome.org/gene/9606:MYOF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZM1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HAE7; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Myoferlin|||N6-acetyllysine|||Necessary for interaction with EHD2|||Phosphoserine|||Reduces interaction with EHD2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057884|||http://purl.uniprot.org/annotation/VAR_031250|||http://purl.uniprot.org/annotation/VAR_031251|||http://purl.uniprot.org/annotation/VAR_031252|||http://purl.uniprot.org/annotation/VAR_049058|||http://purl.uniprot.org/annotation/VAR_049059|||http://purl.uniprot.org/annotation/VAR_085819|||http://purl.uniprot.org/annotation/VSP_001515|||http://purl.uniprot.org/annotation/VSP_001516|||http://purl.uniprot.org/annotation/VSP_001517|||http://purl.uniprot.org/annotation/VSP_023796|||http://purl.uniprot.org/annotation/VSP_023797|||http://purl.uniprot.org/annotation/VSP_023798|||http://purl.uniprot.org/annotation/VSP_023799|||http://purl.uniprot.org/annotation/VSP_023800|||http://purl.uniprot.org/annotation/VSP_023801|||http://purl.uniprot.org/annotation/VSP_023802
http://togogenome.org/gene/9606:ZNF214                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL59                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 214                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047458|||http://purl.uniprot.org/annotation/VAR_019975|||http://purl.uniprot.org/annotation/VAR_019976|||http://purl.uniprot.org/annotation/VAR_057403|||http://purl.uniprot.org/annotation/VAR_057404
http://togogenome.org/gene/9606:PAX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PRA8|||http://purl.uniprot.org/uniprot/D1KF47|||http://purl.uniprot.org/uniprot/F1T0F8|||http://purl.uniprot.org/uniprot/P26367|||http://purl.uniprot.org/uniprot/Q66SS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Homeobox|||In AN1 and ocular anterior segment anomalies; loss of DNA binding ability.|||In AN1.|||In AN1; atypical form.|||In AN1; loss of activity.|||In AN1; mild.|||In AN1; mild; shows 50% lower DNA-binding and transactivation ability than the wild-type protein.|||In AN1; reduced DNA binding ability.|||In AN1; shows almost no binding efficiency; transcriptional activation ability is about 50% lower than that of the wild-type protein.|||In AN1; shows almost no binding efficiency; transcriptional activation ability is about 80% of that of the wild-type protein.|||In AN1; shows only one-quarter to one-third the binding ability of the normal wild-type protein; exhibits normal transactivation.|||In AN1; the mutant homeodomain binds DNA as well as the wild-type homeodomain; the mutant does not modify the DNA-binding properties of the paired domain; the steady-state levels of the full-length mutant protein are higher than those of the wild-type one; a responsive promoter is activated to a higher extent by the mutant protein than by the wild-type protein; the presence of the mutation reduces sensitivity to trypsin digestion.|||In ASGD5.|||In ASGD5; also found in patients with congenital cataract and foveal hypoplasia.|||In BONH.|||In BONH; significant impairment of ability to activate transcription.|||In COAD and COLON; significant impairment of transcriptional activation ability.|||In FVH1; isolated.|||In FVH1; unknown pathological significance.|||In a family with nystagmus associated with a variant form of aniridia.|||In foveal hypoplasia; associated with presenile cataract syndrome.|||In isoform 5a.|||In morning glory disk anomaly; significant impairment of transcriptional activation ability.|||In optic nerve aplasia.|||PAI subdomain|||Paired|||Paired box protein Pax-6|||Polar residues|||RED subdomain|||Required for suppression of NFATC1-mediated transcription|||Shows about two-fold higher binding efficiency than the normal wild-type protein; transcriptional activation ability is about 89% of that of the wild-type protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050185|||http://purl.uniprot.org/annotation/VAR_003808|||http://purl.uniprot.org/annotation/VAR_003809|||http://purl.uniprot.org/annotation/VAR_003810|||http://purl.uniprot.org/annotation/VAR_003811|||http://purl.uniprot.org/annotation/VAR_003812|||http://purl.uniprot.org/annotation/VAR_003813|||http://purl.uniprot.org/annotation/VAR_003814|||http://purl.uniprot.org/annotation/VAR_003815|||http://purl.uniprot.org/annotation/VAR_003816|||http://purl.uniprot.org/annotation/VAR_008693|||http://purl.uniprot.org/annotation/VAR_008694|||http://purl.uniprot.org/annotation/VAR_008695|||http://purl.uniprot.org/annotation/VAR_008696|||http://purl.uniprot.org/annotation/VAR_008697|||http://purl.uniprot.org/annotation/VAR_008698|||http://purl.uniprot.org/annotation/VAR_008699|||http://purl.uniprot.org/annotation/VAR_008700|||http://purl.uniprot.org/annotation/VAR_008701|||http://purl.uniprot.org/annotation/VAR_008702|||http://purl.uniprot.org/annotation/VAR_008703|||http://purl.uniprot.org/annotation/VAR_008704|||http://purl.uniprot.org/annotation/VAR_008705|||http://purl.uniprot.org/annotation/VAR_008706|||http://purl.uniprot.org/annotation/VAR_008707|||http://purl.uniprot.org/annotation/VAR_008708|||http://purl.uniprot.org/annotation/VAR_015065|||http://purl.uniprot.org/annotation/VAR_015066|||http://purl.uniprot.org/annotation/VAR_017540|||http://purl.uniprot.org/annotation/VAR_017541|||http://purl.uniprot.org/annotation/VAR_017542|||http://purl.uniprot.org/annotation/VAR_017543|||http://purl.uniprot.org/annotation/VAR_017544|||http://purl.uniprot.org/annotation/VAR_017545|||http://purl.uniprot.org/annotation/VAR_017546|||http://purl.uniprot.org/annotation/VAR_017547|||http://purl.uniprot.org/annotation/VAR_047860|||http://purl.uniprot.org/annotation/VAR_047861|||http://purl.uniprot.org/annotation/VAR_047862|||http://purl.uniprot.org/annotation/VAR_047863|||http://purl.uniprot.org/annotation/VAR_047864|||http://purl.uniprot.org/annotation/VAR_047865|||http://purl.uniprot.org/annotation/VAR_047866|||http://purl.uniprot.org/annotation/VAR_047867|||http://purl.uniprot.org/annotation/VAR_047868|||http://purl.uniprot.org/annotation/VAR_067698|||http://purl.uniprot.org/annotation/VAR_084825|||http://purl.uniprot.org/annotation/VSP_002366
http://togogenome.org/gene/9606:RNASE8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDE3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Proton acceptor|||Proton donor|||Ribonuclease 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030902|||http://purl.uniprot.org/annotation/VAR_052194
http://togogenome.org/gene/9606:CSNK2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68400                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Casein kinase II subunit alpha|||In OCNDS.|||In isoform 2.|||Interaction with beta subunit|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085883|||http://purl.uniprot.org/annotation/VAR_077045|||http://purl.uniprot.org/annotation/VAR_077046|||http://purl.uniprot.org/annotation/VAR_077047|||http://purl.uniprot.org/annotation/VAR_077048|||http://purl.uniprot.org/annotation/VSP_041925
http://togogenome.org/gene/9606:UBE2G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62253                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||N-acetylmethionine|||N-acetylthreonine; in Ubiquitin-conjugating enzyme E2 G1, N-terminally processed|||Removed; alternate|||UBC core|||Ubiquitin-conjugating enzyme E2 G1|||Ubiquitin-conjugating enzyme E2 G1, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082480|||http://purl.uniprot.org/annotation/PRO_0000424514
http://togogenome.org/gene/9606:ARFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E273|||http://purl.uniprot.org/uniprot/P53367|||http://purl.uniprot.org/uniprot/Q8N8M9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  AH|||Arfaptin-1|||Basic and acidic residues|||Complete loss of phosphorylation by PRKD1.|||Disordered|||In isoform 3.|||In isoform A.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064665|||http://purl.uniprot.org/annotation/VSP_004088|||http://purl.uniprot.org/annotation/VSP_057425
http://togogenome.org/gene/9606:NECAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P71                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ABM|||Disordered|||EF-hand|||In isoform 1.|||In isoform 3.|||N-terminal EF-hand calcium-binding protein 3|||No effect on interaction with APBA3.|||Polar residues|||Pro residues|||Required for interaction with APBA3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073863|||http://purl.uniprot.org/annotation/VAR_048643|||http://purl.uniprot.org/annotation/VSP_000737|||http://purl.uniprot.org/annotation/VSP_000738|||http://purl.uniprot.org/annotation/VSP_000739
http://togogenome.org/gene/9606:MYBPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13203                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like C2-type 1|||Ig-like C2-type 2|||Myosin-binding protein H|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072698|||http://purl.uniprot.org/annotation/VAR_028181|||http://purl.uniprot.org/annotation/VAR_028182|||http://purl.uniprot.org/annotation/VAR_028183
http://togogenome.org/gene/9606:LSM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y5|||http://purl.uniprot.org/uniprot/Q9Y4Y9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Removed|||Sm|||U6 snRNA-associated Sm-like protein LSm5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125572|||http://purl.uniprot.org/annotation/VSP_040991
http://togogenome.org/gene/9606:GEMIN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLC9|||http://purl.uniprot.org/uniprot/Q58EZ8|||http://purl.uniprot.org/uniprot/Q8TEQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with U4 snRNA.|||Abolishes interaction with U4 snRNA. Abolishes interaction with the 7-methylguanosine cap of RNA molecules. No effect on interaction with SMN complex.|||Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes.|||Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules.|||Anaphase-promoting complex subunit 4-like WD40|||Basic and acidic residues|||Disordered|||Gem-associated protein 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with U1 snRNA|||In NEDCAM.|||In NEDCAM; impaired function in spliceosomal snRNP assembly; decreased protein abundance; decreased protein stability; decreased interaction with DDX20; decreased interaction with GEMIN4.|||In NEDCAM; unknown pathological significance.|||Interaction with U4 snRNA|||Interaction with U4 snRNA and with the 7-methylguanosine cap of RNA molecules|||No effect in interaction with U4 snRNA. No effect on interaction with SMN complex.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly decreases interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. Abolishes interaction with 80S ribosomes.|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051004|||http://purl.uniprot.org/annotation/VAR_033807|||http://purl.uniprot.org/annotation/VAR_057604|||http://purl.uniprot.org/annotation/VAR_085836|||http://purl.uniprot.org/annotation/VAR_085837|||http://purl.uniprot.org/annotation/VAR_085838|||http://purl.uniprot.org/annotation/VAR_085839|||http://purl.uniprot.org/annotation/VAR_085840|||http://purl.uniprot.org/annotation/VAR_085841|||http://purl.uniprot.org/annotation/VAR_085842|||http://purl.uniprot.org/annotation/VAR_085843|||http://purl.uniprot.org/annotation/VAR_085844|||http://purl.uniprot.org/annotation/VAR_085845|||http://purl.uniprot.org/annotation/VAR_085846|||http://purl.uniprot.org/annotation/VAR_085847|||http://purl.uniprot.org/annotation/VAR_085848|||http://purl.uniprot.org/annotation/VAR_085849|||http://purl.uniprot.org/annotation/VAR_085850|||http://purl.uniprot.org/annotation/VAR_085851|||http://purl.uniprot.org/annotation/VAR_085852|||http://purl.uniprot.org/annotation/VAR_085853|||http://purl.uniprot.org/annotation/VAR_085854|||http://purl.uniprot.org/annotation/VAR_085855|||http://purl.uniprot.org/annotation/VAR_085856|||http://purl.uniprot.org/annotation/VAR_085857|||http://purl.uniprot.org/annotation/VAR_085858|||http://purl.uniprot.org/annotation/VAR_085859
http://togogenome.org/gene/9606:PUS7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0K6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nucleophile|||Phosphoserine|||Pseudouridylate synthase PUS7L|||TRUD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316785|||http://purl.uniprot.org/annotation/VAR_038392|||http://purl.uniprot.org/annotation/VAR_038393|||http://purl.uniprot.org/annotation/VAR_038394|||http://purl.uniprot.org/annotation/VSP_054568
http://togogenome.org/gene/9606:AEN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes exonuclease activity; when associated with A-114 and A-116.|||Abolishes exonuclease activity; when associated with A-114 and A-258.|||Abolishes exonuclease activity; when associated with A-116 and A-258.|||Apoptosis-enhancing nuclease|||Basic and acidic residues|||Disordered|||Exonuclease|||In isoform 2.|||Nuclear localization signal|||Nucleolar localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324088|||http://purl.uniprot.org/annotation/VAR_039651|||http://purl.uniprot.org/annotation/VAR_039652|||http://purl.uniprot.org/annotation/VAR_039653|||http://purl.uniprot.org/annotation/VSP_032132
http://togogenome.org/gene/9606:QSOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE5|||http://purl.uniprot.org/uniprot/O00391|||http://purl.uniprot.org/uniprot/Q13876                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreased O-glycosylation.|||Decreased protein stability and catalytic activity; when associated with S-119 or T-119.|||Disordered|||ERV/ALR sulfhydryl oxidase|||Helical|||In isoform 2.|||Loss of activity.|||Loss of catalytic activity. Cannot prevent cell detachment after depletion of the endogenous protein.|||Loss of catalytic activity. Decreased protein stability and catalytic activity; when associated with A-72.|||Loss of glycosylation site.|||Loss of glycosylation site. Abolishes secretion. No effect on catalytic activity.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No effect. Reduces activity by 70%; when associated with S-512.|||Nucleophile|||Phosphoserine; by FAM20C|||Redox-active|||Reduces activity by 40%. Reduces activity by 70%; when associated with S-509.|||Reduces activity by 93%.|||Reduces activity by 96%.|||Sulfhydryl oxidase|||Sulfhydryl oxidase 1|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249533|||http://purl.uniprot.org/annotation/PRO_5004182219|||http://purl.uniprot.org/annotation/PRO_5014247022|||http://purl.uniprot.org/annotation/VAR_027429|||http://purl.uniprot.org/annotation/VAR_027430|||http://purl.uniprot.org/annotation/VAR_027431|||http://purl.uniprot.org/annotation/VAR_027432|||http://purl.uniprot.org/annotation/VAR_027433|||http://purl.uniprot.org/annotation/VAR_027434|||http://purl.uniprot.org/annotation/VAR_053652|||http://purl.uniprot.org/annotation/VSP_020489|||http://purl.uniprot.org/annotation/VSP_020490
http://togogenome.org/gene/9606:ZBTB48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K291|||http://purl.uniprot.org/uniprot/B2R702|||http://purl.uniprot.org/uniprot/P10074                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to the telomeric double-stranded 5'-TTAGGG-3' repeat.|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Telomere zinc finger-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047272|||http://purl.uniprot.org/annotation/VAR_052925
http://togogenome.org/gene/9606:SELENOO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVL4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Abolishes redox complex formation.|||Disordered|||Enhances redox complex formation.|||Loss of catalytic activity. Loss of ATP binding.|||Mitochondrion|||No effect on redox complex formation.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein adenylyltransferase SelO, mitochondrial|||Proton acceptor|||Selenocysteine|||Slightly enhances redox complex formation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121399|||http://purl.uniprot.org/annotation/VAR_059952|||http://purl.uniprot.org/annotation/VAR_059953|||http://purl.uniprot.org/annotation/VAR_059954|||http://purl.uniprot.org/annotation/VAR_059955
http://togogenome.org/gene/9606:RPS6KC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1U5|||http://purl.uniprot.org/uniprot/F5H7T0|||http://purl.uniprot.org/uniprot/F6RJM5|||http://purl.uniprot.org/uniprot/Q96S38                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||MIT|||PX|||Phosphoserine|||Polar residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase delta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233127|||http://purl.uniprot.org/annotation/VAR_040647|||http://purl.uniprot.org/annotation/VAR_040648|||http://purl.uniprot.org/annotation/VAR_040649|||http://purl.uniprot.org/annotation/VAR_040650|||http://purl.uniprot.org/annotation/VAR_040651|||http://purl.uniprot.org/annotation/VAR_040652|||http://purl.uniprot.org/annotation/VAR_040653|||http://purl.uniprot.org/annotation/VAR_040654|||http://purl.uniprot.org/annotation/VAR_040655|||http://purl.uniprot.org/annotation/VAR_040656|||http://purl.uniprot.org/annotation/VAR_040657|||http://purl.uniprot.org/annotation/VAR_051635|||http://purl.uniprot.org/annotation/VSP_046333
http://togogenome.org/gene/9606:TMEM138                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QSZ6|||http://purl.uniprot.org/uniprot/Q9NPI0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In JBTS16.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 138                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285700|||http://purl.uniprot.org/annotation/VAR_067059|||http://purl.uniprot.org/annotation/VAR_067060|||http://purl.uniprot.org/annotation/VAR_067061|||http://purl.uniprot.org/annotation/VAR_067062|||http://purl.uniprot.org/annotation/VSP_024891|||http://purl.uniprot.org/annotation/VSP_024892|||http://purl.uniprot.org/annotation/VSP_042588
http://togogenome.org/gene/9606:MSMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1L6U9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Prostate-associated microseminoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338648|||http://purl.uniprot.org/annotation/VAR_043818
http://togogenome.org/gene/9606:B3GNT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289209
http://togogenome.org/gene/9606:RPS6KA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3B5|||http://purl.uniprot.org/uniprot/Q15349                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PDPK1|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086201|||http://purl.uniprot.org/annotation/VAR_040627|||http://purl.uniprot.org/annotation/VAR_040628|||http://purl.uniprot.org/annotation/VSP_017732|||http://purl.uniprot.org/annotation/VSP_041836
http://togogenome.org/gene/9606:FAM174C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM174C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079385
http://togogenome.org/gene/9606:C19orf12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSK7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in families with neurodegeneration with brain iron accumulation; uncertain pathological significance.|||Helical|||In NBIA4 and SPG43; impairs subcellular localization to the endoplasmic reticulum or mitochondrion.|||In NBIA4.|||In NBIA4; impairs subcellular localization to the endoplasmic reticulum or mitochondrion.|||In NBIA4; no effect on its subcellular localization; no cytosolic redistribution seen in response to oxidative stress.|||In NBIA4; predominantly cytosolic distribution with a localization also seen in the mitochondrial matrix; no cytosolic redistribution seen in response to oxidative stress; patient fibroblasts accumulate high levels of mitochondrial calcium and are more prone to oxidative stress-induced apoptosis.|||In NBIA4; unknown pathological significance.|||In isoform 1 and isoform 3.|||In isoform 2.|||In isoform 3.|||Protein C19orf12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296662|||http://purl.uniprot.org/annotation/VAR_066617|||http://purl.uniprot.org/annotation/VAR_066618|||http://purl.uniprot.org/annotation/VAR_066619|||http://purl.uniprot.org/annotation/VAR_066620|||http://purl.uniprot.org/annotation/VAR_066621|||http://purl.uniprot.org/annotation/VAR_066622|||http://purl.uniprot.org/annotation/VAR_069756|||http://purl.uniprot.org/annotation/VAR_069757|||http://purl.uniprot.org/annotation/VAR_069758|||http://purl.uniprot.org/annotation/VAR_069759|||http://purl.uniprot.org/annotation/VAR_069760|||http://purl.uniprot.org/annotation/VAR_069761|||http://purl.uniprot.org/annotation/VAR_069762|||http://purl.uniprot.org/annotation/VAR_069763|||http://purl.uniprot.org/annotation/VAR_069764|||http://purl.uniprot.org/annotation/VAR_070668|||http://purl.uniprot.org/annotation/VAR_070669|||http://purl.uniprot.org/annotation/VAR_076803|||http://purl.uniprot.org/annotation/VAR_076804|||http://purl.uniprot.org/annotation/VSP_027227|||http://purl.uniprot.org/annotation/VSP_027228|||http://purl.uniprot.org/annotation/VSP_037995
http://togogenome.org/gene/9606:MCEMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYE9|||http://purl.uniprot.org/uniprot/Q8IX19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Mast cell-expressed membrane protein 1|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274052|||http://purl.uniprot.org/annotation/VAR_030180|||http://purl.uniprot.org/annotation/VAR_051159|||http://purl.uniprot.org/annotation/VAR_059697
http://togogenome.org/gene/9606:ANGPTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95841                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Angiopoietin-related protein 1|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009118
http://togogenome.org/gene/9606:H1-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3R0T8|||http://purl.uniprot.org/uniprot/P10412                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.4|||In a colorectal cancer sample; somatic mutation.|||N-acetylserine|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195908|||http://purl.uniprot.org/annotation/VAR_036203|||http://purl.uniprot.org/annotation/VAR_049307
http://togogenome.org/gene/9606:ZSWIM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XI8                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Uncharacterized protein ZSWIM9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322596|||http://purl.uniprot.org/annotation/VSP_059340
http://togogenome.org/gene/9606:DIO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55073|||http://purl.uniprot.org/uniprot/Q86TU3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Non standard residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Non standard residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Selenocysteine|||Thyroxine 5-deiodinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154323
http://togogenome.org/gene/9606:OR5K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWC1|||http://purl.uniprot.org/uniprot/Q8NHB7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150600
http://togogenome.org/gene/9606:EOMES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4K0|||http://purl.uniprot.org/uniprot/O95936                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Eomesodermin homolog|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Required for transcription activation|||T-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184459|||http://purl.uniprot.org/annotation/VAR_036069|||http://purl.uniprot.org/annotation/VAR_059827|||http://purl.uniprot.org/annotation/VSP_042161|||http://purl.uniprot.org/annotation/VSP_042162|||http://purl.uniprot.org/annotation/VSP_054801
http://togogenome.org/gene/9606:PCDHB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5E9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003940|||http://purl.uniprot.org/annotation/VSP_055932
http://togogenome.org/gene/9606:FREM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C091                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CSPG 1|||CSPG 10|||CSPG 11|||CSPG 12|||CSPG 2|||CSPG 3|||CSPG 4|||CSPG 5|||CSPG 6|||CSPG 7|||CSPG 8|||CSPG 9|||Calx-beta 1|||Calx-beta 2|||Calx-beta 3|||FRAS1-related extracellular matrix protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010127|||http://purl.uniprot.org/annotation/VAR_055819|||http://purl.uniprot.org/annotation/VAR_059291
http://togogenome.org/gene/9606:ATP6V0C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27449                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Essential for proton translocation|||Helical|||Lumenal|||V-type proton ATPase 16 kDa proteolipid subunit c                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071743
http://togogenome.org/gene/9606:SLC26A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFT5|||http://purl.uniprot.org/uniprot/G3XAC1|||http://purl.uniprot.org/uniprot/Q96MZ1|||http://purl.uniprot.org/uniprot/Q9BXS9|||http://purl.uniprot.org/uniprot/Q9Y3Y1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.|||Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.|||Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Reduced chloride oxalate exchanger activity.|||STAS|||Solute carrier family 26 member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080171|||http://purl.uniprot.org/annotation/VAR_012776|||http://purl.uniprot.org/annotation/VSP_006169|||http://purl.uniprot.org/annotation/VSP_040127|||http://purl.uniprot.org/annotation/VSP_046807|||http://purl.uniprot.org/annotation/VSP_047851|||http://purl.uniprot.org/annotation/VSP_047852|||http://purl.uniprot.org/annotation/VSP_055273|||http://purl.uniprot.org/annotation/VSP_055274
http://togogenome.org/gene/9606:PLCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KWH8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1|||Basic and acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In HPE14.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329007|||http://purl.uniprot.org/annotation/VAR_087460|||http://purl.uniprot.org/annotation/VSP_032901|||http://purl.uniprot.org/annotation/VSP_032902|||http://purl.uniprot.org/annotation/VSP_032903|||http://purl.uniprot.org/annotation/VSP_032904|||http://purl.uniprot.org/annotation/VSP_032905|||http://purl.uniprot.org/annotation/VSP_032906
http://togogenome.org/gene/9606:SYCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synaptonemal complex protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072366|||http://purl.uniprot.org/annotation/VAR_014115|||http://purl.uniprot.org/annotation/VAR_054059|||http://purl.uniprot.org/annotation/VAR_054060|||http://purl.uniprot.org/annotation/VAR_054061
http://togogenome.org/gene/9606:EML5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BV3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Echinoderm microtubule-associated protein-like 5|||In isoform 2.|||In isoform 4.|||In isoform 5.|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 17|||WD 18|||WD 19|||WD 2|||WD 20|||WD 21|||WD 22|||WD 23|||WD 24|||WD 25|||WD 26|||WD 27|||WD 28|||WD 29|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284395|||http://purl.uniprot.org/annotation/VAR_031730|||http://purl.uniprot.org/annotation/VSP_040645|||http://purl.uniprot.org/annotation/VSP_041258|||http://purl.uniprot.org/annotation/VSP_041259|||http://purl.uniprot.org/annotation/VSP_041260|||http://purl.uniprot.org/annotation/VSP_041261
http://togogenome.org/gene/9606:ZNF596                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC21                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 596                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245849|||http://purl.uniprot.org/annotation/VAR_027014|||http://purl.uniprot.org/annotation/VAR_027015|||http://purl.uniprot.org/annotation/VSP_019801|||http://purl.uniprot.org/annotation/VSP_019802|||http://purl.uniprot.org/annotation/VSP_019803|||http://purl.uniprot.org/annotation/VSP_019804
http://togogenome.org/gene/9606:ZNF416                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWM5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 416                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233984
http://togogenome.org/gene/9606:CARM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X55                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dimethylated arginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone-arginine methyltransferase CARM1|||In isoform 1.|||In isoform 2.|||Interaction with C9orf72|||Loss of FBXO9-mediated ubiquitination and subsequent proteasomal degradation.|||Loss of protein methyltransferase activity without affecting ability to regulate replication fork progression.|||N-acetylalanine|||Phosphoserine|||Removed|||Required for nuclear translocation|||SAM-dependent MTase PRMT-type|||Transactivation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212338|||http://purl.uniprot.org/annotation/VSP_012506|||http://purl.uniprot.org/annotation/VSP_012507|||http://purl.uniprot.org/annotation/VSP_039876
http://togogenome.org/gene/9606:COLGALT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Endoplasmic reticulum retention motif|||In BSVD3.|||In BSVD3; loss of galactosyltransferase activity.|||Loss of galactosyltransferase activity; when associated with A-166.|||Loss of galactosyltransferase activity; when associated with A-168.|||Loss of galactosyltransferase activity; when associated with A-461.|||Loss of galactosyltransferase activity; when associated with A-463.|||N-linked (GlcNAc...) asparagine|||No effect on galactosyltransferase activity; when associated with A-585.|||No effect on galactosyltransferase activity; when associated with A-587.|||Procollagen galactosyltransferase 1|||Small decrease of galactosyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309536|||http://purl.uniprot.org/annotation/VAR_081752|||http://purl.uniprot.org/annotation/VAR_081753|||http://purl.uniprot.org/annotation/VAR_081754
http://togogenome.org/gene/9606:PABPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U42                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes self-association, protein aggregation and cell death.|||Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2.|||Interaction with PAPOLA|||Interaction with SKIP|||N-acetylalanine|||Necessary for homooligomerization|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polyadenylate-binding protein 2|||RRM|||Removed|||Stimulates PAPOLA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081711|||http://purl.uniprot.org/annotation/VAR_018179|||http://purl.uniprot.org/annotation/VSP_009847|||http://purl.uniprot.org/annotation/VSP_009848
http://togogenome.org/gene/9606:LOC728392                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C1I1                                                                                  ^@                                                                                  Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:SRPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J2M4|||http://purl.uniprot.org/uniprot/P78362                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||SRSF protein kinase 2|||SRSF protein kinase 2 C-terminal|||SRSF protein kinase 2 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086677|||http://purl.uniprot.org/annotation/PRO_0000414751|||http://purl.uniprot.org/annotation/PRO_0000414752|||http://purl.uniprot.org/annotation/VAR_041114|||http://purl.uniprot.org/annotation/VAR_041115|||http://purl.uniprot.org/annotation/VAR_041116|||http://purl.uniprot.org/annotation/VAR_041117|||http://purl.uniprot.org/annotation/VAR_041118|||http://purl.uniprot.org/annotation/VAR_057111|||http://purl.uniprot.org/annotation/VAR_060390|||http://purl.uniprot.org/annotation/VSP_039386
http://togogenome.org/gene/9606:HS6ST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan-sulfate 6-O-sulfotransferase 3|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190809|||http://purl.uniprot.org/annotation/VAR_028159
http://togogenome.org/gene/9606:IRF2BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU81                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Cys-rich|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interferon regulatory factor 2-binding protein 1|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328729|||http://purl.uniprot.org/annotation/VAR_042502
http://togogenome.org/gene/9606:CKLF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BJH6|||http://purl.uniprot.org/uniprot/Q9UBR5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chemokine-like factor|||Helical|||In isoform 1 and isoform 3.|||In isoform 4 and isoform 3.|||In isoform 5.|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186094|||http://purl.uniprot.org/annotation/VSP_041445|||http://purl.uniprot.org/annotation/VSP_041446|||http://purl.uniprot.org/annotation/VSP_050605|||http://purl.uniprot.org/annotation/VSP_050606
http://togogenome.org/gene/9606:TOM1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2U2|||http://purl.uniprot.org/uniprot/B7Z671|||http://purl.uniprot.org/uniprot/F5H3S6|||http://purl.uniprot.org/uniprot/Q6ZVM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Clathrin-binding|||Disordered|||GAT|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||TOM1-like protein 2|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278790|||http://purl.uniprot.org/annotation/VSP_023390|||http://purl.uniprot.org/annotation/VSP_023391|||http://purl.uniprot.org/annotation/VSP_023392|||http://purl.uniprot.org/annotation/VSP_057214|||http://purl.uniprot.org/annotation/VSP_057215
http://togogenome.org/gene/9606:PBDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDF3|||http://purl.uniprot.org/uniprot/Q9BVG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Protein PBDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254105
http://togogenome.org/gene/9606:SCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43819                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In MC4DN2 and MYP6; reduced cytochrome c oxidase subunit II synthesis and reduced ability to regulate cellular copper homeostasis.|||In MC4DN2.|||In MC4DN2; renders the protein unstable.|||In MYP6; likely benign variant.|||In MYP6; remains stable in mitochondria; reduces the level of the protein copurifying with COA6 by 80%.|||In MYP6; unknown pathological significance.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Protein SCO2 homolog, mitochondrial|||Redox-active|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031922|||http://purl.uniprot.org/annotation/VAR_008874|||http://purl.uniprot.org/annotation/VAR_008875|||http://purl.uniprot.org/annotation/VAR_011738|||http://purl.uniprot.org/annotation/VAR_013238|||http://purl.uniprot.org/annotation/VAR_051912|||http://purl.uniprot.org/annotation/VAR_070053|||http://purl.uniprot.org/annotation/VAR_070054|||http://purl.uniprot.org/annotation/VAR_074010|||http://purl.uniprot.org/annotation/VAR_074011|||http://purl.uniprot.org/annotation/VAR_076281|||http://purl.uniprot.org/annotation/VAR_076282
http://togogenome.org/gene/9606:ADM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4H4                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Adrenomedullin-2|||Disordered|||Intermedin-short|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000977|||http://purl.uniprot.org/annotation/PRO_0000000978|||http://purl.uniprot.org/annotation/PRO_0000000979
http://togogenome.org/gene/9606:HBZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02008                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Turn                                                                                  ^@                                                                                  Hemoglobin subunit zeta|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052851
http://togogenome.org/gene/9606:RPL13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40429                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site                                                                                  ^@                                                                                  Citrulline|||Large ribosomal subunit protein uL13|||Loss of interferon-gamma induced phosphorylation.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine; by ZIPK/DAPK3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000133769
http://togogenome.org/gene/9606:HLCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50747                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BPL/LPL catalytic|||Basic and acidic residues|||Biotin--protein ligase|||Disordered|||In HLCS deficiency.|||In HLCS deficiency; 0.2% activity.|||In HLCS deficiency; 12% activity.|||In HLCS deficiency; 14% of activity; shows elevated KM values for biotin (KM mutant) compared with that of the wild-type form.|||In HLCS deficiency; 22% activity; shows elevated KM values for biotin (KM mutant) compared with that of the wild-type form.|||In HLCS deficiency; 3.4% activity.|||In HLCS deficiency; 4.3% activity.|||In HLCS deficiency; <10% activity.|||In HLCS deficiency; <10% activity; has normal or low KM values for biotin (non-KM mutant).|||In HLCS deficiency; almost no activity.|||In HLCS deficiency; benign variant; conserves enzymatic wild-type activity.|||In HLCS deficiency; has normal or low KM values for biotin (non-KM mutant).|||In HLCS deficiency; has normal or low KM values for biotin (non-KM mutant); growth of patients' fibroblasts is compromised compared with normal fibroblasts; patients cells are not sensitive to biotin-depletion from the media; growth rates cannot be restored by re-administration of biotin; enzyme activity is severely compromised and cannot be increased by additional biotin; turn-over rate for the mutant protein is double that of wild-type enzyme.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064979|||http://purl.uniprot.org/annotation/VAR_005084|||http://purl.uniprot.org/annotation/VAR_009196|||http://purl.uniprot.org/annotation/VAR_009197|||http://purl.uniprot.org/annotation/VAR_009198|||http://purl.uniprot.org/annotation/VAR_009199|||http://purl.uniprot.org/annotation/VAR_009200|||http://purl.uniprot.org/annotation/VAR_009201|||http://purl.uniprot.org/annotation/VAR_013009|||http://purl.uniprot.org/annotation/VAR_021218|||http://purl.uniprot.org/annotation/VAR_021219|||http://purl.uniprot.org/annotation/VAR_021220|||http://purl.uniprot.org/annotation/VAR_035800|||http://purl.uniprot.org/annotation/VAR_046507|||http://purl.uniprot.org/annotation/VAR_046508|||http://purl.uniprot.org/annotation/VAR_046509|||http://purl.uniprot.org/annotation/VAR_046510|||http://purl.uniprot.org/annotation/VAR_046511|||http://purl.uniprot.org/annotation/VAR_046512|||http://purl.uniprot.org/annotation/VAR_046513|||http://purl.uniprot.org/annotation/VAR_046514|||http://purl.uniprot.org/annotation/VAR_046515|||http://purl.uniprot.org/annotation/VAR_046516|||http://purl.uniprot.org/annotation/VAR_046517|||http://purl.uniprot.org/annotation/VAR_073074|||http://purl.uniprot.org/annotation/VAR_073075|||http://purl.uniprot.org/annotation/VSP_061442
http://togogenome.org/gene/9606:CYP1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04798                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 1A1|||In allele CYP1A1*10.|||In allele CYP1A1*11.|||In allele CYP1A1*2B and allele CYP1A1*2C; displays 5.7- and 12-fold increase in catalytic efficiency in the formation of 2-hydroxylated estrogens, 17beta-estradiol and estrone respectively..|||In allele CYP1A1*4; displays similar catalytic efficiency toward estrogens when compared to the wild-type enzyme..|||In allele CYP1A1*5.|||In allele CYP1A1*6.|||In allele CYP1A1*8.|||In allele CYP1A1*9.|||In isoform 2.|||In isoform 3.|||Mitochondrial targeting signal|||O-linked (GlcNAc) serine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051627|||http://purl.uniprot.org/annotation/VAR_001243|||http://purl.uniprot.org/annotation/VAR_008342|||http://purl.uniprot.org/annotation/VAR_009280|||http://purl.uniprot.org/annotation/VAR_016937|||http://purl.uniprot.org/annotation/VAR_016938|||http://purl.uniprot.org/annotation/VAR_016939|||http://purl.uniprot.org/annotation/VAR_016940|||http://purl.uniprot.org/annotation/VAR_016941|||http://purl.uniprot.org/annotation/VAR_016942|||http://purl.uniprot.org/annotation/VAR_020122|||http://purl.uniprot.org/annotation/VAR_023194|||http://purl.uniprot.org/annotation/VAR_023195|||http://purl.uniprot.org/annotation/VAR_024706|||http://purl.uniprot.org/annotation/VAR_024707|||http://purl.uniprot.org/annotation/VAR_024708|||http://purl.uniprot.org/annotation/VAR_033817|||http://purl.uniprot.org/annotation/VAR_033818|||http://purl.uniprot.org/annotation/VSP_053363|||http://purl.uniprot.org/annotation/VSP_053364|||http://purl.uniprot.org/annotation/VSP_053365|||http://purl.uniprot.org/annotation/VSP_053366
http://togogenome.org/gene/9606:TUSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Tumor suppressor candidate gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312284|||http://purl.uniprot.org/annotation/VAR_037471
http://togogenome.org/gene/9606:SLC12A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55017                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished interaction with OXSR1/OSR1 and STK39/SPAK, preventing phosphorylation and activation.|||Abolished sodium and chloride ion cotransporter activity.|||Cytoplasmic|||Decreased phosphorylation by OXSR1/OSR1 and STK39/SPAK.|||Discontinuously helical|||Extracellular|||Helical|||In GTLMNS.|||In GTLMNS; 27% residual Na(+) uptake activity; increased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; no effect on localization at the plasma membrane.|||In GTLMNS; 40% residual Na(+) uptake activity; increased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; no effect on localization at the plasma membrane.|||In GTLMNS; 48% residual Na(+) uptake activity; no effect on localization at the plasma membrane.|||In GTLMNS; 54% residual Na(+) uptake activity; no effect on localization at the plasma membrane.|||In GTLMNS; 58% residual Na(+) uptake activity; decreased MAPK1/3 (ERK1/2) phosphorylation in response to IL18; partial loss of localization at the plasma membrane.|||In GTLMNS; 68% residual Na(+) uptake activity; partial loss of localization at the plasma membrane.|||In GTLMNS; associated with T-192.|||In GTLMNS; associated with deletion of N-566.|||In GTLMNS; complete loss Na(+) uptake activity; partial loss of localization at the plasma membrane.|||In GTLMNS; does not affect MAPK1/3 (ERK1/2) phosphorylation in response to IL18.|||In GTLMNS; impaired protein structure.|||In GTLMNS; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increases sodium transport.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by OXSR1 and STK39|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||Reduced sensitivity to thiazide diuretics.|||Reduced sensitivity to thiazide diuretics. Reduced sodium and chloride ion cotransporter activity.|||Reduced sodium and chloride ion cotransporter activity.|||Solute carrier family 12 member 3|||Strongly reduced sodium and chloride ion cotransporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178026|||http://purl.uniprot.org/annotation/VAR_007113|||http://purl.uniprot.org/annotation/VAR_007114|||http://purl.uniprot.org/annotation/VAR_007115|||http://purl.uniprot.org/annotation/VAR_007116|||http://purl.uniprot.org/annotation/VAR_007117|||http://purl.uniprot.org/annotation/VAR_007118|||http://purl.uniprot.org/annotation/VAR_007119|||http://purl.uniprot.org/annotation/VAR_007120|||http://purl.uniprot.org/annotation/VAR_007121|||http://purl.uniprot.org/annotation/VAR_007122|||http://purl.uniprot.org/annotation/VAR_007123|||http://purl.uniprot.org/annotation/VAR_007124|||http://purl.uniprot.org/annotation/VAR_007125|||http://purl.uniprot.org/annotation/VAR_007126|||http://purl.uniprot.org/annotation/VAR_039475|||http://purl.uniprot.org/annotation/VAR_039476|||http://purl.uniprot.org/annotation/VAR_039477|||http://purl.uniprot.org/annotation/VAR_039478|||http://purl.uniprot.org/annotation/VAR_039479|||http://purl.uniprot.org/annotation/VAR_039480|||http://purl.uniprot.org/annotation/VAR_039481|||http://purl.uniprot.org/annotation/VAR_039482|||http://purl.uniprot.org/annotation/VAR_039483|||http://purl.uniprot.org/annotation/VAR_039484|||http://purl.uniprot.org/annotation/VAR_039485|||http://purl.uniprot.org/annotation/VAR_039486|||http://purl.uniprot.org/annotation/VAR_039487|||http://purl.uniprot.org/annotation/VAR_039488|||http://purl.uniprot.org/annotation/VAR_039489|||http://purl.uniprot.org/annotation/VAR_039490|||http://purl.uniprot.org/annotation/VAR_039491|||http://purl.uniprot.org/annotation/VAR_039492|||http://purl.uniprot.org/annotation/VAR_039493|||http://purl.uniprot.org/annotation/VAR_039494|||http://purl.uniprot.org/annotation/VAR_039495|||http://purl.uniprot.org/annotation/VAR_039496|||http://purl.uniprot.org/annotation/VAR_039497|||http://purl.uniprot.org/annotation/VAR_039498|||http://purl.uniprot.org/annotation/VAR_039499|||http://purl.uniprot.org/annotation/VAR_039500|||http://purl.uniprot.org/annotation/VAR_039501|||http://purl.uniprot.org/annotation/VAR_039502|||http://purl.uniprot.org/annotation/VAR_039503|||http://purl.uniprot.org/annotation/VAR_039504|||http://purl.uniprot.org/annotation/VAR_039505|||http://purl.uniprot.org/annotation/VAR_039506|||http://purl.uniprot.org/annotation/VAR_039507|||http://purl.uniprot.org/annotation/VAR_039508|||http://purl.uniprot.org/annotation/VAR_039509|||http://purl.uniprot.org/annotation/VAR_039510|||http://purl.uniprot.org/annotation/VAR_039511|||http://purl.uniprot.org/annotation/VAR_039512|||http://purl.uniprot.org/annotation/VAR_039513|||http://purl.uniprot.org/annotation/VAR_039514|||http://purl.uniprot.org/annotation/VAR_039515|||http://purl.uniprot.org/annotation/VAR_039516|||http://purl.uniprot.org/annotation/VAR_039517|||http://purl.uniprot.org/annotation/VAR_039518|||http://purl.uniprot.org/annotation/VAR_039519|||http://purl.uniprot.org/annotation/VAR_039520|||http://purl.uniprot.org/annotation/VAR_039521|||http://purl.uniprot.org/annotation/VAR_039522|||http://purl.uniprot.org/annotation/VAR_039523|||http://purl.uniprot.org/annotation/VAR_039524|||http://purl.uniprot.org/annotation/VAR_039525|||http://purl.uniprot.org/annotation/VAR_039526|||http://purl.uniprot.org/annotation/VAR_039527|||http://purl.uniprot.org/annotation/VAR_039528|||http://purl.uniprot.org/annotation/VAR_039529|||http://purl.uniprot.org/annotation/VAR_039530|||http://purl.uniprot.org/annotation/VAR_039531|||http://purl.uniprot.org/annotation/VAR_039532|||http://purl.uniprot.org/annotation/VAR_039533|||http://purl.uniprot.org/annotation/VAR_039534|||http://purl.uniprot.org/annotation/VAR_039535|||http://purl.uniprot.org/annotation/VAR_039536|||http://purl.uniprot.org/annotation/VAR_039537|||http://purl.uniprot.org/annotation/VAR_039538|||http://purl.uniprot.org/annotation/VAR_039539|||http://purl.uniprot.org/annotation/VAR_039540|||http://purl.uniprot.org/annotation/VAR_060106|||http://purl.uniprot.org/annotation/VAR_075931|||http://purl.uniprot.org/annotation/VAR_075932|||http://purl.uniprot.org/annotation/VAR_075933|||http://purl.uniprot.org/annotation/VAR_075934|||http://purl.uniprot.org/annotation/VAR_075935|||http://purl.uniprot.org/annotation/VAR_075936|||http://purl.uniprot.org/annotation/VAR_075937|||http://purl.uniprot.org/annotation/VAR_075938|||http://purl.uniprot.org/annotation/VAR_075939|||http://purl.uniprot.org/annotation/VAR_075940|||http://purl.uniprot.org/annotation/VAR_075941|||http://purl.uniprot.org/annotation/VAR_075942|||http://purl.uniprot.org/annotation/VAR_075943|||http://purl.uniprot.org/annotation/VAR_075944|||http://purl.uniprot.org/annotation/VAR_075945|||http://purl.uniprot.org/annotation/VAR_075946|||http://purl.uniprot.org/annotation/VAR_075947|||http://purl.uniprot.org/annotation/VAR_075948|||http://purl.uniprot.org/annotation/VAR_075949|||http://purl.uniprot.org/annotation/VAR_075950|||http://purl.uniprot.org/annotation/VAR_075951|||http://purl.uniprot.org/annotation/VAR_075952|||http://purl.uniprot.org/annotation/VAR_075953|||http://purl.uniprot.org/annotation/VAR_075954|||http://purl.uniprot.org/annotation/VAR_075955|||http://purl.uniprot.org/annotation/VAR_075956|||http://purl.uniprot.org/annotation/VAR_075957|||http://purl.uniprot.org/annotation/VAR_075958|||http://purl.uniprot.org/annotation/VAR_075959|||http://purl.uniprot.org/annotation/VAR_075960|||http://purl.uniprot.org/annotation/VAR_075961|||http://purl.uniprot.org/annotation/VAR_075962|||http://purl.uniprot.org/annotation/VAR_075963|||http://purl.uniprot.org/annotation/VAR_075964|||http://purl.uniprot.org/annotation/VAR_075965|||http://purl.uniprot.org/annotation/VAR_075966|||http://purl.uniprot.org/annotation/VAR_075967|||http://purl.uniprot.org/annotation/VAR_075968|||http://purl.uniprot.org/annotation/VAR_075969|||http://purl.uniprot.org/annotation/VAR_075970|||http://purl.uniprot.org/annotation/VAR_075971|||http://purl.uniprot.org/annotation/VAR_075972|||http://purl.uniprot.org/annotation/VAR_075973|||http://purl.uniprot.org/annotation/VAR_075974|||http://purl.uniprot.org/annotation/VAR_075975|||http://purl.uniprot.org/annotation/VAR_075976|||http://purl.uniprot.org/annotation/VAR_088220|||http://purl.uniprot.org/annotation/VAR_088221|||http://purl.uniprot.org/annotation/VAR_088222|||http://purl.uniprot.org/annotation/VAR_088223|||http://purl.uniprot.org/annotation/VAR_088224|||http://purl.uniprot.org/annotation/VSP_036318|||http://purl.uniprot.org/annotation/VSP_040100
http://togogenome.org/gene/9606:TRMT61B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVS5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of ability to catalyze the formation of 1-methyladenosine at position 947 of mitochondrial 16S ribosomal RNA.|||Mitochondrion|||Polar residues|||Substrate|||tRNA (adenine(58)-N(1))-methyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311814
http://togogenome.org/gene/9606:SDR42E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUS8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Proton acceptor|||Short-chain dehydrogenase/reductase family 42E member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331754|||http://purl.uniprot.org/annotation/VAR_055344|||http://purl.uniprot.org/annotation/VAR_055345|||http://purl.uniprot.org/annotation/VAR_055346
http://togogenome.org/gene/9606:SORCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes generation of the 104 kDa chain.|||BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||Cleavage|||Cytoplasmic|||Decreased proteolytic processing; when associated with 116-A--A-119.|||Decreased proteolytic processing; when associated with 66-A--A-69.|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PKD|||Pro residues|||SorCS2 104 kDa chain|||SorCS2 122 kDa chain|||SorCS2 18 kDa chain|||Strongly increases generation of the 104 kDa chain.|||VPS10 domain-containing receptor SorCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033172|||http://purl.uniprot.org/annotation/PRO_0000447469|||http://purl.uniprot.org/annotation/PRO_0000447470|||http://purl.uniprot.org/annotation/PRO_0000447471|||http://purl.uniprot.org/annotation/VAR_060109|||http://purl.uniprot.org/annotation/VAR_060110|||http://purl.uniprot.org/annotation/VAR_060111
http://togogenome.org/gene/9606:MYO15B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JP2|||http://purl.uniprot.org/uniprot/Q9H614                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||FERM|||IQ|||MyTH4|||Myosin motor|||Polar residues|||Pro residues|||SH3|||Unconventional myosin-XVB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292047|||http://purl.uniprot.org/annotation/VAR_080141
http://togogenome.org/gene/9606:ZNF471                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX82                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 471                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047603|||http://purl.uniprot.org/annotation/VAR_035583|||http://purl.uniprot.org/annotation/VAR_052836|||http://purl.uniprot.org/annotation/VAR_052837|||http://purl.uniprot.org/annotation/VAR_052838|||http://purl.uniprot.org/annotation/VAR_061951|||http://purl.uniprot.org/annotation/VSP_055955|||http://purl.uniprot.org/annotation/VSP_055956
http://togogenome.org/gene/9606:CACNA2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY47                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cache|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with progressive myoclonus epilepsy and developmental delay; unknown pathological significance.|||Helical|||In CASVDD; impaired regulation of current density and inactivation kinetics of N- and L-type calcium channels.|||In CASVDD; unknown pathological significance.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||Interchain (between alpha-2-2 and delta-2 chains)|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFA|||Voltage-dependent calcium channel subunit alpha-2-2|||Voltage-dependent calcium channel subunit alpha-2/delta-2|||Voltage-dependent calcium channel subunit delta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304637|||http://purl.uniprot.org/annotation/PRO_0000304638|||http://purl.uniprot.org/annotation/PRO_0000304639|||http://purl.uniprot.org/annotation/VAR_035048|||http://purl.uniprot.org/annotation/VAR_057782|||http://purl.uniprot.org/annotation/VAR_083105|||http://purl.uniprot.org/annotation/VAR_083106|||http://purl.uniprot.org/annotation/VAR_083107|||http://purl.uniprot.org/annotation/VAR_085040|||http://purl.uniprot.org/annotation/VSP_028058|||http://purl.uniprot.org/annotation/VSP_028059|||http://purl.uniprot.org/annotation/VSP_028060
http://togogenome.org/gene/9606:SV2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L1I2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239768|||http://purl.uniprot.org/annotation/VSP_045194
http://togogenome.org/gene/9606:LYPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBR3|||http://purl.uniprot.org/uniprot/O95274                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GPI-anchor amidated cysteine|||Ly6/PLAUR domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||UPAR/Ly6|||UPAR/Ly6 1|||UPAR/Ly6 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226751|||http://purl.uniprot.org/annotation/PRO_0000226752|||http://purl.uniprot.org/annotation/PRO_5014298298
http://togogenome.org/gene/9606:LRFN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V364|||http://purl.uniprot.org/uniprot/Q96NI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type-III domain-containing protein 5|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014845|||http://purl.uniprot.org/annotation/PRO_5003457118
http://togogenome.org/gene/9606:FLYWCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VC44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FLYWCH-type 1|||FLYWCH-type 2|||FLYWCH-type 3|||FLYWCH-type 4|||FLYWCH-type 5|||FLYWCH-type zinc finger-containing protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314460|||http://purl.uniprot.org/annotation/VSP_030277|||http://purl.uniprot.org/annotation/VSP_030278|||http://purl.uniprot.org/annotation/VSP_030279|||http://purl.uniprot.org/annotation/VSP_030280|||http://purl.uniprot.org/annotation/VSP_030281
http://togogenome.org/gene/9606:CHAF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13111                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CBX5; when associated with E-240.|||Abolishes interaction with CBX5; when associated with E-242.|||Acidic residues|||Basic and acidic residues|||Binds to CBX1 chromo shadow domain|||Binds to PCNA|||Binds to p60|||Chromatin assembly factor 1 subunit A|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Necessary for homodimerization and competence for chromatin assembly|||Phosphoserine|||Phosphothreonine|||Polar residues|||PxVxL motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089276|||http://purl.uniprot.org/annotation/VAR_055329|||http://purl.uniprot.org/annotation/VAR_055330|||http://purl.uniprot.org/annotation/VAR_055331|||http://purl.uniprot.org/annotation/VAR_055332|||http://purl.uniprot.org/annotation/VAR_055333|||http://purl.uniprot.org/annotation/VSP_004149|||http://purl.uniprot.org/annotation/VSP_004150|||http://purl.uniprot.org/annotation/VSP_004151
http://togogenome.org/gene/9606:TMEM64                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YI46                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Transmembrane protein 64|||VTT domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287342|||http://purl.uniprot.org/annotation/VSP_025441|||http://purl.uniprot.org/annotation/VSP_025442|||http://purl.uniprot.org/annotation/VSP_044998|||http://purl.uniprot.org/annotation/VSP_044999
http://togogenome.org/gene/9606:HSD17B14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPX1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase 14|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054654|||http://purl.uniprot.org/annotation/VAR_052307|||http://purl.uniprot.org/annotation/VAR_052308
http://togogenome.org/gene/9606:IGFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Immunoglobulin-like and fibronectin type III domain-containing protein 1|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347186|||http://purl.uniprot.org/annotation/VAR_046035|||http://purl.uniprot.org/annotation/VAR_046036|||http://purl.uniprot.org/annotation/VSP_035055|||http://purl.uniprot.org/annotation/VSP_035056|||http://purl.uniprot.org/annotation/VSP_035057|||http://purl.uniprot.org/annotation/VSP_035058|||http://purl.uniprot.org/annotation/VSP_035059|||http://purl.uniprot.org/annotation/VSP_035060|||http://purl.uniprot.org/annotation/VSP_045740
http://togogenome.org/gene/9606:KLHL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6TFL4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||In CMH29; loss-of-function variant unable to rescue heart defects and cardiac failure in zebrafish morphants.|||In isoform 2.|||Increased protein stability.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 24|||Weak interaction with CUL3. Weak autoubiquitination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261594|||http://purl.uniprot.org/annotation/VAR_088094|||http://purl.uniprot.org/annotation/VAR_088095|||http://purl.uniprot.org/annotation/VSP_028644|||http://purl.uniprot.org/annotation/VSP_028645
http://togogenome.org/gene/9606:MRGPRE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SM8|||http://purl.uniprot.org/uniprot/W4VSQ4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069760|||http://purl.uniprot.org/annotation/VAR_059325|||http://purl.uniprot.org/annotation/VAR_059326
http://togogenome.org/gene/9606:TMPRSS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57727                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Fails to undergo proteolytic cleavage and is unable to activate ENaC.|||Helical; Signal-anchor for type II membrane protein|||In DFNB8.|||In DFNB8; fails to undergo proteolytic cleavage and is unable to activate ENaC.|||In isoform 6.|||In isoform B.|||In isoform D.|||In isoform E.|||In isoform T.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Transmembrane protease serine 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088690|||http://purl.uniprot.org/annotation/VAR_010781|||http://purl.uniprot.org/annotation/VAR_011678|||http://purl.uniprot.org/annotation/VAR_011679|||http://purl.uniprot.org/annotation/VAR_013101|||http://purl.uniprot.org/annotation/VAR_013490|||http://purl.uniprot.org/annotation/VAR_013491|||http://purl.uniprot.org/annotation/VAR_013492|||http://purl.uniprot.org/annotation/VAR_013493|||http://purl.uniprot.org/annotation/VAR_013494|||http://purl.uniprot.org/annotation/VAR_013495|||http://purl.uniprot.org/annotation/VAR_013496|||http://purl.uniprot.org/annotation/VAR_025354|||http://purl.uniprot.org/annotation/VSP_005391|||http://purl.uniprot.org/annotation/VSP_005392|||http://purl.uniprot.org/annotation/VSP_005393|||http://purl.uniprot.org/annotation/VSP_005394|||http://purl.uniprot.org/annotation/VSP_013184|||http://purl.uniprot.org/annotation/VSP_047695
http://togogenome.org/gene/9606:ADAM20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0E3|||http://purl.uniprot.org/uniprot/O43506                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 20|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029106|||http://purl.uniprot.org/annotation/PRO_0000029107|||http://purl.uniprot.org/annotation/VAR_047311
http://togogenome.org/gene/9606:SARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP81                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In HUPRAS.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Serine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035822|||http://purl.uniprot.org/annotation/VAR_052645|||http://purl.uniprot.org/annotation/VAR_052646|||http://purl.uniprot.org/annotation/VAR_065820|||http://purl.uniprot.org/annotation/VSP_043020
http://togogenome.org/gene/9606:ARHGAP11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KRB8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Transit Peptide                                                                                  ^@                                                                                  Inactive Rho GTPase-activating protein 11B|||Mitochondrion|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317291
http://togogenome.org/gene/9606:SLC25A18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1K4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial glutamate carrier 2|||Phosphoserine|||Polar residues|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090621
http://togogenome.org/gene/9606:OR10H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW93|||http://purl.uniprot.org/uniprot/O60404                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 10H3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150704|||http://purl.uniprot.org/annotation/VAR_020381|||http://purl.uniprot.org/annotation/VAR_020382|||http://purl.uniprot.org/annotation/VAR_024128|||http://purl.uniprot.org/annotation/VAR_034288|||http://purl.uniprot.org/annotation/VAR_034289
http://togogenome.org/gene/9606:HELB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Accumulation in the nucleus due to defects in nuclear export.|||Basic and acidic residues|||DNA helicase B|||Disordered|||Does not affect subcellular location.|||Impaired phosphorylation, inducing accumulation in the nucleus.|||In isoform 2.|||Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-499 and A-506.|||Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-499 and A-510.|||Loss of RPA1-binding, leading to impaired recruitment to sites of double-strand breaks; when associated with A-506 and A-510.|||No ATPase activity.|||Nuclear export signal|||Phosphomimetic mutant; leads to higher localization to the cytoplasm.|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338992|||http://purl.uniprot.org/annotation/VAR_043855|||http://purl.uniprot.org/annotation/VAR_043856|||http://purl.uniprot.org/annotation/VAR_043857|||http://purl.uniprot.org/annotation/VAR_043858|||http://purl.uniprot.org/annotation/VAR_043859|||http://purl.uniprot.org/annotation/VAR_061665|||http://purl.uniprot.org/annotation/VSP_034086|||http://purl.uniprot.org/annotation/VSP_034087
http://togogenome.org/gene/9606:DEFB4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15263                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Mutagenesis Site|||Peptide|||Region|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Defensin beta 4A|||Loss of PIP2 binding and loss of liposomal lysis activity. Decrease in fungal cell permeabilization. Impaired antifungal activity.|||Loss of PIP2 binding and reduced liposomal lysis activity. Impaired antifungal activity. Decrease in fungal cell permeabilization.|||No impact on PIP binding and liposomal lysis activity. Lack of antifungal activity. Lack of fungal cell permeabilization.|||No impact on fungal cell permeabilization. Impaired antifungal activity.|||No impact on fungal cell permeabilization. No impact on antifungal activity.|||Phosphatidylinositol 4,5-bisphosphate (PIP2) binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006968
http://togogenome.org/gene/9606:USP17L17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RBQ6                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421091
http://togogenome.org/gene/9606:ASB15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYV2|||http://purl.uniprot.org/uniprot/Q8WXK1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 15|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066954|||http://purl.uniprot.org/annotation/VAR_060466|||http://purl.uniprot.org/annotation/VAR_060467
http://togogenome.org/gene/9606:SLC49A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Solute carrier family 49 member A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273408|||http://purl.uniprot.org/annotation/VAR_030144|||http://purl.uniprot.org/annotation/VSP_022547|||http://purl.uniprot.org/annotation/VSP_022548|||http://purl.uniprot.org/annotation/VSP_022549
http://togogenome.org/gene/9606:DR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01658|||http://purl.uniprot.org/uniprot/Q658N3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Histone-fold|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein Dr1|||Removed|||Transcription factor CBF/NF-Y/archaeal histone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072440|||http://purl.uniprot.org/annotation/VAR_034506
http://togogenome.org/gene/9606:BATF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic leucine zipper transcriptional factor ATF-like 3|||Basic motif|||Disordered|||Leucine-zipper|||Phosphoserine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326106|||http://purl.uniprot.org/annotation/VAR_039988
http://togogenome.org/gene/9606:JAKMIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AA8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Janus kinase and microtubule-interacting protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050762|||http://purl.uniprot.org/annotation/VAR_022059|||http://purl.uniprot.org/annotation/VAR_035930|||http://purl.uniprot.org/annotation/VSP_002430|||http://purl.uniprot.org/annotation/VSP_028230|||http://purl.uniprot.org/annotation/VSP_055264
http://togogenome.org/gene/9606:PIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12273                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Prolactin-inducible protein|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024288
http://togogenome.org/gene/9606:LBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XYB7                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with atrial septal defects; unknown pathological significance.|||Homeobox|||In isoform 2.|||Transcription factor LBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311328|||http://purl.uniprot.org/annotation/VAR_037227|||http://purl.uniprot.org/annotation/VAR_083939|||http://purl.uniprot.org/annotation/VAR_083940|||http://purl.uniprot.org/annotation/VSP_029522
http://togogenome.org/gene/9606:TMEM47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQJ4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylalanine|||Removed|||Transmembrane protein 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072573
http://togogenome.org/gene/9606:PTPRCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14761                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Protein tyrosine phosphatase receptor type C-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097087|||http://purl.uniprot.org/annotation/VAR_061698
http://togogenome.org/gene/9606:WFDC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUB5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  WAP four-disulfide core domain protein 13|||WAP; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041393
http://togogenome.org/gene/9606:TRIM49D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J1S8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 49D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395402
http://togogenome.org/gene/9606:ESR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A125SXW3|||http://purl.uniprot.org/uniprot/A8KAF4|||http://purl.uniprot.org/uniprot/G4XH65|||http://purl.uniprot.org/uniprot/H0Y4W6|||http://purl.uniprot.org/uniprot/P03372|||http://purl.uniprot.org/uniprot/Q9UBT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with NCOA1, NCOA2 and NCOA3.|||Asymmetric dimethylarginine; by PRMT1|||Decreases phosphorylation and transactivation activity. Abolishes AF-1 transactivation. Insensitive to PPP5C inhibition of transactivation activity.|||Destabilizes the receptor and decreases its affinity for estradiol at 25 degrees Celsius, but not at 4 degrees Celsius.|||Disordered|||Enhances transactivation activity. Insensitive to PPP5C inhibition of transactivation activity.|||Estrogen receptor|||Has higher transcriptional activity in the absence of wild type ER. Inhibits transcriptional activity when coexpressed with the wild type receptor.|||Hinge|||Impairs AF-1 transactivation.|||In ESTRR; highly decreased estrogen receptor activity.|||In ESTRR; results in highly reduced activity.|||In a 80 kDa form found in a breast cancer line; contains an in-frame duplication of exons 6 and 7.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with AKAP13|||Interaction with DDX5; self-association|||Loss of cyclin A-dependent induction of transcriptional activation.|||Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding.|||Loss of methylation.|||Loss of transmembrane localization, no effect on peripheral membrane localization. Impairs activation of estrogen-induced activation of NOS3 and production of nitric oxide. No effect on binding to ERES.|||Mediates interaction with DNTTIP2|||Modulating (transactivation AF-1); mediates interaction with MACROD1|||NR C4-type|||NR LBD|||Nuclear receptor|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by CK2|||Phosphotyrosine; by Tyr-kinases|||Polar residues|||Reduces PELP1-mediated activation of transcriptional activity.|||Required for interaction with NCOA1|||S-palmitoyl cysteine|||Self-association|||Transactivation AF-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053618|||http://purl.uniprot.org/annotation/VAR_004671|||http://purl.uniprot.org/annotation/VAR_004673|||http://purl.uniprot.org/annotation/VAR_010143|||http://purl.uniprot.org/annotation/VAR_018905|||http://purl.uniprot.org/annotation/VAR_033028|||http://purl.uniprot.org/annotation/VAR_033029|||http://purl.uniprot.org/annotation/VAR_070072|||http://purl.uniprot.org/annotation/VAR_078516|||http://purl.uniprot.org/annotation/VSP_003680|||http://purl.uniprot.org/annotation/VSP_042460|||http://purl.uniprot.org/annotation/VSP_042461
http://togogenome.org/gene/9606:CCDC68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2F9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264611|||http://purl.uniprot.org/annotation/VAR_050762
http://togogenome.org/gene/9606:SLC6A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3W8|||http://purl.uniprot.org/uniprot/B7Z589|||http://purl.uniprot.org/uniprot/P48067                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for interaction with EXOC1|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In GCENSG.|||In isoform GlyT-1A.|||In isoform GlyT-1B.|||Phosphoserine|||Sodium- and chloride-dependent glycine transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214780|||http://purl.uniprot.org/annotation/VAR_078074|||http://purl.uniprot.org/annotation/VSP_006270|||http://purl.uniprot.org/annotation/VSP_006271
http://togogenome.org/gene/9606:MZT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AG7                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Mitotic-spindle organizing protein 1|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337015|||http://purl.uniprot.org/annotation/VAR_043562
http://togogenome.org/gene/9606:CIB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YKC8|||http://purl.uniprot.org/uniprot/O75838                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Mass|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mass|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcium and integrin-binding family member 2|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Found in a family with deafness; unknown pathological significance; the patient also carries a likely disease-causing mutation in PDZD7.|||In DFNB48.|||In DFNB48; decreases interaction with TMC1 and TMC2; no loss of localization to stereocilia; does not affect ATP-induced calcium release;.|||In DFNB48; inhibits the ability to decrease ATP-induced calcium release; ; decreases interaction with TMC1 and TMC2; does not affect the localization in the cuticular plate or to the tip of stereocilia; does not affect binding with WHRN.|||In DFNB48; inhibits the ability to decrease ATP-induced calcium release; decreases interaction with TMC1 and TMC2.|||In DFNB48; stimulates the ability to decrease ATP-induced calcium release; decreases interaction with TMC1 and TMC2.|||In DFNB48; unknown pathological significance.|||In DFNB48; unknown pathological significance; decreases interaction with TMC1 and TMC2; no loss of localization to stereocilia; does not affect ATP-induced calcium release.|||In USH1J and DFNB48; decreases interaction with TMC1 and TMC2.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073534|||http://purl.uniprot.org/annotation/VAR_069086|||http://purl.uniprot.org/annotation/VAR_069087|||http://purl.uniprot.org/annotation/VAR_069088|||http://purl.uniprot.org/annotation/VAR_069089|||http://purl.uniprot.org/annotation/VAR_074552|||http://purl.uniprot.org/annotation/VAR_077559|||http://purl.uniprot.org/annotation/VAR_080825|||http://purl.uniprot.org/annotation/VAR_087038|||http://purl.uniprot.org/annotation/VAR_087039|||http://purl.uniprot.org/annotation/VSP_053863|||http://purl.uniprot.org/annotation/VSP_053864|||http://purl.uniprot.org/annotation/VSP_054777
http://togogenome.org/gene/9606:DENND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUS2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DENN domain-containing protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Linker|||Phosphoserine; by ULK1|||Phosphotyrosine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304672|||http://purl.uniprot.org/annotation/VAR_035053|||http://purl.uniprot.org/annotation/VAR_035054|||http://purl.uniprot.org/annotation/VSP_028075|||http://purl.uniprot.org/annotation/VSP_028077|||http://purl.uniprot.org/annotation/VSP_028078|||http://purl.uniprot.org/annotation/VSP_028080|||http://purl.uniprot.org/annotation/VSP_028081
http://togogenome.org/gene/9606:WHRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EGE6|||http://purl.uniprot.org/uniprot/Q9P202                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Polar residues|||Whirlin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065968|||http://purl.uniprot.org/annotation/VAR_020593|||http://purl.uniprot.org/annotation/VAR_020594|||http://purl.uniprot.org/annotation/VAR_020595|||http://purl.uniprot.org/annotation/VAR_020596|||http://purl.uniprot.org/annotation/VAR_036684|||http://purl.uniprot.org/annotation/VAR_036685|||http://purl.uniprot.org/annotation/VAR_036686|||http://purl.uniprot.org/annotation/VAR_036687|||http://purl.uniprot.org/annotation/VAR_036688|||http://purl.uniprot.org/annotation/VAR_057029|||http://purl.uniprot.org/annotation/VSP_012216|||http://purl.uniprot.org/annotation/VSP_012217|||http://purl.uniprot.org/annotation/VSP_012218|||http://purl.uniprot.org/annotation/VSP_012219|||http://purl.uniprot.org/annotation/VSP_012220
http://togogenome.org/gene/9606:MAP2K5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13163                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dual specificity mitogen-activated protein kinase kinase 5|||In isoform 4.|||In isoform A and isoform C.|||In isoform C.|||Inactivation.|||Interaction with MAP3K2/MAP3K3|||Interaction with MAPK7|||PB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086383|||http://purl.uniprot.org/annotation/VAR_040823|||http://purl.uniprot.org/annotation/VAR_040824|||http://purl.uniprot.org/annotation/VAR_046070|||http://purl.uniprot.org/annotation/VSP_021825|||http://purl.uniprot.org/annotation/VSP_021826|||http://purl.uniprot.org/annotation/VSP_043333
http://togogenome.org/gene/9606:GAPDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04406|||http://purl.uniprot.org/uniprot/V9HVZ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited form|||Activates thiol group during catalysis|||Cysteine persulfide|||Deamidated asparagine|||Does not affect glycosylation by C.rodentium protein NleB.|||Drastic reduction of the extent and significant prolongation of the lag phase of free radical-induced aggregation.|||Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding|||Glyceraldehyde-3-phosphate dehydrogenase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Increased free radical-induced aggregation.|||Increased resistance to free radical-induced aggregation.|||Inhibits S-nitrosylation of Cys-247; when associated with M-245.|||Inhibits S-nitrosylation of Cys-247; when associated with M-250.|||Interaction with WARS1|||Markedly reduced glycolytic activity; when associated with S-152 and S-156. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247.|||Markedly reduced glycolytic activity; when associated with S-152 and S-247. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247.|||Markedly reduced glycolytic activity; when associated with S-156 and S-247. Forms free radical-induced aggregates, but to a lesser extent than wild-type protein; when associated with S-156 and S-247. Abolished interaction with TRAF2 and TRAF3.|||Methionine sulfoxide; in vitro|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||No effect on free radical-induced aggregation.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||S-(2-succinyl)cysteine|||S-nitrosocysteine|||S-nitrosocysteine; in reversibly inhibited form|||[IL]-x-C-x-x-[DE] motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145486|||http://purl.uniprot.org/annotation/VAR_018889|||http://purl.uniprot.org/annotation/VAR_049218|||http://purl.uniprot.org/annotation/VSP_047289
http://togogenome.org/gene/9606:LIX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N485                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein limb expression 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232869|||http://purl.uniprot.org/annotation/VAR_026039
http://togogenome.org/gene/9606:CLVS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SYC1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  CRAL-TRIO|||Clavesin-2|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297651|||http://purl.uniprot.org/annotation/VSP_027325
http://togogenome.org/gene/9606:NDUFB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYD0|||http://purl.uniprot.org/uniprot/O43674                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020052|||http://purl.uniprot.org/annotation/VAR_050590|||http://purl.uniprot.org/annotation/VSP_042516
http://togogenome.org/gene/9606:AIRIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX04                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  AFG2-interacting ribosome maturation factor|||Abolishes phosphorylation by CK2 kinase; when associated with A-104 and A-134.|||Abolishes phosphorylation by CK2 kinase; when associated with A-104 and A-182.|||Abolishes phosphorylation by CK2 kinase; when associated with A-134 and A-182.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274382|||http://purl.uniprot.org/annotation/VSP_022733|||http://purl.uniprot.org/annotation/VSP_022734
http://togogenome.org/gene/9606:LACRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZZ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Extracellular glycoprotein lacritin|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021574
http://togogenome.org/gene/9606:WWP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHF6|||http://purl.uniprot.org/uniprot/O00308                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination of POU5F1.|||C2|||Disordered|||Does not affect FBXL15-mediated ubiquitination.|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NEDD4-like E3 ubiquitin-protein ligase WWP2|||Phosphoserine|||Polar residues|||WW|||WW 1|||WW 2|||WW 3|||WW 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120338|||http://purl.uniprot.org/annotation/VSP_044706|||http://purl.uniprot.org/annotation/VSP_046461|||http://purl.uniprot.org/annotation/VSP_054711
http://togogenome.org/gene/9606:SORCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K182|||http://purl.uniprot.org/uniprot/B3KVZ0|||http://purl.uniprot.org/uniprot/B3KWN9|||http://purl.uniprot.org/uniprot/E6Y3F9|||http://purl.uniprot.org/uniprot/E6Y3G0|||http://purl.uniprot.org/uniprot/Q8WY21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||PKD|||Polar residues|||VPS10 domain-containing receptor SorCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033170|||http://purl.uniprot.org/annotation/PRO_5002788691|||http://purl.uniprot.org/annotation/PRO_5003213743|||http://purl.uniprot.org/annotation/PRO_5003215858|||http://purl.uniprot.org/annotation/PRO_5010104052|||http://purl.uniprot.org/annotation/VAR_036374|||http://purl.uniprot.org/annotation/VSP_006204|||http://purl.uniprot.org/annotation/VSP_015140|||http://purl.uniprot.org/annotation/VSP_015141
http://togogenome.org/gene/9606:PARVA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVD7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Alpha-parvin|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In isoform 2.|||Interaction with ARHGAP31|||Loss of interaction with TESK1, however no effect on interaction with ILK; when associated with D-4.|||Loss of interaction with TESK1, however no effect on interaction with ILK; when associated with D-8.|||N-acetylalanine|||Phosphoserine|||Removed|||Required for interaction with TESK1 and ILK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121580|||http://purl.uniprot.org/annotation/VSP_008884|||http://purl.uniprot.org/annotation/VSP_008885
http://togogenome.org/gene/9606:ALDH1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94788                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DIH4; decreased expression.|||In DIH4; decreased retinoic acid biosynthetic process.|||In DIH4; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Retinal dehydrogenase 2|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056422|||http://purl.uniprot.org/annotation/VAR_025439|||http://purl.uniprot.org/annotation/VAR_025440|||http://purl.uniprot.org/annotation/VAR_025441|||http://purl.uniprot.org/annotation/VAR_025442|||http://purl.uniprot.org/annotation/VAR_087721|||http://purl.uniprot.org/annotation/VAR_087722|||http://purl.uniprot.org/annotation/VAR_087723|||http://purl.uniprot.org/annotation/VAR_087724|||http://purl.uniprot.org/annotation/VSP_017363|||http://purl.uniprot.org/annotation/VSP_044496|||http://purl.uniprot.org/annotation/VSP_047259
http://togogenome.org/gene/9606:IQSEC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JU85                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 2|||In XLID1.|||In XLID1; decreased guanine nucleotide exchange factor activity.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245608|||http://purl.uniprot.org/annotation/VAR_063742|||http://purl.uniprot.org/annotation/VAR_063743|||http://purl.uniprot.org/annotation/VAR_063744|||http://purl.uniprot.org/annotation/VAR_063745|||http://purl.uniprot.org/annotation/VAR_078260|||http://purl.uniprot.org/annotation/VSP_041372|||http://purl.uniprot.org/annotation/VSP_041373|||http://purl.uniprot.org/annotation/VSP_041374|||http://purl.uniprot.org/annotation/VSP_059605|||http://purl.uniprot.org/annotation/VSP_059606
http://togogenome.org/gene/9606:HECW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6F3|||http://purl.uniprot.org/uniprot/Q9P2P5                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase HECW2|||Glycyl thioester intermediate|||HECT|||In NDHSAL.|||In isoform 2.|||Interaction with TP73|||Phosphoserine|||Polar residues|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277667|||http://purl.uniprot.org/annotation/VAR_077905|||http://purl.uniprot.org/annotation/VAR_077906|||http://purl.uniprot.org/annotation/VAR_077907|||http://purl.uniprot.org/annotation/VAR_077908|||http://purl.uniprot.org/annotation/VSP_059106|||http://purl.uniprot.org/annotation/VSP_059107|||http://purl.uniprot.org/annotation/VSP_059108
http://togogenome.org/gene/9606:KLRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26717                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Impairs the expression of KLRD1-KLRC2 on the cell surface.|||In allele NKG2-C*02.|||Increases the affinity for HLA-E to a value similar to that observed for HLA-E-KLRD1-KLRC1 complex.|||N-linked (GlcNAc...) asparagine|||NKG2-C type II integral membrane protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046662|||http://purl.uniprot.org/annotation/VAR_013404|||http://purl.uniprot.org/annotation/VAR_013405
http://togogenome.org/gene/9606:ATP1B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54709                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sodium/potassium-transporting ATPase subunit beta-3|||immunoglobulin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219108|||http://purl.uniprot.org/annotation/VSP_056686|||http://purl.uniprot.org/annotation/VSP_056687
http://togogenome.org/gene/9606:PLCB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ66                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform B.|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088486|||http://purl.uniprot.org/annotation/VAR_036547|||http://purl.uniprot.org/annotation/VAR_050541|||http://purl.uniprot.org/annotation/VSP_004718
http://togogenome.org/gene/9606:ZNF90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03938                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 90                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047399
http://togogenome.org/gene/9606:FAM98C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RN3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Protein FAM98C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282428|||http://purl.uniprot.org/annotation/VAR_049030|||http://purl.uniprot.org/annotation/VSP_024142|||http://purl.uniprot.org/annotation/VSP_024143
http://togogenome.org/gene/9606:CCDC85B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15834                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 85B|||Disordered|||Loss of interaction with TCF7L2 and loss of suppression of CTNNB1 activity. Loss of cell growth inhibition.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079908
http://togogenome.org/gene/9606:TCF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GY10|||http://purl.uniprot.org/uniprot/Q99081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  9aaTAD|||BHLH|||Basic and acidic residues|||Class A specific domain|||Decreases interaction with RUNX1T1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CRS3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RUNX1T1|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor 12|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127228|||http://purl.uniprot.org/annotation/VAR_049543|||http://purl.uniprot.org/annotation/VAR_070096|||http://purl.uniprot.org/annotation/VAR_070097|||http://purl.uniprot.org/annotation/VAR_072271|||http://purl.uniprot.org/annotation/VSP_039109|||http://purl.uniprot.org/annotation/VSP_039110|||http://purl.uniprot.org/annotation/VSP_040024|||http://purl.uniprot.org/annotation/VSP_057419|||http://purl.uniprot.org/annotation/VSP_057420
http://togogenome.org/gene/9606:MYOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15173                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Myogenin|||Phosphoserine; by CaMK2G|||Phosphothreonine; by CaMK2G|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127375
http://togogenome.org/gene/9606:BAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92560                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Abolished interaction with FOXK1 and FOXK2.|||Abolishes enzymatic activity. Has no effect on interaction with HCFC1.|||Abolishes interaction with BRCA1.|||Abolishes interaction with HCFC1 without affecting interaction with FOXK1 and FOXK2.|||Abolishes nuclear localization.|||Abolishes ubiquitination by UBE2O.|||Basic residues|||Disordered|||Does not affect interaction with FOXK1 and FOXK2.|||Does not affect nuclear localization.|||Found in a malignant pleural mesothelioma cell line.|||Found in a malignant pleural mesothelioma sample.|||Found in a malignant pleural mesothelioma sample; somatic mutation.|||Found in a malignant pleural mesothelioma sample; somatic mutation; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates.|||Found in a primary uveal melanoma; somatic mutation; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates.|||HBM-like motif|||Important for enzyme activity|||In KURIS.|||In KURIS; loss-of-function variant; increased steady-state level of ubiquitinated H2A are found in patient cells; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; abolishes deubiquitinase activity without affecting its ability to interfere with BRCA1 E3 ligase activity; does not affect localization to the nucleus; has a dominant negative effect on cell growth; does not affect interaction with FOXK1 and FOXK2.|||In KURIS; loss-of-function variant; increased steady-state levels of ubiquitinated H2A are found in patient cells; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus.|||In KURIS; loss-of-function variant; unable to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus.|||In KURIS; unknown pathological significance.|||In KURIS; unknown pathological significance; able to rescue impaired H2AK119ub deubiquitination when expressed in BAP1-deficient cells; does not affect localization to the nucleus.|||In TPDS1.|||In TPDS1; significantly increased risk for renal cell carcinoma.|||In a lung cancer sample; also found in a malignant pleural mesothelioma cell line; induces cytoplasmic accumulation; loss of deubiquitinase activity; up-regulates heat shock response; induces formation of amyloid-beta aggregates.|||In a lung cancer sample; induces cytoplasmic accumulation; impairs deubiquitinase activity; up-regulates heat shock response; induces formation of beta-amyloid aggregates.|||Interaction with BRCA1|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase BAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211069|||http://purl.uniprot.org/annotation/VAR_051517|||http://purl.uniprot.org/annotation/VAR_063498|||http://purl.uniprot.org/annotation/VAR_063499|||http://purl.uniprot.org/annotation/VAR_065976|||http://purl.uniprot.org/annotation/VAR_065977|||http://purl.uniprot.org/annotation/VAR_065978|||http://purl.uniprot.org/annotation/VAR_065979|||http://purl.uniprot.org/annotation/VAR_065980|||http://purl.uniprot.org/annotation/VAR_075251|||http://purl.uniprot.org/annotation/VAR_086937|||http://purl.uniprot.org/annotation/VAR_086938|||http://purl.uniprot.org/annotation/VAR_086939|||http://purl.uniprot.org/annotation/VAR_086940|||http://purl.uniprot.org/annotation/VAR_086941|||http://purl.uniprot.org/annotation/VAR_086942|||http://purl.uniprot.org/annotation/VAR_086943|||http://purl.uniprot.org/annotation/VAR_086944|||http://purl.uniprot.org/annotation/VAR_086945|||http://purl.uniprot.org/annotation/VAR_087531|||http://purl.uniprot.org/annotation/VAR_087532
http://togogenome.org/gene/9606:LAMB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55268                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Domain I|||Domain II|||Domain alpha|||In NPHS5.|||In NPHS5; unknown pathological significance.|||In PIERS and NPHS5; with mild ocular abnormalities.|||In PIERS and NPHS5; with mild ocular abnormalities; associated with F-1393.|||In PIERS and NPHS5; with mild ocular abnormalities; associated with K-1380.|||In PIERS.|||In PIERS; without ocular abnormalities.|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; truncated|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin IV type B|||Laminin N-terminal|||Laminin subunit beta-2|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017068|||http://purl.uniprot.org/annotation/VAR_031968|||http://purl.uniprot.org/annotation/VAR_031969|||http://purl.uniprot.org/annotation/VAR_031970|||http://purl.uniprot.org/annotation/VAR_031971|||http://purl.uniprot.org/annotation/VAR_031972|||http://purl.uniprot.org/annotation/VAR_031973|||http://purl.uniprot.org/annotation/VAR_066492|||http://purl.uniprot.org/annotation/VAR_087602|||http://purl.uniprot.org/annotation/VAR_087603|||http://purl.uniprot.org/annotation/VAR_087604|||http://purl.uniprot.org/annotation/VAR_087605|||http://purl.uniprot.org/annotation/VAR_087606
http://togogenome.org/gene/9606:OBSCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGQ3|||http://purl.uniprot.org/uniprot/Q5VST9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||IQ|||Ig-like|||Ig-like 1|||Ig-like 10|||Ig-like 11|||Ig-like 12|||Ig-like 13|||Ig-like 14|||Ig-like 15|||Ig-like 16|||Ig-like 17|||Ig-like 18|||Ig-like 19|||Ig-like 2|||Ig-like 20|||Ig-like 21|||Ig-like 22|||Ig-like 23|||Ig-like 24|||Ig-like 25|||Ig-like 26|||Ig-like 27|||Ig-like 28|||Ig-like 29|||Ig-like 3|||Ig-like 30|||Ig-like 31|||Ig-like 32|||Ig-like 33|||Ig-like 34|||Ig-like 35|||Ig-like 36|||Ig-like 37|||Ig-like 38|||Ig-like 39|||Ig-like 4|||Ig-like 40|||Ig-like 41|||Ig-like 42|||Ig-like 43|||Ig-like 44|||Ig-like 45|||Ig-like 46|||Ig-like 47|||Ig-like 48|||Ig-like 49|||Ig-like 5|||Ig-like 50|||Ig-like 51|||Ig-like 52|||Ig-like 53|||Ig-like 54|||Ig-like 55|||Ig-like 6|||Ig-like 7|||Ig-like 8|||Ig-like 9|||In RHABDO1; associated with disease susceptibility.|||In RHABDO1; associated with disease susceptibility; greatly reduced protein levels detected by Wester blot in skeletal muscle from a homozygous patient.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Obscurin|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Reduced binding to phosphatidylinositol 3,4-bisphosphate.|||Reduced binding to phosphatidylinositol 4,5-bisphosphate.|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235298|||http://purl.uniprot.org/annotation/VAR_026409|||http://purl.uniprot.org/annotation/VAR_026410|||http://purl.uniprot.org/annotation/VAR_034618|||http://purl.uniprot.org/annotation/VAR_034619|||http://purl.uniprot.org/annotation/VAR_034620|||http://purl.uniprot.org/annotation/VAR_034621|||http://purl.uniprot.org/annotation/VAR_034622|||http://purl.uniprot.org/annotation/VAR_035530|||http://purl.uniprot.org/annotation/VAR_035531|||http://purl.uniprot.org/annotation/VAR_035532|||http://purl.uniprot.org/annotation/VAR_035533|||http://purl.uniprot.org/annotation/VAR_035534|||http://purl.uniprot.org/annotation/VAR_035535|||http://purl.uniprot.org/annotation/VAR_035536|||http://purl.uniprot.org/annotation/VAR_035537|||http://purl.uniprot.org/annotation/VAR_035538|||http://purl.uniprot.org/annotation/VAR_042276|||http://purl.uniprot.org/annotation/VAR_042277|||http://purl.uniprot.org/annotation/VAR_042278|||http://purl.uniprot.org/annotation/VAR_042279|||http://purl.uniprot.org/annotation/VAR_042280|||http://purl.uniprot.org/annotation/VAR_042281|||http://purl.uniprot.org/annotation/VAR_042282|||http://purl.uniprot.org/annotation/VAR_042283|||http://purl.uniprot.org/annotation/VAR_042284|||http://purl.uniprot.org/annotation/VAR_042285|||http://purl.uniprot.org/annotation/VAR_042286|||http://purl.uniprot.org/annotation/VAR_042287|||http://purl.uniprot.org/annotation/VAR_042288|||http://purl.uniprot.org/annotation/VAR_042289|||http://purl.uniprot.org/annotation/VAR_042290|||http://purl.uniprot.org/annotation/VAR_042291|||http://purl.uniprot.org/annotation/VAR_042292|||http://purl.uniprot.org/annotation/VAR_042293|||http://purl.uniprot.org/annotation/VAR_042294|||http://purl.uniprot.org/annotation/VAR_047743|||http://purl.uniprot.org/annotation/VAR_047744|||http://purl.uniprot.org/annotation/VAR_047745|||http://purl.uniprot.org/annotation/VAR_047746|||http://purl.uniprot.org/annotation/VAR_047747|||http://purl.uniprot.org/annotation/VAR_047748|||http://purl.uniprot.org/annotation/VAR_047749|||http://purl.uniprot.org/annotation/VAR_047750|||http://purl.uniprot.org/annotation/VAR_047751|||http://purl.uniprot.org/annotation/VAR_056102|||http://purl.uniprot.org/annotation/VAR_056103|||http://purl.uniprot.org/annotation/VAR_056104|||http://purl.uniprot.org/annotation/VAR_056105|||http://purl.uniprot.org/annotation/VAR_056106|||http://purl.uniprot.org/annotation/VAR_056107|||http://purl.uniprot.org/annotation/VAR_056108|||http://purl.uniprot.org/annotation/VAR_056109|||http://purl.uniprot.org/annotation/VAR_059429|||http://purl.uniprot.org/annotation/VAR_074295|||http://purl.uniprot.org/annotation/VAR_088090|||http://purl.uniprot.org/annotation/VAR_088091|||http://purl.uniprot.org/annotation/VAR_088092|||http://purl.uniprot.org/annotation/VAR_088093|||http://purl.uniprot.org/annotation/VSP_018436|||http://purl.uniprot.org/annotation/VSP_018437|||http://purl.uniprot.org/annotation/VSP_018438|||http://purl.uniprot.org/annotation/VSP_020086|||http://purl.uniprot.org/annotation/VSP_020087|||http://purl.uniprot.org/annotation/VSP_026970
http://togogenome.org/gene/9606:MAP3K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KRN4|||http://purl.uniprot.org/uniprot/Q96HN9|||http://purl.uniprot.org/uniprot/Q99759                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitogen-activated protein kinase kinase kinase 3|||PB1|||Phosphoserine|||Phosphoserine; by SGK1|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086245|||http://purl.uniprot.org/annotation/VAR_037275|||http://purl.uniprot.org/annotation/VAR_037276|||http://purl.uniprot.org/annotation/VAR_040685|||http://purl.uniprot.org/annotation/VSP_035967
http://togogenome.org/gene/9606:RNF144B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z419                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RNF144B|||Helical|||IBR-type|||In isoform 2.|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055911|||http://purl.uniprot.org/annotation/VSP_055853|||http://purl.uniprot.org/annotation/VSP_055854
http://togogenome.org/gene/9606:GNG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50151                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10|||N-acetylserine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012655|||http://purl.uniprot.org/annotation/PRO_0000012656
http://togogenome.org/gene/9606:CLEC4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMR7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member A|||Cytoplasmic|||Decreases HIV-1 binding/entry in cells as well as virus replication.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046612|||http://purl.uniprot.org/annotation/VAR_021260|||http://purl.uniprot.org/annotation/VSP_012842|||http://purl.uniprot.org/annotation/VSP_012844|||http://purl.uniprot.org/annotation/VSP_041348
http://togogenome.org/gene/9606:C2orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWW7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C2orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300121|||http://purl.uniprot.org/annotation/VAR_050712
http://togogenome.org/gene/9606:SLC7A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43246                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cationic amino acid transporter 4|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054269|||http://purl.uniprot.org/annotation/VAR_048155|||http://purl.uniprot.org/annotation/VAR_048156|||http://purl.uniprot.org/annotation/VAR_060989
http://togogenome.org/gene/9606:POLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYJ2|||http://purl.uniprot.org/uniprot/M0R2B7|||http://purl.uniprot.org/uniprot/P28340|||http://purl.uniprot.org/uniprot/Q308M6|||http://purl.uniprot.org/uniprot/Q59FA0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C4-type zinc-finger of DNA polymerase delta|||CysA-type|||CysB motif|||DNA polymerase delta catalytic subunit|||DNA-directed DNA polymerase family B exonuclease|||DNA-directed DNA polymerase family B multifunctional|||Disordered|||Found in a colorectal sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CRCS10.|||In CRCS10; associated with disease susceptibility.|||In MDPL; the mutant enzyme lacks DNA polymerase ability; has decreased exonuclease activity; can bind DNA but is unable to interact with and incorporate dNTPs.|||Loss of exonuclease activity. No effect on DNA polymerase activity.|||Nuclear localization signal|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046442|||http://purl.uniprot.org/annotation/VAR_016146|||http://purl.uniprot.org/annotation/VAR_019340|||http://purl.uniprot.org/annotation/VAR_019341|||http://purl.uniprot.org/annotation/VAR_019342|||http://purl.uniprot.org/annotation/VAR_019343|||http://purl.uniprot.org/annotation/VAR_019344|||http://purl.uniprot.org/annotation/VAR_019345|||http://purl.uniprot.org/annotation/VAR_048878|||http://purl.uniprot.org/annotation/VAR_048879|||http://purl.uniprot.org/annotation/VAR_048880|||http://purl.uniprot.org/annotation/VAR_069333|||http://purl.uniprot.org/annotation/VAR_069334|||http://purl.uniprot.org/annotation/VAR_069335|||http://purl.uniprot.org/annotation/VAR_069336|||http://purl.uniprot.org/annotation/VAR_069337|||http://purl.uniprot.org/annotation/VAR_069338|||http://purl.uniprot.org/annotation/VAR_070231|||http://purl.uniprot.org/annotation/VAR_071966
http://togogenome.org/gene/9606:GOLGA6L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZA4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 6-like protein 6|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332267
http://togogenome.org/gene/9606:CRTAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ79                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cartilage acidic protein 1|||EGF-like|||FG-GAP 1; atypical|||FG-GAP 2; atypical|||FG-GAP 3; atypical|||FG-GAP 4; atypical|||In isoform 2.|||In isoform 3.|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007497|||http://purl.uniprot.org/annotation/VAR_048972|||http://purl.uniprot.org/annotation/VAR_048973|||http://purl.uniprot.org/annotation/VAR_061152|||http://purl.uniprot.org/annotation/VSP_010893|||http://purl.uniprot.org/annotation/VSP_010894|||http://purl.uniprot.org/annotation/VSP_010895
http://togogenome.org/gene/9606:TXNDC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z345|||http://purl.uniprot.org/uniprot/Q96J42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MKS14.|||In MKS14; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Thioredoxin|||Thioredoxin domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296094|||http://purl.uniprot.org/annotation/VAR_036172|||http://purl.uniprot.org/annotation/VAR_082162|||http://purl.uniprot.org/annotation/VAR_087298|||http://purl.uniprot.org/annotation/VSP_027129
http://togogenome.org/gene/9606:CALML6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AKR1|||http://purl.uniprot.org/uniprot/Q8TD86                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Calmodulin-like protein 6|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073548|||http://purl.uniprot.org/annotation/VAR_048588
http://togogenome.org/gene/9606:NFIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16649                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330.|||Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interacts with DR1 and partially affects transcriptional repression; when associated with E-330.|||Interacts with DR1 and partially affects transcriptional repression; when associated with E-332.|||Leucine-zipper|||Necessary for transcriptional repression and sufficient for interaction with DR1|||Nuclear factor interleukin-3-regulated protein|||Phosphoserine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292667
http://togogenome.org/gene/9606:HSPA12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLP2|||http://purl.uniprot.org/uniprot/Q5BKZ8|||http://purl.uniprot.org/uniprot/Q96MM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Heat shock 70 kDa protein 12B|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078294|||http://purl.uniprot.org/annotation/VAR_049621|||http://purl.uniprot.org/annotation/VAR_059362
http://togogenome.org/gene/9606:DPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KMZ8|||http://purl.uniprot.org/uniprot/Q92785                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CSS7.|||In CSS7; abolishes interaction with acetylated histone H3; strongly decreased interaction with methylated histone H3.|||In CSS7; abolishes interaction with acetylated or methylated histone H3.|||In isoform 2.|||N-acetylalanine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Strongly decreased interaction with histones H3 and H4 and loss of function; when associated with A-275 and A-300.|||Strongly decreased interaction with histones H3 and H4 and loss of function; when associated with A-275 and A-346.|||Strongly decreased interaction with histones H3 and H4 and loss of function; when associated with A-300 and A-346.|||Zinc finger protein ubi-d4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168149|||http://purl.uniprot.org/annotation/VAR_081047|||http://purl.uniprot.org/annotation/VAR_081048|||http://purl.uniprot.org/annotation/VAR_081049|||http://purl.uniprot.org/annotation/VAR_081050|||http://purl.uniprot.org/annotation/VAR_081051|||http://purl.uniprot.org/annotation/VSP_055860
http://togogenome.org/gene/9606:FN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLE5|||http://purl.uniprot.org/uniprot/P02751|||http://purl.uniprot.org/uniprot/Q6MZF4|||http://purl.uniprot.org/uniprot/Q6MZM7|||http://purl.uniprot.org/uniprot/Q6N084|||http://purl.uniprot.org/uniprot/Q9UQS6                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anastellin|||Binds to FBLN1|||Cell attachment site|||Cell-attachment|||Collagen-binding|||Critical for collagen binding|||Disordered|||Fibrin- and heparin-binding 1|||Fibrin-binding 2|||Fibronectin|||Fibronectin type-I|||Fibronectin type-I 1|||Fibronectin type-I 10|||Fibronectin type-I 11|||Fibronectin type-I 12|||Fibronectin type-I 2|||Fibronectin type-I 3|||Fibronectin type-I 4|||Fibronectin type-I 5|||Fibronectin type-I 6|||Fibronectin type-I 7|||Fibronectin type-I 8|||Fibronectin type-I 9|||Fibronectin type-II|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13; extra domain A|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8; extra domain B|||Fibronectin type-III 9|||Heparin-binding 2|||Important for superfibronectin formation|||In GFND2.|||In GFND2; reduced binding to heparin, endothelial cells and podocytes; impaired capability to induce stress-fiber formation.|||In SMDCF.|||In SMDCF; the mutant is not secreted.|||In SMDCF; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 1, isoform 3, isoform 4, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10, isoform 14 and isoform 17.|||In isoform 11.|||In isoform 12.|||In isoform 2 and isoform 16.|||In isoform 2.|||In isoform 3, isoform 7, isoform 9, isoform 12, isoform 14 and isoform 17.|||In isoform 4, isoform 5, isoform 10 and isoform 13.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8, isoform 9, isoform 10, isoform 12, isoform 13 and isoform 14.|||In isoform 9, isoform 12 and isoform 17.|||Interchain (with C-2458)|||Interchain (with C-2462)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-684.|||Little effect on ability to form fibronectin aggregates; when associated with A-642; A-682 and A-692.|||Little effect on ability to form fibronectin aggregates; when associated with A-642; A-684 and A-692.|||Little effect on ability to form fibronectin aggregates; when associated with A-682; A-684 and A-692.|||Loss of ability to form fibronectin aggregates; when associated with A-695.|||Loss of ability to form fibronectin aggregates; when associated with A-697.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No effect on secondary structure nor on fibronectin binding nor on activation of p38 K but abolishes polymerization activity; when associated with A-666.|||No effect on secondary structure nor on fibronectin binding nor on activation of p38 kinase but abolishes polymerization activity; when associated with A-663.|||O-linked (GalNAc...) threonine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Pyrrolidone carboxylic acid|||Required for binding to LILRB4|||Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-681.|||Severely compromised ability to form fibronectin aggregates; when associated with A-641 and A-683.|||Severely compromised ability to form fibronectin aggregates; when associated with A-681 and A-683.|||Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-694.|||Slightly enhanced ability to form fibronectin aggregates; when associated with A-691 and A-696.|||Slightly enhanced ability to form fibronectin aggregates; when associated with A-694 and A-696.|||Sulfotyrosine|||Ugl-Y1|||Ugl-Y2|||Ugl-Y3|||V region (type III connecting segment, IIICS)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019235|||http://purl.uniprot.org/annotation/PRO_0000300249|||http://purl.uniprot.org/annotation/PRO_0000300250|||http://purl.uniprot.org/annotation/PRO_0000300251|||http://purl.uniprot.org/annotation/PRO_0000390479|||http://purl.uniprot.org/annotation/PRO_5002866941|||http://purl.uniprot.org/annotation/VAR_036018|||http://purl.uniprot.org/annotation/VAR_036019|||http://purl.uniprot.org/annotation/VAR_036020|||http://purl.uniprot.org/annotation/VAR_043917|||http://purl.uniprot.org/annotation/VAR_043918|||http://purl.uniprot.org/annotation/VAR_043919|||http://purl.uniprot.org/annotation/VAR_043920|||http://purl.uniprot.org/annotation/VAR_043921|||http://purl.uniprot.org/annotation/VAR_056576|||http://purl.uniprot.org/annotation/VAR_056577|||http://purl.uniprot.org/annotation/VAR_059529|||http://purl.uniprot.org/annotation/VAR_061486|||http://purl.uniprot.org/annotation/VAR_080523|||http://purl.uniprot.org/annotation/VAR_080524|||http://purl.uniprot.org/annotation/VAR_080525|||http://purl.uniprot.org/annotation/VAR_080526|||http://purl.uniprot.org/annotation/VAR_080527|||http://purl.uniprot.org/annotation/VAR_080528|||http://purl.uniprot.org/annotation/VSP_060343|||http://purl.uniprot.org/annotation/VSP_060344|||http://purl.uniprot.org/annotation/VSP_060345|||http://purl.uniprot.org/annotation/VSP_060346|||http://purl.uniprot.org/annotation/VSP_060347|||http://purl.uniprot.org/annotation/VSP_060348|||http://purl.uniprot.org/annotation/VSP_060349|||http://purl.uniprot.org/annotation/VSP_060350|||http://purl.uniprot.org/annotation/VSP_060351|||http://purl.uniprot.org/annotation/VSP_060352|||http://purl.uniprot.org/annotation/VSP_060353|||http://purl.uniprot.org/annotation/VSP_060354|||http://purl.uniprot.org/annotation/VSP_060355|||http://purl.uniprot.org/annotation/VSP_060356
http://togogenome.org/gene/9606:RSPO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FU 1|||FU 2|||In isoform 2.|||Loss of LGR4/5/6-binding, no effect on WNT3A signaling; when associated with A-106.|||Loss of LGR4/5/6-binding, no effect on WNT3A signaling; when associated with A-110.|||N-linked (GlcNAc...) asparagine|||R-spondin-3|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234443|||http://purl.uniprot.org/annotation/VSP_018324
http://togogenome.org/gene/9606:OR56B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGI3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 56B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150796|||http://purl.uniprot.org/annotation/VAR_055055
http://togogenome.org/gene/9606:VSTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2DJS5|||http://purl.uniprot.org/uniprot/D2DJS6|||http://purl.uniprot.org/uniprot/Q6UX27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||V-set and transmembrane domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272269|||http://purl.uniprot.org/annotation/VAR_030034|||http://purl.uniprot.org/annotation/VSP_022381|||http://purl.uniprot.org/annotation/VSP_022382|||http://purl.uniprot.org/annotation/VSP_022383
http://togogenome.org/gene/9606:C11orf91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3C1V1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pro residues|||Uncharacterized protein C11orf91                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340697|||http://purl.uniprot.org/annotation/VSP_034218
http://togogenome.org/gene/9606:CNOT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFF9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 8|||Impairs deadenylation and decay of mRNAi-targeted mRNA; when associated with A-40.|||Impairs deadenylation and decay of mRNAi-targeted mRNA; when associated with A-42.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212846|||http://purl.uniprot.org/annotation/VAR_048751|||http://purl.uniprot.org/annotation/VSP_055527|||http://purl.uniprot.org/annotation/VSP_055528
http://togogenome.org/gene/9606:VSIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||V-set and immunoglobulin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313573|||http://purl.uniprot.org/annotation/VAR_049955|||http://purl.uniprot.org/annotation/VSP_045475
http://togogenome.org/gene/9606:WDFY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZQ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with GABARAP and MAP1LC3C.|||Acidic residues|||BEACH|||BEACH-type PH|||Basic and acidic residues|||Decreased interaction with GABARAP, no effect on interaction with MAP1LC3B; when associated with A-3343 and A-3344.|||Decreased interaction with GABARAP, no effect on interaction with MAP1LC3B; when associated with A-3343 and A-3351.|||Decreased interaction with GABARAP, no effect on interaction with MAP1LC3B; when associated with A-3344 and A-3351.|||Decreases interaction with GABARAP and MAP1LC3C.|||Disordered|||FYVE-type|||In MCPH18; increased cellular DVL3 protein levels as compared to the wild-type protein and loss of attenuation of Wnt signaling; when expressed in Drosophila, causes brain anomalies.|||In isoform 2.|||Interaction with ATG5|||Interaction with GABARAP|||Interaction with SQSTM1|||LC3-interacting region (LIR)|||Phosphoserine|||Polar residues|||Sufficient for localization to p62 bodies/ALIS|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat and FYVE domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242693|||http://purl.uniprot.org/annotation/VAR_026864|||http://purl.uniprot.org/annotation/VAR_079130|||http://purl.uniprot.org/annotation/VSP_019475
http://togogenome.org/gene/9606:ORC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7H4|||http://purl.uniprot.org/uniprot/O43929|||http://purl.uniprot.org/uniprot/Q96B14                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||ATPase AAA-type core|||Impairs ORC complex formation.|||In MGORS2.|||In isoform 2.|||In isoform 3.|||N6-methyllysine|||Origin recognition complex subunit 4|||Origin recognition complex subunit 4 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127087|||http://purl.uniprot.org/annotation/VAR_014523|||http://purl.uniprot.org/annotation/VAR_019235|||http://purl.uniprot.org/annotation/VAR_065486|||http://purl.uniprot.org/annotation/VSP_045199|||http://purl.uniprot.org/annotation/VSP_046437
http://togogenome.org/gene/9606:CDK14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK59|||http://purl.uniprot.org/uniprot/E7EUK8|||http://purl.uniprot.org/uniprot/O94921                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes protein kinase activity.|||Cyclin-dependent kinase 14|||Disordered|||In an ovarian mucinous carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086506|||http://purl.uniprot.org/annotation/VAR_046765|||http://purl.uniprot.org/annotation/VAR_046766|||http://purl.uniprot.org/annotation/VSP_004803|||http://purl.uniprot.org/annotation/VSP_038762
http://togogenome.org/gene/9606:THRAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2W1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduces phosphorylation upon DNA damage; when associated with A-406.|||Reduces phosphorylation upon DNA damage; when associated with A-408.|||Removed|||Required for mRNA decay activity|||Required for mRNA splicing activation|||Thyroid hormone receptor-associated protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065583|||http://purl.uniprot.org/annotation/VAR_024552
http://togogenome.org/gene/9606:POLR2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62875                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerases I, II, and III subunit RPABC5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121333
http://togogenome.org/gene/9606:POGZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3K3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-817; A-820 and A-833.|||Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-817; A-820 and A-840.|||Abolishes interaction with CBX1, CBX3 and CBX5; when associated with when associated with A-817; A-833 and A-840.|||Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||DDE-1|||Diminishes interaction with CBX5 and abolishes interaction with CBX1 and CBX5; when associated with A-820; A-833 and A-840.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH CENPB-type|||In isoform 2, isoform 3 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||Integrase domain-binding motif (IBM)|||Loss of phosphorylation. Loss of interaction with PSIP1; when associated with A-1392.|||Loss of phosphorylation. Loss of interaction with PSIP1; when associated with A-1396.|||Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-1392.|||Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-1396.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Pogo transposable element with ZNF domain|||Polar residues|||Pro residues|||Probable disease-associated variant found in patients with ASD.|||Required for interaction with CBX5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047224|||http://purl.uniprot.org/annotation/VAR_031476|||http://purl.uniprot.org/annotation/VAR_073179|||http://purl.uniprot.org/annotation/VSP_010185|||http://purl.uniprot.org/annotation/VSP_010186|||http://purl.uniprot.org/annotation/VSP_010187|||http://purl.uniprot.org/annotation/VSP_010188|||http://purl.uniprot.org/annotation/VSP_030150|||http://purl.uniprot.org/annotation/VSP_046785
http://togogenome.org/gene/9606:TDRD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y872|||http://purl.uniprot.org/uniprot/Q587J7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||CS|||DEAH box|||Disordered|||Helicase ATP-binding|||In isoform 2.|||Polar residues|||Putative ATP-dependent RNA helicase TDRD12|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311968|||http://purl.uniprot.org/annotation/VSP_029675|||http://purl.uniprot.org/annotation/VSP_029676
http://togogenome.org/gene/9606:MFAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55082                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||Microfibril-associated glycoprotein 3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014865|||http://purl.uniprot.org/annotation/VAR_069386|||http://purl.uniprot.org/annotation/VSP_042948
http://togogenome.org/gene/9606:RGS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z285|||http://purl.uniprot.org/uniprot/O94810|||http://purl.uniprot.org/uniprot/Q4TT70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEP|||Diminishes interaction with Gbeta5.|||Disordered|||G protein gamma|||In isoform 2.|||In isoform 3.|||Polar residues|||RGS|||Regulator of G-protein signaling 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204210|||http://purl.uniprot.org/annotation/VAR_024606|||http://purl.uniprot.org/annotation/VAR_061770|||http://purl.uniprot.org/annotation/VSP_023497|||http://purl.uniprot.org/annotation/VSP_046724
http://togogenome.org/gene/9606:LZTS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60299                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Leucine zipper putative tumor suppressor 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050760|||http://purl.uniprot.org/annotation/VSP_039202
http://togogenome.org/gene/9606:GK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXY7|||http://purl.uniprot.org/uniprot/B4DH54|||http://purl.uniprot.org/uniprot/P32189                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carbohydrate kinase FGGY C-terminal|||Carbohydrate kinase FGGY N-terminal|||Glycerol kinase|||In GKD.|||In isoform 1 and isoform 2.|||In isoform 1 and isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059535|||http://purl.uniprot.org/annotation/VAR_001374|||http://purl.uniprot.org/annotation/VAR_001375|||http://purl.uniprot.org/annotation/VAR_001376|||http://purl.uniprot.org/annotation/VAR_001377|||http://purl.uniprot.org/annotation/VAR_010138|||http://purl.uniprot.org/annotation/VAR_015433|||http://purl.uniprot.org/annotation/VAR_068980|||http://purl.uniprot.org/annotation/VAR_068981|||http://purl.uniprot.org/annotation/VSP_000770|||http://purl.uniprot.org/annotation/VSP_000771
http://togogenome.org/gene/9606:CNOT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92600                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 9|||In isoform 2.|||In isoform 3.|||Loss of DNA binding.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327224|||http://purl.uniprot.org/annotation/VAR_042429|||http://purl.uniprot.org/annotation/VSP_054371|||http://purl.uniprot.org/annotation/VSP_055744|||http://purl.uniprot.org/annotation/VSP_055745
http://togogenome.org/gene/9606:TMEM119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4V9L6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||O-linked (GalNAc...) serine|||Phosphoserine|||Transmembrane protein 119                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251220|||http://purl.uniprot.org/annotation/VAR_027663
http://togogenome.org/gene/9606:PSME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1L8|||http://purl.uniprot.org/uniprot/Q06323|||http://purl.uniprot.org/uniprot/Q86SZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Proteasome activator PA28 C-terminal|||Proteasome activator PA28 N-terminal|||Proteasome activator complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161779|||http://purl.uniprot.org/annotation/VAR_011993|||http://purl.uniprot.org/annotation/VAR_011994|||http://purl.uniprot.org/annotation/VSP_046880|||http://purl.uniprot.org/annotation/VSP_055166|||http://purl.uniprot.org/annotation/VSP_055167
http://togogenome.org/gene/9606:IL5RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01344|||http://purl.uniprot.org/uniprot/Q8NHV7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interleukin-5 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Type I cytokine receptor cytokine-binding|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010893|||http://purl.uniprot.org/annotation/PRO_5004314276|||http://purl.uniprot.org/annotation/VAR_020654|||http://purl.uniprot.org/annotation/VAR_020655|||http://purl.uniprot.org/annotation/VSP_001678|||http://purl.uniprot.org/annotation/VSP_001679|||http://purl.uniprot.org/annotation/VSP_001680|||http://purl.uniprot.org/annotation/VSP_001681|||http://purl.uniprot.org/annotation/VSP_046742|||http://purl.uniprot.org/annotation/VSP_047762
http://togogenome.org/gene/9606:SFRP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4F7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  FZ|||NTR|||Secreted frizzled-related protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032555|||http://purl.uniprot.org/annotation/VAR_021412
http://togogenome.org/gene/9606:DRGX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNA5                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Dorsal root ganglia homeobox protein|||Homeobox|||OAR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300814
http://togogenome.org/gene/9606:ZBTB49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||Zinc finger and BTB domain-containing protein 49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047626|||http://purl.uniprot.org/annotation/VAR_057422|||http://purl.uniprot.org/annotation/VAR_057423|||http://purl.uniprot.org/annotation/VAR_057424|||http://purl.uniprot.org/annotation/VAR_073227|||http://purl.uniprot.org/annotation/VSP_016343|||http://purl.uniprot.org/annotation/VSP_057623|||http://purl.uniprot.org/annotation/VSP_057624|||http://purl.uniprot.org/annotation/VSP_057625|||http://purl.uniprot.org/annotation/VSP_057626|||http://purl.uniprot.org/annotation/VSP_057627
http://togogenome.org/gene/9606:DNAH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE73                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Dynein axonemal heavy chain 5|||In CILD3.|||In CILD3; disease phenotype consistent with Kartagener syndrome.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114630|||http://purl.uniprot.org/annotation/VAR_019603|||http://purl.uniprot.org/annotation/VAR_019604|||http://purl.uniprot.org/annotation/VAR_019605|||http://purl.uniprot.org/annotation/VAR_019606|||http://purl.uniprot.org/annotation/VAR_019607|||http://purl.uniprot.org/annotation/VAR_019608|||http://purl.uniprot.org/annotation/VAR_019609|||http://purl.uniprot.org/annotation/VAR_019610|||http://purl.uniprot.org/annotation/VAR_019611|||http://purl.uniprot.org/annotation/VAR_027903|||http://purl.uniprot.org/annotation/VAR_027904|||http://purl.uniprot.org/annotation/VAR_027905|||http://purl.uniprot.org/annotation/VAR_027906|||http://purl.uniprot.org/annotation/VAR_030705|||http://purl.uniprot.org/annotation/VAR_030706|||http://purl.uniprot.org/annotation/VAR_030707|||http://purl.uniprot.org/annotation/VAR_030708|||http://purl.uniprot.org/annotation/VAR_030709|||http://purl.uniprot.org/annotation/VAR_030710|||http://purl.uniprot.org/annotation/VAR_030711|||http://purl.uniprot.org/annotation/VAR_030712|||http://purl.uniprot.org/annotation/VAR_053840|||http://purl.uniprot.org/annotation/VAR_053841|||http://purl.uniprot.org/annotation/VAR_053842|||http://purl.uniprot.org/annotation/VAR_053843|||http://purl.uniprot.org/annotation/VAR_053844|||http://purl.uniprot.org/annotation/VAR_072469|||http://purl.uniprot.org/annotation/VAR_072470|||http://purl.uniprot.org/annotation/VAR_072471
http://togogenome.org/gene/9606:MAGEC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD91                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MAGE 1|||MAGE 2|||Melanoma-associated antigen C3|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156722|||http://purl.uniprot.org/annotation/VAR_053505|||http://purl.uniprot.org/annotation/VAR_053506|||http://purl.uniprot.org/annotation/VAR_053507|||http://purl.uniprot.org/annotation/VAR_060069|||http://purl.uniprot.org/annotation/VSP_043489|||http://purl.uniprot.org/annotation/VSP_043490|||http://purl.uniprot.org/annotation/VSP_043491
http://togogenome.org/gene/9606:OR4F21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95013                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150545
http://togogenome.org/gene/9606:SMURF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCE7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-350 and R-381. Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381.|||Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-350 and R-383. Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-383.|||Abolishes FBXL15-mediated ubiquitination and degradation; when associated with R-381 and R-381.|||C2|||Disordered|||E3 ubiquitin-protein ligase SMURF1|||Fails to ubiquitinate RHOA; when associated with A-28.|||Fails to ubiquitinate RHOA; when associated with A-85.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||In isoform Short.|||Loss of enzyme activity, without abolishing FBXL15-mediated ubiquitination.|||Phosphoserine|||Polar residues|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120326|||http://purl.uniprot.org/annotation/VAR_052959|||http://purl.uniprot.org/annotation/VSP_006812
http://togogenome.org/gene/9606:C17orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW18                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Uncharacterized protein C17orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251202|||http://purl.uniprot.org/annotation/VAR_050899
http://togogenome.org/gene/9606:YIPF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSR8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Protein YIPF4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242632
http://togogenome.org/gene/9606:VPS45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRW7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SCN5.|||In SCN5; patient fibroblasts are characterized by impaired motility and increased apoptosis.|||In isoform 2.|||Phosphoserine|||Vacuolar protein sorting-associated protein 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206312|||http://purl.uniprot.org/annotation/VAR_069865|||http://purl.uniprot.org/annotation/VAR_069866|||http://purl.uniprot.org/annotation/VSP_056739|||http://purl.uniprot.org/annotation/VSP_056740|||http://purl.uniprot.org/annotation/VSP_056741
http://togogenome.org/gene/9606:GATAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||GATA zinc finger domain-containing protein 1|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CMD2B.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288909|||http://purl.uniprot.org/annotation/VAR_032533|||http://purl.uniprot.org/annotation/VAR_068556|||http://purl.uniprot.org/annotation/VAR_068557
http://togogenome.org/gene/9606:PIGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92521                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  GPI mannosyltransferase 3|||Helical|||In DEE80.|||In DEE80; decreased protein levels; decreased cell surface presence of GPI-anchored proteins.|||In DEE80; decreased protein levels; slightly decreased cell surface presence of GPI-anchored proteins.|||In DEE80; no effect on protein levels; decreased cell surface presence of GPI-anchored proteins.|||In DEE80; strongly decreased protein levels; decreased cell surface presence of GPI-anchored proteins.|||In DEE80; strongly decreased protein levels; slightly decreased cell surface presence of GPI-anchored proteins.|||In DEE80; unknown pathological significance.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246251|||http://purl.uniprot.org/annotation/VAR_027027|||http://purl.uniprot.org/annotation/VAR_027028|||http://purl.uniprot.org/annotation/VAR_027029|||http://purl.uniprot.org/annotation/VAR_027030|||http://purl.uniprot.org/annotation/VAR_027031|||http://purl.uniprot.org/annotation/VAR_049224|||http://purl.uniprot.org/annotation/VAR_083070|||http://purl.uniprot.org/annotation/VAR_083071|||http://purl.uniprot.org/annotation/VAR_083072|||http://purl.uniprot.org/annotation/VAR_083073|||http://purl.uniprot.org/annotation/VAR_083074|||http://purl.uniprot.org/annotation/VAR_083075|||http://purl.uniprot.org/annotation/VAR_083076|||http://purl.uniprot.org/annotation/VAR_083077|||http://purl.uniprot.org/annotation/VAR_083078|||http://purl.uniprot.org/annotation/VAR_083079
http://togogenome.org/gene/9606:ZNF728                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKX0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 728                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421023
http://togogenome.org/gene/9606:TBC1D19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5T2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Rab-GAP TBC|||TBC1 domain family member 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208047|||http://purl.uniprot.org/annotation/VAR_030602|||http://purl.uniprot.org/annotation/VAR_030603|||http://purl.uniprot.org/annotation/VSP_053998
http://togogenome.org/gene/9606:ACSL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60488|||http://purl.uniprot.org/uniprot/Q8TAF6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||In XLID63.|||In a colorectal cancer sample; somatic mutation.|||In isoform Short.|||Long-chain-fatty-acid--CoA ligase 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193109|||http://purl.uniprot.org/annotation/VAR_013180|||http://purl.uniprot.org/annotation/VAR_036376|||http://purl.uniprot.org/annotation/VAR_083476|||http://purl.uniprot.org/annotation/VSP_000238
http://togogenome.org/gene/9606:IGFBP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16270                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  IGFBP N-terminal|||Ig-like C2-type|||In RNA edited version.|||In isoform 2.|||Insulin-like growth factor-binding protein 7|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014392|||http://purl.uniprot.org/annotation/VAR_018959|||http://purl.uniprot.org/annotation/VAR_063638|||http://purl.uniprot.org/annotation/VAR_063639|||http://purl.uniprot.org/annotation/VSP_045297
http://togogenome.org/gene/9606:MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8KB75|||http://purl.uniprot.org/uniprot/A7UKX7|||http://purl.uniprot.org/uniprot/A7UKX8|||http://purl.uniprot.org/uniprot/A7UKX9|||http://purl.uniprot.org/uniprot/G3XA89|||http://purl.uniprot.org/uniprot/Q00987                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARF-binding|||Acidic residues|||Basic and acidic residues|||DM2|||Disordered|||E3 ubiquitin-protein ligase Mdm2|||Fails to interact with MDM4.|||In isoform 11.|||In isoform Mdm2-A and isoform Mdm2-A1.|||In isoform Mdm2-A1.|||In isoform Mdm2-B.|||In isoform Mdm2-C.|||In isoform Mdm2-D.|||In isoform Mdm2-E.|||In isoform Mdm2-F.|||In isoform Mdm2-G.|||In isoform Mdm2-alpha.|||Interaction with MTBP|||Interaction with PYHIN1 and necessary for interaction with RFFL and RNF34|||Interaction with USP7|||Loss of ubiquitin ligase E3 activity, enhances protein stability. Does not inhibit interaction with APEX1, but inhibits its ubiquitin ligase E3 activity on APEX1. No effect on its ability to induce apoptosis.|||Loss of ubiquitin ligase E3 activity.|||Necessary for interaction with USP2|||No effect on its ability to induce apoptosis.|||No loss of ubiquitin ligase E3 activity.|||No substantial decrease of ubiquitin ligase E3 activity.|||Nuclear export signal|||Nuclear localization signal|||Nucleolar localization signal|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by SGK1|||Phosphothreonine; by ATM|||Polar residues|||RING-type|||RanBP2-type|||Region II|||SWIB/MDM2|||Significant decrease of ubiquitin ligase E3 activity.|||Sufficient to promote the mitochondrial pathway of apoptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157332|||http://purl.uniprot.org/annotation/VSP_003207|||http://purl.uniprot.org/annotation/VSP_003208|||http://purl.uniprot.org/annotation/VSP_003209|||http://purl.uniprot.org/annotation/VSP_003210|||http://purl.uniprot.org/annotation/VSP_003211|||http://purl.uniprot.org/annotation/VSP_003212|||http://purl.uniprot.org/annotation/VSP_003213|||http://purl.uniprot.org/annotation/VSP_003214|||http://purl.uniprot.org/annotation/VSP_022578|||http://purl.uniprot.org/annotation/VSP_022579|||http://purl.uniprot.org/annotation/VSP_037997
http://togogenome.org/gene/9606:GPRASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JY77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-protein coupled receptor-associated sorting protein 1|||OPRD1-binding|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239050|||http://purl.uniprot.org/annotation/VAR_026579|||http://purl.uniprot.org/annotation/VAR_049263|||http://purl.uniprot.org/annotation/VAR_049264
http://togogenome.org/gene/9606:RD3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJH9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region                                                                                  ^@                                                                                  Disordered|||Protein RD3-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000417456
http://togogenome.org/gene/9606:CD248                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Disordered|||EGF-like; calcium-binding|||Endosialin|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045799|||http://purl.uniprot.org/annotation/VAR_025013|||http://purl.uniprot.org/annotation/VAR_036399|||http://purl.uniprot.org/annotation/VSP_017087
http://togogenome.org/gene/9606:SLC25A44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PGQ0|||http://purl.uniprot.org/uniprot/Q96H78                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253064|||http://purl.uniprot.org/annotation/VAR_050134
http://togogenome.org/gene/9606:SAXO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658L1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Stabilizer of axonemal microtubules 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321839|||http://purl.uniprot.org/annotation/VAR_039359|||http://purl.uniprot.org/annotation/VAR_039360|||http://purl.uniprot.org/annotation/VAR_039361|||http://purl.uniprot.org/annotation/VSP_055086
http://togogenome.org/gene/9606:MYCBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75592                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity in threonine discharge assay, associated with enhanced thiol-sensitive ubiquitin adduct formation.|||Abolished E3 ubiquitin-protein ligase activity.|||Basic and acidic residues|||Basic residues|||DOC|||Disordered|||Does not affect E3 ubiquitin-protein ligase activity.|||E3 ubiquitin-protein ligase MYCBP2|||Filamin|||Important for catalysis|||In isoform 2.|||Increased thiol-sensitive adduct formation.|||PHR domain 1|||PHR domain 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||RAE1 binding|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RING-type; atypical|||Reduced E3 ubiquitin-protein ligase activity in threonine discharge assay.|||Retains activity while also forming a discrete monoubiquitin adduct that is resistant to thiolysis but is reversible after base treatment.|||Tandem cysteine domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055963|||http://purl.uniprot.org/annotation/VAR_030070|||http://purl.uniprot.org/annotation/VAR_052086|||http://purl.uniprot.org/annotation/VSP_014183
http://togogenome.org/gene/9606:NDC80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K031|||http://purl.uniprot.org/uniprot/O14777                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Abrogates binding to RB1.|||DUF5595|||Disordered|||Impaired acetylation, leading to reduced kinetochore-microtubule attachment; when associated with R-53.|||Impaired acetylation, leading to reduced kinetochore-microtubule attachment; when associated with R-59.|||Interaction with NEK2 and ZWINT|||Interaction with PSMC2 and SMC1A|||Interaction with RB1|||Interaction with SMC1A|||Interaction with the C-terminus of CDCA1 and the SPBC24-SPBC25 subcomplex|||Interaction with the N-terminus of CDCA1|||Kinetochore protein NDC80 homolog|||Mimics acetylation, leading to increased kinetochore-microtubule attachment; when associated with Q-53.|||Mimics acetylation, leading to increased kinetochore-microtubule attachment; when associated with Q-59.|||N6-acetyllysine|||Nuclear localization|||Phosphoserine|||Phosphoserine; by NEK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249550|||http://purl.uniprot.org/annotation/VAR_027436|||http://purl.uniprot.org/annotation/VAR_027437|||http://purl.uniprot.org/annotation/VAR_027438
http://togogenome.org/gene/9606:TPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2C3|||http://purl.uniprot.org/uniprot/A0A0P1J1R0|||http://purl.uniprot.org/uniprot/P13693                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Phosphoserine; by PLK1|||Required for reduction of TSC22D1 protein stability|||TCTP|||Translationally-controlled tumor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211268|||http://purl.uniprot.org/annotation/VAR_052273|||http://purl.uniprot.org/annotation/VSP_054838
http://togogenome.org/gene/9606:BRDT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58F21                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo 1|||Bromo 2|||Bromodomain testis-specific protein|||Disordered|||Histone H4K5ac binding|||In SPGF21; no effect on protein expression; unknown pathological significance.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||NET|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239225|||http://purl.uniprot.org/annotation/VAR_026584|||http://purl.uniprot.org/annotation/VAR_026585|||http://purl.uniprot.org/annotation/VAR_026586|||http://purl.uniprot.org/annotation/VAR_041924|||http://purl.uniprot.org/annotation/VAR_041925|||http://purl.uniprot.org/annotation/VAR_041926|||http://purl.uniprot.org/annotation/VAR_041927|||http://purl.uniprot.org/annotation/VAR_041928|||http://purl.uniprot.org/annotation/VAR_041929|||http://purl.uniprot.org/annotation/VAR_047327|||http://purl.uniprot.org/annotation/VAR_047328|||http://purl.uniprot.org/annotation/VAR_047329|||http://purl.uniprot.org/annotation/VAR_079306|||http://purl.uniprot.org/annotation/VSP_019118|||http://purl.uniprot.org/annotation/VSP_044509|||http://purl.uniprot.org/annotation/VSP_044510|||http://purl.uniprot.org/annotation/VSP_044511
http://togogenome.org/gene/9606:SELENOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49908                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Selenocysteine|||Selenoprotein P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022313|||http://purl.uniprot.org/annotation/VAR_023256|||http://purl.uniprot.org/annotation/VAR_023257|||http://purl.uniprot.org/annotation/VAR_023258|||http://purl.uniprot.org/annotation/VAR_023259|||http://purl.uniprot.org/annotation/VAR_023260
http://togogenome.org/gene/9606:FGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1B8|||http://purl.uniprot.org/uniprot/Q14314                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Fibrinogen C-terminal|||Fibroleukin|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009106|||http://purl.uniprot.org/annotation/PRO_5014296870|||http://purl.uniprot.org/annotation/VAR_013066
http://togogenome.org/gene/9606:ACTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62736                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin, aortic smooth muscle|||Actin, aortic smooth muscle, intermediate form|||In AAT6.|||In MSMDS.|||In MYMY5 and MSMDS; disease phenotype include smooth muscle cells dysfunction in organs throughout the body with decreased contractile function in the iris, bladder and gastrointestinal tract.|||Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1|||Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N-acetylglutamate; in Actin, aortic smooth muscle|||N6-methyllysine|||Removed|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000442603|||http://purl.uniprot.org/annotation/PRO_0000442604|||http://purl.uniprot.org/annotation/VAR_011944|||http://purl.uniprot.org/annotation/VAR_011945|||http://purl.uniprot.org/annotation/VAR_011946|||http://purl.uniprot.org/annotation/VAR_045915|||http://purl.uniprot.org/annotation/VAR_045916|||http://purl.uniprot.org/annotation/VAR_045917|||http://purl.uniprot.org/annotation/VAR_045918|||http://purl.uniprot.org/annotation/VAR_045919|||http://purl.uniprot.org/annotation/VAR_045920|||http://purl.uniprot.org/annotation/VAR_045921|||http://purl.uniprot.org/annotation/VAR_045922|||http://purl.uniprot.org/annotation/VAR_045923|||http://purl.uniprot.org/annotation/VAR_062577|||http://purl.uniprot.org/annotation/VAR_062578|||http://purl.uniprot.org/annotation/VAR_062579|||http://purl.uniprot.org/annotation/VAR_062580|||http://purl.uniprot.org/annotation/VAR_062581|||http://purl.uniprot.org/annotation/VAR_064516|||http://purl.uniprot.org/annotation/VAR_085865
http://togogenome.org/gene/9606:HOXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49639                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Basic residues|||Disordered|||Homeobox|||Homeobox protein Hox-A1|||In isoform 1.|||In isoform 2.|||Interaction with OGT|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200030|||http://purl.uniprot.org/annotation/VAR_010305|||http://purl.uniprot.org/annotation/VAR_030576|||http://purl.uniprot.org/annotation/VSP_002376|||http://purl.uniprot.org/annotation/VSP_002377|||http://purl.uniprot.org/annotation/VSP_002378|||http://purl.uniprot.org/annotation/VSP_002379
http://togogenome.org/gene/9606:GDI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3X8|||http://purl.uniprot.org/uniprot/P31150                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In XLID41.|||In XLID41; causes reduced binding and recycling of RAB3A.|||Rab GDP dissociation inhibitor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056671|||http://purl.uniprot.org/annotation/VAR_008130|||http://purl.uniprot.org/annotation/VAR_008131
http://togogenome.org/gene/9606:EBLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CF75                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Endogenous Bornavirus-like nucleoprotein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393911
http://togogenome.org/gene/9606:PCGF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not abolish phosphorylation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||Phosphoserine|||Polycomb group RING finger protein 6|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055989|||http://purl.uniprot.org/annotation/VAR_054312|||http://purl.uniprot.org/annotation/VSP_042007|||http://purl.uniprot.org/annotation/VSP_042008
http://togogenome.org/gene/9606:REXO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  50% reduction in 3'-to-5'exoribonuclease activity.|||Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-178 or A-215.|||Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-178.|||Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with A-179.|||Disruption of homodimerization and loss of 3'-to-5'exoribonuclease activity; when associated with R-179 or A-179.|||Exonuclease|||Important for dinucleotide binding|||In isoform 2.|||In isoform 3.|||Loss of 3'-to-5'exoribonuclease activity.|||Mitochondrion|||N6-acetyllysine|||No effect on 3'-to-5'exoribonuclease activity.|||Oligoribonuclease, mitochondrial|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020273|||http://purl.uniprot.org/annotation/VSP_003775|||http://purl.uniprot.org/annotation/VSP_054954
http://togogenome.org/gene/9606:POLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KNU5|||http://purl.uniprot.org/uniprot/P54098                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA polymerase subunit gamma-1|||DNA-directed DNA polymerase family A palm|||Disordered|||In LS.|||In MTDPS4A.|||In MTDPS4B.|||In PEOA1 and MTDPS4A; unknown pathological significance.|||In PEOA1.|||In PEOA1; can underlie parkinsonism; 45-fold decrease in apparent binding affinity for the incoming nucleoside triphosphate; 2-fold less accurate for basepair substitutions than wild-type.|||In PEOB1 and MTDPS4A.|||In PEOB1 and MTDPS4B.|||In PEOB1, MTDPS4A and MTDPS4B.|||In PEOB1, MTDPS4A, MTDPS4B and LS.|||In PEOB1, SANDO, SCAE and MTDPS4A; results in clearly decreased activity, DNA binding and processivity of the polymerase.|||In PEOB1.|||In PEOB1; also found in SANDO.|||In PEOB1; sporadic case.|||In PEOB1; sporadic case; also in SANDO.|||In PEOB1; unknown pathological significance.|||In PEOB1; with absence of progressive external ophthalmoplegia.|||In SANDO and PEOB1; sporadic case.|||In SANDO and SCAE.|||In SANDO, SCAE and MTDPS4A; unknown pathological significance.|||In SANDO.|||In SANDO; shows DNA binding affinity and processivities similar to the controls.|||In SANDO; sporadic case.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101270|||http://purl.uniprot.org/annotation/VAR_012153|||http://purl.uniprot.org/annotation/VAR_012154|||http://purl.uniprot.org/annotation/VAR_012155|||http://purl.uniprot.org/annotation/VAR_012156|||http://purl.uniprot.org/annotation/VAR_014904|||http://purl.uniprot.org/annotation/VAR_014905|||http://purl.uniprot.org/annotation/VAR_014906|||http://purl.uniprot.org/annotation/VAR_014907|||http://purl.uniprot.org/annotation/VAR_014908|||http://purl.uniprot.org/annotation/VAR_014909|||http://purl.uniprot.org/annotation/VAR_014910|||http://purl.uniprot.org/annotation/VAR_014911|||http://purl.uniprot.org/annotation/VAR_019265|||http://purl.uniprot.org/annotation/VAR_019266|||http://purl.uniprot.org/annotation/VAR_019267|||http://purl.uniprot.org/annotation/VAR_023663|||http://purl.uniprot.org/annotation/VAR_023664|||http://purl.uniprot.org/annotation/VAR_023665|||http://purl.uniprot.org/annotation/VAR_023666|||http://purl.uniprot.org/annotation/VAR_023667|||http://purl.uniprot.org/annotation/VAR_023668|||http://purl.uniprot.org/annotation/VAR_023669|||http://purl.uniprot.org/annotation/VAR_023670|||http://purl.uniprot.org/annotation/VAR_023671|||http://purl.uniprot.org/annotation/VAR_023672|||http://purl.uniprot.org/annotation/VAR_023673|||http://purl.uniprot.org/annotation/VAR_023674|||http://purl.uniprot.org/annotation/VAR_023675|||http://purl.uniprot.org/annotation/VAR_023676|||http://purl.uniprot.org/annotation/VAR_023677|||http://purl.uniprot.org/annotation/VAR_023678|||http://purl.uniprot.org/annotation/VAR_023679|||http://purl.uniprot.org/annotation/VAR_023680|||http://purl.uniprot.org/annotation/VAR_023681|||http://purl.uniprot.org/annotation/VAR_023682|||http://purl.uniprot.org/annotation/VAR_023683|||http://purl.uniprot.org/annotation/VAR_023684|||http://purl.uniprot.org/annotation/VAR_023685|||http://purl.uniprot.org/annotation/VAR_023686|||http://purl.uniprot.org/annotation/VAR_023687|||http://purl.uniprot.org/annotation/VAR_023688|||http://purl.uniprot.org/annotation/VAR_023689|||http://purl.uniprot.org/annotation/VAR_023690|||http://purl.uniprot.org/annotation/VAR_058870|||http://purl.uniprot.org/annotation/VAR_058871|||http://purl.uniprot.org/annotation/VAR_058872|||http://purl.uniprot.org/annotation/VAR_058873|||http://purl.uniprot.org/annotation/VAR_058874|||http://purl.uniprot.org/annotation/VAR_058875|||http://purl.uniprot.org/annotation/VAR_058876|||http://purl.uniprot.org/annotation/VAR_058877|||http://purl.uniprot.org/annotation/VAR_058878|||http://purl.uniprot.org/annotation/VAR_058879|||http://purl.uniprot.org/annotation/VAR_058880|||http://purl.uniprot.org/annotation/VAR_058881|||http://purl.uniprot.org/annotation/VAR_058882|||http://purl.uniprot.org/annotation/VAR_058883|||http://purl.uniprot.org/annotation/VAR_058884|||http://purl.uniprot.org/annotation/VAR_058885|||http://purl.uniprot.org/annotation/VAR_058886|||http://purl.uniprot.org/annotation/VAR_058887|||http://purl.uniprot.org/annotation/VAR_058888|||http://purl.uniprot.org/annotation/VAR_058889|||http://purl.uniprot.org/annotation/VAR_058890|||http://purl.uniprot.org/annotation/VAR_058891|||http://purl.uniprot.org/annotation/VAR_058892|||http://purl.uniprot.org/annotation/VAR_058893|||http://purl.uniprot.org/annotation/VAR_058894|||http://purl.uniprot.org/annotation/VAR_058895|||http://purl.uniprot.org/annotation/VAR_058896|||http://purl.uniprot.org/annotation/VAR_058897|||http://purl.uniprot.org/annotation/VAR_058898|||http://purl.uniprot.org/annotation/VAR_065092|||http://purl.uniprot.org/annotation/VAR_065119
http://togogenome.org/gene/9606:LCE2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA81                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235331
http://togogenome.org/gene/9606:MON1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5, isoform 2 and isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Vacuolar fusion protein MON1 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285761|||http://purl.uniprot.org/annotation/VSP_059430|||http://purl.uniprot.org/annotation/VSP_059431|||http://purl.uniprot.org/annotation/VSP_059432|||http://purl.uniprot.org/annotation/VSP_059433
http://togogenome.org/gene/9606:ZDHHC20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRN8|||http://purl.uniprot.org/uniprot/Q5W0Z9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||Important for selectivity toward medium-length fatty acids|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity.|||Lumenal|||Mildly reduced catalytic activity.|||Moderately reduced catalytic activity. Enhances activity with acyl-CoA with C18 and C20 fatty acid chains.|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC20|||Phosphoserine|||S-palmitoyl cysteine intermediate|||Strongly reduced catalytic activity.|||Strongly reduced catalytic activity. Enhances activity with acyl-CoA with C12 and C14 fatty acid chains.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212906|||http://purl.uniprot.org/annotation/VSP_016276|||http://purl.uniprot.org/annotation/VSP_016277|||http://purl.uniprot.org/annotation/VSP_040481|||http://purl.uniprot.org/annotation/VSP_040482|||http://purl.uniprot.org/annotation/VSP_056002
http://togogenome.org/gene/9606:BRD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPI1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Bromodomain-containing protein 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227664|||http://purl.uniprot.org/annotation/VSP_017564
http://togogenome.org/gene/9606:SPMIP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCR6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Predominantly cytoplasmic rather than nuclear localization.|||Sperm microtubule inner protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296258|||http://purl.uniprot.org/annotation/VAR_034626|||http://purl.uniprot.org/annotation/VSP_027169|||http://purl.uniprot.org/annotation/VSP_027170|||http://purl.uniprot.org/annotation/VSP_027171|||http://purl.uniprot.org/annotation/VSP_042861
http://togogenome.org/gene/9606:PPP1R3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16821                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  CBM21|||Can be associated with insulin resistance.|||Disordered|||Helical|||In T2D.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||PP1-binding motif|||Phosphoserine|||Phosphoserine; by GSK3|||Phosphoserine; by PKA|||Phosphoserine; by PKA and ISPK|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071500|||http://purl.uniprot.org/annotation/VAR_019697|||http://purl.uniprot.org/annotation/VAR_019698|||http://purl.uniprot.org/annotation/VAR_019699|||http://purl.uniprot.org/annotation/VAR_027929|||http://purl.uniprot.org/annotation/VAR_027930|||http://purl.uniprot.org/annotation/VAR_027931|||http://purl.uniprot.org/annotation/VAR_027932|||http://purl.uniprot.org/annotation/VAR_027933|||http://purl.uniprot.org/annotation/VAR_027934|||http://purl.uniprot.org/annotation/VAR_036287|||http://purl.uniprot.org/annotation/VAR_057128|||http://purl.uniprot.org/annotation/VSP_011585|||http://purl.uniprot.org/annotation/VSP_011586
http://togogenome.org/gene/9606:MRGPRX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LA9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member X4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069783|||http://purl.uniprot.org/annotation/VAR_019435|||http://purl.uniprot.org/annotation/VAR_019436|||http://purl.uniprot.org/annotation/VAR_019437|||http://purl.uniprot.org/annotation/VAR_019438|||http://purl.uniprot.org/annotation/VAR_025506|||http://purl.uniprot.org/annotation/VAR_049419
http://togogenome.org/gene/9606:RAD17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75943                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with RAD1; when associated with D-646.|||Abolishes interaction with RAD1; when associated with D-656.|||Basic and acidic residues|||Cell cycle checkpoint protein RAD17|||Disordered|||Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3.|||Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with MCM7|||No effect on phosphorylation by ATR.|||Phosphoserine|||Phosphoserine; by ATR and ATM|||Phosphothreonine|||Polar residues|||Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-646.|||Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-656.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209948|||http://purl.uniprot.org/annotation/VAR_021574|||http://purl.uniprot.org/annotation/VAR_021575|||http://purl.uniprot.org/annotation/VAR_021576|||http://purl.uniprot.org/annotation/VAR_021577|||http://purl.uniprot.org/annotation/VSP_013306|||http://purl.uniprot.org/annotation/VSP_013307|||http://purl.uniprot.org/annotation/VSP_013308|||http://purl.uniprot.org/annotation/VSP_013309
http://togogenome.org/gene/9606:UFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Does not affect neither UBA5-binding nor thioester formation with UFM1.|||Glycyl thioester intermediate|||Impairs binding to UBA5 and thioester formation with UFM1.|||In NEDSG; decreased ability to form thioester bond with UFM1; decreased protein ufmylation.|||Instead of the formation of an intermediate complex with a thiol ester bond between UFC1 (E2-like enzyme) and UFM1 (substrate), a stable complex with an O-ester bond is formed.|||Ubiquitin-fold modifier-conjugating enzyme 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082613|||http://purl.uniprot.org/annotation/VAR_028312|||http://purl.uniprot.org/annotation/VAR_081216|||http://purl.uniprot.org/annotation/VAR_081217
http://togogenome.org/gene/9606:NODAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S42                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In HTX5.|||In HTX5; decrease in signal transduction.|||In HTX5; likely benign variant; decrease in signal transduction.|||In a colorectal cancer sample; somatic mutation.|||Interchain|||N-linked (GlcNAc...) asparagine|||Nodal homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033998|||http://purl.uniprot.org/annotation/PRO_0000033999|||http://purl.uniprot.org/annotation/VAR_015111|||http://purl.uniprot.org/annotation/VAR_036202|||http://purl.uniprot.org/annotation/VAR_038193|||http://purl.uniprot.org/annotation/VAR_038194|||http://purl.uniprot.org/annotation/VAR_062281|||http://purl.uniprot.org/annotation/VAR_062282|||http://purl.uniprot.org/annotation/VAR_062283
http://togogenome.org/gene/9606:TTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WY09|||http://purl.uniprot.org/uniprot/Q15361                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||May be involved in interaction with ARF|||Myb-like|||Myb-like 1|||Myb-like 2|||N-terminal region (NRD)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Transcription termination factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250472|||http://purl.uniprot.org/annotation/VAR_027563|||http://purl.uniprot.org/annotation/VAR_027564|||http://purl.uniprot.org/annotation/VAR_027565|||http://purl.uniprot.org/annotation/VAR_027566|||http://purl.uniprot.org/annotation/VAR_027567|||http://purl.uniprot.org/annotation/VAR_050201|||http://purl.uniprot.org/annotation/VAR_061363
http://togogenome.org/gene/9606:FAM185A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0U4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Protein FAM185A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321830|||http://purl.uniprot.org/annotation/VAR_039356|||http://purl.uniprot.org/annotation/VAR_084592|||http://purl.uniprot.org/annotation/VSP_031804|||http://purl.uniprot.org/annotation/VSP_037078
http://togogenome.org/gene/9606:CD59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13987|||http://purl.uniprot.org/uniprot/Q6FHM9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Almost complete loss of function. Lysis.|||CD59 glycoprotein|||Complete loss of function. Lysis.|||GPI-anchor amidated asparagine|||In HACD59.|||In isoform 2.|||Loss of function. Lysis.|||Loss of glycation mediated inactivation.|||N-linked (Glc) (glycation) lysine|||N-linked (GlcNAc...) asparagine|||No loss of function.|||O-linked (GalNAc...) threonine|||Removed in mature form|||Some loss of function. Some lysis.|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036108|||http://purl.uniprot.org/annotation/PRO_0000036109|||http://purl.uniprot.org/annotation/PRO_5014310456|||http://purl.uniprot.org/annotation/VAR_070124|||http://purl.uniprot.org/annotation/VSP_060064
http://togogenome.org/gene/9606:TGM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22735                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In ARCI1.|||In ARCI1; inhibits cell proliferation.|||In ARCI1; skin phenotype consistent with lamellar ichthyosis.|||In ARCI1; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma.|||In isoform 2.|||Membrane anchorage region|||Phosphoserine|||Phosphothreonine|||Protein-glutamine gamma-glutamyltransferase K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213701|||http://purl.uniprot.org/annotation/VAR_007476|||http://purl.uniprot.org/annotation/VAR_007477|||http://purl.uniprot.org/annotation/VAR_007478|||http://purl.uniprot.org/annotation/VAR_007479|||http://purl.uniprot.org/annotation/VAR_007480|||http://purl.uniprot.org/annotation/VAR_007481|||http://purl.uniprot.org/annotation/VAR_015220|||http://purl.uniprot.org/annotation/VAR_015221|||http://purl.uniprot.org/annotation/VAR_015222|||http://purl.uniprot.org/annotation/VAR_020918|||http://purl.uniprot.org/annotation/VAR_020919|||http://purl.uniprot.org/annotation/VAR_020920|||http://purl.uniprot.org/annotation/VAR_024660|||http://purl.uniprot.org/annotation/VAR_029268|||http://purl.uniprot.org/annotation/VAR_052550|||http://purl.uniprot.org/annotation/VAR_052551|||http://purl.uniprot.org/annotation/VAR_052552|||http://purl.uniprot.org/annotation/VAR_055374|||http://purl.uniprot.org/annotation/VAR_058638|||http://purl.uniprot.org/annotation/VAR_058639|||http://purl.uniprot.org/annotation/VAR_058640|||http://purl.uniprot.org/annotation/VAR_058641|||http://purl.uniprot.org/annotation/VAR_058642|||http://purl.uniprot.org/annotation/VAR_058643|||http://purl.uniprot.org/annotation/VAR_058644|||http://purl.uniprot.org/annotation/VAR_058645|||http://purl.uniprot.org/annotation/VAR_058646|||http://purl.uniprot.org/annotation/VAR_058647|||http://purl.uniprot.org/annotation/VAR_058648|||http://purl.uniprot.org/annotation/VAR_058649|||http://purl.uniprot.org/annotation/VAR_058650|||http://purl.uniprot.org/annotation/VAR_058651|||http://purl.uniprot.org/annotation/VAR_058652|||http://purl.uniprot.org/annotation/VAR_058653|||http://purl.uniprot.org/annotation/VAR_058654|||http://purl.uniprot.org/annotation/VAR_058655|||http://purl.uniprot.org/annotation/VAR_058656|||http://purl.uniprot.org/annotation/VAR_058657|||http://purl.uniprot.org/annotation/VAR_058658|||http://purl.uniprot.org/annotation/VAR_058659|||http://purl.uniprot.org/annotation/VAR_058660|||http://purl.uniprot.org/annotation/VAR_058661|||http://purl.uniprot.org/annotation/VAR_058662|||http://purl.uniprot.org/annotation/VAR_058663|||http://purl.uniprot.org/annotation/VAR_058664|||http://purl.uniprot.org/annotation/VAR_058665|||http://purl.uniprot.org/annotation/VAR_058666|||http://purl.uniprot.org/annotation/VAR_058667|||http://purl.uniprot.org/annotation/VAR_058668|||http://purl.uniprot.org/annotation/VAR_058669|||http://purl.uniprot.org/annotation/VAR_058670|||http://purl.uniprot.org/annotation/VAR_058671|||http://purl.uniprot.org/annotation/VAR_058672|||http://purl.uniprot.org/annotation/VAR_058673|||http://purl.uniprot.org/annotation/VAR_058674|||http://purl.uniprot.org/annotation/VAR_058675|||http://purl.uniprot.org/annotation/VAR_058676|||http://purl.uniprot.org/annotation/VAR_058677|||http://purl.uniprot.org/annotation/VAR_058678|||http://purl.uniprot.org/annotation/VAR_058679|||http://purl.uniprot.org/annotation/VAR_058680|||http://purl.uniprot.org/annotation/VAR_058681|||http://purl.uniprot.org/annotation/VAR_058682|||http://purl.uniprot.org/annotation/VAR_058683|||http://purl.uniprot.org/annotation/VAR_058684|||http://purl.uniprot.org/annotation/VAR_058685|||http://purl.uniprot.org/annotation/VAR_058686|||http://purl.uniprot.org/annotation/VAR_058687|||http://purl.uniprot.org/annotation/VAR_058688|||http://purl.uniprot.org/annotation/VAR_058689|||http://purl.uniprot.org/annotation/VAR_075227|||http://purl.uniprot.org/annotation/VSP_056840
http://togogenome.org/gene/9606:FBXW8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3Y1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box/WD repeat-containing protein 8|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050997|||http://purl.uniprot.org/annotation/VAR_057597|||http://purl.uniprot.org/annotation/VAR_057598|||http://purl.uniprot.org/annotation/VAR_060326|||http://purl.uniprot.org/annotation/VAR_062096|||http://purl.uniprot.org/annotation/VSP_008501
http://togogenome.org/gene/9606:NPAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99742                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Neuronal PAS domain-containing protein 1|||PAC|||PAS 1|||PAS 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127404|||http://purl.uniprot.org/annotation/VSP_054280|||http://purl.uniprot.org/annotation/VSP_054281|||http://purl.uniprot.org/annotation/VSP_054282
http://togogenome.org/gene/9606:ITGAE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38570                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Integrin alpha-E|||Integrin alpha-E heavy chain|||Integrin alpha-E light chain|||Loss of E-cadherin binding.|||N-linked (GlcNAc...) asparagine|||VWFA|||X-domain (extra domain)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016283|||http://purl.uniprot.org/annotation/PRO_0000016284|||http://purl.uniprot.org/annotation/PRO_0000016285|||http://purl.uniprot.org/annotation/VAR_008884|||http://purl.uniprot.org/annotation/VAR_008885|||http://purl.uniprot.org/annotation/VAR_020037|||http://purl.uniprot.org/annotation/VAR_034025|||http://purl.uniprot.org/annotation/VAR_054889|||http://purl.uniprot.org/annotation/VAR_054890|||http://purl.uniprot.org/annotation/VAR_054891
http://togogenome.org/gene/9606:LATS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRM7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||Fails to localize at the centromere during interphase.|||In a lung adenocarcinoma sample; somatic mutation.|||Loss of kinase activity, autophosphorylation and tumor suppressor activity.|||Loss of tumor suppressor activity.|||PPxY motif|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LATS2|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086234|||http://purl.uniprot.org/annotation/VAR_019789|||http://purl.uniprot.org/annotation/VAR_040669|||http://purl.uniprot.org/annotation/VAR_040670|||http://purl.uniprot.org/annotation/VAR_040671|||http://purl.uniprot.org/annotation/VAR_040672|||http://purl.uniprot.org/annotation/VAR_040673|||http://purl.uniprot.org/annotation/VAR_047077
http://togogenome.org/gene/9606:KHK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM6|||http://purl.uniprot.org/uniprot/C9JDL1|||http://purl.uniprot.org/uniprot/P50053                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carbohydrate kinase PfkB|||In FRUCT; loss of ketohexokinase function; insoluble.|||In FRUCT; no effect on ketohexokinase function; decreases enzyme activity but no effect in substrate affinity; decreases thermal stability.|||In isoform A.|||Ketohexokinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080088|||http://purl.uniprot.org/annotation/VAR_006072|||http://purl.uniprot.org/annotation/VAR_006073|||http://purl.uniprot.org/annotation/VAR_006074|||http://purl.uniprot.org/annotation/VSP_004669
http://togogenome.org/gene/9606:YIPF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EC8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-acetylalanine|||Phosphoserine|||Protein YIPF6|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242668|||http://purl.uniprot.org/annotation/VAR_026855|||http://purl.uniprot.org/annotation/VSP_047121
http://togogenome.org/gene/9606:SERPINH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K259|||http://purl.uniprot.org/uniprot/P50454                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  In OI10.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Prevents secretion from ER|||Reactive bond homolog|||Serpin|||Serpin H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032520|||http://purl.uniprot.org/annotation/PRO_5002725468|||http://purl.uniprot.org/annotation/VAR_028445|||http://purl.uniprot.org/annotation/VAR_063602
http://togogenome.org/gene/9606:METTL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1Q9                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||tRNA N(3)-methylcytidine methyltransferase METTL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328847|||http://purl.uniprot.org/annotation/VAR_042547|||http://purl.uniprot.org/annotation/VAR_042548|||http://purl.uniprot.org/annotation/VAR_042549|||http://purl.uniprot.org/annotation/VAR_042550|||http://purl.uniprot.org/annotation/VAR_059465|||http://purl.uniprot.org/annotation/VSP_032816
http://togogenome.org/gene/9606:OTUD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VV17                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolished deubiquitinase activity.|||Basic and acidic residues|||Cys-loop|||Disordered|||His-loop|||Nucleophile|||OTU|||OTU domain-containing protein 1|||UIM|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271018
http://togogenome.org/gene/9606:LOC102724428                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2F2|||http://purl.uniprot.org/uniprot/P57059                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreased kinase activity without affecting much autophosphorylation status.|||Disordered|||Does not autophosphorylation and kinase activity.|||Impaired autophosphorylation and kinase activity.|||In DEE30; no change in subcellular location.|||In a glioblastoma multiforme sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Loss of interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-473.|||Loss of kinase activity.|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Phosphothreonine; by CaMK1|||Phosphothreonine; by LKB1 and GSK3-beta|||Phosphothreonine; by PKA|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex. Reduced inhibition of CRTC3-mediated transcriptional activity.|||Protein kinase|||Proton acceptor|||Putative serine/threonine-protein kinase SIK1B|||RK-rich region; required for cAMP responsiveness and nuclear localization|||Reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity.|||Reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-575.|||Serine/threonine-protein kinase SIK1|||Strongly reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity.|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086659|||http://purl.uniprot.org/annotation/PRO_0000444512|||http://purl.uniprot.org/annotation/VAR_021255|||http://purl.uniprot.org/annotation/VAR_033910|||http://purl.uniprot.org/annotation/VAR_041087|||http://purl.uniprot.org/annotation/VAR_041088|||http://purl.uniprot.org/annotation/VAR_041089|||http://purl.uniprot.org/annotation/VAR_041090|||http://purl.uniprot.org/annotation/VAR_041091|||http://purl.uniprot.org/annotation/VAR_041092|||http://purl.uniprot.org/annotation/VAR_073701|||http://purl.uniprot.org/annotation/VAR_073702|||http://purl.uniprot.org/annotation/VAR_073703
http://togogenome.org/gene/9606:SPON1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCB6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||C-linked (Man) tryptophan; partial|||N-linked (GlcNAc...) asparagine|||Reelin|||Spondin|||Spondin-1|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035865
http://togogenome.org/gene/9606:GRB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4F6|||http://purl.uniprot.org/uniprot/Q14451                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes Ras activity increase and ERK1/2 phosphorylation.|||Abolishes dimerization. Abolishes activation of HRAS.|||Abolishes phosphoinositide binding.|||Disordered|||Global loss of tyrosine phosphorylation. Abolishes interaction with FHL2 and HAX1.|||Growth factor receptor-bound protein 7|||Impairs phosphotyrosine binding by SH2 domain.|||Important for dimerization and for HRAS activation|||Important for lipid binding and for stimulation of cell migration|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphotyrosine; by FAK1|||Pro residues|||Ras-associating|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150344|||http://purl.uniprot.org/annotation/VSP_035500|||http://purl.uniprot.org/annotation/VSP_035501|||http://purl.uniprot.org/annotation/VSP_041665|||http://purl.uniprot.org/annotation/VSP_041666
http://togogenome.org/gene/9606:CPEB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXC1|||http://purl.uniprot.org/uniprot/Q5QP71|||http://purl.uniprot.org/uniprot/Q8NE35                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNA binding.|||Abolishes nuclear export; when associated with A-349.|||Abolishes nuclear export; when associated with A-353.|||Asymmetric dimethylarginine|||Cleavage; by CAPN2|||Cytoplasmic polyadenylation element-binding protein 3|||Disordered|||Does not impair RNA binding.|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||Reduced RNA binding.|||Required for RNA-binding activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269261|||http://purl.uniprot.org/annotation/VAR_029776|||http://purl.uniprot.org/annotation/VSP_022034|||http://purl.uniprot.org/annotation/VSP_022035
http://togogenome.org/gene/9606:TTC29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK62|||http://purl.uniprot.org/uniprot/E7EQ14|||http://purl.uniprot.org/uniprot/G5E9Z5|||http://purl.uniprot.org/uniprot/Q8NA56                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SPGF42.|||In SPGF42; loss of protein expression.|||In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||Tetratricopeptide repeat protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294435|||http://purl.uniprot.org/annotation/VAR_033179|||http://purl.uniprot.org/annotation/VAR_033180|||http://purl.uniprot.org/annotation/VAR_033181|||http://purl.uniprot.org/annotation/VAR_083646|||http://purl.uniprot.org/annotation/VAR_083647|||http://purl.uniprot.org/annotation/VSP_026638
http://togogenome.org/gene/9606:CFAP221                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0U5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 221|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with calmodulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320614|||http://purl.uniprot.org/annotation/VAR_039232|||http://purl.uniprot.org/annotation/VAR_039233|||http://purl.uniprot.org/annotation/VSP_039316|||http://purl.uniprot.org/annotation/VSP_039317|||http://purl.uniprot.org/annotation/VSP_039318|||http://purl.uniprot.org/annotation/VSP_039319|||http://purl.uniprot.org/annotation/VSP_039320|||http://purl.uniprot.org/annotation/VSP_039321
http://togogenome.org/gene/9606:SIGLEC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08ET2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||Loss of interaction with TYROBP.|||N-linked (GlcNAc...) asparagine|||Sialic acid-binding Ig-like lectin 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309314
http://togogenome.org/gene/9606:ANTKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KMW5|||http://purl.uniprot.org/uniprot/Q9BQD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Abolished methyltransferase activity.|||Abolished mitochondrial localization.|||Adenine nucleotide translocase lysine N-methyltransferase|||Disordered|||Does not affect mitochondrial localization.|||Helical|||Methyltransferase (MTase)|||N-terminal sequence (NTS)|||Pre-methyltransferase (preMT)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263721
http://togogenome.org/gene/9606:BBIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  BBSome-interacting protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342378|||http://purl.uniprot.org/annotation/VSP_045981|||http://purl.uniprot.org/annotation/VSP_046433|||http://purl.uniprot.org/annotation/VSP_046434
http://togogenome.org/gene/9606:GABPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06547                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||GA-binding protein subunit beta-1|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Minor effect upon interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-297; A-298 and A-299, or with A-307 and A-310.|||Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-270 and A-271.|||Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-305 and A-306.|||Minor reduction in transcriptional activation; when associated with A-295 or A-305 and A-306.|||Moderately reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-273 and A-275.|||N-acetylserine|||N6-acetyllysine|||No effect on transcriptional activation. Minor reduction in activity; when associated with A-270 and A-271.|||Removed|||Strongly reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-264 and A-265, or A-273 and A-275.|||Strongly reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-297; A-298 and A-299, or with A-307 and A-310.|||Transcription activation and HCFC1 interaction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066993|||http://purl.uniprot.org/annotation/VAR_035613|||http://purl.uniprot.org/annotation/VSP_000275|||http://purl.uniprot.org/annotation/VSP_009337
http://togogenome.org/gene/9606:ACTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35609                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Alpha-actinin-2|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||EF-hand 1|||EF-hand 2|||In CMD1AA.|||In CMH23 and CMD1AA.|||In CMH23.|||In CMYP8.|||In CMYP8; unknown pathological significance.|||In MPD6.|||In MPD6; unknown pathological significance.|||In isoform 2.|||Phosphothreonine|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073435|||http://purl.uniprot.org/annotation/VAR_033487|||http://purl.uniprot.org/annotation/VAR_054628|||http://purl.uniprot.org/annotation/VAR_071970|||http://purl.uniprot.org/annotation/VAR_071971|||http://purl.uniprot.org/annotation/VAR_071972|||http://purl.uniprot.org/annotation/VAR_071973|||http://purl.uniprot.org/annotation/VAR_074292|||http://purl.uniprot.org/annotation/VAR_083364|||http://purl.uniprot.org/annotation/VAR_083365|||http://purl.uniprot.org/annotation/VAR_083366|||http://purl.uniprot.org/annotation/VAR_083367|||http://purl.uniprot.org/annotation/VSP_054923
http://togogenome.org/gene/9606:IGF2BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZI8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 294-E-L-295.|||50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 423-E-L-424.|||50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 294-E-L-295 and 423-E-L-424.|||Disordered|||In isoform 2.|||Insulin-like growth factor 2 mRNA-binding protein 1|||KH 1|||KH 2|||KH 3|||KH 4|||Loss of binding to RBPR and loss of interaction with m6A-modified mRNA; when associated with 423-E-E-424.|||Loss of binding to RBPR and loss of interaction with m6A-modified mRNA; when associated with 505-E-E-506.|||Necessary for interaction with ELAVL4 and binding to TAU mRNA|||Partial reduction in interaction with m6A-modified mRNA; when associated with E-213.|||Partial reduction in interaction with m6A-modified mRNA; when associated with E-294.|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||Sufficient for nuclear export                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282533|||http://purl.uniprot.org/annotation/VSP_045366
http://togogenome.org/gene/9606:GTF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00403                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||Abolishes autoacetylation, represses transcription activity, does not inhibit its association with chromatin to promoter-specific regions and decreases the association of GTF2F1 with chromatin to promoter-specific regions.|||Core promoter DNA-binding|||Decreases BREd-dependent pre-initiation complex formation.|||Defects in transcription start site selection. Supports a level of transcription equivalent to wild-type.|||Does not inhibit interaction with TBP. Inhibits the recruitment of RNA polymerase II into the initiation complex.|||Does not inhibit the formation of the TATA box-bound TBP ternary complex.|||In a colorectal cancer sample; somatic mutation.|||Inhibits interaction with RNA polymerase II; when associated with E-286 and E-290.|||Inhibits interaction with RNA polymerase II; when associated with E-286 and E-295.|||Inhibits interaction with RNA polymerase II; when associated with E-290 and E-295.|||Inhibits interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-185. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-185.|||Inhibits interaction with SSU72; when associated with E-193. Reduces interaction with SSU72; when associated with E-200. Inhibits interaction with VP16; when associated with E-200. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-200.|||Inhibits interaction with TBP.|||N6-acetyllysine; by autocatalysis|||Necessary for TATA box-bound TBP complex formation|||Partial loss of HIV-1 Vpr binding.|||Phosphoserine|||Reduces DNA-binding.|||Reduces interaction with SSU72; when associated with E-185 or E-189. Inhibits interaction with VP16; when associated with E-189. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-189.|||Reduces interaction with SSU72; when associated with E-193 or E-200. Inhibits interaction with VP16; when associated with E-193. Inhibits RNA pol II transcription activation induced by VP16 but does not affect basal transcription; when associated with E-193.|||Reduces interaction with VP16; when associated with L-185.|||Reduces interaction with VP16; when associated with L-189.|||Reduces interaction with VP16; when associated with L-196.|||Reduces interaction with VP16; when associated with L-200.|||Reduces the formation of the TATA box-bound TBP ternary complex.|||TFIIB-type|||Transcription initiation factor IIB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119293|||http://purl.uniprot.org/annotation/VAR_011977|||http://purl.uniprot.org/annotation/VAR_035722
http://togogenome.org/gene/9606:SLC40A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP59                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  About 90% loss of HAMP binding.|||About 95% loss of HAMP binding.|||Associated with mild anemia and a tendency to iron loading. Prevents hepcidin/HAMP-induced degradation. Protects against severe malaria disease.|||Complete loss of HAMP-binding.|||Complete loss of HAMP-dependent ubiquitination. Does not affect protein stability. Does not affect cell surface localization.|||Cytoplasmic|||Extracellular|||Helical|||In HFE4.|||In HFE4; Does not affect protein stability. Does not affect cell surface localization. Increases iron export activity.|||In HFE4; Loss of iron export activity.|||In HFE4; Reduces protein stability. Loss of cell surface localization. Loss of iron export activity. Increases intracellular manganese.|||In HFE4; Reduces protein stability. Loss of cell surface localization. Loss of iron export function. Increases intracellular manganese.|||In iron overload.|||Loss of HAMP-induced endocytosis.|||Loss of iron export activity.|||Loss of iron export activity. Loss of cell surface localization. Increases intracellular manganese.|||Loss of iron export function.|||N-linked (GlcNAc...) asparagine|||No loss of ubiquitination; when associated with R-236.|||No loss of ubiquitination; when associated with R-253.|||Reduces protein stability.|||Reduces protein stability. Loss of cell surface localization. Loss of iron export activity. Increases intracellular manganese.|||Solute carrier family 40 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191310|||http://purl.uniprot.org/annotation/VAR_018980|||http://purl.uniprot.org/annotation/VAR_020295|||http://purl.uniprot.org/annotation/VAR_020296|||http://purl.uniprot.org/annotation/VAR_022594|||http://purl.uniprot.org/annotation/VAR_022595|||http://purl.uniprot.org/annotation/VAR_022596|||http://purl.uniprot.org/annotation/VAR_022597|||http://purl.uniprot.org/annotation/VAR_022598|||http://purl.uniprot.org/annotation/VAR_022599|||http://purl.uniprot.org/annotation/VAR_029299|||http://purl.uniprot.org/annotation/VAR_030057|||http://purl.uniprot.org/annotation/VAR_030058|||http://purl.uniprot.org/annotation/VAR_030059|||http://purl.uniprot.org/annotation/VAR_030060|||http://purl.uniprot.org/annotation/VAR_030061|||http://purl.uniprot.org/annotation/VAR_030062|||http://purl.uniprot.org/annotation/VAR_030063|||http://purl.uniprot.org/annotation/VAR_030064|||http://purl.uniprot.org/annotation/VAR_030065|||http://purl.uniprot.org/annotation/VAR_030066|||http://purl.uniprot.org/annotation/VAR_030067
http://togogenome.org/gene/9606:PRICKLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVG3|||http://purl.uniprot.org/uniprot/B3KVG6|||http://purl.uniprot.org/uniprot/Q96MT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes localization to the nuclear membrane.|||Basic residues|||Cysteine methyl ester|||Disordered|||In EPM1B.|||In EPM1B; affects interaction with REST.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||May be associated with NTD.|||PET|||Phosphoserine|||Prickle-like protein 1|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075889|||http://purl.uniprot.org/annotation/PRO_0000396712|||http://purl.uniprot.org/annotation/VAR_054663|||http://purl.uniprot.org/annotation/VAR_056164|||http://purl.uniprot.org/annotation/VAR_065580|||http://purl.uniprot.org/annotation/VAR_065581|||http://purl.uniprot.org/annotation/VAR_066850|||http://purl.uniprot.org/annotation/VAR_066851|||http://purl.uniprot.org/annotation/VAR_066852|||http://purl.uniprot.org/annotation/VAR_066853|||http://purl.uniprot.org/annotation/VAR_066854|||http://purl.uniprot.org/annotation/VAR_066855|||http://purl.uniprot.org/annotation/VAR_066856|||http://purl.uniprot.org/annotation/VAR_066857|||http://purl.uniprot.org/annotation/VAR_066858
http://togogenome.org/gene/9606:H4C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:RNF31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EP0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-935.|||Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-983.|||Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-935 and A-983.|||Abolished interaction with OTULIN.|||Abolished interaction with SPATA2.|||Abolishes cleavage by caspase.|||Abolishes polyubiquitination activity of LUBAC; when associated with S-699.|||Abolishes polyubiquitination activity of LUBAC; when associated with S-702.|||Abolishes polyubiquitination activity of LUBAC; when associated with S-871.|||Abolishes polyubiquitination activity of LUBAC; when associated with S-874.|||Cleavage; by caspase|||Decreased ubiquitin-binding and ability to promote formation of the bacterial ubiquitin coat.|||Disordered|||Does not affect interaction with OTULIN.|||E3 ubiquitin-protein ligase RNF31|||IBR-type|||In isoform 2.|||In isoform 3.|||Interaction with RBCK1|||LDD domain|||PUB|||Phosphoserine|||Polyubiquitin-binding|||Pro residues|||RING-type 1|||RING-type 2; atypical|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||Reduced interaction with OTULIN.|||Reduced ubiquitination; when associated with R-735 and R-783.|||Reduced ubiquitination; when associated with R-735 and R-875.|||Reduced ubiquitination; when associated with R-783 and R-875.|||TRIAD supradomain|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056069|||http://purl.uniprot.org/annotation/VAR_052102|||http://purl.uniprot.org/annotation/VSP_009647|||http://purl.uniprot.org/annotation/VSP_009648|||http://purl.uniprot.org/annotation/VSP_014006|||http://purl.uniprot.org/annotation/VSP_014007
http://togogenome.org/gene/9606:DLL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR61                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DSL|||Delta-like protein 4|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||Extracellular|||Helical|||In AOS6.|||Interaction with Notch1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007512|||http://purl.uniprot.org/annotation/VAR_075858|||http://purl.uniprot.org/annotation/VAR_075859|||http://purl.uniprot.org/annotation/VAR_075860|||http://purl.uniprot.org/annotation/VAR_075861|||http://purl.uniprot.org/annotation/VAR_075862|||http://purl.uniprot.org/annotation/VAR_075863|||http://purl.uniprot.org/annotation/VAR_075864
http://togogenome.org/gene/9606:PRTFDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoribosyltransferase domain-containing protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318176|||http://purl.uniprot.org/annotation/VSP_031179|||http://purl.uniprot.org/annotation/VSP_031180
http://togogenome.org/gene/9606:RBM45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUH3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||RNA-binding protein 45|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081572|||http://purl.uniprot.org/annotation/VSP_021005|||http://purl.uniprot.org/annotation/VSP_051661|||http://purl.uniprot.org/annotation/VSP_051662
http://togogenome.org/gene/9606:TMEM26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245865|||http://purl.uniprot.org/annotation/VSP_019806|||http://purl.uniprot.org/annotation/VSP_019807
http://togogenome.org/gene/9606:CWH43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DU47|||http://purl.uniprot.org/uniprot/B7ZAJ2|||http://purl.uniprot.org/uniprot/E7EQL2|||http://purl.uniprot.org/uniprot/Q9H720                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||PGAP2-interacting protein|||Required for function in lipid remodeling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320615|||http://purl.uniprot.org/annotation/VAR_039234|||http://purl.uniprot.org/annotation/VAR_039235
http://togogenome.org/gene/9606:UPF3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1J1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Increases NMD activity and translation stimulation.|||Phosphoserine|||Polar residues|||Regulator of nonsense transcripts 3A|||Required for association with EIF4A3 and ECJ core components CASC3, MAGOH and RBM8A|||Required for interaction with UPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215296|||http://purl.uniprot.org/annotation/VAR_062143|||http://purl.uniprot.org/annotation/VSP_012961|||http://purl.uniprot.org/annotation/VSP_012962
http://togogenome.org/gene/9606:CFHR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03591                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Complement factor H-related protein 1|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005896|||http://purl.uniprot.org/annotation/VAR_001980|||http://purl.uniprot.org/annotation/VAR_001981|||http://purl.uniprot.org/annotation/VAR_001982|||http://purl.uniprot.org/annotation/VAR_048816
http://togogenome.org/gene/9606:DNAH17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Dynein axonemal heavy chain 17|||In SPGF39.|||In SPGF39; loss of the outer dynein arms in sperm cells.|||In SPGF39; when associated in cis with L-3499; not expressed in flagellum and loss of the outer dynein arms in sperm cells when associated in cis with L-3499.|||In SPGF39; when associated in cis with P-3595; not expressed in flagellum and loss of the outer dynein arms in sperm cells when associated in cis with P-3595.|||In isoform 4.|||Stalk|||Stem|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323749|||http://purl.uniprot.org/annotation/VAR_039581|||http://purl.uniprot.org/annotation/VAR_062178|||http://purl.uniprot.org/annotation/VAR_062179|||http://purl.uniprot.org/annotation/VAR_062180|||http://purl.uniprot.org/annotation/VAR_083232|||http://purl.uniprot.org/annotation/VAR_083233|||http://purl.uniprot.org/annotation/VAR_083234|||http://purl.uniprot.org/annotation/VAR_083235|||http://purl.uniprot.org/annotation/VAR_083236|||http://purl.uniprot.org/annotation/VSP_032109|||http://purl.uniprot.org/annotation/VSP_032110|||http://purl.uniprot.org/annotation/VSP_032111
http://togogenome.org/gene/9606:FGFBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14512                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibroblast growth factor-binding protein 1|||O-linked (GalNAc...) serine|||Strongly reduces interaction with FGF2.|||Sufficient for interaction with FGF2 and FGF2-induced effects                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245512
http://togogenome.org/gene/9606:CETN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RFM2|||http://purl.uniprot.org/uniprot/E5RJF8|||http://purl.uniprot.org/uniprot/O15182                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Centrin-3|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073563|||http://purl.uniprot.org/annotation/VAR_030846
http://togogenome.org/gene/9606:MTHFD2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H903                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Splice Variant                                                                                  ^@                                                                                  Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial|||In isoform 1 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337097|||http://purl.uniprot.org/annotation/VSP_041877|||http://purl.uniprot.org/annotation/VSP_041878|||http://purl.uniprot.org/annotation/VSP_041879|||http://purl.uniprot.org/annotation/VSP_041880|||http://purl.uniprot.org/annotation/VSP_041881
http://togogenome.org/gene/9606:STK35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDR2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||No autophosphorylation.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086717
http://togogenome.org/gene/9606:TTC32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5I0X7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263100
http://togogenome.org/gene/9606:USH1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL95|||http://purl.uniprot.org/uniprot/Q495M9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Abolishes interaction with MAGI2.|||Basic and acidic residues|||Disordered|||In USH1G; atypical form with mild retinitis pigmentosa and normal vestibular function; also found in patients with autosomal recessive non-syndromic deafness; strongly reduced affinity for USH1C.|||In USH1G; reduced interaction with IFT52 and IFT57.|||Phosphomimetic mutant; does not affect interaction with MAGI2.|||Phosphoserine; by CK2|||Polar residues|||Probable disease-associated variant found in patients with non-syndromic sensorineural hearing loss; reduced interaction with IFT52 and IFT57; failure to rescue the USH1C splicing defect seen in USH1G-depleted cells.|||Reduced affinity for MYO7A.|||SAM|||Strongly reduced affinity for MYO7A.|||pre-mRNA splicing regulator USH1G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067077|||http://purl.uniprot.org/annotation/VAR_023739|||http://purl.uniprot.org/annotation/VAR_060468|||http://purl.uniprot.org/annotation/VAR_072369
http://togogenome.org/gene/9606:NXPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95157                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||II|||III|||IV (linker domain)|||N-linked (GlcNAc...) asparagine|||Neurexophilin-3|||V (Cys-rich)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020065
http://togogenome.org/gene/9606:SLC3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08195                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes dimerization, leucine uptake and interaction with beta-1 integrins.|||Amino acid transporter heavy chain SLC3A2|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Signal-anchor for type II membrane protein|||Impairs both the stability and the trafficking of SLC3A2 to the plasma membrane; when associated with Q-365 Q-381 and Q-424.|||Impairs both the stability and the trafficking of SLC3A2 to the plasma membrane; when associated with Q-365 Q-381 and Q-506.|||Impairs both the stability and the trafficking of SLC3A2 to the plasma membrane; when associated with Q-365; Q-424 and Q-506.|||Impairs both the stability and the trafficking of SLC3A2 to the plasma membrane; when associated with Q-381; Q-424 and Q-506.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interchain (with C-164 in SLC7A5; C-158 in SLC7A11 and C-154 in SLC7A8)|||N-acetylmethionine|||N-acetylserine|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Nearly abolishes leucine transport activity.|||No effect on dimerization, leucine uptake or interaction with beta-1 integrins.|||Phosphoserine|||Phosphothreonine|||Removed|||Strongly decreased leucine transport activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064383|||http://purl.uniprot.org/annotation/VSP_037907|||http://purl.uniprot.org/annotation/VSP_037908|||http://purl.uniprot.org/annotation/VSP_037909|||http://purl.uniprot.org/annotation/VSP_061769
http://togogenome.org/gene/9606:MRPS17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2R5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Mitochondrion|||Small ribosomal subunit protein uS17m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030623
http://togogenome.org/gene/9606:MFSD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ES6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Major facilitator superfamily domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273392|||http://purl.uniprot.org/annotation/VAR_030141
http://togogenome.org/gene/9606:SLC6A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Orphan sodium- and chloride-dependent neurotransmitter transporter NTT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214801|||http://purl.uniprot.org/annotation/VAR_052067|||http://purl.uniprot.org/annotation/VAR_064753|||http://purl.uniprot.org/annotation/VSP_056317
http://togogenome.org/gene/9606:APOBEC3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUX4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase 1|||CMP/dCMP-type deaminase 2|||DNA dC->dU-editing enzyme APOBEC-3F|||Decrease in cytidine deaminase and antiviral activity.|||Decrease in cytidine deaminase and antiviral activity; when associated with A-251.|||Decrease in cytidine deaminase and antiviral activity; when associated with A-67.|||In isoform 2.|||In isoform 3.|||No effect on cytidine deaminase and antiviral activity.|||Proton donor|||Remains able to bind Vif.|||Resistant to HIV-1 Vif and abolishes Vif binding but is still efficiently incorporated into the virion.|||Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion.|||Resistant to HIV-1 Vif and reduces Vif binding.|||Resistant to HIV-1 Vif, reduces Vif binding and abolishes incorporation into the virion.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171757|||http://purl.uniprot.org/annotation/VAR_018145|||http://purl.uniprot.org/annotation/VAR_018146|||http://purl.uniprot.org/annotation/VAR_018147|||http://purl.uniprot.org/annotation/VAR_018148|||http://purl.uniprot.org/annotation/VAR_025058|||http://purl.uniprot.org/annotation/VAR_025059|||http://purl.uniprot.org/annotation/VAR_038355|||http://purl.uniprot.org/annotation/VSP_009803|||http://purl.uniprot.org/annotation/VSP_009804|||http://purl.uniprot.org/annotation/VSP_042754|||http://purl.uniprot.org/annotation/VSP_042755
http://togogenome.org/gene/9606:IYD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VPV9|||http://purl.uniprot.org/uniprot/Q6PHW0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Activity as the wild type.|||Basic and acidic residues|||Disordered|||Helical|||In TDH4; strongly reduces activity; does not respond to the increase of flavin mononucleotide concentration.|||In TDH4; strongly reduces activity; marginally respond to the increase of flavin mononucleotide concentration; reduces protein stability.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Iodotyrosine deiodinase 1|||Nitroreductase|||Reduces activity.|||Strongly reduces activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230278|||http://purl.uniprot.org/annotation/VAR_025785|||http://purl.uniprot.org/annotation/VAR_045963|||http://purl.uniprot.org/annotation/VAR_045964|||http://purl.uniprot.org/annotation/VAR_045965|||http://purl.uniprot.org/annotation/VAR_045966|||http://purl.uniprot.org/annotation/VSP_017802|||http://purl.uniprot.org/annotation/VSP_017803|||http://purl.uniprot.org/annotation/VSP_017805|||http://purl.uniprot.org/annotation/VSP_017806|||http://purl.uniprot.org/annotation/VSP_017807|||http://purl.uniprot.org/annotation/VSP_017809|||http://purl.uniprot.org/annotation/VSP_017810|||http://purl.uniprot.org/annotation/VSP_017812|||http://purl.uniprot.org/annotation/VSP_017813
http://togogenome.org/gene/9606:NOP53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZM5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreased degradation in response to DNA damage. Decreased phosphorylation, degradation and increased interaction with RPL11 in response to DNA damage; when associated with A-233.|||Decreased phosphorylation, degradation and increased interaction with RPL11 in response to DNA damage; when associated with A-289.|||Disordered|||Loss of localization to the nucleolus and in response to DNA damage increased degradation and decreased interaction with RPL11; when associated with D-233.|||Loss of localization to the nucleolus and in response to DNA damage increased degradation and decreased interaction with RPL11; when associated with D-289.|||Mediates interaction with CDKN2A/isoform tumor suppressor ARF|||Mediates interaction with NF2|||Mediates interaction with human herpesvirus 8 protein ORF16|||N-acetylalanine|||Nucleolar localization signal|||Phosphoserine|||Removed|||Ribosome biogenesis protein NOP53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218960|||http://purl.uniprot.org/annotation/VAR_011486|||http://purl.uniprot.org/annotation/VAR_024456
http://togogenome.org/gene/9606:ZNF383                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 383                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047550
http://togogenome.org/gene/9606:KYAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DW13|||http://purl.uniprot.org/uniprot/Q6YP21                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aminotransferase class I/classII|||In isoform 2.|||In isoform 3.|||Kynurenine--oxoglutarate transaminase 3|||N-acetylserine|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287704|||http://purl.uniprot.org/annotation/VAR_032352|||http://purl.uniprot.org/annotation/VSP_025603|||http://purl.uniprot.org/annotation/VSP_025604|||http://purl.uniprot.org/annotation/VSP_042841
http://togogenome.org/gene/9606:STXBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5C0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Pro residues|||Syntaxin-binding protein 5|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051244|||http://purl.uniprot.org/annotation/VAR_035235|||http://purl.uniprot.org/annotation/VSP_016204|||http://purl.uniprot.org/annotation/VSP_016205
http://togogenome.org/gene/9606:C8orf44-SGK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BR1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes activity.|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased activation.|||Nuclear localization signal|||PX|||Partially localized to the membrane.|||Phosphoserine|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086649|||http://purl.uniprot.org/annotation/VAR_035636|||http://purl.uniprot.org/annotation/VAR_041076|||http://purl.uniprot.org/annotation/VSP_041903
http://togogenome.org/gene/9606:CUL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR50|||http://purl.uniprot.org/uniprot/Q13619                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cullin family profile|||Cullin-4A|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Largely reduces interaction with DDB1; abolishes interaction with DDB2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119795|||http://purl.uniprot.org/annotation/VAR_020341|||http://purl.uniprot.org/annotation/VSP_018577
http://togogenome.org/gene/9606:MAP7D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU03|||http://purl.uniprot.org/uniprot/Q3KQU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MAP7 domain-containing protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306807|||http://purl.uniprot.org/annotation/VAR_035312|||http://purl.uniprot.org/annotation/VAR_053970|||http://purl.uniprot.org/annotation/VSP_028483|||http://purl.uniprot.org/annotation/VSP_028484|||http://purl.uniprot.org/annotation/VSP_028485|||http://purl.uniprot.org/annotation/VSP_028486|||http://purl.uniprot.org/annotation/VSP_028487|||http://purl.uniprot.org/annotation/VSP_028488
http://togogenome.org/gene/9606:ARHGEF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286589|||http://purl.uniprot.org/annotation/VAR_032132|||http://purl.uniprot.org/annotation/VAR_032133
http://togogenome.org/gene/9606:POTEI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG38                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Actin-like|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395413
http://togogenome.org/gene/9606:AGBL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU57                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic carboxypeptidase 6|||Disordered|||In isoform 2.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284835|||http://purl.uniprot.org/annotation/VAR_061078|||http://purl.uniprot.org/annotation/VSP_040435|||http://purl.uniprot.org/annotation/VSP_040436
http://togogenome.org/gene/9606:RYR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21817                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3; truncated|||4; truncated|||5|||6|||6 X approximate repeats|||Acidic residues|||Associated in cis with S-2787; may be associated with susceptibility to malignant hyperthermia.|||Associated in cis with W-2676; may be associated with susceptibility to malignant hyperthermia.|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EF-hand|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In CMYP1A and MHS1.|||In CMYP1A and MHS1; 2-3% of the cases; increases calcium-induced calcium release activity.|||In CMYP1A and MHS1; 3-5% of the cases; increases calcium-induced calcium release activity.|||In CMYP1A and MHS1; increases calcium-induced calcium release activity.|||In CMYP1A and MHS1; no difference in the thapsigargin-sensitive calcium stores of cells carrying this mutation and the wild-type; increases calcium-induced calcium release activity.|||In CMYP1A and MHS1; release of calcium from intracellular stores in the absence of any pharmacological activator of RYR.|||In CMYP1A.|||In CMYP1A; increases sensitivity to caffeine and 4-chloro-m-cresol.|||In CMYP1A; release of calcium from intracellular stores in the absence of any pharmacological activator of RYR; smaller thapsigargin-sensitive intracellular calcium stores; normal sensitivity of the calcium release to the RYR inhibitor dantrolene.|||In CMYP1A; severe phenotype.|||In CMYP1A; unknown pathological significance.|||In CMYP1B.|||In KDS.|||In KDS; unknown pathological significance.|||In MHS1 and CMYP1B.|||In MHS1 and KDS.|||In MHS1, CMYP1A and KDS; increases sensitivity to caffeine and 4-chloro-m-cresol; increases calcium-induced calcium release activity.|||In MHS1.|||In MHS1; 10% of the cases; increases calcium-induced calcium release activity.|||In MHS1; has increased sensitivity to both caffeine and halothane.|||In MHS1; increases calcium-induced calcium release activity.|||In MHS1; increases sensitivity to caffeine and 4-chloro-m-cresol; increases calcium-induced calcium release activity.|||In MHS1; induces an increase sensitivity to caffeine.|||In MHS1; induces an increase sensitivity to caffeine; increases calcium-induced calcium release activity.|||In MHS1; requires 2 nucleotide substitutions; unknown pathological significance.|||In MHS1; reveals an altered calcium dependence and increased caffeine sensitivity; increases calcium-induced calcium release activity.|||In MHS1; severe form; increases calcium-induced calcium release activity.|||In MHS1; unknown pathological significance.|||In MHS1; unknown pathological significance; increases calcium-induced calcium release activity.|||In MHS1; unknown pathological significance; slightly increases Ca(2+) release in response to 4-chloro-m-cresol.|||In core/rod disease.|||In isoform 2.|||In isoform 3.|||Increases calcium-induced calcium release activity.|||Increases sensitivity to caffeine and 4-chloro-m-cresol.|||Interaction with CALM|||Interaction with FKBP1A|||Lumenal|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||May be associated with susceptibility to malignant hyperthermia.|||Phosphoserine|||Phosphoserine; by PKA and PKG|||Phosphothreonine|||Phosphotyrosine|||Pore-forming|||Pro residues|||Probable disease-associated variant found in a family with Samaritan myopathy.|||Probable disease-associated variant found in primary myopathy causing fetal akinesia and pregnancy loss.|||Ryanodine receptor 1|||S-nitrosocysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219358|||http://purl.uniprot.org/annotation/VAR_005589|||http://purl.uniprot.org/annotation/VAR_005590|||http://purl.uniprot.org/annotation/VAR_005591|||http://purl.uniprot.org/annotation/VAR_005592|||http://purl.uniprot.org/annotation/VAR_005593|||http://purl.uniprot.org/annotation/VAR_005594|||http://purl.uniprot.org/annotation/VAR_005595|||http://purl.uniprot.org/annotation/VAR_005596|||http://purl.uniprot.org/annotation/VAR_005597|||http://purl.uniprot.org/annotation/VAR_005598|||http://purl.uniprot.org/annotation/VAR_005599|||http://purl.uniprot.org/annotation/VAR_005600|||http://purl.uniprot.org/annotation/VAR_005601|||http://purl.uniprot.org/annotation/VAR_005602|||http://purl.uniprot.org/annotation/VAR_005603|||http://purl.uniprot.org/annotation/VAR_005604|||http://purl.uniprot.org/annotation/VAR_005605|||http://purl.uniprot.org/annotation/VAR_005606|||http://purl.uniprot.org/annotation/VAR_008971|||http://purl.uniprot.org/annotation/VAR_008972|||http://purl.uniprot.org/annotation/VAR_008973|||http://purl.uniprot.org/annotation/VAR_008974|||http://purl.uniprot.org/annotation/VAR_008975|||http://purl.uniprot.org/annotation/VAR_008976|||http://purl.uniprot.org/annotation/VAR_008977|||http://purl.uniprot.org/annotation/VAR_008978|||http://purl.uniprot.org/annotation/VAR_032910|||http://purl.uniprot.org/annotation/VAR_032911|||http://purl.uniprot.org/annotation/VAR_032912|||http://purl.uniprot.org/annotation/VAR_032913|||http://purl.uniprot.org/annotation/VAR_032914|||http://purl.uniprot.org/annotation/VAR_032915|||http://purl.uniprot.org/annotation/VAR_032916|||http://purl.uniprot.org/annotation/VAR_045694|||http://purl.uniprot.org/annotation/VAR_045695|||http://purl.uniprot.org/annotation/VAR_045696|||http://purl.uniprot.org/annotation/VAR_045697|||http://purl.uniprot.org/annotation/VAR_045698|||http://purl.uniprot.org/annotation/VAR_045699|||http://purl.uniprot.org/annotation/VAR_045700|||http://purl.uniprot.org/annotation/VAR_045701|||http://purl.uniprot.org/annotation/VAR_045702|||http://purl.uniprot.org/annotation/VAR_045703|||http://purl.uniprot.org/annotation/VAR_045704|||http://purl.uniprot.org/annotation/VAR_045705|||http://purl.uniprot.org/annotation/VAR_045706|||http://purl.uniprot.org/annotation/VAR_045707|||http://purl.uniprot.org/annotation/VAR_045708|||http://purl.uniprot.org/annotation/VAR_045709|||http://purl.uniprot.org/annotation/VAR_045710|||http://purl.uniprot.org/annotation/VAR_045711|||http://purl.uniprot.org/annotation/VAR_045712|||http://purl.uniprot.org/annotation/VAR_045713|||http://purl.uniprot.org/annotation/VAR_045714|||http://purl.uniprot.org/annotation/VAR_045715|||http://purl.uniprot.org/annotation/VAR_045716|||http://purl.uniprot.org/annotation/VAR_045717|||http://purl.uniprot.org/annotation/VAR_045718|||http://purl.uniprot.org/annotation/VAR_045719|||http://purl.uniprot.org/annotation/VAR_045720|||http://purl.uniprot.org/annotation/VAR_045721|||http://purl.uniprot.org/annotation/VAR_045722|||http://purl.uniprot.org/annotation/VAR_045723|||http://purl.uniprot.org/annotation/VAR_045724|||http://purl.uniprot.org/annotation/VAR_045725|||http://purl.uniprot.org/annotation/VAR_045726|||http://purl.uniprot.org/annotation/VAR_045727|||http://purl.uniprot.org/annotation/VAR_045728|||http://purl.uniprot.org/annotation/VAR_045729|||http://purl.uniprot.org/annotation/VAR_045730|||http://purl.uniprot.org/annotation/VAR_045731|||http://purl.uniprot.org/annotation/VAR_045732|||http://purl.uniprot.org/annotation/VAR_045733|||http://purl.uniprot.org/annotation/VAR_045734|||http://purl.uniprot.org/annotation/VAR_045735|||http://purl.uniprot.org/annotation/VAR_045736|||http://purl.uniprot.org/annotation/VAR_045737|||http://purl.uniprot.org/annotation/VAR_045738|||http://purl.uniprot.org/annotation/VAR_045739|||http://purl.uniprot.org/annotation/VAR_045740|||http://purl.uniprot.org/annotation/VAR_045741|||http://purl.uniprot.org/annotation/VAR_045742|||http://purl.uniprot.org/annotation/VAR_045743|||http://purl.uniprot.org/annotation/VAR_045744|||http://purl.uniprot.org/annotation/VAR_045745|||http://purl.uniprot.org/annotation/VAR_045746|||http://purl.uniprot.org/annotation/VAR_045747|||http://purl.uniprot.org/annotation/VAR_045748|||http://purl.uniprot.org/annotation/VAR_045749|||http://purl.uniprot.org/annotation/VAR_045750|||http://purl.uniprot.org/annotation/VAR_045751|||http://purl.uniprot.org/annotation/VAR_045752|||http://purl.uniprot.org/annotation/VAR_045753|||http://purl.uniprot.org/annotation/VAR_045754|||http://purl.uniprot.org/annotation/VAR_045755|||http://purl.uniprot.org/annotation/VAR_045756|||http://purl.uniprot.org/annotation/VAR_045757|||http://purl.uniprot.org/annotation/VAR_045758|||http://purl.uniprot.org/annotation/VAR_045759|||http://purl.uniprot.org/annotation/VAR_045760|||http://purl.uniprot.org/annotation/VAR_045761|||http://purl.uniprot.org/annotation/VAR_045762|||http://purl.uniprot.org/annotation/VAR_045763|||http://purl.uniprot.org/annotation/VAR_045764|||http://purl.uniprot.org/annotation/VAR_045765|||http://purl.uniprot.org/annotation/VAR_045766|||http://purl.uniprot.org/annotation/VAR_045767|||http://purl.uniprot.org/annotation/VAR_045768|||http://purl.uniprot.org/annotation/VAR_045769|||http://purl.uniprot.org/annotation/VAR_045770|||http://purl.uniprot.org/annotation/VAR_045771|||http://purl.uniprot.org/annotation/VAR_045772|||http://purl.uniprot.org/annotation/VAR_045773|||http://purl.uniprot.org/annotation/VAR_045774|||http://purl.uniprot.org/annotation/VAR_045775|||http://purl.uniprot.org/annotation/VAR_045776|||http://purl.uniprot.org/annotation/VAR_045777|||http://purl.uniprot.org/annotation/VAR_045778|||http://purl.uniprot.org/annotation/VAR_045779|||http://purl.uniprot.org/annotation/VAR_045780|||http://purl.uniprot.org/annotation/VAR_045781|||http://purl.uniprot.org/annotation/VAR_045782|||http://purl.uniprot.org/annotation/VAR_051890|||http://purl.uniprot.org/annotation/VAR_051891|||http://purl.uniprot.org/annotation/VAR_051892|||http://purl.uniprot.org/annotation/VAR_058560|||http://purl.uniprot.org/annotation/VAR_058561|||http://purl.uniprot.org/annotation/VAR_058562|||http://purl.uniprot.org/annotation/VAR_058563|||http://purl.uniprot.org/annotation/VAR_058564|||http://purl.uniprot.org/annotation/VAR_058565|||http://purl.uniprot.org/annotation/VAR_058566|||http://purl.uniprot.org/annotation/VAR_058567|||http://purl.uniprot.org/annotation/VAR_058568|||http://purl.uniprot.org/annotation/VAR_058569|||http://purl.uniprot.org/annotation/VAR_058570|||http://purl.uniprot.org/annotation/VAR_058571|||http://purl.uniprot.org/annotation/VAR_058572|||http://purl.uniprot.org/annotation/VAR_058573|||http://purl.uniprot.org/annotation/VAR_058574|||http://purl.uniprot.org/annotation/VAR_058575|||http://purl.uniprot.org/annotation/VAR_058576|||http://purl.uniprot.org/annotation/VAR_058577|||http://purl.uniprot.org/annotation/VAR_058578|||http://purl.uniprot.org/annotation/VAR_058579|||http://purl.uniprot.org/annotation/VAR_063846|||http://purl.uniprot.org/annotation/VAR_063847|||http://purl.uniprot.org/annotation/VAR_063848|||http://purl.uniprot.org/annotation/VAR_063849|||http://purl.uniprot.org/annotation/VAR_068510|||http://purl.uniprot.org/annotation/VAR_068511|||http://purl.uniprot.org/annotation/VAR_068512|||http://purl.uniprot.org/annotation/VAR_068513|||http://purl.uniprot.org/annotation/VAR_068514|||http://purl.uniprot.org/annotation/VAR_068515|||http://purl.uniprot.org/annotation/VAR_068516|||http://purl.uniprot.org/annotation/VAR_068517|||http://purl.uniprot.org/annotation/VAR_068518|||http://purl.uniprot.org/annotation/VAR_068519|||http://purl.uniprot.org/annotation/VAR_068520|||http://purl.uniprot.org/annotation/VAR_068521|||http://purl.uniprot.org/annotation/VAR_071721|||http://purl.uniprot.org/annotation/VAR_071722|||http://purl.uniprot.org/annotation/VAR_071723|||http://purl.uniprot.org/annotation/VAR_071724|||http://purl.uniprot.org/annotation/VAR_071725|||http://purl.uniprot.org/annotation/VAR_071726|||http://purl.uniprot.org/annotation/VAR_071727|||http://purl.uniprot.org/annotation/VAR_071728|||http://purl.uniprot.org/annotation/VAR_071729|||http://purl.uniprot.org/annotation/VAR_071730|||http://purl.uniprot.org/annotation/VAR_071731|||http://purl.uniprot.org/annotation/VAR_071732|||http://purl.uniprot.org/annotation/VAR_071733|||http://purl.uniprot.org/annotation/VAR_071734|||http://purl.uniprot.org/annotation/VAR_071735|||http://purl.uniprot.org/annotation/VAR_071736|||http://purl.uniprot.org/annotation/VAR_071738|||http://purl.uniprot.org/annotation/VAR_071739|||http://purl.uniprot.org/annotation/VAR_071740|||http://purl.uniprot.org/annotation/VAR_071741|||http://purl.uniprot.org/annotation/VAR_071742|||http://purl.uniprot.org/annotation/VAR_071743|||http://purl.uniprot.org/annotation/VAR_071744|||http://purl.uniprot.org/annotation/VAR_071745|||http://purl.uniprot.org/annotation/VAR_071746|||http://purl.uniprot.org/annotation/VAR_071747|||http://purl.uniprot.org/annotation/VAR_071748|||http://purl.uniprot.org/annotation/VAR_071749|||http://purl.uniprot.org/annotation/VAR_071750|||http://purl.uniprot.org/annotation/VAR_071751|||http://purl.uniprot.org/annotation/VAR_071752|||http://purl.uniprot.org/annotation/VAR_071753|||http://purl.uniprot.org/annotation/VAR_071754|||http://purl.uniprot.org/annotation/VAR_071755|||http://purl.uniprot.org/annotation/VAR_075399|||http://purl.uniprot.org/annotation/VAR_076568|||http://purl.uniprot.org/annotation/VAR_076569|||http://purl.uniprot.org/annotation/VAR_077682|||http://purl.uniprot.org/annotation/VAR_077683|||http://purl.uniprot.org/annotation/VAR_078775|||http://purl.uniprot.org/annotation/VAR_086256|||http://purl.uniprot.org/annotation/VAR_086257|||http://purl.uniprot.org/annotation/VSP_005951|||http://purl.uniprot.org/annotation/VSP_005952
http://togogenome.org/gene/9606:ATIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31939|||http://purl.uniprot.org/uniprot/V9HWH7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AICAR formyltransferase|||Bifunctional purine biosynthesis protein ATIC|||Bifunctional purine biosynthesis protein ATIC, N-terminally processed|||Decreased FAICAR cyclization activity; no change in affinity to FAICAR.|||Decreased affinity to FAICAR; no change in FAICAR cyclization activity.|||IMP cyclohydrolase|||In AICAR; loss of transformylase activity.|||In isoform 2.|||Loss of AICAR transformylase activity.|||MGS-like|||N-acetylmethionine|||N6-acetyllysine|||Proton acceptor; for AICAR formyltransferase activity|||Proton donor/acceptor; for FAICAR cyclization activity|||Removed; alternate|||Transition state stabilizer|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192156|||http://purl.uniprot.org/annotation/PRO_0000434376|||http://purl.uniprot.org/annotation/VAR_019306|||http://purl.uniprot.org/annotation/VAR_019307|||http://purl.uniprot.org/annotation/VSP_053495
http://togogenome.org/gene/9606:HAUS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT25                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HAUS augmin-like complex subunit 8|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319937|||http://purl.uniprot.org/annotation/VAR_039056|||http://purl.uniprot.org/annotation/VSP_031543|||http://purl.uniprot.org/annotation/VSP_047167
http://togogenome.org/gene/9606:DDX41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRK2|||http://purl.uniprot.org/uniprot/Q9UJV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In MPLPF; no effect on localization; changed interaction with spliceosomal complexes.|||In MPLPF; unknown pathological significance.|||In MPLPF; unknown pathological significance; no effect on localization.|||Phosphoserine|||Phosphotyrosine|||Probable ATP-dependent RNA helicase DDX41|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054970|||http://purl.uniprot.org/annotation/VAR_076360|||http://purl.uniprot.org/annotation/VAR_076361|||http://purl.uniprot.org/annotation/VAR_076362
http://togogenome.org/gene/9606:DGUOK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KSL5|||http://purl.uniprot.org/uniprot/E5KSL6|||http://purl.uniprot.org/uniprot/Q16854                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Deoxyguanosine kinase, mitochondrial|||Deoxynucleoside kinase|||In MTDPS3.|||In MTDPS3; significant reduction of activity.|||In NCPH1; impairs adenosine triphosphate binding; reduction of activity.|||In PEOB4; decreased protein levels.|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||Mitochondrion|||N6-acetyllysine|||Proton acceptor|||Reduction of activity.|||Unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016840|||http://purl.uniprot.org/annotation/VAR_019417|||http://purl.uniprot.org/annotation/VAR_019418|||http://purl.uniprot.org/annotation/VAR_023789|||http://purl.uniprot.org/annotation/VAR_076979|||http://purl.uniprot.org/annotation/VAR_076980|||http://purl.uniprot.org/annotation/VAR_076981|||http://purl.uniprot.org/annotation/VAR_076982|||http://purl.uniprot.org/annotation/VAR_076983|||http://purl.uniprot.org/annotation/VSP_003024|||http://purl.uniprot.org/annotation/VSP_003025|||http://purl.uniprot.org/annotation/VSP_003026|||http://purl.uniprot.org/annotation/VSP_056026|||http://purl.uniprot.org/annotation/VSP_056027
http://togogenome.org/gene/9606:RBM47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AV96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Decreased function in regulation of alternative splicing. Decreased pre-mRNA binding. No effect on homodimerization.|||Decreased function in regulation of alternative splicing. No effect on pre-mRNA binding.|||Disordered|||In isoform 2.|||Loss of function in regulation of alternative splicing. Loss of pre-mRNA binding activity. Decreased homodimerization.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Polar residues|||RNA-binding protein 47|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307855|||http://purl.uniprot.org/annotation/VAR_054770|||http://purl.uniprot.org/annotation/VAR_061832|||http://purl.uniprot.org/annotation/VSP_028839
http://togogenome.org/gene/9606:UBE2W                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B02|||http://purl.uniprot.org/uniprot/Q96FI0|||http://purl.uniprot.org/uniprot/X6REH9                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||Impaired substrate ubiquitination of both Tau and ATXN3.|||In isoform 2.|||In isoform 3.|||Loss of predominant nuclear localization.|||Loss of ubiquitin conjugating activity.|||Loss of ubiquitination activity toward various substrates, including POLR2H, ATXN3, STUB1 and MAPT.|||Loss of ubiquitination activity.|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||UBC core|||Ubiquitin-conjugating enzyme E2 W                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232689|||http://purl.uniprot.org/annotation/VSP_017943|||http://purl.uniprot.org/annotation/VSP_042974
http://togogenome.org/gene/9606:TIMM8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XAN8|||http://purl.uniprot.org/uniprot/Q9Y5J9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit Tim8 B|||N-acetylalanine|||Removed|||Tim10-like|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193587
http://togogenome.org/gene/9606:COX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DI26|||http://purl.uniprot.org/uniprot/Q9Y6N1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX11, mitochondrial|||Disordered|||Helical|||In MC4DN23; unknown pathological significance; decreased respiration-derived ATP levels in patient cells.|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006080|||http://purl.uniprot.org/annotation/VAR_048831|||http://purl.uniprot.org/annotation/VAR_088428|||http://purl.uniprot.org/annotation/VSP_046360
http://togogenome.org/gene/9606:NKX6-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78426                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-6.1|||Involved in DNA-binding|||Polar residues|||Repressor domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048951
http://togogenome.org/gene/9606:ERAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R769|||http://purl.uniprot.org/uniprot/Q6P179                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aminopeptidase N-like N-terminal|||Cytoplasmic|||ERAP1-like C-terminal|||Endoplasmic reticulum aminopeptidase 2|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M1 membrane alanine aminopeptidase|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315719|||http://purl.uniprot.org/annotation/VAR_038285|||http://purl.uniprot.org/annotation/VAR_038286|||http://purl.uniprot.org/annotation/VAR_038287|||http://purl.uniprot.org/annotation/VAR_051569|||http://purl.uniprot.org/annotation/VSP_030671|||http://purl.uniprot.org/annotation/VSP_030672|||http://purl.uniprot.org/annotation/VSP_030673|||http://purl.uniprot.org/annotation/VSP_030674|||http://purl.uniprot.org/annotation/VSP_030675
http://togogenome.org/gene/9606:ZNF154                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13106                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 154                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047430|||http://purl.uniprot.org/annotation/VAR_052779|||http://purl.uniprot.org/annotation/VAR_052780|||http://purl.uniprot.org/annotation/VAR_052781|||http://purl.uniprot.org/annotation/VAR_060678
http://togogenome.org/gene/9606:CCDC149                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 149|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344209|||http://purl.uniprot.org/annotation/VSP_034741|||http://purl.uniprot.org/annotation/VSP_034742|||http://purl.uniprot.org/annotation/VSP_034743|||http://purl.uniprot.org/annotation/VSP_042498|||http://purl.uniprot.org/annotation/VSP_042499|||http://purl.uniprot.org/annotation/VSP_042500
http://togogenome.org/gene/9606:MPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95563                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial pyruvate carrier 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212793
http://togogenome.org/gene/9606:SLAMF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVL7|||http://purl.uniprot.org/uniprot/B4DW98|||http://purl.uniprot.org/uniprot/Q9NQ25                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||ITSM|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with FYN when phosphorylated at Tyr-284|||N-linked (GlcNAc...) asparagine|||SLAM family member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014963|||http://purl.uniprot.org/annotation/PRO_5014567690|||http://purl.uniprot.org/annotation/PRO_5014567693|||http://purl.uniprot.org/annotation/VAR_049938|||http://purl.uniprot.org/annotation/VAR_049939|||http://purl.uniprot.org/annotation/VSP_013781|||http://purl.uniprot.org/annotation/VSP_013782|||http://purl.uniprot.org/annotation/VSP_054540|||http://purl.uniprot.org/annotation/VSP_054541|||http://purl.uniprot.org/annotation/VSP_054542|||http://purl.uniprot.org/annotation/VSP_055292|||http://purl.uniprot.org/annotation/VSP_055293
http://togogenome.org/gene/9606:SLC7A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY07                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cationic amino acid transporter 3|||Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054266|||http://purl.uniprot.org/annotation/VAR_048154|||http://purl.uniprot.org/annotation/VAR_064754
http://togogenome.org/gene/9606:STAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52630|||http://purl.uniprot.org/uniprot/R9QE65                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PTORCH3; increased cellular sensitivity to type IIFNs; fails to appropriately traffic USP18 thereby preventing USP18 to inhibit responses to IFN-I.|||In PTORCH3; increased cellular sensitivity to type IIFNs; loss of interaction with USP18 thereby preventing USP18 to inhibit responses to IFN-I.|||In isoform 2.|||Interaction with SFTSV virus NSs|||Interaction with heartland virus NSs|||Mediates interaction with USP18|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by JAK|||Prevents the nuclear import; when associated with A-374.|||Prevents the nuclear import; when associated with A-375.|||Prevents the nuclear import; when associated with A-409.|||Prevents the nuclear import; when associated with A-415.|||Reduces phosphorylation of STAT1 in response to IFN-ALPHA.|||SH2|||Signal transducer and activator of transcription 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182413|||http://purl.uniprot.org/annotation/VAR_014896|||http://purl.uniprot.org/annotation/VAR_014897|||http://purl.uniprot.org/annotation/VAR_014898|||http://purl.uniprot.org/annotation/VAR_014899|||http://purl.uniprot.org/annotation/VAR_014900|||http://purl.uniprot.org/annotation/VAR_014901|||http://purl.uniprot.org/annotation/VAR_019213|||http://purl.uniprot.org/annotation/VAR_052072|||http://purl.uniprot.org/annotation/VAR_084450|||http://purl.uniprot.org/annotation/VAR_084451|||http://purl.uniprot.org/annotation/VSP_046705
http://togogenome.org/gene/9606:RAD18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS91                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not interact with SLF1 and is defective in restoring cell survival after DNA damage; when associated with A-442.|||Does not interact with SLF1 and is defective in restoring cell survival after DNA damage; when associated with A-444.|||E3 ubiquitin-protein ligase RAD18|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LR motif|||Lower activity toward PCNA monoubiquitination.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RING-type|||SAP|||UBZ4-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056149|||http://purl.uniprot.org/annotation/VAR_023423|||http://purl.uniprot.org/annotation/VAR_023424|||http://purl.uniprot.org/annotation/VAR_023425
http://togogenome.org/gene/9606:KRTAP13-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 10 AA approximate repeats|||Keratin-associated protein 13-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185200
http://togogenome.org/gene/9606:RNF135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUD6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase RNF135|||Found in an individual with overgrowth, learning disability and dysmorphic features; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of function in RIG-I signaling pathway; when associated with A-21.|||Loss of function in RIG-I signaling pathway; when associated with A-24.|||Prevents degradation by hepatitis C virus NS3/NS4A.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280557|||http://purl.uniprot.org/annotation/VAR_031165|||http://purl.uniprot.org/annotation/VAR_031166|||http://purl.uniprot.org/annotation/VAR_037652|||http://purl.uniprot.org/annotation/VAR_063495|||http://purl.uniprot.org/annotation/VAR_063496|||http://purl.uniprot.org/annotation/VSP_023785|||http://purl.uniprot.org/annotation/VSP_023786|||http://purl.uniprot.org/annotation/VSP_045359|||http://purl.uniprot.org/annotation/VSP_045360
http://togogenome.org/gene/9606:BNIP3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60238|||http://purl.uniprot.org/uniprot/Q6IBV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like|||BH3|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064957|||http://purl.uniprot.org/annotation/VSP_056248
http://togogenome.org/gene/9606:LIPJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W064                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  Charge relay system|||Lipase member J|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288970|||http://purl.uniprot.org/annotation/VAR_032543
http://togogenome.org/gene/9606:FRMPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1N9|||http://purl.uniprot.org/uniprot/Q68DX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the basolateral membrane localization.|||Disordered|||FERM|||FERM and PDZ domain-containing protein 2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KIND|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306854|||http://purl.uniprot.org/annotation/VAR_035446|||http://purl.uniprot.org/annotation/VAR_055540|||http://purl.uniprot.org/annotation/VAR_055541|||http://purl.uniprot.org/annotation/VAR_061034|||http://purl.uniprot.org/annotation/VAR_065253|||http://purl.uniprot.org/annotation/VAR_072402|||http://purl.uniprot.org/annotation/VSP_028521|||http://purl.uniprot.org/annotation/VSP_028522|||http://purl.uniprot.org/annotation/VSP_028523|||http://purl.uniprot.org/annotation/VSP_028524|||http://purl.uniprot.org/annotation/VSP_028525|||http://purl.uniprot.org/annotation/VSP_028526|||http://purl.uniprot.org/annotation/VSP_028527|||http://purl.uniprot.org/annotation/VSP_028528
http://togogenome.org/gene/9606:PGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75T13                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||GPI inositol-deacylase|||Helical|||In NEDDSBA; results in loss of PI-specific phospholipase C sensitivity which could be rescued by expression of the wild-type protein.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277623|||http://purl.uniprot.org/annotation/VAR_071772|||http://purl.uniprot.org/annotation/VSP_023040|||http://purl.uniprot.org/annotation/VSP_023041|||http://purl.uniprot.org/annotation/VSP_023042|||http://purl.uniprot.org/annotation/VSP_023043|||http://purl.uniprot.org/annotation/VSP_023044
http://togogenome.org/gene/9606:TMEM104                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE00                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 104                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254178|||http://purl.uniprot.org/annotation/VAR_028831|||http://purl.uniprot.org/annotation/VAR_028832|||http://purl.uniprot.org/annotation/VSP_021199|||http://purl.uniprot.org/annotation/VSP_021200
http://togogenome.org/gene/9606:GPR89A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAQ6|||http://purl.uniprot.org/uniprot/P0CG08|||http://purl.uniprot.org/uniprot/X5D7G6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abscisic acid G-protein coupled receptor-like|||Golgi pH regulator A|||Golgi pH regulator B|||Golgi pH regulator conserved|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223260|||http://purl.uniprot.org/annotation/PRO_0000395006|||http://purl.uniprot.org/annotation/VSP_017247|||http://purl.uniprot.org/annotation/VSP_039346|||http://purl.uniprot.org/annotation/VSP_055892|||http://purl.uniprot.org/annotation/VSP_055893
http://togogenome.org/gene/9606:MIOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXC5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||GATOR2 complex protein MIOS|||Impaired amino-acid-mediated mTORC1 activation.|||Impaired assembly of the GATOR2 complex.|||In isoform 2.|||Phosphoserine|||RING-type; atypical|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329404|||http://purl.uniprot.org/annotation/VSP_032979|||http://purl.uniprot.org/annotation/VSP_032980
http://togogenome.org/gene/9606:GUCY1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33402                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Guanylate cyclase|||Guanylate cyclase soluble subunit alpha-2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074113|||http://purl.uniprot.org/annotation/VAR_036420|||http://purl.uniprot.org/annotation/VAR_036421|||http://purl.uniprot.org/annotation/VSP_001814|||http://purl.uniprot.org/annotation/VSP_054154
http://togogenome.org/gene/9606:SIK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5A9|||http://purl.uniprot.org/uniprot/Q9Y2K2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SEMDK; decreased protein expression; decreased kinase activity; no effect on the interaction with DEPTOR, MLST8/GbetaL, RICTOR and RPTOR.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with 14-3-3 proteins in response to cAMP signaling; inhibits cAMP signaling.|||No effect on cAMP signaling.|||No effect on interaction with 14-3-3 proteins, nor on cAMP signaling.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SIK3|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252257|||http://purl.uniprot.org/annotation/VAR_035634|||http://purl.uniprot.org/annotation/VAR_035635|||http://purl.uniprot.org/annotation/VAR_051662|||http://purl.uniprot.org/annotation/VAR_051663|||http://purl.uniprot.org/annotation/VAR_081542|||http://purl.uniprot.org/annotation/VSP_059412|||http://purl.uniprot.org/annotation/VSP_059413|||http://purl.uniprot.org/annotation/VSP_059414|||http://purl.uniprot.org/annotation/VSP_059415|||http://purl.uniprot.org/annotation/VSP_059416|||http://purl.uniprot.org/annotation/VSP_059417
http://togogenome.org/gene/9606:PHF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X169|||http://purl.uniprot.org/uniprot/B7Z887|||http://purl.uniprot.org/uniprot/B7Z8H3|||http://purl.uniprot.org/uniprot/F5H8K3|||http://purl.uniprot.org/uniprot/Q5T6S3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and RIOX1; when associated with A-56.|||Abolishes histone H3K36me3-binding. Abolishes histone H3K36me3-binding and recruitment of the PRC2 complex and RIOX1; when associated with C-50.|||Disordered|||Histone H3K36me3 binding|||Impairs chromatin binding as part of the PRC2 complex.|||Important for PRC2 dimer stability|||In isoform 2.|||In isoform 3.|||In muthPhf19; abolishes histone H3K36me3-binding and impaired activity of the PRC2 complex and subsequent H3K27me3 methylation.|||Interaction with SUZ12|||PHD finger protein 19|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polycomb-like MTF2 factor 2 C-terminal|||Tudor|||Zinc finger PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318570|||http://purl.uniprot.org/annotation/VSP_031222|||http://purl.uniprot.org/annotation/VSP_031223|||http://purl.uniprot.org/annotation/VSP_031224|||http://purl.uniprot.org/annotation/VSP_031225
http://togogenome.org/gene/9606:ZNF623                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75123                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Zinc finger protein 623                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047694|||http://purl.uniprot.org/annotation/VAR_052881|||http://purl.uniprot.org/annotation/VSP_053501
http://togogenome.org/gene/9606:H2AC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FTV9|||http://purl.uniprot.org/uniprot/P0C0S8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055235
http://togogenome.org/gene/9606:DCAF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQT4|||http://purl.uniprot.org/uniprot/Q5QP82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 10|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306833|||http://purl.uniprot.org/annotation/VSP_028513
http://togogenome.org/gene/9606:VDAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21796                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ceramide and phosphatidylcholine binding.|||Beta stranded|||Conformation remains closed and prevents cytochrome c leakage.|||Conformation remains open and constitutively allows cytochrome c efflux.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating|||Loss of PRKN-dependent monoubiquitination increases mitochondria calcium uptake, and ultimately increased apoptosis. Consequently, mitochondria are swelled with defective cristae structures. PRKN-dependent polyubiquitination is unaffected.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-20 and 109-R-R-110.|||PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-20 and R-53.|||PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-12; R-53 and 109-R-R-110.|||PRKN-dependent polybiquitination is decreased, whereas PRKN-dependent monoubiquitination, mitochondrial calcium uptake and apoptosis are unaffected; when associated with R-20; R-53 and 109-R-R-110.|||Phosphoserine|||Phosphoserine; by NEK1|||Phosphothreonine|||Phosphotyrosine|||Removed|||Voltage-dependent anion-selective channel protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050499
http://togogenome.org/gene/9606:CSRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5K2|||http://purl.uniprot.org/uniprot/B4DY28|||http://purl.uniprot.org/uniprot/P21291                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine and glycine-rich protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075715|||http://purl.uniprot.org/annotation/VAR_050144
http://togogenome.org/gene/9606:ECM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94769                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cell attachment site|||Disordered|||Extracellular matrix protein 2|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032731|||http://purl.uniprot.org/annotation/VAR_024646|||http://purl.uniprot.org/annotation/VAR_052010|||http://purl.uniprot.org/annotation/VAR_052011|||http://purl.uniprot.org/annotation/VSP_039114|||http://purl.uniprot.org/annotation/VSP_039115
http://togogenome.org/gene/9606:C4orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1A6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  UPF0462 protein C4orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295714|||http://purl.uniprot.org/annotation/VAR_033334|||http://purl.uniprot.org/annotation/VAR_033335|||http://purl.uniprot.org/annotation/VAR_033336|||http://purl.uniprot.org/annotation/VAR_033337
http://togogenome.org/gene/9606:NTM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P121                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neurotrimin|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015110|||http://purl.uniprot.org/annotation/PRO_0000015111|||http://purl.uniprot.org/annotation/VSP_010939|||http://purl.uniprot.org/annotation/VSP_010940|||http://purl.uniprot.org/annotation/VSP_010941|||http://purl.uniprot.org/annotation/VSP_041165
http://togogenome.org/gene/9606:IP6K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92551                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Inositol hexakisphosphate kinase 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066874|||http://purl.uniprot.org/annotation/VSP_042756
http://togogenome.org/gene/9606:ELN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRT8|||http://purl.uniprot.org/uniprot/B4E3S4|||http://purl.uniprot.org/uniprot/E7EN65|||http://purl.uniprot.org/uniprot/E7ENM0|||http://purl.uniprot.org/uniprot/G3V0G6|||http://purl.uniprot.org/uniprot/G5E950|||http://purl.uniprot.org/uniprot/P15502|||http://purl.uniprot.org/uniprot/Q59H17|||http://purl.uniprot.org/uniprot/Q6ZUN2|||http://purl.uniprot.org/uniprot/Q8NBI4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  4-hydroxyproline|||4-hydroxyproline; partial|||Allysine|||Disordered|||Elastin|||Found as homozygous mutation in a patient with autosomal recessive cutis laxa also carrying a mutation in FBLN5; unknown pathological significance.|||Hydroxyproline|||Hydroxyproline; partial|||In isoform 1, isoform 2, isoform 4 and isoform 5.|||In isoform 1, isoform 2, isoform 5, isoform 6, isoform 7, isoform 8, isoform 10, isoform 11, isoform 12 and isoform 13.|||In isoform 1, isoform 9 and isoform 10.|||In isoform 11.|||In isoform 5 and isoform 12.|||In isoform 5, isoform 6, isoform 7, isoform 8, isoform 11 and isoform 12.|||In isoform 6, isoform 7, isoform 8, isoform 11, isoform 12 and isoform 13.|||In isoform 7.|||In isoform 8 and isoform 11.|||In isoform 8.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021163|||http://purl.uniprot.org/annotation/PRO_5002801176|||http://purl.uniprot.org/annotation/PRO_5003217306|||http://purl.uniprot.org/annotation/PRO_5003219423|||http://purl.uniprot.org/annotation/PRO_5004283926|||http://purl.uniprot.org/annotation/PRO_5004312895|||http://purl.uniprot.org/annotation/PRO_5014567665|||http://purl.uniprot.org/annotation/PRO_5014571900|||http://purl.uniprot.org/annotation/PRO_5015091584|||http://purl.uniprot.org/annotation/VAR_020882|||http://purl.uniprot.org/annotation/VAR_056869|||http://purl.uniprot.org/annotation/VAR_072395|||http://purl.uniprot.org/annotation/VSP_012479|||http://purl.uniprot.org/annotation/VSP_012480|||http://purl.uniprot.org/annotation/VSP_012481|||http://purl.uniprot.org/annotation/VSP_012482|||http://purl.uniprot.org/annotation/VSP_012483|||http://purl.uniprot.org/annotation/VSP_012484|||http://purl.uniprot.org/annotation/VSP_012485|||http://purl.uniprot.org/annotation/VSP_012486|||http://purl.uniprot.org/annotation/VSP_012487|||http://purl.uniprot.org/annotation/VSP_012488
http://togogenome.org/gene/9606:DNHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0I1S4|||http://purl.uniprot.org/uniprot/Q96M86                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Dynein heavy chain AAA 5 extension|||Dynein heavy chain AAA module D4|||Dynein heavy chain C-terminal|||Dynein heavy chain coiled coil stalk|||Dynein heavy chain domain-containing protein 1|||Dynein heavy chain hydrolytic ATP-binding dynein motor region|||Dynein heavy chain linker|||Dynein heavy chain region D6 P-loop|||In SPGF65.|||In SPGF65; low expression, if any, in sperm flagella.|||In SPGF65; unknown pathological significance.|||In SPGF65; unknown pathological significance; low expression, if any, in sperm flagella.|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311985|||http://purl.uniprot.org/annotation/VAR_033353|||http://purl.uniprot.org/annotation/VAR_033354|||http://purl.uniprot.org/annotation/VAR_033355|||http://purl.uniprot.org/annotation/VAR_037388|||http://purl.uniprot.org/annotation/VAR_037389|||http://purl.uniprot.org/annotation/VAR_039308|||http://purl.uniprot.org/annotation/VAR_039309|||http://purl.uniprot.org/annotation/VAR_039310|||http://purl.uniprot.org/annotation/VAR_039311|||http://purl.uniprot.org/annotation/VAR_056829|||http://purl.uniprot.org/annotation/VAR_056830|||http://purl.uniprot.org/annotation/VAR_086769|||http://purl.uniprot.org/annotation/VAR_086770|||http://purl.uniprot.org/annotation/VAR_086771|||http://purl.uniprot.org/annotation/VAR_086772|||http://purl.uniprot.org/annotation/VAR_086773|||http://purl.uniprot.org/annotation/VAR_086774|||http://purl.uniprot.org/annotation/VAR_086775|||http://purl.uniprot.org/annotation/VAR_086776|||http://purl.uniprot.org/annotation/VAR_086777|||http://purl.uniprot.org/annotation/VAR_086778|||http://purl.uniprot.org/annotation/VSP_040682|||http://purl.uniprot.org/annotation/VSP_040683|||http://purl.uniprot.org/annotation/VSP_040684
http://togogenome.org/gene/9606:NAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18440|||http://purl.uniprot.org/uniprot/Q400J6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Arylamine N-acetyltransferase 1|||In allele NAT1*11.|||In allele NAT1*11; catalyzes the N-acetylation of aromatic amines and the O- and N,O-acetylation of their N-hydroxylated metabolites at rates up to 2-fold higher.|||In allele NAT1*14; a slow acetylator.|||In allele NAT1*17; a slow acetylator; has defective enzyme activity.|||In allele NAT1*21.|||In allele NAT1*22.|||In allele NAT1*24.|||In allele NAT1*25.|||In allele NAT1*5.|||N-acetylmethionine|||Reduced enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107904|||http://purl.uniprot.org/annotation/VAR_004606|||http://purl.uniprot.org/annotation/VAR_004607|||http://purl.uniprot.org/annotation/VAR_009069|||http://purl.uniprot.org/annotation/VAR_009070|||http://purl.uniprot.org/annotation/VAR_009071|||http://purl.uniprot.org/annotation/VAR_009072|||http://purl.uniprot.org/annotation/VAR_009073|||http://purl.uniprot.org/annotation/VAR_009074|||http://purl.uniprot.org/annotation/VAR_009510|||http://purl.uniprot.org/annotation/VAR_009511|||http://purl.uniprot.org/annotation/VAR_020384
http://togogenome.org/gene/9606:TOR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPA1|||http://purl.uniprot.org/uniprot/O14656                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Found in a patient with early-onset atypical dystonia and myoclonic features; unknown pathological significance.|||In AMC5.|||In AMC5; increased localization to the nuclear membrane; induces the formation of spheroid bodies in cells.|||In DYT1 and AMC5; acts as a dominant negative; increased identical protein binding; loss of interaction with TOR1AIP1 and TOR1AIP2 with loss of ATPase activity induction; increased localization to the nuclear membrane; decreased ATP-dependent chaperone mediated protein folding; changed nuclear membrane organization.|||In DYT1; increased identical protein binding; decreased ATP-dependent chaperone mediated protein folding; changed nuclear membrane organization.|||In DYT1; increased identical protein binding; decreased ATP-dependent chaperone mediated protein folding; changed nuclear membrane organization; decreased neuron projection development.|||In isoform 2.|||Inhibits sequence signal cleavage.|||Interaction with KLC1|||Interaction with SNAPIN|||Interaction with SYNE3|||Loss of ATP hydrolysis. Loss of interaction with KLHL14. Localizes in the nuclear envelope. No effect on interaction with TOR1AIP1.|||Loss of ATP-binding. No effect on interaction with KLHL14. Increases interaction with TOR1AIP1 and TOR1AIP2. Abolishes interaction with SLC6A3.|||N-glycosylated.|||N-linked (GlcNAc...) (high mannose) asparagine|||Reduces N-glycosylation.|||Torsin-1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005506|||http://purl.uniprot.org/annotation/PRO_5002790276|||http://purl.uniprot.org/annotation/VAR_010788|||http://purl.uniprot.org/annotation/VAR_010789|||http://purl.uniprot.org/annotation/VAR_020449|||http://purl.uniprot.org/annotation/VAR_070932|||http://purl.uniprot.org/annotation/VAR_070933|||http://purl.uniprot.org/annotation/VAR_070934|||http://purl.uniprot.org/annotation/VAR_084705|||http://purl.uniprot.org/annotation/VAR_084706|||http://purl.uniprot.org/annotation/VSP_026605
http://togogenome.org/gene/9606:HAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P81172                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Mass|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Hepcidin-20|||Hepcidin-25|||In HFE2B.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013378|||http://purl.uniprot.org/annotation/PRO_0000013379|||http://purl.uniprot.org/annotation/PRO_0000013380|||http://purl.uniprot.org/annotation/VAR_026648|||http://purl.uniprot.org/annotation/VAR_042512|||http://purl.uniprot.org/annotation/VAR_042513|||http://purl.uniprot.org/annotation/VAR_042514
http://togogenome.org/gene/9606:ZNF221                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK13                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 221                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047462|||http://purl.uniprot.org/annotation/VAR_024201|||http://purl.uniprot.org/annotation/VAR_024202|||http://purl.uniprot.org/annotation/VAR_024203|||http://purl.uniprot.org/annotation/VAR_033557|||http://purl.uniprot.org/annotation/VAR_033558|||http://purl.uniprot.org/annotation/VAR_033559
http://togogenome.org/gene/9606:PBRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BAH 1|||BAH 2|||Basic and acidic residues|||Bromo 1|||Bromo 2|||Bromo 3|||Bromo 4|||Bromo 5|||Bromo 6|||Disordered|||Found in a bladder cancer cell line.|||Found in a brain cancer cell line.|||Found in a breast cancer cell line.|||Found in a case of clear cell renal carcinoma; somatic mutation.|||Found in a colon cancer cell line.|||Found in a endometrial cancer cell line.|||Found in a kidney cancer cell line.|||Found in a lung cancer cell line.|||Found in a malignant melanoma cell line.|||Found in a renal carcinoma cell line.|||Found in a stomach cancer cell line.|||Found in an endometrial cancer cell line.|||Found in an ovary carcinoma cell line.|||Found in hematopoietic and lymphoid cancer cell lines.|||Found in hematopoietic, lymphoid, lung and liver cancer cell lines.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HMG box|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 9.|||In isoform 3.|||In isoform 4 and isoform 9.|||In isoform 4.|||In isoform 5, isoform 7 and isoform 8.|||In isoform 6.|||In isoform 7 and isoform 8.|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Protein polybromo-1|||Requires 2 nucleotide substitutions; found in a colon cancer cell line.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211207|||http://purl.uniprot.org/annotation/VAR_064653|||http://purl.uniprot.org/annotation/VAR_064654|||http://purl.uniprot.org/annotation/VAR_064655|||http://purl.uniprot.org/annotation/VAR_064656|||http://purl.uniprot.org/annotation/VAR_064657|||http://purl.uniprot.org/annotation/VAR_064658|||http://purl.uniprot.org/annotation/VAR_064659|||http://purl.uniprot.org/annotation/VAR_064660|||http://purl.uniprot.org/annotation/VAR_064661|||http://purl.uniprot.org/annotation/VAR_064662|||http://purl.uniprot.org/annotation/VAR_064663|||http://purl.uniprot.org/annotation/VAR_064664|||http://purl.uniprot.org/annotation/VAR_064665|||http://purl.uniprot.org/annotation/VAR_064666|||http://purl.uniprot.org/annotation/VAR_064667|||http://purl.uniprot.org/annotation/VAR_064668|||http://purl.uniprot.org/annotation/VAR_064669|||http://purl.uniprot.org/annotation/VAR_064670|||http://purl.uniprot.org/annotation/VAR_064671|||http://purl.uniprot.org/annotation/VAR_064672|||http://purl.uniprot.org/annotation/VAR_064673|||http://purl.uniprot.org/annotation/VAR_064674|||http://purl.uniprot.org/annotation/VAR_064675|||http://purl.uniprot.org/annotation/VAR_064676|||http://purl.uniprot.org/annotation/VAR_064677|||http://purl.uniprot.org/annotation/VAR_064678|||http://purl.uniprot.org/annotation/VAR_064679|||http://purl.uniprot.org/annotation/VAR_064680|||http://purl.uniprot.org/annotation/VAR_064681|||http://purl.uniprot.org/annotation/VAR_064682|||http://purl.uniprot.org/annotation/VAR_064683|||http://purl.uniprot.org/annotation/VAR_064684|||http://purl.uniprot.org/annotation/VAR_064685|||http://purl.uniprot.org/annotation/VAR_064686|||http://purl.uniprot.org/annotation/VAR_064687|||http://purl.uniprot.org/annotation/VAR_064688|||http://purl.uniprot.org/annotation/VAR_064689|||http://purl.uniprot.org/annotation/VAR_064690|||http://purl.uniprot.org/annotation/VSP_015231|||http://purl.uniprot.org/annotation/VSP_015232|||http://purl.uniprot.org/annotation/VSP_015233|||http://purl.uniprot.org/annotation/VSP_015234|||http://purl.uniprot.org/annotation/VSP_015235|||http://purl.uniprot.org/annotation/VSP_015236|||http://purl.uniprot.org/annotation/VSP_035499
http://togogenome.org/gene/9606:ACBD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6N7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Turn                                                                                  ^@                                                                                  ACB|||Acyl-CoA-binding domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247588
http://togogenome.org/gene/9606:HMGCLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z212|||http://purl.uniprot.org/uniprot/O95896|||http://purl.uniprot.org/uniprot/Q8TB92|||http://purl.uniprot.org/uniprot/Q9NT06                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic|||Abolishes catalytic activity.|||Abolishes myristoylation and induces a subcellular location change.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||Pyruvate carboxyltransferase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334669|||http://purl.uniprot.org/annotation/VSP_033752|||http://purl.uniprot.org/annotation/VSP_038021|||http://purl.uniprot.org/annotation/VSP_038022|||http://purl.uniprot.org/annotation/VSP_044324
http://togogenome.org/gene/9606:EDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5J797|||http://purl.uniprot.org/uniprot/Q92838                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes proteolytic processing.|||Basic and acidic residues|||Cleavage; by furin|||Collagen-like|||Cytoplasmic|||Disordered|||Ectodysplasin-A, membrane form|||Ectodysplasin-A, secreted form|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In STHAGX1 and XHED.|||In STHAGX1.|||In STHAGX1; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling.|||In XHED.|||In XHED; abolishes proteolytic processing.|||In XHED; decreased interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling.|||In XHED; loss of function in EDAR-mediated signaling; not secreted.|||In XHED; loss of interaction with EDAR for isoform 1; decreased interaction with EDA2R for isoform 3; changed downstream signaling.|||In XHED; mild.|||In XHED; unknown pathological significance.|||In XHED; when associated in cis with C-290; loss of function in EDAR-mediated signaling when associated in cis with C-290; not secreted when associated in cis with C-290.|||In XHED; when associated in cis with P-289; loss of function in EDAR-mediated signaling when associated in cis with P-289; not secreted when associated in cis with P-289.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 8.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||TNF family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034538|||http://purl.uniprot.org/annotation/PRO_0000034539|||http://purl.uniprot.org/annotation/VAR_005179|||http://purl.uniprot.org/annotation/VAR_005180|||http://purl.uniprot.org/annotation/VAR_005181|||http://purl.uniprot.org/annotation/VAR_005182|||http://purl.uniprot.org/annotation/VAR_005183|||http://purl.uniprot.org/annotation/VAR_005184|||http://purl.uniprot.org/annotation/VAR_005185|||http://purl.uniprot.org/annotation/VAR_005186|||http://purl.uniprot.org/annotation/VAR_005187|||http://purl.uniprot.org/annotation/VAR_005188|||http://purl.uniprot.org/annotation/VAR_005189|||http://purl.uniprot.org/annotation/VAR_005190|||http://purl.uniprot.org/annotation/VAR_005191|||http://purl.uniprot.org/annotation/VAR_010611|||http://purl.uniprot.org/annotation/VAR_010612|||http://purl.uniprot.org/annotation/VAR_010613|||http://purl.uniprot.org/annotation/VAR_010614|||http://purl.uniprot.org/annotation/VAR_010615|||http://purl.uniprot.org/annotation/VAR_011077|||http://purl.uniprot.org/annotation/VAR_011078|||http://purl.uniprot.org/annotation/VAR_011079|||http://purl.uniprot.org/annotation/VAR_011080|||http://purl.uniprot.org/annotation/VAR_013484|||http://purl.uniprot.org/annotation/VAR_013485|||http://purl.uniprot.org/annotation/VAR_013486|||http://purl.uniprot.org/annotation/VAR_013487|||http://purl.uniprot.org/annotation/VAR_013488|||http://purl.uniprot.org/annotation/VAR_029534|||http://purl.uniprot.org/annotation/VAR_036590|||http://purl.uniprot.org/annotation/VAR_054454|||http://purl.uniprot.org/annotation/VAR_054455|||http://purl.uniprot.org/annotation/VAR_054456|||http://purl.uniprot.org/annotation/VAR_054457|||http://purl.uniprot.org/annotation/VAR_054458|||http://purl.uniprot.org/annotation/VAR_054459|||http://purl.uniprot.org/annotation/VAR_054460|||http://purl.uniprot.org/annotation/VAR_054461|||http://purl.uniprot.org/annotation/VAR_054462|||http://purl.uniprot.org/annotation/VAR_054463|||http://purl.uniprot.org/annotation/VAR_054464|||http://purl.uniprot.org/annotation/VAR_054465|||http://purl.uniprot.org/annotation/VAR_054466|||http://purl.uniprot.org/annotation/VAR_054467|||http://purl.uniprot.org/annotation/VAR_054468|||http://purl.uniprot.org/annotation/VAR_054469|||http://purl.uniprot.org/annotation/VAR_054470|||http://purl.uniprot.org/annotation/VAR_054471|||http://purl.uniprot.org/annotation/VAR_054472|||http://purl.uniprot.org/annotation/VAR_054473|||http://purl.uniprot.org/annotation/VAR_054474|||http://purl.uniprot.org/annotation/VAR_054475|||http://purl.uniprot.org/annotation/VAR_054476|||http://purl.uniprot.org/annotation/VAR_064858|||http://purl.uniprot.org/annotation/VAR_064859|||http://purl.uniprot.org/annotation/VAR_064860|||http://purl.uniprot.org/annotation/VAR_064861|||http://purl.uniprot.org/annotation/VAR_064862|||http://purl.uniprot.org/annotation/VAR_064863|||http://purl.uniprot.org/annotation/VAR_064864|||http://purl.uniprot.org/annotation/VAR_064865|||http://purl.uniprot.org/annotation/VAR_064866|||http://purl.uniprot.org/annotation/VAR_064867|||http://purl.uniprot.org/annotation/VAR_064868|||http://purl.uniprot.org/annotation/VAR_064869|||http://purl.uniprot.org/annotation/VAR_064870|||http://purl.uniprot.org/annotation/VAR_064871|||http://purl.uniprot.org/annotation/VAR_067250|||http://purl.uniprot.org/annotation/VAR_067319|||http://purl.uniprot.org/annotation/VAR_071454|||http://purl.uniprot.org/annotation/VAR_071455|||http://purl.uniprot.org/annotation/VAR_071456|||http://purl.uniprot.org/annotation/VAR_071457|||http://purl.uniprot.org/annotation/VAR_071458|||http://purl.uniprot.org/annotation/VAR_071459|||http://purl.uniprot.org/annotation/VAR_075310|||http://purl.uniprot.org/annotation/VAR_075311|||http://purl.uniprot.org/annotation/VAR_075312|||http://purl.uniprot.org/annotation/VAR_075313|||http://purl.uniprot.org/annotation/VAR_075314|||http://purl.uniprot.org/annotation/VAR_075315|||http://purl.uniprot.org/annotation/VAR_075316|||http://purl.uniprot.org/annotation/VAR_075317|||http://purl.uniprot.org/annotation/VAR_075318|||http://purl.uniprot.org/annotation/VAR_075319|||http://purl.uniprot.org/annotation/VAR_075320|||http://purl.uniprot.org/annotation/VAR_075321|||http://purl.uniprot.org/annotation/VAR_077561|||http://purl.uniprot.org/annotation/VAR_085684|||http://purl.uniprot.org/annotation/VAR_085685|||http://purl.uniprot.org/annotation/VAR_085686|||http://purl.uniprot.org/annotation/VSP_006454|||http://purl.uniprot.org/annotation/VSP_006455|||http://purl.uniprot.org/annotation/VSP_006456|||http://purl.uniprot.org/annotation/VSP_006457|||http://purl.uniprot.org/annotation/VSP_006458|||http://purl.uniprot.org/annotation/VSP_006459|||http://purl.uniprot.org/annotation/VSP_006460|||http://purl.uniprot.org/annotation/VSP_006461|||http://purl.uniprot.org/annotation/VSP_006464|||http://purl.uniprot.org/annotation/VSP_038402
http://togogenome.org/gene/9606:VEZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QSH4|||http://purl.uniprot.org/uniprot/Q14119                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 7 AA repeats of P-[LV]-T-[IL]-T-[ST]-P|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||In CMD1OO; loss of DNA-binding transcription activator activity, RNA polymerase II-specific.|||N6-acetyllysine|||Polar residues|||Vascular endothelial zinc finger 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047435|||http://purl.uniprot.org/annotation/VAR_088235
http://togogenome.org/gene/9606:EPS8L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2J6|||http://purl.uniprot.org/uniprot/Q8TE67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Epidermal growth factor receptor kinase substrate 8-like protein 3|||In HYPT5; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||PTB|||Phosphoserine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239087|||http://purl.uniprot.org/annotation/VAR_026580|||http://purl.uniprot.org/annotation/VAR_026581|||http://purl.uniprot.org/annotation/VAR_026582|||http://purl.uniprot.org/annotation/VAR_050976|||http://purl.uniprot.org/annotation/VAR_050977|||http://purl.uniprot.org/annotation/VAR_083829|||http://purl.uniprot.org/annotation/VSP_019095|||http://purl.uniprot.org/annotation/VSP_019096
http://togogenome.org/gene/9606:LSR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X29                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with familial intrahepatic cholestasis; unknown pathological significance.|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Lipolysis-stimulated lipoprotein receptor|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245308|||http://purl.uniprot.org/annotation/VAR_049902|||http://purl.uniprot.org/annotation/VAR_086706|||http://purl.uniprot.org/annotation/VSP_019691|||http://purl.uniprot.org/annotation/VSP_019692|||http://purl.uniprot.org/annotation/VSP_019693|||http://purl.uniprot.org/annotation/VSP_019694|||http://purl.uniprot.org/annotation/VSP_046797|||http://purl.uniprot.org/annotation/VSP_057210|||http://purl.uniprot.org/annotation/VSP_057211
http://togogenome.org/gene/9606:GET3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43681                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ATPase GET3|||Abolishes ATPase activity, dominantly inhibits the TA protein insertion pathway.|||In CMD2H; contrary to the wild type, the mutant is unable to rescue cardiac failure in zebrafish lacking GET3; results in decreased function in tail-anchored membrane protein insertion into ER membrane; has no effect on thermal stability.|||In CMD2H; when associated in cis with 305-Q--Q-348 del.|||In CMD2H; when associated in cis with variant W-289.|||N-acetylalanine|||Reduces TA protein insertion pathway.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152253|||http://purl.uniprot.org/annotation/VAR_018844|||http://purl.uniprot.org/annotation/VAR_088104|||http://purl.uniprot.org/annotation/VAR_088105|||http://purl.uniprot.org/annotation/VAR_088106
http://togogenome.org/gene/9606:PWP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJV5|||http://purl.uniprot.org/uniprot/Q13610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Periodic tryptophan protein 1 homolog|||Phosphoserine|||Phosphothreonine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051171|||http://purl.uniprot.org/annotation/VAR_033808|||http://purl.uniprot.org/annotation/VSP_056168|||http://purl.uniprot.org/annotation/VSP_056169
http://togogenome.org/gene/9606:RAB29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14966|||http://purl.uniprot.org/uniprot/Q6FGU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by S.Typhimurium viral protease GtgE|||Effector region|||In isoform 2.|||In isoform 3.|||Loss of LRRK2 binding. Does not stimulate LRRK2 kinase activity. Localized to the cytosol.|||Loss of phosphorylation by LRRK2.|||Loss of phosphorylation by LRRK2. Does not stimulate LRRK2 kinase activity; when associated with E-71.|||Loss of phosphorylation by LRRK2. Does not stimulate LRRK2 kinase activity; when associated with E-72.|||Phosphoserine; by LRRK2|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-7L1|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121127|||http://purl.uniprot.org/annotation/VSP_043391|||http://purl.uniprot.org/annotation/VSP_045078
http://togogenome.org/gene/9606:AGO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1P5|||http://purl.uniprot.org/uniprot/Q9H9G7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interaction with guide RNA|||Loss of RNA slicer activity.|||N-acetylmethionine|||PAZ|||Phosphoserine|||Piwi|||Protein argonaute-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194061|||http://purl.uniprot.org/annotation/VSP_041084
http://togogenome.org/gene/9606:ZC3H11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75152                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger CCCH domain-containing protein 11A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213905|||http://purl.uniprot.org/annotation/VAR_052967
http://togogenome.org/gene/9606:NUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BM14|||http://purl.uniprot.org/uniprot/H3BM74|||http://purl.uniprot.org/uniprot/Q9Y5A7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||NEDD8 ultimate buster 1|||NEDD8-binding 1|||NEDD8-binding 2|||No effect on NEDD8-binding.|||Nuclear localization signal|||Partial inhibition of NEDD8-binding.|||Polar residues|||Suppression of NEDD8-binding; when associated with A-464; A-468 and A-587. Suppression of NEDD8-buster function; when associated with A-587.|||Suppression of NEDD8-binding; when associated with A-464; A-468 and A-591. Suppression of NEDD8-buster function; when associated with A-591.|||UBA|||UBA 1|||UBA 2|||UBA 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210992|||http://purl.uniprot.org/annotation/VAR_057369|||http://purl.uniprot.org/annotation/VSP_008335
http://togogenome.org/gene/9606:KCNMB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5BNW5|||http://purl.uniprot.org/uniprot/B7Z513|||http://purl.uniprot.org/uniprot/Q9Y691                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes inactivation of KCNMA1 channel.|||Ball and chain|||Calcium-activated potassium channel subunit beta-2|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||KCNMB2 ball/chain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187051
http://togogenome.org/gene/9606:MSS51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VC12                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||MYND-type|||Putative protein MSS51 homolog, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289109|||http://purl.uniprot.org/annotation/VAR_052993|||http://purl.uniprot.org/annotation/VSP_025898|||http://purl.uniprot.org/annotation/VSP_025899|||http://purl.uniprot.org/annotation/VSP_025900|||http://purl.uniprot.org/annotation/VSP_025901
http://togogenome.org/gene/9606:TMEM14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WU83|||http://purl.uniprot.org/uniprot/C9JCY4|||http://purl.uniprot.org/uniprot/C9JQS0|||http://purl.uniprot.org/uniprot/Q9NUH8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 14B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221172|||http://purl.uniprot.org/annotation/VSP_046899
http://togogenome.org/gene/9606:RPS6KB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBS0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKC|||Pro residues|||Protein kinase|||Proton acceptor|||Ribosomal protein S6 kinase beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086214|||http://purl.uniprot.org/annotation/VAR_040643|||http://purl.uniprot.org/annotation/VAR_040644|||http://purl.uniprot.org/annotation/VAR_040645|||http://purl.uniprot.org/annotation/VAR_040646|||http://purl.uniprot.org/annotation/VSP_056441|||http://purl.uniprot.org/annotation/VSP_056442
http://togogenome.org/gene/9606:FAM222A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U5X8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Protein FAM222A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274239
http://togogenome.org/gene/9606:FABP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0Z7S8                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand                                                                                  ^@                                                                                  Fatty acid-binding protein 9|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317292
http://togogenome.org/gene/9606:MATN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21941                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Cartilage matrix protein|||EGF-like|||N-linked (GlcNAc...) asparagine|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007495
http://togogenome.org/gene/9606:HMCES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FZ2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abasic site processing protein HMCES|||Abolished ability to bind DNA and abolished ability to promote class switch recombination (CSR) in B-cells.|||Abolished interaction with PCNA. Cells are hypersensitive to ionizing radiations.|||Basic and acidic residues|||Cells are hypersensitive to ionizing radiations. Abolished ability to form a covalent cross-link with DNA. Abolished binding to single-stranded DNA (ssDNA).|||Cells are hypersensitive to ionizing radiations. Abolished ability to form a covalent cross-link with DNA. Does not affect single-stranded DNA (ssDNA)-binding. Does not affect ability to promote class switch recombination (CSR) in B-cells.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleophile|||PIP-box|||Phosphoserine|||Polar residues|||Removed|||Required for sensing abasic sites|||Required to stabilize abasic sites|||Strongly reduced binding to single-stranded DNA.|||Thiazolidine linkage to a ring-opened DNA abasic site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164394
http://togogenome.org/gene/9606:DIS3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF46                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Complete loss of exonuclease activity.|||DIS3-like exonuclease 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No change of exonuclease activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314810|||http://purl.uniprot.org/annotation/VAR_038056|||http://purl.uniprot.org/annotation/VAR_038057|||http://purl.uniprot.org/annotation/VAR_038058|||http://purl.uniprot.org/annotation/VSP_030366|||http://purl.uniprot.org/annotation/VSP_030367|||http://purl.uniprot.org/annotation/VSP_030368|||http://purl.uniprot.org/annotation/VSP_030369
http://togogenome.org/gene/9606:EPHA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0R4|||http://purl.uniprot.org/uniprot/Q5JZY3|||http://purl.uniprot.org/uniprot/Q8N289                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-A receptor 10|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protein kinase|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042157|||http://purl.uniprot.org/annotation/PRO_5004314210|||http://purl.uniprot.org/annotation/VAR_042159|||http://purl.uniprot.org/annotation/VAR_042160|||http://purl.uniprot.org/annotation/VAR_042161|||http://purl.uniprot.org/annotation/VAR_042162|||http://purl.uniprot.org/annotation/VAR_042163|||http://purl.uniprot.org/annotation/VAR_042164|||http://purl.uniprot.org/annotation/VAR_055992|||http://purl.uniprot.org/annotation/VAR_055993|||http://purl.uniprot.org/annotation/VAR_055994|||http://purl.uniprot.org/annotation/VAR_055995|||http://purl.uniprot.org/annotation/VAR_055996|||http://purl.uniprot.org/annotation/VSP_015772|||http://purl.uniprot.org/annotation/VSP_015773|||http://purl.uniprot.org/annotation/VSP_015774|||http://purl.uniprot.org/annotation/VSP_015775
http://togogenome.org/gene/9606:PCDHB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5E5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003920|||http://purl.uniprot.org/annotation/VAR_021878|||http://purl.uniprot.org/annotation/VAR_048548|||http://purl.uniprot.org/annotation/VAR_048549|||http://purl.uniprot.org/annotation/VAR_048550|||http://purl.uniprot.org/annotation/VAR_048551
http://togogenome.org/gene/9606:PI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19957                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  2 X tandem repeats of SVP-1 like motif|||Elafin|||SVP-1 clotting 1|||SVP-1 clotting 2|||WAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041357|||http://purl.uniprot.org/annotation/PRO_0000041358|||http://purl.uniprot.org/annotation/VAR_024695|||http://purl.uniprot.org/annotation/VAR_052947
http://togogenome.org/gene/9606:LTBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EG76|||http://purl.uniprot.org/uniprot/Q8WYU6|||http://purl.uniprot.org/uniprot/Q9NS15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In GPHYSD3; unknown pathological significance; no effect on TGF-beta secretion.|||In isoform 2.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||TB|||TB 1|||TB 2|||TB 3|||TB 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007646|||http://purl.uniprot.org/annotation/VAR_080565|||http://purl.uniprot.org/annotation/VSP_009241
http://togogenome.org/gene/9606:GFRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z856|||http://purl.uniprot.org/uniprot/P56159                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||GDNF family receptor alpha-1|||GDNF/GAS1|||GPI-anchor amidated serine|||In RHDA4.|||In isoform 2.|||May be involved in congenital central hypoventilation syndrome.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010777|||http://purl.uniprot.org/annotation/PRO_0000010778|||http://purl.uniprot.org/annotation/VAR_012488|||http://purl.uniprot.org/annotation/VAR_012489|||http://purl.uniprot.org/annotation/VAR_018261|||http://purl.uniprot.org/annotation/VAR_087454|||http://purl.uniprot.org/annotation/VAR_087455|||http://purl.uniprot.org/annotation/VSP_001660
http://togogenome.org/gene/9606:NPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG41                                                                                  ^@                                                                                  Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Neuropeptide B-23|||Neuropeptide B-29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019836|||http://purl.uniprot.org/annotation/PRO_0000019837|||http://purl.uniprot.org/annotation/PRO_0000019838
http://togogenome.org/gene/9606:KCNK16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T55                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform b.|||In isoform c.|||In isoform d.|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101767|||http://purl.uniprot.org/annotation/VAR_052430|||http://purl.uniprot.org/annotation/VAR_063636|||http://purl.uniprot.org/annotation/VAR_063637|||http://purl.uniprot.org/annotation/VSP_039863|||http://purl.uniprot.org/annotation/VSP_039864|||http://purl.uniprot.org/annotation/VSP_039865
http://togogenome.org/gene/9606:SLC27A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2P5                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Long-chain fatty acid transport protein 5|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193213|||http://purl.uniprot.org/annotation/VAR_048243|||http://purl.uniprot.org/annotation/VAR_048244|||http://purl.uniprot.org/annotation/VSP_055810
http://togogenome.org/gene/9606:PLCZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR9|||http://purl.uniprot.org/uniprot/Q86YW0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1|||C2|||Disordered|||EF-hand|||In SPGF17; loss of function in egg activation.|||In isoform 2.|||In isoform 3.|||PI-PLC X-box|||PI-PLC Y-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347244|||http://purl.uniprot.org/annotation/VAR_050542|||http://purl.uniprot.org/annotation/VAR_077876|||http://purl.uniprot.org/annotation/VSP_035076|||http://purl.uniprot.org/annotation/VSP_052862
http://togogenome.org/gene/9606:SYNJ2BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57105                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Mitochondrial intermembrane|||PDZ|||Synaptojanin-2-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072383|||http://purl.uniprot.org/annotation/VAR_051394
http://togogenome.org/gene/9606:PSD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRC4|||http://purl.uniprot.org/uniprot/Q9NYI0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||PH and SEC7 domain-containing protein 3|||Phosphoserine|||Polar residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120205|||http://purl.uniprot.org/annotation/VAR_036947|||http://purl.uniprot.org/annotation/VAR_036948|||http://purl.uniprot.org/annotation/VAR_036949|||http://purl.uniprot.org/annotation/VSP_023029|||http://purl.uniprot.org/annotation/VSP_029155|||http://purl.uniprot.org/annotation/VSP_029156
http://togogenome.org/gene/9606:TSG101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99816                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CEP55 and midbody localization; no effect on interaction with ESCRT-I proteins, PDCD6IP and viral proteins.|||Abolishes interaction with CEP55.|||Disordered|||In isoform 2.|||Interaction with CEP55|||Loss of interaction with VPS28. No effect on interaction with VPS37C.|||N-acetylalanine|||No change in interaction with p6; no effect on HIV-1 budding.|||PTAP motif|||Phosphothreonine|||Polar residues|||Reduces interaction with HIV-1 p6.|||Reduces interaction with HIV-1 p6; impairs HIV-1 budding.|||Reduces interaction with VPS37B and HIV-1 p6; abolishes interaction with PDCD6IP; impairs HIV-1 budding; inhibits down-regulation of EGFR. Abolishes MGRN1-binding. Loss of interaction with ARRDC1.|||Reduces interaction with ubiquitin.|||Reduces interaction with ubiquitin. No effect on MGRN1-binding.|||Reduces interaction with ubiquitin; inhibits down-regulation of EGFR.|||Reduces interaction with ubiquitin; no effect on in interaction with HIV-1 p6.|||Removed|||SB|||Tumor susceptibility gene 101 protein|||UEV                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082606|||http://purl.uniprot.org/annotation/VAR_034572|||http://purl.uniprot.org/annotation/VSP_004440
http://togogenome.org/gene/9606:EMX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04743                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein EMX2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048868|||http://purl.uniprot.org/annotation/VSP_045823
http://togogenome.org/gene/9606:ZNF606                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFC8|||http://purl.uniprot.org/uniprot/Q8WXB4|||http://purl.uniprot.org/uniprot/Q9H7U2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 606                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047688|||http://purl.uniprot.org/annotation/VAR_052872
http://togogenome.org/gene/9606:CARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPV7|||http://purl.uniprot.org/uniprot/P49589                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Basic and acidic residues|||Cysteine--tRNA ligase, cytoplasmic|||Disordered|||In MDBH; 50% reduction of cysteine-tRNA ligase activity.|||In MDBH; 84% reduction of cysteine-tRNA ligase activity.|||In MDBH; loss-of-function variant unable to rescue viability defects in a yeast complementation assay.|||In MDBH; undetectable mutant protein in patient cells; loss-of-function variant unable to rescue viability defects in a yeast complementation assay.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Removed|||tRNA synthetases class I catalytic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159550|||http://purl.uniprot.org/annotation/VAR_084305|||http://purl.uniprot.org/annotation/VAR_084306|||http://purl.uniprot.org/annotation/VAR_084307|||http://purl.uniprot.org/annotation/VAR_084308|||http://purl.uniprot.org/annotation/VSP_006312|||http://purl.uniprot.org/annotation/VSP_043571
http://togogenome.org/gene/9606:SRGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B7B5|||http://purl.uniprot.org/uniprot/B4DFE5|||http://purl.uniprot.org/uniprot/B7Z3G4|||http://purl.uniprot.org/uniprot/B7ZM87|||http://purl.uniprot.org/uniprot/O75044                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished RAC1 GTPase activity; when associated with A-566.|||Abolished RAC1 GTPase activity; when associated with L-527.|||Abolished interaction with ROBO1.|||Basic and acidic residues|||Decreased protein stability.|||Disordered|||Does not affect protein stability.|||F-BAR|||In F-BARx-R5E mutant; abolished binding to membranes; when associated with 234--E--E-238.|||In F-BARx-R5E mutant; abolished binding to membranes; when associated with 54-E-E-55.|||Increased interaction with ROBO1.|||Loss of the ability to stimulate cell migration, to localize at the plasma membrane protrusions and to dimerize.|||Phosphoserine|||Polar residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 2|||Symmetric dimethylarginine; by PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056767|||http://purl.uniprot.org/annotation/VAR_055834
http://togogenome.org/gene/9606:NCLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969V3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BOS complex subunit NCLN|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019687|||http://purl.uniprot.org/annotation/VAR_022552|||http://purl.uniprot.org/annotation/VAR_050276|||http://purl.uniprot.org/annotation/VSP_013851
http://togogenome.org/gene/9606:COQ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||N6-acetyllysine|||Ubiquinone biosynthesis O-methyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035926|||http://purl.uniprot.org/annotation/VAR_020789|||http://purl.uniprot.org/annotation/VAR_020790|||http://purl.uniprot.org/annotation/VAR_061925
http://togogenome.org/gene/9606:IFIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09914                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes PPP-RNA-binding.|||In isoform 2.|||Interaction with PPP-RNA|||Interaction with the 5'-triphosphate group of PPP-RNA|||Interferon-induced protein with tetratricopeptide repeats 1|||Reduced PPP-RNA-binding.|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106344|||http://purl.uniprot.org/annotation/VAR_052614|||http://purl.uniprot.org/annotation/VSP_054831
http://togogenome.org/gene/9606:HGH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BK8|||http://purl.uniprot.org/uniprot/Q9BTY7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Protein HGH1 C-terminal|||Protein HGH1 N-terminal|||Protein HGH1 homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273318
http://togogenome.org/gene/9606:YIPF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8F6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein YIPF7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333007|||http://purl.uniprot.org/annotation/VAR_043036|||http://purl.uniprot.org/annotation/VSP_033431|||http://purl.uniprot.org/annotation/VSP_033432|||http://purl.uniprot.org/annotation/VSP_033433|||http://purl.uniprot.org/annotation/VSP_033434|||http://purl.uniprot.org/annotation/VSP_033435
http://togogenome.org/gene/9606:GNG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1APZ0|||http://purl.uniprot.org/uniprot/P50150                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||G protein gamma|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012621|||http://purl.uniprot.org/annotation/PRO_0000012622
http://togogenome.org/gene/9606:IFNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C391|||http://purl.uniprot.org/uniprot/Q8IU54                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Interferon lambda-1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015511|||http://purl.uniprot.org/annotation/PRO_5036402069|||http://purl.uniprot.org/annotation/VAR_024506
http://togogenome.org/gene/9606:NFKBIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9C2|||http://purl.uniprot.org/uniprot/Q15653                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Disordered|||In isoform 2.|||NF-kappa-B inhibitor beta|||No degradation; when associated with A-19.|||No degradation; when associated with A-23.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by RPS6KA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067004|||http://purl.uniprot.org/annotation/VAR_020771|||http://purl.uniprot.org/annotation/VSP_012409|||http://purl.uniprot.org/annotation/VSP_012410
http://togogenome.org/gene/9606:ACSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTB9|||http://purl.uniprot.org/uniprot/E9PF16|||http://purl.uniprot.org/uniprot/Q96CM8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Medium-chain acyl-CoA ligase ACSF2, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315793|||http://purl.uniprot.org/annotation/VAR_038304|||http://purl.uniprot.org/annotation/VAR_038305|||http://purl.uniprot.org/annotation/VSP_055803|||http://purl.uniprot.org/annotation/VSP_055804|||http://purl.uniprot.org/annotation/VSP_055805
http://togogenome.org/gene/9606:GAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRB2-associated-binding protein 3|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318939|||http://purl.uniprot.org/annotation/VAR_038917|||http://purl.uniprot.org/annotation/VSP_045033|||http://purl.uniprot.org/annotation/VSP_055259
http://togogenome.org/gene/9606:IRX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78412                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Iroquois-class homeodomain protein IRX-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049162
http://togogenome.org/gene/9606:OR2AE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHA4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150471|||http://purl.uniprot.org/annotation/VAR_053138|||http://purl.uniprot.org/annotation/VAR_053139|||http://purl.uniprot.org/annotation/VAR_062019
http://togogenome.org/gene/9606:KRT32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14532                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha2|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063686|||http://purl.uniprot.org/annotation/VAR_056011|||http://purl.uniprot.org/annotation/VAR_056012|||http://purl.uniprot.org/annotation/VAR_056013|||http://purl.uniprot.org/annotation/VAR_056014|||http://purl.uniprot.org/annotation/VAR_056015|||http://purl.uniprot.org/annotation/VAR_056016|||http://purl.uniprot.org/annotation/VAR_060237|||http://purl.uniprot.org/annotation/VAR_060238|||http://purl.uniprot.org/annotation/VAR_060239|||http://purl.uniprot.org/annotation/VAR_060240|||http://purl.uniprot.org/annotation/VAR_069391
http://togogenome.org/gene/9606:SMIM19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E16                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264626
http://togogenome.org/gene/9606:NPVF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCQ7                                                                                  ^@                                                                                  Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Mass|||Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Neuropeptide NPSF|||Neuropeptide NPVF|||Neuropeptide RFRP-1|||Neuropeptide RFRP-2|||Phenylalanine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009920|||http://purl.uniprot.org/annotation/PRO_0000009921|||http://purl.uniprot.org/annotation/PRO_0000009922|||http://purl.uniprot.org/annotation/PRO_0000009923|||http://purl.uniprot.org/annotation/PRO_0000009924|||http://purl.uniprot.org/annotation/PRO_0000009925|||http://purl.uniprot.org/annotation/PRO_0000009926|||http://purl.uniprot.org/annotation/PRO_0000401171|||http://purl.uniprot.org/annotation/VAR_014073|||http://purl.uniprot.org/annotation/VAR_014074|||http://purl.uniprot.org/annotation/VAR_030644|||http://purl.uniprot.org/annotation/VSP_039962
http://togogenome.org/gene/9606:CKMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17540                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cardiolipin-binding|||Creatine kinase S-type, mitochondrial|||Mitochondrion|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016594
http://togogenome.org/gene/9606:ADPGK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRR6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ADP-dependent glucokinase|||ADPK|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184776|||http://purl.uniprot.org/annotation/VAR_060085|||http://purl.uniprot.org/annotation/VSP_013548|||http://purl.uniprot.org/annotation/VSP_013549|||http://purl.uniprot.org/annotation/VSP_013550|||http://purl.uniprot.org/annotation/VSP_013551|||http://purl.uniprot.org/annotation/VSP_013552|||http://purl.uniprot.org/annotation/VSP_013553|||http://purl.uniprot.org/annotation/VSP_013554|||http://purl.uniprot.org/annotation/VSP_035014
http://togogenome.org/gene/9606:PHF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type 1|||C2HC pre-PHD-type 2|||Disordered|||Extended PHD1 domain (ePHD1)|||Extended PHD2 domain (ePHD2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BFLS.|||In BFLS; Loss of interaction with UBTF.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-acetylserine|||Nuclear localization signal|||Nucleolar localization signal|||PHD finger protein 6|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059293|||http://purl.uniprot.org/annotation/VAR_017633|||http://purl.uniprot.org/annotation/VAR_017634|||http://purl.uniprot.org/annotation/VAR_017635|||http://purl.uniprot.org/annotation/VAR_017636|||http://purl.uniprot.org/annotation/VAR_017637|||http://purl.uniprot.org/annotation/VAR_076933|||http://purl.uniprot.org/annotation/VSP_009372|||http://purl.uniprot.org/annotation/VSP_009373|||http://purl.uniprot.org/annotation/VSP_009374|||http://purl.uniprot.org/annotation/VSP_053441|||http://purl.uniprot.org/annotation/VSP_054937
http://togogenome.org/gene/9606:ARMC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z637|||http://purl.uniprot.org/uniprot/Q8IUR7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 13|||ARM 14|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Armadillo repeat-containing protein 8|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284408|||http://purl.uniprot.org/annotation/VSP_024509|||http://purl.uniprot.org/annotation/VSP_024512|||http://purl.uniprot.org/annotation/VSP_024513|||http://purl.uniprot.org/annotation/VSP_024514|||http://purl.uniprot.org/annotation/VSP_044774|||http://purl.uniprot.org/annotation/VSP_045137
http://togogenome.org/gene/9606:KRTAP21-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LHN1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 21-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000386448
http://togogenome.org/gene/9606:FCGRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZI2|||http://purl.uniprot.org/uniprot/P55899                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C1-type|||IgG receptor FcRn large subunit p51|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015157|||http://purl.uniprot.org/annotation/PRO_5014214179
http://togogenome.org/gene/9606:NOL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Nucleolar protein 10|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051101|||http://purl.uniprot.org/annotation/VAR_060041|||http://purl.uniprot.org/annotation/VSP_015454|||http://purl.uniprot.org/annotation/VSP_015455|||http://purl.uniprot.org/annotation/VSP_015456|||http://purl.uniprot.org/annotation/VSP_015457|||http://purl.uniprot.org/annotation/VSP_015458|||http://purl.uniprot.org/annotation/VSP_045122
http://togogenome.org/gene/9606:MBNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A3S3|||http://purl.uniprot.org/uniprot/Q5VZF2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||In isoform 2.|||In isoform 3.|||Muscleblind-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274872|||http://purl.uniprot.org/annotation/VSP_022887|||http://purl.uniprot.org/annotation/VSP_022888
http://togogenome.org/gene/9606:GPER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63ZY2|||http://purl.uniprot.org/uniprot/Q99527                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled estrogen receptor 1|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069310|||http://purl.uniprot.org/annotation/VAR_033319
http://togogenome.org/gene/9606:RBM14-RBM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYI9|||http://purl.uniprot.org/uniprot/Q96PK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein 14|||RRM|||RRM 1|||RRM 2|||TRBP-interacting domain; interaction with STIL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081774|||http://purl.uniprot.org/annotation/VSP_015078|||http://purl.uniprot.org/annotation/VSP_015079|||http://purl.uniprot.org/annotation/VSP_044641|||http://purl.uniprot.org/annotation/VSP_044642|||http://purl.uniprot.org/annotation/VSP_047109|||http://purl.uniprot.org/annotation/VSP_047110|||http://purl.uniprot.org/annotation/VSP_047494|||http://purl.uniprot.org/annotation/VSP_047495
http://togogenome.org/gene/9606:SETDB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15047                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone-lysine N-methyltransferase SETDB1|||In isoform 2.|||In isoform 3.|||MBD|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pre-SET|||Pro residues|||SET|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186064|||http://purl.uniprot.org/annotation/VAR_014284|||http://purl.uniprot.org/annotation/VAR_014285|||http://purl.uniprot.org/annotation/VAR_014286|||http://purl.uniprot.org/annotation/VAR_031281|||http://purl.uniprot.org/annotation/VSP_002217|||http://purl.uniprot.org/annotation/VSP_002218|||http://purl.uniprot.org/annotation/VSP_034600
http://togogenome.org/gene/9606:CAMK2N1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7J9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  CAMK2 inhibitory domain|||Calcium/calmodulin-dependent protein kinase II inhibitor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338393
http://togogenome.org/gene/9606:TRPV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NER1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AD|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with calmodulin|||Loss of sensitivity to capsaicin.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA and PKD|||Phosphoserine; by PKC/PRKCE|||Phosphoserine; by PKC/PRKCE and PKC/PRKCZ|||Phosphothreonine|||Phosphothreonine; by PKA; in vitro|||Reduces sensitivity to capsaicin 40-fold.|||Required for PIP2-mediated channel inhibition|||Selectivity filter|||Transient receptor potential cation channel subfamily V member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215338|||http://purl.uniprot.org/annotation/VAR_022246|||http://purl.uniprot.org/annotation/VAR_057307|||http://purl.uniprot.org/annotation/VAR_057308|||http://purl.uniprot.org/annotation/VAR_057309|||http://purl.uniprot.org/annotation/VAR_071244|||http://purl.uniprot.org/annotation/VSP_056862
http://togogenome.org/gene/9606:OTOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHW6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Otospiralin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021976|||http://purl.uniprot.org/annotation/VAR_020601
http://togogenome.org/gene/9606:COQ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H96                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  4-hydroxybenzoate polyprenyltransferase, mitochondrial|||Helical|||In COQ10D1; decreased 4-hydroxybenzoate decaprenyltransferase activity.|||In COQ10D1; decreased ubiquinone biosynthesis.|||In COQ10D1; loss of ubiquinone biosynthesis.|||In COQ10D1; unknown pathological significance.|||In MSA1; associated with disease susceptibility.|||In MSA1; associated with disease susceptibility; decreased ubiquinone biosynthesis.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228623|||http://purl.uniprot.org/annotation/VAR_025701|||http://purl.uniprot.org/annotation/VAR_068161|||http://purl.uniprot.org/annotation/VAR_068162|||http://purl.uniprot.org/annotation/VAR_068163|||http://purl.uniprot.org/annotation/VAR_070237|||http://purl.uniprot.org/annotation/VAR_070238|||http://purl.uniprot.org/annotation/VAR_070239|||http://purl.uniprot.org/annotation/VAR_070240|||http://purl.uniprot.org/annotation/VAR_070241|||http://purl.uniprot.org/annotation/VAR_070242|||http://purl.uniprot.org/annotation/VAR_070243|||http://purl.uniprot.org/annotation/VAR_070244|||http://purl.uniprot.org/annotation/VAR_070245|||http://purl.uniprot.org/annotation/VAR_070246|||http://purl.uniprot.org/annotation/VAR_070247|||http://purl.uniprot.org/annotation/VAR_070248|||http://purl.uniprot.org/annotation/VAR_070249|||http://purl.uniprot.org/annotation/VAR_070250|||http://purl.uniprot.org/annotation/VAR_070251|||http://purl.uniprot.org/annotation/VAR_076913|||http://purl.uniprot.org/annotation/VAR_076914|||http://purl.uniprot.org/annotation/VAR_078121|||http://purl.uniprot.org/annotation/VSP_017677|||http://purl.uniprot.org/annotation/VSP_017678|||http://purl.uniprot.org/annotation/VSP_061606|||http://purl.uniprot.org/annotation/VSP_061607|||http://purl.uniprot.org/annotation/VSP_061608
http://togogenome.org/gene/9606:ATP5PB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24539                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase F(0) complex subunit B1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002513|||http://purl.uniprot.org/annotation/VAR_013176|||http://purl.uniprot.org/annotation/VAR_033534
http://togogenome.org/gene/9606:LURAP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV03                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Leucine rich adaptor protein 1-like|||N-acetylmethionine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089740|||http://purl.uniprot.org/annotation/VAR_028154|||http://purl.uniprot.org/annotation/VAR_028155|||http://purl.uniprot.org/annotation/VAR_085725
http://togogenome.org/gene/9606:SGMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VZ5                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Completely abolishes enzyme activity. No change in subcellular location.|||Cytoplasmic|||Helical|||In isoform 2.|||Phosphatidylcholine:ceramide cholinephosphotransferase 1|||Phosphoserine|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221068|||http://purl.uniprot.org/annotation/VSP_027223|||http://purl.uniprot.org/annotation/VSP_027224
http://togogenome.org/gene/9606:PRPF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2Q9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for branch point selection|||In RP13.|||In RP13; no effect on interaction with SNRNP200 and EFTUD2.|||In RP13; reduces interaction with EFTUD2, but not with SNRNP200.|||In RP13; reduces interaction with SNRNP200 and EFTUD2.|||Involved in interaction with pre-mRNA 5' splice site|||Linker|||MPN|||N-acetylalanine|||N6,N6-dimethyllysine|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-processing-splicing factor 8|||RNase H homology domain|||Removed|||Required for interaction with EFTUD2 and SNRNP200|||Restriction endonuclease homology domain|||Reverse transcriptase homology domain|||Strongly reduced interaction with RNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097040|||http://purl.uniprot.org/annotation/VAR_022622|||http://purl.uniprot.org/annotation/VAR_022623|||http://purl.uniprot.org/annotation/VAR_022624|||http://purl.uniprot.org/annotation/VAR_022625|||http://purl.uniprot.org/annotation/VAR_022626|||http://purl.uniprot.org/annotation/VAR_022627|||http://purl.uniprot.org/annotation/VAR_022628|||http://purl.uniprot.org/annotation/VAR_022629|||http://purl.uniprot.org/annotation/VAR_022630|||http://purl.uniprot.org/annotation/VAR_022631|||http://purl.uniprot.org/annotation/VAR_022632|||http://purl.uniprot.org/annotation/VAR_022633
http://togogenome.org/gene/9606:MYO1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R643|||http://purl.uniprot.org/uniprot/Q9UBC5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Benign variant; originally reported as possible disease-causing mutation in a patient with hearing loss.|||Found in a patient with hearing loss; unknown pathological significance.|||IQ 1|||IQ 2|||IQ 3|||Myosin motor|||TH1|||Unconventional myosin-Ia                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123438|||http://purl.uniprot.org/annotation/VAR_015945|||http://purl.uniprot.org/annotation/VAR_015946|||http://purl.uniprot.org/annotation/VAR_015947|||http://purl.uniprot.org/annotation/VAR_015948|||http://purl.uniprot.org/annotation/VAR_015949|||http://purl.uniprot.org/annotation/VAR_015950|||http://purl.uniprot.org/annotation/VAR_015951|||http://purl.uniprot.org/annotation/VAR_020320|||http://purl.uniprot.org/annotation/VAR_050207|||http://purl.uniprot.org/annotation/VAR_050208|||http://purl.uniprot.org/annotation/VAR_050209
http://togogenome.org/gene/9606:KLHL20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2M5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-148.|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-150.|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-148 and A-150.|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-146; A-148 and A-150.|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-113; A-146; A-148 and A-150.|||In KLHL20m6; abolishes interaction with CUL3; when associated with A-111; A-113; A-146; A-148 and A-150.|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119123|||http://purl.uniprot.org/annotation/VSP_057026|||http://purl.uniprot.org/annotation/VSP_057027
http://togogenome.org/gene/9606:PARVG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Gamma-parvin|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121585|||http://purl.uniprot.org/annotation/VSP_004540|||http://purl.uniprot.org/annotation/VSP_004541|||http://purl.uniprot.org/annotation/VSP_012953|||http://purl.uniprot.org/annotation/VSP_012954|||http://purl.uniprot.org/annotation/VSP_045145|||http://purl.uniprot.org/annotation/VSP_045146|||http://purl.uniprot.org/annotation/VSP_045147
http://togogenome.org/gene/9606:RAB20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX57                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Effector region|||Ras-related protein Rab-20|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121202|||http://purl.uniprot.org/annotation/VAR_017158
http://togogenome.org/gene/9606:CEBPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53567                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||CCAAT/enhancer-binding protein gamma|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076628
http://togogenome.org/gene/9606:ZBTB24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43167                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In ICF2.|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger and BTB domain-containing protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047734|||http://purl.uniprot.org/annotation/VAR_057458|||http://purl.uniprot.org/annotation/VAR_065846|||http://purl.uniprot.org/annotation/VSP_016221|||http://purl.uniprot.org/annotation/VSP_016222
http://togogenome.org/gene/9606:BMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12645                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein 3|||Disordered|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033836|||http://purl.uniprot.org/annotation/PRO_0000033837|||http://purl.uniprot.org/annotation/VAR_020063|||http://purl.uniprot.org/annotation/VAR_047418|||http://purl.uniprot.org/annotation/VAR_047419|||http://purl.uniprot.org/annotation/VAR_047420|||http://purl.uniprot.org/annotation/VAR_047421
http://togogenome.org/gene/9606:ACER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alkaline ceramidase 1|||Cytoplasmic|||Helical|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247745
http://togogenome.org/gene/9606:ABHD16B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3Z7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Protein ABHD16B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079463|||http://purl.uniprot.org/annotation/VAR_050920
http://togogenome.org/gene/9606:OPCML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0Y0|||http://purl.uniprot.org/uniprot/B2CZX3|||http://purl.uniprot.org/uniprot/B7ZLQ0|||http://purl.uniprot.org/uniprot/Q14982                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In ovarian cancer; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Opioid-binding protein/cell adhesion molecule|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015118|||http://purl.uniprot.org/annotation/PRO_0000015119|||http://purl.uniprot.org/annotation/PRO_5002866684|||http://purl.uniprot.org/annotation/PRO_5014297567|||http://purl.uniprot.org/annotation/VAR_055421|||http://purl.uniprot.org/annotation/VSP_043440|||http://purl.uniprot.org/annotation/VSP_047730|||http://purl.uniprot.org/annotation/VSP_054155
http://togogenome.org/gene/9606:KLHL32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ08|||http://purl.uniprot.org/uniprot/Q96NJ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||In isoform 2 and isoform 3.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119083|||http://purl.uniprot.org/annotation/VAR_028279|||http://purl.uniprot.org/annotation/VAR_028280|||http://purl.uniprot.org/annotation/VAR_050053|||http://purl.uniprot.org/annotation/VSP_054888|||http://purl.uniprot.org/annotation/VSP_054889
http://togogenome.org/gene/9606:FAAP100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4ZI32|||http://purl.uniprot.org/uniprot/Q0VG06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fanconi anemia core complex-associated protein 100|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289130|||http://purl.uniprot.org/annotation/VAR_032582|||http://purl.uniprot.org/annotation/VAR_032583|||http://purl.uniprot.org/annotation/VSP_025922|||http://purl.uniprot.org/annotation/VSP_025923|||http://purl.uniprot.org/annotation/VSP_038262
http://togogenome.org/gene/9606:ARHGAP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5U3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Altered interaction with ARF1 and loss of association to membranes.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 3.|||Interaction with ARF1 and ARF6|||Interaction with CTNNA1|||Loss of GTPase activity and loss of function.|||Omega-N-methylarginine|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 21|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305245|||http://purl.uniprot.org/annotation/VAR_035187|||http://purl.uniprot.org/annotation/VAR_035188|||http://purl.uniprot.org/annotation/VAR_035189|||http://purl.uniprot.org/annotation/VAR_035190|||http://purl.uniprot.org/annotation/VAR_035191|||http://purl.uniprot.org/annotation/VAR_035192|||http://purl.uniprot.org/annotation/VSP_028298|||http://purl.uniprot.org/annotation/VSP_028300|||http://purl.uniprot.org/annotation/VSP_028301
http://togogenome.org/gene/9606:SLC25A25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6KCM7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-terminal transmembrane transporter domain|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Found in patients with recurrent kidney stones formation; unknown pathological significance; no effect on protein abundance; no effect on stability; decreased adenyl nucleotide antiporter activity; no effect on transporter activity regulation by calcium.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||Linker region|||Mitochondrial adenyl nucleotide antiporter SLC25A25|||Mitochondrial intermembrane|||Mitochondrial matrix|||Regulatory N-terminal domain|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317602|||http://purl.uniprot.org/annotation/VAR_087883|||http://purl.uniprot.org/annotation/VSP_031067|||http://purl.uniprot.org/annotation/VSP_031068|||http://purl.uniprot.org/annotation/VSP_031069|||http://purl.uniprot.org/annotation/VSP_031070
http://togogenome.org/gene/9606:SYCP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes fiber formation.|||Basic and acidic residues|||Disordered|||Impairs DNA binding. Abolishes DNA binding; when associated with 52-A--A-57.|||Impairs DNA binding. Abolishes DNA binding; when associated with 88-A--A-91.|||Important for oligomerization and fiber formation|||Interaction with DNA|||Nuclear localization signal|||Phosphoserine|||Synaptonemal complex protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229024
http://togogenome.org/gene/9606:SYT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XYQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Helical|||Phosphothreonine|||Synaptotagmin-10|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183965|||http://purl.uniprot.org/annotation/VAR_034529|||http://purl.uniprot.org/annotation/VAR_034530|||http://purl.uniprot.org/annotation/VAR_034531|||http://purl.uniprot.org/annotation/VAR_059826
http://togogenome.org/gene/9606:GAS2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5E8|||http://purl.uniprot.org/uniprot/Q99501                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of microtubule-end localization and microtubule plus-end tracking. Decreases MAPRE1 binding.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190442|||http://purl.uniprot.org/annotation/VAR_059974|||http://purl.uniprot.org/annotation/VSP_015493|||http://purl.uniprot.org/annotation/VSP_015494|||http://purl.uniprot.org/annotation/VSP_015495|||http://purl.uniprot.org/annotation/VSP_055754
http://togogenome.org/gene/9606:BBS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAM1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 10 protein|||Found in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; rare variant; unknown pathological significance.|||Found in a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; unknown pathological significance.|||Greatly decreases all interactions with BBS7, BBS9 and BBS12 indicating that this residue may be required for overall protein conformation rather than required for ATP binding and substrate folding.|||In BBS10.|||In BBS10; associated with T-188.|||In BBS10; associated with V-636.|||In BBS10; has moderately reduced ability to interact with BBS7 and BBS9.|||In BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 15% of wild-type.|||In BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 19% of wild-type.|||In BBS10; has moderately reduced ability to interact with BBS7 and BBS9; severely reduces the interaction with BBS12; 8% of wild-type.|||In BBS10; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235272|||http://purl.uniprot.org/annotation/VAR_026391|||http://purl.uniprot.org/annotation/VAR_026392|||http://purl.uniprot.org/annotation/VAR_026393|||http://purl.uniprot.org/annotation/VAR_026394|||http://purl.uniprot.org/annotation/VAR_026395|||http://purl.uniprot.org/annotation/VAR_026396|||http://purl.uniprot.org/annotation/VAR_026397|||http://purl.uniprot.org/annotation/VAR_026398|||http://purl.uniprot.org/annotation/VAR_026399|||http://purl.uniprot.org/annotation/VAR_026400|||http://purl.uniprot.org/annotation/VAR_026401|||http://purl.uniprot.org/annotation/VAR_026402|||http://purl.uniprot.org/annotation/VAR_026403|||http://purl.uniprot.org/annotation/VAR_026404|||http://purl.uniprot.org/annotation/VAR_026405|||http://purl.uniprot.org/annotation/VAR_026406|||http://purl.uniprot.org/annotation/VAR_026407|||http://purl.uniprot.org/annotation/VAR_026408|||http://purl.uniprot.org/annotation/VAR_052272|||http://purl.uniprot.org/annotation/VAR_066252|||http://purl.uniprot.org/annotation/VAR_066253|||http://purl.uniprot.org/annotation/VAR_066254|||http://purl.uniprot.org/annotation/VAR_066255|||http://purl.uniprot.org/annotation/VAR_066256|||http://purl.uniprot.org/annotation/VAR_066257|||http://purl.uniprot.org/annotation/VAR_066258|||http://purl.uniprot.org/annotation/VAR_066259|||http://purl.uniprot.org/annotation/VAR_066260|||http://purl.uniprot.org/annotation/VAR_066261|||http://purl.uniprot.org/annotation/VAR_075722|||http://purl.uniprot.org/annotation/VAR_079367|||http://purl.uniprot.org/annotation/VAR_079368
http://togogenome.org/gene/9606:CD58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19256                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In isoform 2.|||In isoform 3.|||Lymphocyte function-associated antigen 3|||N-linked (GlcNAc...) asparagine|||No effect on CD2-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014814|||http://purl.uniprot.org/annotation/VAR_049885|||http://purl.uniprot.org/annotation/VSP_002522|||http://purl.uniprot.org/annotation/VSP_002523|||http://purl.uniprot.org/annotation/VSP_038693
http://togogenome.org/gene/9606:RPUSD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUN4|||http://purl.uniprot.org/uniprot/Q96CM3                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrion|||Pseudouridine synthase RsuA/RluA-like|||Pseudouridylate synthase RPUSD4, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300825|||http://purl.uniprot.org/annotation/VAR_034887|||http://purl.uniprot.org/annotation/VAR_034888|||http://purl.uniprot.org/annotation/VAR_034889|||http://purl.uniprot.org/annotation/VAR_034890|||http://purl.uniprot.org/annotation/VSP_047375
http://togogenome.org/gene/9606:C2orf73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5S3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C2orf73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332213|||http://purl.uniprot.org/annotation/VAR_042973|||http://purl.uniprot.org/annotation/VAR_042974|||http://purl.uniprot.org/annotation/VAR_061571|||http://purl.uniprot.org/annotation/VSP_033353
http://togogenome.org/gene/9606:OR5B21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NL26                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5B21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310474|||http://purl.uniprot.org/annotation/VAR_062041
http://togogenome.org/gene/9606:PTPRJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12913|||http://purl.uniprot.org/uniprot/Q9NPR5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  80% decrease in interaction with MAPK1 and MAPK3.|||Catalytically inactive and substrate trapping with higher affinity for substrate.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Helical|||In a colon cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Receptor-type tyrosine-protein phosphatase eta|||Substrate trapping with much higher affinity for substrate.|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025444|||http://purl.uniprot.org/annotation/PRO_5004335661|||http://purl.uniprot.org/annotation/VAR_015905|||http://purl.uniprot.org/annotation/VAR_015906|||http://purl.uniprot.org/annotation/VAR_024582|||http://purl.uniprot.org/annotation/VAR_038414|||http://purl.uniprot.org/annotation/VAR_038415|||http://purl.uniprot.org/annotation/VAR_038416|||http://purl.uniprot.org/annotation/VAR_038417|||http://purl.uniprot.org/annotation/VSP_043652|||http://purl.uniprot.org/annotation/VSP_043653|||http://purl.uniprot.org/annotation/VSP_060928
http://togogenome.org/gene/9606:TRIM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C030                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding of polyubiquitin to IKBKE.|||B box-type|||B30.2/SPRY|||In isoform 2.|||In isoform 3.|||RING-type|||Reduced higher order self-association and association with TRIM5.|||Tripartite motif-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056202|||http://purl.uniprot.org/annotation/VAR_061823|||http://purl.uniprot.org/annotation/VSP_012087|||http://purl.uniprot.org/annotation/VSP_046924
http://togogenome.org/gene/9606:SBF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PH87|||http://purl.uniprot.org/uniprot/Q86WG5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GRAM|||In isoform 3.|||Myotubularin phosphatase|||Myotubularin-related protein 13|||PH|||Phosphoserine|||Required for homodimerization and interaction with MTMR2|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094945|||http://purl.uniprot.org/annotation/VAR_051766|||http://purl.uniprot.org/annotation/VAR_051767|||http://purl.uniprot.org/annotation/VAR_051768|||http://purl.uniprot.org/annotation/VSP_017157|||http://purl.uniprot.org/annotation/VSP_017158
http://togogenome.org/gene/9606:GINM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NU53                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycoprotein integral membrane protein 1|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019543
http://togogenome.org/gene/9606:CIDEA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60543|||http://purl.uniprot.org/uniprot/Q8N5P9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amphipathic helix|||CIDE-N|||Disordered|||Lipid transferase CIDEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144718|||http://purl.uniprot.org/annotation/VAR_048738
http://togogenome.org/gene/9606:ABAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80404|||http://purl.uniprot.org/uniprot/X5D8S1                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  4-aminobutyrate aminotransferase, mitochondrial|||In GABATD; 25% reduction in 4-aminobutyrate aminotransferase activity.|||Interchain|||Loss of 4-aminobutyrate aminotransferase activity.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001249|||http://purl.uniprot.org/annotation/VAR_008883|||http://purl.uniprot.org/annotation/VAR_018979
http://togogenome.org/gene/9606:DENND6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEG7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Protein DENND6B|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264990
http://togogenome.org/gene/9606:WIZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFV2|||http://purl.uniprot.org/uniprot/M0QXA7|||http://purl.uniprot.org/uniprot/O95785                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CTBP1 and CTBP2 1|||Interaction with CTBP1 and CTBP2 2|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Wiz                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286054|||http://purl.uniprot.org/annotation/VSP_024951|||http://purl.uniprot.org/annotation/VSP_024952|||http://purl.uniprot.org/annotation/VSP_054509|||http://purl.uniprot.org/annotation/VSP_054510|||http://purl.uniprot.org/annotation/VSP_054511|||http://purl.uniprot.org/annotation/VSP_057207|||http://purl.uniprot.org/annotation/VSP_057208
http://togogenome.org/gene/9606:PLEKHA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PX43|||http://purl.uniprot.org/uniprot/Q9HAU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-acetylalanine|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family A member 5|||Polar residues|||Removed|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053883|||http://purl.uniprot.org/annotation/VSP_009775|||http://purl.uniprot.org/annotation/VSP_009776|||http://purl.uniprot.org/annotation/VSP_009777|||http://purl.uniprot.org/annotation/VSP_009778|||http://purl.uniprot.org/annotation/VSP_014595|||http://purl.uniprot.org/annotation/VSP_044678|||http://purl.uniprot.org/annotation/VSP_044679|||http://purl.uniprot.org/annotation/VSP_046861|||http://purl.uniprot.org/annotation/VSP_047514|||http://purl.uniprot.org/annotation/VSP_047515
http://togogenome.org/gene/9606:MGAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43451                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreases alpha-1,4-glucosidase activity toward long oligomaltose substrates having four to seven D-glucose residues.|||Decreases alpha-1,4-glucosidase activity toward maltose.|||Disordered|||Glucoamylase|||Helical; Signal-anchor for type II membrane protein|||In isoform 1.|||Loss of alpha-1,4-glucosidase activity toward maltose.|||Lumenal|||Maltase|||Maltase-glucoamylase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||P-type 1|||P-type 2|||P-type 3|||Polar residues|||Proton donor|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185363|||http://purl.uniprot.org/annotation/VAR_047350|||http://purl.uniprot.org/annotation/VAR_047351|||http://purl.uniprot.org/annotation/VAR_047352|||http://purl.uniprot.org/annotation/VAR_047353|||http://purl.uniprot.org/annotation/VSP_061364
http://togogenome.org/gene/9606:OR5AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW20|||http://purl.uniprot.org/uniprot/Q8NH90                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150575|||http://purl.uniprot.org/annotation/VAR_034215|||http://purl.uniprot.org/annotation/VAR_034216|||http://purl.uniprot.org/annotation/VAR_060007
http://togogenome.org/gene/9606:XG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E289|||http://purl.uniprot.org/uniprot/P55808                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glycoprotein Xg|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022693|||http://purl.uniprot.org/annotation/PRO_5002803766|||http://purl.uniprot.org/annotation/VAR_054063|||http://purl.uniprot.org/annotation/VSP_037319|||http://purl.uniprot.org/annotation/VSP_037320
http://togogenome.org/gene/9606:SOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00570                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  9aaTAD|||Basic residues|||Disordered|||HMG box|||Transcription factor SOX-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048712
http://togogenome.org/gene/9606:COQ6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SFJ1|||http://purl.uniprot.org/uniprot/Q9Y2Z9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAD-binding|||In COQ10D6.|||In COQ10D6; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||Probable disease-associated variant found in patients with Schwannomatosis; loss of function.|||Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207583|||http://purl.uniprot.org/annotation/VAR_014953|||http://purl.uniprot.org/annotation/VAR_033813|||http://purl.uniprot.org/annotation/VAR_033814|||http://purl.uniprot.org/annotation/VAR_052691|||http://purl.uniprot.org/annotation/VAR_068216|||http://purl.uniprot.org/annotation/VAR_068217|||http://purl.uniprot.org/annotation/VAR_068218|||http://purl.uniprot.org/annotation/VAR_075225|||http://purl.uniprot.org/annotation/VAR_078122|||http://purl.uniprot.org/annotation/VSP_044060|||http://purl.uniprot.org/annotation/VSP_044061|||http://purl.uniprot.org/annotation/VSP_044062
http://togogenome.org/gene/9606:PBX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox; TALE-type|||In a colorectal cancer sample; somatic mutation.|||PBC|||PBC-A|||PBC-B|||Polar residues|||Pre-B-cell leukemia transcription factor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049241|||http://purl.uniprot.org/annotation/VAR_036439|||http://purl.uniprot.org/annotation/VAR_059355|||http://purl.uniprot.org/annotation/VAR_059356
http://togogenome.org/gene/9606:CASP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51878                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes protease activity.|||CARD|||Caspase-5 subunit p10|||Caspase-5 subunit p20|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004604|||http://purl.uniprot.org/annotation/PRO_0000004605|||http://purl.uniprot.org/annotation/PRO_0000004606|||http://purl.uniprot.org/annotation/PRO_0000004607|||http://purl.uniprot.org/annotation/VAR_024403|||http://purl.uniprot.org/annotation/VAR_024404|||http://purl.uniprot.org/annotation/VAR_024405|||http://purl.uniprot.org/annotation/VAR_047216|||http://purl.uniprot.org/annotation/VAR_047217|||http://purl.uniprot.org/annotation/VAR_047218|||http://purl.uniprot.org/annotation/VAR_047219|||http://purl.uniprot.org/annotation/VAR_047220|||http://purl.uniprot.org/annotation/VAR_054480|||http://purl.uniprot.org/annotation/VAR_054481|||http://purl.uniprot.org/annotation/VAR_054482|||http://purl.uniprot.org/annotation/VSP_038990|||http://purl.uniprot.org/annotation/VSP_038991|||http://purl.uniprot.org/annotation/VSP_038992|||http://purl.uniprot.org/annotation/VSP_038993|||http://purl.uniprot.org/annotation/VSP_038994|||http://purl.uniprot.org/annotation/VSP_038995
http://togogenome.org/gene/9606:TAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00268                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Minimal region required to interact with TAF12|||N6,N6-dimethyllysine|||Phosphoserine|||Polar residues|||Pro residues|||TAFH|||Transcription initiation factor TFIID subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118869|||http://purl.uniprot.org/annotation/VAR_052258
http://togogenome.org/gene/9606:TMSB4X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VCK8|||http://purl.uniprot.org/uniprot/P62328|||http://purl.uniprot.org/uniprot/Q0P5T0                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Region                                                                                  ^@                                                                                  Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hemoregulatory peptide AcSDKP|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Thymosin beta-4|||Very weak actin binding; no inhibition of actin polymerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034295|||http://purl.uniprot.org/annotation/PRO_0000045920
http://togogenome.org/gene/9606:FAM3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58499                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GG-type lectin|||In isoform A.|||In isoform C.|||N-linked (GlcNAc...) asparagine|||Protein FAM3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008750|||http://purl.uniprot.org/annotation/VAR_021953|||http://purl.uniprot.org/annotation/VSP_001504|||http://purl.uniprot.org/annotation/VSP_001505
http://togogenome.org/gene/9606:ATP2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20020                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Calmodulin-binding subdomain A|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with developmental delay; unknown pathological significance; no effect on calcium ion export across plasma membrane.|||Helical|||In MRD66.|||In MRD66; decreased calcium ion export across plasma membrane.|||In MRD66; decreased calcium ion export across plasma membrane; decreased localization to plasma membrane.|||In isoform A and isoform E.|||In isoform A.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform K.|||N-acetylglycine|||No effect on calcium ion export across plasma membrane.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 1|||Polar residues|||Removed|||Required for basolateral membrane targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046209|||http://purl.uniprot.org/annotation/VAR_000698|||http://purl.uniprot.org/annotation/VAR_087432|||http://purl.uniprot.org/annotation/VAR_087433|||http://purl.uniprot.org/annotation/VAR_087434|||http://purl.uniprot.org/annotation/VAR_087435|||http://purl.uniprot.org/annotation/VAR_087436|||http://purl.uniprot.org/annotation/VAR_087437|||http://purl.uniprot.org/annotation/VAR_087438|||http://purl.uniprot.org/annotation/VAR_087439|||http://purl.uniprot.org/annotation/VAR_087440|||http://purl.uniprot.org/annotation/VAR_087441|||http://purl.uniprot.org/annotation/VAR_087442|||http://purl.uniprot.org/annotation/VAR_087443|||http://purl.uniprot.org/annotation/VAR_087444|||http://purl.uniprot.org/annotation/VAR_087445|||http://purl.uniprot.org/annotation/VSP_059771|||http://purl.uniprot.org/annotation/VSP_059772|||http://purl.uniprot.org/annotation/VSP_059773|||http://purl.uniprot.org/annotation/VSP_059774|||http://purl.uniprot.org/annotation/VSP_059775|||http://purl.uniprot.org/annotation/VSP_059776
http://togogenome.org/gene/9606:KLRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3W0D1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily F member 2|||Loss of function.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000404560
http://togogenome.org/gene/9606:FANCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R9N2|||http://purl.uniprot.org/uniprot/A0A087WW44|||http://purl.uniprot.org/uniprot/Q00597                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fanconi anemia group C protein|||In FANCC.|||In FANCC; loss of activity; loss of CDK1-binding and IFNG-induced STAT1-binding; abnormal EIF2AK2 activation and augmented cell death.|||No effect on protective function from mitomycin C-genotoxicity.|||No effect on protective function from mitomycin C-genotoxicity. Loss of IFNG-induced STAT1-binding.|||No effect on protective function from mitomycin C-genotoxicity. No effect on IFNG-induced STAT1-binding.|||No loss of protection from cross-linking agent-induced toxicity. No effect on IFNG-induced STAT1-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087184|||http://purl.uniprot.org/annotation/VAR_005225|||http://purl.uniprot.org/annotation/VAR_005226|||http://purl.uniprot.org/annotation/VAR_005227|||http://purl.uniprot.org/annotation/VAR_005228|||http://purl.uniprot.org/annotation/VAR_005229|||http://purl.uniprot.org/annotation/VAR_005230|||http://purl.uniprot.org/annotation/VAR_005231|||http://purl.uniprot.org/annotation/VAR_005232|||http://purl.uniprot.org/annotation/VAR_005233|||http://purl.uniprot.org/annotation/VAR_016339
http://togogenome.org/gene/9606:ZNG1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X140|||http://purl.uniprot.org/uniprot/Q9BRT8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CXCC motif|||CobW C-terminal|||CobW/HypB/UreG nucleotide-binding|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Zinc-regulated GTPase metalloprotein activator 1A|||psi-PxLVp motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245523|||http://purl.uniprot.org/annotation/VAR_026979|||http://purl.uniprot.org/annotation/VSP_019731|||http://purl.uniprot.org/annotation/VSP_019732|||http://purl.uniprot.org/annotation/VSP_019733|||http://purl.uniprot.org/annotation/VSP_019734
http://togogenome.org/gene/9606:NAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8T1|||http://purl.uniprot.org/uniprot/B4DKG1|||http://purl.uniprot.org/uniprot/B8ZZS2|||http://purl.uniprot.org/uniprot/Q13506                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform Short.|||NAB co-repressor|||NCD1|||NCD2|||NGFI-A-binding protein 1|||Nab N-terminal|||Nab1 C-terminal|||Necessary for nuclear localization|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077038|||http://purl.uniprot.org/annotation/VSP_003384
http://togogenome.org/gene/9606:TCF24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Transcription factor 24|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000405315
http://togogenome.org/gene/9606:CCDC92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53HC0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 92|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274500|||http://purl.uniprot.org/annotation/VAR_030301|||http://purl.uniprot.org/annotation/VAR_030302|||http://purl.uniprot.org/annotation/VAR_050765|||http://purl.uniprot.org/annotation/VSP_056906
http://togogenome.org/gene/9606:TNNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PY19|||http://purl.uniprot.org/uniprot/H9KVA2|||http://purl.uniprot.org/uniprot/P45378                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In DA2B2.|||In isoform 2, isoform 4 and isoform 7.|||In isoform 3, isoform 4 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylserine|||Phosphoserine|||Removed|||Troponin T, fast skeletal muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186178|||http://purl.uniprot.org/annotation/VAR_026453|||http://purl.uniprot.org/annotation/VAR_082280|||http://purl.uniprot.org/annotation/VSP_007914|||http://purl.uniprot.org/annotation/VSP_007915|||http://purl.uniprot.org/annotation/VSP_007916|||http://purl.uniprot.org/annotation/VSP_009121|||http://purl.uniprot.org/annotation/VSP_034964
http://togogenome.org/gene/9606:KAT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7Z6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes histone acetyltransferase activity.|||C2HC MYST-type|||Disordered|||Found in a severe neurodevelopmental disorder similar to Li-Ghorbani-Weisz-Hubshman syndrome with apparently autosomal recessive inheritance; unknown pathological significance; loss of protein expression.|||Found in a severe neurodevelopmental disorder similar to Li-Ghorbani-Weisz-Hubshman syndrome with apparently autosomal recessive inheritance; unknown pathological significance; no effect on protein expression; no effect on localization to the nucleus; no effect on MSL complex assembly; decreased histone acetyltransferase activity.|||Histone acetyltransferase KAT8|||In LIGOWS; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity.|||In LIGOWS; unknown pathological significance; no effect on protein expression; no effect on MSL complex assembly; decreased histone acetyltransferase activity.|||In isoform 2.|||MYST-type HAT|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Proton donor/acceptor|||Removed|||Strongly reduces histone acetyltransferase activity.|||Sufficient for interaction with KANSL1|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051566|||http://purl.uniprot.org/annotation/VAR_084751|||http://purl.uniprot.org/annotation/VAR_084752|||http://purl.uniprot.org/annotation/VAR_084753|||http://purl.uniprot.org/annotation/VAR_084754|||http://purl.uniprot.org/annotation/VAR_084755|||http://purl.uniprot.org/annotation/VAR_084756|||http://purl.uniprot.org/annotation/VAR_084757|||http://purl.uniprot.org/annotation/VAR_084758|||http://purl.uniprot.org/annotation/VSP_014579
http://togogenome.org/gene/9606:HYCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIT6|||http://purl.uniprot.org/uniprot/B3KUG1|||http://purl.uniprot.org/uniprot/Q8IXS8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hyccin 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278094
http://togogenome.org/gene/9606:MAP3K8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41279|||http://purl.uniprot.org/uniprot/Q6FG25                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Impaired MEK phosphorylation and autophosphorylation activities. No effect on KSR2 binding.|||In isoform 2.|||In oncogenic form.|||Loss of MEK phosphorylation activity and almost abolished autophosphorylation activity. Loss of IL1-stimulated MEK phosphorylation activity but not of IL1-stimulated autophosphorylation activity. No effect on KSR2 binding.|||Loss of MEK phosphorylation activity and almost abolished autophosphorylation activity. No effect on KSR2 binding.|||Mitogen-activated protein kinase kinase kinase 8|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024350|||http://purl.uniprot.org/annotation/VAR_006198|||http://purl.uniprot.org/annotation/VAR_006199|||http://purl.uniprot.org/annotation/VAR_051638|||http://purl.uniprot.org/annotation/VSP_018843
http://togogenome.org/gene/9606:GNGT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14610                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012645|||http://purl.uniprot.org/annotation/PRO_0000012646|||http://purl.uniprot.org/annotation/VAR_049271
http://togogenome.org/gene/9606:RGS22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V112|||http://purl.uniprot.org/uniprot/Q8NE09                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||RGS|||RGS 1|||RGS 2|||Regulator of G-protein signaling 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271376|||http://purl.uniprot.org/annotation/VAR_051797|||http://purl.uniprot.org/annotation/VAR_051798|||http://purl.uniprot.org/annotation/VSP_022306|||http://purl.uniprot.org/annotation/VSP_054225
http://togogenome.org/gene/9606:RNF175                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4F7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Helical|||In isoform 2.|||RING finger protein 175|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245599|||http://purl.uniprot.org/annotation/VAR_026998|||http://purl.uniprot.org/annotation/VAR_026999|||http://purl.uniprot.org/annotation/VAR_027000|||http://purl.uniprot.org/annotation/VAR_027001|||http://purl.uniprot.org/annotation/VSP_055433|||http://purl.uniprot.org/annotation/VSP_055434|||http://purl.uniprot.org/annotation/VSP_055435|||http://purl.uniprot.org/annotation/VSP_055436
http://togogenome.org/gene/9606:CLMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3S3|||http://purl.uniprot.org/uniprot/Q9H6B4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CXADR-like membrane protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In CSBS; affects subcellular location; the mutant protein is localized in the cytoplasm.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293026|||http://purl.uniprot.org/annotation/PRO_5002801155|||http://purl.uniprot.org/annotation/VAR_049824|||http://purl.uniprot.org/annotation/VAR_069713
http://togogenome.org/gene/9606:RUSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIT1|||http://purl.uniprot.org/uniprot/B4DQB8|||http://purl.uniprot.org/uniprot/Q9BVN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-4 complex accessory subunit RUSC1|||Abrogates nuclear redistribution.|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with IKBKG|||Interaction with TRAF6|||Polar residues|||Pro residues|||RUN|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097532|||http://purl.uniprot.org/annotation/VAR_036803|||http://purl.uniprot.org/annotation/VAR_051329|||http://purl.uniprot.org/annotation/VSP_010855|||http://purl.uniprot.org/annotation/VSP_054052|||http://purl.uniprot.org/annotation/VSP_054053
http://togogenome.org/gene/9606:ADRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07550|||http://purl.uniprot.org/uniprot/X5DQM5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization.|||Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins.|||Beta-2 adrenergic receptor|||Cytoplasmic|||Delayed agonist-promoted desensitization.|||Disordered|||Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization.|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of basal palmitoylation.|||Loss of ligand-induced palmitoylation.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphoserine; by BARK|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues|||S-palmitoyl cysteine|||Uncoupled receptor.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069130|||http://purl.uniprot.org/annotation/VAR_003452|||http://purl.uniprot.org/annotation/VAR_003453|||http://purl.uniprot.org/annotation/VAR_003454|||http://purl.uniprot.org/annotation/VAR_003455|||http://purl.uniprot.org/annotation/VAR_009124|||http://purl.uniprot.org/annotation/VAR_009125|||http://purl.uniprot.org/annotation/VAR_009394|||http://purl.uniprot.org/annotation/VAR_025101|||http://purl.uniprot.org/annotation/VAR_049373
http://togogenome.org/gene/9606:SDCBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHN5|||http://purl.uniprot.org/uniprot/G5EA09|||http://purl.uniprot.org/uniprot/O00560                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Disruption of the cooperative binding of C-terminal peptides from FZD7 and phosphatidylinositol-4,5-bisphosphate.|||Disruption of the cooperative binding of C-terminal peptides from FZD7 and phosphatidylinositol-4,5-bisphosphate. Impaired interaction with FZD7 and disruption of the cooperative binding of C-terminal peptides from FZD7 and phosphatidylinositol-4,5-bisphosphate; when associated with A-214.|||Disruption of the cooperative binding of C-terminal peptides from FZD7 and phosphatidylinositol-4,5-bisphosphate. Impaired interaction with FZD7 and disruption of the cooperative binding of C-terminal peptides from FZD7 and phosphatidylinositol-4,5-bisphosphate; when associated with A-250.|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with PDCD6IP|||LYPX(n)L motif 1|||LYPX(n)L motif 2|||LYPX(n)L motif 3|||N-acetylserine|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Phosphotyrosine|||Removed|||Syntenin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184001|||http://purl.uniprot.org/annotation/VAR_013160|||http://purl.uniprot.org/annotation/VSP_038374|||http://purl.uniprot.org/annotation/VSP_038375
http://togogenome.org/gene/9606:PAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIQ0|||http://purl.uniprot.org/uniprot/O43832|||http://purl.uniprot.org/uniprot/P19021                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Copper type II ascorbate-dependent monooxygenase C-terminal|||Copper type II ascorbate-dependent monooxygenase N-terminal|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with RASSF9|||Intragranular|||N-linked (GlcNAc...) asparagine|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Peptidyl-alpha-hydroxyglycine alpha-amidating lyase|||Peptidyl-glycine alpha-amidating monooxygenase|||Peptidylglycine alpha-hydroxylating monooxygenase|||Phosphoserine|||Phosphoserine; by UHMK1; in vitro|||Phosphothreonine|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006361|||http://purl.uniprot.org/annotation/PRO_0000006362|||http://purl.uniprot.org/annotation/PRO_5032865847|||http://purl.uniprot.org/annotation/VAR_055694|||http://purl.uniprot.org/annotation/VSP_001227|||http://purl.uniprot.org/annotation/VSP_001228|||http://purl.uniprot.org/annotation/VSP_001229|||http://purl.uniprot.org/annotation/VSP_038691|||http://purl.uniprot.org/annotation/VSP_042209
http://togogenome.org/gene/9606:ZNF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17014                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||KRAB|||Zinc finger protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047335|||http://purl.uniprot.org/annotation/VSP_040334|||http://purl.uniprot.org/annotation/VSP_040335|||http://purl.uniprot.org/annotation/VSP_040738|||http://purl.uniprot.org/annotation/VSP_040739
http://togogenome.org/gene/9606:GOLGA8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2F4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi-targeting domain|||Golgin subfamily A member 8A|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190070|||http://purl.uniprot.org/annotation/VAR_064650|||http://purl.uniprot.org/annotation/VAR_064651|||http://purl.uniprot.org/annotation/VAR_064652|||http://purl.uniprot.org/annotation/VSP_040753
http://togogenome.org/gene/9606:CRY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2I2P0|||http://purl.uniprot.org/uniprot/Q16526                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Cryptochrome-1|||Disordered|||Electron transfer via tryptophanyl radical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with TIMELESS|||LIR 1|||LIR 10|||LIR 11|||LIR 12|||LIR 13|||LIR 2|||LIR 3|||LIR 4|||LIR 5|||LIR 6|||LIR 7|||LIR 8|||LIR 9|||Loss of binding to KL001.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MAPK|||Photolyase/cryptochrome alpha/beta|||Required for inhibition of CLOCK-BMAL1-mediated transcription                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261140
http://togogenome.org/gene/9606:CAPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9S4|||http://purl.uniprot.org/uniprot/P40121|||http://purl.uniprot.org/uniprot/V9HW69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Gelsolin-like|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||In isoform 2.|||Macrophage-capping protein|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218753|||http://purl.uniprot.org/annotation/VAR_047776|||http://purl.uniprot.org/annotation/VAR_047777|||http://purl.uniprot.org/annotation/VAR_047778|||http://purl.uniprot.org/annotation/VSP_045538
http://togogenome.org/gene/9606:SET                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J8YYJ1|||http://purl.uniprot.org/uniprot/Q01105|||http://purl.uniprot.org/uniprot/Q5VXV3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Breakpoint for translocation to form SET-CAN oncogene|||Dimerization|||Disordered|||Earmuff domain|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In MRD58.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N,N,N-trimethylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Protein SET|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185662|||http://purl.uniprot.org/annotation/VAR_078653|||http://purl.uniprot.org/annotation/VAR_081147|||http://purl.uniprot.org/annotation/VAR_081148|||http://purl.uniprot.org/annotation/VAR_082865|||http://purl.uniprot.org/annotation/VSP_009868|||http://purl.uniprot.org/annotation/VSP_045175|||http://purl.uniprot.org/annotation/VSP_046741
http://togogenome.org/gene/9606:DLG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFT3|||http://purl.uniprot.org/uniprot/A0A590UJ08|||http://purl.uniprot.org/uniprot/B4DF78|||http://purl.uniprot.org/uniprot/Q12959                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disks large homolog 1|||Disordered|||Guanylate kinase-like|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 9.|||In isoform 8 and isoform 9.|||In isoform 9.|||Interaction with SH3 domains|||L27|||Loss of membrane association and DLG2-binding.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for interaction with MARCHF2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094548|||http://purl.uniprot.org/annotation/VAR_054334|||http://purl.uniprot.org/annotation/VAR_054335|||http://purl.uniprot.org/annotation/VAR_054336|||http://purl.uniprot.org/annotation/VSP_003150|||http://purl.uniprot.org/annotation/VSP_012862|||http://purl.uniprot.org/annotation/VSP_012863|||http://purl.uniprot.org/annotation/VSP_012864|||http://purl.uniprot.org/annotation/VSP_012865|||http://purl.uniprot.org/annotation/VSP_045896|||http://purl.uniprot.org/annotation/VSP_045897|||http://purl.uniprot.org/annotation/VSP_045898
http://togogenome.org/gene/9606:SMAD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KYA8|||http://purl.uniprot.org/uniprot/O15105                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  90% reduction in TGF-beta receptor binding.|||Diminishes interaction with SMURF2 and reduces inhibition of TGF-beta signaling.|||Diminishes interaction with SMURF2.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Important for interaction with SMURF2|||In isoform 2.|||In isoform 3.|||Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-64.|||Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-70.|||MH1|||MH2|||Mothers against decapentaplegic homolog 7|||N6-acetyllysine; alternate|||PY-motif|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090872|||http://purl.uniprot.org/annotation/VSP_045197|||http://purl.uniprot.org/annotation/VSP_047540
http://togogenome.org/gene/9606:HSPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54652                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methylation by METTL21A.|||Disordered|||Heat shock-related 70 kDa protein 2|||N6,N6,N6-trimethyllysine; by METTL21A; in vitro|||Nucleotide-binding domain (NBD)|||Phosphoserine|||Phosphothreonine|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078258|||http://purl.uniprot.org/annotation/VAR_032706|||http://purl.uniprot.org/annotation/VAR_032707
http://togogenome.org/gene/9606:DPH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Diphthine methyltransferase|||Disordered|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050906|||http://purl.uniprot.org/annotation/VAR_053437
http://togogenome.org/gene/9606:FOSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15408|||http://purl.uniprot.org/uniprot/Q9H5M2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||Disordered|||Fos-related antigen 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076483|||http://purl.uniprot.org/annotation/VSP_039127|||http://purl.uniprot.org/annotation/VSP_039128|||http://purl.uniprot.org/annotation/VSP_039129|||http://purl.uniprot.org/annotation/VSP_042083
http://togogenome.org/gene/9606:EXPH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1U8|||http://purl.uniprot.org/uniprot/B4E2C3|||http://purl.uniprot.org/uniprot/Q149M6|||http://purl.uniprot.org/uniprot/Q6AI59|||http://purl.uniprot.org/uniprot/Q8NEV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Exophilin-5|||In isoform 2.|||Phosphoserine|||Polar residues|||RabBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190230|||http://purl.uniprot.org/annotation/VAR_030538|||http://purl.uniprot.org/annotation/VAR_030539|||http://purl.uniprot.org/annotation/VAR_030540|||http://purl.uniprot.org/annotation/VAR_030541|||http://purl.uniprot.org/annotation/VAR_030542|||http://purl.uniprot.org/annotation/VAR_030543|||http://purl.uniprot.org/annotation/VAR_030544|||http://purl.uniprot.org/annotation/VAR_030545|||http://purl.uniprot.org/annotation/VAR_030546|||http://purl.uniprot.org/annotation/VAR_030547|||http://purl.uniprot.org/annotation/VAR_030548|||http://purl.uniprot.org/annotation/VAR_030549|||http://purl.uniprot.org/annotation/VAR_030550|||http://purl.uniprot.org/annotation/VAR_030551|||http://purl.uniprot.org/annotation/VAR_030552|||http://purl.uniprot.org/annotation/VAR_057117|||http://purl.uniprot.org/annotation/VAR_057118|||http://purl.uniprot.org/annotation/VAR_057119|||http://purl.uniprot.org/annotation/VAR_057120|||http://purl.uniprot.org/annotation/VAR_057121|||http://purl.uniprot.org/annotation/VSP_007906
http://togogenome.org/gene/9606:PPAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4H7|||http://purl.uniprot.org/uniprot/Q06203|||http://purl.uniprot.org/uniprot/Q59G63                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Amidophosphoribosyltransferase|||Glutamine amidotransferase type-2|||Helical|||N-acetylmethionine|||Nucleophile|||Phosphoribosyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029283|||http://purl.uniprot.org/annotation/PRO_0000029284
http://togogenome.org/gene/9606:RTL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L3V2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BH3|||Disordered|||No effect on interaction with VDAC1.|||Protein Bop|||Reduces the pro-apoptotic activity and interaction with VDAC1.|||Reduces the pro-apoptotic activity, no effect on interaction with VDAC1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295910|||http://purl.uniprot.org/annotation/VAR_034590|||http://purl.uniprot.org/annotation/VAR_034591
http://togogenome.org/gene/9606:MRPS18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVS2                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein mL66|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030625|||http://purl.uniprot.org/annotation/VSP_041245|||http://purl.uniprot.org/annotation/VSP_043496
http://togogenome.org/gene/9606:TMCO5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R9I9|||http://purl.uniprot.org/uniprot/Q8N6Q1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane and coiled-coil domain-containing protein 5A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305153|||http://purl.uniprot.org/annotation/VSP_028246|||http://purl.uniprot.org/annotation/VSP_028247
http://togogenome.org/gene/9606:TSPY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKD2                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Testis-specific Y-encoded protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333197
http://togogenome.org/gene/9606:ELOVL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Di-lysine motif|||Disordered|||Elongation of very long chain fatty acids protein 4|||Helical|||In SCA34.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207542|||http://purl.uniprot.org/annotation/VAR_012492|||http://purl.uniprot.org/annotation/VAR_017043|||http://purl.uniprot.org/annotation/VAR_072565
http://togogenome.org/gene/9606:CCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14618                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Copper chaperone for superoxide dismutase|||Found in a patient with congenital cataracts, hearing loss, neurodegeneration, neonatal hypotonia and hypoglycemia, pericardial effusion and neurodevelopmental regression after infection; the patient also carries a mutation in SLC33A1; mutant protein does not interact with SOD1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HMA|||Phosphoserine|||Reduces copper binding by half; when associated with S-22. Negligible effect on zinc binding.|||Reduces copper binding by half; when associated with S-244. Negligible effect on zinc binding.|||Reduces copper binding by half; when associated with S-246. Negligible effect on zinc binding.|||Reduces copper binding by half; when associated with S-25. Negligible effect on zinc binding.|||Superoxide dismutase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213543|||http://purl.uniprot.org/annotation/VAR_068078
http://togogenome.org/gene/9606:WDR43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15061                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051392
http://togogenome.org/gene/9606:RASL10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92737                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||Ras-like protein family member 10A|||Removed in mature form|||S-farnesyl cysteine|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082706|||http://purl.uniprot.org/annotation/PRO_0000281360|||http://purl.uniprot.org/annotation/VSP_013372
http://togogenome.org/gene/9606:GTF3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92664                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||Transcription factor IIIA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047080|||http://purl.uniprot.org/annotation/VAR_014824|||http://purl.uniprot.org/annotation/VSP_031525|||http://purl.uniprot.org/annotation/VSP_031526
http://togogenome.org/gene/9606:SRSF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16629                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||4|||5; approximate|||6 X 8 AA repeats of R-R-S-R-S-X-S-X|||6; approximate|||Abolishes interaction with NXF1.|||Basic residues|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||RRM|||Serine/arginine-rich splicing factor 7|||Sufficient for interaction with NXF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081932|||http://purl.uniprot.org/annotation/VSP_005872|||http://purl.uniprot.org/annotation/VSP_005873|||http://purl.uniprot.org/annotation/VSP_005874|||http://purl.uniprot.org/annotation/VSP_005875|||http://purl.uniprot.org/annotation/VSP_045840
http://togogenome.org/gene/9606:TYR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L8B082|||http://purl.uniprot.org/uniprot/P14679                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with SHEP3; light/dark skin.|||Cytoplasmic|||Disordered|||Helical|||In OCA-I.|||In OCA1.|||In OCA1A and OCA1B.|||In OCA1A and OCA1B; temperature sensitive variant.|||In OCA1A.|||In OCA1B and OCA1A.|||In OCA1B.|||In isoform 2.|||Lumenal, melanosome|||N-linked (GlcNAc...) asparagine|||Tyrosinase|||Tyrosinase copper-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035879|||http://purl.uniprot.org/annotation/PRO_5014306177|||http://purl.uniprot.org/annotation/VAR_007649|||http://purl.uniprot.org/annotation/VAR_007650|||http://purl.uniprot.org/annotation/VAR_007651|||http://purl.uniprot.org/annotation/VAR_007652|||http://purl.uniprot.org/annotation/VAR_007653|||http://purl.uniprot.org/annotation/VAR_007654|||http://purl.uniprot.org/annotation/VAR_007655|||http://purl.uniprot.org/annotation/VAR_007656|||http://purl.uniprot.org/annotation/VAR_007657|||http://purl.uniprot.org/annotation/VAR_007658|||http://purl.uniprot.org/annotation/VAR_007659|||http://purl.uniprot.org/annotation/VAR_007660|||http://purl.uniprot.org/annotation/VAR_007661|||http://purl.uniprot.org/annotation/VAR_007662|||http://purl.uniprot.org/annotation/VAR_007663|||http://purl.uniprot.org/annotation/VAR_007664|||http://purl.uniprot.org/annotation/VAR_007665|||http://purl.uniprot.org/annotation/VAR_007666|||http://purl.uniprot.org/annotation/VAR_007667|||http://purl.uniprot.org/annotation/VAR_007668|||http://purl.uniprot.org/annotation/VAR_007669|||http://purl.uniprot.org/annotation/VAR_007670|||http://purl.uniprot.org/annotation/VAR_007671|||http://purl.uniprot.org/annotation/VAR_007672|||http://purl.uniprot.org/annotation/VAR_007673|||http://purl.uniprot.org/annotation/VAR_007674|||http://purl.uniprot.org/annotation/VAR_007675|||http://purl.uniprot.org/annotation/VAR_007676|||http://purl.uniprot.org/annotation/VAR_007677|||http://purl.uniprot.org/annotation/VAR_007678|||http://purl.uniprot.org/annotation/VAR_007679|||http://purl.uniprot.org/annotation/VAR_007680|||http://purl.uniprot.org/annotation/VAR_007681|||http://purl.uniprot.org/annotation/VAR_007682|||http://purl.uniprot.org/annotation/VAR_007683|||http://purl.uniprot.org/annotation/VAR_007684|||http://purl.uniprot.org/annotation/VAR_007685|||http://purl.uniprot.org/annotation/VAR_007686|||http://purl.uniprot.org/annotation/VAR_007687|||http://purl.uniprot.org/annotation/VAR_007688|||http://purl.uniprot.org/annotation/VAR_007689|||http://purl.uniprot.org/annotation/VAR_007690|||http://purl.uniprot.org/annotation/VAR_007691|||http://purl.uniprot.org/annotation/VAR_007692|||http://purl.uniprot.org/annotation/VAR_007693|||http://purl.uniprot.org/annotation/VAR_007925|||http://purl.uniprot.org/annotation/VAR_007926|||http://purl.uniprot.org/annotation/VAR_007927|||http://purl.uniprot.org/annotation/VAR_007928|||http://purl.uniprot.org/annotation/VAR_007929|||http://purl.uniprot.org/annotation/VAR_007930|||http://purl.uniprot.org/annotation/VAR_007931|||http://purl.uniprot.org/annotation/VAR_007932|||http://purl.uniprot.org/annotation/VAR_007933|||http://purl.uniprot.org/annotation/VAR_007934|||http://purl.uniprot.org/annotation/VAR_007935|||http://purl.uniprot.org/annotation/VAR_007936|||http://purl.uniprot.org/annotation/VAR_007937|||http://purl.uniprot.org/annotation/VAR_007938|||http://purl.uniprot.org/annotation/VAR_009236|||http://purl.uniprot.org/annotation/VAR_009237|||http://purl.uniprot.org/annotation/VAR_009238|||http://purl.uniprot.org/annotation/VAR_011825|||http://purl.uniprot.org/annotation/VAR_021683|||http://purl.uniprot.org/annotation/VAR_021684|||http://purl.uniprot.org/annotation/VAR_021685|||http://purl.uniprot.org/annotation/VAR_021686|||http://purl.uniprot.org/annotation/VAR_021687|||http://purl.uniprot.org/annotation/VAR_021688|||http://purl.uniprot.org/annotation/VAR_021689|||http://purl.uniprot.org/annotation/VAR_021690|||http://purl.uniprot.org/annotation/VAR_021691|||http://purl.uniprot.org/annotation/VAR_021692|||http://purl.uniprot.org/annotation/VAR_021693|||http://purl.uniprot.org/annotation/VAR_021694|||http://purl.uniprot.org/annotation/VAR_021695|||http://purl.uniprot.org/annotation/VAR_021696|||http://purl.uniprot.org/annotation/VAR_021697|||http://purl.uniprot.org/annotation/VAR_021698|||http://purl.uniprot.org/annotation/VAR_021699|||http://purl.uniprot.org/annotation/VAR_021700|||http://purl.uniprot.org/annotation/VAR_021701|||http://purl.uniprot.org/annotation/VAR_021702|||http://purl.uniprot.org/annotation/VAR_021703|||http://purl.uniprot.org/annotation/VAR_021704|||http://purl.uniprot.org/annotation/VAR_021705|||http://purl.uniprot.org/annotation/VAR_021706|||http://purl.uniprot.org/annotation/VAR_021707|||http://purl.uniprot.org/annotation/VAR_021708|||http://purl.uniprot.org/annotation/VAR_021709|||http://purl.uniprot.org/annotation/VAR_021710|||http://purl.uniprot.org/annotation/VAR_021711|||http://purl.uniprot.org/annotation/VAR_021712|||http://purl.uniprot.org/annotation/VAR_021713|||http://purl.uniprot.org/annotation/VAR_021714|||http://purl.uniprot.org/annotation/VAR_021715|||http://purl.uniprot.org/annotation/VAR_021716|||http://purl.uniprot.org/annotation/VAR_021717|||http://purl.uniprot.org/annotation/VAR_021718|||http://purl.uniprot.org/annotation/VAR_021719|||http://purl.uniprot.org/annotation/VAR_021720|||http://purl.uniprot.org/annotation/VAR_021721|||http://purl.uniprot.org/annotation/VAR_021722|||http://purl.uniprot.org/annotation/VAR_021723|||http://purl.uniprot.org/annotation/VAR_021724|||http://purl.uniprot.org/annotation/VAR_021725|||http://purl.uniprot.org/annotation/VAR_021726|||http://purl.uniprot.org/annotation/VAR_021727|||http://purl.uniprot.org/annotation/VAR_021728|||http://purl.uniprot.org/annotation/VAR_034576|||http://purl.uniprot.org/annotation/VAR_042665|||http://purl.uniprot.org/annotation/VAR_071756|||http://purl.uniprot.org/annotation/VAR_072592|||http://purl.uniprot.org/annotation/VAR_072593|||http://purl.uniprot.org/annotation/VAR_072594|||http://purl.uniprot.org/annotation/VAR_072595|||http://purl.uniprot.org/annotation/VAR_072596|||http://purl.uniprot.org/annotation/VAR_072597|||http://purl.uniprot.org/annotation/VAR_072598|||http://purl.uniprot.org/annotation/VSP_006701|||http://purl.uniprot.org/annotation/VSP_006702
http://togogenome.org/gene/9606:CDK2AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14519                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase 2-associated protein 1|||Does not alter homodimerization.|||In isoform 2.|||Interaction with CDK2AP2|||Interchain|||Phosphoserine; by IKKE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089452|||http://purl.uniprot.org/annotation/VSP_046436
http://togogenome.org/gene/9606:OSCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVF1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Protein OSCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251965|||http://purl.uniprot.org/annotation/VAR_027741|||http://purl.uniprot.org/annotation/VAR_027742|||http://purl.uniprot.org/annotation/VAR_056958|||http://purl.uniprot.org/annotation/VSP_020826|||http://purl.uniprot.org/annotation/VSP_039475|||http://purl.uniprot.org/annotation/VSP_039476|||http://purl.uniprot.org/annotation/VSP_039477
http://togogenome.org/gene/9606:TIMM17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99595                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Mitochondrial import inner membrane translocase subunit Tim17-A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210284|||http://purl.uniprot.org/annotation/VAR_052305
http://togogenome.org/gene/9606:NFYB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VSL3|||http://purl.uniprot.org/uniprot/P25208                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  A domain|||B domain|||Basic and acidic residues|||C domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Nuclear transcription factor Y subunit beta|||Subunit association domain (SAD)|||Transcription factor CBF/NF-Y/archaeal histone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204609
http://togogenome.org/gene/9606:COL6A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8TX70|||http://purl.uniprot.org/uniprot/H0Y393                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Collagen alpha-5(VI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||Polar residues|||Triple-helical region|||VWFA|||VWFA 1|||VWFA 10|||VWFA 2|||VWFA 3|||VWFA 4|||VWFA 5|||VWFA 6|||VWFA 7|||VWFA 8|||VWFA 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000294475|||http://purl.uniprot.org/annotation/PRO_5036499409|||http://purl.uniprot.org/annotation/VAR_043607|||http://purl.uniprot.org/annotation/VAR_043608|||http://purl.uniprot.org/annotation/VAR_059234|||http://purl.uniprot.org/annotation/VAR_059235|||http://purl.uniprot.org/annotation/VAR_059236|||http://purl.uniprot.org/annotation/VAR_059237|||http://purl.uniprot.org/annotation/VAR_059238|||http://purl.uniprot.org/annotation/VAR_059239|||http://purl.uniprot.org/annotation/VAR_059240|||http://purl.uniprot.org/annotation/VAR_059241|||http://purl.uniprot.org/annotation/VAR_061119|||http://purl.uniprot.org/annotation/VSP_033912|||http://purl.uniprot.org/annotation/VSP_033913
http://togogenome.org/gene/9606:IMPDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRZ3|||http://purl.uniprot.org/uniprot/P20839|||http://purl.uniprot.org/uniprot/Q6ZNB1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CBS|||CBS 1|||CBS 2|||Disordered|||Does not alter the enzymatic affinity of the corresponding enzyme; does not affect the affinity for single-stranded nucleic acid.|||In LCA11; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid.|||In RP10.|||In RP10; alters the affinity and/or the specificity of single-stranded nucleic acid.|||In RP10; does not alter the enzymatic affinity of the corresponding enzyme; alters the affinity and/or the specificity of single-stranded nucleic acid.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Inosine-5'-monophosphate dehydrogenase 1|||Omega-N-methylarginine|||Phosphoserine|||Proton acceptor|||Removed|||Thioimidate intermediate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093670|||http://purl.uniprot.org/annotation/VAR_017031|||http://purl.uniprot.org/annotation/VAR_017032|||http://purl.uniprot.org/annotation/VAR_017033|||http://purl.uniprot.org/annotation/VAR_065616|||http://purl.uniprot.org/annotation/VAR_065617|||http://purl.uniprot.org/annotation/VAR_065618|||http://purl.uniprot.org/annotation/VAR_065619|||http://purl.uniprot.org/annotation/VAR_065620|||http://purl.uniprot.org/annotation/VAR_065621|||http://purl.uniprot.org/annotation/VSP_002674|||http://purl.uniprot.org/annotation/VSP_014363|||http://purl.uniprot.org/annotation/VSP_043485|||http://purl.uniprot.org/annotation/VSP_046968|||http://purl.uniprot.org/annotation/VSP_046969|||http://purl.uniprot.org/annotation/VSP_046970
http://togogenome.org/gene/9606:SLC24A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI40                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Loss of N-glycosylation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sodium/potassium/calcium exchanger 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019367|||http://purl.uniprot.org/annotation/VSP_006164
http://togogenome.org/gene/9606:MAML3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JK9|||http://purl.uniprot.org/uniprot/Q9NPV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Mastermind-like protein 3|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129496|||http://purl.uniprot.org/annotation/VAR_046650
http://togogenome.org/gene/9606:MFHAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4C4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Breakpoint for translocation to form chimeric MASL1|||Dominant negative effect on the ERK1/ERK2 signaling pathway and EPO-induced erythroid differentiation.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of GTP-binding.|||Malignant fibrous histiocytoma-amplified sequence 1|||N-acetylalanine|||N6-acetyllysine|||Removed|||Required for interaction with PJA2|||Required for interaction with PPP2R2A|||Roc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308609|||http://purl.uniprot.org/annotation/VAR_036846|||http://purl.uniprot.org/annotation/VAR_036847
http://togogenome.org/gene/9606:TEAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15562                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Pro residues|||TEA|||Transcriptional activation|||Transcriptional enhancer factor TEF-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205932|||http://purl.uniprot.org/annotation/VSP_045126|||http://purl.uniprot.org/annotation/VSP_045127|||http://purl.uniprot.org/annotation/VSP_055673
http://togogenome.org/gene/9606:ANKRD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UB99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 11|||Basic and acidic residues|||Basic residues|||Disordered|||Important for protein degradation|||In KBGS; unknown pathological significance.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066907|||http://purl.uniprot.org/annotation/VAR_075870
http://togogenome.org/gene/9606:PPEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXD3|||http://purl.uniprot.org/uniprot/O14829                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Catalytic|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||IQ|||In isoform 1A.|||In isoform 1B.|||In isoform 2.|||In isoform 3.|||Proton donor|||Serine/threonine-protein phosphatase with EF-hands 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058899|||http://purl.uniprot.org/annotation/VAR_051736|||http://purl.uniprot.org/annotation/VAR_051737|||http://purl.uniprot.org/annotation/VSP_005098|||http://purl.uniprot.org/annotation/VSP_005099|||http://purl.uniprot.org/annotation/VSP_005100|||http://purl.uniprot.org/annotation/VSP_005101|||http://purl.uniprot.org/annotation/VSP_005102
http://togogenome.org/gene/9606:ELAPOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MWY0|||http://purl.uniprot.org/uniprot/B4E116                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endosome/lysosome-associated apoptosis and autophagy regulator family member 2|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||MRH|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333798|||http://purl.uniprot.org/annotation/VAR_043161|||http://purl.uniprot.org/annotation/VAR_043162|||http://purl.uniprot.org/annotation/VAR_043163|||http://purl.uniprot.org/annotation/VSP_033529|||http://purl.uniprot.org/annotation/VSP_033530|||http://purl.uniprot.org/annotation/VSP_043254|||http://purl.uniprot.org/annotation/VSP_043255
http://togogenome.org/gene/9606:ZNF544                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL50|||http://purl.uniprot.org/uniprot/B7ZAY1|||http://purl.uniprot.org/uniprot/J3KQC8|||http://purl.uniprot.org/uniprot/M0QZM7|||http://purl.uniprot.org/uniprot/M0R2F0|||http://purl.uniprot.org/uniprot/Q6NX49                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 544                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047643|||http://purl.uniprot.org/annotation/VAR_052859|||http://purl.uniprot.org/annotation/VAR_052860
http://togogenome.org/gene/9606:IL1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01584                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; S.pyogenes SpeB|||Enhanced integrin binding.|||Important for interaction with integrin|||Increased affinity for integrin ITGAV:ITGB3. Suppression of integrin binding; when associated with E-171; E-190 or E-204. Suppression of integrin binding; when associated with E-179 and E-181.|||Interleukin-1 beta|||Involved in interaction with TMED10 C-terminus|||Involved in receptor binding|||Loss of activation by CASP1; when associated with A-116.|||Loss of activation by CASP1; when associated with A-27.|||No effect on binding to IL1R or on IL1B activity. Markedly reduced activity; when associated with E-171; E-190 and E-204. Markedly reduced activity; when associated with E-179; E-181; E-190 and E-204.|||Promotes release of IL1B precursors through the Gasdermin-D (GSDMD) ring-shaped pore complex.|||Removed in mature form; by CASP1|||Requires 2 nucleotide substitutions.|||Suppression of integrin binding; when associated with E-179 and K-244. Markedly reduced activity; when associated with E-179; E-190; E-204 and C-233.|||Suppression of integrin binding; when associated with E-181 and K-244. Markedly reduced activity; when associated with E-181; E-190; E-204 and C-233.|||Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-171; E-190 and C-233. Markedly reduced activity; when associated with E-179; E-181; E-190 and C-233.|||Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-171; E-204 and C-233. Markedly reduced activity; when associated with E-179; E-181; E-204 and C-233.|||Suppression of integrin binding; when associated with K-244. Markedly reduced activity; when associated with E-190; E-204 and C-233.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015301|||http://purl.uniprot.org/annotation/PRO_0000015302|||http://purl.uniprot.org/annotation/VAR_073951
http://togogenome.org/gene/9606:SST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61278                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Alanine amide|||Disordered|||Neuronostatin|||Somatostatin-14|||Somatostatin-28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033086|||http://purl.uniprot.org/annotation/PRO_0000033087|||http://purl.uniprot.org/annotation/PRO_0000033088|||http://purl.uniprot.org/annotation/PRO_0000447375|||http://purl.uniprot.org/annotation/VAR_034499|||http://purl.uniprot.org/annotation/VAR_034500
http://togogenome.org/gene/9606:PRRX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJS2|||http://purl.uniprot.org/uniprot/Q99811                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||OAR|||Paired mesoderm homeobox protein 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049255
http://togogenome.org/gene/9606:CNTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L3A3|||http://purl.uniprot.org/uniprot/Q02246                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Cell attachment site|||Contactin-2|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated asparagine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014695|||http://purl.uniprot.org/annotation/PRO_0000014696|||http://purl.uniprot.org/annotation/PRO_5002636455|||http://purl.uniprot.org/annotation/VAR_021918|||http://purl.uniprot.org/annotation/VAR_021919|||http://purl.uniprot.org/annotation/VAR_029129|||http://purl.uniprot.org/annotation/VAR_049867
http://togogenome.org/gene/9606:BIK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13323                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  BH3|||Bcl-2-interacting killer|||Cleavage; by RHBDL4/RHBDD1|||Helical|||Inhibits RHBDL4/RHBDD1-induced cleavage.|||Leucine-zipper                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143100|||http://purl.uniprot.org/annotation/VAR_029179|||http://purl.uniprot.org/annotation/VAR_029180|||http://purl.uniprot.org/annotation/VAR_048420
http://togogenome.org/gene/9606:LHFPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||LHFPL tetraspan subfamily member 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244766
http://togogenome.org/gene/9606:LAMB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3R6|||http://purl.uniprot.org/uniprot/Q13751                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Domain I|||Domain II|||Domain alpha|||In JEB1A.|||In JEB1A; somatic second-site mutation.|||In JEB1B.|||In a colorectal cancer sample; somatic mutation.|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5|||Laminin EGF-like 6|||Laminin N-terminal|||Laminin subunit beta-3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017071|||http://purl.uniprot.org/annotation/PRO_5006608208|||http://purl.uniprot.org/annotation/VAR_004170|||http://purl.uniprot.org/annotation/VAR_004171|||http://purl.uniprot.org/annotation/VAR_034060|||http://purl.uniprot.org/annotation/VAR_034061|||http://purl.uniprot.org/annotation/VAR_034062|||http://purl.uniprot.org/annotation/VAR_034063|||http://purl.uniprot.org/annotation/VAR_035820|||http://purl.uniprot.org/annotation/VAR_037309|||http://purl.uniprot.org/annotation/VAR_037310|||http://purl.uniprot.org/annotation/VAR_037311|||http://purl.uniprot.org/annotation/VAR_037312|||http://purl.uniprot.org/annotation/VAR_037313|||http://purl.uniprot.org/annotation/VAR_037314
http://togogenome.org/gene/9606:GIMAP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8P8|||http://purl.uniprot.org/uniprot/Q8NHV1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  AIG1-type G|||Abolishes GTPase activity. No effect on GTP binding and on dimerization.|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 7|||Impairs dimerization and abolishes GTPase activity. No effect on GTP binding.|||Important for catalytic activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190993|||http://purl.uniprot.org/annotation/VAR_049534
http://togogenome.org/gene/9606:FOXD4L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SYB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4-like 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301979
http://togogenome.org/gene/9606:PABPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13310                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N6,N6-dimethyllysine; alternate|||Omega-N-methylarginine|||PABC|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polyadenylate-binding protein 4|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081703|||http://purl.uniprot.org/annotation/VAR_054048|||http://purl.uniprot.org/annotation/VSP_013335|||http://purl.uniprot.org/annotation/VSP_043357
http://togogenome.org/gene/9606:IL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15248                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Interleukin-9|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015627|||http://purl.uniprot.org/annotation/VAR_013079
http://togogenome.org/gene/9606:PADI6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6TGC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In OZEMA16.|||Phosphoserine|||Protein-arginine deiminase type-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220036|||http://purl.uniprot.org/annotation/VAR_078106|||http://purl.uniprot.org/annotation/VAR_078107
http://togogenome.org/gene/9606:CHST9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L1S5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 9|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189655|||http://purl.uniprot.org/annotation/VAR_055150|||http://purl.uniprot.org/annotation/VAR_079095|||http://purl.uniprot.org/annotation/VSP_043865|||http://purl.uniprot.org/annotation/VSP_043866
http://togogenome.org/gene/9606:USP17L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6R6M4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes both enzymatic activity and effects on cell proliferation.|||Disordered|||Mediates interaction with SUDS3|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331644|||http://purl.uniprot.org/annotation/VAR_059750
http://togogenome.org/gene/9606:CYP7B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75881|||http://purl.uniprot.org/uniprot/Q05C57                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 7B1|||Disordered|||Helical|||In SPG5A.|||In SPG5A; unknown pathological significance.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051906|||http://purl.uniprot.org/annotation/VAR_044382|||http://purl.uniprot.org/annotation/VAR_044383|||http://purl.uniprot.org/annotation/VAR_044384|||http://purl.uniprot.org/annotation/VAR_044385|||http://purl.uniprot.org/annotation/VAR_075505|||http://purl.uniprot.org/annotation/VAR_075506|||http://purl.uniprot.org/annotation/VAR_075507|||http://purl.uniprot.org/annotation/VAR_075508|||http://purl.uniprot.org/annotation/VAR_075509|||http://purl.uniprot.org/annotation/VAR_075510|||http://purl.uniprot.org/annotation/VAR_075511|||http://purl.uniprot.org/annotation/VAR_075512|||http://purl.uniprot.org/annotation/VAR_075513|||http://purl.uniprot.org/annotation/VAR_075514|||http://purl.uniprot.org/annotation/VAR_075515|||http://purl.uniprot.org/annotation/VAR_075516|||http://purl.uniprot.org/annotation/VAR_075517|||http://purl.uniprot.org/annotation/VAR_075518
http://togogenome.org/gene/9606:USP43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70EL4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Phosphoserine|||Polar residues|||Pro residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249521|||http://purl.uniprot.org/annotation/VSP_020466|||http://purl.uniprot.org/annotation/VSP_020467|||http://purl.uniprot.org/annotation/VSP_020468|||http://purl.uniprot.org/annotation/VSP_046779
http://togogenome.org/gene/9606:TOR1AIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFQ8|||http://purl.uniprot.org/uniprot/Q9H496                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Interaction with TOR1A|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Torsin-1A-interacting protein 2|||Torsin-1A-interacting protein 2, isoform IFRG15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228838|||http://purl.uniprot.org/annotation/PRO_0000421071
http://togogenome.org/gene/9606:COL3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02461                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||5-hydroxylysine; alternate|||C-terminal propeptide|||Collagen alpha-1(III) chain|||Disordered|||Fibrillar collagen NC1|||In EDSVASC.|||In EDSVASC; Gottron type acrogeria.|||In EDSVASC; mild variant.|||In EDSVASC; requires 2 nucleotide substitutions.|||In EDSVASC; severe variant.|||In EDSVASC; severe.|||In PMGEDSV.|||In PMGEDSV; does not affect interaction with ADGRG1.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In spondyloepiphyseal dysplasia.|||Interchain|||Interchain (with C-1268)|||Interchain (with C-1285)|||N-terminal propeptide|||Nonhelical region (C-terminal)|||Nonhelical region (N-terminal)|||O-linked (Gal...) hydroxylysine; alternate|||Pro residues|||Triple-helical region|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005740|||http://purl.uniprot.org/annotation/PRO_0000005741|||http://purl.uniprot.org/annotation/PRO_0000005742|||http://purl.uniprot.org/annotation/VAR_001767|||http://purl.uniprot.org/annotation/VAR_001768|||http://purl.uniprot.org/annotation/VAR_001769|||http://purl.uniprot.org/annotation/VAR_001770|||http://purl.uniprot.org/annotation/VAR_001771|||http://purl.uniprot.org/annotation/VAR_001772|||http://purl.uniprot.org/annotation/VAR_001773|||http://purl.uniprot.org/annotation/VAR_001774|||http://purl.uniprot.org/annotation/VAR_001775|||http://purl.uniprot.org/annotation/VAR_001776|||http://purl.uniprot.org/annotation/VAR_001777|||http://purl.uniprot.org/annotation/VAR_001778|||http://purl.uniprot.org/annotation/VAR_001779|||http://purl.uniprot.org/annotation/VAR_001780|||http://purl.uniprot.org/annotation/VAR_001781|||http://purl.uniprot.org/annotation/VAR_001782|||http://purl.uniprot.org/annotation/VAR_001783|||http://purl.uniprot.org/annotation/VAR_001784|||http://purl.uniprot.org/annotation/VAR_001785|||http://purl.uniprot.org/annotation/VAR_001786|||http://purl.uniprot.org/annotation/VAR_001787|||http://purl.uniprot.org/annotation/VAR_001788|||http://purl.uniprot.org/annotation/VAR_001789|||http://purl.uniprot.org/annotation/VAR_001790|||http://purl.uniprot.org/annotation/VAR_001791|||http://purl.uniprot.org/annotation/VAR_001792|||http://purl.uniprot.org/annotation/VAR_001793|||http://purl.uniprot.org/annotation/VAR_001794|||http://purl.uniprot.org/annotation/VAR_001795|||http://purl.uniprot.org/annotation/VAR_001796|||http://purl.uniprot.org/annotation/VAR_001797|||http://purl.uniprot.org/annotation/VAR_001798|||http://purl.uniprot.org/annotation/VAR_001799|||http://purl.uniprot.org/annotation/VAR_001800|||http://purl.uniprot.org/annotation/VAR_001801|||http://purl.uniprot.org/annotation/VAR_001802|||http://purl.uniprot.org/annotation/VAR_001803|||http://purl.uniprot.org/annotation/VAR_001804|||http://purl.uniprot.org/annotation/VAR_001805|||http://purl.uniprot.org/annotation/VAR_001806|||http://purl.uniprot.org/annotation/VAR_001807|||http://purl.uniprot.org/annotation/VAR_011095|||http://purl.uniprot.org/annotation/VAR_011096|||http://purl.uniprot.org/annotation/VAR_011097|||http://purl.uniprot.org/annotation/VAR_011098|||http://purl.uniprot.org/annotation/VAR_011099|||http://purl.uniprot.org/annotation/VAR_011100|||http://purl.uniprot.org/annotation/VAR_011101|||http://purl.uniprot.org/annotation/VAR_011102|||http://purl.uniprot.org/annotation/VAR_011103|||http://purl.uniprot.org/annotation/VAR_011104|||http://purl.uniprot.org/annotation/VAR_011105|||http://purl.uniprot.org/annotation/VAR_011106|||http://purl.uniprot.org/annotation/VAR_011107|||http://purl.uniprot.org/annotation/VAR_011108|||http://purl.uniprot.org/annotation/VAR_011109|||http://purl.uniprot.org/annotation/VAR_011110|||http://purl.uniprot.org/annotation/VAR_011111|||http://purl.uniprot.org/annotation/VAR_011112|||http://purl.uniprot.org/annotation/VAR_011113|||http://purl.uniprot.org/annotation/VAR_011114|||http://purl.uniprot.org/annotation/VAR_011115|||http://purl.uniprot.org/annotation/VAR_011116|||http://purl.uniprot.org/annotation/VAR_011117|||http://purl.uniprot.org/annotation/VAR_011118|||http://purl.uniprot.org/annotation/VAR_011119|||http://purl.uniprot.org/annotation/VAR_011120|||http://purl.uniprot.org/annotation/VAR_011121|||http://purl.uniprot.org/annotation/VAR_011122|||http://purl.uniprot.org/annotation/VAR_011123|||http://purl.uniprot.org/annotation/VAR_011124|||http://purl.uniprot.org/annotation/VAR_011125|||http://purl.uniprot.org/annotation/VAR_011126|||http://purl.uniprot.org/annotation/VAR_011127|||http://purl.uniprot.org/annotation/VAR_011128|||http://purl.uniprot.org/annotation/VAR_011129|||http://purl.uniprot.org/annotation/VAR_011130|||http://purl.uniprot.org/annotation/VAR_011131|||http://purl.uniprot.org/annotation/VAR_011132|||http://purl.uniprot.org/annotation/VAR_011133|||http://purl.uniprot.org/annotation/VAR_011134|||http://purl.uniprot.org/annotation/VAR_011135|||http://purl.uniprot.org/annotation/VAR_011136|||http://purl.uniprot.org/annotation/VAR_011137|||http://purl.uniprot.org/annotation/VAR_011138|||http://purl.uniprot.org/annotation/VAR_011139|||http://purl.uniprot.org/annotation/VAR_011140|||http://purl.uniprot.org/annotation/VAR_011141|||http://purl.uniprot.org/annotation/VAR_011142|||http://purl.uniprot.org/annotation/VAR_011143|||http://purl.uniprot.org/annotation/VAR_011144|||http://purl.uniprot.org/annotation/VAR_011145|||http://purl.uniprot.org/annotation/VAR_011146|||http://purl.uniprot.org/annotation/VAR_011147|||http://purl.uniprot.org/annotation/VAR_011148|||http://purl.uniprot.org/annotation/VAR_011149|||http://purl.uniprot.org/annotation/VAR_011150|||http://purl.uniprot.org/annotation/VAR_011151|||http://purl.uniprot.org/annotation/VAR_011152|||http://purl.uniprot.org/annotation/VAR_011153|||http://purl.uniprot.org/annotation/VAR_011154|||http://purl.uniprot.org/annotation/VAR_011155|||http://purl.uniprot.org/annotation/VAR_011156|||http://purl.uniprot.org/annotation/VAR_011157|||http://purl.uniprot.org/annotation/VAR_011158|||http://purl.uniprot.org/annotation/VAR_011159|||http://purl.uniprot.org/annotation/VAR_020012|||http://purl.uniprot.org/annotation/VAR_030115|||http://purl.uniprot.org/annotation/VAR_035738|||http://purl.uniprot.org/annotation/VAR_035739|||http://purl.uniprot.org/annotation/VAR_037007|||http://purl.uniprot.org/annotation/VAR_037008|||http://purl.uniprot.org/annotation/VAR_055665|||http://purl.uniprot.org/annotation/VAR_055666|||http://purl.uniprot.org/annotation/VAR_055667|||http://purl.uniprot.org/annotation/VAR_082043|||http://purl.uniprot.org/annotation/VAR_082044|||http://purl.uniprot.org/annotation/VAR_082045|||http://purl.uniprot.org/annotation/VAR_082046|||http://purl.uniprot.org/annotation/VSP_022502
http://togogenome.org/gene/9606:C1orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LT6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  UPF0739 protein C1orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271092|||http://purl.uniprot.org/annotation/VAR_050701
http://togogenome.org/gene/9606:YWHAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61981                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  14-3-3 protein gamma|||14-3-3 protein gamma, N-terminally processed|||Found in an individual with autism; unknown pathological significance.|||In DEE56.|||In DEE56; unknown pathological significance.|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine; in 14-3-3 protein gamma; alternate; partial|||N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed; partial|||N-acetylvaline; partial|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Probable disease-associated variant found in an individual with neurodevelopmental disorder.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058606|||http://purl.uniprot.org/annotation/PRO_0000367907|||http://purl.uniprot.org/annotation/VAR_080224|||http://purl.uniprot.org/annotation/VAR_080225|||http://purl.uniprot.org/annotation/VAR_080226|||http://purl.uniprot.org/annotation/VAR_080227|||http://purl.uniprot.org/annotation/VAR_080228
http://togogenome.org/gene/9606:VSNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62760                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Removed|||Visinin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073763|||http://purl.uniprot.org/annotation/VAR_047313|||http://purl.uniprot.org/annotation/VAR_047314
http://togogenome.org/gene/9606:NRBF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreased interaction with nuclear receptors.|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear receptor interaction motif|||Nuclear receptor-binding factor 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235816|||http://purl.uniprot.org/annotation/VSP_018488|||http://purl.uniprot.org/annotation/VSP_054555
http://togogenome.org/gene/9606:GDPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5L3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GP-PDE|||Helical|||In isoform 2.|||Lysophospholipase D GDPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251936|||http://purl.uniprot.org/annotation/VSP_036888
http://togogenome.org/gene/9606:KAT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8E8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine-rich protein 2-binding protein|||Disordered|||In isoform 2.|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074603|||http://purl.uniprot.org/annotation/VAR_020466|||http://purl.uniprot.org/annotation/VAR_028034|||http://purl.uniprot.org/annotation/VAR_028035|||http://purl.uniprot.org/annotation/VAR_033839|||http://purl.uniprot.org/annotation/VAR_048166|||http://purl.uniprot.org/annotation/VSP_000070
http://togogenome.org/gene/9606:ALKBH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q83                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  (4R)-5-hydroxyleucine; alternate|||(4R)-5-oxoleucine; alternate|||Acquires the capacity to efficiently repair N1-methyladenine adduct in dsDNA.|||Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3|||Decreases activity against N1-methyladenine.|||Decreases activity by about 60%.|||Decreases activity by about 65%.|||Decreases activity towards ssDNA by 25%. Loss of activity towards dsDNA.|||Disordered|||Fe2OG dioxygenase|||In isoform 2.|||Loss of activity against N1-methyladenine.|||Loss of activity.|||No effect.|||Polar residues|||Strong decrease of activity.|||Strongly increases activity towards dsDNA, possibly by facilitating access to the active site.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239278|||http://purl.uniprot.org/annotation/VAR_026631|||http://purl.uniprot.org/annotation/VAR_026632|||http://purl.uniprot.org/annotation/VSP_019125|||http://purl.uniprot.org/annotation/VSP_019126|||http://purl.uniprot.org/annotation/VSP_019127
http://togogenome.org/gene/9606:CNEP1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8YCP3|||http://purl.uniprot.org/uniprot/Q8N9A8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear envelope phosphatase-regulatory subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286615|||http://purl.uniprot.org/annotation/VSP_025126|||http://purl.uniprot.org/annotation/VSP_025127|||http://purl.uniprot.org/annotation/VSP_025128
http://togogenome.org/gene/9606:AKR1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK69|||http://purl.uniprot.org/uniprot/P52895                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member C2|||Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold.|||Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold.|||In SRXY8; partially impaired activity.|||In isoform 2.|||Increases the low androstenedione reductase activity.|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Proton donor|||Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124637|||http://purl.uniprot.org/annotation/VAR_014748|||http://purl.uniprot.org/annotation/VAR_048216|||http://purl.uniprot.org/annotation/VAR_066632|||http://purl.uniprot.org/annotation/VAR_066633|||http://purl.uniprot.org/annotation/VAR_066634|||http://purl.uniprot.org/annotation/VAR_066635|||http://purl.uniprot.org/annotation/VSP_043779|||http://purl.uniprot.org/annotation/VSP_043780
http://togogenome.org/gene/9606:IGHMBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38935                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AN1-type|||DNA-binding protein SMUBP-2|||Disordered|||In CMT2S.|||In HMN6.|||In HMN6; does not affect ATPase activity; loss of helicase activity on RNA duplices.|||In HMN6; does not affect activity; reduces protein steady-state levels.|||In HMN6; severe reduction of ATPase activity and loss of helicase activity on RNA duplices.|||In HMN6; unknown pathological significance.|||N-acetylalanine|||Nuclear localization signal|||Polar residues|||Pro residues|||R3H|||Removed|||SS DNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080701|||http://purl.uniprot.org/annotation/VAR_020147|||http://purl.uniprot.org/annotation/VAR_021899|||http://purl.uniprot.org/annotation/VAR_021900|||http://purl.uniprot.org/annotation/VAR_022321|||http://purl.uniprot.org/annotation/VAR_022322|||http://purl.uniprot.org/annotation/VAR_022323|||http://purl.uniprot.org/annotation/VAR_022324|||http://purl.uniprot.org/annotation/VAR_022325|||http://purl.uniprot.org/annotation/VAR_022326|||http://purl.uniprot.org/annotation/VAR_022327|||http://purl.uniprot.org/annotation/VAR_022328|||http://purl.uniprot.org/annotation/VAR_022329|||http://purl.uniprot.org/annotation/VAR_022330|||http://purl.uniprot.org/annotation/VAR_022331|||http://purl.uniprot.org/annotation/VAR_022332|||http://purl.uniprot.org/annotation/VAR_022333|||http://purl.uniprot.org/annotation/VAR_022334|||http://purl.uniprot.org/annotation/VAR_022335|||http://purl.uniprot.org/annotation/VAR_022336|||http://purl.uniprot.org/annotation/VAR_022337|||http://purl.uniprot.org/annotation/VAR_022338|||http://purl.uniprot.org/annotation/VAR_022339|||http://purl.uniprot.org/annotation/VAR_022340|||http://purl.uniprot.org/annotation/VAR_024242|||http://purl.uniprot.org/annotation/VAR_024243|||http://purl.uniprot.org/annotation/VAR_055225|||http://purl.uniprot.org/annotation/VAR_055226|||http://purl.uniprot.org/annotation/VAR_058497|||http://purl.uniprot.org/annotation/VAR_058498|||http://purl.uniprot.org/annotation/VAR_058499|||http://purl.uniprot.org/annotation/VAR_058500|||http://purl.uniprot.org/annotation/VAR_058501|||http://purl.uniprot.org/annotation/VAR_058502|||http://purl.uniprot.org/annotation/VAR_058503|||http://purl.uniprot.org/annotation/VAR_058504|||http://purl.uniprot.org/annotation/VAR_058505|||http://purl.uniprot.org/annotation/VAR_058506|||http://purl.uniprot.org/annotation/VAR_072694|||http://purl.uniprot.org/annotation/VAR_072695|||http://purl.uniprot.org/annotation/VAR_072696|||http://purl.uniprot.org/annotation/VAR_072697
http://togogenome.org/gene/9606:LRRC8D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRU1|||http://purl.uniprot.org/uniprot/Q7L1W4|||http://purl.uniprot.org/uniprot/Q96GG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Affects ion selectivity of the channel. Reduced permeability to negatively charged glutamate and gluconate.|||Alters channel anion selectivity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRC8 pannexin-like TM region|||Phosphoserine|||Polar residues|||Volume-regulated anion channel subunit LRRC8D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084493|||http://purl.uniprot.org/annotation/VAR_051132
http://togogenome.org/gene/9606:LRRC36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4G3|||http://purl.uniprot.org/uniprot/Q1X8D7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRRCT|||Leucine-rich repeat-containing protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000275855|||http://purl.uniprot.org/annotation/VAR_047015|||http://purl.uniprot.org/annotation/VAR_047016|||http://purl.uniprot.org/annotation/VAR_047017|||http://purl.uniprot.org/annotation/VSP_022963|||http://purl.uniprot.org/annotation/VSP_022964|||http://purl.uniprot.org/annotation/VSP_057264|||http://purl.uniprot.org/annotation/VSP_057265|||http://purl.uniprot.org/annotation/VSP_057266
http://togogenome.org/gene/9606:GBE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04446|||http://purl.uniprot.org/uniprot/Q59ET0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1,4-alpha-glucan-branching enzyme|||Glycosyl hydrolase family 13 catalytic|||In APBN.|||In GSD4 and APBN.|||In GSD4.|||In GSD4; childhood neuromuscular form; 15 to 25% residual activity.|||In GSD4; loss of activity.|||In GSD4; non-progressive form; impairs protein stability; 50% residual activity.|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188775|||http://purl.uniprot.org/annotation/VAR_022109|||http://purl.uniprot.org/annotation/VAR_022429|||http://purl.uniprot.org/annotation/VAR_022430|||http://purl.uniprot.org/annotation/VAR_022431|||http://purl.uniprot.org/annotation/VAR_022432|||http://purl.uniprot.org/annotation/VAR_022433|||http://purl.uniprot.org/annotation/VAR_022434|||http://purl.uniprot.org/annotation/VAR_022435|||http://purl.uniprot.org/annotation/VAR_022436|||http://purl.uniprot.org/annotation/VAR_034747|||http://purl.uniprot.org/annotation/VAR_034748|||http://purl.uniprot.org/annotation/VAR_034749
http://togogenome.org/gene/9606:PRRX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54821                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In AGOTC.|||In isoform 2.|||N6-acetyllysine|||OAR|||Paired mesoderm homeobox protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049251|||http://purl.uniprot.org/annotation/VAR_066414|||http://purl.uniprot.org/annotation/VSP_002278
http://togogenome.org/gene/9606:ABO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A089QDC1|||http://purl.uniprot.org/uniprot/P16442                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alters substrate specificity of group B transferase.|||Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized.|||Cytoplasmic|||Decreases specific activity of group B transferase almost to zero.|||Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form|||Helical|||Helical; Signal-anchor for type II membrane protein|||Histo-blood group ABO system transferase|||In allele A106 and allele B3.|||In allele A107.|||In allele A2.|||In allele Aw07.|||In allele Aw08 and allele Bw08.|||In allele Aw08.|||In allele B(A).|||In allele B104.|||In allele B106.|||In allele Bel01; loss of manganese binding and reduced catalytic activity.|||In allele Bw08.|||In group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012268|||http://purl.uniprot.org/annotation/PRO_0000012269|||http://purl.uniprot.org/annotation/VAR_003408|||http://purl.uniprot.org/annotation/VAR_003409|||http://purl.uniprot.org/annotation/VAR_003410|||http://purl.uniprot.org/annotation/VAR_003411|||http://purl.uniprot.org/annotation/VAR_003412|||http://purl.uniprot.org/annotation/VAR_003413|||http://purl.uniprot.org/annotation/VAR_003414|||http://purl.uniprot.org/annotation/VAR_019147|||http://purl.uniprot.org/annotation/VAR_019148|||http://purl.uniprot.org/annotation/VAR_019149|||http://purl.uniprot.org/annotation/VAR_019150|||http://purl.uniprot.org/annotation/VAR_019151|||http://purl.uniprot.org/annotation/VAR_019152|||http://purl.uniprot.org/annotation/VAR_019153|||http://purl.uniprot.org/annotation/VAR_019154|||http://purl.uniprot.org/annotation/VAR_033540|||http://purl.uniprot.org/annotation/VAR_033541|||http://purl.uniprot.org/annotation/VAR_036738|||http://purl.uniprot.org/annotation/VAR_036739|||http://purl.uniprot.org/annotation/VAR_036740|||http://purl.uniprot.org/annotation/VAR_036741|||http://purl.uniprot.org/annotation/VAR_036742|||http://purl.uniprot.org/annotation/VAR_036743|||http://purl.uniprot.org/annotation/VAR_036744|||http://purl.uniprot.org/annotation/VAR_036745|||http://purl.uniprot.org/annotation/VAR_055227|||http://purl.uniprot.org/annotation/VAR_072628
http://togogenome.org/gene/9606:FHIP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHF complex subunit HOOK-interacting protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284645|||http://purl.uniprot.org/annotation/VAR_054008|||http://purl.uniprot.org/annotation/VAR_054009
http://togogenome.org/gene/9606:H2AJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTM1                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Histone H2A.J|||In isoform 2.|||N5-methylglutamine|||N6-acetyllysine|||N6-lactoyllysine; alternate|||Phosphothreonine; by DCAF1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344247|||http://purl.uniprot.org/annotation/VSP_034750
http://togogenome.org/gene/9606:LCE3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5B0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 3E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235337
http://togogenome.org/gene/9606:POLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  DNA polymerase kappa|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 7 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||Loss of DNA polymerase activity; when associated with A-199.|||Loss of DNA polymerase activity; when associated with D-198.|||Polar residues|||UBZ4-type 1|||UBZ4-type 2|||UmuC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173990|||http://purl.uniprot.org/annotation/VAR_021246|||http://purl.uniprot.org/annotation/VAR_021247|||http://purl.uniprot.org/annotation/VAR_021248|||http://purl.uniprot.org/annotation/VAR_048886|||http://purl.uniprot.org/annotation/VAR_048887|||http://purl.uniprot.org/annotation/VSP_012801|||http://purl.uniprot.org/annotation/VSP_012802|||http://purl.uniprot.org/annotation/VSP_012803|||http://purl.uniprot.org/annotation/VSP_012804|||http://purl.uniprot.org/annotation/VSP_012805|||http://purl.uniprot.org/annotation/VSP_012806|||http://purl.uniprot.org/annotation/VSP_053406|||http://purl.uniprot.org/annotation/VSP_053407|||http://purl.uniprot.org/annotation/VSP_053408|||http://purl.uniprot.org/annotation/VSP_053409
http://togogenome.org/gene/9606:SLC25A51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1U9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Impaired import of NAD(+) into mitochondria.|||In a breast cancer sample; somatic mutation.|||Mitochondrial nicotinamide adenine dinucleotide transporter SLC25A51|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090711|||http://purl.uniprot.org/annotation/VAR_036333
http://togogenome.org/gene/9606:MORC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTP6|||http://purl.uniprot.org/uniprot/Q8TE76                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  CW-type|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||MORC family CW-type zinc finger protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096539|||http://purl.uniprot.org/annotation/VAR_051197|||http://purl.uniprot.org/annotation/VAR_051198|||http://purl.uniprot.org/annotation/VSP_045025|||http://purl.uniprot.org/annotation/VSP_045026
http://togogenome.org/gene/9606:GPX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07203|||http://purl.uniprot.org/uniprot/Q7L4Q3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Non standard residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutathione peroxidase 1|||In isoform 2.|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Selenocysteine|||Subject to oxidation and hydroselenide loss to dehydroalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066610|||http://purl.uniprot.org/annotation/VAR_007904|||http://purl.uniprot.org/annotation/VAR_020912|||http://purl.uniprot.org/annotation/VAR_020913|||http://purl.uniprot.org/annotation/VAR_020914|||http://purl.uniprot.org/annotation/VAR_020915|||http://purl.uniprot.org/annotation/VSP_047369|||http://purl.uniprot.org/annotation/VSP_047370
http://togogenome.org/gene/9606:ZG16B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G8H6I3|||http://purl.uniprot.org/uniprot/Q96DA0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Jacalin-type lectin|||N-linked (GlcNAc...) asparagine|||Zymogen granule protein 16 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248073|||http://purl.uniprot.org/annotation/VAR_060067
http://togogenome.org/gene/9606:EEF1B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24534                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Elongation factor 1-beta|||GST C-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155021
http://togogenome.org/gene/9606:PANX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with primary ovarian failure associated with intellectual disability and sensorineural hearing loss; unknown pathological significance; no change in glycosylation pattern.|||Helical|||Impaired glycosylation. Loss of GLY1 and GLY2 forms. No effect on oocyte survival.|||Impaired glycosylation; loss of GLY2 form; oocyte death.|||In OZEMA7; impaired glycosylation resulting in the absence of GLY2 and the accumulation of GLY1 forms; associated with increased hemi-channel activity.|||In OZEMA7; impaired glycosylation resulting in the absence of GLY2 and the accumulation of GLY1 forms; associated with increased hemichannel activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No change in glycosylation pattern.|||Pannexin-1|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208484|||http://purl.uniprot.org/annotation/VAR_016098|||http://purl.uniprot.org/annotation/VAR_031225|||http://purl.uniprot.org/annotation/VAR_083161|||http://purl.uniprot.org/annotation/VAR_083162|||http://purl.uniprot.org/annotation/VAR_083163|||http://purl.uniprot.org/annotation/VAR_083164|||http://purl.uniprot.org/annotation/VAR_083165|||http://purl.uniprot.org/annotation/VSP_011476
http://togogenome.org/gene/9606:RAD50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D6Y3|||http://purl.uniprot.org/uniprot/Q92878                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to degrade ATP.|||DNA repair protein RAD50|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Rad50/SbcC-type AAA|||Zinc-hook                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138641|||http://purl.uniprot.org/annotation/VAR_020958|||http://purl.uniprot.org/annotation/VAR_020959|||http://purl.uniprot.org/annotation/VAR_020960|||http://purl.uniprot.org/annotation/VAR_020961|||http://purl.uniprot.org/annotation/VAR_020962|||http://purl.uniprot.org/annotation/VAR_022085|||http://purl.uniprot.org/annotation/VAR_025526|||http://purl.uniprot.org/annotation/VAR_025527|||http://purl.uniprot.org/annotation/VAR_029168|||http://purl.uniprot.org/annotation/VAR_029169|||http://purl.uniprot.org/annotation/VAR_029170|||http://purl.uniprot.org/annotation/VAR_034436|||http://purl.uniprot.org/annotation/VAR_061779|||http://purl.uniprot.org/annotation/VSP_012590|||http://purl.uniprot.org/annotation/VSP_012591
http://togogenome.org/gene/9606:NOL4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0N3|||http://purl.uniprot.org/uniprot/Q6P0R2|||http://purl.uniprot.org/uniprot/Q96MY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleolar protein 4-like|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079456|||http://purl.uniprot.org/annotation/VSP_014667|||http://purl.uniprot.org/annotation/VSP_014668
http://togogenome.org/gene/9606:UPK3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT76                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Uroplakin-3b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022640|||http://purl.uniprot.org/annotation/VAR_034561|||http://purl.uniprot.org/annotation/VAR_047805|||http://purl.uniprot.org/annotation/VSP_037327|||http://purl.uniprot.org/annotation/VSP_054295
http://togogenome.org/gene/9606:ZHX1-C8orf76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EF9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Zinc fingers and homeoboxes protein 1, isoform 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415939
http://togogenome.org/gene/9606:TMEM42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YG0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284495
http://togogenome.org/gene/9606:NPBWR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48146                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Neuropeptides B/W receptor type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069522|||http://purl.uniprot.org/annotation/VAR_003579|||http://purl.uniprot.org/annotation/VAR_035766
http://togogenome.org/gene/9606:ITGB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0X7|||http://purl.uniprot.org/uniprot/B4E0R1|||http://purl.uniprot.org/uniprot/P05107                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation. Reduces COS cell adhesion to ICAM1.|||Cell attachment site|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In LAD1.|||Integrin beta|||Integrin beta subunit VWA|||Integrin beta subunit cytoplasmic|||Integrin beta subunit tail|||Integrin beta-2|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by PKC/PRKCA; in vitro|||Phosphothreonine; by PKC; in vitro|||Polar residues|||Pyrrolidone carboxylic acid|||VWFA|||in ADMIDAS binding site|||in ADMIDAS binding site and liganded-open conformation|||in ADMIDAS binding site and unliganded-closed conformation|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016341|||http://purl.uniprot.org/annotation/PRO_5019772092|||http://purl.uniprot.org/annotation/VAR_003984|||http://purl.uniprot.org/annotation/VAR_003985|||http://purl.uniprot.org/annotation/VAR_003986|||http://purl.uniprot.org/annotation/VAR_003987|||http://purl.uniprot.org/annotation/VAR_003988|||http://purl.uniprot.org/annotation/VAR_003989|||http://purl.uniprot.org/annotation/VAR_003990|||http://purl.uniprot.org/annotation/VAR_003991|||http://purl.uniprot.org/annotation/VAR_003992|||http://purl.uniprot.org/annotation/VAR_013402|||http://purl.uniprot.org/annotation/VAR_013403|||http://purl.uniprot.org/annotation/VAR_030035|||http://purl.uniprot.org/annotation/VAR_065661|||http://purl.uniprot.org/annotation/VAR_065662|||http://purl.uniprot.org/annotation/VAR_065663|||http://purl.uniprot.org/annotation/VAR_065664
http://togogenome.org/gene/9606:LDHAL6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM9|||http://purl.uniprot.org/uniprot/Q9BYZ2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  L-lactate dehydrogenase A-like 6B|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168458|||http://purl.uniprot.org/annotation/VAR_027936|||http://purl.uniprot.org/annotation/VAR_027937|||http://purl.uniprot.org/annotation/VAR_027938|||http://purl.uniprot.org/annotation/VAR_049757
http://togogenome.org/gene/9606:ZNF300                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||Polar residues|||Zinc finger protein 300                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047521|||http://purl.uniprot.org/annotation/VAR_012355|||http://purl.uniprot.org/annotation/VSP_036830|||http://purl.uniprot.org/annotation/VSP_036831|||http://purl.uniprot.org/annotation/VSP_047506
http://togogenome.org/gene/9606:KIF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15058                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||FHA|||In MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant D-849.|||In MCPH20; Decreased expression at the mRNA level and loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody, when analyzed in primary fibroblasts from a patient who is a compound heterozygous with variant V-1221.|||In MCPH20; drastically decreased expression at the mRNA level; loss of localization at the midbody during cytokinesis and consequently loss of CIT/CRIK recruitment to the midbody.|||In MCPH20; unknown pathological significance.|||Kinesin motor|||Kinesin-like protein KIF14|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for CIT-binding|||Required for PRC1-binding|||Required for microtubule-binding with high affinity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125449|||http://purl.uniprot.org/annotation/VAR_037777|||http://purl.uniprot.org/annotation/VAR_080623|||http://purl.uniprot.org/annotation/VAR_080624|||http://purl.uniprot.org/annotation/VAR_080625|||http://purl.uniprot.org/annotation/VAR_080626|||http://purl.uniprot.org/annotation/VAR_080627|||http://purl.uniprot.org/annotation/VAR_080628
http://togogenome.org/gene/9606:LEKR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KP02|||http://purl.uniprot.org/uniprot/Q6ZMV7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region                                                                                  ^@                                                                                  Disordered|||Protein LEKR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325711
http://togogenome.org/gene/9606:ZFY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08048                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Zinc finger Y-chromosomal protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047261|||http://purl.uniprot.org/annotation/VSP_042774|||http://purl.uniprot.org/annotation/VSP_042775|||http://purl.uniprot.org/annotation/VSP_042824|||http://purl.uniprot.org/annotation/VSP_042825|||http://purl.uniprot.org/annotation/VSP_042826
http://togogenome.org/gene/9606:ALDOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04075                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fructose-bisphosphate aldolase A|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In GSD12.|||In GSD12; likely benign variant; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity.|||In GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity.|||In GSD12; thermolabile.|||In isoform 2.|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine|||N6-malonyllysine; alternate|||Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed|||Schiff-base intermediate with dihydroxyacetone-P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216936|||http://purl.uniprot.org/annotation/VAR_000550|||http://purl.uniprot.org/annotation/VAR_044142|||http://purl.uniprot.org/annotation/VAR_044143|||http://purl.uniprot.org/annotation/VAR_044144|||http://purl.uniprot.org/annotation/VAR_048219|||http://purl.uniprot.org/annotation/VAR_048220|||http://purl.uniprot.org/annotation/VAR_085824|||http://purl.uniprot.org/annotation/VSP_047261
http://togogenome.org/gene/9606:SPRED3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EKV1|||http://purl.uniprot.org/uniprot/Q2MJR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||KBD|||Omega-N-methylarginine|||Polar residues|||Pro residues|||SPR|||Sprouty-related, EVH1 domain-containing protein 3|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247431|||http://purl.uniprot.org/annotation/VSP_042949|||http://purl.uniprot.org/annotation/VSP_042950
http://togogenome.org/gene/9606:TLR10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXR5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034739|||http://purl.uniprot.org/annotation/VAR_024669|||http://purl.uniprot.org/annotation/VAR_024670|||http://purl.uniprot.org/annotation/VAR_024671|||http://purl.uniprot.org/annotation/VAR_024672|||http://purl.uniprot.org/annotation/VAR_024673|||http://purl.uniprot.org/annotation/VAR_024674|||http://purl.uniprot.org/annotation/VAR_028125|||http://purl.uniprot.org/annotation/VAR_028126|||http://purl.uniprot.org/annotation/VAR_028127|||http://purl.uniprot.org/annotation/VAR_028128|||http://purl.uniprot.org/annotation/VAR_028129|||http://purl.uniprot.org/annotation/VAR_028130|||http://purl.uniprot.org/annotation/VAR_028131|||http://purl.uniprot.org/annotation/VAR_059832|||http://purl.uniprot.org/annotation/VAR_059833|||http://purl.uniprot.org/annotation/VAR_059834|||http://purl.uniprot.org/annotation/VAR_059835
http://togogenome.org/gene/9606:BBS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7W2|||http://purl.uniprot.org/uniprot/A0A090N8P4|||http://purl.uniprot.org/uniprot/A0A5F9ZGY2|||http://purl.uniprot.org/uniprot/A0A5F9ZH14|||http://purl.uniprot.org/uniprot/A0A5F9ZH74|||http://purl.uniprot.org/uniprot/Q3SYG4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Critical for protein stability|||Disordered|||Fails to restore protein stability; when associated with pathogenic variant BBS9 R-141.|||In BBS9; severe loss of protein stability, probably due to aberrant folding.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with LZTL1|||PTHB1 C-terminal|||PTHB1 N-terminal|||Protein PTHB1|||Seven-bladed beta-propeller                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235269|||http://purl.uniprot.org/annotation/VAR_026389|||http://purl.uniprot.org/annotation/VAR_026390|||http://purl.uniprot.org/annotation/VAR_051289|||http://purl.uniprot.org/annotation/VAR_051290|||http://purl.uniprot.org/annotation/VAR_051291|||http://purl.uniprot.org/annotation/VAR_066292|||http://purl.uniprot.org/annotation/VAR_066293|||http://purl.uniprot.org/annotation/VAR_066294|||http://purl.uniprot.org/annotation/VSP_018421|||http://purl.uniprot.org/annotation/VSP_018422|||http://purl.uniprot.org/annotation/VSP_018423|||http://purl.uniprot.org/annotation/VSP_018424|||http://purl.uniprot.org/annotation/VSP_018425|||http://purl.uniprot.org/annotation/VSP_018426|||http://purl.uniprot.org/annotation/VSP_018427|||http://purl.uniprot.org/annotation/VSP_018428|||http://purl.uniprot.org/annotation/VSP_054063
http://togogenome.org/gene/9606:GABRA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31644                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In DEE79; decreased subcellular localization to the cell membrane resulting in altered protein localization to the synapse and altered gamma-aminobutyric acid signaling pathway.|||In DEE79; decreased subcellular localization to the cell membrane resulting in altered protein localization to the synapse and altered gamma-aminobutyric acid signaling pathway; the mutant subunit decreases the trafficking of the partnering GABRB3 subunit to the cell membrane with no effect on other subunits.|||In DEE79; increased affinity to GABA; decreased maximal GABA-evoked current density.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000444|||http://purl.uniprot.org/annotation/VAR_083201|||http://purl.uniprot.org/annotation/VAR_083202|||http://purl.uniprot.org/annotation/VAR_083203
http://togogenome.org/gene/9606:PPARG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C1F9|||http://purl.uniprot.org/uniprot/D2KUA6|||http://purl.uniprot.org/uniprot/E9PFV2|||http://purl.uniprot.org/uniprot/E9PFX5|||http://purl.uniprot.org/uniprot/P37231                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||In FPLD3.|||In colon cancer; sporadic; somatic mutation; loss of ligand-binding.|||In colon cancer; sporadic; somatic mutation; partial loss of ligand-binding.|||In diabetes.|||In isoform 1 and isoform 3.|||In isoform 3.|||In obesity.|||Interaction with FAM120B|||NR C4-type|||NR LBD|||Nuclear receptor|||O-linked (GlcNAc) threonine|||Peroxisome proliferator-activated receptor gamma|||Phosphoserine|||Significant independent determinant of CIMT; may protect from early atherosclerosis in subject at risk for diabetes; associated with BMI.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053492|||http://purl.uniprot.org/annotation/VAR_010723|||http://purl.uniprot.org/annotation/VAR_010724|||http://purl.uniprot.org/annotation/VAR_010725|||http://purl.uniprot.org/annotation/VAR_010726|||http://purl.uniprot.org/annotation/VAR_010727|||http://purl.uniprot.org/annotation/VAR_010728|||http://purl.uniprot.org/annotation/VAR_016116|||http://purl.uniprot.org/annotation/VAR_022700|||http://purl.uniprot.org/annotation/VAR_022701|||http://purl.uniprot.org/annotation/VSP_003645|||http://purl.uniprot.org/annotation/VSP_043906|||http://purl.uniprot.org/annotation/VSP_043907
http://togogenome.org/gene/9606:ACVR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DPA4|||http://purl.uniprot.org/uniprot/Q04771                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activin receptor type-1|||Almost complete loss of alcaline phosphatase induction; in association with A-325.|||Almost complete loss of alcaline phosphatase induction; in association with V-203.|||Cytoplasmic|||Extracellular|||GS|||Helical|||In FOP.|||In FOP; variant phenotype.|||In FOP; with some atypical features.|||In a melanoma sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase receptor|||Strong induction of SMAD1 phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024394|||http://purl.uniprot.org/annotation/PRO_5014302489|||http://purl.uniprot.org/annotation/VAR_028444|||http://purl.uniprot.org/annotation/VAR_041392|||http://purl.uniprot.org/annotation/VAR_041393|||http://purl.uniprot.org/annotation/VAR_041394|||http://purl.uniprot.org/annotation/VAR_041395|||http://purl.uniprot.org/annotation/VAR_058418|||http://purl.uniprot.org/annotation/VAR_058419|||http://purl.uniprot.org/annotation/VAR_058420|||http://purl.uniprot.org/annotation/VAR_058421|||http://purl.uniprot.org/annotation/VAR_058422|||http://purl.uniprot.org/annotation/VAR_058423|||http://purl.uniprot.org/annotation/VAR_058424|||http://purl.uniprot.org/annotation/VAR_058425
http://togogenome.org/gene/9606:AADACL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P093                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Arylacetamide deacetylase-like 2|||In isoform 2.|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314960|||http://purl.uniprot.org/annotation/VAR_038140|||http://purl.uniprot.org/annotation/VAR_038141|||http://purl.uniprot.org/annotation/VSP_038389|||http://purl.uniprot.org/annotation/VSP_038390
http://togogenome.org/gene/9606:RHBDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75783                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Nucleophile|||Rhomboid-related protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206173|||http://purl.uniprot.org/annotation/VSP_005372
http://togogenome.org/gene/9606:GSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS51|||http://purl.uniprot.org/uniprot/A0A0A0MT01|||http://purl.uniprot.org/uniprot/A0A384MEF1|||http://purl.uniprot.org/uniprot/B7Z4U6|||http://purl.uniprot.org/uniprot/P06396                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-actin interfilament contact point|||Actin-binding, Ca-sensitive|||Actin-severing|||Basic and acidic residues|||Disordered|||Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and N-697 or N-214, N-697 and Q-719.|||Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and N-697 or N-214, Q-236 and N-697.|||Does not result in actin depolymerization activity in absence of calcium. Has actin depolymerization activity in absence of calcium; when associated with N-214 and Q-236, N-214 and Q-719 or N-214, Q-236 and Q-719.|||Gelsolin|||Gelsolin-like|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||In AMYL5.|||In AMYL5; does not result in actin depolymerization in absence of calcium.|||In a breast cancer sample; somatic mutation.|||In isoform 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine; by SRC|||Phosphotyrosine; by SRC; in vitro                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036385|||http://purl.uniprot.org/annotation/PRO_5017394095|||http://purl.uniprot.org/annotation/VAR_007718|||http://purl.uniprot.org/annotation/VAR_007719|||http://purl.uniprot.org/annotation/VAR_024690|||http://purl.uniprot.org/annotation/VAR_033958|||http://purl.uniprot.org/annotation/VAR_036337|||http://purl.uniprot.org/annotation/VAR_036338|||http://purl.uniprot.org/annotation/VAR_036339|||http://purl.uniprot.org/annotation/VAR_061982|||http://purl.uniprot.org/annotation/VSP_018959|||http://purl.uniprot.org/annotation/VSP_042879|||http://purl.uniprot.org/annotation/VSP_054791
http://togogenome.org/gene/9606:OCIAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX40                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||OCIA|||OCIA domain-containing protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299382|||http://purl.uniprot.org/annotation/VSP_027621|||http://purl.uniprot.org/annotation/VSP_027622|||http://purl.uniprot.org/annotation/VSP_046212
http://togogenome.org/gene/9606:PRKAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y478                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  5'-AMP-activated protein kinase subunit beta-1|||Abolishes myristoylation and AMP-enhanced phosphorylation of PRKAA1 or PRKAA2.|||Basic and acidic residues|||Disordered|||Glycogen-binding domain|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204363
http://togogenome.org/gene/9606:H4C8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:RNF41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4P4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase NRDP1|||In isoform 2.|||Loss of activity.|||Loss of activity; when associated with Q-36.|||Loss of activity; when associated with S-34.|||RING-type; degenerate|||SIAH-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223954|||http://purl.uniprot.org/annotation/VSP_044670
http://togogenome.org/gene/9606:TDRD15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCY1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4|||Tudor 5|||Tudor 6|||Tudor 7|||Tudor 8|||Tudor domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421965
http://togogenome.org/gene/9606:DMRTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L9A0|||http://purl.uniprot.org/uniprot/Q96MA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  DM|||Disordered|||Doublesex- and mab-3-related transcription factor B1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316012
http://togogenome.org/gene/9606:SETDB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T68                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Histone-lysine N-methyltransferase SETDB2|||In isoform 2.|||In isoform 3.|||MBD|||Pre-SET|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186088|||http://purl.uniprot.org/annotation/VAR_016976|||http://purl.uniprot.org/annotation/VAR_031282|||http://purl.uniprot.org/annotation/VSP_008413|||http://purl.uniprot.org/annotation/VSP_024034
http://togogenome.org/gene/9606:PDE8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN77|||http://purl.uniprot.org/uniprot/O95263                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B|||In PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PAS|||PDEase|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198840|||http://purl.uniprot.org/annotation/VAR_066503|||http://purl.uniprot.org/annotation/VSP_008081|||http://purl.uniprot.org/annotation/VSP_008082|||http://purl.uniprot.org/annotation/VSP_008083|||http://purl.uniprot.org/annotation/VSP_008084|||http://purl.uniprot.org/annotation/VSP_008085
http://togogenome.org/gene/9606:ZNF787                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DD87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues|||Zinc finger protein 787                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287606|||http://purl.uniprot.org/annotation/VAR_032336
http://togogenome.org/gene/9606:XKR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GH76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase-3, caspase-6 and caspase-7|||Disordered|||Helical|||Phosphoserine|||Polar residues|||XK-related protein 4|||XK-related protein 4, processed form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190777|||http://purl.uniprot.org/annotation/PRO_0000453289
http://togogenome.org/gene/9606:TMEM52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDY8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Transmembrane protein 52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284057|||http://purl.uniprot.org/annotation/VAR_031653|||http://purl.uniprot.org/annotation/VAR_051448|||http://purl.uniprot.org/annotation/VSP_024420
http://togogenome.org/gene/9606:CXCL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02778                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-X-C motif chemokine 10|||CXCL10(1-73)|||Citrulline; by PAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005101|||http://purl.uniprot.org/annotation/PRO_0000005102
http://togogenome.org/gene/9606:CGREF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99674                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4 X 17 AA approximate tandem repeats of P-G-P-R-G-E-A-G-G-Q-A-E-A-[KR]-G-D-A|||4; approximate|||Basic and acidic residues|||Cell growth regulator with EF hand domain protein 1|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073874|||http://purl.uniprot.org/annotation/VAR_047648|||http://purl.uniprot.org/annotation/VAR_047649|||http://purl.uniprot.org/annotation/VAR_047650|||http://purl.uniprot.org/annotation/VAR_061088|||http://purl.uniprot.org/annotation/VAR_081928|||http://purl.uniprot.org/annotation/VAR_081929|||http://purl.uniprot.org/annotation/VAR_081930|||http://purl.uniprot.org/annotation/VSP_060232|||http://purl.uniprot.org/annotation/VSP_060233|||http://purl.uniprot.org/annotation/VSP_060234|||http://purl.uniprot.org/annotation/VSP_060235|||http://purl.uniprot.org/annotation/VSP_060236
http://togogenome.org/gene/9606:EIF3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55884                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mass|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit B|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||RRM|||Sufficient for interaction with EIF3E|||Sufficient for interaction with EIF3J|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123531|||http://purl.uniprot.org/annotation/VAR_047972|||http://purl.uniprot.org/annotation/VAR_047973|||http://purl.uniprot.org/annotation/VSP_017274
http://togogenome.org/gene/9606:PDYN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01213                                                                                  ^@                                                                                  Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Alpha-neoendorphin|||Beta-neoendorphin|||Big dynorphin|||Dynorphin A(1-13)|||Dynorphin A(1-17)|||Dynorphin A(1-8)|||In SCA23.|||In SCA23; PDYN, dynorphin A and dynorphin B are located in Purkinje cells as observed in control cerebellum, but cerebellar tissue with the mutation has decreased levels of SLC1A6 and CALB1, both of which are markers of Purkinje cells; SLC1A6 accumulates and aggregates in patient cerebellar tissue.|||In SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, resulting in an approximately 2-fold decreased level of dynorphin B compared to dynorphin A; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property.|||In SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; mutant dynorphin A is neurotoxic to cultured striatal neurons, suggesting a dominant-negative effect; disrupts membrane property.|||In SCA23; the mutant PDYN protein is produced, but processing to opioid peptides is dramatically affected, with increased levels of dynorphin A compared to dynorphin B; these results suggest slow conversion of dynorphin A to short enkephalins; mutant S-211 dynorphin A is not neurotoxic to cultured striatal neurons; no effect on membrane property.|||Leu-enkephalin|||Leumorphin|||Rimorphin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008176|||http://purl.uniprot.org/annotation/PRO_0000008177|||http://purl.uniprot.org/annotation/PRO_0000008178|||http://purl.uniprot.org/annotation/PRO_0000008179|||http://purl.uniprot.org/annotation/PRO_0000008180|||http://purl.uniprot.org/annotation/PRO_0000008181|||http://purl.uniprot.org/annotation/PRO_0000008182|||http://purl.uniprot.org/annotation/PRO_0000306347|||http://purl.uniprot.org/annotation/PRO_0000306348|||http://purl.uniprot.org/annotation/PRO_0000306349|||http://purl.uniprot.org/annotation/PRO_0000306350|||http://purl.uniprot.org/annotation/PRO_0000306351|||http://purl.uniprot.org/annotation/PRO_0000306352|||http://purl.uniprot.org/annotation/VAR_064913|||http://purl.uniprot.org/annotation/VAR_064914|||http://purl.uniprot.org/annotation/VAR_064915|||http://purl.uniprot.org/annotation/VAR_064916|||http://purl.uniprot.org/annotation/VAR_072266|||http://purl.uniprot.org/annotation/VAR_072267|||http://purl.uniprot.org/annotation/VAR_072268|||http://purl.uniprot.org/annotation/VAR_072269|||http://purl.uniprot.org/annotation/VAR_072270
http://togogenome.org/gene/9606:MAGEB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15480                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||MAGE|||Melanoma-associated antigen B3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156714|||http://purl.uniprot.org/annotation/VAR_021360|||http://purl.uniprot.org/annotation/VAR_021361
http://togogenome.org/gene/9606:RYBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N488                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with GABPB1 and FANK1|||Phosphoserine|||Polar residues|||RING1 and YY1-binding protein|||RanBP2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097550
http://togogenome.org/gene/9606:RIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92963                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. Loss of interaction with AFDN, RLF and RALGDS; when associated with S-53. Loss of interaction with AFDN; when associated with G-55.|||Disordered|||Dominant negative. Loss of interaction with AFDN, RLF and RALGDS.|||GTP-binding protein Rit1|||In NS8; results in increased ELK1 transcriptional activation.|||In NS8; results in increased ELK1 transcriptional activation; results in increased MAPK-ERK signaling.|||In NS8; results in increased MAPK-ERK signaling.|||In isoform 2.|||In isoform 3.|||Loss of interaction with AFDN, RLF and RALGDS; when associated with L-79.|||Loss of interaction with AFDN, but not with RLF and RALGDS; when associated with L-79.|||Probable disease-associated variant found in patients with features of Noonan syndrome.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082725|||http://purl.uniprot.org/annotation/VAR_070149|||http://purl.uniprot.org/annotation/VAR_070150|||http://purl.uniprot.org/annotation/VAR_070151|||http://purl.uniprot.org/annotation/VAR_070152|||http://purl.uniprot.org/annotation/VAR_070153|||http://purl.uniprot.org/annotation/VAR_070154|||http://purl.uniprot.org/annotation/VAR_070155|||http://purl.uniprot.org/annotation/VAR_070156|||http://purl.uniprot.org/annotation/VAR_070157|||http://purl.uniprot.org/annotation/VSP_045306|||http://purl.uniprot.org/annotation/VSP_047114
http://togogenome.org/gene/9606:OAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6K5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  2'-5'-oligoadenylate synthase 3|||Abolishes catalytic activity.|||Impaired dsRNA binding.|||Interaction with dsRNA|||Linker|||N-acetylmethionine|||No effect on catalytic activity. No effect on catalytic activity; when associated with D-76.|||No effect on catalytic activity; when associated with D-145.|||OAS domain 1|||OAS domain 2|||OAS domain 3|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160265|||http://purl.uniprot.org/annotation/VAR_057660|||http://purl.uniprot.org/annotation/VAR_057661|||http://purl.uniprot.org/annotation/VAR_057662|||http://purl.uniprot.org/annotation/VAR_060076|||http://purl.uniprot.org/annotation/VAR_060077|||http://purl.uniprot.org/annotation/VAR_060078|||http://purl.uniprot.org/annotation/VAR_062127
http://togogenome.org/gene/9606:C1QTNF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0IWW5|||http://purl.uniprot.org/uniprot/P60827                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 8|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003541|||http://purl.uniprot.org/annotation/PRO_5035366277
http://togogenome.org/gene/9606:MRPS25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82663                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In COXPD50; severe reduction of MRPS25 protein levels resulting in destabilization of the entire small ribosomal subunit and a decrease of mitochondrial translation rate; causes oxidative phosphorylation defects in patient cells.|||In isoform 2.|||In isoform 3.|||Small ribosomal subunit protein mS25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087708|||http://purl.uniprot.org/annotation/VAR_084766|||http://purl.uniprot.org/annotation/VSP_056422|||http://purl.uniprot.org/annotation/VSP_056423|||http://purl.uniprot.org/annotation/VSP_056424
http://togogenome.org/gene/9606:MTFMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DP5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In COXPD15 and MC1DN27; decreased methionyl-tRNA formyltransferase activity.|||In COXPD15; loss of methionyl-tRNA formyltransferase activity.|||In MC1DN27.|||In isoform 2.|||Methionyl-tRNA formyltransferase, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010093|||http://purl.uniprot.org/annotation/VAR_059289|||http://purl.uniprot.org/annotation/VAR_069303|||http://purl.uniprot.org/annotation/VAR_069304|||http://purl.uniprot.org/annotation/VAR_081461|||http://purl.uniprot.org/annotation/VSP_057059|||http://purl.uniprot.org/annotation/VSP_057060
http://togogenome.org/gene/9606:SLC7A6OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In EPM12; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 1; marked reduction of protein expression in patient cells.|||Phosphoserine|||Polar residues|||Probable RNA polymerase II nuclear localization protein SLC7A6OS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289169|||http://purl.uniprot.org/annotation/VAR_032591|||http://purl.uniprot.org/annotation/VAR_032592|||http://purl.uniprot.org/annotation/VAR_032593|||http://purl.uniprot.org/annotation/VAR_032594|||http://purl.uniprot.org/annotation/VAR_085257
http://togogenome.org/gene/9606:PRKCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RSM7|||http://purl.uniprot.org/uniprot/P17252|||http://purl.uniprot.org/uniprot/Q7Z727                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||C2|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||N-acetylalanine|||N6-acetyllysine|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SYK|||Pro residues|||Protein kinase|||Protein kinase C alpha type|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055679|||http://purl.uniprot.org/annotation/VAR_042301|||http://purl.uniprot.org/annotation/VAR_042302|||http://purl.uniprot.org/annotation/VAR_042303|||http://purl.uniprot.org/annotation/VAR_050558
http://togogenome.org/gene/9606:MYBBP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with MYB|||Myb-binding protein 1A|||N6-acetyllysine|||Nuclear export signal 1|||Nuclear export signal 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for nuclear and nucleolar localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096255|||http://purl.uniprot.org/annotation/VAR_023064|||http://purl.uniprot.org/annotation/VAR_051156|||http://purl.uniprot.org/annotation/VAR_051157|||http://purl.uniprot.org/annotation/VAR_051158|||http://purl.uniprot.org/annotation/VSP_014786
http://togogenome.org/gene/9606:APOC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KPE2|||http://purl.uniprot.org/uniprot/P02656                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Turn                                                                                  ^@                                                                                  Apolipoprotein C-III|||In C-III-0; unglycosylated.|||In HALP2.|||Lipid-binding|||May interact with the LDL receptor|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000168|||http://purl.uniprot.org/annotation/PRO_0000002031|||http://purl.uniprot.org/annotation/PRO_5014296858|||http://purl.uniprot.org/annotation/VAR_000643|||http://purl.uniprot.org/annotation/VAR_000644
http://togogenome.org/gene/9606:IZUMO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1ZYL8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Izumo sperm-egg fusion protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278186|||http://purl.uniprot.org/annotation/VAR_030683|||http://purl.uniprot.org/annotation/VAR_050911|||http://purl.uniprot.org/annotation/VAR_061630|||http://purl.uniprot.org/annotation/VSP_023147|||http://purl.uniprot.org/annotation/VSP_023148|||http://purl.uniprot.org/annotation/VSP_023149|||http://purl.uniprot.org/annotation/VSP_023150
http://togogenome.org/gene/9606:ZNF394                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||SCAN box|||Zinc finger protein 394                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047557|||http://purl.uniprot.org/annotation/VAR_052816|||http://purl.uniprot.org/annotation/VSP_056547|||http://purl.uniprot.org/annotation/VSP_056548
http://togogenome.org/gene/9606:C8orf88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMB2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C8orf88                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425157
http://togogenome.org/gene/9606:SUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53999|||http://purl.uniprot.org/uniprot/Q6IBA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Activated RNA polymerase II transcriptional coactivator p15|||Basic and acidic residues|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with ssDNA|||Loss of ssDNA binding.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Reduced ssDNA binding.|||Regulatory|||Removed|||Transcriptional coactivator p15 (PC4) C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215944|||http://purl.uniprot.org/annotation/VAR_032870
http://togogenome.org/gene/9606:CDK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00534                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase 6|||In MCPH12.|||In a metastatic melanoma sample; somatic mutation.|||N-acetylmethionine|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085789|||http://purl.uniprot.org/annotation/VAR_041978|||http://purl.uniprot.org/annotation/VAR_041979|||http://purl.uniprot.org/annotation/VAR_072638
http://togogenome.org/gene/9606:HRCT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXD1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Histidine-rich carboxyl terminus protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317638
http://togogenome.org/gene/9606:GIMAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8H4|||http://purl.uniprot.org/uniprot/Q9UG22                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  AIG1-type G|||Abolishes GTP-induced dimerization.|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190986|||http://purl.uniprot.org/annotation/VAR_017305|||http://purl.uniprot.org/annotation/VAR_049531|||http://purl.uniprot.org/annotation/VAR_049532
http://togogenome.org/gene/9606:WDR12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53T99|||http://purl.uniprot.org/uniprot/Q9GZL7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MDN1.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylalanine|||NLE|||Phosphoserine|||Reduces interaction with MDN1.|||Removed|||Ribosome biogenesis protein WDR12|||Sufficient for nucleolar localization|||Ubiquitin-like (UBL) domain|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051358|||http://purl.uniprot.org/annotation/VAR_012863|||http://purl.uniprot.org/annotation/VAR_012864|||http://purl.uniprot.org/annotation/VAR_012865|||http://purl.uniprot.org/annotation/VAR_054888
http://togogenome.org/gene/9606:FCER1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30273                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||High affinity immunoglobulin epsilon receptor subunit gamma|||ITAM|||Interchain|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016501
http://togogenome.org/gene/9606:EID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6I1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EP300-interacting inhibitor of differentiation 2|||In isoform 2.|||Omega-N-methylarginine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315901|||http://purl.uniprot.org/annotation/VAR_038351|||http://purl.uniprot.org/annotation/VAR_050964|||http://purl.uniprot.org/annotation/VSP_052648
http://togogenome.org/gene/9606:ARL8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVJ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 8B|||Abolished ubiquitination by RNF167.|||Alters chromosome segregation.|||Diffuse cytoplasmic distribution and loss of localization to lysosomes. No effect on acetylation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Loss of GTP/GDP-binding. Affects chromosome segregation.|||N-acetylmethionine|||No effect on localization and acetylation.|||Note=Mediates targeting to membranes|||Preferentially binds GDP. Alters chromosome segregation. Decreases interaction with VPS41. Loss of lysosomal location. Loss of interaction with PLEKHM1.|||Preferentially binds GTP.|||Prevents GTP hydrolysis. No effect on lysosomal location. Alters lysosomes cellular distribution and motility. Increases interaction with VPS41. No effect on interaction with PLEKHM1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232921|||http://purl.uniprot.org/annotation/VSP_056238
http://togogenome.org/gene/9606:AACS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V21                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acetoacetyl-CoA synthetase|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315784|||http://purl.uniprot.org/annotation/VAR_038303|||http://purl.uniprot.org/annotation/VAR_060997|||http://purl.uniprot.org/annotation/VSP_030701|||http://purl.uniprot.org/annotation/VSP_030702
http://togogenome.org/gene/9606:RPL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18124                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 12 AA tandem repeats|||Large ribosomal subunit protein uL30|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000104633
http://togogenome.org/gene/9606:ARR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36575                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arrestin-C|||In MYP26; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205203|||http://purl.uniprot.org/annotation/VAR_025520|||http://purl.uniprot.org/annotation/VAR_080595|||http://purl.uniprot.org/annotation/VAR_080596|||http://purl.uniprot.org/annotation/VAR_080597|||http://purl.uniprot.org/annotation/VSP_017495
http://togogenome.org/gene/9606:HIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Binding to CtBP|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Hypermethylated in cancer 2 protein|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046945|||http://purl.uniprot.org/annotation/VSP_006829
http://togogenome.org/gene/9606:OR51F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLW9                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  G-protein coupled receptors family 1 profile|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:KIF22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9T5|||http://purl.uniprot.org/uniprot/Q14807                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In SEMDJL2.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF22|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125433|||http://purl.uniprot.org/annotation/VAR_067345|||http://purl.uniprot.org/annotation/VAR_067346|||http://purl.uniprot.org/annotation/VAR_067347|||http://purl.uniprot.org/annotation/VAR_067348|||http://purl.uniprot.org/annotation/VAR_067349|||http://purl.uniprot.org/annotation/VSP_046428
http://togogenome.org/gene/9606:MS4A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3V2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||Membrane-spanning 4-domains subfamily A member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158637|||http://purl.uniprot.org/annotation/VAR_036402
http://togogenome.org/gene/9606:MINDY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5J2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitin hydrolase activity.|||Basic and acidic residues|||Decreased association with 'Lys-48'-linked conjugated ubiquitin.|||Decreased binding to 'Lys-48' tetraubiquitin chains.|||Disordered|||Greatly impairs ubiquitin hydrolase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of binding to 'Lys-48' tetraubiquitin chains.|||No effect on binding to 'Lys-48' tetraubiquitin chains.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Ubiquitin carboxyl-terminal hydrolase MINDY-1|||Ubiquitin-binding|||Ubiquitin-binding domain (UBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344037|||http://purl.uniprot.org/annotation/VAR_044541|||http://purl.uniprot.org/annotation/VSP_034715|||http://purl.uniprot.org/annotation/VSP_037076|||http://purl.uniprot.org/annotation/VSP_037077
http://togogenome.org/gene/9606:TMEM30B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIR4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cell cycle control protein 50B|||Cytoplasmic|||Exoplasmic loop|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244474
http://togogenome.org/gene/9606:ACSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAP4|||http://purl.uniprot.org/uniprot/Q08AH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Acyl-coenzyme A synthetase ACSM1, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306091|||http://purl.uniprot.org/annotation/VAR_035245|||http://purl.uniprot.org/annotation/VAR_035246|||http://purl.uniprot.org/annotation/VAR_048238|||http://purl.uniprot.org/annotation/VSP_028391
http://togogenome.org/gene/9606:S1PR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95136                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In DFNB68.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069427|||http://purl.uniprot.org/annotation/VAR_076391|||http://purl.uniprot.org/annotation/VAR_076392
http://togogenome.org/gene/9606:AGPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3Q4|||http://purl.uniprot.org/uniprot/O00116                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Alkyldihydroxyacetonephosphate synthase, peroxisomal|||Basic and acidic residues|||Disordered|||FAD-binding PCMH-type|||Important for enzyme activity|||In RCDP3.|||In RCDP3; does not affect protein levels.|||In RCDP3; loss of enzyme activity.|||In RCDP3; severely reduced protein levels.|||N6-acetyllysine|||Peroxisome|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020431|||http://purl.uniprot.org/annotation/VAR_005002|||http://purl.uniprot.org/annotation/VAR_025895|||http://purl.uniprot.org/annotation/VAR_025896|||http://purl.uniprot.org/annotation/VAR_066929|||http://purl.uniprot.org/annotation/VAR_066930|||http://purl.uniprot.org/annotation/VAR_066931
http://togogenome.org/gene/9606:APOLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVN6|||http://purl.uniprot.org/uniprot/Q96LR9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Apolipoprotein L domain-containing protein 1|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247275|||http://purl.uniprot.org/annotation/VSP_019960
http://togogenome.org/gene/9606:SLC18A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54219|||http://purl.uniprot.org/uniprot/Q96GL6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chromaffin granule amine transporter|||Cytoplasmic|||Decreases the vesicular uptake of noradrenaline and dopamine.|||Decreases the vesicular uptake of noradrenaline, dopamine and serotonin; may predispose carriers to a increased cortical response to negative stimuli and reduced threat-related amygdala reactivity.|||Disordered|||Found in a patient with bipolar disorder; decreases the vesicular uptake of noradrenaline, dopamine and serotonin.|||Found in a patient with bipolar disorder; has no significant effect on monoamine vesicular uptake.|||Found in patients with bipolar disorder; decreases the vesicular uptake of noradrenaline, dopamine and serotonin.|||Found in patients with bipolar disorder; increases the vesicular uptake of noradrenaline and dopamine.|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal, vesicle|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127510|||http://purl.uniprot.org/annotation/VAR_012065|||http://purl.uniprot.org/annotation/VAR_020033|||http://purl.uniprot.org/annotation/VAR_021856|||http://purl.uniprot.org/annotation/VAR_024632|||http://purl.uniprot.org/annotation/VAR_024633|||http://purl.uniprot.org/annotation/VAR_024634|||http://purl.uniprot.org/annotation/VAR_024635|||http://purl.uniprot.org/annotation/VAR_024636|||http://purl.uniprot.org/annotation/VAR_024637|||http://purl.uniprot.org/annotation/VAR_029149|||http://purl.uniprot.org/annotation/VAR_029150|||http://purl.uniprot.org/annotation/VAR_029151|||http://purl.uniprot.org/annotation/VAR_052002|||http://purl.uniprot.org/annotation/VAR_087305|||http://purl.uniprot.org/annotation/VAR_087306|||http://purl.uniprot.org/annotation/VSP_046304|||http://purl.uniprot.org/annotation/VSP_046305
http://togogenome.org/gene/9606:HBD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N071|||http://purl.uniprot.org/uniprot/P02042                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit delta|||In Adria.|||In Agrinio.|||In Babinga.|||In Bagheria.|||In Campania.|||In Canada; O(2) affinity up.|||In Capri.|||In Catania.|||In Coburg.|||In Corfu/Troodos.|||In Delta'.|||In Etolia.|||In Fitzroy.|||In Flatbush.|||In Grovetown.|||In Honai.|||In Indonesia.|||In LiangCheng.|||In Lucania.|||In MUMC/Corleone.|||In Manzanares; unstable.|||In Melbourne.|||In Metaponto.|||In Monreale.|||In Montechiaro.|||In NYU.|||In Niigata.|||In Ninive.|||In Parkville.|||In Pelendri.|||In Puglia.|||In Pylos.|||In Roosevelt.|||In Sant' Antioco.|||In Sphakia.|||In Ventimiglia.|||In Victoria.|||In Wrens; unstable.|||In Yialousa.|||In Yokoshima.|||In Zagreb.|||In haplotype T11; Kenya.|||N-acetylalanine; in variant Niigata|||Phosphoserine|||Removed|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053167|||http://purl.uniprot.org/annotation/VAR_003096|||http://purl.uniprot.org/annotation/VAR_003097|||http://purl.uniprot.org/annotation/VAR_003098|||http://purl.uniprot.org/annotation/VAR_003099|||http://purl.uniprot.org/annotation/VAR_003100|||http://purl.uniprot.org/annotation/VAR_003101|||http://purl.uniprot.org/annotation/VAR_003102|||http://purl.uniprot.org/annotation/VAR_003103|||http://purl.uniprot.org/annotation/VAR_003104|||http://purl.uniprot.org/annotation/VAR_003105|||http://purl.uniprot.org/annotation/VAR_003106|||http://purl.uniprot.org/annotation/VAR_003107|||http://purl.uniprot.org/annotation/VAR_003108|||http://purl.uniprot.org/annotation/VAR_003109|||http://purl.uniprot.org/annotation/VAR_003110|||http://purl.uniprot.org/annotation/VAR_003111|||http://purl.uniprot.org/annotation/VAR_003112|||http://purl.uniprot.org/annotation/VAR_003113|||http://purl.uniprot.org/annotation/VAR_003114|||http://purl.uniprot.org/annotation/VAR_003115|||http://purl.uniprot.org/annotation/VAR_003116|||http://purl.uniprot.org/annotation/VAR_003117|||http://purl.uniprot.org/annotation/VAR_003118|||http://purl.uniprot.org/annotation/VAR_003119|||http://purl.uniprot.org/annotation/VAR_003120|||http://purl.uniprot.org/annotation/VAR_003121|||http://purl.uniprot.org/annotation/VAR_003122|||http://purl.uniprot.org/annotation/VAR_014277|||http://purl.uniprot.org/annotation/VAR_014278|||http://purl.uniprot.org/annotation/VAR_018740|||http://purl.uniprot.org/annotation/VAR_018741|||http://purl.uniprot.org/annotation/VAR_030499|||http://purl.uniprot.org/annotation/VAR_030500|||http://purl.uniprot.org/annotation/VAR_030501|||http://purl.uniprot.org/annotation/VAR_030502|||http://purl.uniprot.org/annotation/VAR_030503|||http://purl.uniprot.org/annotation/VAR_030504|||http://purl.uniprot.org/annotation/VAR_030505|||http://purl.uniprot.org/annotation/VAR_030506|||http://purl.uniprot.org/annotation/VAR_030507|||http://purl.uniprot.org/annotation/VAR_030508|||http://purl.uniprot.org/annotation/VAR_030509|||http://purl.uniprot.org/annotation/VAR_030510
http://togogenome.org/gene/9606:DDX56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY93                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Complete loss of interaction with IRF3. About 3-4 times less genomic RNA in West Nile virus particles.|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Probable ATP-dependent RNA helicase DDX56|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055058|||http://purl.uniprot.org/annotation/VSP_044869
http://togogenome.org/gene/9606:DHX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU66|||http://purl.uniprot.org/uniprot/Q08211                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase A|||Abolishes nuclear localization.|||Abrogates transcriptional activation and RNA polymerase II binding by the MTAD region. No change in ATP binding and ATPase activities.|||Abrogates transcriptional activation by the MTAD region. No change in RNA polymerase II holoenzyme binding.|||Asymmetric dimethylarginine|||Core helicase|||DEIH box|||DRBM 1|||DRBM 2|||Disordered|||Does not inhibit binding to origins of DNA replication.|||Does not inhibit binding to origins of DNA replication; when associated with A-511.|||Does not inhibit binding to origins of DNA replication; when associated with A-512.|||Does not reduce siRNA-binding and interaction with AGO2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HA2|||Helicase ATP-binding|||Helicase C-terminal|||Helicase-associated|||In isoform 2.|||Inhibits interaction with AGO2, DICER1 and TARBP2. Abrogates helicase activity and transcriptional activation. Does not inhibit binding to origins of DNA replication.|||Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-54.|||Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-53 and A-55.|||Inhibits siRNA-binding and decreases interaction with AGO2; when associated with A-54 and A-55.|||Inhibits siRNA-binding and interaction with AGO2.|||Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-235.|||Inhibits siRNA-binding and interaction with AGO2; when associated with A-234 and A-236.|||Inhibits siRNA-binding and interaction with AGO2; when associated with A-235 and A-236.|||Interaction with BRCA1|||Interaction with CREBBP|||Localizes in the cytoplasm and does not interact with the importin complex.|||Localizes in the nucleus and interacts with the importin complex.|||Localizes in the nucleus and the cytoplasm and interacts weakly with the importin complex.|||MTAD|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Necessary for interaction with H2AX|||Necessary for interaction with RNA polymerase II holoenzyme|||Nuclear localization signal (NLS1)|||Nuclear localization signal (NLS2)|||OB-fold|||Omega-N-methylarginine|||Phosphoserine|||RGG|||Reduces NUP98-induced mRNA transcription and alternative splicing activities.|||Reduces siRNA-binding and interaction with AGO2.|||Reduces siRNA-binding and interaction with AGO2; when associated with A-186.|||Reduces siRNA-binding and interaction with AGO2; when associated with A-187.|||Reduces siRNA-binding and interaction with AGO2; when associated with A-6.|||Reduces siRNA-binding; when associated with A-5.|||siRNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055157|||http://purl.uniprot.org/annotation/VAR_052179|||http://purl.uniprot.org/annotation/VSP_042314
http://togogenome.org/gene/9606:PKM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804F6T5|||http://purl.uniprot.org/uniprot/A0A804F729|||http://purl.uniprot.org/uniprot/B4DNK4|||http://purl.uniprot.org/uniprot/P14618|||http://purl.uniprot.org/uniprot/V9HWB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||Abolished acetylation by EP300. Abolished deacetylation by SIRT6.|||Abolished interaction with phosphorylated CTNNB1. Impaired phosphorylation of histone H3.|||Abolishes both pyruvate kinase and protein kinase activities.|||Abolishes serine binding and allosteric activation.|||Crucial for phosphotyrosine binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired homotetramerization, leading to homodimerization and subsequent activation of the protein kinase activity.|||In isoform 3.|||In isoform M1.|||Interaction with POU5F1|||Intersubunit contact|||Mimics acetylation, promoting homodimerization and ativation of the protein kinase activity.|||N-acetylserine|||N6,N6,N6-trimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pyruvate kinase C-terminal|||Pyruvate kinase PKM|||Pyruvate kinase barrel|||Removed|||Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-403.|||Significant reduction in hydroxylation and in PKM-mediated transcriptional activity of HIF1A; when associated with A-408.|||Transition state stabilizer|||Unable to bind FBP but still activated by serine.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112088|||http://purl.uniprot.org/annotation/VAR_033067|||http://purl.uniprot.org/annotation/VSP_011101|||http://purl.uniprot.org/annotation/VSP_043370
http://togogenome.org/gene/9606:MEFV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2DTW2|||http://purl.uniprot.org/uniprot/O15553                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Basic and acidic residues|||Benign variant; no effect on PYCARD/ASC inflammasome formation.|||Cleavage; by CASP1|||Disordered|||Does not form MEFV- and PSTPIP1-containing perinuclear specks.|||In ADFMF; severe.|||In ARFMF and ADFMF.|||In ARFMF and ADFMF; associated with Q-148 in some patients; no effect on PYCARD/ASC inflammasome formation; no effect on interaction with 14-3-3 proteins.|||In ARFMF and ADFMF; likely benign variant; associated with S-369 and Q-408 in cis; associated with I-694 in some patients.|||In ARFMF and ADFMF; reduced CASP1 interaction; decreased interaction with ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation; when associated with V-694 (PubMed:26347139); no effect on PYCARD/ASC inflammasome formation; no effect on interaction with 14-3-3 proteins.|||In ARFMF and ADFMF; very common mutation particularly in North African Jews; can be associated with amyloidosis development; reduced interaction with CASP1 and with ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation (PubMed:16785446) (PubMed:26347139); effect on autophagic NLRP3 degradation is increased; when associated with I-680; no effect on interaction with CASP1, CASP5, NLRP1, NLRP2 or NLRP3 (PubMed:17431422).|||In ARFMF.|||In ARFMF; associated with Q-148 and S-369 in cis.|||In ARFMF; common mutation; in Iraqi and Ashkenazi Jews, Druze, Armenians; reduced interaction with CASP1 and ULK1 and diminished NLRP3 degradation after induction of autophagy by starvation; when associated with I-680 and V-694; no effect on CASP1 activation; no effect on interaction with 14-3-3 proteins.|||In ARFMF; likely benign variant.|||In ARFMF; reduced penetrance among Ashkenazi Jews.|||In ARFMF; uncertain pathological significance.|||In ARFMF; unknown pathological significance.|||In ARFMF; unknown pathological significance; associated with Q-148 and Q-408 in cis.|||In ARFMF; unknown pathological significance; no effect on PYCARD/ASC inflammasome formation.|||In PAAND; results in constitutive inflammasome activation; increased PYCARD/ASC specks formation; increased caspase-1 activation and IL1B and IL18 production; decreased interaction with 14-3-3 proteins; no effect on interaction with PSTPIP1.|||In PAAND; results in constitutive inflammasome activation; increased PYCARD/ASC specks formation; increased caspase-1 activation and IL1B production; loss of S-242 phosphorylation; loss of interaction with 14-3-3 proteins.|||In isoform 2 and isoform 3.|||In isoform 3.|||In one patient with familial Mediterranean fever.|||Increased PYCARD/ASC specks formation. Decreased interaction with 14-3-3 proteins.|||Interaction with RELA|||Loss of cleavage by CASP1.|||Loss of interaction with 14-3-3 proteins.|||No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 397-I--H-404 and 470-Y--G-488.|||No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 397-I--H-404 and 523-S--D-530.|||No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 470-Y--G-488 and 523-S--D-530.|||No effect on PYCARD/ASC specks formation. Increased interaction with 14-3-3 proteins.|||No effect on PYCARD/ASC specks formation. No effect on interaction with 14-3-3 proteins.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in an autosomal dominant autoinflammatory disease with some similarities to familial Mediterranean fever.|||Pyrin|||Required for homotrimerization and induction of pyroptosomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220364|||http://purl.uniprot.org/annotation/VAR_009051|||http://purl.uniprot.org/annotation/VAR_009052|||http://purl.uniprot.org/annotation/VAR_009053|||http://purl.uniprot.org/annotation/VAR_009054|||http://purl.uniprot.org/annotation/VAR_009055|||http://purl.uniprot.org/annotation/VAR_009056|||http://purl.uniprot.org/annotation/VAR_009057|||http://purl.uniprot.org/annotation/VAR_009059|||http://purl.uniprot.org/annotation/VAR_009060|||http://purl.uniprot.org/annotation/VAR_009061|||http://purl.uniprot.org/annotation/VAR_009062|||http://purl.uniprot.org/annotation/VAR_009063|||http://purl.uniprot.org/annotation/VAR_009064|||http://purl.uniprot.org/annotation/VAR_009065|||http://purl.uniprot.org/annotation/VAR_009066|||http://purl.uniprot.org/annotation/VAR_009067|||http://purl.uniprot.org/annotation/VAR_016824|||http://purl.uniprot.org/annotation/VAR_016826|||http://purl.uniprot.org/annotation/VAR_016827|||http://purl.uniprot.org/annotation/VAR_016828|||http://purl.uniprot.org/annotation/VAR_016829|||http://purl.uniprot.org/annotation/VAR_016830|||http://purl.uniprot.org/annotation/VAR_024376|||http://purl.uniprot.org/annotation/VAR_028326|||http://purl.uniprot.org/annotation/VAR_028327|||http://purl.uniprot.org/annotation/VAR_028328|||http://purl.uniprot.org/annotation/VAR_028329|||http://purl.uniprot.org/annotation/VAR_028330|||http://purl.uniprot.org/annotation/VAR_028331|||http://purl.uniprot.org/annotation/VAR_028332|||http://purl.uniprot.org/annotation/VAR_028333|||http://purl.uniprot.org/annotation/VAR_028334|||http://purl.uniprot.org/annotation/VAR_028335|||http://purl.uniprot.org/annotation/VAR_028336|||http://purl.uniprot.org/annotation/VAR_028337|||http://purl.uniprot.org/annotation/VAR_028338|||http://purl.uniprot.org/annotation/VAR_028339|||http://purl.uniprot.org/annotation/VAR_028340|||http://purl.uniprot.org/annotation/VAR_028341|||http://purl.uniprot.org/annotation/VAR_028342|||http://purl.uniprot.org/annotation/VAR_028343|||http://purl.uniprot.org/annotation/VAR_028344|||http://purl.uniprot.org/annotation/VAR_028345|||http://purl.uniprot.org/annotation/VAR_028346|||http://purl.uniprot.org/annotation/VAR_028347|||http://purl.uniprot.org/annotation/VAR_028348|||http://purl.uniprot.org/annotation/VAR_028349|||http://purl.uniprot.org/annotation/VAR_028350|||http://purl.uniprot.org/annotation/VAR_028351|||http://purl.uniprot.org/annotation/VAR_028352|||http://purl.uniprot.org/annotation/VAR_028353|||http://purl.uniprot.org/annotation/VAR_048398|||http://purl.uniprot.org/annotation/VAR_070795|||http://purl.uniprot.org/annotation/VAR_070796|||http://purl.uniprot.org/annotation/VAR_070797|||http://purl.uniprot.org/annotation/VAR_070798|||http://purl.uniprot.org/annotation/VAR_072382|||http://purl.uniprot.org/annotation/VAR_072383|||http://purl.uniprot.org/annotation/VAR_072384|||http://purl.uniprot.org/annotation/VAR_072385|||http://purl.uniprot.org/annotation/VAR_072386|||http://purl.uniprot.org/annotation/VAR_084466|||http://purl.uniprot.org/annotation/VAR_084467|||http://purl.uniprot.org/annotation/VSP_008223|||http://purl.uniprot.org/annotation/VSP_047663
http://togogenome.org/gene/9606:SPO11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5K1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Meiotic recombination protein SPO11|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145474|||http://purl.uniprot.org/annotation/VAR_023307|||http://purl.uniprot.org/annotation/VAR_029246|||http://purl.uniprot.org/annotation/VAR_052596|||http://purl.uniprot.org/annotation/VAR_052597|||http://purl.uniprot.org/annotation/VSP_006533
http://togogenome.org/gene/9606:ASB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H672                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 7|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066935|||http://purl.uniprot.org/annotation/VSP_008919|||http://purl.uniprot.org/annotation/VSP_008920
http://togogenome.org/gene/9606:CALR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27797|||http://purl.uniprot.org/uniprot/V9HW88                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Motif|||Region|||Repeat|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||3 X approximate repeats|||4 X approximate repeats|||Acidic residues|||Basic and acidic residues|||C-domain|||Calreticulin|||Disordered|||Interaction with PPIB|||N-domain|||N-linked (GlcNAc...) asparagine|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||P-domain|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004173|||http://purl.uniprot.org/annotation/PRO_5014206132
http://togogenome.org/gene/9606:TLNRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1K6                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Removed|||Talin rod domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096441
http://togogenome.org/gene/9606:PTGES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14684                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Essential for protaglandin-E synthase activity|||Helical|||Keeps about 40-50% of prostaglandin-E synthase activity.|||Loss of prostaglandin-E synthase activity.|||Loss of prostaglandin-E synthase activity. Transforms prostaglandin-E synthase activity to prostaglandin-F(2alpha)synthase activity.|||Loss of protaglandin-E synthase activity.|||Lumenal|||No effect on protaglandin-E synthase activity.|||Prostaglandin E synthase|||Reduces protaglandin-E synthase activity by 50%.|||Reduces protaglandin-E synthase activity by 70%.|||Retains 17.8% of protaglandin-E synthase activity.|||Retains 21.3% activity of protaglandin-E synthase activity.|||Retains partial of protaglandin-E synthase activity.|||Slightly reduced protaglandin-E synthase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217745
http://togogenome.org/gene/9606:TRAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JF66|||http://purl.uniprot.org/uniprot/Q6PIZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with PIK3R1.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Interaction with PIK3R1|||Interchain|||Phosphoserine|||Phosphotyrosine|||Polar residues|||T-cell receptor-associated transmembrane adapter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083344|||http://purl.uniprot.org/annotation/VAR_062195|||http://purl.uniprot.org/annotation/VAR_062196
http://togogenome.org/gene/9606:CHMP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMN6|||http://purl.uniprot.org/uniprot/B3KRZ9|||http://purl.uniprot.org/uniprot/B3KUH0|||http://purl.uniprot.org/uniprot/Q8WUX9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Charged multivesicular body protein 7|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211516|||http://purl.uniprot.org/annotation/VSP_056945|||http://purl.uniprot.org/annotation/VSP_056946
http://togogenome.org/gene/9606:MTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13330|||http://purl.uniprot.org/uniprot/Q9BRL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BAH|||Disordered|||ELM2|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 3.|||In isoform Short.|||Interaction with RBBP4|||Loss of acetylation and transcriptional coactivator activity. Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-182.|||Metastasis-associated protein MTA1|||Metastasis-associated protein MTA1 R1|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Pro residues|||Reduced sumoylation and transcriptional corepressor activity.|||Reduced ubiquitination. Significant reduction in ubiquitination; when associated with A-626.|||SANT|||SH3-binding|||SUMO interaction motif 1 (SIM); crucial for efficient sumoylation|||Significant loss of interaction with SUMO1 and SUMO2 and reduced transcriptional corepressor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083493|||http://purl.uniprot.org/annotation/VAR_055847|||http://purl.uniprot.org/annotation/VAR_058965|||http://purl.uniprot.org/annotation/VSP_001601|||http://purl.uniprot.org/annotation/VSP_001602|||http://purl.uniprot.org/annotation/VSP_042207
http://togogenome.org/gene/9606:MYL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02045                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||Myosin light chain 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198745|||http://purl.uniprot.org/annotation/VAR_050459|||http://purl.uniprot.org/annotation/VSP_026448
http://togogenome.org/gene/9606:SLC16A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15374                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Monocarboxylate transporter 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211398|||http://purl.uniprot.org/annotation/VAR_020309|||http://purl.uniprot.org/annotation/VAR_053655|||http://purl.uniprot.org/annotation/VSP_046242|||http://purl.uniprot.org/annotation/VSP_046243|||http://purl.uniprot.org/annotation/VSP_046244|||http://purl.uniprot.org/annotation/VSP_046456|||http://purl.uniprot.org/annotation/VSP_046457|||http://purl.uniprot.org/annotation/VSP_046458
http://togogenome.org/gene/9606:IGDCC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDY8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Immunoglobulin superfamily DCC subclass member 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304622|||http://purl.uniprot.org/annotation/VAR_049966|||http://purl.uniprot.org/annotation/VAR_049967|||http://purl.uniprot.org/annotation/VAR_049968|||http://purl.uniprot.org/annotation/VAR_049969|||http://purl.uniprot.org/annotation/VAR_059391|||http://purl.uniprot.org/annotation/VSP_028046
http://togogenome.org/gene/9606:KRTAP19-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUB9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  26 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 19-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185221
http://togogenome.org/gene/9606:THBS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07996                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C-linked (Man) tryptophan|||Cell attachment site|||Disordered|||EGF-like 1|||EGF-like 2|||Heparin-binding|||In isoform 2.|||Interchain|||Involved in retention in extracellular matrix (ECM); involved in trimer formation|||Laminin G-like|||Loss of N-glycosylation site.|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||Reduces attachment to cells and retention in extracellular matrix (ECM); retention in ECM partially dependent on beta-1 integrin.|||Reduces attachment to cells and retention in extracellular matrix.|||TSP C-terminal|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-3 1|||TSP type-3 2|||TSP type-3 3|||TSP type-3 4|||TSP type-3 5|||TSP type-3 6|||TSP type-3 7|||TSP type-3 8|||Thrombospondin-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000205|||http://purl.uniprot.org/annotation/CAR_000206|||http://purl.uniprot.org/annotation/CAR_000207|||http://purl.uniprot.org/annotation/CAR_000208|||http://purl.uniprot.org/annotation/CAR_000209|||http://purl.uniprot.org/annotation/CAR_000210|||http://purl.uniprot.org/annotation/CAR_000211|||http://purl.uniprot.org/annotation/PRO_0000035842|||http://purl.uniprot.org/annotation/VAR_028938|||http://purl.uniprot.org/annotation/VAR_028939|||http://purl.uniprot.org/annotation/VAR_052657|||http://purl.uniprot.org/annotation/VSP_055757
http://togogenome.org/gene/9606:ADCY6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43306                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 6|||Cytoplasmic|||Extracellular|||Helical|||In LCCS8.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on basal enzyme activity, but increased enzyme activity upon activation via G-proteins or forskolin.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195699|||http://purl.uniprot.org/annotation/VAR_048249|||http://purl.uniprot.org/annotation/VAR_073434|||http://purl.uniprot.org/annotation/VSP_000244
http://togogenome.org/gene/9606:RNF146                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTX7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes the ability to recognize and bind PARsylated proteins.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF146|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Loss of iso-ADP-ribose-binding affinity.|||Loss of iso-ADP-ribose-binding.|||Minor effect on iso-ADP-ribose-binding.|||No effect on Wnt signaling pathway.|||Partially suppression of WNT3A signaling and stabilization of AXIN1, TNKS and TNKS2 with or without WNT3A induction. No effect on TNKS1-binding.|||Phosphoserine|||Polar residues|||RING-type|||Strong decrease in iso-ADP-ribose-binding affinity.|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056107|||http://purl.uniprot.org/annotation/VAR_065249|||http://purl.uniprot.org/annotation/VSP_012968
http://togogenome.org/gene/9606:MAP7D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K1JRJ6|||http://purl.uniprot.org/uniprot/A0A0K1JS24|||http://purl.uniprot.org/uniprot/A0A0M4F6E1|||http://purl.uniprot.org/uniprot/A0A0M4FLI9|||http://purl.uniprot.org/uniprot/Q96T17                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||MAP7 domain-containing protein 2|||N-acetylmethionine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306809|||http://purl.uniprot.org/annotation/VAR_035313|||http://purl.uniprot.org/annotation/VAR_035450|||http://purl.uniprot.org/annotation/VSP_028490|||http://purl.uniprot.org/annotation/VSP_028491|||http://purl.uniprot.org/annotation/VSP_028492|||http://purl.uniprot.org/annotation/VSP_028493|||http://purl.uniprot.org/annotation/VSP_043337|||http://purl.uniprot.org/annotation/VSP_044657|||http://purl.uniprot.org/annotation/VSP_044658
http://togogenome.org/gene/9606:KLHL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58EZ4|||http://purl.uniprot.org/uniprot/Q9P2J3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119110
http://togogenome.org/gene/9606:WDR97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NE52                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 97                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332994|||http://purl.uniprot.org/annotation/VAR_043029|||http://purl.uniprot.org/annotation/VAR_043030|||http://purl.uniprot.org/annotation/VAR_043031|||http://purl.uniprot.org/annotation/VSP_033425|||http://purl.uniprot.org/annotation/VSP_033426
http://togogenome.org/gene/9606:FLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20930                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Filaggrin|||Filaggrin 1|||Filaggrin 10|||Filaggrin 11|||Filaggrin 12|||Filaggrin 13|||Filaggrin 14|||Filaggrin 15|||Filaggrin 16|||Filaggrin 17|||Filaggrin 18|||Filaggrin 19|||Filaggrin 2|||Filaggrin 20|||Filaggrin 21|||Filaggrin 22|||Filaggrin 23|||Filaggrin 3|||Filaggrin 4|||Filaggrin 5|||Filaggrin 6|||Filaggrin 7|||Filaggrin 8|||Filaggrin 9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144036|||http://purl.uniprot.org/annotation/VAR_033931|||http://purl.uniprot.org/annotation/VAR_045968|||http://purl.uniprot.org/annotation/VAR_045969|||http://purl.uniprot.org/annotation/VAR_045970|||http://purl.uniprot.org/annotation/VAR_045971|||http://purl.uniprot.org/annotation/VAR_045972|||http://purl.uniprot.org/annotation/VAR_045973|||http://purl.uniprot.org/annotation/VAR_045974|||http://purl.uniprot.org/annotation/VAR_048472|||http://purl.uniprot.org/annotation/VAR_048473|||http://purl.uniprot.org/annotation/VAR_048474|||http://purl.uniprot.org/annotation/VAR_048475|||http://purl.uniprot.org/annotation/VAR_048476|||http://purl.uniprot.org/annotation/VAR_048477|||http://purl.uniprot.org/annotation/VAR_048478|||http://purl.uniprot.org/annotation/VAR_048479|||http://purl.uniprot.org/annotation/VAR_048480|||http://purl.uniprot.org/annotation/VAR_048481|||http://purl.uniprot.org/annotation/VAR_048482|||http://purl.uniprot.org/annotation/VAR_048483|||http://purl.uniprot.org/annotation/VAR_048484|||http://purl.uniprot.org/annotation/VAR_048485|||http://purl.uniprot.org/annotation/VAR_048486|||http://purl.uniprot.org/annotation/VAR_048487|||http://purl.uniprot.org/annotation/VAR_048488|||http://purl.uniprot.org/annotation/VAR_048489|||http://purl.uniprot.org/annotation/VAR_048490|||http://purl.uniprot.org/annotation/VAR_048491|||http://purl.uniprot.org/annotation/VAR_048492|||http://purl.uniprot.org/annotation/VAR_048493|||http://purl.uniprot.org/annotation/VAR_059155|||http://purl.uniprot.org/annotation/VAR_059156|||http://purl.uniprot.org/annotation/VAR_059157|||http://purl.uniprot.org/annotation/VAR_059158|||http://purl.uniprot.org/annotation/VAR_059159|||http://purl.uniprot.org/annotation/VAR_059160|||http://purl.uniprot.org/annotation/VAR_059161|||http://purl.uniprot.org/annotation/VAR_059162|||http://purl.uniprot.org/annotation/VAR_059163|||http://purl.uniprot.org/annotation/VAR_059164|||http://purl.uniprot.org/annotation/VAR_059165|||http://purl.uniprot.org/annotation/VAR_059166|||http://purl.uniprot.org/annotation/VAR_059167|||http://purl.uniprot.org/annotation/VAR_059168|||http://purl.uniprot.org/annotation/VAR_059169|||http://purl.uniprot.org/annotation/VAR_059170|||http://purl.uniprot.org/annotation/VAR_059171|||http://purl.uniprot.org/annotation/VAR_059172|||http://purl.uniprot.org/annotation/VAR_061049|||http://purl.uniprot.org/annotation/VAR_061050|||http://purl.uniprot.org/annotation/VAR_061051|||http://purl.uniprot.org/annotation/VAR_061052
http://togogenome.org/gene/9606:SNTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13425                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Beta-2-syntrophin|||Calmodulin-binding|||Disordered|||In isoform 2.|||PDZ|||PH 1|||PH 2|||Phosphoserine|||Pro residues|||SU                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184011|||http://purl.uniprot.org/annotation/VAR_014076|||http://purl.uniprot.org/annotation/VAR_073697|||http://purl.uniprot.org/annotation/VSP_006358|||http://purl.uniprot.org/annotation/VSP_006359
http://togogenome.org/gene/9606:OSBPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4L5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes plasma membrane targeting and nuclear localization.|||Decreases plasma membrane targeting and nuclear localization.|||Disordered|||FFAT 1|||FFAT 2|||In isoform 1b, isoform 1d, isoform 2b and isoform 2d.|||In isoform 1c, isoform 1d, isoform 2c and isoform 2d.|||In isoform 2a, isoform 2b, isoform 2c and isoform 2d.|||No effect on interaction with VAPA.|||Oxysterol-binding protein-related protein 3|||PH|||Phosphoserine|||Polar residues|||Reduces VAPA binding. Abolishes association with endoplasmic reticulum.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100371|||http://purl.uniprot.org/annotation/VAR_053548|||http://purl.uniprot.org/annotation/VSP_008219|||http://purl.uniprot.org/annotation/VSP_008220|||http://purl.uniprot.org/annotation/VSP_008221|||http://purl.uniprot.org/annotation/VSP_008222
http://togogenome.org/gene/9606:GRIK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13003                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutamate receptor ionotropic, kainate 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||In RNA edited version.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011547|||http://purl.uniprot.org/annotation/VAR_000308|||http://purl.uniprot.org/annotation/VAR_000309|||http://purl.uniprot.org/annotation/VAR_035695|||http://purl.uniprot.org/annotation/VAR_035696|||http://purl.uniprot.org/annotation/VSP_056588
http://togogenome.org/gene/9606:KLF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43474                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with ZNF296|||Interaction with target DNA|||Krueppel-like factor 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047167|||http://purl.uniprot.org/annotation/VAR_059888|||http://purl.uniprot.org/annotation/VAR_059889|||http://purl.uniprot.org/annotation/VSP_036399|||http://purl.uniprot.org/annotation/VSP_040569|||http://purl.uniprot.org/annotation/VSP_047470|||http://purl.uniprot.org/annotation/VSP_047471|||http://purl.uniprot.org/annotation/VSP_047472|||http://purl.uniprot.org/annotation/VSP_047473
http://togogenome.org/gene/9606:ASTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN99|||http://purl.uniprot.org/uniprot/B7ZKP4|||http://purl.uniprot.org/uniprot/B7ZKP5|||http://purl.uniprot.org/uniprot/O75129|||http://purl.uniprot.org/uniprot/X6R5P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes inositol-4,5-bisphosphate binding. Strongly reduces affinity for inositol-3,4,5-trisphosphate.|||Annexin-like|||Astrotactin-1/2 EGF-like and Fn(III)|||Astrotactin-2|||Astrotactin-2 C-terminal beta-hairpin|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibronectin type-III|||Found in a clear cell renal carcinoma case; somatic mutation.|||Found in a patient with global developmental delay; unknown pathological significance.|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308252|||http://purl.uniprot.org/annotation/VAR_036765|||http://purl.uniprot.org/annotation/VAR_036766|||http://purl.uniprot.org/annotation/VAR_036767|||http://purl.uniprot.org/annotation/VAR_036768|||http://purl.uniprot.org/annotation/VAR_064699|||http://purl.uniprot.org/annotation/VAR_084650|||http://purl.uniprot.org/annotation/VSP_028930|||http://purl.uniprot.org/annotation/VSP_028931|||http://purl.uniprot.org/annotation/VSP_028932|||http://purl.uniprot.org/annotation/VSP_028933|||http://purl.uniprot.org/annotation/VSP_028934|||http://purl.uniprot.org/annotation/VSP_028937
http://togogenome.org/gene/9606:FAM24B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5W8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Protein FAM24B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021224|||http://purl.uniprot.org/annotation/VAR_038485
http://togogenome.org/gene/9606:APLF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW19                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished interaction with XRCC5 and XRCC6.|||Abolished interaction with XRCC5 and XRCC6; impaired localization to the nucleus.|||Abolished interaction with XRCC5 and XRCC6; impaired localization to the nucleus; decreased ability to promote non-homologous end-joining (NHEJ).|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-421. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-421. Does not affect histone chaperone activity; when associated with A-376 and A-421.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-427. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-427. Does not affect histone chaperone activity; when associated with A-376 and A-427.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-421 and A-427. Does not affect histone chaperone activity; when associated with A-379; A-421 and A-427.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-385; A-421 and A-427. Does not affect histone chaperone activity; when associated with A-385; A-421 and A-427.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-421 and A-427. Does not affect histone chaperone activity; when associated with A-421 and A-427.|||Acidic residues|||Aprataxin and PNK-like factor|||Basic and acidic residues|||Decreases phosphorylation by ATM.|||Disordered|||Does not affect interaction with XRCC5 and XRCC6.|||Does not affect interaction with XRCC5 and XRCC6; decreased ability to promote non-homologous end-joining (NHEJ).|||FHA-like|||Flexible linker|||Impaired binding to histones and ability to mediate histone chaperone activity.|||KBM|||NAP1L motif|||PBZ-type 1|||PBZ-type 2|||Phosphoserine|||Phosphoserine; by ATM|||Polar residues|||Reduced interaction with XRCC5 and XRCC6.|||Reduced interaction with XRCC5 and XRCC6; impaired localization to the nucleus.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089342|||http://purl.uniprot.org/annotation/VAR_032299|||http://purl.uniprot.org/annotation/VAR_032300|||http://purl.uniprot.org/annotation/VAR_061557
http://togogenome.org/gene/9606:MRPL35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZE8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein bL35m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030525|||http://purl.uniprot.org/annotation/VAR_030010|||http://purl.uniprot.org/annotation/VAR_034463|||http://purl.uniprot.org/annotation/VAR_051803|||http://purl.uniprot.org/annotation/VAR_054632|||http://purl.uniprot.org/annotation/VAR_054633|||http://purl.uniprot.org/annotation/VAR_054634|||http://purl.uniprot.org/annotation/VSP_036507
http://togogenome.org/gene/9606:ANXA8L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13928|||http://purl.uniprot.org/uniprot/Q5VT79                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A8|||Annexin A8-like protein 1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067503|||http://purl.uniprot.org/annotation/PRO_0000328939|||http://purl.uniprot.org/annotation/VAR_000604|||http://purl.uniprot.org/annotation/VAR_030630|||http://purl.uniprot.org/annotation/VAR_048254|||http://purl.uniprot.org/annotation/VAR_067447|||http://purl.uniprot.org/annotation/VAR_067448|||http://purl.uniprot.org/annotation/VSP_052782|||http://purl.uniprot.org/annotation/VSP_052783|||http://purl.uniprot.org/annotation/VSP_052784|||http://purl.uniprot.org/annotation/VSP_056397|||http://purl.uniprot.org/annotation/VSP_056398|||http://purl.uniprot.org/annotation/VSP_057805
http://togogenome.org/gene/9606:SIN3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ST3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In WITKOS.|||Interaction with HCFC1|||Interaction with HDAC1 and ARID4B|||Interaction with NCOR1|||Interaction with OGT|||Interaction with REST|||Interaction with SAP30|||Interaction with SUDS3 and SAP130|||N6-acetyllysine|||PAH 1|||PAH 2|||PAH 3|||Paired amphipathic helix protein Sin3a|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121537|||http://purl.uniprot.org/annotation/VAR_062129|||http://purl.uniprot.org/annotation/VAR_081785
http://togogenome.org/gene/9606:PHF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Breakpoint for translocation to form NUP98-PHF23 oncogene|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||PHD finger protein 23|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302830|||http://purl.uniprot.org/annotation/VSP_027962|||http://purl.uniprot.org/annotation/VSP_027963|||http://purl.uniprot.org/annotation/VSP_056058|||http://purl.uniprot.org/annotation/VSP_057218
http://togogenome.org/gene/9606:ZNF641                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||KRAB|||Phosphoserine|||Polar residues|||Transactivation|||Zinc finger protein 641                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285301|||http://purl.uniprot.org/annotation/VAR_032009|||http://purl.uniprot.org/annotation/VAR_032010|||http://purl.uniprot.org/annotation/VSP_024867|||http://purl.uniprot.org/annotation/VSP_024868|||http://purl.uniprot.org/annotation/VSP_043422
http://togogenome.org/gene/9606:PROSER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Pro residues|||Proline and serine-rich protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089792|||http://purl.uniprot.org/annotation/VAR_023097|||http://purl.uniprot.org/annotation/VSP_014955
http://togogenome.org/gene/9606:CEP290                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PGB1|||http://purl.uniprot.org/uniprot/J3KNF5|||http://purl.uniprot.org/uniprot/O15078|||http://purl.uniprot.org/uniprot/Q05BJ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Centrosomal protein of 290 kDa|||Centrosomal protein of 290kDa coiled-coil region|||Disordered|||In JBTS5 and SLSN6.|||In JBTS5.|||In JBTS5; benign variant.|||In LCA10 and SLSN6.|||In LCA10, SLSN6 and MKS4.|||In LCA10.|||In LCA10; also found in a patient with night blindness and hearing loss.|||In LCA10; unknown pathological significance.|||In MKS4 and JBTS5.|||In MKS4; unknown pathological significance.|||Interaction with IQCB1|||Polar residues|||Self-association (with itself or C-terminus)|||Self-association (with itself or N-terminus)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089464|||http://purl.uniprot.org/annotation/VAR_028356|||http://purl.uniprot.org/annotation/VAR_031058|||http://purl.uniprot.org/annotation/VAR_031059|||http://purl.uniprot.org/annotation/VAR_031060|||http://purl.uniprot.org/annotation/VAR_031061|||http://purl.uniprot.org/annotation/VAR_064397|||http://purl.uniprot.org/annotation/VAR_064398|||http://purl.uniprot.org/annotation/VAR_064399|||http://purl.uniprot.org/annotation/VAR_064400|||http://purl.uniprot.org/annotation/VAR_064401|||http://purl.uniprot.org/annotation/VAR_066997|||http://purl.uniprot.org/annotation/VAR_067192|||http://purl.uniprot.org/annotation/VAR_068168|||http://purl.uniprot.org/annotation/VAR_075696|||http://purl.uniprot.org/annotation/VAR_087300|||http://purl.uniprot.org/annotation/VAR_087301|||http://purl.uniprot.org/annotation/VAR_087302|||http://purl.uniprot.org/annotation/VAR_087592|||http://purl.uniprot.org/annotation/VAR_087593|||http://purl.uniprot.org/annotation/VAR_087594|||http://purl.uniprot.org/annotation/VAR_087595|||http://purl.uniprot.org/annotation/VAR_087596
http://togogenome.org/gene/9606:ECT2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q008S8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DH|||Epithelial cell-transforming sequence 2 oncogene-like|||F-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336075|||http://purl.uniprot.org/annotation/VAR_043482|||http://purl.uniprot.org/annotation/VAR_043483|||http://purl.uniprot.org/annotation/VAR_051984
http://togogenome.org/gene/9606:REM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYK8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GTP-binding protein REM 2|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122483|||http://purl.uniprot.org/annotation/VAR_055938|||http://purl.uniprot.org/annotation/VSP_056922|||http://purl.uniprot.org/annotation/VSP_056923
http://togogenome.org/gene/9606:GNAQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50148                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl histamine|||Deamidated glutamine; by Photorhabdus PAU_02230|||Found in blue naevi and uveal melanoma samples; somatic mutation; constitutive activation.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(q) subunit alpha|||In SWS; found as somatic mosaic mutation in CMC; also found in melanocytomas sample; somatic mutation; shows significant activation of EPHB2 compared to control.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203760|||http://purl.uniprot.org/annotation/VAR_059319|||http://purl.uniprot.org/annotation/VAR_067270|||http://purl.uniprot.org/annotation/VAR_067271
http://togogenome.org/gene/9606:CRABP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0F7|||http://purl.uniprot.org/uniprot/P29762                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Cellular retinoic acid-binding protein 1|||Cytosolic fatty-acid binding proteins|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067406
http://togogenome.org/gene/9606:C1orf226                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L170                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Uncharacterized protein C1orf226                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334679|||http://purl.uniprot.org/annotation/VSP_040791
http://togogenome.org/gene/9606:NAV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2D6|||http://purl.uniprot.org/uniprot/Q8IVL1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Neuron navigator 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000267198|||http://purl.uniprot.org/annotation/VAR_029640|||http://purl.uniprot.org/annotation/VAR_029641|||http://purl.uniprot.org/annotation/VAR_029642|||http://purl.uniprot.org/annotation/VAR_029643|||http://purl.uniprot.org/annotation/VAR_032252|||http://purl.uniprot.org/annotation/VSP_021924|||http://purl.uniprot.org/annotation/VSP_021925|||http://purl.uniprot.org/annotation/VSP_021926|||http://purl.uniprot.org/annotation/VSP_021927|||http://purl.uniprot.org/annotation/VSP_021928|||http://purl.uniprot.org/annotation/VSP_021929|||http://purl.uniprot.org/annotation/VSP_021930|||http://purl.uniprot.org/annotation/VSP_021931|||http://purl.uniprot.org/annotation/VSP_021932|||http://purl.uniprot.org/annotation/VSP_021933|||http://purl.uniprot.org/annotation/VSP_021934|||http://purl.uniprot.org/annotation/VSP_021935|||http://purl.uniprot.org/annotation/VSP_021936|||http://purl.uniprot.org/annotation/VSP_021937|||http://purl.uniprot.org/annotation/VSP_021938
http://togogenome.org/gene/9606:TOX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94842                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||HMG box|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TOX high mobility group box family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048568|||http://purl.uniprot.org/annotation/VSP_053873|||http://purl.uniprot.org/annotation/VSP_055512
http://togogenome.org/gene/9606:HAPSTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CZ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased interaction with HUWE1. Loss of oligomerization. Increased proteasomal degradation. Loss of stabilization by HAPSTR2.|||Disordered|||HUWE1-associated protein modifying stress responses 1|||HUWE1-binding and HAPSTR1 oligomerization (HBO) domain|||In isoform 2.|||Loss of interaction with HUWE1. No effect on oligomerization.|||Loss of interaction with HUWE1. No effect on oligomerization. No effect on stabilization by HAPSTR2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297627|||http://purl.uniprot.org/annotation/VAR_034657|||http://purl.uniprot.org/annotation/VSP_061734
http://togogenome.org/gene/9606:UQCR10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UDW1                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 9|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193553|||http://purl.uniprot.org/annotation/VAR_052444|||http://purl.uniprot.org/annotation/VSP_041429
http://togogenome.org/gene/9606:SLC38A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99624                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Helical|||In DEE102.|||In DEE102; unknown pathological significance.|||Modulates L-glutamine-induced conductances and Na(+) binding|||N-linked (GlcNAc...) asparagine|||Sodium-coupled neutral amino acid transporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093828|||http://purl.uniprot.org/annotation/VAR_087292|||http://purl.uniprot.org/annotation/VAR_087293|||http://purl.uniprot.org/annotation/VAR_087294|||http://purl.uniprot.org/annotation/VAR_087295|||http://purl.uniprot.org/annotation/VAR_087296|||http://purl.uniprot.org/annotation/VAR_087297
http://togogenome.org/gene/9606:RNF125                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity in vitro.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-37.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-40.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-54.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-57.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-72.|||Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-75.|||Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro. Also abolishes myristoylation and membrane localization.|||C2HC RNF-type|||Disordered|||E3 ubiquitin-protein ligase RNF125|||In TNORS.|||Interaction with the C2HC RNF-type zinc finger|||Interaction with the RING-type zinc finger|||Linker region|||N-myristoyl glycine|||RING-type|||Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with P-217.|||Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with Q-221.|||Removed|||Required for interaction with ubiquitin and for autoubiquitination                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056090|||http://purl.uniprot.org/annotation/VAR_073353|||http://purl.uniprot.org/annotation/VAR_073354|||http://purl.uniprot.org/annotation/VAR_073355
http://togogenome.org/gene/9606:CFAP44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MT7|||http://purl.uniprot.org/uniprot/Q9NUU0|||http://purl.uniprot.org/uniprot/Q9UF55                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cilia- and flagella-associated protein 44|||Disordered|||In SPGF20.|||In isoform 1.|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305102|||http://purl.uniprot.org/annotation/VAR_053435|||http://purl.uniprot.org/annotation/VAR_062105|||http://purl.uniprot.org/annotation/VAR_080886|||http://purl.uniprot.org/annotation/VAR_080887|||http://purl.uniprot.org/annotation/VSP_059893|||http://purl.uniprot.org/annotation/VSP_059894
http://togogenome.org/gene/9606:ELK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19419|||http://purl.uniprot.org/uniprot/Q86SR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  17% reduction in ternary complex formation.|||34% reduction in ternary complex formation.|||9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation.|||9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation.|||Basic and acidic residues|||Disordered|||ETS|||ETS domain-containing protein Elk-1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||No effect on ternary complex formation but loss of transcriptional activity positive regulation by MAD2L2.|||No effect on ternary complex formation.|||Phosphoserine; by MAPK1|||Phosphoserine; by MAPK1 and MAPK8|||Phosphothreonine; by MAPK1|||Reduction in sumoylation.|||Slight reduction in ternary complex formation.|||Sufficient for interaction with MAD2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204095|||http://purl.uniprot.org/annotation/VAR_017108|||http://purl.uniprot.org/annotation/VAR_017109|||http://purl.uniprot.org/annotation/VSP_001466|||http://purl.uniprot.org/annotation/VSP_001467
http://togogenome.org/gene/9606:HMGN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00479                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic and acidic residues|||Disordered|||High mobility group nucleosome-binding domain-containing protein 4|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206704
http://togogenome.org/gene/9606:ACE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYF1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SARS-CoV spike glycoprotein.|||About 50% loss of angiotensin I cleavage but two-fold greater activity with angiotensin II.|||About 80% loss of angiotensin I cleavage.|||About 95% loss of angiotensin I cleavage.|||Angiotensin-converting enzyme 2|||Collectrin-like|||Complete loss of enzyme activity.|||Complete loss of enzyme activity. Does not affect amino acid transport activity of SLC6A19.|||Cytoplasmic|||Disordered|||Endocytic sorting signal|||Essential for cleavage by ADAM17|||Essential for cleavage by TMPRSS11D and TMPRSS2|||Extracellular|||Helical|||In isoform 2.|||Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein.|||Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and L-386.|||Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and Y-330.|||Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-330 and L-386.|||Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein.|||Inhibits interaction with SARS-CoV spike glycoprotein.|||Interaction with SARS-CoV spike glycoprotein|||LIR|||Loss of interaction with NHERF1.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with SARS-CoV spike glycoprotein.|||PDZ-binding|||PTB|||Peptidase M2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Processed angiotensin-converting enzyme 2|||Proton acceptor|||Proton donor|||SH2-binding|||Slightly inhibits interaction with SARS-CoV spike glycoprotein.|||Strongly inhibits interaction with SARS-CoV spike glycoprotein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028570|||http://purl.uniprot.org/annotation/PRO_0000292268|||http://purl.uniprot.org/annotation/VAR_023082|||http://purl.uniprot.org/annotation/VAR_023083|||http://purl.uniprot.org/annotation/VAR_083726|||http://purl.uniprot.org/annotation/VAR_083727|||http://purl.uniprot.org/annotation/VSP_060903
http://togogenome.org/gene/9606:TWIST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVJ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In AMS; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type.|||In BBRSAY; decreased chromatin binding; the mutant binds to alternative chromatin binding sites compared to wild-type.|||In FFDD3.|||Twist-related protein 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127489|||http://purl.uniprot.org/annotation/VAR_072927|||http://purl.uniprot.org/annotation/VAR_074674|||http://purl.uniprot.org/annotation/VAR_074675|||http://purl.uniprot.org/annotation/VAR_074676|||http://purl.uniprot.org/annotation/VAR_074677
http://togogenome.org/gene/9606:VILL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15195                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||In isoform 2.|||Polar residues|||Villin-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218738|||http://purl.uniprot.org/annotation/VAR_052938|||http://purl.uniprot.org/annotation/VAR_052939|||http://purl.uniprot.org/annotation/VAR_081640|||http://purl.uniprot.org/annotation/VSP_006729
http://togogenome.org/gene/9606:ERICH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TMA0|||http://purl.uniprot.org/uniprot/A0A8V8TMB5|||http://purl.uniprot.org/uniprot/A1L162                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glutamate-rich protein 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346762
http://togogenome.org/gene/9606:CTSG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08311                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin G|||Cathepsin G, C-terminal truncated form|||Charge relay system|||Important for antimicrobial activity|||N-linked (GlcNAc...) (complex) asparagine; alternate|||N-linked (GlcNAc...) (paucimannose) asparagine; alternate|||No effect on proteolytic processing, enzyme activation or sorting to cytoplasmic granules.|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027512|||http://purl.uniprot.org/annotation/PRO_0000027513|||http://purl.uniprot.org/annotation/PRO_0000454551|||http://purl.uniprot.org/annotation/PRO_0000454552|||http://purl.uniprot.org/annotation/VAR_006491
http://togogenome.org/gene/9606:NUCB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80303                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Binds to necdin|||Disordered|||EF-hand 1|||EF-hand 2|||GBA|||In isoform 2.|||Nesfatin-1|||Nucleobindin-2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004165|||http://purl.uniprot.org/annotation/PRO_0000419819|||http://purl.uniprot.org/annotation/VAR_020923|||http://purl.uniprot.org/annotation/VAR_024399|||http://purl.uniprot.org/annotation/VSP_036450
http://togogenome.org/gene/9606:KCNQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51787|||http://purl.uniprot.org/uniprot/Q96AI9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal assembly domain|||Cytoplasmic|||Disordered|||Does not interact with AKAP9 and the kinase A (PKA) catalytic subunit and protein phosphatase 1 (PP1); when associated with L-602.|||Does not interact with AKAP9 and the targeting protein kinase A (PKA) catalytic subunit and protein phosphatase 1 (PP1); when associated with I-609.|||Extracellular|||Has a voltage-gated potassium channel activity. Disrupts KCNE4-mediated voltage-gated potassium channel activity inhibition.|||Has a voltage-gated potassium channel activity. Inhibition of voltage-gated potassium channel activity by KCNE4.|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In ATFB3; gain of function.|||In JLNS1 and LQT1; impairs outward potassium current; affects plasma membrane localization.|||In JLNS1.|||In JLNS1; minor changes of wt current (homomultimers); positive voltage shift of the channel activation (heteromultimers).|||In JLNS1; requires 2 nucleotide substitutions; does not affect plasma membrane localization; complete loss of outward currents; enhances outward currents when coexpressed with wild type at equimolar ratio.|||In LQT1 and JLNS1; affects plasma membrane localization; strongly reduces potassium current; impairs binding to AKAP9 and the targeting protein kinase A (PKA) catalytic subunit and protein phosphatase 1 (PP1).|||In LQT1 and JLNS1; impairs outward potassium current; affects plasma membrane localization.|||In LQT1.|||In LQT1; affects channel activity; when expressed in heterologous system the mutant significantly reduces total IKs steady-state and tail currents with a positive shift of the voltage dependence of activation.|||In LQT1; associated with M-254 in a patient.|||In LQT1; associated with M-417 in a patient.|||In LQT1; associated with a fruste phenotype; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; shifts activation of the voltage dependence; deactivates more rapidly; impairs binding with phosphatidylinositol 4,5-bisphosphate.|||In LQT1; benign variant.|||In LQT1; complete loss of outward potassium current when expressed alone and even in the presence of the wild type at variable ratios; decreases plasma membrane localization.|||In LQT1; complete loss of outward potassium current; enhances outward potassium current when co-transfected with wild type; decreases plasma membrane localization.|||In LQT1; decreases IKs amplitude; accelerates the IKs deactivation; effect on plasma membrane localization; reduces up-regulation of Iks through PKA activation.|||In LQT1; decreases delayed rectifier potassium current Iks; prevents the up-regulation of Iks through PKA activation.|||In LQT1; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; impairs binding with Phosphatidylinositol 4,5-bisphosphate.|||In LQT1; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; reduces IKS current density; impairs binding with phosphatidylinositol 4,5-bisphosphate; loss of channel activity.|||In LQT1; decreases outward potassium current; decreases plasma membrane localization.|||In LQT1; familial sudden death.|||In LQT1; functional channel with reduced macroscopic conductance (homomultimers); alteration of normal KVLQT1 function (mut/wt homomultimers).|||In LQT1; loss of channel activity and no interaction with wt KVLQT1 or MINK subunits.|||In LQT1; loss of channel activity.|||In LQT1; loss of function mutation acting in a dominant-negative manner.|||In LQT1; minor changes of wt current (homomultimers); positive voltage shift of the channel activation (heteromultimers).|||In LQT1; no effect on cell membrane localization; slows activation kinetics; accelerates deactivation kinetics; rightshifts the voltage-dependent activation; does not affect cAMP-dependent up-regulation; decreases interaction with KCNE1 C-terminus; does not affect plasma membrane localization; does not affect phosphorylation at S-27 during cAMP-dependent stimulation; reduces IKS current density; impairs binding with Phosphatidylinositol 4,5-bisphosphate.|||In LQT1; reduces IKs density and causes a right-shift of the current?voltage relation of channel activation; reduces cell surface expression; no effect on interaction with AKAP9; does not affect the cAMP-dependent IKs up-regulation.|||In LQT1; slower rate of activation and voltage dependence of activation-inactivation shifted to more positive potentials (homomultimers); channels non-functional (heteromultimers).|||In LQT1; unknown pathological significance.|||In LQT1; unknown pathological significance; hardly any effect on channel activity, shows fast activation.|||In LQT1; unknown pathological significance; no effect on channel activity.|||In SQT2; gain of function.|||In isoform 2.|||Inhibits voltage-gated potassium channel activity.|||Interaction with AKAP9|||Interaction with CALM|||Interaction with CALM; calcium-dependent|||Interaction with KCNE1 C-terminus|||N-linked (GlcNAc...) asparagine|||No effect.|||No phosphorylation by PKA. Decreases delayed rectifier potassium channel activity.|||Phosphoserine|||Phosphoserine; by PKA|||Pore-forming; Name=Segment H5|||Potassium channel|||Potassium channel voltage dependent KCNQ C-terminal|||Potassium voltage-gated channel subfamily KQT member 1|||Pro residues|||Reduced cell surface expression and moderately reduced potassium current.|||Reduced cell surface expression and strongly reduced potassium current.|||Reduced protein expression, probably due to misfolding and proteasomal degradation. No detectable electrophysiological activity. Reduced electrophysiological activity in the presence of KCNE1.|||Reduced protein expression, probably due to misfolding and proteasomal degradation. Significantly reduced electrophysiological activity. Reduced electrophysiological activity in the presence of KCNE1.|||Selectivity filter|||Strongly inhibits SLC5A3 transporter activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054022|||http://purl.uniprot.org/annotation/VAR_001515|||http://purl.uniprot.org/annotation/VAR_001516|||http://purl.uniprot.org/annotation/VAR_001517|||http://purl.uniprot.org/annotation/VAR_001518|||http://purl.uniprot.org/annotation/VAR_001519|||http://purl.uniprot.org/annotation/VAR_001520|||http://purl.uniprot.org/annotation/VAR_001521|||http://purl.uniprot.org/annotation/VAR_001522|||http://purl.uniprot.org/annotation/VAR_001523|||http://purl.uniprot.org/annotation/VAR_001524|||http://purl.uniprot.org/annotation/VAR_001525|||http://purl.uniprot.org/annotation/VAR_001526|||http://purl.uniprot.org/annotation/VAR_001527|||http://purl.uniprot.org/annotation/VAR_001528|||http://purl.uniprot.org/annotation/VAR_001529|||http://purl.uniprot.org/annotation/VAR_001530|||http://purl.uniprot.org/annotation/VAR_001531|||http://purl.uniprot.org/annotation/VAR_001532|||http://purl.uniprot.org/annotation/VAR_001533|||http://purl.uniprot.org/annotation/VAR_001534|||http://purl.uniprot.org/annotation/VAR_001535|||http://purl.uniprot.org/annotation/VAR_001536|||http://purl.uniprot.org/annotation/VAR_001537|||http://purl.uniprot.org/annotation/VAR_001538|||http://purl.uniprot.org/annotation/VAR_001539|||http://purl.uniprot.org/annotation/VAR_001540|||http://purl.uniprot.org/annotation/VAR_001541|||http://purl.uniprot.org/annotation/VAR_001542|||http://purl.uniprot.org/annotation/VAR_001543|||http://purl.uniprot.org/annotation/VAR_001544|||http://purl.uniprot.org/annotation/VAR_001545|||http://purl.uniprot.org/annotation/VAR_008124|||http://purl.uniprot.org/annotation/VAR_008125|||http://purl.uniprot.org/annotation/VAR_008126|||http://purl.uniprot.org/annotation/VAR_008127|||http://purl.uniprot.org/annotation/VAR_008128|||http://purl.uniprot.org/annotation/VAR_008939|||http://purl.uniprot.org/annotation/VAR_008940|||http://purl.uniprot.org/annotation/VAR_008941|||http://purl.uniprot.org/annotation/VAR_008942|||http://purl.uniprot.org/annotation/VAR_008943|||http://purl.uniprot.org/annotation/VAR_008944|||http://purl.uniprot.org/annotation/VAR_008945|||http://purl.uniprot.org/annotation/VAR_008946|||http://purl.uniprot.org/annotation/VAR_008947|||http://purl.uniprot.org/annotation/VAR_008948|||http://purl.uniprot.org/annotation/VAR_008949|||http://purl.uniprot.org/annotation/VAR_008950|||http://purl.uniprot.org/annotation/VAR_008951|||http://purl.uniprot.org/annotation/VAR_008952|||http://purl.uniprot.org/annotation/VAR_008953|||http://purl.uniprot.org/annotation/VAR_008954|||http://purl.uniprot.org/annotation/VAR_009180|||http://purl.uniprot.org/annotation/VAR_009181|||http://purl.uniprot.org/annotation/VAR_009917|||http://purl.uniprot.org/annotation/VAR_009918|||http://purl.uniprot.org/annotation/VAR_009919|||http://purl.uniprot.org/annotation/VAR_009920|||http://purl.uniprot.org/annotation/VAR_009921|||http://purl.uniprot.org/annotation/VAR_009922|||http://purl.uniprot.org/annotation/VAR_009923|||http://purl.uniprot.org/annotation/VAR_009924|||http://purl.uniprot.org/annotation/VAR_009925|||http://purl.uniprot.org/annotation/VAR_009926|||http://purl.uniprot.org/annotation/VAR_009927|||http://purl.uniprot.org/annotation/VAR_009928|||http://purl.uniprot.org/annotation/VAR_009929|||http://purl.uniprot.org/annotation/VAR_009930|||http://purl.uniprot.org/annotation/VAR_009931|||http://purl.uniprot.org/annotation/VAR_009932|||http://purl.uniprot.org/annotation/VAR_009933|||http://purl.uniprot.org/annotation/VAR_009934|||http://purl.uniprot.org/annotation/VAR_010933|||http://purl.uniprot.org/annotation/VAR_010934|||http://purl.uniprot.org/annotation/VAR_015742|||http://purl.uniprot.org/annotation/VAR_023841|||http://purl.uniprot.org/annotation/VAR_048025|||http://purl.uniprot.org/annotation/VAR_048026|||http://purl.uniprot.org/annotation/VAR_065777|||http://purl.uniprot.org/annotation/VAR_065778|||http://purl.uniprot.org/annotation/VAR_068287|||http://purl.uniprot.org/annotation/VAR_068288|||http://purl.uniprot.org/annotation/VAR_068289|||http://purl.uniprot.org/annotation/VAR_068290|||http://purl.uniprot.org/annotation/VAR_068291|||http://purl.uniprot.org/annotation/VAR_068292|||http://purl.uniprot.org/annotation/VAR_068293|||http://purl.uniprot.org/annotation/VAR_068294|||http://purl.uniprot.org/annotation/VAR_068295|||http://purl.uniprot.org/annotation/VAR_068296|||http://purl.uniprot.org/annotation/VAR_068297|||http://purl.uniprot.org/annotation/VAR_068298|||http://purl.uniprot.org/annotation/VAR_068299|||http://purl.uniprot.org/annotation/VAR_068300|||http://purl.uniprot.org/annotation/VAR_068301|||http://purl.uniprot.org/annotation/VAR_068302|||http://purl.uniprot.org/annotation/VAR_068303|||http://purl.uniprot.org/annotation/VAR_068304|||http://purl.uniprot.org/annotation/VAR_068305|||http://purl.uniprot.org/annotation/VAR_068306|||http://purl.uniprot.org/annotation/VAR_068307|||http://purl.uniprot.org/annotation/VAR_068308|||http://purl.uniprot.org/annotation/VAR_068309|||http://purl.uniprot.org/annotation/VAR_068310|||http://purl.uniprot.org/annotation/VAR_068311|||http://purl.uniprot.org/annotation/VAR_068312|||http://purl.uniprot.org/annotation/VAR_068313|||http://purl.uniprot.org/annotation/VAR_068314|||http://purl.uniprot.org/annotation/VAR_068315|||http://purl.uniprot.org/annotation/VAR_068316|||http://purl.uniprot.org/annotation/VAR_068317|||http://purl.uniprot.org/annotation/VAR_068318|||http://purl.uniprot.org/annotation/VAR_068319|||http://purl.uniprot.org/annotation/VAR_068320|||http://purl.uniprot.org/annotation/VAR_068321|||http://purl.uniprot.org/annotation/VAR_068322|||http://purl.uniprot.org/annotation/VAR_068323|||http://purl.uniprot.org/annotation/VAR_068324|||http://purl.uniprot.org/annotation/VAR_074687|||http://purl.uniprot.org/annotation/VAR_074688|||http://purl.uniprot.org/annotation/VAR_074689|||http://purl.uniprot.org/annotation/VAR_074690|||http://purl.uniprot.org/annotation/VAR_074691|||http://purl.uniprot.org/annotation/VAR_074692|||http://purl.uniprot.org/annotation/VAR_074693|||http://purl.uniprot.org/annotation/VAR_074694|||http://purl.uniprot.org/annotation/VAR_074927|||http://purl.uniprot.org/annotation/VAR_074928|||http://purl.uniprot.org/annotation/VAR_074929|||http://purl.uniprot.org/annotation/VAR_074930|||http://purl.uniprot.org/annotation/VAR_074931|||http://purl.uniprot.org/annotation/VAR_074932|||http://purl.uniprot.org/annotation/VAR_074933|||http://purl.uniprot.org/annotation/VAR_074934|||http://purl.uniprot.org/annotation/VAR_074935|||http://purl.uniprot.org/annotation/VAR_074936|||http://purl.uniprot.org/annotation/VAR_074937|||http://purl.uniprot.org/annotation/VAR_074938|||http://purl.uniprot.org/annotation/VAR_074939|||http://purl.uniprot.org/annotation/VAR_074940|||http://purl.uniprot.org/annotation/VAR_074941|||http://purl.uniprot.org/annotation/VAR_074942|||http://purl.uniprot.org/annotation/VAR_074943|||http://purl.uniprot.org/annotation/VAR_074944|||http://purl.uniprot.org/annotation/VAR_074945|||http://purl.uniprot.org/annotation/VAR_074946|||http://purl.uniprot.org/annotation/VAR_074947|||http://purl.uniprot.org/annotation/VAR_074948|||http://purl.uniprot.org/annotation/VAR_074949|||http://purl.uniprot.org/annotation/VAR_074950|||http://purl.uniprot.org/annotation/VAR_074951|||http://purl.uniprot.org/annotation/VAR_074952|||http://purl.uniprot.org/annotation/VAR_074953|||http://purl.uniprot.org/annotation/VAR_074954|||http://purl.uniprot.org/annotation/VAR_074955|||http://purl.uniprot.org/annotation/VAR_074956|||http://purl.uniprot.org/annotation/VAR_074957|||http://purl.uniprot.org/annotation/VAR_074958|||http://purl.uniprot.org/annotation/VAR_074959|||http://purl.uniprot.org/annotation/VAR_074960|||http://purl.uniprot.org/annotation/VAR_074961|||http://purl.uniprot.org/annotation/VAR_074962|||http://purl.uniprot.org/annotation/VAR_074963|||http://purl.uniprot.org/annotation/VAR_074964|||http://purl.uniprot.org/annotation/VAR_074965|||http://purl.uniprot.org/annotation/VAR_074966|||http://purl.uniprot.org/annotation/VAR_074967|||http://purl.uniprot.org/annotation/VAR_074968|||http://purl.uniprot.org/annotation/VAR_074969|||http://purl.uniprot.org/annotation/VAR_074970|||http://purl.uniprot.org/annotation/VAR_074971|||http://purl.uniprot.org/annotation/VAR_074972|||http://purl.uniprot.org/annotation/VAR_074973|||http://purl.uniprot.org/annotation/VAR_074974|||http://purl.uniprot.org/annotation/VAR_074975|||http://purl.uniprot.org/annotation/VAR_074976|||http://purl.uniprot.org/annotation/VAR_074977|||http://purl.uniprot.org/annotation/VAR_074978|||http://purl.uniprot.org/annotation/VAR_074979|||http://purl.uniprot.org/annotation/VAR_074980|||http://purl.uniprot.org/annotation/VAR_074981|||http://purl.uniprot.org/annotation/VAR_074982|||http://purl.uniprot.org/annotation/VAR_074983|||http://purl.uniprot.org/annotation/VAR_074984|||http://purl.uniprot.org/annotation/VAR_074985|||http://purl.uniprot.org/annotation/VAR_074986|||http://purl.uniprot.org/annotation/VAR_074987|||http://purl.uniprot.org/annotation/VAR_074988|||http://purl.uniprot.org/annotation/VAR_074989|||http://purl.uniprot.org/annotation/VAR_074990|||http://purl.uniprot.org/annotation/VAR_074991|||http://purl.uniprot.org/annotation/VAR_074992|||http://purl.uniprot.org/annotation/VAR_074993|||http://purl.uniprot.org/annotation/VAR_074994|||http://purl.uniprot.org/annotation/VAR_074995|||http://purl.uniprot.org/annotation/VAR_074996|||http://purl.uniprot.org/annotation/VAR_074997|||http://purl.uniprot.org/annotation/VAR_074998|||http://purl.uniprot.org/annotation/VAR_074999|||http://purl.uniprot.org/annotation/VAR_075000|||http://purl.uniprot.org/annotation/VAR_075001|||http://purl.uniprot.org/annotation/VAR_075002|||http://purl.uniprot.org/annotation/VAR_075003|||http://purl.uniprot.org/annotation/VAR_075004|||http://purl.uniprot.org/annotation/VAR_075005|||http://purl.uniprot.org/annotation/VAR_075006|||http://purl.uniprot.org/annotation/VAR_075007|||http://purl.uniprot.org/annotation/VAR_075008|||http://purl.uniprot.org/annotation/VAR_075009|||http://purl.uniprot.org/annotation/VAR_075010|||http://purl.uniprot.org/annotation/VAR_075011|||http://purl.uniprot.org/annotation/VAR_075012|||http://purl.uniprot.org/annotation/VAR_075013|||http://purl.uniprot.org/annotation/VAR_075014|||http://purl.uniprot.org/annotation/VAR_075015|||http://purl.uniprot.org/annotation/VAR_075016|||http://purl.uniprot.org/annotation/VAR_075017|||http://purl.uniprot.org/annotation/VAR_075018|||http://purl.uniprot.org/annotation/VAR_075019|||http://purl.uniprot.org/annotation/VAR_075020|||http://purl.uniprot.org/annotation/VAR_075021|||http://purl.uniprot.org/annotation/VAR_075022|||http://purl.uniprot.org/annotation/VAR_075023|||http://purl.uniprot.org/annotation/VAR_075024|||http://purl.uniprot.org/annotation/VAR_075025|||http://purl.uniprot.org/annotation/VAR_075026|||http://purl.uniprot.org/annotation/VAR_075027|||http://purl.uniprot.org/annotation/VAR_075028|||http://purl.uniprot.org/annotation/VAR_075029|||http://purl.uniprot.org/annotation/VAR_075030|||http://purl.uniprot.org/annotation/VAR_075031|||http://purl.uniprot.org/annotation/VAR_075032|||http://purl.uniprot.org/annotation/VAR_075033|||http://purl.uniprot.org/annotation/VAR_075034|||http://purl.uniprot.org/annotation/VAR_075035|||http://purl.uniprot.org/annotation/VAR_080331|||http://purl.uniprot.org/annotation/VAR_080332|||http://purl.uniprot.org/annotation/VAR_080333|||http://purl.uniprot.org/annotation/VAR_080334|||http://purl.uniprot.org/annotation/VAR_080335|||http://purl.uniprot.org/annotation/VSP_000981|||http://purl.uniprot.org/annotation/VSP_000982
http://togogenome.org/gene/9606:NRIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LXXLL motif|||Nuclear receptor-interacting protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271056|||http://purl.uniprot.org/annotation/VSP_053930
http://togogenome.org/gene/9606:OR2G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVX0|||http://purl.uniprot.org/uniprot/Q8NGZ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2G3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150477|||http://purl.uniprot.org/annotation/VAR_034178|||http://purl.uniprot.org/annotation/VAR_053141
http://togogenome.org/gene/9606:SULT1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50226                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Proton acceptor|||Sulfotransferase 1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085128|||http://purl.uniprot.org/annotation/VAR_007426|||http://purl.uniprot.org/annotation/VAR_007427|||http://purl.uniprot.org/annotation/VAR_057340|||http://purl.uniprot.org/annotation/VAR_057341|||http://purl.uniprot.org/annotation/VAR_057342|||http://purl.uniprot.org/annotation/VAR_061887
http://togogenome.org/gene/9606:RAB31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13636                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||No change in GTPase activity.|||Phosphoserine|||Ras-related protein Rab-31|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121232
http://togogenome.org/gene/9606:ARMCX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L4S7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence|||Protein ARMCX6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191374
http://togogenome.org/gene/9606:FAIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVQ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fas apoptotic inhibitory molecule 1|||In isoform 2.|||In isoform 3.|||N-acetylthreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087173|||http://purl.uniprot.org/annotation/VAR_024314|||http://purl.uniprot.org/annotation/VAR_024315|||http://purl.uniprot.org/annotation/VSP_008991|||http://purl.uniprot.org/annotation/VSP_038095
http://togogenome.org/gene/9606:MCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT64|||http://purl.uniprot.org/uniprot/C8YZ26|||http://purl.uniprot.org/uniprot/Q07820                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Abolishes formation of 23 and 21 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-127.|||Abolishes formation of 28 and 17 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-157.|||Abolishes mitochondrial localization and decreases stability.|||Abolishes phosphorylation by MAPK. No effect on phosphorylation induced by okadaic acid or taxol.|||BH1|||BH2|||BH3|||Bcl-2 Bcl-2 homology region 1-3|||Cleavage; by caspase-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Induced myeloid leukemia cell differentiation protein Mcl-1|||Loss of phosphorylation by GSK3 and loss of ubiquitination increasing protein stability.|||No effect on mitochondrial localization.|||No effect on ubiquitination.|||No effect.|||PEST-like|||Phosphoserine|||Phosphoserine; by GSK3-alpha and GSK3-beta|||Phosphothreonine; by MAPK|||Polar residues|||Reduced ubiquitination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143080|||http://purl.uniprot.org/annotation/VAR_024021|||http://purl.uniprot.org/annotation/VAR_024022|||http://purl.uniprot.org/annotation/VAR_054157|||http://purl.uniprot.org/annotation/VSP_000532|||http://purl.uniprot.org/annotation/VSP_000533
http://togogenome.org/gene/9606:GABRR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24046                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit rho-1|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000485|||http://purl.uniprot.org/annotation/VAR_024361|||http://purl.uniprot.org/annotation/VAR_054426|||http://purl.uniprot.org/annotation/VSP_036363|||http://purl.uniprot.org/annotation/VSP_046665
http://togogenome.org/gene/9606:PIBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXW3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS33; loss of function in ciliogenesis.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates modulation of Th2 dominant cytokine production|||Probable disease-associated variant found in patients with microcephaly and intellectual disability; disrupts interaction with CEP63; no effect on interaction with PCM1.|||Progesterone-induced-blocking factor 1|||Required for interaction with PCM1|||Sufficient for NK inhibitory function                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058426|||http://purl.uniprot.org/annotation/VAR_051279|||http://purl.uniprot.org/annotation/VAR_051280|||http://purl.uniprot.org/annotation/VAR_051281|||http://purl.uniprot.org/annotation/VAR_073952|||http://purl.uniprot.org/annotation/VAR_080441|||http://purl.uniprot.org/annotation/VSP_015302|||http://purl.uniprot.org/annotation/VSP_015303|||http://purl.uniprot.org/annotation/VSP_015304|||http://purl.uniprot.org/annotation/VSP_057956
http://togogenome.org/gene/9606:LTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94822                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase listerin|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||In isoform 3.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056304|||http://purl.uniprot.org/annotation/VAR_020957|||http://purl.uniprot.org/annotation/VAR_057218|||http://purl.uniprot.org/annotation/VAR_057219|||http://purl.uniprot.org/annotation/VAR_057220|||http://purl.uniprot.org/annotation/VSP_040138|||http://purl.uniprot.org/annotation/VSP_044911
http://togogenome.org/gene/9606:NT5DC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TFE4|||http://purl.uniprot.org/uniprot/Q9H2R1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  5'-nucleotidase domain-containing protein 1|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N6-acetyllysine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247222|||http://purl.uniprot.org/annotation/VSP_054236
http://togogenome.org/gene/9606:GGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-binding protein GGA1|||Abolishes interaction with ARF1 and RABEP1.|||Abolishes interaction with ARF1, UBC and TSG101.|||Abolishes interaction with ARF1.|||Abolishes interaction with CCDC91.|||Abolishes interaction with IGF2R.|||Abolishes interaction with IGF2R. No effect on the interaction with SORL1.|||Abolishes interaction with RABEP1 and UBC.|||Abolishes interaction with RABEP1, UBC and TSG101.|||Abolishes interaction with RABEP1.|||Autoinhibitory|||Disordered|||GAE|||GAT|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increased interaction with IGF2R.|||Increased interaction with IGF2R. Reduced phosphorylation. No effect on the interaction with SORL1.|||Interaction with ARF3|||N-acetylmethionine|||No effect on interaction with RABEP1.|||Partial loss of clathrin-binding.|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues|||Unstructured hinge|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212680|||http://purl.uniprot.org/annotation/VAR_036522|||http://purl.uniprot.org/annotation/VAR_036523|||http://purl.uniprot.org/annotation/VSP_001744|||http://purl.uniprot.org/annotation/VSP_042806|||http://purl.uniprot.org/annotation/VSP_042807|||http://purl.uniprot.org/annotation/VSP_042808|||http://purl.uniprot.org/annotation/VSP_042809|||http://purl.uniprot.org/annotation/VSP_057352
http://togogenome.org/gene/9606:OR8J3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVE3|||http://purl.uniprot.org/uniprot/Q8NGG0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8J3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150670|||http://purl.uniprot.org/annotation/VAR_048052|||http://purl.uniprot.org/annotation/VAR_048053|||http://purl.uniprot.org/annotation/VAR_048054|||http://purl.uniprot.org/annotation/VAR_048055
http://togogenome.org/gene/9606:PGLYRP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interaction with murein|||N-acetylmuramoyl-L-alanine amidase 1|||N-acetylmuramoyl-L-alanine amidase 2|||N-linked (GlcNAc...) asparagine|||Peptidoglycan recognition protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023924|||http://purl.uniprot.org/annotation/VAR_031586|||http://purl.uniprot.org/annotation/VAR_031587|||http://purl.uniprot.org/annotation/VAR_031588|||http://purl.uniprot.org/annotation/VAR_031589|||http://purl.uniprot.org/annotation/VAR_033283|||http://purl.uniprot.org/annotation/VAR_050503|||http://purl.uniprot.org/annotation/VSP_024388
http://togogenome.org/gene/9606:PSG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQL2|||http://purl.uniprot.org/uniprot/Q00888|||http://purl.uniprot.org/uniprot/Q6P520|||http://purl.uniprot.org/uniprot/Q96QL5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014911|||http://purl.uniprot.org/annotation/PRO_5002790295|||http://purl.uniprot.org/annotation/PRO_5004279375|||http://purl.uniprot.org/annotation/PRO_5014312581|||http://purl.uniprot.org/annotation/VAR_016040|||http://purl.uniprot.org/annotation/VAR_056073|||http://purl.uniprot.org/annotation/VAR_056074|||http://purl.uniprot.org/annotation/VAR_060362|||http://purl.uniprot.org/annotation/VAR_060363|||http://purl.uniprot.org/annotation/VAR_060364|||http://purl.uniprot.org/annotation/VSP_007875|||http://purl.uniprot.org/annotation/VSP_040131|||http://purl.uniprot.org/annotation/VSP_055025
http://togogenome.org/gene/9606:CORO1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31146                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coronin-1A|||Disordered|||In IMD8; the mutation causes a decrease in protein stability; patient T-cell blasts show delayed activation of signaling molecules MAPK3 and MAPK1.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine; by PKC|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050920|||http://purl.uniprot.org/annotation/VAR_011956|||http://purl.uniprot.org/annotation/VAR_070447
http://togogenome.org/gene/9606:TSHZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRE2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox; atypical|||In isoform 2.|||Phosphoserine|||Polar residues|||Teashirt homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047064|||http://purl.uniprot.org/annotation/VAR_026679|||http://purl.uniprot.org/annotation/VAR_026680|||http://purl.uniprot.org/annotation/VSP_046071
http://togogenome.org/gene/9606:DEFA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59665                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  ADP-ribosylarginine; by ART1|||Almost complete loss of bactericidal activity.|||HP 1-56|||Neutrophil defensin 1|||Neutrophil defensin 2|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006771|||http://purl.uniprot.org/annotation/PRO_0000006772|||http://purl.uniprot.org/annotation/PRO_0000006773|||http://purl.uniprot.org/annotation/PRO_0000006774
http://togogenome.org/gene/9606:WDHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75717                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HMG box|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat and HMG-box DNA-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051338|||http://purl.uniprot.org/annotation/VAR_053422|||http://purl.uniprot.org/annotation/VAR_053423|||http://purl.uniprot.org/annotation/VAR_062100|||http://purl.uniprot.org/annotation/VSP_054775
http://togogenome.org/gene/9606:B4GALNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSP5|||http://purl.uniprot.org/uniprot/Q00973                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4 N-acetylgalactosaminyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In SPG26.|||In isoform 2.|||In isoform 3.|||Interchain (with C-412)|||Interchain (with C-529)|||Interchain (with C-80)|||Interchain (with C-82)|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059100|||http://purl.uniprot.org/annotation/PRO_5014085104|||http://purl.uniprot.org/annotation/VAR_012052|||http://purl.uniprot.org/annotation/VAR_012053|||http://purl.uniprot.org/annotation/VAR_049237|||http://purl.uniprot.org/annotation/VAR_070235|||http://purl.uniprot.org/annotation/VAR_070236|||http://purl.uniprot.org/annotation/VSP_055039|||http://purl.uniprot.org/annotation/VSP_055040|||http://purl.uniprot.org/annotation/VSP_055041
http://togogenome.org/gene/9606:PLSCR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PHR9|||http://purl.uniprot.org/uniprot/Q9NRQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  50% decrease in scramblase activity in presence of Ca2+, and 40% decrease in scramblase activity in presence of Mg2+.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||PPxY motif|||Phospholipid scramblase 4|||Phosphotyrosine; by ABL|||Pro residues|||Proline-rich domain (PRD)|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100792|||http://purl.uniprot.org/annotation/VAR_011315|||http://purl.uniprot.org/annotation/VAR_011316|||http://purl.uniprot.org/annotation/VSP_042931|||http://purl.uniprot.org/annotation/VSP_042932
http://togogenome.org/gene/9606:NPPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01160                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Atrial natriuretic peptide|||Atriopeptin-1|||Atriopeptin-2|||Atriopeptin-3|||Auriculin-A|||Auriculin-B|||Auriculin-C|||Auriculin-D|||Cleavage; by CORIN|||Cleavage; by MME|||Disordered|||Important for degradation of atrial natriuretic peptide by IDE|||In ATRST2.|||Kaliuretic peptide|||Long-acting natriuretic peptide|||Loss of cleavage by CORIN.|||Natriuretic peptides A|||No effect on degradation of atrial natriuretic peptide by IDE.|||Phosphoserine|||Reduced degradation of atrial natriuretic peptide by IDE; when associated with N-147--151-YDEL.|||Reduced degradation of atrial natriuretic peptide by IDE; when associated with S-124--126-RDEL.|||Urodilatin|||Vessel dilator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000449721|||http://purl.uniprot.org/annotation/PRO_0000449722|||http://purl.uniprot.org/annotation/PRO_0000449723|||http://purl.uniprot.org/annotation/PRO_0000449724|||http://purl.uniprot.org/annotation/PRO_0000449725|||http://purl.uniprot.org/annotation/PRO_0000449726|||http://purl.uniprot.org/annotation/PRO_0000449727|||http://purl.uniprot.org/annotation/PRO_0000449728|||http://purl.uniprot.org/annotation/PRO_0000449729|||http://purl.uniprot.org/annotation/PRO_0000449730|||http://purl.uniprot.org/annotation/PRO_0000449731|||http://purl.uniprot.org/annotation/PRO_0000449732|||http://purl.uniprot.org/annotation/PRO_0000449733|||http://purl.uniprot.org/annotation/PRO_0000449734|||http://purl.uniprot.org/annotation/VAR_014579|||http://purl.uniprot.org/annotation/VAR_071307|||http://purl.uniprot.org/annotation/VAR_082651
http://togogenome.org/gene/9606:NCOA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6M2K2|||http://purl.uniprot.org/uniprot/F6M2K3|||http://purl.uniprot.org/uniprot/Q14686                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||CREBBP-binding region|||Disordered|||EP300/CRSP3-binding region|||In a breast cancer sample; somatic mutation.|||LXXLL motif 1|||LXXLL motif 2|||N6-acetyllysine|||NCOA1-binding region|||NCOA6IP-binding region|||Nuclear receptor coactivator 6|||Nuclear receptor coactivator 6 TRADD-N|||Phosphoserine|||Phosphoserine; by MAPK; in vitro|||Polar residues|||Pro residues|||Reduced binding to THRB, RXRA, ESR2 and ESR1.|||Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1.|||TBP/GTF2A-binding region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094413|||http://purl.uniprot.org/annotation/VAR_027874|||http://purl.uniprot.org/annotation/VAR_027875|||http://purl.uniprot.org/annotation/VAR_027876|||http://purl.uniprot.org/annotation/VAR_036551|||http://purl.uniprot.org/annotation/VAR_036552
http://togogenome.org/gene/9606:IFITM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMD0                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interferon-induced transmembrane protein 10|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332961
http://togogenome.org/gene/9606:DLGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTN4                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:YME1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96TA2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-dependent zinc metalloprotease YME1L1|||Helical|||In OPA11; does not affect localization to mitochondria; abolishes processing to mature form by MPP; results in decreased mitochondrial protein catabolism; has very low protease activity; results in mitochondrial fragmentation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of ATPase and protease activity. Loss of PRELID1 degradation. Cannot restore OMA1 degradation in YME1L-depleted cells.|||Loss of protease activity. Cannot restore OMA1 degradation in YME1L-depleted cells.|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084667|||http://purl.uniprot.org/annotation/VAR_076869|||http://purl.uniprot.org/annotation/VSP_010017|||http://purl.uniprot.org/annotation/VSP_045336
http://togogenome.org/gene/9606:GON4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4PB67|||http://purl.uniprot.org/uniprot/A4PB68|||http://purl.uniprot.org/uniprot/Q14BN2|||http://purl.uniprot.org/uniprot/Q3T8J9|||http://purl.uniprot.org/uniprot/Q9H986                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||GON-4-like protein|||In isoform 2.|||In isoform 3.|||Myb-like|||PAH 1|||PAH 2|||Phosphoserine|||Polar residues|||Required for interaction with YY1, SIN3A and HDAC1, and transcriptional repression activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197109|||http://purl.uniprot.org/annotation/VAR_024320|||http://purl.uniprot.org/annotation/VAR_056169|||http://purl.uniprot.org/annotation/VAR_056170|||http://purl.uniprot.org/annotation/VAR_056171|||http://purl.uniprot.org/annotation/VAR_056172|||http://purl.uniprot.org/annotation/VSP_016580|||http://purl.uniprot.org/annotation/VSP_016581|||http://purl.uniprot.org/annotation/VSP_016582
http://togogenome.org/gene/9606:CCDC102B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D86                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 102B|||Disordered|||In isoform 2.|||Phosphoserine|||Required for centriolar localization and for interaction with CEP250, CROCC, LRRC45 and NEK2|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-404.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-401 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-210, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-194, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-142, A-210, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-135, A-194, A-210, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-22, A-34, A-142, A-194, A-210, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-21, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.|||Substantial decrease in phosphorylation; when associated with A-22, A-34, A-135, A-142, A-194, A-210, A-401, A-404 and A-406.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079308|||http://purl.uniprot.org/annotation/VAR_022893|||http://purl.uniprot.org/annotation/VAR_022894|||http://purl.uniprot.org/annotation/VAR_047331|||http://purl.uniprot.org/annotation/VAR_047332|||http://purl.uniprot.org/annotation/VAR_047333|||http://purl.uniprot.org/annotation/VAR_047334|||http://purl.uniprot.org/annotation/VSP_014688|||http://purl.uniprot.org/annotation/VSP_014689
http://togogenome.org/gene/9606:MCCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X802|||http://purl.uniprot.org/uniprot/P59942                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Mitochondrial coiled-coil domain protein 1|||Mitochondrion|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021657|||http://purl.uniprot.org/annotation/PRO_5014275540|||http://purl.uniprot.org/annotation/VAR_017161|||http://purl.uniprot.org/annotation/VAR_017162|||http://purl.uniprot.org/annotation/VAR_017163
http://togogenome.org/gene/9606:TM9SF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QYS2|||http://purl.uniprot.org/uniprot/Q9HD45                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 9 superfamily member|||Transmembrane 9 superfamily member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034369|||http://purl.uniprot.org/annotation/PRO_5007352953
http://togogenome.org/gene/9606:GAGE12D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L429                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12B/C/D/E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311977
http://togogenome.org/gene/9606:DDI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TDH0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes aspartic protease activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein DDI1 homolog 2|||Ubiquitin-binding|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287090|||http://purl.uniprot.org/annotation/VSP_025297|||http://purl.uniprot.org/annotation/VSP_025298
http://togogenome.org/gene/9606:OR2B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV76|||http://purl.uniprot.org/uniprot/O76000                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Putative olfactory receptor 2B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150461
http://togogenome.org/gene/9606:KRT36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76013                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||In isoform 2.|||Keratin, type I cuticular Ha6|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063693|||http://purl.uniprot.org/annotation/VAR_020306|||http://purl.uniprot.org/annotation/VAR_024490|||http://purl.uniprot.org/annotation/VAR_024491|||http://purl.uniprot.org/annotation/VAR_049792|||http://purl.uniprot.org/annotation/VAR_049793|||http://purl.uniprot.org/annotation/VAR_049794|||http://purl.uniprot.org/annotation/VSP_036403
http://togogenome.org/gene/9606:SMIM24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75264                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Small integral membrane protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322598
http://togogenome.org/gene/9606:CCDC178                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4G8|||http://purl.uniprot.org/uniprot/B7ZM04|||http://purl.uniprot.org/uniprot/F8W7A7|||http://purl.uniprot.org/uniprot/Q5BJE1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 178|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223316|||http://purl.uniprot.org/annotation/VAR_047010|||http://purl.uniprot.org/annotation/VAR_047011|||http://purl.uniprot.org/annotation/VAR_047012|||http://purl.uniprot.org/annotation/VAR_047013|||http://purl.uniprot.org/annotation/VAR_061624|||http://purl.uniprot.org/annotation/VSP_017257|||http://purl.uniprot.org/annotation/VSP_017258|||http://purl.uniprot.org/annotation/VSP_053415
http://togogenome.org/gene/9606:TBCEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QJ74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||Phosphoserine|||Tubulin-specific chaperone cofactor E-like protein|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239668
http://togogenome.org/gene/9606:CDCA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53HL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Borealin|||Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-169 and A-230.|||Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230.|||Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-94; A-169 and A-230.|||Decrease in AURKB activity and dimer disruption. Decrease in AURKB activity and almost no phosphorylation by TTK; when associated with A-88; A-94 and A-230.|||Decrease in AURKB activity and no effect on the structure.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-204.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-199 and A-219.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-189, A-204, A-219.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-185, A-199, A-204 and A-219.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-171, A-189, A-199, A-204 and A-219.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-106, A-185, A-189, A-199, A-204 and A-219.|||Decreases interaction with SOG1 and SOG2, abolishes localization to centromeres in prometaphase; when associated with A-171, A-185, A-189, A-199, A-204 and A-219.|||Disordered|||Fails to exhibit normal localization to the nucleolus in interphase depleted cells.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of binding to BIRC5; when associated with E-70.|||Loss of binding to BIRC5; when associated with E-74.|||Loss of binding to INCENP; when associated with E-35.|||Loss of binding to INCENP; when associated with Y-46.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-19.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-17 and E-20.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with E-19 and E-20.|||No effect on the structure.|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphothreonine|||Phosphothreonine; by TTK|||Polar residues|||Required for centromere localization|||Required for interaction with INCENP|||Required for interaction with INCENP and BIRC5|||Required for interaction with SENP3|||Required to form a minimal CPC core complex that localizes to the central spindle and midbody and properly executes the role of the CPC during cytokinesis|||Results in reduction but not abolition of phosphorylation.|||Substantial loss of structure.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247075|||http://purl.uniprot.org/annotation/VAR_027063
http://togogenome.org/gene/9606:GLT1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MS3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Glycosyltransferase 1 domain-containing protein 1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312203|||http://purl.uniprot.org/annotation/VSP_029731|||http://purl.uniprot.org/annotation/VSP_029732|||http://purl.uniprot.org/annotation/VSP_029733
http://togogenome.org/gene/9606:RABL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2SW46|||http://purl.uniprot.org/uniprot/Q9UNT1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GDP-locked form; mild defects in ciliary assembly. Loss of interaction with the intraflagellar transport (IFT) complex B via the IFT74-IFT81 heterodimer. Loss of interaction with CEP19. Loss of localization to the centrosome. Loss of localization to the base of the cilium.|||GTP-locked form; interacts with the intraflagellar transport (IFT) complex B via the IFT74-IFT81 heterodimer. Localizes to the base of the cilium and accumulates within the cilium and at the tip in specific puncta.|||In isoform 2.|||In isoform 3.|||Mild defects in ciliary assembly. Loss of interaction with the intraflagellar transport (IFT) complex B via the IFT74-IFT81 heterodimer. Interacts with CEP19.|||Polar residues|||Rab-like protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121264|||http://purl.uniprot.org/annotation/VSP_005532|||http://purl.uniprot.org/annotation/VSP_041061
http://togogenome.org/gene/9606:CLIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95833                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chloride intracellular channel protein 3|||GST C-terminal|||GST N-terminal|||Helical|||In soluble form|||Phosphoserine|||Required for insertion into the membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144207|||http://purl.uniprot.org/annotation/VAR_020424
http://togogenome.org/gene/9606:AHNAK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTV0|||http://purl.uniprot.org/uniprot/Q09666|||http://purl.uniprot.org/uniprot/Q9BVU3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||N6-methyllysine|||Neuroblast differentiation-associated protein AHNAK|||Nuclear localization signal|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064504|||http://purl.uniprot.org/annotation/VAR_039058|||http://purl.uniprot.org/annotation/VAR_039059|||http://purl.uniprot.org/annotation/VAR_039060|||http://purl.uniprot.org/annotation/VAR_039061|||http://purl.uniprot.org/annotation/VAR_039062|||http://purl.uniprot.org/annotation/VAR_039063|||http://purl.uniprot.org/annotation/VAR_039064|||http://purl.uniprot.org/annotation/VAR_039065|||http://purl.uniprot.org/annotation/VAR_039066|||http://purl.uniprot.org/annotation/VAR_039067|||http://purl.uniprot.org/annotation/VAR_039068|||http://purl.uniprot.org/annotation/VAR_061551|||http://purl.uniprot.org/annotation/VAR_061552|||http://purl.uniprot.org/annotation/VSP_044233|||http://purl.uniprot.org/annotation/VSP_044234
http://togogenome.org/gene/9606:IFNA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C382|||http://purl.uniprot.org/uniprot/P01569                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016362|||http://purl.uniprot.org/annotation/PRO_5036402071
http://togogenome.org/gene/9606:MBTPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14703                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes serine protease activity.|||Abolishes serine protease activity. Does not promote FAM20C kinase activity.|||Charge relay system|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Helical|||In SEDKF; due to a nucleotide substitution that creates a dominant splice donor site in exon 9; two different type of transcripts are produced, a major non-functional alternatively spliced transcript with a 41-bp deletion of exon 9, loss of S-414 in the catalytic triad and premature truncation and a normally spliced transcript with variant G-365; the transcript with G-365 produces a catalytically active protein but is the less abundant.|||In SEDKF; unknown pathological significance.|||Lumenal|||Membrane-bound transcription factor site-1 protease|||N-linked (GlcNAc...) asparagine|||Peptidase S8|||Phosphoserine; by FAM20C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027051|||http://purl.uniprot.org/annotation/PRO_0000027052|||http://purl.uniprot.org/annotation/VAR_051822|||http://purl.uniprot.org/annotation/VAR_051823|||http://purl.uniprot.org/annotation/VAR_082197|||http://purl.uniprot.org/annotation/VAR_087565
http://togogenome.org/gene/9606:GPM6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51674                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neuronal membrane glycoprotein M6-a|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159018|||http://purl.uniprot.org/annotation/VAR_014895|||http://purl.uniprot.org/annotation/VSP_045109|||http://purl.uniprot.org/annotation/VSP_046098
http://togogenome.org/gene/9606:RBM24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAI7|||http://purl.uniprot.org/uniprot/Q9BX46                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreases p53/TP53 expression.|||In isoform 2.|||In isoform 3.|||Increases p53/TP53 expression.|||Necessary for interaction with EIF4E|||RNA-binding protein 24|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273370|||http://purl.uniprot.org/annotation/VSP_022526|||http://purl.uniprot.org/annotation/VSP_046775
http://togogenome.org/gene/9606:SFN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31947                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  14-3-3 protein sigma|||In isoform 2.|||Interaction with phosphoserine on interacting protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058643|||http://purl.uniprot.org/annotation/VAR_048095|||http://purl.uniprot.org/annotation/VSP_021768
http://togogenome.org/gene/9606:CAPN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Q1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C2|||Calpain catalytic|||Calpain-6|||Domain III|||In a colorectal cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207717|||http://purl.uniprot.org/annotation/VAR_021084|||http://purl.uniprot.org/annotation/VAR_036048|||http://purl.uniprot.org/annotation/VAR_051515
http://togogenome.org/gene/9606:SACM1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVV3|||http://purl.uniprot.org/uniprot/E9PGZ4|||http://purl.uniprot.org/uniprot/Q9NTJ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Essential for phosphatidylinositol-4-phosphate phosphatase activity|||Helical|||In isoform 2.|||Loss of phosphatidylinositol-4-phosphate phosphatase activity.|||Lumenal|||N6-acetyllysine|||Phosphatidylinositol-3-phosphatase SAC1|||SAC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000450055|||http://purl.uniprot.org/annotation/VAR_038484|||http://purl.uniprot.org/annotation/VSP_056068|||http://purl.uniprot.org/annotation/VSP_056069
http://togogenome.org/gene/9606:ZNF274                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR47|||http://purl.uniprot.org/uniprot/Q96GC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||KRAB 1|||KRAB 2|||Neurotrophin receptor-interacting factor homolog|||SCAN box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047501|||http://purl.uniprot.org/annotation/VAR_064920|||http://purl.uniprot.org/annotation/VSP_006910|||http://purl.uniprot.org/annotation/VSP_006911|||http://purl.uniprot.org/annotation/VSP_006912|||http://purl.uniprot.org/annotation/VSP_006913
http://togogenome.org/gene/9606:PAOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6QHF9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Microbody targeting signal|||N-acetylmethionine|||Peroxisomal N(1)-acetyl-spermine/spermidine oxidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099875|||http://purl.uniprot.org/annotation/VSP_060446|||http://purl.uniprot.org/annotation/VSP_060447|||http://purl.uniprot.org/annotation/VSP_060448|||http://purl.uniprot.org/annotation/VSP_060449|||http://purl.uniprot.org/annotation/VSP_060450|||http://purl.uniprot.org/annotation/VSP_060451
http://togogenome.org/gene/9606:ATP6V1G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 3.|||In isoform 4.|||V-type proton ATPase subunit G 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192904|||http://purl.uniprot.org/annotation/VAR_048343|||http://purl.uniprot.org/annotation/VSP_036423|||http://purl.uniprot.org/annotation/VSP_036426
http://togogenome.org/gene/9606:DNASE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24855                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Deoxyribonuclease-1|||Essential for enzymatic activity|||In allele DNASE1*1.|||In allele DNASE1*3.|||In allele DNASE1*4.|||In allele DNASE1*5.|||In allele DNASE1*6.|||In isoform 2.|||Involved in actin-binding|||N-linked (GlcNAc...) asparagine|||Nitration by tetranitromethane destroys a Ca(2+) binding site and inactivates enzyme                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007277|||http://purl.uniprot.org/annotation/VAR_002264|||http://purl.uniprot.org/annotation/VAR_002265|||http://purl.uniprot.org/annotation/VAR_002266|||http://purl.uniprot.org/annotation/VAR_009300|||http://purl.uniprot.org/annotation/VAR_009301|||http://purl.uniprot.org/annotation/VAR_024434|||http://purl.uniprot.org/annotation/VAR_024435|||http://purl.uniprot.org/annotation/VAR_029172|||http://purl.uniprot.org/annotation/VAR_029173|||http://purl.uniprot.org/annotation/VAR_029174|||http://purl.uniprot.org/annotation/VAR_029175|||http://purl.uniprot.org/annotation/VSP_056974|||http://purl.uniprot.org/annotation/VSP_056975|||http://purl.uniprot.org/annotation/VSP_056976
http://togogenome.org/gene/9606:OSMR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99650                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||In PLCA1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Oncostatin-M-specific receptor subunit beta|||Phosphoserine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259759|||http://purl.uniprot.org/annotation/VAR_028972|||http://purl.uniprot.org/annotation/VAR_028973|||http://purl.uniprot.org/annotation/VAR_028974|||http://purl.uniprot.org/annotation/VAR_028975|||http://purl.uniprot.org/annotation/VAR_043512|||http://purl.uniprot.org/annotation/VAR_043513|||http://purl.uniprot.org/annotation/VAR_043514|||http://purl.uniprot.org/annotation/VAR_043515|||http://purl.uniprot.org/annotation/VAR_065810|||http://purl.uniprot.org/annotation/VAR_065811|||http://purl.uniprot.org/annotation/VAR_065812|||http://purl.uniprot.org/annotation/VSP_021527|||http://purl.uniprot.org/annotation/VSP_021528
http://togogenome.org/gene/9606:LNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase LNX|||In isoform 2.|||Interaction with MAGEB18|||NPXY motif|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055913|||http://purl.uniprot.org/annotation/VSP_005733
http://togogenome.org/gene/9606:FERMT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UX7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  FERM|||Fermitin family homolog 3|||In LAD3; unknown pathological significance; decreases cell adhesion in hematopoietic cells; requires 2 nucleotide substitutions.|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219454|||http://purl.uniprot.org/annotation/VAR_074597|||http://purl.uniprot.org/annotation/VSP_009226
http://togogenome.org/gene/9606:CT45A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMV1|||http://purl.uniprot.org/uniprot/P0DMV2|||http://purl.uniprot.org/uniprot/Q5DJT8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A2|||Cancer/testis antigen family 45 member A8|||Cancer/testis antigen family 45 member A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308947|||http://purl.uniprot.org/annotation/PRO_0000433030|||http://purl.uniprot.org/annotation/PRO_0000433031
http://togogenome.org/gene/9606:PLA2G2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNK4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Group IID secretory phospholipase A2|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022755|||http://purl.uniprot.org/annotation/VAR_012741|||http://purl.uniprot.org/annotation/VAR_055387|||http://purl.uniprot.org/annotation/VAR_055388|||http://purl.uniprot.org/annotation/VAR_055389|||http://purl.uniprot.org/annotation/VAR_055390|||http://purl.uniprot.org/annotation/VAR_055391|||http://purl.uniprot.org/annotation/VSP_060595|||http://purl.uniprot.org/annotation/VSP_060596
http://togogenome.org/gene/9606:DUX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C3U3A0|||http://purl.uniprot.org/uniprot/Q9UBX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes activity as transcriptional activator.|||Altered sequence specificity, with increased affinity for the DNA sequence 5'-TAATCTAATTA-3'.|||Basic and acidic residues|||Decreased DNA binding affinity.|||Decreased activity as transcriptional activator.|||Disordered|||Double homeobox protein 4|||Homeobox|||Homeobox 1|||Homeobox 2|||Important for transcriptional activation of target genes|||In isoform 2.|||Loss of interaction with EP300 and CREBBP.|||Mildly decreased DNA binding affinity.|||No effect on DNA binding affinity.|||No effect on activity as transcriptional activator.|||Polar residues|||Reduced activity as transcriptional activator.|||Required for interaction with EP300 and CREBBP, and for transcriptional activation of target genes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252413|||http://purl.uniprot.org/annotation/VSP_060075|||http://purl.uniprot.org/annotation/VSP_060076
http://togogenome.org/gene/9606:PAX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXV5|||http://purl.uniprot.org/uniprot/P15863                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with neural tube defects; unknown pathological significance.|||In OTFCS2; significantly reduced transactivation of the regulatory sequence of NKX3-2 in cells over-expressing the mutant sequence compared to cells over-expressing wild-type sequence.|||In isoform 2 and isoform 3.|||In isoform 2.|||PAI subdomain|||Paired|||Paired box protein Pax-1|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050172|||http://purl.uniprot.org/annotation/VAR_003787|||http://purl.uniprot.org/annotation/VAR_055369|||http://purl.uniprot.org/annotation/VAR_055370|||http://purl.uniprot.org/annotation/VAR_055371|||http://purl.uniprot.org/annotation/VAR_070922|||http://purl.uniprot.org/annotation/VSP_039095|||http://purl.uniprot.org/annotation/VSP_039096
http://togogenome.org/gene/9606:RAB38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57729                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Motif|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||In a colorectal cancer sample; somatic mutation.|||Not methylated|||Ras-related protein Rab-38|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121251|||http://purl.uniprot.org/annotation/VAR_036415
http://togogenome.org/gene/9606:PNMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND90                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Paraneoplastic antigen Ma1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155199|||http://purl.uniprot.org/annotation/VAR_053595|||http://purl.uniprot.org/annotation/VAR_053596
http://togogenome.org/gene/9606:MMAA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVH4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes binding to GTP and GTPase activity; when associated with A-290.|||Abolishes binding to GTP and GTPase activity; when associated with A-292.|||In MMAA.|||In MMAA; abolishes protein levels; decreases protein stability.|||In MMAA; decreases protein levels.|||In MMAA; decreases protein levels; decreases protein stability; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB.|||In MMAA; decreases protein levels; highly decreases binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB.|||In MMAA; decreases protein levels; no effect on binding to GDP; decreases by 55% GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB.|||In MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB.|||In MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB.|||In MMAA; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; slightly reduces release of AdoCbl by MMAB.|||In MMAA; highly decreases protein levels.|||In MMAA; highly decreases protein levels; decreases protein stability.|||In MMAA; highly decreases protein levels; decreases protein stability; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB.|||In MMAA; no effect on protein levels; no effect on binding to GDP; no effect on GTPase activity; abolishes interaction with MUT; impairs GTPase activity stimulation by MUT; highly reduces release of AdoCbl by MMAB.|||In MMAA; no effect on protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB.|||In MMAA; unknown pathological significance; decreases protein levels; no effect on binding to GDP; no effect on GTPase activity; no effect on interaction with MUT; impairs GTPase activity stimulation by MUT; reduces release of AdoCbl by MMAB.|||Methylmalonic aciduria type A protein, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002285|||http://purl.uniprot.org/annotation/VAR_017202|||http://purl.uniprot.org/annotation/VAR_020423|||http://purl.uniprot.org/annotation/VAR_020835|||http://purl.uniprot.org/annotation/VAR_020836|||http://purl.uniprot.org/annotation/VAR_020837|||http://purl.uniprot.org/annotation/VAR_020838|||http://purl.uniprot.org/annotation/VAR_038804|||http://purl.uniprot.org/annotation/VAR_071919|||http://purl.uniprot.org/annotation/VAR_071920|||http://purl.uniprot.org/annotation/VAR_071921|||http://purl.uniprot.org/annotation/VAR_071922|||http://purl.uniprot.org/annotation/VAR_071923|||http://purl.uniprot.org/annotation/VAR_080004|||http://purl.uniprot.org/annotation/VAR_080005|||http://purl.uniprot.org/annotation/VAR_080006|||http://purl.uniprot.org/annotation/VAR_080007|||http://purl.uniprot.org/annotation/VAR_080008|||http://purl.uniprot.org/annotation/VAR_080009|||http://purl.uniprot.org/annotation/VAR_080010|||http://purl.uniprot.org/annotation/VAR_080011|||http://purl.uniprot.org/annotation/VAR_080012|||http://purl.uniprot.org/annotation/VAR_080013|||http://purl.uniprot.org/annotation/VAR_080014|||http://purl.uniprot.org/annotation/VAR_080015|||http://purl.uniprot.org/annotation/VAR_080016|||http://purl.uniprot.org/annotation/VAR_080017|||http://purl.uniprot.org/annotation/VAR_080018|||http://purl.uniprot.org/annotation/VAR_080019|||http://purl.uniprot.org/annotation/VAR_080020|||http://purl.uniprot.org/annotation/VAR_080021|||http://purl.uniprot.org/annotation/VAR_080022|||http://purl.uniprot.org/annotation/VAR_080023|||http://purl.uniprot.org/annotation/VAR_080024|||http://purl.uniprot.org/annotation/VAR_080025|||http://purl.uniprot.org/annotation/VAR_080026|||http://purl.uniprot.org/annotation/VAR_080027|||http://purl.uniprot.org/annotation/VAR_080028|||http://purl.uniprot.org/annotation/VAR_080029|||http://purl.uniprot.org/annotation/VAR_080030
http://togogenome.org/gene/9606:UTP14C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TAP6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||U3 small nucleolar RNA-associated protein 14 homolog C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065736|||http://purl.uniprot.org/annotation/VAR_022812|||http://purl.uniprot.org/annotation/VAR_022813|||http://purl.uniprot.org/annotation/VAR_051482
http://togogenome.org/gene/9606:SUMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63165                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Interaction with Tula hantavirus|||Abolishes binding to PIAS2.|||Abolishes sumoylation of ZBED1.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Interaction with PIAS2|||N-acetylserine|||Phosphoserine|||Removed|||Small ubiquitin-related modifier 1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035939|||http://purl.uniprot.org/annotation/PRO_0000035940|||http://purl.uniprot.org/annotation/VSP_046756
http://togogenome.org/gene/9606:BMPER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7U6|||http://purl.uniprot.org/uniprot/Q8N8U9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BMP-binding endothelial regulator protein|||In DSD.|||N-linked (GlcNAc...) asparagine|||TIL|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020820|||http://purl.uniprot.org/annotation/PRO_5001861310|||http://purl.uniprot.org/annotation/VAR_028166|||http://purl.uniprot.org/annotation/VAR_065823
http://togogenome.org/gene/9606:CDC37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16543                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hsp90 co-chaperone Cdc37|||Hsp90 co-chaperone Cdc37, N-terminally processed|||N-acetylmethionine|||N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195057|||http://purl.uniprot.org/annotation/PRO_0000423197|||http://purl.uniprot.org/annotation/VAR_022220
http://togogenome.org/gene/9606:MNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50219                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In CURRAS.|||In isoform 2.|||Motor neuron and pancreas homeobox protein 1|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048905|||http://purl.uniprot.org/annotation/VAR_017874|||http://purl.uniprot.org/annotation/VAR_017875|||http://purl.uniprot.org/annotation/VAR_017876|||http://purl.uniprot.org/annotation/VAR_017877|||http://purl.uniprot.org/annotation/VAR_017878|||http://purl.uniprot.org/annotation/VAR_017879|||http://purl.uniprot.org/annotation/VAR_017880|||http://purl.uniprot.org/annotation/VAR_017881|||http://purl.uniprot.org/annotation/VAR_017882|||http://purl.uniprot.org/annotation/VAR_068473|||http://purl.uniprot.org/annotation/VAR_068474|||http://purl.uniprot.org/annotation/VSP_046773|||http://purl.uniprot.org/annotation/VSP_046774
http://togogenome.org/gene/9606:AQP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PS8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||Abolishes permeability to glycerol.|||Aquaporin-10|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||In isoform 2.|||Increased permeability to glycerol at acidic pH.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Nearly abolishes permeability to glycerol.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063967|||http://purl.uniprot.org/annotation/VAR_033519|||http://purl.uniprot.org/annotation/VAR_050063|||http://purl.uniprot.org/annotation/VSP_010211
http://togogenome.org/gene/9606:H3C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:TARBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13395                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmethionine|||Phosphoserine|||Probable methyltransferase TARBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273201|||http://purl.uniprot.org/annotation/VAR_030101|||http://purl.uniprot.org/annotation/VAR_030102|||http://purl.uniprot.org/annotation/VAR_030103|||http://purl.uniprot.org/annotation/VAR_030104|||http://purl.uniprot.org/annotation/VAR_030105|||http://purl.uniprot.org/annotation/VAR_030106|||http://purl.uniprot.org/annotation/VAR_030107|||http://purl.uniprot.org/annotation/VAR_030108|||http://purl.uniprot.org/annotation/VAR_030109|||http://purl.uniprot.org/annotation/VAR_061907
http://togogenome.org/gene/9606:DIP2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RQW6|||http://purl.uniprot.org/uniprot/Q86XV3|||http://purl.uniprot.org/uniprot/Q9Y2E4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Basic and acidic residues|||DMAP1-binding|||Disco-interacting protein 2 homolog C|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050782|||http://purl.uniprot.org/annotation/VAR_035905|||http://purl.uniprot.org/annotation/VAR_035906|||http://purl.uniprot.org/annotation/VAR_035907|||http://purl.uniprot.org/annotation/VSP_056898|||http://purl.uniprot.org/annotation/VSP_056899|||http://purl.uniprot.org/annotation/VSP_056900
http://togogenome.org/gene/9606:CYP4X1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N118                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4X1|||Helical|||In isoform 2.|||In isoform 3.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051862|||http://purl.uniprot.org/annotation/VSP_045889|||http://purl.uniprot.org/annotation/VSP_045890
http://togogenome.org/gene/9606:FAIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein lifeguard 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179087|||http://purl.uniprot.org/annotation/VSP_056989
http://togogenome.org/gene/9606:NMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT39|||http://purl.uniprot.org/uniprot/O60551|||http://purl.uniprot.org/uniprot/Q5VUC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycylpeptide N-tetradecanoyltransferase 2|||Glycylpeptide N-tetradecanoyltransferase C-terminal|||Glycylpeptide N-tetradecanoyltransferase N-terminal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064226
http://togogenome.org/gene/9606:IRAK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y616                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Abolishes phosphorylation. Abolishes interaction with PIN1. Reduces protein stability.|||Cis/trans isomerization of proline peptide bond; by PIN1; dependent on Ser-110 phosphorylation|||Death|||Disordered|||Enhances dimerization.|||In isoform 2.|||Interchain (with C-202); in linked form|||Interchain (with C-287); in linked form|||Interleukin-1 receptor-associated kinase 3|||May be associated with ASRT5.|||May be associated with ASRT5; abolishes phosphorylation of Ser-110; abolishes interaction with PIN1; no effect on cytoplasmic localization; reduces protein stability.|||No effect on the interaction with PIN1.|||Phosphomimic. Slight decrease in the interaction with PIN1. Weak interaction with PIN1 in absence of IL33-mediated dendritic cell stimulation. Increases resistant to degradation. Localizes to the nucleus in absence of stimulus. Does not affect isomerization of Pro-111 peptide bond.|||Phosphoserine|||Phosphoserine; by IRAK1|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086033|||http://purl.uniprot.org/annotation/VAR_019812|||http://purl.uniprot.org/annotation/VAR_031077|||http://purl.uniprot.org/annotation/VAR_033901|||http://purl.uniprot.org/annotation/VAR_035212|||http://purl.uniprot.org/annotation/VAR_035213|||http://purl.uniprot.org/annotation/VAR_035214|||http://purl.uniprot.org/annotation/VAR_035215|||http://purl.uniprot.org/annotation/VAR_035216|||http://purl.uniprot.org/annotation/VAR_040581|||http://purl.uniprot.org/annotation/VAR_040582|||http://purl.uniprot.org/annotation/VAR_040583|||http://purl.uniprot.org/annotation/VAR_040584|||http://purl.uniprot.org/annotation/VAR_040585|||http://purl.uniprot.org/annotation/VAR_040586|||http://purl.uniprot.org/annotation/VAR_040587|||http://purl.uniprot.org/annotation/VSP_041020
http://togogenome.org/gene/9606:KRT20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35900                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Cleavage; by caspases|||Coil 1A|||Coil 1B|||Coil 2|||Found in a renal cell carcinoma sample; somatic mutation.|||Head|||IF rod|||In a colorectal cancer sample; somatic mutation.|||Keratin, type I cytoskeletal 20|||Leads to collapsed filaments.|||Linker 1|||Linker 12|||No effect on keratin filament organization.|||Phosphoserine; by MAPKAPK2, MAPKAPK3 and PKC|||Promotes keratin filament disassembly.|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063675|||http://purl.uniprot.org/annotation/VAR_024489|||http://purl.uniprot.org/annotation/VAR_036367|||http://purl.uniprot.org/annotation/VAR_064726
http://togogenome.org/gene/9606:ITPRID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EUL7|||http://purl.uniprot.org/uniprot/E9PHV5|||http://purl.uniprot.org/uniprot/P28290                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||ITPR-interacting|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein ITPRID2|||Sperm-specific antigen 2 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072211|||http://purl.uniprot.org/annotation/VAR_031186|||http://purl.uniprot.org/annotation/VAR_031187|||http://purl.uniprot.org/annotation/VAR_056998|||http://purl.uniprot.org/annotation/VAR_059724|||http://purl.uniprot.org/annotation/VSP_023865|||http://purl.uniprot.org/annotation/VSP_023866|||http://purl.uniprot.org/annotation/VSP_023867
http://togogenome.org/gene/9606:SYP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08247                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In XLID96.|||In XLID96; unknown pathological significance.|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Repeats, Gly-rich|||Synaptophysin|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179161|||http://purl.uniprot.org/annotation/VAR_062983|||http://purl.uniprot.org/annotation/VAR_062984|||http://purl.uniprot.org/annotation/VAR_062985|||http://purl.uniprot.org/annotation/VAR_062986|||http://purl.uniprot.org/annotation/VAR_062987|||http://purl.uniprot.org/annotation/VAR_062988|||http://purl.uniprot.org/annotation/VAR_062989|||http://purl.uniprot.org/annotation/VAR_079223|||http://purl.uniprot.org/annotation/VSP_056897
http://togogenome.org/gene/9606:SEPTIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43236                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2 and isoform ARTS.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform ARTS.|||Loss of TGF-beta-induced apoptosis. No translocation to the nucleus following TGF-beta treatment. Loss of XIAP-binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Septin-4|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173519|||http://purl.uniprot.org/annotation/VAR_051935|||http://purl.uniprot.org/annotation/VAR_083877|||http://purl.uniprot.org/annotation/VSP_006050|||http://purl.uniprot.org/annotation/VSP_038302|||http://purl.uniprot.org/annotation/VSP_038303|||http://purl.uniprot.org/annotation/VSP_038304|||http://purl.uniprot.org/annotation/VSP_038305|||http://purl.uniprot.org/annotation/VSP_038306|||http://purl.uniprot.org/annotation/VSP_060788|||http://purl.uniprot.org/annotation/VSP_060789
http://togogenome.org/gene/9606:AKAP13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYJ1|||http://purl.uniprot.org/uniprot/B0AZU4|||http://purl.uniprot.org/uniprot/Q12802                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A-kinase anchor protein 13|||Abolishes guanyl nucleotide exchange activity toward RHOA.|||Abolishes interaction with PRKAR2A and leads to constitutive activation of RHOA; when associated with P-1260.|||Abolishes interaction with PRKAR2A.|||Abolishes interaction with PRKAR2Aand leads to constitutive activation of RHOA; when associated with P-1251.|||Abolishes interaction with YWHAB, leading to constitutive activation of RHOA and MAPK14.|||Basic and acidic residues|||DH|||Decreases guanyl nucleotide exchange activity toward RHOA.|||Disordered|||Impairs interaction with IKBKB.|||Important for interaction with MAP2K3|||Important for interaction with PRKAR2A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ESR1|||Loss of guanyl nucleotide exchange activity toward RHOA.|||N6-methyllysine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces guanyl nucleotide exchange activity toward RHOA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080963|||http://purl.uniprot.org/annotation/VAR_030925|||http://purl.uniprot.org/annotation/VAR_030926|||http://purl.uniprot.org/annotation/VAR_030927|||http://purl.uniprot.org/annotation/VAR_030928|||http://purl.uniprot.org/annotation/VAR_030929|||http://purl.uniprot.org/annotation/VAR_030930|||http://purl.uniprot.org/annotation/VAR_030931|||http://purl.uniprot.org/annotation/VAR_030932|||http://purl.uniprot.org/annotation/VAR_030933|||http://purl.uniprot.org/annotation/VAR_030934|||http://purl.uniprot.org/annotation/VAR_030935|||http://purl.uniprot.org/annotation/VAR_030936|||http://purl.uniprot.org/annotation/VAR_051986|||http://purl.uniprot.org/annotation/VAR_051987|||http://purl.uniprot.org/annotation/VSP_023486|||http://purl.uniprot.org/annotation/VSP_023487|||http://purl.uniprot.org/annotation/VSP_023489|||http://purl.uniprot.org/annotation/VSP_023490|||http://purl.uniprot.org/annotation/VSP_023491
http://togogenome.org/gene/9606:TADA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TJ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||SANT|||Transcriptional adapter 2-beta|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313711|||http://purl.uniprot.org/annotation/VSP_030109|||http://purl.uniprot.org/annotation/VSP_030110
http://togogenome.org/gene/9606:HLA-DOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1V0E3M7|||http://purl.uniprot.org/uniprot/A0A1V0E3N1|||http://purl.uniprot.org/uniprot/A0A1V0E3N3|||http://purl.uniprot.org/uniprot/A0A1V0E3N6|||http://purl.uniprot.org/uniprot/A0A1V0E3N7|||http://purl.uniprot.org/uniprot/A0A1V0E3P0|||http://purl.uniprot.org/uniprot/A0A1V0E3P1|||http://purl.uniprot.org/uniprot/A0A1V0E3P3|||http://purl.uniprot.org/uniprot/A0A1V0E3P6|||http://purl.uniprot.org/uniprot/A0A1V0E3P8|||http://purl.uniprot.org/uniprot/A0A1V0E3P9|||http://purl.uniprot.org/uniprot/A0A1V0E3Q1|||http://purl.uniprot.org/uniprot/A0A1V0E3Q2|||http://purl.uniprot.org/uniprot/A0A1V0E3Q3|||http://purl.uniprot.org/uniprot/A0A1V0E3Q4|||http://purl.uniprot.org/uniprot/A0A1V0E3Q5|||http://purl.uniprot.org/uniprot/A0A1V0E3Q6|||http://purl.uniprot.org/uniprot/A0A1V0E3Q7|||http://purl.uniprot.org/uniprot/A0A1V0E3Q8|||http://purl.uniprot.org/uniprot/A0A1V0E3R0|||http://purl.uniprot.org/uniprot/A0A1V0E3R3|||http://purl.uniprot.org/uniprot/A0A1V0E3R4|||http://purl.uniprot.org/uniprot/A0A1V0E3R6|||http://purl.uniprot.org/uniprot/A0A1V0E3R8|||http://purl.uniprot.org/uniprot/A0A1V0E3S0|||http://purl.uniprot.org/uniprot/A0A1V0E3S4|||http://purl.uniprot.org/uniprot/A0A1V0E3S6|||http://purl.uniprot.org/uniprot/A0A1V0E3S7|||http://purl.uniprot.org/uniprot/A0A1V0E3T1|||http://purl.uniprot.org/uniprot/P06340|||http://purl.uniprot.org/uniprot/X5CF87                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DO alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DOA*01:02.|||In allele DOA*01:03.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018962|||http://purl.uniprot.org/annotation/PRO_5010693746|||http://purl.uniprot.org/annotation/PRO_5010694651|||http://purl.uniprot.org/annotation/PRO_5010695548|||http://purl.uniprot.org/annotation/PRO_5010695558|||http://purl.uniprot.org/annotation/PRO_5010700021|||http://purl.uniprot.org/annotation/PRO_5010700024|||http://purl.uniprot.org/annotation/PRO_5010700946|||http://purl.uniprot.org/annotation/PRO_5010702690|||http://purl.uniprot.org/annotation/PRO_5010703567|||http://purl.uniprot.org/annotation/PRO_5010706387|||http://purl.uniprot.org/annotation/PRO_5010708218|||http://purl.uniprot.org/annotation/PRO_5010709128|||http://purl.uniprot.org/annotation/PRO_5010710031|||http://purl.uniprot.org/annotation/PRO_5010710034|||http://purl.uniprot.org/annotation/PRO_5010715626|||http://purl.uniprot.org/annotation/PRO_5010717512|||http://purl.uniprot.org/annotation/PRO_5010719305|||http://purl.uniprot.org/annotation/PRO_5010720199|||http://purl.uniprot.org/annotation/PRO_5010722918|||http://purl.uniprot.org/annotation/PRO_5010723835|||http://purl.uniprot.org/annotation/PRO_5010725613|||http://purl.uniprot.org/annotation/PRO_5010731122|||http://purl.uniprot.org/annotation/PRO_5010732086|||http://purl.uniprot.org/annotation/PRO_5010734777|||http://purl.uniprot.org/annotation/PRO_5010737531|||http://purl.uniprot.org/annotation/PRO_5010739409|||http://purl.uniprot.org/annotation/PRO_5010744845|||http://purl.uniprot.org/annotation/PRO_5010747619|||http://purl.uniprot.org/annotation/PRO_5010747633|||http://purl.uniprot.org/annotation/PRO_5014316165|||http://purl.uniprot.org/annotation/VAR_058126|||http://purl.uniprot.org/annotation/VAR_058127
http://togogenome.org/gene/9606:RRAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62070                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Does not affect lysine fatty-acylation.|||Effector region|||In NS12; also found as somatic mutation in ovarian cancer; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish.|||In NS12; associated in cis with C-75; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish; results in craniofacial patterning defects in zebrafish when associated with C-75.|||In NS12; decreased GAP-stimulated GTPase activity leading to an accumulation of RRAS2 in its GTP-bound active state; increased MAPK signaling; loss of interaction with RASSF5.|||In NS12; increased MAPK signaling.|||In NS12; increased MAPK signaling; results in craniofacial patterning defects when expressed in zebrafish.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Likely benign variant; associated in cis with H-72 in a patient with Noonan syndrome; has no effect on MAPK signaling; has no effect on craniofacial patterning when expressed in zebrafish; results in craniofacial patterning defects in zebrafish when associated with H-72.|||N-acetylalanine|||N6-palmitoyl lysine|||Phosphoserine|||Ras-related protein R-Ras2|||Removed|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine|||Strongly decreased lysine fatty-acylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082652|||http://purl.uniprot.org/annotation/PRO_0000281302|||http://purl.uniprot.org/annotation/VAR_006848|||http://purl.uniprot.org/annotation/VAR_083149|||http://purl.uniprot.org/annotation/VAR_083150|||http://purl.uniprot.org/annotation/VAR_083151|||http://purl.uniprot.org/annotation/VAR_083152|||http://purl.uniprot.org/annotation/VAR_083153|||http://purl.uniprot.org/annotation/VAR_083154|||http://purl.uniprot.org/annotation/VSP_043066|||http://purl.uniprot.org/annotation/VSP_044485|||http://purl.uniprot.org/annotation/VSP_055842
http://togogenome.org/gene/9606:OR5D14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5D14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150592|||http://purl.uniprot.org/annotation/VAR_034221|||http://purl.uniprot.org/annotation/VAR_034222
http://togogenome.org/gene/9606:KIR3DL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5QEB2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Immunoglobulin subtype|||Immunoglobulin subtype 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5040096645
http://togogenome.org/gene/9606:FUT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ENC0|||http://purl.uniprot.org/uniprot/Q11128                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5|||Cytoplasmic|||Decreases both alpha-(1,3)-fucosyltransferase and alpha-(1,4)-fucosyltransferase activity of 50%.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; K-111 and T-118.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and K-111.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and T-118.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; R-110; K-111 and T-118.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated withH-105; R-110; K-111 and T-118.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 oligosaccharide acceptor; when associated with I-87 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 oligosaccharide acceptors; when associated with I-87 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with I-87 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with I-87 and S-92.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and I-87. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and I-87.|||Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and S-92.|||Does not affect alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity.|||Fucosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||Increases alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity. Loss of site-specific fucosylation; when associated with E-125 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; E-125 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; E-125 and V-126.|||Loss of site-specific fucosylation; when associated with R-124 and E-125. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and E-125. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and E-125.|||Loss of site-specific fucosylation; when associated with R-124 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and V-126.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with R-124; E-125 and V-126. Significantly decreases cell-surface expression of VIM2 antigen; when associated with R-124; E-125 and V-126. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221105|||http://purl.uniprot.org/annotation/VAR_022122|||http://purl.uniprot.org/annotation/VAR_055845
http://togogenome.org/gene/9606:PPP6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R861|||http://purl.uniprot.org/uniprot/O00743                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in patients with melanomas; decreased protein phosphatase activity, leading to increased phosphorylation of STING1.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Proton donor|||Removed; alternate|||Serine/threonine-protein phosphatase 6 catalytic subunit|||Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058877|||http://purl.uniprot.org/annotation/PRO_0000424504|||http://purl.uniprot.org/annotation/VAR_085528|||http://purl.uniprot.org/annotation/VAR_085529|||http://purl.uniprot.org/annotation/VAR_085530|||http://purl.uniprot.org/annotation/VSP_038376|||http://purl.uniprot.org/annotation/VSP_041158
http://togogenome.org/gene/9606:EYA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ETN2|||http://purl.uniprot.org/uniprot/O00167                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SIX1.|||Basic and acidic residues|||Disordered|||Eyes absent homolog 2|||In isoform 2.|||In isoform 3.|||Nucleophile|||Polar residues|||Proton donor|||Strongly reduces SIX1 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218646|||http://purl.uniprot.org/annotation/VAR_048964|||http://purl.uniprot.org/annotation/VAR_048965|||http://purl.uniprot.org/annotation/VSP_001490|||http://purl.uniprot.org/annotation/VSP_001491
http://togogenome.org/gene/9606:PLEKHG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JYA6|||http://purl.uniprot.org/uniprot/Q9ULL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family G member 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080964|||http://purl.uniprot.org/annotation/VAR_051988|||http://purl.uniprot.org/annotation/VAR_051989|||http://purl.uniprot.org/annotation/VAR_051990|||http://purl.uniprot.org/annotation/VAR_061797
http://togogenome.org/gene/9606:MGAT4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBM8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288596|||http://purl.uniprot.org/annotation/VAR_032447|||http://purl.uniprot.org/annotation/VSP_056096
http://togogenome.org/gene/9606:TAS2R31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59538                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082309|||http://purl.uniprot.org/annotation/VAR_030684|||http://purl.uniprot.org/annotation/VAR_030685|||http://purl.uniprot.org/annotation/VAR_030686|||http://purl.uniprot.org/annotation/VAR_030687|||http://purl.uniprot.org/annotation/VAR_030688|||http://purl.uniprot.org/annotation/VAR_062090
http://togogenome.org/gene/9606:CNNM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE01                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  CBS 1|||CBS 2|||CNNM transmembrane|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Metal transporter CNNM3|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295763|||http://purl.uniprot.org/annotation/VSP_027082|||http://purl.uniprot.org/annotation/VSP_027083
http://togogenome.org/gene/9606:CPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVL8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Carboxypeptidase O|||GPI-anchor amidated aspartate|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252401|||http://purl.uniprot.org/annotation/PRO_0000437881|||http://purl.uniprot.org/annotation/VAR_027850|||http://purl.uniprot.org/annotation/VAR_027851|||http://purl.uniprot.org/annotation/VAR_036012
http://togogenome.org/gene/9606:CASS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DII4|||http://purl.uniprot.org/uniprot/Q9NQ75                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cas scaffolding protein family member 4|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079425|||http://purl.uniprot.org/annotation/VAR_054084|||http://purl.uniprot.org/annotation/VAR_054085|||http://purl.uniprot.org/annotation/VAR_054086|||http://purl.uniprot.org/annotation/VAR_054087|||http://purl.uniprot.org/annotation/VSP_003806|||http://purl.uniprot.org/annotation/VSP_003807
http://togogenome.org/gene/9606:TAF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15545                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  50% reduction in TAF1-binding, reduced incorporation of TAF7 into TFIID complexes.|||Abolishes methylation in vitro.|||Disordered|||Phosphoserine|||Reduced H3 acetylation and transcription at target promoters.|||Transcription initiation factor TFIID subunit 7|||[KR]-[STA]-K motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118881|||http://purl.uniprot.org/annotation/VAR_005629
http://togogenome.org/gene/9606:GPR82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P67                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 82                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069588
http://togogenome.org/gene/9606:NFAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NET5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the ITAM-mediated-activating activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITAM|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||NFAT activation molecule 1|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015046|||http://purl.uniprot.org/annotation/VAR_049964|||http://purl.uniprot.org/annotation/VAR_049965
http://togogenome.org/gene/9606:MOAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BY2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolished interaction with ATG8 proteins MAP1LC3A, MAP1LC3B and MAP1LC3C.|||Abrogates interaction with BAX, resulting in a nonapoptotic protein.|||BH3-like|||Does not affect interaction with ATG8 proteins MAP1LC3A, MAP1LC3B and MAP1LC3C.|||LIR|||Loss of RASSF1-binding; interacts with BAX in the absence of RASSF1.|||Modulator of apoptosis 1|||No effect on RASSF1-binding.|||No effect on RASSF1-binding; interacts with BAX in the absence of RASSF1.|||RASSF1-binding|||Weakened interaction with BAX, resulting in a nonapoptotic protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155205
http://togogenome.org/gene/9606:SPATA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0W8|||http://purl.uniprot.org/uniprot/V9HVY9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with LCA3.|||In isoform 2.|||In isoform 3.|||Polar residues|||Spermatogenesis-associated protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072104|||http://purl.uniprot.org/annotation/VAR_016912|||http://purl.uniprot.org/annotation/VAR_051370|||http://purl.uniprot.org/annotation/VAR_051371|||http://purl.uniprot.org/annotation/VAR_051372|||http://purl.uniprot.org/annotation/VAR_051373|||http://purl.uniprot.org/annotation/VAR_051374|||http://purl.uniprot.org/annotation/VAR_067191|||http://purl.uniprot.org/annotation/VSP_008341|||http://purl.uniprot.org/annotation/VSP_008342
http://togogenome.org/gene/9606:HIGD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW72                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  HIG1|||HIG1 domain family member 2A, mitochondrial|||Helical|||Mitochondrial matrix|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215777
http://togogenome.org/gene/9606:TNRC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KMH2|||http://purl.uniprot.org/uniprot/O15417                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||BAH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Trinucleotide repeat-containing gene 18 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299142|||http://purl.uniprot.org/annotation/VAR_042722|||http://purl.uniprot.org/annotation/VSP_033124|||http://purl.uniprot.org/annotation/VSP_033126|||http://purl.uniprot.org/annotation/VSP_033127|||http://purl.uniprot.org/annotation/VSP_033128|||http://purl.uniprot.org/annotation/VSP_033129
http://togogenome.org/gene/9606:AP2S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QYZ2|||http://purl.uniprot.org/uniprot/M0R0N4|||http://purl.uniprot.org/uniprot/P53680|||http://purl.uniprot.org/uniprot/X6R390                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP complex mu/sigma subunit|||AP-2 complex subunit sigma|||In HHC3; there is a rightward shift in Ca(2+)concentration-response curves with the mutant compared to wild-type, indicating a decrease in the sensitivity of cells expressing CASR to extracellular calcium.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193804|||http://purl.uniprot.org/annotation/VAR_069570|||http://purl.uniprot.org/annotation/VAR_069571|||http://purl.uniprot.org/annotation/VAR_069572|||http://purl.uniprot.org/annotation/VSP_017352
http://togogenome.org/gene/9606:INCENP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CBX5 and AURKB.|||Abolishes interaction with CBX5.|||Basic and acidic residues|||Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-169.|||Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-167 and A-171.|||Decreases interaction with CBX5, abolishes localization to centromeres in interphase; when associated with A-169 and A-171.|||Disordered|||IN box|||In isoform 2.|||Inner centromere protein|||Interaction with AURKC|||Interaction with CBX5|||Loss of binding to CDCA8 and BIRC5; when associated with R-22.|||Loss of binding to CDCA8 and BIRC5; when associated with R-34.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-39.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-36 and R-40.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-35; R-39 and R-40.|||Loss of localization to the central spindle and midbody in anaphase or cytokinesis; when associated with R-36; R-39 and R-40.|||PXVXL/I motif|||Phosphoserine|||Phosphoserine; by AURKB and AURKC|||Phosphothreonine|||Phosphothreonine; by AURKB and AURKC|||Polar residues|||SAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084201|||http://purl.uniprot.org/annotation/VAR_047127|||http://purl.uniprot.org/annotation/VAR_047128|||http://purl.uniprot.org/annotation/VAR_047129|||http://purl.uniprot.org/annotation/VAR_047130|||http://purl.uniprot.org/annotation/VAR_047131|||http://purl.uniprot.org/annotation/VSP_035651
http://togogenome.org/gene/9606:KBTBD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ATG8 interaction motif (AIM)|||BTB|||Basic and acidic residues|||Decreased interaction with GABARAP and GABARAPL2.|||Decreased interaction with GABARAP and GABARAPL2. Loss of function in TIAM1 ubiquitination and degradation. No effect on assembly of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex.|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 7|||Loss of interaction with CUL3. Loss of function in TIAM1 degradation.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119085
http://togogenome.org/gene/9606:ID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02363|||http://purl.uniprot.org/uniprot/Q53T66                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  BHLH|||DNA-binding protein inhibitor ID-2|||Nuclear export signal|||Phosphoserine|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127240
http://togogenome.org/gene/9606:KCNQ4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQH8|||http://purl.uniprot.org/uniprot/P56696                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  A-domain (Tetramerization)|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In DFNA2A.|||In DFNA2A; dominant negative effect; abolishes potassium current.|||In DFNA2A; loss of potassium selectivity of the pore.|||In isoform 2.|||No effect on inhibition by potassium channel toxin SsTX.|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium channel voltage dependent KCNQ C-terminal|||Potassium voltage-gated channel subfamily KQT member 4|||Resistant to inhibition by potassium channel toxin SsTX. Normal voltage activation.|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054037|||http://purl.uniprot.org/annotation/VAR_001547|||http://purl.uniprot.org/annotation/VAR_008726|||http://purl.uniprot.org/annotation/VAR_008727|||http://purl.uniprot.org/annotation/VAR_008728|||http://purl.uniprot.org/annotation/VAR_010936|||http://purl.uniprot.org/annotation/VAR_010937|||http://purl.uniprot.org/annotation/VAR_058971|||http://purl.uniprot.org/annotation/VAR_065779|||http://purl.uniprot.org/annotation/VSP_001013
http://togogenome.org/gene/9606:PPIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45877                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064147|||http://purl.uniprot.org/annotation/VAR_024319|||http://purl.uniprot.org/annotation/VAR_051770|||http://purl.uniprot.org/annotation/VAR_060712
http://togogenome.org/gene/9606:ADTRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IZ2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Androgen-dependent TFPI-regulating protein|||Cytoplasmic|||Extracellular|||Helical|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||Loss of hydrolase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190100|||http://purl.uniprot.org/annotation/VAR_024365|||http://purl.uniprot.org/annotation/VSP_041965|||http://purl.uniprot.org/annotation/VSP_042868
http://togogenome.org/gene/9606:SDHD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4H7|||http://purl.uniprot.org/uniprot/A0A0S2Z4J3|||http://purl.uniprot.org/uniprot/O14521                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Found in an individual with features of Cowden syndrome; unknown pathological significance; associated with increased manganese superoxide dismutase expression; associated with normal reactive oxygen species; associated with no change in AKT expression but a 1.2-fold increase of MAPK expression.|||Helical|||In MC2DN3; results in highly reduced protein expression; results in impaired cellular respiration.|||In MC2DN3; results in impaired mitochondrial complex II assembly; results in impaired cellular respiration.|||In PGL1 and pheochromocytoma.|||In PGL1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||May increase susceptibility for developing paraganglioma, breast and thyroid carcinoma; may be involved in somatic Merkel cell carcinoma; associated with increased manganese superoxide dismutase expression; associated with increased reactive oxygen species; associated with a 2.0-fold increase in AKT expression and a 1.7-fold increase in MAPK expression.|||May increase susceptibility for developing pheochromocytoma, paraganglioma, intestinal carcinoid tumor and breast, renal and uterus carcinoma; associated with increased manganese superoxide dismutase expression; associated with increased reactive oxygen species; associated with 1.9-fold increase in both AKT and MAPK expression.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Succinate dehydrogenase [ubiquinone] cytochrome b small subunit|||Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006487|||http://purl.uniprot.org/annotation/PRO_5006608294|||http://purl.uniprot.org/annotation/PRO_5006608296|||http://purl.uniprot.org/annotation/VAR_010038|||http://purl.uniprot.org/annotation/VAR_010039|||http://purl.uniprot.org/annotation/VAR_010040|||http://purl.uniprot.org/annotation/VAR_017870|||http://purl.uniprot.org/annotation/VAR_017871|||http://purl.uniprot.org/annotation/VAR_017872|||http://purl.uniprot.org/annotation/VAR_017873|||http://purl.uniprot.org/annotation/VAR_018519|||http://purl.uniprot.org/annotation/VAR_054384|||http://purl.uniprot.org/annotation/VAR_054385|||http://purl.uniprot.org/annotation/VAR_074105|||http://purl.uniprot.org/annotation/VAR_074106|||http://purl.uniprot.org/annotation/VSP_054744|||http://purl.uniprot.org/annotation/VSP_054745|||http://purl.uniprot.org/annotation/VSP_054746|||http://purl.uniprot.org/annotation/VSP_054747
http://togogenome.org/gene/9606:PAPLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXI1|||http://purl.uniprot.org/uniprot/O95428                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Basic and acidic residues|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PLAC|||Papilin|||Polar residues|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324550|||http://purl.uniprot.org/annotation/VAR_039815|||http://purl.uniprot.org/annotation/VAR_039816|||http://purl.uniprot.org/annotation/VAR_039817|||http://purl.uniprot.org/annotation/VAR_039818|||http://purl.uniprot.org/annotation/VAR_039819|||http://purl.uniprot.org/annotation/VAR_039820|||http://purl.uniprot.org/annotation/VAR_039821|||http://purl.uniprot.org/annotation/VAR_039822|||http://purl.uniprot.org/annotation/VAR_039823|||http://purl.uniprot.org/annotation/VAR_039824|||http://purl.uniprot.org/annotation/VAR_039825|||http://purl.uniprot.org/annotation/VSP_032269|||http://purl.uniprot.org/annotation/VSP_032270|||http://purl.uniprot.org/annotation/VSP_032271|||http://purl.uniprot.org/annotation/VSP_032272|||http://purl.uniprot.org/annotation/VSP_032273|||http://purl.uniprot.org/annotation/VSP_032274|||http://purl.uniprot.org/annotation/VSP_037595|||http://purl.uniprot.org/annotation/VSP_037596
http://togogenome.org/gene/9606:ZNF134                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52741|||http://purl.uniprot.org/uniprot/Q5U5N5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Zinc finger protein 134                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047418|||http://purl.uniprot.org/annotation/VAR_052771|||http://purl.uniprot.org/annotation/VAR_052772|||http://purl.uniprot.org/annotation/VAR_052773|||http://purl.uniprot.org/annotation/VSP_035666
http://togogenome.org/gene/9606:LEO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA polymerase-associated protein LEO1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247819|||http://purl.uniprot.org/annotation/VSP_020051
http://togogenome.org/gene/9606:ANKHD1-EIF4EBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Acidic residues|||Ankyrin repeat and KH domain-containing protein 1|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||KH|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306326|||http://purl.uniprot.org/annotation/VAR_035291|||http://purl.uniprot.org/annotation/VAR_035292|||http://purl.uniprot.org/annotation/VAR_035293|||http://purl.uniprot.org/annotation/VAR_048281|||http://purl.uniprot.org/annotation/VSP_028452|||http://purl.uniprot.org/annotation/VSP_028453|||http://purl.uniprot.org/annotation/VSP_028454|||http://purl.uniprot.org/annotation/VSP_028455|||http://purl.uniprot.org/annotation/VSP_028456|||http://purl.uniprot.org/annotation/VSP_028457|||http://purl.uniprot.org/annotation/VSP_028458|||http://purl.uniprot.org/annotation/VSP_044231
http://togogenome.org/gene/9606:ATP5ME                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56385                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  ATP synthase subunit e, mitochondrial|||ATP synthase subunit e, mitochondrial, N-terminally processed|||N6-acetyllysine|||Phosphoserine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071684|||http://purl.uniprot.org/annotation/PRO_0000434346
http://togogenome.org/gene/9606:SMARCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALF6|||http://purl.uniprot.org/uniprot/B4DNT1|||http://purl.uniprot.org/uniprot/B4DSC8|||http://purl.uniprot.org/uniprot/F6T8Q0|||http://purl.uniprot.org/uniprot/F6VDE0|||http://purl.uniprot.org/uniprot/P51531|||http://purl.uniprot.org/uniprot/Q56A76|||http://purl.uniprot.org/uniprot/Q8N9Q1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Associated with schizophrenia in some populations; results in reduced localization to the nucleus; decreased interaction with chromatin.|||Basic and acidic residues|||Bromo|||DEGH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||In BIS.|||In NCBRS.|||In isoform Short.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a patient with non-specific intellectual disability syndrome.|||Probable global transcription activator SNF2L2|||QLQ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074352|||http://purl.uniprot.org/annotation/PRO_5002761800|||http://purl.uniprot.org/annotation/PRO_5004311201|||http://purl.uniprot.org/annotation/PRO_5014567683|||http://purl.uniprot.org/annotation/VAR_049501|||http://purl.uniprot.org/annotation/VAR_049502|||http://purl.uniprot.org/annotation/VAR_068180|||http://purl.uniprot.org/annotation/VAR_068181|||http://purl.uniprot.org/annotation/VAR_068182|||http://purl.uniprot.org/annotation/VAR_068183|||http://purl.uniprot.org/annotation/VAR_068184|||http://purl.uniprot.org/annotation/VAR_068185|||http://purl.uniprot.org/annotation/VAR_068186|||http://purl.uniprot.org/annotation/VAR_068187|||http://purl.uniprot.org/annotation/VAR_068188|||http://purl.uniprot.org/annotation/VAR_068189|||http://purl.uniprot.org/annotation/VAR_068190|||http://purl.uniprot.org/annotation/VAR_068191|||http://purl.uniprot.org/annotation/VAR_068192|||http://purl.uniprot.org/annotation/VAR_068193|||http://purl.uniprot.org/annotation/VAR_068194|||http://purl.uniprot.org/annotation/VAR_068195|||http://purl.uniprot.org/annotation/VAR_068196|||http://purl.uniprot.org/annotation/VAR_068197|||http://purl.uniprot.org/annotation/VAR_068198|||http://purl.uniprot.org/annotation/VAR_068199|||http://purl.uniprot.org/annotation/VAR_068200|||http://purl.uniprot.org/annotation/VAR_068201|||http://purl.uniprot.org/annotation/VAR_068202|||http://purl.uniprot.org/annotation/VAR_068203|||http://purl.uniprot.org/annotation/VAR_068204|||http://purl.uniprot.org/annotation/VAR_068205|||http://purl.uniprot.org/annotation/VAR_068206|||http://purl.uniprot.org/annotation/VAR_068207|||http://purl.uniprot.org/annotation/VAR_068208|||http://purl.uniprot.org/annotation/VAR_076936|||http://purl.uniprot.org/annotation/VAR_076937|||http://purl.uniprot.org/annotation/VAR_078815|||http://purl.uniprot.org/annotation/VAR_085660|||http://purl.uniprot.org/annotation/VAR_085661|||http://purl.uniprot.org/annotation/VAR_085662|||http://purl.uniprot.org/annotation/VAR_085663|||http://purl.uniprot.org/annotation/VAR_085664|||http://purl.uniprot.org/annotation/VAR_085665|||http://purl.uniprot.org/annotation/VAR_085666|||http://purl.uniprot.org/annotation/VAR_085667|||http://purl.uniprot.org/annotation/VAR_085668|||http://purl.uniprot.org/annotation/VAR_085669|||http://purl.uniprot.org/annotation/VAR_085670|||http://purl.uniprot.org/annotation/VAR_085671|||http://purl.uniprot.org/annotation/VAR_085672|||http://purl.uniprot.org/annotation/VAR_085673|||http://purl.uniprot.org/annotation/VAR_085674|||http://purl.uniprot.org/annotation/VSP_000577
http://togogenome.org/gene/9606:ACKR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00590                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Atypical chemokine receptor 2|||C-terminal cytoplasmic tail|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069219|||http://purl.uniprot.org/annotation/VAR_024252|||http://purl.uniprot.org/annotation/VAR_049379|||http://purl.uniprot.org/annotation/VAR_049380|||http://purl.uniprot.org/annotation/VAR_049381
http://togogenome.org/gene/9606:GPR137C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW22|||http://purl.uniprot.org/uniprot/Q6AWC7|||http://purl.uniprot.org/uniprot/Q8N3F9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Integral membrane protein GPR137C|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304803|||http://purl.uniprot.org/annotation/PRO_5002790175|||http://purl.uniprot.org/annotation/VAR_053880
http://togogenome.org/gene/9606:CST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01036                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mass|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cystatin-S|||Diphosphorylated at Ser-21 and Ser-23, also called form S2.|||In a breast cancer sample; somatic mutation.|||Monophosphorylated at Ser-23, also called form S1.|||Phosphoserine|||Reactive site|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006650|||http://purl.uniprot.org/annotation/VAR_036549|||http://purl.uniprot.org/annotation/VAR_048852
http://togogenome.org/gene/9606:NRSN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZP1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Neurensin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221675|||http://purl.uniprot.org/annotation/VAR_053738|||http://purl.uniprot.org/annotation/VAR_053739|||http://purl.uniprot.org/annotation/VAR_062158
http://togogenome.org/gene/9606:PPEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14830                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||IQ|||In isoform PPEF-2(S).|||Polar residues|||Proton donor|||Serine/threonine-protein phosphatase with EF-hands 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058901|||http://purl.uniprot.org/annotation/VAR_010230|||http://purl.uniprot.org/annotation/VAR_055121|||http://purl.uniprot.org/annotation/VAR_055122|||http://purl.uniprot.org/annotation/VAR_055123|||http://purl.uniprot.org/annotation/VAR_055124|||http://purl.uniprot.org/annotation/VAR_061759|||http://purl.uniprot.org/annotation/VSP_005103|||http://purl.uniprot.org/annotation/VSP_005104
http://togogenome.org/gene/9606:MRPS31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92665                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Mitochondrion|||Small ribosomal subunit protein mS31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030594|||http://purl.uniprot.org/annotation/VAR_052049|||http://purl.uniprot.org/annotation/VAR_061812
http://togogenome.org/gene/9606:TMED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15363|||http://purl.uniprot.org/uniprot/Q6FHT8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Disrupts association with coatomer; when associated with A-194-195-A.|||Disrupts association with coatomer; when associated with S-198-199-S.|||GOLD|||Helical|||Interaction with F2RL1|||Lumenal|||No inhibition of coatomer-dependent GTP hydrolysis.|||Reduced surface and total expression of CASR.|||Required for TMED10 and TMED2 cis-Golgi network localization|||Transmembrane emp24 domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010381|||http://purl.uniprot.org/annotation/PRO_5014310442
http://togogenome.org/gene/9606:TSSK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXA6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site                                                                                  ^@                                                                                  Loss of kinase activity. Loss of binding to TSACC.|||Loss of kinase activity. No effect of binding to TSACC.|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227746
http://togogenome.org/gene/9606:ENDOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94919                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Endonuclease domain-containing 1 protein|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019924|||http://purl.uniprot.org/annotation/VAR_022044|||http://purl.uniprot.org/annotation/VAR_022045
http://togogenome.org/gene/9606:TSPAN17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNG2|||http://purl.uniprot.org/uniprot/Q96FV3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219265|||http://purl.uniprot.org/annotation/VAR_057278|||http://purl.uniprot.org/annotation/VSP_011388|||http://purl.uniprot.org/annotation/VSP_011389|||http://purl.uniprot.org/annotation/VSP_011390|||http://purl.uniprot.org/annotation/VSP_011391|||http://purl.uniprot.org/annotation/VSP_025608
http://togogenome.org/gene/9606:ANKRD33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAA8|||http://purl.uniprot.org/uniprot/Q5K617|||http://purl.uniprot.org/uniprot/Q7Z3H0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Disordered|||In isoform 1.|||Photoreceptor ankyrin repeat protein|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243908|||http://purl.uniprot.org/annotation/VAR_059121|||http://purl.uniprot.org/annotation/VAR_059122|||http://purl.uniprot.org/annotation/VAR_059123|||http://purl.uniprot.org/annotation/VAR_082795|||http://purl.uniprot.org/annotation/VSP_059265|||http://purl.uniprot.org/annotation/VSP_059266|||http://purl.uniprot.org/annotation/VSP_059267
http://togogenome.org/gene/9606:CCT6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40227                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||T-complex protein 1 subunit zeta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128355|||http://purl.uniprot.org/annotation/VAR_052268|||http://purl.uniprot.org/annotation/VSP_044918
http://togogenome.org/gene/9606:RASSF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTQ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Ras association domain-containing protein 6|||Ras-associating|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240404|||http://purl.uniprot.org/annotation/VAR_026725|||http://purl.uniprot.org/annotation/VAR_034440|||http://purl.uniprot.org/annotation/VSP_019370|||http://purl.uniprot.org/annotation/VSP_019371|||http://purl.uniprot.org/annotation/VSP_019372
http://togogenome.org/gene/9606:SSX2IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZB07|||http://purl.uniprot.org/uniprot/Q9Y2D8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Afadin- and alpha-actinin-binding protein|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064455|||http://purl.uniprot.org/annotation/VAR_056726|||http://purl.uniprot.org/annotation/VSP_011724|||http://purl.uniprot.org/annotation/VSP_011725|||http://purl.uniprot.org/annotation/VSP_046368
http://togogenome.org/gene/9606:TYW1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUM6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Flavodoxin-like|||In isoform 2.|||Radical SAM core|||S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281827|||http://purl.uniprot.org/annotation/VSP_056092
http://togogenome.org/gene/9606:YWHAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04917|||http://purl.uniprot.org/uniprot/Q9H4N8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Site|||Turn                                                                                  ^@                                                                                  14-3-3|||14-3-3 protein eta|||Interaction with phosphoserine on interacting protein|||N-acetylglycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058623
http://togogenome.org/gene/9606:ZNF830                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NB3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Zinc finger protein 830                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076193|||http://purl.uniprot.org/annotation/VAR_024059|||http://purl.uniprot.org/annotation/VAR_024060|||http://purl.uniprot.org/annotation/VAR_030940|||http://purl.uniprot.org/annotation/VAR_030941|||http://purl.uniprot.org/annotation/VAR_030942
http://togogenome.org/gene/9606:LRRC63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05C16                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 63                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320628|||http://purl.uniprot.org/annotation/VAR_039236|||http://purl.uniprot.org/annotation/VAR_039237|||http://purl.uniprot.org/annotation/VAR_039238|||http://purl.uniprot.org/annotation/VAR_039239
http://togogenome.org/gene/9606:COL9A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14050                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Associated with an increased risk for intervertebral disk disease.|||Cell attachment site|||Collagen alpha-3(IX) chain|||Disordered|||In EDM3.|||In STL6.|||N-linked (GlcNAc...) asparagine|||Nonhelical region 1 (NC1)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Pro residues|||Triple-helical region 1 (COL1)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005848|||http://purl.uniprot.org/annotation/VAR_012660|||http://purl.uniprot.org/annotation/VAR_012661|||http://purl.uniprot.org/annotation/VAR_026467|||http://purl.uniprot.org/annotation/VAR_026468|||http://purl.uniprot.org/annotation/VAR_026469|||http://purl.uniprot.org/annotation/VAR_026470|||http://purl.uniprot.org/annotation/VAR_026471|||http://purl.uniprot.org/annotation/VAR_048808|||http://purl.uniprot.org/annotation/VAR_072736|||http://purl.uniprot.org/annotation/VAR_087540|||http://purl.uniprot.org/annotation/VAR_087541|||http://purl.uniprot.org/annotation/VAR_087542
http://togogenome.org/gene/9606:NHERF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14745                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In NPHLOP2; impairs the interaction with SLC34A1; causes a reduction of SLC34A1 amount on cell membrane and affects SLC34A1-dependent phosphate uptake.|||In NPHLOP2; the mutant expressed in cultured renal cells increases the generation of cAMP by PTH and inhibits phosphate transport.|||In NPHLOP2; the mutant expressed in cultured renal cells increases the generation of cyclic AMP (cAMP) by parathyroid hormone (PTH) and inhibits phosphate transport.|||In isoform 2.|||Loss of MSX binding.|||Loss of interaction with ACE2.|||N-acetylserine|||Na(+)/H(+) exchange regulatory cofactor NHE-RF1|||PDZ 1|||PDZ 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces MSX binding.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096799|||http://purl.uniprot.org/annotation/VAR_034899|||http://purl.uniprot.org/annotation/VAR_048021|||http://purl.uniprot.org/annotation/VAR_048022|||http://purl.uniprot.org/annotation/VAR_067661|||http://purl.uniprot.org/annotation/VSP_055497
http://togogenome.org/gene/9606:ACOT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXI4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 11|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||In isoform 2.|||Mitochondrion|||Phosphoserine|||START                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053813|||http://purl.uniprot.org/annotation/VAR_022119|||http://purl.uniprot.org/annotation/VAR_022120|||http://purl.uniprot.org/annotation/VAR_022121|||http://purl.uniprot.org/annotation/VAR_048190|||http://purl.uniprot.org/annotation/VAR_048191|||http://purl.uniprot.org/annotation/VSP_000160
http://togogenome.org/gene/9606:PTAFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7N8|||http://purl.uniprot.org/uniprot/P25105                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Platelet-activating factor receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070092|||http://purl.uniprot.org/annotation/VAR_011851|||http://purl.uniprot.org/annotation/VAR_011852
http://togogenome.org/gene/9606:KAT6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWN8|||http://purl.uniprot.org/uniprot/Q8WYB5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form KAT6B-CREBBP|||C2HC MYST-type|||Catalytic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H15|||Histone acetyltransferase KAT6B|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with BRPF1|||Interaction with RUNX1 and RUNX2|||MYST-type HAT|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Negatively regulates HAT activity|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Proton donor/acceptor|||SAMD1-like winged helix (WH)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051575|||http://purl.uniprot.org/annotation/VAR_036361|||http://purl.uniprot.org/annotation/VAR_050217|||http://purl.uniprot.org/annotation/VAR_061367|||http://purl.uniprot.org/annotation/VAR_067315|||http://purl.uniprot.org/annotation/VSP_014586|||http://purl.uniprot.org/annotation/VSP_014587
http://togogenome.org/gene/9606:SERTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A2V5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Serine-rich and transmembrane domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331521
http://togogenome.org/gene/9606:SLC25A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJS0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal domain|||Carrier domain|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In NICCD.|||In isoform 2.|||Linker loop domain|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Regulatory N-terminal domain|||Removed|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090600|||http://purl.uniprot.org/annotation/VAR_016601|||http://purl.uniprot.org/annotation/VAR_050126|||http://purl.uniprot.org/annotation/VAR_050127|||http://purl.uniprot.org/annotation/VSP_043747
http://togogenome.org/gene/9606:MAP1LC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658J6|||http://purl.uniprot.org/uniprot/Q9GZQ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished delipidation by ATG4 family proteins.|||Abolishes interaction with TECPR2.|||Cleavage; by ATG4B|||Decreased interaction with Legionella effector RavZ.|||Decreases C18 ceramide binding.|||Impaired localization to autophagosomes.|||Impairs cleavage by ATG4B.|||Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with K-26 and D-57.|||Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with K-26 and Y-27.|||Increased interaction with WDFY3/ALFY, no effect on SQSTM1-binding; when associated with Y-27 and D-57.|||Microtubule-associated proteins 1A/1B light chain 3B|||No effect on interaction with TECPR2.|||No effect on processing of precursor.|||No processing of precursor. No lipidation. Decreases C18 ceramide binding.|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017198|||http://purl.uniprot.org/annotation/PRO_0000017199
http://togogenome.org/gene/9606:PRR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Proline-rich protein 7|||Reduced induction of apoptosis; when associated with F-139; F-153; F-166; F-177 and F-201.|||Reduced induction of apoptosis; when associated with F-139; F-153; F-166; F-177 and F-210.|||Reduced induction of apoptosis; when associated with F-139; F-153; F-166; F-201 and F-210.|||Reduced induction of apoptosis; when associated with F-139; F-153; F-177; F-201 and F-210.|||Reduced induction of apoptosis; when associated with F-139; F-166; F-177; F-201 and F-210.|||Reduced induction of apoptosis; when associated with F-153; F-166; F-177; F-201 and F-210.|||Required for apoptosis induction|||Required for interaction with NMDA receptors|||Required for internalization|||Required for membrane localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328649|||http://purl.uniprot.org/annotation/VAR_042437|||http://purl.uniprot.org/annotation/VSP_032750
http://togogenome.org/gene/9606:MS4A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS57|||http://purl.uniprot.org/uniprot/Q96JA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Membrane-spanning 4-domains subfamily A member 14|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320967|||http://purl.uniprot.org/annotation/VAR_039330|||http://purl.uniprot.org/annotation/VAR_039331|||http://purl.uniprot.org/annotation/VSP_031779|||http://purl.uniprot.org/annotation/VSP_031780|||http://purl.uniprot.org/annotation/VSP_031781|||http://purl.uniprot.org/annotation/VSP_031782|||http://purl.uniprot.org/annotation/VSP_056734
http://togogenome.org/gene/9606:ANKRD18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQR3|||http://purl.uniprot.org/uniprot/Q8IVF6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 18A|||Basic and acidic residues|||CCDC144C-like coiled-coil|||DUF3496|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066912|||http://purl.uniprot.org/annotation/VAR_055507|||http://purl.uniprot.org/annotation/VAR_055508|||http://purl.uniprot.org/annotation/VAR_055509|||http://purl.uniprot.org/annotation/VAR_055510|||http://purl.uniprot.org/annotation/VAR_055511|||http://purl.uniprot.org/annotation/VAR_055512|||http://purl.uniprot.org/annotation/VAR_059118|||http://purl.uniprot.org/annotation/VSP_056912|||http://purl.uniprot.org/annotation/VSP_056913
http://togogenome.org/gene/9606:PRY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14603                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PTPN13-like protein, Y-linked                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097056|||http://purl.uniprot.org/annotation/VSP_004068|||http://purl.uniprot.org/annotation/VSP_004069
http://togogenome.org/gene/9606:ELF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z720|||http://purl.uniprot.org/uniprot/Q15723                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ETS|||ETS-related transcription factor Elf-2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1 and isoform 2.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204087|||http://purl.uniprot.org/annotation/VSP_014154|||http://purl.uniprot.org/annotation/VSP_014155|||http://purl.uniprot.org/annotation/VSP_014156
http://togogenome.org/gene/9606:IL1RN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18510                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-1 receptor antagonist protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015328|||http://purl.uniprot.org/annotation/VAR_049573|||http://purl.uniprot.org/annotation/VSP_002649|||http://purl.uniprot.org/annotation/VSP_002650|||http://purl.uniprot.org/annotation/VSP_002651
http://togogenome.org/gene/9606:SSTR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35346                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKA|||S-palmitoyl cysteine; by ZDHHC5|||Somatostatin receptor type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070130|||http://purl.uniprot.org/annotation/VAR_020073|||http://purl.uniprot.org/annotation/VAR_029222|||http://purl.uniprot.org/annotation/VAR_029223|||http://purl.uniprot.org/annotation/VAR_029224|||http://purl.uniprot.org/annotation/VAR_029225|||http://purl.uniprot.org/annotation/VAR_029226|||http://purl.uniprot.org/annotation/VAR_033484|||http://purl.uniprot.org/annotation/VAR_033485|||http://purl.uniprot.org/annotation/VAR_033486|||http://purl.uniprot.org/annotation/VAR_049442|||http://purl.uniprot.org/annotation/VAR_049443|||http://purl.uniprot.org/annotation/VAR_049444
http://togogenome.org/gene/9606:PSD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDX1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||PH and SEC7 domain-containing protein 4|||Phosphoserine|||Polar residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251731|||http://purl.uniprot.org/annotation/VAR_027712|||http://purl.uniprot.org/annotation/VAR_051921|||http://purl.uniprot.org/annotation/VAR_051922|||http://purl.uniprot.org/annotation/VAR_051923|||http://purl.uniprot.org/annotation/VAR_051924|||http://purl.uniprot.org/annotation/VSP_020772|||http://purl.uniprot.org/annotation/VSP_020773
http://togogenome.org/gene/9606:CD180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99467                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD180 antigen|||Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034741|||http://purl.uniprot.org/annotation/VAR_021978|||http://purl.uniprot.org/annotation/VAR_021979|||http://purl.uniprot.org/annotation/VAR_057298|||http://purl.uniprot.org/annotation/VAR_057299|||http://purl.uniprot.org/annotation/VAR_057300|||http://purl.uniprot.org/annotation/VAR_057301|||http://purl.uniprot.org/annotation/VAR_061859
http://togogenome.org/gene/9606:TFAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KSU5|||http://purl.uniprot.org/uniprot/Q00059                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  HMG box|||HMG box 1|||HMG box 2|||In MTDPS15.|||In isoform 2.|||Intercalates between bases and promotes DNA bending|||Mitochondrion|||Moderate reduction in DNA bending.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Transcription factor A, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013470|||http://purl.uniprot.org/annotation/PRO_5014303264|||http://purl.uniprot.org/annotation/VAR_016124|||http://purl.uniprot.org/annotation/VAR_077842|||http://purl.uniprot.org/annotation/VSP_047019
http://togogenome.org/gene/9606:RIPOR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A499FJE4|||http://purl.uniprot.org/uniprot/B7Z3F0|||http://purl.uniprot.org/uniprot/B7Z5S0|||http://purl.uniprot.org/uniprot/Q96MK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FAM65 N-terminal|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RIPOR family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079484|||http://purl.uniprot.org/annotation/VAR_053914|||http://purl.uniprot.org/annotation/VAR_062194|||http://purl.uniprot.org/annotation/VSP_026496
http://togogenome.org/gene/9606:BIRC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S3|||http://purl.uniprot.org/uniprot/H3BLT4|||http://purl.uniprot.org/uniprot/O15392                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export.|||BIR|||Baculoviral IAP repeat-containing protein 5|||Disrupts interaction with histone H3pT3, no effect on interaction with INCENP.|||Higher affinity for LAMTOR5 binding.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78.|||Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79.|||Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79.|||Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79.|||Interaction with FBXL7|||Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin.|||Loss of FBXL7 binding.|||Loss of FBXL7 mediated polyubiquitination.|||Loss of LAMTOR5 binding.|||Loss of acetylation. Localization primarily within the cytoplasm.|||Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1.|||Loss of cytoprotection.|||Mimics acetylation. Localization primarily within the nucleus.|||Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP.|||N6-acetyllysine|||No change. Loss of interaction with AURKB; when associated with A-70.|||No change. Loss of interaction with AURKB; when associated with A-71.|||Phosphoserine; by AURKC|||Phosphothreonine; by AURKB|||Phosphothreonine; by CDK1 and CDK15|||Phosphothreonine; by CK2; in vitro|||Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122356|||http://purl.uniprot.org/annotation/VAR_021071|||http://purl.uniprot.org/annotation/VSP_002454|||http://purl.uniprot.org/annotation/VSP_020338|||http://purl.uniprot.org/annotation/VSP_020339|||http://purl.uniprot.org/annotation/VSP_020340|||http://purl.uniprot.org/annotation/VSP_020341|||http://purl.uniprot.org/annotation/VSP_020342
http://togogenome.org/gene/9606:LHX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNJ5|||http://purl.uniprot.org/uniprot/P50458                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx2|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075778
http://togogenome.org/gene/9606:FOXH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75593                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fast/FoxH1 motif 1 (FM1)|||Fast/FoxH1 motif 2 (FM2)|||Fork-head|||Forkhead box protein H1|||Loss of activity.|||Pro residues|||SMAD interaction motif (SIM)|||SMAD-interaction domain (SID)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091842|||http://purl.uniprot.org/annotation/VAR_011381|||http://purl.uniprot.org/annotation/VAR_011382
http://togogenome.org/gene/9606:GJD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IC68|||http://purl.uniprot.org/uniprot/Q8N144                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction delta-3 protein|||Gap junction protein cysteine-rich|||Helical|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312990|||http://purl.uniprot.org/annotation/VSP_029984
http://togogenome.org/gene/9606:PARK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99497|||http://purl.uniprot.org/uniprot/V9HWC2                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes detoxification activity on methylglyocal-adducted CoA.|||Abolishes enzymatic activity. Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduces binding to OTUD7B.|||Abolishes enzymatic activity. Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduces binding to OTUD7B. Removes the glycations and restores histone 3. Reduced localization in lipid rafts; when associated with A-46.|||Abolishes oxidation and association with mitochondria. No effect on chaperone activity.|||Cleavage; by CASP6|||Cysteine sulfinic acid (-SO2H); alternate|||DJ-1/PfpI|||Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In PARK7.|||In PARK7; does not affect protein stability and degradation; does not interfere with homodimerization; decreased detoxification activity on methylglyocal-adducted CoA.|||In PARK7; loss of protection against metal cytotoxicity; decreased detoxification activity on methylglyocal-adducted CoA.|||In PARK7; no apparent effect on protein stability; impaired mitochondrial morphology; no effect on detoxification activity on methylglyocal-adducted CoA.|||In PARK7; strongly decreases enzymatic activity; reduces protein stability and leads to increased degradation; ubiquitinated by PRKN leading to its recognition by HDAC6 and targeting to aggresome where is degraded; interferes with homodimerization; abolishes interaction with PIAS2; reduced localization in lipid rafts; almost abolished detoxification activity on methylglyocal-adducted CoA.|||In PARK7; unknown pathological significance.|||Loss of protein and nucleic acid deglycase activity. No effect on mitochondrial translocation. Reduced protease activity. No effect on protection against metal cytotoxicity. No effect on methylglyoxal-adducted glutathione or CoA.|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||No effect on detoxification activity on methylglyocal-adducted CoA.|||No effect on mitochondrial translocation neither on deglycase activity.|||Nucleophile|||Parkinson disease protein 7|||Partially compensates for loss of stability; when associated with P-166.|||Phosphotyrosine|||Probable disease-associated variant found in early-onset Parkinson disease with digenic inheritance; no effect on detoxification activity on methylglyocal-adducted CoA; the patient also carries PINK1 mutation L-399.|||Reduces protein stability. No effect on oxidation.|||Reduces protein stability. No effect on oxidation. Reduced localization in lipid rafts; when associated with A-106.|||Removed|||Removed in mature form|||S-palmitoyl cysteine|||S-palmitoyl cysteine; alternate|||Strongly decreases enzymatic activity.|||Strongly decreases enzymatic activity. Almost abolishes detoxification activity on methylglyocal-adducted CoA.|||Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide.|||Unknown pathological significance; no effect on detoxification activity on methylglyocal-adducted CoA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157849|||http://purl.uniprot.org/annotation/PRO_0000405558|||http://purl.uniprot.org/annotation/VAR_020492|||http://purl.uniprot.org/annotation/VAR_020493|||http://purl.uniprot.org/annotation/VAR_020494|||http://purl.uniprot.org/annotation/VAR_020495|||http://purl.uniprot.org/annotation/VAR_020496|||http://purl.uniprot.org/annotation/VAR_020497|||http://purl.uniprot.org/annotation/VAR_020498|||http://purl.uniprot.org/annotation/VAR_020499|||http://purl.uniprot.org/annotation/VAR_034801|||http://purl.uniprot.org/annotation/VAR_072589|||http://purl.uniprot.org/annotation/VAR_083277|||http://purl.uniprot.org/annotation/VAR_084339
http://togogenome.org/gene/9606:RNASET2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00584                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the effect on degradation of mitochondrion-associated cytosolic rRNAs.|||In LCWM; the loss of a disulfide bond may affect protein folding and stability; the protein is retained in the endoplasmic reticulum and the mitochondria while lysosomal localization is disrupted.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Ribonuclease T2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030987|||http://purl.uniprot.org/annotation/VAR_013004|||http://purl.uniprot.org/annotation/VAR_063596|||http://purl.uniprot.org/annotation/VSP_008405|||http://purl.uniprot.org/annotation/VSP_008406
http://togogenome.org/gene/9606:OR11H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH07                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332963
http://togogenome.org/gene/9606:NID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14112                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||N-linked (GlcNAc...) asparagine|||NIDO|||Nidogen G2 beta-barrel|||Nidogen-2|||O-linked (Xyl...) (chondroitin sulfate) serine|||Omega-N-methylarginine|||Pro residues|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007671|||http://purl.uniprot.org/annotation/VAR_035836|||http://purl.uniprot.org/annotation/VAR_055767|||http://purl.uniprot.org/annotation/VAR_055768|||http://purl.uniprot.org/annotation/VAR_055769|||http://purl.uniprot.org/annotation/VAR_055770|||http://purl.uniprot.org/annotation/VAR_055771|||http://purl.uniprot.org/annotation/VAR_055772|||http://purl.uniprot.org/annotation/VAR_055773|||http://purl.uniprot.org/annotation/VAR_062850|||http://purl.uniprot.org/annotation/VAR_062851|||http://purl.uniprot.org/annotation/VAR_062852|||http://purl.uniprot.org/annotation/VAR_062853|||http://purl.uniprot.org/annotation/VSP_038779|||http://purl.uniprot.org/annotation/VSP_038780
http://togogenome.org/gene/9606:WIPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Binds actin|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||WAS/WASL-interacting protein family member 2|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065975|||http://purl.uniprot.org/annotation/VSP_012967
http://togogenome.org/gene/9606:VN1R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFZ6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=0|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Vomeronasal type-1 receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070214|||http://purl.uniprot.org/annotation/VAR_022798
http://togogenome.org/gene/9606:CTNNBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYA6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Basic and acidic residues|||Beta-catenin-like protein 1|||Disordered|||HEAT 1|||HEAT 2|||In IMD99; when expressed in a B lymphocyte cell line, leads to decreased frequencies of somatic hypermutations, a process involved in the production of isotype-switched high-affinity antibodies, the defect that can be rescued by the wild-type protein; decrease interaction with AICDA, hence impairs AICDA nuclear localization; may decrease protein stability; no effect on interaction with CDC5L.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine|||No change in NLS binding nor folding.|||Nuclear and cytoplasmic localization.|||Nuclear export signal (NES)|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079490|||http://purl.uniprot.org/annotation/VAR_059638|||http://purl.uniprot.org/annotation/VAR_087117|||http://purl.uniprot.org/annotation/VSP_004058|||http://purl.uniprot.org/annotation/VSP_004059|||http://purl.uniprot.org/annotation/VSP_015182|||http://purl.uniprot.org/annotation/VSP_055261
http://togogenome.org/gene/9606:UGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60701                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes hydrolysis of the covalent intermediate between substrate and the catalytic cysteine residue.|||Allosteric switch region|||Disordered|||Impairs protein folding. Decreases affinity for UDP-glucose. No effect on inhibition by UDP-xylose. No effect on hysteresis and cooperativity.|||Important for formation of active hexamer structure|||In DEE84.|||In DEE84; decreased function in glycosaminoglycan biosynthetic process in patient cells; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity.|||In DEE84; severely decreased protein stability; decreased hexamer formation; severe decrease of UDP-glucose 6-dehydrogenase activity.|||In DEE84; unknown pathological significance.|||In DEE84; unknown pathological significance; may affect splicing.|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||Loss of hexamer formation. Causes formation of stable dimers. Strongly decreased specific activity at pH 8.4.|||Loss of hexamer formation. Causes formation of stable dimers. Strongly reduced affinity for NAD and UDP-glucose, and strongly decreased catalytic efficiency at pH 8.6.|||N6-acetyllysine|||Nearly abolishes enzyme activity. Stabilizes the enzyme in a low-activity hexameric conformation.|||No effect on the intrinsically disordered nature of the C-terminus. No effect on affinity for the inhibitor UDP-xylose.|||No significant effect on catalytic activity and on affinity for NAD and UDP-glucose. Decreases affinity for the inhibitor UDP-xylose. Disrupts hysteresis and cooperativity.|||Nucleophile|||Phosphoserine|||Proton donor/acceptor|||Reduced affinity for UDP-glucose, and reduced catalytic efficiency.|||Stabilizes the active conformation of the hexamer. Decreases affinity for UDP-xylose, but not for UDP-glucose. Disrupts hysteresis and cooperativity.|||Strongly decreases affinity for the inhibitor UDP-xylose.|||UDP-glucose 6-dehydrogenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074060|||http://purl.uniprot.org/annotation/VAR_083750|||http://purl.uniprot.org/annotation/VAR_083751|||http://purl.uniprot.org/annotation/VAR_083752|||http://purl.uniprot.org/annotation/VAR_083753|||http://purl.uniprot.org/annotation/VAR_083754|||http://purl.uniprot.org/annotation/VAR_083755|||http://purl.uniprot.org/annotation/VAR_083756|||http://purl.uniprot.org/annotation/VAR_083757|||http://purl.uniprot.org/annotation/VAR_083758|||http://purl.uniprot.org/annotation/VAR_083759|||http://purl.uniprot.org/annotation/VAR_083760|||http://purl.uniprot.org/annotation/VAR_083761|||http://purl.uniprot.org/annotation/VAR_083762|||http://purl.uniprot.org/annotation/VAR_083763|||http://purl.uniprot.org/annotation/VAR_083764|||http://purl.uniprot.org/annotation/VAR_083765|||http://purl.uniprot.org/annotation/VAR_083766|||http://purl.uniprot.org/annotation/VAR_083767|||http://purl.uniprot.org/annotation/VAR_083768|||http://purl.uniprot.org/annotation/VAR_083769|||http://purl.uniprot.org/annotation/VAR_083770|||http://purl.uniprot.org/annotation/VAR_083771|||http://purl.uniprot.org/annotation/VAR_083772|||http://purl.uniprot.org/annotation/VSP_042550|||http://purl.uniprot.org/annotation/VSP_046234
http://togogenome.org/gene/9606:ARHGEF38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXL2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAR|||DH|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||Phosphothreonine|||Rho guanine nucleotide exchange factor 38|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318987|||http://purl.uniprot.org/annotation/VAR_038928|||http://purl.uniprot.org/annotation/VAR_038929|||http://purl.uniprot.org/annotation/VSP_053830
http://togogenome.org/gene/9606:SHISA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJX4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||Protein shisa-3 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330025|||http://purl.uniprot.org/annotation/VAR_042687
http://togogenome.org/gene/9606:PFKP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V3Z0|||http://purl.uniprot.org/uniprot/B1APP6|||http://purl.uniprot.org/uniprot/Q01813                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent 6-phosphofructokinase, platelet type|||C-terminal regulatory PFK domain 2|||Decreased interaction with ATG4B.|||In isoform 2.|||Interdomain linker|||N-acetylmethionine|||N-terminal catalytic PFK domain 1|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphofructokinase|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112024|||http://purl.uniprot.org/annotation/PRO_5019859887|||http://purl.uniprot.org/annotation/VSP_046416
http://togogenome.org/gene/9606:ZNF561                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAD9|||http://purl.uniprot.org/uniprot/Q8N587                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 561                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047650|||http://purl.uniprot.org/annotation/VSP_055964
http://togogenome.org/gene/9606:ZNF440                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYI8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 440                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047589|||http://purl.uniprot.org/annotation/VAR_052828|||http://purl.uniprot.org/annotation/VAR_052829|||http://purl.uniprot.org/annotation/VAR_059915|||http://purl.uniprot.org/annotation/VAR_059916
http://togogenome.org/gene/9606:GTPBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2K2|||http://purl.uniprot.org/uniprot/Q9BX10                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GTP-binding protein 2|||In JABELS; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248500|||http://purl.uniprot.org/annotation/VAR_080975|||http://purl.uniprot.org/annotation/VAR_080976|||http://purl.uniprot.org/annotation/VAR_080977|||http://purl.uniprot.org/annotation/VSP_052154|||http://purl.uniprot.org/annotation/VSP_052155|||http://purl.uniprot.org/annotation/VSP_052156
http://togogenome.org/gene/9606:SERP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Anchor for type IV membrane protein|||Stress-associated endoplasmic reticulum protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274794
http://togogenome.org/gene/9606:TPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07202|||http://purl.uniprot.org/uniprot/Q502Y3|||http://purl.uniprot.org/uniprot/Q6P534                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like; calcium-binding|||Extracellular|||Helical|||In TDH2A.|||In TDH2A; fails to localize to the plasma membrane.|||In TDH2A; loss of activity.|||In TDH2A; partial defect; expressed on the plasma membrane surface at less than half the rate of wild-type enzyme.|||In TDH2A; partial defect; expression slightly lower in efficiency and more degenerative than wild-type enzyme.|||In TDH2A; unknown pathological significance.|||In isoform 2, isoform 2-3, isoform 2-4 and isoform 6.|||In isoform 3 and isoform 2-3.|||In isoform 4 and isoform 2-4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Sushi|||Thyroid peroxidase|||Transition state stabilizer|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023662|||http://purl.uniprot.org/annotation/PRO_5004247508|||http://purl.uniprot.org/annotation/PRO_5004278002|||http://purl.uniprot.org/annotation/VAR_006057|||http://purl.uniprot.org/annotation/VAR_006058|||http://purl.uniprot.org/annotation/VAR_006059|||http://purl.uniprot.org/annotation/VAR_006060|||http://purl.uniprot.org/annotation/VAR_006061|||http://purl.uniprot.org/annotation/VAR_006062|||http://purl.uniprot.org/annotation/VAR_013138|||http://purl.uniprot.org/annotation/VAR_015375|||http://purl.uniprot.org/annotation/VAR_021622|||http://purl.uniprot.org/annotation/VAR_021623|||http://purl.uniprot.org/annotation/VAR_021624|||http://purl.uniprot.org/annotation/VAR_021625|||http://purl.uniprot.org/annotation/VAR_021626|||http://purl.uniprot.org/annotation/VAR_021627|||http://purl.uniprot.org/annotation/VAR_021628|||http://purl.uniprot.org/annotation/VAR_021629|||http://purl.uniprot.org/annotation/VAR_021630|||http://purl.uniprot.org/annotation/VAR_021631|||http://purl.uniprot.org/annotation/VAR_021632|||http://purl.uniprot.org/annotation/VAR_021633|||http://purl.uniprot.org/annotation/VAR_021634|||http://purl.uniprot.org/annotation/VAR_021635|||http://purl.uniprot.org/annotation/VAR_021636|||http://purl.uniprot.org/annotation/VAR_021637|||http://purl.uniprot.org/annotation/VAR_025784|||http://purl.uniprot.org/annotation/VAR_027229|||http://purl.uniprot.org/annotation/VAR_027230|||http://purl.uniprot.org/annotation/VAR_027231|||http://purl.uniprot.org/annotation/VAR_027232|||http://purl.uniprot.org/annotation/VAR_027233|||http://purl.uniprot.org/annotation/VAR_027234|||http://purl.uniprot.org/annotation/VAR_027235|||http://purl.uniprot.org/annotation/VAR_027236|||http://purl.uniprot.org/annotation/VAR_027237|||http://purl.uniprot.org/annotation/VAR_078336|||http://purl.uniprot.org/annotation/VAR_078337|||http://purl.uniprot.org/annotation/VSP_004665|||http://purl.uniprot.org/annotation/VSP_004666|||http://purl.uniprot.org/annotation/VSP_007268|||http://purl.uniprot.org/annotation/VSP_007269|||http://purl.uniprot.org/annotation/VSP_007270
http://togogenome.org/gene/9606:USP49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70CQ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of deubiquitinase activity.|||Nucleophile|||Polar residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080678|||http://purl.uniprot.org/annotation/VSP_011556
http://togogenome.org/gene/9606:CYTH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9W0|||http://purl.uniprot.org/uniprot/Q15438                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-terminal autoinhibitory region|||Cytohesin-1|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||PH|||Reduces guanine exchange factor activity by over 90%.|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120194|||http://purl.uniprot.org/annotation/VSP_006034|||http://purl.uniprot.org/annotation/VSP_055884
http://togogenome.org/gene/9606:COL8A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PP49|||http://purl.uniprot.org/uniprot/P25067                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen alpha-2(VIII) chain|||Disordered|||In FECD1 and PPCD2.|||In FECD1.|||In FECD1; unknown pathological significance.|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005835|||http://purl.uniprot.org/annotation/VAR_017893|||http://purl.uniprot.org/annotation/VAR_017894|||http://purl.uniprot.org/annotation/VAR_017895|||http://purl.uniprot.org/annotation/VAR_017896|||http://purl.uniprot.org/annotation/VAR_017897|||http://purl.uniprot.org/annotation/VAR_017898|||http://purl.uniprot.org/annotation/VAR_017899|||http://purl.uniprot.org/annotation/VAR_017900|||http://purl.uniprot.org/annotation/VAR_021387
http://togogenome.org/gene/9606:DYNAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EMN5|||http://purl.uniprot.org/uniprot/Q8N1N2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CLLAC-motif containing|||Cytoplasmic|||Disordered|||Dynactin-associated protein|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079315|||http://purl.uniprot.org/annotation/VAR_033751|||http://purl.uniprot.org/annotation/VAR_033752
http://togogenome.org/gene/9606:C1QTNF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 5|||Disordered|||In LORD.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003535|||http://purl.uniprot.org/annotation/VAR_032628|||http://purl.uniprot.org/annotation/VAR_032629
http://togogenome.org/gene/9606:MARCHF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitination of ERGIC3 and CFTR, and degradation of CFTR; when associated with S-64. Reduces ubiquitination of DLG1; when associated with S-64, S-106 and S-109. Reduces inhibition of HIV-1 virus production and VSVG protein expression; when associated with S-64. Abolishes ubiquitination of IKBKG/NEMO; when associated with S-64 and Q-90.|||Abolishes ubiquitination of ERGIC3 and CFTR, and degradation of CFTR; when associated with S-67. Reduces ubiquitination of DLG1 ; when associated with S-67, S-106 and S-109. Reduces inhibition of HIV-1 virus production and VSVG protein expression; when associated with S-67. Abolishes ubiquitination of IKBKG/NEMO; when associated with S-67 and Q-90.|||Abolishes ubiquitination of IKBKG/NEMO; when associated with S-64 and S-67.|||Abolishes ubiquitination of and interaction with DLG1; when associated with A-97.|||E3 ubiquitin-protein ligase MARCHF2|||Helical|||In isoform 2.|||RING-CH-type|||Reduces ubiquitination of DLG1. No effect on interaction with DLG1. Abolishes ubiquitination of and interaction with DLG1; when associated with 243-E--V-246 DEL.|||Reduces ubiquitination of DLG1; when associated with S-64, S-67 and S-106.|||Reduces ubiquitination of DLG1; when associated with S-64, S-67 and S-109.|||Required for inhibition of HIV-1 virus production and VSV G protein expression|||Required for interaction with IKBKG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055925|||http://purl.uniprot.org/annotation/VAR_030303|||http://purl.uniprot.org/annotation/VAR_053638|||http://purl.uniprot.org/annotation/VSP_041478
http://togogenome.org/gene/9606:SIX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBA2|||http://purl.uniprot.org/uniprot/Q9NPC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX2|||In a renal hypodysplasia patient.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049297|||http://purl.uniprot.org/annotation/VAR_071207|||http://purl.uniprot.org/annotation/VAR_071208|||http://purl.uniprot.org/annotation/VAR_071209
http://togogenome.org/gene/9606:SCN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99250                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Binds Mu-conotoxin KIIIA|||Binds Mu-conotoxin KIIIA; via amide nitrogen|||Binds Mu-conotoxin KIIIA; via carbonyl oxygen|||Binds SCN2B|||Binds SCN2B; via carbonyl oxygen|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with Dravet syndrome; unknown pathological significance.|||Found in a patient with acute encephalitis with refractory and repetitive partial seizures; unknown pathological significance.|||Found in a patient with acute encephalopathy with biphasic seizures, late reduced diffusion and in a patient with Dravet syndrome; unknown pathological significance.|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with autism; unknown pathological significance.|||Found in a patient with non-specific acute encephalopathy; unknown pathological significance.|||Found in a patient with schizofrenia; unknown pathological significance.|||Found in autism; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IQ|||IV|||Important for channel closure|||In BFIS3.|||In BFIS3; gain of function mutation; hyperpolarizing shift of the activation curve.|||In BFIS3; increased voltage-gated sodium channel activity; decreased overall channel availability during repetitive stimulation; gain of function; no effect on kinetics of activation or inactivation; no effect on voltage dependence of activation.|||In BFIS3; increased voltage-gated sodium channel activity; depolarized shift of steady-state inactivation; increased persistent sodium current; slower fast inactivation; accelerated recovery of fast inactivation; gain of function.|||In BFIS3; increased voltage-gated sodium channel activity; faster recovery from inactivation; gain of function.|||In BFIS3; increased voltage-gated sodium channel activity; gain of function.|||In BFIS3; increased voltage-gated sodium channel activity; impaired fast inactivation; no effect on kinetics of activation or inactivation; no effect on voltage dependence of activation; gain of function.|||In BFIS3; increased voltage-gated sodium channel activity; increased persistent sodium current; gain of function.|||In BFIS3; increased voltage-gated sodium channel activity; modified voltage dependence of activation and inactivation; gain of function.|||In BFIS3; modified voltage-gated sodium channel activity; modified voltage dependence of activation and inactivation.|||In BFIS3; mutant channel inactivates more slowly than wild-type whereas the sodium channel conductance is not affected.|||In BFIS3; unknown pathological significance.|||In DEE11 and EA9; increased voltage-gated sodium channel activity; increased persistent sodium current; gain of function.|||In DEE11 and EA9; unknown pathological significance; no effect on voltage-gated sodium channel activity; higher current density when associated with G-1882.|||In DEE11.|||In DEE11; also found in patients with familial episodic ataxia and impairment of speech development.|||In DEE11; hyperpolarizing shift of the activation curve and increased persitent current; gain of function.|||In DEE11; increased neuronal excitability; increased peak sodium current densities; gain of function.|||In DEE11; increased voltage-gated sodium channel activity; markedly altered the voltage-dependence of the channel; gain of function.|||In DEE11; markedly altered channel voltage-dependence; responds to modified Atkins diet.|||In DEE11; mild form with ataxia.|||In DEE11; modified voltage-gated sodium channel activity; activated with lowered voltage sensitivity; disturbed fast and slow inactivation.|||In DEE11; phenotype consistent with West syndrome; decreased neuronal excitability; decreased peak sodium current densities; loss of function.|||In DEE11; responds to ketogenic diet.|||In DEE11; the disease progresses to West syndrome.|||In DEE11; unknown pathological significance.|||In EA9; gain of function mutation resulting in increased voltage-gated sodium channel activity; hyperpolarized activation; higher current density when associated with A-1522 compared to wild-type or G-1882 alone.|||In EA9; unknown pathological significance.|||In isoform 2.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Pore-forming|||Probable disease-associated variant found in a boy with infantile spasms and bitemporal glucose hypometabolism.|||Probable disease-associated variant found in a patient with autism spectrum disorder.|||Probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; decreased expression; loss of function.|||Probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; faster channel inactivation; fewer channels contribution to macroscopic currents and fewer channels expressed on membrane.|||Probable disease-associated variant found in a patient with autism spectrum disorder; decreased voltage-gated sodium channel activity; faster channel inactivation; loss of function.|||Probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting.|||Probable disease-associated variant found in a patient with autism spectrum disorder; loss of voltage-gated sodium channel activity; non-conducting; no dominant-negative effect.|||Probable disease-associated variant found in a patient with drug-resistant focal epilepsy.|||Probable disease-associated variant found in a patient with early-onset seizures and Rett-like features, including autistic behavior, limited hand function with chorea and profound intellectual disability.|||Probable disease-associated variant found in a patient with intractable epilepsy and severe mental decline; non-conducting; loss of voltage-gated sodium channel activity; dominant-negative.|||Probable disease-associated variant found in a patient with non-syndromic intellectual disability and epilepsy.|||Probable disease-associated variant found in patients with GEFS+.|||Sodium channel protein type 2 subunit alpha|||There is no significant effects on the voltage-dependence of the channel. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048491|||http://purl.uniprot.org/annotation/VAR_029732|||http://purl.uniprot.org/annotation/VAR_029733|||http://purl.uniprot.org/annotation/VAR_029734|||http://purl.uniprot.org/annotation/VAR_029735|||http://purl.uniprot.org/annotation/VAR_029736|||http://purl.uniprot.org/annotation/VAR_029737|||http://purl.uniprot.org/annotation/VAR_029738|||http://purl.uniprot.org/annotation/VAR_029739|||http://purl.uniprot.org/annotation/VAR_029740|||http://purl.uniprot.org/annotation/VAR_029741|||http://purl.uniprot.org/annotation/VAR_029742|||http://purl.uniprot.org/annotation/VAR_064331|||http://purl.uniprot.org/annotation/VAR_065176|||http://purl.uniprot.org/annotation/VAR_065177|||http://purl.uniprot.org/annotation/VAR_065178|||http://purl.uniprot.org/annotation/VAR_065179|||http://purl.uniprot.org/annotation/VAR_065180|||http://purl.uniprot.org/annotation/VAR_065181|||http://purl.uniprot.org/annotation/VAR_069996|||http://purl.uniprot.org/annotation/VAR_069997|||http://purl.uniprot.org/annotation/VAR_069998|||http://purl.uniprot.org/annotation/VAR_069999|||http://purl.uniprot.org/annotation/VAR_070000|||http://purl.uniprot.org/annotation/VAR_070001|||http://purl.uniprot.org/annotation/VAR_070002|||http://purl.uniprot.org/annotation/VAR_070003|||http://purl.uniprot.org/annotation/VAR_070004|||http://purl.uniprot.org/annotation/VAR_070005|||http://purl.uniprot.org/annotation/VAR_070006|||http://purl.uniprot.org/annotation/VAR_070007|||http://purl.uniprot.org/annotation/VAR_070008|||http://purl.uniprot.org/annotation/VAR_070009|||http://purl.uniprot.org/annotation/VAR_070010|||http://purl.uniprot.org/annotation/VAR_072745|||http://purl.uniprot.org/annotation/VAR_073428|||http://purl.uniprot.org/annotation/VAR_073429|||http://purl.uniprot.org/annotation/VAR_075572|||http://purl.uniprot.org/annotation/VAR_078195|||http://purl.uniprot.org/annotation/VAR_078196|||http://purl.uniprot.org/annotation/VAR_078197|||http://purl.uniprot.org/annotation/VAR_078198|||http://purl.uniprot.org/annotation/VAR_078199|||http://purl.uniprot.org/annotation/VAR_078200|||http://purl.uniprot.org/annotation/VAR_078201|||http://purl.uniprot.org/annotation/VAR_078448|||http://purl.uniprot.org/annotation/VAR_078449|||http://purl.uniprot.org/annotation/VAR_078450|||http://purl.uniprot.org/annotation/VAR_078451|||http://purl.uniprot.org/annotation/VAR_078452|||http://purl.uniprot.org/annotation/VAR_078453|||http://purl.uniprot.org/annotation/VAR_078454|||http://purl.uniprot.org/annotation/VAR_078455|||http://purl.uniprot.org/annotation/VAR_078456|||http://purl.uniprot.org/annotation/VAR_078457|||http://purl.uniprot.org/annotation/VAR_078458|||http://purl.uniprot.org/annotation/VAR_078459|||http://purl.uniprot.org/annotation/VAR_078460|||http://purl.uniprot.org/annotation/VAR_078461|||http://purl.uniprot.org/annotation/VAR_078462|||http://purl.uniprot.org/annotation/VAR_078463|||http://purl.uniprot.org/annotation/VAR_078464|||http://purl.uniprot.org/annotation/VAR_078465|||http://purl.uniprot.org/annotation/VAR_078466|||http://purl.uniprot.org/annotation/VAR_078467|||http://purl.uniprot.org/annotation/VAR_078468|||http://purl.uniprot.org/annotation/VAR_078469|||http://purl.uniprot.org/annotation/VAR_078470|||http://purl.uniprot.org/annotation/VAR_078471|||http://purl.uniprot.org/annotation/VAR_078472|||http://purl.uniprot.org/annotation/VAR_078473|||http://purl.uniprot.org/annotation/VAR_078474|||http://purl.uniprot.org/annotation/VAR_078475|||http://purl.uniprot.org/annotation/VAR_078476|||http://purl.uniprot.org/annotation/VAR_078477|||http://purl.uniprot.org/annotation/VAR_078478|||http://purl.uniprot.org/annotation/VAR_078479|||http://purl.uniprot.org/annotation/VAR_078480|||http://purl.uniprot.org/annotation/VAR_078482|||http://purl.uniprot.org/annotation/VAR_078483|||http://purl.uniprot.org/annotation/VAR_078484|||http://purl.uniprot.org/annotation/VAR_078485|||http://purl.uniprot.org/annotation/VAR_078486|||http://purl.uniprot.org/annotation/VAR_078487|||http://purl.uniprot.org/annotation/VAR_078730|||http://purl.uniprot.org/annotation/VAR_078731|||http://purl.uniprot.org/annotation/VAR_078732|||http://purl.uniprot.org/annotation/VAR_078733|||http://purl.uniprot.org/annotation/VAR_078734|||http://purl.uniprot.org/annotation/VAR_078735|||http://purl.uniprot.org/annotation/VAR_078736|||http://purl.uniprot.org/annotation/VAR_078737|||http://purl.uniprot.org/annotation/VAR_078738|||http://purl.uniprot.org/annotation/VAR_078739|||http://purl.uniprot.org/annotation/VAR_078740|||http://purl.uniprot.org/annotation/VAR_078741|||http://purl.uniprot.org/annotation/VAR_078742|||http://purl.uniprot.org/annotation/VAR_078743|||http://purl.uniprot.org/annotation/VAR_078744|||http://purl.uniprot.org/annotation/VAR_078745|||http://purl.uniprot.org/annotation/VAR_078746|||http://purl.uniprot.org/annotation/VAR_078747|||http://purl.uniprot.org/annotation/VAR_078748|||http://purl.uniprot.org/annotation/VAR_078749|||http://purl.uniprot.org/annotation/VAR_078750|||http://purl.uniprot.org/annotation/VAR_078751|||http://purl.uniprot.org/annotation/VAR_081430|||http://purl.uniprot.org/annotation/VAR_081431|||http://purl.uniprot.org/annotation/VAR_081432|||http://purl.uniprot.org/annotation/VAR_081433|||http://purl.uniprot.org/annotation/VAR_081434|||http://purl.uniprot.org/annotation/VAR_081435|||http://purl.uniprot.org/annotation/VAR_081436|||http://purl.uniprot.org/annotation/VSP_001032
http://togogenome.org/gene/9606:NRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GZS7|||http://purl.uniprot.org/uniprot/O14511                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Helical; Note=Internal signal sequence|||Ig-like|||Ig-like C2-type|||In isoform 2.|||In isoform 3 and isoform DON-1B.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform DON-1B.|||In isoform DON-1R.|||N-linked (GlcNAc...) asparagine|||Neuregulin-2|||Polar residues|||Pro residues|||Pro-neuregulin-2, membrane-bound isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019472|||http://purl.uniprot.org/annotation/PRO_0000019473|||http://purl.uniprot.org/annotation/PRO_0000019474|||http://purl.uniprot.org/annotation/VSP_003451|||http://purl.uniprot.org/annotation/VSP_003452|||http://purl.uniprot.org/annotation/VSP_003453|||http://purl.uniprot.org/annotation/VSP_003454|||http://purl.uniprot.org/annotation/VSP_003455|||http://purl.uniprot.org/annotation/VSP_003456|||http://purl.uniprot.org/annotation/VSP_003457|||http://purl.uniprot.org/annotation/VSP_003458|||http://purl.uniprot.org/annotation/VSP_003459
http://togogenome.org/gene/9606:BTBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX70                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein 2|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186210|||http://purl.uniprot.org/annotation/VSP_010562
http://togogenome.org/gene/9606:C3orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BVD1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In HYPT15; loss of expression in homozygous patient cells.|||In HYPT15; reduced expression in homozygous patient cells; does not localize to the cell membrane; decreased interaction with LIPH; results in strongly decreased LIPH-mediated synthesis of 2-acyl lysophosphatidic acid.|||In isoform 2.|||In isoform 3.|||TPA-induced transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248024|||http://purl.uniprot.org/annotation/VAR_027203|||http://purl.uniprot.org/annotation/VAR_027204|||http://purl.uniprot.org/annotation/VAR_059736|||http://purl.uniprot.org/annotation/VAR_087942|||http://purl.uniprot.org/annotation/VAR_087943|||http://purl.uniprot.org/annotation/VSP_036120|||http://purl.uniprot.org/annotation/VSP_036121
http://togogenome.org/gene/9606:ARX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2. Abolishes transcriptional activation of KDM5C.|||Acidic residues|||Disordered|||Homeobox|||Homeobox protein ARX|||In ACCAG; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2.|||In DEE1 and PRTS; also found in non-specific intellectual disability families; frequent variant.|||In DEE1.|||In DEE1; corpus callosum hypoplasia and simplified gyral pattern observed in one patient; reduces sequence-specific DNA-binding; slightly reduces transcriptional repression of LMO1.|||In LISX2.|||In LISX2; abolishes transcriptional activation of KDM5C; abolishes sequence-specific DNA-binding; reduces transcriptional repression of LMO1 and SHOX2.|||In LISX2; severe phenotype.|||In XLID29.|||OAR|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048819|||http://purl.uniprot.org/annotation/VAR_015177|||http://purl.uniprot.org/annotation/VAR_015178|||http://purl.uniprot.org/annotation/VAR_015179|||http://purl.uniprot.org/annotation/VAR_015180|||http://purl.uniprot.org/annotation/VAR_015669|||http://purl.uniprot.org/annotation/VAR_015670|||http://purl.uniprot.org/annotation/VAR_015671|||http://purl.uniprot.org/annotation/VAR_033260|||http://purl.uniprot.org/annotation/VAR_033261|||http://purl.uniprot.org/annotation/VAR_033262|||http://purl.uniprot.org/annotation/VAR_033263
http://togogenome.org/gene/9606:STK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVN8|||http://purl.uniprot.org/uniprot/Q13043                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Disordered|||In isoform 2.|||Loss of activity.|||Loss of homodimerization, activation, and autophosphorylation.|||N-acetylmethionine|||No effect on activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-326.|||Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-349.|||SARAH|||Serine/threonine-protein kinase 4|||Serine/threonine-protein kinase 4 18kDa subunit|||Serine/threonine-protein kinase 4 37kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086691|||http://purl.uniprot.org/annotation/PRO_0000413735|||http://purl.uniprot.org/annotation/PRO_0000413736|||http://purl.uniprot.org/annotation/VAR_027040|||http://purl.uniprot.org/annotation/VAR_041123|||http://purl.uniprot.org/annotation/VAR_041124|||http://purl.uniprot.org/annotation/VAR_041125|||http://purl.uniprot.org/annotation/VAR_041126|||http://purl.uniprot.org/annotation/VSP_019851|||http://purl.uniprot.org/annotation/VSP_019852
http://togogenome.org/gene/9606:NAA16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU51|||http://purl.uniprot.org/uniprot/Q6N069                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-alpha-acetyltransferase 16, NatA auxiliary subunit|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106297|||http://purl.uniprot.org/annotation/VAR_052618|||http://purl.uniprot.org/annotation/VSP_012562|||http://purl.uniprot.org/annotation/VSP_012563|||http://purl.uniprot.org/annotation/VSP_012564|||http://purl.uniprot.org/annotation/VSP_012565|||http://purl.uniprot.org/annotation/VSP_012566|||http://purl.uniprot.org/annotation/VSP_012567|||http://purl.uniprot.org/annotation/VSP_012568|||http://purl.uniprot.org/annotation/VSP_012569
http://togogenome.org/gene/9606:TNIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KP6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes ubiquitin binding; loss of inhibitory activity on NF-kappa-B activation.|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||TNFAIP3-interacting protein 3|||Ubiquitin-binding domain (UBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072607|||http://purl.uniprot.org/annotation/VAR_057006|||http://purl.uniprot.org/annotation/VSP_045101|||http://purl.uniprot.org/annotation/VSP_045102|||http://purl.uniprot.org/annotation/VSP_045103
http://togogenome.org/gene/9606:ARL6IP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMZ5|||http://purl.uniprot.org/uniprot/Q8N6S5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 6-interacting protein 6|||Disordered|||Helical|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307324
http://togogenome.org/gene/9606:ZNF593                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00488                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||Zinc finger protein 593                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047684|||http://purl.uniprot.org/annotation/VAR_059924
http://togogenome.org/gene/9606:GPR173                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS66                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 173                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069650
http://togogenome.org/gene/9606:LRTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat and transmembrane domain-containing protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279756|||http://purl.uniprot.org/annotation/VAR_051144|||http://purl.uniprot.org/annotation/VAR_051145|||http://purl.uniprot.org/annotation/VSP_023507
http://togogenome.org/gene/9606:CEP170B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4F5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 170 kDa protein B|||Disordered|||FHA|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282889|||http://purl.uniprot.org/annotation/VSP_024247|||http://purl.uniprot.org/annotation/VSP_024248
http://togogenome.org/gene/9606:ABCG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-2|||ABC transporter|||Associated with high serum levels of uric acid and increased risk of gout; results in lower urate transport rates compared to wild-type; decreased protein abundance.|||Broad substrate specificity ATP-binding cassette transporter ABCG2|||Cytoplasmic|||Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.|||Decreased protein abundance. Decreased localization to the plasma membrane and retained intracellularly. Loss of ATPase-coupled transmembrane transporter activity.|||Decreased protein abundance. No effect on substrate transmembrane transport.|||Decreased protein abundance; decreased localization to the plasma membrane; no effect on ATPase-coupled transmembrane transporter activity.|||Decreased protein abundance; loss of localization to the plasma membrane.|||Decreased protein abundance; no effect on localization to the plasma membrane; no effect on substrate transmembrane transport; decreased ATPase activity; no effect on ATPase-coupled transmembrane transporter activity.|||Decreases ATPase activity.|||Decreases transport activity.|||Extracellular|||Found in Jr(a-) blood group phenotype.|||Helical|||In isoform 2.|||Increases ATPase activity.|||Interchain|||Loss of glycosylation.|||Loss of phosphorylation by PIM1. Constitutive drug resistance independent of PIM1.|||Loss of phosphorylation by PIM1. Decreased localization to the plasma membrane. Decreased homooligomerization. Loss of function in resistance to drug treatment.|||Loss of protein expression.|||Loss of protein expression; loss of localization to the plasma membrane.|||N-linked (GlcNAc...) asparagine|||No change in ATPase activity.|||No effect on hemin binding.|||No effect on protein abundance; no effect on localization to the plasma membrane; increased ATPase activity; decreased ATPase-coupled transmembrane transporter activity.|||No effect on protein abundance; no effect on localization to the plasma membrane; no effect on ATPase activity; decreased ATPase-coupled transmembrane transporter activity.|||No effect on protein abundance; no effect on localization to the plasma membrane; no effect on ATPase activity; no effect on substrate transmembrane transport.|||No effect on protein abundance; no effect on substrate transmembrane transport.|||No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Decreased substrate-induced ATP hydrolysis. Decreased substrate transport.|||No effect on stability. Decreased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Decreased substrate transport.|||No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased basal and substrate-induced ATP hydrolysis. Increased substrate transport.|||No effect on stability. Increased estrone-3 sulfate ATPase-coupled transmembrane transporter activity. Increased substrate-induced ATP hydrolysis. Increased substrate transport.|||No effect on stability. No effect on estrone-3 sulfate ATPase-coupled transmembrane transporter activity. No effect on substrate-induced ATP hydrolysis. No effect on substrate transport.|||No effect.|||Not glycosylated|||Phosphothreonine; by PIM1|||Strongly reduced binding to hemin but not to PPIX.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093386|||http://purl.uniprot.org/annotation/VAR_018349|||http://purl.uniprot.org/annotation/VAR_018350|||http://purl.uniprot.org/annotation/VAR_020779|||http://purl.uniprot.org/annotation/VAR_020780|||http://purl.uniprot.org/annotation/VAR_022443|||http://purl.uniprot.org/annotation/VAR_022704|||http://purl.uniprot.org/annotation/VAR_022705|||http://purl.uniprot.org/annotation/VAR_022706|||http://purl.uniprot.org/annotation/VAR_022707|||http://purl.uniprot.org/annotation/VAR_022708|||http://purl.uniprot.org/annotation/VAR_022709|||http://purl.uniprot.org/annotation/VAR_030357|||http://purl.uniprot.org/annotation/VAR_030358|||http://purl.uniprot.org/annotation/VAR_035355|||http://purl.uniprot.org/annotation/VAR_067363|||http://purl.uniprot.org/annotation/VAR_067364|||http://purl.uniprot.org/annotation/VAR_067365|||http://purl.uniprot.org/annotation/VAR_067366|||http://purl.uniprot.org/annotation/VAR_082302|||http://purl.uniprot.org/annotation/VAR_082303|||http://purl.uniprot.org/annotation/VAR_082304|||http://purl.uniprot.org/annotation/VAR_082305|||http://purl.uniprot.org/annotation/VAR_082306|||http://purl.uniprot.org/annotation/VAR_082307|||http://purl.uniprot.org/annotation/VAR_082308|||http://purl.uniprot.org/annotation/VAR_082309|||http://purl.uniprot.org/annotation/VSP_014232|||http://purl.uniprot.org/annotation/VSP_014233
http://togogenome.org/gene/9606:HIP1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQW8|||http://purl.uniprot.org/uniprot/B4DPL0|||http://purl.uniprot.org/uniprot/O75146                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  AP180 N-terminal homology (ANTH)|||Basic and acidic residues|||Disordered|||ENTH|||Huntingtin-interacting protein 1 clathrin-binding|||Huntingtin-interacting protein 1-related protein|||I/LWEQ|||Important for actin binding|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Reduced acting binding.|||Strongly reduced actin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083984|||http://purl.uniprot.org/annotation/VAR_020043|||http://purl.uniprot.org/annotation/VAR_051029|||http://purl.uniprot.org/annotation/VAR_051030|||http://purl.uniprot.org/annotation/VAR_051031|||http://purl.uniprot.org/annotation/VAR_070814|||http://purl.uniprot.org/annotation/VSP_054238|||http://purl.uniprot.org/annotation/VSP_054239
http://togogenome.org/gene/9606:CT45A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMU8|||http://purl.uniprot.org/uniprot/P0DMU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A10|||Cancer/testis antigen family 45 member A5|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308950|||http://purl.uniprot.org/annotation/PRO_0000433032
http://togogenome.org/gene/9606:TRAPPC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YXQ9|||http://purl.uniprot.org/uniprot/Q8WVT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In PEBAS; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||Polar residues|||Pro residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Trafficking protein particle complex subunit 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106401|||http://purl.uniprot.org/annotation/VAR_028442|||http://purl.uniprot.org/annotation/VAR_035869|||http://purl.uniprot.org/annotation/VAR_080390
http://togogenome.org/gene/9606:EIF2AK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIT4|||http://purl.uniprot.org/uniprot/B3KY45|||http://purl.uniprot.org/uniprot/Q68DI6|||http://purl.uniprot.org/uniprot/Q9NZJ5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Eukaryotic translation initiation factor 2-alpha kinase 3|||Helical|||In WRS.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024322|||http://purl.uniprot.org/annotation/VAR_011408|||http://purl.uniprot.org/annotation/VAR_011409|||http://purl.uniprot.org/annotation/VAR_011410|||http://purl.uniprot.org/annotation/VAR_011411|||http://purl.uniprot.org/annotation/VAR_040477|||http://purl.uniprot.org/annotation/VAR_040478
http://togogenome.org/gene/9606:PSEN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49810                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In AD4.|||In AD4; increased mitochondrion-endoplasmic reticulum membrane tethering resulting in increased calcium transfer to mitochondria.|||In AD4; late-onset Alzheimer disease.|||In AD4; likely benign variant.|||In AD4; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; loss of function as calcium-leak channel; results in calcium overload in the endoplasmic reticulum; increased mitochondrion-endoplasmic reticulum membrane tethering resulting in increased calcium transfer to mitochondria.|||In AD4; unknown pathological significance.|||In CMD1V and AD4; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Lumenal|||PAL|||Phosphoserine|||Polar residues|||Presenilin-2 CTF subunit|||Presenilin-2 NTF subunit|||Reduces production of amyloid-beta in APP processing and of NICD in NOTCH1 processing. Increased mitochondrion-endoplasmic reticulum membrane tethering resulting in increased calcium transfer to mitochondria.|||Reduces production of amyloid-beta in APP processing.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025603|||http://purl.uniprot.org/annotation/PRO_0000025604|||http://purl.uniprot.org/annotation/VAR_006461|||http://purl.uniprot.org/annotation/VAR_006462|||http://purl.uniprot.org/annotation/VAR_006463|||http://purl.uniprot.org/annotation/VAR_007958|||http://purl.uniprot.org/annotation/VAR_009214|||http://purl.uniprot.org/annotation/VAR_009215|||http://purl.uniprot.org/annotation/VAR_064903|||http://purl.uniprot.org/annotation/VAR_070027|||http://purl.uniprot.org/annotation/VAR_081261|||http://purl.uniprot.org/annotation/VAR_081262|||http://purl.uniprot.org/annotation/VAR_081263|||http://purl.uniprot.org/annotation/VSP_005194|||http://purl.uniprot.org/annotation/VSP_043648
http://togogenome.org/gene/9606:ACAD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q709F0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase family member 11|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||N6-succinyllysine|||Phosphotyrosine|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254145|||http://purl.uniprot.org/annotation/VAR_028826|||http://purl.uniprot.org/annotation/VSP_021187|||http://purl.uniprot.org/annotation/VSP_021188
http://togogenome.org/gene/9606:RFX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q33E94                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Necessary for dimerization|||RFX-type winged-helix|||Transcription factor RFX4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314237|||http://purl.uniprot.org/annotation/VAR_037873|||http://purl.uniprot.org/annotation/VAR_057152|||http://purl.uniprot.org/annotation/VSP_030242|||http://purl.uniprot.org/annotation/VSP_030243|||http://purl.uniprot.org/annotation/VSP_030244|||http://purl.uniprot.org/annotation/VSP_030245|||http://purl.uniprot.org/annotation/VSP_030246
http://togogenome.org/gene/9606:DCSTAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H295                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dendritic cell-specific transmembrane protein|||Extracellular|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072584|||http://purl.uniprot.org/annotation/VAR_051438|||http://purl.uniprot.org/annotation/VSP_044787|||http://purl.uniprot.org/annotation/VSP_044788
http://togogenome.org/gene/9606:EXOC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NX51|||http://purl.uniprot.org/uniprot/Q96A65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Exocyst complex component 4|||Exocyst complex component Sec8 N-terminal|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118934|||http://purl.uniprot.org/annotation/VAR_036292|||http://purl.uniprot.org/annotation/VAR_036293|||http://purl.uniprot.org/annotation/VSP_047159
http://togogenome.org/gene/9606:LYPD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y78                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Able to bind to LRP6.|||Abolishes binding to LRP6.|||GPI-anchor amidated asparagine|||In isoform 2.|||Increased binding to LRP6.|||Ly6/PLAUR domain-containing protein 6|||N-linked (GlcNAc...) asparagine|||NxI motif|||Removed in mature form|||Severly reduces binding to LRP6.|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036178|||http://purl.uniprot.org/annotation/PRO_0000457041|||http://purl.uniprot.org/annotation/VSP_039306|||http://purl.uniprot.org/annotation/VSP_039307
http://togogenome.org/gene/9606:SMYD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Found in a patient with congenital heart defect.|||Found in a renal cell carcinoma sample; somatic mutation.|||MYND-type|||Probable disease-associated variant found in a patient with congenital heart defect; significant loss of interaction with HDAC1; fails to rescue the abnormal cardiac phenotypes defects in zebrafish morphants.|||SET|||SET and MYND domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227784|||http://purl.uniprot.org/annotation/VAR_025626|||http://purl.uniprot.org/annotation/VAR_025627|||http://purl.uniprot.org/annotation/VAR_025628|||http://purl.uniprot.org/annotation/VAR_057495|||http://purl.uniprot.org/annotation/VAR_057496|||http://purl.uniprot.org/annotation/VAR_057497|||http://purl.uniprot.org/annotation/VAR_057498|||http://purl.uniprot.org/annotation/VAR_064755|||http://purl.uniprot.org/annotation/VAR_084711|||http://purl.uniprot.org/annotation/VAR_084712
http://togogenome.org/gene/9606:EFNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20827                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Ephrin RBD|||Ephrin-A1|||Ephrin-A1, secreted form|||GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008353|||http://purl.uniprot.org/annotation/PRO_0000008354|||http://purl.uniprot.org/annotation/PRO_0000389630|||http://purl.uniprot.org/annotation/VAR_014791|||http://purl.uniprot.org/annotation/VSP_017543
http://togogenome.org/gene/9606:PARD6G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with PARD3 and CDC42|||PB1|||PDZ|||Partitioning defective 6 homolog gamma|||Pseudo-CRIB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112518|||http://purl.uniprot.org/annotation/VSP_047586|||http://purl.uniprot.org/annotation/VSP_047587
http://togogenome.org/gene/9606:PHB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99623                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with MAP1LC3B. No effect on interaction with PHB. No effect on mitochondrial location. Abolishes rescue of Parkin-mediated mitophagy.|||Decreases interaction with MAP1LC3B.|||In isoform 2.|||LC3-interaction region|||N-acetylalanine|||N6-acetyllysine|||Necessary for transcriptional repression|||No effect on homodimerization or interaction with PHB. Decreases mitochondrial dynamics. Disrupts mitochondrial-mediated antiviral innate immune response.|||No effect on interaction with MAP1LC3B.|||Phosphoserine|||Phosphotyrosine|||Prohibitin-2|||Reduces helicity. Decreases homodimerization and interaction with PHB. Disrupts mitochondrial dynamics. Disrupts mitochondrial-mediated antiviral innate immune response.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213884|||http://purl.uniprot.org/annotation/VSP_045311
http://togogenome.org/gene/9606:PDGFRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09619|||http://purl.uniprot.org/uniprot/Q59F04                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Breakpoint for insertion to form PDE4DIP-PDGFRB fusion protein|||Breakpoint for translocation to form TRIP11-PDGFRB|||Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In IBGC4; decreased protein abundance; no effect on receptor activity; decreased PDGF signaling pathway.|||In IBGC4; no effect on protein abundance; loss of PDGF beta receptor activity.|||In IBGC4; no effect on protein abundance; no effect on receptor activity; decreased PDGF signaling pathway.|||In IMF1.|||In KOGS.|||In PENTT; gain of function in protein tyrosine kinase activity; shows ligand-independent constitutive signaling.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Loss of interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity.|||Loss of kinase activity. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity.|||Loss of kinase activity; when associated with F-579. No effect on interaction with GRB10.|||Loss of kinase activity; when associated with F-581. Strongly reduces interaction with SRC family kinases. No effect on interaction with GRB10.|||N-linked (GlcNAc...) asparagine|||No effect neither on interaction with GRB10 and RASA1 nor on phosphatidylinositol 3-kinase activity.|||No effect on interaction with GRB10. Abolishes interaction with PLCG1; when associated with F-1021.|||No effect on interaction with RASA1 and on phosphatidylinositol 3-kinase activity.|||Phosphotyrosine; by ABL1 and ABL2|||Phosphotyrosine; by autocatalysis|||Platelet-derived growth factor receptor beta|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces kinase activity. No effect on interaction with GRB10. Abolishes interaction with RASA1. No effect on phosphatidylinositol 3-kinase activity.|||Strongly reduces expression levels.|||Strongly reduces up-regulation of cell proliferation. Abolishes interaction with PLCG1; when associated with F-1009. No effect on interaction with GRB10.|||Strongly reduces up-regulation of cell proliferation; when associated with F-740. Abolishes phosphatidylinositol 3-kinase activity and interaction with NCK1, and slightly reduces interaction with RASA1. No effect on interaction with GRB10.|||Strongly reduces up-regulation of cell proliferation; when associated with F-751. Strongly decreases phosphatidylinositol 3-kinase activity. No effect on interaction with GRB10 and RASA1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016757|||http://purl.uniprot.org/annotation/VAR_034377|||http://purl.uniprot.org/annotation/VAR_035125|||http://purl.uniprot.org/annotation/VAR_042027|||http://purl.uniprot.org/annotation/VAR_042028|||http://purl.uniprot.org/annotation/VAR_042029|||http://purl.uniprot.org/annotation/VAR_042030|||http://purl.uniprot.org/annotation/VAR_042031|||http://purl.uniprot.org/annotation/VAR_049717|||http://purl.uniprot.org/annotation/VAR_069320|||http://purl.uniprot.org/annotation/VAR_069321|||http://purl.uniprot.org/annotation/VAR_069925|||http://purl.uniprot.org/annotation/VAR_069926|||http://purl.uniprot.org/annotation/VAR_075395|||http://purl.uniprot.org/annotation/VAR_075865|||http://purl.uniprot.org/annotation/VAR_075866|||http://purl.uniprot.org/annotation/VSP_056008|||http://purl.uniprot.org/annotation/VSP_056009
http://togogenome.org/gene/9606:TBK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHD2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-466.|||Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-470.|||Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-466 and E-470.|||Abolishes phosphorylation and kinase activity.|||Abrogates both 'Lys-48'-linked and 'Lys-33'-linked ubiquitination.|||Almost abolishes interaction with TANK.|||Decreased kinase activity.|||Decreases interaction with TANK.|||Decreases kinase activity.|||Decreases kinase activity. No effect on phosphorylation.|||Decreases kinase activity. Reduced phosphorylation of STING1.|||Decreases phosphorylation and kinase activity.|||Decreases phosphorylation and kinase activity. Abolishes dimerization.|||Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with A-357 or R-448.|||Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with R-355.|||Decreases ubiquitination. Abolishes ubiquitination, phosphorylation and kinase activity; when associated with R-30.|||Decreases ubiquitination. Abolishes ubiquitination, phosphorylation and kinase activity; when associated with R-401.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In FTDALS4.|||In FTDALS4; loss of kinase activity.|||In FTDALS4; loss of kinase activity; impairs binding to OPTN.|||In FTDALS4; reduced kinase activity.|||In FTDALS4; unknown pathological significance.|||In IIAE8; decreased expression levels.|||In IIAE8; loss of kinase activity; loss of autophosphorylation at S-172; loss of IFNB induction.|||In IIAE8; unknown pathological significance.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||Interaction with AZI2, TANK and TBKBP1|||Loss of IFNB induction.|||Loss of kinase activity.|||Loss of kinase activity. No effect on dimerization. Loss of USP38-mediated degradation.|||No effect on IFNB induction.|||Phosphoserine|||Phosphoserine; by autocatalysis and IKKB|||Protein kinase|||Proton acceptor|||Reduced phosphorylation of STING1.|||Serine/threonine-protein kinase TBK1|||Strongly decreases interaction with AZI2, TANK and TBKBP1. No effect on phosphorylation.|||Strongly decreases interaction with TANK and TBKBP1. No effect on phosphorylation.|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086743|||http://purl.uniprot.org/annotation/VAR_024746|||http://purl.uniprot.org/annotation/VAR_024747|||http://purl.uniprot.org/annotation/VAR_041208|||http://purl.uniprot.org/annotation/VAR_041209|||http://purl.uniprot.org/annotation/VAR_041210|||http://purl.uniprot.org/annotation/VAR_041211|||http://purl.uniprot.org/annotation/VAR_041212|||http://purl.uniprot.org/annotation/VAR_069754|||http://purl.uniprot.org/annotation/VAR_069755|||http://purl.uniprot.org/annotation/VAR_073938|||http://purl.uniprot.org/annotation/VAR_073939|||http://purl.uniprot.org/annotation/VAR_073940|||http://purl.uniprot.org/annotation/VAR_073941|||http://purl.uniprot.org/annotation/VAR_073942|||http://purl.uniprot.org/annotation/VAR_073943|||http://purl.uniprot.org/annotation/VAR_073944|||http://purl.uniprot.org/annotation/VAR_073945|||http://purl.uniprot.org/annotation/VAR_073946|||http://purl.uniprot.org/annotation/VAR_073947|||http://purl.uniprot.org/annotation/VAR_073948|||http://purl.uniprot.org/annotation/VAR_080517|||http://purl.uniprot.org/annotation/VAR_080518|||http://purl.uniprot.org/annotation/VAR_080519|||http://purl.uniprot.org/annotation/VAR_084111|||http://purl.uniprot.org/annotation/VAR_084112|||http://purl.uniprot.org/annotation/VAR_084113|||http://purl.uniprot.org/annotation/VAR_084114|||http://purl.uniprot.org/annotation/VAR_084115|||http://purl.uniprot.org/annotation/VAR_084116|||http://purl.uniprot.org/annotation/VAR_084117|||http://purl.uniprot.org/annotation/VAR_084118|||http://purl.uniprot.org/annotation/VAR_084119|||http://purl.uniprot.org/annotation/VAR_084120|||http://purl.uniprot.org/annotation/VAR_084121
http://togogenome.org/gene/9606:MRGPRD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDS7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member D|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069756
http://togogenome.org/gene/9606:DPYSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK07|||http://purl.uniprot.org/uniprot/Q14195|||http://purl.uniprot.org/uniprot/Q6DEN2|||http://purl.uniprot.org/uniprot/Q8IXW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amidohydrolase-related|||Dihydropyrimidinase-related protein 3|||Disordered|||In isoform LCRMP-4.|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphoserine; by GSK3|||Phosphothreonine|||Phosphothreonine; by GSK3|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165917|||http://purl.uniprot.org/annotation/VAR_020485|||http://purl.uniprot.org/annotation/VSP_042546
http://togogenome.org/gene/9606:ZIC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9L1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||Zinc finger protein ZIC 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047253|||http://purl.uniprot.org/annotation/VSP_017066|||http://purl.uniprot.org/annotation/VSP_017067|||http://purl.uniprot.org/annotation/VSP_044484|||http://purl.uniprot.org/annotation/VSP_045529|||http://purl.uniprot.org/annotation/VSP_046072
http://togogenome.org/gene/9606:C10orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T681                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Phosphoserine|||Uncharacterized protein C10orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274241|||http://purl.uniprot.org/annotation/VAR_030216
http://togogenome.org/gene/9606:TSPAN32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QS1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Tetraspanin-32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219278|||http://purl.uniprot.org/annotation/VSP_003932|||http://purl.uniprot.org/annotation/VSP_003933|||http://purl.uniprot.org/annotation/VSP_003934|||http://purl.uniprot.org/annotation/VSP_003935|||http://purl.uniprot.org/annotation/VSP_003936|||http://purl.uniprot.org/annotation/VSP_003937|||http://purl.uniprot.org/annotation/VSP_003938
http://togogenome.org/gene/9606:CABP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP86                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Calcium-binding protein 5|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073524|||http://purl.uniprot.org/annotation/VAR_020020|||http://purl.uniprot.org/annotation/VAR_033695|||http://purl.uniprot.org/annotation/VAR_048633|||http://purl.uniprot.org/annotation/VAR_048634|||http://purl.uniprot.org/annotation/VAR_048635
http://togogenome.org/gene/9606:SEMA6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3T2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Sema|||Semaphorin-6C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032344|||http://purl.uniprot.org/annotation/VAR_028144|||http://purl.uniprot.org/annotation/VSP_006046|||http://purl.uniprot.org/annotation/VSP_006047
http://togogenome.org/gene/9606:CCDC190                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UF4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 190|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274498|||http://purl.uniprot.org/annotation/VSP_022772|||http://purl.uniprot.org/annotation/VSP_022773|||http://purl.uniprot.org/annotation/VSP_022774
http://togogenome.org/gene/9606:NAPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54920                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Alpha-soluble NSF attachment protein|||Does not affect interaction with GNA12.|||Increases interaction with GNA12.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219056
http://togogenome.org/gene/9606:HUS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60921                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Checkpoint protein HUS1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225003|||http://purl.uniprot.org/annotation/VAR_025414|||http://purl.uniprot.org/annotation/VAR_025415|||http://purl.uniprot.org/annotation/VAR_033999|||http://purl.uniprot.org/annotation/VSP_056702
http://togogenome.org/gene/9606:ZNF502                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBZ5|||http://purl.uniprot.org/uniprot/Q96K08                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 502                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047623|||http://purl.uniprot.org/annotation/VAR_024220|||http://purl.uniprot.org/annotation/VAR_033574|||http://purl.uniprot.org/annotation/VAR_061953
http://togogenome.org/gene/9606:GABRQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN88                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit theta|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000495|||http://purl.uniprot.org/annotation/VAR_030761|||http://purl.uniprot.org/annotation/VAR_030762
http://togogenome.org/gene/9606:GBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32455                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Abolished GDPase activity.|||Abolished GTPase activity.|||Abolished farnesylation and recruitment to the pathogen-containing vacuoles or vacuole-escaped bacteria. Impaired ability to promote pyroptosis in response to T.gondii infection.|||Abolished localization to pathogen-containing vacuoles.|||Constitutively dimeric. Localizes at vesicle-like structures at the plasma membrane.|||Cysteine methyl ester|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 1|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-567 and R-573.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-567 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-562, R-573 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-382, R-567, R-573 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-210, R-562, R-567, R-573 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-209, R-382, R-562, R-567, R-573 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207, R-210, R-382, R-562, R-567, R-573 and R-587.|||In 8KR mutant; abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-209, R-210, R-382, R-562, R-567, R-573 and R-587.|||Loss of GTPase activity. Constitutively monomeric. Expressed throughout the cytoplasm, loss of vesicular accumulation. Impaired ability to promote pyroptosis in response to T.gondii infection.|||Loss of association with membranes.|||Removed in mature form|||S-farnesyl cysteine|||Strongly decreased nucleotide-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190963|||http://purl.uniprot.org/annotation/PRO_0000396777|||http://purl.uniprot.org/annotation/VAR_014849|||http://purl.uniprot.org/annotation/VAR_033950|||http://purl.uniprot.org/annotation/VAR_033951|||http://purl.uniprot.org/annotation/VAR_046550
http://togogenome.org/gene/9606:TLX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31314                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2.|||N6-acetyllysine|||T-cell leukemia homeobox protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049333|||http://purl.uniprot.org/annotation/VSP_043068
http://togogenome.org/gene/9606:ACAD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H845                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Complex I assembly factor ACAD9, mitochondrial|||In MC1DN20.|||In MC1DN20; unknown pathological significance.|||Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000524|||http://purl.uniprot.org/annotation/VAR_033459|||http://purl.uniprot.org/annotation/VAR_071892|||http://purl.uniprot.org/annotation/VAR_071893|||http://purl.uniprot.org/annotation/VAR_071894|||http://purl.uniprot.org/annotation/VAR_071895|||http://purl.uniprot.org/annotation/VAR_071896|||http://purl.uniprot.org/annotation/VAR_071897|||http://purl.uniprot.org/annotation/VAR_071898|||http://purl.uniprot.org/annotation/VAR_071899|||http://purl.uniprot.org/annotation/VAR_071900|||http://purl.uniprot.org/annotation/VAR_071901|||http://purl.uniprot.org/annotation/VAR_071902|||http://purl.uniprot.org/annotation/VAR_071903|||http://purl.uniprot.org/annotation/VAR_071904|||http://purl.uniprot.org/annotation/VAR_071905|||http://purl.uniprot.org/annotation/VAR_076177|||http://purl.uniprot.org/annotation/VAR_076178|||http://purl.uniprot.org/annotation/VAR_076179
http://togogenome.org/gene/9606:DAZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ07|||http://purl.uniprot.org/uniprot/Q13117                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DAZ|||DAZ 1|||DAZ 10|||DAZ 11|||DAZ 12|||DAZ 13|||DAZ 14|||DAZ 15|||DAZ 2|||DAZ 3|||DAZ 4|||DAZ 5|||DAZ 6|||DAZ 7|||DAZ 8|||DAZ 9|||Deleted in azoospermia protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081555|||http://purl.uniprot.org/annotation/VSP_009452|||http://purl.uniprot.org/annotation/VSP_009453
http://togogenome.org/gene/9606:DNAH14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VDD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal heavy chain 14|||GPAGTGKT motif|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286560|||http://purl.uniprot.org/annotation/VAR_032116|||http://purl.uniprot.org/annotation/VAR_032117|||http://purl.uniprot.org/annotation/VAR_057764|||http://purl.uniprot.org/annotation/VSP_031314|||http://purl.uniprot.org/annotation/VSP_031315|||http://purl.uniprot.org/annotation/VSP_031316|||http://purl.uniprot.org/annotation/VSP_031317|||http://purl.uniprot.org/annotation/VSP_038241|||http://purl.uniprot.org/annotation/VSP_038242|||http://purl.uniprot.org/annotation/VSP_038243|||http://purl.uniprot.org/annotation/VSP_038244|||http://purl.uniprot.org/annotation/VSP_038245|||http://purl.uniprot.org/annotation/VSP_038246|||http://purl.uniprot.org/annotation/VSP_038247|||http://purl.uniprot.org/annotation/VSP_038248|||http://purl.uniprot.org/annotation/VSP_038249|||http://purl.uniprot.org/annotation/VSP_038250|||http://purl.uniprot.org/annotation/VSP_038251|||http://purl.uniprot.org/annotation/VSP_038252|||http://purl.uniprot.org/annotation/VSP_038253|||http://purl.uniprot.org/annotation/VSP_038254|||http://purl.uniprot.org/annotation/VSP_038255
http://togogenome.org/gene/9606:GSTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE2|||http://purl.uniprot.org/uniprot/A8K987|||http://purl.uniprot.org/uniprot/P09210                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GST C-terminal|||GST N-terminal|||Glutathione S-transferase A2|||N-acetylalanine|||N6-succinyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185784|||http://purl.uniprot.org/annotation/VAR_012205|||http://purl.uniprot.org/annotation/VAR_012206|||http://purl.uniprot.org/annotation/VAR_014495|||http://purl.uniprot.org/annotation/VAR_014496
http://togogenome.org/gene/9606:RHNO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Inhibits binding to the 9-1-1 complex. Does not inhibit interaction with TOPBP1. Inhibits localizion to sites of DNA damage.|||Polar residues|||RAD9, HUS1, RAD1-interacting nuclear orphan protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263105|||http://purl.uniprot.org/annotation/VSP_045307
http://togogenome.org/gene/9606:ITPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3W7|||http://purl.uniprot.org/uniprot/A0A0S2Z423|||http://purl.uniprot.org/uniprot/Q8WWI0|||http://purl.uniprot.org/uniprot/Q9BY32                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In DEE35; unknown pathological significance.|||In ITPAD; complete loss of enzymatic activity at homozygosity; partial loss of activity without ITP accumulation in heterozygous individuals.|||In isoform 2.|||In isoform 3.|||Inosine triphosphate pyrophosphatase|||N-acetylalanine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178280|||http://purl.uniprot.org/annotation/VAR_015576|||http://purl.uniprot.org/annotation/VAR_075084|||http://purl.uniprot.org/annotation/VSP_042548|||http://purl.uniprot.org/annotation/VSP_045545
http://togogenome.org/gene/9606:CCDC71L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9Z2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Coiled-coil domain-containing protein 71L|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334673|||http://purl.uniprot.org/annotation/VSP_033753
http://togogenome.org/gene/9606:NDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Nucleoporin NDC1|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235240|||http://purl.uniprot.org/annotation/VAR_026388|||http://purl.uniprot.org/annotation/VSP_018396|||http://purl.uniprot.org/annotation/VSP_018397|||http://purl.uniprot.org/annotation/VSP_018398|||http://purl.uniprot.org/annotation/VSP_018399|||http://purl.uniprot.org/annotation/VSP_055331|||http://purl.uniprot.org/annotation/VSP_055332
http://togogenome.org/gene/9606:PTK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05397|||http://purl.uniprot.org/uniprot/Q59GM6|||http://purl.uniprot.org/uniprot/Q59GN8|||http://purl.uniprot.org/uniprot/Q658W2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation. Abolishes interaction with SRC and activation of BMX. Reduces phosphorylation of NEDD9.|||Disordered|||FERM|||Focal adhesion kinase 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In a glioblastoma multiforme sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with ARHGEF28|||Interaction with TGFB1I1|||Loss of interaction with TGFB1I1.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by RET and SRC|||Phosphotyrosine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088077|||http://purl.uniprot.org/annotation/VAR_041682|||http://purl.uniprot.org/annotation/VAR_041683|||http://purl.uniprot.org/annotation/VAR_041684|||http://purl.uniprot.org/annotation/VAR_041685|||http://purl.uniprot.org/annotation/VAR_041686|||http://purl.uniprot.org/annotation/VSP_004967|||http://purl.uniprot.org/annotation/VSP_004968|||http://purl.uniprot.org/annotation/VSP_004969|||http://purl.uniprot.org/annotation/VSP_004970|||http://purl.uniprot.org/annotation/VSP_004971|||http://purl.uniprot.org/annotation/VSP_004972|||http://purl.uniprot.org/annotation/VSP_004973|||http://purl.uniprot.org/annotation/VSP_004974|||http://purl.uniprot.org/annotation/VSP_042168|||http://purl.uniprot.org/annotation/VSP_042169|||http://purl.uniprot.org/annotation/VSP_042170|||http://purl.uniprot.org/annotation/VSP_057268
http://togogenome.org/gene/9606:SEZ6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLJ8|||http://purl.uniprot.org/uniprot/Q9BYH1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||CUB 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1 and isoform 2.|||In isoform 1.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 7.|||In isoform 3.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) serine|||Polar residues|||Seizure 6-like protein|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022323|||http://purl.uniprot.org/annotation/PRO_5014300199|||http://purl.uniprot.org/annotation/VAR_020330|||http://purl.uniprot.org/annotation/VAR_024348|||http://purl.uniprot.org/annotation/VAR_043338|||http://purl.uniprot.org/annotation/VAR_043339|||http://purl.uniprot.org/annotation/VSP_003976|||http://purl.uniprot.org/annotation/VSP_003977|||http://purl.uniprot.org/annotation/VSP_003978|||http://purl.uniprot.org/annotation/VSP_003979|||http://purl.uniprot.org/annotation/VSP_003980|||http://purl.uniprot.org/annotation/VSP_003981|||http://purl.uniprot.org/annotation/VSP_013022
http://togogenome.org/gene/9606:ZNF799                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3YTF2|||http://purl.uniprot.org/uniprot/Q96GE5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 799                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271017|||http://purl.uniprot.org/annotation/VAR_029846|||http://purl.uniprot.org/annotation/VAR_029847|||http://purl.uniprot.org/annotation/VSP_039164
http://togogenome.org/gene/9606:CHRNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32297                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||In BAIPRCK; loss-of-function variant affecting ion transmembrane transport in response to acetylcholine; does not localize to plasma membrane.|||In isoform 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000346|||http://purl.uniprot.org/annotation/VAR_013240|||http://purl.uniprot.org/annotation/VAR_059110|||http://purl.uniprot.org/annotation/VAR_083543|||http://purl.uniprot.org/annotation/VSP_037750|||http://purl.uniprot.org/annotation/VSP_037751
http://togogenome.org/gene/9606:TMX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y320                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Di-lysine motif|||Disordered|||Extracellular|||Helical|||In NEDMCMS.|||In NEDMCMS; increased homodimerization; even in absence of oxidative stress.|||In NEDMCMS; may affect splicing; decreased protein abundance; homozygous patient cells show decreased mitochondrial respiratory reserve capacity and compensatory increased glycolytic activity.|||In NEDMCMS; unknown pathological significance.|||In isoform 2.|||Increased homodimerization even in absence of oxidative stress.|||Phosphoserine|||Thioredoxin|||Thioredoxin-related transmembrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315752|||http://purl.uniprot.org/annotation/VAR_083593|||http://purl.uniprot.org/annotation/VAR_083594|||http://purl.uniprot.org/annotation/VAR_083595|||http://purl.uniprot.org/annotation/VAR_083596|||http://purl.uniprot.org/annotation/VAR_083597|||http://purl.uniprot.org/annotation/VAR_083598|||http://purl.uniprot.org/annotation/VAR_083599|||http://purl.uniprot.org/annotation/VAR_083600|||http://purl.uniprot.org/annotation/VAR_083601|||http://purl.uniprot.org/annotation/VAR_083602|||http://purl.uniprot.org/annotation/VSP_030696
http://togogenome.org/gene/9606:EIF3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00303                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 3 subunit F|||In MRT67; decreased protein abundance.|||MPN|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK11; in vitro|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213964|||http://purl.uniprot.org/annotation/VAR_014452|||http://purl.uniprot.org/annotation/VAR_029267|||http://purl.uniprot.org/annotation/VAR_081783
http://togogenome.org/gene/9606:PEAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H792                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  50% reduction in interaction with GRB2. No effect on interaction with SHC1.|||Acidic residues|||Basic and acidic residues|||Disordered|||Disrupts homodimerization.|||Fails to bind SHC1. Reduced recruitment of SHC1 to focal adhesions. Slightly reduces interaction with GRB2. Does not affect interaction with RASAL2. Does not affect association with integrin ITGB1.|||Impairs interaction with tensin TNS3 and association with integrin ITGB1. 50% reduction in interaction with GRB2. No effect on interaction with unphosphorylated SHC1 but reduces interaction with tyrosine-phosphorylated SHC1. Reduces focal adhesion localization. Reduces cell migration.|||In a bladder carcinoma NOS sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Inactive tyrosine-protein kinase PEAK1|||No effect on focal adhesion subcellular localization. Does not affect colocalization with F-actin.|||No effect on interaction with PRAG1.|||No effect on localization with actin. Decreases localization in focal adhesion. Fails to regulate focal adhesion dynamics. Decreases cell migration.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Required for homodimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250589|||http://purl.uniprot.org/annotation/VAR_041817|||http://purl.uniprot.org/annotation/VAR_041818|||http://purl.uniprot.org/annotation/VAR_041819|||http://purl.uniprot.org/annotation/VAR_041820|||http://purl.uniprot.org/annotation/VAR_041821|||http://purl.uniprot.org/annotation/VAR_041822|||http://purl.uniprot.org/annotation/VAR_041823|||http://purl.uniprot.org/annotation/VAR_041824|||http://purl.uniprot.org/annotation/VAR_041825|||http://purl.uniprot.org/annotation/VAR_041826|||http://purl.uniprot.org/annotation/VAR_041827|||http://purl.uniprot.org/annotation/VAR_041828|||http://purl.uniprot.org/annotation/VAR_041829
http://togogenome.org/gene/9606:MAGOHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A72                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||N-acetylalanine|||Protein mago nashi homolog 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174146|||http://purl.uniprot.org/annotation/VAR_036431
http://togogenome.org/gene/9606:SAMM50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y512                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||N6-methyllysine|||POTRA|||Sorting and assembly machinery component 50 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215939|||http://purl.uniprot.org/annotation/VAR_013768|||http://purl.uniprot.org/annotation/VAR_057338
http://togogenome.org/gene/9606:NKPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7N4I390                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||KAP NTPase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RNF103-CHMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3E7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; N-56 and E-59.|||Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169.|||Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169.|||Abolishes interaction with VPS4A and STAMBP.|||Charged multivesicular body protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs HIV-1 release; when associated with 24-S-A-25.|||Impairs HIV-1 release; when associated with S-28.|||Impairs interaction with VPS4A and STAMBP.|||Important for autoinhibitory function|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62.|||Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48.|||Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169.|||Interaction with STAMBP|||Interaction with VPS4A|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||MIT-interacting motif|||Membrane association; releases autoinhibition.|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211479|||http://purl.uniprot.org/annotation/VSP_041076|||http://purl.uniprot.org/annotation/VSP_042124|||http://purl.uniprot.org/annotation/VSP_042125
http://togogenome.org/gene/9606:CCDC9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 9B|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295733|||http://purl.uniprot.org/annotation/VAR_035620|||http://purl.uniprot.org/annotation/VSP_027037|||http://purl.uniprot.org/annotation/VSP_027038|||http://purl.uniprot.org/annotation/VSP_027039|||http://purl.uniprot.org/annotation/VSP_027040|||http://purl.uniprot.org/annotation/VSP_027041|||http://purl.uniprot.org/annotation/VSP_027042
http://togogenome.org/gene/9606:C15orf40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUR7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||UPF0235 protein C15orf40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139475|||http://purl.uniprot.org/annotation/VAR_069397|||http://purl.uniprot.org/annotation/VSP_046500|||http://purl.uniprot.org/annotation/VSP_046501
http://togogenome.org/gene/9606:PRKCI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41743                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes activity.|||Disordered|||In a metastatic melanoma sample; somatic mutation.|||Interaction with PARD6A|||Loss of interaction with ECT2, PARD6A and with SQSTM1.|||N-acetylproline|||No effect on activity.|||No effect on interaction with SQSTM1.|||No effect on the SRC-mediated phosphorylation state. No effect on SRC-induced enzyme activity. Little effect on TRAF6-mediated activation of NF-kappa-B. Decreased binding to KPNB1/importin-beta.|||No effect on the SRC-mediated phosphorylation state. No effect on SRC-induced enzyme activity. No effect on TRAF6-mediated activation of NF-kappa-B.|||No effect on the SRC-mediated phosphorylation state. Significant reduction of SRC-induced enzyme activity. Greatly reduced TRAF6-mediated activation of NF-kappa-B. Reduces NGF-dependent cell survival.|||PB1|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphotyrosine; by SRC|||Polar residues|||Protein kinase|||Protein kinase C iota type|||Proton acceptor|||Pseudosubstrate|||Regulatory domain|||Removed|||Required for interaction with RAB2|||Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-85.|||Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-91.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055710|||http://purl.uniprot.org/annotation/VAR_042322|||http://purl.uniprot.org/annotation/VAR_042323
http://togogenome.org/gene/9606:MYBPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM48|||http://purl.uniprot.org/uniprot/Q14896                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In CMD1MM.|||In CMH4 and CMD1MM.|||In CMH4, CMD1MM and LVNC10.|||In CMH4.|||In CMH4; also found in a patient with RCM; decreases protein abundance; increases polyubiquitination level; accelerates the degradation process; no effect on phosphorylation; decreases endopeptidase activity; increases apoptotic process.|||In CMH4; benign variant.|||In CMH4; destabilizes the structure of Ig-like C2-type domain 5.|||In CMH4; no effect on protein abundance; no effect on endopeptidase activity.|||In CMH4; unknown pathological significance.|||In CMH4; unknown pathological significance; as well folded and stable as the wild-type.|||In LVNC10.|||In isoform 2.|||May act as a phenotype modifier in cardiomyopathy patients.|||Myosin-binding protein C, cardiac-type|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKA and PKC|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072693|||http://purl.uniprot.org/annotation/VAR_003917|||http://purl.uniprot.org/annotation/VAR_003918|||http://purl.uniprot.org/annotation/VAR_003919|||http://purl.uniprot.org/annotation/VAR_019889|||http://purl.uniprot.org/annotation/VAR_019890|||http://purl.uniprot.org/annotation/VAR_019891|||http://purl.uniprot.org/annotation/VAR_019892|||http://purl.uniprot.org/annotation/VAR_019893|||http://purl.uniprot.org/annotation/VAR_019894|||http://purl.uniprot.org/annotation/VAR_019895|||http://purl.uniprot.org/annotation/VAR_019896|||http://purl.uniprot.org/annotation/VAR_019897|||http://purl.uniprot.org/annotation/VAR_019898|||http://purl.uniprot.org/annotation/VAR_019899|||http://purl.uniprot.org/annotation/VAR_019900|||http://purl.uniprot.org/annotation/VAR_019901|||http://purl.uniprot.org/annotation/VAR_020085|||http://purl.uniprot.org/annotation/VAR_020086|||http://purl.uniprot.org/annotation/VAR_020568|||http://purl.uniprot.org/annotation/VAR_020569|||http://purl.uniprot.org/annotation/VAR_020570|||http://purl.uniprot.org/annotation/VAR_020571|||http://purl.uniprot.org/annotation/VAR_020573|||http://purl.uniprot.org/annotation/VAR_020574|||http://purl.uniprot.org/annotation/VAR_020575|||http://purl.uniprot.org/annotation/VAR_027879|||http://purl.uniprot.org/annotation/VAR_027880|||http://purl.uniprot.org/annotation/VAR_027881|||http://purl.uniprot.org/annotation/VAR_029390|||http://purl.uniprot.org/annotation/VAR_029391|||http://purl.uniprot.org/annotation/VAR_029392|||http://purl.uniprot.org/annotation/VAR_029393|||http://purl.uniprot.org/annotation/VAR_029394|||http://purl.uniprot.org/annotation/VAR_029395|||http://purl.uniprot.org/annotation/VAR_029396|||http://purl.uniprot.org/annotation/VAR_029397|||http://purl.uniprot.org/annotation/VAR_029398|||http://purl.uniprot.org/annotation/VAR_029399|||http://purl.uniprot.org/annotation/VAR_029400|||http://purl.uniprot.org/annotation/VAR_029401|||http://purl.uniprot.org/annotation/VAR_029402|||http://purl.uniprot.org/annotation/VAR_029403|||http://purl.uniprot.org/annotation/VAR_029404|||http://purl.uniprot.org/annotation/VAR_029405|||http://purl.uniprot.org/annotation/VAR_029406|||http://purl.uniprot.org/annotation/VAR_029407|||http://purl.uniprot.org/annotation/VAR_029408|||http://purl.uniprot.org/annotation/VAR_029409|||http://purl.uniprot.org/annotation/VAR_029410|||http://purl.uniprot.org/annotation/VAR_029411|||http://purl.uniprot.org/annotation/VAR_029412|||http://purl.uniprot.org/annotation/VAR_029413|||http://purl.uniprot.org/annotation/VAR_029414|||http://purl.uniprot.org/annotation/VAR_029415|||http://purl.uniprot.org/annotation/VAR_029416|||http://purl.uniprot.org/annotation/VAR_029417|||http://purl.uniprot.org/annotation/VAR_029418|||http://purl.uniprot.org/annotation/VAR_029419|||http://purl.uniprot.org/annotation/VAR_029420|||http://purl.uniprot.org/annotation/VAR_029421|||http://purl.uniprot.org/annotation/VAR_029422|||http://purl.uniprot.org/annotation/VAR_029423|||http://purl.uniprot.org/annotation/VAR_029424|||http://purl.uniprot.org/annotation/VAR_029425|||http://purl.uniprot.org/annotation/VAR_029426|||http://purl.uniprot.org/annotation/VAR_029427|||http://purl.uniprot.org/annotation/VAR_029428|||http://purl.uniprot.org/annotation/VAR_029429|||http://purl.uniprot.org/annotation/VAR_042740|||http://purl.uniprot.org/annotation/VAR_042741|||http://purl.uniprot.org/annotation/VAR_042742|||http://purl.uniprot.org/annotation/VAR_042743|||http://purl.uniprot.org/annotation/VAR_042744|||http://purl.uniprot.org/annotation/VAR_045929|||http://purl.uniprot.org/annotation/VAR_045930|||http://purl.uniprot.org/annotation/VAR_045931|||http://purl.uniprot.org/annotation/VAR_070449|||http://purl.uniprot.org/annotation/VAR_070450|||http://purl.uniprot.org/annotation/VAR_070451|||http://purl.uniprot.org/annotation/VAR_070452|||http://purl.uniprot.org/annotation/VAR_070453|||http://purl.uniprot.org/annotation/VAR_070454|||http://purl.uniprot.org/annotation/VAR_070455|||http://purl.uniprot.org/annotation/VAR_074538|||http://purl.uniprot.org/annotation/VAR_074539|||http://purl.uniprot.org/annotation/VAR_074540|||http://purl.uniprot.org/annotation/VAR_074541|||http://purl.uniprot.org/annotation/VAR_074542|||http://purl.uniprot.org/annotation/VAR_074543|||http://purl.uniprot.org/annotation/VAR_074544|||http://purl.uniprot.org/annotation/VAR_074545|||http://purl.uniprot.org/annotation/VAR_079521|||http://purl.uniprot.org/annotation/VSP_047141
http://togogenome.org/gene/9606:USPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1B1|||http://purl.uniprot.org/uniprot/B3KQ64|||http://purl.uniprot.org/uniprot/Q5W0Q7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the SUMO-specific isopeptidase activity.|||Altered SUMO-binding and SUMO-specific isopeptidase activity.|||Disordered|||In isoform 2.|||Loss of SUMO-binding and catalytic activity.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||SUMO-binding|||SUMO-specific isopeptidase USPL1|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279526|||http://purl.uniprot.org/annotation/VAR_030916|||http://purl.uniprot.org/annotation/VAR_030917|||http://purl.uniprot.org/annotation/VAR_030918|||http://purl.uniprot.org/annotation/VAR_030919|||http://purl.uniprot.org/annotation/VAR_030920|||http://purl.uniprot.org/annotation/VAR_030921|||http://purl.uniprot.org/annotation/VAR_030922|||http://purl.uniprot.org/annotation/VAR_051542|||http://purl.uniprot.org/annotation/VAR_051543|||http://purl.uniprot.org/annotation/VSP_023479
http://togogenome.org/gene/9606:ATG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0Y0                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl thioester intermediate|||In isoform 2.|||Ubiquitin-like-conjugating enzyme ATG10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096183|||http://purl.uniprot.org/annotation/VAR_021562|||http://purl.uniprot.org/annotation/VAR_021563|||http://purl.uniprot.org/annotation/VAR_024370|||http://purl.uniprot.org/annotation/VSP_013272|||http://purl.uniprot.org/annotation/VSP_013273
http://togogenome.org/gene/9606:SLCO1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46721                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In a colorectal cancer sample; somatic mutation.|||In isoform OATP1b.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191042|||http://purl.uniprot.org/annotation/VAR_020289|||http://purl.uniprot.org/annotation/VAR_020290|||http://purl.uniprot.org/annotation/VAR_020291|||http://purl.uniprot.org/annotation/VAR_020292|||http://purl.uniprot.org/annotation/VAR_020293|||http://purl.uniprot.org/annotation/VAR_024644|||http://purl.uniprot.org/annotation/VAR_036409|||http://purl.uniprot.org/annotation/VAR_036823|||http://purl.uniprot.org/annotation/VSP_006130|||http://purl.uniprot.org/annotation/VSP_006131|||http://purl.uniprot.org/annotation/VSP_006132
http://togogenome.org/gene/9606:CDKL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG1|||http://purl.uniprot.org/uniprot/B4DH08|||http://purl.uniprot.org/uniprot/J3KNE8|||http://purl.uniprot.org/uniprot/Q92772                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase-like 2|||Disordered|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian papillary serous adenocarcinoma sample; somatic mutation.|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085814|||http://purl.uniprot.org/annotation/VAR_041987|||http://purl.uniprot.org/annotation/VAR_041988|||http://purl.uniprot.org/annotation/VAR_041989|||http://purl.uniprot.org/annotation/VAR_041990|||http://purl.uniprot.org/annotation/VAR_053928|||http://purl.uniprot.org/annotation/VAR_053929
http://togogenome.org/gene/9606:MYLK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y4U5|||http://purl.uniprot.org/uniprot/A0A8V8TMV3|||http://purl.uniprot.org/uniprot/Q86YV6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||Myosin light chain kinase family member 4|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261030|||http://purl.uniprot.org/annotation/VAR_040864|||http://purl.uniprot.org/annotation/VAR_040865|||http://purl.uniprot.org/annotation/VAR_040866|||http://purl.uniprot.org/annotation/VAR_040867|||http://purl.uniprot.org/annotation/VAR_040868|||http://purl.uniprot.org/annotation/VAR_040869|||http://purl.uniprot.org/annotation/VAR_040870|||http://purl.uniprot.org/annotation/VAR_051650|||http://purl.uniprot.org/annotation/VSP_026948
http://togogenome.org/gene/9606:HRH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2KJ49|||http://purl.uniprot.org/uniprot/Q9H3N8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Histamine H4 receptor|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069693|||http://purl.uniprot.org/annotation/VAR_033477|||http://purl.uniprot.org/annotation/VAR_033478|||http://purl.uniprot.org/annotation/VSP_042737
http://togogenome.org/gene/9606:WDR47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94967                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CTLH|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||LisH|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051397|||http://purl.uniprot.org/annotation/VSP_012093|||http://purl.uniprot.org/annotation/VSP_035045|||http://purl.uniprot.org/annotation/VSP_046727
http://togogenome.org/gene/9606:GJA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6H8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||INTRAMEM|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes formation of gap junctions. No significant effect on formation of functional hemichannels.|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-3 protein|||Helical|||In CTRCT14.|||In CTRCT14; autosomal dominant congenital/infantile 'ant-egg' cataract.|||In CTRCT14; central nuclear cataract with punctate opacities.|||In CTRCT14; nearly abolishes formation of gap junctions; no significant effect on formation of functional hemichannels.|||In CTRCT14; nearly abolishes formation of gap junctions; no significant effect on formation of functional hemichannels; not fully penetrant mutation.|||In CTRCT14; nuclear cataract.|||In CTRCT14; nuclear progressive cataract.|||In CTRCT14; nuclear pulverulent and posterior polar cataract; the mutant affects the formation of gap junction plaques; affects hemichannel permeability.|||In CTRCT14; nuclear pulverulent cataract.|||In CTRCT14; nuclear punctate cataract.|||In CTRCT14; pearl box cataract.|||In CTRCT14; unknown pathological significance.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057810|||http://purl.uniprot.org/annotation/VAR_009158|||http://purl.uniprot.org/annotation/VAR_022426|||http://purl.uniprot.org/annotation/VAR_023447|||http://purl.uniprot.org/annotation/VAR_030020|||http://purl.uniprot.org/annotation/VAR_030021|||http://purl.uniprot.org/annotation/VAR_030022|||http://purl.uniprot.org/annotation/VAR_030023|||http://purl.uniprot.org/annotation/VAR_038796|||http://purl.uniprot.org/annotation/VAR_066710|||http://purl.uniprot.org/annotation/VAR_066711|||http://purl.uniprot.org/annotation/VAR_066712|||http://purl.uniprot.org/annotation/VAR_066713|||http://purl.uniprot.org/annotation/VAR_066714|||http://purl.uniprot.org/annotation/VAR_066715|||http://purl.uniprot.org/annotation/VAR_066716|||http://purl.uniprot.org/annotation/VAR_066717|||http://purl.uniprot.org/annotation/VAR_066718|||http://purl.uniprot.org/annotation/VAR_066719|||http://purl.uniprot.org/annotation/VAR_072762|||http://purl.uniprot.org/annotation/VAR_072763|||http://purl.uniprot.org/annotation/VAR_075211|||http://purl.uniprot.org/annotation/VAR_084808|||http://purl.uniprot.org/annotation/VAR_084809
http://togogenome.org/gene/9606:FCGR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISU3|||http://purl.uniprot.org/uniprot/O75015                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane                                                                                  ^@                                                                                  Abolishes membrane anchoring via glycosylphosphatidylinositol.|||GPI-anchor amidated serine|||Has no effect on membrane anchoring via glycosylphosphatidylinositol.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In allele FCGR3B*01.|||In allele SH.|||Low affinity immunoglobulin gamma Fc region receptor III-B|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015151|||http://purl.uniprot.org/annotation/PRO_0000015152|||http://purl.uniprot.org/annotation/PRO_5017302676|||http://purl.uniprot.org/annotation/VAR_003956|||http://purl.uniprot.org/annotation/VAR_003957|||http://purl.uniprot.org/annotation/VAR_003963|||http://purl.uniprot.org/annotation/VAR_003964|||http://purl.uniprot.org/annotation/VAR_008802
http://togogenome.org/gene/9606:KBTBD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1K0|||http://purl.uniprot.org/uniprot/G3V161|||http://purl.uniprot.org/uniprot/Q8NAB2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119078|||http://purl.uniprot.org/annotation/VAR_056124
http://togogenome.org/gene/9606:ETFRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPR1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Electron transfer flavoprotein regulatory factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251182
http://togogenome.org/gene/9606:ZNF506                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JVG8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||KRAB|||Zinc finger protein 506                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047624|||http://purl.uniprot.org/annotation/VAR_057421|||http://purl.uniprot.org/annotation/VSP_040653
http://togogenome.org/gene/9606:ATRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4LAA3|||http://purl.uniprot.org/uniprot/B4DLW1|||http://purl.uniprot.org/uniprot/P46100                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADD|||Abolishes ATPAse activity, no effect on pericentromeric heterochromatin localization.|||Acidic residues|||Basic and acidic residues|||Basic residues|||DEGH box|||Disordered|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci.|||Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci.|||Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3).|||Impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization.|||Impairs interaction with histone H3 peptides unmethylated at 'Lys-5' (H3K4me0); reduces pericentromeric localization.|||In ATRX.|||In ATRX; atypical; patients presents spastic paraplegia at birth.|||In ATRX; greatly impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci.|||In ATRX; impairs ATPase activity.|||In ATRX; impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci.|||In ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3) and reduces localization to pericentromeric heterochromatin foci.|||In ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3).|||In ATRX; impairs interaction with histone H3 peptides trimethylated at 'Lys-10' (H3K9me3); loss of heterochromatic localization.|||In ATRX; unknown pathological significance.|||In ATRX; without alpha-thalassemia.|||In MRXHF1 and ATRX; originally reported as Juberg-Marsidi syndrome.|||In MRXHF1.|||In MRXHF1; originally reported as Carpenter-Waziri syndrome.|||In isoform 1.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 6.|||Interaction with DAXX|||Interaction with MECP2|||N6-acetyllysine|||Omega-N-methylarginine|||PHD-type|||PHD-type; atypical|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||PxVxL motif|||Transcriptional regulator ATRX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074301|||http://purl.uniprot.org/annotation/VAR_001226|||http://purl.uniprot.org/annotation/VAR_001227|||http://purl.uniprot.org/annotation/VAR_001228|||http://purl.uniprot.org/annotation/VAR_001229|||http://purl.uniprot.org/annotation/VAR_001230|||http://purl.uniprot.org/annotation/VAR_001231|||http://purl.uniprot.org/annotation/VAR_001232|||http://purl.uniprot.org/annotation/VAR_001233|||http://purl.uniprot.org/annotation/VAR_001234|||http://purl.uniprot.org/annotation/VAR_001235|||http://purl.uniprot.org/annotation/VAR_001236|||http://purl.uniprot.org/annotation/VAR_001237|||http://purl.uniprot.org/annotation/VAR_001238|||http://purl.uniprot.org/annotation/VAR_001239|||http://purl.uniprot.org/annotation/VAR_001240|||http://purl.uniprot.org/annotation/VAR_001241|||http://purl.uniprot.org/annotation/VAR_010914|||http://purl.uniprot.org/annotation/VAR_012113|||http://purl.uniprot.org/annotation/VAR_012114|||http://purl.uniprot.org/annotation/VAR_012115|||http://purl.uniprot.org/annotation/VAR_012116|||http://purl.uniprot.org/annotation/VAR_012117|||http://purl.uniprot.org/annotation/VAR_012118|||http://purl.uniprot.org/annotation/VAR_012119|||http://purl.uniprot.org/annotation/VAR_012120|||http://purl.uniprot.org/annotation/VAR_012121|||http://purl.uniprot.org/annotation/VAR_012122|||http://purl.uniprot.org/annotation/VAR_012123|||http://purl.uniprot.org/annotation/VAR_012124|||http://purl.uniprot.org/annotation/VAR_012125|||http://purl.uniprot.org/annotation/VAR_012126|||http://purl.uniprot.org/annotation/VAR_012127|||http://purl.uniprot.org/annotation/VAR_016914|||http://purl.uniprot.org/annotation/VAR_016915|||http://purl.uniprot.org/annotation/VAR_016916|||http://purl.uniprot.org/annotation/VAR_023438|||http://purl.uniprot.org/annotation/VAR_032625|||http://purl.uniprot.org/annotation/VAR_032626|||http://purl.uniprot.org/annotation/VAR_032627|||http://purl.uniprot.org/annotation/VAR_055939|||http://purl.uniprot.org/annotation/VSP_000574|||http://purl.uniprot.org/annotation/VSP_000575|||http://purl.uniprot.org/annotation/VSP_000576|||http://purl.uniprot.org/annotation/VSP_015499|||http://purl.uniprot.org/annotation/VSP_015500|||http://purl.uniprot.org/annotation/VSP_015501
http://togogenome.org/gene/9606:RPLP0                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05388                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Large ribosomal subunit protein uL10|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154758|||http://purl.uniprot.org/annotation/VSP_055867
http://togogenome.org/gene/9606:AANAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0I5|||http://purl.uniprot.org/uniprot/Q16613                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in individuals with delayed sleep phase syndrome; has higher frequency in affected individuals than in healthy controls; unknown pathological significance.|||Important for the catalytic mechanism; involved in substrate deprotonation|||In isoform 2.|||Loss of activation by cAMP.|||N-acetyltransferase|||Phosphoserine|||Phosphothreonine; by PKA|||Serotonin N-acetyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074580|||http://purl.uniprot.org/annotation/VAR_048168|||http://purl.uniprot.org/annotation/VAR_055086|||http://purl.uniprot.org/annotation/VSP_054108
http://togogenome.org/gene/9606:OCRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0TVZ9|||http://purl.uniprot.org/uniprot/Q01968|||http://purl.uniprot.org/uniprot/Q504W7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-phosphatase|||ASH|||Clathrin box 1|||Clathrin box 2|||Disordered|||Does not affect interaction with RAB8A.|||Does not interact with RAB8A. Does not localize to cilia.|||In DENT2 and OCRL.|||In DENT2.|||In OCRL.|||In OCRL; associated with C-337.|||In OCRL; associated with I-361.|||In OCRL; uncertain pathological significance.|||In OCRL; uncertain pathological significance; abolishes FAM109A-, FAM109B- and APPL1-binding.|||In isoform B.|||Inositol polyphosphate 5-phosphatase OCRL|||PH|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209721|||http://purl.uniprot.org/annotation/VAR_010169|||http://purl.uniprot.org/annotation/VAR_010170|||http://purl.uniprot.org/annotation/VAR_010171|||http://purl.uniprot.org/annotation/VAR_010172|||http://purl.uniprot.org/annotation/VAR_010173|||http://purl.uniprot.org/annotation/VAR_010174|||http://purl.uniprot.org/annotation/VAR_010175|||http://purl.uniprot.org/annotation/VAR_010176|||http://purl.uniprot.org/annotation/VAR_010177|||http://purl.uniprot.org/annotation/VAR_010178|||http://purl.uniprot.org/annotation/VAR_010179|||http://purl.uniprot.org/annotation/VAR_010180|||http://purl.uniprot.org/annotation/VAR_010181|||http://purl.uniprot.org/annotation/VAR_010182|||http://purl.uniprot.org/annotation/VAR_010183|||http://purl.uniprot.org/annotation/VAR_010184|||http://purl.uniprot.org/annotation/VAR_010185|||http://purl.uniprot.org/annotation/VAR_010187|||http://purl.uniprot.org/annotation/VAR_010188|||http://purl.uniprot.org/annotation/VAR_010189|||http://purl.uniprot.org/annotation/VAR_022698|||http://purl.uniprot.org/annotation/VAR_022699|||http://purl.uniprot.org/annotation/VAR_023957|||http://purl.uniprot.org/annotation/VAR_023958|||http://purl.uniprot.org/annotation/VAR_064773|||http://purl.uniprot.org/annotation/VAR_064774|||http://purl.uniprot.org/annotation/VAR_064775|||http://purl.uniprot.org/annotation/VAR_064776|||http://purl.uniprot.org/annotation/VAR_064777|||http://purl.uniprot.org/annotation/VAR_064778|||http://purl.uniprot.org/annotation/VAR_064779|||http://purl.uniprot.org/annotation/VAR_064780|||http://purl.uniprot.org/annotation/VAR_064781|||http://purl.uniprot.org/annotation/VAR_064782|||http://purl.uniprot.org/annotation/VAR_064783|||http://purl.uniprot.org/annotation/VAR_064784|||http://purl.uniprot.org/annotation/VAR_064785|||http://purl.uniprot.org/annotation/VAR_064786|||http://purl.uniprot.org/annotation/VAR_064787|||http://purl.uniprot.org/annotation/VAR_064788|||http://purl.uniprot.org/annotation/VAR_064789|||http://purl.uniprot.org/annotation/VAR_064790|||http://purl.uniprot.org/annotation/VAR_064791|||http://purl.uniprot.org/annotation/VAR_064792|||http://purl.uniprot.org/annotation/VAR_064793|||http://purl.uniprot.org/annotation/VAR_064794|||http://purl.uniprot.org/annotation/VSP_002681
http://togogenome.org/gene/9606:KIF3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHG8|||http://purl.uniprot.org/uniprot/E9PES4|||http://purl.uniprot.org/uniprot/J3KPF9|||http://purl.uniprot.org/uniprot/Q05CT3|||http://purl.uniprot.org/uniprot/Q9Y496                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Globular|||Kinesin motor|||Kinesin-like protein KIF3A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125393|||http://purl.uniprot.org/annotation/VAR_055319
http://togogenome.org/gene/9606:MTARC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT66                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||MOSC|||MOSC N-terminal region|||Mitochondrial amidoxime-reducing component 1|||Mitochondrial matrix|||N-myristoyl glycine|||No effect on binding of the molybdenum cofactor; no significant effect on catalytic efficiency toward benzamidoxime; no significant effect on affinity for benzamidoxime.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273335|||http://purl.uniprot.org/annotation/VAR_030129|||http://purl.uniprot.org/annotation/VAR_030130|||http://purl.uniprot.org/annotation/VAR_030131|||http://purl.uniprot.org/annotation/VAR_030132|||http://purl.uniprot.org/annotation/VAR_056941|||http://purl.uniprot.org/annotation/VAR_062273|||http://purl.uniprot.org/annotation/VAR_062274|||http://purl.uniprot.org/annotation/VSP_022511|||http://purl.uniprot.org/annotation/VSP_022512
http://togogenome.org/gene/9606:MKRN2OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BPM6                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  MKRN2 opposite strand protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421254
http://togogenome.org/gene/9606:ST18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60284                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHHC-type 1|||CCHHC-type 2|||CCHHC-type 3|||CCHHC-type 4|||CCHHC-type 5|||CCHHC-type 6|||Disordered|||Polar residues|||Suppression of tumorigenicity 18 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234030|||http://purl.uniprot.org/annotation/VAR_052732
http://togogenome.org/gene/9606:RANBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7F3|||http://purl.uniprot.org/uniprot/Q53GE1|||http://purl.uniprot.org/uniprot/Q9H6Z4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ran-binding protein 3|||RanBD1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097165|||http://purl.uniprot.org/annotation/VAR_051303|||http://purl.uniprot.org/annotation/VSP_011162|||http://purl.uniprot.org/annotation/VSP_011163
http://togogenome.org/gene/9606:APRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07741                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Adenine phosphoribosyltransferase|||In APRTD.|||In APRTD; Icelandic type.|||In APRTD; Japanese type; allele APRT*J; most common mutation.|||In APRTD; Newfoundland type.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149504|||http://purl.uniprot.org/annotation/VAR_006747|||http://purl.uniprot.org/annotation/VAR_006748|||http://purl.uniprot.org/annotation/VAR_006749|||http://purl.uniprot.org/annotation/VAR_019055|||http://purl.uniprot.org/annotation/VAR_022608|||http://purl.uniprot.org/annotation/VAR_022609|||http://purl.uniprot.org/annotation/VAR_037575|||http://purl.uniprot.org/annotation/VAR_069049|||http://purl.uniprot.org/annotation/VAR_069050|||http://purl.uniprot.org/annotation/VAR_069051|||http://purl.uniprot.org/annotation/VSP_045705
http://togogenome.org/gene/9606:SLC1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y860|||http://purl.uniprot.org/uniprot/A0A2R8YFE3|||http://purl.uniprot.org/uniprot/A0A2U3TZS7|||http://purl.uniprot.org/uniprot/A2A2U1|||http://purl.uniprot.org/uniprot/P43004                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Discontinuously helical|||Excitatory amino acid transporter 2|||Extracellular|||Helical|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In DEE41.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202061|||http://purl.uniprot.org/annotation/VAR_077083|||http://purl.uniprot.org/annotation/VAR_077084|||http://purl.uniprot.org/annotation/VAR_080229|||http://purl.uniprot.org/annotation/VSP_037152|||http://purl.uniprot.org/annotation/VSP_054934
http://togogenome.org/gene/9606:GCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92616                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished interaction with RNF14 and decreased interaction with EIF2AK4/GCN2.|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 21|||HEAT 22|||HEAT 23|||HEAT 24|||HEAT 25|||HEAT 26|||HEAT 27|||HEAT 28|||HEAT 29|||HEAT 3|||HEAT 30|||HEAT 31|||HEAT 32|||HEAT 33|||HEAT 34|||HEAT 35|||HEAT 36|||HEAT 37|||HEAT 38|||HEAT 39|||HEAT 4|||HEAT 40|||HEAT 41|||HEAT 42|||HEAT 43|||HEAT 44|||HEAT 45|||HEAT 46|||HEAT 47; degenerate|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||N-acetylalanine|||Phosphoserine|||RWDBD region|||Removed|||Stalled ribosome sensor GCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087443|||http://purl.uniprot.org/annotation/VAR_062228
http://togogenome.org/gene/9606:CNTN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94779                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Contactin-5|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated serine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014717|||http://purl.uniprot.org/annotation/PRO_0000014718|||http://purl.uniprot.org/annotation/VAR_019907|||http://purl.uniprot.org/annotation/VAR_019908|||http://purl.uniprot.org/annotation/VAR_019909|||http://purl.uniprot.org/annotation/VAR_019910|||http://purl.uniprot.org/annotation/VAR_019911|||http://purl.uniprot.org/annotation/VAR_019912|||http://purl.uniprot.org/annotation/VAR_033610|||http://purl.uniprot.org/annotation/VSP_011967|||http://purl.uniprot.org/annotation/VSP_045995
http://togogenome.org/gene/9606:NEPRO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHL5|||http://purl.uniprot.org/uniprot/B4DJ73|||http://purl.uniprot.org/uniprot/B4DUV5|||http://purl.uniprot.org/uniprot/Q6NW34                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In ANXD3; unknown pathological significance.|||In isoform 2.|||Nuclear localization signal|||Nucleolus and neural progenitor protein|||Nucleolus and neural progenitor protein-like N-terminal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225012|||http://purl.uniprot.org/annotation/VAR_025418|||http://purl.uniprot.org/annotation/VAR_025419|||http://purl.uniprot.org/annotation/VAR_025420|||http://purl.uniprot.org/annotation/VAR_025421|||http://purl.uniprot.org/annotation/VAR_025422|||http://purl.uniprot.org/annotation/VAR_084136|||http://purl.uniprot.org/annotation/VAR_084137|||http://purl.uniprot.org/annotation/VSP_017342|||http://purl.uniprot.org/annotation/VSP_017343
http://togogenome.org/gene/9606:ANO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IWH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin-7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289326|||http://purl.uniprot.org/annotation/VAR_032616|||http://purl.uniprot.org/annotation/VAR_065166|||http://purl.uniprot.org/annotation/VSP_026004|||http://purl.uniprot.org/annotation/VSP_026005|||http://purl.uniprot.org/annotation/VSP_026006|||http://purl.uniprot.org/annotation/VSP_026007|||http://purl.uniprot.org/annotation/VSP_026008
http://togogenome.org/gene/9606:SPTBN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H254                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In NEDHND; decreased protein abundance in patient cells homozygous for the mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin beta chain, non-erythrocytic 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073465|||http://purl.uniprot.org/annotation/VAR_048632|||http://purl.uniprot.org/annotation/VAR_079212|||http://purl.uniprot.org/annotation/VSP_000723|||http://purl.uniprot.org/annotation/VSP_000724|||http://purl.uniprot.org/annotation/VSP_000725|||http://purl.uniprot.org/annotation/VSP_000726|||http://purl.uniprot.org/annotation/VSP_000727|||http://purl.uniprot.org/annotation/VSP_000728|||http://purl.uniprot.org/annotation/VSP_046383|||http://purl.uniprot.org/annotation/VSP_046384|||http://purl.uniprot.org/annotation/VSP_046385
http://togogenome.org/gene/9606:ASIC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY37                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acid-sensing ion channel 5|||Activates the channel.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Slightly activates the channel.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335597
http://togogenome.org/gene/9606:BTBD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8SD95|||http://purl.uniprot.org/uniprot/B4DYL8|||http://purl.uniprot.org/uniprot/Q5XKL5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB 1|||BTB 2|||BTB/POZ|||BTB/POZ domain-containing protein 8|||Basic and acidic residues|||Disordered|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239224|||http://purl.uniprot.org/annotation/VAR_033637|||http://purl.uniprot.org/annotation/VAR_048436|||http://purl.uniprot.org/annotation/VAR_060300|||http://purl.uniprot.org/annotation/VAR_060301|||http://purl.uniprot.org/annotation/VAR_060302|||http://purl.uniprot.org/annotation/VAR_060303|||http://purl.uniprot.org/annotation/VAR_060304|||http://purl.uniprot.org/annotation/VAR_060305|||http://purl.uniprot.org/annotation/VAR_060306|||http://purl.uniprot.org/annotation/VAR_060307|||http://purl.uniprot.org/annotation/VAR_060308|||http://purl.uniprot.org/annotation/VAR_060309|||http://purl.uniprot.org/annotation/VAR_060310|||http://purl.uniprot.org/annotation/VSP_061629|||http://purl.uniprot.org/annotation/VSP_061630
http://togogenome.org/gene/9606:RPP40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75818                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Ribonuclease P protein subunit p40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097434|||http://purl.uniprot.org/annotation/VAR_055405|||http://purl.uniprot.org/annotation/VSP_037346
http://togogenome.org/gene/9606:HERC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GLZ8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Probable E3 ubiquitin-protein ligase HERC4|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278216|||http://purl.uniprot.org/annotation/VSP_023172|||http://purl.uniprot.org/annotation/VSP_023173|||http://purl.uniprot.org/annotation/VSP_023174|||http://purl.uniprot.org/annotation/VSP_023175|||http://purl.uniprot.org/annotation/VSP_023176|||http://purl.uniprot.org/annotation/VSP_023178|||http://purl.uniprot.org/annotation/VSP_023179|||http://purl.uniprot.org/annotation/VSP_039551
http://togogenome.org/gene/9606:NCBP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6PVI3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Nuclear cap-binding protein subunit 2-like|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299538
http://togogenome.org/gene/9606:OR52B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW82|||http://purl.uniprot.org/uniprot/Q8NGK2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150768|||http://purl.uniprot.org/annotation/VAR_037834
http://togogenome.org/gene/9606:CAMK2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K161|||http://purl.uniprot.org/uniprot/Q7LDD5|||http://purl.uniprot.org/uniprot/Q8IWE0|||http://purl.uniprot.org/uniprot/Q9UQM7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase type II subunit alpha|||Calmodulin-binding|||Disordered|||In MRD53; decreased protein abundance; increased autophosphorylation; decreased neuronal migration.|||In MRD53; increased basal autophosphorylation.|||In MRD53; increased ubiquitin-mediated proteasomal degradation with a dominant negative effect on wild-type protein; decreased localization to dendritic spines; no effect on holoenzyme assembly; loss of interaction with SHANK3; loss of interaction with GRIN2B; loss of interaction with CACNB2; loss of interaction with LRRC7; loss of interaction with GRM5; decreased protein serine/threonine kinase activity with a dominant negative effect on wild-type protein; decreased autophosphorylation; changed dendritic spine development; decreased neuronal migration.|||In MRD53; no effect on protein abundance; decreased autophosphorylation; decreased neuronal migration.|||In MRD53; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration.|||In MRD53; no effect on protein abundance; loss of autophosphorylation; loss of neuronal migration.|||In MRD53; unknown pathological significance.|||In MRD53; unknown pathological significance; no effect on protein abundance; no effect on autophosphorylation; no effect on neuronal migration.|||In MRT63; decreased oligomerization.|||In isoform B.|||Interaction with BAALC|||Loss of neuronal migration.|||Loss of oligomerization.|||No effect on neuronal migration.|||No effect on neuronal migration; when associated with R-42.|||No effect on protein stability or degradation. No effect on neuronal migration; when associated with P-286.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086091|||http://purl.uniprot.org/annotation/VAR_080579|||http://purl.uniprot.org/annotation/VAR_080580|||http://purl.uniprot.org/annotation/VAR_080581|||http://purl.uniprot.org/annotation/VAR_080582|||http://purl.uniprot.org/annotation/VAR_080583|||http://purl.uniprot.org/annotation/VAR_080584|||http://purl.uniprot.org/annotation/VAR_080585|||http://purl.uniprot.org/annotation/VAR_080586|||http://purl.uniprot.org/annotation/VAR_080587|||http://purl.uniprot.org/annotation/VAR_081160|||http://purl.uniprot.org/annotation/VAR_081161|||http://purl.uniprot.org/annotation/VSP_004766
http://togogenome.org/gene/9606:PPP1R11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2BEK1|||http://purl.uniprot.org/uniprot/O60927                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Atypical RING finger domain 1|||Atypical RING finger domain 2|||Disordered|||E3 ubiquitin-protein ligase PPP1R11|||Loss of function in inducing TLR2 degradation.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239619
http://togogenome.org/gene/9606:PTGIR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43119                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes isoprenylation.|||Cysteine methyl ester|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prostacyclin receptor|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070075|||http://purl.uniprot.org/annotation/PRO_0000240004|||http://purl.uniprot.org/annotation/VAR_024260|||http://purl.uniprot.org/annotation/VAR_061226
http://togogenome.org/gene/9606:TREM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCX1|||http://purl.uniprot.org/uniprot/Q9NZC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects protein maturation.|||Cleavage of ectodomain|||Cytoplasmic|||Decreases LDL, CLU and APOE binding; decreases LDL and CLU uptake into cells; no effect on cell membrane localization.|||Decreases binding to THP-1 cells.|||Does not affect protein structure; no effect on cell membrane localization; increases autophagy in microglia; decreases LDL, CLU and APOE binding; decreases LDL uptake into cells; no effect on CLU uptake into cells; decreases the uptake of APP-LDL complex in macrophages; decreases binding to oligomeric APP cleavage product beta-amyloid peptide 42.|||Does not change protein structure; changes protein stability; increases binding to THP-1 cells.|||Extracellular|||Found in patients with Alzheimer disease; unknown pathological significance; decreases cell membrane localization.|||Found in patients with Alzheimer disease; unknown pathological significance; slightly decreases cell membrane localization.|||Found in patients with late onset Alzheimer disease; unknown pathological significance; decreases cell membrane localization.|||Found in patients with late onset Alzheimer disease; unknown pathological significance; increases cell membrane localization.|||Found in patients with late onset Alzheimer disease; unknown pathological significance; no effect on cell membrane localization.|||Found in patients with late onset Alzheimer disease; unknown pathological significance; no effect on cell membrane localization; no effect on autophagy in microglia; no effect on phagocystosis, including amyloid plaque clearance by microglia; reduces ectodomain shedding caused by proteolytic cleavage by ADAM10, while also reducing the oligomerization of the extracellular domain after shedding; decreases binding to and uptake of LDL and CLU into cells; decreases binding to APOE, phospholipids and oligomeric APP cleavage product beta-amyloid peptide 42.|||Helical|||Ig-like V-type|||Immunoglobulin V-set|||In PLOSL2.|||In PLOSL2; no protein detected by Wester blot.|||In PLOSL2; results in decreased osteoclast differentiation; no TREM2 transcripts can be detected in patient cells homozygous for the variant.|||In PLOSL2; results in defective protein maturation; increases protein aggregation; decreases cell membrane localization.|||In PLOSL2; unknown pathological significance; decreased protein level.|||In PLOSL2; unknown pathological significance; increased localization at the cell membrane.|||In isoform 2.|||In isoform 3.|||Likely benign variant; no effect on protein expression and maturation.|||Loss of LDL, CLU and APOE binding.|||Loss of glycosylation.|||Loss of proteolytic cleavage by ADAM10 and ectodomain shedding. Decreases protein maturation and cell membrane localization.|||May be associated with an increased risk for late-onset Alzheimer disease; accelerates ectodomain shedding but does not alter the cleavage site; decreases cell membrane localization; decreases phagocytosis.|||N-linked (GlcNAc...) asparagine|||No effect on cell membrane localization.|||No effect on protein expression and maturation.|||Results in defective protein maturation and trafficking; loss of proteolytic cleavage by ADAM10 and ectodomain shedding; increases protein aggregation; decreases cell membrane localization; decreased phagocytosis; loss of LDL, CLU and APOE binding; greatly decreases LDL and CLU uptake into cells.|||Results in defective protein maturation and trafficking; loss of proteolytic cleavage by ADAM10 and ectodomain shedding; increases protein aggregation; decreases cell membrane localization; decreases phagocytosis; loss of LDL, CLU and APOE binding; greatly decreases LDL and CLU uptake into cells.|||Triggering receptor expressed on myeloid cells 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014987|||http://purl.uniprot.org/annotation/PRO_5014309966|||http://purl.uniprot.org/annotation/VAR_019334|||http://purl.uniprot.org/annotation/VAR_019335|||http://purl.uniprot.org/annotation/VAR_033625|||http://purl.uniprot.org/annotation/VAR_033626|||http://purl.uniprot.org/annotation/VAR_061329|||http://purl.uniprot.org/annotation/VAR_061330|||http://purl.uniprot.org/annotation/VAR_077696|||http://purl.uniprot.org/annotation/VAR_081676|||http://purl.uniprot.org/annotation/VAR_081677|||http://purl.uniprot.org/annotation/VAR_081678|||http://purl.uniprot.org/annotation/VAR_081679|||http://purl.uniprot.org/annotation/VAR_081680|||http://purl.uniprot.org/annotation/VAR_081812|||http://purl.uniprot.org/annotation/VAR_081813|||http://purl.uniprot.org/annotation/VAR_081814|||http://purl.uniprot.org/annotation/VAR_081815|||http://purl.uniprot.org/annotation/VAR_081816|||http://purl.uniprot.org/annotation/VAR_081817|||http://purl.uniprot.org/annotation/VAR_081818|||http://purl.uniprot.org/annotation/VAR_081819|||http://purl.uniprot.org/annotation/VAR_081820|||http://purl.uniprot.org/annotation/VAR_081821|||http://purl.uniprot.org/annotation/VAR_081822|||http://purl.uniprot.org/annotation/VAR_081823|||http://purl.uniprot.org/annotation/VAR_081824|||http://purl.uniprot.org/annotation/VAR_081825|||http://purl.uniprot.org/annotation/VAR_081826|||http://purl.uniprot.org/annotation/VAR_082839|||http://purl.uniprot.org/annotation/VAR_082840|||http://purl.uniprot.org/annotation/VSP_010792|||http://purl.uniprot.org/annotation/VSP_010793
http://togogenome.org/gene/9606:DACH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DACHbox-C|||DACHbox-N|||Dachshund homolog 1|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with SIN3A|||Interaction with SIX6 and HDAC3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095597|||http://purl.uniprot.org/annotation/VAR_080662|||http://purl.uniprot.org/annotation/VSP_009486|||http://purl.uniprot.org/annotation/VSP_009872|||http://purl.uniprot.org/annotation/VSP_009873
http://togogenome.org/gene/9606:BCLAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bcl-2-associated transcription factor 1|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064888|||http://purl.uniprot.org/annotation/VAR_050692|||http://purl.uniprot.org/annotation/VAR_050693|||http://purl.uniprot.org/annotation/VAR_050694|||http://purl.uniprot.org/annotation/VAR_050695|||http://purl.uniprot.org/annotation/VAR_050696|||http://purl.uniprot.org/annotation/VAR_059591|||http://purl.uniprot.org/annotation/VSP_010369|||http://purl.uniprot.org/annotation/VSP_010370|||http://purl.uniprot.org/annotation/VSP_010371
http://togogenome.org/gene/9606:LDHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00338|||http://purl.uniprot.org/uniprot/V9HWB9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MP31.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increases binding to FLCN.|||L-lactate dehydrogenase A chain|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168411|||http://purl.uniprot.org/annotation/VAR_004180|||http://purl.uniprot.org/annotation/VAR_004181|||http://purl.uniprot.org/annotation/VSP_014261|||http://purl.uniprot.org/annotation/VSP_042206|||http://purl.uniprot.org/annotation/VSP_042786|||http://purl.uniprot.org/annotation/VSP_042787|||http://purl.uniprot.org/annotation/VSP_042788|||http://purl.uniprot.org/annotation/VSP_042789
http://togogenome.org/gene/9606:CHPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPG6|||http://purl.uniprot.org/uniprot/G5E9W2|||http://purl.uniprot.org/uniprot/Q9P2E5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate glucuronyltransferase|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189563|||http://purl.uniprot.org/annotation/VSP_012724|||http://purl.uniprot.org/annotation/VSP_012725
http://togogenome.org/gene/9606:OR2T2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IF00                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150497
http://togogenome.org/gene/9606:IL1RAPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZN1|||http://purl.uniprot.org/uniprot/X5DNQ7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for interaction with PTPRD|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Interaction with NCS1|||Interleukin-1 receptor accessory protein-like 1|||N-linked (GlcNAc...) asparagine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015454|||http://purl.uniprot.org/annotation/PRO_5004954498|||http://purl.uniprot.org/annotation/VAR_062263|||http://purl.uniprot.org/annotation/VAR_062264|||http://purl.uniprot.org/annotation/VAR_062265|||http://purl.uniprot.org/annotation/VAR_062266
http://togogenome.org/gene/9606:SLX1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes endonucleolytic activity.|||Disordered|||GIY-YIG|||In isoform 2.|||Pro residues|||SLX1-type|||Structure-specific endonuclease subunit SLX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332120|||http://purl.uniprot.org/annotation/VSP_033331
http://togogenome.org/gene/9606:PLA2G4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UP65                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-385 and A-402.|||Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-82 and A-385.|||Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-54; A-82 and A-402.|||Abolishes enzyme activity. Reduces lipid droplet formation; when associated with A-82; A-385 and A-402.|||Cysteine methyl ester|||Cytosolic phospholipase A2 gamma|||Has no effect on membrane localization. Decreases the affinity for 1-O-hexadecyl-sn-glycero-3-phosphocholine acyl acceptor in transacylation reaction.|||In isoform 2.|||In isoform 3.|||Loss of prenylation.|||Nucleophile|||PLA2c|||Phosphoserine|||Proton acceptor|||Removed in mature form|||Required for lipid droplet localization|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022995|||http://purl.uniprot.org/annotation/PRO_0000022996|||http://purl.uniprot.org/annotation/VAR_018420|||http://purl.uniprot.org/annotation/VAR_018421|||http://purl.uniprot.org/annotation/VAR_018422|||http://purl.uniprot.org/annotation/VAR_018423|||http://purl.uniprot.org/annotation/VAR_018761|||http://purl.uniprot.org/annotation/VAR_018762|||http://purl.uniprot.org/annotation/VAR_018763|||http://purl.uniprot.org/annotation/VAR_018764|||http://purl.uniprot.org/annotation/VAR_018765|||http://purl.uniprot.org/annotation/VAR_018766|||http://purl.uniprot.org/annotation/VAR_018767|||http://purl.uniprot.org/annotation/VAR_018768|||http://purl.uniprot.org/annotation/VSP_045849|||http://purl.uniprot.org/annotation/VSP_045850
http://togogenome.org/gene/9606:MELTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08582|||http://purl.uniprot.org/uniprot/Q53XS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Antigenic epitope|||Basic and acidic residues|||Disordered|||GPI-anchor amidated cysteine|||In isoform 2.|||Melanotransferrin|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Removed in mature form|||Transferrin-like|||Transferrin-like 1|||Transferrin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035739|||http://purl.uniprot.org/annotation/PRO_0000035740|||http://purl.uniprot.org/annotation/PRO_5014309517|||http://purl.uniprot.org/annotation/VAR_020413|||http://purl.uniprot.org/annotation/VAR_057304|||http://purl.uniprot.org/annotation/VSP_006557|||http://purl.uniprot.org/annotation/VSP_006558
http://togogenome.org/gene/9606:COX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00414|||http://purl.uniprot.org/uniprot/Q7GIM7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 3|||Found in two patients with a diagnosis of mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes syndrome; unknown pathological significance.|||Helical|||Helical; Name=I|||Helical; Name=II|||Helical; Name=III|||Helical; Name=IV|||Helical; Name=V|||Helical; Name=VI|||Helical; Name=VII|||Heme-copper oxidase subunit III family profile|||In LHON; possible rare primary mutation.|||In LHON; secondary mutation; does not seem to directly cause the disease.|||In MT-C4D; with RM-MT.|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183793|||http://purl.uniprot.org/annotation/VAR_002167|||http://purl.uniprot.org/annotation/VAR_002168|||http://purl.uniprot.org/annotation/VAR_002169|||http://purl.uniprot.org/annotation/VAR_008573|||http://purl.uniprot.org/annotation/VAR_008574|||http://purl.uniprot.org/annotation/VAR_008575|||http://purl.uniprot.org/annotation/VAR_008576|||http://purl.uniprot.org/annotation/VAR_008577|||http://purl.uniprot.org/annotation/VAR_033057
http://togogenome.org/gene/9606:MECP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC4|||http://purl.uniprot.org/uniprot/D3YJ43|||http://purl.uniprot.org/uniprot/P51608|||http://purl.uniprot.org/uniprot/Q59FJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||Basic and acidic residues|||Disordered|||In ENS-MECP2; uncertain pathological significance.|||In MRXS13.|||In MRXS13; impairs interaction with ATRX and abolishes ATRX recruitment to heterochromatin.|||In MRXS13; unknown pathological significance.|||In RTT.|||In RTT; abolishes interaction with TBL1X and TBL1XR1.|||In RTT; abolishes interaction with TBL1X.|||In RTT; also in a patient with Angelman syndrome and some typical RTT features.|||In RTT; impairs interaction with ATRX and abolishes ATRX recruitment to heterochromatin.|||In RTT; unknown pathological significance.|||In isoform B.|||Interaction with NCOR2|||Interaction with TBL1XR1|||MBD|||Methyl-CpG-binding protein 2|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||Probable disease-associated variant found in a patient with drug-resistant epilepsy with intellectual disability, parkinsonism and other neurologic symptoms.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096345|||http://purl.uniprot.org/annotation/VAR_010272|||http://purl.uniprot.org/annotation/VAR_010273|||http://purl.uniprot.org/annotation/VAR_010274|||http://purl.uniprot.org/annotation/VAR_010275|||http://purl.uniprot.org/annotation/VAR_010276|||http://purl.uniprot.org/annotation/VAR_010277|||http://purl.uniprot.org/annotation/VAR_010278|||http://purl.uniprot.org/annotation/VAR_010279|||http://purl.uniprot.org/annotation/VAR_010280|||http://purl.uniprot.org/annotation/VAR_010281|||http://purl.uniprot.org/annotation/VAR_010282|||http://purl.uniprot.org/annotation/VAR_010283|||http://purl.uniprot.org/annotation/VAR_017462|||http://purl.uniprot.org/annotation/VAR_017463|||http://purl.uniprot.org/annotation/VAR_017581|||http://purl.uniprot.org/annotation/VAR_018180|||http://purl.uniprot.org/annotation/VAR_018181|||http://purl.uniprot.org/annotation/VAR_018182|||http://purl.uniprot.org/annotation/VAR_018183|||http://purl.uniprot.org/annotation/VAR_018184|||http://purl.uniprot.org/annotation/VAR_018185|||http://purl.uniprot.org/annotation/VAR_018186|||http://purl.uniprot.org/annotation/VAR_018187|||http://purl.uniprot.org/annotation/VAR_018188|||http://purl.uniprot.org/annotation/VAR_018189|||http://purl.uniprot.org/annotation/VAR_018190|||http://purl.uniprot.org/annotation/VAR_018191|||http://purl.uniprot.org/annotation/VAR_018192|||http://purl.uniprot.org/annotation/VAR_018193|||http://purl.uniprot.org/annotation/VAR_018194|||http://purl.uniprot.org/annotation/VAR_018195|||http://purl.uniprot.org/annotation/VAR_018196|||http://purl.uniprot.org/annotation/VAR_018197|||http://purl.uniprot.org/annotation/VAR_018198|||http://purl.uniprot.org/annotation/VAR_018199|||http://purl.uniprot.org/annotation/VAR_018200|||http://purl.uniprot.org/annotation/VAR_018201|||http://purl.uniprot.org/annotation/VAR_018202|||http://purl.uniprot.org/annotation/VAR_018203|||http://purl.uniprot.org/annotation/VAR_018204|||http://purl.uniprot.org/annotation/VAR_018205|||http://purl.uniprot.org/annotation/VAR_018206|||http://purl.uniprot.org/annotation/VAR_018207|||http://purl.uniprot.org/annotation/VAR_018208|||http://purl.uniprot.org/annotation/VAR_018209|||http://purl.uniprot.org/annotation/VAR_018210|||http://purl.uniprot.org/annotation/VAR_018211|||http://purl.uniprot.org/annotation/VAR_018212|||http://purl.uniprot.org/annotation/VAR_018213|||http://purl.uniprot.org/annotation/VAR_018214|||http://purl.uniprot.org/annotation/VAR_018215|||http://purl.uniprot.org/annotation/VAR_018216|||http://purl.uniprot.org/annotation/VAR_018217|||http://purl.uniprot.org/annotation/VAR_018218|||http://purl.uniprot.org/annotation/VAR_018219|||http://purl.uniprot.org/annotation/VAR_018220|||http://purl.uniprot.org/annotation/VAR_018221|||http://purl.uniprot.org/annotation/VAR_018222|||http://purl.uniprot.org/annotation/VAR_018223|||http://purl.uniprot.org/annotation/VAR_018224|||http://purl.uniprot.org/annotation/VAR_018225|||http://purl.uniprot.org/annotation/VAR_018226|||http://purl.uniprot.org/annotation/VAR_023552|||http://purl.uniprot.org/annotation/VAR_023553|||http://purl.uniprot.org/annotation/VAR_023554|||http://purl.uniprot.org/annotation/VAR_023555|||http://purl.uniprot.org/annotation/VAR_023556|||http://purl.uniprot.org/annotation/VAR_023557|||http://purl.uniprot.org/annotation/VAR_023558|||http://purl.uniprot.org/annotation/VAR_023559|||http://purl.uniprot.org/annotation/VAR_037664|||http://purl.uniprot.org/annotation/VAR_037665|||http://purl.uniprot.org/annotation/VAR_078221|||http://purl.uniprot.org/annotation/VAR_078720|||http://purl.uniprot.org/annotation/VSP_022948
http://togogenome.org/gene/9606:SSH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE77                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEK-C|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Pro residues|||Protein phosphatase Slingshot homolog 3|||Removed|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094845|||http://purl.uniprot.org/annotation/VAR_057132|||http://purl.uniprot.org/annotation/VAR_057133|||http://purl.uniprot.org/annotation/VSP_016330|||http://purl.uniprot.org/annotation/VSP_016331|||http://purl.uniprot.org/annotation/VSP_016332|||http://purl.uniprot.org/annotation/VSP_016333|||http://purl.uniprot.org/annotation/VSP_016334|||http://purl.uniprot.org/annotation/VSP_016335|||http://purl.uniprot.org/annotation/VSP_016336
http://togogenome.org/gene/9606:CHD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 5|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Histone-binding|||In PMNDS.|||In PMNDS; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||N5-methylglutamine|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Reduced affinity for trimethylated histone H3K27me3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080230|||http://purl.uniprot.org/annotation/VAR_035475|||http://purl.uniprot.org/annotation/VAR_035476|||http://purl.uniprot.org/annotation/VAR_035477|||http://purl.uniprot.org/annotation/VAR_048729|||http://purl.uniprot.org/annotation/VAR_048730|||http://purl.uniprot.org/annotation/VAR_087312|||http://purl.uniprot.org/annotation/VAR_087313|||http://purl.uniprot.org/annotation/VAR_087314|||http://purl.uniprot.org/annotation/VAR_087315|||http://purl.uniprot.org/annotation/VAR_087316|||http://purl.uniprot.org/annotation/VAR_087317|||http://purl.uniprot.org/annotation/VAR_087318|||http://purl.uniprot.org/annotation/VAR_087319|||http://purl.uniprot.org/annotation/VAR_087320|||http://purl.uniprot.org/annotation/VAR_087321|||http://purl.uniprot.org/annotation/VAR_087322|||http://purl.uniprot.org/annotation/VAR_087323|||http://purl.uniprot.org/annotation/VAR_087324|||http://purl.uniprot.org/annotation/VAR_087325
http://togogenome.org/gene/9606:WFDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCV5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||WAP 1|||WAP 2|||WAP four-disulfide core domain protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041382|||http://purl.uniprot.org/annotation/VAR_057474|||http://purl.uniprot.org/annotation/VSP_006756
http://togogenome.org/gene/9606:OR51I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVE9|||http://purl.uniprot.org/uniprot/Q9H344                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51I2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150758|||http://purl.uniprot.org/annotation/VAR_024143|||http://purl.uniprot.org/annotation/VAR_034321|||http://purl.uniprot.org/annotation/VAR_034322|||http://purl.uniprot.org/annotation/VAR_034323
http://togogenome.org/gene/9606:FMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8Z4|||http://purl.uniprot.org/uniprot/B7Z3M2|||http://purl.uniprot.org/uniprot/B7Z543|||http://purl.uniprot.org/uniprot/P31513|||http://purl.uniprot.org/uniprot/Q53FW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  16% reduction in catalytic efficiency toward trimethylamine and 40% increase toward benzydamine and methyl p-tolyl sulfide.|||2-fold decrease in affinity for trimethylamine; 3-fold decrease in catalytic efficiency toward methimazole; 3-fold increase in catalytic efficiency toward sulindac; 30% increase in catalytic efficiency toward ethylenethiourea.|||35%, 45% and 71% increase in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide, respectively.|||65% increase in catalytic efficiency toward trimethylamine and 60% reduction toward benzydamine and methyl p-tolyl sulfide.|||Flavin-containing monooxygenase 3|||Helical|||In TMAU.|||In TMAU; 90% reduction in catalytic efficiency toward trimethylamine and benzydamine; 34% reduction in catalytic efficiency toward methyl p-tolyl sulfide; nearly no effect on affinity for these substrates.|||In TMAU; loss of activity; affects FAD binding.|||In TMAU; more than 90% reduction in catalytic efficiency toward trimethylamine, benzydamine and methyl p-tolyl sulfide.|||In TMAU; profoundly alters enzyme function.|||Loss of activity.|||Modest increase in catalytic efficiency toward trimethylamine, methimazole, ethylenethiourea and sulindac.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147654|||http://purl.uniprot.org/annotation/VAR_002423|||http://purl.uniprot.org/annotation/VAR_002424|||http://purl.uniprot.org/annotation/VAR_002425|||http://purl.uniprot.org/annotation/VAR_002426|||http://purl.uniprot.org/annotation/VAR_002427|||http://purl.uniprot.org/annotation/VAR_008145|||http://purl.uniprot.org/annotation/VAR_008146|||http://purl.uniprot.org/annotation/VAR_008147|||http://purl.uniprot.org/annotation/VAR_014845|||http://purl.uniprot.org/annotation/VAR_014846|||http://purl.uniprot.org/annotation/VAR_015364|||http://purl.uniprot.org/annotation/VAR_015365|||http://purl.uniprot.org/annotation/VAR_015366|||http://purl.uniprot.org/annotation/VAR_018345|||http://purl.uniprot.org/annotation/VAR_018346|||http://purl.uniprot.org/annotation/VAR_037306|||http://purl.uniprot.org/annotation/VAR_037307|||http://purl.uniprot.org/annotation/VAR_037308|||http://purl.uniprot.org/annotation/VAR_042705|||http://purl.uniprot.org/annotation/VAR_042706|||http://purl.uniprot.org/annotation/VAR_042707
http://togogenome.org/gene/9606:SNW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V3A4|||http://purl.uniprot.org/uniprot/Q13573                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PPIL1.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with PPIL1|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SKI-interacting protein SKIP SNW|||SNW|||SNW domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084827
http://togogenome.org/gene/9606:OTOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRC9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Otoraplin|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019033|||http://purl.uniprot.org/annotation/VAR_024537
http://togogenome.org/gene/9606:CAMSAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NY94|||http://purl.uniprot.org/uniprot/Q5T5Y3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CKK|||Calmodulin-regulated spectrin-associated protein 1|||Calponin-homology (CH)|||Disordered|||In CDCBM12.|||In isoform 2.|||In isoform 3.|||Loss of interaction with SPTBN1.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Sufficient for interaction with SPTBN1|||Sufficient for interaction with calmodulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316828|||http://purl.uniprot.org/annotation/VAR_038398|||http://purl.uniprot.org/annotation/VAR_088401|||http://purl.uniprot.org/annotation/VAR_088402|||http://purl.uniprot.org/annotation/VAR_088403|||http://purl.uniprot.org/annotation/VAR_088404|||http://purl.uniprot.org/annotation/VSP_030800|||http://purl.uniprot.org/annotation/VSP_030801
http://togogenome.org/gene/9606:SYT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00445                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Does not affect Ca(2+) affinity as measured by isothermal titration calorimetry of the mutant protein.|||Helical|||In isoform 2.|||Pro residues|||Synaptotagmin-5|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183951|||http://purl.uniprot.org/annotation/VAR_034528|||http://purl.uniprot.org/annotation/VAR_052240|||http://purl.uniprot.org/annotation/VSP_057177|||http://purl.uniprot.org/annotation/VSP_057178
http://togogenome.org/gene/9606:ATE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KTH0|||http://purl.uniprot.org/uniprot/A0A8I5KZ24|||http://purl.uniprot.org/uniprot/B3KWA3|||http://purl.uniprot.org/uniprot/B4DK25|||http://purl.uniprot.org/uniprot/B4E107|||http://purl.uniprot.org/uniprot/F5GXE4|||http://purl.uniprot.org/uniprot/F8WAC9|||http://purl.uniprot.org/uniprot/O95260                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Arginyl-tRNA--protein transferase 1|||Basic and acidic residues|||Disordered|||In isoform ATE1-2.|||N-end aminoacyl transferase N-terminal|||N-end rule aminoacyl transferase C-terminal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195088|||http://purl.uniprot.org/annotation/VSP_000336
http://togogenome.org/gene/9606:KLHDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228998|||http://purl.uniprot.org/annotation/VAR_033986|||http://purl.uniprot.org/annotation/VAR_033987|||http://purl.uniprot.org/annotation/VAR_050054|||http://purl.uniprot.org/annotation/VAR_061340|||http://purl.uniprot.org/annotation/VSP_017728|||http://purl.uniprot.org/annotation/VSP_017729
http://togogenome.org/gene/9606:CLCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7I4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes proteolytic cleavage.|||Calcium-activated chloride channel regulator 1|||Cleavage; by autolysis|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||Reduces proteolytic cleavage.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333690|||http://purl.uniprot.org/annotation/VAR_043146|||http://purl.uniprot.org/annotation/VAR_043147|||http://purl.uniprot.org/annotation/VAR_054654|||http://purl.uniprot.org/annotation/VAR_054655|||http://purl.uniprot.org/annotation/VAR_054656|||http://purl.uniprot.org/annotation/VAR_054657|||http://purl.uniprot.org/annotation/VAR_054658|||http://purl.uniprot.org/annotation/VAR_054659
http://togogenome.org/gene/9606:ARL5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 5B|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207470
http://togogenome.org/gene/9606:FAM47C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HY64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Putative protein FAM47C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349311|||http://purl.uniprot.org/annotation/VAR_046358
http://togogenome.org/gene/9606:MSGN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Mesogenin-1|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330028|||http://purl.uniprot.org/annotation/VAR_061259|||http://purl.uniprot.org/annotation/VAR_061260
http://togogenome.org/gene/9606:RASD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y272                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Dexamethasone-induced Ras-related protein 1|||Effector region|||In isoform 2.|||Removed in mature form|||S-farnesyl cysteine|||S-nitrosocysteine|||Suppresses NO-induced activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082717|||http://purl.uniprot.org/annotation/PRO_0000281372|||http://purl.uniprot.org/annotation/VSP_046431|||http://purl.uniprot.org/annotation/VSP_046432
http://togogenome.org/gene/9606:NPNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 6.|||Integrin interaction|||MAM|||Nephronectin|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295684|||http://purl.uniprot.org/annotation/VAR_033314|||http://purl.uniprot.org/annotation/VAR_033315|||http://purl.uniprot.org/annotation/VAR_033316|||http://purl.uniprot.org/annotation/VAR_033317|||http://purl.uniprot.org/annotation/VSP_026987|||http://purl.uniprot.org/annotation/VSP_026988|||http://purl.uniprot.org/annotation/VSP_045813|||http://purl.uniprot.org/annotation/VSP_046131
http://togogenome.org/gene/9606:IL36B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZH7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Propeptide|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interleukin-36 beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153646|||http://purl.uniprot.org/annotation/PRO_0000430547|||http://purl.uniprot.org/annotation/VAR_025057|||http://purl.uniprot.org/annotation/VSP_002657
http://togogenome.org/gene/9606:HK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52789                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased hexokinase activity.|||Does not affect activity.|||Hexokinase 1|||Hexokinase 2|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||Hexokinase-2|||Induces a rapid dissociation of D-glucose.|||Mitochondrial-binding peptide (MBP)|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197587|||http://purl.uniprot.org/annotation/VAR_003691|||http://purl.uniprot.org/annotation/VAR_010577|||http://purl.uniprot.org/annotation/VAR_010578|||http://purl.uniprot.org/annotation/VAR_010579|||http://purl.uniprot.org/annotation/VAR_010580|||http://purl.uniprot.org/annotation/VAR_010581|||http://purl.uniprot.org/annotation/VAR_010582|||http://purl.uniprot.org/annotation/VAR_020504|||http://purl.uniprot.org/annotation/VAR_020505|||http://purl.uniprot.org/annotation/VAR_020506|||http://purl.uniprot.org/annotation/VAR_020507|||http://purl.uniprot.org/annotation/VAR_020508|||http://purl.uniprot.org/annotation/VAR_020509
http://togogenome.org/gene/9606:PRR20A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86478|||http://purl.uniprot.org/uniprot/P86479|||http://purl.uniprot.org/uniprot/P86480|||http://purl.uniprot.org/uniprot/P86481|||http://purl.uniprot.org/uniprot/P86496                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 20A|||Proline-rich protein 20B|||Proline-rich protein 20C|||Proline-rich protein 20D|||Proline-rich protein 20E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336092|||http://purl.uniprot.org/annotation/PRO_0000393890|||http://purl.uniprot.org/annotation/PRO_0000393891|||http://purl.uniprot.org/annotation/PRO_0000393892|||http://purl.uniprot.org/annotation/PRO_0000393893
http://togogenome.org/gene/9606:COL25A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y760|||http://purl.uniprot.org/uniprot/A8MWQ5|||http://purl.uniprot.org/uniprot/Q9BXS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to amyloid-beta peptide.|||Basic and acidic residues|||Cleavage; by furin|||Collagen alpha-1(XXV) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like Alzheimer amyloid plaque component|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In CFEOM5; causes loss of stability; causes incorrect folding.|||In isoform 2.|||In isoform 3.|||Interaction with amyloid-beta peptide|||Not secreted.|||Pro residues|||Pyrrolidone carboxylic acid (Glu)|||Reduces binding to amyloid-beta peptide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259611|||http://purl.uniprot.org/annotation/PRO_0000259612|||http://purl.uniprot.org/annotation/VAR_073325|||http://purl.uniprot.org/annotation/VSP_052197|||http://purl.uniprot.org/annotation/VSP_052198|||http://purl.uniprot.org/annotation/VSP_052199|||http://purl.uniprot.org/annotation/VSP_052200
http://togogenome.org/gene/9606:CERS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G23                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished inhibition by sphingosine-1-phosphate; when associated with A-230.|||Abolished inhibition by sphingosine-1-phosphate; when associated with A-325.|||Ceramide synthase 2|||Cytoplasmic|||Disordered|||Helical|||Homeobox-like|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Strongly decreased phosphorylation leading to reduced ceramide synthase activity.|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185509|||http://purl.uniprot.org/annotation/VAR_052325
http://togogenome.org/gene/9606:ADGRE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JNV7|||http://purl.uniprot.org/uniprot/Q9UHX3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cleavage.|||Adhesion G protein-coupled receptor E2|||Cleavage; by autolysis|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In VBU; affects the regulation of mast cells degranulation; results in increased vibration-induced mast cells degranulation; no effect on localization to plasma membrane.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012875|||http://purl.uniprot.org/annotation/PRO_5014296495|||http://purl.uniprot.org/annotation/VAR_026719|||http://purl.uniprot.org/annotation/VAR_026720|||http://purl.uniprot.org/annotation/VAR_026721|||http://purl.uniprot.org/annotation/VAR_061229|||http://purl.uniprot.org/annotation/VAR_061230|||http://purl.uniprot.org/annotation/VAR_078578|||http://purl.uniprot.org/annotation/VSP_041364|||http://purl.uniprot.org/annotation/VSP_041365|||http://purl.uniprot.org/annotation/VSP_041366|||http://purl.uniprot.org/annotation/VSP_041367|||http://purl.uniprot.org/annotation/VSP_047535
http://togogenome.org/gene/9606:SCGB1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4R6|||http://purl.uniprot.org/uniprot/P11684                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interchain (with C-24)|||Interchain (with C-90)|||Uteroglobin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036365|||http://purl.uniprot.org/annotation/PRO_5006608251|||http://purl.uniprot.org/annotation/VAR_012045|||http://purl.uniprot.org/annotation/VAR_012046
http://togogenome.org/gene/9606:P4HA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13674|||http://purl.uniprot.org/uniprot/Q5VSQ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Fe2OG dioxygenase|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prolyl 4-hydroxylase subunit alpha-1|||Strongly reduced affinity for peptide substrate.|||TPR|||procollagen-proline 4-dioxygenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022723|||http://purl.uniprot.org/annotation/PRO_5014310169|||http://purl.uniprot.org/annotation/VSP_004504|||http://purl.uniprot.org/annotation/VSP_044578
http://togogenome.org/gene/9606:ZFYVE16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3T8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes localization to endosomes and association with PI3P.|||Disordered|||FYVE-type|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger FYVE domain-containing protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098716|||http://purl.uniprot.org/annotation/VAR_019489|||http://purl.uniprot.org/annotation/VAR_019490|||http://purl.uniprot.org/annotation/VAR_019491|||http://purl.uniprot.org/annotation/VAR_057492|||http://purl.uniprot.org/annotation/VAR_057493|||http://purl.uniprot.org/annotation/VAR_069368|||http://purl.uniprot.org/annotation/VSP_011019|||http://purl.uniprot.org/annotation/VSP_011020
http://togogenome.org/gene/9606:RIMKLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  ATP-grasp|||Disordered|||N-acetylaspartylglutamate synthase A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282568
http://togogenome.org/gene/9606:C1orf94                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1W5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Uncharacterized protein C1orf94                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280097|||http://purl.uniprot.org/annotation/VAR_031051|||http://purl.uniprot.org/annotation/VAR_031052|||http://purl.uniprot.org/annotation/VAR_050702|||http://purl.uniprot.org/annotation/VSP_042032
http://togogenome.org/gene/9606:DHPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49366                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Deoxyhypusine synthase|||In NEDSSWI; decreased deoxyhypusine synthase activity.|||In NEDSSWI; loss of deoxyhypusine synthase activity.|||In isoform 3.|||In isoform Short.|||Loss of covalent intermediate formation and deoxyhypusine synthesis.|||Nucleophile|||Phosphoserine|||Reduces covalent intermediate formation and deoxyhypusine synthesis by 99.5%. Retains low spermidine cleavage activity.|||Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis.|||Reduces spermidine binding by 98%. Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate.|||Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate.|||Strongly reduced NAD and spermidine binding. Reduced activity.|||Strongly reduced NAD binding.|||Strongly reduced NAD binding. No effect on enzyme activity.|||Strongly reduced NAD binding. Strongly reduced activity.|||Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate.|||Strongly reduced spermidine binding. Reduced activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134469|||http://purl.uniprot.org/annotation/VAR_043005|||http://purl.uniprot.org/annotation/VAR_082649|||http://purl.uniprot.org/annotation/VAR_082650|||http://purl.uniprot.org/annotation/VSP_001351|||http://purl.uniprot.org/annotation/VSP_047564
http://togogenome.org/gene/9606:OR3A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWB3|||http://purl.uniprot.org/uniprot/P47888                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 3A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150520|||http://purl.uniprot.org/annotation/VAR_054961|||http://purl.uniprot.org/annotation/VAR_054962|||http://purl.uniprot.org/annotation/VAR_054963|||http://purl.uniprot.org/annotation/VAR_054964
http://togogenome.org/gene/9606:PRPF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMS4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  Loss of interaction with the RPA complex and loss of recruitment to sites of DNA damage.|||May mediate interaction with PSMC5|||N-acetylserine|||N6-acetyllysine|||Pre-mRNA-processing factor 19|||Removed|||U-box|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051145
http://togogenome.org/gene/9606:AUP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y679                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  Abolishes interaction with UBE2G2.|||Abolishes lipid droplet localization.|||CUE|||Cytoplasmic|||Disordered|||Disrupts topology with the N-terminus in the lumen instead of the cytoplasm. Abolishes lipid droplet localization and lipid droplet clustering.|||Does not affect lipid droplet localization.|||In isoform 2.|||Lipid droplet-regulating VLDL assembly factor AUP1|||N-acetylmethionine|||No effect on interaction with UBE2G2.|||Phosphoserine|||Phosphothreonine|||Reduced formation of lipid droplets.|||Reduced interaction with ER quality control machinery and misfolded substrates; when associated with 306-K--A-308.|||Reduced interaction with ER quality control machinery and misfolded substrates; when associated with 333-L-L-334 Del.|||Reduced lipid droplet clustering.|||Reduced lipid droplet clustering; when associated with 319-V-E-320 and 333-E-D-334.|||Reduced lipid droplet clustering; when associated with R-316 and 319-V-E-320.|||Reduced lipid droplet clustering; when associated with R-316 and 333-E-D-334.|||Significantly reduced interaction with UBE2G2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020765|||http://purl.uniprot.org/annotation/VSP_059683|||http://purl.uniprot.org/annotation/VSP_059684
http://togogenome.org/gene/9606:PRAMEF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SWL7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||PRAME family member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290166
http://togogenome.org/gene/9606:UQCRFS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47985                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 9|||Cytochrome b-c1 complex subunit Rieske, mitochondrial|||Helical|||In MC3DN10; decreased protein abundance.|||In MC3DN10; loss of localization to mitochondrial inner membrane; the mutant protein is distributed over the entire cytosol and in the nucleus.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Rieske                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030664|||http://purl.uniprot.org/annotation/PRO_0000307241|||http://purl.uniprot.org/annotation/VAR_051863|||http://purl.uniprot.org/annotation/VAR_083879|||http://purl.uniprot.org/annotation/VAR_083880
http://togogenome.org/gene/9606:POMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE0|||http://purl.uniprot.org/uniprot/Q9Y6A1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MDDGA1 and MDDGB1; likely benign variant.|||In MDDGA1.|||In MDDGA1; associated with the loss of function of alpha dystroglycan as a matrix receptor.|||In MDDGA1; severe Walker-Warburg syndrome.|||In MDDGB1.|||In MDDGC1; a common founder mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||MIR|||MIR 1|||MIR 2|||MIR 3|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase 1|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121484|||http://purl.uniprot.org/annotation/VAR_015734|||http://purl.uniprot.org/annotation/VAR_015735|||http://purl.uniprot.org/annotation/VAR_022661|||http://purl.uniprot.org/annotation/VAR_022662|||http://purl.uniprot.org/annotation/VAR_026697|||http://purl.uniprot.org/annotation/VAR_034389|||http://purl.uniprot.org/annotation/VAR_034390|||http://purl.uniprot.org/annotation/VAR_034391|||http://purl.uniprot.org/annotation/VAR_034392|||http://purl.uniprot.org/annotation/VAR_065027|||http://purl.uniprot.org/annotation/VAR_065028|||http://purl.uniprot.org/annotation/VAR_065029|||http://purl.uniprot.org/annotation/VAR_065030|||http://purl.uniprot.org/annotation/VAR_065031|||http://purl.uniprot.org/annotation/VAR_065032|||http://purl.uniprot.org/annotation/VAR_065033|||http://purl.uniprot.org/annotation/VAR_065034|||http://purl.uniprot.org/annotation/VAR_065035|||http://purl.uniprot.org/annotation/VAR_065036|||http://purl.uniprot.org/annotation/VSP_007590|||http://purl.uniprot.org/annotation/VSP_007591|||http://purl.uniprot.org/annotation/VSP_041024
http://togogenome.org/gene/9606:MPZL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60487                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found as a heterozygous variant in a patient with non-syndromic hearing impairment; unknown pathological significance.|||Helical|||Ig-like V-type|||In DFNB111.|||Myelin protein zero-like protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014756|||http://purl.uniprot.org/annotation/VAR_081571|||http://purl.uniprot.org/annotation/VAR_081572|||http://purl.uniprot.org/annotation/VAR_081573
http://togogenome.org/gene/9606:TLE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04727                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q domain|||SP domain|||Transducin-like enhancer protein 4|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051283|||http://purl.uniprot.org/annotation/VSP_030497|||http://purl.uniprot.org/annotation/VSP_030498|||http://purl.uniprot.org/annotation/VSP_055169
http://togogenome.org/gene/9606:TRAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12933                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes 'Lys-63'-linked polyubiquitination.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Important for interaction with BIRC2 and BIRC3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphorylation site. Abolishes activation of NF-kappa-B.|||MATH|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||RING-type|||Reduces global phosphorylation. Partial reduction of TNF-dependent activation of NF-kappa-B and activation of JNK.|||Removed|||Slight increase of TNF-dependent activation of NF-kappa-B and activation of JNK.|||Strongly reduced interaction with BIRC3.|||TNF receptor-associated factor 2|||TRAF-type 1|||TRAF-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056399|||http://purl.uniprot.org/annotation/VSP_007401|||http://purl.uniprot.org/annotation/VSP_039687|||http://purl.uniprot.org/annotation/VSP_039688
http://togogenome.org/gene/9606:DUSP16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY84                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) N6-acetyllysine; by EIS|||Basic and acidic residues|||Disordered|||Dual specificity protein phosphatase 16|||In isoform 2.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094826|||http://purl.uniprot.org/annotation/VAR_051753|||http://purl.uniprot.org/annotation/VAR_051754|||http://purl.uniprot.org/annotation/VSP_056981|||http://purl.uniprot.org/annotation/VSP_056982
http://togogenome.org/gene/9606:CCM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cerebral cavernous malformations 2 protein|||Disordered|||Harmonin homology domain|||In CCM2.|||In CCM2; associated with H-215.|||In CCM2; associated with Q-229.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089424|||http://purl.uniprot.org/annotation/VAR_023575|||http://purl.uniprot.org/annotation/VAR_023576|||http://purl.uniprot.org/annotation/VAR_023577|||http://purl.uniprot.org/annotation/VAR_050768|||http://purl.uniprot.org/annotation/VAR_067352|||http://purl.uniprot.org/annotation/VAR_067353|||http://purl.uniprot.org/annotation/VSP_024402|||http://purl.uniprot.org/annotation/VSP_046695|||http://purl.uniprot.org/annotation/VSP_046696
http://togogenome.org/gene/9606:UBR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT12                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR3|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||RING-type; degenerate|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278184|||http://purl.uniprot.org/annotation/VSP_023141|||http://purl.uniprot.org/annotation/VSP_023142|||http://purl.uniprot.org/annotation/VSP_030354|||http://purl.uniprot.org/annotation/VSP_036405
http://togogenome.org/gene/9606:GSDMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAX9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Abolished ability to mediate pyroptosis.|||Abolished cleavage by granzyme A (GZMA), preventing release of the N-terminal moiety (Gasdermin-B, N-terminal) and ability to induce pyroptosis in target cells of cytotoxic T-cells and natural killer (NK) cells.|||Abolished ubiquitination by S.flexneri IpaH7.8.|||Beta stranded|||Cleavage; by CAPS3, CAPS6 and CAPS9|||Cleavage; by ELANE|||Cleavage; by granzyme A|||Decreased ability to trigger pyroptosis.|||Decreased ability to trigger pyroptosis. Abolished ubiquitination by S.flexneri IpaH7.8.|||Decreased interaction with S.flexneri IpaH7.8.|||Decreased interaction with S.flexneri IpaH7.8. Abolished ubiquitination by S.flexneri IpaH7.8; when associated with A-124.|||Decreased interaction with S.flexneri IpaH7.8. Abolished ubiquitination by S.flexneri IpaH7.8; when associated with A-208.|||Decreased interaction with S.flexneri IpaH7.8. Does not affect ability to trigger pyroptosis.|||Disordered|||Does not abolish ubiquitination by S.flexneri IpaH7.8; when associated with R-166.|||Does not abolish ubiquitination by S.flexneri IpaH7.8; when associated with R-308.|||Does not prevent cleavage by granzyme A (GZMA). Reduced ability to trigger pyroptosis.|||Does not relieve autoinhibition.|||Does not relieve autoinhibition. Relieves autoinhibition; when associated with 339-A--A-343.|||Does not relieve autoinhibition. Relieves autoinhibition; when associated with D-399.|||Gasdermin-B|||Gasdermin-B, C-terminal|||Gasdermin-B, N-terminal|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6 and isoform 1.|||Reduced ability to trigger pyroptosis.|||Reduced ability to trigger pyroptosis; when associated with A-26.|||Reduced ability to trigger pyroptosis; when associated with A-51.|||Relieves autoinhibition.|||Slightly decreased formation of pore.|||Triggers pyroptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329058|||http://purl.uniprot.org/annotation/PRO_0000451672|||http://purl.uniprot.org/annotation/PRO_0000451673|||http://purl.uniprot.org/annotation/VAR_042632|||http://purl.uniprot.org/annotation/VAR_042633|||http://purl.uniprot.org/annotation/VAR_042634|||http://purl.uniprot.org/annotation/VAR_042635|||http://purl.uniprot.org/annotation/VAR_042636|||http://purl.uniprot.org/annotation/VAR_042637|||http://purl.uniprot.org/annotation/VSP_061486|||http://purl.uniprot.org/annotation/VSP_061487|||http://purl.uniprot.org/annotation/VSP_061488|||http://purl.uniprot.org/annotation/VSP_061489|||http://purl.uniprot.org/annotation/VSP_061490
http://togogenome.org/gene/9606:SPAST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KRP5|||http://purl.uniprot.org/uniprot/E5KRP6|||http://purl.uniprot.org/uniprot/Q9UBP0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Abolishes ATPase activity.|||Abolishes localization to lipid droplets.|||Abrogates ATP hydrolysis, abolishes microtubule severing, stabilizes the homohexameric form, and promotes microtubule binding and redistribution from the endosome to microtubules.|||Abrogates ATPase activity and abolishes microtubule severing.|||Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin and abolishes microtubule severing.|||Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.|||Acts as a disease modifier; patients carrying a mutated allele of spastin and L-44 on the other allele are affected by severe spastic paraplegia with an early age of onset; may decrease the activity of the alternative promoter which directs the synthesis of isoform 3 and isoform 4.|||Acts as a disease modifier; patients carrying a mutated allele of spastin and Q-45 on the other allele are affected by severe spastic paraplegia with an early age of onset.|||Cytoplasmic|||Cytoplasmic and nuclear.|||Disordered|||Does not affect ATPase activity.|||Does not affect localization to lipid droplets.|||Exclusively cytoplasmic.|||Helical|||Impairs binding to CHMP1B.|||Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-120.|||Impairs binding to CHMP1B. Impairs midbody localization; when associated with D-124.|||In SPG4.|||In SPG4; abrogates ATPase activity and promotes microtubule binding.|||In SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles and impairs traffic from the ER to Golgi.|||In SPG4; abrogates ATPase activity, promotes microtubule binding and the formation of thick microtubule bundles.|||In SPG4; abrogates binding to the tail of beta-3-tubulin, abolishes microtubule severing and promotes the formation of thick microtubule bundles.|||In SPG4; likely benign variant.|||In SPG4; promotes microtubule binding and the formation of thick microtubule bundles.|||In SPG4; promotes microtubule binding.|||In SPG4; requires 2 nucleotide substitutions.|||In SPG4; unknown pathological significance.|||In SPG4; variant form with congenital arachnoid cysts.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Loss of microtubule-binding.|||MIT|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with ATL1|||Required for interaction with RTN1|||Required for interaction with SSNA1 and microtubules|||Required for interaction with microtubules|||Required for interaction with microtubules and microtubule severing|||Required for midbody localization|||Required for nuclear localization|||Spastin|||Sufficient for interaction with CHMP1B|||Sufficient for microtubule severing                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084763|||http://purl.uniprot.org/annotation/VAR_010194|||http://purl.uniprot.org/annotation/VAR_010195|||http://purl.uniprot.org/annotation/VAR_010196|||http://purl.uniprot.org/annotation/VAR_010197|||http://purl.uniprot.org/annotation/VAR_010198|||http://purl.uniprot.org/annotation/VAR_010199|||http://purl.uniprot.org/annotation/VAR_019439|||http://purl.uniprot.org/annotation/VAR_019440|||http://purl.uniprot.org/annotation/VAR_019441|||http://purl.uniprot.org/annotation/VAR_019442|||http://purl.uniprot.org/annotation/VAR_019443|||http://purl.uniprot.org/annotation/VAR_019444|||http://purl.uniprot.org/annotation/VAR_019445|||http://purl.uniprot.org/annotation/VAR_019448|||http://purl.uniprot.org/annotation/VAR_019449|||http://purl.uniprot.org/annotation/VAR_019450|||http://purl.uniprot.org/annotation/VAR_019451|||http://purl.uniprot.org/annotation/VAR_019452|||http://purl.uniprot.org/annotation/VAR_026758|||http://purl.uniprot.org/annotation/VAR_026759|||http://purl.uniprot.org/annotation/VAR_026760|||http://purl.uniprot.org/annotation/VAR_026761|||http://purl.uniprot.org/annotation/VAR_026762|||http://purl.uniprot.org/annotation/VAR_026763|||http://purl.uniprot.org/annotation/VAR_027205|||http://purl.uniprot.org/annotation/VAR_027206|||http://purl.uniprot.org/annotation/VAR_027207|||http://purl.uniprot.org/annotation/VAR_027208|||http://purl.uniprot.org/annotation/VAR_027209|||http://purl.uniprot.org/annotation/VAR_027210|||http://purl.uniprot.org/annotation/VAR_027211|||http://purl.uniprot.org/annotation/VAR_027212|||http://purl.uniprot.org/annotation/VAR_027213|||http://purl.uniprot.org/annotation/VAR_027214|||http://purl.uniprot.org/annotation/VAR_027215|||http://purl.uniprot.org/annotation/VAR_027216|||http://purl.uniprot.org/annotation/VAR_027217|||http://purl.uniprot.org/annotation/VAR_027218|||http://purl.uniprot.org/annotation/VAR_027219|||http://purl.uniprot.org/annotation/VAR_027220|||http://purl.uniprot.org/annotation/VAR_027221|||http://purl.uniprot.org/annotation/VAR_027222|||http://purl.uniprot.org/annotation/VAR_027223|||http://purl.uniprot.org/annotation/VAR_027224|||http://purl.uniprot.org/annotation/VAR_027225|||http://purl.uniprot.org/annotation/VAR_027226|||http://purl.uniprot.org/annotation/VAR_027227|||http://purl.uniprot.org/annotation/VAR_027228|||http://purl.uniprot.org/annotation/VAR_035902|||http://purl.uniprot.org/annotation/VAR_067563|||http://purl.uniprot.org/annotation/VAR_067564|||http://purl.uniprot.org/annotation/VAR_067565|||http://purl.uniprot.org/annotation/VAR_067566|||http://purl.uniprot.org/annotation/VAR_067567|||http://purl.uniprot.org/annotation/VAR_067568|||http://purl.uniprot.org/annotation/VAR_067569|||http://purl.uniprot.org/annotation/VAR_067570|||http://purl.uniprot.org/annotation/VAR_067571|||http://purl.uniprot.org/annotation/VAR_067572|||http://purl.uniprot.org/annotation/VAR_067573|||http://purl.uniprot.org/annotation/VAR_067574|||http://purl.uniprot.org/annotation/VAR_067575|||http://purl.uniprot.org/annotation/VAR_067576|||http://purl.uniprot.org/annotation/VAR_067628|||http://purl.uniprot.org/annotation/VAR_067629|||http://purl.uniprot.org/annotation/VAR_067630|||http://purl.uniprot.org/annotation/VAR_067631|||http://purl.uniprot.org/annotation/VAR_067632|||http://purl.uniprot.org/annotation/VAR_067633|||http://purl.uniprot.org/annotation/VAR_067634|||http://purl.uniprot.org/annotation/VAR_067635|||http://purl.uniprot.org/annotation/VAR_067636|||http://purl.uniprot.org/annotation/VAR_067637|||http://purl.uniprot.org/annotation/VAR_067638|||http://purl.uniprot.org/annotation/VAR_067639|||http://purl.uniprot.org/annotation/VAR_067640|||http://purl.uniprot.org/annotation/VAR_067641|||http://purl.uniprot.org/annotation/VAR_067642|||http://purl.uniprot.org/annotation/VAR_067643|||http://purl.uniprot.org/annotation/VAR_067644|||http://purl.uniprot.org/annotation/VAR_067645|||http://purl.uniprot.org/annotation/VAR_067646|||http://purl.uniprot.org/annotation/VAR_067647|||http://purl.uniprot.org/annotation/VAR_067648|||http://purl.uniprot.org/annotation/VAR_067649|||http://purl.uniprot.org/annotation/VAR_067650|||http://purl.uniprot.org/annotation/VAR_067651|||http://purl.uniprot.org/annotation/VAR_067652|||http://purl.uniprot.org/annotation/VAR_067653|||http://purl.uniprot.org/annotation/VAR_067654|||http://purl.uniprot.org/annotation/VAR_075827|||http://purl.uniprot.org/annotation/VAR_075828|||http://purl.uniprot.org/annotation/VAR_075829|||http://purl.uniprot.org/annotation/VAR_075830|||http://purl.uniprot.org/annotation/VAR_075831|||http://purl.uniprot.org/annotation/VAR_075832|||http://purl.uniprot.org/annotation/VAR_075833|||http://purl.uniprot.org/annotation/VAR_075834|||http://purl.uniprot.org/annotation/VAR_075835|||http://purl.uniprot.org/annotation/VAR_075836|||http://purl.uniprot.org/annotation/VAR_075837|||http://purl.uniprot.org/annotation/VAR_075838|||http://purl.uniprot.org/annotation/VAR_075839|||http://purl.uniprot.org/annotation/VAR_075840|||http://purl.uniprot.org/annotation/VAR_075841|||http://purl.uniprot.org/annotation/VAR_075842|||http://purl.uniprot.org/annotation/VAR_075843|||http://purl.uniprot.org/annotation/VAR_075844|||http://purl.uniprot.org/annotation/VAR_075845|||http://purl.uniprot.org/annotation/VAR_075846|||http://purl.uniprot.org/annotation/VAR_075847|||http://purl.uniprot.org/annotation/VAR_075848|||http://purl.uniprot.org/annotation/VAR_075849|||http://purl.uniprot.org/annotation/VAR_075850|||http://purl.uniprot.org/annotation/VAR_075851|||http://purl.uniprot.org/annotation/VAR_075852|||http://purl.uniprot.org/annotation/VAR_079314|||http://purl.uniprot.org/annotation/VAR_079315|||http://purl.uniprot.org/annotation/VAR_079316|||http://purl.uniprot.org/annotation/VAR_079317|||http://purl.uniprot.org/annotation/VAR_079318|||http://purl.uniprot.org/annotation/VAR_079319|||http://purl.uniprot.org/annotation/VAR_079320|||http://purl.uniprot.org/annotation/VAR_079321|||http://purl.uniprot.org/annotation/VAR_079322|||http://purl.uniprot.org/annotation/VAR_079323|||http://purl.uniprot.org/annotation/VAR_079324|||http://purl.uniprot.org/annotation/VSP_000024|||http://purl.uniprot.org/annotation/VSP_036650
http://togogenome.org/gene/9606:EIF4H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15056                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 4H|||HHV-1 Vhs binding site|||In isoform Short.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081619|||http://purl.uniprot.org/annotation/VSP_005799
http://togogenome.org/gene/9606:DOK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP83|||http://purl.uniprot.org/uniprot/B4DJN1|||http://purl.uniprot.org/uniprot/Q14CB2|||http://purl.uniprot.org/uniprot/Q2TA81|||http://purl.uniprot.org/uniprot/Q99704                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Docking protein 1|||IRS-type PTB|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||No association with GAP; when associated with F-362.|||No association with NCK. No association with GAP; when associated with F-398.|||PH|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by INSR|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187268|||http://purl.uniprot.org/annotation/VSP_003852|||http://purl.uniprot.org/annotation/VSP_003853|||http://purl.uniprot.org/annotation/VSP_038224
http://togogenome.org/gene/9606:OR2L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWR8|||http://purl.uniprot.org/uniprot/Q8NG80                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2L5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150488
http://togogenome.org/gene/9606:SUMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBK3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Formylglycine-generating enzyme|||In MSD.|||In MSD; almost abolished enzyme activity.|||In MSD; decreases its specific enzyme activity to less than 3%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type.|||In MSD; loss of activity.|||In MSD; loss of activity; decreases its specific enzyme activity to about 23%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is decreased.|||In MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is almost comparable to wild-type.|||In MSD; loss of activity; decreases its specific enzyme activity to less than 1%; does not affect localization of the protein in the endoplasmic reticulum of MSD fibroblasts; protein stability is severely decreased.|||In MSD; loss of enzyme activity.|||In MSD; mild phenotype; reduced but not abolished activity.|||In MSD; reduced but not abolished activity.|||In MSD; retains some activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with sulfatases|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||No effect.|||Reduces activity 5-fold.|||Reduces activity by 99%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033456|||http://purl.uniprot.org/annotation/VAR_016052|||http://purl.uniprot.org/annotation/VAR_016053|||http://purl.uniprot.org/annotation/VAR_016054|||http://purl.uniprot.org/annotation/VAR_016055|||http://purl.uniprot.org/annotation/VAR_016056|||http://purl.uniprot.org/annotation/VAR_016057|||http://purl.uniprot.org/annotation/VAR_016058|||http://purl.uniprot.org/annotation/VAR_016059|||http://purl.uniprot.org/annotation/VAR_016060|||http://purl.uniprot.org/annotation/VAR_019050|||http://purl.uniprot.org/annotation/VAR_019051|||http://purl.uniprot.org/annotation/VAR_019052|||http://purl.uniprot.org/annotation/VAR_019053|||http://purl.uniprot.org/annotation/VAR_019054|||http://purl.uniprot.org/annotation/VAR_042602|||http://purl.uniprot.org/annotation/VAR_080468|||http://purl.uniprot.org/annotation/VAR_080469|||http://purl.uniprot.org/annotation/VAR_080470|||http://purl.uniprot.org/annotation/VSP_007877|||http://purl.uniprot.org/annotation/VSP_013185|||http://purl.uniprot.org/annotation/VSP_045414|||http://purl.uniprot.org/annotation/VSP_045415
http://togogenome.org/gene/9606:RAB36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95755                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Effector region|||In isoform 2.|||Ras-related protein Rab-36|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121248|||http://purl.uniprot.org/annotation/VAR_024189|||http://purl.uniprot.org/annotation/VAR_034433|||http://purl.uniprot.org/annotation/VAR_051715|||http://purl.uniprot.org/annotation/VSP_010143
http://togogenome.org/gene/9606:LRP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZR2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12; calcium-binding|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 20|||EGF-like 21|||EGF-like 22|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Endocytosis signal|||Extracellular|||Helical|||In NSCLC cells.|||LDL-receptor class A 1|||LDL-receptor class A 10|||LDL-receptor class A 11|||LDL-receptor class A 12|||LDL-receptor class A 13|||LDL-receptor class A 14|||LDL-receptor class A 15|||LDL-receptor class A 16|||LDL-receptor class A 17|||LDL-receptor class A 18|||LDL-receptor class A 19|||LDL-receptor class A 2|||LDL-receptor class A 20|||LDL-receptor class A 21|||LDL-receptor class A 22|||LDL-receptor class A 23|||LDL-receptor class A 24|||LDL-receptor class A 25|||LDL-receptor class A 26|||LDL-receptor class A 27|||LDL-receptor class A 28|||LDL-receptor class A 29|||LDL-receptor class A 3|||LDL-receptor class A 30|||LDL-receptor class A 31|||LDL-receptor class A 32|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class A 9|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 21|||LDL-receptor class B 22|||LDL-receptor class B 23|||LDL-receptor class B 24|||LDL-receptor class B 25|||LDL-receptor class B 26|||LDL-receptor class B 27|||LDL-receptor class B 28|||LDL-receptor class B 29|||LDL-receptor class B 3|||LDL-receptor class B 30|||LDL-receptor class B 31|||LDL-receptor class B 32|||LDL-receptor class B 33|||LDL-receptor class B 34|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Low-density lipoprotein receptor-related protein 1B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017319|||http://purl.uniprot.org/annotation/VAR_018328|||http://purl.uniprot.org/annotation/VAR_049759|||http://purl.uniprot.org/annotation/VAR_049760|||http://purl.uniprot.org/annotation/VAR_049761|||http://purl.uniprot.org/annotation/VAR_049762|||http://purl.uniprot.org/annotation/VAR_049763
http://togogenome.org/gene/9606:PXDNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1KZ92                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||In isoform PMR1.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Probable oxidoreductase PXDNL|||Proton acceptor|||Transition state stabilizer|||VWFC|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330731|||http://purl.uniprot.org/annotation/VAR_050488|||http://purl.uniprot.org/annotation/VAR_050489|||http://purl.uniprot.org/annotation/VAR_050490|||http://purl.uniprot.org/annotation/VAR_050491|||http://purl.uniprot.org/annotation/VAR_050492|||http://purl.uniprot.org/annotation/VAR_050493|||http://purl.uniprot.org/annotation/VAR_050494|||http://purl.uniprot.org/annotation/VSP_033070|||http://purl.uniprot.org/annotation/VSP_033071|||http://purl.uniprot.org/annotation/VSP_044240|||http://purl.uniprot.org/annotation/VSP_044241
http://togogenome.org/gene/9606:GAK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DS37|||http://purl.uniprot.org/uniprot/O14976                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2 tensin-type|||Cyclin-G-associated kinase|||Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||J|||N-acetylserine|||Omega-N-methylarginine|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085958|||http://purl.uniprot.org/annotation/VAR_040505|||http://purl.uniprot.org/annotation/VAR_040506|||http://purl.uniprot.org/annotation/VAR_040507|||http://purl.uniprot.org/annotation/VAR_040508|||http://purl.uniprot.org/annotation/VAR_040509|||http://purl.uniprot.org/annotation/VAR_040510|||http://purl.uniprot.org/annotation/VAR_040511|||http://purl.uniprot.org/annotation/VAR_040512|||http://purl.uniprot.org/annotation/VAR_040513|||http://purl.uniprot.org/annotation/VAR_040514|||http://purl.uniprot.org/annotation/VAR_040515|||http://purl.uniprot.org/annotation/VSP_054479
http://togogenome.org/gene/9606:TMEM25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1M8|||http://purl.uniprot.org/uniprot/E9PKP3|||http://purl.uniprot.org/uniprot/Q86YD3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014984|||http://purl.uniprot.org/annotation/PRO_5002866118|||http://purl.uniprot.org/annotation/PRO_5003242838|||http://purl.uniprot.org/annotation/VAR_021391|||http://purl.uniprot.org/annotation/VAR_033623|||http://purl.uniprot.org/annotation/VSP_012939|||http://purl.uniprot.org/annotation/VSP_012940|||http://purl.uniprot.org/annotation/VSP_012941|||http://purl.uniprot.org/annotation/VSP_045635
http://togogenome.org/gene/9606:AMELX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99217                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Amelogenin, X isoform|||Disordered|||In AI1E.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001199|||http://purl.uniprot.org/annotation/VAR_000559|||http://purl.uniprot.org/annotation/VAR_037581|||http://purl.uniprot.org/annotation/VAR_037582|||http://purl.uniprot.org/annotation/VAR_037583|||http://purl.uniprot.org/annotation/VSP_000228|||http://purl.uniprot.org/annotation/VSP_000229
http://togogenome.org/gene/9606:RUVBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTR5|||http://purl.uniprot.org/uniprot/B3KRS7|||http://purl.uniprot.org/uniprot/E7ETR0|||http://purl.uniprot.org/uniprot/Q9Y265                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine|||No effect on interaction with NOPCHAP1.|||Reduces ATPase activity. Decreases interaction with NOPCHAP1. No effect on formation of RUVBL1-RUVBL2 heteromeric complex.|||RuvB-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165639|||http://purl.uniprot.org/annotation/VSP_021387|||http://purl.uniprot.org/annotation/VSP_021388
http://togogenome.org/gene/9606:HSPB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Heat shock protein beta-7|||In isoform 2.|||In isoform 3.|||Polar residues|||Required for localization to SC35 splicing speckles|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125941|||http://purl.uniprot.org/annotation/VSP_002424|||http://purl.uniprot.org/annotation/VSP_002425|||http://purl.uniprot.org/annotation/VSP_002426
http://togogenome.org/gene/9606:SALL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Sal-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047020|||http://purl.uniprot.org/annotation/VAR_013155|||http://purl.uniprot.org/annotation/VAR_013156|||http://purl.uniprot.org/annotation/VAR_013157|||http://purl.uniprot.org/annotation/VAR_013158|||http://purl.uniprot.org/annotation/VAR_013159|||http://purl.uniprot.org/annotation/VSP_040502
http://togogenome.org/gene/9606:OR8U1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH10                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8U1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150675|||http://purl.uniprot.org/annotation/VAR_053247|||http://purl.uniprot.org/annotation/VAR_053248|||http://purl.uniprot.org/annotation/VAR_053249|||http://purl.uniprot.org/annotation/VAR_053250|||http://purl.uniprot.org/annotation/VAR_053251|||http://purl.uniprot.org/annotation/VAR_053252|||http://purl.uniprot.org/annotation/VAR_060014|||http://purl.uniprot.org/annotation/VAR_060015|||http://purl.uniprot.org/annotation/VAR_060016
http://togogenome.org/gene/9606:FAM241B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D05                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Protein FAM241B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089790|||http://purl.uniprot.org/annotation/VSP_042153
http://togogenome.org/gene/9606:ZNF823                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16415                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 823                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047778|||http://purl.uniprot.org/annotation/VAR_052909|||http://purl.uniprot.org/annotation/VSP_055972
http://togogenome.org/gene/9606:PHF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Essential to induce neural progenitor proliferation|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||PHD finger protein 10|||PHD-type 1; degenerate|||PHD-type 2; degenerate|||Phosphoserine|||Polar residues|||Removed|||SAY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059297|||http://purl.uniprot.org/annotation/VSP_013440|||http://purl.uniprot.org/annotation/VSP_039090
http://togogenome.org/gene/9606:DEFB103A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A894JZ42|||http://purl.uniprot.org/uniprot/P81534                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Peptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Peptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-defensin 103                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006971|||http://purl.uniprot.org/annotation/PRO_5032611455
http://togogenome.org/gene/9606:WDR20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A088AWN2|||http://purl.uniprot.org/uniprot/Q5JPH5|||http://purl.uniprot.org/uniprot/Q8TBZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Impaired binding to USP12.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 7.|||In isoform 8.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051366|||http://purl.uniprot.org/annotation/VAR_031580|||http://purl.uniprot.org/annotation/VAR_053425|||http://purl.uniprot.org/annotation/VSP_024387|||http://purl.uniprot.org/annotation/VSP_043412|||http://purl.uniprot.org/annotation/VSP_043413|||http://purl.uniprot.org/annotation/VSP_045225|||http://purl.uniprot.org/annotation/VSP_045226|||http://purl.uniprot.org/annotation/VSP_047064|||http://purl.uniprot.org/annotation/VSP_047065
http://togogenome.org/gene/9606:B4GALT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XA83|||http://purl.uniprot.org/uniprot/Q59GB5|||http://purl.uniprot.org/uniprot/Q8WZ95|||http://purl.uniprot.org/uniprot/Q9UBX8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 6|||Cytoplasmic|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080547|||http://purl.uniprot.org/annotation/VAR_054023|||http://purl.uniprot.org/annotation/VSP_056554
http://togogenome.org/gene/9606:SLC38A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVK8|||http://purl.uniprot.org/uniprot/Q8NBW4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes arginine transport. No effect on subcellular location and interaction with Ragulator complex.|||Abolishes association with the Ragulator complex.|||Abolishes association with the Ragulator complex. Abolishes the interaction with the Rag GTPases heterodimer complex.|||Abolishes association with the Ragulator complex. No effect on amino acid transport activity. Abolishes the interaction with the Rag GTPases heterodimer complex.|||Abolishes cholesterol binding; when associated with I-460. Does not affect disrupted arginine-mediated activation of mTORC1; when associated with I-460. Does not affect lysosomal localization; when associated with I-460. Increases interactions with both Rag GTPase and Ragulator subunits; when associated with I-460. Loss of L-glutamine transport stimulation by cholesterol.|||Abolishes interaction with the Ragulator and Rag GTPases complexes.|||Amino acid transporter transmembrane|||CARC motif|||CRAC motif|||Cytoplasmic|||Decreases cholesterol binding. Abolishes cholesterol binding; when associated with I-449. Does not affect disrupted arginine-mediated activation of mTORC1; when associated with I-449. Does not affect lysosomal localization; when associated with I-449. Increases interactions with both Rag GTPase and Ragulator subunits; when associated with I-449. Loss of L-glutamine transport stimulation by cholesterol.|||Disordered|||Does not affect L-glutamine transport activity.|||Does not affect association with the Ragulator complex. Abolishes the interaction with the Rag GTPases heterodimer complex.|||Does not affect interaction with the Ragulator and Rag GTPases complexes.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Important for arginine binding and amino acid transport|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Moderately affects amino acid transport.|||N-linked (GlcNAc...) asparagine|||Neutral amino acid transporter 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328840|||http://purl.uniprot.org/annotation/VAR_042546|||http://purl.uniprot.org/annotation/VSP_032815|||http://purl.uniprot.org/annotation/VSP_045110|||http://purl.uniprot.org/annotation/VSP_045111|||http://purl.uniprot.org/annotation/VSP_045112
http://togogenome.org/gene/9606:PLXNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43157                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by proprotein convertases.|||Abolishes interaction with RAC1 and RND1.|||Cleavage; by proprotein convertases|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||Important for interaction with RAC1 and RND1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of cytoskeleton remodeling in response to SEMA4D.|||N-linked (GlcNAc...) asparagine|||Plexin-B1|||Polar residues|||Pro residues|||Sema|||Strongly reduced interaction with SEMA4D.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024671|||http://purl.uniprot.org/annotation/VAR_036074|||http://purl.uniprot.org/annotation/VAR_050598|||http://purl.uniprot.org/annotation/VAR_050599|||http://purl.uniprot.org/annotation/VSP_011513|||http://purl.uniprot.org/annotation/VSP_011514|||http://purl.uniprot.org/annotation/VSP_011515
http://togogenome.org/gene/9606:EPOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||BC-box|||Disordered|||Elongin BC and Polycomb repressive complex 2-associated protein|||Interaction with SUZ12|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332154
http://togogenome.org/gene/9606:CCDC112                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEF3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 112|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320160|||http://purl.uniprot.org/annotation/VAR_039147|||http://purl.uniprot.org/annotation/VAR_039148|||http://purl.uniprot.org/annotation/VAR_039149|||http://purl.uniprot.org/annotation/VAR_039150|||http://purl.uniprot.org/annotation/VSP_031624
http://togogenome.org/gene/9606:MCM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49736                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Arginine finger|||Basic and acidic residues|||C4-type|||DNA replication licensing factor MCM2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139.|||Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41.|||Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139.|||In DFNA70; increases the apoptotic process; no effect on cell proliferation and cell cycle phase.|||Interaction with DNJC9|||Interaction with KAT7|||Loss of interaction with DNAJC9.|||MCM|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ATR|||Phosphoserine; by CDC7|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduces phosphorylation by ATR.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194087|||http://purl.uniprot.org/annotation/VAR_016137|||http://purl.uniprot.org/annotation/VAR_016138|||http://purl.uniprot.org/annotation/VAR_016139|||http://purl.uniprot.org/annotation/VAR_021111|||http://purl.uniprot.org/annotation/VAR_021112|||http://purl.uniprot.org/annotation/VAR_033298|||http://purl.uniprot.org/annotation/VAR_033299|||http://purl.uniprot.org/annotation/VAR_077049
http://togogenome.org/gene/9606:TMEM132A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q24JP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Binds to HSPA5/GRP78|||Confers cellular localization similar to full-length form|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Transmembrane protein 132A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287096|||http://purl.uniprot.org/annotation/VAR_032262|||http://purl.uniprot.org/annotation/VAR_032263|||http://purl.uniprot.org/annotation/VSP_025302|||http://purl.uniprot.org/annotation/VSP_025303|||http://purl.uniprot.org/annotation/VSP_025304|||http://purl.uniprot.org/annotation/VSP_025305|||http://purl.uniprot.org/annotation/VSP_025306
http://togogenome.org/gene/9606:DDX28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUL7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Variant                                                                                  ^@                                                                                  DEAD|||Helicase ATP-binding|||Helicase C-terminal|||Mitochondrial targeting signal|||Nuclear export signal|||Nuclear localization signal|||Probable ATP-dependent RNA helicase DDX28|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055033|||http://purl.uniprot.org/annotation/VAR_052163
http://togogenome.org/gene/9606:TRIM13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7MTJ6|||http://purl.uniprot.org/uniprot/O60858                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Absence of polyubiquitination. Stability of protein increased. No enhanced apoptosis on ionizing radiation induction. No ubiquitination of AKT1 or MDM2. Decreased p53/TP53 stability. No effect on induction of autophagy during ER stress.|||B box-type|||BTB|||E3 ubiquitin-protein ligase TRIM13|||Helical|||In isoform 2.|||In isoform 3.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056028|||http://purl.uniprot.org/annotation/VAR_013512|||http://purl.uniprot.org/annotation/VSP_005746|||http://purl.uniprot.org/annotation/VSP_005747|||http://purl.uniprot.org/annotation/VSP_038142
http://togogenome.org/gene/9606:NDUFV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56181                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020025|||http://purl.uniprot.org/annotation/VSP_038552
http://togogenome.org/gene/9606:SYCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZC3|||http://purl.uniprot.org/uniprot/B7ZLS9|||http://purl.uniprot.org/uniprot/Q15431                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DNA-binding|||Enables C-terminal tetrameric self-assembly at pH 8.0; when associated with F-721.|||Enables C-terminal tetrameric self-assembly at pH 8.0; when associated with W-717.|||Impairs pH-induced C-terminal tetrameric self-assembly.|||Impairs pH-induced C-terminal tetrameric self-assembly; when associated with A-679.|||Impairs pH-induced C-terminal tetrameric self-assembly; when associated with A-688.|||Impairs self-assembly of N-terminal ends.|||Impairs self-assembly of N-terminal ends; when associated with E-105.|||Impairs self-assembly of N-terminal ends; when associated with E-109.|||Mediates head to head self-assembly of N-terminal ends|||Nuclear localization signal|||Required for pH-induced assembly of C-terminal ends into antiparallel tetramers|||Synaptonemal complex protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072362|||http://purl.uniprot.org/annotation/VAR_046993|||http://purl.uniprot.org/annotation/VAR_046994
http://togogenome.org/gene/9606:TMEM240                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SV17                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In SCA21.|||Phosphoserine|||Transmembrane protein 240                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340728|||http://purl.uniprot.org/annotation/VAR_071906|||http://purl.uniprot.org/annotation/VAR_071907|||http://purl.uniprot.org/annotation/VAR_071908|||http://purl.uniprot.org/annotation/VAR_071909|||http://purl.uniprot.org/annotation/VAR_071910
http://togogenome.org/gene/9606:SERPINA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U17                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Serpin A11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041973|||http://purl.uniprot.org/annotation/VAR_034511|||http://purl.uniprot.org/annotation/VAR_061791
http://togogenome.org/gene/9606:CCDC184                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52MB2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 184|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335681|||http://purl.uniprot.org/annotation/VAR_060278
http://togogenome.org/gene/9606:TBL1XR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JLJ1|||http://purl.uniprot.org/uniprot/Q9BZK7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||F-box-like|||F-box-like/WD repeat-containing protein TBL1XR1|||Found in a patient with epilepsy; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRD41.|||In PRPTS; does not affect assembly into the N-Cor repressor complex.|||LisH|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051266|||http://purl.uniprot.org/annotation/VAR_076753|||http://purl.uniprot.org/annotation/VAR_076754|||http://purl.uniprot.org/annotation/VAR_076755|||http://purl.uniprot.org/annotation/VAR_076756|||http://purl.uniprot.org/annotation/VAR_076757|||http://purl.uniprot.org/annotation/VAR_076758|||http://purl.uniprot.org/annotation/VAR_076759
http://togogenome.org/gene/9606:TSPAN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62079                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219243
http://togogenome.org/gene/9606:ADAMTS18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VYF7|||http://purl.uniprot.org/uniprot/Q6ZN25|||http://purl.uniprot.org/uniprot/Q8TE60                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 18|||Cysteine switch|||Disintegrin|||Disordered|||Helical|||In MMCAT.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029200|||http://purl.uniprot.org/annotation/PRO_0000042163|||http://purl.uniprot.org/annotation/VAR_036152|||http://purl.uniprot.org/annotation/VAR_036153|||http://purl.uniprot.org/annotation/VAR_057083|||http://purl.uniprot.org/annotation/VAR_057084|||http://purl.uniprot.org/annotation/VAR_057085|||http://purl.uniprot.org/annotation/VAR_057086|||http://purl.uniprot.org/annotation/VAR_060231|||http://purl.uniprot.org/annotation/VAR_060232|||http://purl.uniprot.org/annotation/VAR_066554|||http://purl.uniprot.org/annotation/VAR_070849|||http://purl.uniprot.org/annotation/VAR_070850|||http://purl.uniprot.org/annotation/VSP_015776|||http://purl.uniprot.org/annotation/VSP_015777
http://togogenome.org/gene/9606:HS3ST5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZT8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 5|||Loss of enzyme activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Reduces enzyme activity by 93%,.|||Reduces enzyme activity by 98%.|||Reduces enzyme activity by over 99%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085222|||http://purl.uniprot.org/annotation/VAR_052531
http://togogenome.org/gene/9606:CDK18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07002|||http://purl.uniprot.org/uniprot/Q59G02                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 18|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086490|||http://purl.uniprot.org/annotation/VAR_047802|||http://purl.uniprot.org/annotation/VAR_047803|||http://purl.uniprot.org/annotation/VAR_047804|||http://purl.uniprot.org/annotation/VSP_035889
http://togogenome.org/gene/9606:KIR3DL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43629|||http://purl.uniprot.org/uniprot/Q5UCE2|||http://purl.uniprot.org/uniprot/Q8N6C9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Immunoglobulin subtype|||In isoform 2.|||Killer cell immunoglobulin-like receptor 3DL1|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015087|||http://purl.uniprot.org/annotation/PRO_5010140726|||http://purl.uniprot.org/annotation/PRO_5014312250|||http://purl.uniprot.org/annotation/VAR_010319|||http://purl.uniprot.org/annotation/VAR_010320|||http://purl.uniprot.org/annotation/VAR_010321|||http://purl.uniprot.org/annotation/VAR_010322|||http://purl.uniprot.org/annotation/VAR_010323|||http://purl.uniprot.org/annotation/VAR_010324|||http://purl.uniprot.org/annotation/VAR_010336|||http://purl.uniprot.org/annotation/VAR_049987|||http://purl.uniprot.org/annotation/VAR_049988|||http://purl.uniprot.org/annotation/VAR_049989|||http://purl.uniprot.org/annotation/VAR_049990|||http://purl.uniprot.org/annotation/VSP_047633
http://togogenome.org/gene/9606:GLYAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5E3|||http://purl.uniprot.org/uniprot/Q6IB77                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycine N-acyltransferase|||Glycine N-acyltransferase C-terminal|||Glycine N-acyltransferase N-terminal|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281869|||http://purl.uniprot.org/annotation/VAR_031294|||http://purl.uniprot.org/annotation/VAR_031295|||http://purl.uniprot.org/annotation/VSP_024073|||http://purl.uniprot.org/annotation/VSP_024074
http://togogenome.org/gene/9606:CLIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG6|||http://purl.uniprot.org/uniprot/A7E2F7|||http://purl.uniprot.org/uniprot/Q9UDT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CAP-Gly|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly domain-containing linker protein 2|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083515|||http://purl.uniprot.org/annotation/VAR_023618|||http://purl.uniprot.org/annotation/VAR_055636|||http://purl.uniprot.org/annotation/VSP_015682
http://togogenome.org/gene/9606:AHSG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02765                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Alpha-2-HS-glycoprotein chain A|||Alpha-2-HS-glycoprotein chain B|||Connecting peptide|||Cystatin fetuin-A-type 1|||Cystatin fetuin-A-type 2|||Disordered|||In APMR1; unknown pathological significance.|||In allele AHSG*1.|||In allele AHSG*3.|||In allele AHSG*5.|||Interchain (between A and B chains)|||N-linked (GlcNAc...) (complex) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000064|||http://purl.uniprot.org/annotation/CAR_000065|||http://purl.uniprot.org/annotation/CAR_000067|||http://purl.uniprot.org/annotation/CAR_000068|||http://purl.uniprot.org/annotation/PRO_0000008887|||http://purl.uniprot.org/annotation/PRO_0000008888|||http://purl.uniprot.org/annotation/PRO_0000008889|||http://purl.uniprot.org/annotation/VAR_002388|||http://purl.uniprot.org/annotation/VAR_002389|||http://purl.uniprot.org/annotation/VAR_012474|||http://purl.uniprot.org/annotation/VAR_012475|||http://purl.uniprot.org/annotation/VAR_055802|||http://purl.uniprot.org/annotation/VAR_080645
http://togogenome.org/gene/9606:IFNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GV38|||http://purl.uniprot.org/uniprot/P01574                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Interferon beta|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Variant found in a clone obtained from a fibroblast cell line; does not form the essential disulfide bond; results in loss of antiviral activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016400|||http://purl.uniprot.org/annotation/PRO_5030807232|||http://purl.uniprot.org/annotation/VAR_004016|||http://purl.uniprot.org/annotation/VAR_036330
http://togogenome.org/gene/9606:SMIM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HG1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344238
http://togogenome.org/gene/9606:GPR17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G4XH68|||http://purl.uniprot.org/uniprot/Q13304                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Uracil nucleotide/cysteinyl leukotriene receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069536|||http://purl.uniprot.org/annotation/VSP_001987
http://togogenome.org/gene/9606:SNX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60749                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location.|||BAR|||Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN.|||Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN; when associated with A-426.|||Decreases KALRN-dependent lamellipodium formation; no effect on interaction with KALRN; when associated with A-428.|||Disordered|||In isoform 2.|||Interaction with RhoG|||Membrane-binding amphipathic helix|||N6-acetyllysine|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sorting nexin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213838|||http://purl.uniprot.org/annotation/VSP_054785
http://togogenome.org/gene/9606:PRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43663                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Dimerization|||Disordered|||Impairs binding to the POLO box domains of PLK1, preventing phosphorylation by PLK1 and recruitment of PLK1 to the spindle.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||No effect. Abolishes CDK1-mediated phosphorylation, leading to prematurely recruit PLK1 to the spindle during prometaphase and blocking mitotic progression; when associated with A-481.|||No effect. Reduces in vitro cyclin E-CDK2 phosphorylation and causes extensive bundling of microtubules to the mitotic spindle; when associated with A-470.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by PLK1|||Protein regulator of cytokinesis 1|||Required for the interaction with KIF4A|||Spectrin-fold|||Tubulin binding|||Unstructured, Arg/Lys rich|||Weakly reduces binding to the POLO box domains of PLK1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229737|||http://purl.uniprot.org/annotation/VAR_047768|||http://purl.uniprot.org/annotation/VAR_047769|||http://purl.uniprot.org/annotation/VSP_035875|||http://purl.uniprot.org/annotation/VSP_035876|||http://purl.uniprot.org/annotation/VSP_051979|||http://purl.uniprot.org/annotation/VSP_051980
http://togogenome.org/gene/9606:VENTX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95231                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein VENTX|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305938|||http://purl.uniprot.org/annotation/VAR_035243|||http://purl.uniprot.org/annotation/VAR_035244|||http://purl.uniprot.org/annotation/VAR_049591|||http://purl.uniprot.org/annotation/VAR_049592|||http://purl.uniprot.org/annotation/VAR_061269
http://togogenome.org/gene/9606:SERF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75920                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases SNCA binding.|||Disordered|||Drastically decreases SNCA binding.|||In isoform Short.|||Inhibits SNCA binding.|||No effect on SNCA binding.|||Required for SNCA binding|||Slightly decreases SNCA binding.|||Small EDRK-rich factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050710|||http://purl.uniprot.org/annotation/VSP_006057
http://togogenome.org/gene/9606:ZNF282                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y3|||http://purl.uniprot.org/uniprot/Q86YG2|||http://purl.uniprot.org/uniprot/Q9UDV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Pro residues|||Zinc finger protein 282                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047506|||http://purl.uniprot.org/annotation/VAR_052805|||http://purl.uniprot.org/annotation/VSP_056545|||http://purl.uniprot.org/annotation/VSP_056546
http://togogenome.org/gene/9606:FAM83G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6ND36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Completely abolishes phosphorylation by ALK3 in vitro. NEDD9 and ASNS activation in response to BMPs is abolished.|||Disordered|||Found in patient with Joubert syndrome; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM83G|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330817|||http://purl.uniprot.org/annotation/VAR_053903|||http://purl.uniprot.org/annotation/VAR_075713|||http://purl.uniprot.org/annotation/VAR_075714|||http://purl.uniprot.org/annotation/VSP_033120|||http://purl.uniprot.org/annotation/VSP_033121|||http://purl.uniprot.org/annotation/VSP_033122|||http://purl.uniprot.org/annotation/VSP_033123
http://togogenome.org/gene/9606:CDH13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3H7|||http://purl.uniprot.org/uniprot/B7Z9B1|||http://purl.uniprot.org/uniprot/P55290                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-13|||Disordered|||GPI-anchor amidated glycine|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003793|||http://purl.uniprot.org/annotation/PRO_0000003794|||http://purl.uniprot.org/annotation/PRO_0000003795|||http://purl.uniprot.org/annotation/VAR_030632|||http://purl.uniprot.org/annotation/VAR_065747|||http://purl.uniprot.org/annotation/VAR_065748|||http://purl.uniprot.org/annotation/VAR_065749|||http://purl.uniprot.org/annotation/VAR_065750|||http://purl.uniprot.org/annotation/VAR_065751|||http://purl.uniprot.org/annotation/VAR_065752|||http://purl.uniprot.org/annotation/VAR_065753|||http://purl.uniprot.org/annotation/VSP_042696|||http://purl.uniprot.org/annotation/VSP_042697|||http://purl.uniprot.org/annotation/VSP_042794|||http://purl.uniprot.org/annotation/VSP_042795|||http://purl.uniprot.org/annotation/VSP_046714|||http://purl.uniprot.org/annotation/VSP_053739
http://togogenome.org/gene/9606:TBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13207                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes binding to T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence.|||Abolishes repression of tumor suppressor ARF/p14ARF expression.|||Basic and acidic residues|||Disordered|||In VETD; de novo variant; decreased transcriptional regulatory activity; no effect on localization to the nucleus.|||In VETD; unknown pathological significance; decreased transcriptional regulatory activity; no effect on localization to the nucleus.|||Phosphoserine|||Repression domain 1 (RD1)|||Severely impairs repression of tumor suppressor ARF/p14ARF expression.|||T-box|||T-box transcription factor TBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184426|||http://purl.uniprot.org/annotation/VAR_081780|||http://purl.uniprot.org/annotation/VAR_081781
http://togogenome.org/gene/9606:DNM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK06|||http://purl.uniprot.org/uniprot/B7ZAC0|||http://purl.uniprot.org/uniprot/Q05193                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine; alternate|||Disordered|||Dynamin-1|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In DEE31A.|||In DEE31B.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Inhibits receptor-mediated endocytosis.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; alternate|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206563|||http://purl.uniprot.org/annotation/VAR_048904|||http://purl.uniprot.org/annotation/VAR_073710|||http://purl.uniprot.org/annotation/VAR_073711|||http://purl.uniprot.org/annotation/VAR_073712|||http://purl.uniprot.org/annotation/VAR_073713|||http://purl.uniprot.org/annotation/VAR_088263|||http://purl.uniprot.org/annotation/VAR_088264|||http://purl.uniprot.org/annotation/VSP_031518|||http://purl.uniprot.org/annotation/VSP_031519
http://togogenome.org/gene/9606:OTOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9KVB3|||http://purl.uniprot.org/uniprot/Q6ZRI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CTCK|||Disordered|||EGF-like|||In DFNB18B.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Otogelin|||Polar residues|||Pro residues|||TIL|||VWFD|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312148|||http://purl.uniprot.org/annotation/PRO_5003622148|||http://purl.uniprot.org/annotation/VAR_037406|||http://purl.uniprot.org/annotation/VAR_037407|||http://purl.uniprot.org/annotation/VAR_037408|||http://purl.uniprot.org/annotation/VAR_037409|||http://purl.uniprot.org/annotation/VAR_037410|||http://purl.uniprot.org/annotation/VAR_037411|||http://purl.uniprot.org/annotation/VAR_037412|||http://purl.uniprot.org/annotation/VAR_037413|||http://purl.uniprot.org/annotation/VAR_037414|||http://purl.uniprot.org/annotation/VAR_037415|||http://purl.uniprot.org/annotation/VAR_037416|||http://purl.uniprot.org/annotation/VAR_037417|||http://purl.uniprot.org/annotation/VAR_037418|||http://purl.uniprot.org/annotation/VAR_047262|||http://purl.uniprot.org/annotation/VAR_061161|||http://purl.uniprot.org/annotation/VAR_069250|||http://purl.uniprot.org/annotation/VAR_084731|||http://purl.uniprot.org/annotation/VSP_029709|||http://purl.uniprot.org/annotation/VSP_029710|||http://purl.uniprot.org/annotation/VSP_029711|||http://purl.uniprot.org/annotation/VSP_029712|||http://purl.uniprot.org/annotation/VSP_029713|||http://purl.uniprot.org/annotation/VSP_029714
http://togogenome.org/gene/9606:FFAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14842                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Constitutive receptor signaling.|||Cytoplasmic|||Extracellular|||Free fatty acid receptor 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for receptor activation|||N-linked (GlcNAc...) asparagine|||Reduces cell surface expression and response to linolenic acid and synthetic agonists.|||Reduces response to linolenic acid. Reduces response to synthetic agonists.|||Reduces response to linolenic acid. Strongly reduces response to synthetic agonists.|||Reduces response to synthetic agonists.|||Strongly reduces response to linolenic acid. Strongly reduces response to synthetic agonists.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069567|||http://purl.uniprot.org/annotation/VAR_020076
http://togogenome.org/gene/9606:CTU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7A3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cytoplasmic tRNA 2-thiolation protein 1|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282391|||http://purl.uniprot.org/annotation/VAR_031402
http://togogenome.org/gene/9606:GALNT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SR1                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Flexible loop|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 10|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059122|||http://purl.uniprot.org/annotation/VSP_011207|||http://purl.uniprot.org/annotation/VSP_011208|||http://purl.uniprot.org/annotation/VSP_011209|||http://purl.uniprot.org/annotation/VSP_011212|||http://purl.uniprot.org/annotation/VSP_011213|||http://purl.uniprot.org/annotation/VSP_011214
http://togogenome.org/gene/9606:NR5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8R9|||http://purl.uniprot.org/uniprot/O00482                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FTZ-F1 box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Impaired ability to act as an anti-inflammatory role during the hepatic acute phase response.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 5 group A member 2|||Reduced DNA binding. Loss of transactivation.|||Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-342.|||Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-416.|||Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-168 and A-172.|||Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-168.|||Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-172.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053735|||http://purl.uniprot.org/annotation/VSP_003716|||http://purl.uniprot.org/annotation/VSP_003717|||http://purl.uniprot.org/annotation/VSP_054548
http://togogenome.org/gene/9606:GMFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60983                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  ADF-H|||Glia maturation factor beta|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214943
http://togogenome.org/gene/9606:CPNE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCH3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-5|||Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144843|||http://purl.uniprot.org/annotation/VAR_020358|||http://purl.uniprot.org/annotation/VAR_021954|||http://purl.uniprot.org/annotation/VSP_056535
http://togogenome.org/gene/9606:MRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI43|||http://purl.uniprot.org/uniprot/V9HWJ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MTDPS17.|||Mitochondrion|||Proton acceptor|||Ribosomal RNA methyltransferase FtsJ|||rRNA methyltransferase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155576|||http://purl.uniprot.org/annotation/VAR_083280
http://togogenome.org/gene/9606:GCNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Germ cell nuclear acidic protein|||Impairs SUMO2 interaction. Loss of SUMO2 interaction; when associated with 22-A--A-25, 76-A--A-79 and 121-A--A-124. Loss of SUMO2-dependent recruitment to DNA-protein cross-links (DPCs); when associated with 22-A--A-25; 76-A--A-79 and 121-A--A-124.|||Impairs SUMO2 interaction. Loss of SUMO2 interaction; when associated with 22-A--A-25, 76-A--A-79 and 97-A--A-100. Loss of SUMO2-dependent recruitment to DNA-protein cross-links (DPCs); when associated with 22-A--A-25; 76-A--A-79 and 97-A--A-100.|||Impairs SUMO2 interaction. Loss of SUMO2 interaction; when associated with 22-A--A-25, 97-A--A-100 and 121-A--A-124. Loss of SUMO2-dependent recruitment to DNA-protein cross-links (DPCs); when associated with 22-A--A-25; 97-A--A-100 and 121-A--A-124.|||Impairs SUMO2 interaction. Loss of SUMO2 interaction; when associated with 76-A--A-79, 97-A--A-100 and 121-A--A-124. Loss of SUMO2-dependent recruitment to DNA-protein cross-links (DPCs); when associated with 76-A--A-79; 97-A--A-100 and 121-A--A-124.|||In SPGFX4.|||In SPGFX4; unknown pathological significance.|||In SPGFX4; unknown pathological significance; requires 2 nucleotide substitutions.|||Polar residues|||SUMO interaction motif 1 (SIM)|||SprT-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317387|||http://purl.uniprot.org/annotation/VAR_038520|||http://purl.uniprot.org/annotation/VAR_050634|||http://purl.uniprot.org/annotation/VAR_085476|||http://purl.uniprot.org/annotation/VAR_085477|||http://purl.uniprot.org/annotation/VAR_085478|||http://purl.uniprot.org/annotation/VAR_085479|||http://purl.uniprot.org/annotation/VAR_085480|||http://purl.uniprot.org/annotation/VAR_085481|||http://purl.uniprot.org/annotation/VAR_085482|||http://purl.uniprot.org/annotation/VAR_085483|||http://purl.uniprot.org/annotation/VAR_085484|||http://purl.uniprot.org/annotation/VAR_085486|||http://purl.uniprot.org/annotation/VAR_085487|||http://purl.uniprot.org/annotation/VAR_085488|||http://purl.uniprot.org/annotation/VAR_085489|||http://purl.uniprot.org/annotation/VAR_085490|||http://purl.uniprot.org/annotation/VAR_085491|||http://purl.uniprot.org/annotation/VAR_087077
http://togogenome.org/gene/9606:MMP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQS8|||http://purl.uniprot.org/uniprot/P24347                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Disordered|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In a colorectal cancer sample; somatic mutation.|||Peptidase metallopeptidase|||Stromelysin-3|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028770|||http://purl.uniprot.org/annotation/PRO_0000028771|||http://purl.uniprot.org/annotation/PRO_5010105240|||http://purl.uniprot.org/annotation/VAR_022181|||http://purl.uniprot.org/annotation/VAR_022182|||http://purl.uniprot.org/annotation/VAR_022183|||http://purl.uniprot.org/annotation/VAR_022184|||http://purl.uniprot.org/annotation/VAR_029659|||http://purl.uniprot.org/annotation/VAR_036140
http://togogenome.org/gene/9606:UTP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Something about silencing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114326|||http://purl.uniprot.org/annotation/VAR_051897
http://togogenome.org/gene/9606:STARD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSY2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||START|||StAR-related lipid transfer protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220669|||http://purl.uniprot.org/annotation/VAR_052071|||http://purl.uniprot.org/annotation/VSP_014871|||http://purl.uniprot.org/annotation/VSP_014872
http://togogenome.org/gene/9606:CREBRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic motif|||CREB3 regulatory factor|||Disordered|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299306|||http://purl.uniprot.org/annotation/VAR_034795|||http://purl.uniprot.org/annotation/VSP_027601|||http://purl.uniprot.org/annotation/VSP_027602|||http://purl.uniprot.org/annotation/VSP_027603
http://togogenome.org/gene/9606:TUBGCP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gamma-tubulin complex component 4|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078124|||http://purl.uniprot.org/annotation/VSP_040085
http://togogenome.org/gene/9606:APBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02410                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amyloid-beta A4 precursor protein-binding family A member 1|||Autoinhibitory helix linker|||Basic and acidic residues|||Diminishes interaction with APP.|||Disordered|||In isoform 2.|||LIN-2/CASK binding|||Munc-18-1 binding|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064614|||http://purl.uniprot.org/annotation/VAR_050664|||http://purl.uniprot.org/annotation/VSP_053518
http://togogenome.org/gene/9606:SLAIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSS3|||http://purl.uniprot.org/uniprot/B7Z326|||http://purl.uniprot.org/uniprot/Q7L0J2|||http://purl.uniprot.org/uniprot/Q8ND83                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||SLAIN motif-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316962|||http://purl.uniprot.org/annotation/VSP_030832|||http://purl.uniprot.org/annotation/VSP_043256|||http://purl.uniprot.org/annotation/VSP_043257|||http://purl.uniprot.org/annotation/VSP_054118
http://togogenome.org/gene/9606:CDC5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99459                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DNA-binding; when associated with G-31 and G-53.|||Abolishes DNA-binding; when associated with G-31 and G-82.|||Abolishes DNA-binding; when associated with G-53 and G-82.|||Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-411. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-424.|||Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-438. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-417; A-424 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-424 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-411; A-417; A-424 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-385; A-404; A-411; A-417; A-424 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-358; A-385; A-404; A-411; A-417; A-424 and A-438.|||Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-303; A-358; A-385; A-404; A-411; A-417; A-424 and A-438.|||Basic and acidic residues|||Breakpoint for translocation|||Cell division cycle 5-like protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type 1|||HTH myb-type 2|||Interaction with DAPK3|||Interaction with PLRG1|||Interaction with PPP1R8|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with CTNNBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197091|||http://purl.uniprot.org/annotation/VAR_050181
http://togogenome.org/gene/9606:TBCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6Q1|||http://purl.uniprot.org/uniprot/Q15813                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CAP-Gly|||In HRDS and KCS1.|||In PEAMO; decreased function in the organization of microtubule cytoskeleton and mitotic splindle.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed|||Tubulin-specific chaperone E|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083538|||http://purl.uniprot.org/annotation/VAR_032920|||http://purl.uniprot.org/annotation/VAR_032921|||http://purl.uniprot.org/annotation/VAR_032922|||http://purl.uniprot.org/annotation/VAR_032923|||http://purl.uniprot.org/annotation/VAR_077878|||http://purl.uniprot.org/annotation/VSP_053870
http://togogenome.org/gene/9606:UGT2B15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54855                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 2B15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036039|||http://purl.uniprot.org/annotation/VAR_007713|||http://purl.uniprot.org/annotation/VAR_018348
http://togogenome.org/gene/9606:DKK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBU2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007220|||http://purl.uniprot.org/annotation/VAR_021966
http://togogenome.org/gene/9606:D2HGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSR6|||http://purl.uniprot.org/uniprot/B4E3K7|||http://purl.uniprot.org/uniprot/B5MCV2|||http://purl.uniprot.org/uniprot/Q8N465                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  D-2-hydroxyglutarate dehydrogenase, mitochondrial|||FAD-binding PCMH-type|||In D2HGA1; mild phenotype; unknown pathological significance; moderate reduction in catalytic activity.|||In D2HGA1; severe phenotype; unknown pathological significance; almost complete loss of catalytic activity.|||In D2HGA1; severe phenotype; unknown pathological significance; significant reduction in catalytic activity.|||In D2HGA1; unknown pathological significance.|||In D2HGA1; unknown pathological significance; almost complete loss of catalytic activity.|||In D2HGA1; unknown pathological significance; complete loss of catalytic activity.|||In D2HGA1; unknown pathological significance; moderate reduction in catalytic activity.|||In D2HGA1; unknown pathological significance; no effect on catalytic activity.|||In D2HGA1; unknown pathological significance; significant loss of catalytic activity.|||In isoform 2.|||In isoform 3.|||Loss of catalytic activity.|||Mitochondrion|||N6-succinyllysine|||Significantly reduced catalytic activity.|||Slight reduction in catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231674|||http://purl.uniprot.org/annotation/PRO_5002801150|||http://purl.uniprot.org/annotation/VAR_025889|||http://purl.uniprot.org/annotation/VAR_025890|||http://purl.uniprot.org/annotation/VAR_025891|||http://purl.uniprot.org/annotation/VAR_025892|||http://purl.uniprot.org/annotation/VAR_025893|||http://purl.uniprot.org/annotation/VAR_025894|||http://purl.uniprot.org/annotation/VAR_050433|||http://purl.uniprot.org/annotation/VAR_050434|||http://purl.uniprot.org/annotation/VAR_084974|||http://purl.uniprot.org/annotation/VAR_084975|||http://purl.uniprot.org/annotation/VAR_084976|||http://purl.uniprot.org/annotation/VAR_084977|||http://purl.uniprot.org/annotation/VAR_084978|||http://purl.uniprot.org/annotation/VAR_084979|||http://purl.uniprot.org/annotation/VAR_084980|||http://purl.uniprot.org/annotation/VAR_084981|||http://purl.uniprot.org/annotation/VAR_084982|||http://purl.uniprot.org/annotation/VAR_084983|||http://purl.uniprot.org/annotation/VAR_084984|||http://purl.uniprot.org/annotation/VAR_084985|||http://purl.uniprot.org/annotation/VAR_084986|||http://purl.uniprot.org/annotation/VAR_084987|||http://purl.uniprot.org/annotation/VAR_084988|||http://purl.uniprot.org/annotation/VAR_084989|||http://purl.uniprot.org/annotation/VAR_084990|||http://purl.uniprot.org/annotation/VSP_017876|||http://purl.uniprot.org/annotation/VSP_017877|||http://purl.uniprot.org/annotation/VSP_017878|||http://purl.uniprot.org/annotation/VSP_054389|||http://purl.uniprot.org/annotation/VSP_054390
http://togogenome.org/gene/9606:IL17B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHF5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Interleukin-17B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015426
http://togogenome.org/gene/9606:DOC2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14184                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Disordered|||Double C2-like domain-containing protein beta|||In a patient with amyotrophic lateral sclerosis.|||Mediates interaction with DYNLT1|||Mediates interaction with STXBP3|||Negatively regulates targeting to plasma membrane|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079968|||http://purl.uniprot.org/annotation/VAR_065743
http://togogenome.org/gene/9606:ZFAND2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6M9                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269888|||http://purl.uniprot.org/annotation/VAR_055295
http://togogenome.org/gene/9606:BSPRY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0U4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box and SPRY domain-containing protein|||B box-type|||B30.2/SPRY|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244257|||http://purl.uniprot.org/annotation/VAR_026882|||http://purl.uniprot.org/annotation/VAR_026883|||http://purl.uniprot.org/annotation/VAR_048397|||http://purl.uniprot.org/annotation/VSP_019527|||http://purl.uniprot.org/annotation/VSP_019528
http://togogenome.org/gene/9606:ANKS1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CP0|||http://purl.uniprot.org/uniprot/Q92625                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SAM domain-containing protein 1A|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylglycine|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SAM 1|||SAM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066921|||http://purl.uniprot.org/annotation/VAR_021168|||http://purl.uniprot.org/annotation/VAR_048282|||http://purl.uniprot.org/annotation/VSP_056512|||http://purl.uniprot.org/annotation/VSP_056513
http://togogenome.org/gene/9606:NOBOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60393                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein NOBOX|||In POF5.|||In POF5; likely benign variant; decreased nuclear location; intranuclear and cytosolic aggregates.|||In POF5; unknown pathological significance; decreased nuclear location; intranuclear and cytosolic aggregates.|||In POF5; unknown pathological significance; decreased transactivation activity.|||In POF5; unknown pathological significance; decreased transactivation activity; decreased nuclear location; intranuclear and cytosolic aggregates.|||In POF5; unknown pathological significance; loss of transactivation activity; intranuclear and cytosolic aggregates; not statistically significant decrease of nuclear location.|||In POF5; unknown pathological significance; not statistically significant decrease of nuclear location.|||In isoform 2.|||No effect on transactivation activity.|||No effect on transactivation activity; not statistically significant decrease of nuclear location.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268865|||http://purl.uniprot.org/annotation/VAR_036636|||http://purl.uniprot.org/annotation/VAR_036637|||http://purl.uniprot.org/annotation/VAR_036638|||http://purl.uniprot.org/annotation/VAR_036639|||http://purl.uniprot.org/annotation/VAR_036640|||http://purl.uniprot.org/annotation/VAR_061266|||http://purl.uniprot.org/annotation/VAR_066013|||http://purl.uniprot.org/annotation/VAR_066014|||http://purl.uniprot.org/annotation/VAR_066015|||http://purl.uniprot.org/annotation/VAR_078291|||http://purl.uniprot.org/annotation/VAR_078292|||http://purl.uniprot.org/annotation/VAR_078293|||http://purl.uniprot.org/annotation/VAR_078294|||http://purl.uniprot.org/annotation/VAR_078295|||http://purl.uniprot.org/annotation/VAR_078296|||http://purl.uniprot.org/annotation/VSP_028796
http://togogenome.org/gene/9606:IRF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E2GIM5|||http://purl.uniprot.org/uniprot/E2GIM6|||http://purl.uniprot.org/uniprot/E2GIM7|||http://purl.uniprot.org/uniprot/E2GIM8|||http://purl.uniprot.org/uniprot/E2GIM9|||http://purl.uniprot.org/uniprot/M0QYT9|||http://purl.uniprot.org/uniprot/Q14653                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Phosphoserine|||Abolished cleavage by CASP3.|||Abolished interaction with STING1, MAVS or TICAM1.|||Abolishes nuclear export.|||Abolishes nuclear localization.|||Acts as a constitutively activated IRF3.|||Basic and acidic residues|||Cleavage; by CASP3|||Complete loss of viral infection induced phosphorylation.|||Decreased IFNB induction upon Sendai virus infection.|||Decreased interaction with TICAM1.|||Disordered|||Does not affect cleavage by CASP3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Highly diminished ISGylation; when associated with R-193 and R-360.|||Highly diminished ISGylation; when associated with R-193 and R-366.|||Highly diminished ISGylation; when associated with R-360 and R-366.|||IRF tryptophan pentad repeat|||In IIAE7; loss of viral infection-induced phosphorylation at S-386; loss of viral infection-induced homodimerization; loss of viral infection-induced transcription factor activity; unable to activate interferon transcription in response to viral infection; decreased IFNB induction upon Sendai virus infection.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with HERC5|||Interferon regulatory factor 3|||Interferon regulatory factor-3|||Mediates interaction with ZDHHC11|||No effect on IFNB induction upon Sendai virus infection.|||No effect on subcellular localization.|||Nuclear export signal|||Phosphomimetic mutant; interacts with CREBBP; when associated with E-386.|||Phosphomimetic mutant; interacts with CREBBP; when associated with E-396.|||Phosphoserine|||Phosphoserine; by IKKE and TBK1|||Phosphoserine; by TBK1|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154553|||http://purl.uniprot.org/annotation/VAR_011901|||http://purl.uniprot.org/annotation/VAR_011902|||http://purl.uniprot.org/annotation/VAR_011903|||http://purl.uniprot.org/annotation/VAR_049643|||http://purl.uniprot.org/annotation/VAR_075805|||http://purl.uniprot.org/annotation/VAR_084069|||http://purl.uniprot.org/annotation/VAR_084070|||http://purl.uniprot.org/annotation/VAR_084071|||http://purl.uniprot.org/annotation/VAR_084072|||http://purl.uniprot.org/annotation/VAR_084073|||http://purl.uniprot.org/annotation/VSP_043319|||http://purl.uniprot.org/annotation/VSP_046911|||http://purl.uniprot.org/annotation/VSP_046912|||http://purl.uniprot.org/annotation/VSP_047690|||http://purl.uniprot.org/annotation/VSP_047691
http://togogenome.org/gene/9606:KRTAP1-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07627                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In allele KAP1.6.|||In allele KAP1.7.|||Keratin-associated protein 1-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223901|||http://purl.uniprot.org/annotation/VAR_025348|||http://purl.uniprot.org/annotation/VAR_025353
http://togogenome.org/gene/9606:IWS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ST2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  1|||2|||3 X approximate tandem repeats|||3; half-length|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Integrase domain-binding motif (IBM)|||Interaction with SUPT6H and ALYREF|||Loss of interaction with PSIP1; when associated with A-476.|||Loss of interaction with PSIP1; when associated with A-477.|||N-acetylmethionine|||Phosphomimetic mutant. Moderate increase in interaction with PSIP1.|||Phosphoserine|||Phosphothreonine|||Protein IWS1 homolog|||TFIIS N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083346|||http://purl.uniprot.org/annotation/VAR_055975|||http://purl.uniprot.org/annotation/VAR_055976|||http://purl.uniprot.org/annotation/VSP_016992|||http://purl.uniprot.org/annotation/VSP_016993
http://togogenome.org/gene/9606:SRGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10124                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 2 AA tandem repeats of [SF]-G|||Disordered|||O-linked (Xyl...) (glycosaminoglycan) serine|||Serglycin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026679|||http://purl.uniprot.org/annotation/VAR_032761
http://togogenome.org/gene/9606:LARP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRS8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||In isoform 2.|||La-related protein 6|||N-acetylalanine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Polar residues|||RRM|||Removed|||SUZ-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281141|||http://purl.uniprot.org/annotation/VSP_042565
http://togogenome.org/gene/9606:PSMD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00231                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 11|||Does not affect phosphorylation by AMPK; when associated with A-14 and A-272.|||Does not affect phosphorylation by AMPK; when associated with A-79 and A-272.|||Does not affect phosphorylation by AMPK; when associated with A14- and A-79.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||PCI|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173857|||http://purl.uniprot.org/annotation/VSP_044400
http://togogenome.org/gene/9606:AKAP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43687|||http://purl.uniprot.org/uniprot/Q2TAJ5|||http://purl.uniprot.org/uniprot/Q6P4D3|||http://purl.uniprot.org/uniprot/Q9P0M2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A-kinase anchor protein 7 RI-RII subunit-binding|||A-kinase anchor protein 7 isoform gamma|||A-kinase anchor protein 7 isoforms alpha and beta|||Abolishes membrane localization and affects its ability to inhibit ENaC activity in a sodium-dependent manner.|||Disordered|||In isoform Alpha.|||N-myristoyl glycine|||PKA-RII-alpha subunit binding domain|||Polar residues|||RI-alpha-binding|||RII-binding|||Removed|||Required for apical membrane localization|||Required for membrane localization|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064522|||http://purl.uniprot.org/annotation/PRO_0000064523|||http://purl.uniprot.org/annotation/VAR_024246|||http://purl.uniprot.org/annotation/VAR_024247|||http://purl.uniprot.org/annotation/VSP_004101
http://togogenome.org/gene/9606:TEX28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15482                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Testis-specific protein TEX28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184594
http://togogenome.org/gene/9606:FGF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JW05|||http://purl.uniprot.org/uniprot/P10767                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Fibroblast growth factor 6|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008961|||http://purl.uniprot.org/annotation/VAR_018882|||http://purl.uniprot.org/annotation/VAR_018883|||http://purl.uniprot.org/annotation/VAR_018884|||http://purl.uniprot.org/annotation/VAR_018885
http://togogenome.org/gene/9606:KDM1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60341                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone demethylase activity.|||Basic and acidic residues|||Demethylase activity|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CPRF.|||In isoform 2.|||Loss of polyubiquitination.|||Lysine-specific histone demethylase 1A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SWIRM|||Strongly reduces demethylase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099881|||http://purl.uniprot.org/annotation/VAR_076366|||http://purl.uniprot.org/annotation/VAR_076367|||http://purl.uniprot.org/annotation/VAR_076368|||http://purl.uniprot.org/annotation/VSP_011198|||http://purl.uniprot.org/annotation/VSP_011199
http://togogenome.org/gene/9606:FLOT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75955|||http://purl.uniprot.org/uniprot/Q5ST80                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 7|||Flotillin-1|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094044|||http://purl.uniprot.org/annotation/VAR_048415|||http://purl.uniprot.org/annotation/VSP_056227
http://togogenome.org/gene/9606:CGB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Choriogonadotropin subunit beta variant 2|||Disordered|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342549
http://togogenome.org/gene/9606:TIMELESS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PARP1.|||Acidic residues|||Basic and acidic residues|||DNA-binding domain|||Disordered|||In FASPS4; reduced protein stability; mislocalization in cytoplasm; reduced interaction with CRY2; enhanced destabilization of the PER2-CRY2 complex; reduced repressor activity of CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation of PER1; does not affect interaction with PER2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with PARP1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein timeless homolog|||Required for homodimerization and for interaction with CRY1 and CHEK1|||Required for nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072538|||http://purl.uniprot.org/annotation/VAR_021483|||http://purl.uniprot.org/annotation/VAR_021484|||http://purl.uniprot.org/annotation/VAR_021485|||http://purl.uniprot.org/annotation/VAR_036435|||http://purl.uniprot.org/annotation/VAR_036436|||http://purl.uniprot.org/annotation/VAR_047879|||http://purl.uniprot.org/annotation/VAR_047880|||http://purl.uniprot.org/annotation/VAR_047881|||http://purl.uniprot.org/annotation/VAR_047882|||http://purl.uniprot.org/annotation/VAR_047883|||http://purl.uniprot.org/annotation/VAR_047884|||http://purl.uniprot.org/annotation/VAR_087625|||http://purl.uniprot.org/annotation/VSP_051693
http://togogenome.org/gene/9606:MX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9KVC7|||http://purl.uniprot.org/uniprot/P20591                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bundle signaling element (BSE)|||Critical for lipid-binding|||Dynamin-type G|||Fails to sequester viral nucleoproteins, no antiviral activity.|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 2.|||Interferon-induced GTP-binding protein Mx1|||Interferon-induced GTP-binding protein Mx1, N-terminally processed|||Loss of GTP-binding. Loss of potentiation of TRPC6 activity. Loss of protection against viral infection.|||Loss of GTP-binding. Loss of protection against viral infection.|||Loss of GTP-hydrolysis. No effect on GTP-binding, nor on potentiation of TRPC6 activity.|||Loss of antiviral activity towards CCHFV and LACV.|||Middle domain|||N-acetylmethionine; in Interferon-induced GTP-binding protein Mx1; alternate|||No effect on GTP-binding, nor on viral infection.|||Reduced antiviral activity.|||Removed; alternate|||Stalk|||Strong liposome-binding reduction.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206592|||http://purl.uniprot.org/annotation/PRO_0000382943|||http://purl.uniprot.org/annotation/VAR_034116|||http://purl.uniprot.org/annotation/VAR_034117|||http://purl.uniprot.org/annotation/VAR_058010|||http://purl.uniprot.org/annotation/VSP_042904
http://togogenome.org/gene/9606:DCAF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9S7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 17|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300118|||http://purl.uniprot.org/annotation/VAR_050711|||http://purl.uniprot.org/annotation/VSP_027788
http://togogenome.org/gene/9606:FUZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT04                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Protein fuzzy homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312920|||http://purl.uniprot.org/annotation/VAR_037615|||http://purl.uniprot.org/annotation/VAR_037616|||http://purl.uniprot.org/annotation/VAR_037617|||http://purl.uniprot.org/annotation/VSP_029965|||http://purl.uniprot.org/annotation/VSP_029966
http://togogenome.org/gene/9606:KLHDC7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch domain-containing protein 7A|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285085|||http://purl.uniprot.org/annotation/VAR_031913|||http://purl.uniprot.org/annotation/VAR_031914|||http://purl.uniprot.org/annotation/VAR_056126|||http://purl.uniprot.org/annotation/VAR_056127|||http://purl.uniprot.org/annotation/VAR_059441|||http://purl.uniprot.org/annotation/VAR_059442|||http://purl.uniprot.org/annotation/VAR_061341|||http://purl.uniprot.org/annotation/VAR_061342
http://togogenome.org/gene/9606:PLB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWP8|||http://purl.uniprot.org/uniprot/Q6P1J6                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 308-326 AA approximate repeats|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Necessary for membrane localization|||Phospholipase B1, membrane-associated                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324383|||http://purl.uniprot.org/annotation/PRO_5002782169|||http://purl.uniprot.org/annotation/VAR_039793|||http://purl.uniprot.org/annotation/VAR_039794|||http://purl.uniprot.org/annotation/VAR_039795|||http://purl.uniprot.org/annotation/VAR_039796|||http://purl.uniprot.org/annotation/VAR_039797|||http://purl.uniprot.org/annotation/VAR_061358|||http://purl.uniprot.org/annotation/VSP_032225|||http://purl.uniprot.org/annotation/VSP_032226|||http://purl.uniprot.org/annotation/VSP_032227|||http://purl.uniprot.org/annotation/VSP_032228|||http://purl.uniprot.org/annotation/VSP_032229|||http://purl.uniprot.org/annotation/VSP_032230|||http://purl.uniprot.org/annotation/VSP_032231|||http://purl.uniprot.org/annotation/VSP_032232
http://togogenome.org/gene/9606:GRIK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16478                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor ionotropic, kainate 5|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011552|||http://purl.uniprot.org/annotation/VSP_035585
http://togogenome.org/gene/9606:RFESD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAC1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Rieske 1|||Rieske 2|||Rieske domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313813|||http://purl.uniprot.org/annotation/VSP_044452
http://togogenome.org/gene/9606:NUP50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 2 AA repeats of F-G|||Basic and acidic residues|||Binding to CDKN1B|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Nuclear pore complex protein Nup50|||Phosphoserine|||Phosphothreonine|||RanBD1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204868|||http://purl.uniprot.org/annotation/VSP_040633
http://togogenome.org/gene/9606:OGFOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PK18                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Fe2OG dioxygenase|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325885|||http://purl.uniprot.org/annotation/VAR_039948|||http://purl.uniprot.org/annotation/VAR_039949|||http://purl.uniprot.org/annotation/VSP_032462
http://togogenome.org/gene/9606:CYFIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8N7|||http://purl.uniprot.org/uniprot/E7EVJ5|||http://purl.uniprot.org/uniprot/Q96F07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CYRIA/CYRIB Rac1 binding|||Cytoplasmic FMR1-interacting protein 2|||In DEE65.|||In RNA edited version.|||In isoform 2.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279709|||http://purl.uniprot.org/annotation/VAR_030953|||http://purl.uniprot.org/annotation/VAR_080817|||http://purl.uniprot.org/annotation/VAR_080818|||http://purl.uniprot.org/annotation/VAR_080819|||http://purl.uniprot.org/annotation/VSP_052349
http://togogenome.org/gene/9606:TRRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4A5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Bipartite nuclear localization signal|||Catalytic loop|||Disordered|||FAT|||FATC|||Found in a cutaneous malignant melanoma sample; somatic mutation; induces cell transformation and confers resistance to apoptosis.|||G-loop|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DEDDFA.|||In DEDDFA; unknown pathological significance.|||In DEDDFA; unknown pathological significance; also found in a colorectal adenocarcinoma sample; somatic mutation.|||In DFNA75; unknown pathological significance.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with TP53|||N-acetylalanine|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||Transformation/transcription domain-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088851|||http://purl.uniprot.org/annotation/VAR_028359|||http://purl.uniprot.org/annotation/VAR_041658|||http://purl.uniprot.org/annotation/VAR_041659|||http://purl.uniprot.org/annotation/VAR_041660|||http://purl.uniprot.org/annotation/VAR_041661|||http://purl.uniprot.org/annotation/VAR_041662|||http://purl.uniprot.org/annotation/VAR_041663|||http://purl.uniprot.org/annotation/VAR_041664|||http://purl.uniprot.org/annotation/VAR_041665|||http://purl.uniprot.org/annotation/VAR_041666|||http://purl.uniprot.org/annotation/VAR_041667|||http://purl.uniprot.org/annotation/VAR_041668|||http://purl.uniprot.org/annotation/VAR_041669|||http://purl.uniprot.org/annotation/VAR_041670|||http://purl.uniprot.org/annotation/VAR_041671|||http://purl.uniprot.org/annotation/VAR_067754|||http://purl.uniprot.org/annotation/VAR_082969|||http://purl.uniprot.org/annotation/VAR_082970|||http://purl.uniprot.org/annotation/VAR_082971|||http://purl.uniprot.org/annotation/VAR_082972|||http://purl.uniprot.org/annotation/VAR_082973|||http://purl.uniprot.org/annotation/VAR_082974|||http://purl.uniprot.org/annotation/VAR_082975|||http://purl.uniprot.org/annotation/VAR_082976|||http://purl.uniprot.org/annotation/VAR_082977|||http://purl.uniprot.org/annotation/VAR_082978|||http://purl.uniprot.org/annotation/VAR_082979|||http://purl.uniprot.org/annotation/VAR_082980|||http://purl.uniprot.org/annotation/VAR_082981|||http://purl.uniprot.org/annotation/VAR_082982|||http://purl.uniprot.org/annotation/VAR_082983|||http://purl.uniprot.org/annotation/VAR_082984|||http://purl.uniprot.org/annotation/VAR_082985|||http://purl.uniprot.org/annotation/VAR_083794|||http://purl.uniprot.org/annotation/VAR_083795|||http://purl.uniprot.org/annotation/VSP_009102|||http://purl.uniprot.org/annotation/VSP_009103
http://togogenome.org/gene/9606:ART4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93070                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ecto-ADP-ribosyltransferase 4|||GPI-anchor amidated alanine|||In Do(b), Hy1 and Hy2.|||In Hy1 and Hy2.|||In Hy1.|||In Jo(a).|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||TR mART core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019329|||http://purl.uniprot.org/annotation/PRO_0000019330|||http://purl.uniprot.org/annotation/VAR_013707|||http://purl.uniprot.org/annotation/VAR_013708|||http://purl.uniprot.org/annotation/VAR_013709|||http://purl.uniprot.org/annotation/VAR_013710|||http://purl.uniprot.org/annotation/VAR_022266|||http://purl.uniprot.org/annotation/VAR_022267
http://togogenome.org/gene/9606:KIF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52732                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MCLMR.|||Kinesin motor|||Kinesin-like protein KIF11|||N6-acetyllysine|||No mitotic phosphorylation. No binding to spindle apparatus.|||Phosphoserine; by NEK6|||Phosphothreonine|||Phosphothreonine; by CDK1|||Still binds to the mitotic spindle but mitotic progression is impaired.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125372|||http://purl.uniprot.org/annotation/VAR_049682|||http://purl.uniprot.org/annotation/VAR_067829|||http://purl.uniprot.org/annotation/VAR_067830|||http://purl.uniprot.org/annotation/VAR_067831|||http://purl.uniprot.org/annotation/VAR_067832
http://togogenome.org/gene/9606:ZNF713                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N859                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||KRAB|||Zinc finger protein 713                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233285
http://togogenome.org/gene/9606:RBP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R05                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Retinoid-binding protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067403
http://togogenome.org/gene/9606:MGAT4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM21                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A|||Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288581|||http://purl.uniprot.org/annotation/PRO_0000288582|||http://purl.uniprot.org/annotation/VSP_046075|||http://purl.uniprot.org/annotation/VSP_046076|||http://purl.uniprot.org/annotation/VSP_046077
http://togogenome.org/gene/9606:TAS2R42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JPZ2|||http://purl.uniprot.org/uniprot/Q7RTR8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082344|||http://purl.uniprot.org/annotation/VAR_053352|||http://purl.uniprot.org/annotation/VAR_053353|||http://purl.uniprot.org/annotation/VAR_062086|||http://purl.uniprot.org/annotation/VAR_062087|||http://purl.uniprot.org/annotation/VAR_062088|||http://purl.uniprot.org/annotation/VAR_062089
http://togogenome.org/gene/9606:EFCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand and coiled-coil domain-containing protein 1|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234510|||http://purl.uniprot.org/annotation/VAR_050753|||http://purl.uniprot.org/annotation/VSP_039449
http://togogenome.org/gene/9606:PDE4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR0|||http://purl.uniprot.org/uniprot/Q08499                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization.|||Acidic residues|||Basic and acidic residues|||Decreased 3',5'-cyclic-AMP phosphodiesterase activity. Loss of Mg2(+)-binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In ACRDYS2.|||In isoform 1.|||In isoform 10.|||In isoform 12.|||In isoform 2.|||In isoform 3.|||In isoform 5, isoform N3 and isoform 12.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||In isoform N3.|||PDEase|||Phosphoserine|||Polar residues|||Pro residues|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198814|||http://purl.uniprot.org/annotation/VAR_068242|||http://purl.uniprot.org/annotation/VAR_068243|||http://purl.uniprot.org/annotation/VAR_068244|||http://purl.uniprot.org/annotation/VAR_068245|||http://purl.uniprot.org/annotation/VAR_069448|||http://purl.uniprot.org/annotation/VAR_069449|||http://purl.uniprot.org/annotation/VAR_069450|||http://purl.uniprot.org/annotation/VAR_069451|||http://purl.uniprot.org/annotation/VAR_069452|||http://purl.uniprot.org/annotation/VAR_069453|||http://purl.uniprot.org/annotation/VAR_069454|||http://purl.uniprot.org/annotation/VAR_069455|||http://purl.uniprot.org/annotation/VSP_004577|||http://purl.uniprot.org/annotation/VSP_004578|||http://purl.uniprot.org/annotation/VSP_004579|||http://purl.uniprot.org/annotation/VSP_004580|||http://purl.uniprot.org/annotation/VSP_012383|||http://purl.uniprot.org/annotation/VSP_012384|||http://purl.uniprot.org/annotation/VSP_012385|||http://purl.uniprot.org/annotation/VSP_012386|||http://purl.uniprot.org/annotation/VSP_012387|||http://purl.uniprot.org/annotation/VSP_012388|||http://purl.uniprot.org/annotation/VSP_012389|||http://purl.uniprot.org/annotation/VSP_012390|||http://purl.uniprot.org/annotation/VSP_012391|||http://purl.uniprot.org/annotation/VSP_012392|||http://purl.uniprot.org/annotation/VSP_012393|||http://purl.uniprot.org/annotation/VSP_023326|||http://purl.uniprot.org/annotation/VSP_023327
http://togogenome.org/gene/9606:LYSMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K613|||http://purl.uniprot.org/uniprot/Q7Z3D4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248007|||http://purl.uniprot.org/annotation/VSP_020125|||http://purl.uniprot.org/annotation/VSP_020126|||http://purl.uniprot.org/annotation/VSP_020127|||http://purl.uniprot.org/annotation/VSP_020128
http://togogenome.org/gene/9606:RNPEPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAU8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Aminopeptidase RNPEPL1|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095094|||http://purl.uniprot.org/annotation/VAR_036046
http://togogenome.org/gene/9606:CCNB1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR52|||http://purl.uniprot.org/uniprot/Q9NPC3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Zinc Finger                                                                                  ^@                                                                                  Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-30.|||Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-33.|||Abrogates induction of filamentous growth in yeast; when associated with A-30 and A-33.|||E3 ubiquitin-protein ligase CCNB1IP1|||RING-type|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055874
http://togogenome.org/gene/9606:REG1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48304|||http://purl.uniprot.org/uniprot/Q6ICS1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-type lectin|||Lithostathine-1-beta|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017425|||http://purl.uniprot.org/annotation/PRO_5014310486|||http://purl.uniprot.org/annotation/VAR_050121
http://togogenome.org/gene/9606:MORC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CW-type|||In isoform 2.|||MORC family CW-type zinc finger protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248241|||http://purl.uniprot.org/annotation/VAR_051188|||http://purl.uniprot.org/annotation/VAR_051189|||http://purl.uniprot.org/annotation/VAR_051190|||http://purl.uniprot.org/annotation/VAR_051191|||http://purl.uniprot.org/annotation/VAR_051192|||http://purl.uniprot.org/annotation/VAR_051193|||http://purl.uniprot.org/annotation/VAR_051194|||http://purl.uniprot.org/annotation/VAR_051195|||http://purl.uniprot.org/annotation/VAR_051196|||http://purl.uniprot.org/annotation/VAR_059698|||http://purl.uniprot.org/annotation/VSP_055495
http://togogenome.org/gene/9606:ZBBX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MT70|||http://purl.uniprot.org/uniprot/B7ZMD2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type; atypical|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Zinc finger B-box domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325813|||http://purl.uniprot.org/annotation/VAR_046955|||http://purl.uniprot.org/annotation/VAR_048400|||http://purl.uniprot.org/annotation/VAR_048401|||http://purl.uniprot.org/annotation/VAR_048402|||http://purl.uniprot.org/annotation/VAR_048403|||http://purl.uniprot.org/annotation/VAR_048404|||http://purl.uniprot.org/annotation/VAR_048405|||http://purl.uniprot.org/annotation/VAR_061040|||http://purl.uniprot.org/annotation/VSP_035573|||http://purl.uniprot.org/annotation/VSP_054851
http://togogenome.org/gene/9606:BTRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4P6|||http://purl.uniprot.org/uniprot/B2R8L3|||http://purl.uniprot.org/uniprot/B7Z3H4|||http://purl.uniprot.org/uniprot/Q68DS0|||http://purl.uniprot.org/uniprot/Q9Y297                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to DEPTOR, TFE3 and MITF substrates.|||Abolished binding to TFE3 and MITF substrates.|||F-box|||F-box/WD repeat-containing protein 1A|||Homodimerization domain D|||In isoform 2.|||Required for down-regulation of SNAI1|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050980|||http://purl.uniprot.org/annotation/VAR_020119|||http://purl.uniprot.org/annotation/VAR_022027|||http://purl.uniprot.org/annotation/VSP_006764
http://togogenome.org/gene/9606:IL20RB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXL0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||Interleukin-20 receptor subunit beta|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011038|||http://purl.uniprot.org/annotation/VSP_054905|||http://purl.uniprot.org/annotation/VSP_054906|||http://purl.uniprot.org/annotation/VSP_054907
http://togogenome.org/gene/9606:SPATS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||Spermatogenesis-associated serine-rich protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307697
http://togogenome.org/gene/9606:RHBDL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1Y9|||http://purl.uniprot.org/uniprot/Q9NX52                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes protease activity, prevents processing and alters localization to the plasma membrane of N-terminal fragment.|||Abolishes protease activity.|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Nucleophile|||Peptidase S54 rhomboid|||Reduces protease activity.|||Rhomboid-related protein 2|||Rhomboid-related protein 2, C-terminal fragment|||Rhomboid-related protein 2, N-terminal fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206176|||http://purl.uniprot.org/annotation/PRO_0000408509|||http://purl.uniprot.org/annotation/PRO_0000408510|||http://purl.uniprot.org/annotation/VAR_020328|||http://purl.uniprot.org/annotation/VSP_012692
http://togogenome.org/gene/9606:KRT81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14533                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||In MNLIX.|||Keratin, type II cuticular Hb1|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063696|||http://purl.uniprot.org/annotation/VAR_018113|||http://purl.uniprot.org/annotation/VAR_018114|||http://purl.uniprot.org/annotation/VAR_018115|||http://purl.uniprot.org/annotation/VAR_018116|||http://purl.uniprot.org/annotation/VAR_018117|||http://purl.uniprot.org/annotation/VAR_073048
http://togogenome.org/gene/9606:FBXO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3I1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PSMF1.|||Asymmetric dimethylarginine|||Disordered|||F-box|||F-box only protein 7|||Found in two patients with Kufor-Rakeb syndrome also carrying R-877 in ATP13A2.|||Impairs interaction with PRKN.|||Important for dimerization and interaction with PSMF1|||Important for interaction with CDK6|||Important for interaction with PINK1|||In PARK15; no effect on interaction with PRKN.|||In PARK15; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of SIRT7 ubiquitination.|||Omega-N-methylarginine|||RFDP motif|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119885|||http://purl.uniprot.org/annotation/VAR_021408|||http://purl.uniprot.org/annotation/VAR_047938|||http://purl.uniprot.org/annotation/VAR_066022|||http://purl.uniprot.org/annotation/VAR_084192|||http://purl.uniprot.org/annotation/VSP_041073|||http://purl.uniprot.org/annotation/VSP_041074|||http://purl.uniprot.org/annotation/VSP_044723
http://togogenome.org/gene/9606:PPIP5K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PFW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreases 16-fold the affinity for PtdIns(3,4,5)P3.|||Decreases 8-fold the affinity for PtdIns(3,4,5)P3.|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 7.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1|||Phosphoserine|||Polar residues|||Polyphosphoinositide-binding domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315688|||http://purl.uniprot.org/annotation/VSP_030615|||http://purl.uniprot.org/annotation/VSP_030616|||http://purl.uniprot.org/annotation/VSP_030617|||http://purl.uniprot.org/annotation/VSP_030618|||http://purl.uniprot.org/annotation/VSP_030619|||http://purl.uniprot.org/annotation/VSP_030620|||http://purl.uniprot.org/annotation/VSP_030621|||http://purl.uniprot.org/annotation/VSP_030622|||http://purl.uniprot.org/annotation/VSP_030623|||http://purl.uniprot.org/annotation/VSP_030624
http://togogenome.org/gene/9606:HNRNPUL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1KMD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||Heterogeneous nuclear ribonucleoprotein U-like protein 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278142
http://togogenome.org/gene/9606:UQCRHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Transit Peptide                                                                                  ^@                                                                                  Acidic residues|||Cytochrome b-c1 complex subunit 6-like, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000435432
http://togogenome.org/gene/9606:FSCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9T9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibrous sheath CABYR-binding protein|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089952|||http://purl.uniprot.org/annotation/VAR_035678|||http://purl.uniprot.org/annotation/VAR_035679|||http://purl.uniprot.org/annotation/VAR_035680|||http://purl.uniprot.org/annotation/VAR_056874|||http://purl.uniprot.org/annotation/VAR_056875|||http://purl.uniprot.org/annotation/VAR_056876|||http://purl.uniprot.org/annotation/VAR_056877|||http://purl.uniprot.org/annotation/VAR_056878|||http://purl.uniprot.org/annotation/VAR_056879
http://togogenome.org/gene/9606:FAHD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHE4|||http://purl.uniprot.org/uniprot/Q6P2I3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Fumarylacetoacetase-like C-terminal|||Fumarylacetoacetate hydrolase domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289796
http://togogenome.org/gene/9606:RPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7B2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Brix|||Disordered|||Ribosome production factor 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120223|||http://purl.uniprot.org/annotation/VAR_033639|||http://purl.uniprot.org/annotation/VAR_033640
http://togogenome.org/gene/9606:OR4D11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVQ9|||http://purl.uniprot.org/uniprot/Q8NGI4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150543|||http://purl.uniprot.org/annotation/VAR_034197
http://togogenome.org/gene/9606:GPR146                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2Q3|||http://purl.uniprot.org/uniprot/B4DTD6|||http://purl.uniprot.org/uniprot/Q96CH1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 146                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069622
http://togogenome.org/gene/9606:CST9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W186                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cystatin-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314693|||http://purl.uniprot.org/annotation/VAR_038045
http://togogenome.org/gene/9606:NSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L73|||http://purl.uniprot.org/uniprot/Q96MN8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AWS|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase, H3 lysine-36 specific|||In SOTOS.|||In SOTOS; loss of enzyme activity.|||In SOTOS; strongly reduced enzyme activity.|||In isoform 2.|||In isoform 3.|||Inhibits enzyme activity in the absence of bound histone|||Nearly abolished enzyme activity.|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4; atypical|||PWWP 1|||PWWP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||Reduced enzyme activity.|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186070|||http://purl.uniprot.org/annotation/VAR_015775|||http://purl.uniprot.org/annotation/VAR_015776|||http://purl.uniprot.org/annotation/VAR_015777|||http://purl.uniprot.org/annotation/VAR_015778|||http://purl.uniprot.org/annotation/VAR_015779|||http://purl.uniprot.org/annotation/VAR_015780|||http://purl.uniprot.org/annotation/VAR_015781|||http://purl.uniprot.org/annotation/VAR_015782|||http://purl.uniprot.org/annotation/VAR_015783|||http://purl.uniprot.org/annotation/VAR_015784|||http://purl.uniprot.org/annotation/VAR_015785|||http://purl.uniprot.org/annotation/VAR_015786|||http://purl.uniprot.org/annotation/VAR_015787|||http://purl.uniprot.org/annotation/VAR_015788|||http://purl.uniprot.org/annotation/VAR_015789|||http://purl.uniprot.org/annotation/VAR_015790|||http://purl.uniprot.org/annotation/VAR_015791|||http://purl.uniprot.org/annotation/VAR_015792|||http://purl.uniprot.org/annotation/VAR_015793|||http://purl.uniprot.org/annotation/VAR_015794|||http://purl.uniprot.org/annotation/VAR_015795|||http://purl.uniprot.org/annotation/VSP_007682|||http://purl.uniprot.org/annotation/VSP_007683|||http://purl.uniprot.org/annotation/VSP_007684
http://togogenome.org/gene/9606:SEC14L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495V9|||http://purl.uniprot.org/uniprot/Q6XCI7|||http://purl.uniprot.org/uniprot/Q9UDX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||GOLD|||In isoform 2.|||In isoform 3.|||SEC14-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210758|||http://purl.uniprot.org/annotation/VAR_022097|||http://purl.uniprot.org/annotation/VAR_024627|||http://purl.uniprot.org/annotation/VAR_024628|||http://purl.uniprot.org/annotation/VAR_061787|||http://purl.uniprot.org/annotation/VSP_045553|||http://purl.uniprot.org/annotation/VSP_045554
http://togogenome.org/gene/9606:PARP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0C4|||http://purl.uniprot.org/uniprot/E9PK67|||http://purl.uniprot.org/uniprot/E9PNI7|||http://purl.uniprot.org/uniprot/Q53GL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||Abolishes catalytic activity; abolishes interaction with PARP14.|||Abolishes interaction with PCNA.|||Decreased auto-mono-ADP-ribosylation.|||Decreased catalytic activity.|||Decreased interaction with PCNA.|||Disordered|||Does not affect catalytic activity.|||Myc binding|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||PARP catalytic|||PIP-box|||Phosphoserine|||Phosphothreonine|||Protein mono-ADP-ribosyltransferase PARP10|||Strongly decreased catalytic activity.|||Ubiquitin-interacting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252435|||http://purl.uniprot.org/annotation/VAR_027859|||http://purl.uniprot.org/annotation/VAR_027860|||http://purl.uniprot.org/annotation/VAR_027861
http://togogenome.org/gene/9606:SESN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58004                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished 'Lys-63'-linked ubiquitination by RNF167.|||About two-fold prolonged half-life in cycloheximide/CHX time course.|||Basic and acidic residues|||C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||Decreased affinity for leucine. Requires increased leucine concentration to dissociate from GATOR2 and activate TORC1 signaling.|||Decreased alkylhydroperoxide reductase activity and loss of the ability to decrease intracellular reactive oxygen species. No effect on interaction with the GATOR2 complex. No effect on inhibition of TOR signaling.|||Decreased alkylhydroperoxide reductase activity. No effect on the ability to inhibit the TORC1 signaling pathway.|||Decreased leucine-binding.|||Decreased leucine-binding. Promotes interaction with RNF167.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of interaction with GATOR2. No effect on leucine-binding. Unable to mediate leucine-induced inhibition of the TORC1 signaling pathway.|||Loss of interaction with the GATOR2 complex. No effect on leucine-binding.|||Loss of leucine-binding.|||Loss of leucine-binding. Constitutively interacts with the GATOR2 complex.|||Loss of leucine-binding. Promotes interaction with RNF167. Constitutively interacts with the GATOR2 complex.|||N-acetylmethionine|||N-terminal domain; mediates the alkylhydroperoxide reductase activity|||No effect on ability to decrease intracellular reactive oxygen species.|||No effect on alkylhydroperoxide reductase activity.|||No effect on alkylhydroperoxide reductase activity. Altered ability to decrease intracellular reactive oxygen species. No effect on the ability to inhibit the TORC1 signaling pathway.|||No effect on alkylhydroperoxide reductase activity. Loss of interaction with the GATOR2 complex. Unable to inhibit the TORC1 signaling pathway.|||No effect on alkylhydroperoxide reductase activity. No effect on the ability to inhibit the TORC1 signaling pathway.|||No effect on the ability to inhibit the TORC1 signaling pathway.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-373.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-376.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-385.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-387.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-409 and A-411.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-409 and A-415.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-411 and A-415.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-419 and A-422.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-419 and A-426.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with A-422 and A-426.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with C-128.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with E-113.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with L-259 and R-261.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with R-258 and L-259.|||No effect on the ability to inhibit the TORC1 signaling pathway; when associated with R-258 and R-261.|||Phosphoserine|||Sestrin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221181|||http://purl.uniprot.org/annotation/VAR_022101
http://togogenome.org/gene/9606:SNTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Gamma-2-syntrophin|||In isoform 2.|||PDZ|||PH|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184015|||http://purl.uniprot.org/annotation/VAR_034501|||http://purl.uniprot.org/annotation/VAR_034502|||http://purl.uniprot.org/annotation/VAR_034503|||http://purl.uniprot.org/annotation/VSP_039175
http://togogenome.org/gene/9606:TMEM178B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BS89                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 178B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419261
http://togogenome.org/gene/9606:C1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00736                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||CUB 1|||CUB 2|||Charge relay system|||Complement C1r subcomponent|||Complement C1r subcomponent heavy chain|||Complement C1r subcomponent light chain|||Confirmed at protein level.|||EGF-like; calcium-binding|||In EDSPD1.|||In EDSPD1; requires 2 nucleotide substitutions; the mutant is not secreted but retained intracellularly.|||In EDSPD1; the mutant is not secreted but retained intracellularly.|||In EDSPD1; unknown pathological significance.|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Phosphoserine; by CK2|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027577|||http://purl.uniprot.org/annotation/PRO_0000027578|||http://purl.uniprot.org/annotation/PRO_0000027579|||http://purl.uniprot.org/annotation/VAR_016103|||http://purl.uniprot.org/annotation/VAR_018667|||http://purl.uniprot.org/annotation/VAR_018668|||http://purl.uniprot.org/annotation/VAR_018669|||http://purl.uniprot.org/annotation/VAR_018670|||http://purl.uniprot.org/annotation/VAR_047933|||http://purl.uniprot.org/annotation/VAR_077106|||http://purl.uniprot.org/annotation/VAR_077107|||http://purl.uniprot.org/annotation/VAR_077108|||http://purl.uniprot.org/annotation/VAR_077109|||http://purl.uniprot.org/annotation/VAR_077110|||http://purl.uniprot.org/annotation/VAR_077111|||http://purl.uniprot.org/annotation/VAR_077112|||http://purl.uniprot.org/annotation/VAR_077113|||http://purl.uniprot.org/annotation/VAR_077114|||http://purl.uniprot.org/annotation/VAR_077115|||http://purl.uniprot.org/annotation/VAR_077116|||http://purl.uniprot.org/annotation/VAR_077117|||http://purl.uniprot.org/annotation/VAR_077118|||http://purl.uniprot.org/annotation/VAR_077119
http://togogenome.org/gene/9606:LRRC74A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAA2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Leucine-rich repeat-containing protein 74A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306172|||http://purl.uniprot.org/annotation/VSP_028425|||http://purl.uniprot.org/annotation/VSP_028426|||http://purl.uniprot.org/annotation/VSP_028427
http://togogenome.org/gene/9606:ACTR10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ32                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Actin-related protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089131
http://togogenome.org/gene/9606:MMP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60882                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-20|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028833|||http://purl.uniprot.org/annotation/PRO_0000028834|||http://purl.uniprot.org/annotation/VAR_020511|||http://purl.uniprot.org/annotation/VAR_020512|||http://purl.uniprot.org/annotation/VAR_020513|||http://purl.uniprot.org/annotation/VAR_020514|||http://purl.uniprot.org/annotation/VAR_057802
http://togogenome.org/gene/9606:PTGS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35354                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Aspirin-acetylated serine|||Decreased enzyme activity with arachidonic acid. Loss of cyclooxygenase activity; when associated with V-519.|||Decreased protein stability. Increased decrease of protein stability; when associated with A-516.|||Does not affect activation by nitric oxid (NO).|||EGF-like|||For cyclooxygenase activity|||Impairs two-electron hydroperoxide reduction and cyclooxygenase activity.|||Impairs two-electron hydroperoxide reduction.|||Increases two-electron hydroperoxide reduction. Has no effect on cyclooxygenase activity.|||Loss of cyclooxygenase activity. Loss of cyclooxygenase activity; when associated with T-516.|||N-linked (GlcNAc...) asparagine|||No effect on protein stability. Increased decrease of protein stability; when associated with A-371.|||O-acetylserine|||Prevents activation by nitric oxid (NO).|||Prostaglandin G/H synthase 2|||Proton acceptor|||Reduces two-electron hydroperoxide reduction and cyclooxygenase activity. Catalyzes predominantly one-electron hydroperoxide reduction.|||S-nitrosocysteine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023875|||http://purl.uniprot.org/annotation/VAR_011980|||http://purl.uniprot.org/annotation/VAR_011981|||http://purl.uniprot.org/annotation/VAR_016262|||http://purl.uniprot.org/annotation/VAR_016263|||http://purl.uniprot.org/annotation/VAR_016264
http://togogenome.org/gene/9606:H2BC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4S9|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A/H2B/H3|||Histone H2B type 1-C/E/F/G/I|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:SPHK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV83|||http://purl.uniprot.org/uniprot/E9PCV4|||http://purl.uniprot.org/uniprot/Q9NRA0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage and secretion in apoptotic cells. No effect on kinase activity.|||Abolishes nuclear export in response to PMA treatment.|||Abolishes nuclear export.|||Abolishes phosphorylation.|||Basic and acidic residues|||DAGKc|||Decreases SPP production in nucleus. Abolishes increase of histone acetylation. No effect on association with histone 3.|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of location to cell membrane. Not secreted. No effect on kinase activity.|||No effect on cleavage and secretion in apoptotic cells. No effect on kinase activity.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphoserine; by PKD|||Phosphothreonine; by MAPK|||Proton donor/acceptor|||Reduces phosphorylation levels.|||Required for binding to sulfatide and phosphoinositides and for membrane localizatione|||Sphingosine kinase 2|||Strongly reduces phosphorylation levels.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181358|||http://purl.uniprot.org/annotation/VAR_060112|||http://purl.uniprot.org/annotation/VSP_006217|||http://purl.uniprot.org/annotation/VSP_006218|||http://purl.uniprot.org/annotation/VSP_046910|||http://purl.uniprot.org/annotation/VSP_047721|||http://purl.uniprot.org/annotation/VSP_047722
http://togogenome.org/gene/9606:PRRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14669                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-carboxyglutamate|||Abolishes gamma-carboxylation.|||Abolishes interaction with YAP1.|||Cytoplasmic|||Disordered|||Extracellular|||Gla|||Helical|||Impairs propeptide removal.|||LPXY motif; mediates binding to WW domain-containing proteins|||No effect on interaction with YAP1.|||PPXY motif; mediates binding to WW domain-containing proteins|||Pro residues|||Significantly impairs interaction with YAP1.|||Transmembrane gamma-carboxyglutamic acid protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022543|||http://purl.uniprot.org/annotation/PRO_0000022544|||http://purl.uniprot.org/annotation/VAR_020332|||http://purl.uniprot.org/annotation/VAR_051442
http://togogenome.org/gene/9606:MS4A4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDW1|||http://purl.uniprot.org/uniprot/Q4JF27|||http://purl.uniprot.org/uniprot/Q96JQ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Membrane-spanning 4-domains subfamily A member 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158634|||http://purl.uniprot.org/annotation/VAR_024540|||http://purl.uniprot.org/annotation/VAR_053517|||http://purl.uniprot.org/annotation/VAR_062123|||http://purl.uniprot.org/annotation/VSP_007380
http://togogenome.org/gene/9606:HOXD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09016                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-D4|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200210|||http://purl.uniprot.org/annotation/VAR_067445
http://togogenome.org/gene/9606:CD22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20273|||http://purl.uniprot.org/uniprot/Q0EAF5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B-cell receptor CD22|||Cytoplasmic|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like V-type|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform CD22-alpha.|||N-linked (GlcNAc...) asparagine|||Observed with a marginally higher frequency in patients with systemic lupus erythematosus.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014873|||http://purl.uniprot.org/annotation/PRO_5014306732|||http://purl.uniprot.org/annotation/VAR_003913|||http://purl.uniprot.org/annotation/VAR_003914|||http://purl.uniprot.org/annotation/VAR_003915|||http://purl.uniprot.org/annotation/VAR_003916|||http://purl.uniprot.org/annotation/VAR_014133|||http://purl.uniprot.org/annotation/VAR_014134|||http://purl.uniprot.org/annotation/VAR_014135|||http://purl.uniprot.org/annotation/VAR_049903|||http://purl.uniprot.org/annotation/VSP_002531|||http://purl.uniprot.org/annotation/VSP_045363|||http://purl.uniprot.org/annotation/VSP_047223|||http://purl.uniprot.org/annotation/VSP_047224|||http://purl.uniprot.org/annotation/VSP_054619|||http://purl.uniprot.org/annotation/VSP_054620
http://togogenome.org/gene/9606:TFB1M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KTM5|||http://purl.uniprot.org/uniprot/Q8WVM0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity, DNA-binding and SAM-binding. Does not abolish transcription activator function.|||Abolishes methyltransferase activity. Does not affect SAM-binding, DNA-binding nor transcription activator function.|||Dimethyladenosine transferase 1, mitochondrial|||Does not affect SAM-binding, DNA-binding nor transcription activator function.|||Mitochondrion|||Ribosomal RNA adenine methylase transferase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273171|||http://purl.uniprot.org/annotation/VAR_071246|||http://purl.uniprot.org/annotation/VAR_071247|||http://purl.uniprot.org/annotation/VAR_071248
http://togogenome.org/gene/9606:RIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99578                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  GTP-binding protein Rit2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082727|||http://purl.uniprot.org/annotation/VSP_018102|||http://purl.uniprot.org/annotation/VSP_018103
http://togogenome.org/gene/9606:FBLN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53RD9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||Fibulin-7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313655|||http://purl.uniprot.org/annotation/VAR_037689|||http://purl.uniprot.org/annotation/VSP_030084|||http://purl.uniprot.org/annotation/VSP_030085|||http://purl.uniprot.org/annotation/VSP_030086
http://togogenome.org/gene/9606:IRX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||Iroquois-class homeodomain protein IRX-2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049153
http://togogenome.org/gene/9606:ENOSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5Y1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Impairs protein solubility. Abolishes catalytic activity.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Mitochondrial enolase superfamily member 1|||Phosphoserine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331652|||http://purl.uniprot.org/annotation/VAR_042933|||http://purl.uniprot.org/annotation/VAR_042934|||http://purl.uniprot.org/annotation/VAR_042935|||http://purl.uniprot.org/annotation/VSP_033311|||http://purl.uniprot.org/annotation/VSP_033312|||http://purl.uniprot.org/annotation/VSP_033313|||http://purl.uniprot.org/annotation/VSP_033314|||http://purl.uniprot.org/annotation/VSP_047153|||http://purl.uniprot.org/annotation/VSP_047154|||http://purl.uniprot.org/annotation/VSP_055241|||http://purl.uniprot.org/annotation/VSP_055242|||http://purl.uniprot.org/annotation/VSP_055243
http://togogenome.org/gene/9606:RNF121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JQY5|||http://purl.uniprot.org/uniprot/Q9H920                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin ligase RNF121|||Helical|||In isoform 2.|||N-acetylalanine|||RING-type; atypical|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261407|||http://purl.uniprot.org/annotation/VSP_054133
http://togogenome.org/gene/9606:OR13C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVY9|||http://purl.uniprot.org/uniprot/Q8NGS6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150732|||http://purl.uniprot.org/annotation/VAR_024131
http://togogenome.org/gene/9606:MAU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with CDLS1; unknown pathological significance; no effect on interaction with NIBPL.|||In isoform 2.|||In isoform 3.|||MAU2 chromatid cohesion factor homolog|||Sufficient for interaction with NIPBL|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254548|||http://purl.uniprot.org/annotation/VAR_073019|||http://purl.uniprot.org/annotation/VSP_021223|||http://purl.uniprot.org/annotation/VSP_021224|||http://purl.uniprot.org/annotation/VSP_021225|||http://purl.uniprot.org/annotation/VSP_021226
http://togogenome.org/gene/9606:PCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GoLoco 1|||GoLoco 2|||In isoform 2.|||Phosphoserine|||Polar residues|||Purkinje cell protein 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058260|||http://purl.uniprot.org/annotation/VSP_055654
http://togogenome.org/gene/9606:ZMYND19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E35                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Zinc Finger                                                                                  ^@                                                                                  MYND-type; degenerate|||Zinc finger MYND domain-containing protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218319
http://togogenome.org/gene/9606:CTR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PD62                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA polymerase-associated protein CTR9 homolog|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231588
http://togogenome.org/gene/9606:ANKRD42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1DRY3|||http://purl.uniprot.org/uniprot/A1XPJ0|||http://purl.uniprot.org/uniprot/E9PIL2|||http://purl.uniprot.org/uniprot/E9PKE2|||http://purl.uniprot.org/uniprot/E9PP91|||http://purl.uniprot.org/uniprot/F8W6I9|||http://purl.uniprot.org/uniprot/Q8N9B4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 42|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244371|||http://purl.uniprot.org/annotation/VAR_028366|||http://purl.uniprot.org/annotation/VSP_019559|||http://purl.uniprot.org/annotation/VSP_019560|||http://purl.uniprot.org/annotation/VSP_019561
http://togogenome.org/gene/9606:SHISA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DS77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein shisa-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392536|||http://purl.uniprot.org/annotation/VSP_038817|||http://purl.uniprot.org/annotation/VSP_038818|||http://purl.uniprot.org/annotation/VSP_038819
http://togogenome.org/gene/9606:PGA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1S5UZ02|||http://purl.uniprot.org/uniprot/B7Z719|||http://purl.uniprot.org/uniprot/P0DJD7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Pepsin A-4|||Peptidase A1|||Phosphoserine|||pepsin A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415757|||http://purl.uniprot.org/annotation/PRO_0000415758|||http://purl.uniprot.org/annotation/PRO_5013265911|||http://purl.uniprot.org/annotation/PRO_5014274681
http://togogenome.org/gene/9606:ZNF567                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R956|||http://purl.uniprot.org/uniprot/B4E0D0|||http://purl.uniprot.org/uniprot/Q8N184                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2.|||KRAB|||Zinc finger protein 567                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047658|||http://purl.uniprot.org/annotation/VSP_016383|||http://purl.uniprot.org/annotation/VSP_016384
http://togogenome.org/gene/9606:CLDN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95500                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-14|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNB29.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144769|||http://purl.uniprot.org/annotation/VAR_010738|||http://purl.uniprot.org/annotation/VAR_017227|||http://purl.uniprot.org/annotation/VAR_069979|||http://purl.uniprot.org/annotation/VAR_069980|||http://purl.uniprot.org/annotation/VAR_069981|||http://purl.uniprot.org/annotation/VAR_069982|||http://purl.uniprot.org/annotation/VAR_069983
http://togogenome.org/gene/9606:DYNC2I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK66|||http://purl.uniprot.org/uniprot/Q8WVS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Binding to the DYNLT2B-DYNLT1/DYNLT3 dimer|||Cytoplasmic dynein 2 intermediate chain 1|||Disordered|||In SRTD8.|||In SRTD8; Reduces interaction with IFT proteins.|||In SRTD8; does not affect interaction with DYNC2I2.|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242142|||http://purl.uniprot.org/annotation/VAR_026841|||http://purl.uniprot.org/annotation/VAR_026842|||http://purl.uniprot.org/annotation/VAR_070197|||http://purl.uniprot.org/annotation/VAR_079178|||http://purl.uniprot.org/annotation/VAR_083839
http://togogenome.org/gene/9606:ZNF683                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ20                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||Disordered|||In isoform 2.|||Tissue-resident T-cell transcription regulator protein ZNF683                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234002|||http://purl.uniprot.org/annotation/VAR_026155|||http://purl.uniprot.org/annotation/VAR_057442|||http://purl.uniprot.org/annotation/VAR_057443|||http://purl.uniprot.org/annotation/VAR_057444|||http://purl.uniprot.org/annotation/VAR_057445|||http://purl.uniprot.org/annotation/VSP_018167
http://togogenome.org/gene/9606:MARF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4F3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||HTH OST-type 1|||HTH OST-type 2|||HTH OST-type 3|||HTH OST-type 4|||HTH OST-type 5|||HTH OST-type 6|||HTH OST-type 7|||HTH OST-type 8|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Meiosis regulator and mRNA stability factor 1|||NYN|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000276846|||http://purl.uniprot.org/annotation/VSP_022988|||http://purl.uniprot.org/annotation/VSP_037755|||http://purl.uniprot.org/annotation/VSP_037756|||http://purl.uniprot.org/annotation/VSP_037757|||http://purl.uniprot.org/annotation/VSP_037758|||http://purl.uniprot.org/annotation/VSP_037759
http://togogenome.org/gene/9606:SLAIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R9T6|||http://purl.uniprot.org/uniprot/Q9P270                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Abolishes interaction with CLIP1.|||Basic and acidic residues|||Disordered|||Important for interaction with CLIP1|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SLAIN motif-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316965
http://togogenome.org/gene/9606:POM121L12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7R1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||POM121-like protein 12|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348453|||http://purl.uniprot.org/annotation/VAR_046180|||http://purl.uniprot.org/annotation/VAR_046181|||http://purl.uniprot.org/annotation/VAR_046182
http://togogenome.org/gene/9606:SCNN1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51172                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amiloride-sensitive sodium channel subunit delta|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181282|||http://purl.uniprot.org/annotation/VAR_028209|||http://purl.uniprot.org/annotation/VAR_028210|||http://purl.uniprot.org/annotation/VAR_028211|||http://purl.uniprot.org/annotation/VAR_028212|||http://purl.uniprot.org/annotation/VAR_028213|||http://purl.uniprot.org/annotation/VAR_028214|||http://purl.uniprot.org/annotation/VSP_060000|||http://purl.uniprot.org/annotation/VSP_060001|||http://purl.uniprot.org/annotation/VSP_060002
http://togogenome.org/gene/9606:TMEM229B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBD8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Transmembrane protein 229B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263681
http://togogenome.org/gene/9606:MTRES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEI0|||http://purl.uniprot.org/uniprot/Q9P0P8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Transit Peptide                                                                                  ^@                                                                                  Acidic residues|||Decreased RNA-binding; when associated with A-143; A-145: A-149 and A-156. Does not rescue diminished mitochondrial transcription induced by EtBr; when associated with A-143; A-145: A-149 and A-156.|||Decreased RNA-binding; when associated with A-143; A-145: A-149 and A-158. Does not rescue diminished mitochondrial transcription induced by EtBr; when associated with A-143; A-145: A-149 and A-158.|||Decreased RNA-binding; when associated with A-143; A-145: A-156 and A-158. Does not rescue diminished mitochondrial transcription induced by EtBr; when associated with A-143; A-149: A-156 and A-158.|||Decreased RNA-binding; when associated with A-143; A-149: A-156 and A-158. Does not rescue diminished mitochondrial transcription induced by EtBr; when associated with A-143; A-149: A-156 and A-158.|||Decreased RNA-binding; when associated with A-145; A-149: A-156 and A-158. Does not rescue diminished mitochondrial transcription induced by EtBr; when associated with A-145; A-149: A-156 and A-158.|||Disordered|||Mitochondrial transcription rescue factor 1|||Mitochondrion|||Phosphoserine|||S4 RNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089559
http://togogenome.org/gene/9606:C15orf39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Uncharacterized protein C15orf39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244343|||http://purl.uniprot.org/annotation/VAR_026891|||http://purl.uniprot.org/annotation/VAR_026892|||http://purl.uniprot.org/annotation/VAR_026893|||http://purl.uniprot.org/annotation/VAR_026894|||http://purl.uniprot.org/annotation/VSP_019538|||http://purl.uniprot.org/annotation/VSP_019539|||http://purl.uniprot.org/annotation/VSP_019540|||http://purl.uniprot.org/annotation/VSP_019541
http://togogenome.org/gene/9606:RTP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QGT7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Cytoplasmic|||Extracellular|||Helical|||Receptor-transporting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181991|||http://purl.uniprot.org/annotation/VAR_021488
http://togogenome.org/gene/9606:SLC16A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSM3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes creatine efflux activity. Does not affect plasma membrane localization.|||Cytoplasmic|||Decreases creatine efflux activity. Loss of localization to the plasma membrane.|||Decreases in the creatine efflux activity. Does not affect plasma membrane localization.|||Does not affect creatine efflux activity.|||Does not affect creatine efflux activity. Does not affect plasma membrane localization.|||Found in a patient with age-related cataract; unknown pathological significance; decreases creatine transport.|||Helical|||In CTRCT47; loss of localization to the plasma membrane; retained in the endoplasmic reticulum where it undergoes degradation by the proteasome; has no dominant effect on wild-type protein expression and localization.|||Monocarboxylate transporter 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286675|||http://purl.uniprot.org/annotation/VAR_071890|||http://purl.uniprot.org/annotation/VAR_080957
http://togogenome.org/gene/9606:DCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43146|||http://purl.uniprot.org/uniprot/Q49AK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MYO10.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In HGPPS2; unknown pathological significance.|||In MRMV1.|||In MRMV1; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In a colorectal carcinoma.|||In a esophageal carcinoma.|||Interaction with MYO10|||N-linked (GlcNAc...) asparagine|||Netrin receptor DCC|||Phosphoserine; by MAPK1|||Phosphothreonine; by MAPK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014744|||http://purl.uniprot.org/annotation/VAR_003909|||http://purl.uniprot.org/annotation/VAR_003910|||http://purl.uniprot.org/annotation/VAR_003911|||http://purl.uniprot.org/annotation/VAR_024495|||http://purl.uniprot.org/annotation/VAR_035511|||http://purl.uniprot.org/annotation/VAR_056043|||http://purl.uniprot.org/annotation/VAR_060257|||http://purl.uniprot.org/annotation/VAR_060258|||http://purl.uniprot.org/annotation/VAR_060259|||http://purl.uniprot.org/annotation/VAR_079145|||http://purl.uniprot.org/annotation/VAR_079146|||http://purl.uniprot.org/annotation/VAR_079147|||http://purl.uniprot.org/annotation/VAR_079148|||http://purl.uniprot.org/annotation/VAR_079149|||http://purl.uniprot.org/annotation/VAR_079150|||http://purl.uniprot.org/annotation/VAR_079151|||http://purl.uniprot.org/annotation/VAR_079152|||http://purl.uniprot.org/annotation/VAR_079153|||http://purl.uniprot.org/annotation/VAR_079287
http://togogenome.org/gene/9606:OR1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGR6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150416|||http://purl.uniprot.org/annotation/VAR_053114|||http://purl.uniprot.org/annotation/VAR_053115|||http://purl.uniprot.org/annotation/VAR_053116|||http://purl.uniprot.org/annotation/VAR_053117
http://togogenome.org/gene/9606:C4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C0L4                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anaphylatoxin-like|||C4a anaphylatoxin|||C4b-A|||C4d-A|||Complement C4 beta chain|||Complement C4 gamma chain|||Complement C4-A alpha chain|||In allotype C4A1, allotype C4A13.|||In allotype C4A1, allotype C4A2.|||In allotype C4A1, allotype C4A3a, allotype C4A6.|||In allotype C4A1.|||In allotype C4A3a, allotype C4A6.|||In allotype C4A3a.|||In allotype C4A4.|||In allotype C4A6.|||In isoform 2.|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||NTR|||O-linked (GalNAc...) threonine|||Phosphoserine; by FAM20C|||Responsible for effective binding to form amide bonds with immune aggregates or protein antigens|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005966|||http://purl.uniprot.org/annotation/PRO_0000005967|||http://purl.uniprot.org/annotation/PRO_0000005968|||http://purl.uniprot.org/annotation/PRO_0000005969|||http://purl.uniprot.org/annotation/PRO_0000005970|||http://purl.uniprot.org/annotation/PRO_0000005971|||http://purl.uniprot.org/annotation/PRO_0000005972|||http://purl.uniprot.org/annotation/PRO_0000042698|||http://purl.uniprot.org/annotation/VAR_001987|||http://purl.uniprot.org/annotation/VAR_001988|||http://purl.uniprot.org/annotation/VAR_001992|||http://purl.uniprot.org/annotation/VAR_001993|||http://purl.uniprot.org/annotation/VAR_001994|||http://purl.uniprot.org/annotation/VAR_001995|||http://purl.uniprot.org/annotation/VAR_019778|||http://purl.uniprot.org/annotation/VAR_019779|||http://purl.uniprot.org/annotation/VAR_019780|||http://purl.uniprot.org/annotation/VAR_069154|||http://purl.uniprot.org/annotation/VAR_069155|||http://purl.uniprot.org/annotation/VAR_069156|||http://purl.uniprot.org/annotation/VAR_069158|||http://purl.uniprot.org/annotation/VAR_069159|||http://purl.uniprot.org/annotation/VSP_046252
http://togogenome.org/gene/9606:NAA50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EQ69|||http://purl.uniprot.org/uniprot/Q9GZZ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes N-alpha-acetyltransferase activity.|||Decreased acetylation; when associated with 34-A-A-37.|||Decreased acetylation; when associated with A-140.|||In isoform 2.|||N-acetyltransferase|||N-alpha-acetyltransferase 50|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphothreonine|||Phosphotyrosine|||Reduces N-alpha-acetyltransferase activity.|||Restores the acetylation activity of the NatA complex.|||Strongly decreased N-alpha-acetyltransferase activity.|||Strongly decreased N-alpha-acetyltransferase activity. Impaired sister chromatid cohesion during mitosis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284902|||http://purl.uniprot.org/annotation/VSP_024747
http://togogenome.org/gene/9606:TNNC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J7T9|||http://purl.uniprot.org/uniprot/P02585                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In CMYP15; affects regulation of muscle contraction.|||N-acetylthreonine|||Removed|||Troponin C, skeletal muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073703|||http://purl.uniprot.org/annotation/VAR_087978|||http://purl.uniprot.org/annotation/VAR_087979
http://togogenome.org/gene/9606:ARPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15144                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 2|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124033
http://togogenome.org/gene/9606:ZNF628                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EBL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X approximate tandem repeats|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Interaction with TAF4B|||Phosphothreonine|||Pro residues|||Zinc finger protein 628                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246070
http://togogenome.org/gene/9606:GPR88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 88                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069597|||http://purl.uniprot.org/annotation/VAR_054767|||http://purl.uniprot.org/annotation/VAR_054768
http://togogenome.org/gene/9606:UIMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RL1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  AIR|||Abolishes interaction with histone monoubiquitinated H2B without affecting the interaction with H2A.|||Abolishes phosphorylation at this position.|||BRCA1-A complex subunit RAP80|||Basic and acidic residues|||Disordered|||Does not affect symoylation; when associated with A-19; A-31; A-52 and A-61.|||Does not affect symoylation; when associated with A-9; A-19; A-31 and A-52.|||Does not affect symoylation; when associated with A-9; A-19; A-31 and A-61.|||Does not affect symoylation; when associated with A-9; A-19; A-52 and A-61.|||Does not affect symoylation; when associated with A-9; A-31; A-52 and A-61.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs localization to DNA damages sites; when associated with A-92; S-113 and A-117.|||Impairs localization to DNA damages sites; when associated with S-88; S-113 and A-117.|||Impairs the selectivity for 'K-63'-linked ubiquitin.|||Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and A-117.|||Impairs ubiquitin-binding and localization to DNA damages sites; when associated with S-88; A-92 and S-113.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increases the selectivity for 'K-63'-linked ubiquitin.|||LR motif|||Necessary for interaction with NR6A1 C-terminus|||Necessary for interaction with NR6A1 N-terminus|||Necessary for transcriptional repression|||Not associated with susceptibility to breast cancer.|||Phosphoserine|||Polar residues|||Slightly impairs the selectivity for 'K-63'-linked ubiquitin.|||Strongly reduces ubiquitin binding via UIM 1.|||UBZ4-type|||UIM 1|||UIM 2|||UIM-linker|||Zinc-finger-like region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097547|||http://purl.uniprot.org/annotation/VAR_051469|||http://purl.uniprot.org/annotation/VAR_051470|||http://purl.uniprot.org/annotation/VAR_051471|||http://purl.uniprot.org/annotation/VAR_051472|||http://purl.uniprot.org/annotation/VAR_055328|||http://purl.uniprot.org/annotation/VSP_012932|||http://purl.uniprot.org/annotation/VSP_012933|||http://purl.uniprot.org/annotation/VSP_012934|||http://purl.uniprot.org/annotation/VSP_012935|||http://purl.uniprot.org/annotation/VSP_037264|||http://purl.uniprot.org/annotation/VSP_037265
http://togogenome.org/gene/9606:ARK2N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B23                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Increased phosphorylation. Increases muscle specific force.|||Loss of phosphorylation by AMPK. Decreases muscle specific force.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues|||Protein ARK2N|||Required for interaction with CSNK2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079312|||http://purl.uniprot.org/annotation/VAR_080245|||http://purl.uniprot.org/annotation/VSP_014753
http://togogenome.org/gene/9606:SLC2A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dileucine internalization motif|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 2, facilitated glucose transporter member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050373|||http://purl.uniprot.org/annotation/VAR_025426|||http://purl.uniprot.org/annotation/VSP_041402
http://togogenome.org/gene/9606:CEP41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 41 kDa|||Disordered|||Found in a patient with Meckel syndrome; unknown pathological significance.|||Found in a patient with autism; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries a truncating mutation in CC2D2A.|||Probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries a truncating mutation in KIF7.|||Probable disease-associated variant found in a patient with Joubert syndrome; digenic inheritance; the patient also carries mutation A-1447 in CC2D2A.|||Rhodanese                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089489|||http://purl.uniprot.org/annotation/VAR_067053|||http://purl.uniprot.org/annotation/VAR_067054|||http://purl.uniprot.org/annotation/VAR_067055|||http://purl.uniprot.org/annotation/VAR_067056|||http://purl.uniprot.org/annotation/VAR_067057|||http://purl.uniprot.org/annotation/VAR_067058|||http://purl.uniprot.org/annotation/VSP_012246|||http://purl.uniprot.org/annotation/VSP_012247|||http://purl.uniprot.org/annotation/VSP_012248|||http://purl.uniprot.org/annotation/VSP_042579
http://togogenome.org/gene/9606:CT45A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMV1|||http://purl.uniprot.org/uniprot/P0DMV2|||http://purl.uniprot.org/uniprot/Q5DJT8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A2|||Cancer/testis antigen family 45 member A8|||Cancer/testis antigen family 45 member A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308947|||http://purl.uniprot.org/annotation/PRO_0000433030|||http://purl.uniprot.org/annotation/PRO_0000433031
http://togogenome.org/gene/9606:HIVEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15822                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||CCHC HIVEP-type|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047369|||http://purl.uniprot.org/annotation/VAR_057383|||http://purl.uniprot.org/annotation/VAR_057384|||http://purl.uniprot.org/annotation/VAR_057385|||http://purl.uniprot.org/annotation/VAR_057386|||http://purl.uniprot.org/annotation/VAR_057387|||http://purl.uniprot.org/annotation/VAR_057388|||http://purl.uniprot.org/annotation/VAR_057389|||http://purl.uniprot.org/annotation/VAR_057390|||http://purl.uniprot.org/annotation/VAR_057391|||http://purl.uniprot.org/annotation/VAR_057392|||http://purl.uniprot.org/annotation/VAR_059892|||http://purl.uniprot.org/annotation/VAR_059893|||http://purl.uniprot.org/annotation/VSP_037714|||http://purl.uniprot.org/annotation/VSP_037715|||http://purl.uniprot.org/annotation/VSP_037716|||http://purl.uniprot.org/annotation/VSP_037717
http://togogenome.org/gene/9606:ABHD12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5M8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 5.|||In isoform 4.|||In isoform 5.|||Protein ABHD12B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089887|||http://purl.uniprot.org/annotation/VAR_019100|||http://purl.uniprot.org/annotation/VAR_035676|||http://purl.uniprot.org/annotation/VSP_010687|||http://purl.uniprot.org/annotation/VSP_010688|||http://purl.uniprot.org/annotation/VSP_010689|||http://purl.uniprot.org/annotation/VSP_041149|||http://purl.uniprot.org/annotation/VSP_041150
http://togogenome.org/gene/9606:TRIM46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUH1|||http://purl.uniprot.org/uniprot/B7Z4F9|||http://purl.uniprot.org/uniprot/F5GYK0|||http://purl.uniprot.org/uniprot/Q7Z4K8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||COS|||Disordered|||Fibronectin type-III|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Phosphoserine|||Polar residues|||RING-type 1; degenerate|||RING-type 2; degenerate|||Required for microtubule association, proximal axon localization and axon formation|||Required for proximal axon localization, axon formation and migration|||Tripartite motif-containing protein 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056268|||http://purl.uniprot.org/annotation/VSP_011980|||http://purl.uniprot.org/annotation/VSP_011981|||http://purl.uniprot.org/annotation/VSP_011982|||http://purl.uniprot.org/annotation/VSP_011983|||http://purl.uniprot.org/annotation/VSP_011984|||http://purl.uniprot.org/annotation/VSP_045976
http://togogenome.org/gene/9606:H4C11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:EIF4E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSA5|||http://purl.uniprot.org/uniprot/B8ZZ50|||http://purl.uniprot.org/uniprot/B8ZZL3|||http://purl.uniprot.org/uniprot/B9A023|||http://purl.uniprot.org/uniprot/O60573|||http://purl.uniprot.org/uniprot/Q53RG0|||http://purl.uniprot.org/uniprot/Q59FE1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Ability to bind capped mRNA reduced to 13% of wild-type.|||Ability to bind capped mRNA reduced to 40% of wild-type.|||Ability to bind capped mRNA reduced to less than 10% of wild-type.|||Basic and acidic residues|||Disordered|||Does not affect ubiquitination by ARIH1; when associated with R-121; R-130 and R-134.|||Does not affect ubiquitination by ARIH1; when associated with R-121; R-130 and R-222.|||Does not affect ubiquitination by ARIH1; when associated with R-121; R-134 and R-222.|||Does not affect ubiquitination by ARIH1; when associated with R-130; R-134 and R-222.|||EIF4EBP1/2/3 binding|||Eukaryotic translation initiation factor 4E type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Phosphoserine|||Slight reduction in ability to bind capped mRNA.|||Unable to bind capped mRNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193664|||http://purl.uniprot.org/annotation/VSP_054783|||http://purl.uniprot.org/annotation/VSP_054784
http://togogenome.org/gene/9606:SLC36A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495N2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Proton-coupled amino acid transporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326204|||http://purl.uniprot.org/annotation/VAR_040006|||http://purl.uniprot.org/annotation/VAR_040007|||http://purl.uniprot.org/annotation/VAR_040008|||http://purl.uniprot.org/annotation/VAR_040009|||http://purl.uniprot.org/annotation/VAR_040010|||http://purl.uniprot.org/annotation/VSP_032601|||http://purl.uniprot.org/annotation/VSP_032602
http://togogenome.org/gene/9606:KDM5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29375                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARID|||Abolishes DNA-binding.|||Abolishes interaction with histone H3 di- and trimethylated at 'Lys-4'.|||Breakpoint for translocation to form the NUP98-KDM5A fusion protein|||C5HC2|||Decreases DNA-binding.|||Disordered|||GSGFP motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with LMO2|||JmjC|||JmjN|||Lysine-specific demethylase 5A|||No effect on interaction with histone H3 di- and trimethylated at 'Lys-4'.|||No effect on lysine-specific histone demethylase activity; when associated with S-626.|||No effect on lysine-specific histone demethylase activity; when associated with S-636.|||PHD-type 1|||PHD-type 2|||PHD-type 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200584|||http://purl.uniprot.org/annotation/VAR_032984|||http://purl.uniprot.org/annotation/VAR_032985|||http://purl.uniprot.org/annotation/VSP_035746
http://togogenome.org/gene/9606:PLPP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPM3|||http://purl.uniprot.org/uniprot/Q8NBV4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Inactive phospholipid phosphatase 7|||Interaction with MTOR|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239401|||http://purl.uniprot.org/annotation/VAR_026646|||http://purl.uniprot.org/annotation/VAR_026647
http://togogenome.org/gene/9606:ACAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJX1|||http://purl.uniprot.org/uniprot/P24752                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acetyl-CoA acetyltransferase, mitochondrial|||Acyl-thioester intermediate|||In 3KTD.|||In 3KTD; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity.|||In 3KTD; decreased protein abundance; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity.|||In 3KTD; decreased protein stability.|||In 3KTD; decreased protein stability; decreased acetyl-CoAC-acyltransferase activity; less than 10% of the degradative/thiolase activity.|||In 3KTD; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity.|||In 3KTD; loss of protein solubility; loss of acetyl-CoAC-acyltransferase activity; no degradative/thiolase activity.|||In 3KTD; no activity.|||In isoform 2.|||Increases nucleophilicity of active site Cys|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Proton donor/acceptor|||Thiolase C-terminal|||Thiolase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034085|||http://purl.uniprot.org/annotation/VAR_007496|||http://purl.uniprot.org/annotation/VAR_007497|||http://purl.uniprot.org/annotation/VAR_007498|||http://purl.uniprot.org/annotation/VAR_007499|||http://purl.uniprot.org/annotation/VAR_007500|||http://purl.uniprot.org/annotation/VAR_007501|||http://purl.uniprot.org/annotation/VAR_007502|||http://purl.uniprot.org/annotation/VAR_007503|||http://purl.uniprot.org/annotation/VAR_007504|||http://purl.uniprot.org/annotation/VAR_007505|||http://purl.uniprot.org/annotation/VAR_007506|||http://purl.uniprot.org/annotation/VAR_007507|||http://purl.uniprot.org/annotation/VSP_056844|||http://purl.uniprot.org/annotation/VSP_056845
http://togogenome.org/gene/9606:NIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQR4|||http://purl.uniprot.org/uniprot/V9HW91                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mass|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  CN hydrolase|||Less than 3% of wild-type activity using succinamate as substrate.|||Loss of activity using succinamate as substrate.|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Omega-amidase NIT2|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320252|||http://purl.uniprot.org/annotation/VAR_039180
http://togogenome.org/gene/9606:EPHA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21709                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 1|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016798|||http://purl.uniprot.org/annotation/VAR_028265|||http://purl.uniprot.org/annotation/VAR_028266|||http://purl.uniprot.org/annotation/VAR_028267|||http://purl.uniprot.org/annotation/VAR_042115|||http://purl.uniprot.org/annotation/VAR_042116|||http://purl.uniprot.org/annotation/VAR_042117|||http://purl.uniprot.org/annotation/VAR_042118|||http://purl.uniprot.org/annotation/VAR_042119|||http://purl.uniprot.org/annotation/VAR_042120|||http://purl.uniprot.org/annotation/VSP_056010|||http://purl.uniprot.org/annotation/VSP_056011|||http://purl.uniprot.org/annotation/VSP_056012|||http://purl.uniprot.org/annotation/VSP_056013
http://togogenome.org/gene/9606:STRA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJF1|||http://purl.uniprot.org/uniprot/Q7Z7C7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Found in patients with non-obstructive azoospermia; unknown pathological significance.|||Nuclear localization signal (NLS)|||Stimulated by retinoic acid gene 8 protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318114|||http://purl.uniprot.org/annotation/VAR_081144
http://togogenome.org/gene/9606:PYGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11216                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Glycogen phosphorylase, brain form|||Involved in the association of subunits|||May be involved in allosteric control|||N-acetylalanine|||N6-(pyridoxal phosphate)lysine|||Participates in a stacking interaction with the adenine ring of AMP|||Phosphoserine; by PHK; in form phosphorylase A|||Phosphotyrosine|||Pyridoxal 5'-phosphate|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188535|||http://purl.uniprot.org/annotation/VAR_020212|||http://purl.uniprot.org/annotation/VAR_034428
http://togogenome.org/gene/9606:ARID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 2|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CSS6.|||In isoform 2.|||LXXLL|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RFX-type winged-helix|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200577|||http://purl.uniprot.org/annotation/VAR_080566|||http://purl.uniprot.org/annotation/VAR_080567|||http://purl.uniprot.org/annotation/VSP_015230
http://togogenome.org/gene/9606:EXOSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AMU3|||http://purl.uniprot.org/uniprot/Q9Y3B2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exosome complex component CSL4|||Exosome complex component CSL4 C-terminal|||Exosome complex component N-terminal|||In PCH1F; decreased protein abundance.|||Phosphoserine|||S1 motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087127|||http://purl.uniprot.org/annotation/VAR_085726
http://togogenome.org/gene/9606:LYSMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S90                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247996|||http://purl.uniprot.org/annotation/VSP_041083
http://togogenome.org/gene/9606:KRT25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZPD6|||http://purl.uniprot.org/uniprot/Q7Z3Z0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In ARWH3.|||In ARWH3; disruption of keratin intermediate filament formation formed via heterodimerization with KRT5.|||In ARWH3; reduces keratin intermediate filamen formation; impairs cytoskeleton assembly.|||Keratin, type I cytoskeletal 25|||Linker 1|||Linker 12|||Phosphoserine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312691|||http://purl.uniprot.org/annotation/VAR_049786|||http://purl.uniprot.org/annotation/VAR_076303|||http://purl.uniprot.org/annotation/VAR_076304|||http://purl.uniprot.org/annotation/VAR_079711
http://togogenome.org/gene/9606:FXYD6-FXYD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ82|||http://purl.uniprot.org/uniprot/A0A0A6YYL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FXYD domain-containing ion transport regulator|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5011328018|||http://purl.uniprot.org/annotation/PRO_5011332577
http://togogenome.org/gene/9606:NKIRAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYR9                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Effector region|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NF-kappa-B inhibitor-interacting Ras-like protein 2|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225679|||http://purl.uniprot.org/annotation/VSP_017412|||http://purl.uniprot.org/annotation/VSP_043151|||http://purl.uniprot.org/annotation/VSP_044873|||http://purl.uniprot.org/annotation/VSP_044874
http://togogenome.org/gene/9606:KIAA0408                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU52                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Uncharacterized protein KIAA0408                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247177|||http://purl.uniprot.org/annotation/VAR_027082|||http://purl.uniprot.org/annotation/VAR_049510|||http://purl.uniprot.org/annotation/VSP_019942
http://togogenome.org/gene/9606:PHF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR4|||http://purl.uniprot.org/uniprot/A0A1U9X8A3|||http://purl.uniprot.org/uniprot/O43189                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes histone H3K36me3-binding and localization at double-strand breaks (DSBs).|||Abolishes histone H3K36me3-binding.|||Basic and acidic residues|||Disordered|||Impairs histone H3K36me3-binding.|||In isoform 1.|||PHD finger protein 1|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059288|||http://purl.uniprot.org/annotation/VAR_034382|||http://purl.uniprot.org/annotation/VAR_044500|||http://purl.uniprot.org/annotation/VSP_004694|||http://purl.uniprot.org/annotation/VSP_004695
http://togogenome.org/gene/9606:MRPL30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCC3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein uL30m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261649|||http://purl.uniprot.org/annotation/VAR_034462|||http://purl.uniprot.org/annotation/VSP_021746|||http://purl.uniprot.org/annotation/VSP_021747
http://togogenome.org/gene/9606:CLEC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PHK0|||http://purl.uniprot.org/uniprot/P05452                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-type lectin|||In MCDR4; leads to thinning in both the outer nuclear layer and whole retina and to impaired retinal function, when tested in a heterologous system.|||O-linked (GalNAc...) threonine|||Tetranectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017471|||http://purl.uniprot.org/annotation/VAR_004189|||http://purl.uniprot.org/annotation/VAR_004190|||http://purl.uniprot.org/annotation/VAR_012318|||http://purl.uniprot.org/annotation/VAR_087508
http://togogenome.org/gene/9606:TPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29144|||http://purl.uniprot.org/uniprot/Q5VZU9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Charge relay system|||Disordered|||Found in a patient diagnosed with multiple sclerosis; unknown pathological significance.|||Found in a patient diagnosed with multiple sclerosis; unknown pathological significance; decreased protein abundance; not changed aminopeptidase activity.|||In IMD78; decreased protein abundance; decreased aminopeptidase activity.|||In IMD78; loss of expression.|||N-acetylalanine|||N6-acetyllysine|||Peptidase S8|||Peptidase S8/S53|||Phosphoserine|||Removed|||Tripeptidyl peptidase II Ig-like|||Tripeptidyl-peptidase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076422|||http://purl.uniprot.org/annotation/VAR_085640|||http://purl.uniprot.org/annotation/VAR_085641|||http://purl.uniprot.org/annotation/VAR_085642|||http://purl.uniprot.org/annotation/VAR_085643
http://togogenome.org/gene/9606:AGPAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRZ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-acyl-sn-glycerol-3-phosphate acyltransferase gamma|||Cytoplasmic|||HXXXXD motif|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208194|||http://purl.uniprot.org/annotation/VSP_005072|||http://purl.uniprot.org/annotation/VSP_013144
http://togogenome.org/gene/9606:SEC63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5M1|||http://purl.uniprot.org/uniprot/Q9UGP8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Helical|||In PCLD2.|||J|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces cotranslational translocation of APLN precursor/preproapelin.|||SEC63 1|||SEC63 2|||Translocation protein SEC63 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071097|||http://purl.uniprot.org/annotation/VAR_019645|||http://purl.uniprot.org/annotation/VAR_061146|||http://purl.uniprot.org/annotation/VAR_080944|||http://purl.uniprot.org/annotation/VAR_080945|||http://purl.uniprot.org/annotation/VAR_080946|||http://purl.uniprot.org/annotation/VAR_080947|||http://purl.uniprot.org/annotation/VAR_080948|||http://purl.uniprot.org/annotation/VAR_080949|||http://purl.uniprot.org/annotation/VAR_080950|||http://purl.uniprot.org/annotation/VAR_080951|||http://purl.uniprot.org/annotation/VAR_080952
http://togogenome.org/gene/9606:RTL8C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6ZKI3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Retrotransposon Gag-like protein 8C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311726|||http://purl.uniprot.org/annotation/VAR_053975
http://togogenome.org/gene/9606:OR6C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW44|||http://purl.uniprot.org/uniprot/Q9NZP0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150625|||http://purl.uniprot.org/annotation/VAR_034245|||http://purl.uniprot.org/annotation/VAR_053218|||http://purl.uniprot.org/annotation/VAR_053219
http://togogenome.org/gene/9606:PCDHGA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003962|||http://purl.uniprot.org/annotation/VAR_048564|||http://purl.uniprot.org/annotation/VAR_061070|||http://purl.uniprot.org/annotation/VSP_008673|||http://purl.uniprot.org/annotation/VSP_008674
http://togogenome.org/gene/9606:COL4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08572                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3'-bromotyrosine|||Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins.|||Basic and acidic residues|||Canstatin|||Collagen IV NC1|||Collagen alpha-2(IV) chain|||Disordered|||Does not affect COL4A2 and COL4A1 secretion.|||In BSVD2.|||In BSVD2; incomplete penetrance.|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide (7S domain)|||Pro residues|||Probable disease-associated variant found in a family with porencephaly and small-vessel disease in the form of scattered white matter lesions; impairs COL4A2 and COL4A1 secretion; the mutant protein is retained in the endoplasmic reticulum.|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005824|||http://purl.uniprot.org/annotation/PRO_0000005825|||http://purl.uniprot.org/annotation/PRO_0000283775|||http://purl.uniprot.org/annotation/VAR_048796|||http://purl.uniprot.org/annotation/VAR_048797|||http://purl.uniprot.org/annotation/VAR_067551|||http://purl.uniprot.org/annotation/VAR_067552|||http://purl.uniprot.org/annotation/VAR_067553|||http://purl.uniprot.org/annotation/VAR_067554|||http://purl.uniprot.org/annotation/VAR_067555|||http://purl.uniprot.org/annotation/VAR_067556|||http://purl.uniprot.org/annotation/VAR_067557|||http://purl.uniprot.org/annotation/VAR_067558|||http://purl.uniprot.org/annotation/VAR_067836|||http://purl.uniprot.org/annotation/VAR_067837|||http://purl.uniprot.org/annotation/VAR_067838
http://togogenome.org/gene/9606:DDB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16531                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA damage-binding protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with AMBRA1, DTL and DCAF5.|||Impairs interaction with AMBRA1, DTL, DET1, DCAF1, DCAF5, DCAF11 and DCAF8.|||Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11.|||Impairs interaction with DDA1.|||In WHIKERS.|||In isoform 2.|||Interaction with CDT1|||Interaction with CDT1 and CUL4A|||N-acetylserine|||N6-acetyllysine|||Phosphothreonine|||Removed|||Slightly impairs interaction with CUL4A.|||Strongly impairs interaction with CUL4A.|||WD repeat beta-propeller A|||WD repeat beta-propeller B; Interaction with CUL4A|||WD repeat beta-propeller C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079840|||http://purl.uniprot.org/annotation/VAR_023074|||http://purl.uniprot.org/annotation/VAR_086005|||http://purl.uniprot.org/annotation/VAR_086006|||http://purl.uniprot.org/annotation/VAR_086007|||http://purl.uniprot.org/annotation/VAR_086008|||http://purl.uniprot.org/annotation/VAR_086009|||http://purl.uniprot.org/annotation/VSP_055540
http://togogenome.org/gene/9606:VPS52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1B4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar protein sorting-associated protein 52 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213315|||http://purl.uniprot.org/annotation/VSP_056476
http://togogenome.org/gene/9606:ATPSCKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4H8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ATP synthase subunit C lysine N-methyltransferase|||Abolished protein-lysine N-methyltransferase activity and ability to promote chronic pain.|||Abolished protein-lysine N-methyltransferase activity.|||Helical|||In isoform 2.|||N-acetylmethionine|||Required for mitochondrial location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321536|||http://purl.uniprot.org/annotation/VAR_039345|||http://purl.uniprot.org/annotation/VAR_039346|||http://purl.uniprot.org/annotation/VAR_039347|||http://purl.uniprot.org/annotation/VAR_039348|||http://purl.uniprot.org/annotation/VSP_044724
http://togogenome.org/gene/9606:PELO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRX2                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to rescue stalled ribosomes.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Protein pelota homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143188|||http://purl.uniprot.org/annotation/VAR_019777
http://togogenome.org/gene/9606:NEURL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EH8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase NEURL3|||NHR|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325771
http://togogenome.org/gene/9606:ZNF620                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNG0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||KRAB|||Zinc finger protein 620                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047691|||http://purl.uniprot.org/annotation/VSP_016040
http://togogenome.org/gene/9606:UBAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH66|||http://purl.uniprot.org/uniprot/B7Z7P2|||http://purl.uniprot.org/uniprot/Q5T6F2|||http://purl.uniprot.org/uniprot/Q9P0H6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||UBA|||Ubiquitin-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270981|||http://purl.uniprot.org/annotation/VAR_029834|||http://purl.uniprot.org/annotation/VAR_029835|||http://purl.uniprot.org/annotation/VAR_052677|||http://purl.uniprot.org/annotation/VAR_052678|||http://purl.uniprot.org/annotation/VAR_052679|||http://purl.uniprot.org/annotation/VSP_056073
http://togogenome.org/gene/9606:B3GALNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTQ4|||http://purl.uniprot.org/uniprot/O75752|||http://purl.uniprot.org/uniprot/Q49AT3|||http://purl.uniprot.org/uniprot/Q7L9G8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with P1(k) phenotype.|||Associated with P2(k) phenotype.|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219153|||http://purl.uniprot.org/annotation/VAR_019646|||http://purl.uniprot.org/annotation/VAR_019647|||http://purl.uniprot.org/annotation/VAR_025091
http://togogenome.org/gene/9606:SLC22A23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5C7|||http://purl.uniprot.org/uniprot/Q9UFY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 22 member 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308315|||http://purl.uniprot.org/annotation/VSP_028954|||http://purl.uniprot.org/annotation/VSP_028955|||http://purl.uniprot.org/annotation/VSP_028956
http://togogenome.org/gene/9606:GBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VY47|||http://purl.uniprot.org/uniprot/P52951                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein GBX-2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048880
http://togogenome.org/gene/9606:DKC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIY6|||http://purl.uniprot.org/uniprot/O60832                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dyskerin-like|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||H/ACA ribonucleoprotein complex subunit DKC1|||In DKCX and HHS; increases interaction with SHQ1.|||In DKCX.|||In DKCX; decreases interaction with SHQ1.|||In DKCX; due to a 2 nucleotide inversion.|||In DKCX; increases interaction with SHQ1.|||In DKCX; requires 2 nucleotide substitutions.|||In DKCX; results in mislocalization of the telomerase complex without affecting telomerase activity.|||In HHS.|||In HHS; increases interaction with SHQ1.|||In HHS; no effect on interaction with SHQ1.|||In isoform 3.|||Increases interaction with SHQ1.|||N-acetylalanine|||Nuclear and nucleolar localization|||Nucleolar localization|||Nucleophile|||PUA|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121983|||http://purl.uniprot.org/annotation/VAR_006811|||http://purl.uniprot.org/annotation/VAR_006812|||http://purl.uniprot.org/annotation/VAR_006813|||http://purl.uniprot.org/annotation/VAR_006814|||http://purl.uniprot.org/annotation/VAR_006815|||http://purl.uniprot.org/annotation/VAR_009264|||http://purl.uniprot.org/annotation/VAR_010076|||http://purl.uniprot.org/annotation/VAR_010077|||http://purl.uniprot.org/annotation/VAR_010078|||http://purl.uniprot.org/annotation/VAR_010079|||http://purl.uniprot.org/annotation/VAR_010080|||http://purl.uniprot.org/annotation/VAR_010081|||http://purl.uniprot.org/annotation/VAR_010082|||http://purl.uniprot.org/annotation/VAR_010083|||http://purl.uniprot.org/annotation/VAR_010084|||http://purl.uniprot.org/annotation/VAR_015674|||http://purl.uniprot.org/annotation/VAR_015675|||http://purl.uniprot.org/annotation/VAR_015676|||http://purl.uniprot.org/annotation/VAR_022553|||http://purl.uniprot.org/annotation/VAR_063821|||http://purl.uniprot.org/annotation/VAR_063822|||http://purl.uniprot.org/annotation/VAR_063823|||http://purl.uniprot.org/annotation/VAR_063824|||http://purl.uniprot.org/annotation/VAR_063825|||http://purl.uniprot.org/annotation/VAR_080707|||http://purl.uniprot.org/annotation/VSP_042422
http://togogenome.org/gene/9606:TEKT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In SPGF81; unknown pathological significance; loss of protein expression in vivo in patient's spermatozoa, but no effect in transfected cells.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Tektin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184568|||http://purl.uniprot.org/annotation/VAR_024658|||http://purl.uniprot.org/annotation/VAR_024659|||http://purl.uniprot.org/annotation/VAR_034550|||http://purl.uniprot.org/annotation/VAR_053721|||http://purl.uniprot.org/annotation/VAR_088218|||http://purl.uniprot.org/annotation/VAR_088219
http://togogenome.org/gene/9606:CRIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZV1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Antistasin-like 1|||Antistasin-like 2|||Antistasin-like 3|||Antistasin-like 4|||Cell attachment site|||Cysteine-rich motor neuron 1 protein|||Cytoplasmic|||Extracellular|||Helical|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Processed cysteine-rich motor neuron 1 protein|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021001|||http://purl.uniprot.org/annotation/PRO_0000296243|||http://purl.uniprot.org/annotation/VAR_050907|||http://purl.uniprot.org/annotation/VAR_061625
http://togogenome.org/gene/9606:CBX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QYP2|||http://purl.uniprot.org/uniprot/O95931|||http://purl.uniprot.org/uniprot/Q4PNR6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chromo|||Chromobox protein homolog 7|||Disordered|||Loss of cellular lifespan extension.|||Loss of interaction with RNF2.|||Reduced interaction with RNF2.|||Required for cellular lifespan extension                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080212
http://togogenome.org/gene/9606:TBATA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSR7|||http://purl.uniprot.org/uniprot/A0A8I5KS30|||http://purl.uniprot.org/uniprot/B7ZMN4|||http://purl.uniprot.org/uniprot/B7ZMN5|||http://purl.uniprot.org/uniprot/Q96M53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Protein TBATA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089786|||http://purl.uniprot.org/annotation/VAR_022998|||http://purl.uniprot.org/annotation/VSP_035483|||http://purl.uniprot.org/annotation/VSP_035484
http://togogenome.org/gene/9606:SPMIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LM5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein SPMIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325755|||http://purl.uniprot.org/annotation/VAR_039901|||http://purl.uniprot.org/annotation/VAR_039902|||http://purl.uniprot.org/annotation/VAR_039903|||http://purl.uniprot.org/annotation/VAR_039904|||http://purl.uniprot.org/annotation/VAR_039905
http://togogenome.org/gene/9606:CCNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH21|||http://purl.uniprot.org/uniprot/O60583                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Activation of HIV-1 Tat function.|||Basic and acidic residues|||Basic residues|||Cyclin N-terminal|||Cyclin-T2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with MDFIC and MDFI|||Interaction with POLR2A|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080495|||http://purl.uniprot.org/annotation/VSP_001258
http://togogenome.org/gene/9606:NDUFS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z792|||http://purl.uniprot.org/uniprot/O75306                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MC1DN6.|||In MC1DN6; loss of catalytic activity; no change in Km value for ubiquinone-1.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial|||NADH-quinone oxidoreductase subunit D|||Symmetric dimethylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019981|||http://purl.uniprot.org/annotation/VAR_019535|||http://purl.uniprot.org/annotation/VAR_019536|||http://purl.uniprot.org/annotation/VAR_019537|||http://purl.uniprot.org/annotation/VAR_034150|||http://purl.uniprot.org/annotation/VAR_034151|||http://purl.uniprot.org/annotation/VAR_034152|||http://purl.uniprot.org/annotation/VAR_071891|||http://purl.uniprot.org/annotation/VAR_084193|||http://purl.uniprot.org/annotation/VSP_046466
http://togogenome.org/gene/9606:GIPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In DFNB15.|||PDZ|||PDZ domain-containing protein GIPC3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247191|||http://purl.uniprot.org/annotation/VAR_065967|||http://purl.uniprot.org/annotation/VAR_065968|||http://purl.uniprot.org/annotation/VAR_065969|||http://purl.uniprot.org/annotation/VAR_065970|||http://purl.uniprot.org/annotation/VAR_065971|||http://purl.uniprot.org/annotation/VAR_065972|||http://purl.uniprot.org/annotation/VAR_065973
http://togogenome.org/gene/9606:RAB23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULC3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||In CRPT1.|||Phosphoserine|||Polar residues|||Ras-related protein Rab-23|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121211|||http://purl.uniprot.org/annotation/PRO_0000370771|||http://purl.uniprot.org/annotation/VAR_017159|||http://purl.uniprot.org/annotation/VAR_034900|||http://purl.uniprot.org/annotation/VAR_034901|||http://purl.uniprot.org/annotation/VAR_034902|||http://purl.uniprot.org/annotation/VAR_034903|||http://purl.uniprot.org/annotation/VAR_065294|||http://purl.uniprot.org/annotation/VAR_065295
http://togogenome.org/gene/9606:PTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TNI1|||http://purl.uniprot.org/uniprot/P21246                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Chondroitin sulfate A binding|||Chondroitin sulfate binding|||Disordered|||Pleiotrophin|||Pleiotrophin/Midkine C-terminal|||Pleiotrophin/Midkine N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024659|||http://purl.uniprot.org/annotation/PRO_5036463064
http://togogenome.org/gene/9606:MED9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWA0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Mediator of RNA polymerase II transcription subunit 9|||N-acetylalanine|||Phosphoserine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304147
http://togogenome.org/gene/9606:CTAG1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78358                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cancer/testis antigen 1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218922|||http://purl.uniprot.org/annotation/VSP_028548
http://togogenome.org/gene/9606:FOXP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLK5|||http://purl.uniprot.org/uniprot/O15409|||http://purl.uniprot.org/uniprot/Q8N6B5|||http://purl.uniprot.org/uniprot/Q8N6B6|||http://purl.uniprot.org/uniprot/X5D2H2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||CTBP1-binding|||Disordered|||FOXP coiled-coil|||Fork-head|||Forkhead box protein P2|||In SPCH1; reduced interaction with TBR1.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Leucine-zipper|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091879|||http://purl.uniprot.org/annotation/VAR_012278|||http://purl.uniprot.org/annotation/VSP_001558|||http://purl.uniprot.org/annotation/VSP_011532|||http://purl.uniprot.org/annotation/VSP_011533|||http://purl.uniprot.org/annotation/VSP_011534|||http://purl.uniprot.org/annotation/VSP_011535|||http://purl.uniprot.org/annotation/VSP_011536|||http://purl.uniprot.org/annotation/VSP_011537|||http://purl.uniprot.org/annotation/VSP_011538|||http://purl.uniprot.org/annotation/VSP_011539|||http://purl.uniprot.org/annotation/VSP_043464
http://togogenome.org/gene/9606:CHRNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11230                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetylcholine receptor subunit beta|||Cytoplasmic|||Extracellular|||Helical|||In CMS2A.|||In CMS2A; slow-channel mutation; increases gating equilibrium constant by 33-fold, owing to increased opening rate and decreased closing rate; no effect on the choline dissociation rate constant.|||In CMS2C; impairs AChR assembly by disrupting a specific interaction between beta and delta subunits.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by Tyr-kinases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000315|||http://purl.uniprot.org/annotation/VAR_000287|||http://purl.uniprot.org/annotation/VAR_000288|||http://purl.uniprot.org/annotation/VAR_017494|||http://purl.uniprot.org/annotation/VAR_048169|||http://purl.uniprot.org/annotation/VAR_070842|||http://purl.uniprot.org/annotation/VAR_077363|||http://purl.uniprot.org/annotation/VSP_056675
http://togogenome.org/gene/9606:TNFAIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21580                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A20-type 1|||A20-type 2|||A20-type 3|||A20-type 4|||A20-type 5|||A20-type 6|||A20-type 7|||A20p37|||A20p50|||Abolishes interactionj with YWHAZ and YWHAH; no effect on inhibitory activity of TNF-induced NF-kappa-B activation.|||Cleavage; by MALT1|||Disordered|||Impairs polyubiquitin binding, abolishes inhibition of IKK activation.|||Impairs polyubiquitin binding, abolishes inhibition of IKK activation; when associated with A-779.|||Impairs polyubiquitin binding, abolishes inhibition of IKK activation; when associated with A-782.|||Impairs ubiquitination activity. Loss of down-regulation of NF-kappa-B activity; when associated with A-614.|||Impairs ubiquitination activity. Loss of down-regulation of NF-kappa-B activity; when associated with A-615 or R-626.|||In AIFBL1; increases inflammatory cytokine secretion; increases NF-kappaB signaling.|||Interaction with RIPK1|||Interaction with TNIP1|||Interaction with ubiquitin|||Loss of 'Lys-63' deubiquitinating activity. Down-regulation of TNF-induced NF-kappa-B activity less effective.|||Loss of deubiquitinase activity.|||Marked attenuation of ubiquitin ligase activity and inhibition of RIPK1 degradation; when associated with A-624.|||Marked attenuation of ubiquitin ligase activity and inhibition of RIPK1 degradation; when associated with A-627.|||Minor effect on 'Lys-48' deubiquitinase activity.|||Minor effect on 'Lys-48' deubiquitinase activity. Strongly reduced 'Lys-63' deubiquitinase activity.|||N-acetylalanine|||No effect on ubiquitin ligase activity; when associated with A-521.|||No effect on ubiquitin ligase activity; when associated with A-524.|||Nucleophile|||OTU|||Phosphoserine|||Polar residues|||Proton acceptor|||Reduces deubiquitinase activity.|||Removed|||Required for lysosomal localization and for TRAF2 lysosomal degradation|||Required for proteasomal degradation of UBE2N and UBE2D3, TRAF6 deubiquitination, and TAX1BP1 interaction with UBE2N|||Strongly reduced 'Lys-48' deubiquitinase activity.|||Strongly reduced deubiquitinase activity.|||Sufficient for inhibitory activity of TNF-induced NF-kappa-B activity|||TRAF-binding|||Tumor necrosis factor alpha-induced protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188791|||http://purl.uniprot.org/annotation/PRO_0000418127|||http://purl.uniprot.org/annotation/PRO_0000418128|||http://purl.uniprot.org/annotation/VAR_020447|||http://purl.uniprot.org/annotation/VAR_022143|||http://purl.uniprot.org/annotation/VAR_029319|||http://purl.uniprot.org/annotation/VAR_076302
http://togogenome.org/gene/9606:ITGA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E282|||http://purl.uniprot.org/uniprot/O75578                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||Helical|||In isoform 2.|||In isoform 3.|||Integrin alpha-10|||N-linked (GlcNAc...) asparagine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016317|||http://purl.uniprot.org/annotation/VAR_027768|||http://purl.uniprot.org/annotation/VAR_027769|||http://purl.uniprot.org/annotation/VAR_027770|||http://purl.uniprot.org/annotation/VAR_034026|||http://purl.uniprot.org/annotation/VAR_034027|||http://purl.uniprot.org/annotation/VSP_013114|||http://purl.uniprot.org/annotation/VSP_013115|||http://purl.uniprot.org/annotation/VSP_054483
http://togogenome.org/gene/9606:NLRP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59047                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; unknown pathological significance.|||Found in a patient with Silver-Russell syndrome and multi-locus imprinting disturbance; unknown pathological significance.|||Found in a patient with features of Silver-Russell syndrome and multi-locus imprinting disturbance; unknown pathological significance.|||Found in a patient with mild cognitive retardation and multi-locus imprinting disturbance; unknown pathological significance.|||Found in an individual with no overt clinical disease and multi-locus imprinting disturbance; unknown pathological significance.|||Found in patients with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; when associated in cis with Q-76; unknown pathological significance.|||Found in patients with Beckwith-Wiedemann syndrome and multi-locus imprinting disturbance; when associated in cis with T-52; unknown pathological significance.|||Found in patients with female infertility; unknown pathological significance.|||Found in patients with female infertility; unknown pathological significance; reduces protein abundance in oocytes and embryos.|||Found in patients with female infertility; when associated in cis with C-462; unknown pathological significance.|||Found in patients with female infertility; when associated in cis with P-143; unknown pathological significance.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NACHT, LRR and PYD domains-containing protein 5|||Polar residues|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080890|||http://purl.uniprot.org/annotation/VAR_060095|||http://purl.uniprot.org/annotation/VAR_060096|||http://purl.uniprot.org/annotation/VAR_060097|||http://purl.uniprot.org/annotation/VAR_060098|||http://purl.uniprot.org/annotation/VAR_060099|||http://purl.uniprot.org/annotation/VAR_060100|||http://purl.uniprot.org/annotation/VAR_060101|||http://purl.uniprot.org/annotation/VAR_060102|||http://purl.uniprot.org/annotation/VAR_084173|||http://purl.uniprot.org/annotation/VAR_084174|||http://purl.uniprot.org/annotation/VAR_084175|||http://purl.uniprot.org/annotation/VAR_084176|||http://purl.uniprot.org/annotation/VAR_084570|||http://purl.uniprot.org/annotation/VAR_084571|||http://purl.uniprot.org/annotation/VAR_084572|||http://purl.uniprot.org/annotation/VAR_084573|||http://purl.uniprot.org/annotation/VAR_084574|||http://purl.uniprot.org/annotation/VAR_084575|||http://purl.uniprot.org/annotation/VAR_084576|||http://purl.uniprot.org/annotation/VAR_084577|||http://purl.uniprot.org/annotation/VAR_084578|||http://purl.uniprot.org/annotation/VAR_084579|||http://purl.uniprot.org/annotation/VAR_084580|||http://purl.uniprot.org/annotation/VAR_084581|||http://purl.uniprot.org/annotation/VAR_084582|||http://purl.uniprot.org/annotation/VAR_084583|||http://purl.uniprot.org/annotation/VAR_084584
http://togogenome.org/gene/9606:DNAAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kintoun                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089911|||http://purl.uniprot.org/annotation/VAR_024309|||http://purl.uniprot.org/annotation/VAR_057788|||http://purl.uniprot.org/annotation/VSP_008390
http://togogenome.org/gene/9606:OR8D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVG3|||http://purl.uniprot.org/uniprot/Q9GZM6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150660|||http://purl.uniprot.org/annotation/VAR_024117|||http://purl.uniprot.org/annotation/VAR_053244
http://togogenome.org/gene/9606:PADI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULW8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In UHS1; forms large aggregates; decreases protein-arginine deiminase activity.|||In a breast cancer sample; somatic mutation.|||Protein-arginine deiminase type-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220029|||http://purl.uniprot.org/annotation/VAR_020462|||http://purl.uniprot.org/annotation/VAR_020463|||http://purl.uniprot.org/annotation/VAR_035502|||http://purl.uniprot.org/annotation/VAR_053558|||http://purl.uniprot.org/annotation/VAR_053559|||http://purl.uniprot.org/annotation/VAR_078023|||http://purl.uniprot.org/annotation/VAR_078024|||http://purl.uniprot.org/annotation/VAR_078025
http://togogenome.org/gene/9606:CEP128                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU80|||http://purl.uniprot.org/uniprot/Q86TS1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 128 kDa|||Disordered|||In isoform 1.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089946|||http://purl.uniprot.org/annotation/VAR_037835|||http://purl.uniprot.org/annotation/VAR_037836|||http://purl.uniprot.org/annotation/VSP_014752|||http://purl.uniprot.org/annotation/VSP_030194|||http://purl.uniprot.org/annotation/VSP_030195|||http://purl.uniprot.org/annotation/VSP_030196
http://togogenome.org/gene/9606:PEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MQX5|||http://purl.uniprot.org/uniprot/Q9UBV8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 9 AA approximate tandem repeat of [AP]-P-G-G-P-Y-G-G-P-P|||Decreased ubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex.|||Disordered|||Does not affect ubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex.|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Peflin|||Pro residues|||Required for interaction with PDCD6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247045
http://togogenome.org/gene/9606:DAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61803|||http://purl.uniprot.org/uniprot/Q53G02                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1|||Helical|||Lumenal|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124009|||http://purl.uniprot.org/annotation/VAR_018825
http://togogenome.org/gene/9606:UTP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969X6                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in patients with North American Indian childhood cirrhosis; unknown pathological significance; does not affect nucleolar protein location; decreased interaction with HIVEP1 measured in yeast two-hybrid screening.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||U3 small nucleolar RNA-associated protein 4 homolog|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050908|||http://purl.uniprot.org/annotation/VAR_017445|||http://purl.uniprot.org/annotation/VAR_053388|||http://purl.uniprot.org/annotation/VSP_009201|||http://purl.uniprot.org/annotation/VSP_009202|||http://purl.uniprot.org/annotation/VSP_009203
http://togogenome.org/gene/9606:ATG2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAZ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Autophagy-related protein 2 homolog A|||Chorein N-terminal|||Decreased interaction with WDR45/WIPI4 and ability to promote autophagy.|||Disordered|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, E-101, R-167, E-171, R-193, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, E-171, R-193, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-193, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-193, R-200, E-223, R-285 and R-304.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-193, R-200, E-223, R-285 and R-328. In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, K-167, R-171, E-193, K-259 and E-285.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-193, R-200, E-223, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-193, R-200, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, E-171, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, E-101, R-167, R-193, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-54, R-82, R-167, E-171, R-193, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 1; abolished lipid transfer activity; when associated with R-82, E-101, R-167, E-171, R-193, R-200, E-223, R-285, R-304 and R-328.|||In Mutant 2; abolished lipid transfer activity; when associated with D-103, K-167, R-171, E-193, K-259, E-285 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, K-167, E-193, K-259, E-285 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, K-167, R-171, E-193, E-285 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, K-167, R-171, E-193, K-259 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, K-167, R-171, K-259, E-285 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80, D-103, R-171, E-193, K-259, E-285 and R-304.|||In Mutant 2; abolished lipid transfer activity; when associated with E-80,K-167, R-171, E-193, K-259, E-285 and R-304.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||WIPI-interacting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315234|||http://purl.uniprot.org/annotation/VAR_038158|||http://purl.uniprot.org/annotation/VAR_038159|||http://purl.uniprot.org/annotation/VAR_038160|||http://purl.uniprot.org/annotation/VAR_061027|||http://purl.uniprot.org/annotation/VAR_061028|||http://purl.uniprot.org/annotation/VAR_061029|||http://purl.uniprot.org/annotation/VSP_030510|||http://purl.uniprot.org/annotation/VSP_030511|||http://purl.uniprot.org/annotation/VSP_030512|||http://purl.uniprot.org/annotation/VSP_030515|||http://purl.uniprot.org/annotation/VSP_030516
http://togogenome.org/gene/9606:SLCO2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92959                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In PHOAD; unknown pathological significance.|||In PHOAR2 and PHOAD.|||In PHOAR2 and PHOAD; unknown pathological significance.|||In PHOAR2.|||In PHOAR2; reduced activity.|||In PHOAR2; unknown pathological significance.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191058|||http://purl.uniprot.org/annotation/VAR_053674|||http://purl.uniprot.org/annotation/VAR_067598|||http://purl.uniprot.org/annotation/VAR_067599|||http://purl.uniprot.org/annotation/VAR_068352|||http://purl.uniprot.org/annotation/VAR_068636|||http://purl.uniprot.org/annotation/VAR_068637|||http://purl.uniprot.org/annotation/VAR_068638|||http://purl.uniprot.org/annotation/VAR_068639|||http://purl.uniprot.org/annotation/VAR_068640|||http://purl.uniprot.org/annotation/VAR_068641|||http://purl.uniprot.org/annotation/VAR_068642|||http://purl.uniprot.org/annotation/VAR_068643|||http://purl.uniprot.org/annotation/VAR_068644|||http://purl.uniprot.org/annotation/VAR_068645|||http://purl.uniprot.org/annotation/VAR_085955|||http://purl.uniprot.org/annotation/VAR_085956|||http://purl.uniprot.org/annotation/VAR_085957|||http://purl.uniprot.org/annotation/VAR_085958|||http://purl.uniprot.org/annotation/VAR_085959|||http://purl.uniprot.org/annotation/VAR_085960|||http://purl.uniprot.org/annotation/VAR_085961|||http://purl.uniprot.org/annotation/VAR_085962|||http://purl.uniprot.org/annotation/VAR_085963|||http://purl.uniprot.org/annotation/VAR_085964
http://togogenome.org/gene/9606:UBL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11441                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of polyubiquitination by AMFR.|||No effect on interaction with BAG6.|||Phosphoserine|||Reduces tail-anchored proteins delivery.|||Required and sufficient for interaction with BAG6|||Strongly inhibits interaction with BAG6.|||Ubiquitin-like|||Ubiquitin-like protein 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114864
http://togogenome.org/gene/9606:KCNA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17658                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with epilepsy and neurodevelopmental anomalies; unknown pathological significance; affects channel properties resulting in slower channel deactivation.|||Found in a patient with epilepsy but without evidence of neurodevelopmental impairment; unknown pathological significance; affects channel properties resulting in slower channel deactivation.|||Found in a patient with neurodevelopmental anomalies; unknown pathological significance.|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 6|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053990|||http://purl.uniprot.org/annotation/VAR_087560|||http://purl.uniprot.org/annotation/VAR_087561|||http://purl.uniprot.org/annotation/VAR_087562|||http://purl.uniprot.org/annotation/VAR_087563
http://togogenome.org/gene/9606:ZNF518A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AHZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein 518A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240849|||http://purl.uniprot.org/annotation/VAR_046310|||http://purl.uniprot.org/annotation/VAR_046311|||http://purl.uniprot.org/annotation/VSP_019436
http://togogenome.org/gene/9606:LRIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeats and immunoglobulin-like domains protein 1|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014827|||http://purl.uniprot.org/annotation/VAR_031581|||http://purl.uniprot.org/annotation/VAR_031582|||http://purl.uniprot.org/annotation/VAR_031583|||http://purl.uniprot.org/annotation/VAR_031584|||http://purl.uniprot.org/annotation/VAR_031585|||http://purl.uniprot.org/annotation/VAR_049889|||http://purl.uniprot.org/annotation/VAR_049890|||http://purl.uniprot.org/annotation/VSP_011730|||http://purl.uniprot.org/annotation/VSP_011731
http://togogenome.org/gene/9606:ND4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9EC08|||http://purl.uniprot.org/uniprot/P03905                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance.|||Helical|||In LDYT; possible rare primary mutation; decrease in enzyme activity.|||In LHON; primary mutation; almost no vision recovery; most frequent mutation; seems to have no effect on electron transfer activity of the complex in inner mitochondrial membrane preparations.|||In MELAS.|||NADH-ubiquinone oxidoreductase chain 4|||NADH:quinone oxidoreductase/Mrp antiporter membrane subunit|||NADH:ubiquinone oxidoreductase chain 4 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117942|||http://purl.uniprot.org/annotation/VAR_004759|||http://purl.uniprot.org/annotation/VAR_004760|||http://purl.uniprot.org/annotation/VAR_008393|||http://purl.uniprot.org/annotation/VAR_008599|||http://purl.uniprot.org/annotation/VAR_008600|||http://purl.uniprot.org/annotation/VAR_008601|||http://purl.uniprot.org/annotation/VAR_008602|||http://purl.uniprot.org/annotation/VAR_064565
http://togogenome.org/gene/9606:ZNRF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWF5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||Abolishes glycosylation; when associated with S-107 and S-152.|||Abolishes glycosylation; when associated with S-107 and S-229.|||Abolishes glycosylation; when associated with S-152 and S-229.|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase ZNRF4|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277861|||http://purl.uniprot.org/annotation/VAR_030611|||http://purl.uniprot.org/annotation/VAR_030612|||http://purl.uniprot.org/annotation/VAR_030613|||http://purl.uniprot.org/annotation/VAR_030614|||http://purl.uniprot.org/annotation/VAR_030615|||http://purl.uniprot.org/annotation/VAR_030616|||http://purl.uniprot.org/annotation/VAR_030617|||http://purl.uniprot.org/annotation/VAR_030618
http://togogenome.org/gene/9606:STXBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00186                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Mediates interaction with DOC2B|||Syntaxin-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206285|||http://purl.uniprot.org/annotation/VAR_017570|||http://purl.uniprot.org/annotation/VAR_017571|||http://purl.uniprot.org/annotation/VAR_052470
http://togogenome.org/gene/9606:CYSTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1C7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cysteine-rich and transmembrane domain-containing protein 1|||Disordered|||Helical|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296358|||http://purl.uniprot.org/annotation/VAR_034629
http://togogenome.org/gene/9606:CRYGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07316                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Gamma-crystallin B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057586|||http://purl.uniprot.org/annotation/VAR_021140|||http://purl.uniprot.org/annotation/VAR_021141|||http://purl.uniprot.org/annotation/VAR_029517
http://togogenome.org/gene/9606:SCN11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI33                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||Helical; Voltage-sensor; Name=S4 of repeat I|||Helical; Voltage-sensor; Name=S4 of repeat II|||Helical; Voltage-sensor; Name=S4 of repeat III|||Helical; Voltage-sensor; Name=S4 of repeat IV|||I|||II|||III|||IV|||In FEPS3.|||In FEPS3; causes hyperexcitability of dorsal root ganglion neurons; hyperpolarizes channel activation; slows deactivation; depolarizes steady-state fast-inactivation.|||In FEPS3; increased voltage-gated sodium channel activity; causes hyperexcitability of dorsal root ganglion neurons; depolarizes resting membrane potential; enhances spontaneous firing; hyperpolarizes channel activation; slows deactivation; decreases rates of current decay; does not change slow-inactivation.|||In FEPS3; increased voltage-gated sodium channel activity; slows deactivation; depolarizes resting membrane potential; enhances spontaneous firing; decreases rates of current decay; does not change fast-inactivation; does not change slow-inactivation.|||In HSAN7; cold-aggravated peripheral pain seen in some patients; enhances the channel activity by shifting the voltage dependence of channel opening to hyperpolarized potentials thereby giving rise to hyperexcitability of nociceptors; causes hyperexcitability and reduced cold-sensitivity of dorsal root ganglion neurons.|||In HSAN7; increased voltage-gated sodium channel activity; results in excessive channel activity at resting voltages; causes sustained depolarization of nociceptors and impaired generation of action potentials; causes aberrant synaptic transmission; causes transient hyperexcitability of dorsal root ganglion neurons.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pore-forming|||Sodium channel protein type 11 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048510|||http://purl.uniprot.org/annotation/VAR_030002|||http://purl.uniprot.org/annotation/VAR_030003|||http://purl.uniprot.org/annotation/VAR_030004|||http://purl.uniprot.org/annotation/VAR_048697|||http://purl.uniprot.org/annotation/VAR_070919|||http://purl.uniprot.org/annotation/VAR_070920|||http://purl.uniprot.org/annotation/VAR_070921|||http://purl.uniprot.org/annotation/VAR_075250|||http://purl.uniprot.org/annotation/VAR_076679|||http://purl.uniprot.org/annotation/VAR_076680|||http://purl.uniprot.org/annotation/VAR_076681|||http://purl.uniprot.org/annotation/VAR_076682|||http://purl.uniprot.org/annotation/VAR_076683|||http://purl.uniprot.org/annotation/VAR_076684|||http://purl.uniprot.org/annotation/VAR_076685|||http://purl.uniprot.org/annotation/VAR_076686|||http://purl.uniprot.org/annotation/VAR_076687|||http://purl.uniprot.org/annotation/VAR_076688|||http://purl.uniprot.org/annotation/VAR_076689|||http://purl.uniprot.org/annotation/VAR_076690|||http://purl.uniprot.org/annotation/VSP_012259|||http://purl.uniprot.org/annotation/VSP_012260|||http://purl.uniprot.org/annotation/VSP_012261
http://togogenome.org/gene/9606:HTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15515                                                                                  ^@                                                                                  Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Mass|||Modified Residue|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  His1-(31-57)-peptide|||Histatin-1|||Not post-translationally modified.|||Phosphoserine|||Sulfotyrosine; in submandibular gland form|||with 1 phosphate group and 1 sulfate group.|||with 1 phosphate group and 2 sulfate groups.|||with 1 phosphate group and 3 sulfate groups.|||with 1 phosphate group and 4 sulfate groups.|||with 1 phosphate group.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021416|||http://purl.uniprot.org/annotation/PRO_0000021417
http://togogenome.org/gene/9606:LRRC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6Y2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT 1|||LRRCT 2|||LRRNT|||Leucine-rich repeat-containing protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021608|||http://purl.uniprot.org/annotation/VAR_051103|||http://purl.uniprot.org/annotation/VAR_051104|||http://purl.uniprot.org/annotation/VAR_051105|||http://purl.uniprot.org/annotation/VSP_011424|||http://purl.uniprot.org/annotation/VSP_011425
http://togogenome.org/gene/9606:ST3GAL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXB8|||http://purl.uniprot.org/uniprot/Q9Y274                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Type 2 lactosamine alpha-2,3-sialyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149305|||http://purl.uniprot.org/annotation/VAR_049227|||http://purl.uniprot.org/annotation/VSP_047009|||http://purl.uniprot.org/annotation/VSP_047010
http://togogenome.org/gene/9606:RANGRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD47                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased binding to RAN.|||Decreased binding to RAN. Abolishes binding to RAN; when associated with K-50.|||Found in patients with Brugada syndrome; loss of function in enhancing the expression of SCN5A at the cell membrane; unknown pathological significance.|||Found in patients with cardiac arrhythmia and in patients with Brugada syndrome; loss of function in enhancing the expression of SCN5A at the cell membrane; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RAN|||Ran guanine nucleotide release factor|||Strongly decreased binding to RAN. Abolishes binding to RAN; when associated with K-53.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330636|||http://purl.uniprot.org/annotation/VAR_080079|||http://purl.uniprot.org/annotation/VAR_080080|||http://purl.uniprot.org/annotation/VSP_033057|||http://purl.uniprot.org/annotation/VSP_033058|||http://purl.uniprot.org/annotation/VSP_033059|||http://purl.uniprot.org/annotation/VSP_033060|||http://purl.uniprot.org/annotation/VSP_033061
http://togogenome.org/gene/9606:DHX35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5Z1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAH box|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Probable ATP-dependent RNA helicase DHX35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055168|||http://purl.uniprot.org/annotation/VAR_020211|||http://purl.uniprot.org/annotation/VAR_052184|||http://purl.uniprot.org/annotation/VSP_047178
http://togogenome.org/gene/9606:XPO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIA9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Exportin-7|||Importin N-terminal|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204713|||http://purl.uniprot.org/annotation/VAR_026526|||http://purl.uniprot.org/annotation/VAR_026527
http://togogenome.org/gene/9606:GCOM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H8Y6P7|||http://purl.uniprot.org/uniprot/P0CAP1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 4 and isoform 9.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9 and isoform 3.|||In isoform 9.|||Myocardial zonula adherens protein|||No effect on DYNLL1-binding.|||No effect on DYNLL1-binding; when associated with G-436.|||No effect on DYNLL1-binding; when associated with G-448.|||Polar residues|||Required for DYNLL1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000376013|||http://purl.uniprot.org/annotation/VAR_055453|||http://purl.uniprot.org/annotation/VSP_037389|||http://purl.uniprot.org/annotation/VSP_037390|||http://purl.uniprot.org/annotation/VSP_037391|||http://purl.uniprot.org/annotation/VSP_037392|||http://purl.uniprot.org/annotation/VSP_037393|||http://purl.uniprot.org/annotation/VSP_037394|||http://purl.uniprot.org/annotation/VSP_037395|||http://purl.uniprot.org/annotation/VSP_037396|||http://purl.uniprot.org/annotation/VSP_037397|||http://purl.uniprot.org/annotation/VSP_037398
http://togogenome.org/gene/9606:CNTNAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTA1|||http://purl.uniprot.org/uniprot/Q86YZ8|||http://purl.uniprot.org/uniprot/Q9C0A0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein-like 4|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||In isoform 2.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019510|||http://purl.uniprot.org/annotation/PRO_5001831894|||http://purl.uniprot.org/annotation/PRO_5004302649|||http://purl.uniprot.org/annotation/VAR_050268|||http://purl.uniprot.org/annotation/VAR_050269|||http://purl.uniprot.org/annotation/VAR_050270|||http://purl.uniprot.org/annotation/VAR_061371|||http://purl.uniprot.org/annotation/VAR_061372|||http://purl.uniprot.org/annotation/VSP_044464|||http://purl.uniprot.org/annotation/VSP_044465
http://togogenome.org/gene/9606:NEU3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ49                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BNR 1|||BNR 2|||BNR 3|||Decreases enzyme activity.|||Decreases the recruitment within caveola.|||Disordered|||FRIP motif|||In isoform 2.|||Loss of enzyme activity.|||Markedly decreases enzyme activity.|||Markedly decreases the recruitment within caveola.|||Nearly abolishes enzyme activity.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||Sialidase-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208903|||http://purl.uniprot.org/annotation/VAR_055839|||http://purl.uniprot.org/annotation/VSP_054145
http://togogenome.org/gene/9606:AOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06278                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||Aldehyde oxidase|||Decreases homodimerization but nearly no effect on kinetic parameters.|||Disrupts protein stability.|||FAD-binding PCMH-type|||Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate.|||Increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM.|||No effect on dimerization. Loss of oxidase activity.|||No effect on dimerization; no effect on oxidase activity.|||Phosphoserine|||Proton acceptor; for azaheterocycle hydroxylase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166104|||http://purl.uniprot.org/annotation/VAR_047517|||http://purl.uniprot.org/annotation/VAR_047518|||http://purl.uniprot.org/annotation/VAR_061136|||http://purl.uniprot.org/annotation/VAR_070256|||http://purl.uniprot.org/annotation/VAR_070257|||http://purl.uniprot.org/annotation/VAR_070258
http://togogenome.org/gene/9606:NHSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NHS-like protein 2|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341355|||http://purl.uniprot.org/annotation/VAR_044057|||http://purl.uniprot.org/annotation/VSP_060098|||http://purl.uniprot.org/annotation/VSP_060099
http://togogenome.org/gene/9606:RPS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25398                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylalanine|||N6-succinyllysine|||Removed|||Small ribosomal subunit protein eS12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122323
http://togogenome.org/gene/9606:HEXA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3W3|||http://purl.uniprot.org/uniprot/B4DVA7|||http://purl.uniprot.org/uniprot/H3BP20|||http://purl.uniprot.org/uniprot/P06865                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-hexosaminidase|||Beta-hexosaminidase eukaryotic type N-terminal|||Beta-hexosaminidase subunit alpha|||Critical for hydrolysis GM2 gangliosides|||Glycoside hydrolase family 20 catalytic|||In GM2G1.|||In GM2G1; infantile.|||In GM2G1; infantile; Moroccan Jewish.|||In GM2G1; infantile; inactive or unstable protein.|||In GM2G1; infantile; inactive protein.|||In GM2G1; infantile; loss of processing to a mature form; increased degradation.|||In GM2G1; juvenile.|||In GM2G1; juvenile; fails to associate with the beta-subunit to form the enzymatically active heterodimer.|||In GM2G1; late infantile.|||In GM2G1; late onset; inhibited subunit dissociation; loss of processing to a mature form; increased degradation.|||In GM2G1; mild; associated with spinal muscular atrophy.|||In GM2G1; subacute.|||In GM2G1; unknown pathological significance.|||In HEXA pseudodeficiency.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-157.|||No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-115 and Q-295.|||No change of the catalytic activity associated with the alpha-chain. No catalytic activity associated with the alpha-chain; when associated with Q-157 and Q-295.|||Proton donor|||beta-N-acetylhexosaminidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011993|||http://purl.uniprot.org/annotation/PRO_0000011994|||http://purl.uniprot.org/annotation/PRO_5002803588|||http://purl.uniprot.org/annotation/PRO_5003581447|||http://purl.uniprot.org/annotation/PRO_5006608223|||http://purl.uniprot.org/annotation/VAR_003202|||http://purl.uniprot.org/annotation/VAR_003203|||http://purl.uniprot.org/annotation/VAR_003204|||http://purl.uniprot.org/annotation/VAR_003205|||http://purl.uniprot.org/annotation/VAR_003206|||http://purl.uniprot.org/annotation/VAR_003207|||http://purl.uniprot.org/annotation/VAR_003208|||http://purl.uniprot.org/annotation/VAR_003209|||http://purl.uniprot.org/annotation/VAR_003210|||http://purl.uniprot.org/annotation/VAR_003211|||http://purl.uniprot.org/annotation/VAR_003212|||http://purl.uniprot.org/annotation/VAR_003213|||http://purl.uniprot.org/annotation/VAR_003214|||http://purl.uniprot.org/annotation/VAR_003215|||http://purl.uniprot.org/annotation/VAR_003216|||http://purl.uniprot.org/annotation/VAR_003217|||http://purl.uniprot.org/annotation/VAR_003218|||http://purl.uniprot.org/annotation/VAR_003219|||http://purl.uniprot.org/annotation/VAR_003220|||http://purl.uniprot.org/annotation/VAR_003221|||http://purl.uniprot.org/annotation/VAR_003222|||http://purl.uniprot.org/annotation/VAR_003223|||http://purl.uniprot.org/annotation/VAR_003224|||http://purl.uniprot.org/annotation/VAR_003225|||http://purl.uniprot.org/annotation/VAR_003226|||http://purl.uniprot.org/annotation/VAR_003227|||http://purl.uniprot.org/annotation/VAR_003228|||http://purl.uniprot.org/annotation/VAR_003229|||http://purl.uniprot.org/annotation/VAR_003230|||http://purl.uniprot.org/annotation/VAR_003231|||http://purl.uniprot.org/annotation/VAR_003232|||http://purl.uniprot.org/annotation/VAR_003233|||http://purl.uniprot.org/annotation/VAR_003234|||http://purl.uniprot.org/annotation/VAR_003235|||http://purl.uniprot.org/annotation/VAR_003236|||http://purl.uniprot.org/annotation/VAR_003237|||http://purl.uniprot.org/annotation/VAR_003238|||http://purl.uniprot.org/annotation/VAR_003239|||http://purl.uniprot.org/annotation/VAR_003240|||http://purl.uniprot.org/annotation/VAR_003241|||http://purl.uniprot.org/annotation/VAR_003242|||http://purl.uniprot.org/annotation/VAR_003243|||http://purl.uniprot.org/annotation/VAR_003244|||http://purl.uniprot.org/annotation/VAR_003245|||http://purl.uniprot.org/annotation/VAR_003246|||http://purl.uniprot.org/annotation/VAR_017188|||http://purl.uniprot.org/annotation/VAR_017189|||http://purl.uniprot.org/annotation/VAR_022439|||http://purl.uniprot.org/annotation/VAR_022440|||http://purl.uniprot.org/annotation/VAR_022441|||http://purl.uniprot.org/annotation/VAR_022442|||http://purl.uniprot.org/annotation/VAR_058477|||http://purl.uniprot.org/annotation/VAR_077497|||http://purl.uniprot.org/annotation/VAR_077498|||http://purl.uniprot.org/annotation/VAR_077499|||http://purl.uniprot.org/annotation/VAR_077500|||http://purl.uniprot.org/annotation/VAR_077501|||http://purl.uniprot.org/annotation/VAR_077502|||http://purl.uniprot.org/annotation/VSP_056657|||http://purl.uniprot.org/annotation/VSP_056658|||http://purl.uniprot.org/annotation/VSP_056659
http://togogenome.org/gene/9606:HCAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4Y1JWQ0|||http://purl.uniprot.org/uniprot/Q8TDS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hydroxycarboxylic acid receptor 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069603|||http://purl.uniprot.org/annotation/VAR_038713|||http://purl.uniprot.org/annotation/VAR_038714|||http://purl.uniprot.org/annotation/VAR_049400|||http://purl.uniprot.org/annotation/VAR_049401
http://togogenome.org/gene/9606:PPP1R26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T8A7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309218|||http://purl.uniprot.org/annotation/VAR_036906|||http://purl.uniprot.org/annotation/VAR_036907|||http://purl.uniprot.org/annotation/VAR_036908|||http://purl.uniprot.org/annotation/VAR_036909|||http://purl.uniprot.org/annotation/VAR_036910|||http://purl.uniprot.org/annotation/VAR_036911|||http://purl.uniprot.org/annotation/VAR_036912
http://togogenome.org/gene/9606:CCNE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G3DHS8|||http://purl.uniprot.org/uniprot/P24864|||http://purl.uniprot.org/uniprot/V5W5X2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin C-terminal|||Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-E1|||In isoform 3.|||In isoform E1S.|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Phosphothreonine; by GSK3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080449|||http://purl.uniprot.org/annotation/VSP_001253|||http://purl.uniprot.org/annotation/VSP_037381
http://togogenome.org/gene/9606:TENM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZMH4|||http://purl.uniprot.org/uniprot/Q9UKZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with SORBS1 (Ten-1 ICD form)|||Ten-1 intracellular domain|||Teneurin C-terminal-associated peptide|||Teneurin N-terminal|||Teneurin-1|||YD 1|||YD 10|||YD 11|||YD 12|||YD 13|||YD 14|||YD 15|||YD 16|||YD 17|||YD 18|||YD 19|||YD 2|||YD 20|||YD 21|||YD 22|||YD 23|||YD 3|||YD 4|||YD 5|||YD 6|||YD 7|||YD 8|||YD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259498|||http://purl.uniprot.org/annotation/PRO_0000421005|||http://purl.uniprot.org/annotation/PRO_0000421006|||http://purl.uniprot.org/annotation/VAR_036596|||http://purl.uniprot.org/annotation/VAR_036597|||http://purl.uniprot.org/annotation/VAR_036598|||http://purl.uniprot.org/annotation/VAR_036599|||http://purl.uniprot.org/annotation/VAR_036600|||http://purl.uniprot.org/annotation/VAR_053792|||http://purl.uniprot.org/annotation/VAR_053793|||http://purl.uniprot.org/annotation/VAR_053794|||http://purl.uniprot.org/annotation/VAR_053795|||http://purl.uniprot.org/annotation/VAR_076255|||http://purl.uniprot.org/annotation/VSP_043356
http://togogenome.org/gene/9606:DHRS4L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PKH6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 4-like 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312103|||http://purl.uniprot.org/annotation/VAR_037395|||http://purl.uniprot.org/annotation/VSP_029697
http://togogenome.org/gene/9606:BDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02338                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Transit Peptide                                                                                  ^@                                                                                  D-beta-hydroxybutyrate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031960
http://togogenome.org/gene/9606:LDLRAD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect interaction with ITCH; when associated with A-257. Loss of interaction with ITCH; when associated with A-257; A-276; A-277 and A-278.|||Does not affect interaction with ITCH; when associated with A-259. Loss of interaction with ITCH; when associated with A-259; A-276; A-277 and A-278.|||Does not affect interaction with ITCH; when associated with A-276 and A-277.Loss of interaction with ITCH; when associated with A-257; A-259; A-276 and A-277.|||Does not affect interaction with ITCH; when associated with A-276 and A-278.Loss of interaction with ITCH; when associated with A-257; A-259; A-276 and A-278.|||Does not affect interaction with ITCH; when associated with A-277 and A-278. Loss of interaction with ITCH; when associated with A-257; A-259; A-277 and A-278.|||Extracellular|||Helical|||In isoform 2.|||Involved in ITCH interaction|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||Loss of infection by Venezuelan equine encephalitis virus.|||Low-density lipoprotein receptor class A domain-containing protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299378|||http://purl.uniprot.org/annotation/VSP_056254
http://togogenome.org/gene/9606:OR2T34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGX1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150508|||http://purl.uniprot.org/annotation/VAR_067439
http://togogenome.org/gene/9606:MAST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60307                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||Basic residues|||Disordered|||Found in a patient with autism spectrum disorder without history of seizures; unknown pathological significance.|||In DEE108.|||In DEE108; unknown pathological significance.|||Microtubule-associated serine/threonine-protein kinase 3|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086314|||http://purl.uniprot.org/annotation/VAR_040786|||http://purl.uniprot.org/annotation/VAR_051646|||http://purl.uniprot.org/annotation/VAR_051647|||http://purl.uniprot.org/annotation/VAR_087834|||http://purl.uniprot.org/annotation/VAR_087835|||http://purl.uniprot.org/annotation/VAR_087836|||http://purl.uniprot.org/annotation/VAR_087837|||http://purl.uniprot.org/annotation/VAR_087838|||http://purl.uniprot.org/annotation/VAR_087839|||http://purl.uniprot.org/annotation/VAR_087840|||http://purl.uniprot.org/annotation/VAR_087841
http://togogenome.org/gene/9606:TRIM77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I1YAP6|||http://purl.uniprot.org/uniprot/I1YAP7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 77                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421830
http://togogenome.org/gene/9606:SMAD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84022                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Decreased activity.|||Decreased monoubiquitination.|||Diminishes cargo protein export.|||Disordered|||Does not abolish protein nuclear export. Abolishes almost completely acetylation.|||Forms heterotrimers.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced acetylation and 85% reduction in transcriptional activity. Completely abolishes acetylation and 97% reduction in transcriptional activity; when associated with R-333; R-341 and R-409.|||Greatly reduced interaction with DNA and JUN. Abolishes interaction with DNA and JUN; when associated with A-40; A-44 and A-43.|||In LDS3.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased constitutive activity.|||Increased transcriptional activity. Further increased transcriptional activity; when associated with S-208.|||Increased transcriptional activity. No further increase in transcriptional activity with EP300.|||Linker|||Little effect on interaction with DNA or JUN. Abolishes interaction with DNA and JUN; when associated with A-40; A-41 and A-44.|||Little effect on interaction with DNA or JUN. Abolishes interaction with DNA and JUN; when associated with A-41; A-43 and A-44.|||Little effect on interaction with DNA or JUN. Abolishes interaction with JUN; when associated with A-40; A-41 and A-43.|||MH1|||MH2|||Mothers against decapentaplegic homolog 3|||N-acetylserine|||N6-acetyllysine|||No effect on acetylation. Completely abolishes acetylation and 97% reduction in transcriptional activity; when associated with R-333; R-341 and R-378.|||No effect on acetylation. Completely abolishes acetylation and 97% reduction in transcriptional activity; when associated with R-333; R-378 and R-409.|||No effect on acetylation. Completely abolishes acetylation and 97% reduction in transcriptional activity; when associated with R-341; R-378 and R-409.|||Phosphoserine|||Phosphoserine; by CDK2 and CDK4|||Phosphoserine; by CK1|||Phosphoserine; by GSK3 and MAPK|||Phosphoserine; by MAPK|||Phosphoserine; by TGFBR1|||Phosphothreonine; by CDK2 and CDK4|||Phosphothreonine; by CDK2, CDK4 and MAPK|||Reduced interaction with JUN. Loss of transcriptional activity and cooperation with JUN.|||Reduced phosphorylation, increased transcriptional and antiproliferative activities. Further increase in transcriptional and antiproliferative activities; when associated with V-179 and A-213.|||Reduced phosphorylation, increased transcriptional and increased antiproliferative activities. Further increase in transcriptional and antiproliferative activities; when associated with V-8 and A-213.|||Reduced phosphorylation. Increased transcriptional and antiproliferative activities. Further increase in transcriptional and antiproliferative activities; when associated with V-8 and V-179.|||Removed|||Required for interaction with DNA and JUN and for functional cooperation with JUN|||Required for trimerization|||Slightly decreased monoubiquitination.|||Sufficient for interaction with XPO4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090856|||http://purl.uniprot.org/annotation/VAR_036474|||http://purl.uniprot.org/annotation/VAR_052021|||http://purl.uniprot.org/annotation/VAR_065578|||http://purl.uniprot.org/annotation/VAR_065579|||http://purl.uniprot.org/annotation/VAR_067047|||http://purl.uniprot.org/annotation/VAR_067048|||http://purl.uniprot.org/annotation/VAR_067051|||http://purl.uniprot.org/annotation/VSP_042900|||http://purl.uniprot.org/annotation/VSP_043793|||http://purl.uniprot.org/annotation/VSP_045348
http://togogenome.org/gene/9606:ETS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15036                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ETS|||PNT|||Phosphoserine|||Protein C-ets-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204077
http://togogenome.org/gene/9606:PLAAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HDD0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Cytoplasmic|||Helical|||In isoform 2.|||LRAT|||Lumenal|||Phospholipase A and acyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152481|||http://purl.uniprot.org/annotation/VSP_060190
http://togogenome.org/gene/9606:MEP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QKX5|||http://purl.uniprot.org/uniprot/Q16820                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes secretion.|||Cytoplasmic|||Decreased activity toward gastrin.|||EGF-like|||Extracellular|||Helical|||Interchain|||MAM|||MATH|||Mediates preference for acidic residues at subsite P1'|||Meprin A subunit|||Meprin A subunit beta|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Peptidase M12A|||Required for proteolytic processing                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028883|||http://purl.uniprot.org/annotation/PRO_0000028884|||http://purl.uniprot.org/annotation/PRO_5013983298|||http://purl.uniprot.org/annotation/VAR_057064|||http://purl.uniprot.org/annotation/VAR_057065|||http://purl.uniprot.org/annotation/VAR_069387
http://togogenome.org/gene/9606:ST8SIA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43173|||http://purl.uniprot.org/uniprot/Q59GW3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Pro residues|||Proton donor/acceptor|||Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149289|||http://purl.uniprot.org/annotation/VAR_020249
http://togogenome.org/gene/9606:SMYD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GMV2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Histone-lysine N-trimethyltransferase SMYD5|||MYND-type|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227788
http://togogenome.org/gene/9606:NADK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0N4                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NAD kinase 2, mitochondrial|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296292|||http://purl.uniprot.org/annotation/VSP_027192|||http://purl.uniprot.org/annotation/VSP_027193
http://togogenome.org/gene/9606:CHMP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R1T5|||http://purl.uniprot.org/uniprot/O43633                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes interaction with VTA1.|||Charged multivesicular body protein 2a|||Diminishes interaction with VPS4B.|||Diminishes interaction with VTA1.|||Interaction with VPS4B|||Interaction with VTA1|||MIT-interacting motif|||Membrane association; releases autoinhibition.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211462
http://togogenome.org/gene/9606:SGO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5BUA4|||http://purl.uniprot.org/uniprot/Q5FBB7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||D-box 1|||D-box 2|||D-box 3|||Disordered|||Disrupts interaction with CBX5, loss of localization to centromeres in interphase, no effect on localization to centromeres in mitosis; when associated with A-451 and A-453.|||Disrupts interaction with CBX5, loss of localization to centromeres in interphase, no effect on localization to centromeres in mitosis; when associated with A-451 and A-455.|||Disrupts interaction with CBX5, loss of localization to centromeres in interphase, no effect on localization to centromeres in mitosis; when associated with A-453 and A-455.|||In CAID; patient fibroblasts exhibit significantly faster cell proliferation than controls; during mitosis the mutant protein is localized in an ordered fashion around the centromeres but display a rather homogeneous cytoplasmic localization pattern.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 7.|||KEN box|||Loss of centromeric localization.|||Loss of interaction with PPP2CA and PPP2R1A and loss of centromeric localization.|||Loss of phosphorylation and presence of misaligned chromosomes; when associated with A-507.|||Loss of phosphorylation; and presence of misaligned chromosomes; when associated with A-14.|||Loss of proper localization to spindle pole and mitotic spindle. Significant increase in split spindle poles.|||Necessary for interaction with PPP2CA and PPP2R1A|||PXVXL/I motif|||Phosphoserine|||Phosphoserine; by NEK2|||Polar residues|||Shugoshin 1|||Shugoshin C-terminal|||Shugoshin N-terminal coiled-coil                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055436|||http://purl.uniprot.org/annotation/VAR_051968|||http://purl.uniprot.org/annotation/VAR_051969|||http://purl.uniprot.org/annotation/VAR_072709|||http://purl.uniprot.org/annotation/VSP_016790|||http://purl.uniprot.org/annotation/VSP_016791|||http://purl.uniprot.org/annotation/VSP_016792|||http://purl.uniprot.org/annotation/VSP_016793|||http://purl.uniprot.org/annotation/VSP_016794|||http://purl.uniprot.org/annotation/VSP_016795
http://togogenome.org/gene/9606:CANX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27824                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||2-4|||4 X approximate repeats|||Acidic residues|||Basic and acidic residues|||Calnexin|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with PPIB|||Lumenal|||N6-acetyllysine|||P domain (Extended arm)|||Phosphoserine|||Phosphoserine; by MAPK3|||Phosphothreonine|||S-palmitoyl cysteine|||Sufficient to mediate interaction with SGIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004198|||http://purl.uniprot.org/annotation/VSP_055515|||http://purl.uniprot.org/annotation/VSP_055516
http://togogenome.org/gene/9606:SYTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K973|||http://purl.uniprot.org/uniprot/B2R7R4|||http://purl.uniprot.org/uniprot/Q71SF7|||http://purl.uniprot.org/uniprot/Q96C24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||Phosphoserine|||RabBD|||Synaptotagmin-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190216|||http://purl.uniprot.org/annotation/VAR_016076|||http://purl.uniprot.org/annotation/VSP_015237|||http://purl.uniprot.org/annotation/VSP_015238
http://togogenome.org/gene/9606:GSG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY67|||http://purl.uniprot.org/uniprot/Q6UXU4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Germ cell-specific gene 1-like protein|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329464|||http://purl.uniprot.org/annotation/VSP_033004|||http://purl.uniprot.org/annotation/VSP_033516|||http://purl.uniprot.org/annotation/VSP_033517
http://togogenome.org/gene/9606:CLCNKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8H0|||http://purl.uniprot.org/uniprot/P51801                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CBS|||CBS 1|||CBS 2|||Chloride channel protein ClC-Kb|||Cytoplasmic|||Helical|||In BARTS3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094459|||http://purl.uniprot.org/annotation/VAR_001624|||http://purl.uniprot.org/annotation/VAR_001625|||http://purl.uniprot.org/annotation/VAR_001626|||http://purl.uniprot.org/annotation/VAR_001627|||http://purl.uniprot.org/annotation/VAR_001628|||http://purl.uniprot.org/annotation/VAR_014466|||http://purl.uniprot.org/annotation/VAR_014467|||http://purl.uniprot.org/annotation/VAR_014468|||http://purl.uniprot.org/annotation/VAR_014469|||http://purl.uniprot.org/annotation/VAR_024409|||http://purl.uniprot.org/annotation/VAR_033770|||http://purl.uniprot.org/annotation/VAR_033771|||http://purl.uniprot.org/annotation/VAR_033772|||http://purl.uniprot.org/annotation/VAR_033773|||http://purl.uniprot.org/annotation/VAR_046797|||http://purl.uniprot.org/annotation/VAR_046799|||http://purl.uniprot.org/annotation/VAR_046800|||http://purl.uniprot.org/annotation/VAR_046801|||http://purl.uniprot.org/annotation/VAR_069104|||http://purl.uniprot.org/annotation/VSP_045965|||http://purl.uniprot.org/annotation/VSP_045966|||http://purl.uniprot.org/annotation/VSP_045967
http://togogenome.org/gene/9606:ICA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05084                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AH|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Islet cell autoantigen 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084130|||http://purl.uniprot.org/annotation/VSP_047761|||http://purl.uniprot.org/annotation/VSP_055405
http://togogenome.org/gene/9606:DTNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3X3|||http://purl.uniprot.org/uniprot/Q9Y4J8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Dystrobrevin alpha|||In LVNC1; unknown pathological significance.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 14.|||In isoform 15.|||In isoform 17.|||In isoform 2, isoform 5, isoform 8, isoform 13, isoform 14, isoform 15 and isoform 16.|||In isoform 3, isoform 4, isoform 5, isoform 8, isoform 12 and isoform 16.|||In isoform 4, isoform 6, isoform 8, isoform 9, isoform 10, isoform 11, isoform 13, isoform 14, isoform 15, isoform 16 and isoform 17.|||In isoform 6, isoform 8, isoform 10 and isoform 11.|||In isoform 6.|||In isoform 7 and isoform 9.|||Interaction with MAGEE1|||Phosphoserine|||Syntrophin-binding region|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080036|||http://purl.uniprot.org/annotation/VAR_026744|||http://purl.uniprot.org/annotation/VAR_055320|||http://purl.uniprot.org/annotation/VSP_004206|||http://purl.uniprot.org/annotation/VSP_004207|||http://purl.uniprot.org/annotation/VSP_004208|||http://purl.uniprot.org/annotation/VSP_004209|||http://purl.uniprot.org/annotation/VSP_004210|||http://purl.uniprot.org/annotation/VSP_004211|||http://purl.uniprot.org/annotation/VSP_004212|||http://purl.uniprot.org/annotation/VSP_004213|||http://purl.uniprot.org/annotation/VSP_043824|||http://purl.uniprot.org/annotation/VSP_045444|||http://purl.uniprot.org/annotation/VSP_047532|||http://purl.uniprot.org/annotation/VSP_054816|||http://purl.uniprot.org/annotation/VSP_054817|||http://purl.uniprot.org/annotation/VSP_061450
http://togogenome.org/gene/9606:GEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RS7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'-3' exonuclease domain|||Abolishes endonuclease activity on both Hollyday junctions and 5' flap substrates.|||Abolishes endonuclease activity.|||Chromodomain|||Flap endonuclease GEN homolog 1|||Found in a renal cell carcinoma case; somatic mutation.|||In a breast cancer sample; somatic mutation.|||No effect on endonuclease activity on Hollyday junctions. Slightly reduces endonuclease activity on 5' flap substrates.|||No effect on endonuclease activity on both Hollyday junctions and 5' flap substrates.|||Phosphoserine|||Reduces by 25% endonuclease activity on Hollyday junctions and by 65% on 5' flap substrates.|||Reduces by 50% endonuclease activity on both Hollyday junctions and 5' flap substrates.|||Strongly reduces endonuclease activity on both Hollyday junctions and 5' flap substrates.|||XPG-I domain|||XPG-N domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314146|||http://purl.uniprot.org/annotation/VAR_037844|||http://purl.uniprot.org/annotation/VAR_037845|||http://purl.uniprot.org/annotation/VAR_037846|||http://purl.uniprot.org/annotation/VAR_037847|||http://purl.uniprot.org/annotation/VAR_037848|||http://purl.uniprot.org/annotation/VAR_037849|||http://purl.uniprot.org/annotation/VAR_037850|||http://purl.uniprot.org/annotation/VAR_064715
http://togogenome.org/gene/9606:SP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IRW4|||http://purl.uniprot.org/uniprot/Q02446|||http://purl.uniprot.org/uniprot/Q32M51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Phosphoserine|||Polar residues|||Transcription factor Sp4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047144|||http://purl.uniprot.org/annotation/VAR_047975
http://togogenome.org/gene/9606:IL17REL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVW7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Putative interleukin-17 receptor E-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325958|||http://purl.uniprot.org/annotation/VAR_039957|||http://purl.uniprot.org/annotation/VAR_061187
http://togogenome.org/gene/9606:IMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV31                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  S4 RNA-binding|||U3 small nucleolar ribonucleoprotein protein IMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132709
http://togogenome.org/gene/9606:HNMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50135                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Histamine N-methyltransferase|||In MRT51; loss of protein solubility; increased aggregation in the cytoplasm.|||In MRT51; no effect on protein abundance; no effect on protein localization to the cytoplasm; decreased thermal stability; decreased ligand affinity for S-adenosyl-L-methionine; loss of histamine N-methyltransferase activity.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084021|||http://purl.uniprot.org/annotation/VAR_010252|||http://purl.uniprot.org/annotation/VAR_076312|||http://purl.uniprot.org/annotation/VAR_076313|||http://purl.uniprot.org/annotation/VSP_042027|||http://purl.uniprot.org/annotation/VSP_043482|||http://purl.uniprot.org/annotation/VSP_043483
http://togogenome.org/gene/9606:KPNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00629                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||IBB|||Importin subunit alpha-3|||N-acetylalanine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120726
http://togogenome.org/gene/9606:FASTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8I0|||http://purl.uniprot.org/uniprot/A0A090N8Z7|||http://purl.uniprot.org/uniprot/Q14296                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes isoform 4 expression.|||Disordered|||Fas-activated serine/threonine kinase|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087196|||http://purl.uniprot.org/annotation/VAR_021970|||http://purl.uniprot.org/annotation/VAR_042200|||http://purl.uniprot.org/annotation/VSP_042746|||http://purl.uniprot.org/annotation/VSP_042747|||http://purl.uniprot.org/annotation/VSP_044811|||http://purl.uniprot.org/annotation/VSP_058246
http://togogenome.org/gene/9606:POTEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RU33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345419|||http://purl.uniprot.org/annotation/VAR_045825|||http://purl.uniprot.org/annotation/VAR_045826|||http://purl.uniprot.org/annotation/VAR_045827|||http://purl.uniprot.org/annotation/VAR_045828|||http://purl.uniprot.org/annotation/VAR_045829|||http://purl.uniprot.org/annotation/VAR_045830|||http://purl.uniprot.org/annotation/VAR_045831|||http://purl.uniprot.org/annotation/VAR_045832|||http://purl.uniprot.org/annotation/VAR_045833|||http://purl.uniprot.org/annotation/VAR_045834|||http://purl.uniprot.org/annotation/VAR_045835
http://togogenome.org/gene/9606:ZCCHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRD4|||http://purl.uniprot.org/uniprot/Q9C0B9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger CCHC domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150949|||http://purl.uniprot.org/annotation/VAR_060121|||http://purl.uniprot.org/annotation/VSP_055995
http://togogenome.org/gene/9606:SCGB2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13296|||http://purl.uniprot.org/uniprot/Q6NX70                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Mammaglobin-A|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036372|||http://purl.uniprot.org/annotation/PRO_5014310553|||http://purl.uniprot.org/annotation/VSP_009122
http://togogenome.org/gene/9606:ADGRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6U7|||http://purl.uniprot.org/uniprot/A0A0S2Z517|||http://purl.uniprot.org/uniprot/B3KQN7|||http://purl.uniprot.org/uniprot/B3KQV4|||http://purl.uniprot.org/uniprot/B4DM06|||http://purl.uniprot.org/uniprot/Q9Y653                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ADGRG1 C-terminal fragment|||ADGRG1 N-terminal fragment|||Abolishes cleavage but does not affect cell membrane localization or signaling activity.|||Abolishes cleavage.|||Abolishes heparin-binding; when associated with A-28 and A-33.|||Abolishes heparin-binding; when associated with A-29 and A-33.|||Adhesion G-protein coupled receptor G1|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In BFPP; abolishes autoproteolytic cleavage; reduces cell surface localization.|||In BFPP; abolishes interaction with COL3A1.|||In BFPP; abolishes interaction with COL3A1; reduces cell surface localization.|||In BFPP; reduces cell surface localization.|||In BFPP; unclear effects on cell surface localization; blocks downstream RhoA activation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Reduces heparin-binding. Abolishes heparin-binding; when associated with A-28 and A-29.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012880|||http://purl.uniprot.org/annotation/PRO_0000423086|||http://purl.uniprot.org/annotation/PRO_0000423087|||http://purl.uniprot.org/annotation/PRO_5002788638|||http://purl.uniprot.org/annotation/PRO_5002790061|||http://purl.uniprot.org/annotation/PRO_5014239287|||http://purl.uniprot.org/annotation/VAR_017910|||http://purl.uniprot.org/annotation/VAR_017911|||http://purl.uniprot.org/annotation/VAR_026242|||http://purl.uniprot.org/annotation/VAR_026243|||http://purl.uniprot.org/annotation/VAR_026244|||http://purl.uniprot.org/annotation/VAR_026245|||http://purl.uniprot.org/annotation/VAR_026246|||http://purl.uniprot.org/annotation/VAR_049457|||http://purl.uniprot.org/annotation/VAR_049458|||http://purl.uniprot.org/annotation/VAR_069581|||http://purl.uniprot.org/annotation/VAR_069582|||http://purl.uniprot.org/annotation/VAR_069583|||http://purl.uniprot.org/annotation/VAR_069584|||http://purl.uniprot.org/annotation/VSP_035068|||http://purl.uniprot.org/annotation/VSP_047554|||http://purl.uniprot.org/annotation/VSP_047555|||http://purl.uniprot.org/annotation/VSP_047556
http://togogenome.org/gene/9606:PAAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRP4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||Proteasomal ATPase-associated factor 1|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235685|||http://purl.uniprot.org/annotation/VAR_026415|||http://purl.uniprot.org/annotation/VAR_026416|||http://purl.uniprot.org/annotation/VAR_032082|||http://purl.uniprot.org/annotation/VSP_018477|||http://purl.uniprot.org/annotation/VSP_044699
http://togogenome.org/gene/9606:ZGLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C6A0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||GATA-type|||GATA-type zinc finger protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317557
http://togogenome.org/gene/9606:FBXL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box/LRR-repeat protein 7|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119849|||http://purl.uniprot.org/annotation/VSP_054751
http://togogenome.org/gene/9606:CEACAM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75871                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITAM|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||No internalization of bacteria; when associated with F-222.|||No internalization of bacteria; when associated with F-233.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316847|||http://purl.uniprot.org/annotation/VAR_038404|||http://purl.uniprot.org/annotation/VAR_038405
http://togogenome.org/gene/9606:TMEM88B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKF7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 88B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346446
http://togogenome.org/gene/9606:BBS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z626|||http://purl.uniprot.org/uniprot/Q8N3I7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 5 protein|||Found as heterozygous variant in patients with Bardet-Biedl syndrome; might have a modifying effect on disease phenotype.|||Found in patients with Bardet-Biedl syndrome carrying homozygous mutations in other BBS genes; might have a modifying effect on disease phenotype.|||In BBS5.|||In BBS5; found in patient of Sri Lankan origin; not detected in patients of Northern European origin.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223254|||http://purl.uniprot.org/annotation/VAR_025316|||http://purl.uniprot.org/annotation/VAR_025317|||http://purl.uniprot.org/annotation/VAR_066290|||http://purl.uniprot.org/annotation/VAR_066291|||http://purl.uniprot.org/annotation/VAR_072380|||http://purl.uniprot.org/annotation/VSP_017240
http://togogenome.org/gene/9606:PRR11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2SNZ4|||http://purl.uniprot.org/uniprot/Q96HE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  D-box|||Disordered|||KEN box|||Phosphodegron|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243943
http://togogenome.org/gene/9606:PRAMEF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT98                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290164
http://togogenome.org/gene/9606:TEX29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6K0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Testis-expressed protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263699
http://togogenome.org/gene/9606:MIF4GD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5K9|||http://purl.uniprot.org/uniprot/A0A0S2Z5S7|||http://purl.uniprot.org/uniprot/A0A0S2Z5T5|||http://purl.uniprot.org/uniprot/A9UHW6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||MIF4G|||MIF4G domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337089|||http://purl.uniprot.org/annotation/VSP_033877|||http://purl.uniprot.org/annotation/VSP_047408
http://togogenome.org/gene/9606:GOLGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14789                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Golgin subfamily B member 1|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190071|||http://purl.uniprot.org/annotation/VAR_020155|||http://purl.uniprot.org/annotation/VAR_020156|||http://purl.uniprot.org/annotation/VAR_031671|||http://purl.uniprot.org/annotation/VAR_031672|||http://purl.uniprot.org/annotation/VAR_031673|||http://purl.uniprot.org/annotation/VAR_036096|||http://purl.uniprot.org/annotation/VAR_036097|||http://purl.uniprot.org/annotation/VSP_045567|||http://purl.uniprot.org/annotation/VSP_045568|||http://purl.uniprot.org/annotation/VSP_057417|||http://purl.uniprot.org/annotation/VSP_057418
http://togogenome.org/gene/9606:SLC2A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD20                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 2, facilitated glucose transporter member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292014
http://togogenome.org/gene/9606:CSAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V02|||http://purl.uniprot.org/uniprot/Q96JQ3|||http://purl.uniprot.org/uniprot/Q9Y600                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine sulfinic acid decarboxylase|||Disordered|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147006|||http://purl.uniprot.org/annotation/VSP_001307|||http://purl.uniprot.org/annotation/VSP_039002
http://togogenome.org/gene/9606:NPY4R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50391                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 4|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069935|||http://purl.uniprot.org/annotation/VAR_030337|||http://purl.uniprot.org/annotation/VAR_030338
http://togogenome.org/gene/9606:LSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z590|||http://purl.uniprot.org/uniprot/O15116                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue                                                                                  ^@                                                                                  Phosphoserine|||Phosphothreonine|||Sm|||U6 snRNA-associated Sm-like protein LSm1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125554
http://togogenome.org/gene/9606:POP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95707                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Phosphoserine|||Ribonuclease P protein subunit p29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128418
http://togogenome.org/gene/9606:MRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22897                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin 1|||C-type lectin 2|||C-type lectin 3|||C-type lectin 4|||C-type lectin 5|||C-type lectin 6|||C-type lectin 7|||C-type lectin 8|||Cytoplasmic|||Extracellular|||Fibronectin type-II|||Helical|||In isoform 2.|||Macrophage mannose receptor 1|||N-linked (GlcNAc...) asparagine|||Probably protective against leprosy when associated with A-399 and F-407.|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017548|||http://purl.uniprot.org/annotation/VAR_019700|||http://purl.uniprot.org/annotation/VAR_065250|||http://purl.uniprot.org/annotation/VAR_065251|||http://purl.uniprot.org/annotation/VAR_065252|||http://purl.uniprot.org/annotation/VSP_041340|||http://purl.uniprot.org/annotation/VSP_041341
http://togogenome.org/gene/9606:TRAPPC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2L5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||Trafficking protein particle complex subunit 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065641|||http://purl.uniprot.org/annotation/VAR_036270|||http://purl.uniprot.org/annotation/VAR_057814|||http://purl.uniprot.org/annotation/VAR_057815|||http://purl.uniprot.org/annotation/VAR_057816|||http://purl.uniprot.org/annotation/VAR_060250|||http://purl.uniprot.org/annotation/VAR_060251|||http://purl.uniprot.org/annotation/VAR_060252|||http://purl.uniprot.org/annotation/VAR_060253|||http://purl.uniprot.org/annotation/VAR_060254|||http://purl.uniprot.org/annotation/VSP_004000|||http://purl.uniprot.org/annotation/VSP_014454
http://togogenome.org/gene/9606:EBF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNT0|||http://purl.uniprot.org/uniprot/B7Z934|||http://purl.uniprot.org/uniprot/Q9HAK2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C5-type|||Disordered|||IPT/TIG|||In isoform 2.|||Interaction with DNA|||Transcription factor COE DNA-binding|||Transcription factor COE2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107828|||http://purl.uniprot.org/annotation/VAR_048754|||http://purl.uniprot.org/annotation/VSP_055530|||http://purl.uniprot.org/annotation/VSP_055531
http://togogenome.org/gene/9606:TRPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBN4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Basic and acidic residues|||Binds to ITPR1, ITPR2 and ITPR3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform Beta and isoform Gamma.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Eta.|||In isoform Gamma.|||In isoform Zeta.|||Loss of interaction with NHERF1.|||Multimerization domain|||PDZ-binding domain|||Phosphotyrosine; by FYN|||Reduced EGF-induced phosphorylation and decreased association with NHERF1. Loss of EGF-induced phosphorylation and decreased association with NHERF1; when associated with F-959.|||Reduced EGF-induced phosphorylation and decreased association with NHERF1. Loss of EGF-induced phosphorylation and decreased association with NHERF1; when associated with F-972.|||Short transient receptor potential channel 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215314|||http://purl.uniprot.org/annotation/VAR_036452|||http://purl.uniprot.org/annotation/VSP_006567|||http://purl.uniprot.org/annotation/VSP_006568|||http://purl.uniprot.org/annotation/VSP_006569|||http://purl.uniprot.org/annotation/VSP_041262|||http://purl.uniprot.org/annotation/VSP_041439|||http://purl.uniprot.org/annotation/VSP_047747|||http://purl.uniprot.org/annotation/VSP_047748
http://togogenome.org/gene/9606:AMZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W34                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Archaemetzincin-2|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159617|||http://purl.uniprot.org/annotation/VAR_024850|||http://purl.uniprot.org/annotation/VAR_047343|||http://purl.uniprot.org/annotation/VSP_047263
http://togogenome.org/gene/9606:CCN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76076                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CCN family member 5|||IGFBP N-terminal|||In isoform 2.|||TSP type-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014409|||http://purl.uniprot.org/annotation/VAR_049566|||http://purl.uniprot.org/annotation/VSP_056298|||http://purl.uniprot.org/annotation/VSP_056299
http://togogenome.org/gene/9606:SPATA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV1|||http://purl.uniprot.org/uniprot/A8MU33|||http://purl.uniprot.org/uniprot/B4DX17|||http://purl.uniprot.org/uniprot/Q9NWH7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Spermatogenesis-associated protein 6|||Spermatogenesis-associated protein 6 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278441|||http://purl.uniprot.org/annotation/VAR_030774|||http://purl.uniprot.org/annotation/VAR_030775|||http://purl.uniprot.org/annotation/VAR_062174|||http://purl.uniprot.org/annotation/VAR_062175|||http://purl.uniprot.org/annotation/VSP_023277
http://togogenome.org/gene/9606:INTS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N201                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||In NDCAGF.|||In NDCAGF; decreased protein abundance.|||In NDCAGF; unknown pathological significance.|||Integrator complex subunit 1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236044|||http://purl.uniprot.org/annotation/VAR_049627|||http://purl.uniprot.org/annotation/VAR_083352|||http://purl.uniprot.org/annotation/VAR_083353|||http://purl.uniprot.org/annotation/VAR_083354|||http://purl.uniprot.org/annotation/VAR_083355|||http://purl.uniprot.org/annotation/VAR_083356|||http://purl.uniprot.org/annotation/VAR_083357
http://togogenome.org/gene/9606:SHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15464                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Loss of interaction with CD3Z. Alters LAT, PLCG1, VAV1 and LCP2 phosphorylation, MAP kinase signaling, Rac1 and JNK activation, intracellular calcium increase, activation of the nuclear factor for activation of T-cells and subsequent interleukin-2 expression which normally occur upon T-cells stimulation.|||Mediates interaction with LAT, PTK2/FAK1, JAK1 and JAK3|||Phosphoserine|||Polar residues|||SH2|||SH2 domain-containing adapter protein B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246324|||http://purl.uniprot.org/annotation/VSP_019846|||http://purl.uniprot.org/annotation/VSP_019847
http://togogenome.org/gene/9606:LRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07954|||http://purl.uniprot.org/uniprot/Q59FG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12; calcium-binding|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 20|||EGF-like 21|||EGF-like 22|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Extracellular|||Found in a patient with severe intellectual disability, seizures, stereotypic behavior, high pain threshold and sleep disturbances.|||Helical|||In KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with MAFB|||LDL-receptor class A 1|||LDL-receptor class A 10|||LDL-receptor class A 11|||LDL-receptor class A 12|||LDL-receptor class A 13|||LDL-receptor class A 14|||LDL-receptor class A 15|||LDL-receptor class A 16|||LDL-receptor class A 17|||LDL-receptor class A 18|||LDL-receptor class A 19|||LDL-receptor class A 2|||LDL-receptor class A 20|||LDL-receptor class A 21|||LDL-receptor class A 22|||LDL-receptor class A 23|||LDL-receptor class A 24|||LDL-receptor class A 25|||LDL-receptor class A 26|||LDL-receptor class A 27|||LDL-receptor class A 28|||LDL-receptor class A 29|||LDL-receptor class A 3|||LDL-receptor class A 30|||LDL-receptor class A 31|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class A 9|||LDL-receptor class B|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 18|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 21|||LDL-receptor class B 22|||LDL-receptor class B 23|||LDL-receptor class B 24|||LDL-receptor class B 25|||LDL-receptor class B 26|||LDL-receptor class B 27|||LDL-receptor class B 28|||LDL-receptor class B 29|||LDL-receptor class B 3|||LDL-receptor class B 30|||LDL-receptor class B 31|||LDL-receptor class B 32|||LDL-receptor class B 33|||LDL-receptor class B 34|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Loss of interaction with GULP1.|||Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1.|||Low-density lipoprotein receptor-related protein 1 515 kDa subunit|||Low-density lipoprotein receptor-related protein 1 85 kDa subunit|||Low-density lipoprotein receptor-related protein 1 intracellular domain|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||NPXY motif|||No detectable effect on phosphorylation.|||No effect on interaction with GULP1.|||No effect on tyrosine phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Prolow-density lipoprotein receptor-related protein 1|||Recognition site for proteolytical processing|||Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520.|||Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523.|||Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523.|||Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017317|||http://purl.uniprot.org/annotation/PRO_0000302750|||http://purl.uniprot.org/annotation/PRO_0000302751|||http://purl.uniprot.org/annotation/PRO_0000302752|||http://purl.uniprot.org/annotation/VAR_014725|||http://purl.uniprot.org/annotation/VAR_021885|||http://purl.uniprot.org/annotation/VAR_029181|||http://purl.uniprot.org/annotation/VAR_035994|||http://purl.uniprot.org/annotation/VAR_035995|||http://purl.uniprot.org/annotation/VAR_047525|||http://purl.uniprot.org/annotation/VAR_047526|||http://purl.uniprot.org/annotation/VAR_047527|||http://purl.uniprot.org/annotation/VAR_069388|||http://purl.uniprot.org/annotation/VAR_077982|||http://purl.uniprot.org/annotation/VSP_056919|||http://purl.uniprot.org/annotation/VSP_056920
http://togogenome.org/gene/9606:PRAMEF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWM4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156982
http://togogenome.org/gene/9606:IER5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T953                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Immediate early response gene 5-like protein|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334656|||http://purl.uniprot.org/annotation/VAR_043450|||http://purl.uniprot.org/annotation/VSP_033726|||http://purl.uniprot.org/annotation/VSP_033727
http://togogenome.org/gene/9606:LRRC37A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 37A|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337079
http://togogenome.org/gene/9606:SPATA31C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Polar residues|||Pro residues|||Putative spermatogenesis-associated protein 31C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420908|||http://purl.uniprot.org/annotation/VSP_044951|||http://purl.uniprot.org/annotation/VSP_044952
http://togogenome.org/gene/9606:RGS18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS28                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Phosphoserine|||RGS|||Regulator of G-protein signaling 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204227
http://togogenome.org/gene/9606:PRORP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15091                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes ribonuclease activity.|||Does not affect ribonuclease activity.|||In COXPD54; decreased protein levels in homozygous patient cells; impaired mitochondrial RNA processing in homozygous patient cells.|||In COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro.|||In COXPD54; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial ribonuclease P catalytic subunit|||Mitochondrion|||PRORP|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050749|||http://purl.uniprot.org/annotation/VAR_054212|||http://purl.uniprot.org/annotation/VAR_086903|||http://purl.uniprot.org/annotation/VAR_086904|||http://purl.uniprot.org/annotation/VAR_086905|||http://purl.uniprot.org/annotation/VAR_086906|||http://purl.uniprot.org/annotation/VAR_086907|||http://purl.uniprot.org/annotation/VSP_036201|||http://purl.uniprot.org/annotation/VSP_036202|||http://purl.uniprot.org/annotation/VSP_036203
http://togogenome.org/gene/9606:AMN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY45                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein AMN1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289273|||http://purl.uniprot.org/annotation/VSP_054567
http://togogenome.org/gene/9606:HTR1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28221                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 1D|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068927|||http://purl.uniprot.org/annotation/VAR_011834
http://togogenome.org/gene/9606:ZNF503                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Zinc finger protein 503                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292204|||http://purl.uniprot.org/annotation/VAR_032951|||http://purl.uniprot.org/annotation/VSP_026394|||http://purl.uniprot.org/annotation/VSP_026395
http://togogenome.org/gene/9606:ZBTB18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99592                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with DNMT3A|||Phosphoserine|||Zinc finger and BTB domain-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047477|||http://purl.uniprot.org/annotation/VAR_012768|||http://purl.uniprot.org/annotation/VAR_079032|||http://purl.uniprot.org/annotation/VSP_035381
http://togogenome.org/gene/9606:GPD1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N335                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycerol-3-phosphate dehydrogenase 1-like protein|||In BRGDA2; unknown pathological significance; decreased enzymatic activity and significant reduction of sodium current when coexpressed with SCN5A in HEK cells.|||In BRGDA2; unknown pathological significance; decreased enzymatic activity; affects SCN5A membrane expression; reduction of sodium current when coexpressed with SCN5A in HEK cells.|||In BRGDA2; unknown pathological significance; significant reduction of sodium current when coexpressed with SCN5A in HEK cells.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286511|||http://purl.uniprot.org/annotation/VAR_032114|||http://purl.uniprot.org/annotation/VAR_044044|||http://purl.uniprot.org/annotation/VAR_044045|||http://purl.uniprot.org/annotation/VAR_044046|||http://purl.uniprot.org/annotation/VAR_044047
http://togogenome.org/gene/9606:FAM83C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM83C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079459|||http://purl.uniprot.org/annotation/VAR_021946|||http://purl.uniprot.org/annotation/VAR_053900|||http://purl.uniprot.org/annotation/VAR_053901|||http://purl.uniprot.org/annotation/VAR_053902
http://togogenome.org/gene/9606:ZNF835                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2P0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Polar residues|||Zinc finger protein 835                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319111|||http://purl.uniprot.org/annotation/VAR_061977|||http://purl.uniprot.org/annotation/VAR_061978
http://togogenome.org/gene/9606:PITX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75364                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In CTRCT11.|||Nuclear localization signal|||OAR|||Phosphoserine|||Pituitary homeobox 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049229|||http://purl.uniprot.org/annotation/VAR_003767
http://togogenome.org/gene/9606:CITED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99966                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cbp/p300-interacting transactivator 1|||Disordered|||Does not change subcellular localization; when associated with A-176.|||Does not change subcellular localization; when associated with A-178.|||Does not change subcellular localization; when associated with A-91.|||Does not change subcellular localization; when associated with A-95.|||Does not inhibit interaction with ESR1 and ER-coactivation activity.|||Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-165.|||Does not inhibit interaction with ESR1 and ER-coactivation activity. Localizes mainly in the nucleus; when associated with A-167.|||In isoform 2.|||Inhibits interaction with ESR1 and ER-coactivation activity.|||Nuclear export signal|||Polar residues|||Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-67 and A-137.|||Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-63; A-71 and A-137.|||Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-16; A-67; A-71 and A-137.|||Strongly reduces phosphorylation but does not interfere with its NES-dependent nuclear export; when associated with A-63; A-67; A-71 and A-137.|||Strongly reduces phosphorylation; when associated with A-16; A-63; A-67 and A-71.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144724|||http://purl.uniprot.org/annotation/VAR_053038|||http://purl.uniprot.org/annotation/VSP_039897
http://togogenome.org/gene/9606:RIOK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRS2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Abolishes autophosphorylation activity; enhances association with pre-40S ribosomal subunits; inhibits processing of 18S-E pre-rRNA to the mature 18S rRNA.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase RIO1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213526|||http://purl.uniprot.org/annotation/VAR_061777
http://togogenome.org/gene/9606:ONECUT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60422                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  CUT|||Disordered|||Homeobox|||One cut domain family member 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271218
http://togogenome.org/gene/9606:N4BP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15049                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||NEDD4-binding protein 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096682
http://togogenome.org/gene/9606:SAMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6SPF0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with L3MBTL3.|||Acidic residues|||Decreases binding to unmethylated CpG islands.|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||SAM|||SAMD1-like winged helix (WH)|||Slightly decreases binding to unmethylated CpG islands.|||Sterile alpha motif domain-containing protein 1|||Strongly decreases binding to unmethylated CpG islands. Abolishes interaction with KDM1A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279494|||http://purl.uniprot.org/annotation/VAR_061701
http://togogenome.org/gene/9606:CSPG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UVK1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CSPG 1|||CSPG 10|||CSPG 11|||CSPG 12|||CSPG 13|||CSPG 14|||CSPG 15|||CSPG 2|||CSPG 3|||CSPG 4|||CSPG 5|||CSPG 6|||CSPG 7|||CSPG 8|||CSPG 9|||Chondroitin sulfate proteoglycan 4|||Cysteine-containing|||Cytoplasmic|||Disordered|||Extracellular|||Globular or compact configuration stabilized by disulfide bonds|||Helical|||Interaction with COL5A1|||Interaction with COL6A2|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Neurite growth inhibition|||O-linked (Xyl...) (chondroitin sulfate) serine|||PDZ-binding|||Phosphothreonine; by PKC/PRKCA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041962|||http://purl.uniprot.org/annotation/VAR_061733
http://togogenome.org/gene/9606:UBE2L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68036                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decrease in autoubiquitination.|||Does not convert into a lysine reactive E2; when associated with D-119.|||Does not convert into a lysine reactive E2; when associated with D-88.|||Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||Loss of catalytic activity. Prevents ubiquitin-dependent proteasomal degradation of UBE2L3.|||Marked decrease in autoubiquitination.|||N6-acetyllysine|||UBC core|||Ubiquitin-conjugating enzyme E2 L3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082476|||http://purl.uniprot.org/annotation/VSP_045152|||http://purl.uniprot.org/annotation/VSP_047342
http://togogenome.org/gene/9606:ARGFX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Arginine-fifty homeobox|||Disordered|||Homeobox|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311325|||http://purl.uniprot.org/annotation/VAR_037226
http://togogenome.org/gene/9606:NELFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WX92                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||Negative elongation factor B|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219129|||http://purl.uniprot.org/annotation/VSP_059998
http://togogenome.org/gene/9606:MYO3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM71|||http://purl.uniprot.org/uniprot/Q8WXR4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Myosin motor|||Myosin-IIIb|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086415|||http://purl.uniprot.org/annotation/VAR_030605|||http://purl.uniprot.org/annotation/VAR_030606|||http://purl.uniprot.org/annotation/VAR_030607|||http://purl.uniprot.org/annotation/VAR_030608|||http://purl.uniprot.org/annotation/VAR_030609|||http://purl.uniprot.org/annotation/VAR_030610|||http://purl.uniprot.org/annotation/VAR_040886|||http://purl.uniprot.org/annotation/VAR_040887|||http://purl.uniprot.org/annotation/VAR_040888|||http://purl.uniprot.org/annotation/VAR_040889|||http://purl.uniprot.org/annotation/VAR_040890|||http://purl.uniprot.org/annotation/VAR_040891|||http://purl.uniprot.org/annotation/VAR_040892|||http://purl.uniprot.org/annotation/VAR_040893|||http://purl.uniprot.org/annotation/VAR_040894|||http://purl.uniprot.org/annotation/VAR_040895|||http://purl.uniprot.org/annotation/VAR_040896|||http://purl.uniprot.org/annotation/VAR_040897|||http://purl.uniprot.org/annotation/VAR_040898|||http://purl.uniprot.org/annotation/VAR_040899|||http://purl.uniprot.org/annotation/VSP_010162|||http://purl.uniprot.org/annotation/VSP_010163|||http://purl.uniprot.org/annotation/VSP_010164|||http://purl.uniprot.org/annotation/VSP_010165|||http://purl.uniprot.org/annotation/VSP_023111
http://togogenome.org/gene/9606:UHRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase UHRF2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with PCNP|||Interchain|||Methyl-CpG binding and interaction with HDAC1|||No effect on autosumoylation, nor on ZNF131 sumoylation.|||No effect on autosumoylation.|||PHD-type|||Phosphoserine|||Polar residues|||RING-type|||Required for interaction with histone H3|||Ubiquitin-like|||YDG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056147|||http://purl.uniprot.org/annotation/VAR_035961|||http://purl.uniprot.org/annotation/VSP_013874|||http://purl.uniprot.org/annotation/VSP_013875
http://togogenome.org/gene/9606:NECTIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQS3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nectin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226372|||http://purl.uniprot.org/annotation/VAR_049995|||http://purl.uniprot.org/annotation/VSP_017435|||http://purl.uniprot.org/annotation/VSP_017436|||http://purl.uniprot.org/annotation/VSP_046893|||http://purl.uniprot.org/annotation/VSP_046894
http://togogenome.org/gene/9606:TRIM23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36406                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARF-like|||B box-type; degenerate|||E3 ubiquitin-protein ligase TRIM23|||In isoform Beta.|||In isoform Gamma.|||Loss of E3 ubiquitin-protein ligase activity.|||Maintains GTPase activity. Increases interaction with PSCD1.|||RING-type; degenerate|||Suppresses GTPase activity. Decreases interaction with PSCD1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207483|||http://purl.uniprot.org/annotation/VAR_048320|||http://purl.uniprot.org/annotation/VSP_000296|||http://purl.uniprot.org/annotation/VSP_000297
http://togogenome.org/gene/9606:SERPINA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2Z4LCH4|||http://purl.uniprot.org/uniprot/P08185                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Conserved cysteine within steroid binding domain|||Corticosteroid-binding globulin|||In CBG deficiency; Leuven; decreased cortisol-binding affinity.|||In CBG deficiency; Lyon; decreased cortisol-binding affinity.|||N-linked (GlcNAc...) asparagine|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032429|||http://purl.uniprot.org/annotation/PRO_5016343569|||http://purl.uniprot.org/annotation/VAR_007111|||http://purl.uniprot.org/annotation/VAR_016223|||http://purl.uniprot.org/annotation/VAR_024350
http://togogenome.org/gene/9606:SEMA6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3T3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Pro residues|||Sema|||Semaphorin-6B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032341|||http://purl.uniprot.org/annotation/VSP_047625|||http://purl.uniprot.org/annotation/VSP_047626
http://togogenome.org/gene/9606:RRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31350                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the interaction with CCNF. Lack of proteasomal degradation. Increase in the cellular concentration of dATP and dGTP, but not dCTP and dTTP, leading to an imbalance in dNTP pools and genome instability.|||Cy|||Enhances inhibitory effect on Wnt signaling.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Prevents inhibitory effect on Wnt signaling.|||Ribonucleoside-diphosphate reductase subunit M2|||Strongly reduces the interaction with CCNF. Lack of proteasomal degradation. Increase in the cellular concentration of dATP and dGTP, but not dCTP and dTTP, leading to an imbalance in dNTP pools and genome instability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190447|||http://purl.uniprot.org/annotation/VSP_044917
http://togogenome.org/gene/9606:BAMBI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13145                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BMP and activin membrane-bound inhibitor homolog|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020779
http://togogenome.org/gene/9606:MAGEA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9W4|||http://purl.uniprot.org/uniprot/P43361                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156707|||http://purl.uniprot.org/annotation/VAR_053494|||http://purl.uniprot.org/annotation/VAR_053495
http://togogenome.org/gene/9606:ADAMTSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82987                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ADAMTS-like protein 3|||Disordered|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Polar residues|||TSP type-1 1|||TSP type-1 10|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249684|||http://purl.uniprot.org/annotation/VAR_027478|||http://purl.uniprot.org/annotation/VAR_027479|||http://purl.uniprot.org/annotation/VAR_027480|||http://purl.uniprot.org/annotation/VAR_027481|||http://purl.uniprot.org/annotation/VAR_027482|||http://purl.uniprot.org/annotation/VAR_027483|||http://purl.uniprot.org/annotation/VAR_027484|||http://purl.uniprot.org/annotation/VAR_027485|||http://purl.uniprot.org/annotation/VAR_027486|||http://purl.uniprot.org/annotation/VAR_035809|||http://purl.uniprot.org/annotation/VAR_035810|||http://purl.uniprot.org/annotation/VAR_035811|||http://purl.uniprot.org/annotation/VAR_035812|||http://purl.uniprot.org/annotation/VAR_057365|||http://purl.uniprot.org/annotation/VSP_037810
http://togogenome.org/gene/9606:WDR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4E6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051353|||http://purl.uniprot.org/annotation/VSP_015274
http://togogenome.org/gene/9606:C19orf67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||UPF0575 protein C19orf67                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332937
http://togogenome.org/gene/9606:SNRNP70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08621|||http://purl.uniprot.org/uniprot/Q9UFS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||RRM|||Removed|||Required for interaction with U1 RNA|||U1 small nuclear ribonucleoprotein 70 kDa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081880|||http://purl.uniprot.org/annotation/VSP_005847|||http://purl.uniprot.org/annotation/VSP_005848|||http://purl.uniprot.org/annotation/VSP_005849|||http://purl.uniprot.org/annotation/VSP_005850
http://togogenome.org/gene/9606:MFSD4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N468|||http://purl.uniprot.org/uniprot/Q96KX6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Major facilitator superfamily domain-containing protein 4A|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273395|||http://purl.uniprot.org/annotation/VAR_030142|||http://purl.uniprot.org/annotation/VAR_030143|||http://purl.uniprot.org/annotation/VSP_057053
http://togogenome.org/gene/9606:ANKRD35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFX6|||http://purl.uniprot.org/uniprot/F6XZD3|||http://purl.uniprot.org/uniprot/Q8N283                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat domain-containing protein 35|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243910|||http://purl.uniprot.org/annotation/VAR_026870|||http://purl.uniprot.org/annotation/VAR_033506|||http://purl.uniprot.org/annotation/VAR_048278|||http://purl.uniprot.org/annotation/VAR_061017|||http://purl.uniprot.org/annotation/VAR_087983|||http://purl.uniprot.org/annotation/VSP_056916|||http://purl.uniprot.org/annotation/VSP_056917
http://togogenome.org/gene/9606:SNX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60493                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes binding to phosphatidylinositol 3-phosphate.|||Abolishes interaction with retromer cargo-selective subcomplex VPS26A:VPS29:VPS35; when associated with A-28 and A-30.|||Abolishes interaction with retromer cargo-selective subcomplex VPS26A:VPS29:VPS35; when associated with A-28 and A-32.|||Abolishes interaction with retromer cargo-selective subcomplex VPS26A:VPS29:VPS35; when associated with A-30 and A-32.|||Binds predominantly to PtdIns(P5) and weaker to PtdIns(P3) abd PtdIns(P4); involved in neurite outgrowth regulation|||Decreases VPS35 binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increases VPS35 binding.|||Loss of VPS35 binding.|||N-acetylalanine|||Omega-N-methylarginine|||PX|||Phosphoserine|||Removed|||Sorting nexin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213840|||http://purl.uniprot.org/annotation/VSP_006190|||http://purl.uniprot.org/annotation/VSP_012928|||http://purl.uniprot.org/annotation/VSP_014694
http://togogenome.org/gene/9606:PRDM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWZ6|||http://purl.uniprot.org/uniprot/Q9NQV5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a patient with diffuse large B-cell lymphoma; unknown pathological significance.|||In isoform 2.|||PR domain-containing protein 11|||Phosphoserine|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047768|||http://purl.uniprot.org/annotation/VAR_073689|||http://purl.uniprot.org/annotation/VAR_073690|||http://purl.uniprot.org/annotation/VSP_039836
http://togogenome.org/gene/9606:VPS13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7G8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chorein N-terminal|||Disordered|||Found in a patient with intellectual disability and facial dysmorphisms.|||In COH1.|||In COH1; accelerates differentiation of adipose cells; response to insulin is abnormal..|||In COH1; disrupts protein localization to the perinuclear region; Golgi stacks are fragmented, early endosomes are abnormal, lysosomes are enlarged and glycosylation is defective; leads to an accumulation of liquid droplets and accelerates differentiation of adipose cells; response to insulin is abnormal..|||In COH1; early endosomes are abnormal, lysosomes are enlarged and glycosylation is defective.|||In COH1; glycosylation is defective; accelerates differentiation of adipose cells.|||In COH1; leads to an accumulation of liquid droplets and accelerates differentiation of adipose cells; response to insulin is abnormal..|||In COH1; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Intermembrane lipid transfer protein VPS13B|||Localizes the protein to the Golgi apparatus|||Phosphoserine|||Polar residues|||SHR-BD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065880|||http://purl.uniprot.org/annotation/VAR_017759|||http://purl.uniprot.org/annotation/VAR_036325|||http://purl.uniprot.org/annotation/VAR_038422|||http://purl.uniprot.org/annotation/VAR_038423|||http://purl.uniprot.org/annotation/VAR_038424|||http://purl.uniprot.org/annotation/VAR_057750|||http://purl.uniprot.org/annotation/VAR_057751|||http://purl.uniprot.org/annotation/VAR_057752|||http://purl.uniprot.org/annotation/VAR_058749|||http://purl.uniprot.org/annotation/VAR_058750|||http://purl.uniprot.org/annotation/VAR_058751|||http://purl.uniprot.org/annotation/VAR_058752|||http://purl.uniprot.org/annotation/VAR_058753|||http://purl.uniprot.org/annotation/VAR_058754|||http://purl.uniprot.org/annotation/VAR_058755|||http://purl.uniprot.org/annotation/VAR_058756|||http://purl.uniprot.org/annotation/VAR_058757|||http://purl.uniprot.org/annotation/VAR_069429|||http://purl.uniprot.org/annotation/VAR_082932|||http://purl.uniprot.org/annotation/VAR_086594|||http://purl.uniprot.org/annotation/VAR_086595|||http://purl.uniprot.org/annotation/VAR_086596|||http://purl.uniprot.org/annotation/VAR_086597|||http://purl.uniprot.org/annotation/VAR_086598|||http://purl.uniprot.org/annotation/VAR_086599|||http://purl.uniprot.org/annotation/VAR_086600|||http://purl.uniprot.org/annotation/VAR_086601|||http://purl.uniprot.org/annotation/VAR_086602|||http://purl.uniprot.org/annotation/VAR_086603|||http://purl.uniprot.org/annotation/VAR_086604|||http://purl.uniprot.org/annotation/VAR_086605|||http://purl.uniprot.org/annotation/VAR_086606|||http://purl.uniprot.org/annotation/VAR_086607|||http://purl.uniprot.org/annotation/VAR_086608|||http://purl.uniprot.org/annotation/VAR_086609|||http://purl.uniprot.org/annotation/VAR_086610|||http://purl.uniprot.org/annotation/VAR_086611|||http://purl.uniprot.org/annotation/VAR_086612|||http://purl.uniprot.org/annotation/VSP_009404|||http://purl.uniprot.org/annotation/VSP_009405|||http://purl.uniprot.org/annotation/VSP_009406|||http://purl.uniprot.org/annotation/VSP_009407|||http://purl.uniprot.org/annotation/VSP_009408|||http://purl.uniprot.org/annotation/VSP_009409|||http://purl.uniprot.org/annotation/VSP_009410|||http://purl.uniprot.org/annotation/VSP_039837
http://togogenome.org/gene/9606:RAPGEF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RTU6|||http://purl.uniprot.org/uniprot/Q8TEU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 6.|||N-acetylmethionine|||N-terminal Ras-GEF|||PDZ|||Phosphoserine|||Polar residues|||Rap guanine nucleotide exchange factor 6|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068876|||http://purl.uniprot.org/annotation/VAR_057168|||http://purl.uniprot.org/annotation/VAR_057169|||http://purl.uniprot.org/annotation/VAR_057170|||http://purl.uniprot.org/annotation/VAR_057171|||http://purl.uniprot.org/annotation/VAR_059793|||http://purl.uniprot.org/annotation/VSP_045027|||http://purl.uniprot.org/annotation/VSP_050607|||http://purl.uniprot.org/annotation/VSP_050608|||http://purl.uniprot.org/annotation/VSP_050609|||http://purl.uniprot.org/annotation/VSP_050610|||http://purl.uniprot.org/annotation/VSP_050611
http://togogenome.org/gene/9606:CDH19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H159                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-19|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003817|||http://purl.uniprot.org/annotation/PRO_0000003818|||http://purl.uniprot.org/annotation/VSP_047020|||http://purl.uniprot.org/annotation/VSP_047021
http://togogenome.org/gene/9606:TBX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99593                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes acetylation of the protein, leading to impaired transcription factor activity. Impaired subcellular location.|||Basic and acidic residues|||Disordered|||Does not affect acetylation of the protein.|||Does not affect transcription factor activity.|||In HOS.|||In HOS; extensive upper limb malformations; affects transcriptional regulation of MYH6.|||In HOS; extensive upper limb malformations; strongly reduced affinity for DNA.|||In HOS; significant cardiac malformations but only minor skeletal abnormalities; reduced protein stability and strongly reduced affinity for DNA.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Polar residues|||Probable disease-associated variant found in a patient with atrial fibrillation; reduces transcriptional activity; affects transcriptional regulation of NKX2-5 or GATA4.|||Probable disease-associated variant found in a patient with atrial fibrillation; reduces transcriptional activity; affects transcriptional regulation of NKX2-5.|||Probable disease-associated variant found in a patient with sporadic dilated cardiomyopathy; associated with disease susceptibility; associated with significantly decreased transcriptional activity.|||Probable disease-associated variant found in patients with familial dilated cardiomyopathy; associated with disease susceptibility; associated with significantly decreased transcriptional activity.|||T-box|||T-box transcription factor TBX5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184435|||http://purl.uniprot.org/annotation/VAR_007456|||http://purl.uniprot.org/annotation/VAR_009701|||http://purl.uniprot.org/annotation/VAR_009702|||http://purl.uniprot.org/annotation/VAR_015381|||http://purl.uniprot.org/annotation/VAR_015382|||http://purl.uniprot.org/annotation/VAR_074599|||http://purl.uniprot.org/annotation/VAR_074600|||http://purl.uniprot.org/annotation/VAR_076642|||http://purl.uniprot.org/annotation/VAR_076673|||http://purl.uniprot.org/annotation/VSP_006387|||http://purl.uniprot.org/annotation/VSP_006388|||http://purl.uniprot.org/annotation/VSP_046845
http://togogenome.org/gene/9606:REEP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L5BXV2|||http://purl.uniprot.org/uniprot/Q96HR9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In RP77.|||In RP77; decreased protein levels; does not affect localization to endoplasmic reticulum.|||In RP77; decreased protein levels; does not affect localization to endoplasmic reticulum; loss of rod photoreceptor function shown by a mouse knockin model of the mutation.|||In RP77; unknown pathological significance.|||In isoform 2.|||Receptor expression-enhancing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101818|||http://purl.uniprot.org/annotation/VAR_048927|||http://purl.uniprot.org/annotation/VAR_077931|||http://purl.uniprot.org/annotation/VAR_077932|||http://purl.uniprot.org/annotation/VAR_081396|||http://purl.uniprot.org/annotation/VAR_081397|||http://purl.uniprot.org/annotation/VSP_058885
http://togogenome.org/gene/9606:ZNF423                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNG7|||http://purl.uniprot.org/uniprot/B7Z9C7|||http://purl.uniprot.org/uniprot/F5H7S1|||http://purl.uniprot.org/uniprot/Q2M1K9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-574.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-497; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-491; A-528; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-458; A-497; A-528; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-452; A-491; A-497; A-528; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-426; A-458; A-491; A-497; A-528; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-420; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581.|||Abolishes the ability to bind promoter of BMP target genes; when associated with A-426; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581.|||Basic and acidic residues|||C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; atypical|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21; degenerate|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25; degenerate|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||In JBTS19.|||In NPHP14; found at homozygosity in two siblings with nephronophthisis, cerebellar vermis hypoplasia and situs inversus.|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein 423                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308595|||http://purl.uniprot.org/annotation/VAR_036844|||http://purl.uniprot.org/annotation/VAR_068501|||http://purl.uniprot.org/annotation/VAR_068502|||http://purl.uniprot.org/annotation/VSP_057595
http://togogenome.org/gene/9606:GMNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75496                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Geminin|||Homeodomain binding|||In MGORS6.|||N6-acetyllysine|||Necessary and sufficient for interaction with IDAS and CDT1|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148729|||http://purl.uniprot.org/annotation/VAR_024233|||http://purl.uniprot.org/annotation/VAR_033959|||http://purl.uniprot.org/annotation/VAR_033960|||http://purl.uniprot.org/annotation/VAR_033961|||http://purl.uniprot.org/annotation/VAR_053107|||http://purl.uniprot.org/annotation/VAR_053108|||http://purl.uniprot.org/annotation/VAR_076172
http://togogenome.org/gene/9606:CPSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage and polyadenylation specificity factor subunit 2|||Disordered|||Does not inhibit histone 3'-end processing.|||Inhibits histone 3'-end processing.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074393
http://togogenome.org/gene/9606:NUP88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP20|||http://purl.uniprot.org/uniprot/J3KMX1|||http://purl.uniprot.org/uniprot/Q99567                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In FADS4; decreased localization to the nuclear pore complex; decreased interaction with NUP214 and NUP62.|||In FADS4; no effect on localization to the nuclear pore complex; no effect on interaction with NUP214 and NUP62.|||N-acetylalanine|||Nuclear pore complex protein Nup88|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204887|||http://purl.uniprot.org/annotation/VAR_029340|||http://purl.uniprot.org/annotation/VAR_082159|||http://purl.uniprot.org/annotation/VAR_082160|||http://purl.uniprot.org/annotation/VAR_082161
http://togogenome.org/gene/9606:MRPL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX20                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein uL16m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239841|||http://purl.uniprot.org/annotation/VAR_052006|||http://purl.uniprot.org/annotation/VAR_052007|||http://purl.uniprot.org/annotation/VAR_052008
http://togogenome.org/gene/9606:PACSIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TZC3|||http://purl.uniprot.org/uniprot/Q9BY11                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase C and casein kinase substrate in neurons protein 1|||Reduces membrane-binding. Abolishes membrane tubulation.|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161792|||http://purl.uniprot.org/annotation/VAR_053554
http://togogenome.org/gene/9606:H2AC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L7L0                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 3|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230201
http://togogenome.org/gene/9606:SRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZK31|||http://purl.uniprot.org/uniprot/Q8N3F4|||http://purl.uniprot.org/uniprot/Q9GZT4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Strand                                                                                  ^@                                                                                  N6-(pyridoxal phosphate)lysine|||Proton acceptor|||S-nitrosocysteine|||Serine racemase|||Tryptophan synthase beta chain-like PALP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185650
http://togogenome.org/gene/9606:LONRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LON peptidase N-terminal domain and RING finger protein 1|||Lon N-terminal|||Phosphoserine|||Polar residues|||RING-type 1|||RING-type 2|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277669|||http://purl.uniprot.org/annotation/VAR_058706|||http://purl.uniprot.org/annotation/VSP_037971
http://togogenome.org/gene/9606:CRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z478|||http://purl.uniprot.org/uniprot/P06850                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Corticoliberin|||Corticotropin-releasing factor|||Disordered|||Found in patients with autosomal dominant nocturnal frontal lobe epilepsy; unknown pathological significance; results in decreased protein levels; decreased protein secretion.|||Isoleucine amide|||No effect on affinity for CRFR1.|||Pro residues|||Strongly reduced affinity for CRFR1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006212|||http://purl.uniprot.org/annotation/PRO_0000006213|||http://purl.uniprot.org/annotation/PRO_5006608285|||http://purl.uniprot.org/annotation/VAR_075504
http://togogenome.org/gene/9606:TULP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00295                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Phosphoserine|||Tubby-related protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186468|||http://purl.uniprot.org/annotation/VAR_022136|||http://purl.uniprot.org/annotation/VAR_024679|||http://purl.uniprot.org/annotation/VAR_029312|||http://purl.uniprot.org/annotation/VAR_057320|||http://purl.uniprot.org/annotation/VAR_064760
http://togogenome.org/gene/9606:APBB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95704|||http://purl.uniprot.org/uniprot/Q59EH2|||http://purl.uniprot.org/uniprot/Q96DX9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Amyloid-beta A4 precursor protein-binding family B member 3|||In isoform I-214.|||In isoform I-245.|||In isoform I.|||In isoform III.|||In isoform IV.|||PID|||PID 1|||PID 2|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076054|||http://purl.uniprot.org/annotation/VAR_024702|||http://purl.uniprot.org/annotation/VAR_029518|||http://purl.uniprot.org/annotation/VSP_006799|||http://purl.uniprot.org/annotation/VSP_006800|||http://purl.uniprot.org/annotation/VSP_006801|||http://purl.uniprot.org/annotation/VSP_047811|||http://purl.uniprot.org/annotation/VSP_047812|||http://purl.uniprot.org/annotation/VSP_047813|||http://purl.uniprot.org/annotation/VSP_047814
http://togogenome.org/gene/9606:SLC10A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0GE19                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In SSASKS.|||In SSASKS; decreased protein levels; decreased expression at the cell membrane.|||In SSASKS; mild skeletal features; results in altered regulation of calcium homeostasis and abnormal distribution of cellular calcium in patient fibroblasts.|||In SSASKS; unknown pathological significance.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Sodium/bile acid cotransporter 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278250|||http://purl.uniprot.org/annotation/VAR_082056|||http://purl.uniprot.org/annotation/VAR_082057|||http://purl.uniprot.org/annotation/VAR_082058|||http://purl.uniprot.org/annotation/VAR_082059|||http://purl.uniprot.org/annotation/VAR_082060|||http://purl.uniprot.org/annotation/VSP_023215|||http://purl.uniprot.org/annotation/VSP_023216|||http://purl.uniprot.org/annotation/VSP_023217|||http://purl.uniprot.org/annotation/VSP_023218|||http://purl.uniprot.org/annotation/VSP_023219|||http://purl.uniprot.org/annotation/VSP_023220|||http://purl.uniprot.org/annotation/VSP_023221|||http://purl.uniprot.org/annotation/VSP_023222|||http://purl.uniprot.org/annotation/VSP_023223|||http://purl.uniprot.org/annotation/VSP_059321
http://togogenome.org/gene/9606:PCSK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92824                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AC 1|||AC 2|||CRM (Cys-rich motif)|||Cell attachment site|||Charge relay system|||Cleavage; by autolysis|||Cytoplasmic|||Extracellular|||FU 1|||FU 10|||FU 11|||FU 12|||FU 13|||FU 14|||FU 15|||FU 16|||FU 17|||FU 18|||FU 19|||FU 2|||FU 20|||FU 21|||FU 22|||FU 3|||FU 4|||FU 5|||FU 6|||FU 7|||FU 8|||FU 9|||Helical|||In isoform PC6A.|||N-linked (GlcNAc...) asparagine|||P/Homo B|||PLAC|||Peptidase S8|||Proprotein convertase subtilisin/kexin type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027102|||http://purl.uniprot.org/annotation/PRO_0000027103|||http://purl.uniprot.org/annotation/VSP_042017|||http://purl.uniprot.org/annotation/VSP_042018
http://togogenome.org/gene/9606:BEND6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZJ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  BEN|||BEN domain-containing protein 6|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295660|||http://purl.uniprot.org/annotation/VSP_026961|||http://purl.uniprot.org/annotation/VSP_026962|||http://purl.uniprot.org/annotation/VSP_026963|||http://purl.uniprot.org/annotation/VSP_026964|||http://purl.uniprot.org/annotation/VSP_026965|||http://purl.uniprot.org/annotation/VSP_026966
http://togogenome.org/gene/9606:RLF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13129                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger protein Rlf                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047325|||http://purl.uniprot.org/annotation/VAR_052739|||http://purl.uniprot.org/annotation/VAR_052740|||http://purl.uniprot.org/annotation/VAR_052741|||http://purl.uniprot.org/annotation/VAR_052742|||http://purl.uniprot.org/annotation/VAR_061929|||http://purl.uniprot.org/annotation/VAR_061930
http://togogenome.org/gene/9606:DOCK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A015|||http://purl.uniprot.org/uniprot/Q68DL4|||http://purl.uniprot.org/uniprot/Q9H7D0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 5|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189992|||http://purl.uniprot.org/annotation/VAR_033886|||http://purl.uniprot.org/annotation/VAR_033887|||http://purl.uniprot.org/annotation/VAR_053065|||http://purl.uniprot.org/annotation/VAR_053066|||http://purl.uniprot.org/annotation/VSP_021868
http://togogenome.org/gene/9606:ZFAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6H1|||http://purl.uniprot.org/uniprot/E9PBN4|||http://purl.uniprot.org/uniprot/F8W7M8|||http://purl.uniprot.org/uniprot/Q4KMQ4|||http://purl.uniprot.org/uniprot/Q6PJQ2|||http://purl.uniprot.org/uniprot/Q9P243                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in a patient with global developmental delay; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Polar residues|||Zinc finger protein ZFAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047566|||http://purl.uniprot.org/annotation/VAR_024840|||http://purl.uniprot.org/annotation/VAR_045815|||http://purl.uniprot.org/annotation/VAR_052819|||http://purl.uniprot.org/annotation/VAR_084658|||http://purl.uniprot.org/annotation/VSP_016959|||http://purl.uniprot.org/annotation/VSP_034938|||http://purl.uniprot.org/annotation/VSP_034939|||http://purl.uniprot.org/annotation/VSP_045461
http://togogenome.org/gene/9606:BTBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0C5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||BTB/POZ domain-containing protein 1|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186208|||http://purl.uniprot.org/annotation/VSP_047146|||http://purl.uniprot.org/annotation/VSP_047147
http://togogenome.org/gene/9606:APBB1IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5R6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Amyloid beta A4 precursor protein-binding family B member 1-interacting protein|||Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181347|||http://purl.uniprot.org/annotation/VAR_050098|||http://purl.uniprot.org/annotation/VAR_059447|||http://purl.uniprot.org/annotation/VSP_056542|||http://purl.uniprot.org/annotation/VSP_056543
http://togogenome.org/gene/9606:MRGPRX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member X3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069782|||http://purl.uniprot.org/annotation/VAR_019434|||http://purl.uniprot.org/annotation/VAR_025507
http://togogenome.org/gene/9606:PLOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02809                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fe2OG dioxygenase|||In EDSKSCL1.|||In EDSKSCL1; loss of enzyme activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of activity.|||Loss of enzyme activity.|||N-linked (GlcNAc...) asparagine|||Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024678|||http://purl.uniprot.org/annotation/VAR_006354|||http://purl.uniprot.org/annotation/VAR_006355|||http://purl.uniprot.org/annotation/VAR_006356|||http://purl.uniprot.org/annotation/VAR_009269|||http://purl.uniprot.org/annotation/VAR_014220|||http://purl.uniprot.org/annotation/VAR_023466|||http://purl.uniprot.org/annotation/VAR_023467|||http://purl.uniprot.org/annotation/VAR_023468|||http://purl.uniprot.org/annotation/VAR_032754|||http://purl.uniprot.org/annotation/VAR_032755|||http://purl.uniprot.org/annotation/VAR_032756|||http://purl.uniprot.org/annotation/VAR_035479|||http://purl.uniprot.org/annotation/VSP_056300
http://togogenome.org/gene/9606:HCLS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14317                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cortactin 1|||Cortactin 2|||Cortactin 3|||Cortactin 4; truncated|||Disordered|||Hematopoietic lineage cell-specific protein|||In isoform 2.|||Involved in HAX-1 binding|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FGR|||Phosphotyrosine; by SYK and FES|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083921|||http://purl.uniprot.org/annotation/VAR_055006|||http://purl.uniprot.org/annotation/VAR_055007|||http://purl.uniprot.org/annotation/VAR_056910|||http://purl.uniprot.org/annotation/VSP_056429|||http://purl.uniprot.org/annotation/VSP_056430
http://togogenome.org/gene/9606:RPL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07020                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DBA18; unknown pathological significance.|||In isoform 2.|||Large ribosomal subunit protein eL18|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132769|||http://purl.uniprot.org/annotation/VAR_081935|||http://purl.uniprot.org/annotation/VSP_055170
http://togogenome.org/gene/9606:EEF1AKMT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPD7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Abolishes protein-lysine N-methyltransferase activity.|||EEF1A lysine methyltransferase 4|||Phosphotyrosine|||Reduces protein-lysine N-methyltransferase activity.|||Required for methyltransferase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000443290|||http://purl.uniprot.org/annotation/VAR_047752
http://togogenome.org/gene/9606:SRP54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61011                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In SCN8.|||In SCN8; decreased granulocyte proliferation; delayed granulocytic differentiation; impaired signaling; induced autophagy.|||In SCN8; decreased granulocyte proliferation; increased apoptosis.|||In SCN8; decreased granulocyte proliferation; induced autophagy.|||In SCN8; decreases expression levels; decreases GTPase activity; decreases neutrophil numbers and migration capacity.|||In SCN8; decreases expression levels; decreases neutrophil numbers and migration capacity; faster dissociation of the interaction with the SRP receptor subunit SRPRA; reduced SR compaction; impaired interaction with SR; impaired detachment from ribosome; effects on enzymatic activity are unclear as both normal and reduced GTPase activity have been reported.|||In SCN8; decreases expression levels; slightly decreases GTPase activity; decreases neutrophil numbers and migration capacity; decreased granulocyte proliferation; delayed granulocytic differentiation; impaired signaling; increased apoptosis; induced autophagy.|||In isoform 2.|||M-domain|||NG domain|||Signal recognition particle subunit SRP54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101192|||http://purl.uniprot.org/annotation/VAR_083566|||http://purl.uniprot.org/annotation/VAR_083567|||http://purl.uniprot.org/annotation/VAR_083568|||http://purl.uniprot.org/annotation/VAR_083569|||http://purl.uniprot.org/annotation/VAR_083570|||http://purl.uniprot.org/annotation/VAR_083571|||http://purl.uniprot.org/annotation/VAR_083572|||http://purl.uniprot.org/annotation/VAR_083573|||http://purl.uniprot.org/annotation/VSP_043696
http://togogenome.org/gene/9606:PSMD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16401                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 5|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173835|||http://purl.uniprot.org/annotation/VAR_051556|||http://purl.uniprot.org/annotation/VAR_051557|||http://purl.uniprot.org/annotation/VSP_045176
http://togogenome.org/gene/9606:FJX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VR8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Four-jointed box protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333045|||http://purl.uniprot.org/annotation/VAR_043117|||http://purl.uniprot.org/annotation/VAR_062233
http://togogenome.org/gene/9606:TVP23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NH52                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Golgi apparatus membrane protein TVP23 homolog A|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327940|||http://purl.uniprot.org/annotation/VSP_054190
http://togogenome.org/gene/9606:NPIPA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJI5|||http://purl.uniprot.org/uniprot/P0DM63                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Nuclear pore complex-interacting protein family member A7|||Nuclear pore complex-interacting protein family member A8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423919|||http://purl.uniprot.org/annotation/PRO_0000423925
http://togogenome.org/gene/9606:CYP27B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15528                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial|||In VDDR1A.|||In VDDR1A; 11% of wild-type activity.|||In VDDR1A; 2.3% of wild-type activity.|||In VDDR1A; 22% of wild-type activity.|||In VDDR1A; complete loss of activity.|||Mitochondrion|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003622|||http://purl.uniprot.org/annotation/VAR_016952|||http://purl.uniprot.org/annotation/VAR_016953|||http://purl.uniprot.org/annotation/VAR_016954|||http://purl.uniprot.org/annotation/VAR_016955|||http://purl.uniprot.org/annotation/VAR_016956|||http://purl.uniprot.org/annotation/VAR_016957|||http://purl.uniprot.org/annotation/VAR_016958|||http://purl.uniprot.org/annotation/VAR_016959|||http://purl.uniprot.org/annotation/VAR_016960|||http://purl.uniprot.org/annotation/VAR_016961|||http://purl.uniprot.org/annotation/VAR_016967|||http://purl.uniprot.org/annotation/VAR_016968|||http://purl.uniprot.org/annotation/VAR_016969|||http://purl.uniprot.org/annotation/VAR_016970|||http://purl.uniprot.org/annotation/VAR_016971|||http://purl.uniprot.org/annotation/VAR_016972|||http://purl.uniprot.org/annotation/VAR_016973|||http://purl.uniprot.org/annotation/VAR_016974|||http://purl.uniprot.org/annotation/VAR_018841
http://togogenome.org/gene/9606:CLSTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3Q1|||http://purl.uniprot.org/uniprot/O94985                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with APBA2.|||Acidic residues|||CTF1-alpha|||Cadherin|||Cadherin 1|||Cadherin 2|||Calsyntenin-1|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on APBA2-binding.|||Polar residues|||Soluble Alc-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004021|||http://purl.uniprot.org/annotation/PRO_0000323597|||http://purl.uniprot.org/annotation/PRO_0000323598|||http://purl.uniprot.org/annotation/PRO_5002804102|||http://purl.uniprot.org/annotation/VAR_039552|||http://purl.uniprot.org/annotation/VAR_039553|||http://purl.uniprot.org/annotation/VAR_039554|||http://purl.uniprot.org/annotation/VAR_039555|||http://purl.uniprot.org/annotation/VAR_039556|||http://purl.uniprot.org/annotation/VAR_048582|||http://purl.uniprot.org/annotation/VSP_032035
http://togogenome.org/gene/9606:SLC12A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AV02                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 12 member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305287|||http://purl.uniprot.org/annotation/VAR_035199|||http://purl.uniprot.org/annotation/VAR_035200|||http://purl.uniprot.org/annotation/VAR_035201|||http://purl.uniprot.org/annotation/VAR_035202|||http://purl.uniprot.org/annotation/VAR_062148|||http://purl.uniprot.org/annotation/VSP_028327|||http://purl.uniprot.org/annotation/VSP_028328|||http://purl.uniprot.org/annotation/VSP_028329|||http://purl.uniprot.org/annotation/VSP_028330|||http://purl.uniprot.org/annotation/VSP_028331|||http://purl.uniprot.org/annotation/VSP_028332
http://togogenome.org/gene/9606:FLT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36888                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PTPN11/SHP2 and phosphorylation of PTPN11/SHP2.|||Abolishes kinase activity.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand|||In acute lymphoblastic leukemia patients and acute myelogenous leukemia patients; somatic mutation; constitutively activated.|||In acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated.|||In acute lymphoblastic leukemia patients; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No significant effect on tyrosine phosphorylation. Abolishes activation of STAT5A.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Receptor-type tyrosine-protein kinase FLT3|||Reduced phosphorylation of the wild-type kinase in response to ligand binding. No effect on the phosphorylation of the constitutively activated mutant kinase variants. Abolishes activation of STAT5A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016778|||http://purl.uniprot.org/annotation/VAR_034677|||http://purl.uniprot.org/annotation/VAR_034678|||http://purl.uniprot.org/annotation/VAR_042069|||http://purl.uniprot.org/annotation/VAR_042070|||http://purl.uniprot.org/annotation/VAR_042071|||http://purl.uniprot.org/annotation/VAR_042072|||http://purl.uniprot.org/annotation/VAR_054149|||http://purl.uniprot.org/annotation/VAR_061291|||http://purl.uniprot.org/annotation/VAR_065679|||http://purl.uniprot.org/annotation/VAR_065680|||http://purl.uniprot.org/annotation/VAR_065681|||http://purl.uniprot.org/annotation/VAR_065682|||http://purl.uniprot.org/annotation/VAR_065683|||http://purl.uniprot.org/annotation/VAR_065684|||http://purl.uniprot.org/annotation/VSP_041796
http://togogenome.org/gene/9606:CGRRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99675                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Cell growth regulator with RING finger domain protein 1|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055869|||http://purl.uniprot.org/annotation/VAR_052081
http://togogenome.org/gene/9606:TIMM8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YDA8|||http://purl.uniprot.org/uniprot/O60220                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In MTS; disrupts the assembly of the heterohexamer with TIMM13.|||Mitochondrial import inner membrane translocase subunit Tim8 A|||Phosphoserine|||Tim10-like|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193584|||http://purl.uniprot.org/annotation/VAR_010237
http://togogenome.org/gene/9606:DCST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXB8|||http://purl.uniprot.org/uniprot/B4DXE3|||http://purl.uniprot.org/uniprot/Q5T197                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||Dendritic cell-specific transmembrane protein-like|||Disordered|||E3 ubiquitin-protein ligase DCST1|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||RING-type|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278824|||http://purl.uniprot.org/annotation/VAR_030868|||http://purl.uniprot.org/annotation/VAR_056859|||http://purl.uniprot.org/annotation/VSP_023406|||http://purl.uniprot.org/annotation/VSP_023407|||http://purl.uniprot.org/annotation/VSP_045619
http://togogenome.org/gene/9606:IL2RB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14784                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In IMD63.|||In IMD63; decreased protein abundance; changed IL-2 and IL-15 signaling pathways; plasma levels of both IL2 and IL15 were increased; associated with increased amounts of phosphorylated STAT5A.|||Interleukin-2 receptor subunit beta|||N-linked (GlcNAc...) asparagine|||Partial loss of interaction with SHB; when associated with F-418.|||Partial loss of interaction with SHB; when associated with F-536.|||Pro residues|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010878|||http://purl.uniprot.org/annotation/VAR_019998|||http://purl.uniprot.org/annotation/VAR_021994|||http://purl.uniprot.org/annotation/VAR_061186|||http://purl.uniprot.org/annotation/VAR_083103|||http://purl.uniprot.org/annotation/VAR_083104
http://togogenome.org/gene/9606:EGFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2I3|||http://purl.uniprot.org/uniprot/C9JYS6|||http://purl.uniprot.org/uniprot/E7BSV0|||http://purl.uniprot.org/uniprot/F2YGG7|||http://purl.uniprot.org/uniprot/P00533|||http://purl.uniprot.org/uniprot/Q504U8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  50% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092.|||Abolishes autophosphorylation and activation of downstream kinases.|||Abolishes interaction with CBLC.|||Abolishes kinase activity.|||Abolishes palmitoylation.|||Abolishes phosphorylation.|||Approximate|||Constitutively activated kinase.|||Cytoplasmic|||Decreased palmitoylation.|||Decreases intramolecular interactions and facilitates EGF binding.|||Decreases intramolecular interactions and facilitates EGF binding. Increased EGF binding; when associated with A-587; A-590 and A-609.|||Disordered|||Epidermal growth factor receptor|||Extracellular|||Found in a lung cancer sample.|||Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type.|||Found in a lung cancer sample; increased kinase activity.|||Found in a lung cancer sample; more sensitive to gefitinib than wild-type.|||Found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity; more sensitive to gefitinib than wild-type.|||Found in a lung cancer sample; somatic mutation; strongly increased kinase activity; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Important for dimerization, phosphorylation and activation|||Important for interaction with PIK3C2B|||In NISBD2; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased EGF binding.|||Increased EGF binding; when associated with A-587; A-590 and A-609.|||Increased EGF binding; when associated with A-590 and A-609.|||Increased phosphorylation.|||N-linked (GlcNAc...) (complex) asparagine; atypical; partial|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||N-linked (GlcNAc...) asparagine; partial|||N6-(2-hydroxyisobutyryl)lysine|||No change in interaction with PIK3C2B.|||No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016.|||No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016.|||No effect on interaction with CBLC.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC and PKD/PRKD1|||Phosphothreonine; by PKD/PRKD1|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Receptor protein-tyrosine kinase|||Reduced autophosphorylation.|||Reduced phosphorylation.|||S-palmitoyl cysteine|||Strongly decreases interaction with CBLC.|||Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287.|||Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309.|||Strongly reduced phosphorylation.|||Variant EGFR vIII; found in a lung cancer sample; somatic mutation; induces lung cancer when exogenously expressed.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000227|||http://purl.uniprot.org/annotation/PRO_0000016665|||http://purl.uniprot.org/annotation/PRO_5003216067|||http://purl.uniprot.org/annotation/PRO_5003289839|||http://purl.uniprot.org/annotation/PRO_5014586593|||http://purl.uniprot.org/annotation/VAR_019293|||http://purl.uniprot.org/annotation/VAR_019294|||http://purl.uniprot.org/annotation/VAR_019295|||http://purl.uniprot.org/annotation/VAR_019296|||http://purl.uniprot.org/annotation/VAR_019297|||http://purl.uniprot.org/annotation/VAR_019298|||http://purl.uniprot.org/annotation/VAR_019299|||http://purl.uniprot.org/annotation/VAR_019300|||http://purl.uniprot.org/annotation/VAR_026084|||http://purl.uniprot.org/annotation/VAR_026085|||http://purl.uniprot.org/annotation/VAR_026086|||http://purl.uniprot.org/annotation/VAR_026087|||http://purl.uniprot.org/annotation/VAR_026088|||http://purl.uniprot.org/annotation/VAR_026089|||http://purl.uniprot.org/annotation/VAR_026090|||http://purl.uniprot.org/annotation/VAR_026091|||http://purl.uniprot.org/annotation/VAR_026092|||http://purl.uniprot.org/annotation/VAR_026093|||http://purl.uniprot.org/annotation/VAR_026094|||http://purl.uniprot.org/annotation/VAR_026095|||http://purl.uniprot.org/annotation/VAR_026096|||http://purl.uniprot.org/annotation/VAR_026097|||http://purl.uniprot.org/annotation/VAR_026098|||http://purl.uniprot.org/annotation/VAR_026099|||http://purl.uniprot.org/annotation/VAR_026100|||http://purl.uniprot.org/annotation/VAR_026101|||http://purl.uniprot.org/annotation/VAR_026102|||http://purl.uniprot.org/annotation/VAR_026103|||http://purl.uniprot.org/annotation/VAR_042095|||http://purl.uniprot.org/annotation/VAR_042096|||http://purl.uniprot.org/annotation/VAR_066493|||http://purl.uniprot.org/annotation/VAR_069498|||http://purl.uniprot.org/annotation/VAR_069499|||http://purl.uniprot.org/annotation/VAR_069500|||http://purl.uniprot.org/annotation/VAR_069501|||http://purl.uniprot.org/annotation/VAR_069502|||http://purl.uniprot.org/annotation/VAR_069503|||http://purl.uniprot.org/annotation/VAR_069504|||http://purl.uniprot.org/annotation/VAR_069505|||http://purl.uniprot.org/annotation/VAR_072435|||http://purl.uniprot.org/annotation/VSP_002887|||http://purl.uniprot.org/annotation/VSP_002888|||http://purl.uniprot.org/annotation/VSP_002889|||http://purl.uniprot.org/annotation/VSP_002890|||http://purl.uniprot.org/annotation/VSP_002891|||http://purl.uniprot.org/annotation/VSP_002892
http://togogenome.org/gene/9606:PIP5K1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14986|||http://purl.uniprot.org/uniprot/Q7KYT6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase type-1 beta|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185458|||http://purl.uniprot.org/annotation/VAR_023712|||http://purl.uniprot.org/annotation/VSP_016010|||http://purl.uniprot.org/annotation/VSP_016011|||http://purl.uniprot.org/annotation/VSP_054771
http://togogenome.org/gene/9606:GRIN2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15399|||http://purl.uniprot.org/uniprot/Q59G17                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic residues|||Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency.|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||Found in patients with schizophrenia; unknown pathological significance.|||Functional determinant of NMDA receptors|||Glutamate receptor ionotropic, NMDA 2D|||Helical|||In DEE46; gain-of-function mutation that potentiates ionotropic glutamate receptor signaling; mutant receptors are activated by lower concentrations of glutamate and glycine and show slower deactivation after agonist removal as well as decreased sensitivity to allosteric inhibitors indicating that NMDA glutamate receptor activity is changed.|||In a breast cancer sample; somatic mutation.|||Increased glutamate and glycine agonist potency.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine|||Pore-forming|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011583|||http://purl.uniprot.org/annotation/VAR_035698|||http://purl.uniprot.org/annotation/VAR_035699|||http://purl.uniprot.org/annotation/VAR_035700|||http://purl.uniprot.org/annotation/VAR_077103|||http://purl.uniprot.org/annotation/VAR_079975|||http://purl.uniprot.org/annotation/VAR_079976|||http://purl.uniprot.org/annotation/VAR_079977|||http://purl.uniprot.org/annotation/VAR_079978|||http://purl.uniprot.org/annotation/VAR_079979|||http://purl.uniprot.org/annotation/VAR_079980|||http://purl.uniprot.org/annotation/VAR_079981|||http://purl.uniprot.org/annotation/VAR_079982|||http://purl.uniprot.org/annotation/VAR_079983
http://togogenome.org/gene/9606:RFPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75678                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||In isoform 2.|||In isoform 3.|||RING-type; degenerate|||Ret finger protein-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056031|||http://purl.uniprot.org/annotation/VAR_060534|||http://purl.uniprot.org/annotation/VAR_060535|||http://purl.uniprot.org/annotation/VAR_060536|||http://purl.uniprot.org/annotation/VAR_060537|||http://purl.uniprot.org/annotation/VAR_060538|||http://purl.uniprot.org/annotation/VAR_060539|||http://purl.uniprot.org/annotation/VAR_060540|||http://purl.uniprot.org/annotation/VSP_038326|||http://purl.uniprot.org/annotation/VSP_038327|||http://purl.uniprot.org/annotation/VSP_059822|||http://purl.uniprot.org/annotation/VSP_059823
http://togogenome.org/gene/9606:SOX17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6I2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Disordered|||HMG box|||In VUR3.|||In VUR3; increased levels of the mutant protein that is associated with increased suppression of CTNNB1 signaling of the Wnt pathway compared to wild-type.|||Polar residues|||Pro residues|||Sox C-terminal|||Transcription factor SOX-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048765|||http://purl.uniprot.org/annotation/VAR_065168|||http://purl.uniprot.org/annotation/VAR_065169|||http://purl.uniprot.org/annotation/VAR_065170|||http://purl.uniprot.org/annotation/VAR_078774
http://togogenome.org/gene/9606:OPTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBM4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by MMP13|||Cleavage; by MMP2|||Cleavage; by MMP7|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRNT|||N-linked (GlcNAc...) asparagine|||Opticin|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032765|||http://purl.uniprot.org/annotation/VAR_055228|||http://purl.uniprot.org/annotation/VAR_055229|||http://purl.uniprot.org/annotation/VAR_055230
http://togogenome.org/gene/9606:ZNF480                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8E1|||http://purl.uniprot.org/uniprot/F8WEZ9|||http://purl.uniprot.org/uniprot/Q8WV37                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 480                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047607|||http://purl.uniprot.org/annotation/VAR_033569|||http://purl.uniprot.org/annotation/VAR_035584|||http://purl.uniprot.org/annotation/VSP_016214|||http://purl.uniprot.org/annotation/VSP_016215
http://togogenome.org/gene/9606:CACNG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y698                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In MRD10; significantly reduced ability to bind GRIA1 or GRIA2 AMPARs; cell surface expression of GRIA1 is reduced in transfected hippocampal neurons and HEK293 cells producing mutant protein compared to cells producing the wild-type.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Voltage-dependent calcium channel gamma-2 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164673|||http://purl.uniprot.org/annotation/VAR_066599
http://togogenome.org/gene/9606:SWAP70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUB9|||http://purl.uniprot.org/uniprot/E7EMB1|||http://purl.uniprot.org/uniprot/Q9UH65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid and the localization to the loose actin filament arrays.|||Abolishes binding to plasma membrane.|||Affects targeting to loose actin filament arrays.|||EF-hand|||PH|||Reduced binding to phosphatidylinositol 3,4-bisphosphate and reduced association with actin filament.|||Switch-associated protein 70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240280|||http://purl.uniprot.org/annotation/VAR_026717|||http://purl.uniprot.org/annotation/VAR_059548
http://togogenome.org/gene/9606:PSMG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95456                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Proteasome assembly chaperone 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080018|||http://purl.uniprot.org/annotation/VAR_054014|||http://purl.uniprot.org/annotation/VSP_017261
http://togogenome.org/gene/9606:CYP11B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15538|||http://purl.uniprot.org/uniprot/Q8TDD0                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Benign variant; decreases steroid 11-beta-hydroxylase activity.|||Cytochrome P450 11B1, mitochondrial|||In AH4.|||In AH4; abolishes steroid 11-beta-hydroxylase activity.|||In AH4; almost abolishes steroid 11-beta-hydroxylase activity.|||In AH4; classic; abolishes steroid 11-beta-hydroxylase activity.|||In AH4; classic; highly decreases steroid 11-beta-hydroxylase activity.|||In AH4; decreases steroid 11-beta-hydroxylase activity.|||In AH4; high reduction of steroid 11-beta-monooxygenase activity.|||In AH4; highly decreases steroid 11-beta-hydroxylase activity.|||In AH4; non-classic; almost abolishes steroid 11-beta-hydroxylase activity.|||In AH4; non-classic; decreases steroid 11-beta-hydroxylase activity.|||In AH4; non-classic; highly decreases steroid 11-beta-hydroxylase activity.|||In AH4; slightly decreases steroid 11-beta-hydroxylase activity.|||In AH4; unknown pathological significance.|||In isoform 2.|||Mitochondrion|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003596|||http://purl.uniprot.org/annotation/VAR_001260|||http://purl.uniprot.org/annotation/VAR_001261|||http://purl.uniprot.org/annotation/VAR_001262|||http://purl.uniprot.org/annotation/VAR_001263|||http://purl.uniprot.org/annotation/VAR_001264|||http://purl.uniprot.org/annotation/VAR_001265|||http://purl.uniprot.org/annotation/VAR_008687|||http://purl.uniprot.org/annotation/VAR_014145|||http://purl.uniprot.org/annotation/VAR_014146|||http://purl.uniprot.org/annotation/VAR_014147|||http://purl.uniprot.org/annotation/VAR_014148|||http://purl.uniprot.org/annotation/VAR_014149|||http://purl.uniprot.org/annotation/VAR_014150|||http://purl.uniprot.org/annotation/VAR_014638|||http://purl.uniprot.org/annotation/VAR_014639|||http://purl.uniprot.org/annotation/VAR_014640|||http://purl.uniprot.org/annotation/VAR_014641|||http://purl.uniprot.org/annotation/VAR_014642|||http://purl.uniprot.org/annotation/VAR_048462|||http://purl.uniprot.org/annotation/VAR_048463|||http://purl.uniprot.org/annotation/VAR_065196|||http://purl.uniprot.org/annotation/VAR_065197|||http://purl.uniprot.org/annotation/VAR_065666|||http://purl.uniprot.org/annotation/VAR_065667|||http://purl.uniprot.org/annotation/VAR_074493|||http://purl.uniprot.org/annotation/VAR_074494|||http://purl.uniprot.org/annotation/VAR_074495|||http://purl.uniprot.org/annotation/VAR_074496|||http://purl.uniprot.org/annotation/VAR_074497|||http://purl.uniprot.org/annotation/VAR_074498|||http://purl.uniprot.org/annotation/VAR_074499|||http://purl.uniprot.org/annotation/VAR_074500|||http://purl.uniprot.org/annotation/VAR_074501|||http://purl.uniprot.org/annotation/VAR_074502|||http://purl.uniprot.org/annotation/VAR_074503|||http://purl.uniprot.org/annotation/VAR_074504|||http://purl.uniprot.org/annotation/VAR_074505|||http://purl.uniprot.org/annotation/VAR_074506|||http://purl.uniprot.org/annotation/VAR_074507|||http://purl.uniprot.org/annotation/VAR_074508|||http://purl.uniprot.org/annotation/VAR_074509|||http://purl.uniprot.org/annotation/VAR_074510|||http://purl.uniprot.org/annotation/VAR_074511|||http://purl.uniprot.org/annotation/VAR_074512|||http://purl.uniprot.org/annotation/VAR_074513|||http://purl.uniprot.org/annotation/VAR_074514|||http://purl.uniprot.org/annotation/VAR_074515|||http://purl.uniprot.org/annotation/VAR_074516|||http://purl.uniprot.org/annotation/VAR_074517|||http://purl.uniprot.org/annotation/VAR_074518|||http://purl.uniprot.org/annotation/VAR_074519|||http://purl.uniprot.org/annotation/VAR_074520|||http://purl.uniprot.org/annotation/VAR_074521|||http://purl.uniprot.org/annotation/VAR_074522|||http://purl.uniprot.org/annotation/VAR_074523|||http://purl.uniprot.org/annotation/VAR_074524|||http://purl.uniprot.org/annotation/VAR_074525|||http://purl.uniprot.org/annotation/VAR_074526|||http://purl.uniprot.org/annotation/VAR_074527|||http://purl.uniprot.org/annotation/VAR_074528|||http://purl.uniprot.org/annotation/VAR_074529|||http://purl.uniprot.org/annotation/VAR_074530|||http://purl.uniprot.org/annotation/VAR_074531|||http://purl.uniprot.org/annotation/VAR_074532|||http://purl.uniprot.org/annotation/VAR_074533|||http://purl.uniprot.org/annotation/VAR_074534|||http://purl.uniprot.org/annotation/VAR_075553|||http://purl.uniprot.org/annotation/VAR_075554|||http://purl.uniprot.org/annotation/VSP_043308
http://togogenome.org/gene/9606:MICOS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGZ0                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||MICOS complex subunit MIC10|||Mitochondrial intermembrane|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249459|||http://purl.uniprot.org/annotation/VSP_042062|||http://purl.uniprot.org/annotation/VSP_042063
http://togogenome.org/gene/9606:FMNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  DAD|||Disordered|||FH2|||Formin-like protein 3|||GBD/FH3|||In isoform 2.|||In isoform 3 and isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289095|||http://purl.uniprot.org/annotation/VSP_025892|||http://purl.uniprot.org/annotation/VSP_025893
http://togogenome.org/gene/9606:CHCHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6H1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 2|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||In PARK22; does not affect subcellular location.|||In PARK22; unknown pathological significance; does not affect subcellular location.|||May influence risk for Lewy body disorders.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129160|||http://purl.uniprot.org/annotation/VAR_048699|||http://purl.uniprot.org/annotation/VAR_076293|||http://purl.uniprot.org/annotation/VAR_076294|||http://purl.uniprot.org/annotation/VAR_076295|||http://purl.uniprot.org/annotation/VAR_076296|||http://purl.uniprot.org/annotation/VAR_076297|||http://purl.uniprot.org/annotation/VAR_076298|||http://purl.uniprot.org/annotation/VAR_076299|||http://purl.uniprot.org/annotation/VAR_076300|||http://purl.uniprot.org/annotation/VAR_076301
http://togogenome.org/gene/9606:TMEM72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PK05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane protein 72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319055|||http://purl.uniprot.org/annotation/VSP_031343
http://togogenome.org/gene/9606:HSPB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJY1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Heat shock protein beta-8|||In HMN2A; no effect on cytoskeleton architecture; no effect on cytoplasmic location; increased interaction with BAG3.|||In HMN2A; no effect on cytoskeleton architecture; no effect on cytoplasmic location; no effect on interaction with BAG3.|||In HMN2A; strengthen interaction with HSPB1.|||In HMN2A; strengthen interaction with HSPB1; no effect on cytoskeleton architecture; no effect on cytoplasmic location; increased interaction with BAG3.|||In a glioblastoma multiforme sample; somatic mutation.|||Phosphoserine|||Phosphothreonine; by PKC; in vitro|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125945|||http://purl.uniprot.org/annotation/VAR_018504|||http://purl.uniprot.org/annotation/VAR_018505|||http://purl.uniprot.org/annotation/VAR_042244|||http://purl.uniprot.org/annotation/VAR_042245|||http://purl.uniprot.org/annotation/VAR_078133|||http://purl.uniprot.org/annotation/VAR_078134|||http://purl.uniprot.org/annotation/VAR_078135
http://togogenome.org/gene/9606:PDE6G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18545                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166117|||http://purl.uniprot.org/annotation/VAR_009294
http://togogenome.org/gene/9606:EFNA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52803                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Ephrin RBD|||Ephrin-A5|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008377|||http://purl.uniprot.org/annotation/PRO_0000008378|||http://purl.uniprot.org/annotation/VAR_012035
http://togogenome.org/gene/9606:LZTFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ48                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In BBS17.|||In isoform 2.|||In isoform 3.|||Increases BBS4, BBS8 and BBS9 ciliary localization.|||Interaction with BSS9|||Leucine zipper transcription factor-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318757|||http://purl.uniprot.org/annotation/VAR_038877|||http://purl.uniprot.org/annotation/VAR_038878|||http://purl.uniprot.org/annotation/VAR_038879|||http://purl.uniprot.org/annotation/VAR_070104|||http://purl.uniprot.org/annotation/VSP_053428|||http://purl.uniprot.org/annotation/VSP_053429|||http://purl.uniprot.org/annotation/VSP_053430
http://togogenome.org/gene/9606:RPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9Y2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Brix|||Disordered|||RNA-binding|||Ribosome production factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120248|||http://purl.uniprot.org/annotation/VAR_022871|||http://purl.uniprot.org/annotation/VAR_048421
http://togogenome.org/gene/9606:CCT8L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||T-complex protein 1 subunit theta-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347339|||http://purl.uniprot.org/annotation/VAR_046042
http://togogenome.org/gene/9606:TMPRSS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IU58|||http://purl.uniprot.org/uniprot/Q0X0F2|||http://purl.uniprot.org/uniprot/Q7Z410                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Peptidase S1 1|||Peptidase S1 2|||Peptidase S1 3|||Polar residues|||SEA|||Serase-1|||Serase-2|||Serase-3|||Transmembrane protease serine 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027867|||http://purl.uniprot.org/annotation/PRO_0000027868|||http://purl.uniprot.org/annotation/PRO_0000027869|||http://purl.uniprot.org/annotation/PRO_0000027870|||http://purl.uniprot.org/annotation/VAR_021508|||http://purl.uniprot.org/annotation/VAR_021509|||http://purl.uniprot.org/annotation/VAR_021510|||http://purl.uniprot.org/annotation/VAR_033650|||http://purl.uniprot.org/annotation/VAR_051845|||http://purl.uniprot.org/annotation/VAR_051846|||http://purl.uniprot.org/annotation/VAR_061774
http://togogenome.org/gene/9606:REN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00797                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||In ADTKD4; affects ER translocation and processing of nascent preprorenin, resulting in abolished prorenin and renin biosynthesis and secretion.|||In RTD.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase A1|||Renin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026081|||http://purl.uniprot.org/annotation/PRO_0000026082|||http://purl.uniprot.org/annotation/VAR_020375|||http://purl.uniprot.org/annotation/VAR_020376|||http://purl.uniprot.org/annotation/VAR_029171|||http://purl.uniprot.org/annotation/VAR_035087|||http://purl.uniprot.org/annotation/VAR_035088|||http://purl.uniprot.org/annotation/VAR_063770|||http://purl.uniprot.org/annotation/VSP_012899
http://togogenome.org/gene/9606:ADAM32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD9|||http://purl.uniprot.org/uniprot/B4DTC2|||http://purl.uniprot.org/uniprot/Q8TC27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 32|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029138|||http://purl.uniprot.org/annotation/PRO_0000029139|||http://purl.uniprot.org/annotation/PRO_5007491835|||http://purl.uniprot.org/annotation/VAR_051591|||http://purl.uniprot.org/annotation/VAR_055241|||http://purl.uniprot.org/annotation/VAR_055242|||http://purl.uniprot.org/annotation/VAR_055243|||http://purl.uniprot.org/annotation/VAR_055244|||http://purl.uniprot.org/annotation/VAR_061739
http://togogenome.org/gene/9606:SAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L0W4|||http://purl.uniprot.org/uniprot/Q502X4|||http://purl.uniprot.org/uniprot/Q96F10                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetyltransferase|||N6-acetyllysine|||Pro residues|||Proton donor|||Thialysine N-epsilon-acetyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074598|||http://purl.uniprot.org/annotation/VAR_020465
http://togogenome.org/gene/9606:BUD23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43709                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Probable 18S rRNA (guanine-N(7))-methyltransferase|||Resistant to down-regulation in response to TNF and IFNG combined treatment and effective coactivator for NR3C1, even in the presence of TNF and IFNG; when associated R-180.|||Resistant to down-regulation in response to TNF and IFNG combined treatment and effective coactivator for NR3C1, even in the presence of TNF and IFNG; when associated R-196.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204450|||http://purl.uniprot.org/annotation/VSP_011511|||http://purl.uniprot.org/annotation/VSP_054762
http://togogenome.org/gene/9606:OR1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV94|||http://purl.uniprot.org/uniprot/Q15619                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150417|||http://purl.uniprot.org/annotation/VAR_053118
http://togogenome.org/gene/9606:RHOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62745                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB|||ADP-ribosylasparagine; by botulinum toxin|||Abolishes binding to PKN1 and trafficking of EGF receptor.|||Abolishes methylation, palmitoylation and prenylation.|||Cysteine methyl ester|||Effector region|||No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes.|||No effect on palmitoylation or prenylation.|||No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192.|||O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230|||Phosphotyrosine|||Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189.|||Removed in mature form|||Rho-related GTP-binding protein RhoB|||S-farnesyl cysteine; in plasma membrane form|||S-geranylgeranyl cysteine; in endosomal form|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030417|||http://purl.uniprot.org/annotation/PRO_0000030418
http://togogenome.org/gene/9606:BOLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3E2                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  BolA-like protein 1|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201233|||http://purl.uniprot.org/annotation/VAR_033630
http://togogenome.org/gene/9606:HELZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYK8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type; atypical|||DEAA box|||Disordered|||Helicase with zinc finger domain 2|||In isoform 2.|||Interaction with THRAP3|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058561|||http://purl.uniprot.org/annotation/VAR_015597|||http://purl.uniprot.org/annotation/VAR_015598|||http://purl.uniprot.org/annotation/VAR_015599|||http://purl.uniprot.org/annotation/VAR_015600|||http://purl.uniprot.org/annotation/VAR_047038|||http://purl.uniprot.org/annotation/VAR_047039|||http://purl.uniprot.org/annotation/VAR_047040|||http://purl.uniprot.org/annotation/VAR_047041|||http://purl.uniprot.org/annotation/VAR_047042|||http://purl.uniprot.org/annotation/VAR_047043|||http://purl.uniprot.org/annotation/VSP_007297|||http://purl.uniprot.org/annotation/VSP_007298
http://togogenome.org/gene/9606:ZSWIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MP5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  SWIM-type|||Zinc finger SWIM domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223099|||http://purl.uniprot.org/annotation/VAR_053769|||http://purl.uniprot.org/annotation/VAR_062161
http://togogenome.org/gene/9606:DENND1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEH3|||http://purl.uniprot.org/uniprot/Q9HCG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Clathrin box|||DENN domain-containing protein 1A|||Disordered|||FXDXF motif|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Phosphomimetic mutant; abolishes the intramolecular interaction between the DENN domain and the C-terminus of the protein.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242680|||http://purl.uniprot.org/annotation/VSP_019464|||http://purl.uniprot.org/annotation/VSP_019465|||http://purl.uniprot.org/annotation/VSP_034509|||http://purl.uniprot.org/annotation/VSP_034510|||http://purl.uniprot.org/annotation/VSP_034511|||http://purl.uniprot.org/annotation/VSP_034512|||http://purl.uniprot.org/annotation/VSP_034513|||http://purl.uniprot.org/annotation/VSP_034514|||http://purl.uniprot.org/annotation/VSP_040666|||http://purl.uniprot.org/annotation/VSP_040667|||http://purl.uniprot.org/annotation/VSP_040668
http://togogenome.org/gene/9606:USP17L22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RA61                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421096
http://togogenome.org/gene/9606:ASB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBW7|||http://purl.uniprot.org/uniprot/Q96DX5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 9|||Essential for binding to CKB|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066940|||http://purl.uniprot.org/annotation/VSP_000271|||http://purl.uniprot.org/annotation/VSP_043158
http://togogenome.org/gene/9606:SLC4A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2Y0W8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Electroneutral sodium bicarbonate exchanger 1|||Extracellular|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 6 and isoform 8.|||In isoform 7.|||N-linked (GlcNAc) asparagine|||Significant reduction in zinc binding.|||VTVLP; mediates dimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328922|||http://purl.uniprot.org/annotation/VAR_048351|||http://purl.uniprot.org/annotation/VAR_048352|||http://purl.uniprot.org/annotation/VSP_052759|||http://purl.uniprot.org/annotation/VSP_052760|||http://purl.uniprot.org/annotation/VSP_052761|||http://purl.uniprot.org/annotation/VSP_052762|||http://purl.uniprot.org/annotation/VSP_052763|||http://purl.uniprot.org/annotation/VSP_052764|||http://purl.uniprot.org/annotation/VSP_052765
http://togogenome.org/gene/9606:DUSP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6W6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 10|||In isoform 2.|||Interaction with MAP kinases|||Phosphocysteine intermediate|||Reduced enzyme activity with MAPK14.|||Rhodanese|||Strongly reduced affinity for MAPK14. Almost abolishes enzyme activity with MAPK14.|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094813|||http://purl.uniprot.org/annotation/VSP_036549
http://togogenome.org/gene/9606:MXRA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84157|||http://purl.uniprot.org/uniprot/Q6ZR64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Matrix-remodeling-associated protein 7|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072586|||http://purl.uniprot.org/annotation/VSP_022589|||http://purl.uniprot.org/annotation/VSP_022590|||http://purl.uniprot.org/annotation/VSP_024252
http://togogenome.org/gene/9606:HOMER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSC5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases interaction with NFATC2.|||Decreases interaction with NFATC2. Decreases interaction with NFATC2; when associated with N-22. Decreases interaction with NFATC2; when associated with N-22 and S-43. Markedly decreases interaction with NFATC2; when associated with T-30; S-31 and S-43. Markedly decreases interaction with NFATC2; when associated with N-22; T-30 and S-31. Impairs interaction with NFATC2; when associated with N-22; T-30, S-31 and S-43.|||Disordered|||Does not affect interaction with NFATC2. Decreases interaction with NFATC2; when associated with 53-L--S-56. Decreases interaction with NFATC2; when associated with S-43 and 53-L--S-56. Markedly decreases interaction with NFATC2; when associated with T-30 and S-31 and 53-L--S-56. Impairs interaction with NFATC2; when associated with T-30; S-31; S-43 and 53-L--S-56.|||Does not affect interaction with NFATC2. Decreases interaction with NFATC2; when associated with N-22 and 53-L--S-56. Markedly decreases interaction with NFATC2; when associated with T-30; S-31 and 53-L--S-56. Impairs interaction with NFATC2; when associated with N-22; T-30; S-31 and 53-L--S-56.|||Does not affect interaction with NFATC2; when associated with A-36 and A-38. Attenuates inhibition by AKT; when associated with A-36 and A-38.|||Does not affect interaction with NFATC2; when associated with A-36 and A-52. Attenuates inhibition by AKT; when associated with A-36 and A-52.|||Does not affect interaction with NFATC2; when associated with A-38 and A-52. Attenuates inhibition by AKT; when associated with A-38 and A-52.|||Homer protein homolog 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Markedly decreases interaction with NFATC2; when associated with S-43 and 53-L--S-56. Markedly decreases interaction with NFATC2; when associated with N-22 and 53-L--S-56. Impairs interaction with NFATC2; when associated with N-22; S-43 and 53-L--S-56.|||Phosphoserine|||Required for interaction with NFATC2|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191011|||http://purl.uniprot.org/annotation/VAR_017410|||http://purl.uniprot.org/annotation/VSP_009073|||http://purl.uniprot.org/annotation/VSP_009074|||http://purl.uniprot.org/annotation/VSP_009075|||http://purl.uniprot.org/annotation/VSP_009076|||http://purl.uniprot.org/annotation/VSP_009077|||http://purl.uniprot.org/annotation/VSP_045715
http://togogenome.org/gene/9606:USP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94782                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by autolysis|||Disordered|||Loss of autolysis-mediated degradation upon UV irradiation. No effect on catalytic activity.|||Loss of catalytic activity including autolysis.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Strongly reduces interaction with WDR48 and activation by WDR48.|||USP|||Ubiquitin carboxyl-terminal hydrolase 1|||Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080615|||http://purl.uniprot.org/annotation/PRO_0000453162
http://togogenome.org/gene/9606:FTSJ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY81                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes RNA 2'-O-methyltransferase activity; when associated with A-117 and A-157.|||Abolishes RNA 2'-O-methyltransferase activity; when associated with A-31 and A-117.|||Abolishes RNA 2'-O-methyltransferase activity; when associated with A-31 and A-157.|||Acidic residues|||Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155577|||http://purl.uniprot.org/annotation/VAR_023284|||http://purl.uniprot.org/annotation/VAR_023285
http://togogenome.org/gene/9606:FAM163A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GL9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein FAM163A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280256
http://togogenome.org/gene/9606:JARID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92833                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARID|||Abolishes nucleosome binding activity of a minimal SUZ12-RBBP4-AEBP2-JARID2 PRC2 complex.|||Acidic residues|||Basic and acidic residues|||Disordered|||GSGFP motif|||In DIDDF; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||JmjC|||JmjN|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein Jumonji|||Sufficient for interaction with the PRC2 complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200591|||http://purl.uniprot.org/annotation/VAR_087870|||http://purl.uniprot.org/annotation/VAR_087871|||http://purl.uniprot.org/annotation/VSP_038756|||http://purl.uniprot.org/annotation/VSP_038757|||http://purl.uniprot.org/annotation/VSP_045041
http://togogenome.org/gene/9606:ERI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV48                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-5' exoribonuclease 1|||Disordered|||Does not inhibit RNA-binding to the stem-loop structure.|||Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-104.|||Does not inhibit RNA-binding to the stem-loop structure. Does not inhibit RNA-binding to the stem-loop structure, when associated with A-92.|||Exonuclease|||Inhibits 3'-end histone mRNA exonuclease activity.|||Inhibits RNA-binding to the stem-loop structure and 3'-end histone mRNA exonuclease activity.|||Inhibits RNA-binding to the stem-loop structure.|||Phosphoserine|||Proton acceptor|||Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-111.|||Reduces RNA-binding to the stem-loop structure but not 3'-end histone mRNA exonuclease activity; when associated with A-112.|||Reduces slightly RNA-binding to the stem-loop structure.|||Reduces slightly RNA-binding to the stem-loop structure; when associated with A-109.|||Reduces slightly RNA-binding to the stem-loop structure; when associated with A-110.|||Removed|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187007|||http://purl.uniprot.org/annotation/VAR_018107
http://togogenome.org/gene/9606:LCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Y8|||http://purl.uniprot.org/uniprot/E9PJ92|||http://purl.uniprot.org/uniprot/P06239                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mass|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Allows interaction with SQSTM1.|||Found in leukemia.|||In IMD22.|||In isoform 3.|||In isoform Short.|||In leukemia.|||Interaction with PTPRH|||Interactions with CD4 and CD8|||N-myristoyl glycine|||No effect on interaction with SQSTM1.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Tyrosine-protein kinase Lck                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088124|||http://purl.uniprot.org/annotation/VAR_013463|||http://purl.uniprot.org/annotation/VAR_013464|||http://purl.uniprot.org/annotation/VAR_013465|||http://purl.uniprot.org/annotation/VAR_013466|||http://purl.uniprot.org/annotation/VAR_051697|||http://purl.uniprot.org/annotation/VAR_071291|||http://purl.uniprot.org/annotation/VSP_005000|||http://purl.uniprot.org/annotation/VSP_005001|||http://purl.uniprot.org/annotation/VSP_016049
http://togogenome.org/gene/9606:TMEM63C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1W3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium permeable stress-gated cation channel 1|||Disordered|||Helical|||In SPG87.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280730|||http://purl.uniprot.org/annotation/VAR_031193|||http://purl.uniprot.org/annotation/VAR_087513
http://togogenome.org/gene/9606:ESRRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95718                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  6-fold decrease in DNA-binding affinity.|||Disordered|||Essential for ESRRB transcriptional activity and interaction with NCOA3|||Important for stabilizing DNA-binding|||In DFNB35.|||In DFNB35; uncertain pathological significance.|||In isoform 1.|||In isoform 2.|||Interaction with NANOG|||NR C4-type|||NR LBD|||Nuclear receptor|||Steroid hormone receptor ERR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053662|||http://purl.uniprot.org/annotation/VAR_043503|||http://purl.uniprot.org/annotation/VAR_043504|||http://purl.uniprot.org/annotation/VAR_043505|||http://purl.uniprot.org/annotation/VAR_043506|||http://purl.uniprot.org/annotation/VAR_043507|||http://purl.uniprot.org/annotation/VAR_043508|||http://purl.uniprot.org/annotation/VSP_058967|||http://purl.uniprot.org/annotation/VSP_058968
http://togogenome.org/gene/9606:ZNF253                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75346                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 253                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047486|||http://purl.uniprot.org/annotation/VSP_036962
http://togogenome.org/gene/9606:CCDC78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2IDD5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 78|||Disordered|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291841|||http://purl.uniprot.org/annotation/VAR_032867|||http://purl.uniprot.org/annotation/VSP_026252|||http://purl.uniprot.org/annotation/VSP_026253|||http://purl.uniprot.org/annotation/VSP_026254|||http://purl.uniprot.org/annotation/VSP_026255|||http://purl.uniprot.org/annotation/VSP_026256|||http://purl.uniprot.org/annotation/VSP_026257|||http://purl.uniprot.org/annotation/VSP_026258
http://togogenome.org/gene/9606:RAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60763                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In NEDBAF.|||O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230|||Ras-related C3 botulinum toxin substrate 3|||Reduced FBXL19-mediated ubiquitination and subsequent degradation.|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198889|||http://purl.uniprot.org/annotation/PRO_0000281240|||http://purl.uniprot.org/annotation/VAR_083040|||http://purl.uniprot.org/annotation/VAR_083041|||http://purl.uniprot.org/annotation/VAR_083042|||http://purl.uniprot.org/annotation/VAR_083245
http://togogenome.org/gene/9606:SLFNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU6|||http://purl.uniprot.org/uniprot/Q499Z3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Schlafen AlbA-2|||Schlafen-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282998|||http://purl.uniprot.org/annotation/VAR_031459|||http://purl.uniprot.org/annotation/VAR_031460|||http://purl.uniprot.org/annotation/VAR_031461|||http://purl.uniprot.org/annotation/VSP_024275|||http://purl.uniprot.org/annotation/VSP_024276|||http://purl.uniprot.org/annotation/VSP_024277|||http://purl.uniprot.org/annotation/VSP_024278
http://togogenome.org/gene/9606:LRATD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||LRAT|||Pro residues|||Protein LRATD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234348
http://togogenome.org/gene/9606:GARIN1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ3|||http://purl.uniprot.org/uniprot/B4DY15|||http://purl.uniprot.org/uniprot/Q96KD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 1B|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311691|||http://purl.uniprot.org/annotation/VAR_037271|||http://purl.uniprot.org/annotation/VAR_037272|||http://purl.uniprot.org/annotation/VSP_029580|||http://purl.uniprot.org/annotation/VSP_055270|||http://purl.uniprot.org/annotation/VSP_055271
http://togogenome.org/gene/9606:CMKLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99788                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chemerin-like receptor 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069307|||http://purl.uniprot.org/annotation/VSP_001985
http://togogenome.org/gene/9606:NDUFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43677                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020049
http://togogenome.org/gene/9606:AKR1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14550|||http://purl.uniprot.org/uniprot/V9HWI0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member A1|||Complete loss of enzymatic activity.|||Lowers pKa of active site Tyr|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NADP-dependent oxidoreductase|||No change in enzymatic activity.|||Phosphoserine|||Proton donor|||Reduced activity towards daunorubicin.|||Removed|||Strong decrease in enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124617|||http://purl.uniprot.org/annotation/VAR_048212|||http://purl.uniprot.org/annotation/VAR_058909
http://togogenome.org/gene/9606:LAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28838                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cytosol aminopeptidase|||In isoform 2.|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165825|||http://purl.uniprot.org/annotation/VSP_022631
http://togogenome.org/gene/9606:SNX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5X1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-287.|||Abolishes membrane tubulation activity. Abolishes binding to phosphatidylinositol 3-phosphate, but not to phosphatidylinositol 4,5-bisphosphate; when associated with A-313.|||Abolishes membrane tubulation activity; when associated with E-522.|||Abolishes membrane tubulation activity; when associated with E-528.|||BAR|||Critical for tubulation activity|||Disordered|||Loss of membrane binding.|||N6-acetyllysine|||PX|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3|||Sorting nexin-9|||Strongly reduced membrane binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213852
http://togogenome.org/gene/9606:CERCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4B2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Exhibits some galactosyltransferase activity; when associated with D-440; M-451; Q-452 and V-453 in a chimeric construct with COLGALT1.|||Exhibits some galactosyltransferase activity; when associated with D-440; R-450; M-451 and Q-452 in a chimeric construct with COLGALT1.|||Exhibits some galactosyltransferase activity; when associated with D-440; R-450; M-451 and V-453 in a chimeric construct with COLGALT1.|||Exhibits some galactosyltransferase activity; when associated with D-440; R-450; Q-452 and V-453 in a chimeric construct with COLGALT1.|||In isoform 2.|||Inactive glycosyltransferase 25 family member 3|||N-linked (GlcNAc...) asparagine|||No effect on lack of galactosyltransferase activity in a chimeric construct with COLGALT1. Exhibits some galactosyltransferase activity; when associated with R-450; M-451; Q-452 and V-453 in a chimeric construct with COLGALT1.|||Polar residues|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309544|||http://purl.uniprot.org/annotation/VSP_029234
http://togogenome.org/gene/9606:TMEM184B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y519                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Transmembrane protein 184B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211555
http://togogenome.org/gene/9606:KCND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSA2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||Interaction with KCNIP2|||Mediates dendritic targeting|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily D member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054061|||http://purl.uniprot.org/annotation/VSP_057040
http://togogenome.org/gene/9606:HES6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Orange|||Transcription cofactor HES-6|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127214|||http://purl.uniprot.org/annotation/VAR_019540|||http://purl.uniprot.org/annotation/VSP_011152|||http://purl.uniprot.org/annotation/VSP_040128|||http://purl.uniprot.org/annotation/VSP_055615|||http://purl.uniprot.org/annotation/VSP_055616
http://togogenome.org/gene/9606:PLEKHF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWN9|||http://purl.uniprot.org/uniprot/Q96S99                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||PH|||Pleckstrin homology domain-containing family F member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251597
http://togogenome.org/gene/9606:LRRC46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 46|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223919
http://togogenome.org/gene/9606:MMP28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV06|||http://purl.uniprot.org/uniprot/C0H5X0|||http://purl.uniprot.org/uniprot/Q9H239                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In isoform 2.|||Matrix metalloproteinase-28|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028857|||http://purl.uniprot.org/annotation/PRO_0000028858|||http://purl.uniprot.org/annotation/PRO_5014085060|||http://purl.uniprot.org/annotation/PRO_5014301620|||http://purl.uniprot.org/annotation/VSP_040552|||http://purl.uniprot.org/annotation/VSP_040553
http://togogenome.org/gene/9606:BAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6LPK7|||http://purl.uniprot.org/uniprot/Q07812|||http://purl.uniprot.org/uniprot/Q5ZPJ0|||http://purl.uniprot.org/uniprot/Q5ZPJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Apoptosis regulator BAX|||BH1|||BH2|||BH3|||Bcl-2 Bcl-2 homology region 1-3|||Constitutive cytoplasmic location.|||Constitutive mitochondrial location. Enhanced fiber formation with humanin.|||Disordered|||Enhanced fiber formation with humanin.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In a Burkitt lymphoma; loss of homodimerization.|||In a T-cell acute lymphoblastic leukemia cell line; loss of heterodimerization with Bcl-2 or Bcl-X(L).|||In a plasmacytoma cell line.|||In isoform Beta.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma.|||In isoform Psi.|||In isoform Sigma.|||In isoform Zeta.|||N-acetylmethionine|||No loss of polyubiquitination.|||Partial loss of polyubiquitination.|||Pro residues|||Reduces interaction with BCL2L11, homooligomerization and triggering of apoptosis.|||Strongly reduced interaction with MCL1, BCL2, BCL2L1 and BCL2L2. No effect on cytochrome c release and subsequent apoptosis triggered by etoposide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143053|||http://purl.uniprot.org/annotation/VAR_007809|||http://purl.uniprot.org/annotation/VAR_013575|||http://purl.uniprot.org/annotation/VAR_013576|||http://purl.uniprot.org/annotation/VAR_047053|||http://purl.uniprot.org/annotation/VSP_031234|||http://purl.uniprot.org/annotation/VSP_031235|||http://purl.uniprot.org/annotation/VSP_031236|||http://purl.uniprot.org/annotation/VSP_031237|||http://purl.uniprot.org/annotation/VSP_031238|||http://purl.uniprot.org/annotation/VSP_031239|||http://purl.uniprot.org/annotation/VSP_031240|||http://purl.uniprot.org/annotation/VSP_037475
http://togogenome.org/gene/9606:LAMTOR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHA4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In M5 mutant; impaired association with Rag GTPases.|||In isoform 2.|||Ragulator complex protein LAMTOR3|||Required for interaction with LAMTOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221005|||http://purl.uniprot.org/annotation/VSP_046372
http://togogenome.org/gene/9606:OLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTK5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of ATP-binding.|||N6-acetyllysine|||Nuclear export signal|||OBG-type G|||Obg-like ATPase 1|||Retention of ATP-binding specificity.|||TGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122456|||http://purl.uniprot.org/annotation/VAR_036613|||http://purl.uniprot.org/annotation/VSP_002049|||http://purl.uniprot.org/annotation/VSP_002050|||http://purl.uniprot.org/annotation/VSP_002051
http://togogenome.org/gene/9606:SLC30A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWU4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased transport reaction kinetics; decreased affinity for zinc ions; decreased zinc ion import into organelle; no effect on protein abundance.|||Decreased zinc ion transmembrane transport.|||Decreased zinc ion transmembrane transport; when associated with A-106.|||Decreased zinc ion transmembrane transport; when associated with A-137.|||Decreased zinc ion transmembrane transport; when associated with A-220.|||Decreased zinc ion transmembrane transport; when associated with A-345.|||Disordered|||HCH Motif; seals regulatory zinc-binding pocket|||Helical|||In isoform 2.|||Loss of transported zinc binding and decreased zinc ion transmembrane transport; when associated with N-110.|||Loss of transported zinc binding and decreased zinc ion transmembrane transport; when associated with N-224.|||Lumenal, vesicle|||Proton-coupled zinc antiporter SLC30A8|||in chain A|||in chain B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281740|||http://purl.uniprot.org/annotation/VAR_031258|||http://purl.uniprot.org/annotation/VAR_031259|||http://purl.uniprot.org/annotation/VSP_024025
http://togogenome.org/gene/9606:SLC7A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82251                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes amino acid transport activity.|||Basic and acidic residues|||Complete loss of amino acid transport activity.|||Cytoplasmic|||Decreased amino acid transport activity.|||Disordered|||Does not affect amino acid transport activity.|||Extracellular|||Helical|||In CSNU.|||In CSNU; complete loss of amino acid transport activity.|||In CSNU; decreased amino acid transport activity.|||In CSNU; impairs protein stability and dimer formation.|||In CSNU; non-classic type I.|||In CSNU; partial loss of amino acid transport activity.|||In CSNU; severe loss of amino acid transport activity.|||In CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane.|||In CSNU; type I.|||In CSNU; type III.|||In CSNU; type III; decreased amino acid transport activity.|||In CSNU; type III; impairs protein stability and dimer formation.|||In CSNU; type III; partial loss of amino acid transport activity.|||In CSNU; type III; severe loss of amino acid transport activity.|||In CSNU; types I and III.|||In CSNU; unknown pathological significance.|||Interchain (with C-114 in SLC3A1)|||Loss of amino acid transport activity.|||Markedly reduces amino acid transport activity.|||No effect on amino acid transport activity.|||Phosphoserine|||Reduces amino acid transport activity.|||Slightly decreased amino acid transport activity.|||b(0,+)-type amino acid transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054258|||http://purl.uniprot.org/annotation/VAR_010256|||http://purl.uniprot.org/annotation/VAR_010257|||http://purl.uniprot.org/annotation/VAR_010258|||http://purl.uniprot.org/annotation/VAR_010259|||http://purl.uniprot.org/annotation/VAR_010260|||http://purl.uniprot.org/annotation/VAR_014363|||http://purl.uniprot.org/annotation/VAR_014364|||http://purl.uniprot.org/annotation/VAR_014365|||http://purl.uniprot.org/annotation/VAR_015885|||http://purl.uniprot.org/annotation/VAR_018997|||http://purl.uniprot.org/annotation/VAR_018998|||http://purl.uniprot.org/annotation/VAR_018999|||http://purl.uniprot.org/annotation/VAR_019000|||http://purl.uniprot.org/annotation/VAR_019001|||http://purl.uniprot.org/annotation/VAR_019002|||http://purl.uniprot.org/annotation/VAR_019003|||http://purl.uniprot.org/annotation/VAR_019004|||http://purl.uniprot.org/annotation/VAR_019005|||http://purl.uniprot.org/annotation/VAR_019006|||http://purl.uniprot.org/annotation/VAR_019007|||http://purl.uniprot.org/annotation/VAR_019008|||http://purl.uniprot.org/annotation/VAR_019009|||http://purl.uniprot.org/annotation/VAR_019010|||http://purl.uniprot.org/annotation/VAR_019011|||http://purl.uniprot.org/annotation/VAR_019012|||http://purl.uniprot.org/annotation/VAR_019013|||http://purl.uniprot.org/annotation/VAR_022603|||http://purl.uniprot.org/annotation/VAR_022604|||http://purl.uniprot.org/annotation/VAR_048153|||http://purl.uniprot.org/annotation/VAR_072308|||http://purl.uniprot.org/annotation/VAR_072309|||http://purl.uniprot.org/annotation/VAR_072310|||http://purl.uniprot.org/annotation/VAR_072311|||http://purl.uniprot.org/annotation/VAR_072312|||http://purl.uniprot.org/annotation/VAR_072313|||http://purl.uniprot.org/annotation/VAR_072314|||http://purl.uniprot.org/annotation/VAR_072315|||http://purl.uniprot.org/annotation/VAR_072316|||http://purl.uniprot.org/annotation/VAR_072317|||http://purl.uniprot.org/annotation/VAR_072318|||http://purl.uniprot.org/annotation/VAR_072319|||http://purl.uniprot.org/annotation/VAR_072320|||http://purl.uniprot.org/annotation/VAR_072321|||http://purl.uniprot.org/annotation/VAR_072322|||http://purl.uniprot.org/annotation/VAR_072323|||http://purl.uniprot.org/annotation/VAR_072324|||http://purl.uniprot.org/annotation/VAR_072325|||http://purl.uniprot.org/annotation/VAR_072326|||http://purl.uniprot.org/annotation/VAR_072327
http://togogenome.org/gene/9606:ISG20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YMM4|||http://purl.uniprot.org/uniprot/Q96AZ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exonuclease|||In isoform 2.|||Interferon-stimulated gene 20 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084243|||http://purl.uniprot.org/annotation/VSP_012429|||http://purl.uniprot.org/annotation/VSP_012430
http://togogenome.org/gene/9606:ENPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EUF1|||http://purl.uniprot.org/uniprot/Q13822                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 2|||Essential for catalytic activity|||In isoform 2.|||In isoform 3.|||Loss of ability to hydrolyze sphingosylphosphorylcholine.|||Loss of lysophospholipase activity and ability to hydrolyze sphingosylphosphorylcholine.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Reduces lysophospholipase activity by about 50%.|||Reduces lysophospholipase activity by about 70%.|||Removed by furin|||Required for secretion|||SMB|||SMB 1|||SMB 2|||Strongly reduced lysophospholipase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188567|||http://purl.uniprot.org/annotation/PRO_0000281649|||http://purl.uniprot.org/annotation/VAR_057472|||http://purl.uniprot.org/annotation/VAR_057473|||http://purl.uniprot.org/annotation/VAR_060469|||http://purl.uniprot.org/annotation/VSP_006750|||http://purl.uniprot.org/annotation/VSP_036398
http://togogenome.org/gene/9606:STK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94804                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation segment|||Basic and acidic residues|||Disordered|||In TGCT; somatic mutation.|||Loss of kinase activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086697|||http://purl.uniprot.org/annotation/VAR_023827|||http://purl.uniprot.org/annotation/VAR_041131|||http://purl.uniprot.org/annotation/VAR_041132|||http://purl.uniprot.org/annotation/VAR_041133|||http://purl.uniprot.org/annotation/VAR_041134|||http://purl.uniprot.org/annotation/VAR_041135|||http://purl.uniprot.org/annotation/VAR_041136|||http://purl.uniprot.org/annotation/VAR_041137|||http://purl.uniprot.org/annotation/VAR_041138|||http://purl.uniprot.org/annotation/VAR_051671|||http://purl.uniprot.org/annotation/VAR_051672|||http://purl.uniprot.org/annotation/VAR_051673
http://togogenome.org/gene/9606:CFAP74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HLA9|||http://purl.uniprot.org/uniprot/Q9C0B2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 74|||Disordered|||In CILD49; unknown pathological significance.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324664|||http://purl.uniprot.org/annotation/VAR_039873|||http://purl.uniprot.org/annotation/VAR_039874|||http://purl.uniprot.org/annotation/VAR_039875|||http://purl.uniprot.org/annotation/VAR_088022|||http://purl.uniprot.org/annotation/VAR_088023|||http://purl.uniprot.org/annotation/VAR_088024|||http://purl.uniprot.org/annotation/VAR_088025|||http://purl.uniprot.org/annotation/VSP_032345|||http://purl.uniprot.org/annotation/VSP_057369|||http://purl.uniprot.org/annotation/VSP_057370
http://togogenome.org/gene/9606:PRSS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35030|||http://purl.uniprot.org/uniprot/Q7Z5F4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of catalytic activity.|||Peptidase S1|||Required for specificity|||Sulfotyrosine|||Trypsin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028201|||http://purl.uniprot.org/annotation/PRO_0000028202|||http://purl.uniprot.org/annotation/VAR_046794|||http://purl.uniprot.org/annotation/VAR_046795|||http://purl.uniprot.org/annotation/VAR_059788|||http://purl.uniprot.org/annotation/VAR_067459|||http://purl.uniprot.org/annotation/VSP_005409|||http://purl.uniprot.org/annotation/VSP_005410|||http://purl.uniprot.org/annotation/VSP_042074|||http://purl.uniprot.org/annotation/VSP_053779
http://togogenome.org/gene/9606:ROBO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In HGPPS1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Roundabout homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031038|||http://purl.uniprot.org/annotation/VAR_019073|||http://purl.uniprot.org/annotation/VAR_019074|||http://purl.uniprot.org/annotation/VAR_019075|||http://purl.uniprot.org/annotation/VAR_019119|||http://purl.uniprot.org/annotation/VAR_019120|||http://purl.uniprot.org/annotation/VAR_019121|||http://purl.uniprot.org/annotation/VAR_034474|||http://purl.uniprot.org/annotation/VAR_034475|||http://purl.uniprot.org/annotation/VAR_053642|||http://purl.uniprot.org/annotation/VAR_062145|||http://purl.uniprot.org/annotation/VSP_010650|||http://purl.uniprot.org/annotation/VSP_010651
http://togogenome.org/gene/9606:VSX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZR4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CVC|||Disordered|||Homeobox|||In CAASDS.|||In KTCN1.|||In KTCN1; sporadic.|||In KTCN1; unknown pathological significance.|||In KTCN1; unknown pathological significance; also in a patient with retinal dysfunction.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Nuclear localization signal|||Octapeptide motif|||Polar residues|||Visual system homeobox 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049355|||http://purl.uniprot.org/annotation/VAR_014243|||http://purl.uniprot.org/annotation/VAR_014244|||http://purl.uniprot.org/annotation/VAR_014245|||http://purl.uniprot.org/annotation/VAR_014246|||http://purl.uniprot.org/annotation/VAR_014247|||http://purl.uniprot.org/annotation/VAR_014248|||http://purl.uniprot.org/annotation/VAR_063100|||http://purl.uniprot.org/annotation/VAR_066670|||http://purl.uniprot.org/annotation/VAR_066671|||http://purl.uniprot.org/annotation/VAR_066672|||http://purl.uniprot.org/annotation/VAR_076692|||http://purl.uniprot.org/annotation/VSP_002299|||http://purl.uniprot.org/annotation/VSP_002300|||http://purl.uniprot.org/annotation/VSP_002301|||http://purl.uniprot.org/annotation/VSP_002302|||http://purl.uniprot.org/annotation/VSP_002303|||http://purl.uniprot.org/annotation/VSP_039140|||http://purl.uniprot.org/annotation/VSP_039141|||http://purl.uniprot.org/annotation/VSP_039142|||http://purl.uniprot.org/annotation/VSP_039143|||http://purl.uniprot.org/annotation/VSP_039144|||http://purl.uniprot.org/annotation/VSP_039145|||http://purl.uniprot.org/annotation/VSP_039146|||http://purl.uniprot.org/annotation/VSP_039147
http://togogenome.org/gene/9606:CLDN20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA2|||http://purl.uniprot.org/uniprot/P56880                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin|||Claudin-20|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144784|||http://purl.uniprot.org/annotation/PRO_5014247035
http://togogenome.org/gene/9606:AAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JEH3|||http://purl.uniprot.org/uniprot/Q13685                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Angio-associated migratory cell protein|||Disordered|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050832|||http://purl.uniprot.org/annotation/VAR_037061
http://togogenome.org/gene/9606:WDR45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y484                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased interaction with ATG2A. Loss of interaction with ATG2A; when associated with A-15.|||Decreased interaction with ATG2A. Loss of interaction with ATG2A; when associated with A-17.|||In NBIA5.|||In NBIA5; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||L/FRRG motif|||Loss of interaction with AMPK. No effect on interaction with ATG2A.|||No effect on interaction with ATG2A.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat domain phosphoinositide-interacting protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051452|||http://purl.uniprot.org/annotation/VAR_078645|||http://purl.uniprot.org/annotation/VAR_080430|||http://purl.uniprot.org/annotation/VSP_016975|||http://purl.uniprot.org/annotation/VSP_016976
http://togogenome.org/gene/9606:ZNF697                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TEC3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 697                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305138|||http://purl.uniprot.org/annotation/VAR_078436
http://togogenome.org/gene/9606:NUTM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NUT family member 2B|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337992|||http://purl.uniprot.org/annotation/VSP_034025|||http://purl.uniprot.org/annotation/VSP_034026|||http://purl.uniprot.org/annotation/VSP_034027
http://togogenome.org/gene/9606:KIAA0232                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YKK5|||http://purl.uniprot.org/uniprot/Q92628                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA0232                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050738
http://togogenome.org/gene/9606:MTSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM41|||http://purl.uniprot.org/uniprot/O43312                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IMD|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein MTSS 1|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096639|||http://purl.uniprot.org/annotation/VAR_054010|||http://purl.uniprot.org/annotation/VAR_054011|||http://purl.uniprot.org/annotation/VSP_007420|||http://purl.uniprot.org/annotation/VSP_007421|||http://purl.uniprot.org/annotation/VSP_016216|||http://purl.uniprot.org/annotation/VSP_054702
http://togogenome.org/gene/9606:TMEM235                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFC5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 235                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000406902|||http://purl.uniprot.org/annotation/VSP_040887|||http://purl.uniprot.org/annotation/VSP_040888
http://togogenome.org/gene/9606:DCHS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRC0|||http://purl.uniprot.org/uniprot/Q6V1P8|||http://purl.uniprot.org/uniprot/Q6V1P9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin-23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343410|||http://purl.uniprot.org/annotation/VSP_060650|||http://purl.uniprot.org/annotation/VSP_060651
http://togogenome.org/gene/9606:OR1G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW57|||http://purl.uniprot.org/uniprot/P47890                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150434|||http://purl.uniprot.org/annotation/VAR_053122
http://togogenome.org/gene/9606:POMZP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJE2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||POM121 and ZP3 fusion protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204909|||http://purl.uniprot.org/annotation/VAR_056721|||http://purl.uniprot.org/annotation/VSP_046257
http://togogenome.org/gene/9606:POMC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01189                                                                                  ^@                                                                                  Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Beta-endorphin|||Corticotropin|||Corticotropin-like intermediary peptide|||Disordered|||Glutamic acid 1-amide|||Lipotropin beta|||Lipotropin gamma|||May confer susceptibility to obesity; reduces the ability to activate melanocortin receptor 4.|||Melanocyte-stimulating hormone alpha|||Melanocyte-stimulating hormone beta|||Melanotropin gamma|||Met-enkephalin|||N-acetylserine; in Corticotropin|||N-linked (GlcNAc...) asparagine|||NPP|||O-linked (HexNAc...) threonine|||Phenylalanine amide|||Phosphoserine|||Potential peptide|||Valine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024966|||http://purl.uniprot.org/annotation/PRO_0000024967|||http://purl.uniprot.org/annotation/PRO_0000024968|||http://purl.uniprot.org/annotation/PRO_0000024969|||http://purl.uniprot.org/annotation/PRO_0000024970|||http://purl.uniprot.org/annotation/PRO_0000024971|||http://purl.uniprot.org/annotation/PRO_0000024972|||http://purl.uniprot.org/annotation/PRO_0000024973|||http://purl.uniprot.org/annotation/PRO_0000024974|||http://purl.uniprot.org/annotation/PRO_0000024975|||http://purl.uniprot.org/annotation/PRO_0000024976|||http://purl.uniprot.org/annotation/VAR_010699|||http://purl.uniprot.org/annotation/VAR_010700|||http://purl.uniprot.org/annotation/VAR_010701|||http://purl.uniprot.org/annotation/VAR_010714|||http://purl.uniprot.org/annotation/VAR_010715|||http://purl.uniprot.org/annotation/VAR_010716|||http://purl.uniprot.org/annotation/VAR_012201|||http://purl.uniprot.org/annotation/VAR_029314|||http://purl.uniprot.org/annotation/VAR_029762
http://togogenome.org/gene/9606:TBC1D24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULP9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In DEE16.|||In DEE16; loss of function mutation; impairs the interaction with ARF6; overexpression of the mutant protein in primary cortical neurons abolishes the ability to increase neurite length and arborization.|||In DFNA65.|||In DFNB86.|||In DOORS.|||In DOORS; unknown pathological significance.|||In EPRPDC.|||In EPRPDC; results in synaptic vesicle trafficking defects when expressed in a heterologous system; does not affect localization to presynapse when expressed in a heterologous system.|||In EPRPDC; unknown pathological significance.|||In FIME; does not affect the interaction with ARF6; fails to induce neurite overgrowth when overexpressed in primary cortical neurons.|||In FIME; fails to induce neurite overgrowth when overexpressed in primary cortical neurons.|||In FIME; significantly impairs the interaction with ARF6; partially induces neurite overgrowth when overexpressed in primary cortical neurons.|||In isoform 2.|||Phosphoserine|||Rab-GAP TBC|||TBC1 domain family member 24|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288504|||http://purl.uniprot.org/annotation/VAR_064365|||http://purl.uniprot.org/annotation/VAR_064366|||http://purl.uniprot.org/annotation/VAR_064367|||http://purl.uniprot.org/annotation/VAR_070102|||http://purl.uniprot.org/annotation/VAR_070890|||http://purl.uniprot.org/annotation/VAR_070912|||http://purl.uniprot.org/annotation/VAR_070913|||http://purl.uniprot.org/annotation/VAR_070914|||http://purl.uniprot.org/annotation/VAR_070915|||http://purl.uniprot.org/annotation/VAR_070916|||http://purl.uniprot.org/annotation/VAR_070994|||http://purl.uniprot.org/annotation/VAR_070995|||http://purl.uniprot.org/annotation/VAR_072107|||http://purl.uniprot.org/annotation/VAR_078184|||http://purl.uniprot.org/annotation/VAR_078185|||http://purl.uniprot.org/annotation/VAR_083253|||http://purl.uniprot.org/annotation/VAR_083254|||http://purl.uniprot.org/annotation/VAR_083255|||http://purl.uniprot.org/annotation/VAR_083256|||http://purl.uniprot.org/annotation/VAR_083257|||http://purl.uniprot.org/annotation/VAR_083258|||http://purl.uniprot.org/annotation/VSP_025701
http://togogenome.org/gene/9606:UMAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J7I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||UBAP1-MVB12-associated (UMA)-domain containing protein 1|||UMA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431388
http://togogenome.org/gene/9606:ARL14EPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKL9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  ARL14 effector protein-like|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419646
http://togogenome.org/gene/9606:NFIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12857                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear factor 1 A-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100191|||http://purl.uniprot.org/annotation/VSP_036620|||http://purl.uniprot.org/annotation/VSP_046883|||http://purl.uniprot.org/annotation/VSP_046884
http://togogenome.org/gene/9606:MACROD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ69                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Site|||Strand                                                                                  ^@                                                                                  ADP-ribose glycohydrolase MACROD1|||Breakpoint for translocation to form RUNX1-MACROD1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of enzyme activity.|||Macro|||N6-acetyllysine|||N6-succinyllysine|||No significant effect on enzyme activity.|||Reduced enzyme activity.|||Reduced enzyme activity. No significant effect on affinity for substrate.|||Slightly reduced ADP-ribosyl hydrolase activity; when associated with A-174. Reduces O-acetyl-ADP-ribose deacetylase activity by 93%; when associated with A-174. No significant effect on affinity for substrate.|||Slightly reduced ADP-ribosyl hydrolase activity; when associated with A-184. Reduces O-acetyl-ADP-ribose deacetylase activity by 93%; when associated with A-184. No significant effect on affinity for substrate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084485
http://togogenome.org/gene/9606:CA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00918|||http://purl.uniprot.org/uniprot/V9HW21                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with Q-67.|||2-fold decrease in enzyme efficiency, as determined by kcat/KM ratio, and efficiently inhibited by chlorzolamide; when associated with S-65.|||Alpha-carbonic anhydrase|||Carbonic anhydrase 2|||Enhanced activity.|||Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity.|||Enhanced proton transfer; when associated with A-64.|||Fine-tunes the proton-transfer properties of H-64|||Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine|||Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64.|||Impaired activity, not rescued by 4-methylimidazole (4-MI).|||Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64.|||Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5.|||Impaired activity.|||In Jogjakarta.|||In Melbourne.|||In OPTB3.|||In OPTB3; complete loss of activity.|||In OPTB3; in Czechoslovakia.|||In OPTB3; partial loss of activity.|||Involved in the binding of some activators, including histamine and L-histidine|||N-acetylserine|||Normal CO(2) hydrase activity, but impaired stability.|||Normal CO(2) hydrase activity.|||Normal activity.|||Phosphoserine|||Proton donor/acceptor|||Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99.|||Reduced CO(2) hydrase activity.|||Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities.|||Reduced activity.|||Reduced proton transfer rate.|||Reduced proton transfer; when associated with A-64.|||Removed|||Strongly impaired activity.|||Strongly reduced CO(2) hydrase activity.|||Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding.|||Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities.|||Strongly reduced activity and sulfonamide affinity.|||Strongly reduced activity, but enhanced zinc affinity.|||Strongly reduced activity.|||Weakly impaired activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077418|||http://purl.uniprot.org/annotation/VAR_001380|||http://purl.uniprot.org/annotation/VAR_001381|||http://purl.uniprot.org/annotation/VAR_001382|||http://purl.uniprot.org/annotation/VAR_001383|||http://purl.uniprot.org/annotation/VAR_001384|||http://purl.uniprot.org/annotation/VAR_021009|||http://purl.uniprot.org/annotation/VAR_021010
http://togogenome.org/gene/9606:GLB1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW92                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-galactosidase-1-like protein 2|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317513
http://togogenome.org/gene/9606:TPBG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13641                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Impaired trafficking to the cell surface.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduces Wnt inhibitory function.|||Strongly reduces Wnt inhibitory function.|||Trophoblast glycoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019591
http://togogenome.org/gene/9606:KEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A077QP03|||http://purl.uniprot.org/uniprot/P23276                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In KEL1/K antigen.|||In KEL10/Ul(a) antigen.|||In KEL12 antigen.|||In KEL17 antigen.|||In KEL19 antigen.|||In KEL21/Kp(c) antigen.|||In KEL22 antigen.|||In KEL23 antigen.|||In KEL24 antigen.|||In KEL25 antigen.|||In KEL26 antigen.|||In KEL27 antigen.|||In KEL3/Kp(a) antigen.|||In KEL6/Js(a) antigen.|||Interchain (with C-347 in XK)|||Kell blood group glycoprotein|||Loss of Kell-XK complex.|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; in KEL2 antigen|||No loss of Kell-XK complex.|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078227|||http://purl.uniprot.org/annotation/VAR_006731|||http://purl.uniprot.org/annotation/VAR_006732|||http://purl.uniprot.org/annotation/VAR_006733|||http://purl.uniprot.org/annotation/VAR_006734|||http://purl.uniprot.org/annotation/VAR_006735|||http://purl.uniprot.org/annotation/VAR_006736|||http://purl.uniprot.org/annotation/VAR_006737|||http://purl.uniprot.org/annotation/VAR_015120|||http://purl.uniprot.org/annotation/VAR_015121|||http://purl.uniprot.org/annotation/VAR_015122|||http://purl.uniprot.org/annotation/VAR_015123|||http://purl.uniprot.org/annotation/VAR_015124|||http://purl.uniprot.org/annotation/VAR_015125|||http://purl.uniprot.org/annotation/VAR_015126|||http://purl.uniprot.org/annotation/VAR_016265|||http://purl.uniprot.org/annotation/VAR_016266
http://togogenome.org/gene/9606:SLC37A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0S7|||http://purl.uniprot.org/uniprot/B4DUH2|||http://purl.uniprot.org/uniprot/O43826                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Glucose-6-phosphate exchanger SLC37A4|||Helical|||In CDG2W; affects the endoplasmic reticulum subcellular location, relocalizing the protein either to the Golgi apparatus, or to a distinct, non-Golgi compartment, possibly endoplasmic reticulum exit sites; when transfected into HepG2 cells, significantly changes the protein glycosylation pattern, such as that of transferrin; does not affect glucose-6-phosphate transport activity.|||In GSD1B.|||In GSD1B; inactive glucose-6-phosphate transport.|||In GSD1C.|||In isoform 2.|||Major facilitator superfamily (MFS) profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199891|||http://purl.uniprot.org/annotation/VAR_003184|||http://purl.uniprot.org/annotation/VAR_003185|||http://purl.uniprot.org/annotation/VAR_007850|||http://purl.uniprot.org/annotation/VAR_012356|||http://purl.uniprot.org/annotation/VAR_016840|||http://purl.uniprot.org/annotation/VAR_025581|||http://purl.uniprot.org/annotation/VAR_025582|||http://purl.uniprot.org/annotation/VAR_025583|||http://purl.uniprot.org/annotation/VAR_025584|||http://purl.uniprot.org/annotation/VAR_025585|||http://purl.uniprot.org/annotation/VAR_025586|||http://purl.uniprot.org/annotation/VAR_025587|||http://purl.uniprot.org/annotation/VAR_025588|||http://purl.uniprot.org/annotation/VAR_025589|||http://purl.uniprot.org/annotation/VAR_025590|||http://purl.uniprot.org/annotation/VAR_025591|||http://purl.uniprot.org/annotation/VAR_025592|||http://purl.uniprot.org/annotation/VAR_025593|||http://purl.uniprot.org/annotation/VAR_025594|||http://purl.uniprot.org/annotation/VAR_025595|||http://purl.uniprot.org/annotation/VAR_025596|||http://purl.uniprot.org/annotation/VAR_025597|||http://purl.uniprot.org/annotation/VAR_025598|||http://purl.uniprot.org/annotation/VAR_025599|||http://purl.uniprot.org/annotation/VAR_025600|||http://purl.uniprot.org/annotation/VAR_025601|||http://purl.uniprot.org/annotation/VAR_025602|||http://purl.uniprot.org/annotation/VAR_025603|||http://purl.uniprot.org/annotation/VAR_025604|||http://purl.uniprot.org/annotation/VAR_032113|||http://purl.uniprot.org/annotation/VAR_066394|||http://purl.uniprot.org/annotation/VAR_066395|||http://purl.uniprot.org/annotation/VAR_066396|||http://purl.uniprot.org/annotation/VAR_066397|||http://purl.uniprot.org/annotation/VAR_086301|||http://purl.uniprot.org/annotation/VSP_006171
http://togogenome.org/gene/9606:PLS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPW9|||http://purl.uniprot.org/uniprot/P13797                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding 1|||Actin-binding 2|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Calponin-homology (CH) 3|||Calponin-homology (CH) 4|||EF-hand|||EF-hand 1|||EF-hand 2|||In OSTEOP; associated with disease susceptibility.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Plastin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073747|||http://purl.uniprot.org/annotation/VAR_035462|||http://purl.uniprot.org/annotation/VAR_070278|||http://purl.uniprot.org/annotation/VSP_056235|||http://purl.uniprot.org/annotation/VSP_056236|||http://purl.uniprot.org/annotation/VSP_056237
http://togogenome.org/gene/9606:TMEM174                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUU8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 174                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282577|||http://purl.uniprot.org/annotation/VSP_024210
http://togogenome.org/gene/9606:SDHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21912                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||4Fe-4S ferredoxin-type|||Found in a patient with a Cowden-like phenotype; unknown pathological significance; associated with increased manganese superoxide dismutase expression and normal levels of reactive oxygen species; associated with a 1.2-fold increase in AKT expression and 1.3-fold change in MAPK expression.|||Found in a patient with a Cowden-like phenotype; unknown pathological significance; associated with increased manganese superoxide dismutase function and increased levels of reactive oxygen species; associated with a 2.7-fold change in AKT expression and a 1.7-fold increase in MAPK expression.|||In MC2DN4.|||In MC2DN4; decreased succinate dehydrogenase (ubiquinone) activity in homozygous patient cells; decreased protein levels in homozygous patient cells.|||In MC2DN4; decreased succinate dehydrogenase (ubiquinone) activity; decreased protein levels in homozygous patient cells.|||In MC2DN4; unknown pathological significance.|||In PCC and PGL4.|||In PCC.|||In PCC; absence of expression in tumor cells indicating complete loss of SDHB function.|||In PGL4 and PCC.|||In PGL4.|||Interaction with SDHAF1|||Mitochondrion|||N6-acetyllysine|||Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010355|||http://purl.uniprot.org/annotation/VAR_017868|||http://purl.uniprot.org/annotation/VAR_017869|||http://purl.uniprot.org/annotation/VAR_018517|||http://purl.uniprot.org/annotation/VAR_018518|||http://purl.uniprot.org/annotation/VAR_035063|||http://purl.uniprot.org/annotation/VAR_035064|||http://purl.uniprot.org/annotation/VAR_035065|||http://purl.uniprot.org/annotation/VAR_035066|||http://purl.uniprot.org/annotation/VAR_035067|||http://purl.uniprot.org/annotation/VAR_037620|||http://purl.uniprot.org/annotation/VAR_037621|||http://purl.uniprot.org/annotation/VAR_054374|||http://purl.uniprot.org/annotation/VAR_054375|||http://purl.uniprot.org/annotation/VAR_054376|||http://purl.uniprot.org/annotation/VAR_054377|||http://purl.uniprot.org/annotation/VAR_054378|||http://purl.uniprot.org/annotation/VAR_054379|||http://purl.uniprot.org/annotation/VAR_054380|||http://purl.uniprot.org/annotation/VAR_054381|||http://purl.uniprot.org/annotation/VAR_054382|||http://purl.uniprot.org/annotation/VAR_054383|||http://purl.uniprot.org/annotation/VAR_085398|||http://purl.uniprot.org/annotation/VAR_085399|||http://purl.uniprot.org/annotation/VAR_085400|||http://purl.uniprot.org/annotation/VAR_085401|||http://purl.uniprot.org/annotation/VAR_085402
http://togogenome.org/gene/9606:C2CD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y426                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C2|||C2 domain-containing protein 2|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||SMP-LBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045386|||http://purl.uniprot.org/annotation/VAR_050928|||http://purl.uniprot.org/annotation/VAR_050929|||http://purl.uniprot.org/annotation/VSP_041071|||http://purl.uniprot.org/annotation/VSP_041072
http://togogenome.org/gene/9606:EPHB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54753                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Eph LBD|||Ephrin type-B receptor 3|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||Kinase-dead. Loss of autophosphorylation.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Partial loss of phosphorylation and loss of interaction with SH2-containing proteins.|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016831|||http://purl.uniprot.org/annotation/VAR_042176|||http://purl.uniprot.org/annotation/VAR_042177|||http://purl.uniprot.org/annotation/VAR_042178|||http://purl.uniprot.org/annotation/VAR_042179|||http://purl.uniprot.org/annotation/VAR_042180
http://togogenome.org/gene/9606:PYROXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MFM8; also found in a patient with limb-girdle muscular dystrophy; decreased function in cellular response to oxidative stress; no effect on subcellular location in the nucleus and sarcomere. Overexpression in C2C12 cells leads to reduced cell proliferation, migration and differentiation..|||In MFM8; decreased function in cellular response to oxidative stress; no effect on subcellular location at nucleus and sarcomere.|||In isoform 2.|||N-acetylmethionine|||Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327419|||http://purl.uniprot.org/annotation/VAR_077902|||http://purl.uniprot.org/annotation/VAR_077903|||http://purl.uniprot.org/annotation/VSP_055828
http://togogenome.org/gene/9606:DNAI7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E376|||http://purl.uniprot.org/uniprot/Q6TDU7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CASC1 C-terminal|||Dynein axonemal intermediate chain 7|||IC97/Casc1 N-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332731|||http://purl.uniprot.org/annotation/VAR_043008|||http://purl.uniprot.org/annotation/VAR_062232|||http://purl.uniprot.org/annotation/VSP_033380|||http://purl.uniprot.org/annotation/VSP_033381|||http://purl.uniprot.org/annotation/VSP_033382|||http://purl.uniprot.org/annotation/VSP_033383|||http://purl.uniprot.org/annotation/VSP_046917
http://togogenome.org/gene/9606:ZC2HC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TFG8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC/C3H-type 1|||C2HC/C3H-type 2; degenerate|||Disordered|||Polar residues|||Zinc finger C2HC domain-containing protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280252|||http://purl.uniprot.org/annotation/VAR_053853
http://togogenome.org/gene/9606:MARCHF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YJ5|||http://purl.uniprot.org/uniprot/Q8N9T1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Diminishes ability to promote MHC-I internalization.|||Disordered|||E3 ubiquitin-protein ligase MARCHF9|||Helical|||In isoform 2.|||Polar residues|||Pro residues|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274282|||http://purl.uniprot.org/annotation/VAR_030246|||http://purl.uniprot.org/annotation/VAR_030247|||http://purl.uniprot.org/annotation/VSP_022697
http://togogenome.org/gene/9606:FZD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UP38                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012973|||http://purl.uniprot.org/annotation/VAR_049290
http://togogenome.org/gene/9606:RAB28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51157                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 3.|||In isoform L.|||N-acetylserine|||Phosphoserine|||Ras-related protein Rab-28|||Removed|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121227|||http://purl.uniprot.org/annotation/PRO_0000396721|||http://purl.uniprot.org/annotation/VSP_005530|||http://purl.uniprot.org/annotation/VSP_045807
http://togogenome.org/gene/9606:KRT73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Keratin, type II cytoskeletal 73|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314881|||http://purl.uniprot.org/annotation/VAR_038091|||http://purl.uniprot.org/annotation/VAR_038092|||http://purl.uniprot.org/annotation/VAR_038093|||http://purl.uniprot.org/annotation/VAR_038094|||http://purl.uniprot.org/annotation/VAR_038095|||http://purl.uniprot.org/annotation/VSP_030417|||http://purl.uniprot.org/annotation/VSP_030418
http://togogenome.org/gene/9606:NKX2-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z383|||http://purl.uniprot.org/uniprot/E5RH49|||http://purl.uniprot.org/uniprot/P52952                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in patients with isolated congenital asplenia; unknown pathological significance; does not affect DNA binding; impairs transactivation activity.|||Homeobox|||Homeobox protein Nkx-2.5|||In ASD7 and TOF.|||In ASD7 and TOF; somatic mutation.|||In ASD7, TOF, CHNG5, HLHS2 and CTHM; unknown pathological significance; exhibits significant functional impairment with reduction of transactivation properties and dominant-negative effect; the mutant protein activity on the DIO2, TG and TPO promoters is significantly impaired.|||In ASD7.|||In ASD7; somatic mutation.|||In CHNG5; exhibits a significant functional impairment with reduction of transactivation properties and dominant-negative effect which was associated with reduced DNA binding.|||In CTMH.|||In TOF and ASD7.|||In VSD3.|||In VSD3; significantly reduced activation of NPPA gene compared to wild-type.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048937|||http://purl.uniprot.org/annotation/VAR_003752|||http://purl.uniprot.org/annotation/VAR_010116|||http://purl.uniprot.org/annotation/VAR_010117|||http://purl.uniprot.org/annotation/VAR_010118|||http://purl.uniprot.org/annotation/VAR_010119|||http://purl.uniprot.org/annotation/VAR_038212|||http://purl.uniprot.org/annotation/VAR_038213|||http://purl.uniprot.org/annotation/VAR_038214|||http://purl.uniprot.org/annotation/VAR_038215|||http://purl.uniprot.org/annotation/VAR_038216|||http://purl.uniprot.org/annotation/VAR_038217|||http://purl.uniprot.org/annotation/VAR_038218|||http://purl.uniprot.org/annotation/VAR_038219|||http://purl.uniprot.org/annotation/VAR_038220|||http://purl.uniprot.org/annotation/VAR_038221|||http://purl.uniprot.org/annotation/VAR_038222|||http://purl.uniprot.org/annotation/VAR_038223|||http://purl.uniprot.org/annotation/VAR_038224|||http://purl.uniprot.org/annotation/VAR_038225|||http://purl.uniprot.org/annotation/VAR_038226|||http://purl.uniprot.org/annotation/VAR_038227|||http://purl.uniprot.org/annotation/VAR_038228|||http://purl.uniprot.org/annotation/VAR_038229|||http://purl.uniprot.org/annotation/VAR_038230|||http://purl.uniprot.org/annotation/VAR_038231|||http://purl.uniprot.org/annotation/VAR_038232|||http://purl.uniprot.org/annotation/VAR_038233|||http://purl.uniprot.org/annotation/VAR_038234|||http://purl.uniprot.org/annotation/VAR_038235|||http://purl.uniprot.org/annotation/VAR_038236|||http://purl.uniprot.org/annotation/VAR_038237|||http://purl.uniprot.org/annotation/VAR_038238|||http://purl.uniprot.org/annotation/VAR_038239|||http://purl.uniprot.org/annotation/VAR_038240|||http://purl.uniprot.org/annotation/VAR_038241|||http://purl.uniprot.org/annotation/VAR_038242|||http://purl.uniprot.org/annotation/VAR_038243|||http://purl.uniprot.org/annotation/VAR_038244|||http://purl.uniprot.org/annotation/VAR_038245|||http://purl.uniprot.org/annotation/VAR_038246|||http://purl.uniprot.org/annotation/VAR_038247|||http://purl.uniprot.org/annotation/VAR_038248|||http://purl.uniprot.org/annotation/VAR_038249|||http://purl.uniprot.org/annotation/VAR_038250|||http://purl.uniprot.org/annotation/VAR_038251|||http://purl.uniprot.org/annotation/VAR_038252|||http://purl.uniprot.org/annotation/VAR_038253|||http://purl.uniprot.org/annotation/VAR_047869|||http://purl.uniprot.org/annotation/VAR_047870|||http://purl.uniprot.org/annotation/VAR_049581|||http://purl.uniprot.org/annotation/VAR_067586|||http://purl.uniprot.org/annotation/VAR_067587|||http://purl.uniprot.org/annotation/VAR_067588|||http://purl.uniprot.org/annotation/VAR_069058|||http://purl.uniprot.org/annotation/VAR_069590|||http://purl.uniprot.org/annotation/VSP_043492|||http://purl.uniprot.org/annotation/VSP_043493|||http://purl.uniprot.org/annotation/VSP_045481|||http://purl.uniprot.org/annotation/VSP_045482
http://togogenome.org/gene/9606:KIF18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI77                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinesin motor|||Kinesin-like protein KIF18A|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125458|||http://purl.uniprot.org/annotation/VAR_038354|||http://purl.uniprot.org/annotation/VAR_049701|||http://purl.uniprot.org/annotation/VAR_049702
http://togogenome.org/gene/9606:OR4K14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP2|||http://purl.uniprot.org/uniprot/Q8NGD5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150557|||http://purl.uniprot.org/annotation/VAR_053173|||http://purl.uniprot.org/annotation/VAR_053174
http://togogenome.org/gene/9606:KRTAP9-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXZ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||32 X 5 AA repeats of C-C-[CGSVRQH]-[SQTNP]-[PTSI]|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332261
http://togogenome.org/gene/9606:FAM120B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEJ5|||http://purl.uniprot.org/uniprot/B4DG54|||http://purl.uniprot.org/uniprot/B4DSS4|||http://purl.uniprot.org/uniprot/F5GY05|||http://purl.uniprot.org/uniprot/Q96EK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Constitutive coactivator of peroxisome proliferator-activated receptor gamma|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332990|||http://purl.uniprot.org/annotation/VAR_043021|||http://purl.uniprot.org/annotation/VAR_043022|||http://purl.uniprot.org/annotation/VAR_043023|||http://purl.uniprot.org/annotation/VAR_043024|||http://purl.uniprot.org/annotation/VAR_043025|||http://purl.uniprot.org/annotation/VAR_043026|||http://purl.uniprot.org/annotation/VAR_043027|||http://purl.uniprot.org/annotation/VAR_043028|||http://purl.uniprot.org/annotation/VSP_033415|||http://purl.uniprot.org/annotation/VSP_033416|||http://purl.uniprot.org/annotation/VSP_055267
http://togogenome.org/gene/9606:CLEC5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1U7|||http://purl.uniprot.org/uniprot/Q14DL9|||http://purl.uniprot.org/uniprot/Q9NY25                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with TYROBP.|||C-type lectin|||C-type lectin domain family 5 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046632|||http://purl.uniprot.org/annotation/VAR_050110|||http://purl.uniprot.org/annotation/VSP_012839
http://togogenome.org/gene/9606:AGXT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYV1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Alanine--glyoxylate aminotransferase 2, mitochondrial|||Associated with an increased risk for coronary heart disease (CHD) in smoker and diabetic mellitus (DM) patients in a Chinese population; higher plasma symmetric (SDMA) dimethylarginine as well as plasma and urinary beta-aminoisobutyrate (BAIB) concentrations; localized to the mitochondrion as the wild-type; reduces alanine-glyoxylate aminotransferase activity.|||Higher plasma and urinary beta-aminoisobutyrate (BAIB) concentrations.|||In isoform 2.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001269|||http://purl.uniprot.org/annotation/VAR_022140|||http://purl.uniprot.org/annotation/VAR_022141|||http://purl.uniprot.org/annotation/VAR_023483|||http://purl.uniprot.org/annotation/VAR_029513|||http://purl.uniprot.org/annotation/VAR_048231|||http://purl.uniprot.org/annotation/VAR_048232|||http://purl.uniprot.org/annotation/VAR_061006|||http://purl.uniprot.org/annotation/VAR_061007|||http://purl.uniprot.org/annotation/VSP_055802
http://togogenome.org/gene/9606:RUFY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GIA6|||http://purl.uniprot.org/uniprot/Q8WXA3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  FYVE-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||RUN|||RUN and FYVE domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245830|||http://purl.uniprot.org/annotation/VAR_060318|||http://purl.uniprot.org/annotation/VSP_059505|||http://purl.uniprot.org/annotation/VSP_059506|||http://purl.uniprot.org/annotation/VSP_059507|||http://purl.uniprot.org/annotation/VSP_059508|||http://purl.uniprot.org/annotation/VSP_059509|||http://purl.uniprot.org/annotation/VSP_059510
http://togogenome.org/gene/9606:SLC16A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36021                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect localization to the cell membrane. Abolishes T3 uptake activity.|||Does not alter kinetic characteristics of thyroid hormone (TH) transport.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MCT8 deficiency.|||In MCT8 deficiency; atypical form; characterized by developmental delay hypotonia and delayed myelination.|||In MCT8 deficiency; decreased thyroid hormone transport; decreased protein abundance; decreased localization to the plasma membrane.|||In MCT8 deficiency; does not affect homodimerization activity.|||In MCT8 deficiency; does not affect homodimerization activity; impaired thyroid hormone transporter activity; impaired localization to the cell membrane.|||In MCT8 deficiency; impaired homodimerization.|||In MCT8 deficiency; impaired thyroid hormone transporter activity; does not affect localization to the cell membrane.|||In MCT8 deficiency; impaired thyroid hormone transporter activity; impaired localization to the cell membrane.|||In MCT8 deficiency; increased homodimerization activity.|||In MCT8 deficiency; loss of thyroid hormone transport.|||In MCT8 deficiency; results in a mild clinical phenotype; retains some residual thyroid hormone transporter activity.|||Monocarboxylate transporter 8|||N-acetylalanine|||No effect on thyroid hormone (TH) transport.|||No effect on thyroid hormone transport. No effect on protein abundance. No effect on protein localization to the plasma membrane.|||Pro residues|||Reduction of thyroid hormone (TH) transport.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211401|||http://purl.uniprot.org/annotation/VAR_022348|||http://purl.uniprot.org/annotation/VAR_022349|||http://purl.uniprot.org/annotation/VAR_022350|||http://purl.uniprot.org/annotation/VAR_057723|||http://purl.uniprot.org/annotation/VAR_059054|||http://purl.uniprot.org/annotation/VAR_059055|||http://purl.uniprot.org/annotation/VAR_059056|||http://purl.uniprot.org/annotation/VAR_059057|||http://purl.uniprot.org/annotation/VAR_059058|||http://purl.uniprot.org/annotation/VAR_059059|||http://purl.uniprot.org/annotation/VAR_059060|||http://purl.uniprot.org/annotation/VAR_074572|||http://purl.uniprot.org/annotation/VAR_074573|||http://purl.uniprot.org/annotation/VAR_074574|||http://purl.uniprot.org/annotation/VAR_074575|||http://purl.uniprot.org/annotation/VAR_074576|||http://purl.uniprot.org/annotation/VAR_074577|||http://purl.uniprot.org/annotation/VAR_074578|||http://purl.uniprot.org/annotation/VAR_074579|||http://purl.uniprot.org/annotation/VAR_074580|||http://purl.uniprot.org/annotation/VAR_075145|||http://purl.uniprot.org/annotation/VAR_078497|||http://purl.uniprot.org/annotation/VAR_078498
http://togogenome.org/gene/9606:OR6C70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIJ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309493|||http://purl.uniprot.org/annotation/VAR_036971|||http://purl.uniprot.org/annotation/VAR_062050
http://togogenome.org/gene/9606:PCDHGB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-B5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003979|||http://purl.uniprot.org/annotation/VAR_048571|||http://purl.uniprot.org/annotation/VSP_008692|||http://purl.uniprot.org/annotation/VSP_008693
http://togogenome.org/gene/9606:ZNF736                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX44                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 736                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395343
http://togogenome.org/gene/9606:PIGO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEQ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in patients with severe infantile epileptic encephalopathy; unknown pathological significance.|||GPI ethanolamine phosphate transferase 3|||Helical|||In HPMRS2.|||In HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity.|||In HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression.|||In HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression; unknown pathological significance.|||In HPMRS2; decrease in mannose-ethanolamine phosphotransferase activity; increased protein expression.|||In HPMRS2; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with epileptic encephalopathy; decrease in mannose-ethanolamine phosphotransferase activity; decreased protein expression.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058438|||http://purl.uniprot.org/annotation/VAR_036332|||http://purl.uniprot.org/annotation/VAR_068809|||http://purl.uniprot.org/annotation/VAR_071074|||http://purl.uniprot.org/annotation/VAR_079410|||http://purl.uniprot.org/annotation/VAR_079411|||http://purl.uniprot.org/annotation/VAR_079412|||http://purl.uniprot.org/annotation/VAR_079413|||http://purl.uniprot.org/annotation/VAR_079414|||http://purl.uniprot.org/annotation/VAR_079415|||http://purl.uniprot.org/annotation/VAR_079416|||http://purl.uniprot.org/annotation/VSP_003944
http://togogenome.org/gene/9606:TGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RS0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases catalytic activity to 11 percent of wild type.|||Decreases catalytic activity to 13 percent of wild type.|||Decreases catalytic activity to 26 percent of wild type.|||Decreases catalytic activity to 4 percent of wild type.|||Decreases catalytic activity to 5 percent of wild type.|||Decreases catalytic activity to 6 percent of wild type.|||Disordered|||Loss of catalytic activity.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Sufficient for catalytic activity|||Trimethylguanosine synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204468|||http://purl.uniprot.org/annotation/VAR_024734|||http://purl.uniprot.org/annotation/VAR_024735|||http://purl.uniprot.org/annotation/VAR_024736|||http://purl.uniprot.org/annotation/VAR_024737|||http://purl.uniprot.org/annotation/VAR_024738|||http://purl.uniprot.org/annotation/VAR_056241|||http://purl.uniprot.org/annotation/VAR_056242
http://togogenome.org/gene/9606:DDI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTU0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein DDI1 homolog 1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287086|||http://purl.uniprot.org/annotation/VAR_032259|||http://purl.uniprot.org/annotation/VAR_032260|||http://purl.uniprot.org/annotation/VAR_032261
http://togogenome.org/gene/9606:VRK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV63                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Inactive serine/threonine-protein kinase VRK3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086808|||http://purl.uniprot.org/annotation/VAR_041295|||http://purl.uniprot.org/annotation/VAR_041296|||http://purl.uniprot.org/annotation/VAR_041297|||http://purl.uniprot.org/annotation/VAR_041298|||http://purl.uniprot.org/annotation/VAR_041299|||http://purl.uniprot.org/annotation/VAR_041300|||http://purl.uniprot.org/annotation/VAR_041301|||http://purl.uniprot.org/annotation/VAR_051682|||http://purl.uniprot.org/annotation/VAR_051683|||http://purl.uniprot.org/annotation/VAR_051684|||http://purl.uniprot.org/annotation/VSP_008544|||http://purl.uniprot.org/annotation/VSP_008545|||http://purl.uniprot.org/annotation/VSP_043409
http://togogenome.org/gene/9606:ATXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54253|||http://purl.uniprot.org/uniprot/Q96FF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AXH|||Ataxin-1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Interaction with USP7|||No effect on sumoylation.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||RNA-binding|||Reduces phosphorylation but does not affect nuclear localization.|||Self-association|||Sumoylation reduced to 40% of wild-type.|||Sumoylation reduced to 42% of wild-type.|||Sumoylation reduced to 43% of wild-type.|||Sumoylation reduced to 44% of wild-type.|||Sumoylation reduced to 46% of wild-type.|||Sumoylation reduced to 53% of wild-type.|||Sumoylation reduced to 57% of wild-type.|||Sumoylation reduced to 62% of wild-type.|||Sumoylation reduced to 68% of wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064751|||http://purl.uniprot.org/annotation/VAR_046616|||http://purl.uniprot.org/annotation/VAR_046617
http://togogenome.org/gene/9606:PGA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJD9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Pepsin A-5|||Peptidase A1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415759|||http://purl.uniprot.org/annotation/PRO_0000415760
http://togogenome.org/gene/9606:PEX13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92968                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In PBD11B.|||In PBD11B; neonatal adrenoleukodystrophy.|||Interaction with PEX19|||Peroxisomal matrix|||Peroxisomal membrane protein PEX13|||Phosphoserine|||Pro residues|||SH3|||Targeting to peroxisomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058323|||http://purl.uniprot.org/annotation/VAR_009306|||http://purl.uniprot.org/annotation/VAR_087140
http://togogenome.org/gene/9606:MEA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7W8|||http://purl.uniprot.org/uniprot/Q16626                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Male-enhanced antigen 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096341|||http://purl.uniprot.org/annotation/VAR_058297
http://togogenome.org/gene/9606:GPRC5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFY5|||http://purl.uniprot.org/uniprot/Q9BSP0|||http://purl.uniprot.org/uniprot/Q9NQ84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor family C group 5 member C|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012967|||http://purl.uniprot.org/annotation/PRO_5014312658|||http://purl.uniprot.org/annotation/VSP_037725
http://togogenome.org/gene/9606:RDM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG50                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Does not affect its subcellular distribution.|||In isoform 10 and isoform 11.|||In isoform 12.|||In isoform 2, isoform 4, isoform 6, isoform 9 and isoform 11.|||In isoform 3, isoform 4 and isoform 7.|||In isoform 3, isoform 4, isoform 7, isoform 8 and isoform 9.|||In isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||Necessary for nuclear and nucleolar localization|||Necessary for nuclear localization and for nucleolar accumulation in response to heat shock|||RAD52 motif-containing protein 1|||RRM|||Reduces its nuclear and nucleolar accumulation. Increases its cytoplasmic accumulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299528|||http://purl.uniprot.org/annotation/VAR_034835|||http://purl.uniprot.org/annotation/VAR_034836|||http://purl.uniprot.org/annotation/VSP_029648|||http://purl.uniprot.org/annotation/VSP_029649|||http://purl.uniprot.org/annotation/VSP_029650|||http://purl.uniprot.org/annotation/VSP_029653|||http://purl.uniprot.org/annotation/VSP_029654|||http://purl.uniprot.org/annotation/VSP_029655|||http://purl.uniprot.org/annotation/VSP_037151|||http://purl.uniprot.org/annotation/VSP_044856
http://togogenome.org/gene/9606:SLC30A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRI3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased phosphorylation. Increased localization to lysosome.|||Helical|||In TNZD; decreased protein abundance; increased protein aggregation; no dominant negative effect.|||In TNZD; decreased zinc ion import into organelle; dominant negative effect; changed protein localization; retained in endoplasmic reticulum and Golgi; dominant negative effect; results in decreased zinc secretion in milk.|||In isoform 2.|||Increased homodimerization activity.|||Loss of interaction with AP3D1. Loss of localization to lysosome.|||Loss of localization to lysosome.|||Loss of localization to mitochondrial inner membrane. Loss of function in zinc ion import into mitochondrion.|||Lumenal|||Lysosomal targeting motif|||Mitochondrial localization signal|||Phosphoserine|||Proton-coupled zinc antiporter SLC30A2|||in chain A|||in chain B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206094|||http://purl.uniprot.org/annotation/VAR_069309|||http://purl.uniprot.org/annotation/VAR_069310|||http://purl.uniprot.org/annotation/VSP_061729
http://togogenome.org/gene/9606:CDC42BPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DT37                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||CNH|||CRIB|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MRCK gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086397|||http://purl.uniprot.org/annotation/VAR_040840|||http://purl.uniprot.org/annotation/VAR_040841|||http://purl.uniprot.org/annotation/VAR_040842|||http://purl.uniprot.org/annotation/VAR_040843|||http://purl.uniprot.org/annotation/VAR_057105
http://togogenome.org/gene/9606:TEX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Testis-expressed protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072493
http://togogenome.org/gene/9606:ST6GALNAC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV27|||http://purl.uniprot.org/uniprot/Q9BVH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149280|||http://purl.uniprot.org/annotation/PRO_5002803328
http://togogenome.org/gene/9606:TRA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62995                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Basic residues|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Linker|||N-acetylserine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Transformer-2 protein homolog beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081983|||http://purl.uniprot.org/annotation/VSP_005896|||http://purl.uniprot.org/annotation/VSP_005898|||http://purl.uniprot.org/annotation/VSP_005899
http://togogenome.org/gene/9606:NDOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHB4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FAD-binding FR-type|||Flavodoxin-like|||In allele NDOR1*1; shows a decrease in affinity for NADPH and a reduction in ferricyanide reductase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NADPH-dependent diflavin oxidoreductase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319539|||http://purl.uniprot.org/annotation/VAR_039010|||http://purl.uniprot.org/annotation/VSP_031487|||http://purl.uniprot.org/annotation/VSP_046313|||http://purl.uniprot.org/annotation/VSP_046314|||http://purl.uniprot.org/annotation/VSP_053807
http://togogenome.org/gene/9606:CROCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TZA2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Rootletin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239943|||http://purl.uniprot.org/annotation/VAR_059628|||http://purl.uniprot.org/annotation/VAR_059629|||http://purl.uniprot.org/annotation/VAR_059630|||http://purl.uniprot.org/annotation/VAR_061626|||http://purl.uniprot.org/annotation/VAR_061627|||http://purl.uniprot.org/annotation/VAR_083473|||http://purl.uniprot.org/annotation/VAR_083474|||http://purl.uniprot.org/annotation/VSP_052069|||http://purl.uniprot.org/annotation/VSP_052070
http://togogenome.org/gene/9606:SEMA3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14563                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Ig-like C2-type|||In HH16; phenotype consistent with Kallmann syndrome.|||In HH16; phenotype consistent with Kallmann syndrome; digenic; found in a patient also carrying mutation Asp-217 in KAL1.|||In HH16; phenotype consistent with Kallmann syndrome; digenic; found in a patient also carrying mutation Cys-268 in PROKR2.|||In HH16; phenotype consistent with Kallmann syndrome; digenic; found in patients also carrying mutation Cys-268 in PROKR2 or mutation Arg-687 in FGFR1.|||In HH16; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032303|||http://purl.uniprot.org/annotation/VAR_036283|||http://purl.uniprot.org/annotation/VAR_064749|||http://purl.uniprot.org/annotation/VAR_069200|||http://purl.uniprot.org/annotation/VAR_069201|||http://purl.uniprot.org/annotation/VAR_069202|||http://purl.uniprot.org/annotation/VAR_069203|||http://purl.uniprot.org/annotation/VAR_069204|||http://purl.uniprot.org/annotation/VAR_069205|||http://purl.uniprot.org/annotation/VAR_069206|||http://purl.uniprot.org/annotation/VAR_072986|||http://purl.uniprot.org/annotation/VAR_072987|||http://purl.uniprot.org/annotation/VAR_072988|||http://purl.uniprot.org/annotation/VAR_072989|||http://purl.uniprot.org/annotation/VAR_072990
http://togogenome.org/gene/9606:HOOK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJC3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates interaction with AKTIP, VPS16, VPS18, VPS39 and VPS41, AP4M1, FHIP1B, decreases interaction with HOOK2 but does not affect interaction withHOOK3; when associated with 661-A-A-662.|||Abrogates interaction with AKTIP, VPS16, VPS18, VPS39 and VPS41, AP4M1, FHIP1B, decreases interaction with HOOK2 but does not affect interaction withHOOK3; when associated with 669-A-A-670.|||Calponin-homology (CH)|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein Hook homolog 1|||Sufficient for homodimerization, interaction wit HOOK2, HOOK3 and AP4M1|||Sufficient for interaction with AKTIP and VPS18|||Sufficient for interaction with microtubules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219192|||http://purl.uniprot.org/annotation/VAR_035709|||http://purl.uniprot.org/annotation/VAR_077930|||http://purl.uniprot.org/annotation/VSP_056226
http://togogenome.org/gene/9606:CC2D2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2K1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Coiled-coil and C2 domain-containing protein 2A|||Disordered|||In COACH2 and JBTS9.|||In JBTS9 and COACH2.|||In JBTS9.|||In JBTS9; benign variant.|||In JBTS9; digenic inheritance; the patient also carries mutation C-360 in CEP41.|||In JBTS9; unknown pathological significance.|||In MKS6 and JBTS9.|||In MKS6; unknown pathological significance.|||In RP93.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317250|||http://purl.uniprot.org/annotation/VAR_038489|||http://purl.uniprot.org/annotation/VAR_038490|||http://purl.uniprot.org/annotation/VAR_055321|||http://purl.uniprot.org/annotation/VAR_055322|||http://purl.uniprot.org/annotation/VAR_055323|||http://purl.uniprot.org/annotation/VAR_055324|||http://purl.uniprot.org/annotation/VAR_062293|||http://purl.uniprot.org/annotation/VAR_062804|||http://purl.uniprot.org/annotation/VAR_062805|||http://purl.uniprot.org/annotation/VAR_062806|||http://purl.uniprot.org/annotation/VAR_063804|||http://purl.uniprot.org/annotation/VAR_067535|||http://purl.uniprot.org/annotation/VAR_068169|||http://purl.uniprot.org/annotation/VAR_069045|||http://purl.uniprot.org/annotation/VAR_069046|||http://purl.uniprot.org/annotation/VAR_075698|||http://purl.uniprot.org/annotation/VAR_076881|||http://purl.uniprot.org/annotation/VAR_076882|||http://purl.uniprot.org/annotation/VAR_076883|||http://purl.uniprot.org/annotation/VAR_076884|||http://purl.uniprot.org/annotation/VAR_076885|||http://purl.uniprot.org/annotation/VAR_076886|||http://purl.uniprot.org/annotation/VAR_076887|||http://purl.uniprot.org/annotation/VAR_076888|||http://purl.uniprot.org/annotation/VAR_076889|||http://purl.uniprot.org/annotation/VAR_076890|||http://purl.uniprot.org/annotation/VAR_076891|||http://purl.uniprot.org/annotation/VAR_077560|||http://purl.uniprot.org/annotation/VAR_087118|||http://purl.uniprot.org/annotation/VAR_087303|||http://purl.uniprot.org/annotation/VAR_087304|||http://purl.uniprot.org/annotation/VSP_030923|||http://purl.uniprot.org/annotation/VSP_037223|||http://purl.uniprot.org/annotation/VSP_045255|||http://purl.uniprot.org/annotation/VSP_045256|||http://purl.uniprot.org/annotation/VSP_045453|||http://purl.uniprot.org/annotation/VSP_045454
http://togogenome.org/gene/9606:TBC1D14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A071|||http://purl.uniprot.org/uniprot/F5GXK4|||http://purl.uniprot.org/uniprot/Q9P2M4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of inhibition of autophagosome formation; when associated with A-472.|||Loss of inhibition of autophagosome formation; when associated with A-508.|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208040|||http://purl.uniprot.org/annotation/VAR_059856|||http://purl.uniprot.org/annotation/VAR_067442|||http://purl.uniprot.org/annotation/VSP_041460|||http://purl.uniprot.org/annotation/VSP_041461
http://togogenome.org/gene/9606:SPRR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Small proline-rich protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150006|||http://purl.uniprot.org/annotation/VAR_034517
http://togogenome.org/gene/9606:GPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTD8|||http://purl.uniprot.org/uniprot/I6QTG3|||http://purl.uniprot.org/uniprot/P51654|||http://purl.uniprot.org/uniprot/Q53H15                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes proteolytic processing. Abolishes interaction with WNT5A and ability to regulate Wnt signaling. Increases binding of hedgehog protein SHH to the PTC1 receptor and abolishes ability to inhibit hedgehog signaling.|||Cleavage|||GPI-anchor amidated asparagine|||Glypican-3 alpha subunit|||Glypican-3 beta subunit|||In SGBS1.|||In isoform 2.|||In isoform 3.|||Interchain (between alpha and beta chains)|||N-linked (GlcNAc...) asparagine|||No effect on proteolytic processing.|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine; by FAM20C|||Pyrrolidone carboxylic acid|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012310|||http://purl.uniprot.org/annotation/PRO_0000445410|||http://purl.uniprot.org/annotation/PRO_0000445411|||http://purl.uniprot.org/annotation/PRO_5010125021|||http://purl.uniprot.org/annotation/PRO_5010139063|||http://purl.uniprot.org/annotation/PRO_5040102061|||http://purl.uniprot.org/annotation/VAR_021385|||http://purl.uniprot.org/annotation/VAR_069139|||http://purl.uniprot.org/annotation/VSP_046117|||http://purl.uniprot.org/annotation/VSP_046703
http://togogenome.org/gene/9606:HOXA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00056                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A4|||In a breast cancer sample; somatic mutation.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200048|||http://purl.uniprot.org/annotation/VAR_028414|||http://purl.uniprot.org/annotation/VAR_028415|||http://purl.uniprot.org/annotation/VAR_028416|||http://purl.uniprot.org/annotation/VAR_028417|||http://purl.uniprot.org/annotation/VAR_028418|||http://purl.uniprot.org/annotation/VAR_036266
http://togogenome.org/gene/9606:ACTL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JWF8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Actin-like protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232865
http://togogenome.org/gene/9606:CCT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50991                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||T-complex protein 1 subunit delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128332|||http://purl.uniprot.org/annotation/VAR_052266|||http://purl.uniprot.org/annotation/VSP_045537
http://togogenome.org/gene/9606:ECHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Ethylmalonyl-CoA decarboxylase|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||In isoform 6.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273246|||http://purl.uniprot.org/annotation/VSP_022498|||http://purl.uniprot.org/annotation/VSP_042581|||http://purl.uniprot.org/annotation/VSP_042582|||http://purl.uniprot.org/annotation/VSP_042583
http://togogenome.org/gene/9606:PCM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUU9|||http://purl.uniprot.org/uniprot/B9EIS5|||http://purl.uniprot.org/uniprot/Q15154                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Breakpoint for translocation to form PCM1-JAK2 fusion protein|||Breakpoint for translocation to form PCM1-RET fusion protein|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with BBS4|||Interaction with HAP1|||Mediates interaction with DZIP1|||N-acetylalanine|||N6-acetyllysine|||Pericentriolar material 1 protein|||Pericentriolar material 1 protein C-terminal|||Phosphomimetic mutant.|||Phosphorylated.|||Phosphoserine|||Phosphoserine; by PLK4|||Phosphoserine; in variant Ser-159|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274037|||http://purl.uniprot.org/annotation/VAR_030164|||http://purl.uniprot.org/annotation/VAR_030165|||http://purl.uniprot.org/annotation/VAR_030166|||http://purl.uniprot.org/annotation/VAR_030167|||http://purl.uniprot.org/annotation/VAR_030168|||http://purl.uniprot.org/annotation/VAR_030169|||http://purl.uniprot.org/annotation/VAR_030170|||http://purl.uniprot.org/annotation/VAR_047381|||http://purl.uniprot.org/annotation/VAR_047382|||http://purl.uniprot.org/annotation/VAR_047383|||http://purl.uniprot.org/annotation/VAR_047384|||http://purl.uniprot.org/annotation/VSP_022609|||http://purl.uniprot.org/annotation/VSP_022610|||http://purl.uniprot.org/annotation/VSP_022611|||http://purl.uniprot.org/annotation/VSP_059399|||http://purl.uniprot.org/annotation/VSP_059400|||http://purl.uniprot.org/annotation/VSP_059401
http://togogenome.org/gene/9606:GULP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BZV7|||http://purl.uniprot.org/uniprot/Q9UBP9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of dimerization; when associated with P-176.|||Loss of dimerization; when associated with P-183.|||PID|||PTB domain-containing engulfment adapter protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296679|||http://purl.uniprot.org/annotation/VSP_027250|||http://purl.uniprot.org/annotation/VSP_027251|||http://purl.uniprot.org/annotation/VSP_044703|||http://purl.uniprot.org/annotation/VSP_045540
http://togogenome.org/gene/9606:RHBDF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CC6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Inactive rhomboid protein 1|||Loss of N-glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340104|||http://purl.uniprot.org/annotation/VAR_044006
http://togogenome.org/gene/9606:GJB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9U1J4|||http://purl.uniprot.org/uniprot/P29033                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||INTRAMEM|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-2 protein|||Gap junction protein cysteine-rich|||Helical|||In BAPS.|||In DFNA3A.|||In DFNA3A; does not affect protein trafficking; affects the ability to form functional channels; dominant negative effect.|||In DFNA3A; the mutant is targeted to the plasma membrane but fails to transfer ionic calcium or propidium iodide intercellularly suggesting disruption of both ionic and biochemical coupling; heterozygous gap junctions also show dysfunctional intercellular couplings and hemichannel opening confirming the dominant-negative nature of the mutation.|||In DFNB1A.|||In DFNB1A; does not form gap junctions since the mutated protein is confined in the cytoplasm and not transported to the cell membrane; when the mutation is coexpressed with the wild-type protein ionic and biochemical coupling is normal consistent with the recessive nature of the mutation.|||In DFNB1A; it is correctly synthesized and targeted to the plasma membrane; it inefficiently forms intercellular channels that display an abnormal electrical behavior.|||In DFNB1A; sorted to the plasma membrane normally and forms gap junctions that were morphologically and electrically indistinguishable from those of control; the mutation reduces the permeability of GJB2 gap junction channels to inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), resulting in blockade of the Ins(1,4,5)P3-induced inward calcium current in neighboring cells.|||In DFNB1A; the mutant disrupts cellular communication.|||In KIDAD and HID syndrome.|||In KIDAD.|||In PPKDFN and DFNA3A; does not affect protein trafficking; affects the ability to form functional channels; dominant negative effect.|||In PPKDFN; impairs trafficking; localizes intracellularly closed to the nucleus; affects the ability to form functional channels; phenotype can be rescued by coexpression with wild-type protein.|||In PPKDFN; the mutant has a dominant-negative effect on connexin trafficking.|||In PPKDFN; the mutant protein completely prevents the formation of functional channels.|||In VOWNKL and PPKDFN; impairs trafficking; localizes intracellularly closed to the nucleus; affects the ability to form functional channels; phenotype can be rescued by coexpression with wild-type protein.|||In VOWNKL.|||In a patient with congenital erythrokeratodermia; unknown pathological significance.|||In deafness.|||Loss of gap junction ion conductance, probably due to very low open probability of the channels. Can form functional channels with wild-type, but with strongly reduced channel conductance. No visible effect on channel assembly and membrane insertion.|||Loss of gap junction ion conductance.|||May contribute to deafness.|||Strongly reduced insertion into the cell membrane and strongly reduced gap junction plaque assembly.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057855|||http://purl.uniprot.org/annotation/VAR_002137|||http://purl.uniprot.org/annotation/VAR_002138|||http://purl.uniprot.org/annotation/VAR_002139|||http://purl.uniprot.org/annotation/VAR_002140|||http://purl.uniprot.org/annotation/VAR_002141|||http://purl.uniprot.org/annotation/VAR_002142|||http://purl.uniprot.org/annotation/VAR_002143|||http://purl.uniprot.org/annotation/VAR_002144|||http://purl.uniprot.org/annotation/VAR_002145|||http://purl.uniprot.org/annotation/VAR_002146|||http://purl.uniprot.org/annotation/VAR_008709|||http://purl.uniprot.org/annotation/VAR_008710|||http://purl.uniprot.org/annotation/VAR_009965|||http://purl.uniprot.org/annotation/VAR_009966|||http://purl.uniprot.org/annotation/VAR_009967|||http://purl.uniprot.org/annotation/VAR_009968|||http://purl.uniprot.org/annotation/VAR_009969|||http://purl.uniprot.org/annotation/VAR_009970|||http://purl.uniprot.org/annotation/VAR_015453|||http://purl.uniprot.org/annotation/VAR_015454|||http://purl.uniprot.org/annotation/VAR_015455|||http://purl.uniprot.org/annotation/VAR_015456|||http://purl.uniprot.org/annotation/VAR_015457|||http://purl.uniprot.org/annotation/VAR_015458|||http://purl.uniprot.org/annotation/VAR_015459|||http://purl.uniprot.org/annotation/VAR_015460|||http://purl.uniprot.org/annotation/VAR_015461|||http://purl.uniprot.org/annotation/VAR_015935|||http://purl.uniprot.org/annotation/VAR_015936|||http://purl.uniprot.org/annotation/VAR_015937|||http://purl.uniprot.org/annotation/VAR_015938|||http://purl.uniprot.org/annotation/VAR_015939|||http://purl.uniprot.org/annotation/VAR_015940|||http://purl.uniprot.org/annotation/VAR_015941|||http://purl.uniprot.org/annotation/VAR_015942|||http://purl.uniprot.org/annotation/VAR_015943|||http://purl.uniprot.org/annotation/VAR_015944|||http://purl.uniprot.org/annotation/VAR_016839|||http://purl.uniprot.org/annotation/VAR_023605|||http://purl.uniprot.org/annotation/VAR_023606|||http://purl.uniprot.org/annotation/VAR_023607|||http://purl.uniprot.org/annotation/VAR_023608|||http://purl.uniprot.org/annotation/VAR_023609|||http://purl.uniprot.org/annotation/VAR_023610|||http://purl.uniprot.org/annotation/VAR_023611|||http://purl.uniprot.org/annotation/VAR_023612|||http://purl.uniprot.org/annotation/VAR_023613|||http://purl.uniprot.org/annotation/VAR_023614|||http://purl.uniprot.org/annotation/VAR_023615|||http://purl.uniprot.org/annotation/VAR_023616|||http://purl.uniprot.org/annotation/VAR_023617|||http://purl.uniprot.org/annotation/VAR_032749|||http://purl.uniprot.org/annotation/VAR_032750|||http://purl.uniprot.org/annotation/VAR_032751|||http://purl.uniprot.org/annotation/VAR_032752|||http://purl.uniprot.org/annotation/VAR_057959|||http://purl.uniprot.org/annotation/VAR_060798|||http://purl.uniprot.org/annotation/VAR_060799|||http://purl.uniprot.org/annotation/VAR_060800|||http://purl.uniprot.org/annotation/VAR_060801|||http://purl.uniprot.org/annotation/VAR_069519|||http://purl.uniprot.org/annotation/VAR_069520|||http://purl.uniprot.org/annotation/VAR_069521|||http://purl.uniprot.org/annotation/VAR_069522|||http://purl.uniprot.org/annotation/VAR_069523|||http://purl.uniprot.org/annotation/VAR_069524|||http://purl.uniprot.org/annotation/VAR_083826
http://togogenome.org/gene/9606:ZDHHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W6M3|||http://purl.uniprot.org/uniprot/Q9NYG2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Extracellular|||Helical|||Impaired localization leading to localization to the endoplasmic reticulum.|||In isoform 2.|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC3|||Phosphotyrosine|||Probable loss of protein-cysteine S-palmitoyltransferase activity. Loss of function in the TRAIL-activated apoptotic signaling pathway.|||Probable loss of protein-cysteine S-palmitoyltransferase activity. Loss of function in the TRAIL-activated apoptotic signaling pathway. No effect on binding of the TNFRSF10A substrate.|||S-palmitoyl cysteine|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422064|||http://purl.uniprot.org/annotation/VSP_006934
http://togogenome.org/gene/9606:BRME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VDD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Break repair meiotic recombinase recruitment factor 1|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295737|||http://purl.uniprot.org/annotation/VAR_033356|||http://purl.uniprot.org/annotation/VAR_033357|||http://purl.uniprot.org/annotation/VSP_027044
http://togogenome.org/gene/9606:DEFB127                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1M4                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 127                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007002|||http://purl.uniprot.org/annotation/PRO_0000007003|||http://purl.uniprot.org/annotation/VAR_048864|||http://purl.uniprot.org/annotation/VAR_048865
http://togogenome.org/gene/9606:SNAP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95721                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Synaptosomal-associated protein 29|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213601
http://togogenome.org/gene/9606:PPP1R3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZBB8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  CBM21|||Disordered|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 3G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394965|||http://purl.uniprot.org/annotation/VAR_063262
http://togogenome.org/gene/9606:UGT1A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5DT02|||http://purl.uniprot.org/uniprot/Q9HAW8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Decreased estrone and 16alpha-hydroxyestrone glucuronosyltransferase activity.|||Helical|||In isoform 2.|||Increased estriol, 17-epiestriol and 16alpha-hydroxyestrone glucuronosyltransferase activity. Decreased of estrone and 16-epiestriol glucuronosyltransferase activity.|||Loss of estrone and 16alpha-hydroxyestrone glucuronosyltransferase activity.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036009|||http://purl.uniprot.org/annotation/PRO_5014205884|||http://purl.uniprot.org/annotation/VAR_018354|||http://purl.uniprot.org/annotation/VAR_018355|||http://purl.uniprot.org/annotation/VAR_052464|||http://purl.uniprot.org/annotation/VAR_052465|||http://purl.uniprot.org/annotation/VSP_053966
http://togogenome.org/gene/9606:NRSN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ57                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Neurensin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270583|||http://purl.uniprot.org/annotation/VAR_029816|||http://purl.uniprot.org/annotation/VAR_053737
http://togogenome.org/gene/9606:ABCA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT16|||http://purl.uniprot.org/uniprot/Q86UQ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 13|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253573|||http://purl.uniprot.org/annotation/VAR_055470|||http://purl.uniprot.org/annotation/VAR_059087|||http://purl.uniprot.org/annotation/VAR_059088|||http://purl.uniprot.org/annotation/VAR_059089|||http://purl.uniprot.org/annotation/VAR_059090|||http://purl.uniprot.org/annotation/VAR_059091|||http://purl.uniprot.org/annotation/VAR_059092|||http://purl.uniprot.org/annotation/VAR_059093|||http://purl.uniprot.org/annotation/VAR_059094|||http://purl.uniprot.org/annotation/VAR_059095|||http://purl.uniprot.org/annotation/VAR_059096|||http://purl.uniprot.org/annotation/VAR_059097|||http://purl.uniprot.org/annotation/VAR_059098|||http://purl.uniprot.org/annotation/VAR_059099|||http://purl.uniprot.org/annotation/VAR_059100|||http://purl.uniprot.org/annotation/VAR_059101|||http://purl.uniprot.org/annotation/VAR_059102|||http://purl.uniprot.org/annotation/VAR_059103|||http://purl.uniprot.org/annotation/VAR_059104|||http://purl.uniprot.org/annotation/VAR_059105|||http://purl.uniprot.org/annotation/VSP_021068|||http://purl.uniprot.org/annotation/VSP_021069|||http://purl.uniprot.org/annotation/VSP_021070|||http://purl.uniprot.org/annotation/VSP_054633|||http://purl.uniprot.org/annotation/VSP_054634|||http://purl.uniprot.org/annotation/VSP_054635|||http://purl.uniprot.org/annotation/VSP_054636
http://togogenome.org/gene/9606:ZSCAN21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5A6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047297
http://togogenome.org/gene/9606:FAM200B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CF97                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM200B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394262
http://togogenome.org/gene/9606:CD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09564|||http://purl.uniprot.org/uniprot/Q29VG3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 9 AA tandem repeats, potential spacer function|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||T-cell antigen CD7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014633|||http://purl.uniprot.org/annotation/PRO_5014308630|||http://purl.uniprot.org/annotation/VAR_049855
http://togogenome.org/gene/9606:DNAH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0I1S1|||http://purl.uniprot.org/uniprot/Q8IVF4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||AAA+ ATPase|||Basic and acidic residues|||CFDEFNR motif|||Disordered|||Dynein axonemal heavy chain 10|||GPAGTGKT motif|||In SPGF56.|||In SPGF56; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Stalk|||Stem|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318938|||http://purl.uniprot.org/annotation/VAR_038916|||http://purl.uniprot.org/annotation/VAR_060135|||http://purl.uniprot.org/annotation/VAR_060136|||http://purl.uniprot.org/annotation/VAR_060137|||http://purl.uniprot.org/annotation/VAR_060138|||http://purl.uniprot.org/annotation/VAR_060139|||http://purl.uniprot.org/annotation/VAR_060140|||http://purl.uniprot.org/annotation/VAR_062177|||http://purl.uniprot.org/annotation/VAR_086228|||http://purl.uniprot.org/annotation/VAR_086229|||http://purl.uniprot.org/annotation/VAR_086230|||http://purl.uniprot.org/annotation/VAR_086231|||http://purl.uniprot.org/annotation/VSP_033518|||http://purl.uniprot.org/annotation/VSP_033519
http://togogenome.org/gene/9606:FEM1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK73                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Repeat|||Site|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Abolished ability to promote ubiquitination of target proteins such as GLI1.|||Abolished binding to -Gly-Leu-Asp-Arg C-degron at the C-terminus.|||Abolished binding to -Gly-Leu-Asp-Arg C-degron at the C-terminus; when associated with A-131.|||Abolished binding to -Gly-Leu-Asp-Arg C-degron at the C-terminus; when associated with A-82.|||Cleavage; by a caspase-3-like protease|||Does not affect cleavage by a caspase-3-like protease.|||Prevents cleavage by a caspase-3-like protease.|||Protein fem-1 homolog B|||Strongly reduced binding to -Gly-Leu-Asp-Arg C-degron at the C-terminus; when associated with A-163.|||Strongly reduced binding to -Gly-Leu-Asp-Arg C-degron at the C-terminus; when associated with A-193.|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324530
http://togogenome.org/gene/9606:TTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||GRF-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcription termination factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074376|||http://purl.uniprot.org/annotation/VAR_023393|||http://purl.uniprot.org/annotation/VAR_034431|||http://purl.uniprot.org/annotation/VAR_061234|||http://purl.uniprot.org/annotation/VAR_061235|||http://purl.uniprot.org/annotation/VAR_061236|||http://purl.uniprot.org/annotation/VSP_015370|||http://purl.uniprot.org/annotation/VSP_015371
http://togogenome.org/gene/9606:CHMP4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes localization to the Flemming body and ability to delay abscission.|||Basic and acidic residues|||Charged multivesicular body protein 4c|||Disordered|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||Phosphoserine; by AURKB|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211495|||http://purl.uniprot.org/annotation/VAR_052028
http://togogenome.org/gene/9606:TACR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29371                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In HH11.|||In HH11; the patient also carries a mutation in FGFR1.|||In HH11; unequivocal evidence of impaired receptor signaling.|||May contribute to hypogonadotropic hypogonadism in patients carrying disease-causing mutations in FGFR1.|||May contribute to hypogonadotropic hypogonadism in patients carrying disease-causing mutations in SPRY4 or KAL1.|||N-linked (GlcNAc...) asparagine|||Neuromedin-K receptor|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069899|||http://purl.uniprot.org/annotation/VAR_049422|||http://purl.uniprot.org/annotation/VAR_049423|||http://purl.uniprot.org/annotation/VAR_069177|||http://purl.uniprot.org/annotation/VAR_069178|||http://purl.uniprot.org/annotation/VAR_069963|||http://purl.uniprot.org/annotation/VAR_072976|||http://purl.uniprot.org/annotation/VAR_072977
http://togogenome.org/gene/9606:PGM2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCE3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glucose 1,6-bisphosphate synthase|||In NEDHFS.|||Phosphoserine|||Phosphoserine intermediate|||via phosphate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147784|||http://purl.uniprot.org/annotation/VAR_028094|||http://purl.uniprot.org/annotation/VAR_028095|||http://purl.uniprot.org/annotation/VAR_056665|||http://purl.uniprot.org/annotation/VAR_087994|||http://purl.uniprot.org/annotation/VAR_087995
http://togogenome.org/gene/9606:MFSD13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 180                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256224
http://togogenome.org/gene/9606:UBXN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92575                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Interaction with UBQLN1|||Phosphothreonine|||Polar residues|||UBX|||UBX domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211027|||http://purl.uniprot.org/annotation/VAR_052686
http://togogenome.org/gene/9606:CPLANE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494BZW6|||http://purl.uniprot.org/uniprot/Q9H799                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Ciliogenesis and planar polarity effector 1|||Disordered|||Helical|||In JBTS17.|||In OFD6.|||In OFD6; unknown pathological significance.|||In isoform 2.|||May be associated with susceptibility to monomelic amyotrophy.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332133|||http://purl.uniprot.org/annotation/VAR_042948|||http://purl.uniprot.org/annotation/VAR_042949|||http://purl.uniprot.org/annotation/VAR_042950|||http://purl.uniprot.org/annotation/VAR_042951|||http://purl.uniprot.org/annotation/VAR_042952|||http://purl.uniprot.org/annotation/VAR_068165|||http://purl.uniprot.org/annotation/VAR_068166|||http://purl.uniprot.org/annotation/VAR_068167|||http://purl.uniprot.org/annotation/VAR_072544|||http://purl.uniprot.org/annotation/VAR_072553|||http://purl.uniprot.org/annotation/VAR_072554|||http://purl.uniprot.org/annotation/VAR_072555|||http://purl.uniprot.org/annotation/VAR_072556|||http://purl.uniprot.org/annotation/VAR_076776|||http://purl.uniprot.org/annotation/VAR_076777|||http://purl.uniprot.org/annotation/VAR_076778|||http://purl.uniprot.org/annotation/VAR_076779|||http://purl.uniprot.org/annotation/VAR_076780|||http://purl.uniprot.org/annotation/VAR_076781|||http://purl.uniprot.org/annotation/VAR_077558|||http://purl.uniprot.org/annotation/VAR_082878|||http://purl.uniprot.org/annotation/VSP_044052|||http://purl.uniprot.org/annotation/VSP_044053|||http://purl.uniprot.org/annotation/VSP_044054|||http://purl.uniprot.org/annotation/VSP_044055
http://togogenome.org/gene/9606:ANXA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50995|||http://purl.uniprot.org/uniprot/Q5T0G8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A11|||Disordered|||In ALS23; forms cytoplasmic aggregates in patient tissues; no effect on nuclear and cytoplasmic localization; loss of interaction with S100A6.|||In ALS23; unknown pathological significance.|||In ALS23; unknown pathological significance; changed cytoplasmic localization with decreased association with vesicle-like structures; increased interaction with S100A6.|||In ALS23; unknown pathological significance; increased aggregation in the cytoplasm sequestering the wild-type protein in these aggregates; loss of interaction with S100A6.|||In ALS23; unknown pathological significance; no effect on aggregation; loss of interaction with S100A6.|||In IBMWMA.|||In isoform 2.|||N6-acetyllysine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067510|||http://purl.uniprot.org/annotation/VAR_012006|||http://purl.uniprot.org/annotation/VAR_012007|||http://purl.uniprot.org/annotation/VAR_048259|||http://purl.uniprot.org/annotation/VAR_080653|||http://purl.uniprot.org/annotation/VAR_080654|||http://purl.uniprot.org/annotation/VAR_080655|||http://purl.uniprot.org/annotation/VAR_080656|||http://purl.uniprot.org/annotation/VAR_080657|||http://purl.uniprot.org/annotation/VAR_080658|||http://purl.uniprot.org/annotation/VAR_087101|||http://purl.uniprot.org/annotation/VSP_054553
http://togogenome.org/gene/9606:SIGLEC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYZ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to 6'-sulfo sialyl-Lewis X.|||Cytoplasmic|||Disordered|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Indispensable role in 6'-sulfo sialyl-Lewis X|||Minor effects on binding to 6'-sulfo sialyl-Lewis X.|||Modestly affected binding to 6'-sulfo sialyl-Lewis X.|||N-linked (GlcNAc...) asparagine|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 8|||Strongly impaired binding to 6'-sulfo sialyl-Lewis X.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014948|||http://purl.uniprot.org/annotation/VAR_021487|||http://purl.uniprot.org/annotation/VAR_049930|||http://purl.uniprot.org/annotation/VAR_064751|||http://purl.uniprot.org/annotation/VSP_002559|||http://purl.uniprot.org/annotation/VSP_002560
http://togogenome.org/gene/9606:SULT1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00338                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform Long.|||Phosphoserine|||Proton acceptor|||Sulfotransferase 1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085132|||http://purl.uniprot.org/annotation/VAR_021986|||http://purl.uniprot.org/annotation/VAR_021987|||http://purl.uniprot.org/annotation/VAR_061888|||http://purl.uniprot.org/annotation/VSP_006303
http://togogenome.org/gene/9606:DCAF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6F0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 12|||Disordered|||Phosphoserine|||Reduces association with DDB1.|||Required for nuclear location and interaction with MOV10|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306840|||http://purl.uniprot.org/annotation/VAR_035322
http://togogenome.org/gene/9606:CSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09603                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect production of 150-200 kDa subunit.|||Helical|||In isoform 2.|||In isoform 3.|||Interchain|||Loss of 43 kDa subunit.|||Loss of chondroitin sulfate attachment.|||Lumenal|||Macrophage colony-stimulating factor 1|||Macrophage colony-stimulating factor 1 43 kDa subunit|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphothreonine; by FAM20C|||Polar residues|||Processed macrophage colony-stimulating factor 1|||Produces biologically active protein which is secreted.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005857|||http://purl.uniprot.org/annotation/PRO_0000296231|||http://purl.uniprot.org/annotation/PRO_0000457791|||http://purl.uniprot.org/annotation/VAR_020454|||http://purl.uniprot.org/annotation/VAR_020455|||http://purl.uniprot.org/annotation/VAR_022146|||http://purl.uniprot.org/annotation/VAR_029320|||http://purl.uniprot.org/annotation/VAR_048810|||http://purl.uniprot.org/annotation/VAR_048811|||http://purl.uniprot.org/annotation/VSP_001187|||http://purl.uniprot.org/annotation/VSP_001188
http://togogenome.org/gene/9606:SCN4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ93|||http://purl.uniprot.org/uniprot/Q8IWT1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes regulation of channel activity.|||Cytoplasmic|||Decreases protein stability. Causes conformation changes that impair interaction with the alpha subunit.|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||In ATFB17.|||In LQT10; increase in late sodium current.|||In isoform 2.|||In isoform 3.|||Interchain; with alpha subunit|||N-linked (GlcNAc...) asparagine|||Sodium channel subunit beta-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014937|||http://purl.uniprot.org/annotation/PRO_5014298170|||http://purl.uniprot.org/annotation/VAR_043488|||http://purl.uniprot.org/annotation/VAR_071317|||http://purl.uniprot.org/annotation/VAR_071318|||http://purl.uniprot.org/annotation/VSP_046971|||http://purl.uniprot.org/annotation/VSP_053913
http://togogenome.org/gene/9606:IGFBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08833                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 1|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Phosphotyrosine|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014365|||http://purl.uniprot.org/annotation/VAR_003821|||http://purl.uniprot.org/annotation/VAR_011905|||http://purl.uniprot.org/annotation/VAR_049564
http://togogenome.org/gene/9606:HTR1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30939                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 1F|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068937
http://togogenome.org/gene/9606:AK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6K8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Adenylate kinase 1|||Adenylate kinase 2|||Adenylate kinase isoenzyme 5|||In isoform 2.|||In isoform 3.|||LID 1|||LID 2|||NMP 1|||NMP 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158930|||http://purl.uniprot.org/annotation/VAR_059435|||http://purl.uniprot.org/annotation/VSP_037878|||http://purl.uniprot.org/annotation/VSP_037879
http://togogenome.org/gene/9606:ABITRAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX38                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein Abitram                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291928
http://togogenome.org/gene/9606:DIAPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y5N1|||http://purl.uniprot.org/uniprot/O60610|||http://purl.uniprot.org/uniprot/Q6URC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DAD|||Disordered|||FH1|||FH2|||GBD/FH3|||In DFNA1.|||In DFNA1; with thrombocytopenia; affects function in regulation of cytoskeleton organization.|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Partial decrease of phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein diaphanous homolog 1|||Substantial loss of phosphorylation, no increase of phosphorylation in response to cAMP, increased stability, reduced interaction with OSBPL2 and OSBPL10 and reduced mitochondrial movement.|||Substantial loss of phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194893|||http://purl.uniprot.org/annotation/VAR_078862|||http://purl.uniprot.org/annotation/VAR_079874|||http://purl.uniprot.org/annotation/VSP_035870|||http://purl.uniprot.org/annotation/VSP_035871|||http://purl.uniprot.org/annotation/VSP_035872
http://togogenome.org/gene/9606:FGFR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVP5|||http://purl.uniprot.org/uniprot/J3KPQ0|||http://purl.uniprot.org/uniprot/P22455                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibroblast growth factor receptor|||Fibroblast growth factor receptor 4|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In breast pleomorphic lobular sample; somatic mutation.|||In cancer cells, may be associated with accelerated disease progression and increased tumor cell motility, possibly due to increased stability of the protease MMP14; leads to phosphorylation at residue Y-390, resulting in prolonged FGFR4 activity; increases interaction with STAT3, resulting in STAT3 phosphorylation and signaling activation..|||In isoform 2.|||Loss of interaction with PLCG1.|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; in variant R-388|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016787|||http://purl.uniprot.org/annotation/PRO_5002801024|||http://purl.uniprot.org/annotation/PRO_5003771633|||http://purl.uniprot.org/annotation/VAR_014797|||http://purl.uniprot.org/annotation/VAR_029185|||http://purl.uniprot.org/annotation/VAR_042211|||http://purl.uniprot.org/annotation/VAR_042212|||http://purl.uniprot.org/annotation/VAR_042213|||http://purl.uniprot.org/annotation/VAR_046102|||http://purl.uniprot.org/annotation/VAR_046103|||http://purl.uniprot.org/annotation/VAR_046104|||http://purl.uniprot.org/annotation/VAR_046105|||http://purl.uniprot.org/annotation/VAR_049720|||http://purl.uniprot.org/annotation/VSP_035108
http://togogenome.org/gene/9606:DND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand                                                                                  ^@                                                                                  Dead end protein homolog 1|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081568
http://togogenome.org/gene/9606:CFAP206                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYR0|||http://purl.uniprot.org/uniprot/Q8N771                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 206|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089553|||http://purl.uniprot.org/annotation/VAR_033679|||http://purl.uniprot.org/annotation/VAR_033680
http://togogenome.org/gene/9606:TMEM41A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HV5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 41A|||VTT domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271775
http://togogenome.org/gene/9606:TRIM54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYV2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||COS|||Disordered|||In isoform 2.|||Mediates microtubule-binding and homooligomerization|||RING-type|||Tripartite motif-containing protein 54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056282|||http://purl.uniprot.org/annotation/VSP_016061
http://togogenome.org/gene/9606:HTRA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83105                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||IGFBP N-terminal|||Kazal-like|||PDZ|||Serine protease|||Serine protease HTRA4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026951
http://togogenome.org/gene/9606:CCNI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14094                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-I|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080476|||http://purl.uniprot.org/annotation/VAR_016312|||http://purl.uniprot.org/annotation/VSP_056682
http://togogenome.org/gene/9606:TENT4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9H4DBI9|||http://purl.uniprot.org/uniprot/B7ZLL4|||http://purl.uniprot.org/uniprot/Q5XG87                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Localizes to cytoplasm.|||PAP-associated|||Polar residues|||Polymerase nucleotidyl transferase|||Pro residues|||Terminal nucleotidyltransferase 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120308|||http://purl.uniprot.org/annotation/VAR_021175|||http://purl.uniprot.org/annotation/VAR_021176|||http://purl.uniprot.org/annotation/VSP_053732
http://togogenome.org/gene/9606:NPDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Neural proliferation differentiation and control protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021830
http://togogenome.org/gene/9606:MATCAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCT3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Nucleophile|||Putative tyrosine carboxypeptidase MATCAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320617|||http://purl.uniprot.org/annotation/VSP_031685|||http://purl.uniprot.org/annotation/VSP_031686|||http://purl.uniprot.org/annotation/VSP_031687|||http://purl.uniprot.org/annotation/VSP_043322|||http://purl.uniprot.org/annotation/VSP_043323
http://togogenome.org/gene/9606:GDI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50395                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Rab GDP dissociation inhibitor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056679|||http://purl.uniprot.org/annotation/VSP_043469
http://togogenome.org/gene/9606:COL10A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A650AXN9|||http://purl.uniprot.org/uniprot/Q03692                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C1q|||Collagen alpha-1(X) chain|||Disordered|||In SMCD and spondylometaphyseal dysplasia Japanese type.|||In SMCD.|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005770|||http://purl.uniprot.org/annotation/PRO_5025069452|||http://purl.uniprot.org/annotation/VAR_001838|||http://purl.uniprot.org/annotation/VAR_001839|||http://purl.uniprot.org/annotation/VAR_001840|||http://purl.uniprot.org/annotation/VAR_001841|||http://purl.uniprot.org/annotation/VAR_001842|||http://purl.uniprot.org/annotation/VAR_001843|||http://purl.uniprot.org/annotation/VAR_001844|||http://purl.uniprot.org/annotation/VAR_001845|||http://purl.uniprot.org/annotation/VAR_001846|||http://purl.uniprot.org/annotation/VAR_001847|||http://purl.uniprot.org/annotation/VAR_001848|||http://purl.uniprot.org/annotation/VAR_001849|||http://purl.uniprot.org/annotation/VAR_001850|||http://purl.uniprot.org/annotation/VAR_008039|||http://purl.uniprot.org/annotation/VAR_023186|||http://purl.uniprot.org/annotation/VAR_023187|||http://purl.uniprot.org/annotation/VAR_023188|||http://purl.uniprot.org/annotation/VAR_023189|||http://purl.uniprot.org/annotation/VAR_023190|||http://purl.uniprot.org/annotation/VAR_023191|||http://purl.uniprot.org/annotation/VAR_023192|||http://purl.uniprot.org/annotation/VAR_023193|||http://purl.uniprot.org/annotation/VAR_048767
http://togogenome.org/gene/9606:TRIOBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2D6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with TERF1.|||Basic and acidic residues|||Disordered|||Does not affect interaction with TERF1.|||Does not affect interaction with TERF1. Remains associated with TERF1 at the telomere in late prometaphase cells.|||Essentiel for its aggregation|||In DFNB28.|||In isoform 1.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents the localization of TERF1 to the centrosome.|||TRIO and F-actin-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072433|||http://purl.uniprot.org/annotation/VAR_025719|||http://purl.uniprot.org/annotation/VAR_051412|||http://purl.uniprot.org/annotation/VAR_051413|||http://purl.uniprot.org/annotation/VAR_051414|||http://purl.uniprot.org/annotation/VAR_059725|||http://purl.uniprot.org/annotation/VAR_059726|||http://purl.uniprot.org/annotation/VAR_059727|||http://purl.uniprot.org/annotation/VAR_059728|||http://purl.uniprot.org/annotation/VAR_061708|||http://purl.uniprot.org/annotation/VSP_017711|||http://purl.uniprot.org/annotation/VSP_017712|||http://purl.uniprot.org/annotation/VSP_017713|||http://purl.uniprot.org/annotation/VSP_017714|||http://purl.uniprot.org/annotation/VSP_017715|||http://purl.uniprot.org/annotation/VSP_017716|||http://purl.uniprot.org/annotation/VSP_017717|||http://purl.uniprot.org/annotation/VSP_047498|||http://purl.uniprot.org/annotation/VSP_047499|||http://purl.uniprot.org/annotation/VSP_047500|||http://purl.uniprot.org/annotation/VSP_047501
http://togogenome.org/gene/9606:LSM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0W0|||http://purl.uniprot.org/uniprot/O95777                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylthreonine|||Removed|||Sm|||U6 snRNA-associated Sm-like protein LSm8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125582
http://togogenome.org/gene/9606:MARK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0I6|||http://purl.uniprot.org/uniprot/B4DIB3|||http://purl.uniprot.org/uniprot/Q9P0L2|||http://purl.uniprot.org/uniprot/X5D2M4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Constitutively active.|||Disordered|||Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-698.|||Impairs phospholipid-binding, targeting to membrane and vesicle-binding; when associated with S-701.|||Impairs phospholipid-binding.|||In a gastric adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||KA1|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Phosphothreonine; by LKB1 and TAOK1|||Phosphothreonine; by PKC/PRKCZ|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MARK1|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086298|||http://purl.uniprot.org/annotation/VAR_030018|||http://purl.uniprot.org/annotation/VAR_040760|||http://purl.uniprot.org/annotation/VAR_040761|||http://purl.uniprot.org/annotation/VAR_040762|||http://purl.uniprot.org/annotation/VAR_040763|||http://purl.uniprot.org/annotation/VAR_040764|||http://purl.uniprot.org/annotation/VSP_051702|||http://purl.uniprot.org/annotation/VSP_051703|||http://purl.uniprot.org/annotation/VSP_051704
http://togogenome.org/gene/9606:LILRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JWL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Ig-like|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5035250269
http://togogenome.org/gene/9606:NAIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13075                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 1|||In isoform 2.|||NACHT|||Prevents the proper cleavage of pro-CASP9, but does not inhibit the cleavage of pro-CASP3 by CASP9.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122341|||http://purl.uniprot.org/annotation/VAR_026477|||http://purl.uniprot.org/annotation/VSP_047196|||http://purl.uniprot.org/annotation/VSP_047197
http://togogenome.org/gene/9606:TRPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVI8|||http://purl.uniprot.org/uniprot/O94759|||http://purl.uniprot.org/uniprot/Q14DR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes channel activity.|||Abolishes lowering of temperature threshold for activation in response to reactive oxygen species.|||Basic and acidic residues|||Cytoplasmic|||Decreased channel activity in response to ADP-ribose.|||Decreased channel activity.|||Decreases channel activity.|||Disordered|||Expected to abolish the initially proposed hydrolase activity. Does not abolish channel activity in response to ADP-ribose.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Loss of channel activity.|||Mildly decreases channel activity.|||Moderately decreases channel activity.|||Nearly abolishes channel activity.|||No effect on channel activity.|||No effect on channel activity; when associated with G-1407.|||No effect on channel activity; when associated with Q-1400.|||No significant effect on channel activity; when associated with A-302.|||No significant effect on channel activity; when associated with A-358.|||Nudix box|||Nudix hydrolase|||Only slight effect on activity.|||Pore-forming|||Prevents fast inactivation of the channel.|||Strongly increased residual channel activity after exposure to pH 5.5.|||Strongly reduces channel activity at ph 7.3. Increased residual channel activity after exposure to pH 5.5.|||Transient receptor potential cation channel subfamily M member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215326|||http://purl.uniprot.org/annotation/VAR_020032|||http://purl.uniprot.org/annotation/VAR_025216|||http://purl.uniprot.org/annotation/VAR_025217|||http://purl.uniprot.org/annotation/VAR_025218|||http://purl.uniprot.org/annotation/VAR_025219|||http://purl.uniprot.org/annotation/VAR_025220|||http://purl.uniprot.org/annotation/VAR_025221|||http://purl.uniprot.org/annotation/VAR_025222|||http://purl.uniprot.org/annotation/VAR_025223|||http://purl.uniprot.org/annotation/VAR_025224|||http://purl.uniprot.org/annotation/VAR_025225|||http://purl.uniprot.org/annotation/VAR_025226|||http://purl.uniprot.org/annotation/VAR_025227|||http://purl.uniprot.org/annotation/VSP_006574|||http://purl.uniprot.org/annotation/VSP_006575|||http://purl.uniprot.org/annotation/VSP_013018
http://togogenome.org/gene/9606:ANAPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN47|||http://purl.uniprot.org/uniprot/Q9UJX5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 4|||Anaphase-promoting complex subunit 4 long|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs UBE2S-mediated polyubiquitination, decreasing substrate affinity. Does not affect UBE2C-mediated multiubiquitination.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064595|||http://purl.uniprot.org/annotation/VAR_035792|||http://purl.uniprot.org/annotation/VAR_054044|||http://purl.uniprot.org/annotation/VAR_054045|||http://purl.uniprot.org/annotation/VSP_008464|||http://purl.uniprot.org/annotation/VSP_008465|||http://purl.uniprot.org/annotation/VSP_056708
http://togogenome.org/gene/9606:SGSM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVE3|||http://purl.uniprot.org/uniprot/B9A6J5|||http://purl.uniprot.org/uniprot/Q96HU1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||RUN|||Rab-GAP TBC|||SH3|||Small G protein signaling modulator 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307810|||http://purl.uniprot.org/annotation/VAR_051345|||http://purl.uniprot.org/annotation/VAR_051346|||http://purl.uniprot.org/annotation/VSP_052561
http://togogenome.org/gene/9606:ICAM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6I2|||http://purl.uniprot.org/uniprot/Q9UMF0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In a breast cancer sample; somatic mutation.|||Intercellular adhesion molecule 5|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014799|||http://purl.uniprot.org/annotation/VAR_035515|||http://purl.uniprot.org/annotation/VAR_035516|||http://purl.uniprot.org/annotation/VAR_035517|||http://purl.uniprot.org/annotation/VAR_056046|||http://purl.uniprot.org/annotation/VAR_056047
http://togogenome.org/gene/9606:DTX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Probable E3 ubiquitin-protein ligase DTX2|||RING-type|||WWE 1|||WWE 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219083|||http://purl.uniprot.org/annotation/VAR_016920|||http://purl.uniprot.org/annotation/VAR_016921|||http://purl.uniprot.org/annotation/VAR_016922|||http://purl.uniprot.org/annotation/VSP_008350
http://togogenome.org/gene/9606:XRCC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13426|||http://purl.uniprot.org/uniprot/Q7Z763                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished DNA-binding.|||Abolished ability mediate double-strand break repair; impaired nuclear localization.|||Abolished ability to bridge DNA; when associated with E-72 and E-99.|||Abolished cleavage by caspase and ability to regulate phospholipid scramblase activity.|||Abolished interaction with NHEJ1/XLF.|||Abolished interaction with NHEJ1/XLF; when associated with E-4 or E-26 or E-65 or E-71 or E-72. Abolished ability to bridge DNA; when associated with E-65. Abolished ability to bridge DNA; when associated with E-72 and E-90.|||Abolished interaction with NHEJ1/XLF; when associated with E-65.|||Abolished interaction with NHEJ1/XLF; when associated with E-99.|||Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-90 and E-99.|||Abolished nuclear localization of XRCC4 and LIG4. Impaired ability to repair DNA double-strand breaks (DSBs). Reduced ubiquitination by the SCF(FBXW7) complex caused by impaired localization to the nucleus.|||Abolished phosphorylation by CK2, leading to strongly reduced interaction with PNKP.|||Abolished ubiquitination by the SCF(FBXW7) complex.|||Abolishes sumoylation. 5-fold decrease in recombination efficiency. Does not affect nuclear localization of XRCC4 and LIG4.|||Basic and acidic residues|||Cleavage; by caspase-3|||DNA repair protein XRCC4|||Disordered|||Does not affect ability mediate double-strand break repair.|||Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-323 and D-327.|||Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-323 and D-328.|||Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-320, D-327 and D-328.|||Does not affect ability to localize into the nucleus.|||Does not affect interaction with NHEJ1/XLF.|||Does not affect phosphorylation by CK2.|||Does not affect ubiquitination by the SCF(FBXW7) complex.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ability mediate double-strand break repair.|||Impaired ability to localize in the nucleus, without affecting ability to activate phospholipid scramblase activity of XKR4.|||Impaired ability to localize in the nucleus.|||In 2DA; abolished cleavage by caspase and ability to regulate phospholipid scramblase activity.|||In SSMED.|||In SSMED; impaired ability to repair DNA double-strand breaks.|||In SSMED; impairs the protein function in DNA double-strand break repair.|||In SSMED; no expression of the protein is observed; complete loss of function in DNA double-strand break repair.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-323 and A-327.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-323 and A-328.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-320, A-327 and A-328. Does not affect phosphorylation by CK2.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-320, A-323, A-327 and A-328.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-315, A-320, A-323, A-327 and A-328.|||In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-260, A-304, A-315, A-320, A-323, A-327 and A-328.|||In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-315, D-323, D-327 and D-328.|||In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-304, D-320, D-323, D-327 and D-328.|||In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-260, D-315, D-320, D-323, D-327 and D-328.|||In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-304, D-315, D-320, D-323, D-327 and D-328.|||In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-260, D-304, D-315, D-320, D-323, D-327 and D-328.|||In isoform 2.|||In isoform 3.|||Interaction with IFFO1|||Interaction with LIG4|||No change in sumoylation.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine; by CK2|||Phosphothreonine; by PRKDC|||Phosphotyrosine|||Polar residues|||Protein XRCC4, C-terminus|||Reduced phosphorylation by PRKDC. In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-304, A-315, A-320, A-323, A-327 and A-328.|||Reduced ubiquitination by the SCF(FBXW7) complex.|||Slightly reduced phosphorylation by PRKDC. In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-260, A-304, A-315, A-323, A-327 and A-328.|||Strongly decreased interaction with NHEJ1/XLF. Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-99. Abolished interaction with NHEJ1/XLF; when associated with E-102. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066047|||http://purl.uniprot.org/annotation/PRO_0000453296|||http://purl.uniprot.org/annotation/VAR_017810|||http://purl.uniprot.org/annotation/VAR_017811|||http://purl.uniprot.org/annotation/VAR_022310|||http://purl.uniprot.org/annotation/VAR_022311|||http://purl.uniprot.org/annotation/VAR_022312|||http://purl.uniprot.org/annotation/VAR_022313|||http://purl.uniprot.org/annotation/VAR_075822|||http://purl.uniprot.org/annotation/VAR_075823|||http://purl.uniprot.org/annotation/VAR_084965|||http://purl.uniprot.org/annotation/VAR_084966|||http://purl.uniprot.org/annotation/VAR_084967|||http://purl.uniprot.org/annotation/VAR_084968|||http://purl.uniprot.org/annotation/VAR_084969|||http://purl.uniprot.org/annotation/VSP_009473|||http://purl.uniprot.org/annotation/VSP_009474
http://togogenome.org/gene/9606:BET1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DH16|||http://purl.uniprot.org/uniprot/Q9NYM9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BET1-like protein|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Lumenal|||Phosphoserine|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233056
http://togogenome.org/gene/9606:SPACA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/W5XKT8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sperm acrosome membrane-associated protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000434003|||http://purl.uniprot.org/annotation/VSP_057868|||http://purl.uniprot.org/annotation/VSP_057869|||http://purl.uniprot.org/annotation/VSP_057870|||http://purl.uniprot.org/annotation/VSP_057871
http://togogenome.org/gene/9606:GIGYF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Y7W6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  4EHP-binding motif|||Abolishes interaction with DDX6.|||Abolishes interaction with DDX6; when associated with A-300.|||Abolishes interaction with DDX6; when associated with A-306.|||Abolishes interaction with EIF4E2.|||Basic and acidic residues|||DDX6 binding motif|||Disordered|||GRB10-interacting GYF protein 2|||GYF|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In PARK11.|||In PARK11; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||May be associated with PARK11.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Required for GRB10-binding|||Required for interaction with SARS-CoV-2 non-structural protein 2 (nsp2)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270837|||http://purl.uniprot.org/annotation/VAR_044439|||http://purl.uniprot.org/annotation/VAR_044440|||http://purl.uniprot.org/annotation/VAR_044441|||http://purl.uniprot.org/annotation/VAR_044442|||http://purl.uniprot.org/annotation/VAR_044443|||http://purl.uniprot.org/annotation/VAR_044444|||http://purl.uniprot.org/annotation/VAR_044445|||http://purl.uniprot.org/annotation/VAR_044446|||http://purl.uniprot.org/annotation/VAR_044447|||http://purl.uniprot.org/annotation/VAR_044448|||http://purl.uniprot.org/annotation/VAR_044449|||http://purl.uniprot.org/annotation/VAR_051268|||http://purl.uniprot.org/annotation/VAR_077935|||http://purl.uniprot.org/annotation/VAR_077936|||http://purl.uniprot.org/annotation/VAR_077937|||http://purl.uniprot.org/annotation/VAR_077938|||http://purl.uniprot.org/annotation/VAR_077939|||http://purl.uniprot.org/annotation/VAR_077940|||http://purl.uniprot.org/annotation/VAR_077941|||http://purl.uniprot.org/annotation/VAR_077942|||http://purl.uniprot.org/annotation/VAR_077943|||http://purl.uniprot.org/annotation/VAR_077944|||http://purl.uniprot.org/annotation/VAR_077945|||http://purl.uniprot.org/annotation/VAR_077946|||http://purl.uniprot.org/annotation/VAR_077947|||http://purl.uniprot.org/annotation/VAR_077948|||http://purl.uniprot.org/annotation/VAR_077949|||http://purl.uniprot.org/annotation/VSP_022244|||http://purl.uniprot.org/annotation/VSP_043471|||http://purl.uniprot.org/annotation/VSP_044996|||http://purl.uniprot.org/annotation/VSP_044997
http://togogenome.org/gene/9606:LCNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZST4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Lipocalin-like 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348470|||http://purl.uniprot.org/annotation/VAR_046189
http://togogenome.org/gene/9606:KRAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I1SRC5|||http://purl.uniprot.org/uniprot/P01116                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL|||Abolished interaction with GPR131.|||Abolished palmitoylation on Cys; reduced palmitoylation on Lys residues.|||Cysteine methyl ester|||Effector region|||Found in a patient with Costello syndrome, exhibits an increase in intrinsic and guanine nucleotide exchange factor catalyzed nucleotide exchange in combination with an impaired GTPase-activating protein-stimulated GTP hydrolysis but functional in interaction with effectors.|||GTPase KRas|||GTPase KRas, N-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||Hypervariable region|||In AML; expression in 3T3 cell causes cellular transformation; expression in COS cells activates the Ras-MAPK signaling pathway; lower GTPase activity; faster GDP dissociation rate.|||In CFC2 and NS3, exhibits only minor alterations in its in vitro biochemical behavior compared to wild-type protein.|||In CFC2.|||In CFC2; characterized by a defective GTPase-activating protein sensitivity and a strongly reduced interaction with effectors.|||In CFC2; exhibits an increase in intrinsic and guanine nucleotide exchange factor catalyzed nucleotide exchange in combination with an impaired GTPase-activating protein-stimulated GTP hydrolysis but functional in interaction with effectors.|||In GASC and JMML; also found in lung carcinoma; somatic mutation.|||In GASC, JMML and OES; also found in a breast carcinoma cell line; somatic mutation.|||In GASC, JMML and SFM; somatic mutation; also found in pancreatic carcinoma and lung carcinoma; also found in metastatic colorectal cancer.|||In GASC; also found in bladder cancer; somatic mutation.|||In GASC; also found in lung carcinoma, pancreatic carcinoma and colon cancer; also found in metastatic colorectal cancer; somatic mutation; it is constitutively activated and stimulates transcription activation of tumor suppressor genes in non-transformed fibroblasts.|||In GASC; found also in a patient with Costello syndrome; exhibits only minor alterations in its in vitro biochemical behavior compared to wild-type protein.|||In K-Ras-3KR; abolished lysine-palmitoylation.|||In NS3.|||In NS3/CFC2.|||In NS3; affects activity and impairs responsiveness to GTPase activating proteins; characterized by a strong increase of both intrinsic and guanine nucleotide exchanged factor-catalyzed nucleotide exchange leading to an increased level of the activated state.|||In NS3; affects activity and impairs responsiveness to GTPase activating proteins; exhibits only minor alterations in its in vitro biochemical behavior compared to wild-type protein.|||In NS3; characterized by a defective GTPase-activating protein sensitivity and a strongly reduced interaction with effectors.|||In NS3; impairs GTPase-activating protein stimulated GTP hydrolysis with unaffected intrinsic functions and a virtually functional effector interaction.|||In OES; somatic mutation.|||In OES; somatic mutation; also found in colorectal cancer samples.|||In a colorectal cancer sample; somatic mutation.|||In colorectal cancer samples; somatic mutation.|||In isoform 2B.|||In lung cancer and bladder cancer; somatic mutation.|||In lung carcinoma.|||In lung carcinoma; somatic mutation; also found in metastatic colorectal cancer.|||In pylocytic astrocytoma; somatic mutation; increase activation of the Ras pathway.|||N-acetylmethionine; in GTPase KRas; alternate|||N-acetylthreonine; in GTPase KRas, N-terminally processed|||N6-acetyllysine|||N6-palmitoyl lysine|||Removed in mature form|||Removed; alternate|||S-farnesyl cysteine|||S-palmitoyl cysteine|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082641|||http://purl.uniprot.org/annotation/PRO_0000281291|||http://purl.uniprot.org/annotation/PRO_0000326480|||http://purl.uniprot.org/annotation/VAR_006839|||http://purl.uniprot.org/annotation/VAR_006840|||http://purl.uniprot.org/annotation/VAR_006841|||http://purl.uniprot.org/annotation/VAR_016026|||http://purl.uniprot.org/annotation/VAR_016027|||http://purl.uniprot.org/annotation/VAR_016028|||http://purl.uniprot.org/annotation/VAR_016029|||http://purl.uniprot.org/annotation/VAR_016030|||http://purl.uniprot.org/annotation/VAR_026109|||http://purl.uniprot.org/annotation/VAR_026110|||http://purl.uniprot.org/annotation/VAR_026111|||http://purl.uniprot.org/annotation/VAR_026112|||http://purl.uniprot.org/annotation/VAR_034601|||http://purl.uniprot.org/annotation/VAR_036305|||http://purl.uniprot.org/annotation/VAR_036306|||http://purl.uniprot.org/annotation/VAR_036307|||http://purl.uniprot.org/annotation/VAR_036308|||http://purl.uniprot.org/annotation/VAR_064849|||http://purl.uniprot.org/annotation/VAR_064850|||http://purl.uniprot.org/annotation/VAR_064851|||http://purl.uniprot.org/annotation/VAR_064852|||http://purl.uniprot.org/annotation/VAR_064853|||http://purl.uniprot.org/annotation/VAR_064854|||http://purl.uniprot.org/annotation/VAR_065144|||http://purl.uniprot.org/annotation/VAR_065145|||http://purl.uniprot.org/annotation/VAR_065146|||http://purl.uniprot.org/annotation/VAR_069784|||http://purl.uniprot.org/annotation/VAR_069785|||http://purl.uniprot.org/annotation/VAR_082908|||http://purl.uniprot.org/annotation/VAR_082909|||http://purl.uniprot.org/annotation/VAR_082910|||http://purl.uniprot.org/annotation/VAR_082911|||http://purl.uniprot.org/annotation/VAR_083261|||http://purl.uniprot.org/annotation/VAR_083262|||http://purl.uniprot.org/annotation/VSP_011140|||http://purl.uniprot.org/annotation/VSP_011141
http://togogenome.org/gene/9606:FAU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62861                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes FUBI-ribosomal protein S30 processing. Impairs 40S ribosome biogenesis.|||Abolishes FUBI-ribosomal protein S30 processing; when associated with A-73. Impairs 40S ribosome biogenesis.|||Abolishes FUBI-ribosomal protein S30 processing; when associated with A-74. Impairs 40S ribosome biogenesis.|||Basic residues|||Disordered|||N6-succinyllysine|||Small ribosomal subunit protein eS30|||Ubiquitin-like|||Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein|||Ubiquitin-like protein FUBI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173999|||http://purl.uniprot.org/annotation/PRO_0000455003|||http://purl.uniprot.org/annotation/PRO_0000455004|||http://purl.uniprot.org/annotation/VAR_019643|||http://purl.uniprot.org/annotation/VAR_019644
http://togogenome.org/gene/9606:POU2AF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16633                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||OCA|||POU domain class 2-associating factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058018|||http://purl.uniprot.org/annotation/VAR_005521|||http://purl.uniprot.org/annotation/VAR_005522
http://togogenome.org/gene/9606:ZDHHC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0B5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Extracellular|||Helical|||In isoform 2.|||More than 50% loss of FYN-mediated phosphorylation.|||More than 50% loss of activity.|||Omega-N-methylarginine|||Palmitoyltransferase ZDHHC5|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by FYN|||Phosphotyrosine; by LYN|||Polar residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212868|||http://purl.uniprot.org/annotation/VSP_006935
http://togogenome.org/gene/9606:RBM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1T9|||http://purl.uniprot.org/uniprot/J3KPD3|||http://purl.uniprot.org/uniprot/Q9Y580                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-50 and A-52. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-50 and A-52. Does not affect interaction with MEPCE and LARP7; when associated with A-50 and A-52. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-50 and A-52.|||Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-52 and A-54. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-52 and A-54. Does not affect interaction with MEPCE and LARP7; when associated with A-52 and A-54. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-52 and A-54.|||Basic and acidic residues|||Decreases affinity for RNA binding. Abrogates the interaction with 7SK small nuclear RNA (7SK); when associated with A-50 and A-54. Does not affect interaction between HEXIM1, CDK9 and 7SK small nuclear RNA (7SK); when associated with A-50 and A-54. Does not affect interaction with MEPCE and LARP7; when associated with A-50 and A-54. Decreases induction of P-TEFb-dependent DNA damage response (DDR); when associated with A-50 and A-54.|||Decreases affinity for RNA binding. Does not affect The NEXT complex assembly. Impairs snRNA binding.|||Disordered|||Found in a patient with a form of spinal muscular atrophy; unknown pathological significance.|||Impaired interaction with ZCCHC8; when associated with E-25.|||Impaired interaction with ZCCHC8; when associated with E-29.|||Impairs phosphorylation. Impairs phosphorylation; when associated with S-136.|||Impairs phosphorylation. Impairs phosphorylation; when associated with S-204. Prevents PROMPTs accumulation to >50%.|||N-acetylglycine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA-binding protein 7|||RRM|||Reduced interaction with ZCCHC8, and impaired interaction with SF3B2/SAP145; when associated with A-65.|||Reduced interaction with ZCCHC8, and impaired interaction with SF3B2/SAP145; when associated with E-69.|||Removed|||ZCCHC8 binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081761|||http://purl.uniprot.org/annotation/VAR_082580
http://togogenome.org/gene/9606:UBL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95164                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Cysteine methyl ester|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||Ubiquitin-like|||Ubiquitin-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114862|||http://purl.uniprot.org/annotation/PRO_0000248183
http://togogenome.org/gene/9606:FBXO31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGU8|||http://purl.uniprot.org/uniprot/Q5XUX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 31|||Fails to accumulate following gamma-irradiation.|||In isoform 2.|||No effect following gamma-irradiation.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119921|||http://purl.uniprot.org/annotation/VSP_037469
http://togogenome.org/gene/9606:CEBPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49715                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||CCAAT/enhancer-binding protein alpha|||Decreased interaction with TRIB1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In AML; no effect on expression; no effect on DNA-binding or transactivation activity.|||In AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with FOXO1|||Leucine-zipper|||N6-acetyllysine; alternate|||No effect on interaction with TRIB1.|||Phosphoserine|||Phosphoserine; by GSK3|||Phosphothreonine; by GSK3|||Pro residues|||Required for interaction with TRIB1|||Required to functionally cooperate with SREBF1 in promoter activation|||Required to induce adipocyte differentiation|||Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiation|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076613|||http://purl.uniprot.org/annotation/VAR_072677|||http://purl.uniprot.org/annotation/VAR_072678|||http://purl.uniprot.org/annotation/VSP_057547|||http://purl.uniprot.org/annotation/VSP_057548|||http://purl.uniprot.org/annotation/VSP_057607
http://togogenome.org/gene/9606:COX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL88|||http://purl.uniprot.org/uniprot/Q8N8Q8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX18, mitochondrial|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Membrane insertase YidC/Oxa/ALB C-terminal|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020354|||http://purl.uniprot.org/annotation/VSP_022311|||http://purl.uniprot.org/annotation/VSP_022312|||http://purl.uniprot.org/annotation/VSP_022313|||http://purl.uniprot.org/annotation/VSP_022314|||http://purl.uniprot.org/annotation/VSP_022315|||http://purl.uniprot.org/annotation/VSP_022316
http://togogenome.org/gene/9606:NLRC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZW3|||http://purl.uniprot.org/uniprot/Q86WI3|||http://purl.uniprot.org/uniprot/Q9H6Y0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 25|||LRR 26|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NACHT LRR and PYD|||Protein NLRC5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296189|||http://purl.uniprot.org/annotation/VAR_034607|||http://purl.uniprot.org/annotation/VAR_034608|||http://purl.uniprot.org/annotation/VAR_034609|||http://purl.uniprot.org/annotation/VAR_034610|||http://purl.uniprot.org/annotation/VAR_034611|||http://purl.uniprot.org/annotation/VAR_034612|||http://purl.uniprot.org/annotation/VAR_034613|||http://purl.uniprot.org/annotation/VAR_036388|||http://purl.uniprot.org/annotation/VAR_060589|||http://purl.uniprot.org/annotation/VSP_027150|||http://purl.uniprot.org/annotation/VSP_027151|||http://purl.uniprot.org/annotation/VSP_027152|||http://purl.uniprot.org/annotation/VSP_027153|||http://purl.uniprot.org/annotation/VSP_027154|||http://purl.uniprot.org/annotation/VSP_027155|||http://purl.uniprot.org/annotation/VSP_027156|||http://purl.uniprot.org/annotation/VSP_027157
http://togogenome.org/gene/9606:TNFAIP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98066                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to bikunin.|||Abolishes binding to bikunin. Has no effect on transesterification reaction.|||Abolishes binding to bikunin. Impairs binding of hyaluronan to CD44. Decreases hyaluronan-dependent lymphocyte rolling. Has no effect on transesterification reaction.|||Abolishes binding to bikunin. Impairs binding to hyaluronan. Retains the ability to bind heavy chains but cannot transfer them onto hyaluronan. Impairs binding of hyaluronan to CD44. Decreases hyaluronan-dependent lymphocyte rolling.|||CUB|||Decreases binding of hyaluronan to CD44. Decreases hyaluronan-dependent lymphocyte rolling.|||Decreases binding to heparin. Has normal binding to bikunin.|||Decreases binding to heparin. Has normal binding to bikunin. Impairs binding to heparin and decreases the potentiation effect toward bikunin antiprotease activity; when associated with A-55 and A-69. Has no effect on CXCL8-induced neutrophil transmigration; when associated with A-55 and A-69.|||Decreases binding to heparin. Has normal binding to bikunin. Impairs binding to heparin; when associated with A-55 and A-76. Has no effect on CXCL8-induced neutrophil transmigration; when associated with A-55 and A-76.|||Decreases binding to heparin. Has normal binding to bikunin. Impairs binding to heparin; when associated with A-69 and A-76. Has no effect on CXCL8-induced neutrophil transmigration; when associated with A-69 and A-76.|||Has no significant effect on hyaluronan binding to CD44 or hyaluronan-dependent lymphocyte rolling.|||Impairs binding of hyaluronan to CD44. Decreases hyaluronan-dependent lymphocyte rolling.|||Increases binding of hyaluronan to CD44. Has no significant effect on hyaluronan-dependent lymphocyte rolling.|||Link|||N-linked (GlcNAc...) asparagine|||Reduces the binding affinity to calcium ions. Abolishes the interaction with heavy chain ITIH1.|||Tumor necrosis factor-inducible gene 6 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026692|||http://purl.uniprot.org/annotation/VAR_013005
http://togogenome.org/gene/9606:ZNF169                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14929                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 169                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047438|||http://purl.uniprot.org/annotation/VAR_024198|||http://purl.uniprot.org/annotation/VAR_024199|||http://purl.uniprot.org/annotation/VAR_059065|||http://purl.uniprot.org/annotation/VAR_059066|||http://purl.uniprot.org/annotation/VAR_059067
http://togogenome.org/gene/9606:MINDY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8M7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Ubiquitin carboxyl-terminal hydrolase MINDY-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317560|||http://purl.uniprot.org/annotation/VSP_031039
http://togogenome.org/gene/9606:SLC51B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UW2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Organic solute transporter subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331554
http://togogenome.org/gene/9606:GOSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQE0|||http://purl.uniprot.org/uniprot/A0A1W2PR02|||http://purl.uniprot.org/uniprot/A0A1W2PRL0|||http://purl.uniprot.org/uniprot/I3NI02|||http://purl.uniprot.org/uniprot/O14653                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Golgi SNAP receptor complex member 2|||Helical|||Helical; Anchor for type IV membrane protein|||In EPM6 and MYOS; no effect on protein stability; loss of localization to the cis-Golgi network membrane; loss of function; unable to rescue the yeast strain lacking the ortholog Bos1.|||In MYOS.|||In isoform 3.|||In isoform B.|||IxM motif; signal for cargo packaging into COPII-coated vesicles|||Loss of interaction with SEC24C.|||N-acetylmethionine|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212549|||http://purl.uniprot.org/annotation/VAR_024471|||http://purl.uniprot.org/annotation/VAR_065833|||http://purl.uniprot.org/annotation/VAR_087912|||http://purl.uniprot.org/annotation/VAR_087913|||http://purl.uniprot.org/annotation/VSP_001829|||http://purl.uniprot.org/annotation/VSP_043200
http://togogenome.org/gene/9606:CSF1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07333                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes down-regulation of activated CSF1R.|||Activation loop|||Constitutive kinase activity.|||Constitutive kinase activity. Loss of inhibition by imatinib.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Impairs degradation of activated CSF1R.|||In BANDDOS.|||In BANDDOS; impairs phosphorylation of JNK kinases upon stimulation with CSF1.|||In HDLS1.|||In HDLS1; impairs autophosphorylation upon stimulation with CSF1.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||Macrophage colony-stimulating factor 1 receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced kinase activity. Reduced interaction with SRC, FYN and YES1.|||Regulatory juxtamembrane domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016765|||http://purl.uniprot.org/annotation/VAR_011953|||http://purl.uniprot.org/annotation/VAR_042038|||http://purl.uniprot.org/annotation/VAR_042039|||http://purl.uniprot.org/annotation/VAR_042040|||http://purl.uniprot.org/annotation/VAR_042041|||http://purl.uniprot.org/annotation/VAR_042042|||http://purl.uniprot.org/annotation/VAR_042043|||http://purl.uniprot.org/annotation/VAR_042044|||http://purl.uniprot.org/annotation/VAR_049718|||http://purl.uniprot.org/annotation/VAR_061290|||http://purl.uniprot.org/annotation/VAR_067396|||http://purl.uniprot.org/annotation/VAR_067397|||http://purl.uniprot.org/annotation/VAR_067398|||http://purl.uniprot.org/annotation/VAR_067399|||http://purl.uniprot.org/annotation/VAR_067400|||http://purl.uniprot.org/annotation/VAR_067401|||http://purl.uniprot.org/annotation/VAR_067402|||http://purl.uniprot.org/annotation/VAR_067403|||http://purl.uniprot.org/annotation/VAR_067404|||http://purl.uniprot.org/annotation/VAR_067405|||http://purl.uniprot.org/annotation/VAR_067406|||http://purl.uniprot.org/annotation/VAR_067407|||http://purl.uniprot.org/annotation/VAR_067408|||http://purl.uniprot.org/annotation/VAR_067409|||http://purl.uniprot.org/annotation/VAR_067410|||http://purl.uniprot.org/annotation/VAR_067411|||http://purl.uniprot.org/annotation/VAR_072081|||http://purl.uniprot.org/annotation/VAR_072082|||http://purl.uniprot.org/annotation/VAR_072083|||http://purl.uniprot.org/annotation/VAR_083140|||http://purl.uniprot.org/annotation/VAR_083141|||http://purl.uniprot.org/annotation/VAR_083142|||http://purl.uniprot.org/annotation/VAR_083143|||http://purl.uniprot.org/annotation/VAR_083144|||http://purl.uniprot.org/annotation/VAR_083145|||http://purl.uniprot.org/annotation/VAR_083146|||http://purl.uniprot.org/annotation/VAR_083147|||http://purl.uniprot.org/annotation/VSP_047757|||http://purl.uniprot.org/annotation/VSP_047758
http://togogenome.org/gene/9606:NR0B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8P4|||http://purl.uniprot.org/uniprot/P51843                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4 X 67 AA tandem repeats|||4; truncated|||AF-2 motif|||In AHC.|||In AHC; impairs RNA-binding activity.|||In AHC; impairs transcriptional silencing of the StAR promoter.|||In AHC; mild phenotype.|||In AHC; results in a severe loss of repressor activity.|||In AHC; the patient presents an inappropriate tall stature and renal ectopy.|||In isoform 2.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||NR LBD|||Nuclear receptor subfamily 0 group B member 1|||Strongly reduces homodimerization and interaction with NR0B2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053748|||http://purl.uniprot.org/annotation/VAR_004738|||http://purl.uniprot.org/annotation/VAR_004739|||http://purl.uniprot.org/annotation/VAR_004740|||http://purl.uniprot.org/annotation/VAR_004741|||http://purl.uniprot.org/annotation/VAR_004742|||http://purl.uniprot.org/annotation/VAR_004743|||http://purl.uniprot.org/annotation/VAR_004744|||http://purl.uniprot.org/annotation/VAR_004745|||http://purl.uniprot.org/annotation/VAR_004746|||http://purl.uniprot.org/annotation/VAR_018300|||http://purl.uniprot.org/annotation/VAR_018301|||http://purl.uniprot.org/annotation/VAR_018302|||http://purl.uniprot.org/annotation/VAR_018303|||http://purl.uniprot.org/annotation/VAR_018304|||http://purl.uniprot.org/annotation/VAR_018305|||http://purl.uniprot.org/annotation/VAR_018306|||http://purl.uniprot.org/annotation/VAR_031079|||http://purl.uniprot.org/annotation/VAR_031080|||http://purl.uniprot.org/annotation/VAR_031081|||http://purl.uniprot.org/annotation/VSP_023557|||http://purl.uniprot.org/annotation/VSP_023558
http://togogenome.org/gene/9606:CCDC115                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZ99|||http://purl.uniprot.org/uniprot/Q96NT0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 115|||Disordered|||In CDG2O.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279403|||http://purl.uniprot.org/annotation/VAR_075752|||http://purl.uniprot.org/annotation/VAR_075753|||http://purl.uniprot.org/annotation/VSP_056115|||http://purl.uniprot.org/annotation/VSP_056116
http://togogenome.org/gene/9606:NABP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Enhances ATM-dependent signaling.|||In isoform 2.|||Loss of phosphorylation by ATM.|||OB|||Phosphothreonine; by ATM|||Polar residues|||Pro residues|||SOSS complex subunit B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333958|||http://purl.uniprot.org/annotation/VSP_033604
http://togogenome.org/gene/9606:ZNF227                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6M2|||http://purl.uniprot.org/uniprot/Q658S5|||http://purl.uniprot.org/uniprot/Q86WZ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 227                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047468|||http://purl.uniprot.org/annotation/VSP_056544
http://togogenome.org/gene/9606:OR6V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWQ4|||http://purl.uniprot.org/uniprot/Q8N148                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6V1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150639|||http://purl.uniprot.org/annotation/VAR_034251|||http://purl.uniprot.org/annotation/VAR_034252|||http://purl.uniprot.org/annotation/VAR_034253
http://togogenome.org/gene/9606:STAU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRE0|||http://purl.uniprot.org/uniprot/O95793|||http://purl.uniprot.org/uniprot/Q59F99|||http://purl.uniprot.org/uniprot/Q6PJX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||Disordered|||Double-stranded RNA-binding protein Staufen homolog 1|||In isoform 3.|||In isoform Short and isoform 3.|||N-acetylserine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072243|||http://purl.uniprot.org/annotation/PRO_5004252468|||http://purl.uniprot.org/annotation/VSP_004434|||http://purl.uniprot.org/annotation/VSP_043701
http://togogenome.org/gene/9606:RAMAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Interaction with RNMT|||N-acetylthreonine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA guanine-N7 methyltransferase activating subunit|||RNA-binding|||RNMT-activating domain|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089983
http://togogenome.org/gene/9606:ARHGAP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1RLN5|||http://purl.uniprot.org/uniprot/Q8IWW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 12|||Rho-GAP|||SH3|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056713|||http://purl.uniprot.org/annotation/VAR_024454|||http://purl.uniprot.org/annotation/VSP_010326|||http://purl.uniprot.org/annotation/VSP_010327|||http://purl.uniprot.org/annotation/VSP_010328
http://togogenome.org/gene/9606:BOLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3K6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  BolA-like protein 2|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201236|||http://purl.uniprot.org/annotation/VSP_010092|||http://purl.uniprot.org/annotation/VSP_010093
http://togogenome.org/gene/9606:LITAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99732                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes association with cytoplasmic vesicle membranes.|||Abolishes interaction with NEDD4.|||Abolishes interaction with TSG101.|||Abolishes interaction with WWOX. Abolishes interaction with NEDD4. Abolishes interaction with NEDD4 and impairs location at endosomes; when associated with A-61.|||Decreases protein stability and association with early endosome membranes. Impaired function in targeting endocytosed proteins for lysosomal degradation.|||Disordered|||Found as a somatic mutation in a EMPD primary tumor.|||Impaired function in targeting endocytosed proteins for lysosomal degradation.|||In CMT1C.|||In CMT1C; decreases protein stability and association with early endosome membranes; impaired function in targeting endocytosed proteins for lysosomal degradation; does not abolish interaction with NEDD4 and TSG101.|||In CMT1C; does not abolish interaction with NEDD4 and TSG101.|||In isoform 2.|||In isoform 3.|||In one EMPD primary tumor; somatic mutation.|||LITAF|||Lipopolysaccharide-induced tumor necrosis factor-alpha factor|||Membrane-binding amphipathic helix|||No effect on interaction with WWOX. No effect on interaction with NEDD4. Abolishes interaction with NEDD4 and impairs location at endosomes; when associated with A-23.|||No effect on location at endosomes, but impairs protein stability.|||PPxY motif|||PSAP motif; important for interaction with TSG101|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084440|||http://purl.uniprot.org/annotation/VAR_024014|||http://purl.uniprot.org/annotation/VAR_024015|||http://purl.uniprot.org/annotation/VAR_024016|||http://purl.uniprot.org/annotation/VAR_024017|||http://purl.uniprot.org/annotation/VAR_024018|||http://purl.uniprot.org/annotation/VAR_024019|||http://purl.uniprot.org/annotation/VAR_024020|||http://purl.uniprot.org/annotation/VAR_082859|||http://purl.uniprot.org/annotation/VSP_016461|||http://purl.uniprot.org/annotation/VSP_045701
http://togogenome.org/gene/9606:FRY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TBA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Phosphothreonine; by CDK1|||Phosphotyrosine|||Polar residues|||Protein furry homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281674|||http://purl.uniprot.org/annotation/VAR_053831
http://togogenome.org/gene/9606:SBDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5I7|||http://purl.uniprot.org/uniprot/Q9Y3A5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In SDS1.|||In SDS1; strongly reduced release of EIF6 from pre-60S ribosome subunits.|||In SDS1; unknown pathological significance.|||N-acetylserine|||Removed|||Ribosome maturation protein SBDS|||Ribosome maturation protein SDO1/SBDS C-terminal|||Ribosome maturation protein SDO1/SBDS N-terminal|||Ribosome maturation protein SDO1/SBDS central|||Strongly reduced release of EIF6 from pre-60S ribosome subunits.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123762|||http://purl.uniprot.org/annotation/VAR_015390|||http://purl.uniprot.org/annotation/VAR_015391|||http://purl.uniprot.org/annotation/VAR_015392|||http://purl.uniprot.org/annotation/VAR_015393|||http://purl.uniprot.org/annotation/VAR_015394|||http://purl.uniprot.org/annotation/VAR_015395|||http://purl.uniprot.org/annotation/VAR_015396|||http://purl.uniprot.org/annotation/VAR_071673
http://togogenome.org/gene/9606:CELF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YX66|||http://purl.uniprot.org/uniprot/A0A0J9YXJ0|||http://purl.uniprot.org/uniprot/A0A1B0GU44|||http://purl.uniprot.org/uniprot/A0A1B0GUN8|||http://purl.uniprot.org/uniprot/B4DDE7|||http://purl.uniprot.org/uniprot/B4DIB6|||http://purl.uniprot.org/uniprot/B4DT00|||http://purl.uniprot.org/uniprot/B4DZ01|||http://purl.uniprot.org/uniprot/E9PC62|||http://purl.uniprot.org/uniprot/O95319                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUGBP Elav-like family member 2|||Disordered|||In DEE97; mislocalized to the cytoplasm.|||In DEE97; unknown pathological significance; mislocalized to the cytoplasm.|||In isoform 2 and isoform 4.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusion|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295189|||http://purl.uniprot.org/annotation/VAR_052202|||http://purl.uniprot.org/annotation/VAR_086490|||http://purl.uniprot.org/annotation/VAR_086491|||http://purl.uniprot.org/annotation/VSP_026796|||http://purl.uniprot.org/annotation/VSP_026797|||http://purl.uniprot.org/annotation/VSP_026798|||http://purl.uniprot.org/annotation/VSP_026799|||http://purl.uniprot.org/annotation/VSP_026800
http://togogenome.org/gene/9606:TMEM108                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT64|||http://purl.uniprot.org/uniprot/Q6UXF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Interaction with CYFIP2|||Interaction with DST (isoform 1)|||Interaction with SH3GL2|||Polar residues|||Transmembrane protein 108                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243913|||http://purl.uniprot.org/annotation/PRO_5014567664|||http://purl.uniprot.org/annotation/VAR_051427|||http://purl.uniprot.org/annotation/VSP_019494|||http://purl.uniprot.org/annotation/VSP_019495
http://togogenome.org/gene/9606:PHACTR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphatase and actin regulator 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RPEL 1|||RPEL 2|||RPEL 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287306|||http://purl.uniprot.org/annotation/VSP_025436|||http://purl.uniprot.org/annotation/VSP_025437|||http://purl.uniprot.org/annotation/VSP_039730|||http://purl.uniprot.org/annotation/VSP_039731
http://togogenome.org/gene/9606:INTS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0H0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||Integrator complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236099|||http://purl.uniprot.org/annotation/VAR_049628
http://togogenome.org/gene/9606:C16orf86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein C16orf86                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318961
http://togogenome.org/gene/9606:LRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75074                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||Low-density lipoprotein receptor-related protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017323|||http://purl.uniprot.org/annotation/VAR_018171|||http://purl.uniprot.org/annotation/VAR_049764
http://togogenome.org/gene/9606:PRDX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30041                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||For phospholipase activity|||Important for phospholipase activity|||Loss of peroxidase activity, but no effect on phospholipase activity.|||Loss of phospholipase activity, but no effect on peroxidase activity.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Peroxiredoxin-6|||Phosphothreonine|||Phosphothreonine; by MAPK|||Phosphotyrosine|||Removed|||Required and sufficient for targeting to lysosomes and lamellar bodies|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135102
http://togogenome.org/gene/9606:MISP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein MISP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318963|||http://purl.uniprot.org/annotation/VAR_039392
http://togogenome.org/gene/9606:ZNF660                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AZW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Phosphoserine|||Zinc finger protein 660                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047701
http://togogenome.org/gene/9606:GUSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08236                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-glucuronidase|||In MPS7.|||In MPS7; loss of activity.|||In MPS7; very mild phenotype.|||In isoform 2.|||In isoform 3.|||Likely benign variant; associated with beta-glucuronidase pseudodeficiency with no clinical consequences; reduced activity levels.|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012161|||http://purl.uniprot.org/annotation/VAR_003196|||http://purl.uniprot.org/annotation/VAR_003197|||http://purl.uniprot.org/annotation/VAR_003198|||http://purl.uniprot.org/annotation/VAR_003199|||http://purl.uniprot.org/annotation/VAR_003200|||http://purl.uniprot.org/annotation/VAR_003201|||http://purl.uniprot.org/annotation/VAR_016179|||http://purl.uniprot.org/annotation/VAR_037914|||http://purl.uniprot.org/annotation/VAR_037915|||http://purl.uniprot.org/annotation/VAR_037916|||http://purl.uniprot.org/annotation/VAR_037917|||http://purl.uniprot.org/annotation/VAR_037918|||http://purl.uniprot.org/annotation/VAR_037919|||http://purl.uniprot.org/annotation/VAR_037920|||http://purl.uniprot.org/annotation/VAR_037921|||http://purl.uniprot.org/annotation/VAR_037922|||http://purl.uniprot.org/annotation/VAR_037923|||http://purl.uniprot.org/annotation/VAR_037924|||http://purl.uniprot.org/annotation/VAR_037925|||http://purl.uniprot.org/annotation/VAR_037926|||http://purl.uniprot.org/annotation/VAR_037927|||http://purl.uniprot.org/annotation/VAR_037928|||http://purl.uniprot.org/annotation/VAR_037929|||http://purl.uniprot.org/annotation/VAR_037930|||http://purl.uniprot.org/annotation/VAR_037931|||http://purl.uniprot.org/annotation/VAR_037932|||http://purl.uniprot.org/annotation/VAR_037933|||http://purl.uniprot.org/annotation/VAR_037934|||http://purl.uniprot.org/annotation/VAR_037935|||http://purl.uniprot.org/annotation/VAR_037936|||http://purl.uniprot.org/annotation/VAR_055884|||http://purl.uniprot.org/annotation/VAR_058511|||http://purl.uniprot.org/annotation/VAR_058512|||http://purl.uniprot.org/annotation/VAR_058513|||http://purl.uniprot.org/annotation/VAR_058514|||http://purl.uniprot.org/annotation/VAR_058515|||http://purl.uniprot.org/annotation/VAR_058516|||http://purl.uniprot.org/annotation/VAR_058517|||http://purl.uniprot.org/annotation/VAR_058518|||http://purl.uniprot.org/annotation/VAR_058519|||http://purl.uniprot.org/annotation/VSP_001799|||http://purl.uniprot.org/annotation/VSP_054830
http://togogenome.org/gene/9606:FAM83D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4H8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with DYNLL1 and no effect on interaction with HMMR; when associated with 391-A--A-393 and 409-A--A-411.|||Abolishes interaction with DYNLL1 and no effect on interaction with HMMR; when associated with 391-A--A-393 and 442-A--A-444.|||Abolishes interaction with DYNLL1 and no effect on interaction with HMMR; when associated with 409-A--A-411 and 442-A--A-444.|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM83D|||Required for interaction with KIF22 and function in chromosome congression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079460|||http://purl.uniprot.org/annotation/VSP_036446
http://togogenome.org/gene/9606:SPATA31F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRK5|||http://purl.uniprot.org/uniprot/A6NFA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Polar residues|||Protein SPATA31F3|||SPATA31F3-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319052
http://togogenome.org/gene/9606:PRPF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99633                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||Pre-mRNA-splicing factor 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058582|||http://purl.uniprot.org/annotation/VSP_008327|||http://purl.uniprot.org/annotation/VSP_008328
http://togogenome.org/gene/9606:DCAF16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||DDB1- and CUL4-associated factor 16|||Disordered|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301964|||http://purl.uniprot.org/annotation/VAR_034917|||http://purl.uniprot.org/annotation/VAR_034918
http://togogenome.org/gene/9606:VEGFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49765|||http://purl.uniprot.org/uniprot/Q7LAP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform VEGF-B167.|||Interchain|||Platelet-derived growth factor (PDGF) family profile|||Vascular endothelial growth factor B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023398|||http://purl.uniprot.org/annotation/PRO_5014310907|||http://purl.uniprot.org/annotation/VSP_004639|||http://purl.uniprot.org/annotation/VSP_004640
http://togogenome.org/gene/9606:CTNNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6KRI5|||http://purl.uniprot.org/uniprot/P26232|||http://purl.uniprot.org/uniprot/Q49AD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Catenin alpha-2|||Disordered|||In CDCBM9.|||In CDCBM9; loss-of-function variant resulting in decreased neurite length and impaired neuronal migration in patient-derived nerve cells; no protein detected in patient cells.|||In CDCBM9; unknown pathological significance.|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064263|||http://purl.uniprot.org/annotation/VAR_081335|||http://purl.uniprot.org/annotation/VAR_081336|||http://purl.uniprot.org/annotation/VAR_081337|||http://purl.uniprot.org/annotation/VSP_020337|||http://purl.uniprot.org/annotation/VSP_038005|||http://purl.uniprot.org/annotation/VSP_038006|||http://purl.uniprot.org/annotation/VSP_038007|||http://purl.uniprot.org/annotation/VSP_038008|||http://purl.uniprot.org/annotation/VSP_038009
http://togogenome.org/gene/9606:ZNF552                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1H1|||http://purl.uniprot.org/uniprot/Q9H707                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 552                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286810|||http://purl.uniprot.org/annotation/VAR_032177
http://togogenome.org/gene/9606:ZBTB7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15156                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||N6-acetyllysine; by EP300; alternate|||Phosphoserine|||Phosphothreonine|||Pro residues|||Required for interaction with and acetylation by EP300|||Zinc finger and BTB domain-containing protein 7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047719|||http://purl.uniprot.org/annotation/VSP_044721
http://togogenome.org/gene/9606:NTRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KR47|||http://purl.uniprot.org/uniprot/Q16620|||http://purl.uniprot.org/uniprot/Q548C2|||http://purl.uniprot.org/uniprot/Q5VWE5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  BDNF/NT-3 growth factors receptor|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In DEE58; unknown pathological significance.|||In OBHD.|||In OBHD; expressed normally on the cell surface; results in markedly impaired ligand-induced phosphorylation as well as impaired downstream MAPK1 phosphorylation.|||In OBHD; unknown pathological significance.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung carcinoma sample; somatic mutation.|||In isoform 4 and isoform 5.|||In isoform TrkB-N-T1.|||In isoform TrkB-T-Shc and isoform 5.|||In isoform TrkB-T-TK.|||In isoform TrkB-T1 and isoform TrkB-N-T1.|||Interaction with MAPK8IP3/JIP3|||Interaction with PLCG1|||Interaction with SH2D1A|||Interaction with SHC1|||LRR 1|||LRR 2|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016727|||http://purl.uniprot.org/annotation/PRO_5004249812|||http://purl.uniprot.org/annotation/PRO_5014310173|||http://purl.uniprot.org/annotation/PRO_5035269091|||http://purl.uniprot.org/annotation/VAR_011973|||http://purl.uniprot.org/annotation/VAR_016320|||http://purl.uniprot.org/annotation/VAR_041470|||http://purl.uniprot.org/annotation/VAR_046518|||http://purl.uniprot.org/annotation/VAR_046519|||http://purl.uniprot.org/annotation/VAR_046520|||http://purl.uniprot.org/annotation/VAR_049715|||http://purl.uniprot.org/annotation/VAR_065890|||http://purl.uniprot.org/annotation/VAR_080659|||http://purl.uniprot.org/annotation/VAR_080660|||http://purl.uniprot.org/annotation/VAR_080661|||http://purl.uniprot.org/annotation/VSP_002901|||http://purl.uniprot.org/annotation/VSP_002902|||http://purl.uniprot.org/annotation/VSP_002903|||http://purl.uniprot.org/annotation/VSP_002904|||http://purl.uniprot.org/annotation/VSP_041942|||http://purl.uniprot.org/annotation/VSP_042177|||http://purl.uniprot.org/annotation/VSP_042178|||http://purl.uniprot.org/annotation/VSP_042179
http://togogenome.org/gene/9606:IPO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00410|||http://purl.uniprot.org/uniprot/Q9BVS9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 21|||HEAT 22|||HEAT 23|||HEAT 24|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Importin N-terminal|||Importin-5|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Ran-GTP binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120771|||http://purl.uniprot.org/annotation/VAR_012029|||http://purl.uniprot.org/annotation/VAR_012030|||http://purl.uniprot.org/annotation/VAR_012031|||http://purl.uniprot.org/annotation/VAR_012032|||http://purl.uniprot.org/annotation/VAR_012033|||http://purl.uniprot.org/annotation/VSP_037587|||http://purl.uniprot.org/annotation/VSP_037774
http://togogenome.org/gene/9606:ELOVL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5J4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Elongation of very long chain fatty acids protein 6|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282845
http://togogenome.org/gene/9606:INPP4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PE3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Complete loss of lipid phosphatase activity.|||Does not rescue the wortmannin-induced dilation of endosomes due to accumulation of (PtdIns(3,4)P2).|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Inositol polyphosphate-4-phosphatase type I A|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190232|||http://purl.uniprot.org/annotation/VAR_059359|||http://purl.uniprot.org/annotation/VSP_015240|||http://purl.uniprot.org/annotation/VSP_015241|||http://purl.uniprot.org/annotation/VSP_015242
http://togogenome.org/gene/9606:DTX3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase DTX3L|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of catalytic activity but does not affect its capacity to inhibit ITCH catalytic activity; when associated with A-561 and A-596.|||Loss of catalytic activity but does not affect its capacity to inhibit ITCH catalytic activity; when associated with A-561 and A-599.|||Loss of catalytic activity but does not affect its capacity to inhibit ITCH catalytic activity; when associated with A-596 and A-599.|||Loss of catalytic activity. Loss of histone H2B ubiquitination. No effect on STAT1 phosphorylation and on the interaction with PARP9 and STAT1.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219087|||http://purl.uniprot.org/annotation/VAR_036098|||http://purl.uniprot.org/annotation/VAR_048895|||http://purl.uniprot.org/annotation/VAR_048896|||http://purl.uniprot.org/annotation/VSP_038522
http://togogenome.org/gene/9606:TACO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSH4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Translational activator of cytochrome c oxidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175942|||http://purl.uniprot.org/annotation/VAR_052934
http://togogenome.org/gene/9606:RIPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Z8|||http://purl.uniprot.org/uniprot/O43353                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-acetylserine; by Yersinia YopJ|||(Microbial infection) O-acetylserine; by Yersinia YopJ; alternate|||(Microbial infection) O-acetylthreonine; by Yersinia YopJ|||Abolished ability to activate NF-kappa-B downstream of NOD2.|||Abolished activation of NF-kappa-B.|||Abolished ubiquitination by ZNRF4.|||Abolishes interaction with NOD1.|||Abolishes interaction with NOD1. Abolished activation of NF-kappa-B.|||Abolishes protein-kinase activity without preventing ability to activate NF-kappa-B downstream of NOD2.|||Abolishes protein-kinase activity. Reduces FAS-mediated apoptosis.|||Activation segment (AS)|||CARD|||Decreased homooligomerization and ability to transmit NOD2 signaling.|||Decreased interaction with NGFR.|||Decreased phosphorylation and activation. Abolished phosphorylation by LRRK2.|||Decreased polyubiquitination.|||Decreases interaction with NOD2.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helix alphaC|||Impaired interaction with NOD2 and decreased homooligomerization and ability to transmit NOD2 signaling.|||In isoform 2.|||Increased activation of NF-kappa-B.|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by autocatalysis and LRRK2; alternate|||Phosphotyrosine; by CSK|||Phosphotyrosine; by autocatalysis|||Polar residues|||Prevents phosphorylation. Reduces serine and threonine phosphorylation of ARHGEF2.|||Protein kinase|||Proton acceptor|||Receptor-interacting serine/threonine-protein kinase 2|||Reduced formation of filaments and activation of NF-kappa-B.|||Reduced ubiquitination by XIAP and activation of NF-kappa-B; when associated with R-410.|||Reduced ubiquitination by XIAP and activation of NF-kappa-B; when associated with R-538.|||Strongly decreased activation of NF-kappa-B.|||Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B; when associated with E-458.|||Strongly decreased activation of NF-kappa-B. Does not affect activation of NF-kappa-B; when associated with R-445.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086608|||http://purl.uniprot.org/annotation/VAR_041045|||http://purl.uniprot.org/annotation/VAR_041046|||http://purl.uniprot.org/annotation/VAR_041047|||http://purl.uniprot.org/annotation/VSP_013266
http://togogenome.org/gene/9606:PCBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6B9|||http://purl.uniprot.org/uniprot/Q15366                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cleavage, by viral proteinase 3CD|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3, isoform 4, isoform 6 and isoform 7.|||In isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 7 and isoform 8.|||K Homology|||KH 1|||KH 2|||KH 3|||Phosphoserine|||Poly(rC)-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050090|||http://purl.uniprot.org/annotation/VSP_042833|||http://purl.uniprot.org/annotation/VSP_043161|||http://purl.uniprot.org/annotation/VSP_043362|||http://purl.uniprot.org/annotation/VSP_054045
http://togogenome.org/gene/9606:ZNF613                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PF04                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 613                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234597|||http://purl.uniprot.org/annotation/VAR_028096|||http://purl.uniprot.org/annotation/VAR_028097|||http://purl.uniprot.org/annotation/VAR_028098|||http://purl.uniprot.org/annotation/VAR_057428|||http://purl.uniprot.org/annotation/VAR_057429|||http://purl.uniprot.org/annotation/VSP_018388
http://togogenome.org/gene/9606:CASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K249|||http://purl.uniprot.org/uniprot/A8K257|||http://purl.uniprot.org/uniprot/P29466                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cleavage of Gasdermin-D (GSDMD).|||CARD|||Caspase family p10|||Caspase family p20|||Caspase-1 subunit p10|||Caspase-1 subunit p20|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IDL(uncl); abolished cleavage in the interdomain region; when associated with 315-N-N-316.|||In IDL(uncl); abolished cleavage in the interdomain region; when associated with N-297.|||In isoform Beta.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma and isoform Delta.|||Interdomain linker|||Loss of protease activity. Loss of SPHK2 cleavage and release in apoptotic cells.|||Mediates autoprocessing but is unable to interact with Gasdermin-D (GSDMD) and mediate its cleavage.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004521|||http://purl.uniprot.org/annotation/PRO_0000004522|||http://purl.uniprot.org/annotation/PRO_0000004523|||http://purl.uniprot.org/annotation/PRO_0000004524|||http://purl.uniprot.org/annotation/VAR_048615|||http://purl.uniprot.org/annotation/VSP_000797|||http://purl.uniprot.org/annotation/VSP_000798|||http://purl.uniprot.org/annotation/VSP_000799|||http://purl.uniprot.org/annotation/VSP_000800
http://togogenome.org/gene/9606:SLFN13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV92|||http://purl.uniprot.org/uniprot/Q68D06                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished endoribonuclease activity.|||In isoform 2.|||N'-domain region|||Reduced endoribonuclease activity.|||Schlafen family member 13|||Schlafen group 3-like DNA/RNA helicase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282985|||http://purl.uniprot.org/annotation/VAR_031449|||http://purl.uniprot.org/annotation/VAR_031450|||http://purl.uniprot.org/annotation/VAR_031451|||http://purl.uniprot.org/annotation/VAR_053878|||http://purl.uniprot.org/annotation/VAR_053879|||http://purl.uniprot.org/annotation/VSP_024273
http://togogenome.org/gene/9606:CSRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2TDB8|||http://purl.uniprot.org/uniprot/P50461                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine and glycine-rich protein 3|||In CMD1M; unknown pathological significance; decreases interaction with TCAP.|||In CMD1M; unknown pathological significance; increases PKC/PRKCA activity.|||In CMH12; decreases PKC/PRKCA activity.|||In CMH12; decreases interaction with NRAP and ACTN2, decreases zinc-binding and impairs protein stability, decreases PKC/PRKCA activity.|||In isoform 2.|||Increases PKC/PRKCA activity.|||Interaction with CLF2 and isoform 2|||Interaction with TCAP|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075727|||http://purl.uniprot.org/annotation/VAR_015401|||http://purl.uniprot.org/annotation/VAR_045932|||http://purl.uniprot.org/annotation/VAR_045933|||http://purl.uniprot.org/annotation/VAR_045934|||http://purl.uniprot.org/annotation/VAR_076805|||http://purl.uniprot.org/annotation/VSP_058575|||http://purl.uniprot.org/annotation/VSP_058576
http://togogenome.org/gene/9606:LTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06643|||http://purl.uniprot.org/uniprot/Q5STB2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lymphotoxin-beta|||N-linked (GlcNAc...) asparagine|||TNF family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185486|||http://purl.uniprot.org/annotation/VAR_013025|||http://purl.uniprot.org/annotation/VAR_013026|||http://purl.uniprot.org/annotation/VAR_016331|||http://purl.uniprot.org/annotation/VAR_016332|||http://purl.uniprot.org/annotation/VAR_029145|||http://purl.uniprot.org/annotation/VSP_006441|||http://purl.uniprot.org/annotation/VSP_006442
http://togogenome.org/gene/9606:GFM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In COXPD39.|||In COXPD39; unknown pathological significance; may affect splicing.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Ribosome-releasing factor 2, mitochondrial|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007450|||http://purl.uniprot.org/annotation/VAR_053983|||http://purl.uniprot.org/annotation/VAR_053984|||http://purl.uniprot.org/annotation/VAR_053985|||http://purl.uniprot.org/annotation/VAR_060200|||http://purl.uniprot.org/annotation/VAR_060201|||http://purl.uniprot.org/annotation/VAR_060202|||http://purl.uniprot.org/annotation/VAR_082193|||http://purl.uniprot.org/annotation/VAR_082194|||http://purl.uniprot.org/annotation/VAR_082195|||http://purl.uniprot.org/annotation/VSP_001363|||http://purl.uniprot.org/annotation/VSP_038190|||http://purl.uniprot.org/annotation/VSP_038191|||http://purl.uniprot.org/annotation/VSP_038192|||http://purl.uniprot.org/annotation/VSP_038193|||http://purl.uniprot.org/annotation/VSP_038194
http://togogenome.org/gene/9606:RAB6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53S08                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  Ras-related protein Rab-6D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000443825
http://togogenome.org/gene/9606:CILP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75339                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Associated with susceptibility to lumbar disk disease in Japanese; increases binding and inhibition of TGFB1.|||Cartilage intermediate layer protein 1|||Cartilage intermediate layer protein 1 C1|||Cartilage intermediate layer protein 1 C2|||Disordered|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014671|||http://purl.uniprot.org/annotation/PRO_0000014672|||http://purl.uniprot.org/annotation/PRO_0000014673|||http://purl.uniprot.org/annotation/VAR_022768|||http://purl.uniprot.org/annotation/VAR_022769|||http://purl.uniprot.org/annotation/VAR_022770|||http://purl.uniprot.org/annotation/VAR_022771|||http://purl.uniprot.org/annotation/VAR_022772|||http://purl.uniprot.org/annotation/VAR_022773|||http://purl.uniprot.org/annotation/VAR_022774|||http://purl.uniprot.org/annotation/VAR_022775|||http://purl.uniprot.org/annotation/VAR_022776|||http://purl.uniprot.org/annotation/VAR_069430|||http://purl.uniprot.org/annotation/VAR_069431
http://togogenome.org/gene/9606:ZDBF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/N0DVB2|||http://purl.uniprot.org/uniprot/N0DVX5|||http://purl.uniprot.org/uniprot/Q9HCK1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DBF4-type|||DBF4-type zinc finger-containing protein 2|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314166|||http://purl.uniprot.org/annotation/VAR_037853
http://togogenome.org/gene/9606:SERAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JX3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MEGDEL.|||In MEGDEL; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Protein SERAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274671|||http://purl.uniprot.org/annotation/VAR_030342|||http://purl.uniprot.org/annotation/VAR_068442|||http://purl.uniprot.org/annotation/VAR_068443|||http://purl.uniprot.org/annotation/VAR_068444|||http://purl.uniprot.org/annotation/VAR_068445|||http://purl.uniprot.org/annotation/VAR_080230|||http://purl.uniprot.org/annotation/VSP_022857|||http://purl.uniprot.org/annotation/VSP_022858|||http://purl.uniprot.org/annotation/VSP_022859|||http://purl.uniprot.org/annotation/VSP_022860
http://togogenome.org/gene/9606:RTCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00442                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||RNA 3'-terminal phosphate cyclase|||Tele-AMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156410|||http://purl.uniprot.org/annotation/VSP_005915
http://togogenome.org/gene/9606:TMEM156                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N614                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 156                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284505|||http://purl.uniprot.org/annotation/VAR_031756|||http://purl.uniprot.org/annotation/VAR_031757|||http://purl.uniprot.org/annotation/VAR_051430
http://togogenome.org/gene/9606:MT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04731                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1A|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197234|||http://purl.uniprot.org/annotation/VAR_059436|||http://purl.uniprot.org/annotation/VAR_060727
http://togogenome.org/gene/9606:BAZ1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRL2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with SMARCA5/SNF2H, and abolishes the formation of the CHRACISWI chromatin remodeling complex.|||Abolishes interaction with the CHRAC1-POLE3 heterodimer.|||Acidic residues|||Basic and acidic residues|||Bromo|||Bromodomain adjacent to zinc finger domain protein 1A|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with NCOR1|||Required for interaction with SMARCA5 and formation of the CHRAC ISWI chromatin remodeling complex|||Required for interaction with the CHRAC1-POLE3 heterodimer. Required for interaction with the CHRAC1-POLE3 heterodimer|||WAC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211167|||http://purl.uniprot.org/annotation/VAR_028049|||http://purl.uniprot.org/annotation/VAR_048423|||http://purl.uniprot.org/annotation/VSP_000551
http://togogenome.org/gene/9606:RPTOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DKI0|||http://purl.uniprot.org/uniprot/Q8N122                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation after forskolin treatment.|||Abolished phosphorylation by NLK, leading to impaired inhibition of the mTORC1 complex in response to osmotic stress.|||Abolishes AMPK-mediated phosphorylation; when associated with A-722. Does not affect phosphorylation after forskolin treatment.|||Abolishes AMPK-mediated phosphorylation; when associated with A-792.|||Basic and acidic residues|||Decreased phosphorylation, leading to increased activity of the mTORC1 complex.|||Decreased ubiquitination.|||Disordered|||Does not affect ubiquitination.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In Clw1 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes without affecting the composition of the mTORC1 complex.|||In Clw2 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes without affecting the composition of the mTORC1 complex.|||In Clw3 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes without affecting the composition of the mTORC1 complex.|||In Clw4 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes without affecting the composition of the mTORC1 complex.|||In alpha24 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes.|||In alpha26 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes.|||In alpha29 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes.|||In alphax3 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes; when associated with E-597 and A-635.|||In alphax3 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes; when associated with F-560 and A-635.|||In alphax3 mutant; abolished interaction with GTP-bound RRAGA and recruitment to lysosomes; when associated with F-560 and E-597.|||In isoform 2.|||In isoform 3.|||Mimics phosphorylation, leading to impaired interaction with small GTPases Rag and activation of the mTORC1 complex.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by AMPK and RPS6KA1|||Phosphoserine; by MAPK8|||Phosphoserine; by MAPK8, MTOR and NLK|||Phosphoserine; by MTOR|||Phosphoserine; by PKA|||Phosphoserine; by RPS6KA1|||Phosphoserine; by TBK1|||Phosphothreonine|||Phosphothreonine; by MAPK8|||Polar residues|||Reduced acetylation, leading to decreased activation of the mTORC complex.|||Regulatory-associated protein of mTOR|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051200|||http://purl.uniprot.org/annotation/VSP_010174|||http://purl.uniprot.org/annotation/VSP_054042
http://togogenome.org/gene/9606:MISP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-164; A-172; A-214; A-224; A-284; A-287; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-394; A-395; A-397; A-471; A-582 and A-586.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-287 and A-377.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-287 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-284; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-224; A-287; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-214; A-284; A-287; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-172; A-224; A-284; A-287; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-164; A-214; A-224; A-284; A-287; A-377 and A-575.|||Almost complete loss of CDK1 phosphorylation in vitro, loss of PLK1-binding, no effect on cortical localization; when associated with A-78; A-172; A-214; A-224; A-284; A-287; A-377 and A-575.|||Disordered|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-471 and A-582.|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-471 and A-586.|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-397; A-582 and A-586.|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-395; A-471; A-582 and A-586.|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-394; A-397; A-471; A-582 and A-586.|||Drastic reduction in PLK1 phosphorylation in vitro, no effect on cortical localization; when associated with A-382; A-395; A-397; A-471; A-582 and A-586.|||Mitotic interactor and substrate of PLK1|||No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-582.|||No effect on cortical localization; when associated with D-394; D-395; D-397; D-471 and D-586.|||No effect on cortical localization; when associated with D-394; D-395; D-397; D-582 and D-586.|||No effect on cortical localization; when associated with D-394; D-395; D-471; D-582 and D-586.|||No effect on cortical localization; when associated with D-394; D-397; D-471; D-582 and D-586.|||No effect on cortical localization; when associated with D-395; D-397; D-471; D-582 and D-586.|||Phosphoserine|||Phosphoserine; by CDK1; in vitro|||Phosphoserine; by PLK1; in vitro|||Phosphothreonine|||Phosphothreonine; by CDK1; in vitro|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079381|||http://purl.uniprot.org/annotation/VAR_033754|||http://purl.uniprot.org/annotation/VAR_033755|||http://purl.uniprot.org/annotation/VAR_033756|||http://purl.uniprot.org/annotation/VAR_050910|||http://purl.uniprot.org/annotation/VAR_061629
http://togogenome.org/gene/9606:ANKRD53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9V6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 53|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274490|||http://purl.uniprot.org/annotation/VAR_030300|||http://purl.uniprot.org/annotation/VAR_054427|||http://purl.uniprot.org/annotation/VAR_061018|||http://purl.uniprot.org/annotation/VAR_067464|||http://purl.uniprot.org/annotation/VAR_067465|||http://purl.uniprot.org/annotation/VSP_022768|||http://purl.uniprot.org/annotation/VSP_022769
http://togogenome.org/gene/9606:GRM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15303                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CSNB1B; abolishes expression at the cell membrane.|||In a breast cancer sample; somatic mutation.|||Metabotropic glutamate receptor 6|||N-linked (GlcNAc...) asparagine|||No effect on location at the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012934|||http://purl.uniprot.org/annotation/VAR_030756|||http://purl.uniprot.org/annotation/VAR_030757|||http://purl.uniprot.org/annotation/VAR_036195|||http://purl.uniprot.org/annotation/VAR_055876|||http://purl.uniprot.org/annotation/VAR_055877|||http://purl.uniprot.org/annotation/VAR_055878|||http://purl.uniprot.org/annotation/VAR_055879|||http://purl.uniprot.org/annotation/VAR_055880|||http://purl.uniprot.org/annotation/VAR_059310|||http://purl.uniprot.org/annotation/VAR_069817|||http://purl.uniprot.org/annotation/VAR_069818|||http://purl.uniprot.org/annotation/VAR_069819|||http://purl.uniprot.org/annotation/VAR_069820
http://togogenome.org/gene/9606:EPHB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSE0|||http://purl.uniprot.org/uniprot/P29323|||http://purl.uniprot.org/uniprot/Q4LE53|||http://purl.uniprot.org/uniprot/Q6NVW1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by a metalloproteinase|||Cleavage; by gamma-secretase/PS1|||Complete loss of ubiquitination by RNF186.|||Cytoplasmic|||Disordered|||Eph LBD|||EphB2/CTF1|||EphB2/CTF2|||Ephrin type-B receptor 2|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In BDPLT22.|||In isoform 2 and isoform 3.|||In isoform 3.|||In prostate cancer.|||N-linked (GlcNAc...) asparagine|||No loss of ubiquitination by RNF186.|||PDZ-binding (in isoform 2)|||Phosphoserine|||Protein kinase|||Proton acceptor|||SAM|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016827|||http://purl.uniprot.org/annotation/PRO_0000445961|||http://purl.uniprot.org/annotation/PRO_0000445962|||http://purl.uniprot.org/annotation/PRO_5002803525|||http://purl.uniprot.org/annotation/PRO_5004240906|||http://purl.uniprot.org/annotation/PRO_5014587383|||http://purl.uniprot.org/annotation/VAR_032853|||http://purl.uniprot.org/annotation/VAR_032854|||http://purl.uniprot.org/annotation/VAR_032855|||http://purl.uniprot.org/annotation/VAR_032856|||http://purl.uniprot.org/annotation/VAR_032857|||http://purl.uniprot.org/annotation/VAR_032858|||http://purl.uniprot.org/annotation/VAR_042172|||http://purl.uniprot.org/annotation/VAR_042173|||http://purl.uniprot.org/annotation/VAR_042174|||http://purl.uniprot.org/annotation/VAR_042175|||http://purl.uniprot.org/annotation/VAR_082702|||http://purl.uniprot.org/annotation/VSP_003016|||http://purl.uniprot.org/annotation/VSP_003017|||http://purl.uniprot.org/annotation/VSP_015713
http://togogenome.org/gene/9606:RARG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3H3|||http://purl.uniprot.org/uniprot/B7Z4B4|||http://purl.uniprot.org/uniprot/F1D8P1|||http://purl.uniprot.org/uniprot/P13631                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hinge|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Omega-N-methylarginine|||Polar residues|||Retinoic acid receptor gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053472|||http://purl.uniprot.org/annotation/VAR_036061|||http://purl.uniprot.org/annotation/VAR_038554|||http://purl.uniprot.org/annotation/VSP_031080|||http://purl.uniprot.org/annotation/VSP_044776|||http://purl.uniprot.org/annotation/VSP_044777
http://togogenome.org/gene/9606:GPR158                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T848                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cache-like region|||Cytoplasmic|||Disordered|||Does not affect G protein alpha subunit activation.|||Does not affect ability to regulate cAMP levels; when associated with A-135 and A-540.|||Does not affect ability to regulate cAMP levels; when associated with A-135 and A-578.|||Does not affect ability to regulate cAMP levels; when associated with A-540 and A-578.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In M1 mutant; decreased localizatiuon to the nucleus.|||In M2 mutant; decreased localizatiuon to the nucleus.|||In Mut1; decreased interaction with GNAO1.|||In Mut2; does not affect interaction with GNAO1.|||In Mut3; decreased interaction with GNAO1.|||In Mut4; does not affect interaction with GNAO1.|||Induces an increase of cAMP levels.|||Metabotropic glycine receptor|||N-linked (GlcNAc...) asparagine|||Nearly abolished ability to inhibit the GTPase activator activity of RGS7 without affecting glycine-binding.|||Nearly abolished glycine-binding and ability to inhibit the GTPase activator activity of RGS7.|||Phosphoserine|||Polar residues|||VCPWE motif 1|||VCPWE motif 2|||VCPWE motif 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012969|||http://purl.uniprot.org/annotation/VAR_049285|||http://purl.uniprot.org/annotation/VAR_049286
http://togogenome.org/gene/9606:KCNK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SYI1|||http://purl.uniprot.org/uniprot/Q9Y2U2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform B.|||In isoform C.|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel|||Potassium channel subfamily K member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101751|||http://purl.uniprot.org/annotation/VSP_006693|||http://purl.uniprot.org/annotation/VSP_006694|||http://purl.uniprot.org/annotation/VSP_006695|||http://purl.uniprot.org/annotation/VSP_006696
http://togogenome.org/gene/9606:SLC29A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99808                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decrease in the transport capacity and substrate affinity for adenosine. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||Decrease in the transport capacity but no change in affinity for adenosine. Resistance to dipyridamole and dilazep, little or no effect on the sensitivities to nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||Decreased affinity for cytidine and adenosine but not uridine. Resistance to azidothymidine (AZT), dideoxyinosine (ddI), nitrobenzylmercaptopurine riboside (NBMPR), dilazep, dipyridamole and hypoxanthine but not dideoxycytidine (ddC).|||Decreased inosine transport.|||Disordered|||Equilibrative nucleoside transporter 1|||Essential for nucleobase transport|||Extracellular|||Glycosylation-defective.|||Helical|||Impaired protein folding and/or altered trafficking. Decrease in the transport capacity but no change in affinity for adenosine. No effect on the sensitivity to dipyridamole. Resistance to dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||Impaired protein folding and/or altered trafficking. Decrease in the transport capacity for adenosine but no change in substrate affinity. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Increase in the transport capacity and decrease in affinity for inosine. Increase in the transport capacity but no change in affinity for adenosine. Resistance to nitrobenzylmercaptopurine riboside (NBMPR) and dilazep but not dipyridamole.|||Increase in the transport capacity but no change in affinity for adenosine. Resistance to dipyridamole and increase in the sensitivity to dilazep. Little or no effect on the sensitivities to nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||Loss of nucleobase transport; when associated with S-193; S-213; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-193; S-213; S-222; S-297; S-333; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-414 and S-416. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378 and S-416.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-414 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-333; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-297; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-222; S-333; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-213; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-213; S-297; S-333; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-193; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-193; S-222; S-297; S-333; S-378; S-416 and S-439.|||Loss of nucleobase transport; when associated with S-87; S-213; S-222; S-297; S-333; S-378; S-414; S-416 and S-439. No change in nucleobase transport; when associated with S-87; S-213; S-222; S-297; S-333; S-378; S-416 and S-439.|||N-linked (GlcNAc...) asparagine|||No change in the transport capacity but decrease in affinity for adenosine. Resistance to dipyridamole, dilazep, nitrobenzylmercaptopurine riboside (NBMPR), draflazine and soluflazine.|||No effect on glycosylation.|||No effect on subcellular localization and inosine transport.|||No effect on the transport activity for adenosine.|||Not glycosylated|||Phosphoserine|||Reduction of the transport activity for adenosine.|||Removed|||Resistance to nitrobenzylmercaptopurine riboside (NBMPR) and dilazep but not dipyridamole. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209337|||http://purl.uniprot.org/annotation/VAR_036221|||http://purl.uniprot.org/annotation/VAR_036222|||http://purl.uniprot.org/annotation/VAR_053668|||http://purl.uniprot.org/annotation/VAR_053669|||http://purl.uniprot.org/annotation/VSP_056579
http://togogenome.org/gene/9606:PLEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KUE3|||http://purl.uniprot.org/uniprot/Q15149                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4 X 4 AA tandem repeats of G-S-R-X|||Actin-binding|||Basic and acidic residues|||Binding to intermediate filaments|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Central fibrous rod domain|||Disordered|||Globular 1|||Globular 2|||In EBS5A.|||In EBS5B.|||In LGMDR17.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphotyrosine|||Plectin|||Plectin 1|||Plectin 10|||Plectin 11|||Plectin 12|||Plectin 13|||Plectin 14|||Plectin 15|||Plectin 16|||Plectin 17|||Plectin 18|||Plectin 19|||Plectin 2|||Plectin 20|||Plectin 21|||Plectin 22|||Plectin 23|||Plectin 24|||Plectin 25|||Plectin 26|||Plectin 27|||Plectin 28|||Plectin 29|||Plectin 3|||Plectin 30|||Plectin 31|||Plectin 32|||Plectin 33|||Plectin 4|||Plectin 5|||Plectin 6|||Plectin 7|||Plectin 8|||Plectin 9|||Polar residues|||Required for efficient interaction with KRT5 and KRT14 heterodimers|||Required for interaction with intermediate filament proteins|||Required for interaction with type2 keratins, DES and VIM|||SH3|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078135|||http://purl.uniprot.org/annotation/VAR_011336|||http://purl.uniprot.org/annotation/VAR_011337|||http://purl.uniprot.org/annotation/VAR_015817|||http://purl.uniprot.org/annotation/VAR_053585|||http://purl.uniprot.org/annotation/VAR_053586|||http://purl.uniprot.org/annotation/VAR_053587|||http://purl.uniprot.org/annotation/VAR_053588|||http://purl.uniprot.org/annotation/VAR_053589|||http://purl.uniprot.org/annotation/VAR_053590|||http://purl.uniprot.org/annotation/VAR_053591|||http://purl.uniprot.org/annotation/VAR_053592|||http://purl.uniprot.org/annotation/VAR_053593|||http://purl.uniprot.org/annotation/VAR_053594|||http://purl.uniprot.org/annotation/VAR_060088|||http://purl.uniprot.org/annotation/VAR_060089|||http://purl.uniprot.org/annotation/VAR_062133|||http://purl.uniprot.org/annotation/VAR_075706|||http://purl.uniprot.org/annotation/VAR_076564|||http://purl.uniprot.org/annotation/VAR_076565|||http://purl.uniprot.org/annotation/VSP_005030|||http://purl.uniprot.org/annotation/VSP_005031|||http://purl.uniprot.org/annotation/VSP_023510|||http://purl.uniprot.org/annotation/VSP_037100|||http://purl.uniprot.org/annotation/VSP_037101|||http://purl.uniprot.org/annotation/VSP_037102|||http://purl.uniprot.org/annotation/VSP_037103|||http://purl.uniprot.org/annotation/VSP_037104|||http://purl.uniprot.org/annotation/VSP_037105|||http://purl.uniprot.org/annotation/VSP_037106|||http://purl.uniprot.org/annotation/VSP_037107|||http://purl.uniprot.org/annotation/VSP_037108|||http://purl.uniprot.org/annotation/VSP_037109
http://togogenome.org/gene/9606:ENDOU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21128                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolishes endoribonuclease activity and increases RNA-binding activity.|||Abolishes endoribonuclease activity without affecting RNA-binding activity.|||Alternate|||EndoU|||In isoform 2.|||In isoform 3.|||SMB 1|||SMB 2|||Strongly impairs endoribonuclease activity without affecting RNA-binding activity.|||Uridylate-specific endoribonuclease                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036405|||http://purl.uniprot.org/annotation/VSP_039215|||http://purl.uniprot.org/annotation/VSP_039216
http://togogenome.org/gene/9606:ZNF430                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K360|||http://purl.uniprot.org/uniprot/Q2NKJ9|||http://purl.uniprot.org/uniprot/Q9H8G1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||N-acetylmethionine|||Zinc finger protein 430                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047578
http://togogenome.org/gene/9606:EHBP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3D4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 NT-type|||CAAX motif|||Calponin-homology (CH)|||Disordered|||EH domain-binding protein 1-like protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285204|||http://purl.uniprot.org/annotation/VAR_031993|||http://purl.uniprot.org/annotation/VAR_031994|||http://purl.uniprot.org/annotation/VAR_031995|||http://purl.uniprot.org/annotation/VAR_031996|||http://purl.uniprot.org/annotation/VAR_031997|||http://purl.uniprot.org/annotation/VAR_061645
http://togogenome.org/gene/9606:PAFAH1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PFU3|||http://purl.uniprot.org/uniprot/P43034                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In LIS1.|||In LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro.|||In LIS1; reduces neuronal migration in vitro.|||In SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro.|||In SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells.|||In isoform 2.|||Interaction with DCX|||Interaction with NDE1|||Interaction with NDEL1|||Interaction with dynein and dynactin|||LisH|||N6-acetyllysine|||Phosphoserine|||Platelet-activating factor acetylhydrolase IB subunit beta|||Required for self-association and interaction with PAFAH1B2 and PAFAH1B3|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051061|||http://purl.uniprot.org/annotation/VAR_007724|||http://purl.uniprot.org/annotation/VAR_010203|||http://purl.uniprot.org/annotation/VAR_015398|||http://purl.uniprot.org/annotation/VAR_015399|||http://purl.uniprot.org/annotation/VAR_015400|||http://purl.uniprot.org/annotation/VAR_037300|||http://purl.uniprot.org/annotation/VAR_037301|||http://purl.uniprot.org/annotation/VSP_019376|||http://purl.uniprot.org/annotation/VSP_019377|||http://purl.uniprot.org/annotation/VSP_019378|||http://purl.uniprot.org/annotation/VSP_019379
http://togogenome.org/gene/9606:LPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08519                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Apolipoprotein(a)|||Charge relay system|||Disordered|||Kringle 1|||Kringle 10|||Kringle 11|||Kringle 12|||Kringle 13|||Kringle 14|||Kringle 15|||Kringle 16|||Kringle 2|||Kringle 3|||Kringle 4|||Kringle 5|||Kringle 6|||Kringle 7|||Kringle 8|||Kringle 9|||Loss of lysine-sepharose binding.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000455008|||http://purl.uniprot.org/annotation/VAR_006633|||http://purl.uniprot.org/annotation/VAR_047293|||http://purl.uniprot.org/annotation/VAR_047294|||http://purl.uniprot.org/annotation/VAR_047295|||http://purl.uniprot.org/annotation/VAR_047296|||http://purl.uniprot.org/annotation/VAR_047297|||http://purl.uniprot.org/annotation/VAR_047298|||http://purl.uniprot.org/annotation/VAR_047299|||http://purl.uniprot.org/annotation/VAR_047300|||http://purl.uniprot.org/annotation/VAR_047301|||http://purl.uniprot.org/annotation/VAR_047302
http://togogenome.org/gene/9606:SRSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07955|||http://purl.uniprot.org/uniprot/Q59FA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding.|||In FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding.|||In FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding.|||In MR-A; loss of ability to activate splicing.|||In MR-B; strongly inhibits splicing.|||In MR-D; loss of ability to activate splicing.|||In MR-E; loss of ability to activate splicing.|||In RS-A; loss of ability to activate splicing but retains splice site switching.|||In RS-B; retains both splice activation and splice site switching activity.|||In RS-C; loss of ability to activate splicing but retains splice site switching.|||In a breast cancer sample; somatic mutation.|||In isoform ASF-2.|||In isoform ASF-3.|||Interaction with SAFB1|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109.|||Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97.|||Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109.|||RRM|||RRM 1|||RRM 2|||Reduced nucleocytoplasmic shuttling; when associated with D-162.|||Reduced nucleocytoplasmic shuttling; when associated with D-190.|||Removed|||Serine/arginine-rich splicing factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081911|||http://purl.uniprot.org/annotation/VAR_035488|||http://purl.uniprot.org/annotation/VSP_005856|||http://purl.uniprot.org/annotation/VSP_005857|||http://purl.uniprot.org/annotation/VSP_005858
http://togogenome.org/gene/9606:IGFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW32                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Insulin growth factor-like family member 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000044633
http://togogenome.org/gene/9606:ITLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWA0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mass|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Fibrinogen C-terminal|||Forms mainly dimers. Forms mainly monomers; when associated with S-31.|||Forms mainly monomers; when associated with S-48.|||GPI-anchor amidated serine|||Intelectin-1|||Interchain (with C-31)|||Interchain (with C-48)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009143|||http://purl.uniprot.org/annotation/PRO_0000009144|||http://purl.uniprot.org/annotation/VAR_019924|||http://purl.uniprot.org/annotation/VAR_019925
http://togogenome.org/gene/9606:CLCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBD9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cardiotrophin-like cytokine factor 1|||In CISS2; heterozygous compound with a nonsense mutation; unable to bind CNTFR alpha.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015616|||http://purl.uniprot.org/annotation/VAR_028354|||http://purl.uniprot.org/annotation/VSP_044269
http://togogenome.org/gene/9606:TK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4IF54|||http://purl.uniprot.org/uniprot/A5PLM0|||http://purl.uniprot.org/uniprot/B4DIW4|||http://purl.uniprot.org/uniprot/B4E0Z4|||http://purl.uniprot.org/uniprot/J3QRP0|||http://purl.uniprot.org/uniprot/O00142|||http://purl.uniprot.org/uniprot/Q8IZR3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Deoxynucleoside kinase|||Disordered|||In MTDPS2 and PEOB3; reduction of activity; reduced affinity for ATP.|||In MTDPS2.|||In MTDPS2; reduction of activity in muscles.|||In MTDPS2; reduction of activity.|||In MTDPS2; severe form of combined brain and muscular atrophy; depletion of mtDNA in skeletal muscle; normal residual mtDNA in blood and fibroblasts.|||In PEOB3; reduction of activity; reduced affinity for ATP.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mitochondrion|||Proton acceptor|||Thymidine kinase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016842|||http://purl.uniprot.org/annotation/VAR_019419|||http://purl.uniprot.org/annotation/VAR_019420|||http://purl.uniprot.org/annotation/VAR_019421|||http://purl.uniprot.org/annotation/VAR_019422|||http://purl.uniprot.org/annotation/VAR_023790|||http://purl.uniprot.org/annotation/VAR_023791|||http://purl.uniprot.org/annotation/VAR_023792|||http://purl.uniprot.org/annotation/VAR_072789|||http://purl.uniprot.org/annotation/VAR_072790|||http://purl.uniprot.org/annotation/VAR_076984|||http://purl.uniprot.org/annotation/VSP_003028|||http://purl.uniprot.org/annotation/VSP_043503|||http://purl.uniprot.org/annotation/VSP_044459|||http://purl.uniprot.org/annotation/VSP_054606|||http://purl.uniprot.org/annotation/VSP_058694
http://togogenome.org/gene/9606:ADRA1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0ZBE0|||http://purl.uniprot.org/uniprot/P25100                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1D adrenergic receptor|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Pro residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069073
http://togogenome.org/gene/9606:PJA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase Praja-1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055999|||http://purl.uniprot.org/annotation/VAR_052088|||http://purl.uniprot.org/annotation/VAR_052089|||http://purl.uniprot.org/annotation/VSP_007518|||http://purl.uniprot.org/annotation/VSP_046995
http://togogenome.org/gene/9606:MRO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HEAT|||In isoform 2 and isoform 5.|||In isoform 2 and isoform 6.|||Protein maestro                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248197|||http://purl.uniprot.org/annotation/VAR_027261|||http://purl.uniprot.org/annotation/VAR_027262|||http://purl.uniprot.org/annotation/VSP_045711|||http://purl.uniprot.org/annotation/VSP_045712
http://togogenome.org/gene/9606:HCST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBK5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes stable interaction with KLRK1.|||Abrogates cell killing and interaction with GRB2. No effect on interaction with PIK3R1.|||Abrogates cell killing and interaction with PIK3R1. No effect on interaction with GRB2.|||Cytoplasmic|||Extracellular|||GRB2 binding site|||Helical|||Hematopoietic cell signal transducer|||In isoform 2.|||PIK3R1 binding site|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330287|||http://purl.uniprot.org/annotation/VSP_033022
http://togogenome.org/gene/9606:RPL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62829                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Large ribosomal subunit protein uL14|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128612
http://togogenome.org/gene/9606:EFCAB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75071                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 14|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073882|||http://purl.uniprot.org/annotation/VAR_048669|||http://purl.uniprot.org/annotation/VAR_074176
http://togogenome.org/gene/9606:TMEM169                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 169                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271039
http://togogenome.org/gene/9606:SH2D4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SQS7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||SH2|||SH2 domain-containing protein 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308600|||http://purl.uniprot.org/annotation/VAR_056987|||http://purl.uniprot.org/annotation/VAR_056988|||http://purl.uniprot.org/annotation/VSP_029009|||http://purl.uniprot.org/annotation/VSP_029010|||http://purl.uniprot.org/annotation/VSP_029011|||http://purl.uniprot.org/annotation/VSP_029012
http://togogenome.org/gene/9606:PCDHGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003948|||http://purl.uniprot.org/annotation/VAR_021882|||http://purl.uniprot.org/annotation/VAR_048555|||http://purl.uniprot.org/annotation/VSP_008659|||http://purl.uniprot.org/annotation/VSP_008660
http://togogenome.org/gene/9606:NPIPB15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Nuclear pore complex-interacting protein family member B15|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000367122
http://togogenome.org/gene/9606:TWF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IBS0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H 1|||ADF-H 2|||Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Twinfilin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233136|||http://purl.uniprot.org/annotation/VAR_042407|||http://purl.uniprot.org/annotation/VAR_042408|||http://purl.uniprot.org/annotation/VAR_042409
http://togogenome.org/gene/9606:CMTM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZV2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 8|||Helical|||In isoform 2.|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186112|||http://purl.uniprot.org/annotation/VSP_044430
http://togogenome.org/gene/9606:SLC13A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKQ4|||http://purl.uniprot.org/uniprot/Q59HF0|||http://purl.uniprot.org/uniprot/Q9UKG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Solute carrier family 13 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000172495|||http://purl.uniprot.org/annotation/VAR_057193
http://togogenome.org/gene/9606:GASK1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWH4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Golgi-associated kinase 1B|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288864|||http://purl.uniprot.org/annotation/VAR_032514|||http://purl.uniprot.org/annotation/VSP_025794|||http://purl.uniprot.org/annotation/VSP_025795|||http://purl.uniprot.org/annotation/VSP_025796
http://togogenome.org/gene/9606:ALOX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09917                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to COTL1. Impairs interaction with DICER; when associated with A-14 and A-76.|||Almost no loss of activity.|||Decreases arachidonate 5-lipoxygenase activity.|||Decreases arachidonate 5-lipoxygenase activity. Increases leukotriene A4 synthase activity.|||Does not affect arachidonate 5-lipoxygenase activity.|||Does not affect arachidonate 5-lipoxygenase activity. Does not oxygenate arachidonate typical 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine.|||Enhances affinity for arachidonic acid. Impairs arachidonate 5-lipoxygenase activity. Induces arachidonate 15-lipoxygenase activity. Oxygenates typical arachidonate 15-lipoxygenase substrates such as dihomo-gamma-linolenic acid and N-arachidonyl glycine. Synthesizes lipoxin A4 when incubated with a stable 5-lipoxygenase.|||Essential for stabilizing binding to COTL1|||Impairs interaction with DICER1; when associated with A-14 and A-103.|||Impairs interaction with DICER1; when associated with A-76 and A-103.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increases arachidonate 5-lipoxygenase activity.|||Increases arachidonate 5-lipoxygenase activity. Does not affect leukotriene A4 synthase activity.|||Lipoxygenase|||Loss of (5S)-lipoxygenase activity. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity;when associated with W-360; I-425 and M-426. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and M-426. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of linoleic acid to (13S)- and (9 S)-HODE; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and M-426. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and M-426. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and M-426. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and M-426. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and M-426.|||Loss of (5S)-lipoxygenase activity; when associated with I-425 and M-426. Loss of (5S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with I-425; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form mostly (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with I-425: M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with I-425: M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with I-425: M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with I-425: M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with I-425: M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with I-425: M-426 and I-604.|||Loss of (5S)-lipoxygenase activity; when associated with W-360 and I-425. Loss of (5S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and I-425. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; I-425 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; I-425 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; I-425 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; I-425 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; I-425 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; I-425 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; I-425 and I-604.|||Loss of (5S)-lipoxygenase activity; when associated with W-360 and M-426. Loss of (5S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360 and M-426. Exhibits a major (15S)-lipoxygenase activity; when associated with W-360; M-426 and I-604. Does not catalyze oxygenation of arachodonic acid to 5-HETE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of arachodonic acid to form in majority (15S)-HETE and (8S)-HETE but also 12-HETE; when associated with W-360; M-426 and I-604. Abolishes the LTA4-synthase activity; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of linoleic acid to (13S)- and (9S)-HODE; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of (11S)- and (11R)-deutero-linoleic acid to 9-HODE and (13S)-HODE respectively; when associated with W-360; M-426 and I-604. Catalyzes oxygenation of alpha-linolenic acid (ALA) to 13-HOTrE(n-3); when associated with W-360; M-426 and I-604. Catalyzes oxygenation of gamma-linolenic acid (GLA) to 13-HOTrE(n-6) and 10-HOTrE; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of eicosapentaenoic acid (EPA) to 12- and 15-HEPA; when associated with W-360; M-426 and I-604. Catalyzes the oxygenation of docosahexaenoic acid (DHA) to 10- and 17-HDHA; when associated with W-360; M-426 and I-604. Exhibits a lipoxin synthase activity towards (5S)-HETE as major substrates followed by (5S),(15S)-DiHETE and (15S)-HETE; when associated with W-360; M-426 and I-604.|||Loss of phosphorylation site. Permits export from the nucleus.|||No activity.|||No loss of activity.|||PLAT|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by PKA|||Polyunsaturated fatty acid 5-lipoxygenase|||Prevents phosphorylation by PKA.|||Still some substantial activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220693|||http://purl.uniprot.org/annotation/VAR_028018|||http://purl.uniprot.org/annotation/VAR_083301|||http://purl.uniprot.org/annotation/VAR_083302|||http://purl.uniprot.org/annotation/VAR_083303|||http://purl.uniprot.org/annotation/VAR_083304|||http://purl.uniprot.org/annotation/VAR_083305|||http://purl.uniprot.org/annotation/VAR_083306|||http://purl.uniprot.org/annotation/VSP_046998|||http://purl.uniprot.org/annotation/VSP_053534|||http://purl.uniprot.org/annotation/VSP_053535|||http://purl.uniprot.org/annotation/VSP_053536|||http://purl.uniprot.org/annotation/VSP_053537
http://togogenome.org/gene/9606:MRFAP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HT8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict                                                                                  ^@                                                                                  MORF4 family-associated protein 1-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318718
http://togogenome.org/gene/9606:IL33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95760                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  7-fold decrease in affinity for IL1RL1.|||8-fold decrease in affinity for IL1RL1.|||Almost abolishes binding to IL1RL1.|||Cleavage; by CTSG|||Cleavage; by ELANE|||Decreases affinity for IL1RL1.|||Homeodomain-like HTH domain|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RELA|||Interleukin-33|||Interleukin-33 (109-270)|||Interleukin-33 (95-270)|||Interleukin-33 (99-270)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096790|||http://purl.uniprot.org/annotation/PRO_0000430083|||http://purl.uniprot.org/annotation/PRO_0000430084|||http://purl.uniprot.org/annotation/PRO_0000430085|||http://purl.uniprot.org/annotation/PRO_0000430086|||http://purl.uniprot.org/annotation/VAR_049576|||http://purl.uniprot.org/annotation/VSP_042728|||http://purl.uniprot.org/annotation/VSP_044948|||http://purl.uniprot.org/annotation/VSP_045440
http://togogenome.org/gene/9606:ERICH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L0X2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Glutamate-rich protein 6|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291924|||http://purl.uniprot.org/annotation/VAR_032893|||http://purl.uniprot.org/annotation/VAR_032894|||http://purl.uniprot.org/annotation/VAR_062240|||http://purl.uniprot.org/annotation/VSP_026312|||http://purl.uniprot.org/annotation/VSP_026313
http://togogenome.org/gene/9606:PISD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UG56                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Charge relay system; for autoendoproteolytic cleavage activity|||Cleavage (non-hydrolytic); by autocatalysis|||Helical|||In LIBF; loss of autocatalytic processing; decreased protein abundance; decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization.|||In LIBF; loss of autocatalytic processing; probably decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus; decreased cell viability with increased CASP3 and CASP7 activation.|||In isoform 2.|||Loss of autocatalytic processing.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Necessary for localization to both lipid droplets and mitochondria|||Phosphatidylserine decarboxylase alpha chain|||Phosphatidylserine decarboxylase beta chain|||Phosphatidylserine decarboxylase proenzyme, mitochondrial|||Pyruvic acid (Ser); by autocatalysis|||Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029835|||http://purl.uniprot.org/annotation/PRO_0000029836|||http://purl.uniprot.org/annotation/PRO_0000435571|||http://purl.uniprot.org/annotation/VAR_084458|||http://purl.uniprot.org/annotation/VAR_084459|||http://purl.uniprot.org/annotation/VSP_007540
http://togogenome.org/gene/9606:SPACA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Sperm acrosome membrane-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248152|||http://purl.uniprot.org/annotation/VAR_027258
http://togogenome.org/gene/9606:PRPSAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP31|||http://purl.uniprot.org/uniprot/Q14558                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||Phosphoribosyl pyrophosphate synthase-associated protein 1|||Phosphoserine|||Ribose-phosphate pyrophosphokinase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141079|||http://purl.uniprot.org/annotation/VSP_039062
http://togogenome.org/gene/9606:SIK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57059                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreased kinase activity without affecting much autophosphorylation status.|||Disordered|||Does not autophosphorylation and kinase activity.|||Impaired autophosphorylation and kinase activity.|||In DEE30; no change in subcellular location.|||In a glioblastoma multiforme sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Loss of interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-473.|||Loss of kinase activity.|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Phosphothreonine; by CaMK1|||Phosphothreonine; by LKB1 and GSK3-beta|||Phosphothreonine; by PKA|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex. Reduced inhibition of CRTC3-mediated transcriptional activity.|||Protein kinase|||Proton acceptor|||RK-rich region; required for cAMP responsiveness and nuclear localization|||Reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity.|||Reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and, thus, still able to inhibit TORC activity; when associated with A-575.|||Serine/threonine-protein kinase SIK1|||Strongly reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and, thus, still able to inhibit TORC activity.|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086659|||http://purl.uniprot.org/annotation/VAR_021255|||http://purl.uniprot.org/annotation/VAR_033910|||http://purl.uniprot.org/annotation/VAR_041087|||http://purl.uniprot.org/annotation/VAR_041088|||http://purl.uniprot.org/annotation/VAR_041089|||http://purl.uniprot.org/annotation/VAR_041090|||http://purl.uniprot.org/annotation/VAR_041091|||http://purl.uniprot.org/annotation/VAR_041092|||http://purl.uniprot.org/annotation/VAR_073701|||http://purl.uniprot.org/annotation/VAR_073702|||http://purl.uniprot.org/annotation/VAR_073703
http://togogenome.org/gene/9606:MYO1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNW6                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent                                                                                  ^@                                                                                  TH1                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ZNF488                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Important for transcriptional repression activity|||In isoform 2.|||Nuclear localization signal|||Zinc finger protein 488                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047612|||http://purl.uniprot.org/annotation/VAR_033571|||http://purl.uniprot.org/annotation/VAR_033572|||http://purl.uniprot.org/annotation/VAR_033573|||http://purl.uniprot.org/annotation/VSP_055961
http://togogenome.org/gene/9606:CADM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4Z1|||http://purl.uniprot.org/uniprot/Q9BY67|||http://purl.uniprot.org/uniprot/X5D7A8|||http://purl.uniprot.org/uniprot/X5D8W0|||http://purl.uniprot.org/uniprot/X5DQR8|||http://purl.uniprot.org/uniprot/X5DQS5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule 1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes EPB41L3 binding.|||Phosphoserine|||Phosphothreonine|||Strongly reduced affinity for EPB41L3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291968|||http://purl.uniprot.org/annotation/PRO_5002621845|||http://purl.uniprot.org/annotation/PRO_5004953893|||http://purl.uniprot.org/annotation/PRO_5004954306|||http://purl.uniprot.org/annotation/PRO_5004954984|||http://purl.uniprot.org/annotation/PRO_5014110275|||http://purl.uniprot.org/annotation/VAR_061309|||http://purl.uniprot.org/annotation/VSP_047405|||http://purl.uniprot.org/annotation/VSP_047406|||http://purl.uniprot.org/annotation/VSP_047407|||http://purl.uniprot.org/annotation/VSP_052461|||http://purl.uniprot.org/annotation/VSP_052462
http://togogenome.org/gene/9606:SYCE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Synaptonemal complex central element protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262562
http://togogenome.org/gene/9606:PSPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60542                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Interchain|||Persephin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034014
http://togogenome.org/gene/9606:CASK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2RJN6|||http://purl.uniprot.org/uniprot/O14936                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||Guanylate kinase-like|||In FGS4; does not reveal significant alterations induced by the mutation substitution; causes a partial skipping of exon 2 of the protein.|||In MICPCH.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||L27|||L27 1|||L27 2|||PDZ|||Peripheral plasma membrane protein CASK|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Probable disease-associated variant found in a patient with epilepsy and pontocerebellar hypoplasia.|||Protein kinase|||Required for interaction with NRXN1 (via C-terminal tail)|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094568|||http://purl.uniprot.org/annotation/VAR_041956|||http://purl.uniprot.org/annotation/VAR_058719|||http://purl.uniprot.org/annotation/VAR_062996|||http://purl.uniprot.org/annotation/VAR_062997|||http://purl.uniprot.org/annotation/VAR_062998|||http://purl.uniprot.org/annotation/VAR_078710|||http://purl.uniprot.org/annotation/VSP_024421|||http://purl.uniprot.org/annotation/VSP_024422|||http://purl.uniprot.org/annotation/VSP_024423|||http://purl.uniprot.org/annotation/VSP_024424|||http://purl.uniprot.org/annotation/VSP_024425|||http://purl.uniprot.org/annotation/VSP_024426
http://togogenome.org/gene/9606:USP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75604                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of enzymatic activity. Increases the steady-state level of CCND1.|||Loss of enzymatic activity. Increases the steady-state level of MDM2 and MDM4 that leads to attenuation of MDM2-mediated degradation of p53/TP53 and MDM4. Increases the level of p53/TP53 and MDM4 ubiquitin conjugates.|||Necessary for interaction with MDM4|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080616|||http://purl.uniprot.org/annotation/VAR_051519|||http://purl.uniprot.org/annotation/VAR_051520|||http://purl.uniprot.org/annotation/VSP_005256|||http://purl.uniprot.org/annotation/VSP_005257|||http://purl.uniprot.org/annotation/VSP_039559|||http://purl.uniprot.org/annotation/VSP_039560
http://togogenome.org/gene/9606:ADAMTS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2XQZ0|||http://purl.uniprot.org/uniprot/Q8TE57                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 16|||Cysteine switch|||Disintegrin|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Pro residues|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029194|||http://purl.uniprot.org/annotation/PRO_0000029195|||http://purl.uniprot.org/annotation/PRO_5014586248|||http://purl.uniprot.org/annotation/VAR_057076|||http://purl.uniprot.org/annotation/VAR_057077|||http://purl.uniprot.org/annotation/VAR_057078|||http://purl.uniprot.org/annotation/VAR_057079|||http://purl.uniprot.org/annotation/VAR_057080|||http://purl.uniprot.org/annotation/VSP_007664|||http://purl.uniprot.org/annotation/VSP_007665
http://togogenome.org/gene/9606:FIBIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAL6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Fin bud initiation factor homolog|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349211
http://togogenome.org/gene/9606:FNDC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type III domain-containing protein 3B|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284891|||http://purl.uniprot.org/annotation/VAR_031856|||http://purl.uniprot.org/annotation/VAR_035921|||http://purl.uniprot.org/annotation/VAR_047814|||http://purl.uniprot.org/annotation/VSP_024739|||http://purl.uniprot.org/annotation/VSP_024740|||http://purl.uniprot.org/annotation/VSP_024741|||http://purl.uniprot.org/annotation/VSP_024742
http://togogenome.org/gene/9606:CHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14647                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CHD1 helical C-terminal domain (CHCT)|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 2|||DEAH box|||Disordered|||Found in a patient with progressive myoclonus epilepsy; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||In DEE94.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080226|||http://purl.uniprot.org/annotation/VAR_061099|||http://purl.uniprot.org/annotation/VAR_070209|||http://purl.uniprot.org/annotation/VAR_070210|||http://purl.uniprot.org/annotation/VAR_078614|||http://purl.uniprot.org/annotation/VAR_078615|||http://purl.uniprot.org/annotation/VAR_085039|||http://purl.uniprot.org/annotation/VSP_021918|||http://purl.uniprot.org/annotation/VSP_021919|||http://purl.uniprot.org/annotation/VSP_042791
http://togogenome.org/gene/9606:TMEM88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L2J3|||http://purl.uniprot.org/uniprot/Q6PEY1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 88                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251707|||http://purl.uniprot.org/annotation/VAR_027702
http://togogenome.org/gene/9606:HYAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2X3|||http://purl.uniprot.org/uniprot/A0A0S2Z3Q0|||http://purl.uniprot.org/uniprot/B3KUI5|||http://purl.uniprot.org/uniprot/Q12794                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EGF-like|||Hyaluronidase|||Hyaluronidase-1|||In MPS9.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042622|||http://purl.uniprot.org/annotation/PRO_5002790118|||http://purl.uniprot.org/annotation/PRO_5014214204|||http://purl.uniprot.org/annotation/PRO_5014239279|||http://purl.uniprot.org/annotation/VAR_023643|||http://purl.uniprot.org/annotation/VSP_015915|||http://purl.uniprot.org/annotation/VSP_015916|||http://purl.uniprot.org/annotation/VSP_015917|||http://purl.uniprot.org/annotation/VSP_015918|||http://purl.uniprot.org/annotation/VSP_015919|||http://purl.uniprot.org/annotation/VSP_015920|||http://purl.uniprot.org/annotation/VSP_015921|||http://purl.uniprot.org/annotation/VSP_015922
http://togogenome.org/gene/9606:OPRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8K2Q5|||http://purl.uniprot.org/uniprot/G8XRH4|||http://purl.uniprot.org/uniprot/G8XRH5|||http://purl.uniprot.org/uniprot/L0E130|||http://purl.uniprot.org/uniprot/P35372                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ligand binding; when associated with A-142 or S-142.|||Abolishes ligand binding; when associated with A-219 or S-219.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs interaction with calmodulin.|||In isoform 10.|||In isoform 11.|||In isoform 12, isoform 14 and isoform 15.|||In isoform 13.|||In isoform 14.|||In isoform 16.|||In isoform 17.|||In isoform 18.|||In isoform 2 and isoform 15.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Mu-type opioid receptor|||N-linked (GlcNAc...) asparagine|||NPxxY; plays a role in stabilizing the activated conformation of the receptor|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069972|||http://purl.uniprot.org/annotation/VAR_009524|||http://purl.uniprot.org/annotation/VAR_009525|||http://purl.uniprot.org/annotation/VAR_009526|||http://purl.uniprot.org/annotation/VAR_009527|||http://purl.uniprot.org/annotation/VAR_019252|||http://purl.uniprot.org/annotation/VAR_019253|||http://purl.uniprot.org/annotation/VAR_019254|||http://purl.uniprot.org/annotation/VAR_049426|||http://purl.uniprot.org/annotation/VAR_049427|||http://purl.uniprot.org/annotation/VAR_082952|||http://purl.uniprot.org/annotation/VAR_082953|||http://purl.uniprot.org/annotation/VSP_001896|||http://purl.uniprot.org/annotation/VSP_037693|||http://purl.uniprot.org/annotation/VSP_037694|||http://purl.uniprot.org/annotation/VSP_037695|||http://purl.uniprot.org/annotation/VSP_037696|||http://purl.uniprot.org/annotation/VSP_037697|||http://purl.uniprot.org/annotation/VSP_037698|||http://purl.uniprot.org/annotation/VSP_037699|||http://purl.uniprot.org/annotation/VSP_037700|||http://purl.uniprot.org/annotation/VSP_037701|||http://purl.uniprot.org/annotation/VSP_042327|||http://purl.uniprot.org/annotation/VSP_042328|||http://purl.uniprot.org/annotation/VSP_042329|||http://purl.uniprot.org/annotation/VSP_042330|||http://purl.uniprot.org/annotation/VSP_042331|||http://purl.uniprot.org/annotation/VSP_047577|||http://purl.uniprot.org/annotation/VSP_047578
http://togogenome.org/gene/9606:KLHL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59HD9|||http://purl.uniprot.org/uniprot/Q7Z6D5|||http://purl.uniprot.org/uniprot/Q96PQ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119105|||http://purl.uniprot.org/annotation/VAR_033985|||http://purl.uniprot.org/annotation/VAR_050048|||http://purl.uniprot.org/annotation/VSP_008619|||http://purl.uniprot.org/annotation/VSP_008620|||http://purl.uniprot.org/annotation/VSP_045227|||http://purl.uniprot.org/annotation/VSP_047111|||http://purl.uniprot.org/annotation/VSP_047112
http://togogenome.org/gene/9606:NCAPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Condensin complex subunit 3|||Disordered|||HEAT 1|||HEAT 10|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095041|||http://purl.uniprot.org/annotation/VAR_036125|||http://purl.uniprot.org/annotation/VAR_053041|||http://purl.uniprot.org/annotation/VAR_053042
http://togogenome.org/gene/9606:MTHFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42898|||http://purl.uniprot.org/uniprot/Q59GJ6|||http://purl.uniprot.org/uniprot/Q8IU67                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  At homozygosity reduces the risk for colorectal cancer in individuals with adequate folate status; decreased risk for adult acute leukemia; increased risk for NTDFS; increased risk for schizophrenia; thermolabile; decreased affinity for FAD cofactor; 50% reduced activity.|||Decreased risk for adult acute leukemia; thermolabile; decreased activity.|||Disordered|||In MTHFRD.|||In MTHFRD; decreased affinity for FAD cofactor.|||In MTHFRD; loss of methylenetetrahydrofolate reductase activity.|||In MTHFRD; reduced methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH.|||In MTHFRD; reduced methylenetetrahydrofolate reductase activity; reduced affinity for NADPH.|||In MTHFRD; reduces methylenetetrahydrofolate reductase activity; no effect on affinity for NADPH.|||In isoform 2.|||Loss of S-adenosylmethionine-binding.|||Methylenetetrahydrofolate reductase (NADPH)|||No effect on S-adenosylmethionine-binding.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190245|||http://purl.uniprot.org/annotation/VAR_004319|||http://purl.uniprot.org/annotation/VAR_004320|||http://purl.uniprot.org/annotation/VAR_004321|||http://purl.uniprot.org/annotation/VAR_004322|||http://purl.uniprot.org/annotation/VAR_004323|||http://purl.uniprot.org/annotation/VAR_004324|||http://purl.uniprot.org/annotation/VAR_004325|||http://purl.uniprot.org/annotation/VAR_009528|||http://purl.uniprot.org/annotation/VAR_009530|||http://purl.uniprot.org/annotation/VAR_009531|||http://purl.uniprot.org/annotation/VAR_009532|||http://purl.uniprot.org/annotation/VAR_009533|||http://purl.uniprot.org/annotation/VAR_009534|||http://purl.uniprot.org/annotation/VAR_009535|||http://purl.uniprot.org/annotation/VAR_009536|||http://purl.uniprot.org/annotation/VAR_009537|||http://purl.uniprot.org/annotation/VAR_014881|||http://purl.uniprot.org/annotation/VAR_014882|||http://purl.uniprot.org/annotation/VAR_018857|||http://purl.uniprot.org/annotation/VAR_018858|||http://purl.uniprot.org/annotation/VAR_018859|||http://purl.uniprot.org/annotation/VAR_018860|||http://purl.uniprot.org/annotation/VAR_050293|||http://purl.uniprot.org/annotation/VAR_050294|||http://purl.uniprot.org/annotation/VAR_054158|||http://purl.uniprot.org/annotation/VAR_074111|||http://purl.uniprot.org/annotation/VAR_074112|||http://purl.uniprot.org/annotation/VAR_074113|||http://purl.uniprot.org/annotation/VAR_074114|||http://purl.uniprot.org/annotation/VAR_074115|||http://purl.uniprot.org/annotation/VAR_074116|||http://purl.uniprot.org/annotation/VAR_074117|||http://purl.uniprot.org/annotation/VAR_074118|||http://purl.uniprot.org/annotation/VAR_074119|||http://purl.uniprot.org/annotation/VAR_074120|||http://purl.uniprot.org/annotation/VAR_074121|||http://purl.uniprot.org/annotation/VAR_074122|||http://purl.uniprot.org/annotation/VAR_074123|||http://purl.uniprot.org/annotation/VAR_074124|||http://purl.uniprot.org/annotation/VAR_074125|||http://purl.uniprot.org/annotation/VAR_074126|||http://purl.uniprot.org/annotation/VAR_074127|||http://purl.uniprot.org/annotation/VAR_074128|||http://purl.uniprot.org/annotation/VAR_074129|||http://purl.uniprot.org/annotation/VAR_074130|||http://purl.uniprot.org/annotation/VAR_074131|||http://purl.uniprot.org/annotation/VAR_074132|||http://purl.uniprot.org/annotation/VAR_074133|||http://purl.uniprot.org/annotation/VAR_074134|||http://purl.uniprot.org/annotation/VAR_074135|||http://purl.uniprot.org/annotation/VAR_074136|||http://purl.uniprot.org/annotation/VAR_074137|||http://purl.uniprot.org/annotation/VAR_074138|||http://purl.uniprot.org/annotation/VAR_074139|||http://purl.uniprot.org/annotation/VAR_074140|||http://purl.uniprot.org/annotation/VAR_074141|||http://purl.uniprot.org/annotation/VAR_074142|||http://purl.uniprot.org/annotation/VAR_074143|||http://purl.uniprot.org/annotation/VAR_074144|||http://purl.uniprot.org/annotation/VAR_074145|||http://purl.uniprot.org/annotation/VAR_074146|||http://purl.uniprot.org/annotation/VAR_074147|||http://purl.uniprot.org/annotation/VAR_074148|||http://purl.uniprot.org/annotation/VAR_074149|||http://purl.uniprot.org/annotation/VAR_074150|||http://purl.uniprot.org/annotation/VSP_053744
http://togogenome.org/gene/9606:TMTC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K321|||http://purl.uniprot.org/uniprot/Q6ZXV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||DUF1736|||Disordered|||Helical|||In LIS8.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Protein O-mannosyl-transferase TMTC3|||TPR|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280293|||http://purl.uniprot.org/annotation/VAR_077900|||http://purl.uniprot.org/annotation/VAR_077901|||http://purl.uniprot.org/annotation/VSP_023619
http://togogenome.org/gene/9606:ADAMDEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6V5|||http://purl.uniprot.org/uniprot/O15204                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ADAM DEC1|||Disintegrin|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029146|||http://purl.uniprot.org/annotation/PRO_0000029147|||http://purl.uniprot.org/annotation/VAR_021848|||http://purl.uniprot.org/annotation/VAR_024598|||http://purl.uniprot.org/annotation/VSP_043124
http://togogenome.org/gene/9606:ARHGAP27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUM4|||http://purl.uniprot.org/uniprot/Q8N2Y9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphothreonine|||Rho GTPase-activating protein 27|||Rho-GAP|||SH3|||WW 1|||WW 2|||WW 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317578|||http://purl.uniprot.org/annotation/VAR_038551|||http://purl.uniprot.org/annotation/VSP_031053|||http://purl.uniprot.org/annotation/VSP_031054|||http://purl.uniprot.org/annotation/VSP_031055|||http://purl.uniprot.org/annotation/VSP_031056
http://togogenome.org/gene/9606:SLC25A31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0C2                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP/ATP translocase 4|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important for transport activity|||Mitochondrial intermembrane|||Mitochondrial matrix|||Nucleotide carrier signature motif|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297624|||http://purl.uniprot.org/annotation/VAR_074177
http://togogenome.org/gene/9606:OR2A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW49|||http://purl.uniprot.org/uniprot/Q96R48                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150455|||http://purl.uniprot.org/annotation/VAR_053129|||http://purl.uniprot.org/annotation/VAR_053130|||http://purl.uniprot.org/annotation/VAR_059984
http://togogenome.org/gene/9606:PES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDF2|||http://purl.uniprot.org/uniprot/B3KTZ6|||http://purl.uniprot.org/uniprot/F6VXF5|||http://purl.uniprot.org/uniprot/O00541                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine|||Pescadillo homolog|||Reduces incorporation into the PeBoW complex and nucleolar localization and impairs maturation of 28S ribosomal RNA.|||Required for 28S ribosomal RNA processing|||Slightly impairs nucleolar localization.|||Sufficient for interaction with MAP1B|||Sufficient for nucleolar localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186188|||http://purl.uniprot.org/annotation/VAR_034375|||http://purl.uniprot.org/annotation/VAR_053570|||http://purl.uniprot.org/annotation/VAR_053571|||http://purl.uniprot.org/annotation/VSP_013023
http://togogenome.org/gene/9606:MANBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00462                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-mannosidase|||Decreased enzyme activity.|||In MANSB; complete loss of enzyme activity.|||In MANSB; nearly complete loss of enzyme activity.|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity (in vitro).|||No effect on enzyme activity (in vitro). Decreased protein stability.|||No effect on enzyme activity (in vitro). No effect on protein stability.|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012166|||http://purl.uniprot.org/annotation/VAR_026232|||http://purl.uniprot.org/annotation/VAR_026233|||http://purl.uniprot.org/annotation/VAR_059311|||http://purl.uniprot.org/annotation/VAR_081392|||http://purl.uniprot.org/annotation/VAR_081393|||http://purl.uniprot.org/annotation/VAR_081394|||http://purl.uniprot.org/annotation/VAR_081395
http://togogenome.org/gene/9606:SYNCRIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2YQN2|||http://purl.uniprot.org/uniprot/B7Z645|||http://purl.uniprot.org/uniprot/O60506|||http://purl.uniprot.org/uniprot/Q59GL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||1-5|||1-6|||1-7|||1-8|||2-1|||2-2|||2-3|||3 X 4 AA repeats of Y-Y-G-Y|||8 X 3 AA repeats of R-G-G|||Asymmetric dimethylarginine; by PRMT1|||Asymmetric dimethylarginine; by PRMT1; alternate|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein Q|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||Interaction with APOBEC1|||Interaction with SMN|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine; by PRMT1|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081867|||http://purl.uniprot.org/annotation/VSP_009581|||http://purl.uniprot.org/annotation/VSP_009582|||http://purl.uniprot.org/annotation/VSP_009583|||http://purl.uniprot.org/annotation/VSP_009584
http://togogenome.org/gene/9606:HEPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WQI6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Putative cancer susceptibility gene HEPN1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317106|||http://purl.uniprot.org/annotation/VAR_051027
http://togogenome.org/gene/9606:CYP2C18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33260|||http://purl.uniprot.org/uniprot/Q7Z348                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 2C18|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051707|||http://purl.uniprot.org/annotation/VAR_001254|||http://purl.uniprot.org/annotation/VSP_042520
http://togogenome.org/gene/9606:USP17L28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:DUSP23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI5|||http://purl.uniprot.org/uniprot/Q9BVJ7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 23|||Phosphocysteine intermediate|||Removed|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094835|||http://purl.uniprot.org/annotation/VAR_023199|||http://purl.uniprot.org/annotation/VAR_051756
http://togogenome.org/gene/9606:SLC5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13866                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.|||Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.|||Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.|||Cytoplasmic|||Extracellular|||Has no effect on water permeability.|||Has no effect on water permeation.|||Has normal D-glucose and D-galactose transporter activity.|||Helical|||Implicated in sodium coupling|||In GGM.|||In GGM; about 90% reduction in activity.|||In GGM; about 95% reduction in activity.|||In GGM; impairs trafficking to the plasma membrane.|||In GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity.|||In GGM; loss of activity.|||In GGM; requires 2 nucleotide substitutions; about 90% reduction in activity.|||In GGM; slightly decreased activity.|||In isoform 2.|||Involved in sugar-binding/transport and inhibitor binding|||Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.|||Loss of D-glucose transporter activity.|||Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.|||Loss of N-glycosylation.|||Loss of activity.|||Loss of water permeation.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Slightly reduced D-glucose transporter activity.|||Sodium/glucose cotransporter 1|||Strong reduction in D-glucose transporter activity.|||Strong reduction in water permeation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105366|||http://purl.uniprot.org/annotation/VAR_007168|||http://purl.uniprot.org/annotation/VAR_013630|||http://purl.uniprot.org/annotation/VAR_021502|||http://purl.uniprot.org/annotation/VAR_021503|||http://purl.uniprot.org/annotation/VAR_021504|||http://purl.uniprot.org/annotation/VAR_029147|||http://purl.uniprot.org/annotation/VAR_029148|||http://purl.uniprot.org/annotation/VAR_086053|||http://purl.uniprot.org/annotation/VAR_086054|||http://purl.uniprot.org/annotation/VAR_086055|||http://purl.uniprot.org/annotation/VAR_086056|||http://purl.uniprot.org/annotation/VAR_086057|||http://purl.uniprot.org/annotation/VAR_086058|||http://purl.uniprot.org/annotation/VAR_086059|||http://purl.uniprot.org/annotation/VAR_086060|||http://purl.uniprot.org/annotation/VAR_086061|||http://purl.uniprot.org/annotation/VAR_086062|||http://purl.uniprot.org/annotation/VAR_086063|||http://purl.uniprot.org/annotation/VAR_086064|||http://purl.uniprot.org/annotation/VAR_086065|||http://purl.uniprot.org/annotation/VAR_086066|||http://purl.uniprot.org/annotation/VAR_086067|||http://purl.uniprot.org/annotation/VAR_086068|||http://purl.uniprot.org/annotation/VAR_086069|||http://purl.uniprot.org/annotation/VAR_086070|||http://purl.uniprot.org/annotation/VSP_044782
http://togogenome.org/gene/9606:ASCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99929                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Achaete-scute homolog 2|||Disordered|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127130
http://togogenome.org/gene/9606:GNPDA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDQ7                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  For ring-opening step|||Glucosamine-6-phosphate isomerase 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphothreonine|||Proton acceptor; for enolization step|||Proton acceptor; for ring-opening step                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343205|||http://purl.uniprot.org/annotation/VAR_044348|||http://purl.uniprot.org/annotation/VSP_034579|||http://purl.uniprot.org/annotation/VSP_034580|||http://purl.uniprot.org/annotation/VSP_047033|||http://purl.uniprot.org/annotation/VSP_047034
http://togogenome.org/gene/9606:BDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUT1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 6|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042580|||http://purl.uniprot.org/annotation/VAR_023602|||http://purl.uniprot.org/annotation/VSP_015859|||http://purl.uniprot.org/annotation/VSP_039781
http://togogenome.org/gene/9606:C2orf81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQG2|||http://purl.uniprot.org/uniprot/A0A804HJ35|||http://purl.uniprot.org/uniprot/G3XAA6                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:JMJD1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLC8|||http://purl.uniprot.org/uniprot/Q15652                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C6-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||JmjC|||LXXLL motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable JmjC domain-containing histone demethylation protein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084284|||http://purl.uniprot.org/annotation/VAR_049654|||http://purl.uniprot.org/annotation/VAR_049655|||http://purl.uniprot.org/annotation/VAR_049656|||http://purl.uniprot.org/annotation/VAR_049657|||http://purl.uniprot.org/annotation/VAR_049658|||http://purl.uniprot.org/annotation/VAR_049659|||http://purl.uniprot.org/annotation/VAR_061277|||http://purl.uniprot.org/annotation/VSP_018303|||http://purl.uniprot.org/annotation/VSP_018304|||http://purl.uniprot.org/annotation/VSP_018305|||http://purl.uniprot.org/annotation/VSP_043909
http://togogenome.org/gene/9606:LDLRAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LDL-receptor class A|||Low-density lipoprotein receptor class A domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299377|||http://purl.uniprot.org/annotation/VAR_034812
http://togogenome.org/gene/9606:TMOD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZQ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Tropomodulin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186136|||http://purl.uniprot.org/annotation/VAR_052400|||http://purl.uniprot.org/annotation/VSP_056865
http://togogenome.org/gene/9606:PTPRQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZU1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Fibronectin type-III|||Helical|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||protein-tyrosine-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5001832099
http://togogenome.org/gene/9606:TRIM64B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI03                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Putative tripartite motif-containing protein 64B|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340247
http://togogenome.org/gene/9606:HSD11B1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5J1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Hydroxysteroid 11-beta-dehydrogenase 1-like protein|||In isoform 2, isoform 5, isoform 6 and isoform 7.|||In isoform 3 and isoform 6.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 8.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316816|||http://purl.uniprot.org/annotation/VSP_030791|||http://purl.uniprot.org/annotation/VSP_030792|||http://purl.uniprot.org/annotation/VSP_030793|||http://purl.uniprot.org/annotation/VSP_030794|||http://purl.uniprot.org/annotation/VSP_030795|||http://purl.uniprot.org/annotation/VSP_030796|||http://purl.uniprot.org/annotation/VSP_030797
http://togogenome.org/gene/9606:SBNO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Protein strawberry notch homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314560|||http://purl.uniprot.org/annotation/VSP_041216
http://togogenome.org/gene/9606:RAD21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60216                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  64-kDa C-terminal product|||Abolishes binding to SMARCA5.|||Abolishes first cleavage by ESPL1, no effect on nuclear localization.|||Abolishes interaction with SMC1.|||Abolishes second cleavage by ESPL1, no effect on nuclear localization.|||Acidic residues|||Basic and acidic residues|||Cleavage; by ESPL1|||Cleavage; by caspase-3 or caspase-7|||Disordered|||Double-strand-break repair protein rad21 homolog|||Found in a radiation-sensitive cancer patient.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CDLS4.|||In MGS; causes delayed food transit along the gut, when tested in zebrafish; may affect RUNX1 and APOB expression.|||Interaction with NIPBL|||Interaction with STAG1|||Interaction with WAPL and PDS5B|||Loss of cleavage by caspase-3 or caspase-7.|||No effect on cleavage by caspase-3 or caspase-7.|||Phosphoserine|||Phosphothreonine|||Required for interaction with SMARCA5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097872|||http://purl.uniprot.org/annotation/PRO_0000446317|||http://purl.uniprot.org/annotation/VAR_014281|||http://purl.uniprot.org/annotation/VAR_068691|||http://purl.uniprot.org/annotation/VAR_068692|||http://purl.uniprot.org/annotation/VAR_081285|||http://purl.uniprot.org/annotation/VAR_083980
http://togogenome.org/gene/9606:SMG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSL3|||http://purl.uniprot.org/uniprot/E9PD50|||http://purl.uniprot.org/uniprot/Q6TV06|||http://purl.uniprot.org/uniprot/Q92540                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with UPF1; when associated with E-163.|||Abolishes interaction with UPF1; when associated with E-66.|||Basic and acidic residues|||DNA/RNA-binding|||Disordered|||In isoform 2 and isoform 4.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG7|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||TPR 1|||TPR 2|||Telomerase activating protein Est1-like N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076324|||http://purl.uniprot.org/annotation/VAR_051363|||http://purl.uniprot.org/annotation/VAR_051364|||http://purl.uniprot.org/annotation/VSP_016574|||http://purl.uniprot.org/annotation/VSP_016575|||http://purl.uniprot.org/annotation/VSP_016576|||http://purl.uniprot.org/annotation/VSP_047130
http://togogenome.org/gene/9606:ABCA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSU4|||http://purl.uniprot.org/uniprot/O94911                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ABC-type organic anion transporter ABCA8|||Affects localization at the plasma membrane; loss of cholesterol efflux to APOA1.|||Helical|||In isoform 1.|||In isoform 2.|||Loss of expression; loss of cholesterol efflux to APOA1.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250677|||http://purl.uniprot.org/annotation/VAR_027590|||http://purl.uniprot.org/annotation/VAR_027591|||http://purl.uniprot.org/annotation/VAR_027592|||http://purl.uniprot.org/annotation/VAR_027593|||http://purl.uniprot.org/annotation/VAR_048130|||http://purl.uniprot.org/annotation/VAR_048131|||http://purl.uniprot.org/annotation/VAR_048132|||http://purl.uniprot.org/annotation/VAR_084139|||http://purl.uniprot.org/annotation/VAR_084140|||http://purl.uniprot.org/annotation/VSP_060911|||http://purl.uniprot.org/annotation/VSP_060912
http://togogenome.org/gene/9606:DEPDC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QD5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEP|||DEP domain-containing protein 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307737|||http://purl.uniprot.org/annotation/VAR_053972|||http://purl.uniprot.org/annotation/VAR_062212|||http://purl.uniprot.org/annotation/VSP_047180
http://togogenome.org/gene/9606:WNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04628                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In OI15.|||In OI15; completely fails to activate the Wnt-regulated beta-catenin signaling cascade.|||In OI15; reduced capacity to activate canonical Wnt signaling.|||In OSTEOP; associated with susceptibility to early-onset osteoporosis; completely fails to activate the Wnt-regulated beta-catenin signaling cascade.|||In OSTEOP; reduced capacity to activate canonical Wnt signaling.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Proto-oncogene Wnt-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041405|||http://purl.uniprot.org/annotation/VAR_069627|||http://purl.uniprot.org/annotation/VAR_069628|||http://purl.uniprot.org/annotation/VAR_069629|||http://purl.uniprot.org/annotation/VAR_069630|||http://purl.uniprot.org/annotation/VAR_069631|||http://purl.uniprot.org/annotation/VAR_069632|||http://purl.uniprot.org/annotation/VAR_079407|||http://purl.uniprot.org/annotation/VAR_079408
http://togogenome.org/gene/9606:GARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41250                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decrease in catalytic activity by about 10-fold.|||Decrease in catalytic activity by more than 10-fold.|||Displays 62% of wild-type catalytic activity. Displays 20% of wild-type catalytic activity; when associated with G-125.|||Found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; unknown pathological significance.|||Glycine--tRNA ligase|||Has no effect on subcellular localization; results in decreased affinity for glycine.|||In CMT2D and HMN5A; shows a large reduction in aminoacylation activity.|||In CMT2D and HMN5A; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules.|||In CMT2D.|||In CMT2D; demonstrates no change in subcellular location pattern.|||In CMT2D; phenotype overlapping with HMN5A; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type.|||In CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules.|||In CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; unknown pathological significance.|||In CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1.|||In CMT2D; shows a reduction in aminoacylation activity.|||In CMT2D; unknown pathological significance.|||In HMN5A; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1.|||In HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity.|||In HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast.|||In HMN5A; unknown pathological significance.|||In SMAJI.|||In SMAJI; loss of function; based on yeast complementation assay.|||In isoform 2.|||Loss of catalytic activity.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Probable disease-associated variant found in a patient with growth retardation, microcephaly, thinning of the corpus callosum, decreased white matter and brain stem involvement, as well as large calvaria, cerebellar vermis atrophy, dysmorphic features, prominent epicanthal folds, hypotelorism, high-arched palate, delayed motor milestones, apnea and sparse thin scalp hair; reduces to less than 1% aminoacylation activity.|||WHEP-TRS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072998|||http://purl.uniprot.org/annotation/VAR_018718|||http://purl.uniprot.org/annotation/VAR_018719|||http://purl.uniprot.org/annotation/VAR_018720|||http://purl.uniprot.org/annotation/VAR_018721|||http://purl.uniprot.org/annotation/VAR_054865|||http://purl.uniprot.org/annotation/VAR_054866|||http://purl.uniprot.org/annotation/VAR_054867|||http://purl.uniprot.org/annotation/VAR_073187|||http://purl.uniprot.org/annotation/VAR_073188|||http://purl.uniprot.org/annotation/VAR_073189|||http://purl.uniprot.org/annotation/VAR_073190|||http://purl.uniprot.org/annotation/VAR_073191|||http://purl.uniprot.org/annotation/VAR_073192|||http://purl.uniprot.org/annotation/VAR_073193|||http://purl.uniprot.org/annotation/VAR_073194|||http://purl.uniprot.org/annotation/VAR_073195|||http://purl.uniprot.org/annotation/VAR_074016|||http://purl.uniprot.org/annotation/VAR_074017|||http://purl.uniprot.org/annotation/VAR_079827|||http://purl.uniprot.org/annotation/VAR_079828|||http://purl.uniprot.org/annotation/VAR_079829|||http://purl.uniprot.org/annotation/VAR_085141|||http://purl.uniprot.org/annotation/VAR_085142|||http://purl.uniprot.org/annotation/VAR_085143|||http://purl.uniprot.org/annotation/VSP_060970
http://togogenome.org/gene/9606:LRRC56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In CILD39.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||Leucine-rich repeat-containing protein 56|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229923|||http://purl.uniprot.org/annotation/VAR_025782|||http://purl.uniprot.org/annotation/VAR_025783|||http://purl.uniprot.org/annotation/VAR_034090|||http://purl.uniprot.org/annotation/VAR_059694|||http://purl.uniprot.org/annotation/VAR_061678|||http://purl.uniprot.org/annotation/VAR_081775|||http://purl.uniprot.org/annotation/VAR_081776
http://togogenome.org/gene/9606:CMTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYT2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Adrift-type SAM-dependent 2'-O-MTase|||Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2|||Only mildly affects mRNA cap binding and catalytic activity of the enzyme.|||Proton acceptor|||Strongly reduces mRNA cap binding and catalytic activity of the enzyme.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326180|||http://purl.uniprot.org/annotation/VAR_039998|||http://purl.uniprot.org/annotation/VAR_039999|||http://purl.uniprot.org/annotation/VAR_040000|||http://purl.uniprot.org/annotation/VAR_040001|||http://purl.uniprot.org/annotation/VAR_040002
http://togogenome.org/gene/9606:NDUFS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75380|||http://purl.uniprot.org/uniprot/Q6IBC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In MC1DN9.|||Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial|||Zinc finger CHCC-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020020|||http://purl.uniprot.org/annotation/VAR_078947
http://togogenome.org/gene/9606:ALDH9A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49189                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-trimethylaminobutyraldehyde dehydrogenase|||4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed|||In allele ALDH9A1*2.|||In isoform 2.|||In isoform 3.|||N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Proton acceptor|||Removed; alternate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056485|||http://purl.uniprot.org/annotation/PRO_0000434351|||http://purl.uniprot.org/annotation/VAR_011304|||http://purl.uniprot.org/annotation/VSP_056305|||http://purl.uniprot.org/annotation/VSP_060045
http://togogenome.org/gene/9606:LBH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53QV2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||LBH|||Phosphoserine|||Protein LBH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324802
http://togogenome.org/gene/9606:XKR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GH72                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||XK-related protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190788
http://togogenome.org/gene/9606:OR5AU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVW7|||http://purl.uniprot.org/uniprot/Q8NGC0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AU1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150582|||http://purl.uniprot.org/annotation/VAR_047234|||http://purl.uniprot.org/annotation/VAR_047235|||http://purl.uniprot.org/annotation/VAR_047236|||http://purl.uniprot.org/annotation/VAR_062039|||http://purl.uniprot.org/annotation/VAR_062040
http://togogenome.org/gene/9606:SOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U3FYV6|||http://purl.uniprot.org/uniprot/P48431                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||In MCOPS3; unknown pathological significance.|||In mt1; reduced nuclear import; when associated with 56-A--A-58. In mt1.2; reduced nuclear import; when associated with 42-A-A-43 and 113-A--A-115.|||In mt1; reduced nuclear import; when associated with 56-A--A-58. In mt1.2; reduced nuclear import; when associated with 56-A--A-58 and 113-A--A-115.|||In mt2; reduced nuclear import. In mt1.2; reduced nuclear import; when associated with 42-A-A-43 and 56-A--A-58.|||Loss of interaction with L3MBTL3. Loss of ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex. Loss of interaction with PHF20L1; when associated with R-117.|||Loss of interaction with PHF20L1; when associated with R-42.|||N6-methyllysine|||Phosphoserine|||Polar residues|||Transcription factor SOX-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048715|||http://purl.uniprot.org/annotation/VAR_075627|||http://purl.uniprot.org/annotation/VAR_075628|||http://purl.uniprot.org/annotation/VAR_075629
http://togogenome.org/gene/9606:PCDH20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSZ7|||http://purl.uniprot.org/uniprot/Q8N6Y1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Protocadherin-20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004005|||http://purl.uniprot.org/annotation/VAR_036111
http://togogenome.org/gene/9606:L1CAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32004                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Decreased cell-cell adhesion; no effect on subcellular localization; no effect on neurite outgrowth.|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Found in a patient with L1 syndrome; unknown pathological significance.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In HYCX and ACCPX.|||In HYCX and MASA.|||In HYCX and MASA; also found in a patient with the diagnosis of L1 syndrome; also in a patient with hydrocephalus and Hirschsprung disease.|||In HYCX and MASA; also in a patient with hydrocephalus and Hirschsprung disease.|||In HYCX and MASA; associated with callosal agenesis; also found in a patient affected by hydrocephalus with Hirschsprung disease.|||In HYCX and MASA; decrease in neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells; decrease in cell-matrix adhesion; decreased cell migration; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells.|||In HYCX.|||In HYCX; decrease in cell-matrix adhesion; decreased cell migration; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells; no effect on neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells.|||In HYCX; partial loss of axon guidance and loss of proper synapse formation, when assayed in a heterologous system.|||In HYCX; partial loss of localization at the cell surface; retention in the endoplasmic reticulum; in neurons, partial loss of localization to axons, but enriched on proximal dendrites.|||In HYCX; severe.|||In HYCX; severe; loss of localization to the cell surface; retention in the endoplasmic reticulum; loss of axon guidance, when assayed in a heterologous system.|||In HYCX; severe; reduced axon arborization; partial loss of localization at the cell surface; retention in the endoplasmic reticulum; in neurons, restricted to cell bodies and proximal segments of processes; loss of axon guidance and of proper synapse formation, when assayed in a heterologous system.|||In MASA.|||In MASA; associated with callosal agenesis.|||In MASA; decrease in cell-matrix adhesion; decreased cell migration; loss of axon guidance and of proper synapse formation, when assayed in a heterologous system; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells; no effect on neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells.|||In MASA; decrease in neurite outgrowth, when assayed in NGF-treated pheochromocytoma PC12 cells; decrease in cell-matrix adhesion; decreased cell migration; no effect on axon guidance, on subcellular location to synaptic terminals, nor on proper synapse formation, when assayed in a heterologous system; no effect on the localization at the cell surface; no effect on cell proliferation, when transfected in pheochromocytoma PC12 cells.|||In MASA; loss of homophilic interactions at the cell surface; no effect on localization at the cell surface.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of axon guidance, when assayed in a heterologous system, but normal synapse formation.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule L1|||No effect on axon guidance activity, nor on synapse formation, when assayed in a heterologous system.|||No effect on localization at the cell surface.|||Phosphoserine|||Phosphoserine; by CaMK2|||Probable disease-associated variant found in L1 syndrome.|||Probable disease-associated variant found in L1 syndrome; loss of localization at the cell surface; retention in the endoplasmic reticulum; loss of homophilic interactions at the cell surface.|||Probable disease-associated variant found in L1 syndrome; loss of localization at the cell surface; retention in the endoplasmic reticulum; loss of transport into axons; loss of neurite outgrowth; loss of cell-cell adhesion.|||Probable disease-associated variant found in L1 syndrome; requires 2 nucleotide substitutions.|||Probable disease-associated variant found in a patient with L1 syndrome; loss of homophilic interactions at the cell surface; no effect on the localization at the cell surface. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015022|||http://purl.uniprot.org/annotation/VAR_003921|||http://purl.uniprot.org/annotation/VAR_003922|||http://purl.uniprot.org/annotation/VAR_003923|||http://purl.uniprot.org/annotation/VAR_003924|||http://purl.uniprot.org/annotation/VAR_003925|||http://purl.uniprot.org/annotation/VAR_003926|||http://purl.uniprot.org/annotation/VAR_003927|||http://purl.uniprot.org/annotation/VAR_003928|||http://purl.uniprot.org/annotation/VAR_003929|||http://purl.uniprot.org/annotation/VAR_003930|||http://purl.uniprot.org/annotation/VAR_003931|||http://purl.uniprot.org/annotation/VAR_003932|||http://purl.uniprot.org/annotation/VAR_003933|||http://purl.uniprot.org/annotation/VAR_003934|||http://purl.uniprot.org/annotation/VAR_003935|||http://purl.uniprot.org/annotation/VAR_003936|||http://purl.uniprot.org/annotation/VAR_003937|||http://purl.uniprot.org/annotation/VAR_003938|||http://purl.uniprot.org/annotation/VAR_003939|||http://purl.uniprot.org/annotation/VAR_003940|||http://purl.uniprot.org/annotation/VAR_003941|||http://purl.uniprot.org/annotation/VAR_003942|||http://purl.uniprot.org/annotation/VAR_003943|||http://purl.uniprot.org/annotation/VAR_003944|||http://purl.uniprot.org/annotation/VAR_003945|||http://purl.uniprot.org/annotation/VAR_003946|||http://purl.uniprot.org/annotation/VAR_003947|||http://purl.uniprot.org/annotation/VAR_003948|||http://purl.uniprot.org/annotation/VAR_014421|||http://purl.uniprot.org/annotation/VAR_027512|||http://purl.uniprot.org/annotation/VAR_027513|||http://purl.uniprot.org/annotation/VAR_027514|||http://purl.uniprot.org/annotation/VAR_030403|||http://purl.uniprot.org/annotation/VAR_030404|||http://purl.uniprot.org/annotation/VAR_030405|||http://purl.uniprot.org/annotation/VAR_030406|||http://purl.uniprot.org/annotation/VAR_030407|||http://purl.uniprot.org/annotation/VAR_030408|||http://purl.uniprot.org/annotation/VAR_030409|||http://purl.uniprot.org/annotation/VAR_030410|||http://purl.uniprot.org/annotation/VAR_030411|||http://purl.uniprot.org/annotation/VAR_030412|||http://purl.uniprot.org/annotation/VAR_030413|||http://purl.uniprot.org/annotation/VAR_030414|||http://purl.uniprot.org/annotation/VAR_030415|||http://purl.uniprot.org/annotation/VAR_030416|||http://purl.uniprot.org/annotation/VAR_030417|||http://purl.uniprot.org/annotation/VAR_030418|||http://purl.uniprot.org/annotation/VAR_030419|||http://purl.uniprot.org/annotation/VAR_030420|||http://purl.uniprot.org/annotation/VAR_030421|||http://purl.uniprot.org/annotation/VAR_059413|||http://purl.uniprot.org/annotation/VAR_078350|||http://purl.uniprot.org/annotation/VAR_078351|||http://purl.uniprot.org/annotation/VAR_078352|||http://purl.uniprot.org/annotation/VAR_078353|||http://purl.uniprot.org/annotation/VAR_078354|||http://purl.uniprot.org/annotation/VAR_078355|||http://purl.uniprot.org/annotation/VAR_078356|||http://purl.uniprot.org/annotation/VAR_078357|||http://purl.uniprot.org/annotation/VAR_078358|||http://purl.uniprot.org/annotation/VAR_078359|||http://purl.uniprot.org/annotation/VAR_078360|||http://purl.uniprot.org/annotation/VAR_078361|||http://purl.uniprot.org/annotation/VAR_078362|||http://purl.uniprot.org/annotation/VAR_078363|||http://purl.uniprot.org/annotation/VAR_078364|||http://purl.uniprot.org/annotation/VAR_078365|||http://purl.uniprot.org/annotation/VAR_078366|||http://purl.uniprot.org/annotation/VAR_078367|||http://purl.uniprot.org/annotation/VAR_078368|||http://purl.uniprot.org/annotation/VAR_078369|||http://purl.uniprot.org/annotation/VAR_078370|||http://purl.uniprot.org/annotation/VAR_078371|||http://purl.uniprot.org/annotation/VAR_078372|||http://purl.uniprot.org/annotation/VAR_078373|||http://purl.uniprot.org/annotation/VAR_078374|||http://purl.uniprot.org/annotation/VAR_078375|||http://purl.uniprot.org/annotation/VAR_078376|||http://purl.uniprot.org/annotation/VAR_078377|||http://purl.uniprot.org/annotation/VAR_078378|||http://purl.uniprot.org/annotation/VAR_078379|||http://purl.uniprot.org/annotation/VAR_078380|||http://purl.uniprot.org/annotation/VAR_078381|||http://purl.uniprot.org/annotation/VAR_078382|||http://purl.uniprot.org/annotation/VAR_078383|||http://purl.uniprot.org/annotation/VAR_078384|||http://purl.uniprot.org/annotation/VAR_078385|||http://purl.uniprot.org/annotation/VSP_002591|||http://purl.uniprot.org/annotation/VSP_046317
http://togogenome.org/gene/9606:TNFAIP8L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P589                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Complete loss of interaction with BTRC.|||Phosphoserine; by MAP3K7|||Tumor necrosis factor alpha-induced protein 8-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285771
http://togogenome.org/gene/9606:ATP4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR29|||http://purl.uniprot.org/uniprot/P20648|||http://purl.uniprot.org/uniprot/Q658V6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Potassium-transporting ATPase alpha chain 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046253|||http://purl.uniprot.org/annotation/VAR_019428
http://togogenome.org/gene/9606:KMT5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E3VVS3|||http://purl.uniprot.org/uniprot/Q9NQR1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone H4 binding and methyltransferase activity.|||Abolishes methyltransferase activity.|||Alters methyltransferase activity, so that both monomethylation and dimethylation take place.|||Basic and acidic residues|||Basic residues|||Disordered|||Does not affect the interaction with SIRT2. Increases the number of mitotic foci formation. Does not affect methyltransferase activity.|||In isoform 2.|||Increases affinity for histone H4.|||Increases the interaction with SIRT2. Reduces the number of mitotic foci formation. Does not affect methyltransferase activity.|||N-lysine methyltransferase KMT5A|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SET|||Strongly decreases methyltransferase activity.|||Strongly reduces affinity for histone H4 and abolishes methyltransferase activity.|||Strongly reduces affinity for histone H4 and methyltransferase activity.|||Strongly reduces affinity for histone H4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186081|||http://purl.uniprot.org/annotation/VSP_002226|||http://purl.uniprot.org/annotation/VSP_002227
http://togogenome.org/gene/9606:HIPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ33|||http://purl.uniprot.org/uniprot/Q86Z02                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeodomain-interacting protein kinase 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with TP53|||Loss of kinase activity and impaired MAP3K5-JNK inactivation.|||Loss of kinase activity.|||Nuclear localization signal 1 (NLS1)|||Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-1203.|||Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-440 and R-556.|||Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-317; R-556 and R-1203.|||Nuclear subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-25; R-440; R-556 and R-1203.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced sumoylation and cytoplasmic subcellular location. Impaired sumoylation and cytoplasmic subcellular location; when associated with R-317; R-440; R-556 and R-1203.|||Required for localization to nuclear speckles|||SUMO interaction motifs (SIM); required for nuclear localization and kinase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085993|||http://purl.uniprot.org/annotation/VAR_040546|||http://purl.uniprot.org/annotation/VAR_046047|||http://purl.uniprot.org/annotation/VAR_051626|||http://purl.uniprot.org/annotation/VSP_013127|||http://purl.uniprot.org/annotation/VSP_013128|||http://purl.uniprot.org/annotation/VSP_013129|||http://purl.uniprot.org/annotation/VSP_013130|||http://purl.uniprot.org/annotation/VSP_013131
http://togogenome.org/gene/9606:PLPPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBJ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317532
http://togogenome.org/gene/9606:ZNHIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15649                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  HIT-type|||In PEHO; increased protein degradation; decreased protein abundance; does not affect localization to cytoplasm and nucleus.|||In isoform 2.|||Phosphoserine|||Zinc finger HIT domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173550|||http://purl.uniprot.org/annotation/VAR_079193|||http://purl.uniprot.org/annotation/VSP_055155
http://togogenome.org/gene/9606:NAT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHE5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Loss of the cysteine S-conjugate N-acetyltransferase activity. No effect on protein expression.|||Lumenal|||N-acetyltransferase|||N-acetyltransferase 8|||No effect on the cysteine S-conjugate N-acetyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284684|||http://purl.uniprot.org/annotation/VAR_031805|||http://purl.uniprot.org/annotation/VAR_053886
http://togogenome.org/gene/9606:TCFL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TP4|||http://purl.uniprot.org/uniprot/Q9UL49                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BHLH|||Disordered|||In isoform 1.|||In isoform 2.|||Polar residues|||Pro residues|||R1 epitope (recognized by Chagas's antibodies)|||R3 epitope (recognized by Chagas's antibodies)|||Transcription factor-like 5 protein|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127475|||http://purl.uniprot.org/annotation/VAR_049555|||http://purl.uniprot.org/annotation/VAR_061263|||http://purl.uniprot.org/annotation/VSP_002160|||http://purl.uniprot.org/annotation/VSP_030310
http://togogenome.org/gene/9606:CCIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13939|||http://purl.uniprot.org/uniprot/Q8WWB2|||http://purl.uniprot.org/uniprot/Q8WX35                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Calicin|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119067|||http://purl.uniprot.org/annotation/VAR_050039
http://togogenome.org/gene/9606:MMAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EY8                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Corrinoid adenosyltransferase MMAB|||Disordered|||In MMAB.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005568|||http://purl.uniprot.org/annotation/VAR_017203|||http://purl.uniprot.org/annotation/VAR_017204|||http://purl.uniprot.org/annotation/VAR_017205|||http://purl.uniprot.org/annotation/VAR_017206|||http://purl.uniprot.org/annotation/VAR_017207|||http://purl.uniprot.org/annotation/VAR_017208|||http://purl.uniprot.org/annotation/VAR_023471|||http://purl.uniprot.org/annotation/VAR_038803
http://togogenome.org/gene/9606:DENND4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2RAZ6|||http://purl.uniprot.org/uniprot/Q05C90|||http://purl.uniprot.org/uniprot/Q7Z401                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||C-myc promoter-binding protein|||Disordered|||In isoform 2.|||MABP|||PPR|||PPR 1|||PPR 2|||Phosphoserine|||Polar residues|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223952|||http://purl.uniprot.org/annotation/VAR_025362|||http://purl.uniprot.org/annotation/VSP_044630
http://togogenome.org/gene/9606:BBOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75936                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Gamma-butyrobetaine dioxygenase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207085
http://togogenome.org/gene/9606:OPRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41143                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Delta-type opioid receptor|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Improved maturation and increased expression at the cell surface.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069962|||http://purl.uniprot.org/annotation/VAR_012083
http://togogenome.org/gene/9606:MAP4K5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIS2|||http://purl.uniprot.org/uniprot/B3KWC4|||http://purl.uniprot.org/uniprot/Q9Y4K4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CNH|||Disordered|||Loss of kinase activity and ability to activate JNK family.|||Mitogen-activated protein kinase kinase kinase kinase 5|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086282|||http://purl.uniprot.org/annotation/VAR_040747|||http://purl.uniprot.org/annotation/VAR_040748|||http://purl.uniprot.org/annotation/VAR_040749|||http://purl.uniprot.org/annotation/VAR_040750|||http://purl.uniprot.org/annotation/VAR_040751|||http://purl.uniprot.org/annotation/VAR_040752|||http://purl.uniprot.org/annotation/VAR_057102
http://togogenome.org/gene/9606:S100A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60903                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Ancestral calcium site|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Protein S100-A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144002
http://togogenome.org/gene/9606:CLTRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITM8|||http://purl.uniprot.org/uniprot/Q9HBJ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes dimerization. Does not affect cell membrane localization. Does not affect processing by BACE2. Abolishes dimerization; when associated with A-152.|||Cleavage by BACE2|||Collectrin|||Collectrin-like|||Cytoplasmic|||Does not affect dimerization. Does not affect cell membrane localization. Abolishes dimerization; when associated with A-186.|||Does not affet processing by BACE2.|||Extracellular|||Helical|||Increased dimerization leading to hyperoligomerized. Abolishes processing by BACE2. Abolishes localization to the cell membrane.|||Increases processing by BACE2. Decreases of protein abundance.|||Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-76.|||Loss of localization to the cell membrane. Abolishes processing by BACE2. Loss of localization to the cell membrane; when associated with I-93.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245867
http://togogenome.org/gene/9606:GOLGA8J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMD2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8J|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332313
http://togogenome.org/gene/9606:CRYBA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A097PIJ6|||http://purl.uniprot.org/uniprot/P53673                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-crystallin A4|||Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||In CTRCT23.|||In CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer.|||In CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein.|||N-acetylthreonine|||N-terminal arm|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057545|||http://purl.uniprot.org/annotation/VAR_014903|||http://purl.uniprot.org/annotation/VAR_029528|||http://purl.uniprot.org/annotation/VAR_029529|||http://purl.uniprot.org/annotation/VAR_033824|||http://purl.uniprot.org/annotation/VAR_078868
http://togogenome.org/gene/9606:CAPZA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52907                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  F-actin-capping protein subunit alpha-1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208624|||http://purl.uniprot.org/annotation/VAR_073834
http://togogenome.org/gene/9606:SETD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EWN3|||http://purl.uniprot.org/uniprot/Q9C0A6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Histone-lysine N-methyltransferase SETD5|||In MRD23.|||In MRD23; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281905|||http://purl.uniprot.org/annotation/VAR_051336|||http://purl.uniprot.org/annotation/VAR_051337|||http://purl.uniprot.org/annotation/VAR_051338|||http://purl.uniprot.org/annotation/VAR_061705|||http://purl.uniprot.org/annotation/VAR_078954|||http://purl.uniprot.org/annotation/VAR_078955|||http://purl.uniprot.org/annotation/VAR_078956|||http://purl.uniprot.org/annotation/VAR_078957|||http://purl.uniprot.org/annotation/VAR_078958|||http://purl.uniprot.org/annotation/VAR_078959|||http://purl.uniprot.org/annotation/VAR_078960|||http://purl.uniprot.org/annotation/VAR_078961|||http://purl.uniprot.org/annotation/VAR_083220|||http://purl.uniprot.org/annotation/VAR_083221|||http://purl.uniprot.org/annotation/VSP_024094|||http://purl.uniprot.org/annotation/VSP_024095
http://togogenome.org/gene/9606:TMEM266                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3C6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 111-D--L-116, 151-M--I-153, A-175, A-213 and 217-N--S-222.|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 111-D--L-116, 151-M--I-153, A-175, L-184-D-185 and 217-N--S-222.|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 111-D--L-116, 151-M--I-153, A-175, L-184-D-185 and A-213.|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 111-D--L-116, 151-M--I-153, L-184-D-185, A-213 and 217-N--S-222.|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 111-D--L-116, A-175, L-184-D-185, A-213 and 217-N--S-222.|||Despite residues related to HVCN1 channel, does not show ion channel activity; when associated with 151-M--I-153, A-175, L-184-D-185, A-213 and 217-N--S-222.|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||In isoform 2.|||Polar residues|||Transmembrane protein 266                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244094|||http://purl.uniprot.org/annotation/VAR_026880|||http://purl.uniprot.org/annotation/VAR_026881|||http://purl.uniprot.org/annotation/VSP_022108
http://togogenome.org/gene/9606:CFHR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IS28|||http://purl.uniprot.org/uniprot/A0A3B3ISW6|||http://purl.uniprot.org/uniprot/A0A8V8TQS1|||http://purl.uniprot.org/uniprot/P36980                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complement factor H-related protein 2|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005897|||http://purl.uniprot.org/annotation/PRO_5017398427|||http://purl.uniprot.org/annotation/PRO_5036466637|||http://purl.uniprot.org/annotation/VSP_001192
http://togogenome.org/gene/9606:HSPA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5G6|||http://purl.uniprot.org/uniprot/P38646                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In EVPLS.|||In SIDBA4.|||In SIDBA4; unknown pathological significance.|||Interaction with FXN and ISCU|||Interaction with NFS1|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Significant loss of interaction with FXN and ISCU. Significant increase in interaction with NFS1.|||Stress-70 protein, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013563|||http://purl.uniprot.org/annotation/VAR_046482|||http://purl.uniprot.org/annotation/VAR_046483|||http://purl.uniprot.org/annotation/VAR_049622|||http://purl.uniprot.org/annotation/VAR_049623|||http://purl.uniprot.org/annotation/VAR_076662|||http://purl.uniprot.org/annotation/VAR_076663|||http://purl.uniprot.org/annotation/VAR_076664|||http://purl.uniprot.org/annotation/VAR_076665|||http://purl.uniprot.org/annotation/VAR_076666|||http://purl.uniprot.org/annotation/VAR_076667|||http://purl.uniprot.org/annotation/VAR_076668|||http://purl.uniprot.org/annotation/VAR_076669|||http://purl.uniprot.org/annotation/VAR_076670|||http://purl.uniprot.org/annotation/VAR_076671
http://togogenome.org/gene/9606:DPP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4U2|||http://purl.uniprot.org/uniprot/B4DLA8|||http://purl.uniprot.org/uniprot/Q6V1X1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location.|||Abolishes activity; no effect on subcellular location.|||Charge relay system|||Dipeptidyl peptidase 8|||Dipeptidyl peptidase 8 /9 ,N-terminal|||Dipeptidylpeptidase IV N-terminal|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of enzyme activity. Loss of dimerization.|||Peptidase S9 prolyl oligopeptidase catalytic|||Reduced dimerization and reduced enzyme activity.|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122413|||http://purl.uniprot.org/annotation/VSP_013860|||http://purl.uniprot.org/annotation/VSP_013861|||http://purl.uniprot.org/annotation/VSP_013862|||http://purl.uniprot.org/annotation/VSP_013863|||http://purl.uniprot.org/annotation/VSP_013864
http://togogenome.org/gene/9606:FOXO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1X9RU27                                                                                  ^@                                                                                  Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Fork-head|||Pro residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RTP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Cytoplasmic|||Helical|||Receptor-transporting protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181995|||http://purl.uniprot.org/annotation/VAR_057732|||http://purl.uniprot.org/annotation/VAR_057733
http://togogenome.org/gene/9606:ROPN1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with AKAP3.|||In isoform 2.|||Interaction with RHPN1|||Phosphoserine|||RIIa|||Ropporin-1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307393|||http://purl.uniprot.org/annotation/VSP_028745
http://togogenome.org/gene/9606:VWA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GFL6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Cleavage|||EGF-like 1|||EGF-like 2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||VWFA 1|||VWFA 2|||VWFA 3|||von Willebrand factor A domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307362|||http://purl.uniprot.org/annotation/VAR_035418|||http://purl.uniprot.org/annotation/VAR_035419|||http://purl.uniprot.org/annotation/VAR_036641|||http://purl.uniprot.org/annotation/VSP_028737|||http://purl.uniprot.org/annotation/VSP_028738|||http://purl.uniprot.org/annotation/VSP_028739
http://togogenome.org/gene/9606:WDR82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXN9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 82                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279685
http://togogenome.org/gene/9606:CYB561A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H1Q2|||http://purl.uniprot.org/uniprot/Q8NBI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b561|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3|||N-linked (GlcNAc...) asparagine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314838|||http://purl.uniprot.org/annotation/VSP_047358
http://togogenome.org/gene/9606:NWD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULI1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||NACHT|||NACHT and WD repeat domain-containing protein 2|||WD 1|||WD 10|||WD 11|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320920|||http://purl.uniprot.org/annotation/VAR_039304
http://togogenome.org/gene/9606:C3orf38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPI3                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylserine|||Removed|||Uncharacterized protein C3orf38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244989|||http://purl.uniprot.org/annotation/VSP_019621
http://togogenome.org/gene/9606:FANCI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNW8|||http://purl.uniprot.org/uniprot/Q9NVI1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes monoubiquitination by FANCL and UBE2T.|||Disordered|||FANCI helical|||FANCI solenoid 1|||FANCI solenoid 1 cap|||FANCI solenoid 2|||FANCI solenoid 3|||FANCI solenoid 4|||Fanconi anemia group I protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In FANCI.|||In FANCI; abolishes function in DNA repair.|||In FANCI; benign variant; no effect on ubiquitination and DNA repair.|||In isoform 1 and isoform 2.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248376|||http://purl.uniprot.org/annotation/VAR_027278|||http://purl.uniprot.org/annotation/VAR_027279|||http://purl.uniprot.org/annotation/VAR_032689|||http://purl.uniprot.org/annotation/VAR_032690|||http://purl.uniprot.org/annotation/VAR_032691|||http://purl.uniprot.org/annotation/VAR_032692|||http://purl.uniprot.org/annotation/VSP_020257|||http://purl.uniprot.org/annotation/VSP_026069|||http://purl.uniprot.org/annotation/VSP_035606
http://togogenome.org/gene/9606:CDK5R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15078|||http://purl.uniprot.org/uniprot/Q8N619                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Absent from the cell periphery.|||Cleavage; by calpain|||Cyclin-dependent kinase 5 activator 1, p25|||Cyclin-dependent kinase 5 activator 1, p35|||Disordered|||In L-3A mutant; abolished recognition and ubiquitination by the CRL2(FEM1B) complex.|||In L-3R mutant; abolished recognition and ubiquitination by the CRL2(FEM1B) complex, while promoting recognition and ubiquitination by the CRL2(FEM1B) complex.|||Increased susceptibility to calpain.|||N-myristoyl glycine|||Phosphoserine; by CDK5|||Phosphothreonine; by CDK5|||Polar residues|||Reduced susceptibility to calpain.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004794|||http://purl.uniprot.org/annotation/PRO_0000004795
http://togogenome.org/gene/9606:OVGP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12889|||http://purl.uniprot.org/uniprot/Q86YN0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GH18|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Oviduct-specific glycoprotein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011973|||http://purl.uniprot.org/annotation/PRO_5004300531|||http://purl.uniprot.org/annotation/VAR_016109|||http://purl.uniprot.org/annotation/VAR_024459|||http://purl.uniprot.org/annotation/VAR_024460|||http://purl.uniprot.org/annotation/VAR_035752|||http://purl.uniprot.org/annotation/VAR_049199|||http://purl.uniprot.org/annotation/VAR_049200|||http://purl.uniprot.org/annotation/VAR_049201|||http://purl.uniprot.org/annotation/VAR_049202|||http://purl.uniprot.org/annotation/VAR_061190
http://togogenome.org/gene/9606:TLCD4-RWDD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/S4R434                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Helical|||TLC                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:MFSD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUT3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Influences skin pigmentation.|||Major facilitator superfamily domain-containing protein 12|||N-acetylmethionine|||Reduced localization to lysosomes and redirection to the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274522|||http://purl.uniprot.org/annotation/VAR_030309|||http://purl.uniprot.org/annotation/VAR_030310|||http://purl.uniprot.org/annotation/VAR_030311|||http://purl.uniprot.org/annotation/VAR_050300|||http://purl.uniprot.org/annotation/VAR_050301|||http://purl.uniprot.org/annotation/VSP_022779|||http://purl.uniprot.org/annotation/VSP_047665|||http://purl.uniprot.org/annotation/VSP_047666
http://togogenome.org/gene/9606:TBC1D30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VZ81|||http://purl.uniprot.org/uniprot/Q9Y2I9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of GAP activity.|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320652|||http://purl.uniprot.org/annotation/VAR_039261|||http://purl.uniprot.org/annotation/VAR_039262|||http://purl.uniprot.org/annotation/VAR_052544|||http://purl.uniprot.org/annotation/VAR_059857|||http://purl.uniprot.org/annotation/VSP_042427|||http://purl.uniprot.org/annotation/VSP_042428
http://togogenome.org/gene/9606:RSBN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCB5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Lysine-specific demethylase RSBN1L|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299414|||http://purl.uniprot.org/annotation/VSP_027658
http://togogenome.org/gene/9606:WFDC10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1F0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  WAP|||WAP four-disulfide core domain protein 10A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041387
http://togogenome.org/gene/9606:CA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43166                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 7|||In isoform 2.|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077431|||http://purl.uniprot.org/annotation/VSP_044254
http://togogenome.org/gene/9606:MAD2L1BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15013                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interaction with MAD2L1|||Loss of interaction with MAD2L1 and disruption of ability to overcome spindle checkpoint-dependent mitotic arrest; when associated with A-191.|||Loss of interaction with MAD2L1 and disruption of ability to overcome spindle checkpoint-dependent mitotic arrest; when associated with A-83.|||MAD2L1-binding protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096310|||http://purl.uniprot.org/annotation/VSP_046268
http://togogenome.org/gene/9606:GLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMG0|||http://purl.uniprot.org/uniprot/Q53GS7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In CAAHD.|||In LCCS1.|||In LCCS1; allele Fin(Major); does not affect subcellular localization.|||In isoform 2.|||Interaction with NUP155|||Interaction with NUP42|||Mediates the shuttling between the nucleus and the cytoplasm|||Phosphoserine|||Polar residues|||mRNA export factor GLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204822|||http://purl.uniprot.org/annotation/VAR_024056|||http://purl.uniprot.org/annotation/VAR_024057|||http://purl.uniprot.org/annotation/VAR_024058|||http://purl.uniprot.org/annotation/VAR_043874|||http://purl.uniprot.org/annotation/VAR_043875|||http://purl.uniprot.org/annotation/VAR_043876|||http://purl.uniprot.org/annotation/VAR_043877|||http://purl.uniprot.org/annotation/VSP_016486|||http://purl.uniprot.org/annotation/VSP_016487
http://togogenome.org/gene/9606:TPD52L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PPQ1|||http://purl.uniprot.org/uniprot/J3KNE7|||http://purl.uniprot.org/uniprot/Q15730|||http://purl.uniprot.org/uniprot/Q16890                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tumor protein D53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185741|||http://purl.uniprot.org/annotation/VAR_034568|||http://purl.uniprot.org/annotation/VSP_036751|||http://purl.uniprot.org/annotation/VSP_036752|||http://purl.uniprot.org/annotation/VSP_036753|||http://purl.uniprot.org/annotation/VSP_036754|||http://purl.uniprot.org/annotation/VSP_036755
http://togogenome.org/gene/9606:LANCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43813                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Glutathione S-transferase LANCL1|||Loss of glutathione binding.|||N-acetylalanine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191268
http://togogenome.org/gene/9606:MUC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0T3F4|||http://purl.uniprot.org/uniprot/E9PDY6|||http://purl.uniprot.org/uniprot/Q99102                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AMOP|||Cleavage|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Helical|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 15.|||In isoform 16.|||In isoform 17.|||In isoform 2.|||In isoform 3.|||In isoform 5 and isoform 10.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Mucin-4|||Mucin-4 alpha chain|||Mucin-4 beta chain|||N-linked (GlcNAc...) asparagine|||NIDO|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues|||VWFD|||Variable number of tandem repeats (VNTR)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158956|||http://purl.uniprot.org/annotation/PRO_0000274225|||http://purl.uniprot.org/annotation/PRO_0000274226|||http://purl.uniprot.org/annotation/PRO_5002630483|||http://purl.uniprot.org/annotation/PRO_5003242818|||http://purl.uniprot.org/annotation/VAR_030211|||http://purl.uniprot.org/annotation/VAR_030212|||http://purl.uniprot.org/annotation/VAR_030213|||http://purl.uniprot.org/annotation/VAR_056585|||http://purl.uniprot.org/annotation/VAR_056586|||http://purl.uniprot.org/annotation/VAR_056587|||http://purl.uniprot.org/annotation/VAR_065261|||http://purl.uniprot.org/annotation/VAR_065262|||http://purl.uniprot.org/annotation/VSP_022650|||http://purl.uniprot.org/annotation/VSP_022651|||http://purl.uniprot.org/annotation/VSP_022652|||http://purl.uniprot.org/annotation/VSP_022653|||http://purl.uniprot.org/annotation/VSP_022654|||http://purl.uniprot.org/annotation/VSP_022655|||http://purl.uniprot.org/annotation/VSP_022656|||http://purl.uniprot.org/annotation/VSP_022657|||http://purl.uniprot.org/annotation/VSP_022658|||http://purl.uniprot.org/annotation/VSP_022659|||http://purl.uniprot.org/annotation/VSP_022661|||http://purl.uniprot.org/annotation/VSP_022662|||http://purl.uniprot.org/annotation/VSP_022663|||http://purl.uniprot.org/annotation/VSP_022664|||http://purl.uniprot.org/annotation/VSP_022665|||http://purl.uniprot.org/annotation/VSP_022669|||http://purl.uniprot.org/annotation/VSP_022670|||http://purl.uniprot.org/annotation/VSP_022671|||http://purl.uniprot.org/annotation/VSP_022672|||http://purl.uniprot.org/annotation/VSP_022673|||http://purl.uniprot.org/annotation/VSP_022674|||http://purl.uniprot.org/annotation/VSP_022675
http://togogenome.org/gene/9606:HNRNPAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99729                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein A/B|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081492|||http://purl.uniprot.org/annotation/VSP_007826|||http://purl.uniprot.org/annotation/VSP_007828|||http://purl.uniprot.org/annotation/VSP_007829
http://togogenome.org/gene/9606:SLC6A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48065                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Sodium- and chloride-dependent betaine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214788|||http://purl.uniprot.org/annotation/VAR_058704
http://togogenome.org/gene/9606:POC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBT0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SOFT.|||In isoform 2.|||In isoform 3.|||POC1 centriolar protein homolog A|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231522|||http://purl.uniprot.org/annotation/VAR_057627|||http://purl.uniprot.org/annotation/VAR_057628|||http://purl.uniprot.org/annotation/VAR_068884|||http://purl.uniprot.org/annotation/VSP_017836|||http://purl.uniprot.org/annotation/VSP_046398
http://togogenome.org/gene/9606:HOXB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNJ7|||http://purl.uniprot.org/uniprot/P14651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B3|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200117|||http://purl.uniprot.org/annotation/VAR_047729|||http://purl.uniprot.org/annotation/VSP_056434|||http://purl.uniprot.org/annotation/VSP_056815
http://togogenome.org/gene/9606:DNAJB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25685|||http://purl.uniprot.org/uniprot/Q6FHS4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DnaJ homolog subfamily B member 1|||In isoform 2.|||J|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071016|||http://purl.uniprot.org/annotation/VSP_056414
http://togogenome.org/gene/9606:ZC3H13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V4I5|||http://purl.uniprot.org/uniprot/A0PJJ2|||http://purl.uniprot.org/uniprot/B3KQG8|||http://purl.uniprot.org/uniprot/Q5T200                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050778|||http://purl.uniprot.org/annotation/VAR_022727|||http://purl.uniprot.org/annotation/VSP_014252|||http://purl.uniprot.org/annotation/VSP_014253|||http://purl.uniprot.org/annotation/VSP_027202
http://togogenome.org/gene/9606:FAM76A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Polar residues|||Protein FAM76A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245760|||http://purl.uniprot.org/annotation/VSP_019771|||http://purl.uniprot.org/annotation/VSP_019772|||http://purl.uniprot.org/annotation/VSP_043250
http://togogenome.org/gene/9606:OR4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH43                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150560|||http://purl.uniprot.org/annotation/VAR_024094|||http://purl.uniprot.org/annotation/VAR_034201|||http://purl.uniprot.org/annotation/VAR_034202|||http://purl.uniprot.org/annotation/VAR_034203|||http://purl.uniprot.org/annotation/VAR_034204|||http://purl.uniprot.org/annotation/VAR_034205|||http://purl.uniprot.org/annotation/VAR_062036|||http://purl.uniprot.org/annotation/VAR_062037
http://togogenome.org/gene/9606:KIAA0825                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV33                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In PAPA10.|||In isoform 2.|||In isoform 3.|||Uncharacterized protein KIAA0825                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316781|||http://purl.uniprot.org/annotation/VAR_038391|||http://purl.uniprot.org/annotation/VAR_083052|||http://purl.uniprot.org/annotation/VSP_039414|||http://purl.uniprot.org/annotation/VSP_039415|||http://purl.uniprot.org/annotation/VSP_039416|||http://purl.uniprot.org/annotation/VSP_039417|||http://purl.uniprot.org/annotation/VSP_039418
http://togogenome.org/gene/9606:FAM133A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9E0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Protein FAM133A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287619|||http://purl.uniprot.org/annotation/VAR_053907
http://togogenome.org/gene/9606:NOMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPE7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BOS complex subunit NOMO2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021820|||http://purl.uniprot.org/annotation/VAR_016104|||http://purl.uniprot.org/annotation/VAR_034139|||http://purl.uniprot.org/annotation/VSP_013850|||http://purl.uniprot.org/annotation/VSP_053928|||http://purl.uniprot.org/annotation/VSP_053929
http://togogenome.org/gene/9606:TTLL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXZ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Probable tubulin polyglutamylase TTLL9|||TTL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324517|||http://purl.uniprot.org/annotation/VAR_039805|||http://purl.uniprot.org/annotation/VSP_035765|||http://purl.uniprot.org/annotation/VSP_035766|||http://purl.uniprot.org/annotation/VSP_035767|||http://purl.uniprot.org/annotation/VSP_035768|||http://purl.uniprot.org/annotation/VSP_035769
http://togogenome.org/gene/9606:PIGX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBF5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol-glycan biosynthesis class X protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246295|||http://purl.uniprot.org/annotation/VAR_027035|||http://purl.uniprot.org/annotation/VAR_027036|||http://purl.uniprot.org/annotation/VSP_019842
http://togogenome.org/gene/9606:ZNF746                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs DNA-binding and ability to repress PGC-1-alpha (PPARGC1A).|||In isoform 2.|||In isoform 3.|||KRAB|||No effect.|||Pro residues|||Zinc finger protein 746                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253728|||http://purl.uniprot.org/annotation/VSP_041052|||http://purl.uniprot.org/annotation/VSP_041053
http://togogenome.org/gene/9606:THAP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT49                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||HCFC1-binding motif (HBM)|||Phosphoserine|||THAP domain-containing protein 7|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068648|||http://purl.uniprot.org/annotation/VAR_060277
http://togogenome.org/gene/9606:CNIH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4P1|||http://purl.uniprot.org/uniprot/O95406                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122222
http://togogenome.org/gene/9606:AKR1E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JD6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  1,5-anhydro-D-fructose reductase|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||Lowers pKa of active site Tyr|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287880|||http://purl.uniprot.org/annotation/VAR_032356|||http://purl.uniprot.org/annotation/VAR_032357|||http://purl.uniprot.org/annotation/VSP_025614|||http://purl.uniprot.org/annotation/VSP_025615|||http://purl.uniprot.org/annotation/VSP_025616|||http://purl.uniprot.org/annotation/VSP_025617
http://togogenome.org/gene/9606:IGSF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WRI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in autosomal dominant self-limited delayed puberty; unknown pathological significance.|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||Immunoglobulin superfamily member 10|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Probable disease-associated variant found in autosomal dominant self-limited delayed puberty; the mutant protein is not secreted.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286817|||http://purl.uniprot.org/annotation/VAR_032179|||http://purl.uniprot.org/annotation/VAR_032180|||http://purl.uniprot.org/annotation/VAR_032181|||http://purl.uniprot.org/annotation/VAR_032182|||http://purl.uniprot.org/annotation/VAR_032183|||http://purl.uniprot.org/annotation/VAR_032184|||http://purl.uniprot.org/annotation/VAR_032185|||http://purl.uniprot.org/annotation/VAR_032186|||http://purl.uniprot.org/annotation/VAR_061313|||http://purl.uniprot.org/annotation/VAR_078550|||http://purl.uniprot.org/annotation/VAR_078551|||http://purl.uniprot.org/annotation/VAR_078552|||http://purl.uniprot.org/annotation/VAR_078553|||http://purl.uniprot.org/annotation/VSP_025194|||http://purl.uniprot.org/annotation/VSP_025195|||http://purl.uniprot.org/annotation/VSP_025196
http://togogenome.org/gene/9606:TSPY8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW00                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Testis-specific Y-encoded protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000408003
http://togogenome.org/gene/9606:ZCCHC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NZY4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||Disordered|||Does not affect RNA helicase activity of NEXT complex; when associated with A-673.|||Does not affect RNA helicase activity of NEXT complex; when associated with A-674.|||Does not affect RNA helicase activity of NEXT complex; when associated with A-675.|||Does not affect RNA helicase activity of NEXT complex; when associated with A-676.|||Does not alter RNA helicase activity of NEXT complex; when associated with A-662.|||Does not alter RNA helicase activity of NEXT complex; when associated with K-666.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired interaction with ZCCHC8; when associated with E-295.|||Impaired interaction with ZCCHC8; when associated with E-299.|||Impaired phosphorylation by GSK3.|||In PFBMFT5; decreased levels of mature TERC in patient cells consistent with impaired function in RNA processing; decreased levels of mutant protein in patient cells.|||In isoform 2.|||Loss of RNA helicase activity of NEXT complex; when associated with E-688.|||Loss of RNA helicase activity of NEXT complex; when associated with E-692.|||MTREX binding|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by GSK3|||Polar residues|||Pro residues|||RBM7 binding|||Reduced interaction with ZCCHC8; when associated with A-309.|||Reduced interaction with ZCCHC8; when associated with E-313.|||Removed|||Zinc finger CCHC domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150960|||http://purl.uniprot.org/annotation/VAR_034585|||http://purl.uniprot.org/annotation/VAR_083448|||http://purl.uniprot.org/annotation/VSP_013717
http://togogenome.org/gene/9606:MED13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MRD61.|||In MRD61; no effect on protein levels.|||In MRD61; unknown pathological significance.|||LXXLL motif 1|||LXXLL motif 2|||Mediator of RNA polymerase II transcription subunit 13|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065584|||http://purl.uniprot.org/annotation/VAR_057792|||http://purl.uniprot.org/annotation/VAR_057793|||http://purl.uniprot.org/annotation/VAR_083556|||http://purl.uniprot.org/annotation/VAR_083557|||http://purl.uniprot.org/annotation/VAR_083558|||http://purl.uniprot.org/annotation/VAR_083559|||http://purl.uniprot.org/annotation/VAR_083560|||http://purl.uniprot.org/annotation/VAR_083561|||http://purl.uniprot.org/annotation/VAR_083562|||http://purl.uniprot.org/annotation/VAR_083563|||http://purl.uniprot.org/annotation/VAR_083564|||http://purl.uniprot.org/annotation/VAR_083565
http://togogenome.org/gene/9606:GPSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVF5|||http://purl.uniprot.org/uniprot/A0A0A0MSK4|||http://purl.uniprot.org/uniprot/Q86YR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-protein-signaling modulator 1|||GoLoco 1|||GoLoco 2|||GoLoco 3|||GoLoco 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with STK11/LKB1|||Mediates association with membranes|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252402|||http://purl.uniprot.org/annotation/VSP_020937|||http://purl.uniprot.org/annotation/VSP_020938|||http://purl.uniprot.org/annotation/VSP_020939|||http://purl.uniprot.org/annotation/VSP_039028
http://togogenome.org/gene/9606:RECQL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46063                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA helicase Q1|||Abrogates helicase activity.|||Basic and acidic residues|||DEVH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205049|||http://purl.uniprot.org/annotation/VAR_016140|||http://purl.uniprot.org/annotation/VAR_016141|||http://purl.uniprot.org/annotation/VAR_034679|||http://purl.uniprot.org/annotation/VAR_051732
http://togogenome.org/gene/9606:SLC35E2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CK96                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Solute carrier family 35 member E2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305057
http://togogenome.org/gene/9606:CDCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5V8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||CUB domain-containing protein 1|||Cleavage; by ST14/MT-SP1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impaired association with SRC.|||Impaired association with protein kinase PRKCG but not with SRC.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226249|||http://purl.uniprot.org/annotation/VAR_025498|||http://purl.uniprot.org/annotation/VAR_025499|||http://purl.uniprot.org/annotation/VAR_055095|||http://purl.uniprot.org/annotation/VSP_017432|||http://purl.uniprot.org/annotation/VSP_017433|||http://purl.uniprot.org/annotation/VSP_017434
http://togogenome.org/gene/9606:NDST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E139|||http://purl.uniprot.org/uniprot/P52849|||http://purl.uniprot.org/uniprot/S4R438                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2|||Cytoplasmic|||Disordered|||For sulfotransferase activity|||Helical|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 2|||Heparan sulfate N-sulfotransferase 2|||Heparan sulphate-N-deacetylase|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues|||Sulfotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085212|||http://purl.uniprot.org/annotation/VSP_017403|||http://purl.uniprot.org/annotation/VSP_017404
http://togogenome.org/gene/9606:TRAF3IP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43734                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreases E3 ubiquitin ligase activity.|||Disordered|||E3 ubiquitin ligase TRAF3IP2|||In CANDF8; abolishes homotypic interactions with the SEFIR domain of IL17RA, IL17RB and IL17RC; does not affect homodimerization; does not affect SEFIR-independent interactions with other proteins.|||In PSORS13; there is a reducing binding of this variant to TRAF6.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of E3 ubiquitin ligase activity.|||Mediates interaction with TRAF6|||Polar residues|||Pro residues|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089751|||http://purl.uniprot.org/annotation/VAR_024307|||http://purl.uniprot.org/annotation/VAR_031227|||http://purl.uniprot.org/annotation/VAR_047349|||http://purl.uniprot.org/annotation/VAR_070904|||http://purl.uniprot.org/annotation/VSP_004163|||http://purl.uniprot.org/annotation/VSP_035733|||http://purl.uniprot.org/annotation/VSP_040374|||http://purl.uniprot.org/annotation/VSP_047098
http://togogenome.org/gene/9606:SEMA3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JPG5|||http://purl.uniprot.org/uniprot/Q13275|||http://purl.uniprot.org/uniprot/Q59G50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032320|||http://purl.uniprot.org/annotation/VAR_008855|||http://purl.uniprot.org/annotation/VAR_011820|||http://purl.uniprot.org/annotation/VSP_053417
http://togogenome.org/gene/9606:HOXB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17483                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B4|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200122
http://togogenome.org/gene/9606:FIBCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N539                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Complete loss of binding to acetylated bovine serum albumin and chitin.|||Complete loss of binding to acetylated bovine serum albumin and reduced binding to chitin; when associated with A-395.|||Complete loss of binding to acetylated bovine serum albumin and reduced binding to chitin; when associated with N-395.|||Cytoplasmic|||Disordered|||Extracellular|||Fibrinogen C domain-containing protein 1|||Fibrinogen C-terminal|||Helical; Signal-anchor for type II membrane protein|||Implicated in ligand binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Significantly reduced binding to acetylated bovine serum albumin and loss of binding to chitin; when associated with S-405.|||Significantly reduced binding to acetylated bovine serum albumin and loss of binding to chitin; when associated with S-431.|||Slight reduction in binding to acetylated bovine serum albumin and no effect on binding to chitin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294315|||http://purl.uniprot.org/annotation/VSP_026618|||http://purl.uniprot.org/annotation/VSP_026619|||http://purl.uniprot.org/annotation/VSP_026620
http://togogenome.org/gene/9606:OR11L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGX0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150727|||http://purl.uniprot.org/annotation/VAR_034305|||http://purl.uniprot.org/annotation/VAR_053295|||http://purl.uniprot.org/annotation/VAR_053296|||http://purl.uniprot.org/annotation/VAR_053297
http://togogenome.org/gene/9606:ACTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R694|||http://purl.uniprot.org/uniprot/P12814                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Alpha-actinin-1|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||EF-hand|||EF-hand 1|||EF-hand 2|||In BDPLT15.|||In BDPLT15; disorganization of the actin and alpha-actinin 1 filaments.|||In BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with DDN|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine; by FAK1|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073431|||http://purl.uniprot.org/annotation/VAR_053883|||http://purl.uniprot.org/annotation/VAR_053884|||http://purl.uniprot.org/annotation/VAR_069910|||http://purl.uniprot.org/annotation/VAR_069911|||http://purl.uniprot.org/annotation/VAR_069912|||http://purl.uniprot.org/annotation/VAR_069913|||http://purl.uniprot.org/annotation/VAR_069914|||http://purl.uniprot.org/annotation/VAR_069915|||http://purl.uniprot.org/annotation/VAR_069916|||http://purl.uniprot.org/annotation/VSP_041264|||http://purl.uniprot.org/annotation/VSP_043525|||http://purl.uniprot.org/annotation/VSP_047763
http://togogenome.org/gene/9606:IGFBPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WX77                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  IGFBP N-terminal|||Ig-like C2-type|||Insulin-like growth factor-binding protein-like 1|||Kazal-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297687
http://togogenome.org/gene/9606:H2AB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C5Y9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Docking domain|||Histone H2A-Bbd type 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312805
http://togogenome.org/gene/9606:ECPAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJA4                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PCNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95613                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Decrease in calmodulin binding.|||Disordered|||Found in a patient with intellectual disability, no speech, facial and limbs dysmorphisms.|||In isoform 2.|||Interaction with NEK2|||Pericentrin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Produces non-cleavable protein which remains on centrosomes in late mitosis until its levels eventually drop in cells undergoing cytokinesis.|||Stabilizes the C-terminal fragment produced by cleavage.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058257|||http://purl.uniprot.org/annotation/VAR_043878|||http://purl.uniprot.org/annotation/VAR_043879|||http://purl.uniprot.org/annotation/VAR_043880|||http://purl.uniprot.org/annotation/VAR_043881|||http://purl.uniprot.org/annotation/VAR_043882|||http://purl.uniprot.org/annotation/VAR_043883|||http://purl.uniprot.org/annotation/VAR_043884|||http://purl.uniprot.org/annotation/VAR_043885|||http://purl.uniprot.org/annotation/VAR_043886|||http://purl.uniprot.org/annotation/VAR_043887|||http://purl.uniprot.org/annotation/VAR_043888|||http://purl.uniprot.org/annotation/VAR_043889|||http://purl.uniprot.org/annotation/VAR_043890|||http://purl.uniprot.org/annotation/VAR_043891|||http://purl.uniprot.org/annotation/VAR_056961|||http://purl.uniprot.org/annotation/VAR_056962|||http://purl.uniprot.org/annotation/VAR_056963|||http://purl.uniprot.org/annotation/VAR_056964|||http://purl.uniprot.org/annotation/VAR_056965|||http://purl.uniprot.org/annotation/VAR_056966|||http://purl.uniprot.org/annotation/VAR_056967|||http://purl.uniprot.org/annotation/VAR_056968|||http://purl.uniprot.org/annotation/VAR_056969|||http://purl.uniprot.org/annotation/VAR_056970|||http://purl.uniprot.org/annotation/VAR_056971|||http://purl.uniprot.org/annotation/VAR_056972|||http://purl.uniprot.org/annotation/VAR_056973|||http://purl.uniprot.org/annotation/VAR_069420|||http://purl.uniprot.org/annotation/VAR_069421|||http://purl.uniprot.org/annotation/VSP_040104|||http://purl.uniprot.org/annotation/VSP_040105
http://togogenome.org/gene/9606:H2BC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QNW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 2-F|||In isoform 2.|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244826|||http://purl.uniprot.org/annotation/VSP_043431
http://togogenome.org/gene/9606:RHOU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L0Q8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active. Results in increased rates of stress fiber dissolution and cell migration. No effect on ARHGAP30-binding.|||Disordered|||In isoform 2.|||Loss of ARHGAP30-binding.|||Loss of GTP-binding and localization to focal adhesions. No effect on ARHGAP30-binding.|||Loss of PAK3-binding; when associated with S-81 and A-83. No effect on ARHGAP30-binding.|||Loss of binding to PAK3; when associated with A-83 and C-86.|||Loss of binding to PAK3; when associated with S-81 and C-86.|||Loss of subcellular location to plasma and intracellular membranes.|||No effect on ARHGAP30-binding.|||No effect on subcellular location.|||Rho-related GTP-binding protein RhoU|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326435|||http://purl.uniprot.org/annotation/VAR_051975|||http://purl.uniprot.org/annotation/VSP_052732|||http://purl.uniprot.org/annotation/VSP_052733
http://togogenome.org/gene/9606:POLR1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E005|||http://purl.uniprot.org/uniprot/Q9GZS1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase I subunit RPA49|||Decreased acetylation.|||Disordered|||In isoform 1.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073956|||http://purl.uniprot.org/annotation/VAR_022372|||http://purl.uniprot.org/annotation/VAR_022373|||http://purl.uniprot.org/annotation/VAR_022374|||http://purl.uniprot.org/annotation/VSP_059915
http://togogenome.org/gene/9606:MED24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75448                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||LXXLL motif 6|||Mediator of RNA polymerase II transcription subunit 24|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065582|||http://purl.uniprot.org/annotation/VAR_053969|||http://purl.uniprot.org/annotation/VSP_041125
http://togogenome.org/gene/9606:GPX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPY0|||http://purl.uniprot.org/uniprot/E7ETY7|||http://purl.uniprot.org/uniprot/J3KNB5|||http://purl.uniprot.org/uniprot/Q8TED1                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||N-acetylmethionine|||Probable glutathione peroxidase 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317756|||http://purl.uniprot.org/annotation/VAR_060456
http://togogenome.org/gene/9606:BSCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R549|||http://purl.uniprot.org/uniprot/Q96G97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In CGL2; increases localization to nuclear envelope; no effect on its interaction with LDAF1; no rescue of aberrant lipid droplet formation in BSCL2-knockdown cells.|||In SPG17 and HMN5C; also found in patients with hereditary motor and sensory neuropathy type 2; does not affect the function in lipid storage.|||In SPG17 and HMN5C; does not affect protein subcellular location.|||In isoform 2.|||In isoform 3.|||Loss of oligomerization and function in lipid droplet biogenesis; when associated with R-67; A-70; D-156; D-169 and A-175.|||Loss of oligomerization and function in lipid droplet formation; when associated with A-70; A-151; D-156; D-169 and A-175.|||Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-151; D-156; D-169 and A-175.|||Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-156 and A-175.|||Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-156 and D-169.|||Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-169 and A-175.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Seipin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191679|||http://purl.uniprot.org/annotation/VAR_022375|||http://purl.uniprot.org/annotation/VAR_022376|||http://purl.uniprot.org/annotation/VAR_022377|||http://purl.uniprot.org/annotation/VSP_044545|||http://purl.uniprot.org/annotation/VSP_051726|||http://purl.uniprot.org/annotation/VSP_051727
http://togogenome.org/gene/9606:SNAPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SXM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes SNAPC2-binding.|||Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1.|||Basic and acidic residues|||Basic residues|||Decreased binding to SNAPC2.|||Disordered|||H-T-H motif|||HTH myb-type 1|||HTH myb-type 2|||HTH myb-type 3|||Myb-like 1|||Myb-like 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SNAPC2-binding|||SNAPC5-binding|||snRNA-activating protein complex subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197120|||http://purl.uniprot.org/annotation/VAR_050193|||http://purl.uniprot.org/annotation/VAR_050194|||http://purl.uniprot.org/annotation/VAR_059455
http://togogenome.org/gene/9606:KTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Kinectin|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084337|||http://purl.uniprot.org/annotation/VAR_016206|||http://purl.uniprot.org/annotation/VAR_035931|||http://purl.uniprot.org/annotation/VAR_035932|||http://purl.uniprot.org/annotation/VAR_079266|||http://purl.uniprot.org/annotation/VSP_007981|||http://purl.uniprot.org/annotation/VSP_007982|||http://purl.uniprot.org/annotation/VSP_043207
http://togogenome.org/gene/9606:PPP2R1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7B7|||http://purl.uniprot.org/uniprot/P30153                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  HEAT|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In MRD36.|||In MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA.|||In MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA.|||In MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA.|||N-acetylalanine|||N6-acetyllysine|||PP2A subunit B binding|||PP2A subunit C binding|||Polyoma small and medium T antigens Binding|||Removed|||SV40 small T antigen binding|||Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071400|||http://purl.uniprot.org/annotation/VAR_073718|||http://purl.uniprot.org/annotation/VAR_074488|||http://purl.uniprot.org/annotation/VAR_074489|||http://purl.uniprot.org/annotation/VAR_074490
http://togogenome.org/gene/9606:OR6C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW05|||http://purl.uniprot.org/uniprot/Q9NZP2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150624|||http://purl.uniprot.org/annotation/VAR_034243|||http://purl.uniprot.org/annotation/VAR_034244
http://togogenome.org/gene/9606:RAD51D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75771                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA repair protein RAD51 homolog 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||preferentially binds ssDNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122942|||http://purl.uniprot.org/annotation/VAR_020560|||http://purl.uniprot.org/annotation/VAR_020561|||http://purl.uniprot.org/annotation/VAR_020562|||http://purl.uniprot.org/annotation/VAR_020563|||http://purl.uniprot.org/annotation/VAR_020564|||http://purl.uniprot.org/annotation/VAR_079271|||http://purl.uniprot.org/annotation/VSP_005558|||http://purl.uniprot.org/annotation/VSP_005559|||http://purl.uniprot.org/annotation/VSP_005560|||http://purl.uniprot.org/annotation/VSP_005561|||http://purl.uniprot.org/annotation/VSP_005562|||http://purl.uniprot.org/annotation/VSP_005563|||http://purl.uniprot.org/annotation/VSP_005564|||http://purl.uniprot.org/annotation/VSP_005565|||http://purl.uniprot.org/annotation/VSP_005566|||http://purl.uniprot.org/annotation/VSP_043658
http://togogenome.org/gene/9606:UGT1A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60656|||http://purl.uniprot.org/uniprot/Q5DSZ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036008|||http://purl.uniprot.org/annotation/PRO_5014205882|||http://purl.uniprot.org/annotation/VAR_036035|||http://purl.uniprot.org/annotation/VAR_058587|||http://purl.uniprot.org/annotation/VSP_053965
http://togogenome.org/gene/9606:UQCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW78                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC3DN9; decreases protein abundance; reduces complex III formation; reduces complex III activity.|||Loss of localization to the mitochondria.|||Mediates lipid-binding|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome-c reductase complex assembly factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022611|||http://purl.uniprot.org/annotation/VAR_071864
http://togogenome.org/gene/9606:FAM20A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4Y3|||http://purl.uniprot.org/uniprot/L8B8N7|||http://purl.uniprot.org/uniprot/Q8IYA5|||http://purl.uniprot.org/uniprot/Q96MK3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Able to hydrolyze ATP and display some protein kinase activity.|||Disordered|||FAM20 C-terminal|||In AI1G.|||In AI1G; impaired folding of the protein; abolishes ability to activate FAM20C protein kinase activity.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pseudokinase FAM20A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008743|||http://purl.uniprot.org/annotation/VAR_059282|||http://purl.uniprot.org/annotation/VAR_059283|||http://purl.uniprot.org/annotation/VAR_066859|||http://purl.uniprot.org/annotation/VAR_072170|||http://purl.uniprot.org/annotation/VAR_072171|||http://purl.uniprot.org/annotation/VAR_072172
http://togogenome.org/gene/9606:ACTL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-like protein 9|||Disordered|||In SPGF53; unknown pathological significance; abolishes interaction with ACTL7A.|||In SPGF53; unknown pathological significance; reduces interaction with ACTL7A.|||In a colorectal cancer sample; somatic mutation.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332297|||http://purl.uniprot.org/annotation/VAR_043000|||http://purl.uniprot.org/annotation/VAR_043001|||http://purl.uniprot.org/annotation/VAR_043002|||http://purl.uniprot.org/annotation/VAR_043003|||http://purl.uniprot.org/annotation/VAR_043004|||http://purl.uniprot.org/annotation/VAR_085431|||http://purl.uniprot.org/annotation/VAR_085432|||http://purl.uniprot.org/annotation/VAR_085433
http://togogenome.org/gene/9606:CD79B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40259                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B-cell antigen receptor complex-associated protein beta chain|||Cytoplasmic|||Extracellular|||Helical|||ITAM|||Ig-like V-type|||In AGM6.|||In isoform 3.|||In isoform Short.|||Interchain (with C-119 in alpha chain)|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014560|||http://purl.uniprot.org/annotation/VAR_057833|||http://purl.uniprot.org/annotation/VSP_002477|||http://purl.uniprot.org/annotation/VSP_047222
http://togogenome.org/gene/9606:KLHL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBE8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242157
http://togogenome.org/gene/9606:TUBA4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68366                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||In ALS22.|||In ALS22; displays significantly different distribution in terms of incorporation into microtubules.|||In ALS22; displays significantly different distribution in terms of incorporation into microtubules; destabilizes the microtubule network.|||In ALS22; displays significantly lower levels of dimer assembly.|||In isoform 2.|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Tubulin alpha-4A chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048106|||http://purl.uniprot.org/annotation/VAR_072714|||http://purl.uniprot.org/annotation/VAR_072715|||http://purl.uniprot.org/annotation/VAR_072716|||http://purl.uniprot.org/annotation/VAR_072717|||http://purl.uniprot.org/annotation/VAR_072718|||http://purl.uniprot.org/annotation/VSP_055194
http://togogenome.org/gene/9606:NPEPPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z899|||http://purl.uniprot.org/uniprot/E9PLK3|||http://purl.uniprot.org/uniprot/P55786                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||Aminopeptidase N-like N-terminal|||ERAP1-like C-terminal|||In isoform 2.|||Nuclear localization signal|||Peptidase M1 membrane alanine aminopeptidase|||Proton acceptor|||Puromycin-sensitive aminopeptidase|||Reduces catalytic activity by 1,000-fold to 2,500-fold.|||Reduces catalytic activity by 25,000-fold to 100,000-fold.|||Reduces catalytic activity by 300,000-fold to 500,000-fold.|||Reduces catalytic activity by 5,000-fold to 15,000-fold.|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095116|||http://purl.uniprot.org/annotation/VSP_056446|||http://purl.uniprot.org/annotation/VSP_056447
http://togogenome.org/gene/9606:FGD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV73                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 6|||FYVE-type|||In isoform 2.|||PH 1|||PH 2|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080952|||http://purl.uniprot.org/annotation/VAR_024286|||http://purl.uniprot.org/annotation/VAR_051985|||http://purl.uniprot.org/annotation/VSP_013091|||http://purl.uniprot.org/annotation/VSP_013092
http://togogenome.org/gene/9606:ITGB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26012|||http://purl.uniprot.org/uniprot/Q9BUG9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In isoform 2.|||Integrin beta|||Integrin beta subunit VWA|||Integrin beta-8|||N-linked (GlcNAc...) asparagine|||PSI|||VWFA|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016354|||http://purl.uniprot.org/annotation/PRO_5014312665|||http://purl.uniprot.org/annotation/VAR_034028|||http://purl.uniprot.org/annotation/VSP_056531
http://togogenome.org/gene/9606:LETM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95202                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Benign variant; no effect on mitochondrial potassium ion transmembrane transport; it fully rescues defective proton/potassium exchange in letm1-deficient yeast.|||Disordered|||EF-hand|||Helical|||In CONDMIM; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast.|||In CONDMIM; homozygous patient cells show abnormal mitochondrial morphology and altered levels of components of the oxidative phosphorylation machinery; loss of function in mitochondrial potassium ion transmembrane transport; does not rescue defective proton/potassium exchange in letm1-deficient yeast.|||In CONDMIM; homozygous patient cells show altered levels of components of the oxidative phosphorylation machinery; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast.|||In CONDMIM; unknown pathological significance.|||In CONDMIM; unknown pathological significance; decreased function in mitochondrial potassium ion transmembrane transport; does not fully rescue defective proton/potassium exchange in letm1-deficient yeast.|||In isoform 2 and isoform 3.|||In isoform 2.|||Letm1 RBD|||Loss of ability to complement growth defects and morphologic defects of mitochondria in letm1-deficient yeast mutant; when associated with A-382 and A-383.|||Loss of ability to complement growth defects and morphologic defects of mitochondria in letm1-deficient yeast mutant; when associated with A-382 and A-384.|||Loss of ability to complement growth defects and morphologic defects of mitochondria in letm1-deficient yeast mutant; when associated with A-383 and A-384.|||Loss of ability to complement morphologic defects of mitochondria in letm1-deficient yeast mutant. Slightly supports growth of letm1-deficient yeast mutant on minimal essential medium.|||Loss of phosphorylation by PINK1.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial proton/calcium exchanger protein|||Mitochondrion|||N6-acetyllysine|||No effect on mitochondrial potassium ion transmembrane transport; it fully rescues defective proton/potassium exchange in letm1-deficient yeast.|||Phosphomimetic mutant. Increased rate of calcium export from mitochondria.|||Phosphothreonine; by PINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017694|||http://purl.uniprot.org/annotation/VAR_087731|||http://purl.uniprot.org/annotation/VAR_087732|||http://purl.uniprot.org/annotation/VAR_087733|||http://purl.uniprot.org/annotation/VAR_087734|||http://purl.uniprot.org/annotation/VAR_087735|||http://purl.uniprot.org/annotation/VAR_087736|||http://purl.uniprot.org/annotation/VAR_087737|||http://purl.uniprot.org/annotation/VAR_087738|||http://purl.uniprot.org/annotation/VAR_087739|||http://purl.uniprot.org/annotation/VSP_037814|||http://purl.uniprot.org/annotation/VSP_037815|||http://purl.uniprot.org/annotation/VSP_037816
http://togogenome.org/gene/9606:ZNF317                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 1 and isoform 3.|||In isoform 3 and isoform 4.|||KRAB|||Zinc finger protein 317                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047526|||http://purl.uniprot.org/annotation/VAR_019980|||http://purl.uniprot.org/annotation/VSP_006915|||http://purl.uniprot.org/annotation/VSP_006916
http://togogenome.org/gene/9606:KIF2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF1|||http://purl.uniprot.org/uniprot/B7Z6Q6|||http://purl.uniprot.org/uniprot/B7Z7M6|||http://purl.uniprot.org/uniprot/Q99661                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-109 and E-111.|||Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-109.|||Alters interaction with MAPRE1 and association with microtubule growing ends; when associated with E-95 and E-111.|||Disordered|||Globular|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF2C|||Loss of interaction with MAPRE1 and association with microtubule growing ends.|||Microtubule tip localization signal|||N-acetylalanine|||Negative regulator of microtubule-binding|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by AURKB|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125418|||http://purl.uniprot.org/annotation/VAR_049683|||http://purl.uniprot.org/annotation/VSP_002866
http://togogenome.org/gene/9606:PIGM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3S5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Almost abolishes enzyme activity.|||Cytoplasmic|||GPI mannosyltransferase 1|||Helical|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246213|||http://purl.uniprot.org/annotation/VAR_027026
http://togogenome.org/gene/9606:NUBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53384                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic Fe-S cluster assembly factor NUBP1|||In isoform 2.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184943|||http://purl.uniprot.org/annotation/VAR_020359|||http://purl.uniprot.org/annotation/VSP_029043
http://togogenome.org/gene/9606:ALG11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAA5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Does not affect function.|||GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase|||Helical|||In CDG1P.|||In CDG1P; does not affect subcellular localization; results in the accumulation of under-glycosylated proteins.|||Loss of function.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295616|||http://purl.uniprot.org/annotation/VAR_055902|||http://purl.uniprot.org/annotation/VAR_064908|||http://purl.uniprot.org/annotation/VAR_068070|||http://purl.uniprot.org/annotation/VAR_068071|||http://purl.uniprot.org/annotation/VAR_068072|||http://purl.uniprot.org/annotation/VAR_068073
http://togogenome.org/gene/9606:ZNF41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51814                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7 and isoform 2.|||In isoform 7 and isoform 8.|||KRAB|||Rare variant found in patients with X-linked intellectual disability; unknown pathological significance.|||Zinc finger protein 41                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047374|||http://purl.uniprot.org/annotation/VAR_021785|||http://purl.uniprot.org/annotation/VAR_021786|||http://purl.uniprot.org/annotation/VAR_021787|||http://purl.uniprot.org/annotation/VSP_006883|||http://purl.uniprot.org/annotation/VSP_006884|||http://purl.uniprot.org/annotation/VSP_006885|||http://purl.uniprot.org/annotation/VSP_006886|||http://purl.uniprot.org/annotation/VSP_006887|||http://purl.uniprot.org/annotation/VSP_006888
http://togogenome.org/gene/9606:MIB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||E3 ubiquitin-protein ligase MIB1|||Found in a patient with severe intellectual disability, psychomotor delay, no speech, sleep disturbances, feeding problems, abnormal breething, deep-set eyes and short philtrum.|||In LVNC7.|||MIB/HERC2 1|||MIB/HERC2 2|||Phosphoserine|||RING-type 1|||RING-type 2|||RING-type 3|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055943|||http://purl.uniprot.org/annotation/VAR_069385|||http://purl.uniprot.org/annotation/VAR_069620
http://togogenome.org/gene/9606:OXA1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNA0|||http://purl.uniprot.org/uniprot/Q15070|||http://purl.uniprot.org/uniprot/Q2M1J6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Increases homooligomer formation in presence or absence of magnesium.|||Increases strongly homooligomer formation in presence of magnesium, but weakly in absence of magnesium.|||Increases weakly homooligomer formation in presence of magnesium, but strongly in absence of magnesium.|||Increases weakly homooligomer formation in presence or absence of magnesium.|||Membrane insertase YidC/Oxa/ALB C-terminal|||Mitochondrial inner membrane protein OXA1L|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020352|||http://purl.uniprot.org/annotation/VAR_014932|||http://purl.uniprot.org/annotation/VAR_014933|||http://purl.uniprot.org/annotation/VSP_008942|||http://purl.uniprot.org/annotation/VSP_008943|||http://purl.uniprot.org/annotation/VSP_008944|||http://purl.uniprot.org/annotation/VSP_008945
http://togogenome.org/gene/9606:SPRY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43610                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein sprouty homolog 3|||SPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076904|||http://purl.uniprot.org/annotation/VAR_034519
http://togogenome.org/gene/9606:PNPLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AD5                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished ubiquitination by PEX2.|||Cytoplasmic|||DGA/G|||Disordered|||Extracellular|||GXGXXG|||GXSXG|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In NLSDM.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 2|||Phosphoserine|||Phosphoserine; by PKA and FAM20C|||Phosphoserine; in vitro|||Proton acceptor|||Reduces rate of lipid hydrolysis; does not affect the localization around the rim of the adiposomes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292527|||http://purl.uniprot.org/annotation/VAR_032995|||http://purl.uniprot.org/annotation/VAR_032996|||http://purl.uniprot.org/annotation/VAR_032997|||http://purl.uniprot.org/annotation/VAR_032998|||http://purl.uniprot.org/annotation/VSP_026421
http://togogenome.org/gene/9606:CPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15169                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Carboxypeptidase N catalytic chain|||Catalytic|||Disordered|||In CPND.|||O-linked (GalNAc...) threonine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004394|||http://purl.uniprot.org/annotation/VAR_042415
http://togogenome.org/gene/9606:TTI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43156                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2 in response to growth factor deprivation and subsequent ubiquitination and degradation.|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphoserine; by CK2|||TELO2-interacting protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050751|||http://purl.uniprot.org/annotation/VAR_014082|||http://purl.uniprot.org/annotation/VAR_014083|||http://purl.uniprot.org/annotation/VAR_034033|||http://purl.uniprot.org/annotation/VAR_034034|||http://purl.uniprot.org/annotation/VAR_049509
http://togogenome.org/gene/9606:ANXA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08758                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Removed|||[IL]-x-C-x-x-[DE] motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067487
http://togogenome.org/gene/9606:SIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z6B4|||http://purl.uniprot.org/uniprot/Q9H173                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Interaction with HSPA5 and localization to the endoplasmic reticulum|||N-linked (GlcNAc...) asparagine|||Nucleotide exchange factor SIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223354|||http://purl.uniprot.org/annotation/PRO_5006608351|||http://purl.uniprot.org/annotation/VAR_034495
http://togogenome.org/gene/9606:BCAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWE2|||http://purl.uniprot.org/uniprot/P56945                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Breast cancer anti-estrogen resistance protein 1|||CAS family C-terminal|||Disordered|||Divergent helix-loop-helix motif|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||SH3|||SH3-binding|||Serine rich protein interaction|||Substrate for kinases|||Weakens interaction with SH2D3C.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064854|||http://purl.uniprot.org/annotation/VAR_035798|||http://purl.uniprot.org/annotation/VAR_057820|||http://purl.uniprot.org/annotation/VAR_057821|||http://purl.uniprot.org/annotation/VAR_058970|||http://purl.uniprot.org/annotation/VSP_043559|||http://purl.uniprot.org/annotation/VSP_045355|||http://purl.uniprot.org/annotation/VSP_046127|||http://purl.uniprot.org/annotation/VSP_046128|||http://purl.uniprot.org/annotation/VSP_046748|||http://purl.uniprot.org/annotation/VSP_046749|||http://purl.uniprot.org/annotation/VSP_046750|||http://purl.uniprot.org/annotation/VSP_046751
http://togogenome.org/gene/9606:GABRE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78334                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit epsilon|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000471|||http://purl.uniprot.org/annotation/VAR_048175|||http://purl.uniprot.org/annotation/VAR_071089|||http://purl.uniprot.org/annotation/VSP_055776|||http://purl.uniprot.org/annotation/VSP_055777
http://togogenome.org/gene/9606:PPIAL4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H284                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420907
http://togogenome.org/gene/9606:ADAM17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNB2|||http://purl.uniprot.org/uniprot/P78536                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Crambin-like|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 17|||Disordered|||Extracellular|||Helical|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK14|||Pro residues|||SH3-binding|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029088|||http://purl.uniprot.org/annotation/PRO_0000029089|||http://purl.uniprot.org/annotation/PRO_5014298339|||http://purl.uniprot.org/annotation/VAR_051586|||http://purl.uniprot.org/annotation/VAR_051587|||http://purl.uniprot.org/annotation/VSP_005478
http://togogenome.org/gene/9606:ASCL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XD76                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Achaete-scute homolog 4|||Disordered|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317297
http://togogenome.org/gene/9606:PRKAR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R5T5|||http://purl.uniprot.org/uniprot/P10644                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Dimerization and phosphorylation|||Disordered|||Impairs response of PKA to c-AMP.|||In ACRDYS1.|||In ACRDYS1; disrupts cAMP binding.|||In ACRDYS1; impairs response of PKA to c-AMP.|||In ACRDYS1; reduces PKA activity; decreases cAMP binding.|||In ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation.|||In CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit.|||In CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation.|||In CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation.|||In isoform 2.|||Interchain (with C-18)|||Interchain (with C-39)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Pseudophosphorylation motif|||cAMP-dependent protein kinase type I-alpha regulatory subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205377|||http://purl.uniprot.org/annotation/VAR_046894|||http://purl.uniprot.org/annotation/VAR_046895|||http://purl.uniprot.org/annotation/VAR_046896|||http://purl.uniprot.org/annotation/VAR_046897|||http://purl.uniprot.org/annotation/VAR_046898|||http://purl.uniprot.org/annotation/VAR_046899|||http://purl.uniprot.org/annotation/VAR_068241|||http://purl.uniprot.org/annotation/VAR_069456|||http://purl.uniprot.org/annotation/VAR_069457|||http://purl.uniprot.org/annotation/VAR_069458|||http://purl.uniprot.org/annotation/VAR_069459|||http://purl.uniprot.org/annotation/VAR_069460|||http://purl.uniprot.org/annotation/VAR_069461|||http://purl.uniprot.org/annotation/VAR_069462|||http://purl.uniprot.org/annotation/VAR_069463|||http://purl.uniprot.org/annotation/VAR_069464|||http://purl.uniprot.org/annotation/VAR_069465|||http://purl.uniprot.org/annotation/VAR_075533|||http://purl.uniprot.org/annotation/VSP_054833|||http://purl.uniprot.org/annotation/VSP_054834
http://togogenome.org/gene/9606:ALG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BKT4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215447
http://togogenome.org/gene/9606:MORN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ52                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||MORN 1|||MORN 2|||MORN 3|||MORN repeat-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292840|||http://purl.uniprot.org/annotation/VSP_055496
http://togogenome.org/gene/9606:HACD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWC8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313730|||http://purl.uniprot.org/annotation/VAR_037714
http://togogenome.org/gene/9606:RNF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76064                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with ATM-phosphorylated MDC1. Abolishes interaction with human herpesvirus 1 ICP0. Abolishes recruitment to DNA damage sites after UV irradiation, ionizing radiation, or treatment with an alkylating agent.|||Abolishes ubiquitin-ligase activity.|||Disordered|||Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes.|||E3 ubiquitin-protein ligase RNF8|||FHA|||Impairs interaction with UBE2L6/UBCH8 and ability to mediate 'Lys-48'-linked ubiquitination E3 ligase activity, while it still catalyzes 'Lys-63'-linked ubiquitination and still interacts with UBE2N/UBC13.|||In isoform 2.|||In isoform 3.|||Marked reduction of E2-dependent ubiquitination of histone H2A. Loss of UBE2E2- and UBE2N-binding. Loss of nuclear localization.|||Phosphoserine|||Polar residues|||RING-type|||Required for interaction with PIWIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056048|||http://purl.uniprot.org/annotation/VAR_052096|||http://purl.uniprot.org/annotation/VAR_052097|||http://purl.uniprot.org/annotation/VSP_036671|||http://purl.uniprot.org/annotation/VSP_037831|||http://purl.uniprot.org/annotation/VSP_054037|||http://purl.uniprot.org/annotation/VSP_054038
http://togogenome.org/gene/9606:DNAI4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVI9|||http://purl.uniprot.org/uniprot/Q5VTH9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dynein axonemal intermediate chain 4|||In isoform 2.|||In isoform 3.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262773|||http://purl.uniprot.org/annotation/VAR_057635|||http://purl.uniprot.org/annotation/VAR_057636|||http://purl.uniprot.org/annotation/VAR_057637|||http://purl.uniprot.org/annotation/VSP_021812|||http://purl.uniprot.org/annotation/VSP_021815|||http://purl.uniprot.org/annotation/VSP_021816|||http://purl.uniprot.org/annotation/VSP_021817
http://togogenome.org/gene/9606:TET3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43151                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes methylcytosine dioxygenase activity.|||CXXC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In BEFAHRS.|||In BEFAHRS; decreases methylcytosine dioxygenase activity.|||In BEFAHRS; unknown pathological significance; no effect on methylcytosine dioxygenase activity.|||In isoform 2.|||In isoform 3.|||Interaction with DNA|||Methylcytosine dioxygenase TET3|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050750|||http://purl.uniprot.org/annotation/VAR_062235|||http://purl.uniprot.org/annotation/VAR_083831|||http://purl.uniprot.org/annotation/VAR_083832|||http://purl.uniprot.org/annotation/VAR_083833|||http://purl.uniprot.org/annotation/VAR_083834|||http://purl.uniprot.org/annotation/VAR_083835|||http://purl.uniprot.org/annotation/VAR_083836|||http://purl.uniprot.org/annotation/VAR_083837|||http://purl.uniprot.org/annotation/VAR_083838|||http://purl.uniprot.org/annotation/VSP_021628|||http://purl.uniprot.org/annotation/VSP_034192
http://togogenome.org/gene/9606:TMEM86A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2M4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Lysoplasmalogenase TMEM86A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201838|||http://purl.uniprot.org/annotation/VAR_034564
http://togogenome.org/gene/9606:CXCL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2A7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-X-C motif chemokine 16|||Chemokine|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005118|||http://purl.uniprot.org/annotation/VAR_015424|||http://purl.uniprot.org/annotation/VAR_015425
http://togogenome.org/gene/9606:CHI3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36222                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chitinase-3-like protein 1|||GH18|||Important for AKT1 activation and IL8 production|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011965|||http://purl.uniprot.org/annotation/VAR_019838|||http://purl.uniprot.org/annotation/VAR_019839
http://togogenome.org/gene/9606:DRAXIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Draxin|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273243|||http://purl.uniprot.org/annotation/VAR_030114
http://togogenome.org/gene/9606:NIPSNAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQI7|||http://purl.uniprot.org/uniprot/Q9BPW8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NIPSNAP|||Phosphoserine|||Protein NipSnap homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221146|||http://purl.uniprot.org/annotation/VAR_011630
http://togogenome.org/gene/9606:MRPS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82932                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Small ribosomal subunit protein bS6m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000176892
http://togogenome.org/gene/9606:PIEZO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92508                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Does not inactivate the protein. gives rise to mechanically activated currents that inactivate more slowly than wild-type currents, suggesting it could shift the channel kinetics from phasic to tonic.|||Extracellular|||Found in Er(4-) blood group phenotype that is associated with hemolytic disease of the fetus and newborn.|||Found in Er(5-) blood group phenotype that is associated with hemolytic disease of the fetus and newborn.|||Found in Er(a-b+) and Er(a-b-) blood group phenotypes.|||Found in Er(a-b+) blood group phenotype.|||Found in Er(a-b-) blood group phenotype.|||Helical|||In DHS1.|||In DHS1; gives rise to mechanically activated currents that inactivate more slowly than wild-type currents.|||In DHS1; increased cation transport in erythroid cells.|||In LMPHM6; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Piezo-type mechanosensitive ion channel component 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186817|||http://purl.uniprot.org/annotation/VAR_069822|||http://purl.uniprot.org/annotation/VAR_069823|||http://purl.uniprot.org/annotation/VAR_069824|||http://purl.uniprot.org/annotation/VAR_069825|||http://purl.uniprot.org/annotation/VAR_069826|||http://purl.uniprot.org/annotation/VAR_069827|||http://purl.uniprot.org/annotation/VAR_069828|||http://purl.uniprot.org/annotation/VAR_069829|||http://purl.uniprot.org/annotation/VAR_069830|||http://purl.uniprot.org/annotation/VAR_069831|||http://purl.uniprot.org/annotation/VAR_069832|||http://purl.uniprot.org/annotation/VAR_069833|||http://purl.uniprot.org/annotation/VAR_069834|||http://purl.uniprot.org/annotation/VAR_069835|||http://purl.uniprot.org/annotation/VAR_076407|||http://purl.uniprot.org/annotation/VAR_076408|||http://purl.uniprot.org/annotation/VAR_076409|||http://purl.uniprot.org/annotation/VAR_076410|||http://purl.uniprot.org/annotation/VAR_088145|||http://purl.uniprot.org/annotation/VAR_088146|||http://purl.uniprot.org/annotation/VAR_088147|||http://purl.uniprot.org/annotation/VAR_088148|||http://purl.uniprot.org/annotation/VAR_088149|||http://purl.uniprot.org/annotation/VAR_088150
http://togogenome.org/gene/9606:NAXE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Found in a patient with progressive myoclonus epilepsy and developmental delay; unknown pathological significance.|||In PEBEL1.|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||NAD(P)H-hydrate epimerase|||Phosphoserine|||YjeF N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000067606|||http://purl.uniprot.org/annotation/VAR_032992|||http://purl.uniprot.org/annotation/VAR_077991|||http://purl.uniprot.org/annotation/VAR_077992|||http://purl.uniprot.org/annotation/VAR_077993|||http://purl.uniprot.org/annotation/VAR_085045|||http://purl.uniprot.org/annotation/VSP_026417
http://togogenome.org/gene/9606:SLITRK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5Y7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT 1|||LRRNT 2|||SLIT and NTRK-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032683|||http://purl.uniprot.org/annotation/VAR_027758|||http://purl.uniprot.org/annotation/VAR_027759|||http://purl.uniprot.org/annotation/VAR_027760
http://togogenome.org/gene/9606:APOH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKM6|||http://purl.uniprot.org/uniprot/P02749                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-2-glycoprotein 1|||In allele APOH*1.|||In allele APOH*3W; loss of phosphatidylserine-binding.|||Loss of phosphatidylserine-binding.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002059|||http://purl.uniprot.org/annotation/PRO_5033787711|||http://purl.uniprot.org/annotation/VAR_000673|||http://purl.uniprot.org/annotation/VAR_008169|||http://purl.uniprot.org/annotation/VAR_008170|||http://purl.uniprot.org/annotation/VAR_008171|||http://purl.uniprot.org/annotation/VAR_019155|||http://purl.uniprot.org/annotation/VAR_048316
http://togogenome.org/gene/9606:NR0B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15466                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In early-onset obesity; Japanese population; loss of methylation and repressor activity.|||In early-onset obesity; Japanese population; loss of repressor activity.|||In early-onset obesity; Japanese population; slight decrease of repressor activity.|||In early-onset obesity; Japanese population; strong decrease of repressor activity.|||NR LBD|||No effect on repressor activity.|||Nuclear receptor subfamily 0 group B member 2|||Symmetric dimethylarginine; by PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053752|||http://purl.uniprot.org/annotation/VAR_026015|||http://purl.uniprot.org/annotation/VAR_026016|||http://purl.uniprot.org/annotation/VAR_026017|||http://purl.uniprot.org/annotation/VAR_026018|||http://purl.uniprot.org/annotation/VAR_026019|||http://purl.uniprot.org/annotation/VAR_050584
http://togogenome.org/gene/9606:ZNF408                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXY4|||http://purl.uniprot.org/uniprot/Q9H9D4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In EVR6; severely decreased localization to the nucleus.|||In EVR6; unknown pathological significance; does not affect localization to the nucleus.|||In RP72; decreased localization to the nucleus.|||Phosphothreonine|||Polar residues|||Zinc finger protein 408                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047569|||http://purl.uniprot.org/annotation/VAR_052823|||http://purl.uniprot.org/annotation/VAR_074612|||http://purl.uniprot.org/annotation/VAR_074613|||http://purl.uniprot.org/annotation/VAR_074614|||http://purl.uniprot.org/annotation/VAR_074615|||http://purl.uniprot.org/annotation/VAR_074616
http://togogenome.org/gene/9606:C9orf153                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TBE3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Uncharacterized protein C9orf153                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229730|||http://purl.uniprot.org/annotation/VSP_017734
http://togogenome.org/gene/9606:SUGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7W3|||http://purl.uniprot.org/uniprot/B4DYC6|||http://purl.uniprot.org/uniprot/Q9Y2Z0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  CS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein SGT1 homolog|||Removed|||SGS|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106332|||http://purl.uniprot.org/annotation/VSP_013420
http://togogenome.org/gene/9606:OR7D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RA2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150648|||http://purl.uniprot.org/annotation/VAR_053235
http://togogenome.org/gene/9606:MATN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15232                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||In EDM5.|||In EDM5; bilateral hereditary microepiphyseal dysplasia.|||In EDM5; retained and accumulates within the cell.|||In SEMDBCD.|||In isoform 2.|||Matrilin-3|||Omega-N-methylarginine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Secreted normally as the wild-type.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007657|||http://purl.uniprot.org/annotation/VAR_013691|||http://purl.uniprot.org/annotation/VAR_013692|||http://purl.uniprot.org/annotation/VAR_015852|||http://purl.uniprot.org/annotation/VAR_019881|||http://purl.uniprot.org/annotation/VAR_019882|||http://purl.uniprot.org/annotation/VAR_019883|||http://purl.uniprot.org/annotation/VAR_019884|||http://purl.uniprot.org/annotation/VAR_019885|||http://purl.uniprot.org/annotation/VAR_019886|||http://purl.uniprot.org/annotation/VAR_019887|||http://purl.uniprot.org/annotation/VAR_019888|||http://purl.uniprot.org/annotation/VAR_020844|||http://purl.uniprot.org/annotation/VAR_054807|||http://purl.uniprot.org/annotation/VAR_054808|||http://purl.uniprot.org/annotation/VAR_054809|||http://purl.uniprot.org/annotation/VAR_066830|||http://purl.uniprot.org/annotation/VAR_066831|||http://purl.uniprot.org/annotation/VAR_066832|||http://purl.uniprot.org/annotation/VAR_066833|||http://purl.uniprot.org/annotation/VAR_066834|||http://purl.uniprot.org/annotation/VSP_054374
http://togogenome.org/gene/9606:LIMCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2J4|||http://purl.uniprot.org/uniprot/B7Z656|||http://purl.uniprot.org/uniprot/D6RD46|||http://purl.uniprot.org/uniprot/E9PDJ9|||http://purl.uniprot.org/uniprot/G5EA03|||http://purl.uniprot.org/uniprot/Q9UPQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform 2, isoform 4, isoform 5, isoform 6, isoform 8, isoform 9 and isoform 10.|||In isoform 3, isoform 4, isoform 5, isoform 6, isoform 8, isoform 9 and isoform 10.|||In isoform 3, isoform 5, isoform 7 and isoform 8.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4, isoform 5 and isoform 9.|||In isoform 6 and isoform 9.|||In isoform 7.|||LIM and calponin homology domains-containing protein 1|||LIM zinc-binding|||Mediates interaction with MYH9|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293619|||http://purl.uniprot.org/annotation/VAR_033105|||http://purl.uniprot.org/annotation/VSP_026541|||http://purl.uniprot.org/annotation/VSP_026542|||http://purl.uniprot.org/annotation/VSP_026543|||http://purl.uniprot.org/annotation/VSP_026544|||http://purl.uniprot.org/annotation/VSP_026545|||http://purl.uniprot.org/annotation/VSP_026546|||http://purl.uniprot.org/annotation/VSP_026547|||http://purl.uniprot.org/annotation/VSP_026548|||http://purl.uniprot.org/annotation/VSP_026549|||http://purl.uniprot.org/annotation/VSP_026550
http://togogenome.org/gene/9606:EMC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5UCC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||ER membrane protein complex subunit 10|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315048|||http://purl.uniprot.org/annotation/VSP_030473
http://togogenome.org/gene/9606:ARPC5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 5-like protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279480
http://togogenome.org/gene/9606:HKDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT70|||http://purl.uniprot.org/uniprot/Q2TB90                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Hexokinase 1|||Hexokinase 2|||Hexokinase C-terminal|||Hexokinase HKDC1|||Hexokinase N-terminal|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||In RP92; unknown pathological significance; slightly decreased hexokinase activity.|||In isoform 2.|||In isoform 3.|||Mitochondrial-binding peptide (MBP)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299035|||http://purl.uniprot.org/annotation/VAR_034776|||http://purl.uniprot.org/annotation/VAR_034777|||http://purl.uniprot.org/annotation/VAR_034778|||http://purl.uniprot.org/annotation/VAR_034779|||http://purl.uniprot.org/annotation/VAR_034780|||http://purl.uniprot.org/annotation/VAR_086465|||http://purl.uniprot.org/annotation/VSP_027533|||http://purl.uniprot.org/annotation/VSP_027534|||http://purl.uniprot.org/annotation/VSP_027535|||http://purl.uniprot.org/annotation/VSP_027536
http://togogenome.org/gene/9606:AUTS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Autism susceptibility gene 2 protein|||Basic and acidic residues|||Disordered|||Important for regulation of lamellipodia formation|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 5.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064767|||http://purl.uniprot.org/annotation/VAR_013864|||http://purl.uniprot.org/annotation/VSP_003792|||http://purl.uniprot.org/annotation/VSP_043556|||http://purl.uniprot.org/annotation/VSP_043557|||http://purl.uniprot.org/annotation/VSP_057063
http://togogenome.org/gene/9606:AHCTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A.T hook|||Basic and acidic residues|||Disordered|||Important for nuclear localization|||Important for nuclear localization and chromatin binding|||In isoform 2.|||In isoform 3.|||Mediates transcriptional activity|||Necessary for cytoplasmic localization|||Necessary for nuclear localization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein ELYS|||Seven-bladed beta propeller repeats                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246319|||http://purl.uniprot.org/annotation/VAR_027037|||http://purl.uniprot.org/annotation/VAR_027038|||http://purl.uniprot.org/annotation/VSP_019844|||http://purl.uniprot.org/annotation/VSP_042691
http://togogenome.org/gene/9606:ACSM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUN0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A synthetase ACSM5, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306101|||http://purl.uniprot.org/annotation/VAR_035252|||http://purl.uniprot.org/annotation/VAR_035253|||http://purl.uniprot.org/annotation/VAR_035254|||http://purl.uniprot.org/annotation/VAR_035255|||http://purl.uniprot.org/annotation/VAR_055495|||http://purl.uniprot.org/annotation/VAR_055496|||http://purl.uniprot.org/annotation/VAR_061011|||http://purl.uniprot.org/annotation/VSP_028398
http://togogenome.org/gene/9606:HBM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1K0FU50|||http://purl.uniprot.org/uniprot/Q6B0K9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit mu|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282855
http://togogenome.org/gene/9606:DECR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16698                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor|||Reduces enzyme activity by 97%.|||Reduces enzyme activity by 99%. Strongly reduced affinity for substrate and for NADP.|||Reduces enzyme activity by over 99%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031965|||http://purl.uniprot.org/annotation/VAR_012034|||http://purl.uniprot.org/annotation/VSP_056388
http://togogenome.org/gene/9606:CUTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTM9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Copper homeostasis protein cutC homolog|||In a breast cancer sample; somatic mutation.|||Reduces copper binding. Reduces copper binding by 75%; when associated with A-31.|||Reduces copper binding. Reduces copper binding by 75%; when associated with A-52.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215088|||http://purl.uniprot.org/annotation/VAR_036363
http://togogenome.org/gene/9606:DISC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C4P094|||http://purl.uniprot.org/uniprot/C4P096|||http://purl.uniprot.org/uniprot/C4P098|||http://purl.uniprot.org/uniprot/C4P0A4|||http://purl.uniprot.org/uniprot/C4P0A5|||http://purl.uniprot.org/uniprot/C4P0C4|||http://purl.uniprot.org/uniprot/C4P0C8|||http://purl.uniprot.org/uniprot/C4P0D0|||http://purl.uniprot.org/uniprot/C4P0D1|||http://purl.uniprot.org/uniprot/C4P0D2|||http://purl.uniprot.org/uniprot/C4P0D3|||http://purl.uniprot.org/uniprot/Q9NRI5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Associated with susceptibility to schizoaffective disorder.|||Disordered|||Disrupted in schizophrenia 1 protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs interaction with NDEL1; when associated with P-815.|||Impairs interaction with NDEL1; when associated with P-822.|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with ATF4 and ATF5|||Interaction with FBXW7|||Interaction with MAP1A|||Interaction with NDEL1|||Interaction with PAFAH1B1|||Interaction with TRAF3IP1|||Necessary and sufficient for interaction with PCNT and localization at the centrosome|||Reduced ubiquitination.|||Required for localization to punctate cytoplasmic foci                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079916|||http://purl.uniprot.org/annotation/VAR_022437|||http://purl.uniprot.org/annotation/VAR_022438|||http://purl.uniprot.org/annotation/VAR_026704|||http://purl.uniprot.org/annotation/VAR_030422|||http://purl.uniprot.org/annotation/VAR_050954|||http://purl.uniprot.org/annotation/VAR_061642|||http://purl.uniprot.org/annotation/VAR_061643|||http://purl.uniprot.org/annotation/VAR_061644|||http://purl.uniprot.org/annotation/VSP_003849|||http://purl.uniprot.org/annotation/VSP_019314|||http://purl.uniprot.org/annotation/VSP_019315|||http://purl.uniprot.org/annotation/VSP_019316|||http://purl.uniprot.org/annotation/VSP_019317|||http://purl.uniprot.org/annotation/VSP_043214|||http://purl.uniprot.org/annotation/VSP_043583|||http://purl.uniprot.org/annotation/VSP_043584|||http://purl.uniprot.org/annotation/VSP_043585|||http://purl.uniprot.org/annotation/VSP_043586|||http://purl.uniprot.org/annotation/VSP_043587|||http://purl.uniprot.org/annotation/VSP_043588|||http://purl.uniprot.org/annotation/VSP_047525|||http://purl.uniprot.org/annotation/VSP_047526|||http://purl.uniprot.org/annotation/VSP_047527|||http://purl.uniprot.org/annotation/VSP_047528|||http://purl.uniprot.org/annotation/VSP_047529|||http://purl.uniprot.org/annotation/VSP_047530|||http://purl.uniprot.org/annotation/VSP_047531
http://togogenome.org/gene/9606:CPTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA50|||http://purl.uniprot.org/uniprot/S4S694                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  Abolishes phosphoceramide transfer.|||Ceramide-1-phosphate transfer protein|||Glycolipid transfer protein|||Increases phosphoceramide transfer.|||Nearly abolishes phosphoceramide transfer.|||Nearly abolishes phosphoceramide transfer. Induces autophagy in a dominant negative manner.|||No effect.|||Reduces phosphoceramide transfer.|||Slightly decreases phosphoceramide transfer.|||Slightly reduces phosphoceramide transfer.|||Strongly reduces phosphoceramide transfer.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317156
http://togogenome.org/gene/9606:RBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10745                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X approximate tandem repeats|||Disordered|||In RP66; abolishes secretion; results in mis-folded insoluble complexes degraded via the ER-associated protein catabolic process.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Retinol-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021523|||http://purl.uniprot.org/annotation/VAR_035929|||http://purl.uniprot.org/annotation/VAR_051315|||http://purl.uniprot.org/annotation/VAR_069669|||http://purl.uniprot.org/annotation/VAR_069670|||http://purl.uniprot.org/annotation/VAR_069671|||http://purl.uniprot.org/annotation/VAR_069672|||http://purl.uniprot.org/annotation/VAR_069673|||http://purl.uniprot.org/annotation/VAR_069674|||http://purl.uniprot.org/annotation/VAR_069675|||http://purl.uniprot.org/annotation/VAR_069676|||http://purl.uniprot.org/annotation/VAR_069677|||http://purl.uniprot.org/annotation/VAR_069678|||http://purl.uniprot.org/annotation/VAR_069679|||http://purl.uniprot.org/annotation/VAR_069680|||http://purl.uniprot.org/annotation/VAR_069681|||http://purl.uniprot.org/annotation/VAR_069682|||http://purl.uniprot.org/annotation/VAR_069683|||http://purl.uniprot.org/annotation/VAR_069684|||http://purl.uniprot.org/annotation/VAR_069685|||http://purl.uniprot.org/annotation/VAR_069686|||http://purl.uniprot.org/annotation/VAR_069687|||http://purl.uniprot.org/annotation/VAR_069688|||http://purl.uniprot.org/annotation/VAR_069689|||http://purl.uniprot.org/annotation/VAR_069690|||http://purl.uniprot.org/annotation/VAR_069691|||http://purl.uniprot.org/annotation/VAR_069692|||http://purl.uniprot.org/annotation/VAR_069693|||http://purl.uniprot.org/annotation/VAR_069694|||http://purl.uniprot.org/annotation/VAR_069695|||http://purl.uniprot.org/annotation/VAR_069696|||http://purl.uniprot.org/annotation/VAR_069697|||http://purl.uniprot.org/annotation/VAR_069698|||http://purl.uniprot.org/annotation/VAR_069699|||http://purl.uniprot.org/annotation/VAR_069700|||http://purl.uniprot.org/annotation/VAR_069701|||http://purl.uniprot.org/annotation/VAR_069702|||http://purl.uniprot.org/annotation/VAR_069703|||http://purl.uniprot.org/annotation/VAR_069704|||http://purl.uniprot.org/annotation/VAR_069705|||http://purl.uniprot.org/annotation/VAR_069706|||http://purl.uniprot.org/annotation/VAR_069707
http://togogenome.org/gene/9606:UBQLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJZ3|||http://purl.uniprot.org/uniprot/Q9H347                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Polar residues|||STI1|||UBA|||Ubiquilin-3|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211013|||http://purl.uniprot.org/annotation/VAR_020363|||http://purl.uniprot.org/annotation/VAR_034578|||http://purl.uniprot.org/annotation/VAR_052681|||http://purl.uniprot.org/annotation/VAR_052682|||http://purl.uniprot.org/annotation/VAR_052683|||http://purl.uniprot.org/annotation/VAR_052684
http://togogenome.org/gene/9606:SH3BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6E5|||http://purl.uniprot.org/uniprot/P78314                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In CRBM.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphotyrosine; by SYK|||Polar residues|||Pro residues|||SH2|||SH3 domain-binding protein 2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064365|||http://purl.uniprot.org/annotation/VAR_013257|||http://purl.uniprot.org/annotation/VAR_013258|||http://purl.uniprot.org/annotation/VAR_013259|||http://purl.uniprot.org/annotation/VAR_013260|||http://purl.uniprot.org/annotation/VAR_013261|||http://purl.uniprot.org/annotation/VAR_013262|||http://purl.uniprot.org/annotation/VAR_013263|||http://purl.uniprot.org/annotation/VSP_004085|||http://purl.uniprot.org/annotation/VSP_004086|||http://purl.uniprot.org/annotation/VSP_043636|||http://purl.uniprot.org/annotation/VSP_055046
http://togogenome.org/gene/9606:TLX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43711                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||T-cell leukemia homeobox protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049338
http://togogenome.org/gene/9606:COX6A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02221                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 6A2, mitochondrial|||Helical|||In MC4DN18; reduced complex IV assembly; decreased COX6A2 protein stability.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006116|||http://purl.uniprot.org/annotation/VAR_084183|||http://purl.uniprot.org/annotation/VAR_084184
http://togogenome.org/gene/9606:DUSP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEJ0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolishes most of in vitro phosphatase activity.|||Dual specificity protein phosphatase 18|||No effect on in vitro phosphatase activity.|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094828
http://togogenome.org/gene/9606:ZNF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXT5|||http://purl.uniprot.org/uniprot/P17022                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||In isoform 2.|||KRAB|||SCAN box|||Zinc finger protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047340|||http://purl.uniprot.org/annotation/VAR_024835|||http://purl.uniprot.org/annotation/VAR_024836|||http://purl.uniprot.org/annotation/VSP_016947
http://togogenome.org/gene/9606:PPP2R5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13362                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 4.|||In isoform 5.|||In isoform Gamma-1.|||In isoform Gamma-2 and isoform 4.|||N-acetylmethionine|||Nuclear localization signal|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071457|||http://purl.uniprot.org/annotation/VAR_051745|||http://purl.uniprot.org/annotation/VSP_005112|||http://purl.uniprot.org/annotation/VSP_005113|||http://purl.uniprot.org/annotation/VSP_043645|||http://purl.uniprot.org/annotation/VSP_046768
http://togogenome.org/gene/9606:SLC20A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7LNJ1|||http://purl.uniprot.org/uniprot/Q8WUM9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  A|||Drastic reduction of virus infectibility, but conserved virus binding ability.|||Helical|||Loss of sodium-dependent phosphate transporter activity. Able to restore cell proliferation in SLC20A1-deficient HeLa cells to a level identical to that observed in their wild-type counterpart. No effect on its localization to the cell membrane.|||Loss of virus infectibility.|||Phosphoserine|||Sodium-dependent phosphate transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080771
http://togogenome.org/gene/9606:MTCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4B5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Microtubule cross-linking factor 1|||Necessary for colocalization and binding with microtubules|||Necessary for interaction with MARK2 and apicobasal microtubule bundle formation in polarized epithelial cells|||Necessary for self-assembly, microtubule bundling activity and apicobasal microtubule organization|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280113|||http://purl.uniprot.org/annotation/VAR_031073|||http://purl.uniprot.org/annotation/VAR_031074|||http://purl.uniprot.org/annotation/VAR_031075|||http://purl.uniprot.org/annotation/VAR_031076|||http://purl.uniprot.org/annotation/VAR_055942|||http://purl.uniprot.org/annotation/VSP_023549|||http://purl.uniprot.org/annotation/VSP_023550|||http://purl.uniprot.org/annotation/VSP_023551|||http://purl.uniprot.org/annotation/VSP_023552|||http://purl.uniprot.org/annotation/VSP_023553|||http://purl.uniprot.org/annotation/VSP_023554
http://togogenome.org/gene/9606:PCDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0E7|||http://purl.uniprot.org/uniprot/B4DUA8|||http://purl.uniprot.org/uniprot/B4E2D8|||http://purl.uniprot.org/uniprot/Q08174                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000354078|||http://purl.uniprot.org/annotation/PRO_5002804067|||http://purl.uniprot.org/annotation/VAR_047530|||http://purl.uniprot.org/annotation/VAR_047531|||http://purl.uniprot.org/annotation/VAR_047532|||http://purl.uniprot.org/annotation/VSP_000703
http://togogenome.org/gene/9606:ZNF233                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK53|||http://purl.uniprot.org/uniprot/K7ER86                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 233                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304407|||http://purl.uniprot.org/annotation/VAR_035022|||http://purl.uniprot.org/annotation/VAR_035023
http://togogenome.org/gene/9606:STEAP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NZ63                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||STEAP family member 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321512|||http://purl.uniprot.org/annotation/VAR_039339|||http://purl.uniprot.org/annotation/VAR_039340|||http://purl.uniprot.org/annotation/VAR_039341|||http://purl.uniprot.org/annotation/VAR_039342|||http://purl.uniprot.org/annotation/VSP_054116|||http://purl.uniprot.org/annotation/VSP_054117
http://togogenome.org/gene/9606:KRTAP19-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU57|||http://purl.uniprot.org/uniprot/Q3LI70                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue                                                                                  ^@                                                                                  Chain|||Non-terminal Residue                                                                                  ^@                                                                                  Keratin-associated protein 19-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223908
http://togogenome.org/gene/9606:RASSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50749                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Ras association domain-containing protein 2|||Ras-associating|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097172|||http://purl.uniprot.org/annotation/VAR_035825|||http://purl.uniprot.org/annotation/VSP_055851|||http://purl.uniprot.org/annotation/VSP_055852
http://togogenome.org/gene/9606:CD99L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RC16|||http://purl.uniprot.org/uniprot/Q8TCZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CD99 antigen-like protein 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340092|||http://purl.uniprot.org/annotation/VSP_034181|||http://purl.uniprot.org/annotation/VSP_034182|||http://purl.uniprot.org/annotation/VSP_034183|||http://purl.uniprot.org/annotation/VSP_034184|||http://purl.uniprot.org/annotation/VSP_034185|||http://purl.uniprot.org/annotation/VSP_041815|||http://purl.uniprot.org/annotation/VSP_041816|||http://purl.uniprot.org/annotation/VSP_044663
http://togogenome.org/gene/9606:THG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E366|||http://purl.uniprot.org/uniprot/Q9H8R6|||http://purl.uniprot.org/uniprot/Q9NWX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes oligomerization. Loss of enzyme activity.|||Found in a patient with a severe multisystemic growth disorder and cerebellar atrophy; unknown pathological significance.|||In SCAR28; decreased mitochondrial fusion.|||Loss of enzyme activity.|||Probable tRNA(His) guanylyltransferase|||Reduces activity by 95%.|||Reduces activity by 98.5%.|||Reduces activity by 99.5%.|||Slightly reduced enzyme activity.|||Thg1 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284984|||http://purl.uniprot.org/annotation/VAR_031871|||http://purl.uniprot.org/annotation/VAR_083901|||http://purl.uniprot.org/annotation/VAR_083902
http://togogenome.org/gene/9606:BORCS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B45                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  BLOC-1-related complex subunit 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089787
http://togogenome.org/gene/9606:LLGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJJ0|||http://purl.uniprot.org/uniprot/Q6P1M3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decrease of phosphorylation.|||Disordered|||In isoform A.|||In isoform B.|||LLGL scribble cell polarity complex component 2|||Loss of phosphorylation.|||No effect on phosphorylation.|||Phosphoserine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232728|||http://purl.uniprot.org/annotation/VAR_034058|||http://purl.uniprot.org/annotation/VAR_034059|||http://purl.uniprot.org/annotation/VAR_050069|||http://purl.uniprot.org/annotation/VAR_050070|||http://purl.uniprot.org/annotation/VAR_050071|||http://purl.uniprot.org/annotation/VAR_050072|||http://purl.uniprot.org/annotation/VAR_050073|||http://purl.uniprot.org/annotation/VAR_050075|||http://purl.uniprot.org/annotation/VSP_017946|||http://purl.uniprot.org/annotation/VSP_047387|||http://purl.uniprot.org/annotation/VSP_047388
http://togogenome.org/gene/9606:FSD1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG97|||http://purl.uniprot.org/uniprot/B7Z3W5|||http://purl.uniprot.org/uniprot/F8W946|||http://purl.uniprot.org/uniprot/Q8N450|||http://purl.uniprot.org/uniprot/Q9BXM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  B30.2/SPRY|||Basic and acidic residues|||COS|||Disordered|||FSD1-like protein|||Fibronectin type-III|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089405|||http://purl.uniprot.org/annotation/VSP_039645|||http://purl.uniprot.org/annotation/VSP_039646|||http://purl.uniprot.org/annotation/VSP_039647
http://togogenome.org/gene/9606:PHTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PHTF|||Phosphoserine|||Polar residues|||Protein PHTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127423|||http://purl.uniprot.org/annotation/VSP_002144|||http://purl.uniprot.org/annotation/VSP_002145
http://togogenome.org/gene/9606:TMEM117                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VS00|||http://purl.uniprot.org/uniprot/Q05C15|||http://purl.uniprot.org/uniprot/Q9H0C3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-353.|||Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-371.|||Transmembrane protein 117                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251204|||http://purl.uniprot.org/annotation/VAR_027660
http://togogenome.org/gene/9606:CELSR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYQ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cadherin EGF LAG seven-pass G-type receptor 3|||Cytoplasmic|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||Extracellular|||Found in a patient with epileptic encephalopathy; unknown pathological significance.|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Laminin EGF-like|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012918|||http://purl.uniprot.org/annotation/VAR_020022|||http://purl.uniprot.org/annotation/VAR_020023|||http://purl.uniprot.org/annotation/VAR_055101|||http://purl.uniprot.org/annotation/VAR_083108|||http://purl.uniprot.org/annotation/VAR_083109|||http://purl.uniprot.org/annotation/VSP_037125
http://togogenome.org/gene/9606:ALPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Alpha-protein kinase 2|||Alpha-type protein kinase|||Basic and acidic residues|||Disordered|||Ig-like 1|||Ig-like 2|||In a melanoma metastatic sample; somatic mutation.|||In an ovarian undifferentiated carcinoma sample; somatic mutation.|||Polar residues|||Rare variant found in East Asian patients; decreases luminal apoptosis, cell aggregation and basolateral membrane localization in colorectal cancer cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260030|||http://purl.uniprot.org/annotation/VAR_045591|||http://purl.uniprot.org/annotation/VAR_045593|||http://purl.uniprot.org/annotation/VAR_045594|||http://purl.uniprot.org/annotation/VAR_045595|||http://purl.uniprot.org/annotation/VAR_054914|||http://purl.uniprot.org/annotation/VAR_054915|||http://purl.uniprot.org/annotation/VAR_054916|||http://purl.uniprot.org/annotation/VAR_054917|||http://purl.uniprot.org/annotation/VAR_054918|||http://purl.uniprot.org/annotation/VAR_054919|||http://purl.uniprot.org/annotation/VAR_054920|||http://purl.uniprot.org/annotation/VAR_054921|||http://purl.uniprot.org/annotation/VAR_054922|||http://purl.uniprot.org/annotation/VAR_054923|||http://purl.uniprot.org/annotation/VAR_054924|||http://purl.uniprot.org/annotation/VAR_054925|||http://purl.uniprot.org/annotation/VAR_054926|||http://purl.uniprot.org/annotation/VAR_054927|||http://purl.uniprot.org/annotation/VAR_054928|||http://purl.uniprot.org/annotation/VAR_054929|||http://purl.uniprot.org/annotation/VAR_054930|||http://purl.uniprot.org/annotation/VAR_054931|||http://purl.uniprot.org/annotation/VAR_054932|||http://purl.uniprot.org/annotation/VAR_054933|||http://purl.uniprot.org/annotation/VAR_057742|||http://purl.uniprot.org/annotation/VAR_062168|||http://purl.uniprot.org/annotation/VAR_082163|||http://purl.uniprot.org/annotation/VAR_082164|||http://purl.uniprot.org/annotation/VAR_082165|||http://purl.uniprot.org/annotation/VAR_082166|||http://purl.uniprot.org/annotation/VAR_082167|||http://purl.uniprot.org/annotation/VAR_082168|||http://purl.uniprot.org/annotation/VAR_082169|||http://purl.uniprot.org/annotation/VAR_082170|||http://purl.uniprot.org/annotation/VAR_082171|||http://purl.uniprot.org/annotation/VAR_082172|||http://purl.uniprot.org/annotation/VAR_082173|||http://purl.uniprot.org/annotation/VAR_082174
http://togogenome.org/gene/9606:MKLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG30|||http://purl.uniprot.org/uniprot/Q9UL63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CTLH|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||LisH|||Muskelin|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119138|||http://purl.uniprot.org/annotation/VAR_050057|||http://purl.uniprot.org/annotation/VSP_021852
http://togogenome.org/gene/9606:ZNF710                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1W2                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 710                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233708
http://togogenome.org/gene/9606:RRAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55042                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||GTP-binding protein RAD|||Omega-N-methylarginine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122478|||http://purl.uniprot.org/annotation/VAR_049497
http://togogenome.org/gene/9606:GYG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUV6|||http://purl.uniprot.org/uniprot/O15488|||http://purl.uniprot.org/uniprot/Q1ZYL7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a renal cell carcinoma case; somatic mutation.|||Glycogenin-2|||Important for catalytic activity|||In isoform Beta.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma.|||In isoform Zeta.|||Loss of autoglucosylation.|||No loss of activity.|||O-linked (Glc...) tyrosine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215180|||http://purl.uniprot.org/annotation/VAR_010401|||http://purl.uniprot.org/annotation/VAR_024457|||http://purl.uniprot.org/annotation/VAR_031224|||http://purl.uniprot.org/annotation/VAR_053110|||http://purl.uniprot.org/annotation/VAR_064717|||http://purl.uniprot.org/annotation/VSP_001770|||http://purl.uniprot.org/annotation/VSP_001771|||http://purl.uniprot.org/annotation/VSP_001772|||http://purl.uniprot.org/annotation/VSP_001773|||http://purl.uniprot.org/annotation/VSP_001774
http://togogenome.org/gene/9606:FASTKD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CZ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  FAST kinase domain-containing protein 3, mitochondrial|||In a breast cancer sample; somatic mutation.|||Mitochondrion|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284715|||http://purl.uniprot.org/annotation/VAR_031809|||http://purl.uniprot.org/annotation/VAR_031810|||http://purl.uniprot.org/annotation/VAR_036161|||http://purl.uniprot.org/annotation/VAR_057769
http://togogenome.org/gene/9606:AOPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6M6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Motif|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Aminopeptidase O|||In DYT31.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Nucleolar localization signal|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095091|||http://purl.uniprot.org/annotation/VAR_021511|||http://purl.uniprot.org/annotation/VAR_057053|||http://purl.uniprot.org/annotation/VAR_057054|||http://purl.uniprot.org/annotation/VAR_057055|||http://purl.uniprot.org/annotation/VAR_086438|||http://purl.uniprot.org/annotation/VAR_086439|||http://purl.uniprot.org/annotation/VAR_086440|||http://purl.uniprot.org/annotation/VSP_013161|||http://purl.uniprot.org/annotation/VSP_013162|||http://purl.uniprot.org/annotation/VSP_013163|||http://purl.uniprot.org/annotation/VSP_013164|||http://purl.uniprot.org/annotation/VSP_013165
http://togogenome.org/gene/9606:SIRPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78324                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C1-type 1|||Ig-like C1-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Phosphotyrosine; by Tyr-kinases|||Polar residues|||Requires 2 nucleotide substitutions.|||SH2-binding|||SH3-binding|||Tyrosine-protein phosphatase non-receptor type substrate 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014941|||http://purl.uniprot.org/annotation/VAR_015462|||http://purl.uniprot.org/annotation/VAR_015463|||http://purl.uniprot.org/annotation/VAR_015464|||http://purl.uniprot.org/annotation/VAR_015465|||http://purl.uniprot.org/annotation/VAR_015466|||http://purl.uniprot.org/annotation/VAR_015468|||http://purl.uniprot.org/annotation/VAR_015470|||http://purl.uniprot.org/annotation/VAR_015471|||http://purl.uniprot.org/annotation/VAR_015472|||http://purl.uniprot.org/annotation/VAR_015473|||http://purl.uniprot.org/annotation/VAR_015474|||http://purl.uniprot.org/annotation/VAR_015475|||http://purl.uniprot.org/annotation/VAR_015477|||http://purl.uniprot.org/annotation/VAR_015478|||http://purl.uniprot.org/annotation/VAR_015479|||http://purl.uniprot.org/annotation/VAR_015480|||http://purl.uniprot.org/annotation/VAR_015483|||http://purl.uniprot.org/annotation/VAR_015484|||http://purl.uniprot.org/annotation/VAR_015485|||http://purl.uniprot.org/annotation/VAR_015486|||http://purl.uniprot.org/annotation/VAR_015487|||http://purl.uniprot.org/annotation/VAR_015488|||http://purl.uniprot.org/annotation/VAR_015489|||http://purl.uniprot.org/annotation/VAR_015490|||http://purl.uniprot.org/annotation/VAR_015491|||http://purl.uniprot.org/annotation/VAR_015492|||http://purl.uniprot.org/annotation/VAR_015493|||http://purl.uniprot.org/annotation/VAR_015494|||http://purl.uniprot.org/annotation/VAR_015495|||http://purl.uniprot.org/annotation/VAR_015496|||http://purl.uniprot.org/annotation/VAR_015497|||http://purl.uniprot.org/annotation/VAR_015498|||http://purl.uniprot.org/annotation/VAR_015499|||http://purl.uniprot.org/annotation/VAR_015500|||http://purl.uniprot.org/annotation/VAR_015501|||http://purl.uniprot.org/annotation/VAR_015502|||http://purl.uniprot.org/annotation/VAR_015503|||http://purl.uniprot.org/annotation/VAR_015504|||http://purl.uniprot.org/annotation/VAR_015505|||http://purl.uniprot.org/annotation/VAR_015506|||http://purl.uniprot.org/annotation/VAR_015507|||http://purl.uniprot.org/annotation/VAR_015508|||http://purl.uniprot.org/annotation/VAR_015509|||http://purl.uniprot.org/annotation/VAR_015510|||http://purl.uniprot.org/annotation/VAR_015511|||http://purl.uniprot.org/annotation/VAR_015512|||http://purl.uniprot.org/annotation/VSP_007030|||http://purl.uniprot.org/annotation/VSP_040799
http://togogenome.org/gene/9606:PHGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L2EC20|||http://purl.uniprot.org/uniprot/C9JFL3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline, histidine and glycine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395029
http://togogenome.org/gene/9606:H2BC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99880                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-L|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071829|||http://purl.uniprot.org/annotation/VAR_049313
http://togogenome.org/gene/9606:DCAF8L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||DDB1- and CUL4-associated factor 8-like protein 1|||Disordered|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314820|||http://purl.uniprot.org/annotation/VAR_038060
http://togogenome.org/gene/9606:VEZT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBM0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 5.|||In isoform 6.|||Polar residues|||Vezatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065783|||http://purl.uniprot.org/annotation/VAR_014945|||http://purl.uniprot.org/annotation/VAR_046303|||http://purl.uniprot.org/annotation/VAR_046304|||http://purl.uniprot.org/annotation/VAR_046305|||http://purl.uniprot.org/annotation/VAR_046306|||http://purl.uniprot.org/annotation/VSP_004010|||http://purl.uniprot.org/annotation/VSP_004011|||http://purl.uniprot.org/annotation/VSP_004014|||http://purl.uniprot.org/annotation/VSP_004017|||http://purl.uniprot.org/annotation/VSP_040853|||http://purl.uniprot.org/annotation/VSP_040854|||http://purl.uniprot.org/annotation/VSP_040855|||http://purl.uniprot.org/annotation/VSP_040856
http://togogenome.org/gene/9606:CTSE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0MPN9|||http://purl.uniprot.org/uniprot/B4DNU8|||http://purl.uniprot.org/uniprot/P14091                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization.|||Activation peptide|||Cathepsin E form I|||Cathepsin E form II|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025974|||http://purl.uniprot.org/annotation/PRO_0000025975|||http://purl.uniprot.org/annotation/PRO_0000354668|||http://purl.uniprot.org/annotation/PRO_5030722284|||http://purl.uniprot.org/annotation/VAR_014572|||http://purl.uniprot.org/annotation/VAR_061731|||http://purl.uniprot.org/annotation/VSP_059425|||http://purl.uniprot.org/annotation/VSP_059426
http://togogenome.org/gene/9606:SLC25A39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFG5|||http://purl.uniprot.org/uniprot/Q9BZJ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolished glutathione import into mitochondria without affecting the levels of NAD.|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Probable mitochondrial glutathione transporter SLC25A39|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090596|||http://purl.uniprot.org/annotation/VAR_012756|||http://purl.uniprot.org/annotation/VSP_003264
http://togogenome.org/gene/9606:EDF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60869                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Endothelial differentiation-related factor 1|||H-T-H motif|||HTH cro/C1-type|||IQ motif|||In isoform 2.|||In isoform 3.|||Interaction with NR5A2, PPARG and NR1H3|||Interaction with TBP and NR5A1|||Loss of interaction with CALM and higher affinity for TBP. Same effect; when associated with D-65 and D-74.|||Loss of interaction with CALM; when associated with D-40; D-58 and D-91.|||Loss of interaction with CALM; when associated with D-40; D-91 and D-111.|||Loss of interaction with CALM; when associated with D-58; D-91 and D-111.|||N-acetylalanine|||N6-methyllysine|||No effect on CALM-binding.|||No effect on CALM-binding. No effect; when associated with D-65.|||No effect on CALM-binding. No effect; when associated with D-74.|||Partial loss of interaction with CALM. Complete loss of interaction; when associated with D-40; D-58 and D-111.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149795|||http://purl.uniprot.org/annotation/VSP_013336|||http://purl.uniprot.org/annotation/VSP_054701
http://togogenome.org/gene/9606:SPINK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7L1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Kazal-like|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serine protease inhibitor Kazal-type 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337296|||http://purl.uniprot.org/annotation/VAR_043978
http://togogenome.org/gene/9606:IQCB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15051                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disrupts interaction with CEP290, no effect on interaction with BBS1, BBS2, BBS4, BBS8 and BBS9, abolishes ciliogenesis.|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ calmodulin-binding motif-containing protein 1|||Impairs interaction with calmodulin.|||In isoform 2.|||In isoform 3.|||Interaction with BBS1, BBS2, BBS4, BBS7, BBS8 and BBS9|||Interaction with BBS1, BBS8 and BBS9|||Interaction with CEP290, BBS1, BBS2, BBS4, BBS5, BBS7, BBS8 and BBS9|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084225|||http://purl.uniprot.org/annotation/VAR_051074|||http://purl.uniprot.org/annotation/VAR_051075|||http://purl.uniprot.org/annotation/VAR_051076|||http://purl.uniprot.org/annotation/VAR_061668|||http://purl.uniprot.org/annotation/VSP_010245|||http://purl.uniprot.org/annotation/VSP_013943|||http://purl.uniprot.org/annotation/VSP_013944
http://togogenome.org/gene/9606:ELP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EB1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Elongator complex protein 4|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284004|||http://purl.uniprot.org/annotation/VAR_053881|||http://purl.uniprot.org/annotation/VSP_024409|||http://purl.uniprot.org/annotation/VSP_054128|||http://purl.uniprot.org/annotation/VSP_054129
http://togogenome.org/gene/9606:INTS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYI0|||http://purl.uniprot.org/uniprot/Q5TA45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the ability of the Integrator complex to process U1 and U2 snRNA genes.|||Beta-Casp|||HXHXDH motif|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Integrator complex subunit 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259563|||http://purl.uniprot.org/annotation/VSP_021472|||http://purl.uniprot.org/annotation/VSP_021473|||http://purl.uniprot.org/annotation/VSP_045428|||http://purl.uniprot.org/annotation/VSP_046643
http://togogenome.org/gene/9606:TAOK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L7X3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes kinase activity, ability to activate the MAPK8/JNK cascade and cleavage by caspase-3 (CASP3).|||Abolishes phosphorylation by ATM; when associated with A-643 and A-785.|||Abolishes phosphorylation by ATM; when associated with A-643 and A-990.|||Abolishes phosphorylation by ATM; when associated with A-785 and A-990.|||Basic and acidic residues|||Disordered|||Does not abolish cleavage by caspase-3 (CASP3).|||In DDIB.|||In DDIB; affects neuron maturation and migration.|||In DDIB; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of serine/threonine-protein kinase activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086728|||http://purl.uniprot.org/annotation/VAR_041204|||http://purl.uniprot.org/annotation/VAR_086415|||http://purl.uniprot.org/annotation/VAR_086416|||http://purl.uniprot.org/annotation/VAR_086417|||http://purl.uniprot.org/annotation/VAR_086418|||http://purl.uniprot.org/annotation/VAR_086419|||http://purl.uniprot.org/annotation/VAR_086420|||http://purl.uniprot.org/annotation/VAR_086421|||http://purl.uniprot.org/annotation/VAR_086422|||http://purl.uniprot.org/annotation/VAR_086423|||http://purl.uniprot.org/annotation/VAR_086424|||http://purl.uniprot.org/annotation/VAR_086425|||http://purl.uniprot.org/annotation/VAR_086426|||http://purl.uniprot.org/annotation/VAR_086427|||http://purl.uniprot.org/annotation/VAR_086428|||http://purl.uniprot.org/annotation/VAR_086429|||http://purl.uniprot.org/annotation/VAR_086430|||http://purl.uniprot.org/annotation/VAR_086431|||http://purl.uniprot.org/annotation/VAR_086432|||http://purl.uniprot.org/annotation/VSP_015964|||http://purl.uniprot.org/annotation/VSP_015965|||http://purl.uniprot.org/annotation/VSP_015966|||http://purl.uniprot.org/annotation/VSP_043706
http://togogenome.org/gene/9606:PSG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTI5|||http://purl.uniprot.org/uniprot/E7EW65|||http://purl.uniprot.org/uniprot/G3XAA7|||http://purl.uniprot.org/uniprot/M0R0U8|||http://purl.uniprot.org/uniprot/Q00887|||http://purl.uniprot.org/uniprot/Q05DN5|||http://purl.uniprot.org/uniprot/Q13178                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014916|||http://purl.uniprot.org/annotation/PRO_5002803298|||http://purl.uniprot.org/annotation/PRO_5003219028|||http://purl.uniprot.org/annotation/PRO_5004182051|||http://purl.uniprot.org/annotation/PRO_5014101263|||http://purl.uniprot.org/annotation/PRO_5015091848|||http://purl.uniprot.org/annotation/VAR_049925|||http://purl.uniprot.org/annotation/VAR_049926|||http://purl.uniprot.org/annotation/VAR_049927|||http://purl.uniprot.org/annotation/VAR_058296|||http://purl.uniprot.org/annotation/VAR_059410|||http://purl.uniprot.org/annotation/VSP_055602|||http://purl.uniprot.org/annotation/VSP_055603
http://togogenome.org/gene/9606:NBEAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Disordered|||In GPS.|||In a patient with gray platelet syndrome.|||In isoform 2.|||In isoform 3.|||Neurobeachin-like protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333254|||http://purl.uniprot.org/annotation/VAR_043133|||http://purl.uniprot.org/annotation/VAR_043134|||http://purl.uniprot.org/annotation/VAR_043135|||http://purl.uniprot.org/annotation/VAR_043136|||http://purl.uniprot.org/annotation/VAR_043137|||http://purl.uniprot.org/annotation/VAR_066975|||http://purl.uniprot.org/annotation/VAR_066976|||http://purl.uniprot.org/annotation/VAR_066977|||http://purl.uniprot.org/annotation/VAR_066978|||http://purl.uniprot.org/annotation/VAR_066979|||http://purl.uniprot.org/annotation/VAR_066980|||http://purl.uniprot.org/annotation/VAR_066981|||http://purl.uniprot.org/annotation/VAR_066982|||http://purl.uniprot.org/annotation/VAR_066983|||http://purl.uniprot.org/annotation/VAR_066984|||http://purl.uniprot.org/annotation/VAR_066985|||http://purl.uniprot.org/annotation/VSP_033505|||http://purl.uniprot.org/annotation/VSP_033506|||http://purl.uniprot.org/annotation/VSP_033507
http://togogenome.org/gene/9606:TP53I13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Tumor protein p53-inducible protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333824
http://togogenome.org/gene/9606:HCFC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Z7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Host cell factor 2|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119072|||http://purl.uniprot.org/annotation/VAR_033984|||http://purl.uniprot.org/annotation/VAR_050044|||http://purl.uniprot.org/annotation/VSP_057024|||http://purl.uniprot.org/annotation/VSP_057025
http://togogenome.org/gene/9606:CASP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55212                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  130's region|||Abolished activation due to the presence of the N-terminal disordered prodomain. Abolished processing and subsequent activation; when associated with A-179 and A-193.|||Abolished phosphorylation, leading to caspase-6 activation.|||Abolished processing and subsequent activation; when associated with A-23 and A-179.|||Abolished processing and subsequent activation; when associated with A-23 and A-193.|||Caspase-6 subunit p11|||Caspase-6 subunit p18|||Catalytically inactive active-site mutant.|||Decreased ability to hydrolyze substrates.|||Disordered|||In isoform Beta.|||Increased stability.|||Phospho-mimetic mutant; loss of self-activation.|||Phospho-mimetic mutant; prevents caspase-6 autoactivation.|||Phosphoserine|||Phosphoserine; by NUAK1 and AMPK|||Reduced palmitoylation, leading to increased cysteine protease activity.|||S-palmitoyl cysteine|||Tri-arginine exosite                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004608|||http://purl.uniprot.org/annotation/PRO_0000004609|||http://purl.uniprot.org/annotation/PRO_0000004610|||http://purl.uniprot.org/annotation/PRO_0000004611|||http://purl.uniprot.org/annotation/VAR_016130|||http://purl.uniprot.org/annotation/VAR_020126|||http://purl.uniprot.org/annotation/VAR_029242|||http://purl.uniprot.org/annotation/VSP_000805
http://togogenome.org/gene/9606:CFAP58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T655                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 58|||In SPGF49.|||In SPGF49; results in loss of mutant protein; results in axonemal abnormalities.|||In SPGF49; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274317|||http://purl.uniprot.org/annotation/VAR_030255|||http://purl.uniprot.org/annotation/VAR_030256|||http://purl.uniprot.org/annotation/VAR_085209|||http://purl.uniprot.org/annotation/VAR_085210|||http://purl.uniprot.org/annotation/VAR_085211|||http://purl.uniprot.org/annotation/VAR_085546|||http://purl.uniprot.org/annotation/VAR_085547|||http://purl.uniprot.org/annotation/VAR_085548|||http://purl.uniprot.org/annotation/VAR_085549
http://togogenome.org/gene/9606:ACLY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53396|||http://purl.uniprot.org/uniprot/Q4LE36                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-citrate synthase|||ATP-grasp|||CoA-binding|||Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-546.|||Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25) complex; when associated with R-540 and R-554.|||Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. Abolished ubiquitination by the BCR(KLHL25)complex; when associated with R-546 and R-554.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduced enzyme activity.|||Tele-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102781|||http://purl.uniprot.org/annotation/VAR_028230|||http://purl.uniprot.org/annotation/VSP_042201|||http://purl.uniprot.org/annotation/VSP_057230
http://togogenome.org/gene/9606:RNF169                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitin-binding.|||About 90% loss of phosphorylation by DYRK1A; when associated with A-368.|||About 90% loss of phosphorylation by DYRK1A; when associated with A-403.|||Basic and acidic residues|||Disordered|||Does not affect recruitment to DSBs nor ability to inhibit DSBs repair.|||Does not affect ubiquitin-binding but abolishes recruitment to DSBs.|||E3 ubiquitin-protein ligase RNF169|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs recruitment to DSBs.|||LR motif|||MIU motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||UMI motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245598
http://togogenome.org/gene/9606:HMOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT44|||http://purl.uniprot.org/uniprot/B3KSE0|||http://purl.uniprot.org/uniprot/P30519                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||HRM 1|||HRM 2|||Helical|||Helical; Anchor for type IV membrane protein|||Heme oxygenase 2|||Heme oxygenase 2 soluble form|||Important for catalytic activity|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209691|||http://purl.uniprot.org/annotation/PRO_0000455626|||http://purl.uniprot.org/annotation/VAR_021067|||http://purl.uniprot.org/annotation/VAR_021068|||http://purl.uniprot.org/annotation/VSP_055031
http://togogenome.org/gene/9606:TYW5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUC4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity and ability to bind tRNA.|||In isoform 2.|||JmjC|||tRNA wybutosine-synthesizing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309274|||http://purl.uniprot.org/annotation/VAR_036926|||http://purl.uniprot.org/annotation/VSP_029106
http://togogenome.org/gene/9606:VKORC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5X7|||http://purl.uniprot.org/uniprot/A0A0S2Z6I4|||http://purl.uniprot.org/uniprot/Q9BQB6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased vitamin K epoxide reductase activity.|||Decreases enzyme activity by about 80%. Decreases inhibition by warfarin.|||Decreases enzyme activity moderately. Decreases inhibition by warfarin.|||Decreases enzyme activity moderately. Strongly decreases inhibition by warfarin.|||Helical|||In CMRES.|||In VKCFD2; strongly reduced enzyme activity.|||In isoform 2.|||In isoform 3.|||Lumenal|||Nearly abolishes enzyme activity.|||No effect on enzyme activity. Decreases inhibition by warfarin.|||No effect on enzyme activity. Strongly decreases inhibition by warfarin.|||Redox-active|||Reduces enzyme activity by about 25%.|||Reduces enzyme activity by about 70%.|||Reduces enzyme activity by about 75%.|||Reduces enzyme activity by about 80%.|||Reduces enzyme activity by about 80%. Decreases inhibition by warfarin.|||Reduces enzyme activity.|||Vitamin K epoxide reductase|||Vitamin K epoxide reductase complex subunit 1|||vitamin-K-epoxide reductase (warfarin-sensitive)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191668|||http://purl.uniprot.org/annotation/PRO_5006608335|||http://purl.uniprot.org/annotation/VAR_021821|||http://purl.uniprot.org/annotation/VAR_021822|||http://purl.uniprot.org/annotation/VAR_021823|||http://purl.uniprot.org/annotation/VAR_021824|||http://purl.uniprot.org/annotation/VAR_021825|||http://purl.uniprot.org/annotation/VAR_065785|||http://purl.uniprot.org/annotation/VAR_065786|||http://purl.uniprot.org/annotation/VAR_065787|||http://purl.uniprot.org/annotation/VAR_065788|||http://purl.uniprot.org/annotation/VAR_065789|||http://purl.uniprot.org/annotation/VAR_065790|||http://purl.uniprot.org/annotation/VAR_065791|||http://purl.uniprot.org/annotation/VAR_065792|||http://purl.uniprot.org/annotation/VAR_065793|||http://purl.uniprot.org/annotation/VAR_065794|||http://purl.uniprot.org/annotation/VAR_065795|||http://purl.uniprot.org/annotation/VAR_065796|||http://purl.uniprot.org/annotation/VAR_065797|||http://purl.uniprot.org/annotation/VAR_065798|||http://purl.uniprot.org/annotation/VSP_013363|||http://purl.uniprot.org/annotation/VSP_043407
http://togogenome.org/gene/9606:CIMIP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTA8|||http://purl.uniprot.org/uniprot/B7ZW26|||http://purl.uniprot.org/uniprot/B7ZW33                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Ciliary microtubule inner protein 2B|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342383|||http://purl.uniprot.org/annotation/VSP_034438|||http://purl.uniprot.org/annotation/VSP_034439
http://togogenome.org/gene/9606:RABL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZBD5|||http://purl.uniprot.org/uniprot/Q2TAB6|||http://purl.uniprot.org/uniprot/Q6IC14|||http://purl.uniprot.org/uniprot/Q9UBK7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Rab-like protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121263|||http://purl.uniprot.org/annotation/VSP_005531|||http://purl.uniprot.org/annotation/VSP_041060
http://togogenome.org/gene/9606:ZFP69B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJL9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 69 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047697|||http://purl.uniprot.org/annotation/VAR_033584|||http://purl.uniprot.org/annotation/VAR_052884|||http://purl.uniprot.org/annotation/VSP_041647
http://togogenome.org/gene/9606:NUDT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E059|||http://purl.uniprot.org/uniprot/Q86X67                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||NAD(P)H pyrophosphatase NUDT13, mitochondrial|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057111|||http://purl.uniprot.org/annotation/VAR_034160|||http://purl.uniprot.org/annotation/VAR_050413|||http://purl.uniprot.org/annotation/VSP_011417|||http://purl.uniprot.org/annotation/VSP_054559|||http://purl.uniprot.org/annotation/VSP_055695|||http://purl.uniprot.org/annotation/VSP_055696
http://togogenome.org/gene/9606:CTSW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56202                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cathepsin W|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026327|||http://purl.uniprot.org/annotation/PRO_0000026328|||http://purl.uniprot.org/annotation/VAR_057041|||http://purl.uniprot.org/annotation/VAR_058847
http://togogenome.org/gene/9606:KCNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0R4J2E0|||http://purl.uniprot.org/uniprot/A0A6Q8PGM3|||http://purl.uniprot.org/uniprot/Q5JUK3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated potassium channel BK alpha subunit|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In DEE14.|||In DEE14; gain-of-function mutation.|||In DEE14; unknown pathological significance.|||In DEE14; variant homologue in rat has increased channel activity upon positive potentials.|||In ENFL5.|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Pore-forming|||Potassium channel|||Potassium channel subfamily T member 1|||RCK N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054090|||http://purl.uniprot.org/annotation/VAR_069311|||http://purl.uniprot.org/annotation/VAR_069312|||http://purl.uniprot.org/annotation/VAR_069313|||http://purl.uniprot.org/annotation/VAR_069314|||http://purl.uniprot.org/annotation/VAR_069315|||http://purl.uniprot.org/annotation/VAR_069316|||http://purl.uniprot.org/annotation/VAR_069317|||http://purl.uniprot.org/annotation/VAR_069318|||http://purl.uniprot.org/annotation/VAR_078214|||http://purl.uniprot.org/annotation/VAR_078215|||http://purl.uniprot.org/annotation/VAR_078641|||http://purl.uniprot.org/annotation/VAR_078642|||http://purl.uniprot.org/annotation/VAR_078683|||http://purl.uniprot.org/annotation/VAR_078684|||http://purl.uniprot.org/annotation/VAR_078685|||http://purl.uniprot.org/annotation/VSP_015470|||http://purl.uniprot.org/annotation/VSP_015471|||http://purl.uniprot.org/annotation/VSP_044476|||http://purl.uniprot.org/annotation/VSP_055700|||http://purl.uniprot.org/annotation/VSP_055701
http://togogenome.org/gene/9606:NT5C1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXI3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cytosolic 5'-nucleotidase 1A|||Disordered|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144795
http://togogenome.org/gene/9606:MT1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP7|||http://purl.uniprot.org/uniprot/P80294                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1H|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197239
http://togogenome.org/gene/9606:TMEM170B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4T1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 170B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342267
http://togogenome.org/gene/9606:ARPC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92747|||http://purl.uniprot.org/uniprot/V9HVZ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 1A|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050852|||http://purl.uniprot.org/annotation/VSP_056389|||http://purl.uniprot.org/annotation/VSP_056390
http://togogenome.org/gene/9606:FAM111A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PZ2                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolished autocatalytic cleavage.|||Abolished protease activity.|||Charge relay system|||Cleavage; by autolysis|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In GCLEB.|||In GCLEB; enhanced autocatalytic cleavage.|||In KCS2; enhanced autocatalytic cleavage.|||In PIPmt; affects subcellular localization. Impaired PCNA stability and chromatin binding. Does not affect protease activity.|||Interaction with SV40 large T antigen|||PIP-box|||Phosphoserine|||Serine protease FAM111A|||Strongly decreased single-stranded DNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274407|||http://purl.uniprot.org/annotation/VAR_069513|||http://purl.uniprot.org/annotation/VAR_069514|||http://purl.uniprot.org/annotation/VAR_069515|||http://purl.uniprot.org/annotation/VAR_069516|||http://purl.uniprot.org/annotation/VAR_069517|||http://purl.uniprot.org/annotation/VAR_069518
http://togogenome.org/gene/9606:MDH1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JER5|||http://purl.uniprot.org/uniprot/Q5I0G3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a renal cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Lactate/malate dehydrogenase C-terminal|||Putative malate dehydrogenase 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331435|||http://purl.uniprot.org/annotation/VAR_042861|||http://purl.uniprot.org/annotation/VAR_042862|||http://purl.uniprot.org/annotation/VAR_064729|||http://purl.uniprot.org/annotation/VSP_033199|||http://purl.uniprot.org/annotation/VSP_033200|||http://purl.uniprot.org/annotation/VSP_033201
http://togogenome.org/gene/9606:TAGAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N103                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Rho-GAP|||T-cell activation Rho GTPase-activating protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056719|||http://purl.uniprot.org/annotation/VAR_049146|||http://purl.uniprot.org/annotation/VSP_015868|||http://purl.uniprot.org/annotation/VSP_015869|||http://purl.uniprot.org/annotation/VSP_015870|||http://purl.uniprot.org/annotation/VSP_015871|||http://purl.uniprot.org/annotation/VSP_015872
http://togogenome.org/gene/9606:SLC25A32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2D1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In NTD; uncertain pathological significance.|||In NTD; uncertain pathological significance; loss of function; no effect on mitochondrial localization.|||In RREI; decreases succinate dehydrogenase activity and glycerol-3-phosphate dehydrogenase activity.|||In RREI; results in impaired FAD transporter activity and lower FAD, FMN and riboflavin mitochondrial levels, when expressed in murine skeletal muscle cells; motor function impairment shown by a mouse knockin model of the mutation.|||In RREI; results in reduced transcript and protein levels while retaining normal FAD transporter activity, when expressed in murine skeletal muscle cells.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090641|||http://purl.uniprot.org/annotation/VAR_050130|||http://purl.uniprot.org/annotation/VAR_076364|||http://purl.uniprot.org/annotation/VAR_082961|||http://purl.uniprot.org/annotation/VAR_082962|||http://purl.uniprot.org/annotation/VAR_082963|||http://purl.uniprot.org/annotation/VAR_082964|||http://purl.uniprot.org/annotation/VAR_082965|||http://purl.uniprot.org/annotation/VAR_088373|||http://purl.uniprot.org/annotation/VAR_088374
http://togogenome.org/gene/9606:ERBB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15303                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes APC/C-mediated degradation; when associated with A-992 and A-1000.|||Abolishes APC/C-mediated degradation; when associated with A-992 and A-995.|||Abolishes APC/C-mediated degradation; when associated with A-995 and A-1000.|||Abolishes interaction with NEDD4 and impairs ubiquitination.|||Abolishes interaction with NEDD4 and impairs ubiquitination. Promotes nuclear translocation of ERBB4 intracellular domain E4ICD1.|||Abolishes interaction with WWP1; when associated with F-1056.|||Abolishes interaction with WWP1; when associated with F-1301.|||Abolishes kinase activity. Abolishes phosphorylation, proteolytic processing and nuclear localization.|||Abolishes nuclear localization of the ERBB4 intracellular domain.|||Abolishes proteolytic processing and nuclear localization.|||Constitutively activated kinase.|||Constitutively autophosphorylated.|||Cytoplasmic|||Disordered|||ERBB4 intracellular domain|||Extracellular|||Helical|||In ALS19; reduces autophosphorylation upon NRG1 stimulation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform JM-ACYT-2 and isoform JM-BCYT-2.|||In isoform JM-BCYT-1 and isoform JM-BCYT-2.|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1035. Loss of interaction with YAP1 and stimulation of transcription.|||No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1301.|||No effect on kinase activity.|||Nuclear localization signal|||PDZ-binding|||PPxY motif 1|||PPxY motif 2|||PPxY motif 3|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Receptor tyrosine-protein kinase erbB-4|||Strongly reduced autophosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016674|||http://purl.uniprot.org/annotation/PRO_0000396797|||http://purl.uniprot.org/annotation/VAR_042113|||http://purl.uniprot.org/annotation/VAR_042114|||http://purl.uniprot.org/annotation/VAR_070810|||http://purl.uniprot.org/annotation/VAR_070811|||http://purl.uniprot.org/annotation/VSP_002895|||http://purl.uniprot.org/annotation/VSP_022148
http://togogenome.org/gene/9606:C5orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q569G3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C5orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321821
http://togogenome.org/gene/9606:LUM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N669|||http://purl.uniprot.org/uniprot/P51884                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Found in patients with amyotrophic lateral sclerosis.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||Lumican|||N-linked (GlcNAc...) (keratan sulfate) asparagine|||Phosphoserine|||Pyrrolidone carboxylic acid|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032733|||http://purl.uniprot.org/annotation/PRO_5017240581|||http://purl.uniprot.org/annotation/VAR_065763
http://togogenome.org/gene/9606:NBPF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3W6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Neuroblastoma breakpoint family member 10|||Olduvai 1|||Olduvai 10|||Olduvai 11|||Olduvai 12|||Olduvai 13|||Olduvai 14|||Olduvai 15|||Olduvai 16|||Olduvai 17|||Olduvai 18|||Olduvai 19|||Olduvai 2|||Olduvai 20|||Olduvai 21|||Olduvai 22|||Olduvai 23|||Olduvai 24|||Olduvai 25|||Olduvai 26|||Olduvai 27|||Olduvai 28|||Olduvai 29|||Olduvai 3|||Olduvai 30|||Olduvai 31|||Olduvai 32|||Olduvai 33|||Olduvai 34|||Olduvai 35|||Olduvai 36|||Olduvai 37|||Olduvai 38|||Olduvai 39|||Olduvai 4|||Olduvai 40|||Olduvai 41|||Olduvai 42|||Olduvai 5|||Olduvai 6|||Olduvai 7|||Olduvai 8|||Olduvai 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288045
http://togogenome.org/gene/9606:NYAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Involved in CYFIP1- and NCKAP1-binding|||Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320929|||http://purl.uniprot.org/annotation/VSP_031746
http://togogenome.org/gene/9606:GGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ9|||http://purl.uniprot.org/uniprot/P19440                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes gamma-glutamyltranspeptidase activity.|||Abolishes gamma-glutamyltranspeptidase activity. Increases KM for D-gamma-glutamyl-p-nitroanalide by over 1000-fold.|||Cytoplasmic|||Extracellular|||Glutathione hydrolase 1 heavy chain|||Glutathione hydrolase 1 light chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Loss of autocatalytic cleavage, cell membrane localization and decrease in gamma-glutamyltranspeptidase activity; when associated with W-192.|||Loss of autocatalytic cleavage, cell membrane localization and decrease in gamma-glutamyltranspeptidase activity; when associated with Y-193.|||N-linked (GlcNAc...) asparagine|||No effect on gamma-glutamyltranspeptidase activity.|||Nucleophile|||Reduces enzyme activity by 97%.|||Reduces enzyme gamma-glutamyltranspeptidase activity by 90%.|||Reduces enzyme gamma-glutamyltranspeptidase activity by 99%.|||Reduces gamma-glutamyltranspeptidase activity by 66%.|||Reduces gamma-glutamyltranspeptidase activity by 90%.|||Reduces gamma-glutamyltranspeptidase activity by 98%.|||Reduces gamma-glutamyltranspeptidase activity by 99%. Abolishes activity; when associated with A-451.|||Reduces gamma-glutamyltranspeptidase activity by 99%. Abolishes activity; when associated with A-452.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011058|||http://purl.uniprot.org/annotation/PRO_0000011059|||http://purl.uniprot.org/annotation/VAR_018372|||http://purl.uniprot.org/annotation/VAR_018373|||http://purl.uniprot.org/annotation/VAR_018374|||http://purl.uniprot.org/annotation/VAR_025545|||http://purl.uniprot.org/annotation/VAR_025546|||http://purl.uniprot.org/annotation/VAR_049181|||http://purl.uniprot.org/annotation/VSP_001746|||http://purl.uniprot.org/annotation/VSP_001747|||http://purl.uniprot.org/annotation/VSP_008132
http://togogenome.org/gene/9606:ALPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Alpha-protein kinase 3|||Alpha-type protein kinase|||Basic and acidic residues|||Disordered|||Ig-like 1|||Ig-like 2|||In CMH27.|||In a lung large cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260031|||http://purl.uniprot.org/annotation/VAR_028989|||http://purl.uniprot.org/annotation/VAR_028990|||http://purl.uniprot.org/annotation/VAR_028991|||http://purl.uniprot.org/annotation/VAR_028992|||http://purl.uniprot.org/annotation/VAR_028993|||http://purl.uniprot.org/annotation/VAR_041524|||http://purl.uniprot.org/annotation/VAR_041525|||http://purl.uniprot.org/annotation/VAR_041526|||http://purl.uniprot.org/annotation/VAR_041527|||http://purl.uniprot.org/annotation/VAR_041528|||http://purl.uniprot.org/annotation/VAR_041529|||http://purl.uniprot.org/annotation/VAR_041530|||http://purl.uniprot.org/annotation/VAR_041531|||http://purl.uniprot.org/annotation/VAR_041532|||http://purl.uniprot.org/annotation/VAR_041533|||http://purl.uniprot.org/annotation/VAR_057743|||http://purl.uniprot.org/annotation/VAR_057744|||http://purl.uniprot.org/annotation/VAR_057745|||http://purl.uniprot.org/annotation/VAR_079142|||http://purl.uniprot.org/annotation/VAR_079143|||http://purl.uniprot.org/annotation/VAR_079144
http://togogenome.org/gene/9606:RAP1GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47736|||http://purl.uniprot.org/uniprot/X6R8W7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes GTPase activation.|||Disordered|||GoLoco|||Impaired dimerization; when associated with E-100.|||Impaired dimerization; when associated with E-173.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Rap-GAP|||Rap1 GTPase-activating protein 1|||Reduces GTPase activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056743|||http://purl.uniprot.org/annotation/VAR_035547|||http://purl.uniprot.org/annotation/VAR_035548|||http://purl.uniprot.org/annotation/VAR_047792|||http://purl.uniprot.org/annotation/VSP_035256|||http://purl.uniprot.org/annotation/VSP_035257|||http://purl.uniprot.org/annotation/VSP_040260|||http://purl.uniprot.org/annotation/VSP_040261|||http://purl.uniprot.org/annotation/VSP_047025
http://togogenome.org/gene/9606:ASTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6HA08                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Astacin-like metalloendopeptidase|||Disordered|||Peptidase M12A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041964|||http://purl.uniprot.org/annotation/VAR_033491|||http://purl.uniprot.org/annotation/VAR_057063|||http://purl.uniprot.org/annotation/VAR_061734
http://togogenome.org/gene/9606:SLC2A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050381|||http://purl.uniprot.org/annotation/VAR_059852|||http://purl.uniprot.org/annotation/VSP_014449|||http://purl.uniprot.org/annotation/VSP_014450|||http://purl.uniprot.org/annotation/VSP_055253|||http://purl.uniprot.org/annotation/VSP_055254
http://togogenome.org/gene/9606:KCNMB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPA1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated potassium channel subunit beta-3|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187054|||http://purl.uniprot.org/annotation/VAR_018173|||http://purl.uniprot.org/annotation/VAR_018174|||http://purl.uniprot.org/annotation/VAR_018175|||http://purl.uniprot.org/annotation/VAR_018176|||http://purl.uniprot.org/annotation/VAR_018177|||http://purl.uniprot.org/annotation/VSP_009827|||http://purl.uniprot.org/annotation/VSP_009828|||http://purl.uniprot.org/annotation/VSP_009829|||http://purl.uniprot.org/annotation/VSP_009830|||http://purl.uniprot.org/annotation/VSP_046090|||http://purl.uniprot.org/annotation/VSP_046091
http://togogenome.org/gene/9606:CORO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRY9|||http://purl.uniprot.org/uniprot/B3KSZ9|||http://purl.uniprot.org/uniprot/Q6QEF8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coronin-6|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259596|||http://purl.uniprot.org/annotation/VSP_021484|||http://purl.uniprot.org/annotation/VSP_021485|||http://purl.uniprot.org/annotation/VSP_021486|||http://purl.uniprot.org/annotation/VSP_039874
http://togogenome.org/gene/9606:ATXN7L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJY2|||http://purl.uniprot.org/uniprot/Q5T6C5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Ataxin-7-like protein 2|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||SCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278300|||http://purl.uniprot.org/annotation/VAR_053780
http://togogenome.org/gene/9606:ENO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09104|||http://purl.uniprot.org/uniprot/Q6FHV6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Enolase C-terminal TIM barrel|||Enolase N-terminal|||Gamma-enolase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134112|||http://purl.uniprot.org/annotation/VAR_002354|||http://purl.uniprot.org/annotation/VAR_002355|||http://purl.uniprot.org/annotation/VSP_055482
http://togogenome.org/gene/9606:NCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95944                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Natural cytotoxicity triggering receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015031|||http://purl.uniprot.org/annotation/VAR_018634|||http://purl.uniprot.org/annotation/VAR_018635|||http://purl.uniprot.org/annotation/VAR_018636|||http://purl.uniprot.org/annotation/VAR_018637|||http://purl.uniprot.org/annotation/VSP_010409|||http://purl.uniprot.org/annotation/VSP_010410
http://togogenome.org/gene/9606:IFNA14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01570                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-14|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016367
http://togogenome.org/gene/9606:DLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5C6|||http://purl.uniprot.org/uniprot/O00548                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DSL|||Delta-like protein|||Delta-like protein 1|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In NEDBAS.|||In NEDBAS; unknown pathological significance.|||In isoform 2.|||Interaction with MAGI1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007506|||http://purl.uniprot.org/annotation/PRO_5017420133|||http://purl.uniprot.org/annotation/VAR_048976|||http://purl.uniprot.org/annotation/VAR_083465|||http://purl.uniprot.org/annotation/VAR_083466|||http://purl.uniprot.org/annotation/VAR_083467|||http://purl.uniprot.org/annotation/VAR_083468|||http://purl.uniprot.org/annotation/VAR_083469|||http://purl.uniprot.org/annotation/VAR_083470|||http://purl.uniprot.org/annotation/VSP_057186|||http://purl.uniprot.org/annotation/VSP_057187
http://togogenome.org/gene/9606:YTHDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6S0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  3'-5' RNA helicase YTHDC2|||ANK 1|||ANK 2|||Abolished 3'-5' RNA helicase activity.|||Abolished ability to bind N6-methyladenosine (m6A)-containing RNAs.|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Polar residues|||R3H|||YTH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249340|||http://purl.uniprot.org/annotation/VAR_058002|||http://purl.uniprot.org/annotation/VAR_058003
http://togogenome.org/gene/9606:ESPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AK53                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Disordered|||Espin|||In DFNB36.|||In DFNB36; irregular microvillar organization.|||In DFNB36; severe phenotype; severe impairment of microvillar elongation; espin is less efficiently targeted to the microvilli and accumulates in the nucleus.|||In DFNB36; sporadic case with mild phenotype; unknown pathological significance.|||In USH1M; results in impaired elongation of microvilli and stereocilia consistent with a loss of function in parallel actin filament bundle assembly; retains localization to microvilli and stereocilia.|||In isoform 2.|||Loss of targeting to microvilli. Impaired microvillar elongation.|||No effect on localization to microvilli. No effect on microvillar elongation.|||Phosphoserine|||Polar residues|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334666|||http://purl.uniprot.org/annotation/VAR_043451|||http://purl.uniprot.org/annotation/VAR_043452|||http://purl.uniprot.org/annotation/VAR_043453|||http://purl.uniprot.org/annotation/VAR_043454|||http://purl.uniprot.org/annotation/VAR_043455|||http://purl.uniprot.org/annotation/VAR_043456|||http://purl.uniprot.org/annotation/VAR_079505|||http://purl.uniprot.org/annotation/VAR_083335|||http://purl.uniprot.org/annotation/VSP_033728|||http://purl.uniprot.org/annotation/VSP_033729
http://togogenome.org/gene/9606:IPMK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased activity with inositol 1,4,5-trisphosphate. Increased phosphorylation of inositol 1,3,4,5-tetrakisphosphate.|||Decreased activity with inositol 1,4,5-trisphosphate. No effect on phosphorylation of inositol 1,3,4,5-tetrakisphosphate.|||Decreased enzyme activity.|||Disordered|||Inositol polyphosphate multikinase|||Interferes with nuclear localization.|||Loss of enzyme activity.|||Loss of kinase activity and ability to execute necroptosis; when associated with A-146.|||Loss of kinase activity and ability to execute necroptosis; when associated with N-144.|||Moderately decreased enzyme activity.|||N-acetylalanine|||No effect on affinity for phosphatidylinositol 4,5-bisphosphate and mildly increased enzyme activity; when associated with 2-A--P-69 DEL and 279-S--V-365 DEL.|||No effect on affinity for phosphatidylinositol 4,5-bisphosphate and mildly increased enzyme activity; when associated with 2-A--P-69 DEL and 366-G--S-373 DEL.|||No effect on affinity for phosphatidylinositol 4,5-bisphosphate and mildly increased enzyme activity; when associated with 279-S--V-365 DEL and 366-G--S-373.|||Nuclear localization signal|||Phosphoserine|||Removed|||Strongly decreased enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066870|||http://purl.uniprot.org/annotation/VAR_022112
http://togogenome.org/gene/9606:GAGE12J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NER3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339405|||http://purl.uniprot.org/annotation/VAR_037385|||http://purl.uniprot.org/annotation/VAR_037386|||http://purl.uniprot.org/annotation/VAR_037387|||http://purl.uniprot.org/annotation/VAR_043979|||http://purl.uniprot.org/annotation/VAR_087982
http://togogenome.org/gene/9606:KATNBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H079                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site                                                                                  ^@                                                                                  Complete redistribution from the nucleus to the cytoplasm; when associated with A-10; A-11; A-26; A-27; A-28; A-71; A-72; A-73 and A-74.|||Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-27; A-71; A-72; A-73 and A-74.|||Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-28; A-71; A-72; A-73 and A-74.|||Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-27; A-28; A-71; A-72; A-73 and A-74.|||Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-26; A-27; A-28; A-71; A-72; A-73 and A-74.|||Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-11; A-26; A-27; A-28; A-71; A-72; A-73 and A-74.|||KATNB1-like protein 1|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Redistributes from the nucleus to both nucleus and cytoplasm; when associated with A-71; A-72 and A-73. Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-27; A-28; A-71; A-72 and A-73.|||Redistributes from the nucleus to both nucleus and cytoplasm; when associated with A-71; A-72 and A-74. Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-27; A-28; A-71; A-72 and A-74.|||Redistributes from the nucleus to both nucleus and cytoplasm; when associated with A-71; A-73 and A-74. Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-27; A-28; A-71; A-73 and A-74.|||Redistributes from the nucleus to both nucleus and cytoplasm; when associated with A-72; A-73 and A-74. Complete redistribution from the nucleus to the cytoplasm; when associated with A-9; A-10; A-11; A-26; A-27; A-28; A-72; A-73 and A-74.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089981
http://togogenome.org/gene/9606:USP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6JHV3|||http://purl.uniprot.org/uniprot/Q9Y6I4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Does not reduce H2A stability. Interacts more strongly with monoubiquitinated H2A than with nonubiquitinated H2A. Its nuclear localization to chromatin is enhanced.|||Does not reduce monoubiquitinated H2A and H2B stability. Interaction with monoubiquitinated H2A is strongly inhibited.|||In isoform 2.|||N-acetylmethionine|||Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080619|||http://purl.uniprot.org/annotation/VAR_051521|||http://purl.uniprot.org/annotation/VSP_044712
http://togogenome.org/gene/9606:OR2H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X844|||http://purl.uniprot.org/uniprot/O95918                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150480|||http://purl.uniprot.org/annotation/VAR_010227|||http://purl.uniprot.org/annotation/VAR_010228|||http://purl.uniprot.org/annotation/VAR_010229|||http://purl.uniprot.org/annotation/VAR_023231|||http://purl.uniprot.org/annotation/VAR_057540|||http://purl.uniprot.org/annotation/VAR_058087
http://togogenome.org/gene/9606:KRT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13647                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Found in a patient with epidermolysis bullosa simplex with unspecified subtype; unknown pathological significance.|||Head|||IF rod|||In DDD1.|||In DDD1; unknown pathological significance.|||In EBS2A and EBS2C.|||In EBS2A.|||In EBS2A; unknown pathological significance.|||In EBS2A; with laryngeal involvement.|||In EBS2A;.|||In EBS2B and EBS2A; unknown pathological significance.|||In EBS2B.|||In EBS2B; unknown pathological significance.|||In EBS2C and EBS2B; unknown pathological significance.|||In EBS2C and in a patient with epidermolysis bullosa simplex with unspecified subtype; unknown pathological significance; requires 2 nucleotide substitutions.|||In EBS2C, EBS2B and EBS2D.|||In EBS2C.|||In EBS2C; unknown pathological significance.|||In EBS2D.|||In EBS2D; unknown pathological significance.|||In EBS2F.|||Increase in keratin-positive aggregates and keratin intermediate filament networks that are very thin and sparse with short filaments.|||Keratin, type II cytoskeletal 5|||Linker 1|||Linker 12|||No effect on interaction with KRT14 or keratin intermediate filament networks.|||Phosphoserine|||Phosphothreonine; by CDK1|||Polar residues|||Probable disease-associated variant found in a patient with EBS with an unspecified subtype.|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063727|||http://purl.uniprot.org/annotation/VAR_003871|||http://purl.uniprot.org/annotation/VAR_003872|||http://purl.uniprot.org/annotation/VAR_003873|||http://purl.uniprot.org/annotation/VAR_003874|||http://purl.uniprot.org/annotation/VAR_003875|||http://purl.uniprot.org/annotation/VAR_003876|||http://purl.uniprot.org/annotation/VAR_003877|||http://purl.uniprot.org/annotation/VAR_010453|||http://purl.uniprot.org/annotation/VAR_010454|||http://purl.uniprot.org/annotation/VAR_010455|||http://purl.uniprot.org/annotation/VAR_010456|||http://purl.uniprot.org/annotation/VAR_010457|||http://purl.uniprot.org/annotation/VAR_010458|||http://purl.uniprot.org/annotation/VAR_010459|||http://purl.uniprot.org/annotation/VAR_010460|||http://purl.uniprot.org/annotation/VAR_010461|||http://purl.uniprot.org/annotation/VAR_010462|||http://purl.uniprot.org/annotation/VAR_010463|||http://purl.uniprot.org/annotation/VAR_010464|||http://purl.uniprot.org/annotation/VAR_010465|||http://purl.uniprot.org/annotation/VAR_010466|||http://purl.uniprot.org/annotation/VAR_010467|||http://purl.uniprot.org/annotation/VAR_013829|||http://purl.uniprot.org/annotation/VAR_023726|||http://purl.uniprot.org/annotation/VAR_023727|||http://purl.uniprot.org/annotation/VAR_023728|||http://purl.uniprot.org/annotation/VAR_026536|||http://purl.uniprot.org/annotation/VAR_026537|||http://purl.uniprot.org/annotation/VAR_026538|||http://purl.uniprot.org/annotation/VAR_026539|||http://purl.uniprot.org/annotation/VAR_026540|||http://purl.uniprot.org/annotation/VAR_026541|||http://purl.uniprot.org/annotation/VAR_026542|||http://purl.uniprot.org/annotation/VAR_026543|||http://purl.uniprot.org/annotation/VAR_027722|||http://purl.uniprot.org/annotation/VAR_027723|||http://purl.uniprot.org/annotation/VAR_027724|||http://purl.uniprot.org/annotation/VAR_027725|||http://purl.uniprot.org/annotation/VAR_027726|||http://purl.uniprot.org/annotation/VAR_028763|||http://purl.uniprot.org/annotation/VAR_028764|||http://purl.uniprot.org/annotation/VAR_028765|||http://purl.uniprot.org/annotation/VAR_028766|||http://purl.uniprot.org/annotation/VAR_028767|||http://purl.uniprot.org/annotation/VAR_028768|||http://purl.uniprot.org/annotation/VAR_031640|||http://purl.uniprot.org/annotation/VAR_031641|||http://purl.uniprot.org/annotation/VAR_031642|||http://purl.uniprot.org/annotation/VAR_031643|||http://purl.uniprot.org/annotation/VAR_031644|||http://purl.uniprot.org/annotation/VAR_031645|||http://purl.uniprot.org/annotation/VAR_071630|||http://purl.uniprot.org/annotation/VAR_071631|||http://purl.uniprot.org/annotation/VAR_071632|||http://purl.uniprot.org/annotation/VAR_071633|||http://purl.uniprot.org/annotation/VAR_086623|||http://purl.uniprot.org/annotation/VAR_086624|||http://purl.uniprot.org/annotation/VAR_086625|||http://purl.uniprot.org/annotation/VAR_086626|||http://purl.uniprot.org/annotation/VAR_086627|||http://purl.uniprot.org/annotation/VAR_086628|||http://purl.uniprot.org/annotation/VAR_086629|||http://purl.uniprot.org/annotation/VAR_086630|||http://purl.uniprot.org/annotation/VAR_086631|||http://purl.uniprot.org/annotation/VAR_086632|||http://purl.uniprot.org/annotation/VAR_086633|||http://purl.uniprot.org/annotation/VAR_086634|||http://purl.uniprot.org/annotation/VAR_086635|||http://purl.uniprot.org/annotation/VAR_086636|||http://purl.uniprot.org/annotation/VAR_086637|||http://purl.uniprot.org/annotation/VAR_086638|||http://purl.uniprot.org/annotation/VAR_086639|||http://purl.uniprot.org/annotation/VAR_086640|||http://purl.uniprot.org/annotation/VAR_086641|||http://purl.uniprot.org/annotation/VAR_086642|||http://purl.uniprot.org/annotation/VAR_086643|||http://purl.uniprot.org/annotation/VAR_086644|||http://purl.uniprot.org/annotation/VAR_086645|||http://purl.uniprot.org/annotation/VAR_086646|||http://purl.uniprot.org/annotation/VAR_086647|||http://purl.uniprot.org/annotation/VAR_086648|||http://purl.uniprot.org/annotation/VAR_086649|||http://purl.uniprot.org/annotation/VAR_086650|||http://purl.uniprot.org/annotation/VAR_086651|||http://purl.uniprot.org/annotation/VAR_086652|||http://purl.uniprot.org/annotation/VAR_086653|||http://purl.uniprot.org/annotation/VAR_086654
http://togogenome.org/gene/9606:PPP1R3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0D2I0|||http://purl.uniprot.org/uniprot/Q6ZSY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||CBM21|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||PP1-binding motif|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 3F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257496|||http://purl.uniprot.org/annotation/VAR_028918|||http://purl.uniprot.org/annotation/VAR_076266|||http://purl.uniprot.org/annotation/VSP_045003|||http://purl.uniprot.org/annotation/VSP_045004
http://togogenome.org/gene/9606:JUND                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17535                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic motif|||Disordered|||Interchain (with C-172 in FOSB)|||Leucine-zipper|||Loss of interaction with MEN1.|||Loss of phosphorylation; when associated with A-46.|||Loss of phosphorylation; when associated with A-47.|||Loss of phosphorylation; when associated with A-52.|||Loss of phosphorylation; when associated with A-54.|||MAP kinase docking motif; essential for its phosphorylation|||Menin-binding motif (MBM)|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine|||Reduced interaction with MEN1.|||Reduced interaction with MEN1; when associated with E-46.|||Reduced interaction with MEN1; when associated with E-47.|||Transcription factor JunD|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076442|||http://purl.uniprot.org/annotation/VAR_055247
http://togogenome.org/gene/9606:NPHP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JNM7|||http://purl.uniprot.org/uniprot/O15259                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Changed function; unable to rescue the corresponding loss of function zebrafish mutant which displays a cilium function alteration phenotype.|||Disordered|||Does not affect fold stability, as assessed by circular dichroism thermal denaturation melting curves and by NMR spectroscopy. Affects interaction with PKD1.|||Impairs interaction with PACS1; when associated with A-121 and A-123.|||Impairs interaction with PACS1; when associated with A-121 and A-126.|||Impairs interaction with PACS1; when associated with A-123 and A-126.|||In NPHP1; associated with Cogan-type congenital ocular motor apraxia.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of SH3 domain fold.|||Nephrocystin-1|||Phosphoserine; by CK2|||Phosphotyrosine; by FAK2|||Phosphotyrosine; by SRC|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159585|||http://purl.uniprot.org/annotation/VAR_012160|||http://purl.uniprot.org/annotation/VAR_077633|||http://purl.uniprot.org/annotation/VSP_003424|||http://purl.uniprot.org/annotation/VSP_010073|||http://purl.uniprot.org/annotation/VSP_010074|||http://purl.uniprot.org/annotation/VSP_024381
http://togogenome.org/gene/9606:PCDHGA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003954|||http://purl.uniprot.org/annotation/VAR_048557|||http://purl.uniprot.org/annotation/VAR_048558|||http://purl.uniprot.org/annotation/VAR_048559|||http://purl.uniprot.org/annotation/VSP_008665|||http://purl.uniprot.org/annotation/VSP_008666
http://togogenome.org/gene/9606:PACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H813                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Proton-activated chloride channel|||Reduced I(-) permeability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279471|||http://purl.uniprot.org/annotation/VAR_035847|||http://purl.uniprot.org/annotation/VSP_042887
http://togogenome.org/gene/9606:MCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43121                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell surface glycoprotein MUC18|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014891|||http://purl.uniprot.org/annotation/VAR_049915|||http://purl.uniprot.org/annotation/VSP_016938|||http://purl.uniprot.org/annotation/VSP_016939
http://togogenome.org/gene/9606:GPR108                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPR9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Protein GPR108                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045083|||http://purl.uniprot.org/annotation/VAR_056112|||http://purl.uniprot.org/annotation/VAR_060483
http://togogenome.org/gene/9606:RBM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWF3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115.|||Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113.|||Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115.|||Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115.|||CCHC-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits IRES-mediated mRNA translation. Does not inhibit interaction with EIF4A1. Inhibits localization in cytoplasm and cytoplasmic granules upon cell muscle differentiation. Inhibits negative regulation of translation involved in gene silencing by miRNA.|||Interaction with TNPO3|||Phosphoserine|||RNA-binding protein 4|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081754|||http://purl.uniprot.org/annotation/VSP_013413|||http://purl.uniprot.org/annotation/VSP_013414|||http://purl.uniprot.org/annotation/VSP_013415|||http://purl.uniprot.org/annotation/VSP_013416|||http://purl.uniprot.org/annotation/VSP_044493
http://togogenome.org/gene/9606:SGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7S9|||http://purl.uniprot.org/uniprot/Q562F6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Shugoshin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055439|||http://purl.uniprot.org/annotation/VAR_024784|||http://purl.uniprot.org/annotation/VAR_024785|||http://purl.uniprot.org/annotation/VAR_057178|||http://purl.uniprot.org/annotation/VAR_057179|||http://purl.uniprot.org/annotation/VAR_057180|||http://purl.uniprot.org/annotation/VAR_057181|||http://purl.uniprot.org/annotation/VSP_016798|||http://purl.uniprot.org/annotation/VSP_016799|||http://purl.uniprot.org/annotation/VSP_016800
http://togogenome.org/gene/9606:CASC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15234                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Turn                                                                                  ^@                                                                                  Abolishes interaction with EIF4A3, EJC formation and localization in nucleus speckles.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not affect EJC formation.|||Necessary for RNA-binding, interaction with MAGOH and localization in nucleus speckles|||Necessary for localization in cytoplasmic stress granules|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein CASC3|||Sufficient to form the EJC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089324
http://togogenome.org/gene/9606:GATA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92908                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ASD9 and TOF; loss of transcriptional activity.|||In AVSD5; increased transcriptional activity.|||In CTHM; persistent truncus arteriosus; loss of transcriptional activity.|||In PACHD.|||In PACHD; loss of transcriptional activity.|||In TOF; uncertain pathological significance; does not affect transcriptional activity.|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in patients with atrial fibrillation; gain of function; no effect on subcellular localization.|||Probable disease-associated variant found in patients with atrial fibrillation; significant loss of transcriptional activator activity.|||Transcription factor GATA-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083423|||http://purl.uniprot.org/annotation/VAR_067380|||http://purl.uniprot.org/annotation/VAR_067381|||http://purl.uniprot.org/annotation/VAR_067382|||http://purl.uniprot.org/annotation/VAR_067383|||http://purl.uniprot.org/annotation/VAR_067384|||http://purl.uniprot.org/annotation/VAR_067385|||http://purl.uniprot.org/annotation/VAR_067386|||http://purl.uniprot.org/annotation/VAR_067387|||http://purl.uniprot.org/annotation/VAR_067388|||http://purl.uniprot.org/annotation/VAR_067389|||http://purl.uniprot.org/annotation/VAR_067390|||http://purl.uniprot.org/annotation/VAR_078427|||http://purl.uniprot.org/annotation/VAR_078428|||http://purl.uniprot.org/annotation/VAR_078429|||http://purl.uniprot.org/annotation/VAR_078430|||http://purl.uniprot.org/annotation/VAR_078431|||http://purl.uniprot.org/annotation/VAR_078432|||http://purl.uniprot.org/annotation/VSP_035778
http://togogenome.org/gene/9606:PDCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4E4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Phosducin-like protein 2|||Thioredoxin fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246157
http://togogenome.org/gene/9606:CDC42BPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT25                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||CNH|||CRIB|||Cleavage; by CASP3 in vitro|||Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||Increase in autophosphorylation but not kinase activity.|||Loss of CDC42 binding; when associated with A-1579.|||Loss of CDC42 binding; when associated with A-1582.|||Loss of autophosphorylation and kinase activity.|||Loss of kinase activity.|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Prevents cleavage by CASP3, impairs the increase of its kinase activity and impairs extrusion apical actin ring assembly.|||Prevents cleavage by CASP3.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MRCK alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086392|||http://purl.uniprot.org/annotation/VAR_040830|||http://purl.uniprot.org/annotation/VAR_040831|||http://purl.uniprot.org/annotation/VAR_040832|||http://purl.uniprot.org/annotation/VAR_040833|||http://purl.uniprot.org/annotation/VAR_045583|||http://purl.uniprot.org/annotation/VAR_045584|||http://purl.uniprot.org/annotation/VAR_045585|||http://purl.uniprot.org/annotation/VAR_045586|||http://purl.uniprot.org/annotation/VAR_045587|||http://purl.uniprot.org/annotation/VAR_045588|||http://purl.uniprot.org/annotation/VAR_045589|||http://purl.uniprot.org/annotation/VAR_045590|||http://purl.uniprot.org/annotation/VAR_057104|||http://purl.uniprot.org/annotation/VSP_035286|||http://purl.uniprot.org/annotation/VSP_051859|||http://purl.uniprot.org/annotation/VSP_051860|||http://purl.uniprot.org/annotation/VSP_051861|||http://purl.uniprot.org/annotation/VSP_051862|||http://purl.uniprot.org/annotation/VSP_051863
http://togogenome.org/gene/9606:NIPAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NVV3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Magnesium transporter NIPA3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242146|||http://purl.uniprot.org/annotation/VAR_026843
http://togogenome.org/gene/9606:SLC16A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTY0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Monocarboxylate transporter 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287187
http://togogenome.org/gene/9606:PRR16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q569H4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues|||Protein Largen                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308159|||http://purl.uniprot.org/annotation/VAR_061694|||http://purl.uniprot.org/annotation/VSP_028880|||http://purl.uniprot.org/annotation/VSP_028881
http://togogenome.org/gene/9606:MYO7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13402                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||FERM 1|||FERM 2|||Found in a patient with Leber congenital amaurosis; unknown pathological significance.|||Found in patients with retinitis pigmentosa; unknown pathological significance.|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||In DFNA11.|||In DFNA11; disturb calmodulin/MYO7A binding.|||In DFNB2.|||In USH1B.|||In USH1B; atypical.|||In USH1B; is predicted to alter the normal splicing of exon 6.|||In USH1B; unknown pathological significance.|||In isoform 2 and isoform 8.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||MyTH4 1|||MyTH4 2|||Myosin motor|||Phosphoserine|||Phosphothreonine|||SAH|||SH3|||Unconventional myosin-VIIa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123466|||http://purl.uniprot.org/annotation/VAR_009315|||http://purl.uniprot.org/annotation/VAR_009316|||http://purl.uniprot.org/annotation/VAR_009317|||http://purl.uniprot.org/annotation/VAR_009318|||http://purl.uniprot.org/annotation/VAR_009319|||http://purl.uniprot.org/annotation/VAR_009320|||http://purl.uniprot.org/annotation/VAR_009321|||http://purl.uniprot.org/annotation/VAR_009322|||http://purl.uniprot.org/annotation/VAR_009323|||http://purl.uniprot.org/annotation/VAR_009324|||http://purl.uniprot.org/annotation/VAR_009325|||http://purl.uniprot.org/annotation/VAR_009326|||http://purl.uniprot.org/annotation/VAR_009327|||http://purl.uniprot.org/annotation/VAR_009328|||http://purl.uniprot.org/annotation/VAR_009329|||http://purl.uniprot.org/annotation/VAR_009330|||http://purl.uniprot.org/annotation/VAR_009331|||http://purl.uniprot.org/annotation/VAR_009332|||http://purl.uniprot.org/annotation/VAR_009333|||http://purl.uniprot.org/annotation/VAR_009334|||http://purl.uniprot.org/annotation/VAR_009335|||http://purl.uniprot.org/annotation/VAR_009336|||http://purl.uniprot.org/annotation/VAR_009337|||http://purl.uniprot.org/annotation/VAR_009338|||http://purl.uniprot.org/annotation/VAR_009339|||http://purl.uniprot.org/annotation/VAR_009340|||http://purl.uniprot.org/annotation/VAR_009341|||http://purl.uniprot.org/annotation/VAR_009343|||http://purl.uniprot.org/annotation/VAR_009344|||http://purl.uniprot.org/annotation/VAR_009345|||http://purl.uniprot.org/annotation/VAR_009346|||http://purl.uniprot.org/annotation/VAR_009347|||http://purl.uniprot.org/annotation/VAR_009348|||http://purl.uniprot.org/annotation/VAR_024039|||http://purl.uniprot.org/annotation/VAR_024040|||http://purl.uniprot.org/annotation/VAR_024041|||http://purl.uniprot.org/annotation/VAR_024042|||http://purl.uniprot.org/annotation/VAR_024043|||http://purl.uniprot.org/annotation/VAR_024044|||http://purl.uniprot.org/annotation/VAR_024045|||http://purl.uniprot.org/annotation/VAR_024046|||http://purl.uniprot.org/annotation/VAR_024047|||http://purl.uniprot.org/annotation/VAR_024048|||http://purl.uniprot.org/annotation/VAR_024049|||http://purl.uniprot.org/annotation/VAR_024050|||http://purl.uniprot.org/annotation/VAR_024051|||http://purl.uniprot.org/annotation/VAR_024052|||http://purl.uniprot.org/annotation/VAR_024053|||http://purl.uniprot.org/annotation/VAR_024054|||http://purl.uniprot.org/annotation/VAR_024055|||http://purl.uniprot.org/annotation/VAR_027301|||http://purl.uniprot.org/annotation/VAR_027302|||http://purl.uniprot.org/annotation/VAR_027303|||http://purl.uniprot.org/annotation/VAR_027304|||http://purl.uniprot.org/annotation/VAR_027305|||http://purl.uniprot.org/annotation/VAR_027306|||http://purl.uniprot.org/annotation/VAR_027307|||http://purl.uniprot.org/annotation/VAR_027308|||http://purl.uniprot.org/annotation/VAR_027309|||http://purl.uniprot.org/annotation/VAR_027310|||http://purl.uniprot.org/annotation/VAR_027311|||http://purl.uniprot.org/annotation/VAR_027312|||http://purl.uniprot.org/annotation/VAR_027313|||http://purl.uniprot.org/annotation/VAR_027314|||http://purl.uniprot.org/annotation/VAR_027315|||http://purl.uniprot.org/annotation/VAR_027316|||http://purl.uniprot.org/annotation/VAR_056187|||http://purl.uniprot.org/annotation/VAR_056188|||http://purl.uniprot.org/annotation/VAR_066861|||http://purl.uniprot.org/annotation/VAR_071646|||http://purl.uniprot.org/annotation/VAR_071647|||http://purl.uniprot.org/annotation/VAR_074074|||http://purl.uniprot.org/annotation/VAR_077020|||http://purl.uniprot.org/annotation/VAR_079504|||http://purl.uniprot.org/annotation/VSP_003353|||http://purl.uniprot.org/annotation/VSP_003354|||http://purl.uniprot.org/annotation/VSP_003355|||http://purl.uniprot.org/annotation/VSP_003356|||http://purl.uniprot.org/annotation/VSP_003357|||http://purl.uniprot.org/annotation/VSP_003358|||http://purl.uniprot.org/annotation/VSP_003359|||http://purl.uniprot.org/annotation/VSP_003360|||http://purl.uniprot.org/annotation/VSP_045848|||http://purl.uniprot.org/annotation/VSP_053793
http://togogenome.org/gene/9606:DXO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCW8|||http://purl.uniprot.org/uniprot/O77932                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-236.|||Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-253.|||Basic and acidic residues|||Decapping and exoribonuclease protein|||Disordered|||Impaired subcellular location, leading to localization both in cytoplasm and nucleus.|||Phosphoserine|||Phosphothreonine|||RAI1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249822|||http://purl.uniprot.org/annotation/VAR_027492|||http://purl.uniprot.org/annotation/VAR_027493|||http://purl.uniprot.org/annotation/VAR_027494|||http://purl.uniprot.org/annotation/VAR_027495
http://togogenome.org/gene/9606:GPATCH11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N954                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||G patch domain-containing protein 11|||G-patch|||In isoform 2.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279751|||http://purl.uniprot.org/annotation/VSP_023505|||http://purl.uniprot.org/annotation/VSP_023506
http://togogenome.org/gene/9606:RAB8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92930                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Loss of phosphorylation. No effect on GDI1 and GDI2 binding. Reduced binding to CHM and CHML.|||Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM, and CHML.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-8B|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121134|||http://purl.uniprot.org/annotation/PRO_0000370800
http://togogenome.org/gene/9606:RIMBP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNM3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Polar residues|||Pro residues|||RIMS-binding protein 3B|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332274
http://togogenome.org/gene/9606:OLFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IMJ7|||http://purl.uniprot.org/uniprot/Q6IMJ8|||http://purl.uniprot.org/uniprot/Q99784                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||Interchain|||N-linked (GlcNAc...) asparagine|||Noelin|||Olfactomedin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020074|||http://purl.uniprot.org/annotation/PRO_5014310480|||http://purl.uniprot.org/annotation/PRO_5014310481|||http://purl.uniprot.org/annotation/VSP_003759|||http://purl.uniprot.org/annotation/VSP_003760|||http://purl.uniprot.org/annotation/VSP_003761|||http://purl.uniprot.org/annotation/VSP_055625
http://togogenome.org/gene/9606:WNT8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RF47|||http://purl.uniprot.org/uniprot/Q9H1J5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine|||Protein Wnt|||Protein Wnt-8a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041448|||http://purl.uniprot.org/annotation/PRO_5003087767|||http://purl.uniprot.org/annotation/VSP_038706
http://togogenome.org/gene/9606:ANKRD22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYY1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240838|||http://purl.uniprot.org/annotation/VAR_027628|||http://purl.uniprot.org/annotation/VAR_027629|||http://purl.uniprot.org/annotation/VAR_027630|||http://purl.uniprot.org/annotation/VAR_027631
http://togogenome.org/gene/9606:ZNF583                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ND8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 583                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047674|||http://purl.uniprot.org/annotation/VAR_027978
http://togogenome.org/gene/9606:BHLHE23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXG3|||http://purl.uniprot.org/uniprot/Q8NDY6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Class E basic helix-loop-helix protein 23|||Disordered|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245526
http://togogenome.org/gene/9606:OR10A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN8|||http://purl.uniprot.org/uniprot/Q8NH74                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10A6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150689|||http://purl.uniprot.org/annotation/VAR_053263|||http://purl.uniprot.org/annotation/VAR_053264|||http://purl.uniprot.org/annotation/VAR_053265
http://togogenome.org/gene/9606:KLK11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1R3UDR5|||http://purl.uniprot.org/uniprot/Q9UBX7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 1 and isoform 4.|||In isoform 3 and isoform 4.|||Kallikrein-11|||Kallikrein-11 inactive chain 1|||Kallikrein-11 inactive chain 2|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027954|||http://purl.uniprot.org/annotation/PRO_0000027955|||http://purl.uniprot.org/annotation/PRO_0000302061|||http://purl.uniprot.org/annotation/PRO_0000302062|||http://purl.uniprot.org/annotation/PRO_5010376006|||http://purl.uniprot.org/annotation/VAR_021943|||http://purl.uniprot.org/annotation/VAR_024296|||http://purl.uniprot.org/annotation/VAR_051856|||http://purl.uniprot.org/annotation/VSP_005402|||http://purl.uniprot.org/annotation/VSP_043326
http://togogenome.org/gene/9606:NDRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TH30|||http://purl.uniprot.org/uniprot/Q9UGV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein NDRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159577|||http://purl.uniprot.org/annotation/VSP_003419|||http://purl.uniprot.org/annotation/VSP_003420
http://togogenome.org/gene/9606:ZNF843                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N446                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2; degenerate|||Disordered|||Polar residues|||Zinc finger protein 843                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343750
http://togogenome.org/gene/9606:MTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99707                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AdoMet activation|||B12-binding|||B12-binding N-terminal|||Decreases binding to MTRR; when associated with E-963.|||Decreases binding to MTRR; when associated with N-1071.|||Hcy-binding|||In HMAG.|||In isoform 2.|||Methionine synthase|||Phosphothreonine|||Pterin-binding|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204530|||http://purl.uniprot.org/annotation/VAR_004326|||http://purl.uniprot.org/annotation/VAR_004327|||http://purl.uniprot.org/annotation/VAR_004328|||http://purl.uniprot.org/annotation/VAR_004329|||http://purl.uniprot.org/annotation/VAR_004330|||http://purl.uniprot.org/annotation/VAR_004331|||http://purl.uniprot.org/annotation/VAR_050033|||http://purl.uniprot.org/annotation/VAR_061338|||http://purl.uniprot.org/annotation/VSP_057283
http://togogenome.org/gene/9606:TRAF3IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDR0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes microtubules-binding when missing|||Basic and acidic residues|||DISC1-interaction domain|||Disordered|||In SLSN9; does not localize to the ciliary tip.|||In SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4.|||In SLSN9; results in altered folding of the N-terminus; does not localize to the ciliary tip and transition zone; does not affect interaction with IFT20; loss of interaction with MAP4.|||In isoform 2.|||Phosphoserine|||Polar residues|||TRAF3-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299544|||http://purl.uniprot.org/annotation/VAR_034841|||http://purl.uniprot.org/annotation/VAR_034842|||http://purl.uniprot.org/annotation/VAR_034843|||http://purl.uniprot.org/annotation/VAR_051185|||http://purl.uniprot.org/annotation/VAR_061685|||http://purl.uniprot.org/annotation/VAR_075068|||http://purl.uniprot.org/annotation/VAR_075069|||http://purl.uniprot.org/annotation/VAR_075070|||http://purl.uniprot.org/annotation/VAR_075071|||http://purl.uniprot.org/annotation/VSP_027734
http://togogenome.org/gene/9606:FAM184B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM184B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320551|||http://purl.uniprot.org/annotation/VAR_039202|||http://purl.uniprot.org/annotation/VAR_039203
http://togogenome.org/gene/9606:ARHGAP39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS00|||http://purl.uniprot.org/uniprot/B4DK23|||http://purl.uniprot.org/uniprot/Q6PJQ0|||http://purl.uniprot.org/uniprot/Q9C0H5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MyTH4|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||Rho GTPase-activating protein 39|||Rho-GAP|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076092|||http://purl.uniprot.org/annotation/VSP_040749
http://togogenome.org/gene/9606:PEX11G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HA9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Peroxisomal membrane protein 11C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105970|||http://purl.uniprot.org/annotation/VAR_024560|||http://purl.uniprot.org/annotation/VSP_013539
http://togogenome.org/gene/9606:MAP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78559|||http://purl.uniprot.org/uniprot/Q504X9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 3 AA repeats of K-K-[DE]|||Basic and acidic residues|||Disordered|||In isoform 2.|||MAP1 light chain LC2|||MAP1A heavy chain|||Microtubule-associated protein 1A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018600|||http://purl.uniprot.org/annotation/PRO_0000018601|||http://purl.uniprot.org/annotation/PRO_0000418376|||http://purl.uniprot.org/annotation/VAR_039705|||http://purl.uniprot.org/annotation/VAR_039706|||http://purl.uniprot.org/annotation/VAR_039707|||http://purl.uniprot.org/annotation/VAR_039708|||http://purl.uniprot.org/annotation/VAR_039709|||http://purl.uniprot.org/annotation/VAR_039710|||http://purl.uniprot.org/annotation/VAR_039711|||http://purl.uniprot.org/annotation/VAR_039712|||http://purl.uniprot.org/annotation/VAR_039713|||http://purl.uniprot.org/annotation/VAR_039714|||http://purl.uniprot.org/annotation/VAR_039715|||http://purl.uniprot.org/annotation/VAR_039716|||http://purl.uniprot.org/annotation/VAR_039717|||http://purl.uniprot.org/annotation/VAR_039718|||http://purl.uniprot.org/annotation/VAR_039719|||http://purl.uniprot.org/annotation/VAR_039720|||http://purl.uniprot.org/annotation/VAR_039721|||http://purl.uniprot.org/annotation/VAR_039722|||http://purl.uniprot.org/annotation/VAR_039723|||http://purl.uniprot.org/annotation/VAR_039724|||http://purl.uniprot.org/annotation/VAR_039725|||http://purl.uniprot.org/annotation/VAR_039726|||http://purl.uniprot.org/annotation/VAR_039727|||http://purl.uniprot.org/annotation/VAR_039728|||http://purl.uniprot.org/annotation/VAR_056122|||http://purl.uniprot.org/annotation/VAR_059432|||http://purl.uniprot.org/annotation/VAR_059433|||http://purl.uniprot.org/annotation/VSP_040240
http://togogenome.org/gene/9606:SYNE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N205                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Interchain (with C-563 in SUN2); alternate|||Interchain (with C-657 in SUN1)|||KASH|||Nesprin-4|||Perinuclear space|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306264|||http://purl.uniprot.org/annotation/VAR_035284|||http://purl.uniprot.org/annotation/VAR_035285|||http://purl.uniprot.org/annotation/VSP_028444
http://togogenome.org/gene/9606:TNS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J7F3|||http://purl.uniprot.org/uniprot/C9JHU5|||http://purl.uniprot.org/uniprot/Q68CZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation. Abolishes interaction with DLC1 and p85.|||C2 tensin-type|||Constitutive interaction with p85 and interaction with DLC1 after EGF stimulation.|||Constitutive interaction with p85.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PTB|||Phorbol-ester/DAG-type|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH2|||Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1206.|||Significantly reduced interaction with PEAK1; when associated with F-1173 and F-1256.|||Significantly reduced interaction with PEAK1; when associated with F-1206 and F-1256.|||Tensin-3|||Tyrosine specific protein phosphatases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295915|||http://purl.uniprot.org/annotation/VAR_034593|||http://purl.uniprot.org/annotation/VAR_034594|||http://purl.uniprot.org/annotation/VAR_052548|||http://purl.uniprot.org/annotation/VSP_027123|||http://purl.uniprot.org/annotation/VSP_027124|||http://purl.uniprot.org/annotation/VSP_027125|||http://purl.uniprot.org/annotation/VSP_027126|||http://purl.uniprot.org/annotation/VSP_027127
http://togogenome.org/gene/9606:C17orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4C9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Uncharacterized protein C17orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300630|||http://purl.uniprot.org/annotation/VAR_034877|||http://purl.uniprot.org/annotation/VSP_027838|||http://purl.uniprot.org/annotation/VSP_027839
http://togogenome.org/gene/9606:GOLGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92805                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Decreased TBC1D23-binding.|||Disordered|||Drastically reduced targeting to the Golgi apparatus, small decrease in RAB6A-binding.|||GRIP|||Golgin subfamily A member 1|||Loss of RAB6A-binding and of targeting to the Golgi apparatus.|||Loss of TBC1D23-binding.|||No effect on RAB6A-binding, nor on targeting to the Golgi apparatus.|||No effect on TBC1D23-binding.|||No effect on subcellular localization at the Golgi apparatus, small decrease in RAB6A-binding.|||No effect on subcellular localization at the Golgi apparatus.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190052|||http://purl.uniprot.org/annotation/VAR_047842|||http://purl.uniprot.org/annotation/VAR_047843|||http://purl.uniprot.org/annotation/VAR_047844
http://togogenome.org/gene/9606:BIRC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes inhibition of caspases and anti-apoptotic activity.|||Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity.|||BIR|||Baculoviral IAP repeat-containing protein 7|||Baculoviral IAP repeat-containing protein 7 30kDa subunit|||Cleavage; by CASP3 and CASP7|||Disordered|||In isoform 1.|||No change in SMAC interaction and anti-apoptotic activity.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122362|||http://purl.uniprot.org/annotation/PRO_0000416092|||http://purl.uniprot.org/annotation/VAR_020253|||http://purl.uniprot.org/annotation/VSP_002459
http://togogenome.org/gene/9606:S100A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29034                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Protein S100-A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143971
http://togogenome.org/gene/9606:C4BPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04003                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C4b-binding protein alpha chain|||Interchain (with beta chain)|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005888|||http://purl.uniprot.org/annotation/VAR_001978|||http://purl.uniprot.org/annotation/VAR_012038|||http://purl.uniprot.org/annotation/VAR_024420|||http://purl.uniprot.org/annotation/VAR_048815|||http://purl.uniprot.org/annotation/VAR_061123|||http://purl.uniprot.org/annotation/VAR_061124
http://togogenome.org/gene/9606:RRM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LG56                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with combined respiratory complex deficiencies, muscle weakness and hearing loss; unknown pathological significance.|||In MTDPS8A.|||In MTDPS8A; without tubulopathy.|||In MTDPS8B.|||In RCDFRD.|||In colorectal adenocarcinomas cell line; loss of ribonucleotide reductase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Ribonucleoside-diphosphate reductase subunit M2 B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228150|||http://purl.uniprot.org/annotation/VAR_025699|||http://purl.uniprot.org/annotation/VAR_046217|||http://purl.uniprot.org/annotation/VAR_046218|||http://purl.uniprot.org/annotation/VAR_046219|||http://purl.uniprot.org/annotation/VAR_046220|||http://purl.uniprot.org/annotation/VAR_046221|||http://purl.uniprot.org/annotation/VAR_046222|||http://purl.uniprot.org/annotation/VAR_046223|||http://purl.uniprot.org/annotation/VAR_046224|||http://purl.uniprot.org/annotation/VAR_065122|||http://purl.uniprot.org/annotation/VAR_065123|||http://purl.uniprot.org/annotation/VAR_076280|||http://purl.uniprot.org/annotation/VAR_086956|||http://purl.uniprot.org/annotation/VSP_017668|||http://purl.uniprot.org/annotation/VSP_017669|||http://purl.uniprot.org/annotation/VSP_017670|||http://purl.uniprot.org/annotation/VSP_017671|||http://purl.uniprot.org/annotation/VSP_017672|||http://purl.uniprot.org/annotation/VSP_053585
http://togogenome.org/gene/9606:HLA-DQB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01920|||http://purl.uniprot.org/uniprot/Q5SU54|||http://purl.uniprot.org/uniprot/Q5Y7A9|||http://purl.uniprot.org/uniprot/Q5Y7D6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1|||Beta-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DQ beta 1 chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DQB1*02:01 and allele DQB1*02:02.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04 and allele DQB1*02:05; requires 2 nucleotide substitutions.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05 and allele DQB1*06:06.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:10, allele DQB1*03:11, allele DQB1*03:12, allele DQB1*03:14, allele DQB1*03:15, allele DQB1*03:17, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:15, allele DQB1*03:17, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:06, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:12, allele DQB1*03:15, allele DQB1*03:18, allele DQB1*03:20, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*03:26, allele DQB1*04:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:06.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:04, allele DQB1*06:01 and allele DQB1*06:35.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*06:01, allele DQB1*06:28 and allele DQB1*06:35.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:03, allele DQB1*02:04, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:06.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*02:05, allele DQB1*03:02, allele DQB1*03:04, allele DQB1*03:05, allele DQB1*03:07, allele DQB1*03:08, allele DQB1*03:11, allele DQB1*03:14, allele DQB1*03:18 and allele DQB1*06:29.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:23, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*02:01, allele DQB1*02:02, allele DQB1*02:04, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*02:02.|||In allele DQB1*02:04.|||In allele DQB1*03:02, allele DQB1*03:03, allele DQB1*03:05, allele DQB1*03:19, allele DQB1*03:25, allele DQB1*04:01 and allele DQB1*04:02.|||In allele DQB1*03:02, allele DQB1*03:03, allele DQB1*04:01, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12.|||In allele DQB1*03:05, allele DQB1*03:17, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05 and allele DQB1*06:23; requires 2 nucleotide substitutions.|||In allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03 and allele DQB1*05:04; requires 2 nucleotide substitutions.|||In allele DQB1*03:06, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04 and allele DQB1*05:05; requires 2 nucleotide substitutions.|||In allele DQB1*03:07.|||In allele DQB1*03:08, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31 and allele DQB1*06:33.|||In allele DQB1*03:09.|||In allele DQB1*03:11, allele DQB1*03:26, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:05, allele DQB1*06:20 and allele DQB1*06:31.|||In allele DQB1*03:13.|||In allele DQB1*03:15.|||In allele DQB1*03:16.|||In allele DQB1*03:18.|||In allele DQB1*03:20.|||In allele DQB1*03:21.|||In allele DQB1*03:22, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36 and allele DQB1*06:38.|||In allele DQB1*03:23, allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*03:23, allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:20, allele DQB1*06:22, allele DQB1*06:21, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*03:24.|||In allele DQB1*03:25, allele DQB1*04:01, allele DQB1*04:02 and allele DQB1*04:03.|||In allele DQB1*04:01, allele DQB1*04:02, allele DQB1*04:03, allele DQB1*06:02, allele DQB1*06:10, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:29, allele DQB1*06:33 and allele DQB1*06:37.|||In allele DQB1*04:01.|||In allele DQB1*05:01 and allele DQB1*05:02.|||In allele DQB1*05:01, allele DQB1*05:02 and allele DQB1*05:03.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38, allele DQB1*06:39.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:12, allele DQB1*06:14, allele DQB1*06:15, allele DQB1*06:16, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:34, allele DQB1*06:35, allele DQB1*06:36, allele DQB1*06:37, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:35 and allele DQB1*06:37.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:07, allele DQB1*06:08, allele DQB1*06:14, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:25, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:15, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:25, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39; requires 2 nucleotide substitutions.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*05:05, allele DQB1*06:17, allele DQB1*06:24 and allele DQB1*06:30.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12 and allele DQB1*06:36.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*05:03, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12 and allele DQB1*06:36.|||In allele DQB1*05:01, allele DQB1*05:02, allele DQB1*06:02 and allele DQB1*06:12.|||In allele DQB1*05:01, allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:06, allele DQB1*06:08, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:13, allele DQB1*06:17, allele DQB1*06:18, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:27, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*05:02, allele DQB1*05:04, allele DQB1*05:05, allele DQB1*06:10 and allele DQB1*06:25; requires 2 nucleotide substitutions.|||In allele DQB1*05:02.|||In allele DQB1*06:01 and allele DQB1*06:35.|||In allele DQB1*06:01 and allele DQB1*06:35; requires 2 nucleotide substitutions.|||In allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:04, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*06:01, allele DQB1*06:02, allele DQB1*06:03, allele DQB1*06:08, allele DQB1*06:10, allele DQB1*06:11, allele DQB1*06:13, allele DQB1*06:14, allele DQB1*06:16, allele DQB1*06:18, allele DQB1*06:19, allele DQB1*06:20, allele DQB1*06:23, allele DQB1*06:24, allele DQB1*06:27, allele DQB1*06:28, allele DQB1*06:29, allele DQB1*06:30, allele DQB1*06:31, allele DQB1*06:32, allele DQB1*06:33, allele DQB1*06:35 and allele DQB1*06:37.|||In allele DQB1*06:01.|||In allele DQB1*06:02 and allele DQB1*06:12.|||In allele DQB1*06:04, allele DQB1*06:05, allele DQB1*06:07, allele DQB1*06:09, allele DQB1*06:12, allele DQB1*06:15, allele DQB1*06:17, allele DQB1*06:21, allele DQB1*06:22, allele DQB1*06:25, allele DQB1*06:34, allele DQB1*06:36, allele DQB1*06:38 and allele DQB1*06:39.|||In allele DQB1*06:16.|||In allele DQB1*06:33.|||In allele DQB1*06:36.|||In allele DQB1*06:37.|||In allele DQB1*06:38.|||N-linked (GlcNAc...) asparagine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018989|||http://purl.uniprot.org/annotation/PRO_5011947286|||http://purl.uniprot.org/annotation/PRO_5014586887|||http://purl.uniprot.org/annotation/PRO_5014587155|||http://purl.uniprot.org/annotation/VAR_056570|||http://purl.uniprot.org/annotation/VAR_056571|||http://purl.uniprot.org/annotation/VAR_056572|||http://purl.uniprot.org/annotation/VAR_059522|||http://purl.uniprot.org/annotation/VAR_061472|||http://purl.uniprot.org/annotation/VAR_061473|||http://purl.uniprot.org/annotation/VAR_061474|||http://purl.uniprot.org/annotation/VAR_062679|||http://purl.uniprot.org/annotation/VAR_062680|||http://purl.uniprot.org/annotation/VAR_062681|||http://purl.uniprot.org/annotation/VAR_062682|||http://purl.uniprot.org/annotation/VAR_062683|||http://purl.uniprot.org/annotation/VAR_062684|||http://purl.uniprot.org/annotation/VAR_062685|||http://purl.uniprot.org/annotation/VAR_062686|||http://purl.uniprot.org/annotation/VAR_062687|||http://purl.uniprot.org/annotation/VAR_062688|||http://purl.uniprot.org/annotation/VAR_062689|||http://purl.uniprot.org/annotation/VAR_062690|||http://purl.uniprot.org/annotation/VAR_062691|||http://purl.uniprot.org/annotation/VAR_062692|||http://purl.uniprot.org/annotation/VAR_062693|||http://purl.uniprot.org/annotation/VAR_062694|||http://purl.uniprot.org/annotation/VAR_062695|||http://purl.uniprot.org/annotation/VAR_062696|||http://purl.uniprot.org/annotation/VAR_062697|||http://purl.uniprot.org/annotation/VAR_062698|||http://purl.uniprot.org/annotation/VAR_062699|||http://purl.uniprot.org/annotation/VAR_062700|||http://purl.uniprot.org/annotation/VAR_062701|||http://purl.uniprot.org/annotation/VAR_062702|||http://purl.uniprot.org/annotation/VAR_062703|||http://purl.uniprot.org/annotation/VAR_062704|||http://purl.uniprot.org/annotation/VAR_062705|||http://purl.uniprot.org/annotation/VAR_062706|||http://purl.uniprot.org/annotation/VAR_062707|||http://purl.uniprot.org/annotation/VAR_062708|||http://purl.uniprot.org/annotation/VAR_062709|||http://purl.uniprot.org/annotation/VAR_062710|||http://purl.uniprot.org/annotation/VAR_062711|||http://purl.uniprot.org/annotation/VAR_062712|||http://purl.uniprot.org/annotation/VAR_062713|||http://purl.uniprot.org/annotation/VAR_062714|||http://purl.uniprot.org/annotation/VAR_062715|||http://purl.uniprot.org/annotation/VAR_062716|||http://purl.uniprot.org/annotation/VAR_062717|||http://purl.uniprot.org/annotation/VAR_062718|||http://purl.uniprot.org/annotation/VAR_062719|||http://purl.uniprot.org/annotation/VAR_062720|||http://purl.uniprot.org/annotation/VAR_062721|||http://purl.uniprot.org/annotation/VAR_062722|||http://purl.uniprot.org/annotation/VAR_062723|||http://purl.uniprot.org/annotation/VAR_062724|||http://purl.uniprot.org/annotation/VAR_062725|||http://purl.uniprot.org/annotation/VAR_062726|||http://purl.uniprot.org/annotation/VAR_062727|||http://purl.uniprot.org/annotation/VAR_062728|||http://purl.uniprot.org/annotation/VAR_062729|||http://purl.uniprot.org/annotation/VAR_062730|||http://purl.uniprot.org/annotation/VAR_062731|||http://purl.uniprot.org/annotation/VAR_062732|||http://purl.uniprot.org/annotation/VAR_062733|||http://purl.uniprot.org/annotation/VAR_062734|||http://purl.uniprot.org/annotation/VAR_062735|||http://purl.uniprot.org/annotation/VAR_062736|||http://purl.uniprot.org/annotation/VAR_062737|||http://purl.uniprot.org/annotation/VAR_062738|||http://purl.uniprot.org/annotation/VAR_062739|||http://purl.uniprot.org/annotation/VAR_062740|||http://purl.uniprot.org/annotation/VAR_062741|||http://purl.uniprot.org/annotation/VAR_062742|||http://purl.uniprot.org/annotation/VAR_062743|||http://purl.uniprot.org/annotation/VAR_062744|||http://purl.uniprot.org/annotation/VAR_062745|||http://purl.uniprot.org/annotation/VAR_062746|||http://purl.uniprot.org/annotation/VAR_062747|||http://purl.uniprot.org/annotation/VAR_062748|||http://purl.uniprot.org/annotation/VAR_062749|||http://purl.uniprot.org/annotation/VAR_062750|||http://purl.uniprot.org/annotation/VAR_062751|||http://purl.uniprot.org/annotation/VAR_062752|||http://purl.uniprot.org/annotation/VAR_062753|||http://purl.uniprot.org/annotation/VAR_062754|||http://purl.uniprot.org/annotation/VAR_062755|||http://purl.uniprot.org/annotation/VAR_062756|||http://purl.uniprot.org/annotation/VAR_062757
http://togogenome.org/gene/9606:OR5H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW79|||http://purl.uniprot.org/uniprot/A6NKK0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310867|||http://purl.uniprot.org/annotation/VAR_037089|||http://purl.uniprot.org/annotation/VAR_037091|||http://purl.uniprot.org/annotation/VAR_037092|||http://purl.uniprot.org/annotation/VAR_037093
http://togogenome.org/gene/9606:PTRH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y79                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site                                                                                  ^@                                                                                  Chain|||Mutagenesis Site                                                                                  ^@                                                                                  Abolished peptidyl-tRNA activity.|||Peptidyl-tRNA hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240441
http://togogenome.org/gene/9606:HSD17B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37058                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase type 3|||Almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.|||Has 70% of wild-type testosterone 17-beta-dehydrogenase (NADP(+)) activity.|||In MPH.|||In MPH; Cambridge-1; complete loss of activity.|||In MPH; Cambridge-2; affects NADPH cofactor binding.|||In MPH; Gaza; ; almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.|||In MPH; almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.|||In MPH; almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity; no effect on protein abundance; no effect on endoplasmic reticulum location.|||In MPH; complete loss of activity.|||In MPH; loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054573|||http://purl.uniprot.org/annotation/VAR_006953|||http://purl.uniprot.org/annotation/VAR_006954|||http://purl.uniprot.org/annotation/VAR_006955|||http://purl.uniprot.org/annotation/VAR_006956|||http://purl.uniprot.org/annotation/VAR_006957|||http://purl.uniprot.org/annotation/VAR_014870|||http://purl.uniprot.org/annotation/VAR_014871|||http://purl.uniprot.org/annotation/VAR_016067|||http://purl.uniprot.org/annotation/VAR_016068|||http://purl.uniprot.org/annotation/VAR_016069|||http://purl.uniprot.org/annotation/VAR_016070|||http://purl.uniprot.org/annotation/VAR_016071|||http://purl.uniprot.org/annotation/VAR_016072|||http://purl.uniprot.org/annotation/VAR_016073|||http://purl.uniprot.org/annotation/VAR_016074|||http://purl.uniprot.org/annotation/VAR_016203|||http://purl.uniprot.org/annotation/VAR_061844|||http://purl.uniprot.org/annotation/VAR_061845|||http://purl.uniprot.org/annotation/VAR_075369|||http://purl.uniprot.org/annotation/VSP_056640
http://togogenome.org/gene/9606:SCAF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT33|||http://purl.uniprot.org/uniprot/B7Z3A4|||http://purl.uniprot.org/uniprot/B7Z876|||http://purl.uniprot.org/uniprot/Q9UPN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||CID|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||SR-related and CTD-associated factor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081780|||http://purl.uniprot.org/annotation/VAR_052220|||http://purl.uniprot.org/annotation/VSP_056149|||http://purl.uniprot.org/annotation/VSP_056150
http://togogenome.org/gene/9606:GNPTG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||DMAP1-binding|||Disordered|||Does not affect localization to Golgi apparatus.|||In MLIIIC.|||In MLIIIC; decreased localization to Golgi apparatus.|||In MLIIIC; loss of localization to Golgi apparatus.|||Interchain|||MRH|||N-acetylglucosamine-1-phosphotransferase subunit gamma|||N-linked (GlcNAc...) asparagine|||Rare variant; found in individuals suffering from stuttering; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019577|||http://purl.uniprot.org/annotation/VAR_070815|||http://purl.uniprot.org/annotation/VAR_070816|||http://purl.uniprot.org/annotation/VAR_073222|||http://purl.uniprot.org/annotation/VAR_073223|||http://purl.uniprot.org/annotation/VAR_073224|||http://purl.uniprot.org/annotation/VAR_077164|||http://purl.uniprot.org/annotation/VAR_077165|||http://purl.uniprot.org/annotation/VAR_077166
http://togogenome.org/gene/9606:ABCB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP78                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ABC-type oligopeptide transporter ABCB9|||Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-100.|||Decreases lysosomal localization. Loss of lysosomal localization; when associated with A-57.|||Decreases lysosomal localization. Loss of lysosomal localization; when assosiated with R-17. Loss of lysosomal localization; when assosiated with K-45 and K-49. Does not affect peptide transport activity; when assosiated with K-45 and K-49. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.|||Decreases lysosomal localization; when associated with N-45.|||Decreases lysosomal localization; when associated with N-49.|||Helical|||Important for the second trafficking step from the Golgi to the endosomal and lysosomal compartments|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Intramolecular salt bridge with Arg-57. Essential for the release from the ER|||Intramolecular salt bridge with Asp-17. Essential for the release from the ER|||Loss of lysosomal localization. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect dimerization. Does not affect peptide transport activity. Decreases interaction with YIF1B.|||Loss of lysosomal localization. Does not affect lysosomal localization; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-57. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with D-100.|||Loss of lysosomal localization. Does not affect lysosomal localization; when associated with R-17. Does not affect interaction between coreABCB9 and TMD0 domains. Does not affect interaction between coreABCB9 and TMD0 domains; when associated with R-17.|||Loss of lysosomal localization; when assosiated with K-45. Loss of lysosomal localization; when assosiated with K-45 and D-100. Does not affect peptide transport activity; when assosiated with K-45 and D-100.|||Loss of lysosomal localization; when assosiated with K-49. Loss of lysosomal localization; when assosiated with K-49 and D-100. Does not affect peptide transport activity; when assosiated with K-49 and D-100.|||Loss of peptide transport activity; whena ssociated with A-545.|||Loss of peptide transport activity; whena ssociated with A-699.|||No effect on lysosomal localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000252|||http://purl.uniprot.org/annotation/VAR_013701|||http://purl.uniprot.org/annotation/VSP_000027|||http://purl.uniprot.org/annotation/VSP_000029|||http://purl.uniprot.org/annotation/VSP_000030|||http://purl.uniprot.org/annotation/VSP_041884|||http://purl.uniprot.org/annotation/VSP_041885|||http://purl.uniprot.org/annotation/VSP_041886|||http://purl.uniprot.org/annotation/VSP_044884
http://togogenome.org/gene/9606:CDKL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76039                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclin-dependent kinase-like 5|||Disordered|||In DEE2.|||In DEE2; affect activity; causes mislocalization of the protein in the cytoplasm.|||In DEE2; affect activity; does not affect the cellular distribution of the protein.|||In DEE2; causes mislocalization of the protein in the cytoplasm.|||In DEE2; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with autism spectrum disorder.|||Probable disease-associated variant found in a patient with infatile spasms.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085826|||http://purl.uniprot.org/annotation/VAR_023560|||http://purl.uniprot.org/annotation/VAR_023561|||http://purl.uniprot.org/annotation/VAR_023562|||http://purl.uniprot.org/annotation/VAR_036578|||http://purl.uniprot.org/annotation/VAR_037635|||http://purl.uniprot.org/annotation/VAR_037636|||http://purl.uniprot.org/annotation/VAR_041997|||http://purl.uniprot.org/annotation/VAR_041998|||http://purl.uniprot.org/annotation/VAR_041999|||http://purl.uniprot.org/annotation/VAR_058022|||http://purl.uniprot.org/annotation/VAR_058023|||http://purl.uniprot.org/annotation/VAR_058024|||http://purl.uniprot.org/annotation/VAR_058025|||http://purl.uniprot.org/annotation/VAR_058026|||http://purl.uniprot.org/annotation/VAR_058027|||http://purl.uniprot.org/annotation/VAR_058028|||http://purl.uniprot.org/annotation/VAR_058029|||http://purl.uniprot.org/annotation/VAR_058030|||http://purl.uniprot.org/annotation/VAR_058031|||http://purl.uniprot.org/annotation/VAR_058032|||http://purl.uniprot.org/annotation/VAR_071103|||http://purl.uniprot.org/annotation/VAR_078219|||http://purl.uniprot.org/annotation/VAR_078625|||http://purl.uniprot.org/annotation/VAR_078626|||http://purl.uniprot.org/annotation/VAR_078627|||http://purl.uniprot.org/annotation/VAR_078628|||http://purl.uniprot.org/annotation/VAR_078629|||http://purl.uniprot.org/annotation/VAR_078630|||http://purl.uniprot.org/annotation/VAR_078712|||http://purl.uniprot.org/annotation/VAR_078713|||http://purl.uniprot.org/annotation/VAR_078714|||http://purl.uniprot.org/annotation/VAR_083796|||http://purl.uniprot.org/annotation/VAR_083797|||http://purl.uniprot.org/annotation/VAR_083798|||http://purl.uniprot.org/annotation/VAR_083799|||http://purl.uniprot.org/annotation/VSP_060755
http://togogenome.org/gene/9606:DERL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZP9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Derlin-2|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219045
http://togogenome.org/gene/9606:ECE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42892                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Cytoplasmic|||Endothelin-converting enzyme 1|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In HCAD.|||In isoform A.|||In isoform C.|||In isoform D.|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Phosphothreonine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078220|||http://purl.uniprot.org/annotation/VAR_011972|||http://purl.uniprot.org/annotation/VAR_026747|||http://purl.uniprot.org/annotation/VSP_005502|||http://purl.uniprot.org/annotation/VSP_005503|||http://purl.uniprot.org/annotation/VSP_005504
http://togogenome.org/gene/9606:EZR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15311                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ezrin|||FERM|||Interaction with SCYL3|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine; by ROCK2 and PKC/PRKCI|||Phosphotyrosine|||Phosphotyrosine; by PDGFR|||[IL]-x-C-x-x-[DE] motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219408|||http://purl.uniprot.org/annotation/VAR_015112|||http://purl.uniprot.org/annotation/VAR_030572|||http://purl.uniprot.org/annotation/VAR_030573
http://togogenome.org/gene/9606:PLEKHG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZR37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PH|||Pleckstrin homology domain-containing family G member 7|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317287|||http://purl.uniprot.org/annotation/VAR_050513|||http://purl.uniprot.org/annotation/VAR_050514|||http://purl.uniprot.org/annotation/VSP_061133|||http://purl.uniprot.org/annotation/VSP_061134|||http://purl.uniprot.org/annotation/VSP_061135|||http://purl.uniprot.org/annotation/VSP_061136
http://togogenome.org/gene/9606:MGMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEE8|||http://purl.uniprot.org/uniprot/P16455                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased reactivity with O6-benzylguanine.|||Decreases activity towards methylated DNA over 1000-fold. No effect on reactivity with O6-benzylguanine.|||Decreases activity towards methylated DNA over 1000-fold. Slightly reduced reactivity with O6-benzylguanine.|||Loss of DNA repair activity.|||Loss of DNA repair activity. Slightly reduced reactivity with O6-benzylguanine.|||Methylated-DNA--protein-cysteine methyltransferase|||Methylated-DNA-[protein]-cysteine S-methyltransferase DNA binding|||Methylguanine DNA methyltransferase ribonuclease-like|||Nucleophile; methyl group acceptor|||Phosphoserine|||Reduced DNA repair activity. Decreased reactivity with O6-benzylguanine.|||Slightly reduced DNA repair activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139359|||http://purl.uniprot.org/annotation/VAR_014750|||http://purl.uniprot.org/annotation/VAR_014751|||http://purl.uniprot.org/annotation/VAR_014752|||http://purl.uniprot.org/annotation/VAR_014753|||http://purl.uniprot.org/annotation/VAR_014754|||http://purl.uniprot.org/annotation/VAR_014755|||http://purl.uniprot.org/annotation/VAR_020354|||http://purl.uniprot.org/annotation/VAR_029112|||http://purl.uniprot.org/annotation/VAR_056129|||http://purl.uniprot.org/annotation/VAR_056130
http://togogenome.org/gene/9606:TAS2R7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082220|||http://purl.uniprot.org/annotation/VAR_021852|||http://purl.uniprot.org/annotation/VAR_024185|||http://purl.uniprot.org/annotation/VAR_062084
http://togogenome.org/gene/9606:SPRR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35326                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA tandem repeats of P-K-C-P-[EQ]-P-C-P-P|||Disordered|||Small proline-rich protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150008
http://togogenome.org/gene/9606:XPNPEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43895                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated alanine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Xaa-Pro aminopeptidase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026829|||http://purl.uniprot.org/annotation/PRO_0000026830|||http://purl.uniprot.org/annotation/VAR_071310|||http://purl.uniprot.org/annotation/VAR_071311|||http://purl.uniprot.org/annotation/VAR_071312
http://togogenome.org/gene/9606:OR5B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVH3|||http://purl.uniprot.org/uniprot/Q8NH48                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150586|||http://purl.uniprot.org/annotation/VAR_053183|||http://purl.uniprot.org/annotation/VAR_053184|||http://purl.uniprot.org/annotation/VAR_053185|||http://purl.uniprot.org/annotation/VAR_053186|||http://purl.uniprot.org/annotation/VAR_053187|||http://purl.uniprot.org/annotation/VAR_053188|||http://purl.uniprot.org/annotation/VAR_053189|||http://purl.uniprot.org/annotation/VAR_053190
http://togogenome.org/gene/9606:SOX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35712                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||In TOLCAS.|||In TOLCAS; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-404.|||Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-417.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor SOX-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048729|||http://purl.uniprot.org/annotation/VAR_084739|||http://purl.uniprot.org/annotation/VAR_084740|||http://purl.uniprot.org/annotation/VAR_084741|||http://purl.uniprot.org/annotation/VAR_084742|||http://purl.uniprot.org/annotation/VAR_084743|||http://purl.uniprot.org/annotation/VAR_084744|||http://purl.uniprot.org/annotation/VAR_084745|||http://purl.uniprot.org/annotation/VAR_084746|||http://purl.uniprot.org/annotation/VSP_039693|||http://purl.uniprot.org/annotation/VSP_039694|||http://purl.uniprot.org/annotation/VSP_039695|||http://purl.uniprot.org/annotation/VSP_039696
http://togogenome.org/gene/9606:CRTC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53ET0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT6|||CREB-regulated transcription coactivator 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-171.|||Loss of cAMP- and calcium-regulated phosphorylation. Greatly reduced interaction with 14-3-3 proteins. Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins; when associated with A-274.|||N-acetylalanine|||No effect on cAMP- and calcium-regulated phosphorylation.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by AMPK, MARK2, SIK1 and SIK2|||Phosphoserine; by MARK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduced cAMP- and calcium-regulated phosphorylation.|||Removed|||Required for ubiquitination and degradation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318528|||http://purl.uniprot.org/annotation/VAR_038756|||http://purl.uniprot.org/annotation/VAR_038757
http://togogenome.org/gene/9606:PCDHA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Polar residues|||Protocadherin alpha-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003908|||http://purl.uniprot.org/annotation/VSP_000697|||http://purl.uniprot.org/annotation/VSP_000698
http://togogenome.org/gene/9606:CATSPER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W9H2|||http://purl.uniprot.org/uniprot/Q96P56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cation channel sperm-associated protein 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Pore-forming|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Ion transport|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295676|||http://purl.uniprot.org/annotation/VAR_033307|||http://purl.uniprot.org/annotation/VAR_033308|||http://purl.uniprot.org/annotation/VSP_026973|||http://purl.uniprot.org/annotation/VSP_026974|||http://purl.uniprot.org/annotation/VSP_026975|||http://purl.uniprot.org/annotation/VSP_026976|||http://purl.uniprot.org/annotation/VSP_026977
http://togogenome.org/gene/9606:TNMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2S6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BRICHOS|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Tenomodulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144308|||http://purl.uniprot.org/annotation/VSP_054949|||http://purl.uniprot.org/annotation/VSP_054950|||http://purl.uniprot.org/annotation/VSP_054951
http://togogenome.org/gene/9606:PUDP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08623                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Proton donor|||Pseudouridine-5'-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000108068|||http://purl.uniprot.org/annotation/VAR_060625|||http://purl.uniprot.org/annotation/VAR_061094|||http://purl.uniprot.org/annotation/VSP_040029|||http://purl.uniprot.org/annotation/VSP_042020|||http://purl.uniprot.org/annotation/VSP_044804
http://togogenome.org/gene/9606:KCNE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5H1P5|||http://purl.uniprot.org/uniprot/Q8WWG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Potassium voltage-gated channel subfamily E member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144292|||http://purl.uniprot.org/annotation/VAR_024411|||http://purl.uniprot.org/annotation/VAR_030620
http://togogenome.org/gene/9606:NFATC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5B2S0|||http://purl.uniprot.org/uniprot/B5B2S1|||http://purl.uniprot.org/uniprot/Q12968                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X SP repeats|||Calcineurin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylthreonine|||Nuclear export signal|||Nuclear factor of activated T-cells, cytoplasmic 3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||RHD|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205180|||http://purl.uniprot.org/annotation/VAR_051784|||http://purl.uniprot.org/annotation/VAR_051785|||http://purl.uniprot.org/annotation/VAR_051786|||http://purl.uniprot.org/annotation/VAR_051787|||http://purl.uniprot.org/annotation/VAR_051788|||http://purl.uniprot.org/annotation/VSP_005598|||http://purl.uniprot.org/annotation/VSP_005599|||http://purl.uniprot.org/annotation/VSP_005600|||http://purl.uniprot.org/annotation/VSP_005601|||http://purl.uniprot.org/annotation/VSP_005602
http://togogenome.org/gene/9606:ATP5F1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30049                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase subunit delta, mitochondrial|||In MC5DN5; no effect on protein abundance; decreased mitochondrial proton-transporting ATP synthase complex assembly; decreased aerobic respiration in patient cells homozygous for the mutation; partial loss of function confirmed by complementation assays.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002661|||http://purl.uniprot.org/annotation/VAR_081452|||http://purl.uniprot.org/annotation/VAR_081453
http://togogenome.org/gene/9606:KNSTRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y448                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SCC; impaired chromatid cohesion.|||In isoform 2.|||In isoform 3.|||Interaction with SPAG5|||Phosphoserine|||Small kinetochore-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274512|||http://purl.uniprot.org/annotation/VAR_030304|||http://purl.uniprot.org/annotation/VAR_030305|||http://purl.uniprot.org/annotation/VAR_030306|||http://purl.uniprot.org/annotation/VAR_071857|||http://purl.uniprot.org/annotation/VSP_041069|||http://purl.uniprot.org/annotation/VSP_041070
http://togogenome.org/gene/9606:ZP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21754                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In OZEMA3; loss of interaction with ZP2.|||In isoform 3.|||In isoform ZP3B.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Polar residues|||Processed zona pellucida sperm-binding protein 3|||Pyrrolidone carboxylic acid|||Removed in mature form|||ZP|||Zona pellucida sperm-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041709|||http://purl.uniprot.org/annotation/PRO_0000041710|||http://purl.uniprot.org/annotation/PRO_0000304569|||http://purl.uniprot.org/annotation/VAR_058011|||http://purl.uniprot.org/annotation/VAR_058012|||http://purl.uniprot.org/annotation/VAR_058013|||http://purl.uniprot.org/annotation/VAR_079712|||http://purl.uniprot.org/annotation/VSP_006949|||http://purl.uniprot.org/annotation/VSP_006950|||http://purl.uniprot.org/annotation/VSP_037556
http://togogenome.org/gene/9606:CCL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99616                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 13, long chain|||C-C motif chemokine 13, medium chain|||C-C motif chemokine 13, short chain|||Pyrrolidone carboxylic acid; in short chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005201|||http://purl.uniprot.org/annotation/PRO_0000005202|||http://purl.uniprot.org/annotation/PRO_0000005203|||http://purl.uniprot.org/annotation/VAR_024169|||http://purl.uniprot.org/annotation/VAR_048706
http://togogenome.org/gene/9606:TCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20061                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Flexible linker|||Globular C-terminal beta domain|||Globular N-terminal alpha domain|||N-linked (GlcNAc...) asparagine|||Transcobalamin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005561|||http://purl.uniprot.org/annotation/VAR_031923|||http://purl.uniprot.org/annotation/VAR_031924
http://togogenome.org/gene/9606:CIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14578                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||CNH|||Citron Rho-interacting kinase|||Disordered|||In MCPH17; impairs kinase activity; exhibits abnormal mitotic cytokinesis; exhibits multipolar spindles; increases the neurons apoptotic process.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with Rho/Rac|||N-acetylmethionine|||N6-acetyllysine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085908|||http://purl.uniprot.org/annotation/VAR_040417|||http://purl.uniprot.org/annotation/VAR_040418|||http://purl.uniprot.org/annotation/VAR_040419|||http://purl.uniprot.org/annotation/VAR_077442|||http://purl.uniprot.org/annotation/VAR_077443|||http://purl.uniprot.org/annotation/VAR_077444|||http://purl.uniprot.org/annotation/VSP_012434|||http://purl.uniprot.org/annotation/VSP_012435|||http://purl.uniprot.org/annotation/VSP_014507|||http://purl.uniprot.org/annotation/VSP_014508|||http://purl.uniprot.org/annotation/VSP_014509|||http://purl.uniprot.org/annotation/VSP_043301
http://togogenome.org/gene/9606:INHBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1W7|||http://purl.uniprot.org/uniprot/P08476                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with early-onset epithelial ovarian tumor; alters the ratio of secreted activins and ihibins; uncertain pathological significance.|||Found in a patient with early-onset epithelial ovarian tumor; uncertain pathological significance.|||Inhibin beta A chain|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033708|||http://purl.uniprot.org/annotation/PRO_0000033709|||http://purl.uniprot.org/annotation/PRO_5014296864|||http://purl.uniprot.org/annotation/VAR_052566|||http://purl.uniprot.org/annotation/VAR_072640|||http://purl.uniprot.org/annotation/VAR_072641
http://togogenome.org/gene/9606:KCNE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ90                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Found in patients with atrial fibrillation; unknown pathological significance; loss of its inhibitory effects on KCNQ1.|||Found in patients with ventricular fibrillation; unknown pathological significance; loss of its inhibitory effects on KCNQ1.|||Helical|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E regulatory beta subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144294|||http://purl.uniprot.org/annotation/VAR_034048|||http://purl.uniprot.org/annotation/VAR_053037|||http://purl.uniprot.org/annotation/VAR_072679|||http://purl.uniprot.org/annotation/VAR_072680
http://togogenome.org/gene/9606:IFI44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCB0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interferon-induced protein 44|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084165|||http://purl.uniprot.org/annotation/VAR_054647|||http://purl.uniprot.org/annotation/VSP_057031|||http://purl.uniprot.org/annotation/VSP_057032
http://togogenome.org/gene/9606:MAPK11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15759                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||Inactivation.|||Mitogen-activated protein kinase 11|||Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K6|||Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K6|||Phosphotyrosine; by ZAP70|||Protein kinase|||Proton acceptor|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186280|||http://purl.uniprot.org/annotation/VAR_025176|||http://purl.uniprot.org/annotation/VAR_042264|||http://purl.uniprot.org/annotation/VSP_055221|||http://purl.uniprot.org/annotation/VSP_055222|||http://purl.uniprot.org/annotation/VSP_055223
http://togogenome.org/gene/9606:CNDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KN2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-Ala-His dipeptidase|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026809|||http://purl.uniprot.org/annotation/VAR_027147|||http://purl.uniprot.org/annotation/VAR_027148|||http://purl.uniprot.org/annotation/VAR_027149
http://togogenome.org/gene/9606:RAP2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3L5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Ras-related protein Rap-2c|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030221|||http://purl.uniprot.org/annotation/PRO_0000030222
http://togogenome.org/gene/9606:SDR42E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KQB5                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||NAD-dependent epimerase/dehydratase|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:AFAP1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2Q0|||http://purl.uniprot.org/uniprot/Q8N4X5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin filament-associated protein 1-like 2|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphotyrosine|||Reduced interaction with SRC.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050805|||http://purl.uniprot.org/annotation/VAR_050505|||http://purl.uniprot.org/annotation/VAR_050506|||http://purl.uniprot.org/annotation/VAR_050507|||http://purl.uniprot.org/annotation/VAR_054214|||http://purl.uniprot.org/annotation/VSP_014254|||http://purl.uniprot.org/annotation/VSP_014255|||http://purl.uniprot.org/annotation/VSP_014256|||http://purl.uniprot.org/annotation/VSP_036211
http://togogenome.org/gene/9606:LHX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2C1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075789
http://togogenome.org/gene/9606:PAQR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6TCH7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Golgi targeting|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Progestin and adipoQ receptor family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218846|||http://purl.uniprot.org/annotation/VSP_011477|||http://purl.uniprot.org/annotation/VSP_011478|||http://purl.uniprot.org/annotation/VSP_011479|||http://purl.uniprot.org/annotation/VSP_011480
http://togogenome.org/gene/9606:LEUTX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZ59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Abolished catalytic activity; when assiociated with Ile-54-Thr, restores wild-type transcriptional activity.|||Disordered|||Homeobox|||In isoform 2.|||Increased transcriptional activity; when associated with Ala-61-Val, restores wild-type transcriptional activity.|||LEUTX region|||Paired-like homeodomain transcription factor LEUTX|||Polar residues|||Required for binding to the 5'-TAATCC-3' sequence                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343891|||http://purl.uniprot.org/annotation/VSP_060567
http://togogenome.org/gene/9606:TRIM69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YL66|||http://purl.uniprot.org/uniprot/Q86WT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM69|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Loss of E3 ubiquitin-protein ligase activity; when associated with A-61.|||Loss of E3 ubiquitin-protein ligase activity; when associated with A-64.|||Loss of antiviral activity; able to form dimers but not higher-order multimers.|||Loss of antiviral activity; able to form dimers but not higher-order multimers; when associated with A-91.|||Loss of antiviral activity; able to form dimers but not higher-order multimers; when associated with A-96.|||Necessary for nuclear localization|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278236|||http://purl.uniprot.org/annotation/VAR_030704|||http://purl.uniprot.org/annotation/VAR_057226|||http://purl.uniprot.org/annotation/VAR_057227|||http://purl.uniprot.org/annotation/VAR_057228|||http://purl.uniprot.org/annotation/VAR_057229|||http://purl.uniprot.org/annotation/VAR_057230|||http://purl.uniprot.org/annotation/VSP_023200|||http://purl.uniprot.org/annotation/VSP_023201|||http://purl.uniprot.org/annotation/VSP_023202
http://togogenome.org/gene/9606:CASP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VVS7|||http://purl.uniprot.org/uniprot/P55211                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-riboxanated arginine|||Abolished ADP-riboxanation by C.violaceum CopC.|||CARD|||Caspase family p10|||Caspase family p20|||Caspase-9 subunit p10|||Caspase-9 subunit p35|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits tyrosine phosphorylation. Reduces caspase-9 subunit p35 formation in response to genotoxic stress. Attenuates ABL1/c-Abl-mediated caspase-3 activation, DNA fragmentation and UV irradiation-induced apoptosis.|||Phosphoserine|||Phosphothreonine; by MAPK1|||Phosphotyrosine; by ABL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004640|||http://purl.uniprot.org/annotation/PRO_0000004641|||http://purl.uniprot.org/annotation/PRO_0000004642|||http://purl.uniprot.org/annotation/PRO_0000004643|||http://purl.uniprot.org/annotation/VAR_015415|||http://purl.uniprot.org/annotation/VAR_015416|||http://purl.uniprot.org/annotation/VAR_015417|||http://purl.uniprot.org/annotation/VAR_015418|||http://purl.uniprot.org/annotation/VAR_015419|||http://purl.uniprot.org/annotation/VAR_015420|||http://purl.uniprot.org/annotation/VAR_015421|||http://purl.uniprot.org/annotation/VAR_016131|||http://purl.uniprot.org/annotation/VAR_016132|||http://purl.uniprot.org/annotation/VAR_022053|||http://purl.uniprot.org/annotation/VAR_059198|||http://purl.uniprot.org/annotation/VSP_000818|||http://purl.uniprot.org/annotation/VSP_043910|||http://purl.uniprot.org/annotation/VSP_043911|||http://purl.uniprot.org/annotation/VSP_044256
http://togogenome.org/gene/9606:ALG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6U8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,2-mannosyltransferase ALG9|||Breakpoint for translocation|||Cytoplasmic|||Disordered|||Helical|||In CDG1L; impairs activity.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215787|||http://purl.uniprot.org/annotation/VAR_023410|||http://purl.uniprot.org/annotation/VAR_023411|||http://purl.uniprot.org/annotation/VAR_023412|||http://purl.uniprot.org/annotation/VAR_023413|||http://purl.uniprot.org/annotation/VAR_049221|||http://purl.uniprot.org/annotation/VAR_049222|||http://purl.uniprot.org/annotation/VAR_049223|||http://purl.uniprot.org/annotation/VSP_015434|||http://purl.uniprot.org/annotation/VSP_015435
http://togogenome.org/gene/9606:ATP5MJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56378                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ATP synthase subunit ATP5MJ, mitochondrial|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064393|||http://purl.uniprot.org/annotation/VAR_014526|||http://purl.uniprot.org/annotation/VSP_047043
http://togogenome.org/gene/9606:SMARCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58EY4|||http://purl.uniprot.org/uniprot/Q92922                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||BRCT; C-terminus|||BRCT; N-terminus|||Basic and acidic residues|||Chromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In HYC5; associated with disease susceptibility.|||MarR-like|||MarR-like, BRCT and chromo domains module|||Myb-like|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||SANT|||SWI/SNF complex subunit SMARCC1|||SWIRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197115|||http://purl.uniprot.org/annotation/VAR_020883|||http://purl.uniprot.org/annotation/VAR_083428|||http://purl.uniprot.org/annotation/VAR_083429|||http://purl.uniprot.org/annotation/VAR_088111|||http://purl.uniprot.org/annotation/VAR_088112
http://togogenome.org/gene/9606:CBLL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7E2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||E3 ubiquitin-protein ligase CBLL2|||HYB domain|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056316|||http://purl.uniprot.org/annotation/VAR_030340|||http://purl.uniprot.org/annotation/VAR_030341
http://togogenome.org/gene/9606:HSPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZL4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||Disordered|||Hsp70-binding protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084035|||http://purl.uniprot.org/annotation/VAR_023645|||http://purl.uniprot.org/annotation/VAR_080621|||http://purl.uniprot.org/annotation/VSP_015945|||http://purl.uniprot.org/annotation/VSP_053681|||http://purl.uniprot.org/annotation/VSP_053682
http://togogenome.org/gene/9606:DPY19L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2PZI1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Probable C-mannosyltransferase DPY19L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311877|||http://purl.uniprot.org/annotation/VAR_037332|||http://purl.uniprot.org/annotation/VSP_029628
http://togogenome.org/gene/9606:FSHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1D5RMN4|||http://purl.uniprot.org/uniprot/P23945                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activating mutation resulting in 1.5-fold increase in basal cAMP production compared to the wild-type receptor.|||Associated with longer menstrual cycles.|||Cytoplasmic|||Extracellular|||Follicle-stimulating hormone receptor|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In ODG1.|||In ODG1; FSH binding is barely detectable; impaired targeting to the cell membrane; adenylate cyclase stimulation by FSH is 4 +-2% residual activity.|||In ODG1; alters signal transduction of the receptor; adenylate cyclase stimulation by FSH is 24 +-4% residual activity.|||In ODG1; binds FSH with a similar affinity than the wild-type receptor; adenylate cyclase stimulation by FSH is 12 +-3% residual activity.|||In ODG1; impairs cell surface expression.|||In ODG1; totally impairs adenylate cyclase stimulation in vitro; alters the cell surface targeting of the receptor which remains trapped intracellularly.|||In ODG1; very frequent in the Finnish population.|||In OHSS.|||In OHSS; decreases cell surface expression; no effect on hormone binding; increases levels of internalized hormone receptor complex; cAMP levels are similar to basal levels even at high doses of FSH stimulation indicating reduced signaling.|||In OHSS; displays increase in affinity and sensitivity toward hCG and does not show any constitutive activity nor promiscuous activation by TSH.|||In OHSS; displays promiscuous activation by both hCG and TSH together with detectable constitutive activity.|||In OHSS; increase of receptor sensitivity to both hCG and TSH together with an increase in basal activity.|||In OHSS; increases cell surface expression; no effect on hormone binding; increases signaling activity.|||In OHSS; inhibits activation of PI3K/AKT signaling pathway; reduces cAMP production; no effect on ERK1/2 signaling pathway activation.|||In isoform 3.|||In isoform 4.|||In isoform Short.|||In ovarian sex cord tumor; loss of function.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||No change in intracellular cAMP accumulation.|||Reduces intracellular cAMP accumulation.|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012771|||http://purl.uniprot.org/annotation/PRO_5008811855|||http://purl.uniprot.org/annotation/VAR_013903|||http://purl.uniprot.org/annotation/VAR_013904|||http://purl.uniprot.org/annotation/VAR_013905|||http://purl.uniprot.org/annotation/VAR_017244|||http://purl.uniprot.org/annotation/VAR_017245|||http://purl.uniprot.org/annotation/VAR_018045|||http://purl.uniprot.org/annotation/VAR_018046|||http://purl.uniprot.org/annotation/VAR_018047|||http://purl.uniprot.org/annotation/VAR_018048|||http://purl.uniprot.org/annotation/VAR_018049|||http://purl.uniprot.org/annotation/VAR_039279|||http://purl.uniprot.org/annotation/VAR_039280|||http://purl.uniprot.org/annotation/VAR_039281|||http://purl.uniprot.org/annotation/VAR_039282|||http://purl.uniprot.org/annotation/VAR_039283|||http://purl.uniprot.org/annotation/VAR_039284|||http://purl.uniprot.org/annotation/VAR_039285|||http://purl.uniprot.org/annotation/VAR_039286|||http://purl.uniprot.org/annotation/VAR_074535|||http://purl.uniprot.org/annotation/VAR_074536|||http://purl.uniprot.org/annotation/VAR_074537|||http://purl.uniprot.org/annotation/VSP_001953|||http://purl.uniprot.org/annotation/VSP_043181|||http://purl.uniprot.org/annotation/VSP_053411
http://togogenome.org/gene/9606:PPFIBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKA2|||http://purl.uniprot.org/uniprot/Q8ND30                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Liprin-beta-2|||Phosphoserine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191036|||http://purl.uniprot.org/annotation/VAR_049999|||http://purl.uniprot.org/annotation/VSP_047382|||http://purl.uniprot.org/annotation/VSP_047383|||http://purl.uniprot.org/annotation/VSP_047384|||http://purl.uniprot.org/annotation/VSP_047385
http://togogenome.org/gene/9606:MRTFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FUJ8|||http://purl.uniprot.org/uniprot/Q969V6|||http://purl.uniprot.org/uniprot/W0Z7M9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form RBM15-MRTFA|||Disordered|||In IMD66; probable loss-of-function; patient's dendritic cells are morphologically distinct from control dendritic cells and show reduced spreading on fibronectin-coated coverslips, a marked reduction in total F-actin staining and a complete absence of podosomes, a similar phenotype to that of THP1 cells in which MRTFA was silenced.|||Intervening spacer sequence 1|||Intervening spacer sequence 2|||Mediates interaction with SCAI and ACTB|||Myocardin-related transcription factor A|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RPEL|||RPEL 1|||RPEL 2|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126625|||http://purl.uniprot.org/annotation/VAR_021409|||http://purl.uniprot.org/annotation/VAR_084011
http://togogenome.org/gene/9606:TMEFF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Kazal-like 1|||Kazal-like 2|||Polar residues|||Tomoregulin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286056|||http://purl.uniprot.org/annotation/VAR_032060|||http://purl.uniprot.org/annotation/VSP_024959
http://togogenome.org/gene/9606:TTC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92623                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Pro residues|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 9A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106390|||http://purl.uniprot.org/annotation/VAR_060330
http://togogenome.org/gene/9606:C1orf174                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||UPF0688 protein C1orf174                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294244|||http://purl.uniprot.org/annotation/VAR_033152|||http://purl.uniprot.org/annotation/VAR_033153|||http://purl.uniprot.org/annotation/VAR_057829
http://togogenome.org/gene/9606:COA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYJ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cytochrome c oxidase assembly factor 4 homolog, mitochondrial|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314908|||http://purl.uniprot.org/annotation/VSP_030428
http://togogenome.org/gene/9606:CD151                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48509|||http://purl.uniprot.org/uniprot/Q6ZNZ0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD151 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219230|||http://purl.uniprot.org/annotation/VAR_012490|||http://purl.uniprot.org/annotation/VAR_012491|||http://purl.uniprot.org/annotation/VAR_021153|||http://purl.uniprot.org/annotation/VAR_025098
http://togogenome.org/gene/9606:WNT3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56704                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates WLS binding.|||Cleavage; by TIKI1 and TIKI2|||Complete loss of palmitoleoylation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on palmitoleoylation and secretion; the threonine can functionally replace the serine.|||No signaling activity despite the presence of significant amounts of secreted monomeric Wnt3a, exhibits dominant negative properties; when associated with A-334.|||No signaling activity despite the presence of significant amounts of secreted monomeric Wnt3a, exhibits dominant negative properties; when associated with A-335.|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-3a|||Strongly reduced ability to stimulate Wnt-responsive reporters; when associated with Q-298.|||Strongly reduced ability to stimulate Wnt-responsive reporters; when associated with Q-87.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041418|||http://purl.uniprot.org/annotation/VSP_046558
http://togogenome.org/gene/9606:RAX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IS3                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In ARMD6; associated with disease susceptibility; increased transactivation and DNA-binding activity.|||In CORD11; unknown pathological significance; decreased interaction with CRX and increased transactivation activity.|||In CORD11; unknown pathological significance; decreased interaction with CRX and transactivation activity.|||In RP95.|||In RP95; unknown pathological significance.|||Retina and anterior neural fold homeobox protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285048|||http://purl.uniprot.org/annotation/VAR_031907|||http://purl.uniprot.org/annotation/VAR_031908|||http://purl.uniprot.org/annotation/VAR_031909|||http://purl.uniprot.org/annotation/VAR_087740|||http://purl.uniprot.org/annotation/VAR_087741
http://togogenome.org/gene/9606:UACA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Uveal autoantigen with coiled-coil domains and ankyrin repeats                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231650|||http://purl.uniprot.org/annotation/VAR_048313|||http://purl.uniprot.org/annotation/VSP_047199
http://togogenome.org/gene/9606:CA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1Q1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 13|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077440|||http://purl.uniprot.org/annotation/VAR_059207
http://togogenome.org/gene/9606:FARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95363                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  FDX-ACB|||In COXPD14; results in a 4-fold decrease in the catalytic efficiency of amino acid activation mainly due to a decreased affinity for ATP; does not affect Phe binding; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity.|||In COXPD14; results in a decrease in affinity for Phe causing a decrease in aminoacylation activity; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity.|||In COXPD14; results in decreased affinity for tRNA causing a decrease in the catalytic efficiency for tRNA charging; does not affect ATP or Phe binding.|||In SPG77; resulted in severely impaired phenylalanine-tRNA ligase activity.|||Mitochondrion|||N6-acetyllysine|||Phenylalanine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035813|||http://purl.uniprot.org/annotation/VAR_052642|||http://purl.uniprot.org/annotation/VAR_052643|||http://purl.uniprot.org/annotation/VAR_069487|||http://purl.uniprot.org/annotation/VAR_069488|||http://purl.uniprot.org/annotation/VAR_069489|||http://purl.uniprot.org/annotation/VAR_077044
http://togogenome.org/gene/9606:CDK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3F9|||http://purl.uniprot.org/uniprot/D6R9G1|||http://purl.uniprot.org/uniprot/D6RFL0|||http://purl.uniprot.org/uniprot/P50613                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase 7|||Enhanced capacity to bind ATP analogs.|||N-acetylalanine|||No effect on interaction with HINT1.|||No mitotic repression of transcriptional activity of the reconstituted TFIIH complex.|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Phosphothreonine; by CDK2|||Protein kinase|||Proton acceptor|||Removed|||Total loss of activity.|||Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085791|||http://purl.uniprot.org/annotation/VAR_023118|||http://purl.uniprot.org/annotation/VAR_023119
http://togogenome.org/gene/9606:TMCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z591|||http://purl.uniprot.org/uniprot/Q9UM00                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the calcium channel activity.|||Calcium load-activated calcium channel|||Cytoplasmic|||Disordered|||Helical|||In CFSMR1.|||In isoform 2.|||In isoform 3.|||Lumenal|||Phosphoserine|||Retains some of the calcium channel activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244076|||http://purl.uniprot.org/annotation/VAR_076652|||http://purl.uniprot.org/annotation/VAR_076653|||http://purl.uniprot.org/annotation/VSP_019505|||http://purl.uniprot.org/annotation/VSP_060086
http://togogenome.org/gene/9606:NHP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX24                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||H/ACA ribonucleoprotein complex subunit 2|||In DKCB2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136763|||http://purl.uniprot.org/annotation/VAR_065870|||http://purl.uniprot.org/annotation/VAR_065871|||http://purl.uniprot.org/annotation/VAR_065872
http://togogenome.org/gene/9606:COMMD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J287|||http://purl.uniprot.org/uniprot/Q9H0A8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 4|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077393|||http://purl.uniprot.org/annotation/VSP_011394|||http://purl.uniprot.org/annotation/VSP_055664
http://togogenome.org/gene/9606:KATNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In LIS6.|||In LIS6; causes reduced interaction with KATNA1 and NDEL1.|||Interaction with KATNA1 and NDEL1|||Interaction with PAFAH1B1|||Interaction with centrosomes|||Interaction with dynein|||Katanin p80 WD40 repeat-containing subunit B1|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051049|||http://purl.uniprot.org/annotation/VAR_062099|||http://purl.uniprot.org/annotation/VAR_073319|||http://purl.uniprot.org/annotation/VAR_073320|||http://purl.uniprot.org/annotation/VAR_073321
http://togogenome.org/gene/9606:MAP6D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9H5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-10 and C-11.|||Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-5 and C-10.|||Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-5 and C-11.|||MAP6 domain-containing protein 1|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271915
http://togogenome.org/gene/9606:RTP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59025                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||Receptor-transporting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181988|||http://purl.uniprot.org/annotation/VAR_036122|||http://purl.uniprot.org/annotation/VAR_053729|||http://purl.uniprot.org/annotation/VAR_053730
http://togogenome.org/gene/9606:ANKRD28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15084                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 26|||ANK 27|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Marked decrease in phosphorylation. Increased PPP1C-binding. No effect on HNRPK-binding.|||Phosphoserine|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066919|||http://purl.uniprot.org/annotation/VSP_012433|||http://purl.uniprot.org/annotation/VSP_041013|||http://purl.uniprot.org/annotation/VSP_041014
http://togogenome.org/gene/9606:SAP30BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||SAP30-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245791|||http://purl.uniprot.org/annotation/VSP_052091
http://togogenome.org/gene/9606:MS4A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZW8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Membrane-spanning 4-domains subfamily A member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158643|||http://purl.uniprot.org/annotation/VAR_053520|||http://purl.uniprot.org/annotation/VAR_053521|||http://purl.uniprot.org/annotation/VAR_053522|||http://purl.uniprot.org/annotation/VSP_042009
http://togogenome.org/gene/9606:ZNF141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RIY0|||http://purl.uniprot.org/uniprot/Q15928|||http://purl.uniprot.org/uniprot/Q4W5N2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In PAPA6.|||KRAB|||Zinc finger protein 141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047424|||http://purl.uniprot.org/annotation/VAR_012026|||http://purl.uniprot.org/annotation/VAR_012027|||http://purl.uniprot.org/annotation/VAR_019973|||http://purl.uniprot.org/annotation/VAR_069637
http://togogenome.org/gene/9606:ILDR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71H61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Ig-like V-type|||Immunoglobulin-like domain-containing receptor 2|||Lumenal|||Omega-N-methylarginine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278607|||http://purl.uniprot.org/annotation/VAR_049948
http://togogenome.org/gene/9606:PSMG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969U7|||http://purl.uniprot.org/uniprot/Q9P1R6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In PRAAS4; unknown pathological significance.|||In isoform 2.|||Phosphothreonine|||Proteasome assembly chaperone 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322552|||http://purl.uniprot.org/annotation/VAR_085403|||http://purl.uniprot.org/annotation/VSP_055721
http://togogenome.org/gene/9606:LCE1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T751                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235326|||http://purl.uniprot.org/annotation/VAR_053481
http://togogenome.org/gene/9606:LIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15018                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Leukemia inhibitory factor|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017715|||http://purl.uniprot.org/annotation/VSP_045551|||http://purl.uniprot.org/annotation/VSP_045552
http://togogenome.org/gene/9606:BLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51451|||http://purl.uniprot.org/uniprot/Q05D26                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Associated with MODY11; reduces the enhancing effect of BLK on insulin secretion; reduces the inducing effect of BLK on the expression of PDX1 and NKX6-1; found as somatic mutation in a colorectal adenocarcinoma sample.|||Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Tyrosine-protein kinase Blk                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088061|||http://purl.uniprot.org/annotation/VAR_041672|||http://purl.uniprot.org/annotation/VAR_041673
http://togogenome.org/gene/9606:FOXL2NB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUU3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||FOXL2 neighbor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348439
http://togogenome.org/gene/9606:GNPNAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EK6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glucosamine 6-phosphate N-acetyltransferase|||In RHZDAN.|||N-acetyltransferase|||Reduces affinity for glucosamine-6-phosphate 6-fold.|||Slightly reduced catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074553|||http://purl.uniprot.org/annotation/VAR_086302
http://togogenome.org/gene/9606:ACBD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3P7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  60% reduced ability to interact with the 3A protein of enterovirus D68.|||75% reduced ability to interact with the 3A protein of enterovirus D68.|||80% reduced ability to interact with the 3A protein of enterovirus D68.|||95% reduced ability to interact with the 3A protein of enterovirus D68.|||ACB|||Almost complete loss of Golgi loalization.|||Almost complete loss of PI4KB- and TBC1D22B-binding.|||Charged amino-acid region (CAR)|||Complete loss of interaction with PI4KB.|||Differential effect on PI4KB- and TBC1D22B-binding, with PI4KB-binding being much more affected than TBC1D22B-binding.|||Differential loss of PI4KB- and TBC1D22B-binding, with PI4KB-binding being much more affected than TBC1D22B-binding.|||Disordered|||GOLD|||Golgi resident protein GCP60|||Golgi resident protein GCP60, N-terminally processed|||Loss of PI4KB-, TBC1D22A- and TBC1D22B-binding.|||Loss of interaction with PI4KB.|||Membrane-binding|||N-acetylalanine; in Golgi resident protein GCP60, N-terminally processed|||No effect on PI4KB- and TBC1D22B-binding.|||No effect on PI4KB-, TBC1D22A- and TBC1D22B-binding.|||No effect on interaction with PI4KB but loss of interaction with Kobuviral (Aichi) 3A protein. Loss of ability to sensitize PI4KB activation by Kobuviral (Aichi) 3A protein.|||No loss of interaction with PI4KB.|||Partial loss of PI4KB- and TBC1D22B-binding.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Q domain; Interaction with PI4KB, TBC1D22A and TBC1D22B|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214029|||http://purl.uniprot.org/annotation/PRO_0000436449|||http://purl.uniprot.org/annotation/VAR_019615
http://togogenome.org/gene/9606:PAX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23759                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In CMYP19.|||In CMYP19; loss-of-function variant resulting in a reduced muscle stem cell pool; the protein is not detected in patient muscle.|||In isoform 1 and isoform 2.|||In isoform 2.|||OAR|||PAI subdomain|||Paired|||Paired box protein Pax-7|||RED subdomain|||Sufficient to mediate interaction with PAXBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050194|||http://purl.uniprot.org/annotation/VAR_083265|||http://purl.uniprot.org/annotation/VAR_083266|||http://purl.uniprot.org/annotation/VAR_083267|||http://purl.uniprot.org/annotation/VSP_057678|||http://purl.uniprot.org/annotation/VSP_057679
http://togogenome.org/gene/9606:SLC6A20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP91                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Common variant that contributes to hyperglycinuria and iminoglycinuria in patients carrying variants in SLC36A2, SLC6A19 or SLC6A18; results in SLC6A20 inactivation due to a 8-fold decrease of Vmax.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sodium- and chloride-dependent transporter XTRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214812|||http://purl.uniprot.org/annotation/VAR_021862|||http://purl.uniprot.org/annotation/VAR_052068|||http://purl.uniprot.org/annotation/VSP_050002
http://togogenome.org/gene/9606:PODXL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00592|||http://purl.uniprot.org/uniprot/Q96N83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Podocalyxin|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024754|||http://purl.uniprot.org/annotation/PRO_5004322536|||http://purl.uniprot.org/annotation/VAR_012236|||http://purl.uniprot.org/annotation/VAR_012237|||http://purl.uniprot.org/annotation/VAR_055237|||http://purl.uniprot.org/annotation/VAR_055238|||http://purl.uniprot.org/annotation/VAR_060090|||http://purl.uniprot.org/annotation/VAR_062136|||http://purl.uniprot.org/annotation/VSP_037220
http://togogenome.org/gene/9606:VWCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6|||von Willebrand factor C and EGF domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318580|||http://purl.uniprot.org/annotation/VAR_038782|||http://purl.uniprot.org/annotation/VSP_031230|||http://purl.uniprot.org/annotation/VSP_031231
http://togogenome.org/gene/9606:EPM2AIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L775                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EPM2A-interacting protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086992|||http://purl.uniprot.org/annotation/VAR_050969|||http://purl.uniprot.org/annotation/VAR_050970
http://togogenome.org/gene/9606:ERVMER34-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9K5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endogenous retroviral envelope protein HEMO|||Endogenous retroviral envelope protein HEMO, secreted form|||Extracellular|||Helical|||Introduction of a furin cleavage site, promoting proteolytic cleavage of the protein by furin and release in the extracellular medium.|||N-linked (GlcNAc...) asparagine|||Promotes release in the extracellular medium.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341352|||http://purl.uniprot.org/annotation/PRO_0000443800
http://togogenome.org/gene/9606:ZNF519                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 519                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047637|||http://purl.uniprot.org/annotation/VAR_052854|||http://purl.uniprot.org/annotation/VAR_052855|||http://purl.uniprot.org/annotation/VAR_052856|||http://purl.uniprot.org/annotation/VAR_052857
http://togogenome.org/gene/9606:GUCA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3V9|||http://purl.uniprot.org/uniprot/Q9UMX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Guanylyl cyclase-activating protein 2|||In RP48.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073808|||http://purl.uniprot.org/annotation/VAR_009127|||http://purl.uniprot.org/annotation/VAR_065355
http://togogenome.org/gene/9606:DAAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4D1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes actin-binding.|||Actin-binding|||Basic and acidic residues|||DAD|||Disheveled-associated activator of morphogenesis 1|||Disordered|||FH1|||FH2|||GBD/FH3|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194907|||http://purl.uniprot.org/annotation/VSP_008000|||http://purl.uniprot.org/annotation/VSP_008001|||http://purl.uniprot.org/annotation/VSP_008002|||http://purl.uniprot.org/annotation/VSP_008003
http://togogenome.org/gene/9606:COP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHY2|||http://purl.uniprot.org/uniprot/X5D7N8|||http://purl.uniprot.org/uniprot/X5DNY7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes localization to the nucleus.|||Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-136.|||Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-139.|||Disordered|||E3 ubiquitin-protein ligase COP1|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Interaction with TRIB1|||Loss of MTA1 ubiquitination and degradation; when associated with S-156.|||Loss of MTA1 ubiquitination and degradation; when associated with S-159.|||Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-136. Loss of stabilization by COPS6; when associated with S-136.|||Loss of SFN and MTA1 ubiquitination and degradation; when associated with S-139. Loss of stabilization by COPS6; when associated with S-139.|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||Polar residues|||RING-type|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055879|||http://purl.uniprot.org/annotation/VSP_012024|||http://purl.uniprot.org/annotation/VSP_012025|||http://purl.uniprot.org/annotation/VSP_012026|||http://purl.uniprot.org/annotation/VSP_012027|||http://purl.uniprot.org/annotation/VSP_055894|||http://purl.uniprot.org/annotation/VSP_055895
http://togogenome.org/gene/9606:NRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X845|||http://purl.uniprot.org/uniprot/B3KQU6|||http://purl.uniprot.org/uniprot/Q8IXM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Nuclear|||Nurim|||Perinuclear space                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299395|||http://purl.uniprot.org/annotation/VSP_027627|||http://purl.uniprot.org/annotation/VSP_054311|||http://purl.uniprot.org/annotation/VSP_054312
http://togogenome.org/gene/9606:TTYH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKD1|||http://purl.uniprot.org/uniprot/Q8N3U8|||http://purl.uniprot.org/uniprot/Q9BSA4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Protein tweety homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312246|||http://purl.uniprot.org/annotation/VAR_037460|||http://purl.uniprot.org/annotation/VAR_037461|||http://purl.uniprot.org/annotation/VAR_037462|||http://purl.uniprot.org/annotation/VAR_037463|||http://purl.uniprot.org/annotation/VAR_037464|||http://purl.uniprot.org/annotation/VAR_037465|||http://purl.uniprot.org/annotation/VAR_057791|||http://purl.uniprot.org/annotation/VSP_040567
http://togogenome.org/gene/9606:NOP56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00567                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Nop|||Nucleolar protein 56|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219025|||http://purl.uniprot.org/annotation/VAR_014471|||http://purl.uniprot.org/annotation/VAR_028793|||http://purl.uniprot.org/annotation/VAR_028794
http://togogenome.org/gene/9606:KRTAP9-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||17 X 5 AA repeats of C-C-[RQVSGE]-[SPTQ]-[TASP]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185188|||http://purl.uniprot.org/annotation/VAR_046702|||http://purl.uniprot.org/annotation/VAR_046703
http://togogenome.org/gene/9606:C6orf118                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5N4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C6orf118                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089523|||http://purl.uniprot.org/annotation/VAR_022887|||http://purl.uniprot.org/annotation/VAR_022888|||http://purl.uniprot.org/annotation/VAR_050807|||http://purl.uniprot.org/annotation/VAR_050808|||http://purl.uniprot.org/annotation/VAR_050809|||http://purl.uniprot.org/annotation/VAR_050810
http://togogenome.org/gene/9606:SRCIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0H9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with SNAP25|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SRC kinase signaling inhibitor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072011|||http://purl.uniprot.org/annotation/VSP_059450|||http://purl.uniprot.org/annotation/VSP_059451|||http://purl.uniprot.org/annotation/VSP_059452|||http://purl.uniprot.org/annotation/VSP_059453|||http://purl.uniprot.org/annotation/VSP_059454
http://togogenome.org/gene/9606:CNNM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIV9|||http://purl.uniprot.org/uniprot/B4DKF7|||http://purl.uniprot.org/uniprot/B7Z5S3|||http://purl.uniprot.org/uniprot/Q9NRU3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CBS|||CBS 1|||CBS 2|||CNNM transmembrane|||Disordered|||Helical|||In isoform 2.|||Metal transporter CNNM1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295758|||http://purl.uniprot.org/annotation/VAR_057737|||http://purl.uniprot.org/annotation/VSP_027076
http://togogenome.org/gene/9606:ALAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL9|||http://purl.uniprot.org/uniprot/B7Z3I9|||http://purl.uniprot.org/uniprot/P13716|||http://purl.uniprot.org/uniprot/Q6ZMU0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Allele ALAD*2; ALAD*2 heterozygous or homozygous carriers have significantly higher blood lead levels than ALAD*1 homozygotes when exposed to environmental lead; fully active octamer.|||Delta-aminolevulinic acid dehydratase|||Disordered|||In AHEPP; about 95% octamer; about 40% residual activity.|||In AHEPP; mainly octamer; reduced activity.|||In AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity.|||In AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity.|||In AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity.|||In an asymptomatic patient with ALAD deficiency; also found in a hereditary coproporphyria patient carrying the R-279 mutation in CPOX; hexamer with almost no residual activity.|||In isoform 2.|||N6-succinyllysine|||No effect on catalytic activity; when associated with A-131.|||No effect on catalytic activity; when associated with A-223.|||Phosphoserine|||Polar residues|||Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-124.|||Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-132.|||Reduces enzyme activity about 1000000-fold; when associated with A-124 and A-132.|||Schiff-base intermediate with substrate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140526|||http://purl.uniprot.org/annotation/VAR_003633|||http://purl.uniprot.org/annotation/VAR_003634|||http://purl.uniprot.org/annotation/VAR_003635|||http://purl.uniprot.org/annotation/VAR_003636|||http://purl.uniprot.org/annotation/VAR_003637|||http://purl.uniprot.org/annotation/VAR_020973|||http://purl.uniprot.org/annotation/VAR_020974|||http://purl.uniprot.org/annotation/VSP_037866
http://togogenome.org/gene/9606:IGSF9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7W7|||http://purl.uniprot.org/uniprot/Q9UPX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Protein turtle homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306110|||http://purl.uniprot.org/annotation/VAR_076999|||http://purl.uniprot.org/annotation/VAR_077000|||http://purl.uniprot.org/annotation/VSP_054730
http://togogenome.org/gene/9606:HAX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z565|||http://purl.uniprot.org/uniprot/A0A0S2Z591|||http://purl.uniprot.org/uniprot/O00165                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||HCLS1-associated protein X-1|||In SCN3.|||In SCN3; likely benign variant.|||In SCN3; mild form.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Involved in ATP2A2 binding|||Involved in CASP9 binding|||Involved in GNA13 binding|||Involved in HCLS1 binding|||Involved in PKD2 binding|||Involved in PLN binding|||Mediates interaction with UCP3|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||Required for ITGB6 binding|||Required for localization in mitochondria|||Required for localization in sarcoplasmic reticulum                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083906|||http://purl.uniprot.org/annotation/VAR_062258|||http://purl.uniprot.org/annotation/VAR_062259|||http://purl.uniprot.org/annotation/VAR_062260|||http://purl.uniprot.org/annotation/VAR_062261|||http://purl.uniprot.org/annotation/VAR_064514|||http://purl.uniprot.org/annotation/VAR_064515|||http://purl.uniprot.org/annotation/VSP_038536|||http://purl.uniprot.org/annotation/VSP_038537|||http://purl.uniprot.org/annotation/VSP_038538|||http://purl.uniprot.org/annotation/VSP_038539|||http://purl.uniprot.org/annotation/VSP_038543|||http://purl.uniprot.org/annotation/VSP_038544|||http://purl.uniprot.org/annotation/VSP_038545
http://togogenome.org/gene/9606:OR51A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWD5|||http://purl.uniprot.org/uniprot/Q8NGJ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150742|||http://purl.uniprot.org/annotation/VAR_024138|||http://purl.uniprot.org/annotation/VAR_024139|||http://purl.uniprot.org/annotation/VAR_053305|||http://purl.uniprot.org/annotation/VAR_062075
http://togogenome.org/gene/9606:LALBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YV01|||http://purl.uniprot.org/uniprot/P00709                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-lactalbumin|||C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lactose synthase B protein|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018444|||http://purl.uniprot.org/annotation/PRO_5001752441|||http://purl.uniprot.org/annotation/VAR_024526
http://togogenome.org/gene/9606:PODXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) serine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Podocalyxin-like protein 2|||Polar residues|||Reduced sialylation.|||Remains sulfated. Not sulfated and reduced rolling of Jurkat T-cells by more than 50%; when associated with F-118. The rolling of Jurkat T-cells is reduced by more than 80%; when associated with F-118 and A-124.|||Remains sulfated. Not sulfated and reduced rolling of Jurkat T-cells by more than 50%; when associated with F-97. The rolling of Jurkat T-cells is reduced by more than 80%; when associated with F-97 and A-124.|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252129|||http://purl.uniprot.org/annotation/VAR_053599|||http://purl.uniprot.org/annotation/VSP_020876
http://togogenome.org/gene/9606:PSMD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF2|||http://purl.uniprot.org/uniprot/O00487                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 14|||Abolishes ubiquitin thioesterase activity, leading to prevent maintenance of JMJD2A/KDM4A on chromatin.|||JAMM motif|||MPN|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213952
http://togogenome.org/gene/9606:TCTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1J4|||http://purl.uniprot.org/uniprot/A8MW34|||http://purl.uniprot.org/uniprot/B4DIB9|||http://purl.uniprot.org/uniprot/Q05BR9|||http://purl.uniprot.org/uniprot/Q2MV58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Tectonic|||Tectonic-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229796|||http://purl.uniprot.org/annotation/PRO_5014085093|||http://purl.uniprot.org/annotation/PRO_5030002790|||http://purl.uniprot.org/annotation/VSP_017756|||http://purl.uniprot.org/annotation/VSP_017757|||http://purl.uniprot.org/annotation/VSP_017758|||http://purl.uniprot.org/annotation/VSP_017759|||http://purl.uniprot.org/annotation/VSP_017760|||http://purl.uniprot.org/annotation/VSP_017761|||http://purl.uniprot.org/annotation/VSP_017762|||http://purl.uniprot.org/annotation/VSP_017763
http://togogenome.org/gene/9606:RGL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRX4|||http://purl.uniprot.org/uniprot/Q3MIN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with HRAS, MRAS and RIT1|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Pro residues|||Ral guanine nucleotide dissociation stimulator-like 3|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306799|||http://purl.uniprot.org/annotation/VAR_035298|||http://purl.uniprot.org/annotation/VAR_035299|||http://purl.uniprot.org/annotation/VAR_035300|||http://purl.uniprot.org/annotation/VSP_045369
http://togogenome.org/gene/9606:BCAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSI3|||http://purl.uniprot.org/uniprot/O15382                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Branched-chain-amino-acid aminotransferase, mitochondrial|||In HVLI; reduced catalytic activity.|||In isoform B.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||Reduces activity about 6-fold.|||Slight reduction of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001271|||http://purl.uniprot.org/annotation/VAR_048234|||http://purl.uniprot.org/annotation/VAR_084533|||http://purl.uniprot.org/annotation/VAR_084534|||http://purl.uniprot.org/annotation/VSP_000236
http://togogenome.org/gene/9606:FILIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7B0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Filamin-A-interacting protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234540|||http://purl.uniprot.org/annotation/VAR_050995|||http://purl.uniprot.org/annotation/VSP_018344|||http://purl.uniprot.org/annotation/VSP_018345
http://togogenome.org/gene/9606:OR14I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6ND48                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 14I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310414|||http://purl.uniprot.org/annotation/VAR_037030|||http://purl.uniprot.org/annotation/VAR_037031|||http://purl.uniprot.org/annotation/VAR_037032|||http://purl.uniprot.org/annotation/VAR_062073|||http://purl.uniprot.org/annotation/VAR_062074
http://togogenome.org/gene/9606:GOLGA6L10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI86                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Golgin subfamily A member 6-like protein 10|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342266
http://togogenome.org/gene/9606:POLR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH29|||http://purl.uniprot.org/uniprot/B4DHJ3|||http://purl.uniprot.org/uniprot/C9J2Y9|||http://purl.uniprot.org/uniprot/P30876                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase II subunit RPB2|||DNA-directed RNA polymerase subunit 2 hybrid-binding|||N6-methyllysine|||Phosphoserine|||RNA polymerase Rpb2|||RNA polymerase beta subunit protrusion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048085
http://togogenome.org/gene/9606:CCDC43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MW1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 43|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234500|||http://purl.uniprot.org/annotation/VSP_040750
http://togogenome.org/gene/9606:MED30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HR3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 30|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239406|||http://purl.uniprot.org/annotation/VSP_053904
http://togogenome.org/gene/9606:TEKT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969V4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Tektin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184562|||http://purl.uniprot.org/annotation/VAR_022150|||http://purl.uniprot.org/annotation/VAR_022151|||http://purl.uniprot.org/annotation/VAR_034548
http://togogenome.org/gene/9606:THEM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1Q8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Acyl-coenzyme A thioesterase THEM5|||Proton donor/acceptor|||Reduces enzyme activity. Abolishes enzyme activity; when associated with A-160.|||Strongly reduces enzyme activity. Abolishes enzyme activity; when associated with A-183.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284519|||http://purl.uniprot.org/annotation/VAR_031764|||http://purl.uniprot.org/annotation/VAR_031765|||http://purl.uniprot.org/annotation/VAR_031766
http://togogenome.org/gene/9606:GRAMD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HH9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRAM|||GRAM domain-containing protein 2B|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087577|||http://purl.uniprot.org/annotation/VSP_042883|||http://purl.uniprot.org/annotation/VSP_042884|||http://purl.uniprot.org/annotation/VSP_042885|||http://purl.uniprot.org/annotation/VSP_044298|||http://purl.uniprot.org/annotation/VSP_044299
http://togogenome.org/gene/9606:EGLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZT9|||http://purl.uniprot.org/uniprot/R4SCQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Beta(2)beta(3) 'finger-like' loop|||Disordered|||Egl nine homolog 1|||Fe2OG dioxygenase|||In ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity.|||In ECYT3; marked decrease in enzyme activity.|||In isoform 2.|||In isoform 3.|||Increased protection from polycythemia at high altitude; when associated with E-4.|||Increased protection from polycythemia at high altitude; when associated with S-127.|||Little change in enzyme activity.|||MYND-type|||MYND-type; atypical|||N-acetylalanine|||No effect.|||Phosphoserine|||Reduced C-terminal ODD domain (CODD) hxdroxylation of HIF1A.|||Reduced C-terminal ODD domain (CODD) hydroxylation of HIF1A.|||Reduces enzyme activity by 95%.|||Removed|||Required for nuclear export|||S-nitrosocysteine|||Slight increase in enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206661|||http://purl.uniprot.org/annotation/VAR_027371|||http://purl.uniprot.org/annotation/VAR_045902|||http://purl.uniprot.org/annotation/VAR_071858|||http://purl.uniprot.org/annotation/VAR_071859|||http://purl.uniprot.org/annotation/VSP_007569|||http://purl.uniprot.org/annotation/VSP_042191
http://togogenome.org/gene/9606:PDIA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13087                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Contributes to redox potential value|||Disordered|||Impairs interchain disulfide bridge formation.|||In isoform 2.|||Increases formation of a highly stable disulfide-bonded PDIA2 dimer.|||Interchain|||Lowers pKa of C-terminal Cys of first active site|||Lowers pKa of C-terminal Cys of second active site|||N-linked (GlcNAc...) asparagine|||No effect on interchain disulfide bridge formation.|||Nucleophile|||Prevents secretion from ER|||Protein disulfide-isomerase A2|||Redox-active|||Thioredoxin 1|||Thioredoxin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034222|||http://purl.uniprot.org/annotation/VAR_048087|||http://purl.uniprot.org/annotation/VAR_048088|||http://purl.uniprot.org/annotation/VAR_048089|||http://purl.uniprot.org/annotation/VAR_048090|||http://purl.uniprot.org/annotation/VAR_048091|||http://purl.uniprot.org/annotation/VAR_048092|||http://purl.uniprot.org/annotation/VAR_048093|||http://purl.uniprot.org/annotation/VSP_039292
http://togogenome.org/gene/9606:RAD9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WBX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cell cycle checkpoint control protein RAD9B|||In isoform 1, isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226698|||http://purl.uniprot.org/annotation/VSP_017444|||http://purl.uniprot.org/annotation/VSP_017445|||http://purl.uniprot.org/annotation/VSP_017446
http://togogenome.org/gene/9606:CXCL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10145                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Citrulline|||Cleavage; by MMP9|||Cleavage; by thrombin|||Decreases heparin-binding activity. Impairs heparin-binding activity and leukocyte transendothelial migration; when associated with A-94 and A-95.|||IL-8(5-77)|||IL-8(6-77)|||IL-8(7-77)|||IL-8(8-77)|||IL-8(9-77)|||Impairs heparin-binding activity and leukocyte transendothelial migration; when associated with A-91 and A-94.|||Impairs heparin-binding activity and leukocyte transendothelial migration; when associated with A-91 and A-95.|||Interleukin-8|||MDNCF-a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005126|||http://purl.uniprot.org/annotation/PRO_0000005127|||http://purl.uniprot.org/annotation/PRO_0000005128|||http://purl.uniprot.org/annotation/PRO_0000005129|||http://purl.uniprot.org/annotation/PRO_0000005130|||http://purl.uniprot.org/annotation/PRO_0000005131|||http://purl.uniprot.org/annotation/PRO_0000041948
http://togogenome.org/gene/9606:UQCR11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14957                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 10|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193560
http://togogenome.org/gene/9606:DRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21728                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||D(1A) dopamine receptor|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069373|||http://purl.uniprot.org/annotation/VAR_014670|||http://purl.uniprot.org/annotation/VAR_014671|||http://purl.uniprot.org/annotation/VAR_014672|||http://purl.uniprot.org/annotation/VAR_014673|||http://purl.uniprot.org/annotation/VAR_064577|||http://purl.uniprot.org/annotation/VAR_064578
http://togogenome.org/gene/9606:ZKSCAN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Phosphothreonine|||Requires 2 nucleotide substitutions.|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047524|||http://purl.uniprot.org/annotation/VAR_024208|||http://purl.uniprot.org/annotation/VAR_028313|||http://purl.uniprot.org/annotation/VAR_028314|||http://purl.uniprot.org/annotation/VAR_028315|||http://purl.uniprot.org/annotation/VAR_028316|||http://purl.uniprot.org/annotation/VAR_028317|||http://purl.uniprot.org/annotation/VAR_028318|||http://purl.uniprot.org/annotation/VAR_059950|||http://purl.uniprot.org/annotation/VSP_045908
http://togogenome.org/gene/9606:C11orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PAM5|||http://purl.uniprot.org/uniprot/Q9P2W6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C11orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089834
http://togogenome.org/gene/9606:LGI4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D6Y5|||http://purl.uniprot.org/uniprot/Q8N135                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In AMC1.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat LGI family member 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017712|||http://purl.uniprot.org/annotation/PRO_5002680919|||http://purl.uniprot.org/annotation/VAR_080055|||http://purl.uniprot.org/annotation/VAR_080056|||http://purl.uniprot.org/annotation/VAR_080057|||http://purl.uniprot.org/annotation/VSP_009230|||http://purl.uniprot.org/annotation/VSP_009231
http://togogenome.org/gene/9606:UNC5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y8R2|||http://purl.uniprot.org/uniprot/Q6ZN44                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Cytoplasmic|||Death|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||Interaction with DCC|||N-linked (GlcNAc...) asparagine|||Netrin receptor UNC5|||Netrin receptor UNC5A|||TSP type-1|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036068|||http://purl.uniprot.org/annotation/PRO_5025096353|||http://purl.uniprot.org/annotation/VSP_011693|||http://purl.uniprot.org/annotation/VSP_011694|||http://purl.uniprot.org/annotation/VSP_011695
http://togogenome.org/gene/9606:NPIPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2F6|||http://purl.uniprot.org/uniprot/O15103|||http://purl.uniprot.org/uniprot/Q9UND3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear pore complex-interacting protein family member A1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076275|||http://purl.uniprot.org/annotation/VAR_034141
http://togogenome.org/gene/9606:ITIH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RMS9|||http://purl.uniprot.org/uniprot/B7ZKJ8|||http://purl.uniprot.org/uniprot/Q14624                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  35 kDa inter-alpha-trypsin inhibitor heavy chain H4|||70 kDa inter-alpha-trypsin inhibitor heavy chain H4|||Basic and acidic residues|||Cleavage; by kallikrein|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||O-glycosylated at three sites|||O-linked (GalNAc...) threonine|||Potentially active peptide|||Proline-rich (PRR) potential bioactive peptide|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016541|||http://purl.uniprot.org/annotation/PRO_0000016542|||http://purl.uniprot.org/annotation/PRO_0000016543|||http://purl.uniprot.org/annotation/PRO_5002779795|||http://purl.uniprot.org/annotation/PRO_5014568442|||http://purl.uniprot.org/annotation/VAR_013836|||http://purl.uniprot.org/annotation/VAR_027869|||http://purl.uniprot.org/annotation/VAR_027870|||http://purl.uniprot.org/annotation/VAR_027871|||http://purl.uniprot.org/annotation/VAR_027872|||http://purl.uniprot.org/annotation/VAR_027873|||http://purl.uniprot.org/annotation/VSP_002761|||http://purl.uniprot.org/annotation/VSP_002762|||http://purl.uniprot.org/annotation/VSP_044764|||http://purl.uniprot.org/annotation/VSP_044765
http://togogenome.org/gene/9606:EDNRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24530                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes palmitoylation; when associated with S-402 and S-403.|||Abolishes palmitoylation; when associated with S-402 and S-405.|||Abolishes palmitoylation; when associated with S-403 and S-405.|||Associated with increased susceptibility for Hirschsprung disease; sex-dependent gene dosage effect.|||Cytoplasmic|||Disordered|||Endothelin receptor type B|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In HSCR2.|||In HSCR2; decreased calcium release; no effect on cell membrane location.|||In HSCR2; familial; loss of cell membrane location; new cytoplasmic location.|||In HSCR2; sporadic.|||In WS4A.|||In isoform B.|||In isoform C.|||N-linked (GlcNAc...) asparagine|||No effect on cell membrane location.|||Phosphoserine|||Phosphotyrosine|||Probable disease-associated variant found in patients with Waardenburg syndrome 2; decreased calcium release upon endothelin 3 exposure; loss of downstream pathway activation upon endothelin 3 exposure; no effect on cell membrane location; no effect on internalization upon endothelin 3 exposure.|||Probable disease-associated variant found in patients with Waardenburg syndrome 2; loss of cell membrane location; new cytoplasmic location.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012729|||http://purl.uniprot.org/annotation/VAR_003469|||http://purl.uniprot.org/annotation/VAR_003470|||http://purl.uniprot.org/annotation/VAR_003471|||http://purl.uniprot.org/annotation/VAR_003472|||http://purl.uniprot.org/annotation/VAR_003473|||http://purl.uniprot.org/annotation/VAR_003474|||http://purl.uniprot.org/annotation/VAR_003475|||http://purl.uniprot.org/annotation/VAR_014675|||http://purl.uniprot.org/annotation/VAR_014676|||http://purl.uniprot.org/annotation/VAR_014677|||http://purl.uniprot.org/annotation/VAR_014678|||http://purl.uniprot.org/annotation/VAR_015294|||http://purl.uniprot.org/annotation/VAR_019285|||http://purl.uniprot.org/annotation/VAR_024255|||http://purl.uniprot.org/annotation/VAR_078312|||http://purl.uniprot.org/annotation/VAR_078313|||http://purl.uniprot.org/annotation/VAR_078314|||http://purl.uniprot.org/annotation/VAR_078315|||http://purl.uniprot.org/annotation/VSP_001878|||http://purl.uniprot.org/annotation/VSP_001879
http://togogenome.org/gene/9606:ZNF330                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFG9|||http://purl.uniprot.org/uniprot/Q53EN0|||http://purl.uniprot.org/uniprot/Q9Y3S2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C4-type 1|||C4-type 2|||C4-type 3|||C4-type 4|||Disordered|||Nuclear localization signal|||Phosphoserine|||Zinc finger protein 330                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066590|||http://purl.uniprot.org/annotation/VAR_051500|||http://purl.uniprot.org/annotation/VAR_051501
http://togogenome.org/gene/9606:KISS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15726                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cleavage; by MMP2 and MMP9|||Disordered|||Essential for receptor binding and receptor activation|||In HH13; significantly reduced efficacy as well as potency.|||Kisspeptin-10|||Kisspeptin-13|||Kisspeptin-14|||Metastasis-suppressor KiSS-1|||Metastin|||Phenylalanine amide|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021544|||http://purl.uniprot.org/annotation/PRO_0000021545|||http://purl.uniprot.org/annotation/PRO_0000021546|||http://purl.uniprot.org/annotation/PRO_0000021547|||http://purl.uniprot.org/annotation/PRO_0000021548|||http://purl.uniprot.org/annotation/VAR_021396|||http://purl.uniprot.org/annotation/VAR_021397|||http://purl.uniprot.org/annotation/VAR_021398|||http://purl.uniprot.org/annotation/VAR_069179
http://togogenome.org/gene/9606:XPO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAV4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Exportin-5|||Found in a patient with nephrotic syndrome; unknown pathological significance.|||N-acetylalanine|||N6-acetyllysine|||Necessary for interaction with ILF3|||Necessary for interaction with Ran|||Phosphoserine|||Pre-miRNA binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235299|||http://purl.uniprot.org/annotation/VAR_028032|||http://purl.uniprot.org/annotation/VAR_048960|||http://purl.uniprot.org/annotation/VAR_076472
http://togogenome.org/gene/9606:GAL3ST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RP7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Galactose-3-O-sulfotransferase 4|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085209|||http://purl.uniprot.org/annotation/VAR_021989|||http://purl.uniprot.org/annotation/VAR_033736|||http://purl.uniprot.org/annotation/VSP_057006|||http://purl.uniprot.org/annotation/VSP_057007
http://togogenome.org/gene/9606:OXR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N573                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRAM|||In CHEGDD.|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 8.|||In isoform 6.|||In isoform 7.|||LysM|||Mediates oxidative antimutator activity|||Oxidation resistance protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231645|||http://purl.uniprot.org/annotation/VAR_025861|||http://purl.uniprot.org/annotation/VAR_025862|||http://purl.uniprot.org/annotation/VAR_025863|||http://purl.uniprot.org/annotation/VAR_083522|||http://purl.uniprot.org/annotation/VSP_039004|||http://purl.uniprot.org/annotation/VSP_039005|||http://purl.uniprot.org/annotation/VSP_039006|||http://purl.uniprot.org/annotation/VSP_039007|||http://purl.uniprot.org/annotation/VSP_039008|||http://purl.uniprot.org/annotation/VSP_039009|||http://purl.uniprot.org/annotation/VSP_039010|||http://purl.uniprot.org/annotation/VSP_039011|||http://purl.uniprot.org/annotation/VSP_039012|||http://purl.uniprot.org/annotation/VSP_039013|||http://purl.uniprot.org/annotation/VSP_039014|||http://purl.uniprot.org/annotation/VSP_043632|||http://purl.uniprot.org/annotation/VSP_043633
http://togogenome.org/gene/9606:SPTAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5S9|||http://purl.uniprot.org/uniprot/Q13813                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by mu-calpain|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In DEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SH3|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin alpha chain, non-erythrocytic 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073455|||http://purl.uniprot.org/annotation/VAR_012227|||http://purl.uniprot.org/annotation/VAR_035454|||http://purl.uniprot.org/annotation/VAR_035455|||http://purl.uniprot.org/annotation/VAR_035456|||http://purl.uniprot.org/annotation/VAR_035457|||http://purl.uniprot.org/annotation/VAR_038513|||http://purl.uniprot.org/annotation/VAR_063886|||http://purl.uniprot.org/annotation/VAR_063887|||http://purl.uniprot.org/annotation/VSP_012270|||http://purl.uniprot.org/annotation/VSP_012271
http://togogenome.org/gene/9606:CDKN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42771|||http://purl.uniprot.org/uniprot/Q8N726                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase inhibitor 2A|||Disordered|||Found in a patient with multiple primary melanoma; partial loss of CDK4 binding.|||Found in seminoma and medulloblastoma tissues from Li-Fraumeni syndrome patients carrying a mutation in TP53; somatic mutation.|||Found in some patients with melanoma; loss of CDK4 binding.|||Found in some patients with melanoma; partial loss of CDK4 binding.|||In CMM2 and FAMMMPC; impairs the function.|||In CMM2.|||In CMM2; also found in a biliary tract tumor and a patient with uveal melanoma; partial loss of CDK4 binding.|||In CMM2; also found in a lung tumor and a prostate tumor.|||In CMM2; also found in head and neck tumor; somatic mutation.|||In CMM2; impairs the function.|||In CMM2; loss of CDK4 binding.|||In CMM2; partial loss of CDK4 binding.|||In CMM2; requires 2 nucleotide substitutions.|||In CMM2; somatic mutation.|||In a biliary tract tumor and a familial melanoma.|||In a biliary tract tumor.|||In a bladder tumor.|||In a head and neck tumor.|||In a lung tumor and melanoma.|||In a lung tumor.|||In a pancreas tumor and a melanoma; loss of CDK4 binding.|||In a pancreas tumor; also found in head and neck tumor.|||In an esophagus tumor.|||In an esophagus tumor; also found in head and neck tumor; also found in a lung tumor.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform smARF.|||In leukemia.|||In melanoma; loss of CDK4 binding.|||In non-small cell lung carcinoma.|||In pancreas carcinoma; somatic mutation; partial loss of CDK4 binding.|||In some patients with melanoma; impairs the function.|||In squamous cell carcinoma.|||Interaction with CDK5RAP3 and MDM2|||N-acetylmethionine|||Phosphoserine|||Tumor suppressor ARF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144177|||http://purl.uniprot.org/annotation/PRO_0000144180|||http://purl.uniprot.org/annotation/VAR_001408|||http://purl.uniprot.org/annotation/VAR_001409|||http://purl.uniprot.org/annotation/VAR_001410|||http://purl.uniprot.org/annotation/VAR_001411|||http://purl.uniprot.org/annotation/VAR_001412|||http://purl.uniprot.org/annotation/VAR_001413|||http://purl.uniprot.org/annotation/VAR_001414|||http://purl.uniprot.org/annotation/VAR_001415|||http://purl.uniprot.org/annotation/VAR_001416|||http://purl.uniprot.org/annotation/VAR_001417|||http://purl.uniprot.org/annotation/VAR_001418|||http://purl.uniprot.org/annotation/VAR_001419|||http://purl.uniprot.org/annotation/VAR_001420|||http://purl.uniprot.org/annotation/VAR_001421|||http://purl.uniprot.org/annotation/VAR_001422|||http://purl.uniprot.org/annotation/VAR_001423|||http://purl.uniprot.org/annotation/VAR_001424|||http://purl.uniprot.org/annotation/VAR_001425|||http://purl.uniprot.org/annotation/VAR_001426|||http://purl.uniprot.org/annotation/VAR_001427|||http://purl.uniprot.org/annotation/VAR_001428|||http://purl.uniprot.org/annotation/VAR_001429|||http://purl.uniprot.org/annotation/VAR_001430|||http://purl.uniprot.org/annotation/VAR_001431|||http://purl.uniprot.org/annotation/VAR_001432|||http://purl.uniprot.org/annotation/VAR_001433|||http://purl.uniprot.org/annotation/VAR_001434|||http://purl.uniprot.org/annotation/VAR_001435|||http://purl.uniprot.org/annotation/VAR_001436|||http://purl.uniprot.org/annotation/VAR_001437|||http://purl.uniprot.org/annotation/VAR_001438|||http://purl.uniprot.org/annotation/VAR_001439|||http://purl.uniprot.org/annotation/VAR_001440|||http://purl.uniprot.org/annotation/VAR_001441|||http://purl.uniprot.org/annotation/VAR_001442|||http://purl.uniprot.org/annotation/VAR_001443|||http://purl.uniprot.org/annotation/VAR_001444|||http://purl.uniprot.org/annotation/VAR_001445|||http://purl.uniprot.org/annotation/VAR_001446|||http://purl.uniprot.org/annotation/VAR_001447|||http://purl.uniprot.org/annotation/VAR_001448|||http://purl.uniprot.org/annotation/VAR_001449|||http://purl.uniprot.org/annotation/VAR_001450|||http://purl.uniprot.org/annotation/VAR_001451|||http://purl.uniprot.org/annotation/VAR_001452|||http://purl.uniprot.org/annotation/VAR_001453|||http://purl.uniprot.org/annotation/VAR_001454|||http://purl.uniprot.org/annotation/VAR_001455|||http://purl.uniprot.org/annotation/VAR_001456|||http://purl.uniprot.org/annotation/VAR_001457|||http://purl.uniprot.org/annotation/VAR_001458|||http://purl.uniprot.org/annotation/VAR_001459|||http://purl.uniprot.org/annotation/VAR_001460|||http://purl.uniprot.org/annotation/VAR_001461|||http://purl.uniprot.org/annotation/VAR_001462|||http://purl.uniprot.org/annotation/VAR_001463|||http://purl.uniprot.org/annotation/VAR_001464|||http://purl.uniprot.org/annotation/VAR_001465|||http://purl.uniprot.org/annotation/VAR_001466|||http://purl.uniprot.org/annotation/VAR_001467|||http://purl.uniprot.org/annotation/VAR_001468|||http://purl.uniprot.org/annotation/VAR_001469|||http://purl.uniprot.org/annotation/VAR_001470|||http://purl.uniprot.org/annotation/VAR_001471|||http://purl.uniprot.org/annotation/VAR_001472|||http://purl.uniprot.org/annotation/VAR_001473|||http://purl.uniprot.org/annotation/VAR_001474|||http://purl.uniprot.org/annotation/VAR_001475|||http://purl.uniprot.org/annotation/VAR_001476|||http://purl.uniprot.org/annotation/VAR_001477|||http://purl.uniprot.org/annotation/VAR_001478|||http://purl.uniprot.org/annotation/VAR_001479|||http://purl.uniprot.org/annotation/VAR_001480|||http://purl.uniprot.org/annotation/VAR_001481|||http://purl.uniprot.org/annotation/VAR_001482|||http://purl.uniprot.org/annotation/VAR_001483|||http://purl.uniprot.org/annotation/VAR_001484|||http://purl.uniprot.org/annotation/VAR_001486|||http://purl.uniprot.org/annotation/VAR_001487|||http://purl.uniprot.org/annotation/VAR_012317|||http://purl.uniprot.org/annotation/VAR_015818|||http://purl.uniprot.org/annotation/VAR_023604|||http://purl.uniprot.org/annotation/VAR_029287|||http://purl.uniprot.org/annotation/VAR_035068|||http://purl.uniprot.org/annotation/VAR_035069|||http://purl.uniprot.org/annotation/VAR_053028|||http://purl.uniprot.org/annotation/VAR_053029|||http://purl.uniprot.org/annotation/VAR_053030|||http://purl.uniprot.org/annotation/VAR_053031|||http://purl.uniprot.org/annotation/VAR_053032|||http://purl.uniprot.org/annotation/VAR_053033|||http://purl.uniprot.org/annotation/VAR_053034|||http://purl.uniprot.org/annotation/VAR_053035|||http://purl.uniprot.org/annotation/VAR_058549|||http://purl.uniprot.org/annotation/VAR_058550|||http://purl.uniprot.org/annotation/VAR_058551|||http://purl.uniprot.org/annotation/VAR_058552|||http://purl.uniprot.org/annotation/VAR_058553|||http://purl.uniprot.org/annotation/VAR_058554|||http://purl.uniprot.org/annotation/VAR_058555|||http://purl.uniprot.org/annotation/VAR_058556|||http://purl.uniprot.org/annotation/VAR_058557|||http://purl.uniprot.org/annotation/VAR_058558|||http://purl.uniprot.org/annotation/VAR_058559|||http://purl.uniprot.org/annotation/VSP_015864|||http://purl.uniprot.org/annotation/VSP_015865|||http://purl.uniprot.org/annotation/VSP_015866|||http://purl.uniprot.org/annotation/VSP_043577|||http://purl.uniprot.org/annotation/VSP_044962
http://togogenome.org/gene/9606:TM4SF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZW46|||http://purl.uniprot.org/uniprot/Q96DZ7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane 4 L6 family member 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219305|||http://purl.uniprot.org/annotation/VAR_057280|||http://purl.uniprot.org/annotation/VAR_060546|||http://purl.uniprot.org/annotation/VSP_045895
http://togogenome.org/gene/9606:DNAJC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXB1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-591.|||Abolishes disulfide reductase activity; when associated with A-161; A-483 and A-703.|||Abolishes disulfide reductase activity; when associated with A-161; A-591 and A-703.|||Abolishes disulfide reductase activity; when associated with A-483; A-591 and A-703.|||DnaJ homolog subfamily C member 10|||In isoform 2.|||In isoform 3.|||J|||N-linked (GlcNAc...) asparagine|||Prevents interaction with HSPA5, leading to prolonged interaction with substrate proteins.|||Prevents secretion from ER|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3|||Thioredoxin 4|||Trxb 1|||Trxb 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281483|||http://purl.uniprot.org/annotation/VAR_031247|||http://purl.uniprot.org/annotation/VAR_031248|||http://purl.uniprot.org/annotation/VAR_031249|||http://purl.uniprot.org/annotation/VAR_048912|||http://purl.uniprot.org/annotation/VSP_024011|||http://purl.uniprot.org/annotation/VSP_054434|||http://purl.uniprot.org/annotation/VSP_054435
http://togogenome.org/gene/9606:GABRR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DER2|||http://purl.uniprot.org/uniprot/P28476                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit rho-2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000488|||http://purl.uniprot.org/annotation/VSP_044373
http://togogenome.org/gene/9606:PPIE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with KMT2A.|||Abolishes interaction with KMT2A. Abolishes inhibition of KMT2A activity.|||Basic and acidic residues|||Decreased affinity for KMT2A.|||Decreased affinity for RNA.|||Disordered|||Expected to disrupt peptidylproline binding. Decreases interaction with KMT2A. Abolishes inhibition of KMT2A activity.|||Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-191.|||Expected to disrupt proline isomerase activity. Abolishes inhibition of KMT2A activity; when associated with A-196.|||Impairs protein folding.|||In isoform 3.|||In isoform B.|||No effect on interaction with KMT2A.|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase E|||Phosphoserine|||RRM|||Slightly decreased affinity for KMT2A.|||Strongly decreased affinity for KMT2A. Decreased affinity for RNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064157|||http://purl.uniprot.org/annotation/VSP_005181|||http://purl.uniprot.org/annotation/VSP_046370
http://togogenome.org/gene/9606:ADAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55265                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A to I editase|||Abolishes interaction with TNPO1, TNPO1-mediated nuclear import and nuclear location.|||Abolishes nuclear location.|||Abolishes sumoylation.|||Asymmetric dimethylarginine|||Basic and acidic residues|||C-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal|||DRBM 1|||DRBM 2|||DRBM 3|||Decreased nuclear and partially cytoplasmic location.|||Disordered|||Disrupts nuclear localization signal. No effect on RNA binding.|||Disrupts the bi-partite nuclear localization signal and abolishes nuclear location.|||Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and N-723.|||Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and S-719.|||Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with S-719 and N-723.|||Double-stranded RNA-specific adenosine deaminase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In AGS6.|||In DSH.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with Z-DNA|||N-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal|||No effect on nuclear location. No effect on RNA binding.|||No effect on nuclear location; when associated with A-718 and A-721.|||No effect on nuclear location; when associated with A-721 and A-724.|||Phosphoserine|||Phosphothreonine|||Proton donor|||Strongly impaired RNA binding. No effect on nuclear location.|||Z-binding 1|||Z-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171774|||http://purl.uniprot.org/annotation/VAR_017240|||http://purl.uniprot.org/annotation/VAR_017604|||http://purl.uniprot.org/annotation/VAR_017605|||http://purl.uniprot.org/annotation/VAR_021729|||http://purl.uniprot.org/annotation/VAR_024407|||http://purl.uniprot.org/annotation/VAR_026669|||http://purl.uniprot.org/annotation/VAR_035805|||http://purl.uniprot.org/annotation/VAR_048725|||http://purl.uniprot.org/annotation/VAR_069535|||http://purl.uniprot.org/annotation/VAR_069536|||http://purl.uniprot.org/annotation/VAR_069537|||http://purl.uniprot.org/annotation/VAR_069538|||http://purl.uniprot.org/annotation/VAR_069539|||http://purl.uniprot.org/annotation/VAR_069540|||http://purl.uniprot.org/annotation/VAR_069541|||http://purl.uniprot.org/annotation/VAR_069542|||http://purl.uniprot.org/annotation/VSP_008872|||http://purl.uniprot.org/annotation/VSP_008873|||http://purl.uniprot.org/annotation/VSP_008874|||http://purl.uniprot.org/annotation/VSP_019235
http://togogenome.org/gene/9606:RHOD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00212                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes endosomal localization.|||Cysteine methyl ester|||Effector region|||Removed in mature form|||Rho-related GTP-binding protein RhoD|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198863|||http://purl.uniprot.org/annotation/PRO_0000223365|||http://purl.uniprot.org/annotation/VAR_058408
http://togogenome.org/gene/9606:GSTO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78417|||http://purl.uniprot.org/uniprot/V9HWG9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase omega-1|||In allele GSTO1*B; decreased protein stability.|||In allele GSTO1*C; no effect on protein stability.|||In isoform 2.|||In isoform 3.|||Loss of activity.|||N-acetylserine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185884|||http://purl.uniprot.org/annotation/VAR_016811|||http://purl.uniprot.org/annotation/VAR_016813|||http://purl.uniprot.org/annotation/VAR_024484|||http://purl.uniprot.org/annotation/VAR_026583|||http://purl.uniprot.org/annotation/VAR_029269|||http://purl.uniprot.org/annotation/VAR_061231|||http://purl.uniprot.org/annotation/VSP_045819|||http://purl.uniprot.org/annotation/VSP_045820
http://togogenome.org/gene/9606:CRLF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75462                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Cytokine receptor-like factor 1|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like C2-type|||In CISS1.|||In CISS1; together with I-113.|||In CISS1; together with P-114.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011039|||http://purl.uniprot.org/annotation/VAR_017865|||http://purl.uniprot.org/annotation/VAR_017866|||http://purl.uniprot.org/annotation/VAR_028355|||http://purl.uniprot.org/annotation/VAR_033113|||http://purl.uniprot.org/annotation/VAR_070817|||http://purl.uniprot.org/annotation/VAR_070818|||http://purl.uniprot.org/annotation/VAR_070819|||http://purl.uniprot.org/annotation/VAR_070820|||http://purl.uniprot.org/annotation/VAR_070821|||http://purl.uniprot.org/annotation/VAR_070822|||http://purl.uniprot.org/annotation/VAR_070823|||http://purl.uniprot.org/annotation/VAR_070824|||http://purl.uniprot.org/annotation/VAR_070825|||http://purl.uniprot.org/annotation/VAR_070826|||http://purl.uniprot.org/annotation/VAR_070827
http://togogenome.org/gene/9606:APOA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06727                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||13 X 22 AA approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Apolipoprotein A-IV|||Disordered|||In Budapest-2.|||In Seattle-1; may contribute to the development of familial combined hyperlipidemia.|||In Seattle-2; may contribute to the development of familial combined hyperlipidemia.|||In Seattle-3.|||In allele APOA-IV*0 and allele APOA-IV*5; allele APOA-IV*5 is further defined by a silent nucleotide substitution.|||In allele APOA-IV*0A; associated with H-380.|||In allele APOA-IV*1A and allele Budapest-1.|||In allele APOA-IV*1D.|||In allele APOA-IV*2 and allele APOA-IV*0A; associated with E-187 in allele APOA-IV*0A.|||In allele APOA-IV*3.|||In allele APOA-IV*3A.|||In allele Budapest-1.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001975|||http://purl.uniprot.org/annotation/VAR_000626|||http://purl.uniprot.org/annotation/VAR_000627|||http://purl.uniprot.org/annotation/VAR_000628|||http://purl.uniprot.org/annotation/VAR_000629|||http://purl.uniprot.org/annotation/VAR_000630|||http://purl.uniprot.org/annotation/VAR_000631|||http://purl.uniprot.org/annotation/VAR_000632|||http://purl.uniprot.org/annotation/VAR_000633|||http://purl.uniprot.org/annotation/VAR_000634|||http://purl.uniprot.org/annotation/VAR_000635|||http://purl.uniprot.org/annotation/VAR_000636|||http://purl.uniprot.org/annotation/VAR_000637|||http://purl.uniprot.org/annotation/VAR_000638|||http://purl.uniprot.org/annotation/VAR_014610|||http://purl.uniprot.org/annotation/VAR_014611|||http://purl.uniprot.org/annotation/VAR_025443|||http://purl.uniprot.org/annotation/VAR_025444
http://togogenome.org/gene/9606:ITPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14571                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In ANHD; loss of function mutation.|||In isoform Short.|||Inositol 1,4,5-trisphosphate receptor type 2|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153924|||http://purl.uniprot.org/annotation/VAR_055963|||http://purl.uniprot.org/annotation/VAR_055964|||http://purl.uniprot.org/annotation/VAR_055965|||http://purl.uniprot.org/annotation/VAR_073688|||http://purl.uniprot.org/annotation/VSP_002699|||http://purl.uniprot.org/annotation/VSP_002700
http://togogenome.org/gene/9606:MOV10L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEAG box|||Disordered|||In SPGF73.|||In SPGF73; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||RNA helicase Mov10l1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080706|||http://purl.uniprot.org/annotation/VAR_013694|||http://purl.uniprot.org/annotation/VAR_013695|||http://purl.uniprot.org/annotation/VAR_013696|||http://purl.uniprot.org/annotation/VAR_013697|||http://purl.uniprot.org/annotation/VAR_020148|||http://purl.uniprot.org/annotation/VAR_034100|||http://purl.uniprot.org/annotation/VAR_034101|||http://purl.uniprot.org/annotation/VAR_059457|||http://purl.uniprot.org/annotation/VAR_087327|||http://purl.uniprot.org/annotation/VAR_087328|||http://purl.uniprot.org/annotation/VSP_003390|||http://purl.uniprot.org/annotation/VSP_003391|||http://purl.uniprot.org/annotation/VSP_010945|||http://purl.uniprot.org/annotation/VSP_010946|||http://purl.uniprot.org/annotation/VSP_010947|||http://purl.uniprot.org/annotation/VSP_010948|||http://purl.uniprot.org/annotation/VSP_045413|||http://purl.uniprot.org/annotation/VSP_046082|||http://purl.uniprot.org/annotation/VSP_046083
http://togogenome.org/gene/9606:HAGHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DED4|||http://purl.uniprot.org/uniprot/Q6PII5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  Hydroxyacylglutathione hydrolase-like protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Metallo-beta-lactamase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313601|||http://purl.uniprot.org/annotation/VSP_030052|||http://purl.uniprot.org/annotation/VSP_030053|||http://purl.uniprot.org/annotation/VSP_030054|||http://purl.uniprot.org/annotation/VSP_030055|||http://purl.uniprot.org/annotation/VSP_030056
http://togogenome.org/gene/9606:RNMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K946|||http://purl.uniprot.org/uniprot/O43148                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-409. Decreased interaction with RAMAC; when associated with E-409.|||Decreased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-413. Decreased interaction with RAMAC; when associated with E-413.|||Disordered|||Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127.|||Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107.|||Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127.|||In isoform 2.|||Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-450. No change in interaction with RAMAC; when associated with E-450.|||Increased S-adenosyl-L-methionine binding and methyltransferase activity in absence of RAMAC; when associated with E-452. No change in interaction with RAMAC; when associated with E-452.|||Loss of activity.|||Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-398.|||Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-393 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-393 and C-417.|||Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-178; C-398 and C-417. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-178; C-398 and C-417.|||Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417. Complete restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417. Loss of methyltransferase activity in presence or absence of RAMAC; when associated with C-417; C-393 and C-398. Partially restored RAMAC-mediated methyltransferase activity under reducing conditions; when associated with C-417; C-393 and C-398.|||MRNA cap 0 methyltransferase|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Strongly impairs enzyme activity.|||mRNA cap 0 methyltransferase|||mRNA cap binding|||mRNA cap guanine-N7 methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248321|||http://purl.uniprot.org/annotation/VSP_020241
http://togogenome.org/gene/9606:TEX51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUA7|||http://purl.uniprot.org/uniprot/A0A9L9PXS2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Testis-expressed protein 51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000441046|||http://purl.uniprot.org/annotation/PRO_5040430559
http://togogenome.org/gene/9606:DNAJC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5T4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 15|||Helical|||J|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247139|||http://purl.uniprot.org/annotation/VAR_027077
http://togogenome.org/gene/9606:SF3B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13435                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SMN1; Abolishes methylation by PRMT9. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-507 and R-509.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Does not affect methylation by PRMT9.|||Does not affect methylation by PRMT9; when associated with A-506.|||Does not affect methylation by PRMT9; when associated with A-510.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CFM.|||Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-507.|||Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with A-509.|||Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-507. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-507.|||Moderately diminished formation of omega-N monomethylarginine but greatly reduced formation of symmetrical dimethylarginine; when associated with R-509. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with R-508. Abolishes formation of omega-N monomethylarginine and formation of symmetrical dimethylarginine; when associated with K-508 and R-509.|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; by PRMT9; alternate|||Phosphoserine|||Phosphothreonine|||Pro residues|||Required for interaction with PRMT9|||SAP|||Splicing factor 3B subunit 2|||Symmetric dimethylarginine; by PRMT9; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174328|||http://purl.uniprot.org/annotation/VAR_087086|||http://purl.uniprot.org/annotation/VAR_087087
http://togogenome.org/gene/9606:ZNF814                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6K7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 814                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394964
http://togogenome.org/gene/9606:TPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWU9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ACT|||Basic and acidic residues|||Disordered|||In ADHD7; has severely reduced solubility; is completely inactive; loss of function may lead to a reduced serotonin synthesis.|||In RNA edited version.|||In isoform b.|||Linked with susceptibility to major depressive disorder; may be due to a rare RNA editing event; 80% loss of function; decreases solubility; decreases thermal stability; reduces catalytic activity.|||May be associated with susceptibility to bipolar affective disorder; decreases solubility; decreases thermal stability; catalytic activity as the wild type; moderate loss-of-function observed manifested via stability and solubility effect.|||Moderate loss-of-function observed manifested via stability and solubility effect.|||Phosphoserine|||The property of the variant is indistinguishable from the wild-type.|||Tryptophan 5-hydroxylase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205574|||http://purl.uniprot.org/annotation/VAR_026749|||http://purl.uniprot.org/annotation/VAR_046136|||http://purl.uniprot.org/annotation/VAR_058938|||http://purl.uniprot.org/annotation/VAR_058939|||http://purl.uniprot.org/annotation/VAR_058940|||http://purl.uniprot.org/annotation/VAR_058941|||http://purl.uniprot.org/annotation/VAR_058942|||http://purl.uniprot.org/annotation/VAR_058943|||http://purl.uniprot.org/annotation/VAR_058944|||http://purl.uniprot.org/annotation/VAR_065019|||http://purl.uniprot.org/annotation/VAR_065020|||http://purl.uniprot.org/annotation/VSP_040971
http://togogenome.org/gene/9606:CHMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3E7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63.|||Abolishes dimerization; when associated with S-54; N-56 and E-59.|||Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169.|||Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169.|||Abolishes interaction with VPS4A and STAMBP.|||Charged multivesicular body protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs HIV-1 release; when associated with 24-S-A-25.|||Impairs HIV-1 release; when associated with S-28.|||Impairs interaction with VPS4A and STAMBP.|||Important for autoinhibitory function|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62.|||Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48.|||Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169.|||Interaction with STAMBP|||Interaction with VPS4A|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||MIT-interacting motif|||Membrane association; releases autoinhibition.|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211479|||http://purl.uniprot.org/annotation/VSP_041076|||http://purl.uniprot.org/annotation/VSP_042124|||http://purl.uniprot.org/annotation/VSP_042125
http://togogenome.org/gene/9606:EIF3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y262                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 3 subunit L|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||PCI|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084162|||http://purl.uniprot.org/annotation/VSP_045881
http://togogenome.org/gene/9606:PEG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZG9|||http://purl.uniprot.org/uniprot/Q86TG7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Inhibits proteolytic cleavage.|||Necessary for interaction with ACVRL1|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Retrotransposon-derived protein PEG10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323026|||http://purl.uniprot.org/annotation/VSP_032007|||http://purl.uniprot.org/annotation/VSP_032008|||http://purl.uniprot.org/annotation/VSP_061361|||http://purl.uniprot.org/annotation/VSP_061362
http://togogenome.org/gene/9606:MALT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5S1|||http://purl.uniprot.org/uniprot/Q9UDY8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to TRAF6.|||Breakpoint for translocation to form BIRC2-MALT1|||Caspase family p20|||Caspase-like|||Death|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In IMD12.|||In isoform 2.|||Mucosa-associated lymphoid tissue lymphoma translocation protein 1|||N-acetylserine|||Nuclear export signal|||Phosphoserine|||Removed|||Slight decrease in NF-kappa-B activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072821|||http://purl.uniprot.org/annotation/VAR_048620|||http://purl.uniprot.org/annotation/VAR_070857|||http://purl.uniprot.org/annotation/VSP_000844
http://togogenome.org/gene/9606:GALNS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34059|||http://purl.uniprot.org/uniprot/Q6YL38|||http://purl.uniprot.org/uniprot/Q96I49                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Associated with S-409 in a MPS4A patient.|||Catalytic domain|||In MPS4A.|||In MPS4A; associated with M-67 in a patient.|||In MPS4A; intermediate form.|||In MPS4A; loss of enzymatic activity.|||In MPS4A; mild form.|||In MPS4A; mild/intermediate form.|||In MPS4A; mild/intermediate/severe form.|||In MPS4A; mild/severe/intermediate form.|||In MPS4A; reduced enzymatic activity.|||In MPS4A; severe form.|||In MPS4A; severe form; common mutation; found in patients with Irish-British ancestry.|||In a colorectal cancer sample; somatic mutation.|||N-acetylgalactosamine-6-sulfatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033411|||http://purl.uniprot.org/annotation/VAR_007172|||http://purl.uniprot.org/annotation/VAR_007173|||http://purl.uniprot.org/annotation/VAR_007174|||http://purl.uniprot.org/annotation/VAR_007175|||http://purl.uniprot.org/annotation/VAR_007177|||http://purl.uniprot.org/annotation/VAR_007178|||http://purl.uniprot.org/annotation/VAR_007179|||http://purl.uniprot.org/annotation/VAR_007180|||http://purl.uniprot.org/annotation/VAR_007181|||http://purl.uniprot.org/annotation/VAR_007182|||http://purl.uniprot.org/annotation/VAR_007183|||http://purl.uniprot.org/annotation/VAR_007184|||http://purl.uniprot.org/annotation/VAR_007185|||http://purl.uniprot.org/annotation/VAR_007186|||http://purl.uniprot.org/annotation/VAR_007187|||http://purl.uniprot.org/annotation/VAR_007188|||http://purl.uniprot.org/annotation/VAR_007189|||http://purl.uniprot.org/annotation/VAR_007190|||http://purl.uniprot.org/annotation/VAR_007191|||http://purl.uniprot.org/annotation/VAR_007192|||http://purl.uniprot.org/annotation/VAR_007193|||http://purl.uniprot.org/annotation/VAR_007194|||http://purl.uniprot.org/annotation/VAR_007195|||http://purl.uniprot.org/annotation/VAR_007196|||http://purl.uniprot.org/annotation/VAR_007197|||http://purl.uniprot.org/annotation/VAR_007198|||http://purl.uniprot.org/annotation/VAR_007199|||http://purl.uniprot.org/annotation/VAR_007200|||http://purl.uniprot.org/annotation/VAR_007201|||http://purl.uniprot.org/annotation/VAR_007202|||http://purl.uniprot.org/annotation/VAR_007203|||http://purl.uniprot.org/annotation/VAR_007204|||http://purl.uniprot.org/annotation/VAR_007205|||http://purl.uniprot.org/annotation/VAR_007206|||http://purl.uniprot.org/annotation/VAR_007207|||http://purl.uniprot.org/annotation/VAR_007208|||http://purl.uniprot.org/annotation/VAR_007209|||http://purl.uniprot.org/annotation/VAR_007210|||http://purl.uniprot.org/annotation/VAR_007211|||http://purl.uniprot.org/annotation/VAR_007212|||http://purl.uniprot.org/annotation/VAR_007213|||http://purl.uniprot.org/annotation/VAR_007214|||http://purl.uniprot.org/annotation/VAR_007215|||http://purl.uniprot.org/annotation/VAR_007216|||http://purl.uniprot.org/annotation/VAR_007217|||http://purl.uniprot.org/annotation/VAR_007218|||http://purl.uniprot.org/annotation/VAR_007219|||http://purl.uniprot.org/annotation/VAR_007220|||http://purl.uniprot.org/annotation/VAR_007221|||http://purl.uniprot.org/annotation/VAR_007222|||http://purl.uniprot.org/annotation/VAR_007223|||http://purl.uniprot.org/annotation/VAR_007224|||http://purl.uniprot.org/annotation/VAR_007225|||http://purl.uniprot.org/annotation/VAR_007226|||http://purl.uniprot.org/annotation/VAR_007227|||http://purl.uniprot.org/annotation/VAR_007228|||http://purl.uniprot.org/annotation/VAR_007229|||http://purl.uniprot.org/annotation/VAR_007230|||http://purl.uniprot.org/annotation/VAR_007231|||http://purl.uniprot.org/annotation/VAR_007232|||http://purl.uniprot.org/annotation/VAR_007233|||http://purl.uniprot.org/annotation/VAR_007234|||http://purl.uniprot.org/annotation/VAR_007235|||http://purl.uniprot.org/annotation/VAR_007236|||http://purl.uniprot.org/annotation/VAR_007237|||http://purl.uniprot.org/annotation/VAR_007238|||http://purl.uniprot.org/annotation/VAR_007239|||http://purl.uniprot.org/annotation/VAR_024873|||http://purl.uniprot.org/annotation/VAR_024874|||http://purl.uniprot.org/annotation/VAR_024875|||http://purl.uniprot.org/annotation/VAR_024876|||http://purl.uniprot.org/annotation/VAR_024877|||http://purl.uniprot.org/annotation/VAR_024878|||http://purl.uniprot.org/annotation/VAR_024879|||http://purl.uniprot.org/annotation/VAR_024880|||http://purl.uniprot.org/annotation/VAR_024881|||http://purl.uniprot.org/annotation/VAR_024882|||http://purl.uniprot.org/annotation/VAR_024883|||http://purl.uniprot.org/annotation/VAR_024884|||http://purl.uniprot.org/annotation/VAR_024885|||http://purl.uniprot.org/annotation/VAR_024886|||http://purl.uniprot.org/annotation/VAR_024887|||http://purl.uniprot.org/annotation/VAR_024888|||http://purl.uniprot.org/annotation/VAR_024889|||http://purl.uniprot.org/annotation/VAR_024890|||http://purl.uniprot.org/annotation/VAR_024891|||http://purl.uniprot.org/annotation/VAR_024892|||http://purl.uniprot.org/annotation/VAR_024893|||http://purl.uniprot.org/annotation/VAR_024894|||http://purl.uniprot.org/annotation/VAR_024895|||http://purl.uniprot.org/annotation/VAR_024896|||http://purl.uniprot.org/annotation/VAR_024897|||http://purl.uniprot.org/annotation/VAR_024898|||http://purl.uniprot.org/annotation/VAR_024899|||http://purl.uniprot.org/annotation/VAR_024900|||http://purl.uniprot.org/annotation/VAR_024901|||http://purl.uniprot.org/annotation/VAR_024902|||http://purl.uniprot.org/annotation/VAR_024903|||http://purl.uniprot.org/annotation/VAR_024904|||http://purl.uniprot.org/annotation/VAR_024905|||http://purl.uniprot.org/annotation/VAR_024906|||http://purl.uniprot.org/annotation/VAR_024907|||http://purl.uniprot.org/annotation/VAR_024908|||http://purl.uniprot.org/annotation/VAR_024909|||http://purl.uniprot.org/annotation/VAR_024910|||http://purl.uniprot.org/annotation/VAR_024911|||http://purl.uniprot.org/annotation/VAR_024912|||http://purl.uniprot.org/annotation/VAR_024913|||http://purl.uniprot.org/annotation/VAR_024914|||http://purl.uniprot.org/annotation/VAR_024915|||http://purl.uniprot.org/annotation/VAR_024916|||http://purl.uniprot.org/annotation/VAR_024917|||http://purl.uniprot.org/annotation/VAR_024918|||http://purl.uniprot.org/annotation/VAR_024919|||http://purl.uniprot.org/annotation/VAR_024920|||http://purl.uniprot.org/annotation/VAR_024921|||http://purl.uniprot.org/annotation/VAR_036493|||http://purl.uniprot.org/annotation/VAR_071569|||http://purl.uniprot.org/annotation/VAR_071570|||http://purl.uniprot.org/annotation/VAR_071571|||http://purl.uniprot.org/annotation/VAR_071572|||http://purl.uniprot.org/annotation/VAR_071573|||http://purl.uniprot.org/annotation/VAR_071574|||http://purl.uniprot.org/annotation/VAR_071575|||http://purl.uniprot.org/annotation/VAR_071576|||http://purl.uniprot.org/annotation/VAR_071577|||http://purl.uniprot.org/annotation/VAR_071578|||http://purl.uniprot.org/annotation/VAR_071579|||http://purl.uniprot.org/annotation/VAR_071580|||http://purl.uniprot.org/annotation/VAR_071581|||http://purl.uniprot.org/annotation/VAR_071582|||http://purl.uniprot.org/annotation/VAR_071583|||http://purl.uniprot.org/annotation/VAR_071584|||http://purl.uniprot.org/annotation/VAR_071585|||http://purl.uniprot.org/annotation/VAR_071586|||http://purl.uniprot.org/annotation/VAR_071587|||http://purl.uniprot.org/annotation/VAR_071588|||http://purl.uniprot.org/annotation/VAR_071589|||http://purl.uniprot.org/annotation/VAR_071590|||http://purl.uniprot.org/annotation/VAR_071591|||http://purl.uniprot.org/annotation/VAR_071592|||http://purl.uniprot.org/annotation/VAR_071593|||http://purl.uniprot.org/annotation/VAR_071594|||http://purl.uniprot.org/annotation/VAR_071595|||http://purl.uniprot.org/annotation/VAR_071596|||http://purl.uniprot.org/annotation/VAR_071597|||http://purl.uniprot.org/annotation/VAR_071598|||http://purl.uniprot.org/annotation/VAR_071599|||http://purl.uniprot.org/annotation/VAR_071600
http://togogenome.org/gene/9606:KSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PB13|||http://purl.uniprot.org/uniprot/Q6VAB6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Impairs MAP2K1 binding.|||Impairs formation of heterotetramers with MAP2K1, but not the formation of heterodimers.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Kinase suppressor of Ras 2|||Loss of kinase activity.|||Phorbol-ester/DAG-type|||Phosphoserine; by MARK3|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086231|||http://purl.uniprot.org/annotation/VAR_040659|||http://purl.uniprot.org/annotation/VSP_012234|||http://purl.uniprot.org/annotation/VSP_012235|||http://purl.uniprot.org/annotation/VSP_012236|||http://purl.uniprot.org/annotation/VSP_012237
http://togogenome.org/gene/9606:RNF220                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTB9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF220|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HLD23; shows decreased beta-catenin binding.|||In isoform 2.|||Phosphoserine|||RING-type|||Required for targeting to the cytoplasm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277657|||http://purl.uniprot.org/annotation/VAR_086785|||http://purl.uniprot.org/annotation/VAR_086786|||http://purl.uniprot.org/annotation/VSP_055437|||http://purl.uniprot.org/annotation/VSP_055438
http://togogenome.org/gene/9606:CYP4V2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWL3                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4V2|||Helical|||In BCD.|||In BCD; impaired omega hydroxylase activity.|||In isoform 2.|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051859|||http://purl.uniprot.org/annotation/VAR_023084|||http://purl.uniprot.org/annotation/VAR_023085|||http://purl.uniprot.org/annotation/VAR_023086|||http://purl.uniprot.org/annotation/VAR_023087|||http://purl.uniprot.org/annotation/VAR_023088|||http://purl.uniprot.org/annotation/VAR_023089|||http://purl.uniprot.org/annotation/VAR_023090|||http://purl.uniprot.org/annotation/VAR_023091|||http://purl.uniprot.org/annotation/VAR_033821|||http://purl.uniprot.org/annotation/VAR_038606|||http://purl.uniprot.org/annotation/VAR_038607|||http://purl.uniprot.org/annotation/VAR_055379|||http://purl.uniprot.org/annotation/VAR_055380|||http://purl.uniprot.org/annotation/VAR_055381|||http://purl.uniprot.org/annotation/VSP_014918
http://togogenome.org/gene/9606:EPM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95278                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NHLRC1.|||CBM20|||Complete loss of phosphatase activity.|||Complete loss of phosphatase activity. Does not affect glycogen binding.|||Complete loss of phosphatase activity. Does not affect glycogen binding. Does not affect self-interaction. Increases the interaction with PPP1R3C.|||Complete loss of phosphatase activity. No effect on glycogen binding.|||Does not affect glycogen binding.|||Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2.|||Fails to homodimerize. Does not affect carbohydrate binding or phosphatase activity.|||Fails to homodimerize. Does not affect carbohydrate binding, interaction with NHLRC1, phosphatase activity, or ubiquitination by NHLRC1.|||Glucan phosphatase signature motif CXAGXGR|||Impairs protein stability. Strongly reduces phosphatase activity. No effect on glycogen binding.|||In EPM2.|||In EPM2; abolishes interaction with NHLRC1.|||In EPM2; affects phosphatase activity and glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; atypical form; does not affect glycogen binding.|||In EPM2; atypical form; learning difficuties with childhood-onset.|||In EPM2; causes location of isoform 1 at cytoplasmic punctae; does not affect homodimerization of isoform 1 but prevents heterodimerization of isoform 1 and isoform 2.|||In EPM2; does not affect glycogen binding.|||In EPM2; impaired phosphatase activity; does not affect glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; impairs protein stability; affects phosphatase activity; abolishes glycogen binding; abolishes phosphatase activity with insoluble glucan; disrupts the interaction with PPP1R3C.|||In EPM2; impairs protein stability; impairs phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; loss of phosphatase activity; reduced self-interaction capacity; disrupts the interaction with PPP1R3C.|||In EPM2; results in ubiquitin-positive perinuclear aggregates; impairs phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; reduced self-interaction capacity; abolishes interaction with NHLRC1, PPP1R3C and PRKAA2; no effect on phosphorylation of protein.|||In EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C.|||In EPM2; results in ubiquitin-positive perinuclear aggregates; no effect on glycogen binding; abolishes phosphatase activity; may affect proper folding.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Laforin|||Loss of phosphatase activity. Abolishes glycogen binding.|||Loss of phosphatase activity. No effect on glycogen binding.|||No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.|||No effect on homodimerization.|||No effect on phosphatase activity.|||Partial loss of phosphatase activity. Abolishes homodimerization. Abolishes interaction with NHLRC1, PPP1R3C and PRKAA2. Does not affect glycogen binding. Reduces stability of the protein.|||Partial loss of phosphatase activity. Increases interaction with NHLRC1. Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. Does not affect binding to carbohydrate. Does not affect homodimerization.|||Phosphocysteine intermediate|||Phosphoserine; by AMPK|||Required for homodimerization|||Strongly decreased phosphatase activity. No effect on glycogen binding.|||Strongly reduces phosphatase activity. Strongly reduces glycogen binding.|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094838|||http://purl.uniprot.org/annotation/VAR_019465|||http://purl.uniprot.org/annotation/VAR_019466|||http://purl.uniprot.org/annotation/VAR_019467|||http://purl.uniprot.org/annotation/VAR_019468|||http://purl.uniprot.org/annotation/VAR_019469|||http://purl.uniprot.org/annotation/VAR_019470|||http://purl.uniprot.org/annotation/VAR_019471|||http://purl.uniprot.org/annotation/VAR_019472|||http://purl.uniprot.org/annotation/VAR_019473|||http://purl.uniprot.org/annotation/VAR_019474|||http://purl.uniprot.org/annotation/VAR_019475|||http://purl.uniprot.org/annotation/VAR_019476|||http://purl.uniprot.org/annotation/VAR_019477|||http://purl.uniprot.org/annotation/VAR_019478|||http://purl.uniprot.org/annotation/VAR_019479|||http://purl.uniprot.org/annotation/VAR_019480|||http://purl.uniprot.org/annotation/VAR_019481|||http://purl.uniprot.org/annotation/VAR_046383|||http://purl.uniprot.org/annotation/VAR_046384|||http://purl.uniprot.org/annotation/VAR_046385|||http://purl.uniprot.org/annotation/VAR_046386|||http://purl.uniprot.org/annotation/VSP_011015|||http://purl.uniprot.org/annotation/VSP_011016|||http://purl.uniprot.org/annotation/VSP_011017|||http://purl.uniprot.org/annotation/VSP_011018|||http://purl.uniprot.org/annotation/VSP_042493|||http://purl.uniprot.org/annotation/VSP_042494|||http://purl.uniprot.org/annotation/VSP_042495|||http://purl.uniprot.org/annotation/VSP_042496|||http://purl.uniprot.org/annotation/VSP_042497
http://togogenome.org/gene/9606:PIGBOS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2F0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect mitochondrial location but reduces interaction with CLCC1.|||Does not affect mitochondrial location or interaction with CLCC1.|||Helical|||Mitochondrial intermembrane|||Protein PIGBOS1|||Required for interaction with CLCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433799
http://togogenome.org/gene/9606:NSMCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV22                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Interaction with NSMCE3|||Non-structural maintenance of chromosomes element 1 homolog|||Phosphoserine|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270944|||http://purl.uniprot.org/annotation/VAR_029822|||http://purl.uniprot.org/annotation/VAR_029823
http://togogenome.org/gene/9606:SMCO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRQ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Single-pass membrane and coiled-coil domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087319
http://togogenome.org/gene/9606:PRKDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78527                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2638.|||Alleviates phosphorylation, leaves a fully active enzyme with compromised cellular resistance to ionizing radiation without affecting DNA end joining; when associated with A-2647.|||Catalytic loop|||Cleavage; by caspase-3|||DNA-dependent protein kinase catalytic subunit|||Disordered|||FAT|||FATC|||G-loop|||HEAT 1|||HEAT 2|||In IMD26; shows impaired function in response to irradiation and a less severe defect in V(D)J end-joining suggesting that the missense mutation retained some functional capacity; consistent with a loss of function mutation.|||In IMD26; shows increased long palindromic (P)-nucleotide stretches in the immunoglobulin coding joints indicating a defect in hairpin opening and insufficient DCLRE1C activation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Interaction with C1D|||KIP-binding|||Leads to radiation sensitivity and impaired DSB joining. Gives rise to reduced phosphorylation; when associated with A-2612.|||Leucine-zipper|||Loss of interaction with C1D.|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Reduced phosphorylation; when associated with A-2609.|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225598|||http://purl.uniprot.org/annotation/VAR_019179|||http://purl.uniprot.org/annotation/VAR_019180|||http://purl.uniprot.org/annotation/VAR_019181|||http://purl.uniprot.org/annotation/VAR_019182|||http://purl.uniprot.org/annotation/VAR_019183|||http://purl.uniprot.org/annotation/VAR_019184|||http://purl.uniprot.org/annotation/VAR_019185|||http://purl.uniprot.org/annotation/VAR_019186|||http://purl.uniprot.org/annotation/VAR_019187|||http://purl.uniprot.org/annotation/VAR_019188|||http://purl.uniprot.org/annotation/VAR_019189|||http://purl.uniprot.org/annotation/VAR_019190|||http://purl.uniprot.org/annotation/VAR_019191|||http://purl.uniprot.org/annotation/VAR_019192|||http://purl.uniprot.org/annotation/VAR_019193|||http://purl.uniprot.org/annotation/VAR_019194|||http://purl.uniprot.org/annotation/VAR_019195|||http://purl.uniprot.org/annotation/VAR_019196|||http://purl.uniprot.org/annotation/VAR_019197|||http://purl.uniprot.org/annotation/VAR_019198|||http://purl.uniprot.org/annotation/VAR_041602|||http://purl.uniprot.org/annotation/VAR_041603|||http://purl.uniprot.org/annotation/VAR_041604|||http://purl.uniprot.org/annotation/VAR_041605|||http://purl.uniprot.org/annotation/VAR_041606|||http://purl.uniprot.org/annotation/VAR_041607|||http://purl.uniprot.org/annotation/VAR_041608|||http://purl.uniprot.org/annotation/VAR_041609|||http://purl.uniprot.org/annotation/VAR_041610|||http://purl.uniprot.org/annotation/VAR_041611|||http://purl.uniprot.org/annotation/VAR_041612|||http://purl.uniprot.org/annotation/VAR_041613|||http://purl.uniprot.org/annotation/VAR_041614|||http://purl.uniprot.org/annotation/VAR_041615|||http://purl.uniprot.org/annotation/VAR_041616|||http://purl.uniprot.org/annotation/VAR_041617|||http://purl.uniprot.org/annotation/VAR_041618|||http://purl.uniprot.org/annotation/VAR_041619|||http://purl.uniprot.org/annotation/VAR_041620|||http://purl.uniprot.org/annotation/VAR_041621|||http://purl.uniprot.org/annotation/VAR_041622|||http://purl.uniprot.org/annotation/VAR_050534|||http://purl.uniprot.org/annotation/VAR_072569|||http://purl.uniprot.org/annotation/VAR_072570|||http://purl.uniprot.org/annotation/VSP_004708
http://togogenome.org/gene/9606:MYEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2K5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Myelin expression factor 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081655|||http://purl.uniprot.org/annotation/VAR_052209|||http://purl.uniprot.org/annotation/VAR_052210|||http://purl.uniprot.org/annotation/VAR_061829|||http://purl.uniprot.org/annotation/VSP_013451|||http://purl.uniprot.org/annotation/VSP_013452|||http://purl.uniprot.org/annotation/VSP_013453|||http://purl.uniprot.org/annotation/VSP_013454
http://togogenome.org/gene/9606:VAV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKW4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Calponin-homology (CH)|||DH|||Guanine nucleotide exchange factor VAV3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phorbol-ester/DAG-type|||Phosphotyrosine|||SH2|||SH3 1|||SH3 2|||Sufficient for interaction with ROS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080986|||http://purl.uniprot.org/annotation/VAR_033522|||http://purl.uniprot.org/annotation/VAR_033523|||http://purl.uniprot.org/annotation/VAR_051998|||http://purl.uniprot.org/annotation/VAR_061800|||http://purl.uniprot.org/annotation/VSP_001820|||http://purl.uniprot.org/annotation/VSP_041360|||http://purl.uniprot.org/annotation/VSP_041361|||http://purl.uniprot.org/annotation/VSP_042359
http://togogenome.org/gene/9606:ZNF417                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R230|||http://purl.uniprot.org/uniprot/Q8TAU3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 417                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233985|||http://purl.uniprot.org/annotation/VAR_060275|||http://purl.uniprot.org/annotation/VSP_055950
http://togogenome.org/gene/9606:CA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00915|||http://purl.uniprot.org/uniprot/V9HWE3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 1|||Disordered|||In Guam.|||In variant Michigan-1; confers enhanced esterase activity and an additional zinc binding site.|||N-acetylalanine|||Proton donor/acceptor|||Removed|||in variant Michigan-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077409|||http://purl.uniprot.org/annotation/VAR_001378|||http://purl.uniprot.org/annotation/VAR_001379|||http://purl.uniprot.org/annotation/VAR_048679
http://togogenome.org/gene/9606:CHRM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08173                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Muscarinic acetylcholine receptor M4|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069037
http://togogenome.org/gene/9606:MYO16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W883|||http://purl.uniprot.org/uniprot/Q9Y6X6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Actin-binding|||Basic and acidic residues|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||IQ|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Involved in CYFIP1- and NCKAP1-binding|||Myosin motor|||Polar residues|||Pro residues|||Unconventional myosin-XVI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289136|||http://purl.uniprot.org/annotation/VAR_032584|||http://purl.uniprot.org/annotation/VAR_032585|||http://purl.uniprot.org/annotation/VAR_050214|||http://purl.uniprot.org/annotation/VAR_050215|||http://purl.uniprot.org/annotation/VAR_050216|||http://purl.uniprot.org/annotation/VAR_064737|||http://purl.uniprot.org/annotation/VAR_088422|||http://purl.uniprot.org/annotation/VAR_088423|||http://purl.uniprot.org/annotation/VSP_052447|||http://purl.uniprot.org/annotation/VSP_052448|||http://purl.uniprot.org/annotation/VSP_052449|||http://purl.uniprot.org/annotation/VSP_052450|||http://purl.uniprot.org/annotation/VSP_052451
http://togogenome.org/gene/9606:HS3ST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y278                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 2|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085214|||http://purl.uniprot.org/annotation/VAR_052530
http://togogenome.org/gene/9606:WDSUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZF2|||http://purl.uniprot.org/uniprot/Q8N9V3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphothreonine|||SAM|||U-box|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat, SAM and U-box domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278608|||http://purl.uniprot.org/annotation/VAR_030791|||http://purl.uniprot.org/annotation/VAR_030792|||http://purl.uniprot.org/annotation/VAR_030793|||http://purl.uniprot.org/annotation/VSP_023337
http://togogenome.org/gene/9606:GKN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KHR1|||http://purl.uniprot.org/uniprot/Q53YU7|||http://purl.uniprot.org/uniprot/Q9NS71                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BRICHOS|||Gastrokine-1|||In a breast cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021332|||http://purl.uniprot.org/annotation/PRO_5010843964|||http://purl.uniprot.org/annotation/VAR_035923
http://togogenome.org/gene/9606:FCRL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 3|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||No effect on inhibition of cell death. No effect on interaction with INPP5D, PTPN6 and PTPN11. Loss of phosphorylation, calcium influx inhibition and interaction with INPP5D, PTPN6 and PTPN11; when associated with F-650; F-662 and F-692. Alters binding with PTPN6 and PTPN11; when associated with F-692. Decreases calcium influx inhibition; when associated with F-650 and F-662. Decreases calcium influx inhibition; when associated with F-650 and F-692. Decreases calcium influx inhibition; when associated with F-692.|||No effect on inhibition of cell death. No effect on interaction with INPP5D, PTPN6 and PTPN11. Loss of phosphorylation, calcium influx inhibition and interaction with INPP5D, PTPN6 and PTPN11; when associated with F-662; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-662. Decreases calcium influx inhibition; when associated with F-662 and F-722. Decreases calcium influx inhibition; when associated with F-692 and F-722.|||Partially reduces inhibition of cell death. Decreases interaction with INPP5D and PTPN11. No effect on interaction with PTPN6. Loss of phosphorylation, calcium influx inhibition and interaction with INPP5D, PTPN6 and PTPN11; when associated with F-650; F-662 and F-722. Alters binding with PTPN6 and PTPN11; when associated with F-772. Decreases calcium influx inhibition; when associated with F-650 and F-722. Increases calcium influx inhibition; when associated with F-650 and F-662. Decreases calcium influx inhibition; when associated with F-722.|||Phosphotyrosine|||Polar residues|||Reduces inhibition of cell death. Decreases interaction with INPP5D and PTPN6. No effect on interaction with PTPN11. Loss of phosphorylation, calcium influx inhibition and interaction with INPP5D, PTPN6 and PTPN11; when associated with F-650; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-650. Decreases calcium influx inhibition; when associated with F-650 and F-722. Increases calcium influx inhibition; when associated with F-650 and F-722.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331640|||http://purl.uniprot.org/annotation/VAR_042924|||http://purl.uniprot.org/annotation/VAR_042925|||http://purl.uniprot.org/annotation/VAR_042926|||http://purl.uniprot.org/annotation/VAR_042927|||http://purl.uniprot.org/annotation/VAR_042928|||http://purl.uniprot.org/annotation/VSP_033300|||http://purl.uniprot.org/annotation/VSP_033301|||http://purl.uniprot.org/annotation/VSP_033302|||http://purl.uniprot.org/annotation/VSP_033303|||http://purl.uniprot.org/annotation/VSP_033304|||http://purl.uniprot.org/annotation/VSP_033305|||http://purl.uniprot.org/annotation/VSP_033306|||http://purl.uniprot.org/annotation/VSP_033307|||http://purl.uniprot.org/annotation/VSP_033308
http://togogenome.org/gene/9606:EPHX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUS5                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Epoxide hydrolase 4|||Helical; Signal-anchor for type II membrane protein|||Nucleophile|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281378|||http://purl.uniprot.org/annotation/VAR_031235
http://togogenome.org/gene/9606:AASDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFZ3|||http://purl.uniprot.org/uniprot/B4E195|||http://purl.uniprot.org/uniprot/B4E2K0|||http://purl.uniprot.org/uniprot/B7ZAI1|||http://purl.uniprot.org/uniprot/Q4L235|||http://purl.uniprot.org/uniprot/R4GNB1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Beta-alanine-activating enzyme|||Carrier|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315803|||http://purl.uniprot.org/annotation/VAR_038309|||http://purl.uniprot.org/annotation/VAR_038310|||http://purl.uniprot.org/annotation/VAR_038311|||http://purl.uniprot.org/annotation/VAR_038312|||http://purl.uniprot.org/annotation/VAR_038313|||http://purl.uniprot.org/annotation/VAR_061008|||http://purl.uniprot.org/annotation/VAR_061009|||http://purl.uniprot.org/annotation/VSP_030707|||http://purl.uniprot.org/annotation/VSP_030710|||http://purl.uniprot.org/annotation/VSP_030711|||http://purl.uniprot.org/annotation/VSP_030712|||http://purl.uniprot.org/annotation/VSP_030713
http://togogenome.org/gene/9606:RPP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95059                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine                                                                                  ^@                                                                                  Removed|||Ribonuclease P protein subunit p14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140010
http://togogenome.org/gene/9606:BEND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXX8|||http://purl.uniprot.org/uniprot/Q8NDZ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEN|||BEN 1|||BEN 2|||BEN domain-containing protein 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079730|||http://purl.uniprot.org/annotation/VAR_022885|||http://purl.uniprot.org/annotation/VAR_050935|||http://purl.uniprot.org/annotation/VSP_044653|||http://purl.uniprot.org/annotation/VSP_044654
http://togogenome.org/gene/9606:HMCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RW7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||Hemicentin-1|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 13|||Ig-like C2-type 14|||Ig-like C2-type 15|||Ig-like C2-type 16|||Ig-like C2-type 17|||Ig-like C2-type 18|||Ig-like C2-type 19|||Ig-like C2-type 2|||Ig-like C2-type 20|||Ig-like C2-type 21|||Ig-like C2-type 22|||Ig-like C2-type 23|||Ig-like C2-type 24|||Ig-like C2-type 25|||Ig-like C2-type 26|||Ig-like C2-type 27|||Ig-like C2-type 28|||Ig-like C2-type 29|||Ig-like C2-type 3|||Ig-like C2-type 30|||Ig-like C2-type 31|||Ig-like C2-type 32|||Ig-like C2-type 33|||Ig-like C2-type 34|||Ig-like C2-type 35|||Ig-like C2-type 36|||Ig-like C2-type 37|||Ig-like C2-type 38|||Ig-like C2-type 39|||Ig-like C2-type 4|||Ig-like C2-type 40|||Ig-like C2-type 41|||Ig-like C2-type 42|||Ig-like C2-type 43|||Ig-like C2-type 44|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In ARMD1.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nidogen G2 beta-barrel|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045391|||http://purl.uniprot.org/annotation/VAR_024811|||http://purl.uniprot.org/annotation/VAR_024812|||http://purl.uniprot.org/annotation/VAR_024813|||http://purl.uniprot.org/annotation/VAR_024814|||http://purl.uniprot.org/annotation/VAR_024815|||http://purl.uniprot.org/annotation/VAR_024816|||http://purl.uniprot.org/annotation/VAR_024817|||http://purl.uniprot.org/annotation/VAR_024818|||http://purl.uniprot.org/annotation/VAR_049875|||http://purl.uniprot.org/annotation/VAR_049876|||http://purl.uniprot.org/annotation/VAR_049877|||http://purl.uniprot.org/annotation/VSP_016871|||http://purl.uniprot.org/annotation/VSP_016872|||http://purl.uniprot.org/annotation/VSP_016873|||http://purl.uniprot.org/annotation/VSP_016874
http://togogenome.org/gene/9606:ODAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1E959                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Interaction with ARHGEF5|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Odontogenic ameloblast-associated protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000183879|||http://purl.uniprot.org/annotation/VAR_039812|||http://purl.uniprot.org/annotation/VAR_039813
http://togogenome.org/gene/9606:KIF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Kinesin motor|||Kinesin-like protein KIF6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125441|||http://purl.uniprot.org/annotation/VAR_022810|||http://purl.uniprot.org/annotation/VAR_036217|||http://purl.uniprot.org/annotation/VAR_049698|||http://purl.uniprot.org/annotation/VSP_014468|||http://purl.uniprot.org/annotation/VSP_014469|||http://purl.uniprot.org/annotation/VSP_014470|||http://purl.uniprot.org/annotation/VSP_014471
http://togogenome.org/gene/9606:MTMR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QG7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with global developmental delay, spasticity and epilepsy; unknown pathological significance.|||GRAM|||In isoform 2.|||Myotubularin phosphatase|||Myotubularin-related protein 9|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094943|||http://purl.uniprot.org/annotation/VAR_082147|||http://purl.uniprot.org/annotation/VSP_056209
http://togogenome.org/gene/9606:MNDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41218|||http://purl.uniprot.org/uniprot/Q5VUU6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HIN-200|||Myeloid cell nuclear differentiation antigen|||Nuclear localization signal|||Polar residues|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153724|||http://purl.uniprot.org/annotation/VAR_012055|||http://purl.uniprot.org/annotation/VAR_020483|||http://purl.uniprot.org/annotation/VAR_034107
http://togogenome.org/gene/9606:ACTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60709                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG1|||(Microbial infection) Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG1|||Abolished methylation by SETD3.|||Actin, cytoplasmic 1|||Actin, cytoplasmic 1, N-terminally processed|||Decreased interaction with SETD3.|||Does not affect methylation by SETD3.|||Impaired methylation by SETD3.|||In BRWS1.|||In DJO; modifies cell response to latrunculin A.|||Methionine (R)-sulfoxide|||N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed|||N-acetylmethionine|||N6-methyllysine|||Removed; alternate|||Tele-methylhistidine|||Weak methylation by a A-256 or V-256 SETD3 mutant. High methylation by a F-256 and A-274 SETD3 mutant.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000771|||http://purl.uniprot.org/annotation/PRO_0000367073|||http://purl.uniprot.org/annotation/VAR_030026|||http://purl.uniprot.org/annotation/VAR_048185|||http://purl.uniprot.org/annotation/VAR_067810|||http://purl.uniprot.org/annotation/VAR_067811|||http://purl.uniprot.org/annotation/VAR_067812|||http://purl.uniprot.org/annotation/VAR_067813
http://togogenome.org/gene/9606:AQP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y2R4|||http://purl.uniprot.org/uniprot/Q92482                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-3|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063943|||http://purl.uniprot.org/annotation/VAR_025089|||http://purl.uniprot.org/annotation/VSP_003229|||http://purl.uniprot.org/annotation/VSP_003230
http://togogenome.org/gene/9606:SLC22A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15245                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Affects transporter activity; reduction of MPP(+) uptake when associated with V-408.|||Affects transporter activity; reduction of MPP(+) uptake; reduction of serum O-isobutanoyl-(R)-carnitine levels; reduction of MPP(+) uptake when associated with V-408.|||Affects transporter activity; reduction of MPP(+), serotonin and TEA uptake.|||Affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; no MPP(+) uptake when associated with L-160.|||Affects transporter activity; reduction of TEA uptake; reduction o MPP(+) uptake when associated with V-408; largely localized to the plasma membrane.|||Cytoplasmic|||Decreased TEA uptake.|||Does not affect transporter activity; no changes in MPP(+) uptake when associated with F-14; no changes in MPP(+) uptake when associated with F-85; no changes in MPP(+) uptake when associated with L-189; no changes in MPP(+) uptake when associated with H-342; no changes in MPP(+) uptake when associated with M-420 del; no changes in MPP(+) uptake when associated with I-440; no changes in MPP(+) uptake when associated with I-461; no changes in MPP(+) uptake when associated with M-488; reduction of MPP uptake when associated with C-61; no MPP(+) uptake when associated with V-220; reduction of MPP(+) uptake when associated with L-341; no MPP(+) uptake when associated with S-401; no MPP(+) uptake when associated with R-465.|||Exclusively found in the African American population; increased MPP(+) uptake when associated with V-408.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased fenoterol uptake. Increased fenoterol affinity. No change in trospium uptake. No change in terbutaline uptake. No change in terbutaline affinity.|||N-linked (GlcNAc...) asparagine|||No change in fenoterol uptake. Decreased trospium uptake. Decreased trospium affinity.|||No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.|||No changes in MPP(+) uptake when associated with V-408.|||No changes in MPP(+) uptake.|||No changes in MPP(+) uptake; when associated with V-408.|||No changes in both MPP(+) and TEA uptake; abolishes MPP(+) uptake when associated with S-401; largely localized to the plasma membrane.|||Phosphoserine|||Phosphothreonine|||Proline-rich sequence|||Reduction of serum O-isobutanoyl-(R)-carnitine levels; no change in MPP(+) uptake; no changes in MPP(+) uptake when associated with V-408.|||Reduction of the localization to the basolateral membrane; no MPP(+) uptake when associated with V-408.|||Solute carrier family 22 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333875|||http://purl.uniprot.org/annotation/VAR_043319|||http://purl.uniprot.org/annotation/VAR_043320|||http://purl.uniprot.org/annotation/VAR_043321|||http://purl.uniprot.org/annotation/VAR_043322|||http://purl.uniprot.org/annotation/VAR_043323|||http://purl.uniprot.org/annotation/VAR_043324|||http://purl.uniprot.org/annotation/VAR_043325|||http://purl.uniprot.org/annotation/VAR_043326|||http://purl.uniprot.org/annotation/VAR_043327|||http://purl.uniprot.org/annotation/VAR_043328|||http://purl.uniprot.org/annotation/VAR_043329|||http://purl.uniprot.org/annotation/VAR_043330|||http://purl.uniprot.org/annotation/VAR_043331|||http://purl.uniprot.org/annotation/VAR_043332|||http://purl.uniprot.org/annotation/VAR_043333|||http://purl.uniprot.org/annotation/VAR_043334|||http://purl.uniprot.org/annotation/VAR_043335|||http://purl.uniprot.org/annotation/VAR_043336|||http://purl.uniprot.org/annotation/VAR_043337|||http://purl.uniprot.org/annotation/VSP_033587|||http://purl.uniprot.org/annotation/VSP_033588|||http://purl.uniprot.org/annotation/VSP_033589|||http://purl.uniprot.org/annotation/VSP_033590
http://togogenome.org/gene/9606:DMAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPF5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA methyltransferase 1-associated protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079935
http://togogenome.org/gene/9606:SENP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8D3|||http://purl.uniprot.org/uniprot/Q96LD8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity.|||N-acetylmethionine|||No effect on activity.|||Nucleophile|||Protease|||Sentrin-specific protease 8|||Strongly reduces activity.|||Ubiquitin-like protease family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101727|||http://purl.uniprot.org/annotation/VAR_023705
http://togogenome.org/gene/9606:PCDHGC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In NEDGS.|||In NEDGS; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-C4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003987|||http://purl.uniprot.org/annotation/VAR_087337|||http://purl.uniprot.org/annotation/VAR_087338|||http://purl.uniprot.org/annotation/VAR_087339|||http://purl.uniprot.org/annotation/VAR_087340|||http://purl.uniprot.org/annotation/VAR_087341|||http://purl.uniprot.org/annotation/VSP_008700|||http://purl.uniprot.org/annotation/VSP_008701
http://togogenome.org/gene/9606:PRTG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VWP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protogenin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317047|||http://purl.uniprot.org/annotation/VAR_038467|||http://purl.uniprot.org/annotation/VAR_049916|||http://purl.uniprot.org/annotation/VAR_049917
http://togogenome.org/gene/9606:GLYR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49A26                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A.T hook|||Abolished stimulation of KDM1B demethylase activity, reduced affinity for histone H3 of the dimer with KDM1B, but normal KDM1B-binding.|||Basic and acidic residues|||Cytokine-like nuclear factor N-PAC|||Decreased interaction with GATA4; decreased synergistic activation of GATA4 target genes transcription; detrimental effect on cardiomyocyte differentiation.|||Dehydrogenase domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity.|||Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-219.|||Impaired KDM1B-binding and abolished stimulation of KDM1B demethylase activity; when associated with A-223.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with KDM1B|||Interaction with histone H3|||Loss of tetramerization and protein stability.|||No effect on tetramerization or protein stability.|||PWWP|||Phosphoserine|||Required to promote KDM1B demethylase activity toward histone H3K4me1 and H3K4me2|||Slightly reduced stimulation of KDM1B demethylase activity, but normal KDM1B-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312121|||http://purl.uniprot.org/annotation/VAR_037403|||http://purl.uniprot.org/annotation/VAR_037404|||http://purl.uniprot.org/annotation/VAR_037405|||http://purl.uniprot.org/annotation/VAR_086184|||http://purl.uniprot.org/annotation/VSP_029706|||http://purl.uniprot.org/annotation/VSP_029707|||http://purl.uniprot.org/annotation/VSP_029708|||http://purl.uniprot.org/annotation/VSP_038222
http://togogenome.org/gene/9606:ATCAY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5T8|||http://purl.uniprot.org/uniprot/Q86WG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Alters cleavage by CASP3.|||Basic and acidic residues|||CRAL-TRIO|||Caytaxin|||Cleavage; by CASP3|||Completely abolishes interaction with KLC1.|||Disordered|||Helical|||In ATCAY.|||In isoform 2.|||Mediates interaction with GLS|||Reduced interaction with KLC1.|||Required for interaction with KLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210767|||http://purl.uniprot.org/annotation/VAR_017164|||http://purl.uniprot.org/annotation/VSP_008748
http://togogenome.org/gene/9606:C1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13901                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with NCOR1 and NCOR2|||Interaction with NR1D1|||Nuclear nucleic acid-binding protein C1D|||Required for transcriptional repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316300|||http://purl.uniprot.org/annotation/VAR_053990
http://togogenome.org/gene/9606:PTGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X296|||http://purl.uniprot.org/uniprot/P23219                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cyclooxygenase activity.|||Aspirin-acetylated serine|||EGF-like|||For cyclooxygenase activity|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Prostaglandin G/H synthase 1|||Proton acceptor|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023868|||http://purl.uniprot.org/annotation/PRO_5030002792|||http://purl.uniprot.org/annotation/VAR_013451|||http://purl.uniprot.org/annotation/VAR_013452|||http://purl.uniprot.org/annotation/VAR_013453|||http://purl.uniprot.org/annotation/VAR_013454|||http://purl.uniprot.org/annotation/VAR_019161|||http://purl.uniprot.org/annotation/VAR_019162|||http://purl.uniprot.org/annotation/VAR_019163|||http://purl.uniprot.org/annotation/VAR_028017|||http://purl.uniprot.org/annotation/VAR_056663|||http://purl.uniprot.org/annotation/VAR_056664|||http://purl.uniprot.org/annotation/VSP_004673|||http://purl.uniprot.org/annotation/VSP_046932|||http://purl.uniprot.org/annotation/VSP_053936|||http://purl.uniprot.org/annotation/VSP_054862|||http://purl.uniprot.org/annotation/VSP_054863
http://togogenome.org/gene/9606:TRHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34981                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CHNG7; decreased affinity for TRH.|||In CHNG7; loss of thyrotropin-releasing hormone receptor activity.|||In CHNG7; loss of thyrotropin-releasing hormone receptor activity; no effect on localization to plasma membrane.|||N-linked (GlcNAc...) asparagine|||Thyrotropin-releasing hormone receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070187|||http://purl.uniprot.org/annotation/VAR_011857|||http://purl.uniprot.org/annotation/VAR_049450|||http://purl.uniprot.org/annotation/VAR_083281|||http://purl.uniprot.org/annotation/VAR_083282|||http://purl.uniprot.org/annotation/VAR_083283|||http://purl.uniprot.org/annotation/VAR_083284
http://togogenome.org/gene/9606:FGF22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVZ9|||http://purl.uniprot.org/uniprot/K7ELB9|||http://purl.uniprot.org/uniprot/Q9HCT0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor|||Fibroblast growth factor 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008996|||http://purl.uniprot.org/annotation/PRO_5005138237|||http://purl.uniprot.org/annotation/PRO_5031588720
http://togogenome.org/gene/9606:PPP3CC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48454                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Proton donor|||SAPNY motif|||Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058828|||http://purl.uniprot.org/annotation/VAR_061758|||http://purl.uniprot.org/annotation/VSP_037946|||http://purl.uniprot.org/annotation/VSP_045211
http://togogenome.org/gene/9606:MTERF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RIK9|||http://purl.uniprot.org/uniprot/Q96E29                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrion|||Transcription termination factor 3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255457|||http://purl.uniprot.org/annotation/VAR_053786|||http://purl.uniprot.org/annotation/VSP_021292|||http://purl.uniprot.org/annotation/VSP_053985
http://togogenome.org/gene/9606:IL23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPF7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interchain (with C-119 in IL12A)|||Interleukin-23 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259488
http://togogenome.org/gene/9606:KRTAP21-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI59                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Keratin-associated protein 21-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223913
http://togogenome.org/gene/9606:CDC20B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y33                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cell division cycle protein 20 homolog B|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339110|||http://purl.uniprot.org/annotation/VAR_043860|||http://purl.uniprot.org/annotation/VAR_043861|||http://purl.uniprot.org/annotation/VAR_043862|||http://purl.uniprot.org/annotation/VAR_043863|||http://purl.uniprot.org/annotation/VAR_043864|||http://purl.uniprot.org/annotation/VAR_043865|||http://purl.uniprot.org/annotation/VSP_034089|||http://purl.uniprot.org/annotation/VSP_034090|||http://purl.uniprot.org/annotation/VSP_034091|||http://purl.uniprot.org/annotation/VSP_034092|||http://purl.uniprot.org/annotation/VSP_034093|||http://purl.uniprot.org/annotation/VSP_034094|||http://purl.uniprot.org/annotation/VSP_034095
http://togogenome.org/gene/9606:THOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52888                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Thimet oligopeptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078153|||http://purl.uniprot.org/annotation/VSP_056494|||http://purl.uniprot.org/annotation/VSP_056495
http://togogenome.org/gene/9606:OR51T1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFX5|||http://purl.uniprot.org/uniprot/Q8NGJ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51T1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150763
http://togogenome.org/gene/9606:FNBP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSI7|||http://purl.uniprot.org/uniprot/Q5T0N5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||Formin-binding protein 1-like|||Impairs interaction with CDC42 and reduces CDC42-induced actin assembly.|||Impairs interaction with WASL and reduces CDC42-induced actin assembly.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||Interaction with CDC42|||Interaction with DAAM1, DIAPH1 and DIAPH2|||Interaction with DNM1|||Interaction with DNM2 and WASL|||Mediates end-to-end attachment of dimers|||Phosphoserine|||Polar residues|||REM-1|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261434|||http://purl.uniprot.org/annotation/VSP_021709|||http://purl.uniprot.org/annotation/VSP_021710|||http://purl.uniprot.org/annotation/VSP_021711
http://togogenome.org/gene/9606:OTUD7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GQQ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||Basic and acidic residues|||Catalytic|||Disordered|||Does not affect interaction with EGFR.|||Impairs interaction with EGFR.|||In isoform 2.|||Loss of deubiquitinating activity due to stabilization of the autoinhibited conformation.|||Loss of deubiquitinating activity.|||Loss of deubiquitinating activity. Increased ability to interact with polyubiquitin.|||Loss of deubiquitinating activity; when associated with N-358.|||Loss of deubiquitinating activity; when associated with S-194.|||Nuclear localization signal|||Nucleophile|||OTU|||OTU domain-containing protein 7B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||Reduces deubiquitinating activity with 'Lys-11'-linked ubiquitin chains; no effect on cleavage of 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains.|||Reduces deubiquitinating activity.|||Regulatory loop|||Stabilizes the conformation of the regulatory loop|||Strongly reduces deubiquitinating activity.|||TRAF-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188788|||http://purl.uniprot.org/annotation/VSP_046015
http://togogenome.org/gene/9606:TTC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH05|||http://purl.uniprot.org/uniprot/B4DZ42|||http://purl.uniprot.org/uniprot/Q8NEE8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tetratricopeptide repeat protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106403|||http://purl.uniprot.org/annotation/VAR_025542|||http://purl.uniprot.org/annotation/VAR_025543|||http://purl.uniprot.org/annotation/VAR_025544|||http://purl.uniprot.org/annotation/VAR_052626|||http://purl.uniprot.org/annotation/VSP_056854|||http://purl.uniprot.org/annotation/VSP_056855|||http://purl.uniprot.org/annotation/VSP_056856
http://togogenome.org/gene/9606:ATF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17544                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter.|||Basic and acidic residues|||Basic motif|||C2H2-type|||Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51.|||Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53.|||Cyclic AMP-dependent transcription factor ATF-7|||Disordered|||Essential for binding adenovirus 2 E1A|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Greatly reduced JNK2- or adenovirus E1A-mediated transactivation. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-51; A-53 and G-101.|||In isoform 2 and isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 3.|||Leucine-zipper|||No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness.|||No effect on transactivation; when associated with A-145.|||No effect on transactivation; when associated with A-147.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK11|||Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-51. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-51 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and G-101.|||Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-53. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-53 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-53 and G-101.|||Severely reduced TAF12-induced transcriptional activity; when associated with D-33.|||Severely reduced TAF12-induced transcriptional activity; when associated with S-35.|||Severely reduced TAF12-mediated enhancement of transcriptional activity.|||Some reduction in transactivation but, completely abolishes MAPK9-mediated activation. Abolishes MAPK9-mediated and greatly reduces adenovirus E1A-mediated transactivation; when associated with A-51 and A-53. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and A-53.|||Transactivation domain|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076592|||http://purl.uniprot.org/annotation/VSP_060697|||http://purl.uniprot.org/annotation/VSP_060698|||http://purl.uniprot.org/annotation/VSP_060699|||http://purl.uniprot.org/annotation/VSP_060700|||http://purl.uniprot.org/annotation/VSP_060701
http://togogenome.org/gene/9606:KLHL26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R1N0|||http://purl.uniprot.org/uniprot/M0R1P3|||http://purl.uniprot.org/uniprot/Q53HC5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 26|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242688|||http://purl.uniprot.org/annotation/VAR_026861
http://togogenome.org/gene/9606:KCTD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFT7|||http://purl.uniprot.org/uniprot/Q693B1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ|||BTB/POZ domain-containing protein KCTD11|||In isoform 2.|||Potassium channel tetramerisation-type BTB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248591|||http://purl.uniprot.org/annotation/VAR_027354|||http://purl.uniprot.org/annotation/VSP_044086
http://togogenome.org/gene/9606:MMADHC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3L0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cobalamin trafficking protein CblD|||Decreases methylcobalamin levels and mildly increases adenosylcobalamin levels.|||Decreases methylcobalamin levels, but increases adenosylcobalamin levels.|||Decreases methylcobalamin levels, but increases adenosylcobalamin levels. No effect on interaction with MMACHC.|||Decreases methylcobalamin levels.|||Decreases methylcobalamin levels. Impairs interaction with MMACHC.|||Decreases methylcobalamin levels. No effect on interaction with MMACHC.|||In MAHCD; cblD original.|||In MAHCD; cblD variant 1.|||In MAHCD; cblD variant 1; decreases methylcobalamin levels and increases adenosylcobalamin levels; no effect on interaction with MMACHC.|||In MAHCD; cblD variant 1; impairs interaction with MMACHC.|||In MAHCD; cblD variant 2.|||Marginally decreases methylcobalamin levels and strongly increases adenosylcobalamin levels.|||Mildly decreases methylcobalamin levels and strongly increases adenosylcobalamin levels.|||Mitochondrion|||N6-acetyllysine|||No effect on cobalamin levels.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019534|||http://purl.uniprot.org/annotation/VAR_043843|||http://purl.uniprot.org/annotation/VAR_043844|||http://purl.uniprot.org/annotation/VAR_043845|||http://purl.uniprot.org/annotation/VAR_043846|||http://purl.uniprot.org/annotation/VAR_043847
http://togogenome.org/gene/9606:CARD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H257                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished homooligomerization and formation of BCL10-nucleating filaments.|||Basic and acidic residues|||CARD|||Caspase recruitment domain-containing protein 9|||Disordered|||Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B.|||Disruption of the linker region, relieving autoinhibition and leading to activation of NF-kappa-B. Constitutively forms BCL10-nucleating filaments.|||Does not affect zinc-binbing.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IMD103.|||In IMD103; abolished homooligomerization and formation of BCL10-nucleating filaments; reduced cytokine production in response to C.albicans infection; reduced production IgG antibodies in response to C.albicans infection.|||In IMD103; decreased production of cytokines in CD4(+) Th17 cells.|||In IMD103; does not affect formation of the CBM complex but impairs formation of a complex with RASGRF1.|||In IMD103; reduced cytokine production in response to C.albicans infection.|||In IMD103; reduced cytokine production in response to C.albicans infection; does not affect NF-kappa-B transcriptional activity.|||In IMD103; reduced cytokine production in response to C.albicans infection; impaired NF-kappa-B transcriptional activity.|||In IMD103; reduced cytokine production in response to C.albicans infection; impaired NF-kappa-B transcriptional activity; reduced production IgG antibodies in response to C.albicans infection.|||In IMD103; reduced production IgG antibodies in response to C.albicans infection.|||In isoform 2.|||In isoform 3.|||Linker|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CK2|||Reduced cytokine production in response to C.albicans infection. Impaired NF-kappa-B transcriptional activity. Does not affect interaction with BCL10.|||Strongly reduced zinc-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144082|||http://purl.uniprot.org/annotation/VAR_048607|||http://purl.uniprot.org/annotation/VAR_070828|||http://purl.uniprot.org/annotation/VAR_070829|||http://purl.uniprot.org/annotation/VAR_070830|||http://purl.uniprot.org/annotation/VAR_084630|||http://purl.uniprot.org/annotation/VAR_084631|||http://purl.uniprot.org/annotation/VAR_084632|||http://purl.uniprot.org/annotation/VAR_084633|||http://purl.uniprot.org/annotation/VAR_084634|||http://purl.uniprot.org/annotation/VAR_084635|||http://purl.uniprot.org/annotation/VAR_084636|||http://purl.uniprot.org/annotation/VAR_084637|||http://purl.uniprot.org/annotation/VAR_084638|||http://purl.uniprot.org/annotation/VAR_084639|||http://purl.uniprot.org/annotation/VAR_084640|||http://purl.uniprot.org/annotation/VAR_084641|||http://purl.uniprot.org/annotation/VAR_084642|||http://purl.uniprot.org/annotation/VSP_024390|||http://purl.uniprot.org/annotation/VSP_024391|||http://purl.uniprot.org/annotation/VSP_024392|||http://purl.uniprot.org/annotation/VSP_024393
http://togogenome.org/gene/9606:MSTO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUK6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In MMYAT; autosomal dominant; patient cells show decreased mitochondrial fusion and mitochondrial network formation; patient cells show increased mitochondria aggregation and fragmentation.|||In MMYAT; unknown pathological significance.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Protein misato homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304626|||http://purl.uniprot.org/annotation/VAR_035046|||http://purl.uniprot.org/annotation/VAR_079889|||http://purl.uniprot.org/annotation/VAR_079890|||http://purl.uniprot.org/annotation/VAR_079891|||http://purl.uniprot.org/annotation/VSP_028049|||http://purl.uniprot.org/annotation/VSP_028050|||http://purl.uniprot.org/annotation/VSP_028051|||http://purl.uniprot.org/annotation/VSP_028052|||http://purl.uniprot.org/annotation/VSP_028053|||http://purl.uniprot.org/annotation/VSP_028054|||http://purl.uniprot.org/annotation/VSP_028055|||http://purl.uniprot.org/annotation/VSP_028056
http://togogenome.org/gene/9606:MAP1LC3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXW4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by ATG4B|||Impaired phosphorylation by TBK1.|||Microtubule-associated proteins 1A/1B light chain 3C|||No processing of precursor.|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Phospho-mimetic mutant; impaired interaction with ATG4 proteins, preventing cleavage at the C-terminus, conjugation to phosphatidylethanolamine and localization to autophagosomes.|||Phosphoserine; by TBK1|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017204|||http://purl.uniprot.org/annotation/PRO_0000017205
http://togogenome.org/gene/9606:AP1M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNH5|||http://purl.uniprot.org/uniprot/Q59EK3|||http://purl.uniprot.org/uniprot/Q9BXS5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-1 complex subunit mu-1|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||MHD|||N-acetylserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193770|||http://purl.uniprot.org/annotation/VAR_036536|||http://purl.uniprot.org/annotation/VSP_042542
http://togogenome.org/gene/9606:SIRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K128|||http://purl.uniprot.org/uniprot/B0QZ35|||http://purl.uniprot.org/uniprot/E9PC49|||http://purl.uniprot.org/uniprot/Q96EB6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation at Ser-47, restores deacetylation activity and inhibits DNA damage-induced apoptosis.|||Acidic residues|||Basic and acidic residues|||Blocks residue phosphorylation, restores deacetylation activity and inhibits DNA damage-induced apoptosis.|||Deacetylase sirtuin-type|||Disordered|||Greatly diminishes phosphorylation by MAPK8; when associated with A-27 and A-47.|||Greatly diminishes phosphorylation by MAPK8; when associated with A-27 and A-530.|||Greatly diminishes phosphorylation by MAPK8; when associated with A-47 and A-530.|||Impairs in vitro methylation by SETD7; when associated with R-233, R-235 and R-238.|||Impairs in vitro methylation by SETD7; when associated with R-233, R-235a and R-236.|||Impairs in vitro methylation by SETD7; when associated with R-233, R-236 and R-238.|||Impairs in vitro methylation by SETD7; when associated with R-235, R-236 and R-238.|||In isoform 2.|||Interaction with CCAR2|||Interaction with CLOCK|||Interaction with H1-4|||Loss of function; abolishes both protein deacetylase and decrotonylase activities. Reduces the interaction with CCAR2 and APEX1. Increases acetylation of APEX1.|||Loss of interaction with the sumoylated form of CCAR2. No effect on its deacetylation activity.|||N-acetylalanine|||N6-acetyllysine|||NAD-dependent protein deacetylase sirtuin-1|||No effect on phosphorylation (in vitro and in vivo).|||Nuclear export signal|||Nuclear localization signal|||Phosphorylated at one of three serine residues|||Phosphoserine|||Phosphoserine; by CaMK2|||Phosphoserine; by MAPK8|||Phosphothreonine|||Phosphothreonine; by DYRK1A, DYRK3 and MAPK8|||Polar residues|||Proton acceptor|||Reduces in vitro phosphorylation by CDK1. Impairs cell proliferation and cell cycle progression; when associated with A-530.|||Reduces in vitro phosphorylation by CDK1. Impairs cell proliferation and cell cycle progression; when associated with A-540.|||Reduces in vitro phosphorylation by CaMK2; when associated with S-659. Greatly reduces in vivo phosphorylation; when associated with A-659.|||Reduces in vitro phosphorylation by CaMK2; when associated with S-661. Greatly reduces in vivo phosphorylation; when associated with A-661.|||Removed|||Required for interaction with the sumoylated form of CCAR2|||S-nitrosocysteine|||SirtT1 75 kDa fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110256|||http://purl.uniprot.org/annotation/PRO_0000415289|||http://purl.uniprot.org/annotation/VAR_025148|||http://purl.uniprot.org/annotation/VAR_051976|||http://purl.uniprot.org/annotation/VSP_042189
http://togogenome.org/gene/9606:PHLDB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUD6|||http://purl.uniprot.org/uniprot/Q86UU1|||http://purl.uniprot.org/uniprot/Q8NC75                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||FHA|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology-like domain family B member 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053891|||http://purl.uniprot.org/annotation/VSP_016737|||http://purl.uniprot.org/annotation/VSP_016738|||http://purl.uniprot.org/annotation/VSP_016739|||http://purl.uniprot.org/annotation/VSP_016740
http://togogenome.org/gene/9606:ZNF668                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1I4|||http://purl.uniprot.org/uniprot/Q96K58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDGEF; increased DNA damage is detected in patient fibroblasts suggesting decreased fuction in DNA repair; no protein is detected in patient fibroblasts.|||In NEDGEF; increased DNA damage is detected in patient fibroblasts suggesting decreased fuction in DNA repair; reduced protein localization to the nucleus in patient fibroblasts.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Zinc finger protein 668                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251478|||http://purl.uniprot.org/annotation/VAR_027689|||http://purl.uniprot.org/annotation/VAR_027690|||http://purl.uniprot.org/annotation/VAR_027691|||http://purl.uniprot.org/annotation/VAR_035595|||http://purl.uniprot.org/annotation/VAR_035596|||http://purl.uniprot.org/annotation/VAR_035597|||http://purl.uniprot.org/annotation/VAR_035598|||http://purl.uniprot.org/annotation/VAR_087999|||http://purl.uniprot.org/annotation/VAR_088000|||http://purl.uniprot.org/annotation/VSP_053786
http://togogenome.org/gene/9606:LSM14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with DDX6.|||Abolished interaction with EIF4ENIF1/4E-T without affecting interaction with DDX6; when associated with E-22.|||Abolished interaction with EIF4ENIF1/4E-T without affecting interaction with DDX6; when associated with E-29.|||Asymmetric dimethylarginine|||Basic and acidic residues|||DFDF|||Disordered|||Does not affect interaction with DDX6.|||FFD box|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein LSM14 homolog A|||Removed|||Sm|||TFG box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187090|||http://purl.uniprot.org/annotation/VAR_022884|||http://purl.uniprot.org/annotation/VAR_057532|||http://purl.uniprot.org/annotation/VSP_014650|||http://purl.uniprot.org/annotation/VSP_057232
http://togogenome.org/gene/9606:ATP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00846|||http://purl.uniprot.org/uniprot/Q0ZFE3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ATP synthase subunit a|||Helical|||In LHON; possible rate primary mutation.|||In LS and MIBSN.|||In LS, MC5DM1 and APAO.|||In LS.|||In MLASA3.|||In NARP and LS.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082128|||http://purl.uniprot.org/annotation/VAR_000792|||http://purl.uniprot.org/annotation/VAR_000793|||http://purl.uniprot.org/annotation/VAR_000794|||http://purl.uniprot.org/annotation/VAR_000795|||http://purl.uniprot.org/annotation/VAR_000796|||http://purl.uniprot.org/annotation/VAR_000797|||http://purl.uniprot.org/annotation/VAR_008556|||http://purl.uniprot.org/annotation/VAR_008557|||http://purl.uniprot.org/annotation/VAR_008558|||http://purl.uniprot.org/annotation/VAR_008559|||http://purl.uniprot.org/annotation/VAR_008560|||http://purl.uniprot.org/annotation/VAR_008561|||http://purl.uniprot.org/annotation/VAR_008562|||http://purl.uniprot.org/annotation/VAR_021178|||http://purl.uniprot.org/annotation/VAR_021179|||http://purl.uniprot.org/annotation/VAR_021180|||http://purl.uniprot.org/annotation/VAR_021181|||http://purl.uniprot.org/annotation/VAR_021182|||http://purl.uniprot.org/annotation/VAR_021183|||http://purl.uniprot.org/annotation/VAR_021184|||http://purl.uniprot.org/annotation/VAR_021185|||http://purl.uniprot.org/annotation/VAR_021186|||http://purl.uniprot.org/annotation/VAR_021187|||http://purl.uniprot.org/annotation/VAR_021188|||http://purl.uniprot.org/annotation/VAR_021189|||http://purl.uniprot.org/annotation/VAR_021190|||http://purl.uniprot.org/annotation/VAR_021191|||http://purl.uniprot.org/annotation/VAR_021192|||http://purl.uniprot.org/annotation/VAR_021193|||http://purl.uniprot.org/annotation/VAR_073699|||http://purl.uniprot.org/annotation/VAR_073700
http://togogenome.org/gene/9606:CFHR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXR6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Complement factor H-related protein 5|||Found in a patient with atypical hemolytic uremic syndrome.|||Found in patients with atypical hemolytic uremic syndrome.|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005900|||http://purl.uniprot.org/annotation/VAR_035827|||http://purl.uniprot.org/annotation/VAR_048818|||http://purl.uniprot.org/annotation/VAR_048819|||http://purl.uniprot.org/annotation/VAR_048820|||http://purl.uniprot.org/annotation/VAR_048821|||http://purl.uniprot.org/annotation/VAR_063652|||http://purl.uniprot.org/annotation/VAR_063653|||http://purl.uniprot.org/annotation/VAR_069090|||http://purl.uniprot.org/annotation/VAR_069091|||http://purl.uniprot.org/annotation/VAR_069092
http://togogenome.org/gene/9606:YY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15391                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In a breast cancer sample; somatic mutation.|||Mediates transcriptional activation|||Mediates transcriptional repression|||Polar residues|||Transcription factor YY2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323760|||http://purl.uniprot.org/annotation/VAR_039586
http://togogenome.org/gene/9606:SPIRE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AE8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with FMN2.|||Disordered|||Important for interaction with FMN2|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||KIND|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein spire homolog 1|||Removed|||Spir-box|||Strongly reduces interaction with FMN2.|||WH2 1|||WH2 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309569|||http://purl.uniprot.org/annotation/VAR_058695|||http://purl.uniprot.org/annotation/VSP_037925|||http://purl.uniprot.org/annotation/VSP_037926|||http://purl.uniprot.org/annotation/VSP_052595|||http://purl.uniprot.org/annotation/VSP_054464
http://togogenome.org/gene/9606:RNF148                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7C7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||PA|||RING finger protein 148|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255252|||http://purl.uniprot.org/annotation/VAR_028855
http://togogenome.org/gene/9606:C2orf49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J4K0|||http://purl.uniprot.org/uniprot/Q9BVC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ashwin|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268859|||http://purl.uniprot.org/annotation/VAR_029759|||http://purl.uniprot.org/annotation/VSP_054353|||http://purl.uniprot.org/annotation/VSP_054354
http://togogenome.org/gene/9606:HAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92819                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes hyaluronan synthase activity.|||Completely abolishes hyaluronan synthase activity. Cumulates at plasma membrane.|||Completely abolishes hyaluronan synthase activity. Not detected in cytoplasmic vesicles nor at cell membrane. Inability to travel from ER to Golgi. Unresponsive to AMPK-mediated inactivation.|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hyaluronan synthase 2|||Increases protein degradation. Abolishes hyaluronan synthase activity. Does not affect subcellular location.|||O-linked (GlcNAc) serine|||Phosphothreonine|||Prevents O-GlcNAcylation. Increases protein stability. Reduces hyaluronan synthase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197173
http://togogenome.org/gene/9606:DDX25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYS3|||http://purl.uniprot.org/uniprot/Q9UHL0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX25|||DEAD box|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030813|||http://purl.uniprot.org/annotation/VSP_018875
http://togogenome.org/gene/9606:OR4B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVH6|||http://purl.uniprot.org/uniprot/Q8NGF8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150528|||http://purl.uniprot.org/annotation/VAR_034189|||http://purl.uniprot.org/annotation/VAR_034190
http://togogenome.org/gene/9606:PSMA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK43|||http://purl.uniprot.org/uniprot/P25788                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Found in a patient with Nakajo syndrome who also carries a mutation in PSMB8; unknown pathological significance; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome.|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124091|||http://purl.uniprot.org/annotation/VAR_075259|||http://purl.uniprot.org/annotation/VSP_005280
http://togogenome.org/gene/9606:NCAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15394                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015018|||http://purl.uniprot.org/annotation/VAR_047897|||http://purl.uniprot.org/annotation/VAR_047898|||http://purl.uniprot.org/annotation/VSP_056637|||http://purl.uniprot.org/annotation/VSP_056638|||http://purl.uniprot.org/annotation/VSP_056639
http://togogenome.org/gene/9606:TP53TG3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:HDHD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXW7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Haloacid dehalogenase-like hydrolase domain-containing 5|||In isoform 1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020920|||http://purl.uniprot.org/annotation/VAR_033674|||http://purl.uniprot.org/annotation/VAR_050790|||http://purl.uniprot.org/annotation/VAR_050791|||http://purl.uniprot.org/annotation/VSP_003840
http://togogenome.org/gene/9606:URM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTM9                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  1-thioglycine|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||In isoform 2.|||In isoform 3.|||Ubiquitin-related modifier 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089714|||http://purl.uniprot.org/annotation/VSP_040026|||http://purl.uniprot.org/annotation/VSP_054296
http://togogenome.org/gene/9606:ARRDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEK1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Arrestin domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309620
http://togogenome.org/gene/9606:CFAP73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFT4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343715
http://togogenome.org/gene/9606:ACOT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPJ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 13|||Acyl-coenzyme A thioesterase 13, N-terminally processed|||Decreases affinity for substrate.|||In isoform 2.|||Loss of acyl-CoA hydrolase activity.|||N-acetylmethionine|||N-acetylthreonine; in Acyl-coenzyme A thioesterase 13, N-terminally processed|||N6-acetyllysine|||Reduced acyl-CoA hydrolase activity.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156697|||http://purl.uniprot.org/annotation/PRO_0000424501|||http://purl.uniprot.org/annotation/VSP_046101
http://togogenome.org/gene/9606:RNF183                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D59                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes autoubiquitination; when associated with A-13.|||Abolishes autoubiquitination; when associated with A-59.|||Cytoplasmic|||E3 ubiquitin-protein ligase RNF183|||Helical; Anchor for type IV membrane protein|||Loss of autoubiquitination and reduced ubiquitination of BCL2L1; when associated with S-13.|||Loss of autoubiquitination and reduced ubiquitination of BCL2L1; when associated with S-16.|||Loss of autoubiquitination but no effect on ubiquitination of BCL2L1; when associated with R-101 and R-105.|||Loss of autoubiquitination but no effect on ubiquitination of BCL2L1; when associated with R-28 and R-101.|||Loss of autoubiquitination but no effect on ubiquitination of BCL2L1; when associated with R-28 and R-105.|||Lumenal|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247358|||http://purl.uniprot.org/annotation/VAR_027095|||http://purl.uniprot.org/annotation/VAR_027096
http://togogenome.org/gene/9606:FAM156B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein FAM156A/FAM156B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244468
http://togogenome.org/gene/9606:UBE2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969M7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with UBA3|||N-acetylmethionine|||NEDD8-conjugating enzyme UBE2F|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263077|||http://purl.uniprot.org/annotation/VSP_037270|||http://purl.uniprot.org/annotation/VSP_037271|||http://purl.uniprot.org/annotation/VSP_037272|||http://purl.uniprot.org/annotation/VSP_037273|||http://purl.uniprot.org/annotation/VSP_037274|||http://purl.uniprot.org/annotation/VSP_055749|||http://purl.uniprot.org/annotation/VSP_055750
http://togogenome.org/gene/9606:VMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5L0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Vitelline membrane outer layer protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036407|||http://purl.uniprot.org/annotation/VAR_034584|||http://purl.uniprot.org/annotation/VAR_053736|||http://purl.uniprot.org/annotation/VSP_045706|||http://purl.uniprot.org/annotation/VSP_045707|||http://purl.uniprot.org/annotation/VSP_045708|||http://purl.uniprot.org/annotation/VSP_047219
http://togogenome.org/gene/9606:MCM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4A5|||http://purl.uniprot.org/uniprot/C6EMX8|||http://purl.uniprot.org/uniprot/P33993                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||DNA replication licensing factor MCM7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with ATRIP|||Interaction with RAD17|||MCM|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194119|||http://purl.uniprot.org/annotation/VAR_013297|||http://purl.uniprot.org/annotation/VAR_014817|||http://purl.uniprot.org/annotation/VAR_029243|||http://purl.uniprot.org/annotation/VSP_003205|||http://purl.uniprot.org/annotation/VSP_044310
http://togogenome.org/gene/9606:CTXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C2S0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Cortexin-2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284616
http://togogenome.org/gene/9606:NUDT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50583                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]|||In IDDPN.|||N-acetylalanine|||Nudix box|||Nudix hydrolase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057102|||http://purl.uniprot.org/annotation/VAR_087119
http://togogenome.org/gene/9606:KRT75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95678                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In LAHS.|||Keratin, type II cytoskeletal 75|||Linker 1|||Linker 12|||May increase risk to develop PFB; the variant is disruptive at late stages of filament assembly compromising the aggregation of keratin molecules into intermediate filaments.|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314887|||http://purl.uniprot.org/annotation/VAR_038098|||http://purl.uniprot.org/annotation/VAR_038099|||http://purl.uniprot.org/annotation/VAR_038100|||http://purl.uniprot.org/annotation/VAR_038101|||http://purl.uniprot.org/annotation/VAR_038102|||http://purl.uniprot.org/annotation/VAR_038103|||http://purl.uniprot.org/annotation/VAR_038104|||http://purl.uniprot.org/annotation/VAR_038105|||http://purl.uniprot.org/annotation/VAR_038106|||http://purl.uniprot.org/annotation/VAR_038107|||http://purl.uniprot.org/annotation/VAR_038108
http://togogenome.org/gene/9606:ATOH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0H4|||http://purl.uniprot.org/uniprot/Q8N100                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Abolishes heterodimerization with TCF3 isoform E47; no effect on nuclear localization.|||BHLH|||Does not affect DNA-binding activity or transcription activation.|||Found in a sporadic case of optic nerve hypoplasia; unknown pathological significance; does not affect DNA-binding activity but reduces transcription activation.|||Found in patients with bilateral optic nerve hypoplasia; unknown pathological significance; abolishes heterodimerization with TCF3 E47 isoform; reduces DNA-binding ability and abolishes transcriptional activation; no effect on nuclear localization.|||In PHPVAR.|||In PHPVAR; loss of function; polypeptide is stable, but does not bind DNA or activate transcription; does not restore retinal ganglion cell development in retinal explants from a mouse Atoh7 null mutant; abolishes heterodimerization with TCF3 E47 isoform; reduces DNA-binding ability and abolishes transcriptional activation; no effect on nuclear localization.|||In PHPVAR; unknown pathological significance.|||Loss of DNA-binding activity; loss of ability to restore retinal ganglion cell development in retinal explants from a mouse Atoh7 null mutant.|||Transcription factor ATOH7|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292406|||http://purl.uniprot.org/annotation/VAR_072398|||http://purl.uniprot.org/annotation/VAR_072399|||http://purl.uniprot.org/annotation/VAR_072400|||http://purl.uniprot.org/annotation/VAR_072401|||http://purl.uniprot.org/annotation/VAR_085727|||http://purl.uniprot.org/annotation/VAR_085728|||http://purl.uniprot.org/annotation/VAR_085729|||http://purl.uniprot.org/annotation/VAR_085730|||http://purl.uniprot.org/annotation/VAR_085731
http://togogenome.org/gene/9606:NUAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0Y5|||http://purl.uniprot.org/uniprot/Q9H093                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ANPH2; no effect on protein abundance; loss of protein serine/threonine kinase activity; loss of autophosphorylation at T-208; loss of function in regulation of hippo signaling.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In an ovarian Endometrioid carcinoma sample; somatic mutation.|||Loss of autophosphorylation, kinase activity and of anti-apoptotic activity.|||N-acetylmethionine|||NUAK family SNF1-like kinase 2|||Phosphoserine|||Phosphothreonine; by LKB1|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247756|||http://purl.uniprot.org/annotation/VAR_040964|||http://purl.uniprot.org/annotation/VAR_040965|||http://purl.uniprot.org/annotation/VAR_040966|||http://purl.uniprot.org/annotation/VAR_040967|||http://purl.uniprot.org/annotation/VAR_040968|||http://purl.uniprot.org/annotation/VAR_086106
http://togogenome.org/gene/9606:SUN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5G938|||http://purl.uniprot.org/uniprot/O94901                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  EMD-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Interchain (with KASH domain-containing nesprins)|||LMNA-binding|||Nuclear|||Perinuclear space|||Phosphoserine|||SUN|||SUN domain-containing protein 1|||SYNE2-binding|||Sufficient for interaction with SYNE1 and SYNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218911|||http://purl.uniprot.org/annotation/VAR_059828|||http://purl.uniprot.org/annotation/VAR_071065|||http://purl.uniprot.org/annotation/VAR_071066|||http://purl.uniprot.org/annotation/VSP_061216|||http://purl.uniprot.org/annotation/VSP_061217|||http://purl.uniprot.org/annotation/VSP_061218|||http://purl.uniprot.org/annotation/VSP_061219|||http://purl.uniprot.org/annotation/VSP_061220|||http://purl.uniprot.org/annotation/VSP_061221|||http://purl.uniprot.org/annotation/VSP_061222|||http://purl.uniprot.org/annotation/VSP_061223|||http://purl.uniprot.org/annotation/VSP_061224|||http://purl.uniprot.org/annotation/VSP_061225|||http://purl.uniprot.org/annotation/VSP_061226
http://togogenome.org/gene/9606:RAB3IL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBN0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Guanine nucleotide exchange factor for Rab-3A|||In isoform 2.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305295|||http://purl.uniprot.org/annotation/VAR_035203|||http://purl.uniprot.org/annotation/VAR_035204|||http://purl.uniprot.org/annotation/VSP_028344|||http://purl.uniprot.org/annotation/VSP_028345
http://togogenome.org/gene/9606:NCCRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||F-box only protein 50|||FBA|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326028
http://togogenome.org/gene/9606:ARPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6K5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Arpin|||In isoform C15orf38-AP3S2.|||Necessary and sufficient for interaction with ARPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244265|||http://purl.uniprot.org/annotation/VSP_047416
http://togogenome.org/gene/9606:FAM118A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWS6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Protein FAM118A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079572|||http://purl.uniprot.org/annotation/VAR_022808|||http://purl.uniprot.org/annotation/VAR_022809|||http://purl.uniprot.org/annotation/VSP_056990
http://togogenome.org/gene/9606:MED8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G25                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Impairs interaction with the Elongin BC complex; when associated with F-147.|||Impairs interaction with the Elongin BC complex; when associated with P-143.|||In isoform 2.|||In isoform 3.|||Interaction with the Elongin BC complex|||Mediator of RNA polymerase II transcription subunit 8|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096394|||http://purl.uniprot.org/annotation/VSP_007524|||http://purl.uniprot.org/annotation/VSP_035507
http://togogenome.org/gene/9606:TAMALIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with PSCD3|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues|||Protein TAMALIN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087584|||http://purl.uniprot.org/annotation/VSP_015707|||http://purl.uniprot.org/annotation/VSP_015708
http://togogenome.org/gene/9606:SLC2A4RG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Cytoplasmic; when associated with A-273.|||Cytoplasmic; when associated with A-276.|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Nuclear localization signal|||Nuclear; when associated with A-257.|||Nuclear; when associated with A-260.|||Phosphoserine|||Polar residues|||SLC2A4 regulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047208|||http://purl.uniprot.org/annotation/VAR_025005|||http://purl.uniprot.org/annotation/VSP_055908|||http://purl.uniprot.org/annotation/VSP_055909
http://togogenome.org/gene/9606:TMEM259                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTL0|||http://purl.uniprot.org/uniprot/Q4ZIN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Membralin|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096273|||http://purl.uniprot.org/annotation/VSP_014377|||http://purl.uniprot.org/annotation/VSP_014378
http://togogenome.org/gene/9606:RWDD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EV43|||http://purl.uniprot.org/uniprot/Q6NW29                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylserine|||RWD|||RWD domain-containing protein 4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076307|||http://purl.uniprot.org/annotation/VAR_024928|||http://purl.uniprot.org/annotation/VSP_056650
http://togogenome.org/gene/9606:C6orf120                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ79|||http://purl.uniprot.org/uniprot/Q7Z4R8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) asparagine|||UPF0669 protein C6orf120                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297662|||http://purl.uniprot.org/annotation/PRO_5002800877
http://togogenome.org/gene/9606:LY6G6F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L6Z9Z3|||http://purl.uniprot.org/uniprot/Q5SQ64                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2.|||Lymphocyte antigen 6 complex locus protein G6f|||N-linked (GlcNAc...) asparagine|||No phosphorylation. No interaction with GRB2 and GRB7. No phosphorylation increase of p42/44 MAP kinase.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318923|||http://purl.uniprot.org/annotation/PRO_5014272368|||http://purl.uniprot.org/annotation/VAR_038908|||http://purl.uniprot.org/annotation/VAR_038909|||http://purl.uniprot.org/annotation/VAR_038910|||http://purl.uniprot.org/annotation/VAR_038911|||http://purl.uniprot.org/annotation/VSP_055597
http://togogenome.org/gene/9606:GGTLC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C1J8|||http://purl.uniprot.org/uniprot/Q14390                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glutathione hydrolase light chain 2|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205982|||http://purl.uniprot.org/annotation/VAR_035113|||http://purl.uniprot.org/annotation/VAR_055836
http://togogenome.org/gene/9606:OMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E52                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolished protease activity and ability to mediate cleavage of DELE1 in response to mitochondrial stress. Abolished ability to mediate cleavage of PINK1 in depolarized mitochondria.|||Abolishes ability to cleave OPA1 at S1 position.|||Cardiolipin-binding|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2.|||Metalloendopeptidase OMA1, mitochondrial|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Stress-sensor region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302809|||http://purl.uniprot.org/annotation/PRO_0000450313|||http://purl.uniprot.org/annotation/PRO_0000450314|||http://purl.uniprot.org/annotation/VAR_034958|||http://purl.uniprot.org/annotation/VAR_034959|||http://purl.uniprot.org/annotation/VAR_034960|||http://purl.uniprot.org/annotation/VAR_034961|||http://purl.uniprot.org/annotation/VAR_035708|||http://purl.uniprot.org/annotation/VAR_065755|||http://purl.uniprot.org/annotation/VAR_065756|||http://purl.uniprot.org/annotation/VAR_065757|||http://purl.uniprot.org/annotation/VSP_027958
http://togogenome.org/gene/9606:RAVER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Polar residues|||RRM 1|||RRM 2|||RRM 3|||Removed|||Ribonucleoprotein PTB-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081490|||http://purl.uniprot.org/annotation/VSP_013676
http://togogenome.org/gene/9606:AMN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP64|||http://purl.uniprot.org/uniprot/Q9BXJ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In IGS2; loss of interaction with CUBN; strongly reduced CUBN expression at the cell surface.|||In IGS2; reduced presence at the cell membrane; loss of interaction with CUBN; reduced CUBN expression at the cell surface.|||Interaction with CUBN|||Loss of expression at the cell membrane.|||Loss of interaction with CUBN and strongly reduced CUBN expression at the cell surface.|||N-linked (GlcNAc...) asparagine|||No effect.|||Protein amnionless|||Soluble protein amnionless|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020702|||http://purl.uniprot.org/annotation/PRO_0000447651|||http://purl.uniprot.org/annotation/VAR_015733|||http://purl.uniprot.org/annotation/VAR_081906|||http://purl.uniprot.org/annotation/VAR_081907
http://togogenome.org/gene/9606:ATAD3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9A4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 3B|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||N-acetylserine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084800|||http://purl.uniprot.org/annotation/VAR_048120|||http://purl.uniprot.org/annotation/VSP_015637|||http://purl.uniprot.org/annotation/VSP_015638|||http://purl.uniprot.org/annotation/VSP_015639|||http://purl.uniprot.org/annotation/VSP_015640|||http://purl.uniprot.org/annotation/VSP_015641|||http://purl.uniprot.org/annotation/VSP_015642
http://togogenome.org/gene/9606:SAMD15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1V8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||SAM|||Sterile alpha motif domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279427|||http://purl.uniprot.org/annotation/VAR_030890|||http://purl.uniprot.org/annotation/VAR_030891|||http://purl.uniprot.org/annotation/VAR_030892|||http://purl.uniprot.org/annotation/VAR_061613|||http://purl.uniprot.org/annotation/VSP_023431|||http://purl.uniprot.org/annotation/VSP_023432
http://togogenome.org/gene/9606:OR9G4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGQ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9G4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150679|||http://purl.uniprot.org/annotation/VAR_053257|||http://purl.uniprot.org/annotation/VAR_053258|||http://purl.uniprot.org/annotation/VAR_053259
http://togogenome.org/gene/9606:PHLDA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5J5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  PH|||Pleckstrin homology-like domain family A member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053902|||http://purl.uniprot.org/annotation/VAR_050515
http://togogenome.org/gene/9606:COX14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I36                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX14|||Cytoplasmic|||Helical|||In MC4DN10.|||Mitochondrial intermembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263677|||http://purl.uniprot.org/annotation/VAR_067038
http://togogenome.org/gene/9606:AZIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A70                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Antizyme inhibitor 2|||In isoform 2.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4.|||In isoform 6.|||Necessary for polyamine uptake stimulation|||Not modified                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149944|||http://purl.uniprot.org/annotation/VAR_050611|||http://purl.uniprot.org/annotation/VSP_003754|||http://purl.uniprot.org/annotation/VSP_003755|||http://purl.uniprot.org/annotation/VSP_003756|||http://purl.uniprot.org/annotation/VSP_003757|||http://purl.uniprot.org/annotation/VSP_003758
http://togogenome.org/gene/9606:DEFB107B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZN7                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006979
http://togogenome.org/gene/9606:WDR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished formation of N(7)-methylguanine in tRNAs.|||Basic and acidic residues|||Disordered|||Does not affect formation of N(7)-methylguanine in tRNAs.|||Found in a patient with lung cancer; abolished formation of N(7)-methylguanine in tRNAs.|||In GAMOS6; abolished formation of N(7)-methylguanine in tRNAs.|||In GAMOS6; unknown pathological significance.|||In MIGSB; abolished formation of N(7)-methylguanine in tRNAs.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Reduced formation of N(7)-methylguanine in tRNAs.|||Removed|||Slightly reduced formation of N(7)-methylguanine in tRNAs.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051348|||http://purl.uniprot.org/annotation/VAR_020120|||http://purl.uniprot.org/annotation/VAR_033121|||http://purl.uniprot.org/annotation/VAR_033122|||http://purl.uniprot.org/annotation/VAR_081828|||http://purl.uniprot.org/annotation/VAR_081829|||http://purl.uniprot.org/annotation/VAR_081830|||http://purl.uniprot.org/annotation/VAR_087852|||http://purl.uniprot.org/annotation/VSP_036935|||http://purl.uniprot.org/annotation/VSP_036936
http://togogenome.org/gene/9606:BAAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14032                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Abolishes N-acyltransferase activity.|||Bile acid-CoA:amino acid N-acyltransferase|||Charge relay system|||In BACD1.|||In BACD1; contrary to wild-type, undetectable expression in hepatocytes.|||In BACD1; unknown pathological significance.|||In BACD1; unknown pathological significance; contrary to wild-type, undetectable expression in hepatocytes.|||Lowers N-acyltransferase activity; enhanced thioesterase activity presumably dependent on the formation of a bile acid-enzyme covalent intermediate via a thioester bond.|||Phosphoserine|||Retains N-acyltransferase activity.|||Translocation to peroxisomes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202159|||http://purl.uniprot.org/annotation/VAR_023737|||http://purl.uniprot.org/annotation/VAR_052303|||http://purl.uniprot.org/annotation/VAR_085492|||http://purl.uniprot.org/annotation/VAR_085493|||http://purl.uniprot.org/annotation/VAR_085494|||http://purl.uniprot.org/annotation/VAR_085495
http://togogenome.org/gene/9606:SLC39A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP94                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes transport activity.|||Critical for the pH sensitivity|||Cytoplasmic|||Decreased of about 30% in transport activity.|||Decreased of about 35% in transport activity. Alters the pH and voltage modulation of the transporter.|||Decreased of about 60% in transport activity. Does not alter the substrate selectivity of SLC39A2.|||Decreased of about 60% in transport activity. Loss of pH dependence for transport activity.|||Decreased of about 78% in transport activity.|||Decreases of about 72% in transport activity.|||Does not affect pH sensitivity.|||Does not affect transport activity. Reduces affinity for H(+).|||Does not affect transport kinetics parameters. Exhibits a broader substrate selectivity.|||Does not alter the substrate selectivity of SLC39A2.|||Exhibits a broader substrate selectivity.|||Extracellular|||Helical|||In isoform 2.|||Increased of about 35% in transport activity.|||Increased of about 65% in transport activity. Does not change H(+) affinity.|||Zinc transporter ZIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068767|||http://purl.uniprot.org/annotation/VAR_020265|||http://purl.uniprot.org/annotation/VAR_020266|||http://purl.uniprot.org/annotation/VAR_020267|||http://purl.uniprot.org/annotation/VAR_055452|||http://purl.uniprot.org/annotation/VAR_057480|||http://purl.uniprot.org/annotation/VSP_046889|||http://purl.uniprot.org/annotation/VSP_046890
http://togogenome.org/gene/9606:PMAIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13794                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Alters specificity of protein interaction and enhances pro-apoptotic activity; when associated with E-35.|||Alters specificity of protein interaction and enhances pro-apoptotic activity; when associated with I-32.|||BH3|||In isoform 2.|||Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-29 and E-32.|||Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-29 and E-36.|||Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-32 and E-32.|||Phorbol-12-myristate-13-acetate-induced protein 1|||Reduced interaction with BAX.|||Required for mitochondrial location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064644|||http://purl.uniprot.org/annotation/VSP_056247
http://togogenome.org/gene/9606:HNF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E0YMI7|||http://purl.uniprot.org/uniprot/P20823                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes transcription activation.|||Dimerization|||Disordered|||HNF-p1|||Hepatocyte nuclear factor 1-alpha|||Homeobox|||Homeobox; HNF1-type|||In MODY3.|||In MODY3; abolishes interaction with PCBD1 and DNA.|||In MODY3; incomplete penetrance.|||In MODY3; no effect on interaction with PCBD1 and DNA.|||In MODY3; reduces transcription activation by about 50%.|||In MODY3; reduces transcription activation by about 80%.|||In NIDDM; loss of function in positive regulation of DNA-templated transcription.|||In T1D20 and MODY3.|||In T1D20.|||In T1D20; decreased function in positive regulation of DNA-templated transcription.|||In a black African with an atypical form of diabetes; also in an individual with hepatic adenoma and familial early-onset diabetes.|||In a hepatic adenoma sample; somatic mutation.|||In a hepatic multiple adenoma sample; somatic mutation.|||In a hepatocellular carcinoma sample; somatic mutation.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform B.|||In isoform C.|||In late-onset NIDDM.|||In late-onset NIDDM; also in an individual with hepatic hyperplasia and familial early-onset diabetes.|||In late-onset NIDDM; low penetrance; unknown pathological significance.|||Interaction with DNA|||No effect on transcription activation.|||No significant effect on transcription activation.|||Nuclear localization signal|||POU-specific atypical|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces transcription activation by 70%.|||Reduces transcription activation by 75%.|||Strong association with NIDDM susceptibility; unique to the Canadian Oji-Cree population.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049115|||http://purl.uniprot.org/annotation/VAR_003756|||http://purl.uniprot.org/annotation/VAR_003757|||http://purl.uniprot.org/annotation/VAR_003758|||http://purl.uniprot.org/annotation/VAR_003759|||http://purl.uniprot.org/annotation/VAR_003760|||http://purl.uniprot.org/annotation/VAR_003761|||http://purl.uniprot.org/annotation/VAR_007905|||http://purl.uniprot.org/annotation/VAR_007906|||http://purl.uniprot.org/annotation/VAR_010537|||http://purl.uniprot.org/annotation/VAR_010538|||http://purl.uniprot.org/annotation/VAR_010539|||http://purl.uniprot.org/annotation/VAR_010540|||http://purl.uniprot.org/annotation/VAR_010541|||http://purl.uniprot.org/annotation/VAR_010542|||http://purl.uniprot.org/annotation/VAR_010543|||http://purl.uniprot.org/annotation/VAR_010544|||http://purl.uniprot.org/annotation/VAR_010545|||http://purl.uniprot.org/annotation/VAR_010546|||http://purl.uniprot.org/annotation/VAR_010547|||http://purl.uniprot.org/annotation/VAR_010548|||http://purl.uniprot.org/annotation/VAR_010549|||http://purl.uniprot.org/annotation/VAR_010550|||http://purl.uniprot.org/annotation/VAR_010551|||http://purl.uniprot.org/annotation/VAR_010552|||http://purl.uniprot.org/annotation/VAR_010554|||http://purl.uniprot.org/annotation/VAR_010555|||http://purl.uniprot.org/annotation/VAR_010556|||http://purl.uniprot.org/annotation/VAR_010557|||http://purl.uniprot.org/annotation/VAR_010558|||http://purl.uniprot.org/annotation/VAR_010559|||http://purl.uniprot.org/annotation/VAR_010560|||http://purl.uniprot.org/annotation/VAR_010561|||http://purl.uniprot.org/annotation/VAR_010562|||http://purl.uniprot.org/annotation/VAR_010563|||http://purl.uniprot.org/annotation/VAR_010564|||http://purl.uniprot.org/annotation/VAR_010565|||http://purl.uniprot.org/annotation/VAR_010566|||http://purl.uniprot.org/annotation/VAR_010567|||http://purl.uniprot.org/annotation/VAR_010568|||http://purl.uniprot.org/annotation/VAR_010569|||http://purl.uniprot.org/annotation/VAR_010570|||http://purl.uniprot.org/annotation/VAR_010571|||http://purl.uniprot.org/annotation/VAR_010572|||http://purl.uniprot.org/annotation/VAR_010573|||http://purl.uniprot.org/annotation/VAR_012483|||http://purl.uniprot.org/annotation/VAR_012484|||http://purl.uniprot.org/annotation/VAR_012485|||http://purl.uniprot.org/annotation/VAR_012486|||http://purl.uniprot.org/annotation/VAR_033088|||http://purl.uniprot.org/annotation/VAR_033089|||http://purl.uniprot.org/annotation/VAR_033090|||http://purl.uniprot.org/annotation/VAR_033091|||http://purl.uniprot.org/annotation/VAR_033092|||http://purl.uniprot.org/annotation/VAR_033093|||http://purl.uniprot.org/annotation/VAR_033094|||http://purl.uniprot.org/annotation/VAR_033095|||http://purl.uniprot.org/annotation/VAR_033096|||http://purl.uniprot.org/annotation/VAR_063069|||http://purl.uniprot.org/annotation/VAR_079478|||http://purl.uniprot.org/annotation/VAR_079479|||http://purl.uniprot.org/annotation/VSP_002250|||http://purl.uniprot.org/annotation/VSP_002251|||http://purl.uniprot.org/annotation/VSP_002252|||http://purl.uniprot.org/annotation/VSP_002253|||http://purl.uniprot.org/annotation/VSP_047736|||http://purl.uniprot.org/annotation/VSP_047737|||http://purl.uniprot.org/annotation/VSP_047738|||http://purl.uniprot.org/annotation/VSP_047739|||http://purl.uniprot.org/annotation/VSP_053324|||http://purl.uniprot.org/annotation/VSP_053325|||http://purl.uniprot.org/annotation/VSP_053326|||http://purl.uniprot.org/annotation/VSP_054300|||http://purl.uniprot.org/annotation/VSP_054301|||http://purl.uniprot.org/annotation/VSP_054302
http://togogenome.org/gene/9606:DLX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56179                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DLX-6|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049034|||http://purl.uniprot.org/annotation/VSP_040732|||http://purl.uniprot.org/annotation/VSP_047248
http://togogenome.org/gene/9606:YWHAZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0PNI1|||http://purl.uniprot.org/uniprot/P63104                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  14-3-3|||14-3-3 protein zeta/delta|||Abolishes lamellipodia formation and induces filopodia formation.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; gain-of-function mutation in signal transduction; changed regulation of ERK1 and ERK2 cascade; increased interaction with BRAF; increased interaction with RAF1; loss of phosphorylation by CK1 at Thr-232.|||In isoform 2.|||Interaction with phosphoserine on interacting protein|||Loss of homodimerization. Reduced dimerization with YWHAE. Significantly reduced interaction with P53. No enhancement of P53 transcriptional activity.|||Loss of interaction with NOXA1.|||Loss of phosphorylation by CK1.|||Loss of sphingosine-activated PKA phosphorylation. Promotes homodimerization and heterodimerization with YWHAE. Enhanced transcriptional activity of P53.|||N-acetylmethionine|||N6-acetyllysine|||On DNA damage, loss of MAPK8-mediated phosphorylation. Loss of binding ABL1. Attenuates ABL1-mediated apoptosis. No loss of interaction with BAX under stress conditions. Inhibits translocation of BAX to mitochondria.|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphoserine; by PKA and PKB/AKT1|||Phosphothreonine; by CK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058627|||http://purl.uniprot.org/annotation/VAR_082640|||http://purl.uniprot.org/annotation/VAR_082641|||http://purl.uniprot.org/annotation/VAR_082642|||http://purl.uniprot.org/annotation/VAR_082643|||http://purl.uniprot.org/annotation/VSP_047505
http://togogenome.org/gene/9606:ETV3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN32                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||ETS|||ETS translocation variant 3-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325822|||http://purl.uniprot.org/annotation/VAR_039928|||http://purl.uniprot.org/annotation/VAR_039929|||http://purl.uniprot.org/annotation/VAR_039930|||http://purl.uniprot.org/annotation/VAR_048949
http://togogenome.org/gene/9606:EPS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3T6|||http://purl.uniprot.org/uniprot/Q12929                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Amphipathic helix|||Basic and acidic residues|||Disordered|||Effector region|||Epidermal growth factor receptor kinase substrate 8|||Helix bundle 1|||Helix bundle 2|||Helix bundle 3|||Helix bundle 4|||In isoform 2.|||PTB|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086994|||http://purl.uniprot.org/annotation/VAR_050971|||http://purl.uniprot.org/annotation/VAR_050972|||http://purl.uniprot.org/annotation/VSP_056460
http://togogenome.org/gene/9606:CCDC122                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0U0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 122|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286598|||http://purl.uniprot.org/annotation/VAR_061579|||http://purl.uniprot.org/annotation/VSP_025114
http://togogenome.org/gene/9606:MMP16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51512                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In isoform Short.|||Matrix metalloproteinase-16|||N-linked (GlcNAc...) asparagine|||Pro residues|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028812|||http://purl.uniprot.org/annotation/PRO_0000028813|||http://purl.uniprot.org/annotation/VSP_005453|||http://purl.uniprot.org/annotation/VSP_005454
http://togogenome.org/gene/9606:TMEM158                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ71                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 158                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285128|||http://purl.uniprot.org/annotation/VSP_024826
http://togogenome.org/gene/9606:GDPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GP-PDE|||Glycerophosphoinositol inositolphosphodiesterase GDPD2|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251934|||http://purl.uniprot.org/annotation/VSP_042622|||http://purl.uniprot.org/annotation/VSP_042623
http://togogenome.org/gene/9606:SYT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTZ1|||http://purl.uniprot.org/uniprot/A0A8V8TN09|||http://purl.uniprot.org/uniprot/A1L3Y1|||http://purl.uniprot.org/uniprot/Q8NB59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In SCAR11; shows intracellular localization different from that of the wild-type protein; forms a reticular pattern in the cytoplasm; does not show submembranous distribution; is abnormally retained in the endoplasmic reticulum consistent to improper folding.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 7.|||Polar residues|||Synaptotagmin-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183978|||http://purl.uniprot.org/annotation/VAR_066663|||http://purl.uniprot.org/annotation/VAR_066664|||http://purl.uniprot.org/annotation/VSP_011602|||http://purl.uniprot.org/annotation/VSP_011603|||http://purl.uniprot.org/annotation/VSP_011604|||http://purl.uniprot.org/annotation/VSP_011605|||http://purl.uniprot.org/annotation/VSP_011606|||http://purl.uniprot.org/annotation/VSP_011607|||http://purl.uniprot.org/annotation/VSP_011608|||http://purl.uniprot.org/annotation/VSP_046124
http://togogenome.org/gene/9606:OR2Y1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGV0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2Y1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150513|||http://purl.uniprot.org/annotation/VAR_034186|||http://purl.uniprot.org/annotation/VAR_053162|||http://purl.uniprot.org/annotation/VAR_053163
http://togogenome.org/gene/9606:DDX50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ39                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX50|||Basic and acidic residues|||DEVD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055054
http://togogenome.org/gene/9606:CCDC192                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DO97                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 192|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000436441
http://togogenome.org/gene/9606:TBRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM73|||http://purl.uniprot.org/uniprot/B3KRS4|||http://purl.uniprot.org/uniprot/B4DU42|||http://purl.uniprot.org/uniprot/Q969Z0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Does not affect location in mitochondria; fails to rescue the increased accumulation of the level of mature MT-ND3, MT-CO3, MT-CYB or MT-ND5 mRNA in TBRG4-deficient cells; does not abolish the accumulation of the MT-ND5-CYB precursor RNA in a TBRG4-deficient cell line.|||FAST kinase domain-containing protein 4|||In isoform 2.|||Mitochondrion|||Phosphoserine|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273026|||http://purl.uniprot.org/annotation/VAR_030071|||http://purl.uniprot.org/annotation/VAR_030072|||http://purl.uniprot.org/annotation/VSP_022460
http://togogenome.org/gene/9606:NLRP13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ4|||http://purl.uniprot.org/uniprot/Q86W25                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||NACHT|||NACHT, LRR and PYD domains-containing protein 13|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080900|||http://purl.uniprot.org/annotation/VAR_031707|||http://purl.uniprot.org/annotation/VAR_031708
http://togogenome.org/gene/9606:TSPEAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU66                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In DFNB98; unknown pathological significance.|||In ECTD14 and STHAG10.|||In ECTD14 and STHAG10; unknown pathological significance.|||In ECTD14.|||In ECTD14; unknown pathological significance.|||In STHAG10.|||In STHAG10; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Thrombospondin-type laminin G domain and EAR repeat-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022597|||http://purl.uniprot.org/annotation/VAR_036271|||http://purl.uniprot.org/annotation/VAR_081734|||http://purl.uniprot.org/annotation/VAR_081735|||http://purl.uniprot.org/annotation/VAR_081736|||http://purl.uniprot.org/annotation/VAR_087915|||http://purl.uniprot.org/annotation/VAR_087916|||http://purl.uniprot.org/annotation/VAR_087917|||http://purl.uniprot.org/annotation/VAR_087918|||http://purl.uniprot.org/annotation/VAR_087919|||http://purl.uniprot.org/annotation/VAR_087920|||http://purl.uniprot.org/annotation/VAR_087921|||http://purl.uniprot.org/annotation/VAR_087922|||http://purl.uniprot.org/annotation/VAR_087923|||http://purl.uniprot.org/annotation/VAR_087924|||http://purl.uniprot.org/annotation/VAR_087925|||http://purl.uniprot.org/annotation/VAR_087926|||http://purl.uniprot.org/annotation/VAR_087927|||http://purl.uniprot.org/annotation/VSP_004006|||http://purl.uniprot.org/annotation/VSP_004007
http://togogenome.org/gene/9606:CEBPZOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTT3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein CEBPZOS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432372
http://togogenome.org/gene/9606:KLF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57682                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||CTBP-binding motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Krueppel-like factor 3|||Phosphoserine|||Polar residues|||Repressor domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047165|||http://purl.uniprot.org/annotation/VAR_052715|||http://purl.uniprot.org/annotation/VSP_014532
http://togogenome.org/gene/9606:NPPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16860                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Peptide|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  BNP(1-28)|||BNP(1-29)|||BNP(1-30)|||BNP(2-31)|||BNP(3-29)|||BNP(3-30)|||BNP(3-32)|||BNP(4-27)|||BNP(4-29)|||BNP(4-30)|||BNP(4-31)|||BNP(5-29)|||BNP(5-31)|||BNP(5-32)|||Brain natriuretic peptide 29|||Brain natriuretic peptide 32|||Cleavage; by CORIN|||Cleavage; by FAP|||Cleavage; by FURIN or CORIN|||Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-102 and A-105.|||Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-105.|||NT-proBNP|||Natriuretic peptides B|||No effect on proteolytic processing in HEK293 or HL1 cells. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-102.|||O-linked (HexNAc...) serine|||O-linked (HexNAc...) threonine|||O-linked (HexNAc...) threonine; Partial|||O-linked (Xyl...) (chondroitin sulfate) serine|||Prevents O-glycosylation at this residue. Decreased extracellular levels of NPPB due to decreased stability after secretion whereas extracellular levels of brain natriuretic peptide 32 is increased. In HEK293 cells, proteolytic processing by CORIN or FURIN is reduced but in HL1 cells proteolytic processing is not affected.|||proBNP(3-108)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001531|||http://purl.uniprot.org/annotation/PRO_0000001532|||http://purl.uniprot.org/annotation/PRO_0000364993|||http://purl.uniprot.org/annotation/PRO_0000364994|||http://purl.uniprot.org/annotation/PRO_0000364995|||http://purl.uniprot.org/annotation/PRO_0000364996|||http://purl.uniprot.org/annotation/PRO_0000364997|||http://purl.uniprot.org/annotation/PRO_0000364998|||http://purl.uniprot.org/annotation/PRO_0000364999|||http://purl.uniprot.org/annotation/PRO_0000365000|||http://purl.uniprot.org/annotation/PRO_0000365001|||http://purl.uniprot.org/annotation/PRO_0000365002|||http://purl.uniprot.org/annotation/PRO_0000365003|||http://purl.uniprot.org/annotation/PRO_0000365004|||http://purl.uniprot.org/annotation/PRO_0000365005|||http://purl.uniprot.org/annotation/PRO_0000365006|||http://purl.uniprot.org/annotation/PRO_0000365007|||http://purl.uniprot.org/annotation/PRO_0000451939|||http://purl.uniprot.org/annotation/PRO_0000451940|||http://purl.uniprot.org/annotation/VAR_014580|||http://purl.uniprot.org/annotation/VAR_014581|||http://purl.uniprot.org/annotation/VAR_014582
http://togogenome.org/gene/9606:CLN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R601|||http://purl.uniprot.org/uniprot/Q9NWW5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Ceroid-lipofuscinosis neuronal protein 6|||Helical|||In CLN4A.|||In CLN4A; requires 2 nucleotide substitutions.|||In CLN6.|||In CLN6; decreased protein level, resulting from ER membrane-to-cytosol dislocation of the protein followed by proteasome degradation..|||In CLN6; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089862|||http://purl.uniprot.org/annotation/VAR_015683|||http://purl.uniprot.org/annotation/VAR_015684|||http://purl.uniprot.org/annotation/VAR_015685|||http://purl.uniprot.org/annotation/VAR_015686|||http://purl.uniprot.org/annotation/VAR_021549|||http://purl.uniprot.org/annotation/VAR_021550|||http://purl.uniprot.org/annotation/VAR_021551|||http://purl.uniprot.org/annotation/VAR_021552|||http://purl.uniprot.org/annotation/VAR_021553|||http://purl.uniprot.org/annotation/VAR_021554|||http://purl.uniprot.org/annotation/VAR_058436|||http://purl.uniprot.org/annotation/VAR_058437|||http://purl.uniprot.org/annotation/VAR_065834|||http://purl.uniprot.org/annotation/VAR_065835|||http://purl.uniprot.org/annotation/VAR_065836|||http://purl.uniprot.org/annotation/VAR_065837|||http://purl.uniprot.org/annotation/VAR_065838|||http://purl.uniprot.org/annotation/VAR_065839|||http://purl.uniprot.org/annotation/VAR_065840|||http://purl.uniprot.org/annotation/VAR_065841|||http://purl.uniprot.org/annotation/VAR_065842|||http://purl.uniprot.org/annotation/VAR_066904|||http://purl.uniprot.org/annotation/VAR_066905|||http://purl.uniprot.org/annotation/VAR_066906|||http://purl.uniprot.org/annotation/VAR_066907|||http://purl.uniprot.org/annotation/VAR_066908|||http://purl.uniprot.org/annotation/VAR_066909|||http://purl.uniprot.org/annotation/VAR_066910|||http://purl.uniprot.org/annotation/VAR_066911|||http://purl.uniprot.org/annotation/VAR_066912|||http://purl.uniprot.org/annotation/VAR_066913|||http://purl.uniprot.org/annotation/VAR_066914|||http://purl.uniprot.org/annotation/VSP_056197
http://togogenome.org/gene/9606:SOWAHD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein SOWAHD|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315705|||http://purl.uniprot.org/annotation/VAR_061019
http://togogenome.org/gene/9606:IFNW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GUW6|||http://purl.uniprot.org/uniprot/P05000                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon omega-1|||N-linked (GlcNAc...) asparagine|||Or 23 in some molecules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000050|||http://purl.uniprot.org/annotation/PRO_0000016408|||http://purl.uniprot.org/annotation/PRO_5030739920|||http://purl.uniprot.org/annotation/VAR_020028
http://togogenome.org/gene/9606:AIFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PMA0|||http://purl.uniprot.org/uniprot/O95831                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Allows dimerization in absence of NADH.|||Apoptosis-inducing factor 1, mitochondrial|||Disordered|||Disrupts dimerization. Disrupts dimerization; when associated with A-477.|||Disrupts dimerization. Lower efficiency in stabilizing charge-transfer complexes upon coenzyme reduction.|||Disrupts dimerization; when associated with A-443--445-A.|||FAD-dependent oxidoreductase|||FAD/NAD(P)-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4.|||In COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death.|||In COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding.|||In COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding.|||In COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE.|||In DFNX5.|||In DFNX5; unknown pathological significance.|||In SEMDHL.|||In SEMDHL; severe decrease of protein expression.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increases protein dimerization at lower NADH levels.|||Mitochondrial apoptosis-inducing factor C-terminal|||Mitochondrial localization signal|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in patient with mitochondrial encephalomyopathy with moderate clinical severity and slow progressive course despite early onset as well as and cerebellar involvement; decreased protein level; strongly decreased redox potential; strongly decreased NADH oxidase activity; no effect on DNA-binding.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022030|||http://purl.uniprot.org/annotation/PRO_0000401935|||http://purl.uniprot.org/annotation/VAR_063827|||http://purl.uniprot.org/annotation/VAR_067334|||http://purl.uniprot.org/annotation/VAR_069468|||http://purl.uniprot.org/annotation/VAR_072791|||http://purl.uniprot.org/annotation/VAR_076211|||http://purl.uniprot.org/annotation/VAR_076212|||http://purl.uniprot.org/annotation/VAR_076213|||http://purl.uniprot.org/annotation/VAR_076214|||http://purl.uniprot.org/annotation/VAR_076215|||http://purl.uniprot.org/annotation/VAR_076216|||http://purl.uniprot.org/annotation/VAR_076217|||http://purl.uniprot.org/annotation/VAR_076218|||http://purl.uniprot.org/annotation/VAR_076219|||http://purl.uniprot.org/annotation/VAR_076220|||http://purl.uniprot.org/annotation/VAR_076221|||http://purl.uniprot.org/annotation/VAR_083067|||http://purl.uniprot.org/annotation/VAR_083068|||http://purl.uniprot.org/annotation/VAR_083739|||http://purl.uniprot.org/annotation/VAR_083740|||http://purl.uniprot.org/annotation/VAR_083741|||http://purl.uniprot.org/annotation/VSP_004357|||http://purl.uniprot.org/annotation/VSP_022953|||http://purl.uniprot.org/annotation/VSP_043637|||http://purl.uniprot.org/annotation/VSP_043638|||http://purl.uniprot.org/annotation/VSP_046248|||http://purl.uniprot.org/annotation/VSP_060785|||http://purl.uniprot.org/annotation/VSP_060786
http://togogenome.org/gene/9606:GPR39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43194                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases activation by Zn(2+). Abolishes activation by Zn(2+); when associated with A-17.|||Decreases activation by Zn(2+). Abolishes activation by Zn(2+); when associated with A-19.|||Disordered|||Extracellular|||G-protein coupled receptor 39|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Induces very high constitutive activity and eliminates Zn(2+)-induced activation.|||N-linked (GlcNAc...) asparagine|||Not affect constitutive or Zn(2+)-induced activation.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069565|||http://purl.uniprot.org/annotation/VAR_022067|||http://purl.uniprot.org/annotation/VAR_049393
http://togogenome.org/gene/9606:MCF2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y4M6|||http://purl.uniprot.org/uniprot/O15068                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CRAL-TRIO|||DH|||Disordered|||Guanine nucleotide exchange factor DBS|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 9.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 7 and isoform 9.|||In isoform 8.|||PH|||Phosphoserine|||Polar residues|||SH3|||Spectrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080935|||http://purl.uniprot.org/annotation/VSP_026119|||http://purl.uniprot.org/annotation/VSP_026120|||http://purl.uniprot.org/annotation/VSP_026121|||http://purl.uniprot.org/annotation/VSP_026122|||http://purl.uniprot.org/annotation/VSP_026123|||http://purl.uniprot.org/annotation/VSP_026124|||http://purl.uniprot.org/annotation/VSP_026126|||http://purl.uniprot.org/annotation/VSP_026127|||http://purl.uniprot.org/annotation/VSP_026128|||http://purl.uniprot.org/annotation/VSP_039037
http://togogenome.org/gene/9606:GPR139                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A142CHG1|||http://purl.uniprot.org/uniprot/Q6DWJ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 139                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069615
http://togogenome.org/gene/9606:CBR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4T8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoacyl-[acyl-carrier-protein] reductase|||Important for interaction with acyl carrier protein (ACP)|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Proton acceptor|||Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant.|||Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.|||Strongly reduced ability to restore growth of an OAR1-deficient yeast mutant. Strongly reduces NADPH-dependent reductase activity with acetoacetyl-CoA and 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.|||Unable to restore growth of an OAR1-deficient yeast mutant.|||Unable to restore growth of an OAR1-deficient yeast mutant. Abolishes NADPH-dependent reductase activity with acetoacetyl-CoA. Strongly reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.|||Unable to restore growth of an OAR1-deficient yeast mutant. Increases NADPH-dependent reductase activity with acetoacetyl-CoA. Reduces NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on NADH-dependent reductase activities.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319878|||http://purl.uniprot.org/annotation/VAR_039049|||http://purl.uniprot.org/annotation/VSP_031527
http://togogenome.org/gene/9606:SH3BP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0V3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Loss of function. Loss of targeting to the clathrin-coated pits and vesicles. Loss of interaction with DNM2, RRAGB and RRAGC. No effect on localization to the plasma membrane.|||Phosphoserine|||SH3 1|||SH3 2|||SH3 domain-binding protein 4|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274574|||http://purl.uniprot.org/annotation/VAR_030330|||http://purl.uniprot.org/annotation/VAR_030331|||http://purl.uniprot.org/annotation/VSP_022823
http://togogenome.org/gene/9606:SERINC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VE9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Serine incorporator 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330630|||http://purl.uniprot.org/annotation/VSP_033054|||http://purl.uniprot.org/annotation/VSP_033055|||http://purl.uniprot.org/annotation/VSP_042310
http://togogenome.org/gene/9606:DNMT3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBC3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADD|||Basic and acidic residues|||Citrulline|||DNA (cytosine-5)-methyltransferase 3B|||Disordered|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In FSHD4.|||In ICF1.|||In ICF1; unknown pathological significance.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 7.|||In isoform 8.|||Interaction with DNMT1 and DNMT3A|||Interaction with the PRC2/EED-EZH2 complex|||PHD-type; atypical|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM-dependent MTase C5-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088045|||http://purl.uniprot.org/annotation/VAR_011499|||http://purl.uniprot.org/annotation/VAR_011500|||http://purl.uniprot.org/annotation/VAR_011501|||http://purl.uniprot.org/annotation/VAR_011502|||http://purl.uniprot.org/annotation/VAR_011503|||http://purl.uniprot.org/annotation/VAR_011504|||http://purl.uniprot.org/annotation/VAR_011506|||http://purl.uniprot.org/annotation/VAR_011507|||http://purl.uniprot.org/annotation/VAR_011508|||http://purl.uniprot.org/annotation/VAR_011509|||http://purl.uniprot.org/annotation/VAR_011510|||http://purl.uniprot.org/annotation/VAR_022579|||http://purl.uniprot.org/annotation/VAR_022580|||http://purl.uniprot.org/annotation/VAR_022581|||http://purl.uniprot.org/annotation/VAR_033885|||http://purl.uniprot.org/annotation/VAR_077527|||http://purl.uniprot.org/annotation/VAR_077528|||http://purl.uniprot.org/annotation/VAR_077529|||http://purl.uniprot.org/annotation/VAR_077530|||http://purl.uniprot.org/annotation/VSP_005636|||http://purl.uniprot.org/annotation/VSP_005637|||http://purl.uniprot.org/annotation/VSP_005638|||http://purl.uniprot.org/annotation/VSP_005639|||http://purl.uniprot.org/annotation/VSP_005640|||http://purl.uniprot.org/annotation/VSP_005641|||http://purl.uniprot.org/annotation/VSP_045874|||http://purl.uniprot.org/annotation/VSP_045875|||http://purl.uniprot.org/annotation/VSP_045876
http://togogenome.org/gene/9606:OTUD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01804                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes 'Lys-48'- and 'Lys-63'-specific deubiquitinase activity.|||Abolishes 'Lys-48'- and 'Lys-63'-specific deubiquitinase activity. Impairs 'Lys-63'-specific deubiquitinase activity toward MYD88 substrate.|||Abolishes 'Lys-63'-specific deubiquitinase activity by impairing the affinity for 'Lys-63'-linked ubiquitin chain substrate.|||Abolishes interaction with USP7 and USP9X deubiquitinases.|||Basic and acidic residues|||Could be associated with cerebellar ataxia and hypogonadotropic hypogonadism.|||Cys-loop|||Decreases 'Lys-63'-specific deubiquitinase activity. Loss of 'Lys-63'-specific deubiquitinase activity; when associated with A-204.|||Disordered|||His-loop|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Loss of 'Lys-63'-specific deubiquitinase activity; when associated with A-204.|||N-acetylmethionine|||Nucleophile|||OTU|||OTU domain-containing protein 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083979|||http://purl.uniprot.org/annotation/VAR_029377|||http://purl.uniprot.org/annotation/VAR_038848|||http://purl.uniprot.org/annotation/VAR_070050|||http://purl.uniprot.org/annotation/VSP_021671|||http://purl.uniprot.org/annotation/VSP_038830|||http://purl.uniprot.org/annotation/VSP_053825
http://togogenome.org/gene/9606:CYP4F22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT55                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In ARCI5; results in decreased synthesis of omega-hydroxyceramides.|||In ARCI5; results in impaired synthesis of omega-hydroxyceramides.|||Lumenal|||Ultra-long-chain fatty acid omega-hydroxylase|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293731|||http://purl.uniprot.org/annotation/VAR_033118|||http://purl.uniprot.org/annotation/VAR_033119|||http://purl.uniprot.org/annotation/VAR_037441|||http://purl.uniprot.org/annotation/VAR_037442|||http://purl.uniprot.org/annotation/VAR_037443|||http://purl.uniprot.org/annotation/VAR_037444|||http://purl.uniprot.org/annotation/VAR_037445
http://togogenome.org/gene/9606:FGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02675|||http://purl.uniprot.org/uniprot/V9HVY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Beta-chain polymerization, binding distal domain of another fibrin|||Cleavage; by hementin; to prevent blood coagulation|||Cleavage; by plasmin; to break down fibrin clots|||Cleavage; by thrombin; to release fibrinopeptide B|||Disordered|||Fibrinogen C-terminal|||Fibrinogen beta chain|||Fibrinopeptide B|||In Baltimore-2.|||In CAFBN.|||In CAFBN; abolishes fibrinogen secretion.|||In CAFBN; fibrinogen Longmont.|||In CAFBN; homozygous; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion.|||In CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion.|||In Christchurch-2, Seattle-1 and Ijmuiden.|||In DYSFIBRIN; fibrinogen Naples and Milano-2; associated with defective thrombin binding and thrombophilia.|||In Ise.|||In New York-1.|||In Nijmegen.|||In Pontoise-2.|||Interchain (with C-161 in gamma chain)|||Interchain (with C-184 in alpha chain)|||Interchain (with C-45 in gamma chain)|||Interchain (with C-55 in alpha chain)|||Interchain (with C-68 in alpha chain)|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009070|||http://purl.uniprot.org/annotation/PRO_0000009071|||http://purl.uniprot.org/annotation/PRO_5004776896|||http://purl.uniprot.org/annotation/VAR_002402|||http://purl.uniprot.org/annotation/VAR_002403|||http://purl.uniprot.org/annotation/VAR_002404|||http://purl.uniprot.org/annotation/VAR_002405|||http://purl.uniprot.org/annotation/VAR_002406|||http://purl.uniprot.org/annotation/VAR_002407|||http://purl.uniprot.org/annotation/VAR_002408|||http://purl.uniprot.org/annotation/VAR_013091|||http://purl.uniprot.org/annotation/VAR_013092|||http://purl.uniprot.org/annotation/VAR_013093|||http://purl.uniprot.org/annotation/VAR_014169|||http://purl.uniprot.org/annotation/VAR_016908|||http://purl.uniprot.org/annotation/VAR_016909|||http://purl.uniprot.org/annotation/VAR_016910|||http://purl.uniprot.org/annotation/VAR_072620|||http://purl.uniprot.org/annotation/VAR_072724|||http://purl.uniprot.org/annotation/VAR_072725
http://togogenome.org/gene/9606:NRXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEM5|||http://purl.uniprot.org/uniprot/A0A0D9SEQ7|||http://purl.uniprot.org/uniprot/A0A1D5RMU6|||http://purl.uniprot.org/uniprot/E7EQN4|||http://purl.uniprot.org/uniprot/E7ERL8|||http://purl.uniprot.org/uniprot/H0Y568|||http://purl.uniprot.org/uniprot/H7BYC7|||http://purl.uniprot.org/uniprot/P58400|||http://purl.uniprot.org/uniprot/Q9ULB1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Essential for interaction with CBLN1; modulates interaction affinity with NLGN1, NLGN2 and NLGN3; prevents interaction with DAG1/alpha-dystroglycan; modulates interaction with alpha-latrotoxin|||Extracellular|||Helical|||In isoform 2a.|||In isoform 3a and isoform 2a.|||In isoform 3a.|||In isoform 3b.|||In isoform 4 and isoform 2a.|||In isoform 4.|||Interaction with CASK|||Laminin G|||Laminin G-like|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin G-like 6|||N-linked (GlcNAc...) asparagine|||Neurexin-1|||Neurexin-1-beta|||Neurexin/syndecan/glycophorin C|||O-linked (Xyl...) (heparan sulfate) serine|||Phosphoserine; by CASK|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019490|||http://purl.uniprot.org/annotation/PRO_0000019493|||http://purl.uniprot.org/annotation/PRO_5002346753|||http://purl.uniprot.org/annotation/PRO_5003219277|||http://purl.uniprot.org/annotation/PRO_5003219291|||http://purl.uniprot.org/annotation/PRO_5008929789|||http://purl.uniprot.org/annotation/VAR_050265|||http://purl.uniprot.org/annotation/VAR_070274|||http://purl.uniprot.org/annotation/VSP_014541|||http://purl.uniprot.org/annotation/VSP_041353|||http://purl.uniprot.org/annotation/VSP_041354|||http://purl.uniprot.org/annotation/VSP_041355|||http://purl.uniprot.org/annotation/VSP_058200|||http://purl.uniprot.org/annotation/VSP_058201|||http://purl.uniprot.org/annotation/VSP_058202|||http://purl.uniprot.org/annotation/VSP_059057
http://togogenome.org/gene/9606:GPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53RZ9|||http://purl.uniprot.org/uniprot/Q9HCN4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||Abolishes GTPase activity and decreases association with GPN3.|||Disordered|||GPN-loop GTPase 1|||Gly-Pro-Asn (GPN)-loop; involved in dimer interface|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Stabilizes the phosphate intermediate; shared with dimeric partner                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066001|||http://purl.uniprot.org/annotation/VSP_042749|||http://purl.uniprot.org/annotation/VSP_042750|||http://purl.uniprot.org/annotation/VSP_046176|||http://purl.uniprot.org/annotation/VSP_054366
http://togogenome.org/gene/9606:RADIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JH8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dilute|||Disordered|||FHA|||In isoform 1.|||In isoform 2.|||In isoform 3.|||PDZ|||Phosphoserine|||Polar residues|||Ras-associating|||Ras-associating and dilute domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050803|||http://purl.uniprot.org/annotation/VAR_023769|||http://purl.uniprot.org/annotation/VAR_046192|||http://purl.uniprot.org/annotation/VAR_046193|||http://purl.uniprot.org/annotation/VAR_060193|||http://purl.uniprot.org/annotation/VSP_016097|||http://purl.uniprot.org/annotation/VSP_016098|||http://purl.uniprot.org/annotation/VSP_016099|||http://purl.uniprot.org/annotation/VSP_035179
http://togogenome.org/gene/9606:PNOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13519                                                                                  ^@                                                                                  Helix|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Helix|||Peptide|||Propeptide|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Nociceptin|||Nocistatin|||Orphanin FQ2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008325|||http://purl.uniprot.org/annotation/PRO_0000008326|||http://purl.uniprot.org/annotation/PRO_0000008327|||http://purl.uniprot.org/annotation/PRO_0000008328|||http://purl.uniprot.org/annotation/PRO_0000008329|||http://purl.uniprot.org/annotation/VSP_055146
http://togogenome.org/gene/9606:PLCG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19174|||http://purl.uniprot.org/uniprot/Q4LE43|||http://purl.uniprot.org/uniprot/Q9UFY1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1|||C2|||Disordered|||EF-hand|||In isoform 2.|||N-acetylalanine|||PH|||PH 1|||PH 2; first part|||PH 2; second part|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ITK, SYK and TXK|||Phosphotyrosine; by SYK|||Removed|||SH2|||SH2 1|||SH2 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088498|||http://purl.uniprot.org/annotation/VAR_011908|||http://purl.uniprot.org/annotation/VAR_022130|||http://purl.uniprot.org/annotation/VAR_025213|||http://purl.uniprot.org/annotation/VAR_025214|||http://purl.uniprot.org/annotation/VSP_038692
http://togogenome.org/gene/9606:VAX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0K5|||http://purl.uniprot.org/uniprot/Q9UIW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Polar residues|||Ventral anterior homeobox 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049351|||http://purl.uniprot.org/annotation/VAR_020152|||http://purl.uniprot.org/annotation/VAR_067308
http://togogenome.org/gene/9606:STT3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCJ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DK motif|||DXD motif 1|||DXD motif 2|||Disordered|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B|||Helical|||Important for catalytic activity|||Interacts with target acceptor peptide in protein substrate|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Removed|||SVSE motif|||WWDYG motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246001
http://togogenome.org/gene/9606:ZNF587B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ETH6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 587B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416243
http://togogenome.org/gene/9606:C20orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZML9|||http://purl.uniprot.org/uniprot/F5GZA9|||http://purl.uniprot.org/uniprot/Q9NUD7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C20orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079450|||http://purl.uniprot.org/annotation/VAR_056847
http://togogenome.org/gene/9606:TCEA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUM4|||http://purl.uniprot.org/uniprot/O75764                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121452|||http://purl.uniprot.org/annotation/VSP_056838|||http://purl.uniprot.org/annotation/VSP_056839
http://togogenome.org/gene/9606:UGT3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K444|||http://purl.uniprot.org/uniprot/B7Z3N0|||http://purl.uniprot.org/uniprot/Q6NUS8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299150|||http://purl.uniprot.org/annotation/PRO_5005123905|||http://purl.uniprot.org/annotation/PRO_5014205125|||http://purl.uniprot.org/annotation/VAR_034791|||http://purl.uniprot.org/annotation/VSP_044985|||http://purl.uniprot.org/annotation/VSP_044986|||http://purl.uniprot.org/annotation/VSP_044987
http://togogenome.org/gene/9606:DMGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ84|||http://purl.uniprot.org/uniprot/Q9UI17                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aminomethyltransferase folate-binding|||Dimethylglycine dehydrogenase, mitochondrial|||Disordered|||FAD dependent oxidoreductase|||FAD dependent oxidoreductase central|||Glycine cleavage T-protein C-terminal barrel|||In DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Tele-8alpha-FAD histidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010767|||http://purl.uniprot.org/annotation/VAR_011505|||http://purl.uniprot.org/annotation/VAR_014950|||http://purl.uniprot.org/annotation/VAR_014951|||http://purl.uniprot.org/annotation/VAR_014952|||http://purl.uniprot.org/annotation/VSP_056959|||http://purl.uniprot.org/annotation/VSP_056960|||http://purl.uniprot.org/annotation/VSP_056961|||http://purl.uniprot.org/annotation/VSP_056962
http://togogenome.org/gene/9606:DARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI48|||http://purl.uniprot.org/uniprot/Q9H9J7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Aminoacyl-transfer RNA synthetases class-II family profile|||Aspartate|||Aspartate--tRNA ligase, mitochondrial|||In LBSL.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250736|||http://purl.uniprot.org/annotation/VAR_027612|||http://purl.uniprot.org/annotation/VAR_034525|||http://purl.uniprot.org/annotation/VAR_037015|||http://purl.uniprot.org/annotation/VAR_037016|||http://purl.uniprot.org/annotation/VAR_037017|||http://purl.uniprot.org/annotation/VAR_037018|||http://purl.uniprot.org/annotation/VAR_037019|||http://purl.uniprot.org/annotation/VAR_037020|||http://purl.uniprot.org/annotation/VAR_037021|||http://purl.uniprot.org/annotation/VAR_037022|||http://purl.uniprot.org/annotation/VAR_037023|||http://purl.uniprot.org/annotation/VAR_037024|||http://purl.uniprot.org/annotation/VAR_037025
http://togogenome.org/gene/9606:FAM83F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Protein FAM83F|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314950|||http://purl.uniprot.org/annotation/VAR_038134|||http://purl.uniprot.org/annotation/VAR_038135|||http://purl.uniprot.org/annotation/VAR_038136|||http://purl.uniprot.org/annotation/VAR_038137|||http://purl.uniprot.org/annotation/VSP_030448
http://togogenome.org/gene/9606:MTCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94964|||http://purl.uniprot.org/uniprot/X6R3R3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal 80 kDa form|||Cleavage|||DUF4482|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-terminal form|||Phosphoserine|||Protein SOGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050781|||http://purl.uniprot.org/annotation/PRO_0000418054|||http://purl.uniprot.org/annotation/PRO_0000418055|||http://purl.uniprot.org/annotation/VAR_056848|||http://purl.uniprot.org/annotation/VSP_035976|||http://purl.uniprot.org/annotation/VSP_035977|||http://purl.uniprot.org/annotation/VSP_035978|||http://purl.uniprot.org/annotation/VSP_035979|||http://purl.uniprot.org/annotation/VSP_040825|||http://purl.uniprot.org/annotation/VSP_040826
http://togogenome.org/gene/9606:NOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13253                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a case of radioulnar synostosis; unknown pathological significance.|||Found in a family with radioulnar synostosis; unknown pathological significance.|||In BDB2.|||In SYM1A and BDB2.|||In SYM1A and TCC.|||In SYM1A.|||In SYM1A; sporadic; de novo mutation.|||In SYNS1.|||In TCC.|||N-linked (GlcNAc...) asparagine|||Noggin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019813|||http://purl.uniprot.org/annotation/VAR_011361|||http://purl.uniprot.org/annotation/VAR_011362|||http://purl.uniprot.org/annotation/VAR_011363|||http://purl.uniprot.org/annotation/VAR_011364|||http://purl.uniprot.org/annotation/VAR_011365|||http://purl.uniprot.org/annotation/VAR_011366|||http://purl.uniprot.org/annotation/VAR_011367|||http://purl.uniprot.org/annotation/VAR_018324|||http://purl.uniprot.org/annotation/VAR_018325|||http://purl.uniprot.org/annotation/VAR_018326|||http://purl.uniprot.org/annotation/VAR_036997|||http://purl.uniprot.org/annotation/VAR_036998|||http://purl.uniprot.org/annotation/VAR_036999|||http://purl.uniprot.org/annotation/VAR_037000|||http://purl.uniprot.org/annotation/VAR_037001|||http://purl.uniprot.org/annotation/VAR_037605|||http://purl.uniprot.org/annotation/VAR_064541|||http://purl.uniprot.org/annotation/VAR_084488|||http://purl.uniprot.org/annotation/VAR_084489
http://togogenome.org/gene/9606:IRF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00978                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased transcriptional activation in response to type I interferon stimulation.|||Decreased transcriptional activation in response to type I interferon stimulation. Decreased anti-viral immunity.|||Disordered|||Does not affect transcriptional activation in response to type I interferon stimulation; does not affect anti-viral immunity.|||IRF tryptophan pentad repeat|||Interferon regulatory factor 9|||Loss of transcriptional activation in response to type I interferon stimulation. Impaired anti-viral immunity.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154567|||http://purl.uniprot.org/annotation/VAR_083496|||http://purl.uniprot.org/annotation/VAR_083497
http://togogenome.org/gene/9606:KRTAP2-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7H8|||http://purl.uniprot.org/uniprot/Q9BYR9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  10 X 5 AA repeats of C-C-[CDPQRWG]-[APRS]-[CIPSTVD]|||10 X 5 AA repeats of C-C-[CDPQRW]-[ADPRS]-[CIPSTV]|||Keratin-associated protein 2-3|||Keratin-associated protein 2-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185162|||http://purl.uniprot.org/annotation/PRO_0000331452
http://togogenome.org/gene/9606:KANK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALP6|||http://purl.uniprot.org/uniprot/Q5T7N3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||Found in a patient with nephrotic syndrome; unknown pathological significance; no effect on protein localization.|||In isoform 2.|||KN motif and ankyrin repeat domain-containing protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244364|||http://purl.uniprot.org/annotation/VAR_026902|||http://purl.uniprot.org/annotation/VAR_026903|||http://purl.uniprot.org/annotation/VAR_026904|||http://purl.uniprot.org/annotation/VAR_048306|||http://purl.uniprot.org/annotation/VAR_048307|||http://purl.uniprot.org/annotation/VAR_048308|||http://purl.uniprot.org/annotation/VAR_080961|||http://purl.uniprot.org/annotation/VSP_019552|||http://purl.uniprot.org/annotation/VSP_019553
http://togogenome.org/gene/9606:TOM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUF5|||http://purl.uniprot.org/uniprot/O60784                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Clathrin box|||Disordered|||Fails to interact with clathrin heavy chain. Diffuse localization throughout the cell.|||GAT|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD85; decreases interaction with TOLLIP and UBC.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with MYO6|||KRKK|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced binding to phosphatidylinositol monophosphates.|||Reduced interaction with TOLLIP.|||Reduced interaction with TOLLIP. Reduced localization to endosomal vesicles.|||Reduced interaction with UBC/ubiquitin.|||Reduced interaction with clathrin heavy chain.|||Target of Myb1 membrane trafficking protein|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072628|||http://purl.uniprot.org/annotation/VAR_034567|||http://purl.uniprot.org/annotation/VAR_053845|||http://purl.uniprot.org/annotation/VAR_086655|||http://purl.uniprot.org/annotation/VSP_038364|||http://purl.uniprot.org/annotation/VSP_038365|||http://purl.uniprot.org/annotation/VSP_038366
http://togogenome.org/gene/9606:AKNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q64FY1|||http://purl.uniprot.org/uniprot/Q7Z591                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A.T hook|||AKNA|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Microtubule organization protein AKNA|||PEST|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289159|||http://purl.uniprot.org/annotation/VAR_032586|||http://purl.uniprot.org/annotation/VAR_032587|||http://purl.uniprot.org/annotation/VAR_032588|||http://purl.uniprot.org/annotation/VAR_032589|||http://purl.uniprot.org/annotation/VAR_032590|||http://purl.uniprot.org/annotation/VSP_025932|||http://purl.uniprot.org/annotation/VSP_025933|||http://purl.uniprot.org/annotation/VSP_025934|||http://purl.uniprot.org/annotation/VSP_025935|||http://purl.uniprot.org/annotation/VSP_025936|||http://purl.uniprot.org/annotation/VSP_025937|||http://purl.uniprot.org/annotation/VSP_025938|||http://purl.uniprot.org/annotation/VSP_025939|||http://purl.uniprot.org/annotation/VSP_025940
http://togogenome.org/gene/9606:TKTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7I0|||http://purl.uniprot.org/uniprot/P51854                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Important for catalytic activity|||In isoform 2 and isoform 4.|||In isoform 2.|||Proton donor|||Transketolase-like protein 1|||Transketolase-like pyrimidine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191899|||http://purl.uniprot.org/annotation/VAR_029867|||http://purl.uniprot.org/annotation/VAR_029868|||http://purl.uniprot.org/annotation/VAR_087456|||http://purl.uniprot.org/annotation/VSP_022290|||http://purl.uniprot.org/annotation/VSP_022291
http://togogenome.org/gene/9606:ADK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE0|||http://purl.uniprot.org/uniprot/A0A5F9ZH72|||http://purl.uniprot.org/uniprot/A0A5F9ZHJ1|||http://purl.uniprot.org/uniprot/P55263                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes nuclear localization.|||Adenosine kinase|||Carbohydrate kinase PfkB|||In HMAKD; complete loss of adenosine kinase activity.|||In HMAKD; the mutant shows some residual adenosine kinase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Nuclear localization signal|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080053|||http://purl.uniprot.org/annotation/VAR_066640|||http://purl.uniprot.org/annotation/VAR_066641|||http://purl.uniprot.org/annotation/VAR_066642|||http://purl.uniprot.org/annotation/VSP_004668|||http://purl.uniprot.org/annotation/VSP_043526|||http://purl.uniprot.org/annotation/VSP_046713
http://togogenome.org/gene/9606:KIAA0040                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15053                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Uncharacterized protein KIAA0040                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444986
http://togogenome.org/gene/9606:HLA-F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30511|||http://purl.uniprot.org/uniprot/Q5JZ47|||http://purl.uniprot.org/uniprot/Q5JZ48                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class I histocompatibility antigen, alpha chain F|||Helical|||Ig-like|||Ig-like C1-type|||Impairs peptide binding.|||Impairs the anterograde ER-to-Golgi transport.|||Impairs the interaction with 14-3-3 proteins.|||Impairs the interaction with coat protein complex II; impairs the anterograde ER-to-Golgi transport.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sorting signal sequence; Golgi-retention signal; ER-retention signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018884|||http://purl.uniprot.org/annotation/PRO_5004258048|||http://purl.uniprot.org/annotation/PRO_5035395696|||http://purl.uniprot.org/annotation/VAR_018327|||http://purl.uniprot.org/annotation/VAR_056525|||http://purl.uniprot.org/annotation/VAR_056526|||http://purl.uniprot.org/annotation/VSP_038846|||http://purl.uniprot.org/annotation/VSP_040349
http://togogenome.org/gene/9606:RRP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43818                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired acetylation, leading to promote rRNA processing; when associated with R-12.|||Impaired acetylation, leading to promote rRNA processing; when associated with R-25.|||In a breast cancer sample; somatic mutation.|||Mimics acetylation, leading to impaired rRNA processing; when associated with Q-12.|||Mimics acetylation, leading to impaired rRNA processing; when associated with Q-25.|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||U3 small nucleolar RNA-interacting protein 2|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051313|||http://purl.uniprot.org/annotation/VAR_035887|||http://purl.uniprot.org/annotation/VAR_035888
http://togogenome.org/gene/9606:KLHL40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5H9|||http://purl.uniprot.org/uniprot/Q2TBA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Basic and acidic residues|||Disordered|||In NEM8.|||In NEM8; unknown pathological significance.|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274235|||http://purl.uniprot.org/annotation/VAR_030214|||http://purl.uniprot.org/annotation/VAR_030215|||http://purl.uniprot.org/annotation/VAR_069836|||http://purl.uniprot.org/annotation/VAR_069837|||http://purl.uniprot.org/annotation/VAR_069838|||http://purl.uniprot.org/annotation/VAR_069839|||http://purl.uniprot.org/annotation/VAR_069840|||http://purl.uniprot.org/annotation/VAR_069841|||http://purl.uniprot.org/annotation/VAR_069842|||http://purl.uniprot.org/annotation/VAR_069843|||http://purl.uniprot.org/annotation/VAR_069844|||http://purl.uniprot.org/annotation/VAR_069845|||http://purl.uniprot.org/annotation/VAR_069846|||http://purl.uniprot.org/annotation/VAR_069847|||http://purl.uniprot.org/annotation/VAR_077950|||http://purl.uniprot.org/annotation/VAR_077951|||http://purl.uniprot.org/annotation/VAR_077952|||http://purl.uniprot.org/annotation/VSP_022681|||http://purl.uniprot.org/annotation/VSP_022682
http://togogenome.org/gene/9606:PLEKHB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSE9|||http://purl.uniprot.org/uniprot/A0A0A0MSI4|||http://purl.uniprot.org/uniprot/B4DJB7|||http://purl.uniprot.org/uniprot/Q96CS7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PH|||Pleckstrin homology domain-containing family B member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053889|||http://purl.uniprot.org/annotation/VSP_009783|||http://purl.uniprot.org/annotation/VSP_009784|||http://purl.uniprot.org/annotation/VSP_045163|||http://purl.uniprot.org/annotation/VSP_045164|||http://purl.uniprot.org/annotation/VSP_047118
http://togogenome.org/gene/9606:RBIS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0T1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Ribosomal biogenesis factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324604|||http://purl.uniprot.org/annotation/VSP_032304
http://togogenome.org/gene/9606:SLC26A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43511                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; requires 2 nucleotide substitutions; uncertain pathological significance.|||Found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance.|||Found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; unknown pathological significance; retains its ability to transport iodide in vitro.|||Found at heterozygosity in a patient with non-syndromic deafness; uncertain pathological significance.|||Helical|||In DFNB4 and PDS.|||In DFNB4 and PDS; common mutation in Korea and Japan.|||In DFNB4 and PDS; does not affect protein localization to cell membrane; does not affect iodide transport.|||In DFNB4 and PDS; fails to localize to cell membrane; abolishes iodide transport.|||In DFNB4 and PDS; severely reduces iodide transport without affecting protein localization to cell membrane.|||In DFNB4.|||In DFNB4; also found at heterozygosity in a patient with non-syndromic deafness; uncertain pathological significance; loss of cell membrane localization, loss of chloride tranport, chloride-bicarbonate exchanger and chloride-iodide exchanger activities.|||In PDS and DFNB4.|||In PDS and DFNB4; also found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance.|||In PDS and DFNB4; common mutation.|||In PDS and DFNB4; common mutation; fails to localize to cell membrane; abolishes iodide transport.|||In PDS and DFNB4; partially affects protein localization to cell membrane; abolishes iodide transport.|||In PDS.|||In PDS; also found at heterozygosity in a patient with hearing loss and unilateral enlargement of the vestibular aqueduct; uncertain pathological significance.|||In PDS; fails to localize to cell membrane; abolishes iodide transport.|||In PDS; partially affects protein localization to cell membrane; abolishes iodide transport.|||In PDS; retains residual transport function.|||In Pendred syndrome/deafness individuals.|||In isoform 2.|||Pendrin|||STAS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080164|||http://purl.uniprot.org/annotation/VAR_007440|||http://purl.uniprot.org/annotation/VAR_007441|||http://purl.uniprot.org/annotation/VAR_007442|||http://purl.uniprot.org/annotation/VAR_007443|||http://purl.uniprot.org/annotation/VAR_007444|||http://purl.uniprot.org/annotation/VAR_007445|||http://purl.uniprot.org/annotation/VAR_007446|||http://purl.uniprot.org/annotation/VAR_007447|||http://purl.uniprot.org/annotation/VAR_007448|||http://purl.uniprot.org/annotation/VAR_007449|||http://purl.uniprot.org/annotation/VAR_011623|||http://purl.uniprot.org/annotation/VAR_011624|||http://purl.uniprot.org/annotation/VAR_021638|||http://purl.uniprot.org/annotation/VAR_021639|||http://purl.uniprot.org/annotation/VAR_021640|||http://purl.uniprot.org/annotation/VAR_021641|||http://purl.uniprot.org/annotation/VAR_021642|||http://purl.uniprot.org/annotation/VAR_021643|||http://purl.uniprot.org/annotation/VAR_021644|||http://purl.uniprot.org/annotation/VAR_021645|||http://purl.uniprot.org/annotation/VAR_021646|||http://purl.uniprot.org/annotation/VAR_021647|||http://purl.uniprot.org/annotation/VAR_021648|||http://purl.uniprot.org/annotation/VAR_021649|||http://purl.uniprot.org/annotation/VAR_021650|||http://purl.uniprot.org/annotation/VAR_021651|||http://purl.uniprot.org/annotation/VAR_021652|||http://purl.uniprot.org/annotation/VAR_021653|||http://purl.uniprot.org/annotation/VAR_021654|||http://purl.uniprot.org/annotation/VAR_021655|||http://purl.uniprot.org/annotation/VAR_021656|||http://purl.uniprot.org/annotation/VAR_021657|||http://purl.uniprot.org/annotation/VAR_021658|||http://purl.uniprot.org/annotation/VAR_021659|||http://purl.uniprot.org/annotation/VAR_021660|||http://purl.uniprot.org/annotation/VAR_021661|||http://purl.uniprot.org/annotation/VAR_021662|||http://purl.uniprot.org/annotation/VAR_021663|||http://purl.uniprot.org/annotation/VAR_021664|||http://purl.uniprot.org/annotation/VAR_021665|||http://purl.uniprot.org/annotation/VAR_021666|||http://purl.uniprot.org/annotation/VAR_021667|||http://purl.uniprot.org/annotation/VAR_021668|||http://purl.uniprot.org/annotation/VAR_021669|||http://purl.uniprot.org/annotation/VAR_021670|||http://purl.uniprot.org/annotation/VAR_021671|||http://purl.uniprot.org/annotation/VAR_021672|||http://purl.uniprot.org/annotation/VAR_021673|||http://purl.uniprot.org/annotation/VAR_021674|||http://purl.uniprot.org/annotation/VAR_021675|||http://purl.uniprot.org/annotation/VAR_021676|||http://purl.uniprot.org/annotation/VAR_021677|||http://purl.uniprot.org/annotation/VAR_021678|||http://purl.uniprot.org/annotation/VAR_021679|||http://purl.uniprot.org/annotation/VAR_021680|||http://purl.uniprot.org/annotation/VAR_021681|||http://purl.uniprot.org/annotation/VAR_027238|||http://purl.uniprot.org/annotation/VAR_027239|||http://purl.uniprot.org/annotation/VAR_027240|||http://purl.uniprot.org/annotation/VAR_027241|||http://purl.uniprot.org/annotation/VAR_027242|||http://purl.uniprot.org/annotation/VAR_027243|||http://purl.uniprot.org/annotation/VAR_027244|||http://purl.uniprot.org/annotation/VAR_027245|||http://purl.uniprot.org/annotation/VAR_027246|||http://purl.uniprot.org/annotation/VAR_053663|||http://purl.uniprot.org/annotation/VAR_053664|||http://purl.uniprot.org/annotation/VAR_053665|||http://purl.uniprot.org/annotation/VAR_058580|||http://purl.uniprot.org/annotation/VAR_058581|||http://purl.uniprot.org/annotation/VAR_064988|||http://purl.uniprot.org/annotation/VAR_064989|||http://purl.uniprot.org/annotation/VAR_064990|||http://purl.uniprot.org/annotation/VAR_064991|||http://purl.uniprot.org/annotation/VAR_064992|||http://purl.uniprot.org/annotation/VAR_064993|||http://purl.uniprot.org/annotation/VAR_079503|||http://purl.uniprot.org/annotation/VAR_080402|||http://purl.uniprot.org/annotation/VSP_056688
http://togogenome.org/gene/9606:TSC22D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3Y6|||http://purl.uniprot.org/uniprot/Q15714                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||Required for interaction with TGFBR1 and promotion of TGF-beta signaling|||TSC22 domain family protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219365|||http://purl.uniprot.org/annotation/VAR_057311|||http://purl.uniprot.org/annotation/VSP_035324|||http://purl.uniprot.org/annotation/VSP_035325|||http://purl.uniprot.org/annotation/VSP_035326|||http://purl.uniprot.org/annotation/VSP_044939|||http://purl.uniprot.org/annotation/VSP_044940|||http://purl.uniprot.org/annotation/VSP_061917
http://togogenome.org/gene/9606:F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00734                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  4-carboxyglutamate|||Activation peptide fragment 1|||Activation peptide fragment 2|||Charge relay system|||Cleavage; by factor Xa|||Cleavage; by thrombin|||Confirmed at protein level.|||Gla|||High affinity receptor-binding region which is also known as the TP508 peptide|||In FA2D; Barcelona/Madrid.|||In FA2D; Himi-1.|||In FA2D; Himi-2.|||In FA2D; Padua-1.|||In FA2D; Quick-1.|||In FA2D; Quick-2.|||In FA2D; Salakta/Frankfurt.|||In FA2D; Shanghai.|||In FA2D; Tokushima.|||In FA2D; prothrombin type 3; variant confirmed at protein level.|||Interchain (between light and heavy chains)|||Kringle 1|||Kringle 2|||Loss of catalytic activity; no effect on cleavage at R-198 by factor Xa.|||Loss of cleavage by factor Xa.|||N-linked (GlcNAc...) (complex) asparagine|||Peptidase S1|||Prothrombin|||Thrombin heavy chain|||Thrombin light chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028159|||http://purl.uniprot.org/annotation/PRO_0000028160|||http://purl.uniprot.org/annotation/PRO_0000028161|||http://purl.uniprot.org/annotation/PRO_0000028162|||http://purl.uniprot.org/annotation/PRO_0000028163|||http://purl.uniprot.org/annotation/PRO_0000028164|||http://purl.uniprot.org/annotation/VAR_006711|||http://purl.uniprot.org/annotation/VAR_006712|||http://purl.uniprot.org/annotation/VAR_006713|||http://purl.uniprot.org/annotation/VAR_006714|||http://purl.uniprot.org/annotation/VAR_006715|||http://purl.uniprot.org/annotation/VAR_006716|||http://purl.uniprot.org/annotation/VAR_006717|||http://purl.uniprot.org/annotation/VAR_006718|||http://purl.uniprot.org/annotation/VAR_006719|||http://purl.uniprot.org/annotation/VAR_011781|||http://purl.uniprot.org/annotation/VAR_011782|||http://purl.uniprot.org/annotation/VAR_055232|||http://purl.uniprot.org/annotation/VAR_068913
http://togogenome.org/gene/9606:PLEKHS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5Z2|||http://purl.uniprot.org/uniprot/Q5SXH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 1.|||In isoform 3.|||In isoform 4 and isoform 1.|||In isoform 4.|||PH|||Pleckstrin homology domain-containing family S member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320675|||http://purl.uniprot.org/annotation/VAR_039275|||http://purl.uniprot.org/annotation/VAR_080192|||http://purl.uniprot.org/annotation/VSP_060736|||http://purl.uniprot.org/annotation/VSP_060737|||http://purl.uniprot.org/annotation/VSP_060738|||http://purl.uniprot.org/annotation/VSP_060739|||http://purl.uniprot.org/annotation/VSP_060740|||http://purl.uniprot.org/annotation/VSP_060741|||http://purl.uniprot.org/annotation/VSP_060742
http://togogenome.org/gene/9606:MIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16674                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Melanoma-derived growth regulatory protein|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019028|||http://purl.uniprot.org/annotation/VSP_044450
http://togogenome.org/gene/9606:TBC1D10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMP7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of GAP activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rab-GAP TBC|||TBC1 domain family member 10B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315716|||http://purl.uniprot.org/annotation/VSP_030670
http://togogenome.org/gene/9606:TBPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6SJ96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||TATA box-binding protein-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318118|||http://purl.uniprot.org/annotation/VAR_038692
http://togogenome.org/gene/9606:SPRR2G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA approximate tandem repeats|||Disordered|||Small proline-rich protein 2G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150013
http://togogenome.org/gene/9606:CAV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56539                                                                                  ^@                                                                                  Chain|||Crosslink|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain                                                                                  ^@                                                                                  Chain|||Crosslink|||INTRAMEM|||Region|||Sequence Variant|||Topological Domain                                                                                  ^@                                                                                  Caveolin-3|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Helical|||In CMH.|||In HYPCK, RMD2 and MPDT.|||In HYPCK.|||In LQT9 and SIDS.|||In LQT9.|||In LQT9; increase in late sodium current.|||In RMD2 and MPDT.|||In RMD2.|||In RMD2; decreased surface expression of the CAV3 protein.|||In SIDS.|||In a patient with mild proximal myopathy.|||Required for interaction with DAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144140|||http://purl.uniprot.org/annotation/VAR_001402|||http://purl.uniprot.org/annotation/VAR_001403|||http://purl.uniprot.org/annotation/VAR_010742|||http://purl.uniprot.org/annotation/VAR_010743|||http://purl.uniprot.org/annotation/VAR_011512|||http://purl.uniprot.org/annotation/VAR_011513|||http://purl.uniprot.org/annotation/VAR_011514|||http://purl.uniprot.org/annotation/VAR_015374|||http://purl.uniprot.org/annotation/VAR_016207|||http://purl.uniprot.org/annotation/VAR_016208|||http://purl.uniprot.org/annotation/VAR_021016|||http://purl.uniprot.org/annotation/VAR_021017|||http://purl.uniprot.org/annotation/VAR_021018|||http://purl.uniprot.org/annotation/VAR_026696|||http://purl.uniprot.org/annotation/VAR_029540|||http://purl.uniprot.org/annotation/VAR_029541|||http://purl.uniprot.org/annotation/VAR_029542|||http://purl.uniprot.org/annotation/VAR_029543|||http://purl.uniprot.org/annotation/VAR_029544|||http://purl.uniprot.org/annotation/VAR_029545|||http://purl.uniprot.org/annotation/VAR_043694|||http://purl.uniprot.org/annotation/VAR_043695|||http://purl.uniprot.org/annotation/VAR_043696|||http://purl.uniprot.org/annotation/VAR_043697|||http://purl.uniprot.org/annotation/VAR_043698|||http://purl.uniprot.org/annotation/VAR_043699
http://togogenome.org/gene/9606:PUS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WY59|||http://purl.uniprot.org/uniprot/Q9BZE2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||Nucleophile|||Phosphothreonine|||Pseudouridine synthase I TruA alpha/beta|||Removed|||tRNA pseudouridine(38/39) synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057520|||http://purl.uniprot.org/annotation/VAR_030836|||http://purl.uniprot.org/annotation/VAR_030837|||http://purl.uniprot.org/annotation/VAR_030838
http://togogenome.org/gene/9606:NFIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRX8|||http://purl.uniprot.org/uniprot/O00712|||http://purl.uniprot.org/uniprot/Q5VW28                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||In MACID.|||In MACID; likely benign variant; does not affect GFAP transcriptional activation.|||In MACID; significant decrease of GFAP transcriptional activation.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Nuclear factor 1 B-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100195|||http://purl.uniprot.org/annotation/VAR_081859|||http://purl.uniprot.org/annotation/VAR_081860|||http://purl.uniprot.org/annotation/VAR_081861|||http://purl.uniprot.org/annotation/VAR_081862|||http://purl.uniprot.org/annotation/VAR_081863|||http://purl.uniprot.org/annotation/VAR_081864|||http://purl.uniprot.org/annotation/VSP_003545|||http://purl.uniprot.org/annotation/VSP_003546|||http://purl.uniprot.org/annotation/VSP_044462|||http://purl.uniprot.org/annotation/VSP_045065|||http://purl.uniprot.org/annotation/VSP_054713|||http://purl.uniprot.org/annotation/VSP_054714
http://togogenome.org/gene/9606:MPP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUS1|||http://purl.uniprot.org/uniprot/Q96JB8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||L27|||L27 1|||L27 2|||MAGUK p55 subfamily member 4|||PDZ|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094577|||http://purl.uniprot.org/annotation/VAR_022643|||http://purl.uniprot.org/annotation/VAR_050015|||http://purl.uniprot.org/annotation/VSP_003157|||http://purl.uniprot.org/annotation/VSP_003158|||http://purl.uniprot.org/annotation/VSP_003159|||http://purl.uniprot.org/annotation/VSP_003160|||http://purl.uniprot.org/annotation/VSP_013991|||http://purl.uniprot.org/annotation/VSP_013992|||http://purl.uniprot.org/annotation/VSP_013993
http://togogenome.org/gene/9606:ZBTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2K1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to ubiquitin; Abolishes recruitment to DNA lesion sites.|||BTB|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces sumoylation of Lys-328.|||Reduces sumoylation. Does not reduce transcriptional repressive activity. Inhibits sumoylation but does not reduce transcriptional repressive activity; when associated with R-265.|||Reduces sumoylation. Inhibits transcriptional repressive activity. Inhibits sumoylation and reduces transcriptional repressive activity; when associated with R-328.|||UBZ-type|||Zinc finger and BTB domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047707|||http://purl.uniprot.org/annotation/VSP_040976
http://togogenome.org/gene/9606:BMAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic helix-loop-helix ARNT-like protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3, isoform 4, isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 3 and isoform 9.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 9.|||In isoform 6, isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9.|||Interaction with PER2|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273631|||http://purl.uniprot.org/annotation/VAR_030158|||http://purl.uniprot.org/annotation/VAR_030159|||http://purl.uniprot.org/annotation/VSP_022580|||http://purl.uniprot.org/annotation/VSP_022581|||http://purl.uniprot.org/annotation/VSP_022582|||http://purl.uniprot.org/annotation/VSP_022583|||http://purl.uniprot.org/annotation/VSP_022584|||http://purl.uniprot.org/annotation/VSP_022585|||http://purl.uniprot.org/annotation/VSP_044773
http://togogenome.org/gene/9606:KASH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6L0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Perinuclear space|||Protein KASH5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331527|||http://purl.uniprot.org/annotation/VAR_059597|||http://purl.uniprot.org/annotation/VAR_059598
http://togogenome.org/gene/9606:SPDYE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C1S0|||http://purl.uniprot.org/uniprot/Q8NFV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||Speedy protein E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322594
http://togogenome.org/gene/9606:CKAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14008                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1939.|||Abolishes localization to spindle microtubules, no effect on localization to centrosomes and kinetochores; when associated with A-1942.|||Basic and acidic residues|||Cytoskeleton-associated protein 5|||Disordered|||Disrupts interaction with TACC3.|||HEAT 1|||HEAT 10|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||In isoform 3.|||Interaction with TACC3|||N6-acetyllysine|||Phosphoserine|||Polar residues|||TOG 1|||TOG 2|||TOG 3|||TOG 4|||TOG 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089663|||http://purl.uniprot.org/annotation/VAR_045627|||http://purl.uniprot.org/annotation/VSP_035668|||http://purl.uniprot.org/annotation/VSP_036400
http://togogenome.org/gene/9606:PAGE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60829                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of phosphorylation and its ability to potentiate JUN transcriptional activator activity.|||P antigen family member 4|||Phosphoserine; by CLK2|||Phosphoserine; by HIPK1 and CLK2|||Phosphothreonine; by CLK2|||Phosphothreonine; by HIPK1 and CLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148348
http://togogenome.org/gene/9606:INO80C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EIY8|||http://purl.uniprot.org/uniprot/Q6PI98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||INO80 complex subunit C|||In isoform 2.|||In isoform 3.|||Polar residues|||Vps72/YL1 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079317|||http://purl.uniprot.org/annotation/VSP_014531|||http://purl.uniprot.org/annotation/VSP_044967
http://togogenome.org/gene/9606:KCNJ12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14500                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 12|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Interaction with phosphatidylinositides|||Interchain|||PDZ-binding|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||S-nitrosocysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154962|||http://purl.uniprot.org/annotation/VAR_024509|||http://purl.uniprot.org/annotation/VAR_049671|||http://purl.uniprot.org/annotation/VAR_049672|||http://purl.uniprot.org/annotation/VAR_049673|||http://purl.uniprot.org/annotation/VAR_059365|||http://purl.uniprot.org/annotation/VAR_059366|||http://purl.uniprot.org/annotation/VAR_059367|||http://purl.uniprot.org/annotation/VAR_059368
http://togogenome.org/gene/9606:IGFBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JMY1|||http://purl.uniprot.org/uniprot/P18065                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cell attachment site|||Disordered|||Does not disrupt growth-inhibiting activity.|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 2|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014370|||http://purl.uniprot.org/annotation/VAR_018871
http://togogenome.org/gene/9606:KRTAP1-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C5Y4                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 1-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312505
http://togogenome.org/gene/9606:FBXW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKT8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box/WD repeat-containing protein 2|||In isoform 2.|||N6-acetyllysine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050988|||http://purl.uniprot.org/annotation/VSP_012983
http://togogenome.org/gene/9606:RBMY1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDE4|||http://purl.uniprot.org/uniprot/B9EIP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member B|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341537
http://togogenome.org/gene/9606:SEC11C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EJQ7|||http://purl.uniprot.org/uniprot/Q9BY50                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-terminal short (CTS) helix|||Charge relay system|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Loss of catalytic activity.|||Loss of catalytic activity. Slight reduction in protein stability.|||Lumenal|||Moderate reduction in catalytic activity. Reduces protein stability.|||No effect on catalytic activity or protein stability.|||Peptidase S24/S26A/S26B/S26C|||Signal peptidase complex catalytic subunit SEC11C|||Slight reduction in catalytic activity; when associated with D-109.|||Slight reduction in catalytic activity; when associated with R-128.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109548
http://togogenome.org/gene/9606:AFG2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVQ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATPase family gene 2 protein homolog B|||Disordered|||In DFNB119.|||In NEDHLS.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330586|||http://purl.uniprot.org/annotation/VAR_048111|||http://purl.uniprot.org/annotation/VAR_048112|||http://purl.uniprot.org/annotation/VAR_059085|||http://purl.uniprot.org/annotation/VAR_086544|||http://purl.uniprot.org/annotation/VAR_086545|||http://purl.uniprot.org/annotation/VAR_086546|||http://purl.uniprot.org/annotation/VAR_086547|||http://purl.uniprot.org/annotation/VAR_086548|||http://purl.uniprot.org/annotation/VAR_086549|||http://purl.uniprot.org/annotation/VAR_086550|||http://purl.uniprot.org/annotation/VAR_086551|||http://purl.uniprot.org/annotation/VAR_086552|||http://purl.uniprot.org/annotation/VAR_086553|||http://purl.uniprot.org/annotation/VAR_086554|||http://purl.uniprot.org/annotation/VAR_086555|||http://purl.uniprot.org/annotation/VAR_086556|||http://purl.uniprot.org/annotation/VAR_086557|||http://purl.uniprot.org/annotation/VAR_086558|||http://purl.uniprot.org/annotation/VAR_086559|||http://purl.uniprot.org/annotation/VAR_086560|||http://purl.uniprot.org/annotation/VAR_086561|||http://purl.uniprot.org/annotation/VAR_086562|||http://purl.uniprot.org/annotation/VAR_086563|||http://purl.uniprot.org/annotation/VAR_086564|||http://purl.uniprot.org/annotation/VSP_033050|||http://purl.uniprot.org/annotation/VSP_033051|||http://purl.uniprot.org/annotation/VSP_033052|||http://purl.uniprot.org/annotation/VSP_033053
http://togogenome.org/gene/9606:OR5I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVE5|||http://purl.uniprot.org/uniprot/Q13606                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150598|||http://purl.uniprot.org/annotation/VAR_024101|||http://purl.uniprot.org/annotation/VAR_053198|||http://purl.uniprot.org/annotation/VAR_053199|||http://purl.uniprot.org/annotation/VAR_053200
http://togogenome.org/gene/9606:LGALS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05162                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-2|||In a breast cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076924|||http://purl.uniprot.org/annotation/VAR_036570|||http://purl.uniprot.org/annotation/VAR_049767
http://togogenome.org/gene/9606:PCDHB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003936|||http://purl.uniprot.org/annotation/VAR_033710|||http://purl.uniprot.org/annotation/VAR_048554|||http://purl.uniprot.org/annotation/VSP_053862
http://togogenome.org/gene/9606:ORC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8H0|||http://purl.uniprot.org/uniprot/Q13415|||http://purl.uniprot.org/uniprot/Q96F82                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ATPase activity.|||BAH|||Basic and acidic residues|||Disordered|||Histone H4K20me2 binding|||In MGORS1.|||N6-acetyllysine|||Necessary and sufficient for ORC complex assembly|||Origin recognition complex subunit 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127067|||http://purl.uniprot.org/annotation/VAR_014507|||http://purl.uniprot.org/annotation/VAR_014508|||http://purl.uniprot.org/annotation/VAR_014509|||http://purl.uniprot.org/annotation/VAR_014510|||http://purl.uniprot.org/annotation/VAR_014511|||http://purl.uniprot.org/annotation/VAR_014512|||http://purl.uniprot.org/annotation/VAR_014513|||http://purl.uniprot.org/annotation/VAR_014514|||http://purl.uniprot.org/annotation/VAR_050426|||http://purl.uniprot.org/annotation/VAR_065481|||http://purl.uniprot.org/annotation/VAR_065482|||http://purl.uniprot.org/annotation/VAR_065483|||http://purl.uniprot.org/annotation/VAR_065484|||http://purl.uniprot.org/annotation/VAR_065485
http://togogenome.org/gene/9606:RLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04090                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Connecting peptide|||In isoform 2.|||Interchain (between B and A chains)|||Pyrrolidone carboxylic acid|||Relaxin A chain|||Relaxin B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016079|||http://purl.uniprot.org/annotation/PRO_0000016080|||http://purl.uniprot.org/annotation/PRO_0000016081|||http://purl.uniprot.org/annotation/VAR_034444|||http://purl.uniprot.org/annotation/VAR_050007|||http://purl.uniprot.org/annotation/VSP_002711|||http://purl.uniprot.org/annotation/VSP_002712
http://togogenome.org/gene/9606:ATP6AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75787                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by furin-like protease|||Cytoplasmic|||Extracellular|||Helical|||In CDG2R; impairs export from the ER and cleavage, increases N-glycosylation post-translational modification which targets the misfolded protein to degradation via the ER-associated degradation pathway, results in loss of interaction with ATP6AP1.|||In CDG2R; increases degradation rate via the ER-associated degradation pathway; loss of interaction with ATP6AP1.|||In isoform 2.|||Increases cleavage and stability and enhancing localization to the Golgi; when associated with Q-346.|||Increases cleavage and stability enhancing localization to the Golgi; when associated with Q-348.|||Mediates retrograde transport to the ER|||Renin receptor|||Renin receptor C-terminal fragment|||Renin receptor N-terminal fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022203|||http://purl.uniprot.org/annotation/PRO_0000447864|||http://purl.uniprot.org/annotation/PRO_0000447865|||http://purl.uniprot.org/annotation/VAR_051313|||http://purl.uniprot.org/annotation/VAR_051314|||http://purl.uniprot.org/annotation/VAR_082052|||http://purl.uniprot.org/annotation/VAR_082053|||http://purl.uniprot.org/annotation/VSP_056910
http://togogenome.org/gene/9606:SMARCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969G3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HMG box|||In CSS5.|||In MNGMA; found in a case of childhood clear cell meningioma; associated with disease susceptibility.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4 and isoform 5.|||In isoform 5 and isoform 6.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048577|||http://purl.uniprot.org/annotation/VAR_068215|||http://purl.uniprot.org/annotation/VAR_071873|||http://purl.uniprot.org/annotation/VAR_076932|||http://purl.uniprot.org/annotation/VSP_011801|||http://purl.uniprot.org/annotation/VSP_011802|||http://purl.uniprot.org/annotation/VSP_047604|||http://purl.uniprot.org/annotation/VSP_047825|||http://purl.uniprot.org/annotation/VSP_047826
http://togogenome.org/gene/9606:CCDC185                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N715                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 185|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247114|||http://purl.uniprot.org/annotation/VAR_027066|||http://purl.uniprot.org/annotation/VAR_027067|||http://purl.uniprot.org/annotation/VAR_027068|||http://purl.uniprot.org/annotation/VAR_027069
http://togogenome.org/gene/9606:GPR179                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0K8|||http://purl.uniprot.org/uniprot/Q6PRD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cache-like region|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CSNB1E.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Probable G-protein coupled receptor 179                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045397|||http://purl.uniprot.org/annotation/PRO_5001832113|||http://purl.uniprot.org/annotation/VAR_049287|||http://purl.uniprot.org/annotation/VAR_049288|||http://purl.uniprot.org/annotation/VAR_049289|||http://purl.uniprot.org/annotation/VAR_061204|||http://purl.uniprot.org/annotation/VAR_067925|||http://purl.uniprot.org/annotation/VAR_067926|||http://purl.uniprot.org/annotation/VAR_067927|||http://purl.uniprot.org/annotation/VAR_067928
http://togogenome.org/gene/9606:CSTF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12996                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage stimulation factor subunit 3|||Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||HAT 9|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205722|||http://purl.uniprot.org/annotation/VSP_042731|||http://purl.uniprot.org/annotation/VSP_042732|||http://purl.uniprot.org/annotation/VSP_045675|||http://purl.uniprot.org/annotation/VSP_045676
http://togogenome.org/gene/9606:NSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R5R8|||http://purl.uniprot.org/uniprot/P42857                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Neuronal vesicle trafficking-associated protein 1|||Required for GRIP1 interaction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164363|||http://purl.uniprot.org/annotation/VSP_054333
http://togogenome.org/gene/9606:PPID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KN55|||http://purl.uniprot.org/uniprot/Q08752                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with HSP90AB1 and impairs interaction with HSPA8.|||Abolishes interaction with HSP90AB1.|||Chaperone activity|||Impairs interaction with HSP90AB1 and HSPA8.|||Impairs interaction with HSP90AB1.|||Interaction with HSP90AB1|||N6-acetyllysine|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase D|||Phosphoserine|||Removed|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064153|||http://purl.uniprot.org/annotation/VAR_021021|||http://purl.uniprot.org/annotation/VAR_021022|||http://purl.uniprot.org/annotation/VAR_021023|||http://purl.uniprot.org/annotation/VAR_051771
http://togogenome.org/gene/9606:MS4A15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTI9|||http://purl.uniprot.org/uniprot/Q8N5U1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Membrane-spanning 4-domains subfamily A member 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320577|||http://purl.uniprot.org/annotation/VAR_053524|||http://purl.uniprot.org/annotation/VAR_053525|||http://purl.uniprot.org/annotation/VSP_031669|||http://purl.uniprot.org/annotation/VSP_053907
http://togogenome.org/gene/9606:TTYH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYU9|||http://purl.uniprot.org/uniprot/Q9C0H2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect N-glycosylation state.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Induces a stronger permeability to cations.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein tweety homolog 3|||Shows a different ion selectivity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312251|||http://purl.uniprot.org/annotation/PRO_5004315483|||http://purl.uniprot.org/annotation/VSP_029769|||http://purl.uniprot.org/annotation/VSP_029770|||http://purl.uniprot.org/annotation/VSP_042220
http://togogenome.org/gene/9606:COL27A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal propeptide|||Collagen alpha-1(XXVII) chain|||Collagen-like 1|||Collagen-like 10|||Collagen-like 11|||Collagen-like 12|||Collagen-like 13|||Collagen-like 14|||Collagen-like 15|||Collagen-like 16|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Collagen-like 9|||Disordered|||Fibrillar collagen NC1|||In STLS.|||In isoform 2.|||In isoform 3.|||Interchain (with C-1268)|||Interchain (with C-1285)|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Polar residues|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314667|||http://purl.uniprot.org/annotation/PRO_0000314668|||http://purl.uniprot.org/annotation/PRO_5000089163|||http://purl.uniprot.org/annotation/VAR_048784|||http://purl.uniprot.org/annotation/VAR_048785|||http://purl.uniprot.org/annotation/VAR_048786|||http://purl.uniprot.org/annotation/VAR_048787|||http://purl.uniprot.org/annotation/VAR_048788|||http://purl.uniprot.org/annotation/VAR_048789|||http://purl.uniprot.org/annotation/VAR_048790|||http://purl.uniprot.org/annotation/VAR_048791|||http://purl.uniprot.org/annotation/VAR_048792|||http://purl.uniprot.org/annotation/VAR_048793|||http://purl.uniprot.org/annotation/VAR_048794|||http://purl.uniprot.org/annotation/VAR_048795|||http://purl.uniprot.org/annotation/VAR_072564|||http://purl.uniprot.org/annotation/VSP_030347|||http://purl.uniprot.org/annotation/VSP_030348|||http://purl.uniprot.org/annotation/VSP_030349
http://togogenome.org/gene/9606:CNN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15417                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-3|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204776|||http://purl.uniprot.org/annotation/VSP_055191|||http://purl.uniprot.org/annotation/VSP_055192
http://togogenome.org/gene/9606:SEC23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFH5|||http://purl.uniprot.org/uniprot/Q15437                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Gelsolin-like|||In CDAN2.|||In CDAN2; the mutant protein is unstable with less than 5% of protein detectable compared to wild-type.|||In CDAN2; unknown pathological significance.|||In CDAN2; unknown pathological significance; the mutant protein is expressed as the wild-type.|||In CWS7; aberrant aggregation; causes mislocalization of the protein in the cytoplasm; reduces interaction with SAR1A; confers endoplasmic reticulum (ER) stress-mediated cell growth advantage.|||In CWS7; unknown pathological significance.|||N-acetylalanine|||N6-acetyllysine|||Protein transport protein Sec23B|||Removed|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205148|||http://purl.uniprot.org/annotation/VAR_020318|||http://purl.uniprot.org/annotation/VAR_034482|||http://purl.uniprot.org/annotation/VAR_062294|||http://purl.uniprot.org/annotation/VAR_062295|||http://purl.uniprot.org/annotation/VAR_062296|||http://purl.uniprot.org/annotation/VAR_062297|||http://purl.uniprot.org/annotation/VAR_062298|||http://purl.uniprot.org/annotation/VAR_062299|||http://purl.uniprot.org/annotation/VAR_062300|||http://purl.uniprot.org/annotation/VAR_062301|||http://purl.uniprot.org/annotation/VAR_062302|||http://purl.uniprot.org/annotation/VAR_062303|||http://purl.uniprot.org/annotation/VAR_062304|||http://purl.uniprot.org/annotation/VAR_062305|||http://purl.uniprot.org/annotation/VAR_062306|||http://purl.uniprot.org/annotation/VAR_062307|||http://purl.uniprot.org/annotation/VAR_062308|||http://purl.uniprot.org/annotation/VAR_062309|||http://purl.uniprot.org/annotation/VAR_076424|||http://purl.uniprot.org/annotation/VAR_076425|||http://purl.uniprot.org/annotation/VAR_086961|||http://purl.uniprot.org/annotation/VAR_086962
http://togogenome.org/gene/9606:IDUA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35475                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-L-iduronidase|||In IDUA pseudodeficiency.|||In MPS1H and MPS1H/S; in 3% of the MPS1H patients; reduces catalytic activity and protein stability.|||In MPS1H.|||In MPS1H/S and MPS1S.|||In MPS1H/S.|||In MPS1H/S; 0.4% of normal activity.|||In MPS1H/S; 1.5% of normal activity.|||In MPS1H/S; associated with R-423.|||In MPS1H/S; loss of activity.|||In MPS1H/S; reduction of activity and protein levels.|||In MPS1H; MPS1H/S.|||In MPS1H; loss of function; undetectable enzyme activity.|||In MPS1H; uncertain pathological role.|||In MPS1S and MPS1H/S; associated with L-188 in a patient with MPS1H/S; significant reduction of activity and protein levels.|||In MPS1S.|||In MPS1S; 2-3% of normal activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Reduction of protein levels.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012200|||http://purl.uniprot.org/annotation/VAR_003349|||http://purl.uniprot.org/annotation/VAR_003350|||http://purl.uniprot.org/annotation/VAR_003351|||http://purl.uniprot.org/annotation/VAR_003352|||http://purl.uniprot.org/annotation/VAR_003353|||http://purl.uniprot.org/annotation/VAR_003354|||http://purl.uniprot.org/annotation/VAR_003355|||http://purl.uniprot.org/annotation/VAR_003356|||http://purl.uniprot.org/annotation/VAR_003357|||http://purl.uniprot.org/annotation/VAR_003358|||http://purl.uniprot.org/annotation/VAR_003359|||http://purl.uniprot.org/annotation/VAR_003360|||http://purl.uniprot.org/annotation/VAR_003361|||http://purl.uniprot.org/annotation/VAR_003362|||http://purl.uniprot.org/annotation/VAR_003363|||http://purl.uniprot.org/annotation/VAR_003364|||http://purl.uniprot.org/annotation/VAR_003365|||http://purl.uniprot.org/annotation/VAR_003366|||http://purl.uniprot.org/annotation/VAR_003367|||http://purl.uniprot.org/annotation/VAR_003368|||http://purl.uniprot.org/annotation/VAR_003369|||http://purl.uniprot.org/annotation/VAR_003370|||http://purl.uniprot.org/annotation/VAR_003371|||http://purl.uniprot.org/annotation/VAR_003372|||http://purl.uniprot.org/annotation/VAR_003373|||http://purl.uniprot.org/annotation/VAR_003374|||http://purl.uniprot.org/annotation/VAR_003375|||http://purl.uniprot.org/annotation/VAR_003376|||http://purl.uniprot.org/annotation/VAR_003377|||http://purl.uniprot.org/annotation/VAR_003378|||http://purl.uniprot.org/annotation/VAR_003379|||http://purl.uniprot.org/annotation/VAR_017435|||http://purl.uniprot.org/annotation/VAR_017436|||http://purl.uniprot.org/annotation/VAR_017437|||http://purl.uniprot.org/annotation/VAR_020975|||http://purl.uniprot.org/annotation/VAR_020976|||http://purl.uniprot.org/annotation/VAR_020977|||http://purl.uniprot.org/annotation/VAR_020978|||http://purl.uniprot.org/annotation/VAR_020979|||http://purl.uniprot.org/annotation/VAR_020980|||http://purl.uniprot.org/annotation/VAR_020981|||http://purl.uniprot.org/annotation/VAR_020982|||http://purl.uniprot.org/annotation/VAR_020983|||http://purl.uniprot.org/annotation/VAR_020984|||http://purl.uniprot.org/annotation/VAR_020985|||http://purl.uniprot.org/annotation/VAR_020986|||http://purl.uniprot.org/annotation/VAR_020987|||http://purl.uniprot.org/annotation/VAR_066215|||http://purl.uniprot.org/annotation/VAR_066216|||http://purl.uniprot.org/annotation/VAR_066217|||http://purl.uniprot.org/annotation/VAR_066218|||http://purl.uniprot.org/annotation/VAR_066219|||http://purl.uniprot.org/annotation/VAR_066220|||http://purl.uniprot.org/annotation/VAR_066221|||http://purl.uniprot.org/annotation/VAR_066222|||http://purl.uniprot.org/annotation/VAR_066223|||http://purl.uniprot.org/annotation/VAR_066224|||http://purl.uniprot.org/annotation/VAR_066225|||http://purl.uniprot.org/annotation/VAR_066226|||http://purl.uniprot.org/annotation/VAR_066227|||http://purl.uniprot.org/annotation/VAR_066228|||http://purl.uniprot.org/annotation/VAR_066229|||http://purl.uniprot.org/annotation/VAR_066230|||http://purl.uniprot.org/annotation/VAR_066231|||http://purl.uniprot.org/annotation/VAR_072367|||http://purl.uniprot.org/annotation/VAR_072368|||http://purl.uniprot.org/annotation/VSP_057029|||http://purl.uniprot.org/annotation/VSP_057030
http://togogenome.org/gene/9606:PARP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl aspartic acid|||ADP-ribosyl glutamic acid|||Abolished activation by nicked DNA.|||Basic and acidic residues|||Disordered|||Does not affect activation by nicked DNA, while it prevents activation by a 3'-overhang substrate.|||In isoform 2.|||N6-(ADP-ribosyl)lysine|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP3|||Reduced activity on nicked DNA.|||WGR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211329|||http://purl.uniprot.org/annotation/VAR_054622|||http://purl.uniprot.org/annotation/VAR_056643|||http://purl.uniprot.org/annotation/VAR_056644|||http://purl.uniprot.org/annotation/VSP_007863
http://togogenome.org/gene/9606:CD19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15391                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the ability to activate signaling pathways that mediate mobilization of cytoplasmic Ca(2+). Abolishes the ability to restore normal B cell functions and responses to antigenic stimuli.|||Acidic residues|||B-lymphocyte antigen CD19|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on the ability to complement impaired B cell development and functions; when associated with F-348.|||No effect on the ability to complement impaired B cell development and functions; when associated with F-378.|||No effect on the ability to complement impaired B cell development and functions; when associated with F-409.|||No effect on the ability to complement impaired B cell development and functions; when associated with F-421.|||No effect on the ability to complement impaired B cell development and functions; when associated with F-439.|||No effect on the ability to complement impaired B cell development and functions; when associated with F-461.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Strongly reduced tyrosine phosphorylation; when associated with F-500. Abolishes activation of signaling pathways that mediate mobilization of cytoplasmic Ca(2+); when associated with F-500. Abolishes the ability to complement impaired B cell development and functions; when associated with F-500.|||Strongly reduced tyrosine phosphorylation; when associated with F-531. Abolishes activation of signaling pathways that mediate mobilization of cytoplasmic Ca(2+); when associated with F-531. Abolishes the ability to complement impaired B cell development and functions; when associated with F-531.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014648|||http://purl.uniprot.org/annotation/VAR_026963|||http://purl.uniprot.org/annotation/VAR_036987|||http://purl.uniprot.org/annotation/VSP_047194
http://togogenome.org/gene/9606:SF3B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B4                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with pre-mRNA branch site|||N6-acetyllysine|||N6-acetyllysine; alternate|||RRM|||Splicing factor 3B subunit 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081725
http://togogenome.org/gene/9606:RBBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6E9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Interaction with Ebolavirus VP30|||Basic and acidic residues|||Basic residues|||CCHC-type|||DWNN|||Disordered|||E3 ubiquitin-protein ligase RBBP6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RB1|||Interaction with p53|||N6-acetyllysine|||PPxPxY|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234354|||http://purl.uniprot.org/annotation/VAR_026216|||http://purl.uniprot.org/annotation/VAR_051306|||http://purl.uniprot.org/annotation/VAR_051307|||http://purl.uniprot.org/annotation/VSP_018281|||http://purl.uniprot.org/annotation/VSP_018282|||http://purl.uniprot.org/annotation/VSP_018283|||http://purl.uniprot.org/annotation/VSP_018284
http://togogenome.org/gene/9606:UBAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2S7|||http://purl.uniprot.org/uniprot/Q8NBM4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||UBA|||Ubiquitin-associated domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280754|||http://purl.uniprot.org/annotation/VSP_023909|||http://purl.uniprot.org/annotation/VSP_023910|||http://purl.uniprot.org/annotation/VSP_023911|||http://purl.uniprot.org/annotation/VSP_023912|||http://purl.uniprot.org/annotation/VSP_023913|||http://purl.uniprot.org/annotation/VSP_023914
http://togogenome.org/gene/9606:DMPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM55|||http://purl.uniprot.org/uniprot/B4DZE2|||http://purl.uniprot.org/uniprot/E5KR05|||http://purl.uniprot.org/uniprot/E5KR06|||http://purl.uniprot.org/uniprot/E5KR07|||http://purl.uniprot.org/uniprot/I6L989|||http://purl.uniprot.org/uniprot/Q09013                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In a lung small cell carcinoma sample; somatic mutation.|||In isoform 11.|||In isoform 2, isoform 4, isoform 6 and isoform 10.|||In isoform 3 and isoform 4.|||In isoform 5, isoform 6 and isoform 12.|||In isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12.|||In isoform 8.|||In isoform 9.|||Loss of kinase activity.|||Lumenal|||Myotonin-protein kinase|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085924|||http://purl.uniprot.org/annotation/VAR_040452|||http://purl.uniprot.org/annotation/VAR_058334|||http://purl.uniprot.org/annotation/VSP_042098|||http://purl.uniprot.org/annotation/VSP_042099|||http://purl.uniprot.org/annotation/VSP_042100|||http://purl.uniprot.org/annotation/VSP_042101|||http://purl.uniprot.org/annotation/VSP_042102|||http://purl.uniprot.org/annotation/VSP_042103|||http://purl.uniprot.org/annotation/VSP_042104|||http://purl.uniprot.org/annotation/VSP_042105
http://togogenome.org/gene/9606:C20orf173                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LM9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Uncharacterized protein C20orf173                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079483|||http://purl.uniprot.org/annotation/VAR_024334|||http://purl.uniprot.org/annotation/VSP_040891
http://togogenome.org/gene/9606:COMMD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJ95|||http://purl.uniprot.org/uniprot/Q53FR9|||http://purl.uniprot.org/uniprot/Q9P000                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||COMM|||COMM domain-containing protein 9|||Disordered|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077403|||http://purl.uniprot.org/annotation/VSP_041499
http://togogenome.org/gene/9606:ADAM30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBZ7|||http://purl.uniprot.org/uniprot/Q9UKF2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 9 AA approximate repeats|||Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 30|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform Beta.|||Loss of enzymatic activity; when associated with L-338 and L-342.|||Loss of enzymatic activity; when associated with L-338 and L-348.|||Loss of enzymatic activity; when associated with L-342 and L-348.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029136|||http://purl.uniprot.org/annotation/PRO_0000029137|||http://purl.uniprot.org/annotation/PRO_5004315145|||http://purl.uniprot.org/annotation/VAR_024597|||http://purl.uniprot.org/annotation/VAR_061738|||http://purl.uniprot.org/annotation/VSP_005494
http://togogenome.org/gene/9606:PTPN18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99952                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphocysteine intermediate|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094773|||http://purl.uniprot.org/annotation/VAR_047651|||http://purl.uniprot.org/annotation/VSP_043073
http://togogenome.org/gene/9606:MARCKSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49006                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Effector domain involved in lipid-binding and calmodulin-binding|||MARCKS-related protein|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157152
http://togogenome.org/gene/9606:SPIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y657                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone H3K4me3 and H3R8me2a binding|||Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway.|||Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA.|||Impaired binding to histone H3K4me3 and H3R8me2a.|||Impaired binding to histone H3K4me3.|||Impaired phosphorylation.|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by AURKA|||Spindlin-1|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181367|||http://purl.uniprot.org/annotation/VAR_053690
http://togogenome.org/gene/9606:CAVIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969G5                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Caveolae-associated protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CAV1|||Interaction with CAVIN1|||Leucine-zipper|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331412|||http://purl.uniprot.org/annotation/VAR_042851|||http://purl.uniprot.org/annotation/VAR_042852|||http://purl.uniprot.org/annotation/VAR_042853|||http://purl.uniprot.org/annotation/VAR_042854
http://togogenome.org/gene/9606:PPM1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SGD2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PPM-type phosphatase|||Protein phosphatase 1L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057754|||http://purl.uniprot.org/annotation/VAR_050622|||http://purl.uniprot.org/annotation/VSP_016927|||http://purl.uniprot.org/annotation/VSP_037552|||http://purl.uniprot.org/annotation/VSP_037553|||http://purl.uniprot.org/annotation/VSP_037554|||http://purl.uniprot.org/annotation/VSP_037555
http://togogenome.org/gene/9606:MSANTD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H12                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Myb-like|||Myb/SANT-like DNA-binding domain-containing protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292590|||http://purl.uniprot.org/annotation/VSP_053346|||http://purl.uniprot.org/annotation/VSP_053347
http://togogenome.org/gene/9606:ANKRD33B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCL7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 33B|||Basic and acidic residues|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328769
http://togogenome.org/gene/9606:ETAA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ATR-activation domain (AAD)|||Basic and acidic residues|||Disordered|||Ewing's tumor-associated antigen 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Polar residues|||RBM1 motif|||RBM2 motif|||Reduced ability to promote replication fork progression and integrity following DNA damage.|||Reduced interaction with ATR.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280099|||http://purl.uniprot.org/annotation/VAR_031053|||http://purl.uniprot.org/annotation/VAR_031054|||http://purl.uniprot.org/annotation/VAR_031055|||http://purl.uniprot.org/annotation/VAR_031056|||http://purl.uniprot.org/annotation/VAR_035916
http://togogenome.org/gene/9606:ZNF155                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12901                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 155                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047431|||http://purl.uniprot.org/annotation/VAR_035571|||http://purl.uniprot.org/annotation/VAR_057399|||http://purl.uniprot.org/annotation/VAR_060272|||http://purl.uniprot.org/annotation/VAR_060273|||http://purl.uniprot.org/annotation/VAR_069362|||http://purl.uniprot.org/annotation/VSP_047207
http://togogenome.org/gene/9606:PARD6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with PARD3 and CDC42|||Interaction with PRKCI and PRKCZ|||Loss of interaction with ECT2 and PRKCI.|||PB1|||PDZ|||Partitioning defective 6 homolog alpha|||Phosphoserine|||Polar residues|||Pseudo-CRIB|||Slight decrease of interaction with PRKCI. Loss of interaction with PRKCI; when associated with A-28.|||Slight decrease of interaction with PRKCI. Loss of interaction with PRKCI; when associated with A-89.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112513|||http://purl.uniprot.org/annotation/VAR_050454|||http://purl.uniprot.org/annotation/VSP_007459
http://togogenome.org/gene/9606:ING5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GW41|||http://purl.uniprot.org/uniprot/Q8WYH8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Histone H3K4me3 binding|||In isoform 2.|||Inhibitor of growth protein 5|||Inhibitor of growth protein N-terminal histone-binding|||N6-acetyllysine|||Omega-N-methylarginine|||PHD-type|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212671|||http://purl.uniprot.org/annotation/VSP_012528
http://togogenome.org/gene/9606:ST20-MTHFS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYL1                                                                                  ^@                                                                                  Binding Site|||Site                                                                                  ^@                                                                                  Binding Site                                                                                  ^@                                                                                                                                                                    ^@                                                                                  
http://togogenome.org/gene/9606:PTCD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EY7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||PPR 1|||PPR 10|||PPR 2|||PPR 3|||PPR 4|||PPR 5|||PPR 6|||PPR 7|||PPR 8|||PPR 9|||Small ribosomal subunit protein mS39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305028|||http://purl.uniprot.org/annotation/VAR_035154|||http://purl.uniprot.org/annotation/VAR_035155|||http://purl.uniprot.org/annotation/VSP_028191|||http://purl.uniprot.org/annotation/VSP_028192
http://togogenome.org/gene/9606:CD276                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGH0|||http://purl.uniprot.org/uniprot/A8K9J6|||http://purl.uniprot.org/uniprot/Q5ZPR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CD276 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045801|||http://purl.uniprot.org/annotation/VAR_049857|||http://purl.uniprot.org/annotation/VAR_049858|||http://purl.uniprot.org/annotation/VAR_049859|||http://purl.uniprot.org/annotation/VAR_049860|||http://purl.uniprot.org/annotation/VAR_049861|||http://purl.uniprot.org/annotation/VAR_049862|||http://purl.uniprot.org/annotation/VAR_049863|||http://purl.uniprot.org/annotation/VAR_049864|||http://purl.uniprot.org/annotation/VAR_049865|||http://purl.uniprot.org/annotation/VSP_017088|||http://purl.uniprot.org/annotation/VSP_017089|||http://purl.uniprot.org/annotation/VSP_017090|||http://purl.uniprot.org/annotation/VSP_017091
http://togogenome.org/gene/9606:TFEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14948                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Necessary for transcriptional transactivation|||Polar residues|||Transcription factor EC|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313564|||http://purl.uniprot.org/annotation/VAR_037661|||http://purl.uniprot.org/annotation/VAR_037662|||http://purl.uniprot.org/annotation/VAR_037663|||http://purl.uniprot.org/annotation/VSP_030022|||http://purl.uniprot.org/annotation/VSP_030023|||http://purl.uniprot.org/annotation/VSP_030024|||http://purl.uniprot.org/annotation/VSP_030025|||http://purl.uniprot.org/annotation/VSP_030026
http://togogenome.org/gene/9606:BLOC1S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0F0|||http://purl.uniprot.org/uniprot/Q6QNY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Biogenesis of lysosome-related organelles complex 1 subunit 2|||Disordered|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234543|||http://purl.uniprot.org/annotation/VAR_054068|||http://purl.uniprot.org/annotation/VSP_018350
http://togogenome.org/gene/9606:LILRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75019                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||Leukocyte immunoglobulin-like receptor subfamily A member 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014816|||http://purl.uniprot.org/annotation/VAR_049886|||http://purl.uniprot.org/annotation/VAR_049887|||http://purl.uniprot.org/annotation/VAR_059396|||http://purl.uniprot.org/annotation/VSP_008454
http://togogenome.org/gene/9606:ELF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78545                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  9aaTAD|||Disordered|||ETS|||ETS-related transcription factor Elf-3|||In isoform 2.|||No effect on transcriptional repression on KRT4 promoter.|||PNT|||Partially abrogates repressive effect on the KRT4 promoter.|||Partially abrogates repressive effect on the KRT4 promoter; when associated with A-315.|||Partially abrogates repressive effect on the KRT4 promoter; when associated with A-319.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287681|||http://purl.uniprot.org/annotation/VAR_048945|||http://purl.uniprot.org/annotation/VSP_052433
http://togogenome.org/gene/9606:GPR119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDV5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glucose-dependent insulinotropic receptor|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069607|||http://purl.uniprot.org/annotation/VAR_037221
http://togogenome.org/gene/9606:FOXO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12778                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished deacetylation by SIRT6.|||Abolishes PKB/AKT1-mediated phosphorylation but does not prevent phosphorylation of Ser-24 or Ser-256. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with A-24 and A-256. Targeted to the nucleus and enhances transactivation; when associated with A-24.|||Abolishes PKB/AKT1-mediated phosphorylation but does not prevent phosphorylation of Ser-256 or Ser-319. Also inhibits binding of 14-3-3 proteins. Nuclear in unstimulated cells, and little export to cytoplasm on IGF1 stimulation. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with A-256 and A-319. Targeted to the nucleus and enhances transactivation; when associated with A-319.|||Abolishes STK4/MST1-mediated phosphorylation.|||Completely abolishes PKB/AKT1-mediated phosphorylation at all three sites, and inhibits binding of 14-3-3 proteins. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with or without A-24 and A-319. Nuclear in unstimulated cells, and little export to cytoplasm on IGF1 stimulation. Abolishes the ability of IGF1 to suppress transactivation. Prevents T-24 and S-319 phosphorylation. Enhances transactivation; when associated with A-24 and A-319.|||DNA-binding|||Disordered|||Disrupts DNA-binding; when associated with A-245.|||Disrupts DNA-binding; when associated with A-248.|||Does not affect deacetylation by SIRT6.|||Fork-head|||Forkhead box protein O1|||Impaired phosphorylation by CDK1.|||Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-262 and R-265.|||Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-262 and R-274.|||Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-265 and R-274.|||N6-acetyllysine|||No effect on DNA-binding.|||No targeting to the nucleus and disruption of DNA-binding.|||Nuclear localization signal|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CK1|||Phosphoserine; by CK1 and SGK1|||Phosphoserine; by DYRK1A|||Phosphoserine; by PKB/AKT1|||Phosphoserine; by PKB/AKT1 and SGK1|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1 or PKB/AKT2 and SGK1|||Polar residues|||Pro residues|||Reduces DNA binding, promotes nuclear exclusion and partially promotes T-24 and S-319 phosphorylation. Reduces DNA binding, does not promote nuclear exclusion but reduces transactivation; when associated with A-24 and A-319.|||Required for interaction with RUNX2|||Required for interaction with SIRT1|||Sufficient for interaction with NLK|||Targeted to the nucleus and enhances transactivation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091872
http://togogenome.org/gene/9606:PCBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15365|||http://purl.uniprot.org/uniprot/Q53SS8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||K Homology|||KH 1|||KH 2|||KH 3|||N-acetylmethionine|||Phosphoserine|||Poly(rC)-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050087
http://togogenome.org/gene/9606:ACP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZG2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In AI1J.|||In AI1J; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Testicular acid phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259643|||http://purl.uniprot.org/annotation/VAR_078014|||http://purl.uniprot.org/annotation/VAR_078015|||http://purl.uniprot.org/annotation/VAR_078016|||http://purl.uniprot.org/annotation/VAR_078017|||http://purl.uniprot.org/annotation/VAR_078018|||http://purl.uniprot.org/annotation/VSP_021493|||http://purl.uniprot.org/annotation/VSP_021494|||http://purl.uniprot.org/annotation/VSP_021495
http://togogenome.org/gene/9606:RNF138                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJT9|||http://purl.uniprot.org/uniprot/Q8WVD3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2HC RNF-type|||Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination.|||Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination; when associated with A-18.|||Catalytic inactive mutant that abolishes ability to promote DNA resection and homologous recombination; when associated with A-54.|||Disordered|||E3 ubiquitin-protein ligase RNF138|||In isoform 2.|||N-acetylalanine|||Phosphothreonine|||RING-type|||Removed|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261607|||http://purl.uniprot.org/annotation/VAR_052109|||http://purl.uniprot.org/annotation/VSP_021732
http://togogenome.org/gene/9606:OR13D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGV5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150737|||http://purl.uniprot.org/annotation/VAR_055070|||http://purl.uniprot.org/annotation/VAR_055071|||http://purl.uniprot.org/annotation/VAR_055072|||http://purl.uniprot.org/annotation/VAR_055073
http://togogenome.org/gene/9606:MCEE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Methylmalonyl-CoA epimerase, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||VOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012283|||http://purl.uniprot.org/annotation/VAR_019511|||http://purl.uniprot.org/annotation/VAR_049248
http://togogenome.org/gene/9606:LRRC39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DD0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232580|||http://purl.uniprot.org/annotation/VAR_034087|||http://purl.uniprot.org/annotation/VSP_017913
http://togogenome.org/gene/9606:ZNF681                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N22                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5; degenerate|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 681                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305137|||http://purl.uniprot.org/annotation/VAR_035167|||http://purl.uniprot.org/annotation/VAR_035168|||http://purl.uniprot.org/annotation/VAR_063679|||http://purl.uniprot.org/annotation/VAR_063680|||http://purl.uniprot.org/annotation/VSP_039878
http://togogenome.org/gene/9606:WFDC10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUB3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein WFDC10B|||WAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041388|||http://purl.uniprot.org/annotation/VAR_052952|||http://purl.uniprot.org/annotation/VSP_007552
http://togogenome.org/gene/9606:CTSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07858|||http://purl.uniprot.org/uniprot/Q5HYG5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin B|||Cathepsin B heavy chain|||Cathepsin B light chain|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Peptidase C1A papain C-terminal|||Peptidase C1A propeptide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026143|||http://purl.uniprot.org/annotation/PRO_0000026144|||http://purl.uniprot.org/annotation/PRO_0000026145|||http://purl.uniprot.org/annotation/PRO_0000026146|||http://purl.uniprot.org/annotation/PRO_0000026147|||http://purl.uniprot.org/annotation/PRO_5018774595|||http://purl.uniprot.org/annotation/VAR_006724|||http://purl.uniprot.org/annotation/VAR_014696|||http://purl.uniprot.org/annotation/VAR_051511|||http://purl.uniprot.org/annotation/VAR_051512
http://togogenome.org/gene/9606:ERC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15083                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||ERC protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087002|||http://purl.uniprot.org/annotation/VAR_050973
http://togogenome.org/gene/9606:ANKRD60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZ19                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 60|||Disordered|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000414175|||http://purl.uniprot.org/annotation/VAR_014400
http://togogenome.org/gene/9606:PGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCD5|||http://purl.uniprot.org/uniprot/A0A0A0MS75|||http://purl.uniprot.org/uniprot/A0A0S2Z568|||http://purl.uniprot.org/uniprot/A8MYS5|||http://purl.uniprot.org/uniprot/H0YDQ4|||http://purl.uniprot.org/uniprot/Q9UHJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In HPMRS3.|||In isoform 1.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Lumenal|||Polar residues|||Post-GPI attachment to proteins factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326094|||http://purl.uniprot.org/annotation/VAR_069664|||http://purl.uniprot.org/annotation/VAR_069665|||http://purl.uniprot.org/annotation/VAR_069666|||http://purl.uniprot.org/annotation/VAR_069667|||http://purl.uniprot.org/annotation/VAR_069668|||http://purl.uniprot.org/annotation/VAR_088424|||http://purl.uniprot.org/annotation/VSP_032550|||http://purl.uniprot.org/annotation/VSP_032551|||http://purl.uniprot.org/annotation/VSP_045984|||http://purl.uniprot.org/annotation/VSP_045985|||http://purl.uniprot.org/annotation/VSP_053800
http://togogenome.org/gene/9606:ZNF571                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5U8|||http://purl.uniprot.org/uniprot/Q7Z3V5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 571                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047662|||http://purl.uniprot.org/annotation/VAR_023953|||http://purl.uniprot.org/annotation/VAR_023954|||http://purl.uniprot.org/annotation/VAR_023955|||http://purl.uniprot.org/annotation/VAR_031093|||http://purl.uniprot.org/annotation/VAR_052869
http://togogenome.org/gene/9606:ZNF585B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52M93                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 585B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047679|||http://purl.uniprot.org/annotation/VAR_059923
http://togogenome.org/gene/9606:GUCY1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z685|||http://purl.uniprot.org/uniprot/B7Z6G8|||http://purl.uniprot.org/uniprot/B7Z9H9|||http://purl.uniprot.org/uniprot/D6RC99|||http://purl.uniprot.org/uniprot/E9PCN2|||http://purl.uniprot.org/uniprot/Q02153                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Guanylate cyclase|||Guanylate cyclase soluble subunit beta-1|||In isoform 3.|||In isoform HSGC-2.|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074116|||http://purl.uniprot.org/annotation/VSP_001813|||http://purl.uniprot.org/annotation/VSP_054365
http://togogenome.org/gene/9606:DACH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3I1|||http://purl.uniprot.org/uniprot/Q96NX9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  DACHbox-C|||DACHbox-N|||Dachshund homolog 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||SKI/SNO/DAC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095599|||http://purl.uniprot.org/annotation/VSP_009490|||http://purl.uniprot.org/annotation/VSP_009491|||http://purl.uniprot.org/annotation/VSP_009492|||http://purl.uniprot.org/annotation/VSP_044275
http://togogenome.org/gene/9606:COQ10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZV9|||http://purl.uniprot.org/uniprot/B8ZZX2|||http://purl.uniprot.org/uniprot/Q9H8M1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Coenzyme Q-binding protein COQ10 START|||Coenzyme Q-binding protein COQ10 homolog B, mitochondrial|||In isoform 2.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228647|||http://purl.uniprot.org/annotation/VAR_033823|||http://purl.uniprot.org/annotation/VSP_056949
http://togogenome.org/gene/9606:DYNLT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW35                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Dynein light chain Tctex-type protein 2B|||In SRTD17.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316869|||http://purl.uniprot.org/annotation/VAR_078554
http://togogenome.org/gene/9606:PHF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75151                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to H3K4me2 and H3K4me3.|||Abolishes demethylase activity.|||Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056.|||Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954.|||Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056.|||Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056.|||Basic and acidic residues|||Disordered|||Does not alter iron-binding nor activates histone demethylase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||JmjC|||Lysine-specific demethylase PHF2|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059290|||http://purl.uniprot.org/annotation/VAR_047553|||http://purl.uniprot.org/annotation/VAR_051598
http://togogenome.org/gene/9606:SLC22A15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZD6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338619|||http://purl.uniprot.org/annotation/VAR_043813|||http://purl.uniprot.org/annotation/VSP_034059|||http://purl.uniprot.org/annotation/VSP_034060
http://togogenome.org/gene/9606:C1GALT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RA32|||http://purl.uniprot.org/uniprot/Q9NS00                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285064|||http://purl.uniprot.org/annotation/VSP_024809
http://togogenome.org/gene/9606:SPATA31D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C874                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Spermatogenesis-associated protein 31D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349241
http://togogenome.org/gene/9606:WWOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A411HBC7|||http://purl.uniprot.org/uniprot/Q9NZC7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with LITAF.|||Abolishes interaction with TP53, TP73, MAPK8 and ERBB4. Partial loss of interaction with TFAP2C. Loss of phosphorylation. Loss of the proapoptotic activity. Abolishes binding to VOPP1.|||Disordered|||Found in a esophageal cancer sample; somatic mutation.|||Found in a primary colorectal tumor and tumor cells.|||In DEE28.|||In SCAR12.|||In a Burkitt lymphoma cell line.|||In a primary colorectal tumor and a histiocytic lymphoma cell line.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with MAPT|||Loss of phosphorylation by TNK2.|||Loss of phosphorylation.|||Mediates targeting to the mitochondria|||No effect on interaction with LITAF.|||No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with T-28.|||No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with V-29.|||No effect on interaction with TP73.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by TNK2|||Proton acceptor|||WW|||WW 1|||WW 2|||WW domain-containing oxidoreductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054815|||http://purl.uniprot.org/annotation/VAR_023916|||http://purl.uniprot.org/annotation/VAR_023917|||http://purl.uniprot.org/annotation/VAR_023918|||http://purl.uniprot.org/annotation/VAR_023919|||http://purl.uniprot.org/annotation/VAR_023920|||http://purl.uniprot.org/annotation/VAR_023921|||http://purl.uniprot.org/annotation/VAR_023922|||http://purl.uniprot.org/annotation/VAR_023923|||http://purl.uniprot.org/annotation/VAR_052323|||http://purl.uniprot.org/annotation/VAR_070992|||http://purl.uniprot.org/annotation/VAR_070993|||http://purl.uniprot.org/annotation/VAR_072351|||http://purl.uniprot.org/annotation/VAR_082915|||http://purl.uniprot.org/annotation/VSP_016358|||http://purl.uniprot.org/annotation/VSP_016359|||http://purl.uniprot.org/annotation/VSP_016360|||http://purl.uniprot.org/annotation/VSP_016362|||http://purl.uniprot.org/annotation/VSP_016363|||http://purl.uniprot.org/annotation/VSP_016364|||http://purl.uniprot.org/annotation/VSP_016365|||http://purl.uniprot.org/annotation/VSP_016366|||http://purl.uniprot.org/annotation/VSP_016367|||http://purl.uniprot.org/annotation/VSP_016369
http://togogenome.org/gene/9606:C4orf36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KX1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C4orf36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268820|||http://purl.uniprot.org/annotation/VAR_029755|||http://purl.uniprot.org/annotation/VAR_056784
http://togogenome.org/gene/9606:XAGE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||X antigen family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148350
http://togogenome.org/gene/9606:SSU72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes phosphatase activity.|||In isoform 2.|||RNA polymerase II subunit A C-terminal domain phosphatase SSU72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330012|||http://purl.uniprot.org/annotation/VSP_033005
http://togogenome.org/gene/9606:PRRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FWE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Proline-rich transmembrane protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251978|||http://purl.uniprot.org/annotation/VAR_027745|||http://purl.uniprot.org/annotation/VAR_027746|||http://purl.uniprot.org/annotation/VAR_061695|||http://purl.uniprot.org/annotation/VAR_061696|||http://purl.uniprot.org/annotation/VAR_061697|||http://purl.uniprot.org/annotation/VSP_020845|||http://purl.uniprot.org/annotation/VSP_020846|||http://purl.uniprot.org/annotation/VSP_020847
http://togogenome.org/gene/9606:NAALADL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQQ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aminopeptidase NAALADL1|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of enzyme activity.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174123|||http://purl.uniprot.org/annotation/VAR_057155|||http://purl.uniprot.org/annotation/VAR_057156|||http://purl.uniprot.org/annotation/VAR_057157|||http://purl.uniprot.org/annotation/VSP_005343|||http://purl.uniprot.org/annotation/VSP_005344|||http://purl.uniprot.org/annotation/VSP_005345|||http://purl.uniprot.org/annotation/VSP_005346|||http://purl.uniprot.org/annotation/VSP_005347|||http://purl.uniprot.org/annotation/VSP_005348|||http://purl.uniprot.org/annotation/VSP_005349|||http://purl.uniprot.org/annotation/VSP_005350|||http://purl.uniprot.org/annotation/VSP_005351|||http://purl.uniprot.org/annotation/VSP_005352|||http://purl.uniprot.org/annotation/VSP_005353
http://togogenome.org/gene/9606:TNP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05952|||http://purl.uniprot.org/uniprot/Q4VB56                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Nuclear localization signal|||Nuclear transition protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191425|||http://purl.uniprot.org/annotation/VAR_052157
http://togogenome.org/gene/9606:ZNF696                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7X3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Zinc finger protein 696                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233278
http://togogenome.org/gene/9606:GRHPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N605|||http://purl.uniprot.org/uniprot/Q9UBQ7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding|||D-isomer specific 2-hydroxyacid dehydrogenase catalytic|||Glyoxylate reductase/hydroxypyruvate reductase|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Proton donor|||Raises pKa of active site His                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075944|||http://purl.uniprot.org/annotation/VAR_032762|||http://purl.uniprot.org/annotation/VSP_057016|||http://purl.uniprot.org/annotation/VSP_057017|||http://purl.uniprot.org/annotation/VSP_057018
http://togogenome.org/gene/9606:CEP57L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYX8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein CEP57L1|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189534|||http://purl.uniprot.org/annotation/VAR_052396|||http://purl.uniprot.org/annotation/VSP_055660|||http://purl.uniprot.org/annotation/VSP_055661
http://togogenome.org/gene/9606:ABHD17B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEH9|||http://purl.uniprot.org/uniprot/Q5VST6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha/beta hydrolase domain-containing protein 17B|||Charge relay system|||In isoform 2.|||Peptidase S9 prolyl oligopeptidase catalytic|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281111|||http://purl.uniprot.org/annotation/VAR_031230|||http://purl.uniprot.org/annotation/VAR_054080|||http://purl.uniprot.org/annotation/VSP_023975
http://togogenome.org/gene/9606:HLA-B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5FQ95|||http://purl.uniprot.org/uniprot/P01889                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Alpha-3|||Bw6 motif|||Connecting peptide|||Cytoplasmic|||Disordered|||Extracellular|||HLA class I histocompatibility antigen, B alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01 allele B*39:02, allele B*40:02, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01.|||In allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*59:01 and allele B*78:01.|||In allele B*08:01, allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*59:01 and allele B*78:01; requires 2 nucleotide substitutions.|||In allele B*08:01, allele B*13:02, allele B*14:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*42:01, allele B*45:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01, allele B*81:01 and allele B*82:01.|||In allele B*08:01, allele B*13:02, allele B*15:01, allele B*35:01, allele B*40:01, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01.|||In allele B*08:01, allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*53:01, allele B*54:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*81:01 and allele B*82:01.|||In allele B*08:01, allele B*14:01, allele B*18:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*41:01, allele B*42:01, allele B*54:01, allele B*55:01, allele B*59:01 and allele B*67:01; requires 2 nucleotide substitutions.|||In allele B*08:01, allele B*35:01, allele B*51:01, allele B*53:01, allele B*59:01 and allele B*78:01.|||In allele B*08:01, allele B*37:01, allele B*41:01, allele B*42:01, allele B*44:02, allele B*45:01 and allele B*82:01; requires 2 nucleotide substitutions.|||In allele B*08:01; associated with increased risk for rheumatoid arthritis.|||In allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:02, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01.|||In allele B*13:02, allele B*14:01, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*78:01 and allele B*82:01.|||In allele B*13:02, allele B*14:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*81:01.|||In allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01.|||In allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*46:01, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01, allele B*81:01 and allele B*82:01.|||In allele B*13:02, allele B*15:01, allele B*18:01, allele B*27:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01.|||In allele B*13:02, allele B*15:01, allele B*18:01, allele B*37:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01 and allele B*52:01.|||In allele B*13:02, allele B*15:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*39:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*48:01, allele B*49:01, allele B*50:01, allele B*52:01, allele B*57:01 and allele B*58:01; requires 2 nucleotide substitutions.|||In allele B*13:02, allele B*15:01, allele B*46:01 and allele B*57:01.|||In allele B*13:02, allele B*15:01, allele B*46:01 and allele B*57:01; requires 2 nucleotide substitutions.|||In allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01, allele B*78:01, allele B*81:01 and allele B*82:01.|||In allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*35:01, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01, allele B*78:01 and allele B*81:01.|||In allele B*13:02, allele B*18:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*40:02, allele B*44:02, allele B*47:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01 and allele B*82:01.|||In allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*38:01, allele B*44:02, allele B*47:01, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01; part of Bw4 motif involved in the recognition of KIR3DL1.|||In allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01.|||In allele B*13:02, allele B*27:01, allele B*27:05, allele B*37:01, allele B*44:02 and allele B*47:01.|||In allele B*13:02, allele B*27:01, allele B*27:05, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01, allele B*50:01 and allele B*73:01.|||In allele B*13:02, allele B*27:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01.|||In allele B*13:02, allele B*27:01, allele B*38:01, allele B*44:02, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01, allele B*58:01 and allele B*59:01; requires 2 nucleotide substitutions.|||In allele B*13:02, allele B*35:01, allele B*45:01, allele B*49:01, allele B*50:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01 and allele B*82:01.|||In allele B*13:02, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01.|||In allele B*13:02, allele B*41:01, allele B*45:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*73:01 and allele B*78:01.|||In allele B*13:02, allele B*45:01, allele B*49:01, allele B*50:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01 and allele B*82:01; requires 2 nucleotide substitutions.|||In allele B*13:02, allele B*51:01, allele B*52:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*59:01, allele B*73:01 and allele B*78:01.|||In allele B*13:02.|||In allele B*14:01, allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*67:01, allele B*73:01, allele B*78:01 and allele B*82:01.|||In allele B*14:01, allele B*18:01, allele B*51:01, allele B*52:01, allele B*73:01 and allele B*78:01.|||In allele B*14:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01, allele B*50:01 and allele B*73:01.|||In allele B*14:01, allele B*27:01, allele B*27:05, allele B*38:01 and allele B*73:01.|||In allele B*14:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*67:01 and allele B*73:01.|||In allele B*14:01.|||In allele B*15:01 and allele B*46:01.|||In allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*38:01, allele B*39:02, allele B*40:01, allele B*41:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*47:01, allele B*49:01, allele B*50:01, allele B*53:01, allele B*58:01, allele B*67:01 and allele B*82:01.|||In allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*73:01, allele B*78:01 and allele B*82:01.|||In allele B*15:01, allele B*18:01, allele B*35:01, allele B*37:01, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*58:01, allele B*59:01, allele B*78:01 and allele B*82:01.|||In allele B*15:01, allele B*18:01, allele B*35:01, allele B*46:01, allele B*53:01, allele B*57:01 and allele B*58:01.|||In allele B*15:01, allele B*35:01, allele B*44:02, allele B*45:01, allele B*46:01, allele B*49:01, allele B*50:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*78:01 and allele B*82:01; requires 2 nucleotide substitutions.|||In allele B*15:01, allele B*35:01, allele B*46:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*54:01, allele B*55:01, allele B*56:01, allele B*57:01, allele B*58:01, allele B*59:01 and allele B*78:01.|||In allele B*18:01, allele B*27:01, allele B*27:05, allele B*37:01, allele B*40:01, allele B*40:02, allele B*41:01, allele B*45:01, allele B*49:01, allele B*50:01 and allele B*73:01.|||In allele B*18:01, allele B*35:01, allele B*37:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*58:01 and allele B*78:01; requires 2 nucleotide substitutions.|||In allele B*18:01.|||In allele B*27:01 and allele B*27:05.|||In allele B*27:01, allele B*27:05 and allele B*47:01.|||In allele B*27:01, allele B*27:05 and allele B*73:01.|||In allele B*27:01, allele B*27:05, allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01.|||In allele B*27:01, allele B*27:05, allele B*44:02 and allele B*47:01.|||In allele B*27:05, allele B*37:01 and allele B*47:01; requires 2 nucleotide substitutions.|||In allele B*35:01, allele B*37:01, allele B*44:02, allele B*53:01, allele B*57:01 and allele B*58:01.|||In allele B*35:01, allele B*44:02, allele B*53:01, allele B*57:01 and allele B*58:01.|||In allele B*35:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*58:01 and allele B*78:01.|||In allele B*37:01.|||In allele B*38:01, allele B*39:02 and allele B*67:01.|||In allele B*38:01, allele B*49:01, allele B*51:01, allele B*52:01, allele B*53:01, allele B*57:01 and allele B*59:01; part of Bw4 motif involved in the recognition of KIR3DL1.|||In allele B*40:01, allele B*40:02, allele B*41:01, allele B*44:02, allele B*45:01, allele B*47:01, allele B*49:01 and allele B*50:01.|||In allele B*40:01, allele B*48:01 and allele B*81:01.|||In allele B*44:02, allele B*45:01 and allele B*82:01.|||In allele B*44:02.|||In allele B*46:01 and allele B*73:01.|||In allele B*46:01.|||In allele B*46:01; requires 2 nucleotide substitutions.|||In allele B*47:01 and allele B*82:01.|||In allele B*47:01.|||In allele B*48:01, allele B*81:01.|||In allele B*54:01.|||In allele B*57:01 and allele B*58:01.|||In allele B*57:01 and allele B*58:01; requires 2 nucleotide substitutions.|||In allele B*57:01; requires 2 nucleotide substitutions.|||In allele B*73:01.|||In allele B*73:01; requires 2 nucleotide substitutions.|||In allele B*82:01.|||N-linked (GlcNAc...) asparagine|||Polar residues|||VL9 epitope ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018833|||http://purl.uniprot.org/annotation/PRO_5015090251|||http://purl.uniprot.org/annotation/VAR_082483|||http://purl.uniprot.org/annotation/VAR_082484|||http://purl.uniprot.org/annotation/VAR_082485|||http://purl.uniprot.org/annotation/VAR_082486|||http://purl.uniprot.org/annotation/VAR_082487|||http://purl.uniprot.org/annotation/VAR_082488|||http://purl.uniprot.org/annotation/VAR_082489|||http://purl.uniprot.org/annotation/VAR_082490|||http://purl.uniprot.org/annotation/VAR_082491|||http://purl.uniprot.org/annotation/VAR_082492|||http://purl.uniprot.org/annotation/VAR_082493|||http://purl.uniprot.org/annotation/VAR_082494|||http://purl.uniprot.org/annotation/VAR_082495|||http://purl.uniprot.org/annotation/VAR_082496|||http://purl.uniprot.org/annotation/VAR_082497|||http://purl.uniprot.org/annotation/VAR_082498|||http://purl.uniprot.org/annotation/VAR_082499|||http://purl.uniprot.org/annotation/VAR_082500|||http://purl.uniprot.org/annotation/VAR_082501|||http://purl.uniprot.org/annotation/VAR_082502|||http://purl.uniprot.org/annotation/VAR_082503|||http://purl.uniprot.org/annotation/VAR_082504|||http://purl.uniprot.org/annotation/VAR_082505|||http://purl.uniprot.org/annotation/VAR_082506|||http://purl.uniprot.org/annotation/VAR_082507|||http://purl.uniprot.org/annotation/VAR_082508|||http://purl.uniprot.org/annotation/VAR_082509|||http://purl.uniprot.org/annotation/VAR_082510|||http://purl.uniprot.org/annotation/VAR_082511|||http://purl.uniprot.org/annotation/VAR_082512|||http://purl.uniprot.org/annotation/VAR_082513|||http://purl.uniprot.org/annotation/VAR_082514|||http://purl.uniprot.org/annotation/VAR_082515|||http://purl.uniprot.org/annotation/VAR_082516|||http://purl.uniprot.org/annotation/VAR_082517|||http://purl.uniprot.org/annotation/VAR_082518|||http://purl.uniprot.org/annotation/VAR_082519|||http://purl.uniprot.org/annotation/VAR_082520|||http://purl.uniprot.org/annotation/VAR_082521|||http://purl.uniprot.org/annotation/VAR_082522|||http://purl.uniprot.org/annotation/VAR_082523|||http://purl.uniprot.org/annotation/VAR_082524|||http://purl.uniprot.org/annotation/VAR_082525|||http://purl.uniprot.org/annotation/VAR_082526|||http://purl.uniprot.org/annotation/VAR_082527|||http://purl.uniprot.org/annotation/VAR_082528|||http://purl.uniprot.org/annotation/VAR_082529|||http://purl.uniprot.org/annotation/VAR_082530|||http://purl.uniprot.org/annotation/VAR_082531|||http://purl.uniprot.org/annotation/VAR_082532|||http://purl.uniprot.org/annotation/VAR_082533|||http://purl.uniprot.org/annotation/VAR_082534|||http://purl.uniprot.org/annotation/VAR_082535|||http://purl.uniprot.org/annotation/VAR_082536|||http://purl.uniprot.org/annotation/VAR_082537|||http://purl.uniprot.org/annotation/VAR_082538|||http://purl.uniprot.org/annotation/VAR_082539|||http://purl.uniprot.org/annotation/VAR_082540|||http://purl.uniprot.org/annotation/VAR_082541|||http://purl.uniprot.org/annotation/VAR_082542|||http://purl.uniprot.org/annotation/VAR_082543|||http://purl.uniprot.org/annotation/VAR_082544|||http://purl.uniprot.org/annotation/VAR_082545|||http://purl.uniprot.org/annotation/VAR_082546|||http://purl.uniprot.org/annotation/VAR_082547|||http://purl.uniprot.org/annotation/VAR_082548|||http://purl.uniprot.org/annotation/VAR_082549|||http://purl.uniprot.org/annotation/VAR_082550|||http://purl.uniprot.org/annotation/VAR_082551|||http://purl.uniprot.org/annotation/VAR_082552|||http://purl.uniprot.org/annotation/VAR_082553|||http://purl.uniprot.org/annotation/VAR_082554|||http://purl.uniprot.org/annotation/VAR_082555|||http://purl.uniprot.org/annotation/VAR_082556|||http://purl.uniprot.org/annotation/VAR_082557|||http://purl.uniprot.org/annotation/VAR_082558|||http://purl.uniprot.org/annotation/VAR_082559|||http://purl.uniprot.org/annotation/VAR_082560|||http://purl.uniprot.org/annotation/VAR_082561|||http://purl.uniprot.org/annotation/VAR_082562|||http://purl.uniprot.org/annotation/VAR_082563|||http://purl.uniprot.org/annotation/VAR_082564|||http://purl.uniprot.org/annotation/VAR_082565|||http://purl.uniprot.org/annotation/VAR_082566|||http://purl.uniprot.org/annotation/VAR_082567|||http://purl.uniprot.org/annotation/VAR_082568|||http://purl.uniprot.org/annotation/VAR_082569|||http://purl.uniprot.org/annotation/VAR_082570|||http://purl.uniprot.org/annotation/VAR_082571|||http://purl.uniprot.org/annotation/VAR_082572|||http://purl.uniprot.org/annotation/VAR_082573|||http://purl.uniprot.org/annotation/VAR_082574|||http://purl.uniprot.org/annotation/VAR_082575|||http://purl.uniprot.org/annotation/VAR_082576|||http://purl.uniprot.org/annotation/VAR_082577|||http://purl.uniprot.org/annotation/VAR_082578|||http://purl.uniprot.org/annotation/VAR_082579
http://togogenome.org/gene/9606:CT47A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:HAND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61296                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Heart- and neural crest derivatives-expressed protein 2|||In isoform 2.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127191|||http://purl.uniprot.org/annotation/VSP_056880|||http://purl.uniprot.org/annotation/VSP_056881
http://togogenome.org/gene/9606:TRIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3T7C7|||http://purl.uniprot.org/uniprot/Q53F11|||http://purl.uniprot.org/uniprot/Q9H3H1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Core aggregation region|||Disordered|||In COXPD35.|||In COXPD35; reduced tRNA dimethylallyltransferase activity.|||In COXPD35; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with isopentenylpyrophosphate transferase|||Interaction with substrate tRNA|||Matrin-type|||Mitochondrion|||Phosphoserine|||U1-type|||tRNA dimethylallyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019023|||http://purl.uniprot.org/annotation/VAR_020486|||http://purl.uniprot.org/annotation/VAR_080745|||http://purl.uniprot.org/annotation/VAR_080746|||http://purl.uniprot.org/annotation/VAR_080747|||http://purl.uniprot.org/annotation/VAR_080748|||http://purl.uniprot.org/annotation/VAR_080749|||http://purl.uniprot.org/annotation/VAR_080750|||http://purl.uniprot.org/annotation/VAR_085917|||http://purl.uniprot.org/annotation/VSP_010719|||http://purl.uniprot.org/annotation/VSP_010720|||http://purl.uniprot.org/annotation/VSP_010721|||http://purl.uniprot.org/annotation/VSP_012415|||http://purl.uniprot.org/annotation/VSP_053746|||http://purl.uniprot.org/annotation/VSP_053747
http://togogenome.org/gene/9606:GCKR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFN2|||http://purl.uniprot.org/uniprot/Q14397                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with GCK. Abolishes inhibition of GCK.|||Associated with high triglyceride levels and low fasting plasma glucose levels; associated with a reduced risk for type 2 diabetes; the mutant protein is less efficiently regulated by physiological concentrations of fructose-6 phosphate.|||Essential for interaction with GCK|||Glucokinase regulatory protein|||Impairs inhibition of glucokinase.|||Important for interaction with GCK|||In isoform 2.|||No effect on inhibition of glucokinase.|||SIS|||SIS 1|||SIS 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214826|||http://purl.uniprot.org/annotation/VAR_008906|||http://purl.uniprot.org/annotation/VAR_018849|||http://purl.uniprot.org/annotation/VAR_018850|||http://purl.uniprot.org/annotation/VAR_018851|||http://purl.uniprot.org/annotation/VSP_054853|||http://purl.uniprot.org/annotation/VSP_054854
http://togogenome.org/gene/9606:PTBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2RVZ4|||http://purl.uniprot.org/uniprot/B4DSS8|||http://purl.uniprot.org/uniprot/B4DSU5|||http://purl.uniprot.org/uniprot/Q9UKA9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||N-acetylmethionine|||Phosphoserine|||Polypyrimidine tract-binding protein 2|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232928|||http://purl.uniprot.org/annotation/VSP_018015|||http://purl.uniprot.org/annotation/VSP_018016|||http://purl.uniprot.org/annotation/VSP_018017|||http://purl.uniprot.org/annotation/VSP_018018
http://togogenome.org/gene/9606:TDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN41|||http://purl.uniprot.org/uniprot/G3V2F4|||http://purl.uniprot.org/uniprot/Q9NUW8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  125-fold reduction in activity.|||15000-fold reduction in activity.|||3000-fold reduction in activity; abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA.|||Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA.|||Basic and acidic residues|||Disordered|||In SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA.|||In autosomal recessive or sporadic spinocerebellar ataxia affected Japanese individuals.|||In isoform 2.|||Interaction with DNA|||Loss of activity.|||No effect.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor/acceptor|||Reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA.|||Reduces the activity to nearly undetectable levels.|||Slightly reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA.|||Tyrosyl-DNA phosphodiesterase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212486|||http://purl.uniprot.org/annotation/VAR_017144|||http://purl.uniprot.org/annotation/VAR_017145|||http://purl.uniprot.org/annotation/VAR_025817|||http://purl.uniprot.org/annotation/VAR_025818|||http://purl.uniprot.org/annotation/VAR_025819|||http://purl.uniprot.org/annotation/VAR_025820|||http://purl.uniprot.org/annotation/VAR_025821|||http://purl.uniprot.org/annotation/VAR_025822|||http://purl.uniprot.org/annotation/VSP_055765|||http://purl.uniprot.org/annotation/VSP_055766
http://togogenome.org/gene/9606:RGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z494|||http://purl.uniprot.org/uniprot/A0A0S2Z498|||http://purl.uniprot.org/uniprot/P47804                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In RP44.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||RPE-retinal G protein-coupled receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197822|||http://purl.uniprot.org/annotation/VAR_017034|||http://purl.uniprot.org/annotation/VAR_017055|||http://purl.uniprot.org/annotation/VAR_017056|||http://purl.uniprot.org/annotation/VAR_017057|||http://purl.uniprot.org/annotation/VAR_017058|||http://purl.uniprot.org/annotation/VSP_003773|||http://purl.uniprot.org/annotation/VSP_038387
http://togogenome.org/gene/9606:SMAD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15198                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In PPH2; affects SMAD-mediated signaling.|||In isoform B.|||MH1|||MH2|||Mothers against decapentaplegic homolog 9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090875|||http://purl.uniprot.org/annotation/VAR_066871|||http://purl.uniprot.org/annotation/VSP_006182
http://togogenome.org/gene/9606:NKX2-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15522                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Nkx-2.8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048943|||http://purl.uniprot.org/annotation/VAR_003753
http://togogenome.org/gene/9606:ARID5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14865                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 5B|||Abolishes methylation and FSK-dependent DNA-binding of the PHF2-ARID5B complex to promoters.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N6,N6-dimethyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200581|||http://purl.uniprot.org/annotation/VSP_009355|||http://purl.uniprot.org/annotation/VSP_009356|||http://purl.uniprot.org/annotation/VSP_041560|||http://purl.uniprot.org/annotation/VSP_041561
http://togogenome.org/gene/9606:EXT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16394                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes heparan-sulfate biosynthesis.|||Cytoplasmic|||Exostosin-1|||Helical; Signal-anchor for type II membrane protein|||In EXT1.|||In EXT1; loss of activity.|||In EXT1; loss of activity; still able to form an oligomeric complex.|||In EXT1; no loss of activity.|||In chondrosarcoma; no loss of activity.|||In isolated osteochondroma; somatic mutation.|||In multiple osteochondromas.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on heparan-sulfate biosynthesis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149648|||http://purl.uniprot.org/annotation/VAR_002370|||http://purl.uniprot.org/annotation/VAR_002371|||http://purl.uniprot.org/annotation/VAR_002372|||http://purl.uniprot.org/annotation/VAR_002373|||http://purl.uniprot.org/annotation/VAR_002374|||http://purl.uniprot.org/annotation/VAR_002375|||http://purl.uniprot.org/annotation/VAR_002376|||http://purl.uniprot.org/annotation/VAR_002377|||http://purl.uniprot.org/annotation/VAR_012815|||http://purl.uniprot.org/annotation/VAR_012816|||http://purl.uniprot.org/annotation/VAR_012817|||http://purl.uniprot.org/annotation/VAR_012818|||http://purl.uniprot.org/annotation/VAR_012819|||http://purl.uniprot.org/annotation/VAR_012820|||http://purl.uniprot.org/annotation/VAR_012821|||http://purl.uniprot.org/annotation/VAR_012822
http://togogenome.org/gene/9606:TMEM123                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N131                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Porimin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045058|||http://purl.uniprot.org/annotation/VAR_053023|||http://purl.uniprot.org/annotation/VAR_053024|||http://purl.uniprot.org/annotation/VAR_053025|||http://purl.uniprot.org/annotation/VSP_016605
http://togogenome.org/gene/9606:MAB21L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU29|||http://purl.uniprot.org/uniprot/Q08AI8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mab-21-like HhH/H2TH-like|||Protein mab-21-like 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288449|||http://purl.uniprot.org/annotation/VAR_032419|||http://purl.uniprot.org/annotation/VAR_050714|||http://purl.uniprot.org/annotation/VSP_025679|||http://purl.uniprot.org/annotation/VSP_025680|||http://purl.uniprot.org/annotation/VSP_025681|||http://purl.uniprot.org/annotation/VSP_025682
http://togogenome.org/gene/9606:SFRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU3|||http://purl.uniprot.org/uniprot/B3KSM5|||http://purl.uniprot.org/uniprot/Q96HF1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  FZ|||NTR|||Secreted frizzled-related protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032542|||http://purl.uniprot.org/annotation/PRO_5007491839|||http://purl.uniprot.org/annotation/VAR_051963
http://togogenome.org/gene/9606:PDK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15120                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Histidine kinase|||In CMTX6; gain of function; results in a 5-fold increase in kinase activity, decreased sensitivity to pyruvate inhibition, reduced affinity for nucleotides and increased affinity for pyruvate dehydrogenase complex component E2 (PDC-E2), leading to PDC hyperphosphorylation and increased inactivation.|||In a head & neck squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||No effect on kinase activity; when associated with H-120.|||No effect on kinase activity; when associated with N-121.|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023443|||http://purl.uniprot.org/annotation/VAR_042297|||http://purl.uniprot.org/annotation/VAR_070081|||http://purl.uniprot.org/annotation/VAR_070082|||http://purl.uniprot.org/annotation/VAR_070083|||http://purl.uniprot.org/annotation/VSP_043365
http://togogenome.org/gene/9606:RSPH14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHP6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Radial spoke head 14 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097511|||http://purl.uniprot.org/annotation/VAR_015443
http://togogenome.org/gene/9606:MTURN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3F0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of abiity to promote megakaryocyte differentiation, enhance ERK and JNK signaling and up-regulate the expression of FLI1.|||Maturin|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294233|||http://purl.uniprot.org/annotation/VSP_026608|||http://purl.uniprot.org/annotation/VSP_026609|||http://purl.uniprot.org/annotation/VSP_053525
http://togogenome.org/gene/9606:DRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y295                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxylysine|||Developmentally-regulated GTP-binding protein 1|||Impairs JMJD7-mediated hydroxylation.|||N-acetylserine|||OBG-type G|||Phosphothreonine; by STK16|||Reduces the GTPase activity.|||Removed|||Required for interaction with STK16|||TGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205424
http://togogenome.org/gene/9606:ZMAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Polar residues|||Zinc finger matrin-type protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310779|||http://purl.uniprot.org/annotation/VSP_040093
http://togogenome.org/gene/9606:C11orf71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K8C2|||http://purl.uniprot.org/uniprot/Q6IPW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C11orf71                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274325|||http://purl.uniprot.org/annotation/VSP_022711
http://togogenome.org/gene/9606:SORBS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3WKF2|||http://purl.uniprot.org/uniprot/B7Z3D7|||http://purl.uniprot.org/uniprot/B7Z997|||http://purl.uniprot.org/uniprot/O94875                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Alanine amide|||Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 8, isoform 9, isoform 10 and isoform 12.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3, isoform 4, isoform 5, isoform 10 and isoform 12.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 9.|||In isoform 7.|||In isoform 8.|||In isoform 9 and isoform 12.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SoHo|||Sorbin and SH3 domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344477|||http://purl.uniprot.org/annotation/VAR_045624|||http://purl.uniprot.org/annotation/VSP_034791|||http://purl.uniprot.org/annotation/VSP_034792|||http://purl.uniprot.org/annotation/VSP_034793|||http://purl.uniprot.org/annotation/VSP_034794|||http://purl.uniprot.org/annotation/VSP_034795|||http://purl.uniprot.org/annotation/VSP_034796|||http://purl.uniprot.org/annotation/VSP_034797|||http://purl.uniprot.org/annotation/VSP_034798|||http://purl.uniprot.org/annotation/VSP_034799|||http://purl.uniprot.org/annotation/VSP_043665|||http://purl.uniprot.org/annotation/VSP_043666|||http://purl.uniprot.org/annotation/VSP_045640|||http://purl.uniprot.org/annotation/VSP_045641|||http://purl.uniprot.org/annotation/VSP_046219|||http://purl.uniprot.org/annotation/VSP_046220|||http://purl.uniprot.org/annotation/VSP_047056
http://togogenome.org/gene/9606:PRH1-TAS2R14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW62                                                                                  ^@                                                                                  Region|||Transmembrane                                                                                  ^@                                                                                  Transmembrane                                                                                  ^@                                                                                  Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ASAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRP2|||http://purl.uniprot.org/uniprot/Q8TDY4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3|||C4-type|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||PH|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232887|||http://purl.uniprot.org/annotation/VAR_035612|||http://purl.uniprot.org/annotation/VAR_048295|||http://purl.uniprot.org/annotation/VSP_018013|||http://purl.uniprot.org/annotation/VSP_039827
http://togogenome.org/gene/9606:TSPYL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Polar residues|||Testis-specific Y-encoded-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307277|||http://purl.uniprot.org/annotation/VAR_035393|||http://purl.uniprot.org/annotation/VAR_035394
http://togogenome.org/gene/9606:MPPE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR93|||http://purl.uniprot.org/uniprot/Q53F39                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Affects subcellular localization.|||Affects transport of GPI-anchor proteins.|||Calcineurin-like phosphoesterase|||Di-lysine motif|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Metallophosphoesterase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315727|||http://purl.uniprot.org/annotation/VAR_038294|||http://purl.uniprot.org/annotation/VAR_038295|||http://purl.uniprot.org/annotation/VAR_038296|||http://purl.uniprot.org/annotation/VAR_038297|||http://purl.uniprot.org/annotation/VSP_030679|||http://purl.uniprot.org/annotation/VSP_030680|||http://purl.uniprot.org/annotation/VSP_030681|||http://purl.uniprot.org/annotation/VSP_030682|||http://purl.uniprot.org/annotation/VSP_030683
http://togogenome.org/gene/9606:YIPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y548                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein YIPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240868|||http://purl.uniprot.org/annotation/VSP_019437
http://togogenome.org/gene/9606:ZNF662                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS27                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 662                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251196|||http://purl.uniprot.org/annotation/VAR_061961|||http://purl.uniprot.org/annotation/VSP_020745|||http://purl.uniprot.org/annotation/VSP_053783|||http://purl.uniprot.org/annotation/VSP_053784|||http://purl.uniprot.org/annotation/VSP_053785
http://togogenome.org/gene/9606:UBE2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63146                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082447
http://togogenome.org/gene/9606:NR3C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0ZBF6|||http://purl.uniprot.org/uniprot/P08235                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes aldosterone binding and transcription transactivation.|||Abolishes steroid binding and transcription transactivation.|||Alters receptor specificity.|||Decreased coactivator binding.|||Decreased mineralocorticoid receptor activity.|||Decreases aldosterone-binding and cortisol-binding.|||Disordered|||Hinge|||Important for coactivator binding|||In EOHSEP; alters receptor specificity and leads to constitutive activation.|||In PHA1A.|||In PHA1A; abolishes transcription transactivation upon aldosterone binding.|||In PHA1A; abolishes translocation to the nucleus and transcription transactivation upon aldosterone binding.|||In PHA1A; loss of aldosterone binding and transcription transactivation.|||In PHA1A; reduces affinity for aldosterone and transcription transactivation.|||In PHA1A; reduces aldosterone binding.|||In PHA1A; reduces transcription transactivation upon aldosterone binding.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increases aldosterone-binding.|||Loss of coactivator binding.|||Loss of transcription transactivation.|||Mineralocorticoid receptor|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Pro residues|||Reduces aldosterone binding and abolishes transcription transactivation.|||Reduces aldosterone binding and transcription transactivation.|||Reduces transcription transactivation.|||Slightly reduces aldosterone binding and abolishes transcription transactivation.|||Slightly reduces aldosterone binding and transcription transactivation.|||Strong decrease of transcription transactivation.|||Strongly decreases affinity for aldosterone and transcription transactivation.|||Variant of uncertain significance; changed mineralocorticoid receptor activity; changed response curve to aldosterone stimulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053682|||http://purl.uniprot.org/annotation/VAR_014623|||http://purl.uniprot.org/annotation/VAR_014624|||http://purl.uniprot.org/annotation/VAR_014625|||http://purl.uniprot.org/annotation/VAR_014626|||http://purl.uniprot.org/annotation/VAR_015625|||http://purl.uniprot.org/annotation/VAR_015626|||http://purl.uniprot.org/annotation/VAR_015627|||http://purl.uniprot.org/annotation/VAR_029311|||http://purl.uniprot.org/annotation/VAR_031268|||http://purl.uniprot.org/annotation/VAR_031269|||http://purl.uniprot.org/annotation/VAR_031270|||http://purl.uniprot.org/annotation/VAR_031271|||http://purl.uniprot.org/annotation/VAR_031272|||http://purl.uniprot.org/annotation/VAR_031273|||http://purl.uniprot.org/annotation/VAR_031274|||http://purl.uniprot.org/annotation/VAR_031275|||http://purl.uniprot.org/annotation/VAR_031276|||http://purl.uniprot.org/annotation/VAR_031277|||http://purl.uniprot.org/annotation/VAR_031278|||http://purl.uniprot.org/annotation/VAR_031279|||http://purl.uniprot.org/annotation/VAR_036063|||http://purl.uniprot.org/annotation/VSP_007357|||http://purl.uniprot.org/annotation/VSP_007358|||http://purl.uniprot.org/annotation/VSP_007359|||http://purl.uniprot.org/annotation/VSP_007360
http://togogenome.org/gene/9606:GAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY12                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H/ACA ribonucleoprotein complex subunit 1|||In isoform 2.|||RGG-box 1|||RGG-box 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208552|||http://purl.uniprot.org/annotation/VSP_014594
http://togogenome.org/gene/9606:VIPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNY6|||http://purl.uniprot.org/uniprot/P32241                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform Long.|||N-linked (GlcNAc...) asparagine|||Vasoactive intestinal polypeptide receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012855|||http://purl.uniprot.org/annotation/VAR_020021|||http://purl.uniprot.org/annotation/VAR_055041|||http://purl.uniprot.org/annotation/VSP_002010|||http://purl.uniprot.org/annotation/VSP_045143|||http://purl.uniprot.org/annotation/VSP_047271|||http://purl.uniprot.org/annotation/VSP_047272|||http://purl.uniprot.org/annotation/VSP_047273
http://togogenome.org/gene/9606:SLC22A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76082                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In CDSP.|||In CDSP; carnitine transport is reduced to less than 1% of normal.|||In CDSP; carnitine transport is reduced to less than 5% of normal.|||In CDSP; carnitine transport reduced to 1% of wild-type.|||In CDSP; carnitine transport reduced to 2% of wild-type.|||In CDSP; carnitine transport reduced to 20% of wild-type.|||In CDSP; carnitine transport reduced to less than 1% of wild-type.|||In CDSP; carnitine transport reduced to less than 10% of wild-type.|||In CDSP; carnitine transport reduced to less than 2% of wild-type.|||In CDSP; carnitine transport reduced to less than 20% of wild-type.|||In CDSP; carnitine transport reduced to less than 5% of wild-type.|||In CDSP; carnitine transport reduced to less than 6% of wild-type.|||In CDSP; loss of carnitine transport but stimulated organic cation transport; no effect on protein expression.|||In CDSP; loss of carnitine transport.|||In CDSP; markedly reduced carnitine transport compared to the wild-type protein; less than 1% of wild-type activity.|||In CDSP; may affect splicing; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity.|||In CDSP; reduces carnitine transport to 5% of wild-type activity.|||In CDSP; reduces carnitine transport to 5% of wild-type.|||In CDSP; reduces carnitine transport to less than 1% of normal.|||In CDSP; reduces carnitine transport to less than 1% of wild-type activity.|||In CDSP; reduces carnitine transport to less than 1% of wild-type.|||In CDSP; reduces carnitine transport to less than 10% of wild-type activity.|||In CDSP; reduces carnitine transport to less than 10% of wild-type.|||In CDSP; reduces carnitine transport to less than 2% of wild-type activity.|||In CDSP; reduces carnitine transport to less than 2% of wild-type.|||In CDSP; reduces carnitine transport to less than 20% of wild-type activity.|||In CDSP; reduces carnitine transport to less than 20% of wild-type.|||In CDSP; reduces carnitine transport to less than 5% of wild-type activity.|||In CDSP; reduces carnitine transport to less than 5% of wild-type.|||In CDSP; reduces carnitine transport to less-than-1% to 3% of wild-type activity.|||In CDSP; requires 2 nucleotide substitutions; reduces carnitine transport to less than 20% of wild-type activity.|||In CDSP; unknown pathological significance; no effect on carnitine transport.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 30% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 50% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 60% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains 70% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 25% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 30% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 40% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport but the mutant retains more than 60% of wild-type activity.|||In CDSP; unknown pathological significance; reduces carnitine transport to 40% of wild-type.|||In CDSP; unknown pathological significance; reduces carnitine transport to less than 20% of wild-type.|||In isoform 2.|||In isoform 3.|||Loss of both carnitine and organic cation transport functionalities. No effect on protein expression.|||N-linked (GlcNAc...) asparagine|||Organic cation/carnitine transporter 2|||Phosphothreonine|||Phosphotyrosine|||Reduces carnitine transport but the mutant retains more than 20% of wild-type activity.|||Reduces carnitine transport but the mutant retains more than 60% of wild-type activity.|||Reduces expression to 50%. No effect on carnitine transporter activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220500|||http://purl.uniprot.org/annotation/VAR_009252|||http://purl.uniprot.org/annotation/VAR_009253|||http://purl.uniprot.org/annotation/VAR_009254|||http://purl.uniprot.org/annotation/VAR_009255|||http://purl.uniprot.org/annotation/VAR_009256|||http://purl.uniprot.org/annotation/VAR_009257|||http://purl.uniprot.org/annotation/VAR_020347|||http://purl.uniprot.org/annotation/VAR_020348|||http://purl.uniprot.org/annotation/VAR_020349|||http://purl.uniprot.org/annotation/VAR_020350|||http://purl.uniprot.org/annotation/VAR_022564|||http://purl.uniprot.org/annotation/VAR_022565|||http://purl.uniprot.org/annotation/VAR_022566|||http://purl.uniprot.org/annotation/VAR_029315|||http://purl.uniprot.org/annotation/VAR_029316|||http://purl.uniprot.org/annotation/VAR_029317|||http://purl.uniprot.org/annotation/VAR_036816|||http://purl.uniprot.org/annotation/VAR_064109|||http://purl.uniprot.org/annotation/VAR_064110|||http://purl.uniprot.org/annotation/VAR_064111|||http://purl.uniprot.org/annotation/VAR_064112|||http://purl.uniprot.org/annotation/VAR_064113|||http://purl.uniprot.org/annotation/VAR_064114|||http://purl.uniprot.org/annotation/VAR_064115|||http://purl.uniprot.org/annotation/VAR_064116|||http://purl.uniprot.org/annotation/VAR_064117|||http://purl.uniprot.org/annotation/VAR_064118|||http://purl.uniprot.org/annotation/VAR_064119|||http://purl.uniprot.org/annotation/VAR_064120|||http://purl.uniprot.org/annotation/VAR_064121|||http://purl.uniprot.org/annotation/VAR_064122|||http://purl.uniprot.org/annotation/VAR_064123|||http://purl.uniprot.org/annotation/VAR_064124|||http://purl.uniprot.org/annotation/VAR_064125|||http://purl.uniprot.org/annotation/VAR_064126|||http://purl.uniprot.org/annotation/VAR_064127|||http://purl.uniprot.org/annotation/VAR_064128|||http://purl.uniprot.org/annotation/VAR_064129|||http://purl.uniprot.org/annotation/VAR_064130|||http://purl.uniprot.org/annotation/VAR_064131|||http://purl.uniprot.org/annotation/VAR_064132|||http://purl.uniprot.org/annotation/VAR_064133|||http://purl.uniprot.org/annotation/VAR_064134|||http://purl.uniprot.org/annotation/VAR_064135|||http://purl.uniprot.org/annotation/VAR_064136|||http://purl.uniprot.org/annotation/VAR_064137|||http://purl.uniprot.org/annotation/VAR_064138|||http://purl.uniprot.org/annotation/VAR_064139|||http://purl.uniprot.org/annotation/VAR_064140|||http://purl.uniprot.org/annotation/VAR_064141|||http://purl.uniprot.org/annotation/VAR_064142|||http://purl.uniprot.org/annotation/VAR_064143|||http://purl.uniprot.org/annotation/VAR_064144|||http://purl.uniprot.org/annotation/VAR_064145|||http://purl.uniprot.org/annotation/VAR_064146|||http://purl.uniprot.org/annotation/VAR_064147|||http://purl.uniprot.org/annotation/VAR_064148|||http://purl.uniprot.org/annotation/VAR_064149|||http://purl.uniprot.org/annotation/VAR_064150|||http://purl.uniprot.org/annotation/VAR_064151|||http://purl.uniprot.org/annotation/VAR_064152|||http://purl.uniprot.org/annotation/VAR_066842|||http://purl.uniprot.org/annotation/VAR_066843|||http://purl.uniprot.org/annotation/VAR_066844|||http://purl.uniprot.org/annotation/VAR_066845|||http://purl.uniprot.org/annotation/VAR_066846|||http://purl.uniprot.org/annotation/VAR_079640|||http://purl.uniprot.org/annotation/VAR_079641|||http://purl.uniprot.org/annotation/VAR_079642|||http://purl.uniprot.org/annotation/VAR_079643|||http://purl.uniprot.org/annotation/VAR_079644|||http://purl.uniprot.org/annotation/VAR_079645|||http://purl.uniprot.org/annotation/VAR_079646|||http://purl.uniprot.org/annotation/VAR_079647|||http://purl.uniprot.org/annotation/VAR_079648|||http://purl.uniprot.org/annotation/VAR_079649|||http://purl.uniprot.org/annotation/VAR_079650|||http://purl.uniprot.org/annotation/VAR_079651|||http://purl.uniprot.org/annotation/VAR_079652|||http://purl.uniprot.org/annotation/VAR_079653|||http://purl.uniprot.org/annotation/VAR_079654|||http://purl.uniprot.org/annotation/VAR_079655|||http://purl.uniprot.org/annotation/VAR_079656|||http://purl.uniprot.org/annotation/VAR_079657|||http://purl.uniprot.org/annotation/VAR_079658|||http://purl.uniprot.org/annotation/VAR_079659|||http://purl.uniprot.org/annotation/VAR_079660|||http://purl.uniprot.org/annotation/VAR_079661|||http://purl.uniprot.org/annotation/VAR_079662|||http://purl.uniprot.org/annotation/VAR_079663|||http://purl.uniprot.org/annotation/VAR_079664|||http://purl.uniprot.org/annotation/VAR_079665|||http://purl.uniprot.org/annotation/VAR_079666|||http://purl.uniprot.org/annotation/VAR_079667|||http://purl.uniprot.org/annotation/VAR_079668|||http://purl.uniprot.org/annotation/VAR_079669|||http://purl.uniprot.org/annotation/VAR_079670|||http://purl.uniprot.org/annotation/VAR_079671|||http://purl.uniprot.org/annotation/VAR_079672|||http://purl.uniprot.org/annotation/VAR_079673|||http://purl.uniprot.org/annotation/VAR_079674|||http://purl.uniprot.org/annotation/VAR_079675|||http://purl.uniprot.org/annotation/VAR_079676|||http://purl.uniprot.org/annotation/VAR_079677|||http://purl.uniprot.org/annotation/VAR_079678|||http://purl.uniprot.org/annotation/VAR_079679|||http://purl.uniprot.org/annotation/VAR_079680|||http://purl.uniprot.org/annotation/VAR_079681|||http://purl.uniprot.org/annotation/VAR_079682|||http://purl.uniprot.org/annotation/VAR_079683|||http://purl.uniprot.org/annotation/VAR_079684|||http://purl.uniprot.org/annotation/VSP_011120|||http://purl.uniprot.org/annotation/VSP_011121|||http://purl.uniprot.org/annotation/VSP_043904
http://togogenome.org/gene/9606:CDNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AH0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cerebral dopamine neurotrophic factor|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281137|||http://purl.uniprot.org/annotation/VSP_023986
http://togogenome.org/gene/9606:TM7SF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76062                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Delta(14)-sterol reductase TM7SF2|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207500|||http://purl.uniprot.org/annotation/VAR_012716|||http://purl.uniprot.org/annotation/VAR_052153|||http://purl.uniprot.org/annotation/VSP_017898
http://togogenome.org/gene/9606:EDA2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBZ9|||http://purl.uniprot.org/uniprot/B4DQY6|||http://purl.uniprot.org/uniprot/Q9HAV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes TRAF6 association.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058938|||http://purl.uniprot.org/annotation/VAR_044511|||http://purl.uniprot.org/annotation/VAR_044512|||http://purl.uniprot.org/annotation/VSP_011568|||http://purl.uniprot.org/annotation/VSP_011569
http://togogenome.org/gene/9606:USF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DE3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic helix-loop-helix domain-containing protein USF3|||Disordered|||Polar residues|||Rare variant; may be a risk factor for epithelial thyroid carcinoma; results in increased epithelial-mesenchimal transition when coexpressed with 1470-Q--Q-1472 del.|||Rare variant; may be a risk factor for epithelial thyroid carcinoma; results in increased epithelial-mesenchimal transition when coexpressed with Q-1472 del.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295754|||http://purl.uniprot.org/annotation/VAR_033363|||http://purl.uniprot.org/annotation/VAR_033364|||http://purl.uniprot.org/annotation/VAR_055949|||http://purl.uniprot.org/annotation/VAR_055950|||http://purl.uniprot.org/annotation/VAR_063263|||http://purl.uniprot.org/annotation/VAR_080041|||http://purl.uniprot.org/annotation/VAR_080042
http://togogenome.org/gene/9606:DNAJC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75061                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 4 AA approximate tandem repeats|||C2 tensin-type|||Disordered|||In PARK19B; patient fibroblasts show decreased levels of the protein.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||J|||N-acetylmethionine|||Phosphatase tensin-type|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Putative tyrosine-protein phosphatase auxilin|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244516|||http://purl.uniprot.org/annotation/VAR_026908|||http://purl.uniprot.org/annotation/VAR_077924|||http://purl.uniprot.org/annotation/VAR_077925|||http://purl.uniprot.org/annotation/VAR_077926|||http://purl.uniprot.org/annotation/VAR_077927|||http://purl.uniprot.org/annotation/VAR_077928|||http://purl.uniprot.org/annotation/VAR_077929|||http://purl.uniprot.org/annotation/VSP_019579|||http://purl.uniprot.org/annotation/VSP_019580|||http://purl.uniprot.org/annotation/VSP_019581
http://togogenome.org/gene/9606:INS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01308                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Associated with diabetes mellitus type-II; Los-Angeles.|||C peptide|||In Chicago.|||In HPRI; Kyoto.|||In HPRI; Providence.|||In HPRI; impairs post-translational cleavage.|||In MODY10.|||In MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties.|||In PNDM4.|||In PNDM4; uncertain pathological significance.|||In T1D2.|||In Wakayama.|||Insulin A chain|||Insulin B chain|||Interchain (between B and A chains)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015819|||http://purl.uniprot.org/annotation/PRO_0000015820|||http://purl.uniprot.org/annotation/PRO_0000015821|||http://purl.uniprot.org/annotation/VAR_003971|||http://purl.uniprot.org/annotation/VAR_003972|||http://purl.uniprot.org/annotation/VAR_003973|||http://purl.uniprot.org/annotation/VAR_003974|||http://purl.uniprot.org/annotation/VAR_003975|||http://purl.uniprot.org/annotation/VAR_003976|||http://purl.uniprot.org/annotation/VAR_063721|||http://purl.uniprot.org/annotation/VAR_063722|||http://purl.uniprot.org/annotation/VAR_063723|||http://purl.uniprot.org/annotation/VAR_063724|||http://purl.uniprot.org/annotation/VAR_063725|||http://purl.uniprot.org/annotation/VAR_063726|||http://purl.uniprot.org/annotation/VAR_063727|||http://purl.uniprot.org/annotation/VAR_063728|||http://purl.uniprot.org/annotation/VAR_063729|||http://purl.uniprot.org/annotation/VAR_063730|||http://purl.uniprot.org/annotation/VAR_063731|||http://purl.uniprot.org/annotation/VAR_063732|||http://purl.uniprot.org/annotation/VAR_063733|||http://purl.uniprot.org/annotation/VAR_063734|||http://purl.uniprot.org/annotation/VAR_063735|||http://purl.uniprot.org/annotation/VAR_063736|||http://purl.uniprot.org/annotation/VAR_063737|||http://purl.uniprot.org/annotation/VAR_063738|||http://purl.uniprot.org/annotation/VAR_063739|||http://purl.uniprot.org/annotation/VAR_063740|||http://purl.uniprot.org/annotation/VAR_063741
http://togogenome.org/gene/9606:GSTZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR33|||http://purl.uniprot.org/uniprot/A0A0C4DFM0|||http://purl.uniprot.org/uniprot/O43708                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||In MAAID.|||In MAAID; decreased maleylacetoacetate isomerase activity.|||In allele GSTZ1*B and allele GSTZ1*C.|||In allele GSTZ1*C.|||In isoform 2.|||In isoform 3.|||Maleylacetoacetate isomerase|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186022|||http://purl.uniprot.org/annotation/VAR_009705|||http://purl.uniprot.org/annotation/VAR_009706|||http://purl.uniprot.org/annotation/VAR_009707|||http://purl.uniprot.org/annotation/VAR_014505|||http://purl.uniprot.org/annotation/VAR_079259|||http://purl.uniprot.org/annotation/VAR_079260|||http://purl.uniprot.org/annotation/VAR_079261|||http://purl.uniprot.org/annotation/VSP_039862|||http://purl.uniprot.org/annotation/VSP_047392
http://togogenome.org/gene/9606:CROT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKG9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Microbody targeting signal|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal carnitine O-octanoyltransferase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210169|||http://purl.uniprot.org/annotation/VAR_048612|||http://purl.uniprot.org/annotation/VAR_048613|||http://purl.uniprot.org/annotation/VSP_045213|||http://purl.uniprot.org/annotation/VSP_045214|||http://purl.uniprot.org/annotation/VSP_046953
http://togogenome.org/gene/9606:APOBEC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH17                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase 1|||CMP/dCMP-type deaminase 2|||DNA dC->dU-editing enzyme APOBEC-3B|||In isoform 2.|||In isoform 3.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171753|||http://purl.uniprot.org/annotation/VAR_018142|||http://purl.uniprot.org/annotation/VAR_018143|||http://purl.uniprot.org/annotation/VAR_018144|||http://purl.uniprot.org/annotation/VAR_033455|||http://purl.uniprot.org/annotation/VAR_048722|||http://purl.uniprot.org/annotation/VSP_009802|||http://purl.uniprot.org/annotation/VSP_044900
http://togogenome.org/gene/9606:ITSN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7XZY7|||http://purl.uniprot.org/uniprot/F8W7U0|||http://purl.uniprot.org/uniprot/Q15811|||http://purl.uniprot.org/uniprot/Q6PD56                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with FCHSD2.|||Basic and acidic residues|||Bipartite nuclear localization signal; in isoform 2|||C2|||DH|||Decreases specificity for CDC42; when associated with I-1376.|||Decreases specificity for CDC42; when associated with L-1369.|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EH|||EH 1|||EH 2|||In isoform 10, isoform 11 and isoform 12.|||In isoform 13.|||In isoform 2, isoform 3, isoform 7, isoform 10, isoform 11 and isoform 12.|||In isoform 3, isoform 4, isoform 11 and isoform 12.|||In isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 12 and isoform 13.|||In isoform 5.|||In isoform 6.|||In isoform 9.|||Intersectin-1|||KLERQ|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with FCHSD2|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080957|||http://purl.uniprot.org/annotation/VAR_070011|||http://purl.uniprot.org/annotation/VSP_004293|||http://purl.uniprot.org/annotation/VSP_004294|||http://purl.uniprot.org/annotation/VSP_004295|||http://purl.uniprot.org/annotation/VSP_047460|||http://purl.uniprot.org/annotation/VSP_047461|||http://purl.uniprot.org/annotation/VSP_053317|||http://purl.uniprot.org/annotation/VSP_053318|||http://purl.uniprot.org/annotation/VSP_053319|||http://purl.uniprot.org/annotation/VSP_053320|||http://purl.uniprot.org/annotation/VSP_053321|||http://purl.uniprot.org/annotation/VSP_053322
http://togogenome.org/gene/9606:NEMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFY4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Nuclear envelope integral membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332238|||http://purl.uniprot.org/annotation/VSP_056847|||http://purl.uniprot.org/annotation/VSP_056848|||http://purl.uniprot.org/annotation/VSP_056849
http://togogenome.org/gene/9606:ST7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRC1|||http://purl.uniprot.org/uniprot/X5DRA0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Suppressor of tumorigenicity 7 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339202|||http://purl.uniprot.org/annotation/VAR_043932|||http://purl.uniprot.org/annotation/VAR_043933|||http://purl.uniprot.org/annotation/VSP_034108|||http://purl.uniprot.org/annotation/VSP_034109|||http://purl.uniprot.org/annotation/VSP_034110|||http://purl.uniprot.org/annotation/VSP_034111|||http://purl.uniprot.org/annotation/VSP_034112|||http://purl.uniprot.org/annotation/VSP_034113|||http://purl.uniprot.org/annotation/VSP_034114|||http://purl.uniprot.org/annotation/VSP_034115|||http://purl.uniprot.org/annotation/VSP_034116|||http://purl.uniprot.org/annotation/VSP_034117
http://togogenome.org/gene/9606:ACTRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDY3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-related protein T2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089144|||http://purl.uniprot.org/annotation/VAR_020416
http://togogenome.org/gene/9606:PTPDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTF0|||http://purl.uniprot.org/uniprot/A2A3K4|||http://purl.uniprot.org/uniprot/A8K0X7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein tyrosine phosphatase domain-containing protein 1|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312212|||http://purl.uniprot.org/annotation/VAR_037455|||http://purl.uniprot.org/annotation/VSP_029736
http://togogenome.org/gene/9606:SLC22A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y267                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 14|||Strongly reduced riboflavin transport; when associated with A-388 and A-395.|||Strongly reduced riboflavin transport; when associated with A-388 and A-487.|||Strongly reduced riboflavin transport; when associated with A-395 and A-487.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230784|||http://purl.uniprot.org/annotation/VAR_055108|||http://purl.uniprot.org/annotation/VAR_055109|||http://purl.uniprot.org/annotation/VAR_055110|||http://purl.uniprot.org/annotation/VAR_055111|||http://purl.uniprot.org/annotation/VAR_055112|||http://purl.uniprot.org/annotation/VAR_055113|||http://purl.uniprot.org/annotation/VAR_055114|||http://purl.uniprot.org/annotation/VAR_055115|||http://purl.uniprot.org/annotation/VAR_055116
http://togogenome.org/gene/9606:ZNF827                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSR1|||http://purl.uniprot.org/uniprot/Q17R98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Decreased interaction with RBBP4.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Loss of function in NuRD complex recruitment to telomeric regions.|||Mediates direct interaction with RBBP4|||Polar residues|||Pro residues|||RRK motif; mediates NuRD recruitment to telomeres|||Zinc finger protein 827                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325889|||http://purl.uniprot.org/annotation/VSP_032463|||http://purl.uniprot.org/annotation/VSP_032464|||http://purl.uniprot.org/annotation/VSP_032465
http://togogenome.org/gene/9606:FPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21462                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||fMet-Leu-Phe receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069444|||http://purl.uniprot.org/annotation/VAR_003476|||http://purl.uniprot.org/annotation/VAR_003477|||http://purl.uniprot.org/annotation/VAR_003478|||http://purl.uniprot.org/annotation/VAR_055915|||http://purl.uniprot.org/annotation/VAR_055916
http://togogenome.org/gene/9606:CHST11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPF2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes enzyme activity but does not affect stability of the protein.|||Carbohydrate sulfotransferase 11|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In OCBMD.|||In isoform 2.|||Induces a strong decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-223.|||Induces a strong decrease in enzyme activity has no effect on stability of the protein.|||Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-321.|||Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-223 and S-321.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189664|||http://purl.uniprot.org/annotation/VAR_081477|||http://purl.uniprot.org/annotation/VSP_012992
http://togogenome.org/gene/9606:ARHGEF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z547|||http://purl.uniprot.org/uniprot/O94989                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||Found in a child with sporadic epilepsy; unknown pathological significance.|||Phosphoserine|||Phosphotyrosine; by EPHB2|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080932|||http://purl.uniprot.org/annotation/VAR_054215|||http://purl.uniprot.org/annotation/VAR_054216|||http://purl.uniprot.org/annotation/VAR_054217|||http://purl.uniprot.org/annotation/VAR_057189|||http://purl.uniprot.org/annotation/VAR_077835
http://togogenome.org/gene/9606:RPL36AL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Q0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N6-methyllysine|||Ribosomal protein eL42-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149118|||http://purl.uniprot.org/annotation/VAR_051809
http://togogenome.org/gene/9606:EIF4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRM3|||http://purl.uniprot.org/uniprot/E7EX17|||http://purl.uniprot.org/uniprot/P23588|||http://purl.uniprot.org/uniprot/Q7Z5Y0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 4B|||Found in a renal cell carcinoma case; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Non-phosphorylatable mutant whose expression results in reduced SLC4A7 protein levels in TSC2-deficient cells accompanied by decrease in the bicarbonate-dependent flux into nucleotide synthesis.|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Phosphoserine; by RPS6KA1 and RPS6KB1|||Phosphothreonine|||Polar residues|||Pro residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081616|||http://purl.uniprot.org/annotation/VAR_064710|||http://purl.uniprot.org/annotation/VSP_057351
http://togogenome.org/gene/9606:PENK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01210                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Turn                                                                                  ^@                                                                                  Cleavage; by CTSL|||Disordered|||Leu-enkephalin|||Met-enkephalin|||Met-enkephalin-Arg-Gly-Leu|||Met-enkephalin-Arg-Phe|||PENK(114-133)|||PENK(143-183)|||PENK(237-258)|||Phosphoserine|||Synenkephalin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008242|||http://purl.uniprot.org/annotation/PRO_0000008243|||http://purl.uniprot.org/annotation/PRO_0000008244|||http://purl.uniprot.org/annotation/PRO_0000008246|||http://purl.uniprot.org/annotation/PRO_0000008248|||http://purl.uniprot.org/annotation/PRO_0000008249|||http://purl.uniprot.org/annotation/PRO_0000008250|||http://purl.uniprot.org/annotation/PRO_0000008251|||http://purl.uniprot.org/annotation/PRO_0000008252|||http://purl.uniprot.org/annotation/PRO_0000008254|||http://purl.uniprot.org/annotation/PRO_0000377691|||http://purl.uniprot.org/annotation/PRO_0000377692|||http://purl.uniprot.org/annotation/PRO_0000377693|||http://purl.uniprot.org/annotation/VAR_014584|||http://purl.uniprot.org/annotation/VAR_048935
http://togogenome.org/gene/9606:MAN2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49641                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-mannosidase 2x|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 1.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206905|||http://purl.uniprot.org/annotation/VAR_047912|||http://purl.uniprot.org/annotation/VAR_047913|||http://purl.uniprot.org/annotation/VSP_041732|||http://purl.uniprot.org/annotation/VSP_041733|||http://purl.uniprot.org/annotation/VSP_041734
http://togogenome.org/gene/9606:NPHP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z494                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In NPHP3.|||In NPHP3; likely benign variant.|||In RHPD1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-myristoyl glycine|||Nephrocystin-3|||Polar residues|||Removed|||TPR 1|||TPR 10|||TPR 11|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106301|||http://purl.uniprot.org/annotation/VAR_022815|||http://purl.uniprot.org/annotation/VAR_022816|||http://purl.uniprot.org/annotation/VAR_022817|||http://purl.uniprot.org/annotation/VAR_022818|||http://purl.uniprot.org/annotation/VAR_022819|||http://purl.uniprot.org/annotation/VAR_022820|||http://purl.uniprot.org/annotation/VAR_022821|||http://purl.uniprot.org/annotation/VAR_044121|||http://purl.uniprot.org/annotation/VAR_044122|||http://purl.uniprot.org/annotation/VSP_014480|||http://purl.uniprot.org/annotation/VSP_014481|||http://purl.uniprot.org/annotation/VSP_014482|||http://purl.uniprot.org/annotation/VSP_014483|||http://purl.uniprot.org/annotation/VSP_014484|||http://purl.uniprot.org/annotation/VSP_014485|||http://purl.uniprot.org/annotation/VSP_014486|||http://purl.uniprot.org/annotation/VSP_014487|||http://purl.uniprot.org/annotation/VSP_014488|||http://purl.uniprot.org/annotation/VSP_014489|||http://purl.uniprot.org/annotation/VSP_014490|||http://purl.uniprot.org/annotation/VSP_014491
http://togogenome.org/gene/9606:GALNT18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58A54|||http://purl.uniprot.org/uniprot/Q6P9A2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 18|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059141|||http://purl.uniprot.org/annotation/VSP_011234|||http://purl.uniprot.org/annotation/VSP_011235
http://togogenome.org/gene/9606:LCE1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T754                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1F|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235329
http://togogenome.org/gene/9606:PPP4R3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MIZ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 3B|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254603|||http://purl.uniprot.org/annotation/VAR_057734|||http://purl.uniprot.org/annotation/VAR_065187|||http://purl.uniprot.org/annotation/VSP_021258|||http://purl.uniprot.org/annotation/VSP_021259|||http://purl.uniprot.org/annotation/VSP_021260|||http://purl.uniprot.org/annotation/VSP_021261|||http://purl.uniprot.org/annotation/VSP_021262|||http://purl.uniprot.org/annotation/VSP_021263
http://togogenome.org/gene/9606:AFTPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GW0|||http://purl.uniprot.org/uniprot/Q6ULP2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the interaction with CLTCL1/Clathrin.|||Aftiphilin|||Aftiphilin clathrin-binding box|||Basic and acidic residues|||CLTCL1/Clathrin-binding|||Clathrin-binding|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2 and isoform 5.|||In isoform 3.|||Interaction with AP1G1|||Interaction with AP1G1, AP1G2, GGA1 and GGA3|||Phosphoserine|||Phosphothreonine|||Polar residues|||WXXF motif 1|||WXXF motif 2|||WXXF motif 3 (partial)|||WXXF motif 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064488|||http://purl.uniprot.org/annotation/VAR_056728|||http://purl.uniprot.org/annotation/VAR_056729|||http://purl.uniprot.org/annotation/VAR_056730|||http://purl.uniprot.org/annotation/VSP_059492|||http://purl.uniprot.org/annotation/VSP_059493|||http://purl.uniprot.org/annotation/VSP_059494|||http://purl.uniprot.org/annotation/VSP_059495
http://togogenome.org/gene/9606:ERVFRD-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60508                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CKS-17|||CX6CC|||CXXC|||Cleavage|||Cytoplasmic|||Extracellular|||Fusion peptide|||Helical|||Interchain (between SU and TM chains, or C-46 with C-439); in linked form|||N-linked (GlcNAc...) asparagine|||Surface protein|||Syncytin-2|||Transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008439|||http://purl.uniprot.org/annotation/PRO_0000008440|||http://purl.uniprot.org/annotation/PRO_0000008441
http://togogenome.org/gene/9606:PAK1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5C3|||http://purl.uniprot.org/uniprot/Q9NWT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||p21-activated protein kinase-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051125
http://togogenome.org/gene/9606:PRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01236|||http://purl.uniprot.org/uniprot/Q5I0G2|||http://purl.uniprot.org/uniprot/Q5THQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist.|||N-linked (GlcNAc...) asparagine; partial|||Phosphoserine|||Prolactin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032916|||http://purl.uniprot.org/annotation/PRO_5014309965|||http://purl.uniprot.org/annotation/PRO_5014586759
http://togogenome.org/gene/9606:MYH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G1UI33|||http://purl.uniprot.org/uniprot/P35580                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-10|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Probable disease-associated variant found in a patient with intrauterine growth restriction, microcephaly, developmental delay, failure to thrive, congenital bilateral hip dysplasia, cerebral and cerebellar atrophy, hydrocephalus and congenital diaphragmatic hernia.|||Probable disease-associated variant found in a patient with severe intellectual disease, microcephaly and feeding difficulties as well as cerebral atrophy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123421|||http://purl.uniprot.org/annotation/VAR_078649|||http://purl.uniprot.org/annotation/VAR_078650|||http://purl.uniprot.org/annotation/VSP_022013|||http://purl.uniprot.org/annotation/VSP_022014|||http://purl.uniprot.org/annotation/VSP_046033|||http://purl.uniprot.org/annotation/VSP_054974
http://togogenome.org/gene/9606:DAO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBI1|||http://purl.uniprot.org/uniprot/P14920                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Motif|||Non-terminal Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  D-amino-acid oxidase|||Microbody targeting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162761
http://togogenome.org/gene/9606:VAC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with NOS1.|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In SNDC.|||In isoform 2.|||Mediates interaction with the PDZ domain of NOS1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein VAC14 homolog|||Reduces interaction with NOS1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300485|||http://purl.uniprot.org/annotation/VAR_077031|||http://purl.uniprot.org/annotation/VAR_077032|||http://purl.uniprot.org/annotation/VAR_077033|||http://purl.uniprot.org/annotation/VSP_056097
http://togogenome.org/gene/9606:ATG9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q674R7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Autophagy-related protein 9B|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Polar residues|||Pro residues|||Tyrosine-based sorting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314867|||http://purl.uniprot.org/annotation/VAR_061030|||http://purl.uniprot.org/annotation/VSP_030410|||http://purl.uniprot.org/annotation/VSP_030411|||http://purl.uniprot.org/annotation/VSP_030412|||http://purl.uniprot.org/annotation/VSP_030413
http://togogenome.org/gene/9606:SLF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  APIM motif|||Acidic residues|||Basic and acidic residues|||Disordered|||Found in a patient with neurodevelopmental disorder with hypotonia, dysmorphic facies and skin abnormalities; unknown pathological significance.|||In APIMmut; does not affect subcellular location.|||In ATELS1.|||In isoform 2.|||In isoform 3.|||Interaction with SIMC1|||NSE6-like domain|||Phosphoserine|||Polar residues|||Required for interaction with SLF1 and RAD18|||SMC5-SMC6 complex localization factor protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089778|||http://purl.uniprot.org/annotation/VAR_023112|||http://purl.uniprot.org/annotation/VAR_087944|||http://purl.uniprot.org/annotation/VAR_087945|||http://purl.uniprot.org/annotation/VAR_087946|||http://purl.uniprot.org/annotation/VAR_087993|||http://purl.uniprot.org/annotation/VSP_045621|||http://purl.uniprot.org/annotation/VSP_054914|||http://purl.uniprot.org/annotation/VSP_054915
http://togogenome.org/gene/9606:CHRNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK78|||http://purl.uniprot.org/uniprot/P43681|||http://purl.uniprot.org/uniprot/Q4VAQ3|||http://purl.uniprot.org/uniprot/Q59FV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with receptor activation|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In ENFL1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-4|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000351|||http://purl.uniprot.org/annotation/PRO_5022261607|||http://purl.uniprot.org/annotation/VAR_000295|||http://purl.uniprot.org/annotation/VAR_017531|||http://purl.uniprot.org/annotation/VAR_023402|||http://purl.uniprot.org/annotation/VAR_023403|||http://purl.uniprot.org/annotation/VSP_054275|||http://purl.uniprot.org/annotation/VSP_054276
http://togogenome.org/gene/9606:MYO1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00159                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with YWHAB.|||Actin-binding|||IQ 1|||IQ 2|||In isoform 2.|||In isoform 3.|||Increases affinity for YWHAB.|||Myosin motor|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||TH1|||Unconventional myosin-Ic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123445|||http://purl.uniprot.org/annotation/VAR_054855|||http://purl.uniprot.org/annotation/VAR_054856|||http://purl.uniprot.org/annotation/VSP_036861|||http://purl.uniprot.org/annotation/VSP_036862
http://togogenome.org/gene/9606:HS3ST6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QI5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 6|||In HAE8; unknown pathological significance.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085224|||http://purl.uniprot.org/annotation/VAR_085820
http://togogenome.org/gene/9606:GMPPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5P6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MDDGA14; causes protein aggregation.|||In MDDGB14 and MDDGC14.|||In MDDGB14; causes protein aggregation.|||In MDDGB14; the protein remains distributed in the cytoplasm and has no discernable changes compared to wild-type.|||In MDDGC14.|||In MDDGC14; causes protein aggregation.|||In MDDGC14; no change in protein abundance.|||In MDDGC14; no change in protein abundance; shows an increased propensity to form punctate aggregates.|||In MDDGC14; slight reduction in protein abundance.|||In MDDGC14; slight reduction in protein abundance; shows an increased propensity to form punctate aggregates.|||In MDDGC14; the protein remains distributed in the cytoplasm and has no discernable changes compared to wild-type.|||In isoform 2.|||Mannose-1-phosphate guanyltransferase beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307162|||http://purl.uniprot.org/annotation/VAR_035372|||http://purl.uniprot.org/annotation/VAR_035373|||http://purl.uniprot.org/annotation/VAR_070142|||http://purl.uniprot.org/annotation/VAR_070143|||http://purl.uniprot.org/annotation/VAR_070144|||http://purl.uniprot.org/annotation/VAR_070145|||http://purl.uniprot.org/annotation/VAR_070146|||http://purl.uniprot.org/annotation/VAR_070147|||http://purl.uniprot.org/annotation/VAR_070148|||http://purl.uniprot.org/annotation/VAR_079761|||http://purl.uniprot.org/annotation/VAR_079762|||http://purl.uniprot.org/annotation/VAR_079763|||http://purl.uniprot.org/annotation/VAR_079764|||http://purl.uniprot.org/annotation/VAR_079765|||http://purl.uniprot.org/annotation/VAR_079766|||http://purl.uniprot.org/annotation/VAR_079767|||http://purl.uniprot.org/annotation/VAR_079768|||http://purl.uniprot.org/annotation/VAR_079769|||http://purl.uniprot.org/annotation/VAR_079770|||http://purl.uniprot.org/annotation/VAR_079771|||http://purl.uniprot.org/annotation/VSP_028619
http://togogenome.org/gene/9606:WDR53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JBE7|||http://purl.uniprot.org/uniprot/C9JJZ8|||http://purl.uniprot.org/uniprot/Q7Z5U6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051413|||http://purl.uniprot.org/annotation/VAR_033810|||http://purl.uniprot.org/annotation/VAR_035890
http://togogenome.org/gene/9606:WNT5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41221                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In DRS1.|||In DRS1; hypomorphic mutation.|||In DRS1; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-5a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041427|||http://purl.uniprot.org/annotation/PRO_0000352796|||http://purl.uniprot.org/annotation/VAR_066623|||http://purl.uniprot.org/annotation/VAR_066629|||http://purl.uniprot.org/annotation/VAR_083248|||http://purl.uniprot.org/annotation/VAR_083249|||http://purl.uniprot.org/annotation/VSP_035594
http://togogenome.org/gene/9606:FDPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X090|||http://purl.uniprot.org/uniprot/P14324                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Farnesyl pyrophosphate synthase|||Helical|||Important for determining product chain length|||In POROK9.|||In isoform 2.|||N-acetylmethionine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123944|||http://purl.uniprot.org/annotation/VAR_049644|||http://purl.uniprot.org/annotation/VAR_061274|||http://purl.uniprot.org/annotation/VAR_075062|||http://purl.uniprot.org/annotation/VSP_046958
http://togogenome.org/gene/9606:KCNC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48547                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In EPM7; causes a dominant-negative loss of current upon membrane depolarization.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Potassium voltage-gated channel subfamily C member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054051|||http://purl.uniprot.org/annotation/VAR_072705|||http://purl.uniprot.org/annotation/VSP_055129
http://togogenome.org/gene/9606:EIF4G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78344|||http://purl.uniprot.org/uniprot/Q2TU89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 4 gamma 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MI|||MIF4G|||N-acetylmethionine|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||W2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213325|||http://purl.uniprot.org/annotation/VAR_048923|||http://purl.uniprot.org/annotation/VSP_038726
http://togogenome.org/gene/9606:ZNF529                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFR4|||http://purl.uniprot.org/uniprot/Q6P280                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 529                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280419|||http://purl.uniprot.org/annotation/VAR_031147
http://togogenome.org/gene/9606:CALHM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JW98                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 4|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186724|||http://purl.uniprot.org/annotation/VSP_013817|||http://purl.uniprot.org/annotation/VSP_018252|||http://purl.uniprot.org/annotation/VSP_045216
http://togogenome.org/gene/9606:ABCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RUU2|||http://purl.uniprot.org/uniprot/B7XCW9|||http://purl.uniprot.org/uniprot/O95477                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  60-65% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane.|||80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-584.|||80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-581 and K-585.|||80-85% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-584 and K-585.|||85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-371.|||85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-371.|||85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-74.|||90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with E-590.|||90-95% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with K-583.|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||Annulus domain 1|||Annulus domain 2|||Associated with HDL cholesterol.|||Associated with a decreased severity of CAD.|||Associated with higher plasma cholesterol.|||Associated with increased plasma HDL cholesterol.|||Associated with premature coronary heart disease.|||Associated with reduced plasma HDL cholesterol.|||Basic and acidic residues|||Could be associated with reduced plasma HDL cholesterol.|||Decreased palmitoylation; when associated with S-3, S-23 and S-1110.|||Decreased palmitoylation; when associated with S-3, S-23 and S-1111.|||Disordered|||Extracellular|||Gateway domain|||Helical|||Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.|||In FHA1.|||In FHA1; Alabama.|||In FHA1; deficient cellular cholesterol efflux.|||In FHA1; loss of localization to plasma membrane; decreased cholesterol efflux; decreased phospholipid efflux.|||In FHA1; moderately decreased protein abundance; does not affect ATPase activity; moderately decreased phospholipid translocase activity.|||In FHA1; uncertain pathological significance.|||In Scott syndrome; shows impaired trafficking of the mutant protein to the plasma membrane.|||In TGD.|||In TGD; deficient cellular cholesterol efflux.|||In TGD; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane.|||In TGD; loss of interaction with APOE; unable to generate APOE-containing high density lipoproteins; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity.|||In TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity.|||In TGD; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; loss protein subcellular localization to the plasma membrane.|||In TGD; the mutant protein is retained in the endoplasmic reticulum while the wild-type protein is located at the plasma membrane.|||In a colorectal cancer sample; somatic mutation.|||Inhibits ATPase activity; when associated with M-1952. Decreases translocase activity; when associated with M-1952. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-1952.|||Inhibits ATPase activity; when associated with M-939. Decreases translocase activity; when associated with M-939. Does not affect protein subcellular localization in plasma membrane and endosome; when associated with M-939.|||May be associated with increased risk of ischemic heart disease.|||Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased cholesterol efflux. Decreased phospholipid efflux. Decreased palmitoylation; when associated with S-23, S-1110 and S-1111.|||Mild decrease of palmitoylation. Loss of localization to plasma membrane. Decreased palmitoylation; when associated with S-3, S-1110 and S-1111.|||Moderately decreased protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity.|||Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.|||N-linked (GlcNAc...) asparagine|||No effect on phospholipid and cholesterol efflux and on localization to cell membrane.|||No effect on phospholipid and cholesterol efflux or localization to cell membrane. 85-90% reduction in phospholipid and cholesterol efflux but no effect on localization to cell membrane; when associated with C-74 or C-375.|||No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-304.|||No effect on phospholipid and cholesterol efflux or localization to cell membrane; when associated with C-308.|||Phospholipid-transporting ATPase ABCA1|||Phosphoserine|||Phosphoserine; by PKA|||S-palmitoyl cysteine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093288|||http://purl.uniprot.org/annotation/VAR_009145|||http://purl.uniprot.org/annotation/VAR_009146|||http://purl.uniprot.org/annotation/VAR_009147|||http://purl.uniprot.org/annotation/VAR_009148|||http://purl.uniprot.org/annotation/VAR_009149|||http://purl.uniprot.org/annotation/VAR_009150|||http://purl.uniprot.org/annotation/VAR_009151|||http://purl.uniprot.org/annotation/VAR_009152|||http://purl.uniprot.org/annotation/VAR_009153|||http://purl.uniprot.org/annotation/VAR_009154|||http://purl.uniprot.org/annotation/VAR_009155|||http://purl.uniprot.org/annotation/VAR_012618|||http://purl.uniprot.org/annotation/VAR_012619|||http://purl.uniprot.org/annotation/VAR_012620|||http://purl.uniprot.org/annotation/VAR_012621|||http://purl.uniprot.org/annotation/VAR_012622|||http://purl.uniprot.org/annotation/VAR_012623|||http://purl.uniprot.org/annotation/VAR_012624|||http://purl.uniprot.org/annotation/VAR_012625|||http://purl.uniprot.org/annotation/VAR_012626|||http://purl.uniprot.org/annotation/VAR_012627|||http://purl.uniprot.org/annotation/VAR_012628|||http://purl.uniprot.org/annotation/VAR_012629|||http://purl.uniprot.org/annotation/VAR_012630|||http://purl.uniprot.org/annotation/VAR_012631|||http://purl.uniprot.org/annotation/VAR_012632|||http://purl.uniprot.org/annotation/VAR_012633|||http://purl.uniprot.org/annotation/VAR_012634|||http://purl.uniprot.org/annotation/VAR_012635|||http://purl.uniprot.org/annotation/VAR_012636|||http://purl.uniprot.org/annotation/VAR_012637|||http://purl.uniprot.org/annotation/VAR_012638|||http://purl.uniprot.org/annotation/VAR_012639|||http://purl.uniprot.org/annotation/VAR_017016|||http://purl.uniprot.org/annotation/VAR_017529|||http://purl.uniprot.org/annotation/VAR_017530|||http://purl.uniprot.org/annotation/VAR_035724|||http://purl.uniprot.org/annotation/VAR_035725|||http://purl.uniprot.org/annotation/VAR_035726|||http://purl.uniprot.org/annotation/VAR_035727|||http://purl.uniprot.org/annotation/VAR_037968|||http://purl.uniprot.org/annotation/VAR_037969|||http://purl.uniprot.org/annotation/VAR_037970|||http://purl.uniprot.org/annotation/VAR_037971|||http://purl.uniprot.org/annotation/VAR_062481|||http://purl.uniprot.org/annotation/VAR_062482|||http://purl.uniprot.org/annotation/VAR_062483|||http://purl.uniprot.org/annotation/VAR_062484|||http://purl.uniprot.org/annotation/VAR_062485|||http://purl.uniprot.org/annotation/VAR_062486|||http://purl.uniprot.org/annotation/VAR_062487|||http://purl.uniprot.org/annotation/VAR_062488|||http://purl.uniprot.org/annotation/VAR_062489|||http://purl.uniprot.org/annotation/VAR_062490|||http://purl.uniprot.org/annotation/VAR_062491|||http://purl.uniprot.org/annotation/VAR_062492|||http://purl.uniprot.org/annotation/VAR_062493|||http://purl.uniprot.org/annotation/VAR_062494|||http://purl.uniprot.org/annotation/VAR_062495|||http://purl.uniprot.org/annotation/VAR_062496|||http://purl.uniprot.org/annotation/VAR_062497|||http://purl.uniprot.org/annotation/VAR_062498|||http://purl.uniprot.org/annotation/VAR_062499|||http://purl.uniprot.org/annotation/VAR_062500|||http://purl.uniprot.org/annotation/VAR_062501|||http://purl.uniprot.org/annotation/VAR_062502|||http://purl.uniprot.org/annotation/VAR_062503|||http://purl.uniprot.org/annotation/VAR_062504|||http://purl.uniprot.org/annotation/VAR_062505|||http://purl.uniprot.org/annotation/VAR_062506|||http://purl.uniprot.org/annotation/VAR_062507|||http://purl.uniprot.org/annotation/VAR_062508|||http://purl.uniprot.org/annotation/VAR_062509
http://togogenome.org/gene/9606:BRCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46736                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with UIMC1 and SHMT2.|||Abolishes localization to sites of DNA damage and interaction with ABRAXAS2; UIMC1; SHMT2; BABAM2 and BABAM1; when associated with R-23.|||Abolishes localization to sites of DNA damage and interaction with ABRAXAS2; UIMC1; SHMT2; BARAM2 and BABAM1; when associated with R-27.|||Abolishes metalloprotease activity and function in DNA repair.|||In isoform 1 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||JAMM motif|||Loss of deubiquitinase activity.|||Lys-63-specific deubiquitinase BRCC36|||MPN|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213967|||http://purl.uniprot.org/annotation/VAR_050097|||http://purl.uniprot.org/annotation/VSP_003261|||http://purl.uniprot.org/annotation/VSP_037257|||http://purl.uniprot.org/annotation/VSP_037258|||http://purl.uniprot.org/annotation/VSP_037259
http://togogenome.org/gene/9606:CHRAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRG0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Chromatin accessibility complex protein 1|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089656|||http://purl.uniprot.org/annotation/VAR_013755|||http://purl.uniprot.org/annotation/VAR_013756
http://togogenome.org/gene/9606:OGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60502                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates cleavage by caspase-3.|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||GH84|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Nearly abolishes enzyme activity.|||Phosphoserine|||Protein O-GlcNAcase|||Proton donor|||Strongly reduces affinity for glycopeptide substrates. Nearly abolishes enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252118|||http://purl.uniprot.org/annotation/VAR_027761|||http://purl.uniprot.org/annotation/VAR_027762|||http://purl.uniprot.org/annotation/VSP_020866|||http://purl.uniprot.org/annotation/VSP_020867|||http://purl.uniprot.org/annotation/VSP_020868|||http://purl.uniprot.org/annotation/VSP_020869
http://togogenome.org/gene/9606:KIR2DL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S6|||http://purl.uniprot.org/uniprot/A0A376A929                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Immunoglobulin subtype|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5015034607|||http://purl.uniprot.org/annotation/PRO_5017061524
http://togogenome.org/gene/9606:MXRA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In LNCR.|||In LNCR; unknown pathological significance.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Matrix-remodeling-associated protein 5|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254131|||http://purl.uniprot.org/annotation/VAR_028821|||http://purl.uniprot.org/annotation/VAR_056057|||http://purl.uniprot.org/annotation/VAR_056058|||http://purl.uniprot.org/annotation/VAR_056059|||http://purl.uniprot.org/annotation/VAR_060357|||http://purl.uniprot.org/annotation/VAR_060358|||http://purl.uniprot.org/annotation/VAR_060359|||http://purl.uniprot.org/annotation/VAR_060360|||http://purl.uniprot.org/annotation/VAR_072405|||http://purl.uniprot.org/annotation/VAR_072406|||http://purl.uniprot.org/annotation/VAR_072407|||http://purl.uniprot.org/annotation/VAR_072408|||http://purl.uniprot.org/annotation/VAR_072409|||http://purl.uniprot.org/annotation/VAR_072410|||http://purl.uniprot.org/annotation/VAR_072411|||http://purl.uniprot.org/annotation/VAR_072412|||http://purl.uniprot.org/annotation/VAR_072413|||http://purl.uniprot.org/annotation/VAR_072414|||http://purl.uniprot.org/annotation/VAR_072415|||http://purl.uniprot.org/annotation/VAR_076257|||http://purl.uniprot.org/annotation/VAR_076258|||http://purl.uniprot.org/annotation/VAR_076437
http://togogenome.org/gene/9606:MORN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q502X0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  MORN 1|||MORN 2|||MORN repeat-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247457|||http://purl.uniprot.org/annotation/VAR_027106
http://togogenome.org/gene/9606:TAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIR9|||http://purl.uniprot.org/uniprot/Q9NYJ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) S-methylcysteine|||Abolished Cys methylation and ability to bind 'Lys-63'-linked ubiquitin.|||Abolishes ubiquitin binding.|||Asymmetric dimethylarginine|||Basic and acidic residues|||CUE|||Disordered|||Disrupted zinc-finger; abolished methylation at C-673.|||Found in an patient with a form of frontometaphyseal dysplasia; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CHTD2.|||In isoform 2.|||Interaction with polyubiquitin|||Loss of TRIM35-mediated ubiquitination.|||Loss of TRIM60-mediated SUMOylation; when associated with R-329.|||Loss of TRIM60-mediated SUMOylation; when associated with R-562.|||Phosphoserine|||RanBP2-type|||TGF-beta-activated kinase 1 and MAP3K7-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225695|||http://purl.uniprot.org/annotation/VAR_063774|||http://purl.uniprot.org/annotation/VAR_063775|||http://purl.uniprot.org/annotation/VAR_077348|||http://purl.uniprot.org/annotation/VSP_017419|||http://purl.uniprot.org/annotation/VSP_017420
http://togogenome.org/gene/9606:LRRC26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2I0M4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 26|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309360|||http://purl.uniprot.org/annotation/VSP_040058|||http://purl.uniprot.org/annotation/VSP_040205
http://togogenome.org/gene/9606:RAPGEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13905                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by HCK.|||Disordered|||Found in a patient with intellectual disability, frontal epilepsy and mild facial dysmorphism.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform 4.|||In isoform Short.|||N-terminal Ras-GEF|||Phosphoserine|||Phosphotyrosine; by HCK|||Polar residues|||Pro residues|||Rap guanine nucleotide exchange factor 1|||Ras-GEF|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068864|||http://purl.uniprot.org/annotation/VAR_069375|||http://purl.uniprot.org/annotation/VSP_001822|||http://purl.uniprot.org/annotation/VSP_042052|||http://purl.uniprot.org/annotation/VSP_057416
http://togogenome.org/gene/9606:AQP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94778                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-8|||Cysteine persulfide|||Cysteine sulfenic acid (-SOH)|||Cytoplasmic|||Does not affect hydrogen peroxide transport activity under stress condition.|||Does not affect hydrogen peroxide transport under stress condition.|||Does not affect loss of hydrogen peroxide transport after stress.|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||Loss of hydrogen peroxide transport activity under stress condition.|||Loss of hydrogen peroxide transporter activity.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Slightly affect hydrogen peroxide transport after stress.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063961|||http://purl.uniprot.org/annotation/VAR_021933|||http://purl.uniprot.org/annotation/VAR_036484
http://togogenome.org/gene/9606:IFNA17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C355|||http://purl.uniprot.org/uniprot/P01571                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016369|||http://purl.uniprot.org/annotation/PRO_5030515310|||http://purl.uniprot.org/annotation/VAR_013020
http://togogenome.org/gene/9606:MTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14872                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Metal regulatory transcription factor 1|||N-acetylglycine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047220
http://togogenome.org/gene/9606:GDAP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWT8|||http://purl.uniprot.org/uniprot/B7Z1I3|||http://purl.uniprot.org/uniprot/H0UIB3|||http://purl.uniprot.org/uniprot/Q96MZ0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Ganglioside-induced differentiation-associated protein 1-like 1|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186040|||http://purl.uniprot.org/annotation/VAR_036556|||http://purl.uniprot.org/annotation/VSP_008793|||http://purl.uniprot.org/annotation/VSP_008794|||http://purl.uniprot.org/annotation/VSP_053683
http://togogenome.org/gene/9606:COA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IL0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Cytochrome c oxidase assembly factor 8|||In MC4DN17.|||In MC4DN17; low steady-state levels of COX subunits and reduced levels of fully assembled COX; highly decreased COX complex IV activity and decreased COX complex II activity in muscle.|||In MC4DN17; unknown pathological significance.|||In isoform 2.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019559|||http://purl.uniprot.org/annotation/VAR_023000|||http://purl.uniprot.org/annotation/VAR_033745|||http://purl.uniprot.org/annotation/VAR_082029|||http://purl.uniprot.org/annotation/VAR_082030|||http://purl.uniprot.org/annotation/VAR_082031|||http://purl.uniprot.org/annotation/VSP_060246|||http://purl.uniprot.org/annotation/VSP_060247
http://togogenome.org/gene/9606:TNFRSF10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14763|||http://purl.uniprot.org/uniprot/Q7Z2I8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||In isoform 3.|||In isoform Short.|||Polar residues|||TAPE|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 10B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034580|||http://purl.uniprot.org/annotation/VAR_016153|||http://purl.uniprot.org/annotation/VAR_016154|||http://purl.uniprot.org/annotation/VAR_059831|||http://purl.uniprot.org/annotation/VSP_006490|||http://purl.uniprot.org/annotation/VSP_039125
http://togogenome.org/gene/9606:NEUROD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15784                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In DEE72.|||Neurogenic differentiation factor 2|||Nuclear localization signal|||Pro residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127387|||http://purl.uniprot.org/annotation/VAR_082114|||http://purl.uniprot.org/annotation/VAR_082115
http://togogenome.org/gene/9606:ADAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUB4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A to I editase|||Disordered|||In isoform 2.|||Phosphoserine|||Proton donor|||tRNA-specific adenosine deaminase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287646|||http://purl.uniprot.org/annotation/VAR_032340|||http://purl.uniprot.org/annotation/VAR_032341|||http://purl.uniprot.org/annotation/VAR_055649|||http://purl.uniprot.org/annotation/VAR_061098|||http://purl.uniprot.org/annotation/VSP_025579
http://togogenome.org/gene/9606:APOA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02652                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Apolipoprotein A-II|||Cysteinylated ApoA-II monomer.|||Heterodimer with truncated apolipoprotein A-II.|||Homodimer, with 1 methionine sulfoxide, oxidation at Met-49.|||Homodimer, without methionine sulfoxide.|||Homodimer.|||Interchain (with C-136 in APOD); in heterodimeric form|||Methionine sulfoxide|||Monomer.|||O-glycosylated at one site|||Phosphoserine; by FAM20C|||Proapolipoprotein A-II|||Pyrrolidone carboxylic acid|||Truncated apolipoprotein A-II                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002003|||http://purl.uniprot.org/annotation/PRO_0000002004|||http://purl.uniprot.org/annotation/PRO_0000425351
http://togogenome.org/gene/9606:FIGLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6QHK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Factor in the germline alpha|||In POF6; one individual with premature ovarian failure.|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127179|||http://purl.uniprot.org/annotation/VAR_046776|||http://purl.uniprot.org/annotation/VAR_046777|||http://purl.uniprot.org/annotation/VAR_046778
http://togogenome.org/gene/9606:GMFG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R1D2|||http://purl.uniprot.org/uniprot/O60234                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H|||Glia maturation factor gamma|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214947|||http://purl.uniprot.org/annotation/VAR_048196|||http://purl.uniprot.org/annotation/VAR_048197
http://togogenome.org/gene/9606:PXDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGL8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||PX|||PX domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297573|||http://purl.uniprot.org/annotation/VAR_034643|||http://purl.uniprot.org/annotation/VAR_034644|||http://purl.uniprot.org/annotation/VAR_035619
http://togogenome.org/gene/9606:ROR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01973                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical|||Ig-like C2-type|||In DFNB108; impairs plasma membrane location; abolishes downstream NFkB activation.|||In a breast cancer sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 3.|||In isoform Short.|||Inactive tyrosine-protein kinase transmembrane receptor ROR1|||Kringle|||N-linked (GlcNAc...) asparagine|||No effect on kinase activity.|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024458|||http://purl.uniprot.org/annotation/VAR_035713|||http://purl.uniprot.org/annotation/VAR_041779|||http://purl.uniprot.org/annotation/VAR_041780|||http://purl.uniprot.org/annotation/VAR_041781|||http://purl.uniprot.org/annotation/VAR_041782|||http://purl.uniprot.org/annotation/VAR_041783|||http://purl.uniprot.org/annotation/VAR_041784|||http://purl.uniprot.org/annotation/VAR_041785|||http://purl.uniprot.org/annotation/VAR_041786|||http://purl.uniprot.org/annotation/VAR_079530|||http://purl.uniprot.org/annotation/VSP_005008|||http://purl.uniprot.org/annotation/VSP_043663|||http://purl.uniprot.org/annotation/VSP_043664
http://togogenome.org/gene/9606:ATOH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SQ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic motif; degenerate|||Disordered|||Helix-loop-helix motif|||In isoform 2.|||Pro residues|||Transcription factor ATOH8|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323751|||http://purl.uniprot.org/annotation/VAR_039582|||http://purl.uniprot.org/annotation/VSP_032118
http://togogenome.org/gene/9606:C1QTNF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7M4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Adipolin fC1QTNF12|||Adipolin gC1QTNF12|||Basic and acidic residues|||C1q|||Cleavage; by FURIN|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284354|||http://purl.uniprot.org/annotation/PRO_0000430248|||http://purl.uniprot.org/annotation/VAR_054065
http://togogenome.org/gene/9606:RPS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62249                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  N6-acetyllysine|||Phosphoserine|||Removed|||Small ribosomal subunit protein uS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111479
http://togogenome.org/gene/9606:HEY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Hairy/enhancer-of-split related with YRPW motif protein 1|||In isoform 2.|||Orange|||Polar residues|||Transcriptional repression and interaction with NCOR1 and SIN3A|||YRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127217|||http://purl.uniprot.org/annotation/VSP_040997
http://togogenome.org/gene/9606:OR52I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWK8|||http://purl.uniprot.org/uniprot/Q8NH67                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52I2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150779|||http://purl.uniprot.org/annotation/VAR_048082|||http://purl.uniprot.org/annotation/VAR_048083|||http://purl.uniprot.org/annotation/VAR_048084|||http://purl.uniprot.org/annotation/VAR_048085|||http://purl.uniprot.org/annotation/VAR_048086
http://togogenome.org/gene/9606:ZHX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||Interaction with EFNB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for homodimerization|||Required for interaction with NFYA|||Required for nuclear localization|||Required for repressor activity|||Zinc fingers and homeoboxes protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049391|||http://purl.uniprot.org/annotation/VAR_049594|||http://purl.uniprot.org/annotation/VAR_049595|||http://purl.uniprot.org/annotation/VAR_049596
http://togogenome.org/gene/9606:PPP6R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Interaction with PPP6C|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Serine/threonine-protein phosphatase 6 regulatory subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046096
http://togogenome.org/gene/9606:PTK2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14289                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation. Abolishes interaction with SRC.|||Abolishes kinase activity.|||Disordered|||FERM|||Focal adhesion targeting (FAT)|||In isoform 2.|||Interaction with TGFB1I1|||Loss of interaction with NPHP1.|||Loss of phosphorylation site. Strongly reduced interaction with GRB2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Phosphotyrosine; by SRC, FYN and LCK|||Phosphotyrosine; by autocatalysis|||Pro residues|||Protein kinase|||Protein-tyrosine kinase 2-beta|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088081|||http://purl.uniprot.org/annotation/VAR_020284|||http://purl.uniprot.org/annotation/VAR_041687|||http://purl.uniprot.org/annotation/VAR_041688|||http://purl.uniprot.org/annotation/VAR_041689|||http://purl.uniprot.org/annotation/VAR_041690|||http://purl.uniprot.org/annotation/VSP_004981
http://togogenome.org/gene/9606:DHX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7L7|||http://purl.uniprot.org/uniprot/B4DZ28|||http://purl.uniprot.org/uniprot/O60231|||http://purl.uniprot.org/uniprot/Q5SQH4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||Dominant-negative mutant. Impairs pre-mRNA splicing activity. Fails to interact with any of viral RNA forms.|||Helicase ATP-binding|||Helicase C-terminal|||Impairs pre-mRNA splicing activity.|||In NMOAS.|||In NMOAS; unknown pathological significance.|||No loss of pre-mRNA splicing activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055151|||http://purl.uniprot.org/annotation/VAR_057236|||http://purl.uniprot.org/annotation/VAR_057237|||http://purl.uniprot.org/annotation/VAR_057238|||http://purl.uniprot.org/annotation/VAR_083621|||http://purl.uniprot.org/annotation/VAR_083622|||http://purl.uniprot.org/annotation/VAR_083623|||http://purl.uniprot.org/annotation/VAR_083624
http://togogenome.org/gene/9606:BECN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R1X5|||http://purl.uniprot.org/uniprot/B4DQ36|||http://purl.uniprot.org/uniprot/E7EV84|||http://purl.uniprot.org/uniprot/Q14457|||http://purl.uniprot.org/uniprot/W0FFG4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ubiquitination by the DCX(AMBRA1) complex.|||Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-133.|||Abolishes in vitro cleavage by CASP3 and CASP8; when associated with A-149.|||Abolishes in vitro cleavage by CASP3.|||Abolishes in vitro cleavage by CASP8; when associated with A-133.|||Abolishes in vitro cleavage by CASP8; when associated with A-146.|||Atg6 BARA|||Atg6/beclin coiled-coil|||BH3|||Beclin-1|||Beclin-1 BH3|||Beclin-1-C 35 kDa|||Beclin-1-C 37 kDa|||Complete loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-93.|||Decrease in membrane-association.|||Decreases K48 polyubiquitination and stabilizes BECN1.|||Decreases interaction with BCL2L1 isoform Bcl-X(L).|||Decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L).|||Disordered|||Does not affect ubiquitination by the DCX(AMBRA1) complex.|||Evolutionary conserved domain (ECD)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with BCL2 and BCL2L1 isoform Bcl-X(L)|||N-acetylmethionine|||No effect on interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L).|||Partial loss of phosphorylation. Complete loss of phosphorylation and defective autophagic function; when associated with Ala-90.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine; by DAPK1|||Required for membrane-association|||Significantly reduces ubiquitination.|||Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2 and decreases interaction with BCL2L1 isoform Bcl-X(L). Reduces interaction with BCL2L10.|||Weakly decreases interaction with MUHV-4 M11, disrupts interaction with BCL2L1 isoform Bcl-X(L).|||Weakly decreases interaction with MUHV-4 M11, greatly decreases interaction with BCL2L1 isoform Bcl-X(L).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218555|||http://purl.uniprot.org/annotation/PRO_0000435036|||http://purl.uniprot.org/annotation/PRO_0000435037|||http://purl.uniprot.org/annotation/VAR_005236|||http://purl.uniprot.org/annotation/VAR_010384
http://togogenome.org/gene/9606:LEMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Compromises nuclear envelope enrichment.|||Disordered|||Disrupts LEMD2 accumulation within the nuclear envelope (NE) and subsequent NE core enrichment in anaphase cells.|||Does not affect nuclear envelope enrichment.|||Failure to enrich at mictrotubule-containing nuclear envelope core during anaphase.|||Helical|||In CTRCT46.|||In MARUPS.|||In isoform 2.|||LEM|||LEM domain-containing protein 2|||N-acetylalanine|||Phosphoserine|||Removed|||Required for nuclear retention and interaction with LMNA isoform C|||Winged-Helix (WH)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285249|||http://purl.uniprot.org/annotation/VAR_076992|||http://purl.uniprot.org/annotation/VAR_085694|||http://purl.uniprot.org/annotation/VSP_044847
http://togogenome.org/gene/9606:OR2T8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NH00                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311914|||http://purl.uniprot.org/annotation/VAR_037342|||http://purl.uniprot.org/annotation/VAR_037343|||http://purl.uniprot.org/annotation/VAR_037344|||http://purl.uniprot.org/annotation/VAR_037345|||http://purl.uniprot.org/annotation/VAR_037346|||http://purl.uniprot.org/annotation/VAR_037347|||http://purl.uniprot.org/annotation/VAR_062028|||http://purl.uniprot.org/annotation/VAR_062029
http://togogenome.org/gene/9606:ETV6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3C9|||http://purl.uniprot.org/uniprot/P41212                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form CHIC2-ETV6 in AML|||Breakpoint for translocation to form ETV6-AML1 in ALL|||Breakpoint for translocation to form ETV6-MDS2 in MDS|||Breakpoint for translocation to form PAX5-ETV6|||Disordered|||ETS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In THC5; abrogates DNA binding; alters subcellular location; decreases transcriptional repression in a dominant-negative fashion.|||In one individual with AML; somatic mutation; unable to repress transcription.|||N6-acetyllysine; alternate|||No effect.|||No phosphorylation by MAPK14.|||PNT|||Phosphoserine|||Phosphoserine; by MAPK14|||Phosphothreonine|||Polar residues|||Transcription factor ETV6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204121|||http://purl.uniprot.org/annotation/VAR_034600|||http://purl.uniprot.org/annotation/VAR_073322|||http://purl.uniprot.org/annotation/VAR_073323|||http://purl.uniprot.org/annotation/VAR_073324
http://togogenome.org/gene/9606:PLAC8L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4L8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  PLAC8-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311396|||http://purl.uniprot.org/annotation/VAR_037245
http://togogenome.org/gene/9606:MET                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLF5|||http://purl.uniprot.org/uniprot/E6Y365|||http://purl.uniprot.org/uniprot/P08581                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form TPR-MET oncogene|||Cleavage|||Complete loss of kinase activity and of ligand-induced ubiquitination. Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1235.|||Complete loss of kinase activity. Alters interaction with PTPN1 and PTPN2. Loss of interaction with PTPN1 and PTPN2; when associated with F-1234.|||Cytoplasmic|||Extracellular|||Found in a case of cancer of unknown primary origin; the mutated receptor is still functional and can sustain the transformed phenotype; somatic mutation.|||Found in lung cancer also including cases carrying EGFR mutations; unknown pathological significance; decreased hepatocyte growth factor-activated receptor activity; decreased interaction with HGF.|||Helical|||Hepatocyte growth factor receptor|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||In DA11; not phosphorylated in reponse to HGF; severely decreased tyrosin kinase activity.|||In DFNB97.|||In HCC.|||In OSFD; loss of CBL-mediated destabilization.|||In RCCP; causes malignant transformation in cell lines.|||In RCCP; constitutive autophosphorylation.|||In RCCP; constitutive autophosphorylation; causes malignant transformation in cell lines.|||In RCCP; germline mutation.|||In RCCP; somatic mutation.|||In gastric cancer.|||In gastric cancer; prolonged tyrosine phosphorylation in response to HGF/SF; transforming activity in athymic nude mice.|||In isoform 2.|||In isoform 3.|||Interaction with MUC20|||Interaction with RANBP9|||N-linked (GlcNAc...) asparagine|||No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1349 and F-1356.|||No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1349 and F-1365.|||No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1313, F-1356 and F-1365.|||No effect on ligand-induced CBL-mediated ubiquitination; when associated with F-1349, F-1356 and F-1365.|||O-linked (Man) threonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Probable disease-associated variant found in lesional sample from a patient with sporadically occurring, unilateral osteofibrous dysplasia; somatic mutation; complete loss of ligand-induced CBL-mediated ubiquitination, resulting in protein stabilization.|||Protein kinase|||Proton acceptor|||Required for ligand-induced CBL-mediated ubiquitination|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024440|||http://purl.uniprot.org/annotation/PRO_5003215853|||http://purl.uniprot.org/annotation/VAR_006285|||http://purl.uniprot.org/annotation/VAR_006286|||http://purl.uniprot.org/annotation/VAR_006287|||http://purl.uniprot.org/annotation/VAR_006288|||http://purl.uniprot.org/annotation/VAR_006289|||http://purl.uniprot.org/annotation/VAR_006290|||http://purl.uniprot.org/annotation/VAR_006291|||http://purl.uniprot.org/annotation/VAR_006292|||http://purl.uniprot.org/annotation/VAR_006293|||http://purl.uniprot.org/annotation/VAR_006294|||http://purl.uniprot.org/annotation/VAR_032478|||http://purl.uniprot.org/annotation/VAR_032479|||http://purl.uniprot.org/annotation/VAR_032480|||http://purl.uniprot.org/annotation/VAR_032481|||http://purl.uniprot.org/annotation/VAR_032482|||http://purl.uniprot.org/annotation/VAR_032483|||http://purl.uniprot.org/annotation/VAR_032484|||http://purl.uniprot.org/annotation/VAR_032485|||http://purl.uniprot.org/annotation/VAR_032486|||http://purl.uniprot.org/annotation/VAR_032487|||http://purl.uniprot.org/annotation/VAR_032488|||http://purl.uniprot.org/annotation/VAR_032489|||http://purl.uniprot.org/annotation/VAR_032490|||http://purl.uniprot.org/annotation/VAR_032491|||http://purl.uniprot.org/annotation/VAR_032492|||http://purl.uniprot.org/annotation/VAR_032493|||http://purl.uniprot.org/annotation/VAR_041738|||http://purl.uniprot.org/annotation/VAR_041739|||http://purl.uniprot.org/annotation/VAR_041740|||http://purl.uniprot.org/annotation/VAR_064855|||http://purl.uniprot.org/annotation/VAR_064856|||http://purl.uniprot.org/annotation/VAR_064857|||http://purl.uniprot.org/annotation/VAR_075757|||http://purl.uniprot.org/annotation/VAR_076584|||http://purl.uniprot.org/annotation/VAR_076585|||http://purl.uniprot.org/annotation/VAR_079370|||http://purl.uniprot.org/annotation/VAR_087543|||http://purl.uniprot.org/annotation/VSP_005005|||http://purl.uniprot.org/annotation/VSP_042447|||http://purl.uniprot.org/annotation/VSP_042448
http://togogenome.org/gene/9606:STAT5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51692                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with INSR.|||Abolishes phosphorylation by HCK.|||In GHISID1; affects activation by growth hormone or interferon-gamma.|||In GHISID1; transcriptionally inactive.|||In GHISID2; exhibits strong growth hormone-induced phosphorylation, but no subsequent nuclear localization; when forming homodimers with the wild-type protein, may also prevent its nuclear localization following growth hormone-stimulation.|||In GHISID2; loss of DNA-binding ability; when forming homodimers with the wild-type protein, may prevent wild-type binding to DNA; consequently, disruption of transcriptional activity.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by HCK, JAK and PTK6|||Required for interaction with NMI|||SH2|||Signal transducer and activator of transcription 5B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182429|||http://purl.uniprot.org/annotation/VAR_018728|||http://purl.uniprot.org/annotation/VAR_052074|||http://purl.uniprot.org/annotation/VAR_067368|||http://purl.uniprot.org/annotation/VAR_085463|||http://purl.uniprot.org/annotation/VAR_085464|||http://purl.uniprot.org/annotation/VAR_085465
http://togogenome.org/gene/9606:SNRNP27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K513|||http://purl.uniprot.org/uniprot/Q8WVK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein|||U4/U6.U5 small nuclear ribonucleoprotein 27kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223965|||http://purl.uniprot.org/annotation/VAR_025363|||http://purl.uniprot.org/annotation/VAR_025364
http://togogenome.org/gene/9606:EDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2E9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Enhancer of mRNA-decapping protein 4|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Sufficient for nuclear localization|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278962|||http://purl.uniprot.org/annotation/VSP_023412
http://togogenome.org/gene/9606:PABPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VX58|||http://purl.uniprot.org/uniprot/Q9H361                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Dimethylated arginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6,N6-dimethyllysine; alternate|||Omega-N-methylarginine|||PABC|||Phosphoserine|||Phosphotyrosine|||Polyadenylate-binding protein 3|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081702
http://togogenome.org/gene/9606:ZNF37A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVV4|||http://purl.uniprot.org/uniprot/P17032                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 37A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047367|||http://purl.uniprot.org/annotation/VAR_052753
http://togogenome.org/gene/9606:CAPN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3E1|||http://purl.uniprot.org/uniprot/P20807                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calpain catalytic|||Calpain-3|||Disordered|||Domain III|||Domain IV|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In LGMDR1 and LGMDD4.|||In LGMDR1.|||In LGMDR1; severe.|||In LGMDR1; unknown pathological significance.|||In isoform II.|||In isoform III.|||In isoform IV.|||In isoform V.|||Linker|||Loss of activity. No effect on CMYA5-binding. Does not degradate p53/TP53.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207706|||http://purl.uniprot.org/annotation/VAR_001363|||http://purl.uniprot.org/annotation/VAR_001364|||http://purl.uniprot.org/annotation/VAR_001365|||http://purl.uniprot.org/annotation/VAR_001366|||http://purl.uniprot.org/annotation/VAR_001367|||http://purl.uniprot.org/annotation/VAR_001368|||http://purl.uniprot.org/annotation/VAR_001369|||http://purl.uniprot.org/annotation/VAR_001370|||http://purl.uniprot.org/annotation/VAR_009548|||http://purl.uniprot.org/annotation/VAR_009549|||http://purl.uniprot.org/annotation/VAR_009550|||http://purl.uniprot.org/annotation/VAR_009551|||http://purl.uniprot.org/annotation/VAR_009552|||http://purl.uniprot.org/annotation/VAR_009553|||http://purl.uniprot.org/annotation/VAR_009554|||http://purl.uniprot.org/annotation/VAR_009555|||http://purl.uniprot.org/annotation/VAR_009556|||http://purl.uniprot.org/annotation/VAR_009557|||http://purl.uniprot.org/annotation/VAR_009558|||http://purl.uniprot.org/annotation/VAR_009559|||http://purl.uniprot.org/annotation/VAR_009560|||http://purl.uniprot.org/annotation/VAR_009561|||http://purl.uniprot.org/annotation/VAR_009562|||http://purl.uniprot.org/annotation/VAR_009563|||http://purl.uniprot.org/annotation/VAR_009564|||http://purl.uniprot.org/annotation/VAR_009565|||http://purl.uniprot.org/annotation/VAR_009566|||http://purl.uniprot.org/annotation/VAR_009567|||http://purl.uniprot.org/annotation/VAR_009568|||http://purl.uniprot.org/annotation/VAR_009569|||http://purl.uniprot.org/annotation/VAR_009570|||http://purl.uniprot.org/annotation/VAR_009571|||http://purl.uniprot.org/annotation/VAR_009572|||http://purl.uniprot.org/annotation/VAR_009573|||http://purl.uniprot.org/annotation/VAR_009574|||http://purl.uniprot.org/annotation/VAR_009575|||http://purl.uniprot.org/annotation/VAR_009576|||http://purl.uniprot.org/annotation/VAR_009577|||http://purl.uniprot.org/annotation/VAR_009578|||http://purl.uniprot.org/annotation/VAR_009579|||http://purl.uniprot.org/annotation/VAR_009580|||http://purl.uniprot.org/annotation/VAR_009581|||http://purl.uniprot.org/annotation/VAR_009582|||http://purl.uniprot.org/annotation/VAR_009583|||http://purl.uniprot.org/annotation/VAR_009584|||http://purl.uniprot.org/annotation/VAR_009585|||http://purl.uniprot.org/annotation/VAR_009586|||http://purl.uniprot.org/annotation/VAR_009587|||http://purl.uniprot.org/annotation/VAR_009588|||http://purl.uniprot.org/annotation/VAR_009589|||http://purl.uniprot.org/annotation/VAR_009590|||http://purl.uniprot.org/annotation/VAR_009591|||http://purl.uniprot.org/annotation/VAR_009592|||http://purl.uniprot.org/annotation/VAR_009593|||http://purl.uniprot.org/annotation/VAR_009594|||http://purl.uniprot.org/annotation/VAR_009595|||http://purl.uniprot.org/annotation/VAR_009596|||http://purl.uniprot.org/annotation/VAR_009597|||http://purl.uniprot.org/annotation/VAR_009598|||http://purl.uniprot.org/annotation/VAR_009599|||http://purl.uniprot.org/annotation/VAR_009600|||http://purl.uniprot.org/annotation/VAR_015389|||http://purl.uniprot.org/annotation/VAR_022272|||http://purl.uniprot.org/annotation/VAR_047691|||http://purl.uniprot.org/annotation/VAR_076561|||http://purl.uniprot.org/annotation/VSP_005227|||http://purl.uniprot.org/annotation/VSP_005228|||http://purl.uniprot.org/annotation/VSP_005229|||http://purl.uniprot.org/annotation/VSP_007813|||http://purl.uniprot.org/annotation/VSP_044255
http://togogenome.org/gene/9606:STXBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15833|||http://purl.uniprot.org/uniprot/Q53GF4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In FHL5.|||In FHL5; leads to a complete loss of the ability to interact with STX11.|||In isoform 2.|||In isoform 3.|||Syntaxin-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206281|||http://purl.uniprot.org/annotation/VAR_014934|||http://purl.uniprot.org/annotation/VAR_063814|||http://purl.uniprot.org/annotation/VAR_063815|||http://purl.uniprot.org/annotation/VAR_063816|||http://purl.uniprot.org/annotation/VAR_063817|||http://purl.uniprot.org/annotation/VAR_063818|||http://purl.uniprot.org/annotation/VAR_063819|||http://purl.uniprot.org/annotation/VSP_040121|||http://purl.uniprot.org/annotation/VSP_055157
http://togogenome.org/gene/9606:SPHKAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3C7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein SPHKAP|||Basic and acidic residues|||Disordered|||In isoform 2.|||PKA-RII subunit binding domain|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320666|||http://purl.uniprot.org/annotation/VAR_039263|||http://purl.uniprot.org/annotation/VAR_039264|||http://purl.uniprot.org/annotation/VAR_039265|||http://purl.uniprot.org/annotation/VAR_039266|||http://purl.uniprot.org/annotation/VAR_059113|||http://purl.uniprot.org/annotation/VSP_031712
http://togogenome.org/gene/9606:ATG101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSB4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolishes interaction with ATG13; when associated with D-152 and D-152.|||Abolishes interaction with ATG13; when associated with D-152 and D-156.|||Abolishes interaction with ATG13; when associated with D-153 and D-156.|||Autophagy-related protein 101|||Impairs interaction with ATG13; when associated with R-54.|||Impairs interaction with ATG13; when associated with S-31.|||Important for interaction with ATG13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294322
http://togogenome.org/gene/9606:CLIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXU9|||http://purl.uniprot.org/uniprot/A8K6D0|||http://purl.uniprot.org/uniprot/B7Z936|||http://purl.uniprot.org/uniprot/Q8N3C7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||CAP-Gly|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly 3|||CAP-Gly domain-containing linker protein 4|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083529|||http://purl.uniprot.org/annotation/VAR_048675|||http://purl.uniprot.org/annotation/VAR_048676|||http://purl.uniprot.org/annotation/VSP_012969|||http://purl.uniprot.org/annotation/VSP_012970|||http://purl.uniprot.org/annotation/VSP_012971|||http://purl.uniprot.org/annotation/VSP_012972
http://togogenome.org/gene/9606:PSMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62191|||http://purl.uniprot.org/uniprot/Q53XL8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  26S proteasome regulatory subunit 4|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In NEDGTH; unknown pathological significance; contrary to the wild type, it fails to rescue eye defects in Rpt2-null Drosophila.|||In isoform 2.|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084677|||http://purl.uniprot.org/annotation/VAR_087793|||http://purl.uniprot.org/annotation/VSP_055768
http://togogenome.org/gene/9606:IL20RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHF4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||In isoform 3.|||Interleukin-20 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011036|||http://purl.uniprot.org/annotation/VAR_031613|||http://purl.uniprot.org/annotation/VAR_031614|||http://purl.uniprot.org/annotation/VSP_011497|||http://purl.uniprot.org/annotation/VSP_011498|||http://purl.uniprot.org/annotation/VSP_054741
http://togogenome.org/gene/9606:ING3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKQ7|||http://purl.uniprot.org/uniprot/Q9NXR8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K4me3 binding|||In HNSCC.|||In isoform 2.|||In isoform 3.|||Inhibitor of growth protein 3|||Inhibitor of growth protein N-terminal histone-binding|||N6-acetyllysine|||PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212665|||http://purl.uniprot.org/annotation/VAR_021263|||http://purl.uniprot.org/annotation/VSP_012885|||http://purl.uniprot.org/annotation/VSP_012886|||http://purl.uniprot.org/annotation/VSP_012887|||http://purl.uniprot.org/annotation/VSP_012888
http://togogenome.org/gene/9606:HNRNPCL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZW38|||http://purl.uniprot.org/uniprot/P0DMR1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Heterogeneous nuclear ribonucleoprotein C-like 3|||Heterogeneous nuclear ribonucleoprotein C-like 4|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431379|||http://purl.uniprot.org/annotation/PRO_0000431380
http://togogenome.org/gene/9606:CHD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD26                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 6|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Myb-like|||Polar residues|||Required for DNA-dependent ATPase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080231|||http://purl.uniprot.org/annotation/VAR_023363|||http://purl.uniprot.org/annotation/VAR_059213|||http://purl.uniprot.org/annotation/VSP_015296|||http://purl.uniprot.org/annotation/VSP_015297|||http://purl.uniprot.org/annotation/VSP_015298|||http://purl.uniprot.org/annotation/VSP_015299|||http://purl.uniprot.org/annotation/VSP_015300|||http://purl.uniprot.org/annotation/VSP_015301
http://togogenome.org/gene/9606:NXT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPJ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 3.|||In isoform 4.|||NTF2|||NTF2-related export protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194795|||http://purl.uniprot.org/annotation/VSP_037539|||http://purl.uniprot.org/annotation/VSP_037540
http://togogenome.org/gene/9606:SCIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6U3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-severing|||Ca(2+)-dependent actin binding|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||In isoform 2.|||In isoform 3.|||Increases calcium-independent actin-severing activity.|||Loss of actin-binding.|||Phosphotyrosine|||Scinderin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218744|||http://purl.uniprot.org/annotation/VAR_057470|||http://purl.uniprot.org/annotation/VAR_057471|||http://purl.uniprot.org/annotation/VAR_059956|||http://purl.uniprot.org/annotation/VAR_059957|||http://purl.uniprot.org/annotation/VAR_059958|||http://purl.uniprot.org/annotation/VSP_012427|||http://purl.uniprot.org/annotation/VSP_012428|||http://purl.uniprot.org/annotation/VSP_040548
http://togogenome.org/gene/9606:ADGRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94910                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor L1|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In DEDBANP.|||In DEDBANP; decreased G protein-coupled receptor signaling.|||In DEDBANP; decreased G protein-coupled receptor signaling; decreased cell surface localization.|||In DEDBANP; loss of protein expression; loss of G protein-coupled receptor signaling.|||In DEDBANP; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||SUEL-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012907|||http://purl.uniprot.org/annotation/VAR_049463|||http://purl.uniprot.org/annotation/VAR_087773|||http://purl.uniprot.org/annotation/VAR_087774|||http://purl.uniprot.org/annotation/VAR_087775|||http://purl.uniprot.org/annotation/VAR_087776|||http://purl.uniprot.org/annotation/VAR_087777|||http://purl.uniprot.org/annotation/VAR_087778|||http://purl.uniprot.org/annotation/VAR_087779|||http://purl.uniprot.org/annotation/VAR_087780|||http://purl.uniprot.org/annotation/VSP_010099
http://togogenome.org/gene/9606:PABPN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDY0|||http://purl.uniprot.org/uniprot/B6RF28                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Embryonic polyadenylate-binding protein 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349172|||http://purl.uniprot.org/annotation/VSP_035211|||http://purl.uniprot.org/annotation/VSP_035212|||http://purl.uniprot.org/annotation/VSP_035213|||http://purl.uniprot.org/annotation/VSP_035214|||http://purl.uniprot.org/annotation/VSP_040501
http://togogenome.org/gene/9606:C2orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JBF1                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:HAUS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4H7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HAUS augmin-like complex subunit 6|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076217|||http://purl.uniprot.org/annotation/VAR_024926|||http://purl.uniprot.org/annotation/VAR_024927|||http://purl.uniprot.org/annotation/VAR_062243|||http://purl.uniprot.org/annotation/VSP_017017|||http://purl.uniprot.org/annotation/VSP_017018|||http://purl.uniprot.org/annotation/VSP_040919
http://togogenome.org/gene/9606:DDX3X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFS5|||http://purl.uniprot.org/uniprot/O00571                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX3X|||Basic and acidic residues|||Complete loss of ATPase and RNA-unwinding activities. Loss of HIV-1 mRNA nuclear export. Does not promote the translation of HIV-1 RNA. No effect on IFNB1 induction. No effect on RNA-binding. Loss of inhibition of NF-kappa-B-mediated transcriptional activity.|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Does not promote the translation of HIV-1 RNA. No effect on general translation; when associated with A-200; A-230: A-347 and A-348.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-240.|||Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-183 and A-269.|||Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-181; A-240 and A-269.|||Greatly impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFNB1 induction; when associated with A-183; A-240 and A-269.|||Helicase ATP-binding|||Helicase C-terminal|||Impaired interaction with EIF4E; decreased repression of cap-dependent translation. Fails to induce stress granule assembly and to rescue cell viability after stress. No effect on translation of HIV-1 RNA; when associated with A-38.|||Impaired interaction with EIF4E; impaired stress granule formation, decreased repression of cap-dependent translation and decreased ability to enhance IRES-mediated translation. No effect on translation of HIV-1 RNA; when associated with A-43.|||Impairs nuclear export and interaction with XPO1/CMR1.|||Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-456.|||Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-442 and A-520.|||Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-438; A-456 and A-520.|||Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-429; A-442; A-456 and A-520.|||Impairs phosphorylation by TBK1 and fails to synergize with TBK1 in IFN-beta induction; when associated with A-438; A-442; A-456 and A-520.|||In MRXSSB.|||In MRXSSB; also found as a somatic mutation in medulloblastoma; loss of ATPase activity; increased interaction with CSNK1E in the absence of dsRNA; contrary to wild-type protein, strongly interacts with CSNK1A1 and CSNK1D in vivo; strongly increased ability to activate CSNK1E kinase activity, leading to increased DVL phosphorylation, thereby activating Wnt/beta-catenin signaling; increased RNA-binding; no effect on subcellular location.|||In MRXSSB; loss-of-function mutation affecting regulation of Wnt signaling.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In medulloblastoma; somatic mutation; loss of ATPase activity; interacts with CSNK1E, even in the presence of dsRNA; contrary to wild-type protein, strongly interacts with CSNK1A1 and CSNK1D in vivo; strongly increased ability to activate CSNK1E kinase activity, leading to increased DVL phosphorylation, thereby activating Wnt/beta-catenin signaling; no effect on RNA-binding, nor on subcellular location.|||Increased NF-kappa-B-mediated transcriptional activity, contrary to wild-type which is inhibitory in this experimental setting.|||Interaction with CHUK|||Interaction with EIF4E|||Interaction with GSK3B|||Interaction with HCV core protein|||Interaction with IKBKE|||Interaction with NXF1|||Interaction with VACV protein K7|||Interacts with IRF3 and enhances IFNB promoter induction.|||Involved in binding to RNA G-quadruplex|||Involved in stimulation of ATPase activity by DNA and RNA, nucleic acid binding and unwinding and HIV-1 replication|||Loss of ATPase activity.|||Loss of RNA helicase, but not ATPase activity; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, up-regulation of CDKN1A promoter activity, HNF4A-mediated MTTP transcriptional activation, nor on stress granule assembly.|||Loss of both ATPase and RNA helicase activities; decreased up-regulation of CDKN1A promoter activity and HNF4A-mediated MTTP transcriptional activation; no effect on the repression of cap- and IRES-dependent translation, WNT/beta catenin signaling, nor on stress granule assembly. Does not promote the translation of HIV-1 RNA.|||Loss of interaction with TRAF3, reduced TRAF3 'K-63'-linked autoubiquitination.|||Loss of interaction with VACV protein K7, IRF3 activation and IFNB1 promoter induction.|||N-acetylserine|||N6-acetyllysine|||No effect on general translation; when associated with A-200; A-207; A-230 and A-347.|||No effect on general translation; when associated with A-200; A-207; A-230 and A-348.|||No effect on general translation; when associated with A-200; A-207; A-347 and A-348.|||No effect on general translation; when associated with A-207; A-230; A-347 and A-348.|||Nuclear export signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CSNK1E and TBK1; in vitro|||Phosphoserine; by CSNK1E; in vitro|||Phosphoserine; by IKKE|||Phosphoserine; by TBK1|||Phosphoserine; by TBK1; in vitro|||Phosphothreonine; by CSNK1E; in vitro|||Phosphothreonine; by TBK1; in vitro|||Phosphotyrosine|||Polar residues|||Q motif|||Reduces total phosphorylation by 30%. Abolishes interaction with IRF3 and fails to enhance IFNB promoter induction. No effect on interaction with IKBKE.|||Reduces total phosphorylation by 50%. No effect on interaction with IKBKE.|||Reduces total phosphorylation by 60%. No effect on interaction with IKBKE.|||Removed|||Required for TBK1 and IKBKE-dependent IFNB1 activation|||Strong decrease in ATPase activity and RNA-unwinding activity. Does not promote the translation of mRNAs containing long structured 5'UTRs, including that of CCNE1. No effect on the translation of HIV-1 RNA. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055009|||http://purl.uniprot.org/annotation/VAR_035839|||http://purl.uniprot.org/annotation/VAR_075731|||http://purl.uniprot.org/annotation/VAR_075732|||http://purl.uniprot.org/annotation/VAR_075733|||http://purl.uniprot.org/annotation/VAR_075734|||http://purl.uniprot.org/annotation/VAR_075735|||http://purl.uniprot.org/annotation/VAR_075736|||http://purl.uniprot.org/annotation/VAR_075737|||http://purl.uniprot.org/annotation/VAR_075738|||http://purl.uniprot.org/annotation/VAR_075739|||http://purl.uniprot.org/annotation/VAR_075740|||http://purl.uniprot.org/annotation/VAR_075741|||http://purl.uniprot.org/annotation/VAR_075742|||http://purl.uniprot.org/annotation/VAR_075743|||http://purl.uniprot.org/annotation/VAR_075744|||http://purl.uniprot.org/annotation/VAR_075745|||http://purl.uniprot.org/annotation/VAR_075746|||http://purl.uniprot.org/annotation/VAR_075747|||http://purl.uniprot.org/annotation/VAR_075748|||http://purl.uniprot.org/annotation/VAR_075749|||http://purl.uniprot.org/annotation/VAR_075750|||http://purl.uniprot.org/annotation/VAR_083115|||http://purl.uniprot.org/annotation/VSP_042830
http://togogenome.org/gene/9606:OR4C16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150536|||http://purl.uniprot.org/annotation/VAR_034193|||http://purl.uniprot.org/annotation/VAR_053165|||http://purl.uniprot.org/annotation/VAR_053166|||http://purl.uniprot.org/annotation/VAR_053167|||http://purl.uniprot.org/annotation/VAR_053168
http://togogenome.org/gene/9606:PRSS22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN4                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Brain-specific serine protease 4|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027504
http://togogenome.org/gene/9606:BHLHA15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Class A basic helix-loop-helix protein 15|||Disordered|||Phosphothreonine|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127150
http://togogenome.org/gene/9606:PRAMEF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60810                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156978|||http://purl.uniprot.org/annotation/VAR_053607
http://togogenome.org/gene/9606:TIMM21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1K8|||http://purl.uniprot.org/uniprot/Q9BVV7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Mitochondrial import inner membrane translocase subunit Tim21|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043228|||http://purl.uniprot.org/annotation/VAR_052306
http://togogenome.org/gene/9606:TRIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L0X0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TLR4 interactor with leucine rich repeats                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349255|||http://purl.uniprot.org/annotation/VAR_046307|||http://purl.uniprot.org/annotation/VAR_046308|||http://purl.uniprot.org/annotation/VAR_046309|||http://purl.uniprot.org/annotation/VAR_075695
http://togogenome.org/gene/9606:TRAPPC2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL33                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In PEERB; altered intracellular trafficking from the ER to the Golgi to the plasma membrane.|||In isoform 2.|||Trafficking protein particle complex subunit 2-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294451|||http://purl.uniprot.org/annotation/VAR_081978|||http://purl.uniprot.org/annotation/VSP_026641
http://togogenome.org/gene/9606:CCNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95067                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  G2/mitotic-specific cyclin-B2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080361|||http://purl.uniprot.org/annotation/VAR_022221|||http://purl.uniprot.org/annotation/VAR_022222|||http://purl.uniprot.org/annotation/VAR_053052
http://togogenome.org/gene/9606:MCPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEM0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT 1|||BRCT 2|||BRCT 3|||Basic residues|||Disordered|||In MCPH1; mild phenotype.|||In isoform 2 and isoform 3.|||In isoform 2.|||Microcephalin|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096296|||http://purl.uniprot.org/annotation/VAR_046745|||http://purl.uniprot.org/annotation/VAR_046746|||http://purl.uniprot.org/annotation/VAR_046747|||http://purl.uniprot.org/annotation/VAR_046748|||http://purl.uniprot.org/annotation/VAR_046749|||http://purl.uniprot.org/annotation/VAR_046750|||http://purl.uniprot.org/annotation/VAR_046751|||http://purl.uniprot.org/annotation/VAR_046752|||http://purl.uniprot.org/annotation/VAR_046753|||http://purl.uniprot.org/annotation/VAR_046754|||http://purl.uniprot.org/annotation/VAR_046755|||http://purl.uniprot.org/annotation/VAR_046756|||http://purl.uniprot.org/annotation/VAR_046757|||http://purl.uniprot.org/annotation/VSP_046135|||http://purl.uniprot.org/annotation/VSP_046136|||http://purl.uniprot.org/annotation/VSP_046137
http://togogenome.org/gene/9606:CCDC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49A88                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Coiled-coil domain-containing protein 14|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333043|||http://purl.uniprot.org/annotation/VAR_043116|||http://purl.uniprot.org/annotation/VSP_033455|||http://purl.uniprot.org/annotation/VSP_033456|||http://purl.uniprot.org/annotation/VSP_033457|||http://purl.uniprot.org/annotation/VSP_033458|||http://purl.uniprot.org/annotation/VSP_033459|||http://purl.uniprot.org/annotation/VSP_033460|||http://purl.uniprot.org/annotation/VSP_039080
http://togogenome.org/gene/9606:CCDC86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6F5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Citrulline|||Coiled-coil domain-containing protein 86|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286092|||http://purl.uniprot.org/annotation/VAR_032069|||http://purl.uniprot.org/annotation/VSP_056905
http://togogenome.org/gene/9606:SLAMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13291                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disrupts interaction with INPP5D/SHIP-1 and PTPN11/SHP-2, no effect on interaction with SH2D1A.|||Disrupts interaction with SH2D1A; when associated with A-279.|||Disrupts interaction with SH2D1A; when associated with A-325.|||Disrupts interaction with SH2D1A; when associated with F-281.|||Disrupts interaction with SH2D1A; when associated with F-327.|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||Ig-like C2-type|||Ig-like V-type|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with INPP5D/SHIP-1, PTPN11/SHP-2 and SH2D1A.|||No effect on interaction with PTPN11/SHP-2 and SH2D1A.|||Phosphotyrosine; by FYN|||SH2-binding|||Signaling lymphocytic activation molecule                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014959|||http://purl.uniprot.org/annotation/VAR_021924|||http://purl.uniprot.org/annotation/VAR_021925|||http://purl.uniprot.org/annotation/VAR_035524|||http://purl.uniprot.org/annotation/VSP_002567|||http://purl.uniprot.org/annotation/VSP_002568|||http://purl.uniprot.org/annotation/VSP_002569|||http://purl.uniprot.org/annotation/VSP_058033
http://togogenome.org/gene/9606:B3GLCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Y288                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes endoplasmic reticulum localization.|||Beta-1,3-glucosyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252399|||http://purl.uniprot.org/annotation/VAR_027849
http://togogenome.org/gene/9606:SUPT20H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8L1|||http://purl.uniprot.org/uniprot/Q8NEM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spt20-like SEP|||Transcription factor SPT20 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187039|||http://purl.uniprot.org/annotation/VAR_055798|||http://purl.uniprot.org/annotation/VAR_055799|||http://purl.uniprot.org/annotation/VSP_014877|||http://purl.uniprot.org/annotation/VSP_014878|||http://purl.uniprot.org/annotation/VSP_014879|||http://purl.uniprot.org/annotation/VSP_055621
http://togogenome.org/gene/9606:RAB43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity. Disrupts Golgi structure.|||Cysteine methyl ester|||Effector region|||In isoform 3.|||Loss of phosphorylation. No effect on binding of GDI1 and GDI2.|||Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-43|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244615|||http://purl.uniprot.org/annotation/VSP_054030|||http://purl.uniprot.org/annotation/VSP_054031
http://togogenome.org/gene/9606:NCKAP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55160                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In IMD72; loss of function; T-cells display excessive degranulation and granule release; no effect on protein levels in T-cells, nor on interaction with WASF2; when tested in a heterologous system, formed WAVE complexes that poorly interact with ARF1 and could not promote F-actin polymerization upon stimulation with an ARF1-RAC1 dimer; no effect on interaction with RICTOR.|||In IMD72; loss of function; decreased protein levels in T-cells; T-cells display excessive degranulation and granule release.|||In IMD72; loss of function; decreased protein levels in T-cells; decreased interaction with WASF2 and poor formation of WAVE2 complex.|||In IMD72; loss of function; decreased protein levels in T-cells; decreased interaction with WASF2 and poor formation of WAVE2 complex; T-cells display excessive degranulation and granule release; cells exhibit reduced cortical F-actin and aberrant membrane spikes and WAS-mediated puncta, defective cell spreading and lamellipodia and reduced migratory velocity, as well as abnormal activation, blunted proliferation, decreased IL2 and TNF production and defective TCR-induced phosphorylation of mTORC2 complex substrate AKT; homozygous patient neutrophils migrating in chemokine gradients exhibit reduced velocity and directional persistence, unusual elongation and misdirected competing leading edges; no effect on interaction with RICTOR.|||In isoform 2.|||Nck-associated protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216175|||http://purl.uniprot.org/annotation/VAR_049344|||http://purl.uniprot.org/annotation/VAR_059316|||http://purl.uniprot.org/annotation/VAR_084644|||http://purl.uniprot.org/annotation/VAR_084645|||http://purl.uniprot.org/annotation/VAR_084646|||http://purl.uniprot.org/annotation/VAR_084647|||http://purl.uniprot.org/annotation/VSP_045191
http://togogenome.org/gene/9606:LRRC8C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alters channel anion selectivity.|||Basic and acidic residues|||Cytoplasmic|||Decreased amplitudes of swelling-activated current.|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Volume-regulated anion channel subunit LRRC8C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076247|||http://purl.uniprot.org/annotation/VAR_051129|||http://purl.uniprot.org/annotation/VAR_051130|||http://purl.uniprot.org/annotation/VAR_051131
http://togogenome.org/gene/9606:RNF133                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVZ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF133|||Helical|||PA|||Polar residues|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247837
http://togogenome.org/gene/9606:CFI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3L0|||http://purl.uniprot.org/uniprot/B4DRF2|||http://purl.uniprot.org/uniprot/G3XAM2|||http://purl.uniprot.org/uniprot/P05156|||http://purl.uniprot.org/uniprot/Q8WW88                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Complement factor I|||Complement factor I heavy chain|||Complement factor I light chain|||In AHUS3 and ARMD13; the mutant is both expressed and secreted at lower levels than wild-type protein; mediates C3 degradation to a lesser extent than that of controls.|||In AHUS3.|||In CFI deficiency.|||Interchain (between heavy and light chains)|||Interchain (with C-327)|||Kazal-like|||LDL-receptor class A 1|||LDL-receptor class A 2|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027568|||http://purl.uniprot.org/annotation/PRO_0000027569|||http://purl.uniprot.org/annotation/PRO_0000027570|||http://purl.uniprot.org/annotation/PRO_5002725491|||http://purl.uniprot.org/annotation/PRO_5002803245|||http://purl.uniprot.org/annotation/PRO_5004316117|||http://purl.uniprot.org/annotation/PRO_5015091879|||http://purl.uniprot.org/annotation/VAR_026757|||http://purl.uniprot.org/annotation/VAR_030343|||http://purl.uniprot.org/annotation/VAR_030344|||http://purl.uniprot.org/annotation/VAR_034907|||http://purl.uniprot.org/annotation/VAR_034908|||http://purl.uniprot.org/annotation/VAR_063665|||http://purl.uniprot.org/annotation/VAR_063666|||http://purl.uniprot.org/annotation/VAR_063667|||http://purl.uniprot.org/annotation/VAR_063668|||http://purl.uniprot.org/annotation/VAR_063669|||http://purl.uniprot.org/annotation/VAR_063670|||http://purl.uniprot.org/annotation/VAR_063671|||http://purl.uniprot.org/annotation/VAR_063672|||http://purl.uniprot.org/annotation/VAR_070843
http://togogenome.org/gene/9606:TMEM268                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Pro residues|||Transmembrane protein 268                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279425|||http://purl.uniprot.org/annotation/VSP_023426|||http://purl.uniprot.org/annotation/VSP_023427
http://togogenome.org/gene/9606:ACSBG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNS7|||http://purl.uniprot.org/uniprot/B7Z2Y6|||http://purl.uniprot.org/uniprot/Q96GR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Disordered|||Long-chain-fatty-acid--CoA ligase ACSBG1|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315808|||http://purl.uniprot.org/annotation/VAR_038314|||http://purl.uniprot.org/annotation/VAR_038315|||http://purl.uniprot.org/annotation/VAR_038316
http://togogenome.org/gene/9606:RXYLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2B1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In MDDGA10; abolishes xylosyltransferase activity.|||In MDDGA10; unknown pathological significance; loss of binding activity of alpha-dystroglycan (DAG1) for the ligand laminin in fibroblasts from patients; loss of alpha-dystroglycan functional glycosylation in fibroblasts from patients; does not affect Golgi apparatus localization.|||Ribitol-5-phosphate xylosyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072587|||http://purl.uniprot.org/annotation/VAR_069738|||http://purl.uniprot.org/annotation/VAR_069739|||http://purl.uniprot.org/annotation/VAR_085411
http://togogenome.org/gene/9606:HYI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTR5|||http://purl.uniprot.org/uniprot/F6UJY1|||http://purl.uniprot.org/uniprot/Q5T013                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||Proton donor/acceptor|||Putative hydroxypyruvate isomerase|||Xylose isomerase-like TIM barrel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289241|||http://purl.uniprot.org/annotation/VAR_032611|||http://purl.uniprot.org/annotation/VSP_025986|||http://purl.uniprot.org/annotation/VSP_025987
http://togogenome.org/gene/9606:KLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07866|||http://purl.uniprot.org/uniprot/Q7RTQ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation, leading to increased interaction with CLSTN1.|||Basic and acidic residues|||Disordered|||In isoform Cand isoform S.|||In isoform D.|||In isoform G, isoform N and isoform S.|||In isoform I.|||In isoform J and isoform N.|||In isoform J, isoform K and isoform N.|||In isoform P.|||Kinesin light chain 1|||Mimics CLSTN1, leading to decreased interaction with CLSTN1.|||No effect on motor function; when associated with A/D-521.|||No effect on motor function; when associated with A/D-524.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphotyrosine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215092|||http://purl.uniprot.org/annotation/VSP_008017|||http://purl.uniprot.org/annotation/VSP_008018|||http://purl.uniprot.org/annotation/VSP_008019|||http://purl.uniprot.org/annotation/VSP_008020|||http://purl.uniprot.org/annotation/VSP_008021|||http://purl.uniprot.org/annotation/VSP_023323|||http://purl.uniprot.org/annotation/VSP_046424
http://togogenome.org/gene/9606:SAMD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263102|||http://purl.uniprot.org/annotation/VAR_029586
http://togogenome.org/gene/9606:ORAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUB4|||http://purl.uniprot.org/uniprot/Q96SN7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein orai-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234391|||http://purl.uniprot.org/annotation/VAR_053543
http://togogenome.org/gene/9606:FBXL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N461                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box/LRR-repeat protein 16|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Omega-N-methylarginine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119863|||http://purl.uniprot.org/annotation/VAR_028163|||http://purl.uniprot.org/annotation/VSP_056996
http://togogenome.org/gene/9606:PKD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13563|||http://purl.uniprot.org/uniprot/Q9UEU6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes calcium binding via the EF-hand.|||Abolishes increased channel activity due to a gain of function mutation; when associated with P-604.|||Abolishes increased channel opening in response to cAMP and phosphorylation by PKA.|||Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-863.|||Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-860 and A-867.|||Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-849; A-863 and A-867.|||Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-846; A-860; A-863 and A-867.|||Abolishes oligomerization and interaction with PKD1; when associated with A-842; A-849; A-860; A-863 and A-867.|||Abolishes oligomerization and interaction with PKD1; when associated with A-846; A-849; A-860; A-863 and A-867.|||Abolishes phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-80.|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Decreases interaction with PACS1 and enhances expression at the cell membrane. Decreases phosphorylation; when associated with A-721; A-801; A-831 and A-943.|||Decreases phosphorylation of the N-terminal domain. Abolishes the ability to complement a pkd2-deficient zebrafish mutant; when associated with A-76.|||Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-831.|||Decreases phosphorylation; when associated with A-721; A-801; A-812 and A-943.|||Decreases phosphorylation; when associated with A-721; A-812; A-831 and A-943.|||Decreases phosphorylation; when associated with A-801; A-812; A-831 and A-943.|||Disordered|||EF-hand|||Extracellular|||Gain of function mutation.|||Gain-of-function mutation resulting in increased channel activity. Absence of gain of function; when associated with F-605 DEL; when associated with A-201; when associated with V-511; when associated with G-414; when associated with G-420; when associated with Y-684 DEL; when associated with A-684. Increased channel activity; when associated with 736-L-N-737 DEL.|||Helical; Name=5|||Helical; Name=S1|||Helical; Name=S2|||Helical; Name=S3|||Helical; Name=S4|||Helical; Name=S6|||Important for interaction with PACS1 and PACS2|||In PKD2.|||In PKD2; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604.|||In PKD2; loss of function in the release of Ca(2+) stores from the endoplasmic reticulum; no effect on location at the endoplasmic reticulum; affects channel activity as it is able to abolish channel currents induced by the gain-of-function artificial mutant P-604.|||In PKD2; somatic mutation.|||In PKD2; somatic mutation; abolishes channel currents induced by the gain-of-function artificial mutant P-604.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increased channel activity; when associated with P-604.|||Linker|||Loss of calcium-binding site; when associated with A-771.|||Loss of calcium-binding site; when associated with A-774.|||Loss of phosphorylation at Ser-801.|||Loss of phosphorylation at this site. Impairs release of Ca(2+) stores from the endoplasmic reticulum.|||Loss of protein solubility.|||Loss of protein solubility; when associated with K-849.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No effect on channel activation.|||No effect on interaction with PACS1.|||Omega-N-methylarginine|||Phosphomimetic mutant. No effect on release of Ca(2+) stores from the endoplasmic reticulum.|||Phosphoserine|||Polar residues|||Polycystin-2|||Pore-forming|||Selectivity filter|||Strongly decreases interaction with PACS1 and enhances expression at the cell membrane.|||Strongly increases calcium binding affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164356|||http://purl.uniprot.org/annotation/VAR_009195|||http://purl.uniprot.org/annotation/VAR_011072|||http://purl.uniprot.org/annotation/VAR_011073|||http://purl.uniprot.org/annotation/VAR_011074|||http://purl.uniprot.org/annotation/VAR_011075|||http://purl.uniprot.org/annotation/VAR_011076|||http://purl.uniprot.org/annotation/VAR_014919|||http://purl.uniprot.org/annotation/VAR_058820|||http://purl.uniprot.org/annotation/VAR_058821|||http://purl.uniprot.org/annotation/VAR_058822|||http://purl.uniprot.org/annotation/VAR_058823|||http://purl.uniprot.org/annotation/VAR_058824|||http://purl.uniprot.org/annotation/VAR_058825|||http://purl.uniprot.org/annotation/VAR_058826|||http://purl.uniprot.org/annotation/VAR_058827|||http://purl.uniprot.org/annotation/VAR_058828|||http://purl.uniprot.org/annotation/VAR_058829|||http://purl.uniprot.org/annotation/VAR_058830|||http://purl.uniprot.org/annotation/VAR_064394|||http://purl.uniprot.org/annotation/VSP_042479|||http://purl.uniprot.org/annotation/VSP_042480|||http://purl.uniprot.org/annotation/VSP_042481|||http://purl.uniprot.org/annotation/VSP_042482|||http://purl.uniprot.org/annotation/VSP_042483|||http://purl.uniprot.org/annotation/VSP_042484
http://togogenome.org/gene/9606:DEFB113                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KQ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 113                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045340
http://togogenome.org/gene/9606:ARSG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EG1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase G|||Decrease of sulfatase activity.|||In USH4; loss of sulfatase activity toward p-nitrocatechol sulfate; loss of processing of the precursor protein suggesting impaired transport to lysosomes.|||N-linked (GlcNAc...) asparagine|||No sulfatase activity.|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042215|||http://purl.uniprot.org/annotation/VAR_052511|||http://purl.uniprot.org/annotation/VAR_052512|||http://purl.uniprot.org/annotation/VAR_052513|||http://purl.uniprot.org/annotation/VAR_052514|||http://purl.uniprot.org/annotation/VAR_074038|||http://purl.uniprot.org/annotation/VAR_074039|||http://purl.uniprot.org/annotation/VAR_074040|||http://purl.uniprot.org/annotation/VAR_074041|||http://purl.uniprot.org/annotation/VAR_074042|||http://purl.uniprot.org/annotation/VAR_081577
http://togogenome.org/gene/9606:SLC39A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0K1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In CDG2N.|||In CDG2N; loss of manganese ion transmembrane transport; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; no effect on protein abundance.|||In CDG2N; no detectable serum or urinary manganese levels in an affected individual who also carries R-38 mutation.|||In isoform 2.|||In isoform 3.|||Metal cation symporter ZIP8|||N-linked (GlcNAc...) asparagine|||No effect on protein abundance; decreased cadmium ion transmembrane transport; increased resistance to cadmium cytotoxicity; associated with decreased activity of manganese-dependent enzymes.|||Probable disease-associated variant found in patients with Leigh-like syndrome; no effect on protein abundance; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; loss of manganese ion transmembrane transport.|||XEXPHE-motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312707|||http://purl.uniprot.org/annotation/VAR_037551|||http://purl.uniprot.org/annotation/VAR_076241|||http://purl.uniprot.org/annotation/VAR_076242|||http://purl.uniprot.org/annotation/VAR_076243|||http://purl.uniprot.org/annotation/VAR_076244|||http://purl.uniprot.org/annotation/VAR_076245|||http://purl.uniprot.org/annotation/VAR_083148|||http://purl.uniprot.org/annotation/VSP_029884|||http://purl.uniprot.org/annotation/VSP_029885|||http://purl.uniprot.org/annotation/VSP_043675
http://togogenome.org/gene/9606:CPT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAQ8|||http://purl.uniprot.org/uniprot/P50416|||http://purl.uniprot.org/uniprot/Q8WZ48                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3'-nitrotyrosine|||Carnitine O-palmitoyltransferase 1, liver isoform|||Carnitine O-palmitoyltransferase N-terminal|||Choline/carnitine acyltransferase|||Cytoplasmic|||Helical|||In CPT1AD.|||In CPT1AD; decreased activity.|||In CPT1AD; decreased stability.|||In CPT1AD; loss of activity.|||In CPT1AD; reduced protein levels.|||In isoform 2.|||Mitochondrial intermembrane|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210159|||http://purl.uniprot.org/annotation/VAR_020546|||http://purl.uniprot.org/annotation/VAR_020547|||http://purl.uniprot.org/annotation/VAR_020548|||http://purl.uniprot.org/annotation/VAR_020549|||http://purl.uniprot.org/annotation/VAR_020550|||http://purl.uniprot.org/annotation/VAR_020551|||http://purl.uniprot.org/annotation/VAR_020552|||http://purl.uniprot.org/annotation/VAR_020553|||http://purl.uniprot.org/annotation/VAR_020554|||http://purl.uniprot.org/annotation/VAR_020555|||http://purl.uniprot.org/annotation/VAR_020556|||http://purl.uniprot.org/annotation/VAR_020557|||http://purl.uniprot.org/annotation/VAR_020558|||http://purl.uniprot.org/annotation/VAR_020559|||http://purl.uniprot.org/annotation/VAR_046767|||http://purl.uniprot.org/annotation/VAR_046768|||http://purl.uniprot.org/annotation/VAR_046769|||http://purl.uniprot.org/annotation/VSP_012167
http://togogenome.org/gene/9606:ERAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75616                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Era-type G|||G1|||G2|||G3|||G4|||G5|||GTPase Era, mitochondrial|||In PRLTS6; decreased protein abundance; reduced assembly of the mitochondrial ribosomal small subunit.|||In isoform HERA-B.|||KH type-2|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180081|||http://purl.uniprot.org/annotation/VAR_079209|||http://purl.uniprot.org/annotation/VSP_001453
http://togogenome.org/gene/9606:MMP24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VV6|||http://purl.uniprot.org/uniprot/Q9Y5R2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by furin|||Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-24|||PDZ-binding|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||Pro residues|||Processed matrix metalloproteinase-24|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028846|||http://purl.uniprot.org/annotation/PRO_0000028847|||http://purl.uniprot.org/annotation/PRO_0000302758|||http://purl.uniprot.org/annotation/PRO_5004302629|||http://purl.uniprot.org/annotation/VAR_060166
http://togogenome.org/gene/9606:TMEM176A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8H6|||http://purl.uniprot.org/uniprot/Q96HP8                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Transmembrane protein 176A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279872|||http://purl.uniprot.org/annotation/VAR_031032|||http://purl.uniprot.org/annotation/VAR_031033|||http://purl.uniprot.org/annotation/VAR_031034
http://togogenome.org/gene/9606:USP51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70EK9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to deubiquitinate histone H2A; when associated with 665-R. No decrease of total H2AK15ub levels following ionizing radiation; when associated with 665-R.|||Abolishes ability to deubiquitinate histone H2A; when associated with 665-R. Suppresses ionizing radiation-induced H2AK13,15Ub; when associated with 372-R.|||Basic and acidic residues|||Disordered|||Nucleophile|||Pro residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080680
http://togogenome.org/gene/9606:SZT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T011                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in patients with intellectual disability; unknown pathological significance.|||In DEE18.|||In DEE18; alters splice sites and probably alternative splicing.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KICSTOR complex protein SZT2|||Mediates interaction with the GATOR1 complex|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000275898|||http://purl.uniprot.org/annotation/VAR_078573|||http://purl.uniprot.org/annotation/VAR_078574|||http://purl.uniprot.org/annotation/VAR_078575|||http://purl.uniprot.org/annotation/VAR_078576|||http://purl.uniprot.org/annotation/VSP_034456|||http://purl.uniprot.org/annotation/VSP_034457|||http://purl.uniprot.org/annotation/VSP_039913|||http://purl.uniprot.org/annotation/VSP_039914|||http://purl.uniprot.org/annotation/VSP_039915|||http://purl.uniprot.org/annotation/VSP_039916
http://togogenome.org/gene/9606:TRIM28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13263                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes both sumoylation and repression; when associated with R-779. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-779.|||Abolishes both sumoylation and repression; when associated with R-804. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-554 and R-804.|||Abolishes interaction with CBX5; when associated with E-488.|||Abolishes interaction with CBX5; when associated with E-490.|||B box-type 1; atypical|||B box-type 2|||Bromo|||Citrulline|||Complete loss of the PHD finger-mediated stimulatory effect on sumoylation. Loss of binding UBE2I.|||Disordered|||Disrupts the interaction with ZNF350 and amost completely relieves the transcription repressive effect of sumoylated TRIM28.|||Enhances Dox-induced CDKN1A/p21 promoter activation. Decreased sumoylation with or without Dox-treatment.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Greatly reduced interaction with PPP1CA.|||Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-668.|||Greatly reduced sumoylation. Little further effect on sumoylation; when associated with A-668 and/or A-709.|||HP1 box|||In isoform 2.|||Increased interaction with PPP1CA. Greatly decreased phosphorylation on S-824.|||Interaction with MAGEC2|||Involved in binding PPP1CA|||Leucine zipper alpha helical coiled-coil region|||Little effect on sumoylation. Little further effect on sumoylation; when associated with A-653 and/or A-709.|||Moderately reduces sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-575. Relieves the repressor activity on Dox-induced GADD45A transcription and 2-fold increase in phosphorylation at Ser-824; when associated with R-779 and R-804.|||Modestly reduced sumoylation and repression. Abolishes both sumoylation and repression; when associated with R-554.|||Modestly reduces sumoylation and repression.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-824.|||No effect on interaction with PPP1CA nor on sumoylation levels. Decreased sumoylation levels; when associated with D-501 and D-824.|||PHD-type|||Phosphoserine|||Phosphoserine; by ATM and ATR and dsDNA kinase|||Phosphothreonine|||Phosphotyrosine|||PxVxL motif|||RBCC domain|||RING-type|||Reduces nuclear localization activity of ZNF268; when associated with A-65.|||Reduces nuclear localization activity of ZNF268; when associated with A-68.|||Removed|||Some reduced sumoylation and repression.|||Some reduction in interaction with PPP1CA.|||Suppresses Dox-induced CDKN1A/p21 promoter activation. No effect on sumoylation levels. Decreased sumoylation levels; when associated with D-440 and D-501.|||Transcription intermediary factor 1-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056392|||http://purl.uniprot.org/annotation/VAR_042386|||http://purl.uniprot.org/annotation/VSP_010898
http://togogenome.org/gene/9606:DEFB103B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A894JZ42|||http://purl.uniprot.org/uniprot/P81534                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Peptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Peptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-defensin 103                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006971|||http://purl.uniprot.org/annotation/PRO_5032611455
http://togogenome.org/gene/9606:SERPINB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P63                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Reactive bond|||Serpin B12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094119|||http://purl.uniprot.org/annotation/VAR_034513|||http://purl.uniprot.org/annotation/VAR_034514|||http://purl.uniprot.org/annotation/VAR_051952|||http://purl.uniprot.org/annotation/VSP_056279
http://togogenome.org/gene/9606:OSBPL1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ56|||http://purl.uniprot.org/uniprot/B3KU11|||http://purl.uniprot.org/uniprot/Q6GSK5|||http://purl.uniprot.org/uniprot/Q9BXW6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||Disordered|||FFAT|||In isoform 4.|||In isoform A.|||Interaction with RAB7A|||Loss of interaction with MOSPD2.|||Oxysterol-binding protein-related protein 1|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100367|||http://purl.uniprot.org/annotation/VAR_053547|||http://purl.uniprot.org/annotation/VSP_003779|||http://purl.uniprot.org/annotation/VSP_045443
http://togogenome.org/gene/9606:TBX20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In ASD4; gain of function in sequence-specific DNA binding transcription factor activity; gain of function in sequence-specific DNA binding transcription factor activity in the presence of cotranscription factors NKX2-5 and GATA4 or GATA5.|||In ASD4; significant gain of function in sequence-specific DNA binding transcription factor activity; gain of function in sequence-specific DNA binding transcription factor activity in the presence of cotranscription factors NKX2-5 and GATA4 or GATA5.|||Polar residues|||T-box|||T-box transcription factor TBX20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184451|||http://purl.uniprot.org/annotation/VAR_036995|||http://purl.uniprot.org/annotation/VAR_073144
http://togogenome.org/gene/9606:NLRP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W28                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||NACHT|||NACHT, LRR and PYD domains-containing protein 8|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282990|||http://purl.uniprot.org/annotation/VAR_031452|||http://purl.uniprot.org/annotation/VAR_031453|||http://purl.uniprot.org/annotation/VAR_031454|||http://purl.uniprot.org/annotation/VAR_031455|||http://purl.uniprot.org/annotation/VAR_031456|||http://purl.uniprot.org/annotation/VAR_031457|||http://purl.uniprot.org/annotation/VAR_031458|||http://purl.uniprot.org/annotation/VAR_036383|||http://purl.uniprot.org/annotation/VAR_036384|||http://purl.uniprot.org/annotation/VAR_036385|||http://purl.uniprot.org/annotation/VAR_053618|||http://purl.uniprot.org/annotation/VAR_053619|||http://purl.uniprot.org/annotation/VSP_024274
http://togogenome.org/gene/9606:TSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969E8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In DBA14.|||Pre-rRNA-processing protein TSR2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285587|||http://purl.uniprot.org/annotation/VAR_073396
http://togogenome.org/gene/9606:CENPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0S6                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere protein L|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247170|||http://purl.uniprot.org/annotation/VAR_027081|||http://purl.uniprot.org/annotation/VSP_019939|||http://purl.uniprot.org/annotation/VSP_019940|||http://purl.uniprot.org/annotation/VSP_019941
http://togogenome.org/gene/9606:MAGED4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MAGE|||Melanoma-associated antigen D4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156728|||http://purl.uniprot.org/annotation/VSP_009287|||http://purl.uniprot.org/annotation/VSP_009288|||http://purl.uniprot.org/annotation/VSP_009289|||http://purl.uniprot.org/annotation/VSP_035013
http://togogenome.org/gene/9606:KLHL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M94|||http://purl.uniprot.org/uniprot/V9HWF1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  BACK|||BTB|||Decreased interaction with CUL3, especially with the neddylated form of CUL3.|||Decreased interaction with RBBP8 and complete loss of nuclear localization, found exclusively in the cytoplasm.|||Decreased interaction with RBBP8 and increased DNA-end resection and homologous recombination frequency following DNA double-strand breaks compared to the wild-type protein. No significant change in subcellular location.|||Impaired PPP2R5B-binding and proteasomal degradation.|||Impaired homodimerization and PPP2R5B proteasomal degradation. No effect on PPP2R5B-binding.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 15|||No effect on PPP2R5B-binding, nor on homodimerization, but loss of CUL3 recruitment to the KLHL15/PPP2R5B complex and impaired PPP2R5B proteasomal degradation.|||No effect on homodimerization, PPP2R5B-binding, nor on PPP2R5B proteasomal degradation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223949
http://togogenome.org/gene/9606:WDR81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q24JR4|||http://purl.uniprot.org/uniprot/Q562E7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||BEACH|||Disordered|||In CAMRQ2.|||In HYC3.|||In HYC3; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of interaction with MAP1LC3C; when associated with A-544.|||Loss of interaction with MAP1LC3C; when associated with A-547.|||Loss of interaction with MAP1LC3C; when associated with A-577 and A-578.|||Loss of interaction with MAP1LC3C; when associated with A-577 and A-581.|||Loss of interaction with MAP1LC3C; when associated with A-578 and A-581.|||Necessary and sufficient for the interaction with SQSTM1|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 81                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247244|||http://purl.uniprot.org/annotation/PRO_5004202388|||http://purl.uniprot.org/annotation/VAR_062107|||http://purl.uniprot.org/annotation/VAR_068220|||http://purl.uniprot.org/annotation/VAR_079037|||http://purl.uniprot.org/annotation/VAR_081120|||http://purl.uniprot.org/annotation/VAR_081121|||http://purl.uniprot.org/annotation/VSP_019955|||http://purl.uniprot.org/annotation/VSP_044063|||http://purl.uniprot.org/annotation/VSP_044064|||http://purl.uniprot.org/annotation/VSP_044065|||http://purl.uniprot.org/annotation/VSP_044066|||http://purl.uniprot.org/annotation/VSP_044067
http://togogenome.org/gene/9606:SNRPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09234|||http://purl.uniprot.org/uniprot/Q5TAL4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes the binding to U1 snRNP.|||Disordered|||Matrin-type|||N6-acetyllysine|||No effect.|||Phosphoserine|||Phosphotyrosine|||Pro residues|||U1 small nuclear ribonucleoprotein C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097525
http://togogenome.org/gene/9606:CLPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16740                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  ATP-dependent Clp protease proteolytic subunit, mitochondrial|||Abolishes protease activity.|||Disordered|||In PRLTS3.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005516|||http://purl.uniprot.org/annotation/VAR_070092|||http://purl.uniprot.org/annotation/VAR_070093|||http://purl.uniprot.org/annotation/VAR_074160
http://togogenome.org/gene/9606:AIMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MU58|||http://purl.uniprot.org/uniprot/Q13155                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AIMP2 thioredoxin-like|||Aminoacyl tRNA synthase complex-interacting multifunctional protein 2|||GST C-terminal|||Glutathione S-transferase C-terminal|||In HLD17.|||In a lung cancer cell line; no effect on proapoptotic activity.|||In a lung cancer cell line; reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity.|||In isoform 2.|||Interaction with PRKN|||Interaction with TP53|||Nearly abolishes interaction with EPRS1.|||Reduced interaction with TP53, loss of TP53 activation and loss of proapoptotic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221129|||http://purl.uniprot.org/annotation/VAR_025521|||http://purl.uniprot.org/annotation/VAR_050125|||http://purl.uniprot.org/annotation/VAR_058392|||http://purl.uniprot.org/annotation/VAR_058393|||http://purl.uniprot.org/annotation/VAR_058394|||http://purl.uniprot.org/annotation/VAR_081108|||http://purl.uniprot.org/annotation/VSP_059914
http://togogenome.org/gene/9606:IFT22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7X7                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Intraflagellar transport protein 22 homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253733|||http://purl.uniprot.org/annotation/VSP_021112|||http://purl.uniprot.org/annotation/VSP_045182
http://togogenome.org/gene/9606:SPANXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MJ10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Sperm protein associated with the nucleus on the X chromosome N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285539|||http://purl.uniprot.org/annotation/VAR_032025
http://togogenome.org/gene/9606:KRTAP4-12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ66                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31 X 5 AA repeats of C-C-[GRQVIL]-[SPTR]-[VSTQPC]|||4|||5|||6|||7|||8|||9|||In allele KAP4.12-v1.|||Keratin-associated protein 4-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185178|||http://purl.uniprot.org/annotation/VAR_064563
http://togogenome.org/gene/9606:GPR75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95800                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with age-related macular degeneration; unknown pathological significance.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 75                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069583|||http://purl.uniprot.org/annotation/VAR_033471|||http://purl.uniprot.org/annotation/VAR_033472|||http://purl.uniprot.org/annotation/VAR_033473|||http://purl.uniprot.org/annotation/VAR_071258|||http://purl.uniprot.org/annotation/VAR_071259|||http://purl.uniprot.org/annotation/VAR_071260|||http://purl.uniprot.org/annotation/VAR_071261
http://togogenome.org/gene/9606:SNX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5V6|||http://purl.uniprot.org/uniprot/Q9Y5X3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  BAR|||Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-324 and E-328.|||Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-324 and E-330.|||Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-235, E-328 and E-330.|||Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-224, E-324, E-328 and E-330.|||Decreaes phosphoinositide binding, including PtdIns(3,4)P2 and PtdIns(3P); when associated with E-235, E-324, E-328 and E-330.|||Enables homodimerization; when associated with A-280.|||Enables homodimerization; when associated with A-383.|||In isoform 2.|||Interaction with DOCK1|||Membrane-binding amphipathic helix|||N-acetylalanine|||N6-acetyllysine|||No effect on dimerization.|||PX|||Phosphoserine|||Removed|||Sorting nexin-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213844|||http://purl.uniprot.org/annotation/VSP_056386|||http://purl.uniprot.org/annotation/VSP_056387
http://togogenome.org/gene/9606:LBHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRK4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||LBH|||LBH domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444511
http://togogenome.org/gene/9606:PRDM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CA1|||http://purl.uniprot.org/uniprot/Q9NQV8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In EPM10; does not affect interaction with EPM2A and NHLRC1.|||In isoform 2.|||PR domain zinc finger protein 8|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047764|||http://purl.uniprot.org/annotation/VAR_075044|||http://purl.uniprot.org/annotation/VSP_035602|||http://purl.uniprot.org/annotation/VSP_035603
http://togogenome.org/gene/9606:AKR1C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSS8|||http://purl.uniprot.org/uniprot/B4DKT3|||http://purl.uniprot.org/uniprot/P42330                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member C3|||Decrease in the retinaldehyde reductase activity. Exhibits changes in both KM and kcat values.|||Decreases in the retinaldehyde reductase activity. 3-fold decrease in the kcat value, whereas the KM value does not vary.|||Important for substrate specificity|||In isoform 2.|||Involved in ligand recognition and product release|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||No effect on 17beta-HSD activity.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124638|||http://purl.uniprot.org/annotation/VAR_013288|||http://purl.uniprot.org/annotation/VAR_013289|||http://purl.uniprot.org/annotation/VAR_032767|||http://purl.uniprot.org/annotation/VAR_032768|||http://purl.uniprot.org/annotation/VAR_032769|||http://purl.uniprot.org/annotation/VAR_061001|||http://purl.uniprot.org/annotation/VSP_055798
http://togogenome.org/gene/9606:PIGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBL9|||http://purl.uniprot.org/uniprot/Q96IR5|||http://purl.uniprot.org/uniprot/Q96S52                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||GPI transamidase component PIG-S|||Helical|||In GPIBD18.|||In GPIBD18; almost complete loss of function; when tested in PIGS-knockout cells, mediates only very partial restoration of GPI-anchored protein expression at the cell surface; strong decrease in protein level, possibly due to nonsense-mediated mRNA decay.|||In GPIBD18; partial loss of function; when tested in PIGS-knockout cells, mediates partial restoration of GPI-anchored protein expression at the cell surface.|||In GPIBD18; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on function in GPI-anchor attachment to protein.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218604|||http://purl.uniprot.org/annotation/VAR_036510|||http://purl.uniprot.org/annotation/VAR_053582|||http://purl.uniprot.org/annotation/VAR_081579|||http://purl.uniprot.org/annotation/VAR_081580|||http://purl.uniprot.org/annotation/VAR_081581|||http://purl.uniprot.org/annotation/VAR_081582|||http://purl.uniprot.org/annotation/VSP_013158
http://togogenome.org/gene/9606:TC2N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9U0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Tandem C2 domains nuclear protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072414|||http://purl.uniprot.org/annotation/VAR_051405|||http://purl.uniprot.org/annotation/VAR_051406|||http://purl.uniprot.org/annotation/VSP_008572
http://togogenome.org/gene/9606:RELL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||RELT-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249845|||http://purl.uniprot.org/annotation/VAR_027496|||http://purl.uniprot.org/annotation/VAR_027497|||http://purl.uniprot.org/annotation/VAR_027498|||http://purl.uniprot.org/annotation/VAR_027499
http://togogenome.org/gene/9606:DOCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0U2H5|||http://purl.uniprot.org/uniprot/B2RUU3|||http://purl.uniprot.org/uniprot/Q14185                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes Rac GEF activity.|||Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 1|||Disordered|||Interaction with NCK2 (minor)|||Interaction with NCK2 second and third SH3 domain (minor)|||Interaction with NCK2 third SH3 domain (major)|||Phosphoinositide-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3|||SH3-binding; interaction with CRK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189984|||http://purl.uniprot.org/annotation/VAR_059971
http://togogenome.org/gene/9606:BAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92934                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT1|||BH3|||Bcl2-associated agonist of cell death|||Decreased methylation; when associated with K-94.|||Decreased methylation; when associated with K-96.|||Disordered|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ|||Phosphoserine; by PKB/AKT1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143103|||http://purl.uniprot.org/annotation/VAR_015380
http://togogenome.org/gene/9606:FGF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05230                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decrease in LRRC59-binding.|||Dominant-negative mutant. Defective in integrin-binding and in ternary complex formation with integrin and FGFR1. No effect on heparin- and FGFR1-binding. Defective in inducing FGF1 signaling, cell proliferation and cell migration. Defective in inducing angiogenesis, and suppression of angiogenesis in different in vitro and in vivo angiogenesis models.|||Fibroblast growth factor 1|||Heparin-binding|||In isoform 2.|||Loss of CSNK2A-, CSNK2B- and LRRC59-binding. Reduced integrin-binding; when associated with E-134. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134.|||Loss of LRRC59-binding.|||Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD.|||N-acetylalanine|||No effect on LRRC59-binding.|||No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-110.|||No effect on integrin-binding.|||No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-102 and A-109.|||No effect on integrin-binding. No effect on integrin- and heparin-binding, loss of FGFR1-binding, defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with A-109 and A-110.|||Nuclear localization signal|||Reduced integrin-binding; when associated with E-127. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-133 and E-134.|||Reduced integrin-binding; when associated with E-128. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-128; E-133 and E-134.|||Reduced integrin-binding; when associated with E-133. Defective in integrin-, heparin- and FGFR1-binding, and defective in inducing FGF1 signaling, cell proliferation and cell migration; when associated with E-127; E-128 and E-133.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008907|||http://purl.uniprot.org/annotation/PRO_0000008908|||http://purl.uniprot.org/annotation/VAR_021357|||http://purl.uniprot.org/annotation/VSP_036536|||http://purl.uniprot.org/annotation/VSP_036537
http://togogenome.org/gene/9606:DCAF4L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA75                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 4-like protein 2|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245503
http://togogenome.org/gene/9606:NT5DC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KQQ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site                                                                                  ^@                                                                                  Nucleophile|||Proton donor                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RASGEF1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N431                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-terminal Ras-GEF|||Polar residues|||Ras-GEF|||Ras-GEF domain-containing family member 1C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297643|||http://purl.uniprot.org/annotation/VSP_027316
http://togogenome.org/gene/9606:GNA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03113                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-12|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203770|||http://purl.uniprot.org/annotation/VAR_049359|||http://purl.uniprot.org/annotation/VAR_049360|||http://purl.uniprot.org/annotation/VAR_071044|||http://purl.uniprot.org/annotation/VSP_055171|||http://purl.uniprot.org/annotation/VSP_055230|||http://purl.uniprot.org/annotation/VSP_055231
http://togogenome.org/gene/9606:NUSAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 7.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 6.|||In isoform 7.|||Interaction with microtubules|||KEN box|||N6-acetyllysine|||Nucleolar and spindle-associated protein 1|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302034|||http://purl.uniprot.org/annotation/VAR_057779|||http://purl.uniprot.org/annotation/VAR_057780|||http://purl.uniprot.org/annotation/VSP_027910|||http://purl.uniprot.org/annotation/VSP_027911|||http://purl.uniprot.org/annotation/VSP_027912|||http://purl.uniprot.org/annotation/VSP_046805|||http://purl.uniprot.org/annotation/VSP_046806
http://togogenome.org/gene/9606:MRPL32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1V4|||http://purl.uniprot.org/uniprot/Q9BYC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Large ribosomal subunit protein bL32m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030513|||http://purl.uniprot.org/annotation/PRO_5014296877
http://togogenome.org/gene/9606:PNPLA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384DVU0|||http://purl.uniprot.org/uniprot/Q8IY17                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Cytoplasmic|||DGA/G|||Disordered|||Found in a patient with Gordon-Holmes syndrome; unknown pathological significance.|||Found in a patient with sporadic ataxia and BNHS; unknown pathological significance.|||GXGXXG|||GXSXG|||Helical|||In BNHS.|||In LNMS.|||In OMCS.|||In SPG39.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 5.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 6|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292199|||http://purl.uniprot.org/annotation/VAR_032949|||http://purl.uniprot.org/annotation/VAR_032950|||http://purl.uniprot.org/annotation/VAR_044409|||http://purl.uniprot.org/annotation/VAR_044410|||http://purl.uniprot.org/annotation/VAR_071091|||http://purl.uniprot.org/annotation/VAR_071092|||http://purl.uniprot.org/annotation/VAR_071093|||http://purl.uniprot.org/annotation/VAR_071094|||http://purl.uniprot.org/annotation/VAR_071095|||http://purl.uniprot.org/annotation/VAR_071096|||http://purl.uniprot.org/annotation/VAR_071097|||http://purl.uniprot.org/annotation/VAR_071098|||http://purl.uniprot.org/annotation/VAR_071099|||http://purl.uniprot.org/annotation/VAR_071100|||http://purl.uniprot.org/annotation/VAR_073409|||http://purl.uniprot.org/annotation/VAR_073410|||http://purl.uniprot.org/annotation/VAR_073411|||http://purl.uniprot.org/annotation/VAR_073412|||http://purl.uniprot.org/annotation/VAR_073413|||http://purl.uniprot.org/annotation/VAR_073414|||http://purl.uniprot.org/annotation/VAR_073415|||http://purl.uniprot.org/annotation/VAR_073416|||http://purl.uniprot.org/annotation/VSP_059668|||http://purl.uniprot.org/annotation/VSP_059669|||http://purl.uniprot.org/annotation/VSP_059670
http://togogenome.org/gene/9606:KRT71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SY84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In HYPT13; dominant negative; decreased keratin intermediate filament formation.|||Keratin, type II cytoskeletal 71|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314874|||http://purl.uniprot.org/annotation/VAR_038082|||http://purl.uniprot.org/annotation/VAR_038083|||http://purl.uniprot.org/annotation/VAR_038084|||http://purl.uniprot.org/annotation/VAR_038085|||http://purl.uniprot.org/annotation/VAR_038086|||http://purl.uniprot.org/annotation/VAR_071406
http://togogenome.org/gene/9606:SVEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQM1|||http://purl.uniprot.org/uniprot/Q4LDE5|||http://purl.uniprot.org/uniprot/Q5JB40                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8|||EGF-like 9|||HYR|||HYR 1|||HYR 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||Pentraxin (PTX)|||Sushi|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 21|||Sushi 22|||Sushi 23|||Sushi 24|||Sushi 25|||Sushi 26|||Sushi 27|||Sushi 28|||Sushi 29|||Sushi 3|||Sushi 30|||Sushi 31|||Sushi 32|||Sushi 33|||Sushi 34|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9|||Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320179|||http://purl.uniprot.org/annotation/PRO_5004257451|||http://purl.uniprot.org/annotation/VAR_039153|||http://purl.uniprot.org/annotation/VAR_039154|||http://purl.uniprot.org/annotation/VAR_039155|||http://purl.uniprot.org/annotation/VAR_039156|||http://purl.uniprot.org/annotation/VAR_039157|||http://purl.uniprot.org/annotation/VAR_039158|||http://purl.uniprot.org/annotation/VAR_039159|||http://purl.uniprot.org/annotation/VAR_039160|||http://purl.uniprot.org/annotation/VAR_039161|||http://purl.uniprot.org/annotation/VAR_039162|||http://purl.uniprot.org/annotation/VAR_039163|||http://purl.uniprot.org/annotation/VAR_039164|||http://purl.uniprot.org/annotation/VAR_039165|||http://purl.uniprot.org/annotation/VAR_039166|||http://purl.uniprot.org/annotation/VAR_039167|||http://purl.uniprot.org/annotation/VAR_039168|||http://purl.uniprot.org/annotation/VAR_039169|||http://purl.uniprot.org/annotation/VAR_039170|||http://purl.uniprot.org/annotation/VAR_039171|||http://purl.uniprot.org/annotation/VSP_031625|||http://purl.uniprot.org/annotation/VSP_031626|||http://purl.uniprot.org/annotation/VSP_031627|||http://purl.uniprot.org/annotation/VSP_031628
http://togogenome.org/gene/9606:VGLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99990                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Transcription cofactor vestigial-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191347|||http://purl.uniprot.org/annotation/VAR_053735
http://togogenome.org/gene/9606:CRIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52943                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine-rich protein 2|||Disordered|||In isoform 2.|||LIM zinc-binding 1|||LIM zinc-binding 2|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075710|||http://purl.uniprot.org/annotation/VSP_047074
http://togogenome.org/gene/9606:TUSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75896                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue                                                                                  ^@                                                                                  N-myristoyl glycine|||Phosphoserine|||Removed|||Tumor suppressor candidate 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148170
http://togogenome.org/gene/9606:APELA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMC3|||http://purl.uniprot.org/uniprot/X5D2P3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Apelin receptor early endogenous ligand|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425557
http://togogenome.org/gene/9606:SLC12A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF30|||http://purl.uniprot.org/uniprot/Q9UP95                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amino acid permease/ SLC12A|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||SLC12A transporter C-terminal|||Solute carrier family 12 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178030|||http://purl.uniprot.org/annotation/VSP_006108|||http://purl.uniprot.org/annotation/VSP_006109|||http://purl.uniprot.org/annotation/VSP_006110|||http://purl.uniprot.org/annotation/VSP_006111|||http://purl.uniprot.org/annotation/VSP_006112|||http://purl.uniprot.org/annotation/VSP_006113|||http://purl.uniprot.org/annotation/VSP_006114|||http://purl.uniprot.org/annotation/VSP_044596|||http://purl.uniprot.org/annotation/VSP_046146|||http://purl.uniprot.org/annotation/VSP_046369
http://togogenome.org/gene/9606:PCYT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E322|||http://purl.uniprot.org/uniprot/P49585                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2; approximate|||3|||3 X 11 AA approximate tandem repeats; mediates binding and activation by anionic lipid vesicles|||3 X repeats|||Abolishes formation of the interchain disulfide that can be observed when the enzyme is treated with copper phenanthrolene (in vitro).|||Amphipathic|||Basic and acidic residues|||Choline-phosphate cytidylyltransferase A|||Cytidyltransferase-like|||Disordered|||In SMDCRD.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208453|||http://purl.uniprot.org/annotation/VAR_071083|||http://purl.uniprot.org/annotation/VAR_071084|||http://purl.uniprot.org/annotation/VAR_071085|||http://purl.uniprot.org/annotation/VAR_071086|||http://purl.uniprot.org/annotation/VAR_071087|||http://purl.uniprot.org/annotation/VAR_071088
http://togogenome.org/gene/9606:RNASEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05823                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  2-5A binding (P-loop) 1|||2-5A binding (P-loop) 2|||2-5A-dependent ribonuclease|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||C6-type; atypical|||Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA.|||Complete loss of enzymatic activity.|||Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization.|||Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization.|||Disordered|||In isoform 2.|||KEN|||N6-acetyllysine|||No change in enzymatic activity.|||Protein kinase|||Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240.|||Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274.|||Risk factor for prostate cancer; reduced enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067051|||http://purl.uniprot.org/annotation/VAR_012056|||http://purl.uniprot.org/annotation/VAR_012057|||http://purl.uniprot.org/annotation/VAR_013509|||http://purl.uniprot.org/annotation/VAR_013510|||http://purl.uniprot.org/annotation/VAR_042358|||http://purl.uniprot.org/annotation/VAR_042359|||http://purl.uniprot.org/annotation/VAR_042360|||http://purl.uniprot.org/annotation/VSP_056272|||http://purl.uniprot.org/annotation/VSP_056273
http://togogenome.org/gene/9606:TDRD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R910|||http://purl.uniprot.org/uniprot/Q8NAT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||HTH OST-type|||HTH OST-type 1|||HTH OST-type 2|||HTH OST-type 3|||In isoform 1.|||Phosphoserine|||Polar residues|||Tudor|||Tudor domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183166|||http://purl.uniprot.org/annotation/VAR_031209|||http://purl.uniprot.org/annotation/VAR_031210|||http://purl.uniprot.org/annotation/VAR_036706|||http://purl.uniprot.org/annotation/VAR_052422|||http://purl.uniprot.org/annotation/VSP_023968
http://togogenome.org/gene/9606:CTSH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09668                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin H|||Cathepsin H heavy chain|||Cathepsin H light chain|||Cathepsin H mini chain|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026206|||http://purl.uniprot.org/annotation/PRO_0000026207|||http://purl.uniprot.org/annotation/PRO_0000026208|||http://purl.uniprot.org/annotation/PRO_0000026209|||http://purl.uniprot.org/annotation/PRO_0000026210|||http://purl.uniprot.org/annotation/PRO_0000026211|||http://purl.uniprot.org/annotation/VAR_036478|||http://purl.uniprot.org/annotation/VAR_057038|||http://purl.uniprot.org/annotation/VAR_057039|||http://purl.uniprot.org/annotation/VAR_060368|||http://purl.uniprot.org/annotation/VAR_067717
http://togogenome.org/gene/9606:DCAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58WW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDB1- and CUL4-associated factor 6|||Disordered|||IQ|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304401|||http://purl.uniprot.org/annotation/VAR_035020|||http://purl.uniprot.org/annotation/VSP_028019|||http://purl.uniprot.org/annotation/VSP_028020|||http://purl.uniprot.org/annotation/VSP_028021|||http://purl.uniprot.org/annotation/VSP_043312
http://togogenome.org/gene/9606:DOK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKQ6|||http://purl.uniprot.org/uniprot/O60496                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Docking protein 2|||IRS-type PTB|||PH|||Phosphotyrosine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187270|||http://purl.uniprot.org/annotation/VAR_030951|||http://purl.uniprot.org/annotation/VAR_030952|||http://purl.uniprot.org/annotation/VAR_053068
http://togogenome.org/gene/9606:ZFP28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHY6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB 1|||KRAB 2|||Zinc finger protein 28 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047289|||http://purl.uniprot.org/annotation/VAR_024190|||http://purl.uniprot.org/annotation/VAR_052738|||http://purl.uniprot.org/annotation/VSP_055934|||http://purl.uniprot.org/annotation/VSP_055935
http://togogenome.org/gene/9606:BTBD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK27|||http://purl.uniprot.org/uniprot/B4DRI6|||http://purl.uniprot.org/uniprot/Q9Y2F9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||BTB/POZ domain-containing protein 3|||Basic and acidic residues|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186211|||http://purl.uniprot.org/annotation/VSP_041215
http://togogenome.org/gene/9606:GAS2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 2|||In isoform 2.|||Interaction with ADORA2A|||Loss of microtubule-end localization, microtubule plus-end tracking, and decreases MAPRE1 binding; when associated with 369-N--N-370; 503-N-N-504; 590-N-N-591 and 795-N-N-796.|||Loss of microtubule-end localization, microtubule plus-end tracking, and decreases MAPRE1 binding; when associated with 369-N-N-370; 458-N-N-459; 503-N-N-504 and 590-N-N-591.|||Loss of microtubule-end localization, microtubule plus-end tracking, and decreases MAPRE1 binding; when associated with 369-N-N-370; 458-N-N-459; 503-N-N-504 and 795-N-N-796.|||Loss of microtubule-end localization, microtubule plus-end tracking, and decreases MAPRE1 binding; when associated with 369-N-N-370; 458-N-N-459; 590-N-N-591 and 795-N-N-796.|||Loss of microtubule-end localization, microtubule plus-end tracking, and decreases MAPRE1 binding; when associated with 458-N--N-459, 503-N-N-504; 590-N-N-591 and 795-N-N-796.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190444|||http://purl.uniprot.org/annotation/VAR_053100|||http://purl.uniprot.org/annotation/VAR_053101|||http://purl.uniprot.org/annotation/VAR_059975|||http://purl.uniprot.org/annotation/VAR_062004|||http://purl.uniprot.org/annotation/VSP_015497|||http://purl.uniprot.org/annotation/VSP_015498
http://togogenome.org/gene/9606:RPRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS64                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein reprimo                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312752
http://togogenome.org/gene/9606:PMF1-BGLAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT04|||http://purl.uniprot.org/uniprot/Q6P1K2|||http://purl.uniprot.org/uniprot/U3KQ54                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polyamine-modulated factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248237|||http://purl.uniprot.org/annotation/VAR_034147|||http://purl.uniprot.org/annotation/VAR_034148|||http://purl.uniprot.org/annotation/VSP_044638|||http://purl.uniprot.org/annotation/VSP_052136|||http://purl.uniprot.org/annotation/VSP_052137|||http://purl.uniprot.org/annotation/VSP_052138|||http://purl.uniprot.org/annotation/VSP_052139|||http://purl.uniprot.org/annotation/VSP_052140
http://togogenome.org/gene/9606:NOL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Nucleolar protein 7|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096937|||http://purl.uniprot.org/annotation/VSP_014791|||http://purl.uniprot.org/annotation/VSP_014792
http://togogenome.org/gene/9606:APOBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VD83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Apolipoprotein B receptor|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327263|||http://purl.uniprot.org/annotation/VAR_042432|||http://purl.uniprot.org/annotation/VAR_081733|||http://purl.uniprot.org/annotation/VSP_060193|||http://purl.uniprot.org/annotation/VSP_060194
http://togogenome.org/gene/9606:IRX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78413                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||In isoform 2.|||Iroquois-class homeodomain protein IRX-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049157|||http://purl.uniprot.org/annotation/VAR_049583|||http://purl.uniprot.org/annotation/VSP_054304
http://togogenome.org/gene/9606:C10orf105                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEF2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Uncharacterized protein C10orf105                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331530
http://togogenome.org/gene/9606:KCNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16389                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin|||Important for normal, slow channel gating|||In DEE32; affects channel activity; mutant channels display voltage-dependent activation significantly shifted toward negative potentials compared to wild-type; no effect on channel sensitivity to 4-aminopyridine.|||In DEE32; causes a gain of function.|||In DEE32; dominant-negative mutation; loss of channel function.|||In DEE32; loss of channel function.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphotyrosine|||Potassium voltage-gated channel subfamily A member 2|||Probable disease-associated variant found in a patient with drug-resistant epilepsy.|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter|||Tetramerization domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053972|||http://purl.uniprot.org/annotation/VAR_073704|||http://purl.uniprot.org/annotation/VAR_073705|||http://purl.uniprot.org/annotation/VAR_073706|||http://purl.uniprot.org/annotation/VAR_073707|||http://purl.uniprot.org/annotation/VAR_078206|||http://purl.uniprot.org/annotation/VAR_085682|||http://purl.uniprot.org/annotation/VSP_043077
http://togogenome.org/gene/9606:TSPY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01534                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Testis-specific Y-encoded protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185668|||http://purl.uniprot.org/annotation/VAR_016226|||http://purl.uniprot.org/annotation/VAR_016227|||http://purl.uniprot.org/annotation/VAR_016228|||http://purl.uniprot.org/annotation/VSP_008012
http://togogenome.org/gene/9606:VPS28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5H5|||http://purl.uniprot.org/uniprot/Q548N1|||http://purl.uniprot.org/uniprot/Q9UK41                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||VPS28 C-terminal|||VPS28 N-terminal|||Vacuolar protein sorting-associated protein 28 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120951|||http://purl.uniprot.org/annotation/VSP_042028
http://togogenome.org/gene/9606:FLRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-45.|||Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-47.|||Abolishes ADGRL3 binding; when associated with A-43.|||Abolishes ADGRL3 binding; when associated with A-43; A-45 and A-47.|||Abolishes ADGRL3 binding; when associated with A-64. Abolishes ADGRL3 binding; when associated with A-38; A-43 and A-47.|||Abolishes ADGRL3 binding; when associated with A-89.|||Abolishes ADGRL3 binding; when associated with A-91.|||Adds a glycosylation site that strongly reduces homodimerization; when associated with T-183.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Found in a renal cell carcinoma case; somatic mutation.|||Helical|||In HH21.|||In HH21; rare variant associated with susceptibility to disease; patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FGF17.|||In HH21; rare variant associated with susceptibility to disease; the patient has a second mutation in the HH-associated gene FGFR1.|||Interaction with ADGRL3|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane protein FLRT3|||N-linked (GlcNAc...) asparagine|||No effect on homodimerization; when associated with A-181.|||No effect on homodimerization; when associated with A-183.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021280|||http://purl.uniprot.org/annotation/VAR_017152|||http://purl.uniprot.org/annotation/VAR_050997|||http://purl.uniprot.org/annotation/VAR_050998|||http://purl.uniprot.org/annotation/VAR_064714|||http://purl.uniprot.org/annotation/VAR_069950|||http://purl.uniprot.org/annotation/VAR_069951|||http://purl.uniprot.org/annotation/VAR_069952|||http://purl.uniprot.org/annotation/VAR_069953
http://togogenome.org/gene/9606:FLYWCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CP2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FLYWCH family member 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316523
http://togogenome.org/gene/9606:CDH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55283                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003749|||http://purl.uniprot.org/annotation/PRO_0000003750|||http://purl.uniprot.org/annotation/VAR_033699|||http://purl.uniprot.org/annotation/VAR_048504|||http://purl.uniprot.org/annotation/VSP_045548
http://togogenome.org/gene/9606:TINF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSI4                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with TERF1.|||Disordered|||Does not effect interaction with TERF1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DKCA3 and DKCA5.|||In DKCA3.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||TBM|||TERF1-interacting nuclear factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072541|||http://purl.uniprot.org/annotation/VAR_043914|||http://purl.uniprot.org/annotation/VAR_043915|||http://purl.uniprot.org/annotation/VAR_043916|||http://purl.uniprot.org/annotation/VAR_051423|||http://purl.uniprot.org/annotation/VAR_051424|||http://purl.uniprot.org/annotation/VAR_051425|||http://purl.uniprot.org/annotation/VSP_003987|||http://purl.uniprot.org/annotation/VSP_003988|||http://purl.uniprot.org/annotation/VSP_003989
http://togogenome.org/gene/9606:DDX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3RJH1|||http://purl.uniprot.org/uniprot/Q92499                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX1|||Abolishes ability to promote guanylylation of RTCB.|||B30.2/SPRY|||DEAD box|||DEAD-box RNA helicase Q|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Inhibits the transcriptional activity of RELA and attenuates NF-kappa-B-mediated gene expression.|||Interaction with dsRNA|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for interaction with HNRNPK|||Necessary for interaction with RELA|||Necessary for interaction with replicase polyprotein 1ab nsp14 of IBV|||Phosphoserine|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054986|||http://purl.uniprot.org/annotation/VSP_055453|||http://purl.uniprot.org/annotation/VSP_055454|||http://purl.uniprot.org/annotation/VSP_055455
http://togogenome.org/gene/9606:KRT26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3Y9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cytoskeletal 26|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312697|||http://purl.uniprot.org/annotation/VAR_056006
http://togogenome.org/gene/9606:PLEKHO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GL0|||http://purl.uniprot.org/uniprot/Q5T4P9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Disruption of membrane localization and impaired interaction with CK2. Loss of phospholipid binding; when associated with C-42. Loss of phospholipid binding; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and C-44.|||Great loss of binding to capping proteins; when associated with A-155 and A-157.|||In isoform 2.|||Interaction with ATM, CKIP, IFP35 and NMI|||Interaction with capping proteins (CPs)|||Interacts with capping protein|||Negative regulator of AP-1 activity|||No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-155.|||No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-157.|||No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-155. Great loss of binding to capping proteins; when associated with A-155 and A-159.|||No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-157. Great loss of binding to capping proteins; when associated with A-157 and A-159.|||No effect on binding to capping proteins and loss of phospholipid binding; when associated with A-135 and A-137.|||No effect on binding to capping proteins; when associated with A-133 and A-135.|||No effect on binding to capping proteins; when associated with A-133 and A-137.|||No effect on binding to capping proteins; when associated with E-133.|||No effect on binding to capping proteins; when associated with E-135.|||No effect on subcellular localization. No effect on subcellular localization; when associated with C-42. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and W-123.|||No effect on subcellular localization. No effect on subcellular localization; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-44 and W-123.|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family O member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310423|||http://purl.uniprot.org/annotation/VAR_037034|||http://purl.uniprot.org/annotation/VSP_029282
http://togogenome.org/gene/9606:A3GALT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/U3KPV4                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-galactosyltransferase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000436524
http://togogenome.org/gene/9606:RFWD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCD5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to stimulate p53/TP53 ubiquitination. No effect on nuclear localization in response to DNA damage.|||Abolishes interaction with the RPA complex and subsequent recruitment at DNA damage sites.|||Decreased interaction with RAD51; when associated with 36-A--A-38 and 53-A--A-55.|||Decreased interaction with RAD51; when associated with 36-A--A-38 and 70-A--A-72.|||Decreased interaction with RAD51; when associated with 53-A--A-55 and 70-A--A-72.|||Disordered|||Does not affect interaction with the RPA complex and subsequent recruitment at DNA damage sites.|||E3 ubiquitin-protein ligase RFWD3|||In FANCW; abolishes interaction with the RPA complex and subsequent recruitment of the protein at DNA damage sites; decreased function in double-strand break repair via homologous recombination.|||Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-46.|||Markedly decreases phosphorylation following ionizing radiation and abolishes ability to stimulate p53/TP53 ubiquitination; when associated with A-63.|||Phosphoserine; by ATM and ATR|||Polar residues|||RING-type; degenerate|||WD 1|||WD 2|||WD 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278234|||http://purl.uniprot.org/annotation/VAR_030700|||http://purl.uniprot.org/annotation/VAR_030701|||http://purl.uniprot.org/annotation/VAR_030702|||http://purl.uniprot.org/annotation/VAR_030703|||http://purl.uniprot.org/annotation/VAR_078953
http://togogenome.org/gene/9606:RBM12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein 12B|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273366|||http://purl.uniprot.org/annotation/VAR_047291|||http://purl.uniprot.org/annotation/VAR_047292|||http://purl.uniprot.org/annotation/VAR_052219
http://togogenome.org/gene/9606:GRK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35626|||http://purl.uniprot.org/uniprot/Q8N433                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Beta-adrenergic receptor kinase 2|||Disordered|||In a lung bronchoalveolar carcinoma sample; somatic mutation.|||N-terminal|||PH|||Protein kinase|||Proton acceptor|||RGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085632|||http://purl.uniprot.org/annotation/VAR_028005|||http://purl.uniprot.org/annotation/VAR_040380|||http://purl.uniprot.org/annotation/VAR_040381|||http://purl.uniprot.org/annotation/VAR_040382
http://togogenome.org/gene/9606:OR12D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV87|||http://purl.uniprot.org/uniprot/P58182                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 12D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150728|||http://purl.uniprot.org/annotation/VAR_057569|||http://purl.uniprot.org/annotation/VAR_057570|||http://purl.uniprot.org/annotation/VAR_057571|||http://purl.uniprot.org/annotation/VAR_057572|||http://purl.uniprot.org/annotation/VAR_057573|||http://purl.uniprot.org/annotation/VAR_057574|||http://purl.uniprot.org/annotation/VAR_057575|||http://purl.uniprot.org/annotation/VAR_058967
http://togogenome.org/gene/9606:COPZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61923                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coatomer subunit zeta-1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||Reduced interaction with gamma subunit.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193825|||http://purl.uniprot.org/annotation/VSP_053675|||http://purl.uniprot.org/annotation/VSP_053676|||http://purl.uniprot.org/annotation/VSP_055049|||http://purl.uniprot.org/annotation/VSP_055050|||http://purl.uniprot.org/annotation/VSP_055051
http://togogenome.org/gene/9606:TSEN34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT51|||http://purl.uniprot.org/uniprot/E7EQB3|||http://purl.uniprot.org/uniprot/Q9BSV6                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In PCH2C.|||Polar residues|||tRNA intron endonuclease catalytic|||tRNA-splicing endonuclease subunit Sen34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109463|||http://purl.uniprot.org/annotation/VAR_054811|||http://purl.uniprot.org/annotation/VAR_061149
http://togogenome.org/gene/9606:ZNF729                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NN14                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 2; degenerate|||C2H2-type 30|||C2H2-type 31|||C2H2-type 32|||C2H2-type 33|||C2H2-type 34|||C2H2-type 35|||C2H2-type 36|||C2H2-type 37|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 729                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332314
http://togogenome.org/gene/9606:MITD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV92                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization; when associated with A-132 and A-221.|||Abolishes homodimerization; when associated with A-132 and A-225.|||Abolishes homodimerization; when associated with A-221 and A-225.|||Abolishes interaction with CHMP1A, CHMP1B and CHMP2A.|||Abolishes interaction with CHMP1A, CHMP1B and CHMP2A. Abolishes location at the midbody.|||Important for association with membranes|||MIT|||MIT domain-containing protein 1|||Strongly reduces binding to membranes; when associated with E-168 and E-231.|||Strongly reduces binding to membranes; when associated with E-221 and E-220.|||Strongly reduces binding to membranes; when associated with E-221 and E-231.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260495
http://togogenome.org/gene/9606:TDRD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WA0|||http://purl.uniprot.org/uniprot/Q8NDG6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase TDRD9|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333813|||http://purl.uniprot.org/annotation/VSP_033552
http://togogenome.org/gene/9606:EFTUD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX19|||http://purl.uniprot.org/uniprot/Q15029                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  116 kDa U5 small nuclear ribonucleoprotein component|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In MFDM.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091563|||http://purl.uniprot.org/annotation/VAR_014931|||http://purl.uniprot.org/annotation/VAR_067580|||http://purl.uniprot.org/annotation/VAR_067581|||http://purl.uniprot.org/annotation/VAR_067582|||http://purl.uniprot.org/annotation/VSP_044282|||http://purl.uniprot.org/annotation/VSP_055175
http://togogenome.org/gene/9606:PDE9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z475|||http://purl.uniprot.org/uniprot/A0A0S2Z4A3|||http://purl.uniprot.org/uniprot/A0A0S2Z4T6|||http://purl.uniprot.org/uniprot/O76083                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2 fold decreased affinity and catalytic activity for cGMP. 8 fold decreased catalytic activity for cAMP without affecting the affinity for cAMP.|||Basic and acidic residues|||Completely abolishes catalytic activity.|||Decreased affinity and catalytic activity for cGMP and cAMP.|||Disordered|||High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A|||In isoform PDE9A10.|||In isoform PDE9A11.|||In isoform PDE9A12.|||In isoform PDE9A13.|||In isoform PDE9A2, isoform PDE9A3, isoform PDE9A6, isoform PDE9A9 and isoform PDE9A21.|||In isoform PDE9A21.|||In isoform PDE9A3 and isoform PDE9A16.|||In isoform PDE9A4.|||In isoform PDE9A5.|||In isoform PDE9A6, isoform PDE9A12 and isoform PDE9A17.|||In isoform PDE9A7.|||In isoform PDE9A9 and isoform PDE9A18.|||Induces a 2 fold change in inhibitory sensitivity by BAY-73-9961.|||Induces a 6-9 fold change in inhibitory sensitivity by BAY-73-9961.|||Induces a dramatic change in inhibitory sensitivity by BAY-73-9961.|||PDEase|||Phosphoserine|||Proton donor|||Reduces catalytic activity, but has no effect on substrate affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198841|||http://purl.uniprot.org/annotation/VSP_004598|||http://purl.uniprot.org/annotation/VSP_004599|||http://purl.uniprot.org/annotation/VSP_004600|||http://purl.uniprot.org/annotation/VSP_017302|||http://purl.uniprot.org/annotation/VSP_017303|||http://purl.uniprot.org/annotation/VSP_017304|||http://purl.uniprot.org/annotation/VSP_017305|||http://purl.uniprot.org/annotation/VSP_017306|||http://purl.uniprot.org/annotation/VSP_017307|||http://purl.uniprot.org/annotation/VSP_017308|||http://purl.uniprot.org/annotation/VSP_017309|||http://purl.uniprot.org/annotation/VSP_017310|||http://purl.uniprot.org/annotation/VSP_017311|||http://purl.uniprot.org/annotation/VSP_038647
http://togogenome.org/gene/9606:M6PR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GX30|||http://purl.uniprot.org/uniprot/P20645                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation-dependent mannose-6-phosphate receptor|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||MRH|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019226|||http://purl.uniprot.org/annotation/PRO_5003323006
http://togogenome.org/gene/9606:KRTAP10-10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60014                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 5 AA repeats of C-C-X(3)|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185218|||http://purl.uniprot.org/annotation/VAR_017755|||http://purl.uniprot.org/annotation/VAR_053463|||http://purl.uniprot.org/annotation/VAR_053464|||http://purl.uniprot.org/annotation/VAR_060053|||http://purl.uniprot.org/annotation/VAR_060054|||http://purl.uniprot.org/annotation/VAR_060055|||http://purl.uniprot.org/annotation/VAR_062114
http://togogenome.org/gene/9606:REV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AI5|||http://purl.uniprot.org/uniprot/Q9UBZ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes transferase activity; when associated with A-570.|||Abolishes transferase activity; when associated with A-571.|||BRCT|||Basic residues|||DNA repair protein REV1|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with target DNA|||Nuclear localization signal|||Polar residues|||Protein interaction domain; mediates interaction with DNA polymerase zeta|||UmuC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173992|||http://purl.uniprot.org/annotation/VAR_021249|||http://purl.uniprot.org/annotation/VAR_021250|||http://purl.uniprot.org/annotation/VAR_021251|||http://purl.uniprot.org/annotation/VAR_024436|||http://purl.uniprot.org/annotation/VAR_029193|||http://purl.uniprot.org/annotation/VAR_029194|||http://purl.uniprot.org/annotation/VAR_029195|||http://purl.uniprot.org/annotation/VAR_029196|||http://purl.uniprot.org/annotation/VAR_029197|||http://purl.uniprot.org/annotation/VAR_029198|||http://purl.uniprot.org/annotation/VAR_029199|||http://purl.uniprot.org/annotation/VAR_029200|||http://purl.uniprot.org/annotation/VAR_029201|||http://purl.uniprot.org/annotation/VAR_029202|||http://purl.uniprot.org/annotation/VAR_029203|||http://purl.uniprot.org/annotation/VAR_029204|||http://purl.uniprot.org/annotation/VSP_012809|||http://purl.uniprot.org/annotation/VSP_012810|||http://purl.uniprot.org/annotation/VSP_012811|||http://purl.uniprot.org/annotation/VSP_012812
http://togogenome.org/gene/9606:DMTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08495                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Dematin|||Disordered|||HP|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-333.|||Interaction with RASGRF2|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Reduces F-actin bundling but not F-actin binding activity.|||Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-124 and A-403.|||Reduces interaction with plasmodium berghei 14-3-3 protein. Inhibits phosphorylation and interaction with plasmodium berghei 14-3-3 protein; when associated with A-333 and A-403.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218755|||http://purl.uniprot.org/annotation/VSP_004189|||http://purl.uniprot.org/annotation/VSP_044803|||http://purl.uniprot.org/annotation/VSP_057428
http://togogenome.org/gene/9606:ZBTB21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9S0|||http://purl.uniprot.org/uniprot/Q9ULJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6; atypical|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Mediates homodimerization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger and BTB domain-containing protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047515|||http://purl.uniprot.org/annotation/VAR_052807|||http://purl.uniprot.org/annotation/VAR_052808|||http://purl.uniprot.org/annotation/VSP_041349
http://togogenome.org/gene/9606:BMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C8C060|||http://purl.uniprot.org/uniprot/P12643                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bone morphogenetic protein 2|||Cleaved by PCSK5|||Complete loss of type I receptor binding.|||Disordered|||In SSFSC1.|||Interchain|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033824|||http://purl.uniprot.org/annotation/PRO_0000033825|||http://purl.uniprot.org/annotation/PRO_5010110768|||http://purl.uniprot.org/annotation/VAR_020061|||http://purl.uniprot.org/annotation/VAR_020062|||http://purl.uniprot.org/annotation/VAR_024232|||http://purl.uniprot.org/annotation/VAR_052568|||http://purl.uniprot.org/annotation/VAR_052569|||http://purl.uniprot.org/annotation/VAR_052570|||http://purl.uniprot.org/annotation/VAR_080742|||http://purl.uniprot.org/annotation/VAR_080743|||http://purl.uniprot.org/annotation/VAR_080744
http://togogenome.org/gene/9606:KCTD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM4|||http://purl.uniprot.org/uniprot/Q96CX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD12|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191295
http://togogenome.org/gene/9606:KRTAP20-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI60                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 20-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307915
http://togogenome.org/gene/9606:CHAF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13112                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chromatin assembly factor 1 subunit B|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050896|||http://purl.uniprot.org/annotation/VAR_053387
http://togogenome.org/gene/9606:USP48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UV5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DUSP 1|||DUSP 2|||DUSP 3|||Disordered|||In DFNA85; unknown pathological significance; decreased deubiquitinase activity.|||In DFNA85; unknown pathological significance; requires 2 nucleotide substitutions; decreased deubiquitinase activity.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of deubiquitinase activity.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 48|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249523|||http://purl.uniprot.org/annotation/VAR_027427|||http://purl.uniprot.org/annotation/VAR_027428|||http://purl.uniprot.org/annotation/VAR_087940|||http://purl.uniprot.org/annotation/VAR_087941|||http://purl.uniprot.org/annotation/VSP_020471|||http://purl.uniprot.org/annotation/VSP_020472|||http://purl.uniprot.org/annotation/VSP_020473|||http://purl.uniprot.org/annotation/VSP_020474|||http://purl.uniprot.org/annotation/VSP_020475|||http://purl.uniprot.org/annotation/VSP_020476|||http://purl.uniprot.org/annotation/VSP_020477|||http://purl.uniprot.org/annotation/VSP_020478|||http://purl.uniprot.org/annotation/VSP_020479|||http://purl.uniprot.org/annotation/VSP_020480|||http://purl.uniprot.org/annotation/VSP_020481|||http://purl.uniprot.org/annotation/VSP_054487|||http://purl.uniprot.org/annotation/VSP_054488
http://togogenome.org/gene/9606:FZD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULV1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FZ|||Frizzled-4|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In EVR1.|||In EVR1; 48% loss of its wild-type activity; associated in a EVR4 patient with mutation Cys-444 in LPR5.|||In EVR1; benign variant.|||In EVR1; increased signaling activity.|||In EVR1; loss of function.|||In EVR1; minor reduction of its wild-type activity.|||In EVR1; reduced signaling activity in presence of WNT3A but no change in presence of NDP/norrin.|||In a colorectal cancer sample; somatic mutation.|||In retinopathy of prematurity.|||Increased signaling activity in presence of NDP/norrin but not in presence of WNT3A.|||Increased signaling activity in presence of WNT3A but not in presence of NDP/norrin.|||Increased signaling activity.|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||No effect on signaling activity.|||PDZ-binding|||Reduced signaling activity in presence of NDP/norrin.|||Reduced signaling activity.|||Slight increase in signaling activity.|||Slightly increased signaling activity in presence of NDP/norrin and reduced signaling in presence of WNT3A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012985|||http://purl.uniprot.org/annotation/VAR_017777|||http://purl.uniprot.org/annotation/VAR_036413|||http://purl.uniprot.org/annotation/VAR_038947|||http://purl.uniprot.org/annotation/VAR_038948|||http://purl.uniprot.org/annotation/VAR_063920|||http://purl.uniprot.org/annotation/VAR_063921|||http://purl.uniprot.org/annotation/VAR_063922|||http://purl.uniprot.org/annotation/VAR_063923|||http://purl.uniprot.org/annotation/VAR_063924|||http://purl.uniprot.org/annotation/VAR_063925|||http://purl.uniprot.org/annotation/VAR_063926|||http://purl.uniprot.org/annotation/VAR_063927|||http://purl.uniprot.org/annotation/VAR_063928|||http://purl.uniprot.org/annotation/VAR_063929|||http://purl.uniprot.org/annotation/VAR_063930|||http://purl.uniprot.org/annotation/VAR_063931|||http://purl.uniprot.org/annotation/VAR_063932|||http://purl.uniprot.org/annotation/VAR_063933|||http://purl.uniprot.org/annotation/VAR_063934|||http://purl.uniprot.org/annotation/VAR_063935|||http://purl.uniprot.org/annotation/VAR_063936|||http://purl.uniprot.org/annotation/VAR_063937|||http://purl.uniprot.org/annotation/VAR_063938|||http://purl.uniprot.org/annotation/VAR_063939|||http://purl.uniprot.org/annotation/VAR_063940
http://togogenome.org/gene/9606:FAM228A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W67                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM228A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348445|||http://purl.uniprot.org/annotation/VAR_046178
http://togogenome.org/gene/9606:SIAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43255                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase SIAH2|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphoserine; by DYRK2 and MAPK14|||Phosphothreonine; by DYRK2|||Pro residues|||RING-type|||SBD|||SIAH-type|||Strongly reduced phosphorylation by DYRK2; when associated with A-16; A-26; A-28 and A-119.|||Strongly reduced phosphorylation by DYRK2; when associated with A-16; A-26; A-28 and A-68.|||Strongly reduced phosphorylation by DYRK2; when associated with A-16; A-26; A-68 and A-119.|||Strongly reduced phosphorylation by DYRK2; when associated with A-16; A-28; A-68 and A-119.|||Strongly reduced phosphorylation by DYRK2; when associated with A-26; A-28; A-68 and A-119.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056168
http://togogenome.org/gene/9606:TAS2R30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59541                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082323|||http://purl.uniprot.org/annotation/VAR_070809
http://togogenome.org/gene/9606:RMI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9A7                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||RecQ-mediated genome instability protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227546|||http://purl.uniprot.org/annotation/VAR_025556|||http://purl.uniprot.org/annotation/VAR_025557
http://togogenome.org/gene/9606:ZNF260                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5X7|||http://purl.uniprot.org/uniprot/Q3ZCT1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 260                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047320
http://togogenome.org/gene/9606:GPR20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GP3|||http://purl.uniprot.org/uniprot/Q99678                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes G(i) activation.|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 20|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069541|||http://purl.uniprot.org/annotation/VAR_055917|||http://purl.uniprot.org/annotation/VAR_055918|||http://purl.uniprot.org/annotation/VAR_055919
http://togogenome.org/gene/9606:CTAGE9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU28                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||cTAGE family member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395455
http://togogenome.org/gene/9606:NSRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZ33|||http://purl.uniprot.org/uniprot/B7ZL27|||http://purl.uniprot.org/uniprot/Q9H0G5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDSSBA.|||Inhibits nuclear localization and alternative splicing activity.|||Necessary for alternative splicing activity|||Nuclear speckle splicing regulatory protein 1|||Nuclear speckle splicing regulatory protein 1 N-terminal|||Nuclear speckle splicing regulatory protein 1 RS-like|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240434|||http://purl.uniprot.org/annotation/VAR_054104|||http://purl.uniprot.org/annotation/VAR_087656
http://togogenome.org/gene/9606:CD53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQB5|||http://purl.uniprot.org/uniprot/P19397                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Leukocyte surface antigen CD53|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219212
http://togogenome.org/gene/9606:IFI30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13284                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-72.|||Abolishes reducing activity, does not affect dimerization. Abolishes reducing activity; when associated with S-75.|||Gamma-interferon-inducible lysosomal thiol reductase|||N-linked (GlcNAc...) asparagine|||Redox-active|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021328|||http://purl.uniprot.org/annotation/PRO_0000021329|||http://purl.uniprot.org/annotation/PRO_0000021330
http://togogenome.org/gene/9606:SEC24D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6V0|||http://purl.uniprot.org/uniprot/O94855                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Gelsolin-like|||In CLCRP2.|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein transport protein Sec24D|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type|||Zinc finger-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205157|||http://purl.uniprot.org/annotation/VAR_047472|||http://purl.uniprot.org/annotation/VAR_047473|||http://purl.uniprot.org/annotation/VAR_047474|||http://purl.uniprot.org/annotation/VAR_073658|||http://purl.uniprot.org/annotation/VAR_073659|||http://purl.uniprot.org/annotation/VSP_035761
http://togogenome.org/gene/9606:PARPBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ31|||http://purl.uniprot.org/uniprot/Q9NWS1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||PCNA-interacting partner                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280269|||http://purl.uniprot.org/annotation/VAR_031105|||http://purl.uniprot.org/annotation/VSP_023587|||http://purl.uniprot.org/annotation/VSP_023588|||http://purl.uniprot.org/annotation/VSP_023589|||http://purl.uniprot.org/annotation/VSP_023590|||http://purl.uniprot.org/annotation/VSP_023591|||http://purl.uniprot.org/annotation/VSP_023592|||http://purl.uniprot.org/annotation/VSP_023593|||http://purl.uniprot.org/annotation/VSP_023594|||http://purl.uniprot.org/annotation/VSP_023595|||http://purl.uniprot.org/annotation/VSP_023596|||http://purl.uniprot.org/annotation/VSP_023597
http://togogenome.org/gene/9606:SH3BGRL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJC5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  SH3 domain-binding glutamic acid-rich-like protein 2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220747
http://togogenome.org/gene/9606:PEDS1-UBE2V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLL7|||http://purl.uniprot.org/uniprot/Q13404                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Essential for catalytic activity|||Helical|||Histidine box-1|||Histidine box-2|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of plasmanylethanolamine desaturase activity.|||N-acetylalanine|||No effect on desaturase plasmanylethanolamine activity.|||No effect on plasmanylethanolamine desaturase activity.|||Plasmanylethanolamine desaturase 1|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 variant 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082600|||http://purl.uniprot.org/annotation/PRO_0000319993|||http://purl.uniprot.org/annotation/VAR_059732|||http://purl.uniprot.org/annotation/VSP_038032|||http://purl.uniprot.org/annotation/VSP_038033|||http://purl.uniprot.org/annotation/VSP_038034|||http://purl.uniprot.org/annotation/VSP_038035|||http://purl.uniprot.org/annotation/VSP_038036|||http://purl.uniprot.org/annotation/VSP_044818|||http://purl.uniprot.org/annotation/VSP_054091
http://togogenome.org/gene/9606:CES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23141                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5.4-fold decrease in activity with p-nitrophenyl acetate as substrate; no change in affinity for p-nitrophenyl acetate; loss of activity with L- or D-methylphenidate as substrate.|||Abolishes glycosylation.|||Acyl-ester intermediate|||Charge relay system|||Does not result in secretion.|||In isoform 2.|||In isoform 3.|||Liver carboxylesterase 1|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000391359|||http://purl.uniprot.org/annotation/VAR_002357|||http://purl.uniprot.org/annotation/VAR_014314|||http://purl.uniprot.org/annotation/VAR_014594|||http://purl.uniprot.org/annotation/VAR_014595|||http://purl.uniprot.org/annotation/VAR_046954|||http://purl.uniprot.org/annotation/VSP_021026|||http://purl.uniprot.org/annotation/VSP_047158
http://togogenome.org/gene/9606:TMEM200A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2A1|||http://purl.uniprot.org/uniprot/Q86VY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Transmembrane protein 200A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294340
http://togogenome.org/gene/9606:DYRK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1A4|||http://purl.uniprot.org/uniprot/D3JEN2|||http://purl.uniprot.org/uniprot/Q9NR20                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes kinase activity.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of kinase activity.|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085940|||http://purl.uniprot.org/annotation/VAR_010721|||http://purl.uniprot.org/annotation/VAR_010722|||http://purl.uniprot.org/annotation/VAR_014948|||http://purl.uniprot.org/annotation/VAR_033900|||http://purl.uniprot.org/annotation/VAR_040465|||http://purl.uniprot.org/annotation/VSP_013745|||http://purl.uniprot.org/annotation/VSP_057132|||http://purl.uniprot.org/annotation/VSP_057133|||http://purl.uniprot.org/annotation/VSP_057134
http://togogenome.org/gene/9606:C21orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYP8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Uncharacterized protein C21orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079524
http://togogenome.org/gene/9606:LRRIQ4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat and IQ domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332138|||http://purl.uniprot.org/annotation/VAR_042953
http://togogenome.org/gene/9606:PTPRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G1UI20|||http://purl.uniprot.org/uniprot/P10586                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase F|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025432|||http://purl.uniprot.org/annotation/PRO_5003424246|||http://purl.uniprot.org/annotation/VAR_020299|||http://purl.uniprot.org/annotation/VAR_020300|||http://purl.uniprot.org/annotation/VAR_054766|||http://purl.uniprot.org/annotation/VSP_036617
http://togogenome.org/gene/9606:MMRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13201                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  155 kDa platelet multimerin|||C1q|||Cell attachment site|||Disordered|||EGF-like|||EMI|||In isoform 2.|||Multimerin-1|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein Ia*|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007821|||http://purl.uniprot.org/annotation/PRO_0000367047|||http://purl.uniprot.org/annotation/PRO_0000367048|||http://purl.uniprot.org/annotation/VAR_031471|||http://purl.uniprot.org/annotation/VAR_031472|||http://purl.uniprot.org/annotation/VAR_031473|||http://purl.uniprot.org/annotation/VAR_031474|||http://purl.uniprot.org/annotation/VSP_036610|||http://purl.uniprot.org/annotation/VSP_036611
http://togogenome.org/gene/9606:ADARB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS39                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A to I editase|||Basic residues|||DRBM 1|||DRBM 2|||Disordered|||Double-stranded RNA-specific editase B2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||Proton donor|||R-domain (ssRNA-binding)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171782|||http://purl.uniprot.org/annotation/VAR_020438|||http://purl.uniprot.org/annotation/VAR_035806|||http://purl.uniprot.org/annotation/VAR_035807|||http://purl.uniprot.org/annotation/VAR_048726|||http://purl.uniprot.org/annotation/VSP_056926|||http://purl.uniprot.org/annotation/VSP_056927
http://togogenome.org/gene/9606:UCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55851                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Dicarboxylate carrier SLC25A8|||Found in a patient with congenital hyperinsulinism; markedly decreases transporter activity.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial intermembrane|||Mitochondrial matrix|||Purine nucleotide binding|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090664|||http://purl.uniprot.org/annotation/VAR_016129|||http://purl.uniprot.org/annotation/VAR_023998|||http://purl.uniprot.org/annotation/VAR_023999|||http://purl.uniprot.org/annotation/VAR_024000|||http://purl.uniprot.org/annotation/VAR_024001
http://togogenome.org/gene/9606:SPINK14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IE38                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site                                                                                  ^@                                                                                  Kazal-like|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serine protease inhibitor Kazal-type 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000095997
http://togogenome.org/gene/9606:FCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1S4|||http://purl.uniprot.org/uniprot/Q4FZ45|||http://purl.uniprot.org/uniprot/Q9Y324                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PIN|||PINc|||rRNA-processing protein FCF1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089920
http://togogenome.org/gene/9606:PPP1CC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36873                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with microcystin toxin.|||Disordered|||In isoform 2.|||Inhibition by microcystin toxin binding|||Loss of activity.|||N-acetylalanine|||Phosphothreonine|||Proton donor|||Removed|||Serine/threonine-protein phosphatase PP1-gamma catalytic subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058787|||http://purl.uniprot.org/annotation/VAR_051734|||http://purl.uniprot.org/annotation/VSP_005094
http://togogenome.org/gene/9606:MSC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60682                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Musculin|||Nuclear localization signal|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127283
http://togogenome.org/gene/9606:UBE2O                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0C9                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (E3-independent) E2 ubiquitin-conjugating enzyme|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||Loss of function.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280637|||http://purl.uniprot.org/annotation/VAR_031184
http://togogenome.org/gene/9606:TOPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AV47|||http://purl.uniprot.org/uniprot/A7E2X7|||http://purl.uniprot.org/uniprot/Q05BV8|||http://purl.uniprot.org/uniprot/Q92547                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT|||BRCT 1|||BRCT 2|||BRCT 3|||BRCT 4|||BRCT 5|||BRCT 6|||BRCT 7|||BRCT 8|||DNA topoisomerase 2-binding protein 1|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072631|||http://purl.uniprot.org/annotation/VAR_057007|||http://purl.uniprot.org/annotation/VAR_059733|||http://purl.uniprot.org/annotation/VAR_059734
http://togogenome.org/gene/9606:F8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  40-kDa huntingtin-associated protein|||Disordered|||N-acetylalanine|||Nuclear localization signal|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087159
http://togogenome.org/gene/9606:SLC34A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06495|||http://purl.uniprot.org/uniprot/Q7Z725|||http://purl.uniprot.org/uniprot/Q86VN6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Name=M3|||Helical; Name=M4|||Helical; Name=M5|||Helical; Name=M6|||Helical; Name=M7|||Helical; Name=M8|||In FRTS2; loss of function in the homozygous state; loss of localization to cell membrane.|||In HCINF2.|||In HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; a complete intracellular retention and no detectable actin colocalization.|||In HCINF2; loss of phosphate transport activity; loss of localization to apical plasma membrane; display a complete intracellular retention and no detectable actin colocalization.|||In HCINF2; no change in phosphate transport activity; changed localization to the apical plasma membrane; partial retention inside the cell.|||In NPHLOP1; causes hypophosphatemic osteoporosis; results in lower phosphate current, decreases affinity for phosphate and decreases phosphate uptake compared to wild-type; shows a dominant-negative effect.|||In NPHLOP1; causes hypophosphatemic urolithiasis; requires 2 nucleotide substitutions; results in lower phosphate current, decreases affinity for phosphate and decreases phosphate uptake compared to wild-type; shows a dominant-negative effect.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||Sodium-dependent phosphate transport protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068607|||http://purl.uniprot.org/annotation/VAR_024765|||http://purl.uniprot.org/annotation/VAR_024766|||http://purl.uniprot.org/annotation/VAR_063812|||http://purl.uniprot.org/annotation/VAR_077913|||http://purl.uniprot.org/annotation/VAR_077914|||http://purl.uniprot.org/annotation/VAR_077915|||http://purl.uniprot.org/annotation/VAR_077916|||http://purl.uniprot.org/annotation/VAR_077917|||http://purl.uniprot.org/annotation/VAR_077918|||http://purl.uniprot.org/annotation/VAR_077919|||http://purl.uniprot.org/annotation/VAR_077920|||http://purl.uniprot.org/annotation/VSP_042311
http://togogenome.org/gene/9606:CD300LD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXZ3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMRF35-like molecule 5|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Unable to reach the cell surface upon transfection.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320126|||http://purl.uniprot.org/annotation/VAR_059386|||http://purl.uniprot.org/annotation/VAR_059387
http://togogenome.org/gene/9606:TFIP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-patch|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Required for interaction with DHX15|||Required for nuclear speckle localization|||Tuftelin-interacting protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072501|||http://purl.uniprot.org/annotation/VAR_054069|||http://purl.uniprot.org/annotation/VSP_003998|||http://purl.uniprot.org/annotation/VSP_003999
http://togogenome.org/gene/9606:HLA-DOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13765|||http://purl.uniprot.org/uniprot/Q5QNS2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1|||Beta-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DO beta chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DOB*01:02.|||In allele DOB*01:03.|||In allele DOB*01:04.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018963|||http://purl.uniprot.org/annotation/PRO_5014309921|||http://purl.uniprot.org/annotation/VAR_016743|||http://purl.uniprot.org/annotation/VAR_016744|||http://purl.uniprot.org/annotation/VAR_016745|||http://purl.uniprot.org/annotation/VAR_050363
http://togogenome.org/gene/9606:EMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N766                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||ER membrane protein complex subunit 1|||Found in patients with retinitis pigmentosa; unknown pathological significance.|||Helical|||In CAVIPMR.|||In CAVIPMR; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248597|||http://purl.uniprot.org/annotation/VAR_027359|||http://purl.uniprot.org/annotation/VAR_027360|||http://purl.uniprot.org/annotation/VAR_027361|||http://purl.uniprot.org/annotation/VAR_076915|||http://purl.uniprot.org/annotation/VAR_076916|||http://purl.uniprot.org/annotation/VAR_076917|||http://purl.uniprot.org/annotation/VAR_076918|||http://purl.uniprot.org/annotation/VSP_020327|||http://purl.uniprot.org/annotation/VSP_020328|||http://purl.uniprot.org/annotation/VSP_020329
http://togogenome.org/gene/9606:IST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXC9|||http://purl.uniprot.org/uniprot/P53990                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with VTA1, MITD1 and USP8; diminishes interaction with VPS4A.|||Diminishes interaction with VPS4A. Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with A-353. Greatly diminishes interaction with VPS4A; when associated with A-360.|||Diminishes interaction with VPS4A. Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with D-326. Greatly diminishes interaction with VPS4A; when associated with D-323.|||Diminishes interaction with VPS4A. Greatly diminishes interaction with VPS4A; when associated with A-353.|||Diminishes interaction with VPS4A. Greatly diminishes interaction with VPS4A; when associated with D-326.|||Disordered|||IST1 homolog|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Interaction with CHMP1A and CHMP1B|||Interaction with VPS37B|||Interaction with VPS4A, VTA1, MITD1 STAMBP and USP8|||Interaction with VTA1|||MIT-interacting motif|||Phosphoserine|||Phosphotyrosine|||Type-2 MIT-interacting motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050727|||http://purl.uniprot.org/annotation/VSP_017118|||http://purl.uniprot.org/annotation/VSP_017119|||http://purl.uniprot.org/annotation/VSP_017120|||http://purl.uniprot.org/annotation/VSP_047075|||http://purl.uniprot.org/annotation/VSP_047076|||http://purl.uniprot.org/annotation/VSP_055118
http://togogenome.org/gene/9606:ENTPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75355                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of activity.|||Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 3|||Extracellular|||Helical|||In isoform 2.|||Increase of ATPase activity, decrease of ADPase activity.|||Increase of activity, especially the ATP hydrolysis.|||Increase of activity.|||Loss of ATPase activity, increase of ADPase activity.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||No effect.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209910|||http://purl.uniprot.org/annotation/VAR_027541|||http://purl.uniprot.org/annotation/VAR_027542|||http://purl.uniprot.org/annotation/VAR_027543|||http://purl.uniprot.org/annotation/VAR_061384|||http://purl.uniprot.org/annotation/VAR_070813|||http://purl.uniprot.org/annotation/VSP_054237
http://togogenome.org/gene/9606:KCNJ13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60928                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modified Residue|||Motif|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with autosomal recessive retinitis pigmentosa.|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In LCA16.|||In SVD; overexpression produces a non-selective cation current that depolarizes transfected cells and increases their fragility.|||In isoform 2.|||Inward rectifier potassium channel 13|||Phosphoserine; by PKA|||Phosphoserine; by PKC|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154966|||http://purl.uniprot.org/annotation/VAR_016193|||http://purl.uniprot.org/annotation/VAR_043509|||http://purl.uniprot.org/annotation/VAR_043510|||http://purl.uniprot.org/annotation/VAR_043511|||http://purl.uniprot.org/annotation/VAR_066488|||http://purl.uniprot.org/annotation/VAR_066489|||http://purl.uniprot.org/annotation/VAR_066490|||http://purl.uniprot.org/annotation/VAR_066491|||http://purl.uniprot.org/annotation/VSP_042627|||http://purl.uniprot.org/annotation/VSP_042628
http://togogenome.org/gene/9606:STK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ06|||http://purl.uniprot.org/uniprot/A0A384MR07|||http://purl.uniprot.org/uniprot/Q13188                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Disordered|||In an ovarian clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of activity.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Resistant to proteolytic cleavage.|||SARAH|||Serine/threonine-protein kinase 3|||Serine/threonine-protein kinase 3 20kDa subunit|||Serine/threonine-protein kinase 3 36kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086689|||http://purl.uniprot.org/annotation/PRO_0000413713|||http://purl.uniprot.org/annotation/PRO_0000413714|||http://purl.uniprot.org/annotation/VAR_041122|||http://purl.uniprot.org/annotation/VAR_051670|||http://purl.uniprot.org/annotation/VSP_054167
http://togogenome.org/gene/9606:RNF151                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BNJ8|||http://purl.uniprot.org/uniprot/Q2KHN1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||RING finger protein 151|||RING-type|||TRAF-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255254
http://togogenome.org/gene/9606:OR1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVV4|||http://purl.uniprot.org/uniprot/P34982                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes nuclear translocation of ARRB2.|||Abolishes nuclear translocation of ARRB2; when associated with A-230 and A-232.|||Abolishes nuclear translocation of ARRB2; when associated with A-230 and A-239.|||Abolishes nuclear translocation of ARRB2; when associated with A-232 and A-239.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150418|||http://purl.uniprot.org/annotation/VAR_019630|||http://purl.uniprot.org/annotation/VAR_057534|||http://purl.uniprot.org/annotation/VAR_057535|||http://purl.uniprot.org/annotation/VAR_062008
http://togogenome.org/gene/9606:KCNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y85|||http://purl.uniprot.org/uniprot/Q9UIX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BTB|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||Potassium voltage-gated channel subfamily G member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054073|||http://purl.uniprot.org/annotation/VAR_053860|||http://purl.uniprot.org/annotation/VSP_001024|||http://purl.uniprot.org/annotation/VSP_001025
http://togogenome.org/gene/9606:MDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9XBC1|||http://purl.uniprot.org/uniprot/A1Z5I9|||http://purl.uniprot.org/uniprot/Q14676                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates binding to CHEK2.|||Abrogates binding to CHEK2; when associated with A-96 and A-97.|||Abrogates binding to CHEK2; when associated with A-96 and A-98.|||Abrogates binding to CHEK2; when associated with A-97 and A-98.|||Abrogates binding to the MRE11 complex and to CHEK2.|||Acidic residues|||BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with CHEK2|||Interaction with the MRN complex|||Interaction with the PRKDC complex|||Mediator of DNA damage checkpoint protein 1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by ATM|||Polar residues|||Required for nuclear localization (NLS1)|||Required for nuclear localization (NLS2)|||Suppresses RNF4-mediated ubiquitination, accumulates at sites of DNA damage, defective homologous recombination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096316|||http://purl.uniprot.org/annotation/VAR_022843|||http://purl.uniprot.org/annotation/VAR_022844|||http://purl.uniprot.org/annotation/VAR_022845|||http://purl.uniprot.org/annotation/VAR_022846|||http://purl.uniprot.org/annotation/VAR_022847|||http://purl.uniprot.org/annotation/VAR_022848|||http://purl.uniprot.org/annotation/VAR_043922|||http://purl.uniprot.org/annotation/VAR_043923|||http://purl.uniprot.org/annotation/VAR_051160|||http://purl.uniprot.org/annotation/VAR_051161|||http://purl.uniprot.org/annotation/VAR_051162|||http://purl.uniprot.org/annotation/VAR_051163|||http://purl.uniprot.org/annotation/VAR_051164|||http://purl.uniprot.org/annotation/VAR_051165|||http://purl.uniprot.org/annotation/VAR_051166|||http://purl.uniprot.org/annotation/VAR_051167|||http://purl.uniprot.org/annotation/VAR_051168|||http://purl.uniprot.org/annotation/VAR_051169|||http://purl.uniprot.org/annotation/VAR_051170|||http://purl.uniprot.org/annotation/VSP_014593|||http://purl.uniprot.org/annotation/VSP_034103|||http://purl.uniprot.org/annotation/VSP_034104
http://togogenome.org/gene/9606:LRRC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6E9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||PDZ|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:LMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25791                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||LIM zinc-binding 1|||LIM zinc-binding 2|||Rhombotin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075896|||http://purl.uniprot.org/annotation/VSP_038961|||http://purl.uniprot.org/annotation/VSP_038962|||http://purl.uniprot.org/annotation/VSP_038963
http://togogenome.org/gene/9606:FURIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09958                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cell attachment site|||Cell surface signal|||Charge relay system|||Cleavage, first; by autolysis|||Cleavage, second; by autolysis|||Cytoplasmic|||Disordered|||FU 1|||FU 2|||Furin|||Helical|||In cell line LoVo; does not undergo autocatalytic activation and is not transported to the Golgi apparatus.|||Inhibition peptide|||Loss of catalytic activity and propeptide first cleavage. Abnormal accumulation in the early secretory pathway.|||Loss of catalytic activity and propeptide second cleavage and removal. Abnormal accumulation in the early secretory pathway.|||Loss of catalytic activity and, propeptide second cleavage and removal. Normal trafficking to the Golgi.|||Lumenal|||N-linked (GlcNAc...) asparagine|||P/Homo B|||Peptidase S8|||Phosphomimetic mutant. Localization in early endosome is increased.|||Phosphoserine; by CK2|||Polar residues|||Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-773.|||Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-775.|||Trans Golgi network signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027028|||http://purl.uniprot.org/annotation/PRO_0000027029|||http://purl.uniprot.org/annotation/VAR_051821|||http://purl.uniprot.org/annotation/VAR_055343|||http://purl.uniprot.org/annotation/VAR_084542|||http://purl.uniprot.org/annotation/VAR_084543|||http://purl.uniprot.org/annotation/VAR_084544
http://togogenome.org/gene/9606:ANKRD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BM1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 9|||Disordered|||Important role in both nutrient sensing and binding/regulation of IMPDH2|||Inhibits the vesicle-to-rods transition under nutrient-limiting conditions. Inhibits the vesicle-to-rods transition under nutrient-limiting conditions; when associated with C-109. Does not affect the abundance of IMPDH2.|||Inhibits the vesicle-to-rods transition under nutrient-limiting conditions. Inhibits the vesicle-to-rods transition under nutrient-limiting conditions; when associated with C-110. Prevents the colocalization of ANKRD9 with IMPDH2 filaments. Increases the abundance of IMPDH2. Increases the abundance of IMPDH2; when associated with C-110.|||Loss the vesicle-like pattern and becomes diffuse in the cytosol.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066903
http://togogenome.org/gene/9606:SHOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15266                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In LMD.|||In LWD.|||In isoform SHOXB.|||OAR|||SH3-binding|||Short stature homeobox protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049291|||http://purl.uniprot.org/annotation/VAR_012346|||http://purl.uniprot.org/annotation/VAR_019414|||http://purl.uniprot.org/annotation/VAR_019415|||http://purl.uniprot.org/annotation/VAR_019416|||http://purl.uniprot.org/annotation/VSP_002287
http://togogenome.org/gene/9606:PGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XA84|||http://purl.uniprot.org/uniprot/P49763|||http://purl.uniprot.org/uniprot/Q53XY6|||http://purl.uniprot.org/uniprot/Q86TW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heparin-binding|||In isoform PlGF-1 and isoform PlGF-2.|||In isoform PlGF-2 and isoform PlGF-4.|||Interchain|||N-linked (GlcNAc...) asparagine|||Placenta growth factor|||Platelet-derived growth factor (PDGF) family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023420|||http://purl.uniprot.org/annotation/PRO_5003459768|||http://purl.uniprot.org/annotation/PRO_5014309522|||http://purl.uniprot.org/annotation/VSP_004644|||http://purl.uniprot.org/annotation/VSP_004645
http://togogenome.org/gene/9606:ZNF577                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSK1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 577                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234590|||http://purl.uniprot.org/annotation/VAR_033577|||http://purl.uniprot.org/annotation/VAR_055139|||http://purl.uniprot.org/annotation/VAR_055140|||http://purl.uniprot.org/annotation/VAR_055141|||http://purl.uniprot.org/annotation/VAR_055142|||http://purl.uniprot.org/annotation/VAR_055143|||http://purl.uniprot.org/annotation/VAR_055144|||http://purl.uniprot.org/annotation/VAR_055145|||http://purl.uniprot.org/annotation/VSP_040810
http://togogenome.org/gene/9606:FZD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00144                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FZ|||Frizzled-9|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||Required for CTNNB1 accumulation and TCF transcription factor activity|||Required for Wnt-activated receptor activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013003
http://togogenome.org/gene/9606:CLDN34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C241                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-34|||Cytoplasmic|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433220
http://togogenome.org/gene/9606:ABCG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H221                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 8|||Associated significantly with GBD4.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In STSL1.|||In STSL1; decreased maturation of glycan chains.|||In STSL1; strongly decreased maturation of glycan chains.|||In STSL1; unknown pathological significance.|||In isoform 2.|||Loss of ATPase activity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093396|||http://purl.uniprot.org/annotation/VAR_012250|||http://purl.uniprot.org/annotation/VAR_012251|||http://purl.uniprot.org/annotation/VAR_012252|||http://purl.uniprot.org/annotation/VAR_012253|||http://purl.uniprot.org/annotation/VAR_012254|||http://purl.uniprot.org/annotation/VAR_012255|||http://purl.uniprot.org/annotation/VAR_012256|||http://purl.uniprot.org/annotation/VAR_012257|||http://purl.uniprot.org/annotation/VAR_012258|||http://purl.uniprot.org/annotation/VAR_012259|||http://purl.uniprot.org/annotation/VAR_012260|||http://purl.uniprot.org/annotation/VAR_012261|||http://purl.uniprot.org/annotation/VAR_012262|||http://purl.uniprot.org/annotation/VAR_012263|||http://purl.uniprot.org/annotation/VAR_012264|||http://purl.uniprot.org/annotation/VAR_012265|||http://purl.uniprot.org/annotation/VAR_012266|||http://purl.uniprot.org/annotation/VAR_012267|||http://purl.uniprot.org/annotation/VAR_020785|||http://purl.uniprot.org/annotation/VAR_022074|||http://purl.uniprot.org/annotation/VAR_022075|||http://purl.uniprot.org/annotation/VSP_000052
http://togogenome.org/gene/9606:ZNHIT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWK9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Box C/D snoRNA protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIT-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280239|||http://purl.uniprot.org/annotation/VAR_031096|||http://purl.uniprot.org/annotation/VAR_035721|||http://purl.uniprot.org/annotation/VSP_042946
http://togogenome.org/gene/9606:H2AC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QV6                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 1-A|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230199
http://togogenome.org/gene/9606:SLC25A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXI2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Does not significantly change the substrate specificity.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Increases ornithine transport activity.|||Mitochondrial ornithine transporter 2|||Ornithine homo-exchange is enhanced 18-fold. Vmax value 33-fold higher than wild-type.|||Reduces ornithine transport activity.|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090652|||http://purl.uniprot.org/annotation/VAR_017248|||http://purl.uniprot.org/annotation/VAR_017249|||http://purl.uniprot.org/annotation/VAR_017250
http://togogenome.org/gene/9606:C1orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H246                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||Uncharacterized protein C1orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089246
http://togogenome.org/gene/9606:TMEM241                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH40|||http://purl.uniprot.org/uniprot/F5GXY7|||http://purl.uniprot.org/uniprot/Q24JQ0|||http://purl.uniprot.org/uniprot/Q7L033                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 241                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307316|||http://purl.uniprot.org/annotation/PRO_5002800827|||http://purl.uniprot.org/annotation/VAR_035406|||http://purl.uniprot.org/annotation/VSP_028704|||http://purl.uniprot.org/annotation/VSP_028705|||http://purl.uniprot.org/annotation/VSP_028706|||http://purl.uniprot.org/annotation/VSP_028707|||http://purl.uniprot.org/annotation/VSP_028708
http://togogenome.org/gene/9606:MUC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||28 X 19 AA approximate tandem repeats of E-E-S-X-X-X-H-X-X-P-X-X-T-X-T-X-X-X-P|||3|||4|||5|||6|||7|||8|||9|||Cleavage|||Cleavage motif|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Mucin-12|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331620|||http://purl.uniprot.org/annotation/VAR_042906|||http://purl.uniprot.org/annotation/VSP_056721
http://togogenome.org/gene/9606:H3-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NXT2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.3C|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253960|||http://purl.uniprot.org/annotation/VAR_068164
http://togogenome.org/gene/9606:TMEM215                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Transmembrane protein 215                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319324
http://togogenome.org/gene/9606:DCLRE1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJP8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DNA cross-link repair 1A protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin.|||Nuclear focus formation|||Nuclear localization region|||Phosphoserine|||UBZ4-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209116|||http://purl.uniprot.org/annotation/VAR_023286|||http://purl.uniprot.org/annotation/VAR_023287|||http://purl.uniprot.org/annotation/VAR_023288|||http://purl.uniprot.org/annotation/VAR_023289|||http://purl.uniprot.org/annotation/VAR_023290|||http://purl.uniprot.org/annotation/VAR_023291|||http://purl.uniprot.org/annotation/VAR_030574
http://togogenome.org/gene/9606:OR1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD1|||http://purl.uniprot.org/uniprot/Q8NH93                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150443|||http://purl.uniprot.org/annotation/VAR_034169|||http://purl.uniprot.org/annotation/VAR_034170|||http://purl.uniprot.org/annotation/VAR_059979
http://togogenome.org/gene/9606:NOC3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleolar complex protein 3 homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173474|||http://purl.uniprot.org/annotation/VAR_023549|||http://purl.uniprot.org/annotation/VAR_023550|||http://purl.uniprot.org/annotation/VAR_048621|||http://purl.uniprot.org/annotation/VAR_048622|||http://purl.uniprot.org/annotation/VAR_048623|||http://purl.uniprot.org/annotation/VAR_048624
http://togogenome.org/gene/9606:PRSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XMV9|||http://purl.uniprot.org/uniprot/P07478|||http://purl.uniprot.org/uniprot/Q5NV56|||http://purl.uniprot.org/uniprot/Q6PK75                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Abolishes tyrosine sulfation.|||Activation peptide|||Charge relay system|||Peptidase S1|||Required for specificity|||Sulfotyrosine|||Trypsin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028199|||http://purl.uniprot.org/annotation/PRO_0000028200|||http://purl.uniprot.org/annotation/PRO_5012677927|||http://purl.uniprot.org/annotation/PRO_5014309905|||http://purl.uniprot.org/annotation/PRO_5014565763|||http://purl.uniprot.org/annotation/VAR_051858|||http://purl.uniprot.org/annotation/VAR_071761
http://togogenome.org/gene/9606:NAE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13564                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Impairs the formation of the NEDD8-UBA3 thioester.|||In NEDFIH; unknown pathological significance.|||In NEDFIH; unknown pathological significance; decreased protein abundance in homozygous patient cells; patient cells show a decreased amount of neddylated proteins.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with UBA3|||N-acetylalanine|||N6-acetyllysine|||NEDD8-activating enzyme E1 regulatory subunit|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194951|||http://purl.uniprot.org/annotation/VAR_052435|||http://purl.uniprot.org/annotation/VAR_088123|||http://purl.uniprot.org/annotation/VAR_088124|||http://purl.uniprot.org/annotation/VAR_088125|||http://purl.uniprot.org/annotation/VAR_088126|||http://purl.uniprot.org/annotation/VSP_042895|||http://purl.uniprot.org/annotation/VSP_054258|||http://purl.uniprot.org/annotation/VSP_054259
http://togogenome.org/gene/9606:TNRC6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDV7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not impair interaction with AGO2; when associated with A-313; A-345; A-370 and A-420.|||Does not impair interaction with AGO2; when associated with A-313; A-345; A-370 and A-483.|||Does not impair interaction with AGO2; when associated with A-313; A-345; A-420 and A-483.|||Does not impair interaction with AGO2; when associated with A-313; A-370; A-420 and A-483.|||Does not impair interaction with AGO2; when associated with A-345; A-370; A-420 and A-483.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with argonaute family proteins|||PABPC1-interacting motif-2 (PAM2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||Sufficient for interaction with AGO1 and AGO4|||Sufficient for interaction with AGO1, AGO3 and AGO4|||Sufficient for interaction with AGO2|||Trinucleotide repeat-containing gene 6A protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081980|||http://purl.uniprot.org/annotation/VAR_057251|||http://purl.uniprot.org/annotation/VAR_057252|||http://purl.uniprot.org/annotation/VAR_057253|||http://purl.uniprot.org/annotation/VAR_057254|||http://purl.uniprot.org/annotation/VSP_013292|||http://purl.uniprot.org/annotation/VSP_013294|||http://purl.uniprot.org/annotation/VSP_013295|||http://purl.uniprot.org/annotation/VSP_037287|||http://purl.uniprot.org/annotation/VSP_037288|||http://purl.uniprot.org/annotation/VSP_037289
http://togogenome.org/gene/9606:ZNF77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15935                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 77                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047387|||http://purl.uniprot.org/annotation/VAR_033549|||http://purl.uniprot.org/annotation/VAR_033550|||http://purl.uniprot.org/annotation/VAR_033551|||http://purl.uniprot.org/annotation/VAR_052764|||http://purl.uniprot.org/annotation/VAR_059895
http://togogenome.org/gene/9606:GSDMC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolished cleavage by CASP8.|||Cleavage; by CASP8|||Does not affect cleavage by CASP8 in response to alpha-ketoglutarate.|||Gasdermin-C|||Gasdermin-C, C-terminal|||Gasdermin-C, N-terminal|||Impaired cleavage by CASP8 in response to alpha-ketoglutarate.|||Low spontaneous pyroptosis-inducing activity.|||Spontaneous pyroptosis-inducing activity.|||Triggers pyroptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148180|||http://purl.uniprot.org/annotation/PRO_0000451674|||http://purl.uniprot.org/annotation/PRO_0000451675|||http://purl.uniprot.org/annotation/VAR_028138|||http://purl.uniprot.org/annotation/VAR_028139|||http://purl.uniprot.org/annotation/VAR_028140
http://togogenome.org/gene/9606:UNC119B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIH7|||http://purl.uniprot.org/uniprot/Q69YW6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylserine|||N6-acetyllysine|||Protein unc-119 homolog B|||Reduced binding to myristoylated proteins; when associated with A-144 and A-148.|||Reduced binding to myristoylated proteins; when associated with A-144 and A-207.|||Reduced binding to myristoylated proteins; when associated with A-148 and A-207.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337228
http://togogenome.org/gene/9606:ARL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36405                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 3|||Enhances the interaction with RP2.|||Enhances the interaction with RP2. Does not induce a mitotic arrest resulting from the loss of the microtubule-based mitotic spindle. Induces release of myristoylated proteins from UNC119. Interacts with ARL2BP, GOLGA4, PDE6D and UNC119.|||In JBTS35.|||In JBTS35; decreased release of NPHP3 and INPP5E cargos to the cilium.|||In RP83; unknown pathological significance.|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207456|||http://purl.uniprot.org/annotation/VAR_014869|||http://purl.uniprot.org/annotation/VAR_081202|||http://purl.uniprot.org/annotation/VAR_081203|||http://purl.uniprot.org/annotation/VAR_081340
http://togogenome.org/gene/9606:CEP83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VYN8|||http://purl.uniprot.org/uniprot/Q3B787|||http://purl.uniprot.org/uniprot/Q9Y592                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 83 kDa|||Disordered|||In NPHP18; accumulates in the nucleus.|||In NPHP18; accumulates in the nucleus; does not interact with CEP164 and IFT20.|||In NPHP18; does not affect interaction with CEP164 and IFT20.|||In NPHP18; does not interact with CEP164 and IFT20.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234495|||http://purl.uniprot.org/annotation/VAR_058397|||http://purl.uniprot.org/annotation/VAR_071266|||http://purl.uniprot.org/annotation/VAR_071267|||http://purl.uniprot.org/annotation/VAR_071268|||http://purl.uniprot.org/annotation/VAR_071269|||http://purl.uniprot.org/annotation/VAR_071270|||http://purl.uniprot.org/annotation/VSP_037760|||http://purl.uniprot.org/annotation/VSP_037761|||http://purl.uniprot.org/annotation/VSP_037762
http://togogenome.org/gene/9606:NGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A346FYQ1|||http://purl.uniprot.org/uniprot/P01138                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-nerve growth factor|||Found in a patient with congenital insensitivity to pain; uncertain pathological significance.|||In HSAN5; impaired processing of the precursor to mature NGF; nearly abolishes secretion; loss of function in stimulating cell differentiation; loss of the ability to activate the NTRK1 receptor.|||In HSAN5; uncertain pathological significance.|||N-linked (GlcNAc...) asparagine|||Nerve growth factor-related|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019599|||http://purl.uniprot.org/annotation/PRO_0000019600|||http://purl.uniprot.org/annotation/VAR_013783|||http://purl.uniprot.org/annotation/VAR_025553|||http://purl.uniprot.org/annotation/VAR_025554|||http://purl.uniprot.org/annotation/VAR_030659|||http://purl.uniprot.org/annotation/VAR_068478|||http://purl.uniprot.org/annotation/VAR_068479
http://togogenome.org/gene/9606:CT47A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:ABHD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV23                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Cytoplasmic|||Decreased bis(monoacylglycero)phosphate (BMP) hydrolase activity.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Loss of 2-arachidonoyglycerol hydrolase activity.|||Loss of bis(monoacylglycero)phosphate (BMP) hydrolase activity.|||Loss of lipase activity.|||Monoacylglycerol lipase ABHD6|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281575|||http://purl.uniprot.org/annotation/VAR_081595|||http://purl.uniprot.org/annotation/VAR_081596|||http://purl.uniprot.org/annotation/VAR_081597|||http://purl.uniprot.org/annotation/VAR_081598|||http://purl.uniprot.org/annotation/VAR_081599
http://togogenome.org/gene/9606:HASPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJ70|||http://purl.uniprot.org/uniprot/Q8TF76                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation.|||Markedly reduced histone H3 phosphorylation.|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase haspin|||Strongly reduced enzyme activity, markedly reduced affinity for histone H3.|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085989|||http://purl.uniprot.org/annotation/VAR_027405|||http://purl.uniprot.org/annotation/VAR_027406|||http://purl.uniprot.org/annotation/VAR_027407|||http://purl.uniprot.org/annotation/VAR_027408|||http://purl.uniprot.org/annotation/VAR_040540|||http://purl.uniprot.org/annotation/VAR_040541|||http://purl.uniprot.org/annotation/VAR_040542|||http://purl.uniprot.org/annotation/VAR_040543|||http://purl.uniprot.org/annotation/VAR_040544|||http://purl.uniprot.org/annotation/VAR_040545|||http://purl.uniprot.org/annotation/VSP_050671|||http://purl.uniprot.org/annotation/VSP_050672
http://togogenome.org/gene/9606:TSACC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A04|||http://purl.uniprot.org/uniprot/V9GYT6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||TSSK6-activating co-chaperone protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271073|||http://purl.uniprot.org/annotation/VAR_061567
http://togogenome.org/gene/9606:GFI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99684                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abrogates transcriptional repression.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||In NI-CINA; Neutropenic and elevated monocytosis but no history of infectious complications. No effect on DNA binding but diminished GFI1 repression activity.|||In SCN2; zero neutrophil count. marked monocytosis and reduced T- and B-lymphocyte number leading to recurrent infectious complications. Abolishes recognition of DNA binding site of zinc finger. Diminished repression activity and elevated ELA2 expression. No effect on repression of CDKN1A/p21 transcription.|||Phosphoserine|||Required for interaction with RELA|||SNAG domain|||Zinc finger protein Gfi-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047193|||http://purl.uniprot.org/annotation/VAR_016212|||http://purl.uniprot.org/annotation/VAR_016213|||http://purl.uniprot.org/annotation/VAR_052722
http://togogenome.org/gene/9606:SLC38A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969I6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Influences on amino acid transport capacity|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-coupled neutral amino acid transporter 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247860|||http://purl.uniprot.org/annotation/VAR_048123|||http://purl.uniprot.org/annotation/VAR_048124|||http://purl.uniprot.org/annotation/VAR_083479
http://togogenome.org/gene/9606:KHDRBS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 2|||Omega-N-methylarginine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308953|||http://purl.uniprot.org/annotation/VAR_036885
http://togogenome.org/gene/9606:PLSCR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PG75                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phospholipid scramblase family member 5|||Proline-rich domain (PRD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293720|||http://purl.uniprot.org/annotation/VAR_057700|||http://purl.uniprot.org/annotation/VSP_054160
http://togogenome.org/gene/9606:MAVS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z434                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Cleavage by CV3B|||(Microbial infection) Cleavage by protease 2A of enterovirus 71|||(Microbial infection) Cleavage; by HAV protein 3ABC|||(Microbial infection) Cleavage; by HCV and hepatitis GB virus B NS3/4A protease complex|||(Microbial infection) Cleavage; by viral Seneca Valley virus protease 3C|||(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||Abolished UFMylation by UFM1.|||Abolished ability to bind and activate IRF3.|||Abolished ubiquitination by TRIM21.|||Abolished ubiquitination by TRIM31; when associated with R-10 and R-311.|||Abolished ubiquitination by TRIM31; when associated with R-10 and R-461.|||Abolished ubiquitination by TRIM31; when associated with R-311 and R-461.|||Asymmetric dimethylarginine|||Basic and acidic residues|||CARD|||Cleavage; by CASP3|||Complete loss of cleavage by Seneca Valley virus protease 3C.|||Complete loss of cleavage by enterovirus 71.|||Complete loss of cleavage by protease 2A of enterovirus 71.|||Cytoplasmic|||Decreased cleavage by CASP3. Abolished cleavage by CASP3; when associated with A-429.|||Decreased cleavage by CASP3. Abolished cleavage by CASP3; when associated with A-490.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Impairs ability to induce IFN-beta.|||Impairs ability to induce IFN-beta. Loss of interaction with the ATG5-ATG12 conjugate.|||Impairs filament formation and abolishes antiviral signaling activity.|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with TRAF2|||Interaction with TRAF6|||Mitochondrial antiviral-signaling protein|||Mitochondrial intermembrane|||No cleavage by HCV and hepatitis GB virus BNS3/4A protease complex.|||No cleavage by HHAV 3ABC.|||No effect on cleavage by HHAV 3ABC.|||No effect on cleavage by NS3/4A protease complex.|||No effect on cleavage by Seneca Valley virus protease 3C.|||No interaction with TRAF2.|||No interaction with TRAF6; when associated with D-155.|||No interaction with TRAF6; when associated with D-457.|||Phosphoserine|||Phosphoserine; by TBK1|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with NLRX1|||pLxIS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144096|||http://purl.uniprot.org/annotation/VAR_018448|||http://purl.uniprot.org/annotation/VAR_048609|||http://purl.uniprot.org/annotation/VAR_048610|||http://purl.uniprot.org/annotation/VAR_048611|||http://purl.uniprot.org/annotation/VAR_059197|||http://purl.uniprot.org/annotation/VSP_010261|||http://purl.uniprot.org/annotation/VSP_010262|||http://purl.uniprot.org/annotation/VSP_010263|||http://purl.uniprot.org/annotation/VSP_010264|||http://purl.uniprot.org/annotation/VSP_045872|||http://purl.uniprot.org/annotation/VSP_047816|||http://purl.uniprot.org/annotation/VSP_047817|||http://purl.uniprot.org/annotation/VSP_047818
http://togogenome.org/gene/9606:C6orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7F2|||http://purl.uniprot.org/uniprot/O95873|||http://purl.uniprot.org/uniprot/Q9UMP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Uncharacterized protein C6orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089504|||http://purl.uniprot.org/annotation/VAR_022911|||http://purl.uniprot.org/annotation/VAR_056797
http://togogenome.org/gene/9606:SELE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16581                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with coronary artery disease; no effect on ligand-specificity; may increase levels of rolling and adhesion of neutrophils and peripheral blood mononuclear cells to the endothelium; may induce constitutive stimulation of the MAPK signaling pathway, in the absence of leukocyte adhesion.|||C-type lectin|||Cytoplasmic|||Decreased adhesion to cells expressing SELPLG.|||E-selectin|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017492|||http://purl.uniprot.org/annotation/VAR_004191|||http://purl.uniprot.org/annotation/VAR_011790|||http://purl.uniprot.org/annotation/VAR_011791|||http://purl.uniprot.org/annotation/VAR_011792|||http://purl.uniprot.org/annotation/VAR_011793|||http://purl.uniprot.org/annotation/VAR_011794|||http://purl.uniprot.org/annotation/VAR_014300|||http://purl.uniprot.org/annotation/VAR_014301|||http://purl.uniprot.org/annotation/VAR_014302|||http://purl.uniprot.org/annotation/VAR_014303|||http://purl.uniprot.org/annotation/VAR_074189
http://togogenome.org/gene/9606:KPNA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15131                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Disordered|||IBB|||Importin subunit alpha-6|||In a breast cancer sample; somatic mutation.|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120728|||http://purl.uniprot.org/annotation/VAR_036245|||http://purl.uniprot.org/annotation/VAR_036246
http://togogenome.org/gene/9606:NMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08949                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Methionine amide|||Neuromedin-B|||Neuromedin-B-32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003017|||http://purl.uniprot.org/annotation/PRO_0000003018|||http://purl.uniprot.org/annotation/PRO_0000003019|||http://purl.uniprot.org/annotation/VAR_060369|||http://purl.uniprot.org/annotation/VSP_000548
http://togogenome.org/gene/9606:STUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNE7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes E3 ligase activity.|||Disordered|||E3 ubiquitin-protein ligase CHIP|||Found in a patient with progressive myoclonus epilepsy; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In SCAR16.|||In SCAR16; inhibits ubiquitin ligase activity and autoubiquitination.|||In SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination.|||In SCAR16; reduces protein level; reduces ubiquitin ligase activity; does not change autoubiquitination.|||In isoform 2.|||Loss of ability to ubiquitinate FOXP3 and SIRT6.|||Loss of interaction with FOXP3 and its ability to ubiquitinate FOXP3. Loss of interaction with SMAD3, HSPA8, HSP90AA1 and HSP90AB1.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||U-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106329|||http://purl.uniprot.org/annotation/VAR_071293|||http://purl.uniprot.org/annotation/VAR_071294|||http://purl.uniprot.org/annotation/VAR_071295|||http://purl.uniprot.org/annotation/VAR_071296|||http://purl.uniprot.org/annotation/VAR_071297|||http://purl.uniprot.org/annotation/VAR_071298|||http://purl.uniprot.org/annotation/VAR_071299|||http://purl.uniprot.org/annotation/VAR_071300|||http://purl.uniprot.org/annotation/VAR_071301|||http://purl.uniprot.org/annotation/VAR_072348|||http://purl.uniprot.org/annotation/VAR_072349|||http://purl.uniprot.org/annotation/VAR_072350|||http://purl.uniprot.org/annotation/VAR_085041|||http://purl.uniprot.org/annotation/VSP_015947
http://togogenome.org/gene/9606:QKI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY44|||http://purl.uniprot.org/uniprot/Q96PU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by CARM1; alternate|||Basic and acidic residues|||Decrease in target mRNA abundance and 10-fold decrease in RNA binding affinity; when associated with A-130.|||Decrease in target mRNA abundance and 10-fold decrease in RNA binding affinity; when associated with A-97.|||Decrease in target mRNA abundance and 124-fold decrease in RNA binding affinity; when associated with A-190.|||Decrease in target mRNA abundance and 124-fold decrease in RNA binding affinity; when associated with A-193.|||Decrease in target mRNA abundance and 20-fold decrease in RNA binding affinity; when associated with A-120.|||Decrease in target mRNA abundance and 20-fold decrease in RNA binding affinity; when associated with A-124.|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform QKI7.|||In isoform QKI6.|||In isoform QKI7B.|||Involved in RNA binding|||KH|||KH domain-containing RNA-binding protein QKI|||Nuclear localization signal|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Qua1 domain; involved in homodimerization|||Qua2 domain; involved in RNA binding|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239373|||http://purl.uniprot.org/annotation/VAR_036051|||http://purl.uniprot.org/annotation/VSP_019188|||http://purl.uniprot.org/annotation/VSP_019189|||http://purl.uniprot.org/annotation/VSP_019190|||http://purl.uniprot.org/annotation/VSP_019191
http://togogenome.org/gene/9606:ARL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40616                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 1|||Altered Golgi structure with an engorged lumen. Interacts with ARFIP2, GOLGA4, RGPD8, SCOC and UNC119.|||In isoform 2.|||Loss of interaction with ARFIP1 and ARFIP2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207450|||http://purl.uniprot.org/annotation/VSP_056566
http://togogenome.org/gene/9606:MAGI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QZ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 2, isoform 4, isoform 6 and isoform 7.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||Interaction with FCHSD2|||Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||Phosphoserine|||Polar residues|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094589|||http://purl.uniprot.org/annotation/VSP_011664|||http://purl.uniprot.org/annotation/VSP_011665|||http://purl.uniprot.org/annotation/VSP_011666|||http://purl.uniprot.org/annotation/VSP_011667|||http://purl.uniprot.org/annotation/VSP_011668|||http://purl.uniprot.org/annotation/VSP_011669|||http://purl.uniprot.org/annotation/VSP_011670|||http://purl.uniprot.org/annotation/VSP_011671|||http://purl.uniprot.org/annotation/VSP_011672
http://togogenome.org/gene/9606:KIFBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EK5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||KIF-binding protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050791|||http://purl.uniprot.org/annotation/VAR_023311
http://togogenome.org/gene/9606:NACA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H009                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine; alternate|||NAC-A/B|||Nascent polypeptide-associated complex subunit alpha-2|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280746|||http://purl.uniprot.org/annotation/VAR_050218
http://togogenome.org/gene/9606:CLIC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53G01|||http://purl.uniprot.org/uniprot/Q9NZA1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chloride intracellular channel protein 5|||GST C-terminal|||Helical; Note=After insertion into the membrane|||In isoform 1.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144214|||http://purl.uniprot.org/annotation/VAR_047541|||http://purl.uniprot.org/annotation/VAR_059208|||http://purl.uniprot.org/annotation/VSP_000869|||http://purl.uniprot.org/annotation/VSP_000870|||http://purl.uniprot.org/annotation/VSP_044889|||http://purl.uniprot.org/annotation/VSP_044890|||http://purl.uniprot.org/annotation/VSP_044891
http://togogenome.org/gene/9606:SLC9A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GV11|||http://purl.uniprot.org/uniprot/Q92581                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cation/H+ exchanger|||Does not affect post-translational maturation; does not affect membrane sorting, does not affect pH homeostasis in recycling endosomes, does not affect cargo trafficking.|||Does not affect post-translational maturation; does not affect membrane sorting; does not affect pH homeostasis in recycling endosomes; does not affect cargo trafficking.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MRXSCH; decreases protein stability; increased ubiquitination; impairs acidification of endosomes; reduces localization to recycling endosomes; impairs trafficking to plasma membrane; reduces uptake of recycling endosomal cargo.|||In MRXSCH; reduces oligosaccharide maturation; decreases protein stability; partially accumulated in the ER; impairs acidification of endosomes; reduces localization to recycling endosomes; impairs trafficking to plasma membrane; reduces uptake of recycling endosomal cargo.|||In MRXSCH; reduces oligosaccharide maturation; largely retained in the ER; strongly reduces localization to recycling endosomes; strongly impairs trafficking to plasma membrane; strongly reduces uptake of recycling endosomal cargo.|||In isoform 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sodium/hydrogen exchanger 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052362|||http://purl.uniprot.org/annotation/VAR_083536|||http://purl.uniprot.org/annotation/VAR_087516|||http://purl.uniprot.org/annotation/VAR_087517|||http://purl.uniprot.org/annotation/VAR_087518|||http://purl.uniprot.org/annotation/VAR_087519|||http://purl.uniprot.org/annotation/VAR_087520|||http://purl.uniprot.org/annotation/VAR_087521|||http://purl.uniprot.org/annotation/VSP_044868|||http://purl.uniprot.org/annotation/VSP_061774
http://togogenome.org/gene/9606:RUNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01196                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form AML1-EAP in T-MDS and CML, to form type II MACROD1-RUNX1 fusion protein and to form RUNX1-CBFA2T2 in acute myeloid leukemia|||Breakpoint for translocation to form AML1-EMV-1 (or AML1-EAP) in CML and T-MDS, to form AML1-MTG8 (ETO) in AML-M2, to form AML1-CBFA2T3 in therapy-related myeloid malignancies, to form AML1-MECOM in CML and to form type I MACROD1-RUNX1 fusion protein|||Disordered|||Disrupts AML1-MTG8/ETODNA-binding, decreases AML1-MTG8/ETO transforming activity.|||Disrupts interaction of AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity.|||In FPDMM.|||In FPDMM; impaired phosphorylation.|||In isoform AML-1A.|||In isoform AML-1C.|||In isoform AML-1E.|||In isoform AML-1FA.|||In isoform AML-1FB.|||In isoform AML-1FC.|||In isoform AML-1G.|||In isoform AML-1H.|||In isoform AML-1I.|||In isoform AML-1L.|||Interaction with DNA|||Interaction with FOXP3|||Interaction with KAT6A|||Interaction with KAT6B|||Loss of heterodimerization and impaired phosphorylation.|||Loss of heterodimerization and reduced EP300 phosphorylation induction.|||Loss of heterodimerization. Disrupts interactionof AML1-MTG8/ETO with CBFB, no effect on AML1-MTG8/ETO-mediated transformation activity.|||N6-acetyllysine|||No DNA-binding.|||No effect on DNA binding.|||Phosphoserine|||Phosphoserine; by HIPK2|||Phosphothreonine|||Phosphothreonine; by HIPK2|||Polar residues|||Reduced phosphorylation.|||Reduced phosphorylation; when associated with A-273.|||Reduced phosphorylation; when associated with A-276.|||Reduces DNA-binding.|||Runt|||Runt-related transcription factor 1|||Strongly reduces DNA-binding, impaired phosphorylation and reduced EP300 phosphorylation induction.|||Strongly reduces DNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174655|||http://purl.uniprot.org/annotation/VAR_012128|||http://purl.uniprot.org/annotation/VAR_012129|||http://purl.uniprot.org/annotation/VAR_013177|||http://purl.uniprot.org/annotation/VAR_013178|||http://purl.uniprot.org/annotation/VSP_005916|||http://purl.uniprot.org/annotation/VSP_005917|||http://purl.uniprot.org/annotation/VSP_005918|||http://purl.uniprot.org/annotation/VSP_005919|||http://purl.uniprot.org/annotation/VSP_005920|||http://purl.uniprot.org/annotation/VSP_005921|||http://purl.uniprot.org/annotation/VSP_005922|||http://purl.uniprot.org/annotation/VSP_005923|||http://purl.uniprot.org/annotation/VSP_005924|||http://purl.uniprot.org/annotation/VSP_005925|||http://purl.uniprot.org/annotation/VSP_005926|||http://purl.uniprot.org/annotation/VSP_005927|||http://purl.uniprot.org/annotation/VSP_005928|||http://purl.uniprot.org/annotation/VSP_005929
http://togogenome.org/gene/9606:AHNAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||PDZ|||Phosphoserine|||Polar residues|||Protein AHNAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319962|||http://purl.uniprot.org/annotation/VAR_039069|||http://purl.uniprot.org/annotation/VAR_039070|||http://purl.uniprot.org/annotation/VAR_039071|||http://purl.uniprot.org/annotation/VAR_039072|||http://purl.uniprot.org/annotation/VAR_039073|||http://purl.uniprot.org/annotation/VAR_039074|||http://purl.uniprot.org/annotation/VAR_039075|||http://purl.uniprot.org/annotation/VAR_039076|||http://purl.uniprot.org/annotation/VAR_050635|||http://purl.uniprot.org/annotation/VAR_050636|||http://purl.uniprot.org/annotation/VAR_050637|||http://purl.uniprot.org/annotation/VAR_050638|||http://purl.uniprot.org/annotation/VAR_050639|||http://purl.uniprot.org/annotation/VAR_050640|||http://purl.uniprot.org/annotation/VAR_050641|||http://purl.uniprot.org/annotation/VAR_050642|||http://purl.uniprot.org/annotation/VAR_050643|||http://purl.uniprot.org/annotation/VAR_050644|||http://purl.uniprot.org/annotation/VAR_050645|||http://purl.uniprot.org/annotation/VAR_050646|||http://purl.uniprot.org/annotation/VAR_050647|||http://purl.uniprot.org/annotation/VAR_050648|||http://purl.uniprot.org/annotation/VAR_050649|||http://purl.uniprot.org/annotation/VAR_059560|||http://purl.uniprot.org/annotation/VAR_059561|||http://purl.uniprot.org/annotation/VAR_059562|||http://purl.uniprot.org/annotation/VAR_059563|||http://purl.uniprot.org/annotation/VAR_059564|||http://purl.uniprot.org/annotation/VAR_059565|||http://purl.uniprot.org/annotation/VAR_059566|||http://purl.uniprot.org/annotation/VAR_059567|||http://purl.uniprot.org/annotation/VAR_059568|||http://purl.uniprot.org/annotation/VAR_059569|||http://purl.uniprot.org/annotation/VAR_059570|||http://purl.uniprot.org/annotation/VAR_059571|||http://purl.uniprot.org/annotation/VAR_059572|||http://purl.uniprot.org/annotation/VAR_059573|||http://purl.uniprot.org/annotation/VAR_059574|||http://purl.uniprot.org/annotation/VAR_061548|||http://purl.uniprot.org/annotation/VAR_061549|||http://purl.uniprot.org/annotation/VAR_061550|||http://purl.uniprot.org/annotation/VSP_031550|||http://purl.uniprot.org/annotation/VSP_031551
http://togogenome.org/gene/9606:OR6M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK2|||http://purl.uniprot.org/uniprot/Q8NGM8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150632|||http://purl.uniprot.org/annotation/VAR_053222
http://togogenome.org/gene/9606:NTN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTR8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||N-linked (GlcNAc...) asparagine|||NTR|||Netrin-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320575|||http://purl.uniprot.org/annotation/VSP_031667|||http://purl.uniprot.org/annotation/VSP_031668
http://togogenome.org/gene/9606:PCLO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6V0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  10 X 10 AA tandem approximate repeats of P-A-K-P-Q-P-Q-Q-P-X|||Basic and acidic residues|||C2 1|||C2 2|||C4-type|||Disordered|||In isoform 3 and isoform 6.|||In isoform 3.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein piccolo                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058250|||http://purl.uniprot.org/annotation/VAR_056959|||http://purl.uniprot.org/annotation/VAR_056960|||http://purl.uniprot.org/annotation/VSP_059461|||http://purl.uniprot.org/annotation/VSP_059462|||http://purl.uniprot.org/annotation/VSP_059463|||http://purl.uniprot.org/annotation/VSP_059464|||http://purl.uniprot.org/annotation/VSP_059465
http://togogenome.org/gene/9606:DDT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30046                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  D-dopachrome decarboxylase|||In isoform 2.|||Loss of enzyme activity.|||N-acetylproline|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158070|||http://purl.uniprot.org/annotation/VSP_056953
http://togogenome.org/gene/9606:VSTM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W8J5|||http://purl.uniprot.org/uniprot/Q8TAG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Ig-like|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||V-set and transmembrane domain-containing protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014775|||http://purl.uniprot.org/annotation/PRO_5003379416|||http://purl.uniprot.org/annotation/VAR_047034|||http://purl.uniprot.org/annotation/VSP_039817
http://togogenome.org/gene/9606:ATXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS38|||http://purl.uniprot.org/uniprot/C9JQV6|||http://purl.uniprot.org/uniprot/P54252                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Ataxin-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In short isoform 1, due to a stop-gain single nucleotide variant, has reduced half-life due to increased proteasomal degradation, has reduced solubility and increased tendency to form aggregates, increased localization to the nucleus.|||Inhibits substrate trapping.|||Josephin|||Loss of deubiquitination activity.|||No effect on ubiquitination.|||Nucleophile|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Polar residues|||Proton acceptor|||UIM 1|||UIM 2|||UIM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053831|||http://purl.uniprot.org/annotation/VAR_013688|||http://purl.uniprot.org/annotation/VAR_013689|||http://purl.uniprot.org/annotation/VAR_082841|||http://purl.uniprot.org/annotation/VSP_002783|||http://purl.uniprot.org/annotation/VSP_002784|||http://purl.uniprot.org/annotation/VSP_047085|||http://purl.uniprot.org/annotation/VSP_047086
http://togogenome.org/gene/9606:PGM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G03                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Phosphopentomutase|||Phosphoserine|||Phosphoserine intermediate|||Removed|||via phosphate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147781|||http://purl.uniprot.org/annotation/VAR_027968|||http://purl.uniprot.org/annotation/VAR_027969|||http://purl.uniprot.org/annotation/VSP_056221|||http://purl.uniprot.org/annotation/VSP_056222|||http://purl.uniprot.org/annotation/VSP_056223|||http://purl.uniprot.org/annotation/VSP_056224
http://togogenome.org/gene/9606:WDFY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P53                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  FYVE-type|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat and FYVE domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051336
http://togogenome.org/gene/9606:PGBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3X8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PiggyBac transposable element-derived protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288053|||http://purl.uniprot.org/annotation/VSP_025631
http://togogenome.org/gene/9606:ZNF687                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1G0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In PDB6; enhances nuclear localization; increases expression levels; R-937 containing osteoclasts induced by treatment of peripheral blood mononuclear cells with CSF1 and TNFSF11 exhibit a greater number of nuclei, as well as a larger surface area than did those from the control individuals.|||In PDB6; unknown pathological significance.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger protein 687                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234005|||http://purl.uniprot.org/annotation/VAR_052894|||http://purl.uniprot.org/annotation/VAR_052895|||http://purl.uniprot.org/annotation/VAR_076534|||http://purl.uniprot.org/annotation/VAR_076535|||http://purl.uniprot.org/annotation/VSP_018168|||http://purl.uniprot.org/annotation/VSP_018169
http://togogenome.org/gene/9606:UBE2E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z306|||http://purl.uniprot.org/uniprot/P51965                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Polar residues|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082470|||http://purl.uniprot.org/annotation/VAR_061868|||http://purl.uniprot.org/annotation/VSP_045884|||http://purl.uniprot.org/annotation/VSP_047200
http://togogenome.org/gene/9606:NRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRM2|||http://purl.uniprot.org/uniprot/Q86VF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||LIM zinc-binding|||Nebulin 1|||Nebulin 10|||Nebulin 11|||Nebulin 12|||Nebulin 13|||Nebulin 14|||Nebulin 15|||Nebulin 16|||Nebulin 17|||Nebulin 18|||Nebulin 19|||Nebulin 2|||Nebulin 20|||Nebulin 21|||Nebulin 22|||Nebulin 23|||Nebulin 24|||Nebulin 25|||Nebulin 26|||Nebulin 27|||Nebulin 28|||Nebulin 29|||Nebulin 3|||Nebulin 30|||Nebulin 31|||Nebulin 32|||Nebulin 33|||Nebulin 34|||Nebulin 35|||Nebulin 36|||Nebulin 37|||Nebulin 38|||Nebulin 39|||Nebulin 4|||Nebulin 40|||Nebulin 41|||Nebulin 42|||Nebulin 43|||Nebulin 44|||Nebulin 5|||Nebulin 6|||Nebulin 7|||Nebulin 8|||Nebulin 9|||Nebulin-related-anchoring protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250425|||http://purl.uniprot.org/annotation/VAR_027556|||http://purl.uniprot.org/annotation/VAR_027557|||http://purl.uniprot.org/annotation/VAR_027558|||http://purl.uniprot.org/annotation/VAR_027559|||http://purl.uniprot.org/annotation/VAR_027560|||http://purl.uniprot.org/annotation/VAR_034073|||http://purl.uniprot.org/annotation/VAR_034074|||http://purl.uniprot.org/annotation/VAR_034075|||http://purl.uniprot.org/annotation/VAR_034076|||http://purl.uniprot.org/annotation/VAR_034077|||http://purl.uniprot.org/annotation/VAR_034078|||http://purl.uniprot.org/annotation/VAR_034079|||http://purl.uniprot.org/annotation/VAR_034080|||http://purl.uniprot.org/annotation/VAR_050160|||http://purl.uniprot.org/annotation/VAR_050161|||http://purl.uniprot.org/annotation/VAR_050162|||http://purl.uniprot.org/annotation/VAR_050163|||http://purl.uniprot.org/annotation/VAR_050164|||http://purl.uniprot.org/annotation/VAR_050165|||http://purl.uniprot.org/annotation/VAR_061357|||http://purl.uniprot.org/annotation/VSP_052165|||http://purl.uniprot.org/annotation/VSP_052166
http://togogenome.org/gene/9606:SLC23A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK48|||http://purl.uniprot.org/uniprot/Q9UGH3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Solute carrier family 23 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165978|||http://purl.uniprot.org/annotation/VSP_056485
http://togogenome.org/gene/9606:MIPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99797                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  In COXPD31.|||In COXPD31; unknown pathological significance.|||Mitochondrial intermediate peptidase|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028579|||http://purl.uniprot.org/annotation/VAR_038934|||http://purl.uniprot.org/annotation/VAR_038935|||http://purl.uniprot.org/annotation/VAR_038936|||http://purl.uniprot.org/annotation/VAR_038937|||http://purl.uniprot.org/annotation/VAR_078009|||http://purl.uniprot.org/annotation/VAR_078010|||http://purl.uniprot.org/annotation/VAR_078011|||http://purl.uniprot.org/annotation/VAR_078012|||http://purl.uniprot.org/annotation/VAR_078013
http://togogenome.org/gene/9606:THAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVV9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes DNA- and zinc-binding.|||Does not affect DNA-binding.|||HCFC1-binding motif (HBM)|||In DYT6.|||In DYT6; affects DNA-binding.|||In DYT6; lower activity than wild-type.|||In DYT6; mild phenotype; does not affect activity.|||In DYT6; no effect on dimerization.|||In isoform 2.|||Involved in homodimer formation|||Partially affects DNA-binding.|||Strongly affects DNA-binding.|||THAP domain-containing protein 1|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068637|||http://purl.uniprot.org/annotation/VAR_054788|||http://purl.uniprot.org/annotation/VAR_065880|||http://purl.uniprot.org/annotation/VAR_065881|||http://purl.uniprot.org/annotation/VAR_065882|||http://purl.uniprot.org/annotation/VAR_065883|||http://purl.uniprot.org/annotation/VAR_065884|||http://purl.uniprot.org/annotation/VAR_065885|||http://purl.uniprot.org/annotation/VAR_065886|||http://purl.uniprot.org/annotation/VAR_065887|||http://purl.uniprot.org/annotation/VAR_066677|||http://purl.uniprot.org/annotation/VAR_066678|||http://purl.uniprot.org/annotation/VAR_066679|||http://purl.uniprot.org/annotation/VAR_066680|||http://purl.uniprot.org/annotation/VAR_066681|||http://purl.uniprot.org/annotation/VAR_066682|||http://purl.uniprot.org/annotation/VAR_066683|||http://purl.uniprot.org/annotation/VAR_066684|||http://purl.uniprot.org/annotation/VAR_066685|||http://purl.uniprot.org/annotation/VAR_066686|||http://purl.uniprot.org/annotation/VAR_066687|||http://purl.uniprot.org/annotation/VAR_066688|||http://purl.uniprot.org/annotation/VAR_066689|||http://purl.uniprot.org/annotation/VAR_066690|||http://purl.uniprot.org/annotation/VAR_066691|||http://purl.uniprot.org/annotation/VAR_066692|||http://purl.uniprot.org/annotation/VAR_066693|||http://purl.uniprot.org/annotation/VAR_066694|||http://purl.uniprot.org/annotation/VAR_066695|||http://purl.uniprot.org/annotation/VAR_066696|||http://purl.uniprot.org/annotation/VAR_066697|||http://purl.uniprot.org/annotation/VAR_066698|||http://purl.uniprot.org/annotation/VAR_066699|||http://purl.uniprot.org/annotation/VAR_066700|||http://purl.uniprot.org/annotation/VAR_066701|||http://purl.uniprot.org/annotation/VAR_066702|||http://purl.uniprot.org/annotation/VAR_066703|||http://purl.uniprot.org/annotation/VAR_066704|||http://purl.uniprot.org/annotation/VAR_066705|||http://purl.uniprot.org/annotation/VAR_066706|||http://purl.uniprot.org/annotation/VAR_066707|||http://purl.uniprot.org/annotation/VAR_066708|||http://purl.uniprot.org/annotation/VAR_066709|||http://purl.uniprot.org/annotation/VAR_067356|||http://purl.uniprot.org/annotation/VAR_067357|||http://purl.uniprot.org/annotation/VAR_072272|||http://purl.uniprot.org/annotation/VAR_079366|||http://purl.uniprot.org/annotation/VSP_044665|||http://purl.uniprot.org/annotation/VSP_044666
http://togogenome.org/gene/9606:STARD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQZ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Cleavage; by PARL|||Disordered|||Mitochondrion|||Polar residues|||START|||StAR-related lipid transfer protein 7, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220674|||http://purl.uniprot.org/annotation/VAR_020345
http://togogenome.org/gene/9606:CSH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0M6L0F6|||http://purl.uniprot.org/uniprot/A6NIT4|||http://purl.uniprot.org/uniprot/B1A4H9|||http://purl.uniprot.org/uniprot/P0DML3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chorionic somatomammotropin hormone 2|||In isoform 2.|||In isoform 3.|||In monomeric form|||Interchain (with C-208); in dimeric form|||Interchain (with C-215); in dimeric form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000429797|||http://purl.uniprot.org/annotation/PRO_5002698939|||http://purl.uniprot.org/annotation/PRO_5002761478|||http://purl.uniprot.org/annotation/PRO_5005806161|||http://purl.uniprot.org/annotation/VAR_007167|||http://purl.uniprot.org/annotation/VSP_055244|||http://purl.uniprot.org/annotation/VSP_055245
http://togogenome.org/gene/9606:ANKLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A499FJM0|||http://purl.uniprot.org/uniprot/B4DSY8|||http://purl.uniprot.org/uniprot/B4E124|||http://purl.uniprot.org/uniprot/Q8NAG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat and LEM domain-containing protein 1|||Disordered|||GIY-YIG|||In isoform 2.|||Increased nuclear localization.|||LEM|||Loss of endonucleolytic activity.|||Nuclear export signal|||Nuclear localization signal|||Polar residues|||Probable loss of endonucleolytic activity. Fails to induce DNA damage response upon leptomycin-mediated nuclear localization. No nuclear translocation upon treatment with DNA damaging agents. Steady state cytoplasmic localization is not affected.|||Slight increase in nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244370|||http://purl.uniprot.org/annotation/VAR_033507|||http://purl.uniprot.org/annotation/VAR_033508|||http://purl.uniprot.org/annotation/VAR_033509|||http://purl.uniprot.org/annotation/VAR_033510|||http://purl.uniprot.org/annotation/VAR_033511|||http://purl.uniprot.org/annotation/VAR_061015|||http://purl.uniprot.org/annotation/VAR_063681|||http://purl.uniprot.org/annotation/VAR_063682|||http://purl.uniprot.org/annotation/VSP_039879|||http://purl.uniprot.org/annotation/VSP_039880
http://togogenome.org/gene/9606:CCDC103                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW40                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 103|||In CILD17; unknown pathological significance; hypomorphic variant; reduced cilia beat amplitude in homozygous nasal respiratory cells; does not fully rescue abnormal phenotype in a zebrafish animal model.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263636|||http://purl.uniprot.org/annotation/VAR_068449|||http://purl.uniprot.org/annotation/VSP_046037|||http://purl.uniprot.org/annotation/VSP_046038
http://togogenome.org/gene/9606:SRRM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MD48|||http://purl.uniprot.org/uniprot/V5T9A0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Serine/arginine repetitive matrix protein 4|||Serine/arginine repetitive matrix protein C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311911|||http://purl.uniprot.org/annotation/VAR_037339|||http://purl.uniprot.org/annotation/VAR_037340|||http://purl.uniprot.org/annotation/VAR_037341
http://togogenome.org/gene/9606:CD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06126                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||N-linked (GlcNAc...) asparagine|||T-cell surface glycoprotein CD1a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014578|||http://purl.uniprot.org/annotation/VAR_010209|||http://purl.uniprot.org/annotation/VAR_010210|||http://purl.uniprot.org/annotation/VAR_062522
http://togogenome.org/gene/9606:LRRC32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14392                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes Cell surface localization without affecting interaction with Latency-associated peptide (LAP) of TGFB1.|||Abolishes interaction with Latency-associated peptide (LAP) of TGFB1; when associated with A-211.|||Abolishes interaction with Latency-associated peptide (LAP) of TGFB1; when associated with A-350.|||Cytoplasmic|||Extracellular|||Helical|||In CPPRDD.|||Interchain (with C-33 in TGFB1); in linked form|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Transforming growth factor beta activator LRRC32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021615|||http://purl.uniprot.org/annotation/VAR_051113|||http://purl.uniprot.org/annotation/VAR_051114|||http://purl.uniprot.org/annotation/VAR_085139
http://togogenome.org/gene/9606:ST8SIA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61647                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-2,8-sialyltransferase 8F|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149299
http://togogenome.org/gene/9606:PTPN13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12923                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KIND|||Loss of catalytic activity.|||No effect on substrate affinity.|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Reduces substrate affinity 2 fold.|||Reduces substrate affinity 7 fold.|||Strongly decreases catalytic activity.|||Substrate|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219435|||http://purl.uniprot.org/annotation/VAR_016200|||http://purl.uniprot.org/annotation/VAR_016201|||http://purl.uniprot.org/annotation/VAR_024373|||http://purl.uniprot.org/annotation/VAR_024374|||http://purl.uniprot.org/annotation/VAR_048359|||http://purl.uniprot.org/annotation/VAR_048360|||http://purl.uniprot.org/annotation/VAR_048361|||http://purl.uniprot.org/annotation/VSP_000496|||http://purl.uniprot.org/annotation/VSP_000497|||http://purl.uniprot.org/annotation/VSP_007921
http://togogenome.org/gene/9606:DOCK11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 11|||Disordered|||Found in a patient with autoimmune manifestations; unknown pathological significance.|||Found in a patient with autoimmune manifestations; unknown pathological significance; decreased CDC42 activation in patient platelets.|||Found in a patient with autoimmune manifestations; unknown pathological significance; decreased expression in patient platelets and activated T-cells; decreased CDC42 activation in patient platelets.|||Found in a patient with autoimmune manifestations; unknown pathological significance; decreased expression in patient platelets and activated T-cells; impaired CDC42 activation in patient platelets.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299558|||http://purl.uniprot.org/annotation/VAR_034854|||http://purl.uniprot.org/annotation/VAR_088240|||http://purl.uniprot.org/annotation/VAR_088241|||http://purl.uniprot.org/annotation/VAR_088242|||http://purl.uniprot.org/annotation/VAR_088243|||http://purl.uniprot.org/annotation/VAR_088244|||http://purl.uniprot.org/annotation/VAR_088245|||http://purl.uniprot.org/annotation/VAR_088246
http://togogenome.org/gene/9606:FRAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92837                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Involved in GSK-3 binding|||Phosphoserine|||Proto-oncogene FRAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087332
http://togogenome.org/gene/9606:CHST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCG5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085193|||http://purl.uniprot.org/annotation/VAR_052528
http://togogenome.org/gene/9606:TMCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V207|||http://purl.uniprot.org/uniprot/Q9ULS5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Polar residues|||Transmembrane and coiled-coil domain protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184599|||http://purl.uniprot.org/annotation/VAR_063144|||http://purl.uniprot.org/annotation/VAR_063145
http://togogenome.org/gene/9606:RPL41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62945                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix|||Region                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein eL41                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198055
http://togogenome.org/gene/9606:ZSCAN29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BJ4|||http://purl.uniprot.org/uniprot/Q8IWY8|||http://purl.uniprot.org/uniprot/Q96AG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Myb/SANT-like DNA-binding|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234011|||http://purl.uniprot.org/annotation/VAR_057459|||http://purl.uniprot.org/annotation/VAR_059949|||http://purl.uniprot.org/annotation/VSP_018179|||http://purl.uniprot.org/annotation/VSP_018180|||http://purl.uniprot.org/annotation/VSP_018181|||http://purl.uniprot.org/annotation/VSP_018182
http://togogenome.org/gene/9606:GTF2IRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GTF2I-like 1|||GTF2I-like 2|||General transcription factor II-I repeat domain-containing protein 2A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320120|||http://purl.uniprot.org/annotation/VAR_039127|||http://purl.uniprot.org/annotation/VSP_031597|||http://purl.uniprot.org/annotation/VSP_031598|||http://purl.uniprot.org/annotation/VSP_031599|||http://purl.uniprot.org/annotation/VSP_031600|||http://purl.uniprot.org/annotation/VSP_031601|||http://purl.uniprot.org/annotation/VSP_031602|||http://purl.uniprot.org/annotation/VSP_031603|||http://purl.uniprot.org/annotation/VSP_031604
http://togogenome.org/gene/9606:CYP51A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16850                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Lanosterol 14-alpha demethylase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051998|||http://purl.uniprot.org/annotation/VAR_023470|||http://purl.uniprot.org/annotation/VSP_037413
http://togogenome.org/gene/9606:OR52M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGK5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 52M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150785|||http://purl.uniprot.org/annotation/VAR_034349|||http://purl.uniprot.org/annotation/VAR_034350
http://togogenome.org/gene/9606:CIMIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1P6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Ciliary microtubule inner protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079448|||http://purl.uniprot.org/annotation/VAR_033759|||http://purl.uniprot.org/annotation/VAR_033760|||http://purl.uniprot.org/annotation/VAR_061632
http://togogenome.org/gene/9606:PGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06401                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AF1; mediates transcriptional activation|||AF2; mediates transcriptional activation|||AF3; mediates transcriptional activation (in isoform B)|||Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin.|||Decreases protein stability and increases progesterone-induced transcriptional activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Great loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform A.|||LXXL motif 1|||LXXL motif 2|||Mediates transcriptional transrepression (in isoform A)|||Modulating, Pro-Rich|||NR C4-type|||NR LBD|||No change in progestin-induced protein degradation; when associated with A-344. No change in sumoylation; when associated with A-294 and A-344.|||No effect on interaction with CUEDC2. Impaired progesterone-induced transcriptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation; when associated with A-344 and A-345.|||No interaction with SP1. No change in progestin-induced protein degradation; when associated with A-345. No change in sumoylation; when associated with A-294 and A-345.|||Nuclear localization signal|||Nuclear receptor|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by MAPK|||Phosphoserine; by MAPK1|||Polar residues|||Pro residues|||Progesterone receptor|||Reduces transcriptional activation.|||Reduces transcriptional activation; when associated with A-115 and A-118.|||Reduces transcriptional activation; when associated with A-115 and A-119.|||Reduces transcriptional activation; when associated with A-118 and A-119.|||Reduces transcriptional activation; when associated with A-55 and A-58.|||Reduces transcriptional activation; when associated with A-55 and A-59.|||Reduces transcriptional activation; when associated with A-58 and A-59.|||Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531.|||Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053693|||http://purl.uniprot.org/annotation/VAR_014627|||http://purl.uniprot.org/annotation/VAR_014628|||http://purl.uniprot.org/annotation/VAR_016117|||http://purl.uniprot.org/annotation/VAR_016118|||http://purl.uniprot.org/annotation/VAR_019221|||http://purl.uniprot.org/annotation/VAR_019222|||http://purl.uniprot.org/annotation/VAR_019223|||http://purl.uniprot.org/annotation/VAR_019224|||http://purl.uniprot.org/annotation/VAR_019225|||http://purl.uniprot.org/annotation/VAR_019226|||http://purl.uniprot.org/annotation/VAR_019227|||http://purl.uniprot.org/annotation/VAR_019228|||http://purl.uniprot.org/annotation/VAR_025555|||http://purl.uniprot.org/annotation/VSP_003706|||http://purl.uniprot.org/annotation/VSP_046942|||http://purl.uniprot.org/annotation/VSP_047454|||http://purl.uniprot.org/annotation/VSP_047455|||http://purl.uniprot.org/annotation/VSP_053543
http://togogenome.org/gene/9606:PANK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H999                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Increases affinity for ATP and decreases affinity for acetyl-CoA. Increases acetyl-CoA production.|||Loss of catalytic activity but can bind ATP normally.|||Loss of catalytic activity.|||Pantothenate kinase 3|||Prevents acetyl-CoA production.|||Proton acceptor|||Retains 30% of wild-type activity. Refractory to inhibition by acetyl-CoA. Exhibits a 10-fold increase in the Km for pantothenate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161804
http://togogenome.org/gene/9606:MAPKAPK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW41                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Induces constitutive protein kinase activity.|||Kinase defective mutant, abolishes activity.|||MAP kinase-activated protein kinase 5|||Mimicks phosphorylation state and displays a slightly higher protein kinase activity.|||Mimicks phosphorylation state and induces constitutive protein kinase activity.|||No p38-beta/MAPK11-induced activation.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine; by MAPK11, MAPK14, MAPK4, MAPK6 and PKA|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086296|||http://purl.uniprot.org/annotation/VAR_040758|||http://purl.uniprot.org/annotation/VAR_040759|||http://purl.uniprot.org/annotation/VSP_011597
http://togogenome.org/gene/9606:DAPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNJ3|||http://purl.uniprot.org/uniprot/O43293                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation segment|||Cytoplasmic localization.|||Death-associated protein kinase 3|||Greatly reduced kinase activity.|||In a colorectal adenocarcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival.|||In a lung neuroendocrine carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation, cell adhesion and cell survival.|||In an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival.|||In isoform 2.|||Leucine-zipper|||Loss of kinase activity at low concentrations of ATP.|||Loss of kinase activity.|||Loss of phosphorylation by ROCK1, catalytically inactive.|||Loss of phosphorylation by ROCK1.|||Phosphoserine; by DAPK1|||Phosphoserine; by autocatalysis|||Phosphoserine; by autocatalysis and DAPK1|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphothreonine; by autocatalysis and ROCK1|||Phosphothreonine; by autocatalysis, DAPK1 and ROCK1|||Predominantly cytoplasmic localization; phosphomimetic.|||Predominantly nuclear localization.|||Predominantly nuclear localization; when associated with A-427 and A-434.|||Predominantly nuclear localization; when associated with A-427 and A-441.|||Predominantly nuclear localization; when associated with A-434 and A-441.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085914|||http://purl.uniprot.org/annotation/VAR_040438|||http://purl.uniprot.org/annotation/VAR_040439|||http://purl.uniprot.org/annotation/VAR_040440|||http://purl.uniprot.org/annotation/VSP_042059|||http://purl.uniprot.org/annotation/VSP_042060
http://togogenome.org/gene/9606:VAPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95292|||http://purl.uniprot.org/uniprot/Q53XM7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect interaction with the conventional FFAT motif of OSBPL1A. Impairs the interactions of the MSP domain with the phosphorylated FFAT motif of STARD3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||Helical; Anchor for type IV membrane protein|||In ALS8 and SMAPAD; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway; affects interaction with RMDN3; affects cellular calcium homeostasis; induces mislocalization to the non-ER compartments; enhances homodimerization.|||In ALS8; it forms insoluble cytosolic aggregates; cannot activate the UPR pathway through ERN1/IRE1 induction; results in ubiquitinated aggregates accumulation and cell death.|||In isoform 2.|||Involved in binding the phosphorylated serine of the phospho-FFAT motif|||MSP|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Prevents binding to the FFAT motif in target proteins; when associated with D-87.|||Prevents binding to the FFAT motif in target proteins; when associated with D-89.|||Removed|||Vesicle-associated membrane protein-associated protein B/C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213473|||http://purl.uniprot.org/annotation/VAR_026743|||http://purl.uniprot.org/annotation/VAR_067964|||http://purl.uniprot.org/annotation/VSP_003277|||http://purl.uniprot.org/annotation/VSP_003278
http://togogenome.org/gene/9606:ATN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54259|||http://purl.uniprot.org/uniprot/Q86V38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Asymmetric dimethylarginine|||Atrophin-1|||Basic and acidic residues|||Cleavage; by CASP-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HX repeat|||In CHEDDA.|||In CHEDDA; the mutation resulted in a perturbation of the structural and functional integrity of the HX repeat; altered zinc-binding properties of the HX repeat.|||In CHEDDA; unknown pathological significance.|||Involved in binding BAIAP2|||N6-acetyllysine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine|||Polar residues|||Prevents cleavage and suppresses apoptosis.|||Pro residues|||Required for interaction with FAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064730|||http://purl.uniprot.org/annotation/VAR_030937|||http://purl.uniprot.org/annotation/VAR_064038|||http://purl.uniprot.org/annotation/VAR_083058|||http://purl.uniprot.org/annotation/VAR_083059|||http://purl.uniprot.org/annotation/VAR_083060|||http://purl.uniprot.org/annotation/VAR_083061|||http://purl.uniprot.org/annotation/VAR_083062|||http://purl.uniprot.org/annotation/VAR_083063|||http://purl.uniprot.org/annotation/VAR_083064|||http://purl.uniprot.org/annotation/VAR_083065
http://togogenome.org/gene/9606:SLFN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E128|||http://purl.uniprot.org/uniprot/Q08AF3                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Schlafen AlbA-2|||Schlafen family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282982|||http://purl.uniprot.org/annotation/VAR_031445|||http://purl.uniprot.org/annotation/VAR_031446|||http://purl.uniprot.org/annotation/VAR_053876|||http://purl.uniprot.org/annotation/VSP_024271|||http://purl.uniprot.org/annotation/VSP_024272
http://togogenome.org/gene/9606:PKIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C010                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Important for inhibition|||In isoform 2.|||cAMP-dependent protein kinase inhibitor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154538|||http://purl.uniprot.org/annotation/VSP_046922
http://togogenome.org/gene/9606:ELAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5M8|||http://purl.uniprot.org/uniprot/Q9BQ52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In COXPD17.|||In HPC2.|||In HPC2; does not affect the enzymatic activity.|||In HPC2; higher frequency in prostate cancer cases.|||In HPC2; risk factor for disease development; does not affect the enzymatic activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Metallo-beta-lactamase|||Mitochondrion|||Phosphoserine|||Zinc phosphodiesterase ELAC protein 2|||tRNase Z endonuclease                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155828|||http://purl.uniprot.org/annotation/VAR_017425|||http://purl.uniprot.org/annotation/VAR_017426|||http://purl.uniprot.org/annotation/VAR_017427|||http://purl.uniprot.org/annotation/VAR_017428|||http://purl.uniprot.org/annotation/VAR_017429|||http://purl.uniprot.org/annotation/VAR_017430|||http://purl.uniprot.org/annotation/VAR_017431|||http://purl.uniprot.org/annotation/VAR_017432|||http://purl.uniprot.org/annotation/VAR_038210|||http://purl.uniprot.org/annotation/VAR_038211|||http://purl.uniprot.org/annotation/VAR_070844|||http://purl.uniprot.org/annotation/VAR_070845|||http://purl.uniprot.org/annotation/VAR_070846|||http://purl.uniprot.org/annotation/VSP_009168|||http://purl.uniprot.org/annotation/VSP_009169|||http://purl.uniprot.org/annotation/VSP_009170|||http://purl.uniprot.org/annotation/VSP_009171|||http://purl.uniprot.org/annotation/VSP_009172|||http://purl.uniprot.org/annotation/VSP_043449
http://togogenome.org/gene/9606:ZNF540                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDQ6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 4.|||KRAB|||Zinc finger protein 540                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047641|||http://purl.uniprot.org/annotation/VAR_033575|||http://purl.uniprot.org/annotation/VAR_035586|||http://purl.uniprot.org/annotation/VAR_069366|||http://purl.uniprot.org/annotation/VSP_016036|||http://purl.uniprot.org/annotation/VSP_016037
http://togogenome.org/gene/9606:CALML4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GE6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-like protein 4|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314933|||http://purl.uniprot.org/annotation/VAR_048586|||http://purl.uniprot.org/annotation/VAR_048587|||http://purl.uniprot.org/annotation/VSP_030435|||http://purl.uniprot.org/annotation/VSP_030436|||http://purl.uniprot.org/annotation/VSP_047150|||http://purl.uniprot.org/annotation/VSP_055513|||http://purl.uniprot.org/annotation/VSP_055514
http://togogenome.org/gene/9606:CHSY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X52                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate synthase 1|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In TPBS.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189558|||http://purl.uniprot.org/annotation/VAR_021173|||http://purl.uniprot.org/annotation/VAR_028009|||http://purl.uniprot.org/annotation/VAR_065821|||http://purl.uniprot.org/annotation/VAR_065822
http://togogenome.org/gene/9606:NANOGNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5D8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||NANOG neighbor homeobox|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341417
http://togogenome.org/gene/9606:HTR3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6WC43|||http://purl.uniprot.org/uniprot/Q70Z44                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 3D|||Cytoplasmic|||Disordered|||Extracellular|||HA-stretch; determines single-channel conductance in 5-HT3 receptors|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312293|||http://purl.uniprot.org/annotation/VAR_037478|||http://purl.uniprot.org/annotation/VAR_037479|||http://purl.uniprot.org/annotation/VAR_037480|||http://purl.uniprot.org/annotation/VSP_029797|||http://purl.uniprot.org/annotation/VSP_029798|||http://purl.uniprot.org/annotation/VSP_029799|||http://purl.uniprot.org/annotation/VSP_029800|||http://purl.uniprot.org/annotation/VSP_029801|||http://purl.uniprot.org/annotation/VSP_044828|||http://purl.uniprot.org/annotation/VSP_044829|||http://purl.uniprot.org/annotation/VSP_044830
http://togogenome.org/gene/9606:SCNN1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5X2V1|||http://purl.uniprot.org/uniprot/P51170                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amiloride-sensitive sodium channel subunit gamma|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||In LIDLS2; increased sodium channel activity.|||In a colorectal cancer sample; somatic mutation.|||In a patient with bronchiectasis.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181276|||http://purl.uniprot.org/annotation/VAR_014893|||http://purl.uniprot.org/annotation/VAR_014894|||http://purl.uniprot.org/annotation/VAR_015842|||http://purl.uniprot.org/annotation/VAR_015843|||http://purl.uniprot.org/annotation/VAR_015844|||http://purl.uniprot.org/annotation/VAR_034485|||http://purl.uniprot.org/annotation/VAR_036483|||http://purl.uniprot.org/annotation/VAR_081180
http://togogenome.org/gene/9606:TACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EVI4|||http://purl.uniprot.org/uniprot/O75410|||http://purl.uniprot.org/uniprot/Q5HYH0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Decreases interaction with THRA.|||Disordered|||Impairs phosphorylation by AURKC.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 10.|||In isoform 7, isoform 9 and isoform 10.|||In isoform 7.|||In isoform 8.|||Interaction with CH-TOG|||Interaction with LSM7 and SNRPG|||Interaction with TDRD7|||Interaction with YEATS4|||N-acetylalanine|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by AURKC|||Phosphotyrosine|||Polar residues|||Removed|||SPAZ 1|||SPAZ 2|||Transforming acidic coiled-coil-containing protein 1|||Transforming acidic coiled-coil-containing protein C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179986|||http://purl.uniprot.org/annotation/VAR_053703|||http://purl.uniprot.org/annotation/VAR_053704|||http://purl.uniprot.org/annotation/VAR_053705|||http://purl.uniprot.org/annotation/VSP_012637|||http://purl.uniprot.org/annotation/VSP_012638|||http://purl.uniprot.org/annotation/VSP_012639|||http://purl.uniprot.org/annotation/VSP_012640|||http://purl.uniprot.org/annotation/VSP_012641|||http://purl.uniprot.org/annotation/VSP_012642|||http://purl.uniprot.org/annotation/VSP_012643|||http://purl.uniprot.org/annotation/VSP_012644|||http://purl.uniprot.org/annotation/VSP_012645|||http://purl.uniprot.org/annotation/VSP_012646|||http://purl.uniprot.org/annotation/VSP_012647|||http://purl.uniprot.org/annotation/VSP_012648
http://togogenome.org/gene/9606:RAPGEFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGK9|||http://purl.uniprot.org/uniprot/F5H2D5|||http://purl.uniprot.org/uniprot/Q9UHV5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Rap guanine nucleotide exchange factor-like 1|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349202|||http://purl.uniprot.org/annotation/VSP_035217|||http://purl.uniprot.org/annotation/VSP_035385|||http://purl.uniprot.org/annotation/VSP_035386
http://togogenome.org/gene/9606:ABR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2X0|||http://purl.uniprot.org/uniprot/B7Z683|||http://purl.uniprot.org/uniprot/B7Z7Z1|||http://purl.uniprot.org/uniprot/I3L4Y1|||http://purl.uniprot.org/uniprot/Q12979|||http://purl.uniprot.org/uniprot/Q6ZT60                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with DLG4. No effect on synaptic localization.|||Active breakpoint cluster region-related protein|||Basic and acidic residues|||C2|||DH|||Disordered|||In isoform 3.|||In isoform 4.|||In isoform Short.|||Loss of GAP activity; when associated with A-683.|||PH|||Phosphoserine|||Polar residues|||Reduces GAP activity. Loss of GAP activity; when associated with A-795.|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080902|||http://purl.uniprot.org/annotation/VAR_057186|||http://purl.uniprot.org/annotation/VSP_001815|||http://purl.uniprot.org/annotation/VSP_046029|||http://purl.uniprot.org/annotation/VSP_046030|||http://purl.uniprot.org/annotation/VSP_046148
http://togogenome.org/gene/9606:CXorf49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein CXorf49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343895
http://togogenome.org/gene/9606:IFT140                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RY7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In RP80; also found in a patient with Leber congenital amaurosis and renal failure; unknown pathological significance; decreased localization to the basal body.|||In RP80; unknown pathological significance.|||In RP80; unknown pathological significance; decreased localization to the basal body.|||In SRTD9 and RP80; unknown pathological significance; partial to complete loss of basal body localization and increase of cytoplasmic localization.|||In SRTD9.|||In SRTD9; disease phenotype consistent with Mainzer-Saldino syndrome.|||In SRTD9; impairs centrosomal localization.|||In SRTD9; partial to complete loss of basal body localization and increase of cytoplasmic localization.|||In SRTD9; partial to complete loss of basal body localization and increase of cytoplasmic localization; partial loss of function.|||In SRTD9; unknown pathological significance.|||In isoform 2.|||Intraflagellar transport protein 140 homolog|||No effect on localization to the basal body.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051046|||http://purl.uniprot.org/annotation/VAR_053396|||http://purl.uniprot.org/annotation/VAR_053397|||http://purl.uniprot.org/annotation/VAR_053398|||http://purl.uniprot.org/annotation/VAR_053399|||http://purl.uniprot.org/annotation/VAR_053400|||http://purl.uniprot.org/annotation/VAR_053401|||http://purl.uniprot.org/annotation/VAR_053402|||http://purl.uniprot.org/annotation/VAR_053403|||http://purl.uniprot.org/annotation/VAR_062098|||http://purl.uniprot.org/annotation/VAR_068523|||http://purl.uniprot.org/annotation/VAR_068524|||http://purl.uniprot.org/annotation/VAR_068525|||http://purl.uniprot.org/annotation/VAR_068526|||http://purl.uniprot.org/annotation/VAR_068527|||http://purl.uniprot.org/annotation/VAR_068528|||http://purl.uniprot.org/annotation/VAR_068529|||http://purl.uniprot.org/annotation/VAR_070999|||http://purl.uniprot.org/annotation/VAR_071000|||http://purl.uniprot.org/annotation/VAR_071001|||http://purl.uniprot.org/annotation/VAR_071002|||http://purl.uniprot.org/annotation/VAR_071003|||http://purl.uniprot.org/annotation/VAR_071004|||http://purl.uniprot.org/annotation/VAR_071005|||http://purl.uniprot.org/annotation/VAR_071006|||http://purl.uniprot.org/annotation/VAR_071007|||http://purl.uniprot.org/annotation/VAR_071008|||http://purl.uniprot.org/annotation/VAR_078817|||http://purl.uniprot.org/annotation/VAR_080667|||http://purl.uniprot.org/annotation/VAR_080668|||http://purl.uniprot.org/annotation/VAR_080669|||http://purl.uniprot.org/annotation/VAR_080670|||http://purl.uniprot.org/annotation/VAR_080671|||http://purl.uniprot.org/annotation/VAR_080672|||http://purl.uniprot.org/annotation/VAR_080673|||http://purl.uniprot.org/annotation/VAR_080674|||http://purl.uniprot.org/annotation/VAR_080675|||http://purl.uniprot.org/annotation/VAR_080676|||http://purl.uniprot.org/annotation/VAR_080677|||http://purl.uniprot.org/annotation/VAR_080678|||http://purl.uniprot.org/annotation/VAR_080679|||http://purl.uniprot.org/annotation/VAR_080680|||http://purl.uniprot.org/annotation/VAR_080681|||http://purl.uniprot.org/annotation/VAR_080682|||http://purl.uniprot.org/annotation/VAR_080683|||http://purl.uniprot.org/annotation/VSP_056392
http://togogenome.org/gene/9606:VCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSI9|||http://purl.uniprot.org/uniprot/J3KT76|||http://purl.uniprot.org/uniprot/Q969W3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Polar residues|||Protein FAM104A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236182|||http://purl.uniprot.org/annotation/VSP_039868
http://togogenome.org/gene/9606:DIMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGB1|||http://purl.uniprot.org/uniprot/A8K9K8|||http://purl.uniprot.org/uniprot/Q9UNQ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Probable dimethyladenosine transferase|||Ribosomal RNA adenine methylase transferase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101465
http://togogenome.org/gene/9606:SLMAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6C7|||http://purl.uniprot.org/uniprot/B7Z964|||http://purl.uniprot.org/uniprot/Q14BN4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FHA|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Necessary for targeting to centrosomes|||Phosphoserine|||Sarcolemmal membrane-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259662|||http://purl.uniprot.org/annotation/VSP_021499|||http://purl.uniprot.org/annotation/VSP_021500|||http://purl.uniprot.org/annotation/VSP_021501|||http://purl.uniprot.org/annotation/VSP_021502|||http://purl.uniprot.org/annotation/VSP_021503|||http://purl.uniprot.org/annotation/VSP_021504|||http://purl.uniprot.org/annotation/VSP_021505|||http://purl.uniprot.org/annotation/VSP_021506|||http://purl.uniprot.org/annotation/VSP_021507|||http://purl.uniprot.org/annotation/VSP_021508|||http://purl.uniprot.org/annotation/VSP_021509|||http://purl.uniprot.org/annotation/VSP_021510|||http://purl.uniprot.org/annotation/VSP_021511|||http://purl.uniprot.org/annotation/VSP_021512|||http://purl.uniprot.org/annotation/VSP_021513
http://togogenome.org/gene/9606:GDF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99988                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with GFRAL. Abolishes RET phosphorylation and cellular signaling mediated by GFRAL and RET.|||Disordered|||Growth/differentiation factor 15|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on interaction with GFRAL. Attenuates GDF15-mediated food-intake inhibition.|||Polar residues|||Reduces cellular signaling mediated by GFRAL and RET.|||Reduces cellular signaling mediated by GFRAL and RET. Abolishes interaction with GFRAL and GDF15-mediated food-intake inhibition.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033992|||http://purl.uniprot.org/annotation/PRO_0000033993|||http://purl.uniprot.org/annotation/VAR_010386|||http://purl.uniprot.org/annotation/VAR_047646|||http://purl.uniprot.org/annotation/VAR_047647
http://togogenome.org/gene/9606:COG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UP83                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 5|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213510|||http://purl.uniprot.org/annotation/VAR_039142|||http://purl.uniprot.org/annotation/VAR_039143|||http://purl.uniprot.org/annotation/VAR_039182|||http://purl.uniprot.org/annotation/VAR_055664|||http://purl.uniprot.org/annotation/VSP_031610|||http://purl.uniprot.org/annotation/VSP_031611
http://togogenome.org/gene/9606:TNFRSF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02223                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form IL2/TNFRSF17 oncogene|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||TNFR-Cys|||Tumor necrosis factor receptor superfamily member 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058935|||http://purl.uniprot.org/annotation/VAR_012234|||http://purl.uniprot.org/annotation/VAR_018755|||http://purl.uniprot.org/annotation/VAR_018756|||http://purl.uniprot.org/annotation/VAR_018757|||http://purl.uniprot.org/annotation/VAR_018758|||http://purl.uniprot.org/annotation/VAR_018759|||http://purl.uniprot.org/annotation/VAR_061855|||http://purl.uniprot.org/annotation/VSP_047678
http://togogenome.org/gene/9606:ADCY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TZ7|||http://purl.uniprot.org/uniprot/Q8NFM4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 4|||Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195690|||http://purl.uniprot.org/annotation/VSP_055816|||http://purl.uniprot.org/annotation/VSP_055817|||http://purl.uniprot.org/annotation/VSP_055818|||http://purl.uniprot.org/annotation/VSP_055819
http://togogenome.org/gene/9606:ARF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18085                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor 4|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207391|||http://purl.uniprot.org/annotation/VAR_048317
http://togogenome.org/gene/9606:FLACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8B8|||http://purl.uniprot.org/uniprot/Q96Q35                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Flagellum-associated coiled-coil domain-containing protein 1|||In isoform 2.|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064540|||http://purl.uniprot.org/annotation/VAR_045625|||http://purl.uniprot.org/annotation/VSP_046184
http://togogenome.org/gene/9606:POU3F4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y739|||http://purl.uniprot.org/uniprot/P49335                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In DFNX2.|||In DFNX2; somatic mosaicism in 50% of the peripheral blood lymphocytes.|||POU domain, class 3, transcription factor 4|||POU-specific|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100732|||http://purl.uniprot.org/annotation/VAR_003782|||http://purl.uniprot.org/annotation/VAR_003783|||http://purl.uniprot.org/annotation/VAR_003784|||http://purl.uniprot.org/annotation/VAR_003785|||http://purl.uniprot.org/annotation/VAR_003786|||http://purl.uniprot.org/annotation/VAR_015261|||http://purl.uniprot.org/annotation/VAR_067431
http://togogenome.org/gene/9606:HGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4R4|||http://purl.uniprot.org/uniprot/O14964                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||Hepatocyte growth factor-regulated tyrosine kinase substrate|||In isoform 2.|||Interaction with NF2|||Interaction with SNAP25 and TRAK2|||Interaction with SNX1|||Interaction with STAM|||N6-acetyllysine|||N6-succinyllysine|||Phosphotyrosine|||Polar residues|||Strongly reduced ubiquitin-binding. Reduced degradation of ubiquitinated EGFR.|||UIM|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098708|||http://purl.uniprot.org/annotation/VAR_052981|||http://purl.uniprot.org/annotation/VAR_054154|||http://purl.uniprot.org/annotation/VAR_061991|||http://purl.uniprot.org/annotation/VSP_036172
http://togogenome.org/gene/9606:RPS21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63220|||http://purl.uniprot.org/uniprot/Q6FGH5                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Non-terminal Residue|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Small ribosomal subunit protein eS21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194730
http://togogenome.org/gene/9606:TRMT10C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L0Y3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolished mitochondrial tRNA methylation. Does not affect mitochondrial tRNA 5'-end processing.|||In COXPD30; decreased protein abundance; impaired mitochondrial tRNA processing; has no effect on steady-state mitochondrial-mRNA and mitochondrial-tRNA levels but indirectly impairs mitochondrial translation.|||Mitochondrion|||Phosphoserine|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311309|||http://purl.uniprot.org/annotation/VAR_057355|||http://purl.uniprot.org/annotation/VAR_057356|||http://purl.uniprot.org/annotation/VAR_076993|||http://purl.uniprot.org/annotation/VAR_076994
http://togogenome.org/gene/9606:PACSIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FIA3|||http://purl.uniprot.org/uniprot/Q9UNF0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Interaction with HCV NS5A|||Decreased protein interaction with HCVNS5A.|||Disordered|||F-BAR|||In isoform 2.|||Increased protein interaction with HCVNS5A.|||N6-acetyllysine|||NPF1|||NPF2|||NPF3|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Protein kinase C and casein kinase substrate in neurons protein 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161795|||http://purl.uniprot.org/annotation/VAR_013711|||http://purl.uniprot.org/annotation/VAR_013712|||http://purl.uniprot.org/annotation/VAR_053555|||http://purl.uniprot.org/annotation/VSP_004517
http://togogenome.org/gene/9606:PRDM12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4Q4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In HSAN8; no effect on nuclear localization; not able to induce histone H3-K9 dimethylation.|||In HSAN8; reduced protein amount; results in protein aggregation.|||PR domain zinc finger protein 12|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047769|||http://purl.uniprot.org/annotation/VAR_074617|||http://purl.uniprot.org/annotation/VAR_074618|||http://purl.uniprot.org/annotation/VAR_074619|||http://purl.uniprot.org/annotation/VAR_074620|||http://purl.uniprot.org/annotation/VAR_074621|||http://purl.uniprot.org/annotation/VAR_074622|||http://purl.uniprot.org/annotation/VAR_074623
http://togogenome.org/gene/9606:CCNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cyclin-L1|||Cyclin-like 1|||Cyclin-like 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||RS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080480|||http://purl.uniprot.org/annotation/VSP_016120|||http://purl.uniprot.org/annotation/VSP_016121|||http://purl.uniprot.org/annotation/VSP_016122|||http://purl.uniprot.org/annotation/VSP_016123|||http://purl.uniprot.org/annotation/VSP_058299|||http://purl.uniprot.org/annotation/VSP_058300
http://togogenome.org/gene/9606:TERB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||Basic and acidic residues|||Disordered|||In SPGF60.|||In SPGF60; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with TERF1|||Myb-like|||Phosphothreonine|||Polar residues|||Telomere repeats-binding bouquet formation protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320156|||http://purl.uniprot.org/annotation/VAR_086535|||http://purl.uniprot.org/annotation/VAR_086536|||http://purl.uniprot.org/annotation/VAR_087422|||http://purl.uniprot.org/annotation/VAR_087423|||http://purl.uniprot.org/annotation/VSP_031613|||http://purl.uniprot.org/annotation/VSP_031614|||http://purl.uniprot.org/annotation/VSP_031615
http://togogenome.org/gene/9606:RASA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20936|||http://purl.uniprot.org/uniprot/Q59GK3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2|||Disordered|||In CMAVM1.|||In CMAVM1; unknown pathological significance.|||In basal cell carcinomas.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||PH|||Phosphoserine|||Phosphotyrosine|||Ras GTPase-activating protein 1|||Ras-GAP|||SH2|||SH2 1|||SH2 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056636|||http://purl.uniprot.org/annotation/VAR_002650|||http://purl.uniprot.org/annotation/VAR_002651|||http://purl.uniprot.org/annotation/VAR_002652|||http://purl.uniprot.org/annotation/VAR_017744|||http://purl.uniprot.org/annotation/VAR_072088|||http://purl.uniprot.org/annotation/VAR_072089|||http://purl.uniprot.org/annotation/VAR_072090|||http://purl.uniprot.org/annotation/VAR_072091|||http://purl.uniprot.org/annotation/VSP_001625|||http://purl.uniprot.org/annotation/VSP_001626|||http://purl.uniprot.org/annotation/VSP_057432|||http://purl.uniprot.org/annotation/VSP_057433|||http://purl.uniprot.org/annotation/VSP_057434|||http://purl.uniprot.org/annotation/VSP_057435
http://togogenome.org/gene/9606:DHX36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2U1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent DNA/RNA helicase DHX36|||DEAH box|||DSM (DHX36-specific motif)|||Disordered|||Does not inhibit G4-DNA-binding; when associated with A-65.|||Does not inhibit G4-DNA-binding; when associated with A-66.|||Greatly reduces G4-RNA-binding; when associated with P-59.|||Greatly reduces G4-RNA-binding; when associated with P-63.|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Inhibits G4-DNA-binding; when associated with L-55 and L-59.|||Inhibits G4-DNA-binding; when associated with L-55 and L-63.|||Inhibits G4-DNA-binding; when associated with L-59 and L-63.|||Loss of ATPase activity; results in an increased in G4-DNA- and G4-RNA-binding stabilities, increases localization in cytoplasmic stress granules and loss of mRNA deadenylation and mRNA decay.|||N6-acetyllysine|||Necessary for interaction with single-stranded DNA at the 3'-end of the G4-DNA structure|||Necessary for nuclear and nucleolar caps localizations|||Nuclear localization signal|||OB-fold-like subdomains|||Phosphoserine|||RecA-like domain 1|||RecA-like domain 2|||Reduces G4-RNA binding; when associated with A-57, A-59, A-62 and A-63.|||Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-62.|||Reduces G4-RNA-binding; when associated with G-54, A-57, A-59 and A-63.|||Reduces G4-RNA-binding; when associated with G-54, A-57, A-62 and A-63.|||Reduces G4-RNA-binding; when associated with G-54, A-59, A-62 and A-63.|||Required for G4-DNA- and G4-RNA-binding|||Required for recruitment to cytoplasmic stress granules|||Required for the pre-miR-134 transport|||WH domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247530|||http://purl.uniprot.org/annotation/VAR_027140|||http://purl.uniprot.org/annotation/VAR_027141|||http://purl.uniprot.org/annotation/VAR_027142|||http://purl.uniprot.org/annotation/VSP_020006|||http://purl.uniprot.org/annotation/VSP_020007
http://togogenome.org/gene/9606:BEND7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7W2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEN|||BEN domain-containing protein 7|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244080|||http://purl.uniprot.org/annotation/VAR_035501|||http://purl.uniprot.org/annotation/VAR_057830|||http://purl.uniprot.org/annotation/VSP_019506|||http://purl.uniprot.org/annotation/VSP_019507|||http://purl.uniprot.org/annotation/VSP_019508|||http://purl.uniprot.org/annotation/VSP_039846|||http://purl.uniprot.org/annotation/VSP_039847
http://togogenome.org/gene/9606:LEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0Y8|||http://purl.uniprot.org/uniprot/P41159                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In LEPD.|||In LEPD; no effect on secretion; does not bind or activate LEPR.|||Leptin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017685|||http://purl.uniprot.org/annotation/PRO_5014296862|||http://purl.uniprot.org/annotation/VAR_004196|||http://purl.uniprot.org/annotation/VAR_004197|||http://purl.uniprot.org/annotation/VAR_008094|||http://purl.uniprot.org/annotation/VAR_011955|||http://purl.uniprot.org/annotation/VAR_075144
http://togogenome.org/gene/9606:OR6B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IFH4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150621|||http://purl.uniprot.org/annotation/VAR_062047|||http://purl.uniprot.org/annotation/VAR_062048
http://togogenome.org/gene/9606:GEM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55040                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||GTP-binding protein GEM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122475|||http://purl.uniprot.org/annotation/VAR_020097
http://togogenome.org/gene/9606:COL15A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTP7|||http://purl.uniprot.org/uniprot/P39059                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X tandem repeats|||Collagen alpha-1(XV) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Disordered|||Laminin G|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region 1 (NC1)|||Nonhelical region 10 (NC10)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Nonhelical region 4 (NC4)|||Nonhelical region 5 (NC5)|||Nonhelical region 6 (NC6)|||Nonhelical region 7 (NC7)|||Nonhelical region 8 (NC8)|||Nonhelical region 9 (NC9)|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Pro residues|||Restin|||Restin-2|||Restin-3|||Restin-4|||Triple-helical region 1 (COL1)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)|||Triple-helical region 4 (COL4)|||Triple-helical region 5 (COL5)|||Triple-helical region 6 (COL6)|||Triple-helical region 7 (COL7)|||Triple-helical region 8 (COL8)|||Triple-helical region 9 (COL9)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005788|||http://purl.uniprot.org/annotation/PRO_0000005789|||http://purl.uniprot.org/annotation/PRO_0000423014|||http://purl.uniprot.org/annotation/PRO_0000423015|||http://purl.uniprot.org/annotation/PRO_0000423016|||http://purl.uniprot.org/annotation/PRO_5002788660|||http://purl.uniprot.org/annotation/VAR_033787|||http://purl.uniprot.org/annotation/VAR_033788|||http://purl.uniprot.org/annotation/VAR_033789|||http://purl.uniprot.org/annotation/VAR_033790|||http://purl.uniprot.org/annotation/VAR_033791|||http://purl.uniprot.org/annotation/VAR_033792|||http://purl.uniprot.org/annotation/VAR_033793|||http://purl.uniprot.org/annotation/VAR_033794|||http://purl.uniprot.org/annotation/VAR_033795|||http://purl.uniprot.org/annotation/VAR_033796|||http://purl.uniprot.org/annotation/VAR_048776|||http://purl.uniprot.org/annotation/VAR_061114
http://togogenome.org/gene/9606:TRIP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15654                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Disordered|||Exclusively located in nucleus.|||In isoform 2.|||In isoform 3.|||Interaction with MAGI1 and PTPN13|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine; by SRC|||Pro residues|||Reduces interaction with MAGI1.|||Thyroid receptor-interacting protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075908|||http://purl.uniprot.org/annotation/VAR_013309|||http://purl.uniprot.org/annotation/VAR_050171|||http://purl.uniprot.org/annotation/VAR_062262|||http://purl.uniprot.org/annotation/VSP_047621|||http://purl.uniprot.org/annotation/VSP_047622|||http://purl.uniprot.org/annotation/VSP_047623|||http://purl.uniprot.org/annotation/VSP_047624
http://togogenome.org/gene/9606:LY6G6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L6Z9X4|||http://purl.uniprot.org/uniprot/O95868                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated serine|||Lymphocyte antigen 6 complex locus protein G6d|||O-linked (GalNAc...) threonine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323707|||http://purl.uniprot.org/annotation/PRO_0000323708|||http://purl.uniprot.org/annotation/PRO_5014272367|||http://purl.uniprot.org/annotation/VAR_039564|||http://purl.uniprot.org/annotation/VAR_039565
http://togogenome.org/gene/9606:PLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN26|||http://purl.uniprot.org/uniprot/P00750                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||EGF-like|||Fibronectin type-I|||Important for binding to LRP1|||Important for binding to annexin A2|||Important for single-chain activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interchain (between A and B chains)|||Kringle|||Kringle 1|||Kringle 2|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Not glycosylated|||O-linked (Fuc) threonine|||Peptidase S1|||Removed by plasmin|||Tissue-type plasminogen activator|||Tissue-type plasminogen activator chain A|||Tissue-type plasminogen activator chain B|||t-plasminogen activator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000029|||http://purl.uniprot.org/annotation/CAR_000030|||http://purl.uniprot.org/annotation/CAR_000031|||http://purl.uniprot.org/annotation/PRO_0000028348|||http://purl.uniprot.org/annotation/PRO_0000028349|||http://purl.uniprot.org/annotation/PRO_0000028350|||http://purl.uniprot.org/annotation/PRO_0000028351|||http://purl.uniprot.org/annotation/PRO_0000028352|||http://purl.uniprot.org/annotation/PRO_5014567682|||http://purl.uniprot.org/annotation/VAR_011783|||http://purl.uniprot.org/annotation/VAR_020181|||http://purl.uniprot.org/annotation/VAR_038732|||http://purl.uniprot.org/annotation/VAR_038733|||http://purl.uniprot.org/annotation/VSP_005411|||http://purl.uniprot.org/annotation/VSP_005412|||http://purl.uniprot.org/annotation/VSP_015957|||http://purl.uniprot.org/annotation/VSP_028029|||http://purl.uniprot.org/annotation/VSP_028030
http://togogenome.org/gene/9606:EVI2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22794                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein EVI2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021211|||http://purl.uniprot.org/annotation/VSP_038859
http://togogenome.org/gene/9606:METTL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5L8|||http://purl.uniprot.org/uniprot/Q9H7H0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Methyltransferase-like protein 17, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312163|||http://purl.uniprot.org/annotation/PRO_5006608321|||http://purl.uniprot.org/annotation/VAR_037422|||http://purl.uniprot.org/annotation/VAR_037423|||http://purl.uniprot.org/annotation/VAR_072388|||http://purl.uniprot.org/annotation/VSP_029720|||http://purl.uniprot.org/annotation/VSP_029721
http://togogenome.org/gene/9606:STX17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56962                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alters localization to the autophagosome; when associated with Leu-244.|||Alters localization to the autophagosome; when associated with Leu-248.|||Alters localization to the autophagosome; when associated with Leu-264.|||Alters localization to the autophagosome; when associated with Leu-268.|||Cytoplasmic|||Endoplasmic reticulum retention signal|||Helical|||Localizes to the Golgi instead of the endoplasmic reticulum.|||Lumenal|||N-acetylserine|||N6-acetyllysine|||Necessary and sufficient for localization to autophagosome|||Phosphoserine|||Phosphotyrosine; by ABL1|||Removed|||Syntaxin-17|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210228
http://togogenome.org/gene/9606:EEF1AKMT4-ECE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPD6|||http://purl.uniprot.org/uniprot/P0DPD8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EEF1AKMT4-ECE2 readthrough transcript protein|||Endothelin-converting enzyme 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform ECE2-2.|||In isoform ECE2-3.|||Lumenal|||Methyltransferase-like region|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Phosphotyrosine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078223|||http://purl.uniprot.org/annotation/PRO_0000443293|||http://purl.uniprot.org/annotation/VAR_037085|||http://purl.uniprot.org/annotation/VSP_059324|||http://purl.uniprot.org/annotation/VSP_059325
http://togogenome.org/gene/9606:TRPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Great loss of sumoylation and 30% reduction in repression activity. Almost complete loss of sumoylation and 70% reduction in repression activity; when associated with R-1192.|||In TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency.|||In TRPS3.|||In TRPS3; in heterozygous status has a milder effect causing TRPS1.|||In TRPS3; severe.|||In isoform 2.|||In isoform 3.|||Mediates interaction with GLI3|||Mediates interaction with RNF4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcriptional repressor domain|||Very little change in sumoylation and 30% reduction in repression activity. Almost complete loss of sumoylation and 70% reduction in repression activity; when associated with R-1201.|||Zinc finger transcription factor Trps1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083508|||http://purl.uniprot.org/annotation/VAR_012807|||http://purl.uniprot.org/annotation/VAR_012808|||http://purl.uniprot.org/annotation/VAR_012809|||http://purl.uniprot.org/annotation/VAR_012810|||http://purl.uniprot.org/annotation/VAR_012811|||http://purl.uniprot.org/annotation/VAR_038197|||http://purl.uniprot.org/annotation/VAR_038198|||http://purl.uniprot.org/annotation/VAR_038199|||http://purl.uniprot.org/annotation/VSP_037549|||http://purl.uniprot.org/annotation/VSP_037550
http://togogenome.org/gene/9606:SNX17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDM3|||http://purl.uniprot.org/uniprot/B4DQ37|||http://purl.uniprot.org/uniprot/B4DTB8|||http://purl.uniprot.org/uniprot/Q15036                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FERM-like|||In isoform 2.|||No association with endosomes.|||No effect on interaction with CCDC22, CCDC93, VPS26C and VPS35L.|||PTB-like F3 module|||PX|||Phosphoserine|||Ras-associating|||Slightly decreases interaction with CCDC22, CCDC93, VPS26C and VPS35L.|||Sorting nexin-17|||Sorting nexin-17/31 FERM|||Strongly decreases interaction with CCDC22, CCDC93, VPS26C and VPS35L. No effect on endosomal location.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213865|||http://purl.uniprot.org/annotation/VSP_044935
http://togogenome.org/gene/9606:ANGPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTQ9|||http://purl.uniprot.org/uniprot/Q15389                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Angiopoietin-1|||Fibrinogen C-terminal|||In HAE5; decreased oligomerization; decreased interaction with TEK; fails to form proper cell-cell adhesions in an in vitro model of endothelial cell barrier.|||In HAE5; unknown pathological significance; does not affect oligomerization; does not affect interaction with TEK.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009110|||http://purl.uniprot.org/annotation/VAR_069165|||http://purl.uniprot.org/annotation/VAR_085814|||http://purl.uniprot.org/annotation/VAR_085815|||http://purl.uniprot.org/annotation/VAR_085816|||http://purl.uniprot.org/annotation/VSP_046324
http://togogenome.org/gene/9606:SH2D1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60880                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Disrupts interaction with FYN.|||In XLP1.|||In XLP1; abolishes interaction with SLAMF1.|||In XLP1; loss of interaction with CD84 and reduced affinity for SLAMF1.|||In XLP1; loss of interaction with CD84; loss of interaction with non-phosphorylated SLAMF1.|||In XLP1; loss of interaction with CD84; strongly reduced affinity for SLAMF1.|||In XLP1; reduced affinity for SLAMF1 and FYN.|||In XLP1; reduced protein stability and reduced affinity for SLAMF1 and FYN.|||In XLP1; reduced protein stability and reduced affinity for SLAMF1, decreases interaction with FYN.|||In XLP1; reduced protein stability and strongly reduced affinity for SLAMF1, decreases interaction with FYN.|||In XLP1; reduced protein stability and strongly reduced affinity for SLAMF1, disrupts interaction with FYN.|||In XLP1; reduced protein stability.|||In XLP1; unknown pathological significance.|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||In one XLP1 patient; unknown pathological significance.|||Interaction with FYN SH3 domain|||N6-acetyllysine|||SH2|||SH2 domain-containing protein 1A|||Strongly reduced affinity for SLAMF1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097722|||http://purl.uniprot.org/annotation/VAR_005612|||http://purl.uniprot.org/annotation/VAR_005613|||http://purl.uniprot.org/annotation/VAR_005614|||http://purl.uniprot.org/annotation/VAR_018307|||http://purl.uniprot.org/annotation/VAR_048005|||http://purl.uniprot.org/annotation/VAR_048006|||http://purl.uniprot.org/annotation/VAR_048007|||http://purl.uniprot.org/annotation/VAR_048008|||http://purl.uniprot.org/annotation/VAR_048009|||http://purl.uniprot.org/annotation/VAR_048010|||http://purl.uniprot.org/annotation/VAR_048011|||http://purl.uniprot.org/annotation/VAR_048012|||http://purl.uniprot.org/annotation/VAR_048013|||http://purl.uniprot.org/annotation/VAR_048014|||http://purl.uniprot.org/annotation/VAR_048015|||http://purl.uniprot.org/annotation/VAR_048016|||http://purl.uniprot.org/annotation/VAR_048017|||http://purl.uniprot.org/annotation/VAR_048018|||http://purl.uniprot.org/annotation/VAR_048019|||http://purl.uniprot.org/annotation/VAR_048020|||http://purl.uniprot.org/annotation/VAR_088139|||http://purl.uniprot.org/annotation/VAR_088140|||http://purl.uniprot.org/annotation/VAR_088141|||http://purl.uniprot.org/annotation/VAR_088142|||http://purl.uniprot.org/annotation/VAR_088143|||http://purl.uniprot.org/annotation/VAR_088144|||http://purl.uniprot.org/annotation/VSP_004386|||http://purl.uniprot.org/annotation/VSP_004387|||http://purl.uniprot.org/annotation/VSP_004388|||http://purl.uniprot.org/annotation/VSP_004389|||http://purl.uniprot.org/annotation/VSP_004390
http://togogenome.org/gene/9606:CAPRIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KZC0|||http://purl.uniprot.org/uniprot/Q6IMN6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Caprin-2|||Disordered|||Impaired homotrimer formation. No effect on LRP6 binding although LRP6 phosphorylation is significantly reduced.|||In isoform 10.|||In isoform 2, isoform 3 and isoform 9.|||In isoform 2.|||In isoform 3, isoform 7 and isoform 10.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 10.|||Loss of calcium binding and increased homotrimer stability; when associated with Ala-1078.|||Loss of calcium binding and increased homotrimer stability; when associated with Ala-1084.|||No effect on homotrimer formation.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302082|||http://purl.uniprot.org/annotation/VAR_034939|||http://purl.uniprot.org/annotation/VAR_048445|||http://purl.uniprot.org/annotation/VAR_048446|||http://purl.uniprot.org/annotation/VAR_048447|||http://purl.uniprot.org/annotation/VSP_027920|||http://purl.uniprot.org/annotation/VSP_043293|||http://purl.uniprot.org/annotation/VSP_052531|||http://purl.uniprot.org/annotation/VSP_052532|||http://purl.uniprot.org/annotation/VSP_052533|||http://purl.uniprot.org/annotation/VSP_052534|||http://purl.uniprot.org/annotation/VSP_052535|||http://purl.uniprot.org/annotation/VSP_052536|||http://purl.uniprot.org/annotation/VSP_052537|||http://purl.uniprot.org/annotation/VSP_052538|||http://purl.uniprot.org/annotation/VSP_052539
http://togogenome.org/gene/9606:PRKRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H875                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with EIF2AK2|||PRKR-interacting protein 1|||Required for RNA-binding|||Required for nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324787|||http://purl.uniprot.org/annotation/VAR_039882|||http://purl.uniprot.org/annotation/VAR_039883|||http://purl.uniprot.org/annotation/VSP_056088|||http://purl.uniprot.org/annotation/VSP_056089
http://togogenome.org/gene/9606:SPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35270                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by CaMK2. No effect on kinetic parameters.|||In DRDSPRD.|||In DRDSPRD; loss of sepiapterin reductase activity.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by CaMK2; in vitro|||Sepiapterin reductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072149|||http://purl.uniprot.org/annotation/VAR_058007|||http://purl.uniprot.org/annotation/VAR_058008|||http://purl.uniprot.org/annotation/VAR_085775
http://togogenome.org/gene/9606:CMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7K0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  CHCH|||COX assembly mitochondrial protein homolog|||Cx9C motif 1|||Cx9C motif 2|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317185
http://togogenome.org/gene/9606:IDE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISG5|||http://purl.uniprot.org/uniprot/A0A7I2V2P6|||http://purl.uniprot.org/uniprot/B3KSB8|||http://purl.uniprot.org/uniprot/P14735                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases dimerization. No effect on degradation of ANP. Retains the ability to degrade an aberrant form of ANP, when in the presence of both ANP and the aberrant ANP.|||In isoform 2.|||Increases catalytic rate towards INS and amyloid; when associated with C-132.|||Increases catalytic rate towards INS and amyloid; when associated with C-184.|||Increases catalytic rate towards INS and amyloid; when associated with C-426.|||Increases catalytic rate towards INS and amyloid; when associated with C-817.|||Increases catalytic rate towards INS and amyloid; when associated with C-828.|||Increases catalytic rate towards INS and amyloid; when associated with C-899.|||Insulin-degrading enzyme|||Loss of catalytic activity.|||N6-succinyllysine|||No effect on catalytic activity.|||Peptidase M16 C-terminal|||Peptidase M16 N-terminal|||Peptidase M16 middle/third|||Proton acceptor|||Reduced enzyme activity.|||SlyX motif|||Strongly increased enzyme activity.|||Strongly reduced enzyme activity.|||in the exosite                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074404|||http://purl.uniprot.org/annotation/VSP_044303
http://togogenome.org/gene/9606:DUS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKP8|||http://purl.uniprot.org/uniprot/E7EUN9|||http://purl.uniprot.org/uniprot/Q9NX74                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic domain|||DRBM|||Decreased affinity for tRNA.|||Decreased affinity for tRNA. Strongly decreased affinity for tRNA; when associated with A-419.|||Decreased affinity for tRNA. Strongly decreased affinity for tRNA; when associated with A-420.|||Disordered|||Increased affinity for tRNA and increased dihydrouridine synthesis; when associated with K-294.|||Increased affinity for tRNA and increased dihydrouridine synthesis; when associated with K-305.|||Interaction with tRNA|||Mildly decreased affinity for tRNA.|||Phosphoserine|||Polar residues|||Proton donor|||Strongly decreased affinity for tRNA.|||tRNA-dihydrouridine(20) synthase [NAD(P)+]-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162157
http://togogenome.org/gene/9606:XXYLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBI6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with target proteins|||Lumenal|||Xyloside xylosyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234427|||http://purl.uniprot.org/annotation/VSP_018315|||http://purl.uniprot.org/annotation/VSP_018316|||http://purl.uniprot.org/annotation/VSP_018317|||http://purl.uniprot.org/annotation/VSP_018318
http://togogenome.org/gene/9606:BFAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BMP2|||http://purl.uniprot.org/uniprot/Q9NZS9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Bifunctional apoptosis regulator|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||RING-type|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055822|||http://purl.uniprot.org/annotation/VAR_052075|||http://purl.uniprot.org/annotation/VAR_052076|||http://purl.uniprot.org/annotation/VSP_055879|||http://purl.uniprot.org/annotation/VSP_055880
http://togogenome.org/gene/9606:SPAG11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR37|||http://purl.uniprot.org/uniprot/C9IZU7|||http://purl.uniprot.org/uniprot/Q08648|||http://purl.uniprot.org/uniprot/Q6PDA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform EP2B.|||In isoform EP2C.|||In isoform EP2D.|||In isoform EP2E.|||N-linked (GlcNAc...) asparagine|||Sperm-associated antigen 11A|||Sperm-associated antigen 11B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033185|||http://purl.uniprot.org/annotation/PRO_0000314165|||http://purl.uniprot.org/annotation/PRO_5001967081|||http://purl.uniprot.org/annotation/PRO_5002996361|||http://purl.uniprot.org/annotation/VAR_005269|||http://purl.uniprot.org/annotation/VAR_053683|||http://purl.uniprot.org/annotation/VAR_082918|||http://purl.uniprot.org/annotation/VSP_006208|||http://purl.uniprot.org/annotation/VSP_006209|||http://purl.uniprot.org/annotation/VSP_006210|||http://purl.uniprot.org/annotation/VSP_030220|||http://purl.uniprot.org/annotation/VSP_030221|||http://purl.uniprot.org/annotation/VSP_030222|||http://purl.uniprot.org/annotation/VSP_030223|||http://purl.uniprot.org/annotation/VSP_044926|||http://purl.uniprot.org/annotation/VSP_044927
http://togogenome.org/gene/9606:GJB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654ICK0|||http://purl.uniprot.org/uniprot/O75712                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction beta-3 protein|||Gap junction protein cysteine-rich|||Helical|||In DFNA2B.|||In DFNA2B; unknown pathological significance.|||In EKVP1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057862|||http://purl.uniprot.org/annotation/VAR_002147|||http://purl.uniprot.org/annotation/VAR_002148|||http://purl.uniprot.org/annotation/VAR_002149|||http://purl.uniprot.org/annotation/VAR_002150|||http://purl.uniprot.org/annotation/VAR_011978|||http://purl.uniprot.org/annotation/VAR_015085|||http://purl.uniprot.org/annotation/VAR_015086|||http://purl.uniprot.org/annotation/VAR_015087|||http://purl.uniprot.org/annotation/VAR_022423
http://togogenome.org/gene/9606:NFAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94916                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform A.|||In isoform B, isoform Dand isoform E.|||In isoform B.|||In isoform D.|||Increased nuclear localization.|||N6-acetyllysine|||Normal nuclear localization.|||Nuclear factor of activated T-cells 5|||Phosphoserine|||Phosphothreonine; by CDK5|||Polar residues|||RHD|||Reduced nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205183|||http://purl.uniprot.org/annotation/VSP_058784|||http://purl.uniprot.org/annotation/VSP_058785|||http://purl.uniprot.org/annotation/VSP_058786|||http://purl.uniprot.org/annotation/VSP_058787|||http://purl.uniprot.org/annotation/VSP_058788
http://togogenome.org/gene/9606:IL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08700                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Interleukin-3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015516|||http://purl.uniprot.org/annotation/VAR_013071|||http://purl.uniprot.org/annotation/VAR_013072|||http://purl.uniprot.org/annotation/VAR_034014|||http://purl.uniprot.org/annotation/VAR_034015
http://togogenome.org/gene/9606:LYPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0L0|||http://purl.uniprot.org/uniprot/Q6UXB3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||Ly6/PLAUR domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226747|||http://purl.uniprot.org/annotation/PRO_0000226748|||http://purl.uniprot.org/annotation/PRO_5014303374|||http://purl.uniprot.org/annotation/VAR_052701|||http://purl.uniprot.org/annotation/VAR_052702
http://togogenome.org/gene/9606:INO80D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53TQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||INO80 complex subunit D|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319585|||http://purl.uniprot.org/annotation/VAR_039012
http://togogenome.org/gene/9606:HOXD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28358                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D10|||In CVT; also in Charcot-Marie-Tooth disease-like foot deformities.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200226|||http://purl.uniprot.org/annotation/VAR_022582
http://togogenome.org/gene/9606:KREMEN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53F67|||http://purl.uniprot.org/uniprot/Q8NCW0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||Kremen protein 2|||Kringle|||Kringle-containing protein marking the eye and the nose|||N-linked (GlcNAc...) asparagine|||WSC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021568|||http://purl.uniprot.org/annotation/PRO_5004248768|||http://purl.uniprot.org/annotation/VAR_059691|||http://purl.uniprot.org/annotation/VSP_046399|||http://purl.uniprot.org/annotation/VSP_047386|||http://purl.uniprot.org/annotation/VSP_050509|||http://purl.uniprot.org/annotation/VSP_050510|||http://purl.uniprot.org/annotation/VSP_050511|||http://purl.uniprot.org/annotation/VSP_050512|||http://purl.uniprot.org/annotation/VSP_050513|||http://purl.uniprot.org/annotation/VSP_050514
http://togogenome.org/gene/9606:PRPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWQ6|||http://purl.uniprot.org/uniprot/P41219                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In ALS; unknown pathological significance.|||In ALS; unknown pathological significance; leads to filamentous aggregate formation.|||In isoform 2.|||Linker 1|||Linker 2|||Peripherin|||Phosphoserine|||Phosphotyrosine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063779|||http://purl.uniprot.org/annotation/VAR_083259|||http://purl.uniprot.org/annotation/VAR_083260|||http://purl.uniprot.org/annotation/VSP_021159
http://togogenome.org/gene/9606:NCDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBB6                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||In NEDIES; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; in these cells, associated with markedly decreased phosphorylation of ERK1/ERK2, compared to wild-type, suggesting impaired GRM5 activation.|||In NEDIES; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; no effect on phosphorylation of ERK1/ERK2.|||In NEDIES; unknown pathological significance; in the neuroblastoma cell line SH-SY5Y, in which NCDN has been knocked out, does not rescue impaired neurite formation following retinoic acid treatment, contrary to wild-type; no effect on phosphorylation of ERK1/ERK2.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N-acetylserine|||Neurochondrin|||Phosphoserine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324617|||http://purl.uniprot.org/annotation/VAR_039849|||http://purl.uniprot.org/annotation/VAR_039850|||http://purl.uniprot.org/annotation/VAR_085876|||http://purl.uniprot.org/annotation/VAR_085877|||http://purl.uniprot.org/annotation/VAR_085878|||http://purl.uniprot.org/annotation/VAR_085879|||http://purl.uniprot.org/annotation/VSP_032315
http://togogenome.org/gene/9606:ADH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08319|||http://purl.uniprot.org/uniprot/V9HVX7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  All-trans-retinol dehydrogenase [NAD(+)] ADH4|||Enoyl reductase (ER)|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160681|||http://purl.uniprot.org/annotation/VAR_023461|||http://purl.uniprot.org/annotation/VAR_023462|||http://purl.uniprot.org/annotation/VAR_023463|||http://purl.uniprot.org/annotation/VSP_036788
http://togogenome.org/gene/9606:SCN1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PR05|||http://purl.uniprot.org/uniprot/Q07699                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Immunoglobulin V-set|||In ATFB13; the mutant results in highly reduced sodium currents and altered channel gating when coexpressed with SCN5A in a heterologous expression system.|||In ATFB13; the mutant results in reduced sodium currents when coexpressed with SCN5A in a heterologous expression system.|||In DEE52; severely decreased channel localization at the cell membrane.|||In DEE52; unknown pathological significance.|||In GEFSP1.|||In GEFSP1; can rescue the loss of function and defective trafficking to cell membrane phenotype of the SCN1A variant Thr-1852.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with idiopathic childhood epilepsy; de novo mutation; loss of function in increasing sodium channel activity.|||Probable disease-associated variant found in a patient with non-specific cardiac conduction defects.|||Sodium channel subunit beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014926|||http://purl.uniprot.org/annotation/VAR_010165|||http://purl.uniprot.org/annotation/VAR_062523|||http://purl.uniprot.org/annotation/VAR_062524|||http://purl.uniprot.org/annotation/VAR_062525|||http://purl.uniprot.org/annotation/VAR_062526|||http://purl.uniprot.org/annotation/VAR_062527|||http://purl.uniprot.org/annotation/VAR_062528|||http://purl.uniprot.org/annotation/VAR_067341|||http://purl.uniprot.org/annotation/VAR_070219|||http://purl.uniprot.org/annotation/VAR_070220|||http://purl.uniprot.org/annotation/VAR_078019|||http://purl.uniprot.org/annotation/VAR_078020|||http://purl.uniprot.org/annotation/VSP_041982
http://togogenome.org/gene/9606:ZMIZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JLS3|||http://purl.uniprot.org/uniprot/Q9ULJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDDFSA.|||In NEDDFSA; leads to altered positioning of pyramidal neurons.|||In NEDDFSA; leads to altered positioning of pyramidal neurons; decreased transcription coactivator activity; does not affect nuclear localization.|||In NEDDFSA; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||Polar residues|||Pro residues|||SP-RING-type|||Sufficient for transactivation activity; sufficient for interaction with NOTCH1|||Transactivation domain|||Zinc finger MIZ domain-containing protein 1|||Zmiz1 N-terminal tetratricopeptide repeat                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218987|||http://purl.uniprot.org/annotation/VAR_036326|||http://purl.uniprot.org/annotation/VAR_083438|||http://purl.uniprot.org/annotation/VAR_083439|||http://purl.uniprot.org/annotation/VAR_083440|||http://purl.uniprot.org/annotation/VAR_083441|||http://purl.uniprot.org/annotation/VAR_083442|||http://purl.uniprot.org/annotation/VAR_083443|||http://purl.uniprot.org/annotation/VSP_061581
http://togogenome.org/gene/9606:OPN1MW3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04001|||http://purl.uniprot.org/uniprot/P0DN77|||http://purl.uniprot.org/uniprot/P0DN78                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CBD and BCM.|||In CBD.|||In COD5; results in protein misfolding and retention in the endoplasmic reticulum.|||Medium-wave-sensitive opsin 1|||Medium-wave-sensitive opsin 2|||Medium-wave-sensitive opsin 3|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Required for 11-cis-retinal regeneration                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197785|||http://purl.uniprot.org/annotation/PRO_0000435400|||http://purl.uniprot.org/annotation/PRO_0000435401|||http://purl.uniprot.org/annotation/VAR_004841|||http://purl.uniprot.org/annotation/VAR_064051|||http://purl.uniprot.org/annotation/VAR_064052|||http://purl.uniprot.org/annotation/VAR_064053
http://togogenome.org/gene/9606:FBXO45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C2W1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  B30.2/SPRY|||F-box|||F-box/SPRY domain-containing protein 1|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285933
http://togogenome.org/gene/9606:CECR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7WPH3|||http://purl.uniprot.org/uniprot/Q9BXF3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Bromo|||Chromatin remodeling regulator CECR2|||Disordered|||In isoform B.|||In isoform C.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211192|||http://purl.uniprot.org/annotation/VAR_027411|||http://purl.uniprot.org/annotation/VAR_027412|||http://purl.uniprot.org/annotation/VSP_000571|||http://purl.uniprot.org/annotation/VSP_000572|||http://purl.uniprot.org/annotation/VSP_000573|||http://purl.uniprot.org/annotation/VSP_020407
http://togogenome.org/gene/9606:RIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4ADV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Guanine nucleotide exchange factor subunit RIC1|||In CATIFA; patient cells contain normally spliced transcripts corresponding to protein variant P-1265 but also transcripts that fail to splice due to intron 24 retention leading to a stop codon at position 1266; loss-of-function variant affecting procollagen secretion.|||In CATIFA; patient cells contain transcripts that fail to splice due to intron 24 retention leading to a stop codon at position 1266, but also normally spliced transcripts corresponding to protein variant P-1265; loss-of-function variant affecting procollagen secretion.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320662|||http://purl.uniprot.org/annotation/VAR_083541|||http://purl.uniprot.org/annotation/VAR_083542|||http://purl.uniprot.org/annotation/VSP_031706|||http://purl.uniprot.org/annotation/VSP_031707|||http://purl.uniprot.org/annotation/VSP_042408
http://togogenome.org/gene/9606:TNFRSF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93038                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Cytoplasmic|||Death|||Extracellular|||Helical|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6, isoform 7 and isoform 9.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||Suppresses homodimerization, TNFR1 interaction, and apoptosis induction.|||Suppresses homodimerization, and TNFR1 interaction.|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034606|||http://purl.uniprot.org/annotation/VAR_011814|||http://purl.uniprot.org/annotation/VAR_011815|||http://purl.uniprot.org/annotation/VAR_018826|||http://purl.uniprot.org/annotation/VAR_018827|||http://purl.uniprot.org/annotation/VAR_018828|||http://purl.uniprot.org/annotation/VSP_006491|||http://purl.uniprot.org/annotation/VSP_006492|||http://purl.uniprot.org/annotation/VSP_006493|||http://purl.uniprot.org/annotation/VSP_006494|||http://purl.uniprot.org/annotation/VSP_006495|||http://purl.uniprot.org/annotation/VSP_006496|||http://purl.uniprot.org/annotation/VSP_006497|||http://purl.uniprot.org/annotation/VSP_006498|||http://purl.uniprot.org/annotation/VSP_006499|||http://purl.uniprot.org/annotation/VSP_006500|||http://purl.uniprot.org/annotation/VSP_006501|||http://purl.uniprot.org/annotation/VSP_006502|||http://purl.uniprot.org/annotation/VSP_006503|||http://purl.uniprot.org/annotation/VSP_006504
http://togogenome.org/gene/9606:BPIFB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59827                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPI fold-containing family B member 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089159|||http://purl.uniprot.org/annotation/VAR_055998|||http://purl.uniprot.org/annotation/VAR_055999|||http://purl.uniprot.org/annotation/VAR_056000|||http://purl.uniprot.org/annotation/VAR_056001|||http://purl.uniprot.org/annotation/VAR_059372|||http://purl.uniprot.org/annotation/VAR_059373|||http://purl.uniprot.org/annotation/VAR_069042|||http://purl.uniprot.org/annotation/VAR_069043|||http://purl.uniprot.org/annotation/VSP_037828
http://togogenome.org/gene/9606:SLC9C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXW8|||http://purl.uniprot.org/uniprot/Q5TAH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Helical|||Ion transport-like|||N-linked (GlcNAc...) asparagine|||Sodium/hydrogen exchanger 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295706|||http://purl.uniprot.org/annotation/VAR_033331|||http://purl.uniprot.org/annotation/VAR_033332|||http://purl.uniprot.org/annotation/VAR_033333
http://togogenome.org/gene/9606:GP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1G2|||http://purl.uniprot.org/uniprot/P55259|||http://purl.uniprot.org/uniprot/Q68D34                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta hairpin|||D10C|||Disordered|||EGF-like|||External hydrophobic patch (EHP)|||Flexible ZP-N/ZP-C linker|||GPI-anchor amidated asparagine|||Helical|||Impaired interaction with fimH.|||In isoform 2.|||In isoform Alpha.|||In isoform Beta.|||Internal hydrophobic patch (IHP)|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Pancreatic secretory granule membrane major glycoprotein GP2|||Removed in mature form|||ZP|||ZP-C|||ZP-N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041657|||http://purl.uniprot.org/annotation/PRO_0000041658|||http://purl.uniprot.org/annotation/PRO_5004269537|||http://purl.uniprot.org/annotation/VSP_006948|||http://purl.uniprot.org/annotation/VSP_035749|||http://purl.uniprot.org/annotation/VSP_035750
http://togogenome.org/gene/9606:CSGALNACT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate N-acetylgalactosaminyltransferase 1|||Cytoplasmic|||Found in a patient with neuropathy; unknown pathological significance; loss of GalNAc-transferase activity; no effect on protein expression.|||Helical; Signal-anchor for type II membrane protein|||In SDJLABA; loss of GalNAc-transferase activity.|||In SDJLABA; reduced GalNAc-transferase activity.|||In SDJLABA; severely reduced GalNAc transferase activity.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189564|||http://purl.uniprot.org/annotation/VAR_055647|||http://purl.uniprot.org/annotation/VAR_055648|||http://purl.uniprot.org/annotation/VAR_060391|||http://purl.uniprot.org/annotation/VAR_078123|||http://purl.uniprot.org/annotation/VAR_078124|||http://purl.uniprot.org/annotation/VAR_078125|||http://purl.uniprot.org/annotation/VAR_084187|||http://purl.uniprot.org/annotation/VAR_084188|||http://purl.uniprot.org/annotation/VSP_012726|||http://purl.uniprot.org/annotation/VSP_012727|||http://purl.uniprot.org/annotation/VSP_012728
http://togogenome.org/gene/9606:NR1I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8P9|||http://purl.uniprot.org/uniprot/O75469                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes nuclear localization; when associated with 66-A-A-67.|||Abolishes nuclear localization; when associated with 91-A-A-92.|||Bipartite nuclear localization signal|||Hinge|||In allele PXR*2.|||In allele PXR*3.|||In allele PXR*4.|||In isoform 1B and isoform 2B.|||In isoform 1C and isoform 2C.|||In isoform 2A, isoform 2B and isoform 2C.|||In isoform 3.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 1 group I member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053547|||http://purl.uniprot.org/annotation/VAR_012228|||http://purl.uniprot.org/annotation/VAR_012229|||http://purl.uniprot.org/annotation/VAR_012230|||http://purl.uniprot.org/annotation/VAR_018340|||http://purl.uniprot.org/annotation/VAR_018341|||http://purl.uniprot.org/annotation/VAR_018342|||http://purl.uniprot.org/annotation/VAR_018343|||http://purl.uniprot.org/annotation/VAR_033237|||http://purl.uniprot.org/annotation/VAR_033238|||http://purl.uniprot.org/annotation/VAR_050581|||http://purl.uniprot.org/annotation/VSP_003667|||http://purl.uniprot.org/annotation/VSP_003668|||http://purl.uniprot.org/annotation/VSP_003669|||http://purl.uniprot.org/annotation/VSP_026669
http://togogenome.org/gene/9606:CCDC148                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFR7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 148|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326063|||http://purl.uniprot.org/annotation/VAR_039982|||http://purl.uniprot.org/annotation/VAR_039983|||http://purl.uniprot.org/annotation/VAR_039984|||http://purl.uniprot.org/annotation/VSP_032532|||http://purl.uniprot.org/annotation/VSP_032533|||http://purl.uniprot.org/annotation/VSP_032534|||http://purl.uniprot.org/annotation/VSP_032535|||http://purl.uniprot.org/annotation/VSP_032536|||http://purl.uniprot.org/annotation/VSP_045395|||http://purl.uniprot.org/annotation/VSP_045396|||http://purl.uniprot.org/annotation/VSP_045397
http://togogenome.org/gene/9606:NAP1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Nuclear localization signal|||Nucleosome assembly protein 1-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185655|||http://purl.uniprot.org/annotation/VSP_057064
http://togogenome.org/gene/9606:TRIM44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DX7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||B box-type|||Basic and acidic residues|||Disordered|||Does not affect function in negative regulation of PAX6 expression.|||In AN3; affects function and results in increased negative regulation of PAX6 expression compared to wild-type.|||Phosphoserine|||Tripartite motif-containing protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220372|||http://purl.uniprot.org/annotation/VAR_077852|||http://purl.uniprot.org/annotation/VAR_077853
http://togogenome.org/gene/9606:TRAPPC6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SZ2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Impairs interaction with TRAPPC1.|||In NEDMEBA.|||In isoform 2.|||Trafficking protein particle complex subunit 6B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211587|||http://purl.uniprot.org/annotation/VAR_080729|||http://purl.uniprot.org/annotation/VSP_009659
http://togogenome.org/gene/9606:ARHGAP22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFC0|||http://purl.uniprot.org/uniprot/Q7Z5H3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 22|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280469|||http://purl.uniprot.org/annotation/VAR_031153|||http://purl.uniprot.org/annotation/VAR_031154|||http://purl.uniprot.org/annotation/VSP_023703|||http://purl.uniprot.org/annotation/VSP_023704|||http://purl.uniprot.org/annotation/VSP_023705|||http://purl.uniprot.org/annotation/VSP_053502
http://togogenome.org/gene/9606:LPGAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92604                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Transmembrane                                                                                  ^@                                                                                  Acyl-CoA:lysophosphatidylglycerol acyltransferase 1|||HXXXXD motif|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208204
http://togogenome.org/gene/9606:SCPEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB40                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Retinoid-inducible serine carboxypeptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004284|||http://purl.uniprot.org/annotation/VAR_048684|||http://purl.uniprot.org/annotation/VAR_048685|||http://purl.uniprot.org/annotation/VSP_008555|||http://purl.uniprot.org/annotation/VSP_008556
http://togogenome.org/gene/9606:MYL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08590                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In CMH8.|||In CMH8; autosomal recessive.|||In CMH8; with mid-left ventricular chamber thickening.|||Myosin light chain 3|||N,N,N-trimethylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198696|||http://purl.uniprot.org/annotation/VAR_004599|||http://purl.uniprot.org/annotation/VAR_004600|||http://purl.uniprot.org/annotation/VAR_019842|||http://purl.uniprot.org/annotation/VAR_019843|||http://purl.uniprot.org/annotation/VAR_073726
http://togogenome.org/gene/9606:HRAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01112|||http://purl.uniprot.org/uniprot/X5D945                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL|||Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange.|||Cysteine methyl ester|||Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2.|||Effector region|||Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184.|||Found in a patient with severe fetal hydrops and pleural effusion; unknown pathological significance; decreased activation of Ras protein signal transduction.|||GTP-binding activity reduced by factor of 25.|||GTP-binding activity reduced by factor of 30.|||GTPase HRas|||GTPase HRas, N-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypervariable region|||In CMEMS.|||In CSTLO and CMEMS; also found in patients with oral squamous cell carcinoma.|||In CSTLO, bladder carcinoma and CMEMS; constitutively activated; interacts and recruits PLCE1 to plasma membrane.|||In CSTLO.|||In CSTLO; severe mutation.|||In H-Ras-3KR mutant; decreased fatty-acylation.|||In NMTC2; somatic mutation; increases transformation of cultured cell lines.|||In SFM; somatic mutation; shows constitutive activation of the MAPK and PI3K-AKT signaling pathways.|||In isoform 2.|||In melanoma; strongly reduced GTP hydrolysis in the presence of RAF1; increases transformation of cultured cell lines.|||Increased Ras signaling due to impaired ubiquitination.|||Loss of GTP-binding activity.|||Loss of GTPase activity and creation of an autophosphorylation site.|||Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine stimulation of Ras-GTPase activity. Mainly localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-181.|||Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12.|||Loss of interaction with PLCE1; when associated with V-12.|||Moderately increased transformation of cultured cell lines.|||N-acetylmethionine; in GTPase HRas; alternate|||N-acetylthreonine; in GTPase HRas, N-terminally processed|||No effect on interaction with PLCE1; when associated with V-12.|||Removed in mature form|||Removed; alternate|||S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate|||S-farnesyl cysteine|||S-nitrosocysteine|||S-palmitoyl cysteine|||S-palmitoyl cysteine; alternate|||Strongly increased transformation of cultured cell lines.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042996|||http://purl.uniprot.org/annotation/PRO_0000042997|||http://purl.uniprot.org/annotation/PRO_0000326476|||http://purl.uniprot.org/annotation/VAR_006836|||http://purl.uniprot.org/annotation/VAR_006837|||http://purl.uniprot.org/annotation/VAR_006838|||http://purl.uniprot.org/annotation/VAR_026106|||http://purl.uniprot.org/annotation/VAR_026107|||http://purl.uniprot.org/annotation/VAR_026108|||http://purl.uniprot.org/annotation/VAR_045975|||http://purl.uniprot.org/annotation/VAR_045976|||http://purl.uniprot.org/annotation/VAR_045977|||http://purl.uniprot.org/annotation/VAR_045978|||http://purl.uniprot.org/annotation/VAR_045979|||http://purl.uniprot.org/annotation/VAR_045980|||http://purl.uniprot.org/annotation/VAR_045981|||http://purl.uniprot.org/annotation/VAR_045982|||http://purl.uniprot.org/annotation/VAR_045983|||http://purl.uniprot.org/annotation/VAR_068816|||http://purl.uniprot.org/annotation/VAR_068817|||http://purl.uniprot.org/annotation/VAR_068818|||http://purl.uniprot.org/annotation/VAR_078259|||http://purl.uniprot.org/annotation/VSP_041597
http://togogenome.org/gene/9606:C16orf95                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X224|||http://purl.uniprot.org/uniprot/H3BNZ7|||http://purl.uniprot.org/uniprot/Q9H693                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C16orf95                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411091
http://togogenome.org/gene/9606:LRRC10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 10B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346162
http://togogenome.org/gene/9606:PRICKLE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3G6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Found in a patient with myoclonic epilepsy; unknown pathological significance; results in decreased protein activity; less active in stimulating calcium release compared to wild-type.|||Found in patients with severe progressive myoclonic epilepsy; unknown pathological significance; results in increased protein activity when associated with H-148; less active in stimulating calcium release when associated with H-148.|||Found in patients with severe progressive myoclonic epilepsy; unknown pathological significance; results in increased protein activity when associated with I-153; less active in stimulating calcium release when associated with I-153.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||PET|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prickle-like protein 2|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075891|||http://purl.uniprot.org/annotation/PRO_0000396718|||http://purl.uniprot.org/annotation/VAR_065582|||http://purl.uniprot.org/annotation/VAR_065583|||http://purl.uniprot.org/annotation/VAR_065584
http://togogenome.org/gene/9606:LSM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969L4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Sm|||U7 snRNA-associated Sm-like protein LSm10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125585
http://togogenome.org/gene/9606:SPATA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV2|||http://purl.uniprot.org/uniprot/Q9BWV2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Spermatogenesis-associated protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278446|||http://purl.uniprot.org/annotation/VAR_051375|||http://purl.uniprot.org/annotation/VSP_023282|||http://purl.uniprot.org/annotation/VSP_023283|||http://purl.uniprot.org/annotation/VSP_023284
http://togogenome.org/gene/9606:SNRPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63162|||http://purl.uniprot.org/uniprot/X5DP00                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Pro residues|||Repeat-rich region|||Sm|||Small nuclear ribonucleoprotein-associated protein N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125523|||http://purl.uniprot.org/annotation/VSP_056488
http://togogenome.org/gene/9606:ANP32E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0D5|||http://purl.uniprot.org/uniprot/E9PLC4|||http://purl.uniprot.org/uniprot/Q9BTT0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic leucine-rich nuclear phosphoprotein 32 family member E|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ANP32E-m1; abolished ability to interact with the H2A.Z/H2AZ1-H2B dimer.|||In ANP32E-m2; abolished ability to interact with the H2A.Z/H2AZ1-H2B dimer.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||N-acetylmethionine|||ZID domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137599|||http://purl.uniprot.org/annotation/VSP_045618|||http://purl.uniprot.org/annotation/VSP_047262
http://togogenome.org/gene/9606:ID3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02535                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  DNA-binding protein inhibitor ID-3|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127247|||http://purl.uniprot.org/annotation/VAR_016122|||http://purl.uniprot.org/annotation/VAR_030739
http://togogenome.org/gene/9606:KLF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWI3|||http://purl.uniprot.org/uniprot/Q9Y4X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||In isoform 3.|||Krueppel-like factor 12|||N6-methylated lysine; by EHMT2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047182|||http://purl.uniprot.org/annotation/VSP_006876|||http://purl.uniprot.org/annotation/VSP_047486|||http://purl.uniprot.org/annotation/VSP_047487
http://togogenome.org/gene/9606:DYNC2LI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCX1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytoplasmic dynein 2 light intermediate chain 1|||In SRTD15.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318750|||http://purl.uniprot.org/annotation/VAR_038874|||http://purl.uniprot.org/annotation/VAR_038875|||http://purl.uniprot.org/annotation/VAR_038876|||http://purl.uniprot.org/annotation/VAR_077814|||http://purl.uniprot.org/annotation/VAR_077815|||http://purl.uniprot.org/annotation/VSP_031287|||http://purl.uniprot.org/annotation/VSP_031288|||http://purl.uniprot.org/annotation/VSP_031289|||http://purl.uniprot.org/annotation/VSP_031290|||http://purl.uniprot.org/annotation/VSP_031291|||http://purl.uniprot.org/annotation/VSP_031292
http://togogenome.org/gene/9606:FDCSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q540F3|||http://purl.uniprot.org/uniprot/Q8NFU4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide                                                                                  ^@                                                                                  Follicular dendritic cell secreted peptide|||O-glycosylated at one site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021247|||http://purl.uniprot.org/annotation/PRO_5014309539
http://togogenome.org/gene/9606:ZFPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95159                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  B box-type; degenerate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Impairs the interaction with OLGA2/GM130 and cis-Golgi assembly.|||Lumenal|||Polar residues|||RING-type; degenerate|||Zinc finger protein-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056318|||http://purl.uniprot.org/annotation/VAR_034472
http://togogenome.org/gene/9606:SPINDOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUA3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Spindlin interactor and repressor of chromatin-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321528|||http://purl.uniprot.org/annotation/VAR_061607
http://togogenome.org/gene/9606:CST5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28325                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Motif|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cystatin-D|||In 45% of the population.|||Reactive site|||Secondary area of contact|||Variant Arg-46.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006645|||http://purl.uniprot.org/annotation/VAR_002208
http://togogenome.org/gene/9606:CPXM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SM3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||F5/8 type C|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Probable carboxypeptidase X1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004407
http://togogenome.org/gene/9606:VN1R4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5H5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele VN1R4*2 and allele VN1R4*3.|||In allele VN1R4*3.|||In allele VN1R4*4.|||N-linked (GlcNAc...) asparagine|||Vomeronasal type-1 receptor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070217|||http://purl.uniprot.org/annotation/VAR_022799|||http://purl.uniprot.org/annotation/VAR_022800|||http://purl.uniprot.org/annotation/VAR_022801
http://togogenome.org/gene/9606:NEIL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Endonuclease 8-like 2|||FPG-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of glycosylase and AP lyase activity.|||N6-acetyllysine|||No effect on glycosylase and AP lyase activity.|||Phosphoserine|||Proton donor|||Proton donor; for beta-elimination activity|||Proton donor; for delta-elimination activity|||Removed|||Schiff-base intermediate with DNA|||Strongly reduces strand AP lyase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170908|||http://purl.uniprot.org/annotation/VAR_020585|||http://purl.uniprot.org/annotation/VAR_020586|||http://purl.uniprot.org/annotation/VAR_020587|||http://purl.uniprot.org/annotation/VAR_020588|||http://purl.uniprot.org/annotation/VAR_020589|||http://purl.uniprot.org/annotation/VSP_012208|||http://purl.uniprot.org/annotation/VSP_012209|||http://purl.uniprot.org/annotation/VSP_043343
http://togogenome.org/gene/9606:TRIM34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYJ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM34|||In isoform 2.|||RING-type|||Reduced association with TRIM5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056248|||http://purl.uniprot.org/annotation/VAR_019825|||http://purl.uniprot.org/annotation/VAR_019826|||http://purl.uniprot.org/annotation/VAR_052141|||http://purl.uniprot.org/annotation/VSP_011921|||http://purl.uniprot.org/annotation/VSP_011922
http://togogenome.org/gene/9606:DNAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LDG9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dynein axonemal light chain 1|||In CILD16; reduced tethering interaction between DNAH5 and tubulin.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281130|||http://purl.uniprot.org/annotation/VAR_065739|||http://purl.uniprot.org/annotation/VSP_023982|||http://purl.uniprot.org/annotation/VSP_043590
http://togogenome.org/gene/9606:OSGIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y236                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Oxidative stress-induced growth inhibitor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165372|||http://purl.uniprot.org/annotation/VAR_050421|||http://purl.uniprot.org/annotation/VAR_050422|||http://purl.uniprot.org/annotation/VSP_041210
http://togogenome.org/gene/9606:SERPINB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30740|||http://purl.uniprot.org/uniprot/V9HWH1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CARD-binding motif (CBM)|||In isoform 2.|||Leukocyte elastase inhibitor|||Loss of proteinase-3-binding activity but caspase-binding activity remains unaffected; in association with A-343.|||Loss of proteinase-3-binding activity but caspase-binding activity remains unaffected; in association with A-344.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Reactive bond 1|||Reactive bond 2|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094101|||http://purl.uniprot.org/annotation/VAR_051945|||http://purl.uniprot.org/annotation/VSP_056511
http://togogenome.org/gene/9606:BBS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 7 protein|||Found in a patient with Bardet-Biedl syndrome also carrying a frameshift mutation in BBS10 and variant R-834 in KIF7.|||In BBS7.|||In a patient with Meckel-Gruber like syndrome also carrying Y-60 in TTC21B.|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064846|||http://purl.uniprot.org/annotation/VAR_017212|||http://purl.uniprot.org/annotation/VAR_017213|||http://purl.uniprot.org/annotation/VAR_038893|||http://purl.uniprot.org/annotation/VAR_065555|||http://purl.uniprot.org/annotation/VAR_066286|||http://purl.uniprot.org/annotation/VAR_066459|||http://purl.uniprot.org/annotation/VSP_008850
http://togogenome.org/gene/9606:TLCD3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBR7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 1.|||TLC|||TLC domain-containing protein 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185540|||http://purl.uniprot.org/annotation/VSP_008149
http://togogenome.org/gene/9606:RWDD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3V2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enhancement of NFKBIA and NR3C1 sumoylation. No effect on NR3C1 transcriptional activity.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Interaction with UBE2I/UBC9|||RWD|||RWD domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097545|||http://purl.uniprot.org/annotation/VAR_024346|||http://purl.uniprot.org/annotation/VAR_034420|||http://purl.uniprot.org/annotation/VSP_034176|||http://purl.uniprot.org/annotation/VSP_034177|||http://purl.uniprot.org/annotation/VSP_035411|||http://purl.uniprot.org/annotation/VSP_035412
http://togogenome.org/gene/9606:MAOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z242|||http://purl.uniprot.org/uniprot/P27338                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alters specificity towards synthetic inhibitors.|||Amine oxidase|||Amine oxidase [flavin-containing] B|||Complete loss of activity.|||Cytoplasmic|||Dramatic loss of activity.|||Helical|||Helical; Anchor for type IV membrane protein|||Important for catalytic activity|||In isoform 2.|||Mitochondrial intermembrane|||N-acetylserine|||N6-acetyllysine|||No loss of activity.|||Removed|||S-8alpha-FAD cysteine|||Significant loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099859|||http://purl.uniprot.org/annotation/VSP_057047|||http://purl.uniprot.org/annotation/VSP_057048|||http://purl.uniprot.org/annotation/VSP_057049
http://togogenome.org/gene/9606:WDR91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1P6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 91                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295746|||http://purl.uniprot.org/annotation/VAR_033358|||http://purl.uniprot.org/annotation/VSP_027058|||http://purl.uniprot.org/annotation/VSP_027059|||http://purl.uniprot.org/annotation/VSP_027060|||http://purl.uniprot.org/annotation/VSP_027061
http://togogenome.org/gene/9606:BANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||B-cell scaffold protein with ankyrin repeats|||Basic and acidic residues|||DBB|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ITPR2|||May influence susceptibility to SLE.|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251927|||http://purl.uniprot.org/annotation/VAR_027729|||http://purl.uniprot.org/annotation/VAR_027730|||http://purl.uniprot.org/annotation/VAR_027731|||http://purl.uniprot.org/annotation/VSP_020803|||http://purl.uniprot.org/annotation/VSP_020804|||http://purl.uniprot.org/annotation/VSP_020805|||http://purl.uniprot.org/annotation/VSP_034214
http://togogenome.org/gene/9606:PODN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5L7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||Podocan                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262524|||http://purl.uniprot.org/annotation/VAR_029497|||http://purl.uniprot.org/annotation/VAR_029498|||http://purl.uniprot.org/annotation/VSP_021784|||http://purl.uniprot.org/annotation/VSP_037827|||http://purl.uniprot.org/annotation/VSP_039064
http://togogenome.org/gene/9606:MEX3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||KH 1|||KH 2|||Phosphoserine|||Phosphothreonine|||Pro residues|||RING-type|||RNA-binding protein MEX3D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050123|||http://purl.uniprot.org/annotation/VSP_024019|||http://purl.uniprot.org/annotation/VSP_047662
http://togogenome.org/gene/9606:GRPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30550|||http://purl.uniprot.org/uniprot/X5D7H2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Gastrin-releasing peptide receptor|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069662
http://togogenome.org/gene/9606:LCAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK24|||http://purl.uniprot.org/uniprot/P04180                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Decreased enzyme specific activity. Increased PAPC/POPC activity ratio.|||Determinant for substrate specificity|||Found in a patient with intermediate phenotype between LCATD and FED; reduction of activity.|||In FED and LCATD.|||In FED.|||In FED; loss of activity.|||In FED; results in reduced activity.|||In FED; results in reduced protein secretion and activity.|||In LCATD.|||In LCATD; also found in a patient with intermediate phenotype between LCATD and FED; loss of activity.|||In LCATD; partially defective enzyme.|||In a patient with LCATD.|||In a patient with low HDL-cholesterol levels; reduced protein secretion.|||In a patient with low HDL-cholesterol levels; results in reduced activity.|||In a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive.|||Increased activity towards PAPC. Increased PAPC/POPC activity ratio.|||Little change in enzyme specific activity nor in PAPC/POPC activity ratio.|||N-linked (GlcNAc...) (complex) asparagine|||Nucleophile|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphatidylcholine-sterol acyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017802|||http://purl.uniprot.org/annotation/PRO_5007491746|||http://purl.uniprot.org/annotation/VAR_004251|||http://purl.uniprot.org/annotation/VAR_004252|||http://purl.uniprot.org/annotation/VAR_004253|||http://purl.uniprot.org/annotation/VAR_004254|||http://purl.uniprot.org/annotation/VAR_004255|||http://purl.uniprot.org/annotation/VAR_004256|||http://purl.uniprot.org/annotation/VAR_004257|||http://purl.uniprot.org/annotation/VAR_004258|||http://purl.uniprot.org/annotation/VAR_004259|||http://purl.uniprot.org/annotation/VAR_004260|||http://purl.uniprot.org/annotation/VAR_004261|||http://purl.uniprot.org/annotation/VAR_004262|||http://purl.uniprot.org/annotation/VAR_004263|||http://purl.uniprot.org/annotation/VAR_004264|||http://purl.uniprot.org/annotation/VAR_004265|||http://purl.uniprot.org/annotation/VAR_004266|||http://purl.uniprot.org/annotation/VAR_004267|||http://purl.uniprot.org/annotation/VAR_017030|||http://purl.uniprot.org/annotation/VAR_039020|||http://purl.uniprot.org/annotation/VAR_039021|||http://purl.uniprot.org/annotation/VAR_039022|||http://purl.uniprot.org/annotation/VAR_039023|||http://purl.uniprot.org/annotation/VAR_039024|||http://purl.uniprot.org/annotation/VAR_039025|||http://purl.uniprot.org/annotation/VAR_039026|||http://purl.uniprot.org/annotation/VAR_039027|||http://purl.uniprot.org/annotation/VAR_039028|||http://purl.uniprot.org/annotation/VAR_039029|||http://purl.uniprot.org/annotation/VAR_039030|||http://purl.uniprot.org/annotation/VAR_039031|||http://purl.uniprot.org/annotation/VAR_039032|||http://purl.uniprot.org/annotation/VAR_039033|||http://purl.uniprot.org/annotation/VAR_039034|||http://purl.uniprot.org/annotation/VAR_039035|||http://purl.uniprot.org/annotation/VAR_039036|||http://purl.uniprot.org/annotation/VAR_039037|||http://purl.uniprot.org/annotation/VAR_039038|||http://purl.uniprot.org/annotation/VAR_066862|||http://purl.uniprot.org/annotation/VAR_066863|||http://purl.uniprot.org/annotation/VAR_066864|||http://purl.uniprot.org/annotation/VAR_066865|||http://purl.uniprot.org/annotation/VAR_066866|||http://purl.uniprot.org/annotation/VAR_066867|||http://purl.uniprot.org/annotation/VAR_066868
http://togogenome.org/gene/9606:SOCS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14543|||http://purl.uniprot.org/uniprot/Q6FI39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Complete loss of EPO-induced STAT5 signaling suppression. Abolishes binding to JH1.|||Complete loss of EPO-induced STAT5 signaling suppression. No effect on LIF-induced STAT3 signaling. Abolishes binding to JH1.|||Complete loss of EPO-induced STAT5 signaling suppression. No suppression of JAK2 phosphorylation.|||Complete loss of EPO/LIF-induced signaling inhibition. Abolishes binding to JH1.|||Complete loss of EPO/LIF-induced signaling suppression.|||Complete loss of EPO/LIF-induced signaling suppression. No inhibition of JAK2 phosphorylation.|||Disordered|||Extended SH2 subdomain (ESS)|||Greatly impaired binding to Y429/Y431 phosphorylated EPOR.|||Impaired binding to Y429/Y431 phosphorylated EPOR.|||Kinase inhibitory region (KIR)|||Little effect on EPO-induced STAT5 signaling suppression.|||Little effect on EPO-induced signaling suppression.|||Little effect on EPO/LIF signaling.|||No effect on EPO/LIF-induced signaling suppression. Partial suppression of JAK2 phosphorylation. No effect on binding to JH1. Loss of binding to IL12RB2.|||No effect on binding to Y429/Y431 phosphorylated EPOR.|||Partial loss of EPO-induced STAT5 signaling suppression. No effect on LIF-induced signaling suppression. Abolishes binding to JH1. Inhibits JAK2 phosphorylation.|||Pro residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181243|||http://purl.uniprot.org/annotation/VAR_030033
http://togogenome.org/gene/9606:PRDX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30044                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform Cytoplasmic+peroxisomal.|||Loss of antioxidant activity. Loss of S-palmitoylation.|||Loss of antioxidant activity. No change in S-palmitoylation levels.|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No change in antioxidant activity. No change in S-palmitoylation levels.|||Peroxiredoxin-5, mitochondrial|||Phosphoserine|||Redox-active|||S-palmitoyl cysteine|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023793|||http://purl.uniprot.org/annotation/VAR_025049|||http://purl.uniprot.org/annotation/VAR_036406|||http://purl.uniprot.org/annotation/VSP_018829|||http://purl.uniprot.org/annotation/VSP_045783|||http://purl.uniprot.org/annotation/VSP_046682
http://togogenome.org/gene/9606:TCEA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15560|||http://purl.uniprot.org/uniprot/Q6IB64                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Phosphoserine|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121449|||http://purl.uniprot.org/annotation/VSP_047345
http://togogenome.org/gene/9606:REPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFH8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with ASAP1.|||Disordered|||EF-hand|||EH 1|||EH 2|||In isoform 2.|||Interaction with ASAP1|||Interaction with RALBP1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RalBP1-associated Eps domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073831|||http://purl.uniprot.org/annotation/VAR_069419|||http://purl.uniprot.org/annotation/VSP_040086
http://togogenome.org/gene/9606:EHMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCN9|||http://purl.uniprot.org/uniprot/A2ABF8|||http://purl.uniprot.org/uniprot/B7Z852|||http://purl.uniprot.org/uniprot/Q59FM7|||http://purl.uniprot.org/uniprot/Q96KQ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K9me binding|||Histone-lysine N-methyltransferase EHMT2|||Impairs binding to histone H3K9me.|||In isoform 2.|||In isoform 3.|||Interaction with histone H3|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pre-SET|||Removed|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186068|||http://purl.uniprot.org/annotation/VAR_027973|||http://purl.uniprot.org/annotation/VAR_027974|||http://purl.uniprot.org/annotation/VSP_002211|||http://purl.uniprot.org/annotation/VSP_002212|||http://purl.uniprot.org/annotation/VSP_002213
http://togogenome.org/gene/9606:ZNF439                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG37|||http://purl.uniprot.org/uniprot/A0A804HI69|||http://purl.uniprot.org/uniprot/Q8NDP4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 439                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047588|||http://purl.uniprot.org/annotation/VAR_024216|||http://purl.uniprot.org/annotation/VAR_052827
http://togogenome.org/gene/9606:GNAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04899                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||Deamidated glutamine; by Photorhabdus PAU_02230|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-2|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform sGi2.|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203679|||http://purl.uniprot.org/annotation/VSP_017497|||http://purl.uniprot.org/annotation/VSP_043473|||http://purl.uniprot.org/annotation/VSP_043903|||http://purl.uniprot.org/annotation/VSP_054788|||http://purl.uniprot.org/annotation/VSP_054789
http://togogenome.org/gene/9606:RFX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2KHR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-binding protein RFX7|||Disordered|||In isoform 2.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||PxLPxI/L motif; mediates interaction with ANKRA2 and RFXANK|||RFX-type winged-helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342186|||http://purl.uniprot.org/annotation/VAR_044135|||http://purl.uniprot.org/annotation/VAR_044136|||http://purl.uniprot.org/annotation/VAR_044137|||http://purl.uniprot.org/annotation/VSP_034394|||http://purl.uniprot.org/annotation/VSP_061441
http://togogenome.org/gene/9606:RDH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZV5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Transmembrane                                                                                  ^@                                                                                  Helical; Signal-anchor|||Proton acceptor|||Retinol dehydrogenase 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307682
http://togogenome.org/gene/9606:NUTM2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6P9|||http://purl.uniprot.org/uniprot/Q8IVF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NUT family member 2A|||Nuclear Testis protein N-terminal|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266032|||http://purl.uniprot.org/annotation/VSP_034018|||http://purl.uniprot.org/annotation/VSP_034020
http://togogenome.org/gene/9606:MRPL42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6G3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein mL42|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087724
http://togogenome.org/gene/9606:PAGE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||P antigen family member 5|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247361|||http://purl.uniprot.org/annotation/VSP_042547
http://togogenome.org/gene/9606:MAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969L2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||MARVEL|||N-linked (GlcNAc...) asparagine|||Protein MAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156808|||http://purl.uniprot.org/annotation/VAR_050016
http://togogenome.org/gene/9606:LPAR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVQ5|||http://purl.uniprot.org/uniprot/P43657                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In ARWH1 and HYPT8; loss of G protein-coupled receptor signaling; no effect on localization to cell membrane; does not affect protein abundance.|||In ARWH1 and HYPT8; loss of G protein-coupled receptor signaling; reduced localization to cell membrane; decreased protein abundance; increased protein degradation.|||In ARWH1; loss of G protein-coupled receptor signaling; reduced localization to cell membrane; decreased protein abundance; increased protein degradation.|||In HYPT8; loss of G protein-coupled receptor signaling; no effect on localization to cell membrane; does not affect protein abundance.|||In HYPT8; loss of G protein-coupled receptor signaling; reduced localization to cell membrane; decreased protein abundance; increased protein degradation.|||In HYPT8; unknown pathological significance.|||In HYPT8; unknown pathological significance; no effect on G protein-coupled receptor signaling; no effect on localization to cell membrane; does not affect protein abundance.|||Loss of G protein-coupled receptor signaling. Reduced localization to cell membrane. Decreased protein abundance. Increased protein degradation.|||Lysophosphatidic acid receptor 6|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070025|||http://purl.uniprot.org/annotation/VAR_016253|||http://purl.uniprot.org/annotation/VAR_022636|||http://purl.uniprot.org/annotation/VAR_044326|||http://purl.uniprot.org/annotation/VAR_044327|||http://purl.uniprot.org/annotation/VAR_044328|||http://purl.uniprot.org/annotation/VAR_049430|||http://purl.uniprot.org/annotation/VAR_088338|||http://purl.uniprot.org/annotation/VAR_088339|||http://purl.uniprot.org/annotation/VAR_088340|||http://purl.uniprot.org/annotation/VAR_088341|||http://purl.uniprot.org/annotation/VAR_088342|||http://purl.uniprot.org/annotation/VAR_088343
http://togogenome.org/gene/9606:CRISP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54108                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine-rich secretory protein 3|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||SCP|||ShKT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006268|||http://purl.uniprot.org/annotation/VAR_011718|||http://purl.uniprot.org/annotation/VAR_011719|||http://purl.uniprot.org/annotation/VSP_042758|||http://purl.uniprot.org/annotation/VSP_042759
http://togogenome.org/gene/9606:TVP23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QL63|||http://purl.uniprot.org/uniprot/Q9NYZ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Golgi apparatus membrane protein TVP23 homolog|||Golgi apparatus membrane protein TVP23 homolog B|||Helical|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212828|||http://purl.uniprot.org/annotation/PRO_5014098607|||http://purl.uniprot.org/annotation/VAR_060476
http://togogenome.org/gene/9606:APLNR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDH3|||http://purl.uniprot.org/uniprot/B3KQN4|||http://purl.uniprot.org/uniprot/P35414                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Apelin receptor|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069173|||http://purl.uniprot.org/annotation/VAR_049375
http://togogenome.org/gene/9606:SERPINB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36952                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reactive bond homolog|||Serpin B5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032486|||http://purl.uniprot.org/annotation/VAR_022115|||http://purl.uniprot.org/annotation/VAR_055223|||http://purl.uniprot.org/annotation/VAR_055224|||http://purl.uniprot.org/annotation/VSP_037145|||http://purl.uniprot.org/annotation/VSP_037146
http://togogenome.org/gene/9606:PDCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYJ3|||http://purl.uniprot.org/uniprot/Q16342                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||MYND-type|||MYND-type; atypical|||Programmed cell death protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218304|||http://purl.uniprot.org/annotation/VSP_042828|||http://purl.uniprot.org/annotation/VSP_042829|||http://purl.uniprot.org/annotation/VSP_055159|||http://purl.uniprot.org/annotation/VSP_055160|||http://purl.uniprot.org/annotation/VSP_055161|||http://purl.uniprot.org/annotation/VSP_055162
http://togogenome.org/gene/9606:RNF122                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9V4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Helical|||RING finger protein 122|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247852
http://togogenome.org/gene/9606:POLR3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1D9                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  DNA-directed RNA polymerase III subunit RPC6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD101; unknown pathological significance.|||N-acetylalanine|||Removed|||Strongly impaired dsDNA-binding. No effect on interaction with POLR3C.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073972|||http://purl.uniprot.org/annotation/VAR_087291
http://togogenome.org/gene/9606:TMEM94                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9U5|||http://purl.uniprot.org/uniprot/J3QSG7|||http://purl.uniprot.org/uniprot/Q12767                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In IDDCDF.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 94                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050731|||http://purl.uniprot.org/annotation/VAR_019508|||http://purl.uniprot.org/annotation/VAR_081637|||http://purl.uniprot.org/annotation/VSP_011043|||http://purl.uniprot.org/annotation/VSP_060138
http://togogenome.org/gene/9606:DOLPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YN1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Dolichyldiphosphatase 1|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215626|||http://purl.uniprot.org/annotation/VSP_042210
http://togogenome.org/gene/9606:ZFP41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JH32|||http://purl.uniprot.org/uniprot/Q8N8Y5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Zinc finger protein 41 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296186
http://togogenome.org/gene/9606:BTD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43251                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Biotinidase|||CN hydrolase|||In BTD deficiency.|||In BTD deficiency; not detectable protein levels; loss of biotinyl-transferase activity.|||In BTD deficiency; partial.|||In BTD deficiency; profound and partial; 52% decrease in biotinyl-transferase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019707|||http://purl.uniprot.org/annotation/VAR_005113|||http://purl.uniprot.org/annotation/VAR_005114|||http://purl.uniprot.org/annotation/VAR_005115|||http://purl.uniprot.org/annotation/VAR_005116|||http://purl.uniprot.org/annotation/VAR_005117|||http://purl.uniprot.org/annotation/VAR_005118|||http://purl.uniprot.org/annotation/VAR_005119|||http://purl.uniprot.org/annotation/VAR_005120|||http://purl.uniprot.org/annotation/VAR_005121|||http://purl.uniprot.org/annotation/VAR_056238|||http://purl.uniprot.org/annotation/VSP_054925|||http://purl.uniprot.org/annotation/VSP_054926|||http://purl.uniprot.org/annotation/VSP_055921
http://togogenome.org/gene/9606:RRP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14684                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with protein phosphatase PP1 subunits PPP1CB and PPP1CC; when associated with A-684.|||Abolishes interaction with protein phosphatase PP1 subunits PPP1CB and PPP1CC; when associated with A-686.|||Basic and acidic residues|||Citrulline|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosomal RNA processing protein 1 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050729|||http://purl.uniprot.org/annotation/VAR_079135|||http://purl.uniprot.org/annotation/VSP_007801
http://togogenome.org/gene/9606:RGPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYH0|||http://purl.uniprot.org/uniprot/P0DJD1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||Phosphoserine|||Polar residues|||RANBP2-like and GRIP domain-containing protein 2|||RanBD1|||RanBD1 1|||RanBD1 2|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415356
http://togogenome.org/gene/9606:MRPL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0U6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein uL18m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030556|||http://purl.uniprot.org/annotation/VAR_024609
http://togogenome.org/gene/9606:APPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKG1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BAR|||Basic and acidic residues|||DCC-interacting protein 13-alpha|||Decreased interaction with OCRL.|||Disordered|||F&H|||In MODY14; no effect on protein abundance; loss of function in insulin receptor signaling pathway.|||In a breast cancer sample; somatic mutation.|||PH|||PID|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Required for RAB5A binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079985|||http://purl.uniprot.org/annotation/VAR_035909|||http://purl.uniprot.org/annotation/VAR_050958|||http://purl.uniprot.org/annotation/VAR_050959|||http://purl.uniprot.org/annotation/VAR_075857
http://togogenome.org/gene/9606:HDAC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUI4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  6000 fold increase in deacetylase activity.|||Abolishes nuclear export; when associated with A-155; A-358 and A-486.|||Abolishes nuclear export; when associated with A-181; A-358 and A-486. Abolishes phosphorylation by MARK2 and MARK3, interaction with 14-3-3 and localization to the cytoplasm.|||Abolishes nuclear export; when associated with A-192; A-1118 and A-358.|||Abolishes nuclear export; when associated with A-192; A-1118 and A-486.|||Abolishes phosphorylation at S-155.|||Basic and acidic residues|||Contributes to catalysis|||Disordered|||Enhanced deacetylase activity.|||Histone deacetylase|||Histone deacetylase 7|||In a breast cancer sample; somatic mutation.|||In isoform 10.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||Interaction with MEF2A|||Interaction with MEF2C|||Interaction with SIN3A|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by MARK2, MARK3 and PKD/PRKD1|||Phosphoserine; by PKD/PRKD1|||Phosphoserine; by PKD/PRKD2|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription repression 1|||Transcription repression 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114705|||http://purl.uniprot.org/annotation/VAR_036043|||http://purl.uniprot.org/annotation/VSP_007429|||http://purl.uniprot.org/annotation/VSP_007430|||http://purl.uniprot.org/annotation/VSP_007431|||http://purl.uniprot.org/annotation/VSP_008772|||http://purl.uniprot.org/annotation/VSP_038102|||http://purl.uniprot.org/annotation/VSP_038103|||http://purl.uniprot.org/annotation/VSP_038104|||http://purl.uniprot.org/annotation/VSP_038105|||http://purl.uniprot.org/annotation/VSP_038106|||http://purl.uniprot.org/annotation/VSP_038107
http://togogenome.org/gene/9606:RPL27A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46776                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  (3S)-3-hydroxyhistidine|||Basic residues|||Disordered|||Large ribosomal subunit protein uL15|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000104879
http://togogenome.org/gene/9606:TMEM183A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Transmembrane protein 183A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089251|||http://purl.uniprot.org/annotation/VAR_023205|||http://purl.uniprot.org/annotation/VAR_023206|||http://purl.uniprot.org/annotation/VSP_015084
http://togogenome.org/gene/9606:EFHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C19                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand domain-containing protein D2|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073645
http://togogenome.org/gene/9606:C10orf67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYJ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrion|||Polar residues|||Uncharacterized protein C10orf67, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089800|||http://purl.uniprot.org/annotation/VSP_058394|||http://purl.uniprot.org/annotation/VSP_058395
http://togogenome.org/gene/9606:VPS4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN37                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with CHMP1B; diminishes interaction with IST1.|||Abolishes interaction with CHMP6, no effect on interaction with CHMP1A.|||Defective in ATP-binding. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol sorting. Inhibits HIV-1 release. Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with D-64. Greatly diminishes localization to punctate class E compartments; when associated with D-173.|||Defective in ATP-hydrolysis. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol and protein sorting. Inhibits HIV-1 release. Increases binding to CHMP1.|||Diminishes interaction with CHMP1B.|||Diminishes interaction with IST1.|||Disordered|||Found in a patient with a CIMDAG-like intellectual disability syndrome; unknown pathological significance.|||Found in a patient with non-specific intellectual disability; unknown pathological significance.|||Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with Q-173.|||Greatly diminishes localization to punctate class E compartments; when associated with Q-173.|||Impairs HIV-1 release.|||In CIMDAG.|||In CIMDAG; has a dominant negative effect on the regulation of endosomal size resulting in enlarged endosomal vacuoles; patient cells also have abnormal nuclear envelope morphology and primary cilium defects; no effect on protein abundance in patient cells.|||In CIMDAG; has a dominant negative effect on the regulation of endosomal size resulting in enlarged endosomal vacuoles; patient cells also have abnormal nuclear envelope morphology and primary cilium defects; no effect on protein abundance in patient cells; patient-derived induced erythroblasts show defective cytokinesis.|||In CIMDAG; patient peripheral red blood cells show abnormal CD71 expression indicating defective endosomal trafficking.|||In CIMDAG; unknown pathological significance.|||Interaction with CHMP1B|||MIT|||Modestly reduces interaction with CHMP6.|||N6-acetyllysine|||Phosphoserine|||Strongly impairs HIV-1 release.|||Vacuolar protein sorting-associated protein 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084765|||http://purl.uniprot.org/annotation/VAR_078655|||http://purl.uniprot.org/annotation/VAR_085594|||http://purl.uniprot.org/annotation/VAR_085595|||http://purl.uniprot.org/annotation/VAR_085596|||http://purl.uniprot.org/annotation/VAR_085597|||http://purl.uniprot.org/annotation/VAR_085598|||http://purl.uniprot.org/annotation/VAR_085599|||http://purl.uniprot.org/annotation/VAR_085600
http://togogenome.org/gene/9606:UBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAN5|||http://purl.uniprot.org/uniprot/Q9NZI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Grh/CP2 DB|||In isoform 2.|||Phosphoserine|||Polar residues|||Upstream-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229026|||http://purl.uniprot.org/annotation/VAR_025730|||http://purl.uniprot.org/annotation/VAR_049294|||http://purl.uniprot.org/annotation/VSP_017730
http://togogenome.org/gene/9606:TXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9ZYJ2|||http://purl.uniprot.org/uniprot/P10599                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Contributes to redox potential value|||Deprotonates C-terminal active site Cys|||In isoform 2.|||Interchain; alternate|||Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32.|||Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35.|||Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-69.|||Loss of pH-dependence of dimerization.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on reducing activity, interaction with APEX1 and on S-nitrosylation of C-73. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-73.|||Nucleophile|||Redox-active|||Removed|||Retains its reducing activity.|||Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73.|||S-nitrosocysteine|||S-nitrosocysteine; alternate|||Strongly reduced S-nitrosylation of CASP3.|||Strongly reduced interaction with CASP3; when associated with A-70.|||Strongly reduced interaction with CASP3; when associated with A-72.|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120005|||http://purl.uniprot.org/annotation/VSP_045607
http://togogenome.org/gene/9606:FNDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6D8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type III domain-containing protein 4|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271379
http://togogenome.org/gene/9606:SLC15A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16348                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Extracellular domain (ECD)|||Helical|||In hPEPT2*2.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Solute carrier family 15 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064308|||http://purl.uniprot.org/annotation/VAR_047001|||http://purl.uniprot.org/annotation/VAR_047002|||http://purl.uniprot.org/annotation/VAR_047003|||http://purl.uniprot.org/annotation/VAR_047004|||http://purl.uniprot.org/annotation/VAR_047005|||http://purl.uniprot.org/annotation/VAR_047006|||http://purl.uniprot.org/annotation/VAR_047008|||http://purl.uniprot.org/annotation/VSP_043084
http://togogenome.org/gene/9606:CDHR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0L2|||http://purl.uniprot.org/uniprot/Q96JP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-related family member 1|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with Joubert syndrome; unknown pathological significance.|||Helical|||In CORD15.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318498|||http://purl.uniprot.org/annotation/PRO_5014303376|||http://purl.uniprot.org/annotation/VAR_038744|||http://purl.uniprot.org/annotation/VAR_038745|||http://purl.uniprot.org/annotation/VAR_038746|||http://purl.uniprot.org/annotation/VAR_038747|||http://purl.uniprot.org/annotation/VAR_075501|||http://purl.uniprot.org/annotation/VAR_080429|||http://purl.uniprot.org/annotation/VAR_083318|||http://purl.uniprot.org/annotation/VSP_031190|||http://purl.uniprot.org/annotation/VSP_031191
http://togogenome.org/gene/9606:TJP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0K9|||http://purl.uniprot.org/uniprot/A9CQZ8|||http://purl.uniprot.org/uniprot/B4DZK4|||http://purl.uniprot.org/uniprot/G5E9E7|||http://purl.uniprot.org/uniprot/Q07157|||http://purl.uniprot.org/uniprot/Q6MZU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CDC42BPB and MYZAP.|||Abolishes interaction with CDC42BPB.|||Abolishes interaction with GJA1.|||Acidic residues|||Actin-binding region (ABR)|||Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform Short.|||Occludin (OCLN)-binding region|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH3|||Strongly reduced interaction with GJA1.|||Tight junction protein ZO-1|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094540|||http://purl.uniprot.org/annotation/VAR_025153|||http://purl.uniprot.org/annotation/VAR_025154|||http://purl.uniprot.org/annotation/VAR_025155|||http://purl.uniprot.org/annotation/VAR_025156|||http://purl.uniprot.org/annotation/VAR_025157|||http://purl.uniprot.org/annotation/VAR_025158|||http://purl.uniprot.org/annotation/VSP_003148
http://togogenome.org/gene/9606:DEGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15121                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In HLD18.|||In HLD18; decreased function in sphingolipid biosynthetic process.|||In HLD18; decreased function in sphingolipid biosynthetic process; reduced protein levels; increased protein degradation.|||In HLD18; unknown pathological significance.|||N-myristoyl glycine|||Phosphoserine|||Removed|||Sphingolipid delta(4)-desaturase DES1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312727|||http://purl.uniprot.org/annotation/VAR_082594|||http://purl.uniprot.org/annotation/VAR_082595|||http://purl.uniprot.org/annotation/VAR_082596|||http://purl.uniprot.org/annotation/VAR_082597|||http://purl.uniprot.org/annotation/VAR_082598|||http://purl.uniprot.org/annotation/VAR_082599|||http://purl.uniprot.org/annotation/VAR_082600|||http://purl.uniprot.org/annotation/VAR_082601|||http://purl.uniprot.org/annotation/VAR_082602|||http://purl.uniprot.org/annotation/VAR_082603
http://togogenome.org/gene/9606:IL4R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBY1|||http://purl.uniprot.org/uniprot/P24394                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold reduction in IL4 binding.|||100-fold reduction in IL4 binding.|||200-fold reduction in IL4 binding.|||25-fold reduction in IL4 binding.|||35-fold reduction in IL4 binding.|||40-fold reduction in IL4 binding.|||45-fold reduction in IL4 binding.|||50-fold reduction in IL4 binding.|||500-fold reduction in IL4 binding.|||700-fold reduction in IL4 binding.|||>150-fold reduction in IL4 binding.|||Abolishes IRS1 tyrosine phosphorylation. No cell proliferation.|||Associated with atopic asthma and cedar pollen sensitization.|||Associated with atopic dermatitis; lowered total IgE concentration; no effect on IL4-induced signal transduction.|||Associated with cedar pollen sensitization.|||Basic and acidic residues|||Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||ITIM motif|||In 1.8% of the population.|||In isoform 2.|||In isoform 3.|||Increased IL4-induced cell proliferation and STAT6 activation.|||Interleukin-4 receptor subunit alpha|||Little effect on IL4 binding.|||Loss of CD23 gene induction; when associated with F-575 and F-603.|||Loss of CD23 gene induction; when associated with F-575 and F-631.|||Loss of CD23 gene induction; when associated with F-603 and F-631.|||Lowered total IgE concentration.|||Major IL4 binding determinant|||Minor IL4 binding determinant|||N-linked (GlcNAc...) asparagine|||No effect on IL4 binding.|||Phosphotyrosine|||Polar residues|||Required for IL4-induced gene expression|||Required for IRS1 activation and IL4-induced cell growth|||Soluble interleukin-4 receptor subunit alpha|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010887|||http://purl.uniprot.org/annotation/PRO_0000010888|||http://purl.uniprot.org/annotation/PRO_5002779564|||http://purl.uniprot.org/annotation/VAR_008034|||http://purl.uniprot.org/annotation/VAR_008035|||http://purl.uniprot.org/annotation/VAR_011657|||http://purl.uniprot.org/annotation/VAR_011658|||http://purl.uniprot.org/annotation/VAR_011659|||http://purl.uniprot.org/annotation/VAR_011660|||http://purl.uniprot.org/annotation/VAR_011661|||http://purl.uniprot.org/annotation/VAR_011662|||http://purl.uniprot.org/annotation/VAR_011663|||http://purl.uniprot.org/annotation/VAR_019999|||http://purl.uniprot.org/annotation/VAR_020000|||http://purl.uniprot.org/annotation/VAR_049164|||http://purl.uniprot.org/annotation/VAR_049165|||http://purl.uniprot.org/annotation/VAR_059302|||http://purl.uniprot.org/annotation/VAR_059303|||http://purl.uniprot.org/annotation/VSP_011116|||http://purl.uniprot.org/annotation/VSP_011117|||http://purl.uniprot.org/annotation/VSP_053738
http://togogenome.org/gene/9606:ALX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15699|||http://purl.uniprot.org/uniprot/V9HWA7                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  ALX homeobox protein 1|||Homeobox|||N6-acetyllysine; by EP300|||OAR|||Phosphoserine|||Transactivation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048855
http://togogenome.org/gene/9606:ERN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75460                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ability to homodimerize.|||Cytoplasmic|||Disordered|||Helical|||Impaired ability to homodimerize.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Interacts with hydroxy-aryl-aldehyde inhibitors|||KEN|||Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on dimerization. No effect on interaction with P4HB; when associated with S-148 and S-332.|||No effect on dimerization. Weakens dimer; when associated with S-148. No effect on interaction with P4HB; when associated with S-109 and S-148.|||No effect on dimerization. Weakens dimer; when associated with S-332. Abolishes interaction with PDIA6. Prolonged splicing of XBP1, probably due to prolonged activation of PDIA6. Inhibits formation of oxidized multimeric forms of ERN1 in response to ER stress. No effect on interaction with P4HB; when associated with S-109 and S-332.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase/endoribonuclease IRE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024327|||http://purl.uniprot.org/annotation/VAR_040488|||http://purl.uniprot.org/annotation/VAR_040489|||http://purl.uniprot.org/annotation/VAR_040490|||http://purl.uniprot.org/annotation/VAR_040491|||http://purl.uniprot.org/annotation/VAR_040492|||http://purl.uniprot.org/annotation/VAR_040493|||http://purl.uniprot.org/annotation/VAR_040494|||http://purl.uniprot.org/annotation/VSP_034582|||http://purl.uniprot.org/annotation/VSP_034583
http://togogenome.org/gene/9606:PITPNM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5C9|||http://purl.uniprot.org/uniprot/Q9BZ71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDHD|||Disordered|||In CORD5.|||In isoform 2.|||In isoform 3.|||Membrane-associated phosphatidylinositol transfer protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232743|||http://purl.uniprot.org/annotation/VAR_026014|||http://purl.uniprot.org/annotation/VAR_046787|||http://purl.uniprot.org/annotation/VAR_062132|||http://purl.uniprot.org/annotation/VSP_017965|||http://purl.uniprot.org/annotation/VSP_046060
http://togogenome.org/gene/9606:LEPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48357|||http://purl.uniprot.org/uniprot/Q4G138                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Greatly reduced PTPN11 binding; no PTPN11 phosphorylation; no effect on STAT3 phosphorylation.|||Helical|||Ig-like|||In LEPRD; unknown pathological significance.|||In isoform A.|||In isoform C.|||In isoform D.|||In isoform E.|||Leptin receptor|||Leptin-binding|||N-linked (GlcNAc...) asparagine|||No effect on PTPN11 nor STAT3 phosphorylation.|||No effect on PTPN11 phosphorylation; no STAT3 phosphorylation.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by JAK2|||Required for JAK2 activation|||Required for STAT3 phosphorylation|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010904|||http://purl.uniprot.org/annotation/VAR_002703|||http://purl.uniprot.org/annotation/VAR_002704|||http://purl.uniprot.org/annotation/VAR_002705|||http://purl.uniprot.org/annotation/VAR_002706|||http://purl.uniprot.org/annotation/VAR_002707|||http://purl.uniprot.org/annotation/VAR_028201|||http://purl.uniprot.org/annotation/VAR_049167|||http://purl.uniprot.org/annotation/VAR_049168|||http://purl.uniprot.org/annotation/VAR_075723|||http://purl.uniprot.org/annotation/VAR_075724|||http://purl.uniprot.org/annotation/VAR_075725|||http://purl.uniprot.org/annotation/VSP_001688|||http://purl.uniprot.org/annotation/VSP_001689|||http://purl.uniprot.org/annotation/VSP_001690|||http://purl.uniprot.org/annotation/VSP_001691|||http://purl.uniprot.org/annotation/VSP_001692|||http://purl.uniprot.org/annotation/VSP_001693|||http://purl.uniprot.org/annotation/VSP_001694
http://togogenome.org/gene/9606:GRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14416                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs interaction with HTR2A.|||Important for interaction with HTR2A|||Metabotropic glutamate receptor 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012925
http://togogenome.org/gene/9606:SPANXD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Polar residues|||Sperm protein associated with the nucleus on the X chromosome D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189552|||http://purl.uniprot.org/annotation/VAR_034516
http://togogenome.org/gene/9606:OR1D5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVQ6|||http://purl.uniprot.org/uniprot/P58170                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1D5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150422
http://togogenome.org/gene/9606:ZNF507                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCN5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||Phosphoserine|||Zinc finger protein 507                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047625|||http://purl.uniprot.org/annotation/VSP_035357|||http://purl.uniprot.org/annotation/VSP_035358
http://togogenome.org/gene/9606:CALB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK08|||http://purl.uniprot.org/uniprot/A6NER6|||http://purl.uniprot.org/uniprot/P22676                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Calretinin|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073479
http://togogenome.org/gene/9606:SRSF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13247                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes regulatory effect of DYRK1A on alternative splicing of MAPT/Tau exon 10.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform SRP55-2.|||In isoform SRP55-3.|||N6-acetyllysine|||No effect on regulation of alternative splicing of MAPT/Tau exon 10 by DYRK1A.|||Phosphoserine|||Phosphoserine; by DYRK1A|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081930|||http://purl.uniprot.org/annotation/VAR_035489|||http://purl.uniprot.org/annotation/VSP_005869|||http://purl.uniprot.org/annotation/VSP_005870|||http://purl.uniprot.org/annotation/VSP_005871
http://togogenome.org/gene/9606:PTBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95758                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1, isoform 2 and isoform 6.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 4.|||In isoform 7.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polypyrimidine tract-binding protein 3|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081873|||http://purl.uniprot.org/annotation/VSP_010867|||http://purl.uniprot.org/annotation/VSP_010868|||http://purl.uniprot.org/annotation/VSP_035985|||http://purl.uniprot.org/annotation/VSP_035986|||http://purl.uniprot.org/annotation/VSP_045608
http://togogenome.org/gene/9606:SLC12A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXP2|||http://purl.uniprot.org/uniprot/Q9H7I6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amino acid permease/ SLC12A|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||SLC12A transporter C-terminal|||Solute carrier family 12 member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331415|||http://purl.uniprot.org/annotation/VSP_033192|||http://purl.uniprot.org/annotation/VSP_033193|||http://purl.uniprot.org/annotation/VSP_033194|||http://purl.uniprot.org/annotation/VSP_045591|||http://purl.uniprot.org/annotation/VSP_045592
http://togogenome.org/gene/9606:FOXR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein R1|||Found in a patient with a severe neurological disorder; unknown pathological significance; reduced protein expression due to protein instability; protein misfolding; formation of nuclear puncta in some cells; loss of activation of HSPA1A, HSPA6 and DHRS2.|||In isoform 2.|||Polar residues|||Reduced protein expression and formation of nuclear puncta in some cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253778|||http://purl.uniprot.org/annotation/VAR_086656|||http://purl.uniprot.org/annotation/VSP_056600|||http://purl.uniprot.org/annotation/VSP_056601
http://togogenome.org/gene/9606:FNTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49356                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for selectivity against geranylgeranyl diphosphate|||In isoform 2.|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||Phosphothreonine|||Protein farnesyltransferase subunit beta|||Reduced catalytic efficiency.|||Removes the steric hindrance that normally precludes geranylgeranyl diphosphate binding. Reduces farnesyltransferase activity and confers geranylgeranyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119761|||http://purl.uniprot.org/annotation/VSP_054657
http://togogenome.org/gene/9606:CHD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3L8U1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A.T hook-like|||Basic and acidic residues|||Binds A/T-rich DNA|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 9|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2 and isoform 3.|||In isoform 3.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233172|||http://purl.uniprot.org/annotation/VAR_047355|||http://purl.uniprot.org/annotation/VSP_018085|||http://purl.uniprot.org/annotation/VSP_018086
http://togogenome.org/gene/9606:EGLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVT0|||http://purl.uniprot.org/uniprot/F8W1G2|||http://purl.uniprot.org/uniprot/Q3T1B0|||http://purl.uniprot.org/uniprot/Q9H6Z9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with ADRB2 and no increase in cellular abundance of ADRB2.|||Beta(2)beta(3) 'finger-like' loop|||Eliminates hydroxylase activity.|||Fe2OG dioxygenase|||Prolyl hydroxylase EGLN3|||Required for interaction with ADRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206666|||http://purl.uniprot.org/annotation/VAR_050449|||http://purl.uniprot.org/annotation/VAR_050450
http://togogenome.org/gene/9606:PDGFRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15198                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like C2-type 1|||Ig-like C2-type 2|||In CRC; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor receptor-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233090|||http://purl.uniprot.org/annotation/VAR_026052
http://togogenome.org/gene/9606:ICOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53QY6|||http://purl.uniprot.org/uniprot/Q9Y6W8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin V-set|||In isoform 2.|||Inducible T-cell costimulator|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014806|||http://purl.uniprot.org/annotation/PRO_5014309549|||http://purl.uniprot.org/annotation/VSP_010788
http://togogenome.org/gene/9606:KRTAP10-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60372                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||33|||34|||35|||36|||36 X 5 AA repeats of C-C-X(3)|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185212|||http://purl.uniprot.org/annotation/VAR_017694|||http://purl.uniprot.org/annotation/VAR_017695|||http://purl.uniprot.org/annotation/VAR_062112
http://togogenome.org/gene/9606:ADAMTS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNA0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 5|||Basic and acidic residues|||C-linked (Man) tryptophan|||Cleavage; by furin and PCSK7|||Complete loss of catalytic activity.|||Cysteine switch|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029170|||http://purl.uniprot.org/annotation/PRO_0000029171|||http://purl.uniprot.org/annotation/VAR_021849|||http://purl.uniprot.org/annotation/VAR_028199|||http://purl.uniprot.org/annotation/VAR_028200
http://togogenome.org/gene/9606:OR2J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWS4|||http://purl.uniprot.org/uniprot/O76002                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-6*02 and allele 6M1-6*03.|||In allele 6M1-6*03.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2J2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150483|||http://purl.uniprot.org/annotation/VAR_010945|||http://purl.uniprot.org/annotation/VAR_010946|||http://purl.uniprot.org/annotation/VAR_010947|||http://purl.uniprot.org/annotation/VAR_010948
http://togogenome.org/gene/9606:HERC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVU3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3.|||Probable E3 ubiquitin-protein ligase HERC6|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278219|||http://purl.uniprot.org/annotation/VAR_051725|||http://purl.uniprot.org/annotation/VAR_051726|||http://purl.uniprot.org/annotation/VAR_051727|||http://purl.uniprot.org/annotation/VAR_051728|||http://purl.uniprot.org/annotation/VSP_023183|||http://purl.uniprot.org/annotation/VSP_023184|||http://purl.uniprot.org/annotation/VSP_023185
http://togogenome.org/gene/9606:CYP2E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05181                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2E1|||In allele CYP2E1*2; reduced activity.|||In allele CYP2E1*3.|||In allele CYP2E1*4.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051751|||http://purl.uniprot.org/annotation/VAR_008360|||http://purl.uniprot.org/annotation/VAR_008361|||http://purl.uniprot.org/annotation/VAR_008362|||http://purl.uniprot.org/annotation/VAR_024727|||http://purl.uniprot.org/annotation/VAR_055382|||http://purl.uniprot.org/annotation/VAR_055383
http://togogenome.org/gene/9606:USP17L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUK1                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331647
http://togogenome.org/gene/9606:ASIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16515                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acid-sensing ion channel 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181290|||http://purl.uniprot.org/annotation/VAR_052036|||http://purl.uniprot.org/annotation/VSP_015590|||http://purl.uniprot.org/annotation/VSP_015591
http://togogenome.org/gene/9606:SLC5A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92911                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In TDH1.|||Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.|||Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.|||Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.|||Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.|||N-linked (GlcNAc...) asparagine|||No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.|||Phosphoserine; by PKA|||Required for homodimerization|||Requires 2 nucleotide substitutions.|||Significant loss of iodide transport activity but no effect on its localization to the cell membrane.|||Sodium/iodide cotransporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105383|||http://purl.uniprot.org/annotation/VAR_010263|||http://purl.uniprot.org/annotation/VAR_010264|||http://purl.uniprot.org/annotation/VAR_010265|||http://purl.uniprot.org/annotation/VAR_010266|||http://purl.uniprot.org/annotation/VAR_010267|||http://purl.uniprot.org/annotation/VAR_010268|||http://purl.uniprot.org/annotation/VAR_010269|||http://purl.uniprot.org/annotation/VAR_010270|||http://purl.uniprot.org/annotation/VAR_052490
http://togogenome.org/gene/9606:VAMP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95183|||http://purl.uniprot.org/uniprot/Q6FG93                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 5|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206733
http://togogenome.org/gene/9606:GADD45B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75293                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Growth arrest and DNA damage-inducible protein GADD45 beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148334
http://togogenome.org/gene/9606:FAM72A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TYM5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Loss of UNG-binding.|||Protein FAM72A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340256|||http://purl.uniprot.org/annotation/VSP_034205
http://togogenome.org/gene/9606:SIGLEC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL06|||http://purl.uniprot.org/uniprot/E9PL79|||http://purl.uniprot.org/uniprot/Q96LC7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to PTPN6.|||Cytoplasmic|||Disordered|||Disrupts interaction with CD24.|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2, isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 3, isoform 6 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Sialic acid-binding Ig-like lectin 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014950|||http://purl.uniprot.org/annotation/PRO_5002867162|||http://purl.uniprot.org/annotation/PRO_5003245315|||http://purl.uniprot.org/annotation/VAR_019955|||http://purl.uniprot.org/annotation/VAR_019956|||http://purl.uniprot.org/annotation/VSP_002561|||http://purl.uniprot.org/annotation/VSP_002562|||http://purl.uniprot.org/annotation/VSP_002563|||http://purl.uniprot.org/annotation/VSP_002564|||http://purl.uniprot.org/annotation/VSP_002565|||http://purl.uniprot.org/annotation/VSP_045365|||http://purl.uniprot.org/annotation/VSP_045853|||http://purl.uniprot.org/annotation/VSP_045854|||http://purl.uniprot.org/annotation/VSP_045888
http://togogenome.org/gene/9606:IRAK1BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVH5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Interleukin-1 receptor-associated kinase 1-binding protein 1|||Phosphoserine|||Phosphothreonine|||Required for nuclear localization (NLS)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313733
http://togogenome.org/gene/9606:JOSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15040                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Josephin|||Josephin-1|||Loss of deubiquitination activity, no change in subcellular location.|||Nucleophile|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053839|||http://purl.uniprot.org/annotation/VAR_050031
http://togogenome.org/gene/9606:TMT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8H3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N6-adenosine-methyltransferase TMT1A|||Targeting to lipid droplets                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251921|||http://purl.uniprot.org/annotation/VAR_050296
http://togogenome.org/gene/9606:CDK12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYV4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes kinase activity.|||Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 12|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085715|||http://purl.uniprot.org/annotation/VAR_041968|||http://purl.uniprot.org/annotation/VAR_041969|||http://purl.uniprot.org/annotation/VAR_041970|||http://purl.uniprot.org/annotation/VAR_041971|||http://purl.uniprot.org/annotation/VSP_030284|||http://purl.uniprot.org/annotation/VSP_040908|||http://purl.uniprot.org/annotation/VSP_040909|||http://purl.uniprot.org/annotation/VSP_040910
http://togogenome.org/gene/9606:EBF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PEI2|||http://purl.uniprot.org/uniprot/Q7Z5T1|||http://purl.uniprot.org/uniprot/Q9BQW3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C5-type|||Disordered|||IPT/TIG|||In isoform 1.|||Interaction with DNA|||Polar residues|||Transcription factor COE4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107835|||http://purl.uniprot.org/annotation/VSP_026469|||http://purl.uniprot.org/annotation/VSP_026470
http://togogenome.org/gene/9606:SYDE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Pro residues|||Rho GTPase-activating protein SYDE1|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312158|||http://purl.uniprot.org/annotation/VAR_062661|||http://purl.uniprot.org/annotation/VSP_029717
http://togogenome.org/gene/9606:RAD51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06609                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Confers hypersensitivity to hydroxyurea.|||DNA repair protein RAD51 homolog 1|||Disrupts interaction with BRCA2, no effect on homooligomerization, promotes interaction with XPO1 and cytoplasmic localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HhH|||Impaired ubiquitination; when associated with R-58.|||Impaired ubiquitination; when associated with R-64.|||In BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP.|||In FANCR; causes dominant negative loss of function in interstrand cross-link repair; shows high basal DNA-independent ATPase activity; results in decreased DNA binding.|||In FANCR; dominant negative; impaired function in DNA repair via homologous recombination; impaired DNA-binding and formation of nucleoprotein filaments; impaired DNA-dependent ATPase activity; no effect on subcellular location.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with PALB2|||Loss of homooligomerization.|||N-acetylalanine|||Nuclear export signal; masked by the interaction with BRCA2|||Phosphothreonine; by CHEK1|||Phosphotyrosine; by ABL1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122932|||http://purl.uniprot.org/annotation/VAR_010899|||http://purl.uniprot.org/annotation/VAR_076593|||http://purl.uniprot.org/annotation/VAR_076870|||http://purl.uniprot.org/annotation/VSP_005556|||http://purl.uniprot.org/annotation/VSP_041724|||http://purl.uniprot.org/annotation/VSP_041725|||http://purl.uniprot.org/annotation/VSP_043655
http://togogenome.org/gene/9606:MLLT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13015|||http://purl.uniprot.org/uniprot/Q6FGF7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue                                                                                  ^@                                                                                  Constitutive nuclear sequestration.|||Nuclear export signal|||Phosphoserine|||Protein AF1q|||Putative WW-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064471
http://togogenome.org/gene/9606:GAS2L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTH9|||http://purl.uniprot.org/uniprot/G3V1N3|||http://purl.uniprot.org/uniprot/Q86XJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||GAR|||GAS2-like protein 3|||No effect on microtubule localization and MAPRE1 binding; when associated with 373-N-N-374.|||No effect on microtubule localization and MAPRE1 binding; when associated with 461-N-N-462.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190446|||http://purl.uniprot.org/annotation/VAR_033944|||http://purl.uniprot.org/annotation/VAR_033945
http://togogenome.org/gene/9606:LRRTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UE6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane neuronal protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018350|||http://purl.uniprot.org/annotation/VAR_022681
http://togogenome.org/gene/9606:CNGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29973                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C-linker|||Cyclic nucleotide-binding domain (CNBD)|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=S1|||Helical; Name=S2|||Helical; Name=S3|||Helical; Name=S4|||Helical; Name=S5|||Helical; Name=S6|||In RP49.|||N-linked (GlcNAc...) asparagine|||P-helix|||Selectivity filter|||cGMP-gated cation channel alpha-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219308|||http://purl.uniprot.org/annotation/VAR_009295|||http://purl.uniprot.org/annotation/VAR_009296|||http://purl.uniprot.org/annotation/VAR_009297|||http://purl.uniprot.org/annotation/VAR_047385
http://togogenome.org/gene/9606:NEBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76041|||http://purl.uniprot.org/uniprot/Q59FZ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Higher frequency of homozygotes in a cohort of non-familial cardiomyopathy Japanese patients as compared to healthy controls.|||In isoform 2.|||LIM zinc-binding|||Linker|||Nebulette|||Nebulin 1|||Nebulin 10|||Nebulin 11|||Nebulin 12|||Nebulin 13|||Nebulin 14|||Nebulin 15|||Nebulin 16|||Nebulin 17|||Nebulin 18|||Nebulin 19|||Nebulin 2|||Nebulin 20|||Nebulin 21|||Nebulin 22|||Nebulin 23|||Nebulin 3|||Nebulin 4|||Nebulin 5|||Nebulin 6|||Nebulin 7|||Nebulin 8|||Nebulin 9|||Omega-N-methylarginine|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096774|||http://purl.uniprot.org/annotation/VAR_010289|||http://purl.uniprot.org/annotation/VAR_010290|||http://purl.uniprot.org/annotation/VAR_010291|||http://purl.uniprot.org/annotation/VAR_010292|||http://purl.uniprot.org/annotation/VAR_021887|||http://purl.uniprot.org/annotation/VAR_051229|||http://purl.uniprot.org/annotation/VSP_043816|||http://purl.uniprot.org/annotation/VSP_043817|||http://purl.uniprot.org/annotation/VSP_043818
http://togogenome.org/gene/9606:ALPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09923                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated aspartate|||Intestinal-type alkaline phosphatase|||N-linked (GlcNAc...) asparagine|||Phosphoserine intermediate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024037|||http://purl.uniprot.org/annotation/PRO_0000024038|||http://purl.uniprot.org/annotation/VAR_011816|||http://purl.uniprot.org/annotation/VAR_050524
http://togogenome.org/gene/9606:PHF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFV6|||http://purl.uniprot.org/uniprot/Q86YI8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Interaction with trimethylated histone H3 (H3K4)|||Nuclear localization signal|||PHD finger protein 13|||PHD-type|||Polar residues|||Zinc finger PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059304|||http://purl.uniprot.org/annotation/VAR_055285
http://togogenome.org/gene/9606:CETN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG3|||http://purl.uniprot.org/uniprot/Q12798                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Centrin-1|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073559
http://togogenome.org/gene/9606:TMEM208                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KRY7|||http://purl.uniprot.org/uniprot/Q9BTX3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-acetylmethionine|||Transmembrane protein 208                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325967|||http://purl.uniprot.org/annotation/VAR_039958|||http://purl.uniprot.org/annotation/VAR_053933|||http://purl.uniprot.org/annotation/VSP_032505
http://togogenome.org/gene/9606:PLXNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51805                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-A3|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024670|||http://purl.uniprot.org/annotation/VAR_050595|||http://purl.uniprot.org/annotation/VAR_050596|||http://purl.uniprot.org/annotation/VAR_050597|||http://purl.uniprot.org/annotation/VAR_083660
http://togogenome.org/gene/9606:NT5C3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969T7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  7-methylguanosine phosphate-specific 5'-nucleotidase|||In isoform 2.|||N6-acetyllysine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328948|||http://purl.uniprot.org/annotation/VAR_042582|||http://purl.uniprot.org/annotation/VAR_042583|||http://purl.uniprot.org/annotation/VSP_046297
http://togogenome.org/gene/9606:MNAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R688|||http://purl.uniprot.org/uniprot/P51948                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  CDK-activating kinase assembly factor MAT1|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RING-type|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055932|||http://purl.uniprot.org/annotation/VAR_052084|||http://purl.uniprot.org/annotation/VSP_046772
http://togogenome.org/gene/9606:DENR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43583                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Density-regulated protein|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||SUI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130600
http://togogenome.org/gene/9606:UFSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NVU6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Inactive Ufm1-specific protease 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280360|||http://purl.uniprot.org/annotation/VAR_031125
http://togogenome.org/gene/9606:NOMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15155                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BOS complex subunit NOMO1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021819|||http://purl.uniprot.org/annotation/VAR_011496|||http://purl.uniprot.org/annotation/VAR_013312|||http://purl.uniprot.org/annotation/VAR_013313|||http://purl.uniprot.org/annotation/VAR_013314|||http://purl.uniprot.org/annotation/VAR_013315|||http://purl.uniprot.org/annotation/VAR_013316|||http://purl.uniprot.org/annotation/VAR_022551|||http://purl.uniprot.org/annotation/VAR_056956|||http://purl.uniprot.org/annotation/VAR_060370
http://togogenome.org/gene/9606:OR10R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGX6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10R2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150715|||http://purl.uniprot.org/annotation/VAR_054355|||http://purl.uniprot.org/annotation/VAR_054356|||http://purl.uniprot.org/annotation/VAR_054357
http://togogenome.org/gene/9606:NMRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWW6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost no effect.|||In isoform 2.|||Loss of activity.|||Nicotinamide riboside kinase 1|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215891|||http://purl.uniprot.org/annotation/VSP_012676
http://togogenome.org/gene/9606:UNC45B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWX7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||In CTRCT43.|||In MFM11; mislocated away from the A-band to the Z-disk.|||In MFM11; unknown pathological significance; mislocated away from the A-band to the Z-disk.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Protein unc-45 homolog B|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249892|||http://purl.uniprot.org/annotation/VAR_027506|||http://purl.uniprot.org/annotation/VAR_027507|||http://purl.uniprot.org/annotation/VAR_035870|||http://purl.uniprot.org/annotation/VAR_052630|||http://purl.uniprot.org/annotation/VAR_052631|||http://purl.uniprot.org/annotation/VAR_073375|||http://purl.uniprot.org/annotation/VAR_085393|||http://purl.uniprot.org/annotation/VAR_085394|||http://purl.uniprot.org/annotation/VAR_085395|||http://purl.uniprot.org/annotation/VSP_020586|||http://purl.uniprot.org/annotation/VSP_020587
http://togogenome.org/gene/9606:ARL6IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15041                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 6-interacting protein 1|||Cytoplasmic|||Helical|||In SPG61; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064655|||http://purl.uniprot.org/annotation/VAR_082139|||http://purl.uniprot.org/annotation/VSP_057297|||http://purl.uniprot.org/annotation/VSP_057298
http://togogenome.org/gene/9606:SLC35B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78383                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Helical|||In isoform 2.|||Loss of ATP:ADP antiporter activity.|||Phosphoserine|||Solute carrier family 35 member B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213366|||http://purl.uniprot.org/annotation/VAR_023778|||http://purl.uniprot.org/annotation/VSP_054234
http://togogenome.org/gene/9606:SRD5A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8P0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Loss of function.|||Lumenal|||Polyprenol reductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317703
http://togogenome.org/gene/9606:DMRTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Doublesex- and mab-3-related transcription factor C1|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244102|||http://purl.uniprot.org/annotation/VSP_019519
http://togogenome.org/gene/9606:ITCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J02                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase Itchy homolog|||Glycyl thioester intermediate|||Greatly reduced phosphorylation on T-cell stimulation and in the presence of FYN. Increased ITCH-mediated Ub conjugation and degradation of JUNB.|||HECT|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of ubiquitin protein ligase activity. Results in altered endosomal sorting and reduced degradation of CXCR4. Unable to inhibit MAVS-induced activation of INFB.|||MAP kinase docking site|||N-acetylserine|||No effect on phosphorylation on T-cell stimulation nor in the presence of FYN.|||Phosphoserine; by MAPK8|||Phosphoserine; by SGK3|||Phosphothreonine; by MAPK8|||Phosphothreonine; by SGK3|||Phosphotyrosine; by FYN|||Polar residues|||Pro residues|||Removed|||Required for interaction with FYN|||WW 1|||WW 2|||WW 3|||WW 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120317|||http://purl.uniprot.org/annotation/VSP_008451|||http://purl.uniprot.org/annotation/VSP_044732
http://togogenome.org/gene/9606:ENTPD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MY95                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 8|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306882|||http://purl.uniprot.org/annotation/VAR_035339|||http://purl.uniprot.org/annotation/VAR_061385|||http://purl.uniprot.org/annotation/VSP_028559
http://togogenome.org/gene/9606:ZNF268                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6T9|||http://purl.uniprot.org/uniprot/K7EQP6|||http://purl.uniprot.org/uniprot/Q14587|||http://purl.uniprot.org/uniprot/Q2TB61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||KRAB|||Polar residues|||Reduces nuclear localization.|||Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-94.|||Reduces nuclear localization. Inhibits nuclear localization; when associated with A-93 and A-95.|||Reduces nuclear localization. Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-85.|||Reduces nuclear localization. Strongly reduces nuclear localization; when associated with A-94 and A-95.|||Strongly reduces nuclear localization and interaction with TRIM28; when associated with A-86.|||Zinc finger protein 268                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047495|||http://purl.uniprot.org/annotation/VAR_033562|||http://purl.uniprot.org/annotation/VSP_006909|||http://purl.uniprot.org/annotation/VSP_053461|||http://purl.uniprot.org/annotation/VSP_053462|||http://purl.uniprot.org/annotation/VSP_053463|||http://purl.uniprot.org/annotation/VSP_053464|||http://purl.uniprot.org/annotation/VSP_053465|||http://purl.uniprot.org/annotation/VSP_053466|||http://purl.uniprot.org/annotation/VSP_053467|||http://purl.uniprot.org/annotation/VSP_053468|||http://purl.uniprot.org/annotation/VSP_053469|||http://purl.uniprot.org/annotation/VSP_053470|||http://purl.uniprot.org/annotation/VSP_053471
http://togogenome.org/gene/9606:C3orf18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZP18|||http://purl.uniprot.org/uniprot/Q9UK00                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Uncharacterized protein C3orf18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228841|||http://purl.uniprot.org/annotation/VAR_025720|||http://purl.uniprot.org/annotation/VAR_025721|||http://purl.uniprot.org/annotation/VSP_044880
http://togogenome.org/gene/9606:STK33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS39|||http://purl.uniprot.org/uniprot/B4DDH2|||http://purl.uniprot.org/uniprot/F8WAK5|||http://purl.uniprot.org/uniprot/Q9BYT3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232644|||http://purl.uniprot.org/annotation/VAR_041172|||http://purl.uniprot.org/annotation/VAR_041173|||http://purl.uniprot.org/annotation/VAR_041174|||http://purl.uniprot.org/annotation/VAR_041175|||http://purl.uniprot.org/annotation/VAR_041176|||http://purl.uniprot.org/annotation/VAR_061746|||http://purl.uniprot.org/annotation/VSP_017939
http://togogenome.org/gene/9606:KCNK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14649                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Greatly reduces pH sensitivity.|||Helical|||In PPH4; loss of function.|||In PPH4; loss of function; channel activity can be rescued with the use of the phospholipase A2 inhibitor ONO-RS-082.|||In PPH4; loss of function; channel activity cannot be rescued with the use of the phospholipase A2 inhibitor ONO-RS-082.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101744|||http://purl.uniprot.org/annotation/VAR_070126|||http://purl.uniprot.org/annotation/VAR_070127|||http://purl.uniprot.org/annotation/VAR_070128|||http://purl.uniprot.org/annotation/VAR_070129|||http://purl.uniprot.org/annotation/VAR_070130|||http://purl.uniprot.org/annotation/VAR_070131
http://togogenome.org/gene/9606:SMPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXE4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In NEDMABA.|||In NEDMABA; unknown pathological significance.|||In isoform 10.|||In isoform 2, isoform 6, isoform 8 and isoform 10.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||No effect on endoplasmic reticulum location.|||Phosphoserine|||Phosphothreonine|||Sphingomyelin phosphodiesterase 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273163|||http://purl.uniprot.org/annotation/VAR_083329|||http://purl.uniprot.org/annotation/VAR_083330|||http://purl.uniprot.org/annotation/VAR_083331|||http://purl.uniprot.org/annotation/VAR_083332|||http://purl.uniprot.org/annotation/VAR_083333|||http://purl.uniprot.org/annotation/VAR_083334|||http://purl.uniprot.org/annotation/VSP_022479|||http://purl.uniprot.org/annotation/VSP_022480|||http://purl.uniprot.org/annotation/VSP_022481|||http://purl.uniprot.org/annotation/VSP_022482|||http://purl.uniprot.org/annotation/VSP_022483|||http://purl.uniprot.org/annotation/VSP_044495|||http://purl.uniprot.org/annotation/VSP_054382|||http://purl.uniprot.org/annotation/VSP_054383|||http://purl.uniprot.org/annotation/VSP_054384|||http://purl.uniprot.org/annotation/VSP_054385|||http://purl.uniprot.org/annotation/VSP_054386|||http://purl.uniprot.org/annotation/VSP_055343
http://togogenome.org/gene/9606:CHAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUX2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Glutathione-specific gamma-glutamylcyclotransferase 2|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314912|||http://purl.uniprot.org/annotation/VAR_038123
http://togogenome.org/gene/9606:LNP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4G5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Leukemia NUP98 fusion partner 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341357
http://togogenome.org/gene/9606:FUT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K737|||http://purl.uniprot.org/uniprot/P21217                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3|||Cytoplasmic|||Disordered|||Fucosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||In Le(+).|||In Le(-).|||In Le(-); Loss of alpha (1,3/1,4)fucosyltransferase activity..|||In Le(-); about 20% of alpha (1,3/1,4)fucosyltransferase activity.|||In Le(-); completely inactive.|||In Le(-); less than 10% reduction in activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221096|||http://purl.uniprot.org/annotation/VAR_003426|||http://purl.uniprot.org/annotation/VAR_003427|||http://purl.uniprot.org/annotation/VAR_003428|||http://purl.uniprot.org/annotation/VAR_003429|||http://purl.uniprot.org/annotation/VAR_003430|||http://purl.uniprot.org/annotation/VAR_007959|||http://purl.uniprot.org/annotation/VAR_007960|||http://purl.uniprot.org/annotation/VAR_007961|||http://purl.uniprot.org/annotation/VAR_007962|||http://purl.uniprot.org/annotation/VAR_007963|||http://purl.uniprot.org/annotation/VAR_007964|||http://purl.uniprot.org/annotation/VAR_022200|||http://purl.uniprot.org/annotation/VAR_022201|||http://purl.uniprot.org/annotation/VAR_022202|||http://purl.uniprot.org/annotation/VAR_022203
http://togogenome.org/gene/9606:PRSS58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYP2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317763
http://togogenome.org/gene/9606:ROS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08922                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form GOPC-ROS1 fusion protein|||Breakpoint for translocation to form SLC34A2-ROS1 and CD74-ROS1 fusion proteins|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Helical|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||Loss of kinase activity.|||Loss of phosphorylation at Y-2274 and loss of interaction with PTPN11.|||Loss of phosphorylation at Y-2334 and loss of interaction with PTPN11.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proto-oncogene tyrosine-protein kinase ROS|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016722|||http://purl.uniprot.org/annotation/VAR_030648|||http://purl.uniprot.org/annotation/VAR_030649|||http://purl.uniprot.org/annotation/VAR_030650|||http://purl.uniprot.org/annotation/VAR_030651|||http://purl.uniprot.org/annotation/VAR_030652|||http://purl.uniprot.org/annotation/VAR_030653|||http://purl.uniprot.org/annotation/VAR_030654|||http://purl.uniprot.org/annotation/VAR_030655|||http://purl.uniprot.org/annotation/VAR_030656|||http://purl.uniprot.org/annotation/VAR_030657|||http://purl.uniprot.org/annotation/VAR_041442|||http://purl.uniprot.org/annotation/VAR_041443|||http://purl.uniprot.org/annotation/VAR_041444|||http://purl.uniprot.org/annotation/VAR_041445|||http://purl.uniprot.org/annotation/VAR_041446|||http://purl.uniprot.org/annotation/VAR_041447|||http://purl.uniprot.org/annotation/VAR_041448|||http://purl.uniprot.org/annotation/VAR_041449|||http://purl.uniprot.org/annotation/VAR_041450|||http://purl.uniprot.org/annotation/VAR_041451|||http://purl.uniprot.org/annotation/VAR_041452|||http://purl.uniprot.org/annotation/VAR_041453|||http://purl.uniprot.org/annotation/VAR_041454|||http://purl.uniprot.org/annotation/VAR_041455|||http://purl.uniprot.org/annotation/VAR_041456|||http://purl.uniprot.org/annotation/VAR_041457|||http://purl.uniprot.org/annotation/VAR_041458|||http://purl.uniprot.org/annotation/VAR_041459|||http://purl.uniprot.org/annotation/VAR_041460|||http://purl.uniprot.org/annotation/VAR_049712|||http://purl.uniprot.org/annotation/VAR_049713
http://togogenome.org/gene/9606:VWF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04275                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amino-terminal|||CTCK|||CX|||Cell attachment site|||E1|||E2|||Exhibits increased in susceptibility to proteolysis by ADAMTS13.|||In VWD1 and VWD3; defect in secretion and formation of multimers.|||In VWD1; reduced secretion of homodimers and heterodimers with wild type VWD and increased degradation by the proteasome.|||In VWD2.|||In VWD2; Normandy type.|||In VWD2; subtype 2A.|||In VWD3.|||In VWD3; likely benign variant.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Or C-1899 with C-1942|||Reduced secretion and increased intracellular retention. Similar phenotype; when associated with R-1149.|||Reduced secretion and increased intracellular retention. Similar phenotype; when associated with S-1169.|||TIL 1|||TIL 2|||TIL 3|||TIL 4|||VWFA 1; binding site for platelet glycoprotein Ib|||VWFA 2|||VWFA 3; main binding site for collagens type I and III|||VWFC 1|||VWFC 2|||VWFC 3|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4|||von Willebrand antigen 2|||von Willebrand factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022682|||http://purl.uniprot.org/annotation/PRO_0000022683|||http://purl.uniprot.org/annotation/VAR_005782|||http://purl.uniprot.org/annotation/VAR_005783|||http://purl.uniprot.org/annotation/VAR_005784|||http://purl.uniprot.org/annotation/VAR_005785|||http://purl.uniprot.org/annotation/VAR_005786|||http://purl.uniprot.org/annotation/VAR_005787|||http://purl.uniprot.org/annotation/VAR_005788|||http://purl.uniprot.org/annotation/VAR_005789|||http://purl.uniprot.org/annotation/VAR_005790|||http://purl.uniprot.org/annotation/VAR_005791|||http://purl.uniprot.org/annotation/VAR_005792|||http://purl.uniprot.org/annotation/VAR_005793|||http://purl.uniprot.org/annotation/VAR_005794|||http://purl.uniprot.org/annotation/VAR_005795|||http://purl.uniprot.org/annotation/VAR_005796|||http://purl.uniprot.org/annotation/VAR_005797|||http://purl.uniprot.org/annotation/VAR_005798|||http://purl.uniprot.org/annotation/VAR_005799|||http://purl.uniprot.org/annotation/VAR_005800|||http://purl.uniprot.org/annotation/VAR_005801|||http://purl.uniprot.org/annotation/VAR_005802|||http://purl.uniprot.org/annotation/VAR_005803|||http://purl.uniprot.org/annotation/VAR_005804|||http://purl.uniprot.org/annotation/VAR_005805|||http://purl.uniprot.org/annotation/VAR_005806|||http://purl.uniprot.org/annotation/VAR_005807|||http://purl.uniprot.org/annotation/VAR_005808|||http://purl.uniprot.org/annotation/VAR_005809|||http://purl.uniprot.org/annotation/VAR_005810|||http://purl.uniprot.org/annotation/VAR_005811|||http://purl.uniprot.org/annotation/VAR_005812|||http://purl.uniprot.org/annotation/VAR_005813|||http://purl.uniprot.org/annotation/VAR_005814|||http://purl.uniprot.org/annotation/VAR_005815|||http://purl.uniprot.org/annotation/VAR_005816|||http://purl.uniprot.org/annotation/VAR_005817|||http://purl.uniprot.org/annotation/VAR_005818|||http://purl.uniprot.org/annotation/VAR_005819|||http://purl.uniprot.org/annotation/VAR_005820|||http://purl.uniprot.org/annotation/VAR_005821|||http://purl.uniprot.org/annotation/VAR_005822|||http://purl.uniprot.org/annotation/VAR_009141|||http://purl.uniprot.org/annotation/VAR_009142|||http://purl.uniprot.org/annotation/VAR_009143|||http://purl.uniprot.org/annotation/VAR_009144|||http://purl.uniprot.org/annotation/VAR_010242|||http://purl.uniprot.org/annotation/VAR_014630|||http://purl.uniprot.org/annotation/VAR_024553|||http://purl.uniprot.org/annotation/VAR_028446|||http://purl.uniprot.org/annotation/VAR_029656|||http://purl.uniprot.org/annotation/VAR_036276|||http://purl.uniprot.org/annotation/VAR_057023|||http://purl.uniprot.org/annotation/VAR_057024|||http://purl.uniprot.org/annotation/VAR_057025|||http://purl.uniprot.org/annotation/VAR_057026|||http://purl.uniprot.org/annotation/VAR_057027|||http://purl.uniprot.org/annotation/VAR_057028|||http://purl.uniprot.org/annotation/VAR_060591|||http://purl.uniprot.org/annotation/VAR_064925|||http://purl.uniprot.org/annotation/VAR_067340|||http://purl.uniprot.org/annotation/VSP_056527|||http://purl.uniprot.org/annotation/VSP_056528|||http://purl.uniprot.org/annotation/VSP_056529
http://togogenome.org/gene/9606:G6PC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35575                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glucose-6-phosphatase catalytic subunit 1|||Helical|||In GSD1A.|||In GSD1A; complete loss of activity.|||In GSD1A; complete loss of glucose-6-phosphatase activity and reduced enzyme stability.|||In GSD1A; complete loss of glucose-6-phosphatase activity.|||In GSD1A; complete loss of glucose-6-phosphatase activity; prevalent mutation in Ashkenazi Jewish population.|||In GSD1A; loss of catalytic activity.|||In GSD1A; loss of catalytic glucose-6-phosphatase activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of glucose-6-phosphatase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Partial loss of glucose-6-phosphatase activity.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087413|||http://purl.uniprot.org/annotation/VAR_005237|||http://purl.uniprot.org/annotation/VAR_005238|||http://purl.uniprot.org/annotation/VAR_005239|||http://purl.uniprot.org/annotation/VAR_005240|||http://purl.uniprot.org/annotation/VAR_005241|||http://purl.uniprot.org/annotation/VAR_005242|||http://purl.uniprot.org/annotation/VAR_005243|||http://purl.uniprot.org/annotation/VAR_005244|||http://purl.uniprot.org/annotation/VAR_005245|||http://purl.uniprot.org/annotation/VAR_005246|||http://purl.uniprot.org/annotation/VAR_005247|||http://purl.uniprot.org/annotation/VAR_005248|||http://purl.uniprot.org/annotation/VAR_005249|||http://purl.uniprot.org/annotation/VAR_005250|||http://purl.uniprot.org/annotation/VAR_005251|||http://purl.uniprot.org/annotation/VAR_005252|||http://purl.uniprot.org/annotation/VAR_005253|||http://purl.uniprot.org/annotation/VAR_005254|||http://purl.uniprot.org/annotation/VAR_009202|||http://purl.uniprot.org/annotation/VAR_009203|||http://purl.uniprot.org/annotation/VAR_009204|||http://purl.uniprot.org/annotation/VAR_009205|||http://purl.uniprot.org/annotation/VAR_009206|||http://purl.uniprot.org/annotation/VAR_009207|||http://purl.uniprot.org/annotation/VAR_035922|||http://purl.uniprot.org/annotation/VAR_046249|||http://purl.uniprot.org/annotation/VAR_046250|||http://purl.uniprot.org/annotation/VAR_046251|||http://purl.uniprot.org/annotation/VAR_046252|||http://purl.uniprot.org/annotation/VAR_046253|||http://purl.uniprot.org/annotation/VAR_046254|||http://purl.uniprot.org/annotation/VAR_046255|||http://purl.uniprot.org/annotation/VAR_046256|||http://purl.uniprot.org/annotation/VAR_046257|||http://purl.uniprot.org/annotation/VAR_046258|||http://purl.uniprot.org/annotation/VAR_046259|||http://purl.uniprot.org/annotation/VAR_046260|||http://purl.uniprot.org/annotation/VAR_046261|||http://purl.uniprot.org/annotation/VAR_046262|||http://purl.uniprot.org/annotation/VAR_046263|||http://purl.uniprot.org/annotation/VAR_046264|||http://purl.uniprot.org/annotation/VAR_046265|||http://purl.uniprot.org/annotation/VAR_046266|||http://purl.uniprot.org/annotation/VAR_046268|||http://purl.uniprot.org/annotation/VAR_046269|||http://purl.uniprot.org/annotation/VAR_046270|||http://purl.uniprot.org/annotation/VAR_046271|||http://purl.uniprot.org/annotation/VAR_046272|||http://purl.uniprot.org/annotation/VAR_046273|||http://purl.uniprot.org/annotation/VAR_046274|||http://purl.uniprot.org/annotation/VAR_046275|||http://purl.uniprot.org/annotation/VAR_046276|||http://purl.uniprot.org/annotation/VAR_046277|||http://purl.uniprot.org/annotation/VAR_046278|||http://purl.uniprot.org/annotation/VAR_065164|||http://purl.uniprot.org/annotation/VAR_065165|||http://purl.uniprot.org/annotation/VSP_047558|||http://purl.uniprot.org/annotation/VSP_047559
http://togogenome.org/gene/9606:CLEC10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KR22|||http://purl.uniprot.org/uniprot/Q8IUN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 10 member A|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046639|||http://purl.uniprot.org/annotation/VAR_021262|||http://purl.uniprot.org/annotation/VAR_050113|||http://purl.uniprot.org/annotation/VAR_050114|||http://purl.uniprot.org/annotation/VAR_050115|||http://purl.uniprot.org/annotation/VSP_012848|||http://purl.uniprot.org/annotation/VSP_012849|||http://purl.uniprot.org/annotation/VSP_012850|||http://purl.uniprot.org/annotation/VSP_012851
http://togogenome.org/gene/9606:ACADM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z366|||http://purl.uniprot.org/uniprot/B4DJE7|||http://purl.uniprot.org/uniprot/B7Z9I1|||http://purl.uniprot.org/uniprot/P11310|||http://purl.uniprot.org/uniprot/Q5HYG7|||http://purl.uniprot.org/uniprot/Q5T4U5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Changed substrate specificity towards longer acyl chains; when associated with E-280.|||In ACADMD.|||In ACADMD; may alter splicing; decreased fatty acid beta-oxidation.|||In ACADMD; mild or benign clinical phenotype.|||In ACADMD; mild.|||In ACADMD; the thermostability is markedly decreased.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of acyl-CoA dehydrogenase activity.|||Loss of acyl-CoA dehydrogenase activity; when associated with E-280.|||Loss of electron transfer to ETF.|||Medium-chain specific acyl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.|||Phosphothreonine|||Proton acceptor|||Reduces rate of electron transfer to ETF about six-fold.|||Reduces rate of electron transfer to ETF three-fold.|||Reduces rate of electron transfer to ETF two-fold.|||Strongly reduced rate of electron transfer to ETF.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000502|||http://purl.uniprot.org/annotation/VAR_000317|||http://purl.uniprot.org/annotation/VAR_000318|||http://purl.uniprot.org/annotation/VAR_000319|||http://purl.uniprot.org/annotation/VAR_000320|||http://purl.uniprot.org/annotation/VAR_000321|||http://purl.uniprot.org/annotation/VAR_000322|||http://purl.uniprot.org/annotation/VAR_000323|||http://purl.uniprot.org/annotation/VAR_000324|||http://purl.uniprot.org/annotation/VAR_000325|||http://purl.uniprot.org/annotation/VAR_000326|||http://purl.uniprot.org/annotation/VAR_000327|||http://purl.uniprot.org/annotation/VAR_013698|||http://purl.uniprot.org/annotation/VAR_013699|||http://purl.uniprot.org/annotation/VAR_013700|||http://purl.uniprot.org/annotation/VAR_015954|||http://purl.uniprot.org/annotation/VAR_015955|||http://purl.uniprot.org/annotation/VAR_015956|||http://purl.uniprot.org/annotation/VAR_015957|||http://purl.uniprot.org/annotation/VAR_015958|||http://purl.uniprot.org/annotation/VAR_015959|||http://purl.uniprot.org/annotation/VAR_035716|||http://purl.uniprot.org/annotation/VSP_038420
http://togogenome.org/gene/9606:CYB5R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K237|||http://purl.uniprot.org/uniprot/Q6BCY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FAD-binding FR-type|||In isoform 2.|||N6-acetyllysine|||NADH-cytochrome b5 reductase 2|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287548|||http://purl.uniprot.org/annotation/VAR_032321|||http://purl.uniprot.org/annotation/VAR_032322|||http://purl.uniprot.org/annotation/VSP_025559
http://togogenome.org/gene/9606:NXPE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N323                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||NXPE family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307930|||http://purl.uniprot.org/annotation/VAR_036712|||http://purl.uniprot.org/annotation/VAR_036713|||http://purl.uniprot.org/annotation/VSP_028872
http://togogenome.org/gene/9606:ZYG11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WRX3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||Protein zyg-11 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305085|||http://purl.uniprot.org/annotation/VSP_028223
http://togogenome.org/gene/9606:ZNF705D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CH99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||KRAB|||Zinc finger protein 705D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332236
http://togogenome.org/gene/9606:MUC20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N307                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12 X 20 AA approximate tandem repeats of S-S-E-S-S-A-S-S-D-S-P-H-P-V-I-T-P-S-R-A|||12; approximate|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||In isoform 2.|||Interaction with MET|||Involved in oligomerization|||Mucin-20|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317469|||http://purl.uniprot.org/annotation/VAR_038536|||http://purl.uniprot.org/annotation/VAR_038537|||http://purl.uniprot.org/annotation/VAR_038538|||http://purl.uniprot.org/annotation/VAR_038539|||http://purl.uniprot.org/annotation/VAR_038540|||http://purl.uniprot.org/annotation/VAR_038541|||http://purl.uniprot.org/annotation/VAR_054139|||http://purl.uniprot.org/annotation/VAR_054140|||http://purl.uniprot.org/annotation/VAR_054141|||http://purl.uniprot.org/annotation/VAR_054142|||http://purl.uniprot.org/annotation/VAR_054143|||http://purl.uniprot.org/annotation/VAR_056641|||http://purl.uniprot.org/annotation/VSP_030980
http://togogenome.org/gene/9606:H3C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:DCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU60                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Leads to reduced autophagosome formation under autophagy-inducing conditions.|||Leads to the accumulation of autophagosomes under normal growth conditions.|||Loss of decapping activity; when associated with Q-148.|||Nudix box|||Nudix hydrolase|||Phosphoserine|||Polar residues|||Strongly reduced decapping activity.|||m7GpppN-mRNA hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057051|||http://purl.uniprot.org/annotation/VAR_059528|||http://purl.uniprot.org/annotation/VSP_012908
http://togogenome.org/gene/9606:OR1N2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW94|||http://purl.uniprot.org/uniprot/Q8NGR9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150449|||http://purl.uniprot.org/annotation/VAR_048028|||http://purl.uniprot.org/annotation/VAR_048029|||http://purl.uniprot.org/annotation/VAR_048030|||http://purl.uniprot.org/annotation/VAR_062012
http://togogenome.org/gene/9606:PDAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13442                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  28 kDa heat- and acid-stable phosphoprotein|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083897
http://togogenome.org/gene/9606:ZNF761                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ01|||http://purl.uniprot.org/uniprot/Q86XN6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 761                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306880|||http://purl.uniprot.org/annotation/VAR_035335|||http://purl.uniprot.org/annotation/VAR_035336|||http://purl.uniprot.org/annotation/VAR_035337|||http://purl.uniprot.org/annotation/VAR_035338|||http://purl.uniprot.org/annotation/VAR_080210
http://togogenome.org/gene/9606:TBC1D3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431604
http://togogenome.org/gene/9606:ZNF280A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JN84|||http://purl.uniprot.org/uniprot/P59817                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Polar residues|||Zinc finger protein 280A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047055|||http://purl.uniprot.org/annotation/VAR_028218|||http://purl.uniprot.org/annotation/VAR_028219|||http://purl.uniprot.org/annotation/VAR_028220|||http://purl.uniprot.org/annotation/VAR_028221|||http://purl.uniprot.org/annotation/VAR_028222|||http://purl.uniprot.org/annotation/VAR_028223|||http://purl.uniprot.org/annotation/VAR_028224|||http://purl.uniprot.org/annotation/VAR_028225|||http://purl.uniprot.org/annotation/VAR_028226
http://togogenome.org/gene/9606:SNAPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95295                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Interaction with TOR1A|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphotyrosine|||Removed|||SNARE-associated protein Snapin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097556|||http://purl.uniprot.org/annotation/VAR_017423
http://togogenome.org/gene/9606:VTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WY55|||http://purl.uniprot.org/uniprot/Q9NP79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with CHMP5|||Interaction with IST1|||Interaction with VPS4B|||N-acetylalanine|||Polar residues|||Removed|||Vacuolar protein sorting-associated protein VTA1 homolog|||Vta1 C-terminal|||Vta1/callose synthase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089509|||http://purl.uniprot.org/annotation/VAR_053917|||http://purl.uniprot.org/annotation/VSP_056727|||http://purl.uniprot.org/annotation/VSP_056728
http://togogenome.org/gene/9606:AUH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13825                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes RNA-binding; when associated with E-109 and Q-113.|||Abolishes RNA-binding; when associated with N-105 and E-109.|||Abolishes RNA-binding; when associated with N-105 and Q-113.|||In MGCA1; decreased methylglutaconyl-CoA hydratase activity.|||In isoform 2.|||Methylglutaconyl-CoA hydratase, mitochondrial|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||RNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007415|||http://purl.uniprot.org/annotation/VAR_016911|||http://purl.uniprot.org/annotation/VSP_008336
http://togogenome.org/gene/9606:NID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14543                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||NIDO|||Nidogen G2 beta-barrel|||Nidogen-1|||O-linked (GalNAc...) threonine|||Sulfotyrosine|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007669|||http://purl.uniprot.org/annotation/VAR_021904|||http://purl.uniprot.org/annotation/VAR_024264|||http://purl.uniprot.org/annotation/VAR_035835|||http://purl.uniprot.org/annotation/VAR_055760|||http://purl.uniprot.org/annotation/VAR_055761|||http://purl.uniprot.org/annotation/VAR_055762|||http://purl.uniprot.org/annotation/VAR_055763|||http://purl.uniprot.org/annotation/VAR_055764|||http://purl.uniprot.org/annotation/VAR_055765|||http://purl.uniprot.org/annotation/VAR_055766|||http://purl.uniprot.org/annotation/VAR_058123|||http://purl.uniprot.org/annotation/VAR_058124|||http://purl.uniprot.org/annotation/VAR_058125|||http://purl.uniprot.org/annotation/VSP_017254
http://togogenome.org/gene/9606:MAFF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULX9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||Disordered|||In isoform 2.|||Leucine-zipper|||Transcription factor MafF|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076497|||http://purl.uniprot.org/annotation/VSP_043029
http://togogenome.org/gene/9606:CABCOCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVU9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Ciliary-associated calcium-binding coiled-coil protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089819
http://togogenome.org/gene/9606:GLIPR1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWM5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GLIPR1-like protein 1|||GPI-anchor amidated glycine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272653|||http://purl.uniprot.org/annotation/PRO_0000441107|||http://purl.uniprot.org/annotation/VSP_022456
http://togogenome.org/gene/9606:TBC1D9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Arginine finger|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||Rab-GAP TBC|||TBC1 domain family member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288499|||http://purl.uniprot.org/annotation/VAR_052539|||http://purl.uniprot.org/annotation/VAR_052540
http://togogenome.org/gene/9606:CLEC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRP6|||http://purl.uniprot.org/uniprot/B4DV89|||http://purl.uniprot.org/uniprot/E7ESV9|||http://purl.uniprot.org/uniprot/E9PFB4|||http://purl.uniprot.org/uniprot/Q8NC01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 1 member A|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046609|||http://purl.uniprot.org/annotation/VAR_050106
http://togogenome.org/gene/9606:TPI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60174|||http://purl.uniprot.org/uniprot/Q53HE2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Electrophile|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In Manchester; thermolabile.|||In TPID.|||In TPID; Hungary; thermolabile.|||In TPID; no effect on triose-phosphate isomerase activity; changed protein homodimerization activity; the homodimer stability is temperature-dependent and affects the triose-phosphate isomerase activity.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed|||Triosephosphate isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090113|||http://purl.uniprot.org/annotation/VAR_007534|||http://purl.uniprot.org/annotation/VAR_007535|||http://purl.uniprot.org/annotation/VAR_007536|||http://purl.uniprot.org/annotation/VAR_007537|||http://purl.uniprot.org/annotation/VAR_007538|||http://purl.uniprot.org/annotation/VAR_007539|||http://purl.uniprot.org/annotation/VAR_007540|||http://purl.uniprot.org/annotation/VAR_007541|||http://purl.uniprot.org/annotation/VSP_060721|||http://purl.uniprot.org/annotation/VSP_060722
http://togogenome.org/gene/9606:RGS21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M5E4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  RGS|||Regulator of G-protein signaling 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271375
http://togogenome.org/gene/9606:BCL2L15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TBC7                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bcl-2-like protein 15|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283003|||http://purl.uniprot.org/annotation/VAR_031475|||http://purl.uniprot.org/annotation/VSP_047627|||http://purl.uniprot.org/annotation/VSP_047628
http://togogenome.org/gene/9606:SLC39A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1S5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Zinc transporter ZIP11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308410|||http://purl.uniprot.org/annotation/VAR_036812|||http://purl.uniprot.org/annotation/VSP_028976
http://togogenome.org/gene/9606:KIAA0319                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0U9|||http://purl.uniprot.org/uniprot/Q5VV43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dyslexia-associated protein KIAA0319|||Endocytosis signal|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with AP2M1 and impaired endocytosis.|||MANSC|||May be associated with susceptibility to dyslexia.|||N-linked (GlcNAc...) asparagine|||PKD 1|||PKD 2|||PKD 3|||PKD 4|||PKD 5|||PKD/Chitinase|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042946|||http://purl.uniprot.org/annotation/VAR_023837|||http://purl.uniprot.org/annotation/VAR_023838|||http://purl.uniprot.org/annotation/VAR_034032|||http://purl.uniprot.org/annotation/VAR_049505|||http://purl.uniprot.org/annotation/VAR_049506|||http://purl.uniprot.org/annotation/VAR_049507|||http://purl.uniprot.org/annotation/VAR_049508|||http://purl.uniprot.org/annotation/VSP_036234|||http://purl.uniprot.org/annotation/VSP_036235|||http://purl.uniprot.org/annotation/VSP_044971
http://togogenome.org/gene/9606:CBFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13951                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form CBF-beta-MYH11 oncogene in AML, subtype M4EO|||Core-binding factor subunit beta|||In CLCD2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058301|||http://purl.uniprot.org/annotation/VAR_036226|||http://purl.uniprot.org/annotation/VAR_087753|||http://purl.uniprot.org/annotation/VSP_036044
http://togogenome.org/gene/9606:MBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 3.|||MBD|||Methyl-CpG-binding domain protein 2|||Phosphoserine|||Required for interaction with DHX9 and PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096260|||http://purl.uniprot.org/annotation/VSP_011077|||http://purl.uniprot.org/annotation/VSP_011078
http://togogenome.org/gene/9606:SEMA4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKS5|||http://purl.uniprot.org/uniprot/Q9H3S1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In RP35 and CORD10; heterozygous compound with C-350; loss of localization to cell membrane.|||In RP35 and CORD10; heterozygous compound with H-345; loss of localization to cell membrane.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on localization to cell membrane.|||PSI|||Sema|||Semaphorin-4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032322|||http://purl.uniprot.org/annotation/VAR_028322|||http://purl.uniprot.org/annotation/VAR_028323|||http://purl.uniprot.org/annotation/VAR_028324|||http://purl.uniprot.org/annotation/VAR_028325|||http://purl.uniprot.org/annotation/VSP_046381|||http://purl.uniprot.org/annotation/VSP_046382
http://togogenome.org/gene/9606:MUS81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53ES5|||http://purl.uniprot.org/uniprot/Q96NY9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Crossover junction endonuclease MUS81|||Disordered|||ERCC4|||Interaction with BLM|||Loss of activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198858|||http://purl.uniprot.org/annotation/VAR_021990|||http://purl.uniprot.org/annotation/VAR_025340|||http://purl.uniprot.org/annotation/VAR_025341|||http://purl.uniprot.org/annotation/VAR_038521|||http://purl.uniprot.org/annotation/VAR_038522|||http://purl.uniprot.org/annotation/VAR_061988
http://togogenome.org/gene/9606:CA14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3J4|||http://purl.uniprot.org/uniprot/Q9ULX7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 14|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004251|||http://purl.uniprot.org/annotation/PRO_5014297539
http://togogenome.org/gene/9606:HNRNPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEJ3|||http://purl.uniprot.org/uniprot/P31943                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||2 X 16 AA Gly-rich approximate repeats|||2 X 19 AA perfect repeats|||2-1|||2-2|||Dimethylated arginine; alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein H|||Heterogeneous nuclear ribonucleoprotein H, N-terminally processed|||In NEDCDS.|||In NEDCDS; unknown pathological significance.|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H, N-terminally processed|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H; alternate|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081857|||http://purl.uniprot.org/annotation/PRO_0000367119|||http://purl.uniprot.org/annotation/VAR_087781|||http://purl.uniprot.org/annotation/VAR_087782|||http://purl.uniprot.org/annotation/VAR_087783
http://togogenome.org/gene/9606:HOXC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31276                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-C13|||In ECTD9; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200197|||http://purl.uniprot.org/annotation/VAR_012357|||http://purl.uniprot.org/annotation/VAR_079380
http://togogenome.org/gene/9606:STX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4C7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Syntaxin-19|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263709
http://togogenome.org/gene/9606:QRICH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0J4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glutamine-rich protein 2|||In SPGF35.|||In SPGF35; the protein is not detected in patient spermatozoa.|||In SPGF35; unknown pathological significance.|||In SPGF35; weak amount of protein detected in patient spermatozoa.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295814|||http://purl.uniprot.org/annotation/VAR_051295|||http://purl.uniprot.org/annotation/VAR_051296|||http://purl.uniprot.org/annotation/VAR_051297|||http://purl.uniprot.org/annotation/VAR_051298|||http://purl.uniprot.org/annotation/VAR_051299|||http://purl.uniprot.org/annotation/VAR_059711|||http://purl.uniprot.org/annotation/VAR_059712|||http://purl.uniprot.org/annotation/VAR_082018|||http://purl.uniprot.org/annotation/VAR_082019|||http://purl.uniprot.org/annotation/VAR_082020|||http://purl.uniprot.org/annotation/VAR_082021|||http://purl.uniprot.org/annotation/VAR_082022|||http://purl.uniprot.org/annotation/VAR_082023|||http://purl.uniprot.org/annotation/VAR_082024|||http://purl.uniprot.org/annotation/VAR_082025|||http://purl.uniprot.org/annotation/VSP_027101|||http://purl.uniprot.org/annotation/VSP_027102|||http://purl.uniprot.org/annotation/VSP_027103
http://togogenome.org/gene/9606:ACTR3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0K3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 3C|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324333|||http://purl.uniprot.org/annotation/VSP_032218
http://togogenome.org/gene/9606:HOXC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31274                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-C9|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200184|||http://purl.uniprot.org/annotation/VAR_036267
http://togogenome.org/gene/9606:DNAJB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75953                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DnaJ homolog subfamily B member 5|||In isoform 2.|||In isoform 3.|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071023|||http://purl.uniprot.org/annotation/VSP_046223|||http://purl.uniprot.org/annotation/VSP_047250
http://togogenome.org/gene/9606:ZCCHC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVL5|||http://purl.uniprot.org/uniprot/B4DU89|||http://purl.uniprot.org/uniprot/G3XAM1|||http://purl.uniprot.org/uniprot/Q8TBK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Disordered|||In isoform 2.|||Polar residues|||Zinc finger CCHC domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150967|||http://purl.uniprot.org/annotation/VSP_013718
http://togogenome.org/gene/9606:FARP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94887                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||FERM|||FERM, ARHGEF and pleckstrin domain-containing protein 2|||In isoform 2.|||In isoform 3.|||PH 1|||PH 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232755|||http://purl.uniprot.org/annotation/VAR_048363|||http://purl.uniprot.org/annotation/VAR_048364|||http://purl.uniprot.org/annotation/VAR_048365|||http://purl.uniprot.org/annotation/VSP_017977|||http://purl.uniprot.org/annotation/VSP_017978|||http://purl.uniprot.org/annotation/VSP_054840|||http://purl.uniprot.org/annotation/VSP_054841
http://togogenome.org/gene/9606:OR4N4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN2|||http://purl.uniprot.org/uniprot/Q8N0Y3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4N4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150564|||http://purl.uniprot.org/annotation/VAR_048034|||http://purl.uniprot.org/annotation/VAR_048035|||http://purl.uniprot.org/annotation/VAR_048036|||http://purl.uniprot.org/annotation/VAR_048037
http://togogenome.org/gene/9606:KIAA1549                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form KIAA1549-BRAF fusion protein|||Disordered|||Helical|||In RP86; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||UPF0606 protein KIAA1549                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342405|||http://purl.uniprot.org/annotation/VAR_044187|||http://purl.uniprot.org/annotation/VAR_044188|||http://purl.uniprot.org/annotation/VAR_057812|||http://purl.uniprot.org/annotation/VAR_083316|||http://purl.uniprot.org/annotation/VSP_034448|||http://purl.uniprot.org/annotation/VSP_040885|||http://purl.uniprot.org/annotation/VSP_040886
http://togogenome.org/gene/9606:FAM13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SG06|||http://purl.uniprot.org/uniprot/A0A8I5KSB9|||http://purl.uniprot.org/uniprot/Q9NYF5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||Protein FAM13B|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058924|||http://purl.uniprot.org/annotation/VAR_049020|||http://purl.uniprot.org/annotation/VSP_042048|||http://purl.uniprot.org/annotation/VSP_044870|||http://purl.uniprot.org/annotation/VSP_044872
http://togogenome.org/gene/9606:UPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNC1|||http://purl.uniprot.org/uniprot/Q9UBR1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-ureidopropionase|||CN hydrolase|||In UPB1D; complete loss of activity.|||In UPB1D; complete loss of activity; abolishes formation of higher oligomers.|||In UPB1D; strongly reduced activity; reduced formation of higher oligomers.|||In UPB1D; unknown pathological significance; mildly reduced enzyme activity; no effect on formation of higher oligomers.|||Loss of catalytic activity.|||Loss of catalytic activity. Forms dimers, but no higher oligomers.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204051|||http://purl.uniprot.org/annotation/VAR_026752|||http://purl.uniprot.org/annotation/VAR_050280|||http://purl.uniprot.org/annotation/VAR_081207|||http://purl.uniprot.org/annotation/VAR_081208|||http://purl.uniprot.org/annotation/VAR_081209|||http://purl.uniprot.org/annotation/VAR_081210|||http://purl.uniprot.org/annotation/VAR_081211|||http://purl.uniprot.org/annotation/VAR_081212|||http://purl.uniprot.org/annotation/VAR_081213|||http://purl.uniprot.org/annotation/VAR_081214
http://togogenome.org/gene/9606:RUVBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNL2|||http://purl.uniprot.org/uniprot/Q9Y230                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Abolishes ATPase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||No effect on interaction with NOPCHAP1.|||Phosphoserine|||Reduces ATPase activity. Decreases interaction with NOPCHAP1. No effect on formation of RUVBL1-RUVBL2 heteromeric complex.|||Removed|||RuvB-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165644|||http://purl.uniprot.org/annotation/VSP_056584
http://togogenome.org/gene/9606:SMIM10L2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMW4|||http://purl.uniprot.org/uniprot/P0DMW5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Small integral membrane protein 10-like protein 2A|||Small integral membrane protein 10-like protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433232|||http://purl.uniprot.org/annotation/PRO_0000433233
http://togogenome.org/gene/9606:OR6X1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVM0|||http://purl.uniprot.org/uniprot/Q8NH79                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6X1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150640|||http://purl.uniprot.org/annotation/VAR_024110
http://togogenome.org/gene/9606:PIK3C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYT4|||http://purl.uniprot.org/uniprot/B4DPV9|||http://purl.uniprot.org/uniprot/Q8NEB9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 3-kinase catalytic subunit type 3|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine; by AMPK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088802
http://togogenome.org/gene/9606:CD86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0X9R4E0|||http://purl.uniprot.org/uniprot/A8K632|||http://purl.uniprot.org/uniprot/P42081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Polar residues|||T-lymphocyte activation antigen CD86                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014550|||http://purl.uniprot.org/annotation/PRO_5002725457|||http://purl.uniprot.org/annotation/PRO_5010056380|||http://purl.uniprot.org/annotation/VAR_014650|||http://purl.uniprot.org/annotation/VAR_021916|||http://purl.uniprot.org/annotation/VAR_021917|||http://purl.uniprot.org/annotation/VAR_055003|||http://purl.uniprot.org/annotation/VSP_009125|||http://purl.uniprot.org/annotation/VSP_023124|||http://purl.uniprot.org/annotation/VSP_040324|||http://purl.uniprot.org/annotation/VSP_047220|||http://purl.uniprot.org/annotation/VSP_047221
http://togogenome.org/gene/9606:THBS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35442                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alters protein stability.|||Basic and acidic residues|||Cell attachment site|||Disordered|||EGF-like 1|||EGF-like 2|||Heparin-binding|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP C-terminal|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-3 1|||TSP type-3 2|||TSP type-3 3|||TSP type-3 4|||TSP type-3 5|||TSP type-3 6|||TSP type-3 7|||TSP type-3 8|||Thrombospondin-2|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035846|||http://purl.uniprot.org/annotation/VAR_045842|||http://purl.uniprot.org/annotation/VAR_045843
http://togogenome.org/gene/9606:DDX19A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DS24|||http://purl.uniprot.org/uniprot/I3L0H8|||http://purl.uniprot.org/uniprot/Q68DY7|||http://purl.uniprot.org/uniprot/Q9NUU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX19A|||C-terminal lobe|||DEAD box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N-acetylalanine|||N-terminal helix|||N-terminal lobe|||Phosphothreonine|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055021|||http://purl.uniprot.org/annotation/VSP_056954
http://togogenome.org/gene/9606:PHF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||Abolishes homodimerization.|||Abolishes interaction with methylated p53.|||Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||In isoform 2.|||Interchain (with C-100)|||Interchain (with C-96)|||N6-acetyllysine|||PHD finger protein 20|||PHD-type|||Phosphoserine|||Polar residues|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059310|||http://purl.uniprot.org/annotation/VAR_051600|||http://purl.uniprot.org/annotation/VSP_007760|||http://purl.uniprot.org/annotation/VSP_007761
http://togogenome.org/gene/9606:PHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSI2|||http://purl.uniprot.org/uniprot/Q8IXK0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with BMI1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 2|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076286|||http://purl.uniprot.org/annotation/VAR_051276|||http://purl.uniprot.org/annotation/VAR_051277|||http://purl.uniprot.org/annotation/VSP_016914|||http://purl.uniprot.org/annotation/VSP_016915|||http://purl.uniprot.org/annotation/VSP_016916|||http://purl.uniprot.org/annotation/VSP_016917|||http://purl.uniprot.org/annotation/VSP_016918|||http://purl.uniprot.org/annotation/VSP_027217|||http://purl.uniprot.org/annotation/VSP_039755
http://togogenome.org/gene/9606:MED19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JLT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 19|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304766|||http://purl.uniprot.org/annotation/VSP_028121|||http://purl.uniprot.org/annotation/VSP_028122
http://togogenome.org/gene/9606:GPX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18283                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Non standard residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutathione peroxidase 2|||Requires 2 nucleotide substitutions.|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066619|||http://purl.uniprot.org/annotation/VAR_003615|||http://purl.uniprot.org/annotation/VAR_003616|||http://purl.uniprot.org/annotation/VAR_020916|||http://purl.uniprot.org/annotation/VAR_020917
http://togogenome.org/gene/9606:REEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3D2|||http://purl.uniprot.org/uniprot/Q9BRK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In SPG72; abolishes REEP2 interaction with membranes; affects correct shaping of the endoplasmic reticulum.|||In SPG72; reduces REEP2 interaction with membranes; affects correct shaping of the endoplasmic reticulum.|||In isoform 2.|||Phosphoserine|||Receptor expression-enhancing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101823|||http://purl.uniprot.org/annotation/VAR_070996|||http://purl.uniprot.org/annotation/VAR_070997|||http://purl.uniprot.org/annotation/VSP_016633
http://togogenome.org/gene/9606:COX7A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0UI06|||http://purl.uniprot.org/uniprot/P14406                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7A2, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006145|||http://purl.uniprot.org/annotation/VAR_012319
http://togogenome.org/gene/9606:SLC39A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05C42|||http://purl.uniprot.org/uniprot/Q9ULF5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc transporter ZIP10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297632|||http://purl.uniprot.org/annotation/PRO_5004164630|||http://purl.uniprot.org/annotation/VAR_034658|||http://purl.uniprot.org/annotation/VSP_055991
http://togogenome.org/gene/9606:THSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTY7|||http://purl.uniprot.org/uniprot/Q9NS62                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In ANIB12; decreased function in endothelial cell-matrix adhesion; decreased interaction with TLN1.|||In ANIB12; loss of function in endothelial cell-matrix adhesion.|||In ANIB12; loss of function in endothelial cell-matrix adhesion; undetectable protein expression.|||In ANIB12; unknown pathological significance; decreased function in endothelial cell-matrix adhesion; decreased interaction with TLN1.|||In ANIB12; unknown pathological significance; loss of function in endothelial cell-matrix adhesion; decreased interaction with TLN1.|||In LMPHM13.|||In LMPHM13; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TSP type-1|||Thrombospondin type-1 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249584|||http://purl.uniprot.org/annotation/PRO_5005662617|||http://purl.uniprot.org/annotation/VAR_027474|||http://purl.uniprot.org/annotation/VAR_027475|||http://purl.uniprot.org/annotation/VAR_027476|||http://purl.uniprot.org/annotation/VAR_061920|||http://purl.uniprot.org/annotation/VAR_083714|||http://purl.uniprot.org/annotation/VAR_083715|||http://purl.uniprot.org/annotation/VAR_083716|||http://purl.uniprot.org/annotation/VAR_083717|||http://purl.uniprot.org/annotation/VAR_083718|||http://purl.uniprot.org/annotation/VAR_083719|||http://purl.uniprot.org/annotation/VAR_083720|||http://purl.uniprot.org/annotation/VAR_083721|||http://purl.uniprot.org/annotation/VAR_088151|||http://purl.uniprot.org/annotation/VAR_088152|||http://purl.uniprot.org/annotation/VAR_088153|||http://purl.uniprot.org/annotation/VSP_020521|||http://purl.uniprot.org/annotation/VSP_020522|||http://purl.uniprot.org/annotation/VSP_020523
http://togogenome.org/gene/9606:CTDSPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D32                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CTD small phosphatase-like protein 2|||Disordered|||FCP1 homology|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331464|||http://purl.uniprot.org/annotation/VAR_042886|||http://purl.uniprot.org/annotation/VSP_033218
http://togogenome.org/gene/9606:TRAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XAN4|||http://purl.uniprot.org/uniprot/Q15629|||http://purl.uniprot.org/uniprot/Q6FHL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TLC|||Translocating chain-associated membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185530|||http://purl.uniprot.org/annotation/VSP_056213
http://togogenome.org/gene/9606:NDUFA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95167|||http://purl.uniprot.org/uniprot/Q6FGG4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118793|||http://purl.uniprot.org/annotation/VAR_036175
http://togogenome.org/gene/9606:STK16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPS1|||http://purl.uniprot.org/uniprot/B8ZZI5|||http://purl.uniprot.org/uniprot/O75716                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Loss of myristoylation.|||Loss of palmitoylation.|||N-myristoyl glycine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||Serine/threonine-protein kinase 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086701|||http://purl.uniprot.org/annotation/VAR_041140|||http://purl.uniprot.org/annotation/VAR_041141|||http://purl.uniprot.org/annotation/VAR_041142|||http://purl.uniprot.org/annotation/VAR_041143|||http://purl.uniprot.org/annotation/VAR_041144
http://togogenome.org/gene/9606:SEMA5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2B3|||http://purl.uniprot.org/uniprot/C9JKR3|||http://purl.uniprot.org/uniprot/Q9P283                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||PSI|||Sema|||Semaphorin-5B|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032337|||http://purl.uniprot.org/annotation/PRO_5002866681|||http://purl.uniprot.org/annotation/PRO_5002996466|||http://purl.uniprot.org/annotation/VAR_037196|||http://purl.uniprot.org/annotation/VAR_037197|||http://purl.uniprot.org/annotation/VAR_037198|||http://purl.uniprot.org/annotation/VAR_037199|||http://purl.uniprot.org/annotation/VAR_037200|||http://purl.uniprot.org/annotation/VAR_037201|||http://purl.uniprot.org/annotation/VAR_037202|||http://purl.uniprot.org/annotation/VSP_029462|||http://purl.uniprot.org/annotation/VSP_029463|||http://purl.uniprot.org/annotation/VSP_029464|||http://purl.uniprot.org/annotation/VSP_029465|||http://purl.uniprot.org/annotation/VSP_044748
http://togogenome.org/gene/9606:CCDC113                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0I3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 113|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279399|||http://purl.uniprot.org/annotation/VAR_030880|||http://purl.uniprot.org/annotation/VAR_030881|||http://purl.uniprot.org/annotation/VSP_042753
http://togogenome.org/gene/9606:STIMATE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||GXXXG motif|||Helical|||Induces relocalization to cell membrane.|||Required for localization in the endoplasmic reticulum|||Store-operated calcium entry regulator STIMATE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243915
http://togogenome.org/gene/9606:HDAC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY41                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of catalytical activity.|||Complete loss of catalytical activity.|||Complete loss of catalytical activity. Complete loss of catalytical activity; when associated with F-306.|||Decreases the deacetylase activity.|||Enhances the deacetylase activity.|||Histone deacetylase|||Histone deacetylase 8|||In CDLS5.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of catalytic activity.|||Loss of catalytic activity. Complete loss of catalytic activity; when associated with A-101.|||Partial loss of catalytical activity.|||Phosphoserine|||Proton acceptor|||Strongly reduces histone deacetylase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114708|||http://purl.uniprot.org/annotation/VAR_069140|||http://purl.uniprot.org/annotation/VAR_069141|||http://purl.uniprot.org/annotation/VAR_069142|||http://purl.uniprot.org/annotation/VAR_069143|||http://purl.uniprot.org/annotation/VSP_007177|||http://purl.uniprot.org/annotation/VSP_043426|||http://purl.uniprot.org/annotation/VSP_043427|||http://purl.uniprot.org/annotation/VSP_046832|||http://purl.uniprot.org/annotation/VSP_046833|||http://purl.uniprot.org/annotation/VSP_046834|||http://purl.uniprot.org/annotation/VSP_046835|||http://purl.uniprot.org/annotation/VSP_046836|||http://purl.uniprot.org/annotation/VSP_047502
http://togogenome.org/gene/9606:IGIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJ69                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  IgA-inducing protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332153
http://togogenome.org/gene/9606:CD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06729|||http://purl.uniprot.org/uniprot/Q53F96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CD58 binding region 1|||CD58 binding region 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||Immunoglobulin C2-set|||Immunoglobulin V-set|||In a breast cancer sample; somatic mutation.|||Loss of CD58 and CD59 binding.|||Loss of CD58 binding.|||N-linked (GlcNAc...) asparagine|||Pro residues|||T-cell surface antigen CD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014600|||http://purl.uniprot.org/annotation/PRO_5014309512|||http://purl.uniprot.org/annotation/VAR_017104|||http://purl.uniprot.org/annotation/VAR_033608|||http://purl.uniprot.org/annotation/VAR_035504
http://togogenome.org/gene/9606:EDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization and RNA binding; when associated with A-306.|||Abolishes homodimerization and RNA binding; when associated with A-310.|||Abolishes interaction with DDX6; when associated with A-204.|||Abolishes interaction with DDX6; when associated with A-206.|||DFDF|||Disordered|||Enhancer of mRNA-decapping protein 3|||In MRT50; does not enhance DCP2 decapping activity.|||Phosphoserine|||Polar residues|||Required for P-body targeting and interaction with DCP1A|||Required for interaction with DDX6|||Sm|||YjeF N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119054|||http://purl.uniprot.org/annotation/VAR_073963
http://togogenome.org/gene/9606:H3C13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71DI3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolishes S-palmitoylation.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.2|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||S-palmitoyl cysteine|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250357|||http://purl.uniprot.org/annotation/VAR_059313|||http://purl.uniprot.org/annotation/VAR_059314
http://togogenome.org/gene/9606:RNASEH2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TBB1|||http://purl.uniprot.org/uniprot/Q8N451                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In AGS2.|||In AGS2; frequent mutation.|||In AGS2; heterozygous compound with T-177.|||In AGS2; heterozygous compound with T-177; reduces stability of the RNase complex.|||In AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex.|||In AGS2; reduces stability of the RNase complex.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||Ribonuclease H2 subunit B|||Ribonuclease H2 subunit B wHTH|||Rnh202 triple barrel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248378|||http://purl.uniprot.org/annotation/VAR_027280|||http://purl.uniprot.org/annotation/VAR_027281|||http://purl.uniprot.org/annotation/VAR_027282|||http://purl.uniprot.org/annotation/VAR_027283|||http://purl.uniprot.org/annotation/VAR_027284|||http://purl.uniprot.org/annotation/VAR_027285|||http://purl.uniprot.org/annotation/VAR_027286|||http://purl.uniprot.org/annotation/VAR_070611|||http://purl.uniprot.org/annotation/VAR_070612|||http://purl.uniprot.org/annotation/VAR_070613|||http://purl.uniprot.org/annotation/VAR_070614|||http://purl.uniprot.org/annotation/VAR_070615|||http://purl.uniprot.org/annotation/VAR_070616|||http://purl.uniprot.org/annotation/VAR_070617|||http://purl.uniprot.org/annotation/VSP_054039|||http://purl.uniprot.org/annotation/VSP_054040
http://togogenome.org/gene/9606:KISS1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969F8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CPPB1; reduced rate of decline in inositol phosphate accumulation after kisspeptin stimulation; prolonged phosphorylation of ERK.|||In HH8.|||In HH8; 65% reduction of inositol phosphate production.|||In HH8; absence of inositol phosphate accumulation under kisspeptin challenge; normal affinity for kisspeptin.|||In HH8; exhibit profoundly impaired signaling.|||In HH8; mild reduction in ligand-stimulated activity across the ligand dose range.|||In HH8; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD.|||In HH8; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; benign variant; the patient also carries a mutation in FGFR1.|||KiSS-1 receptor|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069695|||http://purl.uniprot.org/annotation/VAR_021392|||http://purl.uniprot.org/annotation/VAR_021393|||http://purl.uniprot.org/annotation/VAR_021394|||http://purl.uniprot.org/annotation/VAR_021395|||http://purl.uniprot.org/annotation/VAR_043906|||http://purl.uniprot.org/annotation/VAR_043907|||http://purl.uniprot.org/annotation/VAR_069961|||http://purl.uniprot.org/annotation/VAR_069962|||http://purl.uniprot.org/annotation/VAR_072975
http://togogenome.org/gene/9606:L3HYPDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EM0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Proton acceptor|||Regains racemase activity, catalyzing the conversion of trans-3-hydroxy-L-proline to cis-3-hydroxy-D-proline. Also catalyzes racemization of L-proline to D-proline, albeit at a very low level. Has lost its original dehydratase activity.|||Trans-3-hydroxy-L-proline dehydratase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288949|||http://purl.uniprot.org/annotation/VAR_032540|||http://purl.uniprot.org/annotation/VAR_032541|||http://purl.uniprot.org/annotation/VAR_032542|||http://purl.uniprot.org/annotation/VAR_062192
http://togogenome.org/gene/9606:EHD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9B9|||http://purl.uniprot.org/uniprot/Q9H223                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 4|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146114|||http://purl.uniprot.org/annotation/VAR_053070
http://togogenome.org/gene/9606:SNCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W754|||http://purl.uniprot.org/uniprot/O76070|||http://purl.uniprot.org/uniprot/Q6FHG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3; approximate|||4|||4 X 11 AA tandem repeats of [EGSA]-K-T-K-[EQ]-[GQ]-V-X(4)|||Basic and acidic residues|||Disordered|||Gamma-synuclein|||Phosphoserine|||Phosphoserine; by BARK1, CaMK2 and CK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184038|||http://purl.uniprot.org/annotation/VAR_007455
http://togogenome.org/gene/9606:PPP2R2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66LE6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071433|||http://purl.uniprot.org/annotation/VAR_057127
http://togogenome.org/gene/9606:RBBP8NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||RBBP8 N-terminal-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079470|||http://purl.uniprot.org/annotation/VAR_056849|||http://purl.uniprot.org/annotation/VAR_056850|||http://purl.uniprot.org/annotation/VAR_056851|||http://purl.uniprot.org/annotation/VAR_056852
http://togogenome.org/gene/9606:FAM219B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XKK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Protein FAM219B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243930|||http://purl.uniprot.org/annotation/VSP_019499|||http://purl.uniprot.org/annotation/VSP_019500|||http://purl.uniprot.org/annotation/VSP_036115|||http://purl.uniprot.org/annotation/VSP_036116
http://togogenome.org/gene/9606:ZSCAN5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ1|||http://purl.uniprot.org/uniprot/Q9BUG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 5A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047752|||http://purl.uniprot.org/annotation/VAR_035603|||http://purl.uniprot.org/annotation/VAR_042964|||http://purl.uniprot.org/annotation/VSP_055989|||http://purl.uniprot.org/annotation/VSP_055990
http://togogenome.org/gene/9606:AGR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD06                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Anterior gradient protein 3|||Leads to Golgi localization;.|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001040
http://togogenome.org/gene/9606:TXLNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40222                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Alpha-taxilin|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189421
http://togogenome.org/gene/9606:FGFBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor-binding protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245860|||http://purl.uniprot.org/annotation/VAR_049065|||http://purl.uniprot.org/annotation/VAR_059287|||http://purl.uniprot.org/annotation/VAR_061171
http://togogenome.org/gene/9606:CLEC18C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCF0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 18 member C|||EGF-like|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324317|||http://purl.uniprot.org/annotation/VSP_032206|||http://purl.uniprot.org/annotation/VSP_032207
http://togogenome.org/gene/9606:PHAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSU1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phagosome assembly factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221083|||http://purl.uniprot.org/annotation/VSP_026623|||http://purl.uniprot.org/annotation/VSP_026624|||http://purl.uniprot.org/annotation/VSP_026625
http://togogenome.org/gene/9606:MARCHF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA1|||http://purl.uniprot.org/uniprot/B3KVK0|||http://purl.uniprot.org/uniprot/G3V1Q5|||http://purl.uniprot.org/uniprot/J3KTN9|||http://purl.uniprot.org/uniprot/Q8NA82                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Probable E3 ubiquitin-protein ligase MARCHF10|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261626|||http://purl.uniprot.org/annotation/VAR_029461|||http://purl.uniprot.org/annotation/VAR_029462|||http://purl.uniprot.org/annotation/VAR_029463
http://togogenome.org/gene/9606:PLA2G4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XP0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2|||Cytosolic phospholipase A2 delta|||In isoform 2.|||Nucleophile|||PLA2c|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247023|||http://purl.uniprot.org/annotation/VAR_027049|||http://purl.uniprot.org/annotation/VAR_027050|||http://purl.uniprot.org/annotation/VAR_027051|||http://purl.uniprot.org/annotation/VAR_057676|||http://purl.uniprot.org/annotation/VAR_057677|||http://purl.uniprot.org/annotation/VAR_057678|||http://purl.uniprot.org/annotation/VAR_057679|||http://purl.uniprot.org/annotation/VSP_019881|||http://purl.uniprot.org/annotation/VSP_019882
http://togogenome.org/gene/9606:NUDCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RS6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CS|||In isoform 2.|||In isoform 3.|||NudC domain-containing protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307704|||http://purl.uniprot.org/annotation/VAR_036632|||http://purl.uniprot.org/annotation/VAR_036633|||http://purl.uniprot.org/annotation/VAR_036634|||http://purl.uniprot.org/annotation/VAR_036635|||http://purl.uniprot.org/annotation/VSP_052557|||http://purl.uniprot.org/annotation/VSP_052558|||http://purl.uniprot.org/annotation/VSP_052559|||http://purl.uniprot.org/annotation/VSP_052560
http://togogenome.org/gene/9606:MIOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Inositol oxygenase|||Phosphoserine|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079148|||http://purl.uniprot.org/annotation/VSP_041667|||http://purl.uniprot.org/annotation/VSP_041668
http://togogenome.org/gene/9606:CPNE6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95741                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-6|||In isoform 2.|||Linker region|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144845|||http://purl.uniprot.org/annotation/VSP_054806
http://togogenome.org/gene/9606:AOAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVT3|||http://purl.uniprot.org/uniprot/P28039                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyloxyacyl hydrolase large subunit|||Acyloxyacyl hydrolase small subunit|||Important for enzyme activity, localization to cytoplasmic vesicles, and protein stability|||In isoform 2.|||Interacts with lipopolysaccharide|||Interchain (between small and large subunit)|||Lipopolysaccharide binding|||Loss of enzyme activity with lipopolysaccharide, due to steric hindrance. No effect on activity with small, synthetic substrate.|||Loss of enzyme activity.|||Loss of glycosylation. No effect on enzyme activity or localization to cytoplasmic vesicles.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes catalytic activity.|||No effect on enzyme activity.|||No effect on enzyme activity; when associated with E-345.|||No effect on enzyme activity; when associated with E-379.|||Saposin B-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020739|||http://purl.uniprot.org/annotation/PRO_0000020740|||http://purl.uniprot.org/annotation/PRO_0000020741|||http://purl.uniprot.org/annotation/PRO_5001831983|||http://purl.uniprot.org/annotation/VAR_020133|||http://purl.uniprot.org/annotation/VAR_033513|||http://purl.uniprot.org/annotation/VAR_050663|||http://purl.uniprot.org/annotation/VSP_042571
http://togogenome.org/gene/9606:NAP1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYV1|||http://purl.uniprot.org/uniprot/Q99457                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Nucleosome assembly protein 1-like 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185657|||http://purl.uniprot.org/annotation/VAR_024545
http://togogenome.org/gene/9606:HTRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83110                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes protease activity. Stabilizes the protein.|||Charge relay system|||IGFBP N-terminal|||In isoform 2.|||Kazal-like|||PDZ|||Serine protease|||Serine protease HTRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026949|||http://purl.uniprot.org/annotation/VSP_012570|||http://purl.uniprot.org/annotation/VSP_012571
http://togogenome.org/gene/9606:SCRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75711|||http://purl.uniprot.org/uniprot/Q6FGG5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Scrapie-responsive protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022283|||http://purl.uniprot.org/annotation/PRO_5010141900|||http://purl.uniprot.org/annotation/VAR_020329
http://togogenome.org/gene/9606:H2AZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71UI9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Histone H2A.V|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Monoisotopic, not modified.|||N6-acetyllysine|||N6-lactoyllysine|||N6-lactoyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239068|||http://purl.uniprot.org/annotation/VAR_059312|||http://purl.uniprot.org/annotation/VSP_042855|||http://purl.uniprot.org/annotation/VSP_044633|||http://purl.uniprot.org/annotation/VSP_045232|||http://purl.uniprot.org/annotation/VSP_046783
http://togogenome.org/gene/9606:RIMBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFD9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Polar residues|||Pro residues|||RIMS-binding protein 3A|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259597|||http://purl.uniprot.org/annotation/VAR_028969
http://togogenome.org/gene/9606:ALKBH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P6C2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity with N(6)-methyladenosine in single-stranded DNA.|||Abolishes catalytic activity.|||Abolishes catalytic activity; when associated with A-277.|||Abolishes catalytic activity; when associated with A-283.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired catalytic activity.|||In isoform 1.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||No effect on catalytic activity with N(6)-methyladenosine in single-stranded DNA.|||No effect on catalytic activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||RNA demethylase ALKBH5|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239283|||http://purl.uniprot.org/annotation/VSP_019130|||http://purl.uniprot.org/annotation/VSP_044226
http://togogenome.org/gene/9606:CXorf66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JRM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Uncharacterized protein CXorf66                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348434|||http://purl.uniprot.org/annotation/VAR_046157
http://togogenome.org/gene/9606:ACACB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00763                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-grasp|||Acetyl-CoA carboxylase 2|||Altered regulation of oligomerization by phosphorylation at S-222.|||Biotin carboxylation|||Biotinyl-binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||Disordered|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of regulation of oligomerization by phosphorylation at S-222.|||Mitochondrion|||N6-biotinyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146767|||http://purl.uniprot.org/annotation/VAR_031255|||http://purl.uniprot.org/annotation/VAR_031256|||http://purl.uniprot.org/annotation/VAR_031257|||http://purl.uniprot.org/annotation/VAR_062667|||http://purl.uniprot.org/annotation/VSP_000547|||http://purl.uniprot.org/annotation/VSP_057081|||http://purl.uniprot.org/annotation/VSP_057082
http://togogenome.org/gene/9606:OR11H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWF9|||http://purl.uniprot.org/uniprot/Q8NG94                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150724
http://togogenome.org/gene/9606:VCX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H320                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||10 X 10 AA tandem repeats of L-S-Q-E-S-[EQ]-V-E-E-P|||2|||3|||4|||5|||6|||7|||8|||9|||Basic residues|||Disordered|||Polar residues|||Variable charge X-linked protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184659|||http://purl.uniprot.org/annotation/VAR_070431|||http://purl.uniprot.org/annotation/VAR_070432
http://togogenome.org/gene/9606:EPB41L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCM4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 4.1-like protein 5|||FERM|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Required for interaction with CRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219406|||http://purl.uniprot.org/annotation/VAR_042699|||http://purl.uniprot.org/annotation/VAR_048357|||http://purl.uniprot.org/annotation/VSP_033034|||http://purl.uniprot.org/annotation/VSP_033035|||http://purl.uniprot.org/annotation/VSP_033036|||http://purl.uniprot.org/annotation/VSP_033037|||http://purl.uniprot.org/annotation/VSP_033038
http://togogenome.org/gene/9606:SLURP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP57                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Secreted Ly-6/uPAR domain-containing protein 2|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440646
http://togogenome.org/gene/9606:GPC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y625                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated serine|||Glypican-6|||Polar residues|||Removed in mature form|||Secreted glypican-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012323|||http://purl.uniprot.org/annotation/PRO_0000012324|||http://purl.uniprot.org/annotation/PRO_0000333851|||http://purl.uniprot.org/annotation/VAR_024229
http://togogenome.org/gene/9606:KCNJ6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48051                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 2|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In KPLBS.|||PDZ-binding|||Phosphoserine|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154942|||http://purl.uniprot.org/annotation/VAR_073430|||http://purl.uniprot.org/annotation/VAR_073431
http://togogenome.org/gene/9606:EID2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D98                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||EP300-interacting inhibitor of differentiation 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315903
http://togogenome.org/gene/9606:POU5F1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06416                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||POU-specific|||Phosphoserine|||Phosphothreonine|||Polar residues|||Putative POU domain, class 5, transcription factor 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100753|||http://purl.uniprot.org/annotation/VAR_067432|||http://purl.uniprot.org/annotation/VAR_067433|||http://purl.uniprot.org/annotation/VAR_067434|||http://purl.uniprot.org/annotation/VAR_067435|||http://purl.uniprot.org/annotation/VAR_067436|||http://purl.uniprot.org/annotation/VAR_067437|||http://purl.uniprot.org/annotation/VAR_067438
http://togogenome.org/gene/9606:FBN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0D8|||http://purl.uniprot.org/uniprot/A8KAY2|||http://purl.uniprot.org/uniprot/Q75N90                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  EGF-like|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17|||EGF-like 18; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 20; calcium-binding|||EGF-like 21; calcium-binding|||EGF-like 22; calcium-binding|||EGF-like 23; calcium-binding|||EGF-like 24; calcium-binding|||EGF-like 25; calcium-binding|||EGF-like 26; calcium-binding|||EGF-like 27; calcium-binding|||EGF-like 28|||EGF-like 29; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 30; calcium-binding|||EGF-like 31; calcium-binding|||EGF-like 32; calcium-binding|||EGF-like 33; calcium-binding|||EGF-like 34; calcium-binding|||EGF-like 35; calcium-binding|||EGF-like 36; calcium-binding|||EGF-like 37; calcium-binding|||EGF-like 38; calcium-binding|||EGF-like 39; calcium-binding|||EGF-like 40; calcium-binding|||EGF-like 41; calcium-binding|||EGF-like 42; calcium-binding|||EGF-like 43; calcium-binding|||EGF-like 44; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibrillin-3|||Fibrillin-3 C-terminal peptide|||N-linked (GlcNAc...) asparagine|||TB|||TB 1|||TB 2|||TB 3|||TB 4|||TB 5|||TB 6|||TB 7|||TB 8|||TB 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007586|||http://purl.uniprot.org/annotation/PRO_0000436891|||http://purl.uniprot.org/annotation/PRO_0000436892|||http://purl.uniprot.org/annotation/PRO_5002722251|||http://purl.uniprot.org/annotation/PRO_5019731312|||http://purl.uniprot.org/annotation/VAR_019493|||http://purl.uniprot.org/annotation/VAR_019494|||http://purl.uniprot.org/annotation/VAR_019495|||http://purl.uniprot.org/annotation/VAR_019496|||http://purl.uniprot.org/annotation/VAR_019497|||http://purl.uniprot.org/annotation/VAR_019498|||http://purl.uniprot.org/annotation/VAR_019499|||http://purl.uniprot.org/annotation/VAR_019500|||http://purl.uniprot.org/annotation/VAR_019501|||http://purl.uniprot.org/annotation/VAR_019502|||http://purl.uniprot.org/annotation/VAR_019503|||http://purl.uniprot.org/annotation/VAR_019504|||http://purl.uniprot.org/annotation/VAR_019505|||http://purl.uniprot.org/annotation/VAR_019506|||http://purl.uniprot.org/annotation/VAR_055736|||http://purl.uniprot.org/annotation/VAR_055737|||http://purl.uniprot.org/annotation/VAR_055738|||http://purl.uniprot.org/annotation/VAR_055739|||http://purl.uniprot.org/annotation/VAR_055740|||http://purl.uniprot.org/annotation/VAR_055741|||http://purl.uniprot.org/annotation/VAR_055742|||http://purl.uniprot.org/annotation/VAR_055743|||http://purl.uniprot.org/annotation/VAR_055744|||http://purl.uniprot.org/annotation/VAR_055745|||http://purl.uniprot.org/annotation/VAR_055746|||http://purl.uniprot.org/annotation/VAR_055747|||http://purl.uniprot.org/annotation/VAR_055748|||http://purl.uniprot.org/annotation/VAR_055749|||http://purl.uniprot.org/annotation/VAR_055750|||http://purl.uniprot.org/annotation/VAR_055751
http://togogenome.org/gene/9606:TRPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL62                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Essential for binding to NHERF1 PDZ domain|||Extracellular|||Found in a patient with severe delayed speech, autism spectrum and Gilles de la Tourette disorders.|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Short transient receptor potential channel 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215318|||http://purl.uniprot.org/annotation/VAR_052369|||http://purl.uniprot.org/annotation/VAR_069415
http://togogenome.org/gene/9606:RAB11FIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L804                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation by MARK2 and induces defects in the reestablishment of junctional complexes.|||Abolishes the interaction with RAB11A and the vesicular localization.|||Abolishes the interaction with REPS1 and AP2A1. Modifies its subcellular location and the endocytosis activity. Enhances homooligomerization.|||Basic and acidic residues|||C2|||Disordered|||FIP-RBD|||In isoform 2.|||NPF 1|||NPF 2|||NPF 3|||Necessary for interaction with AP2A1, RAB11A, subcellular location, endocytosis activity and homooligomerization|||Necessary for its cellular translocation to the plasma membrane|||No effect on the interaction with RAB11A. Abolishes the vesicular localization.|||No effect.|||Phosphoserine|||Phosphoserine; by MARK2|||Polar residues|||Rab11 family-interacting protein 2|||Severe reduction of the interaction with REPS1 and AP2A1. No effects on its subcellular location. Modifies the endocytosis activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097306|||http://purl.uniprot.org/annotation/VAR_051316|||http://purl.uniprot.org/annotation/VSP_056649
http://togogenome.org/gene/9606:NKAIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PFE2|||http://purl.uniprot.org/uniprot/A0A6Q8PFI1|||http://purl.uniprot.org/uniprot/A0A6Q8PFP9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5028163215|||http://purl.uniprot.org/annotation/PRO_5028250651|||http://purl.uniprot.org/annotation/PRO_5028430882
http://togogenome.org/gene/9606:CCP110                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43303                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CCNF.|||CEP97 binding|||Calmodulin-binding|||Centriolar coiled-coil protein of 110 kDa|||Disordered|||In isoform 2.|||Interaction with CEP76|||Loss of centrosome clustering and protection from anaphase catastrophe upon CDK2 inhibition in lung cancer cells.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with CEP290                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089460|||http://purl.uniprot.org/annotation/VAR_019823|||http://purl.uniprot.org/annotation/VAR_019824|||http://purl.uniprot.org/annotation/VAR_056788|||http://purl.uniprot.org/annotation/VAR_056789|||http://purl.uniprot.org/annotation/VAR_056790|||http://purl.uniprot.org/annotation/VSP_011897
http://togogenome.org/gene/9606:TESK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15569|||http://purl.uniprot.org/uniprot/Q8NFJ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes inhibition of SPRY4-mediated repression of cell spreading. No effect on interaction with SPRY4 or colocalization with SPRY4 at vesicular spots in the cytoplasm.|||Disordered|||Dual specificity testis-specific protein kinase 1|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||Omega-N-methylarginine|||Phosphoserine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor|||Required for interaction with PARVA|||Required for interaction with SPRED1 and SPRY2. Required for TESK1-mediated dephosphorylation of SPRY2 and SPRY2 inhibition of ERK phosphorylation|||Required for interaction with YWHAB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086746|||http://purl.uniprot.org/annotation/VAR_035638|||http://purl.uniprot.org/annotation/VAR_041213
http://togogenome.org/gene/9606:RASAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95294                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||C2 1|||C2 2|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||PH|||Ras-GAP|||RasGAP-activating-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056645|||http://purl.uniprot.org/annotation/VAR_031665|||http://purl.uniprot.org/annotation/VAR_031666|||http://purl.uniprot.org/annotation/VAR_031667|||http://purl.uniprot.org/annotation/VSP_001627|||http://purl.uniprot.org/annotation/VSP_047005|||http://purl.uniprot.org/annotation/VSP_047006
http://togogenome.org/gene/9606:GET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00258                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Guided entry of tail-anchored proteins factor 1|||Helical|||In isoform 2.|||Interaction with GET3/TRC40|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065979|||http://purl.uniprot.org/annotation/VAR_051491|||http://purl.uniprot.org/annotation/VSP_043081
http://togogenome.org/gene/9606:COL1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3H5|||http://purl.uniprot.org/uniprot/P08123                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine; alternate|||Allysine|||C-terminal propeptide|||Collagen alpha-2(I) chain|||Disordered|||Fibrillar collagen NC1|||Found in a patient with a variant form of Marfan syndrome; unknown pathological significance.|||Found in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure.|||In EDSARTH2.|||In OI.|||In OI1, OI3 and OI4.|||In OI1.|||In OI1; mild.|||In OI2.|||In OI2; requires 2 nucleotide substitutions.|||In OI3 and OI2.|||In OI3 and OI4.|||In OI3 and OI4; moderate.|||In OI3.|||In OI3; moderate.|||In OI4.|||In OIEDS2.|||In OIEDS2; decreased N-terminal propeptide processing.|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||O-linked (Gal...) hydroxylysine; alternate|||Pro residues|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005804|||http://purl.uniprot.org/annotation/PRO_0000005805|||http://purl.uniprot.org/annotation/PRO_0000005806|||http://purl.uniprot.org/annotation/PRO_5006608209|||http://purl.uniprot.org/annotation/VAR_001851|||http://purl.uniprot.org/annotation/VAR_001852|||http://purl.uniprot.org/annotation/VAR_001853|||http://purl.uniprot.org/annotation/VAR_001854|||http://purl.uniprot.org/annotation/VAR_001855|||http://purl.uniprot.org/annotation/VAR_001857|||http://purl.uniprot.org/annotation/VAR_001858|||http://purl.uniprot.org/annotation/VAR_001859|||http://purl.uniprot.org/annotation/VAR_001860|||http://purl.uniprot.org/annotation/VAR_001861|||http://purl.uniprot.org/annotation/VAR_001862|||http://purl.uniprot.org/annotation/VAR_001863|||http://purl.uniprot.org/annotation/VAR_001864|||http://purl.uniprot.org/annotation/VAR_001865|||http://purl.uniprot.org/annotation/VAR_001866|||http://purl.uniprot.org/annotation/VAR_001867|||http://purl.uniprot.org/annotation/VAR_001868|||http://purl.uniprot.org/annotation/VAR_001869|||http://purl.uniprot.org/annotation/VAR_001870|||http://purl.uniprot.org/annotation/VAR_001871|||http://purl.uniprot.org/annotation/VAR_001872|||http://purl.uniprot.org/annotation/VAR_001874|||http://purl.uniprot.org/annotation/VAR_001875|||http://purl.uniprot.org/annotation/VAR_001876|||http://purl.uniprot.org/annotation/VAR_001877|||http://purl.uniprot.org/annotation/VAR_001878|||http://purl.uniprot.org/annotation/VAR_001879|||http://purl.uniprot.org/annotation/VAR_001880|||http://purl.uniprot.org/annotation/VAR_001881|||http://purl.uniprot.org/annotation/VAR_001882|||http://purl.uniprot.org/annotation/VAR_001883|||http://purl.uniprot.org/annotation/VAR_001884|||http://purl.uniprot.org/annotation/VAR_001885|||http://purl.uniprot.org/annotation/VAR_001886|||http://purl.uniprot.org/annotation/VAR_001887|||http://purl.uniprot.org/annotation/VAR_001888|||http://purl.uniprot.org/annotation/VAR_001889|||http://purl.uniprot.org/annotation/VAR_001890|||http://purl.uniprot.org/annotation/VAR_001891|||http://purl.uniprot.org/annotation/VAR_001892|||http://purl.uniprot.org/annotation/VAR_001893|||http://purl.uniprot.org/annotation/VAR_001894|||http://purl.uniprot.org/annotation/VAR_001895|||http://purl.uniprot.org/annotation/VAR_001896|||http://purl.uniprot.org/annotation/VAR_001897|||http://purl.uniprot.org/annotation/VAR_001898|||http://purl.uniprot.org/annotation/VAR_001899|||http://purl.uniprot.org/annotation/VAR_001900|||http://purl.uniprot.org/annotation/VAR_001901|||http://purl.uniprot.org/annotation/VAR_001902|||http://purl.uniprot.org/annotation/VAR_001903|||http://purl.uniprot.org/annotation/VAR_001904|||http://purl.uniprot.org/annotation/VAR_001905|||http://purl.uniprot.org/annotation/VAR_001906|||http://purl.uniprot.org/annotation/VAR_008119|||http://purl.uniprot.org/annotation/VAR_008120|||http://purl.uniprot.org/annotation/VAR_030116|||http://purl.uniprot.org/annotation/VAR_030117|||http://purl.uniprot.org/annotation/VAR_030118|||http://purl.uniprot.org/annotation/VAR_030119|||http://purl.uniprot.org/annotation/VAR_030120|||http://purl.uniprot.org/annotation/VAR_030121|||http://purl.uniprot.org/annotation/VAR_030122|||http://purl.uniprot.org/annotation/VAR_033040|||http://purl.uniprot.org/annotation/VAR_033041|||http://purl.uniprot.org/annotation/VAR_055677|||http://purl.uniprot.org/annotation/VAR_063343|||http://purl.uniprot.org/annotation/VAR_063344|||http://purl.uniprot.org/annotation/VAR_063345|||http://purl.uniprot.org/annotation/VAR_063346|||http://purl.uniprot.org/annotation/VAR_063347|||http://purl.uniprot.org/annotation/VAR_063348|||http://purl.uniprot.org/annotation/VAR_063349|||http://purl.uniprot.org/annotation/VAR_063350|||http://purl.uniprot.org/annotation/VAR_063351|||http://purl.uniprot.org/annotation/VAR_063352|||http://purl.uniprot.org/annotation/VAR_063353|||http://purl.uniprot.org/annotation/VAR_063354|||http://purl.uniprot.org/annotation/VAR_063355|||http://purl.uniprot.org/annotation/VAR_063356|||http://purl.uniprot.org/annotation/VAR_063357|||http://purl.uniprot.org/annotation/VAR_063358|||http://purl.uniprot.org/annotation/VAR_063359|||http://purl.uniprot.org/annotation/VAR_063360|||http://purl.uniprot.org/annotation/VAR_063361|||http://purl.uniprot.org/annotation/VAR_063362|||http://purl.uniprot.org/annotation/VAR_063363|||http://purl.uniprot.org/annotation/VAR_063364|||http://purl.uniprot.org/annotation/VAR_063365|||http://purl.uniprot.org/annotation/VAR_063366|||http://purl.uniprot.org/annotation/VAR_063367|||http://purl.uniprot.org/annotation/VAR_063368|||http://purl.uniprot.org/annotation/VAR_063369|||http://purl.uniprot.org/annotation/VAR_063370|||http://purl.uniprot.org/annotation/VAR_063371|||http://purl.uniprot.org/annotation/VAR_063372|||http://purl.uniprot.org/annotation/VAR_063373|||http://purl.uniprot.org/annotation/VAR_063374|||http://purl.uniprot.org/annotation/VAR_063375|||http://purl.uniprot.org/annotation/VAR_063376|||http://purl.uniprot.org/annotation/VAR_063377|||http://purl.uniprot.org/annotation/VAR_063378|||http://purl.uniprot.org/annotation/VAR_063379|||http://purl.uniprot.org/annotation/VAR_063380|||http://purl.uniprot.org/annotation/VAR_063381|||http://purl.uniprot.org/annotation/VAR_063382|||http://purl.uniprot.org/annotation/VAR_063383|||http://purl.uniprot.org/annotation/VAR_066386|||http://purl.uniprot.org/annotation/VAR_069633|||http://purl.uniprot.org/annotation/VAR_085153|||http://purl.uniprot.org/annotation/VAR_085154
http://togogenome.org/gene/9606:TRMT10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBZ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MSSGM1.|||In MSSGM1; results in loss of activity; does not affect affinity for Gly-tRNA.|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311315|||http://purl.uniprot.org/annotation/VAR_037222|||http://purl.uniprot.org/annotation/VAR_037223|||http://purl.uniprot.org/annotation/VAR_072420|||http://purl.uniprot.org/annotation/VAR_080046|||http://purl.uniprot.org/annotation/VAR_080047|||http://purl.uniprot.org/annotation/VAR_080048
http://togogenome.org/gene/9606:MACROH2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0M6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Core histone macro-H2A.2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H2A|||Macro|||N6-lactoyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055320
http://togogenome.org/gene/9606:OR7G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR4|||http://purl.uniprot.org/uniprot/Q8NG95                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7G3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150652|||http://purl.uniprot.org/annotation/VAR_024114
http://togogenome.org/gene/9606:LIN37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein lin-37 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238479|||http://purl.uniprot.org/annotation/VAR_051093|||http://purl.uniprot.org/annotation/VAR_061674
http://togogenome.org/gene/9606:TRUB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95900                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrion|||Nucleophile|||Polar residues|||Pseudouridylate synthase TRUB2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252090|||http://purl.uniprot.org/annotation/VAR_027749|||http://purl.uniprot.org/annotation/VAR_051608|||http://purl.uniprot.org/annotation/VAR_051609|||http://purl.uniprot.org/annotation/VSP_056094
http://togogenome.org/gene/9606:ANHX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PGG2                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Anomalous homeobox protein|||Disordered|||Homeobox                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000418211
http://togogenome.org/gene/9606:SH2D7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||SH2|||SH2 domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341254|||http://purl.uniprot.org/annotation/VAR_060127|||http://purl.uniprot.org/annotation/VAR_060128
http://togogenome.org/gene/9606:AXIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4R0|||http://purl.uniprot.org/uniprot/A0A0S2Z4S3|||http://purl.uniprot.org/uniprot/O15169                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Axin-1|||DIX|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In HCC.|||In HCC; also found in hepatoblastoma.|||In hepatoblastoma.|||In isoform 2.|||Interaction with CTNNB1|||Interaction with GSK3B|||Interaction with HIPK2|||Interaction with PPP2CA|||Interaction with RNF111|||Interaction with SIAH1 and SIAH2|||Interaction with TP53|||Loss of interaction with SIAH1. Decreased SIAH1-induced proteasome-mediated ubiquitin-dependent degradation of AXIN1. No effect on interaction with GSK3B.|||Phosphoserine|||Phosphoserine; by CK1|||Phosphothreonine; by GSK3-beta|||Polar residues|||RGS|||Tankyrase-binding motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220888|||http://purl.uniprot.org/annotation/VAR_015589|||http://purl.uniprot.org/annotation/VAR_015590|||http://purl.uniprot.org/annotation/VAR_015591|||http://purl.uniprot.org/annotation/VAR_015592|||http://purl.uniprot.org/annotation/VAR_015593|||http://purl.uniprot.org/annotation/VSP_019398
http://togogenome.org/gene/9606:SMKR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BMG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Small lysine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421259
http://togogenome.org/gene/9606:PROK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58294                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Prokineticin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025807|||http://purl.uniprot.org/annotation/VAR_053610
http://togogenome.org/gene/9606:IDI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3WKR8|||http://purl.uniprot.org/uniprot/Q13907                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Isopentenyl-diphosphate Delta-isomerase 1|||Microbody targeting signal|||N6-acetyllysine|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205222|||http://purl.uniprot.org/annotation/VSP_037889
http://togogenome.org/gene/9606:DIPK2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTD4|||http://purl.uniprot.org/uniprot/Q8NDZ4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Divergent protein kinase domain 2A|||FAM69 protein-kinase|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226037|||http://purl.uniprot.org/annotation/VSP_042939|||http://purl.uniprot.org/annotation/VSP_042940
http://togogenome.org/gene/9606:YARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Z4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||In MLASA2.|||In MLASA2; has a 2-fold reduction in catalytic activity and a reduction in affinity for tRNA-tyr resulting in an overall 9-fold loss of catalytic efficiency.|||Loss of tRNA ligase activity.|||Mildly decreased tRNA ligase activity.|||Mitochondrion|||N6-acetyllysine|||Tyrosine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035830|||http://purl.uniprot.org/annotation/VAR_034534|||http://purl.uniprot.org/annotation/VAR_064188|||http://purl.uniprot.org/annotation/VAR_068646
http://togogenome.org/gene/9606:GLIS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Pro residues|||Zinc finger protein GLIS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047209|||http://purl.uniprot.org/annotation/VAR_033544|||http://purl.uniprot.org/annotation/VAR_047031|||http://purl.uniprot.org/annotation/VAR_047032
http://togogenome.org/gene/9606:SPAG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV0|||http://purl.uniprot.org/uniprot/Q99932                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||Polar residues|||Sperm-associated antigen 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072099|||http://purl.uniprot.org/annotation/VAR_056992|||http://purl.uniprot.org/annotation/VAR_069166|||http://purl.uniprot.org/annotation/VSP_059990|||http://purl.uniprot.org/annotation/VSP_059991|||http://purl.uniprot.org/annotation/VSP_059992
http://togogenome.org/gene/9606:BHLHE40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14503|||http://purl.uniprot.org/uniprot/Q6IB83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes RXRA repression.|||BHLH|||Basic and acidic residues|||Class E basic helix-loop-helix protein 40|||Disordered|||Essential for interaction with BMAL1, E-box binding and repressor activity against the CLOCK-BMAL1 heterodimer|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1, SUMO2 and SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1, SUMO2 and SUMO3); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Loss of interaction with BMAL1 and E-box binding. Significant reduction in its repressor activity against the CLOCK-BMAL1 heterodimer.|||Loss of repressor activity against NR0B2.|||Necessary for interaction with RXRA and repressor activity against RXRA|||No effect on its interaction with BMAL1 or its repressor activity against the CLOCK-BMAL1 heterodimer. Significant reduction in E-box binding.|||No loss of repressor activity against NR0B2.|||Orange|||Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-159.|||Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-279.|||Phosphoserine|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127144
http://togogenome.org/gene/9606:GZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H116                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Decreased repression activity.|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||GDNF-inducible zinc finger protein 1|||In JLSM.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047539|||http://purl.uniprot.org/annotation/VAR_024212|||http://purl.uniprot.org/annotation/VAR_052735|||http://purl.uniprot.org/annotation/VAR_052736|||http://purl.uniprot.org/annotation/VAR_052737|||http://purl.uniprot.org/annotation/VAR_059890|||http://purl.uniprot.org/annotation/VAR_059891|||http://purl.uniprot.org/annotation/VAR_064718|||http://purl.uniprot.org/annotation/VAR_080250|||http://purl.uniprot.org/annotation/VSP_055933
http://togogenome.org/gene/9606:MS4A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PG2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158646|||http://purl.uniprot.org/annotation/VAR_057652
http://togogenome.org/gene/9606:CYB5R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  FAD-binding FR-type|||Helical|||NADH-cytochrome b5 reductase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287545|||http://purl.uniprot.org/annotation/VAR_032320
http://togogenome.org/gene/9606:CREB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5C6|||http://purl.uniprot.org/uniprot/P16220|||http://purl.uniprot.org/uniprot/Q53X93|||http://purl.uniprot.org/uniprot/Q5U0J5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  BZIP|||Basic motif|||Cyclic AMP-responsive element-binding protein 1|||Decreased sumoylation, in vivo and in vitro.|||Decreased sumoylation, in vivo and in vitro. Loss of nuclear localization.|||Disordered|||Does not interact with TOX3 and inhibits induction of transcription by TOX3. Loss of phosphorylation by CaMK4. Loss of phosphorylation by TSSK4.|||Found in a patient with multiple congenital anomalies; does not affect CREB1 phosphorylation at S-119; fails to interact with CREBBP.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation by HIPK2 and subsequent transactivation.|||In isoform 2 and isoform 3.|||In isoform 3.|||KID|||Leucine-zipper|||No effect on sumoylation.|||Phosphoserine|||Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5, SGK1 and TSSK4|||Phosphoserine; by HIPK2|||Potentiated transactivation.|||Required for binding TORCs|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076597|||http://purl.uniprot.org/annotation/VAR_068077|||http://purl.uniprot.org/annotation/VSP_060702|||http://purl.uniprot.org/annotation/VSP_060703
http://togogenome.org/gene/9606:KRT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99456                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In MECD1.|||In MECD1; increased expression of keratins KRT5, KRT6, KRT14 and KRT16 and decreased expression of KRT12 in the corneal epithelium; increased expression of DDIT3/CHOP and CASP12 in the corneal epithelium indicative of up-regulation of the unfolded protein response..|||In MECD1; unknown pathological significance.|||Keratin, type I cytoskeletal 12|||Linker 1|||Linker 12|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063644|||http://purl.uniprot.org/annotation/VAR_003834|||http://purl.uniprot.org/annotation/VAR_003835|||http://purl.uniprot.org/annotation/VAR_008525|||http://purl.uniprot.org/annotation/VAR_008526|||http://purl.uniprot.org/annotation/VAR_008527|||http://purl.uniprot.org/annotation/VAR_008528|||http://purl.uniprot.org/annotation/VAR_009547|||http://purl.uniprot.org/annotation/VAR_013126|||http://purl.uniprot.org/annotation/VAR_013127|||http://purl.uniprot.org/annotation/VAR_031394|||http://purl.uniprot.org/annotation/VAR_031395|||http://purl.uniprot.org/annotation/VAR_031396|||http://purl.uniprot.org/annotation/VAR_031397|||http://purl.uniprot.org/annotation/VAR_031398|||http://purl.uniprot.org/annotation/VAR_049783|||http://purl.uniprot.org/annotation/VAR_072069|||http://purl.uniprot.org/annotation/VAR_072070|||http://purl.uniprot.org/annotation/VAR_072071|||http://purl.uniprot.org/annotation/VAR_072072|||http://purl.uniprot.org/annotation/VAR_072073|||http://purl.uniprot.org/annotation/VAR_083313|||http://purl.uniprot.org/annotation/VAR_083314|||http://purl.uniprot.org/annotation/VAR_083315
http://togogenome.org/gene/9606:NCOA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15788                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes sumoylation; when associated with R-732.|||Abolishes sumoylation; when associated with R-774.|||Asymmetric dimethylarginine|||Breakpoint for translocation to form PAX3-NCOA1 oncogene|||Disordered|||Does not affect sumoylation of the protein.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with CREBBP|||Interaction with STAT3|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||LXXLL motif 6|||LXXLL motif 7|||N-acetylserine|||Nuclear receptor coactivator 1|||PAS|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-693 and A-694.|||Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-752 and A-753.|||Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-693; A-694; A-752 and A-753.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094400|||http://purl.uniprot.org/annotation/VAR_019768|||http://purl.uniprot.org/annotation/VAR_019769|||http://purl.uniprot.org/annotation/VAR_019770|||http://purl.uniprot.org/annotation/VAR_019771|||http://purl.uniprot.org/annotation/VAR_019772|||http://purl.uniprot.org/annotation/VAR_019773|||http://purl.uniprot.org/annotation/VAR_019774|||http://purl.uniprot.org/annotation/VAR_019775|||http://purl.uniprot.org/annotation/VAR_034882|||http://purl.uniprot.org/annotation/VAR_038832|||http://purl.uniprot.org/annotation/VSP_011738|||http://purl.uniprot.org/annotation/VSP_011739
http://togogenome.org/gene/9606:ZNF223                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK11                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 223                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047464|||http://purl.uniprot.org/annotation/VAR_060424|||http://purl.uniprot.org/annotation/VAR_060425
http://togogenome.org/gene/9606:RBPMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3T4|||http://purl.uniprot.org/uniprot/Q93062                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes RNA binding.|||Abolishes RNA binding; when associated with A-100.|||Abolishes RNA binding; when associated with A-97.|||Impairs dimerization and RNA binding.|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||Interaction with RNA|||N-acetylmethionine|||Phosphothreonine|||RNA-binding protein with multiple splicing|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081793|||http://purl.uniprot.org/annotation/VSP_005813|||http://purl.uniprot.org/annotation/VSP_005814|||http://purl.uniprot.org/annotation/VSP_005815|||http://purl.uniprot.org/annotation/VSP_005816
http://togogenome.org/gene/9606:UBXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTZ5|||http://purl.uniprot.org/uniprot/Q04323                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to 'Lys-6'-linked polyubiquitin chains and ability to inhibit E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer.|||Basic and acidic residues|||Disordered|||Does not affect binding to 'Lys-6'-linked polyubiquitin chains and ability to inhibit E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer.|||In isoform 2.|||Interaction with BRCA1|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAPK12|||Phosphothreonine|||Pro residues|||Removed|||UBA|||UBX|||UBX domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211023|||http://purl.uniprot.org/annotation/VAR_057370|||http://purl.uniprot.org/annotation/VSP_020367
http://togogenome.org/gene/9606:INSL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14641                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  C peptide|||Early placenta insulin-like peptide|||Early placenta insulin-like peptide A chain|||Early placenta insulin-like peptide B chain|||Interchain (between B and A chains)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016155|||http://purl.uniprot.org/annotation/PRO_0000016156|||http://purl.uniprot.org/annotation/PRO_0000016157|||http://purl.uniprot.org/annotation/PRO_0000016158
http://togogenome.org/gene/9606:SH3GL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99963                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BAR|||Disordered|||Endophilin-A3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ARC|||Membrane-binding amphipathic helix|||Phosphoserine|||Required for dimerization upon membrane association|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146750|||http://purl.uniprot.org/annotation/VSP_001440|||http://purl.uniprot.org/annotation/VSP_001441|||http://purl.uniprot.org/annotation/VSP_001442
http://togogenome.org/gene/9606:FBXW10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XX13                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box/WD repeat-containing protein 10|||In isoform 2.|||In isoform 3.|||In isoform 4.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315834|||http://purl.uniprot.org/annotation/VAR_038341|||http://purl.uniprot.org/annotation/VAR_038342|||http://purl.uniprot.org/annotation/VAR_057600|||http://purl.uniprot.org/annotation/VSP_030727|||http://purl.uniprot.org/annotation/VSP_030728|||http://purl.uniprot.org/annotation/VSP_030729|||http://purl.uniprot.org/annotation/VSP_039178
http://togogenome.org/gene/9606:CELF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZC1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUGBP Elav-like family member 4|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||Necessary for TNNT2 exon 5 inclusion|||RRM 1|||RRM 2|||RRM 3|||Sufficient for RNA-binding and MSE-dependent splicing activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295221|||http://purl.uniprot.org/annotation/VAR_052203|||http://purl.uniprot.org/annotation/VSP_026828|||http://purl.uniprot.org/annotation/VSP_026829|||http://purl.uniprot.org/annotation/VSP_026830|||http://purl.uniprot.org/annotation/VSP_026831|||http://purl.uniprot.org/annotation/VSP_026832
http://togogenome.org/gene/9606:RIDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52758                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  2-iminobutanoate/2-iminopropanoate deaminase|||N-acetylserine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170308
http://togogenome.org/gene/9606:TNFSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23510                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Tumor necrosis factor ligand superfamily member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185493|||http://purl.uniprot.org/annotation/VSP_056288
http://togogenome.org/gene/9606:AGER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X785|||http://purl.uniprot.org/uniprot/B4DNX3|||http://purl.uniprot.org/uniprot/Q15109                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Advanced glycosylation end product-specific receptor|||Basic and acidic residues|||Complete loss of phosphorylation by PKC/PRKCZ.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 10.|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 8.|||In isoform 9.|||Interchain|||Less monoubiquitinated product and resistant to degradation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC/PRKCZ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014923|||http://purl.uniprot.org/annotation/PRO_5014275534|||http://purl.uniprot.org/annotation/VAR_011338|||http://purl.uniprot.org/annotation/VAR_024500|||http://purl.uniprot.org/annotation/VSP_002551|||http://purl.uniprot.org/annotation/VSP_002552|||http://purl.uniprot.org/annotation/VSP_042011|||http://purl.uniprot.org/annotation/VSP_043528|||http://purl.uniprot.org/annotation/VSP_047884|||http://purl.uniprot.org/annotation/VSP_047885|||http://purl.uniprot.org/annotation/VSP_047886|||http://purl.uniprot.org/annotation/VSP_047887|||http://purl.uniprot.org/annotation/VSP_047888|||http://purl.uniprot.org/annotation/VSP_047889|||http://purl.uniprot.org/annotation/VSP_055321
http://togogenome.org/gene/9606:DUSP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13115                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 4|||In isoform 2.|||N-acetylvaline|||Phosphocysteine intermediate|||Phosphoserine; by MAPK|||Removed|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094798|||http://purl.uniprot.org/annotation/VSP_044667|||http://purl.uniprot.org/annotation/VSP_044668
http://togogenome.org/gene/9606:ZNF189                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0K2|||http://purl.uniprot.org/uniprot/B7ZLK9|||http://purl.uniprot.org/uniprot/O75820                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||Zinc finger protein 189                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047444|||http://purl.uniprot.org/annotation/VAR_025403|||http://purl.uniprot.org/annotation/VSP_006899|||http://purl.uniprot.org/annotation/VSP_006900|||http://purl.uniprot.org/annotation/VSP_006901
http://togogenome.org/gene/9606:GPALPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||GPALPP motif 1|||GPALPP motif 2|||GPALPP motif 3|||GPALPP motif 4|||GPALPP motifs-containing protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293714|||http://purl.uniprot.org/annotation/VSP_026567|||http://purl.uniprot.org/annotation/VSP_026568|||http://purl.uniprot.org/annotation/VSP_026569|||http://purl.uniprot.org/annotation/VSP_026570
http://togogenome.org/gene/9606:SNX32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XE0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||PX|||Sorting nexin-32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320707|||http://purl.uniprot.org/annotation/VAR_039298|||http://purl.uniprot.org/annotation/VAR_039299|||http://purl.uniprot.org/annotation/VAR_039300|||http://purl.uniprot.org/annotation/VSP_031742|||http://purl.uniprot.org/annotation/VSP_031743
http://togogenome.org/gene/9606:CSKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUP2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Citrate synthase-lysine N-methyltransferase CSKMT, mitochondrial|||Inhibits citrate synthase-lysine methyltransferase activity.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349199|||http://purl.uniprot.org/annotation/VAR_046283
http://togogenome.org/gene/9606:NR2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10589                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  COUP transcription factor 1|||Disordered|||In BBSOAS; decreases transcriptional activity.|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Probable disease-associated variant found in a patient with early infantile epileptic encephalopathy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053602|||http://purl.uniprot.org/annotation/VAR_071319|||http://purl.uniprot.org/annotation/VAR_071320|||http://purl.uniprot.org/annotation/VAR_071321|||http://purl.uniprot.org/annotation/VAR_071322|||http://purl.uniprot.org/annotation/VAR_078708
http://togogenome.org/gene/9606:CCDC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PFB9|||http://purl.uniprot.org/uniprot/Q5T9S5|||http://purl.uniprot.org/uniprot/Q6PH87|||http://purl.uniprot.org/uniprot/Q7Z659                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 18|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284775|||http://purl.uniprot.org/annotation/VSP_024636
http://togogenome.org/gene/9606:NCKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J4I5|||http://purl.uniprot.org/uniprot/A0A994J6K9|||http://purl.uniprot.org/uniprot/Q9Y2A7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with intellectual disability; unknown pathological significance.|||Helical|||In isoform 2.|||N-acetylserine|||Nck-associated protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216172|||http://purl.uniprot.org/annotation/VAR_084649|||http://purl.uniprot.org/annotation/VSP_036558
http://togogenome.org/gene/9606:ZNF24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17028                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Necessary and sufficient for nuclear localization|||Partial cytoplasmic accumulation.|||Phosphoserine|||Phosphotyrosine|||SCAN box|||Zinc finger protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047352|||http://purl.uniprot.org/annotation/VAR_012017|||http://purl.uniprot.org/annotation/VAR_012018|||http://purl.uniprot.org/annotation/VSP_039219|||http://purl.uniprot.org/annotation/VSP_039220
http://togogenome.org/gene/9606:PCDH19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU71|||http://purl.uniprot.org/uniprot/Q8TAB3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DEE9.|||In DEE9; disease features overlapping with Dravet syndrome.|||In DEE9; disease features overlapping with Dravet syndrome; associated with Cys-206.|||In DEE9; disease features overlapping with Dravet syndrome; associated with Pro-203.|||In DEE9; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with drug-resistant epilepsy.|||Protocadherin-19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004003|||http://purl.uniprot.org/annotation/VAR_046484|||http://purl.uniprot.org/annotation/VAR_046485|||http://purl.uniprot.org/annotation/VAR_064481|||http://purl.uniprot.org/annotation/VAR_064482|||http://purl.uniprot.org/annotation/VAR_064483|||http://purl.uniprot.org/annotation/VAR_064484|||http://purl.uniprot.org/annotation/VAR_064485|||http://purl.uniprot.org/annotation/VAR_064486|||http://purl.uniprot.org/annotation/VAR_064487|||http://purl.uniprot.org/annotation/VAR_064488|||http://purl.uniprot.org/annotation/VAR_064489|||http://purl.uniprot.org/annotation/VAR_064490|||http://purl.uniprot.org/annotation/VAR_064491|||http://purl.uniprot.org/annotation/VAR_064492|||http://purl.uniprot.org/annotation/VAR_064840|||http://purl.uniprot.org/annotation/VAR_064841|||http://purl.uniprot.org/annotation/VAR_064842|||http://purl.uniprot.org/annotation/VAR_064843|||http://purl.uniprot.org/annotation/VAR_064844|||http://purl.uniprot.org/annotation/VAR_064845|||http://purl.uniprot.org/annotation/VAR_064846|||http://purl.uniprot.org/annotation/VAR_064847|||http://purl.uniprot.org/annotation/VAR_064848|||http://purl.uniprot.org/annotation/VAR_067472|||http://purl.uniprot.org/annotation/VAR_067473|||http://purl.uniprot.org/annotation/VAR_067474|||http://purl.uniprot.org/annotation/VAR_067475|||http://purl.uniprot.org/annotation/VAR_067476|||http://purl.uniprot.org/annotation/VAR_067477|||http://purl.uniprot.org/annotation/VAR_067478|||http://purl.uniprot.org/annotation/VAR_067479|||http://purl.uniprot.org/annotation/VAR_067480|||http://purl.uniprot.org/annotation/VAR_067481|||http://purl.uniprot.org/annotation/VAR_067482|||http://purl.uniprot.org/annotation/VAR_067483|||http://purl.uniprot.org/annotation/VAR_067484|||http://purl.uniprot.org/annotation/VAR_067485|||http://purl.uniprot.org/annotation/VAR_067486|||http://purl.uniprot.org/annotation/VAR_067487|||http://purl.uniprot.org/annotation/VAR_067488|||http://purl.uniprot.org/annotation/VAR_067489|||http://purl.uniprot.org/annotation/VAR_078227|||http://purl.uniprot.org/annotation/VAR_078722|||http://purl.uniprot.org/annotation/VAR_078723|||http://purl.uniprot.org/annotation/VAR_078724|||http://purl.uniprot.org/annotation/VSP_015081|||http://purl.uniprot.org/annotation/VSP_054046
http://togogenome.org/gene/9606:STIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUB5|||http://purl.uniprot.org/uniprot/H0Y860|||http://purl.uniprot.org/uniprot/Q9P246                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No effect on inhibitory activity; when associated with A-80.|||No effect on inhibitory activity; when associated with A-91.|||Phosphoserine|||Polar residues|||SAM|||Stromal interaction molecule 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033328|||http://purl.uniprot.org/annotation/VSP_057171|||http://purl.uniprot.org/annotation/VSP_057172|||http://purl.uniprot.org/annotation/VSP_057173|||http://purl.uniprot.org/annotation/VSP_057174
http://togogenome.org/gene/9606:RBM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Accumulates in speckle-like structures.|||Basic and acidic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor RBM22|||Pro residues|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250546|||http://purl.uniprot.org/annotation/VSP_036832
http://togogenome.org/gene/9606:ZNF358                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW07                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Polar residues|||Pro residues|||Zinc finger protein 358                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047547|||http://purl.uniprot.org/annotation/VAR_061944
http://togogenome.org/gene/9606:BPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17213                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Bactericidal permeability-increasing protein|||C-terminal barrel|||Central sheet, part 1|||Central sheet, part 2|||Central sheet, part 3|||Cleavage sites for elastase|||N-linked (GlcNAc...) asparagine|||N-terminal barrel|||No impairment of secretion and increased propensity for dimer formation.|||No impairment of secretion and/or biological activity. Loss of dimer formation.|||Not secreted.|||Poorly secreted. Loss of LPS-binding and biological activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017154|||http://purl.uniprot.org/annotation/VAR_018401|||http://purl.uniprot.org/annotation/VAR_018402|||http://purl.uniprot.org/annotation/VAR_018403|||http://purl.uniprot.org/annotation/VAR_049728|||http://purl.uniprot.org/annotation/VAR_049729|||http://purl.uniprot.org/annotation/VAR_049730|||http://purl.uniprot.org/annotation/VAR_049732|||http://purl.uniprot.org/annotation/VAR_049733|||http://purl.uniprot.org/annotation/VAR_049734|||http://purl.uniprot.org/annotation/VAR_049735|||http://purl.uniprot.org/annotation/VAR_049736
http://togogenome.org/gene/9606:LMBRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUN5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Affects glycosylation status. Affects glycosylation status; when associated with Q-448.|||Affects glycosylation status; when associated with Q-457.|||Cytoplasmic|||Does not affect glycosylation status; when associated with Q-78.|||Does not affect glycosylation status; when associated with Q-88.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Lysosomal cobalamin transport escort protein LMBD1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||WTKF motif; mediates interaction with adapter protein complex 2 and is essential for its function in clathrin-mediated endocytosis of INSR|||YERL motif; mediates interaction with adapter protein complex 2 and is essential for its function in clathrin-mediated endocytosis of INSR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260515|||http://purl.uniprot.org/annotation/VAR_029047|||http://purl.uniprot.org/annotation/VAR_029048|||http://purl.uniprot.org/annotation/VAR_029049|||http://purl.uniprot.org/annotation/VSP_021629|||http://purl.uniprot.org/annotation/VSP_021630|||http://purl.uniprot.org/annotation/VSP_036539|||http://purl.uniprot.org/annotation/VSP_036540
http://togogenome.org/gene/9606:LRIG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94898                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeats and immunoglobulin-like domains protein 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014829
http://togogenome.org/gene/9606:SCYL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||In isoform 2.|||Interaction with EZR|||N-myristoyl glycine|||No Golgi targeting, accumulates in the cytoplasm.|||Phosphoserine|||Protein kinase|||Protein-associating with the carboxyl-terminal domain of ezrin|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058167|||http://purl.uniprot.org/annotation/VAR_051690|||http://purl.uniprot.org/annotation/VAR_051691|||http://purl.uniprot.org/annotation/VSP_013125
http://togogenome.org/gene/9606:COL22A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen alpha-1(XXII) chain|||Collagen-like 1|||Collagen-like 10|||Collagen-like 11|||Collagen-like 12|||Collagen-like 13|||Collagen-like 14|||Collagen-like 15|||Collagen-like 16|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Collagen-like 9|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317615|||http://purl.uniprot.org/annotation/VAR_038562|||http://purl.uniprot.org/annotation/VAR_038563|||http://purl.uniprot.org/annotation/VAR_038564|||http://purl.uniprot.org/annotation/VSP_031087|||http://purl.uniprot.org/annotation/VSP_038200
http://togogenome.org/gene/9606:PIGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07326|||http://purl.uniprot.org/uniprot/Q6IB04                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In OORS; defective GPI anchor biosynthesis in homozygous patient cells.|||In isoform 2.|||Phosphatidylinositol-glycan biosynthesis class F protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191759|||http://purl.uniprot.org/annotation/VAR_085810|||http://purl.uniprot.org/annotation/VSP_004361
http://togogenome.org/gene/9606:TMEM126A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H061                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 126A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270999|||http://purl.uniprot.org/annotation/VAR_053817|||http://purl.uniprot.org/annotation/VSP_046927
http://togogenome.org/gene/9606:CENPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03188                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Centromere protein C|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MIF2 homology domain II|||MIF2 homology domain III|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089474|||http://purl.uniprot.org/annotation/VAR_069295|||http://purl.uniprot.org/annotation/VAR_069296|||http://purl.uniprot.org/annotation/VSP_057280|||http://purl.uniprot.org/annotation/VSP_057281
http://togogenome.org/gene/9606:DUSP13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6B8I1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Dual specificity protein phosphatase 13A|||In isoform 2.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of enzyme activity. No effect on interaction with MAP3K5.|||No effect on interaction with MAP3K5.|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000381973|||http://purl.uniprot.org/annotation/VAR_058495|||http://purl.uniprot.org/annotation/VSP_046445|||http://purl.uniprot.org/annotation/VSP_046446|||http://purl.uniprot.org/annotation/VSP_046447|||http://purl.uniprot.org/annotation/VSP_046448|||http://purl.uniprot.org/annotation/VSP_046449|||http://purl.uniprot.org/annotation/VSP_047819
http://togogenome.org/gene/9606:LRRC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N456                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084472|||http://purl.uniprot.org/annotation/VAR_028161|||http://purl.uniprot.org/annotation/VAR_028162|||http://purl.uniprot.org/annotation/VSP_015740
http://togogenome.org/gene/9606:AASDHPPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase|||Phosphoserine|||Reduces affinity for magnesium and coenzyme A, and reduces holo-[acyl-carrier-protein] synthase activity by 7-fold.|||Reduces affinity for magnesium by 10-fold, and holo-[acyl-carrier-protein] synthase activity by 30000-fold.|||Reduces affinity for magnesium by 20-fold, and holo-[acyl-carrier-protein] synthase activity by 6500-fold.|||Reduces affinity for magnesium by 200-fold and abolishes holo-[acyl-carrier-protein] synthase activity; when associated with Q-181.|||Reduces affinity for magnesium by 40-fold, and holo-[acyl-carrier-protein] synthase activity by 32000-fold.|||Reduces affinity for magnesium by 7-fold, and holo-[acyl-carrier-protein] synthase activity by 2-fold.|||Reduces affinity for magnesium by 75-fold, and holo-[acyl-carrier-protein] synthase activity by 150-fold.|||Reduces holo-[acyl-carrier-protein] synthase activity by 2000-fold, with only minor change in the affinity for magnesium and coenzyme A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175736|||http://purl.uniprot.org/annotation/VSP_055783|||http://purl.uniprot.org/annotation/VSP_055784
http://togogenome.org/gene/9606:MLANA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR46|||http://purl.uniprot.org/uniprot/Q16655                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Melanoma antigen recognized by T-cells 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096238
http://togogenome.org/gene/9606:PRKCZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05513                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with SQSTM1|||Loss of interaction with SQSTM1 and PARD6B.|||No effect on interaction with SQSTM1 and PARD6B.|||PB1|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1 and PI3K|||Protein kinase|||Protein kinase C zeta type|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055701|||http://purl.uniprot.org/annotation/VAR_035467|||http://purl.uniprot.org/annotation/VAR_042310|||http://purl.uniprot.org/annotation/VAR_042311|||http://purl.uniprot.org/annotation/VAR_050560|||http://purl.uniprot.org/annotation/VSP_041904|||http://purl.uniprot.org/annotation/VSP_046347
http://togogenome.org/gene/9606:RRBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2E9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34; approximate|||35|||36; approximate|||37|||38|||39; approximate|||4|||40|||41|||41 X 10 AA approximate tandem repeats of [TN]-Q-[GSA]-[KRQT]-K-[ATGSV]-[ED]-[GTAS]-[ATIS]-[PQTAS]|||5|||6|||7|||8|||9|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2.|||Lumenal|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosome-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097441|||http://purl.uniprot.org/annotation/VAR_056982|||http://purl.uniprot.org/annotation/VSP_003949|||http://purl.uniprot.org/annotation/VSP_003950
http://togogenome.org/gene/9606:STPG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TH74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||O(6)-methylguanine-induced apoptosis 2|||Phosphotyrosine|||Polar residues|||STPGR 1|||STPGR 2|||STPGR 3|||STPGR 4|||STPGR 5|||STPGR 6|||STPGR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305170|||http://purl.uniprot.org/annotation/VAR_035614|||http://purl.uniprot.org/annotation/VSP_028252|||http://purl.uniprot.org/annotation/VSP_028253|||http://purl.uniprot.org/annotation/VSP_028254
http://togogenome.org/gene/9606:FBXL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N531                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box/LRR-repeat protein 6|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119847|||http://purl.uniprot.org/annotation/VAR_085739|||http://purl.uniprot.org/annotation/VSP_008498
http://togogenome.org/gene/9606:SPC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interaction with the C-terminus of SPBC25|||Interaction with the N-terminus of SPBC25|||Interaction with the NDC80-CDCA1 subcomplex|||Kinetochore protein Spc24|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249559|||http://purl.uniprot.org/annotation/VSP_054243
http://togogenome.org/gene/9606:H2BC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4S9|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A/H2B/H3|||Histone H2B type 1-C/E/F/G/I|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:DCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P81605                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DCD-1|||Dermcidin|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Loss of anion channel activity.|||N6-acetyllysine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Survival-promoting peptide|||in chain A|||in chain B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021081|||http://purl.uniprot.org/annotation/PRO_0000021082|||http://purl.uniprot.org/annotation/PRO_0000021083|||http://purl.uniprot.org/annotation/PRO_0000021084|||http://purl.uniprot.org/annotation/PRO_0000408312|||http://purl.uniprot.org/annotation/VSP_043765|||http://purl.uniprot.org/annotation/VSP_043766|||http://purl.uniprot.org/annotation/VSP_043767
http://togogenome.org/gene/9606:CWC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Decreased EIF4A3-binding; when associated with A-331.|||Decreased EIF4A3-binding; when associated with A-334.|||Disordered|||Loss of EIF4A3-binding.|||MI|||MIF4G|||No effect on EIF4A3 incorporation into EJCs.|||Phosphoserine|||Polar residues|||Pre-mRNA-splicing factor CWC22 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302005|||http://purl.uniprot.org/annotation/VAR_057513|||http://purl.uniprot.org/annotation/VAR_057514|||http://purl.uniprot.org/annotation/VAR_057515
http://togogenome.org/gene/9606:SLC25A46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY98|||http://purl.uniprot.org/uniprot/Q96AG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In HMSN6B; decreased protein abundance.|||In HMSN6B; slightly decreased protein abundance.|||In HMSN6B; unknown pathological significance.|||In HMSN6B; unknown pathological significance; no effect on protein abundance.|||In HMSN6B; unknown pathological significance; slightly decreased protein abundance.|||In PCH1E.|||In PCH1E; decreased protein abundance; loss of function in mitochondrial fission; no effect on localization to the mitochondrial outer membrane.|||In PCH1E; loss of protein expression.|||In isoform 2.|||In isoform 3.|||Mitochondrial outer membrane protein SLC25A46|||Phosphoserine|||Phosphothreonine|||Polar residues|||Solcar|||Solcar 1|||Solcar 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291828|||http://purl.uniprot.org/annotation/VAR_075818|||http://purl.uniprot.org/annotation/VAR_075819|||http://purl.uniprot.org/annotation/VAR_075820|||http://purl.uniprot.org/annotation/VAR_075821|||http://purl.uniprot.org/annotation/VAR_085718|||http://purl.uniprot.org/annotation/VAR_085719|||http://purl.uniprot.org/annotation/VAR_085720|||http://purl.uniprot.org/annotation/VAR_085721|||http://purl.uniprot.org/annotation/VAR_085722|||http://purl.uniprot.org/annotation/VAR_085723|||http://purl.uniprot.org/annotation/VSP_056112|||http://purl.uniprot.org/annotation/VSP_056351
http://togogenome.org/gene/9606:DZIP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYY4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Cilium assembly protein DZIP1L|||Disordered|||In PKD5.|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331306|||http://purl.uniprot.org/annotation/VAR_042756|||http://purl.uniprot.org/annotation/VAR_042757|||http://purl.uniprot.org/annotation/VAR_042758|||http://purl.uniprot.org/annotation/VAR_042759|||http://purl.uniprot.org/annotation/VAR_042760|||http://purl.uniprot.org/annotation/VAR_078962|||http://purl.uniprot.org/annotation/VAR_078963|||http://purl.uniprot.org/annotation/VAR_078964|||http://purl.uniprot.org/annotation/VSP_033158|||http://purl.uniprot.org/annotation/VSP_033159
http://togogenome.org/gene/9606:IQCF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYZ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  IQ|||IQ domain-containing protein F6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343226
http://togogenome.org/gene/9606:EMC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV81                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||ER membrane protein complex subunit 6|||Helical|||Lumenal|||N-acetylalanine|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254156
http://togogenome.org/gene/9606:IQCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ|||IQ domain-containing protein C|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282545|||http://purl.uniprot.org/annotation/VAR_031411|||http://purl.uniprot.org/annotation/VAR_031412|||http://purl.uniprot.org/annotation/VAR_031413|||http://purl.uniprot.org/annotation/VSP_024176|||http://purl.uniprot.org/annotation/VSP_046123
http://togogenome.org/gene/9606:TAS2R16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8E5KFD5|||http://purl.uniprot.org/uniprot/Q9NYV7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with susceptibility to alcoholism.|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082262|||http://purl.uniprot.org/annotation/VAR_020205|||http://purl.uniprot.org/annotation/VAR_034539|||http://purl.uniprot.org/annotation/VAR_080835|||http://purl.uniprot.org/annotation/VAR_080836|||http://purl.uniprot.org/annotation/VAR_080837|||http://purl.uniprot.org/annotation/VAR_080838|||http://purl.uniprot.org/annotation/VAR_080839|||http://purl.uniprot.org/annotation/VAR_080840|||http://purl.uniprot.org/annotation/VAR_080841|||http://purl.uniprot.org/annotation/VAR_080842|||http://purl.uniprot.org/annotation/VAR_080843
http://togogenome.org/gene/9606:SCG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Secretogranin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005461|||http://purl.uniprot.org/annotation/VAR_013827|||http://purl.uniprot.org/annotation/VAR_034484|||http://purl.uniprot.org/annotation/VAR_067273|||http://purl.uniprot.org/annotation/VSP_042876
http://togogenome.org/gene/9606:ZFX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17010|||http://purl.uniprot.org/uniprot/Q59EB9|||http://purl.uniprot.org/uniprot/Q8WXB7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Transcriptional activator Zfx / Zfy|||Zinc finger X-chromosomal protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047258|||http://purl.uniprot.org/annotation/VSP_014371|||http://purl.uniprot.org/annotation/VSP_054512
http://togogenome.org/gene/9606:TBC1D20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BZ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  1000-fold decrease in GAP activity.|||Arginine finger|||Disordered|||Glutamine finger|||Helical|||In isoform 2.|||In isoform 3.|||Rab-GAP TBC|||TBC1 domain family member 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208048|||http://purl.uniprot.org/annotation/VAR_052543|||http://purl.uniprot.org/annotation/VSP_008100|||http://purl.uniprot.org/annotation/VSP_008101|||http://purl.uniprot.org/annotation/VSP_008102|||http://purl.uniprot.org/annotation/VSP_031524
http://togogenome.org/gene/9606:OR5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGJ0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150572|||http://purl.uniprot.org/annotation/VAR_024096|||http://purl.uniprot.org/annotation/VAR_034213
http://togogenome.org/gene/9606:ITGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56199                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Integrin alpha-1|||N-linked (GlcNAc...) asparagine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174215|||http://purl.uniprot.org/annotation/VAR_034022|||http://purl.uniprot.org/annotation/VAR_034023|||http://purl.uniprot.org/annotation/VAR_034024|||http://purl.uniprot.org/annotation/VAR_049630
http://togogenome.org/gene/9606:FSTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12841                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Follistatin-like|||Follistatin-related protein 1|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010111|||http://purl.uniprot.org/annotation/VSP_055075
http://togogenome.org/gene/9606:RALGPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PH|||PXXP|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras-GEF|||Ras-specific guanine nucleotide-releasing factor RalGPS2|||Required for stimulation of nucleotide exchange by RALA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322600|||http://purl.uniprot.org/annotation/VAR_039468|||http://purl.uniprot.org/annotation/VSP_031971|||http://purl.uniprot.org/annotation/VSP_054909
http://togogenome.org/gene/9606:ZMYM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||MYM-type 5|||MYM-type 6|||MYM-type 7|||MYM-type 8|||MYM-type 9|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Zinc finger MYM-type protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299017|||http://purl.uniprot.org/annotation/VAR_034764|||http://purl.uniprot.org/annotation/VAR_035672|||http://purl.uniprot.org/annotation/VSP_027512|||http://purl.uniprot.org/annotation/VSP_027513|||http://purl.uniprot.org/annotation/VSP_027514
http://togogenome.org/gene/9606:SETD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15047                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with S-adenosyl-L-methionine.|||Acidic residues|||Basic and acidic residues|||Disordered|||HCFC1-binding motif (HBM)|||Histone-lysine N-methyltransferase SETD1A|||In EPEDD; affects the development of synapses in a mouse model overexpressing the human protein harboring this variant.|||In NEDSID.|||In NEDSID; causes DNA damage repair defects associated with nucleolytic degradation of nascent DNA at stalled replication forks.|||Interaction with ASH2L, RBBP5 and WDR5|||Interaction with CFP1|||Phosphoserine|||Polar residues|||Post-SET|||Pro residues|||RRM|||SET|||WDR5 interaction motif (WIN)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186056|||http://purl.uniprot.org/annotation/VAR_059318|||http://purl.uniprot.org/annotation/VAR_083962|||http://purl.uniprot.org/annotation/VAR_083963|||http://purl.uniprot.org/annotation/VAR_083964|||http://purl.uniprot.org/annotation/VAR_083965|||http://purl.uniprot.org/annotation/VAR_085008|||http://purl.uniprot.org/annotation/VAR_085029|||http://purl.uniprot.org/annotation/VAR_085030|||http://purl.uniprot.org/annotation/VAR_085031|||http://purl.uniprot.org/annotation/VAR_085032|||http://purl.uniprot.org/annotation/VAR_085033
http://togogenome.org/gene/9606:S100A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31949|||http://purl.uniprot.org/uniprot/V9HWH9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||Interchain|||N-acetylalanine; in Protein S100-A11, N-terminally processed|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein S100-A11|||Protein S100-A11, N-terminally processed|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144009|||http://purl.uniprot.org/annotation/PRO_0000424465
http://togogenome.org/gene/9606:TMEM179                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0S3|||http://purl.uniprot.org/uniprot/Q6ZVK1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 179                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254552|||http://purl.uniprot.org/annotation/VSP_021227|||http://purl.uniprot.org/annotation/VSP_021228
http://togogenome.org/gene/9606:TLE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EMK7|||http://purl.uniprot.org/uniprot/Q04725                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CK2|||Phosphothreonine; by CDK1|||Polar residues|||Q domain|||SP domain|||Transducin-like enhancer protein 2|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051278|||http://purl.uniprot.org/annotation/VAR_069063|||http://purl.uniprot.org/annotation/VSP_045693|||http://purl.uniprot.org/annotation/VSP_045694|||http://purl.uniprot.org/annotation/VSP_046162|||http://purl.uniprot.org/annotation/VSP_046163|||http://purl.uniprot.org/annotation/VSP_046164
http://togogenome.org/gene/9606:MTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94776                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BAH|||Disordered|||ELM2|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Metastasis-associated protein MTA2|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083496|||http://purl.uniprot.org/annotation/VSP_055083
http://togogenome.org/gene/9606:ZNF786                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N393                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 786                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293694|||http://purl.uniprot.org/annotation/VSP_055971
http://togogenome.org/gene/9606:CCL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80098                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 7|||Decreases binding to Link domain of TNFAIP6; when associated with A-41 and A-42.|||Decreases binding to Link domain of TNFAIP6; when associated with A-41 and A-45.|||Decreases binding to Link domain of TNFAIP6; when associated with A-42 and A-45.|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005183
http://togogenome.org/gene/9606:MFAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW70|||http://purl.uniprot.org/uniprot/F5GYX4|||http://purl.uniprot.org/uniprot/F5H413|||http://purl.uniprot.org/uniprot/Q13361                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||In AAT9; expression of the mutant protein is significantly decreased.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Microfibrillar-associated protein 5|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018685|||http://purl.uniprot.org/annotation/PRO_5003322988|||http://purl.uniprot.org/annotation/PRO_5003324759|||http://purl.uniprot.org/annotation/PRO_5014085056|||http://purl.uniprot.org/annotation/VAR_036430|||http://purl.uniprot.org/annotation/VAR_072688|||http://purl.uniprot.org/annotation/VSP_056618
http://togogenome.org/gene/9606:GSAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1B5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Gamma-secretase-activating protein|||Gamma-secretase-activating protein 16 kDa C-terminal form|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335809|||http://purl.uniprot.org/annotation/PRO_0000403728|||http://purl.uniprot.org/annotation/VAR_043467|||http://purl.uniprot.org/annotation/VAR_043468|||http://purl.uniprot.org/annotation/VAR_043469|||http://purl.uniprot.org/annotation/VAR_043470|||http://purl.uniprot.org/annotation/VSP_033771|||http://purl.uniprot.org/annotation/VSP_033772|||http://purl.uniprot.org/annotation/VSP_033773|||http://purl.uniprot.org/annotation/VSP_033774
http://togogenome.org/gene/9606:TUBGCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EQ3|||http://purl.uniprot.org/uniprot/Q9BSJ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gamma tubulin complex component C-terminal|||Gamma tubulin complex component protein N-terminal|||Gamma-tubulin complex component 2|||In PAMDDFS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078113|||http://purl.uniprot.org/annotation/VAR_022126|||http://purl.uniprot.org/annotation/VAR_049249|||http://purl.uniprot.org/annotation/VAR_049250|||http://purl.uniprot.org/annotation/VAR_083747|||http://purl.uniprot.org/annotation/VAR_083748|||http://purl.uniprot.org/annotation/VAR_083749|||http://purl.uniprot.org/annotation/VSP_044698|||http://purl.uniprot.org/annotation/VSP_045982
http://togogenome.org/gene/9606:ERICH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5RHP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glutamate-rich protein 3|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304972|||http://purl.uniprot.org/annotation/VAR_035131|||http://purl.uniprot.org/annotation/VAR_035132|||http://purl.uniprot.org/annotation/VAR_035133|||http://purl.uniprot.org/annotation/VAR_035134|||http://purl.uniprot.org/annotation/VAR_035135|||http://purl.uniprot.org/annotation/VAR_035136|||http://purl.uniprot.org/annotation/VSP_028159|||http://purl.uniprot.org/annotation/VSP_028160|||http://purl.uniprot.org/annotation/VSP_028161|||http://purl.uniprot.org/annotation/VSP_028162|||http://purl.uniprot.org/annotation/VSP_028163
http://togogenome.org/gene/9606:KCNQ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43526|||http://purl.uniprot.org/uniprot/Q53Y30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  40% increase in potassium current amplitude. Ratio of 1:1.|||Abolishes currents without reducing channel protein expression.|||Cytoplasmic|||Decrease of PKA stimulation. Ratio of 1:1.|||Disordered|||Extracellular|||Found in a patient with continuous spikes and waves during sleep; unknown pathological significance.|||Found in a patient with isolated myokymia; leads to a shift of voltage-dependent activation.|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In BFNS1 and DEE7.|||In BFNS1 and DEE7; 20%-40% reduction of wt current in heteromeric channels.|||In BFNS1 and DEE7; decreases the voltage-dependence of the channel.|||In BFNS1.|||In BFNS1; 30%-60% reduction of wt current in heteromeric channels.|||In BFNS1; also in patients with infantile seizures.|||In BFNS1; minor effect on maximal current but clearly exhibits a faster rate of deactivation.|||In BFNS1; moderate effect; less than 50% reduction in current compared with wt heteromeric channels.|||In BFNS1; phenotype manifestations include myokymia in some patients; leads to a shift of voltage-dependent activation of the channel and a dramatic slowing of activation upon depolarization.|||In BFNS1; unknown pathological significance.|||In BFNS1; with infantile seizures.|||In DEE7.|||In DEE7; gain-of-function mutation; results in loss of voltage-dependent channel gating and highly increased potassium currents.|||In DEE7; patient also manifests dyskinesia.|||In DEE7; reduces channel currents by more than 50% in homomeric channels.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Ion transport|||Mediates interaction with SLC5A3|||Mediates interaction with calmodulin|||More than 50% reduction of wt heteromeric current. Ratio of 1:1 and 1:1:2.|||No effect on current or expression.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 2|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054030|||http://purl.uniprot.org/annotation/VAR_010929|||http://purl.uniprot.org/annotation/VAR_010930|||http://purl.uniprot.org/annotation/VAR_010931|||http://purl.uniprot.org/annotation/VAR_010932|||http://purl.uniprot.org/annotation/VAR_026987|||http://purl.uniprot.org/annotation/VAR_026988|||http://purl.uniprot.org/annotation/VAR_026989|||http://purl.uniprot.org/annotation/VAR_026990|||http://purl.uniprot.org/annotation/VAR_026991|||http://purl.uniprot.org/annotation/VAR_026992|||http://purl.uniprot.org/annotation/VAR_026993|||http://purl.uniprot.org/annotation/VAR_043819|||http://purl.uniprot.org/annotation/VAR_078207|||http://purl.uniprot.org/annotation/VAR_078208|||http://purl.uniprot.org/annotation/VAR_078209|||http://purl.uniprot.org/annotation/VAR_078210|||http://purl.uniprot.org/annotation/VAR_078211|||http://purl.uniprot.org/annotation/VAR_078212|||http://purl.uniprot.org/annotation/VAR_078213|||http://purl.uniprot.org/annotation/VAR_078658|||http://purl.uniprot.org/annotation/VAR_078659|||http://purl.uniprot.org/annotation/VAR_078660|||http://purl.uniprot.org/annotation/VAR_078661|||http://purl.uniprot.org/annotation/VAR_078662|||http://purl.uniprot.org/annotation/VAR_078663|||http://purl.uniprot.org/annotation/VAR_078664|||http://purl.uniprot.org/annotation/VAR_078665|||http://purl.uniprot.org/annotation/VAR_078666|||http://purl.uniprot.org/annotation/VAR_078667|||http://purl.uniprot.org/annotation/VAR_078668|||http://purl.uniprot.org/annotation/VAR_078669|||http://purl.uniprot.org/annotation/VAR_078670|||http://purl.uniprot.org/annotation/VAR_078671|||http://purl.uniprot.org/annotation/VAR_078672|||http://purl.uniprot.org/annotation/VAR_078673|||http://purl.uniprot.org/annotation/VAR_078674|||http://purl.uniprot.org/annotation/VAR_078675|||http://purl.uniprot.org/annotation/VAR_078676|||http://purl.uniprot.org/annotation/VAR_078677|||http://purl.uniprot.org/annotation/VAR_078678|||http://purl.uniprot.org/annotation/VAR_078679|||http://purl.uniprot.org/annotation/VAR_078680|||http://purl.uniprot.org/annotation/VSP_000984|||http://purl.uniprot.org/annotation/VSP_000985|||http://purl.uniprot.org/annotation/VSP_000986|||http://purl.uniprot.org/annotation/VSP_000987|||http://purl.uniprot.org/annotation/VSP_000988|||http://purl.uniprot.org/annotation/VSP_000989|||http://purl.uniprot.org/annotation/VSP_000990
http://togogenome.org/gene/9606:IL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTG5|||http://purl.uniprot.org/uniprot/A8K673|||http://purl.uniprot.org/uniprot/P13232|||http://purl.uniprot.org/uniprot/Q5FBX5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In EV5.|||In isoform 2.|||In isoform 3.|||Interleukin-7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015623|||http://purl.uniprot.org/annotation/PRO_5001967146|||http://purl.uniprot.org/annotation/PRO_5002725458|||http://purl.uniprot.org/annotation/PRO_5014586754|||http://purl.uniprot.org/annotation/VAR_081934|||http://purl.uniprot.org/annotation/VSP_042926|||http://purl.uniprot.org/annotation/VSP_047579|||http://purl.uniprot.org/annotation/VSP_047580
http://togogenome.org/gene/9606:EIF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60739|||http://purl.uniprot.org/uniprot/Q6FG85                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 1b|||N-acetylserine|||Phosphoserine|||Removed|||SUI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130558
http://togogenome.org/gene/9606:ZNF446                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDK2|||http://purl.uniprot.org/uniprot/Q9NWS9|||http://purl.uniprot.org/uniprot/Q9UFF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SCAN box|||Zinc finger protein 446                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047596|||http://purl.uniprot.org/annotation/VAR_033566|||http://purl.uniprot.org/annotation/VAR_033567|||http://purl.uniprot.org/annotation/VAR_052833|||http://purl.uniprot.org/annotation/VSP_058945
http://togogenome.org/gene/9606:HSD3B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26439                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2|||Helical|||In AH2.|||In AH2; activity abolished.|||In AH2; late onset; almost normal activity.|||In AH2; late onset; partial loss of activity.|||In AH2; loss of 88% of activity.|||In AH2; mild; 100% of activity.|||In AH2; nonsalt-wasting form.|||In AH2; nonsalt-wasting form; activity abolished.|||In AH2; nonsalt-wasting form; loss of 75% of enzymatic activity for the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione; no effect on endoplasmic reticulum location.|||In AH2; strongly reduced activity.|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087775|||http://purl.uniprot.org/annotation/VAR_000006|||http://purl.uniprot.org/annotation/VAR_000007|||http://purl.uniprot.org/annotation/VAR_000008|||http://purl.uniprot.org/annotation/VAR_000009|||http://purl.uniprot.org/annotation/VAR_000010|||http://purl.uniprot.org/annotation/VAR_000011|||http://purl.uniprot.org/annotation/VAR_010517|||http://purl.uniprot.org/annotation/VAR_010518|||http://purl.uniprot.org/annotation/VAR_010519|||http://purl.uniprot.org/annotation/VAR_010520|||http://purl.uniprot.org/annotation/VAR_010521|||http://purl.uniprot.org/annotation/VAR_010522|||http://purl.uniprot.org/annotation/VAR_010523|||http://purl.uniprot.org/annotation/VAR_010524|||http://purl.uniprot.org/annotation/VAR_010525|||http://purl.uniprot.org/annotation/VAR_010526|||http://purl.uniprot.org/annotation/VAR_010527|||http://purl.uniprot.org/annotation/VAR_010528|||http://purl.uniprot.org/annotation/VAR_010529|||http://purl.uniprot.org/annotation/VAR_010530|||http://purl.uniprot.org/annotation/VAR_010531|||http://purl.uniprot.org/annotation/VAR_010532|||http://purl.uniprot.org/annotation/VAR_010533|||http://purl.uniprot.org/annotation/VAR_010534|||http://purl.uniprot.org/annotation/VAR_010535|||http://purl.uniprot.org/annotation/VAR_014818|||http://purl.uniprot.org/annotation/VAR_015411|||http://purl.uniprot.org/annotation/VAR_048099|||http://purl.uniprot.org/annotation/VAR_065665|||http://purl.uniprot.org/annotation/VAR_070028|||http://purl.uniprot.org/annotation/VAR_083841|||http://purl.uniprot.org/annotation/VSP_037399|||http://purl.uniprot.org/annotation/VSP_037400
http://togogenome.org/gene/9606:PAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13153                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autoinhibition, leading to constitutive kinase activity.|||Abolishes autophosphorylation at Thr-423.|||Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-83.|||Abolishes interaction with CDC42, leading to strongly decreased activity; when associated with L-86.|||Abolishes kinase activity; when associated with R-299.|||Autoregulatory region|||Basic and acidic residues|||CRIB|||Constitutive kinase activity.|||Decreases CDC42-stimulated activity and autophosphorylation.|||Disordered|||GTPase-binding|||In IDDMSSD; gain of function; enhanced PAK1 kinase activity and significantly reduced homodimerization.|||In IDDMSSD; gain-of-function; enhanced PAK1 kinase activity and significantly reduced homodimerization.|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKB and autocatalysis|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by OXSR1|||Phosphothreonine; by autocatalysis, BRSK2 and PDPK1|||Phosphotyrosine|||Phosphotyrosine; by JAK2|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase PAK 1|||Strongly decreases activity. Abolishes kinase activity; when associated with N-389.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086460|||http://purl.uniprot.org/annotation/VAR_051654|||http://purl.uniprot.org/annotation/VAR_081554|||http://purl.uniprot.org/annotation/VAR_081555|||http://purl.uniprot.org/annotation/VSP_017507
http://togogenome.org/gene/9606:LDB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6D0|||http://purl.uniprot.org/uniprot/E9PFI4|||http://purl.uniprot.org/uniprot/G5E9Y7|||http://purl.uniprot.org/uniprot/O43679                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||LIM domain-binding protein 2|||LIM interaction|||LIM interaction domain (LID)|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084387|||http://purl.uniprot.org/annotation/VSP_027825|||http://purl.uniprot.org/annotation/VSP_027826|||http://purl.uniprot.org/annotation/VSP_027827|||http://purl.uniprot.org/annotation/VSP_027828
http://togogenome.org/gene/9606:FLNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75369                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cytoplasmic localization.|||Disordered|||Filamin 1|||Filamin 10|||Filamin 11|||Filamin 12|||Filamin 13|||Filamin 14|||Filamin 15|||Filamin 16|||Filamin 17|||Filamin 18|||Filamin 19|||Filamin 2|||Filamin 20|||Filamin 21|||Filamin 22|||Filamin 23|||Filamin 24|||Filamin 3|||Filamin 4|||Filamin 5|||Filamin 6|||Filamin 7|||Filamin 8|||Filamin 9|||Filamin-B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Hinge 1|||Hinge 2|||In AO1 and AO3.|||In AO1.|||In AO3.|||In BOOMD.|||In LRS.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 7 and isoform 9.|||In isoform 7.|||In isoform 8.|||Interaction with FBLP1|||Interaction with FLNA 1|||Interaction with FLNA 2|||Interaction with INPPL1|||Interaction with the cytoplasmic tail of GP1BA|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Self-association site, tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087298|||http://purl.uniprot.org/annotation/VAR_017182|||http://purl.uniprot.org/annotation/VAR_017183|||http://purl.uniprot.org/annotation/VAR_031392|||http://purl.uniprot.org/annotation/VAR_031393|||http://purl.uniprot.org/annotation/VAR_033069|||http://purl.uniprot.org/annotation/VAR_033070|||http://purl.uniprot.org/annotation/VAR_033071|||http://purl.uniprot.org/annotation/VAR_033072|||http://purl.uniprot.org/annotation/VAR_033073|||http://purl.uniprot.org/annotation/VAR_033074|||http://purl.uniprot.org/annotation/VAR_033075|||http://purl.uniprot.org/annotation/VAR_033076|||http://purl.uniprot.org/annotation/VAR_033077|||http://purl.uniprot.org/annotation/VAR_033078|||http://purl.uniprot.org/annotation/VAR_033079|||http://purl.uniprot.org/annotation/VAR_033080|||http://purl.uniprot.org/annotation/VAR_033081|||http://purl.uniprot.org/annotation/VAR_033082|||http://purl.uniprot.org/annotation/VAR_033083|||http://purl.uniprot.org/annotation/VAR_033084|||http://purl.uniprot.org/annotation/VAR_033085|||http://purl.uniprot.org/annotation/VAR_033086|||http://purl.uniprot.org/annotation/VAR_033087|||http://purl.uniprot.org/annotation/VAR_035917|||http://purl.uniprot.org/annotation/VAR_035918|||http://purl.uniprot.org/annotation/VAR_035919|||http://purl.uniprot.org/annotation/VAR_035920|||http://purl.uniprot.org/annotation/VSP_008773|||http://purl.uniprot.org/annotation/VSP_008774|||http://purl.uniprot.org/annotation/VSP_008775|||http://purl.uniprot.org/annotation/VSP_008776|||http://purl.uniprot.org/annotation/VSP_008777|||http://purl.uniprot.org/annotation/VSP_008778|||http://purl.uniprot.org/annotation/VSP_024113|||http://purl.uniprot.org/annotation/VSP_024114|||http://purl.uniprot.org/annotation/VSP_024115|||http://purl.uniprot.org/annotation/VSP_043446
http://togogenome.org/gene/9606:KBTBD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes CUL3-binding and ability to mediate monoubiquitination of NOLC1 and TCOF1.|||Abolishes substrate-binding and ability to mediate monoubiquitination of NOLC1 and TCOF1.|||BACK|||BTB|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278220|||http://purl.uniprot.org/annotation/VAR_030694|||http://purl.uniprot.org/annotation/VAR_036082|||http://purl.uniprot.org/annotation/VAR_036083|||http://purl.uniprot.org/annotation/VSP_056107
http://togogenome.org/gene/9606:USP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AK7|||http://purl.uniprot.org/uniprot/Q13107                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by PKB/AKT1 in response to EGF signaling.|||Basic and acidic residues|||DUSP|||Disordered|||In isoform 2.|||In isoform 3.|||Interacts with DUSP and ubiquitin-like 1 domains and is required for USP4 activation|||Loss of thiol-dependent deubiquitinase activity. Its ubiquitination by TRIM21 is enhanced. Does affect interaction with HAS2. Does not deubiquitinate HAS2.|||Lowers affinity for ubiquitin characterized by a 10-fold increase in ubiquitin release and a slight reduction in ubiquitin binding.|||Mimics phosphorylation; promoting association with RHEB.|||Moderate reduction in thiol-dependent deubiquitinase activity.|||Necessary for interaction with RB1 and RBL2|||Necessary for interaction with RBL2|||Necessary for interaction with SART3|||Nuclear export signal|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Polar residues|||Proton acceptor|||Reduces the interaction with RB1.|||Regulates ubiquitin dissociation|||Required for USP4 activation by providing conformational flexibility between the DUSP and catalytic domains|||Severe reduction in thiol-dependent deubiquitinase activity.|||USP|||Ubiquitin carboxyl-terminal hydrolase 4|||Ubiquitin-like 1|||Ubiquitin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080621|||http://purl.uniprot.org/annotation/VAR_028180|||http://purl.uniprot.org/annotation/VSP_005258|||http://purl.uniprot.org/annotation/VSP_044814|||http://purl.uniprot.org/annotation/VSP_044815
http://togogenome.org/gene/9606:OLIG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13516                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Oligodendrocyte transcription factor 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127414
http://togogenome.org/gene/9606:POM121C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDR5|||http://purl.uniprot.org/uniprot/B4DET5                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TMIGD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXZ0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane and immunoglobulin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045790|||http://purl.uniprot.org/annotation/VSP_017075|||http://purl.uniprot.org/annotation/VSP_017076
http://togogenome.org/gene/9606:CSNK1G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78368                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Casein kinase I isoform gamma-2|||Disordered|||Phospho-regulated basic and hydrophobic (PRBH) motif|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192842|||http://purl.uniprot.org/annotation/VAR_042086|||http://purl.uniprot.org/annotation/VAR_042087|||http://purl.uniprot.org/annotation/VAR_042088|||http://purl.uniprot.org/annotation/VAR_042089|||http://purl.uniprot.org/annotation/VAR_042090|||http://purl.uniprot.org/annotation/VAR_042091|||http://purl.uniprot.org/annotation/VAR_042092|||http://purl.uniprot.org/annotation/VAR_042093|||http://purl.uniprot.org/annotation/VAR_042094
http://togogenome.org/gene/9606:ARFGEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6D6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes cAMP-induced nuclear localization.|||Basic and acidic residues|||Brefeldin A-inhibited guanine nucleotide-exchange protein 1|||DCB; DCB:DCB domain and DCB:HUS domain interaction|||Disordered|||HUS; DCB:HUS domain interaction|||In DEDISB.|||In DEDISB; decreased protein abundance.|||In a colorectal cancer sample; somatic mutation.|||Inhibits nuclear localization.|||LLoss of interaction with ARL1.|||Loss of interaction with ARL1.|||No effect on cAMP-induced nuclear localization.|||No effect on self-association.|||Nuclear localization signal (NLS)|||Phosphoserine|||Polar residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120207|||http://purl.uniprot.org/annotation/VAR_028749|||http://purl.uniprot.org/annotation/VAR_036155|||http://purl.uniprot.org/annotation/VAR_087629|||http://purl.uniprot.org/annotation/VAR_087630|||http://purl.uniprot.org/annotation/VAR_087631|||http://purl.uniprot.org/annotation/VAR_087632|||http://purl.uniprot.org/annotation/VAR_087633
http://togogenome.org/gene/9606:KANSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3B3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes KAT8 histone acetyltransferase activity.|||Abolishes interaction with KAT8.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In KDVS.|||In isoform 2 and isoform 3.|||In isoform 3.|||KAT8 regulatory NSL complex subunit 1|||N6-acetyllysine|||No effect on interaction with KAT8.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces KAT8 histone acetyltransferase activity.|||Required for activation of KAT8 histone acetyltransferase activity|||Strongly reduces KAT8 histone acetyltransferase activity.|||Sufficient for interaction with KAT8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234565|||http://purl.uniprot.org/annotation/VAR_026287|||http://purl.uniprot.org/annotation/VAR_049515|||http://purl.uniprot.org/annotation/VAR_049516|||http://purl.uniprot.org/annotation/VAR_049517|||http://purl.uniprot.org/annotation/VAR_049518|||http://purl.uniprot.org/annotation/VAR_049519|||http://purl.uniprot.org/annotation/VAR_081891|||http://purl.uniprot.org/annotation/VAR_081892|||http://purl.uniprot.org/annotation/VAR_081893|||http://purl.uniprot.org/annotation/VSP_041132|||http://purl.uniprot.org/annotation/VSP_041133|||http://purl.uniprot.org/annotation/VSP_058944
http://togogenome.org/gene/9606:MRPL34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ48                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein bL34m|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030520
http://togogenome.org/gene/9606:HDHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0R4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Haloacid dehalogenase-like hydrolase domain-containing protein 2|||In isoform 2.|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287203|||http://purl.uniprot.org/annotation/VAR_032289|||http://purl.uniprot.org/annotation/VSP_025373
http://togogenome.org/gene/9606:RPL34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49207                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL34|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131831
http://togogenome.org/gene/9606:TMEM234                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHR3|||http://purl.uniprot.org/uniprot/Q8WY98                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Transmembrane protein 234                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304697|||http://purl.uniprot.org/annotation/PRO_5002803025|||http://purl.uniprot.org/annotation/VSP_028105|||http://purl.uniprot.org/annotation/VSP_028106|||http://purl.uniprot.org/annotation/VSP_028107|||http://purl.uniprot.org/annotation/VSP_028108|||http://purl.uniprot.org/annotation/VSP_028109
http://togogenome.org/gene/9606:EID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6B2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes RB1 binding.|||Acidic residues|||Disordered|||EP300-interacting inhibitor of differentiation 1|||In isoform 2.|||Interaction with NR0B2|||LXCXE motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289156|||http://purl.uniprot.org/annotation/VSP_052454
http://togogenome.org/gene/9606:NPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SE8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Acidic tract A2|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||In isoform 2.|||Interaction between pentamers|||Nucleoplasmin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219487|||http://purl.uniprot.org/annotation/VSP_054261
http://togogenome.org/gene/9606:TXNDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBS9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Prevents secretion from ER|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3|||Thioredoxin domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034183|||http://purl.uniprot.org/annotation/VSP_045181
http://togogenome.org/gene/9606:SLC16A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15403                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Monocarboxylate transporter 7|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211400|||http://purl.uniprot.org/annotation/VAR_053656|||http://purl.uniprot.org/annotation/VAR_053657|||http://purl.uniprot.org/annotation/VAR_053658|||http://purl.uniprot.org/annotation/VAR_053659
http://togogenome.org/gene/9606:LRFN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTN0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type-III domain-containing protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014841|||http://purl.uniprot.org/annotation/VAR_049895
http://togogenome.org/gene/9606:GATM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK19|||http://purl.uniprot.org/uniprot/P50440                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Amidino-cysteine intermediate|||Complete loss of activity.|||Complete loss of activity; when associated with K-233.|||Complete loss of activity; when associated with S-407.|||Decreases glycine amidinotransferase activity.|||Glycine amidinotransferase, mitochondrial|||In CCDS3; decreases glycine amidinotransferase activity.|||In CCDS3; loss of glycine amidinotransferase activity.|||In CCDS3; unknown pathological significance; reduces glycine amidinotransferase activity.|||In FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology and are associated with increased ROS production, activation of the NLRP3 inflammasome and enhanced expression of the profibrotic cytokine IL-18.|||In FRTS1; results in GATM protein aggregation; GATM deposits affect mitochondrial morphology leading to abnormal and elongated mitochondria.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||No effect on activity.|||Phosphoserine|||Significantly reduced activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001206|||http://purl.uniprot.org/annotation/VAR_020305|||http://purl.uniprot.org/annotation/VAR_069816|||http://purl.uniprot.org/annotation/VAR_071789|||http://purl.uniprot.org/annotation/VAR_071790|||http://purl.uniprot.org/annotation/VAR_076483|||http://purl.uniprot.org/annotation/VAR_076484|||http://purl.uniprot.org/annotation/VAR_076485|||http://purl.uniprot.org/annotation/VAR_076486|||http://purl.uniprot.org/annotation/VAR_076487|||http://purl.uniprot.org/annotation/VAR_076488|||http://purl.uniprot.org/annotation/VAR_076489|||http://purl.uniprot.org/annotation/VAR_076490|||http://purl.uniprot.org/annotation/VAR_076491|||http://purl.uniprot.org/annotation/VAR_076492|||http://purl.uniprot.org/annotation/VAR_076493|||http://purl.uniprot.org/annotation/VAR_076494|||http://purl.uniprot.org/annotation/VAR_076495|||http://purl.uniprot.org/annotation/VAR_076496|||http://purl.uniprot.org/annotation/VAR_084378|||http://purl.uniprot.org/annotation/VAR_084379|||http://purl.uniprot.org/annotation/VAR_084380|||http://purl.uniprot.org/annotation/VAR_084381|||http://purl.uniprot.org/annotation/VSP_000235|||http://purl.uniprot.org/annotation/VSP_039871
http://togogenome.org/gene/9606:AMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A088AWN0|||http://purl.uniprot.org/uniprot/P17707|||http://purl.uniprot.org/uniprot/Q6N0B2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  17 percent decrease in catalytic activity. No effect on processing.|||24 percent decrease in catalytic activity. Slight reduction in processing.|||38 percent decrease in catalytic activity. Slight reduction in processing.|||Cleavage (non-hydrolytic); by autolysis|||Greatly reduced catalytic activity and processing.|||Greatly reduced catalytic activity but little effect on processing.|||Greatly reduced catalytic activity. No putrescine-stimulated processing.|||Greatly reduced processing.|||In isoform 2.|||Little effect.|||Loss of activity. Greatly reduced putrescine-stimulated processing.|||Loss of activity. Loss of putrescine-stimulated processing.|||Loss of activity. Normal putrescine-stimulated processing.|||Loss of catalytic activity and processing.|||Loss of processing.|||No effect.|||Phosphoserine|||Proton acceptor; for processing activity|||Proton donor; for catalytic activity|||Pyruvic acid (Ser); by autocatalysis|||S-adenosylmethionine decarboxylase alpha chain|||S-adenosylmethionine decarboxylase beta chain|||Schiff-base intermediate with substrate; via pyruvic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029959|||http://purl.uniprot.org/annotation/PRO_0000029960|||http://purl.uniprot.org/annotation/PRO_5036526309|||http://purl.uniprot.org/annotation/PRO_5036526310|||http://purl.uniprot.org/annotation/PRO_5036529116|||http://purl.uniprot.org/annotation/PRO_5036529117|||http://purl.uniprot.org/annotation/VSP_043209
http://togogenome.org/gene/9606:OR2V2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R30                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2V2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150510|||http://purl.uniprot.org/annotation/VAR_053160|||http://purl.uniprot.org/annotation/VAR_053161
http://togogenome.org/gene/9606:JPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Jupiter microtubule associated homolog 1|||Jupiter microtubule associated homolog 1, N-terminally processed|||N-acetylmethionine|||N-acetylthreonine; in Hematological and neurological expressed 1 protein, N-terminally processed|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054918|||http://purl.uniprot.org/annotation/PRO_0000424487|||http://purl.uniprot.org/annotation/VSP_017132|||http://purl.uniprot.org/annotation/VSP_017133
http://togogenome.org/gene/9606:ERV3-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14264                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  CKS-17|||CX6CC|||CXXC|||Cleavage|||Endogenous retrovirus group 3 member 1 Env polyprotein|||N-linked (GlcNAc...) asparagine|||Surface protein|||Transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008477|||http://purl.uniprot.org/annotation/PRO_0000008478|||http://purl.uniprot.org/annotation/PRO_0000008479|||http://purl.uniprot.org/annotation/VAR_017801|||http://purl.uniprot.org/annotation/VAR_017802|||http://purl.uniprot.org/annotation/VAR_017803|||http://purl.uniprot.org/annotation/VAR_017804|||http://purl.uniprot.org/annotation/VAR_017805|||http://purl.uniprot.org/annotation/VAR_017806
http://togogenome.org/gene/9606:PIWIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J94                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  D-box|||Disordered|||Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with H-379.|||Impairs binding to 2'-O-methylated 3'-end of piRNAs; when associated with Y-381.|||In isoform 2.|||In isoform 3.|||MID region|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; by PRMT5|||Omega-N-methylarginine; by PRMT5; alternate|||PAZ|||Piwi|||Piwi-like protein 1|||Polar residues|||Probable disease-associated variant found in a patient with azoospermia.|||Probable disease-associated variant found in a patient with azoospermia; requires 2 nucleotide substitutions.|||Required for binding 2'-O-methylated 3'-end of piRNAs|||Symmetric dimethylarginine; alternate|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234567|||http://purl.uniprot.org/annotation/VAR_026288|||http://purl.uniprot.org/annotation/VAR_026289|||http://purl.uniprot.org/annotation/VAR_026290|||http://purl.uniprot.org/annotation/VAR_078965|||http://purl.uniprot.org/annotation/VAR_078966|||http://purl.uniprot.org/annotation/VAR_078967|||http://purl.uniprot.org/annotation/VAR_078968|||http://purl.uniprot.org/annotation/VAR_078969|||http://purl.uniprot.org/annotation/VSP_018366|||http://purl.uniprot.org/annotation/VSP_018367|||http://purl.uniprot.org/annotation/VSP_018368|||http://purl.uniprot.org/annotation/VSP_018369
http://togogenome.org/gene/9606:LHX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68G74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295810|||http://purl.uniprot.org/annotation/VSP_047378
http://togogenome.org/gene/9606:SLC35G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N808                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA 1|||EamA 2|||Helical|||Solute carrier family 35 member G3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269553
http://togogenome.org/gene/9606:SPCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6A9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Interaction with HCV NS2 and HCV E2|||(Microbial infection) Interaction with JEV NS2B|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Signal peptidase complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215154
http://togogenome.org/gene/9606:HECTD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VWT9                                                                                  ^@                                                                                  Active Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||HECT|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ZNF518B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Zinc finger protein 518B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317255|||http://purl.uniprot.org/annotation/VAR_038491|||http://purl.uniprot.org/annotation/VAR_038492|||http://purl.uniprot.org/annotation/VAR_061955
http://togogenome.org/gene/9606:CALCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30988                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with change in bone mineral density.|||Calcitonin receptor|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000447620|||http://purl.uniprot.org/annotation/VAR_003580|||http://purl.uniprot.org/annotation/VSP_060209|||http://purl.uniprot.org/annotation/VSP_060211|||http://purl.uniprot.org/annotation/VSP_060212|||http://purl.uniprot.org/annotation/VSP_060213
http://togogenome.org/gene/9606:SSBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X159|||http://purl.uniprot.org/uniprot/P81877                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||LisH|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Single-stranded DNA-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123826|||http://purl.uniprot.org/annotation/VSP_044744|||http://purl.uniprot.org/annotation/VSP_044745|||http://purl.uniprot.org/annotation/VSP_045117|||http://purl.uniprot.org/annotation/VSP_045580
http://togogenome.org/gene/9606:LPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22079                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||In isoform 2.|||Lactoperoxidase|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton acceptor|||Transition state stabilizer|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023649|||http://purl.uniprot.org/annotation/PRO_0000023650|||http://purl.uniprot.org/annotation/VAR_018809|||http://purl.uniprot.org/annotation/VAR_018810|||http://purl.uniprot.org/annotation/VAR_018811|||http://purl.uniprot.org/annotation/VAR_018812|||http://purl.uniprot.org/annotation/VAR_018813|||http://purl.uniprot.org/annotation/VAR_018814|||http://purl.uniprot.org/annotation/VAR_018815|||http://purl.uniprot.org/annotation/VSP_044473
http://togogenome.org/gene/9606:PTCRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTE9|||http://purl.uniprot.org/uniprot/Q6ISU1|||http://purl.uniprot.org/uniprot/Q6ZNR1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Interchain (with TCRB)|||N-linked (GlcNAc...) asparagine|||Pre T-cell antigen receptor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319108|||http://purl.uniprot.org/annotation/PRO_5001831867|||http://purl.uniprot.org/annotation/PRO_5004283902|||http://purl.uniprot.org/annotation/VAR_038957|||http://purl.uniprot.org/annotation/VAR_038958|||http://purl.uniprot.org/annotation/VSP_031445|||http://purl.uniprot.org/annotation/VSP_031446
http://togogenome.org/gene/9606:RIMS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H426                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  C2|||In isoform 2.|||Phosphoserine|||Regulating synaptic membrane exocytosis protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190207|||http://purl.uniprot.org/annotation/VSP_044881
http://togogenome.org/gene/9606:WSB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC76|||http://purl.uniprot.org/uniprot/Q9Y6I7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||SOCS box|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat and SOCS box-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051457|||http://purl.uniprot.org/annotation/VAR_024701|||http://purl.uniprot.org/annotation/VSP_006792|||http://purl.uniprot.org/annotation/VSP_039111|||http://purl.uniprot.org/annotation/VSP_039112|||http://purl.uniprot.org/annotation/VSP_053402|||http://purl.uniprot.org/annotation/VSP_053403
http://togogenome.org/gene/9606:FOLR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41439                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Folate receptor gamma|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008810|||http://purl.uniprot.org/annotation/VAR_081429|||http://purl.uniprot.org/annotation/VSP_060090|||http://purl.uniprot.org/annotation/VSP_060091
http://togogenome.org/gene/9606:FXYD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59646                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FXYD domain-containing ion transport regulator 4|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010366
http://togogenome.org/gene/9606:CHFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes autoubiquitination in vitro.|||Abolishes autoubiquitination. Does not affect phosphorylation.|||Abolishes phosphorylation but not autoubiquitination; when associated with A-205.|||Abolishes phosphorylation but not autoubiquitination; when associated with A-39.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-635.|||Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-641.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase CHFR|||FHA|||Impairs poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1.|||In a patient with non small cell lung carcinomas.|||In a patient with non small cell lung carcinomas; homozygous.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PBZ-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055872|||http://purl.uniprot.org/annotation/VAR_017582|||http://purl.uniprot.org/annotation/VAR_017583|||http://purl.uniprot.org/annotation/VAR_017584|||http://purl.uniprot.org/annotation/VAR_017585|||http://purl.uniprot.org/annotation/VAR_017586|||http://purl.uniprot.org/annotation/VAR_017587|||http://purl.uniprot.org/annotation/VSP_009349|||http://purl.uniprot.org/annotation/VSP_009350|||http://purl.uniprot.org/annotation/VSP_038126|||http://purl.uniprot.org/annotation/VSP_038127
http://togogenome.org/gene/9606:IFIH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYX4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Associated with susceptibility to T1D19.|||CARD 1|||CARD 2|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Helicase ATP-binding|||Helicase C-terminal|||In AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness.|||In AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis.|||In AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis.|||In IMD95; does not bind the double-stranded RNA analog poly(I:C); loss of IFNB1 and NFKB promoter activation after stimulation with poly(I:C), when tested in a luciferase reporter assay.|||In IMD95; no protein detected by Western blot in homozygous patient cells.|||In SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction.|||In isoform 2.|||Increases ISGylation.|||Inhibits multimerization after polyI:C stimulation.|||Interferon-induced helicase C domain-containing protein 1|||Loss of ISGylation, loss of oligomerization, strongly reduced signaling activity and IFNB induction, loss of virus replication restriction, no effect on phosphorylation or RNA-binding; when associated with A-23.|||Loss of ISGylation, loss of oligomerization, strongly reduced signaling activity and IFNB induction, loss of virus replication restriction, no effect on phosphorylation or RNA-binding; when associated with A-43.|||Loss of dsRNA-induced ATPase activity. Loss of MDA-5 signaling pathway.|||Loss of dsRNA-induced ATPase activity. No effect on MDA-5 signaling pathway.|||Loss of dsRNA-induced ATPase activity. No effect on RNA binding. Changed MDA-5 signaling pathway.|||Loss of oligomerization.|||Loss of signaling activity and IFNB induction. Reduced ISGylation. Loss of virus replication restriction.|||Moderately increases signaling.|||No acceleration of DNA degradation, no binding to ATP, and no helicase activity.|||No cleavage and no acceleration of DNA degradation.|||No effect on ISGylation or signaling activity and IFNB induction.|||Phosphoserine|||Phosphoserine; by RIOK3|||Polar residues|||Promotes multimerization after polyI:C stimulation; greatly enhances signaling.|||RLR CTR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102012|||http://purl.uniprot.org/annotation/VAR_021594|||http://purl.uniprot.org/annotation/VAR_021595|||http://purl.uniprot.org/annotation/VAR_031226|||http://purl.uniprot.org/annotation/VAR_071375|||http://purl.uniprot.org/annotation/VAR_071376|||http://purl.uniprot.org/annotation/VAR_071377|||http://purl.uniprot.org/annotation/VAR_071378|||http://purl.uniprot.org/annotation/VAR_071379|||http://purl.uniprot.org/annotation/VAR_071380|||http://purl.uniprot.org/annotation/VAR_071381|||http://purl.uniprot.org/annotation/VAR_071382|||http://purl.uniprot.org/annotation/VAR_073666|||http://purl.uniprot.org/annotation/VAR_087007|||http://purl.uniprot.org/annotation/VAR_087008|||http://purl.uniprot.org/annotation/VSP_013337|||http://purl.uniprot.org/annotation/VSP_013338
http://togogenome.org/gene/9606:OR10G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGC3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150695|||http://purl.uniprot.org/annotation/VAR_053270|||http://purl.uniprot.org/annotation/VAR_053271|||http://purl.uniprot.org/annotation/VAR_053272|||http://purl.uniprot.org/annotation/VAR_053273|||http://purl.uniprot.org/annotation/VAR_085741|||http://purl.uniprot.org/annotation/VAR_085742|||http://purl.uniprot.org/annotation/VAR_085743
http://togogenome.org/gene/9606:KLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4J4|||http://purl.uniprot.org/uniprot/B4DU77|||http://purl.uniprot.org/uniprot/P20151                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kallikrein-2|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027929|||http://purl.uniprot.org/annotation/PRO_0000027930|||http://purl.uniprot.org/annotation/PRO_5014214237|||http://purl.uniprot.org/annotation/VAR_014164|||http://purl.uniprot.org/annotation/VAR_020178|||http://purl.uniprot.org/annotation/VAR_061775|||http://purl.uniprot.org/annotation/VSP_005399|||http://purl.uniprot.org/annotation/VSP_005400|||http://purl.uniprot.org/annotation/VSP_044709
http://togogenome.org/gene/9606:NDUFV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19404                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial|||Phosphotyrosine; by SRC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020003|||http://purl.uniprot.org/annotation/VAR_016167
http://togogenome.org/gene/9606:ZNF850                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0M6|||http://purl.uniprot.org/uniprot/A8MQ14                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20; degenerate|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 2; degenerate|||C2H2-type 30|||C2H2-type 31|||C2H2-type 32|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 850                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332269
http://togogenome.org/gene/9606:MXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLI7|||http://purl.uniprot.org/uniprot/Q05195                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Motif|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  BHLH|||Disordered|||In isoform 2.|||Max dimerization protein 1|||Nuclear localization signal|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127264|||http://purl.uniprot.org/annotation/VSP_043074
http://togogenome.org/gene/9606:MAGEA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43362                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156708|||http://purl.uniprot.org/annotation/VAR_064160
http://togogenome.org/gene/9606:ADAMTSL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VD77|||http://purl.uniprot.org/uniprot/Q6ZMM2|||http://purl.uniprot.org/uniprot/X6R4H8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ADAMTS-like protein 5|||ADAMTS/ADAMTS-like Spacer 1|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NTR|||Pro residues|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249582|||http://purl.uniprot.org/annotation/PRO_5004977044|||http://purl.uniprot.org/annotation/VSP_053358
http://togogenome.org/gene/9606:UBN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ubinuclein-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295725|||http://purl.uniprot.org/annotation/VAR_033347|||http://purl.uniprot.org/annotation/VSP_027021|||http://purl.uniprot.org/annotation/VSP_027022
http://togogenome.org/gene/9606:OR4S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVU1|||http://purl.uniprot.org/uniprot/Q8NGB4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150568
http://togogenome.org/gene/9606:ARHGAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13017                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Basic and acidic residues|||Basic residues|||Disordered|||FF 1|||FF 2|||FF 3|||FF 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Rho GTPase-activating protein 5|||Rho-GAP|||pG1 pseudoGTPase|||pG2 pseudoGTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056702|||http://purl.uniprot.org/annotation/VAR_043980|||http://purl.uniprot.org/annotation/VSP_034164|||http://purl.uniprot.org/annotation/VSP_034165|||http://purl.uniprot.org/annotation/VSP_034166|||http://purl.uniprot.org/annotation/VSP_034167
http://togogenome.org/gene/9606:OR51B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWB2|||http://purl.uniprot.org/uniprot/Q9Y5P1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150745|||http://purl.uniprot.org/annotation/VAR_057576|||http://purl.uniprot.org/annotation/VAR_063114|||http://purl.uniprot.org/annotation/VAR_063115|||http://purl.uniprot.org/annotation/VAR_063116|||http://purl.uniprot.org/annotation/VAR_063117
http://togogenome.org/gene/9606:PEX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56589                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with D-134.|||Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with P-125.|||Cytoplasmic|||Helical|||In PBD10A.|||In PBD10B.|||Interaction with PEX19|||Peroxisomal|||Peroxisomal biogenesis factor 3|||Targeting to peroxisomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208737|||http://purl.uniprot.org/annotation/VAR_009304|||http://purl.uniprot.org/annotation/VAR_053572|||http://purl.uniprot.org/annotation/VAR_078657
http://togogenome.org/gene/9606:MAP2K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46734|||http://purl.uniprot.org/uniprot/Q6FI23                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Constitutive activation.|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 3|||In colon cancer.|||In isoform 1.|||In isoform 2.|||Inactivation.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086378|||http://purl.uniprot.org/annotation/VAR_014208|||http://purl.uniprot.org/annotation/VAR_014209|||http://purl.uniprot.org/annotation/VAR_040817|||http://purl.uniprot.org/annotation/VAR_046062|||http://purl.uniprot.org/annotation/VAR_046063|||http://purl.uniprot.org/annotation/VAR_046064|||http://purl.uniprot.org/annotation/VAR_046065|||http://purl.uniprot.org/annotation/VAR_046066|||http://purl.uniprot.org/annotation/VAR_046067|||http://purl.uniprot.org/annotation/VAR_046068|||http://purl.uniprot.org/annotation/VAR_046069|||http://purl.uniprot.org/annotation/VAR_061742|||http://purl.uniprot.org/annotation/VSP_004877|||http://purl.uniprot.org/annotation/VSP_004878
http://togogenome.org/gene/9606:SYNJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SGJ6|||http://purl.uniprot.org/uniprot/B9EGN3|||http://purl.uniprot.org/uniprot/C9JFZ1|||http://purl.uniprot.org/uniprot/J3KQV8|||http://purl.uniprot.org/uniprot/O43426|||http://purl.uniprot.org/uniprot/Q05CZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 3 AA repeats of N-P-F|||Catalytic|||Disordered|||In DEE53; decreased inositol phosphate phosphatase activity.|||In PARK20.|||In PARK20; impairs the phosphatase activity of the enzyme toward phosphatidylinositol-3-phosphate and phosphatidylinositol-4-phosphate.|||In PARK20; unknown pathological significance; the patient also carries a heterozygous PINK1 truncating mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Likely benign variant; no effect on inositol phosphate phosphatase activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||SAC|||Synaptojanin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209730|||http://purl.uniprot.org/annotation/VAR_047308|||http://purl.uniprot.org/annotation/VAR_047309|||http://purl.uniprot.org/annotation/VAR_049603|||http://purl.uniprot.org/annotation/VAR_070905|||http://purl.uniprot.org/annotation/VAR_070906|||http://purl.uniprot.org/annotation/VAR_078803|||http://purl.uniprot.org/annotation/VAR_078804|||http://purl.uniprot.org/annotation/VAR_078805|||http://purl.uniprot.org/annotation/VAR_078806|||http://purl.uniprot.org/annotation/VSP_002682|||http://purl.uniprot.org/annotation/VSP_002683|||http://purl.uniprot.org/annotation/VSP_035709|||http://purl.uniprot.org/annotation/VSP_035710|||http://purl.uniprot.org/annotation/VSP_035711|||http://purl.uniprot.org/annotation/VSP_041578
http://togogenome.org/gene/9606:CYP3A43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB55                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 3A43|||In allele CYP3A43*2.|||In allele CYP3A43*3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 7.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051814|||http://purl.uniprot.org/annotation/VAR_018050|||http://purl.uniprot.org/annotation/VAR_018051|||http://purl.uniprot.org/annotation/VAR_018052|||http://purl.uniprot.org/annotation/VAR_048449|||http://purl.uniprot.org/annotation/VAR_048450|||http://purl.uniprot.org/annotation/VAR_048451|||http://purl.uniprot.org/annotation/VSP_000609|||http://purl.uniprot.org/annotation/VSP_000610|||http://purl.uniprot.org/annotation/VSP_000611|||http://purl.uniprot.org/annotation/VSP_000612|||http://purl.uniprot.org/annotation/VSP_000613|||http://purl.uniprot.org/annotation/VSP_056736
http://togogenome.org/gene/9606:USP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2K6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-643.|||Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-154.|||Basic and acidic residues|||DUSP 1|||DUSP 2|||Disordered|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080647|||http://purl.uniprot.org/annotation/VAR_051529|||http://purl.uniprot.org/annotation/VAR_051530
http://togogenome.org/gene/9606:ASMTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM43|||http://purl.uniprot.org/uniprot/O95671                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  ASMT-like|||Acetylserotonin O-methyltransferase dimerisation|||Decrease in pyrophosphatase activity.|||Disordered|||Important for substrate specificity; for pyrophosphatase activity|||In isoform 2.|||In isoform 3.|||Loss of pyrophosphatase activity.|||MAF-like|||O-methyltransferase|||Phosphoserine|||Phosphothreonine|||Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein|||Proton acceptor; for pyrophosphatase activity|||Strong decrease in pyrophosphatase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064702|||http://purl.uniprot.org/annotation/VAR_054802|||http://purl.uniprot.org/annotation/VAR_054803|||http://purl.uniprot.org/annotation/VSP_007213|||http://purl.uniprot.org/annotation/VSP_047412
http://togogenome.org/gene/9606:SLC6A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  50% reduction of GABA-uptake.|||90% reduction of GABA-uptake.|||Complete loss of GABA-uptake.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sodium- and chloride-dependent GABA transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214792|||http://purl.uniprot.org/annotation/VAR_011594|||http://purl.uniprot.org/annotation/VSP_043070|||http://purl.uniprot.org/annotation/VSP_044887|||http://purl.uniprot.org/annotation/VSP_044888
http://togogenome.org/gene/9606:C18orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I7GY12|||http://purl.uniprot.org/uniprot/I7HAS0|||http://purl.uniprot.org/uniprot/Q8IYD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Lung adenoma susceptibility protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019561|||http://purl.uniprot.org/annotation/VAR_050903|||http://purl.uniprot.org/annotation/VAR_050904|||http://purl.uniprot.org/annotation/VSP_015085
http://togogenome.org/gene/9606:PROKR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCW9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Prokineticin receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070079|||http://purl.uniprot.org/annotation/VAR_024261
http://togogenome.org/gene/9606:MAPK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEW2|||http://purl.uniprot.org/uniprot/K7ELV1|||http://purl.uniprot.org/uniprot/P31152                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FRIEDE motif|||Mitogen-activated protein kinase 4|||Phosphoserine|||Phosphoserine; by PAK1, PAK2 and PAK3|||Protein kinase|||Proton acceptor|||SEG motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186254|||http://purl.uniprot.org/annotation/VAR_042254|||http://purl.uniprot.org/annotation/VAR_042255
http://togogenome.org/gene/9606:GOLGA6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VDJ1|||http://purl.uniprot.org/uniprot/Q9NYA3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A conserved|||Golgin subfamily A member 6A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190069|||http://purl.uniprot.org/annotation/VAR_047540
http://togogenome.org/gene/9606:S100A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05109                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Loss of antifungal activity.|||Protein S100-A8|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143993
http://togogenome.org/gene/9606:BOK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4A8|||http://purl.uniprot.org/uniprot/Q9UMX3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  BH1|||BH2|||BH3|||BH4|||Bcl-2 Bcl-2 homology region 1-3|||Bcl-2-related ovarian killer protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Interactions with ITPR1|||Nuclear export signal|||Phosphoserine|||Significantly accumulates in the nucleus. Increases apoptotic activity. Does not interact with XPO1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143086|||http://purl.uniprot.org/annotation/VSP_058599
http://togogenome.org/gene/9606:CAB39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y376                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation of STK11/LKB1; when associated with A-240.|||Abolishes activation of STK11/LKB1; when associated with A-243.|||Calcium-binding protein 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209824
http://togogenome.org/gene/9606:CELA3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08861                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 3B|||N-linked (GlcNAc...) asparagine|||Or 16|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000212|||http://purl.uniprot.org/annotation/PRO_0000027699|||http://purl.uniprot.org/annotation/PRO_0000027700|||http://purl.uniprot.org/annotation/VAR_025446
http://togogenome.org/gene/9606:MYOM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52179                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 6 AA tandem repeats|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2.|||Myomesin-1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072684|||http://purl.uniprot.org/annotation/VAR_047221|||http://purl.uniprot.org/annotation/VAR_047222|||http://purl.uniprot.org/annotation/VAR_047223|||http://purl.uniprot.org/annotation/VAR_047224|||http://purl.uniprot.org/annotation/VAR_047225|||http://purl.uniprot.org/annotation/VAR_047226|||http://purl.uniprot.org/annotation/VAR_047227|||http://purl.uniprot.org/annotation/VAR_047228|||http://purl.uniprot.org/annotation/VSP_035663
http://togogenome.org/gene/9606:HSDL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YN16                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Hydroxysteroid dehydrogenase-like protein 2|||In isoform 2.|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-succinyllysine|||Proton acceptor|||SCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319888|||http://purl.uniprot.org/annotation/VSP_031529
http://togogenome.org/gene/9606:SCAMP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K8F5|||http://purl.uniprot.org/uniprot/Q8TAC9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Secretory carrier-associated membrane protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191262|||http://purl.uniprot.org/annotation/VSP_010206|||http://purl.uniprot.org/annotation/VSP_036934
http://togogenome.org/gene/9606:YPEL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62699                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Phosphoserine|||Protein yippee-like 5|||Yippee                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212396
http://togogenome.org/gene/9606:GOLT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3E0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||N-acetylmethionine|||Vesicle transport protein GOT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218582
http://togogenome.org/gene/9606:CDY2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Chromo|||Disordered|||Polar residues|||Testis-specific chromodomain protein Y 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080220
http://togogenome.org/gene/9606:ABCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92887                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 2|||Altered transporter activity.|||Cytoplasmic|||Decreased expression.|||Decreased expression; altered subcellular localization; altered transporter activity.|||Decreased expression; altered subcellular localization; decreased transporter activity.|||Decreased transporter activity.|||Disordered|||Extracellular|||Fails to transport methotrexate and leukotriene C4. Does not affect estradiol glucuronide transport.|||Fails to transport methotrexate, leukotriene C4 and estradiol glucuronide.|||Fails to transport methotrexate; reduces leukotriene C4 transport. Does not affect estradiol glucuronide transport.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=16|||Helical; Name=17|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In DJS.|||In DJS; decreased expression and mislocation to the endoplasmic reticulum.|||In DJS; impaired transport from the endoplasmic reticulum to the apical plasma membrane associated with impaired maturation.|||In DJS; protein is properly localized at the plasma membrane, but transporter activity is impaired.|||N-linked (GlcNAc...) asparagine|||No effect on transporter activity.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093356|||http://purl.uniprot.org/annotation/VAR_000099|||http://purl.uniprot.org/annotation/VAR_010756|||http://purl.uniprot.org/annotation/VAR_013324|||http://purl.uniprot.org/annotation/VAR_013325|||http://purl.uniprot.org/annotation/VAR_013326|||http://purl.uniprot.org/annotation/VAR_013327|||http://purl.uniprot.org/annotation/VAR_013328|||http://purl.uniprot.org/annotation/VAR_013329|||http://purl.uniprot.org/annotation/VAR_013330|||http://purl.uniprot.org/annotation/VAR_020226|||http://purl.uniprot.org/annotation/VAR_020227|||http://purl.uniprot.org/annotation/VAR_020228|||http://purl.uniprot.org/annotation/VAR_020229|||http://purl.uniprot.org/annotation/VAR_020230|||http://purl.uniprot.org/annotation/VAR_020231|||http://purl.uniprot.org/annotation/VAR_020232|||http://purl.uniprot.org/annotation/VAR_020233|||http://purl.uniprot.org/annotation/VAR_020234|||http://purl.uniprot.org/annotation/VAR_024360|||http://purl.uniprot.org/annotation/VAR_029113|||http://purl.uniprot.org/annotation/VAR_029115|||http://purl.uniprot.org/annotation/VAR_029116|||http://purl.uniprot.org/annotation/VAR_029117|||http://purl.uniprot.org/annotation/VAR_029118|||http://purl.uniprot.org/annotation/VAR_047152|||http://purl.uniprot.org/annotation/VAR_070607|||http://purl.uniprot.org/annotation/VAR_070608|||http://purl.uniprot.org/annotation/VAR_070609|||http://purl.uniprot.org/annotation/VAR_070610
http://togogenome.org/gene/9606:DGCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3T5|||http://purl.uniprot.org/uniprot/P98153|||http://purl.uniprot.org/uniprot/Q5CZ70|||http://purl.uniprot.org/uniprot/Q8IWC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Integral membrane protein DGCR2/IDD|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021484|||http://purl.uniprot.org/annotation/PRO_5002866175|||http://purl.uniprot.org/annotation/PRO_5004308666|||http://purl.uniprot.org/annotation/PRO_5040057985|||http://purl.uniprot.org/annotation/VAR_020046|||http://purl.uniprot.org/annotation/VSP_042886|||http://purl.uniprot.org/annotation/VSP_057188|||http://purl.uniprot.org/annotation/VSP_057189
http://togogenome.org/gene/9606:EDEM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J8YX80|||http://purl.uniprot.org/uniprot/Q9BZQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 3|||In CDG2V; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PA|||Polar residues|||Prevents secretion from ER|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210323|||http://purl.uniprot.org/annotation/VAR_059306|||http://purl.uniprot.org/annotation/VAR_086113|||http://purl.uniprot.org/annotation/VAR_086114|||http://purl.uniprot.org/annotation/VAR_086115|||http://purl.uniprot.org/annotation/VAR_086116|||http://purl.uniprot.org/annotation/VSP_056375|||http://purl.uniprot.org/annotation/VSP_056376
http://togogenome.org/gene/9606:LVRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P5U8|||http://purl.uniprot.org/uniprot/Q6Q4G3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aminopeptidase N-like N-terminal|||Aminopeptidase Q|||Cytoplasmic|||Disordered|||ERAP1-like C-terminal|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M1 membrane alanine aminopeptidase|||Polar residues|||Proton acceptor|||Proton donor|||Removed|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247068|||http://purl.uniprot.org/annotation/VAR_027059|||http://purl.uniprot.org/annotation/VAR_027060|||http://purl.uniprot.org/annotation/VAR_027061|||http://purl.uniprot.org/annotation/VSP_019915|||http://purl.uniprot.org/annotation/VSP_019916|||http://purl.uniprot.org/annotation/VSP_019917|||http://purl.uniprot.org/annotation/VSP_019918|||http://purl.uniprot.org/annotation/VSP_019919|||http://purl.uniprot.org/annotation/VSP_019920|||http://purl.uniprot.org/annotation/VSP_019921
http://togogenome.org/gene/9606:GAST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0E3VY36|||http://purl.uniprot.org/uniprot/P01350                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Big gastrin|||Cleavage|||Disordered|||Gastrin|||Gastrin-14|||Gastrin-52|||Gastrin-6|||Gastrin-71|||Gastrin/cholecystokinin peptide hormone|||Phenylalanine amide|||Phosphoserine|||Pyrrolidone carboxylic acid; in form big gastrin|||Pyrrolidone carboxylic acid; in form gastrin|||Removed in mature form|||Small decrease in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with D-86.|||Small increase in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with F-87.|||Sulfotyrosine; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010633|||http://purl.uniprot.org/annotation/PRO_0000010634|||http://purl.uniprot.org/annotation/PRO_0000010635|||http://purl.uniprot.org/annotation/PRO_0000010636|||http://purl.uniprot.org/annotation/PRO_0000010637|||http://purl.uniprot.org/annotation/PRO_0000010638|||http://purl.uniprot.org/annotation/PRO_0000010639|||http://purl.uniprot.org/annotation/PRO_5014224654|||http://purl.uniprot.org/annotation/VAR_049127
http://togogenome.org/gene/9606:CNKSR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9H4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  CRIC|||Connector enhancer of kinase suppressor of ras 3|||DUF1170|||Disordered|||PDZ|||Phosphoserine|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311105
http://togogenome.org/gene/9606:AMER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N944                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  APC membrane recruitment protein 3|||Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320594|||http://purl.uniprot.org/annotation/VAR_039218
http://togogenome.org/gene/9606:OR5D16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGK9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5D16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150593|||http://purl.uniprot.org/annotation/VAR_034223
http://togogenome.org/gene/9606:PCDHA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||Polar residues|||Protocadherin alpha-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003894|||http://purl.uniprot.org/annotation/VAR_061061|||http://purl.uniprot.org/annotation/VSP_000681|||http://purl.uniprot.org/annotation/VSP_000682|||http://purl.uniprot.org/annotation/VSP_000683
http://togogenome.org/gene/9606:POLR2I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36954                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase II subunit RPB9|||N-acetylmethionine|||TFIIS-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121467
http://togogenome.org/gene/9606:TOE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GM8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||In PCH7.|||In PCH7; reduced protein levels.|||In PCH7; reduced protein levels; decreased function in snRNA 3'-end processing.|||In isoform 2.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||Target of EGR1 protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270833|||http://purl.uniprot.org/annotation/VAR_048752|||http://purl.uniprot.org/annotation/VAR_061109|||http://purl.uniprot.org/annotation/VAR_078809|||http://purl.uniprot.org/annotation/VAR_078850|||http://purl.uniprot.org/annotation/VAR_078851|||http://purl.uniprot.org/annotation/VAR_078852|||http://purl.uniprot.org/annotation/VAR_078853|||http://purl.uniprot.org/annotation/VAR_078854|||http://purl.uniprot.org/annotation/VAR_078855|||http://purl.uniprot.org/annotation/VAR_078856|||http://purl.uniprot.org/annotation/VAR_078857|||http://purl.uniprot.org/annotation/VAR_078858|||http://purl.uniprot.org/annotation/VAR_078859|||http://purl.uniprot.org/annotation/VSP_055529
http://togogenome.org/gene/9606:ATP5MF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56134                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ATP synthase subunit f, mitochondrial|||Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194824|||http://purl.uniprot.org/annotation/VSP_000437|||http://purl.uniprot.org/annotation/VSP_046746
http://togogenome.org/gene/9606:PNPLA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NST1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-acylglycerol-3-phosphate O-acyltransferase PNPLA3|||65% loss of 1-acylglycerol-3-phosphate O-acyltransferase catalytic activity.|||67% loss of 1-acylglycerol-3-phosphate O-acyltransferase catalytic activity.|||Associated with increased hepatic fat content and serum aspartate aminotransferase concentrations; probable gain-of-function variant; 2-fold increase in 1-acylglycerol-3-phosphate O-acyltransferase/lysophosphatidic acid acyltransferase activity; results on glycerolipid hydrolysis activity are controversial with reduction in triacylglycerol, diacylglycerol and monoacylglycerol hydrolase activity or no effect compared to wild-type in which this activity may be very low; does not affect subcellular location, nor association with lipid droplets.|||Associated with lower hepatic fat content in African Americans.|||Cytoplasmic|||DGA/G|||GXGXXG|||GXSXG|||Helical; Signal-anchor for type II membrane protein|||In NAFLD1; unknown pathological significance.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on 1-acylglycerol-3-phosphate O-acyltransferase catalytic activity.|||No effect on 1-acylglycerol-3-phosphate O-acyltransferase catalytic activity. Almost completely abolishes triacylglycerol, diacylglycerol and monoacylglycerol hydrolase activity.|||Nucleophile|||PNPLA|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064458|||http://purl.uniprot.org/annotation/VAR_015845|||http://purl.uniprot.org/annotation/VAR_015846|||http://purl.uniprot.org/annotation/VAR_015847|||http://purl.uniprot.org/annotation/VAR_019961|||http://purl.uniprot.org/annotation/VAR_053814|||http://purl.uniprot.org/annotation/VAR_053815|||http://purl.uniprot.org/annotation/VAR_077543|||http://purl.uniprot.org/annotation/VAR_077544|||http://purl.uniprot.org/annotation/VAR_077545|||http://purl.uniprot.org/annotation/VSP_036222
http://togogenome.org/gene/9606:ZSCAN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJ42|||http://purl.uniprot.org/uniprot/O43309                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047403|||http://purl.uniprot.org/annotation/VSP_061227
http://togogenome.org/gene/9606:CCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13500                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  40% reduction in activity.|||50% reduction in activity.|||83% reduction in activity.|||90% reduction in activity.|||95% reduction in activity; strong reduction of receptor binding.|||Abolishes binding to Link domain of TNFAIP6.|||C-C motif chemokine 2|||Involved in GAG binding|||Involved in GAG binding and receptor binding|||Involved in dimerization|||Involved in dimerization, receptor binding and signaling|||Loss of activity.|||Loss of dimerization; slight reduction of activity.|||Loss of signaling.|||N-linked (GlcNAc...) asparagine|||No effect on heparin binding.|||Pyrrolidone carboxylic acid|||Reduction in activity.|||Slight reduction in activity.|||Slight reduction in affinity.|||Strongly reduces heparin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005146
http://togogenome.org/gene/9606:TCP11L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQZ4|||http://purl.uniprot.org/uniprot/Q9NUJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||T-complex protein 11-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313747|||http://purl.uniprot.org/annotation/VAR_037726|||http://purl.uniprot.org/annotation/VAR_037727
http://togogenome.org/gene/9606:RASL10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S79                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In a breast cancer sample; somatic mutation.|||Ras-like protein family member 10B|||Removed in mature form|||S-geranylgeranyl cysteine|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280800|||http://purl.uniprot.org/annotation/PRO_0000281362|||http://purl.uniprot.org/annotation/VAR_036309
http://togogenome.org/gene/9606:PDE4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27815                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||PDEase|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Polar residues|||Pro residues|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198806|||http://purl.uniprot.org/annotation/VAR_059544|||http://purl.uniprot.org/annotation/VAR_059545|||http://purl.uniprot.org/annotation/VSP_004556|||http://purl.uniprot.org/annotation/VSP_004557|||http://purl.uniprot.org/annotation/VSP_004558|||http://purl.uniprot.org/annotation/VSP_004559|||http://purl.uniprot.org/annotation/VSP_004560|||http://purl.uniprot.org/annotation/VSP_004561|||http://purl.uniprot.org/annotation/VSP_038185|||http://purl.uniprot.org/annotation/VSP_038186
http://togogenome.org/gene/9606:OR13G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGZ3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150739|||http://purl.uniprot.org/annotation/VAR_048038|||http://purl.uniprot.org/annotation/VAR_062067|||http://purl.uniprot.org/annotation/VAR_062068|||http://purl.uniprot.org/annotation/VAR_062069
http://togogenome.org/gene/9606:LYSET                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6I4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In DMAN; lower protein expression. Fails to rescue the lysosomal trafficking defect in LYSET-deficient cells. Severe reduction of interaction with GNPTAB.|||In DMAN; no protein expression. Fails to rescue the lysosomal trafficking defect in LYSET-deficient cells.|||In isoform 2.|||In isoform 3.|||Lysosomal enzyme trafficking factor|||Rescues the lysosomal trafficking defect in LYSET-deficient cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089916|||http://purl.uniprot.org/annotation/VAR_085583|||http://purl.uniprot.org/annotation/VAR_087348|||http://purl.uniprot.org/annotation/VSP_036175|||http://purl.uniprot.org/annotation/VSP_045689
http://togogenome.org/gene/9606:MARCHF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UD3                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase MARCHF3|||Helical|||In isoform 2.|||Phosphoserine|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055927|||http://purl.uniprot.org/annotation/VAR_053639|||http://purl.uniprot.org/annotation/VSP_055451|||http://purl.uniprot.org/annotation/VSP_055452
http://togogenome.org/gene/9606:CNNM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4Q7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CBS 1|||CBS 2|||CNNM transmembrane|||Cytoplasmic|||Extracellular|||Helical|||In JALIS.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Metal transporter CNNM4|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295765|||http://purl.uniprot.org/annotation/VAR_033365|||http://purl.uniprot.org/annotation/VAR_035946|||http://purl.uniprot.org/annotation/VAR_058319|||http://purl.uniprot.org/annotation/VAR_058320|||http://purl.uniprot.org/annotation/VAR_058321|||http://purl.uniprot.org/annotation/VAR_058322|||http://purl.uniprot.org/annotation/VSP_054271|||http://purl.uniprot.org/annotation/VSP_054272
http://togogenome.org/gene/9606:LIMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN0|||http://purl.uniprot.org/uniprot/Q9BT23                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||LIM domain-containing protein 2|||LIM zinc-binding|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251207
http://togogenome.org/gene/9606:SRGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6B7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||In NMTC2; does not affect the interaction with ROBO1; decreased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42.|||In NMTC2; does not affect the interaction with ROBO1; slightly increased GTPase activator activity; in SLIT2 and ROBO1-mediated inhibition of CDC42.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056765|||http://purl.uniprot.org/annotation/VAR_075879|||http://purl.uniprot.org/annotation/VAR_075880|||http://purl.uniprot.org/annotation/VAR_075881|||http://purl.uniprot.org/annotation/VAR_075882|||http://purl.uniprot.org/annotation/VAR_075883|||http://purl.uniprot.org/annotation/VSP_010580
http://togogenome.org/gene/9606:TRIM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZR9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||Complete loss of ubiquitination activity on MAP3K7/TAK1.|||Complete loss of ubiquitination activity on TICAM1.|||E3 ubiquitin-protein ligase TRIM8|||In FSGSNEDS.|||In FSGSNEDS; also found in a patient with Coffin-Siris syndrome carrying a likely causative ARID2 mutation.|||In FSGSNEDS; disrupts localization to nuclear bodies.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056206|||http://purl.uniprot.org/annotation/VAR_080568|||http://purl.uniprot.org/annotation/VAR_086209|||http://purl.uniprot.org/annotation/VAR_086210|||http://purl.uniprot.org/annotation/VAR_086211|||http://purl.uniprot.org/annotation/VAR_086212|||http://purl.uniprot.org/annotation/VAR_086213|||http://purl.uniprot.org/annotation/VAR_086214|||http://purl.uniprot.org/annotation/VAR_086215|||http://purl.uniprot.org/annotation/VAR_086216|||http://purl.uniprot.org/annotation/VAR_086217
http://togogenome.org/gene/9606:CATSPERE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SY80                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit epsilon|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251216|||http://purl.uniprot.org/annotation/VAR_027661|||http://purl.uniprot.org/annotation/VAR_035494|||http://purl.uniprot.org/annotation/VAR_061566|||http://purl.uniprot.org/annotation/VSP_020748|||http://purl.uniprot.org/annotation/VSP_020749|||http://purl.uniprot.org/annotation/VSP_044251
http://togogenome.org/gene/9606:SEZ6L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYL5|||http://purl.uniprot.org/uniprot/A0A0A8K8P7|||http://purl.uniprot.org/uniprot/B7Z5L4|||http://purl.uniprot.org/uniprot/Q6UXD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||CUB 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||Pro residues|||Seizure 6-like protein 2|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333888|||http://purl.uniprot.org/annotation/PRO_5001832088|||http://purl.uniprot.org/annotation/PRO_5002038600|||http://purl.uniprot.org/annotation/PRO_5002863966|||http://purl.uniprot.org/annotation/VAR_065205|||http://purl.uniprot.org/annotation/VSP_033595|||http://purl.uniprot.org/annotation/VSP_033596|||http://purl.uniprot.org/annotation/VSP_033597|||http://purl.uniprot.org/annotation/VSP_044739|||http://purl.uniprot.org/annotation/VSP_045702|||http://purl.uniprot.org/annotation/VSP_045703
http://togogenome.org/gene/9606:ALOX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18054                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alteredarachidonate 12(S)-lipoxygenase activity and protein expression.|||Complete loss of arachidonate 12(S)-lipoxygenase activity.|||Does not affect lipoxygenase activity.|||Lipoxygenase|||No effect on arachidonate 12(S)-lipoxygenase activity.|||No effect onarachidonate 12(S)-lipoxygenase activity. No effect on the stereoselectivity of the oxygenation reaction.|||PLAT|||Phosphoserine|||Polyunsaturated fatty acid lipoxygenase ALOX12|||Reduced arachidonate 12(S)-lipoxygenase activity. Alters the stereoselectivity of the oxygenation reaction.|||Reduced arachidonate 12(S)-lipoxygenase activity. No effect on the stereoselectivity of the oxygenation reaction.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220682|||http://purl.uniprot.org/annotation/VAR_004279|||http://purl.uniprot.org/annotation/VAR_018743|||http://purl.uniprot.org/annotation/VAR_018744|||http://purl.uniprot.org/annotation/VAR_018745|||http://purl.uniprot.org/annotation/VAR_030471|||http://purl.uniprot.org/annotation/VAR_082032
http://togogenome.org/gene/9606:HTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15516                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  10-fold reduction in candidacidal activity of His3-(20-43)-peptide; when associated with E-32.|||3-fold reduction in candidacidal activity of His3-(20-43)-peptide.|||Basic residues|||Disordered|||His3-(20-30)-peptide|||His3-(20-31)-peptide|||His3-(20-32)-peptide|||His3-(20-43)-peptide|||His3-(20-44)-peptide|||His3-(24-30)-peptide|||His3-(24-31)-peptide|||His3-(24-32)-peptide|||His3-(25-30)-peptide|||His3-(25-32)-peptide|||His3-(26-30)-peptide|||His3-(26-31)-peptide|||His3-(26-32)-peptide|||His3-(31-43)-peptide|||His3-(31-44)-peptide|||His3-(31-51)-peptide|||His3-(32-43)-peptide|||His3-(32-44)-peptide|||His3-(33-43)-peptide|||His3-(33-44)-peptide|||His3-(34-43)-peptide|||His3-(34-44)-peptide|||His3-(45-51)-peptide|||His3-(47-51)-peptide|||His3-(48-51)-peptide|||Histatin-3|||Important for candidacidal activity|||In histatin-3-2.|||In histatin-3-2; loss of the proteolytic cleavage site.|||No effect on candidacidal activity of His3-(20-43)-peptide.|||Not sulfated                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021418|||http://purl.uniprot.org/annotation/PRO_0000021419|||http://purl.uniprot.org/annotation/PRO_0000021420|||http://purl.uniprot.org/annotation/PRO_0000021421|||http://purl.uniprot.org/annotation/PRO_0000021422|||http://purl.uniprot.org/annotation/PRO_0000021423|||http://purl.uniprot.org/annotation/PRO_0000021424|||http://purl.uniprot.org/annotation/PRO_0000021425|||http://purl.uniprot.org/annotation/PRO_0000021426|||http://purl.uniprot.org/annotation/PRO_0000021427|||http://purl.uniprot.org/annotation/PRO_0000021428|||http://purl.uniprot.org/annotation/PRO_0000021429|||http://purl.uniprot.org/annotation/PRO_0000021430|||http://purl.uniprot.org/annotation/PRO_0000021431|||http://purl.uniprot.org/annotation/PRO_0000021432|||http://purl.uniprot.org/annotation/PRO_0000021433|||http://purl.uniprot.org/annotation/PRO_0000021434|||http://purl.uniprot.org/annotation/PRO_0000021435|||http://purl.uniprot.org/annotation/PRO_0000021436|||http://purl.uniprot.org/annotation/PRO_0000021437|||http://purl.uniprot.org/annotation/PRO_0000021438|||http://purl.uniprot.org/annotation/PRO_0000021439|||http://purl.uniprot.org/annotation/PRO_0000021440|||http://purl.uniprot.org/annotation/PRO_0000021441|||http://purl.uniprot.org/annotation/PRO_0000021442|||http://purl.uniprot.org/annotation/PRO_0000021443|||http://purl.uniprot.org/annotation/VAR_005288|||http://purl.uniprot.org/annotation/VAR_005289
http://togogenome.org/gene/9606:DPYSL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14531                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Dihydropyrimidinase-related protein 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165921
http://togogenome.org/gene/9606:FZD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13467                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-5|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012990|||http://purl.uniprot.org/annotation/VAR_049291
http://togogenome.org/gene/9606:RPAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6T3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylthreonine|||Phosphoserine|||RNA polymerase II-associated protein 3|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302794|||http://purl.uniprot.org/annotation/VAR_057354|||http://purl.uniprot.org/annotation/VSP_027957|||http://purl.uniprot.org/annotation/VSP_044882
http://togogenome.org/gene/9606:WASHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0Z3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes ubiquitination by the TRIM27:MAGEL2 E3 ubiquitin ligase complex and impairs retrograde transport.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs retrograde transport from endosome to Golgi apparatus.|||Polar residues|||Pro residues|||Required for WASH complex assembly|||VCA|||WASH complex subunit 1|||WH2|||WHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329013
http://togogenome.org/gene/9606:SLC35G6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7Q6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA 1|||EamA 2|||Helical|||Solute carrier family 35 member G6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342676|||http://purl.uniprot.org/annotation/VAR_044335|||http://purl.uniprot.org/annotation/VAR_044336|||http://purl.uniprot.org/annotation/VAR_059581
http://togogenome.org/gene/9606:WWC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULE0|||http://purl.uniprot.org/uniprot/T2C6S4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Protein WWC3|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244494|||http://purl.uniprot.org/annotation/VAR_036969|||http://purl.uniprot.org/annotation/VAR_036970|||http://purl.uniprot.org/annotation/VAR_062109|||http://purl.uniprot.org/annotation/VSP_029220|||http://purl.uniprot.org/annotation/VSP_029221
http://togogenome.org/gene/9606:CYC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08574                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome c|||Cytochrome c1, heme protein, mitochondrial|||Helical|||In MC3DN6.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006554|||http://purl.uniprot.org/annotation/VAR_013631|||http://purl.uniprot.org/annotation/VAR_025163|||http://purl.uniprot.org/annotation/VAR_070847|||http://purl.uniprot.org/annotation/VAR_070848
http://togogenome.org/gene/9606:CALHM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5C1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 5|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186726
http://togogenome.org/gene/9606:ZNF71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQZ8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Endothelial zinc finger protein induced by tumor necrosis factor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047381|||http://purl.uniprot.org/annotation/VAR_024196|||http://purl.uniprot.org/annotation/VAR_052762|||http://purl.uniprot.org/annotation/VAR_052763
http://togogenome.org/gene/9606:TMEM125                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AQ2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||Transmembrane protein 125                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251716|||http://purl.uniprot.org/annotation/VAR_035669|||http://purl.uniprot.org/annotation/VAR_051428
http://togogenome.org/gene/9606:NDUFB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1T5|||http://purl.uniprot.org/uniprot/O95178                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Region|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020042
http://togogenome.org/gene/9606:PIK3R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFG1|||http://purl.uniprot.org/uniprot/P27986                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Does not affect insulin-stimulated lipid kinase activity.|||In SHORTS; impairs interaction between PIK3R1 and IRS1 and reduces AKT1-mediated insulin signaling.|||In SHORTS; there is 70 to 90% reduction in the effect of insulin on AKT1 activation, glycogen synthesis and glucose uptake, indicating severe insulin resistance for both proximal and distal PI3K-dependent signaling.|||In a patient with severe insulin resistance; lower insulin-stimulated lipid kinase activity compared with wild-type.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylserine|||Phosphatidylinositol 3-kinase regulatory subunit alpha|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Removed|||Rho-GAP|||SH2|||SH2 1|||SH2 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080758|||http://purl.uniprot.org/annotation/VAR_010023|||http://purl.uniprot.org/annotation/VAR_010024|||http://purl.uniprot.org/annotation/VAR_029562|||http://purl.uniprot.org/annotation/VAR_070221|||http://purl.uniprot.org/annotation/VAR_070222|||http://purl.uniprot.org/annotation/VAR_070223|||http://purl.uniprot.org/annotation/VSP_021841|||http://purl.uniprot.org/annotation/VSP_021842|||http://purl.uniprot.org/annotation/VSP_021843|||http://purl.uniprot.org/annotation/VSP_021844|||http://purl.uniprot.org/annotation/VSP_021845|||http://purl.uniprot.org/annotation/VSP_045903
http://togogenome.org/gene/9606:ZNF766                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HY98                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 766                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280435|||http://purl.uniprot.org/annotation/VAR_052899
http://togogenome.org/gene/9606:TBC1D3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431607
http://togogenome.org/gene/9606:SNRNP35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16560                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||RRM|||U11/U12 small nuclear ribonucleoprotein 35 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307907|||http://purl.uniprot.org/annotation/VSP_028855
http://togogenome.org/gene/9606:SALL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEH2|||http://purl.uniprot.org/uniprot/A9JR48|||http://purl.uniprot.org/uniprot/Q9BXA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 10|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 1 and isoform 2.|||In isoform 2 and isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||Sal-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047024|||http://purl.uniprot.org/annotation/VAR_014132|||http://purl.uniprot.org/annotation/VAR_035552|||http://purl.uniprot.org/annotation/VAR_059887|||http://purl.uniprot.org/annotation/VSP_006832|||http://purl.uniprot.org/annotation/VSP_006833
http://togogenome.org/gene/9606:TMPRSS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98073                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Enteropeptidase catalytic light chain|||Enteropeptidase non-catalytic heavy chain|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (between heavy and light chains)|||LDL-receptor class A 1|||LDL-receptor class A 2|||MAM|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Peptidase S1|||Removed|||SEA|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027719|||http://purl.uniprot.org/annotation/PRO_0000027720|||http://purl.uniprot.org/annotation/VAR_020175|||http://purl.uniprot.org/annotation/VAR_021940|||http://purl.uniprot.org/annotation/VAR_024292|||http://purl.uniprot.org/annotation/VAR_031686|||http://purl.uniprot.org/annotation/VAR_031687|||http://purl.uniprot.org/annotation/VAR_031688|||http://purl.uniprot.org/annotation/VAR_031689|||http://purl.uniprot.org/annotation/VAR_031690
http://togogenome.org/gene/9606:MTBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with MDM2|||Mdm2-binding protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323745|||http://purl.uniprot.org/annotation/VSP_056108|||http://purl.uniprot.org/annotation/VSP_056109
http://togogenome.org/gene/9606:CABP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57796                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcium-binding protein 4|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In CRSD.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073521|||http://purl.uniprot.org/annotation/VAR_029375|||http://purl.uniprot.org/annotation/VSP_012700|||http://purl.uniprot.org/annotation/VSP_012701
http://togogenome.org/gene/9606:MAGEA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAE8|||http://purl.uniprot.org/uniprot/P43363                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 10|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156709|||http://purl.uniprot.org/annotation/VAR_024528|||http://purl.uniprot.org/annotation/VAR_053496
http://togogenome.org/gene/9606:GLO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04760|||http://purl.uniprot.org/uniprot/X5DNM4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Alternate|||Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20.|||In isoform 2.|||Lactoylglutathione lyase|||Loss of phosphorylation.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on NO-mediated modification.|||No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-19. Loss of NO-mediated modification; when associated with A-139.|||No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-20. Loss of NO-mediated modification; when associated with A-139.|||No effect on phosphorylation.|||Phosphothreonine|||Proton donor/acceptor|||Reduces enzyme activity by 99%.|||Reduces enzyme activity by over 99%.|||Removed|||S-glutathionyl cysteine; alternate|||VOC|||Variant Ala-111. The measured range is 2-184.|||Variant Glu-111. The measured range is 2-184.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168076|||http://purl.uniprot.org/annotation/VAR_013481|||http://purl.uniprot.org/annotation/VAR_031078|||http://purl.uniprot.org/annotation/VSP_041632
http://togogenome.org/gene/9606:RGSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLK6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||RGS|||Regulator of G-protein signaling protein-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349305|||http://purl.uniprot.org/annotation/VAR_046356|||http://purl.uniprot.org/annotation/VAR_046357|||http://purl.uniprot.org/annotation/VSP_035347|||http://purl.uniprot.org/annotation/VSP_035348|||http://purl.uniprot.org/annotation/VSP_035349|||http://purl.uniprot.org/annotation/VSP_035350|||http://purl.uniprot.org/annotation/VSP_035351|||http://purl.uniprot.org/annotation/VSP_035352|||http://purl.uniprot.org/annotation/VSP_035353|||http://purl.uniprot.org/annotation/VSP_035354
http://togogenome.org/gene/9606:TPMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51580                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Allele TPMT*2; TPMT*2 allele frequency is 0.5%; seems to be restricted to the Caucasian population; 100-fold reduction in activity; protein shows enhanced degradation.|||Allele TPMT*3A and allele TPMT*3B; very low activity; protein shows enhanced degradation leading to strongly reduced protein levels.|||Allele TPMT*3B and allele TPMT*3C; reduced activity; protein shows enhanced degradation.|||Allele TPMT*5; has very low activity when expressed in a heterologous system.|||Allele TPMT*6; reduced activity.|||Allele TPMT*7; reduced activity.|||Allele TPMT*8; intermediate activity.|||Decreases affinity for 6-mercaptopurine. Slightly decreases catalytic activity.|||N6-acetyllysine|||Phosphoserine|||Thiopurine S-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220102|||http://purl.uniprot.org/annotation/VAR_005636|||http://purl.uniprot.org/annotation/VAR_005637|||http://purl.uniprot.org/annotation/VAR_005638|||http://purl.uniprot.org/annotation/VAR_005639|||http://purl.uniprot.org/annotation/VAR_005640|||http://purl.uniprot.org/annotation/VAR_005641|||http://purl.uniprot.org/annotation/VAR_008715|||http://purl.uniprot.org/annotation/VAR_052368
http://togogenome.org/gene/9606:CLEC2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7M8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 2 member L|||Disordered|||Helical|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339385
http://togogenome.org/gene/9606:LCLAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM26|||http://purl.uniprot.org/uniprot/B4DYR5|||http://purl.uniprot.org/uniprot/Q6UWP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes LPIAT activity. No effect on LPGAT activity.|||Abolishes LPIAT and LPGAT activities.|||Acyltransferase C-terminal|||Does not increase enzyme activity.|||HXXXXD motif|||Helical|||In isoform 2.|||In isoform 3.|||Lysocardiolipin acyltransferase 1|||N6-acetyllysine|||Phospholipid/glycerol acyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291577|||http://purl.uniprot.org/annotation/VAR_032830|||http://purl.uniprot.org/annotation/VSP_026181|||http://purl.uniprot.org/annotation/VSP_026182|||http://purl.uniprot.org/annotation/VSP_044307
http://togogenome.org/gene/9606:MVK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDU6|||http://purl.uniprot.org/uniprot/B7Z301|||http://purl.uniprot.org/uniprot/F5H8H2|||http://purl.uniprot.org/uniprot/Q03426                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  GHMP kinase C-terminal|||GHMP kinase N-terminal|||In HIDS and MEVA.|||In HIDS and POROK3.|||In HIDS.|||In HIDS; most frequent mutation.|||In MEVA and HIDS.|||In MEVA.|||In MEVA; diminished activity.|||In POROK3.|||Mevalonate kinase|||Modest changes in KM for ATP. 100-fold increase in KM for mevalonate. Approximately 2-fold increase in Vmax.|||Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. 4000-fold decrease in Vmax.|||Modest changes in KM for ATP. 20-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax.|||Modest changes in KM for ATP. 40-fold increase in KM for mevalonate. Approximately 2-fold decrease in Vmax.|||No change in protein stability. Decreased kinase activity. Approximately 50-fold decrease in Vmax. Approximately 20- and 40-fold decrease affinities for ATP and mevalonate, respectively.|||No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate.|||No change in protein stability. No effect on kinase activity.|||No change in protein stability. Weak decrease in kinase activity. Approximately 2-fold decrease in Vmax. Approximately 2-fold decrease affinity for ATP and mevalonate.|||No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively.|||No effect on kinase activity. Approximately 4- and 5-fold decrease affinities for ATP and mevalonate, respectively.|||No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively.|||No effect on kinase activity. Approximately 4-fold increase affinity for ATP. Normal affinity for mevalonate.|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156657|||http://purl.uniprot.org/annotation/VAR_004022|||http://purl.uniprot.org/annotation/VAR_004023|||http://purl.uniprot.org/annotation/VAR_004024|||http://purl.uniprot.org/annotation/VAR_004025|||http://purl.uniprot.org/annotation/VAR_004026|||http://purl.uniprot.org/annotation/VAR_004027|||http://purl.uniprot.org/annotation/VAR_009068|||http://purl.uniprot.org/annotation/VAR_010956|||http://purl.uniprot.org/annotation/VAR_010957|||http://purl.uniprot.org/annotation/VAR_010958|||http://purl.uniprot.org/annotation/VAR_010959|||http://purl.uniprot.org/annotation/VAR_010960|||http://purl.uniprot.org/annotation/VAR_010961|||http://purl.uniprot.org/annotation/VAR_010962|||http://purl.uniprot.org/annotation/VAR_010963|||http://purl.uniprot.org/annotation/VAR_010964|||http://purl.uniprot.org/annotation/VAR_010965|||http://purl.uniprot.org/annotation/VAR_010966|||http://purl.uniprot.org/annotation/VAR_010967|||http://purl.uniprot.org/annotation/VAR_010968|||http://purl.uniprot.org/annotation/VAR_029519|||http://purl.uniprot.org/annotation/VAR_029520|||http://purl.uniprot.org/annotation/VAR_029521|||http://purl.uniprot.org/annotation/VAR_029522|||http://purl.uniprot.org/annotation/VAR_029523|||http://purl.uniprot.org/annotation/VAR_029524|||http://purl.uniprot.org/annotation/VAR_029525|||http://purl.uniprot.org/annotation/VAR_029526|||http://purl.uniprot.org/annotation/VAR_029527|||http://purl.uniprot.org/annotation/VAR_075036|||http://purl.uniprot.org/annotation/VAR_075037|||http://purl.uniprot.org/annotation/VAR_075038|||http://purl.uniprot.org/annotation/VAR_075039|||http://purl.uniprot.org/annotation/VAR_075040|||http://purl.uniprot.org/annotation/VAR_075041|||http://purl.uniprot.org/annotation/VAR_075042|||http://purl.uniprot.org/annotation/VAR_075043
http://togogenome.org/gene/9606:HNRNPM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52272|||http://purl.uniprot.org/uniprot/Q59ES8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-[DE]-[RH]-[MLVI]-[GAV]|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein M|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081864|||http://purl.uniprot.org/annotation/VSP_005845
http://togogenome.org/gene/9606:SEMG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02383                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  2-1|||2-2|||3-1|||3-2|||4 X 60 AA tandem repeats, type I|||Basic and acidic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues|||Repeat-rich region|||Semenogelin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032359|||http://purl.uniprot.org/annotation/VAR_024630|||http://purl.uniprot.org/annotation/VAR_024631|||http://purl.uniprot.org/annotation/VAR_034489|||http://purl.uniprot.org/annotation/VAR_034490|||http://purl.uniprot.org/annotation/VAR_034491
http://togogenome.org/gene/9606:HOXD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31277                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D11|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200231|||http://purl.uniprot.org/annotation/VAR_031647
http://togogenome.org/gene/9606:ASS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00966                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Argininosuccinate synthase|||In CTLN1.|||In CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; decreased protein abundance.|||In CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity.|||In CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity.|||In CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; increased thermal stability; loss of argininosuccinate synthase activity.|||In CTLN1; loss of argininosuccinate synthase activity.|||In CTLN1; mild clinical course.|||In CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity.|||In CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity.|||In CTLN1; severe clinical course.|||In CTLN1; severe clinical course; loss of argininosuccinate synthase activity.|||In CTLN1; unknown pathological significance.|||Increased thermal stability; loss of argininosuccinate synthase activity.|||N6-acetyllysine|||N6-acetyllysine; by CLOCK|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.|||Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148554|||http://purl.uniprot.org/annotation/VAR_000681|||http://purl.uniprot.org/annotation/VAR_000682|||http://purl.uniprot.org/annotation/VAR_000683|||http://purl.uniprot.org/annotation/VAR_000684|||http://purl.uniprot.org/annotation/VAR_000685|||http://purl.uniprot.org/annotation/VAR_000686|||http://purl.uniprot.org/annotation/VAR_000687|||http://purl.uniprot.org/annotation/VAR_000688|||http://purl.uniprot.org/annotation/VAR_000689|||http://purl.uniprot.org/annotation/VAR_000690|||http://purl.uniprot.org/annotation/VAR_000691|||http://purl.uniprot.org/annotation/VAR_000692|||http://purl.uniprot.org/annotation/VAR_000693|||http://purl.uniprot.org/annotation/VAR_000694|||http://purl.uniprot.org/annotation/VAR_015891|||http://purl.uniprot.org/annotation/VAR_015892|||http://purl.uniprot.org/annotation/VAR_015893|||http://purl.uniprot.org/annotation/VAR_015894|||http://purl.uniprot.org/annotation/VAR_015895|||http://purl.uniprot.org/annotation/VAR_015896|||http://purl.uniprot.org/annotation/VAR_015897|||http://purl.uniprot.org/annotation/VAR_015898|||http://purl.uniprot.org/annotation/VAR_015899|||http://purl.uniprot.org/annotation/VAR_015900|||http://purl.uniprot.org/annotation/VAR_015901|||http://purl.uniprot.org/annotation/VAR_015902|||http://purl.uniprot.org/annotation/VAR_015903|||http://purl.uniprot.org/annotation/VAR_015904|||http://purl.uniprot.org/annotation/VAR_016007|||http://purl.uniprot.org/annotation/VAR_016008|||http://purl.uniprot.org/annotation/VAR_016009|||http://purl.uniprot.org/annotation/VAR_016010|||http://purl.uniprot.org/annotation/VAR_016011|||http://purl.uniprot.org/annotation/VAR_016012|||http://purl.uniprot.org/annotation/VAR_016013|||http://purl.uniprot.org/annotation/VAR_016014|||http://purl.uniprot.org/annotation/VAR_016015|||http://purl.uniprot.org/annotation/VAR_058337|||http://purl.uniprot.org/annotation/VAR_058338|||http://purl.uniprot.org/annotation/VAR_058339|||http://purl.uniprot.org/annotation/VAR_058340|||http://purl.uniprot.org/annotation/VAR_058341|||http://purl.uniprot.org/annotation/VAR_058342|||http://purl.uniprot.org/annotation/VAR_058343|||http://purl.uniprot.org/annotation/VAR_058344|||http://purl.uniprot.org/annotation/VAR_058345|||http://purl.uniprot.org/annotation/VAR_058346|||http://purl.uniprot.org/annotation/VAR_058347|||http://purl.uniprot.org/annotation/VAR_058348|||http://purl.uniprot.org/annotation/VAR_058349|||http://purl.uniprot.org/annotation/VAR_058350|||http://purl.uniprot.org/annotation/VAR_058351|||http://purl.uniprot.org/annotation/VAR_058352|||http://purl.uniprot.org/annotation/VAR_058353|||http://purl.uniprot.org/annotation/VAR_058354|||http://purl.uniprot.org/annotation/VAR_058355|||http://purl.uniprot.org/annotation/VAR_058356|||http://purl.uniprot.org/annotation/VAR_058357|||http://purl.uniprot.org/annotation/VAR_058358|||http://purl.uniprot.org/annotation/VAR_058359|||http://purl.uniprot.org/annotation/VAR_058360|||http://purl.uniprot.org/annotation/VAR_072792|||http://purl.uniprot.org/annotation/VAR_078387|||http://purl.uniprot.org/annotation/VAR_078388|||http://purl.uniprot.org/annotation/VAR_078389|||http://purl.uniprot.org/annotation/VAR_078390|||http://purl.uniprot.org/annotation/VAR_078391|||http://purl.uniprot.org/annotation/VAR_078392|||http://purl.uniprot.org/annotation/VAR_078393|||http://purl.uniprot.org/annotation/VAR_078394|||http://purl.uniprot.org/annotation/VAR_078395|||http://purl.uniprot.org/annotation/VAR_078396|||http://purl.uniprot.org/annotation/VAR_078397|||http://purl.uniprot.org/annotation/VAR_078398|||http://purl.uniprot.org/annotation/VAR_078399|||http://purl.uniprot.org/annotation/VAR_078400|||http://purl.uniprot.org/annotation/VAR_078401|||http://purl.uniprot.org/annotation/VAR_078402|||http://purl.uniprot.org/annotation/VAR_078403|||http://purl.uniprot.org/annotation/VAR_078404|||http://purl.uniprot.org/annotation/VAR_078405|||http://purl.uniprot.org/annotation/VAR_078406|||http://purl.uniprot.org/annotation/VAR_078407|||http://purl.uniprot.org/annotation/VAR_078408|||http://purl.uniprot.org/annotation/VAR_078409|||http://purl.uniprot.org/annotation/VAR_078410|||http://purl.uniprot.org/annotation/VAR_078411|||http://purl.uniprot.org/annotation/VAR_078412|||http://purl.uniprot.org/annotation/VAR_078413|||http://purl.uniprot.org/annotation/VAR_078414|||http://purl.uniprot.org/annotation/VAR_078415|||http://purl.uniprot.org/annotation/VAR_078416|||http://purl.uniprot.org/annotation/VAR_078417|||http://purl.uniprot.org/annotation/VAR_078418|||http://purl.uniprot.org/annotation/VAR_078419|||http://purl.uniprot.org/annotation/VAR_078420|||http://purl.uniprot.org/annotation/VAR_078421|||http://purl.uniprot.org/annotation/VAR_078422
http://togogenome.org/gene/9606:SLC7A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30825                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||High affinity cationic amino acid transporter 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054261
http://togogenome.org/gene/9606:POLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PY44|||http://purl.uniprot.org/uniprot/H0YDR7|||http://purl.uniprot.org/uniprot/Q14181                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA polymerase alpha subunit B|||DNA polymerase alpha subunit B N-terminal|||DNA polymerase alpha/delta/epsilon subunit B|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194035|||http://purl.uniprot.org/annotation/VAR_033896|||http://purl.uniprot.org/annotation/VAR_033897|||http://purl.uniprot.org/annotation/VSP_056608|||http://purl.uniprot.org/annotation/VSP_056609
http://togogenome.org/gene/9606:ACYP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2U7|||http://purl.uniprot.org/uniprot/P07311                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acylphosphatase|||Acylphosphatase-1|||Acylphosphatase-like|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158535|||http://purl.uniprot.org/annotation/PRO_5003457339|||http://purl.uniprot.org/annotation/VSP_045688
http://togogenome.org/gene/9606:HPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00739                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Haptoglobin-related protein|||In isoform 2.|||Not cleaved|||Peptidase S1|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028486|||http://purl.uniprot.org/annotation/VAR_014571|||http://purl.uniprot.org/annotation/VAR_057161|||http://purl.uniprot.org/annotation/VAR_057162|||http://purl.uniprot.org/annotation/VAR_057163|||http://purl.uniprot.org/annotation/VAR_057164|||http://purl.uniprot.org/annotation/VAR_057165|||http://purl.uniprot.org/annotation/VAR_059789|||http://purl.uniprot.org/annotation/VSP_014529
http://togogenome.org/gene/9606:DNAJC21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5F1R6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||DnaJ homolog subfamily C member 21|||In BMFS3; loss of HSPA8-binding; no effect on PA2G4-, nor on ZNF622-binding.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||J|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281475|||http://purl.uniprot.org/annotation/VAR_036163|||http://purl.uniprot.org/annotation/VAR_061145|||http://purl.uniprot.org/annotation/VAR_076802|||http://purl.uniprot.org/annotation/VSP_024004|||http://purl.uniprot.org/annotation/VSP_024005
http://togogenome.org/gene/9606:ZCCHC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N567                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||CCHC-type 4|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger CCHC domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150965|||http://purl.uniprot.org/annotation/VAR_028164
http://togogenome.org/gene/9606:FBLIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUP2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||FERMT2-binding|||Filamin-binding|||Filamin-binding LIM protein 1|||In isoform 2.|||In isoform 3.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Localizes to cell-ECM adhesions; abolishes FLNA and FLNC interactions; failed to decorate actin filaments.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075732|||http://purl.uniprot.org/annotation/VAR_022842|||http://purl.uniprot.org/annotation/VAR_050145|||http://purl.uniprot.org/annotation/VSP_008781|||http://purl.uniprot.org/annotation/VSP_008782
http://togogenome.org/gene/9606:SMOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4F8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||In OAS.|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||SPARC-related modular calcium-binding protein 1|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020316|||http://purl.uniprot.org/annotation/VAR_034498|||http://purl.uniprot.org/annotation/VAR_069326|||http://purl.uniprot.org/annotation/VAR_069327|||http://purl.uniprot.org/annotation/VAR_069328|||http://purl.uniprot.org/annotation/VSP_008720
http://togogenome.org/gene/9606:ESF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H501                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||ESF1 homolog|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079410|||http://purl.uniprot.org/annotation/VAR_024331|||http://purl.uniprot.org/annotation/VAR_053082|||http://purl.uniprot.org/annotation/VAR_053083
http://togogenome.org/gene/9606:KIAA1958                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8K9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA1958                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050811|||http://purl.uniprot.org/annotation/VSP_015146|||http://purl.uniprot.org/annotation/VSP_054654
http://togogenome.org/gene/9606:FAM163B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C2L3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Protein FAM163B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280258
http://togogenome.org/gene/9606:MFSD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Major facilitator superfamily domain-containing protein 6|||N-acetylalanine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321940|||http://purl.uniprot.org/annotation/VAR_039388
http://togogenome.org/gene/9606:URB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60287                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nucleolar pre-ribosomal-associated protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057939|||http://purl.uniprot.org/annotation/VAR_059705|||http://purl.uniprot.org/annotation/VAR_060586
http://togogenome.org/gene/9606:RAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15918                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Essential for DNA hairpin formation, participates in base-stacking interactions near the cleavage site|||Found in a patient with T and B cell immunodeficiency and progressive multifocal leukoencephalopathy; unknown pathological significance.|||Found in a patient with an atypical form of combined immunodeficiency; unknown pathological significance.|||Found in a patient with common variable immunodeficiency with B cell deficiency; decreased recombinant activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CHIDG and OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome; reduced recombination activity when associated with H-737.|||In CHIDG; reduced recombination activity.|||In OS and CHIDG; reduced recombination activity when associated with T-507.|||In OS and T(-)B(-)NK(+) SCID; found in a patient with an atypical form of severe combined immunodeficiency/Omenn syndrome.|||In OS.|||In OS; also found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome.|||In OS; also in a patient with multiple autoimmune disorders.|||In OS; found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome.|||In T(-)B(-)NK(+) SCID and OS; also found in a patient with an atypical form of severe combined immunodeficiency/Omenn syndrome; decreased recombination activity.|||In T(-)B(-)NK(+) SCID; also found in patients with an atypical form of severe combined immunodeficiency/Omenn syndrome; loss of recombination activity; unknown pathological significance.|||In T(-)B(-)NK(+) SCID; decreased recombination activity.|||In T(-)B(-)NK(+) SCID; unknown pathological significance.|||In T-CMVA.|||In T-CMVA; also found in a patient with an atypical form of severe combined immunodeficiency /Omenn syndrome.|||In isoform 2.|||Interaction with importin alpha-1|||NBD|||No effect on recombination activity.|||Probable disease-associated variant found in a patient with relatively late onset of infections and isolated T-cell lymphopenia; also found in a patient with T and B cell immunodeficiency and progressive multifocal leukoencephalopathy; decreases recombination activity; no effect on protein abundance.|||Probable disease-associated variant found in a patient with severe combined immunodeficiency with maternal fetal engraftment.|||RAG1-type|||RING-type|||V(D)J recombination-activating protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056004|||http://purl.uniprot.org/annotation/VAR_007800|||http://purl.uniprot.org/annotation/VAR_007801|||http://purl.uniprot.org/annotation/VAR_007802|||http://purl.uniprot.org/annotation/VAR_007803|||http://purl.uniprot.org/annotation/VAR_007804|||http://purl.uniprot.org/annotation/VAR_008886|||http://purl.uniprot.org/annotation/VAR_008887|||http://purl.uniprot.org/annotation/VAR_008888|||http://purl.uniprot.org/annotation/VAR_008889|||http://purl.uniprot.org/annotation/VAR_008890|||http://purl.uniprot.org/annotation/VAR_008891|||http://purl.uniprot.org/annotation/VAR_008892|||http://purl.uniprot.org/annotation/VAR_008893|||http://purl.uniprot.org/annotation/VAR_008894|||http://purl.uniprot.org/annotation/VAR_020113|||http://purl.uniprot.org/annotation/VAR_020114|||http://purl.uniprot.org/annotation/VAR_025971|||http://purl.uniprot.org/annotation/VAR_025972|||http://purl.uniprot.org/annotation/VAR_025973|||http://purl.uniprot.org/annotation/VAR_025974|||http://purl.uniprot.org/annotation/VAR_025975|||http://purl.uniprot.org/annotation/VAR_025976|||http://purl.uniprot.org/annotation/VAR_025977|||http://purl.uniprot.org/annotation/VAR_025978|||http://purl.uniprot.org/annotation/VAR_025979|||http://purl.uniprot.org/annotation/VAR_025980|||http://purl.uniprot.org/annotation/VAR_025981|||http://purl.uniprot.org/annotation/VAR_025982|||http://purl.uniprot.org/annotation/VAR_025983|||http://purl.uniprot.org/annotation/VAR_025984|||http://purl.uniprot.org/annotation/VAR_025985|||http://purl.uniprot.org/annotation/VAR_025986|||http://purl.uniprot.org/annotation/VAR_025987|||http://purl.uniprot.org/annotation/VAR_025988|||http://purl.uniprot.org/annotation/VAR_029260|||http://purl.uniprot.org/annotation/VAR_029261|||http://purl.uniprot.org/annotation/VAR_029262|||http://purl.uniprot.org/annotation/VAR_029263|||http://purl.uniprot.org/annotation/VAR_029264|||http://purl.uniprot.org/annotation/VAR_045957|||http://purl.uniprot.org/annotation/VAR_045958|||http://purl.uniprot.org/annotation/VAR_045959|||http://purl.uniprot.org/annotation/VAR_067274|||http://purl.uniprot.org/annotation/VAR_067275|||http://purl.uniprot.org/annotation/VAR_067276|||http://purl.uniprot.org/annotation/VAR_078305|||http://purl.uniprot.org/annotation/VAR_078306|||http://purl.uniprot.org/annotation/VAR_078307|||http://purl.uniprot.org/annotation/VAR_078308|||http://purl.uniprot.org/annotation/VAR_078309|||http://purl.uniprot.org/annotation/VAR_078310|||http://purl.uniprot.org/annotation/VSP_055883
http://togogenome.org/gene/9606:NOSIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6F9|||http://purl.uniprot.org/uniprot/Q9Y314                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nitric oxide synthase-interacting protein|||Nitric oxide synthase-interacting protein zinc-finger|||Nuclear localization signal|||Phosphoserine|||U-box-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280585|||http://purl.uniprot.org/annotation/VAR_031169
http://togogenome.org/gene/9606:TUBA3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPH7|||http://purl.uniprot.org/uniprot/Q1ZYQ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||Detyrosinated tubulin alpha-3C chain|||In isoform 2.|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Tubulin alpha-3C chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048110|||http://purl.uniprot.org/annotation/PRO_0000437399|||http://purl.uniprot.org/annotation/VAR_022068|||http://purl.uniprot.org/annotation/VAR_034541|||http://purl.uniprot.org/annotation/VAR_052666|||http://purl.uniprot.org/annotation/VSP_006678
http://togogenome.org/gene/9606:L2HGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9P8                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In L2HGA.|||In L2HGA; alters protein processing and abolishes catalytic activity.|||In isoform 2.|||L-2-hydroxyglutarate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228129|||http://purl.uniprot.org/annotation/VAR_025681|||http://purl.uniprot.org/annotation/VAR_025682|||http://purl.uniprot.org/annotation/VAR_025683|||http://purl.uniprot.org/annotation/VAR_025684|||http://purl.uniprot.org/annotation/VAR_025685|||http://purl.uniprot.org/annotation/VAR_025686|||http://purl.uniprot.org/annotation/VAR_025687|||http://purl.uniprot.org/annotation/VAR_025688|||http://purl.uniprot.org/annotation/VAR_025689|||http://purl.uniprot.org/annotation/VAR_025690|||http://purl.uniprot.org/annotation/VAR_057808|||http://purl.uniprot.org/annotation/VSP_017662|||http://purl.uniprot.org/annotation/VSP_017663
http://togogenome.org/gene/9606:CDADC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWV3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||CMP/dCMP-type deaminase 1|||CMP/dCMP-type deaminase 2|||Cytidine and dCMP deaminase domain-containing protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear export signal|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300491|||http://purl.uniprot.org/annotation/VSP_027811|||http://purl.uniprot.org/annotation/VSP_027812|||http://purl.uniprot.org/annotation/VSP_027813|||http://purl.uniprot.org/annotation/VSP_027814|||http://purl.uniprot.org/annotation/VSP_027815
http://togogenome.org/gene/9606:CNOT6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0K8|||http://purl.uniprot.org/uniprot/Q96LI5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 6-like|||Decreased deadenylase activity.|||Endonuclease/exonuclease/phosphatase|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Loss of deadenylase activity.|||Nuclease domain|||Proton donor/acceptor|||Required for interaction with CNOT1, CNOT3 and CNOT7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314587|||http://purl.uniprot.org/annotation/VSP_030321|||http://purl.uniprot.org/annotation/VSP_030322|||http://purl.uniprot.org/annotation/VSP_030323
http://togogenome.org/gene/9606:ALDH18A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54886                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Delta-1-pyrroline-5-carboxylate synthase|||Gamma-glutamyl phosphate reductase|||Glutamate 5-kinase|||In ADCL3.|||In ADCL3; no effect on protein abundance; altered sub-mitochondrial distribution; decreased proline biosynthetic process.|||In ARCL3A.|||In ARCL3A; benign variant.|||In ARCL3A; does not affect proline and ornithine biosynthetic activity.|||In ARCL3A; reduction of activity.|||In SPG9A.|||In SPG9A; altered homohexamerization; no effect on localization to the mitochondrion; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process.|||In SPG9A; decreased protein abundance; no effect on localization to the mitochondrion; altered homohexamerization; loss of glutamate 5-kinase activity; no effect on glutamate-5-semialdehyde dehydrogenase activity; decreased amino acid biosynthetic process.|||In SPG9B.|||In isoform Short.|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109769|||http://purl.uniprot.org/annotation/VAR_038482|||http://purl.uniprot.org/annotation/VAR_051792|||http://purl.uniprot.org/annotation/VAR_051793|||http://purl.uniprot.org/annotation/VAR_058006|||http://purl.uniprot.org/annotation/VAR_075884|||http://purl.uniprot.org/annotation/VAR_075885|||http://purl.uniprot.org/annotation/VAR_075886|||http://purl.uniprot.org/annotation/VAR_075887|||http://purl.uniprot.org/annotation/VAR_075888|||http://purl.uniprot.org/annotation/VAR_075889|||http://purl.uniprot.org/annotation/VAR_075890|||http://purl.uniprot.org/annotation/VAR_075891|||http://purl.uniprot.org/annotation/VAR_075892|||http://purl.uniprot.org/annotation/VAR_075893|||http://purl.uniprot.org/annotation/VAR_075894|||http://purl.uniprot.org/annotation/VAR_075895|||http://purl.uniprot.org/annotation/VAR_075896|||http://purl.uniprot.org/annotation/VSP_005215
http://togogenome.org/gene/9606:SARAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK59|||http://purl.uniprot.org/uniprot/Q96BY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dominant-negative mutant; leading to impair inhibition of SOCE.|||Helical|||In isoform 2.|||Lumenal|||Polar residues|||Store-operated calcium entry-associated regulatory factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045485|||http://purl.uniprot.org/annotation/PRO_5007491741|||http://purl.uniprot.org/annotation/VAR_054042|||http://purl.uniprot.org/annotation/VSP_043773
http://togogenome.org/gene/9606:IKZF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6; atypical|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD84; no effect on homodimerization activity; no effect on heterodimerization activity; changed localization; changed DNA-binding transcription activator activity; changed sequence-specific DNA binding; binds novel and non-specific DNA motifs and acts as a dominant negative through its homodimerization and heterodimerization activities.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 14 and isoform 15.|||In isoform 14.|||In isoform 16.|||In isoform 2 and isoform 15.|||In isoform 3 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 9.|||Mediates homodimerization and heterodimerization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein Aiolos                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047090|||http://purl.uniprot.org/annotation/VAR_064724|||http://purl.uniprot.org/annotation/VAR_086041|||http://purl.uniprot.org/annotation/VSP_006840|||http://purl.uniprot.org/annotation/VSP_006841|||http://purl.uniprot.org/annotation/VSP_006842|||http://purl.uniprot.org/annotation/VSP_006843|||http://purl.uniprot.org/annotation/VSP_006844|||http://purl.uniprot.org/annotation/VSP_041274|||http://purl.uniprot.org/annotation/VSP_041275|||http://purl.uniprot.org/annotation/VSP_041276|||http://purl.uniprot.org/annotation/VSP_041277|||http://purl.uniprot.org/annotation/VSP_041278|||http://purl.uniprot.org/annotation/VSP_041279|||http://purl.uniprot.org/annotation/VSP_041280|||http://purl.uniprot.org/annotation/VSP_041281|||http://purl.uniprot.org/annotation/VSP_055353
http://togogenome.org/gene/9606:VBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61758|||http://purl.uniprot.org/uniprot/Q6FH24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Prefoldin subunit 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153652|||http://purl.uniprot.org/annotation/VAR_023371|||http://purl.uniprot.org/annotation/VSP_060081
http://togogenome.org/gene/9606:ZDHHC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVZ1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes palmitoyltransferase activity.|||DHHC|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Palmitoyltransferase ZDHHC19|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212904|||http://purl.uniprot.org/annotation/VAR_052979|||http://purl.uniprot.org/annotation/VSP_056001|||http://purl.uniprot.org/annotation/VSP_060410|||http://purl.uniprot.org/annotation/VSP_060411
http://togogenome.org/gene/9606:MED25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71SY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates interaction with RARA.|||Asymmetric dimethylarginine|||Disordered|||Found in a patient with syndromic intellectual disability; unknown pathological significance.|||In BVSYS; the mutation impairs interaction with the Mediator complex.|||In CMT2B2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with CREBBP|||Interaction with RARA|||Interaction with VP16|||Interaction with the Mediator complex|||LXXLL motif|||Mediator of RNA polymerase II transcription subunit 25|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304952|||http://purl.uniprot.org/annotation/VAR_063521|||http://purl.uniprot.org/annotation/VAR_073949|||http://purl.uniprot.org/annotation/VAR_073950|||http://purl.uniprot.org/annotation/VSP_028143|||http://purl.uniprot.org/annotation/VSP_028146|||http://purl.uniprot.org/annotation/VSP_047570
http://togogenome.org/gene/9606:GRAMD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQF7|||http://purl.uniprot.org/uniprot/B3KUH3|||http://purl.uniprot.org/uniprot/M0QZ12|||http://purl.uniprot.org/uniprot/Q96CP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||GRAM|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein Aster-A|||VASt                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287446|||http://purl.uniprot.org/annotation/VSP_025465|||http://purl.uniprot.org/annotation/VSP_025466
http://togogenome.org/gene/9606:CPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15085                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase A1|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004345|||http://purl.uniprot.org/annotation/PRO_0000004346|||http://purl.uniprot.org/annotation/VAR_048593|||http://purl.uniprot.org/annotation/VAR_054311
http://togogenome.org/gene/9606:SLC4A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6U841                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced glycosylation. Abolishes glycosylation; when associated with Q-677 and Q-687.|||Reduced glycosylation. Abolishes glycosylation; when associated with Q-677 and Q-697.|||Reduced glycosylation. Abolishes glycosylation; when associated with Q-687 and Q-697.|||Sodium-driven chloride bicarbonate exchanger                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245240|||http://purl.uniprot.org/annotation/VSP_019653|||http://purl.uniprot.org/annotation/VSP_044993|||http://purl.uniprot.org/annotation/VSP_054471|||http://purl.uniprot.org/annotation/VSP_054472
http://togogenome.org/gene/9606:BIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2Z2|||http://purl.uniprot.org/uniprot/B7Z6Y2|||http://purl.uniprot.org/uniprot/O00499|||http://purl.uniprot.org/uniprot/Q9BTH3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BAR|||Clathrin-binding|||Disordered|||In CNM2.|||In CNM2; decreased interaction with DNM2.|||In CNM2; results in severely decreased membrane tubulation.|||In isoform BIN1, isoform BIN1+12A and isoform BIN1-13.|||In isoform BIN1-10-13 and isoform BIN1-13.|||In isoform II2 and isoform BIN1+12A.|||In isoform II3 and isoform BIN1.|||In isoform IIB, isoform IIC2, isoform II2, isoform II3, isoform BIN1, isoform BIN1+12A, isoform BIN1-10-13 and isoform BIN1-13.|||In isoform IIB.|||In isoform IIC1 and isoform IIC2.|||In isoform IID.|||Interaction with BIN2|||Myc box-dependent-interacting protein 1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a sporadic case of centronulear myopathy; does not induce membrane tubulation in cultured cells.|||Removed|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192951|||http://purl.uniprot.org/annotation/VAR_037425|||http://purl.uniprot.org/annotation/VAR_037426|||http://purl.uniprot.org/annotation/VAR_081080|||http://purl.uniprot.org/annotation/VAR_081081|||http://purl.uniprot.org/annotation/VAR_081082|||http://purl.uniprot.org/annotation/VAR_081083|||http://purl.uniprot.org/annotation/VAR_081084|||http://purl.uniprot.org/annotation/VAR_081085|||http://purl.uniprot.org/annotation/VSP_000246|||http://purl.uniprot.org/annotation/VSP_000247|||http://purl.uniprot.org/annotation/VSP_000248|||http://purl.uniprot.org/annotation/VSP_000249|||http://purl.uniprot.org/annotation/VSP_000250|||http://purl.uniprot.org/annotation/VSP_000251|||http://purl.uniprot.org/annotation/VSP_000252|||http://purl.uniprot.org/annotation/VSP_000253
http://togogenome.org/gene/9606:DEFB136                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KP8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Defensin beta 136                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045364
http://togogenome.org/gene/9606:LAMA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15230                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||Domain II and I|||Domain IV 1 (domain IV B)|||In BBDS2; unknown pathological significance.|||In NPHS26.|||In NPHS26; unknown pathological significance.|||In isoform 2.|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11; truncated|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 14|||Laminin EGF-like 15|||Laminin EGF-like 16; first part|||Laminin EGF-like 16; second part|||Laminin EGF-like 17|||Laminin EGF-like 18|||Laminin EGF-like 19|||Laminin EGF-like 2|||Laminin EGF-like 20|||Laminin EGF-like 21|||Laminin EGF-like 22|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin IV type A|||Laminin N-terminal|||Laminin subunit alpha-5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017062|||http://purl.uniprot.org/annotation/VAR_030847|||http://purl.uniprot.org/annotation/VAR_030848|||http://purl.uniprot.org/annotation/VAR_030849|||http://purl.uniprot.org/annotation/VAR_030850|||http://purl.uniprot.org/annotation/VAR_030851|||http://purl.uniprot.org/annotation/VAR_030852|||http://purl.uniprot.org/annotation/VAR_030853|||http://purl.uniprot.org/annotation/VAR_030854|||http://purl.uniprot.org/annotation/VAR_030855|||http://purl.uniprot.org/annotation/VAR_030856|||http://purl.uniprot.org/annotation/VAR_030857|||http://purl.uniprot.org/annotation/VAR_030858|||http://purl.uniprot.org/annotation/VAR_030859|||http://purl.uniprot.org/annotation/VAR_030860|||http://purl.uniprot.org/annotation/VAR_047887|||http://purl.uniprot.org/annotation/VAR_047888|||http://purl.uniprot.org/annotation/VAR_087702|||http://purl.uniprot.org/annotation/VAR_087703|||http://purl.uniprot.org/annotation/VAR_087704|||http://purl.uniprot.org/annotation/VAR_087705|||http://purl.uniprot.org/annotation/VAR_087706|||http://purl.uniprot.org/annotation/VAR_087707|||http://purl.uniprot.org/annotation/VAR_087708|||http://purl.uniprot.org/annotation/VAR_087709|||http://purl.uniprot.org/annotation/VAR_087710|||http://purl.uniprot.org/annotation/VAR_087711|||http://purl.uniprot.org/annotation/VSP_057343|||http://purl.uniprot.org/annotation/VSP_057344
http://togogenome.org/gene/9606:SPTLC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Polar residues|||Serine palmitoyltransferase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079426|||http://purl.uniprot.org/annotation/VAR_048230|||http://purl.uniprot.org/annotation/VAR_082794|||http://purl.uniprot.org/annotation/VSP_028167|||http://purl.uniprot.org/annotation/VSP_028168
http://togogenome.org/gene/9606:POLR2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19387|||http://purl.uniprot.org/uniprot/Q6FGR6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB3|||DNA-directed RNA polymerase RpoA/D/Rpb3-type|||Disordered|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132743
http://togogenome.org/gene/9606:NDUFA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95182                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118834|||http://purl.uniprot.org/annotation/VAR_050589
http://togogenome.org/gene/9606:TRAPPC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLN9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Trafficking protein particle complex subunit 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321547|||http://purl.uniprot.org/annotation/VSP_038356|||http://purl.uniprot.org/annotation/VSP_038357|||http://purl.uniprot.org/annotation/VSP_038358|||http://purl.uniprot.org/annotation/VSP_038359
http://togogenome.org/gene/9606:BCL11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L8B567|||http://purl.uniprot.org/uniprot/L8B7P7|||http://purl.uniprot.org/uniprot/L8B862|||http://purl.uniprot.org/uniprot/L8B8F6|||http://purl.uniprot.org/uniprot/Q9C0K0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||B-cell lymphoma/leukemia 11B|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IDDSFTA.|||In IMD49.|||In IMD49; loss of stimulation of T-lymphocyte development; dominant negative loss of activation of IL2 expression; results in reduced binding to known canonical promoters and abnormal binding to novel DNA sites not recognized by the wild-type protein; no effect on interaction with EP300.|||In a colorectal cancer sample; somatic mutation.|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047104|||http://purl.uniprot.org/annotation/VAR_035554|||http://purl.uniprot.org/annotation/VAR_065741|||http://purl.uniprot.org/annotation/VAR_065742|||http://purl.uniprot.org/annotation/VAR_078423|||http://purl.uniprot.org/annotation/VAR_081174|||http://purl.uniprot.org/annotation/VAR_081175|||http://purl.uniprot.org/annotation/VSP_009565
http://togogenome.org/gene/9606:FKBP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62942|||http://purl.uniprot.org/uniprot/Q0VDC6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP1A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075289
http://togogenome.org/gene/9606:OR2B11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVY5|||http://purl.uniprot.org/uniprot/Q5JQS5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2B11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150464|||http://purl.uniprot.org/annotation/VAR_053132|||http://purl.uniprot.org/annotation/VAR_053133|||http://purl.uniprot.org/annotation/VAR_053134|||http://purl.uniprot.org/annotation/VAR_053135|||http://purl.uniprot.org/annotation/VAR_062015
http://togogenome.org/gene/9606:THSD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In AAT12; unknown pathological significance; has no effect on assembly of FBN1-containing microfibrils.|||In AAT12; unknown pathological significance; results in impaired assembly of FBN1-containing microfibrils.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PLAC|||Polar residues|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||Thrombospondin type-1 domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313583|||http://purl.uniprot.org/annotation/VAR_087397|||http://purl.uniprot.org/annotation/VAR_087398|||http://purl.uniprot.org/annotation/VAR_087399|||http://purl.uniprot.org/annotation/VSP_030036|||http://purl.uniprot.org/annotation/VSP_030037|||http://purl.uniprot.org/annotation/VSP_030038|||http://purl.uniprot.org/annotation/VSP_030039|||http://purl.uniprot.org/annotation/VSP_030040|||http://purl.uniprot.org/annotation/VSP_030041|||http://purl.uniprot.org/annotation/VSP_054877|||http://purl.uniprot.org/annotation/VSP_054878
http://togogenome.org/gene/9606:HSFX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GWH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Heat shock transcription factor, X-linked member 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440583
http://togogenome.org/gene/9606:HADHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL44|||http://purl.uniprot.org/uniprot/P40939                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  3-hydroxyacyl-CoA dehydrogenase C-terminal|||3-hydroxyacyl-CoA dehydrogenase NAD binding|||For hydroxyacyl-coenzyme A dehydrogenase activity|||Important for hydroxyacyl-coenzyme A dehydrogenase activity|||Important for long-chain enoyl-CoA hydratase activity|||In AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity.|||In LCHAD deficiency.|||In MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Trifunctional enzyme subunit alpha, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007403|||http://purl.uniprot.org/annotation/VAR_002273|||http://purl.uniprot.org/annotation/VAR_021125|||http://purl.uniprot.org/annotation/VAR_021126|||http://purl.uniprot.org/annotation/VAR_021127|||http://purl.uniprot.org/annotation/VAR_048908|||http://purl.uniprot.org/annotation/VSP_059010|||http://purl.uniprot.org/annotation/VSP_059011
http://togogenome.org/gene/9606:PIK3CD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2K8FKV1|||http://purl.uniprot.org/uniprot/O00329                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation, no effect on lipid kinase activity.|||Abolishes autophosphorylation, reduced lipid kinase activity.|||Abolishes lipid and protein kinase activities.|||Activation loop|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In IMD14A; results in gain of function causing enhanced membrane association and kinase activity.|||In ROCHIS; no protein can be detected by Western blot in patient cells.|||In isoform 2.|||PI3K-ABD|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform|||Phosphoserine; by autocatalysis|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088790|||http://purl.uniprot.org/annotation/VAR_070918|||http://purl.uniprot.org/annotation/VAR_085590|||http://purl.uniprot.org/annotation/VSP_044409|||http://purl.uniprot.org/annotation/VSP_044410
http://togogenome.org/gene/9606:MEF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02080                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199431|||http://purl.uniprot.org/annotation/VSP_042322
http://togogenome.org/gene/9606:CCDC63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V217|||http://purl.uniprot.org/uniprot/Q8NA47                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 63|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288874|||http://purl.uniprot.org/annotation/VAR_050758|||http://purl.uniprot.org/annotation/VSP_054895
http://togogenome.org/gene/9606:TMC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXZ8|||http://purl.uniprot.org/uniprot/Q8IU68                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In EV2.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TMC|||Transmembrane channel-like protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185386|||http://purl.uniprot.org/annotation/VAR_023964|||http://purl.uniprot.org/annotation/VAR_052337|||http://purl.uniprot.org/annotation/VAR_081777|||http://purl.uniprot.org/annotation/VSP_016448
http://togogenome.org/gene/9606:GRB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13322                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2-fold loss of inositide-binding.|||5-fold loss of inositide-binding.|||Disordered|||Growth factor receptor-bound protein 10|||Impairs YWHAE-binding.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||Loss of phosphorylation.|||No effect on NEDD4-binding. No effect on the disruption of the interaction between INSR and IRS1 and IRS2.|||No effect on NEDD4-binding; when associated with A-136 and A-139.|||No effect on NEDD4-binding; when associated with A-136 and A-141.|||No effect on NEDD4-binding; when associated with A-139 and A-141.|||No effect on YWHAE-binding.|||No effect on phosphorylation.|||No net loss of phosphorylation, this may be due to a compensatory phosphorylation of T-422 in vitro.|||PH|||Phosphoserine|||Phosphoserine; by MAPK1 and MAPK3; in vitro|||Phosphoserine; by MTOR and PKB/AKT1|||Phosphoserine; by MTOR, MAPK1 and MAPK3|||Phosphotyrosine; by TEC|||Polar residues|||Ras-associating|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150346|||http://purl.uniprot.org/annotation/VAR_053112|||http://purl.uniprot.org/annotation/VAR_053113|||http://purl.uniprot.org/annotation/VAR_062864|||http://purl.uniprot.org/annotation/VSP_001842|||http://purl.uniprot.org/annotation/VSP_001843|||http://purl.uniprot.org/annotation/VSP_038784
http://togogenome.org/gene/9606:LACTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83111                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-ester intermediate|||Disordered|||Does not affect serine protease activity; shows reduced tumor suppressor activity; shows reduced ability to down-regulate phosphatidylethanolamine (PtdEtn) levels.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Serine beta-lactamase-like protein LACTB, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195476|||http://purl.uniprot.org/annotation/VAR_018299|||http://purl.uniprot.org/annotation/VSP_010011
http://togogenome.org/gene/9606:SNRPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09012                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNA binding.|||Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphothreonine|||RRM 1|||RRM 2|||Removed|||Substantially reduces RNA binding.|||U1 small nuclear ribonucleoprotein A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081887
http://togogenome.org/gene/9606:PPP2R5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14738                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6; approximate|||7; approximate|||8|||8 X 2 AA approximate tandem repeats of Q-P|||Basic and acidic residues|||Disordered|||Found in a patient with delayed psychomotor development, no speech and cataracts; no effect on binding to subunit PPP2CA; no effect on binding to subunit PPP2R1A.|||In MRD35; decreases binding to subunit PPP2CA; decreases binding to subunit PPP2R1A.|||In isoform Delta-2.|||In isoform Delta-3.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3-binding; class I|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071452|||http://purl.uniprot.org/annotation/VAR_069414|||http://purl.uniprot.org/annotation/VAR_073708|||http://purl.uniprot.org/annotation/VAR_073709|||http://purl.uniprot.org/annotation/VAR_074491|||http://purl.uniprot.org/annotation/VAR_074492|||http://purl.uniprot.org/annotation/VSP_005110|||http://purl.uniprot.org/annotation/VSP_005111
http://togogenome.org/gene/9606:SELENOM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWX9                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Modification|||Molecule Processing|||Non standard residue|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Non standard residue|||Signal Peptide                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec)|||Nucleophile|||Selenocysteine|||Selenoprotein M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022298
http://togogenome.org/gene/9606:CXXC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LFL8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  CXXC-type|||CXXC-type zinc finger protein 5|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317548|||http://purl.uniprot.org/annotation/VSP_031013
http://togogenome.org/gene/9606:URAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGE7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Motif|||Sequence Variant                                                                                  ^@                                                                                  Microbody targeting signal|||Proton donor|||Putative 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315240|||http://purl.uniprot.org/annotation/VAR_053987
http://togogenome.org/gene/9606:CHRNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17787|||http://purl.uniprot.org/uniprot/Q5SXY3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In ENFL3.|||In ENFL3; approximately 10-fold increase in acetylcholine sensitivity.|||Increases ligand activation in LS and HS nAChR subtypes.|||Key residue for a rapid dissociation (K(off)) from the conotoxin BuIA|||Key residue that may interfere with effective access of the conotoxin BuIA to the channel binding site|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit beta-2|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000379|||http://purl.uniprot.org/annotation/PRO_5014309962|||http://purl.uniprot.org/annotation/VAR_012714|||http://purl.uniprot.org/annotation/VAR_012715|||http://purl.uniprot.org/annotation/VAR_021564
http://togogenome.org/gene/9606:AMIGO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amphoterin-induced protein 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014513
http://togogenome.org/gene/9606:FAM227A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H4B4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Protein FAM227A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419264|||http://purl.uniprot.org/annotation/VSP_044139|||http://purl.uniprot.org/annotation/VSP_044140
http://togogenome.org/gene/9606:LSM14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX40                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DFDF|||Disordered|||FFD box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Protein LSM14 homolog B|||Removed|||Sm|||TFG box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187093|||http://purl.uniprot.org/annotation/VSP_014658|||http://purl.uniprot.org/annotation/VSP_014659|||http://purl.uniprot.org/annotation/VSP_014660|||http://purl.uniprot.org/annotation/VSP_014661|||http://purl.uniprot.org/annotation/VSP_014662
http://togogenome.org/gene/9606:ITPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13572                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-grasp|||In isoform 2.|||Induces a strong reduction in kinase activity.|||Inositol-tetrakisphosphate 1-kinase|||Loss of kinase activity.|||N6-acetyllysine; by EP300 and CREBBP|||No effect.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220833|||http://purl.uniprot.org/annotation/VSP_016478|||http://purl.uniprot.org/annotation/VSP_016479
http://togogenome.org/gene/9606:EEF1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05639                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl glycerylphosphorylethanolamine|||Abolishes EEF1AKMT4-mediated methylation.|||Abolishes methylation by EEF1AKMT3.|||Disordered|||Elongation factor 1-alpha 2|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||G1|||G2|||G3|||G4|||G5|||In DEE33.|||In MRD38.|||N,N,N-trimethylglycine|||N6,N6,N6-trimethyllysine|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT4|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6,N6-dimethyllysine; alternate; by EEF1AKMT4|||N6-acetyllysine|||N6-methyllysine; alternate|||N6-methyllysine; alternate; by EEF1AKMT4|||Phosphoserine|||Removed|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090891|||http://purl.uniprot.org/annotation/VAR_069395|||http://purl.uniprot.org/annotation/VAR_073807|||http://purl.uniprot.org/annotation/VAR_073808|||http://purl.uniprot.org/annotation/VAR_079033
http://togogenome.org/gene/9606:ZNF33A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR11|||http://purl.uniprot.org/uniprot/A0A0A0MRS1|||http://purl.uniprot.org/uniprot/Q06730                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 33A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047363|||http://purl.uniprot.org/annotation/VAR_052749|||http://purl.uniprot.org/annotation/VAR_052750|||http://purl.uniprot.org/annotation/VAR_052751|||http://purl.uniprot.org/annotation/VSP_046420|||http://purl.uniprot.org/annotation/VSP_055165
http://togogenome.org/gene/9606:HDGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPW1|||http://purl.uniprot.org/uniprot/A8K8G0|||http://purl.uniprot.org/uniprot/B7Z958|||http://purl.uniprot.org/uniprot/P51858                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes secretion and alters location of the protein from inside the exosome to the exosomal surface.|||Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hepatoma-derived growth factor|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nuclear localization signal|||PWWP|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191700|||http://purl.uniprot.org/annotation/VAR_061209|||http://purl.uniprot.org/annotation/VSP_045620|||http://purl.uniprot.org/annotation/VSP_047328
http://togogenome.org/gene/9606:POLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5Q5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Basic and acidic residues|||DNA polymerase nu|||Disordered|||In isoform 2.|||No effect on polymerase activity. Increases accuracy by ten-fold.|||Reduces polymerase activity. No effect on accuracy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227938|||http://purl.uniprot.org/annotation/VAR_025647|||http://purl.uniprot.org/annotation/VAR_025648|||http://purl.uniprot.org/annotation/VAR_025649|||http://purl.uniprot.org/annotation/VAR_025650|||http://purl.uniprot.org/annotation/VAR_025651|||http://purl.uniprot.org/annotation/VAR_025652|||http://purl.uniprot.org/annotation/VAR_025653|||http://purl.uniprot.org/annotation/VAR_025654|||http://purl.uniprot.org/annotation/VSP_054402|||http://purl.uniprot.org/annotation/VSP_054403
http://togogenome.org/gene/9606:MKNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBH9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active.|||Disordered|||In isoform 2.|||Loss of kinase activity; when associated with T-244.|||Loss of kinase activity; when associated with T-249.|||MAP kinase binding|||MAP kinase-interacting serine/threonine-protein kinase 2|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Reduced phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086336|||http://purl.uniprot.org/annotation/VAR_040805|||http://purl.uniprot.org/annotation/VAR_051648|||http://purl.uniprot.org/annotation/VAR_051649|||http://purl.uniprot.org/annotation/VSP_007353|||http://purl.uniprot.org/annotation/VSP_007354
http://togogenome.org/gene/9606:YKT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2J0|||http://purl.uniprot.org/uniprot/O15498                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Decreases palmitoylation by 55%. Prevents palmitoylation; when associated with S-195. Targeted to Golgi and cytosol; when associated with E-42.|||In isoform 2.|||Increases palmitoylation. Targeted to Golgi membranes. Targeted to Golgi and cytosol; when associated with S-194. Targeted to cytosol; when associated with S-195.|||Longin|||Phosphoserine|||Prevents farnesylation. Targeted to cytosol; when associated with E-42. Decreases palmitoylation by 13%. Prevents palmitoylation; when associated with S-194.|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine|||Synaptobrevin homolog YKT6|||V-SNARE coiled-coil homology|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280709|||http://purl.uniprot.org/annotation/PRO_0000396661|||http://purl.uniprot.org/annotation/VSP_056071
http://togogenome.org/gene/9606:P2RX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51575                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In one patient presenting with severe bleeding; somatic mutation; results in a non-functional channel.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 1|||Phosphoserine|||Phosphothreonine|||Pore-forming motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161545|||http://purl.uniprot.org/annotation/VAR_025382|||http://purl.uniprot.org/annotation/VAR_053552
http://togogenome.org/gene/9606:CPSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7B0|||http://purl.uniprot.org/uniprot/O95639                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||CCHC-type|||Cleavage and polyadenylation specificity factor subunit 4|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074402|||http://purl.uniprot.org/annotation/VSP_008601|||http://purl.uniprot.org/annotation/VSP_008602
http://togogenome.org/gene/9606:AP1AR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-1 complex-associated regulatory protein|||Basic and acidic residues|||Decreases interaction with AP1G1; when associated with L-260.|||Decreases interaction with AP1G1; when associated with L-264.|||Disordered|||In isoform 2.|||Interaction with AP1G1|||Loss of association with membranes, no effect on interaction with AP1G1; when associated with 4-S-S-5.|||Loss of association with membranes, no effect on interaction with AP1G1; when associated with 9-S.|||Loss of association with the Arp2/3 complex and endosomal colocalization. Abolishes interaction with KLC2, no effect on interaction with AP1G1.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sufficient for association with the Arp2/3 complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089432|||http://purl.uniprot.org/annotation/VAR_050769|||http://purl.uniprot.org/annotation/VSP_015339
http://togogenome.org/gene/9606:PPOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY76|||http://purl.uniprot.org/uniprot/P50336                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity. Impairs protein folding and/or stability.|||Amine oxidase|||Decreases enzyme activity by 45%.|||Decreases enzyme activity by 50%.|||Decreases enzyme activity by 52%.|||Decreases enzyme activity by 64%.|||Decreases enzyme activity by 75%.|||Decreases enzyme activity by 86%.|||Decreases enzyme activity by 87%. Impairs protein folding and/or stability.|||Decreases enzyme activity by 89%. Impairs protein folding and/or stability.|||Decreases enzyme activity by 90%. Strongly decreases affinity for protoporphyrinogen-IX.|||Decreases enzyme activity by 95%.|||Found in patients with the homozygous variant of variegate porphyria; unknown pathological significance; results in reduction of activity in a prokariotyc expression system but has normal activity when expressed in an eukaryotic system.|||In VP.|||In VP; abolishes activity; impairs protein folding and/or stability.|||In VP; abolishes enzyme activity; impairs protein folding and/or stability.|||In VP; decreases enzyme activity.|||In VP; decreases enzyme activity; impairs protein folding and/or stability.|||In VP; no effect on enzyme activity.|||In VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme.|||In VP; slightly decreases enzyme activity.|||In VP; strongly decreases enzyme activity.|||In VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization.|||In VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme.|||In VP; strongly decreases enzyme activity; impairs protein folding and/or stability.|||In VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization.|||No effect on enzyme activity.|||Protoporphyrinogen oxidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135270|||http://purl.uniprot.org/annotation/VAR_003686|||http://purl.uniprot.org/annotation/VAR_003687|||http://purl.uniprot.org/annotation/VAR_003688|||http://purl.uniprot.org/annotation/VAR_003689|||http://purl.uniprot.org/annotation/VAR_003690|||http://purl.uniprot.org/annotation/VAR_034395|||http://purl.uniprot.org/annotation/VAR_070377|||http://purl.uniprot.org/annotation/VAR_070378|||http://purl.uniprot.org/annotation/VAR_070379|||http://purl.uniprot.org/annotation/VAR_070380|||http://purl.uniprot.org/annotation/VAR_070381|||http://purl.uniprot.org/annotation/VAR_070382|||http://purl.uniprot.org/annotation/VAR_070383|||http://purl.uniprot.org/annotation/VAR_070384|||http://purl.uniprot.org/annotation/VAR_070385|||http://purl.uniprot.org/annotation/VAR_070386|||http://purl.uniprot.org/annotation/VAR_070387|||http://purl.uniprot.org/annotation/VAR_070388|||http://purl.uniprot.org/annotation/VAR_070389|||http://purl.uniprot.org/annotation/VAR_070390|||http://purl.uniprot.org/annotation/VAR_070391|||http://purl.uniprot.org/annotation/VAR_070392|||http://purl.uniprot.org/annotation/VAR_070393|||http://purl.uniprot.org/annotation/VAR_070394|||http://purl.uniprot.org/annotation/VAR_070395|||http://purl.uniprot.org/annotation/VAR_070396|||http://purl.uniprot.org/annotation/VAR_070397|||http://purl.uniprot.org/annotation/VAR_070398|||http://purl.uniprot.org/annotation/VAR_070399|||http://purl.uniprot.org/annotation/VAR_070400|||http://purl.uniprot.org/annotation/VAR_070401|||http://purl.uniprot.org/annotation/VAR_070402|||http://purl.uniprot.org/annotation/VAR_070403|||http://purl.uniprot.org/annotation/VAR_070404|||http://purl.uniprot.org/annotation/VAR_070405|||http://purl.uniprot.org/annotation/VAR_070406|||http://purl.uniprot.org/annotation/VAR_070407|||http://purl.uniprot.org/annotation/VAR_070408|||http://purl.uniprot.org/annotation/VAR_070409|||http://purl.uniprot.org/annotation/VAR_070410|||http://purl.uniprot.org/annotation/VAR_070411|||http://purl.uniprot.org/annotation/VAR_070412|||http://purl.uniprot.org/annotation/VAR_070413|||http://purl.uniprot.org/annotation/VAR_070414|||http://purl.uniprot.org/annotation/VAR_070415|||http://purl.uniprot.org/annotation/VAR_070416|||http://purl.uniprot.org/annotation/VAR_070417|||http://purl.uniprot.org/annotation/VAR_070418|||http://purl.uniprot.org/annotation/VAR_070419|||http://purl.uniprot.org/annotation/VAR_070420|||http://purl.uniprot.org/annotation/VAR_070421|||http://purl.uniprot.org/annotation/VAR_070422|||http://purl.uniprot.org/annotation/VAR_070423|||http://purl.uniprot.org/annotation/VAR_070424|||http://purl.uniprot.org/annotation/VAR_070425|||http://purl.uniprot.org/annotation/VAR_070426|||http://purl.uniprot.org/annotation/VAR_070427|||http://purl.uniprot.org/annotation/VAR_070428|||http://purl.uniprot.org/annotation/VAR_070429
http://togogenome.org/gene/9606:CCNYL1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TMC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-Y-like protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000458444
http://togogenome.org/gene/9606:TMEM250                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YL14                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 250                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420906
http://togogenome.org/gene/9606:ADGRF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C083|||http://purl.uniprot.org/uniprot/Q8IZF5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor F3|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012893|||http://purl.uniprot.org/annotation/VAR_024475|||http://purl.uniprot.org/annotation/VSP_012815|||http://purl.uniprot.org/annotation/VSP_012816|||http://purl.uniprot.org/annotation/VSP_012817|||http://purl.uniprot.org/annotation/VSP_046174|||http://purl.uniprot.org/annotation/VSP_046175
http://togogenome.org/gene/9606:RLIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RLIM|||In TOKAS.|||In isoform 2.|||N-acetylmethionine|||PDZ-binding|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056052|||http://purl.uniprot.org/annotation/VAR_074175|||http://purl.uniprot.org/annotation/VAR_077826|||http://purl.uniprot.org/annotation/VAR_077827|||http://purl.uniprot.org/annotation/VAR_077828|||http://purl.uniprot.org/annotation/VAR_077829|||http://purl.uniprot.org/annotation/VSP_055428|||http://purl.uniprot.org/annotation/VSP_055429
http://togogenome.org/gene/9606:RAPGEF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z278|||http://purl.uniprot.org/uniprot/Q8WZA2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||DEP|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||N-terminal Ras-GEF|||Rap guanine nucleotide exchange factor 4|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068870|||http://purl.uniprot.org/annotation/VSP_007611|||http://purl.uniprot.org/annotation/VSP_007612|||http://purl.uniprot.org/annotation/VSP_007613|||http://purl.uniprot.org/annotation/VSP_054423|||http://purl.uniprot.org/annotation/VSP_054424
http://togogenome.org/gene/9606:MPEG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M385                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta stranded|||Cleavage; by LGMN|||Cleavage; by trypsin|||Decreased defense response to bacterium.|||Helical|||In IMD77; decreased defense response to bacterium.|||In IMD77; unknown pathological significance; decreased defense response to bacterium.|||MACPF|||Macrophage-expressed gene 1 protein|||Macrophage-expressed gene 1 protein, processed form|||N-linked (GlcNAc...) asparagine|||P2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324143|||http://purl.uniprot.org/annotation/PRO_0000459022|||http://purl.uniprot.org/annotation/VAR_051200|||http://purl.uniprot.org/annotation/VAR_051201|||http://purl.uniprot.org/annotation/VAR_051202|||http://purl.uniprot.org/annotation/VAR_085655|||http://purl.uniprot.org/annotation/VAR_085656|||http://purl.uniprot.org/annotation/VAR_085657|||http://purl.uniprot.org/annotation/VAR_085658|||http://purl.uniprot.org/annotation/VAR_085659
http://togogenome.org/gene/9606:ALX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H161                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein aristaless-like 4|||In CRS5; low-penetrance mutation associated with disease susceptibility; results in gain-of-function.|||In PFM2.|||OAR|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048814|||http://purl.uniprot.org/annotation/VAR_010783|||http://purl.uniprot.org/annotation/VAR_010784|||http://purl.uniprot.org/annotation/VAR_010785|||http://purl.uniprot.org/annotation/VAR_010897|||http://purl.uniprot.org/annotation/VAR_058413|||http://purl.uniprot.org/annotation/VAR_069279|||http://purl.uniprot.org/annotation/VAR_069280|||http://purl.uniprot.org/annotation/VAR_069281
http://togogenome.org/gene/9606:HAPLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7T8|||http://purl.uniprot.org/uniprot/H3BTH8|||http://purl.uniprot.org/uniprot/Q96S86                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  Hyaluronan and proteoglycan link protein 3|||Ig-like|||Ig-like V-type|||Link|||Link 1|||Link 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013190|||http://purl.uniprot.org/annotation/PRO_5002722793
http://togogenome.org/gene/9606:ROBO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYV8|||http://purl.uniprot.org/uniprot/Q8WZ75                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In AOVD3; loss of endothelial barrier function in a dextran permeability assay.|||In AOVD3; unknown pathological significance.|||In AOVD3; unknown pathological significance; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Roundabout homolog 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031040|||http://purl.uniprot.org/annotation/VAR_053644|||http://purl.uniprot.org/annotation/VAR_062146|||http://purl.uniprot.org/annotation/VAR_083093|||http://purl.uniprot.org/annotation/VAR_083094|||http://purl.uniprot.org/annotation/VAR_083095|||http://purl.uniprot.org/annotation/VAR_083096|||http://purl.uniprot.org/annotation/VAR_083097|||http://purl.uniprot.org/annotation/VAR_083098|||http://purl.uniprot.org/annotation/VAR_083099|||http://purl.uniprot.org/annotation/VAR_083100|||http://purl.uniprot.org/annotation/VAR_083101|||http://purl.uniprot.org/annotation/VAR_083102|||http://purl.uniprot.org/annotation/VSP_010654|||http://purl.uniprot.org/annotation/VSP_010657|||http://purl.uniprot.org/annotation/VSP_010658|||http://purl.uniprot.org/annotation/VSP_010659
http://togogenome.org/gene/9606:TGFBR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8KWK3|||http://purl.uniprot.org/uniprot/Q03167                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with TGF-beta ligand|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Transforming growth factor beta receptor type 3|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041663|||http://purl.uniprot.org/annotation/PRO_5014220902|||http://purl.uniprot.org/annotation/VAR_014920|||http://purl.uniprot.org/annotation/VAR_020891|||http://purl.uniprot.org/annotation/VAR_020892|||http://purl.uniprot.org/annotation/VAR_020893|||http://purl.uniprot.org/annotation/VAR_020894|||http://purl.uniprot.org/annotation/VAR_057499|||http://purl.uniprot.org/annotation/VAR_066625|||http://purl.uniprot.org/annotation/VSP_040018
http://togogenome.org/gene/9606:DNAJC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes the interaction with MCM2, TONSL and histones H3.3 and H4. Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4.|||Basic and acidic residues|||Disordered|||Disrupts the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4.|||DnaJ homolog subfamily C member 9|||Does not affect interaction with histones.|||Increased binding to histones H3 and H4. Less integration of histones H3 and H4 in chromatin. Increased recruitment of histone deposition factors to chromatin. Trapped on chromatin throughout the cell cycle in a manner depending on histone-binding. Released from chromatin trap; when associated with Ala-224; Ala-227; Ala-238 and Ala-242.|||J|||Partial loss of histone dimer H3-H4 interaction. Reduces the co-chaperone complex formation with MCM2; histone H3.3 and H4.|||Partial loss of histone dimer H3-H4 interaction. Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4.|||Phosphoserine|||Reduces the co-chaperone complex formation with MCM2; histone H3.3 and H4.|||Reduces the formation of the co-chaperone complex with MCM2 and histones H3.3 and H4.|||Required for histone binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071063
http://togogenome.org/gene/9606:GPIHBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||GPI-anchor amidated glycine|||Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1|||Important for LPL transport to the lumenal surface of endothelial cells|||Important for interaction with LPL|||In HLPP1D.|||In HLPP1D; a patient with chylomicronemia; no effect on protein expression at the cell surface; loss of interaction with LPL; loss of interaction with chylomicrons; promotes formation of dimers and oligomers reducing number of monomers.|||In HLPP1D; affects protein expression at the cell surface; reduces interaction with LPL.|||In HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers.|||In HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers.|||In HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers.|||In HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers.|||In HLPP1D; drastically affects interaction with LPL; promotes formation of dimers and oligomers reducing number of monomers.|||In HLPP1D; unknown pathological significance; results in decreased GPIHBP1 expression; promotes formation of dimers and oligomers severely reducing number of monomers; does not affect interaction with LPL when associated in cis with F-14 in one individual.|||It may act as a disease modifier preserving from severe HLPP1D when associated with R-68 or F-89; results in increased GPIHBP1 expression at the cell surface; does not affect interaction with LPL when associated in cis with R-68 in one individual.|||Loss of interaction with LPL. Only slightly increased formation of dimers and oligomers. No effect on number of monomers.|||Loss of sulfotyrosine formation.|||N-linked (GlcNAc...) asparagine|||No discernible effect on interaction with LPL, chylomicrons or APOA5.|||No effect on number of monomers.|||Only slightly increased formation of dimers and oligomers. No effect on number of monomers. Loss of LPL interaction.|||Promotes formation of dimers and oligomers reducing number of monomers.|||Promotes formation of dimers and oligomers reducing number of monomers. Loss of LPL interaction.|||Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL.|||Promotes formation of dimers and oligomers severely reducing number of monomers.|||Removed in mature form|||Retained some interaction with LPL. No effect on number of monomers.|||Sulfotyrosine|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318208|||http://purl.uniprot.org/annotation/PRO_0000429858|||http://purl.uniprot.org/annotation/VAR_044503|||http://purl.uniprot.org/annotation/VAR_044504|||http://purl.uniprot.org/annotation/VAR_058086|||http://purl.uniprot.org/annotation/VAR_071881|||http://purl.uniprot.org/annotation/VAR_071882|||http://purl.uniprot.org/annotation/VAR_071883|||http://purl.uniprot.org/annotation/VAR_071884|||http://purl.uniprot.org/annotation/VAR_077634|||http://purl.uniprot.org/annotation/VAR_077635|||http://purl.uniprot.org/annotation/VAR_077636|||http://purl.uniprot.org/annotation/VAR_077637|||http://purl.uniprot.org/annotation/VAR_077638|||http://purl.uniprot.org/annotation/VAR_077639
http://togogenome.org/gene/9606:TRARG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXB3                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Trafficking regulator of GLUT4 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263639|||http://purl.uniprot.org/annotation/VAR_029589|||http://purl.uniprot.org/annotation/VAR_029590|||http://purl.uniprot.org/annotation/VAR_029591|||http://purl.uniprot.org/annotation/VAR_029592|||http://purl.uniprot.org/annotation/VAR_029593|||http://purl.uniprot.org/annotation/VAR_029594
http://togogenome.org/gene/9606:DNAH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0G6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Dynein axonemal heavy chain 6|||Found in a patient with azoospermia; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317665|||http://purl.uniprot.org/annotation/VAR_080035|||http://purl.uniprot.org/annotation/VSP_031122|||http://purl.uniprot.org/annotation/VSP_031123|||http://purl.uniprot.org/annotation/VSP_031124|||http://purl.uniprot.org/annotation/VSP_031125|||http://purl.uniprot.org/annotation/VSP_031126|||http://purl.uniprot.org/annotation/VSP_031127|||http://purl.uniprot.org/annotation/VSP_031128|||http://purl.uniprot.org/annotation/VSP_031129|||http://purl.uniprot.org/annotation/VSP_031130
http://togogenome.org/gene/9606:RAB18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP72                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In WARBM3.|||In WARBM3; abnormal endoplasmic reticulum structure; in fibroblasts ER spread away from the perinuclear region into the cell periphery and there is a loss of fragmentation of ER tubules.|||In WARBM3; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of localization to lipid droplets and interaction with ZFYVE1.|||N-acetylmethionine|||No loss of localization to lipid droplets and interaction with ZFYVE1.|||Phosphoserine|||Ras-related protein Rab-18|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121193|||http://purl.uniprot.org/annotation/PRO_0000370761|||http://purl.uniprot.org/annotation/VAR_034432|||http://purl.uniprot.org/annotation/VAR_051713|||http://purl.uniprot.org/annotation/VAR_066495|||http://purl.uniprot.org/annotation/VAR_066496|||http://purl.uniprot.org/annotation/VAR_086022|||http://purl.uniprot.org/annotation/VSP_043912|||http://purl.uniprot.org/annotation/VSP_044883
http://togogenome.org/gene/9606:NKG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16617                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein NKG7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164667
http://togogenome.org/gene/9606:EPOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19235                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold reduction in EPO binding.|||16-fold reduction in EPO binding.|||60-fold reduction in EPO binding.|||8-fold reduction in EPO binding.|||Box 1 motif|||Cytoplasmic|||Disordered|||Erythropoietin receptor|||Extracellular|||Fibronectin type-III|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced EPO binding.|||Helical|||ITIM motif|||In ECYT1 and erythroleukemia.|||In isoform EPOR-S.|||In isoform EPOR-T.|||Inhibition of STAT1/STAT3 activity. No effect on STAT5 activity. Some loss of SOCS3 binding.|||Interaction with APS and STAT5, and activation|||Interaction with PTPN6|||Little effect on EPO binding.|||N-linked (GlcNAc...) asparagine|||No effect on STAT1/STAT3 nor STAT5 activity.|||Phosphotyrosine; by JAK2|||Polar residues|||Required for CrkL binding|||Required for STAT1/STAT3 activation|||Required for STAT5/PTPN11/SOCS3 binding|||Required for high-affinity SOCS3 binding|||Required for ligand binding|||Some loss of SOCS3 binding.|||Some reduction in EPO binding.|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010868|||http://purl.uniprot.org/annotation/VAR_027372|||http://purl.uniprot.org/annotation/VAR_027373|||http://purl.uniprot.org/annotation/VAR_033919|||http://purl.uniprot.org/annotation/VSP_009508|||http://purl.uniprot.org/annotation/VSP_009509|||http://purl.uniprot.org/annotation/VSP_009510|||http://purl.uniprot.org/annotation/VSP_009511
http://togogenome.org/gene/9606:PIGP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57054                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In DEE55; reduced GPI-anchor biosynthetic process; may affect expression of isoform A.|||In isoform A.|||In isoform C.|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191783|||http://purl.uniprot.org/annotation/VAR_050538|||http://purl.uniprot.org/annotation/VAR_050539|||http://purl.uniprot.org/annotation/VAR_061521|||http://purl.uniprot.org/annotation/VAR_079291|||http://purl.uniprot.org/annotation/VSP_004202|||http://purl.uniprot.org/annotation/VSP_004203|||http://purl.uniprot.org/annotation/VSP_004204
http://togogenome.org/gene/9606:KLHDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEP7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300464|||http://purl.uniprot.org/annotation/VAR_034873|||http://purl.uniprot.org/annotation/VAR_034874|||http://purl.uniprot.org/annotation/VAR_050056|||http://purl.uniprot.org/annotation/VSP_027807|||http://purl.uniprot.org/annotation/VSP_027808|||http://purl.uniprot.org/annotation/VSP_027809|||http://purl.uniprot.org/annotation/VSP_027810
http://togogenome.org/gene/9606:OTULIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BN8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with RNF31.|||Abolishes deubiquitinase activity.|||Decreased activity toward linear ubiquitin.|||Decreased affinity for linear diubiquitin.|||Disordered|||Does not affect down-regulation of NF-kappa-B signaling.|||Impaired deubiquitinase activity.|||In AIPDS and IMD107; decreased stability; impaired ability to mediate deubiquitination of linear polyubiquitin chains; loss of NF-kappa-B inhibition and increased NF-kappa-B signaling; does not affect ability to interact with RNF31.|||In AIPDS and IMD107; slightly impaired ability to mediate deubiquitination of linear polyubiquitin chains; does not affect ability to interact with RNF31; severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling.|||In AIPDS; decreased function in protein linear deubiquitination.|||In IMD107; loss of NF-kappa-B inhibition and increased NF-kappa-B signaling.|||In IMD107; severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling.|||Linear diubiquitin binding|||Nucleophile|||OTU|||PIM motif|||Phosphotyrosine|||Reduced interaction with RNF31.|||Results in strong reduction of kcat while not affecting KM.|||Severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling.|||Stabilizes H-339 in the active conformation, generating a more reactive enzyme.|||Stabilizes H-339 in the active conformation, generating a more reactive enzyme. Severely decreased NF-kappa-B inhibition and increased NF-kappa-B signaling.|||Strongly reduced interaction with RNF31.|||Ubiquitin thioesterase otulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261637|||http://purl.uniprot.org/annotation/VAR_029469|||http://purl.uniprot.org/annotation/VAR_053819|||http://purl.uniprot.org/annotation/VAR_053820|||http://purl.uniprot.org/annotation/VAR_076865|||http://purl.uniprot.org/annotation/VAR_076866|||http://purl.uniprot.org/annotation/VAR_087550|||http://purl.uniprot.org/annotation/VAR_087551|||http://purl.uniprot.org/annotation/VAR_087552|||http://purl.uniprot.org/annotation/VAR_087553|||http://purl.uniprot.org/annotation/VAR_087554|||http://purl.uniprot.org/annotation/VAR_087555
http://togogenome.org/gene/9606:SMIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVW6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Small integral membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318960
http://togogenome.org/gene/9606:ZNF202                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN61|||http://purl.uniprot.org/uniprot/O95125                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform Alpha.|||KRAB|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger protein 202                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047450|||http://purl.uniprot.org/annotation/VAR_007818|||http://purl.uniprot.org/annotation/VAR_023975|||http://purl.uniprot.org/annotation/VSP_006902
http://togogenome.org/gene/9606:CA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07451|||http://purl.uniprot.org/uniprot/V9HWA3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 3|||Enhanced activity by at least 10-fold.|||Enhanced proton transfer in catalysis.|||Involved in proton transfer|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||S-glutathionyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077426|||http://purl.uniprot.org/annotation/VAR_016180
http://togogenome.org/gene/9606:OR8B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RC9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150656|||http://purl.uniprot.org/annotation/VAR_024115|||http://purl.uniprot.org/annotation/VAR_053239|||http://purl.uniprot.org/annotation/VAR_053240|||http://purl.uniprot.org/annotation/VAR_053241
http://togogenome.org/gene/9606:LINC02210-CRHR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMR5|||http://purl.uniprot.org/uniprot/P34998                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Corticotropin-releasing factor receptor 1|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for antagonist binding|||Important for peptide agonist binding|||In isoform 5.|||In isoform CRF-R2, isoform CRF-R3 and isoform CRF-R4.|||In isoform CRF-R3.|||In isoform CRF-R4.|||Increases antagonist binding.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes antagonist binding.|||Phosphoserine; by PKA|||Pro residues|||Slightly reduces antagonist binding.|||Strongly reduces antagonist binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012814|||http://purl.uniprot.org/annotation/VSP_001996|||http://purl.uniprot.org/annotation/VSP_001997|||http://purl.uniprot.org/annotation/VSP_001998|||http://purl.uniprot.org/annotation/VSP_045434
http://togogenome.org/gene/9606:PELI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FA3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase pellino homolog 1|||FHA; atypical|||Loss of ability to ubiquitinate RIPK3. Loss of interaction with RIPK1, IRAK1 and RIPK3.|||Loss of ability to ubiquitinate RIPK3. No loss of interaction with RIPK3.|||Ring-like domain; necessary for ubiqitination of RIPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194172
http://togogenome.org/gene/9606:EXOC3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VI1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Exocyst complex component 3-like protein|||In a breast cancer sample; somatic mutation.|||Mediates interaction with EXOC2, EXOC4 and EXOC5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309474|||http://purl.uniprot.org/annotation/VAR_036959|||http://purl.uniprot.org/annotation/VAR_036960|||http://purl.uniprot.org/annotation/VAR_037002|||http://purl.uniprot.org/annotation/VAR_037003
http://togogenome.org/gene/9606:PEA15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AKZ4|||http://purl.uniprot.org/uniprot/B1AKZ5|||http://purl.uniprot.org/uniprot/Q15121                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Astrocytic phosphoprotein PEA-15|||DED|||In isoform 2.|||Microtubule-binding|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191282|||http://purl.uniprot.org/annotation/VSP_056174
http://togogenome.org/gene/9606:HOOK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VS8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||Disordered|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein Hook homolog 3|||Required for association with Golgi|||Required for interaction with MSR1|||Sufficient for interaction with microtubules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219197|||http://purl.uniprot.org/annotation/VAR_035710|||http://purl.uniprot.org/annotation/VAR_049363
http://togogenome.org/gene/9606:AZU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20160                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Azurocidin|||Dipeptide found in non-mature form|||Loss of antibiotic activity.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Peptidase S1|||Possesses antibiotic activity|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027705|||http://purl.uniprot.org/annotation/PRO_0000027706|||http://purl.uniprot.org/annotation/PRO_0000435372|||http://purl.uniprot.org/annotation/PRO_0000435373
http://togogenome.org/gene/9606:PLPP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZY2                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphatase activity; when associated with A-109 and with A-146.|||Loss of phosphatase activity; when associated with A-109 and with A-202.|||Loss of phosphatase activity; when associated with A-146 and with A-202.|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phospholipid phosphatase 4|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286943|||http://purl.uniprot.org/annotation/VSP_025237|||http://purl.uniprot.org/annotation/VSP_025238|||http://purl.uniprot.org/annotation/VSP_025239|||http://purl.uniprot.org/annotation/VSP_025240
http://togogenome.org/gene/9606:MIER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3K6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ELM2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mesoderm induction early response protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313680|||http://purl.uniprot.org/annotation/VAR_037699|||http://purl.uniprot.org/annotation/VAR_037700|||http://purl.uniprot.org/annotation/VAR_037701|||http://purl.uniprot.org/annotation/VAR_037702|||http://purl.uniprot.org/annotation/VSP_030099|||http://purl.uniprot.org/annotation/VSP_030100|||http://purl.uniprot.org/annotation/VSP_030101|||http://purl.uniprot.org/annotation/VSP_030102|||http://purl.uniprot.org/annotation/VSP_030103
http://togogenome.org/gene/9606:TEX26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6G2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Testis-expressed protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263723|||http://purl.uniprot.org/annotation/VAR_029615
http://togogenome.org/gene/9606:GPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75487                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with features of Robinow syndrome; unknown pathological significance.|||GPI-anchor amidated serine|||Glypican-4|||In KPTS; increased proteasomal degradation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Removed in mature form|||Secreted glypican-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012315|||http://purl.uniprot.org/annotation/PRO_0000012316|||http://purl.uniprot.org/annotation/PRO_0000333847|||http://purl.uniprot.org/annotation/VAR_016191|||http://purl.uniprot.org/annotation/VAR_016192|||http://purl.uniprot.org/annotation/VAR_082622|||http://purl.uniprot.org/annotation/VAR_082623|||http://purl.uniprot.org/annotation/VAR_083241|||http://purl.uniprot.org/annotation/VSP_056570
http://togogenome.org/gene/9606:TTC23L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IS63|||http://purl.uniprot.org/uniprot/Q6PF05                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Tetratricopeptide repeat protein 23-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336080|||http://purl.uniprot.org/annotation/VAR_043539|||http://purl.uniprot.org/annotation/VAR_043540|||http://purl.uniprot.org/annotation/VAR_043541|||http://purl.uniprot.org/annotation/VAR_043542|||http://purl.uniprot.org/annotation/VAR_043543|||http://purl.uniprot.org/annotation/VAR_043544|||http://purl.uniprot.org/annotation/VSP_033814|||http://purl.uniprot.org/annotation/VSP_033815|||http://purl.uniprot.org/annotation/VSP_033816
http://togogenome.org/gene/9606:GZMM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51124                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Granzyme M|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027421|||http://purl.uniprot.org/annotation/PRO_0000027422|||http://purl.uniprot.org/annotation/VAR_051829
http://togogenome.org/gene/9606:STUM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YW2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Protein stum homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278635
http://togogenome.org/gene/9606:CYP4F12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCS2                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4F12|||Helical|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051857|||http://purl.uniprot.org/annotation/VAR_013244|||http://purl.uniprot.org/annotation/VAR_013245|||http://purl.uniprot.org/annotation/VAR_013246|||http://purl.uniprot.org/annotation/VAR_013247|||http://purl.uniprot.org/annotation/VAR_048459|||http://purl.uniprot.org/annotation/VAR_048460|||http://purl.uniprot.org/annotation/VSP_055581|||http://purl.uniprot.org/annotation/VSP_055582
http://togogenome.org/gene/9606:CRTAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75718                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cartilage-associated protein|||In OI7.|||In OI7; severe form.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006319|||http://purl.uniprot.org/annotation/VAR_032846|||http://purl.uniprot.org/annotation/VAR_053050|||http://purl.uniprot.org/annotation/VAR_054442|||http://purl.uniprot.org/annotation/VAR_063599|||http://purl.uniprot.org/annotation/VAR_063600
http://togogenome.org/gene/9606:SEPTIN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU2|||http://purl.uniprot.org/uniprot/Q8IYM1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to GTP and to SEPTIN11, and also abolishes the ability of SEPTIN12 to form filamentous structures.|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In SPGF10; results in significantly reduced GTP hydrolysis due to impaired GTP binding; disrupts interaction with SEPTIN7, SEPTIN6 and SEPTIN2; absence of SEPTIN12, SEPTIN7, SEPTIN6, SEPTIN2 and SEPTIN4 from the sperm annulus; disrupts interaction with LMNB1.|||In SPGF10; results in significantly reduced GTP hydrolysis; disrupts interaction with SEPTIN7, SEPTIN6 and SEPTIN2; decreases interaction with SPAG4.|||In isoform 2.|||Interaction with SEPTIN7|||Self-association (via N-terminus) to polymerize octameric septin 12-7-6-2/4-2/4-6-7-12 filaments|||Septin-12|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312860|||http://purl.uniprot.org/annotation/VAR_057176|||http://purl.uniprot.org/annotation/VAR_068097|||http://purl.uniprot.org/annotation/VAR_068098|||http://purl.uniprot.org/annotation/VSP_029918
http://togogenome.org/gene/9606:IGF1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J5X1|||http://purl.uniprot.org/uniprot/P08069                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||IRS1- and SHC1-binding|||In IGF1RES; has decreased IGF1R function.|||In IGF1RES; leads to failure of processing of the IGF1R proreceptor to mature IGF1R.|||In IGF1RES; significant decrease in IGF1-induced DNA synthesis and AKT1 phosphorylation in patient fibroblasts.|||In IGF1RES; unknown pathological significance; significant decrease in IGF1-induced DNA synthesis; significant increase in IGF1-induced AKT1 phosphorylation in patient fibroblasts.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a renal chromophobe sample; somatic mutation.|||Insulin-like growth factor 1 receptor alpha chain|||Insulin-like growth factor 1 receptor beta chain|||Kinase inactive. Abolishes tyrosine phosphorylation and abolishes interaction with IRS1, SHC1 and PIK3R1.|||Loss of GRB10-binding.|||N-linked (GlcNAc...) asparagine|||No effect on GRB10-binding.|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Proton donor/acceptor|||Reduces tyrosine phosphorylation. Abolishes interaction with IRS1 and SHC1. Does not abolish interaction with PIK3R1, nor with GRB10.|||Tyrosine-protein kinase receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016681|||http://purl.uniprot.org/annotation/PRO_0000016682|||http://purl.uniprot.org/annotation/PRO_5030167814|||http://purl.uniprot.org/annotation/VAR_018855|||http://purl.uniprot.org/annotation/VAR_018856|||http://purl.uniprot.org/annotation/VAR_034891|||http://purl.uniprot.org/annotation/VAR_034892|||http://purl.uniprot.org/annotation/VAR_034893|||http://purl.uniprot.org/annotation/VAR_034894|||http://purl.uniprot.org/annotation/VAR_034895|||http://purl.uniprot.org/annotation/VAR_034896|||http://purl.uniprot.org/annotation/VAR_034897|||http://purl.uniprot.org/annotation/VAR_041424|||http://purl.uniprot.org/annotation/VAR_041425|||http://purl.uniprot.org/annotation/VAR_041426|||http://purl.uniprot.org/annotation/VAR_041427|||http://purl.uniprot.org/annotation/VAR_041428|||http://purl.uniprot.org/annotation/VAR_076247|||http://purl.uniprot.org/annotation/VAR_076248|||http://purl.uniprot.org/annotation/VAR_076249|||http://purl.uniprot.org/annotation/VAR_076250
http://togogenome.org/gene/9606:PCGF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ06|||http://purl.uniprot.org/uniprot/B3KWT8|||http://purl.uniprot.org/uniprot/B4DTN5|||http://purl.uniprot.org/uniprot/Q3KNV8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with BCORL1|||Polycomb group RING finger protein 3|||RAWUL|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277864|||http://purl.uniprot.org/annotation/VSP_023115
http://togogenome.org/gene/9606:RCBTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR20|||http://purl.uniprot.org/uniprot/Q8NDN9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB 1|||BTB 2|||In RDEOA.|||In RDEOA; unknown pathological significance.|||In isoform 2.|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 and BTB domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206642|||http://purl.uniprot.org/annotation/VAR_024757|||http://purl.uniprot.org/annotation/VAR_024830|||http://purl.uniprot.org/annotation/VAR_077962|||http://purl.uniprot.org/annotation/VAR_077963|||http://purl.uniprot.org/annotation/VAR_077964|||http://purl.uniprot.org/annotation/VAR_077965|||http://purl.uniprot.org/annotation/VAR_077966|||http://purl.uniprot.org/annotation/VAR_077967|||http://purl.uniprot.org/annotation/VSP_040263|||http://purl.uniprot.org/annotation/VSP_040264
http://togogenome.org/gene/9606:INSYN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSG2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Inhibitory synaptic factor 2A|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329446|||http://purl.uniprot.org/annotation/VAR_042679|||http://purl.uniprot.org/annotation/VSP_056622
http://togogenome.org/gene/9606:SHANK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJ45|||http://purl.uniprot.org/uniprot/A6NHU9|||http://purl.uniprot.org/uniprot/Q9UPX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||Found in a child with developmental disabilities; unknown pathological significance.|||In isoform 1.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 4.|||O-linked (GlcNAc) threonine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SAM|||SH3|||SH3 and multiple ankyrin repeat domains protein 2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174673|||http://purl.uniprot.org/annotation/VAR_085767|||http://purl.uniprot.org/annotation/VSP_061470|||http://purl.uniprot.org/annotation/VSP_061471|||http://purl.uniprot.org/annotation/VSP_061472|||http://purl.uniprot.org/annotation/VSP_061473|||http://purl.uniprot.org/annotation/VSP_061474
http://togogenome.org/gene/9606:AGPAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCV5|||http://purl.uniprot.org/uniprot/Q99943                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-acyl-sn-glycerol-3-phosphate acyltransferase alpha|||Cytoplasmic|||EGTR motif|||HXXXXD motif|||Helical|||Lumenal|||Phospholipid/glycerol acyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208190|||http://purl.uniprot.org/annotation/VAR_050593
http://togogenome.org/gene/9606:RTL8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWD3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Retrotransposon Gag-like protein 8A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311693|||http://purl.uniprot.org/annotation/VAR_060162
http://togogenome.org/gene/9606:DUSP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAL9|||http://purl.uniprot.org/uniprot/Q6P9C2|||http://purl.uniprot.org/uniprot/Q99956                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dual specificity protein phosphatase 9|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094812
http://togogenome.org/gene/9606:FGF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A515|||http://purl.uniprot.org/uniprot/P55075                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fibroblast growth factor|||Fibroblast growth factor 8|||In HH6; phenotype consistent with Kallmann syndrome.|||In HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism.|||In HH6; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; some patients also carry mutations in FGFR1.|||In isoform FGF-8A.|||In isoform FGF-8B.|||In isoform FGF-8F.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008970|||http://purl.uniprot.org/annotation/PRO_5005120926|||http://purl.uniprot.org/annotation/VAR_057962|||http://purl.uniprot.org/annotation/VAR_057963|||http://purl.uniprot.org/annotation/VAR_057964|||http://purl.uniprot.org/annotation/VAR_057965|||http://purl.uniprot.org/annotation/VAR_057966|||http://purl.uniprot.org/annotation/VAR_057967|||http://purl.uniprot.org/annotation/VSP_001524|||http://purl.uniprot.org/annotation/VSP_001525|||http://purl.uniprot.org/annotation/VSP_001526
http://togogenome.org/gene/9606:PPP4R4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUP7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with PPP4C.|||Basic and acidic residues|||Diminishes interaction with PPP4C.|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311850|||http://purl.uniprot.org/annotation/VSP_029616|||http://purl.uniprot.org/annotation/VSP_029617
http://togogenome.org/gene/9606:MTHFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11586                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-1-tetrahydrofolate synthase, cytoplasmic|||C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed|||Decreased methylenetetrahydrofolate dehydrogenase (NADP+) activity over 90%. Loss of methenyltetrahydrofolate cyclohydrolase activity.|||Formyltetrahydrofolate synthetase domain|||In CIMAH.|||In NTDFS; associated with disease susceptibility.|||In NTDFS; associated with disease susceptibility; increases risk for congenital heart defects; decreased enzyme stability; no effect on methylenetetrahydrofolate dehydrogenase (NADP+) activity; no effect on formyltetrahydrofolate synthetase activity.|||Methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase (D/C) domain|||Moderate decrease of methylenetetrahydrofolate dehydrogenase (NADP+) activity. Loss of methenyltetrahydrofolate cyclohydrolase activity. Strongly decreased affinity for NADP. Increased affinity for 5,10-methenyltetrahydrofolate.|||N-acetylmethionine|||No effect on methylenetetrahydrofolate dehydrogenase (NADP+) activity. No effect on methenyltetrahydrofolate cyclohydrolase activity. Decreased affinity for NADP.|||Phosphoserine|||Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 50%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 87%.|||Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 75%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 99%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.|||Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity by 99%. Reduced methenyltetrahydrofolate cyclohydrolase activity by 70%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.|||Reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity. Reduced methenyltetrahydrofolate cyclohydrolase activity by 99%. No effect on affinity for NADP and 5,10-methenyltetrahydrofolate.|||Removed; alternate|||Slightly reduced methylenetetrahydrofolate dehydrogenase (NADP+) activity. Slightly reduced methenyltetrahydrofolate cyclohydrolase activity. Decreased affinity for NADP and for 5,10-methenyltetrahydrofolate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199321|||http://purl.uniprot.org/annotation/PRO_0000423280|||http://purl.uniprot.org/annotation/VAR_010241|||http://purl.uniprot.org/annotation/VAR_010251|||http://purl.uniprot.org/annotation/VAR_016232|||http://purl.uniprot.org/annotation/VAR_032789|||http://purl.uniprot.org/annotation/VAR_032790|||http://purl.uniprot.org/annotation/VAR_055458|||http://purl.uniprot.org/annotation/VAR_074075|||http://purl.uniprot.org/annotation/VAR_074076|||http://purl.uniprot.org/annotation/VAR_074077|||http://purl.uniprot.org/annotation/VAR_080873|||http://purl.uniprot.org/annotation/VAR_080874
http://togogenome.org/gene/9606:PCDHGA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60330                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003970|||http://purl.uniprot.org/annotation/VSP_008682|||http://purl.uniprot.org/annotation/VSP_008683
http://togogenome.org/gene/9606:ZNF254                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZJ7|||http://purl.uniprot.org/uniprot/A0A087X0A2|||http://purl.uniprot.org/uniprot/B4E0L9|||http://purl.uniprot.org/uniprot/F5H2M4|||http://purl.uniprot.org/uniprot/O75437|||http://purl.uniprot.org/uniprot/Q7Z2R1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 254                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047487|||http://purl.uniprot.org/annotation/VAR_047461|||http://purl.uniprot.org/annotation/VAR_047462|||http://purl.uniprot.org/annotation/VAR_047463|||http://purl.uniprot.org/annotation/VAR_047464|||http://purl.uniprot.org/annotation/VAR_059906|||http://purl.uniprot.org/annotation/VSP_022010
http://togogenome.org/gene/9606:STK11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4D1|||http://purl.uniprot.org/uniprot/Q15831                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Enhanced phosphorylation at Thr-336 and Ser-428, enhanced cytoplasmic localization and increased kinase activity.|||Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-204.|||In PJS.|||In PJS; abolishes kinase activity, leading to loss of autophosphorylation.|||In PJS; late onset suggests reduced penetrance.|||In PJS; loss of kinase activity, leading to greatly reduced autophosphorylation; fails to phosphorylate PTEN in vitro; no significant effect on nucleocytoplasmic localization.|||In PJS; pathogenicity uncertain; no effect heterotrimeric complex assembly with STRADA and CAB39.|||In TGCT; a tumor with seminoma and teratoma components; associated with severely impaired but detectable kinase activity; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; predominantly nuclear localization.|||In a metastatic melanoma sample; somatic mutation.|||In cervical cancer; somatic mutation.|||In cervical carcinoma; somatic mutation.|||In colorectal cancer; no effect heterotrimeric complex assembly with STRADA and CAB39.|||In colorectal cancer; somatic mutation.|||In colorectal cancer; somatic mutation; impaired kinase activity.|||In colorectal cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.|||In colorectal cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.|||In gastric carcinoma; no effect heterotrimeric complex assembly with STRADA and CAB39.|||In isoform 2.|||In lung cancer; somatic mutation.|||In melanoma; sporadic malignant; somatic mutation.|||In ovarian carcinoma; somatic mutation.|||In sporadic cancer; somatic mutation; Loss of kinase activity.|||In sporadic cancer; somatic mutation; does not affect kinase activity.|||In sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39.|||In sporadic cancer; somatic mutation; impairs heterotrimeric complex assembly with STRADA and CAB39; requires 2 nucleotide substitutions.|||In sporadic cancer; somatic mutation; no effect heterotrimeric complex assembly with STRADA and CAB39.|||In sporadic cancer; somatic mutation; no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39.|||Loss of kinase activity, leading to greatly reduced autophosphorylation.|||Loss of kinase activity, leading to reduced autophosphorylation and acting as a dominant-negative mutant.|||Loss of kinase activity.|||N6-acetyllysine|||No effect on basal nucleocytoplasmic localization, but fails to translocate to the cytoplasm when coexpressed with SIRT1.|||No effect on kinase activity.|||No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39; when associated with A-74.|||Phosphoserine|||Phosphoserine; by autocatalysis, PKA, PKC/PRKCZ and RPS6KA1|||Phosphothreonine; by ATM and autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced phosphorylation.|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine|||Serine/threonine-protein kinase STK11|||Sufficient for interaction with SIRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086699|||http://purl.uniprot.org/annotation/PRO_0000422300|||http://purl.uniprot.org/annotation/VAR_006202|||http://purl.uniprot.org/annotation/VAR_006203|||http://purl.uniprot.org/annotation/VAR_007920|||http://purl.uniprot.org/annotation/VAR_007921|||http://purl.uniprot.org/annotation/VAR_007922|||http://purl.uniprot.org/annotation/VAR_033138|||http://purl.uniprot.org/annotation/VAR_033139|||http://purl.uniprot.org/annotation/VAR_033140|||http://purl.uniprot.org/annotation/VAR_033141|||http://purl.uniprot.org/annotation/VAR_033142|||http://purl.uniprot.org/annotation/VAR_033143|||http://purl.uniprot.org/annotation/VAR_033144|||http://purl.uniprot.org/annotation/VAR_041139|||http://purl.uniprot.org/annotation/VAR_065627|||http://purl.uniprot.org/annotation/VAR_065628|||http://purl.uniprot.org/annotation/VAR_065629|||http://purl.uniprot.org/annotation/VAR_065630|||http://purl.uniprot.org/annotation/VAR_065631|||http://purl.uniprot.org/annotation/VAR_065632|||http://purl.uniprot.org/annotation/VAR_065633|||http://purl.uniprot.org/annotation/VAR_065634|||http://purl.uniprot.org/annotation/VAR_065635|||http://purl.uniprot.org/annotation/VAR_065636|||http://purl.uniprot.org/annotation/VAR_065637|||http://purl.uniprot.org/annotation/VAR_065638|||http://purl.uniprot.org/annotation/VAR_065639|||http://purl.uniprot.org/annotation/VAR_065640|||http://purl.uniprot.org/annotation/VAR_065641|||http://purl.uniprot.org/annotation/VAR_065642|||http://purl.uniprot.org/annotation/VAR_065643|||http://purl.uniprot.org/annotation/VAR_065644|||http://purl.uniprot.org/annotation/VAR_065645|||http://purl.uniprot.org/annotation/VAR_065646|||http://purl.uniprot.org/annotation/VAR_065647|||http://purl.uniprot.org/annotation/VAR_065648|||http://purl.uniprot.org/annotation/VAR_065649|||http://purl.uniprot.org/annotation/VAR_065650|||http://purl.uniprot.org/annotation/VAR_065651|||http://purl.uniprot.org/annotation/VAR_065652|||http://purl.uniprot.org/annotation/VAR_065653|||http://purl.uniprot.org/annotation/VAR_065654|||http://purl.uniprot.org/annotation/VAR_065655|||http://purl.uniprot.org/annotation/VAR_065656|||http://purl.uniprot.org/annotation/VAR_065657|||http://purl.uniprot.org/annotation/VAR_065658|||http://purl.uniprot.org/annotation/VAR_065659|||http://purl.uniprot.org/annotation/VAR_065660|||http://purl.uniprot.org/annotation/VAR_071057|||http://purl.uniprot.org/annotation/VAR_071058|||http://purl.uniprot.org/annotation/VAR_071059|||http://purl.uniprot.org/annotation/VSP_041746
http://togogenome.org/gene/9606:RBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62877                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RBX1|||E3 ubiquitin-protein ligase RBX1, N-terminally processed|||N-acetylalanine; in E3 ubiquitin-protein ligase RBX1, N-terminally processed|||N-acetylmethionine|||Phosphothreonine|||RING-type|||Removed; alternate|||Strong reduction in ligase activity; when associated with A-53.|||Strong reduction in ligase activity; when associated with A-56.|||Strong reduction in ligase activity; when associated with A-75.|||Strong reduction in ligase activity; when associated with A-77.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056013|||http://purl.uniprot.org/annotation/PRO_0000423264
http://togogenome.org/gene/9606:CDC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL80|||http://purl.uniprot.org/uniprot/G5EA36|||http://purl.uniprot.org/uniprot/P30260                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to MCPH1.|||Cell division cycle protein 27 homolog|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||TPR|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106273|||http://purl.uniprot.org/annotation/VAR_014489|||http://purl.uniprot.org/annotation/VAR_035861|||http://purl.uniprot.org/annotation/VSP_047225
http://togogenome.org/gene/9606:ZNF490                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULM2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 490                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047613
http://togogenome.org/gene/9606:NTF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34130                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In GLC1O; also found in patients with normal pressure glaucoma; unknown pathological significance; impaired ligand-mediated TRKB signaling and reduced neurite outgrowth.|||In GLC1O; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Neurotrophin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019669|||http://purl.uniprot.org/annotation/PRO_0000019670|||http://purl.uniprot.org/annotation/VAR_063196|||http://purl.uniprot.org/annotation/VAR_063197|||http://purl.uniprot.org/annotation/VAR_063198|||http://purl.uniprot.org/annotation/VAR_063199|||http://purl.uniprot.org/annotation/VAR_063200|||http://purl.uniprot.org/annotation/VAR_063201|||http://purl.uniprot.org/annotation/VAR_063202|||http://purl.uniprot.org/annotation/VAR_063203|||http://purl.uniprot.org/annotation/VAR_063204|||http://purl.uniprot.org/annotation/VAR_063205|||http://purl.uniprot.org/annotation/VAR_063206|||http://purl.uniprot.org/annotation/VAR_063207|||http://purl.uniprot.org/annotation/VAR_063208|||http://purl.uniprot.org/annotation/VAR_063209
http://togogenome.org/gene/9606:BPTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QQK4|||http://purl.uniprot.org/uniprot/Q12830                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to histone H3K4me3.|||Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Bromo|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K4me3 binding|||In NEDDFL.|||In isoform 2.|||In isoform 4.|||Induces binding to histone H3K4me2.|||Interaction with KEAP1|||Interaction with MAZ|||N6-acetyllysine|||Nucleosome-remodeling factor subunit BPTF|||Omega-N-methylarginine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Strongly reduces binding to histone H3K4me3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087176|||http://purl.uniprot.org/annotation/VAR_080531|||http://purl.uniprot.org/annotation/VAR_080532|||http://purl.uniprot.org/annotation/VAR_080533|||http://purl.uniprot.org/annotation/VSP_020402|||http://purl.uniprot.org/annotation/VSP_020405
http://togogenome.org/gene/9606:LMLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR62|||http://purl.uniprot.org/uniprot/Q96KR4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Leishmanolysin-like peptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303076|||http://purl.uniprot.org/annotation/PRO_5002800981|||http://purl.uniprot.org/annotation/VAR_060158|||http://purl.uniprot.org/annotation/VSP_028002|||http://purl.uniprot.org/annotation/VSP_028003
http://togogenome.org/gene/9606:CPNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FN4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-2|||In isoform 2.|||Linker region|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144836|||http://purl.uniprot.org/annotation/VSP_055536
http://togogenome.org/gene/9606:CENPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H22                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere protein N|||Decreases the binding to centromeres.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249494|||http://purl.uniprot.org/annotation/VAR_027419|||http://purl.uniprot.org/annotation/VAR_048689|||http://purl.uniprot.org/annotation/VAR_048690|||http://purl.uniprot.org/annotation/VSP_020441|||http://purl.uniprot.org/annotation/VSP_020442|||http://purl.uniprot.org/annotation/VSP_044565|||http://purl.uniprot.org/annotation/VSP_044689|||http://purl.uniprot.org/annotation/VSP_044690
http://togogenome.org/gene/9606:TMEM131L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VDJ0|||http://purl.uniprot.org/uniprot/B3KU55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Required for Wnt-signaling inhibition and LRP6 degradation|||Transmembrane protein 131-like|||Transmembrane protein 131-like conserved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328865|||http://purl.uniprot.org/annotation/VAR_042551|||http://purl.uniprot.org/annotation/VAR_042552|||http://purl.uniprot.org/annotation/VAR_042553|||http://purl.uniprot.org/annotation/VAR_042554|||http://purl.uniprot.org/annotation/VAR_042555|||http://purl.uniprot.org/annotation/VSP_032826|||http://purl.uniprot.org/annotation/VSP_032827|||http://purl.uniprot.org/annotation/VSP_032828|||http://purl.uniprot.org/annotation/VSP_032829|||http://purl.uniprot.org/annotation/VSP_057633
http://togogenome.org/gene/9606:KCTD17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5Z5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||BTB|||BTB/POZ domain-containing protein KCTD17|||Disordered|||In DYT26; does not affect cytoplasmic subcellular location.|||In isoform 2.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247841|||http://purl.uniprot.org/annotation/VAR_027157|||http://purl.uniprot.org/annotation/VAR_073806|||http://purl.uniprot.org/annotation/VSP_020072
http://togogenome.org/gene/9606:MNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ70|||http://purl.uniprot.org/uniprot/Q8NEH6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In HTX9; the mutant protein is undetectable in respiratory cilia from an affected patient.|||Meiosis-specific nuclear structural protein 1|||Phosphotyrosine|||Trichohyalin-plectin-homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298921|||http://purl.uniprot.org/annotation/VAR_034737|||http://purl.uniprot.org/annotation/VAR_034738|||http://purl.uniprot.org/annotation/VAR_034739|||http://purl.uniprot.org/annotation/VAR_034740|||http://purl.uniprot.org/annotation/VAR_034741|||http://purl.uniprot.org/annotation/VAR_084460
http://togogenome.org/gene/9606:CIPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0C6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CLOCK-interacting pacemaker|||Disordered|||Loss of predominant localization in the nucleus; when associated with A-186. No effect on CAD- ANDHSPA5-binding; when associated with A-186.|||Loss of predominant localization in the nucleus; when associated with A-187. No effect on CAD- ANDHSPA5-binding; when associated with A-187.|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256133|||http://purl.uniprot.org/annotation/VAR_028881|||http://purl.uniprot.org/annotation/VAR_049526
http://togogenome.org/gene/9606:MLH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40692|||http://purl.uniprot.org/uniprot/Q59EG3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects binding to importins alpha, including KPNA2, hence may affect import to the nucleus.|||Associated with LYNCH2; no effect on MLH1 splicing.|||Associated with LYNCH2; results in partial MLH1 exon 10 skipping on ex vivo splicing assay; decreased mismatch repair activity.|||Basic and acidic residues|||Can be associated with HNPCC in some populations.|||DNA mismatch repair protein Mlh1|||DNA mismatch repair protein S5|||Disordered|||Found in an endometrial cancer sample; somatic mutation.|||In CRC.|||In CRC; sporadic; early onset.|||In CRC; sporadic; somatic mutation; unknown pathological significance.|||In CRC; sporadic; susceptibility to; ATPase function attenuated but not eliminated.|||In CRC; unknown pathological significance.|||In HNPCC; incomplete.|||In HNPCC; unknown pathological significance.|||In LYNCH2 and CRC; abrogates interaction with EXO1; no decrease in mismatch repair activity.|||In LYNCH2 and CRC; unknown pathological significance; no decrease in mismatch repair activity; no effect on nuclear localization.|||In LYNCH2 and MMRCS1; abrogates interaction with EXO1; loss of protein expression; loss of nuclear localization; no effect on MLH1 splicing.|||In LYNCH2.|||In LYNCH2; also found in an endometrial cancer sample; no effect on MLH1 splicing.|||In LYNCH2; also found in sporadic colorectal cancer.|||In LYNCH2; decreased mismatch repair activity.|||In LYNCH2; decreased mismatch repair activity; defective in interaction with PMS2 and EXO1; loss of protein expression; may lose nuclear localization.|||In LYNCH2; decreased mismatch repair activity; defective in interaction with PMS2.|||In LYNCH2; decreased mismatch repair activity; defective in interaction with PMS2; loss of protein expression; loss of nuclear localization.|||In LYNCH2; decreased mismatch repair activity; loss of interaction with PMS2 and EXO1; loss of protein expression; may lose nuclear localization.|||In LYNCH2; decreased mismatch repair activity; loss of nuclear localization.|||In LYNCH2; decreased mismatch repair activity; loss of nuclear localization; normal interaction with PMS2.|||In LYNCH2; decreased mismatch repair activity; loss of protein expression.|||In LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization.|||In LYNCH2; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization; no effect on MLH1 splicing.|||In LYNCH2; decreased mismatch repair activity; no effect on MLH1 splicing; fails to interact with PMS2 and EXO1; loss of nuclear localization.|||In LYNCH2; decreased mismatch repair activity; no effect on nuclear localization.|||In LYNCH2; decreased mismatch repair activity; normal interaction with PMS2; loss of protein expression; loss of nuclear localization.|||In LYNCH2; defective in interaction with PMS2 and EXO1; no decrease in mismatch repair activity.|||In LYNCH2; incomplete.|||In LYNCH2; interacts only very weakly with PMS2; abrogates interaction with EXO1; decreased mismatch repair activity; may lose nuclear localization.|||In LYNCH2; loss of nuclear localization.|||In LYNCH2; loss of protein expression; loss of nuclear localization.|||In LYNCH2; loss of protein expression; normal interaction with PMS2 and EXO1; decreased mismatch repair activity; no effect on nuclear localization.|||In LYNCH2; no decrease in mismatch repair activity.|||In LYNCH2; no effect on MLH1 splicing.|||In LYNCH2; no effect on MLH1 splicing; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization.|||In LYNCH2; no effect on MLH1 splicing; loss of mismatch repair activity.|||In LYNCH2; requires 2 nucleotide substitutions; decreased mismatch repair activity.|||In LYNCH2; results in partial MLH1 exon 10 skipping on ex vivo splicing assay; decreased mismatch repair activity; no effect on nuclear localization.|||In LYNCH2; results in weak MLH1 exon 11 skipping on ex vivo splicing assay; decreased mismatch repair activity; loss of protein expression; loss of nuclear localization.|||In LYNCH2; the protein is unstable; loss of nuclear localization; loss of protein expression; no decrease in mismatch repair activity.|||In LYNCH2; type I; abrogates interaction with EXO1.|||In LYNCH2; type II.|||In LYNCH2; type II; decreased mismatch repair activity.|||In LYNCH2; type II; loss of nuclear localization.|||In LYNCH2; unknown pathological significance.|||In LYNCH2; unknown pathological significance; acts functionally like the wild-type protein.|||In LYNCH2; unknown pathological significance; also found in lobular carcinoma in situ of the breast; no effect on MLH1 splicing.|||In LYNCH2; unknown pathological significance; defective in interaction with PMS2 and EXO1; may lose nuclear localization; loss of protein expression; no decrease in mismatch repair activity.|||In LYNCH2; unknown pathological significance; no decrease in mismatch repair activity.|||In LYNCH2; unknown pathological significance; no decrease in mismatch repair activity; no effect on nuclear localization.|||In LYNCH2; unknown pathological significance; no effect on MLH1 splicing.|||In LYNCH2; unknown pathological significance; no effect on nuclear localization; normal interaction with PMS2 and EXO1.|||In LYNCH2; unknown pathological significance; requires 2 nucleotide substitutions; interacts weakly with PMS2; no decrease in mismatch repair activity; no effect on nuclear localization.|||In MMRCS1; requires 2 nucleotide substitutions.|||In gastric cancer; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with EXO1|||N-acetylserine|||No decrease in mismatch repair activity; no effect on nuclear localization.|||No effect on MLH1 splicing.|||No effect on protein expression.|||Normal interaction with PMS2; no decrease in mismatch repair activity; no effect on nuclear localization.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Reduces by 60% protein expression.|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178000|||http://purl.uniprot.org/annotation/VAR_004433|||http://purl.uniprot.org/annotation/VAR_004434|||http://purl.uniprot.org/annotation/VAR_004435|||http://purl.uniprot.org/annotation/VAR_004436|||http://purl.uniprot.org/annotation/VAR_004437|||http://purl.uniprot.org/annotation/VAR_004438|||http://purl.uniprot.org/annotation/VAR_004439|||http://purl.uniprot.org/annotation/VAR_004440|||http://purl.uniprot.org/annotation/VAR_004441|||http://purl.uniprot.org/annotation/VAR_004442|||http://purl.uniprot.org/annotation/VAR_004443|||http://purl.uniprot.org/annotation/VAR_004444|||http://purl.uniprot.org/annotation/VAR_004445|||http://purl.uniprot.org/annotation/VAR_004446|||http://purl.uniprot.org/annotation/VAR_004447|||http://purl.uniprot.org/annotation/VAR_004448|||http://purl.uniprot.org/annotation/VAR_004449|||http://purl.uniprot.org/annotation/VAR_004450|||http://purl.uniprot.org/annotation/VAR_004451|||http://purl.uniprot.org/annotation/VAR_004452|||http://purl.uniprot.org/annotation/VAR_004453|||http://purl.uniprot.org/annotation/VAR_004454|||http://purl.uniprot.org/annotation/VAR_004455|||http://purl.uniprot.org/annotation/VAR_004456|||http://purl.uniprot.org/annotation/VAR_004457|||http://purl.uniprot.org/annotation/VAR_004458|||http://purl.uniprot.org/annotation/VAR_004459|||http://purl.uniprot.org/annotation/VAR_004460|||http://purl.uniprot.org/annotation/VAR_004461|||http://purl.uniprot.org/annotation/VAR_004462|||http://purl.uniprot.org/annotation/VAR_004463|||http://purl.uniprot.org/annotation/VAR_004464|||http://purl.uniprot.org/annotation/VAR_004465|||http://purl.uniprot.org/annotation/VAR_004466|||http://purl.uniprot.org/annotation/VAR_004467|||http://purl.uniprot.org/annotation/VAR_004468|||http://purl.uniprot.org/annotation/VAR_012902|||http://purl.uniprot.org/annotation/VAR_012903|||http://purl.uniprot.org/annotation/VAR_012904|||http://purl.uniprot.org/annotation/VAR_012905|||http://purl.uniprot.org/annotation/VAR_012906|||http://purl.uniprot.org/annotation/VAR_012907|||http://purl.uniprot.org/annotation/VAR_012908|||http://purl.uniprot.org/annotation/VAR_012909|||http://purl.uniprot.org/annotation/VAR_012910|||http://purl.uniprot.org/annotation/VAR_012911|||http://purl.uniprot.org/annotation/VAR_012912|||http://purl.uniprot.org/annotation/VAR_012913|||http://purl.uniprot.org/annotation/VAR_012914|||http://purl.uniprot.org/annotation/VAR_012915|||http://purl.uniprot.org/annotation/VAR_012916|||http://purl.uniprot.org/annotation/VAR_012917|||http://purl.uniprot.org/annotation/VAR_012918|||http://purl.uniprot.org/annotation/VAR_012919|||http://purl.uniprot.org/annotation/VAR_012920|||http://purl.uniprot.org/annotation/VAR_012921|||http://purl.uniprot.org/annotation/VAR_012922|||http://purl.uniprot.org/annotation/VAR_012923|||http://purl.uniprot.org/annotation/VAR_012924|||http://purl.uniprot.org/annotation/VAR_012925|||http://purl.uniprot.org/annotation/VAR_012926|||http://purl.uniprot.org/annotation/VAR_012927|||http://purl.uniprot.org/annotation/VAR_012928|||http://purl.uniprot.org/annotation/VAR_012929|||http://purl.uniprot.org/annotation/VAR_012930|||http://purl.uniprot.org/annotation/VAR_012931|||http://purl.uniprot.org/annotation/VAR_012932|||http://purl.uniprot.org/annotation/VAR_012933|||http://purl.uniprot.org/annotation/VAR_012934|||http://purl.uniprot.org/annotation/VAR_012935|||http://purl.uniprot.org/annotation/VAR_014876|||http://purl.uniprot.org/annotation/VAR_015689|||http://purl.uniprot.org/annotation/VAR_020469|||http://purl.uniprot.org/annotation/VAR_022663|||http://purl.uniprot.org/annotation/VAR_022664|||http://purl.uniprot.org/annotation/VAR_022665|||http://purl.uniprot.org/annotation/VAR_022666|||http://purl.uniprot.org/annotation/VAR_022667|||http://purl.uniprot.org/annotation/VAR_022668|||http://purl.uniprot.org/annotation/VAR_022669|||http://purl.uniprot.org/annotation/VAR_038023|||http://purl.uniprot.org/annotation/VAR_038024|||http://purl.uniprot.org/annotation/VAR_038025|||http://purl.uniprot.org/annotation/VAR_043383|||http://purl.uniprot.org/annotation/VAR_043384|||http://purl.uniprot.org/annotation/VAR_043385|||http://purl.uniprot.org/annotation/VAR_043386|||http://purl.uniprot.org/annotation/VAR_043387|||http://purl.uniprot.org/annotation/VAR_043388|||http://purl.uniprot.org/annotation/VAR_043389|||http://purl.uniprot.org/annotation/VAR_043390|||http://purl.uniprot.org/annotation/VAR_043391|||http://purl.uniprot.org/annotation/VAR_043392|||http://purl.uniprot.org/annotation/VAR_043393|||http://purl.uniprot.org/annotation/VAR_043394|||http://purl.uniprot.org/annotation/VAR_043395|||http://purl.uniprot.org/annotation/VAR_043396|||http://purl.uniprot.org/annotation/VAR_043397|||http://purl.uniprot.org/annotation/VAR_043398|||http://purl.uniprot.org/annotation/VAR_043399|||http://purl.uniprot.org/annotation/VAR_043400|||http://purl.uniprot.org/annotation/VAR_043401|||http://purl.uniprot.org/annotation/VAR_043402|||http://purl.uniprot.org/annotation/VAR_043403|||http://purl.uniprot.org/annotation/VAR_043404|||http://purl.uniprot.org/annotation/VAR_043405|||http://purl.uniprot.org/annotation/VAR_043406|||http://purl.uniprot.org/annotation/VAR_043407|||http://purl.uniprot.org/annotation/VAR_043408|||http://purl.uniprot.org/annotation/VAR_043409|||http://purl.uniprot.org/annotation/VAR_043410|||http://purl.uniprot.org/annotation/VAR_043411|||http://purl.uniprot.org/annotation/VAR_043412|||http://purl.uniprot.org/annotation/VAR_043413|||http://purl.uniprot.org/annotation/VAR_043414|||http://purl.uniprot.org/annotation/VAR_043415|||http://purl.uniprot.org/annotation/VAR_043416|||http://purl.uniprot.org/annotation/VAR_043417|||http://purl.uniprot.org/annotation/VAR_043418|||http://purl.uniprot.org/annotation/VAR_043419|||http://purl.uniprot.org/annotation/VAR_043420|||http://purl.uniprot.org/annotation/VAR_043421|||http://purl.uniprot.org/annotation/VAR_043422|||http://purl.uniprot.org/annotation/VAR_043423|||http://purl.uniprot.org/annotation/VAR_043424|||http://purl.uniprot.org/annotation/VAR_043425|||http://purl.uniprot.org/annotation/VAR_043426|||http://purl.uniprot.org/annotation/VAR_043427|||http://purl.uniprot.org/annotation/VAR_043428|||http://purl.uniprot.org/annotation/VAR_043429|||http://purl.uniprot.org/annotation/VAR_043430|||http://purl.uniprot.org/annotation/VAR_043431|||http://purl.uniprot.org/annotation/VAR_043432|||http://purl.uniprot.org/annotation/VAR_043433|||http://purl.uniprot.org/annotation/VAR_043434|||http://purl.uniprot.org/annotation/VAR_043435|||http://purl.uniprot.org/annotation/VAR_043436|||http://purl.uniprot.org/annotation/VAR_043437|||http://purl.uniprot.org/annotation/VAR_054522|||http://purl.uniprot.org/annotation/VAR_054523|||http://purl.uniprot.org/annotation/VAR_054524|||http://purl.uniprot.org/annotation/VAR_054525|||http://purl.uniprot.org/annotation/VAR_054526|||http://purl.uniprot.org/annotation/VAR_054527|||http://purl.uniprot.org/annotation/VAR_054528|||http://purl.uniprot.org/annotation/VAR_054529|||http://purl.uniprot.org/annotation/VAR_054530|||http://purl.uniprot.org/annotation/VAR_054531|||http://purl.uniprot.org/annotation/VAR_054532|||http://purl.uniprot.org/annotation/VAR_054533|||http://purl.uniprot.org/annotation/VAR_054534|||http://purl.uniprot.org/annotation/VAR_054535|||http://purl.uniprot.org/annotation/VAR_054536|||http://purl.uniprot.org/annotation/VAR_054537|||http://purl.uniprot.org/annotation/VAR_054538|||http://purl.uniprot.org/annotation/VAR_076338|||http://purl.uniprot.org/annotation/VAR_076339|||http://purl.uniprot.org/annotation/VAR_076340|||http://purl.uniprot.org/annotation/VAR_076341|||http://purl.uniprot.org/annotation/VAR_076342|||http://purl.uniprot.org/annotation/VAR_076343|||http://purl.uniprot.org/annotation/VAR_076344|||http://purl.uniprot.org/annotation/VAR_076345|||http://purl.uniprot.org/annotation/VAR_076346|||http://purl.uniprot.org/annotation/VAR_076347|||http://purl.uniprot.org/annotation/VAR_076348|||http://purl.uniprot.org/annotation/VAR_076349|||http://purl.uniprot.org/annotation/VAR_076350|||http://purl.uniprot.org/annotation/VAR_079812|||http://purl.uniprot.org/annotation/VAR_079813|||http://purl.uniprot.org/annotation/VAR_079814|||http://purl.uniprot.org/annotation/VAR_079815|||http://purl.uniprot.org/annotation/VAR_079816|||http://purl.uniprot.org/annotation/VSP_045201|||http://purl.uniprot.org/annotation/VSP_047023
http://togogenome.org/gene/9606:MAP4K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K602|||http://purl.uniprot.org/uniprot/B3KMM5|||http://purl.uniprot.org/uniprot/Q8IVH8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CNH|||Disordered|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of kinase activity and ability to activate JNK family.|||Mitogen-activated protein kinase kinase kinase kinase 3|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086277|||http://purl.uniprot.org/annotation/VAR_040743|||http://purl.uniprot.org/annotation/VAR_040744|||http://purl.uniprot.org/annotation/VAR_040745|||http://purl.uniprot.org/annotation/VSP_007052|||http://purl.uniprot.org/annotation/VSP_007053
http://togogenome.org/gene/9606:FBXO21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94952|||http://purl.uniprot.org/uniprot/Q4G104|||http://purl.uniprot.org/uniprot/Q8IUQ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 21|||Hemimethylated DNA-binding|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119903|||http://purl.uniprot.org/annotation/VAR_047919|||http://purl.uniprot.org/annotation/VSP_035975
http://togogenome.org/gene/9606:AP2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE8|||http://purl.uniprot.org/uniprot/P63010|||http://purl.uniprot.org/uniprot/Q96EL6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-2 complex subunit beta|||Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding.|||Beta-adaptin appendage C-terminal subdomain|||Clathrin adaptor alpha/beta/gamma-adaptin appendage Ig-like subdomain|||In isoform 2.|||In isoform 3.|||Interaction with ARRB1|||N-acetylthreonine|||N6-acetyllysine|||No effect on interaction with ARRB1.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Removed|||Strongly reduces interaction with ARRB1.|||Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding.|||Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding.|||Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding.|||Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding.|||Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B.|||Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193742|||http://purl.uniprot.org/annotation/VSP_011490|||http://purl.uniprot.org/annotation/VSP_047805
http://togogenome.org/gene/9606:SIRT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDV3|||http://purl.uniprot.org/uniprot/M0QXA0|||http://purl.uniprot.org/uniprot/M0R1N9|||http://purl.uniprot.org/uniprot/Q8N6T7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished NAD-dependent protein deacetylase, deacylase and mono-ADP-ribosyltransferase activities. Impaired ability to recognize and bind double-strand breaks (DSBs) sites.|||Abolished NAD-dependent protein deacetylase, defatty-acylase and mono-ADP-ribosyltransferase activities.|||Abolishes ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs).|||Deacetylase sirtuin-type|||Decreased acetylation level.|||Decreased ubiquitination.|||Disordered|||Does not affect ability to promote DNA repair.|||Does not affect acetylation level.|||Does not affect histone deacetylase activity.|||Does not affect the NAD-dependent protein defatty-acylase activity. Abolished NAD-dependent protein deacetylase and mono-ADP-ribosyltransferase activities.|||Does not affect the mono-ADP-ribosyltransferase activity. Abolished NAD-dependent protein deacetylase and defatty-acylase activities.|||Formation of an covalent adduct with nitro-fatty acid activators|||Found in a family presenting with four cases of perinatal lethality caused by severe neurodevelopmental and cardiac anomalies; abolished histone deacetylase activity; abolished protein demyristoylase activity; decreased ability to recognize and bind double-strand breaks (DSBs) sites; does not affect nuclear localization.|||Found in cervical cancer; somatic mutation; reduced histone deacetylase activity; slightly reduced the protein-lysine demyristoylase activity.|||Found in kidney cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity.|||Found in melanoma; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity.|||Found in non-small cell lung cancer; somatic mutation; does not affect ability to recognize and bind double-strand breaks (DSBs) sites; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity.|||Found in non-small cell lung cancer; somatic mutation; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity.|||Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin.|||Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; reduced histone deacetylase activity; does not affect the protein-lysine demyristoylase activity.|||Found in non-small cell lung cancer; somatic mutation; reduced localization to chromatin; strongly reduced histone deacetylase activity; strongly reduced the protein-lysine demyristoylase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with 296-R--R-300 and R-316.|||In 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with 296-R--R-300 and R-332.|||In 4KR mutant; abolished sumoylation, leading to increased H3K56ac; when associated with R-316 and R-332.|||In AAA mutant; strongly decreased nucleosome-binding; when associated with 206-A--A-208.|||In AAA mutant; strongly decreased nucleosome-binding; when associated with A-45.|||In isoform 2.|||Increased protein-lysine demyristoylase activity.|||Mimics acetylation, leading to impaired ability to recognize and bind double-strand breaks (DSBs) sites.|||Mimics phosphorylation; increased ability to promote DNA repair and recruit PARP1 to double-strand breaks (DSBs).|||N-acetylserine|||N6-acetyllysine|||NAD-dependent protein deacylase sirtuin-6|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine|||Proton acceptor|||Reduced MDL-800 and MDL-801 compounds-binding.|||Removed|||Slightly reduced MDL-800 and MDL-801 compounds-binding.|||Strongly reduced MDL-800 and MDL-801 compounds-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110269|||http://purl.uniprot.org/annotation/VAR_017154|||http://purl.uniprot.org/annotation/VAR_086083|||http://purl.uniprot.org/annotation/VAR_086084|||http://purl.uniprot.org/annotation/VAR_086085|||http://purl.uniprot.org/annotation/VAR_086086|||http://purl.uniprot.org/annotation/VAR_086087|||http://purl.uniprot.org/annotation/VAR_086088|||http://purl.uniprot.org/annotation/VAR_086089|||http://purl.uniprot.org/annotation/VAR_086090|||http://purl.uniprot.org/annotation/VAR_086091|||http://purl.uniprot.org/annotation/VSP_008733
http://togogenome.org/gene/9606:NEFH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12036                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||30 X 6 AA repeats of K-S-P-[AEPV]-[EAK]-[AEVK]|||4|||5|||6|||7|||8|||9|||Acidic residues|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Head|||IF rod|||In ALS.|||In isoform 2.|||Linker 1|||Linker 12|||Linker 2|||Neurofilament heavy polypeptide|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063800|||http://purl.uniprot.org/annotation/VAR_023063|||http://purl.uniprot.org/annotation/VAR_026163|||http://purl.uniprot.org/annotation/VAR_054787|||http://purl.uniprot.org/annotation/VAR_056025|||http://purl.uniprot.org/annotation/VSP_036706
http://togogenome.org/gene/9606:PHOX2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99453                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Confers susceptibility to neuroblastoma.|||Confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma family.|||Disordered|||Homeobox|||In CCHS1.|||Paired mesoderm homeobox protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049262|||http://purl.uniprot.org/annotation/VAR_018257|||http://purl.uniprot.org/annotation/VAR_018258|||http://purl.uniprot.org/annotation/VAR_018259|||http://purl.uniprot.org/annotation/VAR_026969|||http://purl.uniprot.org/annotation/VAR_026970|||http://purl.uniprot.org/annotation/VAR_046900|||http://purl.uniprot.org/annotation/VAR_046901|||http://purl.uniprot.org/annotation/VAR_046902
http://togogenome.org/gene/9606:LSMEM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N112                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Leucine-rich single-pass membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242663
http://togogenome.org/gene/9606:DCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5CTF3|||http://purl.uniprot.org/uniprot/P27707                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  4.5-fold increase in Km.|||Deoxycytidine kinase|||Deoxynucleoside kinase|||Phosphoserine|||Phosphoserine; by CK1|||Phosphothreonine; by CK1|||Proton acceptor|||Strongly increased catalytic efficiency towards deoxycytidine; when associated with M-104 and A-133.|||Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and A-133.|||Strongly increased catalytic efficiency towards deoxycytidine; when associated with V-100 and M-104. Strongly increased catalytic efficiency towards deoxythymidine; when associated with L-104.|||Strongly increased catalytic efficiency towards deoxythymidine; when associated with A-133.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175090
http://togogenome.org/gene/9606:UCHL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTB8|||http://purl.uniprot.org/uniprot/A0A140VJZ4|||http://purl.uniprot.org/uniprot/P15374                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity. Increased interaction with diubiquitin.|||Decreased interaction with diubiquitin. No accumulation of free diubiquitin. Decreased levels of polyubiquitinated lysozyme.|||Important for enzyme activity|||Increased interaction with diubiquitin.|||Interaction with ubiquitin|||Interaction with ubiquitin. Crossover loop which restricts access of large ubiquitin adducts to the active site|||Nucleophile|||Phosphoserine|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site|||Ubiquitin carboxyl-terminal hydrolase isozyme L3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211061
http://togogenome.org/gene/9606:CYB5RL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FAD-binding FR-type|||In isoform 2.|||In isoform 3.|||NADH-cytochrome b5 reductase-like|||Oxidoreductase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337041|||http://purl.uniprot.org/annotation/VAR_043577|||http://purl.uniprot.org/annotation/VSP_033845|||http://purl.uniprot.org/annotation/VSP_040404
http://togogenome.org/gene/9606:SLC25A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12236|||http://purl.uniprot.org/uniprot/Q6I9V5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP/ATP translocase 3|||ADP/ATP translocase 3, N-terminally processed|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important for transport activity|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylmethionine|||N-acetylthreonine; in ADP/ATP translocase 3, N-terminally processed|||N6,N6,N6-trimethyllysine|||N6-acetyllysine|||Nucleotide carrier signature motif|||Removed; alternate|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090584|||http://purl.uniprot.org/annotation/PRO_0000425781|||http://purl.uniprot.org/annotation/VAR_054819
http://togogenome.org/gene/9606:ARHGDIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52566                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Rho GDP-dissociation inhibitor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219016
http://togogenome.org/gene/9606:SPMIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N865                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Sperm-associated microtubule inner protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089587|||http://purl.uniprot.org/annotation/VAR_022781|||http://purl.uniprot.org/annotation/VAR_022782|||http://purl.uniprot.org/annotation/VAR_022783|||http://purl.uniprot.org/annotation/VAR_022784|||http://purl.uniprot.org/annotation/VAR_056809|||http://purl.uniprot.org/annotation/VAR_056810|||http://purl.uniprot.org/annotation/VAR_056811|||http://purl.uniprot.org/annotation/VAR_056812|||http://purl.uniprot.org/annotation/VAR_060608|||http://purl.uniprot.org/annotation/VAR_060609
http://togogenome.org/gene/9606:ANGPTL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43827                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Angiopoietin-related protein 7|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009131|||http://purl.uniprot.org/annotation/VAR_025075|||http://purl.uniprot.org/annotation/VAR_025076|||http://purl.uniprot.org/annotation/VAR_025077
http://togogenome.org/gene/9606:IQCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0W5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  IQ domain-containing protein K|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282574|||http://purl.uniprot.org/annotation/VAR_031416|||http://purl.uniprot.org/annotation/VSP_024204|||http://purl.uniprot.org/annotation/VSP_024205|||http://purl.uniprot.org/annotation/VSP_024206|||http://purl.uniprot.org/annotation/VSP_024207
http://togogenome.org/gene/9606:EME2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4GXA9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Probable crossover junction endonuclease EME2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317373|||http://purl.uniprot.org/annotation/VSP_030938|||http://purl.uniprot.org/annotation/VSP_030939
http://togogenome.org/gene/9606:ISG15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05161                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Does not affect ISG15 signaling, interaction with ITGAL or activation of SRC family tyrosine kinases.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Interacts with activating enzyme|||Interchain (with C-87 in UBE2N); alternate|||Involved in the ligation of specific target proteins|||LRLRGG|||Reduces ISG15 signaling. Strongly reduces ISG15 signaling and abolishes interaction with ITGAL and activation of SRC family tyrosine kinases; when associated with D-102.|||Reduces ISG15 signaling. Strongly reduces ISG15 signaling and abolishes interaction with ITGAL and activation of SRC family tyrosine kinases; when associated with L-96.|||Removed|||Removed in mature form|||S-nitrosocysteine; alternate|||Strongly reduces ISG15 signaling and abolishes interaction with ITGAL and activation of SRC family tyrosine kinases.|||Strongly reduces ISG15 signaling and abolishes interaction with ITGAL.|||Ubiquitin-like 1|||Ubiquitin-like 2|||Ubiquitin-like protein ISG15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035986|||http://purl.uniprot.org/annotation/PRO_0000035987|||http://purl.uniprot.org/annotation/VAR_016181
http://togogenome.org/gene/9606:TAS2R8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082227|||http://purl.uniprot.org/annotation/VAR_024186
http://togogenome.org/gene/9606:PSMB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20618                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NEDMHAL; unknown pathological significance; results in impaired proteasome assembly.|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit beta type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148030|||http://purl.uniprot.org/annotation/PRO_0000259623|||http://purl.uniprot.org/annotation/VAR_051547|||http://purl.uniprot.org/annotation/VAR_051548|||http://purl.uniprot.org/annotation/VAR_087692
http://togogenome.org/gene/9606:NCBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09161                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes nuclear localization and phosphorylation by RPS6KB1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MIF4G|||N6-acetyllysine|||Nuclear cap-binding protein subunit 1|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Phosphothreonine; by RPS6KB1|||Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22.|||Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089364
http://togogenome.org/gene/9606:TPBGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKB5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||N-linked (GlcNAc...) asparagine|||Trophoblast glycoprotein-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419456
http://togogenome.org/gene/9606:FBXO9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK97                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 9|||In isoform 2.|||In isoform 3.|||Phosphoserine|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119886|||http://purl.uniprot.org/annotation/VSP_012979|||http://purl.uniprot.org/annotation/VSP_012980
http://togogenome.org/gene/9606:CFAP95                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTT2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 95|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271063|||http://purl.uniprot.org/annotation/VSP_056887
http://togogenome.org/gene/9606:FAM3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DWX8|||http://purl.uniprot.org/uniprot/P98173|||http://purl.uniprot.org/uniprot/Q9BU27                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  GG-type lectin|||Helical|||ILEI/PANDER|||In isoform 2.|||In isoform 3.|||Protein FAM3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008748|||http://purl.uniprot.org/annotation/VAR_011923|||http://purl.uniprot.org/annotation/VAR_057531|||http://purl.uniprot.org/annotation/VSP_042778|||http://purl.uniprot.org/annotation/VSP_046733
http://togogenome.org/gene/9606:RNF212B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTL3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Polar residues|||RING finger protein 212B|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349181
http://togogenome.org/gene/9606:VPREB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W8C9|||http://purl.uniprot.org/uniprot/P12018                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Complementarity-determining-1|||Complementarity-determining-2|||Disordered|||Framework-1|||Framework-2|||Framework-3|||Ig-like|||Ig-like V-type|||Immunoglobulin iota chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015000|||http://purl.uniprot.org/annotation/VAR_024503|||http://purl.uniprot.org/annotation/VAR_029133|||http://purl.uniprot.org/annotation/VAR_029134
http://togogenome.org/gene/9606:FTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDR3|||http://purl.uniprot.org/uniprot/P02792                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Catalytic site for iron oxidation|||Ferritin light chain|||Ferritin-like diiron|||In HRFTC.|||In NBIA3.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201060|||http://purl.uniprot.org/annotation/VAR_026633|||http://purl.uniprot.org/annotation/VAR_070948
http://togogenome.org/gene/9606:KBTBD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ATG8 interaction motif (AIM)|||BTB|||Decreased interaction with GABARAP and GABARAPL2. Loss of function in TIAM1 ubiquitination and degradation. No effect on assembly of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex.|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch repeat and BTB domain-containing protein 6|||Loss of interaction with CUL3. Loss of function in TIAM1 ubiquitination and degradation.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119084
http://togogenome.org/gene/9606:CITED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTM3|||http://purl.uniprot.org/uniprot/D9ZGF1|||http://purl.uniprot.org/uniprot/Q99967                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cbp/p300-interacting transactivator 2|||Disordered|||In ASD8; demonstrates only about 75% of the repressive activity of wild-type.|||In VSD2; reduces coactivation of the TFAP2C gene to 50% of that obtained with wild-type and represses HIF1A with about 60% efficiency compared to wild-type.|||In isoform 2.|||Inhibits transactivation activity.|||Inhibits transactivation activity; when associated with E-243.|||Inhibits transactivation activity; when associated with E-246.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144726|||http://purl.uniprot.org/annotation/VAR_067583|||http://purl.uniprot.org/annotation/VAR_067584|||http://purl.uniprot.org/annotation/VAR_067585|||http://purl.uniprot.org/annotation/VSP_001089
http://togogenome.org/gene/9606:ZNF197                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14709|||http://purl.uniprot.org/uniprot/Q7Z6G1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||SCAN box|||Zinc finger protein 197                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047448|||http://purl.uniprot.org/annotation/VSP_043021|||http://purl.uniprot.org/annotation/VSP_043022
http://togogenome.org/gene/9606:NUDT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKK9                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-sugar pyrophosphatase|||Catalytic inactive mutant for both ADP-sugar pyrophosphatase and nuclear ATP-synthesis activities. Reduces catalytic rate 6300-fold.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation; generates ATP in the presence of diphosphate.|||N-acetylmethionine|||N6-acetyllysine|||Nudix box|||Nudix hydrolase|||Phosphomimetic mutant; unable to generate ATP in the presence of diphosphate.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces affinity for substrate about 15-fold and reduces catalytic rate about 17-fold.|||Reduces affinity for substrate about 5-fold and reduces catalytic rate 67-fold.|||Reduces affinity for substrate about 6-fold.|||Reduces affinity for substrate about 6-fold. Strongly reduced catalytic activity and strongly reduced affinity for substrate; when associated with A-28.|||Reduces affinity for substrate about 8-fold. Strongly reduced catalytic activity and strongly reduced affinity for substrate; when associated with A-46.|||Reduces catalytic rate 120-fold.|||Reduces catalytic rate 2000-fold.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057048|||http://purl.uniprot.org/annotation/VAR_034159
http://togogenome.org/gene/9606:CUL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7U0|||http://purl.uniprot.org/uniprot/B3KTW0|||http://purl.uniprot.org/uniprot/Q13616                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Cullin family profile|||Cullin-1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119787
http://togogenome.org/gene/9606:KRT83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78385                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||In MNLIX.|||Keratin, type II cuticular Hb3|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063699|||http://purl.uniprot.org/annotation/VAR_018119|||http://purl.uniprot.org/annotation/VAR_018120|||http://purl.uniprot.org/annotation/VAR_018121|||http://purl.uniprot.org/annotation/VAR_023052|||http://purl.uniprot.org/annotation/VAR_073049
http://togogenome.org/gene/9606:NUF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZD4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Interaction with the C-terminus of NDC80 and the SPBC24-SPBC25 subcomplex|||Interaction with the N-terminus of NDC80|||Kinetochore protein Nuf2|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249813|||http://purl.uniprot.org/annotation/VAR_027490|||http://purl.uniprot.org/annotation/VAR_027491
http://togogenome.org/gene/9606:ZNF804B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||Zinc finger protein 804B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289140|||http://purl.uniprot.org/annotation/VAR_054666|||http://purl.uniprot.org/annotation/VAR_054667|||http://purl.uniprot.org/annotation/VAR_054668|||http://purl.uniprot.org/annotation/VAR_054669|||http://purl.uniprot.org/annotation/VAR_059938|||http://purl.uniprot.org/annotation/VAR_061968|||http://purl.uniprot.org/annotation/VAR_061969
http://togogenome.org/gene/9606:ARRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ENA6|||http://purl.uniprot.org/uniprot/P32121|||http://purl.uniprot.org/uniprot/Q59EM5|||http://purl.uniprot.org/uniprot/Q68DZ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CHUK; when associated with A-11; A-12 and A-230.|||Abolishes interaction with CHUK; when associated with A-11; A-12 and A-231.|||Abolishes interaction with CHUK; when associated with A-11; A-230 and A-231.|||Abolishes interaction with CHUK; when associated with A-12; A-230 and A-231.|||Arrestin C-terminal-like|||Beta-arrestin-2|||Disordered|||Hydroxyproline; by PHD2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||Inhibits internalization of CXCR4; no effect on interaction with CXCR4.|||Interaction with AP2B1|||Interaction with TRAF6|||Loss of phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces interaction with CHUK; when associated with A-360.|||Reduces interaction with CHUK; when associated with A-382.|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205199|||http://purl.uniprot.org/annotation/VSP_008194|||http://purl.uniprot.org/annotation/VSP_008195|||http://purl.uniprot.org/annotation/VSP_044697
http://togogenome.org/gene/9606:PCDHAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||Polar residues|||Protocadherin alpha-C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003912|||http://purl.uniprot.org/annotation/VSP_000701|||http://purl.uniprot.org/annotation/VSP_000702
http://togogenome.org/gene/9606:ZNF682                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUX2|||http://purl.uniprot.org/uniprot/O95780                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 682                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234001|||http://purl.uniprot.org/annotation/VAR_052891|||http://purl.uniprot.org/annotation/VAR_052892|||http://purl.uniprot.org/annotation/VAR_052893|||http://purl.uniprot.org/annotation/VSP_018166|||http://purl.uniprot.org/annotation/VSP_044563
http://togogenome.org/gene/9606:FAM120C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W881|||http://purl.uniprot.org/uniprot/Q9NX05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Constitutive coactivator of PPAR-gamma-like protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Omega-N-methylarginine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221628|||http://purl.uniprot.org/annotation/VAR_047538|||http://purl.uniprot.org/annotation/VAR_062001|||http://purl.uniprot.org/annotation/VSP_010519|||http://purl.uniprot.org/annotation/VSP_010520
http://togogenome.org/gene/9606:MERTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12866                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Found in a patient with Leber congenital amaurosis.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In RP38.|||In a head & Neck squamous cell carcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase Mer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024443|||http://purl.uniprot.org/annotation/VAR_020285|||http://purl.uniprot.org/annotation/VAR_021039|||http://purl.uniprot.org/annotation/VAR_021040|||http://purl.uniprot.org/annotation/VAR_021041|||http://purl.uniprot.org/annotation/VAR_021042|||http://purl.uniprot.org/annotation/VAR_021043|||http://purl.uniprot.org/annotation/VAR_021044|||http://purl.uniprot.org/annotation/VAR_021045|||http://purl.uniprot.org/annotation/VAR_021046|||http://purl.uniprot.org/annotation/VAR_021047|||http://purl.uniprot.org/annotation/VAR_021048|||http://purl.uniprot.org/annotation/VAR_021049|||http://purl.uniprot.org/annotation/VAR_029237|||http://purl.uniprot.org/annotation/VAR_041741|||http://purl.uniprot.org/annotation/VAR_041742|||http://purl.uniprot.org/annotation/VAR_041743|||http://purl.uniprot.org/annotation/VAR_041744|||http://purl.uniprot.org/annotation/VAR_041745|||http://purl.uniprot.org/annotation/VAR_041746|||http://purl.uniprot.org/annotation/VAR_041747|||http://purl.uniprot.org/annotation/VAR_051698|||http://purl.uniprot.org/annotation/VAR_067194|||http://purl.uniprot.org/annotation/VAR_067195
http://togogenome.org/gene/9606:TAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5A6|||http://purl.uniprot.org/uniprot/B7Z7P4|||http://purl.uniprot.org/uniprot/Q03518|||http://purl.uniprot.org/uniprot/X5CKB3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||Antigen peptide transporter 1|||Basic and acidic residues|||Complete loss of interaction with TAPBP, resulting in impaired PLC assembly and antigen presentation.|||Cytoplasmic|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Impairs allosteric coupling of peptide transport to ATP hydrolysis, converting the unidirectional active pump into a passive bidirectional nucleotide-gated facilitator. Inactive in peptide transport when associated with 'A-638' of TAP2.|||In a lung cancer cell line deficient in MHC class I presentation.|||In allele TAP1*02:01, allele TAP1*03:01, allele TAP1*04:01 and allele TAP1*x.|||In allele TAP1*02:01, allele TAP1*04:01 and allele TAP1*x.|||In allele TAP1*04:01.|||In allele TAP1*x.|||In isoform 2.|||Inter-subunit salt bridge with TAPBP|||Lumenal|||Part of the peptide-binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093326|||http://purl.uniprot.org/annotation/VAR_000092|||http://purl.uniprot.org/annotation/VAR_000093|||http://purl.uniprot.org/annotation/VAR_013151|||http://purl.uniprot.org/annotation/VAR_013152|||http://purl.uniprot.org/annotation/VAR_013153|||http://purl.uniprot.org/annotation/VAR_013154|||http://purl.uniprot.org/annotation/VAR_013173|||http://purl.uniprot.org/annotation/VAR_016801|||http://purl.uniprot.org/annotation/VAR_016802|||http://purl.uniprot.org/annotation/VAR_016803|||http://purl.uniprot.org/annotation/VAR_047514|||http://purl.uniprot.org/annotation/VAR_048137|||http://purl.uniprot.org/annotation/VAR_048138|||http://purl.uniprot.org/annotation/VAR_060987|||http://purl.uniprot.org/annotation/VSP_061432
http://togogenome.org/gene/9606:SLC35F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXU6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Solute carrier family 35 member F2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307309|||http://purl.uniprot.org/annotation/VSP_028699|||http://purl.uniprot.org/annotation/VSP_028700|||http://purl.uniprot.org/annotation/VSP_028701
http://togogenome.org/gene/9606:ATP5MK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IX5                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  ATP synthase membrane subunit K, mitochondrial|||Helical|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231578
http://togogenome.org/gene/9606:NBPF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWK0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Neuroblastoma breakpoint family member 6|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288041|||http://purl.uniprot.org/annotation/VSP_053911
http://togogenome.org/gene/9606:C6orf226                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5I0X4                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C6orf226                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334680
http://togogenome.org/gene/9606:OR51E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVF8|||http://purl.uniprot.org/uniprot/Q8TCB6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150750|||http://purl.uniprot.org/annotation/VAR_034317|||http://purl.uniprot.org/annotation/VAR_057577
http://togogenome.org/gene/9606:GHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0H5|||http://purl.uniprot.org/uniprot/A0A087X162|||http://purl.uniprot.org/uniprot/P10912                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Benign variant.|||Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Found in a patient with idiopathic short stature; unknown pathological significance.|||Growth hormone receptor|||Growth hormone-binding protein|||Helical|||In GHIP.|||In LARS and GHIP.|||In LARS.|||In LARS; abolishes receptor homodimerization.|||In LARS; almost completely abolishes GH-binding at cell surface and in membrane fractions.|||In LARS; almost completely abolishes GH-binding at cell surface: 26% binding to membrane fractions.|||In LARS; almost completely abolishes GH-binding at cell surface: 53% binding to membrane fractions.|||In LARS; disrupts GH binding.|||In LARS; loss of ability to bind ligand.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No change in shedding activity: No change in hormone binding.|||Phosphoserine|||Required for ADAM17-mediated proteolysis|||Required for endocytosis and down-regulation|||UbE motif|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010957|||http://purl.uniprot.org/annotation/PRO_0000010958|||http://purl.uniprot.org/annotation/PRO_5001832168|||http://purl.uniprot.org/annotation/PRO_5001832170|||http://purl.uniprot.org/annotation/VAR_002708|||http://purl.uniprot.org/annotation/VAR_002709|||http://purl.uniprot.org/annotation/VAR_002710|||http://purl.uniprot.org/annotation/VAR_002711|||http://purl.uniprot.org/annotation/VAR_002712|||http://purl.uniprot.org/annotation/VAR_002713|||http://purl.uniprot.org/annotation/VAR_002714|||http://purl.uniprot.org/annotation/VAR_002715|||http://purl.uniprot.org/annotation/VAR_002716|||http://purl.uniprot.org/annotation/VAR_013937|||http://purl.uniprot.org/annotation/VAR_013938|||http://purl.uniprot.org/annotation/VAR_013939|||http://purl.uniprot.org/annotation/VAR_013940|||http://purl.uniprot.org/annotation/VAR_013941|||http://purl.uniprot.org/annotation/VAR_013942|||http://purl.uniprot.org/annotation/VAR_018426|||http://purl.uniprot.org/annotation/VAR_018427|||http://purl.uniprot.org/annotation/VAR_018428|||http://purl.uniprot.org/annotation/VAR_018429|||http://purl.uniprot.org/annotation/VAR_018430|||http://purl.uniprot.org/annotation/VAR_018431|||http://purl.uniprot.org/annotation/VAR_018432|||http://purl.uniprot.org/annotation/VAR_018433|||http://purl.uniprot.org/annotation/VAR_018434|||http://purl.uniprot.org/annotation/VAR_018435|||http://purl.uniprot.org/annotation/VAR_018436|||http://purl.uniprot.org/annotation/VAR_020002|||http://purl.uniprot.org/annotation/VAR_032704|||http://purl.uniprot.org/annotation/VSP_010225|||http://purl.uniprot.org/annotation/VSP_010226|||http://purl.uniprot.org/annotation/VSP_010227|||http://purl.uniprot.org/annotation/VSP_010228|||http://purl.uniprot.org/annotation/VSP_010229|||http://purl.uniprot.org/annotation/VSP_010230
http://togogenome.org/gene/9606:RBM34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42696                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RNA-binding protein 34|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081790|||http://purl.uniprot.org/annotation/VSP_037037|||http://purl.uniprot.org/annotation/VSP_037038
http://togogenome.org/gene/9606:CCDC170                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYT3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 170|||Required for binding to microtubules and Golgi apparatus location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255256|||http://purl.uniprot.org/annotation/VAR_028856|||http://purl.uniprot.org/annotation/VAR_028857|||http://purl.uniprot.org/annotation/VAR_028858|||http://purl.uniprot.org/annotation/VAR_028859|||http://purl.uniprot.org/annotation/VAR_028860|||http://purl.uniprot.org/annotation/VAR_050805|||http://purl.uniprot.org/annotation/VAR_050806|||http://purl.uniprot.org/annotation/VAR_061591
http://togogenome.org/gene/9606:ATG16L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RG0|||http://purl.uniprot.org/uniprot/Q53SV2|||http://purl.uniprot.org/uniprot/Q676U5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished non-canonical autophagy without affecting canonical autophagy.|||Abolished non-canonical autophagy without affecting canonical autophagy. Impaired conjugation of phosphatidylserine (PS) to LC3 proteins.|||Abolishes interaction with ATG5.|||Abolishes phosphorylation. Impairs interaction with ATG12-ATG5 complex.|||Autophagy-related protein 16|||Autophagy-related protein 16-1|||Caspase cleavage|||Impairs interaction with PPP1CA; when associated with A-540.|||Impairs interaction with PPP1CA; when associated with A-542.|||Impairs interaction with WIPI2.|||In FII mutant; abolished binding to membranes and lipidation to ATG8 family proteins.|||In IBD10; has no effect on the stability of the protein under normal conditions; enhances the cleavage and the degradation mediated by activated CASP3; results in reduced autophagy and defective clearance of intestinal pathogens; impairs interaction with TMEM59; slows TMEM59 intracellular trafficking; increases production of type IIFNs.|||In VRV mutant; abolished binding to membranes and lipidation to ATG8 family proteins.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Interaction with ATG5|||Phosphoserine|||Phosphoserine; by CK2|||Prevents cleavage by activated CASP3.|||RB1CC1-binding|||Reduces interaction with ATG5.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WIPI2-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050848|||http://purl.uniprot.org/annotation/VAR_021834|||http://purl.uniprot.org/annotation/VAR_053386|||http://purl.uniprot.org/annotation/VSP_013386|||http://purl.uniprot.org/annotation/VSP_013387|||http://purl.uniprot.org/annotation/VSP_013388|||http://purl.uniprot.org/annotation/VSP_013389|||http://purl.uniprot.org/annotation/VSP_013390
http://togogenome.org/gene/9606:SPATA31A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313020
http://togogenome.org/gene/9606:PROM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0N0M1|||http://purl.uniprot.org/uniprot/O43490                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In CORD12, STGD4 and MCDR2; affects the interaction with actin.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 5 and isoform 6.|||Loss of acetylation; when associated with Q-225 and Q-257.|||Loss of acetylation; when associated with Q-225 and Q-264.|||Loss of acetylation; when associated with Q-257 and Q-264.|||Loss of expression of the protein in part due to proteasomal degradation; when associated with Q-225 and Q-257.|||Loss of expression of the protein in part due to proteasomal degradation; when associated with Q-225 and Q-264.|||Loss of expression of the protein in part due to proteasomal degradation; when associated with Q-257 and Q-264.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Prominin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025813|||http://purl.uniprot.org/annotation/PRO_5001967430|||http://purl.uniprot.org/annotation/VAR_010382|||http://purl.uniprot.org/annotation/VAR_010383|||http://purl.uniprot.org/annotation/VAR_057961|||http://purl.uniprot.org/annotation/VSP_039069|||http://purl.uniprot.org/annotation/VSP_040000|||http://purl.uniprot.org/annotation/VSP_040001|||http://purl.uniprot.org/annotation/VSP_040002|||http://purl.uniprot.org/annotation/VSP_040003|||http://purl.uniprot.org/annotation/VSP_040004
http://togogenome.org/gene/9606:B4GALT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NY44|||http://purl.uniprot.org/uniprot/A8K5Z0|||http://purl.uniprot.org/uniprot/O60512                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 3|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080537|||http://purl.uniprot.org/annotation/VSP_014106|||http://purl.uniprot.org/annotation/VSP_014107
http://togogenome.org/gene/9606:HEBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRV9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Heme-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116897|||http://purl.uniprot.org/annotation/VAR_053363
http://togogenome.org/gene/9606:ACOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15067                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Cleavage|||In MITCH; gain-of-function; increased dimerization; increased protein levels and peroxisomal acyl-coenzyme A oxidase function; increased levels of reactive oxygen species; no effect on VLCFA levels; no effect on peroxisome location; causes Schwann cell death and myelination defects.|||In Pseudo-NALD; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In pseudo-NALD.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal acyl-CoA oxidase 1, A chain|||Peroxisomal acyl-CoA oxidase 1, B chain|||Peroxisomal acyl-CoA oxidase 1, C chain|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204677|||http://purl.uniprot.org/annotation/PRO_0000447500|||http://purl.uniprot.org/annotation/PRO_0000447501|||http://purl.uniprot.org/annotation/VAR_021529|||http://purl.uniprot.org/annotation/VAR_025789|||http://purl.uniprot.org/annotation/VAR_025790|||http://purl.uniprot.org/annotation/VAR_030619|||http://purl.uniprot.org/annotation/VAR_048182|||http://purl.uniprot.org/annotation/VAR_067040|||http://purl.uniprot.org/annotation/VAR_067041|||http://purl.uniprot.org/annotation/VAR_067042|||http://purl.uniprot.org/annotation/VAR_067043|||http://purl.uniprot.org/annotation/VAR_067044|||http://purl.uniprot.org/annotation/VAR_083893|||http://purl.uniprot.org/annotation/VAR_085887|||http://purl.uniprot.org/annotation/VSP_000146|||http://purl.uniprot.org/annotation/VSP_046129
http://togogenome.org/gene/9606:HNRNPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with HOXB-AS3 peptide; when associated with A-218 and A-225.|||Abolishes interaction with HOXB-AS3 peptide; when associated with A-218 and A-232.|||Abolishes interaction with HOXB-AS3 peptide; when associated with A-225 and A-232.|||Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Globular A domain|||Globular B domain|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein A1|||Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed|||In ALS20.|||In ALS20; increases subcellular localization of HNRNPA1 in cytoplasmic inclusions with stress granules.|||In ALS20; unknown pathological significance.|||In IBMPFD3; reduces binding to UBQLN2.|||In isoform 2.|||In isoform A1-A.|||N-acetylmethionine|||N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed|||N6-acetyllysine; alternate|||No nuclear import nor export.|||Normal nuclear import and export.|||Nuclear targeting sequence (M9)|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MKNK2|||Polar residues|||RNA-binding RGG-box|||RRM 1|||RRM 2|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081828|||http://purl.uniprot.org/annotation/PRO_0000424509|||http://purl.uniprot.org/annotation/VAR_070588|||http://purl.uniprot.org/annotation/VAR_070589|||http://purl.uniprot.org/annotation/VAR_070590|||http://purl.uniprot.org/annotation/VAR_077531|||http://purl.uniprot.org/annotation/VAR_077532|||http://purl.uniprot.org/annotation/VAR_077533|||http://purl.uniprot.org/annotation/VSP_005824|||http://purl.uniprot.org/annotation/VSP_034076
http://togogenome.org/gene/9606:DMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14565                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to ssDNA or dsDNA.|||Abolishes binding to ssDNA.|||Decreases octamer stability.|||In isoform 2.|||Meiotic recombination protein DMC1/LIM15 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122918|||http://purl.uniprot.org/annotation/VAR_018960|||http://purl.uniprot.org/annotation/VAR_061757|||http://purl.uniprot.org/annotation/VSP_055357
http://togogenome.org/gene/9606:ZBED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96006                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes autosumoylation.|||Abolishes homodimerization and nuclear localization. Abolishes homodimerization, multimerization, nuclear localization, and DNA binding activity; when associated with A-604-A-A-605. Abolishes interaction with SUMO1 and reduces sumoylation of CHD3/Mi2-alpha; when associated with 604-A-A-605.|||Abolishes homodimerization, multimerization, interaction with KPNB1, nuclear localization and DNA binding activity. Abolishes interaction with SUMO1 and reduces SUMOylation of CHD3/Mi2-alpha.|||Abolishes interaction with SUMO1.|||Abolishes nuclear localization, however has no effect on homodimerization; when associated with A-530-A-A-531.|||Abolishes nuclear localization, however has no effect on homodimerization; when associated with A-534.|||BED-type|||E3 SUMO-protein ligase ZBED1|||No effect on homodimerization or nuclear localization.|||Nuclear localization signal|||Reduces homodimerization and nuclear localization. Abolishes homodimerization, multimerization, nuclear localization, and DNA binding activity; when associated with A-600-A-A-601. Abolishes interaction with SUMO1 and reduces sumoylation of CHD3/Mi2-alpha; when associated with A-600-A-A-601.|||Required for DNA binding|||Required for interaction with human adenovirus early E1A protein|||Required for nuclear localization and homodimerization|||Required for the formation of higher order complexes of ZBED1 with consensus DNA binding sequences                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066560
http://togogenome.org/gene/9606:EXO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5H6|||http://purl.uniprot.org/uniprot/Q9UQ84                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also enhances DNA-binding to 5'-overhanging flap structures.|||Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also reduces DNA-binding to 5'-overhanging flap structures.|||Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. No effect on DNA-binding to 5'-overhanging flap structures.|||Abrogates exonuclease activity.|||Basic and acidic residues|||Complete loss of nuclear localization.|||Disordered|||Exonuclease 1|||I-domain|||In isoform 2.|||Interaction with MLH1|||Interaction with MSH2|||Interaction with MSH3|||May be associated with a reduced risk of colorectal cancer.|||May be associated with an increased risk of colorectal cancer.|||N-domain|||N6-acetyllysine|||No rescue of HU-induced degradation and loss of HU-induced increase of phosphorylation. No rescue of HU-induced degradation; when associated with A-621. No rescue of HU-induced degradation; when associated with A-454. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-621.|||No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-714.|||No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-621 and A-714.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by ATR|||Phosphothreonine|||Polar residues|||Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770.|||Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with S-640 or E-759.|||XPG N-terminal|||XPG-I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154039|||http://purl.uniprot.org/annotation/VAR_024966|||http://purl.uniprot.org/annotation/VAR_024967|||http://purl.uniprot.org/annotation/VAR_024968|||http://purl.uniprot.org/annotation/VAR_024969|||http://purl.uniprot.org/annotation/VAR_024970|||http://purl.uniprot.org/annotation/VAR_024971|||http://purl.uniprot.org/annotation/VAR_024972|||http://purl.uniprot.org/annotation/VAR_024973|||http://purl.uniprot.org/annotation/VAR_024974|||http://purl.uniprot.org/annotation/VAR_024975|||http://purl.uniprot.org/annotation/VAR_024976|||http://purl.uniprot.org/annotation/VAR_024977|||http://purl.uniprot.org/annotation/VAR_024978|||http://purl.uniprot.org/annotation/VAR_024979|||http://purl.uniprot.org/annotation/VAR_024980|||http://purl.uniprot.org/annotation/VAR_024981|||http://purl.uniprot.org/annotation/VAR_024982|||http://purl.uniprot.org/annotation/VAR_024983|||http://purl.uniprot.org/annotation/VAR_024984|||http://purl.uniprot.org/annotation/VAR_024985|||http://purl.uniprot.org/annotation/VAR_024986|||http://purl.uniprot.org/annotation/VAR_024987|||http://purl.uniprot.org/annotation/VAR_024988|||http://purl.uniprot.org/annotation/VAR_024989|||http://purl.uniprot.org/annotation/VAR_024990|||http://purl.uniprot.org/annotation/VAR_024991|||http://purl.uniprot.org/annotation/VAR_024992|||http://purl.uniprot.org/annotation/VAR_024993|||http://purl.uniprot.org/annotation/VAR_077352|||http://purl.uniprot.org/annotation/VSP_017029|||http://purl.uniprot.org/annotation/VSP_017030
http://togogenome.org/gene/9606:RANBP17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q546R4|||http://purl.uniprot.org/uniprot/Q8IVM9|||http://purl.uniprot.org/uniprot/Q9H2T7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Importin N-terminal|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Ran-binding protein 17|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204718|||http://purl.uniprot.org/annotation/VSP_056669|||http://purl.uniprot.org/annotation/VSP_056670
http://togogenome.org/gene/9606:OR4A15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4A15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150525|||http://purl.uniprot.org/annotation/VAR_055053|||http://purl.uniprot.org/annotation/VAR_055054
http://togogenome.org/gene/9606:USP46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62068                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080674|||http://purl.uniprot.org/annotation/VAR_051540|||http://purl.uniprot.org/annotation/VSP_037618|||http://purl.uniprot.org/annotation/VSP_037619|||http://purl.uniprot.org/annotation/VSP_037620|||http://purl.uniprot.org/annotation/VSP_037621
http://togogenome.org/gene/9606:ONECUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||CUT|||Disordered|||Hepatocyte nuclear factor 6|||Homeobox|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202402|||http://purl.uniprot.org/annotation/VAR_010729
http://togogenome.org/gene/9606:TXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99757                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Contributes to redox potential value|||Deprotonates C-terminal active site Cys|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Nucleophile|||Redox-active|||Thioredoxin|||Thioredoxin, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034150
http://togogenome.org/gene/9606:CSNK2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P67870                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Casein kinase II subunit beta|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In POBINDS.|||In POBINDS; associated in cis with C-86.|||In POBINDS; unknown pathological significance; associated in cis with 5-E--R-215 del.|||Interaction with alpha subunit|||KSSR motif|||N-acetylserine|||N6-acetyllysine; alternate|||No effect on interaction alpha subunit CSNK2A1. Loss on interaction with ARK2N and Epstein-Barr virus EBNA1.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068236|||http://purl.uniprot.org/annotation/VAR_083650|||http://purl.uniprot.org/annotation/VAR_083651|||http://purl.uniprot.org/annotation/VAR_083652|||http://purl.uniprot.org/annotation/VAR_083653|||http://purl.uniprot.org/annotation/VAR_083654|||http://purl.uniprot.org/annotation/VAR_083655
http://togogenome.org/gene/9606:ARG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05089                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Arginase-1|||In ARGIN.|||In ARGIN; 12% of wild-type activity.|||In ARGIN; 20.8% of wild-type activity.|||In ARGIN; 5.2% of wild-type activity.|||In ARGIN; 9.3% of wild-type activity.|||In ARGIN; decreases erythrocyte arginase activity.|||In isoform 2.|||In isoform 3.|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173693|||http://purl.uniprot.org/annotation/VAR_000674|||http://purl.uniprot.org/annotation/VAR_000675|||http://purl.uniprot.org/annotation/VAR_015594|||http://purl.uniprot.org/annotation/VAR_015595|||http://purl.uniprot.org/annotation/VAR_072164|||http://purl.uniprot.org/annotation/VAR_072165|||http://purl.uniprot.org/annotation/VAR_072166|||http://purl.uniprot.org/annotation/VAR_072167|||http://purl.uniprot.org/annotation/VAR_072168|||http://purl.uniprot.org/annotation/VAR_072169|||http://purl.uniprot.org/annotation/VSP_009330|||http://purl.uniprot.org/annotation/VSP_009331
http://togogenome.org/gene/9606:KAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92993                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates sumoylation.|||Abrogates sumoylation. Abolished sumoylation by PIAS4, promoting interaction with PRKDC, leading to decreased repair of DNA double-strand breaks (DSBs) via homologous recombination (HR).|||C2HC MYST-type|||Decreased autoacetylation; leading to decreased acetyltransferase activity and ability to acetylate FOXP3.|||Disordered|||Does not affect phosphorylation; when associated with A-254.|||Does not affect phosphorylation; when associated with A-257.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone acetyltransferase KAT5|||Impaired acetylation, leading to reduced histone acetyltransferase activity. In K6R; abolished autoacetylation; when associated with R-120, R-148, R-150, R-187 and R-189.|||In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-150 and R-187.|||In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-150 and R-189.|||In K6R; abolished autoacetylation; when associated with R-104, R-120, R-148, R-187 and R-189.|||In K6R; abolished autoacetylation; when associated with R-104, R-120, R-150, R-187 and R-189.|||In K6R; abolished autoacetylation; when associated with R-104, R-148, R-150, R-187 and R-189.|||In KAT5(QG/EE) mutant; abolished acetyltransferase activity. Impaired ability to activate CGAS.|||In NEDFASB; decreased histone acetyltransferase activity.|||In isoform 1 and isoform 4.|||In isoform 3 and isoform 4.|||Interaction with ATF2|||Loss of function. Does not affect phosphorylation.|||MYST-type HAT|||Mimics acetylation; promoting interaction with FOXP3 and subsequent acetylation.|||Mimics phosphorylation, promoting protein acetyltransferase activity.|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Phosphoserine; by CDK1 and CDK9|||Phosphoserine; by GSK3|||Proton donor/acceptor|||Reduced phosphorylation, leading to reduced protein acetyltransferase activity. Abolishes phosphorylation; when associated with A-86. Reduced histone acetyltransferase activity. Abolished phosphorylation by GSK3 at S-86.|||Reduced phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced histone acetyltransferase activity. Abolished phosphorylation by GSK3 and decreased acetyltransferase activity.|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051580|||http://purl.uniprot.org/annotation/VAR_059456|||http://purl.uniprot.org/annotation/VAR_085192|||http://purl.uniprot.org/annotation/VAR_085193|||http://purl.uniprot.org/annotation/VAR_085194|||http://purl.uniprot.org/annotation/VSP_007438|||http://purl.uniprot.org/annotation/VSP_009104
http://togogenome.org/gene/9606:ZNF479                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 479                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047606
http://togogenome.org/gene/9606:CD226                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QR77|||http://purl.uniprot.org/uniprot/Q15762                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD226 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014665|||http://purl.uniprot.org/annotation/VAR_018632
http://togogenome.org/gene/9606:NRAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01111                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL|||Abolished phosphorylation by STK19.|||Effector region|||GTPase NRas|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypervariable region|||In CMNS and NCMS; somatic mutation.|||In CMNS and colorectal cancer; somatic mutation.|||In CMNS, NCMS, KNEN and NMTC2; also found in lung carcinoma cell and melanoma; impaired GTP hydrolysis activity, trapping NRAS in a constitutive GTP-bound active conformation; promotes melanomagenesis.|||In KNEN and JMML.|||In KNEN.|||In N-Ras-2KR mutant; decreased fatty-acylation.|||In NS6; hypermorphic mutation.|||In RALD and JMML.|||In leukemia.|||Loss of GTP-binding activity.|||Loss of plasma membrane localization.|||Phosphoserine; by STK19|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043006|||http://purl.uniprot.org/annotation/PRO_0000043007|||http://purl.uniprot.org/annotation/VAR_006845|||http://purl.uniprot.org/annotation/VAR_006846|||http://purl.uniprot.org/annotation/VAR_006847|||http://purl.uniprot.org/annotation/VAR_021194|||http://purl.uniprot.org/annotation/VAR_063084|||http://purl.uniprot.org/annotation/VAR_063085|||http://purl.uniprot.org/annotation/VAR_063086|||http://purl.uniprot.org/annotation/VAR_071129|||http://purl.uniprot.org/annotation/VAR_071130
http://togogenome.org/gene/9606:SEMA3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS98                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257791|||http://purl.uniprot.org/annotation/VAR_030292|||http://purl.uniprot.org/annotation/VAR_051929|||http://purl.uniprot.org/annotation/VAR_051930
http://togogenome.org/gene/9606:BAIAP2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHR4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Binds F-actin|||Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1|||Disordered|||IMD|||Loss ability to induce the formation of actin clusters; induce the formation of long filopodia.|||Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146.|||Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145.|||Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146.|||Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146.|||Phosphoserine|||Phosphothreonine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247854|||http://purl.uniprot.org/annotation/VAR_033515
http://togogenome.org/gene/9606:SH3YL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||Polar residues|||SH3|||SH3 domain-containing YSC84-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341560|||http://purl.uniprot.org/annotation/VSP_034332|||http://purl.uniprot.org/annotation/VSP_034333|||http://purl.uniprot.org/annotation/VSP_034334|||http://purl.uniprot.org/annotation/VSP_034335
http://togogenome.org/gene/9606:RPS6KA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK32                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2.|||No effect on activity.|||Phosphoserine|||Phosphothreonine|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-6|||Strongly decreases activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086209|||http://purl.uniprot.org/annotation/VAR_030670|||http://purl.uniprot.org/annotation/VAR_040637|||http://purl.uniprot.org/annotation/VAR_040638|||http://purl.uniprot.org/annotation/VSP_056181
http://togogenome.org/gene/9606:C19orf44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R2B3|||http://purl.uniprot.org/uniprot/Q9H6X5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DUF4614|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Uncharacterized protein C19orf44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291921|||http://purl.uniprot.org/annotation/VSP_026311
http://togogenome.org/gene/9606:GBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14549                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein GBX-1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048878|||http://purl.uniprot.org/annotation/VAR_049579
http://togogenome.org/gene/9606:PRUNE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TP1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DHH motif|||Disordered|||Essential for homodimerization|||Exopolyphosphatase PRUNE1|||In NMIHBA.|||In NMIHBA; loss of function in regulation of cell proliferation and migration; loss of function in neurogenesis; impaired regulation of microtubule polymerization; increased phosphatase activity; decreased interaction with tubulin beta.|||In NMIHBA; loss of function in regulation of cell proliferation and migration; loss of function in neurogenesis; impaired regulation of microtubule polymerization; increased phosphatase activity; no effect on interaction with tubulin beta.|||In NMIHBA; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 6 and isoform 7.|||N-acetylmethionine|||No change in cAMPPDE activity. Partial loss of cAMPPDE activity; when associated with D-28. Partial loss of cAMPPDE activity; when associated with D-28 and D-179.|||Partial loss of cAMPPDE activity.|||Partial loss of cAMPPDE activity. Partial loss of cAMPPDE activity; when associated with D-106. Partial loss of cAMPPDE activity; when associated with D-106 and D-179.|||Partial loss of cAMPPDE activity. Partial loss of cAMPPDE activity; when associated with D-28 and D-106.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337987|||http://purl.uniprot.org/annotation/VAR_043728|||http://purl.uniprot.org/annotation/VAR_059559|||http://purl.uniprot.org/annotation/VAR_078986|||http://purl.uniprot.org/annotation/VAR_078987|||http://purl.uniprot.org/annotation/VAR_078988|||http://purl.uniprot.org/annotation/VAR_078989|||http://purl.uniprot.org/annotation/VAR_078990|||http://purl.uniprot.org/annotation/VAR_078991|||http://purl.uniprot.org/annotation/VSP_034013|||http://purl.uniprot.org/annotation/VSP_034014|||http://purl.uniprot.org/annotation/VSP_034015|||http://purl.uniprot.org/annotation/VSP_034016|||http://purl.uniprot.org/annotation/VSP_034017
http://togogenome.org/gene/9606:PRR23D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PI22|||http://purl.uniprot.org/uniprot/P0DMB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Proline-rich protein 23D1|||Proline-rich protein 23D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425121|||http://purl.uniprot.org/annotation/PRO_0000425122
http://togogenome.org/gene/9606:MRPS22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82650                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In COXPD5.|||In ODG7; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Small ribosomal subunit protein mS22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087703|||http://purl.uniprot.org/annotation/VAR_042733|||http://purl.uniprot.org/annotation/VAR_081186|||http://purl.uniprot.org/annotation/VAR_081187|||http://purl.uniprot.org/annotation/VSP_056634|||http://purl.uniprot.org/annotation/VSP_056635|||http://purl.uniprot.org/annotation/VSP_056636
http://togogenome.org/gene/9606:HELT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFD8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Hairy and enhancer of split-related protein HELT|||In isoform 2.|||N6-acetyllysine|||Orange|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349378|||http://purl.uniprot.org/annotation/VAR_049540|||http://purl.uniprot.org/annotation/VSP_056737
http://togogenome.org/gene/9606:GPR25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00155                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Probable G-protein coupled receptor 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069544
http://togogenome.org/gene/9606:RINL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS11                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Ras and Rab interactor-like protein|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318973|||http://purl.uniprot.org/annotation/VAR_038926|||http://purl.uniprot.org/annotation/VSP_046909
http://togogenome.org/gene/9606:DGKE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4Q0|||http://purl.uniprot.org/uniprot/P52429                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  DAGKc|||Decreased diacylglycerol kinase activity toward 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol.|||Decreased protein abundance and diacylglycerol kinase activity toward 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol.|||Diacylglycerol kinase epsilon|||Helical|||In AHUS7.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of diacylglycerol kinase activity toward 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218464|||http://purl.uniprot.org/annotation/VAR_036120|||http://purl.uniprot.org/annotation/VAR_069804|||http://purl.uniprot.org/annotation/VAR_069805|||http://purl.uniprot.org/annotation/VSP_056957|||http://purl.uniprot.org/annotation/VSP_056958
http://togogenome.org/gene/9606:WTAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1R4|||http://purl.uniprot.org/uniprot/Q15007                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA-splicing regulator WTAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065983|||http://purl.uniprot.org/annotation/VAR_036854|||http://purl.uniprot.org/annotation/VSP_010278|||http://purl.uniprot.org/annotation/VSP_010279
http://togogenome.org/gene/9606:EMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54852                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Epithelial membrane protein 3|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164660|||http://purl.uniprot.org/annotation/VAR_050609
http://togogenome.org/gene/9606:ZNF600                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IT03|||http://purl.uniprot.org/uniprot/Q6ZNG1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 600                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234593|||http://purl.uniprot.org/annotation/VAR_057427|||http://purl.uniprot.org/annotation/VAR_059925|||http://purl.uniprot.org/annotation/VAR_059926
http://togogenome.org/gene/9606:CARNMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4J0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Carnosine N-methyltransferase|||Disordered|||Impairs N-methyltransferase activity.|||Impairs binding to S-adenosyl-L-methionine. Significantly reduces N-methyltransferase activity.|||Reduces N-methyltransferase activity.|||Significantly reduces N-methyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089685
http://togogenome.org/gene/9606:CLEC4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXI8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member D|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||No effect on already low affinity binding to trehalose-6,6'-dimycolate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046616|||http://purl.uniprot.org/annotation/VAR_021261
http://togogenome.org/gene/9606:OR10G8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVX3|||http://purl.uniprot.org/uniprot/Q8NGN5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10G8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150700
http://togogenome.org/gene/9606:KLK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHX9|||http://purl.uniprot.org/uniprot/P49862                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 2.|||Kallikrein-7|||Major binding site for inhibitory zinc or copper|||N-linked (GlcNAc...) asparagine|||No effect on zinc inhibition.|||No zinc inhibition.|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027942|||http://purl.uniprot.org/annotation/PRO_0000027943|||http://purl.uniprot.org/annotation/VSP_013581
http://togogenome.org/gene/9606:ESRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6T0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Epithelial splicing regulatory protein 2|||In isoform 2.|||Phosphoserine|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273050|||http://purl.uniprot.org/annotation/VAR_030074|||http://purl.uniprot.org/annotation/VAR_030075|||http://purl.uniprot.org/annotation/VAR_057245|||http://purl.uniprot.org/annotation/VSP_022474
http://togogenome.org/gene/9606:ZNF878                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JN71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 878                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393952
http://togogenome.org/gene/9606:MYCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PPD9|||http://purl.uniprot.org/uniprot/P04198|||http://purl.uniprot.org/uniprot/Q9H224                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Abrogates the interaction with AURKA.|||Acidic residues|||BHLH|||Basic and acidic residues|||Disordered|||Does not affect AURKA binding.|||In FGLDS1.|||Interaction with AURKA|||Interaction with AURKA and FBXW7|||Leucine-zipper|||N-myc proto-oncogene protein|||Phosphoserine; by CK2|||Reduces binding to AURKA.|||Reduces interaction with AURKA; when associated with A-28.|||Reduces interaction with AURKA; when associated with A-29.|||Reduces interaction with AURKA; when associated with A-35.|||Reduces interaction with AURKA; when associated with A-36.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127323|||http://purl.uniprot.org/annotation/VAR_031952|||http://purl.uniprot.org/annotation/VAR_031953|||http://purl.uniprot.org/annotation/VAR_031954
http://togogenome.org/gene/9606:OCSTAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR26                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Osteoclast stimulatory transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342121|||http://purl.uniprot.org/annotation/VAR_050919
http://togogenome.org/gene/9606:IRX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78414                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||Iroquois-class homeodomain protein IRX-1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049151
http://togogenome.org/gene/9606:PF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02776                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Phosphoserine|||Platelet factor 4|||Platelet factor 4, short form|||Short form.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005068|||http://purl.uniprot.org/annotation/PRO_0000351217
http://togogenome.org/gene/9606:MAP3K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13233                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In SRXY6.|||In SRXY6; increases phosphorylation of the downstream target MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex.|||In SRXY6; increases phosphorylation of the downstream targets MAPK14 and MAPK3/MAPK1 compared to wild-type and enhances binding of RHOA to the mutant MAP3K1 complex.|||In SRXY6; unknown pathological significance.|||Mitogen-activated protein kinase kinase kinase 1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RING-type|||Removed|||SWIM-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086240|||http://purl.uniprot.org/annotation/VAR_040680|||http://purl.uniprot.org/annotation/VAR_040681|||http://purl.uniprot.org/annotation/VAR_051636|||http://purl.uniprot.org/annotation/VAR_051637|||http://purl.uniprot.org/annotation/VAR_065504|||http://purl.uniprot.org/annotation/VAR_065505|||http://purl.uniprot.org/annotation/VAR_065506|||http://purl.uniprot.org/annotation/VAR_065507
http://togogenome.org/gene/9606:SYNPO2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H987                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Synaptopodin 2-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187675|||http://purl.uniprot.org/annotation/VAR_019671|||http://purl.uniprot.org/annotation/VAR_047065|||http://purl.uniprot.org/annotation/VAR_061835|||http://purl.uniprot.org/annotation/VSP_011495|||http://purl.uniprot.org/annotation/VSP_011496
http://togogenome.org/gene/9606:CKMT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12532                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cardiolipin-binding|||Creatine kinase U-type, mitochondrial|||In isoform 2.|||Mitochondrion|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016590|||http://purl.uniprot.org/annotation/VSP_038045
http://togogenome.org/gene/9606:TOMM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4H5                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial import receptor subunit TOM5 homolog|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230671|||http://purl.uniprot.org/annotation/VSP_046982|||http://purl.uniprot.org/annotation/VSP_046983
http://togogenome.org/gene/9606:ADORA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1F6|||http://purl.uniprot.org/uniprot/B3KVQ4|||http://purl.uniprot.org/uniprot/P29274|||http://purl.uniprot.org/uniprot/X5DNB4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adenosine receptor A2a|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068999|||http://purl.uniprot.org/annotation/VAR_003451|||http://purl.uniprot.org/annotation/VAR_011835|||http://purl.uniprot.org/annotation/VAR_011836
http://togogenome.org/gene/9606:GASK1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFP1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Abolishes proteolytic cleavage; when associated with 119-A-A-120.|||Abolishes proteolytic cleavage; when associated with A-437.|||Cleavage|||Disordered|||Golgi-associated kinase 1A|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301948|||http://purl.uniprot.org/annotation/PRO_0000446051|||http://purl.uniprot.org/annotation/PRO_0000446052|||http://purl.uniprot.org/annotation/VAR_063129|||http://purl.uniprot.org/annotation/VAR_063130
http://togogenome.org/gene/9606:MAPK8IP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYG2|||http://purl.uniprot.org/uniprot/B7ZMF3|||http://purl.uniprot.org/uniprot/E9PFH7|||http://purl.uniprot.org/uniprot/Q9UPT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 3|||Disordered|||In NEDBA.|||In NEDBA; affects axon development when expressed in a heterologous system.|||In NEDBA; unknown pathological significance.|||In isoform 2.|||Interaction with NTRK2|||JNK-binding domain (JBD); essential for its function in axon elongation|||Kinesin-binding domain (KBD); essential for its function in axon elongation|||Leucine zipper-like domain (LZ); essential for its function in axon elongation|||Phosphoserine|||Phosphoserine; by ROCK1|||Phosphothreonine; by MAPK|||Polar residues|||RH1|||RH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220633|||http://purl.uniprot.org/annotation/VAR_049667|||http://purl.uniprot.org/annotation/VAR_082608|||http://purl.uniprot.org/annotation/VAR_082609|||http://purl.uniprot.org/annotation/VAR_082610|||http://purl.uniprot.org/annotation/VAR_082611|||http://purl.uniprot.org/annotation/VAR_082612|||http://purl.uniprot.org/annotation/VAR_082613|||http://purl.uniprot.org/annotation/VAR_082614|||http://purl.uniprot.org/annotation/VAR_082615|||http://purl.uniprot.org/annotation/VSP_024430|||http://purl.uniprot.org/annotation/VSP_024431
http://togogenome.org/gene/9606:GOLGA6L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9W4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Golgin subfamily A member 6-like protein 2|||In isoform 1.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320246|||http://purl.uniprot.org/annotation/VAR_039173|||http://purl.uniprot.org/annotation/VAR_039174|||http://purl.uniprot.org/annotation/VAR_039175|||http://purl.uniprot.org/annotation/VAR_039176|||http://purl.uniprot.org/annotation/VAR_039177|||http://purl.uniprot.org/annotation/VSP_059650|||http://purl.uniprot.org/annotation/VSP_059651|||http://purl.uniprot.org/annotation/VSP_059652|||http://purl.uniprot.org/annotation/VSP_059653|||http://purl.uniprot.org/annotation/VSP_059654
http://togogenome.org/gene/9606:SAMD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NU1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1 and isoform 2.|||In isoform 1, isoform 4, isoform 5 and isoform 6.|||In isoform 2 and isoform 5.|||In isoform 4 and isoform 5.|||Phosphoserine|||Phosphothreonine|||SAM|||Sterile alpha motif domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279500|||http://purl.uniprot.org/annotation/VSP_053647|||http://purl.uniprot.org/annotation/VSP_053648|||http://purl.uniprot.org/annotation/VSP_053649|||http://purl.uniprot.org/annotation/VSP_053650
http://togogenome.org/gene/9606:BPNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX62                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase|||Helical|||In CDP-GPAPP.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289041|||http://purl.uniprot.org/annotation/VAR_065847|||http://purl.uniprot.org/annotation/VAR_065848
http://togogenome.org/gene/9606:CACYBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SIAH1.|||Abolishes interaction with SIAH1; when associated with N-64.|||Abolishes interaction with SIAH1; when associated with N-66.|||CS|||Calcyclin-binding protein|||In isoform 2.|||In isoform 3.|||Interaction with S100A6|||Interaction with SIAH1|||Interaction with SKP1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||SGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185389|||http://purl.uniprot.org/annotation/VSP_010171|||http://purl.uniprot.org/annotation/VSP_010172|||http://purl.uniprot.org/annotation/VSP_046862
http://togogenome.org/gene/9606:RSPH4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTA9|||http://purl.uniprot.org/uniprot/Q5TD94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In CILD11.|||In CILD11; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Radial spoke head protein 4 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313738|||http://purl.uniprot.org/annotation/VAR_037715|||http://purl.uniprot.org/annotation/VAR_037716|||http://purl.uniprot.org/annotation/VAR_037717|||http://purl.uniprot.org/annotation/VAR_037718|||http://purl.uniprot.org/annotation/VAR_037719|||http://purl.uniprot.org/annotation/VAR_055235|||http://purl.uniprot.org/annotation/VAR_070565|||http://purl.uniprot.org/annotation/VSP_030125|||http://purl.uniprot.org/annotation/VSP_030126|||http://purl.uniprot.org/annotation/VSP_030127
http://togogenome.org/gene/9606:HMBOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes binding to telomeric 5'-TTAGGG-3' motif.|||Abolishes binding to telomeric 5'-TTAGGG-3' motif. Confers binding to the non-telomeric 5'-GTGAGT-3' motif.|||Critical for recognition and binding of 5'-TTAGGG-3' motifs in telomeric DNA|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HNF-p1|||Homeobox|||Homeobox-containing protein 1|||Impairs binding to telomeric 5'-TTAGGG-3' motif.|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||POU-specific atypical|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233287|||http://purl.uniprot.org/annotation/VSP_018111|||http://purl.uniprot.org/annotation/VSP_018112|||http://purl.uniprot.org/annotation/VSP_018113|||http://purl.uniprot.org/annotation/VSP_038983|||http://purl.uniprot.org/annotation/VSP_038984|||http://purl.uniprot.org/annotation/VSP_038985
http://togogenome.org/gene/9606:KLRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13241|||http://purl.uniprot.org/uniprot/Q53ZY6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to HLA-E.|||C-type lectin|||Cytoplasmic|||Extracellular|||Has no impact on the affinity for HLA-E.|||Helical|||Helical; Signal-anchor for type II membrane protein|||Impairs binding to HLA-E.|||In isoform 2.|||In isoform 3.|||Interchain (with C-116 in KLRC1/NGK2A)|||N-linked (GlcNAc...) asparagine|||Natural killer cells antigen CD94|||Reduces binding to HLA-E.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046587|||http://purl.uniprot.org/annotation/VAR_050103|||http://purl.uniprot.org/annotation/VSP_003052|||http://purl.uniprot.org/annotation/VSP_003053
http://togogenome.org/gene/9606:PUF60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PL19|||http://purl.uniprot.org/uniprot/E9PQ56|||http://purl.uniprot.org/uniprot/H0YEM1|||http://purl.uniprot.org/uniprot/Q9UHX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In VRJS; loss of function mutation; results in altered dosage of different PUF60 protein forms and abnormal splicing profile of several target genes.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||Inhibits homodimerization|||Inhibits transcriptional repression, interaction with ERCC3 and apoptosis induction|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Poly(U)-binding-splicing factor PUF60|||RRM|||RRM 1|||RRM 2|||RRM 3; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299519|||http://purl.uniprot.org/annotation/VAR_070939|||http://purl.uniprot.org/annotation/VSP_027717|||http://purl.uniprot.org/annotation/VSP_027718|||http://purl.uniprot.org/annotation/VSP_027719
http://togogenome.org/gene/9606:MYPOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Myb-like|||Myb-related transcription factor, partner of profilin|||Nuclear localization signal|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344799
http://togogenome.org/gene/9606:HSF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G112                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Heat shock factor protein 5|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333041|||http://purl.uniprot.org/annotation/VAR_043115|||http://purl.uniprot.org/annotation/VAR_055935|||http://purl.uniprot.org/annotation/VSP_033454
http://togogenome.org/gene/9606:SCARA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMJ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen-like|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||SRCR|||Scavenger receptor class A member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279518|||http://purl.uniprot.org/annotation/VAR_030915|||http://purl.uniprot.org/annotation/VAR_052062|||http://purl.uniprot.org/annotation/VSP_023472|||http://purl.uniprot.org/annotation/VSP_023473|||http://purl.uniprot.org/annotation/VSP_023474|||http://purl.uniprot.org/annotation/VSP_023475
http://togogenome.org/gene/9606:ZBED6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86452                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  BED-type 1|||BED-type 2|||Disordered|||HATC (Hobo-Ac-Tam3) domain|||Phosphoserine|||Polar residues|||Required for nucleolar localization|||Zinc finger BED domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392573
http://togogenome.org/gene/9606:GPBP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Vasculin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324115|||http://purl.uniprot.org/annotation/VAR_039655|||http://purl.uniprot.org/annotation/VAR_039656
http://togogenome.org/gene/9606:SLC27A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14975                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Long-chain fatty acid transport protein 2|||Lumenal|||N6-acetyllysine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193204|||http://purl.uniprot.org/annotation/VAR_046533|||http://purl.uniprot.org/annotation/VSP_042726
http://togogenome.org/gene/9606:ABCC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09428                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 8|||Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=16|||Helical; Name=17|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In HHF1 and PNDM3.|||In HHF1.|||In HHF1; altered intracellular trafficking.|||In HHF1; cannot form a functional channel, due to protein instability or defective transport to the membrane.|||In HHF1; channels insensitive to metabolic inhibition and to activation by ADP.|||In HHF1; does not alter surface expression but channels are not functional.|||In HHF1; highly decreases cell membrane expression; highly reduced traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide.|||In HHF1; mild.|||In HHF1; mild; dominantly inherited; channels insensitive to metabolic inhibition and to activation by ADP.|||In HHF1; modest impairment of channel function.|||In HHF1; no effect on cell membrane expression; no effect on traffic efficiency; dramatically reduced potassium channel response to activators such as MgADP or to diazoxide.|||In HHF1; no effect on cell membrane expression; no effect on traffic efficiency; reduced potassium channel response to activators such as MgADP or to diazoxide.|||In HHF1; reduced channels surface expression and response to ADP.|||In HHF1; severe.|||In HHF1; severe; high frequency in Ashkenazi Jewish patients; defective trafficking and lack of surface expression.|||In HHF1; severe; high prevalence in Finland; loss of channel activity.|||In HHF1; severe; loss of channel activity.|||In LIH; partially impairs ATP-dependent potassium channel function.|||In PNDM3.|||In PNDM3; highly reduced inhibition by ATP when associated with I-229.|||In PNDM3; highly reduced inhibition by ATP when associated with L-1523.|||In PNDM3; mosaic.|||In PNDM3; overactive channel.|||In PNDM3; reduced inhibition by ATP.|||In PNDM3; slightly reduced inhibition by ATP.|||In PNDM3; with neurologic features; reduces the sensitivity of the K(ATP) channel to inhibition by MgATP; increases whole-cell K(ATP) current.|||In TNDM2.|||In TNDM2; overactive channel.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093400|||http://purl.uniprot.org/annotation/VAR_000100|||http://purl.uniprot.org/annotation/VAR_008537|||http://purl.uniprot.org/annotation/VAR_008538|||http://purl.uniprot.org/annotation/VAR_008539|||http://purl.uniprot.org/annotation/VAR_008540|||http://purl.uniprot.org/annotation/VAR_008639|||http://purl.uniprot.org/annotation/VAR_008640|||http://purl.uniprot.org/annotation/VAR_008641|||http://purl.uniprot.org/annotation/VAR_008642|||http://purl.uniprot.org/annotation/VAR_008643|||http://purl.uniprot.org/annotation/VAR_008644|||http://purl.uniprot.org/annotation/VAR_008645|||http://purl.uniprot.org/annotation/VAR_008646|||http://purl.uniprot.org/annotation/VAR_008647|||http://purl.uniprot.org/annotation/VAR_008648|||http://purl.uniprot.org/annotation/VAR_008649|||http://purl.uniprot.org/annotation/VAR_008650|||http://purl.uniprot.org/annotation/VAR_008651|||http://purl.uniprot.org/annotation/VAR_008652|||http://purl.uniprot.org/annotation/VAR_008653|||http://purl.uniprot.org/annotation/VAR_008654|||http://purl.uniprot.org/annotation/VAR_008655|||http://purl.uniprot.org/annotation/VAR_008656|||http://purl.uniprot.org/annotation/VAR_008657|||http://purl.uniprot.org/annotation/VAR_008658|||http://purl.uniprot.org/annotation/VAR_015006|||http://purl.uniprot.org/annotation/VAR_015007|||http://purl.uniprot.org/annotation/VAR_015008|||http://purl.uniprot.org/annotation/VAR_015009|||http://purl.uniprot.org/annotation/VAR_015010|||http://purl.uniprot.org/annotation/VAR_029777|||http://purl.uniprot.org/annotation/VAR_029778|||http://purl.uniprot.org/annotation/VAR_029779|||http://purl.uniprot.org/annotation/VAR_029780|||http://purl.uniprot.org/annotation/VAR_029781|||http://purl.uniprot.org/annotation/VAR_029782|||http://purl.uniprot.org/annotation/VAR_029783|||http://purl.uniprot.org/annotation/VAR_029784|||http://purl.uniprot.org/annotation/VAR_029785|||http://purl.uniprot.org/annotation/VAR_029786|||http://purl.uniprot.org/annotation/VAR_029787|||http://purl.uniprot.org/annotation/VAR_031349|||http://purl.uniprot.org/annotation/VAR_031350|||http://purl.uniprot.org/annotation/VAR_031351|||http://purl.uniprot.org/annotation/VAR_031352|||http://purl.uniprot.org/annotation/VAR_031353|||http://purl.uniprot.org/annotation/VAR_031354|||http://purl.uniprot.org/annotation/VAR_031355|||http://purl.uniprot.org/annotation/VAR_031356|||http://purl.uniprot.org/annotation/VAR_031357|||http://purl.uniprot.org/annotation/VAR_031358|||http://purl.uniprot.org/annotation/VAR_031359|||http://purl.uniprot.org/annotation/VAR_031360|||http://purl.uniprot.org/annotation/VAR_031361|||http://purl.uniprot.org/annotation/VAR_031362|||http://purl.uniprot.org/annotation/VAR_031363|||http://purl.uniprot.org/annotation/VAR_031364|||http://purl.uniprot.org/annotation/VAR_031365|||http://purl.uniprot.org/annotation/VAR_031366|||http://purl.uniprot.org/annotation/VAR_031367|||http://purl.uniprot.org/annotation/VAR_031368|||http://purl.uniprot.org/annotation/VAR_031369|||http://purl.uniprot.org/annotation/VAR_031370|||http://purl.uniprot.org/annotation/VAR_031371|||http://purl.uniprot.org/annotation/VAR_031372|||http://purl.uniprot.org/annotation/VAR_031373|||http://purl.uniprot.org/annotation/VAR_031374|||http://purl.uniprot.org/annotation/VAR_031375|||http://purl.uniprot.org/annotation/VAR_031376|||http://purl.uniprot.org/annotation/VAR_031377|||http://purl.uniprot.org/annotation/VAR_031378|||http://purl.uniprot.org/annotation/VAR_031379|||http://purl.uniprot.org/annotation/VAR_031380|||http://purl.uniprot.org/annotation/VAR_031381|||http://purl.uniprot.org/annotation/VAR_031382|||http://purl.uniprot.org/annotation/VAR_031383|||http://purl.uniprot.org/annotation/VAR_031384|||http://purl.uniprot.org/annotation/VAR_031385|||http://purl.uniprot.org/annotation/VAR_031386|||http://purl.uniprot.org/annotation/VAR_031387|||http://purl.uniprot.org/annotation/VAR_031388|||http://purl.uniprot.org/annotation/VAR_031389|||http://purl.uniprot.org/annotation/VAR_072928|||http://purl.uniprot.org/annotation/VAR_072929|||http://purl.uniprot.org/annotation/VAR_072930|||http://purl.uniprot.org/annotation/VAR_072931|||http://purl.uniprot.org/annotation/VAR_072932|||http://purl.uniprot.org/annotation/VAR_072933|||http://purl.uniprot.org/annotation/VAR_072934|||http://purl.uniprot.org/annotation/VAR_072935|||http://purl.uniprot.org/annotation/VAR_072936|||http://purl.uniprot.org/annotation/VAR_072937|||http://purl.uniprot.org/annotation/VAR_072938|||http://purl.uniprot.org/annotation/VAR_072939|||http://purl.uniprot.org/annotation/VAR_072940|||http://purl.uniprot.org/annotation/VAR_072941|||http://purl.uniprot.org/annotation/VAR_072942|||http://purl.uniprot.org/annotation/VAR_072943|||http://purl.uniprot.org/annotation/VAR_072944|||http://purl.uniprot.org/annotation/VAR_072945|||http://purl.uniprot.org/annotation/VAR_072946|||http://purl.uniprot.org/annotation/VAR_072947|||http://purl.uniprot.org/annotation/VAR_072948|||http://purl.uniprot.org/annotation/VAR_072949|||http://purl.uniprot.org/annotation/VAR_072950|||http://purl.uniprot.org/annotation/VAR_072951|||http://purl.uniprot.org/annotation/VAR_072952|||http://purl.uniprot.org/annotation/VAR_072953|||http://purl.uniprot.org/annotation/VSP_000055|||http://purl.uniprot.org/annotation/VSP_044090
http://togogenome.org/gene/9606:CHIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Cysteine-rich hydrophobic domain-containing protein 1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189554|||http://purl.uniprot.org/annotation/VSP_034830
http://togogenome.org/gene/9606:DRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14416                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||D(2) dopamine receptor|||Decreased palmitoylation; decreased localization to the plasma membrane; decreased stability.|||Disordered|||Extracellular|||Found in patients with alcohol-responsive myoclonus-dystonia; unknown pathological significance; the mutation does not affect functional properties.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for receptor activation|||In isoform 2.|||In isoform 3.|||Interaction with PPP1R9B|||May be associated with a higher risk for schizophrenia.|||N-linked (GlcNAc...) asparagine|||No effect on palmitoylation; no effect on localization to the plasma membrane.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069387|||http://purl.uniprot.org/annotation/VAR_003462|||http://purl.uniprot.org/annotation/VAR_014674|||http://purl.uniprot.org/annotation/VAR_017143|||http://purl.uniprot.org/annotation/VAR_064579|||http://purl.uniprot.org/annotation/VSP_001870|||http://purl.uniprot.org/annotation/VSP_026455
http://togogenome.org/gene/9606:EFEMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3V1|||http://purl.uniprot.org/uniprot/A0A0S2Z4F1|||http://purl.uniprot.org/uniprot/B2R6M6|||http://purl.uniprot.org/uniprot/Q12805                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-containing fibulin-like extracellular matrix protein 1|||EGF-like|||EGF-like 1; atypical|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||In DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mediates interaction with TIMP3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007570|||http://purl.uniprot.org/annotation/PRO_5002781797|||http://purl.uniprot.org/annotation/PRO_5006608236|||http://purl.uniprot.org/annotation/PRO_5014035617|||http://purl.uniprot.org/annotation/VAR_009512|||http://purl.uniprot.org/annotation/VAR_009513|||http://purl.uniprot.org/annotation/VSP_001392|||http://purl.uniprot.org/annotation/VSP_001393|||http://purl.uniprot.org/annotation/VSP_001394|||http://purl.uniprot.org/annotation/VSP_054372|||http://purl.uniprot.org/annotation/VSP_054373
http://togogenome.org/gene/9606:F7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPM2|||http://purl.uniprot.org/uniprot/F5H8B0|||http://purl.uniprot.org/uniprot/P08709                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Charge relay system|||Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin|||Complete loss of O-glycosylation and O-xylosylation by POGLUT1.|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2|||Factor VII heavy chain|||Factor VII light chain|||Gla|||Important for S-112 for O-xylosylation|||In FA7D.|||In FA7D; Charlotte.|||In FA7D; Harrow/Padua.|||In FA7D; Malta-I.|||In FA7D; Malta-II.|||In FA7D; Mie.|||In FA7D; Morioka.|||In FA7D; exhibits no procoagulant activity and is unable to bind tissue factor.|||In FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities.|||In FA7D; results in severely impaired protein secretion.|||In isoform B.|||May be associated with decreased susceptibility to myocardial infarction.|||N-linked (GlcNAc...) asparagine|||No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation.|||O-linked (Fuc) serine|||O-linked (Glc...) serine; alternate|||O-linked (Xyl...) serine; alternate|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000007|||http://purl.uniprot.org/annotation/CAR_000180|||http://purl.uniprot.org/annotation/PRO_0000027729|||http://purl.uniprot.org/annotation/PRO_0000027730|||http://purl.uniprot.org/annotation/PRO_0000027731|||http://purl.uniprot.org/annotation/PRO_5002803761|||http://purl.uniprot.org/annotation/PRO_5003324769|||http://purl.uniprot.org/annotation/VAR_006497|||http://purl.uniprot.org/annotation/VAR_006498|||http://purl.uniprot.org/annotation/VAR_006499|||http://purl.uniprot.org/annotation/VAR_006500|||http://purl.uniprot.org/annotation/VAR_006501|||http://purl.uniprot.org/annotation/VAR_006502|||http://purl.uniprot.org/annotation/VAR_006503|||http://purl.uniprot.org/annotation/VAR_006504|||http://purl.uniprot.org/annotation/VAR_006505|||http://purl.uniprot.org/annotation/VAR_006506|||http://purl.uniprot.org/annotation/VAR_006507|||http://purl.uniprot.org/annotation/VAR_006508|||http://purl.uniprot.org/annotation/VAR_006509|||http://purl.uniprot.org/annotation/VAR_006510|||http://purl.uniprot.org/annotation/VAR_006511|||http://purl.uniprot.org/annotation/VAR_006512|||http://purl.uniprot.org/annotation/VAR_006513|||http://purl.uniprot.org/annotation/VAR_006514|||http://purl.uniprot.org/annotation/VAR_006515|||http://purl.uniprot.org/annotation/VAR_006516|||http://purl.uniprot.org/annotation/VAR_006517|||http://purl.uniprot.org/annotation/VAR_006518|||http://purl.uniprot.org/annotation/VAR_006519|||http://purl.uniprot.org/annotation/VAR_013122|||http://purl.uniprot.org/annotation/VAR_013123|||http://purl.uniprot.org/annotation/VAR_013936|||http://purl.uniprot.org/annotation/VAR_014391|||http://purl.uniprot.org/annotation/VAR_014392|||http://purl.uniprot.org/annotation/VAR_014405|||http://purl.uniprot.org/annotation/VAR_014406|||http://purl.uniprot.org/annotation/VAR_014407|||http://purl.uniprot.org/annotation/VAR_014408|||http://purl.uniprot.org/annotation/VAR_014409|||http://purl.uniprot.org/annotation/VAR_014410|||http://purl.uniprot.org/annotation/VAR_014411|||http://purl.uniprot.org/annotation/VAR_014412|||http://purl.uniprot.org/annotation/VAR_014413|||http://purl.uniprot.org/annotation/VAR_014414|||http://purl.uniprot.org/annotation/VAR_014415|||http://purl.uniprot.org/annotation/VAR_014416|||http://purl.uniprot.org/annotation/VAR_014417|||http://purl.uniprot.org/annotation/VAR_014418|||http://purl.uniprot.org/annotation/VAR_014419|||http://purl.uniprot.org/annotation/VAR_014420|||http://purl.uniprot.org/annotation/VAR_015135|||http://purl.uniprot.org/annotation/VAR_015136|||http://purl.uniprot.org/annotation/VAR_015137|||http://purl.uniprot.org/annotation/VAR_015138|||http://purl.uniprot.org/annotation/VAR_015139|||http://purl.uniprot.org/annotation/VAR_015140|||http://purl.uniprot.org/annotation/VAR_015141|||http://purl.uniprot.org/annotation/VAR_015142|||http://purl.uniprot.org/annotation/VAR_015143|||http://purl.uniprot.org/annotation/VAR_015144|||http://purl.uniprot.org/annotation/VAR_018671|||http://purl.uniprot.org/annotation/VAR_065369|||http://purl.uniprot.org/annotation/VAR_065370|||http://purl.uniprot.org/annotation/VAR_065371|||http://purl.uniprot.org/annotation/VAR_065372|||http://purl.uniprot.org/annotation/VAR_065373|||http://purl.uniprot.org/annotation/VAR_065374|||http://purl.uniprot.org/annotation/VAR_065375|||http://purl.uniprot.org/annotation/VAR_065376|||http://purl.uniprot.org/annotation/VAR_065377|||http://purl.uniprot.org/annotation/VAR_065378|||http://purl.uniprot.org/annotation/VAR_065379|||http://purl.uniprot.org/annotation/VAR_065380|||http://purl.uniprot.org/annotation/VAR_065381|||http://purl.uniprot.org/annotation/VAR_065382|||http://purl.uniprot.org/annotation/VAR_065383|||http://purl.uniprot.org/annotation/VAR_065384|||http://purl.uniprot.org/annotation/VAR_065385|||http://purl.uniprot.org/annotation/VAR_065386|||http://purl.uniprot.org/annotation/VAR_065387|||http://purl.uniprot.org/annotation/VAR_065388|||http://purl.uniprot.org/annotation/VAR_065389|||http://purl.uniprot.org/annotation/VAR_065390|||http://purl.uniprot.org/annotation/VAR_065391|||http://purl.uniprot.org/annotation/VAR_065392|||http://purl.uniprot.org/annotation/VAR_065393|||http://purl.uniprot.org/annotation/VAR_065394|||http://purl.uniprot.org/annotation/VAR_065395|||http://purl.uniprot.org/annotation/VAR_065396|||http://purl.uniprot.org/annotation/VAR_065397|||http://purl.uniprot.org/annotation/VAR_065398|||http://purl.uniprot.org/annotation/VAR_065399|||http://purl.uniprot.org/annotation/VAR_065400|||http://purl.uniprot.org/annotation/VAR_065401|||http://purl.uniprot.org/annotation/VAR_065402|||http://purl.uniprot.org/annotation/VAR_065403|||http://purl.uniprot.org/annotation/VAR_065404|||http://purl.uniprot.org/annotation/VAR_065405|||http://purl.uniprot.org/annotation/VAR_065406|||http://purl.uniprot.org/annotation/VAR_065407|||http://purl.uniprot.org/annotation/VAR_065408|||http://purl.uniprot.org/annotation/VAR_065409|||http://purl.uniprot.org/annotation/VAR_065410|||http://purl.uniprot.org/annotation/VAR_065411|||http://purl.uniprot.org/annotation/VAR_065412|||http://purl.uniprot.org/annotation/VAR_065413|||http://purl.uniprot.org/annotation/VAR_065414|||http://purl.uniprot.org/annotation/VAR_065415|||http://purl.uniprot.org/annotation/VAR_065416|||http://purl.uniprot.org/annotation/VAR_065417|||http://purl.uniprot.org/annotation/VAR_065418|||http://purl.uniprot.org/annotation/VAR_065419|||http://purl.uniprot.org/annotation/VAR_065420|||http://purl.uniprot.org/annotation/VAR_065421|||http://purl.uniprot.org/annotation/VAR_065422|||http://purl.uniprot.org/annotation/VAR_065423|||http://purl.uniprot.org/annotation/VAR_065424|||http://purl.uniprot.org/annotation/VAR_065425|||http://purl.uniprot.org/annotation/VAR_065426|||http://purl.uniprot.org/annotation/VAR_065427|||http://purl.uniprot.org/annotation/VAR_076570|||http://purl.uniprot.org/annotation/VSP_005387
http://togogenome.org/gene/9606:PLIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN8|||http://purl.uniprot.org/uniprot/O60664                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished phosphorylation at Tyr-232 by isoform 1 of CHKA (CHKalpha2).|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||N6-acetyllysine|||Perilipin-3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099890|||http://purl.uniprot.org/annotation/VAR_022780|||http://purl.uniprot.org/annotation/VAR_024559|||http://purl.uniprot.org/annotation/VSP_004664|||http://purl.uniprot.org/annotation/VSP_040325|||http://purl.uniprot.org/annotation/VSP_047038
http://togogenome.org/gene/9606:MICAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTP6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes Monooxygenase activity and impairs ability to control docking and fusion of exocytic carriers.|||Acidic residues|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In MICAL-3NLSMut; abolishes nuclear localization.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM zinc-binding|||Monooxygenase domain|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||[F-actin]-monooxygenase MICAL3|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075846|||http://purl.uniprot.org/annotation/VAR_018263|||http://purl.uniprot.org/annotation/VAR_059451|||http://purl.uniprot.org/annotation/VAR_059452|||http://purl.uniprot.org/annotation/VSP_039485|||http://purl.uniprot.org/annotation/VSP_039486|||http://purl.uniprot.org/annotation/VSP_039487|||http://purl.uniprot.org/annotation/VSP_039488|||http://purl.uniprot.org/annotation/VSP_039489|||http://purl.uniprot.org/annotation/VSP_042600|||http://purl.uniprot.org/annotation/VSP_042601|||http://purl.uniprot.org/annotation/VSP_042602
http://togogenome.org/gene/9606:GOLGA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5G4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Golgin subfamily A member 7|||In isoform 2.|||S-palmitoyl cysteine|||Slightly reduces palmitoylation.|||Strongly reduces palmitoylation. Abolishes palmitoylation and Golgi localization; when associated with A-69.|||Strongly reduces palmitoylation. Abolishes palmitoylation and Golgi localization; when associated with A-72.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213977|||http://purl.uniprot.org/annotation/VSP_046793
http://togogenome.org/gene/9606:SPTBN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2ZZ89|||http://purl.uniprot.org/uniprot/Q01082                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In DDISBA.|||In DDISBA; affects function in neuronal axonal growth; decreased ankyrin binding; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; decreased interaction with SPTAN1; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; forms cytosolic aggregates; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; increased F-actin binding; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; no effect on F-actin binding; disturbs cytoskeleton organization and dynamics.|||In DDISBA; affects function in neuronal axonal growth; reduced F-actin binding; disturbs cytoskeleton organization and dynamics.|||In DDISBA; disturbs cytoskeleton organization and dynamics.|||In DDISBA; distursb cytoskeleton organization and dynamics.|||In DDISBA; unknown pathological significance.|||In isoform 2.|||In isoform Short.|||Interaction with ANK2|||Mediates interaction with CAMSAP1|||N-acetylthreonine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin beta chain, non-erythrocytic 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073461|||http://purl.uniprot.org/annotation/VAR_032641|||http://purl.uniprot.org/annotation/VAR_086305|||http://purl.uniprot.org/annotation/VAR_086306|||http://purl.uniprot.org/annotation/VAR_086307|||http://purl.uniprot.org/annotation/VAR_086308|||http://purl.uniprot.org/annotation/VAR_086309|||http://purl.uniprot.org/annotation/VAR_086310|||http://purl.uniprot.org/annotation/VAR_086311|||http://purl.uniprot.org/annotation/VAR_086312|||http://purl.uniprot.org/annotation/VAR_086313|||http://purl.uniprot.org/annotation/VAR_086314|||http://purl.uniprot.org/annotation/VAR_086315|||http://purl.uniprot.org/annotation/VAR_086316|||http://purl.uniprot.org/annotation/VAR_086317|||http://purl.uniprot.org/annotation/VAR_086318|||http://purl.uniprot.org/annotation/VAR_086319|||http://purl.uniprot.org/annotation/VAR_086320|||http://purl.uniprot.org/annotation/VAR_086321|||http://purl.uniprot.org/annotation/VAR_086322|||http://purl.uniprot.org/annotation/VAR_086323|||http://purl.uniprot.org/annotation/VAR_086324|||http://purl.uniprot.org/annotation/VAR_086325|||http://purl.uniprot.org/annotation/VAR_086326|||http://purl.uniprot.org/annotation/VAR_086327|||http://purl.uniprot.org/annotation/VAR_086328|||http://purl.uniprot.org/annotation/VAR_086329|||http://purl.uniprot.org/annotation/VSP_000720|||http://purl.uniprot.org/annotation/VSP_000721|||http://purl.uniprot.org/annotation/VSP_026054|||http://purl.uniprot.org/annotation/VSP_026055|||http://purl.uniprot.org/annotation/VSP_026056
http://togogenome.org/gene/9606:POLR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14802                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bridging helix|||DNA-directed RNA polymerase III subunit RPC1|||In HLD7.|||In WDRTS.|||In WDRTS; unknown pathological significance.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073947|||http://purl.uniprot.org/annotation/VAR_051873|||http://purl.uniprot.org/annotation/VAR_051874|||http://purl.uniprot.org/annotation/VAR_066516|||http://purl.uniprot.org/annotation/VAR_066517|||http://purl.uniprot.org/annotation/VAR_066518|||http://purl.uniprot.org/annotation/VAR_066519|||http://purl.uniprot.org/annotation/VAR_066520|||http://purl.uniprot.org/annotation/VAR_066521|||http://purl.uniprot.org/annotation/VAR_066522|||http://purl.uniprot.org/annotation/VAR_066523|||http://purl.uniprot.org/annotation/VAR_066524|||http://purl.uniprot.org/annotation/VAR_067004|||http://purl.uniprot.org/annotation/VAR_072338|||http://purl.uniprot.org/annotation/VAR_072339|||http://purl.uniprot.org/annotation/VAR_072340|||http://purl.uniprot.org/annotation/VAR_072341|||http://purl.uniprot.org/annotation/VAR_072342|||http://purl.uniprot.org/annotation/VAR_072343|||http://purl.uniprot.org/annotation/VAR_081999|||http://purl.uniprot.org/annotation/VAR_082000|||http://purl.uniprot.org/annotation/VAR_082001|||http://purl.uniprot.org/annotation/VAR_082002|||http://purl.uniprot.org/annotation/VAR_082003|||http://purl.uniprot.org/annotation/VAR_082004|||http://purl.uniprot.org/annotation/VAR_082005|||http://purl.uniprot.org/annotation/VAR_082006|||http://purl.uniprot.org/annotation/VAR_082007
http://togogenome.org/gene/9606:TONSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Abolished interaction with histone H4 and recruitment to replication forks without affecting interaction with MMS22L.|||Acidic residues|||Basic and acidic residues|||Disordered|||In SEMDSP.|||In SEMDSP; decreased function in double-strand break repair via homologous recombination.|||In SEMDSP; decreased function in double-strand break repair via homologous recombination; decreased protein amount in patient cells.|||In SEMDSP; disease phenotype includes immunologic and hematologic abnormalities.|||In SEMDSP; disease phenotype includes immunologic and hematologic abnormalities; unknown pathological significance.|||In SEMDSP; disease phenotype includes primary aphakia and absent pupils.|||In SEMDSP; unknown pathological significance.|||In SEMDSP; unknown pathological significance; decreased function in double-strand break repair via homologous recombination.|||In SEMDSP; unknown pathological significance; genomic instability; when associated with R-1090.|||In SEMDSP; unknown pathological significance; genomic instability; when associated with R-430.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tonsoku-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326634|||http://purl.uniprot.org/annotation/VAR_042411|||http://purl.uniprot.org/annotation/VAR_042412|||http://purl.uniprot.org/annotation/VAR_042413|||http://purl.uniprot.org/annotation/VAR_042414|||http://purl.uniprot.org/annotation/VAR_083007|||http://purl.uniprot.org/annotation/VAR_083008|||http://purl.uniprot.org/annotation/VAR_083009|||http://purl.uniprot.org/annotation/VAR_083010|||http://purl.uniprot.org/annotation/VAR_083011|||http://purl.uniprot.org/annotation/VAR_083012|||http://purl.uniprot.org/annotation/VAR_083013|||http://purl.uniprot.org/annotation/VAR_083014|||http://purl.uniprot.org/annotation/VAR_083015|||http://purl.uniprot.org/annotation/VAR_083016|||http://purl.uniprot.org/annotation/VAR_083017|||http://purl.uniprot.org/annotation/VAR_083018|||http://purl.uniprot.org/annotation/VAR_083019|||http://purl.uniprot.org/annotation/VAR_083020|||http://purl.uniprot.org/annotation/VAR_083021|||http://purl.uniprot.org/annotation/VAR_083022|||http://purl.uniprot.org/annotation/VAR_083023|||http://purl.uniprot.org/annotation/VAR_083024|||http://purl.uniprot.org/annotation/VAR_083025|||http://purl.uniprot.org/annotation/VAR_083026|||http://purl.uniprot.org/annotation/VAR_086303|||http://purl.uniprot.org/annotation/VAR_086304|||http://purl.uniprot.org/annotation/VSP_032686
http://togogenome.org/gene/9606:PVR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSA9|||http://purl.uniprot.org/uniprot/A0A0C4DG49|||http://purl.uniprot.org/uniprot/A8K4I1|||http://purl.uniprot.org/uniprot/P15151                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DYNLT1 binding|||Extracellular|||Helical|||ITIM motif|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform Beta.|||In isoform Delta.|||In isoform Gamma.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Partial loss of DYNLT1 binding.|||Phosphotyrosine|||Poliovirus receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015131|||http://purl.uniprot.org/annotation/PRO_5001974465|||http://purl.uniprot.org/annotation/PRO_5002722148|||http://purl.uniprot.org/annotation/PRO_5014222192|||http://purl.uniprot.org/annotation/VAR_003952|||http://purl.uniprot.org/annotation/VAR_011736|||http://purl.uniprot.org/annotation/VAR_049994|||http://purl.uniprot.org/annotation/VSP_002617|||http://purl.uniprot.org/annotation/VSP_002618|||http://purl.uniprot.org/annotation/VSP_002619|||http://purl.uniprot.org/annotation/VSP_002620|||http://purl.uniprot.org/annotation/VSP_002621
http://togogenome.org/gene/9606:NFKB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19838                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Basic and acidic residues|||Cleavage (when cotranslationally processed)|||Death|||Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923.|||Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932.|||Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932.|||Decreased phosphorylation by IKBKB/IKKB and decreased generation of the NF-kappa-B p50 subunit from p105.|||Disordered|||Essential for interaction with HIF1AN|||Fails to promote HIF1AN-dependent 2-oxoglutarate decarboxylation.|||GRR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with CFLAR|||N6-acetyllysine; by EP300|||Nuclear factor NF-kappa-B p105 subunit|||Nuclear factor NF-kappa-B p50 subunit|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by GSK3-beta; in vitro|||Phosphoserine; by IKKB|||Phosphoserine; by PKA|||Phosphothreonine|||Prevents p105 proteolysis in response to TNF-alpha.|||RHD|||S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate|||S-nitrosocysteine; alternate|||Suppresses S-nitrosylation-induced inhibition of DNA-binding activity. Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of DNA-binding activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030310|||http://purl.uniprot.org/annotation/PRO_0000030311|||http://purl.uniprot.org/annotation/VAR_016268|||http://purl.uniprot.org/annotation/VAR_016269|||http://purl.uniprot.org/annotation/VAR_016270|||http://purl.uniprot.org/annotation/VAR_016271|||http://purl.uniprot.org/annotation/VAR_016272|||http://purl.uniprot.org/annotation/VAR_016273|||http://purl.uniprot.org/annotation/VSP_021025|||http://purl.uniprot.org/annotation/VSP_042869|||http://purl.uniprot.org/annotation/VSP_042870
http://togogenome.org/gene/9606:ZSCAN22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10073                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047271
http://togogenome.org/gene/9606:CCL25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15444                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-C motif chemokine 25|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005235|||http://purl.uniprot.org/annotation/VAR_044519|||http://purl.uniprot.org/annotation/VAR_044520|||http://purl.uniprot.org/annotation/VAR_044521|||http://purl.uniprot.org/annotation/VSP_001064|||http://purl.uniprot.org/annotation/VSP_043199
http://togogenome.org/gene/9606:TCTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GX1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Tectonic-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229798|||http://purl.uniprot.org/annotation/VSP_042776
http://togogenome.org/gene/9606:COPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14579                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Coatomer subunit epsilon|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193851|||http://purl.uniprot.org/annotation/VAR_054032|||http://purl.uniprot.org/annotation/VAR_054033|||http://purl.uniprot.org/annotation/VSP_042770|||http://purl.uniprot.org/annotation/VSP_042771|||http://purl.uniprot.org/annotation/VSP_045070
http://togogenome.org/gene/9606:NIPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTP0|||http://purl.uniprot.org/uniprot/Q8TAY1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In SPG6.|||In isoform 2.|||Magnesium transporter NIPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191741|||http://purl.uniprot.org/annotation/VAR_023440|||http://purl.uniprot.org/annotation/VAR_023441|||http://purl.uniprot.org/annotation/VSP_017189
http://togogenome.org/gene/9606:PGRMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00264|||http://purl.uniprot.org/uniprot/Q6IB11                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with CYP1A1 and CYP3A4.|||Cytochrome b5 heme-binding|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Membrane-associated progesterone receptor component 1|||Phosphoserine|||Phosphothreonine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121739|||http://purl.uniprot.org/annotation/VSP_054710
http://togogenome.org/gene/9606:INPP5F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITL0|||http://purl.uniprot.org/uniprot/Q9Y2H2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HSac2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of inositol 4-phosphatase activity. Alters TFRC distribution and delays TF recycling.|||Phosphatidylinositide phosphatase SAC2|||Phosphoserine|||SAC|||hSac2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331621|||http://purl.uniprot.org/annotation/VAR_042907|||http://purl.uniprot.org/annotation/VAR_042908|||http://purl.uniprot.org/annotation/VSP_033266|||http://purl.uniprot.org/annotation/VSP_033267|||http://purl.uniprot.org/annotation/VSP_033268|||http://purl.uniprot.org/annotation/VSP_033269|||http://purl.uniprot.org/annotation/VSP_046366|||http://purl.uniprot.org/annotation/VSP_046367
http://togogenome.org/gene/9606:KCNK15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H427                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In allele TASK-5A and allele TASK-5C.|||In allele TASK-5A.|||No effect on lack of functional expression.|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101765|||http://purl.uniprot.org/annotation/VAR_014211|||http://purl.uniprot.org/annotation/VAR_014212|||http://purl.uniprot.org/annotation/VAR_014213|||http://purl.uniprot.org/annotation/VAR_014214
http://togogenome.org/gene/9606:IGSF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein turtle homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306107|||http://purl.uniprot.org/annotation/VAR_035256|||http://purl.uniprot.org/annotation/VAR_035257|||http://purl.uniprot.org/annotation/VAR_035258|||http://purl.uniprot.org/annotation/VAR_035259|||http://purl.uniprot.org/annotation/VAR_035260|||http://purl.uniprot.org/annotation/VSP_047195
http://togogenome.org/gene/9606:METTL27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6F8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Methyltransferase-like protein 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223961|||http://purl.uniprot.org/annotation/VAR_060385|||http://purl.uniprot.org/annotation/VAR_060386
http://togogenome.org/gene/9606:COA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BR5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome c oxidase assembly factor 7|||In SCAN3.|||In SCAN3; results in increased proteasomal degradation; decreased protein levels; decreased amount of protein imported in the mitochondrion intermembrane space.|||In SCAN3; unknown pathological significance.|||N-acetylalanine|||Removed|||Sel1-like 1|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282364|||http://purl.uniprot.org/annotation/VAR_031401|||http://purl.uniprot.org/annotation/VAR_082218|||http://purl.uniprot.org/annotation/VAR_082219|||http://purl.uniprot.org/annotation/VAR_082220|||http://purl.uniprot.org/annotation/VAR_082221
http://togogenome.org/gene/9606:AGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20933                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Blocked amino end (Ser)|||Glycosylasparaginase alpha chain|||Glycosylasparaginase beta chain|||In AGU.|||In AGU; most frequent mutation; abolishes autocatalytic cleavage and enzyme activity.|||In AGU; specifically prevents the proteolytic activation cleavage of AGA in the endoplasmic reticulum.|||In AGU; uncertain pathological significance.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002333|||http://purl.uniprot.org/annotation/PRO_0000002334|||http://purl.uniprot.org/annotation/VAR_005069|||http://purl.uniprot.org/annotation/VAR_005070|||http://purl.uniprot.org/annotation/VAR_005071|||http://purl.uniprot.org/annotation/VAR_005072|||http://purl.uniprot.org/annotation/VAR_005073|||http://purl.uniprot.org/annotation/VAR_005074|||http://purl.uniprot.org/annotation/VAR_005075|||http://purl.uniprot.org/annotation/VAR_015427|||http://purl.uniprot.org/annotation/VAR_015428|||http://purl.uniprot.org/annotation/VAR_015429|||http://purl.uniprot.org/annotation/VAR_015430|||http://purl.uniprot.org/annotation/VAR_015431|||http://purl.uniprot.org/annotation/VAR_015432|||http://purl.uniprot.org/annotation/VAR_033533|||http://purl.uniprot.org/annotation/VAR_061026
http://togogenome.org/gene/9606:SEC14L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RMR2|||http://purl.uniprot.org/uniprot/B3KRP9|||http://purl.uniprot.org/uniprot/Q9UDX3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||GOLD|||In isoform 2.|||SEC14-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210760|||http://purl.uniprot.org/annotation/VAR_024629|||http://purl.uniprot.org/annotation/VAR_051914|||http://purl.uniprot.org/annotation/VAR_051915|||http://purl.uniprot.org/annotation/VAR_051916|||http://purl.uniprot.org/annotation/VSP_045200
http://togogenome.org/gene/9606:RENBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51606                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Activity is about 26% of that of the wild-type.|||Activity is similiar to wild-type.|||Important for enzyme activity|||In isoform 2.|||Leucine-zipper|||Loss of enzyme activity.|||N-acylglucosamine 2-epimerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208949|||http://purl.uniprot.org/annotation/VAR_029339|||http://purl.uniprot.org/annotation/VAR_049182|||http://purl.uniprot.org/annotation/VSP_039022|||http://purl.uniprot.org/annotation/VSP_039023
http://togogenome.org/gene/9606:LMNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03252                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Cysteine methyl ester|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In APLD.|||In EPM9; disrupts fibrillar formation.|||In MCPH27; increased aggregation; changed nuclear envelope organization.|||In a colorectal cancer sample; somatic mutation.|||LTD|||Lamin-B2|||Linker 1|||Linker 2|||May be a risk factor for partial acquired lipodystrophy.|||N6-acetyllysine; alternate|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063820|||http://purl.uniprot.org/annotation/PRO_0000403470|||http://purl.uniprot.org/annotation/VAR_031063|||http://purl.uniprot.org/annotation/VAR_031064|||http://purl.uniprot.org/annotation/VAR_036370|||http://purl.uniprot.org/annotation/VAR_074170|||http://purl.uniprot.org/annotation/VAR_074171|||http://purl.uniprot.org/annotation/VAR_085504|||http://purl.uniprot.org/annotation/VAR_085505
http://togogenome.org/gene/9606:OR5K4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMS3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5K4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312177|||http://purl.uniprot.org/annotation/VAR_037448
http://togogenome.org/gene/9606:LGALS7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47929                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076940
http://togogenome.org/gene/9606:PCDHB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMG6|||http://purl.uniprot.org/uniprot/Q9Y5E7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Protocadherin beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003916|||http://purl.uniprot.org/annotation/PRO_5004240314|||http://purl.uniprot.org/annotation/VAR_020365|||http://purl.uniprot.org/annotation/VAR_033701|||http://purl.uniprot.org/annotation/VAR_033702
http://togogenome.org/gene/9606:OSBPL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 6.|||N-acetylserine|||Oxysterol-binding protein-related protein 6|||PH|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100375|||http://purl.uniprot.org/annotation/VAR_053550|||http://purl.uniprot.org/annotation/VAR_057663|||http://purl.uniprot.org/annotation/VSP_010013|||http://purl.uniprot.org/annotation/VSP_036559|||http://purl.uniprot.org/annotation/VSP_036560|||http://purl.uniprot.org/annotation/VSP_036561|||http://purl.uniprot.org/annotation/VSP_054430|||http://purl.uniprot.org/annotation/VSP_054431
http://togogenome.org/gene/9606:ALOX5AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW23|||http://purl.uniprot.org/uniprot/P20292                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||INTRAMEM|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Arachidonate 5-lipoxygenase-activating protein|||Cytoplasmic|||Decreased affinity for the inhibitor MK-591.|||Helical|||Increased affinity for the inhibitor MK-591.|||Lumenal|||Strongly decreased affinity for the inhibitor MK-591.|||Strongly increased affinity for the inhibitor MK-591.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217751
http://togogenome.org/gene/9606:CCDC121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUS5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 121|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286559|||http://purl.uniprot.org/annotation/VSP_046649
http://togogenome.org/gene/9606:ATP6V0E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHE4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||V-type proton ATPase subunit e 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270199|||http://purl.uniprot.org/annotation/VSP_027104|||http://purl.uniprot.org/annotation/VSP_027105|||http://purl.uniprot.org/annotation/VSP_044857
http://togogenome.org/gene/9606:SMCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q147U7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Single-pass membrane and coiled-coil domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269483|||http://purl.uniprot.org/annotation/VAR_050721|||http://purl.uniprot.org/annotation/VAR_050722
http://togogenome.org/gene/9606:FOXP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Fork-head|||Forkhead box protein P4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091889|||http://purl.uniprot.org/annotation/VAR_036219|||http://purl.uniprot.org/annotation/VSP_043034|||http://purl.uniprot.org/annotation/VSP_043465|||http://purl.uniprot.org/annotation/VSP_043466
http://togogenome.org/gene/9606:HTR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28223                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 2A|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hydrophobic barrier that decreases the speed of ligand binding and dissociation|||In isoform 2.|||Increased ability of hallucinogens to desensitize the receptor.|||Loss of interaction with PATJ, CASK, APBA1, DLG1 and DLG4.|||Loss of interaction with PATJ.|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||No effect on interaction with PATJ. Acquires the binding properties of HTR2C; when associated with S-465.|||No effect on interaction with PATJ. Acquires the binding properties of HTR2C; when associated with S-470.|||PDZ-binding|||Phosphoserine|||Reduced receptor desensitization by nonhallucinogenic agonists.|||Strongly increases dissociation of bound lysergic acid diethylamine, without affecting binding affinity. Reduces signaling via arrestins, but has no effect on signaling via the phosphatidylinositol-calcium second messenger system.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068946|||http://purl.uniprot.org/annotation/VAR_003448|||http://purl.uniprot.org/annotation/VAR_003449|||http://purl.uniprot.org/annotation/VAR_013901|||http://purl.uniprot.org/annotation/VAR_013902|||http://purl.uniprot.org/annotation/VSP_046663
http://togogenome.org/gene/9606:GAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3V5|||http://purl.uniprot.org/uniprot/Q8IVA8|||http://purl.uniprot.org/uniprot/Q99259                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glutamate decarboxylase 1|||In DEE89.|||In DEE89; unknown pathological significance.|||In DEE89; unknown pathological significance; no effect on protein abundance; no effect on splicing.|||In isoform 3.|||In isoform 4.|||N6-(pyridoxal phosphate)lysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146963|||http://purl.uniprot.org/annotation/VAR_011882|||http://purl.uniprot.org/annotation/VAR_011883|||http://purl.uniprot.org/annotation/VAR_011884|||http://purl.uniprot.org/annotation/VAR_018861|||http://purl.uniprot.org/annotation/VAR_031021|||http://purl.uniprot.org/annotation/VAR_085520|||http://purl.uniprot.org/annotation/VAR_085521|||http://purl.uniprot.org/annotation/VAR_085522|||http://purl.uniprot.org/annotation/VSP_009123|||http://purl.uniprot.org/annotation/VSP_009124|||http://purl.uniprot.org/annotation/VSP_054473|||http://purl.uniprot.org/annotation/VSP_054474
http://togogenome.org/gene/9606:ZACN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q401N2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Zinc-activated ligand-gated ion channel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317165|||http://purl.uniprot.org/annotation/VAR_038483|||http://purl.uniprot.org/annotation/VSP_030909|||http://purl.uniprot.org/annotation/VSP_030910|||http://purl.uniprot.org/annotation/VSP_030911|||http://purl.uniprot.org/annotation/VSP_030912
http://togogenome.org/gene/9606:GTF2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35269                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Eliminates putative kinase activity; when associated with A-385.|||Eliminates putative kinase activity; when associated with A-389.|||General transcription factor IIF subunit 1|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211231|||http://purl.uniprot.org/annotation/VAR_039004
http://togogenome.org/gene/9606:COPG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y678                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coatomer subunit gamma-1|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Interaction with ZNF289/ARFGAP2|||Loss of interaction with ZNF289/ARFGAP2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193858|||http://purl.uniprot.org/annotation/VAR_054039
http://togogenome.org/gene/9606:CNRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F85                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CB1 cannabinoid receptor-interacting protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089360|||http://purl.uniprot.org/annotation/VSP_035598
http://togogenome.org/gene/9606:XRCC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13010                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PRKDC and its recruitment to sites of DNA damage.|||EEXXXDL motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Ku|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine|||Phosphothreonine; by PRKDC|||Removed|||X-ray repair cross-complementing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084340|||http://purl.uniprot.org/annotation/VAR_014724|||http://purl.uniprot.org/annotation/VAR_053784
http://togogenome.org/gene/9606:RBFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0V3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondrion|||Putative ribosome-binding factor A, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030226|||http://purl.uniprot.org/annotation/VAR_023233|||http://purl.uniprot.org/annotation/VAR_023234|||http://purl.uniprot.org/annotation/VAR_023235|||http://purl.uniprot.org/annotation/VSP_015118|||http://purl.uniprot.org/annotation/VSP_015119
http://togogenome.org/gene/9606:UBASH3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57075                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to dynamin.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of interaction with CBL.|||Phosphatase-like|||SH3|||UBA|||Ubiquitin-associated and SH3 domain-containing protein A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210994|||http://purl.uniprot.org/annotation/VAR_026971|||http://purl.uniprot.org/annotation/VAR_026972|||http://purl.uniprot.org/annotation/VAR_026973|||http://purl.uniprot.org/annotation/VAR_052675|||http://purl.uniprot.org/annotation/VAR_061921|||http://purl.uniprot.org/annotation/VAR_061922|||http://purl.uniprot.org/annotation/VSP_006703|||http://purl.uniprot.org/annotation/VSP_045549|||http://purl.uniprot.org/annotation/VSP_045550
http://togogenome.org/gene/9606:CBLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUK8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Cerebellin-2|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003551
http://togogenome.org/gene/9606:A1BG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04217|||http://purl.uniprot.org/uniprot/V9HWD8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alpha-1B-glycoprotein|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||Ig-like V-type 3|||Ig-like V-type 4|||Ig-like V-type 5|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014502|||http://purl.uniprot.org/annotation/PRO_5004776942|||http://purl.uniprot.org/annotation/VAR_018369|||http://purl.uniprot.org/annotation/VAR_018370|||http://purl.uniprot.org/annotation/VSP_040323
http://togogenome.org/gene/9606:PTGES3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PB15                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  CS|||Disordered|||In isoform 4.|||In isoform 5.|||Putative protein PTGES3L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000418440|||http://purl.uniprot.org/annotation/VSP_060622|||http://purl.uniprot.org/annotation/VSP_060623|||http://purl.uniprot.org/annotation/VSP_060624
http://togogenome.org/gene/9606:TMEM177                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53S58                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 177                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282646|||http://purl.uniprot.org/annotation/VAR_031421|||http://purl.uniprot.org/annotation/VAR_031422|||http://purl.uniprot.org/annotation/VAR_031423
http://togogenome.org/gene/9606:NDUFB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95169                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC1DN32.|||In MC1DN32; due to a nucleotide substitution that results in exon 4 skipping or in missense variant W-144; patient cells contain both type of transcripts; transcript lacking exon 4 is the most abundant.|||In MC1DN32; due to a nucleotide substitution that results in exon 4 skipping or missense variant W-144; patient cells contain both type of transcripts; transcript with the missense variant is the less abundant.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020046|||http://purl.uniprot.org/annotation/VAR_081466|||http://purl.uniprot.org/annotation/VAR_081467|||http://purl.uniprot.org/annotation/VAR_081468|||http://purl.uniprot.org/annotation/VAR_081469|||http://purl.uniprot.org/annotation/VSP_054842|||http://purl.uniprot.org/annotation/VSP_054843|||http://purl.uniprot.org/annotation/VSP_054844
http://togogenome.org/gene/9606:MBTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BQ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FCS-type|||Impaired interaction with EPC1. Abolished interaction with EPC1; when associated with 259-G--G-263.|||Impaired interaction with EPC1. Abolished interaction with EPC1; when associated with G-236.|||Impaired interaction with EPC1; when associated with 259-D--D-263.|||Impaired interaction with EPC1; when associated with D-236.|||In isoform 2.|||In isoform 3.|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||MBT domain-containing protein 1|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313717|||http://purl.uniprot.org/annotation/VSP_030115|||http://purl.uniprot.org/annotation/VSP_030118|||http://purl.uniprot.org/annotation/VSP_042701|||http://purl.uniprot.org/annotation/VSP_042702
http://togogenome.org/gene/9606:CD200R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD46                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell surface glycoprotein CD200 receptor 1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 1 and isoform 3.|||In isoform 2 and isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015128|||http://purl.uniprot.org/annotation/VAR_014352|||http://purl.uniprot.org/annotation/VAR_014353|||http://purl.uniprot.org/annotation/VAR_014354|||http://purl.uniprot.org/annotation/VAR_031022|||http://purl.uniprot.org/annotation/VSP_061888|||http://purl.uniprot.org/annotation/VSP_061889|||http://purl.uniprot.org/annotation/VSP_061890
http://togogenome.org/gene/9606:SCFD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU76                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Sec1 family domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206290|||http://purl.uniprot.org/annotation/VAR_024687|||http://purl.uniprot.org/annotation/VSP_010710
http://togogenome.org/gene/9606:CHORDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CHORD 1|||CHORD 2|||CS|||Cysteine and histidine-rich domain-containing protein 1|||In isoform 2.|||Interaction with HSP90AA1 and HSP90AB1|||Interaction with PPP5C|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317770|||http://purl.uniprot.org/annotation/VAR_038676|||http://purl.uniprot.org/annotation/VSP_031150
http://togogenome.org/gene/9606:TMPRSS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU80                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Does not undergo proteolytic processing.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In IRIDA.|||In IRIDA; does not undergo proteolytic processing; loss of activity.|||In IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on catalytic activity; autoproteolytic and HJV processing are not affected.|||In IRIDA; no effect on HJV-mediated inhibition of HAMP transcription; no effect on localization to the cell membrane; no effect on catalytic activity; HJV processing is not affected.|||In IRIDA; reduced HJV-mediated inhibition of HAMP transcription; does not undergo proteolytic processing; impaired localization to the cell membrane; able to interact with HJV.|||In IRIDA; reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are impaired.|||In IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; altered catalytic activity; autoproteolytic processing is reduced but it retains the ability to process HJV; able to interact with HJV.|||In IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; loss of catalytic activity; no ability to process HJV.|||In IRIDA; reduced HJV-mediated inhibition of HAMP transcription; reduced localization to the cell membrane; no effect on catalytic activity.|||In IRIDA; reduced expression at the cell surface; partially retained in the Golgi apparatus; does not undergo proteolytic processing; able to interact with HJV; results in reduced inhibition of HAMP promoter.|||In IRIDA; reduced proteolytic processing; reduced expression to plasma membrane; does not affect binding to HJV.|||In IRIDA; results in reduced inhibition of HAMP promoter.|||In IRIDA; severely reduced proteolytic processing; loss of activity.|||In IRIDA; slightly reduced HJV-mediated inhibition of HAMP transcription; loss of catalytic activity; autoproteolytic and HJV processing are significantly reduced.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088696|||http://purl.uniprot.org/annotation/VAR_036296|||http://purl.uniprot.org/annotation/VAR_036297|||http://purl.uniprot.org/annotation/VAR_044434|||http://purl.uniprot.org/annotation/VAR_044435|||http://purl.uniprot.org/annotation/VAR_044436|||http://purl.uniprot.org/annotation/VAR_044437|||http://purl.uniprot.org/annotation/VAR_051841|||http://purl.uniprot.org/annotation/VAR_051842|||http://purl.uniprot.org/annotation/VAR_051843|||http://purl.uniprot.org/annotation/VAR_051844|||http://purl.uniprot.org/annotation/VAR_064075|||http://purl.uniprot.org/annotation/VAR_064076|||http://purl.uniprot.org/annotation/VAR_064077|||http://purl.uniprot.org/annotation/VAR_064078|||http://purl.uniprot.org/annotation/VAR_064079|||http://purl.uniprot.org/annotation/VAR_068665|||http://purl.uniprot.org/annotation/VAR_068666|||http://purl.uniprot.org/annotation/VAR_068667|||http://purl.uniprot.org/annotation/VAR_068668|||http://purl.uniprot.org/annotation/VAR_068669|||http://purl.uniprot.org/annotation/VAR_068670|||http://purl.uniprot.org/annotation/VAR_068671|||http://purl.uniprot.org/annotation/VAR_068672|||http://purl.uniprot.org/annotation/VAR_068673|||http://purl.uniprot.org/annotation/VAR_068674|||http://purl.uniprot.org/annotation/VAR_068675|||http://purl.uniprot.org/annotation/VAR_072901|||http://purl.uniprot.org/annotation/VAR_072902|||http://purl.uniprot.org/annotation/VAR_072903|||http://purl.uniprot.org/annotation/VAR_072904|||http://purl.uniprot.org/annotation/VAR_072905|||http://purl.uniprot.org/annotation/VAR_072906|||http://purl.uniprot.org/annotation/VAR_072907|||http://purl.uniprot.org/annotation/VAR_072908|||http://purl.uniprot.org/annotation/VAR_072909|||http://purl.uniprot.org/annotation/VAR_072910|||http://purl.uniprot.org/annotation/VSP_008379|||http://purl.uniprot.org/annotation/VSP_008380|||http://purl.uniprot.org/annotation/VSP_035562|||http://purl.uniprot.org/annotation/VSP_035563
http://togogenome.org/gene/9606:ADAM28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKT9|||http://purl.uniprot.org/uniprot/Q9UKQ2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 28|||Disordered|||EGF-like|||Extracellular|||Helical|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029128|||http://purl.uniprot.org/annotation/PRO_0000029129|||http://purl.uniprot.org/annotation/PRO_5036073200|||http://purl.uniprot.org/annotation/VAR_024596|||http://purl.uniprot.org/annotation/VAR_057067|||http://purl.uniprot.org/annotation/VAR_057068|||http://purl.uniprot.org/annotation/VAR_057069|||http://purl.uniprot.org/annotation/VAR_057070|||http://purl.uniprot.org/annotation/VAR_057071|||http://purl.uniprot.org/annotation/VAR_057072|||http://purl.uniprot.org/annotation/VAR_066317|||http://purl.uniprot.org/annotation/VAR_066318|||http://purl.uniprot.org/annotation/VAR_066319|||http://purl.uniprot.org/annotation/VAR_066320|||http://purl.uniprot.org/annotation/VAR_066321|||http://purl.uniprot.org/annotation/VSP_005486|||http://purl.uniprot.org/annotation/VSP_005487
http://togogenome.org/gene/9606:PARP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR21                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl aspartic acid|||ADP-ribosyl glutamic acid|||ADP-ribosylcysteine|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of subcellular location at the nuclear envelope.|||N6-(ADP-ribosyl)lysine|||No effect on subcellular location at the nuclear envelope.|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP11|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273419|||http://purl.uniprot.org/annotation/VSP_059435|||http://purl.uniprot.org/annotation/VSP_059436|||http://purl.uniprot.org/annotation/VSP_059437|||http://purl.uniprot.org/annotation/VSP_059438|||http://purl.uniprot.org/annotation/VSP_059439
http://togogenome.org/gene/9606:ZNF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17021                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047339|||http://purl.uniprot.org/annotation/VAR_057382|||http://purl.uniprot.org/annotation/VSP_036651|||http://purl.uniprot.org/annotation/VSP_036652
http://togogenome.org/gene/9606:INPP5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMW4|||http://purl.uniprot.org/uniprot/P32019                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  5-phosphatase|||ASH|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of prenylation and membrane localization.|||PH|||Polar residues|||Removed in mature form|||Rho-GAP|||S-farnesyl cysteine|||Type II inositol 1,4,5-trisphosphate 5-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015640|||http://purl.uniprot.org/annotation/PRO_0000422293|||http://purl.uniprot.org/annotation/VAR_028002|||http://purl.uniprot.org/annotation/VAR_061270|||http://purl.uniprot.org/annotation/VSP_012820|||http://purl.uniprot.org/annotation/VSP_012821|||http://purl.uniprot.org/annotation/VSP_013902|||http://purl.uniprot.org/annotation/VSP_013903
http://togogenome.org/gene/9606:ST6GAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15907                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-galactoside alpha-2,6-sialyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on dimerization and on location at the Golgi stack.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149249|||http://purl.uniprot.org/annotation/VSP_056076
http://togogenome.org/gene/9606:PXMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR77                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Peroxisomal|||Peroxisomal membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218929
http://togogenome.org/gene/9606:BLTP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JNW5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with STX6. No effect on early endosome location.|||Bridge-like lipid transfer protein family member 3B|||Chorein N-terminal|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295719|||http://purl.uniprot.org/annotation/VAR_051467|||http://purl.uniprot.org/annotation/VAR_051468|||http://purl.uniprot.org/annotation/VAR_061719|||http://purl.uniprot.org/annotation/VSP_027014|||http://purl.uniprot.org/annotation/VSP_027015
http://togogenome.org/gene/9606:LAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of interaction with Lassa virus protein GPC.|||Cytoplasmic|||Disordered|||First lumenal domain|||Helical|||Hinge|||In isoform 2.|||Lumenal|||Lysosome-associated membrane glycoprotein 1|||N-linked (GlcNAc...) (polylactosaminoglycan) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine|||Pro residues|||Second lumenal domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017104|||http://purl.uniprot.org/annotation/VAR_046450|||http://purl.uniprot.org/annotation/VSP_056032
http://togogenome.org/gene/9606:LILRB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSZ8|||http://purl.uniprot.org/uniprot/A0A8Q3SHR1|||http://purl.uniprot.org/uniprot/Q8NHJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||Leukocyte immunoglobulin-like receptor subfamily B member 4|||No significant change in APOE-mediated activation of LILRB4.|||Phosphoserine|||Polar residues|||Required for APOE-mediated activation of LILRB4|||Significant reduction in APOE-mediated activation of LILRB4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014823|||http://purl.uniprot.org/annotation/PRO_5001974217|||http://purl.uniprot.org/annotation/PRO_5035886238|||http://purl.uniprot.org/annotation/VAR_017014|||http://purl.uniprot.org/annotation/VAR_017015|||http://purl.uniprot.org/annotation/VAR_025501|||http://purl.uniprot.org/annotation/VAR_025502|||http://purl.uniprot.org/annotation/VAR_025503|||http://purl.uniprot.org/annotation/VAR_025504|||http://purl.uniprot.org/annotation/VAR_025505|||http://purl.uniprot.org/annotation/VAR_030939|||http://purl.uniprot.org/annotation/VAR_047846|||http://purl.uniprot.org/annotation/VSP_008460|||http://purl.uniprot.org/annotation/VSP_035939
http://togogenome.org/gene/9606:CCDC60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWA6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 60|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239665|||http://purl.uniprot.org/annotation/VAR_033667|||http://purl.uniprot.org/annotation/VAR_033668|||http://purl.uniprot.org/annotation/VAR_033669
http://togogenome.org/gene/9606:PDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20941|||http://purl.uniprot.org/uniprot/Q52LP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosducin|||Phosducin thioredoxin-like|||Phosphoserine; by PKA|||Thioredoxin fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163752|||http://purl.uniprot.org/annotation/VSP_043880|||http://purl.uniprot.org/annotation/VSP_053778
http://togogenome.org/gene/9606:ATAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T9B4|||http://purl.uniprot.org/uniprot/A0A7P0T9U2|||http://purl.uniprot.org/uniprot/Q8NBU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||ATPase AAA-type core|||Cytoplasmic|||Helical|||In HKPX4; severely decreased ATAD1 mRNA expression in lymphoblastoid cells derived from the patient compared to an unaffected control.|||In HKPX4; unknown pathological significance; likely affects splicing due to removal of the splice donor site of intron 2.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Mitochondrial intermembrane|||Outer mitochondrial transmembrane helix translocase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084791|||http://purl.uniprot.org/annotation/VAR_035903|||http://purl.uniprot.org/annotation/VAR_080830|||http://purl.uniprot.org/annotation/VAR_080831|||http://purl.uniprot.org/annotation/VSP_037304
http://togogenome.org/gene/9606:SLC7A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z502|||http://purl.uniprot.org/uniprot/Q9UM01                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In LPI.|||In LPI; failed to induce cationic amino acid transport activity.|||In LPI; failed to induce sodium-independent cationic amino acid and sodium-dependent neutral amino acid transport activity.|||In LPI; failed to induce sodium-independent cationic amino acid and sodium-dependent neutral amino acid transport activity; does not affect heterodimerization with SLC3A2; affects expression level.|||In LPI; moderately reduced cationic amino acid transport activity.|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Y+L amino acid transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054281|||http://purl.uniprot.org/annotation/VAR_010261|||http://purl.uniprot.org/annotation/VAR_010262|||http://purl.uniprot.org/annotation/VAR_010999|||http://purl.uniprot.org/annotation/VAR_011000|||http://purl.uniprot.org/annotation/VAR_030595|||http://purl.uniprot.org/annotation/VAR_030596|||http://purl.uniprot.org/annotation/VAR_030597|||http://purl.uniprot.org/annotation/VAR_030598|||http://purl.uniprot.org/annotation/VAR_030599|||http://purl.uniprot.org/annotation/VAR_036609|||http://purl.uniprot.org/annotation/VAR_039092|||http://purl.uniprot.org/annotation/VAR_039093|||http://purl.uniprot.org/annotation/VAR_039094|||http://purl.uniprot.org/annotation/VAR_039095|||http://purl.uniprot.org/annotation/VAR_039096|||http://purl.uniprot.org/annotation/VAR_039097|||http://purl.uniprot.org/annotation/VAR_039098|||http://purl.uniprot.org/annotation/VAR_039099|||http://purl.uniprot.org/annotation/VAR_039100|||http://purl.uniprot.org/annotation/VAR_039101|||http://purl.uniprot.org/annotation/VAR_039102|||http://purl.uniprot.org/annotation/VAR_039103
http://togogenome.org/gene/9606:POLD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSD7|||http://purl.uniprot.org/uniprot/Q9HCU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of PCNA binding and of degradation after UV irradiation.|||Complete loss of PCNA binding.|||Complete loss of PCNA binding; when associated with 10-AA-11.|||Complete loss of PCNA binding; when associated with A-7.|||DNA polymerase delta subunit 4|||Decreased PCNA binding. No effect on PCNA binding, but normal degradation after UV irradiation; when associated with Q-4 and Y-10. Increased stability following UV irradiation and no trough during S phase; when associated with A-16 and A-17.|||Disordered|||In isoform 2.|||Increased stability following UV irradiation and no trough during S phase; when associated with A-15 and A-16.|||Increased stability following UV irradiation and no trough during S phase; when associated with A-15 and A-17.|||No effect on PCNA binding, nor on degradation after UV irradiation; when associated with Q-4. No effect on PCNA binding, but normal degradation after UV irradiation with Q-4 and A-15.|||No effect on PCNA binding, nor on degradation after UV irradiation; when associated with Y-10. No effect on PCNA binding, but normal degradation after UV irradiation; when associated with Y-10 and A-15.|||No effect on PCNA binding.|||No effect on ubiquitination. Loss of ubiquitination, when associated with R-15, R-25, R-74 and R-89.|||No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-25 and R-74.|||No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-25 and R-89.|||No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-74 and R-89.|||No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-25, R-74 and R-89.|||PCNA-interaction protein motif (PIP box)|||Strongly increased stability following UV irradiation; when associated with A-8.|||Strongly increased stability following UV irradiation; when associated with A-9.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186051|||http://purl.uniprot.org/annotation/VAR_022269|||http://purl.uniprot.org/annotation/VAR_057526|||http://purl.uniprot.org/annotation/VSP_046864
http://togogenome.org/gene/9606:ERP44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEE7|||http://purl.uniprot.org/uniprot/Q9BS26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Endoplasmic reticulum resident protein 44|||Interaction with ITPR1|||Interchain (with ERO1A)|||Polar residues|||Prevents secretion from ER|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034180|||http://purl.uniprot.org/annotation/PRO_5035402821
http://togogenome.org/gene/9606:SVIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Removed|||Small VCP/p97-interacting protein|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072337
http://togogenome.org/gene/9606:ZNF679                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYX0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 679                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233999|||http://purl.uniprot.org/annotation/VAR_033586|||http://purl.uniprot.org/annotation/VAR_033587|||http://purl.uniprot.org/annotation/VAR_033588|||http://purl.uniprot.org/annotation/VAR_033589
http://togogenome.org/gene/9606:CPNE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z370|||http://purl.uniprot.org/uniprot/Q4G168|||http://purl.uniprot.org/uniprot/Q96A23                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Copine C-terminal|||Copine-4|||In isoform 2.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144841|||http://purl.uniprot.org/annotation/VSP_001214
http://togogenome.org/gene/9606:P3H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVL5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fe2OG dioxygenase|||In MCVD; loss of function.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Prolyl 3-hydroxylase 2|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240356|||http://purl.uniprot.org/annotation/VAR_036123|||http://purl.uniprot.org/annotation/VAR_066637|||http://purl.uniprot.org/annotation/VSP_053814
http://togogenome.org/gene/9606:RALGAPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUI1|||http://purl.uniprot.org/uniprot/A0A7P0TAR5|||http://purl.uniprot.org/uniprot/H0YJB5|||http://purl.uniprot.org/uniprot/Q6GYQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Has no effect on interaction with RALGAPB but causes loss of activity.|||In NEDHRIT.|||In NEDHRIT; undetectable protein expression.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||Minimal domain that binds to TCF3/E12|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ral GTPase-activating protein subunit alpha-1|||Rap-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056753|||http://purl.uniprot.org/annotation/VAR_019804|||http://purl.uniprot.org/annotation/VAR_083728|||http://purl.uniprot.org/annotation/VAR_083729|||http://purl.uniprot.org/annotation/VAR_083730|||http://purl.uniprot.org/annotation/VAR_083731|||http://purl.uniprot.org/annotation/VSP_011324|||http://purl.uniprot.org/annotation/VSP_011325|||http://purl.uniprot.org/annotation/VSP_011326|||http://purl.uniprot.org/annotation/VSP_011327|||http://purl.uniprot.org/annotation/VSP_011328|||http://purl.uniprot.org/annotation/VSP_011329|||http://purl.uniprot.org/annotation/VSP_054485
http://togogenome.org/gene/9606:NOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGA6|||http://purl.uniprot.org/uniprot/Q1ZYL4|||http://purl.uniprot.org/uniprot/Q9Y5S8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced basal and phorbol ester-stimulated ROS generation, which may decrease resistance to infection by enteric pathogens, such as Campylobacter jejuni.|||Helical|||In isoform NOH-1LV.|||In isoform NOH-1S.|||Interaction with NOXO1|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 1|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210148|||http://purl.uniprot.org/annotation/VAR_049101|||http://purl.uniprot.org/annotation/VAR_049102|||http://purl.uniprot.org/annotation/VAR_061176|||http://purl.uniprot.org/annotation/VAR_075548|||http://purl.uniprot.org/annotation/VSP_001577|||http://purl.uniprot.org/annotation/VSP_001578|||http://purl.uniprot.org/annotation/VSP_001579
http://togogenome.org/gene/9606:TUBB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13509|||http://purl.uniprot.org/uniprot/Q53G92                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Acidic residues|||Disordered|||In CDCBM1; can form tubulin heterodimers that are properly incorporated into microtubules; the microtubules are less stable than wild-type.|||In CDCBM1; does not form tubulin heterodimers.|||In CDCBM1; does not form tubulin heterodimers; patient fibroblasts show no major alterations in the microtubule network, but the microtubules are less stable than wild-type.|||In CDCBM1; reduced heterodimers formation.|||In CFEOM3A; affects heterodimers formation; affects microtubules polymerization and depolymerization rates.|||In CFEOM3A; affects heterodimers formation; results in increased stability and reduced dynamics of microtubules.|||In CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures.|||In CFEOM3A; severe phenotype with congenital facial weakness, congenital wrist and finger contractures; affects microtubules polymerization and depolymerization rates.|||In CFEOM3A; severe phenotype with congenital facial weakness; lower extremity weakness and sensory loss in the second to third decade of life in one patient; affects microtubules polymerization and depolymerization rates.|||In CFEOM3A; some patients with lower extremity weakness and sensory loss in the second to third decade of life; also found in patients without CFEOM3A who developed polyneuropathy.|||In isoform 2.|||MREI motif|||Phosphoserine|||Phosphoserine; by CDK1|||Tubulin beta-3 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048250|||http://purl.uniprot.org/annotation/VAR_062758|||http://purl.uniprot.org/annotation/VAR_062759|||http://purl.uniprot.org/annotation/VAR_062760|||http://purl.uniprot.org/annotation/VAR_062761|||http://purl.uniprot.org/annotation/VAR_062762|||http://purl.uniprot.org/annotation/VAR_062763|||http://purl.uniprot.org/annotation/VAR_062764|||http://purl.uniprot.org/annotation/VAR_062765|||http://purl.uniprot.org/annotation/VAR_066206|||http://purl.uniprot.org/annotation/VAR_066207|||http://purl.uniprot.org/annotation/VAR_066208|||http://purl.uniprot.org/annotation/VAR_066209|||http://purl.uniprot.org/annotation/VSP_054659
http://togogenome.org/gene/9606:LAMTOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IAA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished N-myristoylation and subsequent palmitoylation.|||Abolished palmitoylation and recruitment to lysosomes, leading to impaired activation of the mTORC1 complex.|||Basic and acidic residues|||Decreased palmitoylation.|||Disordered|||Does not affect interaction with RRAGA and RRAGC in vitro.|||Does not affect interaction with ZDHHC3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired assembly of the Ragulator complex.|||Impaired recruiment of Rag GTPases (RRAGA and RRAGC) to the lysosomal membrane.|||Interaction with LAMTOR2 and LAMTOR3|||N-myristoyl glycine|||Phosphoserine|||Ragulator complex protein LAMTOR1|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274292|||http://purl.uniprot.org/annotation/VAR_030250
http://togogenome.org/gene/9606:XBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17861                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Cleavage; by HM13/SPP|||Cytoplasmic|||Disordered|||Does not induce glycosylation.|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increases translational pausing of its own mRNA.|||Induces glycosylation.|||Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-200.|||Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-203.|||Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-200 and L-203.|||Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-199; L-200 and L-203.|||Leucine-zipper|||Lumenal|||Necessary for the translational pausing of its own mRNA|||Nuclear localization signal (NLS); in isoforms 1 and isoform 2|||Phosphoserine|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with D-198 and E-205.|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and D-196.|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and E-193.|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-193 and D-196.|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and D-198.|||Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and E-205.|||Reduces translational pausing, membrane targeting and cytoplasmic splicing of its own mRNA.|||X-box-binding protein 1|||X-box-binding protein 1, cytoplasmic form|||X-box-binding protein 1, luminal form|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076543|||http://purl.uniprot.org/annotation/PRO_0000431891|||http://purl.uniprot.org/annotation/PRO_0000431892|||http://purl.uniprot.org/annotation/VAR_033023|||http://purl.uniprot.org/annotation/VAR_035998|||http://purl.uniprot.org/annotation/VSP_012936
http://togogenome.org/gene/9606:ZNF251                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRH9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 251                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047485
http://togogenome.org/gene/9606:CNPY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2B0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Prevents secretion from ER|||Protein canopy homolog 2|||Saposin B-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031666|||http://purl.uniprot.org/annotation/VSP_010884|||http://purl.uniprot.org/annotation/VSP_010885
http://togogenome.org/gene/9606:ALDH1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75891|||http://purl.uniprot.org/uniprot/Q53H87                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase domain|||Carrier|||Cytosolic 10-formyltetrahydrofolate dehydrogenase|||Essential for catalytic activity|||Hydrolase domain|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity.|||N6-acetyllysine|||N6-succinyllysine|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199419|||http://purl.uniprot.org/annotation/VAR_036101|||http://purl.uniprot.org/annotation/VAR_052290|||http://purl.uniprot.org/annotation/VAR_052291|||http://purl.uniprot.org/annotation/VAR_052292|||http://purl.uniprot.org/annotation/VAR_052293|||http://purl.uniprot.org/annotation/VAR_052295|||http://purl.uniprot.org/annotation/VAR_052296|||http://purl.uniprot.org/annotation/VAR_052297|||http://purl.uniprot.org/annotation/VAR_052298|||http://purl.uniprot.org/annotation/VAR_052299|||http://purl.uniprot.org/annotation/VSP_045569|||http://purl.uniprot.org/annotation/VSP_047260|||http://purl.uniprot.org/annotation/VSP_057429|||http://purl.uniprot.org/annotation/VSP_057430
http://togogenome.org/gene/9606:SASH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94885                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with TRAF6.|||Basic and acidic residues|||Disordered|||In CAPOK; affects the regulation of cell mobility; patient fibroblasts migrate better than control fibroblasts.|||In DUH1.|||In DUH1; affects the regulation of cell mobility resulting in increased melanocyte migration; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability.|||In DUH1; increased interaction with GNAS; increased interaction with IQGAP1; increased protein levels; increased protein stability.|||In DUH1; unknown pathological significance.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with TRAF6|||SAM 1|||SAM 2|||SAM and SH3 domain-containing protein 1|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097597|||http://purl.uniprot.org/annotation/VAR_031714|||http://purl.uniprot.org/annotation/VAR_031715|||http://purl.uniprot.org/annotation/VAR_082102|||http://purl.uniprot.org/annotation/VAR_082103|||http://purl.uniprot.org/annotation/VAR_082104|||http://purl.uniprot.org/annotation/VAR_082105|||http://purl.uniprot.org/annotation/VAR_082106|||http://purl.uniprot.org/annotation/VAR_082107|||http://purl.uniprot.org/annotation/VAR_082108|||http://purl.uniprot.org/annotation/VAR_082109|||http://purl.uniprot.org/annotation/VAR_082110
http://togogenome.org/gene/9606:WDR13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1Z4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine; alternate|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051361|||http://purl.uniprot.org/annotation/VAR_060284|||http://purl.uniprot.org/annotation/VSP_054010
http://togogenome.org/gene/9606:ZDHHC23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PRJ8|||http://purl.uniprot.org/uniprot/B3KXV3|||http://purl.uniprot.org/uniprot/E9PAP7|||http://purl.uniprot.org/uniprot/Q8IYP9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC23|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212912|||http://purl.uniprot.org/annotation/VAR_047389|||http://purl.uniprot.org/annotation/VAR_047390|||http://purl.uniprot.org/annotation/VAR_047391|||http://purl.uniprot.org/annotation/VAR_047392
http://togogenome.org/gene/9606:MPV17L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2QL34                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Mpv17-like protein|||Targeting to peroxisomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333178|||http://purl.uniprot.org/annotation/VSP_033462|||http://purl.uniprot.org/annotation/VSP_033463
http://togogenome.org/gene/9606:DENND10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IRE4|||http://purl.uniprot.org/uniprot/B4DMU4|||http://purl.uniprot.org/uniprot/B4DNL9|||http://purl.uniprot.org/uniprot/Q8TCE6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  DENN domain-containing protein 10|||In isoform 2.|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187034|||http://purl.uniprot.org/annotation/PRO_5002803726|||http://purl.uniprot.org/annotation/VSP_038301
http://togogenome.org/gene/9606:OR51G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGK0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150755|||http://purl.uniprot.org/annotation/VAR_034319|||http://purl.uniprot.org/annotation/VAR_053327
http://togogenome.org/gene/9606:SRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Pro residues|||Steroid receptor RNA activator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234105|||http://purl.uniprot.org/annotation/VAR_052060
http://togogenome.org/gene/9606:POMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y244                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Motif                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||High-affinity association with the preproteasome|||Proteasome maturation protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247184
http://togogenome.org/gene/9606:GPRIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVF9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G protein-regulated inducer of neurite outgrowth 3|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251950|||http://purl.uniprot.org/annotation/VAR_051019|||http://purl.uniprot.org/annotation/VAR_051020|||http://purl.uniprot.org/annotation/VAR_051021|||http://purl.uniprot.org/annotation/VAR_051022|||http://purl.uniprot.org/annotation/VAR_051023|||http://purl.uniprot.org/annotation/VAR_051024
http://togogenome.org/gene/9606:PTH2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFN8|||http://purl.uniprot.org/uniprot/P49190                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Parathyroid hormone 2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012849
http://togogenome.org/gene/9606:TDRD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHU6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||HTH OST-type 1|||HTH OST-type 2|||HTH OST-type 3|||In CTRCT36.|||In isoform 2.|||In isoform 3.|||Interaction with CABLES1|||Interaction with CDK17|||Phosphoserine|||Tudor 1|||Tudor 2|||Tudor domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183169|||http://purl.uniprot.org/annotation/VAR_019070|||http://purl.uniprot.org/annotation/VAR_033044|||http://purl.uniprot.org/annotation/VAR_065247|||http://purl.uniprot.org/annotation/VSP_041314|||http://purl.uniprot.org/annotation/VSP_041315|||http://purl.uniprot.org/annotation/VSP_041316
http://togogenome.org/gene/9606:RGS19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP94|||http://purl.uniprot.org/uniprot/P49795                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells.|||Disordered|||Interaction with GIPC|||Phosphoserine|||Phosphoserine; by MAPK1 and MAPK3|||RGS|||Regulator of G-protein signaling 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204229
http://togogenome.org/gene/9606:BCL2L12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0X8ASA9|||http://purl.uniprot.org/uniprot/A0A0X8AT42|||http://purl.uniprot.org/uniprot/I6LJZ5|||http://purl.uniprot.org/uniprot/I6LJZ6|||http://purl.uniprot.org/uniprot/I6LJZ8|||http://purl.uniprot.org/uniprot/M0R1K0|||http://purl.uniprot.org/uniprot/Q9HB09                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BH2|||Bcl-2-like protein 12|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143072|||http://purl.uniprot.org/annotation/VAR_048419|||http://purl.uniprot.org/annotation/VSP_000522|||http://purl.uniprot.org/annotation/VSP_000523|||http://purl.uniprot.org/annotation/VSP_043269
http://togogenome.org/gene/9606:FKBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13451|||http://purl.uniprot.org/uniprot/Q2TA84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased acetylation; promotes interaction with AKT1 and PHLPP1; when associated with R-155.|||Decreased acetylation; promotes interaction with AKT1 and PHLPP1; when associated with R-28.|||Disordered|||In isoform 2.|||Mimics acetylation; impaired interaction with AKT1 and PHLPP1; when associated with Q-155.|||Mimics acetylation; impaired interaction with AKT1 and PHLPP1; when associated with Q-28.|||N-acetylmethionine|||N6-acetyllysine|||PPIase FKBP-type|||PPIase FKBP-type 1|||PPIase FKBP-type 2|||Peptidyl-prolyl cis-trans isomerase FKBP5|||Phosphoserine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075324|||http://purl.uniprot.org/annotation/VSP_044820|||http://purl.uniprot.org/annotation/VSP_044821
http://togogenome.org/gene/9606:OR2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW34|||http://purl.uniprot.org/uniprot/Q8NH16                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150486|||http://purl.uniprot.org/annotation/VAR_053144|||http://purl.uniprot.org/annotation/VAR_053145
http://togogenome.org/gene/9606:THY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJA4|||http://purl.uniprot.org/uniprot/P04216                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Alternate|||GPI-anchor amidated cysteine; alternate|||Ig-like|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pyrrolidone carboxylic acid|||Removed in mature form|||Thy-1 membrane glycoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014973|||http://purl.uniprot.org/annotation/PRO_0000014974|||http://purl.uniprot.org/annotation/PRO_5014298166
http://togogenome.org/gene/9606:TMEM60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2L4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 60                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072581|||http://purl.uniprot.org/annotation/VAR_051449
http://togogenome.org/gene/9606:SESN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6P5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||In isoform T1.|||In isoform T3.|||Loss of the ability to decrease intracellular reactive oxygen species.|||N-terminal domain; may mediate the alkylhydroperoxide reductase activity|||Phosphoserine|||Sestrin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221178|||http://purl.uniprot.org/annotation/VAR_014210|||http://purl.uniprot.org/annotation/VSP_006059|||http://purl.uniprot.org/annotation/VSP_006060
http://togogenome.org/gene/9606:CCDC73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRK6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 73|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285294|||http://purl.uniprot.org/annotation/VSP_024861|||http://purl.uniprot.org/annotation/VSP_024862|||http://purl.uniprot.org/annotation/VSP_024863
http://togogenome.org/gene/9606:MEGF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7M0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||Extracellular|||Helical|||In CRPT2.|||In isoform 2.|||Kelch 1|||Kelch 10|||Kelch 11|||Kelch 12|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch 7|||Kelch 8|||Kelch 9|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Multiple epidermal growth factor-like domains protein 8|||N-linked (GlcNAc...) asparagine|||PSI 1|||PSI 2|||PSI 3|||PSI 4|||PSI 5|||PSI 6|||PSI 7|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055629|||http://purl.uniprot.org/annotation/VAR_069305|||http://purl.uniprot.org/annotation/VAR_069306|||http://purl.uniprot.org/annotation/VAR_069307|||http://purl.uniprot.org/annotation/VSP_036067
http://togogenome.org/gene/9606:TMEM167A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBQ9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein kish-A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247768
http://togogenome.org/gene/9606:SLC9A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBY0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sodium/hydrogen exchanger 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052352|||http://purl.uniprot.org/annotation/VAR_035964|||http://purl.uniprot.org/annotation/VAR_035965
http://togogenome.org/gene/9606:CEP89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ST8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 89 kDa|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288809|||http://purl.uniprot.org/annotation/VAR_063122|||http://purl.uniprot.org/annotation/VAR_063123|||http://purl.uniprot.org/annotation/VSP_039181|||http://purl.uniprot.org/annotation/VSP_039182|||http://purl.uniprot.org/annotation/VSP_039183
http://togogenome.org/gene/9606:CFAP57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVY5|||http://purl.uniprot.org/uniprot/Q96MR6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 57|||In isoform 2.|||Rare variant found in a patient with Van der Woude syndrome; unknown pathological significance.|||WD|||WD 1|||WD 10|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242653|||http://purl.uniprot.org/annotation/VAR_026850|||http://purl.uniprot.org/annotation/VAR_026851|||http://purl.uniprot.org/annotation/VAR_026852|||http://purl.uniprot.org/annotation/VAR_066494|||http://purl.uniprot.org/annotation/VSP_039520|||http://purl.uniprot.org/annotation/VSP_039521
http://togogenome.org/gene/9606:SFTPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  4-hydroxyproline|||C-type lectin|||Collagen-like|||Disordered|||In ILD2; impaired secretion.|||In ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted.|||In ILD2; unknown pathological significance; impaired secretion.|||In allele 1A(0).|||In allele 1A(1), allele 1A(3) and allele 1A(4).|||In allele 1A.|||Interchain|||N-linked (GlcNAc...) asparagine|||Pro residues|||Pulmonary surfactant-associated protein A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017458|||http://purl.uniprot.org/annotation/VAR_021293|||http://purl.uniprot.org/annotation/VAR_021294|||http://purl.uniprot.org/annotation/VAR_021295|||http://purl.uniprot.org/annotation/VAR_021296|||http://purl.uniprot.org/annotation/VAR_063518|||http://purl.uniprot.org/annotation/VAR_063519|||http://purl.uniprot.org/annotation/VAR_063520|||http://purl.uniprot.org/annotation/VAR_086122|||http://purl.uniprot.org/annotation/VAR_086123|||http://purl.uniprot.org/annotation/VAR_086124|||http://purl.uniprot.org/annotation/VAR_086125|||http://purl.uniprot.org/annotation/VAR_086126|||http://purl.uniprot.org/annotation/VAR_086127|||http://purl.uniprot.org/annotation/VAR_086128|||http://purl.uniprot.org/annotation/VAR_086129
http://togogenome.org/gene/9606:PDLIM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z481|||http://purl.uniprot.org/uniprot/B7Z8X5|||http://purl.uniprot.org/uniprot/Q96HC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2 and isoform 3.|||In isoform 2, isoform 4, isoform 6 and isoform 7.|||In isoform 2, isoform 6 and isoform 7.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||PDZ|||PDZ and LIM domain protein 5|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075877|||http://purl.uniprot.org/annotation/VAR_023779|||http://purl.uniprot.org/annotation/VAR_046662|||http://purl.uniprot.org/annotation/VAR_046663|||http://purl.uniprot.org/annotation/VAR_046664|||http://purl.uniprot.org/annotation/VAR_046665|||http://purl.uniprot.org/annotation/VAR_046666|||http://purl.uniprot.org/annotation/VSP_039075|||http://purl.uniprot.org/annotation/VSP_039076|||http://purl.uniprot.org/annotation/VSP_039077|||http://purl.uniprot.org/annotation/VSP_039078|||http://purl.uniprot.org/annotation/VSP_039206|||http://purl.uniprot.org/annotation/VSP_039207|||http://purl.uniprot.org/annotation/VSP_045098|||http://purl.uniprot.org/annotation/VSP_045099|||http://purl.uniprot.org/annotation/VSP_053796|||http://purl.uniprot.org/annotation/VSP_053797
http://togogenome.org/gene/9606:RTCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3I0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes tRNA ligase activity.|||GMP-histidine intermediate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||RNA-splicing ligase RtcB homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255241|||http://purl.uniprot.org/annotation/VAR_028853|||http://purl.uniprot.org/annotation/VAR_052485
http://togogenome.org/gene/9606:CYB561D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14569                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b561|||Cytoplasmic|||Helical|||Lumenal|||Removed|||Transmembrane reductase CYB561D2|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000151036
http://togogenome.org/gene/9606:CIAO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76071                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to HSC20.|||Does not affect binding to HSC20.|||LYR motif; required for interaction with HSC20|||Probable cytosolic iron-sulfur protein assembly protein CIAO1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051389
http://togogenome.org/gene/9606:DSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08554|||http://purl.uniprot.org/uniprot/Q9HB00                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cytoplasmic|||Desmocollin-1|||Extracellular|||Helical|||In isoform 1B.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003863|||http://purl.uniprot.org/annotation/PRO_0000003864|||http://purl.uniprot.org/annotation/PRO_5010148200|||http://purl.uniprot.org/annotation/VAR_055579|||http://purl.uniprot.org/annotation/VAR_055580|||http://purl.uniprot.org/annotation/VAR_061059|||http://purl.uniprot.org/annotation/VSP_000651|||http://purl.uniprot.org/annotation/VSP_000652
http://togogenome.org/gene/9606:ZMYM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ78                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with ETV5. Abolished repression activity.|||Abolishes interaction with ETV5. No effect on repression activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Increases repression activity.|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||No effect on repression activity.|||Zinc finger MYM-type protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191380|||http://purl.uniprot.org/annotation/VAR_025508|||http://purl.uniprot.org/annotation/VAR_025509|||http://purl.uniprot.org/annotation/VAR_062160|||http://purl.uniprot.org/annotation/VSP_011442|||http://purl.uniprot.org/annotation/VSP_011443|||http://purl.uniprot.org/annotation/VSP_011444|||http://purl.uniprot.org/annotation/VSP_011445|||http://purl.uniprot.org/annotation/VSP_034645|||http://purl.uniprot.org/annotation/VSP_034646|||http://purl.uniprot.org/annotation/VSP_034647
http://togogenome.org/gene/9606:C11orf98                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PRG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C11orf98                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432396
http://togogenome.org/gene/9606:MAPK15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD08                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Does not increase dopamine transporter activity. Impairs kinase activity.|||Does not rescue inhibition of O-glycosylation in MAPK15-depleted cells; when associated with A-175.|||Impairs chromatin binding; when associated with A-390. Increases kinase activity; when associated with A-390.|||Impairs chromatin binding; when associated with A-398. Increases kinase activity; when associated with A-398.|||Impairs interaction with GABARAP and MAP1LC3B. Affects subcellular localization in autophagosome. Does not induce autophagy.|||Impairs interaction with PCNA. Associates with chromatin.|||In isoform 2.|||In isoform 3.|||Loss of autophosphorylation and activity. Does not increase dopamine transporter activity. Impairs kinase activity. Does not rescue cilium assembly in MAPK15-depleted cells.|||Loss of autophosphorylation and activity. Heavily phosphorylated at Thr-175.|||Loss of autophosphorylation and activity. Still heavily phosphorylated at Tyr-177. Does not rescues inhibition of O-glycosylation in MAPK15-depleted cells; when associated with F-177.|||Markedly decreases interaction with ESRRA. Impairs interaction with ESRRA; when associated with A-265 and 268-A--A-269. Loses the ability to re-localize ESRRA to the cytoplasm. Does not affect subcellular location in cytoplasm in presence of ESRRA.Loses the ability to repress ESRRA transcriptional activity.|||Markedly decreases interaction with ESRRA. Impairs interaction with ESRRA; when associated with A-281 and 284-A--A-285. Loses the ability to re-localize ESRRA to the cytoplasm. Does not affect subcellular location in cytoplasm in presence of ESRRA. Loses the ability to repress ESRRA transcriptional activity.|||Mitogen-activated protein kinase 15|||Necessary to interact with ESRRA, to regulate its subcellular localization and to inhibit its transcriptional activity|||Not phosphorylated at Thr-175 and Tyr-177.|||Omega-N-methylarginine|||PXXXP motif|||PXXXP motif; regulates binding with chromatin and interaction with PCNA|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Requires for interaction with GABARAP, MAP1LC3B AND GABARAPL1|||TXY|||Unable to induce the formation of autophagosomal structures. Is able to bind to MAP1LC3B and to colocalize with this protein to autophagosomal structures. Does not induce phosphorylation by methyl methanesulfonate. Loas of phosphorylation. Dominant negative mutant. Not phosphorylated at Thr-175 and Tyr-177.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232637|||http://purl.uniprot.org/annotation/VAR_061535|||http://purl.uniprot.org/annotation/VAR_061536|||http://purl.uniprot.org/annotation/VSP_017918|||http://purl.uniprot.org/annotation/VSP_017919|||http://purl.uniprot.org/annotation/VSP_017920|||http://purl.uniprot.org/annotation/VSP_017921
http://togogenome.org/gene/9606:SOS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07890                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||DH|||Disordered|||In NS9.|||In NS9; unknown pathological significance.|||In isoform 2.|||N-terminal Ras-GEF|||PH|||Polar residues|||Pro residues|||Ras-GEF|||Son of sevenless homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068896|||http://purl.uniprot.org/annotation/VAR_034441|||http://purl.uniprot.org/annotation/VAR_054327|||http://purl.uniprot.org/annotation/VAR_054328|||http://purl.uniprot.org/annotation/VAR_075686|||http://purl.uniprot.org/annotation/VAR_075687|||http://purl.uniprot.org/annotation/VAR_075688|||http://purl.uniprot.org/annotation/VAR_075689|||http://purl.uniprot.org/annotation/VAR_075690|||http://purl.uniprot.org/annotation/VAR_075691|||http://purl.uniprot.org/annotation/VAR_075692|||http://purl.uniprot.org/annotation/VSP_054492
http://togogenome.org/gene/9606:PRIMPOL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5S6SZ32|||http://purl.uniprot.org/uniprot/Q96LW4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished Mn(2+) DNA primase activity.|||Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 519-R--A-522.|||Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 551-R--A-554.|||Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-419.|||Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-426.|||Abolishes DNA primase activity, while it increases DNA polymerase activity.|||Abolishes DNA primase and polymerase activities.|||DNA-directed primase/polymerase protein|||Disordered|||Does not affect DNA primase activity.|||In AxA; abolished DNA primase and polymerase activities.|||In MYP22; reduced DNA polymerase and DNA primase activities; reduced DNA-binding.|||In isoform 2.|||In mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with G-419.|||In mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with Y-426.|||Interaction with RPA1|||Phosphoserine|||Polar residues|||RPA1-binding motif 1|||RPA1-binding motif 2|||Reduced DNA primase activity.|||Zinc knuckle motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279395|||http://purl.uniprot.org/annotation/VAR_030878|||http://purl.uniprot.org/annotation/VAR_030879|||http://purl.uniprot.org/annotation/VAR_070120|||http://purl.uniprot.org/annotation/VSP_053600
http://togogenome.org/gene/9606:IL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3F7|||http://purl.uniprot.org/uniprot/P20809                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Important for interaction with IL11RA and for the stimulation of cell proliferation|||Important for interaction with IL6ST and for the stimulation of cell proliferation|||In isoform 2.|||Increases affinity for IL11RA and stimulation of cell proliferation.|||Interleukin-11|||Strongly increases affinity for IL11RA and stimulation of cell proliferation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015618|||http://purl.uniprot.org/annotation/PRO_5014297536|||http://purl.uniprot.org/annotation/VAR_016313|||http://purl.uniprot.org/annotation/VAR_016314|||http://purl.uniprot.org/annotation/VSP_046936
http://togogenome.org/gene/9606:EEF1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26641|||http://purl.uniprot.org/uniprot/Q53YD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-1-gamma C-terminal|||Elongation factor 1-gamma|||GST C-terminal|||GST N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208813|||http://purl.uniprot.org/annotation/VSP_056204
http://togogenome.org/gene/9606:ZNF345                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCE4|||http://purl.uniprot.org/uniprot/Q14585                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 345                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047544
http://togogenome.org/gene/9606:HES4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PB28|||http://purl.uniprot.org/uniprot/Q9HCC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||Orange|||Transcription factor HES-4|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127211
http://togogenome.org/gene/9606:FANCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15360                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Fanconi anemia group A protein|||In FANCA.|||In FANCA; benign variant.|||In FANCA; likely benign variant.|||In FANCA; loss of function.|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087179|||http://purl.uniprot.org/annotation/VAR_009637|||http://purl.uniprot.org/annotation/VAR_009638|||http://purl.uniprot.org/annotation/VAR_009639|||http://purl.uniprot.org/annotation/VAR_009640|||http://purl.uniprot.org/annotation/VAR_009641|||http://purl.uniprot.org/annotation/VAR_009642|||http://purl.uniprot.org/annotation/VAR_009643|||http://purl.uniprot.org/annotation/VAR_009644|||http://purl.uniprot.org/annotation/VAR_009645|||http://purl.uniprot.org/annotation/VAR_009646|||http://purl.uniprot.org/annotation/VAR_009647|||http://purl.uniprot.org/annotation/VAR_009648|||http://purl.uniprot.org/annotation/VAR_009649|||http://purl.uniprot.org/annotation/VAR_009650|||http://purl.uniprot.org/annotation/VAR_009651|||http://purl.uniprot.org/annotation/VAR_009652|||http://purl.uniprot.org/annotation/VAR_009653|||http://purl.uniprot.org/annotation/VAR_009654|||http://purl.uniprot.org/annotation/VAR_009655|||http://purl.uniprot.org/annotation/VAR_009656|||http://purl.uniprot.org/annotation/VAR_009657|||http://purl.uniprot.org/annotation/VAR_009658|||http://purl.uniprot.org/annotation/VAR_017496|||http://purl.uniprot.org/annotation/VAR_017497|||http://purl.uniprot.org/annotation/VAR_017498|||http://purl.uniprot.org/annotation/VAR_017499|||http://purl.uniprot.org/annotation/VAR_017500|||http://purl.uniprot.org/annotation/VAR_017501|||http://purl.uniprot.org/annotation/VAR_017502|||http://purl.uniprot.org/annotation/VAR_017503|||http://purl.uniprot.org/annotation/VAR_017504|||http://purl.uniprot.org/annotation/VAR_017505|||http://purl.uniprot.org/annotation/VAR_038012|||http://purl.uniprot.org/annotation/VAR_038013|||http://purl.uniprot.org/annotation/VAR_038014|||http://purl.uniprot.org/annotation/VAR_038015|||http://purl.uniprot.org/annotation/VAR_038016|||http://purl.uniprot.org/annotation/VAR_038017|||http://purl.uniprot.org/annotation/VAR_038018|||http://purl.uniprot.org/annotation/VAR_038019|||http://purl.uniprot.org/annotation/VAR_038020|||http://purl.uniprot.org/annotation/VAR_038021|||http://purl.uniprot.org/annotation/VAR_050982|||http://purl.uniprot.org/annotation/VAR_050983|||http://purl.uniprot.org/annotation/VAR_050984|||http://purl.uniprot.org/annotation/VAR_050985|||http://purl.uniprot.org/annotation/VAR_050986|||http://purl.uniprot.org/annotation/VAR_050987|||http://purl.uniprot.org/annotation/VAR_061649|||http://purl.uniprot.org/annotation/VSP_007039|||http://purl.uniprot.org/annotation/VSP_054682
http://togogenome.org/gene/9606:CDK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDL9|||http://purl.uniprot.org/uniprot/E7ESI2|||http://purl.uniprot.org/uniprot/G3V5T9|||http://purl.uniprot.org/uniprot/P24941                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2-fold increase in activity.|||Abolishes activity.|||CDK7 binding|||Cyclin-dependent kinase 2|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphothreonine|||Phosphothreonine; by CAK and CCRK|||Phosphotyrosine|||Phosphotyrosine; by WEE1|||Protein kinase|||Proton acceptor|||Reduced phosphorylation by CAK and reduced kinase activity.|||Reduced phosphorylation by CAK.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085769|||http://purl.uniprot.org/annotation/VAR_016157|||http://purl.uniprot.org/annotation/VAR_019988|||http://purl.uniprot.org/annotation/VAR_041972|||http://purl.uniprot.org/annotation/VAR_053927|||http://purl.uniprot.org/annotation/VSP_041998
http://togogenome.org/gene/9606:MYH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11055|||http://purl.uniprot.org/uniprot/Q5GJ67                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In CPSFS1A.|||In CPSFS1A; unknown pathological significance.|||In CPSFS1B.|||In DA2A and DA2B3.|||In DA2A.|||In DA2B3.|||In DA2B3; unknown pathological significance.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin tail|||Myosin-3|||N6,N6,N6-trimethyllysine|||Originally found in DA2B3 patients.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123394|||http://purl.uniprot.org/annotation/VAR_030196|||http://purl.uniprot.org/annotation/VAR_030197|||http://purl.uniprot.org/annotation/VAR_030370|||http://purl.uniprot.org/annotation/VAR_030371|||http://purl.uniprot.org/annotation/VAR_030372|||http://purl.uniprot.org/annotation/VAR_030373|||http://purl.uniprot.org/annotation/VAR_030374|||http://purl.uniprot.org/annotation/VAR_030375|||http://purl.uniprot.org/annotation/VAR_030376|||http://purl.uniprot.org/annotation/VAR_030377|||http://purl.uniprot.org/annotation/VAR_030378|||http://purl.uniprot.org/annotation/VAR_030379|||http://purl.uniprot.org/annotation/VAR_030380|||http://purl.uniprot.org/annotation/VAR_030381|||http://purl.uniprot.org/annotation/VAR_030382|||http://purl.uniprot.org/annotation/VAR_030383|||http://purl.uniprot.org/annotation/VAR_030384|||http://purl.uniprot.org/annotation/VAR_056173|||http://purl.uniprot.org/annotation/VAR_056174|||http://purl.uniprot.org/annotation/VAR_074668|||http://purl.uniprot.org/annotation/VAR_074669|||http://purl.uniprot.org/annotation/VAR_074670|||http://purl.uniprot.org/annotation/VAR_082274|||http://purl.uniprot.org/annotation/VAR_082275|||http://purl.uniprot.org/annotation/VAR_082276|||http://purl.uniprot.org/annotation/VAR_082277|||http://purl.uniprot.org/annotation/VAR_082278|||http://purl.uniprot.org/annotation/VAR_082279
http://togogenome.org/gene/9606:YRDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Improved mitochondrial targeting sequence (MTS), leading to increased import into mitochondria.|||In GAMOS10; decreased formation of tRNA threonylcarbamoyladenosine modification.|||In GAMOS10; slightly decreased formation of tRNA threonylcarbamoyladenosine modification.|||Mitochondrion|||Phosphoserine|||Threonylcarbamoyl-AMP synthase|||YrdC-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341402|||http://purl.uniprot.org/annotation/VAR_085771|||http://purl.uniprot.org/annotation/VAR_085772|||http://purl.uniprot.org/annotation/VAR_085773
http://togogenome.org/gene/9606:VRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9L2|||http://purl.uniprot.org/uniprot/Q86Y07                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with MAP3K7|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase VRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086806|||http://purl.uniprot.org/annotation/VAR_017095|||http://purl.uniprot.org/annotation/VAR_041293|||http://purl.uniprot.org/annotation/VAR_041294|||http://purl.uniprot.org/annotation/VAR_051681|||http://purl.uniprot.org/annotation/VSP_008533|||http://purl.uniprot.org/annotation/VSP_008534|||http://purl.uniprot.org/annotation/VSP_008535|||http://purl.uniprot.org/annotation/VSP_008536|||http://purl.uniprot.org/annotation/VSP_008537|||http://purl.uniprot.org/annotation/VSP_008538
http://togogenome.org/gene/9606:P2RX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15547                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 6|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161557|||http://purl.uniprot.org/annotation/VAR_020338|||http://purl.uniprot.org/annotation/VAR_057664|||http://purl.uniprot.org/annotation/VSP_044799
http://togogenome.org/gene/9606:GDF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RC63|||http://purl.uniprot.org/uniprot/Q9UK05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Growth/differentiation factor 2|||In HHT5; impaired protein processing and function.|||Interaction with ENG|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033902|||http://purl.uniprot.org/annotation/PRO_0000033903|||http://purl.uniprot.org/annotation/PRO_5002781578|||http://purl.uniprot.org/annotation/VAR_070689|||http://purl.uniprot.org/annotation/VAR_070690|||http://purl.uniprot.org/annotation/VAR_070691
http://togogenome.org/gene/9606:DNAJC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H819                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Transmembrane                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 18|||Helical|||J|||Loss of colocalization with SV40-induced foci upon SV40 invection.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244085
http://togogenome.org/gene/9606:CDRT15L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXV6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  CMT1A duplicated region transcript 15 protein-like protein|||Disordered|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349377
http://togogenome.org/gene/9606:AGTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50052                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished angiotensin II-binding.|||Cytoplasmic|||Does not affect angiotensin II-binding.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helix VIII|||N-linked (GlcNAc...) asparagine|||Rare variant found in patients with X-linked intellectual disability; unknown pathological significance.|||Type-2 angiotensin II receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069167|||http://purl.uniprot.org/annotation/VAR_011849|||http://purl.uniprot.org/annotation/VAR_011850|||http://purl.uniprot.org/annotation/VAR_049374|||http://purl.uniprot.org/annotation/VAR_065946|||http://purl.uniprot.org/annotation/VAR_065947|||http://purl.uniprot.org/annotation/VAR_065948
http://togogenome.org/gene/9606:OAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00973                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2'-5'-oligoadenylate synthase 1|||Decreased enzyme activity.|||In IMD100; results in increased 2'-5'-oligoadenylate synthetase activity leading to increased RNase L-mediated cellular RNA degradation, translational arrest and apoptosis.|||In isoform p42.|||In isoform p44.|||In isoform p48.|||Interaction with dsRNA|||Loss of activity; when associated with A-331 and A-332.|||Loss of activity; when associated with A-331 and A-333.|||Loss of activity; when associated with A-332 and A-333.|||Loss of activity; when associated with A-75.|||Loss of activity; when associated with A-77.|||Loss of enzyme activity.|||Not prenylated and diffusely distributed. Loss of antiviral activity.|||S-geranylgeranyl cysteine|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160259|||http://purl.uniprot.org/annotation/VAR_034872|||http://purl.uniprot.org/annotation/VAR_057658|||http://purl.uniprot.org/annotation/VAR_057659|||http://purl.uniprot.org/annotation/VAR_060471|||http://purl.uniprot.org/annotation/VAR_060472|||http://purl.uniprot.org/annotation/VAR_060473|||http://purl.uniprot.org/annotation/VAR_087200|||http://purl.uniprot.org/annotation/VAR_087201|||http://purl.uniprot.org/annotation/VAR_087202|||http://purl.uniprot.org/annotation/VAR_087203|||http://purl.uniprot.org/annotation/VSP_003738|||http://purl.uniprot.org/annotation/VSP_003739|||http://purl.uniprot.org/annotation/VSP_003740|||http://purl.uniprot.org/annotation/VSP_060747|||http://purl.uniprot.org/annotation/VSP_060748
http://togogenome.org/gene/9606:USP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7G6J4N4|||http://purl.uniprot.org/uniprot/Q14694                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with G3BP1 and ability to inhibit stress granule formation.|||Abolished interaction with G3BP1.|||Abolishes deubiquitinating activity and ability to deubiquitinate 40S ribosomal proteins.|||Abolishes phosphorylation by ATM; when associated with A-337.|||Abolishes phosphorylation by ATM; when associated with A-42.|||Decreased but not abolished interaction with G3BP1.|||Disordered|||G3BP1-binding|||In isoform 2.|||In isoform 3.|||Interaction with p53/TP53|||N-acetylalanine|||Nucleophile|||Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with D-337.|||Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with E-42.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Phosphothreonine; by ATM|||Polar residues|||Proton acceptor|||Removed|||USP|||Ubiquitin carboxyl-terminal hydrolase 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080629|||http://purl.uniprot.org/annotation/VAR_015859|||http://purl.uniprot.org/annotation/VAR_015860|||http://purl.uniprot.org/annotation/VAR_015861|||http://purl.uniprot.org/annotation/VSP_038868|||http://purl.uniprot.org/annotation/VSP_038869
http://togogenome.org/gene/9606:DOCK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BY6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 10|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190002|||http://purl.uniprot.org/annotation/VSP_007716|||http://purl.uniprot.org/annotation/VSP_007717|||http://purl.uniprot.org/annotation/VSP_047731
http://togogenome.org/gene/9606:MRPS23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In COXPD46.|||N-acetylalanine|||N6-acetyllysine|||Removed|||Small ribosomal subunit protein mS23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087705|||http://purl.uniprot.org/annotation/VAR_076269
http://togogenome.org/gene/9606:PPP1R7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK83|||http://purl.uniprot.org/uniprot/Q15435                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Completely abolishes the interaction with protein phosphatase 1.|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-acetylalanine|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 7|||Removed|||Severely impaired the binding of protein phosphatase 1.|||Severely impairs the binding of protein phosphatase 1.|||U2A'/phosphoprotein 32 family A C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239613|||http://purl.uniprot.org/annotation/VSP_019244|||http://purl.uniprot.org/annotation/VSP_019245|||http://purl.uniprot.org/annotation/VSP_019246|||http://purl.uniprot.org/annotation/VSP_055672
http://togogenome.org/gene/9606:TMEM262                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PQX1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit TMEM262|||Cytoplasmic|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000424961
http://togogenome.org/gene/9606:ADORA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YWR0|||http://purl.uniprot.org/uniprot/H6VQ59|||http://purl.uniprot.org/uniprot/P0DMS8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenosine receptor A3|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069010|||http://purl.uniprot.org/annotation/VAR_035755|||http://purl.uniprot.org/annotation/VAR_049366|||http://purl.uniprot.org/annotation/VAR_049367
http://togogenome.org/gene/9606:CRTC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UUV7|||http://purl.uniprot.org/uniprot/Q8TEF4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CREB-regulated transcription coactivator 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||Phosphoserine|||Phosphoserine; by SIK2|||Phosphothreonine|||Polar residues|||Required for interaction with HTLV-1 TAX|||Required for interaction with PPP2CA and PPP2R1A|||Transducer of regulated CREB activity C-terminal|||Transducer of regulated CREB activity middle|||Translocates to the cytoplasm. Represses basal TORC3 activity towards CREB.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318531|||http://purl.uniprot.org/annotation/VAR_038758|||http://purl.uniprot.org/annotation/VAR_038759|||http://purl.uniprot.org/annotation/VSP_031220
http://togogenome.org/gene/9606:APOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02654                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Apolipoprotein C-I|||More susceptible to N-terminal truncation and shows greater distribution to the VLDL than the protein with T-71.|||Truncated apolipoprotein C-I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002014|||http://purl.uniprot.org/annotation/PRO_0000391843|||http://purl.uniprot.org/annotation/VAR_014183|||http://purl.uniprot.org/annotation/VAR_029011
http://togogenome.org/gene/9606:IZUMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXV1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Izumo sperm-egg fusion protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295736|||http://purl.uniprot.org/annotation/VAR_050912|||http://purl.uniprot.org/annotation/VSP_027043
http://togogenome.org/gene/9606:TPGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTW0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Tubulin polyglutamylase complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249316|||http://purl.uniprot.org/annotation/VSP_020401
http://togogenome.org/gene/9606:MPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05164                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  84 kDa myeloperoxidase|||89 kDa myeloperoxidase|||Cysteine sulfenic acid (-SOH)|||In MPOD.|||In MPOD; affects proteolytic processing and secretion.|||In MPOD; suppress post-translational processing.|||In a colorectal cancer sample; somatic mutation.|||In isoform H14.|||In isoform H7.|||Interchain|||Myeloperoxidase|||Myeloperoxidase heavy chain|||Myeloperoxidase light chain|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Transition state stabilizer|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000220|||http://purl.uniprot.org/annotation/PRO_0000023651|||http://purl.uniprot.org/annotation/PRO_0000023653|||http://purl.uniprot.org/annotation/PRO_0000023654|||http://purl.uniprot.org/annotation/PRO_0000023655|||http://purl.uniprot.org/annotation/PRO_0000023656|||http://purl.uniprot.org/annotation/VAR_012066|||http://purl.uniprot.org/annotation/VAR_015377|||http://purl.uniprot.org/annotation/VAR_015378|||http://purl.uniprot.org/annotation/VAR_015379|||http://purl.uniprot.org/annotation/VAR_023995|||http://purl.uniprot.org/annotation/VAR_023996|||http://purl.uniprot.org/annotation/VAR_023997|||http://purl.uniprot.org/annotation/VAR_036517|||http://purl.uniprot.org/annotation/VSP_007206|||http://purl.uniprot.org/annotation/VSP_007207
http://togogenome.org/gene/9606:LACTBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y608                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Beta-lactamase-related|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:HAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00219|||http://purl.uniprot.org/uniprot/Q96RV2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hyaluronan synthase 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197178|||http://purl.uniprot.org/annotation/VAR_049317|||http://purl.uniprot.org/annotation/VSP_042022
http://togogenome.org/gene/9606:ROPN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C74                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  RIIa|||Ropporin-1-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307398|||http://purl.uniprot.org/annotation/VAR_035442|||http://purl.uniprot.org/annotation/VAR_035443|||http://purl.uniprot.org/annotation/VAR_057789
http://togogenome.org/gene/9606:DONSON                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYP3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MISSLA.|||In MISSLA; loss of nuclear localization.|||In MISSLA; reduced nuclear localization.|||In MISSLA; reduced protein level; reduced nuclear localization.|||In MISSLA; unknown pathological significance.|||In MISSLA; unknown pathological significance; reduced protein level; no effect on nuclear localization; does not complement loss of endogenous DONSON when tested for the rescue of the spontaneous fork stalling observed after DONSON depletion.|||In isoform 2.|||In isoform 3.|||No effect on nuclear localization; complements loss of endogenous DONSON by rescuing the spontaneous fork stalling observed after DONSON depletion.|||Phosphoserine|||Protein downstream neighbor of Son                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079979|||http://purl.uniprot.org/annotation/VAR_079330|||http://purl.uniprot.org/annotation/VAR_079331|||http://purl.uniprot.org/annotation/VAR_079332|||http://purl.uniprot.org/annotation/VAR_079333|||http://purl.uniprot.org/annotation/VAR_079334|||http://purl.uniprot.org/annotation/VAR_079335|||http://purl.uniprot.org/annotation/VAR_079336|||http://purl.uniprot.org/annotation/VAR_079337|||http://purl.uniprot.org/annotation/VAR_079338|||http://purl.uniprot.org/annotation/VAR_079339|||http://purl.uniprot.org/annotation/VAR_079340|||http://purl.uniprot.org/annotation/VAR_079341|||http://purl.uniprot.org/annotation/VAR_079342|||http://purl.uniprot.org/annotation/VAR_079343|||http://purl.uniprot.org/annotation/VSP_004192|||http://purl.uniprot.org/annotation/VSP_004193|||http://purl.uniprot.org/annotation/VSP_004194|||http://purl.uniprot.org/annotation/VSP_004195
http://togogenome.org/gene/9606:THAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with HCFC1.|||Disordered|||HCFC1-binding motif (HBM)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||THAP domain-containing protein 3|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068644|||http://purl.uniprot.org/annotation/VSP_015136|||http://purl.uniprot.org/annotation/VSP_015137|||http://purl.uniprot.org/annotation/VSP_015138|||http://purl.uniprot.org/annotation/VSP_015139
http://togogenome.org/gene/9606:SLC22A24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4F4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Decreased sterol transport; probable decreased expression due to nonsense-mediated decay.|||Helical|||In isoform 2.|||In isoform 3.|||Steroid transmembrane transporter SLC22A24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317526|||http://purl.uniprot.org/annotation/VAR_083069|||http://purl.uniprot.org/annotation/VSP_060488|||http://purl.uniprot.org/annotation/VSP_060489|||http://purl.uniprot.org/annotation/VSP_060490
http://togogenome.org/gene/9606:ZNF836                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNA1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18; degenerate|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 836                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319434|||http://purl.uniprot.org/annotation/VAR_039001|||http://purl.uniprot.org/annotation/VAR_039002
http://togogenome.org/gene/9606:ARL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282387
http://togogenome.org/gene/9606:DNAJC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75165                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 13|||In PARK; sporadic case; unknown pathological significance.|||In PARK; unknown pathological significance.|||In PARK; unknown pathological significance; affects regulation of endosomal membrane trafficking as indicated by accumulation of transferrin in endosomal compartments.|||Involved in membrane association|||J|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071072|||http://purl.uniprot.org/annotation/VAR_047458|||http://purl.uniprot.org/annotation/VAR_047459|||http://purl.uniprot.org/annotation/VAR_047460|||http://purl.uniprot.org/annotation/VAR_061144|||http://purl.uniprot.org/annotation/VAR_073784|||http://purl.uniprot.org/annotation/VAR_073785|||http://purl.uniprot.org/annotation/VAR_073786|||http://purl.uniprot.org/annotation/VAR_073787|||http://purl.uniprot.org/annotation/VAR_076716|||http://purl.uniprot.org/annotation/VAR_076717|||http://purl.uniprot.org/annotation/VAR_076718|||http://purl.uniprot.org/annotation/VAR_076719|||http://purl.uniprot.org/annotation/VAR_076720|||http://purl.uniprot.org/annotation/VAR_076721|||http://purl.uniprot.org/annotation/VAR_076722|||http://purl.uniprot.org/annotation/VAR_076723|||http://purl.uniprot.org/annotation/VAR_076724|||http://purl.uniprot.org/annotation/VAR_076725|||http://purl.uniprot.org/annotation/VAR_076726|||http://purl.uniprot.org/annotation/VAR_076727|||http://purl.uniprot.org/annotation/VAR_076728
http://togogenome.org/gene/9606:EIF4EBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13542                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes folding of the intrinsically disordered protein without affecting greatly affinity for EIF4E even when the protein is fully phosphorylated; when associated with V-39.|||Abolishes folding of the intrinsically disordered protein without affecting greatly affinity for EIF4E even when the protein is fully phosphorylated; when associated with V-48.|||Acidic residues do not mimic phosphorylation state. Does not induce folding of the intrinsically disordered protein; when associated with D-37 or E-37.|||Acidic residues do not mimic phosphorylation state. Does not induce folding of the intrinsically disordered protein; when associated with D-46 or E-46.|||Deamidated asparagine|||Disordered|||Eukaryotic translation initiation factor 4E-binding protein 2|||Impaired binding to EIF4E.|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine; by MTOR|||Secondary EIF4E binding site|||TOS motif|||YXXXXLphi motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190516
http://togogenome.org/gene/9606:PET100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJ07                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC4DN12; results in impaired complex IV assembly.|||Mitochondrion|||Protein PET100 homolog, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413099|||http://purl.uniprot.org/annotation/VAR_084179
http://togogenome.org/gene/9606:LCE3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA77                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235334
http://togogenome.org/gene/9606:GALNTL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5D8G0|||http://purl.uniprot.org/uniprot/Q49A17                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase-like 6|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325774|||http://purl.uniprot.org/annotation/VSP_032402
http://togogenome.org/gene/9606:PRAMEF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95522                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156986|||http://purl.uniprot.org/annotation/VAR_053608|||http://purl.uniprot.org/annotation/VAR_053609
http://togogenome.org/gene/9606:AGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2A4E4|||http://purl.uniprot.org/uniprot/P35573                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  4-alpha-glucanotransferase|||Amylo-1,6-glucosidase|||Eukaryotic glycogen debranching enzyme N-terminal|||Glycogen debranching enzyme|||Glycogen debranching enzyme C-terminal|||Glycogen debranching enzyme central|||Glycogen debranching enzyme glucanotransferase|||In GSD3; deficient in ability to bind glycogen; unstable due to enhanced ubiquitination; forms aggresomes upon proteasome impairment.|||In isoform 5.|||In isoform 6.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087450|||http://purl.uniprot.org/annotation/VAR_009230|||http://purl.uniprot.org/annotation/VAR_009231|||http://purl.uniprot.org/annotation/VAR_009621|||http://purl.uniprot.org/annotation/VAR_009622|||http://purl.uniprot.org/annotation/VAR_020389|||http://purl.uniprot.org/annotation/VAR_028051|||http://purl.uniprot.org/annotation/VAR_028052|||http://purl.uniprot.org/annotation/VAR_028053|||http://purl.uniprot.org/annotation/VAR_028054|||http://purl.uniprot.org/annotation/VAR_028055|||http://purl.uniprot.org/annotation/VAR_032084|||http://purl.uniprot.org/annotation/VAR_032085|||http://purl.uniprot.org/annotation/VAR_051010|||http://purl.uniprot.org/annotation/VSP_004270|||http://purl.uniprot.org/annotation/VSP_004271
http://togogenome.org/gene/9606:FAM43B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Protein FAM43B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187026
http://togogenome.org/gene/9606:ITPR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8K3|||http://purl.uniprot.org/uniprot/Q14573|||http://purl.uniprot.org/uniprot/Q59ES2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CMT1J.|||In CMT1J; decreased inositol trisphosphate-mediated calcium release and altered calcium homeostasis in patient fibroblasts.|||In CMT1J; unknown pathological significance.|||Inositol 1,4,5-trisphosphate receptor type 3|||Ion transport|||MIR|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Phosphoserine|||Polar residues|||RIH|||RyR/IP3R Homology associated                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153928|||http://purl.uniprot.org/annotation/VAR_046978|||http://purl.uniprot.org/annotation/VAR_046979|||http://purl.uniprot.org/annotation/VAR_046980|||http://purl.uniprot.org/annotation/VAR_046981|||http://purl.uniprot.org/annotation/VAR_046982|||http://purl.uniprot.org/annotation/VAR_046983|||http://purl.uniprot.org/annotation/VAR_046984|||http://purl.uniprot.org/annotation/VAR_049604|||http://purl.uniprot.org/annotation/VAR_087822|||http://purl.uniprot.org/annotation/VAR_087823|||http://purl.uniprot.org/annotation/VAR_087824
http://togogenome.org/gene/9606:EPSTI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J88                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Epithelial-stromal interaction protein 1|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314034|||http://purl.uniprot.org/annotation/VAR_082880|||http://purl.uniprot.org/annotation/VAR_082881|||http://purl.uniprot.org/annotation/VSP_030201|||http://purl.uniprot.org/annotation/VSP_030202
http://togogenome.org/gene/9606:KNCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6PVL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Kinocilin|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311265|||http://purl.uniprot.org/annotation/VSP_040405
http://togogenome.org/gene/9606:PGK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR3|||http://purl.uniprot.org/uniprot/P07205                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylserine|||N6-acetyllysine|||Phosphoglycerate kinase 2|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145832
http://togogenome.org/gene/9606:SMR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99954                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Pro residues|||Submaxillary gland androgen-regulated protein 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022116|||http://purl.uniprot.org/annotation/VAR_056989|||http://purl.uniprot.org/annotation/VAR_060392|||http://purl.uniprot.org/annotation/VAR_060393
http://togogenome.org/gene/9606:PRMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99873                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity.|||N6-acetyllysine|||N6-succinyllysine|||No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-322. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-322.|||No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-359.|||No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-322 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-322 and A-359.|||Phosphoserine|||Protein arginine N-methyltransferase 1|||SAM-dependent MTase PRMT-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212321|||http://purl.uniprot.org/annotation/VAR_037501|||http://purl.uniprot.org/annotation/VAR_037502|||http://purl.uniprot.org/annotation/VSP_005208|||http://purl.uniprot.org/annotation/VSP_005209|||http://purl.uniprot.org/annotation/VSP_059419|||http://purl.uniprot.org/annotation/VSP_059420
http://togogenome.org/gene/9606:CHRNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05901                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000383|||http://purl.uniprot.org/annotation/VAR_048173
http://togogenome.org/gene/9606:XCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBD3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cytokine SCM-1 beta|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005251|||http://purl.uniprot.org/annotation/VAR_048713|||http://purl.uniprot.org/annotation/VAR_059212
http://togogenome.org/gene/9606:WDR70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305144
http://togogenome.org/gene/9606:GNG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63215                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3|||Phosphoserine|||Phosphothreonine|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012617|||http://purl.uniprot.org/annotation/PRO_0000012618
http://togogenome.org/gene/9606:FH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4C3|||http://purl.uniprot.org/uniprot/P07954                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage.|||Does not affect phosphorylation by PRKDC.|||Fumarase C C-terminal|||Fumarate hydratase, mitochondrial|||Fumarate lyase N-terminal|||Important for catalytic activity|||In FMRD and HLRCC.|||In FMRD.|||In HLRCC.|||In HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair.|||In isoform Cytoplasmic.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphomimetic mutant; promotes interaction with H2AZ1, leading to increased localization to chromatin in response to DNA damage.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PRKDC|||Proton donor/acceptor|||Removed|||in site B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010319|||http://purl.uniprot.org/annotation/VAR_002445|||http://purl.uniprot.org/annotation/VAR_002446|||http://purl.uniprot.org/annotation/VAR_002447|||http://purl.uniprot.org/annotation/VAR_002448|||http://purl.uniprot.org/annotation/VAR_013497|||http://purl.uniprot.org/annotation/VAR_013498|||http://purl.uniprot.org/annotation/VAR_013499|||http://purl.uniprot.org/annotation/VAR_013500|||http://purl.uniprot.org/annotation/VAR_013501|||http://purl.uniprot.org/annotation/VAR_013502|||http://purl.uniprot.org/annotation/VAR_013503|||http://purl.uniprot.org/annotation/VAR_081606|||http://purl.uniprot.org/annotation/VSP_018965
http://togogenome.org/gene/9606:FAM131C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AQ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Pro residues|||Protein FAM131C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280401|||http://purl.uniprot.org/annotation/VAR_031130|||http://purl.uniprot.org/annotation/VAR_031131|||http://purl.uniprot.org/annotation/VAR_031132|||http://purl.uniprot.org/annotation/VAR_031133|||http://purl.uniprot.org/annotation/VAR_031134
http://togogenome.org/gene/9606:CCDC120                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HB5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 120|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||Involved in CYTH2-binding|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254141|||http://purl.uniprot.org/annotation/VSP_042859|||http://purl.uniprot.org/annotation/VSP_047104|||http://purl.uniprot.org/annotation/VSP_054527
http://togogenome.org/gene/9606:ABCB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1D2|||http://purl.uniprot.org/uniprot/P08183                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-dependent translocase ABCB1|||Common allele; associated with susceptibility to IBD13; has decreased enzyme activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colchicine-selected multidrug-resistant cell line; confers increased resistance to colchicine.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Rare allele.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093332|||http://purl.uniprot.org/annotation/VAR_013361|||http://purl.uniprot.org/annotation/VAR_013362|||http://purl.uniprot.org/annotation/VAR_014704|||http://purl.uniprot.org/annotation/VAR_015001|||http://purl.uniprot.org/annotation/VAR_015002|||http://purl.uniprot.org/annotation/VAR_015003|||http://purl.uniprot.org/annotation/VAR_015004|||http://purl.uniprot.org/annotation/VAR_015005|||http://purl.uniprot.org/annotation/VAR_018351|||http://purl.uniprot.org/annotation/VAR_018352|||http://purl.uniprot.org/annotation/VAR_018353|||http://purl.uniprot.org/annotation/VAR_022276|||http://purl.uniprot.org/annotation/VAR_022277|||http://purl.uniprot.org/annotation/VAR_022278|||http://purl.uniprot.org/annotation/VAR_022279|||http://purl.uniprot.org/annotation/VAR_022280|||http://purl.uniprot.org/annotation/VAR_022281|||http://purl.uniprot.org/annotation/VAR_035737|||http://purl.uniprot.org/annotation/VAR_055423|||http://purl.uniprot.org/annotation/VAR_055424|||http://purl.uniprot.org/annotation/VAR_055425|||http://purl.uniprot.org/annotation/VAR_055426|||http://purl.uniprot.org/annotation/VAR_055427|||http://purl.uniprot.org/annotation/VAR_055428|||http://purl.uniprot.org/annotation/VAR_055429|||http://purl.uniprot.org/annotation/VSP_055769
http://togogenome.org/gene/9606:HOXB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17481|||http://purl.uniprot.org/uniprot/Q8N8T3                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200148
http://togogenome.org/gene/9606:OGFRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TC84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Opioid growth factor receptor-like protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314142|||http://purl.uniprot.org/annotation/VAR_037842|||http://purl.uniprot.org/annotation/VAR_037843
http://togogenome.org/gene/9606:KIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10721                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-741.|||Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-746.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Important for interaction with phosphotyrosine-binding proteins|||In GIST.|||In GIST; somatic mutation.|||In MASTC; constitutively activated.|||In MASTC; somatic mutation; constitutively activated; requires 2 nucleotide substitutions.|||In MASTC; sporadic case; somatic mutation; dominant negative mutation; loss of autophosphorylation.|||In MASTC; sporadic case; somatic mutation; requires 2 nucleotide substitutions; constitutively activated and is much more rapidly autophosphorylated than wild type.|||In MASTC; unknown pathological significance.|||In MASTSYS and MASTC; also found in acute myeloid leukemia and a germ cell tumor of the testis; somatic mutation; constitutively activated.|||In MASTSYS, MASTC and mast cell leukemia; somatic mutation; constitutively activated; loss of interaction with MPDZ.|||In PBT.|||In PBT; severe.|||In PBT; with sensorineural deafness.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a germ cell tumor of the testis; somatic mutation.|||In a testicular tumor; seminoma; somatic mutation; constitutively activated.|||In isoform 2.|||In isoform 3.|||In mast cell disease; systemic.|||Mast/stem cell growth factor receptor Kit|||N-linked (GlcNAc...) asparagine|||No decrease in activity. Leads to autophosphorylation at Tyr-900.|||Phosphoserine|||Phosphoserine; by PKC/PRKCA|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduces autophosphorylation in response to KITLG/SCF.|||Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-571.|||Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-939.|||Stronger interaction with MPDZ.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016754|||http://purl.uniprot.org/annotation/VAR_004104|||http://purl.uniprot.org/annotation/VAR_004105|||http://purl.uniprot.org/annotation/VAR_004106|||http://purl.uniprot.org/annotation/VAR_004107|||http://purl.uniprot.org/annotation/VAR_004108|||http://purl.uniprot.org/annotation/VAR_004109|||http://purl.uniprot.org/annotation/VAR_004110|||http://purl.uniprot.org/annotation/VAR_007965|||http://purl.uniprot.org/annotation/VAR_023828|||http://purl.uniprot.org/annotation/VAR_023829|||http://purl.uniprot.org/annotation/VAR_023830|||http://purl.uniprot.org/annotation/VAR_033123|||http://purl.uniprot.org/annotation/VAR_033124|||http://purl.uniprot.org/annotation/VAR_033125|||http://purl.uniprot.org/annotation/VAR_033126|||http://purl.uniprot.org/annotation/VAR_033127|||http://purl.uniprot.org/annotation/VAR_033128|||http://purl.uniprot.org/annotation/VAR_033129|||http://purl.uniprot.org/annotation/VAR_033130|||http://purl.uniprot.org/annotation/VAR_033131|||http://purl.uniprot.org/annotation/VAR_033132|||http://purl.uniprot.org/annotation/VAR_033133|||http://purl.uniprot.org/annotation/VAR_033134|||http://purl.uniprot.org/annotation/VAR_033135|||http://purl.uniprot.org/annotation/VAR_033136|||http://purl.uniprot.org/annotation/VAR_033137|||http://purl.uniprot.org/annotation/VAR_042021|||http://purl.uniprot.org/annotation/VAR_042022|||http://purl.uniprot.org/annotation/VAR_042023|||http://purl.uniprot.org/annotation/VAR_042024|||http://purl.uniprot.org/annotation/VAR_042025|||http://purl.uniprot.org/annotation/VAR_042026|||http://purl.uniprot.org/annotation/VAR_061289|||http://purl.uniprot.org/annotation/VAR_081062|||http://purl.uniprot.org/annotation/VAR_081063|||http://purl.uniprot.org/annotation/VAR_081064|||http://purl.uniprot.org/annotation/VAR_081065|||http://purl.uniprot.org/annotation/VSP_038385|||http://purl.uniprot.org/annotation/VSP_060976
http://togogenome.org/gene/9606:MYH15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2K3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-15|||N6,N6,N6-trimethyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274233|||http://purl.uniprot.org/annotation/VAR_030235|||http://purl.uniprot.org/annotation/VAR_030236|||http://purl.uniprot.org/annotation/VAR_030237|||http://purl.uniprot.org/annotation/VAR_030238|||http://purl.uniprot.org/annotation/VAR_046376
http://togogenome.org/gene/9606:MPV17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Z9|||http://purl.uniprot.org/uniprot/P39210                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Affects ion selectivity of the channel.|||Determines ion selectivity|||Does not affect conductance and gating properties of the channel.|||Does not affect gating properties of the channel.|||Helical|||In CMT2EE.|||In MTDPS6 and CMT2EE; results in incomplete closing of the channel.|||In MTDPS6.|||In MTDPS6; does not completely rescue iridophores loss in zebrafish 'tra' mutants; may cause protein instability and decay.|||In MTDPS6; results in altered ribonucleotide incorporation in mtDNA from patient fibroblasts.|||In MTDPS6; unknown pathological significance.|||Protein Mpv17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218927|||http://purl.uniprot.org/annotation/VAR_026217|||http://purl.uniprot.org/annotation/VAR_026218|||http://purl.uniprot.org/annotation/VAR_026219|||http://purl.uniprot.org/annotation/VAR_076199|||http://purl.uniprot.org/annotation/VAR_076200|||http://purl.uniprot.org/annotation/VAR_076201|||http://purl.uniprot.org/annotation/VAR_076202|||http://purl.uniprot.org/annotation/VAR_076203|||http://purl.uniprot.org/annotation/VAR_076204|||http://purl.uniprot.org/annotation/VAR_082226|||http://purl.uniprot.org/annotation/VAR_082227|||http://purl.uniprot.org/annotation/VAR_082228|||http://purl.uniprot.org/annotation/VAR_082229|||http://purl.uniprot.org/annotation/VAR_082230|||http://purl.uniprot.org/annotation/VAR_082231|||http://purl.uniprot.org/annotation/VAR_082232|||http://purl.uniprot.org/annotation/VAR_082233|||http://purl.uniprot.org/annotation/VAR_082234|||http://purl.uniprot.org/annotation/VAR_082235|||http://purl.uniprot.org/annotation/VAR_082236|||http://purl.uniprot.org/annotation/VAR_082237|||http://purl.uniprot.org/annotation/VAR_082238|||http://purl.uniprot.org/annotation/VAR_082239|||http://purl.uniprot.org/annotation/VAR_082240|||http://purl.uniprot.org/annotation/VAR_082241|||http://purl.uniprot.org/annotation/VAR_082242|||http://purl.uniprot.org/annotation/VAR_082243|||http://purl.uniprot.org/annotation/VAR_082244
http://togogenome.org/gene/9606:TTC39B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTQ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||TPR 1|||TPR 2|||Tetratricopeptide repeat protein 39B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292000|||http://purl.uniprot.org/annotation/VAR_032926|||http://purl.uniprot.org/annotation/VAR_054078|||http://purl.uniprot.org/annotation/VSP_026355|||http://purl.uniprot.org/annotation/VSP_042798|||http://purl.uniprot.org/annotation/VSP_042799|||http://purl.uniprot.org/annotation/VSP_042800|||http://purl.uniprot.org/annotation/VSP_042801|||http://purl.uniprot.org/annotation/VSP_042802|||http://purl.uniprot.org/annotation/VSP_042803
http://togogenome.org/gene/9606:ANXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04083                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Peptide|||Repeat|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Abolishes secretion and modulation of exocytosis.|||Abolishes secretion and nearly abolishes modulation of exocytosis.|||Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A1|||Annexin Ac2-26|||Cleavage; by CTSG|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||N-acetylalanine|||N6-acetyllysine|||No effect on secretion and modulation of exocytosis.|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by TRPM7|||Phosphothreonine|||Phosphotyrosine; by EGFR|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067460|||http://purl.uniprot.org/annotation/PRO_0000454556
http://togogenome.org/gene/9606:ARCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YIW5|||http://purl.uniprot.org/uniprot/P48444                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coatomer subunit delta|||Disordered|||In isoform 2.|||MHD|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193841|||http://purl.uniprot.org/annotation/VAR_011788|||http://purl.uniprot.org/annotation/VAR_011789|||http://purl.uniprot.org/annotation/VSP_045636
http://togogenome.org/gene/9606:MTIF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46199|||http://purl.uniprot.org/uniprot/Q6P1N2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  G1|||G2|||G3|||G4|||G5|||Mitochondrion|||Phosphothreonine|||Tr-type G|||Translation initiation factor IF-2, mitochondrial|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014480|||http://purl.uniprot.org/annotation/VAR_014883|||http://purl.uniprot.org/annotation/VAR_054428
http://togogenome.org/gene/9606:IGF2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11717                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cation-independent mannose-6-phosphate receptor|||Cytoplasmic|||Disordered|||Fibronectin type-II|||Helical|||Lumenal|||MRH 1|||MRH 10|||MRH 11|||MRH 12|||MRH 14|||MRH 15|||MRH 2|||MRH 3|||MRH 4|||MRH 5|||MRH 6|||MRH 7|||MRH 8|||MRH 9|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019229|||http://purl.uniprot.org/annotation/VAR_014722|||http://purl.uniprot.org/annotation/VAR_020470|||http://purl.uniprot.org/annotation/VAR_020471|||http://purl.uniprot.org/annotation/VAR_020472|||http://purl.uniprot.org/annotation/VAR_020473|||http://purl.uniprot.org/annotation/VAR_020474|||http://purl.uniprot.org/annotation/VAR_020475|||http://purl.uniprot.org/annotation/VAR_020476|||http://purl.uniprot.org/annotation/VAR_020477|||http://purl.uniprot.org/annotation/VAR_021304|||http://purl.uniprot.org/annotation/VAR_021305|||http://purl.uniprot.org/annotation/VAR_021306|||http://purl.uniprot.org/annotation/VAR_021307|||http://purl.uniprot.org/annotation/VAR_021308|||http://purl.uniprot.org/annotation/VAR_021309|||http://purl.uniprot.org/annotation/VAR_021310|||http://purl.uniprot.org/annotation/VAR_021311|||http://purl.uniprot.org/annotation/VAR_021312|||http://purl.uniprot.org/annotation/VAR_021313|||http://purl.uniprot.org/annotation/VAR_021314|||http://purl.uniprot.org/annotation/VAR_021315|||http://purl.uniprot.org/annotation/VAR_021316|||http://purl.uniprot.org/annotation/VAR_050428|||http://purl.uniprot.org/annotation/VAR_050429|||http://purl.uniprot.org/annotation/VAR_050430
http://togogenome.org/gene/9606:SEPTIN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFQ9|||http://purl.uniprot.org/uniprot/B7ZVZ1|||http://purl.uniprot.org/uniprot/Q92599                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Removed|||Septin-8|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173533|||http://purl.uniprot.org/annotation/VSP_009643|||http://purl.uniprot.org/annotation/VSP_009644|||http://purl.uniprot.org/annotation/VSP_054085|||http://purl.uniprot.org/annotation/VSP_054086
http://togogenome.org/gene/9606:MANBAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Protein MANBAL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194179
http://togogenome.org/gene/9606:GMPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36959                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  GMP reductase 1|||Proton donor/acceptor|||Thioimidate intermediate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093723|||http://purl.uniprot.org/annotation/VAR_003969|||http://purl.uniprot.org/annotation/VAR_003970
http://togogenome.org/gene/9606:QSOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ERV/ALR sulfhydryl oxidase|||Helical|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Redox-active|||Sulfhydryl oxidase 2|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249538|||http://purl.uniprot.org/annotation/VAR_027435
http://togogenome.org/gene/9606:RPL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62913|||http://purl.uniprot.org/uniprot/Q5VVD0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In DBA7.|||In isoform 2.|||Large ribosomal subunit protein uL5|||Large ribosomal subunit protein uL5 C-terminal|||Large ribosomal subunit protein uL5 N-terminal|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125082|||http://purl.uniprot.org/annotation/VAR_055448|||http://purl.uniprot.org/annotation/VAR_055449|||http://purl.uniprot.org/annotation/VSP_008320
http://togogenome.org/gene/9606:ATP13A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VNC1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||INTRAMEM|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Probable cation-transporting ATPase 13A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318675|||http://purl.uniprot.org/annotation/VAR_038849|||http://purl.uniprot.org/annotation/VAR_038850|||http://purl.uniprot.org/annotation/VAR_038851|||http://purl.uniprot.org/annotation/VSP_031258|||http://purl.uniprot.org/annotation/VSP_031259|||http://purl.uniprot.org/annotation/VSP_031260|||http://purl.uniprot.org/annotation/VSP_031261
http://togogenome.org/gene/9606:C1orf131                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein C1orf131                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285029|||http://purl.uniprot.org/annotation/VAR_031906|||http://purl.uniprot.org/annotation/VSP_059466|||http://purl.uniprot.org/annotation/VSP_059467|||http://purl.uniprot.org/annotation/VSP_059468|||http://purl.uniprot.org/annotation/VSP_059469
http://togogenome.org/gene/9606:UPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00526                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Uroplakin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022630|||http://purl.uniprot.org/annotation/PRO_0000022631|||http://purl.uniprot.org/annotation/VAR_051473|||http://purl.uniprot.org/annotation/VAR_062246
http://togogenome.org/gene/9606:FGFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A141AXF1|||http://purl.uniprot.org/uniprot/D2CGD1|||http://purl.uniprot.org/uniprot/P21802|||http://purl.uniprot.org/uniprot/S4R381                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Constitutive kinase activity.|||Cytoplasmic|||Disordered|||Extracellular|||Fibroblast growth factor receptor|||Fibroblast growth factor receptor 2|||Helical|||Heparin-binding|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In APRS and PS; common mutation.|||In APRS; common mutation.|||In APRS; requires 2 nucleotide substitutions.|||In BBDS1.|||In BBDS1; the mutation selectively reduces plasma-membrane levels of the protein and markedly diminishes the receptor's responsiveness to extracellular FGF.|||In BSTVS.|||In CS and JWS.|||In CS and PS.|||In CS, JWS and PS; forms disulfide-linked dimers with constitutive kinase activity, is retained in an intracellular compartment and not detected at the cell surface.|||In CS, JWS, PS and ABS2.|||In CS, PS and ABS2.|||In CS.|||In CS; constitutive kinase activity.|||In FSPC; constitutive kinase activity.|||In LADD1.|||In LADD1; strongly reduced kinase activity.|||In PS and BSTVS.|||In PS and CS.|||In PS.|||In PS; constitutive kinase activity.|||In PS; requires 2 nucleotide substitutions.|||In PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation.|||In PS; type 2.|||In SCS.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis.|||In an ovarian serous carcinoma sample; somatic mutation.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||In craniosynostosis.|||In craniosynostosis; constitutive kinase activity.|||In isoform 10.|||In isoform 13.|||In isoform 14.|||In isoform 15.|||In isoform 17.|||In isoform 2, isoform 7, isoform 11 and isoform 16.|||In isoform 3, isoform 4, isoform 11, isoform 12, isoform 13 and isoform 16.|||In isoform 4, isoform 15 and isoform 16.|||In isoform 4, isoform 5, isoform 6, isoform 7, isoform 10 and isoform 12.|||In isoform 4.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||Increases fibroblast proliferation. Decreases phosphorylation of PLCG1 and FRS2. Decreases activation of MAP kinases.|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced N-glycosylation. Reduced expression at the cell surface.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016783|||http://purl.uniprot.org/annotation/PRO_5007491846|||http://purl.uniprot.org/annotation/PRO_5014087146|||http://purl.uniprot.org/annotation/VAR_004112|||http://purl.uniprot.org/annotation/VAR_004113|||http://purl.uniprot.org/annotation/VAR_004114|||http://purl.uniprot.org/annotation/VAR_004115|||http://purl.uniprot.org/annotation/VAR_004116|||http://purl.uniprot.org/annotation/VAR_004117|||http://purl.uniprot.org/annotation/VAR_004118|||http://purl.uniprot.org/annotation/VAR_004119|||http://purl.uniprot.org/annotation/VAR_004120|||http://purl.uniprot.org/annotation/VAR_004121|||http://purl.uniprot.org/annotation/VAR_004122|||http://purl.uniprot.org/annotation/VAR_004123|||http://purl.uniprot.org/annotation/VAR_004124|||http://purl.uniprot.org/annotation/VAR_004125|||http://purl.uniprot.org/annotation/VAR_004126|||http://purl.uniprot.org/annotation/VAR_004127|||http://purl.uniprot.org/annotation/VAR_004128|||http://purl.uniprot.org/annotation/VAR_004129|||http://purl.uniprot.org/annotation/VAR_004130|||http://purl.uniprot.org/annotation/VAR_004131|||http://purl.uniprot.org/annotation/VAR_004132|||http://purl.uniprot.org/annotation/VAR_004133|||http://purl.uniprot.org/annotation/VAR_004134|||http://purl.uniprot.org/annotation/VAR_004135|||http://purl.uniprot.org/annotation/VAR_004136|||http://purl.uniprot.org/annotation/VAR_004137|||http://purl.uniprot.org/annotation/VAR_004138|||http://purl.uniprot.org/annotation/VAR_004139|||http://purl.uniprot.org/annotation/VAR_004140|||http://purl.uniprot.org/annotation/VAR_004141|||http://purl.uniprot.org/annotation/VAR_004142|||http://purl.uniprot.org/annotation/VAR_004143|||http://purl.uniprot.org/annotation/VAR_004144|||http://purl.uniprot.org/annotation/VAR_004145|||http://purl.uniprot.org/annotation/VAR_004146|||http://purl.uniprot.org/annotation/VAR_004147|||http://purl.uniprot.org/annotation/VAR_015011|||http://purl.uniprot.org/annotation/VAR_015012|||http://purl.uniprot.org/annotation/VAR_017258|||http://purl.uniprot.org/annotation/VAR_017259|||http://purl.uniprot.org/annotation/VAR_017260|||http://purl.uniprot.org/annotation/VAR_017261|||http://purl.uniprot.org/annotation/VAR_017262|||http://purl.uniprot.org/annotation/VAR_017263|||http://purl.uniprot.org/annotation/VAR_017264|||http://purl.uniprot.org/annotation/VAR_017265|||http://purl.uniprot.org/annotation/VAR_017266|||http://purl.uniprot.org/annotation/VAR_017267|||http://purl.uniprot.org/annotation/VAR_017268|||http://purl.uniprot.org/annotation/VAR_017269|||http://purl.uniprot.org/annotation/VAR_017270|||http://purl.uniprot.org/annotation/VAR_017271|||http://purl.uniprot.org/annotation/VAR_017272|||http://purl.uniprot.org/annotation/VAR_017273|||http://purl.uniprot.org/annotation/VAR_017274|||http://purl.uniprot.org/annotation/VAR_017275|||http://purl.uniprot.org/annotation/VAR_017276|||http://purl.uniprot.org/annotation/VAR_017277|||http://purl.uniprot.org/annotation/VAR_017278|||http://purl.uniprot.org/annotation/VAR_017279|||http://purl.uniprot.org/annotation/VAR_017280|||http://purl.uniprot.org/annotation/VAR_017281|||http://purl.uniprot.org/annotation/VAR_023788|||http://purl.uniprot.org/annotation/VAR_029884|||http://purl.uniprot.org/annotation/VAR_029885|||http://purl.uniprot.org/annotation/VAR_029886|||http://purl.uniprot.org/annotation/VAR_036380|||http://purl.uniprot.org/annotation/VAR_042204|||http://purl.uniprot.org/annotation/VAR_042205|||http://purl.uniprot.org/annotation/VAR_042206|||http://purl.uniprot.org/annotation/VAR_046071|||http://purl.uniprot.org/annotation/VAR_067977|||http://purl.uniprot.org/annotation/VAR_067978|||http://purl.uniprot.org/annotation/VAR_075856|||http://purl.uniprot.org/annotation/VSP_002964|||http://purl.uniprot.org/annotation/VSP_002965|||http://purl.uniprot.org/annotation/VSP_002966|||http://purl.uniprot.org/annotation/VSP_002967|||http://purl.uniprot.org/annotation/VSP_002968|||http://purl.uniprot.org/annotation/VSP_002969|||http://purl.uniprot.org/annotation/VSP_002970|||http://purl.uniprot.org/annotation/VSP_002971|||http://purl.uniprot.org/annotation/VSP_002972|||http://purl.uniprot.org/annotation/VSP_002973|||http://purl.uniprot.org/annotation/VSP_002974|||http://purl.uniprot.org/annotation/VSP_002975|||http://purl.uniprot.org/annotation/VSP_002976|||http://purl.uniprot.org/annotation/VSP_002978|||http://purl.uniprot.org/annotation/VSP_002984|||http://purl.uniprot.org/annotation/VSP_019608|||http://purl.uniprot.org/annotation/VSP_019609|||http://purl.uniprot.org/annotation/VSP_041914|||http://purl.uniprot.org/annotation/VSP_041915
http://togogenome.org/gene/9606:PPRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EVG6|||http://purl.uniprot.org/uniprot/Q5VV67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Necessary for interaction with CREB1 and NRF1|||Necessary for interaction with CREB1 and NRF1 and for transcriptional coactivation|||Peroxisome proliferator-activated receptor gamma coactivator-related protein 1|||Phosphoserine|||Polar residues|||Pro residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296666|||http://purl.uniprot.org/annotation/VAR_034633|||http://purl.uniprot.org/annotation/VAR_034634|||http://purl.uniprot.org/annotation/VAR_074628|||http://purl.uniprot.org/annotation/VSP_027229|||http://purl.uniprot.org/annotation/VSP_027230|||http://purl.uniprot.org/annotation/VSP_027231
http://togogenome.org/gene/9606:MTIF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2K0                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||Translation initiation factor IF-3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280037|||http://purl.uniprot.org/annotation/VAR_031045|||http://purl.uniprot.org/annotation/VAR_031046
http://togogenome.org/gene/9606:UTP23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||rRNA-processing protein UTP23 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285634|||http://purl.uniprot.org/annotation/VAR_032031|||http://purl.uniprot.org/annotation/VAR_032032|||http://purl.uniprot.org/annotation/VAR_032033|||http://purl.uniprot.org/annotation/VSP_024874|||http://purl.uniprot.org/annotation/VSP_024875
http://togogenome.org/gene/9606:TTC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95801                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Essential for interaction with CDC6|||Essential for interaction with HSPA8|||Loss of interaction with HSPA8.|||N-acetylmethionine|||No effect on interaction with HSPA8 and HSP90AB1. Loss of interaction with CDC6.|||No effect on interaction with HSPA8, HSP90AB1 and CDC6.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106379|||http://purl.uniprot.org/annotation/VAR_031713
http://togogenome.org/gene/9606:LCE1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235324
http://togogenome.org/gene/9606:CDC42SE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Modified Residue                                                                                  ^@                                                                                  CDC42 small effector protein 2|||CRIB|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334639
http://togogenome.org/gene/9606:RDH16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75452|||http://purl.uniprot.org/uniprot/Q59FX7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Decreases androsterone dehydrogenase activity; when associated with F-176.|||Decreases androsterone dehydrogenase activity; when associated with R-180.|||Helical|||Proton acceptor|||Retinol dehydrogenase 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307693
http://togogenome.org/gene/9606:NTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00634                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site; atypical|||Disordered|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||NTR|||Netrin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017085|||http://purl.uniprot.org/annotation/VAR_050086
http://togogenome.org/gene/9606:PADI4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM07                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Citrulline|||Does not affect catalytic activity.|||Impaired binding of TDFAInhibitor.|||Protein-arginine deiminase type-4|||Strongly reduces enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220033|||http://purl.uniprot.org/annotation/VAR_020639|||http://purl.uniprot.org/annotation/VAR_020640|||http://purl.uniprot.org/annotation/VAR_020641|||http://purl.uniprot.org/annotation/VAR_020642|||http://purl.uniprot.org/annotation/VAR_027401|||http://purl.uniprot.org/annotation/VAR_027402|||http://purl.uniprot.org/annotation/VAR_027403|||http://purl.uniprot.org/annotation/VAR_027404|||http://purl.uniprot.org/annotation/VAR_053560|||http://purl.uniprot.org/annotation/VAR_053561|||http://purl.uniprot.org/annotation/VAR_053562
http://togogenome.org/gene/9606:STYX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUJ0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Confers phosphatase activity. Dephosphorylates MAPK1. Does not affect interaction with FBXW7 and nuclear localization.|||Disordered|||Increases interaction with FBXW7.|||Interaction with FBXW7|||Loss of interaction with FBXW7. Does not affect interaction with MAPK1 and nuclear localization.|||Phosphoserine|||Serine/threonine/tyrosine-interacting protein|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094950
http://togogenome.org/gene/9606:NUGGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear GTPase SLIP-GC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299479|||http://purl.uniprot.org/annotation/VAR_034823|||http://purl.uniprot.org/annotation/VAR_034824|||http://purl.uniprot.org/annotation/VAR_034825|||http://purl.uniprot.org/annotation/VAR_034826|||http://purl.uniprot.org/annotation/VAR_056814
http://togogenome.org/gene/9606:KCTD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MP8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD7|||Disordered|||In EPM3.|||In EPM3; results in markedly diminished localization at the cell membrane and appearance of prominent cytoplasmic aggregates.|||In EPM3; uncertain pathological significance.|||In isoform 2.|||Probable disease-associated variant found in a patient with opsoclonus-myoclonus ataxia-like syndrome.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251476|||http://purl.uniprot.org/annotation/VAR_068775|||http://purl.uniprot.org/annotation/VAR_068776|||http://purl.uniprot.org/annotation/VAR_068777|||http://purl.uniprot.org/annotation/VAR_068778|||http://purl.uniprot.org/annotation/VAR_068779|||http://purl.uniprot.org/annotation/VAR_068780|||http://purl.uniprot.org/annotation/VSP_020760
http://togogenome.org/gene/9606:MOCS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95396                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes sulfurtransferase activity.|||Adenylyltransferase and sulfurtransferase MOCS3|||Cysteine persulfide|||Cysteine persulfide intermediate; for sulfurtransferase activity|||Does not affect sulfurtransferase activity.|||Does not affect sulfurtransferase specificity and activity.|||Glycyl thioester intermediate; for adenylyltransferase activity|||Impairs sulfurtransferase activity.|||Interaction with NFS1|||Results in 470-fold increased activity.|||Results in 90-fold increased activity.|||Rhodanese                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120583|||http://purl.uniprot.org/annotation/VAR_049349
http://togogenome.org/gene/9606:DNTTIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H147                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  A.T hook|||Basic and acidic residues|||Deoxynucleotidyltransferase terminal-interacting protein 1|||Disordered|||H-T-H motif|||Important for DNA and nucleosome binding|||Important for dimerization|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072473|||http://purl.uniprot.org/annotation/VAR_014956
http://togogenome.org/gene/9606:MARCHF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5K0|||http://purl.uniprot.org/uniprot/B7ZAR7|||http://purl.uniprot.org/uniprot/F5H6W4|||http://purl.uniprot.org/uniprot/Q9H992                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase MARCHF7|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274415|||http://purl.uniprot.org/annotation/VAR_030284|||http://purl.uniprot.org/annotation/VAR_030285|||http://purl.uniprot.org/annotation/VAR_030286|||http://purl.uniprot.org/annotation/VSP_054406
http://togogenome.org/gene/9606:GABRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34903                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder and no epileptic seizures; unknown pathological significance.|||Gamma-aminobutyric acid receptor subunit alpha-3|||Helical|||In EPILX2.|||In EPILX2; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000437|||http://purl.uniprot.org/annotation/VAR_087845|||http://purl.uniprot.org/annotation/VAR_087846|||http://purl.uniprot.org/annotation/VAR_087847|||http://purl.uniprot.org/annotation/VAR_087848|||http://purl.uniprot.org/annotation/VAR_087849
http://togogenome.org/gene/9606:AP3D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14617                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP-3 complex subunit delta-1|||Basic and acidic residues|||Basic residues|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193766|||http://purl.uniprot.org/annotation/VAR_033517|||http://purl.uniprot.org/annotation/VAR_033518|||http://purl.uniprot.org/annotation/VSP_000165|||http://purl.uniprot.org/annotation/VSP_000166|||http://purl.uniprot.org/annotation/VSP_000167|||http://purl.uniprot.org/annotation/VSP_000168|||http://purl.uniprot.org/annotation/VSP_017106
http://togogenome.org/gene/9606:SKA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX90                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Spindle and kinetochore-associated protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089878|||http://purl.uniprot.org/annotation/VAR_023113|||http://purl.uniprot.org/annotation/VAR_057831|||http://purl.uniprot.org/annotation/VAR_057832|||http://purl.uniprot.org/annotation/VSP_037245|||http://purl.uniprot.org/annotation/VSP_040527|||http://purl.uniprot.org/annotation/VSP_040528
http://togogenome.org/gene/9606:PCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTT2|||http://purl.uniprot.org/uniprot/Q16822                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoenolpyruvate carboxykinase C-terminal P-loop|||Phosphoenolpyruvate carboxykinase GTP-utilising N-terminal|||Phosphoenolpyruvate carboxykinase [GTP], mitochondrial|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023568|||http://purl.uniprot.org/annotation/VAR_042445|||http://purl.uniprot.org/annotation/VAR_042446|||http://purl.uniprot.org/annotation/VAR_042447|||http://purl.uniprot.org/annotation/VAR_056662|||http://purl.uniprot.org/annotation/VSP_038783|||http://purl.uniprot.org/annotation/VSP_059389
http://togogenome.org/gene/9606:LTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01374|||http://purl.uniprot.org/uniprot/Q5STV3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In allele 8.1.|||In allele TNFB*2.|||Lymphotoxin-alpha|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine; partial|||TNF family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000048|||http://purl.uniprot.org/annotation/PRO_0000034463|||http://purl.uniprot.org/annotation/PRO_5014309953|||http://purl.uniprot.org/annotation/VAR_007511|||http://purl.uniprot.org/annotation/VAR_007512|||http://purl.uniprot.org/annotation/VAR_013023|||http://purl.uniprot.org/annotation/VAR_013024
http://togogenome.org/gene/9606:S100G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29377                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||N-acetylserine|||Phosphoserine|||Protein S100-G|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144027
http://togogenome.org/gene/9606:BRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92994|||http://purl.uniprot.org/uniprot/V9HVY2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||Acidic residues|||Disordered|||In CFDS.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9.|||Phosphoserine|||Phosphothreonine|||TFIIB-type|||Transcription factor IIIB 90 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119347|||http://purl.uniprot.org/annotation/VAR_035723|||http://purl.uniprot.org/annotation/VAR_072710|||http://purl.uniprot.org/annotation/VAR_072711|||http://purl.uniprot.org/annotation/VAR_072712|||http://purl.uniprot.org/annotation/VAR_072713|||http://purl.uniprot.org/annotation/VSP_006396|||http://purl.uniprot.org/annotation/VSP_006397|||http://purl.uniprot.org/annotation/VSP_006398|||http://purl.uniprot.org/annotation/VSP_006399|||http://purl.uniprot.org/annotation/VSP_006400|||http://purl.uniprot.org/annotation/VSP_014697|||http://purl.uniprot.org/annotation/VSP_043835|||http://purl.uniprot.org/annotation/VSP_043836|||http://purl.uniprot.org/annotation/VSP_044244|||http://purl.uniprot.org/annotation/VSP_045045|||http://purl.uniprot.org/annotation/VSP_045046
http://togogenome.org/gene/9606:SPNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2V7                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Protein spinster homolog 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305039|||http://purl.uniprot.org/annotation/VAR_035157|||http://purl.uniprot.org/annotation/VSP_028194|||http://purl.uniprot.org/annotation/VSP_028195|||http://purl.uniprot.org/annotation/VSP_028196|||http://purl.uniprot.org/annotation/VSP_036389
http://togogenome.org/gene/9606:KLF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JT82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 17|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047555|||http://purl.uniprot.org/annotation/VAR_026198|||http://purl.uniprot.org/annotation/VAR_052719|||http://purl.uniprot.org/annotation/VAR_052720|||http://purl.uniprot.org/annotation/VAR_052721
http://togogenome.org/gene/9606:ANKMY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV38                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat and MYND domain-containing protein 2|||Basic and acidic residues|||Disordered|||MYND-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247166
http://togogenome.org/gene/9606:ATP1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05023                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CMT2DD; no effect on Na(+)-dependent currents.|||In CMT2DD; shows fewer Na(+)-dependent currents than wild-type protein.|||In CMT2DD; unknown pathological significance.|||In CMT2DD; unknown pathological significance; requires 2 nucleotide substitutions.|||In HOMGSMR2; results in altered sodium and potassium transport as shown by in vitro functional expression of the homologous rat variant.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoinositide-3 kinase binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Sodium/potassium-transporting ATPase subunit alpha-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002483|||http://purl.uniprot.org/annotation/PRO_0000002484|||http://purl.uniprot.org/annotation/VAR_048374|||http://purl.uniprot.org/annotation/VAR_081039|||http://purl.uniprot.org/annotation/VAR_081040|||http://purl.uniprot.org/annotation/VAR_081041|||http://purl.uniprot.org/annotation/VAR_081042|||http://purl.uniprot.org/annotation/VAR_081043|||http://purl.uniprot.org/annotation/VAR_081044|||http://purl.uniprot.org/annotation/VAR_081045|||http://purl.uniprot.org/annotation/VAR_081937|||http://purl.uniprot.org/annotation/VAR_081938|||http://purl.uniprot.org/annotation/VAR_081939|||http://purl.uniprot.org/annotation/VSP_000415|||http://purl.uniprot.org/annotation/VSP_000416|||http://purl.uniprot.org/annotation/VSP_044242|||http://purl.uniprot.org/annotation/VSP_047309
http://togogenome.org/gene/9606:HBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D1MGQ2|||http://purl.uniprot.org/uniprot/P69905                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by N.americanus apr-2|||Causes alpha-thalassemia.|||Globin family profile|||Hemoglobin subunit alpha|||Hemopressin|||In Adana; unstable; causes alpha-thalassemia.|||In Aichi; slightly unstable.|||In Al-Ain Abu Dhabi.|||In Anantharaj.|||In Ann Arbor; unstable.|||In Atago; O(2) affinity up.|||In Attleboro; O(2) affinity up.|||In Auckland; unstable.|||In Aztec.|||In Bari.|||In Bassett; markedly reduced oxygen affinity.|||In Beijing.|||In Bibba; unstable; causes alpha-thalassemia.|||In Boghe.|||In Bourmedes.|||In Broomfield.|||In Campinas.|||In Catonsville.|||In Cemenelum; O(2) affinity up.|||In Chad.|||In Chapel Hill.|||In Charolles.|||In Chiapas.|||In Chicago.|||In ChongQing; O(2) affinity up.|||In Clinic; unstable; causes alpha-thalassemia.|||In Contaldo; unstable.|||In Cordele; unstable.|||In Dallas; O(2) affinity up.|||In Daneskgah-Teheran.|||In Davenport.|||In Denmark Hill; O(2) affinity up.|||In Duan.|||In Dunn; O(2) affinity up.|||In Etobicoke; O(2) affinity up.|||In Evans; unstable.|||In Evanston; O(2) affinity up.|||In Ferndown; O(2) affinity up.|||In Fontainebleau.|||In Fort Worth.|||In Fort de France; O(2) affinity up.|||In Fukutomi; O(2) affinity up.|||In G-Pest.|||In G-Philadelphia.|||In Garden State.|||In Godavari; O(2) affinity up.|||In Grady.|||In Guizhou.|||In HBH; hemoglobin Aghia Sophia.|||In Hanamaki; O(2) affinity up.|||In Handa; O(2) affinity up.|||In Handsworth.|||In Harbin; slightly unstable.|||In Hasharon/Sinai; unstable.|||In Hekinan.|||In Hikoshima/Shimonoseki.|||In Hirosaki; unstable.|||In Hobart.|||In Hopkins-II; unstable.|||In Inkster; O(2) affinity up.|||In Iwata; unstable.|||In J-Abidjan.|||In J-Anatolia.|||In J-Buda.|||In J-Cape Town; O(2) affinity up.|||In J-Habana.|||In J-Kurosh.|||In J-Medellin.|||In J-Meerut/J-Birmingham.|||In J-Nyanza.|||In J-Paris 1/J-Aljezur.|||In J-Rovigo; unstable.|||In J-Tashikuergan.|||In J-Tongariki.|||In J-Toronto.|||In Jackson.|||In Kanagawa; O(2) affinity up.|||In Karachi.|||In Kawachi; O(2) affinity up.|||In Kokura; also in Umi/Michigan; unstable.|||In Kurdistan.|||In Kurosaki.|||In L-Persian Gulf.|||In Le Lamentin.|||In Legnano; O(2) affinity up.|||In Lille.|||In Loire; O(2) affinity up.|||In Luxembourg; unstable.|||In M-Boston/M-Osaka; O(2) affinity down.|||In Manitoba; slightly unstable.|||In Melusine.|||In Milledgeville; O(2) affinity up.|||In Miyano; O(2) affinity up.|||In Moabit; unstable.|||In Montefiore; O(2) affinity up.|||In Montgomery.|||In Nigeria.|||In Noko.|||In Nouakchott.|||In Nunobiki; O(2) affinity up.|||In O-Padova.|||In Ottawa/Siam.|||In Owari.|||In Ozieri.|||In Pavie.|||In Persepolis.|||In Petah Tikva; unstable; causes alpha-thalassemia.|||In Phnom Penh.|||In Plasencia; family with moderate microcytosis and hypochromia.|||In Pontoise; unstable.|||In Port Huron.|||In Port Phillip; unstable.|||In Prato; unstable.|||In Q-Iran.|||In Queens/Ogi.|||In Questembert; highly unstable; causes alpha-thalassemia.|||In Quong Sze; causes alpha-thalassemia.|||In Ravenscourt Park; causes alpha-thalassemia.|||In Reims; slightly unstable.|||In Rouen/Ethiopia; O(2) affinity up.|||In Russ.|||In Savaria.|||In Sawara; O(2) affinity up.|||In Setif; unstable.|||In Shenyang; unstable.|||In Singapore.|||In Spanish town.|||In Stanleyville-2.|||In Suan-Dok; unstable; causes alpha-thalassemia.|||In Sun Prairie; unstable.|||In Suresnes; O(2) affinity up.|||In Swan River.|||In Thailand.|||In Thionville; O(2) affinity down.|||In Tokoname; O(2) affinity up.|||In Tottori; unstable.|||In Toyama.|||In Tunis-Bizerte; unstable; causes alpha-thalassemia.|||In Turriff.|||In Twin Peaks.|||In Ube-4.|||In Val de Marne; O(2) affinity up.|||In West One.|||In Westmead.|||In Woodville; O(2) affinity up.|||In Yuda; O(2) affinity down.|||In Zaire.|||In Zambia.|||N-linked (Glc) (glycation) lysine|||N-linked (Glc) (glycation) lysine; alternate|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Not glycated|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||distal binding residue|||proximal binding residue ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052653|||http://purl.uniprot.org/annotation/PRO_0000455882|||http://purl.uniprot.org/annotation/VAR_002719|||http://purl.uniprot.org/annotation/VAR_002720|||http://purl.uniprot.org/annotation/VAR_002721|||http://purl.uniprot.org/annotation/VAR_002722|||http://purl.uniprot.org/annotation/VAR_002723|||http://purl.uniprot.org/annotation/VAR_002724|||http://purl.uniprot.org/annotation/VAR_002725|||http://purl.uniprot.org/annotation/VAR_002726|||http://purl.uniprot.org/annotation/VAR_002727|||http://purl.uniprot.org/annotation/VAR_002728|||http://purl.uniprot.org/annotation/VAR_002729|||http://purl.uniprot.org/annotation/VAR_002730|||http://purl.uniprot.org/annotation/VAR_002731|||http://purl.uniprot.org/annotation/VAR_002732|||http://purl.uniprot.org/annotation/VAR_002733|||http://purl.uniprot.org/annotation/VAR_002734|||http://purl.uniprot.org/annotation/VAR_002735|||http://purl.uniprot.org/annotation/VAR_002736|||http://purl.uniprot.org/annotation/VAR_002737|||http://purl.uniprot.org/annotation/VAR_002738|||http://purl.uniprot.org/annotation/VAR_002739|||http://purl.uniprot.org/annotation/VAR_002740|||http://purl.uniprot.org/annotation/VAR_002741|||http://purl.uniprot.org/annotation/VAR_002742|||http://purl.uniprot.org/annotation/VAR_002743|||http://purl.uniprot.org/annotation/VAR_002744|||http://purl.uniprot.org/annotation/VAR_002745|||http://purl.uniprot.org/annotation/VAR_002746|||http://purl.uniprot.org/annotation/VAR_002747|||http://purl.uniprot.org/annotation/VAR_002748|||http://purl.uniprot.org/annotation/VAR_002749|||http://purl.uniprot.org/annotation/VAR_002750|||http://purl.uniprot.org/annotation/VAR_002751|||http://purl.uniprot.org/annotation/VAR_002752|||http://purl.uniprot.org/annotation/VAR_002753|||http://purl.uniprot.org/annotation/VAR_002754|||http://purl.uniprot.org/annotation/VAR_002755|||http://purl.uniprot.org/annotation/VAR_002756|||http://purl.uniprot.org/annotation/VAR_002757|||http://purl.uniprot.org/annotation/VAR_002758|||http://purl.uniprot.org/annotation/VAR_002759|||http://purl.uniprot.org/annotation/VAR_002760|||http://purl.uniprot.org/annotation/VAR_002761|||http://purl.uniprot.org/annotation/VAR_002762|||http://purl.uniprot.org/annotation/VAR_002763|||http://purl.uniprot.org/annotation/VAR_002764|||http://purl.uniprot.org/annotation/VAR_002765|||http://purl.uniprot.org/annotation/VAR_002766|||http://purl.uniprot.org/annotation/VAR_002767|||http://purl.uniprot.org/annotation/VAR_002768|||http://purl.uniprot.org/annotation/VAR_002769|||http://purl.uniprot.org/annotation/VAR_002770|||http://purl.uniprot.org/annotation/VAR_002771|||http://purl.uniprot.org/annotation/VAR_002772|||http://purl.uniprot.org/annotation/VAR_002773|||http://purl.uniprot.org/annotation/VAR_002774|||http://purl.uniprot.org/annotation/VAR_002775|||http://purl.uniprot.org/annotation/VAR_002776|||http://purl.uniprot.org/annotation/VAR_002777|||http://purl.uniprot.org/annotation/VAR_002778|||http://purl.uniprot.org/annotation/VAR_002779|||http://purl.uniprot.org/annotation/VAR_002780|||http://purl.uniprot.org/annotation/VAR_002781|||http://purl.uniprot.org/annotation/VAR_002782|||http://purl.uniprot.org/annotation/VAR_002783|||http://purl.uniprot.org/annotation/VAR_002784|||http://purl.uniprot.org/annotation/VAR_002785|||http://purl.uniprot.org/annotation/VAR_002786|||http://purl.uniprot.org/annotation/VAR_002787|||http://purl.uniprot.org/annotation/VAR_002788|||http://purl.uniprot.org/annotation/VAR_002789|||http://purl.uniprot.org/annotation/VAR_002790|||http://purl.uniprot.org/annotation/VAR_002791|||http://purl.uniprot.org/annotation/VAR_002792|||http://purl.uniprot.org/annotation/VAR_002793|||http://purl.uniprot.org/annotation/VAR_002794|||http://purl.uniprot.org/annotation/VAR_002795|||http://purl.uniprot.org/annotation/VAR_002796|||http://purl.uniprot.org/annotation/VAR_002797|||http://purl.uniprot.org/annotation/VAR_002798|||http://purl.uniprot.org/annotation/VAR_002799|||http://purl.uniprot.org/annotation/VAR_002800|||http://purl.uniprot.org/annotation/VAR_002801|||http://purl.uniprot.org/annotation/VAR_002802|||http://purl.uniprot.org/annotation/VAR_002803|||http://purl.uniprot.org/annotation/VAR_002804|||http://purl.uniprot.org/annotation/VAR_002805|||http://purl.uniprot.org/annotation/VAR_002806|||http://purl.uniprot.org/annotation/VAR_002807|||http://purl.uniprot.org/annotation/VAR_002808|||http://purl.uniprot.org/annotation/VAR_002809|||http://purl.uniprot.org/annotation/VAR_002810|||http://purl.uniprot.org/annotation/VAR_002811|||http://purl.uniprot.org/annotation/VAR_002812|||http://purl.uniprot.org/annotation/VAR_002813|||http://purl.uniprot.org/annotation/VAR_002814|||http://purl.uniprot.org/annotation/VAR_002815|||http://purl.uniprot.org/annotation/VAR_002816|||http://purl.uniprot.org/annotation/VAR_002817|||http://purl.uniprot.org/annotation/VAR_002818|||http://purl.uniprot.org/annotation/VAR_002819|||http://purl.uniprot.org/annotation/VAR_002820|||http://purl.uniprot.org/annotation/VAR_002821|||http://purl.uniprot.org/annotation/VAR_002822|||http://purl.uniprot.org/annotation/VAR_002823|||http://purl.uniprot.org/annotation/VAR_002824|||http://purl.uniprot.org/annotation/VAR_002825|||http://purl.uniprot.org/annotation/VAR_002826|||http://purl.uniprot.org/annotation/VAR_002827|||http://purl.uniprot.org/annotation/VAR_002828|||http://purl.uniprot.org/annotation/VAR_002829|||http://purl.uniprot.org/annotation/VAR_002830|||http://purl.uniprot.org/annotation/VAR_002831|||http://purl.uniprot.org/annotation/VAR_002832|||http://purl.uniprot.org/annotation/VAR_002833|||http://purl.uniprot.org/annotation/VAR_002834|||http://purl.uniprot.org/annotation/VAR_002835|||http://purl.uniprot.org/annotation/VAR_002836|||http://purl.uniprot.org/annotation/VAR_002837|||http://purl.uniprot.org/annotation/VAR_002838|||http://purl.uniprot.org/annotation/VAR_002839|||http://purl.uniprot.org/annotation/VAR_002840|||http://purl.uniprot.org/annotation/VAR_002841|||http://purl.uniprot.org/annotation/VAR_002842|||http://purl.uniprot.org/annotation/VAR_002843|||http://purl.uniprot.org/annotation/VAR_002844|||http://purl.uniprot.org/annotation/VAR_002845|||http://purl.uniprot.org/annotation/VAR_002846|||http://purl.uniprot.org/annotation/VAR_002847|||http://purl.uniprot.org/annotation/VAR_002848|||http://purl.uniprot.org/annotation/VAR_002849|||http://purl.uniprot.org/annotation/VAR_002850|||http://purl.uniprot.org/annotation/VAR_002851|||http://purl.uniprot.org/annotation/VAR_002852|||http://purl.uniprot.org/annotation/VAR_002853|||http://purl.uniprot.org/annotation/VAR_002854|||http://purl.uniprot.org/annotation/VAR_002855|||http://purl.uniprot.org/annotation/VAR_012662|||http://purl.uniprot.org/annotation/VAR_020775|||http://purl.uniprot.org/annotation/VAR_025002|||http://purl.uniprot.org/annotation/VAR_025387|||http://purl.uniprot.org/annotation/VAR_025388|||http://purl.uniprot.org/annotation/VAR_025389|||http://purl.uniprot.org/annotation/VAR_025390|||http://purl.uniprot.org/annotation/VAR_025391|||http://purl.uniprot.org/annotation/VAR_025392|||http://purl.uniprot.org/annotation/VAR_035242|||http://purl.uniprot.org/annotation/VAR_038149|||http://purl.uniprot.org/annotation/VAR_038150|||http://purl.uniprot.org/annotation/VAR_049272|||http://purl.uniprot.org/annotation/VAR_066401
http://togogenome.org/gene/9606:DDX52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM65|||http://purl.uniprot.org/uniprot/Q9Y2R4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Probable ATP-dependent RNA helicase DDX52|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055060|||http://purl.uniprot.org/annotation/VAR_060235
http://togogenome.org/gene/9606:OR4D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15615                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150537|||http://purl.uniprot.org/annotation/VAR_057546|||http://purl.uniprot.org/annotation/VAR_060479
http://togogenome.org/gene/9606:PSMB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2I4|||http://purl.uniprot.org/uniprot/P28072|||http://purl.uniprot.org/uniprot/Q6IAT9                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylalanine|||Nucleophile|||Phosphothreonine|||Proteasome subunit beta type-6|||Removed|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026613|||http://purl.uniprot.org/annotation/PRO_0000026614|||http://purl.uniprot.org/annotation/VAR_020030
http://togogenome.org/gene/9606:NCEH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTJ9|||http://purl.uniprot.org/uniprot/Q6PIU2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha/beta hydrolase fold-3|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||Lumenal|||N-linked (GlcNAc...) asparagine|||Neutral cholesterol ester hydrolase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265939|||http://purl.uniprot.org/annotation/VAR_047099|||http://purl.uniprot.org/annotation/VAR_047100|||http://purl.uniprot.org/annotation/VAR_047101|||http://purl.uniprot.org/annotation/VSP_037518|||http://purl.uniprot.org/annotation/VSP_037519
http://togogenome.org/gene/9606:TPD52L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYR3|||http://purl.uniprot.org/uniprot/A0A087WZ51|||http://purl.uniprot.org/uniprot/O43399|||http://purl.uniprot.org/uniprot/Q68E05|||http://purl.uniprot.org/uniprot/Q6FGS1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 7.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tumor protein D54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185744|||http://purl.uniprot.org/annotation/VSP_006547|||http://purl.uniprot.org/annotation/VSP_036756|||http://purl.uniprot.org/annotation/VSP_038361|||http://purl.uniprot.org/annotation/VSP_045154|||http://purl.uniprot.org/annotation/VSP_047409
http://togogenome.org/gene/9606:FCRL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PJ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Breakpoint for insertion to form FCRL4-IGHA1 fusion protein|||Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 4|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||Loss of function, phosphorylation and interaction with PTPN6 and PTPN11.|||Loss of interaction with PTPN6 and PTPN11 and partial loss of function and phosphorylation.|||N-linked (GlcNAc...) asparagine|||No effect on function, phosphorylation and interaction with PTPN6 and PTPN11.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331642|||http://purl.uniprot.org/annotation/VAR_042929|||http://purl.uniprot.org/annotation/VAR_042930|||http://purl.uniprot.org/annotation/VAR_042931|||http://purl.uniprot.org/annotation/VAR_042932|||http://purl.uniprot.org/annotation/VSP_033310
http://togogenome.org/gene/9606:EPHA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29322                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 8|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Mediates interaction with ANKS1A and ANKS1B|||Mediates interaction with PIK3CG and required for endocytosis|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016822|||http://purl.uniprot.org/annotation/VAR_022107|||http://purl.uniprot.org/annotation/VAR_024514|||http://purl.uniprot.org/annotation/VAR_042153|||http://purl.uniprot.org/annotation/VAR_042154|||http://purl.uniprot.org/annotation/VAR_042155|||http://purl.uniprot.org/annotation/VAR_042156|||http://purl.uniprot.org/annotation/VAR_042157|||http://purl.uniprot.org/annotation/VAR_042158|||http://purl.uniprot.org/annotation/VAR_061292|||http://purl.uniprot.org/annotation/VSP_041946|||http://purl.uniprot.org/annotation/VSP_041947
http://togogenome.org/gene/9606:SKP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13309                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||F-box|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Mediates interaction with IFI27|||Mediates interaction with hepatitis C virus non-structural protein NS5A|||N6-acetyllysine; by p300/EP300|||Nuclear localization signal|||Phosphoserine|||S-phase kinase-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119954|||http://purl.uniprot.org/annotation/VAR_016984|||http://purl.uniprot.org/annotation/VAR_016985|||http://purl.uniprot.org/annotation/VSP_008432|||http://purl.uniprot.org/annotation/VSP_044931|||http://purl.uniprot.org/annotation/VSP_044932
http://togogenome.org/gene/9606:PIAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75925                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3; approximate|||4 X 4 AA repeats of N-T-S-L|||4; approximate|||Cleavage; by caspase-3, -6, and -8|||Cleavage; by caspase-6 and -8|||Completely blocks cleavage by caspase-3, -6, and -8 and dramatic suppression of EBVDNA replication; when associated with A-100.|||Completely blocks cleavage by caspase-3, -6, and -8 and dramatic suppression of EBVDNA replication; when associated with A-433.|||Disordered|||E3 SUMO-protein ligase PIAS1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||LXXLL motif|||Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding.|||N-acetylalanine|||No effect on cleavages by caspase-6 and -8.|||Nuclear localization signal|||PINIT|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Required for interaction with MSX1|||SAP|||SP-RING-type|||SUMO1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218974|||http://purl.uniprot.org/annotation/VSP_056219|||http://purl.uniprot.org/annotation/VSP_057195|||http://purl.uniprot.org/annotation/VSP_057196
http://togogenome.org/gene/9606:FLNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21333|||http://purl.uniprot.org/uniprot/Q60FE5|||http://purl.uniprot.org/uniprot/Q6NXF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-135.|||Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-42 and R-43.|||Abrogates ASB2alpha-mediated degradation without altering ASB2alpha binding; when associated with R-43 and R-135.|||Actin-binding|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cleavage; by calpain|||Disordered|||Filamin|||Filamin 1|||Filamin 10|||Filamin 11|||Filamin 12|||Filamin 13|||Filamin 14|||Filamin 15|||Filamin 16|||Filamin 17|||Filamin 18|||Filamin 19|||Filamin 2|||Filamin 20|||Filamin 21|||Filamin 22|||Filamin 23|||Filamin 24|||Filamin 3|||Filamin 4|||Filamin 5|||Filamin 6|||Filamin 7|||Filamin 8|||Filamin 9|||Filamin-A|||Found in a child with developmental disabilities; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hinge 1|||Hinge 2|||In CVDPX.|||In FGS2.|||In FMD1.|||In FMD1; does not inhibit interaction with MIS18BP1.|||In FMD1; unknown pathological significance.|||In MNS.|||In MNS; does not inhibit interaction with MIS18BP1.|||In MNS; unknown pathological significance.|||In OPD1.|||In OPD1; unknown pathological significance.|||In OPD2.|||In OPD2; unknown pathological significance.|||In PVNH1.|||In TOD.|||In isoform 2.|||In otopalatodigital spectrum disorder.|||Interaction with furin|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with macrothrombocytopenia.|||Removed|||Self-association site, tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087296|||http://purl.uniprot.org/annotation/VAR_012831|||http://purl.uniprot.org/annotation/VAR_012832|||http://purl.uniprot.org/annotation/VAR_012833|||http://purl.uniprot.org/annotation/VAR_012834|||http://purl.uniprot.org/annotation/VAR_012835|||http://purl.uniprot.org/annotation/VAR_015699|||http://purl.uniprot.org/annotation/VAR_015700|||http://purl.uniprot.org/annotation/VAR_015701|||http://purl.uniprot.org/annotation/VAR_015702|||http://purl.uniprot.org/annotation/VAR_015703|||http://purl.uniprot.org/annotation/VAR_015704|||http://purl.uniprot.org/annotation/VAR_015713|||http://purl.uniprot.org/annotation/VAR_015714|||http://purl.uniprot.org/annotation/VAR_015715|||http://purl.uniprot.org/annotation/VAR_015716|||http://purl.uniprot.org/annotation/VAR_015717|||http://purl.uniprot.org/annotation/VAR_015718|||http://purl.uniprot.org/annotation/VAR_015719|||http://purl.uniprot.org/annotation/VAR_015720|||http://purl.uniprot.org/annotation/VAR_015721|||http://purl.uniprot.org/annotation/VAR_015722|||http://purl.uniprot.org/annotation/VAR_015723|||http://purl.uniprot.org/annotation/VAR_022734|||http://purl.uniprot.org/annotation/VAR_031305|||http://purl.uniprot.org/annotation/VAR_031306|||http://purl.uniprot.org/annotation/VAR_031307|||http://purl.uniprot.org/annotation/VAR_031308|||http://purl.uniprot.org/annotation/VAR_031309|||http://purl.uniprot.org/annotation/VAR_031310|||http://purl.uniprot.org/annotation/VAR_031311|||http://purl.uniprot.org/annotation/VAR_031312|||http://purl.uniprot.org/annotation/VAR_032083|||http://purl.uniprot.org/annotation/VAR_058720|||http://purl.uniprot.org/annotation/VAR_058721|||http://purl.uniprot.org/annotation/VAR_064156|||http://purl.uniprot.org/annotation/VAR_064157|||http://purl.uniprot.org/annotation/VAR_064158|||http://purl.uniprot.org/annotation/VAR_064159|||http://purl.uniprot.org/annotation/VAR_067251|||http://purl.uniprot.org/annotation/VAR_069803|||http://purl.uniprot.org/annotation/VAR_076500|||http://purl.uniprot.org/annotation/VAR_076501|||http://purl.uniprot.org/annotation/VAR_076502|||http://purl.uniprot.org/annotation/VAR_076503|||http://purl.uniprot.org/annotation/VAR_076504|||http://purl.uniprot.org/annotation/VAR_076505|||http://purl.uniprot.org/annotation/VAR_076506|||http://purl.uniprot.org/annotation/VAR_085766|||http://purl.uniprot.org/annotation/VSP_035454
http://togogenome.org/gene/9606:RNF217                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVC8|||http://purl.uniprot.org/uniprot/Q8TC41                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF217|||Helical|||IBR-type|||In isoform 2.|||Polar residues|||Pro residues|||RING-type|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084128|||http://purl.uniprot.org/annotation/VAR_024160|||http://purl.uniprot.org/annotation/VSP_054705|||http://purl.uniprot.org/annotation/VSP_054706
http://togogenome.org/gene/9606:TKTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC2|||http://purl.uniprot.org/uniprot/Q9H0I9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Important for catalytic activity|||Proton donor|||Transketolase-like protein 2|||Transketolase-like pyrimidine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285200|||http://purl.uniprot.org/annotation/VAR_031990|||http://purl.uniprot.org/annotation/VAR_031991
http://togogenome.org/gene/9606:VPS26C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14972                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Vacuolar protein sorting-associated protein 26C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073016|||http://purl.uniprot.org/annotation/VSP_056598
http://togogenome.org/gene/9606:CCDC154                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI56                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 154                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332270
http://togogenome.org/gene/9606:MCTP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DN12                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||C2 3|||Disordered|||Found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance.|||Found in a patient with left-sided obstructive cardiac lesions; unknown pathological significance; alters Ca(2+)-binding affinity.|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Multiple C2 and transmembrane domain-containing protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294472|||http://purl.uniprot.org/annotation/VAR_033190|||http://purl.uniprot.org/annotation/VAR_073421|||http://purl.uniprot.org/annotation/VAR_073422|||http://purl.uniprot.org/annotation/VAR_073423|||http://purl.uniprot.org/annotation/VAR_073424|||http://purl.uniprot.org/annotation/VAR_073425|||http://purl.uniprot.org/annotation/VAR_073426|||http://purl.uniprot.org/annotation/VAR_073427|||http://purl.uniprot.org/annotation/VSP_026662|||http://purl.uniprot.org/annotation/VSP_026664|||http://purl.uniprot.org/annotation/VSP_026665|||http://purl.uniprot.org/annotation/VSP_026666|||http://purl.uniprot.org/annotation/VSP_038981|||http://purl.uniprot.org/annotation/VSP_038982
http://togogenome.org/gene/9606:CUTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60888                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform A.|||In isoform C.|||O-glycosylated at one site|||Protein CutA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006379|||http://purl.uniprot.org/annotation/VSP_013225|||http://purl.uniprot.org/annotation/VSP_013226
http://togogenome.org/gene/9606:OR4C11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN6|||http://purl.uniprot.org/uniprot/Q6IEV9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150532|||http://purl.uniprot.org/annotation/VAR_057543|||http://purl.uniprot.org/annotation/VAR_057544|||http://purl.uniprot.org/annotation/VAR_057545
http://togogenome.org/gene/9606:CCL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16627                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 14|||HCC-1(3-74)|||HCC-1(4-74)|||HCC-1(9-74)|||In isoform HCC-3.|||O-linked (GalNAc...) serine; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005204|||http://purl.uniprot.org/annotation/PRO_0000005205|||http://purl.uniprot.org/annotation/PRO_0000005206|||http://purl.uniprot.org/annotation/PRO_0000005207|||http://purl.uniprot.org/annotation/VAR_048707|||http://purl.uniprot.org/annotation/VSP_001060
http://togogenome.org/gene/9606:SLC11A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with susceptibility to infection with Mycobacterium ulcerans.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Natural resistance-associated macrophage protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212588|||http://purl.uniprot.org/annotation/VAR_004629|||http://purl.uniprot.org/annotation/VAR_004630|||http://purl.uniprot.org/annotation/VAR_004631|||http://purl.uniprot.org/annotation/VSP_047875|||http://purl.uniprot.org/annotation/VSP_047876
http://togogenome.org/gene/9606:KRTAP16-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUX0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||11 X 5 AA repeats of C-C-X(3)|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||Keratin-associated protein 16-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348959
http://togogenome.org/gene/9606:NUP210                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEM1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BIG2|||Confirmed at protein level.|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nuclear pore membrane glycoprotein 210|||Perinuclear space|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236046|||http://purl.uniprot.org/annotation/VAR_026474|||http://purl.uniprot.org/annotation/VAR_026475|||http://purl.uniprot.org/annotation/VAR_026476|||http://purl.uniprot.org/annotation/VAR_028147|||http://purl.uniprot.org/annotation/VAR_028148|||http://purl.uniprot.org/annotation/VAR_028149|||http://purl.uniprot.org/annotation/VAR_028150|||http://purl.uniprot.org/annotation/VAR_028151|||http://purl.uniprot.org/annotation/VAR_028152|||http://purl.uniprot.org/annotation/VAR_028153|||http://purl.uniprot.org/annotation/VSP_018567|||http://purl.uniprot.org/annotation/VSP_018568
http://togogenome.org/gene/9606:SUPT5H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00267                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10 X 8 AA approximate tandem repeats of P-[TS]-P-S-P-[QA]-[SG]-Y, motif CTR2|||9 X 7 AA approximate tandem repeats of G-S-[QR]-T-P-X-[YQ], motif CTR1|||Acidic residues|||Asymmetric dimethylarginine; by PRMT1; alternate|||Basic and acidic residues|||CTR1-1; approximate|||CTR1-2|||CTR1-3|||CTR1-4|||CTR1-5|||CTR1-6|||CTR1-7|||CTR1-8|||CTR1-9|||CTR2-1|||CTR2-10|||CTR2-2; approximate|||CTR2-3; approximate|||CTR2-4; half-length|||CTR2-5; approximate|||CTR2-6|||CTR2-7; approximate|||CTR2-8|||CTR2-9|||Defective in regulation of transcriptional elongation.|||Disordered|||Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698.|||Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698.|||Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696.|||Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698.|||Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698.|||Interaction with RNA polymerase II|||Interaction with SUPT4H1|||KOW 1|||KOW 2|||KOW 3|||KOW 4|||KOW 5|||N6-acetyllysine|||Omega-N-methylarginine; by PRMT1 and PRMT5; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK9|||Polar residues|||Pro residues|||Symmetric dimethylarginine; by PRMT5; alternate|||Transcription elongation factor SPT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208468|||http://purl.uniprot.org/annotation/VSP_016282
http://togogenome.org/gene/9606:PSMC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJS3|||http://purl.uniprot.org/uniprot/P62195                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  26S proteasome regulatory subunit 8|||AAA+ ATPase|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||May mediate interaction with PRPF9|||N-acetylalanine|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084721|||http://purl.uniprot.org/annotation/VAR_035901|||http://purl.uniprot.org/annotation/VAR_048119|||http://purl.uniprot.org/annotation/VSP_045441
http://togogenome.org/gene/9606:NCOA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R5V0|||http://purl.uniprot.org/uniprot/Q13772|||http://purl.uniprot.org/uniprot/Q96E88                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for rearrangement to form RET/PTC3 oncogene|||Decreased interaction with PPAR and RXR.|||Disordered|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform Beta.|||Nuclear coactivator|||Nuclear receptor coactivator 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094410|||http://purl.uniprot.org/annotation/VAR_009190|||http://purl.uniprot.org/annotation/VAR_009191|||http://purl.uniprot.org/annotation/VAR_009192|||http://purl.uniprot.org/annotation/VAR_009193|||http://purl.uniprot.org/annotation/VAR_014928|||http://purl.uniprot.org/annotation/VSP_003409|||http://purl.uniprot.org/annotation/VSP_046348|||http://purl.uniprot.org/annotation/VSP_046349
http://togogenome.org/gene/9606:ARSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFZ2|||http://purl.uniprot.org/uniprot/B4DVI5|||http://purl.uniprot.org/uniprot/P15289                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Abolishes enzyme activity.|||Abolishes formation of 3-oxoalanine (also known as C-formylglycine, FGly). Strongly decreases enzyme activity.|||Arylsulfatase A|||Arylsulfatase A component B|||Arylsulfatase A component C|||Disordered|||In MLD.|||In MLD; adult form.|||In MLD; adult type.|||In MLD; adult type; causes a severe reduction of enzyme activity.|||In MLD; adult type; enzyme activity reduced to 50% of wild-type enzyme.|||In MLD; adult-onset.|||In MLD; early-infantile form.|||In MLD; enzyme activity reduced to 0.6% of wild-type enzyme.|||In MLD; enzyme activity reduced to 15.6% of wild-type enzyme.|||In MLD; enzyme activity reduced to 2.4% of wild-type enzyme.|||In MLD; enzyme activity reduced to 2.8% of wild-type enzyme.|||In MLD; enzyme activity reduced to 4.7% of wild-type enzyme.|||In MLD; enzyme activity reduced to 5% of wild-type enzyme.|||In MLD; enzyme activity reduced to less than 1% of normal activity.|||In MLD; infantile form.|||In MLD; infantile-onset.|||In MLD; infantile-onset; causes a severe reduction of enzyme activity.|||In MLD; intermediate.|||In MLD; juvenile form.|||In MLD; juvenile-onset.|||In MLD; juvenile-onset; causes a severe reduction of enzyme activity.|||In MLD; juvenile-onset; results in highly reduced enzyme activity and stability; the mutant enzyme is kept in a prelysosomal compartment.|||In MLD; juvenile-onset; retains about 12% of specific enzyme activity; the mutant protein is unstable; results in more rapid enzyme degradation in lysosomes; addition of the cysteine protease inhibitor leupeptin increases the amount of the enzyme activity; displays a modest reduction in the octamerization process of the enzyme at low pH.|||In MLD; juvenile/adult-onset; generates 5% as much activity as the parallel normal control.|||In MLD; juvenile/adult-onset; mild; common mutation; decreased enzyme activity.|||In MLD; late-infantile and juvenile-onset.|||In MLD; late-infantile form.|||In MLD; late-infantile form; complete loss of enzyme activity.|||In MLD; late-infantile form; no enzyme residual activity.|||In MLD; late-infantile form; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment.|||In MLD; late-infantile-onset.|||In MLD; late-infantile-onset; enzyme activity reduced to less than 1%; the mutant protein is more rapidly degraded in lysosomes; strongly interferes with the octamerization process of the enzyme at low pH.|||In MLD; late-infantile-onset; loss of enzymatic activity.|||In MLD; late-infantile; decreased enzymatic activity.|||In MLD; late-onset.|||In MLD; loss of enzymatic activity.|||In MLD; low amounts of residual enzyme activity; leads to a decreased stability of the mutant enzyme.|||In MLD; mild.|||In MLD; no enzyme residual activity.|||In MLD; severe late-infantile type; loss of enzymatic activity.|||In MLD; severe.|||In MLD; severe; 13% of normal activity.|||In MLD; severe; 35% of normal activity.|||In MLD; severe; no enzyme residual activity.|||In MLD; severe; no enzyme residual activity; leads to a decreased stability of the mutant enzyme; causes an arrest of the mutant enzyme polypeptide in a prelysosomal compartment.|||In MLD; significantly lower activity than wild-type protein.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Often found in association with a nucleotide substitution in the polyadenylation signal downstream of the stop codon; this association defines an ARSA pseudodeficiency allele found in individuals with low enzymatic activities but no clinical manifestations; no effect on activity; no effect on protein abundance; loss of N-glycosylation.|||Retains 90% of activity.|||Strongly reduces formation of 3-oxoalanine (also known as C-formylglycine, FGly).|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033417|||http://purl.uniprot.org/annotation/PRO_0000033418|||http://purl.uniprot.org/annotation/PRO_0000033419|||http://purl.uniprot.org/annotation/PRO_5002801052|||http://purl.uniprot.org/annotation/PRO_5014019428|||http://purl.uniprot.org/annotation/VAR_007243|||http://purl.uniprot.org/annotation/VAR_007244|||http://purl.uniprot.org/annotation/VAR_007245|||http://purl.uniprot.org/annotation/VAR_007246|||http://purl.uniprot.org/annotation/VAR_007247|||http://purl.uniprot.org/annotation/VAR_007248|||http://purl.uniprot.org/annotation/VAR_007249|||http://purl.uniprot.org/annotation/VAR_007250|||http://purl.uniprot.org/annotation/VAR_007251|||http://purl.uniprot.org/annotation/VAR_007252|||http://purl.uniprot.org/annotation/VAR_007253|||http://purl.uniprot.org/annotation/VAR_007254|||http://purl.uniprot.org/annotation/VAR_007255|||http://purl.uniprot.org/annotation/VAR_007256|||http://purl.uniprot.org/annotation/VAR_007257|||http://purl.uniprot.org/annotation/VAR_007258|||http://purl.uniprot.org/annotation/VAR_007259|||http://purl.uniprot.org/annotation/VAR_007260|||http://purl.uniprot.org/annotation/VAR_007261|||http://purl.uniprot.org/annotation/VAR_007262|||http://purl.uniprot.org/annotation/VAR_007263|||http://purl.uniprot.org/annotation/VAR_007264|||http://purl.uniprot.org/annotation/VAR_007265|||http://purl.uniprot.org/annotation/VAR_007266|||http://purl.uniprot.org/annotation/VAR_007267|||http://purl.uniprot.org/annotation/VAR_007268|||http://purl.uniprot.org/annotation/VAR_007269|||http://purl.uniprot.org/annotation/VAR_007270|||http://purl.uniprot.org/annotation/VAR_007271|||http://purl.uniprot.org/annotation/VAR_007272|||http://purl.uniprot.org/annotation/VAR_007273|||http://purl.uniprot.org/annotation/VAR_007274|||http://purl.uniprot.org/annotation/VAR_007275|||http://purl.uniprot.org/annotation/VAR_007276|||http://purl.uniprot.org/annotation/VAR_007277|||http://purl.uniprot.org/annotation/VAR_007278|||http://purl.uniprot.org/annotation/VAR_007279|||http://purl.uniprot.org/annotation/VAR_007280|||http://purl.uniprot.org/annotation/VAR_007281|||http://purl.uniprot.org/annotation/VAR_007282|||http://purl.uniprot.org/annotation/VAR_007283|||http://purl.uniprot.org/annotation/VAR_007284|||http://purl.uniprot.org/annotation/VAR_007285|||http://purl.uniprot.org/annotation/VAR_007286|||http://purl.uniprot.org/annotation/VAR_007287|||http://purl.uniprot.org/annotation/VAR_007288|||http://purl.uniprot.org/annotation/VAR_007289|||http://purl.uniprot.org/annotation/VAR_007290|||http://purl.uniprot.org/annotation/VAR_007291|||http://purl.uniprot.org/annotation/VAR_007292|||http://purl.uniprot.org/annotation/VAR_007293|||http://purl.uniprot.org/annotation/VAR_008132|||http://purl.uniprot.org/annotation/VAR_008133|||http://purl.uniprot.org/annotation/VAR_018838|||http://purl.uniprot.org/annotation/VAR_018839|||http://purl.uniprot.org/annotation/VAR_054164|||http://purl.uniprot.org/annotation/VAR_054165|||http://purl.uniprot.org/annotation/VAR_054166|||http://purl.uniprot.org/annotation/VAR_054167|||http://purl.uniprot.org/annotation/VAR_054168|||http://purl.uniprot.org/annotation/VAR_054169|||http://purl.uniprot.org/annotation/VAR_054170|||http://purl.uniprot.org/annotation/VAR_054171|||http://purl.uniprot.org/annotation/VAR_054172|||http://purl.uniprot.org/annotation/VAR_054173|||http://purl.uniprot.org/annotation/VAR_054174|||http://purl.uniprot.org/annotation/VAR_054175|||http://purl.uniprot.org/annotation/VAR_054176|||http://purl.uniprot.org/annotation/VAR_054177|||http://purl.uniprot.org/annotation/VAR_054178|||http://purl.uniprot.org/annotation/VAR_054179|||http://purl.uniprot.org/annotation/VAR_054180|||http://purl.uniprot.org/annotation/VAR_054181|||http://purl.uniprot.org/annotation/VAR_054182|||http://purl.uniprot.org/annotation/VAR_054183|||http://purl.uniprot.org/annotation/VAR_054184|||http://purl.uniprot.org/annotation/VAR_054185|||http://purl.uniprot.org/annotation/VAR_054186|||http://purl.uniprot.org/annotation/VAR_054187|||http://purl.uniprot.org/annotation/VAR_054188|||http://purl.uniprot.org/annotation/VAR_054189|||http://purl.uniprot.org/annotation/VAR_054190|||http://purl.uniprot.org/annotation/VAR_054191|||http://purl.uniprot.org/annotation/VAR_054192|||http://purl.uniprot.org/annotation/VAR_054193|||http://purl.uniprot.org/annotation/VAR_054194|||http://purl.uniprot.org/annotation/VAR_054195|||http://purl.uniprot.org/annotation/VAR_054196|||http://purl.uniprot.org/annotation/VAR_054197|||http://purl.uniprot.org/annotation/VAR_054198|||http://purl.uniprot.org/annotation/VAR_054199|||http://purl.uniprot.org/annotation/VAR_054200|||http://purl.uniprot.org/annotation/VAR_054201|||http://purl.uniprot.org/annotation/VAR_054202|||http://purl.uniprot.org/annotation/VAR_054203|||http://purl.uniprot.org/annotation/VAR_054204|||http://purl.uniprot.org/annotation/VAR_054205|||http://purl.uniprot.org/annotation/VAR_054206|||http://purl.uniprot.org/annotation/VAR_054207|||http://purl.uniprot.org/annotation/VAR_054208|||http://purl.uniprot.org/annotation/VAR_054209|||http://purl.uniprot.org/annotation/VAR_054210|||http://purl.uniprot.org/annotation/VAR_054211|||http://purl.uniprot.org/annotation/VAR_067414|||http://purl.uniprot.org/annotation/VAR_067415|||http://purl.uniprot.org/annotation/VAR_067416|||http://purl.uniprot.org/annotation/VAR_067417|||http://purl.uniprot.org/annotation/VAR_067418|||http://purl.uniprot.org/annotation/VSP_046190
http://togogenome.org/gene/9606:PHYHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SRE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Phosphothreonine|||Phytanoyl-CoA dioxygenase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313633|||http://purl.uniprot.org/annotation/VAR_050529|||http://purl.uniprot.org/annotation/VSP_030077|||http://purl.uniprot.org/annotation/VSP_030078
http://togogenome.org/gene/9606:ZNF701                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NWZ7|||http://purl.uniprot.org/uniprot/Q9NV72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 701                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233281|||http://purl.uniprot.org/annotation/VAR_033592|||http://purl.uniprot.org/annotation/VAR_033593|||http://purl.uniprot.org/annotation/VAR_033594|||http://purl.uniprot.org/annotation/VAR_052898|||http://purl.uniprot.org/annotation/VAR_060432|||http://purl.uniprot.org/annotation/VAR_060433|||http://purl.uniprot.org/annotation/VAR_061964|||http://purl.uniprot.org/annotation/VSP_055969
http://togogenome.org/gene/9606:METTL25B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FB5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Methyltransferase-like protein 25B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289052|||http://purl.uniprot.org/annotation/VAR_032564|||http://purl.uniprot.org/annotation/VSP_054043|||http://purl.uniprot.org/annotation/VSP_054044
http://togogenome.org/gene/9606:TARM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1Q6|||http://purl.uniprot.org/uniprot/B6A8C7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Immunoglobulin subtype|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||T-cell-interacting, activating receptor on myeloid cells protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394231|||http://purl.uniprot.org/annotation/VAR_063151|||http://purl.uniprot.org/annotation/VAR_063152|||http://purl.uniprot.org/annotation/VAR_063153|||http://purl.uniprot.org/annotation/VSP_039225
http://togogenome.org/gene/9606:SLC47A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FL8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes membrane subcellular location. Abolishes TEA transport.|||Cytoplasmic|||Decreased TEA and metformin uptake.|||Disordered|||Does not affect membrane subcellular location. Abolishes TEA transport.|||Does not affect membrane subcellular location. Decreases TEA transport.|||Does not affect membrane subcellular location. Decreases TEA transport. Higher affinity for cimetidine and reduced affinity to TEA.|||Extracellular|||Found in a patient with renal disease; unknown pathological significance; decreases plasma membrane expression; decreases TEA and metformin transport; Vmax value for TEA transport is decreased.|||Found in a patient with renal disease; unknown pathological significance; decreases plasma membrane expression; transport of TEA and metformin are reduced by at least 90%.|||Found in a patient with renal disease; unknown pathological significance; does not affect plasma membrane expression; decreases TEA and metformin transport; Vmax value for TEA transport is decreased; Km value for TEA is increased.|||Found in a patient with renal disease; unknown pathological significance; does not affect plasma membrane localization; decreases TEA transport; Km value for TEA is increased; does not affect metformin transport.|||Helical|||In isoform 2.|||In isoform 3.|||Likely benign variant; does not affect plasma membrane expression; does not affect TEA and metformin transport.|||Multidrug and toxin extrusion protein 1|||N-acetylmethionine|||No change in subcellular location and abolition of MATE1-dependent TEA transport activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312845|||http://purl.uniprot.org/annotation/VAR_037587|||http://purl.uniprot.org/annotation/VAR_087027|||http://purl.uniprot.org/annotation/VAR_087028|||http://purl.uniprot.org/annotation/VAR_087029|||http://purl.uniprot.org/annotation/VAR_087030|||http://purl.uniprot.org/annotation/VAR_087031|||http://purl.uniprot.org/annotation/VSP_029903|||http://purl.uniprot.org/annotation/VSP_029904|||http://purl.uniprot.org/annotation/VSP_029905
http://togogenome.org/gene/9606:CGAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N884                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37|||(Microbial infection) Deamidated glutamine; by herpes simplex virus 1/HHV-1 UL37|||5-glutamyl glutamate|||5-glutamyl polyglutamate|||Abolished binding to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and abolished association with the cell membrane.|||Abolished export from the nucleus to the cytosol in response to DNA stimulation.|||Abolished interaction with nucleosomes and tethering to chromatin, leading to strong constitutive activation in the absence of DNA.|||Abolished nuclear localization.|||Abolished nucleotidyltransferase activity.|||Abolished palmitoylation by ZDHHC18, leading to increased DNA-binding and enzyme activity.|||Abolished poly-ADP-ribosylation by PARP1, stimulating interferon production.|||Abolishes DNA binding and enzyme activity.|||Abolishes DNA binding and enzyme activity. Abolishes stimulation of interferon production. Decreased localization to the nucleus.|||Abolishes DNA-binding but does not affect translocation to the nucleus following treatment with etoposide; when associated with A-384.|||Abolishes DNA-binding but does not affect translocation to the nucleus following treatment with etoposide; when associated with A-407.|||Abolishes enzyme activity and stimulation of interferon production. Does not affect subcellular location to the nucleus and cytosol.|||Abolishes enzyme activity. Abolishes stimulation of interferon production.|||Abolishes enzyme activity. Abolishes stimulation of interferon production. Abolishes DNA-binding but does not affect translocation to the nucleus following treatment with etoposide; when associated with 171-K--L-174 Del.|||Abolishes enzyme activity. Does not affect translocation to the nucleus following treatment with etoposide. Abolished cleavage by CASP3.|||Abolishes enzyme activity. No effect on stimulation of interferon production.|||Abolishes enzyme activity; when associated with I-376 and I-436.|||Abolishes enzyme activity; when associated with Q-211 and I-376.|||Abolishes homodimerization and subsequent nucleotidyltransferase activity. Abolishes stimulation of interferon production. Does not affect subcellular location to the nucleus and cytosol.|||Abolishes stimulation of interferon production.|||Abolishes stimulation of interferon production. Abolishes DNA-binding but does not affect translocation to the nucleus following treatment with etoposide; when associated with 210-A--A-214.|||Abolishes stimulation of interferon production; when associated with E-236 and E-254. Does not affect interaction with nucleosomes.|||Abolishes stimulation of interferon production; when associated with E-236 and E-327. Abolished interaction with nucleosomes.|||Abolishes stimulation of interferon production; when associated with E-254 and E-327. Strongly decreased interaction with nucleosomes and tethering to chromatin, leading to constitutive activation in the absence of DNA.|||Abolishes stimulation of interferon production; when associated with E-400.|||Abolishes stimulation of interferon production; when associated with E-403.|||Acetylation-mimetic mutant; no effect.|||Acetylation-mimetic mutant; reduced enzyme activity.|||Alters enzyme activity, leading to the appearance of 3'-5' linked cGAMP. Abolishes enzyme activity; when associated with Q-211 and I-436.|||Arginine-anchor|||Cleavage; by CASP1|||Cleavage; by CASP3|||Cyclic GMP-AMP synthase|||DNA-binding|||Decreased acetylation by KAT5, leading to decreased stimulation of interferon production.|||Decreased cyclic GMP-AMP synthase activity.|||Decreased interaction with histones H2A and H2B.|||Disordered|||Does not affect interaction with nucleosomes.|||Enhanced stimulation of interferon production. Does not affect chromosome localization.|||Found in patients with tumors; dominant mutation; reduced nucleotidyltransferase activity.|||Found in patients with uterine endometrioid carcinoma, reduced nucleotidyltransferase activity.|||Gains susceptibility to mouse-specific RU.521; when associated with C-434.|||Gains susceptibility to mouse-specific RU.521; when associated with H-482.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Highly decreases cleavage by CASP1 and enhances type IIFN and RSAD2 induction upon DNA virus infection.|||Highly decreases cleavage by CASP1 and enhances type IIFN and RSAD2 induction upon DNA virus infection. Abolishes cleavage by CASP1, enhances RSAD2 induction upon DNA virus infection but no effect on cleavage by CASP5; when associated with A-157. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90 and A-95. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90; A-95 and A-157.|||Highly decreases cleavage by CASP1 and enhances type IIFN and enhances RSAD2 induction upon DNA virus infection.|||Impaired association with collided ribosomes in response to translation stress. Abolishes stimulation of interferon production. Decreased interaction with nucleosomes.|||Impaired association with collided ribosomes in response to translation stress. Decreased interaction with histones H2A and H2B.|||Impaired association with collided ribosomes in response to translation stress. Decreased interaction with nucleosomes.|||Impaired association with collided ribosomes in response to translation stress. Does not affect interaction with histones H2A and H2B.|||Impaired association with collided ribosomes in response to translation stress. Strongly decreased interaction with histones H2A and H2B.|||Impaired type-I interferon production in response to DNA stimulation.|||Important for preferential detection of curved long DNA|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130 and D-143.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-68, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||In isoform 2.|||Induces alteration of the DNA-binding surface and leads to increased synthesis of cyclic GMP-AMP (cGAMP); when associated with N-187.|||Induces alteration of the DNA-binding surface and leads to increased synthesis of cyclic GMP-AMP (cGAMP); when associated with R-195.|||Interaction with collided ribosomes|||KKH-loop|||KRKR-loop|||Loss of ubiquitination by MARCHF8.|||More than 75% inhibition of interferon beta production.|||N6-acetyllysine|||N6-methyllysine|||No effect on stimulation of interferon production.|||No effect on stimulation of interferon production. Strongly decreased ubiquitination by RNF185; when associated with R-173.|||No effect on type IIFN and RSAD2 induction. Highly decreases cleavage by CASP1 and enhances type IIFN and enhances RSAD2 induction upon DNA virus infection. Abolishes cleavage by CASP1, enhances RSAD2 induction upon DNA virus infection but no effect on cleavage by CASP5; when associated with A-140. Abolishes cleavage by CASP1; when associated with A-33; A-67; A-90; A-95 and A-140.|||No effect on type IIFN and RSAD2 induction. No effect on cleavage by CASP1. No effect on cleavage by CASP1; when associated with A-67; A-90 and A-95. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-67; A-90; A-95 and A-140. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-67; A-90; A-95; A-140 and A-157.|||No effect on type IIFN and RSAD2 induction. No effect on cleavage by CASP1; when associated with A-33; A-67 and A-90. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90 and A-140. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-90; A-140 and A-157.|||No effect on type IIFN and RSAD2 induction. No effect on cleavage by CASP1; when associated with A-33; A-67 and A-95. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-95 and A-140. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-67; A-95; A-140 and A-157.|||No effect on type IIFN and RSAD2 induction. No effect on cleavage by CASP1; when associated with A-33; A-90 and A-95. Highly decreases cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-90; A-95 and A-140. Abolishes cleavage by CASP1 and enhances RSAD2 induction upon DNA virus infection; when associated with A-33; A-90; A-95; A-140 and A-157.|||No effect.|||Nuclear export signal|||Nuclear localization signal|||Phospho-mimetic mutant; decreased ability to trigger type-I interferon production.|||Phospho-mimetic mutant; decreased nucleotidyltransferase activity.|||Phospho-mimetic mutant; decreased nucleotidyltransferase activity. In 20DE phospho-mimetic mutant; causes inactivation of nucleotidyltransferase activity; when associates with D-13, E-18, D-23, E-35, D-37, D-57, D-59, D-64, E-77, E-91, D-94, E-97, D-98, D-116, D-120, D-129, E-130, D-143 and D-149.|||Phospho-mimetic mutant; increased cyclic GMP-AMP synthase activity.|||Phosphomimetic mutant; reduced translocation to the nucleus following treatment with etoposide.|||Phosphoserine|||Phosphoserine; by CDK1 and PKB|||Phosphothreonine|||Phosphotyrosine; by BLK|||PolyADP-ribosyl aspartic acid|||Prevents activation in response to DNA-binding; leading to abolished enzyme activity and stimulation of interferon production.|||Reduced enzyme activity. Decreased ubiquitination and SQSTM1-mediated autophagic degradation.|||Reduced nucleotidyltransferase activity.|||Reduced nucleotidyltransferase activity. Abolished nucleotidyltransferase activity; when associated with E-285.|||Reduced sumoylation.|||Required for activation upon DNA viral infection|||Required for association with the cell membrane|||S-palmitoyl cysteine|||Slightly decreased interaction with histones H2A and H2B.|||Strongly decreased interaction with histones H2A and H2B.|||Strongly decreased ubiquitination by RNF185; when associated with R-384.|||Strongly reduced nucleotidyltransferase activity.|||Strongly reduced nucleotidyltransferase activity. Abolished nucleotidyltransferase activity; when associated with E-275.|||Strongly reduced tyrosine phosphorylation.|||Strongly reduces enzyme activity and stimulation of interferon production.|||Strongly reduces enzyme activity and stimulation of interferon production; when associated with A-173.|||Strongly reduces enzyme activity and stimulation of interferon production; when associated with A-176. No effect on stimulation of interferon production.|||Strongly reduces stimulation of interferon production. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089543|||http://purl.uniprot.org/annotation/VAR_033677|||http://purl.uniprot.org/annotation/VAR_050811|||http://purl.uniprot.org/annotation/VAR_085524|||http://purl.uniprot.org/annotation/VAR_085525|||http://purl.uniprot.org/annotation/VSP_014388|||http://purl.uniprot.org/annotation/VSP_014389
http://togogenome.org/gene/9606:TMEM276-ZFTRAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTL6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 4 and isoform 2.|||In isoform 4.|||RING-type; degenerate|||TRAF-type|||Zinc finger TRAF-type-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328852|||http://purl.uniprot.org/annotation/VSP_061632|||http://purl.uniprot.org/annotation/VSP_061633|||http://purl.uniprot.org/annotation/VSP_061634|||http://purl.uniprot.org/annotation/VSP_061635
http://togogenome.org/gene/9606:GAGE12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L429|||http://purl.uniprot.org/uniprot/O76087                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12B/C/D/E|||G antigen 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148345|||http://purl.uniprot.org/annotation/PRO_0000311977
http://togogenome.org/gene/9606:ACSL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULC5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Long-chain-fatty-acid--CoA ligase 5|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193112|||http://purl.uniprot.org/annotation/VAR_022117|||http://purl.uniprot.org/annotation/VAR_036377|||http://purl.uniprot.org/annotation/VAR_036378|||http://purl.uniprot.org/annotation/VAR_048240|||http://purl.uniprot.org/annotation/VSP_037947|||http://purl.uniprot.org/annotation/VSP_038233
http://togogenome.org/gene/9606:C7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10643|||http://purl.uniprot.org/uniprot/Q05CI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||C-linked (Man) tryptophan; partial|||CCP 1|||CCP 2|||Complement component C7|||Confirmed at protein level.|||Disordered|||EGF-like|||Factor I module (FIM) 1|||Factor I module (FIM) 2|||In C7D.|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Polar residues|||Sushi 1|||Sushi 2|||TSP type-1 1|||TSP type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023583|||http://purl.uniprot.org/annotation/PRO_5004164590|||http://purl.uniprot.org/annotation/VAR_012643|||http://purl.uniprot.org/annotation/VAR_012644|||http://purl.uniprot.org/annotation/VAR_012645|||http://purl.uniprot.org/annotation/VAR_012646|||http://purl.uniprot.org/annotation/VAR_012647|||http://purl.uniprot.org/annotation/VAR_022023|||http://purl.uniprot.org/annotation/VAR_033798|||http://purl.uniprot.org/annotation/VAR_033799|||http://purl.uniprot.org/annotation/VAR_050480|||http://purl.uniprot.org/annotation/VAR_081726
http://togogenome.org/gene/9606:LYN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K379|||http://purl.uniprot.org/uniprot/B4DQ79|||http://purl.uniprot.org/uniprot/P07948|||http://purl.uniprot.org/uniprot/Q6NUK7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autoinhibition and thereby increases kinase activity.|||Disordered|||Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498.|||Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499.|||Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499.|||Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3.|||Loss of kinase activity.|||Loss of localization to the cell membrane; when associated with A-2.|||Loss of localization to the cell membrane; when associated with A-3.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis, CSK and MATK|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Strongly reduced kinase activity.|||Tyrosine-protein kinase Lyn                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088129|||http://purl.uniprot.org/annotation/VAR_041737|||http://purl.uniprot.org/annotation/VSP_005002
http://togogenome.org/gene/9606:GRB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14449                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-fold increase in PI(3,4,5)P3-binding affinity; when associated with G-245.|||4-fold increase in PI(3,4,5)P3-binding affinity; when associated with S-246.|||Growth factor receptor-bound protein 14|||In a patient with amyotrophic lateral sclerosis.|||In isoform 2.|||Loss of inhibition of AKT1 activation; when associated with A-348. Loss of inhibition of MAPK3 phosphorylation; when associated with A-348. No effect on INSR-binding; when associated with A-348.|||Loss of inhibition of AKT1 activation; when associated with A-349. Loss of inhibition of MAPK3 phosphorylation; when associated with A-349. No effect on INSR-binding; when associated with A-349.|||N-acetylthreonine|||No effect on PI(3,4,5)P3-binding.|||PH|||Partial loss of INSR-binding. Loss of inhibition of AKT1 activation. Loss of inhibition of MAPK3 phosphorylation. Loss of NRAS-binding.|||Partial loss of INSR-binding. Loss of inhibition of AKT1 activation. Loss of inhibition of MAPK3 phosphorylation. Loss of translocation to the plasma membrane upon insulin-stimulation. More than 3-fold decrease in PI(3,4,5)P3-binding affinity.|||Phosphoserine|||Phosphothreonine|||Ras-associating|||Removed|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150348|||http://purl.uniprot.org/annotation/VAR_065758|||http://purl.uniprot.org/annotation/VAR_065759|||http://purl.uniprot.org/annotation/VSP_056582|||http://purl.uniprot.org/annotation/VSP_056583
http://togogenome.org/gene/9606:OSBPL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXP9|||http://purl.uniprot.org/uniprot/Q9BZF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Oxysterol-binding protein-related protein 7|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100377|||http://purl.uniprot.org/annotation/VAR_053551|||http://purl.uniprot.org/annotation/VAR_060080|||http://purl.uniprot.org/annotation/VAR_060081|||http://purl.uniprot.org/annotation/VSP_057227|||http://purl.uniprot.org/annotation/VSP_057228
http://togogenome.org/gene/9606:GID4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXL6|||http://purl.uniprot.org/uniprot/Q8IVV7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glucose-induced degradation protein 4 homolog|||Interaction with the N-terminal Pro (Pro/N-degron) of proteins that are targeted for degradation|||Loss of interaction with peptides with a Pro/N-degron.|||Strongly decreased affinity for peptides with a Pro/N-degron.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079302
http://togogenome.org/gene/9606:CCDC59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P031                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Thyroid transcription factor 1-associated protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298941
http://togogenome.org/gene/9606:RBMS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XE24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||Polar residues|||RNA-binding motif, single-stranded-interacting protein 3|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274906|||http://purl.uniprot.org/annotation/VSP_022927|||http://purl.uniprot.org/annotation/VSP_022928|||http://purl.uniprot.org/annotation/VSP_022929|||http://purl.uniprot.org/annotation/VSP_022930|||http://purl.uniprot.org/annotation/VSP_022931
http://togogenome.org/gene/9606:SAMSN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSI8|||http://purl.uniprot.org/uniprot/S6FRS6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Important for interaction with 14-3-3 proteins|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SAM|||SAM domain-containing protein SAMSN-1|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097574|||http://purl.uniprot.org/annotation/VAR_051331|||http://purl.uniprot.org/annotation/VSP_008119|||http://purl.uniprot.org/annotation/VSP_008120
http://togogenome.org/gene/9606:ORMDL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N138                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disrupted ceramide binding; impaired negative regulation of SPT complex activity in the presence of ceramides; in the absence of ceramides, reduced affinity of SPT complex towards palmitoyl-CoA.|||Helical|||Hydroxyproline|||Impaired negative regulation of SPT complex activity in the presence of ceramides.|||Important for ceramide level-sensing|||In isoform 2.|||Increased protein levels; decreased ubiquitination; increased negative regulation of SPT complex activity.|||Lumenal|||No effect on the negative regulation of SPT complex activity in the presence of ceramides.|||ORM1-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215639|||http://purl.uniprot.org/annotation/VSP_016052
http://togogenome.org/gene/9606:OCEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H607                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||OCEL|||Occludin/ELL domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271531|||http://purl.uniprot.org/annotation/VAR_034356|||http://purl.uniprot.org/annotation/VAR_034357
http://togogenome.org/gene/9606:NOTCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04721|||http://purl.uniprot.org/uniprot/Q6IQ50|||http://purl.uniprot.org/uniprot/Q9UFD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 10|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18; calcium-binding|||EGF-like 19|||EGF-like 2|||EGF-like 20; calcium-binding|||EGF-like 21; calcium-binding|||EGF-like 22|||EGF-like 23; calcium-binding|||EGF-like 24; calcium-binding|||EGF-like 25; calcium-binding|||EGF-like 26; calcium-binding|||EGF-like 27; calcium-binding|||EGF-like 28|||EGF-like 29|||EGF-like 3|||EGF-like 30; calcium-binding|||EGF-like 31; calcium-binding|||EGF-like 32; calcium-binding|||EGF-like 33|||EGF-like 34|||EGF-like 35|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Essential for O-xylosylation|||Extracellular|||Helical|||In ALGS2.|||In HJCYS.|||In HJCYS; loss of interaction with FBW7; decreased ubiquitination.|||LNR 1|||LNR 2|||LNR 3|||Loss of interaction with FBW7. Results in decreased ubiquitination and degradation.|||N-linked (GlcNAc...) asparagine|||Negative regulatory region (NRR)|||Neurogenic locus notch homolog protein 2|||Notch 2 extracellular truncation|||Notch 2 intracellular domain|||Notch C-terminal|||O-linked (Glc...) serine; alternate|||O-linked (Xyl...) serine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007683|||http://purl.uniprot.org/annotation/PRO_0000007684|||http://purl.uniprot.org/annotation/PRO_0000007685|||http://purl.uniprot.org/annotation/PRO_5004275902|||http://purl.uniprot.org/annotation/VAR_029361|||http://purl.uniprot.org/annotation/VAR_031463|||http://purl.uniprot.org/annotation/VAR_080195|||http://purl.uniprot.org/annotation/VAR_080196|||http://purl.uniprot.org/annotation/VAR_080197|||http://purl.uniprot.org/annotation/VAR_080198|||http://purl.uniprot.org/annotation/VAR_080199|||http://purl.uniprot.org/annotation/VAR_080200|||http://purl.uniprot.org/annotation/VAR_080201|||http://purl.uniprot.org/annotation/VAR_080202|||http://purl.uniprot.org/annotation/VAR_080203|||http://purl.uniprot.org/annotation/VAR_080204|||http://purl.uniprot.org/annotation/VAR_080205|||http://purl.uniprot.org/annotation/VAR_080206
http://togogenome.org/gene/9606:BCAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7W3|||http://purl.uniprot.org/uniprot/O75934                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||N-acetylalanine|||Phosphoserine|||Pre-mRNA-splicing factor SPF27|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064861|||http://purl.uniprot.org/annotation/VAR_035799
http://togogenome.org/gene/9606:SEC23IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DDHD|||Disordered|||In isoform 2.|||Interaction with SEC23A|||Phosphoserine|||Polar residues|||Pro residues|||SAM|||SEC23-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097554|||http://purl.uniprot.org/annotation/VAR_019806|||http://purl.uniprot.org/annotation/VSP_011831|||http://purl.uniprot.org/annotation/VSP_011832
http://togogenome.org/gene/9606:DEFB121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDM0|||http://purl.uniprot.org/uniprot/Q5GRF9|||http://purl.uniprot.org/uniprot/Q5J5C9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 121                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006991|||http://purl.uniprot.org/annotation/PRO_5017339660
http://togogenome.org/gene/9606:HEPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG76|||http://purl.uniprot.org/uniprot/Q1HE23|||http://purl.uniprot.org/uniprot/Q9BQS7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Hephaestin|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plastocyanin-like|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||type 1 copper site|||type 2 copper site|||type 3 copper site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002915|||http://purl.uniprot.org/annotation/PRO_5005693585|||http://purl.uniprot.org/annotation/PRO_5014509642|||http://purl.uniprot.org/annotation/VAR_024379|||http://purl.uniprot.org/annotation/VSP_011627|||http://purl.uniprot.org/annotation/VSP_047331|||http://purl.uniprot.org/annotation/VSP_047332
http://togogenome.org/gene/9606:ART1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52961                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||GPI-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||TR mART core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019311|||http://purl.uniprot.org/annotation/PRO_0000019312|||http://purl.uniprot.org/annotation/VAR_034125|||http://purl.uniprot.org/annotation/VAR_034126|||http://purl.uniprot.org/annotation/VAR_053526
http://togogenome.org/gene/9606:SLC43A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75387                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Large neutral amino acids transporter small subunit 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218640|||http://purl.uniprot.org/annotation/VAR_053670|||http://purl.uniprot.org/annotation/VAR_053671|||http://purl.uniprot.org/annotation/VSP_051620
http://togogenome.org/gene/9606:PMP22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MU75|||http://purl.uniprot.org/uniprot/Q01453|||http://purl.uniprot.org/uniprot/Q6FH25                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In CMT1A and DSS.|||In CMT1A.|||In CMT1A; with focally folded myelin sheaths.|||In CMT1E.|||In DSS and CMT1A.|||In DSS.|||In HNPP and CMT1A.|||In HNPP.|||N-linked (GlcNAc...) asparagine|||Peripheral myelin protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164650|||http://purl.uniprot.org/annotation/VAR_006359|||http://purl.uniprot.org/annotation/VAR_006360|||http://purl.uniprot.org/annotation/VAR_006361|||http://purl.uniprot.org/annotation/VAR_006362|||http://purl.uniprot.org/annotation/VAR_006363|||http://purl.uniprot.org/annotation/VAR_006364|||http://purl.uniprot.org/annotation/VAR_006365|||http://purl.uniprot.org/annotation/VAR_006366|||http://purl.uniprot.org/annotation/VAR_006367|||http://purl.uniprot.org/annotation/VAR_006368|||http://purl.uniprot.org/annotation/VAR_006369|||http://purl.uniprot.org/annotation/VAR_006370|||http://purl.uniprot.org/annotation/VAR_006371|||http://purl.uniprot.org/annotation/VAR_006372|||http://purl.uniprot.org/annotation/VAR_006373|||http://purl.uniprot.org/annotation/VAR_006374|||http://purl.uniprot.org/annotation/VAR_006375|||http://purl.uniprot.org/annotation/VAR_006376|||http://purl.uniprot.org/annotation/VAR_006377|||http://purl.uniprot.org/annotation/VAR_006378|||http://purl.uniprot.org/annotation/VAR_006379|||http://purl.uniprot.org/annotation/VAR_009659|||http://purl.uniprot.org/annotation/VAR_009660|||http://purl.uniprot.org/annotation/VAR_009661|||http://purl.uniprot.org/annotation/VAR_009662|||http://purl.uniprot.org/annotation/VAR_009663|||http://purl.uniprot.org/annotation/VAR_009664|||http://purl.uniprot.org/annotation/VAR_029960|||http://purl.uniprot.org/annotation/VAR_029961|||http://purl.uniprot.org/annotation/VAR_029962|||http://purl.uniprot.org/annotation/VAR_029963|||http://purl.uniprot.org/annotation/VAR_029964|||http://purl.uniprot.org/annotation/VAR_029965|||http://purl.uniprot.org/annotation/VAR_029966|||http://purl.uniprot.org/annotation/VAR_029967|||http://purl.uniprot.org/annotation/VAR_029968|||http://purl.uniprot.org/annotation/VAR_029969|||http://purl.uniprot.org/annotation/VAR_029970
http://togogenome.org/gene/9606:ACP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13686                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In SPENCDI.|||N-linked (GlcNAc...) asparagine|||Tartrate-resistant acid phosphatase type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023981|||http://purl.uniprot.org/annotation/VAR_020602|||http://purl.uniprot.org/annotation/VAR_020603|||http://purl.uniprot.org/annotation/VAR_029288|||http://purl.uniprot.org/annotation/VAR_065920|||http://purl.uniprot.org/annotation/VAR_065921|||http://purl.uniprot.org/annotation/VAR_065922|||http://purl.uniprot.org/annotation/VAR_065923|||http://purl.uniprot.org/annotation/VAR_065924|||http://purl.uniprot.org/annotation/VAR_065925|||http://purl.uniprot.org/annotation/VAR_065926|||http://purl.uniprot.org/annotation/VAR_065927|||http://purl.uniprot.org/annotation/VAR_065928
http://togogenome.org/gene/9606:HNRNPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07910                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoproteins C1/C2|||In isoform 3.|||In isoform 4.|||In isoform C1 and isoform 4.|||Loss of sumoylation.|||N-acetylalanine|||N6-acetyllysine; alternate|||No effect on sumoylation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081844|||http://purl.uniprot.org/annotation/VSP_005831|||http://purl.uniprot.org/annotation/VSP_019225|||http://purl.uniprot.org/annotation/VSP_019226
http://togogenome.org/gene/9606:DMRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5R6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DM|||Disordered|||Doublesex- and mab-3-related transcription factor 1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207042|||http://purl.uniprot.org/annotation/VAR_009954|||http://purl.uniprot.org/annotation/VAR_009955|||http://purl.uniprot.org/annotation/VAR_009956|||http://purl.uniprot.org/annotation/VAR_009957|||http://purl.uniprot.org/annotation/VSP_042959|||http://purl.uniprot.org/annotation/VSP_042960|||http://purl.uniprot.org/annotation/VSP_042961|||http://purl.uniprot.org/annotation/VSP_042962
http://togogenome.org/gene/9606:EXTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GZK1|||http://purl.uniprot.org/uniprot/Q8N8F1|||http://purl.uniprot.org/uniprot/Q9UBQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Exostosin-like 2|||Glycosyl transferase 64|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Processed exostosin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149655|||http://purl.uniprot.org/annotation/PRO_0000296227
http://togogenome.org/gene/9606:ERBIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Erbin|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 9.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188301|||http://purl.uniprot.org/annotation/VAR_019346|||http://purl.uniprot.org/annotation/VAR_019347|||http://purl.uniprot.org/annotation/VAR_019348|||http://purl.uniprot.org/annotation/VAR_028304|||http://purl.uniprot.org/annotation/VAR_046673|||http://purl.uniprot.org/annotation/VAR_046674|||http://purl.uniprot.org/annotation/VAR_068905|||http://purl.uniprot.org/annotation/VSP_010802|||http://purl.uniprot.org/annotation/VSP_010803|||http://purl.uniprot.org/annotation/VSP_010804|||http://purl.uniprot.org/annotation/VSP_010805|||http://purl.uniprot.org/annotation/VSP_010806|||http://purl.uniprot.org/annotation/VSP_010807|||http://purl.uniprot.org/annotation/VSP_044536|||http://purl.uniprot.org/annotation/VSP_047389
http://togogenome.org/gene/9606:POC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0MNP0|||http://purl.uniprot.org/uniprot/Q8TC44                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In CORD20; disrupts interaction with FAM161A; localization of the mutant is cytosolic without enrichment at specific subcellular sites.|||In isoform 2.|||POC1 centriolar protein homolog B|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051410|||http://purl.uniprot.org/annotation/VAR_071916|||http://purl.uniprot.org/annotation/VAR_071917|||http://purl.uniprot.org/annotation/VSP_047066
http://togogenome.org/gene/9606:MMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08254                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Disordered|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Pro residues|||Stromelysin-1|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028728|||http://purl.uniprot.org/annotation/PRO_0000028729|||http://purl.uniprot.org/annotation/VAR_013090
http://togogenome.org/gene/9606:TMEM222                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0R3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In NEDMOSBA.|||In NEDMOSBA; unknown pathological significance.|||In isoform 2.|||Transmembrane protein 222                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247963|||http://purl.uniprot.org/annotation/VAR_086147|||http://purl.uniprot.org/annotation/VAR_086148|||http://purl.uniprot.org/annotation/VAR_086149|||http://purl.uniprot.org/annotation/VAR_086150|||http://purl.uniprot.org/annotation/VAR_086151|||http://purl.uniprot.org/annotation/VSP_020090
http://togogenome.org/gene/9606:DGCR6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY27                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein DGCR6L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070260|||http://purl.uniprot.org/annotation/VAR_055870|||http://purl.uniprot.org/annotation/VAR_055871
http://togogenome.org/gene/9606:TAF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15573                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||TATA box-binding protein-associated factor RNA polymerase I subunit A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227987|||http://purl.uniprot.org/annotation/VAR_052253|||http://purl.uniprot.org/annotation/VSP_017635
http://togogenome.org/gene/9606:CCDC32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV29                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 32|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298937|||http://purl.uniprot.org/annotation/VAR_034743|||http://purl.uniprot.org/annotation/VSP_027485|||http://purl.uniprot.org/annotation/VSP_027486|||http://purl.uniprot.org/annotation/VSP_027487
http://togogenome.org/gene/9606:UBAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK64|||http://purl.uniprot.org/uniprot/Q9BSL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylmethionine|||STI1|||UBA|||UBA 1|||UBA 2|||Ubiquitin-associated domain-containing protein 1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250449|||http://purl.uniprot.org/annotation/VAR_027562
http://togogenome.org/gene/9606:RAB5IF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUV8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GEL complex subunit OPTI|||Helical|||In CFSMR2; no RAB5IF protein detected by Western blot in patient fibroblasts.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079415|||http://purl.uniprot.org/annotation/VAR_087487|||http://purl.uniprot.org/annotation/VSP_003795|||http://purl.uniprot.org/annotation/VSP_003796|||http://purl.uniprot.org/annotation/VSP_003797|||http://purl.uniprot.org/annotation/VSP_047233
http://togogenome.org/gene/9606:NME1-NME2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22392                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Decreased single-stranded DNA-binding and nucleotide-binding activity. No effect on 3D-structure.|||In isoform 3.|||Interaction with AKAP13|||Nucleoside diphosphate kinase B|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137117|||http://purl.uniprot.org/annotation/VSP_036708
http://togogenome.org/gene/9606:TSTD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0UI37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  N6-succinyllysine|||Rhodanese|||Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419460
http://togogenome.org/gene/9606:KLHL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PKX1|||http://purl.uniprot.org/uniprot/Q9C0H6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119104|||http://purl.uniprot.org/annotation/VSP_002818
http://togogenome.org/gene/9606:CLPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76031                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial|||Abolishes ATP hydrolysis.|||Basic and acidic residues|||ClpX-type ZB|||Disordered|||In EPP2; results in decreased ATP hydrolysis; cells with the mutant protein show increased ALA levels and accumulation of the heme biosynthesis intermediate protoporphyrin IX.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005518|||http://purl.uniprot.org/annotation/VAR_048826|||http://purl.uniprot.org/annotation/VAR_081001
http://togogenome.org/gene/9606:AJUBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LIM domain-containing protein ajuba|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Nuclear localization signal|||Phosphoserine|||Polar residues|||PreLIM|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312625|||http://purl.uniprot.org/annotation/VSP_044227
http://togogenome.org/gene/9606:IFT56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVF1|||http://purl.uniprot.org/uniprot/B7Z2T3|||http://purl.uniprot.org/uniprot/Q96CU4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In BRENS; decreased protein abundance; associated with abnormal ciliary structure and function.|||In BRENS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Intraflagellar transport protein 56|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289082|||http://purl.uniprot.org/annotation/VAR_032568|||http://purl.uniprot.org/annotation/VAR_086383|||http://purl.uniprot.org/annotation/VAR_086384|||http://purl.uniprot.org/annotation/VSP_043751|||http://purl.uniprot.org/annotation/VSP_044791
http://togogenome.org/gene/9606:SRY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7WPU8|||http://purl.uniprot.org/uniprot/Q05066                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes acetylation. Does not abolish interaction with EP300. Does not abolish DNA-binding. Enhances cytoplasmic localization. Abolishes interaction with KPNB1.|||Abolishes its phosphorylation by PKA. Does not enhance its DNA-binding activity. Abolishes stimulation of transcription repression.|||Abolishes nuclear localization.|||Disordered|||Does not abolish acetylation activity.|||Does not abolish acetylation.|||HMG box|||In SRXY1.|||In SRXY1; alters interaction with DNA and DNA bending.|||In SRXY1; localizes mainly in the cytoplasm.|||In SRXY1; partial; also in two patients with a Turner syndrome phenotype.|||N6-acetyllysine|||Necessary for interaction with SLC9A3R2|||Necessary for interaction with ZNF208 isoform KRAB-O|||Reduces nuclear localization. Reduces DNA-binding. Does not reduce interaction with KPNB1 and CAML. Does not affectnuclear import.|||Reduces nuclear localization. Strongly reduces nuclear localization; when associated with G-62. Reduces interaction with KPNB1. Does not reduce interaction with CAML. Does not abolish DNA-binding.|||Required for nuclear localization|||Sex-determining region Y protein|||Strongly reduces nuclear localization. Abolishes DNA-binding. Does not reduce interaction with KPNB1 and CAML.|||Strongly reduces nuclear localization. Strongly reduces nuclear localization; when associated with W-133. Reduces interaction with KPNB1.|||Sufficient for interaction with EP300|||Sufficient for interaction with KPNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048671|||http://purl.uniprot.org/annotation/VAR_003717|||http://purl.uniprot.org/annotation/VAR_003718|||http://purl.uniprot.org/annotation/VAR_003719|||http://purl.uniprot.org/annotation/VAR_003720|||http://purl.uniprot.org/annotation/VAR_003721|||http://purl.uniprot.org/annotation/VAR_003722|||http://purl.uniprot.org/annotation/VAR_003723|||http://purl.uniprot.org/annotation/VAR_003724|||http://purl.uniprot.org/annotation/VAR_003725|||http://purl.uniprot.org/annotation/VAR_003726|||http://purl.uniprot.org/annotation/VAR_003727|||http://purl.uniprot.org/annotation/VAR_003728|||http://purl.uniprot.org/annotation/VAR_003729|||http://purl.uniprot.org/annotation/VAR_003730|||http://purl.uniprot.org/annotation/VAR_003731|||http://purl.uniprot.org/annotation/VAR_003732|||http://purl.uniprot.org/annotation/VAR_003733|||http://purl.uniprot.org/annotation/VAR_003734|||http://purl.uniprot.org/annotation/VAR_017298|||http://purl.uniprot.org/annotation/VAR_017299|||http://purl.uniprot.org/annotation/VAR_017300|||http://purl.uniprot.org/annotation/VAR_017301|||http://purl.uniprot.org/annotation/VAR_017302|||http://purl.uniprot.org/annotation/VAR_017303|||http://purl.uniprot.org/annotation/VAR_017304|||http://purl.uniprot.org/annotation/VAR_030019|||http://purl.uniprot.org/annotation/VAR_078433
http://togogenome.org/gene/9606:KRTAP4-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||30 X 5 AA repeats of C-C-[IRQVEL]-[SPTR]-[STVQRCP]|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 4-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185181
http://togogenome.org/gene/9606:KCNF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3M0                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily F member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054072
http://togogenome.org/gene/9606:SIKE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRV8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Suppressor of IKBKE 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299050|||http://purl.uniprot.org/annotation/VSP_027543
http://togogenome.org/gene/9606:TMEM150C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EJG8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Transmembrane protein 150C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395032|||http://purl.uniprot.org/annotation/VSP_039350
http://togogenome.org/gene/9606:AKT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0LPE5|||http://purl.uniprot.org/uniprot/B3KVH4|||http://purl.uniprot.org/uniprot/P31749                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-fold activation and 18-fold activation; when associated with D-473.|||55% inhibition of activation.|||7-fold activation and 25-fold activation; when associated with D-308.|||AGC-kinase C-terminal|||Abolished serine/threonine-protein kinase activity.|||Abolishes phosphorylation at Thr-308.|||Cleavage; by caspase-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs interaction with PtdIns(3,4,5)P3 and PtdIns(3,4)P2.|||In CWS6.|||In PROTEUSS and breast cancer; also detected in colorectal and ovarian cancer; somatic mutation; results in increased phosphorylation at T-308 and higher basal ubiquitination; the mutant protein is more efficiently recruited to the plasma membrane; alters phosphatidylinositiol phosphates lipid specificity of the AKT1 PH domain.|||In isoform 2.|||N6-acetyllysine|||No effect on membrane localization. Loss of membrane localization; when associated with Q-20.|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||PH|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by IKKE, MTOR and TBK1; alternate|||Phosphothreonine|||Phosphothreonine; by IKKE, PDPK1 and TBK1|||Phosphotyrosine|||Phosphotyrosine; by TNK2|||Protein kinase|||Proton acceptor|||RAC-alpha serine/threonine-protein kinase|||Reduces O-GlcNAc levels; Reduces O-GlcNAc levels even more; when associated with A-305.|||Reduces O-GlcNAc levels; Reduces O-GlcNAc levels even more; when associated with A-312.|||Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473.|||Slight increase of phosphorylation at T-308 and S-473.|||Substantial reduction of phosphorylation at T-308 and S-473, loss of AKT activation, and loss of binding to PIP3 as well as IGF1-induced membrane recruitment.|||Substantial reduction of phosphorylation at T-308 and S-473, reduced AKT activation, and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization; when associated with K-17.|||Substantial reduction of ubiquitination, phosphorylation at T-308 and S-473, AKT activation as well as IGF1-induced membrane recruitment. Decrease in ubiquitination and phosphorylation at T-308 as well as impaired association with the membrane; when associated with K-17.|||Substantial reduction of ubiquitination, phosphorylation at T-308 and S-473, AKT activation, loss of binding to PIP3 as well as IGF1-induced membrane recruitment.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085605|||http://purl.uniprot.org/annotation/VAR_051617|||http://purl.uniprot.org/annotation/VAR_055422|||http://purl.uniprot.org/annotation/VAR_069791|||http://purl.uniprot.org/annotation/VAR_069792|||http://purl.uniprot.org/annotation/VSP_056180
http://togogenome.org/gene/9606:RPSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG17|||http://purl.uniprot.org/uniprot/P08865                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by ST3; site 1|||Cleavage; by ST3; site 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In ICAS; reduced protein levels.|||Interaction with PPP1R16B|||Laminin-binding|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein uS2|||Small ribosomal subunit protein uS2 C-terminal|||[DE]-W-[ST] 1|||[DE]-W-[ST] 2|||[DE]-W-[ST] 3|||[DE]-W-[ST] 4|||[DE]-W-[ST] 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134358|||http://purl.uniprot.org/annotation/VAR_025522|||http://purl.uniprot.org/annotation/VAR_075092|||http://purl.uniprot.org/annotation/VAR_075093|||http://purl.uniprot.org/annotation/VAR_075094|||http://purl.uniprot.org/annotation/VAR_075095|||http://purl.uniprot.org/annotation/VAR_075096|||http://purl.uniprot.org/annotation/VAR_075097|||http://purl.uniprot.org/annotation/VAR_075098|||http://purl.uniprot.org/annotation/VAR_075099
http://togogenome.org/gene/9606:SPINK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RJC5|||http://purl.uniprot.org/uniprot/Q5DT21                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333808
http://togogenome.org/gene/9606:PINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXM7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with A-219 and A-362. Loss of enzyme activity and impaired localization of PRKN to mitochondria; when associated with M-219 and A-362.|||Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with A-219 and A-384. Loss of enzyme activity and impaired localization of PRKN to mitochondria; when associated with M-219 and A-384.|||Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with Ala-362 and Ala-384.|||Cytoplasmic|||Disordered|||Helical|||In 3EA; impaired ability to localize to the outer mitochondrial membrane.|||In PARK6.|||In PARK6; abolishes kinase activity.|||In PARK6; decreases PRKN and SNCAIP ubiquitination and degradation; slightly decreases Drp1 phosphorylation.|||In PARK6; early-onset.|||In PARK6; fails to maintain mitochondrial membrane potential; full-length mutant has no effect on autophosphorylation; strongly reduces interaction with PRKN; decreases PRKN and SNCAIP ubiquitination and degradation; decreases Drp1 phosphorylation.|||In PARK6; mitochondria are deformed and dysfunctional with decreased mitochondrial membrane potential; shows increased apoptosis; increased oxidative stress; decreased phosphorylation of DNM1L and Drp1.|||In PARK6; no effect on autophosphorylation; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space.|||In PARK6; strongly reduces interaction with PRKN.|||In PARK6; strongly reduces interaction with PRKN; reduced ubiquitination of MIRO1.|||In PARK6; unknown pathological significance.|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||Loss of activity. Abolishes Drp1 phosphorylation. No effect on localization to mitochondria.|||Loss of enzyme activity and impaired localization of PRKN to mitochondria; when associated with A-362 and A-384.|||May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions.|||Mitochondrial intermembrane|||Mitochondrion|||Phosphoserine; by autocatalysis|||Probable disease-associated variant found in early-onset Parkinson disease with digenic inheritance; found in a patient also carrying mutation S-39 in PARK7; decreases PRKN and SNCAIP ubiquitination and degradation.|||Protein kinase|||Proton acceptor|||Required for outer membrane localization|||Serine/threonine-protein kinase PINK1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024369|||http://purl.uniprot.org/annotation/VAR_018993|||http://purl.uniprot.org/annotation/VAR_018994|||http://purl.uniprot.org/annotation/VAR_018995|||http://purl.uniprot.org/annotation/VAR_018996|||http://purl.uniprot.org/annotation/VAR_041010|||http://purl.uniprot.org/annotation/VAR_041011|||http://purl.uniprot.org/annotation/VAR_041012|||http://purl.uniprot.org/annotation/VAR_041013|||http://purl.uniprot.org/annotation/VAR_041014|||http://purl.uniprot.org/annotation/VAR_041015|||http://purl.uniprot.org/annotation/VAR_041016|||http://purl.uniprot.org/annotation/VAR_041017|||http://purl.uniprot.org/annotation/VAR_046566|||http://purl.uniprot.org/annotation/VAR_046567|||http://purl.uniprot.org/annotation/VAR_046568|||http://purl.uniprot.org/annotation/VAR_046569|||http://purl.uniprot.org/annotation/VAR_046570|||http://purl.uniprot.org/annotation/VAR_046571|||http://purl.uniprot.org/annotation/VAR_046572|||http://purl.uniprot.org/annotation/VAR_046573|||http://purl.uniprot.org/annotation/VAR_046574|||http://purl.uniprot.org/annotation/VAR_046575|||http://purl.uniprot.org/annotation/VAR_046576|||http://purl.uniprot.org/annotation/VAR_046577|||http://purl.uniprot.org/annotation/VAR_046578|||http://purl.uniprot.org/annotation/VAR_046579|||http://purl.uniprot.org/annotation/VAR_046580|||http://purl.uniprot.org/annotation/VAR_046581|||http://purl.uniprot.org/annotation/VAR_046582|||http://purl.uniprot.org/annotation/VAR_046583|||http://purl.uniprot.org/annotation/VAR_046584|||http://purl.uniprot.org/annotation/VAR_046585|||http://purl.uniprot.org/annotation/VAR_046586|||http://purl.uniprot.org/annotation/VAR_046587|||http://purl.uniprot.org/annotation/VAR_046588|||http://purl.uniprot.org/annotation/VAR_046589|||http://purl.uniprot.org/annotation/VAR_046590|||http://purl.uniprot.org/annotation/VAR_046591|||http://purl.uniprot.org/annotation/VAR_046592|||http://purl.uniprot.org/annotation/VAR_046593|||http://purl.uniprot.org/annotation/VAR_046594|||http://purl.uniprot.org/annotation/VAR_046595|||http://purl.uniprot.org/annotation/VAR_046596|||http://purl.uniprot.org/annotation/VAR_046597|||http://purl.uniprot.org/annotation/VAR_046598|||http://purl.uniprot.org/annotation/VAR_046599|||http://purl.uniprot.org/annotation/VAR_046600|||http://purl.uniprot.org/annotation/VAR_046601|||http://purl.uniprot.org/annotation/VAR_046602|||http://purl.uniprot.org/annotation/VAR_046603|||http://purl.uniprot.org/annotation/VAR_046604|||http://purl.uniprot.org/annotation/VAR_046605|||http://purl.uniprot.org/annotation/VAR_046606|||http://purl.uniprot.org/annotation/VAR_046607|||http://purl.uniprot.org/annotation/VAR_046608|||http://purl.uniprot.org/annotation/VAR_046609|||http://purl.uniprot.org/annotation/VAR_046610|||http://purl.uniprot.org/annotation/VAR_046611|||http://purl.uniprot.org/annotation/VAR_046612|||http://purl.uniprot.org/annotation/VAR_062773|||http://purl.uniprot.org/annotation/VAR_062774|||http://purl.uniprot.org/annotation/VAR_062775|||http://purl.uniprot.org/annotation/VAR_062776|||http://purl.uniprot.org/annotation/VAR_062777|||http://purl.uniprot.org/annotation/VAR_062778|||http://purl.uniprot.org/annotation/VAR_062779|||http://purl.uniprot.org/annotation/VAR_064344|||http://purl.uniprot.org/annotation/VAR_078934|||http://purl.uniprot.org/annotation/VAR_078935|||http://purl.uniprot.org/annotation/VAR_084338|||http://purl.uniprot.org/annotation/VSP_050754|||http://purl.uniprot.org/annotation/VSP_050755
http://togogenome.org/gene/9606:H2AC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04908|||http://purl.uniprot.org/uniprot/Q08AJ9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1-B/E|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055237
http://togogenome.org/gene/9606:BAG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6M6|||http://purl.uniprot.org/uniprot/Q9UL15                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  BAG|||BAG 1|||BAG 2|||BAG 3|||BAG 4|||BAG 5|||BAG family molecular chaperone regulator 5|||In CMD2F.|||In CMD2F; loss of interaction with HSPA8.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088872|||http://purl.uniprot.org/annotation/VAR_058712|||http://purl.uniprot.org/annotation/VAR_086932|||http://purl.uniprot.org/annotation/VAR_086933|||http://purl.uniprot.org/annotation/VSP_037996
http://togogenome.org/gene/9606:FGF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVY9|||http://purl.uniprot.org/uniprot/O60258                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor 17|||In HH20.|||In HH20; rare variant associated with susceptibility to disease; some patients have a second mutation in another HH-associated gene including FGFR1, HS6ST1 and FLRT3; the mutant has reduced ability to activate FGFR1.|||In HH20; the mutant has reduced ability to activate FGFR1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008985|||http://purl.uniprot.org/annotation/VAR_069947|||http://purl.uniprot.org/annotation/VAR_069948|||http://purl.uniprot.org/annotation/VAR_069949|||http://purl.uniprot.org/annotation/VSP_008715
http://togogenome.org/gene/9606:DEFB105A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1I4|||http://purl.uniprot.org/uniprot/Q8NG35                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 105                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006975|||http://purl.uniprot.org/annotation/PRO_5034019771
http://togogenome.org/gene/9606:NUDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y266                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by PLK1; when associated with A-274.|||Abolishes phosphorylation by PLK1; when associated with A-326.|||Basic and acidic residues|||CS|||Disordered|||Interaction with EML4|||N6-acetyllysine|||Nuclear localization signal|||Nuclear migration protein nudC|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057990
http://togogenome.org/gene/9606:GPR45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5B0C1|||http://purl.uniprot.org/uniprot/Q9Y5Y3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069574|||http://purl.uniprot.org/annotation/VAR_035759|||http://purl.uniprot.org/annotation/VAR_049394
http://togogenome.org/gene/9606:SLC28A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43868|||http://purl.uniprot.org/uniprot/Q2M2A7|||http://purl.uniprot.org/uniprot/Q53H72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Concentrative nucleoside transporter C-terminal|||Concentrative nucleoside transporter N-terminal|||Disordered|||Helical|||Nucleoside transporter/FeoB GTPase Gate|||Phosphoserine|||Sodium/nucleoside cotransporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070450|||http://purl.uniprot.org/annotation/VAR_022001|||http://purl.uniprot.org/annotation/VAR_024639|||http://purl.uniprot.org/annotation/VAR_024640|||http://purl.uniprot.org/annotation/VAR_024641|||http://purl.uniprot.org/annotation/VAR_024642|||http://purl.uniprot.org/annotation/VAR_024643|||http://purl.uniprot.org/annotation/VAR_028724|||http://purl.uniprot.org/annotation/VAR_036817|||http://purl.uniprot.org/annotation/VAR_036818|||http://purl.uniprot.org/annotation/VAR_036819|||http://purl.uniprot.org/annotation/VAR_036820|||http://purl.uniprot.org/annotation/VAR_036821
http://togogenome.org/gene/9606:PLD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV08                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5'-3' exonuclease PLD3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Impairs myotube formation.|||In SCA46; unknown pathological significance; reduced lysosomal localization; induces retention in the ER; reduction of proteolityc cleavage; loss of exonuclease activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Originally reported as risk factor for Alzheimer disease; unknown pathological significance; does not reduce either amyloid-beta levels or APP expression.|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||Slightly increased plasma membrane localization, does not affect delivery to lysosomes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280326|||http://purl.uniprot.org/annotation/VAR_071186|||http://purl.uniprot.org/annotation/VAR_075905|||http://purl.uniprot.org/annotation/VAR_075906|||http://purl.uniprot.org/annotation/VAR_075907|||http://purl.uniprot.org/annotation/VAR_075908|||http://purl.uniprot.org/annotation/VAR_075909|||http://purl.uniprot.org/annotation/VAR_075910|||http://purl.uniprot.org/annotation/VAR_075911|||http://purl.uniprot.org/annotation/VAR_075912|||http://purl.uniprot.org/annotation/VAR_075913|||http://purl.uniprot.org/annotation/VAR_075914|||http://purl.uniprot.org/annotation/VAR_075915|||http://purl.uniprot.org/annotation/VAR_075916|||http://purl.uniprot.org/annotation/VAR_075917|||http://purl.uniprot.org/annotation/VAR_075918|||http://purl.uniprot.org/annotation/VAR_075919|||http://purl.uniprot.org/annotation/VAR_075920|||http://purl.uniprot.org/annotation/VAR_075921|||http://purl.uniprot.org/annotation/VAR_075922|||http://purl.uniprot.org/annotation/VAR_075923
http://togogenome.org/gene/9606:TAAR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RI8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070158|||http://purl.uniprot.org/annotation/VAR_019794|||http://purl.uniprot.org/annotation/VAR_019795|||http://purl.uniprot.org/annotation/VAR_019796|||http://purl.uniprot.org/annotation/VAR_019797|||http://purl.uniprot.org/annotation/VAR_019798|||http://purl.uniprot.org/annotation/VAR_019799|||http://purl.uniprot.org/annotation/VAR_019800|||http://purl.uniprot.org/annotation/VAR_061227
http://togogenome.org/gene/9606:ENC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14682|||http://purl.uniprot.org/uniprot/Q53XS2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||Ectoderm-neural cortex protein 1|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119068|||http://purl.uniprot.org/annotation/VAR_050040|||http://purl.uniprot.org/annotation/VSP_045074
http://togogenome.org/gene/9606:ZNF610                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9Z0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 610                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234595|||http://purl.uniprot.org/annotation/VAR_033582|||http://purl.uniprot.org/annotation/VAR_052873|||http://purl.uniprot.org/annotation/VAR_052874|||http://purl.uniprot.org/annotation/VAR_052875|||http://purl.uniprot.org/annotation/VSP_018387
http://togogenome.org/gene/9606:CASD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ77|||http://purl.uniprot.org/uniprot/Q96PB1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes O-acetyltransferase activity.|||Acyl-ester intermediate|||Cas1p 10 TM acyl transferase|||Cytoplasmic|||Helical|||Lumenal|||N-acetylneuraminate 9-O-acetyltransferase|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307230|||http://purl.uniprot.org/annotation/VAR_035383
http://togogenome.org/gene/9606:DEFB118                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTK2|||http://purl.uniprot.org/uniprot/Q96PH6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Defensin beta 118|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006983|||http://purl.uniprot.org/annotation/PRO_0000006984|||http://purl.uniprot.org/annotation/PRO_5034113193|||http://purl.uniprot.org/annotation/VAR_061133
http://togogenome.org/gene/9606:CTSZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBR2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin Z|||N-linked (GlcNAc...) asparagine|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026285|||http://purl.uniprot.org/annotation/PRO_0000026286|||http://purl.uniprot.org/annotation/VAR_010254|||http://purl.uniprot.org/annotation/VAR_010255|||http://purl.uniprot.org/annotation/VAR_033719
http://togogenome.org/gene/9606:CEP68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76N32                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 68 kDa|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||Prevents binding to BTRC and down-regulation of CEP68 during mitosis.|||Reduces CEP68 binding to BTRC.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089494|||http://purl.uniprot.org/annotation/VAR_022363|||http://purl.uniprot.org/annotation/VAR_050794|||http://purl.uniprot.org/annotation/VAR_050795|||http://purl.uniprot.org/annotation/VAR_050796|||http://purl.uniprot.org/annotation/VAR_050797|||http://purl.uniprot.org/annotation/VSP_013476
http://togogenome.org/gene/9606:GLYATL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU03                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glycine N-acyltransferase-like protein 2|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281875|||http://purl.uniprot.org/annotation/VAR_031296|||http://purl.uniprot.org/annotation/VAR_031297|||http://purl.uniprot.org/annotation/VAR_031298
http://togogenome.org/gene/9606:ITFG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5P1|||http://purl.uniprot.org/uniprot/Q969R8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  FG-GAP 1; atypical|||FG-GAP 2; atypical|||In isoform 2.|||KICSTOR complex protein ITFG2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289292|||http://purl.uniprot.org/annotation/VSP_055985|||http://purl.uniprot.org/annotation/VSP_055986
http://togogenome.org/gene/9606:VPS4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75351                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with VTA1.|||Basic and acidic residues|||Defective in vacuolar protein sorting.|||Disordered|||Impairs HIV-1 release.|||Induces thermal instability.|||MIT|||Phosphoserine|||Reduces HIV-1 release 10-fold; when associated with D-15.|||Reduces HIV-1 release 10-fold; when associated with D-66.|||Reduces HIV-1 release 2-fold.|||Reduces HIV-1 release 3-fold.|||Strongly impairs HIV-1 release.|||Vacuolar protein sorting-associated protein 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084767|||http://purl.uniprot.org/annotation/VAR_023385
http://togogenome.org/gene/9606:SMIM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EJ46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Small integral membrane protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000424385|||http://purl.uniprot.org/annotation/VSP_060203
http://togogenome.org/gene/9606:CLBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein CLBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274387
http://togogenome.org/gene/9606:TOP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11388                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to the antibody MPM2.|||Acidic residues|||Basic and acidic residues|||DNA topoisomerase 2-alpha|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs bending of target DNA. Strongly reduced DNA cleavage.|||Important for DNA bending; intercalates between base pairs of target DNA|||In amsacrine resistant cells.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In teniposide (VM-26) resistant cells.|||Interaction with DNA|||Interaction with PLSCR1|||N-acetylmethionine|||N6-acetyllysine; alternate|||Nuclear export signal|||O-(5'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphothreonine; by PLK3|||Polar residues|||Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.|||Strongly reduced DNA cleavage.|||Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.|||Toprim|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145363|||http://purl.uniprot.org/annotation/VAR_007532|||http://purl.uniprot.org/annotation/VAR_007533|||http://purl.uniprot.org/annotation/VAR_029245|||http://purl.uniprot.org/annotation/VAR_052594|||http://purl.uniprot.org/annotation/VAR_052595|||http://purl.uniprot.org/annotation/VSP_006529|||http://purl.uniprot.org/annotation/VSP_006530|||http://purl.uniprot.org/annotation/VSP_006531
http://togogenome.org/gene/9606:PIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1W9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086532|||http://purl.uniprot.org/annotation/VAR_041008|||http://purl.uniprot.org/annotation/VAR_041009
http://togogenome.org/gene/9606:ADRA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0ZBD3|||http://purl.uniprot.org/uniprot/P35348                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-348.|||Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-342 and A-349.|||Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-335; A-348 and A-349.|||Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-334; A-342; A-348 and A-349.|||Abolishes targeting to the nuclear membrane of cardiac myocytes; when associated with A-335; A-342; A-348 and A-349.|||Alpha-1A adrenergic receptor|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphoserine; by PKA|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069063|||http://purl.uniprot.org/annotation/VAR_019509|||http://purl.uniprot.org/annotation/VAR_035756|||http://purl.uniprot.org/annotation/VAR_049370|||http://purl.uniprot.org/annotation/VAR_049371|||http://purl.uniprot.org/annotation/VAR_049372|||http://purl.uniprot.org/annotation/VSP_011044|||http://purl.uniprot.org/annotation/VSP_011045|||http://purl.uniprot.org/annotation/VSP_011046|||http://purl.uniprot.org/annotation/VSP_011047|||http://purl.uniprot.org/annotation/VSP_011048|||http://purl.uniprot.org/annotation/VSP_011049|||http://purl.uniprot.org/annotation/VSP_011050|||http://purl.uniprot.org/annotation/VSP_011051|||http://purl.uniprot.org/annotation/VSP_011052|||http://purl.uniprot.org/annotation/VSP_011053|||http://purl.uniprot.org/annotation/VSP_011054|||http://purl.uniprot.org/annotation/VSP_011055
http://togogenome.org/gene/9606:XKR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZMN2|||http://purl.uniprot.org/uniprot/Q5GH77                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||XK-related protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190776|||http://purl.uniprot.org/annotation/VAR_053740|||http://purl.uniprot.org/annotation/VAR_053741|||http://purl.uniprot.org/annotation/VAR_053742|||http://purl.uniprot.org/annotation/VAR_053743
http://togogenome.org/gene/9606:GBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PP8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished GTPase activity, without affecting ability to inhibit HIV-1 infectivity.|||Cysteine methyl ester|||Decreased nucleotide-binding, without affecting ability to inhibit HIV-1 infectivity.|||Does not affect GTPase activity.|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 5|||In MMMD mutant; abolished dimerization and ability to restrict HIV-1; when associated with 417-A--A-421.|||In MMMD mutant; abolished dimerization and ability to restrict HIV-1; when associated with 464-A--A-476.|||In isoform 2.|||Loss of GTPase activity. No effect on tetramerization. Does not affect ability to inhibit HIV-1 infectivity.|||Loss of isoprenylation and of localization at the Golgi apparatus.|||Loss of isoprenylation and of localization at the Golgi apparatus. Impaired ability to restrict HIV-1.|||NLRP3-binding|||No effect.|||Promotes ubiquitination and degradation by S. flexneri IpaH9.8.|||Removed in mature form|||Required for tetramerization, but not for dimerization|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190969|||http://purl.uniprot.org/annotation/PRO_0000370785|||http://purl.uniprot.org/annotation/VAR_033956|||http://purl.uniprot.org/annotation/VAR_053104|||http://purl.uniprot.org/annotation/VSP_044362|||http://purl.uniprot.org/annotation/VSP_044363
http://togogenome.org/gene/9606:HMG20B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0W2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||In isoform 2.|||In isoform 3.|||Loss of DNA binding activity of the BHC histone deacetylase complex.|||Phosphoserine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048575|||http://purl.uniprot.org/annotation/VSP_037131|||http://purl.uniprot.org/annotation/VSP_037132
http://togogenome.org/gene/9606:DCAF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT20|||http://purl.uniprot.org/uniprot/Q9NV06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 13|||Disordered|||In isoform 2.|||N6-acetyllysine|||Pro residues|||Required for nucleolar location|||Sof1-like protein|||Translation initiation factor beta propellor-like|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310428|||http://purl.uniprot.org/annotation/VAR_037035|||http://purl.uniprot.org/annotation/VAR_037036|||http://purl.uniprot.org/annotation/VSP_029283|||http://purl.uniprot.org/annotation/VSP_029284
http://togogenome.org/gene/9606:ATP2C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E295|||http://purl.uniprot.org/uniprot/B4E2Q0|||http://purl.uniprot.org/uniprot/P98194                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Calcium-transporting ATPase type 2C member 1|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Decreases calcium-dependent autophosphorylation and the ATPase activity; when associated with A-41.|||Decreases calcium-dependent autophosphorylation and the ATPase activity; when associated with A-50.|||Decreases calcium-dependent autophosphorylation.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Impairs pump activity.|||In HHD.|||In HHD; decreases protein expression.|||In HHD; has normal catalytic cycle.|||In HHD; impairs calcium- and manganese-dependent autophosphorylation.|||In HHD; impairs manganese-dependent autophosphorylation in the presence of ATP; impairs manganese transporter activity.|||In HHD; impairs phosphoenzyme dephosphorylation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9 and isoform 8.|||Increases manganese transporter activity.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046223|||http://purl.uniprot.org/annotation/VAR_008803|||http://purl.uniprot.org/annotation/VAR_008804|||http://purl.uniprot.org/annotation/VAR_008805|||http://purl.uniprot.org/annotation/VAR_008806|||http://purl.uniprot.org/annotation/VAR_008807|||http://purl.uniprot.org/annotation/VAR_008808|||http://purl.uniprot.org/annotation/VAR_010130|||http://purl.uniprot.org/annotation/VAR_010131|||http://purl.uniprot.org/annotation/VAR_010132|||http://purl.uniprot.org/annotation/VAR_019523|||http://purl.uniprot.org/annotation/VAR_019524|||http://purl.uniprot.org/annotation/VAR_022672|||http://purl.uniprot.org/annotation/VAR_022673|||http://purl.uniprot.org/annotation/VAR_022674|||http://purl.uniprot.org/annotation/VAR_022675|||http://purl.uniprot.org/annotation/VAR_022676|||http://purl.uniprot.org/annotation/VAR_022677|||http://purl.uniprot.org/annotation/VAR_048373|||http://purl.uniprot.org/annotation/VAR_079698|||http://purl.uniprot.org/annotation/VAR_079699|||http://purl.uniprot.org/annotation/VAR_079700|||http://purl.uniprot.org/annotation/VAR_079701|||http://purl.uniprot.org/annotation/VAR_079702|||http://purl.uniprot.org/annotation/VSP_000408|||http://purl.uniprot.org/annotation/VSP_000409|||http://purl.uniprot.org/annotation/VSP_000410|||http://purl.uniprot.org/annotation/VSP_014102|||http://purl.uniprot.org/annotation/VSP_045892|||http://purl.uniprot.org/annotation/VSP_055036|||http://purl.uniprot.org/annotation/VSP_055037
http://togogenome.org/gene/9606:KMT2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14686|||http://purl.uniprot.org/uniprot/Q59FG6|||http://purl.uniprot.org/uniprot/Q6PIA1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 5 AA repeats of S/P-P-P-E/P-E/A|||2|||3|||4|||5|||6|||7|||8|||9|||Abolishes interaction with S-adenosyl-L-methionine.|||Asymmetric dimethylarginine|||Basic and acidic residues|||C2HC pre-PHD-type 1; degenerate|||C2HC pre-PHD-type 2|||Disordered|||FYR C-terminal|||FYR N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase 2D|||In BCAHH.|||In BCAHH; affects secondary structure as shown by circular dichroism analysis.|||In BCAHH; unknown pathological significance.|||In KABUK1.|||In KABUK1; unknown pathological significance.|||In isoform 3.|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||LXXLL motif 6|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4|||PHD-type 5|||PHD-type 6|||PHD-type 7|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||RING-type 1; atypical|||RING-type 2; degenerate|||RING-type 3; atypical|||SET|||WDR5 interaction motif (WIN)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124878|||http://purl.uniprot.org/annotation/VAR_017115|||http://purl.uniprot.org/annotation/VAR_057359|||http://purl.uniprot.org/annotation/VAR_063830|||http://purl.uniprot.org/annotation/VAR_063831|||http://purl.uniprot.org/annotation/VAR_063832|||http://purl.uniprot.org/annotation/VAR_063833|||http://purl.uniprot.org/annotation/VAR_063834|||http://purl.uniprot.org/annotation/VAR_064370|||http://purl.uniprot.org/annotation/VAR_064371|||http://purl.uniprot.org/annotation/VAR_064372|||http://purl.uniprot.org/annotation/VAR_064373|||http://purl.uniprot.org/annotation/VAR_064374|||http://purl.uniprot.org/annotation/VAR_064375|||http://purl.uniprot.org/annotation/VAR_064376|||http://purl.uniprot.org/annotation/VAR_064377|||http://purl.uniprot.org/annotation/VAR_064378|||http://purl.uniprot.org/annotation/VAR_064379|||http://purl.uniprot.org/annotation/VAR_074216|||http://purl.uniprot.org/annotation/VAR_074217|||http://purl.uniprot.org/annotation/VAR_074218|||http://purl.uniprot.org/annotation/VAR_074219|||http://purl.uniprot.org/annotation/VAR_074220|||http://purl.uniprot.org/annotation/VAR_074221|||http://purl.uniprot.org/annotation/VAR_074222|||http://purl.uniprot.org/annotation/VAR_074223|||http://purl.uniprot.org/annotation/VAR_074224|||http://purl.uniprot.org/annotation/VAR_074225|||http://purl.uniprot.org/annotation/VAR_074226|||http://purl.uniprot.org/annotation/VAR_074227|||http://purl.uniprot.org/annotation/VAR_074228|||http://purl.uniprot.org/annotation/VAR_074229|||http://purl.uniprot.org/annotation/VAR_074230|||http://purl.uniprot.org/annotation/VAR_074231|||http://purl.uniprot.org/annotation/VAR_074232|||http://purl.uniprot.org/annotation/VAR_074233|||http://purl.uniprot.org/annotation/VAR_074234|||http://purl.uniprot.org/annotation/VAR_074235|||http://purl.uniprot.org/annotation/VAR_074236|||http://purl.uniprot.org/annotation/VAR_074237|||http://purl.uniprot.org/annotation/VAR_074238|||http://purl.uniprot.org/annotation/VAR_074239|||http://purl.uniprot.org/annotation/VAR_074240|||http://purl.uniprot.org/annotation/VAR_074241|||http://purl.uniprot.org/annotation/VAR_074242|||http://purl.uniprot.org/annotation/VAR_074243|||http://purl.uniprot.org/annotation/VAR_074244|||http://purl.uniprot.org/annotation/VAR_074245|||http://purl.uniprot.org/annotation/VAR_074246|||http://purl.uniprot.org/annotation/VAR_074247|||http://purl.uniprot.org/annotation/VAR_074248|||http://purl.uniprot.org/annotation/VAR_074249|||http://purl.uniprot.org/annotation/VAR_074250|||http://purl.uniprot.org/annotation/VAR_074251|||http://purl.uniprot.org/annotation/VAR_074252|||http://purl.uniprot.org/annotation/VAR_074253|||http://purl.uniprot.org/annotation/VAR_074254|||http://purl.uniprot.org/annotation/VAR_074255|||http://purl.uniprot.org/annotation/VAR_074256|||http://purl.uniprot.org/annotation/VAR_074257|||http://purl.uniprot.org/annotation/VAR_074258|||http://purl.uniprot.org/annotation/VAR_074259|||http://purl.uniprot.org/annotation/VAR_074260|||http://purl.uniprot.org/annotation/VAR_074261|||http://purl.uniprot.org/annotation/VAR_087947|||http://purl.uniprot.org/annotation/VAR_087948|||http://purl.uniprot.org/annotation/VAR_087949|||http://purl.uniprot.org/annotation/VAR_087950|||http://purl.uniprot.org/annotation/VAR_087951|||http://purl.uniprot.org/annotation/VAR_087952|||http://purl.uniprot.org/annotation/VAR_087953|||http://purl.uniprot.org/annotation/VAR_087954|||http://purl.uniprot.org/annotation/VAR_087955|||http://purl.uniprot.org/annotation/VAR_087956|||http://purl.uniprot.org/annotation/VAR_087957|||http://purl.uniprot.org/annotation/VAR_087958|||http://purl.uniprot.org/annotation/VAR_087959|||http://purl.uniprot.org/annotation/VAR_087960|||http://purl.uniprot.org/annotation/VAR_087961|||http://purl.uniprot.org/annotation/VAR_087962|||http://purl.uniprot.org/annotation/VAR_087963|||http://purl.uniprot.org/annotation/VAR_087964|||http://purl.uniprot.org/annotation/VAR_087965|||http://purl.uniprot.org/annotation/VAR_087966|||http://purl.uniprot.org/annotation/VAR_087967|||http://purl.uniprot.org/annotation/VAR_087968|||http://purl.uniprot.org/annotation/VAR_087969|||http://purl.uniprot.org/annotation/VAR_087970|||http://purl.uniprot.org/annotation/VSP_008560
http://togogenome.org/gene/9606:PLPP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14495                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dityrosine basolateral targeting motif|||Extracellular|||Helical|||Integrin-binding motif|||Loss of basolateral localization in polarized cells.|||Loss of binding to integrin. Loss of function in integrin-mediated cell-cell interaction.|||Mediates interaction with CTNND1|||N-linked (GlcNAc...) asparagine|||No effect on basolateral localization in polarized cells.|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phospholipid phosphatase 3|||Phosphoserine|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220912
http://togogenome.org/gene/9606:TAX1BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSG5|||http://purl.uniprot.org/uniprot/Q86VP1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of MAP1LC3B binding.|||Complete loss of TBK1 and RB1CC1 binding.|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Normal affinity for ubiquitin.|||Oligomerization|||Phosphoserine|||Phosphoserine; by IKKA|||Polar residues|||Reduced affinity for ubiquitin.|||Tax1-binding protein 1|||UBZ1-type|||UBZ1-type 1|||UBZ1-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234554|||http://purl.uniprot.org/annotation/VAR_026286|||http://purl.uniprot.org/annotation/VAR_035665|||http://purl.uniprot.org/annotation/VAR_051415|||http://purl.uniprot.org/annotation/VSP_018354|||http://purl.uniprot.org/annotation/VSP_018355|||http://purl.uniprot.org/annotation/VSP_045921
http://togogenome.org/gene/9606:ABCA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78363|||http://purl.uniprot.org/uniprot/Q6AI28                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||Abolishes basal and retinal-stimulated ATP hydrolysis.|||Benign variant.|||Cleavage; by trypsin|||Cytoplasmic|||Decreases 11-cis-Retinal binding affinity by 50%.|||Decreases solubility at 50%. Loss of intracellular vesicle localization. Does not affect substrate binding. Reduces basal ATPase activity.|||Disordered|||Does not affect protein abundance. Does not affect ATPase activity. Moderately decreased phospholipid translocase activity.|||Does not affect protein folding; when associated with Q-1087. Loss of ATPase activity; when associated with Q-1087.|||Does not affect protein folding; when associated with Q-2096. Loss of ATPase activity; when associated with Q-2096.|||Does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity.|||Essential for ATP binding and ATPase activity|||Extracellular|||Found in a patient with chorioretinal atrophy; unknown pathological significance.|||Found in a patient with chorioretinal atrophy; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity.|||Found in a patient with macular dystrophy; unknown pathological significance.|||Found in a patient with pattern dystrophy; unknown pathological significance.|||Helical|||Highly decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.|||In ARMD2 and STGD1; also found in patients with fundus flavimaculatus; reduced ATP-binding capacity.|||In ARMD2 and STGD1; reduced ATP-binding capacity; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; very low substrate binding.|||In ARMD2 and STGD1; unknown pathological significance; ATP-binding capacity and retinal stimulation as in wild-type.|||In ARMD2, FFM and STGD1; also found in a patient with cone dystrophy.|||In ARMD2.|||In CORD3 and STGD1; unknown pathological significance.|||In CORD3, ARMD2 and STGD1; unknown pathological significance; increased retinal-stimulated ATP hydrolysis.|||In CORD3.|||In CORD3; unknown pathological significance.|||In CORD3; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding.|||In FFM and STGD1.|||In FFM and STGD1; decreases solubilized at 70%; does not affect intracellular vesicle localization; does not affect substrate binding; drastically reduces basal ATPase activity with little or no substrate stimulation.|||In FFM.|||In FFM; highly reduced ATP-binding capacity; abolishes basal and retinal-stimulated ATP hydrolysis.|||In FFM; unknown pathological significance.|||In RP19; unknown pathological significance.|||In STGD1 and ARMD2; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; Increases N-Ret-PE binding.|||In STGD1 and ARMD2; highly reduced ATP-binding capacity; inhibition of ATP hydrolysis by retinal.|||In STGD1 and CORD3.|||In STGD1 and CORD3; common mutation in southern Europe; reduced ATP-binding capacity.|||In STGD1 and CORD3; may act as a modifier of macular dystrophy in patients who also have a Trp-172 mutation in PRPH2.|||In STGD1 and CORD3; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine.|||In STGD1 and CORD3; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis.|||In STGD1 and CORD3; reduced retinal-stimulated ATP hydrolysis.|||In STGD1 and CORD3; unknown pathological significance.|||In STGD1 and FFM.|||In STGD1 and FFM; also found in a patient with chorioretinal atrophy; highly reduced ATP-binding capacity.|||In STGD1 and FFM; also found in a patient with chorioretinal atrophy; reduced retinal-stimulated ATP hydrolysis; does not affect secondary structure; oss of structural flexibility; significantly decreases all-trans-retinal binding.|||In STGD1 and FFM; reduced ATP-binding capacity.|||In STGD1 and FFM; unknown pathological significance.|||In STGD1 and RP19; unknown pathological significance.|||In STGD1, FFM and CORD3.|||In STGD1, FFM and CORD3; also found in a patient with bull's eye maculopathy; mild alteration probably leading to disease phenotype only in combination with a more severe allele; frequent mutation in northern Europe in linkage disequilibrium with the polymorphic variant Q-943; reduced ATP-binding capacity and retinal-stimulated ATP hydrolysis; significantly attenuates 11-cis-retinal binding; decreases about 80% the N-retinylidene-phosphatidylethanolamine transport activity; stimulates modestely the retinal-stimulated ATPase activity; does not affect ATP-independent N-retinylidene-phosphatidylethanolamine binding. Does not affect ATP-dependent release of N-retinylidene-phosphatidylethanolamine; significantly reduces phosphatidylethanolamine flippase activity.|||In STGD1, FFM and CORD3; also found patients with cone dystrophy and with macular dystrophy; frequent mutation; may be associated with ARMD2; inhibition of ATP hydrolysis by retinal.|||In STGD1, FFM and CORD3; frequent mutation; reduced ATP-binding and retinal-stimulated ATP hydrolysis; decreases solubility at 70%; does not affect intracellular vesicle localization; significantly reduces substrate binding in the absence of ATP; reduces basal ATPase activity.|||In STGD1, FFM and CORD3; reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis; does not affect solubility; does not affect intracellular vesicle localization; significantly reduces substrate binding; drastically reduces basal ATPase activity with little or no substrate stimulation.|||In STGD1, FFM, ARMD2 and CORD3; found in a patient with bull's eye maculopathy; unknown pathological significance.|||In STGD1.|||In STGD1; also found in a patient with bull's eye maculopathy; unknown pathological significance; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity.|||In STGD1; also found in a patient with chorioretinal atrophy; reduced ATP-binding capacity; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase.|||In STGD1; also found in a patient with chorioretinal atrophy; reduced retinal-stimulated ATP hydrolysis.|||In STGD1; also found in a patient with macular dystrophy; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity; very low substrate binding.|||In STGD1; also found in a patient with macular dystrophy; unknown pathological significance.|||In STGD1; does not affect intracellular vesicle localization; does not affect solubility; significantly reduces N-Ret-PE binding; drastically reduces basal ATPase activity with little or no all trans retinal stimulation.|||In STGD1; does not affect secondary structure; decreases structural flexibility; significantly decreases all-trans-retinal binding.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; decreases N-Ret-PE binding in the range of 40-70%.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; does not affect N-Ret-PE binding.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; decreases N-Ret-PE binding in the range of 40-70%.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; increases N-Ret-PE binding.|||In STGD1; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; very low substrate binding.|||In STGD1; found in a patient with age-related macular degeneration; unknown pathological significance.|||In STGD1; found in a patient with bull's eye maculopathy; unknown pathological significance.|||In STGD1; found in a patient with chorioretinal atrophy; unknown pathological significance.|||In STGD1; highly decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity.|||In STGD1; highly reduced ATP-binding capacity.|||In STGD1; highly reduced ATP-binding capacity; abolishes retinal-stimulated ATP hydrolysis.|||In STGD1; highly reduced ATP-binding capacity; decreases solubility at 50 %; loss of intracellular vesicle localization; drastically reduced basal activity with little or no substrate stimulation.|||In STGD1; highly reduced ATP-binding capacity; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding.|||In STGD1; inhibition of ATP hydrolysis by retinal.|||In STGD1; loss of the majority of alpha-helical secondary structure; does not bind all-trans-retinal; does not affect conformational change.|||In STGD1; may predispose to develop retinal toxicity after treatment with chloroquine and hydroxychloroquine.|||In STGD1; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity.|||In STGD1; moderately decreased protein abundance; moderately decreased ATPase activity; moderately decreased phospholipid translocase activity.|||In STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase.|||In STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; very low substrate binding.|||In STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity.|||In STGD1; moderately decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity.|||In STGD1; reduced ATP-binding capacity.|||In STGD1; reduced basal and retinal-stimulated ATP-hydrolysis.|||In STGD1; reduced retinal-stimulated ATP hydrolysis.|||In STGD1; reduced retinal-stimulated ATP hydrolysis; moderately decreased protein abundance; highly decreased ATPase activity; highly decreased phospholipid translocase activity; decreases about 60% the N-retinylidene-phosphatidylethanolamine transfer activity; stimulates modestly the retinal-stimulated ATPase activity; does not affect ATP-independent N-retinylidene-phosphatidylethanolamine binding; does not affect ATP-dependent release of N-retinylidene-phosphatidylethanolamine; significantly reduces phosphatidylethanolamine flippase activity.|||In STGD1; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding.|||In STGD1; slightly reduced retinal-stimulated ATP hydrolysis; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; does not affect N-Ret-PE binding.|||In STGD1; unknown pathological significance.|||In STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; decreases basal ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase.|||In STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; increases N-Ret-PE binding.|||In STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle; does not affect both basal and N-Ret-PE-stimulated ATPase activity; very low substrate binding.|||In STGD1; unknown pathological significance; does not affect solubility; does not affect location in cytoplasmic vesicle;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity.|||In STGD1; unknown pathological significance; loss of cytoplasmic vesicle localization; decreases ATPase activity between 50% and 80%; decreases modestly N-Ret-PE-stimulated ATPase; decreases solubility below 50%; significantly reduces N-Ret-PE binding in the absence of ATP.|||In STGD1; unknown pathological significance; moderately decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; decreases modestly N-Ret-PE-stimulated ATPase.|||In STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity.|||In STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization; very low substrate binding.|||In STGD1; unknown pathological significance; severely decreases solubility; loss of cytoplasmic vesicle localization;decreases basal ATPase activity below 50%; loss of N-Ret-PE-induced stimulation in ATPase activity; very low substrate binding.|||In a breast cancer sample; somatic mutation.|||In linkage disequilibrium with A-863 in the European population and STGD1; found in a patient with macular dystrophy; unknown pathological significance; decreases 11-cis-Retinal binding affinity by 100-fold.|||Inhibition of retinal-stimulated ATP hydrolysis.|||Inhibits ATPase activity; when associated with M-1978. Decreases translocase activity; when associated with M-1978. Does not affect protein subcellular localization in endoplasmic reticulum; when associated with M-1978. Loss of ATP-dependent all-trans-retinal transport; when associated with M-1978. Loss in N-retinylidene-PE transfer activity. Inhibits ATPase activity with increasing retinal concentration. Does not affect N-retinylidene-PE binding. Impairs ATP-dependent release of N-retinylidene-PE. Significantly reduces PE flippase activity.|||Inhibits ATPase activity; when associated with M-969. Decreases translocase activity; when associated with M-969. Does not affect protein subcellular localization in endoplasmic reticulum; when associated with M-969. Loss of ATP-dependent all-trans-retinal transport; when associated with M-1978. Loss in N-retinylidene-PE transfer activity. Inhibits ATPase activity with increasing retinal concentration. Does not affect ATP-independent N-retinylidene-PE binding. Does not affect ATP-dependent of N-retinylidene-PE release. Significantly reduces PE flippase activity. Inhibition of retinal-stimulated ATP hydrolysis.|||Interchain|||Moderately decreased protein abundance. Moderately decreased ATPase activity. Moderately decreased phospholipid translocase activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Retinal-specific phospholipid-transporting ATPase ABCA4|||Severely decreases solubility. Loss of cytoplasmic vesicle localization. Decreases basal ATPase activity below 50%. Loss of N-Ret-PE-induced stimulation in ATPase activity.|||Severely decreases solubility; loss of cytoplasmic vesicle localization; decreases basal ATPase activity below 50%; severely decreases N-Ret-PE-stimulated ATPase activity; very low substrate binding.|||Unknown pathological significance. ^@                                                                                  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uniprot.org/annotation/VAR_012602|||http://purl.uniprot.org/annotation/VAR_012603|||http://purl.uniprot.org/annotation/VAR_012604|||http://purl.uniprot.org/annotation/VAR_012605|||http://purl.uniprot.org/annotation/VAR_012606|||http://purl.uniprot.org/annotation/VAR_012607|||http://purl.uniprot.org/annotation/VAR_012608|||http://purl.uniprot.org/annotation/VAR_012609|||http://purl.uniprot.org/annotation/VAR_012610|||http://purl.uniprot.org/annotation/VAR_012611|||http://purl.uniprot.org/annotation/VAR_012612|||http://purl.uniprot.org/annotation/VAR_012613|||http://purl.uniprot.org/annotation/VAR_012614|||http://purl.uniprot.org/annotation/VAR_012615|||http://purl.uniprot.org/annotation/VAR_012616|||http://purl.uniprot.org/annotation/VAR_012617|||http://purl.uniprot.org/annotation/VAR_014703|||http://purl.uniprot.org/annotation/VAR_035736|||http://purl.uniprot.org/annotation/VAR_067427|||http://purl.uniprot.org/annotation/VAR_067428|||http://purl.uniprot.org/annotation/VAR_067429|||http://purl.uniprot.org/annotation/VAR_067430|||http://purl.uniprot.org/annotation/VAR_084833|||http://purl.uniprot.org/annotation/VAR_084834|||http://purl.uniprot.org/annotation/VAR_084835|||http://purl.uniprot.org/annotation/VAR_084836|||http://purl.uniprot.org/annotation/VAR_084837|||http://purl.uniprot.org/annotation/VAR_084838|||http://purl.uniprot.org/annotation/VAR_084839|||http://purl.uniprot.org/annotation/VAR_084840|||http://purl.uniprot.org/annotation/VAR_084841|||http://purl.uniprot.org/annotation/VAR_084842|||http://purl.uniprot.org/annotation/VAR_084843|||http://purl.uniprot.org/annotation/VAR_084844|||http://purl.uniprot.org/annotation/VAR_084845|||http://purl.uniprot.org/annotation/VAR_084846|||http://purl.uniprot.org/annotation/VAR_084847|||http://purl.uniprot.org/annotation/VAR_084848|||http://purl.uniprot.org/annotation/VAR_084849|||http://purl.uniprot.org/annotation/VAR_084850|||http://purl.uniprot.org/annotation/VAR_084851|||http://purl.uniprot.org/annotation/VAR_084852|||http://purl.uniprot.org/annotation/VAR_084853|||http://purl.uniprot.org/annotation/VAR_084854|||http://purl.uniprot.org/annotation/VAR_084855|||http://purl.uniprot.org/annotation/VAR_084856|||http://purl.uniprot.org/annotation/VAR_084857|||http://purl.uniprot.org/annotation/VAR_084858|||http://purl.uniprot.org/annotation/VAR_084859|||http://purl.uniprot.org/annotation/VAR_084860|||http://purl.uniprot.org/annotation/VAR_084861|||http://purl.uniprot.org/annotation/VAR_084862|||http://purl.uniprot.org/annotation/VAR_084863|||http://purl.uniprot.org/annotation/VAR_084864|||http://purl.uniprot.org/annotation/VAR_084865|||http://purl.uniprot.org/annotation/VAR_084866|||http://purl.uniprot.org/annotation/VAR_084867|||http://purl.uniprot.org/annotation/VAR_084868|||http://purl.uniprot.org/annotation/VAR_084869|||http://purl.uniprot.org/annotation/VAR_084870|||http://purl.uniprot.org/annotation/VAR_084871|||http://purl.uniprot.org/annotation/VAR_084872|||http://purl.uniprot.org/annotation/VAR_084873|||http://purl.uniprot.org/annotation/VAR_084874|||http://purl.uniprot.org/annotation/VAR_084875|||http://purl.uniprot.org/annotation/VAR_084876|||http://purl.uniprot.org/annotation/VAR_084877|||http://purl.uniprot.org/annotation/VAR_084878|||http://purl.uniprot.org/annotation/VAR_084879|||http://purl.uniprot.org/annotation/VAR_084880|||http://purl.uniprot.org/annotation/VAR_084881|||http://purl.uniprot.org/annotation/VAR_084882|||http://purl.uniprot.org/annotation/VAR_084883|||http://purl.uniprot.org/annotation/VAR_084884|||http://purl.uniprot.org/annotation/VAR_084885|||http://purl.uniprot.org/annotation/VAR_084886|||http://purl.uniprot.org/annotation/VAR_084887|||http://purl.uniprot.org/annotation/VAR_084888|||http://purl.uniprot.org/annotation/VAR_084889|||http://purl.uniprot.org/annotation/VAR_084890|||http://purl.uniprot.org/annotation/VAR_084891|||http://purl.uniprot.org/annotation/VAR_084892|||http://purl.uniprot.org/annotation/VAR_084893|||http://purl.uniprot.org/annotation/VAR_084894|||http://purl.uniprot.org/annotation/VAR_084895|||http://purl.uniprot.org/annotation/VAR_084896|||http://purl.uniprot.org/annotation/VAR_084897|||http://purl.uniprot.org/annotation/VAR_084898|||http://purl.uniprot.org/annotation/VAR_084899|||http://purl.uniprot.org/annotation/VAR_084900|||http://purl.uniprot.org/annotation/VAR_084901|||http://purl.uniprot.org/annotation/VAR_084902|||http://purl.uniprot.org/annotation/VAR_084903|||http://purl.uniprot.org/annotation/VAR_084904|||http://purl.uniprot.org/annotation/VAR_084905|||http://purl.uniprot.org/annotation/VAR_084906|||http://purl.uniprot.org/annotation/VAR_084907|||http://purl.uniprot.org/annotation/VAR_084908|||http://purl.uniprot.org/annotation/VAR_084909|||http://purl.uniprot.org/annotation/VAR_084910|||http://purl.uniprot.org/annotation/VAR_084911|||http://purl.uniprot.org/annotation/VAR_084912|||http://purl.uniprot.org/annotation/VAR_084913|||http://purl.uniprot.org/annotation/VAR_084914|||http://purl.uniprot.org/annotation/VAR_084915|||http://purl.uniprot.org/annotation/VAR_084916|||http://purl.uniprot.org/annotation/VAR_084917|||http://purl.uniprot.org/annotation/VAR_084918|||http://purl.uniprot.org/annotation/VAR_084919|||http://purl.uniprot.org/annotation/VAR_084920|||http://purl.uniprot.org/annotation/VAR_084921|||http://purl.uniprot.org/annotation/VAR_084922|||http://purl.uniprot.org/annotation/VAR_084923|||http://purl.uniprot.org/annotation/VAR_084924|||http://purl.uniprot.org/annotation/VAR_084925|||http://purl.uniprot.org/annotation/VAR_084926|||http://purl.uniprot.org/annotation/VAR_084927|||http://purl.uniprot.org/annotation/VAR_084928|||http://purl.uniprot.org/annotation/VAR_084929|||http://purl.uniprot.org/annotation/VAR_084930|||http://purl.uniprot.org/annotation/VAR_084931|||http://purl.uniprot.org/annotation/VAR_084932|||http://purl.uniprot.org/annotation/VAR_084933|||http://purl.uniprot.org/annotation/VAR_084934|||http://purl.uniprot.org/annotation/VAR_084935|||http://purl.uniprot.org/annotation/VAR_084936|||http://purl.uniprot.org/annotation/VAR_084937|||http://purl.uniprot.org/annotation/VAR_084938|||http://purl.uniprot.org/annotation/VAR_084939|||http://purl.uniprot.org/annotation/VAR_084940|||http://purl.uniprot.org/annotation/VAR_084941|||http://purl.uniprot.org/annotation/VAR_084942|||http://purl.uniprot.org/annotation/VAR_084943|||http://purl.uniprot.org/annotation/VAR_084944|||http://purl.uniprot.org/annotation/VAR_084945|||http://purl.uniprot.org/annotation/VAR_084946|||http://purl.uniprot.org/annotation/VAR_084947|||http://purl.uniprot.org/annotation/VAR_084948|||http://purl.uniprot.org/annotation/VAR_084949|||http://purl.uniprot.org/annotation/VAR_084950|||http://purl.uniprot.org/annotation/VAR_084951|||http://purl.uniprot.org/annotation/VAR_084952|||http://purl.uniprot.org/annotation/VAR_084953|||http://purl.uniprot.org/annotation/VAR_084954|||http://purl.uniprot.org/annotation/VAR_084955|||http://purl.uniprot.org/annotation/VAR_084956|||http://purl.uniprot.org/annotation/VAR_084957|||http://purl.uniprot.org/annotation/VAR_084958|||http://purl.uniprot.org/annotation/VAR_084959|||http://purl.uniprot.org/annotation/VAR_084960|||http://purl.uniprot.org/annotation/VAR_084961|||http://purl.uniprot.org/annotation/VAR_084962|||http://purl.uniprot.org/annotation/VAR_084963|||http://purl.uniprot.org/annotation/VAR_084964|||http://purl.uniprot.org/annotation/VAR_085009|||http://purl.uniprot.org/annotation/VAR_085010|||http://purl.uniprot.org/annotation/VAR_085011|||http://purl.uniprot.org/annotation/VAR_085012|||http://purl.uniprot.org/annotation/VAR_085013|||http://purl.uniprot.org/annotation/VAR_085014|||http://purl.uniprot.org/annotation/VAR_085015|||http://purl.uniprot.org/annotation/VAR_085016|||http://purl.uniprot.org/annotation/VAR_085017|||http://purl.uniprot.org/annotation/VAR_085018|||http://purl.uniprot.org/annotation/VAR_085019|||http://purl.uniprot.org/annotation/VAR_085020|||http://purl.uniprot.org/annotation/VAR_085021|||http://purl.uniprot.org/annotation/VAR_085022|||http://purl.uniprot.org/annotation/VAR_085023|||http://purl.uniprot.org/annotation/VAR_085024|||http://purl.uniprot.org/annotation/VAR_085025|||http://purl.uniprot.org/annotation/VAR_085026|||http://purl.uniprot.org/annotation/VAR_085027|||http://purl.uniprot.org/annotation/VAR_085028
http://togogenome.org/gene/9606:RBM20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T481                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-1060; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1080 and A-1120.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1080 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1060; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-876; A-980; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-742; A-980; A-1060; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-685; A-876; A-980; A-1060; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-679; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-660; A-685; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210.|||In A10 mutant; does not affect nuclear localization; when associated with A-679; A-685; A-742; A-876; A-980; A-1060; A-1080; A-1120 and A-1210.|||In CMD1DD.|||In CMD1DD; also found in patients with left ventricular non-compaction.|||In CMD1DD; causes the formation of anomalous isoforms in TTN (Titin); impaired localization to the nucleus, leading to mislocalization to the cytoplasm.|||In CMD1DD; decreased stability; impaired mRNA splicing of target mRNAs.|||In CMD1DD; impaired localization to the nucleus, leading to mislocalization to the cytoplasm.|||In CMD1DD; impaired mRNA splicing of TTN (Titin) mRNA.|||In CMD1DD; impaired mRNA splicing of target mRNAs; does not affect nuclear localization.|||In CMD1DD; impaired splicing of target mRNAs, such as TTN, CAMK2D and CACNA1C; decreased localization to the nucleus associated with relocalization to P-body and stress granules.|||In CMD1DD; unknown pathological significance.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-1060, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1080 and D-1120.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1080 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1060, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-876, D-980, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-742, D-980, D-1060, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-685, D-876, D-980, D-1060, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-679, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-660, D-685, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210.|||In D10 mutant; mimics phosphorylation; does not prevent nuclear localization but induces increased localization to cytoplasmic ribonucleoprotein granules; when associated with D-679, D-685, D-742, D-876, D-980, D-1060, D-1080, D-1120 and D-1210.|||Matrin-type|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding protein 20|||RRM|||RS|||U1-type ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328824|||http://purl.uniprot.org/annotation/VAR_042532|||http://purl.uniprot.org/annotation/VAR_042533|||http://purl.uniprot.org/annotation/VAR_063092|||http://purl.uniprot.org/annotation/VAR_063093|||http://purl.uniprot.org/annotation/VAR_063094|||http://purl.uniprot.org/annotation/VAR_063095|||http://purl.uniprot.org/annotation/VAR_063096|||http://purl.uniprot.org/annotation/VAR_068802|||http://purl.uniprot.org/annotation/VAR_068803|||http://purl.uniprot.org/annotation/VAR_068804|||http://purl.uniprot.org/annotation/VAR_068805|||http://purl.uniprot.org/annotation/VAR_068806|||http://purl.uniprot.org/annotation/VAR_086515|||http://purl.uniprot.org/annotation/VAR_086516|||http://purl.uniprot.org/annotation/VAR_086517|||http://purl.uniprot.org/annotation/VAR_086518|||http://purl.uniprot.org/annotation/VAR_086519|||http://purl.uniprot.org/annotation/VAR_086520|||http://purl.uniprot.org/annotation/VAR_086521|||http://purl.uniprot.org/annotation/VAR_086522|||http://purl.uniprot.org/annotation/VAR_086523|||http://purl.uniprot.org/annotation/VAR_086524|||http://purl.uniprot.org/annotation/VAR_086525|||http://purl.uniprot.org/annotation/VAR_086526|||http://purl.uniprot.org/annotation/VAR_086527|||http://purl.uniprot.org/annotation/VAR_086528|||http://purl.uniprot.org/annotation/VAR_086529|||http://purl.uniprot.org/annotation/VAR_086530|||http://purl.uniprot.org/annotation/VAR_086531|||http://purl.uniprot.org/annotation/VAR_086532|||http://purl.uniprot.org/annotation/VAR_086533
http://togogenome.org/gene/9606:SMIM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58511                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079517|||http://purl.uniprot.org/annotation/VAR_054066
http://togogenome.org/gene/9606:GIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09681                                                                                  ^@                                                                                  Helix|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Helix|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Gastric inhibitory polypeptide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011214|||http://purl.uniprot.org/annotation/PRO_0000011215|||http://purl.uniprot.org/annotation/PRO_0000011216|||http://purl.uniprot.org/annotation/VAR_021897|||http://purl.uniprot.org/annotation/VAR_033973
http://togogenome.org/gene/9606:COQ8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D53                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AAAS motif|||Atypical kinase COQ8B, mitochondrial|||Basic and acidic residues|||Disordered|||Helical|||In NPHS9.|||In isoform 2.|||KxGQ motif|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271797|||http://purl.uniprot.org/annotation/VAR_029995|||http://purl.uniprot.org/annotation/VAR_041420|||http://purl.uniprot.org/annotation/VAR_041421|||http://purl.uniprot.org/annotation/VAR_041422|||http://purl.uniprot.org/annotation/VAR_041423|||http://purl.uniprot.org/annotation/VAR_070552|||http://purl.uniprot.org/annotation/VAR_070553|||http://purl.uniprot.org/annotation/VAR_070554|||http://purl.uniprot.org/annotation/VAR_070555|||http://purl.uniprot.org/annotation/VAR_070556|||http://purl.uniprot.org/annotation/VAR_076861|||http://purl.uniprot.org/annotation/VAR_076862|||http://purl.uniprot.org/annotation/VAR_076863|||http://purl.uniprot.org/annotation/VSP_022357
http://togogenome.org/gene/9606:FABP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFH5                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  Fatty acid-binding protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342881
http://togogenome.org/gene/9606:PLK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00444                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to phosphorylate CDC25C and CHEK2.|||Activating mutant.|||Basic and acidic residues|||Catalytically inactive mutant that causes some centrosome amplification above background levels when overexpressed.|||Cryptic POLO box 1 (CPB1)|||Cryptic POLO box 2 (CPB2)|||Decreases substantially the interaction with TENT5C. Does not affect localization to the centrosome. Loss of TENT5C recruitment to the centrosome.|||Disordered|||Does not affect the interaction with TENT5C.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||POLO box|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PLK4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086567|||http://purl.uniprot.org/annotation/VAR_019632|||http://purl.uniprot.org/annotation/VAR_041027|||http://purl.uniprot.org/annotation/VAR_041028|||http://purl.uniprot.org/annotation/VAR_041029|||http://purl.uniprot.org/annotation/VAR_041030|||http://purl.uniprot.org/annotation/VAR_041031|||http://purl.uniprot.org/annotation/VAR_041032|||http://purl.uniprot.org/annotation/VAR_041033|||http://purl.uniprot.org/annotation/VSP_038116|||http://purl.uniprot.org/annotation/VSP_038117
http://togogenome.org/gene/9606:MICU3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XE3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcium uptake protein 3, mitochondrial|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251230
http://togogenome.org/gene/9606:SHISA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DD7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Protein shisa-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254090|||http://purl.uniprot.org/annotation/VAR_028811
http://togogenome.org/gene/9606:TEX47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBZ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Testis-expressed protein 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321827|||http://purl.uniprot.org/annotation/VAR_039351|||http://purl.uniprot.org/annotation/VAR_039352|||http://purl.uniprot.org/annotation/VAR_039353|||http://purl.uniprot.org/annotation/VAR_039354|||http://purl.uniprot.org/annotation/VAR_039355
http://togogenome.org/gene/9606:RAB25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57735                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Ras-related protein Rab-25|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121215|||http://purl.uniprot.org/annotation/PRO_0000370821
http://togogenome.org/gene/9606:PWWP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PWWP|||PWWP domain-containing protein 2B|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240878|||http://purl.uniprot.org/annotation/VAR_037233|||http://purl.uniprot.org/annotation/VAR_037234|||http://purl.uniprot.org/annotation/VSP_054223|||http://purl.uniprot.org/annotation/VSP_054224
http://togogenome.org/gene/9606:NFKBIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRT5|||http://purl.uniprot.org/uniprot/A8K778|||http://purl.uniprot.org/uniprot/Q5STV6|||http://purl.uniprot.org/uniprot/Q9UBC1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||NF-kappa-B inhibitor-like protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067009|||http://purl.uniprot.org/annotation/VAR_017798|||http://purl.uniprot.org/annotation/VSP_041075|||http://purl.uniprot.org/annotation/VSP_046261
http://togogenome.org/gene/9606:UBE2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVK1|||http://purl.uniprot.org/uniprot/A0A0A0MSE8|||http://purl.uniprot.org/uniprot/O00762|||http://purl.uniprot.org/uniprot/Q5TZN3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of function; inhibition of cyclin-B degradation.|||N-acetylalanine|||Phosphoserine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082560|||http://purl.uniprot.org/annotation/VAR_007694|||http://purl.uniprot.org/annotation/VSP_045647|||http://purl.uniprot.org/annotation/VSP_045648|||http://purl.uniprot.org/annotation/VSP_045649
http://togogenome.org/gene/9606:DNAAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN4|||http://purl.uniprot.org/uniprot/Q8NEP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dynein axonemal assembly factor 1|||In CILD13.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232889|||http://purl.uniprot.org/annotation/VAR_047662|||http://purl.uniprot.org/annotation/VAR_047663|||http://purl.uniprot.org/annotation/VAR_047664|||http://purl.uniprot.org/annotation/VAR_047665|||http://purl.uniprot.org/annotation/VAR_047666|||http://purl.uniprot.org/annotation/VAR_047667|||http://purl.uniprot.org/annotation/VAR_047668|||http://purl.uniprot.org/annotation/VAR_047669|||http://purl.uniprot.org/annotation/VAR_047670|||http://purl.uniprot.org/annotation/VAR_047671|||http://purl.uniprot.org/annotation/VAR_047672|||http://purl.uniprot.org/annotation/VAR_063097|||http://purl.uniprot.org/annotation/VAR_063098|||http://purl.uniprot.org/annotation/VSP_036354|||http://purl.uniprot.org/annotation/VSP_036355|||http://purl.uniprot.org/annotation/VSP_036356
http://togogenome.org/gene/9606:BMP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUF7|||http://purl.uniprot.org/uniprot/P22004|||http://purl.uniprot.org/uniprot/Q4VBA3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein 6|||Disordered|||In IO; associated with disease susceptibility.|||In IO; associated with disease susceptibility; results in decreased activation of hepcidin expression in cultured liver cells.|||In IO; associated with disease susceptibility; some patients also carry a HFE variant; decreased function in positive regulation of SMAD protein signal transduction; results in partial activation of hepcidin expression; affects post-translational processing resulting in reduced amount of the mature form; results in impaired secretion.|||In a colorectal cancer sample; somatic mutation.|||Interchain|||N-linked (GlcNAc...) asparagine|||Polar residues|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033870|||http://purl.uniprot.org/annotation/PRO_0000033871|||http://purl.uniprot.org/annotation/VAR_036200|||http://purl.uniprot.org/annotation/VAR_036201|||http://purl.uniprot.org/annotation/VAR_047055|||http://purl.uniprot.org/annotation/VAR_087884|||http://purl.uniprot.org/annotation/VAR_087885|||http://purl.uniprot.org/annotation/VAR_087886|||http://purl.uniprot.org/annotation/VAR_087887|||http://purl.uniprot.org/annotation/VAR_087888|||http://purl.uniprot.org/annotation/VAR_087889|||http://purl.uniprot.org/annotation/VAR_087890
http://togogenome.org/gene/9606:KLHL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ60                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119106|||http://purl.uniprot.org/annotation/VAR_056125
http://togogenome.org/gene/9606:SPDYE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6XC90|||http://purl.uniprot.org/uniprot/Q495Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Speedy protein E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332292|||http://purl.uniprot.org/annotation/VSP_039851
http://togogenome.org/gene/9606:COPS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5H7|||http://purl.uniprot.org/uniprot/B3KM48|||http://purl.uniprot.org/uniprot/D6RAX7|||http://purl.uniprot.org/uniprot/Q9BT78                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  COP9 signalosome complex subunit 4|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||PCI|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120987|||http://purl.uniprot.org/annotation/VSP_046336
http://togogenome.org/gene/9606:NIPSNAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75323                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein NipSnap homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221148|||http://purl.uniprot.org/annotation/VSP_044708
http://togogenome.org/gene/9606:INS-IGF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WCM5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Insulin, isoform 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422829
http://togogenome.org/gene/9606:KCTD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXV2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD5|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191291
http://togogenome.org/gene/9606:ZNF100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYN0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 100                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047405|||http://purl.uniprot.org/annotation/VAR_057395|||http://purl.uniprot.org/annotation/VAR_060422
http://togogenome.org/gene/9606:IL12RB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIX0|||http://purl.uniprot.org/uniprot/B4DGA4|||http://purl.uniprot.org/uniprot/B7ZB60|||http://purl.uniprot.org/uniprot/Q99665                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes in vitro STAT4 binding to a phosphorylated Y-800 peptide.|||Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||In isoform 2.|||In isoform 3.|||Interleukin-12 receptor subunit beta-2|||Loss of STAT4 activation. Abolishes SOCS3 binding.|||N-linked (GlcNAc...) asparagine|||No effect on in vitro STAT4 binding to a phosphorylated Y-800 peptide.|||No loss of STAT4 activation. No loss of SOCS3 binding.|||Phosphotyrosine|||Required for STAT4 binding|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010920|||http://purl.uniprot.org/annotation/PRO_5002803262|||http://purl.uniprot.org/annotation/PRO_5002866305|||http://purl.uniprot.org/annotation/PRO_5040043817|||http://purl.uniprot.org/annotation/VAR_014805|||http://purl.uniprot.org/annotation/VAR_014806|||http://purl.uniprot.org/annotation/VAR_014807|||http://purl.uniprot.org/annotation/VAR_014808|||http://purl.uniprot.org/annotation/VAR_016097|||http://purl.uniprot.org/annotation/VAR_019525|||http://purl.uniprot.org/annotation/VAR_019526|||http://purl.uniprot.org/annotation/VAR_019527|||http://purl.uniprot.org/annotation/VAR_021278|||http://purl.uniprot.org/annotation/VAR_021279|||http://purl.uniprot.org/annotation/VAR_021280|||http://purl.uniprot.org/annotation/VAR_049169|||http://purl.uniprot.org/annotation/VSP_011112|||http://purl.uniprot.org/annotation/VSP_011113|||http://purl.uniprot.org/annotation/VSP_044784
http://togogenome.org/gene/9606:KRTAP25-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LHN0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 25-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308251|||http://purl.uniprot.org/annotation/VAR_060063
http://togogenome.org/gene/9606:RP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B2JLU2|||http://purl.uniprot.org/uniprot/O75695                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-CAP/cofactor C-like|||Disordered|||Does not reduce affinity for mouse ARL3; when associated with A-31.|||Does not reduce affinity for mouse ARL3; when associated with A-32.|||In RP2.|||In RP2; loss of membrane association; enhances interaction with ARL3.|||In RP2; reduces affinity for ARL3 150-fold and inhibits the GTP-hydrolysis rate of ARL3.|||In RP2; reduces affinity for ARL3 800-fold; loss of stimulation of tubulin GTPase activity; no effect on subcellular location.|||In RP2; uncertain pathological significance.|||Loss of membrane association.|||N-myristoyl glycine|||Protein XRP2|||Reduces affinity and GTP-hydrolysis rate for mouse ARL3.|||Reduces affinity for ARL3 3-fold.|||Reduces affinity for mouse ARL3.|||Reduces affinity for mouse ARL3; when associated with A-28.|||Reduces affinity for mouse ARL3; when associated with A-29.|||Reduces affinity for mouse ARL3; when associated with H-120.|||Reduces affinity for mouse ARL3; when associated with S-121.|||Removed|||S-palmitoyl cysteine|||Targeting to internal membranes. Loss of targeting to the plasma membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080047|||http://purl.uniprot.org/annotation/VAR_008497|||http://purl.uniprot.org/annotation/VAR_008498|||http://purl.uniprot.org/annotation/VAR_008499|||http://purl.uniprot.org/annotation/VAR_008500|||http://purl.uniprot.org/annotation/VAR_014535|||http://purl.uniprot.org/annotation/VAR_014536|||http://purl.uniprot.org/annotation/VAR_018069|||http://purl.uniprot.org/annotation/VAR_018070|||http://purl.uniprot.org/annotation/VAR_018071|||http://purl.uniprot.org/annotation/VAR_018072|||http://purl.uniprot.org/annotation/VAR_018073|||http://purl.uniprot.org/annotation/VAR_018074|||http://purl.uniprot.org/annotation/VAR_018075|||http://purl.uniprot.org/annotation/VAR_026058|||http://purl.uniprot.org/annotation/VAR_053961|||http://purl.uniprot.org/annotation/VAR_068353
http://togogenome.org/gene/9606:AGAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VW22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 6|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2.|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284674|||http://purl.uniprot.org/annotation/VSP_040815
http://togogenome.org/gene/9606:FAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CS3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FAS-associated factor 2|||N-acetylalanine|||N6-acetyllysine|||Removed|||UBA|||UBX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244064
http://togogenome.org/gene/9606:OR5M11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVL9|||http://purl.uniprot.org/uniprot/Q96RB7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150609|||http://purl.uniprot.org/annotation/VAR_034231|||http://purl.uniprot.org/annotation/VAR_034232
http://togogenome.org/gene/9606:LGMN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53XC6|||http://purl.uniprot.org/uniprot/Q96CY7|||http://purl.uniprot.org/uniprot/Q99538                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||In isoform 2.|||In isoform 3.|||Increases catalytic activity at pH 5.5.|||Legumain|||Loss of autoactivation.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026502|||http://purl.uniprot.org/annotation/PRO_0000026503|||http://purl.uniprot.org/annotation/PRO_5014309527|||http://purl.uniprot.org/annotation/VAR_024588|||http://purl.uniprot.org/annotation/VSP_056454|||http://purl.uniprot.org/annotation/VSP_056455|||http://purl.uniprot.org/annotation/VSP_056456
http://togogenome.org/gene/9606:PCDHB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN66                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003928|||http://purl.uniprot.org/annotation/VAR_021880|||http://purl.uniprot.org/annotation/VAR_024392|||http://purl.uniprot.org/annotation/VAR_024393|||http://purl.uniprot.org/annotation/VAR_031619|||http://purl.uniprot.org/annotation/VAR_031620|||http://purl.uniprot.org/annotation/VAR_055581|||http://purl.uniprot.org/annotation/VAR_055582|||http://purl.uniprot.org/annotation/VAR_055583|||http://purl.uniprot.org/annotation/VAR_055584|||http://purl.uniprot.org/annotation/VAR_055585|||http://purl.uniprot.org/annotation/VAR_055586
http://togogenome.org/gene/9606:OTOF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC10                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AUNB1 and DFNB9.|||In AUNB1.|||In DFNB9 and AUNB1; temperature sensitive AUNB1 phenotype with severe hearing loss during febrile illness.|||In DFNB9.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 2 and isoform 5.|||In isoform 3.|||Otoferlin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057881|||http://purl.uniprot.org/annotation/VAR_028028|||http://purl.uniprot.org/annotation/VAR_028029|||http://purl.uniprot.org/annotation/VAR_028030|||http://purl.uniprot.org/annotation/VAR_032226|||http://purl.uniprot.org/annotation/VAR_032227|||http://purl.uniprot.org/annotation/VAR_032228|||http://purl.uniprot.org/annotation/VAR_032229|||http://purl.uniprot.org/annotation/VAR_032230|||http://purl.uniprot.org/annotation/VAR_032231|||http://purl.uniprot.org/annotation/VAR_032232|||http://purl.uniprot.org/annotation/VAR_032233|||http://purl.uniprot.org/annotation/VAR_032234|||http://purl.uniprot.org/annotation/VAR_032235|||http://purl.uniprot.org/annotation/VAR_032236|||http://purl.uniprot.org/annotation/VAR_032237|||http://purl.uniprot.org/annotation/VAR_032238|||http://purl.uniprot.org/annotation/VAR_032239|||http://purl.uniprot.org/annotation/VAR_032240|||http://purl.uniprot.org/annotation/VAR_032241|||http://purl.uniprot.org/annotation/VAR_032242|||http://purl.uniprot.org/annotation/VAR_035895|||http://purl.uniprot.org/annotation/VAR_035896|||http://purl.uniprot.org/annotation/VAR_046003|||http://purl.uniprot.org/annotation/VAR_046004|||http://purl.uniprot.org/annotation/VAR_046005|||http://purl.uniprot.org/annotation/VAR_046006|||http://purl.uniprot.org/annotation/VAR_046007|||http://purl.uniprot.org/annotation/VAR_046008|||http://purl.uniprot.org/annotation/VAR_049057|||http://purl.uniprot.org/annotation/VSP_001507|||http://purl.uniprot.org/annotation/VSP_001508|||http://purl.uniprot.org/annotation/VSP_001509|||http://purl.uniprot.org/annotation/VSP_001510|||http://purl.uniprot.org/annotation/VSP_001511
http://togogenome.org/gene/9606:TG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01266                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes thyroxine (T4) production.|||Abolishes thyroxine (T4) production; when associated with F-1310, F-2573 and F-2766.|||Abolishes thyroxine (T4) production; when associated with F-24, F-1310 and F-2573.|||Abolishes thyroxine (T4) production; when associated with F-24, F-1310 and F-2766.|||Abolishes thyroxine (T4) production; when associated with F-24, F-2573 and F-2766.|||Associated with AITD3.|||Benign variant.|||Cholinesterase-like (ChEL)|||Diiodotyrosine|||Diiodotyrosine; alternate|||Disordered|||In AITD3; unknown pathological significance.|||In TDH3.|||In TDH3; autosomal recessive.|||In TDH3; reduces thyroglobulin synthesis and secretion; promotes thyroglobulin retention within the endoplasmic reticulum.|||In TDH3; unknown pathological significance.|||In isoform 2.|||Iodotyrosine|||Iodotyrosine; alternate|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Requires 2 nucleotide substitutions.|||Severe loss of thyroxine (T4) production; when associated with F-108, F-2540 and F-2766. Abolishes thyroxine (T4) production; when associated with F-108, F-149, F-2540 and F-2766.|||Severe loss of thyroxine (T4) production; when associated with F-108, F-2540 and F-2766. Abolishes thyroxine (T4) production; when associated with F-108, F-234, F-2540 and F-2766.|||Severe loss of thyroxine (T4) production; when associated with F-149 or F-234, and F-108 and F-2540. Abolishes thyroxine (T4) production; when associated with F-108, F-149, F-234 and F-2540.|||Severe loss of thyroxine (T4) production; when associated with F-149 or F-234, and F-108 and F-2766. Abolishes thyroxine (T4) production; when associated with F-108, F-149, F-234 and F-2766.|||Severe loss of thyroxine (T4) production; when associated with F-149 or F-234, and F-2540 and F-2766. Abolishes thyroxine (T4) production; when associated with F-149, F-234, F-2540 and F-2766.|||Sulfotyrosine; alternate|||Thyroglobulin|||Thyroglobulin type-1 1|||Thyroglobulin type-1 10|||Thyroglobulin type-1 11|||Thyroglobulin type-1 2|||Thyroglobulin type-1 3|||Thyroglobulin type-1 4|||Thyroglobulin type-1 5|||Thyroglobulin type-1 6|||Thyroglobulin type-1 7|||Thyroglobulin type-1 8|||Thyroglobulin type-1 9|||Thyroxine|||Thyroxine; alternate|||Triiodothyronine; alternate|||Type II|||Type IIIA|||Type IIIB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008636|||http://purl.uniprot.org/annotation/VAR_002365|||http://purl.uniprot.org/annotation/VAR_010212|||http://purl.uniprot.org/annotation/VAR_010213|||http://purl.uniprot.org/annotation/VAR_010214|||http://purl.uniprot.org/annotation/VAR_010215|||http://purl.uniprot.org/annotation/VAR_010216|||http://purl.uniprot.org/annotation/VAR_010217|||http://purl.uniprot.org/annotation/VAR_010218|||http://purl.uniprot.org/annotation/VAR_010219|||http://purl.uniprot.org/annotation/VAR_010220|||http://purl.uniprot.org/annotation/VAR_010221|||http://purl.uniprot.org/annotation/VAR_010222|||http://purl.uniprot.org/annotation/VAR_016190|||http://purl.uniprot.org/annotation/VAR_016852|||http://purl.uniprot.org/annotation/VAR_016853|||http://purl.uniprot.org/annotation/VAR_016854|||http://purl.uniprot.org/annotation/VAR_016855|||http://purl.uniprot.org/annotation/VAR_016856|||http://purl.uniprot.org/annotation/VAR_016857|||http://purl.uniprot.org/annotation/VAR_016858|||http://purl.uniprot.org/annotation/VAR_016859|||http://purl.uniprot.org/annotation/VAR_016860|||http://purl.uniprot.org/annotation/VAR_016861|||http://purl.uniprot.org/annotation/VAR_016862|||http://purl.uniprot.org/annotation/VAR_016863|||http://purl.uniprot.org/annotation/VAR_049077|||http://purl.uniprot.org/annotation/VAR_049078|||http://purl.uniprot.org/annotation/VAR_049079|||http://purl.uniprot.org/annotation/VAR_049080|||http://purl.uniprot.org/annotation/VAR_049081|||http://purl.uniprot.org/annotation/VAR_049082|||http://purl.uniprot.org/annotation/VAR_049083|||http://purl.uniprot.org/annotation/VAR_049084|||http://purl.uniprot.org/annotation/VAR_049085|||http://purl.uniprot.org/annotation/VAR_049086|||http://purl.uniprot.org/annotation/VAR_061173|||http://purl.uniprot.org/annotation/VAR_063034|||http://purl.uniprot.org/annotation/VAR_063035|||http://purl.uniprot.org/annotation/VAR_063036|||http://purl.uniprot.org/annotation/VAR_063037|||http://purl.uniprot.org/annotation/VAR_063038|||http://purl.uniprot.org/annotation/VAR_078338|||http://purl.uniprot.org/annotation/VSP_012655
http://togogenome.org/gene/9606:MBOAT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N66                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In MRT57.|||In isoform 2.|||In isoform 3.|||Lumenal|||Lysophospholipid acyltransferase 7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317457|||http://purl.uniprot.org/annotation/VAR_038526|||http://purl.uniprot.org/annotation/VAR_038527|||http://purl.uniprot.org/annotation/VAR_078044|||http://purl.uniprot.org/annotation/VSP_030967|||http://purl.uniprot.org/annotation/VSP_030968
http://togogenome.org/gene/9606:RNASE11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GAN5|||http://purl.uniprot.org/uniprot/Q8TAA1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Probable ribonuclease 11|||Proton acceptor|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030908|||http://purl.uniprot.org/annotation/PRO_5014309809|||http://purl.uniprot.org/annotation/VAR_052195|||http://purl.uniprot.org/annotation/VAR_052196
http://togogenome.org/gene/9606:ATP6V1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16864                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||V-type proton ATPase subunit F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144799|||http://purl.uniprot.org/annotation/VAR_048348|||http://purl.uniprot.org/annotation/VSP_045952
http://togogenome.org/gene/9606:PDE4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07343|||http://purl.uniprot.org/uniprot/Q59GM8|||http://purl.uniprot.org/uniprot/Q68CX5|||http://purl.uniprot.org/uniprot/X5DNX5|||http://purl.uniprot.org/uniprot/X5DR82                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Changes substrate selectivity from cAMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with A-567 and Q-575.|||Changes substrate selectivity from cAMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with A-567 and W-652.|||Changes substrate selectivity from cAMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with Q-575 and W-652.|||Disordered|||In isoform PDE4B2.|||In isoform PDE4B3.|||In isoform PDE4B5.|||Increases substrate selectivity for cGMP.|||PDEase|||Phosphoserine|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198809|||http://purl.uniprot.org/annotation/VAR_034373|||http://purl.uniprot.org/annotation/VSP_004571|||http://purl.uniprot.org/annotation/VSP_004572|||http://purl.uniprot.org/annotation/VSP_047723|||http://purl.uniprot.org/annotation/VSP_047724
http://togogenome.org/gene/9606:GPR33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D8VER1|||http://purl.uniprot.org/uniprot/Q49SQ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069553|||http://purl.uniprot.org/annotation/VAR_088064
http://togogenome.org/gene/9606:CTCFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XGM0|||http://purl.uniprot.org/uniprot/A6XGM9|||http://purl.uniprot.org/uniprot/Q8NI51|||http://purl.uniprot.org/uniprot/V9GY73|||http://purl.uniprot.org/uniprot/V9GYX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 11.|||In isoform 2.|||In isoform 3, isoform 6 and isoform 10.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5 and isoform 10.|||In isoform 6 and isoform 11.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Transcriptional repressor CTCFL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047226|||http://purl.uniprot.org/annotation/VAR_023213|||http://purl.uniprot.org/annotation/VAR_023214|||http://purl.uniprot.org/annotation/VAR_032766|||http://purl.uniprot.org/annotation/VAR_057374|||http://purl.uniprot.org/annotation/VSP_045155|||http://purl.uniprot.org/annotation/VSP_045156|||http://purl.uniprot.org/annotation/VSP_045157|||http://purl.uniprot.org/annotation/VSP_045158|||http://purl.uniprot.org/annotation/VSP_045159|||http://purl.uniprot.org/annotation/VSP_045160|||http://purl.uniprot.org/annotation/VSP_047058|||http://purl.uniprot.org/annotation/VSP_047059|||http://purl.uniprot.org/annotation/VSP_047725|||http://purl.uniprot.org/annotation/VSP_047726|||http://purl.uniprot.org/annotation/VSP_054899
http://togogenome.org/gene/9606:TSHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTJ0|||http://purl.uniprot.org/uniprot/P16473                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cell surface expression.|||Abolishes sulfation. Inhibits intracellular cAMP accumulation.|||Cytoplasmic|||Does not contribute to the genetic susceptibility to Graves disease.|||Extracellular|||Found in toxic thyroid nodules.|||Found in toxic thyroid nodules; 5 times higher levels of basal cAMP than wild-type TSHR and slightly less response to maximal TSH stimulation.|||Found in toxic thyroid nodules; 8 to 9 times higher levels of basal cAMP than wild-type TSHR and similar response to maximal TSH stimulation.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CHNG1.|||In CHNG1; abolishes cell membrane location; abolishes adenylate cyclase-activating G-protein coupled receptor signaling pathway; abolishes phospholipase C-activating G-protein coupled receptor signaling pathway.|||In CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production.|||In CHNG1; impairs adenylate cyclase activation.|||In CHNG1; lack of adenylate cyclase activation.|||In CHNG1; no effect on cell membrane location; upon TSH stimulation decreases more phospholipase C-activating G-protein coupled receptor signaling pathway than adenylate cyclase-activating G-protein coupled receptor signaling pathway.|||In CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding.|||In CHNG1; severe hypothyroidism.|||In HTFG; enhances receptor response to chorionic gonadotropin.|||In HTNA; 11-fold increase in specific constitutive activity associated with reduction in receptor protein expression.|||In HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules.|||In HTNA; found in hyperfunctioning thyroid adenomas.|||In HTNA; found in non-adenomatous hyperfunctioning nodules.|||In HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas.|||In HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma.|||In HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules.|||In HTNA; found in toxic thyroid nodules.|||In HTNA; gain of function.|||In HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system.|||In HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas.|||In HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas.|||In HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas.|||In a patient with Graves disease.|||In hyperthyroidism; associated with autonomously functioning thyroid nodules; 3.3-fold increase in basal cAMP level.|||In hyperthyroidism; associated with hyperfunctioning thyroid adenomas.|||In hyperthyroidism; associated with hyperfunctioning thyroid adenomas; gain of function; requires 2 nucleotide substitutions.|||In hyperthyroidism; congenital with severe thyrotoxicosis.|||In hyperthyroidism; congenital; due to a toxic adenoma.|||In hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas.|||In hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas; also in hyperfunctioning insular carcinoma; with severe thyrotoxicosis; gain of function.|||In hyperthyroidism; found in toxic thyroid nodules; associated with hyperfunctioning thyroid adenomas; gain of function.|||In isoform 3.|||In isoform Short.|||In papillary cancer.|||In thyroid carcinoma; with thyrotoxicosis; gain of function.|||In toxic thyroid adenoma; requires 2 nucleotide substitutions; somatic mutation; constitutively activates the cAMP cascade.|||Inhibits intracellular cAMP accumulation.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||May be a predisposing factor in toxic multinodular goiter pathogenesis; activation of the cAMP cascade does not differ from the wild-type.|||N-linked (GlcNAc...) asparagine|||No change in intracellular cAMP accumulation.|||PDZ-binding|||Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation.|||Reduces sulfation. No change in intracellular cAMP accumulation.|||Reduces sulfation. Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation.|||Sulfotyrosine|||Thyrotropin receptor ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012786|||http://purl.uniprot.org/annotation/PRO_5013980011|||http://purl.uniprot.org/annotation/VAR_003564|||http://purl.uniprot.org/annotation/VAR_003565|||http://purl.uniprot.org/annotation/VAR_003566|||http://purl.uniprot.org/annotation/VAR_003567|||http://purl.uniprot.org/annotation/VAR_003568|||http://purl.uniprot.org/annotation/VAR_003569|||http://purl.uniprot.org/annotation/VAR_003570|||http://purl.uniprot.org/annotation/VAR_003571|||http://purl.uniprot.org/annotation/VAR_003572|||http://purl.uniprot.org/annotation/VAR_003573|||http://purl.uniprot.org/annotation/VAR_003574|||http://purl.uniprot.org/annotation/VAR_003575|||http://purl.uniprot.org/annotation/VAR_003576|||http://purl.uniprot.org/annotation/VAR_003577|||http://purl.uniprot.org/annotation/VAR_003578|||http://purl.uniprot.org/annotation/VAR_011519|||http://purl.uniprot.org/annotation/VAR_011520|||http://purl.uniprot.org/annotation/VAR_011521|||http://purl.uniprot.org/annotation/VAR_011522|||http://purl.uniprot.org/annotation/VAR_011523|||http://purl.uniprot.org/annotation/VAR_011524|||http://purl.uniprot.org/annotation/VAR_011525|||http://purl.uniprot.org/annotation/VAR_011526|||http://purl.uniprot.org/annotation/VAR_011527|||http://purl.uniprot.org/annotation/VAR_011528|||http://purl.uniprot.org/annotation/VAR_011529|||http://purl.uniprot.org/annotation/VAR_011530|||http://purl.uniprot.org/annotation/VAR_011531|||http://purl.uniprot.org/annotation/VAR_011532|||http://purl.uniprot.org/annotation/VAR_011533|||http://purl.uniprot.org/annotation/VAR_011534|||http://purl.uniprot.org/annotation/VAR_011535|||http://purl.uniprot.org/annotation/VAR_011536|||http://purl.uniprot.org/annotation/VAR_011537|||http://purl.uniprot.org/annotation/VAR_011538|||http://purl.uniprot.org/annotation/VAR_011539|||http://purl.uniprot.org/annotation/VAR_011540|||http://purl.uniprot.org/annotation/VAR_011541|||http://purl.uniprot.org/annotation/VAR_011542|||http://purl.uniprot.org/annotation/VAR_011543|||http://purl.uniprot.org/annotation/VAR_011544|||http://purl.uniprot.org/annotation/VAR_011545|||http://purl.uniprot.org/annotation/VAR_011546|||http://purl.uniprot.org/annotation/VAR_011547|||http://purl.uniprot.org/annotation/VAR_011548|||http://purl.uniprot.org/annotation/VAR_011549|||http://purl.uniprot.org/annotation/VAR_011550|||http://purl.uniprot.org/annotation/VAR_011551|||http://purl.uniprot.org/annotation/VAR_011552|||http://purl.uniprot.org/annotation/VAR_011553|||http://purl.uniprot.org/annotation/VAR_011554|||http://purl.uniprot.org/annotation/VAR_011555|||http://purl.uniprot.org/annotation/VAR_011556|||http://purl.uniprot.org/annotation/VAR_011557|||http://purl.uniprot.org/annotation/VAR_011558|||http://purl.uniprot.org/annotation/VAR_011559|||http://purl.uniprot.org/annotation/VAR_011560|||http://purl.uniprot.org/annotation/VAR_017295|||http://purl.uniprot.org/annotation/VAR_017296|||http://purl.uniprot.org/annotation/VAR_017297|||http://purl.uniprot.org/annotation/VAR_021495|||http://purl.uniprot.org/annotation/VAR_021496|||http://purl.uniprot.org/annotation/VAR_021497|||http://purl.uniprot.org/annotation/VAR_021498|||http://purl.uniprot.org/annotation/VAR_021499|||http://purl.uniprot.org/annotation/VAR_021500|||http://purl.uniprot.org/annotation/VAR_021501|||http://purl.uniprot.org/annotation/VAR_055925|||http://purl.uniprot.org/annotation/VAR_075585|||http://purl.uniprot.org/annotation/VAR_075586|||http://purl.uniprot.org/annotation/VSP_001981|||http://purl.uniprot.org/annotation/VSP_001982|||http://purl.uniprot.org/annotation/VSP_044643|||http://purl.uniprot.org/annotation/VSP_044644
http://togogenome.org/gene/9606:NT5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCD5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'(3')-deoxyribonucleotidase, cytosolic type|||In isoform 2.|||Nucleophile|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164371|||http://purl.uniprot.org/annotation/VAR_048102|||http://purl.uniprot.org/annotation/VSP_008710|||http://purl.uniprot.org/annotation/VSP_008711|||http://purl.uniprot.org/annotation/VSP_008712
http://togogenome.org/gene/9606:ANKRD16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P6B7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 16|||In isoform 2.|||Required to capture Ser that is misactivated by AARS/AlaRS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240831|||http://purl.uniprot.org/annotation/VAR_026832|||http://purl.uniprot.org/annotation/VAR_033503|||http://purl.uniprot.org/annotation/VSP_047046|||http://purl.uniprot.org/annotation/VSP_047047
http://togogenome.org/gene/9606:CD8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01732|||http://purl.uniprot.org/uniprot/Q6ZVS2|||http://purl.uniprot.org/uniprot/Q8TAW8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Complete loss of palmitoylation.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||Immunoglobulin V-set|||In CD8 deficiency; prevents CD8 expression.|||In isoform 2.|||In isoform 3.|||Prevents CD8 expression.|||S-palmitoyl cysteine|||T-cell surface glycoprotein CD8 alpha chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014638|||http://purl.uniprot.org/annotation/PRO_5004313944|||http://purl.uniprot.org/annotation/VAR_021020|||http://purl.uniprot.org/annotation/VSP_012653|||http://purl.uniprot.org/annotation/VSP_054438
http://togogenome.org/gene/9606:ZC3H6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61129|||http://purl.uniprot.org/uniprot/Q6ZN12                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213901
http://togogenome.org/gene/9606:GTF2H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13889                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||General transcription factor IIH subunit 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119251|||http://purl.uniprot.org/annotation/VSP_055153
http://togogenome.org/gene/9606:SRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19623                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmethionine|||PABS|||Proton acceptor|||Spermidine synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156445|||http://purl.uniprot.org/annotation/VAR_011807
http://togogenome.org/gene/9606:COQ9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75208                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Abolishes interaction with COQ7.|||Disordered|||Impairs interaction with COQ7.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Polar residues|||Ubiquinone biosynthesis protein COQ9, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228637|||http://purl.uniprot.org/annotation/VSP_017683|||http://purl.uniprot.org/annotation/VSP_017684
http://togogenome.org/gene/9606:COA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTJ3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase assembly factor 6 homolog|||In MC4DN13.|||In MC4DN13; mistargeted to the mitochondrial matrix; loss of interaction with SCO2 and MT-CO2.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280399|||http://purl.uniprot.org/annotation/VAR_075046|||http://purl.uniprot.org/annotation/VAR_075047|||http://purl.uniprot.org/annotation/VSP_023655|||http://purl.uniprot.org/annotation/VSP_023656
http://togogenome.org/gene/9606:SEC61G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60059                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-acetylmethionine|||Phosphoserine|||Protein transport protein Sec61 subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000104195
http://togogenome.org/gene/9606:IFIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T7D6|||http://purl.uniprot.org/uniprot/O14879|||http://purl.uniprot.org/uniprot/Q5T765                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Disordered|||Interferon-induced protein with tetratricopeptide repeats 3|||Phosphoserine|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106349
http://togogenome.org/gene/9606:PATL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JE40|||http://purl.uniprot.org/uniprot/H0YMQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In OZEMA4.|||In OZEMA4; unknown pathological significance.|||Polar residues|||Protein PAT1 homolog 2|||mRNA decay factor PAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000404577|||http://purl.uniprot.org/annotation/VAR_064549|||http://purl.uniprot.org/annotation/VAR_080255|||http://purl.uniprot.org/annotation/VAR_080256|||http://purl.uniprot.org/annotation/VAR_080257|||http://purl.uniprot.org/annotation/VAR_080258|||http://purl.uniprot.org/annotation/VAR_080259|||http://purl.uniprot.org/annotation/VAR_080260|||http://purl.uniprot.org/annotation/VAR_080261|||http://purl.uniprot.org/annotation/VAR_080262
http://togogenome.org/gene/9606:ZNF584                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQS1|||http://purl.uniprot.org/uniprot/F6W0P0|||http://purl.uniprot.org/uniprot/Q8IVC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||KRAB|||Zinc finger protein 584                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047676|||http://purl.uniprot.org/annotation/VAR_033579|||http://purl.uniprot.org/annotation/VAR_033580
http://togogenome.org/gene/9606:SHANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9KV90|||http://purl.uniprot.org/uniprot/Q9Y566                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM|||SH3|||SH3 and multiple ankyrin repeat domains protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174671|||http://purl.uniprot.org/annotation/VAR_022123|||http://purl.uniprot.org/annotation/VAR_036541|||http://purl.uniprot.org/annotation/VAR_036542|||http://purl.uniprot.org/annotation/VAR_055318|||http://purl.uniprot.org/annotation/VSP_006069|||http://purl.uniprot.org/annotation/VSP_006070|||http://purl.uniprot.org/annotation/VSP_006071
http://togogenome.org/gene/9606:RBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28749                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Domain A|||Domain B|||In isoform 2.|||No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated with 657-A--A-660.|||No effect on phosphorylation by CDK2.|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by CDK2 and CDK4|||Phosphothreonine; by CDK2|||Phosphothreonine; by CDK4|||Pocket; binds T and E1A|||Reduces S-640 phosphorylation by CDK2 and CDK4.|||Retinoblastoma-like protein 1|||Spacer|||Strongly reduces phosphorylation by CDK2 and CDK4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167839|||http://purl.uniprot.org/annotation/VAR_034443|||http://purl.uniprot.org/annotation/VSP_017496
http://togogenome.org/gene/9606:PLA2G4F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PKZ7|||http://purl.uniprot.org/uniprot/Q68DD2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C2|||Cytosolic phospholipase A2 zeta|||In isoform 2.|||In isoform 3.|||Nucleophile|||PLA2c|||Phospholipase A2|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247027|||http://purl.uniprot.org/annotation/PRO_5002686184|||http://purl.uniprot.org/annotation/VAR_027054|||http://purl.uniprot.org/annotation/VAR_053553|||http://purl.uniprot.org/annotation/VSP_019887|||http://purl.uniprot.org/annotation/VSP_019888|||http://purl.uniprot.org/annotation/VSP_019889
http://togogenome.org/gene/9606:E2F5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15329                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  DEF box|||Dimerization|||Disordered|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Polar residues|||Pro residues|||RBL2 association|||Transactivation|||Transcription factor E2F5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219469|||http://purl.uniprot.org/annotation/VAR_014348|||http://purl.uniprot.org/annotation/VSP_040098|||http://purl.uniprot.org/annotation/VSP_044660
http://togogenome.org/gene/9606:C22orf39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5X5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||UPF0545 protein C22orf39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326130|||http://purl.uniprot.org/annotation/VSP_046502
http://togogenome.org/gene/9606:ADAMTS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76LX8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 13|||Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73.|||Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71.|||C-linked (Man) tryptophan|||CUB 1|||CUB 2|||Cell attachment site|||Cysteine-rich|||Disintegrin|||Disordered|||Does not affect protein secretion.|||Does not affect protein secretion; normal proteolytic activity.|||Dramatically reduced affinity for calcium.|||Found in a patient with hemolytic uremic syndrome.|||In TTP.|||In TTP; affects protein secretion.|||In TTP; affects protein secretion; the mutant protein has reduced protease activity.|||In TTP; impairs protein secretion and proteolytic activity.|||In TTP; impairs protein secretion.|||In TTP; impairs protein secretion; the mutant protein has reduced protease activity.|||In TTP; low activity.|||In TTP; mild effect on protein secretion; strong reduction of proteolytic activity.|||In TTP; reduces protein secretion and proteolytic activity.|||In a patient with thrombotic thrombocytopenic purpura.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No change in calcium dependence for proteolysis.|||No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-965.|||No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-399.|||No effect on cleavage of VWF and little change in secretion of ADAMTS13.|||No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1027.|||No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1087.|||No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-907.|||No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-698.|||O-linked (Fuc...) serine|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247510|||http://purl.uniprot.org/annotation/PRO_0000247511|||http://purl.uniprot.org/annotation/VAR_027109|||http://purl.uniprot.org/annotation/VAR_027110|||http://purl.uniprot.org/annotation/VAR_027111|||http://purl.uniprot.org/annotation/VAR_027112|||http://purl.uniprot.org/annotation/VAR_027113|||http://purl.uniprot.org/annotation/VAR_027114|||http://purl.uniprot.org/annotation/VAR_027115|||http://purl.uniprot.org/annotation/VAR_027116|||http://purl.uniprot.org/annotation/VAR_027117|||http://purl.uniprot.org/annotation/VAR_027118|||http://purl.uniprot.org/annotation/VAR_027119|||http://purl.uniprot.org/annotation/VAR_027120|||http://purl.uniprot.org/annotation/VAR_027121|||http://purl.uniprot.org/annotation/VAR_027122|||http://purl.uniprot.org/annotation/VAR_027123|||http://purl.uniprot.org/annotation/VAR_027124|||http://purl.uniprot.org/annotation/VAR_027125|||http://purl.uniprot.org/annotation/VAR_027126|||http://purl.uniprot.org/annotation/VAR_027127|||http://purl.uniprot.org/annotation/VAR_027128|||http://purl.uniprot.org/annotation/VAR_027129|||http://purl.uniprot.org/annotation/VAR_027130|||http://purl.uniprot.org/annotation/VAR_027131|||http://purl.uniprot.org/annotation/VAR_027132|||http://purl.uniprot.org/annotation/VAR_027133|||http://purl.uniprot.org/annotation/VAR_027134|||http://purl.uniprot.org/annotation/VAR_027135|||http://purl.uniprot.org/annotation/VAR_027136|||http://purl.uniprot.org/annotation/VAR_027137|||http://purl.uniprot.org/annotation/VAR_027138|||http://purl.uniprot.org/annotation/VAR_027139|||http://purl.uniprot.org/annotation/VAR_027162|||http://purl.uniprot.org/annotation/VAR_027163|||http://purl.uniprot.org/annotation/VAR_027164|||http://purl.uniprot.org/annotation/VAR_027165|||http://purl.uniprot.org/annotation/VAR_027166|||http://purl.uniprot.org/annotation/VAR_067770|||http://purl.uniprot.org/annotation/VAR_067771|||http://purl.uniprot.org/annotation/VAR_067772|||http://purl.uniprot.org/annotation/VAR_067773|||http://purl.uniprot.org/annotation/VAR_067774|||http://purl.uniprot.org/annotation/VAR_067775|||http://purl.uniprot.org/annotation/VAR_067776|||http://purl.uniprot.org/annotation/VAR_067777|||http://purl.uniprot.org/annotation/VAR_067778|||http://purl.uniprot.org/annotation/VAR_067779|||http://purl.uniprot.org/annotation/VAR_067780|||http://purl.uniprot.org/annotation/VAR_067781|||http://purl.uniprot.org/annotation/VAR_067782|||http://purl.uniprot.org/annotation/VAR_067783|||http://purl.uniprot.org/annotation/VAR_067784|||http://purl.uniprot.org/annotation/VAR_067785|||http://purl.uniprot.org/annotation/VAR_067786|||http://purl.uniprot.org/annotation/VAR_067787|||http://purl.uniprot.org/annotation/VAR_067788|||http://purl.uniprot.org/annotation/VAR_067789|||http://purl.uniprot.org/annotation/VAR_067790|||http://purl.uniprot.org/annotation/VAR_067791|||http://purl.uniprot.org/annotation/VAR_067792|||http://purl.uniprot.org/annotation/VAR_067793|||http://purl.uniprot.org/annotation/VAR_067794|||http://purl.uniprot.org/annotation/VSP_020002|||http://purl.uniprot.org/annotation/VSP_020003|||http://purl.uniprot.org/annotation/VSP_055537|||http://purl.uniprot.org/annotation/VSP_055538|||http://purl.uniprot.org/annotation/VSP_055539
http://togogenome.org/gene/9606:LRTOMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ04                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In DFNB63.|||In DFNB63; unknown pathological significance.|||In isoform 2.|||Transmembrane O-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000354093|||http://purl.uniprot.org/annotation/VAR_047554|||http://purl.uniprot.org/annotation/VAR_047555|||http://purl.uniprot.org/annotation/VAR_047556|||http://purl.uniprot.org/annotation/VAR_054955|||http://purl.uniprot.org/annotation/VAR_054956|||http://purl.uniprot.org/annotation/VAR_054957|||http://purl.uniprot.org/annotation/VAR_079506|||http://purl.uniprot.org/annotation/VSP_036898
http://togogenome.org/gene/9606:PUM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL34|||http://purl.uniprot.org/uniprot/Q8TB72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenine-nucleotide binding in RNA target|||Basic and acidic residues|||Disordered|||Guanine-nucleotide binding in RNA target|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with SNAPIN|||Non-specific-nucleotide binding in RNA target|||Omega-N-methylarginine|||PUM-HD|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pumilio|||Pumilio 1|||Pumilio 2|||Pumilio 3|||Pumilio 4|||Pumilio 5|||Pumilio 6|||Pumilio 7|||Pumilio 8|||Pumilio homolog 2|||Uracil-nucleotide binding in RNA target                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075919|||http://purl.uniprot.org/annotation/VAR_057100|||http://purl.uniprot.org/annotation/VSP_009319|||http://purl.uniprot.org/annotation/VSP_009320|||http://purl.uniprot.org/annotation/VSP_053705
http://togogenome.org/gene/9606:MCF2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CRAL-TRIO|||DH|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Polar residues|||Probable guanine nucleotide exchange factor MCF2L2|||Spectrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337087|||http://purl.uniprot.org/annotation/VAR_043587|||http://purl.uniprot.org/annotation/VAR_043588|||http://purl.uniprot.org/annotation/VAR_043589|||http://purl.uniprot.org/annotation/VAR_043590|||http://purl.uniprot.org/annotation/VAR_043591|||http://purl.uniprot.org/annotation/VAR_043592|||http://purl.uniprot.org/annotation/VAR_043593|||http://purl.uniprot.org/annotation/VAR_043594|||http://purl.uniprot.org/annotation/VAR_043595|||http://purl.uniprot.org/annotation/VAR_043596|||http://purl.uniprot.org/annotation/VAR_043597|||http://purl.uniprot.org/annotation/VSP_033872|||http://purl.uniprot.org/annotation/VSP_033873|||http://purl.uniprot.org/annotation/VSP_033874|||http://purl.uniprot.org/annotation/VSP_033875|||http://purl.uniprot.org/annotation/VSP_033876
http://togogenome.org/gene/9606:CHADL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chondroadherin-like protein|||Disordered|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT 1|||LRRNT 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299548|||http://purl.uniprot.org/annotation/VAR_059805|||http://purl.uniprot.org/annotation/VAR_061805|||http://purl.uniprot.org/annotation/VSP_027735
http://togogenome.org/gene/9606:FCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00602                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  A domain; contributes to trimerization|||Abolishes interaction with all sialic acid-containing glycans.|||B domain; contributes to trimerization|||Collagen-like|||Disordered|||Fibrinogen C-terminal|||Ficolin-1|||In a colorectal cancer sample; somatic mutation.|||Inhibits binding to the 9-O-acetylated sialic acid derivatives.|||Mediates specificity for sialic acids|||N-linked (GlcNAc...) asparagine|||P domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009136|||http://purl.uniprot.org/annotation/VAR_024450|||http://purl.uniprot.org/annotation/VAR_036341|||http://purl.uniprot.org/annotation/VAR_061172
http://togogenome.org/gene/9606:PPP1R14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A00                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Inhibitory|||Phosphoserine|||Phosphothreonine; by PKC|||Protein phosphatase 1 regulatory subunit 14A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071486|||http://purl.uniprot.org/annotation/VSP_011841
http://togogenome.org/gene/9606:MSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWR7|||http://purl.uniprot.org/uniprot/Q68DK7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with KAT8|||Interaction with MSL2|||Male-specific lethal 1 homolog|||N6-acetyllysine|||Nuclear localization signal|||PEHE|||Phosphoserine|||Phosphothreonine|||Pro residues|||Sufficient for interaction with MSL3 MRG domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349236|||http://purl.uniprot.org/annotation/VSP_035236|||http://purl.uniprot.org/annotation/VSP_035237
http://togogenome.org/gene/9606:UBE3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15386                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||Abolishes E3 ubiquitin-protein ligase activity. No stimulation of in vitro CAND2 ubiquitination.|||Basic and acidic residues|||Cis-determinant of acceptor ubiquitin-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); by autocatalysis|||Glycyl thioester intermediate|||HECT|||IQ|||In isoform 2.|||In isoform 3.|||Increased E3 ubiquitin-protein ligase activity.|||Reduced E3 ubiquitin-protein ligase activity.|||Ubiquitin-protein ligase E3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194982|||http://purl.uniprot.org/annotation/VSP_013953|||http://purl.uniprot.org/annotation/VSP_013954|||http://purl.uniprot.org/annotation/VSP_013955|||http://purl.uniprot.org/annotation/VSP_013956|||http://purl.uniprot.org/annotation/VSP_013957
http://togogenome.org/gene/9606:GPR62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAM0|||http://purl.uniprot.org/uniprot/Q9BZJ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 62|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069580|||http://purl.uniprot.org/annotation/VAR_055920|||http://purl.uniprot.org/annotation/VAR_067702|||http://purl.uniprot.org/annotation/VAR_067703
http://togogenome.org/gene/9606:TP73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFW9|||http://purl.uniprot.org/uniprot/O15350                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform Alpha|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation of isoform beta by ABL1.|||Impaired phosphorylation.|||In CILD47.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform Beta and isoform dN-Beta.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma and isoform dN-Gamma.|||In isoform Zeta.|||In isoform dN-Alpha, isoform dN-Beta, isoform dN-Gamma and isoform 11.|||Interaction with HIPK2|||Loss of interaction with WWOX.|||Oligomerization|||PPxY motif|||Phosphothreonine; by PLK1|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by SRC and HCK|||Polar residues|||SAM|||Strongly diminishes sumoylation but does not affect transcriptional activity.|||Transactivation|||Tumor protein p73|||p53 DNA-binding|||p53 tetramerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185728|||http://purl.uniprot.org/annotation/VAR_086144|||http://purl.uniprot.org/annotation/VAR_086145|||http://purl.uniprot.org/annotation/VSP_006539|||http://purl.uniprot.org/annotation/VSP_006540|||http://purl.uniprot.org/annotation/VSP_006541|||http://purl.uniprot.org/annotation/VSP_006542|||http://purl.uniprot.org/annotation/VSP_006543|||http://purl.uniprot.org/annotation/VSP_006544|||http://purl.uniprot.org/annotation/VSP_006545|||http://purl.uniprot.org/annotation/VSP_006546|||http://purl.uniprot.org/annotation/VSP_014368|||http://purl.uniprot.org/annotation/VSP_045082|||http://purl.uniprot.org/annotation/VSP_053809|||http://purl.uniprot.org/annotation/VSP_053810
http://togogenome.org/gene/9606:PARP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||BRCT|||Disordered|||Interaction with the major vault protein|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein mono-ADP-ribosyltransferase PARP4|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211330|||http://purl.uniprot.org/annotation/VAR_016090|||http://purl.uniprot.org/annotation/VAR_016091|||http://purl.uniprot.org/annotation/VAR_056645|||http://purl.uniprot.org/annotation/VAR_056646|||http://purl.uniprot.org/annotation/VAR_056647|||http://purl.uniprot.org/annotation/VAR_056648|||http://purl.uniprot.org/annotation/VAR_056649|||http://purl.uniprot.org/annotation/VAR_056650|||http://purl.uniprot.org/annotation/VAR_056651|||http://purl.uniprot.org/annotation/VAR_056652|||http://purl.uniprot.org/annotation/VAR_056653
http://togogenome.org/gene/9606:GTPBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43824                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Hflx-type G|||Putative GTP-binding protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304798
http://togogenome.org/gene/9606:QRSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0R6                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-ester intermediate|||Charge relay system|||Disordered|||Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial|||In COXPD40.|||In COXPD40; highly decreased glutaminyl-tRNAGln biosynthesis via transamidation.|||In COXPD40; requires 2 nucleotide substitutions; unknown pathological significance.|||In COXPD40; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316767|||http://purl.uniprot.org/annotation/VAR_038389|||http://purl.uniprot.org/annotation/VAR_038390|||http://purl.uniprot.org/annotation/VAR_076270|||http://purl.uniprot.org/annotation/VAR_076271|||http://purl.uniprot.org/annotation/VAR_083983|||http://purl.uniprot.org/annotation/VAR_083984|||http://purl.uniprot.org/annotation/VAR_083985|||http://purl.uniprot.org/annotation/VSP_030773|||http://purl.uniprot.org/annotation/VSP_030774
http://togogenome.org/gene/9606:CD36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1B1|||http://purl.uniprot.org/uniprot/B7Z6C3|||http://purl.uniprot.org/uniprot/E9PLT1|||http://purl.uniprot.org/uniprot/P16671                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination induced by lipids. Enhances fatty acid uptake.|||Critical for TLR4-TLR6 dimerization and signaling|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In PG4D; type I.|||In PG4D; type I; degradation in the cytoplasm due to defects in maturation.|||In individuals from a malaria endemic area in West Africa.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with PTK2, PXN and LYN|||N-linked (GlcNAc...) asparagine|||No effect on cell surface location, nor on oxLDL-induced NF-kappa-B activation.|||No effect on cell surface location. Loss of oxLDL-induced NF-kappa-B activation.|||No effect on cell surface location. Loss of oxLDL-induced NF-kappa-B activation. Loss of complex formation with TLR4 and TLR6.|||Platelet glycoprotein 4|||Removed|||Required for interaction with thrombospondins, THBS1 and THBS2|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144151|||http://purl.uniprot.org/annotation/VAR_013918|||http://purl.uniprot.org/annotation/VAR_017913|||http://purl.uniprot.org/annotation/VAR_017914|||http://purl.uniprot.org/annotation/VAR_017915|||http://purl.uniprot.org/annotation/VAR_017916|||http://purl.uniprot.org/annotation/VAR_017917|||http://purl.uniprot.org/annotation/VAR_017918|||http://purl.uniprot.org/annotation/VAR_017919|||http://purl.uniprot.org/annotation/VAR_019049|||http://purl.uniprot.org/annotation/VAR_071161|||http://purl.uniprot.org/annotation/VAR_071162|||http://purl.uniprot.org/annotation/VSP_055976|||http://purl.uniprot.org/annotation/VSP_055977|||http://purl.uniprot.org/annotation/VSP_055978|||http://purl.uniprot.org/annotation/VSP_055979
http://togogenome.org/gene/9606:ABL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00519|||http://purl.uniprot.org/uniprot/Q59FK4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity.|||Basic and acidic residues|||Breakpoint for translocation to form BCR-ABL and NUP214-ABL1 fusion proteins|||CAP|||DNA-binding|||Disordered|||F-actin-binding|||In CHDSKM; increases kinase activity; no effect on protein levels.|||In a lung large cell carcinoma sample; somatic mutation.|||In a melanoma sample; somatic mutation.|||In isoform IB.|||Kinase activation loop|||N-myristoyl glycine|||N6-acetyllysine; by EP300|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||Nuclear localization signal 3|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases|||Polar residues|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Tyrosine-protein kinase ABL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088050|||http://purl.uniprot.org/annotation/VAR_025043|||http://purl.uniprot.org/annotation/VAR_025044|||http://purl.uniprot.org/annotation/VAR_025045|||http://purl.uniprot.org/annotation/VAR_025046|||http://purl.uniprot.org/annotation/VAR_032676|||http://purl.uniprot.org/annotation/VAR_032677|||http://purl.uniprot.org/annotation/VAR_032678|||http://purl.uniprot.org/annotation/VAR_051692|||http://purl.uniprot.org/annotation/VAR_051693|||http://purl.uniprot.org/annotation/VAR_051694|||http://purl.uniprot.org/annotation/VAR_079482|||http://purl.uniprot.org/annotation/VAR_079483|||http://purl.uniprot.org/annotation/VSP_004957
http://togogenome.org/gene/9606:HLA-DQB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2H4Z4R5|||http://purl.uniprot.org/uniprot/A2ADX3|||http://purl.uniprot.org/uniprot/P05538|||http://purl.uniprot.org/uniprot/Q5SR05                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1|||Beta-2|||Cytoplasmic|||Disordered|||Extracellular|||HLA class II histocompatibility antigen, DQ beta 2 chain|||Helical|||Ig-like|||Ig-like C1-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018992|||http://purl.uniprot.org/annotation/PRO_5014565236|||http://purl.uniprot.org/annotation/PRO_5014586897|||http://purl.uniprot.org/annotation/PRO_5015080583|||http://purl.uniprot.org/annotation/VAR_069445|||http://purl.uniprot.org/annotation/VAR_069446|||http://purl.uniprot.org/annotation/VAR_069447|||http://purl.uniprot.org/annotation/VSP_045914|||http://purl.uniprot.org/annotation/VSP_045915
http://togogenome.org/gene/9606:TSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRM8|||http://purl.uniprot.org/uniprot/Q15631                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA/RNA binding|||In isoform 2.|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Translin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191683|||http://purl.uniprot.org/annotation/VSP_044937|||http://purl.uniprot.org/annotation/VSP_044938
http://togogenome.org/gene/9606:BMERB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||bMERB|||bMERB domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079281|||http://purl.uniprot.org/annotation/VSP_047232
http://togogenome.org/gene/9606:LIME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT39|||http://purl.uniprot.org/uniprot/Q9H400                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to CSK.|||Abolishes binding to LCK and reduces binding to FYN.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Interaction with CSK|||Interaction with GRB2|||Interaction with LCK and PIK3R1|||Interaction with LCK, PLCG2 and PIK3R1|||Lck-interacting transmembrane adapter 1|||No change in binding to LCK, CSK or FYN.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LCK|||Reduces binding to CSK.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083332|||http://purl.uniprot.org/annotation/PRO_5001831882|||http://purl.uniprot.org/annotation/VAR_053918|||http://purl.uniprot.org/annotation/VSP_016642
http://togogenome.org/gene/9606:EN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05925                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein engrailed-1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000196062
http://togogenome.org/gene/9606:CCDC96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M329                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 96|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234096|||http://purl.uniprot.org/annotation/VAR_026162
http://togogenome.org/gene/9606:KCNIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4N3|||http://purl.uniprot.org/uniprot/Q6PIL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  EF-hand|||EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with KCND2|||KIS|||Kv channel-interacting protein 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073825|||http://purl.uniprot.org/annotation/VSP_015066|||http://purl.uniprot.org/annotation/VSP_015067|||http://purl.uniprot.org/annotation/VSP_015068|||http://purl.uniprot.org/annotation/VSP_043321
http://togogenome.org/gene/9606:MED28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H204                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region|||Turn                                                                                  ^@                                                                                  Disordered|||Mediator of RNA polymerase II transcription subunit 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000113981
http://togogenome.org/gene/9606:LRRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75325                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat neuronal protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014849|||http://purl.uniprot.org/annotation/VAR_021921|||http://purl.uniprot.org/annotation/VAR_021922|||http://purl.uniprot.org/annotation/VAR_049898|||http://purl.uniprot.org/annotation/VAR_049899|||http://purl.uniprot.org/annotation/VAR_049900
http://togogenome.org/gene/9606:EXOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KP1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Exocyst complex component 2|||IPT/TIG|||Impaired cytokinesis. Loss of RALA-binding. No change in localization to the midbody during cytokinesis.|||In NEDFACH; decreased protein abundance; shows defective ARL13B cilium membrane localization.|||In NEDFACH; unknown pathological significance; no effect on protein abundance.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118918|||http://purl.uniprot.org/annotation/VAR_048956|||http://purl.uniprot.org/annotation/VAR_085744|||http://purl.uniprot.org/annotation/VAR_085745|||http://purl.uniprot.org/annotation/VAR_085746
http://togogenome.org/gene/9606:ANO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XXA6|||http://purl.uniprot.org/uniprot/Q9NW72                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin-1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Unlikely to bind calcium but may play an important structural role                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288435|||http://purl.uniprot.org/annotation/VAR_032417|||http://purl.uniprot.org/annotation/VAR_032418|||http://purl.uniprot.org/annotation/VSP_025665|||http://purl.uniprot.org/annotation/VSP_025666|||http://purl.uniprot.org/annotation/VSP_025667|||http://purl.uniprot.org/annotation/VSP_025668|||http://purl.uniprot.org/annotation/VSP_025669|||http://purl.uniprot.org/annotation/VSP_025670|||http://purl.uniprot.org/annotation/VSP_025671|||http://purl.uniprot.org/annotation/VSP_061539|||http://purl.uniprot.org/annotation/VSP_061540|||http://purl.uniprot.org/annotation/VSP_061541
http://togogenome.org/gene/9606:SHTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0MZ66                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 8.|||In isoform 5 and isoform 8.|||In isoform 6.|||In isoform 7.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphothreonine|||Polar residues|||Pro residues|||Shootin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295740|||http://purl.uniprot.org/annotation/VSP_027050|||http://purl.uniprot.org/annotation/VSP_027051|||http://purl.uniprot.org/annotation/VSP_027052|||http://purl.uniprot.org/annotation/VSP_027053|||http://purl.uniprot.org/annotation/VSP_036497|||http://purl.uniprot.org/annotation/VSP_036498|||http://purl.uniprot.org/annotation/VSP_036499
http://togogenome.org/gene/9606:PGM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KN95|||http://purl.uniprot.org/uniprot/O95394                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-D-phosphohexomutase C-terminal|||Alpha-D-phosphohexomutase alpha/beta/alpha|||In IMD23; decreased function in UUDP-N-acetylglucosamine biosynthetic process; no effect on protein abundance.|||In IMD23; decreased phosphoacetylglucosamine mutase activity.|||In IMD23; decreased phosphoacetylglucosamine mutase activity; decreased protein abundance.|||In IMD23; decreased phosphoacetylglucosamine mutase activity; no effect on protein abundance.|||In IMD23; loss of phosphoacetylglucosamine mutase activity.|||In allele PGM3*2.|||In isoform 2.|||In isoform 3.|||Loss of activity.|||N-acetylmethionine|||Phosphoacetylglucosamine mutase|||Phosphoserine|||Phosphoserine intermediate|||Phosphothreonine|||via phosphate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148013|||http://purl.uniprot.org/annotation/VAR_013489|||http://purl.uniprot.org/annotation/VAR_071359|||http://purl.uniprot.org/annotation/VAR_071360|||http://purl.uniprot.org/annotation/VAR_071361|||http://purl.uniprot.org/annotation/VAR_071362|||http://purl.uniprot.org/annotation/VAR_071363|||http://purl.uniprot.org/annotation/VAR_071364|||http://purl.uniprot.org/annotation/VAR_071365|||http://purl.uniprot.org/annotation/VAR_071366|||http://purl.uniprot.org/annotation/VSP_047319|||http://purl.uniprot.org/annotation/VSP_047320
http://togogenome.org/gene/9606:ZNF714                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WU35|||http://purl.uniprot.org/uniprot/Q96N38                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 714                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331749|||http://purl.uniprot.org/annotation/VAR_042936|||http://purl.uniprot.org/annotation/VAR_042937|||http://purl.uniprot.org/annotation/VAR_057448|||http://purl.uniprot.org/annotation/VSP_033319|||http://purl.uniprot.org/annotation/VSP_033320|||http://purl.uniprot.org/annotation/VSP_033321
http://togogenome.org/gene/9606:CR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PDY4|||http://purl.uniprot.org/uniprot/P17927                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Complement receptor type 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MCC(b) antigen.|||In Sl(2)/Vil antigen and Sl(3) antigen.|||In Sl(3) antigen.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pyrrolidone carboxylic acid|||Sushi|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 21|||Sushi 22|||Sushi 23|||Sushi 24|||Sushi 25|||Sushi 26|||Sushi 27|||Sushi 28|||Sushi 29|||Sushi 3|||Sushi 30|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006009|||http://purl.uniprot.org/annotation/PRO_5003244036|||http://purl.uniprot.org/annotation/VAR_013819|||http://purl.uniprot.org/annotation/VAR_013820|||http://purl.uniprot.org/annotation/VAR_013821|||http://purl.uniprot.org/annotation/VAR_013822|||http://purl.uniprot.org/annotation/VAR_013823|||http://purl.uniprot.org/annotation/VAR_013824|||http://purl.uniprot.org/annotation/VAR_013825|||http://purl.uniprot.org/annotation/VAR_013826|||http://purl.uniprot.org/annotation/VAR_020263|||http://purl.uniprot.org/annotation/VAR_055685|||http://purl.uniprot.org/annotation/VAR_055686
http://togogenome.org/gene/9606:HSPA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11021|||http://purl.uniprot.org/uniprot/V9HWB4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||78 kDa glucose-regulated protein|||Complete loss of in vitro methylation by METTL21A.|||Disordered|||Endoplasmic reticulum chaperone BiP|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired ATPase activity.|||Interdomain linker|||N6,N6,N6-trimethyllysine; by METTL21A; in vitro|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-succinyllysine|||Nucleotide-binding (NBD)|||O-AMP-threonine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; alternate|||Prevents secretion from ER|||Required for interaction with KIAA1324|||Substrate-binding (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013566|||http://purl.uniprot.org/annotation/PRO_5004776903|||http://purl.uniprot.org/annotation/VAR_025815
http://togogenome.org/gene/9606:DPP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPB8|||http://purl.uniprot.org/uniprot/Q9NY33                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dipeptidyl peptidase 3|||In isoform 2.|||In isoform 4.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078238|||http://purl.uniprot.org/annotation/VAR_021850|||http://purl.uniprot.org/annotation/VAR_033494|||http://purl.uniprot.org/annotation/VAR_033495|||http://purl.uniprot.org/annotation/VAR_051597|||http://purl.uniprot.org/annotation/VSP_005510|||http://purl.uniprot.org/annotation/VSP_044696
http://togogenome.org/gene/9606:P4HB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8S5|||http://purl.uniprot.org/uniprot/P07237                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation at this site but protein is still phosphorylated at other sites. No changes in chaperone or enzyme activity.|||Acidic residues|||Contributes to redox potential value|||Disordered|||In CLCRP1; impairs ability to act as a disulfide isomerase enzyme.|||Lowers pKa of C-terminal Cys of first active site|||Lowers pKa of C-terminal Cys of second active site|||N6-acetyllysine|||N6-succinyllysine|||Nucleophile|||Phosphomimetic mutant. Does not affect enzyme or chaperone activity.|||Phosphomimetic mutant. Does not affect enzyme or chaperone activity. Does not increase binding to ERN1.|||Phosphomimetic mutant. Reduced resistance to protease digestion, sugesting adoption of an open conformation. Increased chaperone activity. Decreased enzyme activity. Increased binding to ERN1.|||Phosphoserine|||Phosphoserine; by FAM20C|||Prevents secretion from ER|||Protein disulfide-isomerase|||Redox-active|||Reduced interaction with ERN1. Abolishes interaction with ERN1; when associated with I-128.|||Reduced interaction with ERN1. Abolishes interaction with ERN1; when associated with W-403.|||Thioredoxin 1|||Thioredoxin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034195|||http://purl.uniprot.org/annotation/PRO_5014202969|||http://purl.uniprot.org/annotation/VAR_073440
http://togogenome.org/gene/9606:SLC25A33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSK2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291785|||http://purl.uniprot.org/annotation/VAR_032861
http://togogenome.org/gene/9606:H4C16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:ADGRL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBW9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor L4|||Cleavage|||Cytoplasmic|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012870|||http://purl.uniprot.org/annotation/VAR_047072|||http://purl.uniprot.org/annotation/VAR_047073|||http://purl.uniprot.org/annotation/VAR_047074
http://togogenome.org/gene/9606:SDHC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4B7|||http://purl.uniprot.org/uniprot/A0A0S2Z4C9|||http://purl.uniprot.org/uniprot/Q99643                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Non-terminal Residue|||Signal Peptide|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Succinate dehydrogenase cytochrome b560 subunit, mitochondrial|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003634|||http://purl.uniprot.org/annotation/PRO_5013289043|||http://purl.uniprot.org/annotation/VSP_041381|||http://purl.uniprot.org/annotation/VSP_041382|||http://purl.uniprot.org/annotation/VSP_041383
http://togogenome.org/gene/9606:UAP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KQV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Substrate binding|||UDP-N-acetylhexosamine pyrophosphorylase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324580|||http://purl.uniprot.org/annotation/VAR_039839|||http://purl.uniprot.org/annotation/VAR_039840|||http://purl.uniprot.org/annotation/VSP_032280
http://togogenome.org/gene/9606:PRSS33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NF86                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Peptidase S1|||Serine protease 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299316
http://togogenome.org/gene/9606:NALCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZF0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects voltage sensitivity.|||Cytoplasmic|||Decreases channel activity.|||Disordered|||Does not affect the voltage sensitivity.|||Does not exhibited altered current kinetics.|||Drastically more sensitive to Ca(2+) block.|||Exhibits altered current kinetics.|||Extracellular|||Found in patients with distal arthrogryposis and central hypertonia; unknown pathological significance.|||Found in patients with neurodevelopmental disease and hypotonia; unknown pathological significance.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||Helical; Voltage-sensor; Name=S4 of repeat I|||Helical; Voltage-sensor; Name=S4 of repeat II|||Helical; Voltage-sensor; Name=S4 of repeat III|||Helical; Voltage-sensor; Name=S4 of repeat IV|||In CLIFAHDD and IHPRF1; nearly eliminates wild-type protein expression; dominant-negative mutation; decreases membrane expression; induces higher current density and slower inactivation.|||In CLIFAHDD and IHPRF1; nearly eliminates wild-type protein expression; dominant-negative mutation; decreases membrane expressioninduces higher current density and slower inactivation.|||In CLIFAHDD.|||In CLIFAHDD; found in patients with neurodevelopmental disease and hypotonia; unknown pathological significance.|||In IHPRF1; loss of function.|||In isoform 2.|||In isoform 3.|||Increases channel activity.|||Moderately more sensitive to Ca(2+) block.|||N-linked (GlcNAc...) asparagine|||No effect on the blockage of NALCN pore by Ca(2+).|||No effect on the channel activity.|||Polar residues|||Pore-forming|||Sodium leak channel NALCN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314010|||http://purl.uniprot.org/annotation/VAR_070599|||http://purl.uniprot.org/annotation/VAR_073361|||http://purl.uniprot.org/annotation/VAR_073362|||http://purl.uniprot.org/annotation/VAR_073363|||http://purl.uniprot.org/annotation/VAR_073364|||http://purl.uniprot.org/annotation/VAR_073365|||http://purl.uniprot.org/annotation/VAR_073366|||http://purl.uniprot.org/annotation/VAR_073367|||http://purl.uniprot.org/annotation/VAR_073368|||http://purl.uniprot.org/annotation/VAR_076674|||http://purl.uniprot.org/annotation/VAR_076675|||http://purl.uniprot.org/annotation/VAR_076676|||http://purl.uniprot.org/annotation/VAR_076677|||http://purl.uniprot.org/annotation/VAR_076678|||http://purl.uniprot.org/annotation/VSP_030188|||http://purl.uniprot.org/annotation/VSP_030189|||http://purl.uniprot.org/annotation/VSP_030190|||http://purl.uniprot.org/annotation/VSP_030191
http://togogenome.org/gene/9606:ZNFX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2E3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In IMD91.|||In IMD91; unknown pathological significance.|||In isoform 2.|||NF-X1-type 1|||NF-X1-type 2|||NF-X1-type 3|||NF-X1-type 4|||NF-X1-type 5|||NF-X1-type 6|||NFX1-type zinc finger-containing protein 1|||Polar residues|||RZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050795|||http://purl.uniprot.org/annotation/VAR_014078|||http://purl.uniprot.org/annotation/VAR_014079|||http://purl.uniprot.org/annotation/VAR_014080|||http://purl.uniprot.org/annotation/VAR_014081|||http://purl.uniprot.org/annotation/VAR_024487|||http://purl.uniprot.org/annotation/VAR_051504|||http://purl.uniprot.org/annotation/VAR_085313|||http://purl.uniprot.org/annotation/VAR_085314|||http://purl.uniprot.org/annotation/VAR_085315|||http://purl.uniprot.org/annotation/VAR_085316|||http://purl.uniprot.org/annotation/VAR_085317|||http://purl.uniprot.org/annotation/VAR_085318|||http://purl.uniprot.org/annotation/VAR_085319|||http://purl.uniprot.org/annotation/VSP_002434|||http://purl.uniprot.org/annotation/VSP_002435
http://togogenome.org/gene/9606:CERS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DE47|||http://purl.uniprot.org/uniprot/P27544|||http://purl.uniprot.org/uniprot/Q5XG75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Ceramide synthase 1|||Helical|||In EPM8.|||In EPM8; expressed and localized properly to the ER; impaired ceramide synthase activity.|||In EPM8; unknown pathological significance.|||In isoform 2.|||Loss of ceramide synthase activity.|||N-acetylalanine|||Removed|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185507|||http://purl.uniprot.org/annotation/VAR_073336|||http://purl.uniprot.org/annotation/VAR_085037|||http://purl.uniprot.org/annotation/VAR_085038|||http://purl.uniprot.org/annotation/VSP_003049
http://togogenome.org/gene/9606:MRAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G30                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||Found in a patient with obesity; unknown pathological significance.|||Helical|||Melanocortin-2 receptor accessory protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089522|||http://purl.uniprot.org/annotation/VAR_069986|||http://purl.uniprot.org/annotation/VAR_069987|||http://purl.uniprot.org/annotation/VAR_069988
http://togogenome.org/gene/9606:CDK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11802                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase 4|||In CMM3.|||In CMM3; somatic and familial; generates a dominant oncogene resistant to inhibition by p16(INK4a).|||In CMM3; sporadic.|||In isoform 2.|||N-acetylalanine|||No effect on in vitro phosphorylation by CDK7. Greatly reduced T-172 phosphorylation and enzyme activity.|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Removed|||Required for binding D-type cyclins|||Retains moderate enzyme activity.|||Weak enzyme activity towards RB1, but no effect on binding of CCDN1 nor CCDN3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085778|||http://purl.uniprot.org/annotation/VAR_006200|||http://purl.uniprot.org/annotation/VAR_006201|||http://purl.uniprot.org/annotation/VAR_021152|||http://purl.uniprot.org/annotation/VAR_029153|||http://purl.uniprot.org/annotation/VAR_041976|||http://purl.uniprot.org/annotation/VSP_056487
http://togogenome.org/gene/9606:CT83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H943                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Kita-kyushu lung cancer antigen 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293736
http://togogenome.org/gene/9606:GSDMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by S.pyogenes SpeB|||Abolished cleavage by S.pyogenes effector protein SpeB, preventing pyroptosis.|||Beta stranded|||Gasdermin-A|||Gasdermin-A, C-terminal|||Gasdermin-A, N-terminal|||Spontaneous pyroptosis-inducing activity.|||Triggers pyroptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148173|||http://purl.uniprot.org/annotation/PRO_0000451664|||http://purl.uniprot.org/annotation/PRO_0000451665|||http://purl.uniprot.org/annotation/VAR_035010|||http://purl.uniprot.org/annotation/VAR_035011|||http://purl.uniprot.org/annotation/VAR_035012|||http://purl.uniprot.org/annotation/VAR_062005
http://togogenome.org/gene/9606:TEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42680                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||PH|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis, LYN and JAK2|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Tyrosine-protein kinase Tec                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088170|||http://purl.uniprot.org/annotation/VAR_041850|||http://purl.uniprot.org/annotation/VAR_041851
http://togogenome.org/gene/9606:RGS7BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKB7|||http://purl.uniprot.org/uniprot/Q6MZT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Polar residues|||Regulator of G-protein signaling 7-binding protein|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287595|||http://purl.uniprot.org/annotation/VAR_032334
http://togogenome.org/gene/9606:NPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6C0|||http://purl.uniprot.org/uniprot/P61916                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In NPC2.|||In NPC2; leads to the synthesis of misfolded recombinant proteins that colocalized with an endoplasmic reticulum marker; normally secreted but unable to correct cholesterol storage in NPC2-deficient cells.|||In NPC2; results in the synthesis of functional recombinant proteins correctly targeted to lysosomes.|||In NPC2; unable to bind cholesterol.|||In isoform 2.|||MD-2-related lipid-recognition|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||NPC intracellular cholesterol transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019854|||http://purl.uniprot.org/annotation/PRO_5014214248|||http://purl.uniprot.org/annotation/VAR_011899|||http://purl.uniprot.org/annotation/VAR_015848|||http://purl.uniprot.org/annotation/VAR_015849|||http://purl.uniprot.org/annotation/VAR_043303|||http://purl.uniprot.org/annotation/VAR_043304|||http://purl.uniprot.org/annotation/VAR_043305|||http://purl.uniprot.org/annotation/VAR_043306|||http://purl.uniprot.org/annotation/VAR_043307|||http://purl.uniprot.org/annotation/VSP_056459
http://togogenome.org/gene/9606:NMUR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZQ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuromedin-U receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069910|||http://purl.uniprot.org/annotation/VAR_023941|||http://purl.uniprot.org/annotation/VAR_023942|||http://purl.uniprot.org/annotation/VAR_023943|||http://purl.uniprot.org/annotation/VAR_023944|||http://purl.uniprot.org/annotation/VAR_032770
http://togogenome.org/gene/9606:TRIM61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EBN2                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||Putative tripartite motif-containing protein 61|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272303
http://togogenome.org/gene/9606:ARL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P5N6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 16|||Loss of the inhibition of RIGI-mediated antiviral response activity. Loss of GTP binding activity. Loss of interaction with RIGI.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264630|||http://purl.uniprot.org/annotation/VAR_059129
http://togogenome.org/gene/9606:SETD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYW2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AWS|||Basic and acidic residues|||Disordered|||Does not affect interaction with hyperphosphorylated POLR2A.|||Does not affect methyltransferase activity.|||Found in a patient with autism; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase SETD2|||Impaired methyltransferase activity.|||Impairs interaction with hyperphosphorylated POLR2A.|||In ALL; unknown pathological significance; somatic mutation.|||In AML; Impairs interaction with hyperphosphorylated POLR2A; unknown pathological significance; somatic mutation.|||In AML; unknown pathological significance; somatic mutation.|||In LLS; unknown pathological significance.|||In MRD70.|||In RAPAS.|||In RCC; defects in recruitment of the MutS alpha complex.|||In isoform 2.|||In isoform 3.|||Increased methyltransferase activity.|||Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528.|||Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531.|||Interaction with POLR2A|||Interaction with TUBA1A|||Loss of methyltransferase activity.|||Loss of methyltransferase activity. Abolishes ability to monomethylate STAT1.|||Low charge region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||SET|||Strongly reduced methyltransferase activity.|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252367|||http://purl.uniprot.org/annotation/VAR_027839|||http://purl.uniprot.org/annotation/VAR_027840|||http://purl.uniprot.org/annotation/VAR_027841|||http://purl.uniprot.org/annotation/VAR_061216|||http://purl.uniprot.org/annotation/VAR_069812|||http://purl.uniprot.org/annotation/VAR_069813|||http://purl.uniprot.org/annotation/VAR_076536|||http://purl.uniprot.org/annotation/VAR_078707|||http://purl.uniprot.org/annotation/VAR_079054|||http://purl.uniprot.org/annotation/VAR_079055|||http://purl.uniprot.org/annotation/VAR_079056|||http://purl.uniprot.org/annotation/VAR_079057|||http://purl.uniprot.org/annotation/VAR_079058|||http://purl.uniprot.org/annotation/VAR_079059|||http://purl.uniprot.org/annotation/VAR_079060|||http://purl.uniprot.org/annotation/VAR_079061|||http://purl.uniprot.org/annotation/VAR_079062|||http://purl.uniprot.org/annotation/VAR_079063|||http://purl.uniprot.org/annotation/VAR_079064|||http://purl.uniprot.org/annotation/VAR_079065|||http://purl.uniprot.org/annotation/VAR_079066|||http://purl.uniprot.org/annotation/VAR_079067|||http://purl.uniprot.org/annotation/VAR_079068|||http://purl.uniprot.org/annotation/VAR_079069|||http://purl.uniprot.org/annotation/VAR_079070|||http://purl.uniprot.org/annotation/VAR_079071|||http://purl.uniprot.org/annotation/VAR_079072|||http://purl.uniprot.org/annotation/VAR_079073|||http://purl.uniprot.org/annotation/VAR_079074|||http://purl.uniprot.org/annotation/VAR_079075|||http://purl.uniprot.org/annotation/VAR_079076|||http://purl.uniprot.org/annotation/VAR_079077|||http://purl.uniprot.org/annotation/VAR_079078|||http://purl.uniprot.org/annotation/VAR_079079|||http://purl.uniprot.org/annotation/VAR_079080|||http://purl.uniprot.org/annotation/VAR_079081|||http://purl.uniprot.org/annotation/VAR_079082|||http://purl.uniprot.org/annotation/VAR_079083|||http://purl.uniprot.org/annotation/VAR_079084|||http://purl.uniprot.org/annotation/VAR_079085|||http://purl.uniprot.org/annotation/VAR_079086|||http://purl.uniprot.org/annotation/VAR_079087|||http://purl.uniprot.org/annotation/VAR_079088|||http://purl.uniprot.org/annotation/VAR_087881|||http://purl.uniprot.org/annotation/VAR_087882|||http://purl.uniprot.org/annotation/VSP_020914|||http://purl.uniprot.org/annotation/VSP_020915
http://togogenome.org/gene/9606:MALL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13021                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Helical|||MAL-like protein|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156811
http://togogenome.org/gene/9606:SFXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWM7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylmethionine|||Sideroflexin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000177037
http://togogenome.org/gene/9606:PDPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MT40|||http://purl.uniprot.org/uniprot/B4DZL5|||http://purl.uniprot.org/uniprot/Q8NCN5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Aminomethyltransferase folate-binding|||FAD dependent oxidoreductase|||FAD dependent oxidoreductase central|||Glycine cleavage T-protein C-terminal barrel|||In isoform 2.|||Mitochondrion|||Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328740|||http://purl.uniprot.org/annotation/VAR_042504|||http://purl.uniprot.org/annotation/VSP_056077
http://togogenome.org/gene/9606:NAP1L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NT1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Nucleosome assembly protein 1-like 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317142|||http://purl.uniprot.org/annotation/VAR_050227
http://togogenome.org/gene/9606:PPDPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pancreatic progenitor cell differentiation and proliferation factor|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079468|||http://purl.uniprot.org/annotation/VSP_003823|||http://purl.uniprot.org/annotation/VSP_003824
http://togogenome.org/gene/9606:C4orf17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C4orf17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089433|||http://purl.uniprot.org/annotation/VAR_028110|||http://purl.uniprot.org/annotation/VAR_028111|||http://purl.uniprot.org/annotation/VAR_028112|||http://purl.uniprot.org/annotation/VSP_056907|||http://purl.uniprot.org/annotation/VSP_056908
http://togogenome.org/gene/9606:APOBEC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW27                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||Proton donor|||Putative C->U-editing enzyme APOBEC-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239355|||http://purl.uniprot.org/annotation/VAR_026639|||http://purl.uniprot.org/annotation/VAR_026640|||http://purl.uniprot.org/annotation/VAR_026641|||http://purl.uniprot.org/annotation/VAR_026642|||http://purl.uniprot.org/annotation/VAR_026643|||http://purl.uniprot.org/annotation/VAR_048724
http://togogenome.org/gene/9606:DSE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YE23|||http://purl.uniprot.org/uniprot/A0A2U3TZJ0|||http://purl.uniprot.org/uniprot/B7Z765|||http://purl.uniprot.org/uniprot/Q9UL01                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Critical for catalysis|||Cytoplasmic|||Dermatan-sulfate epimerase|||Helical|||Heparinase II N-terminal|||Impairs catalytic activity.|||In EDSMC2; shows a loss of epimerase activity towards partially desulfated dermatan sulfate; patient-derived fibroblasts show also a significant reduction in activity.|||Lumenal|||Moderately reduced catalytic activity.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) (paucimannose) asparagine|||No significant effect on catalytic activity.|||Proton donor|||Severely impairs catalytic activity.|||Very low levels of protein expression and no detectable catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223311|||http://purl.uniprot.org/annotation/PRO_5015763649|||http://purl.uniprot.org/annotation/PRO_5039982408|||http://purl.uniprot.org/annotation/VAR_034481|||http://purl.uniprot.org/annotation/VAR_053833|||http://purl.uniprot.org/annotation/VAR_053834|||http://purl.uniprot.org/annotation/VAR_070911
http://togogenome.org/gene/9606:BCORL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9F3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||BCL-6 corepressor-like protein 1|||Basic and acidic residues|||Disordered|||Found in a patient with Uruguay faciocardiomusculoskeletal syndrome; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In SHUVER; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||In isoform 4.|||Nuclear localization signal|||PCGF Ub-like fold domain (PUFD); required for the interaction with the KDM2B-SKP1 heterodimeric complex|||Phosphoserine|||Polar residues|||Pro residues|||Slightly inhibits interaction with PCGF1.|||Strongly reduced repressor activity. Interferes with CTBP1 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312268|||http://purl.uniprot.org/annotation/VAR_037467|||http://purl.uniprot.org/annotation/VAR_037468|||http://purl.uniprot.org/annotation/VAR_061020|||http://purl.uniprot.org/annotation/VAR_070559|||http://purl.uniprot.org/annotation/VAR_080909|||http://purl.uniprot.org/annotation/VAR_082288|||http://purl.uniprot.org/annotation/VAR_082289|||http://purl.uniprot.org/annotation/VAR_082290|||http://purl.uniprot.org/annotation/VSP_061439|||http://purl.uniprot.org/annotation/VSP_061440
http://togogenome.org/gene/9606:SOX14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95416                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding                                                                                  ^@                                                                                  HMG box|||Transcription factor SOX-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048758
http://togogenome.org/gene/9606:PRKAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54619                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'-AMP-activated protein kinase subunit gamma-1|||AMPK pseudosubstrate|||CBS 1|||CBS 2|||CBS 3|||CBS 4|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine; by ULK1|||Phosphothreonine; by ULK1|||Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Does not affect ADP activation of phosphorylation of PRKAA1 or PRKAA2.|||Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204377|||http://purl.uniprot.org/annotation/VAR_033453|||http://purl.uniprot.org/annotation/VAR_033454|||http://purl.uniprot.org/annotation/VSP_046711|||http://purl.uniprot.org/annotation/VSP_046712
http://togogenome.org/gene/9606:ASTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8Y4|||http://purl.uniprot.org/uniprot/B1AJS1|||http://purl.uniprot.org/uniprot/O14525                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Astrotactin-1|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 1 and isoform 3.|||In isoform 3.|||MACPF|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007481|||http://purl.uniprot.org/annotation/PRO_5002759907|||http://purl.uniprot.org/annotation/PRO_5014297010|||http://purl.uniprot.org/annotation/VAR_036764|||http://purl.uniprot.org/annotation/VAR_055713|||http://purl.uniprot.org/annotation/VAR_069030|||http://purl.uniprot.org/annotation/VAR_069031|||http://purl.uniprot.org/annotation/VSP_001371|||http://purl.uniprot.org/annotation/VSP_045069
http://togogenome.org/gene/9606:FOXI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQN5                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein I2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320118
http://togogenome.org/gene/9606:CYSLTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q38Q88|||http://purl.uniprot.org/uniprot/Q38Q91|||http://purl.uniprot.org/uniprot/Q9Y271                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cysteinyl leukotriene receptor 1|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069299
http://togogenome.org/gene/9606:FANCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fanconi anemia group E protein|||In FANCE; uncertain pathological significance.|||Interaction with FANCC|||Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-346.|||Non-phosphorylatable by CHEK1, not polyubiquitinated and unable to complement the mitomycin C hypersensitivity of cells lacking FANCE; when associated with A-374.|||Phosphoserine|||Phosphoserine; by CHEK1|||Phosphothreonine; by CHEK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087187|||http://purl.uniprot.org/annotation/VAR_023372|||http://purl.uniprot.org/annotation/VAR_023373|||http://purl.uniprot.org/annotation/VAR_023374|||http://purl.uniprot.org/annotation/VAR_023375|||http://purl.uniprot.org/annotation/VAR_023376|||http://purl.uniprot.org/annotation/VAR_038022
http://togogenome.org/gene/9606:ZNF486                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G180|||http://purl.uniprot.org/uniprot/Q96H40                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 486                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047611
http://togogenome.org/gene/9606:MYL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A32                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||In DA1C.|||In DA1C; unknown pathological significance.|||Myosin regulatory light chain 11|||N,N,N-trimethylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283746|||http://purl.uniprot.org/annotation/VAR_085167|||http://purl.uniprot.org/annotation/VAR_085168|||http://purl.uniprot.org/annotation/VAR_085169|||http://purl.uniprot.org/annotation/VAR_085170
http://togogenome.org/gene/9606:ZBTB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95625|||http://purl.uniprot.org/uniprot/Q59H97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRT69; impaired localization to the nucleolus.|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047727|||http://purl.uniprot.org/annotation/VAR_021894|||http://purl.uniprot.org/annotation/VAR_047465|||http://purl.uniprot.org/annotation/VAR_080760|||http://purl.uniprot.org/annotation/VAR_082098
http://togogenome.org/gene/9606:VWA5B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TIE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326173|||http://purl.uniprot.org/annotation/VAR_039994|||http://purl.uniprot.org/annotation/VAR_039995|||http://purl.uniprot.org/annotation/VAR_039996|||http://purl.uniprot.org/annotation/VAR_039997|||http://purl.uniprot.org/annotation/VSP_032580|||http://purl.uniprot.org/annotation/VSP_032581|||http://purl.uniprot.org/annotation/VSP_032582|||http://purl.uniprot.org/annotation/VSP_040399|||http://purl.uniprot.org/annotation/VSP_040400|||http://purl.uniprot.org/annotation/VSP_040401|||http://purl.uniprot.org/annotation/VSP_040402|||http://purl.uniprot.org/annotation/VSP_040403
http://togogenome.org/gene/9606:UBE2I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K503|||http://purl.uniprot.org/uniprot/B0QYN7|||http://purl.uniprot.org/uniprot/P63279                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Glycyl thioester intermediate|||Impairs binding to RANBP2.|||Impairs binding to SUMO1 and catalytic activity.|||Impairs catalytic activity.|||Interaction with RANBP2|||Interaction with SUMO1|||Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels.|||N-acetylserine|||N6-acetyllysine|||No effect on catalytic activity.|||Phosphoserine; by CDK1|||Removed|||SUMO-conjugating enzyme UBC9|||Slightly impairs binding to RANBP2.|||Substrate binding|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082454
http://togogenome.org/gene/9606:NRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16656                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Dimerization|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform 4.|||In isoform Short.|||Nuclear localization signal|||Nuclear respiratory factor 1|||Phosphoserine; by CK2|||Required for transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100208|||http://purl.uniprot.org/annotation/VSP_003598|||http://purl.uniprot.org/annotation/VSP_054330|||http://purl.uniprot.org/annotation/VSP_054331
http://togogenome.org/gene/9606:GET4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5D6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Golgi to ER traffic protein 4 homolog|||In CDG2Y; unknown pathological significance.|||In isoform 2.|||Inhibits interaction with BAG6.|||Interacts with BAG6|||N-acetylalanine|||No effect on interaction with BAG6.|||Phosphoserine|||Reduces tail-anchored protein delivery.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228104|||http://purl.uniprot.org/annotation/VAR_088084|||http://purl.uniprot.org/annotation/VAR_088085|||http://purl.uniprot.org/annotation/VSP_017652
http://togogenome.org/gene/9606:SLC25A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z382|||http://purl.uniprot.org/uniprot/A0A0S2Z3G3|||http://purl.uniprot.org/uniprot/F6RGN5|||http://purl.uniprot.org/uniprot/Q9UBX3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In MTDPS19; no protein detected in patient cells.|||In isoform 2.|||Mitochondrial dicarboxylate carrier|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090609|||http://purl.uniprot.org/annotation/VAR_084678|||http://purl.uniprot.org/annotation/VSP_003267
http://togogenome.org/gene/9606:CDV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6R9V8|||http://purl.uniprot.org/uniprot/D6RDN0|||http://purl.uniprot.org/uniprot/D6RFH2|||http://purl.uniprot.org/uniprot/Q9UKY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein CDV3 homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299560|||http://purl.uniprot.org/annotation/VSP_027760|||http://purl.uniprot.org/annotation/VSP_027761|||http://purl.uniprot.org/annotation/VSP_041357|||http://purl.uniprot.org/annotation/VSP_041358|||http://purl.uniprot.org/annotation/VSP_041359
http://togogenome.org/gene/9606:TMC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5K3|||http://purl.uniprot.org/uniprot/B7Z946|||http://purl.uniprot.org/uniprot/F5GYU8|||http://purl.uniprot.org/uniprot/Q6UXY8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||TMC|||Transmembrane channel-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289966|||http://purl.uniprot.org/annotation/VAR_057285|||http://purl.uniprot.org/annotation/VAR_061850|||http://purl.uniprot.org/annotation/VSP_026043|||http://purl.uniprot.org/annotation/VSP_026044|||http://purl.uniprot.org/annotation/VSP_026045|||http://purl.uniprot.org/annotation/VSP_026046
http://togogenome.org/gene/9606:AR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUX9|||http://purl.uniprot.org/uniprot/F1D8N5|||http://purl.uniprot.org/uniprot/G4VV16|||http://purl.uniprot.org/uniprot/P10275|||http://purl.uniprot.org/uniprot/Q9NUA2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  20% lower transactivation capacity.|||Alters receptor specificity, so that transcription is activated by the antiandrogen cyproterone acetate.|||Androgen receptor|||Decrease in CSK-induced phosphorylation.|||Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-269.|||Decrease of CSK-induced phosphorylation and phosphorylation by TNK2. Complete loss of TNK2-dependent phosphorylation; when associated with F-365.|||Decrease of CSK-induced phosphorylation.|||Disordered|||Found in prostate cancer.|||Found in prostate cancer; found in bone metastases; alters receptor specificity so that transcription is activated by antiandrogens such as cyproterone acetate.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatest decrease of CSK-induced phosphorylation and inhibition of transcriptional activity induced by EGF.|||In AIS and PAIS.|||In AIS and PAIS; almost complete loss of androgen binding.|||In AIS and PAIS; associated with G-598 in a PAIS patient; loss of DNA-binding activity.|||In AIS and prostate cancer.|||In AIS.|||In AIS; 25% androgen binding.|||In AIS; abolishes dimerization.|||In AIS; almost complete loss of androgen binding and transcription activation.|||In AIS; almost complete loss of transcription activation.|||In AIS; frequent mutation; loss of androgen binding.|||In AIS; loss of androgen binding and of transactivation.|||In AIS; loss of androgen binding.|||In AIS; loss of transactivation.|||In AIS; low androgen binding and transactivation.|||In AIS; reduced transcription and DNA binding.|||In AIS; strongly reduced transcription activation.|||In AIS; unknown pathological significance.|||In PAIS and AIS.|||In PAIS and breast cancer.|||In PAIS and breast cancer; defective nuclear localization.|||In PAIS and prostate cancer.|||In PAIS and prostate cancer; partial loss of androgen binding.|||In PAIS, AIS and prostate cancer; reduced transcription activation.|||In PAIS.|||In PAIS; 50% reduction in transactivation.|||In PAIS; associated with P-618 in a PAIS patient; normal androgen binding; does not activate transcription; impairs DNA binding.|||In a patient with isolated hypospadias.|||In a patient with severe hypospadias.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In prostate cancer.|||In prostate cancer; found in bone metastases.|||In prostate cancer; gain in function.|||In prostate cancer; increases affinity for testosterone and androgen sensitivity; increased transcription activation.|||In prostate cancer; increases transcription activation.|||In prostate cancer; loss of DNA binding; somatic mutation.|||In prostate cancer; somatic mutation.|||Interaction with CCAR1|||Interaction with HIPK3|||Interaction with KAT7|||Interaction with LPXN|||Interaction with ZNF318|||Interaction with coactivator FXXLF and FXXFY motifs|||Interaction with coactivator LXXL and FXXFY motifs|||Loss of transcription activation in the presence of androgen and of interaction with NCOA2.|||Loss of transcription activation in the presence of androgen.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Partially prevents ubiquitination by RNF6.|||Phosphoserine|||Phosphoserine; by CDK9|||Phosphoserine; by STK4/MST1|||Phosphotyrosine; by CSK|||Phosphotyrosine; by CSK and TNK2|||Polar residues|||Prevents ubiquitination by RNF6. Prevents AR transcriptional activation by RNF14 in absence of hormone.|||Reduced cell growth.|||Reduced transcription activation in the presence of androgen.|||Strongly decreased transcription activation in the presence of androgen.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053704|||http://purl.uniprot.org/annotation/VAR_004679|||http://purl.uniprot.org/annotation/VAR_004680|||http://purl.uniprot.org/annotation/VAR_004681|||http://purl.uniprot.org/annotation/VAR_004684|||http://purl.uniprot.org/annotation/VAR_004685|||http://purl.uniprot.org/annotation/VAR_004686|||http://purl.uniprot.org/annotation/VAR_004687|||http://purl.uniprot.org/annotation/VAR_004688|||http://purl.uniprot.org/annotation/VAR_004689|||http://purl.uniprot.org/annotation/VAR_004690|||http://purl.uniprot.org/annotation/VAR_004691|||http://purl.uniprot.org/annotation/VAR_004692|||http://purl.uniprot.org/annotation/VAR_004693|||http://purl.uniprot.org/annotation/VAR_004694|||http://purl.uniprot.org/annotation/VAR_004695|||http://purl.uniprot.org/annotation/VAR_004696|||http://purl.uniprot.org/annotation/VAR_004697|||http://purl.uniprot.org/annotation/VAR_004698|||http://purl.uniprot.org/annotation/VAR_004699|||http://purl.uniprot.org/annotation/VAR_004700|||http://purl.uniprot.org/annotation/VAR_004701|||http://purl.uniprot.org/annotation/VAR_004702|||http://purl.uniprot.org/annotation/VAR_004703|||http://purl.uniprot.org/annotation/VAR_004704|||http://purl.uniprot.org/annotation/VAR_004705|||http://purl.uniprot.org/annotation/VAR_004707|||http://purl.uniprot.org/annotation/VAR_004708|||http://purl.uniprot.org/annotation/VAR_004709|||http://purl.uniprot.org/annotation/VAR_004710|||http://purl.uniprot.org/annotation/VAR_004711|||http://purl.uniprot.org/annotation/VAR_004712|||http://purl.uniprot.org/annotation/VAR_004713|||http://purl.uniprot.org/annotation/VAR_004714|||http://purl.uniprot.org/annotation/VAR_004715|||http://purl.uniprot.org/annotation/VAR_004716|||http://purl.uniprot.org/annotation/VAR_004717|||http://purl.uniprot.org/annotation/VAR_004718|||http://purl.uniprot.org/annotation/VAR_004719|||http://purl.uniprot.org/annotation/VAR_004720|||http://purl.uniprot.org/annotation/VAR_004721|||http://purl.uniprot.org/annotation/VAR_004722|||http://purl.uniprot.org/annotation/VAR_004723|||http://purl.uniprot.org/annotation/VAR_004724|||http://purl.uniprot.org/annotation/VAR_004725|||http://purl.uniprot.org/annotation/VAR_004726|||http://purl.uniprot.org/annotation/VAR_004727|||http://purl.uniprot.org/annotation/VAR_004728|||http://purl.uniprot.org/annotation/VAR_004729|||http://purl.uniprot.org/annotation/VAR_004730|||http://purl.uniprot.org/annotation/VAR_004731|||http://purl.uniprot.org/annotation/VAR_004732|||http://purl.uniprot.org/annotation/VAR_004733|||http://purl.uniprot.org/annotation/VAR_004734|||http://purl.uniprot.org/annotation/VAR_004735|||http://purl.uniprot.org/annotation/VAR_004736|||http://purl.uniprot.org/annotation/VAR_009224|||http://purl.uniprot.org/annotation/VAR_009225|||http://purl.uniprot.org/annotation/VAR_009226|||http://purl.uniprot.org/annotation/VAR_009227|||http://purl.uniprot.org/annotation/VAR_009228|||http://purl.uniprot.org/annotation/VAR_009229|||http://purl.uniprot.org/annotation/VAR_009711|||http://purl.uniprot.org/annotation/VAR_009712|||http://purl.uniprot.org/annotation/VAR_009713|||http://purl.uniprot.org/annotation/VAR_009714|||http://purl.uniprot.org/annotation/VAR_009715|||http://purl.uniprot.org/annotation/VAR_009716|||http://purl.uniprot.org/annotation/VAR_009717|||http://purl.uniprot.org/annotation/VAR_009718|||http://purl.uniprot.org/annotation/VAR_009719|||http://purl.uniprot.org/annotation/VAR_009720|||http://purl.uniprot.org/annotation/VAR_009721|||http://purl.uniprot.org/annotation/VAR_009722|||http://purl.uniprot.org/annotation/VAR_009723|||http://purl.uniprot.org/annotation/VAR_009725|||http://purl.uniprot.org/annotation/VAR_009726|||http://purl.uniprot.org/annotation/VAR_009727|||http://purl.uniprot.org/annotation/VAR_009728|||http://purl.uniprot.org/annotation/VAR_009729|||http://purl.uniprot.org/annotation/VAR_009730|||http://purl.uniprot.org/annotation/VAR_009731|||http://purl.uniprot.org/annotation/VAR_009732|||http://purl.uniprot.org/annotation/VAR_009733|||http://purl.uniprot.org/annotation/VAR_009734|||http://purl.uniprot.org/annotation/VAR_009735|||http://purl.uniprot.org/annotation/VAR_009736|||http://purl.uniprot.org/annotation/VAR_009737|||http://purl.uniprot.org/annotation/VAR_009738|||http://purl.uniprot.org/annotation/VAR_009739|||http://purl.uniprot.org/annotation/VAR_009740|||http://purl.uniprot.org/annotation/VAR_009741|||http://purl.uniprot.org/annotation/VAR_009742|||http://purl.uniprot.org/annotation/VAR_009743|||http://purl.uniprot.org/annotation/VAR_009744|||http://purl.uniprot.org/annotation/VAR_009745|||http://purl.uniprot.org/annotation/VAR_009746|||http://purl.uniprot.org/annotation/VAR_009747|||http://purl.uniprot.org/annotation/VAR_009748|||http://purl.uniprot.org/annotation/VAR_009749|||http://purl.uniprot.org/annotation/VAR_009750|||http://purl.uniprot.org/annotation/VAR_009751|||http://purl.uniprot.org/annotation/VAR_009752|||http://purl.uniprot.org/annotation/VAR_009753|||http://purl.uniprot.org/annotation/VAR_009754|||http://purl.uniprot.org/annotation/VAR_009755|||http://purl.uniprot.org/annotation/VAR_009756|||http://purl.uniprot.org/annotation/VAR_009757|||http://purl.uniprot.org/annotation/VAR_009758|||http://purl.uniprot.org/annotation/VAR_009760|||http://purl.uniprot.org/annotation/VAR_009761|||http://purl.uniprot.org/annotation/VAR_009762|||http://purl.uniprot.org/annotation/VAR_009763|||http://purl.uniprot.org/annotation/VAR_009764|||http://purl.uniprot.org/annotation/VAR_009765|||http://purl.uniprot.org/annotation/VAR_009766|||http://purl.uniprot.org/annotation/VAR_009767|||http://purl.uniprot.org/annotation/VAR_009768|||http://purl.uniprot.org/annotation/VAR_009769|||http://purl.uniprot.org/annotation/VAR_009770|||http://purl.uniprot.org/annotation/VAR_009771|||http://purl.uniprot.org/annotation/VAR_009772|||http://purl.uniprot.org/annotation/VAR_009773|||http://purl.uniprot.org/annotation/VAR_009774|||http://purl.uniprot.org/annotation/VAR_009775|||http://purl.uniprot.org/annotation/VAR_009776|||http://purl.uniprot.org/annotation/VAR_009777|||http://purl.uniprot.org/annotation/VAR_009778|||http://purl.uniprot.org/annotation/VAR_009779|||http://purl.uniprot.org/annotation/VAR_009780|||http://purl.uniprot.org/annotation/VAR_009781|||http://purl.uniprot.org/annotation/VAR_009782|||http://purl.uniprot.org/annotation/VAR_009783|||http://purl.uniprot.org/annotation/VAR_009784|||http://purl.uniprot.org/annotation/VAR_009785|||http://purl.uniprot.org/annotation/VAR_009786|||http://purl.uniprot.org/annotation/VAR_009787|||http://purl.uniprot.org/annotation/VAR_009788|||http://purl.uniprot.org/annotation/VAR_009789|||http://purl.uniprot.org/annotation/VAR_009790|||http://purl.uniprot.org/annotation/VAR_009791|||http://purl.uniprot.org/annotation/VAR_009792|||http://purl.uniprot.org/annotation/VAR_009793|||http://purl.uniprot.org/annotation/VAR_009794|||http://purl.uniprot.org/annotation/VAR_009795|||http://purl.uniprot.org/annotation/VAR_009796|||http://purl.uniprot.org/annotation/VAR_009797|||http://purl.uniprot.org/annotation/VAR_009798|||http://purl.uniprot.org/annotation/VAR_009799|||http://purl.uniprot.org/annotation/VAR_009800|||http://purl.uniprot.org/annotation/VAR_009801|||http://purl.uniprot.org/annotation/VAR_009802|||http://purl.uniprot.org/annotation/VAR_009803|||http://purl.uniprot.org/annotation/VAR_009804|||http://purl.uniprot.org/annotation/VAR_009805|||http://purl.uniprot.org/annotation/VAR_009806|||http://purl.uniprot.org/annotation/VAR_009807|||http://purl.uniprot.org/annotation/VAR_009808|||http://purl.uniprot.org/annotation/VAR_009809|||http://purl.uniprot.org/annotation/VAR_009810|||http://purl.uniprot.org/annotation/VAR_009811|||http://purl.uniprot.org/annotation/VAR_009812|||http://purl.uniprot.org/annotation/VAR_009813|||http://purl.uniprot.org/annotation/VAR_009814|||http://purl.uniprot.org/annotation/VAR_009815|||http://purl.uniprot.org/annotation/VAR_009816|||http://purl.uniprot.org/annotation/VAR_009817|||http://purl.uniprot.org/annotation/VAR_009818|||http://purl.uniprot.org/annotation/VAR_009819|||http://purl.uniprot.org/annotation/VAR_009820|||http://purl.uniprot.org/annotation/VAR_009821|||http://purl.uniprot.org/annotation/VAR_009822|||http://purl.uniprot.org/annotation/VAR_009823|||http://purl.uniprot.org/annotation/VAR_009824|||http://purl.uniprot.org/annotation/VAR_009825|||http://purl.uniprot.org/annotation/VAR_009826|||http://purl.uniprot.org/annotation/VAR_009827|||http://purl.uniprot.org/annotation/VAR_009828|||http://purl.uniprot.org/annotation/VAR_009829|||http://purl.uniprot.org/annotation/VAR_009830|||http://purl.uniprot.org/annotation/VAR_009831|||http://purl.uniprot.org/annotation/VAR_009832|||http://purl.uniprot.org/annotation/VAR_009833|||http://purl.uniprot.org/annotation/VAR_009834|||http://purl.uniprot.org/annotation/VAR_009835|||http://purl.uniprot.org/annotation/VAR_009836|||http://purl.uniprot.org/annotation/VAR_009837|||http://purl.uniprot.org/annotation/VAR_009838|||http://purl.uniprot.org/annotation/VAR_009839|||http://purl.uniprot.org/annotation/VAR_009840|||http://purl.uniprot.org/annotation/VAR_009841|||http://purl.uniprot.org/annotation/VAR_009842|||http://purl.uniprot.org/annotation/VAR_009843|||http://purl.uniprot.org/annotation/VAR_009844|||http://purl.uniprot.org/annotation/VAR_009845|||http://purl.uniprot.org/annotation/VAR_009846|||http://purl.uniprot.org/annotation/VAR_009847|||http://purl.uniprot.org/annotation/VAR_009848|||http://purl.uniprot.org/annotation/VAR_009849|||http://purl.uniprot.org/annotation/VAR_009850|||http://purl.uniprot.org/annotation/VAR_009851|||http://purl.uniprot.org/annotation/VAR_009852|||http://purl.uniprot.org/annotation/VAR_009853|||http://purl.uniprot.org/annotation/VAR_009854|||http://purl.uniprot.org/annotation/VAR_009855|||http://purl.uniprot.org/annotation/VAR_009856|||http://purl.uniprot.org/annotation/VAR_009857|||http://purl.uniprot.org/annotation/VAR_009858|||http://purl.uniprot.org/annotation/VAR_009859|||http://purl.uniprot.org/annotation/VAR_009860|||http://purl.uniprot.org/annotation/VAR_009861|||http://purl.uniprot.org/annotation/VAR_009862|||http://purl.uniprot.org/annotation/VAR_009863|||http://purl.uniprot.org/annotation/VAR_013474|||http://purl.uniprot.org/annotation/VAR_013475|||http://purl.uniprot.org/annotation/VAR_013476|||http://purl.uniprot.org/annotation/VAR_013477|||http://purl.uniprot.org/annotation/VAR_013478|||http://purl.uniprot.org/annotation/VAR_013479|||http://purl.uniprot.org/annotation/VAR_013480|||http://purl.uniprot.org/annotation/VSP_036889|||http://purl.uniprot.org/annotation/VSP_036890|||http://purl.uniprot.org/annotation/VSP_058166|||http://purl.uniprot.org/annotation/VSP_058167|||http://purl.uniprot.org/annotation/VSP_058168|||http://purl.uniprot.org/annotation/VSP_058169
http://togogenome.org/gene/9606:OAZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54368                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Ornithine decarboxylase antizyme 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220849|||http://purl.uniprot.org/annotation/VAR_022215|||http://purl.uniprot.org/annotation/VAR_022216|||http://purl.uniprot.org/annotation/VAR_022217|||http://purl.uniprot.org/annotation/VAR_022218|||http://purl.uniprot.org/annotation/VAR_022219
http://togogenome.org/gene/9606:USP17L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTZ2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253963
http://togogenome.org/gene/9606:DPP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCJ8|||http://purl.uniprot.org/uniprot/B4DKB5|||http://purl.uniprot.org/uniprot/Q0GLB7|||http://purl.uniprot.org/uniprot/Q0GLB9|||http://purl.uniprot.org/uniprot/Q8N608                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes sorting to the cell surface and dimerization.|||Cytoplasmic|||Dipeptidylpeptidase IV N-terminal|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactive dipeptidyl peptidase 10|||Mediates effects on KCND2|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122417|||http://purl.uniprot.org/annotation/VAR_057061|||http://purl.uniprot.org/annotation/VAR_057062|||http://purl.uniprot.org/annotation/VAR_059759|||http://purl.uniprot.org/annotation/VSP_013873|||http://purl.uniprot.org/annotation/VSP_044466|||http://purl.uniprot.org/annotation/VSP_047152
http://togogenome.org/gene/9606:MRPS30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP92                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL65                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087720|||http://purl.uniprot.org/annotation/VAR_028023|||http://purl.uniprot.org/annotation/VAR_052048
http://togogenome.org/gene/9606:ZNF132                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ54|||http://purl.uniprot.org/uniprot/P52740                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 132                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047416|||http://purl.uniprot.org/annotation/VAR_012024|||http://purl.uniprot.org/annotation/VAR_047229|||http://purl.uniprot.org/annotation/VSP_035665
http://togogenome.org/gene/9606:SSTR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32745                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Somatostatin receptor type 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070124|||http://purl.uniprot.org/annotation/VAR_011853|||http://purl.uniprot.org/annotation/VAR_020072|||http://purl.uniprot.org/annotation/VAR_029219|||http://purl.uniprot.org/annotation/VAR_029220|||http://purl.uniprot.org/annotation/VAR_029221|||http://purl.uniprot.org/annotation/VAR_049440
http://togogenome.org/gene/9606:CRYAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3B9|||http://purl.uniprot.org/uniprot/P02511|||http://purl.uniprot.org/uniprot/V9HW27                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-crystallin B chain|||Basic and acidic residues|||Disordered|||In CMD1II.|||In CTRCT16; unknown pathological significance.|||In MFM2.|||In MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC; cytoplasmic aggregation.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; partial|||O-linked (GlcNAc) threonine|||Phosphoserine|||Probable disease-associated variant found in patients with restrictive cardiomyopathy; reduces CRYAB and DES localization at the Z-bands and the intercalated disk in the myocardium; cytoplasmic aggregations of CRYAB and DES.|||SHSP|||Susceptible to oxidation|||With 1 phosphate group.|||With 2 phosphate groups.|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125907|||http://purl.uniprot.org/annotation/VAR_007899|||http://purl.uniprot.org/annotation/VAR_014607|||http://purl.uniprot.org/annotation/VAR_014608|||http://purl.uniprot.org/annotation/VAR_069528|||http://purl.uniprot.org/annotation/VAR_070035|||http://purl.uniprot.org/annotation/VAR_070036|||http://purl.uniprot.org/annotation/VAR_079841|||http://purl.uniprot.org/annotation/VAR_084806|||http://purl.uniprot.org/annotation/VAR_084807
http://togogenome.org/gene/9606:APOE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3D5|||http://purl.uniprot.org/uniprot/P02649                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 22 AA approximate tandem repeats|||Apolipoprotein E|||Changes the plasma lipoprotein distribution of ApoE4 to the HDL.|||Confirmed at protein level.|||Decreased binding to LDL receptor.|||Found in a patient with hypercholesterolemia; unknown pathological significance; ApoE1 Weisgraber.|||Found in a patient with hypercholesterolemia; unknown pathological significance; ApoE4 Freiburg.|||Homooligomerization|||In ApoE1 HE; requires 2 nucleotide substitutions.|||In ApoE2 Dunedin.|||In ApoE2 Fukuoka.|||In ApoE2 WG.|||In ApoE2-type; no hyperlipidemia.|||In ApoE3 Basel.|||In ApoE3 Freiburg.|||In ApoE3 HB.|||In ApoE3*.|||In ApoE3*; decreased binding to LDL receptor.|||In ApoE4 HG.|||In ApoE4 PD.|||In ApoE5 Frankfurt.|||In ApoE5-type; no hyperlipidemia.|||In ApoE5; associated with hyperlipoproteinemia and atherosclerosis; increased binding to LDL receptor.|||In HLPP3 and AD2; ApoE4, ApoE3 Leiden, ApoE3**, ApoE5-Frankfurt and ApoE5-type; ApoE3 Leiden and ApoE3** are associated with HLPP3; ApoE4 is associated with AD2; changed protein structure; no effect on binding to LDL receptor; decreased association with HDL and enrichment in VLDL and IDL; may prevent the interaction with MAP2 and MAPT; changed interaction with APP/A4 amyloid-beta peptide; increased ability to induce APP transcription; increased C-terminal proteolytic processing in neurons; decreased function in neurite outgrowth; ApoE4 is associated with higher susceptibility to SARS-CoV-2 infection in neurons and astrocytes.|||In HLPP3; ApoE1 Harrisburg; decreased binding to LDL receptor; probable dominant negative effect; decreased in vitro binding to heparin.|||In HLPP3; ApoE2 Christchurch; decreased binding to LDL receptor.|||In HLPP3; ApoE2**.|||In HLPP3; ApoE2, ApoE2 Fukuoka, ApoE1 Weisgraber and ApoE3**; ApoE3** is associated with HLPP3; changed protein structure; decreased binding to LDLR and other lipoprotein receptors; decreased in vitro binding to heparin; no effect on distribution among plasma lipoproteins.|||In HLPP3; ApoE2-type.|||In HLPP3; ApoE3 Leiden; no effect on glycosylation.|||In HLPP3; ApoE3 Washington.|||In HLPP3; ApoE3**.|||In HLPP3; ApoE4 Philadelphia, ApoE5 French-Canadian and ApoE5-type; only ApoE4 Philadelphia is associated with HLPP3.|||In HLPP3; ApoE7 Suita.|||In HLPP3; also found in a patient with hypercholesterolemia; ApoE4 Philadelphia and ApoE2-type.|||In HLPP3; unknown pathological significance; ApoEKochi.|||In LPG; ApoE2 Kyoto.|||In LPG; ApoE2 Sendai; decreased binding to LDL receptor; induces intraglomerular deposition of ApoE-containing lipoproteins.|||In SBHD; also found in patients with a diagnosis of familial combined hyperlipidemia.|||Increased binding to LDL receptor; when associated with A-167.|||Increased binding to LDL receptor; when associated with R-157.|||LDL and other lipoprotein receptors binding|||Lipid-binding and lipoprotein association|||Loss of O-glycosylation.|||Methionine sulfoxide|||N-linked (Glc) (glycation) lysine|||No effect on plasma lipoprotein distribution.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine; by FAM20C|||Restores the LDL receptor binding activity of ApoE2.|||Specificity for association with VLDL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001987|||http://purl.uniprot.org/annotation/PRO_5006608239|||http://purl.uniprot.org/annotation/VAR_000645|||http://purl.uniprot.org/annotation/VAR_000646|||http://purl.uniprot.org/annotation/VAR_000647|||http://purl.uniprot.org/annotation/VAR_000648|||http://purl.uniprot.org/annotation/VAR_000649|||http://purl.uniprot.org/annotation/VAR_000650|||http://purl.uniprot.org/annotation/VAR_000651|||http://purl.uniprot.org/annotation/VAR_000652|||http://purl.uniprot.org/annotation/VAR_000653|||http://purl.uniprot.org/annotation/VAR_000654|||http://purl.uniprot.org/annotation/VAR_000655|||http://purl.uniprot.org/annotation/VAR_000656|||http://purl.uniprot.org/annotation/VAR_000657|||http://purl.uniprot.org/annotation/VAR_000658|||http://purl.uniprot.org/annotation/VAR_000659|||http://purl.uniprot.org/annotation/VAR_000660|||http://purl.uniprot.org/annotation/VAR_000661|||http://purl.uniprot.org/annotation/VAR_000662|||http://purl.uniprot.org/annotation/VAR_000663|||http://purl.uniprot.org/annotation/VAR_000664|||http://purl.uniprot.org/annotation/VAR_000665|||http://purl.uniprot.org/annotation/VAR_000666|||http://purl.uniprot.org/annotation/VAR_000667|||http://purl.uniprot.org/annotation/VAR_000668|||http://purl.uniprot.org/annotation/VAR_000669|||http://purl.uniprot.org/annotation/VAR_000670|||http://purl.uniprot.org/annotation/VAR_000671|||http://purl.uniprot.org/annotation/VAR_000672|||http://purl.uniprot.org/annotation/VAR_014114|||http://purl.uniprot.org/annotation/VAR_016789|||http://purl.uniprot.org/annotation/VAR_035015|||http://purl.uniprot.org/annotation/VAR_042734|||http://purl.uniprot.org/annotation/VAR_042735|||http://purl.uniprot.org/annotation/VAR_081136
http://togogenome.org/gene/9606:JAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78504|||http://purl.uniprot.org/uniprot/Q99740                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||DSL|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 10|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13|||EGF-like 14|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 2; atypical|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9|||Extracellular|||Found in a patient with pulmonary stenosis; unknown pathological significance; the mutant is able to activate Notch signaling.|||Found in patient with tetralogy of Fallot and pulmonary stenosis; unknown pathological significance.|||Helical|||Important for interaction with NOTCH1|||In ALGS1.|||In ALGS1; loss of expression at the cell membrane.|||In ALGS1; the mutant is unable to activate Notch signaling.|||In ALGS1; unknown pathological significance.|||In CMT2HH; decreased glycosylation; decreased expression at the cell membrane due to partial retention in the endoplasmic reticulum.|||In DCHE; the mutant is unable to activate Notch signaling.|||In TOF; temperature sensitive mutation; the protein is abnormally glycosylated and retained intracellularly; unable to activate Notch signaling.|||In TOF; the mutant is unable to activate Notch signaling.|||In biliary atresia; extrahepatic.|||In isoform 2.|||Likely benign variant; the mutant is able to activate Notch signaling.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein jagged-1|||Strongly reduced NOTCH1 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007625|||http://purl.uniprot.org/annotation/VAR_013186|||http://purl.uniprot.org/annotation/VAR_013187|||http://purl.uniprot.org/annotation/VAR_013188|||http://purl.uniprot.org/annotation/VAR_013189|||http://purl.uniprot.org/annotation/VAR_013190|||http://purl.uniprot.org/annotation/VAR_013191|||http://purl.uniprot.org/annotation/VAR_013192|||http://purl.uniprot.org/annotation/VAR_013193|||http://purl.uniprot.org/annotation/VAR_013194|||http://purl.uniprot.org/annotation/VAR_013195|||http://purl.uniprot.org/annotation/VAR_013196|||http://purl.uniprot.org/annotation/VAR_013197|||http://purl.uniprot.org/annotation/VAR_013198|||http://purl.uniprot.org/annotation/VAR_013199|||http://purl.uniprot.org/annotation/VAR_013200|||http://purl.uniprot.org/annotation/VAR_013201|||http://purl.uniprot.org/annotation/VAR_013202|||http://purl.uniprot.org/annotation/VAR_013203|||http://purl.uniprot.org/annotation/VAR_013204|||http://purl.uniprot.org/annotation/VAR_013205|||http://purl.uniprot.org/annotation/VAR_013206|||http://purl.uniprot.org/annotation/VAR_013207|||http://purl.uniprot.org/annotation/VAR_026296|||http://purl.uniprot.org/annotation/VAR_026297|||http://purl.uniprot.org/annotation/VAR_026298|||http://purl.uniprot.org/annotation/VAR_026299|||http://purl.uniprot.org/annotation/VAR_026300|||http://purl.uniprot.org/annotation/VAR_026301|||http://purl.uniprot.org/annotation/VAR_026302|||http://purl.uniprot.org/annotation/VAR_026303|||http://purl.uniprot.org/annotation/VAR_026304|||http://purl.uniprot.org/annotation/VAR_026305|||http://purl.uniprot.org/annotation/VAR_026306|||http://purl.uniprot.org/annotation/VAR_026307|||http://purl.uniprot.org/annotation/VAR_026308|||http://purl.uniprot.org/annotation/VAR_026309|||http://purl.uniprot.org/annotation/VAR_026310|||http://purl.uniprot.org/annotation/VAR_026311|||http://purl.uniprot.org/annotation/VAR_026312|||http://purl.uniprot.org/annotation/VAR_026313|||http://purl.uniprot.org/annotation/VAR_026314|||http://purl.uniprot.org/annotation/VAR_026315|||http://purl.uniprot.org/annotation/VAR_026316|||http://purl.uniprot.org/annotation/VAR_026317|||http://purl.uniprot.org/annotation/VAR_026318|||http://purl.uniprot.org/annotation/VAR_026319|||http://purl.uniprot.org/annotation/VAR_026320|||http://purl.uniprot.org/annotation/VAR_026321|||http://purl.uniprot.org/annotation/VAR_026322|||http://purl.uniprot.org/annotation/VAR_026323|||http://purl.uniprot.org/annotation/VAR_026324|||http://purl.uniprot.org/annotation/VAR_026325|||http://purl.uniprot.org/annotation/VAR_026326|||http://purl.uniprot.org/annotation/VAR_026327|||http://purl.uniprot.org/annotation/VAR_026328|||http://purl.uniprot.org/annotation/VAR_026329|||http://purl.uniprot.org/annotation/VAR_026330|||http://purl.uniprot.org/annotation/VAR_026331|||http://purl.uniprot.org/annotation/VAR_026332|||http://purl.uniprot.org/annotation/VAR_026333|||http://purl.uniprot.org/annotation/VAR_026334|||http://purl.uniprot.org/annotation/VAR_026335|||http://purl.uniprot.org/annotation/VAR_026336|||http://purl.uniprot.org/annotation/VAR_026337|||http://purl.uniprot.org/annotation/VAR_048985|||http://purl.uniprot.org/annotation/VAR_071513|||http://purl.uniprot.org/annotation/VAR_080875|||http://purl.uniprot.org/annotation/VAR_080876|||http://purl.uniprot.org/annotation/VAR_080877|||http://purl.uniprot.org/annotation/VAR_086413|||http://purl.uniprot.org/annotation/VAR_086414|||http://purl.uniprot.org/annotation/VSP_056532
http://togogenome.org/gene/9606:MYLIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TIA5|||http://purl.uniprot.org/uniprot/Q8WY64                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes autoubiquitination.|||Abolishes ubiquitin ligase activity.|||Critical for homodimerization|||E3 ubiquitin-protein ligase MYLIP|||FERM|||In isoform 2.|||Inhibits LDLR degradation.|||RING-type|||Unable to clear LDLR from the plasma membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055972|||http://purl.uniprot.org/annotation/VAR_019805|||http://purl.uniprot.org/annotation/VSP_011828|||http://purl.uniprot.org/annotation/VSP_011829
http://togogenome.org/gene/9606:LAMTOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Q5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In M6 mutant; impaired assembly of the Ragulator complex.|||In M7 mutant; impaired association with Rag GTPases.|||In isoform 2.|||In isoform 3.|||Ragulator complex protein LAMTOR2|||Required for location at endosomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220960|||http://purl.uniprot.org/annotation/VSP_036543|||http://purl.uniprot.org/annotation/VSP_040980
http://togogenome.org/gene/9606:STAG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6W5U7|||http://purl.uniprot.org/uniprot/Q9UJ98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Cohesin subunit SA-3|||Disordered|||In POF8 and SPGF61.|||In POF8.|||In SPGF61.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||SCD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120188|||http://purl.uniprot.org/annotation/VAR_086738|||http://purl.uniprot.org/annotation/VAR_086739|||http://purl.uniprot.org/annotation/VAR_086740|||http://purl.uniprot.org/annotation/VAR_086741|||http://purl.uniprot.org/annotation/VSP_006996|||http://purl.uniprot.org/annotation/VSP_006997|||http://purl.uniprot.org/annotation/VSP_054742
http://togogenome.org/gene/9606:LRRC37B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSJ3|||http://purl.uniprot.org/uniprot/B4DZ43|||http://purl.uniprot.org/uniprot/F5H5K1|||http://purl.uniprot.org/uniprot/Q96QE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRC37A/B like protein 1 C-terminal|||Leucine-rich repeat-containing protein 37 N-terminal|||Leucine-rich repeat-containing protein 37B|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232653|||http://purl.uniprot.org/annotation/VSP_054513
http://togogenome.org/gene/9606:TSSK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0ZT99|||http://purl.uniprot.org/uniprot/Q96PF2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||May be associated with infertility.|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086768|||http://purl.uniprot.org/annotation/VAR_041241|||http://purl.uniprot.org/annotation/VAR_041242|||http://purl.uniprot.org/annotation/VAR_041243|||http://purl.uniprot.org/annotation/VAR_041244|||http://purl.uniprot.org/annotation/VAR_051677|||http://purl.uniprot.org/annotation/VAR_059770
http://togogenome.org/gene/9606:PTPN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3V3|||http://purl.uniprot.org/uniprot/B7Z9V1|||http://purl.uniprot.org/uniprot/B7ZA03|||http://purl.uniprot.org/uniprot/P26045|||http://purl.uniprot.org/uniprot/Q8N4S3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FERM|||In isoform 2 and isoform 3.|||In isoform 3.|||PDZ|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219433|||http://purl.uniprot.org/annotation/VAR_055252|||http://purl.uniprot.org/annotation/VAR_055253|||http://purl.uniprot.org/annotation/VAR_055254|||http://purl.uniprot.org/annotation/VAR_055255|||http://purl.uniprot.org/annotation/VAR_055256|||http://purl.uniprot.org/annotation/VSP_046309|||http://purl.uniprot.org/annotation/VSP_046310
http://togogenome.org/gene/9606:ABT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULW3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Activator of basal transcription 1|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233168
http://togogenome.org/gene/9606:ARF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62330                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor 6|||Abolished lysine-myristoylation, leading to decreased localization to membranes.|||Constitutively active. Inhibits filopodia formation and dendritic branching.|||Constitutively inactivated. Fails to associate with membranes. Does not inhibit filopodia formation.|||Fails to associate with membranes.|||N-myristoyl glycine|||N6-myristoyl lysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207400
http://togogenome.org/gene/9606:SLC22A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4U2R8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of PAH transport activity.|||Cytoplasmic|||Decrease in the level of membrane protein expression and 70 % loss of PAH uptake.|||Decrease in the level of membrane protein expression, 70 % loss of PAH uptake, increased affinity for cidofovir, lower Vmax for PAH, and lower Km and Vmax for cidofovir.|||Disordered|||Extracellular|||Helical|||Important for interaction with cidofovir|||Important for interaction with cidofovir and PAH|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Increase in substrate affinity.|||Loss of membrane protein expression and little uptake of cidofovir.|||Lower Vmax; increase in substrate affinity and increase in the affinity for the nucleoside phosphonate analogs cidofovir, adefovir and tenofovir.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324166|||http://purl.uniprot.org/annotation/VAR_039682|||http://purl.uniprot.org/annotation/VAR_039683|||http://purl.uniprot.org/annotation/VAR_039684|||http://purl.uniprot.org/annotation/VAR_047878|||http://purl.uniprot.org/annotation/VSP_032168|||http://purl.uniprot.org/annotation/VSP_032169
http://togogenome.org/gene/9606:FRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q64ET8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Protein FRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300690|||http://purl.uniprot.org/annotation/VSP_055076
http://togogenome.org/gene/9606:RTN4R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZR6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Decreases interaction with MAG; when associated with D-277.|||Decreases interaction with MAG; when associated with D-279.|||Disordered|||GPI-anchor amidated serine|||Impaired ganglioside binding.|||In SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth.|||In SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; decreased interaction with MAG and OMG; no effect on interaction with RTN4.|||In SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; does not affect interaction with MAG, RTN4 and OMG.|||In SCZD; associated with disease susceptibility; unable to mediate down-regulation of axonal growth; does not affect interaction with MAG, RTN4, OMG, NGFR and LINGO1.|||In SCZD; unknown pathological significance.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Mildly decreases interaction with MAG.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with MAG.|||Removed in mature form|||Reticulon-4 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022253|||http://purl.uniprot.org/annotation/PRO_0000022254|||http://purl.uniprot.org/annotation/VAR_079154|||http://purl.uniprot.org/annotation/VAR_079155|||http://purl.uniprot.org/annotation/VAR_079224|||http://purl.uniprot.org/annotation/VAR_079225|||http://purl.uniprot.org/annotation/VAR_079226|||http://purl.uniprot.org/annotation/VAR_079227|||http://purl.uniprot.org/annotation/VAR_079228|||http://purl.uniprot.org/annotation/VAR_079229|||http://purl.uniprot.org/annotation/VAR_079230|||http://purl.uniprot.org/annotation/VAR_079231|||http://purl.uniprot.org/annotation/VAR_079232|||http://purl.uniprot.org/annotation/VAR_079233|||http://purl.uniprot.org/annotation/VAR_079234|||http://purl.uniprot.org/annotation/VAR_079235|||http://purl.uniprot.org/annotation/VAR_079236|||http://purl.uniprot.org/annotation/VAR_079237
http://togogenome.org/gene/9606:ARMH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUU6|||http://purl.uniprot.org/uniprot/Q5T2E6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Armadillo-like helical|||Armadillo-like helical domain-containing protein 3|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284515|||http://purl.uniprot.org/annotation/VSP_024552|||http://purl.uniprot.org/annotation/VSP_024553|||http://purl.uniprot.org/annotation/VSP_024554
http://togogenome.org/gene/9606:TMED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13445                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Extracellular|||GOLD|||Helical|||In a breast cancer sample; somatic mutation.|||Significant loss of interaction with IL1RL1.|||Transmembrane emp24 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248019|||http://purl.uniprot.org/annotation/VAR_036533
http://togogenome.org/gene/9606:AAGAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PD74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha- and gamma-adaptin-binding protein p34|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058134|||http://purl.uniprot.org/annotation/VAR_021533|||http://purl.uniprot.org/annotation/VSP_054597
http://togogenome.org/gene/9606:RPL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62917                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  (3S)-3-hydroxyhistidine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL2|||No incorporation into translating E.coli polysomes; ribosomes assembled normally. Significantly reduced translational activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129743|||http://purl.uniprot.org/annotation/VAR_019658
http://togogenome.org/gene/9606:EIF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55010                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Arginine finger|||Basic and acidic residues|||Disordered|||Disruption of binding to eIF1 and EIF2-beta (EIF2S2); when associated with 305-D-D-306.|||Disruption of binding to eIF1 and EIF2-beta (EIF2S2); when associated with 347-K-K-348.|||Eukaryotic translation initiation factor 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||Loss of ability to promote hydrolysis of GTP.|||Phosphoserine|||Phosphothreonine|||Pro residues|||W2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212516|||http://purl.uniprot.org/annotation/VAR_036467
http://togogenome.org/gene/9606:PEX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00623                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to activate the E3 ubiquitin-protein ligase activity of PEX10. Abolishes interaction with PEX19; when associated with Q-307.|||Abolishes interaction with PEX19; when associated with W-304.|||Cytoplasmic|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||In PBD-CG3 and PBD3B.|||In PBD-CG3.|||In PBD-CG3; benign variant.|||In PBD3A.|||In PBD3B; attenuates interaction with PEX10 and decreases peroxisomal protein import.|||Peroxisomal matrix|||Peroxisome assembly protein 12|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218610|||http://purl.uniprot.org/annotation/VAR_031998|||http://purl.uniprot.org/annotation/VAR_050495|||http://purl.uniprot.org/annotation/VAR_058389|||http://purl.uniprot.org/annotation/VAR_058390|||http://purl.uniprot.org/annotation/VAR_058391|||http://purl.uniprot.org/annotation/VAR_087150|||http://purl.uniprot.org/annotation/VAR_087151
http://togogenome.org/gene/9606:C12orf56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C12orf56                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320926|||http://purl.uniprot.org/annotation/VSP_031745
http://togogenome.org/gene/9606:GALT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Y7|||http://purl.uniprot.org/uniprot/B2RAT6|||http://purl.uniprot.org/uniprot/P07902                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Galactose-1-phosphate uridyl transferase C-terminal|||Galactose-1-phosphate uridyl transferase N-terminal|||Galactose-1-phosphate uridylyltransferase|||In GALAC1.|||In GALAC1; 15% of normal activity.|||In GALAC1; 18-fold decrease in activity.|||In GALAC1; 2-fold decrease in activity.|||In GALAC1; 3-fold decrease in activity.|||In GALAC1; 4% of normal activity.|||In GALAC1; about 5% of normal galactose uridylyltransferase activity.|||In GALAC1; affects protein stability.|||In GALAC1; allele Duarte; exists as allelic variants Duarte-1 and Duarte-2; Duarte-1 has normal or increased activity; Duarte-2 has activity reduced to about 35-45% of normal.|||In GALAC1; approximately 3% of normal activity.|||In GALAC1; loss of activity.|||In GALAC1; mild.|||In GALAC1; most common mutation; 10% of normal galactose uridylyltransferase activity; impairs protein folding.|||In GALAC1; no enzymatic activity.|||In GALAC1; reduced enzyme activity.|||In GALAC1; results in no detectable protein in the soluble fraction.|||In GALAC1; severe; impairs protein folding; nearly abolishes enzyme activity.|||In GALAC1; strongly reduces galactose uridylyltransferase activity.|||In GALAC1; unstable protein.|||In isoform 2.|||Polar residues|||Tele-UMP-histidine intermediate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000169882|||http://purl.uniprot.org/annotation/VAR_002548|||http://purl.uniprot.org/annotation/VAR_002549|||http://purl.uniprot.org/annotation/VAR_002550|||http://purl.uniprot.org/annotation/VAR_002551|||http://purl.uniprot.org/annotation/VAR_002552|||http://purl.uniprot.org/annotation/VAR_002553|||http://purl.uniprot.org/annotation/VAR_002554|||http://purl.uniprot.org/annotation/VAR_002555|||http://purl.uniprot.org/annotation/VAR_002556|||http://purl.uniprot.org/annotation/VAR_002557|||http://purl.uniprot.org/annotation/VAR_002558|||http://purl.uniprot.org/annotation/VAR_002559|||http://purl.uniprot.org/annotation/VAR_002560|||http://purl.uniprot.org/annotation/VAR_002561|||http://purl.uniprot.org/annotation/VAR_002562|||http://purl.uniprot.org/annotation/VAR_002563|||http://purl.uniprot.org/annotation/VAR_002564|||http://purl.uniprot.org/annotation/VAR_002565|||http://purl.uniprot.org/annotation/VAR_002566|||http://purl.uniprot.org/annotation/VAR_002567|||http://purl.uniprot.org/annotation/VAR_002568|||http://purl.uniprot.org/annotation/VAR_002569|||http://purl.uniprot.org/annotation/VAR_002570|||http://purl.uniprot.org/annotation/VAR_002571|||http://purl.uniprot.org/annotation/VAR_002572|||http://purl.uniprot.org/annotation/VAR_002573|||http://purl.uniprot.org/annotation/VAR_002574|||http://purl.uniprot.org/annotation/VAR_002575|||http://purl.uniprot.org/annotation/VAR_002576|||http://purl.uniprot.org/annotation/VAR_002577|||http://purl.uniprot.org/annotation/VAR_002578|||http://purl.uniprot.org/annotation/VAR_002579|||http://purl.uniprot.org/annotation/VAR_002580|||http://purl.uniprot.org/annotation/VAR_002581|||http://purl.uniprot.org/annotation/VAR_002582|||http://purl.uniprot.org/annotation/VAR_002583|||http://purl.uniprot.org/annotation/VAR_002584|||http://purl.uniprot.org/annotation/VAR_002585|||http://purl.uniprot.org/annotation/VAR_002586|||http://purl.uniprot.org/annotation/VAR_002587|||http://purl.uniprot.org/annotation/VAR_002588|||http://purl.uniprot.org/annotation/VAR_002589|||http://purl.uniprot.org/annotation/VAR_002590|||http://purl.uniprot.org/annotation/VAR_002591|||http://purl.uniprot.org/annotation/VAR_002592|||http://purl.uniprot.org/annotation/VAR_002593|||http://purl.uniprot.org/annotation/VAR_002594|||http://purl.uniprot.org/annotation/VAR_002595|||http://purl.uniprot.org/annotation/VAR_002596|||http://purl.uniprot.org/annotation/VAR_002597|||http://purl.uniprot.org/annotation/VAR_002598|||http://purl.uniprot.org/annotation/VAR_002599|||http://purl.uniprot.org/annotation/VAR_002600|||http://purl.uniprot.org/annotation/VAR_002601|||http://purl.uniprot.org/annotation/VAR_002602|||http://purl.uniprot.org/annotation/VAR_002603|||http://purl.uniprot.org/annotation/VAR_002604|||http://purl.uniprot.org/annotation/VAR_002605|||http://purl.uniprot.org/annotation/VAR_002606|||http://purl.uniprot.org/annotation/VAR_002607|||http://purl.uniprot.org/annotation/VAR_002608|||http://purl.uniprot.org/annotation/VAR_002609|||http://purl.uniprot.org/annotation/VAR_002610|||http://purl.uniprot.org/annotation/VAR_002611|||http://purl.uniprot.org/annotation/VAR_002612|||http://purl.uniprot.org/annotation/VAR_002613|||http://purl.uniprot.org/annotation/VAR_002614|||http://purl.uniprot.org/annotation/VAR_002615|||http://purl.uniprot.org/annotation/VAR_002616|||http://purl.uniprot.org/annotation/VAR_002617|||http://purl.uniprot.org/annotation/VAR_002618|||http://purl.uniprot.org/annotation/VAR_002619|||http://purl.uniprot.org/annotation/VAR_002620|||http://purl.uniprot.org/annotation/VAR_002621|||http://purl.uniprot.org/annotation/VAR_002622|||http://purl.uniprot.org/annotation/VAR_002623|||http://purl.uniprot.org/annotation/VAR_002624|||http://purl.uniprot.org/annotation/VAR_002625|||http://purl.uniprot.org/annotation/VAR_002626|||http://purl.uniprot.org/annotation/VAR_002627|||http://purl.uniprot.org/annotation/VAR_002628|||http://purl.uniprot.org/annotation/VAR_002629|||http://purl.uniprot.org/annotation/VAR_002630|||http://purl.uniprot.org/annotation/VAR_002631|||http://purl.uniprot.org/annotation/VAR_008042|||http://purl.uniprot.org/annotation/VAR_008043|||http://purl.uniprot.org/annotation/VAR_008044|||http://purl.uniprot.org/annotation/VAR_008045|||http://purl.uniprot.org/annotation/VAR_008046|||http://purl.uniprot.org/annotation/VAR_008047|||http://purl.uniprot.org/annotation/VAR_008048|||http://purl.uniprot.org/annotation/VAR_023328|||http://purl.uniprot.org/annotation/VAR_023329|||http://purl.uniprot.org/annotation/VAR_023330|||http://purl.uniprot.org/annotation/VAR_023331|||http://purl.uniprot.org/annotation/VAR_068531|||http://purl.uniprot.org/annotation/VAR_068532|||http://purl.uniprot.org/annotation/VAR_068533|||http://purl.uniprot.org/annotation/VAR_068534|||http://purl.uniprot.org/annotation/VAR_068535|||http://purl.uniprot.org/annotation/VAR_068536|||http://purl.uniprot.org/annotation/VAR_068537|||http://purl.uniprot.org/annotation/VAR_068538|||http://purl.uniprot.org/annotation/VAR_068539|||http://purl.uniprot.org/annotation/VAR_068540|||http://purl.uniprot.org/annotation/VAR_068541|||http://purl.uniprot.org/annotation/VAR_068542|||http://purl.uniprot.org/annotation/VAR_068543|||http://purl.uniprot.org/annotation/VAR_068544|||http://purl.uniprot.org/annotation/VAR_068545|||http://purl.uniprot.org/annotation/VAR_068546|||http://purl.uniprot.org/annotation/VAR_068547|||http://purl.uniprot.org/annotation/VAR_068548|||http://purl.uniprot.org/annotation/VAR_068549|||http://purl.uniprot.org/annotation/VAR_068550|||http://purl.uniprot.org/annotation/VAR_068551|||http://purl.uniprot.org/annotation/VAR_068552|||http://purl.uniprot.org/annotation/VAR_068553|||http://purl.uniprot.org/annotation/VAR_068554|||http://purl.uniprot.org/annotation/VAR_068555|||http://purl.uniprot.org/annotation/VAR_068824|||http://purl.uniprot.org/annotation/VAR_068825|||http://purl.uniprot.org/annotation/VAR_068826|||http://purl.uniprot.org/annotation/VAR_068827|||http://purl.uniprot.org/annotation/VAR_068828|||http://purl.uniprot.org/annotation/VAR_068829|||http://purl.uniprot.org/annotation/VAR_068830|||http://purl.uniprot.org/annotation/VAR_072793|||http://purl.uniprot.org/annotation/VAR_072794|||http://purl.uniprot.org/annotation/VAR_072795|||http://purl.uniprot.org/annotation/VAR_072796|||http://purl.uniprot.org/annotation/VAR_072797|||http://purl.uniprot.org/annotation/VAR_072798|||http://purl.uniprot.org/annotation/VAR_072799|||http://purl.uniprot.org/annotation/VAR_072800|||http://purl.uniprot.org/annotation/VAR_072801|||http://purl.uniprot.org/annotation/VSP_045604|||http://purl.uniprot.org/annotation/VSP_045605
http://togogenome.org/gene/9606:LCN15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWW0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Lipocalin-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317518|||http://purl.uniprot.org/annotation/VAR_059453|||http://purl.uniprot.org/annotation/VAR_059454
http://togogenome.org/gene/9606:PRAMEF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWM3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290163
http://togogenome.org/gene/9606:AGTRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6RW13                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with AGTR1|||Phosphoserine|||Phosphothreonine|||Type-1 angiotensin II receptor-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064735|||http://purl.uniprot.org/annotation/VAR_023075|||http://purl.uniprot.org/annotation/VSP_014839|||http://purl.uniprot.org/annotation/VSP_039290|||http://purl.uniprot.org/annotation/VSP_039291|||http://purl.uniprot.org/annotation/VSP_040406
http://togogenome.org/gene/9606:GTPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00178                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||G1|||G2|||G3|||G4|||G5|||GTP-binding protein 1|||Phosphoserine|||Polar residues|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122469|||http://purl.uniprot.org/annotation/VAR_049496
http://togogenome.org/gene/9606:OR52R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGF1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52R1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150791|||http://purl.uniprot.org/annotation/VAR_059061|||http://purl.uniprot.org/annotation/VAR_059062|||http://purl.uniprot.org/annotation/VAR_059063|||http://purl.uniprot.org/annotation/VAR_059064
http://togogenome.org/gene/9606:PAPPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXP8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SSDA.|||In SSDA; loss of catalytic activity toward IGFBP3 and IGFBP5.|||In isoform 2.|||Loss of activity.|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||Or C-754 with C-783|||Or C-788 with C-771|||Pappalysin-2|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029249|||http://purl.uniprot.org/annotation/PRO_0000029250|||http://purl.uniprot.org/annotation/VAR_051595|||http://purl.uniprot.org/annotation/VAR_051596|||http://purl.uniprot.org/annotation/VAR_086132|||http://purl.uniprot.org/annotation/VAR_086133|||http://purl.uniprot.org/annotation/VSP_012194|||http://purl.uniprot.org/annotation/VSP_012195
http://togogenome.org/gene/9606:PRMT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GT2|||http://purl.uniprot.org/uniprot/Q9NR22                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by autocatalysis|||Decreases homooligomerization and cell membrane localization. No effect on homodimerization, S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-345 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-345 and A-382.|||Disordered|||In isoform 2.|||Loss of cell membrane localization.|||N-myristoyl glycine|||No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-295.|||No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-349.|||No effect on homodimerization but decreased homooligomerization; when associated with A-295 and A-349.|||No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-345. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-345.|||No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-382.|||Omega-N-methylarginine; by autocatalysis|||Protein arginine N-methyltransferase 8|||Removed|||SAM-dependent MTase PRMT-type|||SH3-binding 1|||SH3-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212329|||http://purl.uniprot.org/annotation/VSP_037466
http://togogenome.org/gene/9606:DAZL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK77|||http://purl.uniprot.org/uniprot/Q92904                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DAZ|||Deleted in azoospermia-like|||Disordered|||Homodimerization|||In isoform 2.|||May be associated with susceptibility to spermatogenic failure in Asian individuals; this substitution may lead to affect the DAZL transcript stability and prevent its translation.|||Phosphotyrosine|||RRM|||Severely impaired RNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081559|||http://purl.uniprot.org/annotation/VAR_017780|||http://purl.uniprot.org/annotation/VAR_017781|||http://purl.uniprot.org/annotation/VAR_069231|||http://purl.uniprot.org/annotation/VSP_043208
http://togogenome.org/gene/9606:VAV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR07|||http://purl.uniprot.org/uniprot/B2R8B5|||http://purl.uniprot.org/uniprot/P15498|||http://purl.uniprot.org/uniprot/Q96D37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes transforming activity.|||Calponin-homology (CH)|||DH|||In isoform 2.|||Loss of interaction with SYK.|||PH|||Phorbol-ester/DAG-type|||Phosphotyrosine|||Proto-oncogene vav|||SH2|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080980|||http://purl.uniprot.org/annotation/VAR_051997|||http://purl.uniprot.org/annotation/VSP_047563
http://togogenome.org/gene/9606:ATP10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94823                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Abolishes autophosphorylation and ATPase flippase activity.|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Found in a family with Parkinson disease; unknown pathological significance.|||Found in a patient with early-onset Parkinson disease; unknown pathological significance.|||Found in a patient with early-onset Parkinson disease; unknown pathological significance; has no effect on ATPase flippase activity.|||Found in a patient with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity.|||Found in a patient with early-onset Parkinson disease; unknown pathological significance; loss of protein expression and loss-of-function.|||Found in patients with Parkinson disease; unknown pathological significance.|||Found in patients with early-onset Parkinson disease; unknown pathological significance; impaired ATPase flippase activity.|||Helical|||Impaired ATPase flippase activity.|||In isoform B and isoform C.|||In isoform C.|||Loss of ATPase flippase activity.|||Phospholipid-transporting ATPase VB|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046381|||http://purl.uniprot.org/annotation/VAR_048384|||http://purl.uniprot.org/annotation/VAR_084141|||http://purl.uniprot.org/annotation/VAR_084142|||http://purl.uniprot.org/annotation/VAR_084143|||http://purl.uniprot.org/annotation/VAR_084144|||http://purl.uniprot.org/annotation/VAR_084145|||http://purl.uniprot.org/annotation/VAR_084146|||http://purl.uniprot.org/annotation/VAR_084147|||http://purl.uniprot.org/annotation/VAR_084148|||http://purl.uniprot.org/annotation/VAR_084149|||http://purl.uniprot.org/annotation/VAR_084150|||http://purl.uniprot.org/annotation/VAR_084151|||http://purl.uniprot.org/annotation/VAR_084152|||http://purl.uniprot.org/annotation/VAR_084153|||http://purl.uniprot.org/annotation/VAR_084190|||http://purl.uniprot.org/annotation/VAR_084191|||http://purl.uniprot.org/annotation/VSP_007305|||http://purl.uniprot.org/annotation/VSP_007306|||http://purl.uniprot.org/annotation/VSP_007307
http://togogenome.org/gene/9606:SLITRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Able to promote neurite outgrowth as the wild-type.|||Cytoplasmic|||Disordered|||Does not affect surface expression.|||Extracellular|||Helical|||In TTM; unknown pathological significance; does not affect synaptogenesis.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT 1|||LRRNT 2|||Loss of phosphorylation. Not able to promote neurite outgrowth.|||Phosphoserine; by CK2|||Polar residues|||Probable disease-associated variant found in a patient with obsessive-compulsive disorder; decreased levels of mature protein; decreased localization to the cell membrane surface expression; decreased function in synaptogenesis.|||SLIT and NTRK-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032673|||http://purl.uniprot.org/annotation/VAR_027755|||http://purl.uniprot.org/annotation/VAR_077626|||http://purl.uniprot.org/annotation/VAR_077627|||http://purl.uniprot.org/annotation/VAR_077628|||http://purl.uniprot.org/annotation/VAR_077629
http://togogenome.org/gene/9606:PKN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5Z2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes autophosphorylation and catalytic activity.|||Abolishes catalytic activity.|||Abolishes phosphorylation.|||Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor|||REM-1 1|||REM-1 2|||REM-1 3|||Serine/threonine-protein kinase N3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055725|||http://purl.uniprot.org/annotation/VAR_042346|||http://purl.uniprot.org/annotation/VAR_050565
http://togogenome.org/gene/9606:SPRYD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||B30.2/SPRY|||Disordered|||SPRY domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240854
http://togogenome.org/gene/9606:XPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBH6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EXS|||Extracellular|||Helical|||Important for inositol polyphosphate binding|||In IBGC6; dominant negative; phosphate efflux is impaired; loss of localization to the plasma membrane.|||In IBGC6; phosphate efflux is decreased; present at the plasma membrane.|||In IBGC6; phosphate efflux is impaired; present at the plasma membrane.|||In isoform 2.|||Loss of localization to the plasma membrane.|||Phosphoserine|||Phosphothreonine|||SPX|||Solute carrier family 53 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315853|||http://purl.uniprot.org/annotation/VAR_038350|||http://purl.uniprot.org/annotation/VAR_073840|||http://purl.uniprot.org/annotation/VAR_073841|||http://purl.uniprot.org/annotation/VAR_073842|||http://purl.uniprot.org/annotation/VAR_073843|||http://purl.uniprot.org/annotation/VAR_087987|||http://purl.uniprot.org/annotation/VAR_087988|||http://purl.uniprot.org/annotation/VAR_087989|||http://purl.uniprot.org/annotation/VSP_030748
http://togogenome.org/gene/9606:WDR83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRX9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat domain-containing protein 83                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235263|||http://purl.uniprot.org/annotation/VAR_053410|||http://purl.uniprot.org/annotation/VAR_053411
http://togogenome.org/gene/9606:DEFB131A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59861                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 131A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007006
http://togogenome.org/gene/9606:FIGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HY92                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fidgetin|||Inhibits the ability to sever and depolymerize microtubules.|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250748|||http://purl.uniprot.org/annotation/VAR_027613|||http://purl.uniprot.org/annotation/VAR_027614|||http://purl.uniprot.org/annotation/VAR_027615
http://togogenome.org/gene/9606:ELAVL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14576                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ELAV-like protein 3|||In isoform 2.|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081581|||http://purl.uniprot.org/annotation/VSP_005789
http://togogenome.org/gene/9606:ZNF549                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9A3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 549                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234583|||http://purl.uniprot.org/annotation/VAR_059921|||http://purl.uniprot.org/annotation/VSP_018379
http://togogenome.org/gene/9606:CAMK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YIY3|||http://purl.uniprot.org/uniprot/Q14012                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1|||Calmodulin-binding|||Catalytically inactive form; prevents CDK4 activation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a metastatic melanoma sample; somatic mutation.|||Loss of activation by CaMKK1.|||Nuclear export signal|||Partial activation in absence of CaMKK1.|||Phosphoserine|||Phosphothreonine; by CaMKK1 and CaMKK2|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086076|||http://purl.uniprot.org/annotation/VAR_040596|||http://purl.uniprot.org/annotation/VAR_040597
http://togogenome.org/gene/9606:SULT4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2E1|||http://purl.uniprot.org/uniprot/Q9BR01                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phosphothreonine|||Sulfotransferase|||Sulfotransferase 4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085167|||http://purl.uniprot.org/annotation/VSP_006304
http://togogenome.org/gene/9606:CDX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14627                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein CDX-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048852
http://togogenome.org/gene/9606:RPTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XPR3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Polar residues|||Repetin|||S-100-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144040|||http://purl.uniprot.org/annotation/VAR_059177
http://togogenome.org/gene/9606:OLFM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EIS8|||http://purl.uniprot.org/uniprot/K7EKW2|||http://purl.uniprot.org/uniprot/O95897                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Completely blocks secretion. Also significantly inhibits secretion of OLFM1 and OLFM3.|||In a colorectal cancer sample; somatic mutation; no effect on secretion.|||N-linked (GlcNAc...) asparagine|||No effect on secretion.|||Noelin-2|||Olfactomedin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020078|||http://purl.uniprot.org/annotation/PRO_5032938992|||http://purl.uniprot.org/annotation/VAR_022550|||http://purl.uniprot.org/annotation/VAR_036532|||http://purl.uniprot.org/annotation/VAR_050423
http://togogenome.org/gene/9606:CISH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Cytokine-inducible SH2-containing protein|||Disordered|||In isoform 1B.|||In isoform 1C.|||Pro residues|||SH2|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181231|||http://purl.uniprot.org/annotation/VSP_006194|||http://purl.uniprot.org/annotation/VSP_006195
http://togogenome.org/gene/9606:KLC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0B6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Kinesin light chain 2|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215095|||http://purl.uniprot.org/annotation/VAR_020379|||http://purl.uniprot.org/annotation/VSP_043486
http://togogenome.org/gene/9606:PAK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0AZM9|||http://purl.uniprot.org/uniprot/Q9P286                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CRIB|||Complete loss of CDC42 binding and CDC42-mediated autophosphorylation.|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Linker|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086477|||http://purl.uniprot.org/annotation/VAR_021865|||http://purl.uniprot.org/annotation/VAR_040978|||http://purl.uniprot.org/annotation/VAR_040979|||http://purl.uniprot.org/annotation/VAR_040980|||http://purl.uniprot.org/annotation/VAR_040981|||http://purl.uniprot.org/annotation/VAR_040982|||http://purl.uniprot.org/annotation/VAR_040983|||http://purl.uniprot.org/annotation/VAR_040984|||http://purl.uniprot.org/annotation/VAR_040985
http://togogenome.org/gene/9606:CARD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TES3|||http://purl.uniprot.org/uniprot/Q9BXL7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Abolished homodimerization.|||Basic and acidic residues|||CARD|||Caspase recruitment domain-containing protein 11|||Disordered|||Guanylate kinase-like|||In BENTA; results in protein aggregation; constitutive activation of NF-kappa-B signaling.|||In IMD11A; results in defective NF-kappa-B activation.|||In IMD11B; no effect on protein abundance; decreased interaction with BCL10; dominant negative effect on NF-kappa-B signaling; dominant negative effect on TORC1 signaling.|||In IMD11B; no effect on protein abundance; dominant negative effect on NF-kappaB signaling; dominant negative effect on TORC1 signaling.|||Inhibitory domain (ID)|||Interchain|||Linker|||PDZ|||Phosphoserine|||Phosphoserine; by PKC/PRKCB and PKC/PRKCQ|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144086|||http://purl.uniprot.org/annotation/VAR_028117|||http://purl.uniprot.org/annotation/VAR_028118|||http://purl.uniprot.org/annotation/VAR_069710|||http://purl.uniprot.org/annotation/VAR_069711|||http://purl.uniprot.org/annotation/VAR_079158|||http://purl.uniprot.org/annotation/VAR_079284|||http://purl.uniprot.org/annotation/VAR_079285|||http://purl.uniprot.org/annotation/VAR_079286
http://togogenome.org/gene/9606:TADA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0Y4|||http://purl.uniprot.org/uniprot/A0A087WWR4|||http://purl.uniprot.org/uniprot/B3KU13|||http://purl.uniprot.org/uniprot/O75478                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH myb-type|||In isoform 2.|||Myb-like|||Phosphoserine; in variant Ser-6|||Polar residues|||SANT|||SWIRM|||Transcriptional adapter 2-alpha|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197083|||http://purl.uniprot.org/annotation/VAR_047466|||http://purl.uniprot.org/annotation/VAR_047467|||http://purl.uniprot.org/annotation/VAR_047468|||http://purl.uniprot.org/annotation/VSP_040347|||http://purl.uniprot.org/annotation/VSP_040348
http://togogenome.org/gene/9606:RARRES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49788                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cystatin LXN-type 1|||Cystatin LXN-type 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type III membrane protein|||In isoform 1.|||Lumenal|||O-linked (Xyl...) (chondroitin sulfate) serine|||Retinoic acid receptor responder protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191346|||http://purl.uniprot.org/annotation/VAR_053612|||http://purl.uniprot.org/annotation/VAR_060094|||http://purl.uniprot.org/annotation/VSP_010697|||http://purl.uniprot.org/annotation/VSP_010698
http://togogenome.org/gene/9606:IL17RB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRM6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interleukin-17 receptor B|||N-linked (GlcNAc...) asparagine|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011032|||http://purl.uniprot.org/annotation/VAR_019209|||http://purl.uniprot.org/annotation/VAR_019210|||http://purl.uniprot.org/annotation/VAR_019211|||http://purl.uniprot.org/annotation/VAR_019212|||http://purl.uniprot.org/annotation/VAR_049178|||http://purl.uniprot.org/annotation/VAR_049179|||http://purl.uniprot.org/annotation/VAR_059304|||http://purl.uniprot.org/annotation/VSP_001740|||http://purl.uniprot.org/annotation/VSP_001741
http://togogenome.org/gene/9606:MTX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13505                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||Metaxin-1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220991|||http://purl.uniprot.org/annotation/VAR_047376|||http://purl.uniprot.org/annotation/VSP_035741|||http://purl.uniprot.org/annotation/VSP_035742
http://togogenome.org/gene/9606:GDNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3T2|||http://purl.uniprot.org/uniprot/A0A0S2Z3V2|||http://purl.uniprot.org/uniprot/P39905                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glial cell line-derived neurotrophic factor|||In HSCR3.|||In HSCR3; sporadic form.|||In HSCR3; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||Interchain|||May be a risk factor for Hirschsprung disease.|||N-linked (GlcNAc...) asparagine|||Risk factor for Hirschsprung disease.|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034004|||http://purl.uniprot.org/annotation/PRO_0000034005|||http://purl.uniprot.org/annotation/PRO_5006608233|||http://purl.uniprot.org/annotation/PRO_5006608250|||http://purl.uniprot.org/annotation/VAR_009494|||http://purl.uniprot.org/annotation/VAR_009495|||http://purl.uniprot.org/annotation/VAR_009496|||http://purl.uniprot.org/annotation/VAR_009497|||http://purl.uniprot.org/annotation/VAR_018152|||http://purl.uniprot.org/annotation/VSP_006420|||http://purl.uniprot.org/annotation/VSP_026368|||http://purl.uniprot.org/annotation/VSP_042298
http://togogenome.org/gene/9606:CHURC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 1.|||In isoform 2.|||In isoform 3.|||Protein Churchill                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089665|||http://purl.uniprot.org/annotation/VSP_061409|||http://purl.uniprot.org/annotation/VSP_061410|||http://purl.uniprot.org/annotation/VSP_061411|||http://purl.uniprot.org/annotation/VSP_061412
http://togogenome.org/gene/9606:TNFSF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14788|||http://purl.uniprot.org/uniprot/Q54A98|||http://purl.uniprot.org/uniprot/Q5T9Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In OPTB2.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Reduces affinity for TNFRSF11B.|||TNF family profile|||Tumor necrosis factor ligand superfamily member 11, membrane form|||Tumor necrosis factor ligand superfamily member 11, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034514|||http://purl.uniprot.org/annotation/PRO_0000034515|||http://purl.uniprot.org/annotation/VAR_037424|||http://purl.uniprot.org/annotation/VSP_006446|||http://purl.uniprot.org/annotation/VSP_006447
http://togogenome.org/gene/9606:ARHGEF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15085                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RGSL|||Rho guanine nucleotide exchange factor 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080928|||http://purl.uniprot.org/annotation/VAR_024285|||http://purl.uniprot.org/annotation/VAR_061795|||http://purl.uniprot.org/annotation/VSP_042003
http://togogenome.org/gene/9606:ADCY9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60503                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 9|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in 37.5% of the Asian population, in 30% of the Caucasian population and in 16.3% of the African-American population; reduced adenylyl cyclase activity in response to stimulation of the beta-adregnergic receptor by Mn(2+) agonists isoproteronol and NaF; increased albuterol-stimulated adenylyl cyclase activity in the presence of corticosteroid.|||Guanylate cyclase 1|||Guanylate cyclase 2|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195708|||http://purl.uniprot.org/annotation/VAR_023750|||http://purl.uniprot.org/annotation/VAR_070887
http://togogenome.org/gene/9606:FMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01740                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Flavin-containing monooxygenase 1|||Helical|||In isoform 2.|||Lumenal|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147639|||http://purl.uniprot.org/annotation/VAR_015358|||http://purl.uniprot.org/annotation/VAR_015359|||http://purl.uniprot.org/annotation/VAR_015360|||http://purl.uniprot.org/annotation/VAR_022204|||http://purl.uniprot.org/annotation/VAR_022205|||http://purl.uniprot.org/annotation/VAR_022206|||http://purl.uniprot.org/annotation/VAR_022207|||http://purl.uniprot.org/annotation/VAR_022208|||http://purl.uniprot.org/annotation/VAR_022209|||http://purl.uniprot.org/annotation/VSP_054543
http://togogenome.org/gene/9606:RASSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WH2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylserine|||Ras association domain-containing protein 3|||Ras-associating|||Removed|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240396|||http://purl.uniprot.org/annotation/VAR_026724|||http://purl.uniprot.org/annotation/VSP_019353|||http://purl.uniprot.org/annotation/VSP_019354
http://togogenome.org/gene/9606:ATP6V1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUZ7|||http://purl.uniprot.org/uniprot/Q9UI12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase V1 complex subunit H C-terminal|||In isoform 2.|||Phosphoserine|||V-type proton ATPase subunit H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124193|||http://purl.uniprot.org/annotation/VSP_012274
http://togogenome.org/gene/9606:RPL37A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61513                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Large ribosomal subunit protein eL43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139817
http://togogenome.org/gene/9606:C1orf167                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXP5|||http://purl.uniprot.org/uniprot/A2VCK6|||http://purl.uniprot.org/uniprot/Q5SNV9|||http://purl.uniprot.org/uniprot/Q8NDG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C1orf167                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306118|||http://purl.uniprot.org/annotation/VAR_035266|||http://purl.uniprot.org/annotation/VAR_035267|||http://purl.uniprot.org/annotation/VAR_035268|||http://purl.uniprot.org/annotation/VAR_035269|||http://purl.uniprot.org/annotation/VAR_035270|||http://purl.uniprot.org/annotation/VAR_035271|||http://purl.uniprot.org/annotation/VAR_035272|||http://purl.uniprot.org/annotation/VAR_035273|||http://purl.uniprot.org/annotation/VAR_035274|||http://purl.uniprot.org/annotation/VAR_035275|||http://purl.uniprot.org/annotation/VAR_035276|||http://purl.uniprot.org/annotation/VSP_028420
http://togogenome.org/gene/9606:RPS28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62857                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  N-acetylmethionine|||Phosphoserine|||Small ribosomal subunit protein eS28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136822
http://togogenome.org/gene/9606:HHLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J7D0|||http://purl.uniprot.org/uniprot/Q9UM44                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||HERV-H LTR-associating protein 2|||Helical|||Ig-like|||Ig-like C1-type|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249709|||http://purl.uniprot.org/annotation/PRO_5002997139|||http://purl.uniprot.org/annotation/VAR_027487|||http://purl.uniprot.org/annotation/VAR_027488|||http://purl.uniprot.org/annotation/VAR_027489|||http://purl.uniprot.org/annotation/VSP_054729
http://togogenome.org/gene/9606:PREX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCU6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEP 1|||DEP 2|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||PDZ|||PH|||Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080965|||http://purl.uniprot.org/annotation/VAR_023210|||http://purl.uniprot.org/annotation/VAR_023211|||http://purl.uniprot.org/annotation/VAR_023212|||http://purl.uniprot.org/annotation/VAR_057191|||http://purl.uniprot.org/annotation/VAR_057192|||http://purl.uniprot.org/annotation/VAR_061798|||http://purl.uniprot.org/annotation/VAR_061799|||http://purl.uniprot.org/annotation/VSP_001818|||http://purl.uniprot.org/annotation/VSP_001819|||http://purl.uniprot.org/annotation/VSP_015090|||http://purl.uniprot.org/annotation/VSP_015091
http://togogenome.org/gene/9606:DIAPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60879                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DAD|||Disordered|||FH1|||FH2|||GBD/FH3|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Pro residues|||Protein diaphanous homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194895|||http://purl.uniprot.org/annotation/VAR_049095|||http://purl.uniprot.org/annotation/VAR_049096|||http://purl.uniprot.org/annotation/VSP_001573|||http://purl.uniprot.org/annotation/VSP_012955|||http://purl.uniprot.org/annotation/VSP_012956
http://togogenome.org/gene/9606:UPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DND0|||http://purl.uniprot.org/uniprot/Q16831|||http://purl.uniprot.org/uniprot/Q86Y75                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Nucleoside phosphorylase|||Uridine phosphorylase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063191|||http://purl.uniprot.org/annotation/VSP_001279|||http://purl.uniprot.org/annotation/VSP_001280
http://togogenome.org/gene/9606:BEX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXY8                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||His cluster|||In isoform 2.|||Omega-N-methylarginine|||Protein BEX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229777|||http://purl.uniprot.org/annotation/VSP_046808
http://togogenome.org/gene/9606:BTNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXE8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin-like protein 3|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014540|||http://purl.uniprot.org/annotation/VSP_012716|||http://purl.uniprot.org/annotation/VSP_012717
http://togogenome.org/gene/9606:OR6N1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGY5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6N1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150633|||http://purl.uniprot.org/annotation/VAR_024106|||http://purl.uniprot.org/annotation/VAR_024107|||http://purl.uniprot.org/annotation/VAR_024108|||http://purl.uniprot.org/annotation/VAR_024109|||http://purl.uniprot.org/annotation/VAR_053223
http://togogenome.org/gene/9606:EVPLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZ36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Envoplakin-like protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395323|||http://purl.uniprot.org/annotation/VAR_063399
http://togogenome.org/gene/9606:PLCB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01970                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3|||C2|||Disordered|||In SMDCD; strong reduction in protein levels and marked increase in cellular phosphatidylinositol 4,5 bisphosphate levels in patient cells.|||In isoform 2.|||Interaction with SHANK2|||N-acetylalanine|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088491|||http://purl.uniprot.org/annotation/VAR_029229|||http://purl.uniprot.org/annotation/VAR_084509|||http://purl.uniprot.org/annotation/VSP_046054
http://togogenome.org/gene/9606:METTL26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S19                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Methyltransferase-like 26|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337114|||http://purl.uniprot.org/annotation/VAR_064368|||http://purl.uniprot.org/annotation/VSP_033918|||http://purl.uniprot.org/annotation/VSP_033919|||http://purl.uniprot.org/annotation/VSP_045804|||http://purl.uniprot.org/annotation/VSP_046838|||http://purl.uniprot.org/annotation/VSP_046839
http://togogenome.org/gene/9606:RFX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8HWS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-binding protein RFX6|||Disordered|||In MTCHRS; abolishes DNA-binding.|||In MTCHRS; induces a slight reduction in DNA-binding; in a patient still alive at age 4.5 years.|||In MTCHRS; inhibits the transactivation of the insulin and beta-cell L-type calcium channel genes.|||RFX-type winged-helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313721|||http://purl.uniprot.org/annotation/VAR_037709|||http://purl.uniprot.org/annotation/VAR_037710|||http://purl.uniprot.org/annotation/VAR_037711|||http://purl.uniprot.org/annotation/VAR_061768|||http://purl.uniprot.org/annotation/VAR_062978|||http://purl.uniprot.org/annotation/VAR_062979|||http://purl.uniprot.org/annotation/VAR_074215
http://togogenome.org/gene/9606:TRIM55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYV6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||B box-type|||COS|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Pro residues|||RING-type|||Rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance.|||Tripartite motif-containing protein 55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056286|||http://purl.uniprot.org/annotation/VAR_052144|||http://purl.uniprot.org/annotation/VAR_074078|||http://purl.uniprot.org/annotation/VAR_074079|||http://purl.uniprot.org/annotation/VAR_074080|||http://purl.uniprot.org/annotation/VAR_074081|||http://purl.uniprot.org/annotation/VAR_074082|||http://purl.uniprot.org/annotation/VAR_074083|||http://purl.uniprot.org/annotation/VAR_074084|||http://purl.uniprot.org/annotation/VAR_074085|||http://purl.uniprot.org/annotation/VAR_074086|||http://purl.uniprot.org/annotation/VAR_074087|||http://purl.uniprot.org/annotation/VAR_074088|||http://purl.uniprot.org/annotation/VAR_074089|||http://purl.uniprot.org/annotation/VAR_074090|||http://purl.uniprot.org/annotation/VAR_074091|||http://purl.uniprot.org/annotation/VAR_082913|||http://purl.uniprot.org/annotation/VSP_015996|||http://purl.uniprot.org/annotation/VSP_015997|||http://purl.uniprot.org/annotation/VSP_015998
http://togogenome.org/gene/9606:EFCAB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5THR3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 10|||EF-hand 11|||EF-hand 12|||EF-hand 13|||EF-hand 14|||EF-hand 15|||EF-hand 16|||EF-hand 17|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||EF-hand 7|||EF-hand 8|||EF-hand 9|||EF-hand calcium-binding domain-containing protein 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with AR|||Interaction with PARK7|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246024|||http://purl.uniprot.org/annotation/VAR_048648|||http://purl.uniprot.org/annotation/VAR_048649|||http://purl.uniprot.org/annotation/VAR_048650|||http://purl.uniprot.org/annotation/VAR_048651|||http://purl.uniprot.org/annotation/VAR_048652|||http://purl.uniprot.org/annotation/VAR_048653|||http://purl.uniprot.org/annotation/VAR_048654|||http://purl.uniprot.org/annotation/VAR_048655|||http://purl.uniprot.org/annotation/VAR_048656|||http://purl.uniprot.org/annotation/VSP_019808|||http://purl.uniprot.org/annotation/VSP_019809|||http://purl.uniprot.org/annotation/VSP_019810|||http://purl.uniprot.org/annotation/VSP_019811|||http://purl.uniprot.org/annotation/VSP_019812|||http://purl.uniprot.org/annotation/VSP_019813|||http://purl.uniprot.org/annotation/VSP_034831|||http://purl.uniprot.org/annotation/VSP_034832
http://togogenome.org/gene/9606:SOS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07889                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||Found in patients with Noonan syndrome.|||In NS4.|||In NS4; increases the basal level of active RAS; prolonges RAS activation after EGF stimulation and enhances ERK activation.|||In NS4; one patient with Noonan syndrome also carries a likely causative mutation in RAF1; the mutant protein cannot induce ERK1 phosphorylation.|||In NS4; promotes constitutive RAS activation and enhances ERK activation.|||In NS4; requires 2 nucleotide substitutions.|||In a patient with Noonan syndrome.|||In isoform 2.|||Increases MAPK3 phosphorylation in response to EGF stimulation.|||Loss of phosphorylation, disruption of interaction with YWHAB and YWHAE, and modest increase in the magnitude and duration of EGF-induced MAPK1/3 phosphorylation; when associated with A-1134.|||Loss of phosphorylation, disruption of interaction with YWHAB and YWHAE, and modest increase in the magnitude and duration of EGF-induced MAPK1/3 phosphorylation; when associated with A-1161.|||N-terminal Ras-GEF|||PH|||Phosphoserine|||Phosphoserine; by RPS6KA3|||Polar residues|||Pro residues|||Ras-GEF|||Son of sevenless homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068894|||http://purl.uniprot.org/annotation/VAR_030423|||http://purl.uniprot.org/annotation/VAR_030424|||http://purl.uniprot.org/annotation/VAR_030425|||http://purl.uniprot.org/annotation/VAR_030426|||http://purl.uniprot.org/annotation/VAR_030427|||http://purl.uniprot.org/annotation/VAR_030428|||http://purl.uniprot.org/annotation/VAR_030429|||http://purl.uniprot.org/annotation/VAR_030430|||http://purl.uniprot.org/annotation/VAR_030431|||http://purl.uniprot.org/annotation/VAR_030432|||http://purl.uniprot.org/annotation/VAR_030433|||http://purl.uniprot.org/annotation/VAR_030434|||http://purl.uniprot.org/annotation/VAR_030435|||http://purl.uniprot.org/annotation/VAR_030436|||http://purl.uniprot.org/annotation/VAR_030437|||http://purl.uniprot.org/annotation/VAR_030438|||http://purl.uniprot.org/annotation/VAR_030439|||http://purl.uniprot.org/annotation/VAR_030440|||http://purl.uniprot.org/annotation/VAR_030441|||http://purl.uniprot.org/annotation/VAR_030442|||http://purl.uniprot.org/annotation/VAR_030443|||http://purl.uniprot.org/annotation/VAR_064504|||http://purl.uniprot.org/annotation/VAR_064505|||http://purl.uniprot.org/annotation/VAR_064506|||http://purl.uniprot.org/annotation/VAR_066031|||http://purl.uniprot.org/annotation/VAR_066032|||http://purl.uniprot.org/annotation/VAR_066033|||http://purl.uniprot.org/annotation/VAR_066034|||http://purl.uniprot.org/annotation/VAR_066035|||http://purl.uniprot.org/annotation/VAR_066036|||http://purl.uniprot.org/annotation/VAR_066037|||http://purl.uniprot.org/annotation/VAR_066038|||http://purl.uniprot.org/annotation/VAR_066039|||http://purl.uniprot.org/annotation/VAR_066040|||http://purl.uniprot.org/annotation/VAR_066041|||http://purl.uniprot.org/annotation/VAR_066042|||http://purl.uniprot.org/annotation/VAR_066043|||http://purl.uniprot.org/annotation/VAR_066044|||http://purl.uniprot.org/annotation/VAR_066045|||http://purl.uniprot.org/annotation/VAR_066046|||http://purl.uniprot.org/annotation/VAR_066047|||http://purl.uniprot.org/annotation/VAR_066048|||http://purl.uniprot.org/annotation/VAR_066049|||http://purl.uniprot.org/annotation/VAR_066050|||http://purl.uniprot.org/annotation/VAR_066051|||http://purl.uniprot.org/annotation/VAR_066052|||http://purl.uniprot.org/annotation/VAR_066053|||http://purl.uniprot.org/annotation/VAR_066054|||http://purl.uniprot.org/annotation/VAR_066055|||http://purl.uniprot.org/annotation/VAR_066056|||http://purl.uniprot.org/annotation/VAR_066057|||http://purl.uniprot.org/annotation/VAR_066058|||http://purl.uniprot.org/annotation/VAR_066059|||http://purl.uniprot.org/annotation/VSP_056463|||http://purl.uniprot.org/annotation/VSP_056464|||http://purl.uniprot.org/annotation/VSP_056465
http://togogenome.org/gene/9606:EFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2Z2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Elongation factor-like GTPase 1|||In SDS2; unknown pathological significance.|||In isoform 2.|||Loss of GTPase activity. Abolishes dissociation of EIF6 from 60S pre-ribosome subunits.|||N6-acetyllysine|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313805|||http://purl.uniprot.org/annotation/VAR_037746|||http://purl.uniprot.org/annotation/VAR_037747|||http://purl.uniprot.org/annotation/VAR_037748|||http://purl.uniprot.org/annotation/VAR_080513|||http://purl.uniprot.org/annotation/VAR_080514|||http://purl.uniprot.org/annotation/VSP_030152
http://togogenome.org/gene/9606:ZNF404                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q494X3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 404                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305136|||http://purl.uniprot.org/annotation/VAR_057419|||http://purl.uniprot.org/annotation/VAR_070605
http://togogenome.org/gene/9606:C9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02748                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta stranded|||C-linked (Man) tryptophan|||C-linked (Man) tryptophan; partial|||Cleavage; by thrombin|||Complement component C9|||Complement component C9a|||Complement component C9b|||Creates an artifactual disulfide bond that prevents the conformation change required for oligomerization and pore formation; when associated with C-283.|||Creates an artifactual disulfide bond that prevents the conformation change required for oligomerization and pore formation; when associated with C-427.|||EGF-like|||In ARMD15.|||In C9D.|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023602|||http://purl.uniprot.org/annotation/PRO_0000023603|||http://purl.uniprot.org/annotation/PRO_0000023604|||http://purl.uniprot.org/annotation/VAR_012648|||http://purl.uniprot.org/annotation/VAR_022024|||http://purl.uniprot.org/annotation/VAR_027651|||http://purl.uniprot.org/annotation/VAR_033802|||http://purl.uniprot.org/annotation/VAR_050481|||http://purl.uniprot.org/annotation/VAR_061503|||http://purl.uniprot.org/annotation/VAR_070940
http://togogenome.org/gene/9606:SUGCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAC7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In GA3; inactive enzyme; healthy individuals who have abnormal quantities of glutaric acid but low 3-hydroxyglutaric acid.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Mitochondrion|||N6-acetyllysine|||Nucleophile|||Succinate--hydroxymethylglutarate CoA-transferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194726|||http://purl.uniprot.org/annotation/VAR_054852|||http://purl.uniprot.org/annotation/VSP_014721|||http://purl.uniprot.org/annotation/VSP_014722|||http://purl.uniprot.org/annotation/VSP_043291
http://togogenome.org/gene/9606:SPRR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35325                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA tandem repeats of P-K-C-P-[EQ]-P-C-P-P|||Disordered|||Small proline-rich protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150009|||http://purl.uniprot.org/annotation/VAR_034518
http://togogenome.org/gene/9606:CNGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16281                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cyclic nucleotide-gated cation channel alpha-3|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with Leber congenital amaurosis; unknown pathological significance.|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||In ACHM2.|||In ACHM2; also found in patients with cone-rod dystrophy.|||In ACHM2; also found in patients with cone-rod dystrophy; does not form functional homomeric or heteromeric channels.|||In ACHM2; also found in patients with cone-rod dystrophy; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius.|||In ACHM2; also found in patients with cone-rod dystrophy; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration.|||In ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 1.8; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature.|||In ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; the channel density into the cell membrane is considerably improved by decreasing the cultivation temparature.|||In ACHM2; does not reveal any detectable calcium influx upon agonist application at 37 degrees Celsius; the channel function could be restored by incubating the transfected cells at 27 degrees Celsius; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; a substantial reduction of macroscopic cGMP maximum current to only one-third of the mean value for wild-type CNGA3 + CNGB3 is observed for the mutant CNGA3 + CNGB3; is in large part located in the cell membrane at 37 and 27 degrees Celsius.|||In ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is significantly reduced.|||In ACHM2; mutant CNGA3 alone or together with the CNGB3 subunit exhibit an increase in apparent affinity for cGMP and an increase in the relative agonist efficacy of cAMP compared with cGMP; cell surface expression levels is unchanged.|||In ACHM2; the K(1/2) value is shifted toward a higher cGMP concentration by a factor of 3.0; no positive influence of the CNGB3 subunit in the cGMP sensitivity is observed; average cGMP maximum current is decreased to half of the mean wild-type value for the mutant CNGA3 + CNGB3.|||In ACHM2; the dose-response relationship for cGMP-activation is shifted toward a lower cGMP concentration; the left shift in the dose-response relationship of the mutant CNGA3 is less distinctive than in homomeric channels with this mutation indicating a partial rescue effect of the CNGB3 subunit; is in large part located in the cell membrane at 37 and 27 degrees Celsius.|||In ACHM2; unknown pathological significance; the dose-response relationship for cGMP-activation is not significantly different from that of wild-type CNGA3; the dose-response relationship of the mutant CNGA3 + CNGB3 is similar to that of the wild-type protein; the channel density into the cell membrane is considerably improved by decreasing the cultivation temperature.|||In isoform 2.|||In isoform 3.|||Polar residues|||Probable disease-associated variant found in patients with cone-rod dystrophy. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219317|||http://purl.uniprot.org/annotation/VAR_010902|||http://purl.uniprot.org/annotation/VAR_010903|||http://purl.uniprot.org/annotation/VAR_010904|||http://purl.uniprot.org/annotation/VAR_010905|||http://purl.uniprot.org/annotation/VAR_010906|||http://purl.uniprot.org/annotation/VAR_010907|||http://purl.uniprot.org/annotation/VAR_010908|||http://purl.uniprot.org/annotation/VAR_010909|||http://purl.uniprot.org/annotation/VAR_010910|||http://purl.uniprot.org/annotation/VAR_021963|||http://purl.uniprot.org/annotation/VAR_047565|||http://purl.uniprot.org/annotation/VAR_047566|||http://purl.uniprot.org/annotation/VAR_047567|||http://purl.uniprot.org/annotation/VAR_047568|||http://purl.uniprot.org/annotation/VAR_047569|||http://purl.uniprot.org/annotation/VAR_047570|||http://purl.uniprot.org/annotation/VAR_047571|||http://purl.uniprot.org/annotation/VAR_047572|||http://purl.uniprot.org/annotation/VAR_047573|||http://purl.uniprot.org/annotation/VAR_047574|||http://purl.uniprot.org/annotation/VAR_047575|||http://purl.uniprot.org/annotation/VAR_047576|||http://purl.uniprot.org/annotation/VAR_047577|||http://purl.uniprot.org/annotation/VAR_047578|||http://purl.uniprot.org/annotation/VAR_047579|||http://purl.uniprot.org/annotation/VAR_047580|||http://purl.uniprot.org/annotation/VAR_047581|||http://purl.uniprot.org/annotation/VAR_047582|||http://purl.uniprot.org/annotation/VAR_047583|||http://purl.uniprot.org/annotation/VAR_047584|||http://purl.uniprot.org/annotation/VAR_047585|||http://purl.uniprot.org/annotation/VAR_047586|||http://purl.uniprot.org/annotation/VAR_047587|||http://purl.uniprot.org/annotation/VAR_047588|||http://purl.uniprot.org/annotation/VAR_047589|||http://purl.uniprot.org/annotation/VAR_047590|||http://purl.uniprot.org/annotation/VAR_047591|||http://purl.uniprot.org/annotation/VAR_047592|||http://purl.uniprot.org/annotation/VAR_047593|||http://purl.uniprot.org/annotation/VAR_047594|||http://purl.uniprot.org/annotation/VAR_047595|||http://purl.uniprot.org/annotation/VAR_047596|||http://purl.uniprot.org/annotation/VAR_047597|||http://purl.uniprot.org/annotation/VAR_047598|||http://purl.uniprot.org/annotation/VAR_047599|||http://purl.uniprot.org/annotation/VAR_047600|||http://purl.uniprot.org/annotation/VAR_047601|||http://purl.uniprot.org/annotation/VAR_047602|||http://purl.uniprot.org/annotation/VAR_047603|||http://purl.uniprot.org/annotation/VAR_047604|||http://purl.uniprot.org/annotation/VAR_047605|||http://purl.uniprot.org/annotation/VAR_066860|||http://purl.uniprot.org/annotation/VAR_069398|||http://purl.uniprot.org/annotation/VAR_071435|||http://purl.uniprot.org/annotation/VAR_071436|||http://purl.uniprot.org/annotation/VAR_071438|||http://purl.uniprot.org/annotation/VAR_071439|||http://purl.uniprot.org/annotation/VAR_071440|||http://purl.uniprot.org/annotation/VAR_071441|||http://purl.uniprot.org/annotation/VAR_071442|||http://purl.uniprot.org/annotation/VAR_071443|||http://purl.uniprot.org/annotation/VAR_071444|||http://purl.uniprot.org/annotation/VAR_071445|||http://purl.uniprot.org/annotation/VAR_071446|||http://purl.uniprot.org/annotation/VAR_071447|||http://purl.uniprot.org/annotation/VAR_071448|||http://purl.uniprot.org/annotation/VAR_071449|||http://purl.uniprot.org/annotation/VAR_071450|||http://purl.uniprot.org/annotation/VAR_071451|||http://purl.uniprot.org/annotation/VAR_075493|||http://purl.uniprot.org/annotation/VSP_042525|||http://purl.uniprot.org/annotation/VSP_057075
http://togogenome.org/gene/9606:COL11A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFS1|||http://purl.uniprot.org/uniprot/A0A0G2JL78|||http://purl.uniprot.org/uniprot/P13942|||http://purl.uniprot.org/uniprot/Q4VXY6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal propeptide|||Collagen alpha-2(XI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Disordered|||Fibrillar collagen NC1|||In DFNA13.|||In DFNB53.|||In OSMEDA.|||In OSMEDB.|||In isoform 2, isoform 5, isoform 6 and isoform 8.|||In isoform 3, isoform 5, isoform 7 and isoform 8.|||In isoform 4, isoform 6, isoform 7 and isoform 8.|||In isoform 9.|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||Polar residues|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005840|||http://purl.uniprot.org/annotation/PRO_0000005841|||http://purl.uniprot.org/annotation/PRO_5014509640|||http://purl.uniprot.org/annotation/PRO_5014586577|||http://purl.uniprot.org/annotation/PRO_5038209132|||http://purl.uniprot.org/annotation/VAR_001907|||http://purl.uniprot.org/annotation/VAR_010655|||http://purl.uniprot.org/annotation/VAR_010656|||http://purl.uniprot.org/annotation/VAR_013591|||http://purl.uniprot.org/annotation/VAR_013592|||http://purl.uniprot.org/annotation/VAR_013593|||http://purl.uniprot.org/annotation/VAR_013594|||http://purl.uniprot.org/annotation/VAR_013595|||http://purl.uniprot.org/annotation/VAR_013596|||http://purl.uniprot.org/annotation/VAR_013597|||http://purl.uniprot.org/annotation/VAR_025276|||http://purl.uniprot.org/annotation/VAR_033797|||http://purl.uniprot.org/annotation/VAR_048804|||http://purl.uniprot.org/annotation/VAR_048805|||http://purl.uniprot.org/annotation/VAR_048806|||http://purl.uniprot.org/annotation/VAR_048807|||http://purl.uniprot.org/annotation/VAR_072731|||http://purl.uniprot.org/annotation/VAR_072732|||http://purl.uniprot.org/annotation/VAR_079875|||http://purl.uniprot.org/annotation/VSP_001167|||http://purl.uniprot.org/annotation/VSP_001168|||http://purl.uniprot.org/annotation/VSP_001169|||http://purl.uniprot.org/annotation/VSP_043432|||http://purl.uniprot.org/annotation/VSP_043433
http://togogenome.org/gene/9606:NFATC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14934                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2 approximate SP repeats|||Calcineurin-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||IPT/TIG|||In isoform 11, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 21 and isoform 24.|||In isoform 12, isoform 13 and isoform 18.|||In isoform 19, isoform 20 and isoform 21.|||In isoform 2, isoform 3 and isoform 11.|||In isoform 22, isoform 23 and isoform 24.|||In isoform 3, isoform 5, isoform 7, isoform 8, isoform 10, isoform 13, isoform 20 and isoform 23.|||In isoform 4, isoform 5 and isoform 14.|||In isoform 6, isoform 7 and isoform 15.|||In isoform 9, isoform 10 and isoform 17.|||Marked decrease in phosphorylation by MAPK8 or MAPK9. Complete loss of phosphorylation by MAPK8 or MAPK9, but no effect on MAPK8/9-binding; when associated with A-213. Decreased transcriptional activity; when associated with A-213.|||Marked decrease in phosphorylation by MAPK8 or MAPK9. Complete loss of phosphorylation by MAPK8 or MAPK9, but no effect on MAPK8/9-binding; when associated with A-217. Decreased transcriptional activity; when associated with A-217.|||Nuclear factor of activated T-cells, cytoplasmic 4|||Nuclear localization signal|||Phosphoserine; by MAPK7 and MAPK14|||Phosphoserine; by MAPK8 and MAPK9|||Phosphoserine; by RPS6KA3|||Polar residues|||Pro residues|||Promotes nuclear localization and increases transcriptional activity; when associated with A-168.|||Promotes nuclear localization and increases transcriptional activity; when associated with A-170.|||RHD|||SP 1|||SP 2; approximate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205182|||http://purl.uniprot.org/annotation/VAR_046985|||http://purl.uniprot.org/annotation/VAR_046986|||http://purl.uniprot.org/annotation/VAR_046987|||http://purl.uniprot.org/annotation/VSP_036697|||http://purl.uniprot.org/annotation/VSP_036698|||http://purl.uniprot.org/annotation/VSP_036699|||http://purl.uniprot.org/annotation/VSP_036700|||http://purl.uniprot.org/annotation/VSP_036701|||http://purl.uniprot.org/annotation/VSP_036702|||http://purl.uniprot.org/annotation/VSP_036703|||http://purl.uniprot.org/annotation/VSP_036704|||http://purl.uniprot.org/annotation/VSP_036705
http://togogenome.org/gene/9606:IL34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMJ4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interleukin-34|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294348|||http://purl.uniprot.org/annotation/VAR_033164|||http://purl.uniprot.org/annotation/VAR_056920|||http://purl.uniprot.org/annotation/VSP_035079
http://togogenome.org/gene/9606:INTS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75QN2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NEDCHS; alters the assembly of the Integrator complex.|||In NEDCHS; occurs in a splice site resulting in altered splicing and probable nonsense-mediated mRNA decay.|||In isoform 2.|||Integrator complex subunit 8|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259553|||http://purl.uniprot.org/annotation/VAR_083358|||http://purl.uniprot.org/annotation/VAR_083359|||http://purl.uniprot.org/annotation/VSP_021469
http://togogenome.org/gene/9606:HPCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84074                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In DYT2.|||In DYT2; no effect on protein localization; no effect on protein abundance; no effect on protein stability; no effect on protein 3D structure; decreased oligomerization; changed calcium-binding; effect on cooperativity for calcium-binding; no effect on affinity for calcium; no effect on interaction with voltage-dependent calcium channels.|||In DYT2; no effect on protein localization; no effect on protein abundance; no effect on protein stability; no effect on protein 3D structure; decreased oligomerization; no effect on calcium-binding; no effect on affinity for calcium; increased interaction with voltage-dependent calcium channels.|||N-myristoyl glycine|||Neuron-specific calcium-binding protein hippocalcin|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073768|||http://purl.uniprot.org/annotation/VAR_048662|||http://purl.uniprot.org/annotation/VAR_073803|||http://purl.uniprot.org/annotation/VAR_073804|||http://purl.uniprot.org/annotation/VAR_073805
http://togogenome.org/gene/9606:ADIPOQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K660|||http://purl.uniprot.org/uniprot/B2R773|||http://purl.uniprot.org/uniprot/Q15848                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||4-hydroxyproline; partial|||5-hydroxylysine|||Abolishes sialylated isoforms.|||Adiponectin|||Associated with low plasma adiponectin concentration and risk for diabetes mellitus type 2; does not assemble into trimers resulting in impaired secretion from the cell.|||Basic and acidic residues|||C1q|||Collagen-like|||Disordered|||Does not form high molecular weight multimers.|||Impaired formation of HMW multimers; when associated with R-101.|||Impaired formation of HMW multimers; when associated with R-65.|||Impaired formation of HMW multimers; when associated with R-68.|||Impaired formation of HMW multimers; when associated with R-77.|||Impaired formation of MMW and HMW multimers.|||In ADPND; does not assemble into trimers resulting in impaired secretion from the cell.|||Interchain; in form MMW and form HMW|||No change in sialylated isoforms.|||No effect on formation of HMW multimers.|||Not glycosylated|||Not hydroxylated|||O-linked (Gal...) hydroxylysine; partial|||O-linked (GalNAc...) threonine|||S-(2-succinyl)cysteine|||Some loss of sialylated isoforms.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003543|||http://purl.uniprot.org/annotation/PRO_5002781808|||http://purl.uniprot.org/annotation/PRO_5014297568|||http://purl.uniprot.org/annotation/VAR_013273|||http://purl.uniprot.org/annotation/VAR_013274|||http://purl.uniprot.org/annotation/VAR_013275|||http://purl.uniprot.org/annotation/VAR_013276|||http://purl.uniprot.org/annotation/VAR_013277|||http://purl.uniprot.org/annotation/VAR_013278|||http://purl.uniprot.org/annotation/VAR_027395|||http://purl.uniprot.org/annotation/VAR_027396
http://togogenome.org/gene/9606:S1PR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H228                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069436|||http://purl.uniprot.org/annotation/VAR_033466|||http://purl.uniprot.org/annotation/VSP_013369|||http://purl.uniprot.org/annotation/VSP_013370
http://togogenome.org/gene/9606:PABIR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DI96|||http://purl.uniprot.org/uniprot/Q6P4D5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PABIR family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254547|||http://purl.uniprot.org/annotation/VSP_021222|||http://purl.uniprot.org/annotation/VSP_044990|||http://purl.uniprot.org/annotation/VSP_044991|||http://purl.uniprot.org/annotation/VSP_044992
http://togogenome.org/gene/9606:ZNF790                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMI3|||http://purl.uniprot.org/uniprot/Q6PG37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 790                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261336|||http://purl.uniprot.org/annotation/VAR_057453|||http://purl.uniprot.org/annotation/VAR_060434
http://togogenome.org/gene/9606:HBG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZU8|||http://purl.uniprot.org/uniprot/P69891                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit gamma-1|||In Baskent.|||In Beech island.|||In Bonaire.|||In Calluna.|||In Cobb.|||In Dammam.|||In Dickinson.|||In Forest Park; associated with T-76.|||In Fukuyama.|||In Iwata.|||In Izumi/Kotobuki.|||In Jamaica.|||In Jiangsu.|||In Kuala Lumpur.|||In Macedonia-I.|||In Pendergrass.|||In Pordenone.|||In Sardinia/Forest Park; associated with N-74.|||In Siena/Hull.|||In Texas-1.|||In Victoria jubilee.|||In Woodstock.|||In Xin-su.|||In Xinjiang; unstable.|||In Yamaguchi.|||N-acetylglycine; in form Hb F1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||S-nitrosocysteine|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053253|||http://purl.uniprot.org/annotation/VAR_003124|||http://purl.uniprot.org/annotation/VAR_003125|||http://purl.uniprot.org/annotation/VAR_003127|||http://purl.uniprot.org/annotation/VAR_003128|||http://purl.uniprot.org/annotation/VAR_003130|||http://purl.uniprot.org/annotation/VAR_003135|||http://purl.uniprot.org/annotation/VAR_003138|||http://purl.uniprot.org/annotation/VAR_003141|||http://purl.uniprot.org/annotation/VAR_003142|||http://purl.uniprot.org/annotation/VAR_003143|||http://purl.uniprot.org/annotation/VAR_003145|||http://purl.uniprot.org/annotation/VAR_003147|||http://purl.uniprot.org/annotation/VAR_003149|||http://purl.uniprot.org/annotation/VAR_003153|||http://purl.uniprot.org/annotation/VAR_003158|||http://purl.uniprot.org/annotation/VAR_003159|||http://purl.uniprot.org/annotation/VAR_003160|||http://purl.uniprot.org/annotation/VAR_003161|||http://purl.uniprot.org/annotation/VAR_003163|||http://purl.uniprot.org/annotation/VAR_003164|||http://purl.uniprot.org/annotation/VAR_003165|||http://purl.uniprot.org/annotation/VAR_003168|||http://purl.uniprot.org/annotation/VAR_003173|||http://purl.uniprot.org/annotation/VAR_003175|||http://purl.uniprot.org/annotation/VAR_003177
http://togogenome.org/gene/9606:DDX60L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKC9|||http://purl.uniprot.org/uniprot/Q5H9U9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Polar residues|||Probable ATP-dependent RNA helicase DDX60-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318155|||http://purl.uniprot.org/annotation/VAR_055897|||http://purl.uniprot.org/annotation/VAR_055898|||http://purl.uniprot.org/annotation/VAR_055899|||http://purl.uniprot.org/annotation/VAR_055900|||http://purl.uniprot.org/annotation/VAR_055901|||http://purl.uniprot.org/annotation/VSP_040820|||http://purl.uniprot.org/annotation/VSP_040821|||http://purl.uniprot.org/annotation/VSP_040822
http://togogenome.org/gene/9606:OR4D6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGJ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150540|||http://purl.uniprot.org/annotation/VAR_024091|||http://purl.uniprot.org/annotation/VAR_024092|||http://purl.uniprot.org/annotation/VAR_024093|||http://purl.uniprot.org/annotation/VAR_034194|||http://purl.uniprot.org/annotation/VAR_034195|||http://purl.uniprot.org/annotation/VAR_034196|||http://purl.uniprot.org/annotation/VAR_053169
http://togogenome.org/gene/9606:FMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HJ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Protein FMC1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328780|||http://purl.uniprot.org/annotation/VAR_042520|||http://purl.uniprot.org/annotation/VSP_047244
http://togogenome.org/gene/9606:ITGB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RT22|||http://purl.uniprot.org/uniprot/P18084                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||Integrin beta|||Integrin beta subunit VWA|||Integrin beta subunit cytoplasmic|||Integrin beta subunit tail|||Integrin beta-5|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||VWFA|||in ADMIDAS binding site|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016348|||http://purl.uniprot.org/annotation/PRO_5014306163|||http://purl.uniprot.org/annotation/VAR_024290|||http://purl.uniprot.org/annotation/VAR_049634|||http://purl.uniprot.org/annotation/VAR_049635
http://togogenome.org/gene/9606:SLC10A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12908                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glycosylation.|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with Crohn disease; abolishes taurocholate transport.|||Helical|||Ileal sodium/bile acid cotransporter|||In PBAM1; abolishes taurocholate transport.|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation.|||Not glycosylated|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052339|||http://purl.uniprot.org/annotation/VAR_004613|||http://purl.uniprot.org/annotation/VAR_004614|||http://purl.uniprot.org/annotation/VAR_004615|||http://purl.uniprot.org/annotation/VAR_004616|||http://purl.uniprot.org/annotation/VAR_024837|||http://purl.uniprot.org/annotation/VAR_024838
http://togogenome.org/gene/9606:PIERCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BN46                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Piercer of microtubule wall 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089728|||http://purl.uniprot.org/annotation/VSP_014466|||http://purl.uniprot.org/annotation/VSP_014467
http://togogenome.org/gene/9606:TLR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR96                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 25|||LRR 26|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034737|||http://purl.uniprot.org/annotation/VAR_024668|||http://purl.uniprot.org/annotation/VAR_034555|||http://purl.uniprot.org/annotation/VAR_036077|||http://purl.uniprot.org/annotation/VAR_036078|||http://purl.uniprot.org/annotation/VAR_052364|||http://purl.uniprot.org/annotation/VAR_052365|||http://purl.uniprot.org/annotation/VSP_006520|||http://purl.uniprot.org/annotation/VSP_006521|||http://purl.uniprot.org/annotation/VSP_006522|||http://purl.uniprot.org/annotation/VSP_006523
http://togogenome.org/gene/9606:TRIM73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||RING-type|||Tripartite motif-containing protein 73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056278
http://togogenome.org/gene/9606:CMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23946|||http://purl.uniprot.org/uniprot/Q4FEB3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027433|||http://purl.uniprot.org/annotation/PRO_0000027434|||http://purl.uniprot.org/annotation/VAR_011770|||http://purl.uniprot.org/annotation/VAR_011771|||http://purl.uniprot.org/annotation/VAR_029190|||http://purl.uniprot.org/annotation/VSP_056947
http://togogenome.org/gene/9606:TREH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43280                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor|||Removed in mature form|||Trehalase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012051|||http://purl.uniprot.org/annotation/PRO_0000012052|||http://purl.uniprot.org/annotation/VAR_049205|||http://purl.uniprot.org/annotation/VAR_049206|||http://purl.uniprot.org/annotation/VAR_049207|||http://purl.uniprot.org/annotation/VAR_049208|||http://purl.uniprot.org/annotation/VAR_061191|||http://purl.uniprot.org/annotation/VSP_035440
http://togogenome.org/gene/9606:ERCC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28715                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DNA excision repair protein ERCC-5|||DNA-binding; H2TH (helix-2turn-helix) motif which binds double-stranded DNA|||DNA-binding; may bind double-stranded DNA|||DNA-binding; may bind to the undamaged single-strand DNA of the DNA repair bubble|||Disordered|||Found in a patient diagnosed with multiple sclerosis; unknown pathological significance.|||I-domain|||In XP-G; combined with features of Cockayne syndrome.|||In XP-G; mild form.|||In XP-G; mild form; residual activity.|||In XP-G; patient cells show a strong DNA repair defect in response to UV light but not in response to oxidative stress; decreased nucleotide-excision repair activity.|||In XP-G; reduced stability and greatly impaired endonuclease activity.|||In isoform 2.|||In isoform 3.|||Interaction with ERCC6/CSB|||Interaction with PCNA|||N-domain|||N6-acetyllysine|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Polar residues|||Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with 955-A-A-956 and A-978.|||Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with 955-A-A-956 and A-981.|||Reduced protein stability, two-fold decrease in 15-nt bubble DNA incision activity and smaller decrease in YDNA incision activity; when associated with A-978 and A-981.|||Requires 2 nucleotide substitutions.|||Slight reduction in endonuclease activity. Increased affinity for bubble DNA.|||Spacer region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154031|||http://purl.uniprot.org/annotation/VAR_007732|||http://purl.uniprot.org/annotation/VAR_007733|||http://purl.uniprot.org/annotation/VAR_007734|||http://purl.uniprot.org/annotation/VAR_014829|||http://purl.uniprot.org/annotation/VAR_015280|||http://purl.uniprot.org/annotation/VAR_017096|||http://purl.uniprot.org/annotation/VAR_017097|||http://purl.uniprot.org/annotation/VAR_020431|||http://purl.uniprot.org/annotation/VAR_020432|||http://purl.uniprot.org/annotation/VAR_020433|||http://purl.uniprot.org/annotation/VAR_020434|||http://purl.uniprot.org/annotation/VAR_020435|||http://purl.uniprot.org/annotation/VAR_020436|||http://purl.uniprot.org/annotation/VAR_023120|||http://purl.uniprot.org/annotation/VAR_023121|||http://purl.uniprot.org/annotation/VAR_023122|||http://purl.uniprot.org/annotation/VAR_023123|||http://purl.uniprot.org/annotation/VAR_023124|||http://purl.uniprot.org/annotation/VAR_023125|||http://purl.uniprot.org/annotation/VAR_046373|||http://purl.uniprot.org/annotation/VAR_046374|||http://purl.uniprot.org/annotation/VAR_046375|||http://purl.uniprot.org/annotation/VAR_075773|||http://purl.uniprot.org/annotation/VAR_075774|||http://purl.uniprot.org/annotation/VAR_085644|||http://purl.uniprot.org/annotation/VSP_035380|||http://purl.uniprot.org/annotation/VSP_053828|||http://purl.uniprot.org/annotation/VSP_053829
http://togogenome.org/gene/9606:CCDC168                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat transmembrane protein CCDC168|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342529|||http://purl.uniprot.org/annotation/VAR_044210|||http://purl.uniprot.org/annotation/VAR_044211|||http://purl.uniprot.org/annotation/VAR_044212|||http://purl.uniprot.org/annotation/VAR_044213|||http://purl.uniprot.org/annotation/VAR_044214|||http://purl.uniprot.org/annotation/VAR_044215|||http://purl.uniprot.org/annotation/VAR_044216|||http://purl.uniprot.org/annotation/VAR_044217|||http://purl.uniprot.org/annotation/VAR_044218|||http://purl.uniprot.org/annotation/VAR_044219|||http://purl.uniprot.org/annotation/VAR_044220|||http://purl.uniprot.org/annotation/VAR_044221|||http://purl.uniprot.org/annotation/VAR_044222|||http://purl.uniprot.org/annotation/VAR_044223|||http://purl.uniprot.org/annotation/VAR_044224
http://togogenome.org/gene/9606:MDFIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1T7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In LMPHM12.|||In LMPHM12; unknown pathological significance.|||In isoform 1.|||MDFI|||MyoD family inhibitor domain-containing protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280222|||http://purl.uniprot.org/annotation/VAR_087574|||http://purl.uniprot.org/annotation/VAR_087575|||http://purl.uniprot.org/annotation/VSP_037970
http://togogenome.org/gene/9606:SLC1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43007                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In SPATCCM; does not affect localization at the cell surface; decreased uptake of L-serine and L-alanine; Vmax is decreased by at least 50% for both substrates; 3-fold increase of affinity for L-serine; 2-fold increase of affinity for L-alanine.|||In SPATCCM; does not affect localization at the cell surface; loss of uptake of L-serine and L-alanine.|||In isoform 2.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neutral amino acid transporter A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202079|||http://purl.uniprot.org/annotation/VAR_011878|||http://purl.uniprot.org/annotation/VAR_011879|||http://purl.uniprot.org/annotation/VAR_075085|||http://purl.uniprot.org/annotation/VAR_075086|||http://purl.uniprot.org/annotation/VSP_042880|||http://purl.uniprot.org/annotation/VSP_042881
http://togogenome.org/gene/9606:MYLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KTQ1|||http://purl.uniprot.org/uniprot/Q05B97|||http://purl.uniprot.org/uniprot/Q05B98|||http://purl.uniprot.org/uniprot/Q15746                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||1-5; truncated|||2-1; truncated|||2-2|||2-3|||2-4|||2-5|||2-6|||5 X 28 AA approximate tandem repeats|||6 X 12 AA approximate tandem repeats|||Actin-binding (calcium/calmodulin-insensitive)|||Actin-binding (calcium/calmodulin-sensitive)|||Basic and acidic residues|||Calmodulin-binding|||Disordered|||Fibronectin type-III|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In AAT7; 4-fold reduced affinity for calmodulin; decreased kinase activity compared to wild-type protein.|||In AAT7; 7-fold reduced affinity for calmodulin; 6-fold decreased Vmax.|||In AAT7; decreases kinase activity.|||In AAT7; unknown pathological significance.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3B.|||In isoform 3A and isoform 3B.|||In isoform 4.|||In isoform 5 and isoform 9.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform Del-1790, isoform 8 and isoform 9.|||Loss of acetylation and no kinase activity repression by NAA10/ARD1.|||Myosin light chain kinase, smooth muscle|||Myosin light chain kinase, smooth muscle, deglutamylated form|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by ABL1 and SRC|||Phosphotyrosine; by SRC|||Polar residues|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024354|||http://purl.uniprot.org/annotation/PRO_0000403731|||http://purl.uniprot.org/annotation/VAR_019986|||http://purl.uniprot.org/annotation/VAR_019987|||http://purl.uniprot.org/annotation/VAR_040847|||http://purl.uniprot.org/annotation/VAR_040848|||http://purl.uniprot.org/annotation/VAR_040849|||http://purl.uniprot.org/annotation/VAR_040850|||http://purl.uniprot.org/annotation/VAR_040851|||http://purl.uniprot.org/annotation/VAR_040852|||http://purl.uniprot.org/annotation/VAR_040853|||http://purl.uniprot.org/annotation/VAR_040854|||http://purl.uniprot.org/annotation/VAR_040855|||http://purl.uniprot.org/annotation/VAR_040856|||http://purl.uniprot.org/annotation/VAR_040857|||http://purl.uniprot.org/annotation/VAR_040858|||http://purl.uniprot.org/annotation/VAR_040859|||http://purl.uniprot.org/annotation/VAR_057106|||http://purl.uniprot.org/annotation/VAR_057107|||http://purl.uniprot.org/annotation/VAR_057108|||http://purl.uniprot.org/annotation/VAR_057109|||http://purl.uniprot.org/annotation/VAR_065570|||http://purl.uniprot.org/annotation/VAR_065571|||http://purl.uniprot.org/annotation/VAR_065572|||http://purl.uniprot.org/annotation/VAR_065573|||http://purl.uniprot.org/annotation/VAR_065574|||http://purl.uniprot.org/annotation/VAR_065575|||http://purl.uniprot.org/annotation/VAR_065576|||http://purl.uniprot.org/annotation/VAR_065577|||http://purl.uniprot.org/annotation/VAR_083423|||http://purl.uniprot.org/annotation/VAR_083424|||http://purl.uniprot.org/annotation/VAR_083425|||http://purl.uniprot.org/annotation/VSP_004791|||http://purl.uniprot.org/annotation/VSP_004793|||http://purl.uniprot.org/annotation/VSP_004794|||http://purl.uniprot.org/annotation/VSP_004795|||http://purl.uniprot.org/annotation/VSP_018845|||http://purl.uniprot.org/annotation/VSP_018846|||http://purl.uniprot.org/annotation/VSP_053791
http://togogenome.org/gene/9606:CCNO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22674                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-O|||Disordered|||In CILD29.|||In CILD29; decreases formation of basal bodies in multiciliated cells.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000176175|||http://purl.uniprot.org/annotation/VAR_029081|||http://purl.uniprot.org/annotation/VAR_071197|||http://purl.uniprot.org/annotation/VAR_077581|||http://purl.uniprot.org/annotation/VSP_021655|||http://purl.uniprot.org/annotation/VSP_021656
http://togogenome.org/gene/9606:SURF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1G8|||http://purl.uniprot.org/uniprot/B7Z7A8|||http://purl.uniprot.org/uniprot/O15260                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Helical|||In isoform 2.|||In isoform 3.|||Removed|||Surfeit locus protein 4|||Targeted to the Golgi.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127664|||http://purl.uniprot.org/annotation/VSP_006307|||http://purl.uniprot.org/annotation/VSP_006308|||http://purl.uniprot.org/annotation/VSP_054686|||http://purl.uniprot.org/annotation/VSP_054687
http://togogenome.org/gene/9606:GABRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47870                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Displays reduced current rundown following repeated receptor activation.|||Extracellular|||Gamma-aminobutyric acid receptor subunit beta-2|||Helical|||In IECEE2; loss of localization to the cell membrane; retained intracellularly it affects the cell surface expression of the GABA receptor; decreased GABA receptor activity.|||In IECEE2; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000459|||http://purl.uniprot.org/annotation/VAR_080712|||http://purl.uniprot.org/annotation/VAR_080713|||http://purl.uniprot.org/annotation/VAR_080714|||http://purl.uniprot.org/annotation/VAR_080715|||http://purl.uniprot.org/annotation/VAR_080716|||http://purl.uniprot.org/annotation/VAR_080717|||http://purl.uniprot.org/annotation/VAR_080718|||http://purl.uniprot.org/annotation/VAR_080719|||http://purl.uniprot.org/annotation/VAR_080720|||http://purl.uniprot.org/annotation/VSP_038823|||http://purl.uniprot.org/annotation/VSP_038824|||http://purl.uniprot.org/annotation/VSP_038825|||http://purl.uniprot.org/annotation/VSP_038826|||http://purl.uniprot.org/annotation/VSP_038827|||http://purl.uniprot.org/annotation/VSP_038828
http://togogenome.org/gene/9606:PSMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13200                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||PC 1|||PC 2|||PC 3|||PC 4|||PC 5|||PC 6|||PC 7|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Required for interaction with UBLCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173810|||http://purl.uniprot.org/annotation/VAR_051554|||http://purl.uniprot.org/annotation/VAR_051555|||http://purl.uniprot.org/annotation/VAR_067451|||http://purl.uniprot.org/annotation/VSP_055065|||http://purl.uniprot.org/annotation/VSP_055066
http://togogenome.org/gene/9606:NCOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J0Q5|||http://purl.uniprot.org/uniprot/C9JE98|||http://purl.uniprot.org/uniprot/Q9Y618                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with TBL1X.|||Abolishes interaction with the apo LBD of RARA. No change on interaction on the addition of inverse agonist BMS493.|||Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493.|||Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||CORNR box of ID1|||CORNR box of ID2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH myb-type|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||Interaction with SIN3A/B|||Myb-like|||N6-acetyllysine|||Nuclear receptor corepressor 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with RARA in the absence of its ligand|||SANT|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055622|||http://purl.uniprot.org/annotation/VAR_054751|||http://purl.uniprot.org/annotation/VAR_060073|||http://purl.uniprot.org/annotation/VAR_060074|||http://purl.uniprot.org/annotation/VSP_003412|||http://purl.uniprot.org/annotation/VSP_003413|||http://purl.uniprot.org/annotation/VSP_036595
http://togogenome.org/gene/9606:HIF3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBI6|||http://purl.uniprot.org/uniprot/H0YDZ5|||http://purl.uniprot.org/uniprot/M0R104|||http://purl.uniprot.org/uniprot/Q9Y2N7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||BHLH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypoxia-inducible factor 3-alpha|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||LAPYISMD|||LRRLL|||NTAD|||No loss of ubiquitination. Reduced ubiquitination; when associated with R-467.|||No loss of ubiquitination. Reduced ubiquitination; when associated with R-570.|||Nuclear export signal|||Nuclear localization signal|||ODD|||PAS|||PAS 1|||PAS 2|||Polar residues|||Reduced hydroxylation activity. Reduced ubiquitination.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284414|||http://purl.uniprot.org/annotation/VAR_031731|||http://purl.uniprot.org/annotation/VAR_031732|||http://purl.uniprot.org/annotation/VSP_024518|||http://purl.uniprot.org/annotation/VSP_024519|||http://purl.uniprot.org/annotation/VSP_024520|||http://purl.uniprot.org/annotation/VSP_024521|||http://purl.uniprot.org/annotation/VSP_024523|||http://purl.uniprot.org/annotation/VSP_024525|||http://purl.uniprot.org/annotation/VSP_024526|||http://purl.uniprot.org/annotation/VSP_043429
http://togogenome.org/gene/9606:SNUPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95149                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with KPNB1 and m3G-cap U1 snRNP import receptor activity.|||Disordered|||IBB|||Interaction with m3G-cap structure|||N-acetylmethionine|||Necessary for binding to the m3G-cap structure|||Necessary for interaction with KPNB1 and m3G-cap U1 and U5 snRNP import receptor activity|||Necessary for interaction with XPO1|||Phosphoserine|||Polar residues|||Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity.|||Reduces binding to m3G-cap structure.|||Snurportin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191071
http://togogenome.org/gene/9606:CGGBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFW8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  CGG triplet repeat-binding protein 1|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252415
http://togogenome.org/gene/9606:TMEM45A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWC5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 45A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072569
http://togogenome.org/gene/9606:ACSM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FZ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A synthetase ACSM3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306097|||http://purl.uniprot.org/annotation/VAR_035249|||http://purl.uniprot.org/annotation/VAR_035250|||http://purl.uniprot.org/annotation/VAR_035251|||http://purl.uniprot.org/annotation/VAR_048239|||http://purl.uniprot.org/annotation/VSP_028395|||http://purl.uniprot.org/annotation/VSP_028396
http://togogenome.org/gene/9606:IFTAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VG3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Intraflagellar transport-associated protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288854|||http://purl.uniprot.org/annotation/VSP_025793
http://togogenome.org/gene/9606:GAGE12G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76087|||http://purl.uniprot.org/uniprot/P0CL80|||http://purl.uniprot.org/uniprot/P0CL81|||http://purl.uniprot.org/uniprot/P0CL82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12F|||G antigen 12G|||G antigen 12I|||G antigen 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148345|||http://purl.uniprot.org/annotation/PRO_0000311978|||http://purl.uniprot.org/annotation/PRO_0000407492|||http://purl.uniprot.org/annotation/PRO_0000407493|||http://purl.uniprot.org/annotation/VSP_040953
http://togogenome.org/gene/9606:GSTM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5E9|||http://purl.uniprot.org/uniprot/P28161|||http://purl.uniprot.org/uniprot/Q0D2I8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 2|||Important for substrate specificity|||In isoform 2.|||Phosphoserine|||Reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185818|||http://purl.uniprot.org/annotation/VAR_049486|||http://purl.uniprot.org/annotation/VSP_045614
http://togogenome.org/gene/9606:KLF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95600                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||Abolishes sumoylation. No change in nuclear location. Increases transcriptional activity and cell cycle progression. Abolishes sumoylation; when associated with R-217.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Krueppel-like factor 8|||No change in sumoylation. Abolishes sumoylation; when associated with R-67.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047176|||http://purl.uniprot.org/annotation/VSP_045460|||http://purl.uniprot.org/annotation/VSP_047480|||http://purl.uniprot.org/annotation/VSP_047481
http://togogenome.org/gene/9606:FAM25G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3EWG3|||http://purl.uniprot.org/uniprot/B3EWG5|||http://purl.uniprot.org/uniprot/B3EWG6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM25A|||Protein FAM25C|||Protein FAM25G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270919|||http://purl.uniprot.org/annotation/PRO_0000416047|||http://purl.uniprot.org/annotation/PRO_0000416048|||http://purl.uniprot.org/annotation/VAR_054062
http://togogenome.org/gene/9606:TBKBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MCY6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Homodimerization|||In isoform 2.|||Interaction with TBK1 and IKBKE|||Phosphoserine|||Polar residues|||Pro residues|||TANK-binding kinase 1-binding protein 1|||UBZ1-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324654|||http://purl.uniprot.org/annotation/VSP_052714|||http://purl.uniprot.org/annotation/VSP_052715
http://togogenome.org/gene/9606:SAP30L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes nucleolar localization.|||Atypical|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP30L|||Impairs nuclear localization.|||Important for DNA and phosphoinositide binding|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Redox-active|||Reduces transcriptional repressor activity, reduces localization in nucleoli, but has no effect on association with histone deacylase complexes.|||Strongly reduces affinity for DNA and for phosphoinositides.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309500|||http://purl.uniprot.org/annotation/VSP_046221|||http://purl.uniprot.org/annotation/VSP_046860
http://togogenome.org/gene/9606:OSBPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKJ8|||http://purl.uniprot.org/uniprot/E7ET92|||http://purl.uniprot.org/uniprot/Q9H1P3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Does not significantly impair 25-hydroxycholesterol binding.|||In isoform 2.|||Loss of increased cholesterol and decreased phosphatidylinositide accumulation at the cell membrane.|||Loss of the ability to promote cholesterol accumulation at the cell membrane. No effect on phosphatidylinositide levels at the cell membrane.|||Mildly decreased 25-hydroxycholesterol binding.|||No effect on phosphatidylinositide binding, but decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport.|||No effect on phosphatidylinositide binding, but impaired tetramerization and decreased cholesterol binding, plus decreased cholesterol and phosphatidylinositide transport.|||Oxysterol-binding protein-related protein 2|||Phosphoserine|||Polar residues|||Reduces 25-hydroxycholesterol binding.|||Reduces 25-hydroxycholesterol binding. Loss of 22(R)-hydroxycholesterol binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100369|||http://purl.uniprot.org/annotation/VSP_003781
http://togogenome.org/gene/9606:KRTAP4-9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||29 X 5 AA repeats of C-C-[RQVHIEK]-[SPTR]-[VSTQCRNP]|||3|||4|||5|||6|||7|||8|||9|||In allele KAP.9-v1.|||Keratin-associated protein 4-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185176|||http://purl.uniprot.org/annotation/VAR_064552
http://togogenome.org/gene/9606:OPLAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14841                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  5-oxoprolinase|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208577|||http://purl.uniprot.org/annotation/VAR_050425
http://togogenome.org/gene/9606:NOTO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein notochord|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343223|||http://purl.uniprot.org/annotation/VAR_059353|||http://purl.uniprot.org/annotation/VAR_059354
http://togogenome.org/gene/9606:RAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63000                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N6-palmitoyl lysine|||(Microbial infection) O-AMP-threonine; by Vibrio VopS|||(Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate|||(Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate|||(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB, and by P.sordellii toxin TcsL; alternate|||(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate|||Abolishes AMPylation by Haemophilus IbpA.|||Abolishes AMPylation by Vibrio VopS.|||Constitutively active. Interacts with PARD6 proteins. Increases nuclear localization and up-regulates transcriptional activity of NR3C2. Doesn't interact with CYRIB. Increases interaction with GARRE1.|||Constitutively active. Interacts with PARD6 proteins. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. No effect on interaction with RAPH1. Interacts with CYRIB. No interaction with PPP5C; when associated with V-30 or S-35. Translocates to the plasma membrane; also when associated with V-30 or S-35.|||Constitutively inactivated. Abolishes interaction with PARD6 proteins. No effect on NR3C2 transcriptional activity. No interaction with PPP5C. Doesn't activate PPP5C phosphatase activity and translocate PPP5C to the plasma membrane. Doesn't interact with CYRIB.|||Cysteine methyl ester|||Decreased palmitoylation by the V.cholerae toxin RtxA.|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In 2RA mutant; does not affect palmitoylation by the V.cholerae toxin RtxA.|||In 4KA mutant; abolished palmitoylation by the V.cholerae toxin RtxA.|||In MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation.|||In MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect.|||In MRD48; increased substrate adhesion-dependent cell spreading; constitutively active.|||In MRD48; unknown pathological significance.|||In isoform B.|||Loss of AKT-mediated phosphorylation and FBXL19-induced polyubiquitination.|||Loss of FBXL19-induced polyubiquitination.|||No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61.|||Phosphoserine|||Polybasic region; required for nuclear import|||Ras-related C3 botulinum toxin substrate 1|||Removed in mature form|||S-geranylgeranyl cysteine|||Slightly decreased palmitoylation by the V.cholerae toxin RtxA.|||Strongly reduced interaction with PLCB2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042036|||http://purl.uniprot.org/annotation/PRO_0000042037|||http://purl.uniprot.org/annotation/VAR_014540|||http://purl.uniprot.org/annotation/VAR_014541|||http://purl.uniprot.org/annotation/VAR_014542|||http://purl.uniprot.org/annotation/VAR_014543|||http://purl.uniprot.org/annotation/VAR_014544|||http://purl.uniprot.org/annotation/VAR_014545|||http://purl.uniprot.org/annotation/VAR_014546|||http://purl.uniprot.org/annotation/VAR_014547|||http://purl.uniprot.org/annotation/VAR_014548|||http://purl.uniprot.org/annotation/VAR_014549|||http://purl.uniprot.org/annotation/VAR_014550|||http://purl.uniprot.org/annotation/VAR_033303|||http://purl.uniprot.org/annotation/VAR_080454|||http://purl.uniprot.org/annotation/VAR_080455|||http://purl.uniprot.org/annotation/VAR_080456|||http://purl.uniprot.org/annotation/VAR_080457|||http://purl.uniprot.org/annotation/VAR_080458|||http://purl.uniprot.org/annotation/VAR_080459|||http://purl.uniprot.org/annotation/VAR_080460|||http://purl.uniprot.org/annotation/VSP_005710
http://togogenome.org/gene/9606:ASAH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0B6|||http://purl.uniprot.org/uniprot/Q13510|||http://purl.uniprot.org/uniprot/Q53H01                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acid ceramidase N-terminal|||Acid ceramidase subunit alpha|||Acid ceramidase subunit beta|||Choloylglycine hydrolase/NAAA C-terminal|||Decreased rate of autocatalytic processing.|||Important for catalytic activity|||In FRBRL.|||In FRBRL; decreased ceramide catabolic process.|||In FRBRL; loss of ceramidase activity.|||In FRBRL; unknown pathological significance.|||In FRBRL; unknown pathological significance; loss of ceramidase activity.|||In SMAPME; decreased protein abundance; alters the splicing of ASAH1 transcripts.|||In SMAPME; loss of protein abundance; the corresponding mRNA is not detected and probably degraded.|||In SMAPME; results in reduced activity.|||In SMAPME; unknown pathological significance; decreased ceramide catabolic process.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interchain (between alpha and beta subunits)|||Loss of autocatalytic processing. Loss of ceramidase activity.|||Loss of ceramide catabolic process.|||Mildly decreased autocatalytic processing. Loss of ceramidase activity.|||Moderately decreased autocatalytic processing, but loss of ceramidase activity, when associated with 169-Q--Q-171.|||Moderately decreased autocatalytic processing, but loss of ceramidase activity, when associated with Q-176.|||N-linked (GlcNAc...) asparagine|||No effect on autocatalytic processing, but loss of ceramidase activity, when associated with 165-Q--Q-167.|||No effect on autocatalytic processing, but loss of ceramidase activity, when associated with Q-80.|||No effect on autocatalytic processing, but strongly decreased ceramidase activity.|||No effect on ceramide catabolic process.|||Nucleophile|||Strongly decreased autocatalytic processing. Mildly decreased ceramidase activity.|||Strongly decreased autocatalytic processing. Moderately decreased ceramidase activity.|||Strongly decreased autocatalytic processing. Strongly decreased ceramidase activity.|||ceramidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002312|||http://purl.uniprot.org/annotation/PRO_0000002313|||http://purl.uniprot.org/annotation/PRO_5002725388|||http://purl.uniprot.org/annotation/PRO_5004249093|||http://purl.uniprot.org/annotation/VAR_008860|||http://purl.uniprot.org/annotation/VAR_008861|||http://purl.uniprot.org/annotation/VAR_008862|||http://purl.uniprot.org/annotation/VAR_021579|||http://purl.uniprot.org/annotation/VAR_021580|||http://purl.uniprot.org/annotation/VAR_021581|||http://purl.uniprot.org/annotation/VAR_021582|||http://purl.uniprot.org/annotation/VAR_021583|||http://purl.uniprot.org/annotation/VAR_021584|||http://purl.uniprot.org/annotation/VAR_021585|||http://purl.uniprot.org/annotation/VAR_021586|||http://purl.uniprot.org/annotation/VAR_021587|||http://purl.uniprot.org/annotation/VAR_038166|||http://purl.uniprot.org/annotation/VAR_038167|||http://purl.uniprot.org/annotation/VAR_038168|||http://purl.uniprot.org/annotation/VAR_038169|||http://purl.uniprot.org/annotation/VAR_038170|||http://purl.uniprot.org/annotation/VAR_057979|||http://purl.uniprot.org/annotation/VAR_057980|||http://purl.uniprot.org/annotation/VAR_068722|||http://purl.uniprot.org/annotation/VAR_071994|||http://purl.uniprot.org/annotation/VAR_071995|||http://purl.uniprot.org/annotation/VAR_072247|||http://purl.uniprot.org/annotation/VAR_081279|||http://purl.uniprot.org/annotation/VAR_081280|||http://purl.uniprot.org/annotation/VAR_081281|||http://purl.uniprot.org/annotation/VAR_081282|||http://purl.uniprot.org/annotation/VAR_082799|||http://purl.uniprot.org/annotation/VAR_082800|||http://purl.uniprot.org/annotation/VSP_037504|||http://purl.uniprot.org/annotation/VSP_046284|||http://purl.uniprot.org/annotation/VSP_046285
http://togogenome.org/gene/9606:SLC44A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJH4|||http://purl.uniprot.org/uniprot/A0A1U9X8K7|||http://purl.uniprot.org/uniprot/Q53GD3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Breakpoint for translocation with NEU1|||Choline transporter-like protein 4|||Cytoplasmic|||Decreases glycosylation levels. Decreases thiamine pyrophosphate uptake.|||Decreases glycosylation levels. No effect on thiamine pyrophosphate uptake.|||Extracellular|||Helical|||In DFNA72; decreases choline transmembrane transporter activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation.|||No effect on thiamine pyrophosphate transporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191723|||http://purl.uniprot.org/annotation/VAR_023406|||http://purl.uniprot.org/annotation/VAR_023407|||http://purl.uniprot.org/annotation/VAR_023408|||http://purl.uniprot.org/annotation/VAR_023409|||http://purl.uniprot.org/annotation/VAR_036210|||http://purl.uniprot.org/annotation/VAR_036211|||http://purl.uniprot.org/annotation/VAR_047020|||http://purl.uniprot.org/annotation/VAR_047021|||http://purl.uniprot.org/annotation/VAR_078848|||http://purl.uniprot.org/annotation/VAR_078849|||http://purl.uniprot.org/annotation/VSP_030998|||http://purl.uniprot.org/annotation/VSP_046236|||http://purl.uniprot.org/annotation/VSP_046821
http://togogenome.org/gene/9606:PNISR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T9Z6|||http://purl.uniprot.org/uniprot/A0A7P0Z4K1|||http://purl.uniprot.org/uniprot/Q3B7B6|||http://purl.uniprot.org/uniprot/Q6PJQ9|||http://purl.uniprot.org/uniprot/Q8TF01                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Arginine/serine-rich protein PNISR|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081947|||http://purl.uniprot.org/annotation/VSP_014458|||http://purl.uniprot.org/annotation/VSP_014459
http://togogenome.org/gene/9606:GNAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTJ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(t) subunit alpha-3|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342671
http://togogenome.org/gene/9606:CRACR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4Y2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 4A|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283044|||http://purl.uniprot.org/annotation/VAR_031479|||http://purl.uniprot.org/annotation/VAR_031480|||http://purl.uniprot.org/annotation/VAR_031481|||http://purl.uniprot.org/annotation/VAR_031482|||http://purl.uniprot.org/annotation/VSP_024290|||http://purl.uniprot.org/annotation/VSP_024291|||http://purl.uniprot.org/annotation/VSP_024292|||http://purl.uniprot.org/annotation/VSP_024293|||http://purl.uniprot.org/annotation/VSP_039545
http://togogenome.org/gene/9606:C1orf53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUE5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  Phosphoserine|||Uncharacterized protein C1orf53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271012
http://togogenome.org/gene/9606:POF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In POF2B; disrupts binding to nonmuscle actin filaments; abolishes tight junction localization; altered ciliogenesis and cystogenesis.|||In isoform 1.|||In isoform 3.|||Protein POF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253911|||http://purl.uniprot.org/annotation/VAR_028753|||http://purl.uniprot.org/annotation/VAR_028754|||http://purl.uniprot.org/annotation/VAR_028755|||http://purl.uniprot.org/annotation/VAR_028756|||http://purl.uniprot.org/annotation/VAR_028757|||http://purl.uniprot.org/annotation/VAR_028758|||http://purl.uniprot.org/annotation/VAR_028759|||http://purl.uniprot.org/annotation/VAR_028760|||http://purl.uniprot.org/annotation/VSP_021149|||http://purl.uniprot.org/annotation/VSP_021150|||http://purl.uniprot.org/annotation/VSP_021151
http://togogenome.org/gene/9606:MMEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS82|||http://purl.uniprot.org/uniprot/Q495T6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||Membrane metallo-endopeptidase-like 1|||Membrane metallo-endopeptidase-like 1, soluble form|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248415|||http://purl.uniprot.org/annotation/PRO_0000248416|||http://purl.uniprot.org/annotation/VAR_027348|||http://purl.uniprot.org/annotation/VSP_020287|||http://purl.uniprot.org/annotation/VSP_020288|||http://purl.uniprot.org/annotation/VSP_020289
http://togogenome.org/gene/9606:TMEM260                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX78                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished O-mannosyltransferase activity.|||Helical|||In SHDRA.|||In SHDRA; decreased stability.|||In SHDRA; reduced expression of isoform 1 due to nonsense-mediated decay in patient-derived cells.|||In SHDRA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase TMEM260                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089905|||http://purl.uniprot.org/annotation/VAR_057823|||http://purl.uniprot.org/annotation/VAR_057824|||http://purl.uniprot.org/annotation/VAR_078766|||http://purl.uniprot.org/annotation/VAR_088292|||http://purl.uniprot.org/annotation/VAR_088293|||http://purl.uniprot.org/annotation/VAR_088294|||http://purl.uniprot.org/annotation/VAR_088295|||http://purl.uniprot.org/annotation/VAR_088296|||http://purl.uniprot.org/annotation/VSP_008621|||http://purl.uniprot.org/annotation/VSP_058993|||http://purl.uniprot.org/annotation/VSP_058994
http://togogenome.org/gene/9606:TAFA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LR4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Chemokine-like protein TAFA-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042728
http://togogenome.org/gene/9606:TRIM39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCP5|||http://purl.uniprot.org/uniprot/Q9HCM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM39|||In isoform 2.|||Interaction with CDKN1A|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056257|||http://purl.uniprot.org/annotation/VSP_005755
http://togogenome.org/gene/9606:NEK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51957|||http://purl.uniprot.org/uniprot/Q05DF6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N6-methyllysine|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086425|||http://purl.uniprot.org/annotation/VAR_040915|||http://purl.uniprot.org/annotation/VAR_040916|||http://purl.uniprot.org/annotation/VAR_040917|||http://purl.uniprot.org/annotation/VAR_040918|||http://purl.uniprot.org/annotation/VAR_040919|||http://purl.uniprot.org/annotation/VAR_040920|||http://purl.uniprot.org/annotation/VAR_040921|||http://purl.uniprot.org/annotation/VSP_037123|||http://purl.uniprot.org/annotation/VSP_037124|||http://purl.uniprot.org/annotation/VSP_043334
http://togogenome.org/gene/9606:DHTKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-oxoadipate dehydrogenase complex component E1|||Disordered|||In AAKAD.|||In AAKAD; affects the overall activity of OADHC complex; affects assembly with DLST leading to impaired channeling of reaction intermediates.|||In AAKAD; decreased interaction with DLST.|||In AAKAD; unknown pathological significance.|||In AAKAD; unknown pathological significance; requires 2 nucleotide substitutions.|||In AAKAD; unknown pathological significance; thermally more labile than wild-type protein.|||Mitochondrion|||N6-succinyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307936|||http://purl.uniprot.org/annotation/VAR_036715|||http://purl.uniprot.org/annotation/VAR_036716|||http://purl.uniprot.org/annotation/VAR_036717|||http://purl.uniprot.org/annotation/VAR_036718|||http://purl.uniprot.org/annotation/VAR_036719|||http://purl.uniprot.org/annotation/VAR_069585|||http://purl.uniprot.org/annotation/VAR_085786|||http://purl.uniprot.org/annotation/VAR_085787|||http://purl.uniprot.org/annotation/VAR_085788|||http://purl.uniprot.org/annotation/VAR_085789|||http://purl.uniprot.org/annotation/VAR_085790|||http://purl.uniprot.org/annotation/VAR_085791|||http://purl.uniprot.org/annotation/VAR_085792
http://togogenome.org/gene/9606:HRH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTK7|||http://purl.uniprot.org/uniprot/P25021                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for histamine binding|||Essential for tiotidine binding and implicated in H2 selectivity|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Histamine H2 receptor|||Implicated in histamine binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069684|||http://purl.uniprot.org/annotation/VAR_009958|||http://purl.uniprot.org/annotation/VAR_009959|||http://purl.uniprot.org/annotation/VAR_009960|||http://purl.uniprot.org/annotation/VSP_043594
http://togogenome.org/gene/9606:DNASE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00115                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Deoxyribonuclease-2-alpha|||In AIPCS; complete loss of DNase activity in a single radial enzyme diffusion assay, confirmed by deficiency in DNA degradation in the granulocytes of a homozygous patient; no effect on expression level.|||In AIPCS; reduced DNase activity.|||In AIPCS; the genetic variation producing this missense variant predominantly affects splicing and the protein resulting from this aberrant splicing may be unstable; reduced DNase activity.|||In isoform 2.|||Loss of activity, but not of DNA-binding.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||No effect.|||Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-212; Q-266 and Q-290.|||Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-266.|||Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-290.|||Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-266 and Q-290.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007291|||http://purl.uniprot.org/annotation/VAR_012044|||http://purl.uniprot.org/annotation/VAR_048870|||http://purl.uniprot.org/annotation/VAR_048871|||http://purl.uniprot.org/annotation/VAR_087103|||http://purl.uniprot.org/annotation/VAR_087104|||http://purl.uniprot.org/annotation/VAR_087105|||http://purl.uniprot.org/annotation/VSP_056921
http://togogenome.org/gene/9606:OTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00480                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In OTCD.|||In OTCD; early onset; decreased ornithine carbamoyltransferase activity; 2.1% of wild-type activity.|||In OTCD; early onset; loss of ornithine carbamoyltransferase activity.|||In OTCD; early onset; loss of ornithine carbamoyltransferase activity; 0.9% of wild-type activity.|||In OTCD; female; late onset.|||In OTCD; late onset.|||In OTCD; late onset; decreased ornithine carbamoyltransferase activity; 8.9% activity.|||In OTCD; loss of ornithine carbamoyltransferase activity.|||In OTCD; mild.|||In OTCD; most common variant; loss of ornithine carbamoyltransferase activity; activity is 100-fold lower.|||In OTCD; neonatal.|||In OTCD; neonatal/late onset.|||In OTCD; neonatal; decreased ornithine carbamoyltransferase activity; 3.7% activity.|||Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-23.|||Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-15 and G-26.|||Loss of cleavage of the transit peptide and loss of localization to mitochondrial matrix; when associated with G-23 and G-26.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Ornithine transcarbamylase, mitochondrial|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020334|||http://purl.uniprot.org/annotation/VAR_004843|||http://purl.uniprot.org/annotation/VAR_004844|||http://purl.uniprot.org/annotation/VAR_004845|||http://purl.uniprot.org/annotation/VAR_004846|||http://purl.uniprot.org/annotation/VAR_004847|||http://purl.uniprot.org/annotation/VAR_004848|||http://purl.uniprot.org/annotation/VAR_004849|||http://purl.uniprot.org/annotation/VAR_004850|||http://purl.uniprot.org/annotation/VAR_004851|||http://purl.uniprot.org/annotation/VAR_004852|||http://purl.uniprot.org/annotation/VAR_004853|||http://purl.uniprot.org/annotation/VAR_004854|||http://purl.uniprot.org/annotation/VAR_004855|||http://purl.uniprot.org/annotation/VAR_004856|||http://purl.uniprot.org/annotation/VAR_004857|||http://purl.uniprot.org/annotation/VAR_004858|||http://purl.uniprot.org/annotation/VAR_004859|||http://purl.uniprot.org/annotation/VAR_004860|||http://purl.uniprot.org/annotation/VAR_004861|||http://purl.uniprot.org/annotation/VAR_004862|||http://purl.uniprot.org/annotation/VAR_004863|||http://purl.uniprot.org/annotation/VAR_004864|||http://purl.uniprot.org/annotation/VAR_004865|||http://purl.uniprot.org/annotation/VAR_004866|||http://purl.uniprot.org/annotation/VAR_004867|||http://purl.uniprot.org/annotation/VAR_004868|||http://purl.uniprot.org/annotation/VAR_004869|||http://purl.uniprot.org/annotation/VAR_004870|||http://purl.uniprot.org/annotation/VAR_004871|||http://purl.uniprot.org/annotation/VAR_004872|||http://purl.uniprot.org/annotation/VAR_004873|||http://purl.uniprot.org/annotation/VAR_004874|||http://purl.uniprot.org/annotation/VAR_004875|||http://purl.uniprot.org/annotation/VAR_004876|||http://purl.uniprot.org/annotation/VAR_004877|||http://purl.uniprot.org/annotation/VAR_004878|||http://purl.uniprot.org/annotation/VAR_004879|||http://purl.uniprot.org/annotation/VAR_004880|||http://purl.uniprot.org/annotation/VAR_004881|||http://purl.uniprot.org/annotation/VAR_004882|||http://purl.uniprot.org/annotation/VAR_004883|||http://purl.uniprot.org/annotation/VAR_004884|||http://purl.uniprot.org/annotation/VAR_004885|||http://purl.uniprot.org/annotation/VAR_004886|||http://purl.uniprot.org/annotation/VAR_004887|||http://purl.uniprot.org/annotation/VAR_004888|||http://purl.uniprot.org/annotation/VAR_004889|||http://purl.uniprot.org/annotation/VAR_004890|||http://purl.uniprot.org/annotation/VAR_004891|||http://purl.uniprot.org/annotation/VAR_004892|||http://purl.uniprot.org/annotation/VAR_004893|||http://purl.uniprot.org/annotation/VAR_004894|||http://purl.uniprot.org/annotation/VAR_004895|||http://purl.uniprot.org/annotation/VAR_004896|||http://purl.uniprot.org/annotation/VAR_004897|||http://purl.uniprot.org/annotation/VAR_004898|||http://purl.uniprot.org/annotation/VAR_004899|||http://purl.uniprot.org/annotation/VAR_004900|||http://purl.uniprot.org/annotation/VAR_004901|||http://purl.uniprot.org/annotation/VAR_004902|||http://purl.uniprot.org/annotation/VAR_004903|||http://purl.uniprot.org/annotation/VAR_004904|||http://purl.uniprot.org/annotation/VAR_004905|||http://purl.uniprot.org/annotation/VAR_004906|||http://purl.uniprot.org/annotation/VAR_004907|||http://purl.uniprot.org/annotation/VAR_004908|||http://purl.uniprot.org/annotation/VAR_004909|||http://purl.uniprot.org/annotation/VAR_004910|||http://purl.uniprot.org/annotation/VAR_004911|||http://purl.uniprot.org/annotation/VAR_004912|||http://purl.uniprot.org/annotation/VAR_004913|||http://purl.uniprot.org/annotation/VAR_004914|||http://purl.uniprot.org/annotation/VAR_004915|||http://purl.uniprot.org/annotation/VAR_004916|||http://purl.uniprot.org/annotation/VAR_004917|||http://purl.uniprot.org/annotation/VAR_004918|||http://purl.uniprot.org/annotation/VAR_004919|||http://purl.uniprot.org/annotation/VAR_004920|||http://purl.uniprot.org/annotation/VAR_004921|||http://purl.uniprot.org/annotation/VAR_004922|||http://purl.uniprot.org/annotation/VAR_004923|||http://purl.uniprot.org/annotation/VAR_004924|||http://purl.uniprot.org/annotation/VAR_004925|||http://purl.uniprot.org/annotation/VAR_004926|||http://purl.uniprot.org/annotation/VAR_004927|||http://purl.uniprot.org/annotation/VAR_004928|||http://purl.uniprot.org/annotation/VAR_004929|||http://purl.uniprot.org/annotation/VAR_004930|||http://purl.uniprot.org/annotation/VAR_004931|||http://purl.uniprot.org/annotation/VAR_004932|||http://purl.uniprot.org/annotation/VAR_004933|||http://purl.uniprot.org/annotation/VAR_004934|||http://purl.uniprot.org/annotation/VAR_004935|||http://purl.uniprot.org/annotation/VAR_004936|||http://purl.uniprot.org/annotation/VAR_004937|||http://purl.uniprot.org/annotation/VAR_004938|||http://purl.uniprot.org/annotation/VAR_004939|||http://purl.uniprot.org/annotation/VAR_004940|||http://purl.uniprot.org/annotation/VAR_004941|||http://purl.uniprot.org/annotation/VAR_004942|||http://purl.uniprot.org/annotation/VAR_004943|||http://purl.uniprot.org/annotation/VAR_004944|||http://purl.uniprot.org/annotation/VAR_004946|||http://purl.uniprot.org/annotation/VAR_004947|||http://purl.uniprot.org/annotation/VAR_004948|||http://purl.uniprot.org/annotation/VAR_009233|||http://purl.uniprot.org/annotation/VAR_009234|||http://purl.uniprot.org/annotation/VAR_009235|||http://purl.uniprot.org/annotation/VAR_010605|||http://purl.uniprot.org/annotation/VAR_010606|||http://purl.uniprot.org/annotation/VAR_010607|||http://purl.uniprot.org/annotation/VAR_010608|||http://purl.uniprot.org/annotation/VAR_010609|||http://purl.uniprot.org/annotation/VAR_010610|||http://purl.uniprot.org/annotation/VAR_012651|||http://purl.uniprot.org/annotation/VAR_012652|||http://purl.uniprot.org/annotation/VAR_012653|||http://purl.uniprot.org/annotation/VAR_012654|||http://purl.uniprot.org/annotation/VAR_012655|||http://purl.uniprot.org/annotation/VAR_012656|||http://purl.uniprot.org/annotation/VAR_012657
http://togogenome.org/gene/9606:CCDC51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ER9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial potassium channel|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288868|||http://purl.uniprot.org/annotation/VAR_032515|||http://purl.uniprot.org/annotation/VSP_025800
http://togogenome.org/gene/9606:RAB9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51151                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||Loss of interaction with HPS4; when associated with L-40 or L-44 or L-61.|||Loss of interaction with HPS4; when associated with L-66.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Ras-related protein Rab-9A|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121139
http://togogenome.org/gene/9606:NME6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG91|||http://purl.uniprot.org/uniprot/A0A2R8Y7V2|||http://purl.uniprot.org/uniprot/C9JQB1|||http://purl.uniprot.org/uniprot/O75414                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Nucleoside diphosphate kinase 6|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137127|||http://purl.uniprot.org/annotation/VSP_036882|||http://purl.uniprot.org/annotation/VSP_036883
http://togogenome.org/gene/9606:TTC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49A97|||http://purl.uniprot.org/uniprot/Q6MZP1|||http://purl.uniprot.org/uniprot/Q96AE7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Tetratricopeptide repeat protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106406|||http://purl.uniprot.org/annotation/VAR_034135|||http://purl.uniprot.org/annotation/VAR_052627|||http://purl.uniprot.org/annotation/VSP_056857|||http://purl.uniprot.org/annotation/VSP_056858|||http://purl.uniprot.org/annotation/VSP_056859
http://togogenome.org/gene/9606:MCF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9S6|||http://purl.uniprot.org/uniprot/P10911                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CRAL-TRIO|||DBL-transforming protein|||DH|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||MCF2-transforming protein|||PH|||Proto-oncogene DBL|||Spectrin|||Transformation capability reduced; no stimulation of GDP dissociation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030432|||http://purl.uniprot.org/annotation/PRO_0000030433|||http://purl.uniprot.org/annotation/PRO_0000030434|||http://purl.uniprot.org/annotation/VSP_008150|||http://purl.uniprot.org/annotation/VSP_008151|||http://purl.uniprot.org/annotation/VSP_008152|||http://purl.uniprot.org/annotation/VSP_008153|||http://purl.uniprot.org/annotation/VSP_046118
http://togogenome.org/gene/9606:KLRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26718                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Inhibits association with the HCST signaling dimer.|||N-linked (GlcNAc...) asparagine|||NKG2-D type II integral membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046665|||http://purl.uniprot.org/annotation/VAR_013295|||http://purl.uniprot.org/annotation/VAR_030738
http://togogenome.org/gene/9606:WFDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC57                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||WAP|||WAP four-disulfide core domain protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041365|||http://purl.uniprot.org/annotation/VAR_036489|||http://purl.uniprot.org/annotation/VAR_052948|||http://purl.uniprot.org/annotation/VAR_052949
http://togogenome.org/gene/9606:BATF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16520                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic leucine zipper transcriptional factor ATF-like|||Basic motif|||Disordered|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076595
http://togogenome.org/gene/9606:CLTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVQ6|||http://purl.uniprot.org/uniprot/Q00610                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding site for the uncoating ATPase, involved in lattice disassembly|||CHCR|||CHCR 1|||CHCR 2|||CHCR 3|||CHCR 4|||CHCR 5|||CHCR 6|||CHCR 7|||Clathrin heavy chain 1|||Clathrin heavy chain linker core motif|||Disrupts spindle localization and interaction with TACC3.|||Disrupts spindle localization.|||Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-506.|||Disrupts spindle localization; when associated with E-444, E-445, E-500 and E-507.|||Disrupts spindle localization; when associated with E-444, E-445, E-506 and E-507.|||Disrupts spindle localization; when associated with E-444, E-500, E-506 and E-507.|||Disrupts spindle localization; when associated with E-445, E-500 E-506 and E-507.|||Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-506.|||Disrupts spindle localization; when associated with E-481, E-487, E-500 and E-507.|||Disrupts spindle localization; when associated with E-481, E-487, E-506 and E-507.|||Disrupts spindle localization; when associated with E-481, E-500, E-506 and E-507.|||Disrupts spindle localization; when associated with E-487, E-500, E-506 and E-507.|||Distal segment|||Flexible linker|||Globular terminal domain|||Heavy chain arm|||In MRD56.|||In MRD56; unknown pathological significance.|||In isoform 2.|||Involved in binding clathrin light chain|||Involved in spindle localization and interaction with TACC3|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proximal segment|||Removed|||Trimerization|||WD40-like repeat 1|||WD40-like repeat 2|||WD40-like repeat 3|||WD40-like repeat 4|||WD40-like repeat 5|||WD40-like repeat 6|||WD40-like repeat 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205778|||http://purl.uniprot.org/annotation/VAR_080721|||http://purl.uniprot.org/annotation/VAR_080722|||http://purl.uniprot.org/annotation/VAR_080723|||http://purl.uniprot.org/annotation/VAR_080724|||http://purl.uniprot.org/annotation/VAR_080725|||http://purl.uniprot.org/annotation/VAR_080726|||http://purl.uniprot.org/annotation/VAR_080727|||http://purl.uniprot.org/annotation/VAR_080728|||http://purl.uniprot.org/annotation/VSP_011570|||http://purl.uniprot.org/annotation/VSP_011571
http://togogenome.org/gene/9606:POLR3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUI4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerase III subunit RPC3|||Disordered|||Loss of interaction with POLR3G and POLR3GL. No effect on interaction with POLR3F.|||Mild decrease in ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL.|||Phosphoserine|||Strongly decreased ssDNA-binding. No effect on interaction with POLR3F, POLR3G, nor with POLR3GL.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073963|||http://purl.uniprot.org/annotation/VAR_019083
http://togogenome.org/gene/9606:SSX4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60224                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||KRAB-related|||Polar residues|||Protein SSX4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181831|||http://purl.uniprot.org/annotation/VSP_054114|||http://purl.uniprot.org/annotation/VSP_054115
http://togogenome.org/gene/9606:AK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MA6                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Adenylate kinase 1|||Adenylate kinase 2|||Adenylate kinase 8|||In isoform 2.|||LID 1|||LID 2|||NMP 1|||NMP 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279383|||http://purl.uniprot.org/annotation/VAR_030873|||http://purl.uniprot.org/annotation/VAR_030874|||http://purl.uniprot.org/annotation/VSP_023419
http://togogenome.org/gene/9606:KRTAP9-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||16 X 5 AA repeats of C-C-[RQVSHE]-[SPTN]-[TASPI]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185189
http://togogenome.org/gene/9606:KCNJ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2X9V0|||http://purl.uniprot.org/uniprot/D2XBF0|||http://purl.uniprot.org/uniprot/P48549                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G protein-activated inward rectifier potassium channel 1|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In isoform 2.|||Inward rectifier potassium channel C-terminal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154938|||http://purl.uniprot.org/annotation/VAR_049669|||http://purl.uniprot.org/annotation/VSP_045432|||http://purl.uniprot.org/annotation/VSP_045433
http://togogenome.org/gene/9606:SOHLH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JUK2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In ODG5.|||In SPGF32; unknown pathological significance; does not have any significant effect on its transactivation.|||In isoform 2.|||Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315698|||http://purl.uniprot.org/annotation/VAR_038281|||http://purl.uniprot.org/annotation/VAR_038282|||http://purl.uniprot.org/annotation/VAR_064060|||http://purl.uniprot.org/annotation/VAR_064061|||http://purl.uniprot.org/annotation/VAR_080221|||http://purl.uniprot.org/annotation/VSP_039904
http://togogenome.org/gene/9606:LCN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDK0|||http://purl.uniprot.org/uniprot/Q6JVE9|||http://purl.uniprot.org/uniprot/Q6ZT51|||http://purl.uniprot.org/uniprot/Q8NBE9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Epididymal-specific lipocalin-8|||Helical|||In isoform 2.|||Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017916|||http://purl.uniprot.org/annotation/VSP_040219
http://togogenome.org/gene/9606:PRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14222                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Beta stranded; Name=CH1|||Beta stranded; Name=CH2|||C2|||EGF-like|||Important for oligomerization|||In FHL2.|||MACPF|||N-linked (GlcNAc...) asparagine|||Perforin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023609|||http://purl.uniprot.org/annotation/VAR_010744|||http://purl.uniprot.org/annotation/VAR_010745|||http://purl.uniprot.org/annotation/VAR_010746|||http://purl.uniprot.org/annotation/VAR_010747|||http://purl.uniprot.org/annotation/VAR_010748|||http://purl.uniprot.org/annotation/VAR_010749|||http://purl.uniprot.org/annotation/VAR_010772|||http://purl.uniprot.org/annotation/VAR_010773|||http://purl.uniprot.org/annotation/VAR_010774|||http://purl.uniprot.org/annotation/VAR_010775|||http://purl.uniprot.org/annotation/VAR_029773|||http://purl.uniprot.org/annotation/VAR_050482|||http://purl.uniprot.org/annotation/VAR_061504
http://togogenome.org/gene/9606:MOBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3W1|||http://purl.uniprot.org/uniprot/Q13875                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 10 AA tandem repeats of P-R-S-P-P-R-S-E-R-Q|||Basic and acidic residues|||Disordered|||FYVE-type zinc finger|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Myelin-associated oligodendrocyte basic protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281025|||http://purl.uniprot.org/annotation/VSP_023933|||http://purl.uniprot.org/annotation/VSP_023934|||http://purl.uniprot.org/annotation/VSP_023935|||http://purl.uniprot.org/annotation/VSP_055152
http://togogenome.org/gene/9606:TATDN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17R31                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Putative deoxyribonuclease TATDN3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313595|||http://purl.uniprot.org/annotation/VSP_030048|||http://purl.uniprot.org/annotation/VSP_044448|||http://purl.uniprot.org/annotation/VSP_045263|||http://purl.uniprot.org/annotation/VSP_045742
http://togogenome.org/gene/9606:DISP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2K9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein dispatched homolog 3|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308329|||http://purl.uniprot.org/annotation/VAR_036796|||http://purl.uniprot.org/annotation/VAR_036797|||http://purl.uniprot.org/annotation/VAR_036798|||http://purl.uniprot.org/annotation/VAR_036799|||http://purl.uniprot.org/annotation/VAR_036800|||http://purl.uniprot.org/annotation/VAR_061496|||http://purl.uniprot.org/annotation/VSP_028966
http://togogenome.org/gene/9606:LMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAP4|||http://purl.uniprot.org/uniprot/Q9NYC6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||LIM domain only protein 3|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075817|||http://purl.uniprot.org/annotation/VSP_045312|||http://purl.uniprot.org/annotation/VSP_045313|||http://purl.uniprot.org/annotation/VSP_047379
http://togogenome.org/gene/9606:SPMAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MV24                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Sperm microtubule associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340710|||http://purl.uniprot.org/annotation/VAR_044022
http://togogenome.org/gene/9606:PJA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43164                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase Praja-2|||In isoform 2.|||Interaction with PRKAR1A, PRKAR2A and PRKAR2B|||Mediates interaction with TBC1D31|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues|||RING-type; atypical|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278230|||http://purl.uniprot.org/annotation/VAR_030698|||http://purl.uniprot.org/annotation/VAR_030699|||http://purl.uniprot.org/annotation/VAR_057215|||http://purl.uniprot.org/annotation/VSP_023198
http://togogenome.org/gene/9606:RETN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD89                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interchain|||Resistin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030341|||http://purl.uniprot.org/annotation/VSP_055861
http://togogenome.org/gene/9606:BAIAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94812                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAI1-associated protein 3|||C2 1|||C2 2|||Disordered|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||MHD1|||MHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064819|||http://purl.uniprot.org/annotation/VAR_026667|||http://purl.uniprot.org/annotation/VAR_050687|||http://purl.uniprot.org/annotation/VSP_019231|||http://purl.uniprot.org/annotation/VSP_019232|||http://purl.uniprot.org/annotation/VSP_044673|||http://purl.uniprot.org/annotation/VSP_047000|||http://purl.uniprot.org/annotation/VSP_047001
http://togogenome.org/gene/9606:DEUP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PLX9|||http://purl.uniprot.org/uniprot/Q05D60                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Deuterosome assembly protein 1|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297829|||http://purl.uniprot.org/annotation/VAR_050759|||http://purl.uniprot.org/annotation/VAR_050760|||http://purl.uniprot.org/annotation/VAR_050761|||http://purl.uniprot.org/annotation/VAR_059601|||http://purl.uniprot.org/annotation/VSP_027367|||http://purl.uniprot.org/annotation/VSP_027368
http://togogenome.org/gene/9606:FGF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVY0|||http://purl.uniprot.org/uniprot/P11487                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor|||Fibroblast growth factor 3|||In LAMM.|||In LAMM; probably impairs secretion.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008946|||http://purl.uniprot.org/annotation/PRO_5033951579|||http://purl.uniprot.org/annotation/VAR_031848|||http://purl.uniprot.org/annotation/VAR_060492
http://togogenome.org/gene/9606:NUP35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFH5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Nucleoporin NUP35|||Phosphoserine|||Phosphothreonine|||RRM Nup35-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234294|||http://purl.uniprot.org/annotation/VSP_056210|||http://purl.uniprot.org/annotation/VSP_056211
http://togogenome.org/gene/9606:GRM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R693|||http://purl.uniprot.org/uniprot/B9EGG9|||http://purl.uniprot.org/uniprot/Q14831|||http://purl.uniprot.org/uniprot/Q59G95                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not rescue axon outgrowth defects when expressed in an heterologous system; when associated with K-675. Decreased protein abundance due to increased proteasomal degradation; when associated with K-675. Loss of localization to the cell membrane; when associated with K-675.|||Does not rescue axon outgrowth defects when expressed in an heterologous system; when associated with W-658. Decreased protein abundance due to increased proteasomal degradation; when associated with W-658. Loss of localization to the cell membrane; when associated with W-658.|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In NEDSHBA.|||In NEDSHBA; does not rescue axon outgrowth defects when expressed in an heterologous system.|||In NEDSHBA; does not rescue axon outgrowth defects when expressed in an heterologous system; decreased protein abundance; increased proteasomal degradation; decreased homodimerization; decreased localization to the cell membrane.|||In NEDSHBA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Metabotropic glutamate receptor 7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Rescues axon outgrowth defects when expressed in an heterologous system. Unchanged protein abundance. Does not affect localization to the plasma membrane. Does not affect N-glycosylation. Does not affect homodimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012938|||http://purl.uniprot.org/annotation/PRO_5002780101|||http://purl.uniprot.org/annotation/PRO_5002883268|||http://purl.uniprot.org/annotation/VAR_003584|||http://purl.uniprot.org/annotation/VAR_049276|||http://purl.uniprot.org/annotation/VAR_049277|||http://purl.uniprot.org/annotation/VAR_084620|||http://purl.uniprot.org/annotation/VAR_084621|||http://purl.uniprot.org/annotation/VAR_084622|||http://purl.uniprot.org/annotation/VAR_084623|||http://purl.uniprot.org/annotation/VAR_084624|||http://purl.uniprot.org/annotation/VAR_084625|||http://purl.uniprot.org/annotation/VAR_084626|||http://purl.uniprot.org/annotation/VAR_084627|||http://purl.uniprot.org/annotation/VSP_015732|||http://purl.uniprot.org/annotation/VSP_015733|||http://purl.uniprot.org/annotation/VSP_015734|||http://purl.uniprot.org/annotation/VSP_015735
http://togogenome.org/gene/9606:RGL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCN2|||http://purl.uniprot.org/uniprot/Q8IZJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Ral-GDS-related protein|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068890|||http://purl.uniprot.org/annotation/PRO_5004231340|||http://purl.uniprot.org/annotation/VAR_016244|||http://purl.uniprot.org/annotation/VAR_016245|||http://purl.uniprot.org/annotation/VAR_016246|||http://purl.uniprot.org/annotation/VAR_016247|||http://purl.uniprot.org/annotation/VAR_051905|||http://purl.uniprot.org/annotation/VAR_051906|||http://purl.uniprot.org/annotation/VAR_051907|||http://purl.uniprot.org/annotation/VAR_051908|||http://purl.uniprot.org/annotation/VSP_055850
http://togogenome.org/gene/9606:NXF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59E96|||http://purl.uniprot.org/uniprot/Q9UBU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||35% reduction in mRNA export activity.|||60% reduction in mRNA export activity.|||90% reduction in mRNA export activity.|||98% reduction in mRNA export activity.|||Abolishes interaction with THOC5 and CHTOP, no effect on interaction with NXT1; enhances intramolecular interaction between RBD and NTF2, reduces RNA binding and mRNA export.|||Abolishes interaction with THOC5 and CHTOP.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Decreases the export of mRNAs from the nucleus.|||Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-383. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and A-594.|||Diminishes nuclear rim staining and 80% reduction in mRNA export activity; when associated with R-386. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-386 and A-594.|||Disordered|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-100.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-91, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-89, A-97, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-82, A-91, A-97, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-81, A-89, A-91, A-97, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-78, A-82, A-89, A-91, A-97, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-71, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105.|||Greatly reduces RNA binding and no effect on interaction with ALYREF/THOC4; when associated with A-78, A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105.|||Impairs intramolecular interaction between RBD and NTF2.|||Impairs intramolecular interaction between RBD and NTF2; when associated with D-456.|||Impairs intramolecular interaction between RBD and NTF2; when associated with D-459.|||In isoform 2.|||Interaction with ALYREF/THOC4 and LUZP4|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Major non-specific RNA-binding|||Minor non-specific RNA-binding|||N-acetylalanine|||NTF2|||Nuclear RNA export factor 1|||Nuclear RNA export factor Tap RNA-binding|||Nuclear export signal|||Nuclear localization signal|||Omega-N-methylarginine; alternate|||Phosphoserine|||RNA-binding (RBD)|||RRM|||Removed|||Suppresses FG-nucleoporin binding.|||Suppresses FG-nucleoporin binding. Diminishes nuclear rim staining and 88% reduction in mRNA export activity. Complete loss of nuclear rim staining and mRNA export activity; when associated with R-383 and R-386.|||TAP-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220529|||http://purl.uniprot.org/annotation/VSP_041427|||http://purl.uniprot.org/annotation/VSP_041428
http://togogenome.org/gene/9606:MRPL51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4U2R6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL51|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273082|||http://purl.uniprot.org/annotation/VAR_030079
http://togogenome.org/gene/9606:TAPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJJ3|||http://purl.uniprot.org/uniprot/Q6NXT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In OCLSBG; causes mislocalization of the protein in the cytoplasm; impairs cilium formation.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Transmembrane anterior posterior transformation protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328872|||http://purl.uniprot.org/annotation/VAR_042568|||http://purl.uniprot.org/annotation/VAR_042569|||http://purl.uniprot.org/annotation/VAR_076497|||http://purl.uniprot.org/annotation/VSP_032842
http://togogenome.org/gene/9606:CRLF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0E2W4|||http://purl.uniprot.org/uniprot/Q9HC73                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytokine receptor-like factor 2|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011041|||http://purl.uniprot.org/annotation/PRO_5003007861|||http://purl.uniprot.org/annotation/VSP_008786|||http://purl.uniprot.org/annotation/VSP_008787|||http://purl.uniprot.org/annotation/VSP_057463
http://togogenome.org/gene/9606:APOA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4RUS7|||http://purl.uniprot.org/uniprot/Q6Q788                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Apolipoprotein A-V|||Associated with high plasma triglyceride levels.|||Decreased heparin-binding.|||In allele APOA5*3; associated with high plasma triglyceride levels.|||Phosphoserine|||Phosphothreonine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001981|||http://purl.uniprot.org/annotation/PRO_5014221346|||http://purl.uniprot.org/annotation/VAR_021165|||http://purl.uniprot.org/annotation/VAR_021166|||http://purl.uniprot.org/annotation/VAR_021167|||http://purl.uniprot.org/annotation/VAR_035124
http://togogenome.org/gene/9606:SERPIND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05546|||http://purl.uniprot.org/uniprot/Q8IVC0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X 11 AA approximate repeats, Asp/Glu-rich (acidic) (hirudin-like)|||Chemotactic activity|||Glycosaminoglycan-binding site|||Greatly reduced thrombin inhibition. Normal glycosaminoglycan affinity.|||Heparin cofactor 2|||In THPH10.|||In THPH10; Oslo; decreased affinity for dermatan sulfate.|||In THPH10; Tokushima; impaired secretion of the mutant molecules.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Normal thrombin inhibition and glycosaminoglycan affinity.|||Phosphoserine; by FAM20C|||Reactive bond|||Reduced heparin- and no dermatan sulfate-activated inhibition.|||Serpin|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032494|||http://purl.uniprot.org/annotation/PRO_5004308992|||http://purl.uniprot.org/annotation/VAR_007112|||http://purl.uniprot.org/annotation/VAR_011746|||http://purl.uniprot.org/annotation/VAR_011747|||http://purl.uniprot.org/annotation/VAR_011748|||http://purl.uniprot.org/annotation/VAR_011749|||http://purl.uniprot.org/annotation/VAR_051953|||http://purl.uniprot.org/annotation/VAR_051954|||http://purl.uniprot.org/annotation/VAR_054977|||http://purl.uniprot.org/annotation/VAR_054978
http://togogenome.org/gene/9606:PDCD6IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUM4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CEP55.|||Abolishes interaction with CEP55; inhibits support of cytokinesis.|||Abolishes interaction with CHMP4B and abolishes rescue of PTAP-type L domain-deficient HIV-1 p6.|||Abolishes interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6; no effect on cytokinesis, nor on midbody formation.|||Abolishes interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6.|||Abolishes interaction with SH3GL1 and SH3GL2; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6.|||Abolishes interaction with TSG101; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6.|||BRO1|||Decreased interaction with CEP55.|||Diminishes rescue of PTAP-type L domain-deficient HIV-1 p6.|||Disordered|||Does not support cytokinesis; loss of normal midbody formation; loss of CHMP4A-, CHMP4B- and CHMP4C-binding in a yeast two-hybrid assay; impairs rescue of PTAP-type L domain-deficient HIV-1 p6; no effect on localization to the midbody.|||Does not support cytokinesis; loss of normal midbody formation; loss of CHMP4A-, CHMP4B- and CHMP4C-binding in a yeast two-hybrid assay; no effect on localization to the midbody; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6.|||Does not support the formation of normal midbodies; loss of localization to the midbody; loss of CD2AP-, CEP55-, SH3GL2-, SH3KBP1-, TSG101-binding in a yeast two-hybrid assay.|||Essential to promote virus budding|||Greatly diminishes rescue of PTAP-type L domain--deficient HIV-1 p6.|||Greatly diminishes rescue of PTAP-type L domain-deficient HIV-1 p6.|||Impairs rescue of PTAP-type L domain-deficient HIV-1 p6.|||In isoform 2.|||In isoform 3.|||Interaction with CEP55|||Interaction with CHMP4A, CHMP4B and CHMP4C|||Interaction with EIAV p9|||Interaction with SDCBP|||Interaction with TSG101|||Loss of CEP55-binding in a yeast two-hybrid assay.|||Loss of homooligomerization; reduced TSG101-binding; impaired HIV-1 release.|||Loss of homoologimerization and reduced TSG101-binding; decreased HIV-1 release; no effect on cytokinesis. Almost complete loss of TSG101-binding and impaired cytokinesis; when associated with 717-A--A-720.|||Loss of interaction with SDCBP.|||Loss of midbody localization; does not support cytokinesis; loss of CEP55-binding in a yeast two-hybrid assay; no effect on HIV-1 release.|||N-acetylalanine|||N6-acetyllysine|||No effect on CEP55-binding in a yeast two-hybrid assay.|||No effect on interaction with HIV-1 p6.|||No effect on interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6.|||No effect on midbody formation, nor on cytokinesis; reduced TSG101-binding; no effect on HIV-1 release. Almost complete loss of TSG101-binding and impaired cytokinesis; when associated with 852-A--A-855.|||No effect on midbody formation; loss of CD2AP- and SH3KBP1-binding in a yeast two-hybrid assay; no effect on HIV-1 release.|||No effect on midbody formation; loss of SH3GL2-binding in a yeast two-hybrid assay.|||No effect on rescue of PTAP-type L domain-deficient HIV-1 p6.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Programmed cell death 6-interacting protein|||Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6.|||Removed|||Self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218891|||http://purl.uniprot.org/annotation/VAR_024381|||http://purl.uniprot.org/annotation/VAR_053017|||http://purl.uniprot.org/annotation/VAR_053018|||http://purl.uniprot.org/annotation/VAR_053019|||http://purl.uniprot.org/annotation/VAR_053020|||http://purl.uniprot.org/annotation/VAR_068975|||http://purl.uniprot.org/annotation/VAR_069765|||http://purl.uniprot.org/annotation/VSP_044860|||http://purl.uniprot.org/annotation/VSP_057190|||http://purl.uniprot.org/annotation/VSP_057191
http://togogenome.org/gene/9606:TIGD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Polar residues|||Tigger transposable element-derived protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272615
http://togogenome.org/gene/9606:RNF150                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RIE5|||http://purl.uniprot.org/uniprot/Q9ULK6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||PA|||RING finger protein 150|||RING-type|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280697|||http://purl.uniprot.org/annotation/VSP_023843|||http://purl.uniprot.org/annotation/VSP_023844|||http://purl.uniprot.org/annotation/VSP_023845|||http://purl.uniprot.org/annotation/VSP_023846|||http://purl.uniprot.org/annotation/VSP_023847
http://togogenome.org/gene/9606:CERS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished ceramide synthase activity.|||Ceramide synthase 6|||Cytoplasmic|||Decreased phosphorylation.|||Disordered|||Does not affect ceramide synthase activity.|||Helical|||Homeobox-like|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185516|||http://purl.uniprot.org/annotation/VSP_045162
http://togogenome.org/gene/9606:DPCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVM2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein DPCD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323723|||http://purl.uniprot.org/annotation/VAR_039574|||http://purl.uniprot.org/annotation/VAR_039575
http://togogenome.org/gene/9606:ZFP82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3Y299|||http://purl.uniprot.org/uniprot/Q8N141                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 82 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233164
http://togogenome.org/gene/9606:BTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06187|||http://purl.uniprot.org/uniprot/Q5JY90                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||CAV1-binding|||Defective in mediating calcium response.|||Disordered|||Found in patients with chronic lymphocytic leukemia; unknown pathological significance; results in resistance to ibrutinib therapy; results in a protein that is reversibly inhibited by ibrutinib; disrupts the covalent binding between the enzyme and ibrutinib.|||In XLA.|||In XLA; growth hormone deficiency.|||In XLA; loss of activity.|||In XLA; loss of phosphorylation of GTF2I.|||In XLA; mild.|||In XLA; mild; interferes with substrate binding and/or domain interactions.|||In XLA; mild; interferes with substrate binding.|||In XLA; moderate.|||In XLA; moderate; interferes with substrate binding.|||In XLA; no effect on phosphorylation of GTF2I.|||In XLA; severe.|||In XLA; severe; disturbs ATP-binding.|||In XLA; severe; prevents activation due to absence of contact between the catalytic loop and the regulatory phosphorylated residue.|||In a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.|||In isoform BTK-C.|||Inositol-(1,3,4,5)-tetrakisphosphate 1-binding|||Large decrease in binding by SH3BP5.|||Loss of phosphorylation of GTF2I.|||N-acetylalanine|||No effect on phosphorylation of GTF2I.|||PH|||Phosphoserine|||Phosphoserine; by PKC/PRKCB|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by LYN and SYK|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Tyrosine-protein kinase BTK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088065|||http://purl.uniprot.org/annotation/VAR_006216|||http://purl.uniprot.org/annotation/VAR_006217|||http://purl.uniprot.org/annotation/VAR_006218|||http://purl.uniprot.org/annotation/VAR_006219|||http://purl.uniprot.org/annotation/VAR_006220|||http://purl.uniprot.org/annotation/VAR_006221|||http://purl.uniprot.org/annotation/VAR_006222|||http://purl.uniprot.org/annotation/VAR_006223|||http://purl.uniprot.org/annotation/VAR_006224|||http://purl.uniprot.org/annotation/VAR_006225|||http://purl.uniprot.org/annotation/VAR_006226|||http://purl.uniprot.org/annotation/VAR_006227|||http://purl.uniprot.org/annotation/VAR_006228|||http://purl.uniprot.org/annotation/VAR_006229|||http://purl.uniprot.org/annotation/VAR_006230|||http://purl.uniprot.org/annotation/VAR_006231|||http://purl.uniprot.org/annotation/VAR_006232|||http://purl.uniprot.org/annotation/VAR_006233|||http://purl.uniprot.org/annotation/VAR_006234|||http://purl.uniprot.org/annotation/VAR_006235|||http://purl.uniprot.org/annotation/VAR_006236|||http://purl.uniprot.org/annotation/VAR_006237|||http://purl.uniprot.org/annotation/VAR_006238|||http://purl.uniprot.org/annotation/VAR_006239|||http://purl.uniprot.org/annotation/VAR_006240|||http://purl.uniprot.org/annotation/VAR_006241|||http://purl.uniprot.org/annotation/VAR_006242|||http://purl.uniprot.org/annotation/VAR_006243|||http://purl.uniprot.org/annotation/VAR_006244|||http://purl.uniprot.org/annotation/VAR_006245|||http://purl.uniprot.org/annotation/VAR_006246|||http://purl.uniprot.org/annotation/VAR_006247|||http://purl.uniprot.org/annotation/VAR_006248|||http://purl.uniprot.org/annotation/VAR_006249|||http://purl.uniprot.org/annotation/VAR_006251|||http://purl.uniprot.org/annotation/VAR_006252|||http://purl.uniprot.org/annotation/VAR_006253|||http://purl.uniprot.org/annotation/VAR_006254|||http://purl.uniprot.org/annotation/VAR_006255|||http://purl.uniprot.org/annotation/VAR_006256|||http://purl.uniprot.org/annotation/VAR_006257|||http://purl.uniprot.org/annotation/VAR_006258|||http://purl.uniprot.org/annotation/VAR_006259|||http://purl.uniprot.org/annotation/VAR_006260|||http://purl.uniprot.org/annotation/VAR_006261|||http://purl.uniprot.org/annotation/VAR_006262|||http://purl.uniprot.org/annotation/VAR_006263|||http://purl.uniprot.org/annotation/VAR_006264|||http://purl.uniprot.org/annotation/VAR_006265|||http://purl.uniprot.org/annotation/VAR_006267|||http://purl.uniprot.org/annotation/VAR_006268|||http://purl.uniprot.org/annotation/VAR_006269|||http://purl.uniprot.org/annotation/VAR_006270|||http://purl.uniprot.org/annotation/VAR_006271|||http://purl.uniprot.org/annotation/VAR_006272|||http://purl.uniprot.org/annotation/VAR_006273|||http://purl.uniprot.org/annotation/VAR_006274|||http://purl.uniprot.org/annotation/VAR_006275|||http://purl.uniprot.org/annotation/VAR_006276|||http://purl.uniprot.org/annotation/VAR_006277|||http://purl.uniprot.org/annotation/VAR_006278|||http://purl.uniprot.org/annotation/VAR_006279|||http://purl.uniprot.org/annotation/VAR_006280|||http://purl.uniprot.org/annotation/VAR_006281|||http://purl.uniprot.org/annotation/VAR_008291|||http://purl.uniprot.org/annotation/VAR_008292|||http://purl.uniprot.org/annotation/VAR_008293|||http://purl.uniprot.org/annotation/VAR_008294|||http://purl.uniprot.org/annotation/VAR_008295|||http://purl.uniprot.org/annotation/VAR_008296|||http://purl.uniprot.org/annotation/VAR_008297|||http://purl.uniprot.org/annotation/VAR_008298|||http://purl.uniprot.org/annotation/VAR_008299|||http://purl.uniprot.org/annotation/VAR_008300|||http://purl.uniprot.org/annotation/VAR_008301|||http://purl.uniprot.org/annotation/VAR_008302|||http://purl.uniprot.org/annotation/VAR_008303|||http://purl.uniprot.org/annotation/VAR_008304|||http://purl.uniprot.org/annotation/VAR_008305|||http://purl.uniprot.org/annotation/VAR_008306|||http://purl.uniprot.org/annotation/VAR_008307|||http://purl.uniprot.org/annotation/VAR_008308|||http://purl.uniprot.org/annotation/VAR_008309|||http://purl.uniprot.org/annotation/VAR_008310|||http://purl.uniprot.org/annotation/VAR_008311|||http://purl.uniprot.org/annotation/VAR_008312|||http://purl.uniprot.org/annotation/VAR_008313|||http://purl.uniprot.org/annotation/VAR_008314|||http://purl.uniprot.org/annotation/VAR_008315|||http://purl.uniprot.org/annotation/VAR_008316|||http://purl.uniprot.org/annotation/VAR_008317|||http://purl.uniprot.org/annotation/VAR_008318|||http://purl.uniprot.org/annotation/VAR_008319|||http://purl.uniprot.org/annotation/VAR_008320|||http://purl.uniprot.org/annotation/VAR_008321|||http://purl.uniprot.org/annotation/VAR_008322|||http://purl.uniprot.org/annotation/VAR_008323|||http://purl.uniprot.org/annotation/VAR_008324|||http://purl.uniprot.org/annotation/VAR_008325|||http://purl.uniprot.org/annotation/VAR_008326|||http://purl.uniprot.org/annotation/VAR_008327|||http://purl.uniprot.org/annotation/VAR_008328|||http://purl.uniprot.org/annotation/VAR_008330|||http://purl.uniprot.org/annotation/VAR_008331|||http://purl.uniprot.org/annotation/VAR_008332|||http://purl.uniprot.org/annotation/VAR_008333|||http://purl.uniprot.org/annotation/VAR_008334|||http://purl.uniprot.org/annotation/VAR_008335|||http://purl.uniprot.org/annotation/VAR_008960|||http://purl.uniprot.org/annotation/VAR_008961|||http://purl.uniprot.org/annotation/VAR_008962|||http://purl.uniprot.org/annotation/VAR_008963|||http://purl.uniprot.org/annotation/VAR_008964|||http://purl.uniprot.org/annotation/VAR_008965|||http://purl.uniprot.org/annotation/VAR_041676|||http://purl.uniprot.org/annotation/VAR_041677|||http://purl.uniprot.org/annotation/VAR_074309|||http://purl.uniprot.org/annotation/VSP_053838
http://togogenome.org/gene/9606:GRK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTQ7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Cysteine methyl ester|||In a metastatic melanoma sample; somatic mutation.|||No effect on kinase activity. Increase kinase activity; when associated with A-23.|||No effect on kinase activity. Increase kinase activity; when associated with A-36.|||Phosphoserine; by PKA|||Protein kinase|||Proton acceptor|||RGS|||Removed in mature form|||Rhodopsin kinase GRK7|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024332|||http://purl.uniprot.org/annotation/PRO_0000024333|||http://purl.uniprot.org/annotation/VAR_040527|||http://purl.uniprot.org/annotation/VAR_040528|||http://purl.uniprot.org/annotation/VAR_040529|||http://purl.uniprot.org/annotation/VAR_040530|||http://purl.uniprot.org/annotation/VAR_040531|||http://purl.uniprot.org/annotation/VAR_040532|||http://purl.uniprot.org/annotation/VAR_040533|||http://purl.uniprot.org/annotation/VAR_040534|||http://purl.uniprot.org/annotation/VAR_040535|||http://purl.uniprot.org/annotation/VAR_040536|||http://purl.uniprot.org/annotation/VAR_040537|||http://purl.uniprot.org/annotation/VAR_040538|||http://purl.uniprot.org/annotation/VAR_051624
http://togogenome.org/gene/9606:RSBN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 4.|||Lysine-specific demethylase 9|||Nuclear localization signal|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299412|||http://purl.uniprot.org/annotation/VSP_027656
http://togogenome.org/gene/9606:RGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08116                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||RGS|||Regulator of G-protein signaling 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204175|||http://purl.uniprot.org/annotation/VSP_036422
http://togogenome.org/gene/9606:ARGLU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Arginine and glutamate-rich protein 1|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288438|||http://purl.uniprot.org/annotation/VSP_025674|||http://purl.uniprot.org/annotation/VSP_053685
http://togogenome.org/gene/9606:OR2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95006                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150470|||http://purl.uniprot.org/annotation/VAR_022048|||http://purl.uniprot.org/annotation/VAR_034172|||http://purl.uniprot.org/annotation/VAR_034173
http://togogenome.org/gene/9606:VPS9D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2B5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||VPS9|||VPS9 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079279|||http://purl.uniprot.org/annotation/VSP_040306
http://togogenome.org/gene/9606:ARHGEF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN02|||http://purl.uniprot.org/uniprot/Q8IW93                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||PH|||Rho guanine nucleotide exchange factor 19|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285131|||http://purl.uniprot.org/annotation/VAR_031950|||http://purl.uniprot.org/annotation/VAR_031951|||http://purl.uniprot.org/annotation/VSP_024827
http://togogenome.org/gene/9606:MUC5AC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98088                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  107 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P|||17 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P|||34 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P|||58 X 8 AA approximate tandem repeats of T-T-S-T-T-S-A-P|||9 X Cys-rich subdomain repeats|||Abolishes cleavage.|||C-linked (Man) tryptophan|||CTCK|||Cleavage|||Cys-rich subdomain 1|||Cys-rich subdomain 2|||Cys-rich subdomain 3|||Cys-rich subdomain 4|||Cys-rich subdomain 5|||Cys-rich subdomain 6|||Cys-rich subdomain 7|||Cys-rich subdomain 8|||Cys-rich subdomain 9|||Disordered|||Mucin-5AC|||N-linked (GlcNAc...) asparagine|||No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum.|||O-linked (GalNAc) threonine|||Polar residues|||TIL 1|||TIL 2|||TIL 3|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158957|||http://purl.uniprot.org/annotation/VAR_036832
http://togogenome.org/gene/9606:VWA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||In HMNMYO.|||In HMNMYO; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphotyrosine|||Pro residues|||VWFA|||von Willebrand factor A domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307156|||http://purl.uniprot.org/annotation/VAR_085457|||http://purl.uniprot.org/annotation/VAR_085458|||http://purl.uniprot.org/annotation/VSP_028617|||http://purl.uniprot.org/annotation/VSP_046651|||http://purl.uniprot.org/annotation/VSP_046652
http://togogenome.org/gene/9606:USP27X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNY8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished deubiquitinase activity; impaired ability to mediate deubiquitination of CGAS.|||Abolished deubiquitinase activity; impaired ability to mediate deubiquitination of RIGI; when associated with A-380.|||Abolished deubiquitinase activity; impaired ability to mediate deubiquitination of RIGI; when associated with S-87.|||In XLID105.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306334|||http://purl.uniprot.org/annotation/VAR_077830
http://togogenome.org/gene/9606:UCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55089                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide                                                                                  ^@                                                                                  Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Reduced affinity for CRHR1.|||Reduced affinity for CRHR2.|||Strongly reduced affinity for CRHR2.|||Urocortin|||Valine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006233|||http://purl.uniprot.org/annotation/PRO_0000006234
http://togogenome.org/gene/9606:FOXD4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVK3|||http://purl.uniprot.org/uniprot/Q9NU39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091824|||http://purl.uniprot.org/annotation/VAR_059299
http://togogenome.org/gene/9606:CDIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2V0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CDAN1-interacting nuclease 1|||In CDAN1B.|||In CDAN1B; no effect on gene expression and protein level; impaired erythroid cell differentiation; no effect on nuclear and cytoplasmic location.|||In CDAN1B; reduced gene expression and protein level; impaired erythroid cell differentiation; increased S-phase of the cell-cycle; no effect on nuclear and cytoplasmic location.|||In CDAN1B; unknown pathological significance.|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271044|||http://purl.uniprot.org/annotation/VAR_059622|||http://purl.uniprot.org/annotation/VAR_070876|||http://purl.uniprot.org/annotation/VAR_070877|||http://purl.uniprot.org/annotation/VAR_082037|||http://purl.uniprot.org/annotation/VAR_082038|||http://purl.uniprot.org/annotation/VAR_082039|||http://purl.uniprot.org/annotation/VAR_082040|||http://purl.uniprot.org/annotation/VAR_086958|||http://purl.uniprot.org/annotation/VAR_086959|||http://purl.uniprot.org/annotation/VAR_086960|||http://purl.uniprot.org/annotation/VSP_022271
http://togogenome.org/gene/9606:TKFC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJH7|||http://purl.uniprot.org/uniprot/Q3LXA3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes both kinase and FMN cyclase activities.|||Abolishes kinase activity but not FMN cyclase activity.|||Decreases both kinase and FMN cyclase activities.|||DhaK|||DhaL|||Disordered|||Highly decreases kinase activity. No effect on FMN cyclase activity.|||In TKFCD; reduced protein levels in patient cells; very severe decrease of triokinase and glycerone kinase activities.|||In TKFCD; very severe decrease of triokinase and glycerone kinase activities.|||In isoform 2.|||Phosphoserine|||Slightly decreases kinase activity. No effect on FMN cyclase activity.|||Tele-hemiaminal-histidine intermediate|||Triokinase/FMN cyclase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121525|||http://purl.uniprot.org/annotation/VAR_028108|||http://purl.uniprot.org/annotation/VAR_054780|||http://purl.uniprot.org/annotation/VAR_083849|||http://purl.uniprot.org/annotation/VAR_083850|||http://purl.uniprot.org/annotation/VSP_057181
http://togogenome.org/gene/9606:DEPDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TB30                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEP|||DEP domain-containing protein 1A|||In isoform 2.|||Interaction with ZNF224|||Phosphoserine|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284786|||http://purl.uniprot.org/annotation/VAR_059798|||http://purl.uniprot.org/annotation/VSP_024652|||http://purl.uniprot.org/annotation/VSP_024653
http://togogenome.org/gene/9606:PMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIH7|||http://purl.uniprot.org/uniprot/B7ZAA0|||http://purl.uniprot.org/uniprot/I6L9H5|||http://purl.uniprot.org/uniprot/P54277|||http://purl.uniprot.org/uniprot/Q3BDU3                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||HMG box|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||PMS1 protein homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178004|||http://purl.uniprot.org/annotation/VAR_012967|||http://purl.uniprot.org/annotation/VAR_012968|||http://purl.uniprot.org/annotation/VAR_014877|||http://purl.uniprot.org/annotation/VAR_014878|||http://purl.uniprot.org/annotation/VAR_014879|||http://purl.uniprot.org/annotation/VAR_014880|||http://purl.uniprot.org/annotation/VAR_019166|||http://purl.uniprot.org/annotation/VSP_042676|||http://purl.uniprot.org/annotation/VSP_042677|||http://purl.uniprot.org/annotation/VSP_043371|||http://purl.uniprot.org/annotation/VSP_047692
http://togogenome.org/gene/9606:TBC1D10C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV04                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Carabin|||Disordered|||Glutamine finger|||In isoform 2.|||Interaction with calcineurin|||Loss of GAP activity.|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284467|||http://purl.uniprot.org/annotation/VSP_045992|||http://purl.uniprot.org/annotation/VSP_045993
http://togogenome.org/gene/9606:MC4R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32245                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Common variant associated with lower body mass index and obesity risk; also associated with lower risk for type 2 diabetes and coronary artery disease; increased MC4R signaling; increased surface expression.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In obesity.|||In obesity; completely unable to generate cAMP in response to ligand; shows evidence of impaired cell surface expression.|||In obesity; completely unable to generate cAMP in response to ligand; shows impaired cell surface expression.|||In obesity; decreased MC4R signaling; shows evidence of impaired cell surface expression.|||In obesity; does not bind alpha-MSH.|||In obesity; loss of plasma membrane localization; loss of receptor function.|||In obesity; no activity.|||In obesity; partial activity.|||In obesity; shows a partial cAMP response to alpha-MSH.|||In obesity; shows reduced cAMP response to alpha-MSH; retains normal affinity for the antagonist AGRP.|||In obesity; shows significantly impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor.|||In obesity; shows the same affinity as the wild-type but significant impairment of cAMP-induced activity in response to melanotan II compared with the wild-type receptor.|||In obesity; signaling properties in response to alpha-MSH, beta-MSH and gamma-1-MSH are impaired.|||In obesity; the mutant receptor is expressed well on the cell surface but is completely devoid of ligand binding and cAMP generation in response to agonist stimulation.|||Interchain|||Melanocortin receptor 4|||N-linked (GlcNAc...) asparagine|||No effect on MC4R signaling.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069722|||http://purl.uniprot.org/annotation/VAR_010704|||http://purl.uniprot.org/annotation/VAR_010705|||http://purl.uniprot.org/annotation/VAR_010706|||http://purl.uniprot.org/annotation/VAR_010707|||http://purl.uniprot.org/annotation/VAR_010708|||http://purl.uniprot.org/annotation/VAR_010709|||http://purl.uniprot.org/annotation/VAR_010710|||http://purl.uniprot.org/annotation/VAR_010711|||http://purl.uniprot.org/annotation/VAR_010712|||http://purl.uniprot.org/annotation/VAR_015357|||http://purl.uniprot.org/annotation/VAR_038632|||http://purl.uniprot.org/annotation/VAR_038633|||http://purl.uniprot.org/annotation/VAR_038634|||http://purl.uniprot.org/annotation/VAR_038635|||http://purl.uniprot.org/annotation/VAR_038636|||http://purl.uniprot.org/annotation/VAR_038637|||http://purl.uniprot.org/annotation/VAR_038638|||http://purl.uniprot.org/annotation/VAR_038639|||http://purl.uniprot.org/annotation/VAR_038640|||http://purl.uniprot.org/annotation/VAR_038641|||http://purl.uniprot.org/annotation/VAR_038642|||http://purl.uniprot.org/annotation/VAR_038643|||http://purl.uniprot.org/annotation/VAR_038644|||http://purl.uniprot.org/annotation/VAR_038645|||http://purl.uniprot.org/annotation/VAR_038646|||http://purl.uniprot.org/annotation/VAR_038647|||http://purl.uniprot.org/annotation/VAR_038648|||http://purl.uniprot.org/annotation/VAR_038649|||http://purl.uniprot.org/annotation/VAR_038650|||http://purl.uniprot.org/annotation/VAR_038651|||http://purl.uniprot.org/annotation/VAR_038652|||http://purl.uniprot.org/annotation/VAR_038653|||http://purl.uniprot.org/annotation/VAR_038654|||http://purl.uniprot.org/annotation/VAR_077570
http://togogenome.org/gene/9606:RBM38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0Z9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||RNA-binding protein 38|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081812|||http://purl.uniprot.org/annotation/VAR_015225|||http://purl.uniprot.org/annotation/VAR_015226|||http://purl.uniprot.org/annotation/VAR_015227|||http://purl.uniprot.org/annotation/VAR_059823|||http://purl.uniprot.org/annotation/VSP_035881
http://togogenome.org/gene/9606:GIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VXI9|||http://purl.uniprot.org/uniprot/F8W822|||http://purl.uniprot.org/uniprot/Q14161|||http://purl.uniprot.org/uniprot/Q68DM7|||http://purl.uniprot.org/uniprot/Q6FI58                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ARF GTPase-activating protein GIT1 C-terminal|||ARF GTPase-activating protein GIT2|||Arf GTPase-activating protein GIT1/2 coiled-coil|||Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 10.|||In isoform 2.|||In isoform 3, isoform 4, isoform 6 and isoform 11.|||In isoform 4 and isoform 8.|||In isoform 5, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 6, isoform 7 and isoform 11.|||In isoform 9.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074203|||http://purl.uniprot.org/annotation/VAR_024368|||http://purl.uniprot.org/annotation/VAR_048324|||http://purl.uniprot.org/annotation/VAR_048325|||http://purl.uniprot.org/annotation/VSP_000303|||http://purl.uniprot.org/annotation/VSP_000304|||http://purl.uniprot.org/annotation/VSP_000305|||http://purl.uniprot.org/annotation/VSP_000306|||http://purl.uniprot.org/annotation/VSP_000307|||http://purl.uniprot.org/annotation/VSP_000308|||http://purl.uniprot.org/annotation/VSP_000309|||http://purl.uniprot.org/annotation/VSP_008654|||http://purl.uniprot.org/annotation/VSP_026456
http://togogenome.org/gene/9606:CORO2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9S3|||http://purl.uniprot.org/uniprot/Q92828                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coronin-2A|||DUF1899|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050928|||http://purl.uniprot.org/annotation/VAR_053390|||http://purl.uniprot.org/annotation/VAR_053391
http://togogenome.org/gene/9606:SDR16C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3Y7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Epidermal retinol dehydrogenase 2|||Helical|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305973|||http://purl.uniprot.org/annotation/VAR_035234|||http://purl.uniprot.org/annotation/VSP_028389
http://togogenome.org/gene/9606:EHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R571|||http://purl.uniprot.org/uniprot/B2R5U3|||http://purl.uniprot.org/uniprot/Q9H4M9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATP-binding and localizes to cytoplasm.|||Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 1|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Greatly reduces oligomerization and interaction with RAB11FIP2.|||Loss of accumulation at the ciliary pocket. Loss of function in ciliogenesis. Abolishes interaction with RAB11FIP2. No effect on MICALL1 localization; when associated with E-483.|||Loss of accumulation at the ciliary pocket. Loss of function in ciliogenesis. Loss of association with tubulovesicular structures and altered MICALL1 localization. No effect on MICALL1 localization; when associated with A-485.|||Loss of interaction with MICALL1.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146109
http://togogenome.org/gene/9606:PAX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C0KTE5|||http://purl.uniprot.org/uniprot/C0KTF5|||http://purl.uniprot.org/uniprot/E7EQT0|||http://purl.uniprot.org/uniprot/E7ERK2|||http://purl.uniprot.org/uniprot/E7ERW5|||http://purl.uniprot.org/uniprot/E7ES87|||http://purl.uniprot.org/uniprot/Q02548                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form PAX5-ETV6|||Breakpoint for translocation to form PAX5-FOXP1|||Breakpoint for translocation to form PAX5-ZNF521|||Disordered|||In ALL3; confers susceptibility to ALL3; reduced transcription factor activity.|||In isoform 10.|||In isoform 11.|||In isoform 2 and isoform 9.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||PAI subdomain|||Paired|||Paired box protein Pax-5|||Polar residues|||Pro residues|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050183|||http://purl.uniprot.org/annotation/VAR_034370|||http://purl.uniprot.org/annotation/VAR_070672|||http://purl.uniprot.org/annotation/VAR_070673|||http://purl.uniprot.org/annotation/VAR_070674|||http://purl.uniprot.org/annotation/VAR_070675|||http://purl.uniprot.org/annotation/VAR_070676|||http://purl.uniprot.org/annotation/VAR_070677|||http://purl.uniprot.org/annotation/VAR_070678|||http://purl.uniprot.org/annotation/VAR_070679|||http://purl.uniprot.org/annotation/VAR_070680|||http://purl.uniprot.org/annotation/VAR_070681|||http://purl.uniprot.org/annotation/VAR_070682|||http://purl.uniprot.org/annotation/VAR_070683|||http://purl.uniprot.org/annotation/VAR_070684|||http://purl.uniprot.org/annotation/VAR_070685|||http://purl.uniprot.org/annotation/VAR_070686|||http://purl.uniprot.org/annotation/VSP_044115|||http://purl.uniprot.org/annotation/VSP_044116|||http://purl.uniprot.org/annotation/VSP_044117|||http://purl.uniprot.org/annotation/VSP_044118|||http://purl.uniprot.org/annotation/VSP_044119|||http://purl.uniprot.org/annotation/VSP_044120|||http://purl.uniprot.org/annotation/VSP_044121|||http://purl.uniprot.org/annotation/VSP_047827|||http://purl.uniprot.org/annotation/VSP_047828|||http://purl.uniprot.org/annotation/VSP_047829|||http://purl.uniprot.org/annotation/VSP_047830|||http://purl.uniprot.org/annotation/VSP_047831|||http://purl.uniprot.org/annotation/VSP_047832
http://togogenome.org/gene/9606:RAB4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61018                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl serotonin|||Cysteine methyl ester|||Effector region|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Ras-related protein Rab-4B|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121099|||http://purl.uniprot.org/annotation/VSP_013567
http://togogenome.org/gene/9606:KRTAP10-9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60411                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||25 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185217|||http://purl.uniprot.org/annotation/VAR_017739|||http://purl.uniprot.org/annotation/VAR_060052
http://togogenome.org/gene/9606:TGM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPS8|||http://purl.uniprot.org/uniprot/O43548                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In PSS2; completely abolishes the enzyme activity.|||In isoform Short.|||N-acetylalanine|||Polar residues|||Protein-glutamine gamma-glutamyltransferase 5|||Removed|||Transglutaminase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213713|||http://purl.uniprot.org/annotation/VAR_013248|||http://purl.uniprot.org/annotation/VAR_013249|||http://purl.uniprot.org/annotation/VAR_025848|||http://purl.uniprot.org/annotation/VAR_025849|||http://purl.uniprot.org/annotation/VAR_052564|||http://purl.uniprot.org/annotation/VAR_052565|||http://purl.uniprot.org/annotation/VSP_006415
http://togogenome.org/gene/9606:DNAAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQM4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal assembly factor 6|||In CILD36; almost complete loss of inner dynein arms and less loss of outer dynein arms in motor cilia; immotile cilia; abolishes interaction with DNAI2.|||In CILD36; almost complete loss of outer dynein arms and inner dynein arms in motor cilia; immotile cilia.|||In CILD36; defective preassembly of outer and inner dynein arms.|||In CILD36; no effect on expression at protein level; almost complete loss of outer dynein arms and inner dynein arms in motor cilia; immotile cilia; abolishes interaction with DNAI2.|||In CILD36; strongly decreased expression at protein level; almost complete loss of outer dynein arms and less loss of inner dynein arms in motor cilia; decreased cilia movement; no effect on trans-Golgi network location; abolishes interaction with DNAI2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079736|||http://purl.uniprot.org/annotation/VAR_078066|||http://purl.uniprot.org/annotation/VAR_083176|||http://purl.uniprot.org/annotation/VAR_083177|||http://purl.uniprot.org/annotation/VAR_083178|||http://purl.uniprot.org/annotation/VAR_083179
http://togogenome.org/gene/9606:ZBTB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVD4|||http://purl.uniprot.org/uniprot/Q9P1Z0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired HIPK2-mediated phosphorylation; when associated with A-795 and A-797.|||Impaired HIPK2-mediated phosphorylation; when associated with A-795 and A-983.|||Impaired HIPK2-mediated phosphorylation; when associated with A-797 and A-983.|||Interaction with CBFA2T3|||Phosphoserine|||Phosphothreonine; by HIPK2|||Polar residues|||Pro residues|||Zinc finger and BTB domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047712|||http://purl.uniprot.org/annotation/VAR_018383|||http://purl.uniprot.org/annotation/VAR_052913|||http://purl.uniprot.org/annotation/VAR_052914
http://togogenome.org/gene/9606:BMX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51813                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes almost completely the SRC-induced phosphorylation of BMX.|||Btk-type|||CAV1-binding|||Cytoplasmic tyrosine-protein kinase BMX|||In a lung large cell carcinoma sample; somatic mutation.|||PH|||Phosphotyrosine; by SRC and autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088063|||http://purl.uniprot.org/annotation/VAR_041674|||http://purl.uniprot.org/annotation/VAR_041675
http://togogenome.org/gene/9606:LIPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2IBA6|||http://purl.uniprot.org/uniprot/Q8WWY8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||In ARWH2.|||In HYPT7 and ARWH2.|||In HYPT7.|||Lipase|||Lipase member H|||Loss of lipase activity.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273321|||http://purl.uniprot.org/annotation/PRO_5014565290|||http://purl.uniprot.org/annotation/VAR_030125|||http://purl.uniprot.org/annotation/VAR_059050|||http://purl.uniprot.org/annotation/VAR_088344
http://togogenome.org/gene/9606:SPDYE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Speedy protein E5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328811
http://togogenome.org/gene/9606:PPFIA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75145                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Liprin-alpha-3|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191029|||http://purl.uniprot.org/annotation/VAR_017757|||http://purl.uniprot.org/annotation/VSP_009392
http://togogenome.org/gene/9606:FAM110A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pro residues|||Protein FAM110A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079435|||http://purl.uniprot.org/annotation/VAR_060150
http://togogenome.org/gene/9606:CD109                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YHK3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Bait region (approximate)|||CD109 antigen|||GPI-anchor amidated alanine|||In a colorectal cancer sample; somatic mutation.|||In allele Gov(b).|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255945|||http://purl.uniprot.org/annotation/PRO_0000255946|||http://purl.uniprot.org/annotation/VAR_028875|||http://purl.uniprot.org/annotation/VAR_028876|||http://purl.uniprot.org/annotation/VAR_028877|||http://purl.uniprot.org/annotation/VAR_028878|||http://purl.uniprot.org/annotation/VAR_028879|||http://purl.uniprot.org/annotation/VAR_036236|||http://purl.uniprot.org/annotation/VAR_036237|||http://purl.uniprot.org/annotation/VAR_048105|||http://purl.uniprot.org/annotation/VAR_048106|||http://purl.uniprot.org/annotation/VAR_048107|||http://purl.uniprot.org/annotation/VAR_048108|||http://purl.uniprot.org/annotation/VAR_074179|||http://purl.uniprot.org/annotation/VSP_021312|||http://purl.uniprot.org/annotation/VSP_021313|||http://purl.uniprot.org/annotation/VSP_021314|||http://purl.uniprot.org/annotation/VSP_021315
http://togogenome.org/gene/9606:VCAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19320                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In isoform 2.|||In isoform 3.|||Loss of RAC1 activation and subsequent leukocyte transmigration.|||N-linked (GlcNAc...) asparagine|||Soluble Vascular Cell Adhesion Molecule-1|||Vascular cell adhesion protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014997|||http://purl.uniprot.org/annotation/PRO_0000457762|||http://purl.uniprot.org/annotation/VAR_014309|||http://purl.uniprot.org/annotation/VAR_014310|||http://purl.uniprot.org/annotation/VAR_014311|||http://purl.uniprot.org/annotation/VAR_014312|||http://purl.uniprot.org/annotation/VAR_049951|||http://purl.uniprot.org/annotation/VAR_049952|||http://purl.uniprot.org/annotation/VAR_049953|||http://purl.uniprot.org/annotation/VSP_002580|||http://purl.uniprot.org/annotation/VSP_044636
http://togogenome.org/gene/9606:NNMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ53|||http://purl.uniprot.org/uniprot/P40261                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Citrulline; alternate|||Decreases N-methyltransferase activity.|||Has no effect on N-methyltransferase activity.|||Loss of N-methyltransferase activity like its citrullinated counterpart.|||Loss of N-methyltransferase activity.|||N6-acetyllysine|||Nicotinamide N-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159706
http://togogenome.org/gene/9606:FAM167B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTA0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Protein FAM167B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221434
http://togogenome.org/gene/9606:GALNT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXK2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In CRCS1.|||In CRCS1; germline mutation; loss of activity.|||In CRCS1; germline mutation; partial loss of activity.|||In CRCS1; germline mutation; reduction of activity.|||In CRCS1; somatic mutation; loss of activity.|||In isoform 2.|||Lumenal|||Polypeptide N-acetylgalactosaminyltransferase 12|||Pro residues|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059128|||http://purl.uniprot.org/annotation/VAR_064352|||http://purl.uniprot.org/annotation/VAR_064353|||http://purl.uniprot.org/annotation/VAR_064354|||http://purl.uniprot.org/annotation/VAR_064355|||http://purl.uniprot.org/annotation/VAR_064356|||http://purl.uniprot.org/annotation/VAR_064357|||http://purl.uniprot.org/annotation/VAR_064358|||http://purl.uniprot.org/annotation/VAR_064359|||http://purl.uniprot.org/annotation/VAR_064360|||http://purl.uniprot.org/annotation/VAR_064361|||http://purl.uniprot.org/annotation/VAR_064362|||http://purl.uniprot.org/annotation/VAR_064363|||http://purl.uniprot.org/annotation/VAR_064364|||http://purl.uniprot.org/annotation/VAR_068509|||http://purl.uniprot.org/annotation/VSP_011217
http://togogenome.org/gene/9606:FAM78B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0K0|||http://purl.uniprot.org/uniprot/Q5VT40                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Protein FAM78B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265114
http://togogenome.org/gene/9606:SIGLEC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43699                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014946|||http://purl.uniprot.org/annotation/VAR_014252|||http://purl.uniprot.org/annotation/VAR_014253|||http://purl.uniprot.org/annotation/VSP_002553|||http://purl.uniprot.org/annotation/VSP_002554|||http://purl.uniprot.org/annotation/VSP_035811|||http://purl.uniprot.org/annotation/VSP_035812|||http://purl.uniprot.org/annotation/VSP_045387|||http://purl.uniprot.org/annotation/VSP_045388|||http://purl.uniprot.org/annotation/VSP_046070
http://togogenome.org/gene/9606:IRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10914|||http://purl.uniprot.org/uniprot/Q6FHN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||IRF tryptophan pentad repeat|||In GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity.|||In GASC; the mutation abolishes DNA binding and transactivating activities.|||Interferon regulatory factor 1|||Large loss of sumoylation. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-275.|||Loss of acetylation. Partial loss of DNA-binding and transcriptional activity.|||N6-acetyllysine|||Polar residues|||Some loss of sumoylation. Partial inhibition of acetylation and activity. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-299.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154545|||http://purl.uniprot.org/annotation/VAR_065134|||http://purl.uniprot.org/annotation/VAR_065135
http://togogenome.org/gene/9606:TGFBI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Q2|||http://purl.uniprot.org/uniprot/Q15582                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Associated with Leu-124 in atypical granular dystrophy; French granular variant.|||Cell attachment site|||EMI|||FAS1|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||Found in lattice corneal dystrophy; unclassified form.|||Found in lattice corneal dystrophy; unclassified form; late-onset.|||In CDA; most common mutation in Japanese.|||In CDGG1; common mutation in Europe and United States; rare in Japan.|||In CDGG1; late-onset; mild ocular irritation and reduction in visual acuity.|||In CDL1.|||In CDL1; associated with D-546.|||In CDL1; associated with Q-551.|||In CDL1; cysteinylated; no effect on the disulfide bond pattern.|||In CDL1; delayed age of onset.|||In CDL1; late-onset and unilateral phenotype.|||In CDL1; late-onset.|||In CDL1; late-onset; found also in sporadic cases.|||In CDL1; severe phenotype; delayed age of onset.|||In CDL3A.|||In CDRB.|||In CDTB; originally thought to cause CDRB.|||In EBMD.|||In EBMD; unknown pathological significance.|||In asymmetric lattice corneal dystrophy.|||In granular corneal dystrophy; unclassified form; Hanoi.|||In granular corneal dystrophy; unclassified form; with centrifuge pattern of opacities.|||In lattice corneal dystrophy; unclassified form.|||Phosphoserine|||S-cysteinyl cysteine|||Transforming growth factor-beta-induced protein ig-h3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008769|||http://purl.uniprot.org/annotation/PRO_5006608252|||http://purl.uniprot.org/annotation/VAR_005077|||http://purl.uniprot.org/annotation/VAR_005078|||http://purl.uniprot.org/annotation/VAR_005079|||http://purl.uniprot.org/annotation/VAR_005080|||http://purl.uniprot.org/annotation/VAR_005081|||http://purl.uniprot.org/annotation/VAR_005082|||http://purl.uniprot.org/annotation/VAR_005083|||http://purl.uniprot.org/annotation/VAR_012444|||http://purl.uniprot.org/annotation/VAR_012445|||http://purl.uniprot.org/annotation/VAR_012446|||http://purl.uniprot.org/annotation/VAR_012447|||http://purl.uniprot.org/annotation/VAR_012448|||http://purl.uniprot.org/annotation/VAR_012449|||http://purl.uniprot.org/annotation/VAR_012450|||http://purl.uniprot.org/annotation/VAR_014335|||http://purl.uniprot.org/annotation/VAR_018484|||http://purl.uniprot.org/annotation/VAR_018485|||http://purl.uniprot.org/annotation/VAR_018486|||http://purl.uniprot.org/annotation/VAR_018487|||http://purl.uniprot.org/annotation/VAR_018488|||http://purl.uniprot.org/annotation/VAR_018489|||http://purl.uniprot.org/annotation/VAR_031531|||http://purl.uniprot.org/annotation/VAR_031532|||http://purl.uniprot.org/annotation/VAR_031533|||http://purl.uniprot.org/annotation/VAR_031534|||http://purl.uniprot.org/annotation/VAR_031535|||http://purl.uniprot.org/annotation/VAR_031536|||http://purl.uniprot.org/annotation/VAR_031537|||http://purl.uniprot.org/annotation/VAR_031538|||http://purl.uniprot.org/annotation/VAR_031539|||http://purl.uniprot.org/annotation/VAR_031540|||http://purl.uniprot.org/annotation/VAR_031541|||http://purl.uniprot.org/annotation/VAR_031542|||http://purl.uniprot.org/annotation/VAR_031543|||http://purl.uniprot.org/annotation/VAR_031544|||http://purl.uniprot.org/annotation/VAR_031545|||http://purl.uniprot.org/annotation/VAR_031546|||http://purl.uniprot.org/annotation/VAR_077904
http://togogenome.org/gene/9606:RNASE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34096|||http://purl.uniprot.org/uniprot/Q53XB4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Proton acceptor|||Proton donor|||Pyrrolidone carboxylic acid|||Ribonuclease 4|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030883|||http://purl.uniprot.org/annotation/PRO_5014205860|||http://purl.uniprot.org/annotation/VAR_024618
http://togogenome.org/gene/9606:AKAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24588|||http://purl.uniprot.org/uniprot/Q6PG46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  A kinase-anchoring proteins AKAP-5 and AKAP-12 calmodulin (CaM)-binding|||A-kinase anchor protein 5|||AKAP CaM-binding|||Basic and acidic residues|||Disordered|||Essential to the intracellular anchoring function|||Loss of palmitoylation by ZDHHC2; when associated with S-129.|||Loss of palmitoylation by ZDHHC2; when associated with S-36.|||PKA-RII subunit binding domain|||Phosphoserine|||Polar residues|||Prevents or diminishes RII binding.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064529|||http://purl.uniprot.org/annotation/VAR_056732|||http://purl.uniprot.org/annotation/VAR_056733|||http://purl.uniprot.org/annotation/VAR_060735
http://togogenome.org/gene/9606:MAP3K21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCX8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 21|||Phosphoserine|||Phosphoserine; by autocatalysis and MAP4K1|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086268|||http://purl.uniprot.org/annotation/VAR_040729|||http://purl.uniprot.org/annotation/VAR_040730|||http://purl.uniprot.org/annotation/VAR_040731|||http://purl.uniprot.org/annotation/VAR_040732|||http://purl.uniprot.org/annotation/VAR_040733|||http://purl.uniprot.org/annotation/VAR_040734|||http://purl.uniprot.org/annotation/VAR_040735|||http://purl.uniprot.org/annotation/VAR_040736|||http://purl.uniprot.org/annotation/VAR_040737|||http://purl.uniprot.org/annotation/VAR_040738|||http://purl.uniprot.org/annotation/VSP_051731|||http://purl.uniprot.org/annotation/VSP_051732|||http://purl.uniprot.org/annotation/VSP_051733|||http://purl.uniprot.org/annotation/VSP_051734
http://togogenome.org/gene/9606:ECE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPD6|||http://purl.uniprot.org/uniprot/P0DPD8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EEF1AKMT4-ECE2 readthrough transcript protein|||Endothelin-converting enzyme 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform ECE2-2.|||In isoform ECE2-3.|||Lumenal|||Methyltransferase-like region|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Phosphotyrosine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078223|||http://purl.uniprot.org/annotation/PRO_0000443293|||http://purl.uniprot.org/annotation/VAR_037085|||http://purl.uniprot.org/annotation/VSP_059324|||http://purl.uniprot.org/annotation/VSP_059325
http://togogenome.org/gene/9606:GPR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1DAM6|||http://purl.uniprot.org/uniprot/P46095                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 6|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069514|||http://purl.uniprot.org/annotation/VSP_055105
http://togogenome.org/gene/9606:CTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16619                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cardiotrophin-1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058762|||http://purl.uniprot.org/annotation/VAR_014938|||http://purl.uniprot.org/annotation/VSP_042725
http://togogenome.org/gene/9606:TSNAXIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXD0|||http://purl.uniprot.org/uniprot/E7ENJ7|||http://purl.uniprot.org/uniprot/Q2TAA8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Translin-associated factor X-interacting protein 1|||Translin-associated factor X-interacting protein 1 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323608|||http://purl.uniprot.org/annotation/VSP_052710
http://togogenome.org/gene/9606:CDC20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12834                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell division cycle protein 20 homolog|||Disordered|||Does not affect its ability to bind the APC/C complex; when associated with R-485.|||Does not affect its ability to bind the APC/C complex; when associated with R-490.|||Found in a patient with mosaic variagated aneuploidy syndrome 1; unknown pathological significance; decreased interaction with BUB1B during the formation of the mitotic checkpoint complex; shows normal kinetochore localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In OZEMA14.|||In OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization.|||In OZEMA14; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; slightly decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization.|||In OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; fails to localize to the kinetochore.|||In OZEMA14; severely decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization.|||In OZEMA14; unknown pathological significance.|||In OZEMA14; unknown pathological significance; decreased function in metaphase/anaphase transition of meiosis I; does not fully rescue metaphase I arrest in CDC20-knocked down mouse oocytes; decreased function in positive regulation of anaphase-promoting complex-dependent catabolic process; shows normal kinetochore localization.|||Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-72; A-153; A-157 and A-161.|||Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-41; A-92; A-153; A-157 and A-161.|||Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-153 and A-161.|||Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-42; A-72; A-92; A-157 and A-161.|||Loss of BUB1-mediated phosphorylation and inhibition and partially defective spindle-assembly checkpoint; when associated with A-72; A-92; A-153; A-157 and A-161.|||Loss of interaction with MAD2L1.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050900|||http://purl.uniprot.org/annotation/VAR_030368|||http://purl.uniprot.org/annotation/VAR_030369|||http://purl.uniprot.org/annotation/VAR_088388|||http://purl.uniprot.org/annotation/VAR_088389|||http://purl.uniprot.org/annotation/VAR_088390|||http://purl.uniprot.org/annotation/VAR_088391|||http://purl.uniprot.org/annotation/VAR_088392|||http://purl.uniprot.org/annotation/VAR_088393|||http://purl.uniprot.org/annotation/VAR_088394|||http://purl.uniprot.org/annotation/VAR_088395|||http://purl.uniprot.org/annotation/VAR_088396|||http://purl.uniprot.org/annotation/VAR_088397
http://togogenome.org/gene/9606:ANKRD24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF21                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 24|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328836|||http://purl.uniprot.org/annotation/VAR_042536|||http://purl.uniprot.org/annotation/VAR_042537|||http://purl.uniprot.org/annotation/VAR_042538|||http://purl.uniprot.org/annotation/VAR_042539|||http://purl.uniprot.org/annotation/VSP_032811
http://togogenome.org/gene/9606:IL36G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZH8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interleukin-36 gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153648|||http://purl.uniprot.org/annotation/PRO_0000430549|||http://purl.uniprot.org/annotation/VAR_024505|||http://purl.uniprot.org/annotation/VSP_013002
http://togogenome.org/gene/9606:PRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXM0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34|||35|||36|||37|||38|||39|||4|||40|||41|||42|||43|||44|||45|||46|||47|||48|||49|||5|||50|||51|||52|||53|||54|||55|||55 X 5 AA approximate tandem repeats of [LVMAG]-[PSREQC]-[EDKL]-[LIVMAP]-[AQKHRPE]; that may have a tripeptide spacer of [LV]-P-[KER]|||6|||7|||8|||9|||Acidic residues|||Disordered|||Found in a patient with a complex hereditary motor and sensory neuropathy form associated with dysarthria, joints hypermobility and cerebellar signs; unknown pathological significance.|||In CMT4F.|||In isoform 2.|||In isoform 3.|||Nearly abolishes export from the nucleus.|||Nuclear export signal|||Nuclear localization signal|||PDZ|||Periaxin|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058563|||http://purl.uniprot.org/annotation/VAR_013056|||http://purl.uniprot.org/annotation/VAR_013057|||http://purl.uniprot.org/annotation/VAR_013058|||http://purl.uniprot.org/annotation/VAR_013059|||http://purl.uniprot.org/annotation/VAR_013060|||http://purl.uniprot.org/annotation/VAR_013061|||http://purl.uniprot.org/annotation/VAR_013062|||http://purl.uniprot.org/annotation/VAR_013063|||http://purl.uniprot.org/annotation/VAR_013064|||http://purl.uniprot.org/annotation/VAR_013065|||http://purl.uniprot.org/annotation/VAR_069093|||http://purl.uniprot.org/annotation/VAR_073295|||http://purl.uniprot.org/annotation/VAR_073296|||http://purl.uniprot.org/annotation/VSP_004363|||http://purl.uniprot.org/annotation/VSP_004364|||http://purl.uniprot.org/annotation/VSP_040352
http://togogenome.org/gene/9606:IFNA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C2Z1|||http://purl.uniprot.org/uniprot/P01566                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016366|||http://purl.uniprot.org/annotation/PRO_5030868068|||http://purl.uniprot.org/annotation/VAR_029227
http://togogenome.org/gene/9606:SECTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVN6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Secreted and transmembrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022286
http://togogenome.org/gene/9606:PGRMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15173                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||Disordered|||Helical|||In isoform 2.|||Membrane-associated progesterone receptor component 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121743|||http://purl.uniprot.org/annotation/VSP_053500
http://togogenome.org/gene/9606:ZNF595                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B7G3|||http://purl.uniprot.org/uniprot/A0A075B7G4|||http://purl.uniprot.org/uniprot/B4DU56|||http://purl.uniprot.org/uniprot/B4DX79|||http://purl.uniprot.org/uniprot/Q8IYB9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 595                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047686|||http://purl.uniprot.org/annotation/VAR_061958
http://togogenome.org/gene/9606:PIK3AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUJ8|||http://purl.uniprot.org/uniprot/Q86YV3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DBB|||Disordered|||In isoform 2.|||In isoform 3.|||Necessary and sufficient to mediate inhibition of NF-kappa-B downstream of activated TLRs; may mediate interaction with MYD88 and TIRAP|||Phosphoinositide 3-kinase adapter protein 1|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by SYK|||Polar residues|||Pro residues|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341273|||http://purl.uniprot.org/annotation/VAR_044035|||http://purl.uniprot.org/annotation/VAR_044036|||http://purl.uniprot.org/annotation/VAR_044037|||http://purl.uniprot.org/annotation/VAR_044038|||http://purl.uniprot.org/annotation/VSP_034238|||http://purl.uniprot.org/annotation/VSP_034239|||http://purl.uniprot.org/annotation/VSP_034240
http://togogenome.org/gene/9606:SHROOM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY47|||http://purl.uniprot.org/uniprot/Q8TF72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ASD1|||ASD2|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Protein Shroom3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286066|||http://purl.uniprot.org/annotation/VAR_032062|||http://purl.uniprot.org/annotation/VAR_032063|||http://purl.uniprot.org/annotation/VAR_032064|||http://purl.uniprot.org/annotation/VAR_032065|||http://purl.uniprot.org/annotation/VSP_024965|||http://purl.uniprot.org/annotation/VSP_024966|||http://purl.uniprot.org/annotation/VSP_024967|||http://purl.uniprot.org/annotation/VSP_024968
http://togogenome.org/gene/9606:CFAP157                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JU67                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 157|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307224|||http://purl.uniprot.org/annotation/VAR_050845|||http://purl.uniprot.org/annotation/VSP_028641|||http://purl.uniprot.org/annotation/VSP_028642
http://togogenome.org/gene/9606:TMEM216                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QT25|||http://purl.uniprot.org/uniprot/Q9P0N5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In JBTS2 and MKS2.|||In JBTS2.|||In MKS2.|||In isoform 2 and isoform 3.|||In isoform 2.|||Transmembrane protein 216                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318955|||http://purl.uniprot.org/annotation/VAR_063388|||http://purl.uniprot.org/annotation/VAR_064028|||http://purl.uniprot.org/annotation/VAR_064029|||http://purl.uniprot.org/annotation/VAR_064030|||http://purl.uniprot.org/annotation/VAR_064031|||http://purl.uniprot.org/annotation/VAR_068170|||http://purl.uniprot.org/annotation/VSP_040295|||http://purl.uniprot.org/annotation/VSP_040296
http://togogenome.org/gene/9606:RNF111                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes SUMO binding.|||Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 326-A--A-329.|||Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 382-A--A-385.|||Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 326-A--A-329 and 382-A--A-385.|||Basic and acidic residues|||Basic residues|||Disordered|||E3 ubiquitin-protein ligase Arkadia|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interaction with AXIN1|||Loss of affinity to SUMO1 and SUMO2.|||No loss of affinity toward SUMO1 and SUMO2.|||Polar residues|||Pro residues|||RING-type; atypical|||SUMO interaction motif 1 (SIM)|||SUMO interaction motif 2 (SIM)|||SUMO interaction motif 3 (SIM)|||Ubiquitin binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280690|||http://purl.uniprot.org/annotation/VAR_031185|||http://purl.uniprot.org/annotation/VAR_057216|||http://purl.uniprot.org/annotation/VSP_023840|||http://purl.uniprot.org/annotation/VSP_023841
http://togogenome.org/gene/9606:PRR27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZM9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339182|||http://purl.uniprot.org/annotation/VAR_043927|||http://purl.uniprot.org/annotation/VAR_043928
http://togogenome.org/gene/9606:EARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPH6                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||In COXPD12.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Probable glutamate--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254560|||http://purl.uniprot.org/annotation/VAR_028840|||http://purl.uniprot.org/annotation/VAR_069235|||http://purl.uniprot.org/annotation/VAR_069236|||http://purl.uniprot.org/annotation/VAR_069237|||http://purl.uniprot.org/annotation/VAR_069238|||http://purl.uniprot.org/annotation/VAR_069239|||http://purl.uniprot.org/annotation/VAR_069240|||http://purl.uniprot.org/annotation/VAR_069241|||http://purl.uniprot.org/annotation/VAR_069242|||http://purl.uniprot.org/annotation/VAR_069243|||http://purl.uniprot.org/annotation/VAR_069244|||http://purl.uniprot.org/annotation/VAR_069245|||http://purl.uniprot.org/annotation/VAR_069246|||http://purl.uniprot.org/annotation/VAR_069247|||http://purl.uniprot.org/annotation/VAR_076183|||http://purl.uniprot.org/annotation/VAR_076184|||http://purl.uniprot.org/annotation/VSP_057203
http://togogenome.org/gene/9606:C2CD4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  C2|||C2 calcium-dependent domain-containing protein 4C|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293734
http://togogenome.org/gene/9606:LSM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4Z0|||http://purl.uniprot.org/uniprot/U3KQK1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Sm|||U6 snRNA-associated Sm-like protein LSm4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125564
http://togogenome.org/gene/9606:PYHIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6K0P9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HIN-200|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||Polar residues|||Pyrin|||Pyrin and HIN domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334524|||http://purl.uniprot.org/annotation/VSP_033657|||http://purl.uniprot.org/annotation/VSP_033658|||http://purl.uniprot.org/annotation/VSP_033659|||http://purl.uniprot.org/annotation/VSP_033660
http://togogenome.org/gene/9606:CTNS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3I9|||http://purl.uniprot.org/uniprot/A0A0S2Z3K3|||http://purl.uniprot.org/uniprot/I3L4A9|||http://purl.uniprot.org/uniprot/O60931                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished localization to the cell membrane. Does not affect cystine transport.|||Abolished steady-state transport current.|||Abolished steady-state transport current. Decreased midpoint potential.|||Abolished steady-state transport current. Decreased midpoint potential. Impaired dielectric distance. Accelerated the time course.|||Abolished transient cxurrents. Abolished steady-state transport current.|||Accelerated the time course.|||Cystinosin|||Cytoplasmic|||Decreased glycosylation.|||Decreased midpoint potential. Accelerated the time course.|||Disordered|||Does not affect cystine transport.|||Does not affect localization to the lysosome.|||Found in patients with cystinosis; uncertain pathological significance.|||Gain-of-function mutant that shows higher transport of cystine.|||Helical|||Impaired dielectric distance.|||In CTNS.|||In CTNS; abolished cystine transport.|||In CTNS; atypical; abolished cystine transport.|||In CTNS; atypical; does not affect cystine transport.|||In CTNS; atypical; slightly decreased cystine transport.|||In CTNS; does not affect cystine transport.|||In CTNS; partial relocation to the cell membrane; abolished cystine transport.|||In CTNSANN; decreased cystine transport.|||In CTNSJAN.|||In CTNSJAN; abolished cystine transport.|||In CTNSJAN; decreased cystine transport.|||In CTNSJAN; protein misfolding leading to decreased stability; decreased cystine transport.|||In delta(A) mutant; abolished localization to the lysosome; when associated with deletion of 362-G--L-366.|||In delta(B) mutant; does not abolish localization to the lysosome; when associated with deletion of 362-G--L-366.|||In isoform 2.|||In mu(a) mutant; abolished localization to the lysosome; when associated with deletion of 362-G--L-366.|||In mu(b) mutant; does not abolish localization to the lysosome; when associated with deletion of 362-G--L-366.|||Lumenal|||Lysosomal targeting motif|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||PQ-loop 1|||PQ-loop 2|||Slightly decreased cystine transport.|||Slightly decreased midpoint potential. Impaired dielectric distance.|||Strongly reduced but not abolished localization to the lysosome, leading to partial relocation to the cell membrane.|||Strongly reduced but not abolished localization to the lysosome, leading to partial relocation to the cell membrane. Abolished localization to the lysosome; when associated with 281-A--A-284 or deletion of 280-K--N-288. Does not abolish localization to the lysosome; when associated with 286-A--A-289 or deletion of 289-F--S-298.|||Strongly reduced steady-state transport current. Slightly decreased midpoint potential.|||protonated residue following cystine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205514|||http://purl.uniprot.org/annotation/PRO_5006608210|||http://purl.uniprot.org/annotation/PRO_5006608255|||http://purl.uniprot.org/annotation/VAR_010285|||http://purl.uniprot.org/annotation/VAR_010286|||http://purl.uniprot.org/annotation/VAR_010287|||http://purl.uniprot.org/annotation/VAR_010288|||http://purl.uniprot.org/annotation/VAR_010674|||http://purl.uniprot.org/annotation/VAR_010677|||http://purl.uniprot.org/annotation/VAR_010678|||http://purl.uniprot.org/annotation/VAR_010679|||http://purl.uniprot.org/annotation/VAR_010680|||http://purl.uniprot.org/annotation/VAR_010681|||http://purl.uniprot.org/annotation/VAR_010682|||http://purl.uniprot.org/annotation/VAR_010683|||http://purl.uniprot.org/annotation/VAR_010684|||http://purl.uniprot.org/annotation/VAR_010689|||http://purl.uniprot.org/annotation/VAR_010690|||http://purl.uniprot.org/annotation/VAR_010691|||http://purl.uniprot.org/annotation/VAR_010692|||http://purl.uniprot.org/annotation/VAR_010694|||http://purl.uniprot.org/annotation/VAR_010695|||http://purl.uniprot.org/annotation/VAR_010697|||http://purl.uniprot.org/annotation/VAR_010698|||http://purl.uniprot.org/annotation/VAR_012314|||http://purl.uniprot.org/annotation/VAR_012315|||http://purl.uniprot.org/annotation/VAR_037318|||http://purl.uniprot.org/annotation/VAR_037319|||http://purl.uniprot.org/annotation/VAR_037320|||http://purl.uniprot.org/annotation/VAR_037321|||http://purl.uniprot.org/annotation/VAR_037322|||http://purl.uniprot.org/annotation/VAR_037323|||http://purl.uniprot.org/annotation/VAR_037324|||http://purl.uniprot.org/annotation/VAR_060371|||http://purl.uniprot.org/annotation/VAR_067490|||http://purl.uniprot.org/annotation/VAR_067491|||http://purl.uniprot.org/annotation/VAR_067492|||http://purl.uniprot.org/annotation/VAR_067493|||http://purl.uniprot.org/annotation/VAR_067494|||http://purl.uniprot.org/annotation/VAR_067495|||http://purl.uniprot.org/annotation/VAR_067496|||http://purl.uniprot.org/annotation/VAR_067497|||http://purl.uniprot.org/annotation/VAR_067498|||http://purl.uniprot.org/annotation/VAR_084186|||http://purl.uniprot.org/annotation/VSP_038377
http://togogenome.org/gene/9606:UGT2B10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36537                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 2B10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036034|||http://purl.uniprot.org/annotation/VSP_054337
http://togogenome.org/gene/9606:FDXR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSZ4|||http://purl.uniprot.org/uniprot/A0A0A0MT64|||http://purl.uniprot.org/uniprot/A0A0A0MTN9|||http://purl.uniprot.org/uniprot/A0A0A0MTR6|||http://purl.uniprot.org/uniprot/A0A0C4DFN8|||http://purl.uniprot.org/uniprot/A0A0C4DGN7|||http://purl.uniprot.org/uniprot/P22570                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAD/NAD(P)-binding|||In ANOA.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform Long.|||Mitochondrion|||NADPH:adrenodoxin oxidoreductase, mitochondrial|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019420|||http://purl.uniprot.org/annotation/VAR_004624|||http://purl.uniprot.org/annotation/VAR_025192|||http://purl.uniprot.org/annotation/VAR_025193|||http://purl.uniprot.org/annotation/VAR_025194|||http://purl.uniprot.org/annotation/VAR_025195|||http://purl.uniprot.org/annotation/VAR_025196|||http://purl.uniprot.org/annotation/VAR_025197|||http://purl.uniprot.org/annotation/VAR_025198|||http://purl.uniprot.org/annotation/VAR_025199|||http://purl.uniprot.org/annotation/VAR_080376|||http://purl.uniprot.org/annotation/VAR_080377|||http://purl.uniprot.org/annotation/VAR_080378|||http://purl.uniprot.org/annotation/VAR_080379|||http://purl.uniprot.org/annotation/VAR_080380|||http://purl.uniprot.org/annotation/VSP_003416|||http://purl.uniprot.org/annotation/VSP_045135|||http://purl.uniprot.org/annotation/VSP_046669|||http://purl.uniprot.org/annotation/VSP_046670|||http://purl.uniprot.org/annotation/VSP_046671|||http://purl.uniprot.org/annotation/VSP_046672|||http://purl.uniprot.org/annotation/VSP_046673
http://togogenome.org/gene/9606:PPP1R18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCJ8|||http://purl.uniprot.org/uniprot/Q6NYC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-542.|||Decrease binding to PP1. Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-540.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phostensin|||Phostensin/Taperin N-terminal|||Phostensin/Taperin PP1-binding|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050807|||http://purl.uniprot.org/annotation/VAR_034045|||http://purl.uniprot.org/annotation/VAR_046132|||http://purl.uniprot.org/annotation/VAR_046133|||http://purl.uniprot.org/annotation/VSP_014258|||http://purl.uniprot.org/annotation/VSP_014259|||http://purl.uniprot.org/annotation/VSP_057117|||http://purl.uniprot.org/annotation/VSP_057118|||http://purl.uniprot.org/annotation/VSP_057119
http://togogenome.org/gene/9606:NOX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227596|||http://purl.uniprot.org/annotation/VAR_049103
http://togogenome.org/gene/9606:MSMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15800                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In MCCPD.|||In MCCPD; unknown pathological significance.|||In isoform 2.|||Methylsterol monooxygenase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117033|||http://purl.uniprot.org/annotation/VAR_048898|||http://purl.uniprot.org/annotation/VAR_076531|||http://purl.uniprot.org/annotation/VAR_076532|||http://purl.uniprot.org/annotation/VAR_076533|||http://purl.uniprot.org/annotation/VSP_044585
http://togogenome.org/gene/9606:ISM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AKI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  AMOP|||Basic and acidic residues|||Disordered|||Isthmin-1|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348256|||http://purl.uniprot.org/annotation/VAR_052664
http://togogenome.org/gene/9606:UBR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4S7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR4|||Helical|||In a breast cancer sample; somatic mutation.|||In a melanoma patient.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286861|||http://purl.uniprot.org/annotation/VAR_032193|||http://purl.uniprot.org/annotation/VAR_032194|||http://purl.uniprot.org/annotation/VAR_032195|||http://purl.uniprot.org/annotation/VAR_032196|||http://purl.uniprot.org/annotation/VAR_035540|||http://purl.uniprot.org/annotation/VSP_025200|||http://purl.uniprot.org/annotation/VSP_025201|||http://purl.uniprot.org/annotation/VSP_025202|||http://purl.uniprot.org/annotation/VSP_025203|||http://purl.uniprot.org/annotation/VSP_025204|||http://purl.uniprot.org/annotation/VSP_025205|||http://purl.uniprot.org/annotation/VSP_025206|||http://purl.uniprot.org/annotation/VSP_025207|||http://purl.uniprot.org/annotation/VSP_025208|||http://purl.uniprot.org/annotation/VSP_025209
http://togogenome.org/gene/9606:H2AC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99878                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 1-J|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055239
http://togogenome.org/gene/9606:UNC93A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WB7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein unc-93 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190036|||http://purl.uniprot.org/annotation/VAR_022650|||http://purl.uniprot.org/annotation/VAR_022651|||http://purl.uniprot.org/annotation/VAR_022652|||http://purl.uniprot.org/annotation/VAR_022653|||http://purl.uniprot.org/annotation/VAR_022654|||http://purl.uniprot.org/annotation/VAR_052473|||http://purl.uniprot.org/annotation/VAR_052474|||http://purl.uniprot.org/annotation/VAR_052475|||http://purl.uniprot.org/annotation/VAR_059849|||http://purl.uniprot.org/annotation/VAR_061874|||http://purl.uniprot.org/annotation/VSP_042772
http://togogenome.org/gene/9606:TRABD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IYB5|||http://purl.uniprot.org/uniprot/Q86V40                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Metalloprotease TIKI|||Metalloprotease TIKI1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325807|||http://purl.uniprot.org/annotation/PRO_5002997061|||http://purl.uniprot.org/annotation/VAR_039920|||http://purl.uniprot.org/annotation/VAR_039921|||http://purl.uniprot.org/annotation/VAR_039922|||http://purl.uniprot.org/annotation/VSP_038837
http://togogenome.org/gene/9606:ARMC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9G4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||Armadillo repeat-containing protein 12|||In isoform 2.|||In isoform 3.|||Interaction with TBC1D15|||Loss of interaction with RBBP4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230163|||http://purl.uniprot.org/annotation/VSP_017800|||http://purl.uniprot.org/annotation/VSP_017801
http://togogenome.org/gene/9606:SLC35D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76EJ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Nucleotide sugar transporter SLC35D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313080|||http://purl.uniprot.org/annotation/VAR_037653|||http://purl.uniprot.org/annotation/VSP_030006
http://togogenome.org/gene/9606:CD3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YIY5|||http://purl.uniprot.org/uniprot/P09693                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes lysosomal targeting.|||Cytoplasmic|||Di-leucine motif|||Diminished but persistent lysosomal targeting.|||Extracellular|||Helical|||ITAM|||Ig-like|||Immunoglobulin subtype 2|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine|||Phosphoserine; by PKC|||T-cell surface glycoprotein CD3 gamma chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014615|||http://purl.uniprot.org/annotation/PRO_5014298165|||http://purl.uniprot.org/annotation/VAR_049854
http://togogenome.org/gene/9606:ABRAXAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWZ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes formation of a heterotetramer with BRCA1. Does not affect interaction with a first BRCA1 chain.|||Abolishes phosphorylation of the pSXXF motif and the interaction with BRCA1 but does not affect the interaction with UIMC1/RAP80. Strongly decreases recruitment of BRCA1 to sites of DNA damage. No effect on homodimerization.|||BRCA1-A complex subunit Abraxas 1|||Basic and acidic residues|||Decreases formation of a heterotetramer with BRCA1.|||Disordered|||In BC; results in reduced DSB repair efficiency; primarily localizes to the cytoplasm and has reduced nuclear localization; does not affect interaction with BRCA1; results in highly reduced interaction with UIMC1/RAP80.|||In isoform 2.|||MPN|||No effect on formation of a heterotetramer with BRCA1.|||No effect on homodimerization. Mildly decreased recruitment of BRCA1 to sites of DNA damage.|||Not associated with susceptibility to breast cancer.|||Permits formation of a heterotetramer with BRCA1.|||Phosphoserine|||Phosphothreonine|||pSXXF motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278575|||http://purl.uniprot.org/annotation/VAR_030790|||http://purl.uniprot.org/annotation/VAR_054054|||http://purl.uniprot.org/annotation/VAR_054055|||http://purl.uniprot.org/annotation/VAR_071865|||http://purl.uniprot.org/annotation/VSP_058196
http://togogenome.org/gene/9606:TSTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFU3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cysteine persulfide intermediate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leads to the loss of catalytic activity.|||Rhodanese|||Thiosulfate:glutathione sulfurtransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139423|||http://purl.uniprot.org/annotation/VSP_014151|||http://purl.uniprot.org/annotation/VSP_014152|||http://purl.uniprot.org/annotation/VSP_014153
http://togogenome.org/gene/9606:EOGT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5NDL2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF domain-specific O-linked N-acetylglucosamine transferase|||In AOS4.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Partial loss of activity.|||Prevents secretion from ER|||Required for optimal activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301970|||http://purl.uniprot.org/annotation/VAR_070090|||http://purl.uniprot.org/annotation/VAR_070091|||http://purl.uniprot.org/annotation/VSP_027897|||http://purl.uniprot.org/annotation/VSP_027898|||http://purl.uniprot.org/annotation/VSP_027899
http://togogenome.org/gene/9606:ITGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM0|||http://purl.uniprot.org/uniprot/P26006                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes palmitoylation.|||Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In JEB7.|||In isoform 2.|||Integrin alpha-2|||Integrin alpha-3|||Integrin alpha-3 heavy chain|||Integrin alpha-3 light chain|||Interaction with HPS5|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016238|||http://purl.uniprot.org/annotation/PRO_0000016239|||http://purl.uniprot.org/annotation/PRO_0000016240|||http://purl.uniprot.org/annotation/PRO_5014203841|||http://purl.uniprot.org/annotation/VAR_055967|||http://purl.uniprot.org/annotation/VAR_055968|||http://purl.uniprot.org/annotation/VAR_055969|||http://purl.uniprot.org/annotation/VAR_068808|||http://purl.uniprot.org/annotation/VAR_077512|||http://purl.uniprot.org/annotation/VAR_077513|||http://purl.uniprot.org/annotation/VSP_002721
http://togogenome.org/gene/9606:EP300                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09472|||http://purl.uniprot.org/uniprot/Q7Z6C1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  40% decrease in activity.|||40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628.|||70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625.|||70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628.|||90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628.|||Abolished acetyltransferase activity.|||Abolished acetyltransferase and acyltransferase activities. Abolishes autoacetylation. Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. No acetylation of RXRA.|||Abolishes AMPK-mediated phosphorylation.|||Abolishes autoacetylation. Loss of acetyltransferase activity.|||Abolishes interaction with NCOA2.|||Abolishes sumoylation and transcriptional repression when associated with A-1024.|||Abolishes sumoylation and transcriptional repression; when associated with A-1020.|||Abolishes sumoylation and transcriptional repression; when associated with R-1020.|||Abolishes sumoylation and transcriptional repression; when associated with R-1024.|||Asymmetric dimethylarginine; by CARM1|||Asymmetric dimethylarginine; by CARM1; alternate|||Basic and acidic residues|||Basic residues|||Binding region for E1A adenovirus|||Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A|||Bromo|||CBP/p300-type HAT|||CRD1; mediates transcriptional repression|||Citrulline; by PADI4; alternate|||Disordered|||Found in a patient with spinocerebellar ataxia; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Histone acetyltransferase p300|||In MKHK2.|||In a breast cancer sample.|||In a colorectal cancer sample.|||In a pancreatic cancer sample.|||Increased acetyltransferase activity.|||Inhibits interaction with HIF1A and transcription activation; when associated with A-344.|||Inhibits interaction with HIF1A and transcription activation; when associated with A-345.|||Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2.|||Inhibits interaction with HIF1A. Reduces interaction with CITED2.|||Interaction with ALX1|||Interaction with HTLV-1 Tax|||Interaction with NCOA2|||Interaction with RORA|||Interaction with histone|||KIX|||Loss of activity; when associated with R-1396.|||Loss of activity; when associated with R-1397.|||Loss of activity; when associated with W-1396.|||Loss of activity; when associated with W-1397.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-acetyllysine; by autocatalysis|||No effect on interaction with NCOA2.|||Nuclear localization signal|||Phosphomimetic mutant that leads to descreased interaction with nuclear receptors.|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues|||Pro residues|||Removed|||Strongly reduces interaction with NCOA2.|||TAZ-type|||TAZ-type 1|||TAZ-type 2|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211193|||http://purl.uniprot.org/annotation/VAR_014428|||http://purl.uniprot.org/annotation/VAR_014429|||http://purl.uniprot.org/annotation/VAR_014430|||http://purl.uniprot.org/annotation/VAR_014431|||http://purl.uniprot.org/annotation/VAR_020425|||http://purl.uniprot.org/annotation/VAR_038376|||http://purl.uniprot.org/annotation/VAR_038377|||http://purl.uniprot.org/annotation/VAR_055554|||http://purl.uniprot.org/annotation/VAR_074021|||http://purl.uniprot.org/annotation/VAR_080731|||http://purl.uniprot.org/annotation/VAR_081986|||http://purl.uniprot.org/annotation/VAR_081987
http://togogenome.org/gene/9606:ZNF28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17035                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047357|||http://purl.uniprot.org/annotation/VAR_036841|||http://purl.uniprot.org/annotation/VAR_036842|||http://purl.uniprot.org/annotation/VAR_036843|||http://purl.uniprot.org/annotation/VSP_029007
http://togogenome.org/gene/9606:KCTD18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4A2|||http://purl.uniprot.org/uniprot/Q6PI47                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ|||BTB/POZ domain-containing protein KCTD18|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Potassium channel tetramerisation-type BTB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248596|||http://purl.uniprot.org/annotation/VAR_027355|||http://purl.uniprot.org/annotation/VAR_027356|||http://purl.uniprot.org/annotation/VAR_027357|||http://purl.uniprot.org/annotation/VAR_027358|||http://purl.uniprot.org/annotation/VSP_020323|||http://purl.uniprot.org/annotation/VSP_020324|||http://purl.uniprot.org/annotation/VSP_020325|||http://purl.uniprot.org/annotation/VSP_020326
http://togogenome.org/gene/9606:STMN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EVN3|||http://purl.uniprot.org/uniprot/Q9H169                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||S-palmitoyl cysteine|||SLD|||Stathmin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182406|||http://purl.uniprot.org/annotation/VSP_006279|||http://purl.uniprot.org/annotation/VSP_055279|||http://purl.uniprot.org/annotation/VSP_055280
http://togogenome.org/gene/9606:C3orf84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BNL1|||http://purl.uniprot.org/uniprot/H3BQU4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Domain of unknown function with conserved HDNR motif|||Uncharacterized protein C3orf84                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423415
http://togogenome.org/gene/9606:NT5E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21589|||http://purl.uniprot.org/uniprot/Q6NZX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  5'-Nucleotidase C-terminal|||5'-nucleotidase|||Calcineurin-like phosphoesterase|||GPI-anchor amidated serine|||Helical|||In CALJA; absence from the plasma-membrane; exhibits no catalytic AMPase activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000015|||http://purl.uniprot.org/annotation/PRO_0000000016|||http://purl.uniprot.org/annotation/PRO_5004277669|||http://purl.uniprot.org/annotation/VAR_022091|||http://purl.uniprot.org/annotation/VAR_048103|||http://purl.uniprot.org/annotation/VAR_065185|||http://purl.uniprot.org/annotation/VSP_043076
http://togogenome.org/gene/9606:KCNJ18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7U540                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases the single-channel open probability (Po) without altering its conductance.|||Disordered|||Extracellular|||Found in a patient with hypokalemic periodic paralysis without hyperthyroidism; reduces potassium inward and outward currents density.|||Found in a patient with sporadic periodic paralysis; unknown pathological significance; abolishes potassium inward and outward currents density; reduces cell surface abundance.|||Found in a patient with sporadic periodic paralysis; unknown pathological significance; decreases potassium inward and outward currents density; reduces cell surface abundance; reduces conductance; dominant negative mutation.|||Helical|||In TTPP2.|||In TTPP2; abolishes potassium inward and outward currents density.|||In TTPP2; hypermorphic; longer time required for half-maximal current degradation.|||In TTPP2; reduces potassium inward and outward currents density.|||In TTPP2; small decrease in current density.|||In TTPP2; unknown pathological significance; decreases potassium inward and outward currents density; reduces cell surface abundance; reduces open propability; dominant negative mutation.|||Inward rectifier potassium channel 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395171|||http://purl.uniprot.org/annotation/VAR_063286|||http://purl.uniprot.org/annotation/VAR_063287|||http://purl.uniprot.org/annotation/VAR_063288|||http://purl.uniprot.org/annotation/VAR_063289|||http://purl.uniprot.org/annotation/VAR_079830|||http://purl.uniprot.org/annotation/VAR_079831|||http://purl.uniprot.org/annotation/VAR_079832|||http://purl.uniprot.org/annotation/VAR_079833|||http://purl.uniprot.org/annotation/VAR_079834|||http://purl.uniprot.org/annotation/VAR_079835|||http://purl.uniprot.org/annotation/VAR_079836|||http://purl.uniprot.org/annotation/VAR_079837|||http://purl.uniprot.org/annotation/VAR_079838|||http://purl.uniprot.org/annotation/VAR_079839
http://togogenome.org/gene/9606:MESP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRJ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 2 AA tandem repeats of G-Q|||CPLCP|||Disordered|||Mesoderm posterior protein 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304404|||http://purl.uniprot.org/annotation/VAR_035021
http://togogenome.org/gene/9606:LUZP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DE3|||http://purl.uniprot.org/uniprot/Q86V48                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Leucine zipper protein 1|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234550|||http://purl.uniprot.org/annotation/VAR_026283|||http://purl.uniprot.org/annotation/VAR_026284|||http://purl.uniprot.org/annotation/VAR_026285|||http://purl.uniprot.org/annotation/VAR_056932|||http://purl.uniprot.org/annotation/VAR_056933|||http://purl.uniprot.org/annotation/VAR_056934|||http://purl.uniprot.org/annotation/VSP_018351|||http://purl.uniprot.org/annotation/VSP_018352|||http://purl.uniprot.org/annotation/VSP_018353
http://togogenome.org/gene/9606:FUT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8P8|||http://purl.uniprot.org/uniprot/Q546E0|||http://purl.uniprot.org/uniprot/Q9BYC5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-(1,6)-fucosyltransferase|||Complete loss of activity.|||Cytoplasmic|||Decreases activity to 3%.|||GT23|||Helical|||Helical; Signal-anchor for type II membrane protein|||Important for donor substrate binding|||In CDGF1; complete loss of total core fucosylated N-glycans in patient's serum and fibroblasts compared to controls.|||In CDGF1; drastic decrease of protein level in patient's fibroblasts and complete loss of total core fucosylated N-glycans in serum and fibroblasts compared to controls.|||In CDGF1; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of enzyme activity.|||Lumenal|||No effect on enzyme activity.|||Phosphoserine|||SH3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080526|||http://purl.uniprot.org/annotation/VAR_033537|||http://purl.uniprot.org/annotation/VAR_054038|||http://purl.uniprot.org/annotation/VAR_080978|||http://purl.uniprot.org/annotation/VAR_080979|||http://purl.uniprot.org/annotation/VAR_080980|||http://purl.uniprot.org/annotation/VAR_082143|||http://purl.uniprot.org/annotation/VSP_001807|||http://purl.uniprot.org/annotation/VSP_001808|||http://purl.uniprot.org/annotation/VSP_046837|||http://purl.uniprot.org/annotation/VSP_053361|||http://purl.uniprot.org/annotation/VSP_053362
http://togogenome.org/gene/9606:R3HDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRA6|||http://purl.uniprot.org/uniprot/B5MCG9|||http://purl.uniprot.org/uniprot/Q9Y2K5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||R3H|||R3H domain-containing protein 2|||SUZ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050787|||http://purl.uniprot.org/annotation/VAR_059713|||http://purl.uniprot.org/annotation/VSP_026087|||http://purl.uniprot.org/annotation/VSP_026088|||http://purl.uniprot.org/annotation/VSP_057391|||http://purl.uniprot.org/annotation/VSP_057392
http://togogenome.org/gene/9606:ANO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX12|||http://purl.uniprot.org/uniprot/Q4KMQ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin dimerisation|||Anoctamin-6|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191757|||http://purl.uniprot.org/annotation/VAR_028109|||http://purl.uniprot.org/annotation/VSP_042893|||http://purl.uniprot.org/annotation/VSP_046819|||http://purl.uniprot.org/annotation/VSP_046820
http://togogenome.org/gene/9606:SIDT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||SID1 transmembrane family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032575|||http://purl.uniprot.org/annotation/VAR_057184|||http://purl.uniprot.org/annotation/VAR_057185|||http://purl.uniprot.org/annotation/VAR_061793|||http://purl.uniprot.org/annotation/VSP_039174
http://togogenome.org/gene/9606:GABARAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95166|||http://purl.uniprot.org/uniprot/Q6IAW1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Site|||Strand                                                                                  ^@                                                                                  Cleavage; by ATG4B|||Gamma-aminobutyric acid receptor-associated protein|||Impairs localization at the autophagosomal membrane.|||Inhibits interaction with TECPR2.|||Interaction with GABRG2|||Interaction with GPHN|||Interaction with beta-tubulin|||No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with H-25 and H-54.|||No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with Q-24 and H-25.|||No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with Q-24 and H-54.|||No effect on interaction with TECPR2.|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212363|||http://purl.uniprot.org/annotation/PRO_0000423065
http://togogenome.org/gene/9606:CLEC17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS10                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 17, member A|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319428|||http://purl.uniprot.org/annotation/VSP_039405|||http://purl.uniprot.org/annotation/VSP_039406|||http://purl.uniprot.org/annotation/VSP_039407|||http://purl.uniprot.org/annotation/VSP_039408
http://togogenome.org/gene/9606:ACOXL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V3X2|||http://purl.uniprot.org/uniprot/B4DU63|||http://purl.uniprot.org/uniprot/Q9NUZ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA oxidase C-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Acyl-coenzyme A oxidase-like protein|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305100|||http://purl.uniprot.org/annotation/VAR_035164|||http://purl.uniprot.org/annotation/VAR_035165|||http://purl.uniprot.org/annotation/VSP_028237|||http://purl.uniprot.org/annotation/VSP_028238|||http://purl.uniprot.org/annotation/VSP_028239|||http://purl.uniprot.org/annotation/VSP_046900
http://togogenome.org/gene/9606:RSRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IZ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In MRT70.|||In MRT70; results in highly reduced transcript levels.|||In isoform 2.|||Polar residues|||Serine/Arginine-related protein 53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097496|||http://purl.uniprot.org/annotation/VAR_082245|||http://purl.uniprot.org/annotation/VAR_082246|||http://purl.uniprot.org/annotation/VSP_013120
http://togogenome.org/gene/9606:HOXC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31275                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-C12|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200194
http://togogenome.org/gene/9606:SLC30A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6M5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 2 AA approximate repeats of H-G|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Loss of N-glycosylation. No effect on localization to the plasma membrane. Increased stability at the plasma membrane. No effect on resistance to zinc-induced cytotoxicity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Proton-coupled zinc antiporter SLC30A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206090
http://togogenome.org/gene/9606:SELENBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13228                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In EHMTO; loss of methanethiol oxidation in patient cells.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Methanethiol oxidase|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174633|||http://purl.uniprot.org/annotation/VAR_080207|||http://purl.uniprot.org/annotation/VAR_080208|||http://purl.uniprot.org/annotation/VAR_080209|||http://purl.uniprot.org/annotation/VSP_038440|||http://purl.uniprot.org/annotation/VSP_045425|||http://purl.uniprot.org/annotation/VSP_055126
http://togogenome.org/gene/9606:ADPRS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX46                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylhydrolase ARH3|||Abolished ability to bind and hydrolyze proteins ADP-ribosylated on serine. No effect on hydrolase activity.|||Abolishes hydrolase activity.|||Complete loss of activity.|||Complete loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine.|||Complete loss of activity. Abolishes Mg(2+) and ADP-ribose binding. Does not affect recruitment to DNA lesion regions following DNA damage. Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them.|||Complete loss of activity. Abolishes Mg(2+) binding. Retains ability to bind ADP-ribose. Does not affect recruitment to DNA lesion regions following DNA damage. Strongly reduced ability to hydrolyze proteins ADP-ribosylated on serine.|||Complete loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them.|||Glutamate flap|||In CONDSIAS; no detectable protein in patient fibroblasts.|||In CONDSIAS; no detectable protein levels in patient fibroblasts.|||In CONDSIAS; severely reduced protein levels in patient fibroblasts; decreased stability and reduced Tm; reduced alpha-helix content and altered secondary structure detected by circular dichroism spectroscopy.|||In CONDSIAS; unknown pathological significance.|||In CONDSIAS; unknown pathological significance; reduced protein abundance; increased levels of ADP-ribose; May result in protein misfolding or aggregation.|||In CONDSIAS; unknown pathological significance; results in accumulation of poly(ADP-ribose) in the nucleus of patient cells after exposure to H(2)O(2); reduced protein abundance in fibroblasts; localization to the cytoplasm in fibroblasts; no effect on hydrolase activity in vitro; may result in reduced protein stability.|||No effect on hydrolase activity.|||Partial loss of activity.|||Phosphothreonine|||Reduces hydrolase activity.|||Retains ability to bind proteins ADP-ribosylated on serine but is unable to hydrolyze them.|||Significant loss of activity.|||Significant loss of activity. Abolished recruitment to DNA lesion regions following DNA damage. Abolished ability to hydrolyze proteins ADP-ribosylated on serine.|||Significant loss of activity. Does not affect recruitment to DNA lesion regions following DNA damage. Strongly reduced ability to hydrolyze proteins ADP-ribosylated on serine.|||Slight reduction in activity toward poly(ADP-ribose). Does not affect ability to degrade O-acetyl-ADP-D-ribose.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277613|||http://purl.uniprot.org/annotation/VAR_030579|||http://purl.uniprot.org/annotation/VAR_081264|||http://purl.uniprot.org/annotation/VAR_081265|||http://purl.uniprot.org/annotation/VAR_081266|||http://purl.uniprot.org/annotation/VAR_081267|||http://purl.uniprot.org/annotation/VAR_081268|||http://purl.uniprot.org/annotation/VAR_081269|||http://purl.uniprot.org/annotation/VAR_081270|||http://purl.uniprot.org/annotation/VAR_081271|||http://purl.uniprot.org/annotation/VAR_085654
http://togogenome.org/gene/9606:ARID1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14497                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 1A|||Acidic residues|||Asymmetric dimethylarginine|||Disordered|||Displays nucleocytoplasmic localization and increased stability; when associated with 1370-T-T-1371.|||Displays nucleocytoplasmic localization and increased stability; when associated with T-1383.|||Found in a breast cancer sample; somatic mutation.|||Found in a clear cell renal carcinoma case; somatic mutation.|||Found in a clear cell renal carcinoma; somatic mutation.|||Found in a gastric cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||LXXLL|||N-acetylalanine|||N6-acetyllysine|||No effect on subcellular localization.|||Nuclear localization signal|||Omega-N-methylarginine|||Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1073.|||Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1096.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200575|||http://purl.uniprot.org/annotation/VAR_064695|||http://purl.uniprot.org/annotation/VAR_064696|||http://purl.uniprot.org/annotation/VAR_068021|||http://purl.uniprot.org/annotation/VAR_068022|||http://purl.uniprot.org/annotation/VAR_068023|||http://purl.uniprot.org/annotation/VAR_076938|||http://purl.uniprot.org/annotation/VSP_015225|||http://purl.uniprot.org/annotation/VSP_037157
http://togogenome.org/gene/9606:ZC3H12D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A288                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||In isoform 2.|||In isoform 3.|||In some sporadic lung cancer sample; appears to cause loss of tumor suppressor activity.|||Inhibits interleukin IL6 mRNA instability.|||Necessary for interaction with ZC3H12A|||Pro residues|||Probable ribonuclease ZC3H12D|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348931|||http://purl.uniprot.org/annotation/VAR_046199|||http://purl.uniprot.org/annotation/VAR_046200|||http://purl.uniprot.org/annotation/VSP_040794|||http://purl.uniprot.org/annotation/VSP_040795|||http://purl.uniprot.org/annotation/VSP_052853
http://togogenome.org/gene/9606:DCTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDU9|||http://purl.uniprot.org/uniprot/A8K8J9|||http://purl.uniprot.org/uniprot/B3KTX4|||http://purl.uniprot.org/uniprot/Q13561|||http://purl.uniprot.org/uniprot/V9HW58                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynactin subunit 2|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079821|||http://purl.uniprot.org/annotation/VSP_040485|||http://purl.uniprot.org/annotation/VSP_040486
http://togogenome.org/gene/9606:OR2A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150457|||http://purl.uniprot.org/annotation/VAR_034171
http://togogenome.org/gene/9606:CYTIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60759                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytohesin-interacting protein|||Found in a renal cell carcinoma case; somatic mutation.|||In isoform 2.|||Interaction with CYTH1|||No membrane-association. No change in the binding to CYTH1; when associated with A-90 and A-92.|||No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-90.|||No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-92.|||PDZ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097061|||http://purl.uniprot.org/annotation/VAR_023534|||http://purl.uniprot.org/annotation/VAR_051287|||http://purl.uniprot.org/annotation/VAR_064706|||http://purl.uniprot.org/annotation/VSP_055502
http://togogenome.org/gene/9606:PDGFC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRA1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  CUB|||Cleavage|||Essential for cleavage by PLAT.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interchain (with C-274)|||Interchain (with C-286)|||Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells.|||N-linked (GlcNAc...) asparagine|||Not essential for cleavage by PLAT.|||Platelet-derived growth factor C, latent form|||Platelet-derived growth factor C, receptor-binding form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343871|||http://purl.uniprot.org/annotation/PRO_0000343872|||http://purl.uniprot.org/annotation/VSP_034701|||http://purl.uniprot.org/annotation/VSP_034702|||http://purl.uniprot.org/annotation/VSP_034703|||http://purl.uniprot.org/annotation/VSP_047606
http://togogenome.org/gene/9606:ZSWIM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P217                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||SWIM-type|||Zinc finger SWIM domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223103|||http://purl.uniprot.org/annotation/VAR_053770
http://togogenome.org/gene/9606:U2AF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26368                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-hydroxylysine; by JMJD6|||5-hydroxylysine; by JMJD6; alternate|||Basic and acidic residues|||Basic residues|||Decreases affinity for UAF1 by 2 orders of magnitude.|||Decreases affinity for UAF1 by 3 orders of magnitude.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylserine|||N6-acetyllysine; alternate|||Necessary and sufficient to stimulate pre-mRNAs 3'-end cleavage in a CFIm complex-dependent manner|||No effect.|||Phosphoserine|||RRM 1|||RRM 2|||RRM 3|||Reduces interaction with SF1.|||Removed|||Required for interaction with PRPF19|||Splicing factor U2AF 65 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081988|||http://purl.uniprot.org/annotation/VSP_035414
http://togogenome.org/gene/9606:AVIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75366                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Advillin|||Core|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||Headpiece|||In NPHS21; inhibited actin bundling capacity; decreases interaction with PLCE1; disrupted EGF-induced diacylglycerol generation by PLCE1.|||In NPHS21; inhibited actin bundling capacity; slightly decreased interaction with PLCE1; disrupted EGF-induced diacylglycerol generation by PLCE1.|||In NPHS21; unknown pathological significance.|||In isoform 2.|||Phosphotyrosine|||Reduces interaction with F-actin.|||Required for interaction with F-actin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218736|||http://purl.uniprot.org/annotation/VAR_054974|||http://purl.uniprot.org/annotation/VAR_083229|||http://purl.uniprot.org/annotation/VAR_083230|||http://purl.uniprot.org/annotation/VAR_083231|||http://purl.uniprot.org/annotation/VSP_036961
http://togogenome.org/gene/9606:CES2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00748                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acyl-ester intermediate|||Charge relay system|||Cocaine esterase|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008572|||http://purl.uniprot.org/annotation/VAR_018396|||http://purl.uniprot.org/annotation/VAR_018397|||http://purl.uniprot.org/annotation/VSP_010161|||http://purl.uniprot.org/annotation/VSP_059804
http://togogenome.org/gene/9606:NLRC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPP4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CARD|||In AIFEC; results in a gain of function mutation with constitutive activation of caspase-1.|||In FCAS4; the mutation increases oligomerization of the NLRC4 protein; results in hyperactivation of caspase-1 with an increase in IL1B protein secretion.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NLR family CARD domain-containing protein 4|||Nucleotide-binding domain (NBD)|||Phosphoserine|||Winged-helix domain (WHD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144087|||http://purl.uniprot.org/annotation/VAR_072484|||http://purl.uniprot.org/annotation/VAR_072485|||http://purl.uniprot.org/annotation/VAR_072645|||http://purl.uniprot.org/annotation/VSP_000784|||http://purl.uniprot.org/annotation/VSP_000785|||http://purl.uniprot.org/annotation/VSP_000786|||http://purl.uniprot.org/annotation/VSP_000787|||http://purl.uniprot.org/annotation/VSP_000788
http://togogenome.org/gene/9606:TBX21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL17                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Disordered|||Essential for its interaction with RUNX1 and its ability to inhibit RUNX1 transcriptional activity and suppress TH17 lineage development|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IMD88; loss of binding to DNA; loss of transcriptional activity shown in IFNG promoter-driven luciferase assay; unable to activate IFNG production.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by ITK|||T-box|||T-box transcription factor TBX21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184453|||http://purl.uniprot.org/annotation/VAR_020252|||http://purl.uniprot.org/annotation/VAR_029275|||http://purl.uniprot.org/annotation/VAR_086466
http://togogenome.org/gene/9606:CXorf49B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein CXorf49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343895
http://togogenome.org/gene/9606:KIAA0930                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein KIAA0930                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255938|||http://purl.uniprot.org/annotation/VSP_021309|||http://purl.uniprot.org/annotation/VSP_021310
http://togogenome.org/gene/9606:CBLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23435                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Peptide|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes GRID2 interaction.; when associated with A-122 and A-124.|||Abolishes GRID2 interaction.; when associated with A-122 and A-147.|||Abolishes GRID2 interaction.; when associated with A-124 and A-147.|||Abolishes hexamer formation; when associated with S-34. Abolishes interaction with NRXN1 isoform 3B; when associated with S-34. Abolishes GRID2 interaction.; when associated with S-34.|||Abolishes hexamer formation; when associated with S-38. Abolishes interaction with NRXN1; when associated with S-38. Abolishes GRID2 interaction; when associated with S-38.|||C1q|||Cerebellin|||Cerebellin-1|||Essential for interaction with GRID2|||Essential for interaction with NRXN1 and linker of two C1q trimers into disulfide-linked hexamers|||Interchain|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with CBLN3, and homotrimerization|||[des-Ser1]-cerebellin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003546|||http://purl.uniprot.org/annotation/PRO_0000274209|||http://purl.uniprot.org/annotation/PRO_0000274210
http://togogenome.org/gene/9606:MBD3L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDZ8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative methyl-CpG-binding domain protein 3-like 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349234
http://togogenome.org/gene/9606:SEPTIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6H6|||http://purl.uniprot.org/uniprot/Q15019                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  G1 motif|||G3 motif|||G4 motif|||Important for dimerization|||In isoform 2.|||In isoform 3.|||Loss of dimerization.|||Loss of phosphorylation.|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Septin-2|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173515|||http://purl.uniprot.org/annotation/VSP_038271|||http://purl.uniprot.org/annotation/VSP_055176
http://togogenome.org/gene/9606:CACNG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBN1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Voltage-dependent calcium channel gamma-4 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164678
http://togogenome.org/gene/9606:NOCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK39                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decreased activity as transcriptional repressor.|||Disordered|||Interaction with PPARG|||Lack of catalytic activity.|||Mitochondrion|||No effect on activity as transcriptional repressor.|||No effect on catalytic activity.|||Nocturnin|||Reduced catalytic activity.|||Slightly decreased activity as transcriptional repressor.|||Slightly increased activity as transcriptional repressor. Lack of catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218568|||http://purl.uniprot.org/annotation/VAR_047096
http://togogenome.org/gene/9606:STX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKR0|||http://purl.uniprot.org/uniprot/Q13190                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||IxM motif; signal for cargo packaging into COPII-coated vesicles|||Loss of interaction with SEC24C.|||Syntaxin-5|||T-SNARE coiled-coil homology|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210205|||http://purl.uniprot.org/annotation/VAR_035642|||http://purl.uniprot.org/annotation/VAR_052248|||http://purl.uniprot.org/annotation/VAR_052249|||http://purl.uniprot.org/annotation/VAR_081529|||http://purl.uniprot.org/annotation/VSP_020119|||http://purl.uniprot.org/annotation/VSP_020120
http://togogenome.org/gene/9606:CD34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28906                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hematopoietic progenitor cell antigen CD34|||In isoform CD34-T.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020900|||http://purl.uniprot.org/annotation/VAR_050774|||http://purl.uniprot.org/annotation/VSP_004159|||http://purl.uniprot.org/annotation/VSP_004160
http://togogenome.org/gene/9606:MAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3Z1|||http://purl.uniprot.org/uniprot/P11137|||http://purl.uniprot.org/uniprot/Q6NYC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KNDC1|||MAP2/Tau projection|||Microtubule-associated protein 2|||Phosphoserine|||Phosphoserine; by MARK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072747|||http://purl.uniprot.org/annotation/VAR_019612|||http://purl.uniprot.org/annotation/VAR_019613|||http://purl.uniprot.org/annotation/VAR_036014|||http://purl.uniprot.org/annotation/VAR_036015|||http://purl.uniprot.org/annotation/VAR_050019|||http://purl.uniprot.org/annotation/VAR_050020|||http://purl.uniprot.org/annotation/VAR_050021|||http://purl.uniprot.org/annotation/VAR_050022|||http://purl.uniprot.org/annotation/VSP_003197|||http://purl.uniprot.org/annotation/VSP_011302|||http://purl.uniprot.org/annotation/VSP_043596|||http://purl.uniprot.org/annotation/VSP_043597|||http://purl.uniprot.org/annotation/VSP_043598
http://togogenome.org/gene/9606:LIAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0L7|||http://purl.uniprot.org/uniprot/O43766|||http://purl.uniprot.org/uniprot/Q6P5Q6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In HGCLAS.|||In isoform 2.|||In isoform 3.|||Lipoyl synthase N-terminal|||Lipoyl synthase, mitochondrial|||Mitochondrion|||Radical SAM core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017723|||http://purl.uniprot.org/annotation/VAR_067839|||http://purl.uniprot.org/annotation/VSP_047380|||http://purl.uniprot.org/annotation/VSP_047381|||http://purl.uniprot.org/annotation/VSP_054764
http://togogenome.org/gene/9606:FOXK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01167                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished SUMOylation; when associated with R-527.|||Abolished SUMOylation; when associated with R-633.|||Abolishes DNA-binding.|||Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation.|||DNA-binding; major groove|||DNA-binding; minor groove|||Decreased phosphorylation leading to increased stability of the protein; when associated with A-373.|||Decreased phosphorylation leading to increased stability of the protein; when associated with A-428.|||Decreases DNA-binding to 20%.|||Decreases DNA-binding to 25%.|||Decreases DNA-binding to 40%.|||Decreases DNA-binding to 70%.|||Disordered|||FHA|||Fork-head|||Forkhead box protein K2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly reduces interaction with DVL2.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||No effect on interaction with DVL2.|||Omega-N-methylarginine|||Phosphomimetic mutant; decreased phosphorylation leading to decreased stability of the protein; when associated with D-373.|||Phosphomimetic mutant; decreased phosphorylation leading to decreased stability of the protein; when associated with D-428.|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Polar residues|||Reduced interaction with BAP1.|||Removed|||Required for interaction with DVL2 and SUDS3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091858|||http://purl.uniprot.org/annotation/VSP_001559|||http://purl.uniprot.org/annotation/VSP_001560|||http://purl.uniprot.org/annotation/VSP_001561
http://togogenome.org/gene/9606:GLUL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8YXX4|||http://purl.uniprot.org/uniprot/P15104                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases ribolosomal 40S subunit synthesis. Loss of nucleolar location of BYSL.|||GS beta-grasp|||GS catalytic|||Glutamine synthetase|||In CSGD; reduced glutamine synthetase activity.|||In CSGD; suggests reduced glutamine synthetase activity.|||N-acetylthreonine|||Phosphoserine|||Phosphotyrosine|||Reduced ability to mediate autopalmitoylation.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153139|||http://purl.uniprot.org/annotation/VAR_026560|||http://purl.uniprot.org/annotation/VAR_026561
http://togogenome.org/gene/9606:NEGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3B1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuronal growth regulator 1|||Phosphotyrosine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015037|||http://purl.uniprot.org/annotation/PRO_0000015038|||http://purl.uniprot.org/annotation/VSP_056313
http://togogenome.org/gene/9606:RXFP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWV0|||http://purl.uniprot.org/uniprot/A0A0A0MT52|||http://purl.uniprot.org/uniprot/B3KV27|||http://purl.uniprot.org/uniprot/B4DGP2|||http://purl.uniprot.org/uniprot/Q59H16|||http://purl.uniprot.org/uniprot/Q9HBX9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LDL-receptor class A|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||Leads to constitutive increase of basal cAMP.|||N-linked (GlcNAc...) asparagine|||Relaxin receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069700|||http://purl.uniprot.org/annotation/PRO_5014085090|||http://purl.uniprot.org/annotation/VSP_001984|||http://purl.uniprot.org/annotation/VSP_029877|||http://purl.uniprot.org/annotation/VSP_029878|||http://purl.uniprot.org/annotation/VSP_029879|||http://purl.uniprot.org/annotation/VSP_054375|||http://purl.uniprot.org/annotation/VSP_054376
http://togogenome.org/gene/9606:OR7D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR1|||http://purl.uniprot.org/uniprot/Q8NG98                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||High sensitivity to androstenone and androstadienone.|||Impaired response to androstenone and androstadienone.|||Impaired response to androstenone and androstadienone; when associated with M-133.|||Impaired response to androstenone and androstadienone; when associated with W-88.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7D4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150649|||http://purl.uniprot.org/annotation/VAR_037778|||http://purl.uniprot.org/annotation/VAR_037779|||http://purl.uniprot.org/annotation/VAR_037780|||http://purl.uniprot.org/annotation/VAR_037781|||http://purl.uniprot.org/annotation/VAR_037782|||http://purl.uniprot.org/annotation/VAR_037783|||http://purl.uniprot.org/annotation/VAR_037784|||http://purl.uniprot.org/annotation/VAR_037785|||http://purl.uniprot.org/annotation/VAR_037786|||http://purl.uniprot.org/annotation/VAR_037787|||http://purl.uniprot.org/annotation/VAR_037788|||http://purl.uniprot.org/annotation/VAR_037789|||http://purl.uniprot.org/annotation/VAR_037790|||http://purl.uniprot.org/annotation/VAR_062056
http://togogenome.org/gene/9606:CYTH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2V8|||http://purl.uniprot.org/uniprot/Q9UIA0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  C-terminal autoinhibitory region|||Cytohesin-4|||PH|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120203|||http://purl.uniprot.org/annotation/VAR_051920
http://togogenome.org/gene/9606:DDX27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6D5|||http://purl.uniprot.org/uniprot/Q96GQ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||No interaction with PEBOW complex.|||Nuclear localization signal|||Phosphoserine|||Probable ATP-dependent RNA helicase DDX27|||Q motif|||Required for interaction with the PEBOW complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055031|||http://purl.uniprot.org/annotation/VAR_022849
http://togogenome.org/gene/9606:NRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K171|||http://purl.uniprot.org/uniprot/P48552                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes CTBP binding but retains transcriptional repressor activity.|||Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression.|||Abolishes interaction with CTBP1.|||Basic and acidic residues|||CTBP-binding|||CTBP-binding; principal site|||Disordered|||Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443.|||Disrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568.|||Disrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression.|||Disrupts transcriptional repression.|||Does not disrupt nuclear hormone receptor-dependent transcription repression.|||Does not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with ZNF366|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||LXXLL motif 6|||LXXLL motif 7|||LXXLL motif 8|||LXXLL motif 9|||Ligand-dependent nuclear receptor binding|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear receptor-interacting protein 1|||Nuclear receptor-interacting protein 1 repression|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression.|||Repression domain 1|||Repression domain 2|||Repression domain 3|||Repression domain 4|||Required for targeting to small nuclear foci                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057951|||http://purl.uniprot.org/annotation/VAR_023706|||http://purl.uniprot.org/annotation/VAR_023707|||http://purl.uniprot.org/annotation/VAR_023708|||http://purl.uniprot.org/annotation/VAR_023709|||http://purl.uniprot.org/annotation/VAR_023710|||http://purl.uniprot.org/annotation/VAR_034142|||http://purl.uniprot.org/annotation/VAR_051241|||http://purl.uniprot.org/annotation/VAR_051242
http://togogenome.org/gene/9606:UBE2M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4T4|||http://purl.uniprot.org/uniprot/P61081                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Forms a stable complex with NEDD8, which prevents subsequent NEDD8 conjugation to cullins.|||Glycyl thioester intermediate|||Impairs thioester intermediate formation.|||Interaction with UBA3|||N-acetylmethionine|||N6-acetyllysine|||NEDD8-conjugating enzyme Ubc12|||No effect on thioester intermediate formation.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Slightly impairs thioester intermediate formation.|||Strongly impairs thioester intermediate formation.|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082488
http://togogenome.org/gene/9606:PECAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16284                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  6-fold decrease in association with membrane microdomains.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In isoform Delta12.|||In isoform Delta13.|||In isoform Delta14-15 and isoform Delta15.|||In isoform Delta14-15.|||In isoform Delta14.|||In isoform Delta15.|||Lacks homophilic binding ability and is distributed over the entire plasma membrane.|||Loss of Tyr-690 phosphorylation. Does not inhibit targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. Loss of interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-690.|||May play a role in cytoprotective signaling|||Membrane-bound segment which detaches upon phosphorylation|||N-linked (GlcNAc...) asparagine|||No effect on Tyr-713 phosphorylation. Inhibits targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. No effect on interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-713.|||Phosphoserine|||Phosphotyrosine; by FER|||Platelet endothelial cell adhesion molecule|||Polar residues|||Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-151.|||Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-84.|||Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-84 and Q-151.|||Reduced homophilic cell adhesion; when associated with E-112; E-188 and E-190.|||Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-188.|||Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-190.|||Reduced homophilic cell adhesion; when associated with E-74; E-188 and E-190.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014895|||http://purl.uniprot.org/annotation/VAR_013145|||http://purl.uniprot.org/annotation/VAR_059402|||http://purl.uniprot.org/annotation/VAR_059403|||http://purl.uniprot.org/annotation/VAR_059404|||http://purl.uniprot.org/annotation/VAR_059405|||http://purl.uniprot.org/annotation/VSP_011806|||http://purl.uniprot.org/annotation/VSP_011807|||http://purl.uniprot.org/annotation/VSP_011808|||http://purl.uniprot.org/annotation/VSP_011809|||http://purl.uniprot.org/annotation/VSP_011810|||http://purl.uniprot.org/annotation/VSP_011811
http://togogenome.org/gene/9606:TIGD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT04                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||In isoform 2.|||Tigger transposable element-derived protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272620|||http://purl.uniprot.org/annotation/VSP_022453
http://togogenome.org/gene/9606:STK40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2I9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252261|||http://purl.uniprot.org/annotation/VAR_041200|||http://purl.uniprot.org/annotation/VAR_041201|||http://purl.uniprot.org/annotation/VAR_041202|||http://purl.uniprot.org/annotation/VAR_041203|||http://purl.uniprot.org/annotation/VSP_020896|||http://purl.uniprot.org/annotation/VSP_020897|||http://purl.uniprot.org/annotation/VSP_020898|||http://purl.uniprot.org/annotation/VSP_020899|||http://purl.uniprot.org/annotation/VSP_020900
http://togogenome.org/gene/9606:TNKS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95271                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Loss of activity; when associated with A-1184.|||Loss of activity; when associated with A-1291.|||PARP catalytic|||Polar residues|||Poly [ADP-ribose] polymerase tankyrase-1|||Pro residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211333|||http://purl.uniprot.org/annotation/VSP_004538|||http://purl.uniprot.org/annotation/VSP_004539
http://togogenome.org/gene/9606:CUZD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||CUB and zona pellucida-like domain-containing protein 1|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233331|||http://purl.uniprot.org/annotation/VAR_061992|||http://purl.uniprot.org/annotation/VSP_052018|||http://purl.uniprot.org/annotation/VSP_052019
http://togogenome.org/gene/9606:ZNF138                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRG3|||http://purl.uniprot.org/uniprot/A0A0A0MT90|||http://purl.uniprot.org/uniprot/A2RRP7|||http://purl.uniprot.org/uniprot/C9JHF6|||http://purl.uniprot.org/uniprot/P52744                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6; degenerate|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||KRAB|||Zinc finger protein 138                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047422|||http://purl.uniprot.org/annotation/VAR_057398|||http://purl.uniprot.org/annotation/VSP_044921|||http://purl.uniprot.org/annotation/VSP_047446|||http://purl.uniprot.org/annotation/VSP_047447
http://togogenome.org/gene/9606:STX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y82                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||Phosphoserine|||Removed|||Syntaxin-12|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210223|||http://purl.uniprot.org/annotation/VAR_035643
http://togogenome.org/gene/9606:RSPO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2MKA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation of Wnt signaling.|||Abolishes activation of Wnt signaling. Abolishes LGR4 binding.|||Basic and acidic residues|||Disordered|||FU 1|||FU 2|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes activation of Wnt signaling.|||No effect on activation of Wnt signaling.|||Polar residues|||R-spondin-1|||Reduces activation of Wnt signaling.|||Strongly reduces activation of Wnt signaling.|||Strongly reduces affinity for LGR4.|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234436|||http://purl.uniprot.org/annotation/VSP_018320|||http://purl.uniprot.org/annotation/VSP_043265
http://togogenome.org/gene/9606:HIRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54198                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates binding to ASF1A.|||Disordered|||Impairs binding to ASF1A.|||Impairs binding to ASF1A; when associated with K-458.|||Impairs binding to ASF1A; when associated with K-460.|||Impairs binding to CCNA1 and phosphorylation by CDK2.|||Impairs phosphorylation by CDK2.|||In isoform Short.|||Interaction with ASF1A|||Interaction with CCNA1|||Interaction with PAX3|||Interaction with histone H2B|||Interaction with histone H4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK2|||Polar residues|||Protein HIRA|||Required for repression of histone gene transcription|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051019|||http://purl.uniprot.org/annotation/VSP_006772
http://togogenome.org/gene/9606:LRRC4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NT99                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 4B|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231654
http://togogenome.org/gene/9606:STARD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y365                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by CK2|||START|||START domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220661
http://togogenome.org/gene/9606:PTPRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VU56|||http://purl.uniprot.org/uniprot/P23467|||http://purl.uniprot.org/uniprot/Q68D73|||http://purl.uniprot.org/uniprot/Q86VA4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase beta|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025436|||http://purl.uniprot.org/annotation/VAR_057135|||http://purl.uniprot.org/annotation/VAR_057136|||http://purl.uniprot.org/annotation/VAR_057137|||http://purl.uniprot.org/annotation/VAR_057138|||http://purl.uniprot.org/annotation/VAR_057139|||http://purl.uniprot.org/annotation/VAR_062251|||http://purl.uniprot.org/annotation/VAR_062252|||http://purl.uniprot.org/annotation/VSP_038521|||http://purl.uniprot.org/annotation/VSP_040484|||http://purl.uniprot.org/annotation/VSP_053944
http://togogenome.org/gene/9606:ACAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15057                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Arf-GAP|||Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2|||BAR|||C4-type|||Disordered|||Loss of GAP activity.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074210
http://togogenome.org/gene/9606:KLHDC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PID8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with CUL2|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 10|||Loss of interaction with CUL2. No effect on MAP3K5 activation.|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319436|||http://purl.uniprot.org/annotation/VAR_039005|||http://purl.uniprot.org/annotation/VAR_039006|||http://purl.uniprot.org/annotation/VAR_039007|||http://purl.uniprot.org/annotation/VAR_039008|||http://purl.uniprot.org/annotation/VAR_039009|||http://purl.uniprot.org/annotation/VSP_031484
http://togogenome.org/gene/9606:INTS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68E01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Integrator complex subunit 3|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259534|||http://purl.uniprot.org/annotation/VSP_021446|||http://purl.uniprot.org/annotation/VSP_038130|||http://purl.uniprot.org/annotation/VSP_038131|||http://purl.uniprot.org/annotation/VSP_038132
http://togogenome.org/gene/9606:FRMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A2Y4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FERM|||FERM domain-containing protein 3|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318098|||http://purl.uniprot.org/annotation/VAR_048366|||http://purl.uniprot.org/annotation/VSP_031162|||http://purl.uniprot.org/annotation/VSP_031163|||http://purl.uniprot.org/annotation/VSP_031164|||http://purl.uniprot.org/annotation/VSP_031165|||http://purl.uniprot.org/annotation/VSP_031166|||http://purl.uniprot.org/annotation/VSP_031167
http://togogenome.org/gene/9606:TMED7-TICAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYA0|||http://purl.uniprot.org/uniprot/Q86XR7|||http://purl.uniprot.org/uniprot/Q9Y3B3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||COPI vesicle coat-binding|||COPII vesicle coat-binding|||Complete loss of phosphorylation in response to LPS.|||Cytoplasmic|||Disordered|||GOLD|||Helical|||In isoform 2.|||Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4.|||Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation.|||Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal.|||Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B.|||No effect on phosphorylation.|||Phosphoserine; by PKC/PRKCE|||Phosphotyrosine|||Removed|||Results in relocalization from membrane to cytosol; Loss of ability to transduce TLR4-signal. Loss of TLR2-mediated activation of IRF7.|||Significant decrease of localization in the membrane.|||TIR|||TIR domain-containing adapter molecule 2|||Transmembrane emp24 domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010395|||http://purl.uniprot.org/annotation/PRO_0000317689|||http://purl.uniprot.org/annotation/PRO_5002034149|||http://purl.uniprot.org/annotation/VSP_046247|||http://purl.uniprot.org/annotation/VSP_047437
http://togogenome.org/gene/9606:AARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49588                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alanine--tRNA ligase, cytoplasmic|||Decreases editing activity.|||Decreases misincorporation of Cys instead of Ala.|||Found in a patient with distal hereditary motor neuropathy; unknown pathological significance.|||In CMT2N.|||In CMT2N; severely reduces enzyme activity.|||In DEE29; decreases protein abundance; decreases aminoacylation activity; no effect on the editing activity.|||In DEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency.|||In DEE29; results in 10-fold reduction in aminoacylation efficiency.|||In HDLS2; unknown pathological significance.|||In TTD8; unknown pathological significance.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075281|||http://purl.uniprot.org/annotation/VAR_028204|||http://purl.uniprot.org/annotation/VAR_063527|||http://purl.uniprot.org/annotation/VAR_067084|||http://purl.uniprot.org/annotation/VAR_073293|||http://purl.uniprot.org/annotation/VAR_073719|||http://purl.uniprot.org/annotation/VAR_073720|||http://purl.uniprot.org/annotation/VAR_079703|||http://purl.uniprot.org/annotation/VAR_086780|||http://purl.uniprot.org/annotation/VAR_086781|||http://purl.uniprot.org/annotation/VAR_086782|||http://purl.uniprot.org/annotation/VAR_086783|||http://purl.uniprot.org/annotation/VAR_086784|||http://purl.uniprot.org/annotation/VSP_057201|||http://purl.uniprot.org/annotation/VSP_057202
http://togogenome.org/gene/9606:RPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04843                                                                                  ^@                                                                                  Chain|||Crosslink|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-acetyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022241
http://togogenome.org/gene/9606:AWAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6E213                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Acyl-CoA wax alcohol acyltransferase 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249052
http://togogenome.org/gene/9606:EXOC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ07|||http://purl.uniprot.org/uniprot/Q63HP7|||http://purl.uniprot.org/uniprot/Q9UPT5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exocyst complex component 7|||Exocyst complex subunit Exo70 C-terminal|||In NEDSEBA; unknown pathological significance.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118960|||http://purl.uniprot.org/annotation/VAR_085057|||http://purl.uniprot.org/annotation/VAR_085058|||http://purl.uniprot.org/annotation/VSP_001483|||http://purl.uniprot.org/annotation/VSP_008876|||http://purl.uniprot.org/annotation/VSP_008877|||http://purl.uniprot.org/annotation/VSP_008878|||http://purl.uniprot.org/annotation/VSP_041098|||http://purl.uniprot.org/annotation/VSP_041099
http://togogenome.org/gene/9606:ZSWIM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q19AV6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  In ODG10.|||SWIM-type|||Zinc finger SWIM domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307403|||http://purl.uniprot.org/annotation/VAR_087123
http://togogenome.org/gene/9606:ZNF491                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8L2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 491                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047614
http://togogenome.org/gene/9606:RPS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A3R6|||http://purl.uniprot.org/uniprot/P62753                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyarginine|||ADP-ribosyl glutamic acid|||Abolishes hydroxylation by KDM8.|||Abolishes phosphorylation by PASK.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK|||Small ribosomal subunit protein eS6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137312|||http://purl.uniprot.org/annotation/VAR_025314
http://togogenome.org/gene/9606:OR56A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWP3|||http://purl.uniprot.org/uniprot/P0C7T3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 56A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343673
http://togogenome.org/gene/9606:CNBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA66                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclic nucleotide-binding domain-containing protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291777|||http://purl.uniprot.org/annotation/VAR_032859|||http://purl.uniprot.org/annotation/VAR_032860|||http://purl.uniprot.org/annotation/VAR_061108
http://togogenome.org/gene/9606:PHETA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4B1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||F&H|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of OCRL-binding.|||Loss of OCRL-binding. Drastically reduces membrane targeting.|||PH|||Phosphoserine|||Pro residues|||Sesquipedalian-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254572|||http://purl.uniprot.org/annotation/VSP_021239|||http://purl.uniprot.org/annotation/VSP_021240|||http://purl.uniprot.org/annotation/VSP_021241|||http://purl.uniprot.org/annotation/VSP_021242|||http://purl.uniprot.org/annotation/VSP_044836
http://togogenome.org/gene/9606:PARP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q460N5|||http://purl.uniprot.org/uniprot/Q8N546                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PARP10.|||Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Macro 1|||Macro 2|||Macro 3|||PARP catalytic|||Phosphoserine|||Protein mono-ADP-ribosyltransferase PARP14|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247589|||http://purl.uniprot.org/annotation/VSP_020013|||http://purl.uniprot.org/annotation/VSP_020014|||http://purl.uniprot.org/annotation/VSP_020017|||http://purl.uniprot.org/annotation/VSP_020018|||http://purl.uniprot.org/annotation/VSP_020019|||http://purl.uniprot.org/annotation/VSP_040876
http://togogenome.org/gene/9606:MARCKS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29966|||http://purl.uniprot.org/uniprot/Q6NVI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding (PSD)|||Disordered|||Myristoylated alanine-rich C-kinase substrate|||N-myristoyl glycine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157148|||http://purl.uniprot.org/annotation/VAR_025825|||http://purl.uniprot.org/annotation/VAR_025826
http://togogenome.org/gene/9606:DBNDD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dysbindin domain-containing protein 2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191003|||http://purl.uniprot.org/annotation/VSP_007753|||http://purl.uniprot.org/annotation/VSP_040767|||http://purl.uniprot.org/annotation/VSP_040768|||http://purl.uniprot.org/annotation/VSP_046691
http://togogenome.org/gene/9606:VCF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KUH0|||http://purl.uniprot.org/uniprot/Q5XKR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polar residues|||Protein FAM104B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239034|||http://purl.uniprot.org/annotation/VAR_055796|||http://purl.uniprot.org/annotation/VSP_019078|||http://purl.uniprot.org/annotation/VSP_019079|||http://purl.uniprot.org/annotation/VSP_044976|||http://purl.uniprot.org/annotation/VSP_046644|||http://purl.uniprot.org/annotation/VSP_046645
http://togogenome.org/gene/9606:ATP1B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14415                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Sodium/potassium-transporting ATPase subunit beta-2|||immunoglobulin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219104|||http://purl.uniprot.org/annotation/VAR_030339|||http://purl.uniprot.org/annotation/VAR_061031
http://togogenome.org/gene/9606:SLC25A17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP73|||http://purl.uniprot.org/uniprot/B4DU97|||http://purl.uniprot.org/uniprot/F6RTR7|||http://purl.uniprot.org/uniprot/O43808                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Impairs interaction with PEX19.|||Localizes in the cytoplasm.|||Lumenal|||Necessary for targeting to peroxisomes and interaction with PEX19|||No effect on interaction with PEX19.|||Peroxisomal membrane protein PMP34|||Peroxisome localization signal|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090705|||http://purl.uniprot.org/annotation/VAR_050139
http://togogenome.org/gene/9606:PLA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9W0|||http://purl.uniprot.org/uniprot/Q53H76                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Involved in the recognition of diacyl-phospholipids|||Lipase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phospholipase A1 member A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273330|||http://purl.uniprot.org/annotation/VAR_030126|||http://purl.uniprot.org/annotation/VAR_030127|||http://purl.uniprot.org/annotation/VAR_030128|||http://purl.uniprot.org/annotation/VSP_022507|||http://purl.uniprot.org/annotation/VSP_022508|||http://purl.uniprot.org/annotation/VSP_022509|||http://purl.uniprot.org/annotation/VSP_044944
http://togogenome.org/gene/9606:UBLCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVY7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Aberrant diffuse pan-cellular localization and loss of binding to PSMD2.|||FCP1 homology|||Loss of binding to PSMD2 and PSMC2, and loss of inhibitory effect on proteasome activity; when associated with E-49.|||Loss of binding to PSMD2 and PSMC2, and loss of inhibitory effect on proteasome activity; when associated with E-51.|||Loss of catalytic activity. No effect on interaction with 19S regulatory particle but loss of catalytic activity; when associated with A-145.|||N-acetylalanine|||N6-acetyllysine|||No effect on interaction with 19S regulatory particle but loss of catalytic activity; when associated with A-143.|||No effect on proteasome binding or nuclear localization.|||Removed|||Ubiquitin-like|||Ubiquitin-like domain-containing CTD phosphatase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242640
http://togogenome.org/gene/9606:SPZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA5|||http://purl.uniprot.org/uniprot/Q9BXG8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic motif|||Disordered|||Helix-loop-helix motif|||Leucine-zipper|||Phosphoserine|||Polar residues|||Spermatogenic leucine zipper protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280507|||http://purl.uniprot.org/annotation/VAR_031160|||http://purl.uniprot.org/annotation/VAR_031161
http://togogenome.org/gene/9606:TRMT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GJ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrion|||Nucleophile|||Proton acceptor|||tRNA (uracil-5-)-methyltransferase homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311932|||http://purl.uniprot.org/annotation/VAR_037355|||http://purl.uniprot.org/annotation/VSP_029643|||http://purl.uniprot.org/annotation/VSP_029644
http://togogenome.org/gene/9606:ELFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7U0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Protein ELFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343738
http://togogenome.org/gene/9606:ZNF556                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ3|||http://purl.uniprot.org/uniprot/Q9HAH1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 556                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274876|||http://purl.uniprot.org/annotation/VAR_030355|||http://purl.uniprot.org/annotation/VAR_052863|||http://purl.uniprot.org/annotation/VAR_052864|||http://purl.uniprot.org/annotation/VAR_052865
http://togogenome.org/gene/9606:CAMK2G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2Q3DQE3|||http://purl.uniprot.org/uniprot/B3KY86|||http://purl.uniprot.org/uniprot/Q13280|||http://purl.uniprot.org/uniprot/Q13555|||http://purl.uniprot.org/uniprot/Q5SWX3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase II association-domain|||Calcium/calmodulin-dependent protein kinase type II subunit gamma|||Calmodulin-binding|||Disordered|||In MRD59; gain-of-function variant affecting regulation of neurite formation and arborization; results in constitutive autophosphorylation.|||In isoform 11.|||In isoform 2, isoform 8, isoform 9 and isoform 11.|||In isoform 3, isoform 7 and isoform 10.|||In isoform 4, isoform 5 and isoform 10.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 9.|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086101|||http://purl.uniprot.org/annotation/VAR_042430|||http://purl.uniprot.org/annotation/VAR_069390|||http://purl.uniprot.org/annotation/VSP_004778|||http://purl.uniprot.org/annotation/VSP_013349|||http://purl.uniprot.org/annotation/VSP_013350|||http://purl.uniprot.org/annotation/VSP_032699|||http://purl.uniprot.org/annotation/VSP_032700|||http://purl.uniprot.org/annotation/VSP_035456|||http://purl.uniprot.org/annotation/VSP_036027|||http://purl.uniprot.org/annotation/VSP_059393|||http://purl.uniprot.org/annotation/VSP_059394
http://togogenome.org/gene/9606:SYAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A49                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  BSD|||Disordered|||Inhibits interaction with AKT1, mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' and adipocyte differentiation.|||Phosphoserine|||Phosphothreonine|||Synapse-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072355
http://togogenome.org/gene/9606:SP140                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVW8|||http://purl.uniprot.org/uniprot/Q0VGE4|||http://purl.uniprot.org/uniprot/Q13342|||http://purl.uniprot.org/uniprot/Q8IWJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo|||Disordered|||HSR|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform LYSp100-A and isoform 6.|||In isoform LYSp100-A.|||In isoform Sp140.|||Nuclear body protein SP140|||Nuclear localization signal|||PHD-type|||Phosphothreonine|||Polar residues|||SAND                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211206|||http://purl.uniprot.org/annotation/VAR_055555|||http://purl.uniprot.org/annotation/VAR_055556|||http://purl.uniprot.org/annotation/VAR_055557|||http://purl.uniprot.org/annotation/VAR_055558|||http://purl.uniprot.org/annotation/VSP_000558|||http://purl.uniprot.org/annotation/VSP_000559|||http://purl.uniprot.org/annotation/VSP_000560|||http://purl.uniprot.org/annotation/VSP_000561|||http://purl.uniprot.org/annotation/VSP_000562|||http://purl.uniprot.org/annotation/VSP_043235|||http://purl.uniprot.org/annotation/VSP_043236|||http://purl.uniprot.org/annotation/VSP_055922|||http://purl.uniprot.org/annotation/VSP_055923|||http://purl.uniprot.org/annotation/VSP_055924
http://togogenome.org/gene/9606:NAPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FHY4|||http://purl.uniprot.org/uniprot/Q99747                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gamma-soluble NSF attachment protein|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219063|||http://purl.uniprot.org/annotation/VAR_020129|||http://purl.uniprot.org/annotation/VAR_052027|||http://purl.uniprot.org/annotation/VSP_056355
http://togogenome.org/gene/9606:CLDN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95484                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes HCV infection susceptibility in cell culture.|||Claudin-9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mildly decrease HCV infection susceptibility in cell culture.|||No effect on HCV infection susceptibility in cell culture.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144755
http://togogenome.org/gene/9606:HYAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43820                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like|||Hyaluronidase-3|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248200|||http://purl.uniprot.org/annotation/VAR_027263|||http://purl.uniprot.org/annotation/VSP_020192|||http://purl.uniprot.org/annotation/VSP_020193|||http://purl.uniprot.org/annotation/VSP_020194
http://togogenome.org/gene/9606:SCX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic helix-loop-helix transcription factor scleraxis|||Disordered|||Pro residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273317
http://togogenome.org/gene/9606:ZNF514                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||KRAB|||Zinc finger protein 514                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047633
http://togogenome.org/gene/9606:H3C14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71DI3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolishes S-palmitoylation.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.2|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||S-palmitoyl cysteine|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250357|||http://purl.uniprot.org/annotation/VAR_059313|||http://purl.uniprot.org/annotation/VAR_059314
http://togogenome.org/gene/9606:CARHSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2V2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  CSD|||Calcium-regulated heat-stable protein 1|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Reduced affinity for single-stranded DNA.|||Reduced affinity for single-stranded DNA. Abolishes location at cytoplasmic stress granules.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100230
http://togogenome.org/gene/9606:ACADVL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPA6|||http://purl.uniprot.org/uniprot/P49748                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Catalytic|||Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.|||Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.|||Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.|||Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.|||Disordered|||In ACADVLD.|||In ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane.|||In ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro.|||In ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates.|||In ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding.|||In ACADVLD; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.|||Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.|||Membrane-anchoring|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||S-nitrosocysteine|||Very long-chain specific acyl-CoA dehydrogenase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000515|||http://purl.uniprot.org/annotation/VAR_000330|||http://purl.uniprot.org/annotation/VAR_000331|||http://purl.uniprot.org/annotation/VAR_000332|||http://purl.uniprot.org/annotation/VAR_000333|||http://purl.uniprot.org/annotation/VAR_000334|||http://purl.uniprot.org/annotation/VAR_000335|||http://purl.uniprot.org/annotation/VAR_000336|||http://purl.uniprot.org/annotation/VAR_000337|||http://purl.uniprot.org/annotation/VAR_000338|||http://purl.uniprot.org/annotation/VAR_000339|||http://purl.uniprot.org/annotation/VAR_000340|||http://purl.uniprot.org/annotation/VAR_000341|||http://purl.uniprot.org/annotation/VAR_000342|||http://purl.uniprot.org/annotation/VAR_000343|||http://purl.uniprot.org/annotation/VAR_000344|||http://purl.uniprot.org/annotation/VAR_000345|||http://purl.uniprot.org/annotation/VAR_000346|||http://purl.uniprot.org/annotation/VAR_000347|||http://purl.uniprot.org/annotation/VAR_000348|||http://purl.uniprot.org/annotation/VAR_000349|||http://purl.uniprot.org/annotation/VAR_000350|||http://purl.uniprot.org/annotation/VAR_000351|||http://purl.uniprot.org/annotation/VAR_000352|||http://purl.uniprot.org/annotation/VAR_000353|||http://purl.uniprot.org/annotation/VAR_000354|||http://purl.uniprot.org/annotation/VAR_000355|||http://purl.uniprot.org/annotation/VAR_000356|||http://purl.uniprot.org/annotation/VAR_000357|||http://purl.uniprot.org/annotation/VAR_000358|||http://purl.uniprot.org/annotation/VAR_000359|||http://purl.uniprot.org/annotation/VAR_000360|||http://purl.uniprot.org/annotation/VAR_000361|||http://purl.uniprot.org/annotation/VAR_000362|||http://purl.uniprot.org/annotation/VAR_000363|||http://purl.uniprot.org/annotation/VAR_000364|||http://purl.uniprot.org/annotation/VAR_000365|||http://purl.uniprot.org/annotation/VAR_010101|||http://purl.uniprot.org/annotation/VAR_010102|||http://purl.uniprot.org/annotation/VAR_010103|||http://purl.uniprot.org/annotation/VAR_010104|||http://purl.uniprot.org/annotation/VAR_010105|||http://purl.uniprot.org/annotation/VAR_010106|||http://purl.uniprot.org/annotation/VAR_011990|||http://purl.uniprot.org/annotation/VAR_011991|||http://purl.uniprot.org/annotation/VAR_029286|||http://purl.uniprot.org/annotation/VAR_048176|||http://purl.uniprot.org/annotation/VAR_083892|||http://purl.uniprot.org/annotation/VSP_007734|||http://purl.uniprot.org/annotation/VSP_046031
http://togogenome.org/gene/9606:DDX3Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15523                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX3Y|||Basic and acidic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055011|||http://purl.uniprot.org/annotation/VSP_055456|||http://purl.uniprot.org/annotation/VSP_055457|||http://purl.uniprot.org/annotation/VSP_055458
http://togogenome.org/gene/9606:IL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C389|||http://purl.uniprot.org/uniprot/Q9GZX6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interleukin-22|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015383|||http://purl.uniprot.org/annotation/PRO_5036208299|||http://purl.uniprot.org/annotation/VAR_013078
http://togogenome.org/gene/9606:VDR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11473                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Abolishes nuclear export.|||Disordered|||Hinge|||In VDDR2A.|||In VDDR2A; decreased calcitriol receptor activity; decreased affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; decreased interaction with NCOR1; decreased interaction with NCOA1; decreased sequence-specific DNA-binding.|||In VDDR2A; loss of calcitriol receptor activity; decreased affinity for calcitriol by a factor of 1000; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding.|||In VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; decreased ligand-independent localization to the nucleus; loss of interaction with RXRA; loss of interaction with NCOR1; loss of interaction with NCOA1; loss of sequence-specific DNA-binding.|||In VDDR2A; loss of calcitriol receptor activity; loss of affinity for calcitriol; no effect on ligand-independent localization to the nucleus.|||In VDDR2A; loss of calcitriol receptor activity; no effect on interaction with RXRA; changed interaction with NCOR1; loss of interaction with NCOA1; no effect on sequence-specific DNA-binding.|||In isoform 2.|||Interaction with coactivator LXXLL motif|||NR C4-type|||NR LBD|||Nuclear receptor|||Polar residues|||Promotes heterodimerization with RXRA; when associated with A-61 and A-62.|||Promotes heterodimerization with RXRA; when associated with A-75.|||Vitamin D3 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053542|||http://purl.uniprot.org/annotation/VAR_004656|||http://purl.uniprot.org/annotation/VAR_004657|||http://purl.uniprot.org/annotation/VAR_004658|||http://purl.uniprot.org/annotation/VAR_004659|||http://purl.uniprot.org/annotation/VAR_004660|||http://purl.uniprot.org/annotation/VAR_004661|||http://purl.uniprot.org/annotation/VAR_004662|||http://purl.uniprot.org/annotation/VAR_004663|||http://purl.uniprot.org/annotation/VAR_004664|||http://purl.uniprot.org/annotation/VAR_004665|||http://purl.uniprot.org/annotation/VAR_004666|||http://purl.uniprot.org/annotation/VAR_004667|||http://purl.uniprot.org/annotation/VAR_029309|||http://purl.uniprot.org/annotation/VAR_029310|||http://purl.uniprot.org/annotation/VAR_079325|||http://purl.uniprot.org/annotation/VAR_079326|||http://purl.uniprot.org/annotation/VAR_079327|||http://purl.uniprot.org/annotation/VSP_047218
http://togogenome.org/gene/9606:OR13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD8|||http://purl.uniprot.org/uniprot/Q8NGR1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150730
http://togogenome.org/gene/9606:SMAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15797                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the formation of the CHIP-SMAD1 complex.|||Decreases interaction with RANBPL3.|||Disordered|||Found in a patient with primary pulmonary hypertension; unknown pathological significance; affects SMAD-mediated signaling.|||In isoform 2.|||Increases interaction with RANBPL3.|||L3 loop|||Loss of phosphorylation.|||MH1|||MH2|||Mothers against decapentaplegic homolog 1|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by MINK1, TNIK and MAP4K4|||Polar residues|||Pro residues|||Reduced trimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090847|||http://purl.uniprot.org/annotation/VAR_066869|||http://purl.uniprot.org/annotation/VSP_057163|||http://purl.uniprot.org/annotation/VSP_057164|||http://purl.uniprot.org/annotation/VSP_057165|||http://purl.uniprot.org/annotation/VSP_057166
http://togogenome.org/gene/9606:GEMIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14893                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Gem-associated protein 2|||Impairs binding to SMN1.|||Impairs binding to Sm complex proteins.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||May play a minor inhibitory role in snRNA binding to 5Sm (SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG) during snRNP assembly by inserting into the RNA binding pocket of 5Sm|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087455|||http://purl.uniprot.org/annotation/VSP_013543|||http://purl.uniprot.org/annotation/VSP_013544|||http://purl.uniprot.org/annotation/VSP_013545|||http://purl.uniprot.org/annotation/VSP_013546|||http://purl.uniprot.org/annotation/VSP_013547|||http://purl.uniprot.org/annotation/VSP_061433
http://togogenome.org/gene/9606:CIB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK09|||http://purl.uniprot.org/uniprot/Q99828                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcium and integrin-binding protein 1|||Cytoplasmic localization.|||EF-hand|||EF-hand 1|||EF-hand 2|||In EV3; absence of CIB1 protein in homozygous patient cells.|||In isoform 2.|||Inhibits translocation to the plasma membrane. Increased apoptosis after TNF stimulation.|||Loss of binding to ITGA2B.|||Loss of binding to ITGA2B. Does not inhibit interaction with PAK1.|||Loss of binding to ITGAV.|||Loss of phosphorylation by PKD/PRKD2; in isoform 2.|||N-myristoyl glycine|||No effect on phosphorylation by PKD/PRKD2; in isoform 2.|||Phosphomimetic; promotes tumor growth by an indirect mechanism; in isoform 2.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073531|||http://purl.uniprot.org/annotation/VAR_019565|||http://purl.uniprot.org/annotation/VAR_048636|||http://purl.uniprot.org/annotation/VAR_081784|||http://purl.uniprot.org/annotation/VSP_053740
http://togogenome.org/gene/9606:TNFSF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5JA19|||http://purl.uniprot.org/uniprot/O95150                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Important for binding TNFRSF6B|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 15, membrane form|||Tumor necrosis factor ligand superfamily member 15, secreted form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185505|||http://purl.uniprot.org/annotation/PRO_0000333234|||http://purl.uniprot.org/annotation/VAR_043130|||http://purl.uniprot.org/annotation/VSP_033492|||http://purl.uniprot.org/annotation/VSP_033493|||http://purl.uniprot.org/annotation/VSP_033494
http://togogenome.org/gene/9606:ADGRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor A1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In an acute myeloid leukemia, somatic mutation.|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070337|||http://purl.uniprot.org/annotation/VAR_055931|||http://purl.uniprot.org/annotation/VAR_055932|||http://purl.uniprot.org/annotation/VAR_082826|||http://purl.uniprot.org/annotation/VSP_040207|||http://purl.uniprot.org/annotation/VSP_040208|||http://purl.uniprot.org/annotation/VSP_040209
http://togogenome.org/gene/9606:MOSPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJG1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||MSP|||Motile sperm domain-containing protein 1|||Nuclear export signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213459|||http://purl.uniprot.org/annotation/VAR_036601|||http://purl.uniprot.org/annotation/VSP_014043|||http://purl.uniprot.org/annotation/VSP_014044
http://togogenome.org/gene/9606:FMOD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS64|||http://purl.uniprot.org/uniprot/Q06828|||http://purl.uniprot.org/uniprot/Q12833                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibromodulin|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) (keratan sulfate) asparagine|||N-linked (GlcNAc...) asparagine|||Not sulfated|||Pyrrolidone carboxylic acid|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032739
http://togogenome.org/gene/9606:KCNK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B6VPR3|||http://purl.uniprot.org/uniprot/O95279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel|||Potassium channel subfamily K member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101749|||http://purl.uniprot.org/annotation/VAR_052425
http://togogenome.org/gene/9606:ARHGEF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQ72|||http://purl.uniprot.org/uniprot/B7Z344|||http://purl.uniprot.org/uniprot/B7Z6G2|||http://purl.uniprot.org/uniprot/E9PDQ5|||http://purl.uniprot.org/uniprot/Q14155|||http://purl.uniprot.org/uniprot/Q5W9H1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||DH|||Disordered|||Found in a clear cell renal carcinoma case; somatic mutation.|||In isoform 1 and isoform 5.|||In isoform 1 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||N-acetylmethionine|||N-acetylthreonine|||PH|||Phosphoserine|||Phosphoserine; by CaMK1|||Polar residues|||Removed|||Rho guanine nucleotide exchange factor 7|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080921|||http://purl.uniprot.org/annotation/VAR_064694|||http://purl.uniprot.org/annotation/VSP_011032|||http://purl.uniprot.org/annotation/VSP_011033|||http://purl.uniprot.org/annotation/VSP_011034|||http://purl.uniprot.org/annotation/VSP_011035|||http://purl.uniprot.org/annotation/VSP_034639
http://togogenome.org/gene/9606:FBXL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXK8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 12|||Found in a renal cell carcinoma case; somatic mutation.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119857|||http://purl.uniprot.org/annotation/VAR_064712|||http://purl.uniprot.org/annotation/VSP_008859
http://togogenome.org/gene/9606:PPAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MV53|||http://purl.uniprot.org/uniprot/Q9NQ55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Brix|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Suppressor of SWI4 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120257|||http://purl.uniprot.org/annotation/VAR_022157|||http://purl.uniprot.org/annotation/VAR_048422|||http://purl.uniprot.org/annotation/VSP_003973|||http://purl.uniprot.org/annotation/VSP_046377
http://togogenome.org/gene/9606:NDUFB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43676                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Abolished histidine methylation by METTL9.|||Helical|||In MC1DN25.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3|||Pros-methylhistidine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118797|||http://purl.uniprot.org/annotation/VAR_078939|||http://purl.uniprot.org/annotation/VAR_078940
http://togogenome.org/gene/9606:TRPV6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1D0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Abolishes channel activity.|||Abolishes phosphorylation by PKC/PRKCA, achieves faster channel inactivation and no effect on binding to calmodulin.|||Cytoplasmic|||Decreases channel activity.|||Decreases channel opening, and thereby decreases channel activity.|||Decreases channel opening, and thereby strongly decreases channel activity.|||Extracellular|||Helical|||In HRPTTN; decreased localization at the plasma membrane; loss of calcium ion import across plasma membrane.|||In HRPTTN; decreased localization at the plasma membrane; no change in calcium ion import across plasma membrane.|||In HRPTTN; induces cell death most likely through intracellular calcium overload; increased calcium ion import across plasma membrane; may lack intracellular calcium-dependent inactivation.|||In isoform 2.|||Interaction with S100A10|||Interaction with calmodulin|||Likely benign variant; no effect on localization at the plasma membrane; no change in calcium ion import across plasma membrane.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKC/PRKCA|||Phosphotyrosine; by SRC|||Pore-forming|||Selectivity filter|||Transient receptor potential cation channel subfamily V member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215354|||http://purl.uniprot.org/annotation/VAR_022251|||http://purl.uniprot.org/annotation/VAR_022252|||http://purl.uniprot.org/annotation/VAR_022253|||http://purl.uniprot.org/annotation/VAR_052393|||http://purl.uniprot.org/annotation/VAR_081865|||http://purl.uniprot.org/annotation/VAR_081866|||http://purl.uniprot.org/annotation/VAR_081867|||http://purl.uniprot.org/annotation/VAR_081868|||http://purl.uniprot.org/annotation/VAR_081869|||http://purl.uniprot.org/annotation/VAR_081870|||http://purl.uniprot.org/annotation/VAR_081871|||http://purl.uniprot.org/annotation/VSP_013439
http://togogenome.org/gene/9606:PRLH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P81277|||http://purl.uniprot.org/uniprot/Q53QV7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Phenylalanine amide|||Prolactin-releasing peptide PrRP20|||Prolactin-releasing peptide PrRP31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022144|||http://purl.uniprot.org/annotation/PRO_0000022145|||http://purl.uniprot.org/annotation/PRO_0000022146|||http://purl.uniprot.org/annotation/PRO_5014309551
http://togogenome.org/gene/9606:CCR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51681|||http://purl.uniprot.org/uniprot/Q38L21                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349; abolishes interaction with ARRB2; when associated with S-337; S-342 and S-349.|||APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349; abolishes interaction with ARRB2; when associated with S-336; S-342 and S-349.|||APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-349.|||APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-342.|||Associated with susceptibility to HIV-1; reduced cell surface expression; may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors.|||C-C chemokine receptor type 5|||Cytoplasmic|||Decreases to 40% surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection.|||Decreases to 40% surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection.|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In INCCR5-45C.|||In INCCR5-467.|||In INCCR5-71A.|||In INCCR5-71A; results in absent sulfation and greatly decreased binding CCL4 and CCL5 when associated with D-3, D-10 and D-15; restored most CCL4 binding when associated with D-3 and D-15.|||In INCCR5-72A.|||In KECCR5-116.|||In KECCR5-3B.|||In MWCCR5-107.|||In MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112.|||In MWCCR5-1567.|||In THCCR5-2.|||In THCCR5-5.|||In TZCCR5-179.|||In TZCCR5-181A and MWCCR5-107.|||In UGCCR5-145A.|||In UGCCR5-145B.|||In UGCCR5-145C.|||In ZWCCR5-7.|||No change in glycosylation status and binds CCL4 as efficiently as wild type. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-6; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-6 only.|||No change in glycosylation status and greatly decreased CCL4 binding. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-7; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-7 only.|||No sulfation and greatly decreased binding of CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restored most CCL4 binding; when associated with D-10 and D-15.|||No sulfation and greatly decreased binding of CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15.|||No sulfation and greatly decreased binding of CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10.|||No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15.|||No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14.|||No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15.|||No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15.|||O-linked (GalNAc...) serine|||Phosphoserine; by BARK1|||Protects against HIV-1 infection; CD4+ T-cells from R-106 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression.|||Protects against HIV-1 infection; CD4+ T-cells from R-178 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression.|||S-palmitoyl cysteine|||Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16.|||Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17.|||Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323.|||Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324.|||Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324.|||Sulfotyrosine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069257|||http://purl.uniprot.org/annotation/VAR_003481|||http://purl.uniprot.org/annotation/VAR_003482|||http://purl.uniprot.org/annotation/VAR_003483|||http://purl.uniprot.org/annotation/VAR_003484|||http://purl.uniprot.org/annotation/VAR_003485|||http://purl.uniprot.org/annotation/VAR_003486|||http://purl.uniprot.org/annotation/VAR_003487|||http://purl.uniprot.org/annotation/VAR_003488|||http://purl.uniprot.org/annotation/VAR_003489|||http://purl.uniprot.org/annotation/VAR_003490|||http://purl.uniprot.org/annotation/VAR_003491|||http://purl.uniprot.org/annotation/VAR_003492|||http://purl.uniprot.org/annotation/VAR_003493|||http://purl.uniprot.org/annotation/VAR_003494|||http://purl.uniprot.org/annotation/VAR_003495|||http://purl.uniprot.org/annotation/VAR_003496|||http://purl.uniprot.org/annotation/VAR_003497|||http://purl.uniprot.org/annotation/VAR_003498|||http://purl.uniprot.org/annotation/VAR_003499|||http://purl.uniprot.org/annotation/VAR_003500|||http://purl.uniprot.org/annotation/VAR_003501|||http://purl.uniprot.org/annotation/VAR_003502|||http://purl.uniprot.org/annotation/VAR_003503|||http://purl.uniprot.org/annotation/VAR_003504|||http://purl.uniprot.org/annotation/VAR_003505|||http://purl.uniprot.org/annotation/VAR_011839|||http://purl.uniprot.org/annotation/VAR_011840|||http://purl.uniprot.org/annotation/VAR_011841|||http://purl.uniprot.org/annotation/VAR_011842|||http://purl.uniprot.org/annotation/VAR_011843|||http://purl.uniprot.org/annotation/VAR_012481|||http://purl.uniprot.org/annotation/VAR_024066|||http://purl.uniprot.org/annotation/VAR_024067|||http://purl.uniprot.org/annotation/VAR_024068|||http://purl.uniprot.org/annotation/VAR_024069|||http://purl.uniprot.org/annotation/VAR_024070|||http://purl.uniprot.org/annotation/VAR_024071|||http://purl.uniprot.org/annotation/VAR_080410
http://togogenome.org/gene/9606:RASGEF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAM2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 2.|||N-terminal Ras-GEF|||Ras-GEF|||Ras-GEF domain-containing family member 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297638|||http://purl.uniprot.org/annotation/VSP_027313|||http://purl.uniprot.org/annotation/VSP_027314
http://togogenome.org/gene/9606:SLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFT9|||http://purl.uniprot.org/uniprot/O00631                                                                                  ^@                                                                                  Helix|||Molecule Processing|||Peptide|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helix|||Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Sarcolipin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045898
http://togogenome.org/gene/9606:C16orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWD8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphothreonine|||Transmembrane protein C16orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279442
http://togogenome.org/gene/9606:NLRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C3VPR7|||http://purl.uniprot.org/uniprot/Q7RTR2|||http://purl.uniprot.org/uniprot/Q8NF06                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Almost no effect on TRAF6-binding.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NLR family CARD domain-containing protein 3|||Strong decrease of TRAF6-binding.|||TRAF6-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296187|||http://purl.uniprot.org/annotation/VAR_034606|||http://purl.uniprot.org/annotation/VSP_027135|||http://purl.uniprot.org/annotation/VSP_027136|||http://purl.uniprot.org/annotation/VSP_027137|||http://purl.uniprot.org/annotation/VSP_027138
http://togogenome.org/gene/9606:GFI1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8F3|||http://purl.uniprot.org/uniprot/Q5VTD9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with ARIH2|||Mediates interaction with GATA1|||N6,N6-dimethyllysine|||Prevents DNA-binding.|||SNAG domain|||Zinc finger protein Gfi-1b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306327|||http://purl.uniprot.org/annotation/VAR_035556|||http://purl.uniprot.org/annotation/VSP_028459
http://togogenome.org/gene/9606:COL2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02458                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyproline|||4-hydroxyproline|||5-hydroxylysine|||Basic and acidic residues|||Chondrocalcin|||Cleavage; by procollagen C-endopeptidase|||Cleavage; by procollagen N-endopeptidase|||Collagen alpha-1(II) chain|||Disordered|||Fibrillar collagen NC1|||In ACG2 and SEDC.|||In ACG2.|||In ANFH1 and LCPD.|||In ANFH1.|||In CZECHD.|||In DRRD.|||In EDMMD and STL1.|||In KD.|||In KD; abnormal allele expressed in the cartilage.|||In OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis.|||In PLSD-T.|||In PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2.|||In SEDC and hypochondrogenesis; lethal.|||In SEDC.|||In SEDSTN.|||In SEMDSTWK.|||In STL1.|||In STL1O.|||In VPED.|||In hypochondrogenesis.|||In hypochondrogenesis; lethal.|||In isoform 1.|||In isoform 3.|||In spondylometaphyseal dysplasia; congenital type.|||Interchain (with C-1289)|||Interchain (with C-1306)|||Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC.|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Nonhelical region (C-terminal)|||O-linked (Gal...) hydroxylysine|||Pro residues|||Triple-helical region|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005729|||http://purl.uniprot.org/annotation/PRO_0000005730|||http://purl.uniprot.org/annotation/PRO_0000005731|||http://purl.uniprot.org/annotation/VAR_001738|||http://purl.uniprot.org/annotation/VAR_001739|||http://purl.uniprot.org/annotation/VAR_001740|||http://purl.uniprot.org/annotation/VAR_001741|||http://purl.uniprot.org/annotation/VAR_001742|||http://purl.uniprot.org/annotation/VAR_001743|||http://purl.uniprot.org/annotation/VAR_001744|||http://purl.uniprot.org/annotation/VAR_001745|||http://purl.uniprot.org/annotation/VAR_001746|||http://purl.uniprot.org/annotation/VAR_001747|||http://purl.uniprot.org/annotation/VAR_001748|||http://purl.uniprot.org/annotation/VAR_001749|||http://purl.uniprot.org/annotation/VAR_001751|||http://purl.uniprot.org/annotation/VAR_001752|||http://purl.uniprot.org/annotation/VAR_001753|||http://purl.uniprot.org/annotation/VAR_001754|||http://purl.uniprot.org/annotation/VAR_001755|||http://purl.uniprot.org/annotation/VAR_001756|||http://purl.uniprot.org/annotation/VAR_001757|||http://purl.uniprot.org/annotation/VAR_001758|||http://purl.uniprot.org/annotation/VAR_001759|||http://purl.uniprot.org/annotation/VAR_001760|||http://purl.uniprot.org/annotation/VAR_001761|||http://purl.uniprot.org/annotation/VAR_001762|||http://purl.uniprot.org/annotation/VAR_001763|||http://purl.uniprot.org/annotation/VAR_001764|||http://purl.uniprot.org/annotation/VAR_001765|||http://purl.uniprot.org/annotation/VAR_001766|||http://purl.uniprot.org/annotation/VAR_017105|||http://purl.uniprot.org/annotation/VAR_017638|||http://purl.uniprot.org/annotation/VAR_017639|||http://purl.uniprot.org/annotation/VAR_017640|||http://purl.uniprot.org/annotation/VAR_017641|||http://purl.uniprot.org/annotation/VAR_017642|||http://purl.uniprot.org/annotation/VAR_017643|||http://purl.uniprot.org/annotation/VAR_017644|||http://purl.uniprot.org/annotation/VAR_017645|||http://purl.uniprot.org/annotation/VAR_017646|||http://purl.uniprot.org/annotation/VAR_017647|||http://purl.uniprot.org/annotation/VAR_017648|||http://purl.uniprot.org/annotation/VAR_017649|||http://purl.uniprot.org/annotation/VAR_017650|||http://purl.uniprot.org/annotation/VAR_017651|||http://purl.uniprot.org/annotation/VAR_017652|||http://purl.uniprot.org/annotation/VAR_019836|||http://purl.uniprot.org/annotation/VAR_019837|||http://purl.uniprot.org/annotation/VAR_023925|||http://purl.uniprot.org/annotation/VAR_023926|||http://purl.uniprot.org/annotation/VAR_023927|||http://purl.uniprot.org/annotation/VAR_023928|||http://purl.uniprot.org/annotation/VAR_023929|||http://purl.uniprot.org/annotation/VAR_023930|||http://purl.uniprot.org/annotation/VAR_023931|||http://purl.uniprot.org/annotation/VAR_023932|||http://purl.uniprot.org/annotation/VAR_023933|||http://purl.uniprot.org/annotation/VAR_023934|||http://purl.uniprot.org/annotation/VAR_023935|||http://purl.uniprot.org/annotation/VAR_024819|||http://purl.uniprot.org/annotation/VAR_024820|||http://purl.uniprot.org/annotation/VAR_024821|||http://purl.uniprot.org/annotation/VAR_024822|||http://purl.uniprot.org/annotation/VAR_024823|||http://purl.uniprot.org/annotation/VAR_024824|||http://purl.uniprot.org/annotation/VAR_024825|||http://purl.uniprot.org/annotation/VAR_024826|||http://purl.uniprot.org/annotation/VAR_033782|||http://purl.uniprot.org/annotation/VAR_033783|||http://purl.uniprot.org/annotation/VAR_033784|||http://purl.uniprot.org/annotation/VAR_033785|||http://purl.uniprot.org/annotation/VAR_063891|||http://purl.uniprot.org/annotation/VAR_063892|||http://purl.uniprot.org/annotation/VAR_063893|||http://purl.uniprot.org/annotation/VAR_063894|||http://purl.uniprot.org/annotation/VAR_063895|||http://purl.uniprot.org/annotation/VAR_063896|||http://purl.uniprot.org/annotation/VAR_063897|||http://purl.uniprot.org/annotation/VAR_063898|||http://purl.uniprot.org/annotation/VAR_066836|||http://purl.uniprot.org/annotation/VAR_066837|||http://purl.uniprot.org/annotation/VAR_075729|||http://purl.uniprot.org/annotation/VAR_075730|||http://purl.uniprot.org/annotation/VAR_079748|||http://purl.uniprot.org/annotation/VSP_022365|||http://purl.uniprot.org/annotation/VSP_022366
http://togogenome.org/gene/9606:EXD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9H8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3'-5' exonuclease|||Disordered|||Exonuclease mut-7 homolog|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319059|||http://purl.uniprot.org/annotation/VAR_038945|||http://purl.uniprot.org/annotation/VAR_062225|||http://purl.uniprot.org/annotation/VSP_031344|||http://purl.uniprot.org/annotation/VSP_031345|||http://purl.uniprot.org/annotation/VSP_031346|||http://purl.uniprot.org/annotation/VSP_031347|||http://purl.uniprot.org/annotation/VSP_031348|||http://purl.uniprot.org/annotation/VSP_031349|||http://purl.uniprot.org/annotation/VSP_031350|||http://purl.uniprot.org/annotation/VSP_059361|||http://purl.uniprot.org/annotation/VSP_059362
http://togogenome.org/gene/9606:PLCG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16885                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2|||C2|||Found in patients with chronic lymphocytic leukemia; associated with BTK mutation S-481; unknown pathological significance; results in resistance to ibrutinib therapy.|||In APLAID; results in increased epidermal growth factor-stimulated production of intracellular IP3 and increased intracellular calcium release; is a hypermorphic mutation.|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphotyrosine|||Phosphotyrosine; by BTK|||SH2 1|||SH2 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088501|||http://purl.uniprot.org/annotation/VAR_031560|||http://purl.uniprot.org/annotation/VAR_031561|||http://purl.uniprot.org/annotation/VAR_047427|||http://purl.uniprot.org/annotation/VAR_047428|||http://purl.uniprot.org/annotation/VAR_069211|||http://purl.uniprot.org/annotation/VAR_074310|||http://purl.uniprot.org/annotation/VAR_074311
http://togogenome.org/gene/9606:MAGEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of interaction with NSMCE1.|||MAGE|||Melanoma-associated antigen F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156732|||http://purl.uniprot.org/annotation/VAR_057651
http://togogenome.org/gene/9606:MFAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Microfibrillar-associated protein 1|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096458
http://togogenome.org/gene/9606:RNF113B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||RING finger protein 113B|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056088|||http://purl.uniprot.org/annotation/VAR_052104
http://togogenome.org/gene/9606:TSC22D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN36|||http://purl.uniprot.org/uniprot/O75157                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Pro residues|||TSC22 domain family protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219369|||http://purl.uniprot.org/annotation/VAR_052408|||http://purl.uniprot.org/annotation/VSP_013202
http://togogenome.org/gene/9606:ANKEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NU02                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat and EF-hand domain-containing protein 1|||EF-hand|||In a breast cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066899|||http://purl.uniprot.org/annotation/VAR_024172|||http://purl.uniprot.org/annotation/VAR_033500|||http://purl.uniprot.org/annotation/VAR_033501|||http://purl.uniprot.org/annotation/VAR_033502|||http://purl.uniprot.org/annotation/VAR_035609
http://togogenome.org/gene/9606:SH3BP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60239                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of guanine nucleotide exchange factor activity.|||Loss of phosphorylation and binding by phospho-JNK; when associated with A-347.|||Loss of phosphorylation and binding by phospho-JNK; when associated with A-349.|||No change of phosphorylation or binding by phospho-JNK; when associated with A-434.|||No change of phosphorylation or binding by phospho-JNK; when associated with A-436.|||Phosphoserine|||Phosphoserine; by MAPK12 and MAPK9|||Polar residues|||SH3 domain-binding protein 5|||Sufficient for interaction with RAB11A and for guanine nucleotide exchange activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064368|||http://purl.uniprot.org/annotation/VSP_042854
http://togogenome.org/gene/9606:PRPF39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||In isoform 2.|||Phosphoserine|||Pre-mRNA-processing factor 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259648|||http://purl.uniprot.org/annotation/VSP_021496|||http://purl.uniprot.org/annotation/VSP_021497
http://togogenome.org/gene/9606:IER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTL4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Immediate early response gene 2 protein|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190435|||http://purl.uniprot.org/annotation/VAR_057581
http://togogenome.org/gene/9606:DKKL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK15|||http://purl.uniprot.org/uniprot/Q9UK85                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Dickkopf-like protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007228|||http://purl.uniprot.org/annotation/PRO_5007491747|||http://purl.uniprot.org/annotation/VAR_021967|||http://purl.uniprot.org/annotation/VAR_021968|||http://purl.uniprot.org/annotation/VAR_024432|||http://purl.uniprot.org/annotation/VAR_053061|||http://purl.uniprot.org/annotation/VAR_053062|||http://purl.uniprot.org/annotation/VAR_053063
http://togogenome.org/gene/9606:YEATS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W0J4|||http://purl.uniprot.org/uniprot/O95619                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Diacetylated histone H3 binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired binding to histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac), and subsequent deposition of histone H2AZ1/H2A.Z into specific chromatin regions; when associated with A-74.|||Impaired binding to histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac), and subsequent deposition of histone H2AZ1/H2A.Z into specific chromatin regions; when associated with A-93.|||Impaired binding to histone H3 succinylated at 'Lys-122' (H3K122succ).|||Interaction with MLLT10|||Interaction with TACC1|||Interacts with diacetylated histone H3|||YEATS|||YEATS domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066204
http://togogenome.org/gene/9606:BICD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD16|||http://purl.uniprot.org/uniprot/Q96FU2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In SMALED2A.|||In SMALED2A; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein.|||In SMALED2A; causes Golgi fragmentation.|||In SMALED2A; causes Golgi fragmentation; affects interaction with RAB6A and DNAI1 and the subcellular location of the protein.|||In SMALED2A; the mutation causes increased interaction with dynein; the mutant protein accumulates abnormally in the perinuclear region where it forms ring-like structures that colocalize with RAB6A.|||In SMALED2B.|||In isoform 2.|||Interaction with KIF5A|||Interaction with RANBP2|||Interacts with DYNLL1, DYNC1H1, DYNC1I2, DCTN1 and DCTN2|||Interacts with RAB6A|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Protein bicaudal D homolog 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205359|||http://purl.uniprot.org/annotation/VAR_070111|||http://purl.uniprot.org/annotation/VAR_070112|||http://purl.uniprot.org/annotation/VAR_070113|||http://purl.uniprot.org/annotation/VAR_070114|||http://purl.uniprot.org/annotation/VAR_070115|||http://purl.uniprot.org/annotation/VAR_070116|||http://purl.uniprot.org/annotation/VAR_070117|||http://purl.uniprot.org/annotation/VAR_070118|||http://purl.uniprot.org/annotation/VAR_081854|||http://purl.uniprot.org/annotation/VAR_081855|||http://purl.uniprot.org/annotation/VAR_081856|||http://purl.uniprot.org/annotation/VAR_081857|||http://purl.uniprot.org/annotation/VSP_007969
http://togogenome.org/gene/9606:SPART                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDV9|||http://purl.uniprot.org/uniprot/Q8N0X7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with IST1. Does not localize to the midbody.|||Abolishes interaction with ITCH and WWP1.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In SPG20; significant decrease in protein expression; significantly reduced COX respiratory chain complex IV activity in muscle mitochondria.|||In SPG20; unknown pathological significance.|||MIT|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Senescence|||Spartin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072119|||http://purl.uniprot.org/annotation/VAR_079569|||http://purl.uniprot.org/annotation/VAR_079570
http://togogenome.org/gene/9606:COL17A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  120 kDa linear IgA disease antigen|||97 kDa linear IgA disease antigen|||Basic and acidic residues|||Collagen alpha-1(XVII) chain|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In ERED.|||In JEB4.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with DST and for the recruitment of DST to hemidesmosome|||Nonhelical region (NC1)|||Nonhelical region (NC16)|||Phosphoserine; by CK2|||Polar residues|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059406|||http://purl.uniprot.org/annotation/PRO_0000342555|||http://purl.uniprot.org/annotation/PRO_0000342556|||http://purl.uniprot.org/annotation/VAR_017593|||http://purl.uniprot.org/annotation/VAR_017594|||http://purl.uniprot.org/annotation/VAR_017595|||http://purl.uniprot.org/annotation/VAR_017596|||http://purl.uniprot.org/annotation/VAR_017597|||http://purl.uniprot.org/annotation/VAR_017598|||http://purl.uniprot.org/annotation/VAR_017599|||http://purl.uniprot.org/annotation/VAR_017600|||http://purl.uniprot.org/annotation/VAR_017601|||http://purl.uniprot.org/annotation/VAR_017602|||http://purl.uniprot.org/annotation/VAR_048781|||http://purl.uniprot.org/annotation/VAR_074627|||http://purl.uniprot.org/annotation/VSP_024940|||http://purl.uniprot.org/annotation/VSP_024941
http://togogenome.org/gene/9606:ABCG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H222                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 5|||Abolishes increase of the very low basal ATPase activity by cholate.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In STSL2.|||In STSL2; decreased maturation of glycan chains.|||In STSL2; loss of normal maturation of glycan chains.|||In STSL2; strongly decreased maturation of glycan chains.|||In STSL2; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Strongly decreases cholesterol secretion into bile.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093393|||http://purl.uniprot.org/annotation/VAR_012244|||http://purl.uniprot.org/annotation/VAR_012245|||http://purl.uniprot.org/annotation/VAR_012246|||http://purl.uniprot.org/annotation/VAR_012247|||http://purl.uniprot.org/annotation/VAR_012248|||http://purl.uniprot.org/annotation/VAR_012249|||http://purl.uniprot.org/annotation/VAR_020781|||http://purl.uniprot.org/annotation/VAR_020782|||http://purl.uniprot.org/annotation/VAR_020783|||http://purl.uniprot.org/annotation/VAR_020784|||http://purl.uniprot.org/annotation/VAR_033457|||http://purl.uniprot.org/annotation/VAR_048142|||http://purl.uniprot.org/annotation/VAR_086593|||http://purl.uniprot.org/annotation/VSP_055770
http://togogenome.org/gene/9606:IPPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8X2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EXKPK motif|||Inositol-pentakisphosphate 2-kinase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110529|||http://purl.uniprot.org/annotation/VAR_049641|||http://purl.uniprot.org/annotation/VAR_049642
http://togogenome.org/gene/9606:HS6ST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60243                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Heparan-sulfate 6-O-sulfotransferase 1|||In HH15.|||In HH15; 15 to 30% reduction in enzymatic activity compared to wild-type.|||In HH15; approximately 30% reduction in enzymatic activity compared to wild-type when heparan sulfate is the acceptor substrate.|||In HH15; with anosmia; 30 to 70% reduction in enzymatic activity compared to wild-type.|||In HH15; with anosmia; results in Kallmann syndrome in the presence of FGFR1 mutation Gln-250; approximately 50% reduction in enzymatic activity compared to wild-type.|||In HH15; with or without anosmia; results in Kallmann syndrome in the presence of NSMF mutation Ala-480; 25 to 35% reduction in enzymatic activity compared to wild-type.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190801|||http://purl.uniprot.org/annotation/VAR_069283|||http://purl.uniprot.org/annotation/VAR_069284|||http://purl.uniprot.org/annotation/VAR_069285|||http://purl.uniprot.org/annotation/VAR_069286|||http://purl.uniprot.org/annotation/VAR_069287|||http://purl.uniprot.org/annotation/VAR_072980|||http://purl.uniprot.org/annotation/VSP_037048|||http://purl.uniprot.org/annotation/VSP_037049
http://togogenome.org/gene/9606:SLC52A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PKE4|||http://purl.uniprot.org/uniprot/Q9HAB3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In BVVLS2; decreased riboflavin transport.|||In BVVLS2; decreased riboflavin transport; decreased localization to plasma membrane; no effect on protein abundance.|||In BVVLS2; decreased riboflavin transport; no effect on localization to plasma membrane.|||In BVVLS2; loss of riboflavin transport; loss of localization to plasma membrane; no effect on protein abundance.|||In BVVLS2; strong decrease in riboflavin transport; no effect on localization to plasma membrane; no effect on protein abundance.|||In BVVLS2; strongly decreased riboflavin transport.|||Riboflavin transporter|||Solute carrier family 52, riboflavin transporter, member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042631|||http://purl.uniprot.org/annotation/PRO_5040054234|||http://purl.uniprot.org/annotation/VAR_068694|||http://purl.uniprot.org/annotation/VAR_077433|||http://purl.uniprot.org/annotation/VAR_077434|||http://purl.uniprot.org/annotation/VAR_077435|||http://purl.uniprot.org/annotation/VAR_077436|||http://purl.uniprot.org/annotation/VAR_077437|||http://purl.uniprot.org/annotation/VAR_077438|||http://purl.uniprot.org/annotation/VAR_077439|||http://purl.uniprot.org/annotation/VAR_077440|||http://purl.uniprot.org/annotation/VAR_077441
http://togogenome.org/gene/9606:KRT17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04695|||http://purl.uniprot.org/uniprot/Q14666                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S1.|||Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S4.|||Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S1.|||Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In PC2 and SM.|||In PC2.|||In SM and PC2.|||In SM.|||Keratin, type I cytoskeletal 17|||Linker 1|||Linker 12|||No significant effect on T-cell proliferation but can induce IFN-gamma production when part of the altered peptide epitope S2.|||No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2.|||No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4.|||No significant effect on T-cell proliferation or IFN-gamma production when part of the altered peptide epitope S1.|||Peptide epitope S1; induces T-cell and keratinocyte proliferation and IFN-gamma production|||Peptide epitope S2; induces T-cell proliferation and IFN-gamma production|||Peptide epitope S4; induces T-cell and keratinocyte proliferation and IFN-gamma production|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Phosphothreonine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063664|||http://purl.uniprot.org/annotation/VAR_003847|||http://purl.uniprot.org/annotation/VAR_003848|||http://purl.uniprot.org/annotation/VAR_003849|||http://purl.uniprot.org/annotation/VAR_003850|||http://purl.uniprot.org/annotation/VAR_003851|||http://purl.uniprot.org/annotation/VAR_010512|||http://purl.uniprot.org/annotation/VAR_010513|||http://purl.uniprot.org/annotation/VAR_017068|||http://purl.uniprot.org/annotation/VAR_017069|||http://purl.uniprot.org/annotation/VAR_017070|||http://purl.uniprot.org/annotation/VAR_017071|||http://purl.uniprot.org/annotation/VAR_017072|||http://purl.uniprot.org/annotation/VAR_017073|||http://purl.uniprot.org/annotation/VAR_017074|||http://purl.uniprot.org/annotation/VAR_037083|||http://purl.uniprot.org/annotation/VAR_072441|||http://purl.uniprot.org/annotation/VAR_072442|||http://purl.uniprot.org/annotation/VAR_072443|||http://purl.uniprot.org/annotation/VAR_072444|||http://purl.uniprot.org/annotation/VAR_072445
http://togogenome.org/gene/9606:PAK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCU6|||http://purl.uniprot.org/uniprot/O75914                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Autoregulatory region|||Basic and acidic residues|||CRIB|||Disordered|||GTPase-binding|||In XLID30.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Linker|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086469|||http://purl.uniprot.org/annotation/VAR_023825|||http://purl.uniprot.org/annotation/VAR_023826|||http://purl.uniprot.org/annotation/VAR_046764|||http://purl.uniprot.org/annotation/VSP_010242|||http://purl.uniprot.org/annotation/VSP_041839|||http://purl.uniprot.org/annotation/VSP_041840
http://togogenome.org/gene/9606:ADM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35318                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Adrenomedullin|||Arginine amide|||Disordered|||PreproAM C-terminal fragment|||Proadrenomedullin N-20 terminal peptide|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000961|||http://purl.uniprot.org/annotation/PRO_0000000962|||http://purl.uniprot.org/annotation/PRO_0000000963|||http://purl.uniprot.org/annotation/PRO_0000000964|||http://purl.uniprot.org/annotation/VAR_014861|||http://purl.uniprot.org/annotation/VAR_048205
http://togogenome.org/gene/9606:ZNF329                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UD4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Phosphoserine|||Zinc finger protein 329                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307288|||http://purl.uniprot.org/annotation/VAR_035403|||http://purl.uniprot.org/annotation/VAR_060428
http://togogenome.org/gene/9606:ELAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H777                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolsihed tRNase activity and ability to repair tRNAs downstream of ANKZF1.|||Proton acceptor|||Zinc phosphodiesterase ELAC protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155825|||http://purl.uniprot.org/annotation/VAR_017424
http://togogenome.org/gene/9606:TEX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXF1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  HEAT|||In isoform 2.|||Phosphothreonine|||Testis-expressed protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072491|||http://purl.uniprot.org/annotation/VSP_043704|||http://purl.uniprot.org/annotation/VSP_043705
http://togogenome.org/gene/9606:RIMBP3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJZ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Polar residues|||Pro residues|||RIMS-binding protein 3C|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332275
http://togogenome.org/gene/9606:ORC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13416                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Involved in LRWD1-binding|||Origin recognition complex subunit 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127075|||http://purl.uniprot.org/annotation/VAR_014515|||http://purl.uniprot.org/annotation/VAR_021276
http://togogenome.org/gene/9606:SPATA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6I5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Spermatogenesis-associated protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251198
http://togogenome.org/gene/9606:GPATCH2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G patch domain-containing protein 2-like|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089927|||http://purl.uniprot.org/annotation/VAR_056838|||http://purl.uniprot.org/annotation/VSP_014714|||http://purl.uniprot.org/annotation/VSP_014716|||http://purl.uniprot.org/annotation/VSP_039861
http://togogenome.org/gene/9606:CSNK1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DER9|||http://purl.uniprot.org/uniprot/P48729|||http://purl.uniprot.org/uniprot/Q6PJ06                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Casein kinase I isoform alpha|||Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192822|||http://purl.uniprot.org/annotation/VAR_042073|||http://purl.uniprot.org/annotation/VSP_035455|||http://purl.uniprot.org/annotation/VSP_055131
http://togogenome.org/gene/9606:NR4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GXF0|||http://purl.uniprot.org/uniprot/P22736|||http://purl.uniprot.org/uniprot/Q6ZMM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AF-2|||Abolishes binding to activity regulator Cytosporone B.|||Binds lipopolysaccharide|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of interaction with RXRA.|||NR C4-type|||NR LBD|||No impact on the interaction with RXRA.|||Nuclear receptor|||Nuclear receptor subfamily 4immunitygroup A member 1|||Phosphoserine|||Phosphoserine; by PKA|||Pro residues|||Required for binding NBRE-containing DNA|||Required for nuclear import|||Required for the interaction with RXRA|||Strongly weakens interaction with STK11.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053715|||http://purl.uniprot.org/annotation/VAR_061534|||http://purl.uniprot.org/annotation/VSP_043086|||http://purl.uniprot.org/annotation/VSP_047769|||http://purl.uniprot.org/annotation/VSP_047770
http://togogenome.org/gene/9606:CCDC28B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0TB33|||http://purl.uniprot.org/uniprot/Q9BUN5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 28B|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234094|||http://purl.uniprot.org/annotation/VAR_056776|||http://purl.uniprot.org/annotation/VSP_046552
http://togogenome.org/gene/9606:NDST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0V5|||http://purl.uniprot.org/uniprot/Q9H3R1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4|||Cytoplasmic|||For sulfotransferase activity|||Helical|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 4|||Heparan sulfate N-sulfotransferase 4|||Heparan sulphate-N-deacetylase|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sulfotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225661|||http://purl.uniprot.org/annotation/VAR_061890|||http://purl.uniprot.org/annotation/VSP_056256|||http://purl.uniprot.org/annotation/VSP_056257|||http://purl.uniprot.org/annotation/VSP_056258
http://togogenome.org/gene/9606:TTC9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6N2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||TPR 1|||TPR 2|||Tetratricopeptide repeat protein 9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294459|||http://purl.uniprot.org/annotation/VAR_052625|||http://purl.uniprot.org/annotation/VSP_026650
http://togogenome.org/gene/9606:CMTM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 3|||Disordered|||Helical|||In isoform 2.|||MARVEL|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186101|||http://purl.uniprot.org/annotation/VSP_008256|||http://purl.uniprot.org/annotation/VSP_008257
http://togogenome.org/gene/9606:TREX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TZT0|||http://purl.uniprot.org/uniprot/Q9NSU2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Exonuclease|||Helical|||In AGS1 and SLE.|||In AGS1 and SLE; primary fibroblasts from an AGS1 patient carrying H-169 show defective G1/S transition and chronic G2/MDNA damage checkpoint activation; strongly reduces activity.|||In AGS1; autosomal dominant form; no effect on dsDNA exonuclease activity; abolishes ssDNA exonuclease activity.|||In AGS1; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity.|||In AGS1; heterozygous compound with H-169; loss of activity.|||In AGS1; increases ubiquitination levels; no effect on exonuclease activity.|||In AGS1; reduces activity by 75%.|||In CHBL1 and AGS1; autosomal dominant form; loss of 3'-to-5' DNA exonuclease activity; abolished ability to degrade micronuclear DNA and restrict activation of innate immune response.|||In SLE.|||In SLE; associated in cis with P-302.|||In SLE; associated in cis with S-282.|||In SLE; decreases ubiquitination levels; decreases colocalization with UBQLN1; no effect on exonuclease activity.|||In SLE; increases ubiquitination levels; no effect on exonuclease activity.|||In isoform 1.|||In isoform 2.|||Interaction with UBQLN1|||Necessary for cytoplasmic retention|||Necessary for endoplasmic reticulum localization|||No effect on ubiquitination.|||Phosphoserine|||Polar residues|||Proton donor/acceptor|||Reduces ubiquitination.|||Reduces ubiquitination. Strongly reduces ubiquitination; when associated with R-271.|||Reduces ubiquitination. Strongly reduces ubiquitination; when associated with R-277.|||Three-prime repair exonuclease 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109868|||http://purl.uniprot.org/annotation/VAR_028319|||http://purl.uniprot.org/annotation/VAR_028320|||http://purl.uniprot.org/annotation/VAR_028321|||http://purl.uniprot.org/annotation/VAR_032940|||http://purl.uniprot.org/annotation/VAR_037948|||http://purl.uniprot.org/annotation/VAR_037949|||http://purl.uniprot.org/annotation/VAR_037950|||http://purl.uniprot.org/annotation/VAR_037951|||http://purl.uniprot.org/annotation/VAR_037952|||http://purl.uniprot.org/annotation/VAR_037953|||http://purl.uniprot.org/annotation/VAR_037954|||http://purl.uniprot.org/annotation/VAR_037955|||http://purl.uniprot.org/annotation/VAR_037956|||http://purl.uniprot.org/annotation/VAR_070899|||http://purl.uniprot.org/annotation/VAR_070900|||http://purl.uniprot.org/annotation/VAR_070901|||http://purl.uniprot.org/annotation/VAR_070902|||http://purl.uniprot.org/annotation/VSP_010445|||http://purl.uniprot.org/annotation/VSP_059279
http://togogenome.org/gene/9606:LRRC41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15345                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 3.|||Interaction with Elongin BC complex|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 41|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096645|||http://purl.uniprot.org/annotation/VAR_051117|||http://purl.uniprot.org/annotation/VSP_009234|||http://purl.uniprot.org/annotation/VSP_009235
http://togogenome.org/gene/9606:SDHAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRP4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||Succinate dehydrogenase assembly factor 3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042653
http://togogenome.org/gene/9606:MYNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPC7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Myoneurin|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248217|||http://purl.uniprot.org/annotation/VSP_020213|||http://purl.uniprot.org/annotation/VSP_020214|||http://purl.uniprot.org/annotation/VSP_020215|||http://purl.uniprot.org/annotation/VSP_020216|||http://purl.uniprot.org/annotation/VSP_020217
http://togogenome.org/gene/9606:DUSP22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NLC8|||http://purl.uniprot.org/uniprot/Q9NRW4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Dual specificity protein phosphatase 22|||In isoform 2.|||N-myristoyl glycine|||Phosphocysteine intermediate|||Phosphoserine|||Removed|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244751|||http://purl.uniprot.org/annotation/VAR_026912|||http://purl.uniprot.org/annotation/VSP_019614
http://togogenome.org/gene/9606:WDR31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA23|||http://purl.uniprot.org/uniprot/Q8NC90                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051380|||http://purl.uniprot.org/annotation/VAR_053426|||http://purl.uniprot.org/annotation/VSP_010418
http://togogenome.org/gene/9606:C17orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||Uncharacterized protein C17orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284612|||http://purl.uniprot.org/annotation/VAR_031779|||http://purl.uniprot.org/annotation/VAR_031780|||http://purl.uniprot.org/annotation/VAR_031781|||http://purl.uniprot.org/annotation/VAR_031782|||http://purl.uniprot.org/annotation/VAR_031783|||http://purl.uniprot.org/annotation/VAR_031784|||http://purl.uniprot.org/annotation/VAR_031785|||http://purl.uniprot.org/annotation/VSP_024572|||http://purl.uniprot.org/annotation/VSP_024573|||http://purl.uniprot.org/annotation/VSP_024574
http://togogenome.org/gene/9606:LRRC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN2|||http://purl.uniprot.org/uniprot/B3KUK5|||http://purl.uniprot.org/uniprot/B4DW88|||http://purl.uniprot.org/uniprot/Q9C0I9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076242|||http://purl.uniprot.org/annotation/VAR_051110|||http://purl.uniprot.org/annotation/VSP_017039|||http://purl.uniprot.org/annotation/VSP_017040|||http://purl.uniprot.org/annotation/VSP_017041|||http://purl.uniprot.org/annotation/VSP_017042
http://togogenome.org/gene/9606:PLGRKT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Plasminogen receptor (KT)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089695
http://togogenome.org/gene/9606:PROX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92786                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Essential for nuclear localization, interaction with RORG, repression of RORG transcriptional activator activity|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeo-Prospero|||Interaction with RORG|||Phosphoserine|||Polar residues|||Prospero|||Prospero homeobox protein 1|||Prospero-type homeo                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208880|||http://purl.uniprot.org/annotation/VAR_049362
http://togogenome.org/gene/9606:WHAMM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF30                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases nucleation-promoting factor activity and Arp2/3 complex activation.|||Disordered|||Mediates actin nucleation|||Mediates association with membranes|||Mediates interaction with microtubules|||Phosphoserine|||Polar residues|||Pro residues|||WASP homolog-associated protein with actin, membranes and microtubules|||WH2 1|||WH2 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295100|||http://purl.uniprot.org/annotation/VAR_033209|||http://purl.uniprot.org/annotation/VAR_033210|||http://purl.uniprot.org/annotation/VAR_033211|||http://purl.uniprot.org/annotation/VAR_051489|||http://purl.uniprot.org/annotation/VAR_051490|||http://purl.uniprot.org/annotation/VAR_061721
http://togogenome.org/gene/9606:BBC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PG8|||http://purl.uniprot.org/uniprot/Q9BXH1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes BLC2-binding. Impairs growth inhibitory activity. No effect on mitochondrial subcellular location.|||BH3|||Basic residues|||Bcl-2-binding component 3, isoforms 1/2|||Bcl-2-binding component 3, isoforms 3/4|||Disordered|||Impairs p53/TP53-dependent apoptosis.|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143083|||http://purl.uniprot.org/annotation/PRO_0000417572|||http://purl.uniprot.org/annotation/VSP_012238|||http://purl.uniprot.org/annotation/VSP_043781
http://togogenome.org/gene/9606:SNX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5W9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes lipid-binding.|||Disordered|||Impairs function in membrane trafficking.|||Important for membrane trafficking|||In isoform 2.|||PX|||Sorting nexin-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213856|||http://purl.uniprot.org/annotation/VSP_056594
http://togogenome.org/gene/9606:GOLGA6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDN3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 6B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332248|||http://purl.uniprot.org/annotation/VAR_042994
http://togogenome.org/gene/9606:KLHL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFZ5|||http://purl.uniprot.org/uniprot/E9PEX9|||http://purl.uniprot.org/uniprot/O95198                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119101|||http://purl.uniprot.org/annotation/VSP_042837|||http://purl.uniprot.org/annotation/VSP_047004
http://togogenome.org/gene/9606:FAM53A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JYQ7|||http://purl.uniprot.org/uniprot/Q6NSI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein FAM53A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261628
http://togogenome.org/gene/9606:ZNF808                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4W9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 808                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304991|||http://purl.uniprot.org/annotation/VAR_045823|||http://purl.uniprot.org/annotation/VAR_045824|||http://purl.uniprot.org/annotation/VSP_034946
http://togogenome.org/gene/9606:MSH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52701|||http://purl.uniprot.org/uniprot/Q3SWU9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to H3K36me3 and DNA mismatch repair activity.|||Basic and acidic residues|||DNA mismatch repair protein Msh6|||Decreased mismatch repair activity.|||Disordered|||In CRC and ENDMC; unknown pathological significance.|||In CRC and LYNCH5; decreased mismatch repair activity; loss of protein expression.|||In CRC and LYNCH5; unknown pathological significance.|||In CRC and LYNCH5; unknown pathological significance; normal mismatch repair activity.|||In CRC, breast cancer and leukemia; unknown pathological significance.|||In CRC; somatic mutation.|||In CRC; sporadic; unknown pathological significance; normal mismatch repair activity.|||In CRC; unknown pathological significance.|||In CRC; unknown pathological significance; normal mismatch repair activity.|||In CRC; unknown pathological significance; somatic mutation.|||In HNPCC; unknown pathological significance.|||In LYNCH5 and CRC; unknown pathological significance; normal mismatch repair activity.|||In LYNCH5, CRC and ENDMC; unknown pathological significance; normal mismatch repair activity.|||In LYNCH5.|||In LYNCH5; decreased mismatch repair activity; displays marked impairment of heterodimerization with MSH2.|||In LYNCH5; unknown pathological significance; no impairment of heterodimerization with MSH2; normal mismatch repair activity.|||In LYNCH5; unknown pathological significance; normal mismatch repair activity.|||In isoform 3.|||In isoform 4.|||In isoform GTBP-alt.|||In multiple colorectal adenoma.|||N6-acetyllysine|||No effect on mismatch binding, complete loss of DNA repair function when associated with MSH2 mutant R-675.|||Normal mismatch repair activity.|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115207|||http://purl.uniprot.org/annotation/VAR_004490|||http://purl.uniprot.org/annotation/VAR_004491|||http://purl.uniprot.org/annotation/VAR_004492|||http://purl.uniprot.org/annotation/VAR_012955|||http://purl.uniprot.org/annotation/VAR_012956|||http://purl.uniprot.org/annotation/VAR_012957|||http://purl.uniprot.org/annotation/VAR_012958|||http://purl.uniprot.org/annotation/VAR_012959|||http://purl.uniprot.org/annotation/VAR_012960|||http://purl.uniprot.org/annotation/VAR_012961|||http://purl.uniprot.org/annotation/VAR_012962|||http://purl.uniprot.org/annotation/VAR_012963|||http://purl.uniprot.org/annotation/VAR_012964|||http://purl.uniprot.org/annotation/VAR_012965|||http://purl.uniprot.org/annotation/VAR_012966|||http://purl.uniprot.org/annotation/VAR_014902|||http://purl.uniprot.org/annotation/VAR_029244|||http://purl.uniprot.org/annotation/VAR_038032|||http://purl.uniprot.org/annotation/VAR_038033|||http://purl.uniprot.org/annotation/VAR_038034|||http://purl.uniprot.org/annotation/VAR_038035|||http://purl.uniprot.org/annotation/VAR_038036|||http://purl.uniprot.org/annotation/VAR_038037|||http://purl.uniprot.org/annotation/VAR_038038|||http://purl.uniprot.org/annotation/VAR_038039|||http://purl.uniprot.org/annotation/VAR_038040|||http://purl.uniprot.org/annotation/VAR_038041|||http://purl.uniprot.org/annotation/VAR_042274|||http://purl.uniprot.org/annotation/VAR_042275|||http://purl.uniprot.org/annotation/VAR_043943|||http://purl.uniprot.org/annotation/VAR_043944|||http://purl.uniprot.org/annotation/VAR_043945|||http://purl.uniprot.org/annotation/VAR_043946|||http://purl.uniprot.org/annotation/VAR_043947|||http://purl.uniprot.org/annotation/VAR_043948|||http://purl.uniprot.org/annotation/VAR_043949|||http://purl.uniprot.org/annotation/VAR_043950|||http://purl.uniprot.org/annotation/VAR_043951|||http://purl.uniprot.org/annotation/VAR_043952|||http://purl.uniprot.org/annotation/VAR_043953|||http://purl.uniprot.org/annotation/VAR_043954|||http://purl.uniprot.org/annotation/VAR_043955|||http://purl.uniprot.org/annotation/VAR_043956|||http://purl.uniprot.org/annotation/VAR_043957|||http://purl.uniprot.org/annotation/VAR_043958|||http://purl.uniprot.org/annotation/VAR_043959|||http://purl.uniprot.org/annotation/VAR_043960|||http://purl.uniprot.org/annotation/VAR_043961|||http://purl.uniprot.org/annotation/VAR_043962|||http://purl.uniprot.org/annotation/VAR_043963|||http://purl.uniprot.org/annotation/VAR_043964|||http://purl.uniprot.org/annotation/VAR_043965|||http://purl.uniprot.org/annotation/VAR_043966|||http://purl.uniprot.org/annotation/VAR_043967|||http://purl.uniprot.org/annotation/VAR_043968|||http://purl.uniprot.org/annotation/VAR_043969|||http://purl.uniprot.org/annotation/VAR_043970|||http://purl.uniprot.org/annotation/VAR_043971|||http://purl.uniprot.org/annotation/VAR_043972|||http://purl.uniprot.org/annotation/VAR_043973|||http://purl.uniprot.org/annotation/VAR_043974|||http://purl.uniprot.org/annotation/VAR_067294|||http://purl.uniprot.org/annotation/VAR_067295|||http://purl.uniprot.org/annotation/VAR_067296|||http://purl.uniprot.org/annotation/VAR_067297|||http://purl.uniprot.org/annotation/VAR_067298|||http://purl.uniprot.org/annotation/VAR_067299|||http://purl.uniprot.org/annotation/VAR_068710|||http://purl.uniprot.org/annotation/VAR_068711|||http://purl.uniprot.org/annotation/VAR_068712|||http://purl.uniprot.org/annotation/VAR_076356|||http://purl.uniprot.org/annotation/VAR_076357|||http://purl.uniprot.org/annotation/VSP_003291|||http://purl.uniprot.org/annotation/VSP_003292|||http://purl.uniprot.org/annotation/VSP_054419|||http://purl.uniprot.org/annotation/VSP_055020
http://togogenome.org/gene/9606:TBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20226|||http://purl.uniprot.org/uniprot/Q32MN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||TATA-box-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153956|||http://purl.uniprot.org/annotation/VAR_016987|||http://purl.uniprot.org/annotation/VSP_045488
http://togogenome.org/gene/9606:TNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L0S7|||http://purl.uniprot.org/uniprot/B2RU35|||http://purl.uniprot.org/uniprot/B7Z6H8|||http://purl.uniprot.org/uniprot/Q0VG54|||http://purl.uniprot.org/uniprot/Q0VG55|||http://purl.uniprot.org/uniprot/Q59G71|||http://purl.uniprot.org/uniprot/Q86VB0|||http://purl.uniprot.org/uniprot/Q9HBL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with PPP1CA. Reduces interaction with DLC1. Increases phosphorylation of some Ser/Thr residues. Reduced rate of cell spreading and impaired cell polarization. Reduced phosphorylation of MYL12B.|||Basic and acidic residues|||C2 tensin-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||No effect on interaction with DLC1.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||PTB|||Phorbol-ester/DAG-type|||Phosphatase tensin-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Reduces interaction with DLC1 but does not affect interaction with PPP1CA. Impaired cell polarization. Reduced phosphorylation of MYL12B.|||Reduces interaction with DLC1.|||SH2|||Tensin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215900|||http://purl.uniprot.org/annotation/VAR_047066|||http://purl.uniprot.org/annotation/VAR_047067|||http://purl.uniprot.org/annotation/VAR_047068|||http://purl.uniprot.org/annotation/VAR_047070|||http://purl.uniprot.org/annotation/VAR_047071|||http://purl.uniprot.org/annotation/VAR_048004|||http://purl.uniprot.org/annotation/VAR_087223|||http://purl.uniprot.org/annotation/VSP_061738|||http://purl.uniprot.org/annotation/VSP_061739|||http://purl.uniprot.org/annotation/VSP_061740|||http://purl.uniprot.org/annotation/VSP_061741|||http://purl.uniprot.org/annotation/VSP_061742
http://togogenome.org/gene/9606:ECEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6F7YIA8|||http://purl.uniprot.org/uniprot/O95672                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endothelin-converting enzyme-like 1|||Helical|||Helical; Signal-anchor for type II membrane protein|||In DA5D.|||In DA5D; patients have ophthalmoplegia.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078224|||http://purl.uniprot.org/annotation/VAR_012813|||http://purl.uniprot.org/annotation/VAR_012814|||http://purl.uniprot.org/annotation/VAR_069747|||http://purl.uniprot.org/annotation/VAR_069993|||http://purl.uniprot.org/annotation/VAR_069994|||http://purl.uniprot.org/annotation/VAR_069995|||http://purl.uniprot.org/annotation/VSP_017544
http://togogenome.org/gene/9606:MAK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK28|||http://purl.uniprot.org/uniprot/F8VBW7|||http://purl.uniprot.org/uniprot/P20794                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes autophosphorylation and impairs kinase activity.|||Abolishes autophosphorylation.|||Basic and acidic residues|||Disordered|||In RP62.|||In RP62; results in a complete loss of kinase activity compared to wild-type.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MAK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086284|||http://purl.uniprot.org/annotation/VAR_042006|||http://purl.uniprot.org/annotation/VAR_042007|||http://purl.uniprot.org/annotation/VAR_042008|||http://purl.uniprot.org/annotation/VAR_042009|||http://purl.uniprot.org/annotation/VAR_042010|||http://purl.uniprot.org/annotation/VAR_053932|||http://purl.uniprot.org/annotation/VAR_066988|||http://purl.uniprot.org/annotation/VAR_066989|||http://purl.uniprot.org/annotation/VAR_066990|||http://purl.uniprot.org/annotation/VAR_066991|||http://purl.uniprot.org/annotation/VAR_066992|||http://purl.uniprot.org/annotation/VAR_066993|||http://purl.uniprot.org/annotation/VSP_042470|||http://purl.uniprot.org/annotation/VSP_042471
http://togogenome.org/gene/9606:GLYATL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZD4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Glycine N-acyltransferase-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336055
http://togogenome.org/gene/9606:RAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60671                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes association of the 9-1-1 complex with RAD17.|||Cell cycle checkpoint protein RAD1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225005|||http://purl.uniprot.org/annotation/VAR_051718|||http://purl.uniprot.org/annotation/VAR_051719|||http://purl.uniprot.org/annotation/VAR_051720|||http://purl.uniprot.org/annotation/VAR_051721|||http://purl.uniprot.org/annotation/VAR_055376|||http://purl.uniprot.org/annotation/VSP_017334|||http://purl.uniprot.org/annotation/VSP_017335|||http://purl.uniprot.org/annotation/VSP_017336
http://togogenome.org/gene/9606:SCGB1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95969                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 1D member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036379|||http://purl.uniprot.org/annotation/VAR_020254|||http://purl.uniprot.org/annotation/VAR_020255
http://togogenome.org/gene/9606:ZFYVE27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6J9|||http://purl.uniprot.org/uniprot/Q5T4F4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Alters interaction with RAB11A; when associated with A-13.|||Alters interaction with RAB11A; when associated with A-49.|||Cytoplasmic|||Disordered|||FYVE-type|||Helical|||In SPG33; no effect on its function in the regulation of ER morphology and stability, no effect on its localization to ER but according to PubMed:16826525 an aberrant subcellular localization to cell membrane seen, altered interaction with SPAST, increased susceptibility to ER stress, no effect on its interaction with REEP1, REEP5 and ATL1 and increased protein stability.|||In isoform 2, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 4 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of interaction with VAPA and loss of function in cell projections formation.|||Lumenal|||Necessary for interaction with KIF5A|||Necessary for interaction with RAB11A and function in neurite outgrowth|||Necessary for interaction with VAPA and function in cell projections formation|||Protrudin|||Sufficient for homooligomerization|||Sufficient for localization to endoplasmic reticulum tubular network and for interactions with REEP1, REEP5, ATL1, ATL2, ATL3 and SPAST                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245601|||http://purl.uniprot.org/annotation/VAR_027002|||http://purl.uniprot.org/annotation/VAR_027003|||http://purl.uniprot.org/annotation/VAR_027269|||http://purl.uniprot.org/annotation/VSP_019751|||http://purl.uniprot.org/annotation/VSP_019752|||http://purl.uniprot.org/annotation/VSP_019753|||http://purl.uniprot.org/annotation/VSP_019754|||http://purl.uniprot.org/annotation/VSP_019755|||http://purl.uniprot.org/annotation/VSP_019756|||http://purl.uniprot.org/annotation/VSP_045265|||http://purl.uniprot.org/annotation/VSP_045266|||http://purl.uniprot.org/annotation/VSP_046051
http://togogenome.org/gene/9606:TGIF2LY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox protein TGIF2LY|||Homeobox; TALE-type|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049332
http://togogenome.org/gene/9606:GNE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y223                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase|||In NM.|||In NM; decreased epimerase activity; decreased kinase activity.|||In NM; decreased epimerase activity; severely decreased kinase activity.|||In NM; decreased kinase activity; does not affect homohexamers formation.|||In NM; moderate phenotype with unusual involvement of quadriceps.|||In NM; results in decreased epimerase activity corresponding to 10-30% of wild-type activity; decreased kinase activity; impaired homohexamers formation.|||In NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity.|||In NM; results in decreased epimerase activity corresponding to 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation.|||In NM; results in decreased epimerase activity corresponding to 50% of the wild-type; severely decreased kinase activity corresponding to less than 10% of wild-type activity.|||In NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; decreased kinase activity; impaired homohexamers formation.|||In NM; results in decreased epimerase activity corresponding to less than 10% of wild-type activity; impaired homohexamers formation.|||In NM; results in decreased epimerase activity corresponding to less than 20% of wild-type activity; no effect on kinase activity; impaired homohexamers formation.|||In NM; retains 70% of wild-type epimerase activity; decreased kinase activity; does not affect homohexamers formation.|||In NM; retains 70% of wild-type epimerase; decreased kinase activity.|||In NM; retains 70-80% of wild-type epimerase activity; severely decreased kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation.|||In NM; retains 80% of wild-type epimerase activity; decreased kinase activity corresponding to 60% of wild-type; requires 2 nucleotide substitutions.|||In NM; retains 80% of wild-type epimerase activity; retains 75% of wild-type kinase activity.|||In NM; unknown pathological significance; retains 90% of wild-type epimerase activity; retains 75% of wild-type kinase activity.|||In SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac.|||In SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In sialuria.|||N-acetylmannosamine kinase|||UDP-N-acetylglucosamine 2-epimerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095716|||http://purl.uniprot.org/annotation/VAR_017945|||http://purl.uniprot.org/annotation/VAR_017946|||http://purl.uniprot.org/annotation/VAR_017947|||http://purl.uniprot.org/annotation/VAR_017948|||http://purl.uniprot.org/annotation/VAR_017949|||http://purl.uniprot.org/annotation/VAR_017950|||http://purl.uniprot.org/annotation/VAR_017951|||http://purl.uniprot.org/annotation/VAR_017952|||http://purl.uniprot.org/annotation/VAR_017953|||http://purl.uniprot.org/annotation/VAR_017954|||http://purl.uniprot.org/annotation/VAR_017955|||http://purl.uniprot.org/annotation/VAR_017956|||http://purl.uniprot.org/annotation/VAR_017957|||http://purl.uniprot.org/annotation/VAR_017958|||http://purl.uniprot.org/annotation/VAR_017959|||http://purl.uniprot.org/annotation/VAR_017960|||http://purl.uniprot.org/annotation/VAR_017961|||http://purl.uniprot.org/annotation/VAR_017962|||http://purl.uniprot.org/annotation/VAR_017963|||http://purl.uniprot.org/annotation/VAR_017964|||http://purl.uniprot.org/annotation/VAR_017965|||http://purl.uniprot.org/annotation/VAR_017966|||http://purl.uniprot.org/annotation/VAR_021771|||http://purl.uniprot.org/annotation/VAR_021772|||http://purl.uniprot.org/annotation/VAR_021773|||http://purl.uniprot.org/annotation/VAR_021774|||http://purl.uniprot.org/annotation/VAR_021775|||http://purl.uniprot.org/annotation/VAR_021776|||http://purl.uniprot.org/annotation/VAR_021777|||http://purl.uniprot.org/annotation/VAR_021778|||http://purl.uniprot.org/annotation/VAR_021779|||http://purl.uniprot.org/annotation/VAR_021780|||http://purl.uniprot.org/annotation/VAR_021781|||http://purl.uniprot.org/annotation/VAR_021782|||http://purl.uniprot.org/annotation/VAR_021783|||http://purl.uniprot.org/annotation/VAR_021784|||http://purl.uniprot.org/annotation/VAR_087335|||http://purl.uniprot.org/annotation/VAR_087336|||http://purl.uniprot.org/annotation/VSP_041027|||http://purl.uniprot.org/annotation/VSP_041028|||http://purl.uniprot.org/annotation/VSP_043474|||http://purl.uniprot.org/annotation/VSP_043975|||http://purl.uniprot.org/annotation/VSP_043976
http://togogenome.org/gene/9606:CREB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43889                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic motif|||Cleavage; by PS1|||Cyclic AMP-responsive element-binding protein 3|||Cytoplasmic|||Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 2).|||Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 2).|||Does not bind to DNA but retains its ability to interact with HCFC1. Reduces transcriptional activation of unfolded protein response elements (UPRE)-containing promoter. Colocalizes with HCFC1 in the ER membrane.|||Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 78-A--A-81 (isoform 1).|||Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 56-A-A-57 and 78-A--A-81 (isoform 1).|||Does not inhibit proteolytic cleavage and transcriptional activation.|||Does not retain HCFC1 in the cytoplasm, does not interact with HCFC1, does not activate promoter and fail to protect cells from a productive infection by HSV-1.|||HCFC1-binding-motif (HBM)|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Inhibits interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 56-A-A-57. Colocalizes with HCFC1 in the nucleus (isoform 1).|||Inhibits proteolytic cleavage and transcriptional activation.|||LXXLL motif 1|||LXXLL motif 2|||Leucine-zipper|||Lumenal|||N-linked (GlcNAc...) asparagine|||Processed cyclic AMP-responsive element-binding protein 3|||Transcription activation (acidic)|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076602|||http://purl.uniprot.org/annotation/PRO_0000296204|||http://purl.uniprot.org/annotation/VSP_059386
http://togogenome.org/gene/9606:C2orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU43                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C2orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089345
http://togogenome.org/gene/9606:DHRS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13268                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 2, mitochondrial|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054642|||http://purl.uniprot.org/annotation/VAR_035846|||http://purl.uniprot.org/annotation/VSP_038179
http://togogenome.org/gene/9606:OR5AR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVM6|||http://purl.uniprot.org/uniprot/Q8NGP9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150579|||http://purl.uniprot.org/annotation/VAR_062038
http://togogenome.org/gene/9606:NELFE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X830|||http://purl.uniprot.org/uniprot/P18615                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||30 X 2 AA approximate tandem repeats of R-[DSNE]|||4|||5; approximate|||6|||7|||8|||9|||Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-151 and Q-172.|||Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-151 and Q-374.|||Abolished poly-ADP-ribosylation by PARP1; when associated with Q-122; Q-172 and Q-374.|||Abolished poly-ADP-ribosylation by PARP1; when associated with Q-151; Q-172 and Q-374.|||Abolishes interaction with RNA but not the interaction with other proteins of the NELF complex.|||Basic and acidic residues|||Decreased phosphorylation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Mimics phosphorylation, promoting its release from chromatin.|||Negative elongation factor E|||Phosphoserine|||Phosphoserine; by CDK9|||Phosphothreonine|||Polar residues|||PolyADP-ribosyl glutamic acid|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081802|||http://purl.uniprot.org/annotation/VSP_056151|||http://purl.uniprot.org/annotation/VSP_056152
http://togogenome.org/gene/9606:DNMBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTX1|||http://purl.uniprot.org/uniprot/A0A1C7CYY6|||http://purl.uniprot.org/uniprot/B3KY33|||http://purl.uniprot.org/uniprot/Q6XZF7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BAR|||Basic and acidic residues|||DH|||Decreased interaction of SH3 domain 6 with L.monocytogenes InlC.|||Disordered|||Dynamin-binding protein|||In CTRCT48.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5|||SH3 6|||Wild-type interaction of SH3 domain 6 with L.monocytogenes InlC.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079959|||http://purl.uniprot.org/annotation/VAR_024339|||http://purl.uniprot.org/annotation/VAR_050955|||http://purl.uniprot.org/annotation/VAR_050956|||http://purl.uniprot.org/annotation/VAR_050957|||http://purl.uniprot.org/annotation/VAR_081450|||http://purl.uniprot.org/annotation/VSP_012079
http://togogenome.org/gene/9606:OTOP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3TZI1|||http://purl.uniprot.org/uniprot/Q7RTS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||Helical|||Phosphoserine|||Proton channel OTOP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313822|||http://purl.uniprot.org/annotation/VAR_037762|||http://purl.uniprot.org/annotation/VAR_037763|||http://purl.uniprot.org/annotation/VAR_037764|||http://purl.uniprot.org/annotation/VAR_062217
http://togogenome.org/gene/9606:RNF26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY78                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  About 4-fold increase of stability (from 30 min to 2 hours).|||E3 ubiquitin-protein ligase RNF26|||Helical|||RING-type|||Strongly decreased E3 ubiquitin-protein ligase activity due to impaired interaction with E2 enzymes. Impaired ability to retain vesicles in the perinuclear cloud.|||Strongly decreased E3 ubiquitin-protein ligase activity. Impaired ability to mediate ubiquitination of TMEM173/STING.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056068
http://togogenome.org/gene/9606:ZFPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW38|||http://purl.uniprot.org/uniprot/Q9NPQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||CCHC FOG-type|||CCHC FOG-type 1|||CCHC FOG-type 2|||CCHC FOG-type 3|||CCHC FOG-type 4|||CCHC FOG-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CTHM.|||In SRXY9 and TOF; reduced its ability to interact with GATA4.|||In SRXY9; results in reduced transactivation activity on the AMH promoter; abolished its ability to interact with GATA4.|||In SRXY9; results in reduced transactivation activity on the AMH promoter; does not affect its ability to interact with GATA4.|||In TOF and CTHM; does not affect its ability to interact with GATA4.|||In TOF; slightly impairs its ability to interact with GATA4.|||In isoform 2.|||Interaction with CTBP2|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Zinc finger protein ZFPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221043|||http://purl.uniprot.org/annotation/VAR_017942|||http://purl.uniprot.org/annotation/VAR_017943|||http://purl.uniprot.org/annotation/VAR_017944|||http://purl.uniprot.org/annotation/VAR_024178|||http://purl.uniprot.org/annotation/VAR_030760|||http://purl.uniprot.org/annotation/VAR_071104|||http://purl.uniprot.org/annotation/VAR_071105|||http://purl.uniprot.org/annotation/VAR_072074|||http://purl.uniprot.org/annotation/VAR_072075|||http://purl.uniprot.org/annotation/VSP_009701|||http://purl.uniprot.org/annotation/VSP_009702
http://togogenome.org/gene/9606:BTN3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K547|||http://purl.uniprot.org/uniprot/O00481                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin subfamily 3 member A1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014532|||http://purl.uniprot.org/annotation/PRO_5002722157|||http://purl.uniprot.org/annotation/VAR_021170|||http://purl.uniprot.org/annotation/VAR_028788|||http://purl.uniprot.org/annotation/VAR_061305|||http://purl.uniprot.org/annotation/VAR_061306|||http://purl.uniprot.org/annotation/VSP_012714|||http://purl.uniprot.org/annotation/VSP_012715|||http://purl.uniprot.org/annotation/VSP_042034|||http://purl.uniprot.org/annotation/VSP_045062
http://togogenome.org/gene/9606:POTEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5A3E0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Actin-like|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member F|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307859
http://togogenome.org/gene/9606:MFSD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14728                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||Major facilitator superfamily domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324658
http://togogenome.org/gene/9606:CCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48745                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CCN family member 3|||CTCK|||IGFBP N-terminal|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||TSP type-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014415|||http://purl.uniprot.org/annotation/VAR_049568|||http://purl.uniprot.org/annotation/VAR_049569
http://togogenome.org/gene/9606:GSE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14687                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Genetic suppressor element 1|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050730|||http://purl.uniprot.org/annotation/VAR_029546|||http://purl.uniprot.org/annotation/VAR_029547|||http://purl.uniprot.org/annotation/VAR_035926|||http://purl.uniprot.org/annotation/VSP_021820|||http://purl.uniprot.org/annotation/VSP_021821
http://togogenome.org/gene/9606:VASH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8A9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished tyrosine carboxypeptidase activity on alpha-tubulin.|||Abolished tyrosine carboxypeptidase activity on alpha-tubulin. Abolished tyrosine carboxypeptidase activity on alpha-tubulin; when associated with A-146.|||Abolished tyrosine carboxypeptidase activity on alpha-tubulin. Abolished tyrosine carboxypeptidase activity on alpha-tubulin; when associated with A-222.|||Almost abolished interaction with VASH1.|||Basic and acidic residues|||Cleavage|||Disappearance of 36, 32 and 27 kDa processed forms.|||Disappearance of 42 kDa processed form.|||Disordered|||In isoform 2.|||Involved in heparin-binding and antiangiogenic activity|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-194. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-203.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-194. Strognly reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-203.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-256. No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-258. No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-276.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-141. Abolished tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-77 and R-141.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-141. Abolished tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-81 and R-141.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-77. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-81. Abolished tyrosine carboxypeptidase activity on alpha-tubulin; when associated with R-77 and R-81.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin. Strongly reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-258. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-258. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-256. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-276.|||No effect on tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-194. Reduced tyrosine carboxypeptidase activity on alpha-tubulin; when associated with E-203.|||Reduced tyrosine carboxypeptidase activity on alpha-tubulin.|||Slightly reduced tyrosine carboxypeptidase activity on alpha-tubulin.|||Strongly reduced interaction with SVBP.|||Tubulinyl-Tyr carboxypeptidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189980|||http://purl.uniprot.org/annotation/VSP_013324|||http://purl.uniprot.org/annotation/VSP_013325
http://togogenome.org/gene/9606:LCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13094                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Lymphocyte cytosolic protein 2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084368|||http://purl.uniprot.org/annotation/VAR_070803
http://togogenome.org/gene/9606:SORBS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60504                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Binds to SOS|||Binds to vinculin|||Disordered|||In isoform Beta.|||Loss of SOS-binding ability.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||Removed|||SH3 1|||SH3 2|||SH3 3|||SoHo|||Vinexin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065830|||http://purl.uniprot.org/annotation/VAR_055019|||http://purl.uniprot.org/annotation/VAR_055020|||http://purl.uniprot.org/annotation/VAR_057019|||http://purl.uniprot.org/annotation/VSP_004489
http://togogenome.org/gene/9606:PRH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02810                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Decreased phosphorylation by FAM20C; when associated with A-24.|||Decreased phosphorylation by FAM20C; when associated with A-38.|||Disordered|||In allele PRH1-DB.|||In allele PRH1-PA and allele PRH1-DB.|||In allele PRH1-PA; interferes with proteolytic cleavage at Arg-122.|||In allele PRH1-PIF, allele PRH1-PA and allele PRH1-DB.|||In allele PRH2-2.|||In allele PRH2-3.|||Inhibits hydroxyapatite formation, binds to hydroxyapatite and calcium|||O-linked (GlcA) serine; alternate|||Peptide P-C|||Phosphoserine; alternate|||Phosphoserine; by FAM20C|||Phosphoserine; by FAM20C; alternate|||Polar residues|||Pro residues|||Pyrrolidone carboxylic acid|||Salivary acidic proline-rich phosphoprotein 1/2|||Salivary acidic proline-rich phosphoprotein 3/4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022137|||http://purl.uniprot.org/annotation/PRO_0000022138|||http://purl.uniprot.org/annotation/PRO_0000022139|||http://purl.uniprot.org/annotation/VAR_005563|||http://purl.uniprot.org/annotation/VAR_005564|||http://purl.uniprot.org/annotation/VAR_005565|||http://purl.uniprot.org/annotation/VAR_023240|||http://purl.uniprot.org/annotation/VAR_023241|||http://purl.uniprot.org/annotation/VAR_023242
http://togogenome.org/gene/9606:CDCA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GX58|||http://purl.uniprot.org/uniprot/F8WDL1|||http://purl.uniprot.org/uniprot/J3KMY0|||http://purl.uniprot.org/uniprot/Q99618                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Cell division cycle-associated protein 3|||Disordered|||F-box-like|||KEN box|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287708
http://togogenome.org/gene/9606:MOK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ07                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MAPK/MAK/MRK overlapping kinase|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086341|||http://purl.uniprot.org/annotation/VAR_024576|||http://purl.uniprot.org/annotation/VAR_042011|||http://purl.uniprot.org/annotation/VAR_042012|||http://purl.uniprot.org/annotation/VAR_042013|||http://purl.uniprot.org/annotation/VAR_042014|||http://purl.uniprot.org/annotation/VAR_042015|||http://purl.uniprot.org/annotation/VAR_070930|||http://purl.uniprot.org/annotation/VSP_009142|||http://purl.uniprot.org/annotation/VSP_009143|||http://purl.uniprot.org/annotation/VSP_009144|||http://purl.uniprot.org/annotation/VSP_009145|||http://purl.uniprot.org/annotation/VSP_009146|||http://purl.uniprot.org/annotation/VSP_054734|||http://purl.uniprot.org/annotation/VSP_054735
http://togogenome.org/gene/9606:TBX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRD9|||http://purl.uniprot.org/uniprot/O60806                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  In IAD.|||T-box|||T-box transcription factor TBX19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184449|||http://purl.uniprot.org/annotation/VAR_018387
http://togogenome.org/gene/9606:NETO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32NC3|||http://purl.uniprot.org/uniprot/Q8NC67                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Neuropilin and tolloid-like protein 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021801|||http://purl.uniprot.org/annotation/PRO_5004221100|||http://purl.uniprot.org/annotation/VAR_051232|||http://purl.uniprot.org/annotation/VSP_012856|||http://purl.uniprot.org/annotation/VSP_012857|||http://purl.uniprot.org/annotation/VSP_053795
http://togogenome.org/gene/9606:DLL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DSL|||Delta-like protein 3|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Helical|||In SCDO1.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007509|||http://purl.uniprot.org/annotation/VAR_009952|||http://purl.uniprot.org/annotation/VAR_016776|||http://purl.uniprot.org/annotation/VAR_046782|||http://purl.uniprot.org/annotation/VAR_046783|||http://purl.uniprot.org/annotation/VAR_046784|||http://purl.uniprot.org/annotation/VSP_045249
http://togogenome.org/gene/9606:IL17RC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAC3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 4, isoform 6 and isoform 8.|||In isoform 4.|||In isoform 5, isoform 7 and isoform 8.|||In isoform 6 and isoform 7.|||Interleukin-17 receptor C|||N-linked (GlcNAc...) asparagine|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011034|||http://purl.uniprot.org/annotation/VAR_022680|||http://purl.uniprot.org/annotation/VSP_014138|||http://purl.uniprot.org/annotation/VSP_014139|||http://purl.uniprot.org/annotation/VSP_014140|||http://purl.uniprot.org/annotation/VSP_014141|||http://purl.uniprot.org/annotation/VSP_047291|||http://purl.uniprot.org/annotation/VSP_047292
http://togogenome.org/gene/9606:LRRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYS8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084491|||http://purl.uniprot.org/annotation/VAR_051140|||http://purl.uniprot.org/annotation/VAR_051141|||http://purl.uniprot.org/annotation/VAR_051142
http://togogenome.org/gene/9606:TCERG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14776                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||FF 1|||FF 2|||FF 3|||FF 4|||FF 5|||FF 6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150.|||No effect.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448.|||Transcription elongation regulator 1|||WW 1|||WW 2|||WW 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076063|||http://purl.uniprot.org/annotation/VSP_026933
http://togogenome.org/gene/9606:REXO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exonuclease|||In isoform 2.|||RNA exonuclease 5|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287345|||http://purl.uniprot.org/annotation/VSP_025443
http://togogenome.org/gene/9606:AMHR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16671                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Anti-Muellerian hormone type-2 receptor|||Cytoplasmic|||Extracellular|||Helical|||In PMDS2.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024408|||http://purl.uniprot.org/annotation/VAR_015525|||http://purl.uniprot.org/annotation/VAR_015526|||http://purl.uniprot.org/annotation/VAR_015527|||http://purl.uniprot.org/annotation/VAR_015528|||http://purl.uniprot.org/annotation/VAR_015529|||http://purl.uniprot.org/annotation/VAR_015530|||http://purl.uniprot.org/annotation/VAR_015531|||http://purl.uniprot.org/annotation/VAR_015532|||http://purl.uniprot.org/annotation/VAR_031057|||http://purl.uniprot.org/annotation/VAR_069048|||http://purl.uniprot.org/annotation/VSP_044548|||http://purl.uniprot.org/annotation/VSP_045281
http://togogenome.org/gene/9606:ILF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12906                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||DRBM 1|||DRBM 2|||DZF|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 5.|||Interaction with PRMT1|||Interleukin enhancer-binding factor 3|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKR|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126070|||http://purl.uniprot.org/annotation/VAR_022159|||http://purl.uniprot.org/annotation/VAR_048906|||http://purl.uniprot.org/annotation/VSP_003883|||http://purl.uniprot.org/annotation/VSP_003884|||http://purl.uniprot.org/annotation/VSP_003885|||http://purl.uniprot.org/annotation/VSP_003886|||http://purl.uniprot.org/annotation/VSP_003887|||http://purl.uniprot.org/annotation/VSP_003888|||http://purl.uniprot.org/annotation/VSP_003889|||http://purl.uniprot.org/annotation/VSP_003890|||http://purl.uniprot.org/annotation/VSP_003891
http://togogenome.org/gene/9606:EIF2B5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13144                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In VWM5.|||In VWM5; Cree leukoencephalopathy type.|||In VWM5; with ovarian failure.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine|||Removed|||Translation initiation factor eIF-2B subunit epsilon|||W2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156073|||http://purl.uniprot.org/annotation/VAR_012291|||http://purl.uniprot.org/annotation/VAR_012292|||http://purl.uniprot.org/annotation/VAR_012293|||http://purl.uniprot.org/annotation/VAR_012294|||http://purl.uniprot.org/annotation/VAR_012323|||http://purl.uniprot.org/annotation/VAR_012324|||http://purl.uniprot.org/annotation/VAR_012325|||http://purl.uniprot.org/annotation/VAR_012326|||http://purl.uniprot.org/annotation/VAR_012327|||http://purl.uniprot.org/annotation/VAR_012328|||http://purl.uniprot.org/annotation/VAR_012329|||http://purl.uniprot.org/annotation/VAR_012330|||http://purl.uniprot.org/annotation/VAR_012331|||http://purl.uniprot.org/annotation/VAR_012332|||http://purl.uniprot.org/annotation/VAR_012333|||http://purl.uniprot.org/annotation/VAR_016845|||http://purl.uniprot.org/annotation/VAR_016846|||http://purl.uniprot.org/annotation/VAR_048919|||http://purl.uniprot.org/annotation/VAR_068457|||http://purl.uniprot.org/annotation/VAR_068458|||http://purl.uniprot.org/annotation/VAR_068459|||http://purl.uniprot.org/annotation/VAR_068460|||http://purl.uniprot.org/annotation/VAR_068461|||http://purl.uniprot.org/annotation/VAR_068462|||http://purl.uniprot.org/annotation/VAR_068463|||http://purl.uniprot.org/annotation/VAR_068464|||http://purl.uniprot.org/annotation/VAR_068465|||http://purl.uniprot.org/annotation/VAR_068466|||http://purl.uniprot.org/annotation/VAR_068467|||http://purl.uniprot.org/annotation/VAR_068468|||http://purl.uniprot.org/annotation/VAR_068469
http://togogenome.org/gene/9606:ZNF461                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRP8|||http://purl.uniprot.org/uniprot/Q8TAF7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 461                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047196|||http://purl.uniprot.org/annotation/VAR_052834|||http://purl.uniprot.org/annotation/VSP_011396
http://togogenome.org/gene/9606:GRSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12849                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  G-rich sequence factor 1|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-255; A-259; A-320; A-406 and A-410.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-255; A-259; A-320; A-406 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-255; A-259; A-320; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-255; A-259; A-406; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-255; A-320; A-406; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-223; A-259; A-320; A-406; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-159; A-255; A-259; A-320; A-406; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-155; A-223; A-255; A-259; A-320; A-406; A-410 and A-470.|||Impairs RNA-binding and melting of G-quadruplex RNA structures; when associated with A-159; A-223; A-255; A-259; A-320; A-406; A-410 and A-470.|||In isoform 2.|||Mitochondrion|||Phosphoserine|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081597|||http://purl.uniprot.org/annotation/VAR_047537|||http://purl.uniprot.org/annotation/VSP_043118
http://togogenome.org/gene/9606:PALLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RTX2|||http://purl.uniprot.org/uniprot/Q8WX93                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2, isoform 5, isoform 8 and isoform 9.|||In isoform 2.|||In isoform 3 and isoform 8.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||In isoform 9.|||Interaction with ACTN|||Interaction with EPS8|||Interaction with EZR|||Interaction with LASP1|||Interaction with SORBS2, SPIN90 and SRC|||Interaction with SORBS2, SPIN90, SRC and PFN1|||Interaction with VASP|||Palladin|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302720|||http://purl.uniprot.org/annotation/VAR_034940|||http://purl.uniprot.org/annotation/VAR_059401|||http://purl.uniprot.org/annotation/VSP_027925|||http://purl.uniprot.org/annotation/VSP_027926|||http://purl.uniprot.org/annotation/VSP_027927|||http://purl.uniprot.org/annotation/VSP_027928|||http://purl.uniprot.org/annotation/VSP_027929|||http://purl.uniprot.org/annotation/VSP_027930|||http://purl.uniprot.org/annotation/VSP_043794|||http://purl.uniprot.org/annotation/VSP_043795
http://togogenome.org/gene/9606:LDHC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA7|||http://purl.uniprot.org/uniprot/P07864                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  L-lactate dehydrogenase C chain|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168479|||http://purl.uniprot.org/annotation/VAR_034068
http://togogenome.org/gene/9606:FLRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43155                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane protein FLRT2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021279|||http://purl.uniprot.org/annotation/VAR_050996
http://togogenome.org/gene/9606:CRPPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM1|||http://purl.uniprot.org/uniprot/A4D126                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  D-ribitol-5-phosphate cytidylyltransferase|||D-ribitol-5-phosphate cytidylyltransferase C-terminal|||Disordered|||In MDDGA7.|||In MDDGA7; also found in a patient with an atypical phenotype presenting with limb-girdle muscular dystrophy, ocular features and cerebellar involvement.|||In MDDGC7.|||In MDDGC7; atypical form presenting with congenital muscular dystrophy.|||In MDDGC7; atypical form with learning difficulties.|||In MDDGC7; decreased alpha-dystroglycan glycosylation.|||In isoform 2.|||Positions substrate for the nucleophilic attack|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343697|||http://purl.uniprot.org/annotation/VAR_068101|||http://purl.uniprot.org/annotation/VAR_068102|||http://purl.uniprot.org/annotation/VAR_068103|||http://purl.uniprot.org/annotation/VAR_069740|||http://purl.uniprot.org/annotation/VAR_069741|||http://purl.uniprot.org/annotation/VAR_069742|||http://purl.uniprot.org/annotation/VAR_069743|||http://purl.uniprot.org/annotation/VAR_069744|||http://purl.uniprot.org/annotation/VAR_071955|||http://purl.uniprot.org/annotation/VAR_071956|||http://purl.uniprot.org/annotation/VAR_078948|||http://purl.uniprot.org/annotation/VAR_078949|||http://purl.uniprot.org/annotation/VAR_078950|||http://purl.uniprot.org/annotation/VAR_078951|||http://purl.uniprot.org/annotation/VAR_078952|||http://purl.uniprot.org/annotation/VAR_078970|||http://purl.uniprot.org/annotation/VSP_044044
http://togogenome.org/gene/9606:SERPING1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL26|||http://purl.uniprot.org/uniprot/P05155                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 4 AA tandem repeats of [QE]-P-T-[TQ]|||Disordered|||In HAE1.|||In HAE1; phenotype consistent with hereditary angioedema type 1.|||In HAE1; phenotype consistent with hereditary angioedema type 2.|||In HAE1; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; in variant TA|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Plasma protease C1 inhibitor|||Polar residues|||Reactive bond|||Reactive bond for chymotrypsin|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032514|||http://purl.uniprot.org/annotation/PRO_5014303310|||http://purl.uniprot.org/annotation/VAR_007012|||http://purl.uniprot.org/annotation/VAR_007013|||http://purl.uniprot.org/annotation/VAR_007014|||http://purl.uniprot.org/annotation/VAR_007015|||http://purl.uniprot.org/annotation/VAR_007016|||http://purl.uniprot.org/annotation/VAR_007017|||http://purl.uniprot.org/annotation/VAR_007018|||http://purl.uniprot.org/annotation/VAR_007019|||http://purl.uniprot.org/annotation/VAR_007020|||http://purl.uniprot.org/annotation/VAR_007021|||http://purl.uniprot.org/annotation/VAR_007022|||http://purl.uniprot.org/annotation/VAR_007023|||http://purl.uniprot.org/annotation/VAR_007024|||http://purl.uniprot.org/annotation/VAR_007025|||http://purl.uniprot.org/annotation/VAR_007026|||http://purl.uniprot.org/annotation/VAR_007027|||http://purl.uniprot.org/annotation/VAR_007028|||http://purl.uniprot.org/annotation/VAR_007029|||http://purl.uniprot.org/annotation/VAR_007030|||http://purl.uniprot.org/annotation/VAR_007031|||http://purl.uniprot.org/annotation/VAR_011751|||http://purl.uniprot.org/annotation/VAR_027374|||http://purl.uniprot.org/annotation/VAR_027375|||http://purl.uniprot.org/annotation/VAR_027376|||http://purl.uniprot.org/annotation/VAR_027379|||http://purl.uniprot.org/annotation/VAR_027380|||http://purl.uniprot.org/annotation/VAR_027381|||http://purl.uniprot.org/annotation/VAR_027382|||http://purl.uniprot.org/annotation/VAR_027383|||http://purl.uniprot.org/annotation/VAR_027384|||http://purl.uniprot.org/annotation/VAR_046202|||http://purl.uniprot.org/annotation/VAR_068832|||http://purl.uniprot.org/annotation/VAR_068833|||http://purl.uniprot.org/annotation/VAR_068834|||http://purl.uniprot.org/annotation/VAR_068835|||http://purl.uniprot.org/annotation/VAR_068836|||http://purl.uniprot.org/annotation/VAR_068837|||http://purl.uniprot.org/annotation/VAR_068838|||http://purl.uniprot.org/annotation/VAR_068839|||http://purl.uniprot.org/annotation/VAR_068840|||http://purl.uniprot.org/annotation/VAR_068841|||http://purl.uniprot.org/annotation/VAR_068842|||http://purl.uniprot.org/annotation/VAR_068843|||http://purl.uniprot.org/annotation/VAR_068844|||http://purl.uniprot.org/annotation/VAR_071701|||http://purl.uniprot.org/annotation/VAR_071702|||http://purl.uniprot.org/annotation/VAR_071703|||http://purl.uniprot.org/annotation/VAR_071704|||http://purl.uniprot.org/annotation/VSP_056662|||http://purl.uniprot.org/annotation/VSP_056663
http://togogenome.org/gene/9606:PDE1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS69|||http://purl.uniprot.org/uniprot/Q14123                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C|||In DFNA74; increased 3',5'-cyclic-AMP phosphodiesterase activity; increased 3',5'-cyclic-GMP phosphodiesterase activity; approximately 10-fold increase in 3',5'-cyclic-AMP and 3-fold for 3',5'-cyclic-GMP compared to wild-type.|||In isoform 3.|||In isoform PDE1C1.|||N-acetylmethionine|||PDEase|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198792|||http://purl.uniprot.org/annotation/VAR_081215|||http://purl.uniprot.org/annotation/VSP_004552|||http://purl.uniprot.org/annotation/VSP_004553|||http://purl.uniprot.org/annotation/VSP_044468
http://togogenome.org/gene/9606:PON3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15166                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Not cleaved|||Phosphoserine|||Proton acceptor|||Serum paraoxonase/lactonase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223290|||http://purl.uniprot.org/annotation/VAR_021082|||http://purl.uniprot.org/annotation/VAR_021083
http://togogenome.org/gene/9606:CHKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y259                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Choline/ethanolamine kinase|||In MDCMC.|||In MDCMC; decreased choline kinase activity.|||In MDCMC; loss of choline kinase activity; decreased amount of phosphatidylcholine in patients cells.|||In MDCMC; severely decreased choline kinase activity.|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206222|||http://purl.uniprot.org/annotation/VAR_081791|||http://purl.uniprot.org/annotation/VAR_081792|||http://purl.uniprot.org/annotation/VAR_081793|||http://purl.uniprot.org/annotation/VAR_081794|||http://purl.uniprot.org/annotation/VAR_081795|||http://purl.uniprot.org/annotation/VAR_081796|||http://purl.uniprot.org/annotation/VAR_081797|||http://purl.uniprot.org/annotation/VAR_081798|||http://purl.uniprot.org/annotation/VAR_081799|||http://purl.uniprot.org/annotation/VAR_081800|||http://purl.uniprot.org/annotation/VAR_081801|||http://purl.uniprot.org/annotation/VSP_034248|||http://purl.uniprot.org/annotation/VSP_034249
http://togogenome.org/gene/9606:TMPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E972|||http://purl.uniprot.org/uniprot/P42166|||http://purl.uniprot.org/uniprot/P42167|||http://purl.uniprot.org/uniprot/Q59G12                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Peptide|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Peptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects the interaction with LMNA.|||Basic and acidic residues|||Binds lamins B|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform Gamma.|||In isoform Zeta.|||LEM|||LEM-like|||Lamina-associated polypeptide 2, isoform alpha|||Lamina-associated polypeptide 2, isoforms beta/gamma|||Linker|||Lumenal|||N6-acetyllysine|||NAKAP95-binding C|||NAKAP95-binding N|||Nuclear localization signal|||Nucleoplasmic|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Thymopentin|||Thymopoietin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017674|||http://purl.uniprot.org/annotation/PRO_0000017675|||http://purl.uniprot.org/annotation/PRO_0000017676|||http://purl.uniprot.org/annotation/PRO_0000017677|||http://purl.uniprot.org/annotation/PRO_0000017678|||http://purl.uniprot.org/annotation/PRO_0000045841|||http://purl.uniprot.org/annotation/VAR_005635|||http://purl.uniprot.org/annotation/VAR_014786|||http://purl.uniprot.org/annotation/VAR_049773|||http://purl.uniprot.org/annotation/VAR_049774|||http://purl.uniprot.org/annotation/VAR_049775|||http://purl.uniprot.org/annotation/VAR_049776|||http://purl.uniprot.org/annotation/VAR_049777|||http://purl.uniprot.org/annotation/VAR_049778|||http://purl.uniprot.org/annotation/VAR_049779|||http://purl.uniprot.org/annotation/VSP_004456|||http://purl.uniprot.org/annotation/VSP_056162|||http://purl.uniprot.org/annotation/VSP_056163
http://togogenome.org/gene/9606:DPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5QL29|||http://purl.uniprot.org/uniprot/C8C3P2|||http://purl.uniprot.org/uniprot/E9PDV3|||http://purl.uniprot.org/uniprot/Q6PJ73|||http://purl.uniprot.org/uniprot/Q92782                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 3.|||PHD-type|||PHD-type 1|||PHD-type 2|||Zinc finger protein neuro-d4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168145|||http://purl.uniprot.org/annotation/VSP_061234|||http://purl.uniprot.org/annotation/VSP_061235|||http://purl.uniprot.org/annotation/VSP_061236
http://togogenome.org/gene/9606:RSPH6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0K4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Polar residues|||Radial spoke head protein 6 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312760|||http://purl.uniprot.org/annotation/VAR_037560
http://togogenome.org/gene/9606:RGS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49798                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||RGS|||Regulator of G-protein signaling 4|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204185|||http://purl.uniprot.org/annotation/VAR_051795|||http://purl.uniprot.org/annotation/VSP_043853|||http://purl.uniprot.org/annotation/VSP_043854|||http://purl.uniprot.org/annotation/VSP_043855|||http://purl.uniprot.org/annotation/VSP_043856
http://togogenome.org/gene/9606:MRPL48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GC5                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein mL48|||Mitochondrion|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261657|||http://purl.uniprot.org/annotation/VAR_029473|||http://purl.uniprot.org/annotation/VSP_054130
http://togogenome.org/gene/9606:ARHGEF16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTS4|||http://purl.uniprot.org/uniprot/Q5VV41                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DH|||Disordered|||In isoform 2.|||N-acetylalanine|||PDZ-binding motif|||PH|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed|||Required for RHOG activation and mediates interaction with EPHA2|||Rho guanine nucleotide exchange factor 16|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233690|||http://purl.uniprot.org/annotation/VAR_059796|||http://purl.uniprot.org/annotation/VAR_059797|||http://purl.uniprot.org/annotation/VAR_061796|||http://purl.uniprot.org/annotation/VAR_083184|||http://purl.uniprot.org/annotation/VSP_018149
http://togogenome.org/gene/9606:HEATR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RTY3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||Protein HEATR9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287176|||http://purl.uniprot.org/annotation/VAR_032281|||http://purl.uniprot.org/annotation/VAR_035685|||http://purl.uniprot.org/annotation/VSP_025349|||http://purl.uniprot.org/annotation/VSP_025350|||http://purl.uniprot.org/annotation/VSP_036493|||http://purl.uniprot.org/annotation/VSP_036494|||http://purl.uniprot.org/annotation/VSP_036495|||http://purl.uniprot.org/annotation/VSP_036496
http://togogenome.org/gene/9606:RPL37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61927                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Large ribosomal subunit protein eL37|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139705
http://togogenome.org/gene/9606:CYLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQC7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished K63-deubiquitinase activity; decreased inhibition of NF-kappa-B; no impact on interaction with TBK1, OPTN and SQSTM.|||Abolishes binding to TRAF2.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-439 and E-441.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-439 and E-444.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-441 and E-444.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-439; E-441 and E-444.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-436; E-439; E-441 and E-444.|||Abolishes deubiquitination of TRAF2; when associated with E-418; E-432; E-436; E-439; E-441 and E-444.|||Abolishes deubiquitination of TRAF2; when associated with E-422; E-432; E-436; E-439; E-441 and E-444.|||B-box|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly 3|||Disordered|||Impaired interaction with SPATA2.|||In FTDALS8; increased K63-deubiquitinase activity; increased inhibition of NF-kappa-B; no impact on interaction with TBK1, OPTN and SQSTM.|||In FTDALS8; unknown pathological significance.|||In MFT1 and BRSS.|||In isoform 2.|||Interaction with IKBKG/NEMO|||Interaction with TRAF2|||Interaction with TRIP|||Loss of deubiquitinating activity.|||Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-439 and A-441.|||Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-439 and A-444.|||Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-441 and A-444.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||Reduced phosphorylation; when associated with A-418; A-432 and A-436. Loss of phosphorylation; when associated with A-418; A-432; A-436; A-439; A-441 and A-444.|||Reduced phosphorylation; when associated with A-422; A-432 and A-436. Loss of phosphorylation; when associated with A-422; A-432; A-436; A-439; A-441 and A-444.|||Slightly reduced phosphorylation; when associated with A-432. Reduced phosphorylation; when associated with A-418; A-422 and A-432. Loss of phosphorylation; when associated with A-418; A-422; A-432; A-439; A-441 and A-444.|||Slightly reduced phosphorylation; when associated with A-436. Reduced phosphorylation; when associated with A-418; A-422 and A-436. Loss of phosphorylation; when associated with A-418; A-422; A-436; A-439; A-441 and A-444.|||USP|||Ubiquitin carboxyl-terminal hydrolase CYLD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080698|||http://purl.uniprot.org/annotation/VAR_045967|||http://purl.uniprot.org/annotation/VAR_085113|||http://purl.uniprot.org/annotation/VAR_085114|||http://purl.uniprot.org/annotation/VAR_085115|||http://purl.uniprot.org/annotation/VAR_085116|||http://purl.uniprot.org/annotation/VSP_011277
http://togogenome.org/gene/9606:ASPHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U4P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aspartate beta-hydroxylase domain-containing protein 1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254595
http://togogenome.org/gene/9606:MUSK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSY1|||http://purl.uniprot.org/uniprot/O15146                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FZ|||Helical|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||In CMS9.|||In CMS9; affects interaction with DOK7 and impairs MUSK phosphorylation; altered AChR clustering.|||In CMS9; does not affect catalytic kinase activity; reduces protein expression and stability.|||In CMS9; reduces AChR aggregation in developing neuromuscular junction.|||In FADS1; reduces agrin-dependent AChR aggregation and tyrosine kinase activity in developing neuromuscular junction.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||Mild decrease in kinase activity.|||Muscle, skeletal receptor tyrosine-protein kinase|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CK2|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Severe loss of kinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024446|||http://purl.uniprot.org/annotation/VAR_021930|||http://purl.uniprot.org/annotation/VAR_023046|||http://purl.uniprot.org/annotation/VAR_033837|||http://purl.uniprot.org/annotation/VAR_041748|||http://purl.uniprot.org/annotation/VAR_041749|||http://purl.uniprot.org/annotation/VAR_041750|||http://purl.uniprot.org/annotation/VAR_041751|||http://purl.uniprot.org/annotation/VAR_041752|||http://purl.uniprot.org/annotation/VAR_041753|||http://purl.uniprot.org/annotation/VAR_041754|||http://purl.uniprot.org/annotation/VAR_041755|||http://purl.uniprot.org/annotation/VAR_041756|||http://purl.uniprot.org/annotation/VAR_041757|||http://purl.uniprot.org/annotation/VAR_041758|||http://purl.uniprot.org/annotation/VAR_041759|||http://purl.uniprot.org/annotation/VAR_066604|||http://purl.uniprot.org/annotation/VAR_066605|||http://purl.uniprot.org/annotation/VAR_072785|||http://purl.uniprot.org/annotation/VAR_072786|||http://purl.uniprot.org/annotation/VAR_072787|||http://purl.uniprot.org/annotation/VAR_072788|||http://purl.uniprot.org/annotation/VSP_035958|||http://purl.uniprot.org/annotation/VSP_035959|||http://purl.uniprot.org/annotation/VSP_035960
http://togogenome.org/gene/9606:WDFY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWB7|||http://purl.uniprot.org/uniprot/Q9H8N9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Zinc Finger                                                                                  ^@                                                                                  FYVE-type|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat and FYVE domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051335
http://togogenome.org/gene/9606:FOXQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C009                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein Q1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091890|||http://purl.uniprot.org/annotation/VAR_031606|||http://purl.uniprot.org/annotation/VAR_031607
http://togogenome.org/gene/9606:TXNRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2S5|||http://purl.uniprot.org/uniprot/Q16881                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteinyl-selenocysteine (Cys-Sec)|||Disordered|||FAD/NAD(P)-binding|||Glutaredoxin|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-acetylmethionine|||N6-succinyllysine|||Phosphotyrosine|||Proton acceptor|||Pyridine nucleotide-disulphide oxidoreductase dimerisation|||Redox-active|||Required for interaction with ESR1 and ESR2|||Selenocysteine|||Thioredoxin reductase 1, cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030286|||http://purl.uniprot.org/annotation/VAR_051776|||http://purl.uniprot.org/annotation/VSP_031558|||http://purl.uniprot.org/annotation/VSP_031559|||http://purl.uniprot.org/annotation/VSP_031560|||http://purl.uniprot.org/annotation/VSP_031561|||http://purl.uniprot.org/annotation/VSP_031562|||http://purl.uniprot.org/annotation/VSP_031563|||http://purl.uniprot.org/annotation/VSP_031564|||http://purl.uniprot.org/annotation/VSP_031565|||http://purl.uniprot.org/annotation/VSP_053819
http://togogenome.org/gene/9606:NPRL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTW4                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolished GTPase activating protein activity toward RagA/RRAGA.|||Arginine finger|||Decreased ubiquitination by the GATOR2 complex.|||Does not affect the GTPase activating protein activity of the GATOR1 complex.|||Does not affect ubiquitination by the GATOR2 complex.|||GATOR1 complex protein NPRL2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In FFEVF2.|||In FFEVF2; unknown pathological significance.|||In RL1 mutant; abolished ability of the GATOR1 complex to inhibit mTORC1 signaling.|||In RL2 mutant; does not affect ability of the GATOR1 complex to inhibit mTORC1 signaling.|||In isoform 2.|||Interaction with PDPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213319|||http://purl.uniprot.org/annotation/VAR_077122|||http://purl.uniprot.org/annotation/VAR_077123|||http://purl.uniprot.org/annotation/VAR_077124|||http://purl.uniprot.org/annotation/VAR_077125|||http://purl.uniprot.org/annotation/VSP_010329|||http://purl.uniprot.org/annotation/VSP_010330|||http://purl.uniprot.org/annotation/VSP_010331
http://togogenome.org/gene/9606:UHMK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAS1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Loss of kinase activity.|||Protein kinase|||Proton acceptor|||RRM|||Serine/threonine-protein kinase Kist                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086777|||http://purl.uniprot.org/annotation/VAR_041272|||http://purl.uniprot.org/annotation/VAR_041273|||http://purl.uniprot.org/annotation/VSP_004908|||http://purl.uniprot.org/annotation/VSP_004909|||http://purl.uniprot.org/annotation/VSP_046145
http://togogenome.org/gene/9606:SLC17A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00624                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sodium-dependent phosphate transport protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220940|||http://purl.uniprot.org/annotation/VSP_020638|||http://purl.uniprot.org/annotation/VSP_054712
http://togogenome.org/gene/9606:CDK13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14004                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 13|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CHDFIDD.|||In RNA edited version.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085711|||http://purl.uniprot.org/annotation/VAR_022381|||http://purl.uniprot.org/annotation/VAR_022382|||http://purl.uniprot.org/annotation/VAR_022383|||http://purl.uniprot.org/annotation/VAR_022384|||http://purl.uniprot.org/annotation/VAR_022385|||http://purl.uniprot.org/annotation/VAR_022386|||http://purl.uniprot.org/annotation/VAR_022387|||http://purl.uniprot.org/annotation/VAR_041965|||http://purl.uniprot.org/annotation/VAR_041966|||http://purl.uniprot.org/annotation/VAR_041967|||http://purl.uniprot.org/annotation/VAR_053926|||http://purl.uniprot.org/annotation/VAR_066526|||http://purl.uniprot.org/annotation/VAR_078598|||http://purl.uniprot.org/annotation/VAR_078599|||http://purl.uniprot.org/annotation/VAR_078600|||http://purl.uniprot.org/annotation/VAR_078601|||http://purl.uniprot.org/annotation/VAR_079422|||http://purl.uniprot.org/annotation/VAR_079423|||http://purl.uniprot.org/annotation/VSP_013579
http://togogenome.org/gene/9606:DGKD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16760                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  DAGKc|||Decreased interaction with AP2A2.|||Decreased interaction with AP2A2; when associated with A-369.|||Decreased interaction with AP2A2; when associated with A-372.|||Diacylglycerol kinase delta|||Disordered|||In isoform 1.|||Loss of homooligomerization.|||PH|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Pro residues|||Regulates association with membranes|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218462|||http://purl.uniprot.org/annotation/VSP_012891
http://togogenome.org/gene/9606:JUP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z487|||http://purl.uniprot.org/uniprot/P14923                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Abolishes glycosylation. Does not affect binding to CDH1, DSC1 or DSG1.|||Does not affect glycosylation.|||In ARVD12; affects the structure and distribution of mechanical and electrical cell junctions.|||In ARVD12; unknown pathological significance.|||Interaction with DSC1|||Interaction with DSC1 and DSG1|||Junction plakoglobin|||N-acetylmethionine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Reduces glycosylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064278|||http://purl.uniprot.org/annotation/VAR_037803|||http://purl.uniprot.org/annotation/VAR_037804|||http://purl.uniprot.org/annotation/VAR_065698|||http://purl.uniprot.org/annotation/VAR_065699|||http://purl.uniprot.org/annotation/VAR_065700
http://togogenome.org/gene/9606:ERVV-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6SEH9|||http://purl.uniprot.org/uniprot/M9QSX5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endogenous retrovirus group V member 2 Env polyprotein|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411001|||http://purl.uniprot.org/annotation/PRO_5004102019
http://togogenome.org/gene/9606:PKD2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1L4F0|||http://purl.uniprot.org/uniprot/Q9P0L9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-728 and A-731.|||Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-728 and A-735.|||Abolishes homooligomer formation; when associated with A-710; A-714; A-717; A-731 and A-735.|||Abolishes homooligomer formation; when associated with A-710; A-714; A-728; A-731 and A-735.|||Abolishes homooligomer formation; when associated with A-710; A-717; A-728; A-731 and A-735.|||Abolishes homooligomer formation; when associated with A-714; A-717; A-728; A-731 and A-735.|||Abolishes ion channel activity.|||Basic and acidic residues|||Cytoplasmic|||Decreased channel activity.|||Disordered|||Does not affect ion channel activity.|||EF-hand|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increased channel activity.|||Increased permeability of dimethylamine and trimethylamine and decreased permeability of magnesium.|||Loss of channel activity.|||Loss of channel activity. No effect on expression at the cell membrane.|||Loss of phosphatidylinositol-4,5-bisphosphate binding.|||Mildly increased channel activity.|||N-linked (GlcNAc...) asparagine|||No effect on channel activity.|||No effect on channel activity. No effect on expression at the cell membrane.|||Polycystin|||Polycystin cation channel PKD1/PKD2|||Polycystin-2-like protein 1|||Pore-forming|||Required for homooligomerization|||S-palmitoyl cysteine|||Strongly decreased channel activity. No effect on expression at the cell membrane. Loss of palmitoylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164360|||http://purl.uniprot.org/annotation/VAR_024569|||http://purl.uniprot.org/annotation/VAR_024570|||http://purl.uniprot.org/annotation/VAR_050555|||http://purl.uniprot.org/annotation/VAR_050556|||http://purl.uniprot.org/annotation/VAR_050557|||http://purl.uniprot.org/annotation/VSP_004728|||http://purl.uniprot.org/annotation/VSP_004729|||http://purl.uniprot.org/annotation/VSP_004730|||http://purl.uniprot.org/annotation/VSP_004731|||http://purl.uniprot.org/annotation/VSP_053718
http://togogenome.org/gene/9606:LIMS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW19|||http://purl.uniprot.org/uniprot/P0CW20                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LIM and senescent cell antigen-like-containing domain protein 3|||LIM and senescent cell antigen-like-containing domain protein 4|||LIM zinc-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266013|||http://purl.uniprot.org/annotation/PRO_0000409553|||http://purl.uniprot.org/annotation/VSP_054392
http://togogenome.org/gene/9606:MRPS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82914                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||Small ribosomal subunit protein uS15m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030614
http://togogenome.org/gene/9606:LRCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2L9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat and calponin homology domain-containing protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084478|||http://purl.uniprot.org/annotation/VAR_051133|||http://purl.uniprot.org/annotation/VAR_051134|||http://purl.uniprot.org/annotation/VSP_010635|||http://purl.uniprot.org/annotation/VSP_010636|||http://purl.uniprot.org/annotation/VSP_044474
http://togogenome.org/gene/9606:SSNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43805                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Does not affect oligomer formation; when associated with S-18 and S-23.|||Does not affect oligomer formation; when associated with S-18 and S-30.|||Does not affect oligomer formation; when associated with S-23 and S-30.|||Important for localization to the centrosome|||In a breast cancer sample; somatic mutation.|||Microtubule nucleation factor SSNA1|||N-acetylthreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114483|||http://purl.uniprot.org/annotation/VAR_036343
http://togogenome.org/gene/9606:PTGDR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13258                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prostaglandin D2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070047|||http://purl.uniprot.org/annotation/VAR_033482|||http://purl.uniprot.org/annotation/VAR_033483|||http://purl.uniprot.org/annotation/VAR_054975|||http://purl.uniprot.org/annotation/VAR_054976|||http://purl.uniprot.org/annotation/VSP_055141|||http://purl.uniprot.org/annotation/VSP_055142
http://togogenome.org/gene/9606:APOBEC3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2CML4                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent                                                                                  ^@                                                                                  CMP/dCMP-type deaminase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:FOXA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55318                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fork-head|||Hepatocyte nuclear factor 3-gamma|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091800|||http://purl.uniprot.org/annotation/VAR_008859
http://togogenome.org/gene/9606:GARIN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEG0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Golgi-associated RAB2 interactor protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266044|||http://purl.uniprot.org/annotation/VAR_029638|||http://purl.uniprot.org/annotation/VAR_029639
http://togogenome.org/gene/9606:IFNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05014                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In alpha-4B.|||Interferon alpha-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016361|||http://purl.uniprot.org/annotation/VAR_013002|||http://purl.uniprot.org/annotation/VAR_013003|||http://purl.uniprot.org/annotation/VAR_034010
http://togogenome.org/gene/9606:KRTAP12-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60329                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 5 AA approximate repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 12-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185199
http://togogenome.org/gene/9606:PNMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11086                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  No significant effect on protein expression and enzyme activity with octopamine as substrate.|||Phenylethanolamine N-methyltransferase|||Phosphoserine|||Reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine 6-fold. Decreases affinity for S-adenosyl-L-methionine 2-fold.|||Removed|||Significant decrease in protein expression and enzyme activity with octopamine as substrate.|||Slight increase in protein expression and enzyme activity with octopamine as substrate.|||Strongly increases KM for phenylethanolamine and S-adenosyl-L-methionine.|||Strongly reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine 200-fold. Decreases affinity for S-adenosyl-L-methionine 3-fold.|||Strongly reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine and S-adenosyl-L-methionine 3-fold.|||Strongly reduced enzyme activity towards phenylethanolamine. Increases affinity for S-adenosyl-L-methionine.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159709|||http://purl.uniprot.org/annotation/VAR_024547|||http://purl.uniprot.org/annotation/VAR_029351|||http://purl.uniprot.org/annotation/VAR_036829|||http://purl.uniprot.org/annotation/VAR_036830|||http://purl.uniprot.org/annotation/VAR_036831|||http://purl.uniprot.org/annotation/VAR_037611|||http://purl.uniprot.org/annotation/VAR_037612|||http://purl.uniprot.org/annotation/VAR_037613|||http://purl.uniprot.org/annotation/VAR_037614
http://togogenome.org/gene/9606:MMP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50281                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In WNCHRS; results in increased MMP14 proteasomal degradation and reduced protein localization to cell membrane.|||Matrix metalloproteinase-14|||Phosphotyrosine; by PKDCC|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028798|||http://purl.uniprot.org/annotation/PRO_0000028799|||http://purl.uniprot.org/annotation/VAR_021029|||http://purl.uniprot.org/annotation/VAR_021030|||http://purl.uniprot.org/annotation/VAR_021031|||http://purl.uniprot.org/annotation/VAR_021032|||http://purl.uniprot.org/annotation/VAR_021033|||http://purl.uniprot.org/annotation/VAR_021034|||http://purl.uniprot.org/annotation/VAR_021035|||http://purl.uniprot.org/annotation/VAR_031267|||http://purl.uniprot.org/annotation/VAR_070567
http://togogenome.org/gene/9606:THAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6K1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HCFC1-binding motif (HBM)|||In isoform 2.|||THAP domain-containing protein 5|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333817|||http://purl.uniprot.org/annotation/VSP_033558
http://togogenome.org/gene/9606:MAGED4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MAGE|||Melanoma-associated antigen D4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156728|||http://purl.uniprot.org/annotation/VSP_009287|||http://purl.uniprot.org/annotation/VSP_009288|||http://purl.uniprot.org/annotation/VSP_009289|||http://purl.uniprot.org/annotation/VSP_035013
http://togogenome.org/gene/9606:UBXN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LJ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Reduced interaction with VCP.|||UBX|||UBX domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211029
http://togogenome.org/gene/9606:OR51A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGJ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150743|||http://purl.uniprot.org/annotation/VAR_034313|||http://purl.uniprot.org/annotation/VAR_034314|||http://purl.uniprot.org/annotation/VAR_053306|||http://purl.uniprot.org/annotation/VAR_062076|||http://purl.uniprot.org/annotation/VAR_062077
http://togogenome.org/gene/9606:OR7A17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR5|||http://purl.uniprot.org/uniprot/O14581                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7A17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150645|||http://purl.uniprot.org/annotation/VAR_053228|||http://purl.uniprot.org/annotation/VAR_053229|||http://purl.uniprot.org/annotation/VAR_053230|||http://purl.uniprot.org/annotation/VAR_053231
http://togogenome.org/gene/9606:CYP4F11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBI6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4F11|||Does not affect enzyme activity.|||Helical|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051856|||http://purl.uniprot.org/annotation/VAR_060265|||http://purl.uniprot.org/annotation/VAR_060266|||http://purl.uniprot.org/annotation/VAR_071198
http://togogenome.org/gene/9606:USP30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUS5|||http://purl.uniprot.org/uniprot/Q70CQ3                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Loss of deubiquitinase activity and impaired ability to inhibit mitophagy. Increased TOMM20 ubiquitination.|||Loss of mitochondrial subcellular location. Located in the endoplasmic reticulum.|||Mitochondrial intermembrane|||No change in mitochondrial subcellular location; when associated with N-30 and N-33.|||No effect on subcellular location; when associated with N-28 and N-30.|||No effect on subcellular location; when associated with N-28 and N-33.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080662|||http://purl.uniprot.org/annotation/VAR_059751
http://togogenome.org/gene/9606:ASPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQ07|||http://purl.uniprot.org/uniprot/B7ZM96|||http://purl.uniprot.org/uniprot/Q12797                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aspartyl beta-hydroxylase/Triadin|||Aspartyl/asparaginyl beta-hydroxylase|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In FDLAB.|||In isoform 11.|||In isoform 2, isoform 5, isoform 6, isoform 8, isoform 9 and isoform 11.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4, isoform 5, isoform 8, isoform 9 and isoform 10.|||In isoform 3, isoform 5, isoform 7, isoform 8 and isoform 9.|||In isoform 5.|||In isoform 6 and isoform 9.|||In isoform 7.|||Increase in cytoplasmic Ca(2+) via activation of endogenous CRAC channels.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064706|||http://purl.uniprot.org/annotation/VAR_053781|||http://purl.uniprot.org/annotation/VAR_071821|||http://purl.uniprot.org/annotation/VSP_039165|||http://purl.uniprot.org/annotation/VSP_039166|||http://purl.uniprot.org/annotation/VSP_039167|||http://purl.uniprot.org/annotation/VSP_039168|||http://purl.uniprot.org/annotation/VSP_039169|||http://purl.uniprot.org/annotation/VSP_039170|||http://purl.uniprot.org/annotation/VSP_044235|||http://purl.uniprot.org/annotation/VSP_044236|||http://purl.uniprot.org/annotation/VSP_044237|||http://purl.uniprot.org/annotation/VSP_044238|||http://purl.uniprot.org/annotation/VSP_059345
http://togogenome.org/gene/9606:SLC6A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01959                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contributes to high-affinity binding to cocaine|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In PKDYS1; loss of dopamine:sodium symporter activity.|||In a breast cancer sample; somatic mutation.|||Interaction with TGFB1I1|||Interchain|||N-linked (GlcNAc...) asparagine|||Sodium-dependent dopamine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214751|||http://purl.uniprot.org/annotation/VAR_014180|||http://purl.uniprot.org/annotation/VAR_036158|||http://purl.uniprot.org/annotation/VAR_036159|||http://purl.uniprot.org/annotation/VAR_063771|||http://purl.uniprot.org/annotation/VAR_063772|||http://purl.uniprot.org/annotation/VAR_064580
http://togogenome.org/gene/9606:RAET1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VY80                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||In allele ULBP6*01 and allele ULBP6*04.|||In allele ULBP6*01, allele ULBP6*02 and allele ULBP6*04.|||In allele ULBP6*01; affects KLRK1-binding affinity and KLRK1-mediated cytotoxic response.|||In allele ULBP6*01; no effect on KLRK1-binding affinity.|||MHC class I alpha-1 like|||MHC class I alpha-2 like|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UL16-binding protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320324|||http://purl.uniprot.org/annotation/PRO_0000320325|||http://purl.uniprot.org/annotation/VAR_039183|||http://purl.uniprot.org/annotation/VAR_039184|||http://purl.uniprot.org/annotation/VAR_039185|||http://purl.uniprot.org/annotation/VAR_079132
http://togogenome.org/gene/9606:NOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A286YF65|||http://purl.uniprot.org/uniprot/Q9HC29                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATG16L1-binding motif|||Abolished NF-kappa-B activation in response to muramyl dipeptide stimulation.|||Abolished NF-kappa-B activation in response to muramyl dipeptide stimulation. Decreased interaction with RIPK2.|||Abolished binding to ubiquitin; when associated with R-104.|||Abolished binding to ubiquitin; when associated with R-200.|||Abolished localization to the cell membrane.|||Abolished palmitoylation and localization to the cell membrane; when associated with S-1033.|||Abolished palmitoylation and localization to the cell membrane; when associated with S-395.|||Abolished pattern recognition receptor activity.|||CARD|||CARD 1|||CARD 2|||Constitutive NF-kappa-B activation.|||Constitutive NF-kappa-B activation; when associated with I-637.|||Constitutive NF-kappa-B activation; when associated with I-719.|||Constitutive NF-kappa-B activation; when associated with R-680.|||Constitutive NF-kappa-B activation; when associated with R-731.|||Constitutive NF-kappa-B activation; when associated with V-725.|||Constitutive NF-kappa-B activation; when associated with Y-710.|||Decreased ability to promote NF-kappa-B activation.|||Decreased binding to muramyl dipeptide (MDP).|||Decreased response to muramyl dipeptide (MDP).|||Does not affect NF-kappa-B activation in response to muramyl dipeptide stimulation.|||Does not affect ability to promote NF-kappa-B activation.|||Does not affect activity.|||Does not affect response to muramyl dipeptide (MDP).|||Dominant-negative mutant. Abolished NF-kappa-B activation in response to muramyl dipeptide stimulation. Decreased interaction with RIPK2.|||Hyperactive.|||In BLAUS and IBD1; unknown pathological significance.|||In BLAUS.|||In BLAUS; atypical form with cardiac infiltration; sporadic case; unknown pathological significance; hyperactive.|||In BLAUS; hyperactive.|||In BLAUS; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation.|||In BLAUS; no disruption of NOD2-CARD9 interaction; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation.|||In BLAUS; somatic mosaicism in 4.9% to 11% of peripheral blood cells; hyperactive; constitutive NF-kappa-B activation in absence of muramyl dipeptide stimulation; abolishes interaction with LDOC1, ANKHD1, PPP2R3B, ENTR1 and TRIM41; decreases interaction with RIPK2 and PPP1R12C; no effect on interaction with CHMP5.|||In BLAUS; unknown pathological significance; hyperactive.|||In BLAUS; unknown pathological significance; not hyperactive.|||In IBD1 and YAOS; associated with disease susceptibility; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation; decreases half-life of protein; abolishes interaction with ANKHD1, ENTR1 and TRIM41; decreases interaction with RIPK2 and PPP1R12C; no effect on interaction with CHMP5, LDOC1 and PPP2R3B.|||In IBD1 and YAOS; associated with disease susceptibility; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation; no disruption of NOD2-CARD9 interaction; decreases half-life of protein; abolishes interaction with ANKHD1, ENTR1 and TRIM41; increases interaction with RIPK2 and PPP2R3B; decreases interaction with LDOC1 and PPP1R12C; no effect on interaction with CHMP5; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation.|||In IBD1; abolished NF-kappa-B activation in response to muramyl dipeptide stimulation; decreased localization to the cell membrane.|||In IBD1; also found in patients with ulcerative colitis; unknown pathological significance.|||In IBD1; decreased NF-kappa-B activation in response to muramyl dipeptide stimulation.|||In IBD1; unknown pathological significance.|||In IBD1; unknown pathological significance; no disruption of NOD2-CARD9 interaction.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increased NF-kappa-B activation in response to muramyl dipeptide stimulation.|||Increased palmitoylation and protein stability, leading to constitutive NF-kappa-B activation.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||No activation.|||No disruption in NOD2-CARD9 interaction. Decreased NF-kappa-B activation in response to muramyl dipeptide stimulation.|||No disruption of NOD2-CARD9 interaction.|||Nucleotide-binding oligomerization domain-containing protein 2|||Required for CARD9 binding|||S-palmitoyl cysteine|||Slightly decreased response to muramyl dipeptide (MDP).|||Strongly decreased binding to muramyl dipeptide (MDP). ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004418|||http://purl.uniprot.org/annotation/VAR_012665|||http://purl.uniprot.org/annotation/VAR_012666|||http://purl.uniprot.org/annotation/VAR_012667|||http://purl.uniprot.org/annotation/VAR_012668|||http://purl.uniprot.org/annotation/VAR_012669|||http://purl.uniprot.org/annotation/VAR_012670|||http://purl.uniprot.org/annotation/VAR_012671|||http://purl.uniprot.org/annotation/VAR_012672|||http://purl.uniprot.org/annotation/VAR_012673|||http://purl.uniprot.org/annotation/VAR_012674|||http://purl.uniprot.org/annotation/VAR_012675|||http://purl.uniprot.org/annotation/VAR_012676|||http://purl.uniprot.org/annotation/VAR_012677|||http://purl.uniprot.org/annotation/VAR_012678|||http://purl.uniprot.org/annotation/VAR_012679|||http://purl.uniprot.org/annotation/VAR_012680|||http://purl.uniprot.org/annotation/VAR_012681|||http://purl.uniprot.org/annotation/VAR_012682|||http://purl.uniprot.org/annotation/VAR_012683|||http://purl.uniprot.org/annotation/VAR_012684|||http://purl.uniprot.org/annotation/VAR_012685|||http://purl.uniprot.org/annotation/VAR_012686|||http://purl.uniprot.org/annotation/VAR_012687|||http://purl.uniprot.org/annotation/VAR_012688|||http://purl.uniprot.org/annotation/VAR_012689|||http://purl.uniprot.org/annotation/VAR_012690|||http://purl.uniprot.org/annotation/VAR_012691|||http://purl.uniprot.org/annotation/VAR_012692|||http://purl.uniprot.org/annotation/VAR_012693|||http://purl.uniprot.org/annotation/VAR_012694|||http://purl.uniprot.org/annotation/VAR_012695|||http://purl.uniprot.org/annotation/VAR_012696|||http://purl.uniprot.org/annotation/VAR_012697|||http://purl.uniprot.org/annotation/VAR_012698|||http://purl.uniprot.org/annotation/VAR_012699|||http://purl.uniprot.org/annotation/VAR_012700|||http://purl.uniprot.org/annotation/VAR_012701|||http://purl.uniprot.org/annotation/VAR_012702|||http://purl.uniprot.org/annotation/VAR_012703|||http://purl.uniprot.org/annotation/VAR_012704|||http://purl.uniprot.org/annotation/VAR_023822|||http://purl.uniprot.org/annotation/VAR_023823|||http://purl.uniprot.org/annotation/VAR_023824|||http://purl.uniprot.org/annotation/VAR_024402|||http://purl.uniprot.org/annotation/VAR_036871|||http://purl.uniprot.org/annotation/VAR_036872|||http://purl.uniprot.org/annotation/VAR_065228|||http://purl.uniprot.org/annotation/VAR_073180|||http://purl.uniprot.org/annotation/VAR_073228|||http://purl.uniprot.org/annotation/VAR_073229|||http://purl.uniprot.org/annotation/VAR_073230|||http://purl.uniprot.org/annotation/VAR_073231|||http://purl.uniprot.org/annotation/VAR_073232|||http://purl.uniprot.org/annotation/VAR_073233|||http://purl.uniprot.org/annotation/VAR_073234|||http://purl.uniprot.org/annotation/VAR_073235|||http://purl.uniprot.org/annotation/VAR_073236|||http://purl.uniprot.org/annotation/VAR_073237|||http://purl.uniprot.org/annotation/VAR_073238|||http://purl.uniprot.org/annotation/VAR_073239|||http://purl.uniprot.org/annotation/VAR_073240|||http://purl.uniprot.org/annotation/VAR_073241|||http://purl.uniprot.org/annotation/VAR_073242|||http://purl.uniprot.org/annotation/VAR_073243|||http://purl.uniprot.org/annotation/VAR_073244|||http://purl.uniprot.org/annotation/VAR_073245|||http://purl.uniprot.org/annotation/VAR_073246|||http://purl.uniprot.org/annotation/VAR_073247|||http://purl.uniprot.org/annotation/VAR_073248|||http://purl.uniprot.org/annotation/VAR_073249|||http://purl.uniprot.org/annotation/VAR_088136|||http://purl.uniprot.org/annotation/VAR_088137|||http://purl.uniprot.org/annotation/VAR_088138|||http://purl.uniprot.org/annotation/VSP_018689|||http://purl.uniprot.org/annotation/VSP_046567|||http://purl.uniprot.org/annotation/VSP_046568
http://togogenome.org/gene/9606:IRF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1B1|||http://purl.uniprot.org/uniprot/M9RSF4|||http://purl.uniprot.org/uniprot/Q92985                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by viral EV 71 protease 3C and EV68 protease 3C|||(Microbial infection) Cleavage; by viral EV68 protease 3C|||Abolished IFNB induction upon Sendai virus infection.|||Abolishes IFNB induction upon Sendai virus infection.|||Complete loss of TBK1 and IKKE phosphorylation.|||Complete loss of cleavage by enterovirus 71.|||Complete loss of inactivation of IFN-I production; when associated with A-167.|||Complete loss of inactivation of IFN-I production; when associated with R-189.|||Decreased IFNB induction upon Sendai virus infection.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||IRF tryptophan pentad repeat|||In IMD39; loss of function mutation; shows abnormal localization to the cytoplasm rather than the nucleus; abolished IFNB induction upon Sendai virus infection.|||In isoform B.|||In isoform C.|||In isoform D.|||Interferon regulatory factor 7|||Interferon regulatory factor-3|||Loss of NEURL3-mediated ubiquitination.|||Loss of acetylation, DNA-binding and activity.|||Loss of acetylation, increased DNA-binding and activity; when associated with R-93.|||Loss of acetylation, increased DNA-binding and activity; when associated with T-90.|||N6-acetyllysine; by KAT2A and KAT2B|||Necessary for the interaction with NMI|||No effect IFNB induction upon Sendai virus infection.|||No effect on IFNB induction upon Sendai virus infection.|||No effect on cleavage by enterovirus 71.|||Phosphoserine|||Phosphoserine; by TBK1 and IKKE|||Requires 2 nucleotide substitutions; no effect on IFNB induction upon Sendai virus infection.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154562|||http://purl.uniprot.org/annotation/VAR_027957|||http://purl.uniprot.org/annotation/VAR_034017|||http://purl.uniprot.org/annotation/VAR_061273|||http://purl.uniprot.org/annotation/VAR_073779|||http://purl.uniprot.org/annotation/VAR_084074|||http://purl.uniprot.org/annotation/VAR_084075|||http://purl.uniprot.org/annotation/VAR_084076|||http://purl.uniprot.org/annotation/VAR_084077|||http://purl.uniprot.org/annotation/VAR_084078|||http://purl.uniprot.org/annotation/VAR_084079|||http://purl.uniprot.org/annotation/VAR_084080|||http://purl.uniprot.org/annotation/VAR_084081|||http://purl.uniprot.org/annotation/VAR_084082|||http://purl.uniprot.org/annotation/VAR_084083|||http://purl.uniprot.org/annotation/VAR_084084|||http://purl.uniprot.org/annotation/VSP_002757|||http://purl.uniprot.org/annotation/VSP_002758|||http://purl.uniprot.org/annotation/VSP_002759|||http://purl.uniprot.org/annotation/VSP_002760
http://togogenome.org/gene/9606:SIGMAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T9D5|||http://purl.uniprot.org/uniprot/A0A7P0Z4C2|||http://purl.uniprot.org/uniprot/A2A3U5|||http://purl.uniprot.org/uniprot/B4DR71|||http://purl.uniprot.org/uniprot/Q99720                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-terminal hydrophobic region|||Cytoplasmic|||Disordered|||Helical|||Important for ligand binding|||Important for ligand-binding|||In ALS16; the mutation decreases the viability of motor neurons; the mutant protein is shifted to lower density membranes and forms detergent-resistant complexes; there is an almost 2-fold increase in apoptosis in response to stress compared to controls.|||In DSMA2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lumenal|||No effect on ligand-binding.|||Reduces ligand-binding. No effect on subcellular localization.|||Sigma non-opioid intracellular receptor 1|||Targeting to endoplasmic reticulum-associated lipid droplets                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268652|||http://purl.uniprot.org/annotation/VAR_029750|||http://purl.uniprot.org/annotation/VAR_029751|||http://purl.uniprot.org/annotation/VAR_067311|||http://purl.uniprot.org/annotation/VAR_078816|||http://purl.uniprot.org/annotation/VSP_021981|||http://purl.uniprot.org/annotation/VSP_021982|||http://purl.uniprot.org/annotation/VSP_021983|||http://purl.uniprot.org/annotation/VSP_021984|||http://purl.uniprot.org/annotation/VSP_021985|||http://purl.uniprot.org/annotation/VSP_021986
http://togogenome.org/gene/9606:SPEN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T58                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In RATARS.|||In RATARS; uncertain pathological significance.|||In a breast cancer sample; somatic mutation.|||Interaction with MSX2|||Interaction with RBPSUH|||Msx2-interacting protein|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RID|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||SPOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081627|||http://purl.uniprot.org/annotation/VAR_017119|||http://purl.uniprot.org/annotation/VAR_017120|||http://purl.uniprot.org/annotation/VAR_017121|||http://purl.uniprot.org/annotation/VAR_035483|||http://purl.uniprot.org/annotation/VAR_035484|||http://purl.uniprot.org/annotation/VAR_052208|||http://purl.uniprot.org/annotation/VAR_085747|||http://purl.uniprot.org/annotation/VAR_085748|||http://purl.uniprot.org/annotation/VAR_085749|||http://purl.uniprot.org/annotation/VAR_085750|||http://purl.uniprot.org/annotation/VAR_085751|||http://purl.uniprot.org/annotation/VAR_085752|||http://purl.uniprot.org/annotation/VAR_085753|||http://purl.uniprot.org/annotation/VAR_085754|||http://purl.uniprot.org/annotation/VAR_085755|||http://purl.uniprot.org/annotation/VAR_085756|||http://purl.uniprot.org/annotation/VAR_085757|||http://purl.uniprot.org/annotation/VAR_085758
http://togogenome.org/gene/9606:CENPQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L2Z9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes the recruitment CENPE to kinetochores but has no effect on recruitment of PLK1 to knetochores.|||Basic and acidic residues|||Centromere protein Q|||Disordered|||No loss of the recruitment CENPE to kinetochores.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089534|||http://purl.uniprot.org/annotation/VAR_022857|||http://purl.uniprot.org/annotation/VAR_024303
http://togogenome.org/gene/9606:TIMM17B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60830                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Mitochondrial import inner membrane translocase subunit Tim17-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210287|||http://purl.uniprot.org/annotation/VSP_047215
http://togogenome.org/gene/9606:AKAP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GIA7|||http://purl.uniprot.org/uniprot/Q6PJH3|||http://purl.uniprot.org/uniprot/Q99996                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein 9|||Basic and acidic residues|||Disordered|||In LQT11.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 1, isoform 4, isoform 5 and isoform 6.|||In isoform 1.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PKA-RII subunit binding domain|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064534|||http://purl.uniprot.org/annotation/VAR_010926|||http://purl.uniprot.org/annotation/VAR_024249|||http://purl.uniprot.org/annotation/VAR_030162|||http://purl.uniprot.org/annotation/VAR_030163|||http://purl.uniprot.org/annotation/VAR_035785|||http://purl.uniprot.org/annotation/VAR_035786|||http://purl.uniprot.org/annotation/VAR_043489|||http://purl.uniprot.org/annotation/VAR_043490|||http://purl.uniprot.org/annotation/VAR_043491|||http://purl.uniprot.org/annotation/VAR_043492|||http://purl.uniprot.org/annotation/VSP_059522|||http://purl.uniprot.org/annotation/VSP_059523|||http://purl.uniprot.org/annotation/VSP_059524|||http://purl.uniprot.org/annotation/VSP_059525|||http://purl.uniprot.org/annotation/VSP_059526|||http://purl.uniprot.org/annotation/VSP_059527|||http://purl.uniprot.org/annotation/VSP_059528
http://togogenome.org/gene/9606:ZC3H11C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLD8|||http://purl.uniprot.org/uniprot/B4DYM8|||http://purl.uniprot.org/uniprot/P0DQW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Polar residues|||Zinc finger CCCH domain-containing protein 11C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000457096
http://togogenome.org/gene/9606:CALHM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5R3K3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 6|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283781|||http://purl.uniprot.org/annotation/VAR_053085|||http://purl.uniprot.org/annotation/VAR_053086|||http://purl.uniprot.org/annotation/VAR_071081|||http://purl.uniprot.org/annotation/VSP_055698|||http://purl.uniprot.org/annotation/VSP_055699
http://togogenome.org/gene/9606:SPICE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Z3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spindle and centriole-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282413|||http://purl.uniprot.org/annotation/VAR_050756|||http://purl.uniprot.org/annotation/VAR_050757
http://togogenome.org/gene/9606:FXR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51116                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Agenet-like 1|||Agenet-like 2|||Basic and acidic residues|||Disordered|||KH 1|||KH 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding protein FXR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050110|||http://purl.uniprot.org/annotation/VAR_055979|||http://purl.uniprot.org/annotation/VAR_067039
http://togogenome.org/gene/9606:PSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PKW4|||http://purl.uniprot.org/uniprot/Q86YI3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of GEF activity, loss of ARF6 localization to the cleavage furrow and, later in cytokinesis, to the midbody ring.|||Loss of localization to the plasma membrane during interphase and to the cleavage furrow during cytokinesis. No effect on ARF6 localization to the cleavage furrow and, later in cytokinesis, to the midbody ring.|||PH|||PH and SEC7 domain-containing protein 1|||Phosphoserine|||Polar residues|||Pro residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318298|||http://purl.uniprot.org/annotation/VSP_031186
http://togogenome.org/gene/9606:MAFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHW3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In INSDM; may prevent phosphorylation at S-65; may enhance protein stability.|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor MafA|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320274|||http://purl.uniprot.org/annotation/VAR_080790
http://togogenome.org/gene/9606:AMY1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTE7|||http://purl.uniprot.org/uniprot/P0DTE8|||http://purl.uniprot.org/uniprot/P0DUB6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-amylase 1A|||Alpha-amylase 1B|||Alpha-amylase 1C|||Deamidated asparagine; partial|||Deamidated asparagine; partial; alternate|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001401|||http://purl.uniprot.org/annotation/PRO_0000450820|||http://purl.uniprot.org/annotation/PRO_0000450821
http://togogenome.org/gene/9606:NUP62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37198                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 2 AA repeats of F-G|||Disordered|||In SNDI.|||Interchain (with NUP155)|||N-acetylserine|||Nuclear pore glycoprotein p62|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Removed|||Required for centrosome localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204880|||http://purl.uniprot.org/annotation/VAR_013467|||http://purl.uniprot.org/annotation/VAR_028064|||http://purl.uniprot.org/annotation/VAR_028065|||http://purl.uniprot.org/annotation/VAR_034904
http://togogenome.org/gene/9606:CFAP298                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57076                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 298|||In CILD26; unknown pathological significance; hypomorphic mutation.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079523|||http://purl.uniprot.org/annotation/VAR_070200|||http://purl.uniprot.org/annotation/VAR_070201|||http://purl.uniprot.org/annotation/VAR_070202
http://togogenome.org/gene/9606:TMEM220                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSZ3|||http://purl.uniprot.org/uniprot/Q6QAJ8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 220                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319424|||http://purl.uniprot.org/annotation/VSP_031477
http://togogenome.org/gene/9606:RNF130                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2HIY3|||http://purl.uniprot.org/uniprot/Q86XS8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||E3 ubiquitin-protein ligase RNF130|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PA|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030718|||http://purl.uniprot.org/annotation/VSP_055642|||http://purl.uniprot.org/annotation/VSP_055643
http://togogenome.org/gene/9606:POFUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H488                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to activate NOTCH signaling.|||GDP-fucose protein O-fucosyltransferase 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on ability to activate NOTCH signaling.|||Prevents secretion from ER|||Strongly impaired ability to activate NOTCH signaling.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012148|||http://purl.uniprot.org/annotation/VAR_049231|||http://purl.uniprot.org/annotation/VAR_049232|||http://purl.uniprot.org/annotation/VSP_001809
http://togogenome.org/gene/9606:RPL39L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EH5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Ribosomal protein eL39-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127027
http://togogenome.org/gene/9606:GPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP07|||http://purl.uniprot.org/uniprot/A0A096LPJ3|||http://purl.uniprot.org/uniprot/A0A9L9PXT0|||http://purl.uniprot.org/uniprot/C9JFE4|||http://purl.uniprot.org/uniprot/Q13098                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  COP9 signalosome complex subunit 1|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||PCI|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120959|||http://purl.uniprot.org/annotation/VSP_011882|||http://purl.uniprot.org/annotation/VSP_036240|||http://purl.uniprot.org/annotation/VSP_036241|||http://purl.uniprot.org/annotation/VSP_036242
http://togogenome.org/gene/9606:CTRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40313                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like protease CTRL-1|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027660|||http://purl.uniprot.org/annotation/PRO_0000027661|||http://purl.uniprot.org/annotation/VAR_021939|||http://purl.uniprot.org/annotation/VAR_051834
http://togogenome.org/gene/9606:UGT2B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06133                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 2B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036028|||http://purl.uniprot.org/annotation/VAR_007712|||http://purl.uniprot.org/annotation/VAR_011328|||http://purl.uniprot.org/annotation/VAR_011329|||http://purl.uniprot.org/annotation/VAR_060713|||http://purl.uniprot.org/annotation/VAR_060714|||http://purl.uniprot.org/annotation/VAR_060715|||http://purl.uniprot.org/annotation/VAR_060716|||http://purl.uniprot.org/annotation/VAR_060717|||http://purl.uniprot.org/annotation/VSP_056679|||http://purl.uniprot.org/annotation/VSP_056680|||http://purl.uniprot.org/annotation/VSP_056869|||http://purl.uniprot.org/annotation/VSP_056870
http://togogenome.org/gene/9606:NPTXR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95502                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Neuronal pentraxin receptor|||Pentraxin (PTX)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162506
http://togogenome.org/gene/9606:PDE6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHV7|||http://purl.uniprot.org/uniprot/P35913                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GAF 1|||GAF 2|||In CSNBAD2.|||In RP40.|||In RP40; autosomal dominant.|||In RP40; autosomal recessive and autosomal dominant.|||In RP40; autosomal recessive.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||PDEase|||Proton donor|||Removed|||Removed in mature form|||Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023348|||http://purl.uniprot.org/annotation/PRO_0000023349|||http://purl.uniprot.org/annotation/VAR_006050|||http://purl.uniprot.org/annotation/VAR_006051|||http://purl.uniprot.org/annotation/VAR_006052|||http://purl.uniprot.org/annotation/VAR_009283|||http://purl.uniprot.org/annotation/VAR_009284|||http://purl.uniprot.org/annotation/VAR_009285|||http://purl.uniprot.org/annotation/VAR_009286|||http://purl.uniprot.org/annotation/VAR_009287|||http://purl.uniprot.org/annotation/VAR_009288|||http://purl.uniprot.org/annotation/VAR_009289|||http://purl.uniprot.org/annotation/VAR_009290|||http://purl.uniprot.org/annotation/VAR_009291|||http://purl.uniprot.org/annotation/VAR_009292|||http://purl.uniprot.org/annotation/VAR_009293|||http://purl.uniprot.org/annotation/VAR_054868|||http://purl.uniprot.org/annotation/VAR_054869|||http://purl.uniprot.org/annotation/VAR_068361|||http://purl.uniprot.org/annotation/VAR_068362|||http://purl.uniprot.org/annotation/VSP_036884|||http://purl.uniprot.org/annotation/VSP_044919
http://togogenome.org/gene/9606:ANKRD37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E066|||http://purl.uniprot.org/uniprot/Q7Z713                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Motif|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 37|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244361|||http://purl.uniprot.org/annotation/VAR_048279
http://togogenome.org/gene/9606:LYZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4C5|||http://purl.uniprot.org/uniprot/P61626                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||In AMYL8.|||Lysozyme C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018467|||http://purl.uniprot.org/annotation/PRO_5014298326|||http://purl.uniprot.org/annotation/VAR_004280|||http://purl.uniprot.org/annotation/VAR_004281|||http://purl.uniprot.org/annotation/VAR_012050
http://togogenome.org/gene/9606:UPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7L5|||http://purl.uniprot.org/uniprot/B3KY55|||http://purl.uniprot.org/uniprot/Q92900                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes NMD.|||Abolishes ability to interact with UPF2/RENT2 and copurifies with greater amounts of SMG1, SMG8 and SMG9. Increases interaction with DHX34. No effect on interaction with SMG1-DHX34-UPF1 complex.|||Abolishes interaction with UPF2. Decreases interaction with DHX34.|||Abolishes interaction with UPF2. No effect on interaction with DHX34.|||C3H|||C4|||CC/SHH/C|||DNA2/NAM7 helicase-like C-terminal|||Decreases interaction with DHX34; when associated with E-508.|||Decreases interaction with DHX34; when associated with R-506.|||Disordered|||Impairs ATPase activity and ATP binding.|||Impairs ATPase activity, no effect on ATP binding.|||Impairs RNA binding.|||Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1107.|||Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1127.|||Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1107 and A-1127.|||Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1089, A-1107 and A-1127.|||Impairs phosphorylation.|||In isoform 2.|||Inhibits histone mRNA degradation, ATPase activity and ATP binding. No effect on interaction with DHX34.|||Inhibits histone mRNA degradation.|||Loss of ATPase activity and helicase activity.|||Loss of ATPase activity and helicase activity. Inhibits ZC3H12A-mediated IL6 mRNA degradation.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Prevents dephosphorylation and targets the protein to the P-body.|||Regulator of nonsense transcripts 1|||Still phosphorylated but with less efficiency.|||Sufficient for interaction with RENT2|||Upf1|||Upf1 CH-rich|||[ST]-Q motif 1|||[ST]-Q motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080716|||http://purl.uniprot.org/annotation/VAR_056207|||http://purl.uniprot.org/annotation/VSP_003393
http://togogenome.org/gene/9606:ARMC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6L4                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Repeat|||Splice Variant|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||Armadillo repeat-containing protein 7|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242666|||http://purl.uniprot.org/annotation/VSP_056936|||http://purl.uniprot.org/annotation/VSP_056937
http://togogenome.org/gene/9606:SLC35F4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4IF30|||http://purl.uniprot.org/uniprot/G3V4Z9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA|||Helical|||In isoform 2.|||Solute carrier family 35 member F4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311965|||http://purl.uniprot.org/annotation/VSP_029669
http://togogenome.org/gene/9606:BUB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJF3|||http://purl.uniprot.org/uniprot/O43684                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Mitotic checkpoint protein BUB3|||N6-acetyllysine|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050891|||http://purl.uniprot.org/annotation/VSP_038655
http://togogenome.org/gene/9606:SRP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37108                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphotyrosine|||Removed|||Signal recognition particle 14 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135189|||http://purl.uniprot.org/annotation/VAR_028057|||http://purl.uniprot.org/annotation/VAR_028058|||http://purl.uniprot.org/annotation/VAR_028059|||http://purl.uniprot.org/annotation/VAR_028060|||http://purl.uniprot.org/annotation/VAR_028061|||http://purl.uniprot.org/annotation/VAR_028062
http://togogenome.org/gene/9606:SLC17A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2U8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Vesicular|||Vesicular glutamate transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318169|||http://purl.uniprot.org/annotation/VAR_038710|||http://purl.uniprot.org/annotation/VAR_038711
http://togogenome.org/gene/9606:ITGAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13349|||http://purl.uniprot.org/uniprot/Q59H14                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Integrin alpha-D|||N-linked (GlcNAc...) asparagine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016296|||http://purl.uniprot.org/annotation/PRO_5001425908
http://togogenome.org/gene/9606:ECI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGA2|||http://purl.uniprot.org/uniprot/O75521                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ACB|||ECH-like|||Enoyl-CoA delta isomerase 2|||Important for catalytic activity|||In isoform 2.|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214027|||http://purl.uniprot.org/annotation/VAR_058493|||http://purl.uniprot.org/annotation/VAR_058494|||http://purl.uniprot.org/annotation/VSP_037854
http://togogenome.org/gene/9606:ZNF285                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLR9|||http://purl.uniprot.org/uniprot/K7EIK6|||http://purl.uniprot.org/uniprot/Q96NJ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 285                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000378106|||http://purl.uniprot.org/annotation/VAR_057972|||http://purl.uniprot.org/annotation/VAR_057973|||http://purl.uniprot.org/annotation/VSP_037502
http://togogenome.org/gene/9606:C4orf3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-acetylmethionine|||Uncharacterized protein C4orf3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325784|||http://purl.uniprot.org/annotation/VAR_039911|||http://purl.uniprot.org/annotation/VAR_039912|||http://purl.uniprot.org/annotation/VSP_032405
http://togogenome.org/gene/9606:STOML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYB4|||http://purl.uniprot.org/uniprot/Q9UJZ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Band 7|||Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKC/PRKCZ|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Stomatin-like protein 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094031|||http://purl.uniprot.org/annotation/VAR_026830|||http://purl.uniprot.org/annotation/VSP_054651
http://togogenome.org/gene/9606:KHDRBS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07666                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Asymmetric dimethylarginine; by PRMT1|||Asymmetric dimethylarginine; partial; by PRMT1|||Completely blocks nuclear localization.|||Dimethylated arginine; in A2780 ovarian carcinoma cell line|||Disordered|||Disrupts binding to poly(A). Decreased binding to the BCL2L1 mRNA. Loss of function in BCL2L1 splicing. Changed nuclear localization.|||Disrupts homodimerization, impairs influence on alternative splicing.|||Disrupts interaction with APC.|||Fails to influence alternative splicing of CD44, NRXN2 and NRXN3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs homodimerization.|||Impairs interaction with APC.|||In isoform 2.|||In isoform 3.|||Interaction with HNRNPA1|||Interaction with ZBTB7A|||Involved in homodimerization|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 1|||N6-acetyllysine; alternate|||No effect on the nuclear localization.|||Omega-N-methylarginine|||Omega-N-methylarginine; by PRMT1|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Phosphotyrosine|||Phosphotyrosine; by PTK6|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050124|||http://purl.uniprot.org/annotation/VSP_051719|||http://purl.uniprot.org/annotation/VSP_051720
http://togogenome.org/gene/9606:HOMER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U5K4|||http://purl.uniprot.org/uniprot/Q86YM7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homer protein homolog 1|||In isoform 2.|||In isoform 3.|||N-acetylglycine|||Phosphoserine|||Polar residues|||Removed|||Required for tetramerization|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191005|||http://purl.uniprot.org/annotation/VSP_009057|||http://purl.uniprot.org/annotation/VSP_009058|||http://purl.uniprot.org/annotation/VSP_009059
http://togogenome.org/gene/9606:FTHL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPV7|||http://purl.uniprot.org/uniprot/Q9BXU8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Ferritin heavy polypeptide-like 17|||Ferritin-like diiron                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201068|||http://purl.uniprot.org/annotation/VAR_033929|||http://purl.uniprot.org/annotation/VAR_049060
http://togogenome.org/gene/9606:RAB11FIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75154                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  ARF-binding domain (ABD)|||Abolishes Rab11-binding.|||Abolishes Rab11-binding. Capable of binding to DYNC1LI1. Impaired trafficking towards the pericentrosomal endosomal recycling compartment (ERC).|||Disordered|||EF-hand 1|||EF-hand 2|||FIP-RBD|||Important for binding to DYNC1LI1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by CDK1|||Polar residues|||Pro residues|||Rab11 family-interacting protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073879|||http://purl.uniprot.org/annotation/VSP_038664|||http://purl.uniprot.org/annotation/VSP_038665|||http://purl.uniprot.org/annotation/VSP_038666
http://togogenome.org/gene/9606:PLD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7P1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactive phospholipase D5|||N-linked (GlcNAc...) asparagine|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288606|||http://purl.uniprot.org/annotation/VSP_025724|||http://purl.uniprot.org/annotation/VSP_025725|||http://purl.uniprot.org/annotation/VSP_025726|||http://purl.uniprot.org/annotation/VSP_025727
http://togogenome.org/gene/9606:RPGRIP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX34|||http://purl.uniprot.org/uniprot/B7ZKJ9|||http://purl.uniprot.org/uniprot/H3BV03|||http://purl.uniprot.org/uniprot/Q68CZ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Associated with the development of retinal degeneration in individuals with ciliopathies caused by mutations in other genes; found in patients with Leber congenital amaurosis, Senior-Loken syndrome, Joubert syndrome and Bardet-Biedl syndrome; abrogates interaction with RPGR.|||Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||Found in a patient with Leber congenital amaurosis.|||In COACH3.|||In JBTS7.|||In JBTS7; affects interaction with NPHP4.|||In JBTS7; also in a patient with Leber congenital amaurosis; affects interaction with NPHP4.|||In JBTS7; seems not to affect interaction with NPHP4.|||In MKS5.|||In a patient with Leber congenital amaurosis.|||In a patient with Meckel-Gruber like syndrome also carrying L-220 and V-280 in TTC21B; also found in patients with Leber congenital amaurosis and a patient with Bardet-Biedl syndrome.|||In isoform 2.|||In patients with Leber congenital amaurosis.|||Polar residues|||Protein fantom                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291267|||http://purl.uniprot.org/annotation/VAR_039393|||http://purl.uniprot.org/annotation/VAR_039394|||http://purl.uniprot.org/annotation/VAR_039395|||http://purl.uniprot.org/annotation/VAR_039396|||http://purl.uniprot.org/annotation/VAR_039397|||http://purl.uniprot.org/annotation/VAR_039398|||http://purl.uniprot.org/annotation/VAR_063805|||http://purl.uniprot.org/annotation/VAR_065556|||http://purl.uniprot.org/annotation/VAR_066476|||http://purl.uniprot.org/annotation/VAR_066477|||http://purl.uniprot.org/annotation/VAR_066478|||http://purl.uniprot.org/annotation/VAR_066479|||http://purl.uniprot.org/annotation/VAR_066480|||http://purl.uniprot.org/annotation/VAR_066481|||http://purl.uniprot.org/annotation/VAR_066482|||http://purl.uniprot.org/annotation/VAR_066483|||http://purl.uniprot.org/annotation/VAR_069234|||http://purl.uniprot.org/annotation/VAR_076824|||http://purl.uniprot.org/annotation/VAR_076825|||http://purl.uniprot.org/annotation/VSP_026161|||http://purl.uniprot.org/annotation/VSP_026162
http://togogenome.org/gene/9606:WASHC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12768                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In SPG8.|||In SPG8; does not alter subcellular distribution; no effect on its binding to VCP; no effect on assembly in the WASH complex.|||In SPG8; dopamine responsive spasticity.|||In SPG8; fails to rescue the curly phenotype in a zebrafish model; no effect on assembly in the WASH complex.|||Phosphoserine|||WASH complex subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050733|||http://purl.uniprot.org/annotation/VAR_031955|||http://purl.uniprot.org/annotation/VAR_031956|||http://purl.uniprot.org/annotation/VAR_031957|||http://purl.uniprot.org/annotation/VAR_069984|||http://purl.uniprot.org/annotation/VAR_069985|||http://purl.uniprot.org/annotation/VAR_072417
http://togogenome.org/gene/9606:KDR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35968                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation of PLCG1 and MAP kinases in response to VEGFA.|||Abolishes reorganization of the actin cytoskeleton and cell migration in response to VEGFA.|||Abolishes stimulation of nitric oxide synthesis.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In HCI; associated with disease susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced and KDR activity is increased compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation predicts to result in loss-of-function and disruption of the normal association of these molecules.|||In HCI; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with SHB|||Interchain (with C-189 in SLC31A1)|||Loss of enzyme activity.|||Loss of phosphorylation site. Abolishes reorganization of the actin cytoskeleton in response to VEGFA.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Redox-active|||Significantly higher kinase activity.|||Strongly reduced autophosphorylation and activation of MAP kinases.|||Strongly reduced autophosphorylation and kinase activity.|||Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1054.|||Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1059.|||Strongly reduced autophosphorylation. Reduces phosphorylation of PLCG1.|||Vascular endothelial growth factor receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016771|||http://purl.uniprot.org/annotation/VAR_020353|||http://purl.uniprot.org/annotation/VAR_022071|||http://purl.uniprot.org/annotation/VAR_036126|||http://purl.uniprot.org/annotation/VAR_036127|||http://purl.uniprot.org/annotation/VAR_042053|||http://purl.uniprot.org/annotation/VAR_042054|||http://purl.uniprot.org/annotation/VAR_042055|||http://purl.uniprot.org/annotation/VAR_042056|||http://purl.uniprot.org/annotation/VAR_042057|||http://purl.uniprot.org/annotation/VAR_042058|||http://purl.uniprot.org/annotation/VAR_042059|||http://purl.uniprot.org/annotation/VAR_042060|||http://purl.uniprot.org/annotation/VAR_042061|||http://purl.uniprot.org/annotation/VAR_046679|||http://purl.uniprot.org/annotation/VAR_046680|||http://purl.uniprot.org/annotation/VAR_063147|||http://purl.uniprot.org/annotation/VSP_041988|||http://purl.uniprot.org/annotation/VSP_041989|||http://purl.uniprot.org/annotation/VSP_041990|||http://purl.uniprot.org/annotation/VSP_041991
http://togogenome.org/gene/9606:SLC37A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TED4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Glucose-6-phosphate exchanger SLC37A2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308322|||http://purl.uniprot.org/annotation/VAR_036794|||http://purl.uniprot.org/annotation/VAR_061803|||http://purl.uniprot.org/annotation/VSP_028960|||http://purl.uniprot.org/annotation/VSP_028961|||http://purl.uniprot.org/annotation/VSP_028962|||http://purl.uniprot.org/annotation/VSP_028963
http://togogenome.org/gene/9606:GABPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8IE48|||http://purl.uniprot.org/uniprot/Q06546|||http://purl.uniprot.org/uniprot/Q8IYS3                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||ETS|||GA-binding protein alpha chain|||PNT|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204127|||http://purl.uniprot.org/annotation/VAR_020315|||http://purl.uniprot.org/annotation/VAR_020316
http://togogenome.org/gene/9606:CLEC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P126                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 1 member B|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITAM|||In isoform 2.|||Loss of activation upon podoplanin or rhodocytin stimulation.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Significant reduction in rhodocytin binding.|||Substantial reduction in rhodocytin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280043|||http://purl.uniprot.org/annotation/VAR_031047|||http://purl.uniprot.org/annotation/VAR_031048|||http://purl.uniprot.org/annotation/VAR_031049|||http://purl.uniprot.org/annotation/VAR_031050|||http://purl.uniprot.org/annotation/VSP_023515
http://togogenome.org/gene/9606:ACTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63267                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished methylation by SETD3.|||Actin, gamma-enteric smooth muscle|||Actin, gamma-enteric smooth muscle, intermediate form|||Found in a severe infantile gastrointestinal motility disorder; unknown pathological significance.|||In MMIHS5 and VSCM1.|||In MMIHS5.|||In MMIHS5; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle.|||In MMIHS5; interferes with proper polymerization into thin filaments.|||In VSCM1 and MMIHS5.|||In VSCM1.|||In VSCM1; interferes with proper polymerization into thin filaments.|||In VSCM1; unknown pathological significance.|||In isoform 2.|||Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-51); by Vibrio toxins RtxA and VgrG1|||Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-271); by Vibrio toxins RtxA and VgrG1|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N-acetylglutamate; in Actin, gamma-enteric smooth muscle|||Removed|||Slightly decreased methylation by SETD3.|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000442949|||http://purl.uniprot.org/annotation/PRO_0000442950|||http://purl.uniprot.org/annotation/VAR_071279|||http://purl.uniprot.org/annotation/VAR_071280|||http://purl.uniprot.org/annotation/VAR_071281|||http://purl.uniprot.org/annotation/VAR_071282|||http://purl.uniprot.org/annotation/VAR_071283|||http://purl.uniprot.org/annotation/VAR_071284|||http://purl.uniprot.org/annotation/VAR_071285|||http://purl.uniprot.org/annotation/VAR_071286|||http://purl.uniprot.org/annotation/VAR_071287|||http://purl.uniprot.org/annotation/VAR_071288|||http://purl.uniprot.org/annotation/VAR_071289|||http://purl.uniprot.org/annotation/VAR_071290|||http://purl.uniprot.org/annotation/VAR_085866|||http://purl.uniprot.org/annotation/VAR_085867|||http://purl.uniprot.org/annotation/VAR_085868|||http://purl.uniprot.org/annotation/VAR_085869|||http://purl.uniprot.org/annotation/VAR_085870|||http://purl.uniprot.org/annotation/VAR_085871|||http://purl.uniprot.org/annotation/VAR_085872|||http://purl.uniprot.org/annotation/VAR_085873|||http://purl.uniprot.org/annotation/VAR_085874|||http://purl.uniprot.org/annotation/VSP_045861
http://togogenome.org/gene/9606:RTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKG5|||http://purl.uniprot.org/uniprot/B9EK54                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||DUF4939|||Disordered|||Helical|||Polar residues|||Retrotransposon-like protein 1|||Reverse transcriptase/retrotransposon-derived protein RNase H-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339233|||http://purl.uniprot.org/annotation/VAR_043937
http://togogenome.org/gene/9606:EPHA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1T8|||http://purl.uniprot.org/uniprot/B3KS12|||http://purl.uniprot.org/uniprot/Q6UWM0|||http://purl.uniprot.org/uniprot/Q9UF33                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-A receptor 6|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235684|||http://purl.uniprot.org/annotation/PRO_5004280772|||http://purl.uniprot.org/annotation/VAR_042149|||http://purl.uniprot.org/annotation/VAR_055991|||http://purl.uniprot.org/annotation/VSP_018473|||http://purl.uniprot.org/annotation/VSP_018474|||http://purl.uniprot.org/annotation/VSP_018475|||http://purl.uniprot.org/annotation/VSP_018476|||http://purl.uniprot.org/annotation/VSP_054716|||http://purl.uniprot.org/annotation/VSP_054717
http://togogenome.org/gene/9606:ZNF718                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXZ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 718                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233286|||http://purl.uniprot.org/annotation/VAR_059933|||http://purl.uniprot.org/annotation/VAR_059934|||http://purl.uniprot.org/annotation/VAR_059935|||http://purl.uniprot.org/annotation/VAR_059936|||http://purl.uniprot.org/annotation/VSP_018110
http://togogenome.org/gene/9606:H4C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:DCUN1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM76|||http://purl.uniprot.org/uniprot/C9JVE2|||http://purl.uniprot.org/uniprot/Q96GG9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  DCN1-like protein 1|||DCUN1|||Essential for interaction with UBE2M|||Loss of ability to stimulate cullin neddylation.|||Loss of binding to CAND1 and CUL-RBX1 complex but retains binding to UBE2M.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and A-241.Does not affect both nucleus and cytoplasm localization; when associated with A-211 and A-241. Reduces cullin neddylation; when associated with A-211 and A-241. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with A-211 and A-241. Loss of CUL2 interaction; when associated with A-211 and A-241. Reduces neddylation on CUL2; when associated with A-211 and A-241. Reduces interaction with VHL and HIF1A; when associated with A-211 and A-241. Does not affect interaction with SOCS1; when associated with A-211 and A-241. Does not affect DCUN1D1 monoubiquitylation; when associated with A-211 and A-241.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with A-211 and R-235.Does not affect both nucleus and cytoplasm localization; when associated withA-211 and R-235. Reduces cullin neddylation; when associated with A-211 and R-235. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with A-211 and R-235. Loss of CUL2 interaction; when associated with A-211 and R-235. Reduces neddylation on CUL2; when associated with A-211 and R-235. Reduces interaction with VHL and HIF1A; when associated with A-211 and R-235. Does not affect interaction with SOCS1; when associated with A-211 and R-235. Does not affect DCUN1D1 monoubiquitylation; when associated with A-211 and R-235.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CAND1 and RBX1; when associated with R-235 and A-241. Does not affect both nucleus and cytoplasm localization; when associated with R-235 and A-241. Reduces cullin neddylation; when associated with R-235 and A-241. Loss of interaction with CUL1, CUL2, CUL3, CULA4 and CULA4; when associated with R-235 and A-241. Loss of CUL2 interaction; when associated with R-235 and A-241. Reduces neddylation on CUL2; when associated with R-235 and A-241. Reduces interaction with VHL and HIF1A; when associated with R-235 and A-241. Does not affect interaction with SOCS1; when associated with R-235 and A-241. Does not affect DCUN1D1 monoubiquitylation; when associated with R-235 and A-241.|||Loss of ubiquitin binding; when associated with A-15, A-16 and A-44.|||Loss of ubiquitin binding; when associated with A-15, A-16 and A-45.|||Loss of ubiquitin binding; when associated with A-15, A-44 and A-45.|||Loss of ubiquitin binding; when associated with A-16, A-44 and A-45.|||N-acetylmethionine|||UBA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129498
http://togogenome.org/gene/9606:OR2A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWD8|||http://purl.uniprot.org/uniprot/Q96R45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150456
http://togogenome.org/gene/9606:DAPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJW8|||http://purl.uniprot.org/uniprot/M1E9T5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Death-associated protein-like 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316835|||http://purl.uniprot.org/annotation/VAR_038402|||http://purl.uniprot.org/annotation/VAR_038403
http://togogenome.org/gene/9606:PDSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YH6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  All trans-polyprenyl-diphosphate synthase PDSS2|||In COQ10D3.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123978|||http://purl.uniprot.org/annotation/VAR_049645|||http://purl.uniprot.org/annotation/VAR_055398|||http://purl.uniprot.org/annotation/VSP_017098|||http://purl.uniprot.org/annotation/VSP_017099
http://togogenome.org/gene/9606:ZNF776                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RN90|||http://purl.uniprot.org/uniprot/B4DSC6|||http://purl.uniprot.org/uniprot/Q68DI1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 776                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305140
http://togogenome.org/gene/9606:PIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11309                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased kinase activity.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Increased kinase activity.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase pim-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043349|||http://purl.uniprot.org/annotation/VAR_041004|||http://purl.uniprot.org/annotation/VAR_041005|||http://purl.uniprot.org/annotation/VAR_041006|||http://purl.uniprot.org/annotation/VAR_041007|||http://purl.uniprot.org/annotation/VSP_059829
http://togogenome.org/gene/9606:TBC1D7-LOC100130357                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0N9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished formation of the TSC-TBC complex; when associated with 81-A--A-84.|||Abolished formation of the TSC-TBC complex; when associated with A-121. Abolished interaction with TSC1 and TSC2; when associated with 94-A-A-95.|||Abolished interaction with TSC1.|||Abolished interaction with TSC1. Abolished interaction with TSC1 and TSC2; when associated with A-81--A-84.|||Decreased interaction with TSC1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Rab-GAP TBC|||TBC1 domain family member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208031|||http://purl.uniprot.org/annotation/VAR_052537|||http://purl.uniprot.org/annotation/VAR_052538|||http://purl.uniprot.org/annotation/VSP_041480|||http://purl.uniprot.org/annotation/VSP_044186|||http://purl.uniprot.org/annotation/VSP_044892
http://togogenome.org/gene/9606:SNX24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y343                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||PX|||Phosphoserine|||Sorting nexin-24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213872|||http://purl.uniprot.org/annotation/VSP_012034
http://togogenome.org/gene/9606:DDX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with RANBP9|||Phosphoserine|||Polar residues|||Probable ATP-dependent RNA helicase DDX4|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054977|||http://purl.uniprot.org/annotation/VAR_019574|||http://purl.uniprot.org/annotation/VAR_052159|||http://purl.uniprot.org/annotation/VSP_011197|||http://purl.uniprot.org/annotation/VSP_046132|||http://purl.uniprot.org/annotation/VSP_046133|||http://purl.uniprot.org/annotation/VSP_047177
http://togogenome.org/gene/9606:AXIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ES00|||http://purl.uniprot.org/uniprot/Q9Y2T1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Axin-2|||Basic and acidic residues|||DIX|||Disordered|||Interaction with GSK3B|||Interaction with SIAH1 and SIAH2|||Interaction with beta-catenin|||Polar residues|||RGS|||Tankyrase-binding motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220895|||http://purl.uniprot.org/annotation/VAR_054860
http://togogenome.org/gene/9606:CACNA1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR67|||http://purl.uniprot.org/uniprot/A0A0A0MSA1|||http://purl.uniprot.org/uniprot/A0A804HI37|||http://purl.uniprot.org/uniprot/A0A804HIJ8|||http://purl.uniprot.org/uniprot/A0A804HJB6|||http://purl.uniprot.org/uniprot/A0A804HKC4|||http://purl.uniprot.org/uniprot/E9PDI6|||http://purl.uniprot.org/uniprot/F5H522|||http://purl.uniprot.org/uniprot/Q13936|||http://purl.uniprot.org/uniprot/Q59GU3|||http://purl.uniprot.org/uniprot/Q5V9X9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AID/alpha-interaction domain; mediates interaction with the beta subunit|||Affects voltage-dependent inhibition by dihydropyridines; when associated with F-954.|||Affects voltage-dependent inhibition by dihydropyridines; when associated with I-958.|||Basic and acidic residues|||Calcium ion selectivity and permeability|||Calmodulin-binding|||Calmodulin-binding IQ region|||Cytoplasmic|||Dihydropyridine binding|||Disordered|||Extracellular|||Found in a clear cell renal carcinoma case; somatic mutation.|||Found in a patient with autism; unknown pathological significance.|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||Important for interaction with STAC1, STAC2 and STAC3|||Important for localization in at the junctional membrane|||In BRGDA3; unknown pathological significance; affects channel activity.|||In LQT8.|||In LQT8; gain of function activity.|||In LQT8; gain-of-function effect on channel activity.|||In LQT8; gain-of-function effect on channel activity; slower inactivation.|||In LQT8; leads to increased calcium currents; increased surface membrane expression of the channel.|||In LQT8; unknown pathological significance.|||In LQT8; unknown pathological significance; increased channel activity.|||In LQT8; unknown pathological significance; no effect on channel activity.|||In NEDHLSS.|||In NEDHLSS; affects voltage-gated calcium channel activity resulting in decreased current density when expressed in a heterologous system.|||In NEDHLSS; unknown pathological significance.|||In TS and LQT8; electrophysiological phenotype characterized by loss of current density and gain-of-function shift in activation leading to increased steady-state current; gain of function activity.|||In TS.|||In TS; affects voltage-gated calcium channel activity resulting in a marked decrease in peak currents and increased late currents.|||In TS; affects voltage-gated calcium channel activity resulting in loss of calcium selectivity; mutant channels show a marked increase in sodium-mediated inward currents and potassium-mediated outward currents.|||In TS; causes a nearly complete loss of voltage-dependent channel inactivation.|||In TS; only with cardiac manifestation; decreased current density; associated with slower inactivation.|||In TS; only with cardiac manifestation; decreased current density; associated with slower inactivation; altered localization.|||In isoform 10, isoform 13, isoform 14, isoform 15, isoform 24, isoform 25, isoform 27 and isoform 29.|||In isoform 11, isoform 12, isoform 13, isoform 14, isoform 15, isoform 17, isoform 19, isoform 20, isoform 21, isoform 22, isoform 23, isoform 24, isoform 25, isoform 26, isoform 27, isoform 29, isoform 30, isoform 31, isoform 32, isoform 35 and isoform 37.|||In isoform 14.|||In isoform 15.|||In isoform 16, isoform 17, isoform 18 and isoform 28.|||In isoform 2, isoform 18 and isoform 28.|||In isoform 3, isoform 16, isoform 17, isoform 18, isoform 23, isoform 28, isoform 36 and isoform 37.|||In isoform 34.|||In isoform 35.|||In isoform 4, isoform 19, isoform 20, isoform 21, isoform 23, isoform 26, isoform 27, isoform 29, isoform 32 and isoform 33.|||In isoform 5, isoform 12, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 22, isoform 24, isoform 25, isoform 28, isoform 31, isoform 35, isoform 36 and isoform 37.|||In isoform 6, isoform 12, isoform 14, isoform 15, isoform 19, isoform 20, isoform 23, isoform 24, isoform 25, isoform 26, isoform 27, isoform 28, isoform 29, isoform 30 and isoform 33.|||In isoform 7, isoform 13, isoform 16, isoform 17, isoform 18, isoform 21, isoform 22, isoform 35, isoform 36 and isoform 37.|||In isoform 8, isoform 19, isoform 25, isoform 28, isoform 29 and isoform 32.|||In isoform 9 and isoform 26.|||Interaction with STAC2|||Ion transport|||Loss of a low-affinity interaction with CALM1. No effect on channel inactivation by Ca(2+) and calmodulin.|||Loss of channel inactivation by Ca(2+) and calmodulin; when associated with 1666-A--A-1670.|||Loss of selectivity for divalent over monovalent cations.|||Mildly decreased channel activity. No effect on channel inactivation. Loss of channel inactivation by Ca(2+) and calmodulin; when associated with A-1672.|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Pore-forming|||Pro residues|||Rare variant; found in a case of sudden unexplained death in the young; unknown pathological significance; results in increased whole-cell calcium currents.|||Rare variant; found in a case of sudden unexplained death in the young; unknown pathological significance; results in reduced whole-cell calcium currents.|||Selectivity filter of repeat I|||Selectivity filter of repeat II|||Selectivity filter of repeat III|||Selectivity filter of repeat IV|||Voltage-dependent L-type calcium channel subunit alpha-1C|||Voltage-dependent calcium channel alpha-1 subunit IQ ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053928|||http://purl.uniprot.org/annotation/VAR_001495|||http://purl.uniprot.org/annotation/VAR_001496|||http://purl.uniprot.org/annotation/VAR_026741|||http://purl.uniprot.org/annotation/VAR_026742|||http://purl.uniprot.org/annotation/VAR_044039|||http://purl.uniprot.org/annotation/VAR_044040|||http://purl.uniprot.org/annotation/VAR_045987|||http://purl.uniprot.org/annotation/VAR_045988|||http://purl.uniprot.org/annotation/VAR_059223|||http://purl.uniprot.org/annotation/VAR_059224|||http://purl.uniprot.org/annotation/VAR_061102|||http://purl.uniprot.org/annotation/VAR_064700|||http://purl.uniprot.org/annotation/VAR_072381|||http://purl.uniprot.org/annotation/VAR_075148|||http://purl.uniprot.org/annotation/VAR_075149|||http://purl.uniprot.org/annotation/VAR_075150|||http://purl.uniprot.org/annotation/VAR_075151|||http://purl.uniprot.org/annotation/VAR_075152|||http://purl.uniprot.org/annotation/VAR_075153|||http://purl.uniprot.org/annotation/VAR_075154|||http://purl.uniprot.org/annotation/VAR_075155|||http://purl.uniprot.org/annotation/VAR_075156|||http://purl.uniprot.org/annotation/VAR_075157|||http://purl.uniprot.org/annotation/VAR_075158|||http://purl.uniprot.org/annotation/VAR_075159|||http://purl.uniprot.org/annotation/VAR_075160|||http://purl.uniprot.org/annotation/VAR_075161|||http://purl.uniprot.org/annotation/VAR_075162|||http://purl.uniprot.org/annotation/VAR_075163|||http://purl.uniprot.org/annotation/VAR_075164|||http://purl.uniprot.org/annotation/VAR_075165|||http://purl.uniprot.org/annotation/VAR_075166|||http://purl.uniprot.org/annotation/VAR_075167|||http://purl.uniprot.org/annotation/VAR_075168|||http://purl.uniprot.org/annotation/VAR_075169|||http://purl.uniprot.org/annotation/VAR_075170|||http://purl.uniprot.org/annotation/VAR_075171|||http://purl.uniprot.org/annotation/VAR_075172|||http://purl.uniprot.org/annotation/VAR_075173|||http://purl.uniprot.org/annotation/VAR_075174|||http://purl.uniprot.org/annotation/VAR_075175|||http://purl.uniprot.org/annotation/VAR_075176|||http://purl.uniprot.org/annotation/VAR_075177|||http://purl.uniprot.org/annotation/VAR_075178|||http://purl.uniprot.org/annotation/VAR_076414|||http://purl.uniprot.org/annotation/VAR_076415|||http://purl.uniprot.org/annotation/VAR_078701|||http://purl.uniprot.org/annotation/VAR_082632|||http://purl.uniprot.org/annotation/VAR_082633|||http://purl.uniprot.org/annotation/VAR_082634|||http://purl.uniprot.org/annotation/VAR_082635|||http://purl.uniprot.org/annotation/VAR_087754|||http://purl.uniprot.org/annotation/VAR_087755|||http://purl.uniprot.org/annotation/VAR_087756|||http://purl.uniprot.org/annotation/VAR_087757|||http://purl.uniprot.org/annotation/VAR_087758|||http://purl.uniprot.org/annotation/VAR_087759|||http://purl.uniprot.org/annotation/VAR_087760|||http://purl.uniprot.org/annotation/VAR_087761|||http://purl.uniprot.org/annotation/VAR_087762|||http://purl.uniprot.org/annotation/VAR_087763|||http://purl.uniprot.org/annotation/VAR_087764|||http://purl.uniprot.org/annotation/VAR_087765|||http://purl.uniprot.org/annotation/VAR_087766|||http://purl.uniprot.org/annotation/VAR_087767|||http://purl.uniprot.org/annotation/VAR_087768|||http://purl.uniprot.org/annotation/VAR_087769|||http://purl.uniprot.org/annotation/VAR_087770|||http://purl.uniprot.org/annotation/VAR_087771|||http://purl.uniprot.org/annotation/VAR_087772|||http://purl.uniprot.org/annotation/VSP_000885|||http://purl.uniprot.org/annotation/VSP_000886|||http://purl.uniprot.org/annotation/VSP_000887|||http://purl.uniprot.org/annotation/VSP_000888|||http://purl.uniprot.org/annotation/VSP_000889|||http://purl.uniprot.org/annotation/VSP_000890|||http://purl.uniprot.org/annotation/VSP_000891|||http://purl.uniprot.org/annotation/VSP_000892|||http://purl.uniprot.org/annotation/VSP_000893|||http://purl.uniprot.org/annotation/VSP_000894|||http://purl.uniprot.org/annotation/VSP_000895|||http://purl.uniprot.org/annotation/VSP_022503|||http://purl.uniprot.org/annotation/VSP_022504|||http://purl.uniprot.org/annotation/VSP_035146|||http://purl.uniprot.org/annotation/VSP_035877
http://togogenome.org/gene/9606:MAGEA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43358                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||MAGE|||Melanoma-associated antigen 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156704|||http://purl.uniprot.org/annotation/VAR_004284|||http://purl.uniprot.org/annotation/VAR_036582|||http://purl.uniprot.org/annotation/VAR_076262|||http://purl.uniprot.org/annotation/VAR_078319
http://togogenome.org/gene/9606:NMUR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB89                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuromedin-U receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069906
http://togogenome.org/gene/9606:TDP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDM5|||http://purl.uniprot.org/uniprot/O95551                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes function, but retains ability to interact with SMAD3; when associated with A-88.|||Abolishes function, but retains ability to interact with SMAD3; when associated with A-92.|||Decreased phosphodiesterase activity.|||Disordered|||Endonuclease/exonuclease/phosphatase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with 5' end of substrate DNA|||Loss of phosphodiesterase activity.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by ACVR1B|||Proton donor/acceptor|||Slightly decreased phosphodiesterase activity.|||Strongly decreased phosphodiesterase activity.|||Strongly reduced phosphodiesterase activity.|||Tyrosyl-DNA phosphodiesterase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065678|||http://purl.uniprot.org/annotation/VAR_022634|||http://purl.uniprot.org/annotation/VAR_022635|||http://purl.uniprot.org/annotation/VAR_051464|||http://purl.uniprot.org/annotation/VAR_076867|||http://purl.uniprot.org/annotation/VSP_038523|||http://purl.uniprot.org/annotation/VSP_038524
http://togogenome.org/gene/9606:CLEC4G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKQ2|||http://purl.uniprot.org/uniprot/Q08G24|||http://purl.uniprot.org/uniprot/Q6UXB4|||http://purl.uniprot.org/uniprot/Q6XYD1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member G|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223691
http://togogenome.org/gene/9606:TPRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMQ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||Taperin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330309|||http://purl.uniprot.org/annotation/VSP_033027|||http://purl.uniprot.org/annotation/VSP_033028|||http://purl.uniprot.org/annotation/VSP_039038|||http://purl.uniprot.org/annotation/VSP_039039
http://togogenome.org/gene/9606:RHD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B1R0Y1|||http://purl.uniprot.org/uniprot/B4DLT8|||http://purl.uniprot.org/uniprot/E7EVW1|||http://purl.uniprot.org/uniprot/Q02161|||http://purl.uniprot.org/uniprot/Q1KT12|||http://purl.uniprot.org/uniprot/Q5XLS8|||http://purl.uniprot.org/uniprot/Q5XLT0|||http://purl.uniprot.org/uniprot/Q5XLT3|||http://purl.uniprot.org/uniprot/Q7RU08|||http://purl.uniprot.org/uniprot/Q9UPC8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Ammonium transporter AmtB-like|||Blood group Rh(D) polypeptide|||Found in RhDVa(FK) and RhDVa(TT); may be associated with low RHD expression, resulting in a weak D phenotype.|||Found in RhDVa(FK), RhDVa(TO), RhDVa(TT) and RhDYo.|||Found in RhDVa(TO) and RhDVa(TT).|||Found in RhDVa(TT).|||Helical|||In Tar antigen.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||May be associated with low RHD expression, resulting in a weak D phenotype.|||May be associated with moderate decrease in RHD expression, resulting in DHMi phenotype.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168190|||http://purl.uniprot.org/annotation/VAR_006919|||http://purl.uniprot.org/annotation/VAR_006920|||http://purl.uniprot.org/annotation/VAR_013304|||http://purl.uniprot.org/annotation/VAR_013305|||http://purl.uniprot.org/annotation/VAR_013306|||http://purl.uniprot.org/annotation/VAR_013307|||http://purl.uniprot.org/annotation/VAR_034455|||http://purl.uniprot.org/annotation/VAR_034456|||http://purl.uniprot.org/annotation/VAR_034457|||http://purl.uniprot.org/annotation/VAR_035615|||http://purl.uniprot.org/annotation/VAR_047996|||http://purl.uniprot.org/annotation/VAR_047997|||http://purl.uniprot.org/annotation/VAR_047998|||http://purl.uniprot.org/annotation/VAR_086023|||http://purl.uniprot.org/annotation/VAR_086024|||http://purl.uniprot.org/annotation/VAR_086025|||http://purl.uniprot.org/annotation/VAR_086026|||http://purl.uniprot.org/annotation/VAR_086027|||http://purl.uniprot.org/annotation/VAR_086028|||http://purl.uniprot.org/annotation/VAR_086029|||http://purl.uniprot.org/annotation/VAR_086030|||http://purl.uniprot.org/annotation/VAR_086031|||http://purl.uniprot.org/annotation/VAR_086032|||http://purl.uniprot.org/annotation/VAR_086033|||http://purl.uniprot.org/annotation/VAR_086034|||http://purl.uniprot.org/annotation/VAR_086035|||http://purl.uniprot.org/annotation/VAR_086036|||http://purl.uniprot.org/annotation/VAR_086037|||http://purl.uniprot.org/annotation/VAR_086038|||http://purl.uniprot.org/annotation/VAR_086039|||http://purl.uniprot.org/annotation/VSP_005706|||http://purl.uniprot.org/annotation/VSP_005707|||http://purl.uniprot.org/annotation/VSP_005708|||http://purl.uniprot.org/annotation/VSP_047795|||http://purl.uniprot.org/annotation/VSP_047796|||http://purl.uniprot.org/annotation/VSP_047797|||http://purl.uniprot.org/annotation/VSP_047798
http://togogenome.org/gene/9606:EPB41L4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GC2|||http://purl.uniprot.org/uniprot/Q9H329|||http://purl.uniprot.org/uniprot/Q9NSG9|||http://purl.uniprot.org/uniprot/Q9NX84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 4.1-like protein 4B|||Basic and acidic residues|||Disordered|||FERM|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219404|||http://purl.uniprot.org/annotation/VAR_048356|||http://purl.uniprot.org/annotation/VSP_007202|||http://purl.uniprot.org/annotation/VSP_007203
http://togogenome.org/gene/9606:CBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83916|||http://purl.uniprot.org/uniprot/Q6IBN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand                                                                                  ^@                                                                                  Abolishes homodimer formation and binding to EMSY.|||Basic and acidic residues|||Chromo|||Chromo 1|||Chromo 2; shadow subtype|||Chromobox protein homolog 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3A7 binding|||Histone H3K9me2 binding|||Interacts with the PxVxL motif of TRIM28/TIF1B|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080199
http://togogenome.org/gene/9606:MBNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VM6|||http://purl.uniprot.org/uniprot/Q9NR56                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||In DM1; unknown pathological significance.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||Muscleblind-like protein 1|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089178|||http://purl.uniprot.org/annotation/VAR_076508|||http://purl.uniprot.org/annotation/VAR_076509|||http://purl.uniprot.org/annotation/VAR_076510|||http://purl.uniprot.org/annotation/VSP_006429|||http://purl.uniprot.org/annotation/VSP_006430|||http://purl.uniprot.org/annotation/VSP_043799|||http://purl.uniprot.org/annotation/VSP_043800|||http://purl.uniprot.org/annotation/VSP_044903
http://togogenome.org/gene/9606:CAMK1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NX5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1G|||Calmodulin-binding|||Disordered|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In isoform 2.|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086084|||http://purl.uniprot.org/annotation/VAR_020530|||http://purl.uniprot.org/annotation/VAR_040600|||http://purl.uniprot.org/annotation/VAR_040601|||http://purl.uniprot.org/annotation/VSP_012138
http://togogenome.org/gene/9606:MXD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14582                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Interaction with SIN3A and SIN3B|||Max dimerization protein 4|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127266
http://togogenome.org/gene/9606:SERTAD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||SERTA|||SERTA domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314139
http://togogenome.org/gene/9606:SEPHS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49903                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for catalytic activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased ATP-binding.|||Loss of ATP-binding.|||N-acetylserine|||No change in ATP-binding.|||Reduced ATP-binding.|||Removed|||Selenide, water dikinase 1|||Strongly reduced ADP hydrolysis.|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127648|||http://purl.uniprot.org/annotation/VSP_046701|||http://purl.uniprot.org/annotation/VSP_046702|||http://purl.uniprot.org/annotation/VSP_047451
http://togogenome.org/gene/9606:HPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWY4                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylserine|||ADP-ribosyltyrosine|||Abolished interaction with PARP2, leading to destabilize the PARP2-nucleosome complex.|||Abolished serine ADP-ribosylation by PARP1 and PARP2.|||Disordered|||Does not affect serine ADP-ribosylation by PARP1 and PARP2.|||Does not affect serine ADP-ribosylation of histones.|||Histone PARylation factor 1|||Interaction with PARP1|||Loss of ability to bind PARP1 and histones. Abolishes PARP1 ability to mediate ADP-ribosylation.|||N-acetylmethionine|||N6-acetyllysine|||PolyADP-ribosyl aspartic acid|||PolyADP-ribosyl glutamic acid|||Promotes auto-ADP-ribosylation of PARP1.|||Promotes auto-ADP-ribosylation of PARP1. Abolished interaction with PARP1.|||Proton donor|||Strongly reduced serine ADP-ribosylation by PARP1 and PARP2.|||Strongly reduced serine ADP-ribosylation by PARP1 and PARP2. Decreases PARP1 ability to mediate tyrosine ADP-ribosylation. Promotes auto-ADP-ribosylation of PARP1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294446|||http://purl.uniprot.org/annotation/VAR_033183|||http://purl.uniprot.org/annotation/VAR_033184
http://togogenome.org/gene/9606:STXBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWJ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||PDZ|||Phosphoserine|||Syntaxin-binding protein 4|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076330|||http://purl.uniprot.org/annotation/VAR_056999|||http://purl.uniprot.org/annotation/VAR_063103|||http://purl.uniprot.org/annotation/VSP_017175|||http://purl.uniprot.org/annotation/VSP_017176|||http://purl.uniprot.org/annotation/VSP_017177|||http://purl.uniprot.org/annotation/VSP_017178
http://togogenome.org/gene/9606:CD55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AP13|||http://purl.uniprot.org/uniprot/P08174                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complement decay-accelerating factor|||Disordered|||GPI-anchor amidated serine|||In CHAPLE; increased complement activation.|||In Cr(a-) antigen.|||In Dr(a-) antigen.|||In GUTI(-) antigen.|||In Tc(b) antigen.|||In Tc(c) antigen.|||In WES(a) antigen.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006000|||http://purl.uniprot.org/annotation/PRO_0000006001|||http://purl.uniprot.org/annotation/PRO_5002761429|||http://purl.uniprot.org/annotation/VAR_001997|||http://purl.uniprot.org/annotation/VAR_001998|||http://purl.uniprot.org/annotation/VAR_001999|||http://purl.uniprot.org/annotation/VAR_002000|||http://purl.uniprot.org/annotation/VAR_002001|||http://purl.uniprot.org/annotation/VAR_015884|||http://purl.uniprot.org/annotation/VAR_079373|||http://purl.uniprot.org/annotation/VSP_001200|||http://purl.uniprot.org/annotation/VSP_047634|||http://purl.uniprot.org/annotation/VSP_047635|||http://purl.uniprot.org/annotation/VSP_047636|||http://purl.uniprot.org/annotation/VSP_047637|||http://purl.uniprot.org/annotation/VSP_047638
http://togogenome.org/gene/9606:HPSE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y251                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes processing, secretion and enzyme activity.|||Alteration of the correct processing of heparanase which results in the cleavage at an upstream site in the linker peptide and no activation of proheparanase.|||Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-162; Q-200; Q-217; Q-238 and Q-459.|||Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-178; Q-200; Q-217; Q-238 and Q-459.|||Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-200; Q-238 and Q-459.|||Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-217; Q-238 and Q-459.|||Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-238.|||Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-459.|||Heparanase 50 kDa subunit|||Heparanase 8 kDa subunit|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In some hepatocellular carcinoma.|||Linker peptide|||Loss of heparanase activity.|||Loss of heparanase activity. No effect on HPSE-mediated cell adhesion.|||N-linked (GlcNAc...) asparagine|||No association with GS-modified heparin; when associated with K-158.|||No effect on processing nor secretion. No enzyme activity detected.|||No effect on processing, secretion nor enzyme activity.|||No reduction in heparanase activity.|||Normal processing.|||Nucleophile|||Proton donor|||Required for heterodimerization with the heparanase 8 kDa subunit|||Required for transferring proheparanase to the Golgi apparatus, secretion and subsequent enzyme activity and for enhancement of PKB/AKT1 phosphorylation|||Strong decrease in heparanase activity.|||Two-fold increase in the level of secretion upon addition of GS-modified heparin. No association with GS-modified heparin; when associated with K-161.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042260|||http://purl.uniprot.org/annotation/PRO_0000042261|||http://purl.uniprot.org/annotation/PRO_0000042262|||http://purl.uniprot.org/annotation/VAR_023600|||http://purl.uniprot.org/annotation/VAR_068907|||http://purl.uniprot.org/annotation/VSP_044537|||http://purl.uniprot.org/annotation/VSP_044664|||http://purl.uniprot.org/annotation/VSP_053730|||http://purl.uniprot.org/annotation/VSP_053731
http://togogenome.org/gene/9606:ADAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DHV7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Adenosine deaminase-like protein|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285090|||http://purl.uniprot.org/annotation/VSP_024821|||http://purl.uniprot.org/annotation/VSP_042782
http://togogenome.org/gene/9606:DNAJC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KA82|||http://purl.uniprot.org/uniprot/Q13217                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 3|||Flexible linker|||J|||Phosphoserine; by FAM20C|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071045|||http://purl.uniprot.org/annotation/PRO_5014297543
http://togogenome.org/gene/9606:ZDHHC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GR4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||In isoform 2.|||In isoform 3.|||Loss of protein-cysteine S-palmitoyltransferase activity.|||Lumenal|||Palmitoyltransferase ZDHHC12|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212884|||http://purl.uniprot.org/annotation/VAR_023833|||http://purl.uniprot.org/annotation/VAR_023834|||http://purl.uniprot.org/annotation/VSP_006945|||http://purl.uniprot.org/annotation/VSP_016271
http://togogenome.org/gene/9606:FBXO28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 28|||Found in a renal cell carcinoma case; somatic mutation.|||In DEE100.|||In DEE100; unknown pathological significance.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119917|||http://purl.uniprot.org/annotation/VAR_064713|||http://purl.uniprot.org/annotation/VAR_087015|||http://purl.uniprot.org/annotation/VAR_087016|||http://purl.uniprot.org/annotation/VAR_087017|||http://purl.uniprot.org/annotation/VAR_087018|||http://purl.uniprot.org/annotation/VAR_087019|||http://purl.uniprot.org/annotation/VSP_047265|||http://purl.uniprot.org/annotation/VSP_047266
http://togogenome.org/gene/9606:SMPDL3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92484                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acid sphingomyelinase-like phosphodiesterase 3a|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002328|||http://purl.uniprot.org/annotation/VAR_048338|||http://purl.uniprot.org/annotation/VAR_048339|||http://purl.uniprot.org/annotation/VSP_054640
http://togogenome.org/gene/9606:IFI35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80217                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interferon-induced 35 kDa protein|||Leucine-zipper|||NID 1|||NID 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159704|||http://purl.uniprot.org/annotation/VAR_063758|||http://purl.uniprot.org/annotation/VAR_082872|||http://purl.uniprot.org/annotation/VSP_003569
http://togogenome.org/gene/9606:GNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVK2|||http://purl.uniprot.org/uniprot/P62873                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1|||In MRD42.|||In MRD42; also found in patient with hematologic malignancies; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways.|||In MRD42; also found in patients with acute lymphoblastic T-cell leukemia; reduces interaction with GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR and MAPK pathways.|||In MRD42; decreases receptor-driven G protein activation; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance.|||In MRD42; decreases receptor-driven G protein activation; decreases protein abundance; decreases complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit.|||In MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance; no effect on complex formation with gamma subunit.|||In MRD42; decreases receptor-driven G protein activation; decreases trimer formation with alpha and gamma subunit; no effect on protein abundance;no effect on complex formation with gamma subunit.|||In MRD42; decreases receptor-driven G protein activation; increases trimer formation with alpha and gamma subunits; no effect on protein abundance; no effect on complex formation with gamma subunit.|||In MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; decreases trimer formation with alpha and gamma subunit.|||In MRD42; decreases receptor-driven G protein activation; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits.|||In MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with alpha and gamma subunits; no effect on receptor-driven G protein activation.|||In MRD42; unknown pathological significance; no effect on protein abundance; no effect on complex formation with gamma subunit; no effect on trimer formation with apha and gamma subunits; no effect on receptor-driven G protein activation.|||In isoform 2.|||N-acetylserine|||Phosphohistidine|||Phosphoserine|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127687|||http://purl.uniprot.org/annotation/VAR_076643|||http://purl.uniprot.org/annotation/VAR_076644|||http://purl.uniprot.org/annotation/VAR_076645|||http://purl.uniprot.org/annotation/VAR_076646|||http://purl.uniprot.org/annotation/VAR_076647|||http://purl.uniprot.org/annotation/VAR_076648|||http://purl.uniprot.org/annotation/VAR_076649|||http://purl.uniprot.org/annotation/VAR_076650|||http://purl.uniprot.org/annotation/VAR_076651|||http://purl.uniprot.org/annotation/VAR_078279|||http://purl.uniprot.org/annotation/VAR_078280|||http://purl.uniprot.org/annotation/VAR_078281|||http://purl.uniprot.org/annotation/VAR_078282|||http://purl.uniprot.org/annotation/VAR_078283|||http://purl.uniprot.org/annotation/VAR_078284|||http://purl.uniprot.org/annotation/VAR_078285|||http://purl.uniprot.org/annotation/VAR_078286|||http://purl.uniprot.org/annotation/VAR_078287|||http://purl.uniprot.org/annotation/VAR_078288|||http://purl.uniprot.org/annotation/VSP_055232
http://togogenome.org/gene/9606:KIF16B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK74|||http://purl.uniprot.org/uniprot/A0A1B0GTU3|||http://purl.uniprot.org/uniprot/Q96L93                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes PtdIns(3)P-binding.|||Disordered|||FHA|||Impairs plus end-directed microtubule-dependent motor activity, leading to impair EGFR recycling.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1229.|||Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1232.|||Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1229 and A-1232.|||Induces a 30-fold decrease in PtdIns(3)P-binding.|||Induces a 5-fold decrease in PtdIns(3)P-binding and abolishes endosome localization. Induces a 25-fold decrease in PtdIns(3)P-binding; when associated with A-1248.|||Induces a 6-fold decrease in PtdIns(3)P-binding.|||Induces a 7-fold decrease in PtdIns(3)P-binding and abolishes endosome localization. Induces a 25-fold decrease in PtdIns(3)P-binding; when associated with A-1249.|||Kinesin motor|||Kinesin-like protein KIF16B|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125466|||http://purl.uniprot.org/annotation/VAR_019396|||http://purl.uniprot.org/annotation/VAR_019397|||http://purl.uniprot.org/annotation/VAR_019398|||http://purl.uniprot.org/annotation/VAR_036218|||http://purl.uniprot.org/annotation/VAR_049700|||http://purl.uniprot.org/annotation/VAR_065248|||http://purl.uniprot.org/annotation/VSP_010851|||http://purl.uniprot.org/annotation/VSP_010852|||http://purl.uniprot.org/annotation/VSP_015858|||http://purl.uniprot.org/annotation/VSP_041318
http://togogenome.org/gene/9606:FAM171A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMX9|||http://purl.uniprot.org/uniprot/Q5VUB5|||http://purl.uniprot.org/uniprot/Q9Y438                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreases glycosylation levels. Abolishes glycosylation; when associated with A-159.|||Decreases glycosylation levels. Abolishes glycosylation; when associated with A-194.|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation.|||Phosphoserine|||Polar residues|||Protein FAM171A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274263|||http://purl.uniprot.org/annotation/VAR_030220
http://togogenome.org/gene/9606:MIA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JRA6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Mediates interaction with MIA2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C|||Polar residues|||Pro residues|||Proline-rich domain (PRD); mediates interaction with the COPII coat subunits SEC23A and SEC23B|||SEC16A-interacting region (SIR); required for its localization to endoplasmic reticulum exit sites and for its interaction with SEC16A|||SH3|||Transport and Golgi organization protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288998|||http://purl.uniprot.org/annotation/VAR_032546|||http://purl.uniprot.org/annotation/VAR_032547|||http://purl.uniprot.org/annotation/VAR_032548|||http://purl.uniprot.org/annotation/VAR_032549|||http://purl.uniprot.org/annotation/VAR_032550|||http://purl.uniprot.org/annotation/VSP_025860|||http://purl.uniprot.org/annotation/VSP_025861|||http://purl.uniprot.org/annotation/VSP_025862|||http://purl.uniprot.org/annotation/VSP_025863|||http://purl.uniprot.org/annotation/VSP_025864
http://togogenome.org/gene/9606:USP26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXU7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In SPGFX6; unknown pathological significance; decreased protein abundance in patient sperm.|||Loss of deubiquitinase activity. Decreased regulation of androgen receptor signaling pathway.|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080655|||http://purl.uniprot.org/annotation/VAR_063413|||http://purl.uniprot.org/annotation/VAR_063414|||http://purl.uniprot.org/annotation/VAR_063415|||http://purl.uniprot.org/annotation/VAR_063416|||http://purl.uniprot.org/annotation/VAR_063417|||http://purl.uniprot.org/annotation/VAR_063418|||http://purl.uniprot.org/annotation/VAR_088309|||http://purl.uniprot.org/annotation/VAR_088310
http://togogenome.org/gene/9606:FAM240A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVK7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Protein FAM240A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000441719
http://togogenome.org/gene/9606:ZNF57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5HJR3|||http://purl.uniprot.org/uniprot/B4DXX0|||http://purl.uniprot.org/uniprot/G3V131|||http://purl.uniprot.org/uniprot/Q68EA5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 57                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274878|||http://purl.uniprot.org/annotation/VAR_052760|||http://purl.uniprot.org/annotation/VAR_052761|||http://purl.uniprot.org/annotation/VAR_061931
http://togogenome.org/gene/9606:CDC23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJX2                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell division cycle protein 23 homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Inhibits APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-339.|||Inhibits APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-374.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106270|||http://purl.uniprot.org/annotation/VAR_019232|||http://purl.uniprot.org/annotation/VAR_024675|||http://purl.uniprot.org/annotation/VSP_008429|||http://purl.uniprot.org/annotation/VSP_008430|||http://purl.uniprot.org/annotation/VSP_037678
http://togogenome.org/gene/9606:POU5F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7G0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||POU domain, class 5, transcription factor 2|||POU-specific                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100756
http://togogenome.org/gene/9606:GLRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23416                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycine receptor subunit alpha-2|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||In MRXSP.|||In MRXSP; affects channel activity; results in slower channel closing and increased conductance consistent with a gain-of-function effect; results in prolonged inhibitory post-synaptic currents.|||In MRXSP; fails to rescue abnormal outgrowth of spinal motor neuron axons in zebrafish morphants; mutant channels show severely decreased sensitivity to glycine and are unable to respond to physiological glycine levels; results in reduced protein expression; reduced localization to the cell membrane.|||In MRXSP; mutant channels show severely decreased sensitivity to glycine and are unable to respond to physiological glycine levels; results in reduced protein expression; reduced localization to the cell membrane.|||In MRXSP; unknown pathological significance.|||In isoform 3.|||In isoform Alpha-2B.|||N-linked (GlcNAc...) asparagine|||No effect on the kinetics of inhibitory post-synaptic currents.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000416|||http://purl.uniprot.org/annotation/VAR_087062|||http://purl.uniprot.org/annotation/VAR_087063|||http://purl.uniprot.org/annotation/VAR_087064|||http://purl.uniprot.org/annotation/VAR_087065|||http://purl.uniprot.org/annotation/VAR_087066|||http://purl.uniprot.org/annotation/VAR_087067|||http://purl.uniprot.org/annotation/VAR_087068|||http://purl.uniprot.org/annotation/VAR_087069|||http://purl.uniprot.org/annotation/VAR_087070|||http://purl.uniprot.org/annotation/VAR_087071|||http://purl.uniprot.org/annotation/VAR_087072|||http://purl.uniprot.org/annotation/VSP_000082|||http://purl.uniprot.org/annotation/VSP_045465
http://togogenome.org/gene/9606:SLC5A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCU2|||http://purl.uniprot.org/uniprot/B4DUU7|||http://purl.uniprot.org/uniprot/Q2T9H3|||http://purl.uniprot.org/uniprot/Q9GZV3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  40% reduction in choline transmembrane transporter activity; found in 0.06 of Ashkenazi Jews.|||Cytoplasmic|||Decreased choline transmembrane transporter activity, only 20% of wild-type choline uptake activity.|||Decreased choline transmembrane transporter activity, only 5% of wild-type choline uptake activity.|||Decreased protein internalization. Increased choline transmembrane transporter activity.|||Decreased protein internalization; when associated with 531-L-V-532. Increased choline transmembrane transporter activity; when associated with 531-L-V-532.|||Decreased protein internalization; when associated with V-538. Increased choline transmembrane transporter activity; when associated with V-538.|||Dileucine-like motif|||Extracellular|||Helical|||High affinity choline transporter 1|||In CMS20; decreased choline transmembrane transporter activity; no effect on localization at plasma membrane.|||In CMS20; loss of choline transmembrane transporter activity; no effect on localization at plasma membrane.|||In CMS20; no effect on localization at plasma membrane.|||In CMS20; unknown pathological significance.|||Loss of protein internalization to vesicular structures in neurons. Increased choline transmembrane transporter activity.|||Mediates interaction with SEC14L1|||N-linked (GlcNAc...) asparagine|||No change in protein internalization. No change in choline transmembrane transporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105391|||http://purl.uniprot.org/annotation/VAR_020524|||http://purl.uniprot.org/annotation/VAR_077854|||http://purl.uniprot.org/annotation/VAR_077855|||http://purl.uniprot.org/annotation/VAR_077856|||http://purl.uniprot.org/annotation/VAR_077857|||http://purl.uniprot.org/annotation/VAR_077858|||http://purl.uniprot.org/annotation/VAR_077859|||http://purl.uniprot.org/annotation/VAR_077860|||http://purl.uniprot.org/annotation/VAR_077861|||http://purl.uniprot.org/annotation/VAR_077862|||http://purl.uniprot.org/annotation/VAR_077863
http://togogenome.org/gene/9606:CPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15086                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase B|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004371|||http://purl.uniprot.org/annotation/PRO_0000004372|||http://purl.uniprot.org/annotation/VAR_048598
http://togogenome.org/gene/9606:BMPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13873                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bone morphogenetic protein receptor type-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In PPH1.|||In PPH1; abnormal subcellular localization; significant increase in apoptosis of endothelial cells; significant decrease in proliferation of endothelial cells; significant decrease in nitric oxide synthesis by endothelial cells; significant increase in endothelin 1 synthesis by endothelial cells.|||In PPH1; alters alternative splicing of BMPR2.|||In PPH1; changed localization to the plasma membrane.|||In PPH1; complete loss of function.|||In PPH1; leads to constitutive activation of the MAPK14 pathway.|||In PPH1; loss of localization to the plasma membrane; localized to the cytoplasm.|||In PPH1; significant decrease in nitric oxide synthesis by endothelial cells.|||In PPH1; sporadic.|||In PPH1; unknown pathological significance; unchanged subcellular localization.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Unchanged subcellular localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024415|||http://purl.uniprot.org/annotation/VAR_013670|||http://purl.uniprot.org/annotation/VAR_013671|||http://purl.uniprot.org/annotation/VAR_013672|||http://purl.uniprot.org/annotation/VAR_013673|||http://purl.uniprot.org/annotation/VAR_013674|||http://purl.uniprot.org/annotation/VAR_013675|||http://purl.uniprot.org/annotation/VAR_013676|||http://purl.uniprot.org/annotation/VAR_013677|||http://purl.uniprot.org/annotation/VAR_013678|||http://purl.uniprot.org/annotation/VAR_013679|||http://purl.uniprot.org/annotation/VAR_013680|||http://purl.uniprot.org/annotation/VAR_013681|||http://purl.uniprot.org/annotation/VAR_013682|||http://purl.uniprot.org/annotation/VAR_013683|||http://purl.uniprot.org/annotation/VAR_019996|||http://purl.uniprot.org/annotation/VAR_033109|||http://purl.uniprot.org/annotation/VAR_033110|||http://purl.uniprot.org/annotation/VAR_033111|||http://purl.uniprot.org/annotation/VAR_073041|||http://purl.uniprot.org/annotation/VAR_073042|||http://purl.uniprot.org/annotation/VAR_079588|||http://purl.uniprot.org/annotation/VAR_079589|||http://purl.uniprot.org/annotation/VAR_079590|||http://purl.uniprot.org/annotation/VAR_079591|||http://purl.uniprot.org/annotation/VAR_079592|||http://purl.uniprot.org/annotation/VAR_079593|||http://purl.uniprot.org/annotation/VAR_079594|||http://purl.uniprot.org/annotation/VAR_079595|||http://purl.uniprot.org/annotation/VAR_079596|||http://purl.uniprot.org/annotation/VAR_079597|||http://purl.uniprot.org/annotation/VAR_079598|||http://purl.uniprot.org/annotation/VAR_079599|||http://purl.uniprot.org/annotation/VAR_079600|||http://purl.uniprot.org/annotation/VAR_079601|||http://purl.uniprot.org/annotation/VSP_054441|||http://purl.uniprot.org/annotation/VSP_054442
http://togogenome.org/gene/9606:TIMM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y584                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In COXPD43.|||In COXPD43; affects assembly or stability of the translocase.|||Mitochondrial import inner membrane translocase subunit Tim22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210298|||http://purl.uniprot.org/annotation/VAR_084014|||http://purl.uniprot.org/annotation/VAR_084015
http://togogenome.org/gene/9606:STPG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N801                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein STPG4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311684|||http://purl.uniprot.org/annotation/VAR_050715|||http://purl.uniprot.org/annotation/VAR_050716|||http://purl.uniprot.org/annotation/VSP_047926
http://togogenome.org/gene/9606:TRAPPC3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T215                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||S-palmitoyl cysteine|||Trafficking protein particle complex subunit 3-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305083|||http://purl.uniprot.org/annotation/VSP_028222
http://togogenome.org/gene/9606:TNNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13805                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine; by CK2|||Troponin T, slow skeletal muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186168|||http://purl.uniprot.org/annotation/VSP_006639|||http://purl.uniprot.org/annotation/VSP_006640
http://togogenome.org/gene/9606:NDUFAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q330K2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In MC1DN17.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||NADH dehydrogenase (ubiquinone) complex I, assembly factor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291772|||http://purl.uniprot.org/annotation/VAR_047770|||http://purl.uniprot.org/annotation/VAR_076272|||http://purl.uniprot.org/annotation/VAR_076273|||http://purl.uniprot.org/annotation/VAR_076274|||http://purl.uniprot.org/annotation/VAR_076275|||http://purl.uniprot.org/annotation/VAR_076276|||http://purl.uniprot.org/annotation/VAR_084382|||http://purl.uniprot.org/annotation/VSP_026230|||http://purl.uniprot.org/annotation/VSP_026231|||http://purl.uniprot.org/annotation/VSP_026232
http://togogenome.org/gene/9606:CYB5R4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L1T6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CS|||Cytochrome b5 heme-binding|||Cytochrome b5 reductase 4|||Disordered|||FAD-binding FR-type|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Polar residues|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287556|||http://purl.uniprot.org/annotation/VAR_032323|||http://purl.uniprot.org/annotation/VAR_032324|||http://purl.uniprot.org/annotation/VAR_032325|||http://purl.uniprot.org/annotation/VAR_036240|||http://purl.uniprot.org/annotation/VAR_036241|||http://purl.uniprot.org/annotation/VAR_047967|||http://purl.uniprot.org/annotation/VAR_047968|||http://purl.uniprot.org/annotation/VAR_047969
http://togogenome.org/gene/9606:MT1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BRY8|||http://purl.uniprot.org/uniprot/P04733                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1F|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197237
http://togogenome.org/gene/9606:IGBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78318                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PPP2CA.|||Basic and acidic residues|||Cleavage; by calpain|||Disordered|||Immunoglobulin-binding protein 1|||Interaction with MID1|||Interaction with PPP2CA|||N-acetylalanine|||N6-acetyllysine|||Removed|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218618|||http://purl.uniprot.org/annotation/VAR_049570
http://togogenome.org/gene/9606:HK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52790                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Hexokinase 1|||Hexokinase 2|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||Hexokinase-3|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197590|||http://purl.uniprot.org/annotation/VAR_034004|||http://purl.uniprot.org/annotation/VAR_036186|||http://purl.uniprot.org/annotation/VAR_036187
http://togogenome.org/gene/9606:HCRTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMV7|||http://purl.uniprot.org/uniprot/O43613                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes response to orexin-A.|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for responses to orexin|||N-linked (GlcNAc...) asparagine|||Orexin/Hypocretin receptor type 1|||Required for response to orexin-A|||Strongly impairs response to orexin-A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069984|||http://purl.uniprot.org/annotation/VAR_022063|||http://purl.uniprot.org/annotation/VAR_033480|||http://purl.uniprot.org/annotation/VAR_044505|||http://purl.uniprot.org/annotation/VAR_044506
http://togogenome.org/gene/9606:PKLR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30613                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PKHYP.|||In PKRD.|||In PKRD; Amish; no conformational change.|||In PKRD; Aomori.|||In PKRD; Beaujon.|||In PKRD; Brescia.|||In PKRD; Complete loss in the responsiveness to fructose 1,6-bisphosphate, FBP.|||In PKRD; Conakry.|||In PKRD; Dordrecht.|||In PKRD; Fukushima/Maebashi/Sendai.|||In PKRD; Hadano.|||In PKRD; Hirosaki.|||In PKRD; Hong Kong.|||In PKRD; Kamata.|||In PKRD; Katsushika.|||In PKRD; Linz.|||In PKRD; Mantova; almost complete inactivation.|||In PKRD; Moriguchi.|||In PKRD; Naniwa.|||In PKRD; Osaka.|||In PKRD; Paris.|||In PKRD; Parma.|||In PKRD; Sapporo.|||In PKRD; Sassari.|||In PKRD; Tjaereborg; unstability of the protein and decrease in catalytic activity.|||In PKRD; Tokyo/Beirut; no conformational change.|||In PKRD; Val de Marne.|||In PKRD; instability of the protein.|||In PKRD; loss of catalytical activity.|||In PKRD; no conformational change.|||In isoform L-type.|||Phosphoserine|||Pyruvate kinase PKLR|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112094|||http://purl.uniprot.org/annotation/VAR_004028|||http://purl.uniprot.org/annotation/VAR_004029|||http://purl.uniprot.org/annotation/VAR_004030|||http://purl.uniprot.org/annotation/VAR_004031|||http://purl.uniprot.org/annotation/VAR_004032|||http://purl.uniprot.org/annotation/VAR_004033|||http://purl.uniprot.org/annotation/VAR_004034|||http://purl.uniprot.org/annotation/VAR_004035|||http://purl.uniprot.org/annotation/VAR_004036|||http://purl.uniprot.org/annotation/VAR_004037|||http://purl.uniprot.org/annotation/VAR_004038|||http://purl.uniprot.org/annotation/VAR_004039|||http://purl.uniprot.org/annotation/VAR_004040|||http://purl.uniprot.org/annotation/VAR_004041|||http://purl.uniprot.org/annotation/VAR_004042|||http://purl.uniprot.org/annotation/VAR_004043|||http://purl.uniprot.org/annotation/VAR_004044|||http://purl.uniprot.org/annotation/VAR_004045|||http://purl.uniprot.org/annotation/VAR_004046|||http://purl.uniprot.org/annotation/VAR_004047|||http://purl.uniprot.org/annotation/VAR_004048|||http://purl.uniprot.org/annotation/VAR_004049|||http://purl.uniprot.org/annotation/VAR_004050|||http://purl.uniprot.org/annotation/VAR_004051|||http://purl.uniprot.org/annotation/VAR_004052|||http://purl.uniprot.org/annotation/VAR_004053|||http://purl.uniprot.org/annotation/VAR_004054|||http://purl.uniprot.org/annotation/VAR_004055|||http://purl.uniprot.org/annotation/VAR_004056|||http://purl.uniprot.org/annotation/VAR_004057|||http://purl.uniprot.org/annotation/VAR_004058|||http://purl.uniprot.org/annotation/VAR_004059|||http://purl.uniprot.org/annotation/VAR_004060|||http://purl.uniprot.org/annotation/VAR_004061|||http://purl.uniprot.org/annotation/VAR_004062|||http://purl.uniprot.org/annotation/VAR_004063|||http://purl.uniprot.org/annotation/VAR_004064|||http://purl.uniprot.org/annotation/VAR_004065|||http://purl.uniprot.org/annotation/VAR_004066|||http://purl.uniprot.org/annotation/VAR_004067|||http://purl.uniprot.org/annotation/VAR_004068|||http://purl.uniprot.org/annotation/VAR_004069|||http://purl.uniprot.org/annotation/VAR_004070|||http://purl.uniprot.org/annotation/VAR_004071|||http://purl.uniprot.org/annotation/VAR_004072|||http://purl.uniprot.org/annotation/VAR_004073|||http://purl.uniprot.org/annotation/VAR_004074|||http://purl.uniprot.org/annotation/VAR_004075|||http://purl.uniprot.org/annotation/VAR_004076|||http://purl.uniprot.org/annotation/VAR_011435|||http://purl.uniprot.org/annotation/VAR_011436|||http://purl.uniprot.org/annotation/VAR_011437|||http://purl.uniprot.org/annotation/VAR_011438|||http://purl.uniprot.org/annotation/VAR_011439|||http://purl.uniprot.org/annotation/VAR_011440|||http://purl.uniprot.org/annotation/VAR_011441|||http://purl.uniprot.org/annotation/VAR_011442|||http://purl.uniprot.org/annotation/VAR_011443|||http://purl.uniprot.org/annotation/VAR_011444|||http://purl.uniprot.org/annotation/VAR_011445|||http://purl.uniprot.org/annotation/VAR_011446|||http://purl.uniprot.org/annotation/VAR_011447|||http://purl.uniprot.org/annotation/VAR_011448|||http://purl.uniprot.org/annotation/VAR_011449|||http://purl.uniprot.org/annotation/VAR_011450|||http://purl.uniprot.org/annotation/VAR_011451|||http://purl.uniprot.org/annotation/VAR_011452|||http://purl.uniprot.org/annotation/VAR_011453|||http://purl.uniprot.org/annotation/VAR_011454|||http://purl.uniprot.org/annotation/VAR_011455|||http://purl.uniprot.org/annotation/VAR_011456|||http://purl.uniprot.org/annotation/VAR_011457|||http://purl.uniprot.org/annotation/VAR_011458|||http://purl.uniprot.org/annotation/VAR_011459|||http://purl.uniprot.org/annotation/VAR_011460|||http://purl.uniprot.org/annotation/VAR_011461|||http://purl.uniprot.org/annotation/VAR_011462|||http://purl.uniprot.org/annotation/VAR_011463|||http://purl.uniprot.org/annotation/VAR_011464|||http://purl.uniprot.org/annotation/VAR_011465|||http://purl.uniprot.org/annotation/VAR_011466|||http://purl.uniprot.org/annotation/VAR_011467|||http://purl.uniprot.org/annotation/VAR_011468|||http://purl.uniprot.org/annotation/VAR_011469|||http://purl.uniprot.org/annotation/VAR_011470|||http://purl.uniprot.org/annotation/VAR_011471|||http://purl.uniprot.org/annotation/VAR_011472|||http://purl.uniprot.org/annotation/VAR_011473|||http://purl.uniprot.org/annotation/VAR_011474|||http://purl.uniprot.org/annotation/VAR_011475|||http://purl.uniprot.org/annotation/VAR_011476|||http://purl.uniprot.org/annotation/VAR_011477|||http://purl.uniprot.org/annotation/VAR_011478|||http://purl.uniprot.org/annotation/VAR_011479|||http://purl.uniprot.org/annotation/VAR_011480|||http://purl.uniprot.org/annotation/VAR_011481|||http://purl.uniprot.org/annotation/VAR_011482|||http://purl.uniprot.org/annotation/VAR_018848|||http://purl.uniprot.org/annotation/VAR_058467|||http://purl.uniprot.org/annotation/VAR_058468|||http://purl.uniprot.org/annotation/VAR_058469|||http://purl.uniprot.org/annotation/VAR_058470|||http://purl.uniprot.org/annotation/VAR_058471|||http://purl.uniprot.org/annotation/VAR_058472|||http://purl.uniprot.org/annotation/VAR_058473|||http://purl.uniprot.org/annotation/VAR_058474|||http://purl.uniprot.org/annotation/VAR_058475|||http://purl.uniprot.org/annotation/VAR_058476|||http://purl.uniprot.org/annotation/VSP_002883
http://togogenome.org/gene/9606:LAMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25391                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Domain II and I|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 14; first part|||Laminin EGF-like 14; second part|||Laminin EGF-like 15|||Laminin EGF-like 16|||Laminin EGF-like 17|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; first part|||Laminin EGF-like 5; second part|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin IV type A 1|||Laminin IV type A 2|||Laminin N-terminal|||Laminin subunit alpha-1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017054|||http://purl.uniprot.org/annotation/VAR_056132|||http://purl.uniprot.org/annotation/VAR_056133|||http://purl.uniprot.org/annotation/VAR_056134|||http://purl.uniprot.org/annotation/VAR_056135|||http://purl.uniprot.org/annotation/VAR_056136|||http://purl.uniprot.org/annotation/VAR_056137|||http://purl.uniprot.org/annotation/VAR_056138|||http://purl.uniprot.org/annotation/VAR_056139|||http://purl.uniprot.org/annotation/VAR_060785|||http://purl.uniprot.org/annotation/VAR_060786|||http://purl.uniprot.org/annotation/VAR_060787|||http://purl.uniprot.org/annotation/VAR_060788|||http://purl.uniprot.org/annotation/VAR_061347
http://togogenome.org/gene/9606:SNRPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62314                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of interaction with CLNS1A.|||Required for interaction with SMN1|||Sm|||Small nuclear ribonucleoprotein Sm D1|||Sufficient for interaction with CLNS1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122201
http://togogenome.org/gene/9606:KCNMB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16558                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated potassium channel subunit beta-1|||Cytoplasmic|||Extracellular|||Has a protective effect against diastolic hypertension.|||Helical; Name=1|||Helical; Name=2|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187046|||http://purl.uniprot.org/annotation/VAR_019325|||http://purl.uniprot.org/annotation/VAR_047009|||http://purl.uniprot.org/annotation/VSP_009822|||http://purl.uniprot.org/annotation/VSP_009823
http://togogenome.org/gene/9606:EXOSC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXG8|||http://purl.uniprot.org/uniprot/Q06265                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARE binding|||Abolishes interaction with SETX.|||Basic and acidic residues|||Basic residues|||Disordered|||Exoribonuclease phosphorolytic|||Exosome complex component RRP45|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In PCH1D; reduced EXOSC9 and exosome levels in patient cells.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N6-acetyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139971|||http://purl.uniprot.org/annotation/VAR_014924|||http://purl.uniprot.org/annotation/VAR_051867|||http://purl.uniprot.org/annotation/VAR_081052|||http://purl.uniprot.org/annotation/VAR_081053|||http://purl.uniprot.org/annotation/VSP_025555|||http://purl.uniprot.org/annotation/VSP_025556
http://togogenome.org/gene/9606:ZWINT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95229                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with NDC80 and ZW10|||Polar residues|||ZW10 interactor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066594|||http://purl.uniprot.org/annotation/VAR_028783|||http://purl.uniprot.org/annotation/VAR_051505|||http://purl.uniprot.org/annotation/VSP_047660
http://togogenome.org/gene/9606:COL23A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen alpha-1(XXIII) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245226|||http://purl.uniprot.org/annotation/VAR_026964|||http://purl.uniprot.org/annotation/VSP_019627|||http://purl.uniprot.org/annotation/VSP_019628|||http://purl.uniprot.org/annotation/VSP_019629|||http://purl.uniprot.org/annotation/VSP_019630|||http://purl.uniprot.org/annotation/VSP_019631
http://togogenome.org/gene/9606:PHF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG57|||http://purl.uniprot.org/uniprot/O94880                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||PHD finger protein 14|||PHD-type|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059306|||http://purl.uniprot.org/annotation/VAR_018480|||http://purl.uniprot.org/annotation/VSP_061645|||http://purl.uniprot.org/annotation/VSP_061646|||http://purl.uniprot.org/annotation/VSP_061647
http://togogenome.org/gene/9606:MMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15546                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Monocyte to macrophage differentiation factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218854
http://togogenome.org/gene/9606:YPEL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NS1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Phosphothreonine|||Phosphotyrosine|||Protein yippee-like 4|||Yippee                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212392
http://togogenome.org/gene/9606:OR6C65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW71|||http://purl.uniprot.org/uniprot/A6NJZ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C65                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310466|||http://purl.uniprot.org/annotation/VAR_037049|||http://purl.uniprot.org/annotation/VAR_037050
http://togogenome.org/gene/9606:TRMU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75648                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acts as a disease modifier in patients with aminoglycoside-induced deafness and a mutation in mitochondrial 12S rRNA; affects tRNA processing by decreasing thiolation and increasing aminoacylation of tRNAs; the mutant has lower thermal stability than wild-type; does not affect import in the mitochondria.|||Cysteine persulfide intermediate|||Disordered|||In LFIT.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||Interaction with tRNA|||Interaction with target base in tRNA|||Loss of activity.|||Mitochondrial tRNA-specific 2-thiouridylase 1|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121708|||http://purl.uniprot.org/annotation/VAR_027268|||http://purl.uniprot.org/annotation/VAR_046380|||http://purl.uniprot.org/annotation/VAR_046381|||http://purl.uniprot.org/annotation/VAR_046382|||http://purl.uniprot.org/annotation/VAR_063428|||http://purl.uniprot.org/annotation/VAR_063429|||http://purl.uniprot.org/annotation/VAR_063430|||http://purl.uniprot.org/annotation/VAR_063431|||http://purl.uniprot.org/annotation/VSP_035391|||http://purl.uniprot.org/annotation/VSP_035392|||http://purl.uniprot.org/annotation/VSP_035393|||http://purl.uniprot.org/annotation/VSP_035394|||http://purl.uniprot.org/annotation/VSP_035395
http://togogenome.org/gene/9606:KRT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19013                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In WSN1.|||In allele K4A1.|||In alleles K4A1 and K4A2.|||Keratin, type II cytoskeletal 4|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063722|||http://purl.uniprot.org/annotation/VAR_003869|||http://purl.uniprot.org/annotation/VAR_012845|||http://purl.uniprot.org/annotation/VAR_016038|||http://purl.uniprot.org/annotation/VAR_083057
http://togogenome.org/gene/9606:NARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPX5|||http://purl.uniprot.org/uniprot/Q96I59|||http://purl.uniprot.org/uniprot/Q9H5H1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Aminoacyl-transfer RNA synthetases class-II family profile|||In COXPD24.|||In COXPD24; does not form homodimers; does not affect localization to mitochondrion.|||In COXPD24; unknown pathological significance; no effect on homodimer formation; does not affect localization to mitochondrion.|||In DFNB94; probable loss-of-function variant; unable to rescue mitochondrial respiratory chain defects in NARS2 null fibroblasts; does not affect homodimerization; does not affect localization to mitochondrion.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Probable asparagine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250722|||http://purl.uniprot.org/annotation/VAR_052636|||http://purl.uniprot.org/annotation/VAR_073250|||http://purl.uniprot.org/annotation/VAR_073723|||http://purl.uniprot.org/annotation/VAR_073724|||http://purl.uniprot.org/annotation/VAR_082311|||http://purl.uniprot.org/annotation/VAR_086708|||http://purl.uniprot.org/annotation/VAR_086709|||http://purl.uniprot.org/annotation/VSP_054120
http://togogenome.org/gene/9606:HYOU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5T6|||http://purl.uniprot.org/uniprot/A0A494C039|||http://purl.uniprot.org/uniprot/B3KXH0|||http://purl.uniprot.org/uniprot/B7Z602|||http://purl.uniprot.org/uniprot/B7Z766|||http://purl.uniprot.org/uniprot/Q6IN67|||http://purl.uniprot.org/uniprot/Q9Y4L1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hypoxia up-regulated protein 1|||In IMD59; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013538|||http://purl.uniprot.org/annotation/PRO_5002790417|||http://purl.uniprot.org/annotation/PRO_5002863969|||http://purl.uniprot.org/annotation/PRO_5004274750|||http://purl.uniprot.org/annotation/PRO_5036073198|||http://purl.uniprot.org/annotation/PRO_5040001568|||http://purl.uniprot.org/annotation/VAR_081773|||http://purl.uniprot.org/annotation/VAR_081774|||http://purl.uniprot.org/annotation/VSP_056364|||http://purl.uniprot.org/annotation/VSP_056365|||http://purl.uniprot.org/annotation/VSP_056366
http://togogenome.org/gene/9606:SDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1S6|||http://purl.uniprot.org/uniprot/P31431                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Neurexin/syndecan/glycophorin C|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Syndecan-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033511|||http://purl.uniprot.org/annotation/VAR_021851|||http://purl.uniprot.org/annotation/VSP_044449
http://togogenome.org/gene/9606:HACD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ81                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In CMYP11.|||In CMYP11; loss of very-long-chain 3-hydroxyacyl-CoA dehydratase activity.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349315|||http://purl.uniprot.org/annotation/VAR_046366|||http://purl.uniprot.org/annotation/VAR_046367|||http://purl.uniprot.org/annotation/VAR_046368|||http://purl.uniprot.org/annotation/VAR_046369|||http://purl.uniprot.org/annotation/VAR_087514|||http://purl.uniprot.org/annotation/VAR_087515|||http://purl.uniprot.org/annotation/VSP_035363|||http://purl.uniprot.org/annotation/VSP_035364
http://togogenome.org/gene/9606:ZNF648                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T619                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Polar residues|||Zinc finger protein 648                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252162|||http://purl.uniprot.org/annotation/VAR_033585|||http://purl.uniprot.org/annotation/VAR_052887
http://togogenome.org/gene/9606:RND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92730                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with UBXD5.|||Cysteine methyl ester|||Effector region|||Impairs interaction with UBXD5.|||Removed in mature form|||Rho-related GTP-binding protein Rho6|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198874|||http://purl.uniprot.org/annotation/PRO_0000281226|||http://purl.uniprot.org/annotation/VAR_020188
http://togogenome.org/gene/9606:RBBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09028                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased interaction with ZNF827.|||Decreased interaction with ZNF827; when associated with A-231.|||Decreased interaction with ZNF827; when associated with A-277.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone-binding protein RBBP4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ARMC12|||Loss of interaction with ARMC12.|||Loss of interaction with ZNF827 and loss of localization to telomeres.|||Loss of interaction with ZNF827 and loss of localization to telomeres; when associated with A-126 and A-128.|||Loss of interaction with ZNF827 and loss of localization to telomeres; when associated with A-126 and A-179.|||Loss of interaction with ZNF827 and loss of localization to telomeres; when associated with A-128 and A-179.|||Loss of interaction with ZNF827 and loss of localization to telomeres; when associated with A-43.|||Loss of interaction with ZNF827 and loss of localization to telomeres; when associated with A-73.|||Loss of interaction with ZNF827.|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051186|||http://purl.uniprot.org/annotation/VSP_040087|||http://purl.uniprot.org/annotation/VSP_040088|||http://purl.uniprot.org/annotation/VSP_040089
http://togogenome.org/gene/9606:ACBD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2A7|||http://purl.uniprot.org/uniprot/B7Z2R7|||http://purl.uniprot.org/uniprot/B7Z9D0|||http://purl.uniprot.org/uniprot/Q5T8D3|||http://purl.uniprot.org/uniprot/Q8NCM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  ACB|||Acyl-CoA-binding domain-containing protein 5|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287377|||http://purl.uniprot.org/annotation/VAR_032301|||http://purl.uniprot.org/annotation/VSP_025446|||http://purl.uniprot.org/annotation/VSP_025447|||http://purl.uniprot.org/annotation/VSP_025448|||http://purl.uniprot.org/annotation/VSP_025449
http://togogenome.org/gene/9606:EBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QYX0|||http://purl.uniprot.org/uniprot/Q15125                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase|||EXPERA|||Helical|||In CDPX2.|||In MEND; patients have increased concentrations of plasma 8(9)-cholestenol, 8-dehydrocholesterol and 7-dehydrocholesterol; probable hypomorphic mutation.|||In MEND; patients have increased concentrations of plasma 8-dehydrocholesterol and 8(9)-cholestenol; probable hypomorphic mutation.|||In MEND; patients have increased plasma levels of 8(9)-cholestenol; probable hypomorphic mutation.|||In MEND; patients have mildly increased concentrations of plasma 8(9)-cholestenol and 8-dehydrocholesterol; probable hypomorphic mutation.|||N-acetylthreonine|||No effect on catalytic activity.|||Reduces catalytic activity to less than 10% of wild-type.|||Reduces catalytic activity to less than 2% of wild-type.|||Reduces catalytic activity to less than 35% of wild-type.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174342|||http://purl.uniprot.org/annotation/VAR_012105|||http://purl.uniprot.org/annotation/VAR_012106|||http://purl.uniprot.org/annotation/VAR_012107|||http://purl.uniprot.org/annotation/VAR_012108|||http://purl.uniprot.org/annotation/VAR_074633|||http://purl.uniprot.org/annotation/VAR_074634|||http://purl.uniprot.org/annotation/VAR_074635|||http://purl.uniprot.org/annotation/VAR_074636|||http://purl.uniprot.org/annotation/VAR_074637
http://togogenome.org/gene/9606:OR13C8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVC7|||http://purl.uniprot.org/uniprot/Q8NGS7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150735|||http://purl.uniprot.org/annotation/VAR_034307
http://togogenome.org/gene/9606:VEPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14D04                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with TGFBR1|||PH|||Ventricular zone-expressed PH domain-containing protein homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297955|||http://purl.uniprot.org/annotation/VAR_034692|||http://purl.uniprot.org/annotation/VAR_034693|||http://purl.uniprot.org/annotation/VAR_034694|||http://purl.uniprot.org/annotation/VAR_034695|||http://purl.uniprot.org/annotation/VAR_034696|||http://purl.uniprot.org/annotation/VAR_034697|||http://purl.uniprot.org/annotation/VAR_034698|||http://purl.uniprot.org/annotation/VAR_061683|||http://purl.uniprot.org/annotation/VSP_027431|||http://purl.uniprot.org/annotation/VSP_027432|||http://purl.uniprot.org/annotation/VSP_027433|||http://purl.uniprot.org/annotation/VSP_047655|||http://purl.uniprot.org/annotation/VSP_047656
http://togogenome.org/gene/9606:SMAD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43541                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes monoubiquitination by UBE2O.|||Dimethylated arginine; alternate|||Disordered|||Found in a patient with congenital mitral valve prolapse.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In AOVD2.|||In AOVD2; decreased inhibition of BMP signaling pathway.|||In AOVD2; unknown pathological significance.|||In CRS7; associated with disease susceptibility.|||In CRS7; associated with disease susceptibility; de novo mutation.|||In CRS7; unknown pathological significance.|||In RUS; associated with disease susceptibility.|||In RUS; unknown pathological significance.|||In isoform B.|||In isoform D.|||Loss of SMAD1-binding and of inhibition of BMP-SMAD1 signaling. No effect on interaction with BMPR1B and TGFBR1.|||Loss of in vitro phosphorylation by PRKX.|||Loss of interaction with BMPR1B, TGFBR1 and SMAD1.|||MH1|||MH2|||Mothers against decapentaplegic homolog 6|||Omega-N-methylarginine; alternate|||Phosphoserine; by PRKX; in vitro|||Probable disease-associated variant found in a patient with radioulnar synostosis and macrocephaly; associated with disease susceptibility.|||Probable disease-associated variant found in a patient with radioulnar synostosis and microcephaly; associated with disease susceptibility.|||Probable disease-associated variant found in a patient with radioulnar synostosis, pectus carinatum and macrocephaly.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090869|||http://purl.uniprot.org/annotation/VAR_068074|||http://purl.uniprot.org/annotation/VAR_068075|||http://purl.uniprot.org/annotation/VAR_068076|||http://purl.uniprot.org/annotation/VAR_077592|||http://purl.uniprot.org/annotation/VAR_077593|||http://purl.uniprot.org/annotation/VAR_077594|||http://purl.uniprot.org/annotation/VAR_077595|||http://purl.uniprot.org/annotation/VAR_078924|||http://purl.uniprot.org/annotation/VAR_078925|||http://purl.uniprot.org/annotation/VAR_078926|||http://purl.uniprot.org/annotation/VAR_078927|||http://purl.uniprot.org/annotation/VAR_078928|||http://purl.uniprot.org/annotation/VAR_084468|||http://purl.uniprot.org/annotation/VAR_084469|||http://purl.uniprot.org/annotation/VAR_084470|||http://purl.uniprot.org/annotation/VAR_084471|||http://purl.uniprot.org/annotation/VAR_084472|||http://purl.uniprot.org/annotation/VAR_084473|||http://purl.uniprot.org/annotation/VAR_084474|||http://purl.uniprot.org/annotation/VAR_084475|||http://purl.uniprot.org/annotation/VAR_084476|||http://purl.uniprot.org/annotation/VAR_084477|||http://purl.uniprot.org/annotation/VAR_084478|||http://purl.uniprot.org/annotation/VAR_084479|||http://purl.uniprot.org/annotation/VAR_084480|||http://purl.uniprot.org/annotation/VAR_084481|||http://purl.uniprot.org/annotation/VAR_084482|||http://purl.uniprot.org/annotation/VAR_084483|||http://purl.uniprot.org/annotation/VAR_084484|||http://purl.uniprot.org/annotation/VAR_084485|||http://purl.uniprot.org/annotation/VAR_084486|||http://purl.uniprot.org/annotation/VAR_084487|||http://purl.uniprot.org/annotation/VSP_006179|||http://purl.uniprot.org/annotation/VSP_006180|||http://purl.uniprot.org/annotation/VSP_035489|||http://purl.uniprot.org/annotation/VSP_035490
http://togogenome.org/gene/9606:SOCS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9R6|||http://purl.uniprot.org/uniprot/Q8WXH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||SH2|||SOCS box|||Suppressor of cytokine signaling 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181247
http://togogenome.org/gene/9606:GPNMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14956|||http://purl.uniprot.org/uniprot/Q96F58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In PLCA3.|||In PLCA3; may be expressed at much lower levels than wild-type protein; mislocalized to the endoplasmic reticulum and nuclear envelope.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PKD|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane glycoprotein NMB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024709|||http://purl.uniprot.org/annotation/PRO_5014589243|||http://purl.uniprot.org/annotation/VAR_012076|||http://purl.uniprot.org/annotation/VAR_012077|||http://purl.uniprot.org/annotation/VAR_036262|||http://purl.uniprot.org/annotation/VAR_036263|||http://purl.uniprot.org/annotation/VAR_050603|||http://purl.uniprot.org/annotation/VAR_050604|||http://purl.uniprot.org/annotation/VAR_050605|||http://purl.uniprot.org/annotation/VAR_080643|||http://purl.uniprot.org/annotation/VAR_080644|||http://purl.uniprot.org/annotation/VSP_013001
http://togogenome.org/gene/9606:ARID3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 3C|||Acidic residues|||Disordered|||Polar residues|||Pro residues|||REKLES                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333001|||http://purl.uniprot.org/annotation/VAR_043033|||http://purl.uniprot.org/annotation/VAR_043034
http://togogenome.org/gene/9606:KRT31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15323                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha1|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063684|||http://purl.uniprot.org/annotation/VAR_046989|||http://purl.uniprot.org/annotation/VAR_046990|||http://purl.uniprot.org/annotation/VAR_046991
http://togogenome.org/gene/9606:FBXL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ME1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 18|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119867|||http://purl.uniprot.org/annotation/VAR_055800|||http://purl.uniprot.org/annotation/VAR_087450|||http://purl.uniprot.org/annotation/VAR_087451|||http://purl.uniprot.org/annotation/VSP_061754|||http://purl.uniprot.org/annotation/VSP_061755|||http://purl.uniprot.org/annotation/VSP_061756|||http://purl.uniprot.org/annotation/VSP_061757|||http://purl.uniprot.org/annotation/VSP_061758|||http://purl.uniprot.org/annotation/VSP_061759
http://togogenome.org/gene/9606:PPARGC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM40|||http://purl.uniprot.org/uniprot/Q86YN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes DNA transcriptional activity when missing|||Acidic residues|||Basic and acidic residues|||Disordered|||HCFC1-binding-motif (HBM)|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||LXXLL motif 1|||LXXLL motif 2|||Peroxisome proliferator-activated receptor gamma coactivator 1-beta|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||Reduces DNA transcriptional activity.|||Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 155-AAQKAA-160.|||Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 343-AREAA-347.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240158|||http://purl.uniprot.org/annotation/VAR_026698|||http://purl.uniprot.org/annotation/VAR_026699|||http://purl.uniprot.org/annotation/VAR_026700|||http://purl.uniprot.org/annotation/VAR_026701|||http://purl.uniprot.org/annotation/VSP_019299|||http://purl.uniprot.org/annotation/VSP_019300|||http://purl.uniprot.org/annotation/VSP_019301|||http://purl.uniprot.org/annotation/VSP_043374
http://togogenome.org/gene/9606:NECAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Adaptin ear-binding coat-associated protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||WXXF motif 1|||WXXF motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213071|||http://purl.uniprot.org/annotation/VAR_034154|||http://purl.uniprot.org/annotation/VSP_013234|||http://purl.uniprot.org/annotation/VSP_013235|||http://purl.uniprot.org/annotation/VSP_013236|||http://purl.uniprot.org/annotation/VSP_041726
http://togogenome.org/gene/9606:TSPAN13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95857|||http://purl.uniprot.org/uniprot/Q6FGK0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Tetraspanin-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219258
http://togogenome.org/gene/9606:RAB27A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51159                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SYTL2.|||Cysteine methyl ester|||Effector region|||GDP-locked. Abolishes interaction with UNC13D and localization to lysosomes. Increases interaction with DENND10. Disrupts late endocytic pathway homeostasis.|||GTP-locked. decreases interaction with DENND10.|||In GS2; does not affect GTP binding; cannot interact with MLPH; significant reduction in interaction with UNC13D; abolishes localization to lysosomes.|||In GS2; interferes with melanosome transport.|||In GS2; strongly affects GTP binding; cannot interact with MLPH.|||In isoform Short.|||N-acetylserine|||Phosphoserine|||Ras-related protein Rab-27A|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121221|||http://purl.uniprot.org/annotation/VAR_010654|||http://purl.uniprot.org/annotation/VAR_011334|||http://purl.uniprot.org/annotation/VAR_011335|||http://purl.uniprot.org/annotation/VAR_028206|||http://purl.uniprot.org/annotation/VAR_028207|||http://purl.uniprot.org/annotation/VAR_028208|||http://purl.uniprot.org/annotation/VSP_005529
http://togogenome.org/gene/9606:CCRL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8C0|||http://purl.uniprot.org/uniprot/O00421                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor-like 2|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236798|||http://purl.uniprot.org/annotation/VAR_026488|||http://purl.uniprot.org/annotation/VAR_026489|||http://purl.uniprot.org/annotation/VAR_026490|||http://purl.uniprot.org/annotation/VAR_049385|||http://purl.uniprot.org/annotation/VSP_018584
http://togogenome.org/gene/9606:TAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSY6|||http://purl.uniprot.org/uniprot/A0A8I5KV60|||http://purl.uniprot.org/uniprot/A0A8I5QJR0|||http://purl.uniprot.org/uniprot/B3KMD8|||http://purl.uniprot.org/uniprot/Q6P1X5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||In NEDFCF.|||In NEDFCF; unknown pathological significance.|||Phosphoserine|||Polar residues|||Transcription initiation factor TFIID subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252424|||http://purl.uniprot.org/annotation/VAR_027854|||http://purl.uniprot.org/annotation/VAR_027855|||http://purl.uniprot.org/annotation/VAR_027856|||http://purl.uniprot.org/annotation/VAR_027857|||http://purl.uniprot.org/annotation/VAR_057263|||http://purl.uniprot.org/annotation/VAR_070945|||http://purl.uniprot.org/annotation/VAR_070946|||http://purl.uniprot.org/annotation/VAR_070947
http://togogenome.org/gene/9606:MARK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L34                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||KA1|||MAP/microtubule affinity-regulating kinase 4|||Mimicks phosphorylation state, leading to increased activity. Decreases mTORC1 activity.|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086307|||http://purl.uniprot.org/annotation/VAR_040766|||http://purl.uniprot.org/annotation/VAR_040767|||http://purl.uniprot.org/annotation/VSP_004946
http://togogenome.org/gene/9606:RASGRP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDF6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||EF-hand|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of cell membrane targeting.|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||RAS guanyl-releasing protein 4|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315213|||http://purl.uniprot.org/annotation/VAR_038144|||http://purl.uniprot.org/annotation/VAR_038145|||http://purl.uniprot.org/annotation/VAR_038146|||http://purl.uniprot.org/annotation/VAR_038147|||http://purl.uniprot.org/annotation/VAR_038148|||http://purl.uniprot.org/annotation/VAR_057172|||http://purl.uniprot.org/annotation/VSP_030479|||http://purl.uniprot.org/annotation/VSP_030480|||http://purl.uniprot.org/annotation/VSP_043138|||http://purl.uniprot.org/annotation/VSP_043176|||http://purl.uniprot.org/annotation/VSP_043392|||http://purl.uniprot.org/annotation/VSP_046907|||http://purl.uniprot.org/annotation/VSP_046908
http://togogenome.org/gene/9606:C19orf53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNZ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Leydig cell tumor 10 kDa protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084343|||http://purl.uniprot.org/annotation/VAR_053783
http://togogenome.org/gene/9606:RUBCNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRV7|||http://purl.uniprot.org/uniprot/B7ZBN5|||http://purl.uniprot.org/uniprot/Q9H714                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished acetylation by KAT5/TIP60 and abolished ability to promote autophagosome maturation; when associated with R-483, R-523, R-533 and R-573.|||Abolished acetylation by KAT5/TIP60 and abolished ability to promote autophagosome maturation; when associated with R-483, R-523, R-533 and R-633.|||Abolished acetylation by KAT5/TIP60 and abolished ability to promote autophagosome maturation; when associated with R-483, R-523, R-573 and R-633.|||Abolished acetylation by KAT5/TIP60 and abolished ability to promote autophagosome maturation; when associated with R-483, R-533, R-573 and R-633.|||Abolished acetylation by KAT5/TIP60 and abolished ability to promote autophagosome maturation; when associated with R-523, R-533, R-573 and R-633.|||Abolished phosphorylation by MTOR, leading to promote interaction with STX17 and autophagosome maturation.|||Abolishes interaction with UVRAG.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with UVRAG|||N6-acetyllysine|||Phosphomimetic mutant; impaired interaction with STX17 and abolished ability to promote autophagosome maturation.|||Phosphoserine; by MTOR|||Protein associated with UVRAG as autophagy enhancer|||Rubicon Homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089880|||http://purl.uniprot.org/annotation/VAR_022912|||http://purl.uniprot.org/annotation/VSP_014708|||http://purl.uniprot.org/annotation/VSP_014709|||http://purl.uniprot.org/annotation/VSP_014710|||http://purl.uniprot.org/annotation/VSP_014711|||http://purl.uniprot.org/annotation/VSP_014712|||http://purl.uniprot.org/annotation/VSP_014713|||http://purl.uniprot.org/annotation/VSP_055260
http://togogenome.org/gene/9606:ZNF213                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4L6|||http://purl.uniprot.org/uniprot/O14771                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||KRAB|||SCAN box|||Zinc finger protein 213                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047457|||http://purl.uniprot.org/annotation/VSP_055942|||http://purl.uniprot.org/annotation/VSP_055943
http://togogenome.org/gene/9606:GFPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4X9|||http://purl.uniprot.org/uniprot/B3KMR8|||http://purl.uniprot.org/uniprot/O94808                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant                                                                                  ^@                                                                                  For GATase activity|||Glutamine amidotransferase type-2|||Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2|||Phosphoserine|||Removed|||SIS|||SIS 1|||SIS 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135283|||http://purl.uniprot.org/annotation/VAR_013311
http://togogenome.org/gene/9606:NOTUM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P988                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity. Unable to mediate serine depalmitoleoylation of WNT proteins.|||Charge relay system|||Disordered|||N-linked (GlcNAc...) asparagine|||Palmitoleoyl-protein carboxylesterase NOTUM|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318755
http://togogenome.org/gene/9606:COL6A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDP3|||http://purl.uniprot.org/uniprot/P12110                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cell attachment site|||Collagen alpha-2(VI) chain|||Disordered|||In BTHLM1.|||In BTHLM1; results in reduced intracellular collagen VI assembly and secretion.|||In UCMD1.|||In UCMD1; prevents collagen VI assembly.|||In UCMD1; results in severe collagen VI matrix deficiencies.|||In isoform 2C2A'.|||In isoform 2C2A.|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||Phosphoserine|||Phosphothreonine|||Pro residues|||Triple-helical region|||VWFA|||VWFA 1|||VWFA 2|||VWFA 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005832|||http://purl.uniprot.org/annotation/PRO_5017320625|||http://purl.uniprot.org/annotation/VAR_013589|||http://purl.uniprot.org/annotation/VAR_013590|||http://purl.uniprot.org/annotation/VAR_030315|||http://purl.uniprot.org/annotation/VAR_030316|||http://purl.uniprot.org/annotation/VAR_048801|||http://purl.uniprot.org/annotation/VAR_048802|||http://purl.uniprot.org/annotation/VAR_048803|||http://purl.uniprot.org/annotation/VAR_058225|||http://purl.uniprot.org/annotation/VAR_058226|||http://purl.uniprot.org/annotation/VAR_058227|||http://purl.uniprot.org/annotation/VAR_058228|||http://purl.uniprot.org/annotation/VAR_058229|||http://purl.uniprot.org/annotation/VAR_058230|||http://purl.uniprot.org/annotation/VAR_058231|||http://purl.uniprot.org/annotation/VAR_058232|||http://purl.uniprot.org/annotation/VAR_058233|||http://purl.uniprot.org/annotation/VAR_058234|||http://purl.uniprot.org/annotation/VAR_058235|||http://purl.uniprot.org/annotation/VAR_058236|||http://purl.uniprot.org/annotation/VAR_058237|||http://purl.uniprot.org/annotation/VAR_058238|||http://purl.uniprot.org/annotation/VAR_058239|||http://purl.uniprot.org/annotation/VAR_058240|||http://purl.uniprot.org/annotation/VAR_058241|||http://purl.uniprot.org/annotation/VAR_076959|||http://purl.uniprot.org/annotation/VAR_076960|||http://purl.uniprot.org/annotation/VAR_076961|||http://purl.uniprot.org/annotation/VAR_076962|||http://purl.uniprot.org/annotation/VAR_076963|||http://purl.uniprot.org/annotation/VSP_001161|||http://purl.uniprot.org/annotation/VSP_001162|||http://purl.uniprot.org/annotation/VSP_001163|||http://purl.uniprot.org/annotation/VSP_001164
http://togogenome.org/gene/9606:NRARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6K4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Notch-regulated ankyrin repeat-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325079
http://togogenome.org/gene/9606:ARV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2C2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In DEE38; loss of protein stability; yeast complementation assays show that the variant does not rescue cell growth.|||In DEE38; loss of protein stability; yeast complementation assays show that the variant does partially rescue cell growth.|||Protein ARV1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228659|||http://purl.uniprot.org/annotation/VAR_033525|||http://purl.uniprot.org/annotation/VAR_077050|||http://purl.uniprot.org/annotation/VAR_077051
http://togogenome.org/gene/9606:MAML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Breakpoint for translocation to form the CRTC1-MAML2 and MAML2-CRTC1 fusion proteins|||Disordered|||Mastermind-like protein 2|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129495|||http://purl.uniprot.org/annotation/VAR_063127
http://togogenome.org/gene/9606:OR8G5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVX5|||http://purl.uniprot.org/uniprot/A0A126GW95|||http://purl.uniprot.org/uniprot/Q8NG78                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8G5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150664
http://togogenome.org/gene/9606:LIPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT32|||http://purl.uniprot.org/uniprot/P38571                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||In CESD and WOD.|||In CESD; significant loss of enzyme activity.|||In isoform 2.|||Lysosomal acid lipase/cholesteryl ester hydrolase|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity.|||Removed in mature form|||Significant loss of enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017799|||http://purl.uniprot.org/annotation/PRO_0000450225|||http://purl.uniprot.org/annotation/VAR_004247|||http://purl.uniprot.org/annotation/VAR_004248|||http://purl.uniprot.org/annotation/VAR_004249|||http://purl.uniprot.org/annotation/VAR_004250|||http://purl.uniprot.org/annotation/VAR_026523|||http://purl.uniprot.org/annotation/VAR_026524|||http://purl.uniprot.org/annotation/VAR_049821|||http://purl.uniprot.org/annotation/VSP_018596|||http://purl.uniprot.org/annotation/VSP_018597
http://togogenome.org/gene/9606:PFAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9T9|||http://purl.uniprot.org/uniprot/O15067|||http://purl.uniprot.org/uniprot/Q6P4B4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glutamine amidotransferase type-1|||Nucleophile|||Phosphoribosylformylglycinamidine synthase|||Phosphoribosylformylglycinamidine synthase N-terminal|||Phosphoribosylformylglycinamidine synthase linker|||Phosphoserine|||Phosphothreonine|||PurM-like C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100401|||http://purl.uniprot.org/annotation/VAR_055008|||http://purl.uniprot.org/annotation/VAR_055009|||http://purl.uniprot.org/annotation/VAR_055010|||http://purl.uniprot.org/annotation/VAR_055011
http://togogenome.org/gene/9606:PEX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60683                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||Cytoplasmic|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||In PBD6A.|||In PBD6B and PBD6A.|||In PBD6B.|||In PBD6B; neonatal adrenoleukodystrophy; abolished E3 ubiquitin-protein ligase activity.|||In isoform 2.|||Peroxisomal matrix|||Peroxisome biogenesis factor 10|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056376|||http://purl.uniprot.org/annotation/VAR_007805|||http://purl.uniprot.org/annotation/VAR_058388|||http://purl.uniprot.org/annotation/VAR_087145|||http://purl.uniprot.org/annotation/VAR_087146|||http://purl.uniprot.org/annotation/VAR_087147|||http://purl.uniprot.org/annotation/VAR_087148|||http://purl.uniprot.org/annotation/VAR_087149|||http://purl.uniprot.org/annotation/VSP_005771
http://togogenome.org/gene/9606:ANKRD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXR5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 10|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066905|||http://purl.uniprot.org/annotation/VAR_020095|||http://purl.uniprot.org/annotation/VSP_034637|||http://purl.uniprot.org/annotation/VSP_034638
http://togogenome.org/gene/9606:PALS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZG1|||http://purl.uniprot.org/uniprot/Q9NZW5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Guanylate kinase-like|||L27 1|||L27 2|||PDZ|||Phosphotyrosine|||Protein PALS2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094584
http://togogenome.org/gene/9606:PRRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5M6|||http://purl.uniprot.org/uniprot/A0A0S2Z5N9|||http://purl.uniprot.org/uniprot/Q9BZD6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-carboxyglutamate|||Cytoplasmic|||Extracellular|||Gla|||Helical|||LPXY motif; mediates binding to WW domain-containing proteins|||PPXY motif; mediates binding to WW domain-containing proteins|||Phosphoserine|||Reduced binding to MAGI1, MAGI3, NEDD4, NEDD4L, WWTR1 and YAP1.|||Reduced binding to MAGI1. No effect on binding to MAGI3, NEDD4, NEDD4L, WWTR1 or YAP1.|||Transmembrane gamma-carboxyglutamic acid protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022551|||http://purl.uniprot.org/annotation/PRO_0000022552|||http://purl.uniprot.org/annotation/PRO_5007027865|||http://purl.uniprot.org/annotation/PRO_5014239322|||http://purl.uniprot.org/annotation/VAR_051443|||http://purl.uniprot.org/annotation/VAR_051444|||http://purl.uniprot.org/annotation/VAR_051445
http://togogenome.org/gene/9606:PLRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43660                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Pleiotropic regulator 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051133|||http://purl.uniprot.org/annotation/VSP_008804
http://togogenome.org/gene/9606:MINAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59773                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Compromises cholesterol recruitment to the perinuclear region; when associated with A-112.|||Compromises cholesterol recruitment to the perinuclear region; when associated with A-117.|||Helical|||In DFNB120; enhances angiogenesis; enhances MAPK signaling pathway.|||Major intrinsically disordered NOTCH2-binding receptor 1-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157135|||http://purl.uniprot.org/annotation/VAR_087627
http://togogenome.org/gene/9606:TEX48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Testis-expressed protein 48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440612
http://togogenome.org/gene/9606:DLEU7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UYE1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Leukemia-associated protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281767|||http://purl.uniprot.org/annotation/VAR_031280|||http://purl.uniprot.org/annotation/VSP_024027
http://togogenome.org/gene/9606:YIPF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969M3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In MEDS2; no effect on differentiation and function of pancreatic beta cells; increased endoplasmic reticulum stress-induced apoptosis; decreased in C-peptide levels associated with increased proinsulin accumulation.|||In MEDS2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with Sec23|||Lumenal|||Protein YIPF5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234328|||http://purl.uniprot.org/annotation/VAR_085533|||http://purl.uniprot.org/annotation/VAR_085534|||http://purl.uniprot.org/annotation/VAR_085535|||http://purl.uniprot.org/annotation/VAR_085536|||http://purl.uniprot.org/annotation/VAR_085537|||http://purl.uniprot.org/annotation/VSP_018253|||http://purl.uniprot.org/annotation/VSP_018254
http://togogenome.org/gene/9606:BID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55957                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BH3|||BH3-interacting domain death agonist|||BH3-interacting domain death agonist p11|||BH3-interacting domain death agonist p13|||BH3-interacting domain death agonist p15|||Cleavage|||Cleavage; by CASP6|||Cleavage;by CASP6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143101|||http://purl.uniprot.org/annotation/PRO_0000223231|||http://purl.uniprot.org/annotation/PRO_0000223232|||http://purl.uniprot.org/annotation/PRO_0000223233|||http://purl.uniprot.org/annotation/VAR_018845|||http://purl.uniprot.org/annotation/VAR_025332|||http://purl.uniprot.org/annotation/VAR_061041|||http://purl.uniprot.org/annotation/VSP_017266|||http://purl.uniprot.org/annotation/VSP_017267|||http://purl.uniprot.org/annotation/VSP_017268|||http://purl.uniprot.org/annotation/VSP_017269
http://togogenome.org/gene/9606:SPATA20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB22                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Spermatogenesis-associated protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278450|||http://purl.uniprot.org/annotation/VAR_030777|||http://purl.uniprot.org/annotation/VAR_030778|||http://purl.uniprot.org/annotation/VAR_030779|||http://purl.uniprot.org/annotation/VSP_023288|||http://purl.uniprot.org/annotation/VSP_023289|||http://purl.uniprot.org/annotation/VSP_023290|||http://purl.uniprot.org/annotation/VSP_023291|||http://purl.uniprot.org/annotation/VSP_023292
http://togogenome.org/gene/9606:CBY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein chibby homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340100
http://togogenome.org/gene/9606:MLLT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55197|||http://purl.uniprot.org/uniprot/Q59EQ6|||http://purl.uniprot.org/uniprot/Q6N002                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2HC pre-PHD-type|||DNA-binding|||Disordered|||Does not affect interaction with histone H3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with histone H3.|||Impairs interaction with histone H3. Reduces association to chromatin. Does not rescued histone H3 'Lys-79' dimethylation (H3K79me2) levels in MLLT10-depleted cells. Does not rescued DOT1L-target genes in MLLT10-depleted cells.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||Interaction with FSTL3|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient A)|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient B)|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient C)|||Leucine-zipper|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Protein AF-10|||Required for interaction with histone H3|||Self-association|||Transactivation domain; required for DOT1L-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215935|||http://purl.uniprot.org/annotation/VSP_043044|||http://purl.uniprot.org/annotation/VSP_043045|||http://purl.uniprot.org/annotation/VSP_044552|||http://purl.uniprot.org/annotation/VSP_044553|||http://purl.uniprot.org/annotation/VSP_047517|||http://purl.uniprot.org/annotation/VSP_047518|||http://purl.uniprot.org/annotation/VSP_047519
http://togogenome.org/gene/9606:ABHD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2C6G3|||http://purl.uniprot.org/uniprot/Q96I13                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Disordered|||Protein ABHD8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281382
http://togogenome.org/gene/9606:H1-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16402                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.3|||N-acetylserine|||N6-(beta-hydroxybutyryl)lysine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195907|||http://purl.uniprot.org/annotation/VAR_049306
http://togogenome.org/gene/9606:SUCLG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I99                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-grasp|||Important for substrate specificity|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033356|||http://purl.uniprot.org/annotation/VAR_052499|||http://purl.uniprot.org/annotation/VAR_052500|||http://purl.uniprot.org/annotation/VSP_042013
http://togogenome.org/gene/9606:DBF4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BRCT|||DBF4-type|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein DBF4 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317553|||http://purl.uniprot.org/annotation/VSP_031014|||http://purl.uniprot.org/annotation/VSP_031015|||http://purl.uniprot.org/annotation/VSP_031016|||http://purl.uniprot.org/annotation/VSP_031017|||http://purl.uniprot.org/annotation/VSP_031018|||http://purl.uniprot.org/annotation/VSP_031019
http://togogenome.org/gene/9606:ZNF365                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70YC5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type; degenerate|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Protein ZNF365                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076374|||http://purl.uniprot.org/annotation/VAR_024325|||http://purl.uniprot.org/annotation/VSP_016596|||http://purl.uniprot.org/annotation/VSP_016597|||http://purl.uniprot.org/annotation/VSP_016598|||http://purl.uniprot.org/annotation/VSP_016599|||http://purl.uniprot.org/annotation/VSP_016600
http://togogenome.org/gene/9606:RCHY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PM5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity.|||CHY-type|||CTCHY-type|||In isoform 2 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||Phosphoserine|||RING finger and CHY zinc finger domain-containing protein 1|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056312|||http://purl.uniprot.org/annotation/VSP_038467|||http://purl.uniprot.org/annotation/VSP_038468|||http://purl.uniprot.org/annotation/VSP_044085|||http://purl.uniprot.org/annotation/VSP_053385|||http://purl.uniprot.org/annotation/VSP_053386|||http://purl.uniprot.org/annotation/VSP_053787|||http://purl.uniprot.org/annotation/VSP_053788
http://togogenome.org/gene/9606:ELOVL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXB9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Elongation of very long chain fatty acids protein 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207538|||http://purl.uniprot.org/annotation/VAR_039039|||http://purl.uniprot.org/annotation/VAR_039040
http://togogenome.org/gene/9606:NKX2-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43699                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Nkx-2.1|||In BHC.|||In BHC; decrease in DNA-binding; no effect on transcription activation from thyroglobulin/TG, nor from pulmonary surfactant-associated protein C/SFTPC gene promoters.|||In BHC; loss of transcription activation.|||In BHC; unknown pathological significance.|||In CAHTP.|||In NMTC1; loss of transcription regulatory region DNA binding; decreased transcription factor activity, sequence-specific DNA binding; tested for the thyroglobulin gene; associated with dominant impairment of thyroid-specific genes transcription and increased thyroid cells proliferation.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049343|||http://purl.uniprot.org/annotation/VAR_015188|||http://purl.uniprot.org/annotation/VAR_015189|||http://purl.uniprot.org/annotation/VAR_034906|||http://purl.uniprot.org/annotation/VAR_073040|||http://purl.uniprot.org/annotation/VAR_075209|||http://purl.uniprot.org/annotation/VAR_075210|||http://purl.uniprot.org/annotation/VAR_075769|||http://purl.uniprot.org/annotation/VAR_077542|||http://purl.uniprot.org/annotation/VSP_037890
http://togogenome.org/gene/9606:INTS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWZ3|||http://purl.uniprot.org/uniprot/Q96SY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Integrator complex subunit 14|||Integrator complex subunit 14 C-terminal|||Integrator complex subunit 14 beta-barrel|||N6-acetyllysine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296266|||http://purl.uniprot.org/annotation/VSP_027180|||http://purl.uniprot.org/annotation/VSP_027181|||http://purl.uniprot.org/annotation/VSP_043277|||http://purl.uniprot.org/annotation/VSP_044250
http://togogenome.org/gene/9606:SHCBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEM2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||Phosphoserine|||Phosphothreonine|||Removed|||SHC SH2 domain-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076315|||http://purl.uniprot.org/annotation/VAR_051354|||http://purl.uniprot.org/annotation/VAR_051355
http://togogenome.org/gene/9606:KIF13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQT8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by MARK2; when associated with A-1389.|||Abolishes phosphorylation by MARK2; when associated with A-1410.|||Basic and acidic residues|||CAP-Gly|||Disordered|||FHA|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF13B|||Phosphoserine|||Phosphoserine; by MARK2|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125448|||http://purl.uniprot.org/annotation/VAR_055982|||http://purl.uniprot.org/annotation/VSP_056360|||http://purl.uniprot.org/annotation/VSP_056361
http://togogenome.org/gene/9606:TEX14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWB6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||D-box|||Disordered|||GPPX3Y|||In PBD-1; reduced ability to interact with PLK1.|||In PBD-5; reduced ability to interact with PLK1.|||In SPGF23.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Inactive serine/threonine-protein kinase TEX14|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246995|||http://purl.uniprot.org/annotation/VAR_041388|||http://purl.uniprot.org/annotation/VAR_041389|||http://purl.uniprot.org/annotation/VAR_041390|||http://purl.uniprot.org/annotation/VAR_041391|||http://purl.uniprot.org/annotation/VAR_087420|||http://purl.uniprot.org/annotation/VSP_019868|||http://purl.uniprot.org/annotation/VSP_019869
http://togogenome.org/gene/9606:RIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4U0|||http://purl.uniprot.org/uniprot/Q13671                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by PKD and the interaction with 14-3-3 proteins.|||Disordered|||In isoform RIN1-delta.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKD/PRKD1|||Phosphotyrosine; by ABL1 and ABL2|||Pro residues|||Ras and 14-3-3 protein binding region|||Ras and Rab interactor 1|||Ras-associating|||SH2|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191317|||http://purl.uniprot.org/annotation/VSP_004377
http://togogenome.org/gene/9606:AGTPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNS1|||http://purl.uniprot.org/uniprot/Q9UPW5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic carboxypeptidase 1|||Cytosolic carboxypeptidase N-terminal|||Disordered|||In CONDCA.|||In CONDCA; decreased tubulin deglutamylation asshown by in vitro functional expression of the homologous murine variant.|||In CONDCA; decreased tubulin deglutamylation shown by in vitro functional expression of the homologous murine variant.|||In CONDCA; loss of tubulin deglutamylation; patient cells show lack of protein and excess of tubulin polyglutamylation.|||In CONDCA; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Nucleophile|||Peptidase M14 carboxypeptidase A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308690|||http://purl.uniprot.org/annotation/VAR_036884|||http://purl.uniprot.org/annotation/VAR_081908|||http://purl.uniprot.org/annotation/VAR_081909|||http://purl.uniprot.org/annotation/VAR_081910|||http://purl.uniprot.org/annotation/VAR_081911|||http://purl.uniprot.org/annotation/VAR_081912|||http://purl.uniprot.org/annotation/VAR_081913|||http://purl.uniprot.org/annotation/VAR_081914|||http://purl.uniprot.org/annotation/VAR_081915|||http://purl.uniprot.org/annotation/VAR_081916|||http://purl.uniprot.org/annotation/VSP_029044|||http://purl.uniprot.org/annotation/VSP_040422
http://togogenome.org/gene/9606:DVL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14641                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost abolishes interaction with FOXK2.|||Basic and acidic residues|||DEP|||DIX|||Disordered|||Found in a renal cell carcinoma case; somatic mutation.|||No effect on interaction with FOXK2.|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Reduces interaction with FOXK2.|||Required for interaction with FOXK2|||Segment polarity protein dishevelled homolog DVL-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145746|||http://purl.uniprot.org/annotation/VAR_064708
http://togogenome.org/gene/9606:GPA33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99795                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell surface A33 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014770|||http://purl.uniprot.org/annotation/VAR_020079|||http://purl.uniprot.org/annotation/VAR_049874
http://togogenome.org/gene/9606:SPATA46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0L3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Spermatogenesis-associated protein 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279458|||http://purl.uniprot.org/annotation/VAR_030904|||http://purl.uniprot.org/annotation/VAR_030905
http://togogenome.org/gene/9606:GPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R138|||http://purl.uniprot.org/uniprot/P21695                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycerol-3-phosphate dehydrogenase NAD-dependent C-terminal|||Glycerol-3-phosphate dehydrogenase NAD-dependent N-terminal|||Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic|||In HTGTI.|||In isoform 2.|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138079|||http://purl.uniprot.org/annotation/VAR_029492|||http://purl.uniprot.org/annotation/VAR_029493|||http://purl.uniprot.org/annotation/VAR_049220|||http://purl.uniprot.org/annotation/VAR_067425|||http://purl.uniprot.org/annotation/VAR_067426|||http://purl.uniprot.org/annotation/VAR_071967|||http://purl.uniprot.org/annotation/VSP_045999
http://togogenome.org/gene/9606:CSNK1G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6M4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Casein kinase I isoform gamma-3|||Disordered|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192846|||http://purl.uniprot.org/annotation/VSP_004749|||http://purl.uniprot.org/annotation/VSP_010256|||http://purl.uniprot.org/annotation/VSP_047053|||http://purl.uniprot.org/annotation/VSP_047054|||http://purl.uniprot.org/annotation/VSP_047055
http://togogenome.org/gene/9606:CCDC85A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PX6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Coiled-coil domain-containing protein 85A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271104
http://togogenome.org/gene/9606:PCED1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1Q7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||PC-esterase domain-containing protein 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079446|||http://purl.uniprot.org/annotation/VAR_021945|||http://purl.uniprot.org/annotation/VSP_003818|||http://purl.uniprot.org/annotation/VSP_003819|||http://purl.uniprot.org/annotation/VSP_013917|||http://purl.uniprot.org/annotation/VSP_013918
http://togogenome.org/gene/9606:ZNF263                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14978                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in a patient with hypothalamic hamartoma; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger protein 263                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047491|||http://purl.uniprot.org/annotation/VAR_052801|||http://purl.uniprot.org/annotation/VAR_052802|||http://purl.uniprot.org/annotation/VAR_061943|||http://purl.uniprot.org/annotation/VAR_084704
http://togogenome.org/gene/9606:STK31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG1|||http://purl.uniprot.org/uniprot/B3KY91|||http://purl.uniprot.org/uniprot/Q9BXU1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Protein kinase|||Serine/threonine-protein kinase 31|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086715|||http://purl.uniprot.org/annotation/VAR_031600|||http://purl.uniprot.org/annotation/VAR_031601|||http://purl.uniprot.org/annotation/VAR_031602|||http://purl.uniprot.org/annotation/VAR_031603|||http://purl.uniprot.org/annotation/VAR_031604|||http://purl.uniprot.org/annotation/VAR_031605|||http://purl.uniprot.org/annotation/VAR_041150|||http://purl.uniprot.org/annotation/VAR_041151|||http://purl.uniprot.org/annotation/VAR_041152|||http://purl.uniprot.org/annotation/VAR_041153|||http://purl.uniprot.org/annotation/VAR_041154|||http://purl.uniprot.org/annotation/VAR_041155|||http://purl.uniprot.org/annotation/VAR_041156|||http://purl.uniprot.org/annotation/VAR_041157|||http://purl.uniprot.org/annotation/VAR_041158|||http://purl.uniprot.org/annotation/VAR_041159|||http://purl.uniprot.org/annotation/VAR_041160|||http://purl.uniprot.org/annotation/VAR_041161|||http://purl.uniprot.org/annotation/VAR_041162|||http://purl.uniprot.org/annotation/VAR_051675|||http://purl.uniprot.org/annotation/VSP_024389|||http://purl.uniprot.org/annotation/VSP_045210
http://togogenome.org/gene/9606:TMEM190                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||P-type|||Polar residues|||Transmembrane protein 190                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312282
http://togogenome.org/gene/9606:RELT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Z4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AI3C; unknown pathological significance.|||Loss of interaction with STK39.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||RFRV motif; mediates interaction with STK39|||TNFR-Cys|||Tumor necrosis factor receptor superfamily member 19L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034599|||http://purl.uniprot.org/annotation/VAR_022614|||http://purl.uniprot.org/annotation/VAR_082198
http://togogenome.org/gene/9606:PRR32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ATL7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336102|||http://purl.uniprot.org/annotation/VAR_059650|||http://purl.uniprot.org/annotation/VAR_061638
http://togogenome.org/gene/9606:ZNF527                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 527                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047639|||http://purl.uniprot.org/annotation/VSP_040341
http://togogenome.org/gene/9606:BRCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51587                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCA2 1|||BRCA2 2|||BRCA2 3|||BRCA2 4|||BRCA2 5|||BRCA2 6|||BRCA2 7|||BRCA2 8|||Basic and acidic residues|||Benign variant; no effect on homologous recombination-mediated DNA repair; no effect on interaction with SEM1.|||Benign variant; no effect on homology-directed repair activity.|||Breast cancer type 2 susceptibility protein|||Disordered|||Disrupts interaction with SEM1.|||Impaired interaction with RAD51.|||In BC and ovarian cancer; unknown pathological significance.|||In BC and ovarian cancer; unknown pathological significance; no effect on homology-directed repair activity.|||In BC and pancreas cancer.|||In BC.|||In BC; abolishes interaction with PALB2.|||In BC; also found in pancreatic cancer; decreased homology-directed repair activity.|||In BC; benign variant; no effect on homology-directed repair activity.|||In BC; has defective function consistent with pathogenicity; major splicing aberration identified with this mutant; reduced homology-directed repair activity.|||In BC; has defective function consistent with pathogenicity; multifactorial likelihood analysis provides evidence for pathogenicity; reduced homology-directed repair activity.|||In BC; major splicing aberration identified with this mutant; multifactorial likelihood analysis provides evidence for pathogenicity.|||In BC; reduced homology-directed repair activity.|||In BC; somatic mutation.|||In BC; unknown pathological significance.|||In BC; unknown pathological significance; decreased homology-directed repair activity.|||In BC; unknown pathological significance; disrupts interaction with SEM1 promoting interaction with XPO1 and BRCA2 cytoplasmic localization; in heterozygous state promotes RAD51 cytoplasmic localization; reduced homology-directed repair activity.|||In BC; unknown pathological significance; no effect on homologous recombination-mediated DNA repair; no effect on interaction with SEM1.|||In BC; unknown pathological significance; no effect on homology-directed repair activity.|||In BC; unknown pathological significance; reduced homology-directed repair activity.|||In FANCD1; affects protein splicing and expression; decreases homologous recombination-mediated DNA repair.|||In FANCD1; hypersensitive to DNA damage; disrupts interaction with SEM1; decreased homology-directed repair activity.|||In FANCD1; hypersensitive to DNA damage; reduced homology-directed repair activity; no effect on interaction with SEM1.|||In a patient with ovarian cancer; unknown pathological significance; no effect on homology-directed repair activity.|||In bladder cancer.|||In lung cancer.|||In melanoma.|||In one patient with BC.|||In one patient with BC; normal RNA expression and splicing.|||In one patient with esophageal carcinoma.|||In one patient with esophageal carcinoma; somatic mutation.|||In one patient with esophageal carcinoma; somatic mutation; decreased homology-directed repair activity.|||In one patient with pancreatic cancer.|||In ovarian cancer and BC; somatic mutation; unknown pathological significance; small decrease of homology-directed repair activity.|||In ovarian cancer and renal cancer; unknown pathological significance.|||In ovarian cancer.|||In ovarian cancer; unknown pathological significance.|||Interaction with FANCD2|||Interaction with HSF2BP|||Interaction with NPM1|||Interaction with PALB2|||Interaction with POLH|||Interaction with RAD51|||Interaction with SEM1|||Loss of phosphorylation by CHEK1 and CHEK2 (in vitro).|||Nuclear export signal; masked by interaction with SEM1|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Phosphothreonine|||Phosphothreonine; by CHEK1 and CHEK2|||Polar residues|||Required for stimulation of POLH DNA polymerization activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064984|||http://purl.uniprot.org/annotation/VAR_005085|||http://purl.uniprot.org/annotation/VAR_005086|||http://purl.uniprot.org/annotation/VAR_005087|||http://purl.uniprot.org/annotation/VAR_005088|||http://purl.uniprot.org/annotation/VAR_005089|||http://purl.uniprot.org/annotation/VAR_005090|||http://purl.uniprot.org/annotation/VAR_005091|||http://purl.uniprot.org/annotation/VAR_005092|||http://purl.uniprot.org/annotation/VAR_005093|||http://purl.uniprot.org/annotation/VAR_005094|||http://purl.uniprot.org/annotation/VAR_005095|||http://purl.uniprot.org/annotation/VAR_005096|||http://purl.uniprot.org/annotation/VAR_005097|||http://purl.uniprot.org/annotation/VAR_005098|||http://purl.uniprot.org/annotation/VAR_005099|||http://purl.uniprot.org/annotation/VAR_005100|||http://purl.uniprot.org/annotation/VAR_005101|||http://purl.uniprot.org/annotation/VAR_005102|||http://purl.uniprot.org/annotation/VAR_005103|||http://purl.uniprot.org/annotation/VAR_005104|||http://purl.uniprot.org/annotation/VAR_005105|||http://purl.uniprot.org/annotation/VAR_005106|||http://purl.uniprot.org/annotation/VAR_005107|||http://purl.uniprot.org/annotation/VAR_005108|||http://purl.uniprot.org/annotation/VAR_005109|||http://purl.uniprot.org/annotation/VAR_005110|||http://purl.uniprot.org/annotation/VAR_005111|||http://purl.uniprot.org/annotation/VAR_005112|||http://purl.uniprot.org/annotation/VAR_008766|||http://purl.uniprot.org/annotation/VAR_008767|||http://purl.uniprot.org/annotation/VAR_008768|||http://purl.uniprot.org/annotation/VAR_008769|||http://purl.uniprot.org/annotation/VAR_008770|||http://purl.uniprot.org/annotation/VAR_008771|||http://purl.uniprot.org/annotation/VAR_008772|||http://purl.uniprot.org/annotation/VAR_008773|||http://purl.uniprot.org/annotation/VAR_008774|||http://purl.uniprot.org/annotation/VAR_008775|||http://purl.uniprot.org/annotation/VAR_008776|||http://purl.uniprot.org/annotation/VAR_008777|||http://purl.uniprot.org/annotation/VAR_008778|||http://purl.uniprot.org/annotation/VAR_008779|||http://purl.uniprot.org/annotation/VAR_008780|||http://purl.uniprot.org/annotation/VAR_008781|||http://purl.uniprot.org/annotation/VAR_008782|||http://purl.uniprot.org/annotation/VAR_008783|||http://purl.uniprot.org/annotation/VAR_008784|||http://purl.uniprot.org/annotation/VAR_008785|||http://purl.uniprot.org/annotation/VAR_008786|||http://purl.uniprot.org/annotation/VAR_008787|||http://purl.uniprot.org/annotation/VAR_008788|||http://purl.uniprot.org/annotation/VAR_008789|||http://purl.uniprot.org/annotation/VAR_008790|||http://purl.uniprot.org/annotation/VAR_008791|||http://purl.uniprot.org/annotation/VAR_008792|||http://purl.uniprot.org/annotation/VAR_008793|||http://purl.uniprot.org/annotation/VAR_008794|||http://purl.uniprot.org/annotation/VAR_008795|||http://purl.uniprot.org/annotation/VAR_008796|||http://purl.uniprot.org/annotation/VAR_018661|||http://purl.uniprot.org/annotation/VAR_018908|||http://purl.uniprot.org/annotation/VAR_018909|||http://purl.uniprot.org/annotation/VAR_018910|||http://purl.uniprot.org/annotation/VAR_018911|||http://purl.uniprot.org/annotation/VAR_018912|||http://purl.uniprot.org/annotation/VAR_018913|||http://purl.uniprot.org/annotation/VAR_018914|||http://purl.uniprot.org/annotation/VAR_018915|||http://purl.uniprot.org/annotation/VAR_018916|||http://purl.uniprot.org/annotation/VAR_018917|||http://purl.uniprot.org/annotation/VAR_020705|||http://purl.uniprot.org/annotation/VAR_020706|||http://purl.uniprot.org/annotation/VAR_020707|||http://purl.uniprot.org/annotation/VAR_020708|||http://purl.uniprot.org/annotation/VAR_020709|||http://purl.uniprot.org/annotation/VAR_020710|||http://purl.uniprot.org/annotation/VAR_020711|||http://purl.uniprot.org/annotation/VAR_020712|||http://purl.uniprot.org/annotation/VAR_020713|||http://purl.uniprot.org/annotation/VAR_020714|||http://purl.uniprot.org/annotation/VAR_020715|||http://purl.uniprot.org/annotation/VAR_020716|||http://purl.uniprot.org/annotation/VAR_020717|||http://purl.uniprot.org/annotation/VAR_020718|||http://purl.uniprot.org/annotation/VAR_020719|||http://purl.uniprot.org/annotation/VAR_020720|||http://purl.uniprot.org/annotation/VAR_020721|||http://purl.uniprot.org/annotation/VAR_020722|||http://purl.uniprot.org/annotation/VAR_020723|||http://purl.uniprot.org/annotation/VAR_020724|||http://purl.uniprot.org/annotation/VAR_020725|||http://purl.uniprot.org/annotation/VAR_020726|||http://purl.uniprot.org/annotation/VAR_020727|||http://purl.uniprot.org/annotation/VAR_020728|||http://purl.uniprot.org/annotation/VAR_020729|||http://purl.uniprot.org/annotation/VAR_020730|||http://purl.uniprot.org/annotation/VAR_020731|||http://purl.uniprot.org/annotation/VAR_020732|||http://purl.uniprot.org/annotation/VAR_020733|||http://purl.uniprot.org/annotation/VAR_020734|||http://purl.uniprot.org/annotation/VAR_020735|||http://purl.uniprot.org/annotation/VAR_020736|||http://purl.uniprot.org/annotation/VAR_020737|||http://purl.uniprot.org/annotation/VAR_020738|||http://purl.uniprot.org/annotation/VAR_020739|||http://purl.uniprot.org/annotation/VAR_020740|||http://purl.uniprot.org/annotation/VAR_020741|||http://purl.uniprot.org/annotation/VAR_020742|||http://purl.uniprot.org/annotation/VAR_020743|||http://purl.uniprot.org/annotation/VAR_020744|||http://purl.uniprot.org/annotation/VAR_020745|||http://purl.uniprot.org/annotation/VAR_028167|||http://purl.uniprot.org/annotation/VAR_028168|||http://purl.uniprot.org/annotation/VAR_028169|||http://purl.uniprot.org/annotation/VAR_032712|||http://purl.uniprot.org/annotation/VAR_032713|||http://purl.uniprot.org/annotation/VAR_032714|||http://purl.uniprot.org/annotation/VAR_032715|||http://purl.uniprot.org/annotation/VAR_032716|||http://purl.uniprot.org/annotation/VAR_032717|||http://purl.uniprot.org/annotation/VAR_032718|||http://purl.uniprot.org/annotation/VAR_032719|||http://purl.uniprot.org/annotation/VAR_032720|||http://purl.uniprot.org/annotation/VAR_032721|||http://purl.uniprot.org/annotation/VAR_032722|||http://purl.uniprot.org/annotation/VAR_032723|||http://purl.uniprot.org/annotation/VAR_032724|||http://purl.uniprot.org/annotation/VAR_032725|||http://purl.uniprot.org/annotation/VAR_032726|||http://purl.uniprot.org/annotation/VAR_032727|||http://purl.uniprot.org/annotation/VAR_032728|||http://purl.uniprot.org/annotation/VAR_032729|||http://purl.uniprot.org/annotation/VAR_032730|||http://purl.uniprot.org/annotation/VAR_032731|||http://purl.uniprot.org/annotation/VAR_032732|||http://purl.uniprot.org/annotation/VAR_032733|||http://purl.uniprot.org/annotation/VAR_032734|||http://purl.uniprot.org/annotation/VAR_032735|||http://purl.uniprot.org/annotation/VAR_035436|||http://purl.uniprot.org/annotation/VAR_056751|||http://purl.uniprot.org/annotation/VAR_056752|||http://purl.uniprot.org/annotation/VAR_056753|||http://purl.uniprot.org/annotation/VAR_056754|||http://purl.uniprot.org/annotation/VAR_056755|||http://purl.uniprot.org/annotation/VAR_056756|||http://purl.uniprot.org/annotation/VAR_056757|||http://purl.uniprot.org/annotation/VAR_056758|||http://purl.uniprot.org/annotation/VAR_056759|||http://purl.uniprot.org/annotation/VAR_056760|||http://purl.uniprot.org/annotation/VAR_056761|||http://purl.uniprot.org/annotation/VAR_061563|||http://purl.uniprot.org/annotation/VAR_063911|||http://purl.uniprot.org/annotation/VAR_063912|||http://purl.uniprot.org/annotation/VAR_063913|||http://purl.uniprot.org/annotation/VAR_063914|||http://purl.uniprot.org/annotation/VAR_063915|||http://purl.uniprot.org/annotation/VAR_063916|||http://purl.uniprot.org/annotation/VAR_063917|||http://purl.uniprot.org/annotation/VAR_063918|||http://purl.uniprot.org/annotation/VAR_076440
http://togogenome.org/gene/9606:CRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5IJ48                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9|||Found in a fetus with ventriculomegaly with cystic kidney disease; unknown pathological significance.|||Helical|||In FSGS9.|||In FSGS9; loss of function mutation.|||In FSGS9; moderate loss of function mutation.|||In FSGS9; unknown pathological significance.|||In FSGS9; when associated in cis with 1098-C--I-1285 del; unknown pathological significance.|||In FSGS9; when associated in cis with A-1076; unknown pathological significance.|||In FSGS9; when associated in cis with C-1115; unknown pathological significance.|||In FSGS9; when associated in cis with C-498; unknown pathological significance.|||In FSGS9; when associated in cis with C-628; unknown pathological significance.|||In FSGS9; when associated in cis with M-902 and 149-E--I-1285 del; unknown pathological significance.|||In FSGS9; when associated in cis with M-902 and S-1064; unknown pathological significance.|||In FSGS9; when associated in cis with S-1064 and 149-E--I-1285 del; unknown pathological significance.|||In RP; unknown pathological significance; reduces protein stability and expression.|||In VMCKD.|||In VMCKD. In VMCKD; when associated in cis with A-643; unknown pathological significance. In FSGS9; when associated in cis with K-643; unknown pathological significance.|||In VMCKD; when associated in cis with K-800; unknown pathological significance.|||In VMCKD; when associated in cis with K-800; unknown pathological significance. In FSGS9; when associated in cis with K-800; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with EPB41L5|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with P-1260 and E-1264.|||No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and E-1264.|||No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and P-1260.|||O-linked (Glc...) serine|||Protein crumbs homolog 2|||Required for maximum inhibition of APP amyloid-beta peptide secretion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007502|||http://purl.uniprot.org/annotation/VAR_022984|||http://purl.uniprot.org/annotation/VAR_022985|||http://purl.uniprot.org/annotation/VAR_022986|||http://purl.uniprot.org/annotation/VAR_022987|||http://purl.uniprot.org/annotation/VAR_022988|||http://purl.uniprot.org/annotation/VAR_022989|||http://purl.uniprot.org/annotation/VAR_022990|||http://purl.uniprot.org/annotation/VAR_022991|||http://purl.uniprot.org/annotation/VAR_022992|||http://purl.uniprot.org/annotation/VAR_022993|||http://purl.uniprot.org/annotation/VAR_022994|||http://purl.uniprot.org/annotation/VAR_048974|||http://purl.uniprot.org/annotation/VAR_061153|||http://purl.uniprot.org/annotation/VAR_073266|||http://purl.uniprot.org/annotation/VAR_073267|||http://purl.uniprot.org/annotation/VAR_073268|||http://purl.uniprot.org/annotation/VAR_073269|||http://purl.uniprot.org/annotation/VAR_073270|||http://purl.uniprot.org/annotation/VAR_073271|||http://purl.uniprot.org/annotation/VAR_073272|||http://purl.uniprot.org/annotation/VAR_084122|||http://purl.uniprot.org/annotation/VAR_084123|||http://purl.uniprot.org/annotation/VAR_084124|||http://purl.uniprot.org/annotation/VAR_084125|||http://purl.uniprot.org/annotation/VAR_084126|||http://purl.uniprot.org/annotation/VAR_084127|||http://purl.uniprot.org/annotation/VAR_084128|||http://purl.uniprot.org/annotation/VAR_084129|||http://purl.uniprot.org/annotation/VAR_084130|||http://purl.uniprot.org/annotation/VAR_084131|||http://purl.uniprot.org/annotation/VAR_084132|||http://purl.uniprot.org/annotation/VAR_084133|||http://purl.uniprot.org/annotation/VAR_084134|||http://purl.uniprot.org/annotation/VSP_014737|||http://purl.uniprot.org/annotation/VSP_014738|||http://purl.uniprot.org/annotation/VSP_014739|||http://purl.uniprot.org/annotation/VSP_014740
http://togogenome.org/gene/9606:SELENON                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||In CMYP3.|||In CMYP3; decreased function in the regulation of ryanodine receptor activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Selenocysteine|||Selenoprotein N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022311|||http://purl.uniprot.org/annotation/VAR_019635|||http://purl.uniprot.org/annotation/VAR_019636|||http://purl.uniprot.org/annotation/VAR_019637|||http://purl.uniprot.org/annotation/VAR_019638|||http://purl.uniprot.org/annotation/VAR_019639|||http://purl.uniprot.org/annotation/VAR_019640|||http://purl.uniprot.org/annotation/VAR_019641|||http://purl.uniprot.org/annotation/VAR_038845|||http://purl.uniprot.org/annotation/VAR_038846|||http://purl.uniprot.org/annotation/VAR_038847|||http://purl.uniprot.org/annotation/VAR_058462|||http://purl.uniprot.org/annotation/VAR_058463|||http://purl.uniprot.org/annotation/VAR_058464|||http://purl.uniprot.org/annotation/VSP_011372
http://togogenome.org/gene/9606:CEP120                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLH5|||http://purl.uniprot.org/uniprot/Q8N960                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 1|||C2 2|||Centrosomal protein of 120 kDa|||Disordered|||Found in a patient with Meckel syndrome; unknown pathological significance.|||In JBTS31; unknown pathological significance.|||In SRTD13; also found in a patient with more complex ciliopathy.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348262|||http://purl.uniprot.org/annotation/VAR_046126|||http://purl.uniprot.org/annotation/VAR_046127|||http://purl.uniprot.org/annotation/VAR_046128|||http://purl.uniprot.org/annotation/VAR_046129|||http://purl.uniprot.org/annotation/VAR_073672|||http://purl.uniprot.org/annotation/VAR_077553|||http://purl.uniprot.org/annotation/VAR_077554|||http://purl.uniprot.org/annotation/VAR_077555|||http://purl.uniprot.org/annotation/VAR_077556|||http://purl.uniprot.org/annotation/VAR_077557|||http://purl.uniprot.org/annotation/VSP_035123|||http://purl.uniprot.org/annotation/VSP_035124|||http://purl.uniprot.org/annotation/VSP_035125
http://togogenome.org/gene/9606:TMEM135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UB9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 135                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284622|||http://purl.uniprot.org/annotation/VAR_031787|||http://purl.uniprot.org/annotation/VAR_031788|||http://purl.uniprot.org/annotation/VAR_031789|||http://purl.uniprot.org/annotation/VSP_024579
http://togogenome.org/gene/9606:DUSP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16690                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Dual specificity protein phosphatase 5|||Nuclear localization signal|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094802|||http://purl.uniprot.org/annotation/VAR_020298|||http://purl.uniprot.org/annotation/VAR_047368|||http://purl.uniprot.org/annotation/VAR_059777|||http://purl.uniprot.org/annotation/VAR_059778
http://togogenome.org/gene/9606:PRRC2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EPN9|||http://purl.uniprot.org/uniprot/Q9Y520                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||BAT2 N-terminal|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein PRRC2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349239|||http://purl.uniprot.org/annotation/VAR_046290|||http://purl.uniprot.org/annotation/VAR_046291|||http://purl.uniprot.org/annotation/VAR_046292|||http://purl.uniprot.org/annotation/VAR_046293|||http://purl.uniprot.org/annotation/VAR_046294|||http://purl.uniprot.org/annotation/VAR_046295|||http://purl.uniprot.org/annotation/VAR_046296|||http://purl.uniprot.org/annotation/VAR_046297|||http://purl.uniprot.org/annotation/VAR_046298|||http://purl.uniprot.org/annotation/VAR_046299|||http://purl.uniprot.org/annotation/VAR_059584|||http://purl.uniprot.org/annotation/VSP_035244|||http://purl.uniprot.org/annotation/VSP_035245|||http://purl.uniprot.org/annotation/VSP_035246|||http://purl.uniprot.org/annotation/VSP_035247|||http://purl.uniprot.org/annotation/VSP_035248|||http://purl.uniprot.org/annotation/VSP_035249|||http://purl.uniprot.org/annotation/VSP_035250
http://togogenome.org/gene/9606:FBXO40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH90                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 40|||TRAF-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119938|||http://purl.uniprot.org/annotation/VAR_030005
http://togogenome.org/gene/9606:NEUROD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7T3|||http://purl.uniprot.org/uniprot/Q96NK8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  BHLH|||Disordered|||Neurogenic differentiation factor 6|||Nuclear localization signal|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127393
http://togogenome.org/gene/9606:TAAR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14804                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070154|||http://purl.uniprot.org/annotation/VAR_055923|||http://purl.uniprot.org/annotation/VAR_055924
http://togogenome.org/gene/9606:ABCA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUA7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 9|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250680|||http://purl.uniprot.org/annotation/VAR_027594|||http://purl.uniprot.org/annotation/VAR_027595|||http://purl.uniprot.org/annotation/VAR_027596|||http://purl.uniprot.org/annotation/VAR_027597|||http://purl.uniprot.org/annotation/VSP_020705|||http://purl.uniprot.org/annotation/VSP_020706|||http://purl.uniprot.org/annotation/VSP_020707|||http://purl.uniprot.org/annotation/VSP_020708|||http://purl.uniprot.org/annotation/VSP_020709
http://togogenome.org/gene/9606:GON7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||EKC/KEOPS complex subunit GON7|||In GAMOS9; slightly decreased formation of tRNA threonylcarbamoyladenosine modification.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089945|||http://purl.uniprot.org/annotation/VAR_085774
http://togogenome.org/gene/9606:UCP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4G5|||http://purl.uniprot.org/uniprot/P55916                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 3.|||In isoform UCP3S.|||In obesity.|||In severe obesity with type 2 diabetes.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Purine nucleotide binding|||Putative mitochondrial transporter UCP3|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090672|||http://purl.uniprot.org/annotation/VAR_004407|||http://purl.uniprot.org/annotation/VAR_004408|||http://purl.uniprot.org/annotation/VAR_050136|||http://purl.uniprot.org/annotation/VSP_003270|||http://purl.uniprot.org/annotation/VSP_003271
http://togogenome.org/gene/9606:ARHGEF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZG4|||http://purl.uniprot.org/uniprot/Q6ZSZ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type; degenerate|||DH|||Disordered|||In RP78.|||In RP78; decreased function in positive regulation of Rho protein signal transduction; loss of function in regulation of actomyosin structure organization.|||In RP78; no effect on function in positive regulation of Rho protein signal transduction; decreased function in regulation of actomyosin structure organization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341415|||http://purl.uniprot.org/annotation/VAR_044066|||http://purl.uniprot.org/annotation/VAR_044067|||http://purl.uniprot.org/annotation/VAR_063099|||http://purl.uniprot.org/annotation/VAR_078919|||http://purl.uniprot.org/annotation/VAR_078920|||http://purl.uniprot.org/annotation/VAR_078921|||http://purl.uniprot.org/annotation/VAR_078922|||http://purl.uniprot.org/annotation/VSP_059874|||http://purl.uniprot.org/annotation/VSP_059875|||http://purl.uniprot.org/annotation/VSP_059876|||http://purl.uniprot.org/annotation/VSP_059877
http://togogenome.org/gene/9606:SLC26A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58743                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Contributes to anion binding|||Controls the electromotile activity|||Cytoplasmic|||Decreases salicylate inhibition.|||Disordered|||Extended region for STAS domain|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5a|||Helical; Name=5b|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||Involved in motor function|||N-linked (GlcNAc...) asparagine|||Prestin|||STAS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080167|||http://purl.uniprot.org/annotation/VSP_010190|||http://purl.uniprot.org/annotation/VSP_010191|||http://purl.uniprot.org/annotation/VSP_010192|||http://purl.uniprot.org/annotation/VSP_010193|||http://purl.uniprot.org/annotation/VSP_010194|||http://purl.uniprot.org/annotation/VSP_010195|||http://purl.uniprot.org/annotation/VSP_043153|||http://purl.uniprot.org/annotation/VSP_047640
http://togogenome.org/gene/9606:CYP27A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02318                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Impairs sterol 26-hydroxylase activity.|||Impairs sterol 26-hydroxylase activity; confers demethylase activity.|||Impairs sterol 26-hydroxylase activity; when associated with A-240 and A-244.|||Impairs sterol 26-hydroxylase activity; when associated with A-240 and A-248.|||Impairs sterol 26-hydroxylase activity; when associated with A-244 and A-248.|||In CTX.|||In CTX; impairs sterol 26-hydroxylase activity.|||Mitochondrion|||N6-acetyllysine|||Reduces sterol 26-hydroxylase activity.|||Sterol 26-hydroxylase, mitochondrial|||Sterol-binding|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003618|||http://purl.uniprot.org/annotation/VAR_001303|||http://purl.uniprot.org/annotation/VAR_001304|||http://purl.uniprot.org/annotation/VAR_012285|||http://purl.uniprot.org/annotation/VAR_012286|||http://purl.uniprot.org/annotation/VAR_012287|||http://purl.uniprot.org/annotation/VAR_012288|||http://purl.uniprot.org/annotation/VAR_016966|||http://purl.uniprot.org/annotation/VAR_048467|||http://purl.uniprot.org/annotation/VAR_061046
http://togogenome.org/gene/9606:DCBLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||Cytoplasmic|||Discoidin, CUB and LCCL domain-containing protein 2|||Disordered|||Extracellular|||F5/8 type C|||Helical|||In isoform 2.|||LCCL|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021078|||http://purl.uniprot.org/annotation/VAR_050944|||http://purl.uniprot.org/annotation/VAR_050945|||http://purl.uniprot.org/annotation/VSP_010715
http://togogenome.org/gene/9606:TOR1AIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTV8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Interaction with TOR1A|||Methionine sulfoxide|||N-linked (GlcNAc...) asparagine|||Nuclear|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues|||Torsin-1A-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228835|||http://purl.uniprot.org/annotation/VAR_025717|||http://purl.uniprot.org/annotation/VAR_025718|||http://purl.uniprot.org/annotation/VAR_034566|||http://purl.uniprot.org/annotation/VAR_035818|||http://purl.uniprot.org/annotation/VSP_055704|||http://purl.uniprot.org/annotation/VSP_055705|||http://purl.uniprot.org/annotation/VSP_061934
http://togogenome.org/gene/9606:EDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20800                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cleavage; by KEL|||Disordered|||Endothelin-2|||Endothelin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008093|||http://purl.uniprot.org/annotation/PRO_0000008094|||http://purl.uniprot.org/annotation/PRO_0000008095|||http://purl.uniprot.org/annotation/VAR_018817|||http://purl.uniprot.org/annotation/VAR_033914
http://togogenome.org/gene/9606:IQSEC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPP2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 3|||In isoform 2.|||PH|||Phosphoserine|||Polar residues|||Pro residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245610|||http://purl.uniprot.org/annotation/VAR_061789|||http://purl.uniprot.org/annotation/VSP_035695|||http://purl.uniprot.org/annotation/VSP_035696|||http://purl.uniprot.org/annotation/VSP_035697
http://togogenome.org/gene/9606:EML3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL97|||http://purl.uniprot.org/uniprot/Q32P44                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Echinoderm microtubule-associated protein-like 3|||HELP|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation and impaired interaction with TUBG1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8.|||N-acetylmethionine|||No loss of phosphorylation.|||Phosphoserine|||Phosphothreonine; by CDK1|||Polar residues|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284390|||http://purl.uniprot.org/annotation/VAR_031725|||http://purl.uniprot.org/annotation/VAR_082934|||http://purl.uniprot.org/annotation/VSP_024483|||http://purl.uniprot.org/annotation/VSP_039926|||http://purl.uniprot.org/annotation/VSP_039927|||http://purl.uniprot.org/annotation/VSP_039928
http://togogenome.org/gene/9606:ITGAV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RXH0|||http://purl.uniprot.org/uniprot/P06756                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 2.|||In isoform 3.|||Increases ligand-binding activity.|||Integrin alpha-2|||Integrin alpha-V|||Integrin alpha-V heavy chain|||Integrin alpha-V light chain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016301|||http://purl.uniprot.org/annotation/PRO_0000016302|||http://purl.uniprot.org/annotation/PRO_0000016303|||http://purl.uniprot.org/annotation/PRO_5001425273|||http://purl.uniprot.org/annotation/VAR_024289|||http://purl.uniprot.org/annotation/VAR_031547|||http://purl.uniprot.org/annotation/VAR_055970|||http://purl.uniprot.org/annotation/VSP_024351|||http://purl.uniprot.org/annotation/VSP_044914
http://togogenome.org/gene/9606:ADGRG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SQ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADGRG6 C-terminal fragment|||ADGRG6 N-terminal fragment|||Abolishes G-protein-mediated cAMP release.|||Adhesion G-protein coupled receptor G6|||CUB|||Cleavage|||Cleavage; by furin like-convertase|||Cytoplasmic|||Disordered|||Extracellular|||Found in patients with aggressive periodontitis; impairs cAMP production; abrogates osteoblastic differentiation.|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In LCCS9.|||In LCCS9; decreases the autoprocessing/cleavage of the receptor.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Inhibits receptor signaling in absence of type IV collagen|||Mediates interaction with laminin-2|||Mediates interaction with type IV collagen|||N-linked (GlcNAc...) asparagine|||No cleavage and not detected at the cell surface.|||No cleavage but detected at cell surface.|||No cleavage.|||No effect on G-protein-mediated cAMP release.|||No effect on cleavage.|||Pentraxin (PTX)|||Phosphoserine|||Stachel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012902|||http://purl.uniprot.org/annotation/PRO_0000438596|||http://purl.uniprot.org/annotation/PRO_0000438597|||http://purl.uniprot.org/annotation/VAR_024478|||http://purl.uniprot.org/annotation/VAR_054128|||http://purl.uniprot.org/annotation/VAR_054129|||http://purl.uniprot.org/annotation/VAR_075146|||http://purl.uniprot.org/annotation/VAR_075147|||http://purl.uniprot.org/annotation/VAR_076965|||http://purl.uniprot.org/annotation/VSP_010747|||http://purl.uniprot.org/annotation/VSP_010748
http://togogenome.org/gene/9606:SCHIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPB3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform SCHIP1-2.|||In isoform SCHIP1-3.|||In isoform SCHIP1-4.|||Phosphoserine|||Polar residues|||Schwannomin-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288927|||http://purl.uniprot.org/annotation/VAR_032534|||http://purl.uniprot.org/annotation/VAR_051332|||http://purl.uniprot.org/annotation/VSP_025827|||http://purl.uniprot.org/annotation/VSP_025828|||http://purl.uniprot.org/annotation/VSP_025829|||http://purl.uniprot.org/annotation/VSP_025830
http://togogenome.org/gene/9606:ZHX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||Homeobox 5|||Phosphoserine|||Phosphothreonine|||Required for dimerization|||Required for interaction with NFYA|||Required for nuclear localization|||Required for repressor activity|||Zinc fingers and homeoboxes protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049388
http://togogenome.org/gene/9606:DHRS7C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNS2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 7C|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333755|||http://purl.uniprot.org/annotation/VAR_043150|||http://purl.uniprot.org/annotation/VSP_054852
http://togogenome.org/gene/9606:FUS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35637|||http://purl.uniprot.org/uniprot/Q13344|||http://purl.uniprot.org/uniprot/Q6IBQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Breakpoint for translocation to form FUS/TLS-CHOP oncogene|||Breakpoint for translocation to form chimeric FUS/ATF1 protein|||Disordered|||Does not affect protein nuclear localization.|||Found in a patient with frontotemporal lobar degeneration.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ALS6 and ETM4.|||In ALS6.|||In ALS6; results in aberrant trafficking and cytoplasmic retention of the protein.|||In ALS6; unknown pathological significance.|||In ETM4.|||In a breast cancer sample; somatic mutation.|||In isoform Short.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||RNA-binding protein FUS|||RRM|||RanBP2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081591|||http://purl.uniprot.org/annotation/VAR_035481|||http://purl.uniprot.org/annotation/VAR_054837|||http://purl.uniprot.org/annotation/VAR_054838|||http://purl.uniprot.org/annotation/VAR_054839|||http://purl.uniprot.org/annotation/VAR_054840|||http://purl.uniprot.org/annotation/VAR_054841|||http://purl.uniprot.org/annotation/VAR_054842|||http://purl.uniprot.org/annotation/VAR_054843|||http://purl.uniprot.org/annotation/VAR_054844|||http://purl.uniprot.org/annotation/VAR_054845|||http://purl.uniprot.org/annotation/VAR_054846|||http://purl.uniprot.org/annotation/VAR_054847|||http://purl.uniprot.org/annotation/VAR_054848|||http://purl.uniprot.org/annotation/VAR_054849|||http://purl.uniprot.org/annotation/VAR_065229|||http://purl.uniprot.org/annotation/VAR_068918|||http://purl.uniprot.org/annotation/VAR_068919|||http://purl.uniprot.org/annotation/VAR_068920|||http://purl.uniprot.org/annotation/VAR_068921|||http://purl.uniprot.org/annotation/VAR_068922|||http://purl.uniprot.org/annotation/VAR_068923|||http://purl.uniprot.org/annotation/VAR_068924|||http://purl.uniprot.org/annotation/VAR_077328|||http://purl.uniprot.org/annotation/VSP_005798
http://togogenome.org/gene/9606:KCTD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVF5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD4|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191289
http://togogenome.org/gene/9606:CKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12277|||http://purl.uniprot.org/uniprot/V9HWH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||42% of wild-type activity.|||Basic and acidic residues|||Complete loss of activity.|||Creatine kinase B-type|||Disordered|||Internal MTS-like signal|||No change in activity.|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211966|||http://purl.uniprot.org/annotation/VAR_025838|||http://purl.uniprot.org/annotation/VAR_025839|||http://purl.uniprot.org/annotation/VAR_049674
http://togogenome.org/gene/9606:ZNF362                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0B9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 362                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300812
http://togogenome.org/gene/9606:POR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PY49|||http://purl.uniprot.org/uniprot/P16435                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||FAD-binding FR-type|||Flavodoxin-like|||Helical|||In ABS1 and DISPORD; significant reduction of activity.|||In ABS1.|||In ABS1; significant reduction of activity.|||In DISPORD; complete loss of activity.|||In DISPORD; significant reduction of activity.|||Lumenal|||N-acetylglycine|||NADPH--cytochrome P450 reductase|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167596|||http://purl.uniprot.org/annotation/VAR_004617|||http://purl.uniprot.org/annotation/VAR_004618|||http://purl.uniprot.org/annotation/VAR_021154|||http://purl.uniprot.org/annotation/VAR_021155|||http://purl.uniprot.org/annotation/VAR_021156|||http://purl.uniprot.org/annotation/VAR_021157|||http://purl.uniprot.org/annotation/VAR_021158|||http://purl.uniprot.org/annotation/VAR_021159|||http://purl.uniprot.org/annotation/VAR_021160|||http://purl.uniprot.org/annotation/VAR_021161|||http://purl.uniprot.org/annotation/VAR_047885|||http://purl.uniprot.org/annotation/VAR_047886
http://togogenome.org/gene/9606:TLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15399                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Interaction with bacterial lipopeptide|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||May confer susceptibility to leprosy.|||N-linked (GlcNAc...) asparagine|||Severe impairment of activity.|||TIR|||Toll-like receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034705|||http://purl.uniprot.org/annotation/VAR_018474|||http://purl.uniprot.org/annotation/VAR_031916|||http://purl.uniprot.org/annotation/VAR_031917|||http://purl.uniprot.org/annotation/VAR_031918|||http://purl.uniprot.org/annotation/VAR_031919|||http://purl.uniprot.org/annotation/VAR_031920|||http://purl.uniprot.org/annotation/VAR_031921|||http://purl.uniprot.org/annotation/VAR_052358|||http://purl.uniprot.org/annotation/VAR_052359|||http://purl.uniprot.org/annotation/VAR_066340|||http://purl.uniprot.org/annotation/VAR_066341|||http://purl.uniprot.org/annotation/VAR_066342|||http://purl.uniprot.org/annotation/VAR_066343|||http://purl.uniprot.org/annotation/VAR_066344|||http://purl.uniprot.org/annotation/VAR_066345|||http://purl.uniprot.org/annotation/VAR_066346|||http://purl.uniprot.org/annotation/VAR_066347|||http://purl.uniprot.org/annotation/VAR_066348
http://togogenome.org/gene/9606:TRIAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43715                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Site|||Strand                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Impairs interaction with PRELID3A.|||Important for interaction with PRELID3A|||N-acetylmethionine|||TP53-regulated inhibitor of apoptosis 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220523
http://togogenome.org/gene/9606:ZSWIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEG5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase ZSWIM2|||RING-type 1|||RING-type 2|||SWIM-type|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223097
http://togogenome.org/gene/9606:PCDHB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003938|||http://purl.uniprot.org/annotation/VAR_059189
http://togogenome.org/gene/9606:CCNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20248                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-A2|||Disordered|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080338|||http://purl.uniprot.org/annotation/VAR_018819
http://togogenome.org/gene/9606:MGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWI9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MAX gene-associated protein|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||T-box|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342692|||http://purl.uniprot.org/annotation/VAR_044341|||http://purl.uniprot.org/annotation/VAR_044342|||http://purl.uniprot.org/annotation/VAR_044343|||http://purl.uniprot.org/annotation/VAR_057268|||http://purl.uniprot.org/annotation/VSP_060177
http://togogenome.org/gene/9606:GSKIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0R6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Abolishes interaction with PRKAR2A and PRKAR2B. Abolishes acquired resistance against oxidative stress-induced apoptosis under activated cAMP signaling. Decreases PKA-mediated DNM1L phosphorylation.|||Abolishes interaction with PRKAR2A. Prevents the Wnt-induced transcription. Does not alter the phosphorylation of CTNNB1 in the presence of Wnt.|||Disordered|||GSK3B-interacting protein|||Interaction with GSK3B and acts as GSK3B inhibitor|||Loss of interaction with GSK3B. Abolishes GSK3B-mediated phosphorylation. Prevents beta-catenin accumulation in the cytoplasm and nucleus. Prevents the Wnt-induced transcription. Decreases PKA-mediated phosphorylation of GSK3B. Abolishes acquired resistance against oxidative stress-induced apoptosis under activated cAMP signaling. Decreases PKA-mediated DNM1L phosphorylation.|||No effect on GSK3B-mediated phosphorylation. Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A-109.Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A-113 and A-115.|||No effect on GSK3B-mediated phosphorylation. Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A-109.Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A109 and A-113.|||No effect on GSK3B-mediated phosphorylation. Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A-113. Reduces to 30 % GSK3B-mediated phosphorylation; when associated with A-113 and A-115.|||Required for GSK3B interaction; contributes to a protective effect against H(2)O(2)-induced apoptosis|||Required for PRKAR2A interaction; contributes to a protective effect against H(2)O(2)-induced apoptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220951
http://togogenome.org/gene/9606:SPEG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15772                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||Ig-like 7|||Ig-like 8|||Ig-like 9|||In CNM5.|||In a gastric adenocarcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Striated muscle preferentially expressed protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072666|||http://purl.uniprot.org/annotation/VAR_041101|||http://purl.uniprot.org/annotation/VAR_041102|||http://purl.uniprot.org/annotation/VAR_041103|||http://purl.uniprot.org/annotation/VAR_041104|||http://purl.uniprot.org/annotation/VAR_041105|||http://purl.uniprot.org/annotation/VAR_041106|||http://purl.uniprot.org/annotation/VAR_041107|||http://purl.uniprot.org/annotation/VAR_041108|||http://purl.uniprot.org/annotation/VAR_041109|||http://purl.uniprot.org/annotation/VAR_041110|||http://purl.uniprot.org/annotation/VAR_041111|||http://purl.uniprot.org/annotation/VAR_041112|||http://purl.uniprot.org/annotation/VAR_041113|||http://purl.uniprot.org/annotation/VAR_059769|||http://purl.uniprot.org/annotation/VAR_071808|||http://purl.uniprot.org/annotation/VSP_018258|||http://purl.uniprot.org/annotation/VSP_018259|||http://purl.uniprot.org/annotation/VSP_018261|||http://purl.uniprot.org/annotation/VSP_018262|||http://purl.uniprot.org/annotation/VSP_036071
http://togogenome.org/gene/9606:CRHR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7T4|||http://purl.uniprot.org/uniprot/Q13324                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Corticotropin-releasing factor receptor 2|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform CRF2-beta.|||In isoform CRF2-gamma.|||In isoform D.|||In isoform E.|||In isoform F.|||In isoform desQ.|||N-linked (GlcNAc...) asparagine|||Not cleaved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012820|||http://purl.uniprot.org/annotation/VAR_049455|||http://purl.uniprot.org/annotation/VSP_001999|||http://purl.uniprot.org/annotation/VSP_002000|||http://purl.uniprot.org/annotation/VSP_053564|||http://purl.uniprot.org/annotation/VSP_053565|||http://purl.uniprot.org/annotation/VSP_053566|||http://purl.uniprot.org/annotation/VSP_053567
http://togogenome.org/gene/9606:NCF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z457|||http://purl.uniprot.org/uniprot/A0A8V8TMB9|||http://purl.uniprot.org/uniprot/P19878                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Impairs interaction with NCF4.|||In CGD2.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Neutrophil cytosol factor 2|||PB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||SH3 1|||SH3 2|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106361|||http://purl.uniprot.org/annotation/VAR_008904|||http://purl.uniprot.org/annotation/VAR_008905|||http://purl.uniprot.org/annotation/VAR_017387|||http://purl.uniprot.org/annotation/VAR_017388|||http://purl.uniprot.org/annotation/VAR_017389|||http://purl.uniprot.org/annotation/VAR_017390|||http://purl.uniprot.org/annotation/VAR_018477|||http://purl.uniprot.org/annotation/VAR_018478|||http://purl.uniprot.org/annotation/VAR_034129|||http://purl.uniprot.org/annotation/VAR_034130|||http://purl.uniprot.org/annotation/VAR_052620|||http://purl.uniprot.org/annotation/VAR_052621|||http://purl.uniprot.org/annotation/VAR_065002|||http://purl.uniprot.org/annotation/VAR_065003|||http://purl.uniprot.org/annotation/VAR_065004|||http://purl.uniprot.org/annotation/VAR_065005|||http://purl.uniprot.org/annotation/VAR_065006|||http://purl.uniprot.org/annotation/VAR_065007|||http://purl.uniprot.org/annotation/VAR_065008|||http://purl.uniprot.org/annotation/VAR_065009|||http://purl.uniprot.org/annotation/VAR_065010|||http://purl.uniprot.org/annotation/VAR_065011|||http://purl.uniprot.org/annotation/VAR_065012|||http://purl.uniprot.org/annotation/VAR_065013|||http://purl.uniprot.org/annotation/VAR_065014|||http://purl.uniprot.org/annotation/VAR_065015|||http://purl.uniprot.org/annotation/VAR_065016|||http://purl.uniprot.org/annotation/VAR_065017|||http://purl.uniprot.org/annotation/VSP_045259|||http://purl.uniprot.org/annotation/VSP_045260|||http://purl.uniprot.org/annotation/VSP_045261
http://togogenome.org/gene/9606:NEURL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR09                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||NHR|||Neuralized-like protein 2|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181257|||http://purl.uniprot.org/annotation/VAR_052033
http://togogenome.org/gene/9606:IL1RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6K4|||http://purl.uniprot.org/uniprot/Q9NPH3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for interaction with PTPRD|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-1 receptor accessory protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015450|||http://purl.uniprot.org/annotation/PRO_5002725529|||http://purl.uniprot.org/annotation/VAR_053383|||http://purl.uniprot.org/annotation/VSP_008050|||http://purl.uniprot.org/annotation/VSP_008051|||http://purl.uniprot.org/annotation/VSP_008052|||http://purl.uniprot.org/annotation/VSP_041256
http://togogenome.org/gene/9606:KRT39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6A163                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cytoskeletal 39|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314853|||http://purl.uniprot.org/annotation/VAR_038075|||http://purl.uniprot.org/annotation/VAR_038076|||http://purl.uniprot.org/annotation/VAR_038077
http://togogenome.org/gene/9606:SLC17A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYT1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In POROK8.|||In isoform 2.|||In isoform 3.|||Voltage-gated purine nucleotide uniporter SLC17A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084849|||http://purl.uniprot.org/annotation/VAR_055326|||http://purl.uniprot.org/annotation/VAR_056128|||http://purl.uniprot.org/annotation/VAR_071983|||http://purl.uniprot.org/annotation/VAR_071984|||http://purl.uniprot.org/annotation/VSP_010344|||http://purl.uniprot.org/annotation/VSP_010345|||http://purl.uniprot.org/annotation/VSP_010346
http://togogenome.org/gene/9606:LRRC47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1G4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 47|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223926|||http://purl.uniprot.org/annotation/VAR_035471|||http://purl.uniprot.org/annotation/VAR_051118|||http://purl.uniprot.org/annotation/VAR_051119
http://togogenome.org/gene/9606:SPATA31D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Spermatogenesis-associated protein 31D4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332289
http://togogenome.org/gene/9606:PROX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V3G0|||http://purl.uniprot.org/uniprot/Q3B8N5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with intellectual disability, seizures, mild hypotonia and no speech.|||Homeo-Prospero|||In isoform 2.|||Polar residues|||Pro residues|||Prospero|||Prospero homeobox protein 2|||Prospero-type homeo                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342677|||http://purl.uniprot.org/annotation/VAR_069378|||http://purl.uniprot.org/annotation/VSP_034528
http://togogenome.org/gene/9606:AMOTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2J4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Angiomotin-like protein 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ-binding|||Phosphoserine|||Phosphotyrosine; by FGFR1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190672|||http://purl.uniprot.org/annotation/VAR_023535|||http://purl.uniprot.org/annotation/VAR_055497|||http://purl.uniprot.org/annotation/VAR_055498|||http://purl.uniprot.org/annotation/VAR_055499|||http://purl.uniprot.org/annotation/VSP_015711|||http://purl.uniprot.org/annotation/VSP_037826|||http://purl.uniprot.org/annotation/VSP_044081
http://togogenome.org/gene/9606:IMPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29218                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  50-fold reduction in activity.|||In isoform 2.|||In isoform 3.|||Inositol monophosphatase 1|||Loss of activity.|||Phosphothreonine|||Reduced enzyme activity with myo-inositol 1-phosphate.|||Strongly reduced affinity for myo-inositol 1-phosphate and strongly reduced enzyme activity with myo-inositol 1-phosphate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142513|||http://purl.uniprot.org/annotation/VAR_049600|||http://purl.uniprot.org/annotation/VSP_042521|||http://purl.uniprot.org/annotation/VSP_046308
http://togogenome.org/gene/9606:EIF3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14152                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||20|||21|||22|||23; truncated|||24|||25 X 10 AA approximate tandem repeats of [DE]-[DE]-[DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT]|||25; approximate|||2; truncated|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit A|||In isoform 2.|||Interaction with EIF3B|||N6-acetyllysine|||PCI|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123537|||http://purl.uniprot.org/annotation/VAR_024438|||http://purl.uniprot.org/annotation/VAR_048921|||http://purl.uniprot.org/annotation/VAR_048922|||http://purl.uniprot.org/annotation/VSP_055471
http://togogenome.org/gene/9606:ZNF470                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ECI4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Nuclear localization signal|||Zinc finger protein 470                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280413|||http://purl.uniprot.org/annotation/VAR_031143|||http://purl.uniprot.org/annotation/VAR_031144|||http://purl.uniprot.org/annotation/VAR_031145|||http://purl.uniprot.org/annotation/VAR_061950|||http://purl.uniprot.org/annotation/VSP_023660|||http://purl.uniprot.org/annotation/VSP_023661
http://togogenome.org/gene/9606:HTRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDW9|||http://purl.uniprot.org/uniprot/A0A8Q3SIX7|||http://purl.uniprot.org/uniprot/O43464                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Helical|||IAP-binding motif|||In MGCA8; loss of protein expression.|||In MGCA8; may lead to skipping of exon 7 and the resultant protein may be truncated; loss of protein expression in patient cells homozygous for the mutation.|||In PARK13.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with XIAP. Loss of inhibition of XIAP activity.|||Loss of protease activity.|||May be a risk factor for Parkinson disease; reduced protease activity.|||Mitochondrion|||PDZ|||Serine protease|||Serine protease HTRA2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026945|||http://purl.uniprot.org/annotation/PRO_0000026946|||http://purl.uniprot.org/annotation/VAR_027349|||http://purl.uniprot.org/annotation/VAR_027350|||http://purl.uniprot.org/annotation/VAR_046134|||http://purl.uniprot.org/annotation/VAR_046135|||http://purl.uniprot.org/annotation/VAR_076967|||http://purl.uniprot.org/annotation/VAR_076968|||http://purl.uniprot.org/annotation/VAR_076969|||http://purl.uniprot.org/annotation/VAR_077960|||http://purl.uniprot.org/annotation/VAR_077961|||http://purl.uniprot.org/annotation/VSP_005359|||http://purl.uniprot.org/annotation/VSP_005360|||http://purl.uniprot.org/annotation/VSP_005361|||http://purl.uniprot.org/annotation/VSP_005362
http://togogenome.org/gene/9606:SRPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SB4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1.|||In isoform 3.|||No effect on protein phosphorylation.|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues|||Protein kinase|||Protein phosphorylation impaired at this position.|||Proton acceptor|||SRSF protein kinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086674|||http://purl.uniprot.org/annotation/VAR_051669|||http://purl.uniprot.org/annotation/VSP_042130|||http://purl.uniprot.org/annotation/VSP_057356
http://togogenome.org/gene/9606:FBXO24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2D3|||http://purl.uniprot.org/uniprot/O75426                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 24|||In isoform 2.|||In isoform 3.|||In isoform 4.|||RCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119909|||http://purl.uniprot.org/annotation/VAR_049042|||http://purl.uniprot.org/annotation/VSP_011351|||http://purl.uniprot.org/annotation/VSP_011352|||http://purl.uniprot.org/annotation/VSP_011353|||http://purl.uniprot.org/annotation/VSP_043458|||http://purl.uniprot.org/annotation/VSP_043459
http://togogenome.org/gene/9606:LEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q659G9|||http://purl.uniprot.org/uniprot/Q9UJU2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CTNNB1-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||HMG box|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Lymphoid enhancer-binding factor 1|||Phosphoserine|||Phosphoserine; by NLK|||Phosphothreonine; by NLK|||Reduced phosphorylation by NLK; when associated with A-155.|||Reduced phosphorylation by NLK; when associated with A-166.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048595|||http://purl.uniprot.org/annotation/VAR_035935|||http://purl.uniprot.org/annotation/VSP_002188|||http://purl.uniprot.org/annotation/VSP_007022|||http://purl.uniprot.org/annotation/VSP_040068|||http://purl.uniprot.org/annotation/VSP_040069|||http://purl.uniprot.org/annotation/VSP_044877
http://togogenome.org/gene/9606:FLVCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPI3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6; approximate|||7; approximate|||8|||8 X 6 AA tandem repeats of P-S-[VS]-S-[VIAG]-[HNP]|||Basic and acidic residues|||Disordered|||Helical|||Heme transporter FLVCR2|||In PVHH.|||In isoform 2.|||Loss of heme-binding activity.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084846|||http://purl.uniprot.org/annotation/VAR_018271|||http://purl.uniprot.org/annotation/VAR_050299|||http://purl.uniprot.org/annotation/VAR_064043|||http://purl.uniprot.org/annotation/VAR_064044|||http://purl.uniprot.org/annotation/VAR_064045|||http://purl.uniprot.org/annotation/VAR_064410|||http://purl.uniprot.org/annotation/VAR_064411|||http://purl.uniprot.org/annotation/VAR_064412|||http://purl.uniprot.org/annotation/VAR_064413|||http://purl.uniprot.org/annotation/VAR_064414|||http://purl.uniprot.org/annotation/VAR_064415|||http://purl.uniprot.org/annotation/VSP_043048|||http://purl.uniprot.org/annotation/VSP_043049
http://togogenome.org/gene/9606:FAM98B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LJ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||Protein FAM98B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187188|||http://purl.uniprot.org/annotation/VSP_060151|||http://purl.uniprot.org/annotation/VSP_060152
http://togogenome.org/gene/9606:RIOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6M8YDW1|||http://purl.uniprot.org/uniprot/Q8IUF8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes demethylase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||JmjC|||Phosphoserine|||Ribosomal oxygenase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308377|||http://purl.uniprot.org/annotation/VAR_036811|||http://purl.uniprot.org/annotation/VAR_054079|||http://purl.uniprot.org/annotation/VAR_062241|||http://purl.uniprot.org/annotation/VSP_038373|||http://purl.uniprot.org/annotation/VSP_052587|||http://purl.uniprot.org/annotation/VSP_052588|||http://purl.uniprot.org/annotation/VSP_052589|||http://purl.uniprot.org/annotation/VSP_052590
http://togogenome.org/gene/9606:USP54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7X1|||http://purl.uniprot.org/uniprot/Q70EL1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Inactive ubiquitin carboxyl-terminal hydrolase 54|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249530|||http://purl.uniprot.org/annotation/VAR_036360|||http://purl.uniprot.org/annotation/VAR_047258|||http://purl.uniprot.org/annotation/VAR_047259|||http://purl.uniprot.org/annotation/VAR_047260|||http://purl.uniprot.org/annotation/VSP_026525|||http://purl.uniprot.org/annotation/VSP_026526|||http://purl.uniprot.org/annotation/VSP_029922|||http://purl.uniprot.org/annotation/VSP_035674|||http://purl.uniprot.org/annotation/VSP_035675|||http://purl.uniprot.org/annotation/VSP_035676|||http://purl.uniprot.org/annotation/VSP_035677|||http://purl.uniprot.org/annotation/VSP_035678
http://togogenome.org/gene/9606:NAA20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZB2|||http://purl.uniprot.org/uniprot/P61599                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MRT73.|||In MRT73; decreased complex formation with NAA25 and decreased N-acetylation catalytic activity in vitro for all 4 types of substrates; does not affect protein stability.|||In MRT73; decreases interaction with NAA25; may reduce protein capacity to acetylate Met-Glu N-terminal peptides; does not affect protein stability.|||In MRT73; strong decrease in N-acetylation catalytic activity in vitro for substrates Met-Glu, Met-Asn and Met-Gln, but not Met-Asp; does not affect protein stability.|||In isoform 2.|||N-acetyltransferase|||N-alpha-acetyltransferase 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074534|||http://purl.uniprot.org/annotation/VAR_086809|||http://purl.uniprot.org/annotation/VAR_086810|||http://purl.uniprot.org/annotation/VAR_088425|||http://purl.uniprot.org/annotation/VAR_088426|||http://purl.uniprot.org/annotation/VSP_045644
http://togogenome.org/gene/9606:CHMP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZZ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  (Microbial infection) N6-stearoyl lysine|||Charged multivesicular body protein 5|||Decreased stearoylation in response to S.flexneri infection.|||Disordered|||In isoform 2.|||Interaction with VTA1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211500|||http://purl.uniprot.org/annotation/VSP_042556
http://togogenome.org/gene/9606:TMPRSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15393                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interchain (between non-catalytic and catalytic chains)|||LDL-receptor class A|||Loss of activity.|||Loss of cleavage.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Transmembrane protease serine 2 catalytic chain|||Transmembrane protease serine 2 non-catalytic chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027855|||http://purl.uniprot.org/annotation/PRO_0000027856|||http://purl.uniprot.org/annotation/VAR_011692|||http://purl.uniprot.org/annotation/VAR_027674|||http://purl.uniprot.org/annotation/VAR_038002|||http://purl.uniprot.org/annotation/VAR_038003|||http://purl.uniprot.org/annotation/VAR_038004|||http://purl.uniprot.org/annotation/VAR_084538|||http://purl.uniprot.org/annotation/VAR_084539|||http://purl.uniprot.org/annotation/VAR_084540|||http://purl.uniprot.org/annotation/VAR_084541|||http://purl.uniprot.org/annotation/VSP_045083
http://togogenome.org/gene/9606:CSRNP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteine/serine-rich nuclear protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114786|||http://purl.uniprot.org/annotation/VAR_055100
http://togogenome.org/gene/9606:KATNAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUK7|||http://purl.uniprot.org/uniprot/Q9BW62                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Basic and acidic residues|||Disordered|||Katanin p60 ATPase-containing subunit A-like 1|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by DYRK2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084601
http://togogenome.org/gene/9606:SGSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X241|||http://purl.uniprot.org/uniprot/Q2NKQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Important for interaction with RAB9A and RAB9B|||In isoform 2 and isoform 3.|||In isoform 2.|||Polar residues|||RUN|||Rab-GAP TBC|||Required for interaction with RAP family members|||Small G protein signaling modulator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284833|||http://purl.uniprot.org/annotation/VAR_031834|||http://purl.uniprot.org/annotation/VAR_031835|||http://purl.uniprot.org/annotation/VSP_024665|||http://purl.uniprot.org/annotation/VSP_024666|||http://purl.uniprot.org/annotation/VSP_024667|||http://purl.uniprot.org/annotation/VSP_024668
http://togogenome.org/gene/9606:ZNF485                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCK3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 485                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223953|||http://purl.uniprot.org/annotation/VAR_059920|||http://purl.uniprot.org/annotation/VSP_055957
http://togogenome.org/gene/9606:MRPS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D3                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrion|||Phosphothreonine|||Small ribosomal subunit protein bS16m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030618|||http://purl.uniprot.org/annotation/VAR_031525|||http://purl.uniprot.org/annotation/VSP_056498
http://togogenome.org/gene/9606:HECW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76N89                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase HECW1|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Phosphoserine|||Polar residues|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277665|||http://purl.uniprot.org/annotation/VSP_054642
http://togogenome.org/gene/9606:CYP19A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11511|||http://purl.uniprot.org/uniprot/Q05CU4|||http://purl.uniprot.org/uniprot/Q8TCA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  1.6 fold decrease in affinity for androstenedione substrate; slightly affects PKA-mediated reduction in catalytic activity as measured in vitro by estrone synthesis from androstenedione (49% decrease compared with 36% for the wild-type protein); no effect on PKG/PRKG1-mediated reduction in catalytic activity in vitro.|||2.5 fold decrease in affinity for androstenedione substrate; slightly affects PKA-mediated reduction in catalytic activity as measured by estrone synthesis from androstenedione in vitro (28% decrease compared with 36% for the wild-type protein) and PKG/PRKG1-mediated reduction in catalytic activity in vitro (15% decrease compared with 30% for the wild-type protein).|||Aromatase|||Found in deaf patients; unknown pathological significance.|||Helical|||In AROD.|||In AROD; 0.4% of wild-type activity.|||In AROD; 1.1% of wild-type activity.|||In AROD; complete loss of activity.|||In AROD; strongly reduced aromatase activity; 81% reduction of androstenedione metabolism compared to wild-type.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051955|||http://purl.uniprot.org/annotation/VAR_016962|||http://purl.uniprot.org/annotation/VAR_016963|||http://purl.uniprot.org/annotation/VAR_016964|||http://purl.uniprot.org/annotation/VAR_016965|||http://purl.uniprot.org/annotation/VAR_018406|||http://purl.uniprot.org/annotation/VAR_023428|||http://purl.uniprot.org/annotation/VAR_023429|||http://purl.uniprot.org/annotation/VAR_054152|||http://purl.uniprot.org/annotation/VAR_072784|||http://purl.uniprot.org/annotation/VAR_077526|||http://purl.uniprot.org/annotation/VAR_079486|||http://purl.uniprot.org/annotation/VSP_055583|||http://purl.uniprot.org/annotation/VSP_055584
http://togogenome.org/gene/9606:TMEM51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSA0|||http://purl.uniprot.org/uniprot/Q9NW97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Polar residues|||Transmembrane protein 51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072577|||http://purl.uniprot.org/annotation/VAR_051446|||http://purl.uniprot.org/annotation/VAR_051447
http://togogenome.org/gene/9606:CLEC4F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z704|||http://purl.uniprot.org/uniprot/B7ZMM1|||http://purl.uniprot.org/uniprot/Q8N1N0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member F|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046622|||http://purl.uniprot.org/annotation/VAR_054429|||http://purl.uniprot.org/annotation/VAR_054430|||http://purl.uniprot.org/annotation/VAR_054431|||http://purl.uniprot.org/annotation/VSP_056330
http://togogenome.org/gene/9606:PAPSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43252                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  30% decrease in activity.|||Abolishes inhibition by the substrate adenylyl sulfate.|||Adenylyl-sulfate kinase|||Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1|||Increased activity.|||Loss of activity.|||N-acetylmethionine|||N6-acetyllysine|||Sulfate adenylyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105959|||http://purl.uniprot.org/annotation/VAR_014064|||http://purl.uniprot.org/annotation/VAR_014065
http://togogenome.org/gene/9606:LRP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H02|||http://purl.uniprot.org/uniprot/Q9Y561                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CUB|||CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||Low-density lipoprotein receptor-related protein 12|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017339|||http://purl.uniprot.org/annotation/VAR_049766|||http://purl.uniprot.org/annotation/VSP_040992
http://togogenome.org/gene/9606:SYT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0AZL9|||http://purl.uniprot.org/uniprot/Q8IV01|||http://purl.uniprot.org/uniprot/Q8NDM9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||Phosphoserine|||Synaptotagmin-12|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183972|||http://purl.uniprot.org/annotation/VAR_034532
http://togogenome.org/gene/9606:SEPHS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99611                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Non standard residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Disordered|||Important for catalytic activity|||N-acetylalanine|||Phosphoserine|||Removed|||Selenide, water dikinase 2|||Selenocysteine|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127650|||http://purl.uniprot.org/annotation/VAR_052345
http://togogenome.org/gene/9606:BARX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein BarH-like 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048834|||http://purl.uniprot.org/annotation/VAR_010927|||http://purl.uniprot.org/annotation/VSP_034700
http://togogenome.org/gene/9606:TYMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04818|||http://purl.uniprot.org/uniprot/Q53Y97                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DKCD.|||In DKCD; reduced TYMS levels in patient cells.|||In DKCD; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoserine|||Removed|||Thymidylate synthase|||Thymidylate synthase/dCMP hydroxymethylase|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140901|||http://purl.uniprot.org/annotation/VAR_087693|||http://purl.uniprot.org/annotation/VAR_087694|||http://purl.uniprot.org/annotation/VAR_087695|||http://purl.uniprot.org/annotation/VAR_087696|||http://purl.uniprot.org/annotation/VSP_047745|||http://purl.uniprot.org/annotation/VSP_047746
http://togogenome.org/gene/9606:NPTX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15818                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In SCA50.|||In SCA50; does not affect secretion; does not affect multimerization.|||In SCA50; unknown pathological significance.|||In SCA50; unknown pathological significance; abolishes secretion; loss of multimerization ability.|||N-linked (GlcNAc...) asparagine|||Neuronal pentraxin-1|||Pentraxin (PTX)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023547|||http://purl.uniprot.org/annotation/VAR_087974|||http://purl.uniprot.org/annotation/VAR_087975|||http://purl.uniprot.org/annotation/VAR_087976|||http://purl.uniprot.org/annotation/VAR_087977
http://togogenome.org/gene/9606:GCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30793|||http://purl.uniprot.org/uniprot/Q8IZH9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in patients with DRD; unknown pathological significance.|||GTP cyclohydrolase 1|||GTP cyclohydrolase I|||In DRD.|||In HGCH-3.|||In HPABH4B and DRD; phenotype presenting with dystonia and myoclonus.|||In HPABH4B; intermediate phenotype presenting with dystonia and motor delay.|||In HPABH4B; severe hyperphenylalaninemia.|||In isoform GCH-2.|||In isoform GCH-3.|||In isoform GCH-4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119478|||http://purl.uniprot.org/annotation/VAR_002632|||http://purl.uniprot.org/annotation/VAR_002633|||http://purl.uniprot.org/annotation/VAR_002634|||http://purl.uniprot.org/annotation/VAR_002635|||http://purl.uniprot.org/annotation/VAR_002636|||http://purl.uniprot.org/annotation/VAR_002637|||http://purl.uniprot.org/annotation/VAR_002638|||http://purl.uniprot.org/annotation/VAR_002639|||http://purl.uniprot.org/annotation/VAR_002640|||http://purl.uniprot.org/annotation/VAR_002641|||http://purl.uniprot.org/annotation/VAR_002642|||http://purl.uniprot.org/annotation/VAR_002643|||http://purl.uniprot.org/annotation/VAR_002644|||http://purl.uniprot.org/annotation/VAR_002645|||http://purl.uniprot.org/annotation/VAR_002646|||http://purl.uniprot.org/annotation/VAR_002647|||http://purl.uniprot.org/annotation/VAR_002648|||http://purl.uniprot.org/annotation/VAR_002649|||http://purl.uniprot.org/annotation/VAR_016888|||http://purl.uniprot.org/annotation/VAR_016889|||http://purl.uniprot.org/annotation/VAR_016890|||http://purl.uniprot.org/annotation/VAR_016891|||http://purl.uniprot.org/annotation/VAR_016892|||http://purl.uniprot.org/annotation/VAR_016893|||http://purl.uniprot.org/annotation/VAR_016894|||http://purl.uniprot.org/annotation/VAR_016895|||http://purl.uniprot.org/annotation/VAR_016896|||http://purl.uniprot.org/annotation/VAR_016897|||http://purl.uniprot.org/annotation/VAR_016898|||http://purl.uniprot.org/annotation/VAR_016899|||http://purl.uniprot.org/annotation/VAR_016900|||http://purl.uniprot.org/annotation/VAR_016901|||http://purl.uniprot.org/annotation/VAR_016902|||http://purl.uniprot.org/annotation/VAR_016903|||http://purl.uniprot.org/annotation/VAR_016904|||http://purl.uniprot.org/annotation/VAR_016905|||http://purl.uniprot.org/annotation/VAR_016906|||http://purl.uniprot.org/annotation/VAR_016907|||http://purl.uniprot.org/annotation/VAR_054112|||http://purl.uniprot.org/annotation/VAR_072733|||http://purl.uniprot.org/annotation/VAR_072734|||http://purl.uniprot.org/annotation/VAR_072735|||http://purl.uniprot.org/annotation/VSP_001610|||http://purl.uniprot.org/annotation/VSP_001611|||http://purl.uniprot.org/annotation/VSP_001612|||http://purl.uniprot.org/annotation/VSP_001613|||http://purl.uniprot.org/annotation/VSP_001614
http://togogenome.org/gene/9606:PSMB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28070                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  In PRAAS3; decreased protein maturation; changed proteasome assembly; poor incorporation into 20S and 26S proteasomes.|||In PRAAS3; digenic inheritance; patient also carries a mutation in PSMB8; no effect on protein abundance; changed proteasome assembly; poor incorporation into 20S and 26S proteasomes.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit beta type-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026579|||http://purl.uniprot.org/annotation/PRO_0000026580|||http://purl.uniprot.org/annotation/VAR_012072|||http://purl.uniprot.org/annotation/VAR_013115|||http://purl.uniprot.org/annotation/VAR_075255|||http://purl.uniprot.org/annotation/VAR_081126
http://togogenome.org/gene/9606:TMTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUR5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 1 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Protein O-mannosyl-transferase TMTC1|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280288|||http://purl.uniprot.org/annotation/VAR_031112|||http://purl.uniprot.org/annotation/VSP_023611|||http://purl.uniprot.org/annotation/VSP_023612|||http://purl.uniprot.org/annotation/VSP_023613|||http://purl.uniprot.org/annotation/VSP_023614|||http://purl.uniprot.org/annotation/VSP_023615|||http://purl.uniprot.org/annotation/VSP_023616|||http://purl.uniprot.org/annotation/VSP_023617|||http://purl.uniprot.org/annotation/VSP_041823
http://togogenome.org/gene/9606:KARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15046                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of tRNA ligase activity.|||Basic and acidic residues|||Disordered|||Disrupts interaction with AIMP2 and the multisynthase complex.|||Disrupts interaction with AIMP2 and the multisynthase complex. Increases production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity.|||Found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; unknown pathological significance.|||In CMTRIB.|||In CMTRIB; severely affects enzyme activity.|||In DEAPLE and LEPID; decreases tRNA-lysine aminoacylation; induces protein aggregation; releases from the subunit complex; no effect on cytoplasmic location; no effect on oligomerization.|||In DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation.|||In DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization.|||In DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation.|||In DEAPLE; unknown pathological significance.|||In DFNB89.|||In LEPID; decreases tRNA-lysine aminoacylation activity of both the mitochondrial and cytosolic forms. Does not rescue the developmental defects caused by KARS1 depletion in xenopus.|||In LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus.|||In LEPID; unknown pathological significance.|||In isoform Mitochondrial.|||Induces protein aggregation. Releases from the subunit complex.|||Loss of nuclear localization, but no effect on packaging into HIV-1.|||Lysine--tRNA ligase|||N-acetylalanine|||N6-acetyllysine|||Phosphomimetic mutant that strongly enhances translocation into the nucleus and production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Strongly decreased tRNA ligase activity.|||Strongly reduced production of diadenosine tetraphosphate (Ap4A). Reduced protein phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152765|||http://purl.uniprot.org/annotation/VAR_016105|||http://purl.uniprot.org/annotation/VAR_052640|||http://purl.uniprot.org/annotation/VAR_064911|||http://purl.uniprot.org/annotation/VAR_064912|||http://purl.uniprot.org/annotation/VAR_070233|||http://purl.uniprot.org/annotation/VAR_070234|||http://purl.uniprot.org/annotation/VAR_079741|||http://purl.uniprot.org/annotation/VAR_079742|||http://purl.uniprot.org/annotation/VAR_079743|||http://purl.uniprot.org/annotation/VAR_079744|||http://purl.uniprot.org/annotation/VAR_079745|||http://purl.uniprot.org/annotation/VAR_079746|||http://purl.uniprot.org/annotation/VAR_085386|||http://purl.uniprot.org/annotation/VAR_085387|||http://purl.uniprot.org/annotation/VAR_085388|||http://purl.uniprot.org/annotation/VAR_085389|||http://purl.uniprot.org/annotation/VAR_085390|||http://purl.uniprot.org/annotation/VAR_085391|||http://purl.uniprot.org/annotation/VSP_038481
http://togogenome.org/gene/9606:ESM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ30                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Endothelial cell-specific molecule 1|||IGFBP N-terminal|||In isoform 2.|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014394|||http://purl.uniprot.org/annotation/VSP_042631
http://togogenome.org/gene/9606:LMNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MQX1|||http://purl.uniprot.org/uniprot/P02545|||http://purl.uniprot.org/uniprot/Q5TCI8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by endoprotease|||Coil 1A|||Coil 1B|||Coil 2|||Completely inhibits tail cleavage.|||Cysteine methyl ester|||Decreased accumulation to the double-strand break (DSB) sites.|||Decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death.|||Disordered|||Does not affect tail cleavage.|||Found in patient with atrial fibrillation.|||Found in patients with atrial fibrillation; unknown pathological significance.|||Found in patients with lipodystrophy; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2.|||Found in patients with skeletal and cardiac muscular dystrophies; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2.|||Found in patients with skeletal and cardiac muscular dystrophies; unknown pathological significance; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||Heptad change of phase|||IF rod|||In CMD1A and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In CMD1A, FPLD2 and MADA.|||In CMD1A.|||In CMD1A; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci.|||In CMD1A; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death.|||In CMD1A; dramatically aberrant localization with almost no nuclear rim staining and formation of intranuclear foci.|||In CMD1A; dramatically aberrant localization with almost no nuclear rim staining and increased formation of intranuclear foci.|||In CMD1A; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In CMD1A; dramatically increases the size of intranuclear speckles and reduces their number; this phenotype is only partially reversed by coexpression of the G-192 mutation and wild-type lamin-C; precludes insertion of lamin-C into the nuclear envelope when co-transfected with the G-192 LMNA; G-192 lamin-C expression totally disrupts the SUMO1 pattern.|||In CMD1A; grossly abnormal nuclear shape with the nuclear envelope producing prominent lobules in about 10% of cultured skin fibroblasts from heterozygous patients.|||In CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In CMD1A; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreased sumoylation; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; associated with increased cell death.|||In CMD1A; no effect on nuclear morphology and lamin A localization.|||In CMD1A; no effect on nuclear morphology but restricts lamin A to the cytoplasm.|||In CMD1A; unknown pathological significance.|||In CMDA1.|||In CMDHH.|||In CMDHH; phenotype originally designated as atypical Werner syndrome.|||In CMT2; autosomal dominant form.|||In CMT2B1.|||In EDMD2 and CMD1A; aberrant localization with decreased nuclear rim staining and increased formation of intranuclear foci.|||In EDMD2 and CMD1A; modest and non-specific nuclear membrane alterations; the phenotype is entirely reversed by coexpression of the S-541 mutation and wild-type lamin-C.|||In EDMD2 and FPLD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; abnormal nuclear localization; forms nuclear foci in about 13% of cultured skin fibroblasts from heterozygous patients; no effect on protein level.|||In EDMD2 and MDCL.|||In EDMD2 and MDCL; aberrant localization with decreased nuclear rim staining and formation of intranuclear foci when transfected in C2C12 myoblasts; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; interacts with itself and with wild-type LMNA and LMNB1; no effect on protein level.|||In EDMD2.|||In EDMD2; abnormal nuclear localization in a honeycomb expression pattern in about 11% of cultured skin fibroblasts from heterozygous patients; no effect on protein level.|||In EDMD2; abnormal nuclear localization in a honeycomb expression pattern in about 22% of cultured skin fibroblasts from heterozygous patients; enhances the interaction with SYNE2; no effect on nuclear localization; no effect on protein level.|||In EDMD2; abnormal nuclear localization; forms nuclear foci in about 8% of cultured skin fibroblasts from heterozygous patients; interacts with itself and with wild-type LMNA and LMNB1; no effect on protein level.|||In EDMD2; dramatically aberrant localization with decreased nuclear rim staining and formation of intranuclear foci; distribution of endogenous LMNA, LMNB1 and LMNB2 are altered in cells expressing this mutant; causes an increased loss of endogenous EMD from the nuclear envelope; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In EDMD2; found also in a patient with limb-girdle muscular dystrophy; sporadic.|||In EDMD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In EDMD2; interacts with itself and with wild-type LMNA and LMNB1; reduced binding to SUN1; no decrease in the stability compared with wild-type.|||In EDMD2; mis-localized in the nucleus; causes nuclear deformations and LMNB1 redistribution.|||In EDMD2; mis-localized in the nucleus; does not alter nuclear size or shape.|||In EDMD2; mislocalized in the nucleus; does not alter nuclear size or shape.|||In EDMD2; no effect on protein level; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients.|||In EDMD2; no obvious effect on nuclear morphology in cultured skin fibroblasts from heterozygous patients; no effect on protein level.|||In EDMD3.|||In FPLD2 and CMD1A; no effect on nuclear morphology and lamin A localization.|||In FPLD2.|||In FPLD2; abnormal nuclear localization in a honeycomb expression pattern in about 10% of cultured skin fibroblasts from heterozygous patients; no effect on protein level.|||In FPLD2; increase in nuclear blebbing and formation of honeycomb-like structures in the nuclei with no accumulation of prelamin A in skin fibroblasts; causes oligomerization of the C-terminal globular domain of lamins A and C under no-reducing conditions and increases binding affinity for DNA; increases sensitivity to oxidative stress; no significant differences in stability and structure compared with the wild-type.|||In FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type.|||In FPLD2; interacts with itself and with wild-type LMNA and LMNB1; no decrease in the stability compared with wild-type; decreases binding affinity for DNA; increases sensitivity to oxidative stress.|||In HGPS and EDMD2; unknown pathological significance; partially inhibits tail cleavage.|||In HGPS.|||In HGPS; atypical form with late onset; abnormal nuclear morphology with single or multple blebs, lobulation and occasional ringed or donut shaped nuclei.|||In HGPS; atypical.|||In HGPS; might be associated with early and severe strokes.|||In HGPS; phenotype originally designated as atypical Werner syndrome.|||In HGPS; reduced binding to SUN1; may affect splicing by activating a cryptic splice donor site.|||In MADA.|||In MDCL and EDMD2.|||In MDCL and EDMD2; mislocalized in the nucleus; causes nuclear deformations and LMNB1 redistribution.|||In MDCL.|||In an atypical progeroid patient; diagnosed as Seip syndrome; unknown pathological significance.|||In an atypical progeroid patient; diagnosed as Werner syndrome.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform ADelta10.|||In isoform C.|||Increased accumulation to the double-strand break (DSB) sites.|||Interaction with MLIP|||LTD|||Lamin-A/C|||Linker 1|||Linker 2|||Loss of interaction with IFFO1.|||Loss of interaction with NARF. Abolishes farnesylation.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Necessary and sufficient for the interaction with IFFO1|||Nuclear localization signal|||Partially inhibits tail cleavage.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prelamin-A/C|||Probable disease-associated variant found in a patient with metabolic syndrome.|||Probable disease-associated variant found in patient with severe metabolic syndrome; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2.|||Probable disease-associated variant found in patients with metabolic syndromes; no effect on nuclear lamin A localization; no effect on the interaction with SYNE2.|||Rare variant; found in patients with atrial fibrillation; unknown pathological significance; no effect on nuclear lamin A localization; enhances the interaction with SYNE2; causes nuclear deformations in heat shock experiments.|||Removed in Lamin-A/C form|||Removed in Prelamin-A/C form and in Lamin-A/C form|||S-farnesyl cysteine|||Stutter|||Tail ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063810|||http://purl.uniprot.org/annotation/PRO_0000398835|||http://purl.uniprot.org/annotation/PRO_0000398836|||http://purl.uniprot.org/annotation/PRO_0000403442|||http://purl.uniprot.org/annotation/VAR_009971|||http://purl.uniprot.org/annotation/VAR_009972|||http://purl.uniprot.org/annotation/VAR_009974|||http://purl.uniprot.org/annotation/VAR_009975|||http://purl.uniprot.org/annotation/VAR_009976|||http://purl.uniprot.org/annotation/VAR_009977|||http://purl.uniprot.org/annotation/VAR_009978|||http://purl.uniprot.org/annotation/VAR_009979|||http://purl.uniprot.org/annotation/VAR_009980|||http://purl.uniprot.org/annotation/VAR_009981|||http://purl.uniprot.org/annotation/VAR_009982|||http://purl.uniprot.org/annotation/VAR_009983|||http://purl.uniprot.org/annotation/VAR_009984|||http://purl.uniprot.org/annotation/VAR_009985|||http://purl.uniprot.org/annotation/VAR_009986|||http://purl.uniprot.org/annotation/VAR_009987|||http://purl.uniprot.org/annotation/VAR_009988|||http://purl.uniprot.org/annotation/VAR_009989|||http://purl.uniprot.org/annotation/VAR_009990|||http://purl.uniprot.org/annotation/VAR_009991|||http://purl.uniprot.org/annotation/VAR_009992|||http://purl.uniprot.org/annotation/VAR_009993|||http://purl.uniprot.org/annotation/VAR_009994|||http://purl.uniprot.org/annotation/VAR_009995|||http://purl.uniprot.org/annotation/VAR_009996|||http://purl.uniprot.org/annotation/VAR_009997|||http://purl.uniprot.org/annotation/VAR_009998|||http://purl.uniprot.org/annotation/VAR_016205|||http://purl.uniprot.org/annotation/VAR_016913|||http://purl.uniprot.org/annotation/VAR_017656|||http://purl.uniprot.org/annotation/VAR_017657|||http://purl.uniprot.org/annotation/VAR_017658|||http://purl.uniprot.org/annotation/VAR_017659|||http://purl.uniprot.org/annotation/VAR_017660|||http://purl.uniprot.org/annotation/VAR_017661|||http://purl.uniprot.org/annotation/VAR_017662|||http://purl.uniprot.org/annotation/VAR_017663|||http://purl.uniprot.org/annotation/VAR_017664|||http://purl.uniprot.org/annotation/VAR_018727|||http://purl.uniprot.org/annotation/VAR_034706|||http://purl.uniprot.org/annotation/VAR_034707|||http://purl.uniprot.org/annotation/VAR_034708|||http://purl.uniprot.org/annotation/VAR_034709|||http://purl.uniprot.org/annotation/VAR_034710|||http://purl.uniprot.org/annotation/VAR_039745|||http://purl.uniprot.org/annotation/VAR_039746|||http://purl.uniprot.org/annotation/VAR_039747|||http://purl.uniprot.org/annotation/VAR_039748|||http://purl.uniprot.org/annotation/VAR_039749|||http://purl.uniprot.org/annotation/VAR_039750|||http://purl.uniprot.org/annotation/VAR_039751|||http://purl.uniprot.org/annotation/VAR_039752|||http://purl.uniprot.org/annotation/VAR_039753|||http://purl.uniprot.org/annotation/VAR_039754|||http://purl.uniprot.org/annotation/VAR_039755|||http://purl.uniprot.org/annotation/VAR_039756|||http://purl.uniprot.org/annotation/VAR_039757|||http://purl.uniprot.org/annotation/VAR_039758|||http://purl.uniprot.org/annotation/VAR_039759|||http://purl.uniprot.org/annotation/VAR_039760|||http://purl.uniprot.org/annotation/VAR_039761|||http://purl.uniprot.org/annotation/VAR_039762|||http://purl.uniprot.org/annotation/VAR_039763|||http://purl.uniprot.org/annotation/VAR_039764|||http://purl.uniprot.org/annotation/VAR_039765|||http://purl.uniprot.org/annotation/VAR_039766|||http://purl.uniprot.org/annotation/VAR_039767|||http://purl.uniprot.org/annotation/VAR_039768|||http://purl.uniprot.org/annotation/VAR_039769|||http://purl.uniprot.org/annotation/VAR_039770|||http://purl.uniprot.org/annotation/VAR_039771|||http://purl.uniprot.org/annotation/VAR_039772|||http://purl.uniprot.org/annotation/VAR_039773|||http://purl.uniprot.org/annotation/VAR_039774|||http://purl.uniprot.org/annotation/VAR_039775|||http://purl.uniprot.org/annotation/VAR_039776|||http://purl.uniprot.org/annotation/VAR_039777|||http://purl.uniprot.org/annotation/VAR_039778|||http://purl.uniprot.org/annotation/VAR_039779|||http://purl.uniprot.org/annotation/VAR_039780|||http://purl.uniprot.org/annotation/VAR_039781|||http://purl.uniprot.org/annotation/VAR_039782|||http://purl.uniprot.org/annotation/VAR_039783|||http://purl.uniprot.org/annotation/VAR_039784|||http://purl.uniprot.org/annotation/VAR_039785|||http://purl.uniprot.org/annotation/VAR_039786|||http://purl.uniprot.org/annotation/VAR_039787|||http://purl.uniprot.org/annotation/VAR_039788|||http://purl.uniprot.org/annotation/VAR_039789|||http://purl.uniprot.org/annotation/VAR_039790|||http://purl.uniprot.org/annotation/VAR_039791|||http://purl.uniprot.org/annotation/VAR_039792|||http://purl.uniprot.org/annotation/VAR_063588|||http://purl.uniprot.org/annotation/VAR_063589|||http://purl.uniprot.org/annotation/VAR_063590|||http://purl.uniprot.org/annotation/VAR_063591|||http://purl.uniprot.org/annotation/VAR_063592|||http://purl.uniprot.org/annotation/VAR_063593|||http://purl.uniprot.org/annotation/VAR_063594|||http://purl.uniprot.org/annotation/VAR_064055|||http://purl.uniprot.org/annotation/VAR_064962|||http://purl.uniprot.org/annotation/VAR_064963|||http://purl.uniprot.org/annotation/VAR_064964|||http://purl.uniprot.org/annotation/VAR_064965|||http://purl.uniprot.org/annotation/VAR_064966|||http://purl.uniprot.org/annotation/VAR_064967|||http://purl.uniprot.org/annotation/VAR_064968|||http://purl.uniprot.org/annotation/VAR_064969|||http://purl.uniprot.org/annotation/VAR_064970|||http://purl.uniprot.org/annotation/VAR_064971|||http://purl.uniprot.org/annotation/VAR_064972|||http://purl.uniprot.org/annotation/VAR_064973|||http://purl.uniprot.org/annotation/VAR_064974|||http://purl.uniprot.org/annotation/VAR_064975|||http://purl.uniprot.org/annotation/VAR_064976|||http://purl.uniprot.org/annotation/VAR_067257|||http://purl.uniprot.org/annotation/VAR_067258|||http://purl.uniprot.org/annotation/VAR_067697|||http://purl.uniprot.org/annotation/VAR_070174|||http://purl.uniprot.org/annotation/VAR_070175|||http://purl.uniprot.org/annotation/VAR_070176|||http://purl.uniprot.org/annotation/VAR_070177|||http://purl.uniprot.org/annotation/VAR_070178|||http://purl.uniprot.org/annotation/VAR_070179|||http://purl.uniprot.org/annotation/VAR_070180|||http://purl.uniprot.org/annotation/VAR_070181|||http://purl.uniprot.org/annotation/VAR_070182|||http://purl.uniprot.org/annotation/VAR_071968|||http://purl.uniprot.org/annotation/VAR_072817|||http://purl.uniprot.org/annotation/VAR_072818|||http://purl.uniprot.org/annotation/VAR_072819|||http://purl.uniprot.org/annotation/VAR_072820|||http://purl.uniprot.org/annotation/VAR_072821|||http://purl.uniprot.org/annotation/VAR_072822|||http://purl.uniprot.org/annotation/VAR_072823|||http://purl.uniprot.org/annotation/VAR_072824|||http://purl.uniprot.org/annotation/VAR_072825|||http://purl.uniprot.org/annotation/VAR_072826|||http://purl.uniprot.org/annotation/VAR_076562|||http://purl.uniprot.org/annotation/VAR_076563|||http://purl.uniprot.org/annotation/VSP_002468|||http://purl.uniprot.org/annotation/VSP_002469|||http://purl.uniprot.org/annotation/VSP_002470|||http://purl.uniprot.org/annotation/VSP_045977|||http://purl.uniprot.org/annotation/VSP_045978|||http://purl.uniprot.org/annotation/VSP_045979|||http://purl.uniprot.org/annotation/VSP_053503|||http://purl.uniprot.org/annotation/VSP_053504|||http://purl.uniprot.org/annotation/VSP_053505
http://togogenome.org/gene/9606:RIIAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  RIIa|||RIIa domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342467
http://togogenome.org/gene/9606:MRRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E11                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||Mitochondrion|||Ribosome-recycling factor, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031080|||http://purl.uniprot.org/annotation/VAR_051885|||http://purl.uniprot.org/annotation/VSP_013483|||http://purl.uniprot.org/annotation/VSP_013484|||http://purl.uniprot.org/annotation/VSP_013485|||http://purl.uniprot.org/annotation/VSP_013486|||http://purl.uniprot.org/annotation/VSP_013487|||http://purl.uniprot.org/annotation/VSP_013488|||http://purl.uniprot.org/annotation/VSP_013489|||http://purl.uniprot.org/annotation/VSP_013490|||http://purl.uniprot.org/annotation/VSP_042019
http://togogenome.org/gene/9606:CEACAM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14002                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 7|||GPI-anchor amidated serine|||Ig-like C2-type|||Ig-like V-type|||In isoform 2b.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014570|||http://purl.uniprot.org/annotation/PRO_0000014571|||http://purl.uniprot.org/annotation/VAR_024494|||http://purl.uniprot.org/annotation/VAR_049848|||http://purl.uniprot.org/annotation/VAR_059384|||http://purl.uniprot.org/annotation/VSP_002488
http://togogenome.org/gene/9606:HEPACAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVW5|||http://purl.uniprot.org/uniprot/C9JN07                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Found in a renal cell carcinoma sample; somatic mutation.|||HEPACAM family member 2|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332220|||http://purl.uniprot.org/annotation/PRO_5002996483|||http://purl.uniprot.org/annotation/VAR_042976|||http://purl.uniprot.org/annotation/VAR_042977|||http://purl.uniprot.org/annotation/VAR_064721|||http://purl.uniprot.org/annotation/VSP_033355|||http://purl.uniprot.org/annotation/VSP_044322
http://togogenome.org/gene/9606:LRFN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type-III domain-containing protein 4|||Loss of DLG1-, DLG3- and DLG4-binding.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014843|||http://purl.uniprot.org/annotation/VAR_024499
http://togogenome.org/gene/9606:SSRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08945                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by caspase.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Cleavage; by caspase-3 and/or caspase-7|||Disordered|||FACT complex subunit SSRP1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657.|||Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688.|||Unable to bind DNA; when associated with A-657 and A-688.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048606|||http://purl.uniprot.org/annotation/VAR_052495|||http://purl.uniprot.org/annotation/VAR_052496
http://togogenome.org/gene/9606:PTGER4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJF5|||http://purl.uniprot.org/uniprot/P35408                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prostaglandin E2 receptor EP4 subtype                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070064
http://togogenome.org/gene/9606:DGKZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13574                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Basic residues|||DAGKc|||Diacylglycerol kinase zeta|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6, isoform 7, isoform 5 and isoform 4.|||In isoform 6.|||In isoform 7.|||Loss of interaction with SNTG1.|||MARCKS homology|||Mediates interaction with RASGRP1|||Nuclear export signal|||PDZ-binding|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218468|||http://purl.uniprot.org/annotation/VAR_069059|||http://purl.uniprot.org/annotation/VAR_083552|||http://purl.uniprot.org/annotation/VSP_060597|||http://purl.uniprot.org/annotation/VSP_060598|||http://purl.uniprot.org/annotation/VSP_060599|||http://purl.uniprot.org/annotation/VSP_060600|||http://purl.uniprot.org/annotation/VSP_060601|||http://purl.uniprot.org/annotation/VSP_060602|||http://purl.uniprot.org/annotation/VSP_060603
http://togogenome.org/gene/9606:WWP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0M0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitin transfer; when associated with A-848.|||Abolishes ubiquitin transfer; when associated with A-855.|||C2|||Disordered|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||In isoform 3.|||In isoform 6.|||NEDD4-like E3 ubiquitin-protein ligase WWP1|||No effect.|||Polar residues|||Reduces ubiquitin transfer.|||Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845.|||Required for ubiquitin-thioester formation|||Strongly reduces ubiquitin transfer.|||Strongly reduces ubiquitin transfer; when associated with P-804.|||Strongly reduces ubiquitin transfer; when associated with P-806.|||WW 1|||WW 2|||WW 3|||WW 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120336|||http://purl.uniprot.org/annotation/VSP_007600|||http://purl.uniprot.org/annotation/VSP_007601|||http://purl.uniprot.org/annotation/VSP_007602|||http://purl.uniprot.org/annotation/VSP_007603
http://togogenome.org/gene/9606:GGTLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX51                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain                                                                                  ^@                                                                                  Glutathione hydrolase light chain 1|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205983
http://togogenome.org/gene/9606:FOXD4L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VV16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4-like 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301978
http://togogenome.org/gene/9606:ANGEL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z297|||http://purl.uniprot.org/uniprot/B7Z5N3|||http://purl.uniprot.org/uniprot/Q5VTE6|||http://purl.uniprot.org/uniprot/Q96AL9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Endonuclease/exonuclease/phosphatase|||In isoform 2.|||Protein angel homolog 2|||Protein angel homolog 2 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305080|||http://purl.uniprot.org/annotation/VAR_050290|||http://purl.uniprot.org/annotation/VSP_028216
http://togogenome.org/gene/9606:IFT57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWB7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Impairs the interaction with HIP1.|||Intraflagellar transport protein 57 homolog|||pDED                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328884
http://togogenome.org/gene/9606:OR10S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGN2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150716|||http://purl.uniprot.org/annotation/VAR_054358|||http://purl.uniprot.org/annotation/VAR_054359|||http://purl.uniprot.org/annotation/VAR_054360
http://togogenome.org/gene/9606:KLRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26715                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Decreases interaction with INPP5D/SHIP-1; when associated A-38.|||Decreases interaction with INPP5D/SHIP-1; when associated A-6.|||Disordered|||Extracellular|||Has little impact on affinity for HLA-E.|||Has no impact on affinity for HLA-E.|||Has no impact on the affinity for HLA-E.|||Helical; Signal-anchor for type II membrane protein|||Immunoreceptor tyrosine-based inhibition motif (ITIM)|||Impairs binding to HLA-E.|||Impairs phosphorylation, interaction with INPP5D/SHIP-1 and NK cell functional inhibition; when associated F-40.|||Impairs phosphorylation, interaction with INPP5D/SHIP-1 and NK cell functional inhibition; when associated F-8.|||In isoform NKG2-B.|||Interchain (with C-59 in KLRD1)|||N-linked (GlcNAc...) asparagine|||NKG2-A/NKG2-B type II integral membrane protein|||Phosphotyrosine|||Polar residues|||Reduces binding to HLA-E.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046659|||http://purl.uniprot.org/annotation/VAR_050120|||http://purl.uniprot.org/annotation/VSP_003062
http://togogenome.org/gene/9606:ESYT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0FGR9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||C2 3|||Cytoplasmic|||Disordered|||Extended synaptotagmin-3|||Helical|||In isoform 2.|||Polar residues|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314899|||http://purl.uniprot.org/annotation/VAR_038117|||http://purl.uniprot.org/annotation/VAR_038118|||http://purl.uniprot.org/annotation/VAR_053835|||http://purl.uniprot.org/annotation/VAR_062173|||http://purl.uniprot.org/annotation/VSP_030424|||http://purl.uniprot.org/annotation/VSP_030425
http://togogenome.org/gene/9606:ZNF891                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MT65                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||KRAB|||Zinc finger protein 891                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349185
http://togogenome.org/gene/9606:USP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75317                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Impaired binding to WDR20; when associated with Ala-287.|||Impaired binding to WDR20; when associated with Asp-279.|||Impaired binding to WDR48.|||Impaired binding to WDR48; when associated with Ala-240.|||Impaired binding to WDR48; when associated with Ala-241.|||Loss of activity.|||Nucleophile|||Polar residues|||Proton acceptor|||Strong reduction of activity.|||USP|||Ubiquitin carboxyl-terminal hydrolase 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080634
http://togogenome.org/gene/9606:RPL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02878|||http://purl.uniprot.org/uniprot/Q8TBK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||Large ribosomal subunit protein eL6|||Large ribosomal subunit protein uL6 N-terminal|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171009|||http://purl.uniprot.org/annotation/VAR_025313|||http://purl.uniprot.org/annotation/VAR_036437|||http://purl.uniprot.org/annotation/VAR_051810
http://togogenome.org/gene/9606:OR51D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVM2|||http://purl.uniprot.org/uniprot/Q8NGF3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 51D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150749|||http://purl.uniprot.org/annotation/VAR_053323
http://togogenome.org/gene/9606:OSBPL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ6|||http://purl.uniprot.org/uniprot/Q9BXB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Oxysterol-binding protein-related protein 11|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100381|||http://purl.uniprot.org/annotation/VAR_036100
http://togogenome.org/gene/9606:PFDN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15212|||http://purl.uniprot.org/uniprot/Q5STK2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Prefoldin subunit 6|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124850
http://togogenome.org/gene/9606:MAP3K14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D39|||http://purl.uniprot.org/uniprot/Q99558                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes 'Lys-63'-linked ubiquitination.|||Basic residues|||Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||Interaction with ZFP91|||Loss of autophosphorylation and 'Lys-63'-linked ubiquitination.|||Mitogen-activated protein kinase kinase kinase 14|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086266|||http://purl.uniprot.org/annotation/VAR_040711|||http://purl.uniprot.org/annotation/VAR_040712|||http://purl.uniprot.org/annotation/VAR_040713|||http://purl.uniprot.org/annotation/VAR_040714|||http://purl.uniprot.org/annotation/VAR_040715|||http://purl.uniprot.org/annotation/VAR_051641|||http://purl.uniprot.org/annotation/VAR_051642
http://togogenome.org/gene/9606:CYP7A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22680                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome P450 7A1|||Helical|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051901|||http://purl.uniprot.org/annotation/VAR_001259|||http://purl.uniprot.org/annotation/VAR_018376|||http://purl.uniprot.org/annotation/VAR_018377|||http://purl.uniprot.org/annotation/VAR_059152
http://togogenome.org/gene/9606:ASTE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RG30|||http://purl.uniprot.org/uniprot/Q2TB18                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asteroid|||Disordered|||In isoform 2.|||Protein asteroid homolog 1|||XPG N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310458|||http://purl.uniprot.org/annotation/VSP_056699|||http://purl.uniprot.org/annotation/VSP_056700
http://togogenome.org/gene/9606:MAPKBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60336                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In NPHP20; unknown pathological significance; no effect on localization at the spindle pole; no effect on interaction with WDR62; no effect on interaction with MAPK9.|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitogen-activated protein kinase-binding protein 1|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||WD 1|||WD 10|||WD 11|||WD 12|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334158|||http://purl.uniprot.org/annotation/VAR_043343|||http://purl.uniprot.org/annotation/VAR_043344|||http://purl.uniprot.org/annotation/VAR_043345|||http://purl.uniprot.org/annotation/VAR_077958|||http://purl.uniprot.org/annotation/VSP_033629|||http://purl.uniprot.org/annotation/VSP_033630|||http://purl.uniprot.org/annotation/VSP_033631|||http://purl.uniprot.org/annotation/VSP_033632|||http://purl.uniprot.org/annotation/VSP_033633|||http://purl.uniprot.org/annotation/VSP_033634|||http://purl.uniprot.org/annotation/VSP_033635
http://togogenome.org/gene/9606:RILPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969X0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Loss of interaction with RAB8A, RAB10 and RAB12.|||Phosphoserine|||RH1|||RH2|||RILP-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317005
http://togogenome.org/gene/9606:GOLGA6L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEF3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Golgin subfamily A member 6-like protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332264
http://togogenome.org/gene/9606:BRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HL36|||http://purl.uniprot.org/uniprot/Q9BX63                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1.|||Basic and acidic residues|||DEAH box|||Disordered|||Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities.|||Disrupts the interaction with BRCA1.|||Does not affect the interaction with BRCA1.|||Fanconi anemia group J protein|||Helicase ATP-binding|||In BC; early onset; loss of ATPase and helicase activities.|||In BC; early onset; reduces helicase efficiency on longer substrates.|||In FANCJ.|||In FANCJ; associated with C-647.|||In FANCJ; associated with C-707.|||In FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity.|||In a patient with ovarian cancer; unknown pathological significance.|||In isoform 2.|||Interaction with BRCA1|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055173|||http://purl.uniprot.org/annotation/VAR_020896|||http://purl.uniprot.org/annotation/VAR_020897|||http://purl.uniprot.org/annotation/VAR_020898|||http://purl.uniprot.org/annotation/VAR_020899|||http://purl.uniprot.org/annotation/VAR_020900|||http://purl.uniprot.org/annotation/VAR_020901|||http://purl.uniprot.org/annotation/VAR_020902|||http://purl.uniprot.org/annotation/VAR_020903|||http://purl.uniprot.org/annotation/VAR_020904|||http://purl.uniprot.org/annotation/VAR_020905|||http://purl.uniprot.org/annotation/VAR_020906|||http://purl.uniprot.org/annotation/VAR_020907|||http://purl.uniprot.org/annotation/VAR_023700|||http://purl.uniprot.org/annotation/VAR_023701|||http://purl.uniprot.org/annotation/VAR_023702|||http://purl.uniprot.org/annotation/VAR_023703|||http://purl.uniprot.org/annotation/VAR_023704|||http://purl.uniprot.org/annotation/VAR_052192|||http://purl.uniprot.org/annotation/VAR_052193|||http://purl.uniprot.org/annotation/VSP_012540|||http://purl.uniprot.org/annotation/VSP_012541
http://togogenome.org/gene/9606:TRIM49D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J1S8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 49D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395402
http://togogenome.org/gene/9606:SASS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYM7|||http://purl.uniprot.org/uniprot/Q495U0|||http://purl.uniprot.org/uniprot/Q6UVJ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fails to multimerize via N-terminus.|||In MCPH14; impairs the centriole-forming function of the protein.|||PISA|||Phosphoserine|||SAS-6 coiled-coil|||Spindle assembly abnormal protein 6 N-terminal|||Spindle assembly abnormal protein 6 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189972|||http://purl.uniprot.org/annotation/VAR_021590|||http://purl.uniprot.org/annotation/VAR_073833
http://togogenome.org/gene/9606:CALM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ51|||http://purl.uniprot.org/uniprot/P0DP23|||http://purl.uniprot.org/uniprot/P0DP24|||http://purl.uniprot.org/uniprot/P0DP25|||http://purl.uniprot.org/uniprot/Q96HY3                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT6; decreased calcium-binding affinity; not changed binding to RYR2; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed action potential duration.|||In LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release.|||In LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2.|||In LQT15.|||In LQT15; reduction in calcium affinity.|||In LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT16.|||In LQT16; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Necessary and sufficient for interaction with PCP4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CaMK4|||Phosphotyrosine|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000439932|||http://purl.uniprot.org/annotation/PRO_0000439933|||http://purl.uniprot.org/annotation/PRO_0000439934|||http://purl.uniprot.org/annotation/VAR_069222|||http://purl.uniprot.org/annotation/VAR_073275|||http://purl.uniprot.org/annotation/VAR_073276|||http://purl.uniprot.org/annotation/VAR_073277|||http://purl.uniprot.org/annotation/VAR_073279|||http://purl.uniprot.org/annotation/VAR_073280|||http://purl.uniprot.org/annotation/VAR_073281|||http://purl.uniprot.org/annotation/VAR_073282|||http://purl.uniprot.org/annotation/VAR_078261|||http://purl.uniprot.org/annotation/VAR_078262|||http://purl.uniprot.org/annotation/VAR_078263|||http://purl.uniprot.org/annotation/VAR_078541|||http://purl.uniprot.org/annotation/VAR_078542|||http://purl.uniprot.org/annotation/VAR_078543|||http://purl.uniprot.org/annotation/VAR_078544|||http://purl.uniprot.org/annotation/VAR_083814|||http://purl.uniprot.org/annotation/VAR_083815|||http://purl.uniprot.org/annotation/VAR_083816
http://togogenome.org/gene/9606:SPMAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2T0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Sperm microtubule associated protein 2|||THEG 1|||THEG 2|||THEG 3|||THEG 4|||THEG 5|||THEG 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306267|||http://purl.uniprot.org/annotation/VAR_035286|||http://purl.uniprot.org/annotation/VAR_035287|||http://purl.uniprot.org/annotation/VAR_035288|||http://purl.uniprot.org/annotation/VAR_035289|||http://purl.uniprot.org/annotation/VSP_028446
http://togogenome.org/gene/9606:CEP192                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEP8|||http://purl.uniprot.org/uniprot/Q9HCK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 192 kDa|||Disordered|||Hydroxyproline|||In isoform 1 and isoform 2.|||In isoform 2.|||Increased presence on interphasic centrosomes, and decreased presence on mitotic centrosomes; no ubiquitination and unchanged levels in response to hypoxia.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312495|||http://purl.uniprot.org/annotation/VAR_037514|||http://purl.uniprot.org/annotation/VAR_037515|||http://purl.uniprot.org/annotation/VAR_050782|||http://purl.uniprot.org/annotation/VAR_050783|||http://purl.uniprot.org/annotation/VAR_050784|||http://purl.uniprot.org/annotation/VAR_050785|||http://purl.uniprot.org/annotation/VAR_050786|||http://purl.uniprot.org/annotation/VAR_050787|||http://purl.uniprot.org/annotation/VAR_050788|||http://purl.uniprot.org/annotation/VAR_050789|||http://purl.uniprot.org/annotation/VSP_059657|||http://purl.uniprot.org/annotation/VSP_059658|||http://purl.uniprot.org/annotation/VSP_059659
http://togogenome.org/gene/9606:MZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28698                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform MZF1B-C.|||Myeloid zinc finger 1|||Phosphoserine|||Pro residues|||SCAN box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047375|||http://purl.uniprot.org/annotation/VAR_014826|||http://purl.uniprot.org/annotation/VAR_047677|||http://purl.uniprot.org/annotation/VAR_047678|||http://purl.uniprot.org/annotation/VAR_047679|||http://purl.uniprot.org/annotation/VAR_047680|||http://purl.uniprot.org/annotation/VSP_006889|||http://purl.uniprot.org/annotation/VSP_006890|||http://purl.uniprot.org/annotation/VSP_047013|||http://purl.uniprot.org/annotation/VSP_047014
http://togogenome.org/gene/9606:SLC6A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WY96|||http://purl.uniprot.org/uniprot/B4E140|||http://purl.uniprot.org/uniprot/P31641|||http://purl.uniprot.org/uniprot/Q59GD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In HTRDC; decreased taurine transport activity; does not affect protein abundance; does not affect cell membrane localization.|||In HTRDC; severely decreased taurine transport activity in patient cells; does not affect cell membrane localization.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium- and chloride-dependent taurine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214767|||http://purl.uniprot.org/annotation/VAR_011767|||http://purl.uniprot.org/annotation/VAR_011768|||http://purl.uniprot.org/annotation/VAR_083336|||http://purl.uniprot.org/annotation/VAR_083337|||http://purl.uniprot.org/annotation/VSP_044961
http://togogenome.org/gene/9606:HSPA12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43301                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Heat shock 70 kDa protein 12A|||N-acetylalanine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078292
http://togogenome.org/gene/9606:SCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00767                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal|||Phosphoserine|||Stearoyl-CoA desaturase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185395|||http://purl.uniprot.org/annotation/VAR_025994
http://togogenome.org/gene/9606:ZBTB47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFB7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Pro residues|||Zinc finger and BTB domain-containing protein 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251896|||http://purl.uniprot.org/annotation/VAR_027715|||http://purl.uniprot.org/annotation/VSP_054051
http://togogenome.org/gene/9606:GPR135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ08                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 135|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069612|||http://purl.uniprot.org/annotation/VAR_024259|||http://purl.uniprot.org/annotation/VAR_049402
http://togogenome.org/gene/9606:ABCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61221                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family E member 1|||Abolishes ubiquitination by CNOT4 and diminished the ability to recruit autophagy receptors to damaged mitochondria and to nuclear encoded respiratory chain component mRNA-ribonucleoproteins complexes.|||Confirmed at protein level.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093316|||http://purl.uniprot.org/annotation/VAR_068914
http://togogenome.org/gene/9606:HADH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK76|||http://purl.uniprot.org/uniprot/B3KTT6|||http://purl.uniprot.org/uniprot/Q16836                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-hydroxyacyl-CoA dehydrogenase C-terminal|||3-hydroxyacyl-CoA dehydrogenase NAD binding|||Found in a patient with Reye-like syndrome. Does not affect 3-hydroxyacyl-CoA dehydrogenase activity. Increases KM value for NADH. Does not affect dimerization.|||Found in a patient with Reye-like syndrome; loss of 3-hydroxyacyl-CoA dehydrogenase activity. Does not affect dimerization.|||Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial|||Important for catalytic activity|||In HADH deficiency.|||In HHF4; loss of 3-hydroxyacyl-CoA dehydrogenase activity.|||In isoform 2 and isoform 3.|||In isoform 2.|||Mitochondrion|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007406|||http://purl.uniprot.org/annotation/VAR_024079|||http://purl.uniprot.org/annotation/VAR_024080|||http://purl.uniprot.org/annotation/VAR_024081|||http://purl.uniprot.org/annotation/VAR_026764|||http://purl.uniprot.org/annotation/VAR_055701|||http://purl.uniprot.org/annotation/VAR_083648|||http://purl.uniprot.org/annotation/VAR_083649|||http://purl.uniprot.org/annotation/VSP_016551|||http://purl.uniprot.org/annotation/VSP_016552
http://togogenome.org/gene/9606:CMC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56277                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Turn                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cx9C motif-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096614
http://togogenome.org/gene/9606:GALNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L7NY50|||http://purl.uniprot.org/uniprot/B7Z6K2|||http://purl.uniprot.org/uniprot/Q10471                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In CDG2T; loss of ApoC-III glycosylation.|||In CDG2T; loss-of-funtion variant resulting in lack of ApoC-III and IgA1 glycosylation.|||In CDG2T; loss-of-funtion variant resulting in lack of ApoC-III glycosylation; b.|||In isoform 2.|||Likely benign variant; does not affect ApoC-III glycosylation.|||Loss of enzyme activity.|||Lumenal|||Not glycosylated|||Phosphoserine|||Polypeptide N-acetylgalactosaminyltransferase|||Polypeptide N-acetylgalactosaminyltransferase 2|||Polypeptide N-acetylgalactosaminyltransferase 2 soluble form|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012265|||http://purl.uniprot.org/annotation/PRO_0000223391|||http://purl.uniprot.org/annotation/PRO_5009874075|||http://purl.uniprot.org/annotation/VAR_019575|||http://purl.uniprot.org/annotation/VAR_049240|||http://purl.uniprot.org/annotation/VAR_084283|||http://purl.uniprot.org/annotation/VAR_084284|||http://purl.uniprot.org/annotation/VAR_084285|||http://purl.uniprot.org/annotation/VAR_084286|||http://purl.uniprot.org/annotation/VAR_084287|||http://purl.uniprot.org/annotation/VAR_084288|||http://purl.uniprot.org/annotation/VSP_056491|||http://purl.uniprot.org/annotation/VSP_056492|||http://purl.uniprot.org/annotation/VSP_056493
http://togogenome.org/gene/9606:MB21D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in patients with squamous cell carcinomas; oncogenic.|||Nucleotidyltransferase MB21D2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239303|||http://purl.uniprot.org/annotation/VAR_085526
http://togogenome.org/gene/9606:RFPL4AL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VTS6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||RING-type; degenerate|||Ret finger protein-like 4A-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422543
http://togogenome.org/gene/9606:NUPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60356                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Impairs interaction with RNF2.|||In isoform 2.|||Nuclear localization signal|||Nuclear protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058007|||http://purl.uniprot.org/annotation/VSP_053816
http://togogenome.org/gene/9606:FAM91A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUD8|||http://purl.uniprot.org/uniprot/E7ER68|||http://purl.uniprot.org/uniprot/Q658Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||FAM91 C-terminal|||FAM91 N-terminal|||Phosphoserine|||Polar residues|||Protein FAM91A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282552|||http://purl.uniprot.org/annotation/VAR_057768|||http://purl.uniprot.org/annotation/VAR_067449
http://togogenome.org/gene/9606:POLR3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15318                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA-directed RNA polymerase III subunit RPC7|||Disordered|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073978
http://togogenome.org/gene/9606:TP53TG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2B4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||TP53-target gene 5 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072405|||http://purl.uniprot.org/annotation/VAR_051397|||http://purl.uniprot.org/annotation/VAR_051398|||http://purl.uniprot.org/annotation/VAR_051399|||http://purl.uniprot.org/annotation/VAR_051400|||http://purl.uniprot.org/annotation/VAR_051401|||http://purl.uniprot.org/annotation/VAR_051402|||http://purl.uniprot.org/annotation/VAR_051403
http://togogenome.org/gene/9606:ZNF727                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUV8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Putative zinc finger protein 727                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346157
http://togogenome.org/gene/9606:ZSCAN30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGV0|||http://purl.uniprot.org/uniprot/Q86W11                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||SCAN box|||Zinc finger and SCAN domain-containing protein 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300694|||http://purl.uniprot.org/annotation/VAR_059914|||http://purl.uniprot.org/annotation/VSP_027861|||http://purl.uniprot.org/annotation/VSP_027862
http://togogenome.org/gene/9606:SLC18B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT16                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||MFS-type transporter SLC18B1|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294450|||http://purl.uniprot.org/annotation/VAR_033185|||http://purl.uniprot.org/annotation/VAR_061382|||http://purl.uniprot.org/annotation/VAR_063260
http://togogenome.org/gene/9606:CCL3L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16619                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  C-C motif chemokine 3-like 1|||Cleavage; by DPP4|||LD78-beta(3-70)|||LD78-beta(5-70)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005161|||http://purl.uniprot.org/annotation/PRO_0000005162|||http://purl.uniprot.org/annotation/PRO_0000005163
http://togogenome.org/gene/9606:APCDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8J025                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HYPT1; dominant-negative mutant that perturbs the translational processing from the endoplasmic reticulum to the plasma membrane.|||N-linked (GlcNAc...) asparagine|||Protein APCDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227520|||http://purl.uniprot.org/annotation/VAR_050667|||http://purl.uniprot.org/annotation/VAR_063497
http://togogenome.org/gene/9606:PDE8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60658                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increases sensitivity to several nonselective or family selective PDE inhibitors.|||Involved in RAF1-binding|||PAC|||PAS|||PDEase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Proton donor|||Reduces interaction with RAF1; when associated with A-454 and A-455.|||Reduces interaction with RAF1; when associated with A-460 and A-461.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198838|||http://purl.uniprot.org/annotation/VAR_069109|||http://purl.uniprot.org/annotation/VSP_004597|||http://purl.uniprot.org/annotation/VSP_041674|||http://purl.uniprot.org/annotation/VSP_041675|||http://purl.uniprot.org/annotation/VSP_041676|||http://purl.uniprot.org/annotation/VSP_041677|||http://purl.uniprot.org/annotation/VSP_041678|||http://purl.uniprot.org/annotation/VSP_041679|||http://purl.uniprot.org/annotation/VSP_046017
http://togogenome.org/gene/9606:LZTS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP66|||http://purl.uniprot.org/uniprot/Q9BRK4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Induces nuclear accumulation. Impairs nuclear exclusion of beta-catenin; when associated with A-38.|||Induces nuclear accumulation. Impairs nuclear exclusion of beta-catenin; when associated with A-640.|||Leucine zipper putative tumor suppressor 2|||Nuclear export signal|||Phosphoserine|||Polar residues|||Pro residues|||Required for centrosomal localization|||Sufficient for interaction with CTNNB1|||Sufficient for interaction with KATNB1 and for inhibition of katanin-mediated microtubule severing                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182974|||http://purl.uniprot.org/annotation/VAR_018277|||http://purl.uniprot.org/annotation/VAR_036364|||http://purl.uniprot.org/annotation/VAR_036365
http://togogenome.org/gene/9606:MICALL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWK3|||http://purl.uniprot.org/uniprot/Q8IY33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Forms an intramolecular interaction with the C-terminal coiled coil domain keeping the protein in a closed conformation|||Forms an intramolecular interaction with the N-terminal Calponin-homology and LIM zinc-binding domains-containing region keeping the protein in a closed conformation|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM zinc-binding|||MICAL-like protein 2|||Mediates interaction with RAB13 and is required for transition from the closed to the opened conformation|||Mediates targeting to the cell plasma membrane|||Necessary and sufficient for interaction with actinins|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075850|||http://purl.uniprot.org/annotation/PRO_5004281478|||http://purl.uniprot.org/annotation/VAR_034071|||http://purl.uniprot.org/annotation/VAR_034072|||http://purl.uniprot.org/annotation/VAR_050159|||http://purl.uniprot.org/annotation/VAR_061356|||http://purl.uniprot.org/annotation/VSP_009854|||http://purl.uniprot.org/annotation/VSP_009855|||http://purl.uniprot.org/annotation/VSP_009856|||http://purl.uniprot.org/annotation/VSP_009857|||http://purl.uniprot.org/annotation/VSP_009858
http://togogenome.org/gene/9606:LPCAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NF37                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Di-lysine motif|||Disordered|||EF-hand 1|||EF-hand 2|||HXXXXD motif|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Lysophosphatidylcholine acyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247064
http://togogenome.org/gene/9606:BYSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13895                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bystin|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186114|||http://purl.uniprot.org/annotation/VAR_033641|||http://purl.uniprot.org/annotation/VAR_048439
http://togogenome.org/gene/9606:ALYREF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PB61|||http://purl.uniprot.org/uniprot/Q86V81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Citrulline|||Dimethylated arginine; alternate|||Disordered|||Interaction with HHV-8 ORF57 protein and with ICP27 from HHV-1|||N-acetylalanine|||N6-acetyllysine|||N6-methyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||RRM|||Removed|||Sufficient for RNA-binding, interaction with NXF1-NXT1 heterodimer|||THO complex subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081974
http://togogenome.org/gene/9606:USP17L26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:HORMAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7B1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  HORMA|||HORMA domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284669|||http://purl.uniprot.org/annotation/VAR_031802|||http://purl.uniprot.org/annotation/VAR_031803
http://togogenome.org/gene/9606:USP39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1B2|||http://purl.uniprot.org/uniprot/B3KMG1|||http://purl.uniprot.org/uniprot/B3KPG7|||http://purl.uniprot.org/uniprot/B7Z7L9|||http://purl.uniprot.org/uniprot/Q53GS9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of CHK2 and NFKBIA deubiquitination.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||UBP-type|||UBP-type; degenerate|||USP|||Ubiquitin carboxyl-terminal hydrolase 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223962|||http://purl.uniprot.org/annotation/VSP_045167|||http://purl.uniprot.org/annotation/VSP_045168|||http://purl.uniprot.org/annotation/VSP_046822
http://togogenome.org/gene/9606:FUT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4F1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-(1,3)-fucosyltransferase 10|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 7.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299002|||http://purl.uniprot.org/annotation/VAR_034759|||http://purl.uniprot.org/annotation/VAR_034760|||http://purl.uniprot.org/annotation/VAR_034761|||http://purl.uniprot.org/annotation/VAR_034762|||http://purl.uniprot.org/annotation/VSP_027498|||http://purl.uniprot.org/annotation/VSP_027499|||http://purl.uniprot.org/annotation/VSP_027500|||http://purl.uniprot.org/annotation/VSP_027501|||http://purl.uniprot.org/annotation/VSP_027502|||http://purl.uniprot.org/annotation/VSP_027503|||http://purl.uniprot.org/annotation/VSP_027504|||http://purl.uniprot.org/annotation/VSP_027505|||http://purl.uniprot.org/annotation/VSP_027506
http://togogenome.org/gene/9606:FAM178B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV66|||http://purl.uniprot.org/uniprot/Q8IXR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil SMC6 And NSE5 INteracting (CANIN)|||Disordered|||In isoform 2.|||In isoform 4.|||Pro residues|||Protein FAM178B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320193|||http://purl.uniprot.org/annotation/VAR_039172|||http://purl.uniprot.org/annotation/VSP_060401|||http://purl.uniprot.org/annotation/VSP_060402|||http://purl.uniprot.org/annotation/VSP_060403
http://togogenome.org/gene/9606:SLC1A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7Q5|||http://purl.uniprot.org/uniprot/P48664                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Discontinuously helical|||Disordered|||Excitatory amino acid transporter 4|||Helical|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202070|||http://purl.uniprot.org/annotation/VSP_055130
http://togogenome.org/gene/9606:PIR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00625                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Pirin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214051|||http://purl.uniprot.org/annotation/VAR_050543
http://togogenome.org/gene/9606:RPL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26373                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In SEMDIST.|||In isoform 2.|||Large ribosomal subunit protein eL13|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192919|||http://purl.uniprot.org/annotation/VAR_051801|||http://purl.uniprot.org/annotation/VAR_051802|||http://purl.uniprot.org/annotation/VAR_083551|||http://purl.uniprot.org/annotation/VSP_046028
http://togogenome.org/gene/9606:KHDC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSQ8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative KHDC1-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395326
http://togogenome.org/gene/9606:SLC38A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Regulates protein turnover upon amino acid deprivation|||Sodium-coupled neutral amino acid symporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311369|||http://purl.uniprot.org/annotation/VAR_037235|||http://purl.uniprot.org/annotation/VSP_029553|||http://purl.uniprot.org/annotation/VSP_029554
http://togogenome.org/gene/9606:APCDD1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDQ9|||http://purl.uniprot.org/uniprot/Q8NCL9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  APCDD1|||Helical|||N-linked (GlcNAc...) asparagine|||Protein APCDD1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264234|||http://purl.uniprot.org/annotation/VAR_029625|||http://purl.uniprot.org/annotation/VAR_029626|||http://purl.uniprot.org/annotation/VAR_029627|||http://purl.uniprot.org/annotation/VAR_050668
http://togogenome.org/gene/9606:EPHX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34913                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AB hydrolase-1|||Bifunctional epoxide hydrolase 2|||Decreased phosphatase activity; no effect on epoxyde hydrolase activity.|||Epoxide hydrolase|||In isoform 2.|||In isoform 3.|||Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity.|||Loss of phosphatase activity.|||Microbody targeting signal|||N6-acetyllysine|||N6-succinyllysine|||No effect on phosphatase activity and epoxyde hydrolase activity.|||No effect on phosphatase activity; decreased epoxyde hydrolase activity.|||Nucleophile|||Phosphatase|||Phosphoserine|||Proton acceptor|||Proton donor|||S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084111|||http://purl.uniprot.org/annotation/VAR_014852|||http://purl.uniprot.org/annotation/VAR_022613|||http://purl.uniprot.org/annotation/VAR_033991|||http://purl.uniprot.org/annotation/VAR_051059|||http://purl.uniprot.org/annotation/VAR_055392|||http://purl.uniprot.org/annotation/VAR_055393|||http://purl.uniprot.org/annotation/VAR_055394|||http://purl.uniprot.org/annotation/VAR_055395|||http://purl.uniprot.org/annotation/VAR_055396|||http://purl.uniprot.org/annotation/VAR_055397|||http://purl.uniprot.org/annotation/VSP_045597|||http://purl.uniprot.org/annotation/VSP_045598
http://togogenome.org/gene/9606:GARIN5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5Q1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi-associated RAB2 interactor protein 5B|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341369|||http://purl.uniprot.org/annotation/VAR_070950
http://togogenome.org/gene/9606:PTGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8N7|||http://purl.uniprot.org/uniprot/V9HW32                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alcohol dehydrogenase-like C-terminal|||In isoform 2.|||Increases affinity for 15-keto-PGE2. Reduces affinity for NADP and Vmax.|||Oxidoreductase N-terminal|||Prostaglandin reductase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218070|||http://purl.uniprot.org/annotation/VSP_013526|||http://purl.uniprot.org/annotation/VSP_013527
http://togogenome.org/gene/9606:NDUFS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75489                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MC1DN8; decrease in enzyme activity; impaired assembly of complex I; increased protein instability and aggregation; compound heterozygous with I-145.|||In MC1DN8; decrease in enzyme activity; increased protein instability and aggregation; compound heterozygous with W-199.|||In MC1DN8; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I.|||In isoform 2.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019998|||http://purl.uniprot.org/annotation/VAR_012036|||http://purl.uniprot.org/annotation/VAR_081411|||http://purl.uniprot.org/annotation/VAR_081412|||http://purl.uniprot.org/annotation/VAR_081413|||http://purl.uniprot.org/annotation/VSP_057065|||http://purl.uniprot.org/annotation/VSP_057066
http://togogenome.org/gene/9606:PINX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  (Microbial infection) Cleavage by enterovirus 71 protease 3C|||Abolishes cleavage by enterovirus 71.|||Abolishes interaction with TERF1.|||Basic and acidic residues|||Disordered|||Does not affect interaction with TERF1.|||G-patch|||In isoform 2.|||PIN2/TERF1-interacting telomerase inhibitor 1|||Phosphoserine|||Polar residues|||TBM|||Telomerase inhibitory domain (TID)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058443|||http://purl.uniprot.org/annotation/VAR_054024|||http://purl.uniprot.org/annotation/VAR_054025|||http://purl.uniprot.org/annotation/VAR_054026|||http://purl.uniprot.org/annotation/VAR_054027|||http://purl.uniprot.org/annotation/VAR_054028|||http://purl.uniprot.org/annotation/VSP_003945|||http://purl.uniprot.org/annotation/VSP_003946
http://togogenome.org/gene/9606:ZNF783                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMS7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 1.|||KRAB|||N-acetylalanine|||Removed|||Zinc finger protein 783                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270995|||http://purl.uniprot.org/annotation/VAR_069466|||http://purl.uniprot.org/annotation/VSP_061289|||http://purl.uniprot.org/annotation/VSP_061290
http://togogenome.org/gene/9606:TBCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HI02|||http://purl.uniprot.org/uniprot/A0A804HIN6|||http://purl.uniprot.org/uniprot/A0A804HJU6|||http://purl.uniprot.org/uniprot/Q9BTW9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||In PEBAT.|||In PEBAT; decreased function in neuron morphogenesis; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin.|||In PEBAT; decreased function in neuron morphogenesis; severely decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin.|||In PEBAT; decreased function in tubulin complex assembly.|||In PEBAT; decreased function in tubulin complex assembly; increased protein degradation.|||In PEBAT; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin.|||In PEBAT; decreased interaction with TBCE; decreased interaction with beta tubulin; does not affect interaction with ARL2.|||In PEBAT; decreased protein abundance; does not affect localization to centrosome.|||In PEBAT; decreased protein abundance; severely decreased interaction with beta tubulin; does not affect localization to centrosome.|||In PEBAT; severely decreased interaction with beta tubulin; does not affect localization to centrosome.|||In PEBAT; severely decreased protein abundance; does not affect localization to centrosome; decreased interaction with ARL2; decreased interaction with TBCE; decreased interaction with beta tubulin.|||In PEBAT; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Tubulin-specific chaperone D|||Tubulin-specific chaperone D C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080049|||http://purl.uniprot.org/annotation/VAR_057264|||http://purl.uniprot.org/annotation/VAR_057265|||http://purl.uniprot.org/annotation/VAR_057266|||http://purl.uniprot.org/annotation/VAR_057267|||http://purl.uniprot.org/annotation/VAR_077968|||http://purl.uniprot.org/annotation/VAR_077969|||http://purl.uniprot.org/annotation/VAR_077970|||http://purl.uniprot.org/annotation/VAR_077971|||http://purl.uniprot.org/annotation/VAR_077972|||http://purl.uniprot.org/annotation/VAR_077973|||http://purl.uniprot.org/annotation/VAR_077974|||http://purl.uniprot.org/annotation/VAR_077975|||http://purl.uniprot.org/annotation/VAR_077976|||http://purl.uniprot.org/annotation/VAR_077977|||http://purl.uniprot.org/annotation/VAR_077978|||http://purl.uniprot.org/annotation/VAR_077979|||http://purl.uniprot.org/annotation/VAR_077980|||http://purl.uniprot.org/annotation/VSP_017210|||http://purl.uniprot.org/annotation/VSP_017211|||http://purl.uniprot.org/annotation/VSP_017212|||http://purl.uniprot.org/annotation/VSP_017213|||http://purl.uniprot.org/annotation/VSP_017214|||http://purl.uniprot.org/annotation/VSP_017215|||http://purl.uniprot.org/annotation/VSP_017216|||http://purl.uniprot.org/annotation/VSP_017217|||http://purl.uniprot.org/annotation/VSP_017218
http://togogenome.org/gene/9606:SDHAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Mitochondrion|||Succinate dehydrogenase assembly factor 4, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244340|||http://purl.uniprot.org/annotation/VAR_026890|||http://purl.uniprot.org/annotation/VAR_053598
http://togogenome.org/gene/9606:SOCS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14512                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Loss of IRS1 ubiquitination and degradation.|||Mediates interaction with SORBS3|||Pro residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181253|||http://purl.uniprot.org/annotation/VSP_021645
http://togogenome.org/gene/9606:CHRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11229|||http://purl.uniprot.org/uniprot/Q53XZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binds to snake venom muscarinic toxin 7|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Muscarinic acetylcholine receptor M1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Subtype-specific residue that binds to snake venom muscarinic toxin 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069015|||http://purl.uniprot.org/annotation/VSP_056651
http://togogenome.org/gene/9606:KLHL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZB44|||http://purl.uniprot.org/uniprot/Q96HC9|||http://purl.uniprot.org/uniprot/Q9P2N7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||Found in a renal cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119115|||http://purl.uniprot.org/annotation/VAR_064725|||http://purl.uniprot.org/annotation/VAR_069423|||http://purl.uniprot.org/annotation/VSP_037530|||http://purl.uniprot.org/annotation/VSP_037531|||http://purl.uniprot.org/annotation/VSP_037532|||http://purl.uniprot.org/annotation/VSP_037533
http://togogenome.org/gene/9606:CACNA2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ERK3|||http://purl.uniprot.org/uniprot/P54289|||http://purl.uniprot.org/uniprot/Q9UIU0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cache|||Cytoplasmic|||Extracellular|||Helical|||In DEE110; does not promote calcium currents in transfected cells indicating loss of function in the positive regulation of voltage-gated calcium channel activity; severely decreased localization at the cell membrane; undergoes limited proteolytic cleavage.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||Interchain (between alpha-2-1 and delta-1 chains)|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWA N-terminal|||VWFA|||Voltage-dependent calcium channel subunit alpha-2-1|||Voltage-dependent calcium channel subunit alpha-2/delta-1|||Voltage-dependent calcium channel subunit delta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005001|||http://purl.uniprot.org/annotation/PRO_0000005002|||http://purl.uniprot.org/annotation/PRO_0000304633|||http://purl.uniprot.org/annotation/PRO_5003219288|||http://purl.uniprot.org/annotation/PRO_5004335235|||http://purl.uniprot.org/annotation/VAR_035047|||http://purl.uniprot.org/annotation/VAR_053960|||http://purl.uniprot.org/annotation/VAR_087875|||http://purl.uniprot.org/annotation/VSP_038348|||http://purl.uniprot.org/annotation/VSP_038349|||http://purl.uniprot.org/annotation/VSP_038350
http://togogenome.org/gene/9606:MAGEB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15479|||http://purl.uniprot.org/uniprot/Q53G50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen B2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156713|||http://purl.uniprot.org/annotation/VAR_027675|||http://purl.uniprot.org/annotation/VAR_027676
http://togogenome.org/gene/9606:KRTAP20-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI61                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 20-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223911|||http://purl.uniprot.org/annotation/VAR_060060|||http://purl.uniprot.org/annotation/VAR_060061|||http://purl.uniprot.org/annotation/VAR_060062
http://togogenome.org/gene/9606:CLIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00299|||http://purl.uniprot.org/uniprot/Q53FB0|||http://purl.uniprot.org/uniprot/Q5SRT3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alternate|||Chloride intracellular channel protein 1|||GST C-terminal|||Helical; Note=After insertion into the membrane|||Loss of dimerization and of ion transport activity.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Required for insertion into the membrane|||S-glutathionyl cysteine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144201
http://togogenome.org/gene/9606:TPST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60704                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes sulfotransferase activity.|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Interaction with peptide substrate|||Loss of sulfotransferase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nearly complete loss of enzymatic activity.|||Prevents dimerization and decreases enzyme activity.|||Prevents dimerization and strongly decreases enzyme activity.|||Protein-tyrosine sulfotransferase 2|||Proton donor/acceptor|||Slightly decreased sulfotransferase activity.|||Strongly reduced enzymatic activity.|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189829
http://togogenome.org/gene/9606:LARGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95461|||http://purl.uniprot.org/uniprot/X5DR28                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glucuronyltransferase activity|||Glucuronyltransferase activity is present while xylosyltransferase activity is abolished.|||Helical|||Helical; Signal-anchor for type II membrane protein|||In MDDGA6.|||In MDDGB6.|||In isoform 2.|||Loss of function and abolishes subcellular location.|||Loss of function, but does not abolish subcellular location.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyl- and glucuronyltransferase LARGE1|||Xylosyltransferase activity|||Xylosyltransferase activity is present while glucuronyltransferase activity is abolished.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206060|||http://purl.uniprot.org/annotation/VAR_013685|||http://purl.uniprot.org/annotation/VAR_013686|||http://purl.uniprot.org/annotation/VAR_013687|||http://purl.uniprot.org/annotation/VAR_019811|||http://purl.uniprot.org/annotation/VAR_065064|||http://purl.uniprot.org/annotation/VAR_065065|||http://purl.uniprot.org/annotation/VAR_075304|||http://purl.uniprot.org/annotation/VSP_014536
http://togogenome.org/gene/9606:OTUB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DC9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes deubiquitinase activity.|||Affects its ability to cleave 'K63'-linked ubiquitin.|||In isoform 2.|||Loss of function in vitro.|||Nucleophile|||OTU|||Required to orient and stabilize the active site H-224|||Ubiquitin thioesterase OTUB2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221010|||http://purl.uniprot.org/annotation/VSP_009465
http://togogenome.org/gene/9606:OLFML3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNG0|||http://purl.uniprot.org/uniprot/M1LAK4|||http://purl.uniprot.org/uniprot/Q9NRN5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Olfactomedin-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020092|||http://purl.uniprot.org/annotation/PRO_5014306204|||http://purl.uniprot.org/annotation/VSP_014128|||http://purl.uniprot.org/annotation/VSP_014129|||http://purl.uniprot.org/annotation/VSP_014130|||http://purl.uniprot.org/annotation/VSP_014131
http://togogenome.org/gene/9606:TRAPPC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q05                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Phosphoserine|||Trafficking protein particle complex subunit 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341586|||http://purl.uniprot.org/annotation/VSP_034349|||http://purl.uniprot.org/annotation/VSP_034350
http://togogenome.org/gene/9606:MYB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10242|||http://purl.uniprot.org/uniprot/Q708E9                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||H-T-H motif|||HTH myb-type|||HTH myb-type 1|||HTH myb-type 2|||HTH myb-type 3|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||Interaction with HIPK2 and NLK|||Leucine-zipper|||Myb-like|||N6-acetyllysine|||N6-acetyllysine; alternate|||Negative regulatory domain|||Phosphoserine|||Phosphothreonine|||Transcription activation domain (PubMed:2189102)|||Transcriptional activator Myb                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197048|||http://purl.uniprot.org/annotation/VAR_050188|||http://purl.uniprot.org/annotation/VAR_050189|||http://purl.uniprot.org/annotation/VSP_003293|||http://purl.uniprot.org/annotation/VSP_003294|||http://purl.uniprot.org/annotation/VSP_003295|||http://purl.uniprot.org/annotation/VSP_003296|||http://purl.uniprot.org/annotation/VSP_003297|||http://purl.uniprot.org/annotation/VSP_003298|||http://purl.uniprot.org/annotation/VSP_003299|||http://purl.uniprot.org/annotation/VSP_046658|||http://purl.uniprot.org/annotation/VSP_046659|||http://purl.uniprot.org/annotation/VSP_046660|||http://purl.uniprot.org/annotation/VSP_046661|||http://purl.uniprot.org/annotation/VSP_053389
http://togogenome.org/gene/9606:SEPTIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH03                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||In isoform 3.|||Neuronal-specific septin-3|||Phosphoserine|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173517|||http://purl.uniprot.org/annotation/VSP_006049|||http://purl.uniprot.org/annotation/VSP_025398|||http://purl.uniprot.org/annotation/VSP_025399
http://togogenome.org/gene/9606:HSD17B12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GQ0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Allows the conversion of androstenedione to testosterone.|||Di-lysine motif|||Helical|||In isoform 2.|||No effect.|||Proton acceptor|||Very-long-chain 3-oxoacyl-CoA reductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248368|||http://purl.uniprot.org/annotation/VAR_027277|||http://purl.uniprot.org/annotation/VSP_056380|||http://purl.uniprot.org/annotation/VSP_056381
http://togogenome.org/gene/9606:ATF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2D1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Cyclic AMP-dependent transcription factor ATF-5|||Decreases protein levels.|||Disordered|||Highly increases protein levels. No effect on protein stability enhanced by IL1B.|||Increases protein levels.|||Increases protein levels. No effect on protein stability enhanced by IL1B.|||Interaction with PTP4A1|||Leucine-zipper|||N6-acetyllysine; by EP300|||No effect on protein levels. No effect on protein stability enhanced by IL1B.|||Not phosphorylated; when associated with 92-A--A-94 and A-126.|||Not phosphorylated; when associated with 92-A--A-94 and A-190.|||Not phosphorylated; when associated with A-126 and A-190.|||Phosphoserine|||Pro residues|||Required for protein stabilization induced by IL1B|||Resistant to cleavage by CASP3.|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076586|||http://purl.uniprot.org/annotation/VAR_022786
http://togogenome.org/gene/9606:SLC9A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48764                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes sodium:proton antiporter activity. Does not affect cell membrane expression or localization to recycling endosomes.|||Cytoplasmic|||Decreases cell membrane expression. Increases sodium:proton antiporter activity.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In DIAR8; decreases cell membrane expression; reduces Na(+)/H(+) exchange activity.|||In DIAR8; decreases cell membrane expression; strongly reduces Na(+)/H(+) exchange activity.|||In DIAR8; decreases cell membrane localization; strongly reduces Na(+)/H(+) exchange activity.|||In DIAR8; unknown pathological significance.|||In DIAR8; unknown pathological significance; does not affect cell membrane localization; reduces weakly Na(+)/H(+) exchange activity.|||In isoform 2.|||Increases sodium:proton antiporter activity.|||Increases sodium:proton antiporter activity; when associated with A-638.|||Interaction with AHCYL1|||Interaction with EZR|||Interaction with NHERF4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by SGK1|||Sodium/hydrogen exchanger 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052356|||http://purl.uniprot.org/annotation/VAR_060593|||http://purl.uniprot.org/annotation/VAR_076419|||http://purl.uniprot.org/annotation/VAR_076420|||http://purl.uniprot.org/annotation/VAR_076421|||http://purl.uniprot.org/annotation/VAR_076422|||http://purl.uniprot.org/annotation/VAR_088073|||http://purl.uniprot.org/annotation/VSP_053989
http://togogenome.org/gene/9606:PGLS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K7|||http://purl.uniprot.org/uniprot/O95336                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  6-phosphogluconolactonase|||Glucosamine/galactosamine-6-phosphate isomerase|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090078
http://togogenome.org/gene/9606:POLE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA polymerase epsilon subunit 3|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208341|||http://purl.uniprot.org/annotation/VAR_023464|||http://purl.uniprot.org/annotation/VAR_023465|||http://purl.uniprot.org/annotation/VAR_057527
http://togogenome.org/gene/9606:MED11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P086                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Mediator of RNA polymerase II transcription subunit 11|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304308
http://togogenome.org/gene/9606:ADAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWY7|||http://purl.uniprot.org/uniprot/Q6P2G0|||http://purl.uniprot.org/uniprot/Q99965                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 2|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029042|||http://purl.uniprot.org/annotation/PRO_0000029043|||http://purl.uniprot.org/annotation/PRO_5014567691|||http://purl.uniprot.org/annotation/PRO_5014587392|||http://purl.uniprot.org/annotation/VAR_035217|||http://purl.uniprot.org/annotation/VSP_005471
http://togogenome.org/gene/9606:HRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23327                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||2-4|||2-5|||2-6|||4 X tandem repeats, acidic|||6 X approximate tandem repeats|||Acidic residues|||Basic and acidic residues|||Disordered|||Metal-binding|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Sarcoplasmic reticulum histidine-rich calcium-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022414|||http://purl.uniprot.org/annotation/VAR_005623|||http://purl.uniprot.org/annotation/VAR_011622|||http://purl.uniprot.org/annotation/VAR_021931
http://togogenome.org/gene/9606:INTS6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSJ4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 3.|||Integrator complex subunit 6-like|||Phosphoserine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076215|||http://purl.uniprot.org/annotation/VAR_069425|||http://purl.uniprot.org/annotation/VSP_016867
http://togogenome.org/gene/9606:DNAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96015                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Dynein axonemal light chain 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195136
http://togogenome.org/gene/9606:WDFY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W7HCV9|||http://purl.uniprot.org/uniprot/Q6ZS81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat- and FYVE domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251254|||http://purl.uniprot.org/annotation/VAR_027684|||http://purl.uniprot.org/annotation/VAR_027685|||http://purl.uniprot.org/annotation/VAR_047261|||http://purl.uniprot.org/annotation/VSP_020750|||http://purl.uniprot.org/annotation/VSP_020751|||http://purl.uniprot.org/annotation/VSP_035683|||http://purl.uniprot.org/annotation/VSP_035684|||http://purl.uniprot.org/annotation/VSP_035685|||http://purl.uniprot.org/annotation/VSP_035686|||http://purl.uniprot.org/annotation/VSP_035687
http://togogenome.org/gene/9606:FCER1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12319                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||High affinity immunoglobulin epsilon receptor subunit alpha|||Ig-like 1|||Ig-like 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015161|||http://purl.uniprot.org/annotation/VAR_020091|||http://purl.uniprot.org/annotation/VAR_020092
http://togogenome.org/gene/9606:SMUG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z526|||http://purl.uniprot.org/uniprot/Q53HV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-binding|||Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A.|||Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C. hoC-excising activity for hoC/A, hoC/T and hoC/C.|||In isoform 2.|||Loss of damage-excising activity for U/G. Weak, but significant activity toward hoU/G, hmU/A and fU/A.|||Loss of damage-excising activity.|||Markedly impaired damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C.|||Markedly impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A.|||No effect on damage-excising activity for U/G, hoU/G, hmU/A and fU/A.|||Single-strand selective monofunctional uracil DNA glycosylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071992|||http://purl.uniprot.org/annotation/VAR_023243|||http://purl.uniprot.org/annotation/VAR_023244|||http://purl.uniprot.org/annotation/VSP_015150|||http://purl.uniprot.org/annotation/VSP_015151
http://togogenome.org/gene/9606:B3GNTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q67FW5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289220|||http://purl.uniprot.org/annotation/VAR_032603
http://togogenome.org/gene/9606:SYCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1R9|||http://purl.uniprot.org/uniprot/Q8N0S2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Synaptonemal complex central element protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261426|||http://purl.uniprot.org/annotation/VAR_029385|||http://purl.uniprot.org/annotation/VAR_029386|||http://purl.uniprot.org/annotation/VAR_029387|||http://purl.uniprot.org/annotation/VSP_021690|||http://purl.uniprot.org/annotation/VSP_021691|||http://purl.uniprot.org/annotation/VSP_021692
http://togogenome.org/gene/9606:CFAP43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDM7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 43|||In HYDNP1.|||In SPGF19.|||In SPGF19; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310989|||http://purl.uniprot.org/annotation/VAR_037130|||http://purl.uniprot.org/annotation/VAR_037131|||http://purl.uniprot.org/annotation/VAR_037132|||http://purl.uniprot.org/annotation/VAR_037133|||http://purl.uniprot.org/annotation/VAR_080878|||http://purl.uniprot.org/annotation/VAR_080879|||http://purl.uniprot.org/annotation/VAR_080880|||http://purl.uniprot.org/annotation/VAR_080881|||http://purl.uniprot.org/annotation/VAR_080882|||http://purl.uniprot.org/annotation/VAR_080883|||http://purl.uniprot.org/annotation/VAR_080884|||http://purl.uniprot.org/annotation/VAR_080885|||http://purl.uniprot.org/annotation/VAR_083523|||http://purl.uniprot.org/annotation/VSP_029369|||http://purl.uniprot.org/annotation/VSP_029370|||http://purl.uniprot.org/annotation/VSP_029371|||http://purl.uniprot.org/annotation/VSP_029372|||http://purl.uniprot.org/annotation/VSP_029373|||http://purl.uniprot.org/annotation/VSP_029374
http://togogenome.org/gene/9606:KIF21A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4S6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Does not bind to KANK1 or KANK2.|||In CFEOM1.|||In CFEOM1; de novo mutation.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Interaction with KANK1 and KANK2|||Kinesin motor|||Kinesin-like protein KIF21A|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Very weak binding affinity for KANK1 and KANK2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125462|||http://purl.uniprot.org/annotation/VAR_019399|||http://purl.uniprot.org/annotation/VAR_019400|||http://purl.uniprot.org/annotation/VAR_019401|||http://purl.uniprot.org/annotation/VAR_019402|||http://purl.uniprot.org/annotation/VAR_019403|||http://purl.uniprot.org/annotation/VAR_019404|||http://purl.uniprot.org/annotation/VAR_027021|||http://purl.uniprot.org/annotation/VAR_074031|||http://purl.uniprot.org/annotation/VAR_074032|||http://purl.uniprot.org/annotation/VAR_074033|||http://purl.uniprot.org/annotation/VAR_074034|||http://purl.uniprot.org/annotation/VSP_010870|||http://purl.uniprot.org/annotation/VSP_010871|||http://purl.uniprot.org/annotation/VSP_010872|||http://purl.uniprot.org/annotation/VSP_046790|||http://purl.uniprot.org/annotation/VSP_046791|||http://purl.uniprot.org/annotation/VSP_046792
http://togogenome.org/gene/9606:FAM184A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BY63|||http://purl.uniprot.org/uniprot/Q6P9G8|||http://purl.uniprot.org/uniprot/Q8NB25                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein FAM184A|||Protein FAM184A/B N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089512|||http://purl.uniprot.org/annotation/VAR_054101|||http://purl.uniprot.org/annotation/VAR_054102|||http://purl.uniprot.org/annotation/VAR_054103|||http://purl.uniprot.org/annotation/VSP_007446|||http://purl.uniprot.org/annotation/VSP_007447|||http://purl.uniprot.org/annotation/VSP_039102|||http://purl.uniprot.org/annotation/VSP_039103|||http://purl.uniprot.org/annotation/VSP_044520
http://togogenome.org/gene/9606:MIGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK63|||http://purl.uniprot.org/uniprot/B7ZLZ8|||http://purl.uniprot.org/uniprot/F8W7S1|||http://purl.uniprot.org/uniprot/Q8NAN2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitoguardin 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285646|||http://purl.uniprot.org/annotation/VSP_024878|||http://purl.uniprot.org/annotation/VSP_024879
http://togogenome.org/gene/9606:UTP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3A2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Probable U3 small nucleolar RNA-associated protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211042|||http://purl.uniprot.org/annotation/VSP_056872
http://togogenome.org/gene/9606:NOXRED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NXP6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||NADP-dependent oxidoreductase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280279|||http://purl.uniprot.org/annotation/VSP_038392
http://togogenome.org/gene/9606:FAM24A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFZ4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Protein FAM24A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317244
http://togogenome.org/gene/9606:CNTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26441                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Ciliary neurotrophic factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149519|||http://purl.uniprot.org/annotation/VAR_013924|||http://purl.uniprot.org/annotation/VAR_033777
http://togogenome.org/gene/9606:XAGE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SY49|||http://purl.uniprot.org/uniprot/Q8WWM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GAGE|||Polar residues|||X antigen family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148352
http://togogenome.org/gene/9606:SAXO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ57|||http://purl.uniprot.org/uniprot/F6S232|||http://purl.uniprot.org/uniprot/Q8IYX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Mn 1|||Mn 10|||Mn 12|||Mn 2|||Mn 3|||Mn 4|||Mn 5|||Mn 6|||Mn 7|||Mn 8|||Mn 9|||No effect on subcellular location.|||Polar residues|||Stabilizer of axonemal microtubules 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089737|||http://purl.uniprot.org/annotation/VAR_023229|||http://purl.uniprot.org/annotation/VAR_023230|||http://purl.uniprot.org/annotation/VAR_057807
http://togogenome.org/gene/9606:ADAM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78325|||http://purl.uniprot.org/uniprot/Q14C66                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 8|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029060|||http://purl.uniprot.org/annotation/PRO_5014306935|||http://purl.uniprot.org/annotation/VAR_059760|||http://purl.uniprot.org/annotation/VAR_061735|||http://purl.uniprot.org/annotation/VAR_061736|||http://purl.uniprot.org/annotation/VAR_061737|||http://purl.uniprot.org/annotation/VAR_069144|||http://purl.uniprot.org/annotation/VAR_069145|||http://purl.uniprot.org/annotation/VSP_046154|||http://purl.uniprot.org/annotation/VSP_046155|||http://purl.uniprot.org/annotation/VSP_046156|||http://purl.uniprot.org/annotation/VSP_046157|||http://purl.uniprot.org/annotation/VSP_046158|||http://purl.uniprot.org/annotation/VSP_046159
http://togogenome.org/gene/9606:ZDHHC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXF8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Lumenal|||Palmitoyltransferase ZDHHC7|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212874|||http://purl.uniprot.org/annotation/VAR_028360|||http://purl.uniprot.org/annotation/VAR_036261|||http://purl.uniprot.org/annotation/VSP_006942
http://togogenome.org/gene/9606:GLS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X004|||http://purl.uniprot.org/uniprot/Q9UI32                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Basic and acidic residues|||Disordered|||Glutaminase liver isoform, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011625|||http://purl.uniprot.org/annotation/VAR_031615|||http://purl.uniprot.org/annotation/VSP_057009|||http://purl.uniprot.org/annotation/VSP_057010
http://togogenome.org/gene/9606:PRIMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PRAD|||Pro residues|||Proline-rich membrane anchor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022107|||http://purl.uniprot.org/annotation/VAR_035980|||http://purl.uniprot.org/annotation/VSP_008494|||http://purl.uniprot.org/annotation/VSP_008495
http://togogenome.org/gene/9606:CPEB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5K1VW61|||http://purl.uniprot.org/uniprot/A0A5K1VW71|||http://purl.uniprot.org/uniprot/A0A5K1VW79|||http://purl.uniprot.org/uniprot/A0A5K1VW93|||http://purl.uniprot.org/uniprot/Q7Z5Q1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cytoplasmic polyadenylation element-binding protein 2|||Disordered|||In isoform 2 and isoform 6.|||In isoform 2, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 6 and isoform 7.|||In isoform 4 and isoform 5.|||In isoform 7 and isoform 8.|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269259|||http://purl.uniprot.org/annotation/VSP_022030|||http://purl.uniprot.org/annotation/VSP_022031|||http://purl.uniprot.org/annotation/VSP_022032|||http://purl.uniprot.org/annotation/VSP_027372|||http://purl.uniprot.org/annotation/VSP_055670
http://togogenome.org/gene/9606:BPNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95861                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'(2'),5'-bisphosphate nucleotidase 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142527|||http://purl.uniprot.org/annotation/VSP_009937|||http://purl.uniprot.org/annotation/VSP_054807|||http://purl.uniprot.org/annotation/VSP_054808
http://togogenome.org/gene/9606:MNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99583                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Leucine-zipper|||Max-binding protein MNT|||N-acetylserine|||Pro residues|||Removed|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127281|||http://purl.uniprot.org/annotation/VAR_061258
http://togogenome.org/gene/9606:OR51Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH59                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150761|||http://purl.uniprot.org/annotation/VAR_024144|||http://purl.uniprot.org/annotation/VAR_034326|||http://purl.uniprot.org/annotation/VAR_034327|||http://purl.uniprot.org/annotation/VAR_034328|||http://purl.uniprot.org/annotation/VAR_053329|||http://purl.uniprot.org/annotation/VAR_053330
http://togogenome.org/gene/9606:DENND2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78524                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DENN domain-containing protein 2B|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with ABL1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247448|||http://purl.uniprot.org/annotation/VAR_027101|||http://purl.uniprot.org/annotation/VAR_027102|||http://purl.uniprot.org/annotation/VAR_027103|||http://purl.uniprot.org/annotation/VAR_027104|||http://purl.uniprot.org/annotation/VAR_030642|||http://purl.uniprot.org/annotation/VSP_019987|||http://purl.uniprot.org/annotation/VSP_019988
http://togogenome.org/gene/9606:SREBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR77|||http://purl.uniprot.org/uniprot/P36956                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  9aaTAD|||Abolished transactivation activity.|||BHLH|||Basic and acidic residues|||Cleavage; by MBTPS1|||Cleavage; by MBTPS2|||Cleavage; by caspase-3 and caspase-7|||Cytoplasmic|||Disordered|||Helical|||In HMD.|||In IFAP2 and HMD; loss of sterol-regulated protein processing; loss of localization to the nucleus; decreased DNA-binding transcription factor activity RNA polymerase II-specific.|||In IFAP2; loss of sterol-regulated protein processing; loss of localization to the nucleus; decreased DNA-binding transcription factor activity RNA polymerase II-specific.|||In isoform 4.|||In isoform SREBP-1B and isoform SREBP-1C.|||In isoform SREBP-1C and isoform SREBP-1cDelta.|||In isoform SREBP-1aDelta and isoform SREBP-1cDelta.|||Interaction with LMNA|||Leucine-zipper|||Loss of proteolytic processing in response to low sterol.|||Loss of proteolytic processing in response to low sterol. Transcriptionally inactive.|||Lumenal|||No effect on proteolytic processing.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by SIK1|||Polar residues|||Pro residues|||Processed sterol regulatory element-binding protein 1|||Sterol regulatory element-binding protein 1|||Strong reduction of proteolytic processing in response to low sterol.|||Transcriptional activation (acidic)|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127447|||http://purl.uniprot.org/annotation/PRO_0000314029|||http://purl.uniprot.org/annotation/VAR_038468|||http://purl.uniprot.org/annotation/VAR_038469|||http://purl.uniprot.org/annotation/VAR_038470|||http://purl.uniprot.org/annotation/VAR_038471|||http://purl.uniprot.org/annotation/VAR_038472|||http://purl.uniprot.org/annotation/VAR_038473|||http://purl.uniprot.org/annotation/VAR_038474|||http://purl.uniprot.org/annotation/VAR_038475|||http://purl.uniprot.org/annotation/VAR_085079|||http://purl.uniprot.org/annotation/VAR_085080|||http://purl.uniprot.org/annotation/VAR_085081|||http://purl.uniprot.org/annotation/VAR_085082|||http://purl.uniprot.org/annotation/VSP_002149|||http://purl.uniprot.org/annotation/VSP_002150|||http://purl.uniprot.org/annotation/VSP_030859|||http://purl.uniprot.org/annotation/VSP_047598|||http://purl.uniprot.org/annotation/VSP_047599
http://togogenome.org/gene/9606:PPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15181                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Inorganic pyrophosphatase|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137567|||http://purl.uniprot.org/annotation/VAR_036358
http://togogenome.org/gene/9606:NDUFB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95168                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylserine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118800|||http://purl.uniprot.org/annotation/VSP_042719
http://togogenome.org/gene/9606:BCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3N9|||http://purl.uniprot.org/uniprot/P20749                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||B-cell lymphoma 3 protein|||Disordered|||Phosphoserine|||Phosphoserine; by GSK3|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066976
http://togogenome.org/gene/9606:REXO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1G1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exonuclease|||Interaction with ELOA|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA exonuclease 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239232|||http://purl.uniprot.org/annotation/VAR_026587|||http://purl.uniprot.org/annotation/VAR_057148|||http://purl.uniprot.org/annotation/VAR_057149|||http://purl.uniprot.org/annotation/VAR_060444
http://togogenome.org/gene/9606:FKTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2W4|||http://purl.uniprot.org/uniprot/O75072                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decrease in ribitol-5-phosphate transferase activity.|||Helical; Signal-anchor for type II membrane protein|||In CMD1X.|||In MDDGA4.|||In MDDGA4; loss of normal location in Golgi membranes.|||In MDDGB4 and MDDGC4; the mutant protein is expressed and localized correctly within the cell, decrease in ribitol-5-phosphate transferase activity..|||In MDDGB4.|||In MDDGC4.|||In a breast cancer sample; somatic mutation.|||In a patient diagnosed with Walker-Warburg syndrome.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Required and sufficient for interaction with POMGNT1|||Ribitol-5-phosphate transferase FKTN|||Ribitol-5-phosphate transferase FKTN N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204720|||http://purl.uniprot.org/annotation/VAR_018278|||http://purl.uniprot.org/annotation/VAR_018279|||http://purl.uniprot.org/annotation/VAR_033926|||http://purl.uniprot.org/annotation/VAR_033927|||http://purl.uniprot.org/annotation/VAR_036334|||http://purl.uniprot.org/annotation/VAR_036335|||http://purl.uniprot.org/annotation/VAR_039287|||http://purl.uniprot.org/annotation/VAR_039288|||http://purl.uniprot.org/annotation/VAR_039289|||http://purl.uniprot.org/annotation/VAR_061296|||http://purl.uniprot.org/annotation/VAR_065050|||http://purl.uniprot.org/annotation/VAR_065051|||http://purl.uniprot.org/annotation/VAR_065052|||http://purl.uniprot.org/annotation/VAR_065053|||http://purl.uniprot.org/annotation/VAR_065054|||http://purl.uniprot.org/annotation/VSP_045961
http://togogenome.org/gene/9606:OR2M3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV67|||http://purl.uniprot.org/uniprot/Q8NG83                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2M3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150492
http://togogenome.org/gene/9606:TICAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage by CV3B|||(Microbial infection) Cleavage; by viral EV68 protease C|||(Microbial infection) Cleavage; by viral HAV 3CD|||(Microbial infection) Cleavage; by viral HCV NS3/4A|||(Microbial infection) Cleavage; by viral Seneca Valley virus protease 3C|||Abolished ability to activate IRF3.|||Abolished interaction with IRF3.|||Abolishes interaction with TLR3.|||Complete loss of cleavage by CV3B; when associated with A-653; A-659 and A-671.|||Complete loss of cleavage by CV3B; when associated with A-653; A-659 and A-702.|||Complete loss of cleavage by CV3B; when associated with A-653; A-671 and A-702.|||Complete loss of cleavage by CV3B; when associated with A-659; A-671 and A-702.|||Complete loss of cleavage by HCVNS3/4A protease.|||Complete loss of cleavage by Seneca Valley virus protease 3C.|||Decreased interaction with IRF3.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IIAE6; no effect on IFNB induction.|||In a breast cancer sample; somatic mutation.|||Inhibition of IFNB induction.|||Loss of TCAM1-induced NF-kappa-B activation. Reduces interaction with TRAF6 and activation of NF-kappa-B signaling pathway; when associated with A-88 and A-303.|||Loss of TCAM1-induced NF-kappa-B and IRF3 activation.|||No cleavage by HAV 3CD.|||No effect on IFNB induction.|||No effect on cleavage by Seneca Valley virus protease 3C.|||Phosphoserine; by TBK1|||Polar residues|||Pro residues|||Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-252 and A-303.|||Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-88 and A-252.|||Resistant to caspase cleavage, no effect on TRIM38-mediated degradation; when associated with E-281.|||Resistant to caspase cleavage, no effect on TRIM38-mediated degradation; when associated with E-289.|||Sufficient to induce apoptosis|||TIR|||TIR domain-containing adapter molecule 1|||TRAF6-binding|||TRIF-NTD|||pLxIS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317663|||http://purl.uniprot.org/annotation/VAR_038789|||http://purl.uniprot.org/annotation/VAR_051416|||http://purl.uniprot.org/annotation/VAR_051417|||http://purl.uniprot.org/annotation/VAR_051418|||http://purl.uniprot.org/annotation/VAR_069082|||http://purl.uniprot.org/annotation/VAR_084053|||http://purl.uniprot.org/annotation/VAR_084054|||http://purl.uniprot.org/annotation/VAR_084055|||http://purl.uniprot.org/annotation/VAR_084056|||http://purl.uniprot.org/annotation/VAR_084057|||http://purl.uniprot.org/annotation/VAR_084058|||http://purl.uniprot.org/annotation/VAR_084059|||http://purl.uniprot.org/annotation/VAR_084060|||http://purl.uniprot.org/annotation/VAR_084061|||http://purl.uniprot.org/annotation/VAR_084062|||http://purl.uniprot.org/annotation/VAR_084063|||http://purl.uniprot.org/annotation/VAR_084064|||http://purl.uniprot.org/annotation/VAR_084065|||http://purl.uniprot.org/annotation/VAR_084066|||http://purl.uniprot.org/annotation/VAR_084067|||http://purl.uniprot.org/annotation/VAR_084068
http://togogenome.org/gene/9606:TMEM97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BJF2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes DTG binding.|||Cytoplasmic|||Decreases DTG binding.|||EXPERA|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||No effect on DTG binding.|||Sigma intracellular receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254567
http://togogenome.org/gene/9606:BRD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60885                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to acetylated histones.|||Acetylated histone binding|||BID region|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form BDR4-NUTM1 fusion protein|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 4|||C-terminal (CTD) region|||Decreases interaction with JMJD6 and NSD3.No effect on interaction with histone 4 acetylated.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired phosphorylation by CK2 and binding to acetylated histones.|||In isoform B.|||In isoform C.|||N6-acetyllysine; alternate|||NET|||NPS region|||Phosphoserine|||Phosphoserine; by CK2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211183|||http://purl.uniprot.org/annotation/VAR_041919|||http://purl.uniprot.org/annotation/VAR_041920|||http://purl.uniprot.org/annotation/VAR_041921|||http://purl.uniprot.org/annotation/VAR_041922|||http://purl.uniprot.org/annotation/VAR_041923|||http://purl.uniprot.org/annotation/VAR_048427|||http://purl.uniprot.org/annotation/VSP_010902|||http://purl.uniprot.org/annotation/VSP_010903|||http://purl.uniprot.org/annotation/VSP_047671
http://togogenome.org/gene/9606:HDLBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4E5|||http://purl.uniprot.org/uniprot/B2R5V9|||http://purl.uniprot.org/uniprot/Q00341                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||K Homology|||KH 1|||KH 10|||KH 11|||KH 12|||KH 13|||KH 14|||KH 2|||KH 3|||KH 4|||KH 5|||KH 6|||KH 7|||KH 8|||KH 9|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Vigilin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050131|||http://purl.uniprot.org/annotation/VAR_024511|||http://purl.uniprot.org/annotation/VAR_029279|||http://purl.uniprot.org/annotation/VAR_036052|||http://purl.uniprot.org/annotation/VAR_036053|||http://purl.uniprot.org/annotation/VAR_047976|||http://purl.uniprot.org/annotation/VAR_055981|||http://purl.uniprot.org/annotation/VSP_044924|||http://purl.uniprot.org/annotation/VSP_044925
http://togogenome.org/gene/9606:CCDC83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 83|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288881|||http://purl.uniprot.org/annotation/VAR_032525|||http://purl.uniprot.org/annotation/VSP_025808|||http://purl.uniprot.org/annotation/VSP_025809|||http://purl.uniprot.org/annotation/VSP_025810|||http://purl.uniprot.org/annotation/VSP_025811
http://togogenome.org/gene/9606:MEIOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N635                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SPGF22.|||In isoform 2.|||Meiosis-specific with OB domain-containing protein|||OB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337134|||http://purl.uniprot.org/annotation/VAR_043620|||http://purl.uniprot.org/annotation/VAR_059624|||http://purl.uniprot.org/annotation/VAR_061619|||http://purl.uniprot.org/annotation/VAR_080034|||http://purl.uniprot.org/annotation/VSP_047664
http://togogenome.org/gene/9606:TMEM256                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2U0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N6-acetyllysine|||Transmembrane protein 256                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287170
http://togogenome.org/gene/9606:GRID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43424                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Essential for dimerization|||Extracellular|||Glutamate receptor ionotropic, delta-2|||Helical|||Impairs the ability of the LBD to induce pore closure. No effect on synapse assembly. No effect on cerebellar parallel fiber-Purkinje cell synapse formation. Abolishes D-Serine?dependent long term synaptic depression at PF-PC synapses. Does not affect motor coordination.|||In SCAR18.|||In SCAR18; constitutively open the extracellular-glutamate-gated ion channel.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with AP4M1|||Interaction with CBLN1 homotrimer|||Monomeric form. Does not dimerize. Weakly interacts with C1q domain of CBLN1. Forms intermediate synapse. Abolishes cerebellar parallel fiber-Purkinje cell synapse formation. Abolishes D-Serine?dependent long term synaptic depression at PF-PC synapses. Does not recover motor coordination in experiment of transfection in Grid2-null mice.|||N-linked (GlcNAc...) asparagine|||No effect on CBLN1 interaction; when associated with D76.|||No effect on CBLN1 interaction; when associated with D76. No effect on CBLN1 binding; when associated with D-76; A-343; A-346 and A-349. No effect on synapse assembly; when associated with A-343; A-346 and A-349. No effect on cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-343; A-346 and A-349. Does not affect D-Serine?dependent long term synaptic depression at PF-PC synapses; when associated with A-343; A-346 and A-349. Does not affect motor coordination; when associated with A-343; A-346 and A-349.|||No effect on CBLN1 interaction; when associated with D76. No effect on CBLN1 binding; when associated with D-76; A-343; A-346 and A-350. No effect on synapse assembly; when associated with A-343; A-346 and A-350. No effect on cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-343; A-346 and A-350. Does not affect D-Serine?dependent long term synaptic depression at PF-PC synapses; when associated with A-343; A-346 and A-350. Does not affect motor coordination; when associated with A-343; A-346 and A-350.|||No effect on CBLN1 interaction; when associated with D76. No effect on CBLN1 binding; when associated with D-76; A-343; A-349 and A-350. No effect on synapse assembly; when associated with A-343; A-349 and A-350. No effect on cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-343; A-349 and A-350. Does not affect D-Serine?dependent long term synaptic depression at PF-PC synapses; when associated with A-343; A-349 and A-350. Does not affect motor coordination; when associated with A-343; A-349 and A-350.|||No effect on CBLN1 interaction; when associated with D76. No effect on CBLN1 binding; when associated with D-76; A-346; A-349 and A-350. No effect on synapse assembly; when associated with A-346; A-349 and A-350. No effect on cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-346; A-349 and A-350. Does not affect D-Serine?dependent long term synaptic depression at PF-PC synapses; when associated with A-346; A-349 and A-350. Does not affect motor coordination; when associated with A-346; A-349 and A-350.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Reduces binding to CBLN1; when associated with D76.|||Reduces binding to CBLN1; when associated with D76. Abolishes CBLN1 binding; when associated with A-24; A-26; A-61 and D-76. Abolishes synapse assembly; when associated with A-24; A-26 and A-61. Abolishes cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-24; A-26 and A-61. Abolishes D-Serine-dependent long term synaptic depression at PF-PC synapses; when associated with A-24; A-26 and A-61.|||Reduces binding to CBLN1; when associated with D76. Abolishes CBLN1 binding; when associated with A-24; A-26; D-76 and A-345. Abolishes synapse assembly; when associated with A-24; A-26 and A-345. Abolishes cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-24; A-26 and A-345. Abolishes D-Serine-dependent long term synaptic depression at PF-PC synapses; when associated with A-24; A-26 and A-345.|||Reduces binding to CBLN1; when associated with D76. Abolishes CBLN1 binding; when associated with A-24; A-61; D-76 and A-345. Abolishes synapse assembly; when associated with A-24; A-61 and A-345. Abolishes cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-24; A-61 and A-345. Abolishes D-Serine-dependent long term synaptic depression at PF-PC synapses; when associated with A-24; A-61 and A-345.|||Reduces binding to CBLN1; when associated with D76. Abolishes CBLN1 binding; when associated with A-26; A-61; D-76 and A-345. Abolishes synapse assembly; when associated with A-26; A-61 and A-345. Abolishes cerebellar parallel fiber-Purkinje cell synapse formation; when associated with A-26; A-61 and A-345. Abolishes D-Serine-dependent long term synaptic depression at PF-PC synapses; when associated with A-26; A-61 and A-345. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011564|||http://purl.uniprot.org/annotation/VAR_035697|||http://purl.uniprot.org/annotation/VAR_055016|||http://purl.uniprot.org/annotation/VAR_055017|||http://purl.uniprot.org/annotation/VAR_055018|||http://purl.uniprot.org/annotation/VAR_074166|||http://purl.uniprot.org/annotation/VAR_074167|||http://purl.uniprot.org/annotation/VAR_074168|||http://purl.uniprot.org/annotation/VSP_054704
http://togogenome.org/gene/9606:SMC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2S1ZR87|||http://purl.uniprot.org/uniprot/Q96SB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Flexible hinge|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||RecF/RecN/SMC N-terminal|||Structural maintenance of chromosomes protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270956|||http://purl.uniprot.org/annotation/VAR_029826|||http://purl.uniprot.org/annotation/VAR_029827|||http://purl.uniprot.org/annotation/VAR_035875|||http://purl.uniprot.org/annotation/VAR_052441|||http://purl.uniprot.org/annotation/VAR_052442|||http://purl.uniprot.org/annotation/VSP_022253
http://togogenome.org/gene/9606:DSCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVC3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Sister chromatid cohesion protein DCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318064|||http://purl.uniprot.org/annotation/VAR_038682
http://togogenome.org/gene/9606:CFH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SG88|||http://purl.uniprot.org/uniprot/P08603                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  About 10% loss of heparin-binding.|||About 20% loss of C3b binding.|||About 20% loss of heparin-binding.|||About 30% loss of C3b binding.|||About 40% loss of C3b binding.|||About 50% loss of C3b binding.|||Associated with ARMD4.|||Associated with basal laminar drusen.|||Associated with hemolytic uremic syndrome and basal laminar drusen.|||Complement factor H|||Confirmed at protein level.|||In AHUS1.|||In AHUS1; atypical.|||In AHUS1; variant confirmed at protein level.|||In CFHD and ARMD4; rare penetrant mutation that confers high risk of age-related macular degeneration.|||In CFHD.|||In CFHD; variant confirmed at protein level.|||In CFHD; with membranoproliferative glomerulonephritis.|||In CFHD; with membranoproliferative glomerulonephritis; affects binding of factor H to C3b and shows defective complement regulation.|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005894|||http://purl.uniprot.org/annotation/PRO_5002346915|||http://purl.uniprot.org/annotation/VAR_001979|||http://purl.uniprot.org/annotation/VAR_019405|||http://purl.uniprot.org/annotation/VAR_019406|||http://purl.uniprot.org/annotation/VAR_019407|||http://purl.uniprot.org/annotation/VAR_019408|||http://purl.uniprot.org/annotation/VAR_019409|||http://purl.uniprot.org/annotation/VAR_020261|||http://purl.uniprot.org/annotation/VAR_023836|||http://purl.uniprot.org/annotation/VAR_025092|||http://purl.uniprot.org/annotation/VAR_025093|||http://purl.uniprot.org/annotation/VAR_025094|||http://purl.uniprot.org/annotation/VAR_025095|||http://purl.uniprot.org/annotation/VAR_025096|||http://purl.uniprot.org/annotation/VAR_025097|||http://purl.uniprot.org/annotation/VAR_025864|||http://purl.uniprot.org/annotation/VAR_025865|||http://purl.uniprot.org/annotation/VAR_025866|||http://purl.uniprot.org/annotation/VAR_025867|||http://purl.uniprot.org/annotation/VAR_025868|||http://purl.uniprot.org/annotation/VAR_025869|||http://purl.uniprot.org/annotation/VAR_025870|||http://purl.uniprot.org/annotation/VAR_025871|||http://purl.uniprot.org/annotation/VAR_025872|||http://purl.uniprot.org/annotation/VAR_025873|||http://purl.uniprot.org/annotation/VAR_025874|||http://purl.uniprot.org/annotation/VAR_025875|||http://purl.uniprot.org/annotation/VAR_025876|||http://purl.uniprot.org/annotation/VAR_025877|||http://purl.uniprot.org/annotation/VAR_025878|||http://purl.uniprot.org/annotation/VAR_025879|||http://purl.uniprot.org/annotation/VAR_025880|||http://purl.uniprot.org/annotation/VAR_025881|||http://purl.uniprot.org/annotation/VAR_025882|||http://purl.uniprot.org/annotation/VAR_025883|||http://purl.uniprot.org/annotation/VAR_025884|||http://purl.uniprot.org/annotation/VAR_025885|||http://purl.uniprot.org/annotation/VAR_025886|||http://purl.uniprot.org/annotation/VAR_025887|||http://purl.uniprot.org/annotation/VAR_025888|||http://purl.uniprot.org/annotation/VAR_031978|||http://purl.uniprot.org/annotation/VAR_031979|||http://purl.uniprot.org/annotation/VAR_031980|||http://purl.uniprot.org/annotation/VAR_031981|||http://purl.uniprot.org/annotation/VAR_031982|||http://purl.uniprot.org/annotation/VAR_031983|||http://purl.uniprot.org/annotation/VAR_031984|||http://purl.uniprot.org/annotation/VAR_031985|||http://purl.uniprot.org/annotation/VAR_031986|||http://purl.uniprot.org/annotation/VAR_043892|||http://purl.uniprot.org/annotation/VAR_043893|||http://purl.uniprot.org/annotation/VAR_043894|||http://purl.uniprot.org/annotation/VAR_043895|||http://purl.uniprot.org/annotation/VAR_043896|||http://purl.uniprot.org/annotation/VAR_055683|||http://purl.uniprot.org/annotation/VAR_055684|||http://purl.uniprot.org/annotation/VAR_063648|||http://purl.uniprot.org/annotation/VAR_063649|||http://purl.uniprot.org/annotation/VAR_063650|||http://purl.uniprot.org/annotation/VAR_063651|||http://purl.uniprot.org/annotation/VSP_001190|||http://purl.uniprot.org/annotation/VSP_001191
http://togogenome.org/gene/9606:LAMB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07942|||http://purl.uniprot.org/uniprot/Q8TAS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Domain I|||Domain II|||Domain alpha|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; truncated|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin IV type B|||Laminin N-terminal|||Laminin subunit beta-1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017065|||http://purl.uniprot.org/annotation/VAR_014698|||http://purl.uniprot.org/annotation/VAR_014699|||http://purl.uniprot.org/annotation/VAR_032774|||http://purl.uniprot.org/annotation/VAR_061349
http://togogenome.org/gene/9606:CYB5R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00387                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased NADH-cytochrome b5 reductase activity, highly increases Km for NADH and decreases Kcat.|||Decreases protein stability and slightly decreases NADH-cytochrome b5 reductase activity.|||FAD-binding FR-type|||In METHB-CYB5R3.|||In METHB-CYB5R3; type 1.|||In METHB-CYB5R3; type 1; 62% of activity.|||In METHB-CYB5R3; type 1; 77% of activity.|||In METHB-CYB5R3; type 1; reduced protein stability; no effect on NADH-cytochrome b5 reductase activity.|||In METHB-CYB5R3; type 1; retains approximately 38% of residual NADH-cytochrome b5 reductase activity.|||In METHB-CYB5R3; type 1; retains approximately 58% of residual NADH-cytochrome b5 reductase activity.|||In METHB-CYB5R3; type 2.|||In METHB-CYB5R3; type 2; Hiroshima; decreased NADH-cytochrome b5 reductase activity; highly increased Km for NADH and decreased Kcat.|||In METHB-CYB5R3; type2; almost complete loss of activity.|||In isoform 2.|||In isoform 3.|||Loss of 30% of NADH-cytochrome b5 reductase activity.|||Loss of 80% of NADH-cytochrome b5 reductase activity.|||N-myristoyl glycine|||N6-acetyllysine|||NADH-cytochrome b5 reductase 3|||No effect on NADH-cytochrome b5 reductase activity.|||No effect on protein stability and NADH-cytochrome b5 reductase activity.|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019392|||http://purl.uniprot.org/annotation/VAR_004619|||http://purl.uniprot.org/annotation/VAR_004620|||http://purl.uniprot.org/annotation/VAR_004621|||http://purl.uniprot.org/annotation/VAR_004622|||http://purl.uniprot.org/annotation/VAR_004623|||http://purl.uniprot.org/annotation/VAR_010750|||http://purl.uniprot.org/annotation/VAR_010751|||http://purl.uniprot.org/annotation/VAR_010752|||http://purl.uniprot.org/annotation/VAR_010753|||http://purl.uniprot.org/annotation/VAR_010754|||http://purl.uniprot.org/annotation/VAR_010755|||http://purl.uniprot.org/annotation/VAR_018419|||http://purl.uniprot.org/annotation/VAR_037315|||http://purl.uniprot.org/annotation/VAR_037316|||http://purl.uniprot.org/annotation/VSP_010200|||http://purl.uniprot.org/annotation/VSP_042827
http://togogenome.org/gene/9606:CIMIP2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJV1|||http://purl.uniprot.org/uniprot/B8ZZ55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Ciliary microtubule inner protein 2C|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332277|||http://purl.uniprot.org/annotation/VAR_042998|||http://purl.uniprot.org/annotation/VAR_054056
http://togogenome.org/gene/9606:LAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZY6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||Linker for activation of T-cells family member 2|||No change in phosphorylation upon BCR activation.|||Phosphoserine|||Phosphotyrosine|||Reduces phosphorylation upon BCR activation.|||S-palmitoyl cysteine|||Slightly reduces phosphorylation upon BCR activation.|||Strongly reduces phosphorylation upon BCR activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083334|||http://purl.uniprot.org/annotation/VSP_016643
http://togogenome.org/gene/9606:MED22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15528                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform Surf5A.|||Mediator of RNA polymerase II transcription subunit 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178838|||http://purl.uniprot.org/annotation/VSP_006309
http://togogenome.org/gene/9606:ALDH3B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2D4|||http://purl.uniprot.org/uniprot/P43353                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Splice Variant                                                                                  ^@                                                                                  Aldehyde dehydrogenase|||Aldehyde dehydrogenase family 3 member B1|||Cysteine methyl ester|||In isoform 2.|||N-acetylmethionine|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056481|||http://purl.uniprot.org/annotation/PRO_0000424193|||http://purl.uniprot.org/annotation/VSP_014040
http://togogenome.org/gene/9606:IL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35225                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Associated with increased risk for asthma development; at homozygosity associated with higher levels of serum total IgE in some allergic rhinitis patients.|||Interleukin-13|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015547|||http://purl.uniprot.org/annotation/VAR_010037
http://togogenome.org/gene/9606:EFCAB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUY7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 11|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286580|||http://purl.uniprot.org/annotation/VAR_032129|||http://purl.uniprot.org/annotation/VAR_032130|||http://purl.uniprot.org/annotation/VAR_032131|||http://purl.uniprot.org/annotation/VSP_025100|||http://purl.uniprot.org/annotation/VSP_025101|||http://purl.uniprot.org/annotation/VSP_041089|||http://purl.uniprot.org/annotation/VSP_041090|||http://purl.uniprot.org/annotation/VSP_054591|||http://purl.uniprot.org/annotation/VSP_055729
http://togogenome.org/gene/9606:ZNF382                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SR6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Mediates interaction with TRIM28|||Represses transcription|||Required for transcriptional repression activity; probably mediates sequence-specific DNA-binding|||Zinc finger protein 382                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047549|||http://purl.uniprot.org/annotation/VAR_054226|||http://purl.uniprot.org/annotation/VSP_036224|||http://purl.uniprot.org/annotation/VSP_036225
http://togogenome.org/gene/9606:HHAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5N1|||http://purl.uniprot.org/uniprot/Q5VTY9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||INTRAMEM|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Essential for palmitoylation of SHH|||Helical|||In NNMS; loss of palmitoyltransferase activity; unable to carry out SHH and DHH palmitoylation; does not affect HHAT protein levels.|||In NNMS; unknown pathological significance.|||In a lung cancer cell line.|||In a melanoma cell line; abolishes GTP-binding.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Lumenal|||No significant effect on catalytic activity. Defective HHAT-mediated palmitoyl-CoA uptake into microsomal membranes.|||Protein-cysteine N-palmitoyltransferase HHAT|||Reduced catalytic activity. Defective HHAT-mediated palmitoyl-CoA uptake into microsomal membranes.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213134|||http://purl.uniprot.org/annotation/VAR_024743|||http://purl.uniprot.org/annotation/VAR_024744|||http://purl.uniprot.org/annotation/VAR_024745|||http://purl.uniprot.org/annotation/VAR_050024|||http://purl.uniprot.org/annotation/VAR_061336|||http://purl.uniprot.org/annotation/VAR_085239|||http://purl.uniprot.org/annotation/VAR_085240|||http://purl.uniprot.org/annotation/VSP_016685|||http://purl.uniprot.org/annotation/VSP_016686|||http://purl.uniprot.org/annotation/VSP_016687|||http://purl.uniprot.org/annotation/VSP_016688|||http://purl.uniprot.org/annotation/VSP_016689|||http://purl.uniprot.org/annotation/VSP_043481|||http://purl.uniprot.org/annotation/VSP_044968
http://togogenome.org/gene/9606:SND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK49|||http://purl.uniprot.org/uniprot/Q7KZF4                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Removed|||Staphylococcal nuclease domain-containing protein 1|||TNase-like|||TNase-like 1|||TNase-like 2|||TNase-like 3|||TNase-like 4|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183180
http://togogenome.org/gene/9606:OR6C76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW16|||http://purl.uniprot.org/uniprot/A6NM76                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C76                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310868
http://togogenome.org/gene/9606:YWHAE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62258|||http://purl.uniprot.org/uniprot/V9HW98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  14-3-3|||14-3-3 protein epsilon|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform SV.|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058618|||http://purl.uniprot.org/annotation/VSP_040621
http://togogenome.org/gene/9606:P2RY14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5JUU3|||http://purl.uniprot.org/uniprot/Q15391                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070044|||http://purl.uniprot.org/annotation/VAR_035767
http://togogenome.org/gene/9606:DPY19L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In SPGF9.|||In SPGF9; unknown pathological significance.|||In isoform 2.|||Nuclear|||Perinuclear space|||Polar residues|||Probable C-mannosyltransferase DPY19L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311879|||http://purl.uniprot.org/annotation/VAR_037333|||http://purl.uniprot.org/annotation/VAR_037334|||http://purl.uniprot.org/annotation/VAR_037335|||http://purl.uniprot.org/annotation/VAR_062214|||http://purl.uniprot.org/annotation/VAR_086978|||http://purl.uniprot.org/annotation/VAR_086979|||http://purl.uniprot.org/annotation/VAR_086980|||http://purl.uniprot.org/annotation/VAR_086981|||http://purl.uniprot.org/annotation/VAR_086982|||http://purl.uniprot.org/annotation/VAR_086983|||http://purl.uniprot.org/annotation/VAR_086984|||http://purl.uniprot.org/annotation/VAR_086985|||http://purl.uniprot.org/annotation/VAR_086986|||http://purl.uniprot.org/annotation/VSP_056136
http://togogenome.org/gene/9606:UBE2J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGS0|||http://purl.uniprot.org/uniprot/Q8N2K1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Glycyl thioester intermediate|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||UBC core|||Ubiquitin-conjugating enzyme E2 J2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082596|||http://purl.uniprot.org/annotation/VSP_011572|||http://purl.uniprot.org/annotation/VSP_045219
http://togogenome.org/gene/9606:DDO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99489                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  D-aspartate oxidase|||In a breast cancer sample; somatic mutation.|||In isoform 3 and isoform 4.|||In isoform DDO-2 and isoform 4.|||Microbody targeting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162770|||http://purl.uniprot.org/annotation/VAR_014939|||http://purl.uniprot.org/annotation/VAR_014940|||http://purl.uniprot.org/annotation/VAR_014941|||http://purl.uniprot.org/annotation/VAR_036244|||http://purl.uniprot.org/annotation/VSP_001269|||http://purl.uniprot.org/annotation/VSP_037664
http://togogenome.org/gene/9606:ATXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VQP2|||http://purl.uniprot.org/uniprot/Q2M2R5|||http://purl.uniprot.org/uniprot/Q99700                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Ataxin-2|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064756|||http://purl.uniprot.org/annotation/VAR_047629|||http://purl.uniprot.org/annotation/VAR_047630|||http://purl.uniprot.org/annotation/VSP_011574|||http://purl.uniprot.org/annotation/VSP_011575|||http://purl.uniprot.org/annotation/VSP_011576|||http://purl.uniprot.org/annotation/VSP_011577|||http://purl.uniprot.org/annotation/VSP_011578|||http://purl.uniprot.org/annotation/VSP_011579|||http://purl.uniprot.org/annotation/VSP_011580|||http://purl.uniprot.org/annotation/VSP_011581|||http://purl.uniprot.org/annotation/VSP_011582|||http://purl.uniprot.org/annotation/VSP_057285|||http://purl.uniprot.org/annotation/VSP_057286|||http://purl.uniprot.org/annotation/VSP_057287
http://togogenome.org/gene/9606:KRT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08729                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Dimethylated arginine; alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Head|||IF rod|||Interaction with HPV16 E7|||Keratin, type II cytoskeletal 7|||Linker 1|||Linker 12|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063725|||http://purl.uniprot.org/annotation/VAR_016321|||http://purl.uniprot.org/annotation/VAR_060731
http://togogenome.org/gene/9606:CFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23528                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H|||Cofilin-1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by NRK|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214898
http://togogenome.org/gene/9606:PPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50897                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CLN1.|||In CLN1; juvenile onset.|||In CLN1; late infantile form.|||In CLN1; onset in adulthood; retained in the endoplasmic reticulum rather than reaching the lysosome.|||In CLN1; retained in the endoplasmic reticulum rather than reaching the lysosome.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Palmitoyl-protein thioesterase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025550|||http://purl.uniprot.org/annotation/VAR_005548|||http://purl.uniprot.org/annotation/VAR_005549|||http://purl.uniprot.org/annotation/VAR_005550|||http://purl.uniprot.org/annotation/VAR_005551|||http://purl.uniprot.org/annotation/VAR_005552|||http://purl.uniprot.org/annotation/VAR_005553|||http://purl.uniprot.org/annotation/VAR_005554|||http://purl.uniprot.org/annotation/VAR_005555|||http://purl.uniprot.org/annotation/VAR_005556|||http://purl.uniprot.org/annotation/VAR_005557|||http://purl.uniprot.org/annotation/VAR_005558|||http://purl.uniprot.org/annotation/VAR_005559|||http://purl.uniprot.org/annotation/VAR_005560|||http://purl.uniprot.org/annotation/VAR_018511|||http://purl.uniprot.org/annotation/VAR_058434|||http://purl.uniprot.org/annotation/VAR_066874|||http://purl.uniprot.org/annotation/VAR_066875|||http://purl.uniprot.org/annotation/VAR_066876|||http://purl.uniprot.org/annotation/VAR_066877|||http://purl.uniprot.org/annotation/VAR_066878|||http://purl.uniprot.org/annotation/VAR_066879|||http://purl.uniprot.org/annotation/VAR_066880|||http://purl.uniprot.org/annotation/VAR_066881|||http://purl.uniprot.org/annotation/VAR_066882|||http://purl.uniprot.org/annotation/VSP_042033
http://togogenome.org/gene/9606:AGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RZG9|||http://purl.uniprot.org/uniprot/Q9UPQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1|||Basic and acidic residues|||C4-type|||Disordered|||In a family with an autistic patient.|||In an autistic patient.|||In isoform 2.|||In isoform 3.|||Loss of GAP activity.|||Loss of GAP activity. No effect on AP-3-binding.|||N-acetylmethionine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074218|||http://purl.uniprot.org/annotation/VAR_019550|||http://purl.uniprot.org/annotation/VAR_026446|||http://purl.uniprot.org/annotation/VAR_026447|||http://purl.uniprot.org/annotation/VAR_026448|||http://purl.uniprot.org/annotation/VAR_026449|||http://purl.uniprot.org/annotation/VAR_026450|||http://purl.uniprot.org/annotation/VSP_011181|||http://purl.uniprot.org/annotation/VSP_011182|||http://purl.uniprot.org/annotation/VSP_011183
http://togogenome.org/gene/9606:MPPED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15442                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Metallophosphoesterase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053403|||http://purl.uniprot.org/annotation/VSP_056871
http://togogenome.org/gene/9606:HAUS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99871                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HAUS augmin-like complex subunit 7|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097552|||http://purl.uniprot.org/annotation/VSP_037669|||http://purl.uniprot.org/annotation/VSP_040920|||http://purl.uniprot.org/annotation/VSP_040921
http://togogenome.org/gene/9606:THOC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5S6STF9|||http://purl.uniprot.org/uniprot/Q6I9Y2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Interaction with NIF3L1|||Interaction with THOC5|||N-acetylglycine|||N6-acetyllysine|||Phosphothreonine|||Removed|||THO complex subunit 7 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310754
http://togogenome.org/gene/9606:CCAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N163                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to SIRT1.|||Basic and acidic residues|||Cell cycle and apoptosis regulator protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Interaction with MCC|||Interaction with NR1D1|||Loss of sumoylation.|||N6-acetyllysine; by KAT8|||N6-methyllysine|||No effect on sumoylation.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by ATM, ATR and CK2|||Polar residues|||Significantly increases association with SIRT1 and induces p53 acetylation and apoptosis. Increases sumoylation and the interaction of the sumoylated form with SIRT1. Promotes CCAR2-PSIA3 interaction. Decreases CCAR2-SENP1 interaction.|||Significantly reduces association with SIRT1. Decreases sumoylation and the interaction of the sumoylated form with SIRT1. Inhibits CCAR2-PSIA3 interaction. Increases CCAR2-SENP1 interaction. Down-regulation of the signals related with the epithelial-mesenchymal transition of gastric cancer cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050813|||http://purl.uniprot.org/annotation/VSP_017092
http://togogenome.org/gene/9606:SSC4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTU2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||Scavenger receptor cysteine-rich domain-containing group B protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000067535|||http://purl.uniprot.org/annotation/VAR_052063|||http://purl.uniprot.org/annotation/VSP_052695|||http://purl.uniprot.org/annotation/VSP_052696
http://togogenome.org/gene/9606:GPR137                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N19|||http://purl.uniprot.org/uniprot/Q9NQC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Integral membrane protein GPR137|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269996|||http://purl.uniprot.org/annotation/VSP_022121|||http://purl.uniprot.org/annotation/VSP_022122|||http://purl.uniprot.org/annotation/VSP_043278|||http://purl.uniprot.org/annotation/VSP_043592|||http://purl.uniprot.org/annotation/VSP_043593
http://togogenome.org/gene/9606:RAB30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15771                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||Ras-related protein Rab-30|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121230|||http://purl.uniprot.org/annotation/PRO_0000370826|||http://purl.uniprot.org/annotation/VSP_055833|||http://purl.uniprot.org/annotation/VSP_055834
http://togogenome.org/gene/9606:ID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41134                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-binding protein inhibitor ID-1|||In isoform ID-B.|||Nuclear export signal|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127236|||http://purl.uniprot.org/annotation/VAR_049544|||http://purl.uniprot.org/annotation/VSP_002108
http://togogenome.org/gene/9606:KRTCAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53RY4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Keratinocyte-associated protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226985|||http://purl.uniprot.org/annotation/VSP_017530
http://togogenome.org/gene/9606:PPIL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUA2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase-like 4|||Phosphoserine|||Phosphothreonine|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233052
http://togogenome.org/gene/9606:PPP2CA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUN1|||http://purl.uniprot.org/uniprot/P67775                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NEDLBA; almost complete loss of phosphatase activity in an in vitro assay; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; strongly decreased interaction with PP2A subunit B components PPP2R2A and PPP2R3A; increased interaction with PP2A subunit B component STRN3; no effect on interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D and PPP2R5E.|||In NEDLBA; almost complete loss of phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; decreased interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E and PPP2R3A; no effect on interaction with PP2A subunit B component PPP2R2A.|||In NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on C-terminal methylation; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; no effect on interaction with PP2A subunit B components.|||In NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; decreased interaction with PP2A subunit B component PPP2R5D; increased interaction with PP2A subunit B component STRN3; no effect on interaction with other PP2A subunit B components.|||In NEDLBA; decreased phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; increased interaction with PP2A subunit B component STRN3; no effect on interaction with other PP2A subunit B components.|||In NEDLBA; increased phosphatase activity in an in vitro assay; no effect on C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D and PPP2R5E; no effect on interaction with PP2A subunit B components PPP2R2A and PPP2R3A.|||In NEDLBA; loss of phosphatase activity in an in vitro assay; complete loss of interaction with PP2A subunit APPP2R1A/PPP2R1B; interacts with alpha4/IGBP1; loss of interaction with PP2A subunit B components.|||In NEDLBA; loss of phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B component PPP2R2A; decreased interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5E, PPP2R3A and STRN3.|||In NEDLBA; may be expressed at very low levels, if any.|||In NEDLBA; no effect on phosphatase activity in an in vitro assay; no effect on the interaction with PP2A subunit APPP2R1A/PPP2R1B; no effect on interaction with PP2A subunit B components.|||In NEDLBA; severe decrease in phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; decreased interaction with PP2A subunit APPP2R1A/PPP2R1B; loss of interaction with PP2A subunit B components PPP2R2A, PPP2R5A, PPP2R5B, PPP2R5E, PPP2R3A and STRN3; decreased interaction with PP2A subunit B components PPP2R5C and PPP2R5D.|||In NEDLBA; unknown pathological significance.|||In isoform 2.|||Leucine methyl ester|||Loss of binding to PP2AB-alpha regulatory subunit.|||Loss of phosphatase activity.|||Phosphotyrosine|||Proton donor|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058839|||http://purl.uniprot.org/annotation/VAR_051735|||http://purl.uniprot.org/annotation/VAR_082064|||http://purl.uniprot.org/annotation/VAR_082065|||http://purl.uniprot.org/annotation/VAR_082066|||http://purl.uniprot.org/annotation/VAR_082067|||http://purl.uniprot.org/annotation/VAR_082068|||http://purl.uniprot.org/annotation/VAR_082069|||http://purl.uniprot.org/annotation/VAR_082070|||http://purl.uniprot.org/annotation/VAR_082071|||http://purl.uniprot.org/annotation/VAR_082072|||http://purl.uniprot.org/annotation/VAR_082073|||http://purl.uniprot.org/annotation/VAR_082074|||http://purl.uniprot.org/annotation/VAR_082075|||http://purl.uniprot.org/annotation/VSP_044320
http://togogenome.org/gene/9606:RUNDC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59EK9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Interaction with RAP2A|||Phosphoserine|||Phosphothreonine|||RUN|||RUN domain-containing protein 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324155|||http://purl.uniprot.org/annotation/VSP_032153|||http://purl.uniprot.org/annotation/VSP_032154|||http://purl.uniprot.org/annotation/VSP_032155|||http://purl.uniprot.org/annotation/VSP_032156
http://togogenome.org/gene/9606:DYM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTS9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Does not affect protein localization to Golgi apparatus. Prevents myristoylation in vitro.|||Dymeclin|||In DMC; results in protein mis-localization and aggregation.|||In SMC1.|||In SMC1; does not affect protein localization.|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086883|||http://purl.uniprot.org/annotation/VAR_022740|||http://purl.uniprot.org/annotation/VAR_054499|||http://purl.uniprot.org/annotation/VAR_065293|||http://purl.uniprot.org/annotation/VSP_036442|||http://purl.uniprot.org/annotation/VSP_036443
http://togogenome.org/gene/9606:ZNF22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17026                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Zinc finger protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047348|||http://purl.uniprot.org/annotation/VAR_035566|||http://purl.uniprot.org/annotation/VAR_052747
http://togogenome.org/gene/9606:OR8J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGP2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150669|||http://purl.uniprot.org/annotation/VAR_034268|||http://purl.uniprot.org/annotation/VAR_034269|||http://purl.uniprot.org/annotation/VAR_060013
http://togogenome.org/gene/9606:LIPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y3S0|||http://purl.uniprot.org/uniprot/Q5D1Q2|||http://purl.uniprot.org/uniprot/Q6XZB0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Lipase|||Lipase member I|||N-linked (GlcNAc...) asparagine|||No activity.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042779|||http://purl.uniprot.org/annotation/VAR_023760|||http://purl.uniprot.org/annotation/VAR_023761|||http://purl.uniprot.org/annotation/VAR_023762|||http://purl.uniprot.org/annotation/VAR_023763|||http://purl.uniprot.org/annotation/VSP_016090|||http://purl.uniprot.org/annotation/VSP_053896|||http://purl.uniprot.org/annotation/VSP_053897|||http://purl.uniprot.org/annotation/VSP_053898|||http://purl.uniprot.org/annotation/VSP_053899|||http://purl.uniprot.org/annotation/VSP_053900|||http://purl.uniprot.org/annotation/VSP_053901|||http://purl.uniprot.org/annotation/VSP_053902|||http://purl.uniprot.org/annotation/VSP_053903
http://togogenome.org/gene/9606:FBXO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNA0|||http://purl.uniprot.org/uniprot/D6RAJ6|||http://purl.uniprot.org/uniprot/Q9UKT5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization.|||Abolishes interaction with TERF1.|||F-box|||F-box only protein 4|||In esophagus cancer sample.|||In esophagus cancer sample; impairs homodimerization and reduces ubiquitin ligase activity.|||In esophagus cancer samples.|||In esophagus cancer samples; impairs interaction with SKP1.|||In isoform 2.|||No effect on homodimerization.|||Phosphoserine|||Reduces homodimerization.|||Reduces homodimerization. Reduces ubiquitination of CCND1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119879|||http://purl.uniprot.org/annotation/VAR_063500|||http://purl.uniprot.org/annotation/VAR_063501|||http://purl.uniprot.org/annotation/VAR_063502|||http://purl.uniprot.org/annotation/VAR_063503|||http://purl.uniprot.org/annotation/VAR_063504|||http://purl.uniprot.org/annotation/VSP_012977|||http://purl.uniprot.org/annotation/VSP_012978
http://togogenome.org/gene/9606:FAM171B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P995                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein FAM171B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287148|||http://purl.uniprot.org/annotation/VAR_032269|||http://purl.uniprot.org/annotation/VSP_040122|||http://purl.uniprot.org/annotation/VSP_040123
http://togogenome.org/gene/9606:PFKFB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60825                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2|||Constitutively active mutant that cannot be phosphorylated and further activated by AMPK.|||Disordered|||Fructose-2,6-bisphosphatase|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by BRAF|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179964|||http://purl.uniprot.org/annotation/VSP_004675
http://togogenome.org/gene/9606:PLSCR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRY6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with PDCD6; when associated with A-49.|||Disordered|||Fails to enhance apoptosis mediated by PRKCD activators.|||Helical|||Mitochondrial intermembrane|||No effect on the interaction with PDCD6.|||PPxY motif|||Phospholipid scramblase 3|||Phosphothreonine; by PKC/PRKCD|||Pro residues|||Proline-rich domain (PRD)|||Promotes apoptosis, more potent in lipid flippase activity.|||Reduced phospholipid scramblase activity. Reduced calcium and magnesium-binding. Diminished apoptotic responsiveness. Defective mitochondrial structure and oxidative function. Reduced binding affinity for Pb(2+) and Hg(2+) ions. Increased cardiolipin biosynthesis from glycerol and decreased cardiolipin resynthesis from linoleic acid.|||Reduces interaction with PDCD6.|||Reduces interaction with PDCD6. Abolishes interaction with PDCD6; when associated with A-52.|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100789|||http://purl.uniprot.org/annotation/VAR_015568
http://togogenome.org/gene/9606:MINPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNW1                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Greatly diminishes phosphatase activity.|||In NMTC2.|||In NMTC2; somatic mutation.|||In PCH16; loss of enzymatic activity.|||In PCH16; unknown pathological significance.|||In PCH16; unknown pathological significance; contary to wild-type, does not rescue normal growth in a MINPP1 knockout cell line.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Multiple inositol polyphosphate phosphatase 1|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Strong reduction of 2,3-bisphosphoglycerate 3-phosphatase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019582|||http://purl.uniprot.org/annotation/VAR_022836|||http://purl.uniprot.org/annotation/VAR_022837|||http://purl.uniprot.org/annotation/VAR_086289|||http://purl.uniprot.org/annotation/VAR_086290|||http://purl.uniprot.org/annotation/VAR_086291|||http://purl.uniprot.org/annotation/VAR_086292|||http://purl.uniprot.org/annotation/VAR_086293|||http://purl.uniprot.org/annotation/VAR_086294|||http://purl.uniprot.org/annotation/VAR_086295|||http://purl.uniprot.org/annotation/VSP_014552|||http://purl.uniprot.org/annotation/VSP_014553|||http://purl.uniprot.org/annotation/VSP_014554|||http://purl.uniprot.org/annotation/VSP_014555|||http://purl.uniprot.org/annotation/VSP_044569
http://togogenome.org/gene/9606:TF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJA6|||http://purl.uniprot.org/uniprot/P02787|||http://purl.uniprot.org/uniprot/Q06AH7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Dimethylated arginine|||In ATRAF.|||In allele TF*B2.|||In allele TF*BV.|||In allele TF*C2.|||In allele TF*C3; associated with a reduction in total iron binding capacity; risk factor for iron deficiency anemia in menstruating white women.|||In allele TF*CHI.|||In allele TF*D1.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine; atypical; partial|||O-linked (GalNAc...) serine|||Phosphoserine; by FAM20C|||Serotransferrin|||Transferrin-like|||Transferrin-like 1|||Transferrin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000073|||http://purl.uniprot.org/annotation/CAR_000074|||http://purl.uniprot.org/annotation/CAR_000075|||http://purl.uniprot.org/annotation/PRO_0000035715|||http://purl.uniprot.org/annotation/PRO_5004165272|||http://purl.uniprot.org/annotation/VAR_007544|||http://purl.uniprot.org/annotation/VAR_007545|||http://purl.uniprot.org/annotation/VAR_011997|||http://purl.uniprot.org/annotation/VAR_011998|||http://purl.uniprot.org/annotation/VAR_011999|||http://purl.uniprot.org/annotation/VAR_012000|||http://purl.uniprot.org/annotation/VAR_012001|||http://purl.uniprot.org/annotation/VAR_012997|||http://purl.uniprot.org/annotation/VAR_012998|||http://purl.uniprot.org/annotation/VAR_012999|||http://purl.uniprot.org/annotation/VAR_029280|||http://purl.uniprot.org/annotation/VAR_034569|||http://purl.uniprot.org/annotation/VAR_034570|||http://purl.uniprot.org/annotation/VAR_034571|||http://purl.uniprot.org/annotation/VAR_038810|||http://purl.uniprot.org/annotation/VAR_058199
http://togogenome.org/gene/9606:CPLX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6F4|||http://purl.uniprot.org/uniprot/Q8WVH0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Complexin-3|||Cysteine methyl ester|||Disordered|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239272|||http://purl.uniprot.org/annotation/PRO_0000240233
http://togogenome.org/gene/9606:TTC9C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5M4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 9C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294465|||http://purl.uniprot.org/annotation/VSP_056610|||http://purl.uniprot.org/annotation/VSP_056611
http://togogenome.org/gene/9606:ANXA2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Annexin-2 receptor|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295727|||http://purl.uniprot.org/annotation/VAR_033348|||http://purl.uniprot.org/annotation/VAR_033349
http://togogenome.org/gene/9606:MLST8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MTOR.|||Does not affect ubiquitination by the SCF(FBXW7) complex.|||Impairs interaction with MTOR.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by CDK1|||Reduced ubiquitination by the SCF(FBXW7) complex.|||Target of rapamycin complex subunit LST8|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326499|||http://purl.uniprot.org/annotation/VSP_032665|||http://purl.uniprot.org/annotation/VSP_032666|||http://purl.uniprot.org/annotation/VSP_032667|||http://purl.uniprot.org/annotation/VSP_032668|||http://purl.uniprot.org/annotation/VSP_047368
http://togogenome.org/gene/9606:H2AC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FTV9|||http://purl.uniprot.org/uniprot/P0C0S8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055235
http://togogenome.org/gene/9606:SULT6B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG03|||http://purl.uniprot.org/uniprot/Q6IMI4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Proton acceptor|||Sulfotransferase|||Sulfotransferase 6B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085171|||http://purl.uniprot.org/annotation/VAR_052522|||http://purl.uniprot.org/annotation/VAR_052523|||http://purl.uniprot.org/annotation/VAR_052524|||http://purl.uniprot.org/annotation/VAR_052525|||http://purl.uniprot.org/annotation/VAR_052526|||http://purl.uniprot.org/annotation/VAR_052527|||http://purl.uniprot.org/annotation/VAR_059853|||http://purl.uniprot.org/annotation/VSP_013111
http://togogenome.org/gene/9606:DDA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW61                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  DET1- and DDB1-associated protein 1|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310270
http://togogenome.org/gene/9606:CSRNP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQ49|||http://purl.uniprot.org/uniprot/Q8WYN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Cysteine/serine-rich nuclear protein 3|||Cysteine/serine-rich nuclear protein N-terminal|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114788|||http://purl.uniprot.org/annotation/VAR_035993|||http://purl.uniprot.org/annotation/VSP_034258|||http://purl.uniprot.org/annotation/VSP_034259
http://togogenome.org/gene/9606:SERINC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13530                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Serine incorporator 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218970|||http://purl.uniprot.org/annotation/VAR_014315|||http://purl.uniprot.org/annotation/VSP_056833
http://togogenome.org/gene/9606:IGFBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24592                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 6|||O-linked (HexNAc...) serine|||O-linked (HexNAc...) threonine|||Polar residues|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014389|||http://purl.uniprot.org/annotation/VAR_011907|||http://purl.uniprot.org/annotation/VAR_018932|||http://purl.uniprot.org/annotation/VAR_018933|||http://purl.uniprot.org/annotation/VAR_049565
http://togogenome.org/gene/9606:RCVRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35243                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH)|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interaction with GRK1|||Interchain, redox-active|||N-myristoyl glycine|||Recoverin|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073759
http://togogenome.org/gene/9606:NKX3-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78367                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Nkx-3.2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048947
http://togogenome.org/gene/9606:INVS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M1I4|||http://purl.uniprot.org/uniprot/Q9Y283                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3-hydroxyasparagine|||ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||D-box 1|||D-box 2|||Disordered|||IQ 1|||IQ 2|||In NPHP2.|||In NPHP2; impairs ability to target DVL1 for degradation.|||In isoform 2.|||In isoform 3.|||Inversin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067016|||http://purl.uniprot.org/annotation/VAR_022822|||http://purl.uniprot.org/annotation/VAR_022823|||http://purl.uniprot.org/annotation/VAR_044119|||http://purl.uniprot.org/annotation/VAR_044120|||http://purl.uniprot.org/annotation/VSP_014495|||http://purl.uniprot.org/annotation/VSP_014496|||http://purl.uniprot.org/annotation/VSP_014497
http://togogenome.org/gene/9606:SHISA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWI4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Protein shisa-2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022615
http://togogenome.org/gene/9606:KIF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG5|||http://purl.uniprot.org/uniprot/Q8N4N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Kinesin motor|||Kinesin-like protein KIF2B|||Phosphoserine; by PLK1|||Phosphothreonine; by PLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253715|||http://purl.uniprot.org/annotation/VAR_028717|||http://purl.uniprot.org/annotation/VAR_028718|||http://purl.uniprot.org/annotation/VAR_028719|||http://purl.uniprot.org/annotation/VAR_028720|||http://purl.uniprot.org/annotation/VAR_061279
http://togogenome.org/gene/9606:SNAPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13487                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pro residues|||snRNA-activating protein complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072020|||http://purl.uniprot.org/annotation/VAR_011806
http://togogenome.org/gene/9606:AHI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T7Z8|||http://purl.uniprot.org/uniprot/Q8N157|||http://purl.uniprot.org/uniprot/Q8NER0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS3.|||In JBTS3; alters interaction with HAP1 and NPHP1; loss of NPHP1AHI1(2):NPHP1(2) tetramers; loss of localization at cilium basal body and cell-cell junctions; loss of positive modulation of classical Wnt signaling; decreased interaction with CTNNB1.|||In JBTS3; loss of localization at cilium basal body and cell-cell junctions.|||In JBTS3; loss of localization at the primary cilium; loss of positive modulation of classical Wnt signaling; no effect on interaction with CTNNB1.|||In isoform 2.|||In isoform 3.|||Interaction with HAP1|||Jouberin|||Phosphoserine|||Polar residues|||SH3|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050838|||http://purl.uniprot.org/annotation/VAR_023391|||http://purl.uniprot.org/annotation/VAR_037892|||http://purl.uniprot.org/annotation/VAR_037893|||http://purl.uniprot.org/annotation/VAR_037894|||http://purl.uniprot.org/annotation/VAR_037895|||http://purl.uniprot.org/annotation/VAR_037896|||http://purl.uniprot.org/annotation/VAR_037897|||http://purl.uniprot.org/annotation/VAR_037898|||http://purl.uniprot.org/annotation/VAR_037899|||http://purl.uniprot.org/annotation/VAR_037900|||http://purl.uniprot.org/annotation/VAR_037901|||http://purl.uniprot.org/annotation/VAR_068171|||http://purl.uniprot.org/annotation/VAR_071194|||http://purl.uniprot.org/annotation/VAR_076820|||http://purl.uniprot.org/annotation/VAR_076821|||http://purl.uniprot.org/annotation/VAR_076822|||http://purl.uniprot.org/annotation/VAR_080417|||http://purl.uniprot.org/annotation/VSP_015353|||http://purl.uniprot.org/annotation/VSP_015354|||http://purl.uniprot.org/annotation/VSP_015355|||http://purl.uniprot.org/annotation/VSP_015356
http://togogenome.org/gene/9606:SLC6A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8J1|||http://purl.uniprot.org/uniprot/Q9UN76                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214795
http://togogenome.org/gene/9606:EMSY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z589                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with CBX1.|||Abolishes interaction with ZMYND11.|||BRCA2-interacting transcriptional repressor EMSY|||Disordered|||ENT|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 7.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 6.|||Interaction with BRCA2|||Interaction with ZMYND11|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086968|||http://purl.uniprot.org/annotation/VSP_010431|||http://purl.uniprot.org/annotation/VSP_020774|||http://purl.uniprot.org/annotation/VSP_020775|||http://purl.uniprot.org/annotation/VSP_054139|||http://purl.uniprot.org/annotation/VSP_054140|||http://purl.uniprot.org/annotation/VSP_054141|||http://purl.uniprot.org/annotation/VSP_054142|||http://purl.uniprot.org/annotation/VSP_054143
http://togogenome.org/gene/9606:GPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPH9|||http://purl.uniprot.org/uniprot/P35052                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GPI-anchor amidated serine|||Glypican-1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on protein yield. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-79.|||O-linked (Xyl...) (heparan sulfate) serine|||Protein yield reduced by half. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-116.|||Removed in mature form|||Secreted glypican-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012295|||http://purl.uniprot.org/annotation/PRO_0000012296|||http://purl.uniprot.org/annotation/PRO_0000333837|||http://purl.uniprot.org/annotation/PRO_5017329104|||http://purl.uniprot.org/annotation/VAR_033977|||http://purl.uniprot.org/annotation/VAR_036044|||http://purl.uniprot.org/annotation/VSP_055225|||http://purl.uniprot.org/annotation/VSP_055226|||http://purl.uniprot.org/annotation/VSP_055227
http://togogenome.org/gene/9606:FGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08830                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Fibrinogen C-terminal|||Fibrinogen-like protein 1|||Interchain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009105|||http://purl.uniprot.org/annotation/VAR_024002|||http://purl.uniprot.org/annotation/VAR_024003|||http://purl.uniprot.org/annotation/VAR_024004|||http://purl.uniprot.org/annotation/VAR_024005|||http://purl.uniprot.org/annotation/VAR_024006|||http://purl.uniprot.org/annotation/VAR_024007|||http://purl.uniprot.org/annotation/VAR_049067|||http://purl.uniprot.org/annotation/VAR_049068
http://togogenome.org/gene/9606:PRAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases homodimerization.|||Decreases homodimerization. Abolished interaction with PEAK1. Decreases cell migration.|||Decreases homodimerization. Abolished interaction with PEAK1. No effect on cell migration.|||Decreases homodimerization. Decreases interaction with PEAK1.|||Disordered|||Inactive tyrosine-protein kinase PRAG1|||No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1.|||No effect on homodimerization. Decreases oligomerization. Decreases interaction with PEAK1. No effect on cell migration.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Required for homodimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263008|||http://purl.uniprot.org/annotation/VAR_041803|||http://purl.uniprot.org/annotation/VAR_041804|||http://purl.uniprot.org/annotation/VAR_041805|||http://purl.uniprot.org/annotation/VAR_041806|||http://purl.uniprot.org/annotation/VAR_041807|||http://purl.uniprot.org/annotation/VAR_041808|||http://purl.uniprot.org/annotation/VAR_041809|||http://purl.uniprot.org/annotation/VAR_041810|||http://purl.uniprot.org/annotation/VAR_041811|||http://purl.uniprot.org/annotation/VAR_041812|||http://purl.uniprot.org/annotation/VAR_041813|||http://purl.uniprot.org/annotation/VAR_041814|||http://purl.uniprot.org/annotation/VAR_041815|||http://purl.uniprot.org/annotation/VAR_041816
http://togogenome.org/gene/9606:MTMR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYA4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||Myotubularin phosphatase|||Myotubularin-related protein 4|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304809|||http://purl.uniprot.org/annotation/VAR_035110|||http://purl.uniprot.org/annotation/VAR_035111|||http://purl.uniprot.org/annotation/VAR_035112
http://togogenome.org/gene/9606:H2BC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4S9|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A/H2B/H3|||Histone H2B type 1-C/E/F/G/I|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:TTLL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT98                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  40% decreased polyglutamylase activity.|||45% decreased binding to microtubules. Decreased polyglutamylase activity. 76% decreased binding to microtubules; when associated with 425-E--E-427.|||69% decreased polyglutamylase activity.|||70% decreased polyglutamylase activity.|||76% decreased binding to microtubules; when associated with 385-E--E-393.|||Basic and acidic residues|||Binds negatively charged residues of beta-tubulin C-terminal tails|||Decreased polyglutamylase activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of polyglutamylase activity.|||Nearly abolished polyglutamylase activity.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL7|||c-MTBD region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212444|||http://purl.uniprot.org/annotation/VSP_015199|||http://purl.uniprot.org/annotation/VSP_015200|||http://purl.uniprot.org/annotation/VSP_015201|||http://purl.uniprot.org/annotation/VSP_015202
http://togogenome.org/gene/9606:PCGF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polycomb group RING finger protein 5|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277868|||http://purl.uniprot.org/annotation/VSP_023118|||http://purl.uniprot.org/annotation/VSP_023119
http://togogenome.org/gene/9606:FRMPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SYB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with GPSM2.|||Disordered|||FERM|||FERM and PDZ domain-containing protein 1|||Important for interaction with GPSM2|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||PDZ|||Polar residues|||Strongly reduces GPSM2 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306805|||http://purl.uniprot.org/annotation/VAR_035306|||http://purl.uniprot.org/annotation/VAR_035307|||http://purl.uniprot.org/annotation/VAR_035308|||http://purl.uniprot.org/annotation/VAR_035309|||http://purl.uniprot.org/annotation/VAR_035310|||http://purl.uniprot.org/annotation/VAR_035311|||http://purl.uniprot.org/annotation/VAR_035445|||http://purl.uniprot.org/annotation/VSP_056060|||http://purl.uniprot.org/annotation/VSP_056061|||http://purl.uniprot.org/annotation/VSP_056062|||http://purl.uniprot.org/annotation/VSP_056063|||http://purl.uniprot.org/annotation/VSP_056064
http://togogenome.org/gene/9606:PRR5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNU3|||http://purl.uniprot.org/uniprot/Q6MZQ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Proline-rich protein 5-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332709|||http://purl.uniprot.org/annotation/VAR_043006|||http://purl.uniprot.org/annotation/VAR_043007|||http://purl.uniprot.org/annotation/VSP_033375|||http://purl.uniprot.org/annotation/VSP_033376|||http://purl.uniprot.org/annotation/VSP_033377|||http://purl.uniprot.org/annotation/VSP_033378|||http://purl.uniprot.org/annotation/VSP_033379|||http://purl.uniprot.org/annotation/VSP_044981|||http://purl.uniprot.org/annotation/VSP_044982
http://togogenome.org/gene/9606:ZNF592                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 12; atypical|||C2H2-type 13|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5; atypical|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in a patient with clinical features of Galloway-Mowat syndrome; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger protein 592                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047682|||http://purl.uniprot.org/annotation/VAR_047033|||http://purl.uniprot.org/annotation/VAR_064583
http://togogenome.org/gene/9606:REC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95072                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Meiotic recombination protein REC8 homolog|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097878|||http://purl.uniprot.org/annotation/VAR_051722|||http://purl.uniprot.org/annotation/VAR_051723|||http://purl.uniprot.org/annotation/VAR_058128|||http://purl.uniprot.org/annotation/VSP_037649
http://togogenome.org/gene/9606:NTSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30989                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes palmitoylation; when associated with S-381.|||Abolishes palmitoylation; when associated with S-383.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neurotensin binding|||Neurotensin receptor type 1|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069946|||http://purl.uniprot.org/annotation/VAR_020071|||http://purl.uniprot.org/annotation/VAR_049424|||http://purl.uniprot.org/annotation/VAR_059328
http://togogenome.org/gene/9606:CSNK1A1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N752                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Casein kinase I isoform alpha-like|||Disordered|||In a colorectal cancer sample; somatic mutation.|||N6-acetyllysine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192830|||http://purl.uniprot.org/annotation/VAR_034047|||http://purl.uniprot.org/annotation/VAR_036450|||http://purl.uniprot.org/annotation/VAR_042074|||http://purl.uniprot.org/annotation/VAR_042075|||http://purl.uniprot.org/annotation/VAR_042076|||http://purl.uniprot.org/annotation/VAR_042077|||http://purl.uniprot.org/annotation/VAR_042078|||http://purl.uniprot.org/annotation/VAR_042079|||http://purl.uniprot.org/annotation/VAR_042080
http://togogenome.org/gene/9606:CEP164                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 164 kDa|||Disordered|||In NPHP15.|||In isoform 2.|||Interaction with ATRIP|||Phosphoserine|||Phosphoserine; by ATR and ATM|||Polar residues|||Prevents phosphorylation.|||Pro residues|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312494|||http://purl.uniprot.org/annotation/VAR_037511|||http://purl.uniprot.org/annotation/VAR_037512|||http://purl.uniprot.org/annotation/VAR_037513|||http://purl.uniprot.org/annotation/VAR_068503|||http://purl.uniprot.org/annotation/VAR_068504|||http://purl.uniprot.org/annotation/VSP_029843|||http://purl.uniprot.org/annotation/VSP_029844
http://togogenome.org/gene/9606:TMEM147                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVK8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BOS complex subunit TMEM147|||Cytoplasmic|||Helical|||In NEDFLPH.|||In NEDFLPH; decreased stability.|||In NEDFLPH; impaired endoplasmic reticulum organization.|||In NEDFLPH; slightly decreased stability; impaired endoplasmic reticulum organization.|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271701|||http://purl.uniprot.org/annotation/VAR_051429|||http://purl.uniprot.org/annotation/VAR_087576|||http://purl.uniprot.org/annotation/VAR_087577|||http://purl.uniprot.org/annotation/VAR_087578|||http://purl.uniprot.org/annotation/VAR_087579|||http://purl.uniprot.org/annotation/VAR_087580|||http://purl.uniprot.org/annotation/VAR_087581|||http://purl.uniprot.org/annotation/VSP_047210
http://togogenome.org/gene/9606:CWF19L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5E9|||http://purl.uniprot.org/uniprot/Q69YN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CWF19-like protein 1|||Cwf19-like C-terminal|||Cwf19-like protein C-terminal|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315641|||http://purl.uniprot.org/annotation/VAR_038264|||http://purl.uniprot.org/annotation/VAR_038265|||http://purl.uniprot.org/annotation/VAR_038266|||http://purl.uniprot.org/annotation/VAR_038267|||http://purl.uniprot.org/annotation/VSP_030586|||http://purl.uniprot.org/annotation/VSP_030587|||http://purl.uniprot.org/annotation/VSP_030588
http://togogenome.org/gene/9606:NUP153                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49790                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Interacts with HIV-1 capsid protein p24 (CA)|||1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||29 X 2 AA repeats of F-G|||3|||4|||5|||6|||7|||8|||9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Nuclear pore complex protein Nup153|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||RanBP2-type 4|||Reduces binding to HIV-1 capsid protein p24 (CA).|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204842|||http://purl.uniprot.org/annotation/VAR_046554|||http://purl.uniprot.org/annotation/VAR_046555|||http://purl.uniprot.org/annotation/VAR_046556|||http://purl.uniprot.org/annotation/VAR_046557|||http://purl.uniprot.org/annotation/VAR_046558|||http://purl.uniprot.org/annotation/VAR_046559|||http://purl.uniprot.org/annotation/VAR_070841|||http://purl.uniprot.org/annotation/VSP_054265|||http://purl.uniprot.org/annotation/VSP_055134
http://togogenome.org/gene/9606:KDM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3VM53|||http://purl.uniprot.org/uniprot/I3VM54|||http://purl.uniprot.org/uniprot/Q9Y2K7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosylarginine|||Abolishes association with centromeric heterochromatin; when associated with A-571 and A-574. Loss of its ability to repress the transcriptional activator activity of the CLOCK-BMAL1 heterodimer; when associated with A-574.|||Abolishes association with centromeric heterochromatin; when associated with A-571 and A-577. Loss of its ability to repress the transcriptional activator activity of the CLOCK-BMAL1 heterodimer; when associated with A-577.|||Abolishes association with centromeric heterochromatin; when associated with A-574 and A-577.|||Abolishes histone demethylase activity. No loss of its ability to repress the transcriptional activator activity of the CLOCK-BMAL1 heterodimer.|||Abolishes lysine-specific histone demethylase activity.|||Acidic residues|||Basic and acidic residues|||CXXC-type|||Disordered|||F-box|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||JmjC|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Lysine-specific demethylase 2A|||No loss of its ability to repress the transcriptional activator activity of the CLOCK-BMAL1 heterodimer; when associated with A-620.|||No loss of its ability to repress the transcriptional activator activity of the CLOCK-BMAL1 heterodimer; when associated with A-623.|||PHD-type|||Phosphoserine|||Phosphothreonine|||Reduced interaction with UBB.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119855|||http://purl.uniprot.org/annotation/VSP_017468|||http://purl.uniprot.org/annotation/VSP_017469|||http://purl.uniprot.org/annotation/VSP_017470|||http://purl.uniprot.org/annotation/VSP_046938|||http://purl.uniprot.org/annotation/VSP_046939|||http://purl.uniprot.org/annotation/VSP_046940
http://togogenome.org/gene/9606:MPHOSPH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99550                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased ubiquitination and increased protein stability.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with CEP97|||Interaction with KIF24|||Loss of phosphorylation and localization at distal ends of the mother centriole. Significant decrease in ubiquitination; when associated with A-788.|||M-phase phosphoprotein 9|||Phosphoserine|||Phosphoserine; by TTBK2|||Polar residues|||Reduced phosphorylation. Significant decrease in ubiquitination; when associated with A-781.|||Required for its centrosomal localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096557|||http://purl.uniprot.org/annotation/VAR_047643|||http://purl.uniprot.org/annotation/VAR_047644|||http://purl.uniprot.org/annotation/VSP_035838
http://togogenome.org/gene/9606:ESCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FWF5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHH-type|||Decreased thermal stability. Strongly decreased enzyme activity.|||Decreased thermal stability.Strongly decreased enzyme activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Loss of autoacetylation.|||N-acetyltransferase ESCO1|||Nearly abolishes autoacetylation.|||No effect on association with chromosomes.|||Phosphoserine|||Polar residues|||Reduced autoacetylation.|||Significant reduction in autoacetylation.|||Strongly decreased enzyme activity.|||Strongly decreased enzyme activity. No effect on thermal stability.|||Strongly reduced autoacetylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074539|||http://purl.uniprot.org/annotation/VAR_022648|||http://purl.uniprot.org/annotation/VAR_048167|||http://purl.uniprot.org/annotation/VSP_014029|||http://purl.uniprot.org/annotation/VSP_014030
http://togogenome.org/gene/9606:MAT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP5|||http://purl.uniprot.org/uniprot/P31153                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Flexible loop|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||S-adenosylmethionine synthase isoform type-2|||S-adenosylmethionine synthetase C-terminal|||S-adenosylmethionine synthetase N-terminal|||S-adenosylmethionine synthetase central|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174435|||http://purl.uniprot.org/annotation/VSP_056186|||http://purl.uniprot.org/annotation/VSP_056187
http://togogenome.org/gene/9606:SREK1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9Q2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CCHC-type|||Disordered|||Phosphoserine|||Phosphothreonine|||Protein SREK1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311922
http://togogenome.org/gene/9606:FBXW5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969U6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  D-box|||F-box|||F-box/WD repeat-containing protein 5|||Impairs phosphorylation by PLK4 and enhances ubiquitination of SASS6.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by PLK4|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050992|||http://purl.uniprot.org/annotation/VAR_053393|||http://purl.uniprot.org/annotation/VSP_009479|||http://purl.uniprot.org/annotation/VSP_009480
http://togogenome.org/gene/9606:AP4E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM48|||http://purl.uniprot.org/uniprot/Q9UPM8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-4 complex subunit epsilon-1|||Clathrin/coatomer adaptor adaptin-like N-terminal|||Found in deaf patients; unknown pathological significance.|||In STUT1; slightly decreased assembly of the AP-4 complex.|||In STUT1; unknown pathological significance.|||In isoform 2.|||Interaction with TEPSIN|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193769|||http://purl.uniprot.org/annotation/VAR_031621|||http://purl.uniprot.org/annotation/VAR_076619|||http://purl.uniprot.org/annotation/VAR_076620|||http://purl.uniprot.org/annotation/VAR_076621|||http://purl.uniprot.org/annotation/VAR_076622|||http://purl.uniprot.org/annotation/VAR_076623|||http://purl.uniprot.org/annotation/VAR_076624|||http://purl.uniprot.org/annotation/VAR_076625|||http://purl.uniprot.org/annotation/VAR_076626|||http://purl.uniprot.org/annotation/VAR_076627|||http://purl.uniprot.org/annotation/VAR_076628|||http://purl.uniprot.org/annotation/VAR_076629|||http://purl.uniprot.org/annotation/VAR_076630|||http://purl.uniprot.org/annotation/VAR_076631|||http://purl.uniprot.org/annotation/VAR_076632|||http://purl.uniprot.org/annotation/VAR_076633|||http://purl.uniprot.org/annotation/VAR_076634|||http://purl.uniprot.org/annotation/VAR_076635|||http://purl.uniprot.org/annotation/VAR_076636|||http://purl.uniprot.org/annotation/VAR_076637|||http://purl.uniprot.org/annotation/VAR_076638|||http://purl.uniprot.org/annotation/VAR_076639|||http://purl.uniprot.org/annotation/VAR_076640|||http://purl.uniprot.org/annotation/VAR_076641|||http://purl.uniprot.org/annotation/VAR_079485|||http://purl.uniprot.org/annotation/VSP_046009
http://togogenome.org/gene/9606:SKIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12757                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 5.|||In isoform SNOA.|||In isoform SNOI.|||In isoform SNON2.|||Phosphoserine|||Polar residues|||Ski-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129387|||http://purl.uniprot.org/annotation/VAR_011677|||http://purl.uniprot.org/annotation/VSP_004392|||http://purl.uniprot.org/annotation/VSP_004393|||http://purl.uniprot.org/annotation/VSP_004394|||http://purl.uniprot.org/annotation/VSP_004395|||http://purl.uniprot.org/annotation/VSP_004396|||http://purl.uniprot.org/annotation/VSP_040099
http://togogenome.org/gene/9606:NICN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSH3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nicolin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096814|||http://purl.uniprot.org/annotation/VSP_011420
http://togogenome.org/gene/9606:PCMTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV79                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AdoMet binding motif|||BC-box|||CUL-box|||Disordered|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Protein-L-isoaspartate O-methyltransferase domain-containing protein 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111927|||http://purl.uniprot.org/annotation/VSP_008546|||http://purl.uniprot.org/annotation/VSP_008547|||http://purl.uniprot.org/annotation/VSP_008548
http://togogenome.org/gene/9606:LTBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14767                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-terminal domain|||Cell attachment site|||Disordered|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 20; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Gain-of-function. Forms a complex with TGFB1.|||Heparin-binding|||In WMS3.|||Latent-transforming growth factor beta-binding protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TB 1|||TB 2|||TB 3|||TB 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007643|||http://purl.uniprot.org/annotation/VAR_055752|||http://purl.uniprot.org/annotation/VAR_059270|||http://purl.uniprot.org/annotation/VAR_060337|||http://purl.uniprot.org/annotation/VAR_068647
http://togogenome.org/gene/9606:RHOJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4E5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Causes constitutive activation.|||Cysteine methyl ester|||Does not affect localization to the plasma membrane.|||Dominant negative mutant.|||Effector region|||Impaired localization to the plasma membrane.|||In isoform 2.|||Removed in mature form|||Rho-related GTP-binding protein RhoJ|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198869|||http://purl.uniprot.org/annotation/PRO_0000281220|||http://purl.uniprot.org/annotation/VSP_007231
http://togogenome.org/gene/9606:RABGGTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53611                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Geranylgeranyl transferase type-2 subunit beta|||N-acetylglycine|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||PFTB 6|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119772
http://togogenome.org/gene/9606:UGCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16739                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Motif|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Q/R)XXRW|||Ceramide glucosyltransferase|||Cytoplasmic|||D1|||D2|||D3|||Helical|||Lumenal|||May play an important role in binding to the inhibitors DEPC and PDMP|||N6-acetyllysine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059176
http://togogenome.org/gene/9606:AKR1B10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60218                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member B10|||Decreased affinity and reduced catalytic activity towards 4-hydroxynonenal.|||Increased affinity and reduced catalytic activity towards all-trans-retinaldehyde.|||Lowers pKa of active site Tyr|||N6-acetyllysine|||Proton donor|||Reduced catalytic activity towards all-trans-retinaldehyde.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124632|||http://purl.uniprot.org/annotation/VAR_013287|||http://purl.uniprot.org/annotation/VAR_020077|||http://purl.uniprot.org/annotation/VAR_020078
http://togogenome.org/gene/9606:ARHGEF37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1IGU5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  BAR|||DH|||Disordered|||Rho guanine nucleotide exchange factor 37|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337050|||http://purl.uniprot.org/annotation/VAR_043579|||http://purl.uniprot.org/annotation/VAR_043580|||http://purl.uniprot.org/annotation/VAR_043581|||http://purl.uniprot.org/annotation/VAR_043582|||http://purl.uniprot.org/annotation/VAR_043583
http://togogenome.org/gene/9606:SLC27A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1M0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Correlates with lower body mass index, triglyceride concentrations, systolic blood pressure, insulin concentrations and homeostasis model assessment index.|||Helical|||In IPS.|||In isoform 2.|||Long-chain fatty acid transport protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193209|||http://purl.uniprot.org/annotation/VAR_023783|||http://purl.uniprot.org/annotation/VAR_063192|||http://purl.uniprot.org/annotation/VAR_063193|||http://purl.uniprot.org/annotation/VAR_063194|||http://purl.uniprot.org/annotation/VAR_063195|||http://purl.uniprot.org/annotation/VAR_064500|||http://purl.uniprot.org/annotation/VSP_055808|||http://purl.uniprot.org/annotation/VSP_055809
http://togogenome.org/gene/9606:CYP4B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13584|||http://purl.uniprot.org/uniprot/Q8IZB0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4B1|||Helical|||In allele CYP4B1*2 and allele CYP4B1*7.|||In allele CYP4B1*2, allele CYP4B1*7 and allele CYP4B1*5.|||In allele CYP4B1*2.|||In allele CYP4B1*3 and allele CYP4B1*6.|||In allele CYP4B1*4.|||In allele CYP4B1*6.|||In isoform 2.|||Phosphoserine|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051819|||http://purl.uniprot.org/annotation/VAR_018357|||http://purl.uniprot.org/annotation/VAR_018358|||http://purl.uniprot.org/annotation/VAR_018359|||http://purl.uniprot.org/annotation/VAR_018360|||http://purl.uniprot.org/annotation/VAR_018361|||http://purl.uniprot.org/annotation/VAR_018362|||http://purl.uniprot.org/annotation/VAR_048453|||http://purl.uniprot.org/annotation/VAR_048454|||http://purl.uniprot.org/annotation/VAR_048455|||http://purl.uniprot.org/annotation/VAR_048456|||http://purl.uniprot.org/annotation/VAR_055377|||http://purl.uniprot.org/annotation/VAR_055378|||http://purl.uniprot.org/annotation/VSP_038419
http://togogenome.org/gene/9606:BRSK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJF6|||http://purl.uniprot.org/uniprot/B4DLY3|||http://purl.uniprot.org/uniprot/Q8IWQ3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Constitutively activated.|||Constitutively activated. Promotes formation of actin stress fibers.|||Decreased activation of kinase activity.|||Decreased phosphorylation. Nearly abolishes stimulation of insulin secretion.|||Disordered|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||KEN box|||Loss of catalytic activity. Causes disintegration of actin stress fibers.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Phosphothreonine; by PKA|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase BRSK2|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085670|||http://purl.uniprot.org/annotation/VSP_008154|||http://purl.uniprot.org/annotation/VSP_008155|||http://purl.uniprot.org/annotation/VSP_008156|||http://purl.uniprot.org/annotation/VSP_008157|||http://purl.uniprot.org/annotation/VSP_013945|||http://purl.uniprot.org/annotation/VSP_022603|||http://purl.uniprot.org/annotation/VSP_022604|||http://purl.uniprot.org/annotation/VSP_055679
http://togogenome.org/gene/9606:DNER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFT8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Delta and Notch-like epidermal growth factor-related receptor|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8; calcium-binding|||EGF-like 9|||Extracellular|||Follistatin-like|||Helical|||Interaction with AP1G1 and somatodendritic targeting|||Interaction with NOTCH1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253557|||http://purl.uniprot.org/annotation/VAR_028380
http://togogenome.org/gene/9606:SPOCK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTJ2|||http://purl.uniprot.org/uniprot/B4DI52|||http://purl.uniprot.org/uniprot/Q9BQ16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 1, isoform 8 and isoform 9.|||In isoform 2 and isoform 9.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Kazal-like|||O-linked (Xyl...) (glycosaminoglycan) serine|||Testican-3|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026703|||http://purl.uniprot.org/annotation/VAR_051562|||http://purl.uniprot.org/annotation/VSP_005334|||http://purl.uniprot.org/annotation/VSP_005335|||http://purl.uniprot.org/annotation/VSP_013598|||http://purl.uniprot.org/annotation/VSP_043681|||http://purl.uniprot.org/annotation/VSP_045104|||http://purl.uniprot.org/annotation/VSP_045899|||http://purl.uniprot.org/annotation/VSP_045900|||http://purl.uniprot.org/annotation/VSP_046686|||http://purl.uniprot.org/annotation/VSP_046687
http://togogenome.org/gene/9606:GIMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJR0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  AIG1-type G|||GTPase IMAP family member GIMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419199
http://togogenome.org/gene/9606:ANKRD20A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKR9|||http://purl.uniprot.org/uniprot/Q5TYW2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 20A1|||Basic and acidic residues|||CCDC144C-like coiled-coil|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240834
http://togogenome.org/gene/9606:ATP5MC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48201                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Site|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  ATP synthase F(0) complex subunit C3, mitochondrial|||Helical|||In DYTSPG.|||Mitochondrion|||N6,N6,N6-trimethyllysine|||Reversibly protonated during proton transport                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002567|||http://purl.uniprot.org/annotation/VAR_011922|||http://purl.uniprot.org/annotation/VAR_086710
http://togogenome.org/gene/9606:IRAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43187                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Death|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||Interleukin-1 receptor-associated kinase-like 2|||Phosphoserine|||Polar residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086032|||http://purl.uniprot.org/annotation/VAR_030527|||http://purl.uniprot.org/annotation/VAR_030528|||http://purl.uniprot.org/annotation/VAR_030529|||http://purl.uniprot.org/annotation/VAR_030530|||http://purl.uniprot.org/annotation/VAR_030531|||http://purl.uniprot.org/annotation/VAR_030532|||http://purl.uniprot.org/annotation/VAR_041342|||http://purl.uniprot.org/annotation/VAR_041343|||http://purl.uniprot.org/annotation/VAR_041344|||http://purl.uniprot.org/annotation/VAR_041345|||http://purl.uniprot.org/annotation/VAR_041346|||http://purl.uniprot.org/annotation/VAR_041347|||http://purl.uniprot.org/annotation/VAR_041348|||http://purl.uniprot.org/annotation/VAR_041349
http://togogenome.org/gene/9606:ITPKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9J0|||http://purl.uniprot.org/uniprot/P27987                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||In isoform 2.|||Inositol-trisphosphate 3-kinase B|||Loss of kinase activity.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066868|||http://purl.uniprot.org/annotation/VAR_022380|||http://purl.uniprot.org/annotation/VAR_023768|||http://purl.uniprot.org/annotation/VAR_053444|||http://purl.uniprot.org/annotation/VSP_016092
http://togogenome.org/gene/9606:PSMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK70|||http://purl.uniprot.org/uniprot/B7Z571|||http://purl.uniprot.org/uniprot/P35998                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  26S proteasome regulatory subunit 7|||AAA+ ATPase|||Disordered|||In isoform 2.|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084709|||http://purl.uniprot.org/annotation/VSP_056178
http://togogenome.org/gene/9606:NCKAP5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCH0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  (S/T)X(I/L)P motif 1|||(S/T)X(I/L)P motif 2|||(S/T)X(I/L)P motif 3; required for interaction with MAPRE1|||Disordered|||In isoform 2.|||In isoform 4.|||Loss of interaction with MAPRE1 and significantly reduced localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 486-A-A-487 and 818-A-A-819.|||Mediates interaction with CDK5RAP2 and is required for homodimerization and microtubule bundle formation|||Mediates interaction with beta-tubulin and is required for microtubule bundle formation|||Nck-associated protein 5-like|||No decrease in localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 486-A-A-487 and 928-A-A-929.|||No decrease in localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 818-A-A-819 and 928-A-A-929.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288447|||http://purl.uniprot.org/annotation/VSP_025678|||http://purl.uniprot.org/annotation/VSP_033818|||http://purl.uniprot.org/annotation/VSP_033819
http://togogenome.org/gene/9606:HMGB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15347                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cysteine sulfonic acid (-SO3H)|||Cysteine sulfonic acid (-SO3H); alternate|||Disordered|||HMG box 1|||HMG box 2|||High mobility group protein B3|||In disulfide HMGB3; alternate|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048539|||http://purl.uniprot.org/annotation/VAR_049558|||http://purl.uniprot.org/annotation/VAR_064162
http://togogenome.org/gene/9606:FEV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99581                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for insertion to form EWS-FEV fusion protein|||ETS|||May mediate active transcriptional repression|||Protein FEV                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344204
http://togogenome.org/gene/9606:EPS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z240|||http://purl.uniprot.org/uniprot/P42566                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 3 AA repeats of D-P-F|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EH 1|||EH 2|||EH 3|||Epidermal growth factor receptor substrate 15|||In isoform 2.|||Interaction with DAB2|||Loss of interaction with STON2 NPF motifs.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by EGFR|||Polar residues|||Pro residues|||Removed|||SH3-binding|||UIM 1|||UIM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146116|||http://purl.uniprot.org/annotation/VAR_016142|||http://purl.uniprot.org/annotation/VSP_036168|||http://purl.uniprot.org/annotation/VSP_036169
http://togogenome.org/gene/9606:G6PD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL00|||http://purl.uniprot.org/uniprot/P11413                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Does not impair dimerization and catalytic activity.|||Found in Santa Maria and Mount Sinai; associated with C-387 in Mount Sinai; class IV and class I.|||Glucose-6-phosphate 1-dehydrogenase|||Glucose-6-phosphate dehydrogenase C-terminal|||Glucose-6-phosphate dehydrogenase NAD-binding|||Impairs dimerization and reduces catalytic activity in cells under oxidative stress.|||Impairs dimerization and reduces catalytic activity.|||In Chinese-4.|||In Chinese-5.|||In Coimbra; class II.|||In Dindori; class II; 5% of activity.|||In Ierapetra; class II.|||In Kaiping; class II.|||In Mexico City; class III.|||In NSHA; A(-) type I; class III; frequent in African population.|||In NSHA; A- type 2; class III.|||In NSHA; A- type 3; class III.|||In NSHA; Alhambra; class I.|||In NSHA; Andalus; class I.|||In NSHA; Aures; class II.|||In NSHA; Bari; class I.|||In NSHA; Beverly Hills; class I.|||In NSHA; Bhavnagar; decreased enzyme stability.|||In NSHA; Campinas; class I.|||In NSHA; Canton; class II; frequent in China.|||In NSHA; Cassano; class II.|||In NSHA; Chatham; class III.|||In NSHA; Chinese-1; class II.|||In NSHA; Chinese-3; class II.|||In NSHA; Chinese-II/Maewo/Union; class II; <1% activity.|||In NSHA; Corum; class I.|||In NSHA; Cosenza; class II.|||In NSHA; Gahoe; class III; frequent in Chinese.|||In NSHA; Guadajalara and Mount Sinai; class I.|||In NSHA; Harilaou; class I.|||In NSHA; Herlev; loss of glucose-6-phosphate dehydrogenase activity.|||In NSHA; Ilesha; class III.|||In NSHA; Iowa; class I.|||In NSHA; Japan; class I.|||In NSHA; Kalyan/Kerala; class III.|||In NSHA; Konan/Ube; class III.|||In NSHA; Lagosanto; class III.|||In NSHA; Loma Linda; class I.|||In NSHA; Mahidol; class III; associated with reduced density of Plasmodium vivax but not Plasmodium falciparum in Southeast Asians; reduced activity.|||In NSHA; Metaponto; class III.|||In NSHA; Minnesota; class I.|||In NSHA; Montalbano; class III.|||In NSHA; Namoru; 4% activity.|||In NSHA; Naone; 1% activity.|||In NSHA; Nashville/Anaheim; class I.|||In NSHA; Orissa; class III; frequent in Indian tribal populations.|||In NSHA; Pawnee; class I.|||In NSHA; Plymouth; class I.|||In NSHA; Puerto Limon; class I.|||In NSHA; Riverside; class I.|||In NSHA; Santa Maria; class I.|||In NSHA; Santiago de Cuba; class I.|||In NSHA; Santiago; class I.|||In NSHA; Sassari/Cagliari; class II; frequent in the Mediterranean.|||In NSHA; Seattle; class III.|||In NSHA; Shinshu; class I.|||In NSHA; Sibari; class III.|||In NSHA; Stonybrook; class I.|||In NSHA; Sunderland; class I.|||In NSHA; Swansea; class I.|||In NSHA; Telti/Kobe; class I.|||In NSHA; Tokyo; class I.|||In NSHA; Tomah; class I.|||In NSHA; Vancouver; class I.|||In NSHA; Vanua Lava; 4% activity.|||In NSHA; Viangchan/Jammu; class II.|||In NSHA; Wayne; class I.|||In NSHA; Wexham; class I.|||In Nilgiris; class II.|||In Rehovot.|||In Sinnai.|||In isoform 3.|||In isoform Long.|||Inhibits catalytic activity. Does not impair dimerization.|||N-acetylalanine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068083|||http://purl.uniprot.org/annotation/VAR_002450|||http://purl.uniprot.org/annotation/VAR_002451|||http://purl.uniprot.org/annotation/VAR_002452|||http://purl.uniprot.org/annotation/VAR_002453|||http://purl.uniprot.org/annotation/VAR_002454|||http://purl.uniprot.org/annotation/VAR_002455|||http://purl.uniprot.org/annotation/VAR_002456|||http://purl.uniprot.org/annotation/VAR_002457|||http://purl.uniprot.org/annotation/VAR_002458|||http://purl.uniprot.org/annotation/VAR_002459|||http://purl.uniprot.org/annotation/VAR_002460|||http://purl.uniprot.org/annotation/VAR_002461|||http://purl.uniprot.org/annotation/VAR_002462|||http://purl.uniprot.org/annotation/VAR_002463|||http://purl.uniprot.org/annotation/VAR_002464|||http://purl.uniprot.org/annotation/VAR_002465|||http://purl.uniprot.org/annotation/VAR_002466|||http://purl.uniprot.org/annotation/VAR_002467|||http://purl.uniprot.org/annotation/VAR_002468|||http://purl.uniprot.org/annotation/VAR_002469|||http://purl.uniprot.org/annotation/VAR_002470|||http://purl.uniprot.org/annotation/VAR_002471|||http://purl.uniprot.org/annotation/VAR_002472|||http://purl.uniprot.org/annotation/VAR_002473|||http://purl.uniprot.org/annotation/VAR_002474|||http://purl.uniprot.org/annotation/VAR_002475|||http://purl.uniprot.org/annotation/VAR_002476|||http://purl.uniprot.org/annotation/VAR_002477|||http://purl.uniprot.org/annotation/VAR_002478|||http://purl.uniprot.org/annotation/VAR_002479|||http://purl.uniprot.org/annotation/VAR_002480|||http://purl.uniprot.org/annotation/VAR_002481|||http://purl.uniprot.org/annotation/VAR_002482|||http://purl.uniprot.org/annotation/VAR_002483|||http://purl.uniprot.org/annotation/VAR_002484|||http://purl.uniprot.org/annotation/VAR_002485|||http://purl.uniprot.org/annotation/VAR_002486|||http://purl.uniprot.org/annotation/VAR_002487|||http://purl.uniprot.org/annotation/VAR_002488|||http://purl.uniprot.org/annotation/VAR_002489|||http://purl.uniprot.org/annotation/VAR_002490|||http://purl.uniprot.org/annotation/VAR_002491|||http://purl.uniprot.org/annotation/VAR_002492|||http://purl.uniprot.org/annotation/VAR_002493|||http://purl.uniprot.org/annotation/VAR_002494|||http://purl.uniprot.org/annotation/VAR_002495|||http://purl.uniprot.org/annotation/VAR_002496|||http://purl.uniprot.org/annotation/VAR_002497|||http://purl.uniprot.org/annotation/VAR_002498|||http://purl.uniprot.org/annotation/VAR_002499|||http://purl.uniprot.org/annotation/VAR_002500|||http://purl.uniprot.org/annotation/VAR_002501|||http://purl.uniprot.org/annotation/VAR_002502|||http://purl.uniprot.org/annotation/VAR_002503|||http://purl.uniprot.org/annotation/VAR_002504|||http://purl.uniprot.org/annotation/VAR_002505|||http://purl.uniprot.org/annotation/VAR_002506|||http://purl.uniprot.org/annotation/VAR_002507|||http://purl.uniprot.org/annotation/VAR_002508|||http://purl.uniprot.org/annotation/VAR_002509|||http://purl.uniprot.org/annotation/VAR_002510|||http://purl.uniprot.org/annotation/VAR_002511|||http://purl.uniprot.org/annotation/VAR_002512|||http://purl.uniprot.org/annotation/VAR_002513|||http://purl.uniprot.org/annotation/VAR_002514|||http://purl.uniprot.org/annotation/VAR_002515|||http://purl.uniprot.org/annotation/VAR_020535|||http://purl.uniprot.org/annotation/VAR_075555|||http://purl.uniprot.org/annotation/VAR_081894|||http://purl.uniprot.org/annotation/VAR_081895|||http://purl.uniprot.org/annotation/VAR_081896|||http://purl.uniprot.org/annotation/VSP_001592|||http://purl.uniprot.org/annotation/VSP_037802
http://togogenome.org/gene/9606:RNF24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y225                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Helical|||In isoform 2.|||RING finger protein 24|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056063|||http://purl.uniprot.org/annotation/VSP_041026
http://togogenome.org/gene/9606:VPS36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VN1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GLUE C-terminal|||GLUE N-terminal|||In isoform 2.|||No effect on interaction with ubiquitin.|||Reduces affinity for ubiquitin up to 10-fold.|||Vacuolar protein-sorting-associated protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215222|||http://purl.uniprot.org/annotation/VSP_015342
http://togogenome.org/gene/9606:KIF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIQ8|||http://purl.uniprot.org/uniprot/Q2M1P5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found as heterozygous variant in a patient with Bardet-Biedl syndrome; hypomorphic variant in vitro.|||In ACLS; atypical phenotype; unknown pathological significance.|||In ACLS; may affect splicing; hypomorphic mutation in vitro.|||In AGBK.|||In BBS; the patient also carries homozygous mutation R-390 in BBS1; may affect splicing; hypomorphic variant in vitro.|||In BBS; the patient is a compound heterozygote for a truncating mutation and mutation R-390 in BBS1; hypomorphic variant in vitro.|||In BBS; the patient is a compound heterozygote for two frameshift mutations in BBS9; hypomorphic variant in vitro.|||In JBTS12; found in a patient with Joubert syndrome that also carries mutations L-358 and T-833 in TMEM67.|||Interaction with DLG5|||Interaction with SMO|||Kinesin motor|||Kinesin-like protein KIF7|||Phosphoserine|||Polar residues|||Rare variant found in a patient with Bardet-Biedl syndrome also carrying a frameshift mutation in BBS10 and variant P-293 in BBS7.|||Sufficient for interaction with NPHP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307146|||http://purl.uniprot.org/annotation/VAR_035363|||http://purl.uniprot.org/annotation/VAR_035364|||http://purl.uniprot.org/annotation/VAR_061287|||http://purl.uniprot.org/annotation/VAR_066450|||http://purl.uniprot.org/annotation/VAR_066451|||http://purl.uniprot.org/annotation/VAR_066452|||http://purl.uniprot.org/annotation/VAR_066453|||http://purl.uniprot.org/annotation/VAR_066454|||http://purl.uniprot.org/annotation/VAR_066455|||http://purl.uniprot.org/annotation/VAR_066456|||http://purl.uniprot.org/annotation/VAR_066457|||http://purl.uniprot.org/annotation/VAR_066458|||http://purl.uniprot.org/annotation/VAR_071185|||http://purl.uniprot.org/annotation/VAR_077692|||http://purl.uniprot.org/annotation/VAR_077693|||http://purl.uniprot.org/annotation/VAR_077694|||http://purl.uniprot.org/annotation/VAR_077695
http://togogenome.org/gene/9606:ZNF501                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CX3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||Zinc finger protein 501                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047621|||http://purl.uniprot.org/annotation/VAR_024219|||http://purl.uniprot.org/annotation/VAR_061952|||http://purl.uniprot.org/annotation/VSP_010173
http://togogenome.org/gene/9606:NR1H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXU5|||http://purl.uniprot.org/uniprot/B5MBY7|||http://purl.uniprot.org/uniprot/F1D8N1|||http://purl.uniprot.org/uniprot/Q13133                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with NCOA2 without affecting interaction with GPS2; when associated with 268-A--A-273.|||Abolishes interaction with NCOA2 without affecting interaction with GPS2; when associated with 438-A-A-439.|||Disordered|||In isoform 2.|||In isoform 3.|||NR C4-type|||NR LBD|||Nuclear receptor|||Oxysterols receptor LXR-alpha|||Transactivation AF-1; required for ligand-independent transactivation function|||Transactivation AF-2; required for ligand-dependent transactivation function; mediates interaction with CCAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053535|||http://purl.uniprot.org/annotation/VAR_050580|||http://purl.uniprot.org/annotation/VSP_003664|||http://purl.uniprot.org/annotation/VSP_044960
http://togogenome.org/gene/9606:NXF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4D5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Inactivates CRM1 binding; when associated with R-300.|||Inactivates CRM1 binding; when associated with R-302.|||NTF2|||Nuclear RNA export factor 3|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220534|||http://purl.uniprot.org/annotation/VAR_050419|||http://purl.uniprot.org/annotation/VSP_057068|||http://purl.uniprot.org/annotation/VSP_057069|||http://purl.uniprot.org/annotation/VSP_057070
http://togogenome.org/gene/9606:TRPM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX84                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes kinase activity but does not affect expression levels or binding to RACK1.|||Alpha-type protein kinase|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HOMG1; impairs heterodimer formation resulting in intracellular retention.|||In HOMG1; loss of function; no effect on cell membrane localization.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform M6-kinase 1.|||In isoform M6-kinase 2.|||In isoform M6-kinase 3.|||In isoform TRPM6b.|||In isoform TRPM6c.|||In isoform TRPM6t.|||No effect on function or cell membrane localization.|||Phosphothreonine; by autocatalysis|||Polar residues|||Pore-forming|||Proton acceptor|||Significantly decreases autophosphorylation. Does not alter binding to RACK1 but prevents inhibition by RACK1.|||Significantly decreases autophosphorylation. Does not alter binding to RACK1 or inhibition by RACK1.|||Transient receptor potential cation channel subfamily M member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215329|||http://purl.uniprot.org/annotation/VAR_019963|||http://purl.uniprot.org/annotation/VAR_019964|||http://purl.uniprot.org/annotation/VAR_019965|||http://purl.uniprot.org/annotation/VAR_019966|||http://purl.uniprot.org/annotation/VAR_042387|||http://purl.uniprot.org/annotation/VAR_042388|||http://purl.uniprot.org/annotation/VAR_042389|||http://purl.uniprot.org/annotation/VAR_042390|||http://purl.uniprot.org/annotation/VAR_042391|||http://purl.uniprot.org/annotation/VAR_042392|||http://purl.uniprot.org/annotation/VAR_042393|||http://purl.uniprot.org/annotation/VAR_042394|||http://purl.uniprot.org/annotation/VAR_052380|||http://purl.uniprot.org/annotation/VAR_071480|||http://purl.uniprot.org/annotation/VAR_071481|||http://purl.uniprot.org/annotation/VAR_071482|||http://purl.uniprot.org/annotation/VAR_071483|||http://purl.uniprot.org/annotation/VAR_071484|||http://purl.uniprot.org/annotation/VSP_012069|||http://purl.uniprot.org/annotation/VSP_012070|||http://purl.uniprot.org/annotation/VSP_012071|||http://purl.uniprot.org/annotation/VSP_012072|||http://purl.uniprot.org/annotation/VSP_012073|||http://purl.uniprot.org/annotation/VSP_012074|||http://purl.uniprot.org/annotation/VSP_012075|||http://purl.uniprot.org/annotation/VSP_012076
http://togogenome.org/gene/9606:ARSH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FYA8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase H|||Helical|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295623
http://togogenome.org/gene/9606:PCDHB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5E6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003918|||http://purl.uniprot.org/annotation/VAR_020366|||http://purl.uniprot.org/annotation/VAR_024391|||http://purl.uniprot.org/annotation/VAR_033703
http://togogenome.org/gene/9606:ZNF705G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUZ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||KRAB|||Putative zinc finger protein 705G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342396
http://togogenome.org/gene/9606:PI16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||Peptidase inhibitor 16|||Polar residues|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287633|||http://purl.uniprot.org/annotation/VAR_032337|||http://purl.uniprot.org/annotation/VAR_032338|||http://purl.uniprot.org/annotation/VSP_025574
http://togogenome.org/gene/9606:MFF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS29|||http://purl.uniprot.org/uniprot/A0A9L9PY92|||http://purl.uniprot.org/uniprot/Q9GZY8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mff-like|||Mitochondrial fission factor|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289184|||http://purl.uniprot.org/annotation/VAR_036028|||http://purl.uniprot.org/annotation/VAR_053915|||http://purl.uniprot.org/annotation/VAR_053916|||http://purl.uniprot.org/annotation/VSP_025954|||http://purl.uniprot.org/annotation/VSP_025955|||http://purl.uniprot.org/annotation/VSP_025956|||http://purl.uniprot.org/annotation/VSP_025957|||http://purl.uniprot.org/annotation/VSP_025958
http://togogenome.org/gene/9606:TASOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein TASOR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299542|||http://purl.uniprot.org/annotation/VAR_034838|||http://purl.uniprot.org/annotation/VAR_034839|||http://purl.uniprot.org/annotation/VAR_034840|||http://purl.uniprot.org/annotation/VAR_050848|||http://purl.uniprot.org/annotation/VAR_050849|||http://purl.uniprot.org/annotation/VAR_050850|||http://purl.uniprot.org/annotation/VAR_050851|||http://purl.uniprot.org/annotation/VAR_050852|||http://purl.uniprot.org/annotation/VAR_050853|||http://purl.uniprot.org/annotation/VAR_061601|||http://purl.uniprot.org/annotation/VAR_061602|||http://purl.uniprot.org/annotation/VSP_027733
http://togogenome.org/gene/9606:SLC5A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD19|||http://purl.uniprot.org/uniprot/Q9Y289                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Decrease in biotin transport.|||Disordered|||Helical|||In COMNB; no effect on membrane localization.|||In SMVTD and COMNB; reduced membrane localization; impaired biotin transport.|||In SMVTD; impaired biotin transport.|||In SMVTD; reduced membrane localization; impaired biotin transport.|||Loss of apical membrane localization in polarized cells. Basolateral localization in polarized cells.|||Loss of biotin transport. Loss of membrane localization.|||N-linked (GlcNAc...) asparagine|||No effect on biotin transport.|||No effect on protein levels or membrane localization.|||Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.|||Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.|||Reduced membrane localization. Decrease in biotin transport (decreased Vmax, no change in Km).|||Reduced membrane localization. Decrease in biotin transport.|||Reduced protein levels. Decrease in biotin transport.|||Resistant to phorbol 12-myristate 13-acetate (PMA)-induced inhibition of biotin transport. No effect on protein levels or membrane localization.|||Slight decrease in protein levels. Decrease in biotin transport.|||Sodium-dependent multivitamin transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105386|||http://purl.uniprot.org/annotation/VAR_052491|||http://purl.uniprot.org/annotation/VAR_052492|||http://purl.uniprot.org/annotation/VAR_084535|||http://purl.uniprot.org/annotation/VAR_084536|||http://purl.uniprot.org/annotation/VAR_084537|||http://purl.uniprot.org/annotation/VAR_087446|||http://purl.uniprot.org/annotation/VAR_087447
http://togogenome.org/gene/9606:NCSTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPQ8|||http://purl.uniprot.org/uniprot/A0A8V8TPR8|||http://purl.uniprot.org/uniprot/B4DR82|||http://purl.uniprot.org/uniprot/Q92542                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In ACNINV1.|||In isoform 2.|||Increases production of amyloid-beta (beta-APP40 and beta-APP42) in APP processing.|||N-linked (GlcNAc...) asparagine|||Nicastrin|||Nicastrin small lobe|||No effect on gamma-secretase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019681|||http://purl.uniprot.org/annotation/PRO_5002800944|||http://purl.uniprot.org/annotation/PRO_5036452765|||http://purl.uniprot.org/annotation/PRO_5040044585|||http://purl.uniprot.org/annotation/VAR_050274|||http://purl.uniprot.org/annotation/VAR_050275|||http://purl.uniprot.org/annotation/VAR_067756|||http://purl.uniprot.org/annotation/VSP_008385|||http://purl.uniprot.org/annotation/VSP_008386
http://togogenome.org/gene/9606:LYRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43325                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  LYR motif-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174310
http://togogenome.org/gene/9606:LRP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75581                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes Wnt/beta-catenin signaling.|||Abolishes phosphorylation of PPPSP motif B. Reduced Wnt/beta-catenin signaling.|||Abolishes ubiquitination, no change in plasma membrane location in the presence of MESD but greatly reduced Wnt-signaling activity. Exhibits full Wnt-signaling activity and no change in plasma membrane location; when associated with A-1394 and A-1399.|||Beta-propeller 1|||Beta-propeller 2|||Beta-propeller 3|||Beta-propeller 4|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Enhanced AXIN1 binding and increased beta-catenin activity by 2.2-fold. Further enhanced AXIN1 binding and increases beta-catenin activity by 3.3-fold; when associated with A-1430.|||Enhanced AXIN1 binding. Further enhanced AXIN1 binding and increases beta-catenin activity by 3.3-fold; when associated with A-1420.|||Extracellular|||Found in a patient with congenital hydrocephalus; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced phosphorylation of PPPSP motif A. Greatly reduced Wnt/beta-catenin signaling.|||Helical|||In ADCAD2.|||In ADCAD2; impairs Wnt signaling in vitro.|||In ADCAD2; impairs Wnt signaling.|||In STHAG7; impairs Wnt signaling; prevents transport to plasma membrane location.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 18|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Low-density lipoprotein receptor-related protein 6|||N-linked (GlcNAc...) asparagine|||No change in the phosphorylation state of PPPSP motif A. Greatly reduced Wnt/beta-catenin signaling.|||No change in the phosphorylation state of PPPSP motif A. Little reduction of Wnt/beta-catenin signaling.|||No change in the phosphorylation state of PPPSP motif. Increased Wnt/beta-catenin signaling.|||No change in the phosphorylation state of PPPSP motif. No reduction of Wnt/beta-catenin signaling.|||No change in the phosphorylation state of PPPSP motif. Some reduction in Wnt/beta-catenin signaling.|||No effect on the phosphorylation state of PPPSP motif B.|||PPPSP motif A|||PPPSP motif B|||PPPSP motif C|||PPPSP motif D|||PPPSP motif E|||Phosphoserine; by CDK14, GRK5 and GRK6|||Phosphoserine; by CK1|||Phosphothreonine|||Phosphothreonine; by CK1|||S-palmitoyl cysteine|||Some loss of phosphorylation of PPPSP motif A. Little reduction in Wnt/beta-catenin signaling.|||Some reduction of palmitoylation, and little change in plasma membrane location in the presence of MESD nor in Wnt-signaling activity. Completely abolishes palmitoylation, no plasma membrane location, greatly reduced Wnt-signaling activity but no effect on ubiquitination; when associated with A-1394. Exhibits full Wnt-signaling activity and no change in plasma membrane location in the in presence of MESD; when associated with A-1394 and R-1403.|||Some reduction of palmitoylation, little change in plasma membrane location in the presence of MESD nor in Wnt-signaling activity. Completely abolishes palmitoylation, no plasma membrane location, greatly reduced Wnt-signaling activity but no effect on ubiquitination; when associated with A-1399. Exhibits full Wnt-signaling activity and no change in plasma membrane location; when associated with A-1399 and R-1403.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017330|||http://purl.uniprot.org/annotation/VAR_024520|||http://purl.uniprot.org/annotation/VAR_030349|||http://purl.uniprot.org/annotation/VAR_030350|||http://purl.uniprot.org/annotation/VAR_034701|||http://purl.uniprot.org/annotation/VAR_034702|||http://purl.uniprot.org/annotation/VAR_076207|||http://purl.uniprot.org/annotation/VAR_076208|||http://purl.uniprot.org/annotation/VAR_076209|||http://purl.uniprot.org/annotation/VAR_076210|||http://purl.uniprot.org/annotation/VAR_083431
http://togogenome.org/gene/9606:C8orf34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49A92                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Uncharacterized protein C8orf34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330039|||http://purl.uniprot.org/annotation/VAR_042690|||http://purl.uniprot.org/annotation/VAR_042691|||http://purl.uniprot.org/annotation/VSP_059473|||http://purl.uniprot.org/annotation/VSP_059474|||http://purl.uniprot.org/annotation/VSP_059475|||http://purl.uniprot.org/annotation/VSP_059476|||http://purl.uniprot.org/annotation/VSP_059477|||http://purl.uniprot.org/annotation/VSP_059478
http://togogenome.org/gene/9606:KLHL30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0D2K2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274594
http://togogenome.org/gene/9606:CCDC87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 87                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295145|||http://purl.uniprot.org/annotation/VAR_033224|||http://purl.uniprot.org/annotation/VAR_056782
http://togogenome.org/gene/9606:RCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAC5|||http://purl.uniprot.org/uniprot/Q9P258                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Loss of interaction with RAC1 and loss of regulation of RAC1 activation.|||Loss of interaction with RAC1.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein RCC2|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||Required for interaction with RAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206652
http://togogenome.org/gene/9606:LRRN4CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND94                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||LRRN4 C-terminal-like protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317752
http://togogenome.org/gene/9606:BLNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2MD54|||http://purl.uniprot.org/uniprot/Q2MD59|||http://purl.uniprot.org/uniprot/Q8WV28                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||B-cell linker protein|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphotyrosine; by SYK|||Polar residues|||SH2|||Significant phosphorylation reduction; when associated with F-72; F-84 and F-178.|||Significant phosphorylation reduction; when associated with F-72; F-84 and F-96.|||Significant phosphorylation reduction; when associated with F-72; F-96 and F-178.|||Significant phosphorylation reduction; when associated with F-84; F-96 and F-178.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064940|||http://purl.uniprot.org/annotation/VSP_016178|||http://purl.uniprot.org/annotation/VSP_045324
http://togogenome.org/gene/9606:SPATA6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4H0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Spermatogenesis associated 6-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089704|||http://purl.uniprot.org/annotation/VAR_053838|||http://purl.uniprot.org/annotation/VAR_053839|||http://purl.uniprot.org/annotation/VSP_014315|||http://purl.uniprot.org/annotation/VSP_014316|||http://purl.uniprot.org/annotation/VSP_014317|||http://purl.uniprot.org/annotation/VSP_043770
http://togogenome.org/gene/9606:PRPF4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13523                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a breast cancer sample; somatic mutation.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase PRP4 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086586|||http://purl.uniprot.org/annotation/VAR_035633|||http://purl.uniprot.org/annotation/VAR_046969|||http://purl.uniprot.org/annotation/VAR_047798
http://togogenome.org/gene/9606:BCL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00512|||http://purl.uniprot.org/uniprot/Q1JQ81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with CTNNB1.|||Abolishes interaction with CTNNB1; when associated with A-366.|||Abolishes interaction with CTNNB1; when associated with A-369.|||Asymmetric dimethylarginine|||B-cell CLL/lymphoma 9 protein|||B-cell lymphoma 9 beta-catenin binding|||Basic and acidic residues|||Disordered|||Interaction with CTNNB1|||Interaction with PYGO1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064885|||http://purl.uniprot.org/annotation/VAR_046545|||http://purl.uniprot.org/annotation/VAR_046546
http://togogenome.org/gene/9606:HEYL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Hairy/enhancer-of-split related with YRPW motif-like protein|||Orange|||Polar residues|||Transcriptional repression and interaction with NCOR1 and SIN3A|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286429|||http://purl.uniprot.org/annotation/VAR_032112
http://togogenome.org/gene/9606:ACSBG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD4|||http://purl.uniprot.org/uniprot/A0A7P0Z4L8|||http://purl.uniprot.org/uniprot/B4DYU1|||http://purl.uniprot.org/uniprot/Q5FVE4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Long-chain-fatty-acid--CoA ligase ACSBG2|||Results in a shift of the pH optimum to a more acidic pH without affecting substrate specificity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315812|||http://purl.uniprot.org/annotation/VAR_038317|||http://purl.uniprot.org/annotation/VAR_038318|||http://purl.uniprot.org/annotation/VAR_038319|||http://purl.uniprot.org/annotation/VAR_038320|||http://purl.uniprot.org/annotation/VAR_038321|||http://purl.uniprot.org/annotation/VAR_038322|||http://purl.uniprot.org/annotation/VAR_038323|||http://purl.uniprot.org/annotation/VAR_038324|||http://purl.uniprot.org/annotation/VSP_030717|||http://purl.uniprot.org/annotation/VSP_030718|||http://purl.uniprot.org/annotation/VSP_030719
http://togogenome.org/gene/9606:HNRNPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDT2|||http://purl.uniprot.org/uniprot/P55795                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||2 X 16 AA Gly-rich approximate repeats|||2 X 19 AA perfect repeats|||2-1|||2-2|||Dimethylated arginine; alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein H2|||Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed|||In MRXSB.|||N-acetylmethionine|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein H2, N-terminally processed|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081859|||http://purl.uniprot.org/annotation/PRO_0000434385|||http://purl.uniprot.org/annotation/VAR_077233|||http://purl.uniprot.org/annotation/VAR_077234|||http://purl.uniprot.org/annotation/VAR_077235
http://togogenome.org/gene/9606:DMWD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09019|||http://purl.uniprot.org/uniprot/Q8WUW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dystrophia myotonica WD repeat-containing protein|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050956
http://togogenome.org/gene/9606:F5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12259                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||2 X 17 AA tandem repeats|||2-1|||2-10|||2-11|||2-12|||2-13|||2-14|||2-15|||2-16|||2-17|||2-18|||2-19|||2-2|||2-20|||2-21|||2-22|||2-23|||2-24|||2-25|||2-26|||2-27|||2-28|||2-29|||2-3|||2-30|||2-31|||2-32|||2-33|||2-34|||2-35|||2-4|||2-5|||2-6|||2-7|||2-8|||2-9|||35 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T|||Activation peptide (connecting region)|||B|||Cleavage; by activated protein C|||Cleavage; by thrombin|||Coagulation factor V|||Coagulation factor V heavy chain|||Coagulation factor V light chain|||Disordered|||F5/8 type A 1|||F5/8 type A 2|||F5/8 type A 3|||F5/8 type C 1|||F5/8 type C 2|||In FA5D; Seoul 2.|||In FA5D; impairs both factor V secretion and activity.|||In Hong Kong; does not predispose to clinical thrombosis.|||In THPH2.|||In THPH2; Cambridge.|||In THPH2; Liverpool; mutant protein is expressed with an additional carbohydrate chain.|||In THPH2; Nijkerk.|||In THPH2; factor VLeiden; associated with susceptibility to Budd-Chiari syndrome; associated with susceptibility to ischemic stroke.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||Polar residues|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002978|||http://purl.uniprot.org/annotation/PRO_0000002979|||http://purl.uniprot.org/annotation/PRO_0000002980|||http://purl.uniprot.org/annotation/PRO_0000002981|||http://purl.uniprot.org/annotation/VAR_001213|||http://purl.uniprot.org/annotation/VAR_001214|||http://purl.uniprot.org/annotation/VAR_001215|||http://purl.uniprot.org/annotation/VAR_013620|||http://purl.uniprot.org/annotation/VAR_013621|||http://purl.uniprot.org/annotation/VAR_013622|||http://purl.uniprot.org/annotation/VAR_013886|||http://purl.uniprot.org/annotation/VAR_013887|||http://purl.uniprot.org/annotation/VAR_013888|||http://purl.uniprot.org/annotation/VAR_013889|||http://purl.uniprot.org/annotation/VAR_013890|||http://purl.uniprot.org/annotation/VAR_013891|||http://purl.uniprot.org/annotation/VAR_013892|||http://purl.uniprot.org/annotation/VAR_013893|||http://purl.uniprot.org/annotation/VAR_013894|||http://purl.uniprot.org/annotation/VAR_013895|||http://purl.uniprot.org/annotation/VAR_013896|||http://purl.uniprot.org/annotation/VAR_013897|||http://purl.uniprot.org/annotation/VAR_013898|||http://purl.uniprot.org/annotation/VAR_013899|||http://purl.uniprot.org/annotation/VAR_017329|||http://purl.uniprot.org/annotation/VAR_021297|||http://purl.uniprot.org/annotation/VAR_021298|||http://purl.uniprot.org/annotation/VAR_021299|||http://purl.uniprot.org/annotation/VAR_021300|||http://purl.uniprot.org/annotation/VAR_021301|||http://purl.uniprot.org/annotation/VAR_021302|||http://purl.uniprot.org/annotation/VAR_032698|||http://purl.uniprot.org/annotation/VAR_032699|||http://purl.uniprot.org/annotation/VAR_032700|||http://purl.uniprot.org/annotation/VAR_032701|||http://purl.uniprot.org/annotation/VAR_034603|||http://purl.uniprot.org/annotation/VAR_035817|||http://purl.uniprot.org/annotation/VAR_047740|||http://purl.uniprot.org/annotation/VAR_047741
http://togogenome.org/gene/9606:RIPOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7B3|||http://purl.uniprot.org/uniprot/A0A2R8YEE0|||http://purl.uniprot.org/uniprot/B7Z5J9|||http://purl.uniprot.org/uniprot/B7Z6D6|||http://purl.uniprot.org/uniprot/B7Z6U4|||http://purl.uniprot.org/uniprot/F5GX51|||http://purl.uniprot.org/uniprot/F5H029|||http://purl.uniprot.org/uniprot/Q9Y4F9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FAM65 N-terminal|||In DFNA21; does not affect expression level; contrary to wild-type, does not rescue the morphological defects observed in hair cells of knockout mice, which include hair bundle polarity and cohesion and length of stereocilia.|||In isoform 2.|||Inhibits interaction with RHOA and does not prevent T cell proliferation inhibition; in isoform 2.|||Inhibits interaction with RHOA; in isoform 2.|||Involved in cell filopodia formation|||Phosphoserine|||Phosphoserine; in isoform 2|||Polar residues|||Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-341; A-523 and A-585 (isoform 2).|||Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-37; A-341 and A-523 (isoform 2).|||Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-37; A-341 and A-585 (isoform 2).|||Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-21; A-37; A-523 and A-585 (isoform 2).|||Reduces phosphorylation, interaction with HDAC6, YWHAB and 14-3-3 proteins, localization at the front of the neutrophil upon chemokine stimulation and prevents T cell proliferation inhibition; when associated with A-37; A-341; A-523 and A-585 (isoform 2).|||Rho family-interacting cell polarization regulator 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289114|||http://purl.uniprot.org/annotation/VAR_032572|||http://purl.uniprot.org/annotation/VAR_032573|||http://purl.uniprot.org/annotation/VAR_032574|||http://purl.uniprot.org/annotation/VAR_032575|||http://purl.uniprot.org/annotation/VAR_032576|||http://purl.uniprot.org/annotation/VAR_032577|||http://purl.uniprot.org/annotation/VAR_062193|||http://purl.uniprot.org/annotation/VAR_087100|||http://purl.uniprot.org/annotation/VSP_025904|||http://purl.uniprot.org/annotation/VSP_025905|||http://purl.uniprot.org/annotation/VSP_025906
http://togogenome.org/gene/9606:OPALIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS47|||http://purl.uniprot.org/uniprot/A0A0A0MTN4|||http://purl.uniprot.org/uniprot/Q96PE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Opalin|||Required for plasma membrane localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072591|||http://purl.uniprot.org/annotation/VSP_042943|||http://purl.uniprot.org/annotation/VSP_046290|||http://purl.uniprot.org/annotation/VSP_054892
http://togogenome.org/gene/9606:USP9X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J4R6|||http://purl.uniprot.org/uniprot/A0A994J6S4|||http://purl.uniprot.org/uniprot/Q6P468|||http://purl.uniprot.org/uniprot/Q86X58|||http://purl.uniprot.org/uniprot/Q93008                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DUF3517|||Disordered|||Does not restore RICTOR expression levels when introduced into cells where endogenous USP9X has been silenced.|||In MRXS99F.|||In MRXS99F; decreased expression levels.|||In XLID99; unknown pathological significance; does not affect interaction with DCX; reduced subcellular localization in the axonal growth cones.|||In isoform 2.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Probable ubiquitin carboxyl-terminal hydrolase FAF-X|||Proton acceptor|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080689|||http://purl.uniprot.org/annotation/VAR_071131|||http://purl.uniprot.org/annotation/VAR_071132|||http://purl.uniprot.org/annotation/VAR_086077|||http://purl.uniprot.org/annotation/VAR_086078|||http://purl.uniprot.org/annotation/VAR_086079|||http://purl.uniprot.org/annotation/VAR_086080|||http://purl.uniprot.org/annotation/VAR_086081|||http://purl.uniprot.org/annotation/VAR_086082|||http://purl.uniprot.org/annotation/VSP_060711
http://togogenome.org/gene/9606:NALF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75949                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||NALCN channel auxiliary factor 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072598|||http://purl.uniprot.org/annotation/VAR_043975
http://togogenome.org/gene/9606:ZNF230                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIE0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||KRNB|||Zinc finger protein 230                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047471|||http://purl.uniprot.org/annotation/VAR_014827|||http://purl.uniprot.org/annotation/VAR_030534|||http://purl.uniprot.org/annotation/VAR_030535
http://togogenome.org/gene/9606:FAM210B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  DUF1279|||Disordered|||Helical|||Mitochondrion|||Polar residues|||Protein FAM210B, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079451|||http://purl.uniprot.org/annotation/VAR_033763
http://togogenome.org/gene/9606:UBE2Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7E8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||In isoform 2.|||N-acetylmethionine|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223876|||http://purl.uniprot.org/annotation/VSP_017296
http://togogenome.org/gene/9606:CST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1J1|||http://purl.uniprot.org/uniprot/P01034                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cystatin|||Cystatin-C|||In AMYL6.|||In ARMD11; alters processing and glycosylation.|||Phosphoserine; by FAM20C|||Reactive site|||Secondary area of contact|||Shows a dual distribution to the Golgi apparatus and to the mitochondria.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006639|||http://purl.uniprot.org/annotation/PRO_5018595643|||http://purl.uniprot.org/annotation/VAR_002207|||http://purl.uniprot.org/annotation/VAR_011893
http://togogenome.org/gene/9606:ARHGAP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2F6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Polar residues|||Ras-associating|||Rho GTPase-activating protein 20|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283086|||http://purl.uniprot.org/annotation/VAR_031489|||http://purl.uniprot.org/annotation/VAR_031490|||http://purl.uniprot.org/annotation/VSP_024294|||http://purl.uniprot.org/annotation/VSP_024295|||http://purl.uniprot.org/annotation/VSP_024296
http://togogenome.org/gene/9606:SH2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14492                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2|||SH2B adapter protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064647|||http://purl.uniprot.org/annotation/VSP_059358
http://togogenome.org/gene/9606:ZNF500                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60304                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||KRAB|||SCAN box|||Zinc finger protein 500                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047620|||http://purl.uniprot.org/annotation/VSP_055962
http://togogenome.org/gene/9606:NAAA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02083                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes decrease of enzyme activity at pH 6 and pH 7.|||Decreased autoproteolytic cleavage and strongly reduced enzyme activity with liposome-bound substrate. Loss of enzyme activity with Triton-solubilized substrate.|||Important for enzyme activity|||In isoform 2.|||In isoform 3.|||Loss of autoproteolytic cleavage and loss of enzyme activity.|||Loss of one glycosylation site.|||N-acylethanolamine-hydrolyzing acid amidase|||N-acylethanolamine-hydrolyzing acid amidase subunit alpha|||N-acylethanolamine-hydrolyzing acid amidase subunit beta|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Strongly reduced enzyme activity both with liposome-bound and Triton-solubilized substrate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002318|||http://purl.uniprot.org/annotation/PRO_0000419650|||http://purl.uniprot.org/annotation/PRO_0000419651|||http://purl.uniprot.org/annotation/VAR_028428|||http://purl.uniprot.org/annotation/VAR_048336|||http://purl.uniprot.org/annotation/VAR_048337|||http://purl.uniprot.org/annotation/VSP_000328|||http://purl.uniprot.org/annotation/VSP_000329|||http://purl.uniprot.org/annotation/VSP_000330
http://togogenome.org/gene/9606:DUOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dual oxidase 2|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Found in a patient with very early onset inflammatory bowel disease; unknown pathological significance; no effect on subcellular location; significantly reduced ROS generation, which may decrease resistance to infection by enteric pathogens, such as Escherichia coli.|||Helical|||In TDH6.|||In TDH6; the enzyme is non-functional; expressed at the cell surface of cells albeit at low level.|||Interaction with TXNDC11|||Interchain (with C-167 in DUOXA2)|||Interchain (with C-233 in DUOXA2)|||N-linked (GlcNAc...) asparagine|||Peroxidase-like; mediates peroxidase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223349|||http://purl.uniprot.org/annotation/VAR_025323|||http://purl.uniprot.org/annotation/VAR_025324|||http://purl.uniprot.org/annotation/VAR_025325|||http://purl.uniprot.org/annotation/VAR_047075|||http://purl.uniprot.org/annotation/VAR_061177|||http://purl.uniprot.org/annotation/VAR_064619|||http://purl.uniprot.org/annotation/VAR_075549|||http://purl.uniprot.org/annotation/VAR_075550
http://togogenome.org/gene/9606:PAQR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVX9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane progestin receptor epsilon                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218852
http://togogenome.org/gene/9606:MAP3K7CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0EVZ7|||http://purl.uniprot.org/uniprot/B0EVZ8|||http://purl.uniprot.org/uniprot/B4DFW0|||http://purl.uniprot.org/uniprot/P57077                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MAP3K7 C-terminal-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072423|||http://purl.uniprot.org/annotation/VAR_083830|||http://purl.uniprot.org/annotation/VSP_060759
http://togogenome.org/gene/9606:SYT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||Omega-N-methylarginine|||Synaptotagmin-3|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183945|||http://purl.uniprot.org/annotation/VAR_036389
http://togogenome.org/gene/9606:SERINC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Removed|||Serine incorporator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218966|||http://purl.uniprot.org/annotation/VAR_052275|||http://purl.uniprot.org/annotation/VAR_052276|||http://purl.uniprot.org/annotation/VAR_052277
http://togogenome.org/gene/9606:OTOP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTS6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||Proton channel OTOP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313820|||http://purl.uniprot.org/annotation/VAR_037760|||http://purl.uniprot.org/annotation/VAR_037761
http://togogenome.org/gene/9606:SLAMF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1U5|||http://purl.uniprot.org/uniprot/Q96DU3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes SLAMF6-mediated cytotoxity, disrupts interaction with SH2D1B and retains interaction with SH2D1A.|||Cytoplasmic|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Inhibits dimerization.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Reduced SLAMF6-mediated cytotoxity.|||Retains reduced SLAMF6-mediated cytotoxity, disrupts interaction with SH2D1A and retains interaction with SH2D1B; when associated with F-273.|||Retains reduced SLAMF6-mediated cytotoxity, disrupts interaction with SH2D1A and retains interaction with SH2D1B; when associated with F-309.|||SLAM family member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014961|||http://purl.uniprot.org/annotation/PRO_5002801112|||http://purl.uniprot.org/annotation/VSP_034620|||http://purl.uniprot.org/annotation/VSP_043230
http://togogenome.org/gene/9606:TMEM168                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0V1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a family diagnosed with inherited Brugada syndrome; unknown pathological significance; does not affect nuclear membrane localization. Reduces cardiomyocyte cell surface expression of SCN5A. Decreases in Na(+) current in cardiomyocytes.|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 168                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284630|||http://purl.uniprot.org/annotation/VAR_087377|||http://purl.uniprot.org/annotation/VSP_056846
http://togogenome.org/gene/9606:BBS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFJ9                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 1 protein|||In BBS1.|||In a patient with Bardet-Biedl syndrome.|||In a patient with Meckel-Gruber like syndrome also carrying L-753 in TTC21B and a variant in CC2D2A.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064841|||http://purl.uniprot.org/annotation/VAR_017214|||http://purl.uniprot.org/annotation/VAR_017215|||http://purl.uniprot.org/annotation/VAR_017216|||http://purl.uniprot.org/annotation/VAR_017217|||http://purl.uniprot.org/annotation/VAR_038880|||http://purl.uniprot.org/annotation/VAR_038881|||http://purl.uniprot.org/annotation/VAR_038882|||http://purl.uniprot.org/annotation/VAR_038883|||http://purl.uniprot.org/annotation/VAR_038884|||http://purl.uniprot.org/annotation/VAR_038885|||http://purl.uniprot.org/annotation/VAR_038886|||http://purl.uniprot.org/annotation/VAR_038887|||http://purl.uniprot.org/annotation/VAR_038888|||http://purl.uniprot.org/annotation/VAR_065554|||http://purl.uniprot.org/annotation/VAR_066278|||http://purl.uniprot.org/annotation/VAR_066279|||http://purl.uniprot.org/annotation/VAR_066485|||http://purl.uniprot.org/annotation/VAR_066486|||http://purl.uniprot.org/annotation/VSP_008854|||http://purl.uniprot.org/annotation/VSP_054152|||http://purl.uniprot.org/annotation/VSP_054153
http://togogenome.org/gene/9606:ABHD16A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X777|||http://purl.uniprot.org/uniprot/B3KNX9|||http://purl.uniprot.org/uniprot/O95870                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Cytoplasmic|||Helical|||In SPG86.|||In SPG86; no protein detected in homozygous patient cells; increased levels of phosphatidylserine and decreased levels of lysophosphatidylserine in homozygous patient cells, indicating loss of function in phosphatidylserine catabolism.|||In SPG86; unknown pathological significance.|||In isoform 2.|||Phosphatidylserine lipase ABHD16A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064833|||http://purl.uniprot.org/annotation/VAR_086886|||http://purl.uniprot.org/annotation/VAR_086887|||http://purl.uniprot.org/annotation/VAR_086888|||http://purl.uniprot.org/annotation/VAR_086889|||http://purl.uniprot.org/annotation/VAR_086890|||http://purl.uniprot.org/annotation/VAR_086891|||http://purl.uniprot.org/annotation/VAR_086892|||http://purl.uniprot.org/annotation/VAR_086893|||http://purl.uniprot.org/annotation/VSP_043825
http://togogenome.org/gene/9606:RPUSD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P087                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrial mRNA pseudouridine synthase RPUSD3|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300822|||http://purl.uniprot.org/annotation/VAR_034885|||http://purl.uniprot.org/annotation/VAR_034886|||http://purl.uniprot.org/annotation/VAR_059763|||http://purl.uniprot.org/annotation/VSP_027869|||http://purl.uniprot.org/annotation/VSP_027870
http://togogenome.org/gene/9606:C1QTNF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0INC0|||http://purl.uniprot.org/uniprot/A0A499FIM1|||http://purl.uniprot.org/uniprot/Q9BXJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 2|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003530|||http://purl.uniprot.org/annotation/PRO_5017319562
http://togogenome.org/gene/9606:GCM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75603                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal conserved inhibitory domain (CCID)|||Chorion-specific transcription factor GCMb|||Disordered|||GCM|||In FIH2; abolishes DNA binding ability.|||In FIH2; abolishes normal DNA binding ability of the protein.|||In FIH2; exerts a dominant-negative effect to abolish transactivation capacity.|||In FIH2; the mutation causes loss-of-function; abolishes transactivation capacity despite normal subcellular localization, protein stability and DNA-binding specificity.|||In FIH2; transcription of mRNA, but loss of protein expression.|||In HRPT4; found on the same allele as E-251; gain-of-function mutation; increases transcriptional activity.|||In HRPT4; found on the same allele as Q-379; gain-of-function mutation; increases transcriptional activity.|||In HRPT4; gain-of-function mutation; increases transcriptional activity.|||In HRPT4; unknown pathological significance.|||Shows normal transcriptional activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126650|||http://purl.uniprot.org/annotation/VAR_049130|||http://purl.uniprot.org/annotation/VAR_049131|||http://purl.uniprot.org/annotation/VAR_049132|||http://purl.uniprot.org/annotation/VAR_049133|||http://purl.uniprot.org/annotation/VAR_058044|||http://purl.uniprot.org/annotation/VAR_058045|||http://purl.uniprot.org/annotation/VAR_065495|||http://purl.uniprot.org/annotation/VAR_065496|||http://purl.uniprot.org/annotation/VAR_065497|||http://purl.uniprot.org/annotation/VAR_065498|||http://purl.uniprot.org/annotation/VAR_076838|||http://purl.uniprot.org/annotation/VAR_078579|||http://purl.uniprot.org/annotation/VAR_078580|||http://purl.uniprot.org/annotation/VAR_078581|||http://purl.uniprot.org/annotation/VAR_078582
http://togogenome.org/gene/9606:PSRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0M8|||http://purl.uniprot.org/uniprot/Q6PGN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Disordered|||G2 and S phase-expressed protein 1 N-terminal|||In isoform A and isoform D.|||In isoform B.|||In isoform D.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proline/serine-rich coiled-coil protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273728|||http://purl.uniprot.org/annotation/VAR_051288|||http://purl.uniprot.org/annotation/VSP_022591|||http://purl.uniprot.org/annotation/VSP_022592|||http://purl.uniprot.org/annotation/VSP_022593|||http://purl.uniprot.org/annotation/VSP_022602
http://togogenome.org/gene/9606:TMUB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFQ1|||http://purl.uniprot.org/uniprot/E7ESS3|||http://purl.uniprot.org/uniprot/Q71RG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Transmembrane and ubiquitin-like domain-containing protein 2|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245312|||http://purl.uniprot.org/annotation/VAR_052695|||http://purl.uniprot.org/annotation/VSP_019700|||http://purl.uniprot.org/annotation/VSP_019701|||http://purl.uniprot.org/annotation/VSP_019702|||http://purl.uniprot.org/annotation/VSP_019703|||http://purl.uniprot.org/annotation/VSP_019704
http://togogenome.org/gene/9606:ANO10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW15                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Anoctamin-10|||Cytoplasmic|||Extracellular|||Helical|||In SCAR10.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289957|||http://purl.uniprot.org/annotation/VAR_032638|||http://purl.uniprot.org/annotation/VAR_032639|||http://purl.uniprot.org/annotation/VAR_032640|||http://purl.uniprot.org/annotation/VAR_064888|||http://purl.uniprot.org/annotation/VSP_026033|||http://purl.uniprot.org/annotation/VSP_038211|||http://purl.uniprot.org/annotation/VSP_038212|||http://purl.uniprot.org/annotation/VSP_045885
http://togogenome.org/gene/9606:CEBPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15744                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic motif|||CCAAT/enhancer-binding protein epsilon|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD108; gain-of-function variant resulting in increased DNA-binding transcription factor activity and decreased association with transcriptional repressors.|||In SGD1.|||In SGD1; decreased function in positive regulation of DNA-templated transcription; loss of interaction with GATA1; decreased interaction with SPI1; no effect on localization to nucleus; no effect on DNA binding; no effect on dimerization.|||Leucine-zipper|||Phosphoserine|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076624|||http://purl.uniprot.org/annotation/VAR_078996|||http://purl.uniprot.org/annotation/VAR_087819|||http://purl.uniprot.org/annotation/VAR_087820|||http://purl.uniprot.org/annotation/VAR_087821
http://togogenome.org/gene/9606:MS4A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5J8X5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Membrane-spanning 4-domains subfamily A member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315055|||http://purl.uniprot.org/annotation/VAR_057654|||http://purl.uniprot.org/annotation/VAR_062124|||http://purl.uniprot.org/annotation/VAR_062125|||http://purl.uniprot.org/annotation/VSP_030476|||http://purl.uniprot.org/annotation/VSP_030477
http://togogenome.org/gene/9606:HERC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK41|||http://purl.uniprot.org/uniprot/Q15034                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl thioester intermediate|||HECT|||In isoform 2.|||Probable E3 ubiquitin-protein ligase HERC3|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206651|||http://purl.uniprot.org/annotation/VAR_051729|||http://purl.uniprot.org/annotation/VSP_056343|||http://purl.uniprot.org/annotation/VSP_056344
http://togogenome.org/gene/9606:SLC29A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTT9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Equilibrative nucleoside transporter 4|||Essential for cation selectivity|||Extracellular|||Functional with increased dopamine, serotonin and MPP(+) uptake.|||Functional with slight increased dopamine, serotonin and MPP(+) uptake.|||Helical|||In isoform 2.|||Loss of dopamine, serotonin and MPP(+) uptake.|||Loss of dopamine, serotonin and MPP(+) uptake; gain of uridine transport activity.|||Loss of dopamine, serotonin and MPP(+) uptake; increased uridine uptake.|||Loss of dopamine, serotonin and MPP(+) uptake; no uridine uptake activity.|||Loss of dopamine, serotonin, adenosine and MPP(+) uptake; gain of uridine transport activity.|||N-linked (GlcNAc...) asparagine|||No change in adenosine uptake.|||No change in dopamine, serotonin and MPP(+) uptake; no uridine uptake activity.|||No significant change in dopamine, serotonin and MPP(+) uptake.|||Reduced dopamine, serotonin and MPP(+) uptake.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326251|||http://purl.uniprot.org/annotation/VAR_040044|||http://purl.uniprot.org/annotation/VAR_040045|||http://purl.uniprot.org/annotation/VAR_040046|||http://purl.uniprot.org/annotation/VSP_032647
http://togogenome.org/gene/9606:PLEKHA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R0J1|||http://purl.uniprot.org/uniprot/Q9H4M7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family A member 4|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053880|||http://purl.uniprot.org/annotation/VAR_056667|||http://purl.uniprot.org/annotation/VAR_056668|||http://purl.uniprot.org/annotation/VAR_056669|||http://purl.uniprot.org/annotation/VAR_056670|||http://purl.uniprot.org/annotation/VSP_009770|||http://purl.uniprot.org/annotation/VSP_009771|||http://purl.uniprot.org/annotation/VSP_009772
http://togogenome.org/gene/9606:TAF9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Transcription initiation factor TFIID subunit 9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118891
http://togogenome.org/gene/9606:DHODH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02127                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Dihydroorotate dehydrogenase (quinone), mitochondrial|||Helical|||In POADS.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion; not cleaved|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029884|||http://purl.uniprot.org/annotation/VAR_022094|||http://purl.uniprot.org/annotation/VAR_062412|||http://purl.uniprot.org/annotation/VAR_062413|||http://purl.uniprot.org/annotation/VAR_062414|||http://purl.uniprot.org/annotation/VAR_062415|||http://purl.uniprot.org/annotation/VAR_062416|||http://purl.uniprot.org/annotation/VAR_062417|||http://purl.uniprot.org/annotation/VAR_062418|||http://purl.uniprot.org/annotation/VAR_062419|||http://purl.uniprot.org/annotation/VAR_062420|||http://purl.uniprot.org/annotation/VAR_062421
http://togogenome.org/gene/9606:XCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46094|||http://purl.uniprot.org/uniprot/Q502V0|||http://purl.uniprot.org/uniprot/Q689E2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chemokine XC receptor 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070221
http://togogenome.org/gene/9606:EIF2AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19525|||http://purl.uniprot.org/uniprot/Q8IW76                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Interaction with HCV NS5A|||1|||15-fold decrease in K3L binding affinity and thus resistance of mutated PKR to K3L inhibition.|||2|||2 X 13 AA approximate repeats|||DRBM|||DRBM 1|||DRBM 2|||Dimerization|||Disordered|||Found in a patient with dysmorphic facies, syndactyly, congenital microcephaly and global developmental delay; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Impairs dsRNA binding but not dimerization or activity.|||In DYT33; gain-of-function variant resulting in increased levels of phosphorylated EIF2AK2 and EIF2A in patient cells compared to controls.|||In DYT33; unknown pathological significance.|||In DYT33; unknown pathological significance; gain-of-function variant resulting in increased levels of phosphorylated EIF2AK2 and EIF2A in patient cells compared to controls.|||In FL-PKR-2AI; moderate loss of activity but no effect on dsRNA binding.|||In FL-PKR-2AII; no effect on activity.|||In LEUDEN; unknown pathological significance.|||In LEUDEN; unknown pathological significance; reduced phosphorylation of eukaryotic translation initiation factor 2-alpha in patient cells.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with EIF2S1/EIF-2ALPHA|||Interaction with TRAF5|||Interferon-induced, double-stranded RNA-activated protein kinase|||Loss of PKR inhibition by HCMV protein TRS1.|||Loss of activity.|||Moderate loss of activity.|||Moderate loss of activity; when associated with A-242 and A-255.|||Moderate loss of activity; when associated with A-255 and A-258.|||N-acetylalanine|||No effect on PKR inhibition by HCMV protein TRS1.|||No effect on enzymatic activity; when associated with A-83; A-88 and A-89.|||No effect on enzymatic activity; when associated with A-83; A-88 and A-90.|||No effect on enzymatic activity; when associated with A-83; A-89 and A-90.|||No effect on enzymatic activity; when associated with A-88; A-89 and A-90.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||Significant loss of activity and impairs autophosphorylation of T-451.|||Significant loss of activity; loss of dsRNA binding and dimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085945|||http://purl.uniprot.org/annotation/VAR_040474|||http://purl.uniprot.org/annotation/VAR_040475|||http://purl.uniprot.org/annotation/VAR_040476|||http://purl.uniprot.org/annotation/VAR_084260|||http://purl.uniprot.org/annotation/VAR_084261|||http://purl.uniprot.org/annotation/VAR_084262|||http://purl.uniprot.org/annotation/VAR_084263|||http://purl.uniprot.org/annotation/VAR_084264|||http://purl.uniprot.org/annotation/VAR_084265|||http://purl.uniprot.org/annotation/VAR_084266|||http://purl.uniprot.org/annotation/VAR_084267|||http://purl.uniprot.org/annotation/VAR_084268|||http://purl.uniprot.org/annotation/VAR_086715|||http://purl.uniprot.org/annotation/VAR_086716|||http://purl.uniprot.org/annotation/VAR_086717|||http://purl.uniprot.org/annotation/VSP_046177
http://togogenome.org/gene/9606:ENGASE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BRCT|||Basic and acidic residues|||Cytosolic endo-beta-N-acetylglucosaminidase|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328867|||http://purl.uniprot.org/annotation/VAR_060188|||http://purl.uniprot.org/annotation/VAR_060189|||http://purl.uniprot.org/annotation/VSP_032835|||http://purl.uniprot.org/annotation/VSP_032836|||http://purl.uniprot.org/annotation/VSP_032837|||http://purl.uniprot.org/annotation/VSP_032838
http://togogenome.org/gene/9606:ZNF619                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RW3|||http://purl.uniprot.org/uniprot/Q8N2I2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Zinc finger protein 619                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234601|||http://purl.uniprot.org/annotation/VSP_043080|||http://purl.uniprot.org/annotation/VSP_055715|||http://purl.uniprot.org/annotation/VSP_055716
http://togogenome.org/gene/9606:CASP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49662                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-riboxanated arginine|||Abolished ability to cleave Gasdermin-D (GSDMD).|||Abolished autoprocessing and ability to form a heterotetramer composed of Caspase-4 subunit p10 and Caspase-4 subunit p20, preventing ability to cleave GSDMD and induce pyroptosis.|||Abolished interaction with Gasdermin-D (GSDMD) and ability to mediate its cleavage.|||CARD|||Caspase-4 subunit p10|||Caspase-4 subunit p20|||Cleavage; by autolysis|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of autocatalysis.|||Loss of enzymatic activity. Loss of LPS-induced pyroptosis. No effect on the interaction with LPS. Decrease in cell death induced by TMEM214 overexpression. Does not support IL1B and IL18 secretion following UVB irradiation.|||N-acetylalanine|||Phosphoserine|||Removed|||Required for LPS-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004596|||http://purl.uniprot.org/annotation/PRO_0000004597|||http://purl.uniprot.org/annotation/PRO_0000004598|||http://purl.uniprot.org/annotation/PRO_0000004599|||http://purl.uniprot.org/annotation/VAR_061081|||http://purl.uniprot.org/annotation/VAR_061082|||http://purl.uniprot.org/annotation/VAR_075654|||http://purl.uniprot.org/annotation/VSP_043495|||http://purl.uniprot.org/annotation/VSP_058177|||http://purl.uniprot.org/annotation/VSP_058178|||http://purl.uniprot.org/annotation/VSP_058179|||http://purl.uniprot.org/annotation/VSP_058180|||http://purl.uniprot.org/annotation/VSP_058181|||http://purl.uniprot.org/annotation/VSP_058182
http://togogenome.org/gene/9606:STC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52823                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Stanniocalcin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033297|||http://purl.uniprot.org/annotation/PRO_0000033298|||http://purl.uniprot.org/annotation/VSP_057169
http://togogenome.org/gene/9606:PTPRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6H0|||http://purl.uniprot.org/uniprot/O14522                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Found in a patient with severe intellectual disability, behavioral problems, microcephaly, congenital cardiac defect and herniation of the abdominal diaphragm; also observed in some colorectal cancers; reduced phosphatase activity; unknown pathological significance.|||Helical|||Ig-like|||Ig-like C2-type|||In a colorectal cancer.|||In a colorectal cancer; reduced phosphatase activity.|||In a gastric cancer.|||In a lung cancer.|||In a lung cancer; reduced phosphatase activity.|||In an acute myeloid leukemia sample; somatic mutation.|||In isoform 1.|||In some colorectal cancers.|||MAM|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Receptor-type tyrosine-protein phosphatase T|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025463|||http://purl.uniprot.org/annotation/PRO_5001705160|||http://purl.uniprot.org/annotation/VAR_020746|||http://purl.uniprot.org/annotation/VAR_020747|||http://purl.uniprot.org/annotation/VAR_020748|||http://purl.uniprot.org/annotation/VAR_020749|||http://purl.uniprot.org/annotation/VAR_020750|||http://purl.uniprot.org/annotation/VAR_020751|||http://purl.uniprot.org/annotation/VAR_020752|||http://purl.uniprot.org/annotation/VAR_020753|||http://purl.uniprot.org/annotation/VAR_020754|||http://purl.uniprot.org/annotation/VAR_020755|||http://purl.uniprot.org/annotation/VAR_020756|||http://purl.uniprot.org/annotation/VAR_020757|||http://purl.uniprot.org/annotation/VAR_020758|||http://purl.uniprot.org/annotation/VAR_020759|||http://purl.uniprot.org/annotation/VAR_020760|||http://purl.uniprot.org/annotation/VAR_020761|||http://purl.uniprot.org/annotation/VAR_020762|||http://purl.uniprot.org/annotation/VAR_020763|||http://purl.uniprot.org/annotation/VAR_020764|||http://purl.uniprot.org/annotation/VAR_020765|||http://purl.uniprot.org/annotation/VAR_020766|||http://purl.uniprot.org/annotation/VAR_020767|||http://purl.uniprot.org/annotation/VAR_020768|||http://purl.uniprot.org/annotation/VAR_020769|||http://purl.uniprot.org/annotation/VAR_020770|||http://purl.uniprot.org/annotation/VAR_028795|||http://purl.uniprot.org/annotation/VAR_028796|||http://purl.uniprot.org/annotation/VAR_054144|||http://purl.uniprot.org/annotation/VSP_040385|||http://purl.uniprot.org/annotation/VSP_040386
http://togogenome.org/gene/9606:OR11H12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RN74                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11H12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344798
http://togogenome.org/gene/9606:KBTBD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JR72                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  BTB|||In NEM6.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393906|||http://purl.uniprot.org/annotation/VAR_064889|||http://purl.uniprot.org/annotation/VAR_064890|||http://purl.uniprot.org/annotation/VAR_064891
http://togogenome.org/gene/9606:ETFDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEQ0|||http://purl.uniprot.org/uniprot/Q16134                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  4Fe-4S ferredoxin-type|||Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial|||In GA2C.|||In GA2C; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008661|||http://purl.uniprot.org/annotation/VAR_036134|||http://purl.uniprot.org/annotation/VAR_055711|||http://purl.uniprot.org/annotation/VAR_062966|||http://purl.uniprot.org/annotation/VAR_075438|||http://purl.uniprot.org/annotation/VAR_075439|||http://purl.uniprot.org/annotation/VAR_075440|||http://purl.uniprot.org/annotation/VAR_075441|||http://purl.uniprot.org/annotation/VAR_075442|||http://purl.uniprot.org/annotation/VAR_075443|||http://purl.uniprot.org/annotation/VAR_075444|||http://purl.uniprot.org/annotation/VAR_075445|||http://purl.uniprot.org/annotation/VAR_075446|||http://purl.uniprot.org/annotation/VAR_075447|||http://purl.uniprot.org/annotation/VAR_075448|||http://purl.uniprot.org/annotation/VAR_075449|||http://purl.uniprot.org/annotation/VAR_075450|||http://purl.uniprot.org/annotation/VAR_075451|||http://purl.uniprot.org/annotation/VAR_075452|||http://purl.uniprot.org/annotation/VAR_075453|||http://purl.uniprot.org/annotation/VAR_075454|||http://purl.uniprot.org/annotation/VAR_075455|||http://purl.uniprot.org/annotation/VAR_075456|||http://purl.uniprot.org/annotation/VAR_075457|||http://purl.uniprot.org/annotation/VAR_075458|||http://purl.uniprot.org/annotation/VAR_075459|||http://purl.uniprot.org/annotation/VAR_075460|||http://purl.uniprot.org/annotation/VSP_055158
http://togogenome.org/gene/9606:ZNF99                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXY4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; degenerate|||C2H2-type 9|||KRAB|||Zinc finger protein 99                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000429127|||http://purl.uniprot.org/annotation/VAR_044501|||http://purl.uniprot.org/annotation/VAR_061935
http://togogenome.org/gene/9606:LORICRIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23490                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-312)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-89)|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-154); alternate|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-212); alternate|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-213); alternate|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-216); alternate|||Loricrin|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084458|||http://purl.uniprot.org/annotation/VAR_047712|||http://purl.uniprot.org/annotation/VAR_061676|||http://purl.uniprot.org/annotation/VAR_065891
http://togogenome.org/gene/9606:NFYA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23511                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform Short.|||NFYA/HAP2-type|||Nuclear transcription factor Y subunit alpha|||Phosphoserine|||Subunit association domain (SAD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198768|||http://purl.uniprot.org/annotation/VSP_000849
http://togogenome.org/gene/9606:KANSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9L4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KAT8 regulatory NSL complex subunit 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278292|||http://purl.uniprot.org/annotation/VAR_030767|||http://purl.uniprot.org/annotation/VAR_030768|||http://purl.uniprot.org/annotation/VSP_042530|||http://purl.uniprot.org/annotation/VSP_042531
http://togogenome.org/gene/9606:PFKM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0Y5|||http://purl.uniprot.org/uniprot/A0A2R8Y891|||http://purl.uniprot.org/uniprot/P08237                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent 6-phosphofructokinase, muscle type|||C-terminal regulatory PFK domain 2|||Disordered|||In GSD7; Ashkenazi.|||In GSD7; Italian.|||In GSD7; Japanese.|||In GSD7; Spanish; complete loss of enzyme activity.|||In GSD7; loss of activity shown by complementation assays in yeast.|||In isoform 2.|||In isoform 3.|||Interdomain linker|||N-acetylthreonine|||N-terminal catalytic PFK domain 1|||N6-(2-hydroxyisobutyryl)lysine|||O-linked (GlcNAc) serine|||Phosphofructokinase|||Phosphoserine|||Proton acceptor|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112016|||http://purl.uniprot.org/annotation/VAR_006063|||http://purl.uniprot.org/annotation/VAR_006064|||http://purl.uniprot.org/annotation/VAR_006065|||http://purl.uniprot.org/annotation/VAR_006066|||http://purl.uniprot.org/annotation/VAR_006067|||http://purl.uniprot.org/annotation/VAR_006068|||http://purl.uniprot.org/annotation/VAR_006069|||http://purl.uniprot.org/annotation/VAR_072239|||http://purl.uniprot.org/annotation/VAR_072240|||http://purl.uniprot.org/annotation/VAR_072241|||http://purl.uniprot.org/annotation/VAR_072242|||http://purl.uniprot.org/annotation/VSP_004667|||http://purl.uniprot.org/annotation/VSP_046125
http://togogenome.org/gene/9606:CLCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXK0|||http://purl.uniprot.org/uniprot/P51790                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CBS|||CBS 1|||CBS 2|||Changes channel selectivity from I(-)>Cl(-) to Cl(-)>I(-).|||Cytoplasmic|||Di-leucine internalization motif; mediates targeting to late endosome and lysosome membranes|||H(+)/Cl(-) exchange transporter 3|||Helical|||In NEDHYBA.|||In NEDHYBA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport|||Mediates proton transfer from the protein to the inner aqueous phase|||N-linked (GlcNAc...) asparagine|||Note=Loop between two helices|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094438|||http://purl.uniprot.org/annotation/VAR_086219|||http://purl.uniprot.org/annotation/VAR_086220|||http://purl.uniprot.org/annotation/VAR_086221|||http://purl.uniprot.org/annotation/VAR_086222|||http://purl.uniprot.org/annotation/VAR_086223|||http://purl.uniprot.org/annotation/VAR_086224|||http://purl.uniprot.org/annotation/VAR_086225|||http://purl.uniprot.org/annotation/VAR_086226|||http://purl.uniprot.org/annotation/VSP_016073|||http://purl.uniprot.org/annotation/VSP_045105|||http://purl.uniprot.org/annotation/VSP_054415
http://togogenome.org/gene/9606:TOPORS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abrogates E3 ubiquitin-protein ligase activity.|||Basic and acidic residues|||Basic residues|||Disordered|||E3 ubiquitin-protein ligase Topors|||E3 ubiquitin-protein ligase activity|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Increase in E3 ubiquitin-protein ligase activity and increased binding to UBE2D1. No effect on SUMO1-protein ligase activity.|||Interaction with SUMO1|||Interaction with TOP1|||Interaction with UBE2I|||Interaction with p53/TP53|||Loss of phosphorylation but no effect on E3 ubiquitin-protein ligase activity.|||Loss of phosphorylation by PLK1 and increases in p53/TP53 stability.|||No effect on sumoylation.|||Phosphoserine|||Phosphoserine; by PLK1|||Polar residues|||RING-type|||Required for DNA-binding|||Required for sumoylation and localization to discrete nuclear foci|||Strongly reduces sumoylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232626|||http://purl.uniprot.org/annotation/VAR_037629|||http://purl.uniprot.org/annotation/VAR_037630|||http://purl.uniprot.org/annotation/VAR_037631|||http://purl.uniprot.org/annotation/VAR_037632|||http://purl.uniprot.org/annotation/VSP_017916|||http://purl.uniprot.org/annotation/VSP_017917
http://togogenome.org/gene/9606:ADRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08588                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1 adrenergic receptor|||Common variant associated with low mean resting heart rate; associated with decreased mortality risk in patients with congestive heart failure.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increased beta1-adrenergic receptor activity; increased basal activity and increased coupling to heterotrimeric G protein Gs that stimulates the adenylyl cyclase.|||Loss of interaction with GOPC.|||Loss of interaction with GOPC. Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation.|||Loss of interaction with GOPC; when associated with A-477.|||Loss of interaction with RAPGEF2.|||Loss of interaction with RAPGEF2. Abolishes agonist-induced Ras activation.|||N-linked (GlcNAc...) asparagine|||PDZ-Binding|||Partial loss of interaction with GOPC.|||Phosphoserine|||Phosphoserine; by PKA|||Pro residues|||Rare variant associated with short sleep; results in decreased adenylate cyclase-activating adrenergic receptor signaling; decreased protein stability.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069118|||http://purl.uniprot.org/annotation/VAR_009879|||http://purl.uniprot.org/annotation/VAR_009880|||http://purl.uniprot.org/annotation/VAR_055909|||http://purl.uniprot.org/annotation/VAR_055910|||http://purl.uniprot.org/annotation/VAR_055911|||http://purl.uniprot.org/annotation/VAR_055912|||http://purl.uniprot.org/annotation/VAR_055913|||http://purl.uniprot.org/annotation/VAR_082587
http://togogenome.org/gene/9606:PORCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H237                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Drastic loss of palmitoylation.|||Extracellular|||Helical|||In FODH.|||In a patient with focal dermal hypoplasia also carrying a frameshift mutation; uncertain pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Loss of function.|||Protein-serine O-palmitoleoyltransferase porcupine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213137|||http://purl.uniprot.org/annotation/VAR_035089|||http://purl.uniprot.org/annotation/VAR_035090|||http://purl.uniprot.org/annotation/VAR_058899|||http://purl.uniprot.org/annotation/VAR_058900|||http://purl.uniprot.org/annotation/VAR_058901|||http://purl.uniprot.org/annotation/VAR_058902|||http://purl.uniprot.org/annotation/VAR_058903|||http://purl.uniprot.org/annotation/VAR_058904|||http://purl.uniprot.org/annotation/VAR_058905|||http://purl.uniprot.org/annotation/VAR_058906|||http://purl.uniprot.org/annotation/VAR_065189|||http://purl.uniprot.org/annotation/VAR_065190|||http://purl.uniprot.org/annotation/VAR_065191|||http://purl.uniprot.org/annotation/VAR_065192|||http://purl.uniprot.org/annotation/VAR_065193|||http://purl.uniprot.org/annotation/VAR_066061|||http://purl.uniprot.org/annotation/VSP_015886|||http://purl.uniprot.org/annotation/VSP_015887|||http://purl.uniprot.org/annotation/VSP_015888|||http://purl.uniprot.org/annotation/VSP_055419
http://togogenome.org/gene/9606:OR5B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R09                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150585|||http://purl.uniprot.org/annotation/VAR_053181|||http://purl.uniprot.org/annotation/VAR_053182
http://togogenome.org/gene/9606:XPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23025                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  DNA repair protein complementing XP-A cells|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In XP-A.|||In XP-A; mild form.|||In XP-A; severe form.|||Interaction with CEP164 and required for UV resistance|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208648|||http://purl.uniprot.org/annotation/VAR_007727|||http://purl.uniprot.org/annotation/VAR_007728|||http://purl.uniprot.org/annotation/VAR_007729|||http://purl.uniprot.org/annotation/VAR_007730|||http://purl.uniprot.org/annotation/VAR_007731|||http://purl.uniprot.org/annotation/VAR_014203|||http://purl.uniprot.org/annotation/VAR_014799|||http://purl.uniprot.org/annotation/VAR_020324|||http://purl.uniprot.org/annotation/VAR_029325|||http://purl.uniprot.org/annotation/VAR_037907|||http://purl.uniprot.org/annotation/VAR_061987
http://togogenome.org/gene/9606:GCFC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4UHR0|||http://purl.uniprot.org/uniprot/B3KUM5|||http://purl.uniprot.org/uniprot/P16383|||http://purl.uniprot.org/uniprot/Q9BVX3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GCF C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Intron Large complex component GCFC2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087441|||http://purl.uniprot.org/annotation/VAR_051005|||http://purl.uniprot.org/annotation/VAR_051006|||http://purl.uniprot.org/annotation/VAR_051007|||http://purl.uniprot.org/annotation/VAR_051008|||http://purl.uniprot.org/annotation/VAR_051009|||http://purl.uniprot.org/annotation/VSP_021798|||http://purl.uniprot.org/annotation/VSP_054362|||http://purl.uniprot.org/annotation/VSP_054363|||http://purl.uniprot.org/annotation/VSP_057398|||http://purl.uniprot.org/annotation/VSP_057399
http://togogenome.org/gene/9606:SCN1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35498                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with autism.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a child with developmental disabilities; unknown pathological significance.|||Found in a child with sporadic epilepsy; unknown pathological significance.|||Found in a patient acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance.|||Found in a patient with acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance.|||Found in a patient with an unclassified form of epilepsy; also found in a patient with epilepsy-aphasia and febrile seizures plus; unknown pathological significance.|||Found in a patient with autism; unknown pathological significance.|||Found in a patient with epilepsy-aphasia and febrile seizures plus; unknown pathological significance.|||Found in a patient with febrile seizures and non-specific acute encephalopathy; unknown pathological significance.|||Found in a patient with infantile epileptic spasms also carrying a PLPPR4 variant; unknown pathological significance.|||Found in a patient with intractable epilepsy and in a patient with generalized epilepsy with febril seizures; also found in patients with autism; unknown pathological significance.|||Found in a patient with intractable epilepsy and patients with Dravet syndrome; found in a patient with acute necrotizing encephalopathy and also found in a patient with acute encephalopathy with biphasic seizures and late reduced diffusion; unknown pathological significance.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IQ|||IV|||In DEE6B.|||In DRVT and GEFSP2.|||In DRVT and GEFSP2; GEFSP2 phenotype consists of partial epilepsy with antecedent febrile seizures and seizure aggravation by antiepileptic drugs; loss-of-function mutation resulting in complete absence of sodium current.|||In DRVT and ICEGTC.|||In DRVT and ICEGTC; borderline DRVT phenotype.|||In DRVT and ICEGTC; results in a non-functional channel.|||In DRVT.|||In DRVT; also found in a child with febrile status epilepticus who developed liver failure.|||In DRVT; also found in a patient with an unclassified form of epilepsy.|||In DRVT; also found in a patient with cryptogenic focal epilepsy.|||In DRVT; also found in a patient with cryptogenic generalized epilepsy.|||In DRVT; also in a patient with myoclonic astatic epilepsy.|||In DRVT; borderline phenotype in some patients.|||In DRVT; borderline phenotype with spike wave activity in some patients.|||In DRVT; borderline phenotype with spike wave activity in some patients; results in a non-functional channel.|||In DRVT; borderline phenotype with spike wave activity.|||In DRVT; borderline phenotype.|||In DRVT; borderline phenotype; also found in a patient with focal epilepsy.|||In DRVT; complete loss of sodium ion transmembrane transport.|||In DRVT; functional channel displaying decreased peak current densities but increased persistent current.|||In DRVT; loss-of-function mutation resulting in complete absence of sodium current.|||In DRVT; results in a non-functional channel.|||In DRVT; results in decreased peak current densities; causes a negative shift in the half-maximal steady-state inactivation and delayed recovery from fast inactivation.|||In DRVT; results in impaired channel fast inactivation and significantly increased persistent current.|||In DRVT; some patients have a borderline DRVT phenotype.|||In DRVT; unknown pathological significance.|||In FEB3A; also found in patients with early infantile epileptic encephalopathy; unknown pathological significance.|||In FEB3A; loss of function.|||In FHM3.|||In GEFSP2 and DRVT.|||In GEFSP2 and DRVT; borderline phenotype.|||In GEFSP2 and DRVT; causes a positive shift in the voltage dependence of channel activation, slower recovery from slow inactivation and lower levels of current compared with the wild-type channel.|||In GEFSP2 and ICEGTC.|||In GEFSP2.|||In GEFSP2; also found in patients with Panayiotopoulos syndrome.|||In GEFSP2; causes a positive shift in the voltage dependence of sodium channel fast inactivation; causes an increase in the magnitude of the persistent current; causes delay in the kinetics of inactivation and significantly reduces interaction with SCN1B.|||In GEFSP2; causes hyperpolarized shifts in the voltage dependence of activation and steady-state inactivation.|||In GEFSP2; changed voltage-gated sodium channel activity; exhibits a depolarizing shift in the voltage dependence of activation.|||In GEFSP2; changed voltage-gated sodium channel activity; exhibits a depolarizing shift in the voltage dependence of activation; shows a 50% reduction in current density and accelerates recovery from slow inactivation.|||In GEFSP2; complete loss of sodium ion transmembrane transport.|||In GEFSP2; disease phenotype consists of partial epilepsy with antecedent febrile seizures and seizure aggravation by antiepileptic drugs; loss-of-function mutation resulting in complete absence of sodium current.|||In GEFSP2; loss of function; defective trafficking to cell membrane and no inhibition of its interaction with SCN1B.|||In GEFSP2; results in impaired channel fast inactivation and significantly increased persistent current.|||In GEFSP2; unknown pathological significance.|||In ICEGTC and DRVT.|||In ICEGTC.|||In ICEGTC; loss-of-function mutation resulting in absence of sodium current.|||In ICEGTC; reduced function; decreased peak current density; results in a negative shift of inactivation and positive shift of activation.|||In ICEGTC; results in decreased peak current density but significantly greater levels of persistent non-inactivating current compared to wild-type channel.|||In ICEGTC; results in greater levels of persistent non-inactivating current compared to wild-type.|||In ICEGTC; results in increased peak current density and delayed slow inactivation onset; recovery from slow inactivation is delayed.|||In ICEGTC; results in reduced peak current density and hyperpolarizing shift in inactivation.|||In a patient with cryptogenic focal epilepsy.|||In infantile spasms.|||In isoform 2.|||In isoform 3.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||Key residue that permits the spider beta/delta-theraphotoxin-Pre1a to inhibit fast inactivation of the channel|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Probable disease-associated variant found in a patient with Lennon-Gastaut syndrome.|||Probable disease-associated variant found in a patient with an unclassified form of epilepsy.|||Probable disease-associated variant found in a patient with cryptogenic focal epilepsy.|||Probable disease-associated variant found in a patient with cryptogenic generalized epilepsy.|||Probable disease-associated variant found in a patient with drug-resistant epilepsy and mild cognitive impairment.|||Probable disease-associated variant found in a patient with myoclonic astatic epilepsy.|||Probable disease-associated variant found in patients with Panayiotopoulos syndrome.|||S1-S2 loop of repeat IV|||S3b-S4 loop of repeat IV|||Sodium channel protein type 1 subunit alpha ^@                                                                                  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org/annotation/VAR_073547|||http://purl.uniprot.org/annotation/VAR_073548|||http://purl.uniprot.org/annotation/VAR_073549|||http://purl.uniprot.org/annotation/VAR_073550|||http://purl.uniprot.org/annotation/VAR_073551|||http://purl.uniprot.org/annotation/VAR_073552|||http://purl.uniprot.org/annotation/VAR_073553|||http://purl.uniprot.org/annotation/VAR_073554|||http://purl.uniprot.org/annotation/VAR_073555|||http://purl.uniprot.org/annotation/VAR_073556|||http://purl.uniprot.org/annotation/VAR_073557|||http://purl.uniprot.org/annotation/VAR_073558|||http://purl.uniprot.org/annotation/VAR_073559|||http://purl.uniprot.org/annotation/VAR_073560|||http://purl.uniprot.org/annotation/VAR_073561|||http://purl.uniprot.org/annotation/VAR_073562|||http://purl.uniprot.org/annotation/VAR_073563|||http://purl.uniprot.org/annotation/VAR_073564|||http://purl.uniprot.org/annotation/VAR_073565|||http://purl.uniprot.org/annotation/VAR_073566|||http://purl.uniprot.org/annotation/VAR_073567|||http://purl.uniprot.org/annotation/VAR_073568|||http://purl.uniprot.org/annotation/VAR_073569|||http://purl.uniprot.org/annotation/VAR_073570|||http://purl.uniprot.org/annotation/VAR_073571|||http://purl.uniprot.org/annotation/VAR_073572|||http://purl.uniprot.org/annotation/VAR_073573|||http://purl.uniprot.org/annotation/VAR_073574|||http://purl.uniprot.org/annotation/VAR_073575|||http://purl.uniprot.org/annotation/VAR_073576|||http://purl.uniprot.org/annotation/VAR_073577|||http://purl.uniprot.org/annotation/VAR_073578|||http://purl.uniprot.org/annotation/VAR_073579|||http://purl.uniprot.org/annotation/VAR_073580|||http://purl.uniprot.org/annotation/VAR_073581|||http://purl.uniprot.org/annotation/VAR_073582|||http://purl.uniprot.org/annotation/VAR_073583|||http://purl.uniprot.org/annotation/VAR_073584|||http://purl.uniprot.org/annotation/VAR_073585|||http://purl.uniprot.org/annotation/VAR_073586|||http://purl.uniprot.org/annotation/VAR_073587|||http://purl.uniprot.org/annotation/VAR_073588|||http://purl.uniprot.org/annotation/VAR_073589|||http://purl.uniprot.org/annotation/VAR_073590|||http://purl.uniprot.org/annotation/VAR_073591|||http://purl.uniprot.org/annotation/VAR_073592|||http://purl.uniprot.org/annotation/VAR_073593|||http://purl.uniprot.org/annotation/VAR_073594|||http://purl.uniprot.org/annotation/VAR_073595|||http://purl.uniprot.org/annotation/VAR_073596|||http://purl.uniprot.org/annotation/VAR_073597|||http://purl.uniprot.org/annotation/VAR_073598|||http://purl.uniprot.org/annotation/VAR_073599|||http://purl.uniprot.org/annotation/VAR_073600|||http://purl.uniprot.org/annotation/VAR_073601|||http://purl.uniprot.org/annotation/VAR_073602|||http://purl.uniprot.org/annotation/VAR_073603|||http://purl.uniprot.org/annotation/VAR_073604|||http://purl.uniprot.org/annotation/VAR_073605|||http://purl.uniprot.org/annotation/VAR_073606|||http://purl.uniprot.org/annotation/VAR_073607|||http://purl.uniprot.org/annotation/VAR_073608|||http://purl.uniprot.org/annotation/VAR_073609|||http://purl.uniprot.org/annotation/VAR_073610|||http://purl.uniprot.org/annotation/VAR_073611|||http://purl.uniprot.org/annotation/VAR_073612|||http://purl.uniprot.org/annotation/VAR_073613|||http://purl.uniprot.org/annotation/VAR_073614|||http://purl.uniprot.org/annotation/VAR_073615|||http://purl.uniprot.org/annotation/VAR_073616|||http://purl.uniprot.org/annotation/VAR_073617|||http://purl.uniprot.org/annotation/VAR_073618|||http://purl.uniprot.org/annotation/VAR_073619|||http://purl.uniprot.org/annotation/VAR_073620|||http://purl.uniprot.org/annotation/VAR_073621|||http://purl.uniprot.org/annotation/VAR_073622|||http://purl.uniprot.org/annotation/VAR_073623|||http://purl.uniprot.org/annotation/VAR_073624|||http://purl.uniprot.org/annotation/VAR_073625|||http://purl.uniprot.org/annotation/VAR_073626|||http://purl.uniprot.org/annotation/VAR_073627|||http://purl.uniprot.org/annotation/VAR_073628|||http://purl.uniprot.org/annotation/VAR_073629|||http://purl.uniprot.org/annotation/VAR_073630|||http://purl.uniprot.org/annotation/VAR_073631|||http://purl.uniprot.org/annotation/VAR_073632|||http://purl.uniprot.org/annotation/VAR_073633|||http://purl.uniprot.org/annotation/VAR_073634|||http://purl.uniprot.org/annotation/VAR_073635|||http://purl.uniprot.org/annotation/VAR_073636|||http://purl.uniprot.org/annotation/VAR_073637|||http://purl.uniprot.org/annotation/VAR_073638|||http://purl.uniprot.org/annotation/VAR_073639|||http://purl.uniprot.org/annotation/VAR_073640|||http://purl.uniprot.org/annotation/VAR_073641|||http://purl.uniprot.org/annotation/VAR_073642|||http://purl.uniprot.org/annotation/VAR_073643|||http://purl.uniprot.org/annotation/VAR_073644|||http://purl.uniprot.org/annotation/VAR_073645|||http://purl.uniprot.org/annotation/VAR_073646|||http://purl.uniprot.org/annotation/VAR_073647|||http://purl.uniprot.org/annotation/VAR_073648|||http://purl.uniprot.org/annotation/VAR_073649|||http://purl.uniprot.org/annotation/VAR_073650|||http://purl.uniprot.org/annotation/VAR_073651|||http://purl.uniprot.org/annotation/VAR_073652|||http://purl.uniprot.org/annotation/VAR_073653|||http://purl.uniprot.org/annotation/VAR_073654|||http://purl.uniprot.org/annotation/VAR_073655|||http://purl.uniprot.org/annotation/VAR_073656|||http://purl.uniprot.org/annotation/VAR_075569|||http://purl.uniprot.org/annotation/VAR_075570|||http://purl.uniprot.org/annotation/VAR_075571|||http://purl.uniprot.org/annotation/VAR_077831|||http://purl.uniprot.org/annotation/VAR_078192|||http://purl.uniprot.org/annotation/VAR_078193|||http://purl.uniprot.org/annotation/VAR_078194|||http://purl.uniprot.org/annotation/VAR_078611|||http://purl.uniprot.org/annotation/VAR_078725|||http://purl.uniprot.org/annotation/VAR_078726|||http://purl.uniprot.org/annotation/VAR_078727|||http://purl.uniprot.org/annotation/VAR_078728|||http://purl.uniprot.org/annotation/VAR_078729|||http://purl.uniprot.org/annotation/VAR_085768|||http://purl.uniprot.org/annotation/VAR_085926|||http://purl.uniprot.org/annotation/VAR_085927|||http://purl.uniprot.org/annotation/VAR_085928|||http://purl.uniprot.org/annotation/VAR_085929|||http://purl.uniprot.org/annotation/VAR_085930|||http://purl.uniprot.org/annotation/VAR_088154|||http://purl.uniprot.org/annotation/VSP_001031|||http://purl.uniprot.org/annotation/VSP_045399
http://togogenome.org/gene/9606:TRIM52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KQM7|||http://purl.uniprot.org/uniprot/A0A8I5KRY2|||http://purl.uniprot.org/uniprot/A0A8I5KW90|||http://purl.uniprot.org/uniprot/A0A8I5KXQ2|||http://purl.uniprot.org/uniprot/A0A8I5KYD8|||http://purl.uniprot.org/uniprot/Q96A61                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||E3 ubiquitin-protein ligase TRIM52|||Important for rapid proteolytic degradation by the proteasome|||In isoform 2.|||RING-type|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056280|||http://purl.uniprot.org/annotation/VSP_060452|||http://purl.uniprot.org/annotation/VSP_060453
http://togogenome.org/gene/9606:BRSK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDC3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes activation of kinase activity.|||Basic and acidic residues|||Disordered|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of kinase activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase BRSK1|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085669|||http://purl.uniprot.org/annotation/VAR_040394|||http://purl.uniprot.org/annotation/VAR_040395|||http://purl.uniprot.org/annotation/VAR_040396|||http://purl.uniprot.org/annotation/VAR_040397|||http://purl.uniprot.org/annotation/VAR_040398|||http://purl.uniprot.org/annotation/VAR_040399|||http://purl.uniprot.org/annotation/VSP_008158|||http://purl.uniprot.org/annotation/VSP_041742
http://togogenome.org/gene/9606:CAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DPU2|||http://purl.uniprot.org/uniprot/Q01518                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylyl cyclase-associated protein 1|||C-CAP/cofactor C-like|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205696|||http://purl.uniprot.org/annotation/VAR_028419|||http://purl.uniprot.org/annotation/VAR_028420|||http://purl.uniprot.org/annotation/VAR_028421|||http://purl.uniprot.org/annotation/VAR_028422|||http://purl.uniprot.org/annotation/VAR_028423|||http://purl.uniprot.org/annotation/VAR_028424|||http://purl.uniprot.org/annotation/VSP_036038
http://togogenome.org/gene/9606:DCAF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBB7|||http://purl.uniprot.org/uniprot/Q96JK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DDB1- and CUL4-associated factor 5|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051369|||http://purl.uniprot.org/annotation/VSP_010386|||http://purl.uniprot.org/annotation/VSP_055647
http://togogenome.org/gene/9606:ATP5F1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06576|||http://purl.uniprot.org/uniprot/V9HW31                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  AAA+ ATPase|||ATP synthase subunit beta, mitochondrial|||In HUMOP2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002443|||http://purl.uniprot.org/annotation/VAR_048371|||http://purl.uniprot.org/annotation/VAR_074188|||http://purl.uniprot.org/annotation/VAR_087864
http://togogenome.org/gene/9606:KNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01042                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Peptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  4-hydroxyproline; partial|||Basic and acidic residues|||Basic residues|||Bradykinin|||Cleavage; by ACE|||Cleavage; by kallikrein|||Cystatin kininogen-type 1|||Cystatin kininogen-type 2|||Cystatin kininogen-type 3|||Disordered|||In HAE6.|||In HAE6; unknown pathological significance.|||In T-kinin peptide.|||In isoform 3.|||In isoform LMW.|||Interchain (between heavy and light chains)|||Kininogen-1|||Kininogen-1 heavy chain|||Kininogen-1 light chain|||Low molecular weight growth-promoting factor|||Lysyl-bradykinin|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-glycosylated at one site only|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine; by FAM20C|||Polar residues|||Pyrrolidone carboxylic acid; in mature form|||T-kinin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006685|||http://purl.uniprot.org/annotation/PRO_0000006686|||http://purl.uniprot.org/annotation/PRO_0000006687|||http://purl.uniprot.org/annotation/PRO_0000006688|||http://purl.uniprot.org/annotation/PRO_0000006689|||http://purl.uniprot.org/annotation/PRO_0000006690|||http://purl.uniprot.org/annotation/PRO_0000372485|||http://purl.uniprot.org/annotation/VAR_019277|||http://purl.uniprot.org/annotation/VAR_019278|||http://purl.uniprot.org/annotation/VAR_019279|||http://purl.uniprot.org/annotation/VAR_028937|||http://purl.uniprot.org/annotation/VAR_048853|||http://purl.uniprot.org/annotation/VAR_048854|||http://purl.uniprot.org/annotation/VAR_048855|||http://purl.uniprot.org/annotation/VAR_055233|||http://purl.uniprot.org/annotation/VAR_085817|||http://purl.uniprot.org/annotation/VAR_085818|||http://purl.uniprot.org/annotation/VSP_001261|||http://purl.uniprot.org/annotation/VSP_001262|||http://purl.uniprot.org/annotation/VSP_047307|||http://purl.uniprot.org/annotation/VSP_047308
http://togogenome.org/gene/9606:NAA15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBE5|||http://purl.uniprot.org/uniprot/Q9BXJ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Disordered|||In MRD50.|||In MRD50; unknown pathological significance.|||In isoform 2.|||Interaction with HYPK|||N-alpha-acetyltransferase 15, NatA auxiliary subunit|||N6-acetyllysine|||Phosphoserine|||Reduces NatA complex stability and reduces catalytic activity.|||Reduces binding to HYPK, increases binding to NAA50. Increases catalytic activity of the NatA complex while retaining the interaction with NAA10.|||Reduces binding to NAA50, but increases binding to HYPK. Reduces catalytic activity of the NatA complex while retaining the interaction with NAA10.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106294|||http://purl.uniprot.org/annotation/VAR_080534|||http://purl.uniprot.org/annotation/VAR_080535|||http://purl.uniprot.org/annotation/VAR_080536|||http://purl.uniprot.org/annotation/VAR_080537|||http://purl.uniprot.org/annotation/VAR_080538|||http://purl.uniprot.org/annotation/VAR_080539|||http://purl.uniprot.org/annotation/VAR_080540|||http://purl.uniprot.org/annotation/VAR_080541|||http://purl.uniprot.org/annotation/VAR_080542|||http://purl.uniprot.org/annotation/VSP_012560|||http://purl.uniprot.org/annotation/VSP_012561
http://togogenome.org/gene/9606:HSPA1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34931                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Heat shock 70 kDa protein 1-like|||No rescue of PRKN translocation deficit in knockout cells.|||Nucleotide-binding domain (NBD)|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078255|||http://purl.uniprot.org/annotation/VAR_003820|||http://purl.uniprot.org/annotation/VAR_025841|||http://purl.uniprot.org/annotation/VAR_025842|||http://purl.uniprot.org/annotation/VAR_025843|||http://purl.uniprot.org/annotation/VAR_025844|||http://purl.uniprot.org/annotation/VAR_025845|||http://purl.uniprot.org/annotation/VAR_025846
http://togogenome.org/gene/9606:SCG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05408                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-terminal peptide|||Disordered|||In isoform 2.|||N-terminal peptide|||Neuroendocrine protein 7B2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000041|||http://purl.uniprot.org/annotation/PRO_0000000042|||http://purl.uniprot.org/annotation/PRO_0000000043|||http://purl.uniprot.org/annotation/VSP_011754
http://togogenome.org/gene/9606:ZBTB8OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8C8MQ05|||http://purl.uniprot.org/uniprot/A8K0B5|||http://purl.uniprot.org/uniprot/D3DPQ2|||http://purl.uniprot.org/uniprot/Q8IWT0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes ability to activate tRNA ligase activity of RTCB.|||Archease|||In isoform 2.|||N-acetylalanine|||Protein archease|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285950|||http://purl.uniprot.org/annotation/VSP_024926
http://togogenome.org/gene/9606:GPR171                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14626                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 171|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069649|||http://purl.uniprot.org/annotation/VAR_049408
http://togogenome.org/gene/9606:SMIM18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKX4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421256
http://togogenome.org/gene/9606:CT45A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308946
http://togogenome.org/gene/9606:ABCG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45844                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 1|||Affects ATP binding. Does not affect efflux of 7beta-hydroxycholesterol. Does not affect localization at plasma membrane. Does not affect homodimerization. Decreases cholesterol and phospholipids efflux. Does not affect heretodimerization with ABCG4.|||Cytoplasmic|||Does not affect ABCG1-mediated cholesterol efflux; when associated with I-498.|||Does not affect ABCG1-mediated cholesterol efflux; when associated with I-499.|||Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-498.|||Dramatically reduces the ability of ABCG1 to mediate cholesterol efflux; when associated with I-499.|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||No significant effect.|||S-palmitoyl cysteine|||Significantly decreases ABCG1-mediated cholesterol efflux.|||Significantly reduces interaction with CAV1; when associated with A-491. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-491.|||Significantly reduces interaction with CAV1; when associated with A-493. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-493.|||Significantly reduces interaction with CAV1; when associated with A-498. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-498. Affects subcellular location at plasma membrane; when associated with A-498. Affects ABCG1 traffincking to the plasma membrane; when associated with A-498.|||Significantly reduces interaction with CAV1; when associated with A-499. Significantly reduces ABCG1-mediated cholesterol efflux; when associated with A-499. Affects subcellular location at plasma membrane; when associated with A-499. Affects ABCG1 traffincking to the plasma membrane; when associated with A-499.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093384|||http://purl.uniprot.org/annotation/VAR_012279|||http://purl.uniprot.org/annotation/VSP_000046|||http://purl.uniprot.org/annotation/VSP_000047|||http://purl.uniprot.org/annotation/VSP_000048|||http://purl.uniprot.org/annotation/VSP_000049|||http://purl.uniprot.org/annotation/VSP_000050|||http://purl.uniprot.org/annotation/VSP_000051|||http://purl.uniprot.org/annotation/VSP_010718
http://togogenome.org/gene/9606:CMTM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX76                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 6|||Cytoplasmic|||Extracellular|||Helical|||MARVEL|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186107|||http://purl.uniprot.org/annotation/VAR_061998
http://togogenome.org/gene/9606:GBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A068F658|||http://purl.uniprot.org/uniprot/B7Z6S9|||http://purl.uniprot.org/uniprot/P04062                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1000-fold decreases of glucosylceramidase activity.|||Decreased glucosylceramidase activity.|||Disordered|||Found in a patient with Parkinson disease; unknown pathological significance.|||Glycosyl hydrolase family 30 TIM-barrel|||Glycosyl hydrolase family 30 beta sandwich|||In GD and GD1.|||In GD and GD1; mild.|||In GD and GD3.|||In GD.|||In GD1 and GD2.|||In GD1 and GD2; also found in a patient with Parkinson disease.|||In GD1 and GD2; also found in patients with Parkinson disease; no effect on protein abundance; decreased glucosylceramidase activity.|||In GD1 and GD2; decreased glucosylceramidase activity; 13% of normal activity.|||In GD1 and GD2; decreased glucosylceramidase activity; 14% of normal activity; increases susceptibility to proteolytic degradation.|||In GD1 and GD3.|||In GD1 and GD3; decreased glucosylceramide catabolic process.|||In GD1 and GD3; severe; decreased glucosylceramidase activity; 12% of normal activity.|||In GD1, GD2 and GD3.|||In GD1, GD2 and GD3; also associated with I-400 in a patient with Gaucher disease type II; severely decreased glucosylceramidase activity.|||In GD1, GD2 and GD3; common mutation; associated with susceptibility to Parkinson disease; gene conversion; alters protein stability; increased proteasomal degradation; decreased protein abundance; very low glucosylceramide catabolic process; severe decrease of glucosylceramidase activity; 3% of normal activity when expressed in a heterologous system.|||In GD1, GD2 and GD3; unknown pathological significance; associated in cis with H-448 in all patients analyzed.|||In GD1, GD2, GD3 and GD3C; associated in cis with Q-294 in some patients; at homozygosity it causes GD3C; also found in a patient with Parkinson disease; loss of glucosylceramidase activity; alters protein stability.|||In GD1.|||In GD1; also found in a patient with Parkinson disease.|||In GD1; benign variant; found in patients who also carry a causative variant on the same allele; decreased glucosylceramidase activity; 42% of normal activity.|||In GD1; common mutation; associated with susceptibility to Parkinson disease; increased proteasomal degradation; decreased protein abundance; decreased glucosylceramide catabolic process; decreased glucosylceramidase activity; 23% of normal activity when expressed in a heterologous system; alters interaction with saposin-C.|||In GD1; decreased glucosylceramidase activity.|||In GD1; decreased glucosylceramidase activity; 20% of normal activity.|||In GD1; decreased glucosylceramidase activity; 4-6% of normal activity.|||In GD1; decreased glucosylceramidase activity; 7% of normal activity when expressed in a heterologous system.|||In GD1; decreased glucosylceramide catabolic process.|||In GD1; decreased protein abundance; decreased glucosylceramide catabolic process.|||In GD1; likely benign variant.|||In GD1; loss of glucosylceramidase activity.|||In GD1; loss of glucosylceramide catabolic process.|||In GD1; mild.|||In GD1; mild; decreased glucosylceramidase activity; 8% of normal activity; increases susceptibility to proteolytic degradation.|||In GD1; severely decreased glucosylceramidase activity.|||In GD1; severely decreased glucosylceramidase activity; 3% of normal activity when expressed in a heterologous system.|||In GD1; severely decreased glucosylceramidase activity; less than 5% of normal activity.|||In GD1; unknown pathological significance.|||In GD1; unknown pathological significance; also found in a patient with Parkinson disease.|||In GD1; unknown pathological significance; associated in cis with D-460 in one patient with Gaucher disease type 1; no effect on glucosylceramidase activity.|||In GD1; very low glucosylceramidase activity.|||In GD1; when associated in cis with R-490; loss of glucosylceramidase activity.|||In GD2 and GD3.|||In GD2.|||In GD2; decreased glucosylceramidase activity; 16% of normal activity; increases susceptibility to proteolytic degradation.|||In GD2; decreased glucosylceramide catabolic process.|||In GD2; loss of glucosylceramidase activity.|||In GD2; loss of glucosylceramide catabolic process.|||In GD2; severe; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation.|||In GD2; unknown pathological significance; when associated in cis with R-241.|||In GD3.|||In GD3; loss of glucosylceramidase activity; results in glycosphingolipid accumulation in brain and liver of a knockin mouse model due to impaired glucosylceramidase activity.|||In GD3; loss of glucosylceramide catabolic process.|||In GD3; severe; unknown pathological significance.|||In GD; also found in a patient with Parkinson disease; decreased glucosylceramidase activity; 7% of normal activity.|||In GD; decreased glucosylceramidase activity; 10% of normal activity; increases susceptibility to proteolytic degradation.|||In GD; decreased glucosylceramidase activity; 12% of normal activity.|||In GD; decreased glucosylceramidase activity; 15% of normal activity; increases susceptibility to proteolytic degradation.|||In GD; decreased glucosylceramidase activity; 16% of normal activity.|||In GD; decreased glucosylceramidase activity; 17% of normal activity.|||In GD; decreased glucosylceramidase activity; 22% of normal activity.|||In GD; decreased glucosylceramidase activity; 4% of normal activity.|||In GD; decreased glucosylceramidase activity; 4% of normal activity; increases susceptibility to proteolytic degradation.|||In GD; decreased glucosylceramidase activity; 5% of normal activity.|||In GD; decreased glucosylceramidase activity; 6% of normal activity; alters protein stability and increases susceptibility to proteolytic degradation.|||In GD; decreased glucosylceramidase activity; 8% of normal activity; increases susceptibility to proteolytic degradation.|||In GD; decreased glucosylceramidase activity; 9% of normal activity; increases susceptibility to proteolytic degradation.|||In GD; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation.|||In GD; loss of glucosylceramidase activity;.|||In GD; mild.|||In GD; neuronopathic and perinatal lethal forms; loss of glucosylceramidase activity.|||In GD; unknown pathological significance.|||In GDPL, GD1 and GD2.|||In GDPL.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform Short.|||Likely benign variant; found in a patient with Parkinson disease.|||Loss of glucosylceramidase activity.|||Lysosomal acid glucosylceramidase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Severe decrease of glucosylceramidase activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012177|||http://purl.uniprot.org/annotation/VAR_003255|||http://purl.uniprot.org/annotation/VAR_003256|||http://purl.uniprot.org/annotation/VAR_003257|||http://purl.uniprot.org/annotation/VAR_003258|||http://purl.uniprot.org/annotation/VAR_003259|||http://purl.uniprot.org/annotation/VAR_003260|||http://purl.uniprot.org/annotation/VAR_003261|||http://purl.uniprot.org/annotation/VAR_003262|||http://purl.uniprot.org/annotation/VAR_003263|||http://purl.uniprot.org/annotation/VAR_003264|||http://purl.uniprot.org/annotation/VAR_003265|||http://purl.uniprot.org/annotation/VAR_003266|||http://purl.uniprot.org/annotation/VAR_003267|||http://purl.uniprot.org/annotation/VAR_003268|||http://purl.uniprot.org/annotation/VAR_003269|||http://purl.uniprot.org/annotation/VAR_003270|||http://purl.uniprot.org/annotation/VAR_003271|||http://purl.uniprot.org/annotation/VAR_003272|||http://purl.uniprot.org/annotation/VAR_003273|||http://purl.uniprot.org/annotation/VAR_003274|||http://purl.uniprot.org/annotation/VAR_003275|||http://purl.uniprot.org/annotation/VAR_003276|||http://purl.uniprot.org/annotation/VAR_003277|||http://purl.uniprot.org/annotation/VAR_003278|||http://purl.uniprot.org/annotation/VAR_003279|||http://purl.uniprot.org/annotation/VAR_003280|||http://purl.uniprot.org/annotation/VAR_003281|||http://purl.uniprot.org/annotation/VAR_003282|||http://purl.uniprot.org/annotation/VAR_003283|||http://purl.uniprot.org/annotation/VAR_003284|||http://purl.uniprot.org/annotation/VAR_003285|||http://purl.uniprot.org/annotation/VAR_003286|||http://purl.uniprot.org/annotation/VAR_003287|||http://purl.uniprot.org/annotation/VAR_003288|||http://purl.uniprot.org/annotation/VAR_003289|||http://purl.uniprot.org/annotation/VAR_003290|||http://purl.uniprot.org/annotation/VAR_003291|||http://purl.uniprot.org/annotation/VAR_003292|||http://purl.uniprot.org/annotation/VAR_003293|||http://purl.uniprot.org/annotation/VAR_003294|||http://purl.uniprot.org/annotation/VAR_003295|||http://purl.uniprot.org/annotation/VAR_003296|||http://purl.uniprot.org/annotation/VAR_003297|||http://purl.uniprot.org/annotation/VAR_003298|||http://purl.uniprot.org/annotation/VAR_003299|||http://purl.uniprot.org/annotation/VAR_003300|||http://purl.uniprot.org/annotation/VAR_003301|||http://purl.uniprot.org/annotation/VAR_003302|||http://purl.uniprot.org/annotation/VAR_003303|||http://purl.uniprot.org/annotation/VAR_003304|||http://purl.uniprot.org/annotation/VAR_003305|||http://purl.uniprot.org/annotation/VAR_003306|||http://purl.uniprot.org/annotation/VAR_003307|||http://purl.uniprot.org/annotation/VAR_003308|||http://purl.uniprot.org/annotation/VAR_003309|||http://purl.uniprot.org/annotation/VAR_003310|||http://purl.uniprot.org/annotation/VAR_003311|||http://purl.uniprot.org/annotation/VAR_003312|||http://purl.uniprot.org/annotation/VAR_003313|||http://purl.uniprot.org/annotation/VAR_003314|||http://purl.uniprot.org/annotation/VAR_003315|||http://purl.uniprot.org/annotation/VAR_003316|||http://purl.uniprot.org/annotation/VAR_003317|||http://purl.uniprot.org/annotation/VAR_003318|||http://purl.uniprot.org/annotation/VAR_003319|||http://purl.uniprot.org/annotation/VAR_003320|||http://purl.uniprot.org/annotation/VAR_003321|||http://purl.uniprot.org/annotation/VAR_003322|||http://purl.uniprot.org/annotation/VAR_003323|||http://purl.uniprot.org/annotation/VAR_003324|||http://purl.uniprot.org/annotation/VAR_003325|||http://purl.uniprot.org/annotation/VAR_003326|||http://purl.uniprot.org/annotation/VAR_003327|||http://purl.uniprot.org/annotation/VAR_003328|||http://purl.uniprot.org/annotation/VAR_009033|||http://purl.uniprot.org/annotation/VAR_009034|||http://purl.uniprot.org/annotation/VAR_009035|||http://purl.uniprot.org/annotation/VAR_009036|||http://purl.uniprot.org/annotation/VAR_009037|||http://purl.uniprot.org/annotation/VAR_009038|||http://purl.uniprot.org/annotation/VAR_009039|||http://purl.uniprot.org/annotation/VAR_009040|||http://purl.uniprot.org/annotation/VAR_009041|||http://purl.uniprot.org/annotation/VAR_009042|||http://purl.uniprot.org/annotation/VAR_009043|||http://purl.uniprot.org/annotation/VAR_009044|||http://purl.uniprot.org/annotation/VAR_009045|||http://purl.uniprot.org/annotation/VAR_009046|||http://purl.uniprot.org/annotation/VAR_009047|||http://purl.uniprot.org/annotation/VAR_009048|||http://purl.uniprot.org/annotation/VAR_009049|||http://purl.uniprot.org/annotation/VAR_009050|||http://purl.uniprot.org/annotation/VAR_010059|||http://purl.uniprot.org/annotation/VAR_010060|||http://purl.uniprot.org/annotation/VAR_010062|||http://purl.uniprot.org/annotation/VAR_010063|||http://purl.uniprot.org/annotation/VAR_010064|||http://purl.uniprot.org/annotation/VAR_010065|||http://purl.uniprot.org/annotation/VAR_010066|||http://purl.uniprot.org/annotation/VAR_010067|||http://purl.uniprot.org/annotation/VAR_010068|||http://purl.uniprot.org/annotation/VAR_010069|||http://purl.uniprot.org/annotation/VAR_010070|||http://purl.uniprot.org/annotation/VAR_010071|||http://purl.uniprot.org/annotation/VAR_010072|||http://purl.uniprot.org/annotation/VAR_010073|||http://purl.uniprot.org/annotation/VAR_010074|||http://purl.uniprot.org/annotation/VAR_010075|||http://purl.uniprot.org/annotation/VAR_032197|||http://purl.uniprot.org/annotation/VAR_032198|||http://purl.uniprot.org/annotation/VAR_032199|||http://purl.uniprot.org/annotation/VAR_032200|||http://purl.uniprot.org/annotation/VAR_032201|||http://purl.uniprot.org/annotation/VAR_032202|||http://purl.uniprot.org/annotation/VAR_032203|||http://purl.uniprot.org/annotation/VAR_032204|||http://purl.uniprot.org/annotation/VAR_032205|||http://purl.uniprot.org/annotation/VAR_032206|||http://purl.uniprot.org/annotation/VAR_032207|||http://purl.uniprot.org/annotation/VAR_032208|||http://purl.uniprot.org/annotation/VAR_032209|||http://purl.uniprot.org/annotation/VAR_032210|||http://purl.uniprot.org/annotation/VAR_032211|||http://purl.uniprot.org/annotation/VAR_032212|||http://purl.uniprot.org/annotation/VAR_032213|||http://purl.uniprot.org/annotation/VAR_032214|||http://purl.uniprot.org/annotation/VAR_032215|||http://purl.uniprot.org/annotation/VAR_032216|||http://purl.uniprot.org/annotation/VAR_032217|||http://purl.uniprot.org/annotation/VAR_032394|||http://purl.uniprot.org/annotation/VAR_032395|||http://purl.uniprot.org/annotation/VAR_032396|||http://purl.uniprot.org/annotation/VAR_032397|||http://purl.uniprot.org/annotation/VAR_032398|||http://purl.uniprot.org/annotation/VAR_032399|||http://purl.uniprot.org/annotation/VAR_032400|||http://purl.uniprot.org/annotation/VAR_032401|||http://purl.uniprot.org/annotation/VAR_032402|||http://purl.uniprot.org/annotation/VAR_032403|||http://purl.uniprot.org/annotation/VAR_032404|||http://purl.uniprot.org/annotation/VAR_032405|||http://purl.uniprot.org/annotation/VAR_032406|||http://purl.uniprot.org/annotation/VAR_032407|||http://purl.uniprot.org/annotation/VAR_032408|||http://purl.uniprot.org/annotation/VAR_032409|||http://purl.uniprot.org/annotation/VAR_032410|||http://purl.uniprot.org/annotation/VAR_032411|||http://purl.uniprot.org/annotation/VAR_032412|||http://purl.uniprot.org/annotation/VAR_032413|||http://purl.uniprot.org/annotation/VAR_032414|||http://purl.uniprot.org/annotation/VAR_032415|||http://purl.uniprot.org/annotation/VAR_032416|||http://purl.uniprot.org/annotation/VAR_063066|||http://purl.uniprot.org/annotation/VAR_063067|||http://purl.uniprot.org/annotation/VAR_063068|||http://purl.uniprot.org/annotation/VAR_081188|||http://purl.uniprot.org/annotation/VAR_081189|||http://purl.uniprot.org/annotation/VAR_081190|||http://purl.uniprot.org/annotation/VAR_081191|||http://purl.uniprot.org/annotation/VAR_081192|||http://purl.uniprot.org/annotation/VAR_081193|||http://purl.uniprot.org/annotation/VAR_081194|||http://purl.uniprot.org/annotation/VAR_081195|||http://purl.uniprot.org/annotation/VAR_081196|||http://purl.uniprot.org/annotation/VAR_081197|||http://purl.uniprot.org/annotation/VAR_081198|||http://purl.uniprot.org/annotation/VAR_081199|||http://purl.uniprot.org/annotation/VAR_081200|||http://purl.uniprot.org/annotation/VAR_081201|||http://purl.uniprot.org/annotation/VAR_088437|||http://purl.uniprot.org/annotation/VAR_088438|||http://purl.uniprot.org/annotation/VAR_088439|||http://purl.uniprot.org/annotation/VAR_088440|||http://purl.uniprot.org/annotation/VAR_088441|||http://purl.uniprot.org/annotation/VAR_088442|||http://purl.uniprot.org/annotation/VAR_088443|||http://purl.uniprot.org/annotation/VAR_088444|||http://purl.uniprot.org/annotation/VAR_088445|||http://purl.uniprot.org/annotation/VSP_018800|||http://purl.uniprot.org/annotation/VSP_025216|||http://purl.uniprot.org/annotation/VSP_025217|||http://purl.uniprot.org/annotation/VSP_025218|||http://purl.uniprot.org/annotation/VSP_054655|||http://purl.uniprot.org/annotation/VSP_054656
http://togogenome.org/gene/9606:FABP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A077H155|||http://purl.uniprot.org/uniprot/O15540|||http://purl.uniprot.org/uniprot/Q59HE4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, brain|||In isoform 2.|||Lipocalin/cytosolic fatty-acid binding|||N-acetylvaline|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067373|||http://purl.uniprot.org/annotation/VAR_049012|||http://purl.uniprot.org/annotation/VSP_055490
http://togogenome.org/gene/9606:PLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4D4|||http://purl.uniprot.org/uniprot/A8K9L3|||http://purl.uniprot.org/uniprot/B4DI30|||http://purl.uniprot.org/uniprot/P60201                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In HLD1 and SPG2.|||In HLD1.|||In SPG2.|||In SPG2; partially retained in the endoplasmic reticulum; does not induce unfolded protein response.|||In isoform DM-20.|||Myelin proteolipid protein|||O-palmitoyl serine|||Phosphoserine|||Phosphothreonine|||Probable disease-associated variant found in Pelizaeus-Merzbacher disease/X-linked spastic paraplegia.|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159005|||http://purl.uniprot.org/annotation/VAR_004546|||http://purl.uniprot.org/annotation/VAR_004547|||http://purl.uniprot.org/annotation/VAR_004548|||http://purl.uniprot.org/annotation/VAR_004550|||http://purl.uniprot.org/annotation/VAR_004551|||http://purl.uniprot.org/annotation/VAR_004552|||http://purl.uniprot.org/annotation/VAR_004553|||http://purl.uniprot.org/annotation/VAR_004554|||http://purl.uniprot.org/annotation/VAR_004555|||http://purl.uniprot.org/annotation/VAR_004556|||http://purl.uniprot.org/annotation/VAR_004557|||http://purl.uniprot.org/annotation/VAR_004558|||http://purl.uniprot.org/annotation/VAR_004559|||http://purl.uniprot.org/annotation/VAR_004560|||http://purl.uniprot.org/annotation/VAR_004561|||http://purl.uniprot.org/annotation/VAR_004562|||http://purl.uniprot.org/annotation/VAR_004563|||http://purl.uniprot.org/annotation/VAR_004565|||http://purl.uniprot.org/annotation/VAR_007956|||http://purl.uniprot.org/annotation/VAR_015014|||http://purl.uniprot.org/annotation/VAR_015015|||http://purl.uniprot.org/annotation/VAR_015016|||http://purl.uniprot.org/annotation/VAR_015017|||http://purl.uniprot.org/annotation/VAR_015018|||http://purl.uniprot.org/annotation/VAR_015019|||http://purl.uniprot.org/annotation/VAR_015020|||http://purl.uniprot.org/annotation/VAR_015021|||http://purl.uniprot.org/annotation/VAR_015022|||http://purl.uniprot.org/annotation/VAR_015023|||http://purl.uniprot.org/annotation/VAR_015024|||http://purl.uniprot.org/annotation/VAR_015025|||http://purl.uniprot.org/annotation/VAR_015026|||http://purl.uniprot.org/annotation/VAR_015027|||http://purl.uniprot.org/annotation/VAR_015028|||http://purl.uniprot.org/annotation/VAR_015029|||http://purl.uniprot.org/annotation/VAR_015030|||http://purl.uniprot.org/annotation/VAR_015031|||http://purl.uniprot.org/annotation/VAR_015032|||http://purl.uniprot.org/annotation/VAR_015033|||http://purl.uniprot.org/annotation/VAR_015034|||http://purl.uniprot.org/annotation/VAR_015035|||http://purl.uniprot.org/annotation/VAR_015036|||http://purl.uniprot.org/annotation/VAR_015037|||http://purl.uniprot.org/annotation/VAR_015038|||http://purl.uniprot.org/annotation/VAR_015039|||http://purl.uniprot.org/annotation/VAR_015040|||http://purl.uniprot.org/annotation/VAR_015041|||http://purl.uniprot.org/annotation/VAR_015042|||http://purl.uniprot.org/annotation/VAR_015043|||http://purl.uniprot.org/annotation/VAR_015044|||http://purl.uniprot.org/annotation/VAR_015045|||http://purl.uniprot.org/annotation/VAR_015046|||http://purl.uniprot.org/annotation/VAR_015047|||http://purl.uniprot.org/annotation/VAR_015048|||http://purl.uniprot.org/annotation/VAR_015049|||http://purl.uniprot.org/annotation/VAR_015050|||http://purl.uniprot.org/annotation/VAR_015051|||http://purl.uniprot.org/annotation/VAR_015052|||http://purl.uniprot.org/annotation/VAR_046906|||http://purl.uniprot.org/annotation/VAR_046907|||http://purl.uniprot.org/annotation/VAR_046908|||http://purl.uniprot.org/annotation/VAR_046909|||http://purl.uniprot.org/annotation/VAR_046910|||http://purl.uniprot.org/annotation/VAR_046911|||http://purl.uniprot.org/annotation/VAR_046912|||http://purl.uniprot.org/annotation/VAR_046913|||http://purl.uniprot.org/annotation/VAR_046914|||http://purl.uniprot.org/annotation/VAR_046915|||http://purl.uniprot.org/annotation/VAR_046916|||http://purl.uniprot.org/annotation/VAR_046917|||http://purl.uniprot.org/annotation/VAR_046918|||http://purl.uniprot.org/annotation/VAR_046919|||http://purl.uniprot.org/annotation/VAR_046920|||http://purl.uniprot.org/annotation/VAR_070667|||http://purl.uniprot.org/annotation/VSP_003325
http://togogenome.org/gene/9606:SLC10A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KNW5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sodium-dependent organic anion transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309215|||http://purl.uniprot.org/annotation/VAR_036904|||http://purl.uniprot.org/annotation/VAR_036905
http://togogenome.org/gene/9606:GOLGA8N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WBI6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8N|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420861
http://togogenome.org/gene/9606:SCTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47872|||http://purl.uniprot.org/uniprot/Q8IV17                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Secretin receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012852|||http://purl.uniprot.org/annotation/PRO_5004308991|||http://purl.uniprot.org/annotation/VAR_033970|||http://purl.uniprot.org/annotation/VAR_049456
http://togogenome.org/gene/9606:CASP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3G5|||http://purl.uniprot.org/uniprot/A0A0S2Z3Z5|||http://purl.uniprot.org/uniprot/Q92851                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes proteolytic activity.|||Associated with ALPS2A; does not interfere with apoptosis in a dominant negative manner.|||Caspase family p10|||Caspase family p20|||Caspase-10 subunit p12|||Caspase-10 subunit p23/17|||DED|||DED 1|||DED 2|||Disordered|||Does not interfere with apoptosis in a dominant negative manner.|||Found in a T-acute lymphoblastic leukemia sample; somatic mutation.|||Found in a colon cancer sample; somatic mutation.|||Found in a multiple myeloma sample; somatic mutation.|||In ALPS2A.|||In GASC; somatic mutation; impairs CASP10-mediated apoptosis.|||In NHL; somatic mutation.|||In isoform 6.|||In isoform 7.|||In isoform B and isoform 5.|||In isoform B, isoform D and isoform 6.|||In isoform C.|||Not associated with significantly altered cutaneous melanoma risk.|||The mutant protein has defective apoptosis and exerts a dominant-negative effect when cotransfected with the wild-type protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004644|||http://purl.uniprot.org/annotation/PRO_0000004645|||http://purl.uniprot.org/annotation/PRO_0000004646|||http://purl.uniprot.org/annotation/VAR_014071|||http://purl.uniprot.org/annotation/VAR_014072|||http://purl.uniprot.org/annotation/VAR_037428|||http://purl.uniprot.org/annotation/VAR_037429|||http://purl.uniprot.org/annotation/VAR_037430|||http://purl.uniprot.org/annotation/VAR_037431|||http://purl.uniprot.org/annotation/VAR_055361|||http://purl.uniprot.org/annotation/VAR_055362|||http://purl.uniprot.org/annotation/VAR_065233|||http://purl.uniprot.org/annotation/VAR_065234|||http://purl.uniprot.org/annotation/VAR_065235|||http://purl.uniprot.org/annotation/VAR_082802|||http://purl.uniprot.org/annotation/VAR_082803|||http://purl.uniprot.org/annotation/VAR_082804|||http://purl.uniprot.org/annotation/VSP_000819|||http://purl.uniprot.org/annotation/VSP_000820|||http://purl.uniprot.org/annotation/VSP_000821|||http://purl.uniprot.org/annotation/VSP_000822|||http://purl.uniprot.org/annotation/VSP_037229|||http://purl.uniprot.org/annotation/VSP_053333|||http://purl.uniprot.org/annotation/VSP_053334
http://togogenome.org/gene/9606:KLRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZS2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Killer cell lectin-like receptor subfamily F member 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046591|||http://purl.uniprot.org/annotation/VAR_047544|||http://purl.uniprot.org/annotation/VSP_010390|||http://purl.uniprot.org/annotation/VSP_010391|||http://purl.uniprot.org/annotation/VSP_010392|||http://purl.uniprot.org/annotation/VSP_010393|||http://purl.uniprot.org/annotation/VSP_010394
http://togogenome.org/gene/9606:FANCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB91                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Fanconi anemia group B protein|||N-acetylthreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087181|||http://purl.uniprot.org/annotation/VAR_069426
http://togogenome.org/gene/9606:POMK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5K3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In MDDGA12.|||In MDDGA12; loss of kinase activity.|||In a lung small cell carcinoma sample; somatic mutation.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Protein O-mannose kinase|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262996|||http://purl.uniprot.org/annotation/VAR_041372|||http://purl.uniprot.org/annotation/VAR_041373|||http://purl.uniprot.org/annotation/VAR_041374|||http://purl.uniprot.org/annotation/VAR_041375|||http://purl.uniprot.org/annotation/VAR_041376|||http://purl.uniprot.org/annotation/VAR_069625|||http://purl.uniprot.org/annotation/VAR_069626|||http://purl.uniprot.org/annotation/VAR_072560
http://togogenome.org/gene/9606:MZT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZ87|||http://purl.uniprot.org/uniprot/Q6NZ67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Mitotic-spindle organizing protein 2B|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338988|||http://purl.uniprot.org/annotation/VAR_043853|||http://purl.uniprot.org/annotation/VAR_043854
http://togogenome.org/gene/9606:TPX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q643R0|||http://purl.uniprot.org/uniprot/Q9ULW0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Aurora-A binding|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||TPX2 C-terminal|||TPX2 central|||Targeting protein for Xklp2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065581|||http://purl.uniprot.org/annotation/VAR_036269|||http://purl.uniprot.org/annotation/VSP_057355
http://togogenome.org/gene/9606:PXMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6I8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peroxisomal membrane protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218932|||http://purl.uniprot.org/annotation/VAR_015426|||http://purl.uniprot.org/annotation/VSP_041217|||http://purl.uniprot.org/annotation/VSP_041218
http://togogenome.org/gene/9606:CCL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80075                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 8|||MCP-2(6-76)|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005188|||http://purl.uniprot.org/annotation/PRO_0000005189|||http://purl.uniprot.org/annotation/VAR_001633|||http://purl.uniprot.org/annotation/VAR_048704
http://togogenome.org/gene/9606:ADHFE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWW8                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Hydroxyacid-oxoacid transhydrogenase, mitochondrial|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322996|||http://purl.uniprot.org/annotation/VAR_039470|||http://purl.uniprot.org/annotation/VAR_054015|||http://purl.uniprot.org/annotation/VSP_031984|||http://purl.uniprot.org/annotation/VSP_031985|||http://purl.uniprot.org/annotation/VSP_031986
http://togogenome.org/gene/9606:COQ10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MF6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Coenzyme Q-binding protein COQ10 homolog A, mitochondrial|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228644|||http://purl.uniprot.org/annotation/VAR_025703|||http://purl.uniprot.org/annotation/VAR_048828|||http://purl.uniprot.org/annotation/VSP_017685|||http://purl.uniprot.org/annotation/VSP_046918
http://togogenome.org/gene/9606:NKAIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWY5|||http://purl.uniprot.org/uniprot/Q8IVV8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079437|||http://purl.uniprot.org/annotation/PRO_5002788463|||http://purl.uniprot.org/annotation/VAR_037051|||http://purl.uniprot.org/annotation/VAR_037052|||http://purl.uniprot.org/annotation/VAR_037053|||http://purl.uniprot.org/annotation/VAR_037054
http://togogenome.org/gene/9606:INSL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y581                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Connecting peptide|||Insulin-like peptide INSL6|||Insulin-like peptide INSL6 A chain|||Insulin-like peptide INSL6 B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016172|||http://purl.uniprot.org/annotation/PRO_0000016173|||http://purl.uniprot.org/annotation/PRO_0000016174|||http://purl.uniprot.org/annotation/PRO_0000016175|||http://purl.uniprot.org/annotation/PRO_0000016176|||http://purl.uniprot.org/annotation/VAR_024329
http://togogenome.org/gene/9606:KDM6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0R0|||http://purl.uniprot.org/uniprot/A0A804HJA2|||http://purl.uniprot.org/uniprot/B4E0L8|||http://purl.uniprot.org/uniprot/B7ZKN1|||http://purl.uniprot.org/uniprot/B7ZKN5|||http://purl.uniprot.org/uniprot/B7ZKN6|||http://purl.uniprot.org/uniprot/E1U0S6|||http://purl.uniprot.org/uniprot/F5H5V6|||http://purl.uniprot.org/uniprot/F5H6S1|||http://purl.uniprot.org/uniprot/F8W8R6|||http://purl.uniprot.org/uniprot/O15550|||http://purl.uniprot.org/uniprot/Q59HG3|||http://purl.uniprot.org/uniprot/Q86TD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone demethylase activity.|||Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In a patient with chronic myelomonocytic leukemia.|||Interaction with SUPT6H|||JmjC|||Lysine-specific demethylase 6A|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106409|||http://purl.uniprot.org/annotation/VAR_014492|||http://purl.uniprot.org/annotation/VAR_014493|||http://purl.uniprot.org/annotation/VAR_020313|||http://purl.uniprot.org/annotation/VAR_035871|||http://purl.uniprot.org/annotation/VAR_046527|||http://purl.uniprot.org/annotation/VAR_067225|||http://purl.uniprot.org/annotation/VAR_067226|||http://purl.uniprot.org/annotation/VAR_067227
http://togogenome.org/gene/9606:ZNF114                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 114                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285296|||http://purl.uniprot.org/annotation/VAR_052769|||http://purl.uniprot.org/annotation/VAR_052770|||http://purl.uniprot.org/annotation/VSP_024864
http://togogenome.org/gene/9606:IL1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01583                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  About 50% loss of cytokine secretion after DNA damage.|||Interleukin-1 alpha|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-myristoyl lysine|||Nuclear localization signal (NLS)|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015265|||http://purl.uniprot.org/annotation/PRO_0000015266|||http://purl.uniprot.org/annotation/VAR_014304|||http://purl.uniprot.org/annotation/VAR_014305|||http://purl.uniprot.org/annotation/VAR_014306|||http://purl.uniprot.org/annotation/VAR_014600|||http://purl.uniprot.org/annotation/VAR_014601
http://togogenome.org/gene/9606:MOB3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70IA8                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  MOB kinase activator 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193574
http://togogenome.org/gene/9606:RPS4Y2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD47                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  S4 RNA-binding|||Small ribosomal subunit protein eS4, Y isoform 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130818
http://togogenome.org/gene/9606:AGFG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2D6|||http://purl.uniprot.org/uniprot/O95081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Arf-GAP domain and FG repeat-containing protein 2|||C4-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204828|||http://purl.uniprot.org/annotation/VAR_050566|||http://purl.uniprot.org/annotation/VSP_010667|||http://purl.uniprot.org/annotation/VSP_010668
http://togogenome.org/gene/9606:LRIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2V4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Fibronectin type-III|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014835|||http://purl.uniprot.org/annotation/VAR_020081|||http://purl.uniprot.org/annotation/VAR_049891|||http://purl.uniprot.org/annotation/VAR_049892|||http://purl.uniprot.org/annotation/VAR_049893
http://togogenome.org/gene/9606:OR5T2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGG2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5T2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150614|||http://purl.uniprot.org/annotation/VAR_054349|||http://purl.uniprot.org/annotation/VAR_054350|||http://purl.uniprot.org/annotation/VAR_054351|||http://purl.uniprot.org/annotation/VAR_054352|||http://purl.uniprot.org/annotation/VAR_054353|||http://purl.uniprot.org/annotation/VAR_054354
http://togogenome.org/gene/9606:LHFPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUX7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||LHFPL tetraspan subfamily member 2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244763|||http://purl.uniprot.org/annotation/VAR_026913
http://togogenome.org/gene/9606:PCDHGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003950|||http://purl.uniprot.org/annotation/VAR_048556|||http://purl.uniprot.org/annotation/VSP_008661|||http://purl.uniprot.org/annotation/VSP_008662
http://togogenome.org/gene/9606:P3R3URF-PIK3R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXM8|||http://purl.uniprot.org/uniprot/F6TDL0|||http://purl.uniprot.org/uniprot/Q68CY7|||http://purl.uniprot.org/uniprot/Q7Z3W2                                                                                  ^@                                                                                  Coiled-Coil|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||SH2                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:USP17L30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:ATP8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Q0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Exoplasmic loop|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Involved in the recognition of the lipid substrate on the exoplasmic side|||Involved in the release of the transported lipid into the cytosolic leaflet|||Phospholipid-transporting ATPase IA|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046360|||http://purl.uniprot.org/annotation/VAR_022003|||http://purl.uniprot.org/annotation/VSP_000431|||http://purl.uniprot.org/annotation/VSP_040977
http://togogenome.org/gene/9606:PDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7N6|||http://purl.uniprot.org/uniprot/Q15118                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Histidine kinase|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||Phosphotyrosine; by FGFR1|||Phosphotyrosine; by FGFR1, ABL1, FLT3 and JAK2|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023437|||http://purl.uniprot.org/annotation/VAR_042295|||http://purl.uniprot.org/annotation/VAR_050477|||http://purl.uniprot.org/annotation/VSP_055172
http://togogenome.org/gene/9606:JMJD7-PLA2G4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C869                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes enzyme activity.|||C2|||Cytosolic phospholipase A2 beta|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No effect.|||Nucleophile|||PLA2c|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247021|||http://purl.uniprot.org/annotation/VAR_027047|||http://purl.uniprot.org/annotation/VAR_027048|||http://purl.uniprot.org/annotation/VAR_034365|||http://purl.uniprot.org/annotation/VAR_060082|||http://purl.uniprot.org/annotation/VSP_019871|||http://purl.uniprot.org/annotation/VSP_039387|||http://purl.uniprot.org/annotation/VSP_039388|||http://purl.uniprot.org/annotation/VSP_039389|||http://purl.uniprot.org/annotation/VSP_039390
http://togogenome.org/gene/9606:SLC22A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP53|||http://purl.uniprot.org/uniprot/Q96S37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In RHUC1.|||In RHUC1; reduced urate transport.|||In RHUC1; reduced urate transport; reduced localization at the plasma membrane.|||In RHUC1; strongly reduced urate transport.|||In RHUC1; unknown pathological significance; affects urate transport.|||In RHUC1; unknown pathological significance; no effect on urate transport; no effect on its localization to cell membrane.|||In RHUC1; unknown pathological significance; reduced urate transport; abolishes localization to cell membrane.|||In RHUC1; unknown pathological significance; reduced urate transport; decreased localization to cell membrane.|||In RHUC1; unknown pathological significance; reduced urate transport; no effect on its localization to cell membrane.|||In RHUC1; unknown pathological significance; strongly reduced urate transport; abolishes localization to cell membrane.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In some gout patients; uncertain pathological significance.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Solute carrier family 22 member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307944|||http://purl.uniprot.org/annotation/VAR_036720|||http://purl.uniprot.org/annotation/VAR_036721|||http://purl.uniprot.org/annotation/VAR_036722|||http://purl.uniprot.org/annotation/VAR_036723|||http://purl.uniprot.org/annotation/VAR_036724|||http://purl.uniprot.org/annotation/VAR_036725|||http://purl.uniprot.org/annotation/VAR_036726|||http://purl.uniprot.org/annotation/VAR_036727|||http://purl.uniprot.org/annotation/VAR_036728|||http://purl.uniprot.org/annotation/VAR_036729|||http://purl.uniprot.org/annotation/VAR_036730|||http://purl.uniprot.org/annotation/VAR_036731|||http://purl.uniprot.org/annotation/VAR_036732|||http://purl.uniprot.org/annotation/VAR_036733|||http://purl.uniprot.org/annotation/VAR_036734|||http://purl.uniprot.org/annotation/VAR_036735|||http://purl.uniprot.org/annotation/VAR_036736|||http://purl.uniprot.org/annotation/VAR_036737|||http://purl.uniprot.org/annotation/VAR_075344|||http://purl.uniprot.org/annotation/VAR_084699|||http://purl.uniprot.org/annotation/VAR_084700|||http://purl.uniprot.org/annotation/VAR_084701|||http://purl.uniprot.org/annotation/VAR_084702|||http://purl.uniprot.org/annotation/VAR_084703|||http://purl.uniprot.org/annotation/VSP_028879|||http://purl.uniprot.org/annotation/VSP_054054|||http://purl.uniprot.org/annotation/VSP_054055
http://togogenome.org/gene/9606:MIEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QY95|||http://purl.uniprot.org/uniprot/Q9H0J7|||http://purl.uniprot.org/uniprot/Q9NQG6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-368.|||Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-342 and E-372.|||Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with D-201; E-368 and E-372.|||Abolishes nucleotide-binding, but not DNM1L recruitment; when associated with E-342; E-368 and E-372.|||Cytoplasmic|||Dimerization|||Disordered|||Helical|||Important for interaction with DNM1L|||In isoform 2.|||Mab-21-like HhH/H2TH-like|||Mitochondrial dynamics protein MIEF1|||Mitochondrial intermembrane|||No effect on mitochondrial localization. Impairs DNM1L recruitment.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310448|||http://purl.uniprot.org/annotation/VAR_037040|||http://purl.uniprot.org/annotation/VAR_037041|||http://purl.uniprot.org/annotation/VAR_037042|||http://purl.uniprot.org/annotation/VAR_037043|||http://purl.uniprot.org/annotation/VSP_056383|||http://purl.uniprot.org/annotation/VSP_056384
http://togogenome.org/gene/9606:ZG16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60844                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Jacalin-type lectin|||Zymogen granule membrane protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017570|||http://purl.uniprot.org/annotation/VAR_034587|||http://purl.uniprot.org/annotation/VAR_034588|||http://purl.uniprot.org/annotation/VAR_070695
http://togogenome.org/gene/9606:GTF2IRD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EKJ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GTF2I-like 1|||GTF2I-like 2|||General transcription factor II-I repeat domain-containing protein 2B|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320121|||http://purl.uniprot.org/annotation/VSP_031605|||http://purl.uniprot.org/annotation/VSP_031606
http://togogenome.org/gene/9606:SRSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08170                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Polar residues|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081925|||http://purl.uniprot.org/annotation/VAR_052230|||http://purl.uniprot.org/annotation/VAR_052231|||http://purl.uniprot.org/annotation/VAR_052232|||http://purl.uniprot.org/annotation/VAR_052233
http://togogenome.org/gene/9606:CPLANE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU20                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Ciliogenesis and planar polarity effector 2|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284538|||http://purl.uniprot.org/annotation/VAR_031772|||http://purl.uniprot.org/annotation/VAR_079173
http://togogenome.org/gene/9606:COL24A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WDM8|||http://purl.uniprot.org/uniprot/Q17RW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Collagen alpha-1(XXIV) chain|||Collagen-like 1|||Collagen-like 10|||Collagen-like 11|||Collagen-like 12|||Collagen-like 13|||Collagen-like 14|||Collagen-like 15|||Collagen-like 16|||Collagen-like 17|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Collagen-like 9|||Disordered|||Fibrillar collagen NC1|||In isoform 2.|||Laminin G|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317616|||http://purl.uniprot.org/annotation/PRO_5003385512|||http://purl.uniprot.org/annotation/VAR_038565|||http://purl.uniprot.org/annotation/VAR_055672|||http://purl.uniprot.org/annotation/VAR_055673|||http://purl.uniprot.org/annotation/VAR_055674|||http://purl.uniprot.org/annotation/VAR_055675|||http://purl.uniprot.org/annotation/VAR_055676|||http://purl.uniprot.org/annotation/VAR_061116|||http://purl.uniprot.org/annotation/VAR_062865|||http://purl.uniprot.org/annotation/VSP_031090
http://togogenome.org/gene/9606:RBM14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Z0|||http://purl.uniprot.org/uniprot/A0A0S2Z567|||http://purl.uniprot.org/uniprot/A0A0S2Z5V2|||http://purl.uniprot.org/uniprot/Q96PK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein 14|||RRM|||RRM 1|||RRM 2|||TRBP-interacting domain; interaction with STIL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081774|||http://purl.uniprot.org/annotation/VSP_015078|||http://purl.uniprot.org/annotation/VSP_015079|||http://purl.uniprot.org/annotation/VSP_044641|||http://purl.uniprot.org/annotation/VSP_044642|||http://purl.uniprot.org/annotation/VSP_047109|||http://purl.uniprot.org/annotation/VSP_047110|||http://purl.uniprot.org/annotation/VSP_047494|||http://purl.uniprot.org/annotation/VSP_047495
http://togogenome.org/gene/9606:GAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43903                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Cleavage; by a caspase during apoptosis|||Disordered|||GAR|||Growth arrest-specific protein 2|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190440|||http://purl.uniprot.org/annotation/VSP_055080|||http://purl.uniprot.org/annotation/VSP_055081
http://togogenome.org/gene/9606:PTHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12272|||http://purl.uniprot.org/uniprot/Q53XY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic residues|||Disordered|||Important for receptor binding|||In BDE2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Osteostatin|||PTHrP[1-36]|||PTHrP[38-94]|||Parathyroid hormone-related protein|||Polar residues|||Reduced affinity for PTH1R.|||Strongly reduced affinity for PTH1R.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023224|||http://purl.uniprot.org/annotation/PRO_0000023225|||http://purl.uniprot.org/annotation/PRO_0000023226|||http://purl.uniprot.org/annotation/PRO_0000023227|||http://purl.uniprot.org/annotation/PRO_0000023228|||http://purl.uniprot.org/annotation/PRO_5014309530|||http://purl.uniprot.org/annotation/VAR_036433|||http://purl.uniprot.org/annotation/VAR_063711|||http://purl.uniprot.org/annotation/VAR_063712|||http://purl.uniprot.org/annotation/VSP_004534|||http://purl.uniprot.org/annotation/VSP_004535
http://togogenome.org/gene/9606:NDUFV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KNH5|||http://purl.uniprot.org/uniprot/P49821                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MC1DN4.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial|||NADH-ubiquinone oxidoreductase 51kDa subunit iron-sulphur binding|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019976|||http://purl.uniprot.org/annotation/VAR_008846|||http://purl.uniprot.org/annotation/VAR_008847|||http://purl.uniprot.org/annotation/VAR_014480|||http://purl.uniprot.org/annotation/VAR_014481|||http://purl.uniprot.org/annotation/VAR_019534|||http://purl.uniprot.org/annotation/VSP_003730
http://togogenome.org/gene/9606:CMTM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FZ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 7|||Helical|||In isoform 2.|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186110|||http://purl.uniprot.org/annotation/VSP_042566
http://togogenome.org/gene/9606:SFT2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95562                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Vesicle transport protein SFT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238610
http://togogenome.org/gene/9606:CHRNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15822                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with receptor activation|||Changes ligand activation kinetics in a alpha-2(+):alpha-2(-) subunit interface (in LS nAChR subtype).|||Cytoplasmic|||Decreases ligand activation in LS nAChR subtype; no effect in HS nAChR subtype.|||Disordered|||Extracellular|||Helical|||In BFIS6; unknown pathological significance.|||In ENFL4; markedly increases receptor sensitivity to acetylcholine.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000340|||http://purl.uniprot.org/annotation/VAR_027639|||http://purl.uniprot.org/annotation/VAR_027640|||http://purl.uniprot.org/annotation/VAR_027641|||http://purl.uniprot.org/annotation/VAR_076498|||http://purl.uniprot.org/annotation/VSP_055156
http://togogenome.org/gene/9606:LAS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4W2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In WTS; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Ribosomal biogenesis protein LAS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211559|||http://purl.uniprot.org/annotation/VAR_036587|||http://purl.uniprot.org/annotation/VAR_077824|||http://purl.uniprot.org/annotation/VAR_077825|||http://purl.uniprot.org/annotation/VSP_015178|||http://purl.uniprot.org/annotation/VSP_015179|||http://purl.uniprot.org/annotation/VSP_015180|||http://purl.uniprot.org/annotation/VSP_015181
http://togogenome.org/gene/9606:PROKR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1T0|||http://purl.uniprot.org/uniprot/Q8NFJ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In HH3.|||In HH3; benign variant; signaling activity is impaired.|||In HH3; decreased signaling activity.|||In HH3; likely benign variant.|||In HH3; phenotype consistent with Kallmann syndrome.|||In HH3; phenotype consistent with Kallmann syndrome; decreased signaling activity.|||In HH3; phenotype consistent with Kallmann syndrome; decreased signaling activity; abolished ligand binding.|||In HH3; phenotype consistent with Kallmann syndrome; signaling activity is impaired.|||In HH3; phenotype consistent with Kallmann syndrome; signaling activity is impaired; impaired cell surface-targeting.|||In HH3; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; decreased signaling activity.|||In HH3; triallelic inheritance; the patient also carries mutations in GNRH1 and FGFR1.|||N-linked (GlcNAc...) asparagine|||Prokineticin receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070083|||http://purl.uniprot.org/annotation/VAR_030957|||http://purl.uniprot.org/annotation/VAR_030958|||http://purl.uniprot.org/annotation/VAR_030959|||http://purl.uniprot.org/annotation/VAR_030960|||http://purl.uniprot.org/annotation/VAR_030961|||http://purl.uniprot.org/annotation/VAR_030962|||http://purl.uniprot.org/annotation/VAR_030963|||http://purl.uniprot.org/annotation/VAR_030964|||http://purl.uniprot.org/annotation/VAR_030965|||http://purl.uniprot.org/annotation/VAR_030966|||http://purl.uniprot.org/annotation/VAR_030967|||http://purl.uniprot.org/annotation/VAR_069964|||http://purl.uniprot.org/annotation/VAR_069965|||http://purl.uniprot.org/annotation/VAR_072173|||http://purl.uniprot.org/annotation/VAR_072174|||http://purl.uniprot.org/annotation/VAR_072175|||http://purl.uniprot.org/annotation/VAR_072176|||http://purl.uniprot.org/annotation/VAR_072978|||http://purl.uniprot.org/annotation/VAR_072979
http://togogenome.org/gene/9606:RAB1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0U4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-(2-cholinephosphoryl)serine|||(Microbial infection) O-AMP-tyrosine|||Abolishes AMPylation by Legionella DrrA.|||Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association.|||Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half.|||Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio.|||Abolishes phosphocholination by Legionella AnkX.|||Cysteine methyl ester|||Disordered|||Effector region|||N-acetylmethionine|||No effect on GDI1 binding. Reduces prenylation in vitro, but not in vivo. No effect on interaction with REP1/CHM; 100-fold refunction in intrinsic GTPase activity.|||No effect on prenylation.|||Prevent formation of autophagosomes.|||Ras-related protein Rab-1B|||S-geranylgeranyl cysteine|||Switch 2 region; required for interaction with REP1/CHM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121061
http://togogenome.org/gene/9606:ZP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60852|||http://purl.uniprot.org/uniprot/V9HWI9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||P-type|||Processed zona pellucida sperm-binding protein 1|||Removed in mature form|||ZP|||Zona pellucida sperm-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041677|||http://purl.uniprot.org/annotation/PRO_0000041678|||http://purl.uniprot.org/annotation/PRO_0000304553|||http://purl.uniprot.org/annotation/PRO_5004777246|||http://purl.uniprot.org/annotation/VAR_052996
http://togogenome.org/gene/9606:TCL1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56279                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Greatly reduced binding to AKT1, AKT2 and AKT3. Abolishes nuclear transport of AKT1.|||Greatly reduced binding to AKT2. Abolishes nuclear transport of AKT1.|||Slightly increased binding to AKT2.|||Slightly reduced binding to AKT2.|||T-cell leukemia/lymphoma protein 1A|||Unable to homodimerize but has no effect on interaction with AKT1, AKT2 or AKT3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184488|||http://purl.uniprot.org/annotation/VAR_053718
http://togogenome.org/gene/9606:OR52B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RD2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150767|||http://purl.uniprot.org/annotation/VAR_054126
http://togogenome.org/gene/9606:BMP2K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSY1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BMP-2-inducible protein kinase|||Basic and acidic residues|||Disordered|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085663|||http://purl.uniprot.org/annotation/VAR_040388|||http://purl.uniprot.org/annotation/VAR_040389|||http://purl.uniprot.org/annotation/VAR_040390|||http://purl.uniprot.org/annotation/VAR_051618|||http://purl.uniprot.org/annotation/VAR_051619|||http://purl.uniprot.org/annotation/VAR_059765|||http://purl.uniprot.org/annotation/VSP_008091|||http://purl.uniprot.org/annotation/VSP_008092|||http://purl.uniprot.org/annotation/VSP_008093
http://togogenome.org/gene/9606:LARP4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92615                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||La-related protein 4B|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281139
http://togogenome.org/gene/9606:P2RY12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7T1|||http://purl.uniprot.org/uniprot/Q9H244                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ADP binding.|||Cytoplasmic|||Decreases affinity for ADP.|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In BDPLT8.|||N-linked (GlcNAc...) asparagine|||No effect on ADP binding.|||P2Y purinoceptor 12|||Phosphoserine|||Slightly decreases affinity for ADP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070036|||http://purl.uniprot.org/annotation/VAR_025383|||http://purl.uniprot.org/annotation/VAR_025384|||http://purl.uniprot.org/annotation/VAR_049431|||http://purl.uniprot.org/annotation/VAR_072802
http://togogenome.org/gene/9606:OR10K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV64|||http://purl.uniprot.org/uniprot/Q8NGX5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150711
http://togogenome.org/gene/9606:ATF7IP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U623                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Activating transcription factor 7-interacting protein 2|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281784|||http://purl.uniprot.org/annotation/VAR_031286|||http://purl.uniprot.org/annotation/VAR_031287|||http://purl.uniprot.org/annotation/VAR_053872|||http://purl.uniprot.org/annotation/VSP_024042|||http://purl.uniprot.org/annotation/VSP_024043
http://togogenome.org/gene/9606:SLC9C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Ion transport-like|||N-linked (GlcNAc...) asparagine|||Sodium/hydrogen exchanger 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295704|||http://purl.uniprot.org/annotation/VAR_033324|||http://purl.uniprot.org/annotation/VAR_033325|||http://purl.uniprot.org/annotation/VAR_033326|||http://purl.uniprot.org/annotation/VAR_033327|||http://purl.uniprot.org/annotation/VAR_033328|||http://purl.uniprot.org/annotation/VAR_033329|||http://purl.uniprot.org/annotation/VAR_033330|||http://purl.uniprot.org/annotation/VAR_050233|||http://purl.uniprot.org/annotation/VAR_061369|||http://purl.uniprot.org/annotation/VSP_027010
http://togogenome.org/gene/9606:PITPNM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R787|||http://purl.uniprot.org/uniprot/O00562                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Causes association with lipid droplets.|||DDHD|||Disordered|||In isoform 2.|||Loss of interaction with VAPB.|||Membrane-associated phosphatidylinositol transfer protein 1|||No detectable effect on phosphorylation; when associated with A-389 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-1222.|||No detectable effect on phosphorylation; when associated with A-389 and A-793. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-794.|||No detectable effect on phosphorylation; when associated with A-793 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-794 and A-1222.|||No effect on phosphorylation.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues|||Prevents association with lipid droplets.|||Reduced phosphorylation.|||Slightly reduced phosphorylation. Strongly reduced phosphorylation; when associated with A-794 or A-389. Loss of threonine phosphorylation; when associated with A-389; A-793 and A-1222.|||Strongly reduced phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232738|||http://purl.uniprot.org/annotation/VSP_021157
http://togogenome.org/gene/9606:MED16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2X0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mediator of RNA polymerase II transcription subunit 16|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051292|||http://purl.uniprot.org/annotation/VAR_053958|||http://purl.uniprot.org/annotation/VAR_053959|||http://purl.uniprot.org/annotation/VSP_028749|||http://purl.uniprot.org/annotation/VSP_028750|||http://purl.uniprot.org/annotation/VSP_051721|||http://purl.uniprot.org/annotation/VSP_051722|||http://purl.uniprot.org/annotation/VSP_051723|||http://purl.uniprot.org/annotation/VSP_051724
http://togogenome.org/gene/9606:FA2H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5A8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||Fatty acid 2-hydroxylase|||Fatty acid hydroxylase|||Helical|||In SPG35.|||In SPG35; patients present spastic paraparesis associated with leukodystrophy and dystonia.|||In SPG35; significantly reduced enzymatic function.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312349|||http://purl.uniprot.org/annotation/VAR_037503|||http://purl.uniprot.org/annotation/VAR_054893|||http://purl.uniprot.org/annotation/VAR_064620|||http://purl.uniprot.org/annotation/VAR_064621|||http://purl.uniprot.org/annotation/VAR_065245|||http://purl.uniprot.org/annotation/VSP_056135
http://togogenome.org/gene/9606:SETD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE22                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||SET|||SET domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300496|||http://purl.uniprot.org/annotation/VAR_034875|||http://purl.uniprot.org/annotation/VAR_034876|||http://purl.uniprot.org/annotation/VSP_043790|||http://purl.uniprot.org/annotation/VSP_043791
http://togogenome.org/gene/9606:CAGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC20                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cancer-associated gene 1 protein|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280750|||http://purl.uniprot.org/annotation/VAR_031200|||http://purl.uniprot.org/annotation/VAR_031201|||http://purl.uniprot.org/annotation/VSP_023902|||http://purl.uniprot.org/annotation/VSP_023969|||http://purl.uniprot.org/annotation/VSP_023970|||http://purl.uniprot.org/annotation/VSP_023971|||http://purl.uniprot.org/annotation/VSP_047149
http://togogenome.org/gene/9606:SYCP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFB8|||http://purl.uniprot.org/uniprot/Q5T4T6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes localization to centromeres.|||Basic and acidic residues|||Disordered|||Does not affect localization to centromeres.|||In isoform 2.|||Polar residues|||Synaptonemal complex protein 2 Spt16M-like|||Synaptonemal complex protein 2 armadillo-repeat-like|||Synaptonemal complex protein 2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333809|||http://purl.uniprot.org/annotation/VAR_043169|||http://purl.uniprot.org/annotation/VAR_043170|||http://purl.uniprot.org/annotation/VAR_043171|||http://purl.uniprot.org/annotation/VAR_069417|||http://purl.uniprot.org/annotation/VAR_079007|||http://purl.uniprot.org/annotation/VAR_079008|||http://purl.uniprot.org/annotation/VSP_033545
http://togogenome.org/gene/9606:CGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2M7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cingulin|||Disordered|||Head|||In isoform 2.|||Interaction with TJP1/ZO1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail|||ZIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089763|||http://purl.uniprot.org/annotation/VAR_057809|||http://purl.uniprot.org/annotation/VSP_037039|||http://purl.uniprot.org/annotation/VSP_037040
http://togogenome.org/gene/9606:CFLAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A336TY74|||http://purl.uniprot.org/uniprot/B4E361|||http://purl.uniprot.org/uniprot/E9PAP3|||http://purl.uniprot.org/uniprot/O15519|||http://purl.uniprot.org/uniprot/Q59F61                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes proteolytic processing.|||CASP8 and FADD-like apoptosis regulator subunit p12|||CASP8 and FADD-like apoptosis regulator subunit p43|||Caspase|||Caspase family p20|||Cleavage; by CASP8|||DED|||DED 1|||DED 2|||Decreases apoptosis-inducing activity. Reduces interaction with caspase-3 and proteolytic processing.|||In isoform 10.|||In isoform 11, isoform 7 and isoform 3.|||In isoform 12.|||In isoform 13.|||In isoform 14.|||In isoform 2.|||In isoform 3, isoform 7 and isoform 15.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 9.|||In isoform 9.|||Interaction with CASP3|||Interaction with CASP8|||Interaction with CASP8 propeptide|||Interaction with CASP8 subunits p18 and p10|||Interaction with FADD|||Interaction with TRAF1 and TRAF2|||Not proteolytically processed and involved in apoptosis inhibition                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004678|||http://purl.uniprot.org/annotation/PRO_0000004679|||http://purl.uniprot.org/annotation/VAR_048619|||http://purl.uniprot.org/annotation/VSP_000824|||http://purl.uniprot.org/annotation/VSP_000825|||http://purl.uniprot.org/annotation/VSP_000826|||http://purl.uniprot.org/annotation/VSP_000827|||http://purl.uniprot.org/annotation/VSP_000828|||http://purl.uniprot.org/annotation/VSP_000829|||http://purl.uniprot.org/annotation/VSP_000830|||http://purl.uniprot.org/annotation/VSP_000831|||http://purl.uniprot.org/annotation/VSP_000832|||http://purl.uniprot.org/annotation/VSP_000833|||http://purl.uniprot.org/annotation/VSP_000834|||http://purl.uniprot.org/annotation/VSP_000835|||http://purl.uniprot.org/annotation/VSP_000836|||http://purl.uniprot.org/annotation/VSP_000837|||http://purl.uniprot.org/annotation/VSP_000838|||http://purl.uniprot.org/annotation/VSP_000839|||http://purl.uniprot.org/annotation/VSP_000840|||http://purl.uniprot.org/annotation/VSP_000841
http://togogenome.org/gene/9606:HSPB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12988|||http://purl.uniprot.org/uniprot/Q6ICS9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant                                                                                  ^@                                                                                  Heat shock protein beta-3|||In HMN2C.|||SHSP|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125936|||http://purl.uniprot.org/annotation/VAR_061271|||http://purl.uniprot.org/annotation/VAR_063773
http://togogenome.org/gene/9606:CREB3L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEY5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage by SP1.|||Basic motif|||Cleavage; by PS1|||Cyclic AMP-responsive element-binding protein 3-like protein 4|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Leucine-zipper|||Lumenal|||N-linked (GlcNAc...) asparagine|||Processed cyclic AMP-responsive element-binding protein 3-like protein 4|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288079|||http://purl.uniprot.org/annotation/PRO_0000296219|||http://purl.uniprot.org/annotation/VAR_048444|||http://purl.uniprot.org/annotation/VSP_045426
http://togogenome.org/gene/9606:DPPA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Developmental pluripotency-associated 5 protein|||KH; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311975
http://togogenome.org/gene/9606:RANBP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP49|||http://purl.uniprot.org/uniprot/Q6VN20                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  B30.2/SPRY|||CTLH|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||LisH|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Ran-binding protein 10|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305237|||http://purl.uniprot.org/annotation/VSP_055839|||http://purl.uniprot.org/annotation/VSP_055840|||http://purl.uniprot.org/annotation/VSP_055841
http://togogenome.org/gene/9606:NPBWR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NIL7|||http://purl.uniprot.org/uniprot/P48145                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Neuropeptides B/W receptor type 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069518|||http://purl.uniprot.org/annotation/VAR_035765|||http://purl.uniprot.org/annotation/VAR_047788|||http://purl.uniprot.org/annotation/VAR_047789
http://togogenome.org/gene/9606:TUBGCP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WU06|||http://purl.uniprot.org/uniprot/B4DYP7|||http://purl.uniprot.org/uniprot/Q96CW5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gamma tubulin complex component C-terminal|||Gamma tubulin complex component protein N-terminal|||Gamma-tubulin complex component 3|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078118|||http://purl.uniprot.org/annotation/VAR_049251|||http://purl.uniprot.org/annotation/VSP_001620|||http://purl.uniprot.org/annotation/VSP_001621|||http://purl.uniprot.org/annotation/VSP_001622|||http://purl.uniprot.org/annotation/VSP_001623
http://togogenome.org/gene/9606:ICE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2F5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Little elongation complex subunit 1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295724|||http://purl.uniprot.org/annotation/VAR_033341|||http://purl.uniprot.org/annotation/VAR_033342|||http://purl.uniprot.org/annotation/VAR_033343|||http://purl.uniprot.org/annotation/VAR_033344|||http://purl.uniprot.org/annotation/VAR_033345|||http://purl.uniprot.org/annotation/VAR_033346|||http://purl.uniprot.org/annotation/VAR_055943
http://togogenome.org/gene/9606:H3-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16695                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1t|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221248
http://togogenome.org/gene/9606:CNTN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWV2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Contactin-4|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated serine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014711|||http://purl.uniprot.org/annotation/PRO_0000014712|||http://purl.uniprot.org/annotation/VAR_035507|||http://purl.uniprot.org/annotation/VAR_035508|||http://purl.uniprot.org/annotation/VSP_011961|||http://purl.uniprot.org/annotation/VSP_011962|||http://purl.uniprot.org/annotation/VSP_044270
http://togogenome.org/gene/9606:ADAMTS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6REX0|||http://purl.uniprot.org/uniprot/P58397                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 12|||Basic and acidic residues|||Cysteine switch|||Disintegrin|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Peptidase M12B propeptide|||Polar residues|||Pro residues|||Spacer 1|||Spacer 2|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029186|||http://purl.uniprot.org/annotation/PRO_0000029187|||http://purl.uniprot.org/annotation/PRO_5003087765|||http://purl.uniprot.org/annotation/VAR_057074|||http://purl.uniprot.org/annotation/VAR_057075|||http://purl.uniprot.org/annotation/VAR_058972|||http://purl.uniprot.org/annotation/VAR_059761|||http://purl.uniprot.org/annotation/VAR_059762|||http://purl.uniprot.org/annotation/VSP_013141|||http://purl.uniprot.org/annotation/VSP_013142|||http://purl.uniprot.org/annotation/VSP_038151
http://togogenome.org/gene/9606:SBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95248                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRAM|||In CMT4B3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Myotubularin phosphatase|||Myotubularin-related protein 5|||N6-methyllysine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094938|||http://purl.uniprot.org/annotation/VAR_070046|||http://purl.uniprot.org/annotation/VAR_070047|||http://purl.uniprot.org/annotation/VSP_015158|||http://purl.uniprot.org/annotation/VSP_059427
http://togogenome.org/gene/9606:ZDHHC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY34|||http://purl.uniprot.org/uniprot/Q96MV8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Lumenal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC15|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212893|||http://purl.uniprot.org/annotation/VSP_013206|||http://purl.uniprot.org/annotation/VSP_013207|||http://purl.uniprot.org/annotation/VSP_013208
http://togogenome.org/gene/9606:WNT16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBV4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||In isoform Wnt-16a.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041471|||http://purl.uniprot.org/annotation/VAR_036289|||http://purl.uniprot.org/annotation/VAR_052957|||http://purl.uniprot.org/annotation/VAR_052958|||http://purl.uniprot.org/annotation/VSP_006797
http://togogenome.org/gene/9606:ZFAND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCF1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066580|||http://purl.uniprot.org/annotation/VSP_014988|||http://purl.uniprot.org/annotation/VSP_046404|||http://purl.uniprot.org/annotation/VSP_054080|||http://purl.uniprot.org/annotation/VSP_054081
http://togogenome.org/gene/9606:CDK5RAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JB5                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alters cleavage by CASP3 in vitro. Prevents apoptosis-induced cleavage in vivo; when associated with E-268 and E-282.|||Alters cleavage by CASP3 in vitro. Prevents apoptosis-induced cleavage in vivo; when associated with E-268 and E-311.|||Alters cleavage by CASP3 in vitro. Prevents apoptosis-induced cleavage in vivo; when associated with E-282 and E-311.|||CDK5 regulatory subunit-associated protein 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Required for interaction with UFL1 and mediates interaction with CHEK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220516|||http://purl.uniprot.org/annotation/VAR_048688|||http://purl.uniprot.org/annotation/VSP_007566|||http://purl.uniprot.org/annotation/VSP_007567|||http://purl.uniprot.org/annotation/VSP_007568|||http://purl.uniprot.org/annotation/VSP_055646
http://togogenome.org/gene/9606:MRFAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y605                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  MORF4 family-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306176
http://togogenome.org/gene/9606:DENND5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1S3|||http://purl.uniprot.org/uniprot/Q6ZUT9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DENN domain-containing protein 5B|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||PLAT|||Phosphoserine|||Phosphothreonine|||RUN|||RUN 1|||RUN 2|||Removed|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326531|||http://purl.uniprot.org/annotation/VAR_040076|||http://purl.uniprot.org/annotation/VAR_040077|||http://purl.uniprot.org/annotation/VSP_032672|||http://purl.uniprot.org/annotation/VSP_032673|||http://purl.uniprot.org/annotation/VSP_032674|||http://purl.uniprot.org/annotation/VSP_032675|||http://purl.uniprot.org/annotation/VSP_032676|||http://purl.uniprot.org/annotation/VSP_032677|||http://purl.uniprot.org/annotation/VSP_032678
http://togogenome.org/gene/9606:P3H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92791                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Endoplasmic reticulum protein SC65|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150367|||http://purl.uniprot.org/annotation/VAR_020417
http://togogenome.org/gene/9606:ECRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1Z8                                                                                  ^@                                                                                  Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Augurin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250514|||http://purl.uniprot.org/annotation/PRO_0000363237|||http://purl.uniprot.org/annotation/PRO_0000363238|||http://purl.uniprot.org/annotation/VAR_050962
http://togogenome.org/gene/9606:TMBIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSM0|||http://purl.uniprot.org/uniprot/B4DUD2|||http://purl.uniprot.org/uniprot/Q969X1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Pro residues|||Protein lifeguard 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179090|||http://purl.uniprot.org/annotation/VAR_017382
http://togogenome.org/gene/9606:SRGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43295                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-BAR|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Rho-GAP|||SH3|||SLIT-ROBO Rho GTPase-activating protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056769|||http://purl.uniprot.org/annotation/VAR_035550|||http://purl.uniprot.org/annotation/VAR_049159|||http://purl.uniprot.org/annotation/VSP_010581|||http://purl.uniprot.org/annotation/VSP_010582|||http://purl.uniprot.org/annotation/VSP_010583
http://togogenome.org/gene/9606:H2AC21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUE6                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 2-B|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227505|||http://purl.uniprot.org/annotation/VAR_035802
http://togogenome.org/gene/9606:PPM1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULR3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Decreased enzymatic activity.|||Disordered|||Omega-N-methylarginine|||PPM-type phosphatase|||Phosphoserine|||Phosphothreonine|||Protein phosphatase 1H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286603
http://togogenome.org/gene/9606:TEDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SX3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||Tubulin epsilon and delta complex protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330692|||http://purl.uniprot.org/annotation/VSP_033062|||http://purl.uniprot.org/annotation/VSP_033063|||http://purl.uniprot.org/annotation/VSP_033064|||http://purl.uniprot.org/annotation/VSP_033065|||http://purl.uniprot.org/annotation/VSP_033066|||http://purl.uniprot.org/annotation/VSP_045690
http://togogenome.org/gene/9606:RAP1GDS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNU0|||http://purl.uniprot.org/uniprot/P52306|||http://purl.uniprot.org/uniprot/Q6U7G8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein|||Critical for catalytic activity|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 6.|||Interacts with polybasic regions in GTPases|||N6-acetyllysine|||Nuclear export signal (NES)|||Prevents binding to prenylated RHOA|||Rap1 GTPase-GDP dissociation stimulator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056759|||http://purl.uniprot.org/annotation/VAR_049158|||http://purl.uniprot.org/annotation/VAR_069149|||http://purl.uniprot.org/annotation/VSP_001658|||http://purl.uniprot.org/annotation/VSP_043660|||http://purl.uniprot.org/annotation/VSP_046214|||http://purl.uniprot.org/annotation/VSP_047041
http://togogenome.org/gene/9606:NPHS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60500                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Binds to NPHS2|||Cytoplasmic|||Disordered|||Does not affect protein expression on the cell surface.|||Extracellular|||Fibronectin type-III|||Found in patients with nephrotic syndrome; unknown pathological significance.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||In NPHS1.|||In NPHS1; benign variant.|||In NPHS1; does not affect protein expression on the cell surface.|||In NPHS1; lack of protein expression on the cell surface.|||In NPHS1; lack of protein expression on the cell surface; the mutant protein is retained in the endoplasmic reticulum.|||In NPHS1; the mutant protein is retained in the endoplasmic reticulum.|||In NPHS1; unknown pathological significance.|||In isoform 2.|||Increased mTORC1 complex activation.|||N-linked (GlcNAc...) asparagine|||Nephrin|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by FYN|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015052|||http://purl.uniprot.org/annotation/VAR_013029|||http://purl.uniprot.org/annotation/VAR_013030|||http://purl.uniprot.org/annotation/VAR_013031|||http://purl.uniprot.org/annotation/VAR_013032|||http://purl.uniprot.org/annotation/VAR_013033|||http://purl.uniprot.org/annotation/VAR_013034|||http://purl.uniprot.org/annotation/VAR_013035|||http://purl.uniprot.org/annotation/VAR_013036|||http://purl.uniprot.org/annotation/VAR_013037|||http://purl.uniprot.org/annotation/VAR_013038|||http://purl.uniprot.org/annotation/VAR_013039|||http://purl.uniprot.org/annotation/VAR_013040|||http://purl.uniprot.org/annotation/VAR_013041|||http://purl.uniprot.org/annotation/VAR_013042|||http://purl.uniprot.org/annotation/VAR_013043|||http://purl.uniprot.org/annotation/VAR_013044|||http://purl.uniprot.org/annotation/VAR_013045|||http://purl.uniprot.org/annotation/VAR_013046|||http://purl.uniprot.org/annotation/VAR_013047|||http://purl.uniprot.org/annotation/VAR_013048|||http://purl.uniprot.org/annotation/VAR_013049|||http://purl.uniprot.org/annotation/VAR_013050|||http://purl.uniprot.org/annotation/VAR_013051|||http://purl.uniprot.org/annotation/VAR_013052|||http://purl.uniprot.org/annotation/VAR_013053|||http://purl.uniprot.org/annotation/VAR_013054|||http://purl.uniprot.org/annotation/VAR_013055|||http://purl.uniprot.org/annotation/VAR_049970|||http://purl.uniprot.org/annotation/VAR_049971|||http://purl.uniprot.org/annotation/VAR_049972|||http://purl.uniprot.org/annotation/VAR_064194|||http://purl.uniprot.org/annotation/VAR_064195|||http://purl.uniprot.org/annotation/VAR_064196|||http://purl.uniprot.org/annotation/VAR_064197|||http://purl.uniprot.org/annotation/VAR_064198|||http://purl.uniprot.org/annotation/VAR_064199|||http://purl.uniprot.org/annotation/VAR_064200|||http://purl.uniprot.org/annotation/VAR_064201|||http://purl.uniprot.org/annotation/VAR_064202|||http://purl.uniprot.org/annotation/VAR_064203|||http://purl.uniprot.org/annotation/VAR_064204|||http://purl.uniprot.org/annotation/VAR_064205|||http://purl.uniprot.org/annotation/VAR_064206|||http://purl.uniprot.org/annotation/VAR_064207|||http://purl.uniprot.org/annotation/VAR_064208|||http://purl.uniprot.org/annotation/VAR_064209|||http://purl.uniprot.org/annotation/VAR_064210|||http://purl.uniprot.org/annotation/VAR_064211|||http://purl.uniprot.org/annotation/VAR_064212|||http://purl.uniprot.org/annotation/VAR_064213|||http://purl.uniprot.org/annotation/VAR_064214|||http://purl.uniprot.org/annotation/VAR_064215|||http://purl.uniprot.org/annotation/VAR_064216|||http://purl.uniprot.org/annotation/VAR_064217|||http://purl.uniprot.org/annotation/VAR_064218|||http://purl.uniprot.org/annotation/VAR_064219|||http://purl.uniprot.org/annotation/VAR_064220|||http://purl.uniprot.org/annotation/VAR_064221|||http://purl.uniprot.org/annotation/VAR_064222|||http://purl.uniprot.org/annotation/VAR_064223|||http://purl.uniprot.org/annotation/VAR_064224|||http://purl.uniprot.org/annotation/VAR_064225|||http://purl.uniprot.org/annotation/VAR_064226|||http://purl.uniprot.org/annotation/VAR_064227|||http://purl.uniprot.org/annotation/VAR_064228|||http://purl.uniprot.org/annotation/VAR_067252|||http://purl.uniprot.org/annotation/VAR_072161|||http://purl.uniprot.org/annotation/VAR_072162|||http://purl.uniprot.org/annotation/VAR_072163|||http://purl.uniprot.org/annotation/VAR_072375|||http://purl.uniprot.org/annotation/VAR_072376|||http://purl.uniprot.org/annotation/VAR_072377|||http://purl.uniprot.org/annotation/VAR_072378|||http://purl.uniprot.org/annotation/VAR_072379|||http://purl.uniprot.org/annotation/VAR_075252|||http://purl.uniprot.org/annotation/VAR_075253|||http://purl.uniprot.org/annotation/VAR_075254|||http://purl.uniprot.org/annotation/VAR_079794|||http://purl.uniprot.org/annotation/VAR_079795|||http://purl.uniprot.org/annotation/VAR_079796|||http://purl.uniprot.org/annotation/VSP_002598
http://togogenome.org/gene/9606:BCL9L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZX0|||http://purl.uniprot.org/uniprot/Q86UU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||B-cell CLL/lymphoma 9-like protein|||B-cell lymphoma 9 beta-catenin binding|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Necessary for interaction with CTNNB1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314079|||http://purl.uniprot.org/annotation/VSP_030205|||http://purl.uniprot.org/annotation/VSP_030206|||http://purl.uniprot.org/annotation/VSP_030207|||http://purl.uniprot.org/annotation/VSP_030208
http://togogenome.org/gene/9606:FLNC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14315|||http://purl.uniprot.org/uniprot/Q59H94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Actin-binding|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Does not affect sarcomere structure or contractile performance in mutant induced pluripotent stem cell-derived cardiomyocytes.|||Filamin|||Filamin 1|||Filamin 10|||Filamin 11|||Filamin 12|||Filamin 13|||Filamin 14|||Filamin 15|||Filamin 16|||Filamin 17|||Filamin 18|||Filamin 19|||Filamin 2|||Filamin 20; mediates interaction with XIRP1|||Filamin 21|||Filamin 22|||Filamin 23|||Filamin 24|||Filamin 3|||Filamin 4|||Filamin 5|||Filamin 6|||Filamin 7|||Filamin 8|||Filamin 9|||Filamin-C|||Hinge 1|||Hinge 2|||In CMH26; increased actin aggregation; localized in perinuclear region of cytoplasm.|||In CMH26; increased aggregation; localized in perinuclear region of cytoplasm.|||In CMH26; unknown pathological significance.|||In CMH26; unknown pathological significance; increased aggregation; localized in perinuclear region of cytoplasm.|||In MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in significantly decreased nuclear localization with formation of intracellular protein aggregates.|||In MPD4; results in slightly decreased thermal stability and increased actin-binding activity; results in the formation of intracellular protein aggregates.|||In RCM5; increased protein aggregates; effect on cytoplasm localization; localized in perinuclear region of cytoplasm; no effect on expression.|||In RCM5; no effect on cytoplasm localization; no effect on expression.|||In isoform 2.|||Interaction with INPPL1|||Intradomain insert; mediate targeting to Z lines|||No effect on sarcomere structure or contractile performance in mutant induced pluripotent stem cell-derived cardiomyocytes.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Self-association site, tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087301|||http://purl.uniprot.org/annotation/VAR_015705|||http://purl.uniprot.org/annotation/VAR_015706|||http://purl.uniprot.org/annotation/VAR_015707|||http://purl.uniprot.org/annotation/VAR_015708|||http://purl.uniprot.org/annotation/VAR_015709|||http://purl.uniprot.org/annotation/VAR_015710|||http://purl.uniprot.org/annotation/VAR_015711|||http://purl.uniprot.org/annotation/VAR_066212|||http://purl.uniprot.org/annotation/VAR_066213|||http://purl.uniprot.org/annotation/VAR_077036|||http://purl.uniprot.org/annotation/VAR_077037|||http://purl.uniprot.org/annotation/VAR_077038|||http://purl.uniprot.org/annotation/VAR_077039|||http://purl.uniprot.org/annotation/VAR_077040|||http://purl.uniprot.org/annotation/VAR_077041|||http://purl.uniprot.org/annotation/VAR_077042|||http://purl.uniprot.org/annotation/VAR_077043|||http://purl.uniprot.org/annotation/VAR_085683|||http://purl.uniprot.org/annotation/VSP_007579
http://togogenome.org/gene/9606:POLI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNA4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA polymerase iota|||DNA-binding|||Disordered|||Large decrease in catalytic activity efficiency which is partially rescued by the presence of Mn(2+) instead Mg(2+).|||Polar residues|||Proton acceptor|||Small decrease in catalytic activity efficiency which is partially rescued by the presence of Mn(2+) instead Mg(2+).|||Ubiquitin-binding 1 (UBM1)|||Ubiquitin-binding 2 (UBM2)|||UmuC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173988|||http://purl.uniprot.org/annotation/VAR_021239|||http://purl.uniprot.org/annotation/VAR_021240|||http://purl.uniprot.org/annotation/VAR_021241|||http://purl.uniprot.org/annotation/VAR_021242|||http://purl.uniprot.org/annotation/VAR_021243|||http://purl.uniprot.org/annotation/VAR_021244|||http://purl.uniprot.org/annotation/VAR_021245
http://togogenome.org/gene/9606:OR2T12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG77                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150504|||http://purl.uniprot.org/annotation/VAR_053157|||http://purl.uniprot.org/annotation/VAR_060003|||http://purl.uniprot.org/annotation/VAR_060004|||http://purl.uniprot.org/annotation/VAR_060005|||http://purl.uniprot.org/annotation/VAR_060006
http://togogenome.org/gene/9606:TIMD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||T-cell immunoglobulin and mucin domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042103|||http://purl.uniprot.org/annotation/VAR_049946|||http://purl.uniprot.org/annotation/VAR_049947|||http://purl.uniprot.org/annotation/VSP_045474
http://togogenome.org/gene/9606:TMSB15A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG34|||http://purl.uniprot.org/uniprot/P0CG35|||http://purl.uniprot.org/uniprot/P0DX04                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Removed|||Thymosin beta-15A|||Thymosin beta-15B|||Thymosin beta-15C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185159|||http://purl.uniprot.org/annotation/PRO_0000395401|||http://purl.uniprot.org/annotation/PRO_0000457394
http://togogenome.org/gene/9606:COA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z2J3|||http://purl.uniprot.org/uniprot/Q9GZY4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly factor 1 homolog|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279407
http://togogenome.org/gene/9606:TRIM66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Z5E822|||http://purl.uniprot.org/uniprot/A0A994J7V7|||http://purl.uniprot.org/uniprot/O15016                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B box-type 1; atypical|||B box-type 2|||Basic and acidic residues|||Bromo|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||PHD-type|||Polar residues|||Pro residues|||PxVxL motif|||Tripartite motif-containing protein 66                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220375|||http://purl.uniprot.org/annotation/VSP_061677|||http://purl.uniprot.org/annotation/VSP_061678|||http://purl.uniprot.org/annotation/VSP_061679|||http://purl.uniprot.org/annotation/VSP_061680|||http://purl.uniprot.org/annotation/VSP_061681
http://togogenome.org/gene/9606:ALG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y673                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dolichyl-phosphate beta-glucosyltransferase|||Helical; Signal-anchor for type II membrane protein|||In PKD7.|||In PKD7; unable to rescue defective PKD1 glycosylation and maturation in ALG5-deficient cells.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059098|||http://purl.uniprot.org/annotation/VAR_087727|||http://purl.uniprot.org/annotation/VAR_087728|||http://purl.uniprot.org/annotation/VAR_087729|||http://purl.uniprot.org/annotation/VSP_041019
http://togogenome.org/gene/9606:CCDC91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D28|||http://purl.uniprot.org/uniprot/Q7Z6B0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 91|||Disordered|||GGA1-binding motif|||Homodimerization|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087478|||http://purl.uniprot.org/annotation/VAR_021531|||http://purl.uniprot.org/annotation/VAR_021532|||http://purl.uniprot.org/annotation/VSP_013243|||http://purl.uniprot.org/annotation/VSP_013244
http://togogenome.org/gene/9606:MELK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1G6|||http://purl.uniprot.org/uniprot/Q14680                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation of serine/threonine-protein kinase activity and has only weak activity.|||Abolishes autophosphorylation on tyrosine but still active on exogenous substrates.|||Abolishes dependence to reducing agents; when associated with V-29; A-89; A-154; A-168; A-169; A-204; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-154; A-168; A-169; A-204; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204 and A-286.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-204; and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-169; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-168; A-204; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-154; A-169; A-204; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-29; V-70; A-89; A-168; A-169; A-204; A-286 and A-339.|||Abolishes dependence to reducing agents; when associated with V-70; A-89; A-154; A-168; A-169; A-204; A-286 and A-339.|||Abolishes enzymatic activity.|||Autoinhibitory region|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Inactive.|||Inhibits interaction with PPP1R8.|||KA1|||Maternal embryonic leucine zipper kinase|||No effect on interaction with PPP1R8.|||Phosphomimetic mutant that has similar kinase activity as wild-type.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity.|||UBA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086323|||http://purl.uniprot.org/annotation/VAR_040794|||http://purl.uniprot.org/annotation/VAR_040795|||http://purl.uniprot.org/annotation/VAR_040796|||http://purl.uniprot.org/annotation/VAR_040797|||http://purl.uniprot.org/annotation/VAR_040798|||http://purl.uniprot.org/annotation/VSP_044715|||http://purl.uniprot.org/annotation/VSP_045208|||http://purl.uniprot.org/annotation/VSP_045209|||http://purl.uniprot.org/annotation/VSP_045430|||http://purl.uniprot.org/annotation/VSP_045431|||http://purl.uniprot.org/annotation/VSP_046759|||http://purl.uniprot.org/annotation/VSP_046760
http://togogenome.org/gene/9606:LBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14739                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic residues|||Delta(14)-sterol reductase LBR|||Disordered|||Helical|||In GRBGD; significant reduction in affinity for NADPH; loss of cholesterol biosynthesis; does not affect protein stability.|||In PHA.|||In REYNS.|||In SKPHA.|||In SKPHA; unknown pathological significance.|||N6-acetyllysine|||Nuclear|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207510|||http://purl.uniprot.org/annotation/VAR_017841|||http://purl.uniprot.org/annotation/VAR_017842|||http://purl.uniprot.org/annotation/VAR_020209|||http://purl.uniprot.org/annotation/VAR_024318|||http://purl.uniprot.org/annotation/VAR_052155|||http://purl.uniprot.org/annotation/VAR_063811|||http://purl.uniprot.org/annotation/VAR_081005|||http://purl.uniprot.org/annotation/VAR_081006|||http://purl.uniprot.org/annotation/VAR_081007|||http://purl.uniprot.org/annotation/VAR_081220|||http://purl.uniprot.org/annotation/VAR_081221
http://togogenome.org/gene/9606:GRIK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8D9PH79|||http://purl.uniprot.org/uniprot/A0A8D9UJ88|||http://purl.uniprot.org/uniprot/A6H8K8|||http://purl.uniprot.org/uniprot/B2RAP6|||http://purl.uniprot.org/uniprot/Q16099                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor|||Glutamate receptor ionotropic, kainate 4|||Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011549|||http://purl.uniprot.org/annotation/PRO_5014297001|||http://purl.uniprot.org/annotation/PRO_5027143014|||http://purl.uniprot.org/annotation/PRO_5034275875|||http://purl.uniprot.org/annotation/PRO_5034945418|||http://purl.uniprot.org/annotation/VAR_046998|||http://purl.uniprot.org/annotation/VAR_046999
http://togogenome.org/gene/9606:TMEM37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EMC0|||http://purl.uniprot.org/uniprot/Q86SV2|||http://purl.uniprot.org/uniprot/Q8WXS4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Voltage-dependent calcium channel gamma-like subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225601
http://togogenome.org/gene/9606:DUS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1R4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Proton donor|||tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247226
http://togogenome.org/gene/9606:SGCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13326                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-sarcoglycan|||Helical; Signal-anchor for type II membrane protein|||In LGMDR5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175248|||http://purl.uniprot.org/annotation/VAR_010397|||http://purl.uniprot.org/annotation/VAR_010398|||http://purl.uniprot.org/annotation/VAR_010399|||http://purl.uniprot.org/annotation/VAR_010430|||http://purl.uniprot.org/annotation/VAR_012202|||http://purl.uniprot.org/annotation/VAR_081101
http://togogenome.org/gene/9606:PDXK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z2Y4|||http://purl.uniprot.org/uniprot/O00764|||http://purl.uniprot.org/uniprot/V9HWC3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  15-fold decrease in pyridoxal kinase activity, and a 7-fold decrease in affinity for pyridoxal.|||2-fold decrease in pyridoxal kinase activity and pyridoxal affinity.|||In HMSN6C; decreased pyridoxal kinase activity.|||In HMSN6C; decreased pyridoxal kinase activity; decreased affinity for ATP; decreased affinity for pyridoxal 5'-phosphate; no effect on protein abundance.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Proton acceptor|||Pyridoxal kinase|||Pyridoxamine kinase/Phosphomethylpyrimidine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213335|||http://purl.uniprot.org/annotation/VAR_083156|||http://purl.uniprot.org/annotation/VAR_083157|||http://purl.uniprot.org/annotation/VSP_004653|||http://purl.uniprot.org/annotation/VSP_010671
http://togogenome.org/gene/9606:CLASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ERI8|||http://purl.uniprot.org/uniprot/O75122                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CLIP-associating protein 2|||Decreases affinity for microtubules; when associated with A-191; E-667; E-833; A-838 and A-839.|||Decreases affinity for microtubules; when associated with E-106; A-191; E-667; A-838 and A-839.|||Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-838.|||Decreases affinity for microtubules; when associated with E-106; A-191; E-667; E-833 and A-839.|||Decreases affinity for microtubules; when associated with E-106; A-191; E-833; A-838 and A-839.|||Decreases affinity for microtubules; when associated with E-106; E-667; E-833; A-838 and A-839.|||Disordered|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||In isoform 2.|||In isoform 3.|||Interaction with RSN and localization to the Golgi and kinetochores|||Interaction with microtubules, MAPRE1 and MAPRE3|||No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 496-A-A-497.|||No effect on MAPRE1 binding. Abolishes interaction with MAPRE1; when associated with 519-A-A-520.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-537.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-533 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-529; D-537 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-525; D-533; D-537 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-507; D-529; D-533; D-537 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-503; D-525; D-529; D-533; D-537 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-499; D-507; D-525; D-529; D-533; D-537 and D-541.|||Phosphomimetic mutant that reduces MAPRE1 binding; when associated with D-503; D-507; D-525; D-529; D-533; D-537 and D-541.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 496-S-S-497.|||Reduced targeting to the growing microtubule plus ends. Loss of interaction with MAPRE1 and targeting to the growing microtubule plus ends; when associated with 519-S-S-520.|||Required for cortical localization|||SXIP motif 1; mediates interaction with MAPRE1 and targeting to microtubule plus ends|||SXIP motif 2; mediates interaction with MAPRE1 and targeting to microtubule plus ends|||TOG|||TOG 1|||TOG 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089849|||http://purl.uniprot.org/annotation/VSP_015805|||http://purl.uniprot.org/annotation/VSP_015806|||http://purl.uniprot.org/annotation/VSP_015807|||http://purl.uniprot.org/annotation/VSP_057273|||http://purl.uniprot.org/annotation/VSP_057274|||http://purl.uniprot.org/annotation/VSP_057275|||http://purl.uniprot.org/annotation/VSP_057276
http://togogenome.org/gene/9606:C16orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolished phosphorylation and interaction with PPP3CA.|||Abolishes interaction with PPP3CA.|||In isoform 2.|||No effect on phosphorylation.|||Phosphothreonine|||Required for interaction with PPP3CA|||Uncharacterized protein C16orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264621|||http://purl.uniprot.org/annotation/VSP_061477
http://togogenome.org/gene/9606:SLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13239                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-224.|||Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-229.|||Abolishes interaction with CBL. Does not affect dimerization; when associated with S-224 and S-229.|||Abolishes interaction with CBL. Slightly affects dimerization.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Removed|||SH2|||SH3|||SLA C-terminal|||Src-like-adapter|||Strongly reduces interaction with ZAP70, CD3Z, SYK and LAT.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071946|||http://purl.uniprot.org/annotation/VAR_061706|||http://purl.uniprot.org/annotation/VSP_055122|||http://purl.uniprot.org/annotation/VSP_055123|||http://purl.uniprot.org/annotation/VSP_055124|||http://purl.uniprot.org/annotation/VSP_055125
http://togogenome.org/gene/9606:DSN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3X3|||http://purl.uniprot.org/uniprot/Q9H410                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kinetochore-associated protein DSN1 homolog|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079481|||http://purl.uniprot.org/annotation/VSP_003826|||http://purl.uniprot.org/annotation/VSP_043204|||http://purl.uniprot.org/annotation/VSP_044281
http://togogenome.org/gene/9606:LCMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60294                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||tRNA wybutosine-synthesizing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204423|||http://purl.uniprot.org/annotation/VAR_022081|||http://purl.uniprot.org/annotation/VAR_023378|||http://purl.uniprot.org/annotation/VAR_023379|||http://purl.uniprot.org/annotation/VAR_023380
http://togogenome.org/gene/9606:BDNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0E3SU01|||http://purl.uniprot.org/uniprot/P23560                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes processing by MBTPS1.|||BDNF precursor form|||Brain-derived neurotrophic factor|||Cleavage; by MBTPS1|||Found in a patient with congenital central hypoventilation syndrome; unknown pathological significance.|||Found in a small consanguineous family with intellectual disability; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Nerve growth factor-related|||Strongly associated with susceptibility to eating disorders such as anorexia nervosa and bulimia nervosa; associated with poorer episodic memory; may have a protective effect in obsessive-compulsive disorder; impairs localization to secretory granules or synapses; decreases density of dendritic mushroom spines and synapses.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019633|||http://purl.uniprot.org/annotation/PRO_0000019634|||http://purl.uniprot.org/annotation/PRO_0000447533|||http://purl.uniprot.org/annotation/PRO_5014203264|||http://purl.uniprot.org/annotation/VAR_004626|||http://purl.uniprot.org/annotation/VAR_011797|||http://purl.uniprot.org/annotation/VAR_011798|||http://purl.uniprot.org/annotation/VAR_011799|||http://purl.uniprot.org/annotation/VAR_018260|||http://purl.uniprot.org/annotation/VAR_080766|||http://purl.uniprot.org/annotation/VSP_037948|||http://purl.uniprot.org/annotation/VSP_038099|||http://purl.uniprot.org/annotation/VSP_038100|||http://purl.uniprot.org/annotation/VSP_038101
http://togogenome.org/gene/9606:MS4A6E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DS6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 6E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158642|||http://purl.uniprot.org/annotation/VAR_015654|||http://purl.uniprot.org/annotation/VAR_053518|||http://purl.uniprot.org/annotation/VAR_053519
http://togogenome.org/gene/9606:SOX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06945                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Abolished acetylation by KAT5.|||Disordered|||Does not affect acetylation by KAT5.|||HMG box|||In IDDSDF; loss DNA-binding transcription factor activity.|||In IDDSDF; loss of DNA-binding transcription factor activity.|||N6-acetyllysine|||Polar residues|||Transcription factor SOX-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048724|||http://purl.uniprot.org/annotation/VAR_083360|||http://purl.uniprot.org/annotation/VAR_083361|||http://purl.uniprot.org/annotation/VAR_083362|||http://purl.uniprot.org/annotation/VAR_083363
http://togogenome.org/gene/9606:PRKAR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY43|||http://purl.uniprot.org/uniprot/P31323                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Dimerization and phosphorylation|||Disordered|||Phosphoserine|||Phosphothreonine|||cAMP-dependent protein kinase type II-beta regulatory subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205390|||http://purl.uniprot.org/annotation/VAR_046549
http://togogenome.org/gene/9606:ALDH8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2A2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  2-aminomuconic semialdehyde dehydrogenase|||About 65-fold loss of catalytic efficiency.|||Complete loss of activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312954|||http://purl.uniprot.org/annotation/VAR_037618|||http://purl.uniprot.org/annotation/VSP_029972|||http://purl.uniprot.org/annotation/VSP_039759|||http://purl.uniprot.org/annotation/VSP_039760|||http://purl.uniprot.org/annotation/VSP_043279
http://togogenome.org/gene/9606:GFRAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXV0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GDNF family receptor alpha-like|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Required for interaction with GDF15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240124|||http://purl.uniprot.org/annotation/VAR_036234|||http://purl.uniprot.org/annotation/VAR_053105|||http://purl.uniprot.org/annotation/VAR_053106
http://togogenome.org/gene/9606:IL17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16552                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Decreases the affinity for IL17RA by 5-fold.|||Decreases the affinity for IL17RA.|||Has no effect on the affinity for IL17RA.|||Impairs binding to IL17RA and IL17RC.|||Interleukin-17A|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015423
http://togogenome.org/gene/9606:EFCAB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZ26                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340648
http://togogenome.org/gene/9606:ZNF391                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJN7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Zinc finger protein 391                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299034|||http://purl.uniprot.org/annotation/VAR_034774|||http://purl.uniprot.org/annotation/VAR_034775
http://togogenome.org/gene/9606:HJV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K466|||http://purl.uniprot.org/uniprot/Q6ZVN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by autolysis|||Disordered|||GPI-anchor amidated aspartate|||Helical|||Hemojuvelin|||In HFE2A.|||In isoform b.|||In isoform c.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Removed in mature form|||Repulsive guidance molecule C-terminal|||Repulsive guidance molecule N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030398|||http://purl.uniprot.org/annotation/PRO_0000030399|||http://purl.uniprot.org/annotation/VAR_019617|||http://purl.uniprot.org/annotation/VAR_019618|||http://purl.uniprot.org/annotation/VAR_019619|||http://purl.uniprot.org/annotation/VAR_019620|||http://purl.uniprot.org/annotation/VAR_019621|||http://purl.uniprot.org/annotation/VAR_019622|||http://purl.uniprot.org/annotation/VAR_019623|||http://purl.uniprot.org/annotation/VAR_019624|||http://purl.uniprot.org/annotation/VAR_019625|||http://purl.uniprot.org/annotation/VAR_019626|||http://purl.uniprot.org/annotation/VAR_019627|||http://purl.uniprot.org/annotation/VAR_019628|||http://purl.uniprot.org/annotation/VAR_019629|||http://purl.uniprot.org/annotation/VAR_019927|||http://purl.uniprot.org/annotation/VAR_053636|||http://purl.uniprot.org/annotation/VSP_011319|||http://purl.uniprot.org/annotation/VSP_011320
http://togogenome.org/gene/9606:FAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAW7|||http://purl.uniprot.org/uniprot/B2RBI0|||http://purl.uniprot.org/uniprot/Q96K12|||http://purl.uniprot.org/uniprot/Q9NUX8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Fatty acyl-CoA reductase 2|||Fatty acyl-CoA reductase C-terminal|||Helical|||In isoform 2.|||Peroxisomal|||Thioester reductase (TE)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261401|||http://purl.uniprot.org/annotation/VSP_055648
http://togogenome.org/gene/9606:PROCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Endothelial protein C receptor|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021191|||http://purl.uniprot.org/annotation/VAR_012282
http://togogenome.org/gene/9606:C7orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU49                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C7orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089590
http://togogenome.org/gene/9606:SNTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13884                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-1-syntrophin|||Calmodulin-binding|||Disordered|||In isoform 2.|||N-acetylalanine|||PDZ|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SU                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184009|||http://purl.uniprot.org/annotation/VSP_006354|||http://purl.uniprot.org/annotation/VSP_006355
http://togogenome.org/gene/9606:MYL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12829                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||In ATFB18.|||Myosin light chain 4|||N,N,N-trimethylalanine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198699|||http://purl.uniprot.org/annotation/VAR_050458|||http://purl.uniprot.org/annotation/VAR_077959
http://togogenome.org/gene/9606:ZC3H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger CCCH domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213896|||http://purl.uniprot.org/annotation/VAR_018457|||http://purl.uniprot.org/annotation/VAR_018458|||http://purl.uniprot.org/annotation/VAR_018459|||http://purl.uniprot.org/annotation/VAR_018460|||http://purl.uniprot.org/annotation/VAR_018461|||http://purl.uniprot.org/annotation/VAR_057484|||http://purl.uniprot.org/annotation/VAR_057485|||http://purl.uniprot.org/annotation/VAR_057486|||http://purl.uniprot.org/annotation/VAR_057487|||http://purl.uniprot.org/annotation/VAR_057488|||http://purl.uniprot.org/annotation/VAR_060402|||http://purl.uniprot.org/annotation/VAR_060403|||http://purl.uniprot.org/annotation/VAR_060404|||http://purl.uniprot.org/annotation/VAR_060405|||http://purl.uniprot.org/annotation/VAR_060406|||http://purl.uniprot.org/annotation/VAR_060407|||http://purl.uniprot.org/annotation/VSP_010272|||http://purl.uniprot.org/annotation/VSP_010273
http://togogenome.org/gene/9606:GID8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWU2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  CTLH|||Glucose-induced degradation protein 8 homolog|||Interaction with CTNNB1|||LisH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079411
http://togogenome.org/gene/9606:WDPCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95876                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CHDTHP; impairs protein stability.|||In a patient with Bardet-Biedl syndrome compound heterozygous for mutations in BBS12.|||In a patient with Meckel syndrome compound heterozygous for mutations in CC2D2A.|||In isoform 2.|||In isoform 3.|||WD 1|||WD 2|||WD repeat-containing and planar cell polarity effector protein fritz homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325802|||http://purl.uniprot.org/annotation/VAR_039919|||http://purl.uniprot.org/annotation/VAR_064770|||http://purl.uniprot.org/annotation/VAR_064771|||http://purl.uniprot.org/annotation/VAR_064772|||http://purl.uniprot.org/annotation/VAR_073251|||http://purl.uniprot.org/annotation/VSP_032408|||http://purl.uniprot.org/annotation/VSP_032409|||http://purl.uniprot.org/annotation/VSP_032410
http://togogenome.org/gene/9606:E2F7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of DNA-binding and E2F-dependent repression.|||Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-185.|||Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-334.|||Phosphoserine|||Polar residues|||Transcription factor E2F7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298907|||http://purl.uniprot.org/annotation/VAR_034732|||http://purl.uniprot.org/annotation/VAR_034733|||http://purl.uniprot.org/annotation/VAR_034734|||http://purl.uniprot.org/annotation/VSP_027473|||http://purl.uniprot.org/annotation/VSP_027474|||http://purl.uniprot.org/annotation/VSP_044617
http://togogenome.org/gene/9606:CEACAM16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2WEN9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 16|||Ig-like C2-type 1|||Ig-like C2-type 2|||In DFNA4B.|||In DFNA4B; impairs homooligomerization of the protein; decreases secretion of the protein.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297564|||http://purl.uniprot.org/annotation/VAR_067769|||http://purl.uniprot.org/annotation/VAR_072720
http://togogenome.org/gene/9606:TMCO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RE09|||http://purl.uniprot.org/uniprot/Q6UWJ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cation/H+ exchanger|||Found in a patient with cornea guttata with anterior polar cataracts; unknown pathological significance.|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane and coiled-coil domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249856|||http://purl.uniprot.org/annotation/PRO_5014214300|||http://purl.uniprot.org/annotation/VAR_050037|||http://purl.uniprot.org/annotation/VAR_050038|||http://purl.uniprot.org/annotation/VAR_076964|||http://purl.uniprot.org/annotation/VSP_020561|||http://purl.uniprot.org/annotation/VSP_020562|||http://purl.uniprot.org/annotation/VSP_020563|||http://purl.uniprot.org/annotation/VSP_020564
http://togogenome.org/gene/9606:WFDC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K0|||http://purl.uniprot.org/uniprot/Q9BQY6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||In isoform 2.|||WAP|||WAP four-disulfide core domain protein 6|||WAP; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041383|||http://purl.uniprot.org/annotation/PRO_5014231573|||http://purl.uniprot.org/annotation/VSP_007550|||http://purl.uniprot.org/annotation/VSP_007551
http://togogenome.org/gene/9606:RHBDF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJF5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In TOC.|||In isoform 2.|||Inactive rhomboid protein 2|||Involved in interaction with FRMD8|||Lumenal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341938|||http://purl.uniprot.org/annotation/VAR_044125|||http://purl.uniprot.org/annotation/VAR_044126|||http://purl.uniprot.org/annotation/VAR_044127|||http://purl.uniprot.org/annotation/VAR_067827|||http://purl.uniprot.org/annotation/VAR_067828|||http://purl.uniprot.org/annotation/VSP_034368
http://togogenome.org/gene/9606:AAAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aladin|||Disordered|||In AAAS.|||In AAAS; unknown pathological significance.|||In isoform 2.|||Microbody targeting signal|||N-acetylcysteine|||Phosphoserine|||Pro residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050828|||http://purl.uniprot.org/annotation/VAR_012804|||http://purl.uniprot.org/annotation/VAR_012805|||http://purl.uniprot.org/annotation/VAR_012806|||http://purl.uniprot.org/annotation/VAR_037060|||http://purl.uniprot.org/annotation/VAR_080414|||http://purl.uniprot.org/annotation/VAR_080415|||http://purl.uniprot.org/annotation/VAR_080416|||http://purl.uniprot.org/annotation/VSP_043014
http://togogenome.org/gene/9606:ARHGEF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AMR3|||http://purl.uniprot.org/uniprot/O43307                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  DH|||Disordered|||In DEE8.|||In DEE8; affects dendritic gephrin clustering and trafficking of GABA-A receptors to synapses.|||In isoform 2.|||In isoform 3.|||Interaction with GPHN|||PH|||Phosphoserine|||Probable disease-associated variant found in a patient with moderate intellectual disability, speech delay and sleep disturbances.|||Rho guanine nucleotide exchange factor 9|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253895|||http://purl.uniprot.org/annotation/VAR_028752|||http://purl.uniprot.org/annotation/VAR_069370|||http://purl.uniprot.org/annotation/VAR_072742|||http://purl.uniprot.org/annotation/VSP_042920|||http://purl.uniprot.org/annotation/VSP_042921|||http://purl.uniprot.org/annotation/VSP_044555
http://togogenome.org/gene/9606:OCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04671                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with green/hazel eye color.|||Associated with nonblue eye color; could be a biomarker of cutaneous cancer risk.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In OCA2 and unclassified OCA.|||In OCA2.|||In OCA2; mild.|||In OCA2; mild/severe.|||In OCA2; mild; AROA form.|||In OCA2; no effect on flow of chloride ions; no effect on subcellular location; no effect on luminal pH.|||In OCA2; reduced flow of chloride ions; no effect on subcellular location; slightly increased luminal pH.|||In OCA2; severe.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In unclassified OCA.|||N-linked (GlcNAc...) asparagine|||P protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000172509|||http://purl.uniprot.org/annotation/VAR_006117|||http://purl.uniprot.org/annotation/VAR_006118|||http://purl.uniprot.org/annotation/VAR_006119|||http://purl.uniprot.org/annotation/VAR_006120|||http://purl.uniprot.org/annotation/VAR_006121|||http://purl.uniprot.org/annotation/VAR_006122|||http://purl.uniprot.org/annotation/VAR_006123|||http://purl.uniprot.org/annotation/VAR_006124|||http://purl.uniprot.org/annotation/VAR_006125|||http://purl.uniprot.org/annotation/VAR_006126|||http://purl.uniprot.org/annotation/VAR_006127|||http://purl.uniprot.org/annotation/VAR_006128|||http://purl.uniprot.org/annotation/VAR_006129|||http://purl.uniprot.org/annotation/VAR_006130|||http://purl.uniprot.org/annotation/VAR_006131|||http://purl.uniprot.org/annotation/VAR_006132|||http://purl.uniprot.org/annotation/VAR_006133|||http://purl.uniprot.org/annotation/VAR_006134|||http://purl.uniprot.org/annotation/VAR_006135|||http://purl.uniprot.org/annotation/VAR_006136|||http://purl.uniprot.org/annotation/VAR_006137|||http://purl.uniprot.org/annotation/VAR_006138|||http://purl.uniprot.org/annotation/VAR_006139|||http://purl.uniprot.org/annotation/VAR_006140|||http://purl.uniprot.org/annotation/VAR_006141|||http://purl.uniprot.org/annotation/VAR_006142|||http://purl.uniprot.org/annotation/VAR_006143|||http://purl.uniprot.org/annotation/VAR_006144|||http://purl.uniprot.org/annotation/VAR_006145|||http://purl.uniprot.org/annotation/VAR_006146|||http://purl.uniprot.org/annotation/VAR_007939|||http://purl.uniprot.org/annotation/VAR_007940|||http://purl.uniprot.org/annotation/VAR_020622|||http://purl.uniprot.org/annotation/VAR_020623|||http://purl.uniprot.org/annotation/VAR_020624|||http://purl.uniprot.org/annotation/VAR_020625|||http://purl.uniprot.org/annotation/VAR_020626|||http://purl.uniprot.org/annotation/VAR_020627|||http://purl.uniprot.org/annotation/VAR_020628|||http://purl.uniprot.org/annotation/VAR_020629|||http://purl.uniprot.org/annotation/VAR_020630|||http://purl.uniprot.org/annotation/VAR_020631|||http://purl.uniprot.org/annotation/VAR_020632|||http://purl.uniprot.org/annotation/VAR_020633|||http://purl.uniprot.org/annotation/VAR_020634|||http://purl.uniprot.org/annotation/VAR_020635|||http://purl.uniprot.org/annotation/VAR_020636|||http://purl.uniprot.org/annotation/VAR_020637|||http://purl.uniprot.org/annotation/VAR_020638|||http://purl.uniprot.org/annotation/VAR_021682|||http://purl.uniprot.org/annotation/VAR_022019|||http://purl.uniprot.org/annotation/VAR_032094|||http://purl.uniprot.org/annotation/VAR_032095|||http://purl.uniprot.org/annotation/VAR_032096|||http://purl.uniprot.org/annotation/VAR_032097|||http://purl.uniprot.org/annotation/VAR_036468|||http://purl.uniprot.org/annotation/VAR_043700|||http://purl.uniprot.org/annotation/VAR_043701|||http://purl.uniprot.org/annotation/VAR_043702|||http://purl.uniprot.org/annotation/VAR_072600|||http://purl.uniprot.org/annotation/VAR_072601|||http://purl.uniprot.org/annotation/VSP_012284|||http://purl.uniprot.org/annotation/VSP_012285|||http://purl.uniprot.org/annotation/VSP_012286
http://togogenome.org/gene/9606:MS4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11836                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abrogates recognition by some antibodies; when associated with D-163 and D-166. Slight decrease of rituximab binding; when associated with D-163 and D-166.|||Abrogates recognition by therapeutic antibodies, including rituximab; when associated with S-172.|||Acidic residues|||B-lymphocyte antigen CD20|||Cytoplasmic|||Decreased binding of some antibodies. No effect on rituximab binding.|||Disordered|||Epitope 1|||Epitope 2|||Epitope 3 (recognized by antibodies, including Rituximab)|||Extracellular|||Helical|||In isoform 2.|||Marked reduction in rituximab binding. Abrogates recognition by antibodies, including rituximab; when associated with S-170.|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158627|||http://purl.uniprot.org/annotation/VSP_057058
http://togogenome.org/gene/9606:PRAMEF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Putative PRAME family member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290161
http://togogenome.org/gene/9606:CGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKQ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Choriogonadotropin subunit beta variant 1|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342548|||http://purl.uniprot.org/annotation/VAR_055838|||http://purl.uniprot.org/annotation/VSP_034490|||http://purl.uniprot.org/annotation/VSP_034491
http://togogenome.org/gene/9606:CRYBB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26998                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-crystallin B3|||Beta-crystallin B3, N-terminally processed|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||C-terminal arm|||Connecting peptide|||In CTRCT22.|||In CTRCT22; unknown pathological significance.|||N-acetylalanine; in Beta-crystallin B3, N-terminally processed|||N-acetylmethionine|||N-terminal arm|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057560|||http://purl.uniprot.org/annotation/PRO_0000421774|||http://purl.uniprot.org/annotation/VAR_025277|||http://purl.uniprot.org/annotation/VAR_025278|||http://purl.uniprot.org/annotation/VAR_025279|||http://purl.uniprot.org/annotation/VAR_025280|||http://purl.uniprot.org/annotation/VAR_070031|||http://purl.uniprot.org/annotation/VAR_084792
http://togogenome.org/gene/9606:APOL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPW4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Apolipoprotein L4|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002041|||http://purl.uniprot.org/annotation/VAR_053008|||http://purl.uniprot.org/annotation/VAR_053009|||http://purl.uniprot.org/annotation/VAR_053010|||http://purl.uniprot.org/annotation/VAR_059966|||http://purl.uniprot.org/annotation/VAR_059967|||http://purl.uniprot.org/annotation/VAR_059968|||http://purl.uniprot.org/annotation/VSP_000295|||http://purl.uniprot.org/annotation/VSP_024380
http://togogenome.org/gene/9606:JAKMIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWB6|||http://purl.uniprot.org/uniprot/Q96N16                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||Janus kinase and microtubule-interacting protein 1|||Janus kinase and microtubule-interacting protein C-terminal|||Mediates association with microtubules|||Mediates interaction with TYK2 and GABBR1|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323008|||http://purl.uniprot.org/annotation/VAR_039471|||http://purl.uniprot.org/annotation/VAR_039472|||http://purl.uniprot.org/annotation/VSP_031989|||http://purl.uniprot.org/annotation/VSP_031990|||http://purl.uniprot.org/annotation/VSP_031991|||http://purl.uniprot.org/annotation/VSP_031992|||http://purl.uniprot.org/annotation/VSP_031993|||http://purl.uniprot.org/annotation/VSP_031994|||http://purl.uniprot.org/annotation/VSP_031995|||http://purl.uniprot.org/annotation/VSP_031996|||http://purl.uniprot.org/annotation/VSP_031997
http://togogenome.org/gene/9606:MYO5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQX4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Dilute|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||In isoform 2.|||Myosin N-terminal SH3-like|||Myosin motor|||N-acetylalanine|||Removed|||Unconventional myosin-Vc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123463|||http://purl.uniprot.org/annotation/VAR_010646|||http://purl.uniprot.org/annotation/VAR_010647|||http://purl.uniprot.org/annotation/VAR_024544|||http://purl.uniprot.org/annotation/VAR_056186|||http://purl.uniprot.org/annotation/VAR_061365|||http://purl.uniprot.org/annotation/VSP_056592|||http://purl.uniprot.org/annotation/VSP_056593
http://togogenome.org/gene/9606:WFIKKN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NZ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Disordered|||Ig-like C2-type|||Kazal-like|||N-linked (GlcNAc...) asparagine|||NTR|||Reactive bond|||WAP|||WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307816
http://togogenome.org/gene/9606:MRPL33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75394                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein bL33m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238625|||http://purl.uniprot.org/annotation/VSP_042822
http://togogenome.org/gene/9606:TIE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTW8|||http://purl.uniprot.org/uniprot/P35590                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In LMPHM11; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor Tie-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024471|||http://purl.uniprot.org/annotation/VAR_041852|||http://purl.uniprot.org/annotation/VAR_041853|||http://purl.uniprot.org/annotation/VAR_041854|||http://purl.uniprot.org/annotation/VAR_085888|||http://purl.uniprot.org/annotation/VAR_085889|||http://purl.uniprot.org/annotation/VSP_047607|||http://purl.uniprot.org/annotation/VSP_047608|||http://purl.uniprot.org/annotation/VSP_047609|||http://purl.uniprot.org/annotation/VSP_047610
http://togogenome.org/gene/9606:ARFGEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FR3|||http://purl.uniprot.org/uniprot/Q86TH5|||http://purl.uniprot.org/uniprot/Q9Y6D5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PRKAR2B and impairs TNFRSF1A release.|||Basic and acidic residues|||Brefeldin A-inhibited guanine nucleotide-exchange protein 2|||DCB; DCB:DCB domain and DCB:HUS domain interaction|||Disordered|||Disturbs membrane organization at the TGN, impairs association of the AP-1 complex and GGA1 with the TGN membranes.|||HUS; DCB:HUS domain interaction|||In PVNH2; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Mon2/Sec7/BIG1-like HDS|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SEC7|||Sec7/BIG1-like C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120208|||http://purl.uniprot.org/annotation/VAR_028750|||http://purl.uniprot.org/annotation/VAR_036156|||http://purl.uniprot.org/annotation/VAR_037438|||http://purl.uniprot.org/annotation/VAR_069404
http://togogenome.org/gene/9606:SEMA4G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Pro residues|||Sema|||Semaphorin-4G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032333|||http://purl.uniprot.org/annotation/VSP_035067|||http://purl.uniprot.org/annotation/VSP_043883
http://togogenome.org/gene/9606:SUZ12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QQW9|||http://purl.uniprot.org/uniprot/Q15022                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Breakpoint for translocation to form JAZF1-SUZ12 oncogene|||C2H2-type|||Disordered|||Fails to form a PRC2.1 dimer.|||Fails to form a PRC2.1 dimer. Reduced H3K27me3 enrichment on PRC2 target genes.|||Fails to interact with JARID2; when associated with A-86.|||Fails to interact with JARID2; when associated with A-90.|||Fails to interact with PHF19. The PRC2.1 dimer forms but is unstable.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In IMMAS.|||In IMMAS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2.|||In IMMAS; unknown pathological significance.|||Interaction with AEBP2 and PHF19|||Interaction with JARID2 and EPOP|||No effect on interaction with PHF19. The PRC2.1 dimer forms but is unstable.|||Phosphoserine|||Polar residues|||Polycomb protein SUZ12|||Polycomb protein VEFS-Box|||VEFS-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047057|||http://purl.uniprot.org/annotation/VAR_028100|||http://purl.uniprot.org/annotation/VAR_078318|||http://purl.uniprot.org/annotation/VAR_083817|||http://purl.uniprot.org/annotation/VAR_083818|||http://purl.uniprot.org/annotation/VAR_083819|||http://purl.uniprot.org/annotation/VAR_083820
http://togogenome.org/gene/9606:RXFP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSD7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Relaxin-3 receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070104
http://togogenome.org/gene/9606:ASB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y574                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 4|||Essential for interaction with HIF1AN|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066928|||http://purl.uniprot.org/annotation/VAR_033512|||http://purl.uniprot.org/annotation/VSP_042668
http://togogenome.org/gene/9606:ELANE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08246                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Found in patients with severe congenital or cyclic neutropenia.|||In CH and SCN1.|||In CH and SCN1; loss of interaction with NOTCH2NL and loss of NOTCH2NL and NOTCH2 proteolytic cleavage.|||In CH.|||In CH; unknown pathological significance.|||In SCN1 and CH.|||In SCN1.|||In SCN1; located on the same allele as L-101; reduces proteolytic enzyme activity by slightly less than half; together with L-101 shows an additive effect with minimal remaining enzyme activity.|||In SCN1; located on the same allele as L-98; reduces proteolytic enzyme activity by slightly less than half; together with L-98 shows an additive effect with minimal remaining enzyme activity.|||In SCN1; the patient also carries mutation Lys-116 in G6PC3.|||In SCN1; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Neutrophil elastase|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027703|||http://purl.uniprot.org/annotation/PRO_0000027704|||http://purl.uniprot.org/annotation/VAR_019237|||http://purl.uniprot.org/annotation/VAR_019238|||http://purl.uniprot.org/annotation/VAR_019239|||http://purl.uniprot.org/annotation/VAR_038609|||http://purl.uniprot.org/annotation/VAR_038610|||http://purl.uniprot.org/annotation/VAR_038611|||http://purl.uniprot.org/annotation/VAR_038612|||http://purl.uniprot.org/annotation/VAR_038613|||http://purl.uniprot.org/annotation/VAR_038614|||http://purl.uniprot.org/annotation/VAR_038615|||http://purl.uniprot.org/annotation/VAR_038616|||http://purl.uniprot.org/annotation/VAR_038617|||http://purl.uniprot.org/annotation/VAR_038618|||http://purl.uniprot.org/annotation/VAR_038619|||http://purl.uniprot.org/annotation/VAR_038620|||http://purl.uniprot.org/annotation/VAR_038621|||http://purl.uniprot.org/annotation/VAR_038622|||http://purl.uniprot.org/annotation/VAR_038623|||http://purl.uniprot.org/annotation/VAR_038624|||http://purl.uniprot.org/annotation/VAR_038625|||http://purl.uniprot.org/annotation/VAR_064512|||http://purl.uniprot.org/annotation/VAR_064513|||http://purl.uniprot.org/annotation/VAR_070696|||http://purl.uniprot.org/annotation/VAR_070697|||http://purl.uniprot.org/annotation/VAR_070698|||http://purl.uniprot.org/annotation/VAR_070699|||http://purl.uniprot.org/annotation/VAR_070700|||http://purl.uniprot.org/annotation/VAR_070701|||http://purl.uniprot.org/annotation/VAR_070702|||http://purl.uniprot.org/annotation/VAR_070703|||http://purl.uniprot.org/annotation/VAR_070704|||http://purl.uniprot.org/annotation/VAR_070705|||http://purl.uniprot.org/annotation/VAR_070706|||http://purl.uniprot.org/annotation/VAR_070707|||http://purl.uniprot.org/annotation/VAR_070708|||http://purl.uniprot.org/annotation/VAR_070709|||http://purl.uniprot.org/annotation/VAR_070710|||http://purl.uniprot.org/annotation/VAR_070711|||http://purl.uniprot.org/annotation/VAR_070712|||http://purl.uniprot.org/annotation/VAR_070713|||http://purl.uniprot.org/annotation/VAR_070714|||http://purl.uniprot.org/annotation/VAR_070715|||http://purl.uniprot.org/annotation/VAR_070716|||http://purl.uniprot.org/annotation/VAR_070717|||http://purl.uniprot.org/annotation/VAR_070718|||http://purl.uniprot.org/annotation/VAR_070719|||http://purl.uniprot.org/annotation/VAR_070720|||http://purl.uniprot.org/annotation/VAR_070721|||http://purl.uniprot.org/annotation/VAR_070722|||http://purl.uniprot.org/annotation/VAR_070723|||http://purl.uniprot.org/annotation/VAR_070724|||http://purl.uniprot.org/annotation/VAR_070725|||http://purl.uniprot.org/annotation/VAR_070726|||http://purl.uniprot.org/annotation/VAR_070727|||http://purl.uniprot.org/annotation/VAR_070728|||http://purl.uniprot.org/annotation/VAR_070729|||http://purl.uniprot.org/annotation/VAR_070730|||http://purl.uniprot.org/annotation/VAR_070731|||http://purl.uniprot.org/annotation/VAR_070732|||http://purl.uniprot.org/annotation/VAR_070733|||http://purl.uniprot.org/annotation/VAR_070734|||http://purl.uniprot.org/annotation/VAR_070735|||http://purl.uniprot.org/annotation/VAR_070736|||http://purl.uniprot.org/annotation/VAR_070737|||http://purl.uniprot.org/annotation/VAR_070738|||http://purl.uniprot.org/annotation/VAR_070739|||http://purl.uniprot.org/annotation/VAR_070740|||http://purl.uniprot.org/annotation/VAR_070741|||http://purl.uniprot.org/annotation/VAR_070742|||http://purl.uniprot.org/annotation/VAR_070743|||http://purl.uniprot.org/annotation/VAR_070744|||http://purl.uniprot.org/annotation/VAR_070745|||http://purl.uniprot.org/annotation/VAR_070746|||http://purl.uniprot.org/annotation/VAR_070747|||http://purl.uniprot.org/annotation/VAR_070748|||http://purl.uniprot.org/annotation/VAR_070749|||http://purl.uniprot.org/annotation/VAR_070750|||http://purl.uniprot.org/annotation/VAR_070751|||http://purl.uniprot.org/annotation/VAR_070752|||http://purl.uniprot.org/annotation/VAR_070753|||http://purl.uniprot.org/annotation/VAR_070754|||http://purl.uniprot.org/annotation/VAR_070755|||http://purl.uniprot.org/annotation/VAR_070756|||http://purl.uniprot.org/annotation/VAR_070757|||http://purl.uniprot.org/annotation/VAR_070758|||http://purl.uniprot.org/annotation/VAR_070759|||http://purl.uniprot.org/annotation/VAR_070760|||http://purl.uniprot.org/annotation/VAR_070761|||http://purl.uniprot.org/annotation/VAR_070762|||http://purl.uniprot.org/annotation/VAR_070763|||http://purl.uniprot.org/annotation/VAR_070764|||http://purl.uniprot.org/annotation/VAR_070765|||http://purl.uniprot.org/annotation/VAR_070766
http://togogenome.org/gene/9606:LHFPL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAF8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In DFNB67.|||LHFPL tetraspan subfamily member 5 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285922|||http://purl.uniprot.org/annotation/VAR_032055|||http://purl.uniprot.org/annotation/VAR_032056|||http://purl.uniprot.org/annotation/VAR_032057|||http://purl.uniprot.org/annotation/VAR_079038
http://togogenome.org/gene/9606:GAP43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17677|||http://purl.uniprot.org/uniprot/Q5U058                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ|||In isoform 2.|||Inhibits axonal and dendritic filopodia formation and reduces dendritic and axonal branching.|||Neuromodulin|||Neuromodulin (GAP-43) C-terminal|||Neuromodulin gap junction N-terminal|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by PHK and PKC|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159596|||http://purl.uniprot.org/annotation/VAR_014172|||http://purl.uniprot.org/annotation/VAR_050271|||http://purl.uniprot.org/annotation/VSP_042783
http://togogenome.org/gene/9606:PRAMEF27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3QJZ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000435289
http://togogenome.org/gene/9606:AIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14862                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to homooligomerize.|||Fails to activate interleukin-1 beta production.|||HIN-200|||Impaired ability to form AIM2 inflammasome filaments in response to double-stranded DNA (dsDNA).|||Impaired ability to homooligomerize.|||Impaired ability to nucleate with PYCARD/ASC.|||Impaired double-stranded DNA (dsDNA)-binding, preventing homooligomerization.|||Impaired homooligomerization.|||Impairs DNA binding.|||Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337.|||Impairs DNA binding; when associated with A-160; A-K162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337.|||In Mut1; abolished interaction with PYCARD/ASC.|||In Mut2; abolished interaction with PYCARD/ASC. Abolished ability to bind double-stranded DNA (dsDNA).|||Interferon-inducible protein AIM2|||Pyrin|||Strongly impaired ability to homooligomerize.|||Strongly reduced ability to homooligomerize upon double-stranded DNA (dsDNA)-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153726|||http://purl.uniprot.org/annotation/VAR_022022|||http://purl.uniprot.org/annotation/VAR_043379
http://togogenome.org/gene/9606:LAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00515                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  8 X SEK repeats|||Basic and acidic residues|||Disordered|||Ladinin-1|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SEK 1|||SEK 2|||SEK 3|||SEK 4|||SEK 5|||SEK 6|||SEK 7|||SEK 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084349|||http://purl.uniprot.org/annotation/VAR_046539|||http://purl.uniprot.org/annotation/VAR_046540|||http://purl.uniprot.org/annotation/VAR_046541|||http://purl.uniprot.org/annotation/VAR_046542|||http://purl.uniprot.org/annotation/VAR_046543|||http://purl.uniprot.org/annotation/VAR_046544
http://togogenome.org/gene/9606:SNCAIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z616|||http://purl.uniprot.org/uniprot/B7Z995|||http://purl.uniprot.org/uniprot/Q9Y6H5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Decreases interaction with SIAH1 and formation of cytoplasmic inclusion bodies; when associated with N-79.|||Decreases interaction with SIAH1 and formation of cytoplasmic inclusion bodies; when associated with N-81.|||Disordered|||Found in patients with symptoms of Parkinson disease; unknown pathological significance; reduced number of cytoplasmic inclusions in cells expressing C-621 compared with cells expressing wild-type (wt) protein when subjected to proteasomal inhibition; C-621 transfected cells are more susceptible to staurosporine-induced cell death than cells expressing wt protein.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 6.|||Polar residues|||Synphilin-1|||Synphilin-1 alpha-Synuclein-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067068|||http://purl.uniprot.org/annotation/VAR_025667|||http://purl.uniprot.org/annotation/VAR_048312|||http://purl.uniprot.org/annotation/VAR_065358|||http://purl.uniprot.org/annotation/VAR_065359|||http://purl.uniprot.org/annotation/VSP_038839|||http://purl.uniprot.org/annotation/VSP_038840|||http://purl.uniprot.org/annotation/VSP_038841|||http://purl.uniprot.org/annotation/VSP_038842|||http://purl.uniprot.org/annotation/VSP_038843|||http://purl.uniprot.org/annotation/VSP_038844|||http://purl.uniprot.org/annotation/VSP_038845
http://togogenome.org/gene/9606:PPP2R2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00005                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Probable disease-associated variant found in a patient with moderate intellectual disability, authism and intractable epilepsy.|||Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071421|||http://purl.uniprot.org/annotation/VAR_051738|||http://purl.uniprot.org/annotation/VAR_078654|||http://purl.uniprot.org/annotation/VSP_037976|||http://purl.uniprot.org/annotation/VSP_037977|||http://purl.uniprot.org/annotation/VSP_037978|||http://purl.uniprot.org/annotation/VSP_037979|||http://purl.uniprot.org/annotation/VSP_044923|||http://purl.uniprot.org/annotation/VSP_045748
http://togogenome.org/gene/9606:FAM217B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2D0|||http://purl.uniprot.org/uniprot/Q9NTX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||Polar residues|||Protein FAM217B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079485|||http://purl.uniprot.org/annotation/VAR_035691|||http://purl.uniprot.org/annotation/VAR_050922
http://togogenome.org/gene/9606:CD82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27701                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD82 antigen|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219226|||http://purl.uniprot.org/annotation/VAR_052326|||http://purl.uniprot.org/annotation/VSP_045656
http://togogenome.org/gene/9606:INTS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HW7                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||In isoform 2.|||In isoform 3.|||Integrator complex subunit 4|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259538|||http://purl.uniprot.org/annotation/VSP_021448|||http://purl.uniprot.org/annotation/VSP_021449|||http://purl.uniprot.org/annotation/VSP_021450|||http://purl.uniprot.org/annotation/VSP_021452|||http://purl.uniprot.org/annotation/VSP_021453
http://togogenome.org/gene/9606:DEFB4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15263                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Mutagenesis Site|||Peptide|||Region|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Defensin beta 4A|||Loss of PIP2 binding and loss of liposomal lysis activity. Decrease in fungal cell permeabilization. Impaired antifungal activity.|||Loss of PIP2 binding and reduced liposomal lysis activity. Impaired antifungal activity. Decrease in fungal cell permeabilization.|||No impact on PIP binding and liposomal lysis activity. Lack of antifungal activity. Lack of fungal cell permeabilization.|||No impact on fungal cell permeabilization. Impaired antifungal activity.|||No impact on fungal cell permeabilization. No impact on antifungal activity.|||Phosphatidylinositol 4,5-bisphosphate (PIP2) binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006968
http://togogenome.org/gene/9606:YTHDF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5A9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased binding to RNAs.|||Disordered|||In isoform 2.|||Interaction with m6A-containing mRNAs|||Localization to mRNA processing bodies (P-bodies)|||N-acetylserine|||Phosphoserine|||Polar residues|||Reduced binding to N6-methyladenosine (m6A)-containing RNAs.|||Reduced binding to N6-methyladenosine (m6A)-containing RNAs. Reduced ability to undergo liquid-liquid phase separation. Reduced binding to C5-methylcytosine (m5C)-containing RNAs.|||Reduced binding to N6-methyladenosine (m6A)-containing RNAs. Reduced ability to undergo liquid-liquid phase separation; when associated with A-432.|||Removed|||Slightly decreased binding to RNAs.|||YTH|||YTH domain-containing family protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223075|||http://purl.uniprot.org/annotation/VAR_053744|||http://purl.uniprot.org/annotation/VAR_053745|||http://purl.uniprot.org/annotation/VSP_009297
http://togogenome.org/gene/9606:DPYSL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPU6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dihydropyrimidinase-related protein 5|||In RTSC4; reduced inhibition of dendrite development in transfected primary neurons; decreased interaction with MAP2; decreased interaction with TUBB3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165924|||http://purl.uniprot.org/annotation/VAR_086051|||http://purl.uniprot.org/annotation/VAR_086052
http://togogenome.org/gene/9606:FAM241A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8J7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Uncharacterized protein FAM241A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286629|||http://purl.uniprot.org/annotation/VAR_032150
http://togogenome.org/gene/9606:AGO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6I8PTZ8|||http://purl.uniprot.org/uniprot/B2RAD8|||http://purl.uniprot.org/uniprot/B3KME0|||http://purl.uniprot.org/uniprot/Q5TA58|||http://purl.uniprot.org/uniprot/Q9UL18                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Confers modest RNA cleavage activity; when associated with H-805.|||Confers modest RNA cleavage activity; when associated with Q-675 and H-805.|||Disordered|||Does not confer enzyme activity by itself. Confers low RNA cleavage activity; when associated with H-805. Confers modest RNA cleavage activity; when associated with S-670 and H-805.|||Does not confer enzyme activity by itself. Confers modest RNA cleavage activity; when associated with F-674.|||Impairs access of bound RNA to the active site|||In NEDLBAS.|||In NEDLBAS; unknown pathological significance.|||Interaction with guide RNA|||PAZ|||Piwi|||Protein argonaute-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194055|||http://purl.uniprot.org/annotation/VAR_078651|||http://purl.uniprot.org/annotation/VAR_088406|||http://purl.uniprot.org/annotation/VAR_088407|||http://purl.uniprot.org/annotation/VAR_088408|||http://purl.uniprot.org/annotation/VAR_088409|||http://purl.uniprot.org/annotation/VAR_088410|||http://purl.uniprot.org/annotation/VAR_088411|||http://purl.uniprot.org/annotation/VAR_088412|||http://purl.uniprot.org/annotation/VAR_088413|||http://purl.uniprot.org/annotation/VAR_088414|||http://purl.uniprot.org/annotation/VAR_088415|||http://purl.uniprot.org/annotation/VAR_088416|||http://purl.uniprot.org/annotation/VAR_088417|||http://purl.uniprot.org/annotation/VAR_088418|||http://purl.uniprot.org/annotation/VAR_088419|||http://purl.uniprot.org/annotation/VAR_088420|||http://purl.uniprot.org/annotation/VAR_088421
http://togogenome.org/gene/9606:OLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78380                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization.|||Abolishes binding to acetylated LDL (AcLDL).|||Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229.|||Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231.|||Abolishes homodimerization.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-256.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-264.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-256 and S-264.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-243; S-256 and S-264.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-172; S-243; S-256 and S-264.|||Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-155; S-172; S-243; S-256 and S-264.|||Abolishes sorting into the cell surface; when associated with 22-E--E-25.|||C-type lectin|||Cytoplasmic|||Disordered|||Does not affect binding to acetylated LDL (AcLDL).|||Does not affect glycosylation state.|||Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL).|||Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Abolishes binding to acetylated LDL (AcLDL); when associated with Q-226 and N-231.|||Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL).|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199.|||Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236.|||Impairs binding to acetylated LDL (AcLDL); when associated with A-240.|||Impairs binding to acetylated LDL (AcLDL); when associated with L-193.|||Impairs protein folding and transport.|||Impairs sorting into the cell surface but retains ability to bind oxLDL. Abolishes sorting into the cell surface; when associated with K-69.|||In isoform 2.|||In isoform 3.|||Interchain|||Myocardial infarction susceptibility.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Neck|||No effect.|||Not glycosylated|||Oxidized low-density lipoprotein receptor 1|||Oxidized low-density lipoprotein receptor 1, soluble form|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017443|||http://purl.uniprot.org/annotation/PRO_0000017444|||http://purl.uniprot.org/annotation/VAR_023200|||http://purl.uniprot.org/annotation/VSP_042555|||http://purl.uniprot.org/annotation/VSP_045277
http://togogenome.org/gene/9606:KLF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y9|||http://purl.uniprot.org/uniprot/X5DNR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 13|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047184
http://togogenome.org/gene/9606:MINAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Major intrinsically disordered Notch2-binding receptor 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157133|||http://purl.uniprot.org/annotation/VAR_022042|||http://purl.uniprot.org/annotation/VAR_034044
http://togogenome.org/gene/9606:CPNE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75131                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-3|||Phosphoserine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144838|||http://purl.uniprot.org/annotation/VAR_024424|||http://purl.uniprot.org/annotation/VAR_048848
http://togogenome.org/gene/9606:TTLL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased binding to microtubules and polyglutamylase activity; when associated with E-416 and E-419.|||Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 2.|||Polar residues|||Pro residues|||TTL|||Tubulin polyglutamylase TTLL11|||c-MTBD region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212445|||http://purl.uniprot.org/annotation/VSP_057853|||http://purl.uniprot.org/annotation/VSP_057854
http://togogenome.org/gene/9606:ANXA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13928                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A8|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067503|||http://purl.uniprot.org/annotation/VAR_000604|||http://purl.uniprot.org/annotation/VAR_030630|||http://purl.uniprot.org/annotation/VSP_056397|||http://purl.uniprot.org/annotation/VSP_056398|||http://purl.uniprot.org/annotation/VSP_057805
http://togogenome.org/gene/9606:ZNF236                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J9JID5|||http://purl.uniprot.org/uniprot/Q9UL36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform A.|||Polar residues|||Zinc finger protein 236                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047476|||http://purl.uniprot.org/annotation/VAR_057410|||http://purl.uniprot.org/annotation/VAR_057411|||http://purl.uniprot.org/annotation/VAR_057412|||http://purl.uniprot.org/annotation/VAR_057413|||http://purl.uniprot.org/annotation/VAR_065094|||http://purl.uniprot.org/annotation/VSP_006907|||http://purl.uniprot.org/annotation/VSP_006908
http://togogenome.org/gene/9606:KAZN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q674X7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PPL|||Kazrin|||Phosphoserine|||Polar residues|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322453|||http://purl.uniprot.org/annotation/VAR_060168|||http://purl.uniprot.org/annotation/VAR_060169|||http://purl.uniprot.org/annotation/VSP_031898|||http://purl.uniprot.org/annotation/VSP_031899|||http://purl.uniprot.org/annotation/VSP_031900|||http://purl.uniprot.org/annotation/VSP_031901|||http://purl.uniprot.org/annotation/VSP_031902|||http://purl.uniprot.org/annotation/VSP_031903
http://togogenome.org/gene/9606:IGFLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EL86|||http://purl.uniprot.org/uniprot/Q9H665                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||IGF-like family receptor 1|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290357|||http://purl.uniprot.org/annotation/PRO_5003900797|||http://purl.uniprot.org/annotation/VAR_032775|||http://purl.uniprot.org/annotation/VSP_026145
http://togogenome.org/gene/9606:LMBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVP7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Limb region 1 protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053906|||http://purl.uniprot.org/annotation/VAR_031900|||http://purl.uniprot.org/annotation/VSP_016888|||http://purl.uniprot.org/annotation/VSP_017441
http://togogenome.org/gene/9606:RDH12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z613|||http://purl.uniprot.org/uniprot/Q96NR8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Non-terminal Residue|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Does not affect the protection against the toxicity of 4-hydroxynonenal in the retina.|||Found in a patient with LCA13.|||In LCA13.|||In LCA13; abolishes protection against the toxicity of 4-hydroxynonenal in the retina; results in aberrant activity in interconverting isomers of retinol and retinal; the activity profiles depend on presence or absence of variant Q-161; genetic background may act as a modifier of variant effect.|||In LCA13; diminished activity in interconverting isomers of retinol and retinal.|||In LCA13; exhibits a profound loss of catalytic activity.|||In RP53.|||In RP53; early onset; unknown pathological significance.|||In retinal dystrophy; exhibits a profound loss of catalytic activity.|||In retinal dystrophy; unknown pathological significance.|||In retinal dystrophy; unknown pathological significance; exhibits a loss of catalytic activity.|||Proton acceptor|||Retinol dehydrogenase 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054766|||http://purl.uniprot.org/annotation/PRO_5006608295|||http://purl.uniprot.org/annotation/VAR_020858|||http://purl.uniprot.org/annotation/VAR_020859|||http://purl.uniprot.org/annotation/VAR_020860|||http://purl.uniprot.org/annotation/VAR_020861|||http://purl.uniprot.org/annotation/VAR_020862|||http://purl.uniprot.org/annotation/VAR_020863|||http://purl.uniprot.org/annotation/VAR_020864|||http://purl.uniprot.org/annotation/VAR_020865|||http://purl.uniprot.org/annotation/VAR_028281|||http://purl.uniprot.org/annotation/VAR_064163|||http://purl.uniprot.org/annotation/VAR_064164|||http://purl.uniprot.org/annotation/VAR_064165|||http://purl.uniprot.org/annotation/VAR_064166|||http://purl.uniprot.org/annotation/VAR_064167|||http://purl.uniprot.org/annotation/VAR_064168|||http://purl.uniprot.org/annotation/VAR_064169|||http://purl.uniprot.org/annotation/VAR_064170|||http://purl.uniprot.org/annotation/VAR_064171|||http://purl.uniprot.org/annotation/VAR_064172|||http://purl.uniprot.org/annotation/VAR_064173|||http://purl.uniprot.org/annotation/VAR_064174|||http://purl.uniprot.org/annotation/VAR_064175|||http://purl.uniprot.org/annotation/VAR_064176|||http://purl.uniprot.org/annotation/VAR_064177|||http://purl.uniprot.org/annotation/VAR_064178|||http://purl.uniprot.org/annotation/VAR_064179|||http://purl.uniprot.org/annotation/VAR_067193|||http://purl.uniprot.org/annotation/VAR_081222
http://togogenome.org/gene/9606:ALG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y672                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase|||Helical|||In CDG1C.|||May act as disease modifier and exacerbate clinical severity in patients with a congenital disorder of glycosylation; slightly decreased function as shown by rescue experiments of defective glycosylation in an alg6-deficient S.cerevisiae strain.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174156|||http://purl.uniprot.org/annotation/VAR_013441|||http://purl.uniprot.org/annotation/VAR_013442|||http://purl.uniprot.org/annotation/VAR_013443|||http://purl.uniprot.org/annotation/VAR_013444|||http://purl.uniprot.org/annotation/VAR_022511|||http://purl.uniprot.org/annotation/VAR_022512|||http://purl.uniprot.org/annotation/VAR_022513|||http://purl.uniprot.org/annotation/VAR_022514|||http://purl.uniprot.org/annotation/VAR_022515|||http://purl.uniprot.org/annotation/VAR_055493
http://togogenome.org/gene/9606:TIMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35625                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  In SFD.|||Involved in metalloproteinase-binding|||Mediates interaction with EFEMP1|||Metalloproteinase inhibitor 3|||NTR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034341|||http://purl.uniprot.org/annotation/VAR_007508|||http://purl.uniprot.org/annotation/VAR_007509|||http://purl.uniprot.org/annotation/VAR_007510|||http://purl.uniprot.org/annotation/VAR_008290|||http://purl.uniprot.org/annotation/VAR_010901
http://togogenome.org/gene/9606:B3GNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2A9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219172|||http://purl.uniprot.org/annotation/VAR_022644|||http://purl.uniprot.org/annotation/VAR_074178
http://togogenome.org/gene/9606:RPS6KA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15418                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphoserine; by PDPK1|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086198|||http://purl.uniprot.org/annotation/VAR_021864|||http://purl.uniprot.org/annotation/VSP_041380|||http://purl.uniprot.org/annotation/VSP_041580|||http://purl.uniprot.org/annotation/VSP_057469
http://togogenome.org/gene/9606:C1orf216                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||UPF0500 protein C1orf216                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309178
http://togogenome.org/gene/9606:RNH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13489                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  2 X 5 AA tandem repeats of S-L-D-I-Q|||25-fold reduction in binding affinity for RNASE2.|||40-fold reduction in binding affinity for RNASE2.|||A significant decrease in binding affinity with RNASE1, slight decrease for the ANG ligand, no real change in binding affinity for RNASE2.|||Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-264 and A-319.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Ribonuclease inhibitor|||Substantially decreased binding affinity for RNASE2. Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-262 and A-264.|||Substantially decreased binding affinity for RNASE2. Binding affinity decreased 5000-fold over the wild type for RNASE2; when associated with A-262 and A-319.|||Substantially decreases binding affinity for RNASE1, ANG and RNASE2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097343|||http://purl.uniprot.org/annotation/VAR_014726
http://togogenome.org/gene/9606:SPPL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCT7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 4.|||Loss of intramembrane-cleaving activity toward ITM2B, TNF and the simian foamy virus envelope glycoprotein gp130.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||PAL|||Polar residues|||Pro residues|||Signal peptide peptidase-like 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073909|||http://purl.uniprot.org/annotation/VAR_059780|||http://purl.uniprot.org/annotation/VSP_005204|||http://purl.uniprot.org/annotation/VSP_009221|||http://purl.uniprot.org/annotation/VSP_009222
http://togogenome.org/gene/9606:CXCL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42830|||http://purl.uniprot.org/uniprot/Q6I9S7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  C-X-C motif chemokine|||C-X-C motif chemokine 5|||Chemokine interleukin-8-like|||Cleavage; by cathepsin G|||ENA-78(8-78)|||ENA-78(9-78)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005075|||http://purl.uniprot.org/annotation/PRO_0000005076|||http://purl.uniprot.org/annotation/PRO_0000005077|||http://purl.uniprot.org/annotation/PRO_5014205942
http://togogenome.org/gene/9606:FHIP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0V3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FHF complex subunit HOOK interacting protein 2A|||Found in a patient with microcephaly severe intellectual disability, ataxia, behavioral abnormalities and speech problems; unknown pathological significance.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284648|||http://purl.uniprot.org/annotation/VAR_031793|||http://purl.uniprot.org/annotation/VAR_031794|||http://purl.uniprot.org/annotation/VAR_084432|||http://purl.uniprot.org/annotation/VSP_024590|||http://purl.uniprot.org/annotation/VSP_024591
http://togogenome.org/gene/9606:PRB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EXA8|||http://purl.uniprot.org/uniprot/E9PAL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5014088914|||http://purl.uniprot.org/annotation/PRO_5014089021
http://togogenome.org/gene/9606:MTO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Z2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In COXPD10.|||In isoform 1 and isoform 5.|||In isoform 1.|||In isoform 2.|||In isoform 6.|||In isoform 7.|||Mitochondrion|||N6-methyllysine|||Protein MTO1 homolog, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042688|||http://purl.uniprot.org/annotation/VAR_068693|||http://purl.uniprot.org/annotation/VSP_001748|||http://purl.uniprot.org/annotation/VSP_001749|||http://purl.uniprot.org/annotation/VSP_001750|||http://purl.uniprot.org/annotation/VSP_001751|||http://purl.uniprot.org/annotation/VSP_040985|||http://purl.uniprot.org/annotation/VSP_040986
http://togogenome.org/gene/9606:H2BC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23527                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-O|||N-acetylproline; partial|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071834
http://togogenome.org/gene/9606:FLAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFF5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAD synthase|||In LSMFLAD; decreased protein stability; decreased affinity for FMN; reduced Vmax; decreased FMN adenylyltransferase activity.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Mitochondrion|||Molybdenum cofactor biosynthesis protein-like|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302737|||http://purl.uniprot.org/annotation/VAR_077069|||http://purl.uniprot.org/annotation/VAR_077070|||http://purl.uniprot.org/annotation/VSP_027947|||http://purl.uniprot.org/annotation/VSP_027948|||http://purl.uniprot.org/annotation/VSP_027949|||http://purl.uniprot.org/annotation/VSP_027950|||http://purl.uniprot.org/annotation/VSP_027951|||http://purl.uniprot.org/annotation/VSP_027952|||http://purl.uniprot.org/annotation/VSP_027953|||http://purl.uniprot.org/annotation/VSP_027954
http://togogenome.org/gene/9606:REDIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Uncharacterized protein C12orf40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348051|||http://purl.uniprot.org/annotation/VAR_061610|||http://purl.uniprot.org/annotation/VSP_035082|||http://purl.uniprot.org/annotation/VSP_035083|||http://purl.uniprot.org/annotation/VSP_035084|||http://purl.uniprot.org/annotation/VSP_035085|||http://purl.uniprot.org/annotation/VSP_035086
http://togogenome.org/gene/9606:NUCB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7Q1|||http://purl.uniprot.org/uniprot/Q02818                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Binds to GNAI2 and GNAI3|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||GBA|||Nucleobindin-1|||O-glycosylated at one site|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004162|||http://purl.uniprot.org/annotation/PRO_5002722191|||http://purl.uniprot.org/annotation/VAR_012151|||http://purl.uniprot.org/annotation/VAR_012152|||http://purl.uniprot.org/annotation/VAR_061087
http://togogenome.org/gene/9606:VPS50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JG6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NEDMSC; unknown pathological significance; decreased protein levels in homozygous patient cells; reduced TFRC recycling to the cell surface in homozygous patient cells.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Syndetin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307265|||http://purl.uniprot.org/annotation/VAR_086711|||http://purl.uniprot.org/annotation/VSP_028658|||http://purl.uniprot.org/annotation/VSP_028659|||http://purl.uniprot.org/annotation/VSP_045572
http://togogenome.org/gene/9606:EFR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14156                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Induces localization to the cytosol.|||Phosphoserine|||Protein EFR3 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050724|||http://purl.uniprot.org/annotation/VAR_047247|||http://purl.uniprot.org/annotation/VAR_047248|||http://purl.uniprot.org/annotation/VAR_075101|||http://purl.uniprot.org/annotation/VAR_075102|||http://purl.uniprot.org/annotation/VAR_075103|||http://purl.uniprot.org/annotation/VAR_075104|||http://purl.uniprot.org/annotation/VAR_075105|||http://purl.uniprot.org/annotation/VAR_075106|||http://purl.uniprot.org/annotation/VAR_075107|||http://purl.uniprot.org/annotation/VAR_075108|||http://purl.uniprot.org/annotation/VAR_075109|||http://purl.uniprot.org/annotation/VAR_075110|||http://purl.uniprot.org/annotation/VAR_075111|||http://purl.uniprot.org/annotation/VAR_075112|||http://purl.uniprot.org/annotation/VAR_075113|||http://purl.uniprot.org/annotation/VAR_075114|||http://purl.uniprot.org/annotation/VAR_075115|||http://purl.uniprot.org/annotation/VAR_075116|||http://purl.uniprot.org/annotation/VAR_075117|||http://purl.uniprot.org/annotation/VAR_075118|||http://purl.uniprot.org/annotation/VAR_075119|||http://purl.uniprot.org/annotation/VAR_075120|||http://purl.uniprot.org/annotation/VAR_075121|||http://purl.uniprot.org/annotation/VAR_075122|||http://purl.uniprot.org/annotation/VAR_075123|||http://purl.uniprot.org/annotation/VAR_075124|||http://purl.uniprot.org/annotation/VAR_075125|||http://purl.uniprot.org/annotation/VSP_022217|||http://purl.uniprot.org/annotation/VSP_022218
http://togogenome.org/gene/9606:ZNF415                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTG1|||http://purl.uniprot.org/uniprot/Q09FC8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Zinc finger protein 415                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286808|||http://purl.uniprot.org/annotation/VAR_032166|||http://purl.uniprot.org/annotation/VAR_032167|||http://purl.uniprot.org/annotation/VAR_032168|||http://purl.uniprot.org/annotation/VAR_032169|||http://purl.uniprot.org/annotation/VAR_032170|||http://purl.uniprot.org/annotation/VSP_025175|||http://purl.uniprot.org/annotation/VSP_025176|||http://purl.uniprot.org/annotation/VSP_025177|||http://purl.uniprot.org/annotation/VSP_025178|||http://purl.uniprot.org/annotation/VSP_044807
http://togogenome.org/gene/9606:C9orf72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LT7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Guanine nucleotide exchange factor C9orf72|||In isoform 2.|||Required for the homodimerization of the C9orf72-SMCR8 complex|||cDENN C9ORF72-type|||dDENN C9ORF72-type|||uDENN C9ORF72-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089711|||http://purl.uniprot.org/annotation/VAR_050827|||http://purl.uniprot.org/annotation/VSP_014745|||http://purl.uniprot.org/annotation/VSP_014746
http://togogenome.org/gene/9606:SULT1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50225                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In allele SULT1A1*2; has a lower sulfotransferase activity.|||In isoform 2.|||Increased activity towards p-nitrophenol.|||Increased sensitivity of enzyme activity to heat inactivation.|||Phosphoserine|||Proton acceptor|||Sulfotransferase 1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085127|||http://purl.uniprot.org/annotation/VAR_007425|||http://purl.uniprot.org/annotation/VAR_009302|||http://purl.uniprot.org/annotation/VAR_009303|||http://purl.uniprot.org/annotation/VAR_014889|||http://purl.uniprot.org/annotation/VAR_028721|||http://purl.uniprot.org/annotation/VAR_057339|||http://purl.uniprot.org/annotation/VAR_061886|||http://purl.uniprot.org/annotation/VSP_040101
http://togogenome.org/gene/9606:CXCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09341                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  GRO-alpha(4-73)|||GRO-alpha(5-73)|||GRO-alpha(6-73)|||Growth-regulated alpha protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005049|||http://purl.uniprot.org/annotation/PRO_0000005050|||http://purl.uniprot.org/annotation/PRO_0000005051|||http://purl.uniprot.org/annotation/PRO_0000005052
http://togogenome.org/gene/9606:NUP42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15504                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||FG 1|||FG 10|||FG 11|||FG 12|||FG 2|||FG 3|||FG 4|||FG 5|||FG 6|||FG 7|||FG 8|||FG 9|||In isoform 2.|||In isoform 3.|||Interaction with GLE1|||Interaction with HIV-1 Vpr|||Nucleoporin NUP42|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204895|||http://purl.uniprot.org/annotation/VAR_050572|||http://purl.uniprot.org/annotation/VAR_050573|||http://purl.uniprot.org/annotation/VSP_016480|||http://purl.uniprot.org/annotation/VSP_016481|||http://purl.uniprot.org/annotation/VSP_016482
http://togogenome.org/gene/9606:MRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IN84                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrion|||rRNA methyltransferase 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273202|||http://purl.uniprot.org/annotation/VAR_061906|||http://purl.uniprot.org/annotation/VSP_022494
http://togogenome.org/gene/9606:ZNF639                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UID6                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CTNNA2|||Phosphoserine|||Zinc finger protein 639                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047696
http://togogenome.org/gene/9606:GBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PP9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190968|||http://purl.uniprot.org/annotation/VAR_028283|||http://purl.uniprot.org/annotation/VAR_028284|||http://purl.uniprot.org/annotation/VAR_028285|||http://purl.uniprot.org/annotation/VAR_028286|||http://purl.uniprot.org/annotation/VAR_028287|||http://purl.uniprot.org/annotation/VAR_028288|||http://purl.uniprot.org/annotation/VAR_033952|||http://purl.uniprot.org/annotation/VAR_033953|||http://purl.uniprot.org/annotation/VAR_033954|||http://purl.uniprot.org/annotation/VAR_033955
http://togogenome.org/gene/9606:MCFD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF17|||http://purl.uniprot.org/uniprot/Q8NI22                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||In F5F8D2.|||In F5F8D2; interferes with protein folding.|||In isoform 2.|||In isoform 3.|||Multiple coagulation factor deficiency protein 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004159|||http://purl.uniprot.org/annotation/VAR_019076|||http://purl.uniprot.org/annotation/VAR_019077|||http://purl.uniprot.org/annotation/VAR_072245|||http://purl.uniprot.org/annotation/VAR_072246|||http://purl.uniprot.org/annotation/VSP_043814|||http://purl.uniprot.org/annotation/VSP_043815
http://togogenome.org/gene/9606:APAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14727                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation of pro-caspase-9 independent of cytochrome c. Increased ability to induce apoptosis.|||Apoptotic protease-activating factor 1|||CARD|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||Interpropeller linker|||NB-ARC|||No association with APAF-1. No binding to pro-caspase-9.|||WD 1-1|||WD 1-2|||WD 1-3|||WD 1-4|||WD 1-5|||WD 1-6|||WD 1-7|||WD 2-1|||WD 2-2|||WD 2-3|||WD 2-4|||WD 2-5|||WD 2-6|||WD 2-7|||WD 2-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050844|||http://purl.uniprot.org/annotation/VSP_006759|||http://purl.uniprot.org/annotation/VSP_006760|||http://purl.uniprot.org/annotation/VSP_006761|||http://purl.uniprot.org/annotation/VSP_006762|||http://purl.uniprot.org/annotation/VSP_008965|||http://purl.uniprot.org/annotation/VSP_008966
http://togogenome.org/gene/9606:HLX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14774                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||H2.0-like homeobox protein|||Homeobox|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048978|||http://purl.uniprot.org/annotation/VAR_037162|||http://purl.uniprot.org/annotation/VAR_037163|||http://purl.uniprot.org/annotation/VAR_049582
http://togogenome.org/gene/9606:PCOLCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15113                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cleavage|||Disordered|||N-linked (GlcNAc...) asparagine|||NTR|||Phosphoserine|||Procollagen C-endopeptidase enhancer 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022023
http://togogenome.org/gene/9606:LTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29376                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished homodimerization following interaction with ALKAL1.|||Abolishes interaction with PI3-kinase subunit p85, impairs PI3 kinase activity and leads to apoptosis (demonstrated with chimeric EGFR-LTK).|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs phosphorylation of CBLC (demonstrated with chimeric EGFR-LTK).|||In isoform 2 and isoform 5.|||In isoform 5.|||In isoform Lambda P1.|||In isoform Lambda P3.|||Increases autophosphorylation and interaction with PI3-kinase subunit p85 (demonstrated with chimeric EGFR-LTK).|||Leukocyte tyrosine kinase receptor|||Loss of interaction with PLCG1, PI3-kinase subunit p85, Ras GTPase-activating protein and RAF1.|||May possibly contribute to susceptibility to systemic lupus erythematosus; increases autophosphorylation and interaction with PI3-kinase subunit p85.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016738|||http://purl.uniprot.org/annotation/VAR_031569|||http://purl.uniprot.org/annotation/VAR_046106|||http://purl.uniprot.org/annotation/VAR_046107|||http://purl.uniprot.org/annotation/VAR_046108|||http://purl.uniprot.org/annotation/VAR_046109|||http://purl.uniprot.org/annotation/VAR_046110|||http://purl.uniprot.org/annotation/VAR_046111|||http://purl.uniprot.org/annotation/VAR_065465|||http://purl.uniprot.org/annotation/VSP_002946|||http://purl.uniprot.org/annotation/VSP_002947|||http://purl.uniprot.org/annotation/VSP_002948|||http://purl.uniprot.org/annotation/VSP_002949|||http://purl.uniprot.org/annotation/VSP_035109|||http://purl.uniprot.org/annotation/VSP_044521
http://togogenome.org/gene/9606:RIBC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4K1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  RIB43A-like with coiled-coils protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254098|||http://purl.uniprot.org/annotation/VAR_028812|||http://purl.uniprot.org/annotation/VAR_028813|||http://purl.uniprot.org/annotation/VAR_028814
http://togogenome.org/gene/9606:RAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4L5|||http://purl.uniprot.org/uniprot/L7RRS6|||http://purl.uniprot.org/uniprot/P04049                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Catalytically inactive.|||Constitutively active and highly phosphorylated on S-338, inhibited by PPP5C. Reduced kinase activity; when associated with 338-A-A-339. Constitutively active and non-inhibited by PPP5C; when associated with 338-D-E-339.|||Disordered|||In CMD1NN; shows a mild increase in kinase activity.|||In CMD1NN; shows impaired kinase activity and reduced MAPK3 activation with this mutation.|||In NS5 and LPRD2; shows in vitro greater kinase activity and enhanced ERK activation than wild-type.|||In NS5 and LPRD2; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type.|||In NS5.|||In NS5; has reduced or absent kinase activity.|||In NS5; shows greater kinase activity and enhanced MAPK1 activation than wild-type.|||In NS5; shows in vitro greater kinase activity and enhanced MAPK1 activation than wild-type.|||In a lung adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation; increased ERK activation.|||In hypertrophic cardiomyopathy; unknown pathological significance.|||In isoform 2.|||Increased kinase activity but can still be inhibited by PPP5C; when associated with D-491.|||Increased kinase activity but can still be inhibited by PPP5C; when associated with D-494.|||Interaction with PEBP1/RKIP|||Loss of methylation. Increased stability and catalytic activity in response to EGF treatment.|||Non-inhibited by PPP5C. Constitutively active and non-inhibited by PPP5C; when associated with 340-D-D-341.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphoserine; by PAK1, PAK2 and PAK3|||Phosphoserine; by PAK1, PAK2, PAK3 and PAK5|||Phosphoserine; by PKA and MAPK1|||Phosphoserine; by PKA, PKC and PKB/AKT1|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by PKA|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SRC|||Polar residues|||Protein kinase|||Proton acceptor|||RAF proto-oncogene serine/threonine-protein kinase|||RBD|||Reduced kinase activity; when associated with 340-D-D-341.|||Symmetric dimethylarginine; by PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086596|||http://purl.uniprot.org/annotation/VAR_018840|||http://purl.uniprot.org/annotation/VAR_037807|||http://purl.uniprot.org/annotation/VAR_037808|||http://purl.uniprot.org/annotation/VAR_037809|||http://purl.uniprot.org/annotation/VAR_037810|||http://purl.uniprot.org/annotation/VAR_037811|||http://purl.uniprot.org/annotation/VAR_037812|||http://purl.uniprot.org/annotation/VAR_037813|||http://purl.uniprot.org/annotation/VAR_037814|||http://purl.uniprot.org/annotation/VAR_037815|||http://purl.uniprot.org/annotation/VAR_037816|||http://purl.uniprot.org/annotation/VAR_037817|||http://purl.uniprot.org/annotation/VAR_037818|||http://purl.uniprot.org/annotation/VAR_037819|||http://purl.uniprot.org/annotation/VAR_037820|||http://purl.uniprot.org/annotation/VAR_037821|||http://purl.uniprot.org/annotation/VAR_041037|||http://purl.uniprot.org/annotation/VAR_041038|||http://purl.uniprot.org/annotation/VAR_071844|||http://purl.uniprot.org/annotation/VAR_071845|||http://purl.uniprot.org/annotation/VAR_071846|||http://purl.uniprot.org/annotation/VAR_071847|||http://purl.uniprot.org/annotation/VAR_071848|||http://purl.uniprot.org/annotation/VAR_071849|||http://purl.uniprot.org/annotation/VSP_034649
http://togogenome.org/gene/9606:TMEM63B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T3F8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CSC1-like protein 2|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280728|||http://purl.uniprot.org/annotation/VAR_031192|||http://purl.uniprot.org/annotation/VSP_023889|||http://purl.uniprot.org/annotation/VSP_023890|||http://purl.uniprot.org/annotation/VSP_023891|||http://purl.uniprot.org/annotation/VSP_023892
http://togogenome.org/gene/9606:ACSS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1R2|||http://purl.uniprot.org/uniprot/Q9H6R3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Acetyl-coenzyme A synthetase N-terminal|||Acyl-CoA synthetase short-chain family member 3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320624|||http://purl.uniprot.org/annotation/VSP_031692
http://togogenome.org/gene/9606:SAC3D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WC89                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||PCI                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:BSPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q075Z2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Binder of sperm protein homolog 1|||Fibronectin type-II 1|||Fibronectin type-II 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326156
http://togogenome.org/gene/9606:GIPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2I7|||http://purl.uniprot.org/uniprot/O14908                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PDZ|||PDZ domain-containing protein GIPC1|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087492|||http://purl.uniprot.org/annotation/VSP_044296
http://togogenome.org/gene/9606:REG1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7G6|||http://purl.uniprot.org/uniprot/P05451                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-type lectin|||Lithostathine-1-alpha|||O-linked (GalNAc) threonine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017424|||http://purl.uniprot.org/annotation/PRO_5002724681
http://togogenome.org/gene/9606:ANKRD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE5|||http://purl.uniprot.org/uniprot/Q92527                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066902|||http://purl.uniprot.org/annotation/VSP_037160
http://togogenome.org/gene/9606:ATP6V1E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA8|||http://purl.uniprot.org/uniprot/Q96A05                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  V-type proton ATPase subunit E 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282344
http://togogenome.org/gene/9606:HBS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZV0|||http://purl.uniprot.org/uniprot/Q9Y450                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with developmental disorder; unknown pathological significance.|||G1|||G2|||G3|||G4|||G5|||HBS1-like protein|||In isoform 2.|||In isoform 3.|||Interaction with the exosome complex|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091491|||http://purl.uniprot.org/annotation/VAR_048963|||http://purl.uniprot.org/annotation/VAR_087990|||http://purl.uniprot.org/annotation/VSP_013624|||http://purl.uniprot.org/annotation/VSP_041068
http://togogenome.org/gene/9606:DEFA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59665                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  ADP-ribosylarginine; by ART1|||Almost complete loss of bactericidal activity.|||HP 1-56|||Neutrophil defensin 1|||Neutrophil defensin 2|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006771|||http://purl.uniprot.org/annotation/PRO_0000006772|||http://purl.uniprot.org/annotation/PRO_0000006773|||http://purl.uniprot.org/annotation/PRO_0000006774
http://togogenome.org/gene/9606:UQCC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YU5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical; Signal-anchor for type II membrane protein|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome c reductase complex assembly factor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340273|||http://purl.uniprot.org/annotation/VAR_062284
http://togogenome.org/gene/9606:OR4F17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWN0|||http://purl.uniprot.org/uniprot/Q8NGA8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 4F17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150550
http://togogenome.org/gene/9606:ARPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59998                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 4|||In DEVLO.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylthreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124049|||http://purl.uniprot.org/annotation/VAR_087805|||http://purl.uniprot.org/annotation/VSP_046150|||http://purl.uniprot.org/annotation/VSP_046151|||http://purl.uniprot.org/annotation/VSP_046753
http://togogenome.org/gene/9606:DLX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56177|||http://purl.uniprot.org/uniprot/X5D2F9                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DLX-1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049020|||http://purl.uniprot.org/annotation/VAR_028443|||http://purl.uniprot.org/annotation/VSP_043589
http://togogenome.org/gene/9606:HMGN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZE9|||http://purl.uniprot.org/uniprot/A0A994J3W4|||http://purl.uniprot.org/uniprot/A0A9L9PXC9|||http://purl.uniprot.org/uniprot/Q15651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||High mobility group nucleosome-binding domain-containing protein 3|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232574|||http://purl.uniprot.org/annotation/VSP_017907|||http://purl.uniprot.org/annotation/VSP_017908
http://togogenome.org/gene/9606:TUT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFM7|||http://purl.uniprot.org/uniprot/Q5TAX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation.|||Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-450.|||Decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-452.|||Disordered|||In isoform 2.|||Loss of LIN28A and pre-let-7 RNA binding and loss of pre-let-7 RNA uridylylation; when associated with A-306.|||Loss of LIN28A and pre-let-7 RNA binding and loss of pre-let-7 RNA uridylylation; when associated with A-309.|||Loss of interaction with LIN28A and pre-let-7 RNA.|||Loss of nucleotidyltransferase activity and stabilization of pre-let-7 miRNAs. Abolishes inhibition of LIRE1 retrotransposition.|||Matrin-type|||Omega-N-methylarginine|||PAP-associated 1|||PAP-associated 2|||Phosphoserine|||Polar residues|||Required for interaction with LIN28A and pre-let-7 RNA|||Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation.|||Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-321.|||Strongly decreased LIN28A and pre-let-7 RNA binding and pre-let-7 RNA uridylylation; when associated with A-324.|||Sufficient for monouridylation activity|||Terminal uridylyltransferase 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150970|||http://purl.uniprot.org/annotation/VAR_028402|||http://purl.uniprot.org/annotation/VSP_038135|||http://purl.uniprot.org/annotation/VSP_038136
http://togogenome.org/gene/9606:FGF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by proprotein convertases|||Disordered|||Fibroblast growth factor 23|||Fibroblast growth factor 23 C-terminal peptide|||Fibroblast growth factor 23 N-terminal peptide|||In ADHR; C-terminal processing is abolished.|||In ADHR; C-terminal processing is abolished; reduced proteolysis by PHEX; resistant to cleavage by furin.|||In ADHR; partially resistant to cleavage by furin.|||In HFTC2.|||In HFTC2; full-length and N-terminal fragments are barely detectable, whereas a C-terminal fragment with the same molecular weight as that from wild-type can be detected.|||In HFTC2; only the C-terminal fragment is secreted, whereas the intact protein is retained in the Golgi complex.|||Loss of glycosylation.|||O-linked (GalNAc) threonine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008998|||http://purl.uniprot.org/annotation/PRO_0000352875|||http://purl.uniprot.org/annotation/PRO_0000352876|||http://purl.uniprot.org/annotation/VAR_010717|||http://purl.uniprot.org/annotation/VAR_010718|||http://purl.uniprot.org/annotation/VAR_010719|||http://purl.uniprot.org/annotation/VAR_010720|||http://purl.uniprot.org/annotation/VAR_018887|||http://purl.uniprot.org/annotation/VAR_023831|||http://purl.uniprot.org/annotation/VAR_071711|||http://purl.uniprot.org/annotation/VAR_071712|||http://purl.uniprot.org/annotation/VAR_071713
http://togogenome.org/gene/9606:ERI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEX5|||http://purl.uniprot.org/uniprot/B4DN03|||http://purl.uniprot.org/uniprot/O43414                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ERI1 exoribonuclease 3|||Exonuclease|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317626|||http://purl.uniprot.org/annotation/VSP_031103|||http://purl.uniprot.org/annotation/VSP_031104
http://togogenome.org/gene/9606:SLC12A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM24|||http://purl.uniprot.org/uniprot/P55011|||http://purl.uniprot.org/uniprot/Q53ZR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished cation-chloride cotransporter activity.|||Amino acid permease N-terminal|||Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Does not affect cation-chloride cotransporter activity.|||Extracellular|||Helical|||In DELMNES.|||In DELMNES; requires 2 nucleotide substitutions.|||In DFNA78.|||In DFNA78; reduced chloride transmembrane transport.|||In isoform 2.|||N-acetylmethionine|||Nearly abolished cation-chloride cotransporter activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||Polar residues|||RFXV motif 1|||RFXV motif 2|||Reduced cation-chloride cotransporter activity.|||SLC12A transporter C-terminal|||Severely impairs transporter activity.|||Slighly reduced cation-chloride cotransporter activity.|||Slightly reduced cation-chloride cotransporter activity.|||Solute carrier family 12 member 2|||Strongly reduced cation-chloride cotransporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178023|||http://purl.uniprot.org/annotation/VAR_085083|||http://purl.uniprot.org/annotation/VAR_085084|||http://purl.uniprot.org/annotation/VAR_085085|||http://purl.uniprot.org/annotation/VAR_085086|||http://purl.uniprot.org/annotation/VAR_085087|||http://purl.uniprot.org/annotation/VAR_085088|||http://purl.uniprot.org/annotation/VAR_085089|||http://purl.uniprot.org/annotation/VAR_085090|||http://purl.uniprot.org/annotation/VAR_085091|||http://purl.uniprot.org/annotation/VSP_006105
http://togogenome.org/gene/9606:ITIH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19823                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mass|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  4-carboxyglutamate|||Aspartate 1-(chondroitin 4-sulfate)-ester|||Inter-alpha-trypsin inhibitor heavy chain H2|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-glycosylated at three sites|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Phosphoserine; by FAM20C|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000140|||http://purl.uniprot.org/annotation/CAR_000214|||http://purl.uniprot.org/annotation/CAR_000215|||http://purl.uniprot.org/annotation/CAR_000216|||http://purl.uniprot.org/annotation/CAR_000217|||http://purl.uniprot.org/annotation/PRO_0000016517|||http://purl.uniprot.org/annotation/PRO_0000016518|||http://purl.uniprot.org/annotation/PRO_0000016519|||http://purl.uniprot.org/annotation/VAR_055248|||http://purl.uniprot.org/annotation/VAR_055249|||http://purl.uniprot.org/annotation/VAR_055250
http://togogenome.org/gene/9606:PIGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2K4ZA02|||http://purl.uniprot.org/uniprot/P37287                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glycosyl transferase family 1|||Helical|||In MCAHS2.|||In MCAHS2; decreased function in GPI anchor biosynthesis; does not fully restore GPI-anchored CD59 surface expression when transfected in PIGA-null cells; does not rescue defective HAMP expression in PIGA-deficient cells overexpressing HJV, suggesting absent or reduced HJV anchorage at the cell membrane.|||In MCAHS2; unknown pathological significance.|||In NEDEPH; does not fully rescue defective HAMP expression in PIGA-deficient cells overexpressing HJV, suggesting decreased function in GPI anchor biosynthesis and absent or reduced HJV anchorage at the cell membrane.|||In NEDEPH; does not rescue defective HAMP expression in PIGA-deficient cells overexpressing HJV, suggesting decreased function in GPI anchor biosynthesis and absent or reduced HJV anchorage at the cell membrane.|||In NEDEPH; unknown pathological significance.|||In PNH1.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PIGA GPI anchor biosynthesis|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit A|||Phosphoserine|||Probable disease-associated variant found in a patient with infantile onset epileptic encephalopathy with dyskinesia and microcephaly.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080326|||http://purl.uniprot.org/annotation/VAR_005531|||http://purl.uniprot.org/annotation/VAR_005532|||http://purl.uniprot.org/annotation/VAR_015436|||http://purl.uniprot.org/annotation/VAR_015437|||http://purl.uniprot.org/annotation/VAR_015438|||http://purl.uniprot.org/annotation/VAR_015439|||http://purl.uniprot.org/annotation/VAR_015440|||http://purl.uniprot.org/annotation/VAR_015441|||http://purl.uniprot.org/annotation/VAR_015442|||http://purl.uniprot.org/annotation/VAR_071069|||http://purl.uniprot.org/annotation/VAR_071070|||http://purl.uniprot.org/annotation/VAR_071071|||http://purl.uniprot.org/annotation/VAR_071072|||http://purl.uniprot.org/annotation/VAR_071073|||http://purl.uniprot.org/annotation/VAR_078230|||http://purl.uniprot.org/annotation/VAR_078721|||http://purl.uniprot.org/annotation/VAR_087043|||http://purl.uniprot.org/annotation/VAR_087044|||http://purl.uniprot.org/annotation/VAR_087045|||http://purl.uniprot.org/annotation/VAR_087046|||http://purl.uniprot.org/annotation/VSP_001802|||http://purl.uniprot.org/annotation/VSP_043366|||http://purl.uniprot.org/annotation/VSP_043367
http://togogenome.org/gene/9606:TM7SF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS93                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 7 superfamily member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022537|||http://purl.uniprot.org/annotation/VAR_034556|||http://purl.uniprot.org/annotation/VAR_051437
http://togogenome.org/gene/9606:RNF40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6K1|||http://purl.uniprot.org/uniprot/O75150                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with RB1.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase BRE1B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055839|||http://purl.uniprot.org/annotation/VAR_055021|||http://purl.uniprot.org/annotation/VAR_055022|||http://purl.uniprot.org/annotation/VSP_016681|||http://purl.uniprot.org/annotation/VSP_016682|||http://purl.uniprot.org/annotation/VSP_016683
http://togogenome.org/gene/9606:ERF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50548                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||ETS|||ETS domain-containing transcription factor ERF|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CHYTS.|||In CRS4.|||In isoform 2.|||Loss of a phosphorylation site.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204101|||http://purl.uniprot.org/annotation/VAR_048947|||http://purl.uniprot.org/annotation/VAR_070098|||http://purl.uniprot.org/annotation/VAR_070099|||http://purl.uniprot.org/annotation/VAR_078043|||http://purl.uniprot.org/annotation/VSP_055487
http://togogenome.org/gene/9606:CCDC177                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQR7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 177|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089954
http://togogenome.org/gene/9606:MDM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 189-A--A-195; 232-A--A-238 and 306-A--A-312.|||Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 189-A--A-195 and 232-A--A-238.|||Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 189-A--A-195 and 306-A--A-312.|||Loss of microtubule binding, no loss of centrosomal localization, little effect on microtubule stability, loss of ability to block centriole reduplication and defective blocking of normal centriole duplication; when associated with 9-A--A-15; 232-A--A-238 and 306-A--A-312.|||Nuclear protein MDM1|||Phosphoserine|||Polar residues|||Pro residues|||ST]-E-Y-X(3)-F motif 1; required for efficient microtubule binding and stabilization|||ST]-E-Y-X(3)-F motif 2; required for efficient microtubule binding and stabilization|||ST]-E-Y-X(3)-F motif 3; required for efficient microtubule binding and stabilization|||ST]-E-Y-X(3)-F motif 4; required for efficient microtubule binding and stabilization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299059|||http://purl.uniprot.org/annotation/VAR_034782|||http://purl.uniprot.org/annotation/VAR_034783|||http://purl.uniprot.org/annotation/VAR_034784|||http://purl.uniprot.org/annotation/VAR_034785|||http://purl.uniprot.org/annotation/VSP_027544|||http://purl.uniprot.org/annotation/VSP_027545|||http://purl.uniprot.org/annotation/VSP_027546|||http://purl.uniprot.org/annotation/VSP_027547|||http://purl.uniprot.org/annotation/VSP_046400|||http://purl.uniprot.org/annotation/VSP_046401
http://togogenome.org/gene/9606:SLC25A26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70HW3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In COXPD28; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity.|||In COXPD28; loss of S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity.|||In COXPD28; unknown pathological significance; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity.|||In COXPD28; unknown pathological significance; decreased protein abundance; decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine antiporter activity.|||In isoform 2 and isoform 3.|||In isoform 3.|||Mitochondrial S-adenosylmethionine carrier protein|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317587|||http://purl.uniprot.org/annotation/VAR_058973|||http://purl.uniprot.org/annotation/VAR_076305|||http://purl.uniprot.org/annotation/VAR_076306|||http://purl.uniprot.org/annotation/VAR_076307|||http://purl.uniprot.org/annotation/VAR_080244|||http://purl.uniprot.org/annotation/VAR_087910|||http://purl.uniprot.org/annotation/VAR_087911|||http://purl.uniprot.org/annotation/VSP_031062|||http://purl.uniprot.org/annotation/VSP_031063|||http://purl.uniprot.org/annotation/VSP_031064
http://togogenome.org/gene/9606:ODF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14990                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 5 AA repeats of [RC]-C-L-C-D|||C-X-P repeat region|||Outer dense fiber protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058024|||http://purl.uniprot.org/annotation/VAR_005523|||http://purl.uniprot.org/annotation/VAR_031684|||http://purl.uniprot.org/annotation/VAR_051251
http://togogenome.org/gene/9606:GABRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTP4|||http://purl.uniprot.org/uniprot/E7EWG0|||http://purl.uniprot.org/uniprot/O00591                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit pi|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000492|||http://purl.uniprot.org/annotation/PRO_5022255021|||http://purl.uniprot.org/annotation/PRO_5022255851|||http://purl.uniprot.org/annotation/VAR_020323|||http://purl.uniprot.org/annotation/VAR_036034
http://togogenome.org/gene/9606:PSMD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00233                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 9|||Basic and acidic residues|||Disordered|||In isoform 3.|||In isoform p27-S.|||PDZ|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173852|||http://purl.uniprot.org/annotation/VAR_009953|||http://purl.uniprot.org/annotation/VAR_057047|||http://purl.uniprot.org/annotation/VAR_057048|||http://purl.uniprot.org/annotation/VAR_057049|||http://purl.uniprot.org/annotation/VSP_005300|||http://purl.uniprot.org/annotation/VSP_046004
http://togogenome.org/gene/9606:NCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62166                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||Interaction with IL1RAPL1|||N-myristoyl glycine|||Neuronal calcium sensor 1|||No effect on interaction with RIC8A.|||Reduces calcium binding; when associated with A-117 or A-165. Abolishes calcium binding; when associated with A-117 and A-165.|||Reduces calcium binding; when associated with A-117. Abolishes calcium binding; when associated with T-81 and A-117.|||Reduces calcium binding; when associated with T-81. Abolishes calcium binding; when associated with T-81 and A-165.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073788|||http://purl.uniprot.org/annotation/VSP_046312
http://togogenome.org/gene/9606:KRI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C108|||http://purl.uniprot.org/uniprot/Q8N9T8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Kri1-like C-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein KRI1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298976|||http://purl.uniprot.org/annotation/VAR_034751|||http://purl.uniprot.org/annotation/VAR_034752|||http://purl.uniprot.org/annotation/VAR_034753|||http://purl.uniprot.org/annotation/VAR_034754|||http://purl.uniprot.org/annotation/VAR_034755|||http://purl.uniprot.org/annotation/VAR_034756|||http://purl.uniprot.org/annotation/VAR_034757|||http://purl.uniprot.org/annotation/VAR_034758
http://togogenome.org/gene/9606:ZNF711                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PK66|||http://purl.uniprot.org/uniprot/Q9Y462                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In XLID97.|||In XLID97; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Required for transcriptional activation|||Transcriptional activator Zfx / Zfy|||Zinc finger protein 711                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047329|||http://purl.uniprot.org/annotation/VAR_062990|||http://purl.uniprot.org/annotation/VAR_062991|||http://purl.uniprot.org/annotation/VAR_062992|||http://purl.uniprot.org/annotation/VAR_062993|||http://purl.uniprot.org/annotation/VAR_062994|||http://purl.uniprot.org/annotation/VAR_062995|||http://purl.uniprot.org/annotation/VAR_078572|||http://purl.uniprot.org/annotation/VSP_016912|||http://purl.uniprot.org/annotation/VSP_039887
http://togogenome.org/gene/9606:PIAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75928|||http://purl.uniprot.org/uniprot/Q2TA77                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to SUMO1.|||Disordered|||E3 SUMO-protein ligase PIAS2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3.|||In isoform PIAS2-alpha.|||LXXLL motif|||Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding.|||Nuclear localization signal|||PINIT|||Phosphoserine|||Reduces affinity for SUMO1.|||SAP|||SP-RING-type|||SUMO1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218976|||http://purl.uniprot.org/annotation/VAR_056693|||http://purl.uniprot.org/annotation/VSP_012196|||http://purl.uniprot.org/annotation/VSP_012197|||http://purl.uniprot.org/annotation/VSP_050008|||http://purl.uniprot.org/annotation/VSP_050009
http://togogenome.org/gene/9606:TAX1BP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14907                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with KCNJ4.|||Found in a patient with dilated cardiomyopathy and septo-optic dysplasia; unknown pathological significance.|||N-acetylserine|||PDZ|||Phosphoserine|||Removed|||Tax1-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233943|||http://purl.uniprot.org/annotation/VAR_073966
http://togogenome.org/gene/9606:SLC7A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBB6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In RP68.|||In RP68; affects subcellular location.|||In RP68; uncertain pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 7 member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307360|||http://purl.uniprot.org/annotation/VAR_035417|||http://purl.uniprot.org/annotation/VAR_071050|||http://purl.uniprot.org/annotation/VAR_071051|||http://purl.uniprot.org/annotation/VAR_071052|||http://purl.uniprot.org/annotation/VAR_071053|||http://purl.uniprot.org/annotation/VAR_071054|||http://purl.uniprot.org/annotation/VAR_071055|||http://purl.uniprot.org/annotation/VAR_071056
http://togogenome.org/gene/9606:CHAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15335                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chondroadherin|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032773|||http://purl.uniprot.org/annotation/VAR_030631|||http://purl.uniprot.org/annotation/VAR_052019
http://togogenome.org/gene/9606:AKAP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02952|||http://purl.uniprot.org/uniprot/Q86TJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein 12|||AKAP CaM-binding 1|||AKAP CaM-binding 2|||AKAP CaM-binding 3|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Involved in PKC-binding|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RII-binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064519|||http://purl.uniprot.org/annotation/VAR_035115|||http://purl.uniprot.org/annotation/VAR_035116|||http://purl.uniprot.org/annotation/VAR_035117|||http://purl.uniprot.org/annotation/VAR_035118|||http://purl.uniprot.org/annotation/VAR_035119|||http://purl.uniprot.org/annotation/VAR_035120|||http://purl.uniprot.org/annotation/VAR_035121|||http://purl.uniprot.org/annotation/VAR_035122|||http://purl.uniprot.org/annotation/VAR_035780|||http://purl.uniprot.org/annotation/VAR_056731|||http://purl.uniprot.org/annotation/VSP_004110|||http://purl.uniprot.org/annotation/VSP_004111|||http://purl.uniprot.org/annotation/VSP_028133|||http://purl.uniprot.org/annotation/VSP_028134
http://togogenome.org/gene/9606:IGF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E3UN46|||http://purl.uniprot.org/uniprot/P01344                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A|||Abolishes proteolytical processing.|||B|||C|||D|||Decreases mature IGF2 levels.|||Disordered|||Does not affect integrin binding. Defective integrin binding and IGF2 signaling; when associated with E-48; E-58 and E-61.|||Does not affect integrin binding. Defective integrin binding and IGF2 signaling; when associated with E-48; E-58 and E-62.|||Does not affect integrin binding. Defective integrin binding and IGF2 signaling; when associated with E-48; E-61 and E-62.|||Does not affect integrin binding. Defective integrin binding and IGF2 signaling; when associated with E-58; E-61 and E-62.|||E peptide|||Important for interaction with integrin|||In SRS3.|||In isoform 2.|||In isoform 3.|||Insulin-like|||Insulin-like growth factor II|||Insulin-like growth factor II Ala-25 Del|||No effect in proteolytical processing.|||O-linked (GalNAc...) threonine|||Preptin|||Slight but significant increase in integrin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015717|||http://purl.uniprot.org/annotation/PRO_0000015718|||http://purl.uniprot.org/annotation/PRO_0000015719|||http://purl.uniprot.org/annotation/PRO_0000370376|||http://purl.uniprot.org/annotation/PRO_5003182530|||http://purl.uniprot.org/annotation/VAR_011959|||http://purl.uniprot.org/annotation/VAR_011960|||http://purl.uniprot.org/annotation/VAR_011961|||http://purl.uniprot.org/annotation/VAR_084336|||http://purl.uniprot.org/annotation/VSP_002708|||http://purl.uniprot.org/annotation/VSP_045624
http://togogenome.org/gene/9606:GATA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15976                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes sumoylation.|||Disordered|||Erythroid transcription factor|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In HAEADA; altered transcriptional activity at canonical GATA1 target genes, affecting both silencing and activation of select genes necessary for effective terminal red cell production; may affect binding to specific genomic loci; partial loss of nuclear localization.|||In HAEADA; altered transcriptional activity at canonical GATA1 target genes, affecting both silencing and activation of select genes necessary for effective terminal red cell production; partial loss of nuclear localization.|||In XDAT; partially disrupts the interaction with ZFPM1.|||In XDAT; severe impairment of ZFPM1 binding and erythroid differentiation in vitro.|||In XDAT; stronger loss of affinity than of G-218-GATA1 for ZFPM1 and disturbed GATA1 self-association.|||In XLTT; does not affect ZFPM1 binding; reduced affinity to palindromic GATA sites; supports erythroid maturation less efficiently than wild-type GATA1.|||In isoform 2.|||In isoform 3.|||Increase of dissociation rate from bound DNA.|||Increased sumoylation in vitro.|||Interaction with CALCOCO1|||Interaction with MED1 and CCAR1|||Loss of sumoylation.|||N6-acetyllysine|||N6-acetyllysine; by CREBBP|||N6-acetyllysine; by EP300|||Phosphoserine|||Required for interaction with ZFPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083397|||http://purl.uniprot.org/annotation/VAR_010115|||http://purl.uniprot.org/annotation/VAR_012706|||http://purl.uniprot.org/annotation/VAR_012707|||http://purl.uniprot.org/annotation/VAR_033114|||http://purl.uniprot.org/annotation/VAR_033115|||http://purl.uniprot.org/annotation/VAR_087448|||http://purl.uniprot.org/annotation/VAR_087449|||http://purl.uniprot.org/annotation/VSP_014782|||http://purl.uniprot.org/annotation/VSP_041451
http://togogenome.org/gene/9606:C8orf82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1X6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||UPF0598 protein C8orf82                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340669|||http://purl.uniprot.org/annotation/VSP_034215
http://togogenome.org/gene/9606:LYSMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 2|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248002|||http://purl.uniprot.org/annotation/VAR_027198|||http://purl.uniprot.org/annotation/VAR_027199|||http://purl.uniprot.org/annotation/VSP_020123
http://togogenome.org/gene/9606:GTF2A1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA3|||http://purl.uniprot.org/uniprot/Q9UNN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||TFIIA-alpha and beta-like factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072495|||http://purl.uniprot.org/annotation/VSP_040935
http://togogenome.org/gene/9606:KRT222                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1A0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  IF rod|||In isoform 2.|||Keratin-like protein KRT222                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344215|||http://purl.uniprot.org/annotation/VSP_034744
http://togogenome.org/gene/9606:SLC16A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKS0|||http://purl.uniprot.org/uniprot/P53985                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AZD3965 does not inhibit lactate transmembrane transporter activity. The affinity for AZD3965 is reduced by 55 folds.|||AZD3965 inhibition is reduced by approximately 2 folds. The affinity for AZD3965 is decreased by 10 folds.|||Abolishes binding with AZD3965.|||Abolishes lactate transmembrane transporter activity.|||Abolishes lactate transmembrane transporter activity. Abolishes expression at the cell membrane.|||Abolishes lactate transmembrane transporter activity. Reduces plasma membrane localization.|||Basic and acidic residues|||Complete loss of lactate transmembrane transporter activity.|||Complete loss of transport lactate transmembrane transporter activity.|||Cytoplasmic|||Decreases interaction with BSN isoform 2.|||Disordered|||Does not affect plasma membrane localization.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MCT1D.|||In SDLT.|||In isoform 2.|||Monocarboxylate transporter 1|||Phosphoserine|||Phosphothreonine|||Reduces lactate transmembrane transporter activity by 50%.|||Reduces lactate transmembrane transporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211381|||http://purl.uniprot.org/annotation/VAR_010434|||http://purl.uniprot.org/annotation/VAR_010435|||http://purl.uniprot.org/annotation/VAR_010436|||http://purl.uniprot.org/annotation/VAR_054804|||http://purl.uniprot.org/annotation/VAR_072428|||http://purl.uniprot.org/annotation/VSP_056191
http://togogenome.org/gene/9606:SARDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K596|||http://purl.uniprot.org/uniprot/Q9UL12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Aminomethyltransferase folate-binding|||Disordered|||FAD dependent oxidoreductase|||FAD dependent oxidoreductase central|||Glycine cleavage T-protein C-terminal barrel|||In SARCOS.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphotyrosine|||Sarcosine dehydrogenase, mitochondrial|||Tele-8alpha-FAD histidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010770|||http://purl.uniprot.org/annotation/VAR_019687|||http://purl.uniprot.org/annotation/VAR_019688|||http://purl.uniprot.org/annotation/VAR_039077|||http://purl.uniprot.org/annotation/VAR_039078|||http://purl.uniprot.org/annotation/VAR_069272|||http://purl.uniprot.org/annotation/VAR_069273|||http://purl.uniprot.org/annotation/VSP_056309
http://togogenome.org/gene/9606:OSM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCX1|||http://purl.uniprot.org/uniprot/P13725                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Inactive.|||Inhibits propeptide cleavage.|||N-linked (GlcNAc...) asparagine|||Oncostatin-M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017720|||http://purl.uniprot.org/annotation/PRO_0000017721|||http://purl.uniprot.org/annotation/VAR_049782
http://togogenome.org/gene/9606:KRTAP5-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8H2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||11 X 4 AA repeats of C-C-X-P|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 5-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184101|||http://purl.uniprot.org/annotation/VAR_060115|||http://purl.uniprot.org/annotation/VAR_060116|||http://purl.uniprot.org/annotation/VAR_060117|||http://purl.uniprot.org/annotation/VAR_060118|||http://purl.uniprot.org/annotation/VAR_060119
http://togogenome.org/gene/9606:OR10H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWJ7|||http://purl.uniprot.org/uniprot/O60403                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a child with sporadic epilepsy; unknown pathological significance.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150703|||http://purl.uniprot.org/annotation/VAR_022049|||http://purl.uniprot.org/annotation/VAR_062062|||http://purl.uniprot.org/annotation/VAR_077833
http://togogenome.org/gene/9606:NPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXD5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Involved in proton transfer during cleavage|||N-acetylneuraminate lyase|||Schiff-base intermediate with substrate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273352|||http://purl.uniprot.org/annotation/VSP_022518|||http://purl.uniprot.org/annotation/VSP_022519|||http://purl.uniprot.org/annotation/VSP_022520|||http://purl.uniprot.org/annotation/VSP_022521|||http://purl.uniprot.org/annotation/VSP_022522
http://togogenome.org/gene/9606:HIBCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL0|||http://purl.uniprot.org/uniprot/Q6NVY1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-hydroxyisobutyryl-CoA hydrolase, mitochondrial|||Enoyl-CoA hydratase/isomerase|||In HIBCHD.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284929|||http://purl.uniprot.org/annotation/VAR_031869|||http://purl.uniprot.org/annotation/VAR_031870|||http://purl.uniprot.org/annotation/VSP_024780
http://togogenome.org/gene/9606:ASB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z670|||http://purl.uniprot.org/uniprot/Q8WXH4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 11|||In isoform 2.|||In isoform 3.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066944|||http://purl.uniprot.org/annotation/VAR_048286|||http://purl.uniprot.org/annotation/VAR_048287|||http://purl.uniprot.org/annotation/VAR_069428|||http://purl.uniprot.org/annotation/VSP_043087|||http://purl.uniprot.org/annotation/VSP_047127
http://togogenome.org/gene/9606:SLC47A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VL8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with renal disease; unknown pathological significance; abolishes TEA transport activity; decreases plasma membrane localization.|||Found in a patient with renal disease; unknown pathological significance; abolishes plasma membrane localization.|||Helical|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Multidrug and toxin extrusion protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311952|||http://purl.uniprot.org/annotation/VAR_037358|||http://purl.uniprot.org/annotation/VAR_086946|||http://purl.uniprot.org/annotation/VAR_086947|||http://purl.uniprot.org/annotation/VSP_029656|||http://purl.uniprot.org/annotation/VSP_029657|||http://purl.uniprot.org/annotation/VSP_029658|||http://purl.uniprot.org/annotation/VSP_029659|||http://purl.uniprot.org/annotation/VSP_029660|||http://purl.uniprot.org/annotation/VSP_029661|||http://purl.uniprot.org/annotation/VSP_029662|||http://purl.uniprot.org/annotation/VSP_029663|||http://purl.uniprot.org/annotation/VSP_029664
http://togogenome.org/gene/9606:PNLIPRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RR3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT|||Pancreatic lipase-related protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286602|||http://purl.uniprot.org/annotation/VAR_032141|||http://purl.uniprot.org/annotation/VAR_032142|||http://purl.uniprot.org/annotation/VAR_032143|||http://purl.uniprot.org/annotation/VAR_060285|||http://purl.uniprot.org/annotation/VAR_060286
http://togogenome.org/gene/9606:GAGE12C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L429                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12B/C/D/E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311977
http://togogenome.org/gene/9606:ACSL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB13|||http://purl.uniprot.org/uniprot/B4DFW3|||http://purl.uniprot.org/uniprot/Q9UKU0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 1 and isoform 8.|||In isoform 2.|||In isoform 3, isoform 2 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 9.|||Long-chain-fatty-acid--CoA ligase 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193115|||http://purl.uniprot.org/annotation/VSP_000241|||http://purl.uniprot.org/annotation/VSP_021024|||http://purl.uniprot.org/annotation/VSP_037819|||http://purl.uniprot.org/annotation/VSP_037820|||http://purl.uniprot.org/annotation/VSP_037821|||http://purl.uniprot.org/annotation/VSP_037822|||http://purl.uniprot.org/annotation/VSP_037823|||http://purl.uniprot.org/annotation/VSP_046954
http://togogenome.org/gene/9606:FAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FAS-associated factor 1|||In isoform Short.|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBA|||UBX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211038|||http://purl.uniprot.org/annotation/VSP_006704
http://togogenome.org/gene/9606:PGBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JS3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||PiggyBac transposable element-derived protein 1|||SCAN box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288052|||http://purl.uniprot.org/annotation/VAR_032384|||http://purl.uniprot.org/annotation/VAR_032385|||http://purl.uniprot.org/annotation/VAR_032386|||http://purl.uniprot.org/annotation/VAR_032387|||http://purl.uniprot.org/annotation/VAR_032388|||http://purl.uniprot.org/annotation/VAR_032389|||http://purl.uniprot.org/annotation/VAR_032390|||http://purl.uniprot.org/annotation/VAR_051273
http://togogenome.org/gene/9606:TMEM39A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV64                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 39A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279224|||http://purl.uniprot.org/annotation/VAR_030871|||http://purl.uniprot.org/annotation/VAR_036095|||http://purl.uniprot.org/annotation/VSP_023416|||http://purl.uniprot.org/annotation/VSP_023417
http://togogenome.org/gene/9606:PDZD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Helical|||In IDDADF.|||PDZ|||PDZ domain-containing protein 8|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Pro residues|||SMP-LTD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058299|||http://purl.uniprot.org/annotation/VAR_051265|||http://purl.uniprot.org/annotation/VAR_051266|||http://purl.uniprot.org/annotation/VAR_087700
http://togogenome.org/gene/9606:CD207                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ71                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member K|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In BIRGD; abolishes mannose-binding ability.|||Loss of binding to 6'-sulfo-LacNAc and 6-sulfo-GlcNAc.|||Loss of binding to 6'-sulfo-LacNAc and invertase.|||Loss of binding to 6'-sulfo-LacNAc.|||N-linked (GlcNAc...) asparagine|||No effect on mannose-binding ability.|||Significant reduction in mannose-binding ability.|||Significant reduction in mannose-binding ability; significant decrease in thermal stability; increased sensitivity of sugar binding to pH change.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223693|||http://purl.uniprot.org/annotation/VAR_054781|||http://purl.uniprot.org/annotation/VAR_054782|||http://purl.uniprot.org/annotation/VAR_054783|||http://purl.uniprot.org/annotation/VAR_054784|||http://purl.uniprot.org/annotation/VAR_056151|||http://purl.uniprot.org/annotation/VAR_059448|||http://purl.uniprot.org/annotation/VAR_063828
http://togogenome.org/gene/9606:TANK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7S3|||http://purl.uniprot.org/uniprot/Q6NW12|||http://purl.uniprot.org/uniprot/Q92844                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by viral Seneca Valley virus protease 3C|||Abolishes interaction with TRAF2 and TRAF3.|||Abolishes interaction with TRAF2; greatly diminishes interaction with TRAF3.|||Cleavage by EMCV protease 3C|||Complete loss of cleavage by Seneca Valley virus protease 3C.|||Diminishes interaction with TRAF2 and TRAF3.|||In isoform 3.|||In isoform Short.|||Interaction with TBK1 and IKBKE|||N-acetylmethionine|||Necessary for interaction with TRAF6|||Necessary for interaction with ZC3H12A|||No effect on cleavage by Seneca Valley virus protease 3C.|||Phosphoserine|||Phosphothreonine|||TRAF family member interaction|||TRAF family member-associated NF-kappa-B activator|||UBZ1-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072427|||http://purl.uniprot.org/annotation/VAR_051409|||http://purl.uniprot.org/annotation/VAR_051410|||http://purl.uniprot.org/annotation/VAR_051411|||http://purl.uniprot.org/annotation/VSP_004442|||http://purl.uniprot.org/annotation/VSP_004443|||http://purl.uniprot.org/annotation/VSP_043702|||http://purl.uniprot.org/annotation/VSP_043703
http://togogenome.org/gene/9606:GPR78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7M4|||http://purl.uniprot.org/uniprot/Q96P69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 78|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||No effect on constitutive activity.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069585|||http://purl.uniprot.org/annotation/VAR_024258|||http://purl.uniprot.org/annotation/VAR_033474|||http://purl.uniprot.org/annotation/VAR_033475
http://togogenome.org/gene/9606:RABGGTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92696                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Geranylgeranyl transferase type-2 subunit alpha|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||PFTA 1|||PFTA 2|||PFTA 3|||PFTA 4|||PFTA 5|||PFTA 6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119757|||http://purl.uniprot.org/annotation/VAR_020406
http://togogenome.org/gene/9606:NMRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPI5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Loss of activity.|||Nicotinamide riboside kinase 2|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215894|||http://purl.uniprot.org/annotation/VAR_024549|||http://purl.uniprot.org/annotation/VSP_054332
http://togogenome.org/gene/9606:TTC28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Phosphoserine|||Polar residues|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 17|||TPR 18|||TPR 19|||TPR 2|||TPR 20|||TPR 21|||TPR 22|||TPR 23|||TPR 24|||TPR 25|||TPR 26|||TPR 27|||TPR 28|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106427
http://togogenome.org/gene/9606:CLUL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5R4|||http://purl.uniprot.org/uniprot/F5GWQ8|||http://purl.uniprot.org/uniprot/Q15846                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Clusterin C-terminal|||Clusterin N-terminal|||Clusterin-like protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005552
http://togogenome.org/gene/9606:NACAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15069                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||NAC-A/B|||NAC-alpha domain-containing protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280748|||http://purl.uniprot.org/annotation/VAR_031195|||http://purl.uniprot.org/annotation/VAR_031196|||http://purl.uniprot.org/annotation/VAR_031197|||http://purl.uniprot.org/annotation/VAR_031198|||http://purl.uniprot.org/annotation/VAR_031199
http://togogenome.org/gene/9606:CINP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW66                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 2-interacting protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326055|||http://purl.uniprot.org/annotation/VAR_039979|||http://purl.uniprot.org/annotation/VAR_039980|||http://purl.uniprot.org/annotation/VSP_045342|||http://purl.uniprot.org/annotation/VSP_045343|||http://purl.uniprot.org/annotation/VSP_046386
http://togogenome.org/gene/9606:SYN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17600                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A|||Asymmetric dimethylarginine|||B; linker|||C; actin-binding and synaptic-vesicle binding|||D; Pro-rich linker|||Disordered|||E|||In XLID50; affects excitatory and inhibitory synaptic transmission leading to neuronal hyperexcitability; fails to rescue defective synaptic vesicle exocytosis in SYN1-knockout mouse neurons; results in severely decreased phosphorylation by CaMK2 and MAPK1; results in delayed axon elongation when tested in SYN1-knockout mouse neurons; severely reduced interaction with SYN2; has no effect on protein targeting to presynapse.|||In XLID50; results in reduced synaptic vesicle mobility, increased clustering of synaptic vesicles at presynatptic terminals and increased frequency of miniature excitatory postsynaptic currents.|||In XLID50; unknown pathological significance; no effect on phosphorylation by CaMK2 and MAPK1; has no effect on axon elongation when tested in SYN1-knockout mouse neurons; slightly reduced protein targeting to presynapse.|||In isoform IB.|||No effect on phosphorylation by CaMK2 and MAPK1; has no effect on axon elongation when tested in SYN1-knockout mouse neurons; slightly reduced protein targeting to presynapse.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CaMK1 and PKA|||Phosphoserine; by CaMK2|||Phosphoserine; by PDPK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Synapsin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183018|||http://purl.uniprot.org/annotation/VAR_086821|||http://purl.uniprot.org/annotation/VAR_086822|||http://purl.uniprot.org/annotation/VAR_086823|||http://purl.uniprot.org/annotation/VAR_086824|||http://purl.uniprot.org/annotation/VSP_006316|||http://purl.uniprot.org/annotation/VSP_006317
http://togogenome.org/gene/9606:L3MBTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5X6|||http://purl.uniprot.org/uniprot/Q969R5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Lethal(3)malignant brain tumor-like protein 2|||MBT|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084448|||http://purl.uniprot.org/annotation/VAR_015093|||http://purl.uniprot.org/annotation/VAR_033998|||http://purl.uniprot.org/annotation/VAR_061675|||http://purl.uniprot.org/annotation/VSP_003904|||http://purl.uniprot.org/annotation/VSP_003905|||http://purl.uniprot.org/annotation/VSP_003906|||http://purl.uniprot.org/annotation/VSP_003907
http://togogenome.org/gene/9606:KCNN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYJ0|||http://purl.uniprot.org/uniprot/Q9UGI6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||Found in a family with non-cirrhotic portal hypertension; unknown pathological significance; gain-of-function variant leading to constitutive activity with very low calcium levels; does not affect interaction with CALM1.|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In ZLS3; gain-of-function variant leading to increased channel sensitivity to calcium and faster channel activation; does not affect interaction with CALM1.|||In isoform 2.|||In isoform 3.|||No effect on inhibition by apamin.|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Pro residues|||Reduced inhibition by apamin.|||Small conductance calcium-activated potassium channel protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155013|||http://purl.uniprot.org/annotation/VAR_081088|||http://purl.uniprot.org/annotation/VAR_083434|||http://purl.uniprot.org/annotation/VAR_083435|||http://purl.uniprot.org/annotation/VAR_083436|||http://purl.uniprot.org/annotation/VAR_083437|||http://purl.uniprot.org/annotation/VSP_039461|||http://purl.uniprot.org/annotation/VSP_039462|||http://purl.uniprot.org/annotation/VSP_047641
http://togogenome.org/gene/9606:PAN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58A45                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Knob domain|||Necessary and sufficient for interaction with PABPC1 but not needed for interaction with PAN2|||PABPC-interacting motif-2 (PAM-2)|||PAN2-PAN3 deadenylation complex subunit PAN3|||Phosphoserine|||Polar residues|||Pseudokinase domain|||Reduces interaction with polyadenylate-binding protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280525|||http://purl.uniprot.org/annotation/VSP_023753|||http://purl.uniprot.org/annotation/VSP_023754|||http://purl.uniprot.org/annotation/VSP_023755|||http://purl.uniprot.org/annotation/VSP_041648|||http://purl.uniprot.org/annotation/VSP_041649
http://togogenome.org/gene/9606:TMEM176B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7V7|||http://purl.uniprot.org/uniprot/Q3YBM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Transmembrane protein 176B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279875|||http://purl.uniprot.org/annotation/VAR_031035|||http://purl.uniprot.org/annotation/VAR_031036|||http://purl.uniprot.org/annotation/VAR_031037|||http://purl.uniprot.org/annotation/VAR_031038|||http://purl.uniprot.org/annotation/VAR_031039|||http://purl.uniprot.org/annotation/VAR_057766|||http://purl.uniprot.org/annotation/VSP_046283
http://togogenome.org/gene/9606:CT47A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:RRAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10301                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||No effect on interaction with OSBPL3.|||Ras-related protein R-Ras|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082650|||http://purl.uniprot.org/annotation/PRO_0000281300
http://togogenome.org/gene/9606:ABHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTE1|||http://purl.uniprot.org/uniprot/Q8WU67                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Phospholipase ABHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280208|||http://purl.uniprot.org/annotation/VAR_031089|||http://purl.uniprot.org/annotation/VSP_056137|||http://purl.uniprot.org/annotation/VSP_056138
http://togogenome.org/gene/9606:LNPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; to produce pregnancy serum form|||Cytoplasmic|||Dileucine internalization motif|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Leucyl-cystinyl aminopeptidase|||Leucyl-cystinyl aminopeptidase, pregnancy serum form|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Tankyrase binding|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095114|||http://purl.uniprot.org/annotation/PRO_0000292264|||http://purl.uniprot.org/annotation/VAR_012812|||http://purl.uniprot.org/annotation/VAR_031616|||http://purl.uniprot.org/annotation/VAR_031617|||http://purl.uniprot.org/annotation/VAR_051567|||http://purl.uniprot.org/annotation/VAR_051568|||http://purl.uniprot.org/annotation/VSP_005448|||http://purl.uniprot.org/annotation/VSP_005449
http://togogenome.org/gene/9606:PLBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4A8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) (high mannose) asparagine; alternate|||N-linked (GlcNAc...) (hybrid) asparagine; alternate|||N-linked (GlcNAc...) asparagine|||Phospholipase B-like 1|||Phospholipase B-like 1 chain A|||Phospholipase B-like 1 chain B|||Phospholipase B-like 1 chain C|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286106|||http://purl.uniprot.org/annotation/PRO_0000425421|||http://purl.uniprot.org/annotation/PRO_0000425422|||http://purl.uniprot.org/annotation/PRO_0000425423|||http://purl.uniprot.org/annotation/PRO_0000425424|||http://purl.uniprot.org/annotation/VAR_032072|||http://purl.uniprot.org/annotation/VAR_032073|||http://purl.uniprot.org/annotation/VAR_032074
http://togogenome.org/gene/9606:BANP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5C2|||http://purl.uniprot.org/uniprot/A0A0S2Z5G4|||http://purl.uniprot.org/uniprot/A0A0S2Z5M2|||http://purl.uniprot.org/uniprot/A0A804HKG3|||http://purl.uniprot.org/uniprot/B3KM38|||http://purl.uniprot.org/uniprot/B4DE54|||http://purl.uniprot.org/uniprot/Q8N9N5|||http://purl.uniprot.org/uniprot/Q9NSS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  BEN|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 2, isoform 3, isoform 6 and isoform 7.|||In isoform 2, isoform 4, isoform 5 and isoform 7.|||In isoform 3.|||In isoform 5.|||Interaction with CUX1 and HDAC1|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Protein BANP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297910|||http://purl.uniprot.org/annotation/VSP_027396|||http://purl.uniprot.org/annotation/VSP_027398|||http://purl.uniprot.org/annotation/VSP_027399|||http://purl.uniprot.org/annotation/VSP_027400|||http://purl.uniprot.org/annotation/VSP_027401|||http://purl.uniprot.org/annotation/VSP_027402|||http://purl.uniprot.org/annotation/VSP_043558
http://togogenome.org/gene/9606:SLC25A42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VD7|||http://purl.uniprot.org/uniprot/Q8NHH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In MECREN; loss-of-function variant unable to rescue motor deficiencies in zebrafish morphants.|||Mitochondrial coenzyme A transporter SLC25A42|||Polar residues|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292336|||http://purl.uniprot.org/annotation/VAR_032970|||http://purl.uniprot.org/annotation/VAR_032971|||http://purl.uniprot.org/annotation/VAR_082152
http://togogenome.org/gene/9606:DIRAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95057                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||GTP-binding protein Di-Ras1|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191648|||http://purl.uniprot.org/annotation/PRO_0000370775
http://togogenome.org/gene/9606:OAZ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y7Y4|||http://purl.uniprot.org/uniprot/Q9UMX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Ornithine decarboxylase antizyme 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220859|||http://purl.uniprot.org/annotation/VSP_056789|||http://purl.uniprot.org/annotation/VSP_056790|||http://purl.uniprot.org/annotation/VSP_056791
http://togogenome.org/gene/9606:SLC2A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14672                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Changes subcellular location mainly to the plasma membrane.|||Cytoplasmic|||Dileucine internalization motif|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In T2D.|||In isoform 2.|||Interaction with SRFBP1|||Loss of palmitoylation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine|||S-palmitoyl cysteine|||Solute carrier family 2, facilitated glucose transporter member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050363|||http://purl.uniprot.org/annotation/VAR_007170|||http://purl.uniprot.org/annotation/VAR_007171|||http://purl.uniprot.org/annotation/VAR_012060|||http://purl.uniprot.org/annotation/VAR_020336|||http://purl.uniprot.org/annotation/VAR_052503|||http://purl.uniprot.org/annotation/VSP_056331|||http://purl.uniprot.org/annotation/VSP_056332
http://togogenome.org/gene/9606:PLEKHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEE1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Omega-N-methylarginine|||PH|||Pleckstrin homology domain-containing family D member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349196
http://togogenome.org/gene/9606:TAS2R20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59543                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082331|||http://purl.uniprot.org/annotation/VAR_053356|||http://purl.uniprot.org/annotation/VAR_053357|||http://purl.uniprot.org/annotation/VAR_053358|||http://purl.uniprot.org/annotation/VAR_053359|||http://purl.uniprot.org/annotation/VAR_053360|||http://purl.uniprot.org/annotation/VAR_053361
http://togogenome.org/gene/9606:DHX58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C10                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX58|||Abolishes RNA binding.|||DECH box|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||Loss of dsRNA-induced ATPase activity.|||Loss of dsRNA-induced ATPase activity. Loss of ds-RNA binding. No effect on cytoplasmic pattern recognition receptor signaling pathway in response to virus.|||Loss of dsRNA-induced ATPase activity. No effect on cytoplasmic pattern recognition receptor signaling pathway in response to virus.|||Loss of dsRNA-induced ATPase activity. No effect on ds-RNA binding. No effect on cytoplasmic pattern recognition receptor signaling pathway in response to virus.|||RLR CTR|||RNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102010|||http://purl.uniprot.org/annotation/VAR_019394|||http://purl.uniprot.org/annotation/VAR_019395|||http://purl.uniprot.org/annotation/VAR_049336|||http://purl.uniprot.org/annotation/VAR_049337|||http://purl.uniprot.org/annotation/VAR_083645
http://togogenome.org/gene/9606:ENOPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHY7                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Enolase-phosphatase E1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254007|||http://purl.uniprot.org/annotation/VSP_021160
http://togogenome.org/gene/9606:STH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Saitohin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072272|||http://purl.uniprot.org/annotation/VAR_019548
http://togogenome.org/gene/9606:TMED7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010395|||http://purl.uniprot.org/annotation/VSP_046247
http://togogenome.org/gene/9606:PTTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95997|||http://purl.uniprot.org/uniprot/Q6IAL9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Abolishes ubiquitination and subsequent degradation; when associated with A-61.|||Abolishes ubiquitination and subsequent degradation; when associated with A-64.|||D-box|||Disordered|||N-acetylalanine|||Phosphoserine; by CDK1|||Removed|||SH3-binding|||Securin|||Strongly reduces transforming capability; when associated with A-163.|||Strongly reduces transforming capability; when associated with L-170; A-172 and L-173.|||TEK-box 1|||TEK-box 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206361
http://togogenome.org/gene/9606:CFAP210                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX81|||http://purl.uniprot.org/uniprot/Q0VFZ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region                                                                                  ^@                                                                                  Cilia- and flagella- associated protein 210|||Disordered|||Trichohyalin-plectin-homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318846
http://togogenome.org/gene/9606:DLX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92988                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein DLX-4|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049028|||http://purl.uniprot.org/annotation/VSP_002236|||http://purl.uniprot.org/annotation/VSP_017043
http://togogenome.org/gene/9606:HDGFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK8|||http://purl.uniprot.org/uniprot/Q5TGJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Hepatoma-derived growth factor-like protein 1|||PWWP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334652|||http://purl.uniprot.org/annotation/VAR_043447
http://togogenome.org/gene/9606:FSIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA03                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibrous sheath-interacting protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314918|||http://purl.uniprot.org/annotation/VAR_038124|||http://purl.uniprot.org/annotation/VAR_038125|||http://purl.uniprot.org/annotation/VAR_038126|||http://purl.uniprot.org/annotation/VAR_038127|||http://purl.uniprot.org/annotation/VAR_038128|||http://purl.uniprot.org/annotation/VAR_038129
http://togogenome.org/gene/9606:NGRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neugrin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294483|||http://purl.uniprot.org/annotation/VAR_053905|||http://purl.uniprot.org/annotation/VAR_053906|||http://purl.uniprot.org/annotation/VSP_039710|||http://purl.uniprot.org/annotation/VSP_039711
http://togogenome.org/gene/9606:KBTBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY47                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119077|||http://purl.uniprot.org/annotation/VAR_037766|||http://purl.uniprot.org/annotation/VAR_037767|||http://purl.uniprot.org/annotation/VAR_037768|||http://purl.uniprot.org/annotation/VAR_037769|||http://purl.uniprot.org/annotation/VAR_037770|||http://purl.uniprot.org/annotation/VAR_037771|||http://purl.uniprot.org/annotation/VAR_037772
http://togogenome.org/gene/9606:VSIG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IQ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||V-set and immunoglobulin domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015004|||http://purl.uniprot.org/annotation/VSP_014119
http://togogenome.org/gene/9606:OR2J3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWT2|||http://purl.uniprot.org/uniprot/O76001                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-3*02; decreased response to C3HEX.|||In allele 6M1-3*03 and allele 6M1-3*04.|||In allele 6M1-3*03.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2J3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150484|||http://purl.uniprot.org/annotation/VAR_010949|||http://purl.uniprot.org/annotation/VAR_010950|||http://purl.uniprot.org/annotation/VAR_010951|||http://purl.uniprot.org/annotation/VAR_010952
http://togogenome.org/gene/9606:CLDN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R687|||http://purl.uniprot.org/uniprot/P56749                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-12|||Cytoplasmic|||Extracellular|||Helical|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144765
http://togogenome.org/gene/9606:TOX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15405                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HMG box|||In isoform 2.|||Polar residues|||TOX high mobility group box family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286353|||http://purl.uniprot.org/annotation/VAR_055952|||http://purl.uniprot.org/annotation/VAR_055953|||http://purl.uniprot.org/annotation/VSP_043095|||http://purl.uniprot.org/annotation/VSP_043096
http://togogenome.org/gene/9606:ADSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTV4|||http://purl.uniprot.org/uniprot/Q8N142                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Adenylosuccinate synthetase isozyme 1|||Disordered|||In MPD5; decreased protein abundance; decreased stability; decreased adenylosuccinate synthase activity.|||In isoform 2.|||Proton acceptor|||Proton donor|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095132|||http://purl.uniprot.org/annotation/VAR_076998|||http://purl.uniprot.org/annotation/VSP_008421
http://togogenome.org/gene/9606:PRICKLE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5U0|||http://purl.uniprot.org/uniprot/B7Z8D2|||http://purl.uniprot.org/uniprot/H0Y413|||http://purl.uniprot.org/uniprot/O43900                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In LOAM; acts as a modifier allele increasing the penetrance and expressivity of LHON-associated mtDNA mutations; reduced protein levels; does not affect localization to mitochondria; results in altered complex V stability and activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||PET|||Phosphoserine|||Polar residues|||Prickle planar cell polarity protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075822|||http://purl.uniprot.org/annotation/VAR_036188|||http://purl.uniprot.org/annotation/VAR_050169|||http://purl.uniprot.org/annotation/VAR_084628|||http://purl.uniprot.org/annotation/VSP_056568|||http://purl.uniprot.org/annotation/VSP_056569
http://togogenome.org/gene/9606:OR5D13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5D13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150591|||http://purl.uniprot.org/annotation/VAR_024099|||http://purl.uniprot.org/annotation/VAR_024100|||http://purl.uniprot.org/annotation/VAR_034220
http://togogenome.org/gene/9606:XPO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QU8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Exportin-6|||Importin N-terminal|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235301|||http://purl.uniprot.org/annotation/VAR_048961|||http://purl.uniprot.org/annotation/VSP_055756
http://togogenome.org/gene/9606:GDAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXN4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||Disordered|||Ganglioside-induced differentiation-associated protein 2|||In SCAR27.|||In isoform 2.|||Macro|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331394|||http://purl.uniprot.org/annotation/VAR_042843|||http://purl.uniprot.org/annotation/VAR_042844|||http://purl.uniprot.org/annotation/VAR_042845|||http://purl.uniprot.org/annotation/VAR_042846|||http://purl.uniprot.org/annotation/VAR_082087|||http://purl.uniprot.org/annotation/VSP_033186
http://togogenome.org/gene/9606:PCDHA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H34|||http://purl.uniprot.org/uniprot/Q9UN74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Polar residues|||Protocadherin alpha-4|||Required for interaction with FYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003890|||http://purl.uniprot.org/annotation/VAR_024390|||http://purl.uniprot.org/annotation/VAR_059180|||http://purl.uniprot.org/annotation/VSP_000677|||http://purl.uniprot.org/annotation/VSP_000678
http://togogenome.org/gene/9606:DCBLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8Z6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||Cytoplasmic|||Discoidin, CUB and LCCL domain-containing protein 1|||Disordered|||Extracellular|||F5/8 type C|||Helical|||In isoform 2.|||LCCL|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021076|||http://purl.uniprot.org/annotation/VSP_040221|||http://purl.uniprot.org/annotation/VSP_040222
http://togogenome.org/gene/9606:ATP5MC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06055                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  ATP synthase F(0) complex subunit C2, mitochondrial|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6,N6,N6-trimethyllysine|||Reversibly protonated during proton transport                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002562|||http://purl.uniprot.org/annotation/VAR_011920|||http://purl.uniprot.org/annotation/VAR_011921|||http://purl.uniprot.org/annotation/VSP_037348|||http://purl.uniprot.org/annotation/VSP_037349
http://togogenome.org/gene/9606:KPNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00505                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Disordered|||IBB|||Importin subunit alpha-4|||In SPG88; decreased interaction with RCC1 and DDX21; no effect on interaction with NCBP1 and NCBP2.|||In SPG88; decreased interaction with RCC1, DDX21, NCBP1 and NCBP2; compared to the wild type, the mutant shows increased cytoplasmic levels.|||In SPG88; loss of interaction with DDX21 and NCBP1; severely decreased interaction with RCC1 and NCBP2; compared to the wild type, the mutant shows increased cytoplasmic levels.|||In SPG88; loss of interaction with RCC1, DDX21, NCBP1 and NCBP2.|||In SPG88; loss of interaction with RCC1; severely decreased interaction with DDX21 and NCBP1; no effect on interaction with NCBP2.|||N-acetylalanine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120724|||http://purl.uniprot.org/annotation/VAR_014454|||http://purl.uniprot.org/annotation/VAR_087813|||http://purl.uniprot.org/annotation/VAR_087814|||http://purl.uniprot.org/annotation/VAR_087815|||http://purl.uniprot.org/annotation/VAR_087816|||http://purl.uniprot.org/annotation/VAR_087817|||http://purl.uniprot.org/annotation/VAR_087818
http://togogenome.org/gene/9606:PCDHGA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003960|||http://purl.uniprot.org/annotation/VAR_048561|||http://purl.uniprot.org/annotation/VAR_048562|||http://purl.uniprot.org/annotation/VAR_048563|||http://purl.uniprot.org/annotation/VSP_008671|||http://purl.uniprot.org/annotation/VSP_008672
http://togogenome.org/gene/9606:NBPF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZJ2                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Olduvai                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TBC1D17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Disordered|||Glutamine finger|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Rab-GAP TBC|||Required for interaction with OPTN|||Strongly decreased inhibition of Rab8-mediated transferrin receptor (TfR) endocytic trafficking; enhanced Rab8 localization on ERC tubules and Rab8 interaction with TfR; impaired inhibitory effect on autophagy.|||TBC1 domain family member 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208045|||http://purl.uniprot.org/annotation/VAR_024655|||http://purl.uniprot.org/annotation/VAR_060276|||http://purl.uniprot.org/annotation/VSP_047344|||http://purl.uniprot.org/annotation/VSP_053997
http://togogenome.org/gene/9606:MCCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK29|||http://purl.uniprot.org/uniprot/Q9HCC0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-CoA binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||In MCC2D.|||In MCC2D; asymptomatic form.|||In MCC2D; has some wild-type residual activity.|||In MCC2D; mild form.|||In MCC2D; produces severely decreased wild-type residual activity.|||In MCC2D; severe and mild form.|||In MCC2D; severe form.|||In MCC2D; shows virtually no enzyme activity.|||In MCC2D; unknown pathological significance.|||In isoform 2.|||Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000291|||http://purl.uniprot.org/annotation/VAR_012792|||http://purl.uniprot.org/annotation/VAR_012793|||http://purl.uniprot.org/annotation/VAR_012794|||http://purl.uniprot.org/annotation/VAR_012795|||http://purl.uniprot.org/annotation/VAR_012796|||http://purl.uniprot.org/annotation/VAR_012797|||http://purl.uniprot.org/annotation/VAR_012798|||http://purl.uniprot.org/annotation/VAR_012799|||http://purl.uniprot.org/annotation/VAR_012800|||http://purl.uniprot.org/annotation/VAR_012801|||http://purl.uniprot.org/annotation/VAR_038630|||http://purl.uniprot.org/annotation/VAR_067199|||http://purl.uniprot.org/annotation/VAR_067200|||http://purl.uniprot.org/annotation/VAR_072507|||http://purl.uniprot.org/annotation/VAR_072508|||http://purl.uniprot.org/annotation/VAR_072509|||http://purl.uniprot.org/annotation/VAR_072510|||http://purl.uniprot.org/annotation/VAR_072511|||http://purl.uniprot.org/annotation/VAR_072512|||http://purl.uniprot.org/annotation/VAR_072513|||http://purl.uniprot.org/annotation/VAR_072514|||http://purl.uniprot.org/annotation/VAR_072515|||http://purl.uniprot.org/annotation/VAR_072516|||http://purl.uniprot.org/annotation/VAR_072517|||http://purl.uniprot.org/annotation/VAR_072518|||http://purl.uniprot.org/annotation/VAR_072519|||http://purl.uniprot.org/annotation/VAR_072520|||http://purl.uniprot.org/annotation/VAR_072521|||http://purl.uniprot.org/annotation/VAR_072522|||http://purl.uniprot.org/annotation/VAR_072523|||http://purl.uniprot.org/annotation/VAR_072524|||http://purl.uniprot.org/annotation/VAR_072525|||http://purl.uniprot.org/annotation/VAR_072526|||http://purl.uniprot.org/annotation/VAR_072527|||http://purl.uniprot.org/annotation/VAR_072528|||http://purl.uniprot.org/annotation/VAR_072529|||http://purl.uniprot.org/annotation/VAR_072530|||http://purl.uniprot.org/annotation/VAR_072531|||http://purl.uniprot.org/annotation/VAR_072532|||http://purl.uniprot.org/annotation/VAR_072533|||http://purl.uniprot.org/annotation/VAR_072534|||http://purl.uniprot.org/annotation/VAR_072535|||http://purl.uniprot.org/annotation/VAR_072536|||http://purl.uniprot.org/annotation/VAR_072537|||http://purl.uniprot.org/annotation/VAR_072538|||http://purl.uniprot.org/annotation/VAR_077291|||http://purl.uniprot.org/annotation/VAR_077292|||http://purl.uniprot.org/annotation/VAR_077293|||http://purl.uniprot.org/annotation/VAR_077294|||http://purl.uniprot.org/annotation/VAR_077295|||http://purl.uniprot.org/annotation/VAR_077296|||http://purl.uniprot.org/annotation/VAR_077297|||http://purl.uniprot.org/annotation/VAR_077298|||http://purl.uniprot.org/annotation/VAR_077299|||http://purl.uniprot.org/annotation/VAR_077300|||http://purl.uniprot.org/annotation/VAR_077301|||http://purl.uniprot.org/annotation/VAR_077302|||http://purl.uniprot.org/annotation/VAR_077303|||http://purl.uniprot.org/annotation/VAR_077304|||http://purl.uniprot.org/annotation/VAR_077305|||http://purl.uniprot.org/annotation/VAR_077306|||http://purl.uniprot.org/annotation/VSP_000069
http://togogenome.org/gene/9606:RBM46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Probable RNA-binding protein 46|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305315|||http://purl.uniprot.org/annotation/VSP_055251|||http://purl.uniprot.org/annotation/VSP_055252
http://togogenome.org/gene/9606:ATP9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSI8|||http://purl.uniprot.org/uniprot/O43861|||http://purl.uniprot.org/uniprot/Q69YZ7|||http://purl.uniprot.org/uniprot/Q7Z3J4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||P-type ATPase C-terminal|||Probable phospholipid-transporting ATPase IIB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046377|||http://purl.uniprot.org/annotation/VAR_047557|||http://purl.uniprot.org/annotation/VAR_047558|||http://purl.uniprot.org/annotation/VAR_047559|||http://purl.uniprot.org/annotation/VAR_061037|||http://purl.uniprot.org/annotation/VSP_035790
http://togogenome.org/gene/9606:SMIM23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Small integral membrane protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341237|||http://purl.uniprot.org/annotation/VAR_057736
http://togogenome.org/gene/9606:TAS2R13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYV9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082247|||http://purl.uniprot.org/annotation/VAR_021853|||http://purl.uniprot.org/annotation/VAR_036432
http://togogenome.org/gene/9606:CNNM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8M5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CBS 1|||CBS 2|||CNNM transmembrane|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HOMG6; reduced activity; electrophysiological analysis shows that magnesium-sensitive sodium currents are significantly diminished and are blocked by increased extracellular magnesium concentrations.|||In HOMGSMR1.|||In HOMGSMR1; results in decreased cellular uptake of magnesium.|||In HOMGSMR1; results in reduced protein membrane expression.|||In HOMGSMR1; results in reduced protein membrane expression; decreases cellular uptake of magnesium.|||In isoform 2.|||In isoform 3.|||Metal transporter CNNM2|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295760|||http://purl.uniprot.org/annotation/VAR_065259|||http://purl.uniprot.org/annotation/VAR_065260|||http://purl.uniprot.org/annotation/VAR_073848|||http://purl.uniprot.org/annotation/VAR_073849|||http://purl.uniprot.org/annotation/VAR_073850|||http://purl.uniprot.org/annotation/VAR_073851|||http://purl.uniprot.org/annotation/VSP_027077|||http://purl.uniprot.org/annotation/VSP_027078|||http://purl.uniprot.org/annotation/VSP_027080
http://togogenome.org/gene/9606:TP53TG3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:SEBOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein SEBOX|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311336|||http://purl.uniprot.org/annotation/VAR_037228
http://togogenome.org/gene/9606:FAHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P587                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acylpyruvase FAHD1, mitochondrial|||Impaired oxaloacetate decarboxylase activity.|||In isoform 2.|||In isoform 3.|||Loss of catalytic activity; when associated with A-102.|||Loss of catalytic activity; when associated with A-106.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156829|||http://purl.uniprot.org/annotation/VAR_049014|||http://purl.uniprot.org/annotation/VSP_013741|||http://purl.uniprot.org/annotation/VSP_046259
http://togogenome.org/gene/9606:PLPP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK38|||http://purl.uniprot.org/uniprot/Q8NEB5                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphatase activity; when associated with A-115 and with A-152.|||Loss of phosphatase activity; when associated with A-115 and with A-208.|||Loss of phosphatase activity; when associated with A-152 and with A-208.|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Phospholipid phosphatase 5|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286945|||http://purl.uniprot.org/annotation/VSP_025241|||http://purl.uniprot.org/annotation/VSP_025242|||http://purl.uniprot.org/annotation/VSP_040055|||http://purl.uniprot.org/annotation/VSP_054076|||http://purl.uniprot.org/annotation/VSP_054077
http://togogenome.org/gene/9606:CASR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41180                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes G-protein coupled receptor activity.|||Abolishes G-protein coupled receptor signaling pathway.|||Abolishes ability of agonist AMG 416 to activate G-protein-coupled receptor activity.|||Abolishes ability to sense calcium or magnesium levels.|||Associated with high serum level of calcium; is also a potential predisposing factor in disorders of bone and mineral metabolism.|||Associated with low serum level of calcium.|||Cysteine-rich (CR)|||Cytoplasmic|||Decreased G-protein coupled receptor signaling pathway.|||Disordered|||Does not demonstrate reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; does not fail to be inserted in the microsomes and does undergo proper glycosylation.|||Extracellular|||Extracellular calcium-sensing receptor|||Found in a patient with primary hyperparathyroidism detected at adulthood; mutant CASR is activated by a higher calcium concentrations than the wild-type.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for ability of agonist AMG 416 to activate G-protein-coupled receptor activity|||In EIG8.|||In EIG8; patients present juvenile myoclonus epilepsy.|||In HHC1.|||In HHC1; Abolished G-protein coupled receptor activity.|||In HHC1; G-protein coupled receptor signaling pathway; less markedly impaired relative to wild-type than L-227; does not affect cell membrane localization.|||In HHC1; although the mutant receptor is expressed normally at the cell surface it is unresponsive with respect to intracellular signaling (MAPK activation) to increases in extracellular calcium concentrations.|||In HHC1; decreased G-protein coupled receptor signaling pathway.|||In HHC1; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization.|||In HHC1; decreased protein level.|||In HHC1; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation.|||In HHC1; does not affect homodimerization; impaired N-glycosylation; impaired cell membrane localization; decreased G-protein coupled receptor signaling pathway.|||In HHC1; has a dose-response curve shifted to the right relative to that of wild-type; demonstrates reduced intracellular and plasma membrane expression and signaling to the MAPK pathway in response to extracellular calcium relative to wild-type; fails to be inserted in the microsomes and does not undergo proper glycosylation.|||In HHC1; impaired homodimerization; impaired cell membrane localization.|||In HHC1; loss-of-function mutation; the quantity of the mutant receptor is higher than that of the wild-type receptor; dose-response curves show that the mutation significantly reduces the sensitivity of the receptor to extracellular calcium concentrations.|||In HHC1; mild; decreased G-protein coupled receptor signaling pathway.|||In HYPOC1.|||In HYPOC1; also in HYPOC1 associated with clinical features of Bartter syndrome; shifts the concentration-response curve of calcium ions to the left.|||In HYPOC1; associated with clinical features of Bartter syndrome.|||In HYPOC1; does not affect the total accumulation of inositol phosphates as a function of extracellular calcium concentrations in transfected cells.|||In HYPOC1; does not produce a significant activating effect; decreased cell surface receptor expression.|||In HYPOC1; increased G-protein coupled receptor signaling pathway.|||In HYPOC1; increased G-protein coupled receptor signaling pathway; does not affect cell membrane localization.|||In HYPOC1; induces a significant shift to the left relative to the wild-type protein in the MAPK response to increasing extracellular calcium concentrations.|||In HYPOC1; leftward shift in the concentration-response curve for the mutant receptor; cells cotransfected with both the wild-type and the mutant receptor show an EC(50) similar to the mutant; a gain-of-function mutation rendering the receptor more sensitive than normal to activation.|||In HYPOC1; shifts the concentration-response curve of calcium ions to the left.|||In HYPOC1; the EC(50) of the mutant is significantly lower than that of wild-type.|||In HYPOC1; the concentration-response curve of the mutant receptor is left-shifted and its EC(50) is significantly lower than that of the wild-type.|||In HYPOC1; the mutation shifts the concentration-response curve to the left and increases maximal activity.|||In HYPOC1; there is a significant leftward shift in the concentration response curves for the effects of extracellular calcium on both intracellular calcium mobilization and MAPK activity.|||In NSHPT and HHC1.|||In NSHPT.|||In NSHPT; Abolished G-protein coupled receptor activity.|||In NSHPT; decreased G-protein coupled receptor signaling pathway; does not affect cell membrane localization.|||In isoform 2.|||Interaction with RNF19A|||Interchain|||Ligand-binding 1 (LB1)|||Ligand-binding 2 (LB2)|||Mutation found in a patient with primary hyperparathyroidism detected at adulthood; inactivating mutation; mutant CASR is activated by a higher calcium concentrations than the wild-type.|||N-linked (GlcNAc...) asparagine|||Nearly abolished G-protein coupled receptor activity.|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with hypercalciuric hypercalcemia; mutant CASR has a right-shifted dose-response to extracellular calcium concentrations; activated by a higher calcium concentrations than the wild-type. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012946|||http://purl.uniprot.org/annotation/VAR_003585|||http://purl.uniprot.org/annotation/VAR_003586|||http://purl.uniprot.org/annotation/VAR_003587|||http://purl.uniprot.org/annotation/VAR_003588|||http://purl.uniprot.org/annotation/VAR_003589|||http://purl.uniprot.org/annotation/VAR_003590|||http://purl.uniprot.org/annotation/VAR_003591|||http://purl.uniprot.org/annotation/VAR_003592|||http://purl.uniprot.org/annotation/VAR_003593|||http://purl.uniprot.org/annotation/VAR_003594|||http://purl.uniprot.org/annotation/VAR_003595|||http://purl.uniprot.org/annotation/VAR_003596|||http://purl.uniprot.org/annotation/VAR_003597|||http://purl.uniprot.org/annotation/VAR_003598|||http://purl.uniprot.org/annotation/VAR_003599|||http://purl.uniprot.org/annotation/VAR_003600|||http://purl.uniprot.org/annotation/VAR_003601|||http://purl.uniprot.org/annotation/VAR_012649|||http://purl.uniprot.org/annotation/VAR_014450|||http://purl.uniprot.org/annotation/VAR_014451|||http://purl.uniprot.org/annotation/VAR_015414|||http://purl.uniprot.org/annotation/VAR_020220|||http://purl.uniprot.org/annotation/VAR_020221|||http://purl.uniprot.org/annotation/VAR_021019|||http://purl.uniprot.org/annotation/VAR_058046|||http://purl.uniprot.org/annotation/VAR_058047|||http://purl.uniprot.org/annotation/VAR_058048|||http://purl.uniprot.org/annotation/VAR_058049|||http://purl.uniprot.org/annotation/VAR_058050|||http://purl.uniprot.org/annotation/VAR_058051|||http://purl.uniprot.org/annotation/VAR_058052|||http://purl.uniprot.org/annotation/VAR_058053|||http://purl.uniprot.org/annotation/VAR_058054|||http://purl.uniprot.org/annotation/VAR_058055|||http://purl.uniprot.org/annotation/VAR_058056|||http://purl.uniprot.org/annotation/VAR_058057|||http://purl.uniprot.org/annotation/VAR_058058|||http://purl.uniprot.org/annotation/VAR_058059|||http://purl.uniprot.org/annotation/VAR_058060|||http://purl.uniprot.org/annotation/VAR_058061|||http://purl.uniprot.org/annotation/VAR_058062|||http://purl.uniprot.org/annotation/VAR_058063|||http://purl.uniprot.org/annotation/VAR_058064|||http://purl.uniprot.org/annotation/VAR_058065|||http://purl.uniprot.org/annotation/VAR_058066|||http://purl.uniprot.org/annotation/VAR_058067|||http://purl.uniprot.org/annotation/VAR_058068|||http://purl.uniprot.org/annotation/VAR_058069|||http://purl.uniprot.org/annotation/VAR_058070|||http://purl.uniprot.org/annotation/VAR_058071|||http://purl.uniprot.org/annotation/VAR_058072|||http://purl.uniprot.org/annotation/VAR_058073|||http://purl.uniprot.org/annotation/VAR_058074|||http://purl.uniprot.org/annotation/VAR_058075|||http://purl.uniprot.org/annotation/VAR_058076|||http://purl.uniprot.org/annotation/VAR_058077|||http://purl.uniprot.org/annotation/VAR_058078|||http://purl.uniprot.org/annotation/VAR_058079|||http://purl.uniprot.org/annotation/VAR_058080|||http://purl.uniprot.org/annotation/VAR_058081|||http://purl.uniprot.org/annotation/VAR_058082|||http://purl.uniprot.org/annotation/VAR_058083|||http://purl.uniprot.org/annotation/VAR_058084|||http://purl.uniprot.org/annotation/VAR_060206|||http://purl.uniprot.org/annotation/VAR_060207|||http://purl.uniprot.org/annotation/VAR_060208|||http://purl.uniprot.org/annotation/VAR_060209|||http://purl.uniprot.org/annotation/VAR_060210|||http://purl.uniprot.org/annotation/VAR_065198|||http://purl.uniprot.org/annotation/VAR_065199|||http://purl.uniprot.org/annotation/VAR_065200|||http://purl.uniprot.org/annotation/VAR_065201|||http://purl.uniprot.org/annotation/VAR_065202|||http://purl.uniprot.org/annotation/VAR_065203|||http://purl.uniprot.org/annotation/VAR_065494|||http://purl.uniprot.org/annotation/VAR_078139|||http://purl.uniprot.org/annotation/VAR_078140|||http://purl.uniprot.org/annotation/VAR_078141|||http://purl.uniprot.org/annotation/VAR_078142|||http://purl.uniprot.org/annotation/VAR_078143|||http://purl.uniprot.org/annotation/VAR_078144|||http://purl.uniprot.org/annotation/VAR_078145|||http://purl.uniprot.org/annotation/VAR_078146|||http://purl.uniprot.org/annotation/VAR_078147|||http://purl.uniprot.org/annotation/VAR_078148|||http://purl.uniprot.org/annotation/VAR_078149|||http://purl.uniprot.org/annotation/VAR_078150|||http://purl.uniprot.org/annotation/VAR_078151|||http://purl.uniprot.org/annotation/VAR_078152|||http://purl.uniprot.org/annotation/VAR_078153|||http://purl.uniprot.org/annotation/VAR_078154|||http://purl.uniprot.org/annotation/VAR_078155|||http://purl.uniprot.org/annotation/VAR_078156|||http://purl.uniprot.org/annotation/VAR_078157|||http://purl.uniprot.org/annotation/VAR_078158|||http://purl.uniprot.org/annotation/VAR_078159|||http://purl.uniprot.org/annotation/VAR_078160|||http://purl.uniprot.org/annotation/VAR_078161|||http://purl.uniprot.org/annotation/VAR_078162|||http://purl.uniprot.org/annotation/VAR_078163|||http://purl.uniprot.org/annotation/VAR_078164|||http://purl.uniprot.org/annotation/VAR_078165|||http://purl.uniprot.org/annotation/VAR_078166|||http://purl.uniprot.org/annotation/VAR_078167|||http://purl.uniprot.org/annotation/VAR_078168|||http://purl.uniprot.org/annotation/VAR_078169|||http://purl.uniprot.org/annotation/VAR_078170|||http://purl.uniprot.org/annotation/VAR_078171|||http://purl.uniprot.org/annotation/VAR_078172|||http://purl.uniprot.org/annotation/VAR_078173|||http://purl.uniprot.org/annotation/VAR_078174|||http://purl.uniprot.org/annotation/VAR_078175|||http://purl.uniprot.org/annotation/VAR_078176|||http://purl.uniprot.org/annotation/VAR_078177|||http://purl.uniprot.org/annotation/VAR_078178|||http://purl.uniprot.org/annotation/VAR_078179|||http://purl.uniprot.org/annotation/VAR_078180|||http://purl.uniprot.org/annotation/VAR_078181|||http://purl.uniprot.org/annotation/VAR_078182|||http://purl.uniprot.org/annotation/VAR_078183|||http://purl.uniprot.org/annotation/VSP_002035
http://togogenome.org/gene/9606:SLC27A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Long-chain fatty acid transport protein 1|||Sufficient for oligomerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193201|||http://purl.uniprot.org/annotation/VSP_055806|||http://purl.uniprot.org/annotation/VSP_055807
http://togogenome.org/gene/9606:HMX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU54                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein HMX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294366
http://togogenome.org/gene/9606:CASZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRV8|||http://purl.uniprot.org/uniprot/Q86V15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a patient with congenital heart defect; severe decrease of positive regulation of transcription from TH promoter.|||Zinc finger protein castor homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046912|||http://purl.uniprot.org/annotation/VAR_077466|||http://purl.uniprot.org/annotation/VSP_027093|||http://purl.uniprot.org/annotation/VSP_027094
http://togogenome.org/gene/9606:PBLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZK5|||http://purl.uniprot.org/uniprot/P30039                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phenazine biosynthesis-like domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162383|||http://purl.uniprot.org/annotation/VAR_022684|||http://purl.uniprot.org/annotation/VAR_022685|||http://purl.uniprot.org/annotation/VAR_072403|||http://purl.uniprot.org/annotation/VSP_053822
http://togogenome.org/gene/9606:RABGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3P9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Arginine finger|||Disordered|||Glutamine finger|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab GTPase-activating protein 1|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298779|||http://purl.uniprot.org/annotation/VSP_052510|||http://purl.uniprot.org/annotation/VSP_052511|||http://purl.uniprot.org/annotation/VSP_052512|||http://purl.uniprot.org/annotation/VSP_052513|||http://purl.uniprot.org/annotation/VSP_052514|||http://purl.uniprot.org/annotation/VSP_052515
http://togogenome.org/gene/9606:PYDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56P42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Pyrin|||Pyrin domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348427|||http://purl.uniprot.org/annotation/VAR_046150
http://togogenome.org/gene/9606:DNAH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLI9|||http://purl.uniprot.org/uniprot/B4E1S1|||http://purl.uniprot.org/uniprot/Q8TD57                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||Dynein axonemal heavy chain 3|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322544|||http://purl.uniprot.org/annotation/VAR_039412|||http://purl.uniprot.org/annotation/VAR_039413|||http://purl.uniprot.org/annotation/VAR_039414|||http://purl.uniprot.org/annotation/VAR_039415|||http://purl.uniprot.org/annotation/VAR_039416|||http://purl.uniprot.org/annotation/VAR_039417|||http://purl.uniprot.org/annotation/VAR_039418|||http://purl.uniprot.org/annotation/VAR_039419|||http://purl.uniprot.org/annotation/VAR_039420|||http://purl.uniprot.org/annotation/VAR_039421|||http://purl.uniprot.org/annotation/VAR_039422|||http://purl.uniprot.org/annotation/VAR_039423|||http://purl.uniprot.org/annotation/VAR_039424|||http://purl.uniprot.org/annotation/VSP_031919|||http://purl.uniprot.org/annotation/VSP_031920|||http://purl.uniprot.org/annotation/VSP_031921|||http://purl.uniprot.org/annotation/VSP_031922|||http://purl.uniprot.org/annotation/VSP_031923|||http://purl.uniprot.org/annotation/VSP_031924|||http://purl.uniprot.org/annotation/VSP_031925
http://togogenome.org/gene/9606:ZBTB46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494BZW5|||http://purl.uniprot.org/uniprot/Q6ZMU8|||http://purl.uniprot.org/uniprot/Q86UZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047746|||http://purl.uniprot.org/annotation/VAR_030629
http://togogenome.org/gene/9606:BNIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12983|||http://purl.uniprot.org/uniprot/Q6NVY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  BCL2/adenovirus E1B 19 kDa protein-interacting protein 3|||BH3|||Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064964
http://togogenome.org/gene/9606:ARL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Q4                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 11|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207479|||http://purl.uniprot.org/annotation/VAR_023742|||http://purl.uniprot.org/annotation/VAR_023743|||http://purl.uniprot.org/annotation/VAR_023744|||http://purl.uniprot.org/annotation/VAR_023745|||http://purl.uniprot.org/annotation/VAR_048318
http://togogenome.org/gene/9606:SPECC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RMV2|||http://purl.uniprot.org/uniprot/Q69YQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Cytospin-A|||Disordered|||In OBLFC1; severely impairs the stabilization of microtubules.|||In TBHS1; has an abnormal punctate expression pattern; has a drastically reduced ability to stabilize microtubules.|||In TBHS1; unknown pathological significance.|||In isoform 2.|||No effect on the stabilization of microtubules.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231018|||http://purl.uniprot.org/annotation/VAR_060448|||http://purl.uniprot.org/annotation/VAR_060449|||http://purl.uniprot.org/annotation/VAR_060450|||http://purl.uniprot.org/annotation/VAR_060451|||http://purl.uniprot.org/annotation/VAR_060452|||http://purl.uniprot.org/annotation/VAR_066872|||http://purl.uniprot.org/annotation/VAR_066873|||http://purl.uniprot.org/annotation/VAR_073384|||http://purl.uniprot.org/annotation/VAR_073385|||http://purl.uniprot.org/annotation/VAR_081478|||http://purl.uniprot.org/annotation/VAR_081479|||http://purl.uniprot.org/annotation/VSP_047359
http://togogenome.org/gene/9606:PPIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23284                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Impairs interaction with CLGN and CANX.|||In OI9; patients have white sclerae, normal dentition, no rhizomelia or severe deformity of long bones.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase B|||Prevents secretion from ER|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025479|||http://purl.uniprot.org/annotation/VAR_047711|||http://purl.uniprot.org/annotation/VAR_063436
http://togogenome.org/gene/9606:CORIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1D5|||http://purl.uniprot.org/uniprot/B4E1Y7|||http://purl.uniprot.org/uniprot/B4E2W9|||http://purl.uniprot.org/uniprot/J3KR83|||http://purl.uniprot.org/uniprot/Q9Y5Q5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment.|||Affects autocatalytic cleavage and production of Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment.|||Atrial natriuretic peptide-converting enzyme|||Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment|||Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment|||Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment|||Atrial natriuretic peptide-converting enzyme, N-terminal propeptide|||Atrial natriuretic peptide-converting enzyme, activated protease fragment|||Basic and acidic residues|||Charge relay system|||Cleavage|||Cleavage; by autolysis|||Cytoplasmic|||DDNN motif|||Disordered|||Does not affect autocatalytic cleavage.|||Extracellular|||FZ|||FZ 1|||FZ 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||Impairs cell membrane targeting; when associated with A-26.|||Impairs cell membrane targeting; when associated with A-30.|||In PEE5.|||In isoform 2.|||Interchain (between N-terminal propeptide and activated protease fragment chains)|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||Loss of activity towards NPPA.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088673|||http://purl.uniprot.org/annotation/PRO_0000391765|||http://purl.uniprot.org/annotation/PRO_0000391766|||http://purl.uniprot.org/annotation/PRO_0000417984|||http://purl.uniprot.org/annotation/PRO_0000417985|||http://purl.uniprot.org/annotation/PRO_0000417986|||http://purl.uniprot.org/annotation/VAR_038000|||http://purl.uniprot.org/annotation/VAR_038001|||http://purl.uniprot.org/annotation/VAR_067795|||http://purl.uniprot.org/annotation/VAR_067796|||http://purl.uniprot.org/annotation/VAR_067797|||http://purl.uniprot.org/annotation/VSP_043952
http://togogenome.org/gene/9606:DTHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMT9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Death|||Death domain-containing protein 1|||In isoform 2.|||ZU5 1|||ZU5 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349274|||http://purl.uniprot.org/annotation/VAR_046339|||http://purl.uniprot.org/annotation/VAR_046340|||http://purl.uniprot.org/annotation/VAR_046341|||http://purl.uniprot.org/annotation/VAR_046342|||http://purl.uniprot.org/annotation/VSP_035302|||http://purl.uniprot.org/annotation/VSP_035303
http://togogenome.org/gene/9606:ZNF133                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52736                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KRAB|||Zinc finger protein 133                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047417|||http://purl.uniprot.org/annotation/VAR_028228|||http://purl.uniprot.org/annotation/VAR_028229|||http://purl.uniprot.org/annotation/VSP_039148|||http://purl.uniprot.org/annotation/VSP_055021|||http://purl.uniprot.org/annotation/VSP_055022|||http://purl.uniprot.org/annotation/VSP_055023
http://togogenome.org/gene/9606:IL1RL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB29                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||Interleukin-1 receptor-like 2|||N-linked (GlcNAc...) asparagine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015445|||http://purl.uniprot.org/annotation/VAR_025259|||http://purl.uniprot.org/annotation/VAR_025260|||http://purl.uniprot.org/annotation/VAR_053378|||http://purl.uniprot.org/annotation/VSP_056292|||http://purl.uniprot.org/annotation/VSP_056293|||http://purl.uniprot.org/annotation/VSP_056294
http://togogenome.org/gene/9606:FAM114A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG4|||http://purl.uniprot.org/uniprot/B3KTE4|||http://purl.uniprot.org/uniprot/B4DQT0|||http://purl.uniprot.org/uniprot/E7ESJ7|||http://purl.uniprot.org/uniprot/I6L9D5|||http://purl.uniprot.org/uniprot/Q9NRY5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Protein FAM114A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274564
http://togogenome.org/gene/9606:CD164                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6R9B4|||http://purl.uniprot.org/uniprot/Q04900                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Required for endosomal and lysosomal localization|||Sialomucin core protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019292|||http://purl.uniprot.org/annotation/VSP_037972|||http://purl.uniprot.org/annotation/VSP_037973|||http://purl.uniprot.org/annotation/VSP_037974|||http://purl.uniprot.org/annotation/VSP_038018|||http://purl.uniprot.org/annotation/VSP_038019
http://togogenome.org/gene/9606:UCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25874|||http://purl.uniprot.org/uniprot/Q4KMT7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with an increased waist-to-hip ratio.|||Associated with susceptibility to type II diabetes mellitus.|||Cysteine sulfenic acid (-SOH)|||Does not affect H(+) transmembrane transport activity.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial brown fat uncoupling protein 1|||Mitochondrial intermembrane|||Mitochondrial matrix|||Severely reduced H(+) transmembrane transport activity.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090657|||http://purl.uniprot.org/annotation/VAR_022840|||http://purl.uniprot.org/annotation/VAR_022841
http://togogenome.org/gene/9606:RTL8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RB0                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Retrotransposon Gag-like protein 8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311694
http://togogenome.org/gene/9606:FAM216A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUB2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein FAM216A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288861|||http://purl.uniprot.org/annotation/VAR_032513
http://togogenome.org/gene/9606:OR6C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RD1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150623|||http://purl.uniprot.org/annotation/VAR_034239|||http://purl.uniprot.org/annotation/VAR_034240|||http://purl.uniprot.org/annotation/VAR_034241|||http://purl.uniprot.org/annotation/VAR_034242
http://togogenome.org/gene/9606:LHX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48742|||http://purl.uniprot.org/uniprot/Q58F18                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075769
http://togogenome.org/gene/9606:CACUL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  CDK2-associated and cullin domain-containing protein 1|||Disordered|||In isoform 2.|||In isoform 4.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119817|||http://purl.uniprot.org/annotation/VSP_013933|||http://purl.uniprot.org/annotation/VSP_013936|||http://purl.uniprot.org/annotation/VSP_013937
http://togogenome.org/gene/9606:RAB33B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0Z5|||http://purl.uniprot.org/uniprot/Q9H082                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||In SMC2.|||In SMC2; strongly inhibits protein expression and may disrupt the Golgi apparatus structure.|||No loss of SGSM2-stimulated GTPase activity.|||Ras-related protein Rab-33B|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121239|||http://purl.uniprot.org/annotation/VAR_068854|||http://purl.uniprot.org/annotation/VAR_068855
http://togogenome.org/gene/9606:CD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06127                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||SRCR 1|||SRCR 2|||SRCR 3|||T-cell surface glycoprotein CD5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033222|||http://purl.uniprot.org/annotation/VAR_020411|||http://purl.uniprot.org/annotation/VAR_024649|||http://purl.uniprot.org/annotation/VAR_058203
http://togogenome.org/gene/9606:TGIF2-RAB5IF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYL0                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Helical|||Homeobox KN                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PARD3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PDZ 1|||PDZ 2|||PDZ 3|||Partitioning defective 3 homolog B|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185072|||http://purl.uniprot.org/annotation/VAR_015664|||http://purl.uniprot.org/annotation/VAR_015665|||http://purl.uniprot.org/annotation/VAR_015666|||http://purl.uniprot.org/annotation/VAR_056642|||http://purl.uniprot.org/annotation/VSP_007476|||http://purl.uniprot.org/annotation/VSP_007477|||http://purl.uniprot.org/annotation/VSP_007478|||http://purl.uniprot.org/annotation/VSP_007479|||http://purl.uniprot.org/annotation/VSP_007543|||http://purl.uniprot.org/annotation/VSP_054048
http://togogenome.org/gene/9606:RNASEK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5S7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Ribonuclease kappa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344221|||http://purl.uniprot.org/annotation/VSP_046496
http://togogenome.org/gene/9606:MARCHF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2E8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Site|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase MARCHF4|||Helical|||Polar residues|||Pro residues|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055930
http://togogenome.org/gene/9606:PEAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VY43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||EMI|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Platelet endothelial aggregation receptor 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309737|||http://purl.uniprot.org/annotation/VAR_048978|||http://purl.uniprot.org/annotation/VAR_048979|||http://purl.uniprot.org/annotation/VAR_048980|||http://purl.uniprot.org/annotation/VAR_061158
http://togogenome.org/gene/9606:GPR85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0T8|||http://purl.uniprot.org/uniprot/P60893|||http://purl.uniprot.org/uniprot/Q8NEN2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance; induces response to endoplasmic reticulum stress; negative regulation of dendrite morphogenesis.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 85                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069591|||http://purl.uniprot.org/annotation/VAR_074204|||http://purl.uniprot.org/annotation/VAR_074205
http://togogenome.org/gene/9606:COX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12887                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC4DN3.|||In isoform 2.|||Mitochondrion|||Protoheme IX farnesyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035923|||http://purl.uniprot.org/annotation/VAR_026562|||http://purl.uniprot.org/annotation/VAR_026563|||http://purl.uniprot.org/annotation/VAR_026564|||http://purl.uniprot.org/annotation/VAR_026565|||http://purl.uniprot.org/annotation/VAR_026566|||http://purl.uniprot.org/annotation/VAR_057371|||http://purl.uniprot.org/annotation/VAR_057372|||http://purl.uniprot.org/annotation/VAR_057373|||http://purl.uniprot.org/annotation/VAR_060233|||http://purl.uniprot.org/annotation/VAR_060234|||http://purl.uniprot.org/annotation/VAR_064768|||http://purl.uniprot.org/annotation/VAR_076181|||http://purl.uniprot.org/annotation/VAR_076182|||http://purl.uniprot.org/annotation/VSP_056867|||http://purl.uniprot.org/annotation/VSP_056868
http://togogenome.org/gene/9606:TSPAN16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKR8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Tetraspanin-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219264|||http://purl.uniprot.org/annotation/VAR_052329|||http://purl.uniprot.org/annotation/VAR_052330|||http://purl.uniprot.org/annotation/VAR_052331|||http://purl.uniprot.org/annotation/VSP_056723|||http://purl.uniprot.org/annotation/VSP_056724|||http://purl.uniprot.org/annotation/VSP_056725|||http://purl.uniprot.org/annotation/VSP_056726
http://togogenome.org/gene/9606:CDC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTU6|||http://purl.uniprot.org/uniprot/B2R6V2|||http://purl.uniprot.org/uniprot/O00311                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell division cycle 7-related protein kinase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085763|||http://purl.uniprot.org/annotation/VAR_019255|||http://purl.uniprot.org/annotation/VAR_019256|||http://purl.uniprot.org/annotation/VAR_019257|||http://purl.uniprot.org/annotation/VAR_019258|||http://purl.uniprot.org/annotation/VAR_019259|||http://purl.uniprot.org/annotation/VAR_040403|||http://purl.uniprot.org/annotation/VAR_040404|||http://purl.uniprot.org/annotation/VAR_040405|||http://purl.uniprot.org/annotation/VAR_040406
http://togogenome.org/gene/9606:ANKRD31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7Z5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat domain-containing protein 31|||Basic and acidic residues|||Disordered|||Polar residues|||RAMA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328839|||http://purl.uniprot.org/annotation/VAR_042542|||http://purl.uniprot.org/annotation/VAR_042543|||http://purl.uniprot.org/annotation/VAR_042544|||http://purl.uniprot.org/annotation/VAR_042545
http://togogenome.org/gene/9606:IMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ENR5|||http://purl.uniprot.org/uniprot/Q96G21                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue                                                                                  ^@                                                                                  Brix|||U3 small nucleolar ribonucleoprotein protein IMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120236
http://togogenome.org/gene/9606:MIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I4AY87|||http://purl.uniprot.org/uniprot/P14174                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Causes formation of interchain disulfide bonds with Cys-81 from another subunit.|||Macrophage migration inhibitory factor|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Proton acceptor; via imino nitrogen|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158062
http://togogenome.org/gene/9606:ZNF428                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L9C8|||http://purl.uniprot.org/uniprot/Q96B54                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||Disordered|||Phosphothreonine|||Zinc finger protein 428                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312346
http://togogenome.org/gene/9606:GTPBP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1E9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GTP-binding protein 10|||In isoform 2.|||In isoform 3.|||OBG-type G|||Obg                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312630|||http://purl.uniprot.org/annotation/VAR_037543|||http://purl.uniprot.org/annotation/VAR_037544|||http://purl.uniprot.org/annotation/VAR_037545|||http://purl.uniprot.org/annotation/VAR_037546|||http://purl.uniprot.org/annotation/VSP_029880|||http://purl.uniprot.org/annotation/VSP_029881|||http://purl.uniprot.org/annotation/VSP_029882
http://togogenome.org/gene/9606:CRCT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteine-rich C-terminal protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096812|||http://purl.uniprot.org/annotation/VAR_050906
http://togogenome.org/gene/9606:SSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43308                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Translocon-associated protein subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033290
http://togogenome.org/gene/9606:COL6A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZW00|||http://purl.uniprot.org/uniprot/D9ZGF2|||http://purl.uniprot.org/uniprot/P12111|||http://purl.uniprot.org/uniprot/Q63HQ4|||http://purl.uniprot.org/uniprot/Q8N4Z1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine; alternate|||BPTI/Kunitz inhibitor|||Basic and acidic residues|||Cell attachment site|||Collagen alpha-3(VI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Disordered|||Fibronectin type-III|||In BTHLM1.|||In DYT27.|||In UCMD1.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Interchain|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||O-linked (Gal...) hydroxylysine; alternate|||Phosphoserine|||Phosphothreonine|||Reactive bond|||Triple-helical region|||VWFA|||VWFA 1|||VWFA 10|||VWFA 11|||VWFA 12|||VWFA 2|||VWFA 3|||VWFA 4|||VWFA 5|||VWFA 6|||VWFA 7|||VWFA 8|||VWFA 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005847|||http://purl.uniprot.org/annotation/PRO_5002867314|||http://purl.uniprot.org/annotation/PRO_5004267193|||http://purl.uniprot.org/annotation/PRO_5036280698|||http://purl.uniprot.org/annotation/VAR_001910|||http://purl.uniprot.org/annotation/VAR_001911|||http://purl.uniprot.org/annotation/VAR_047279|||http://purl.uniprot.org/annotation/VAR_047280|||http://purl.uniprot.org/annotation/VAR_047281|||http://purl.uniprot.org/annotation/VAR_047282|||http://purl.uniprot.org/annotation/VAR_047283|||http://purl.uniprot.org/annotation/VAR_047284|||http://purl.uniprot.org/annotation/VAR_047285|||http://purl.uniprot.org/annotation/VAR_047286|||http://purl.uniprot.org/annotation/VAR_047287|||http://purl.uniprot.org/annotation/VAR_047288|||http://purl.uniprot.org/annotation/VAR_058242|||http://purl.uniprot.org/annotation/VAR_058243|||http://purl.uniprot.org/annotation/VAR_058244|||http://purl.uniprot.org/annotation/VAR_058245|||http://purl.uniprot.org/annotation/VAR_058246|||http://purl.uniprot.org/annotation/VAR_058247|||http://purl.uniprot.org/annotation/VAR_058248|||http://purl.uniprot.org/annotation/VAR_058249|||http://purl.uniprot.org/annotation/VAR_058250|||http://purl.uniprot.org/annotation/VAR_058251|||http://purl.uniprot.org/annotation/VAR_058252|||http://purl.uniprot.org/annotation/VAR_058253|||http://purl.uniprot.org/annotation/VAR_058254|||http://purl.uniprot.org/annotation/VAR_058255|||http://purl.uniprot.org/annotation/VAR_058256|||http://purl.uniprot.org/annotation/VAR_058257|||http://purl.uniprot.org/annotation/VAR_058258|||http://purl.uniprot.org/annotation/VAR_058259|||http://purl.uniprot.org/annotation/VAR_058260|||http://purl.uniprot.org/annotation/VAR_058261|||http://purl.uniprot.org/annotation/VAR_058262|||http://purl.uniprot.org/annotation/VAR_058263|||http://purl.uniprot.org/annotation/VAR_058264|||http://purl.uniprot.org/annotation/VAR_073836|||http://purl.uniprot.org/annotation/VAR_073837|||http://purl.uniprot.org/annotation/VAR_073838|||http://purl.uniprot.org/annotation/VAR_073839|||http://purl.uniprot.org/annotation/VSP_001172|||http://purl.uniprot.org/annotation/VSP_043434|||http://purl.uniprot.org/annotation/VSP_043435|||http://purl.uniprot.org/annotation/VSP_043436|||http://purl.uniprot.org/annotation/VSP_045718|||http://purl.uniprot.org/annotation/VSP_045719
http://togogenome.org/gene/9606:SELENOH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZQ5                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Non standard residue                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec); redox-active|||N6-acetyllysine|||Selenocysteine|||Selenoprotein H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097667
http://togogenome.org/gene/9606:IFNA21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GUQ6|||http://purl.uniprot.org/uniprot/P01568                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016370|||http://purl.uniprot.org/annotation/PRO_5031569905|||http://purl.uniprot.org/annotation/VAR_049638|||http://purl.uniprot.org/annotation/VAR_055325
http://togogenome.org/gene/9606:PHB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K401|||http://purl.uniprot.org/uniprot/P35232|||http://purl.uniprot.org/uniprot/Q53FV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 7|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphothreonine|||Phosphotyrosine|||Prohibitin 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213878|||http://purl.uniprot.org/annotation/VAR_006479|||http://purl.uniprot.org/annotation/VAR_006480|||http://purl.uniprot.org/annotation/VSP_054922
http://togogenome.org/gene/9606:SIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3P8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glycosylation.|||Abolishes interaction with CSK and impairs inhibition of NF-AT activation.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with CSK|||Interaction with GRB2|||Interaction with PTPN11|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on interaction with PTPN11 or GRB2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces interaction with GRB2. Abolishes interaction with GRB2; when associated with F-188.|||Reduces interaction with GRB2. Abolishes interaction with GRB2; when associated with F-90.|||Reduces interaction with PTPN11, no effect on inhibition of NF-AT activation.|||Signaling threshold-regulating transmembrane adapter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045152
http://togogenome.org/gene/9606:SEPTIN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU15                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Found in patients with teratozoospermia; unknown pathological significance; sperm heads are malformed and contain vacuoles; chromatin packaging and structure is abnormal with an increase in fragmented DNA; decreases sperm filamentous structure formation; loss of SEPTIN14 and ACTN4 localization to cell filament structures; no effect on interaction with ACTN4.|||G1 motif|||G3 motif|||G4 motif|||Required for interaction with SEPTIN4. Required for migration of cortical neurons during corticogenesis|||Septin-14|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294425|||http://purl.uniprot.org/annotation/VAR_085117|||http://purl.uniprot.org/annotation/VAR_085118
http://togogenome.org/gene/9606:EBI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14213                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Fibronectin type-III 1|||Fibronectin type-III 2|||Interleukin-27 subunit beta|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010937|||http://purl.uniprot.org/annotation/VAR_024342|||http://purl.uniprot.org/annotation/VAR_049171
http://togogenome.org/gene/9606:WRAP53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUR4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by ATM and impaired ability to promote DNA repair.|||Disordered|||In DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli.|||In DKCB3; shortened telomeres; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Telomerase Cajal body protein 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242696|||http://purl.uniprot.org/annotation/VAR_026865|||http://purl.uniprot.org/annotation/VAR_026866|||http://purl.uniprot.org/annotation/VAR_026867|||http://purl.uniprot.org/annotation/VAR_057618|||http://purl.uniprot.org/annotation/VAR_057619|||http://purl.uniprot.org/annotation/VAR_057620|||http://purl.uniprot.org/annotation/VAR_065873|||http://purl.uniprot.org/annotation/VAR_065874|||http://purl.uniprot.org/annotation/VAR_065875|||http://purl.uniprot.org/annotation/VAR_065876
http://togogenome.org/gene/9606:C3orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1S2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylalanine|||Protein C3orf33|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254577|||http://purl.uniprot.org/annotation/VAR_028846|||http://purl.uniprot.org/annotation/VAR_028847|||http://purl.uniprot.org/annotation/VSP_046233
http://togogenome.org/gene/9606:LSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7L8|||http://purl.uniprot.org/uniprot/P33241                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Lymphocyte-specific protein 1|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084503|||http://purl.uniprot.org/annotation/VAR_011867|||http://purl.uniprot.org/annotation/VAR_011868|||http://purl.uniprot.org/annotation/VAR_061680|||http://purl.uniprot.org/annotation/VSP_045655|||http://purl.uniprot.org/annotation/VSP_045983
http://togogenome.org/gene/9606:IFNE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WN2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon epsilon|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317631|||http://purl.uniprot.org/annotation/VAR_049639
http://togogenome.org/gene/9606:RAB1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8M7|||http://purl.uniprot.org/uniprot/P62820|||http://purl.uniprot.org/uniprot/Q5U0I6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||(Microbial infection) O-(2-cholinephosphoryl)serine|||Abolished arginine GlcNAcylation; when associated with A-74 and A-111. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-111.|||Abolished arginine GlcNAcylation; when associated with A-74 and A-82. Abolished arginine GlcNAcylation; when associated with 72-A--A-74 and A-82.|||Abolished arginine GlcNAcylation; when associated with A-82 and A-111.|||Disordered|||Dominant negative mutant. Strongly reduces the levels of CASR present at the cell-surface.|||Effector region|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine; by CDK1|||Polar residues|||Ras-related protein Rab-1A|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121056|||http://purl.uniprot.org/annotation/VSP_005525|||http://purl.uniprot.org/annotation/VSP_005526
http://togogenome.org/gene/9606:CSTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H114                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cystatin|||Cystatin-like 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006662|||http://purl.uniprot.org/annotation/VAR_024425|||http://purl.uniprot.org/annotation/VAR_024426|||http://purl.uniprot.org/annotation/VAR_033841|||http://purl.uniprot.org/annotation/VAR_033842|||http://purl.uniprot.org/annotation/VAR_033843
http://togogenome.org/gene/9606:FERMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AC1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes lipid-binding via the N-terminus; when associated with 74-A--A-81.|||Abolishes lipid-binding via the N-terminus; when associated with A-40.|||Abolishes phosphatidylinositol phosphate binding.|||Basic and acidic residues|||Disordered|||FERM|||Fermitin family homolog 2|||Impairs ITGB3 binding. Abolishes enhancement of talin-mediated integrin activation.|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with membranes containing phosphatidylinositol phosphate|||PH|||Phosphoserine|||Reduces integrin activation; when associated with A-383.|||Reduces phosphatidylinositol phosphate binding.|||Reduces phosphatidylinositol phosphate binding. Reduces integrin activation; when associated with A-385.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219456|||http://purl.uniprot.org/annotation/VSP_008783|||http://purl.uniprot.org/annotation/VSP_008784|||http://purl.uniprot.org/annotation/VSP_008785
http://togogenome.org/gene/9606:PPP1R35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Does not affect centriole localization; when associated with A-79. Does not affect interaction with RTTN; when associated with A-79.|||Does not affect centriole localization; when associated with A-81. Does not affect interaction with RTTN; when associated with A-81.|||Does not affect centrosome localization; when associated with A-45 and A-47. Does not affect interaction with RTTN; when associated with A-45 and A-47.|||Does not affect centrosome localization; when associated with A-45 and A-52. Does not affect interaction with RTTN; when associated with A-45 and A-52.|||Does not affect centrosome localization; when associated with A-47 and A-52. Does not affect interaction with RTTN; when associated with A-47 and A-52.|||Does not affect centrosome localization; when associated with D-45 and D-47. Does not affect interaction with RTTN; when associated with D-45 and D-47.|||Does not affect centrosome localization; when associated with D-45 and D-52. Does not affect interaction with RTTN; when associated with D-45 and D-52.|||Does not affect centrosome localization; when associated with D-47 and D-52. Does not affect interaction with RTTN; when associated with D-47 and D-52.|||Phosphoserine|||Pro residues|||Protein phosphatase 1 regulatory subunit 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271356
http://togogenome.org/gene/9606:MSRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXL7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  30-fold reduction in activity.|||500-fold reduction in activity.|||7000-fold reduction in activity.|||Disordered|||Endoplasmic reticulum retention signal|||In DFNB74; abolishes zinc-binding and enzymatic activity.|||In isoform 2.|||Methionine-R-sulfoxide reductase B3|||MsrB|||N6-acetyllysine|||Nucleophile|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327240|||http://purl.uniprot.org/annotation/VAR_064904|||http://purl.uniprot.org/annotation/VSP_040883
http://togogenome.org/gene/9606:MOGAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PD6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  2-acylglycerol O-acyltransferase 1|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249058|||http://purl.uniprot.org/annotation/VAR_027389|||http://purl.uniprot.org/annotation/VAR_055695
http://togogenome.org/gene/9606:ZNF572                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3I7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||Polar residues|||Zinc finger protein 572                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251223|||http://purl.uniprot.org/annotation/VAR_027664|||http://purl.uniprot.org/annotation/VAR_027665|||http://purl.uniprot.org/annotation/VAR_027666|||http://purl.uniprot.org/annotation/VAR_027667|||http://purl.uniprot.org/annotation/VAR_035591
http://togogenome.org/gene/9606:H2BC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06899                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-J|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071836
http://togogenome.org/gene/9606:TRAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0N0|||http://purl.uniprot.org/uniprot/B7Z218|||http://purl.uniprot.org/uniprot/B7ZAE5|||http://purl.uniprot.org/uniprot/Q9UPV9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HAP1 N-terminal|||In DEE68; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with HGS|||Interaction with OGT|||Loss of interaction with OGT, but interacts with KIF5B and RHOT1/2 and is able to localize to mitochondria. Increased O-glycosylation of this protein by OGT.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Phosphoserine|||Polar residues|||Reduced O-glycosylation of this protein.|||Reduced O-glycosylation of this protein; when associated with A-829.|||Reduced O-glycosylation of this protein; when associated with A-830.|||Trafficking kinesin-binding protein 1|||Trafficking kinesin-binding protein C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058037|||http://purl.uniprot.org/annotation/VAR_081639|||http://purl.uniprot.org/annotation/VSP_010839|||http://purl.uniprot.org/annotation/VSP_010840|||http://purl.uniprot.org/annotation/VSP_010841|||http://purl.uniprot.org/annotation/VSP_045558|||http://purl.uniprot.org/annotation/VSP_045559|||http://purl.uniprot.org/annotation/VSP_045560
http://togogenome.org/gene/9606:ZRSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSD0|||http://purl.uniprot.org/uniprot/Q15696                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Signal Peptide|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||RRM|||U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082001|||http://purl.uniprot.org/annotation/PRO_5035241810
http://togogenome.org/gene/9606:TCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17987                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||T-complex protein 1 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128302|||http://purl.uniprot.org/annotation/VAR_036258
http://togogenome.org/gene/9606:TTC31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AM3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281149|||http://purl.uniprot.org/annotation/VAR_047357|||http://purl.uniprot.org/annotation/VAR_047358|||http://purl.uniprot.org/annotation/VSP_023990|||http://purl.uniprot.org/annotation/VSP_023991
http://togogenome.org/gene/9606:EPCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16422                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Changed glycosylation pattern. Complete loss of glycosylation and substantial decrease in protein expression; when associated with A-111 and A-198.|||Changed glycosylation pattern. Complete loss of glycosylation and substantial decrease in protein expression; when associated with A-74 and A-198.|||Cytoplasmic|||Decreased glycosylation, reduced protein stability and significant decrease in protein expression. Complete loss of glycosylation and substantial decrease in protein expression; when associated with A-74 and A-111.|||Epithelial cell adhesion molecule|||Extracellular|||Helical|||In DIAR5.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022467|||http://purl.uniprot.org/annotation/VAR_018329|||http://purl.uniprot.org/annotation/VAR_063829
http://togogenome.org/gene/9606:CENPV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7K6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes chromatin hypercondensation phenotype induced by overexpression of wild-type protein.|||Abolishes chromatin hypercondensation phenotype induced by overexpression of wild-type protein; when associated with A-172.|||Abolishes chromatin hypercondensation phenotype induced by overexpression of wild-type protein; when associated with A-177.|||Basic and acidic residues|||CENP-V/GFA|||Centromere protein V|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244359|||http://purl.uniprot.org/annotation/VSP_019549|||http://purl.uniprot.org/annotation/VSP_019550
http://togogenome.org/gene/9606:MAPK14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0K5|||http://purl.uniprot.org/uniprot/L7RSM2|||http://purl.uniprot.org/uniprot/Q16539                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Emulation of the active state. Increase in activity; when associated with A-176.|||Emulation of the active state. Increase in activity; when associated with S-327 or L-327.|||Impairs MAP2K6/MKK6-dependent autophosphorylation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 5.|||In isoform CSBP1.|||In isoform Exip.|||In isoform Mxi2.|||Loss of kinase activity.|||Lowered kinase activity.|||Mitogen-activated protein kinase 14|||N-acetylserine|||N6-acetyllysine|||No effect on either the kinase activity or tyrosine phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis|||Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis|||Phosphotyrosine; by ZAP70|||Protein kinase|||Proton acceptor|||Removed|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186291|||http://purl.uniprot.org/annotation/VAR_042270|||http://purl.uniprot.org/annotation/VAR_042271|||http://purl.uniprot.org/annotation/VAR_042272|||http://purl.uniprot.org/annotation/VSP_004842|||http://purl.uniprot.org/annotation/VSP_004843|||http://purl.uniprot.org/annotation/VSP_004844|||http://purl.uniprot.org/annotation/VSP_004845|||http://purl.uniprot.org/annotation/VSP_057194
http://togogenome.org/gene/9606:CTNNAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBT7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-catulin|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064268|||http://purl.uniprot.org/annotation/VAR_020924|||http://purl.uniprot.org/annotation/VAR_020925|||http://purl.uniprot.org/annotation/VAR_020926|||http://purl.uniprot.org/annotation/VAR_020927|||http://purl.uniprot.org/annotation/VAR_020928|||http://purl.uniprot.org/annotation/VAR_033845|||http://purl.uniprot.org/annotation/VAR_053370|||http://purl.uniprot.org/annotation/VSP_012582|||http://purl.uniprot.org/annotation/VSP_012583
http://togogenome.org/gene/9606:NTHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KTI5|||http://purl.uniprot.org/uniprot/P78549                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  85-fold reduction in activity. Uncouples the glycosylase activity from the lyase activity. Shows glycosylase activity without any detectable AP-lyase activity during the first 10 min of the reaction.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Endonuclease III-like protein 1|||HhH|||HhH-GPD|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||Inactivates enzyme.|||Mitochondrion|||Nucleophile; for N-glycosylase activity|||Phosphoserine|||Polar residues|||Sorted to both nuclei and mitochondria.|||Sorted to the cytoplasm.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102227|||http://purl.uniprot.org/annotation/VAR_016125|||http://purl.uniprot.org/annotation/VAR_016126|||http://purl.uniprot.org/annotation/VAR_016127|||http://purl.uniprot.org/annotation/VAR_016128|||http://purl.uniprot.org/annotation/VAR_029318|||http://purl.uniprot.org/annotation/VSP_054292|||http://purl.uniprot.org/annotation/VSP_054293
http://togogenome.org/gene/9606:KCNJ8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15842                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 8|||Cytoplasmic|||Disordered|||Extracellular|||Found in Brugada syndrome and other J-wave syndromes; unknown pathological significance; the mutant channel displays an increase in glibenclamide-sensitive potassium currents compared to wild type.|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In HTOCD; unknown pathological significance; displays gain of function; displays reduced ATP sensitivity.|||In HTOCD; unknown pathological significance; displays gain of function; increased open state stability, reduced sensitivity to ATP inhibition and increased channel activity; almost completely abolishes high affinity sensitivity to glibenclamide, an inhibitor of ATP-sensitive potassium channels.|||In SIDS; the mutant channel displays reduced potassium currents compared to wild type.|||No effect on channel activity.|||Phosphoserine|||Polar residues|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154947|||http://purl.uniprot.org/annotation/VAR_049670|||http://purl.uniprot.org/annotation/VAR_065225|||http://purl.uniprot.org/annotation/VAR_065878|||http://purl.uniprot.org/annotation/VAR_065879|||http://purl.uniprot.org/annotation/VAR_075226|||http://purl.uniprot.org/annotation/VAR_079518
http://togogenome.org/gene/9606:METTL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUU2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Methyltransferase-like protein 22|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286591|||http://purl.uniprot.org/annotation/VAR_032134|||http://purl.uniprot.org/annotation/VAR_032135|||http://purl.uniprot.org/annotation/VAR_059623|||http://purl.uniprot.org/annotation/VAR_061617|||http://purl.uniprot.org/annotation/VSP_025106|||http://purl.uniprot.org/annotation/VSP_025107|||http://purl.uniprot.org/annotation/VSP_025108
http://togogenome.org/gene/9606:LYPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2G4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Ly6/PLAUR domain-containing protein 1|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226741|||http://purl.uniprot.org/annotation/PRO_0000226742|||http://purl.uniprot.org/annotation/VSP_021583|||http://purl.uniprot.org/annotation/VSP_021584|||http://purl.uniprot.org/annotation/VSP_046981
http://togogenome.org/gene/9606:ANPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15144|||http://purl.uniprot.org/uniprot/Q59E93                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aminopeptidase N|||Aminopeptidase N-like N-terminal|||Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity.|||Cytoplasmic|||Cytosolic Ser/Thr-rich junction|||Disordered|||ERAP1-like C-terminal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Loss of aminopeptidase activity.|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||Necessary and sufficient to mediate interaction with HCoV-229E|||No change in receptor activity and HCoV-229E infection.|||No change of receptor activity and HCoV-229E infection.|||Peptidase M1 membrane alanine aminopeptidase|||Proton acceptor|||Removed|||Sulfotyrosine|||Transition state stabilizer|||Very low receptor activity and HCoV-229E infection.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095081|||http://purl.uniprot.org/annotation/VAR_006727|||http://purl.uniprot.org/annotation/VAR_006728|||http://purl.uniprot.org/annotation/VAR_014736|||http://purl.uniprot.org/annotation/VAR_014737|||http://purl.uniprot.org/annotation/VAR_031262|||http://purl.uniprot.org/annotation/VAR_031263|||http://purl.uniprot.org/annotation/VAR_031264|||http://purl.uniprot.org/annotation/VAR_031265|||http://purl.uniprot.org/annotation/VAR_031266
http://togogenome.org/gene/9606:SIGLEC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Sialic acid-binding Ig-like lectin 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014951|||http://purl.uniprot.org/annotation/VSP_008764
http://togogenome.org/gene/9606:SEZ6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at two sites|||Polar residues|||Pro residues|||Seizure protein 6 homolog|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341346|||http://purl.uniprot.org/annotation/VAR_044048|||http://purl.uniprot.org/annotation/VAR_044049|||http://purl.uniprot.org/annotation/VAR_044050|||http://purl.uniprot.org/annotation/VAR_044051|||http://purl.uniprot.org/annotation/VAR_044052|||http://purl.uniprot.org/annotation/VAR_044053|||http://purl.uniprot.org/annotation/VAR_044054|||http://purl.uniprot.org/annotation/VSP_034250|||http://purl.uniprot.org/annotation/VSP_034251|||http://purl.uniprot.org/annotation/VSP_034252|||http://purl.uniprot.org/annotation/VSP_034253
http://togogenome.org/gene/9606:HTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L0R6P0|||http://purl.uniprot.org/uniprot/P86397                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes ability to complement a htd2-delta mutant yeast.|||Hydroxyacyl-thioester dehydratase type 2, mitochondrial|||MaoC-like|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000390489|||http://purl.uniprot.org/annotation/PRO_5014101210
http://togogenome.org/gene/9606:DPYSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1C7CYX9|||http://purl.uniprot.org/uniprot/Q16555|||http://purl.uniprot.org/uniprot/Q59GB4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amidohydrolase-related|||Asymmetric dimethylarginine|||Dihydropyrimidinase-related protein 2|||Disordered|||Greatly diminishes binding to 3F4 antibody.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1.|||N6-succinyllysine|||No effect.|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Phosphothreonine; by ROCK2|||Phosphotyrosine|||Phosphotyrosine; by FYN|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165913|||http://purl.uniprot.org/annotation/VAR_022016|||http://purl.uniprot.org/annotation/VAR_036316|||http://purl.uniprot.org/annotation/VSP_044941
http://togogenome.org/gene/9606:PACS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In DEE66; increased interaction with SIRT1; increased interaction with HDAC1; increased interaction with TRPV1.|||In isoform 2.|||In isoform 4.|||Phosphofurin acidic cluster sorting protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259511|||http://purl.uniprot.org/annotation/VAR_028947|||http://purl.uniprot.org/annotation/VAR_053798|||http://purl.uniprot.org/annotation/VAR_081137|||http://purl.uniprot.org/annotation/VSP_021409|||http://purl.uniprot.org/annotation/VSP_021410|||http://purl.uniprot.org/annotation/VSP_030294|||http://purl.uniprot.org/annotation/VSP_053815
http://togogenome.org/gene/9606:NIM1K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY84                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Constitutively active.|||Disordered|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||Loss of autophosphorylation and kinase activity.|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase NIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247666|||http://purl.uniprot.org/annotation/VAR_040945|||http://purl.uniprot.org/annotation/VAR_040946|||http://purl.uniprot.org/annotation/VAR_040947|||http://purl.uniprot.org/annotation/VAR_040948|||http://purl.uniprot.org/annotation/VAR_040949|||http://purl.uniprot.org/annotation/VAR_040950
http://togogenome.org/gene/9606:AGMAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSE5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Guanidino acid hydrolase, mitochondrial|||Increased guanidino hydrolase activity toward taurocyamine; can hydrolyze guanidinopropanoate with low efficiency; inactive toward L-arginine.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002089|||http://purl.uniprot.org/annotation/VAR_023485|||http://purl.uniprot.org/annotation/VAR_048332
http://togogenome.org/gene/9606:ARL6IP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75915                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||N-acetylmethionine|||PRA1 family protein 3|||Required for homodimer formation and heterodimer formation with ARL6IP1|||Targeting to endoplasmic reticulum membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220883
http://togogenome.org/gene/9606:SLFN12L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEE8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Schlafen family member 12-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336097|||http://purl.uniprot.org/annotation/VAR_043551|||http://purl.uniprot.org/annotation/VAR_043552|||http://purl.uniprot.org/annotation/VAR_043553|||http://purl.uniprot.org/annotation/VAR_043554|||http://purl.uniprot.org/annotation/VSP_040137
http://togogenome.org/gene/9606:POLR2G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62487                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB7|||Reduces RNA-binding.|||Strongly reduces RNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073986
http://togogenome.org/gene/9606:WRAP73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2S5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein WRAP73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051356|||http://purl.uniprot.org/annotation/VAR_057624|||http://purl.uniprot.org/annotation/VAR_057625
http://togogenome.org/gene/9606:UBA52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62987|||http://purl.uniprot.org/uniprot/Q3MIH3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Site|||Strand                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosylthreonine|||ADP-ribosylglycine|||Abolishes HLTF-mediated polyubiquitination of PCNA.|||Essential for function|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interacts with activating enzyme|||Large ribosomal subunit protein eL40|||Loss of ADP-ribosylation.|||Loss of DTX3L-mediated polyubiquitination of histone H3 and H4.|||N6,N6,N6-trimethyllysine|||No effect on ADP-ribosylation, when associated with K-72.|||No effect on ADP-ribosylation, when associated with K-74.|||No effect on ADP-ribosylation.|||No effect on HLTF-mediated polyubiquitination of PCNA.|||Phosphomimetic mutant that binds and activates PRKN.|||Phosphomimetic mutant that can recruit PRKN to mitochondria.|||Phosphoserine; by PINK1|||Prevents phosphorylation in case of mitophagy. Impaired translocation of PRKN to mitochondria.|||Ubiquitin|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000396433|||http://purl.uniprot.org/annotation/PRO_0000396434
http://togogenome.org/gene/9606:FASN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49327                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyl and malonyl transferases|||Beta-ketoacyl reductase|||C-terminal hotdog fold|||Carrier|||Enoyl reductase|||Fatty acid synthase|||For beta-ketoacyl synthase activity|||For malonyltransferase activity|||For thioesterase activity|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Ketosynthase family 3 (KS3)|||N-acetylmethionine|||N-terminal hotdog fold|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||O-(pantetheine 4'-phosphoryl)serine; alternate|||PKS/mFAS DH|||Phosphoserine|||Phosphoserine; alternate|||Phosphothreonine|||Proton acceptor; for dehydratase activity|||Proton donor; for dehydratase activity|||S-nitrosocysteine|||Thioesterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180276|||http://purl.uniprot.org/annotation/VAR_055479|||http://purl.uniprot.org/annotation/VAR_055480|||http://purl.uniprot.org/annotation/VAR_055481|||http://purl.uniprot.org/annotation/VAR_079534
http://togogenome.org/gene/9606:CDKL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5H1ZRP5|||http://purl.uniprot.org/uniprot/Q00532                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase-like 1|||In isoform 2.|||In isoform 3.|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085810|||http://purl.uniprot.org/annotation/VAR_020576|||http://purl.uniprot.org/annotation/VAR_020577|||http://purl.uniprot.org/annotation/VAR_020578|||http://purl.uniprot.org/annotation/VAR_020579|||http://purl.uniprot.org/annotation/VSP_041239|||http://purl.uniprot.org/annotation/VSP_041240|||http://purl.uniprot.org/annotation/VSP_041241|||http://purl.uniprot.org/annotation/VSP_041242|||http://purl.uniprot.org/annotation/VSP_059391|||http://purl.uniprot.org/annotation/VSP_059392
http://togogenome.org/gene/9606:MRGPRX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB1                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member X2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069775|||http://purl.uniprot.org/annotation/VAR_019433|||http://purl.uniprot.org/annotation/VAR_024739|||http://purl.uniprot.org/annotation/VAR_024740|||http://purl.uniprot.org/annotation/VAR_049418
http://togogenome.org/gene/9606:DAZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJH5|||http://purl.uniprot.org/uniprot/Q9NQZ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DAZ|||DAZ 1|||DAZ 2|||DAZ 3|||DAZ 4|||DAZ 5|||DAZ 6|||DAZ 7|||DAZ 8|||DAZ 9|||Deleted in azoospermia protein 1|||Disordered|||In isoform 2.|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081554|||http://purl.uniprot.org/annotation/VSP_056239|||http://purl.uniprot.org/annotation/VSP_056240
http://togogenome.org/gene/9606:EEF1AKMT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AZ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EEF1A lysine methyltransferase 3|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291850|||http://purl.uniprot.org/annotation/VAR_032869|||http://purl.uniprot.org/annotation/VSP_026268|||http://purl.uniprot.org/annotation/VSP_026269|||http://purl.uniprot.org/annotation/VSP_026270|||http://purl.uniprot.org/annotation/VSP_026271
http://togogenome.org/gene/9606:TMED5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3A6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GOLD|||Helical|||In isoform 2.|||Lumenal|||Transmembrane emp24 domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010389|||http://purl.uniprot.org/annotation/VAR_017150|||http://purl.uniprot.org/annotation/VSP_046365
http://togogenome.org/gene/9606:TEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WV5                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  2-fold reduction in binding affinity for STN1.|||2.5-fold reduction in binding affinity for STN1.|||CST complex subunit TEN1|||OB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334683
http://togogenome.org/gene/9606:GOLGA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPI8|||http://purl.uniprot.org/uniprot/A0A8V8TQI6|||http://purl.uniprot.org/uniprot/A0A9L9PX25|||http://purl.uniprot.org/uniprot/C9J0Y3|||http://purl.uniprot.org/uniprot/Q13439|||http://purl.uniprot.org/uniprot/Q49A56                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes Golgi localization.|||Basic and acidic residues|||Disordered|||GRIP|||Golgin subfamily A member 4|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with MACF1|||Loss of TBC1D23-binding.|||Loss of localization at the Golgi apparatus.|||Loss of localization at the Golgi apparatus. Loss of ARL1-binding.|||N-linked (GlcNAc...) asparagine|||No effect on localization at the Golgi apparatus.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190059|||http://purl.uniprot.org/annotation/VAR_033975|||http://purl.uniprot.org/annotation/VAR_033976|||http://purl.uniprot.org/annotation/VAR_049258|||http://purl.uniprot.org/annotation/VSP_004274|||http://purl.uniprot.org/annotation/VSP_004275|||http://purl.uniprot.org/annotation/VSP_044819
http://togogenome.org/gene/9606:RAPGEF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MQ07|||http://purl.uniprot.org/uniprot/Q5JPD2|||http://purl.uniprot.org/uniprot/Q92565                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||N-terminal Ras-GEF|||Rap guanine nucleotide exchange factor 5|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068873|||http://purl.uniprot.org/annotation/PRO_5002724124|||http://purl.uniprot.org/annotation/PRO_5004258017|||http://purl.uniprot.org/annotation/VSP_007616
http://togogenome.org/gene/9606:NPIPA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJI5|||http://purl.uniprot.org/uniprot/P0DM63                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Nuclear pore complex-interacting protein family member A7|||Nuclear pore complex-interacting protein family member A8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423919|||http://purl.uniprot.org/annotation/PRO_0000423925
http://togogenome.org/gene/9606:NOP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPE3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  H/ACA ribonucleoprotein complex subunit 3|||In DKCB1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149001|||http://purl.uniprot.org/annotation/VAR_043725
http://togogenome.org/gene/9606:ST13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA6|||http://purl.uniprot.org/uniprot/B4E0U6|||http://purl.uniprot.org/uniprot/P50502|||http://purl.uniprot.org/uniprot/Q0IJ56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hsc70-interacting protein|||Hsp70-interacting protein N-terminal|||N6-acetyllysine|||Phosphoserine; by GRK5|||STI1|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190811|||http://purl.uniprot.org/annotation/VAR_011900
http://togogenome.org/gene/9606:COCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3TZE7|||http://purl.uniprot.org/uniprot/O43405                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cochlin|||Disordered|||In DFNA9.|||In DFNA9; affects protein deposition to the extracellular matrix.|||In DFNA9; does not affect protein deposition to the extracellular matrix.|||In DFNA9; induces disulfide bond dimer formation; keeps dimer in the cell and reduces secretion; monomeric and/or homodimeric mutant forms do not prevent interaction with type II collagen.|||In DFNA9; some families may manifest Meniere disease-like symptoms; does not affect protein deposition to the extracellular matrix.|||In DFNB110.|||In isoform 2.|||LCCL|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020968|||http://purl.uniprot.org/annotation/PRO_5015780790|||http://purl.uniprot.org/annotation/VAR_008532|||http://purl.uniprot.org/annotation/VAR_008533|||http://purl.uniprot.org/annotation/VAR_008534|||http://purl.uniprot.org/annotation/VAR_008535|||http://purl.uniprot.org/annotation/VAR_008536|||http://purl.uniprot.org/annotation/VAR_011925|||http://purl.uniprot.org/annotation/VAR_011926|||http://purl.uniprot.org/annotation/VAR_017175|||http://purl.uniprot.org/annotation/VAR_022259|||http://purl.uniprot.org/annotation/VAR_022260|||http://purl.uniprot.org/annotation/VAR_022261|||http://purl.uniprot.org/annotation/VAR_050896|||http://purl.uniprot.org/annotation/VAR_070034|||http://purl.uniprot.org/annotation/VAR_072249|||http://purl.uniprot.org/annotation/VAR_072250|||http://purl.uniprot.org/annotation/VAR_072251|||http://purl.uniprot.org/annotation/VAR_072252|||http://purl.uniprot.org/annotation/VAR_072253|||http://purl.uniprot.org/annotation/VAR_072254|||http://purl.uniprot.org/annotation/VAR_079876|||http://purl.uniprot.org/annotation/VAR_081173|||http://purl.uniprot.org/annotation/VSP_056538
http://togogenome.org/gene/9606:ALKBH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KRA9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6|||Basic and acidic residues|||Disordered|||Fe2OG dioxygenase|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323716|||http://purl.uniprot.org/annotation/VSP_032056|||http://purl.uniprot.org/annotation/VSP_032057
http://togogenome.org/gene/9606:JAML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUI3|||http://purl.uniprot.org/uniprot/Q496M4|||http://purl.uniprot.org/uniprot/Q86YT9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||Immunoglobulin V-set|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Junctional adhesion molecule-like|||Loss of the ability to homodimerize, loss of interaction with CXADR and loss of function in cell-cell adhesion.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015074|||http://purl.uniprot.org/annotation/VAR_049974|||http://purl.uniprot.org/annotation/VAR_049975|||http://purl.uniprot.org/annotation/VAR_049976|||http://purl.uniprot.org/annotation/VSP_014830|||http://purl.uniprot.org/annotation/VSP_014831|||http://purl.uniprot.org/annotation/VSP_014832|||http://purl.uniprot.org/annotation/VSP_054911
http://togogenome.org/gene/9606:MAP4K4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3V5|||http://purl.uniprot.org/uniprot/E7EN19|||http://purl.uniprot.org/uniprot/O95819|||http://purl.uniprot.org/uniprot/V9HWH3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In isoform 2, isoform 3 and isoform 6.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||Mediates interaction with RAP2A|||Mitogen-activated protein kinase kinase kinase kinase 4|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086280|||http://purl.uniprot.org/annotation/VAR_040746|||http://purl.uniprot.org/annotation/VAR_082893|||http://purl.uniprot.org/annotation/VSP_007054|||http://purl.uniprot.org/annotation/VSP_007055|||http://purl.uniprot.org/annotation/VSP_007056|||http://purl.uniprot.org/annotation/VSP_007057|||http://purl.uniprot.org/annotation/VSP_007058|||http://purl.uniprot.org/annotation/VSP_058855|||http://purl.uniprot.org/annotation/VSP_058856
http://togogenome.org/gene/9606:LIG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49916                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ligase activity with blunt-ended DNA, but not with nicked DNA.|||BRCT|||DNA ligase 3|||Disordered|||In MTDPS20.|||In MTDPS20; may affect exon 9 splicing; decreased interaction with POLG; does not rescue cerebellar defects in a LIG3 deficiency zebrafish model.|||In MTDPS20; severely decreased protein levels.|||In MTDPS20; severely decreased protein levels; does not rescue cerebellar defects in a LIG3 deficiency zebrafish model.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interaction with DNA|||Mitochondrion|||N6-AMP-lysine intermediate|||Nearly abolishes ligase activity with blunt-ended DNA, but not with nicked DNA.|||PARP-type|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059574|||http://purl.uniprot.org/annotation/VAR_018807|||http://purl.uniprot.org/annotation/VAR_020196|||http://purl.uniprot.org/annotation/VAR_020197|||http://purl.uniprot.org/annotation/VAR_021938|||http://purl.uniprot.org/annotation/VAR_036513|||http://purl.uniprot.org/annotation/VAR_072387|||http://purl.uniprot.org/annotation/VAR_087020|||http://purl.uniprot.org/annotation/VAR_087021|||http://purl.uniprot.org/annotation/VAR_087022|||http://purl.uniprot.org/annotation/VAR_087023|||http://purl.uniprot.org/annotation/VAR_087024|||http://purl.uniprot.org/annotation/VAR_087025|||http://purl.uniprot.org/annotation/VAR_087026|||http://purl.uniprot.org/annotation/VSP_001302|||http://purl.uniprot.org/annotation/VSP_057464
http://togogenome.org/gene/9606:FOXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15353                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Does not affect transcriptional activity as shown by a transcriptional reporter assay.|||Fork-head|||Forkhead box protein N1|||In TIDAND and TLIND.|||In TIDAND and TLIND; severely reduced transcriptional activity as shown by a transcriptional reporter assay.|||In TIDTA; decreased transcriptional activity as shown by a transcriptional reporter assay.|||In TLIND.|||In TLIND; unknown pathological significance.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091866|||http://purl.uniprot.org/annotation/VAR_010376|||http://purl.uniprot.org/annotation/VAR_020025|||http://purl.uniprot.org/annotation/VAR_020026|||http://purl.uniprot.org/annotation/VAR_021843|||http://purl.uniprot.org/annotation/VAR_083857|||http://purl.uniprot.org/annotation/VAR_083858|||http://purl.uniprot.org/annotation/VAR_083859|||http://purl.uniprot.org/annotation/VAR_083860|||http://purl.uniprot.org/annotation/VAR_083861|||http://purl.uniprot.org/annotation/VAR_083862|||http://purl.uniprot.org/annotation/VAR_083863|||http://purl.uniprot.org/annotation/VAR_083864|||http://purl.uniprot.org/annotation/VAR_083865
http://togogenome.org/gene/9606:SGMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHU3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes enzyme activity by about 70%. No change in subcellular location.|||Basic and acidic residues|||Completely abolishes enzyme activity. No change in subcellular location.|||Cytoplasmic|||Disordered|||Helical|||In CDL; loss of enzymatic activity; does not localize to plasma membrane.|||In CDLSMD; unknown pathological significance; no effect on enzymatic activity; does not localize to plasma membrane; accumulates in the endoplasmic reticulum.|||Little effect on palmitoylation; when associated with A-343 or A-348. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with A-343 and A-348.|||Phosphatidylcholine:ceramide cholinephosphotransferase 2|||S-palmitoyl cysteine|||Strongly decreases palmitoylation; when associated with A-343. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with 331-A-A-332 and A-343.|||Strongly decreases palmitoylation; when associated with A-348. Abolishes palmitoylation and dramatically reduces plasma membrane localization; when associated with 331-A-A-332 and A-348.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221072|||http://purl.uniprot.org/annotation/VAR_052025|||http://purl.uniprot.org/annotation/VAR_082674|||http://purl.uniprot.org/annotation/VAR_082675|||http://purl.uniprot.org/annotation/VAR_082676
http://togogenome.org/gene/9606:PDZRN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGD1|||http://purl.uniprot.org/uniprot/Q6ZMN7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 4.|||PDZ|||PDZ 1|||PDZ 2|||PDZ domain-containing RING finger protein 4|||Polar residues|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055920|||http://purl.uniprot.org/annotation/VAR_020966|||http://purl.uniprot.org/annotation/VAR_035951|||http://purl.uniprot.org/annotation/VSP_012611|||http://purl.uniprot.org/annotation/VSP_012612|||http://purl.uniprot.org/annotation/VSP_012614|||http://purl.uniprot.org/annotation/VSP_012615
http://togogenome.org/gene/9606:LONP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EN44|||http://purl.uniprot.org/uniprot/Q86WA8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Lon N-terminal|||Lon protease homolog 2, peroxisomal|||Lon proteolytic|||Loss of peroxisomal localization.|||Microbody targeting signal|||N-acetylserine|||Reduces degradation of self-processed forms of TYSND1. Loss of ACOX1-processing.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287640|||http://purl.uniprot.org/annotation/VSP_056190
http://togogenome.org/gene/9606:PRAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 12 AA repeats of K-P-P-[PQ]-P-[EQ]-[VAF]-T-D-L-P-K|||Basic and acidic residues|||Disordered|||PML-RARA-regulated adapter molecule 1|||Phosphoserine|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270171|||http://purl.uniprot.org/annotation/VAR_029808|||http://purl.uniprot.org/annotation/VAR_029809|||http://purl.uniprot.org/annotation/VAR_029810|||http://purl.uniprot.org/annotation/VAR_061692
http://togogenome.org/gene/9606:PPM1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75688                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform Beta-2, isoform 4 and isoform 5.|||In isoform Beta-2.|||In isoform Beta-X.|||N-myristoyl glycine|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Protein phosphatase 1B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057746|||http://purl.uniprot.org/annotation/VSP_005087|||http://purl.uniprot.org/annotation/VSP_005088|||http://purl.uniprot.org/annotation/VSP_041085|||http://purl.uniprot.org/annotation/VSP_043641|||http://purl.uniprot.org/annotation/VSP_043642|||http://purl.uniprot.org/annotation/VSP_043643|||http://purl.uniprot.org/annotation/VSP_043644
http://togogenome.org/gene/9606:C5orf46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWT4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Uncharacterized protein C5orf46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317636|||http://purl.uniprot.org/annotation/VAR_056787|||http://purl.uniprot.org/annotation/VSP_031115
http://togogenome.org/gene/9606:BEND4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU67                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  BEN|||BEN domain-containing protein 4|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076190|||http://purl.uniprot.org/annotation/VSP_016488|||http://purl.uniprot.org/annotation/VSP_016489|||http://purl.uniprot.org/annotation/VSP_016490|||http://purl.uniprot.org/annotation/VSP_016491|||http://purl.uniprot.org/annotation/VSP_016492|||http://purl.uniprot.org/annotation/VSP_016493|||http://purl.uniprot.org/annotation/VSP_036338
http://togogenome.org/gene/9606:SP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02086                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcription factor Sp2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047140|||http://purl.uniprot.org/annotation/VSP_022021
http://togogenome.org/gene/9606:PRKCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24723                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Associated with susceptibility to ischemic stroke; increases autophosphorylation and kinase activity.|||C2|||Disordered|||In a aLLTEL/AML1+ sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Protein kinase|||Protein kinase C eta type|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055705|||http://purl.uniprot.org/annotation/VAR_034604|||http://purl.uniprot.org/annotation/VAR_042312|||http://purl.uniprot.org/annotation/VAR_042313|||http://purl.uniprot.org/annotation/VAR_042314|||http://purl.uniprot.org/annotation/VAR_042315|||http://purl.uniprot.org/annotation/VAR_042316|||http://purl.uniprot.org/annotation/VAR_042317|||http://purl.uniprot.org/annotation/VAR_042318|||http://purl.uniprot.org/annotation/VAR_042438|||http://purl.uniprot.org/annotation/VAR_060736|||http://purl.uniprot.org/annotation/VSP_056572
http://togogenome.org/gene/9606:GUCY1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU69|||http://purl.uniprot.org/uniprot/Q02108                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Guanylate cyclase|||Guanylate cyclase soluble subunit alpha-1|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074110|||http://purl.uniprot.org/annotation/VAR_049257|||http://purl.uniprot.org/annotation/VSP_045477
http://togogenome.org/gene/9606:GTF2H5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZYL4                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  General transcription factor IIH subunit 5|||In TTD3.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119256|||http://purl.uniprot.org/annotation/VAR_022647
http://togogenome.org/gene/9606:DAB2IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWQ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form KMT2A/MLL1-DAB2IP|||C2|||Disabled homolog 2-interacting protein|||Disordered|||Does not inhibit interaction with MAP3K5. Does not reduce GSK3B-induced beta-catenin transcription activity, TNF-alpha-induced apoptosis, ARF6-mediated TLR4-TIRAP-MyD88 signaling inhibition, Ras and NF-kappa-B activities and tumor development. Does not suppress tumor development; when associated with A-728.|||Does not reduce interaction with 14-3-3 proteins.|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||Inhibits phosphorylation and TNF-alpha-induced MAP3K5 dephosphorylation. Reduces interaction with 14-3-3 proteins, AKT1, a regulatory p85 subunit, MAP3K5, RIPK1, TRAF2 and TNF-alpha-induced MAP3K5-JNK signaling and apoptosis. Reduces RAS activity. Does not reduce GSK3B-induced beta catenin-mediated transcription activity. Does not reduce NF-kappa-B activity, cell invasion, epithelial-to-mesenchymal transition (EMT) and tumor development. Does not suppress tumor development; when associated with R-413.|||Necessary for interaction with AKT1|||PH|||Phosphoserine|||Phosphoserine; by MAP3K5 and RIPK1|||Polar residues|||Pro residues|||Ras-GAP|||Reduces interaction with KDR/VEGFR2. Does not inhibit interaction with MAP3K5.|||Reduces interaction with a regulatory p85 subunit of the PI3K complex. Inhibits MAP3K5 active form increase, AKT1 active form decrease, PI3K-p85 complex activity inhibition and TNF-induced apoptosis.|||Significantly reduces interaction with MAP3K5. Does not reduce interaction with KDR/VEGFR2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252407|||http://purl.uniprot.org/annotation/VAR_056858|||http://purl.uniprot.org/annotation/VSP_020952|||http://purl.uniprot.org/annotation/VSP_020953|||http://purl.uniprot.org/annotation/VSP_020954|||http://purl.uniprot.org/annotation/VSP_047361
http://togogenome.org/gene/9606:PROP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JQ02|||http://purl.uniprot.org/uniprot/O75360                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein prophet of Pit-1|||In CPHD2.|||In CPHD2; displays a significant decrease in DNA binding on a paired-box response element (PRDQ9) and trans-activation of a luciferase reporter gene.|||In CPHD2; familial.|||In CPHD2; familial; no detectable DNA binding observed with the mutant protein in electromobility shift assays; whereas in vitro translated PROP1 and the mutant proteins were similar in their expression and electrophoretic properties.|||In CPHD2; impairs binding of the mutated protein to DNA target sequences.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049271|||http://purl.uniprot.org/annotation/VAR_003768|||http://purl.uniprot.org/annotation/VAR_003769|||http://purl.uniprot.org/annotation/VAR_003770|||http://purl.uniprot.org/annotation/VAR_012746|||http://purl.uniprot.org/annotation/VAR_014531|||http://purl.uniprot.org/annotation/VAR_054972|||http://purl.uniprot.org/annotation/VAR_054973|||http://purl.uniprot.org/annotation/VAR_063235|||http://purl.uniprot.org/annotation/VAR_063236
http://togogenome.org/gene/9606:MYLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32MK0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Myosin light chain kinase 3|||Phosphoserine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272200|||http://purl.uniprot.org/annotation/VAR_035630|||http://purl.uniprot.org/annotation/VAR_058335|||http://purl.uniprot.org/annotation/VAR_058336|||http://purl.uniprot.org/annotation/VSP_044312
http://togogenome.org/gene/9606:ZCCHC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYQ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||Zinc finger CCHC domain-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150975|||http://purl.uniprot.org/annotation/VAR_024703|||http://purl.uniprot.org/annotation/VAR_036492|||http://purl.uniprot.org/annotation/VAR_053754|||http://purl.uniprot.org/annotation/VAR_053755|||http://purl.uniprot.org/annotation/VSP_013843
http://togogenome.org/gene/9606:WDR35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2L0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CED2.|||In SRTD7 and SRTD7/20; the SRTD7/20 patient also carries variant INTU 276-Q--L-942 del; chondrocyte cell lines from a patient show a reduction of cilia indicating a defect in ciliogenesis.|||In SRTD7.|||In SRTD7; chondrocyte cell lines from the patient show a reduction of cilia indicating a defect in ciliogenesis.|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051384|||http://purl.uniprot.org/annotation/VAR_053428|||http://purl.uniprot.org/annotation/VAR_053429|||http://purl.uniprot.org/annotation/VAR_062102|||http://purl.uniprot.org/annotation/VAR_062103|||http://purl.uniprot.org/annotation/VAR_064581|||http://purl.uniprot.org/annotation/VAR_064582|||http://purl.uniprot.org/annotation/VAR_065955|||http://purl.uniprot.org/annotation/VAR_076784|||http://purl.uniprot.org/annotation/VAR_080632|||http://purl.uniprot.org/annotation/VAR_080633|||http://purl.uniprot.org/annotation/VSP_009732
http://togogenome.org/gene/9606:UBE2V2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0M8W4|||http://purl.uniprot.org/uniprot/Q15819                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 variant 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082602|||http://purl.uniprot.org/annotation/VAR_052431|||http://purl.uniprot.org/annotation/VAR_052433
http://togogenome.org/gene/9606:NRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9V7|||http://purl.uniprot.org/uniprot/O14786|||http://purl.uniprot.org/uniprot/Q59F20|||http://purl.uniprot.org/uniprot/Q68DN3|||http://purl.uniprot.org/uniprot/Q6AWA9|||http://purl.uniprot.org/uniprot/Q6X907                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||F5/8 type C|||F5/8 type C 1|||F5/8 type C 2|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||MAM|||N-linked (GlcNAc...) asparagine|||Neuropilin|||Neuropilin-1|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (chondroitin sulfate) serine; alternate|||O-linked (Xyl...) (heparan sulfate) serine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021859|||http://purl.uniprot.org/annotation/PRO_5002722238|||http://purl.uniprot.org/annotation/PRO_5004269541|||http://purl.uniprot.org/annotation/PRO_5004270632|||http://purl.uniprot.org/annotation/PRO_5004282614|||http://purl.uniprot.org/annotation/VAR_046536|||http://purl.uniprot.org/annotation/VAR_046537|||http://purl.uniprot.org/annotation/VAR_056957|||http://purl.uniprot.org/annotation/VSP_004339|||http://purl.uniprot.org/annotation/VSP_004340|||http://purl.uniprot.org/annotation/VSP_053498
http://togogenome.org/gene/9606:GJA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654ICQ6|||http://purl.uniprot.org/uniprot/Q969M2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-10 protein|||Gap junction protein cysteine-rich|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312989
http://togogenome.org/gene/9606:INKA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Inka box 1|||Inka box 2|||PAK4-inhibitor INKA1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239717
http://togogenome.org/gene/9606:EIF4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14240                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEAD box|||Disordered|||Eukaryotic initiation factor 4A-II|||Helicase ATP-binding|||Helicase C-terminal|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphothreonine|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054938|||http://purl.uniprot.org/annotation/VAR_035838|||http://purl.uniprot.org/annotation/VAR_052158|||http://purl.uniprot.org/annotation/VSP_009629
http://togogenome.org/gene/9606:PELP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEX7|||http://purl.uniprot.org/uniprot/B4DR36|||http://purl.uniprot.org/uniprot/C9JFV4|||http://purl.uniprot.org/uniprot/E7EV54|||http://purl.uniprot.org/uniprot/Q8IZL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||LXXLL motif 1|||LXXLL motif 10|||LXXLL motif 11|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||LXXLL motif 5|||LXXLL motif 6|||LXXLL motif 7|||LXXLL motif 8|||LXXLL motif 9|||N-acetylalanine|||Not sumoylated.|||PELP1 middle|||Phosphoserine|||Phosphothreonine|||Pre-rRNA-processing protein RIX1 N-terminal|||Pro residues|||Proline-, glutamic acid- and leucine-rich protein 1|||Removed|||Required for modulation of ESR1 transcriptional activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252135|||http://purl.uniprot.org/annotation/VAR_027766
http://togogenome.org/gene/9606:CEACAM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40198                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation and 30% reduction in bacterial uptake. More than 60% reduction in bacterial uptake and loss of RAC1 stimulation; when associated with F-230.|||Loss of phosphorylation and 30% reduction in bacterial uptake. More than 60% reduction in bacterial uptake and loss of RAC1 stimulation; when associated with F-241.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014565|||http://purl.uniprot.org/annotation/VAR_003905|||http://purl.uniprot.org/annotation/VSP_002486|||http://purl.uniprot.org/annotation/VSP_002487
http://togogenome.org/gene/9606:ATP6AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MQW4|||http://purl.uniprot.org/uniprot/Q15904                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by furin|||Cytoplasmic|||Helical|||In IMD47.|||In IMD47; probable loss of proton-transporting V-type ATPase complex assembly in yeast; unable to restore V-ATPase-dependent growth in Voa1 mutant yeast.|||In IMD47; restores V-ATPase-dependent growth in Voa1 mutant yeast.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Retained in the endoplasmic reticulum when transfected into yeast cells. Restores V-ATPase-dependent growth in Voa1 mutant yeast.|||V-type proton ATPase subunit S1|||V-type proton ATPase subunit S1 luminal|||V-type proton ATPase subunit S1/VOA1 transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002543|||http://purl.uniprot.org/annotation/PRO_0000454041|||http://purl.uniprot.org/annotation/PRO_5017442004|||http://purl.uniprot.org/annotation/VAR_077021|||http://purl.uniprot.org/annotation/VAR_077022|||http://purl.uniprot.org/annotation/VAR_077023|||http://purl.uniprot.org/annotation/VAR_077024
http://togogenome.org/gene/9606:RHEBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAI7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active.|||Cysteine methyl ester|||Effector region|||GTPase RhebL1|||In isoform 2.|||Partially deficient in guanine nucleotide binding.|||Partially impaired in RPS6K1 activation.|||Removed in mature form|||S-farnesyl cysteine|||Significant decrease in NF-kappa B activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324292|||http://purl.uniprot.org/annotation/PRO_0000324293|||http://purl.uniprot.org/annotation/VSP_040851|||http://purl.uniprot.org/annotation/VSP_040852
http://togogenome.org/gene/9606:AAMDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7C9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||MTH138-like domain|||Mth938 domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239814|||http://purl.uniprot.org/annotation/VAR_052696|||http://purl.uniprot.org/annotation/VSP_019266|||http://purl.uniprot.org/annotation/VSP_019267|||http://purl.uniprot.org/annotation/VSP_019268|||http://purl.uniprot.org/annotation/VSP_019269
http://togogenome.org/gene/9606:OCM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CE71                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Putative oncomodulin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392643
http://togogenome.org/gene/9606:USP17L21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6R901                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421095
http://togogenome.org/gene/9606:MT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47944                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  Metallothionein-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197255|||http://purl.uniprot.org/annotation/VAR_034110|||http://purl.uniprot.org/annotation/VAR_034111|||http://purl.uniprot.org/annotation/VAR_034112
http://togogenome.org/gene/9606:ZNF148                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Zinc finger protein 148                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047427|||http://purl.uniprot.org/annotation/VSP_055938|||http://purl.uniprot.org/annotation/VSP_055939
http://togogenome.org/gene/9606:C16orf90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C16orf90                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343581
http://togogenome.org/gene/9606:CS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75390                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Citrate synthase, mitochondrial|||Does not inhibit methylation.|||Inhibits methylation.|||Mitochondrion|||N6,N6,N6-trimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005471
http://togogenome.org/gene/9606:RUNX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13761                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Runt|||Runt-related transcription factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174662|||http://purl.uniprot.org/annotation/VSP_005949
http://togogenome.org/gene/9606:APPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEU8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BAR|||Breakpoint for chromosomal translocation|||DCC-interacting protein 13-beta|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||PID|||Required for RAB5A binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079987|||http://purl.uniprot.org/annotation/VAR_021505|||http://purl.uniprot.org/annotation/VSP_044771|||http://purl.uniprot.org/annotation/VSP_044772
http://togogenome.org/gene/9606:MZB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU39                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Motif|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Does not affect activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Marginal zone B- and B1-cell-specific protein|||No significant activity.|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318740|||http://purl.uniprot.org/annotation/VSP_031280|||http://purl.uniprot.org/annotation/VSP_031281|||http://purl.uniprot.org/annotation/VSP_038332|||http://purl.uniprot.org/annotation/VSP_038333|||http://purl.uniprot.org/annotation/VSP_038334|||http://purl.uniprot.org/annotation/VSP_039073|||http://purl.uniprot.org/annotation/VSP_039074
http://togogenome.org/gene/9606:MRPS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIP9|||http://purl.uniprot.org/uniprot/P82675                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||S5 DRBM|||Small ribosomal subunit protein uS5m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131685|||http://purl.uniprot.org/annotation/VSP_005725|||http://purl.uniprot.org/annotation/VSP_005726
http://togogenome.org/gene/9606:STARD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59095                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  START|||StAR-related lipid transfer protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220672|||http://purl.uniprot.org/annotation/VAR_024651
http://togogenome.org/gene/9606:LRRC61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 61                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236796|||http://purl.uniprot.org/annotation/VAR_051123
http://togogenome.org/gene/9606:PTPRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD43                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Helical|||In isoform 2.|||In isoform 3.|||Loss of activity. Acts as a dominant negative mutant.|||Loss of activity. No induction of apoptosis.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase H|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318950|||http://purl.uniprot.org/annotation/VAR_038918|||http://purl.uniprot.org/annotation/VAR_038919|||http://purl.uniprot.org/annotation/VAR_038920|||http://purl.uniprot.org/annotation/VAR_038921|||http://purl.uniprot.org/annotation/VAR_038922|||http://purl.uniprot.org/annotation/VAR_061762|||http://purl.uniprot.org/annotation/VAR_061763|||http://purl.uniprot.org/annotation/VAR_061764|||http://purl.uniprot.org/annotation/VSP_031318|||http://purl.uniprot.org/annotation/VSP_054222
http://togogenome.org/gene/9606:ACKR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPB9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Atypical chemokine receptor 4|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069296
http://togogenome.org/gene/9606:MYO19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E218|||http://purl.uniprot.org/uniprot/B7Z1T7|||http://purl.uniprot.org/uniprot/Q96H55                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes localization to mitochondrion outer membrane.|||Actin-binding|||Does not affect localization to mitochondrion outer membrane.|||IQ 1|||IQ 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MyMOMA region|||Myosin motor|||Phosphoserine|||Rigor-like phenotype due to disruption of ATP-binding. Does not affect localization to mitochondrion.|||Unconventional myosin-XIX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332969|||http://purl.uniprot.org/annotation/VAR_043018|||http://purl.uniprot.org/annotation/VAR_043019|||http://purl.uniprot.org/annotation/VAR_043020|||http://purl.uniprot.org/annotation/VSP_033402|||http://purl.uniprot.org/annotation/VSP_033403|||http://purl.uniprot.org/annotation/VSP_033404|||http://purl.uniprot.org/annotation/VSP_033405|||http://purl.uniprot.org/annotation/VSP_033406
http://togogenome.org/gene/9606:ARG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78540                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Arginase-2, mitochondrial|||Disordered|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002084|||http://purl.uniprot.org/annotation/VAR_033520
http://togogenome.org/gene/9606:MAGI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4H4|||http://purl.uniprot.org/uniprot/Q86UL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 2.|||Interaction with DDN|||Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094586|||http://purl.uniprot.org/annotation/VSP_008435
http://togogenome.org/gene/9606:SVOPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N434                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Putative transporter SVOPL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294461|||http://purl.uniprot.org/annotation/VAR_033188|||http://purl.uniprot.org/annotation/VSP_026651|||http://purl.uniprot.org/annotation/VSP_026652
http://togogenome.org/gene/9606:SAGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Sarcoma antigen 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286971|||http://purl.uniprot.org/annotation/VAR_032243|||http://purl.uniprot.org/annotation/VAR_032244
http://togogenome.org/gene/9606:ASIC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KPF5|||http://purl.uniprot.org/uniprot/Q96FT7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acid-sensing ion channel 4|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on channel function.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181304|||http://purl.uniprot.org/annotation/VAR_052038|||http://purl.uniprot.org/annotation/VAR_052039|||http://purl.uniprot.org/annotation/VAR_059806|||http://purl.uniprot.org/annotation/VSP_061443|||http://purl.uniprot.org/annotation/VSP_061444|||http://purl.uniprot.org/annotation/VSP_061445
http://togogenome.org/gene/9606:TMEM102                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9M5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Transmembrane protein 102                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263648|||http://purl.uniprot.org/annotation/VAR_029595
http://togogenome.org/gene/9606:BPY2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14599                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Testis-specific basic protein Y 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184664
http://togogenome.org/gene/9606:RPP38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78345                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Removed|||Ribonuclease P protein subunit p38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136783|||http://purl.uniprot.org/annotation/VAR_023960|||http://purl.uniprot.org/annotation/VAR_023961|||http://purl.uniprot.org/annotation/VAR_023962|||http://purl.uniprot.org/annotation/VAR_029298|||http://purl.uniprot.org/annotation/VAR_051811|||http://purl.uniprot.org/annotation/VAR_051812|||http://purl.uniprot.org/annotation/VAR_051813
http://togogenome.org/gene/9606:AATK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C175|||http://purl.uniprot.org/uniprot/Q6ZMQ8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||In a lung adenocarcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LMTK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248300|||http://purl.uniprot.org/annotation/VAR_027267|||http://purl.uniprot.org/annotation/VAR_032679|||http://purl.uniprot.org/annotation/VAR_032680|||http://purl.uniprot.org/annotation/VAR_032681|||http://purl.uniprot.org/annotation/VAR_032682|||http://purl.uniprot.org/annotation/VAR_032683|||http://purl.uniprot.org/annotation/VAR_032684|||http://purl.uniprot.org/annotation/VAR_032685|||http://purl.uniprot.org/annotation/VAR_032686|||http://purl.uniprot.org/annotation/VAR_032687|||http://purl.uniprot.org/annotation/VAR_032688|||http://purl.uniprot.org/annotation/VSP_020225|||http://purl.uniprot.org/annotation/VSP_020226|||http://purl.uniprot.org/annotation/VSP_020227|||http://purl.uniprot.org/annotation/VSP_020228
http://togogenome.org/gene/9606:C14orf93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFZ6|||http://purl.uniprot.org/uniprot/Q9H972                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Uncharacterized protein C14orf93                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020950|||http://purl.uniprot.org/annotation/VAR_050875|||http://purl.uniprot.org/annotation/VSP_007850
http://togogenome.org/gene/9606:LPCAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q643R3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||HXXXXD motif|||Helical|||Lysophospholipid acyltransferase LPCAT4|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247054
http://togogenome.org/gene/9606:GARIN1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NXP2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Golgi-associated RAB2 interactor protein 1A|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311689|||http://purl.uniprot.org/annotation/VAR_037267|||http://purl.uniprot.org/annotation/VAR_037268|||http://purl.uniprot.org/annotation/VAR_037269|||http://purl.uniprot.org/annotation/VAR_037270|||http://purl.uniprot.org/annotation/VSP_029581
http://togogenome.org/gene/9606:PRAMEF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXH5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156981
http://togogenome.org/gene/9606:AKIRIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9L7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Akirin-1|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||SYVS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274318|||http://purl.uniprot.org/annotation/VSP_042769
http://togogenome.org/gene/9606:RPS6KB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23443                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Acidic residues|||Autoinhibitory domain|||Basic and acidic residues|||Disordered|||Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-441 and E-444.|||Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-441 and E-447.|||Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-444 and E-447.|||Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-441; E-444 and E-447.|||Greatly reduces activity. Greatly reduces phosphorylation at T-412 and moderately reduces phosphorylation at T-252.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform Alpha II.|||Loss of activity. Loss of phosphorylation at T-412.|||Mimics phosphorylation. Facilitates phosphorylation of T-252 by PDPK1; when associated with E-434; E-441; E-444 and E-447. Mimics phosphorylation. No effect on interaction with PDPK1 and phosphorylation of T-252. Impairs association with the eIF3 complex.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MTOR, NEK6 and NEK7|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||Ribosomal protein S6 kinase beta-1|||TOS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024342|||http://purl.uniprot.org/annotation/VAR_035628|||http://purl.uniprot.org/annotation/VAR_040639|||http://purl.uniprot.org/annotation/VAR_040640|||http://purl.uniprot.org/annotation/VAR_040641|||http://purl.uniprot.org/annotation/VAR_040642|||http://purl.uniprot.org/annotation/VSP_018839|||http://purl.uniprot.org/annotation/VSP_054613|||http://purl.uniprot.org/annotation/VSP_054614|||http://purl.uniprot.org/annotation/VSP_055026
http://togogenome.org/gene/9606:HIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK46|||http://purl.uniprot.org/uniprot/O00291                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes 3-phosphoinositide-binding; when associated with E-56.|||Abolishes 3-phosphoinositide-binding; when associated with E-58.|||Abolishes HIP1-induced cell death.|||Disordered|||ENTH|||Huntingtin-interacting protein 1|||I/LWEQ|||Important for actin binding|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Reduces AR-induced nuclear translocation.|||pDED                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083986|||http://purl.uniprot.org/annotation/VAR_051032|||http://purl.uniprot.org/annotation/VSP_044736|||http://purl.uniprot.org/annotation/VSP_057400
http://togogenome.org/gene/9606:OR5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD5|||http://purl.uniprot.org/uniprot/Q8NGI9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150573|||http://purl.uniprot.org/annotation/VAR_024097|||http://purl.uniprot.org/annotation/VAR_048045
http://togogenome.org/gene/9606:PBOV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZY1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Prostate and breast cancer overexpressed gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076285|||http://purl.uniprot.org/annotation/VAR_059707
http://togogenome.org/gene/9606:DCAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4B6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes serine/threonine-protein kinase kinase activity.|||Acidic residues|||Basic and acidic residues|||Chromo|||DDB1- and CUL4-associated factor 1|||DWD box 1|||DWD box 2|||Disordered|||Does not affect serine/threonine-protein kinase kinase activity.|||In isoform 2.|||In isoform 3.|||Interaction with NF2|||LisH|||Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1247.|||Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1283.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein kinase-like|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD repeat-like region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287473|||http://purl.uniprot.org/annotation/VAR_051486|||http://purl.uniprot.org/annotation/VAR_051487|||http://purl.uniprot.org/annotation/VAR_051488|||http://purl.uniprot.org/annotation/VSP_025498|||http://purl.uniprot.org/annotation/VSP_025499
http://togogenome.org/gene/9606:VCX3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H321                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 10 AA tandem repeats of L-S-Q-E-S-[EQ]-V-E-E-P|||2|||3|||4|||5|||6|||7|||8|||9|||Acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Polar residues|||Variable charge X-linked protein 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184662|||http://purl.uniprot.org/annotation/VAR_037644|||http://purl.uniprot.org/annotation/VSP_054105
http://togogenome.org/gene/9606:ATP2A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9K1|||http://purl.uniprot.org/uniprot/Q93084                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In a breast cancer sample; somatic mutation.|||In isoform SERCA3B.|||In isoform SERCA3C.|||In isoform SERCA3D.|||In isoform SERCA3E.|||In isoform SERCA3F.|||In isoform SERCA3G.|||Interaction with phospholamban 1|||Interaction with phospholamban 2|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Sarcoplasmic/endoplasmic reticulum calcium ATPase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046202|||http://purl.uniprot.org/annotation/VAR_036498|||http://purl.uniprot.org/annotation/VAR_048372|||http://purl.uniprot.org/annotation/VSP_060844|||http://purl.uniprot.org/annotation/VSP_060845|||http://purl.uniprot.org/annotation/VSP_060846|||http://purl.uniprot.org/annotation/VSP_060847|||http://purl.uniprot.org/annotation/VSP_060848|||http://purl.uniprot.org/annotation/VSP_060849
http://togogenome.org/gene/9606:SLC25A22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H936                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In DEE3; disrupts L-glutamate transporter activity.|||Mitochondrial glutamate carrier 1|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090619|||http://purl.uniprot.org/annotation/VAR_022737
http://togogenome.org/gene/9606:PLA2G4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C869                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes enzyme activity.|||C2|||Cytosolic phospholipase A2 beta|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No effect.|||Nucleophile|||PLA2c|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247021|||http://purl.uniprot.org/annotation/VAR_027047|||http://purl.uniprot.org/annotation/VAR_027048|||http://purl.uniprot.org/annotation/VAR_034365|||http://purl.uniprot.org/annotation/VAR_060082|||http://purl.uniprot.org/annotation/VSP_019871|||http://purl.uniprot.org/annotation/VSP_039387|||http://purl.uniprot.org/annotation/VSP_039388|||http://purl.uniprot.org/annotation/VSP_039389|||http://purl.uniprot.org/annotation/VSP_039390
http://togogenome.org/gene/9606:LRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02750|||http://purl.uniprot.org/uniprot/Q68CK4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||Leucine-rich alpha-2-glycoprotein|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020579|||http://purl.uniprot.org/annotation/PRO_5010141389|||http://purl.uniprot.org/annotation/VAR_024245|||http://purl.uniprot.org/annotation/VAR_050629
http://togogenome.org/gene/9606:WFDC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK68|||http://purl.uniprot.org/uniprot/Q8IUA0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||WAP|||WAP 1|||WAP 2|||WAP 3|||WAP four-disulfide core domain protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041384|||http://purl.uniprot.org/annotation/PRO_5007491793|||http://purl.uniprot.org/annotation/VAR_021910|||http://purl.uniprot.org/annotation/VAR_030861
http://togogenome.org/gene/9606:SRSF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Polar residues|||RRM|||Removed|||Serine/arginine-rich splicing factor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304412|||http://purl.uniprot.org/annotation/VSP_028026
http://togogenome.org/gene/9606:DENND11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1U4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  DENN domain-containing protein 11|||Disordered|||N-acetylvaline|||Omega-N-methylarginine|||Removed|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315221
http://togogenome.org/gene/9606:DTYMK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23919|||http://purl.uniprot.org/uniprot/Q53F55|||http://purl.uniprot.org/uniprot/Q6FGU2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In CONPM; loss of catalytic activity in patient fibroblasts.|||In CONPM; unknown pathological significance.|||In isoform 2.|||LID|||N-acetylalanine|||N6-acetyllysine|||Removed|||Thymidylate kinase|||Thymidylate kinase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155210|||http://purl.uniprot.org/annotation/VAR_087114|||http://purl.uniprot.org/annotation/VAR_087115|||http://purl.uniprot.org/annotation/VAR_087116|||http://purl.uniprot.org/annotation/VSP_054164
http://togogenome.org/gene/9606:ELMOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DM88|||http://purl.uniprot.org/uniprot/E9PLM8|||http://purl.uniprot.org/uniprot/Q8N336                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  ELMO|||ELMO domain-containing protein 1|||In isoform 2 and isoform 3.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225014|||http://purl.uniprot.org/annotation/VSP_044832|||http://purl.uniprot.org/annotation/VSP_044833
http://togogenome.org/gene/9606:ZNF560                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MR9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a colorectal cancer sample; somatic mutation.|||KRAB 1|||KRAB 2|||Zinc finger protein 560                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234589|||http://purl.uniprot.org/annotation/VAR_035588|||http://purl.uniprot.org/annotation/VAR_052866
http://togogenome.org/gene/9606:CAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPR0|||http://purl.uniprot.org/uniprot/J3KNB4|||http://purl.uniprot.org/uniprot/P49913                                                                                  ^@                                                                                  Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Domain Extent|||Helix|||Mass|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Active core|||Antibacterial peptide FALL-39|||Antibacterial peptide FF-33|||Antibacterial peptide KR-20|||Antibacterial peptide KS-30|||Antibacterial peptide LL-23|||Antibacterial peptide LL-29|||Antibacterial peptide LL-37|||Antibacterial peptide RK-31|||Cathelicidin antimicrobial peptide C-terminal|||Cathelin-like domain (CLD)|||Disrupts oligomerization. Loss of antimicrobial activity.|||Impacts oligomerization. Loss of antimicrobial activity.|||Loss of antimicrobial activity against M.luteus.|||No impact on antimicrobial activity against M.luteus.|||Precursor form pro-cathelicidin.|||Propeptide Cathelin-like domain (CLD).|||Reduced antimicrobial activity against M.luteus.|||Slightly increased MIC against E.coli K12 (MIC=15 compared to MIC=5).|||Slightly increased MIC against E.coli K12 (MIC=25 compared to MIC=5).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004722|||http://purl.uniprot.org/annotation/PRO_0000004723|||http://purl.uniprot.org/annotation/PRO_0000004724|||http://purl.uniprot.org/annotation/PRO_0000456767|||http://purl.uniprot.org/annotation/PRO_0000456768|||http://purl.uniprot.org/annotation/PRO_0000456769|||http://purl.uniprot.org/annotation/PRO_0000456770|||http://purl.uniprot.org/annotation/PRO_0000456771|||http://purl.uniprot.org/annotation/PRO_0000456772
http://togogenome.org/gene/9606:SYNGR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF5|||http://purl.uniprot.org/uniprot/O95473                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||MARVEL|||Synaptogyrin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183998|||http://purl.uniprot.org/annotation/VAR_052245
http://togogenome.org/gene/9606:CLMN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUQ2|||http://purl.uniprot.org/uniprot/Q96JQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calmin|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089854|||http://purl.uniprot.org/annotation/VAR_050866
http://togogenome.org/gene/9606:SPAG16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYB5|||http://purl.uniprot.org/uniprot/Q4G1A2|||http://purl.uniprot.org/uniprot/Q8N0X2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||Sperm-associated antigen 16 protein|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051223|||http://purl.uniprot.org/annotation/VAR_022366|||http://purl.uniprot.org/annotation/VAR_022367|||http://purl.uniprot.org/annotation/VAR_053418|||http://purl.uniprot.org/annotation/VSP_013493|||http://purl.uniprot.org/annotation/VSP_013494|||http://purl.uniprot.org/annotation/VSP_013495|||http://purl.uniprot.org/annotation/VSP_013496|||http://purl.uniprot.org/annotation/VSP_013497|||http://purl.uniprot.org/annotation/VSP_013498|||http://purl.uniprot.org/annotation/VSP_013499|||http://purl.uniprot.org/annotation/VSP_013500|||http://purl.uniprot.org/annotation/VSP_013501|||http://purl.uniprot.org/annotation/VSP_013502
http://togogenome.org/gene/9606:ZFP36L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNA8|||http://purl.uniprot.org/uniprot/Q07352                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Inhibits MAPKAPK2-mediated ARE-containing mRNA stabilization; when associated with A-54 and A-203. Inhibits interaction with 14-3-3 proteins and AKT1-mediated ARE-containing mRNA stabilization; when associated with A-203. Inhibits interaction with 14-3-3 proteins and AKT1-mediated ARE-containing mRNA stabilization, but does not affect ARE binding; when associated with A-90.|||Inhibits MAPKAPK2-mediated ARE-containing mRNA stabilization; when associated with A-92 and A-203.|||Inhibits interaction with 14-3-3 proteins and AKT1-mediated ARE-containing mRNA stabilization, but does not affect ARE binding; when associated with A-92.|||Inhibits interaction with 14-3-3 proteins and AKT1-mediated ARE-containing mRNA stabilization; when associated with A-92. Inhibits MAPKAPK2-mediated ARE-containing mRNA stabilization; when associated with A-54 and A-92.|||Inhibits p38 MAPK-mediated LDLR mRNA stabilization, but does not inhibit interaction with CNOT1 and CNOT7; when associated with A-334.|||Inhibits p38 MAPK-mediated LDLR mRNA stabilization, but does not inhibit interaction with CNOT1 and CNOT7; when associated with A-336.|||Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activation|||Necessary for mRNA decay activation|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by PKB/AKT1|||Phosphoserine; by PKB/AKT1 and MAPKAPK2|||Phosphoserine; by RPS6KA1|||Polar residues|||Reduces binding to ARE-containing mRNAs and ARE-mediated mRNA decay. Inhibits binding to ARE-containing mRNAs and ARE-mediated mRNA decay; when associated with R-120.|||Reduces binding to ARE-containing mRNAs and ARE-mediated mRNA decay. Inhibits binding to ARE-containing mRNAs and ARE-mediated mRNA decay; when associated with R-158.|||mRNA decay activator protein ZFP36L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089167
http://togogenome.org/gene/9606:CARNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM72                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-grasp|||Carnosine synthase 1|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329036|||http://purl.uniprot.org/annotation/VAR_042625|||http://purl.uniprot.org/annotation/VAR_060320|||http://purl.uniprot.org/annotation/VSP_032925|||http://purl.uniprot.org/annotation/VSP_032926|||http://purl.uniprot.org/annotation/VSP_053735|||http://purl.uniprot.org/annotation/VSP_053736
http://togogenome.org/gene/9606:SPTLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15269|||http://purl.uniprot.org/uniprot/Q6NUL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aminotransferase class I/classII|||Cytoplasmic|||Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.|||Disordered|||Does not affect catalytic activity towards serine; does not affect the interaction with SPTLC2.|||Found in a patient with HSAN1A; uncertain pathological significance.|||Helical|||In ALS27 and HSAN1A; reduced canonical activity towards serine and increased production of deoxysphingolipids.|||In ALS27; increased production of sphinganine and ceramides, when expressed in induced pluripotent stem cells (iPSC) differentiated into motor neuron-like cells; decreased response to inhibition mediated by ORMDL3 and ceramide; no effect on the interaction with ORMDL3.|||In ALS27; this variant can be caused by 2 genetic variations, one of which has been shown to affect splicing, leading to exon 2 skipping; in patient's whole blood sample, only exon 2 deletion was observed, but not the missense variant per se; when exon 2 deletion variant is expressed in induced pluripotent stem cells (iPSC) differentiated into motor neuron-like cells, increased production of sphinganine and ceramides is observed; when exon 2 deletion variant is transfected into HEK293 cells, decreased response to inhibition mediated by ORMDL3 or ceramide is observed.|||In ALS27; unknown pathological significance.|||In HSAN1A; inactive in the heterodimeric SPT complex; largely reduced canonical activity towards serine; contrary to wild-type, uses alanine as substrate leading to the formation of 1-deoxysphinganine (1-deoxySa); does not affect the interaction with SPTLC2.|||In HSAN1A; reduced canonical activity towards serine and increased production of deoxysphingolipids; no effect on subcellular location at the endoplasmic reticulum.|||In HSAN1A; reduced canonical activity towards serine; does not affect the interaction with SPTLC2.|||In HSAN1A; severe form with early onset; reduced canonical activity towards serine and increased production of deoxysphingolipids; no effect on subcellular location at the endoplasmic reticulum.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased serine palmitoyltransferase activity and sphingolipid content.|||Interaction with SPTLC2|||Lumenal|||Phosphotyrosine; by ABL|||Serine palmitoyltransferase 1|||Strongly decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163853|||http://purl.uniprot.org/annotation/VAR_011392|||http://purl.uniprot.org/annotation/VAR_011393|||http://purl.uniprot.org/annotation/VAR_011394|||http://purl.uniprot.org/annotation/VAR_036610|||http://purl.uniprot.org/annotation/VAR_037889|||http://purl.uniprot.org/annotation/VAR_037890|||http://purl.uniprot.org/annotation/VAR_066245|||http://purl.uniprot.org/annotation/VAR_066246|||http://purl.uniprot.org/annotation/VAR_068476|||http://purl.uniprot.org/annotation/VAR_073294|||http://purl.uniprot.org/annotation/VAR_088446|||http://purl.uniprot.org/annotation/VAR_088447|||http://purl.uniprot.org/annotation/VAR_088448|||http://purl.uniprot.org/annotation/VAR_088449|||http://purl.uniprot.org/annotation/VAR_088450|||http://purl.uniprot.org/annotation/VSP_043127|||http://purl.uniprot.org/annotation/VSP_043128
http://togogenome.org/gene/9606:NEO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FP8|||http://purl.uniprot.org/uniprot/Q92859                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neogenin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015043|||http://purl.uniprot.org/annotation/VAR_027954|||http://purl.uniprot.org/annotation/VSP_002593|||http://purl.uniprot.org/annotation/VSP_043330|||http://purl.uniprot.org/annotation/VSP_047134
http://togogenome.org/gene/9606:IL36A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHA7                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Interleukin-36 alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153644|||http://purl.uniprot.org/annotation/PRO_0000430545|||http://purl.uniprot.org/annotation/VAR_024504|||http://purl.uniprot.org/annotation/VAR_025055|||http://purl.uniprot.org/annotation/VAR_025056
http://togogenome.org/gene/9606:CIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQR4|||http://purl.uniprot.org/uniprot/A0A7P0T9K5|||http://purl.uniprot.org/uniprot/Q96RK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Found in a patient with Snijders Blok-Campeau syndrome; unknown pathological significance; the patient also carries a likely causative variation in CHD3.|||HMG box|||In MRD45.|||In MRD45; decreased protein expression.|||In MRD45; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Interaction with ATXN1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein capicua homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048598|||http://purl.uniprot.org/annotation/VAR_028302|||http://purl.uniprot.org/annotation/VAR_035936|||http://purl.uniprot.org/annotation/VAR_035937|||http://purl.uniprot.org/annotation/VAR_065090|||http://purl.uniprot.org/annotation/VAR_079294|||http://purl.uniprot.org/annotation/VAR_079295|||http://purl.uniprot.org/annotation/VAR_081527
http://togogenome.org/gene/9606:TNIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RGJ2|||http://purl.uniprot.org/uniprot/Q8NFZ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitin binding.|||Abolishes ubiquitin binding; loss of inhibitory activity on NF-kappa-B activation.|||Basic and acidic residues|||CCHC NOA-type|||Disordered|||Found in patients with gastrointestinal diffuse large cell lymphoma; impairs inhibitory activity on CARD11-induced NF-kappa-B activation.|||Found in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; impairs inhibitory activity on CARD11-induced NF-kappa-B activation and impairs interaction with TNFAIP3.|||In isoform 2.|||Phosphoserine|||Reduces phosphorylation.|||Reduces phosphorylation; reduces CHUK-mediated NF-kappa-B activation.|||TNFAIP3-interacting protein 2|||Ubiquitin-binding domain (UBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322583|||http://purl.uniprot.org/annotation/VAR_039463|||http://purl.uniprot.org/annotation/VAR_067969|||http://purl.uniprot.org/annotation/VAR_067970|||http://purl.uniprot.org/annotation/VSP_052701
http://togogenome.org/gene/9606:ADGRE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2Y6|||http://purl.uniprot.org/uniprot/A8K653|||http://purl.uniprot.org/uniprot/Q14246                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor E1|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012873|||http://purl.uniprot.org/annotation/PRO_5002722124|||http://purl.uniprot.org/annotation/PRO_5002724657|||http://purl.uniprot.org/annotation/VAR_027616|||http://purl.uniprot.org/annotation/VAR_027617|||http://purl.uniprot.org/annotation/VAR_027618|||http://purl.uniprot.org/annotation/VAR_027619|||http://purl.uniprot.org/annotation/VAR_027620|||http://purl.uniprot.org/annotation/VAR_027621|||http://purl.uniprot.org/annotation/VAR_027622|||http://purl.uniprot.org/annotation/VAR_027623|||http://purl.uniprot.org/annotation/VAR_027624|||http://purl.uniprot.org/annotation/VAR_027625|||http://purl.uniprot.org/annotation/VAR_027626|||http://purl.uniprot.org/annotation/VAR_027627|||http://purl.uniprot.org/annotation/VAR_046976|||http://purl.uniprot.org/annotation/VAR_046977|||http://purl.uniprot.org/annotation/VSP_009594|||http://purl.uniprot.org/annotation/VSP_045521|||http://purl.uniprot.org/annotation/VSP_045522|||http://purl.uniprot.org/annotation/VSP_045523|||http://purl.uniprot.org/annotation/VSP_045524
http://togogenome.org/gene/9606:NAA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9N2|||http://purl.uniprot.org/uniprot/P41227                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation by IKKB and reduces cell growth.|||Basic and acidic residues|||Disordered|||In NATD; decreased protein stability; strong decrease in N-terminal acetylation activity in vitro.|||In NATD; reduced N-terminal acetyltransferase activity; impaired interaction with NAA15 and NAA50; does not affect cytoplasmic localization.|||In NATD; reduced monomeric N-terminal acetyltransferase activity in vitro.|||In isoform 2.|||Interaction with NAA15|||Loss of its ability to acetylate HSPA1A and HSPA1B.|||N-acetylmethionine|||N-acetyltransferase|||N-alpha-acetyltransferase 10|||N6-acetyllysine; by autocatalysis|||Phosphoserine|||Phosphoserine; by IKKB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074532|||http://purl.uniprot.org/annotation/VAR_066652|||http://purl.uniprot.org/annotation/VAR_075206|||http://purl.uniprot.org/annotation/VAR_082604|||http://purl.uniprot.org/annotation/VSP_046205|||http://purl.uniprot.org/annotation/VSP_046206
http://togogenome.org/gene/9606:FNDC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Fibronectin type III domain-containing protein 7|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328880|||http://purl.uniprot.org/annotation/VAR_042570|||http://purl.uniprot.org/annotation/VAR_042571|||http://purl.uniprot.org/annotation/VAR_042572|||http://purl.uniprot.org/annotation/VAR_042573
http://togogenome.org/gene/9606:RRAGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQG4|||http://purl.uniprot.org/uniprot/Q9HB90                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active mutant. Increased RPTOR-binding.|||Disordered|||Found in a patient with idiopathic dilated cardiomyopathy; renders cells partially insensitive to amino acid deprivation and result in activated mTORC1 signaling.|||Found in patients with follicular lymphoma; increased activation of mTORC1.|||Found in patients with follicular lymphoma; maintains the GDP-bound state leading to constitutive activation of mTORC1.|||Maintains GTP-bound state, leading to inactivate mTORC1. Decreased RPTOR-binding.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Promotes interaction with GATOR1 in the GAP mode.|||Ras-related GTP-binding protein C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239951|||http://purl.uniprot.org/annotation/VAR_076511|||http://purl.uniprot.org/annotation/VAR_088360|||http://purl.uniprot.org/annotation/VAR_088361|||http://purl.uniprot.org/annotation/VAR_088362|||http://purl.uniprot.org/annotation/VAR_088363|||http://purl.uniprot.org/annotation/VAR_088364|||http://purl.uniprot.org/annotation/VAR_088365|||http://purl.uniprot.org/annotation/VAR_088366|||http://purl.uniprot.org/annotation/VAR_088367
http://togogenome.org/gene/9606:TIRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58753                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes NF-kappa-B activation.|||Disordered|||Does not affect NF-kappa-B activation and TNF production.|||Hypomorphic variant resulting in impaired NF-kappa-B activation and TNF production; loss of interaction with MYD88.|||In isoform 2.|||In isoform 3.|||Polar residues|||TIR|||The functional impact of this variant is unclear; it has been reported both to affect interaction with TLR2, hence attenuating TLR2 signal transduction and to have no effect on NF-kappa-B activation and TNF production.|||Toll/interleukin-1 receptor domain-containing adapter protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072547|||http://purl.uniprot.org/annotation/VAR_019143|||http://purl.uniprot.org/annotation/VAR_019144|||http://purl.uniprot.org/annotation/VAR_019145|||http://purl.uniprot.org/annotation/VAR_019146|||http://purl.uniprot.org/annotation/VAR_036691|||http://purl.uniprot.org/annotation/VAR_061713|||http://purl.uniprot.org/annotation/VSP_010765|||http://purl.uniprot.org/annotation/VSP_017239
http://togogenome.org/gene/9606:MPDU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4W8|||http://purl.uniprot.org/uniprot/B4DLH7|||http://purl.uniprot.org/uniprot/J3QW43|||http://purl.uniprot.org/uniprot/O75352                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In CDG1F.|||In isoform 2.|||Mannose-P-dolichol utilization defect 1 protein|||N-acetylalanine|||PQ-loop 1|||PQ-loop 2|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221034|||http://purl.uniprot.org/annotation/VAR_021388|||http://purl.uniprot.org/annotation/VAR_021389|||http://purl.uniprot.org/annotation/VAR_021390|||http://purl.uniprot.org/annotation/VAR_047757|||http://purl.uniprot.org/annotation/VAR_047758|||http://purl.uniprot.org/annotation/VSP_056349|||http://purl.uniprot.org/annotation/VSP_056350
http://togogenome.org/gene/9606:BAIAP2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2|||Disordered|||IMD|||In isoform 2.|||Phosphoserine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256130|||http://purl.uniprot.org/annotation/VSP_021324
http://togogenome.org/gene/9606:C1orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TB16|||http://purl.uniprot.org/uniprot/Q8WWF1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Uncharacterized protein C1orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251200|||http://purl.uniprot.org/annotation/PRO_5014586923
http://togogenome.org/gene/9606:ROBO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W703|||http://purl.uniprot.org/uniprot/Q9HCK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In VUR2.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Roundabout homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031036|||http://purl.uniprot.org/annotation/PRO_5035731291|||http://purl.uniprot.org/annotation/VAR_032960|||http://purl.uniprot.org/annotation/VAR_032961|||http://purl.uniprot.org/annotation/VSP_010647|||http://purl.uniprot.org/annotation/VSP_043394
http://togogenome.org/gene/9606:PROSER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||Polar residues|||Proline and serine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274309|||http://purl.uniprot.org/annotation/VAR_030253|||http://purl.uniprot.org/annotation/VAR_030254|||http://purl.uniprot.org/annotation/VSP_055641
http://togogenome.org/gene/9606:GRK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPS5|||http://purl.uniprot.org/uniprot/P43250                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1100-fold defects in kinase activity.|||12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-6.|||12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-7.|||140-fold defects in kinase activity.|||AGC-kinase C-terminal|||Abolishes palmitoylation; when associated with S-561 and S-562.|||Abolishes palmitoylation; when associated with S-561 and S-565.|||Abolishes palmitoylation; when associated with S-562 and S-565.|||Disordered|||G protein-coupled receptor kinase 6|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform GRK6B.|||In isoform GRK6C.|||N-terminal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||RGS|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085974|||http://purl.uniprot.org/annotation/VAR_040524|||http://purl.uniprot.org/annotation/VAR_040525|||http://purl.uniprot.org/annotation/VAR_040526|||http://purl.uniprot.org/annotation/VSP_004938|||http://purl.uniprot.org/annotation/VSP_041813|||http://purl.uniprot.org/annotation/VSP_041814
http://togogenome.org/gene/9606:CXCR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0N3|||http://purl.uniprot.org/uniprot/O00574                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-X-C chemokine receptor type 6|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In STRL33.3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069365|||http://purl.uniprot.org/annotation/VAR_003506|||http://purl.uniprot.org/annotation/VAR_024253
http://togogenome.org/gene/9606:SLX1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes endonucleolytic activity.|||Disordered|||GIY-YIG|||In isoform 2.|||Pro residues|||SLX1-type|||Structure-specific endonuclease subunit SLX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332120|||http://purl.uniprot.org/annotation/VSP_033331
http://togogenome.org/gene/9606:C1orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6N3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||UPF0690 protein C1orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254630|||http://purl.uniprot.org/annotation/VSP_021267|||http://purl.uniprot.org/annotation/VSP_021268|||http://purl.uniprot.org/annotation/VSP_021269|||http://purl.uniprot.org/annotation/VSP_021270
http://togogenome.org/gene/9606:EXOC3L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RC7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exocyst complex component 3-like protein 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274380|||http://purl.uniprot.org/annotation/VAR_030273|||http://purl.uniprot.org/annotation/VAR_030274|||http://purl.uniprot.org/annotation/VAR_030275|||http://purl.uniprot.org/annotation/VAR_030276|||http://purl.uniprot.org/annotation/VAR_062863
http://togogenome.org/gene/9606:PIGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2B2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In CHIME.|||In isoform 2.|||N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207167|||http://purl.uniprot.org/annotation/VAR_068221|||http://purl.uniprot.org/annotation/VSP_056886
http://togogenome.org/gene/9606:PLCXD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXD1|||http://purl.uniprot.org/uniprot/Q63HM9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  PI-PLC X domain-containing protein 3|||PI-PLC X-box|||Phosphatidylinositol-specific phospholipase C X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305693
http://togogenome.org/gene/9606:SMG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND04                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ALKUS.|||In isoform 2.|||In isoform 3.|||Nonsense-mediated mRNA decay factor SMG8|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304974|||http://purl.uniprot.org/annotation/VAR_035137|||http://purl.uniprot.org/annotation/VAR_085550|||http://purl.uniprot.org/annotation/VAR_085551|||http://purl.uniprot.org/annotation/VSP_028164|||http://purl.uniprot.org/annotation/VSP_028165|||http://purl.uniprot.org/annotation/VSP_028166
http://togogenome.org/gene/9606:RNF168                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to ubiquitinate KDM4A.|||Basic and acidic residues|||Disordered|||Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-16.|||Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-19.|||Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes.|||Does not affect ubiquitin-binding but impairs recruitment to DSBs.|||E3 ubiquitin-protein ligase RNF168|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired ability to bind ubiquitin.|||Impairs ability to form foci following ionizing radiation and impaired binding to 'Lys-63'-linked ubiquitin.|||LR motif 1|||LR motif 2|||MIU motif 1|||MIU motif 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||Still able to bind 'Lys-63'-linked ubiquitin.|||UMI motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245596|||http://purl.uniprot.org/annotation/VAR_026997|||http://purl.uniprot.org/annotation/VAR_034466|||http://purl.uniprot.org/annotation/VAR_052110
http://togogenome.org/gene/9606:EGFLAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HQ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibronectin type-III 1|||Fibronectin type-III 2|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||Pikachurin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306803|||http://purl.uniprot.org/annotation/VAR_035302|||http://purl.uniprot.org/annotation/VAR_035303|||http://purl.uniprot.org/annotation/VAR_035304|||http://purl.uniprot.org/annotation/VAR_035305|||http://purl.uniprot.org/annotation/VAR_055718|||http://purl.uniprot.org/annotation/VAR_055719|||http://purl.uniprot.org/annotation/VSP_028475|||http://purl.uniprot.org/annotation/VSP_028476|||http://purl.uniprot.org/annotation/VSP_028477|||http://purl.uniprot.org/annotation/VSP_028478|||http://purl.uniprot.org/annotation/VSP_028481
http://togogenome.org/gene/9606:ZNF420                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAQ5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 420                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047575|||http://purl.uniprot.org/annotation/VSP_055951|||http://purl.uniprot.org/annotation/VSP_055952
http://togogenome.org/gene/9606:CA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUB4|||http://purl.uniprot.org/uniprot/O43570                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase|||Carbonic anhydrase 12|||Cytoplasmic|||Extracellular|||Helical|||In HYCHL; severe decrease of activity in the presence of physiological NaCl concentrations; mutant enzyme is highly inhibited by acetazolamide and shows higher sensitivity to inhibition by anions compared to wild-type; the mutation affects the chloride-mediated negative feedback regulation of the enzyme leading to excessive chloride secretion in sweat; no effect on localization to cell membrane.|||In HYCHL; severe decrease of activity in the presence of physiological NaCl concentrations; no effect on localization to cell membrane.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004248|||http://purl.uniprot.org/annotation/PRO_5014085058|||http://purl.uniprot.org/annotation/VAR_065292|||http://purl.uniprot.org/annotation/VAR_081182|||http://purl.uniprot.org/annotation/VSP_000772
http://togogenome.org/gene/9606:SULT2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00204                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10-fold increase in specific activity for DHEA sulfation. 10-fold increase in substrate affinity for DHEA and pregnenolone. No effect on substrate affinity for PAPS. Increases enzyme stability.|||Abolishes nuclear localization.|||Disordered|||In ARCI14; unknown pathological significance.|||In isoform 2.|||Increases the cholesterol sulfotransferase activity.|||Loss of the cholesterol sulfotransferase activity.|||No change in subcellular localization.|||Phosphoserine|||Pro residues|||Proton acceptor|||Sulfotransferase 2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085149|||http://purl.uniprot.org/annotation/VAR_020887|||http://purl.uniprot.org/annotation/VAR_020888|||http://purl.uniprot.org/annotation/VAR_021988|||http://purl.uniprot.org/annotation/VAR_079210|||http://purl.uniprot.org/annotation/VAR_079211|||http://purl.uniprot.org/annotation/VSP_012510
http://togogenome.org/gene/9606:PSMA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K4|||http://purl.uniprot.org/uniprot/O14818                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Displays impaired G1/S transition and S/G2 progression.|||Found in patient with severe intellectual disability; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphotyrosine; by ABL1 and ABL2|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124142|||http://purl.uniprot.org/annotation/VAR_078692|||http://purl.uniprot.org/annotation/VSP_005281|||http://purl.uniprot.org/annotation/VSP_046556|||http://purl.uniprot.org/annotation/VSP_046557
http://togogenome.org/gene/9606:IRX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78415                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||Iroquois-class homeodomain protein IRX-3|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049155|||http://purl.uniprot.org/annotation/VAR_055957|||http://purl.uniprot.org/annotation/VAR_061267
http://togogenome.org/gene/9606:ODF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C3TX97|||http://purl.uniprot.org/uniprot/Q2M2E3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Outer dense fiber protein 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304722|||http://purl.uniprot.org/annotation/VAR_035060|||http://purl.uniprot.org/annotation/VAR_035061|||http://purl.uniprot.org/annotation/VAR_035062
http://togogenome.org/gene/9606:HOMEZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox and leucine zipper protein Homez|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049135|||http://purl.uniprot.org/annotation/VAR_055956|||http://purl.uniprot.org/annotation/VSP_054303
http://togogenome.org/gene/9606:HSPA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKX5|||http://purl.uniprot.org/uniprot/B3KSM6|||http://purl.uniprot.org/uniprot/P17066                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of in vitro methylation by METTL21A.|||Disordered|||Heat shock 70 kDa protein 6|||N6,N6,N6-trimethyllysine; by METTL21A; in vitro|||Nucleotide-binding domain (NBD)|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078264|||http://purl.uniprot.org/annotation/VAR_024182|||http://purl.uniprot.org/annotation/VAR_024183|||http://purl.uniprot.org/annotation/VAR_049605|||http://purl.uniprot.org/annotation/VAR_049606|||http://purl.uniprot.org/annotation/VAR_049607|||http://purl.uniprot.org/annotation/VAR_049608|||http://purl.uniprot.org/annotation/VAR_049609|||http://purl.uniprot.org/annotation/VAR_049610|||http://purl.uniprot.org/annotation/VAR_049611|||http://purl.uniprot.org/annotation/VAR_049612|||http://purl.uniprot.org/annotation/VAR_049613|||http://purl.uniprot.org/annotation/VAR_049614|||http://purl.uniprot.org/annotation/VAR_049615|||http://purl.uniprot.org/annotation/VAR_049616|||http://purl.uniprot.org/annotation/VAR_049617|||http://purl.uniprot.org/annotation/VAR_049618|||http://purl.uniprot.org/annotation/VAR_059360|||http://purl.uniprot.org/annotation/VAR_059361|||http://purl.uniprot.org/annotation/VAR_060718|||http://purl.uniprot.org/annotation/VAR_060719|||http://purl.uniprot.org/annotation/VAR_060720|||http://purl.uniprot.org/annotation/VAR_060721
http://togogenome.org/gene/9606:SLC5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31639|||http://purl.uniprot.org/uniprot/Q8WY15                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreases D-glucose transporter activity.|||Extracellular|||Helical|||Implicated in sodium coupling|||In GLYS.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.|||Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.|||Sodium/glucose cotransporter 2|||Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105372|||http://purl.uniprot.org/annotation/VAR_019310|||http://purl.uniprot.org/annotation/VSP_056333|||http://purl.uniprot.org/annotation/VSP_056334
http://togogenome.org/gene/9606:KIFC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIFC2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125429|||http://purl.uniprot.org/annotation/VAR_049684|||http://purl.uniprot.org/annotation/VAR_049685|||http://purl.uniprot.org/annotation/VSP_056102|||http://purl.uniprot.org/annotation/VSP_056103|||http://purl.uniprot.org/annotation/VSP_056104
http://togogenome.org/gene/9606:TMEM71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5X7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 71                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278283|||http://purl.uniprot.org/annotation/VSP_023259|||http://purl.uniprot.org/annotation/VSP_023260
http://togogenome.org/gene/9606:ACTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63261                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG1|||(Microbial infection) Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG1|||Actin, cytoplasmic 2|||Actin, cytoplasmic 2, N-terminally processed|||Found in a patient with isolated coloboma; decreased incorporation into F-actin; decreased interaction with cofilin; loss of interaction with TWF1, CAPZB and profilin.|||In BRWS2.|||In DFNA20.|||In DFNA20; unknown pathological significance.|||Methionine (R)-sulfoxide|||N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial|||N-acetylmethionine|||N6-methyllysine|||Removed; alternate|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000831|||http://purl.uniprot.org/annotation/PRO_0000367100|||http://purl.uniprot.org/annotation/VAR_032434|||http://purl.uniprot.org/annotation/VAR_032435|||http://purl.uniprot.org/annotation/VAR_032436|||http://purl.uniprot.org/annotation/VAR_032437|||http://purl.uniprot.org/annotation/VAR_032438|||http://purl.uniprot.org/annotation/VAR_032439|||http://purl.uniprot.org/annotation/VAR_048186|||http://purl.uniprot.org/annotation/VAR_067814|||http://purl.uniprot.org/annotation/VAR_067815|||http://purl.uniprot.org/annotation/VAR_067816|||http://purl.uniprot.org/annotation/VAR_067817|||http://purl.uniprot.org/annotation/VAR_067818|||http://purl.uniprot.org/annotation/VAR_067819|||http://purl.uniprot.org/annotation/VAR_067824|||http://purl.uniprot.org/annotation/VAR_067825|||http://purl.uniprot.org/annotation/VAR_067826|||http://purl.uniprot.org/annotation/VAR_079849|||http://purl.uniprot.org/annotation/VAR_079878|||http://purl.uniprot.org/annotation/VAR_079879
http://togogenome.org/gene/9606:PHEX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNS0|||http://purl.uniprot.org/uniprot/B4DWG8|||http://purl.uniprot.org/uniprot/P78562                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In XLHR.|||In XLHR; sporadic.|||N-linked (GlcNAc...) asparagine|||Peptidase M13|||Peptidase M13 C-terminal|||Peptidase M13 N-terminal|||Phosphate-regulating neutral endopeptidase PHEX|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078228|||http://purl.uniprot.org/annotation/VAR_006738|||http://purl.uniprot.org/annotation/VAR_006739|||http://purl.uniprot.org/annotation/VAR_006740|||http://purl.uniprot.org/annotation/VAR_006741|||http://purl.uniprot.org/annotation/VAR_006742|||http://purl.uniprot.org/annotation/VAR_006743|||http://purl.uniprot.org/annotation/VAR_006744|||http://purl.uniprot.org/annotation/VAR_006745|||http://purl.uniprot.org/annotation/VAR_006746|||http://purl.uniprot.org/annotation/VAR_010616|||http://purl.uniprot.org/annotation/VAR_010617|||http://purl.uniprot.org/annotation/VAR_010618|||http://purl.uniprot.org/annotation/VAR_010619|||http://purl.uniprot.org/annotation/VAR_010620|||http://purl.uniprot.org/annotation/VAR_010621|||http://purl.uniprot.org/annotation/VAR_010622|||http://purl.uniprot.org/annotation/VAR_010623|||http://purl.uniprot.org/annotation/VAR_010624|||http://purl.uniprot.org/annotation/VAR_010625|||http://purl.uniprot.org/annotation/VAR_010626|||http://purl.uniprot.org/annotation/VAR_010627|||http://purl.uniprot.org/annotation/VAR_010628|||http://purl.uniprot.org/annotation/VAR_010629|||http://purl.uniprot.org/annotation/VAR_010630|||http://purl.uniprot.org/annotation/VAR_010631|||http://purl.uniprot.org/annotation/VAR_010632|||http://purl.uniprot.org/annotation/VAR_010633|||http://purl.uniprot.org/annotation/VAR_010634|||http://purl.uniprot.org/annotation/VAR_010635|||http://purl.uniprot.org/annotation/VAR_010636|||http://purl.uniprot.org/annotation/VAR_010637|||http://purl.uniprot.org/annotation/VAR_010638|||http://purl.uniprot.org/annotation/VAR_010639
http://togogenome.org/gene/9606:ERMARD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6L9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Endoplasmic reticulum membrane-associated RNA degradation protein|||Helical|||In PVNH6; may decrease protein stability.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295626|||http://purl.uniprot.org/annotation/VAR_033300|||http://purl.uniprot.org/annotation/VAR_070433|||http://purl.uniprot.org/annotation/VSP_026951|||http://purl.uniprot.org/annotation/VSP_026952|||http://purl.uniprot.org/annotation/VSP_053708
http://togogenome.org/gene/9606:HCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4G3|||http://purl.uniprot.org/uniprot/P08631                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes palmitoylation and localization at the cell membrane.|||Constitutively activated kinase, leading to cellular transformation.|||Disordered|||In AIPCV; results in increased activation of inflammatory response; decreased protein abundance in patient cells; increased protein degradation; results in increased kinase activity and autophosphorylation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Loss of kinase activity.|||Myristoylation and palmitoylation are abolished, leading to entirely cytoplasmic localization; in isoform 2.|||N-myristoyl glycine|||Palmitoylation is abolished, some cytoplasmic and no calveolar localization; in isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced catalytic activity and higher affinity for target peptides.|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Slight palmitoylation, cytoplasmic and caveolar localization; in isoform 1;.|||Tyrosine-protein kinase HCK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024433|||http://purl.uniprot.org/annotation/VAR_033836|||http://purl.uniprot.org/annotation/VAR_041707|||http://purl.uniprot.org/annotation/VAR_041708|||http://purl.uniprot.org/annotation/VAR_041709|||http://purl.uniprot.org/annotation/VAR_088298|||http://purl.uniprot.org/annotation/VSP_018858|||http://purl.uniprot.org/annotation/VSP_041926
http://togogenome.org/gene/9606:DEFB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60022                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Mass|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-defensin 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006899|||http://purl.uniprot.org/annotation/PRO_0000006900|||http://purl.uniprot.org/annotation/VAR_014925|||http://purl.uniprot.org/annotation/VAR_014926|||http://purl.uniprot.org/annotation/VAR_018405
http://togogenome.org/gene/9606:UQCRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22695                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 2, mitochondrial|||In MC3DN5.|||In a colorectal cancer sample; somatic mutation.|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026791|||http://purl.uniprot.org/annotation/VAR_029336|||http://purl.uniprot.org/annotation/VAR_034582|||http://purl.uniprot.org/annotation/VAR_034583|||http://purl.uniprot.org/annotation/VAR_036479|||http://purl.uniprot.org/annotation/VAR_069709
http://togogenome.org/gene/9606:DNAH12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZR08                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||CFDEFNR motif|||Dynein axonemal heavy chain 12|||GPAGTGKT motif|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000370324|||http://purl.uniprot.org/annotation/VAR_034829|||http://purl.uniprot.org/annotation/VAR_034830|||http://purl.uniprot.org/annotation/VAR_034831|||http://purl.uniprot.org/annotation/VAR_034832|||http://purl.uniprot.org/annotation/VAR_037390|||http://purl.uniprot.org/annotation/VAR_037391|||http://purl.uniprot.org/annotation/VAR_060142|||http://purl.uniprot.org/annotation/VAR_060143|||http://purl.uniprot.org/annotation/VAR_060144|||http://purl.uniprot.org/annotation/VAR_060145|||http://purl.uniprot.org/annotation/VAR_060146|||http://purl.uniprot.org/annotation/VAR_060147|||http://purl.uniprot.org/annotation/VSP_036920|||http://purl.uniprot.org/annotation/VSP_036921|||http://purl.uniprot.org/annotation/VSP_036922|||http://purl.uniprot.org/annotation/VSP_036923|||http://purl.uniprot.org/annotation/VSP_036924|||http://purl.uniprot.org/annotation/VSP_039335|||http://purl.uniprot.org/annotation/VSP_039336
http://togogenome.org/gene/9606:ARPP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HI65|||http://purl.uniprot.org/uniprot/A8K0T4|||http://purl.uniprot.org/uniprot/A8K1F3|||http://purl.uniprot.org/uniprot/Q9UBL0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||R3H|||Removed|||SUZ|||cAMP-regulated phosphoprotein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064682|||http://purl.uniprot.org/annotation/VSP_029469|||http://purl.uniprot.org/annotation/VSP_029470|||http://purl.uniprot.org/annotation/VSP_029471|||http://purl.uniprot.org/annotation/VSP_029472|||http://purl.uniprot.org/annotation/VSP_029473|||http://purl.uniprot.org/annotation/VSP_029474|||http://purl.uniprot.org/annotation/VSP_029475|||http://purl.uniprot.org/annotation/VSP_029476
http://togogenome.org/gene/9606:OSBPL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 7.|||N-acetylalanine|||Oxysterol-binding protein-related protein 9|||PH|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100379|||http://purl.uniprot.org/annotation/VAR_069380|||http://purl.uniprot.org/annotation/VSP_003782|||http://purl.uniprot.org/annotation/VSP_036779|||http://purl.uniprot.org/annotation/VSP_036780|||http://purl.uniprot.org/annotation/VSP_036781|||http://purl.uniprot.org/annotation/VSP_043630|||http://purl.uniprot.org/annotation/VSP_043631
http://togogenome.org/gene/9606:RAD23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4W4|||http://purl.uniprot.org/uniprot/P54727                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Impairs interaction with EEF1A1.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||STI1|||UBA|||UBA 1|||UBA 2|||UV excision repair protein RAD23 homolog B|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114906|||http://purl.uniprot.org/annotation/VAR_014350|||http://purl.uniprot.org/annotation/VSP_045606
http://togogenome.org/gene/9606:ITM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43736                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BRICHOS|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Integral membrane protein 2A|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154818|||http://purl.uniprot.org/annotation/VAR_034029|||http://purl.uniprot.org/annotation/VAR_034030|||http://purl.uniprot.org/annotation/VSP_042562
http://togogenome.org/gene/9606:SLC12A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y666                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 12 member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178039|||http://purl.uniprot.org/annotation/VAR_028748|||http://purl.uniprot.org/annotation/VSP_006119|||http://purl.uniprot.org/annotation/VSP_006120
http://togogenome.org/gene/9606:UBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR1|||In JBS.|||In JBS; decreased, but detectable activity in a yeast-based assay.|||In JBS; prevents proper folding of the UBR-type zinc finger; may decrease protein stability; loss of activity in a yeast-based assay.|||In JBS; strong decrease in activity in a yeast-based assay.|||In JBS; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RING-type; atypical|||Removed|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056136|||http://purl.uniprot.org/annotation/VAR_024741|||http://purl.uniprot.org/annotation/VAR_024742|||http://purl.uniprot.org/annotation/VAR_034467|||http://purl.uniprot.org/annotation/VAR_052116|||http://purl.uniprot.org/annotation/VAR_061822|||http://purl.uniprot.org/annotation/VAR_075179|||http://purl.uniprot.org/annotation/VAR_075180|||http://purl.uniprot.org/annotation/VAR_075181|||http://purl.uniprot.org/annotation/VAR_075182|||http://purl.uniprot.org/annotation/VAR_075183|||http://purl.uniprot.org/annotation/VAR_075184|||http://purl.uniprot.org/annotation/VAR_075185|||http://purl.uniprot.org/annotation/VAR_075186|||http://purl.uniprot.org/annotation/VAR_075187|||http://purl.uniprot.org/annotation/VAR_075188|||http://purl.uniprot.org/annotation/VAR_075189|||http://purl.uniprot.org/annotation/VAR_075190|||http://purl.uniprot.org/annotation/VAR_075191|||http://purl.uniprot.org/annotation/VAR_075192|||http://purl.uniprot.org/annotation/VAR_075193|||http://purl.uniprot.org/annotation/VAR_075194|||http://purl.uniprot.org/annotation/VAR_075195|||http://purl.uniprot.org/annotation/VAR_075196|||http://purl.uniprot.org/annotation/VAR_075197|||http://purl.uniprot.org/annotation/VSP_015164|||http://purl.uniprot.org/annotation/VSP_015165
http://togogenome.org/gene/9606:TMEM131                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92545                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane protein 131                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097538
http://togogenome.org/gene/9606:CNDP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KP4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosolic non-specific dipeptidase|||Important for catalytic activity|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185272|||http://purl.uniprot.org/annotation/VAR_057154|||http://purl.uniprot.org/annotation/VSP_038203
http://togogenome.org/gene/9606:TRIM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8M5|||http://purl.uniprot.org/uniprot/Q9UDY6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||In isoform Beta.|||RING-type|||Tripartite motif-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056211|||http://purl.uniprot.org/annotation/VAR_052127|||http://purl.uniprot.org/annotation/VAR_052128|||http://purl.uniprot.org/annotation/VSP_005748
http://togogenome.org/gene/9606:SAMD4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QZ22|||http://purl.uniprot.org/uniprot/Q5PRF9|||http://purl.uniprot.org/uniprot/Q66K25|||http://purl.uniprot.org/uniprot/Q8IXP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Smaug homolog 2|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260080
http://togogenome.org/gene/9606:ERH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84090                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Enhancer of rudimentary homolog|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219351
http://togogenome.org/gene/9606:CCDC183                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5S1|||http://purl.uniprot.org/uniprot/Q96IG8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 183|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293465|||http://purl.uniprot.org/annotation/VAR_033046|||http://purl.uniprot.org/annotation/VAR_033047|||http://purl.uniprot.org/annotation/VAR_033048|||http://purl.uniprot.org/annotation/VAR_033049|||http://purl.uniprot.org/annotation/VAR_063112|||http://purl.uniprot.org/annotation/VSP_026477|||http://purl.uniprot.org/annotation/VSP_026478|||http://purl.uniprot.org/annotation/VSP_026479|||http://purl.uniprot.org/annotation/VSP_026481|||http://purl.uniprot.org/annotation/VSP_026482|||http://purl.uniprot.org/annotation/VSP_026483|||http://purl.uniprot.org/annotation/VSP_026484
http://togogenome.org/gene/9606:ME3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R995|||http://purl.uniprot.org/uniprot/Q16798|||http://purl.uniprot.org/uniprot/Q6TCH8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Important for activity|||In isoform 2.|||Malic enzyme N-terminal|||Malic enzyme NAD-binding|||Mitochondrion|||NADP-dependent malic enzyme, mitochondrial|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018539|||http://purl.uniprot.org/annotation/VAR_047369|||http://purl.uniprot.org/annotation/VAR_047370|||http://purl.uniprot.org/annotation/VSP_056626|||http://purl.uniprot.org/annotation/VSP_056627
http://togogenome.org/gene/9606:SLC30A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR19|||http://purl.uniprot.org/uniprot/Q6XR72                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium/manganese antiporter SLC30A10|||Cytoplasmic|||Decreased calcium:manganese antiporter activity.|||Decreased interaction with SLC30A3. No effect on self-association. Decreased zinc ion transmembrane transporter activity. Decreased EGF-induced ERK1/2 phosphorylation.|||Disordered|||Extracellular|||Helical|||Important for coupling of manganese to calcium transport|||In HMNDYT1.|||In HMNDYT1; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; increased proteasomal degradation; decreased function in intracellular manganese ion homeostasis.|||In HMNDYT1; loss of localization to the plasma membrane; retained in the endoplasmic reticulum; increased proteasomal degradation; loss of function in intracellular manganese ion homeostasis.|||In isoform 2.|||In isoform 3.|||Loss of calcium:manganese antiporter activity and increased zinc ion transmembrane transporter activity; when associated with H-43 and F-242.|||Loss of calcium:manganese antiporter activity and increased zinc ion transmembrane transporter activity; when associated with H-43 and V-52.|||Loss of calcium:manganese antiporter activity.|||Loss of calcium:manganese antiporter activity. Uncoupling between manganese and calcium exchange.|||Loss of localization to the plasma membrane.|||No effect on localization to the plasma membrane. Changed calcium:manganese antiporter activity. Enhanced coupling between manganese and calcium exchange.|||No effect on localization to the plasma membrane. Loss of calcium:manganese antiporter activity.|||No effect on localization to the plasma membrane. Loss of calcium:manganese antiporter activity. Loss of calcium:manganese antiporter activity and increased zinc ion transmembrane transporter activity; when associated with V-52 and F-242.|||No effect on localization to the plasma membrane. Loss of manganese ion export across plasma membrane.|||No effect on localization to the plasma membrane. No effect on calcium:manganese antiporter activity.|||No effect on localization to the plasma membrane. No effect on localization to the plasma membrane and decreased calcium:manganese antiporter activity; when associated with A-127.|||No effect on localization to the plasma membrane. No effect on localization to the plasma membrane and decreased calcium:manganese antiporter activity; when associated with A-244.|||Required for plasma membrane localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312580|||http://purl.uniprot.org/annotation/VAR_072573|||http://purl.uniprot.org/annotation/VAR_072574|||http://purl.uniprot.org/annotation/VAR_072575|||http://purl.uniprot.org/annotation/VAR_072576|||http://purl.uniprot.org/annotation/VAR_072577|||http://purl.uniprot.org/annotation/VSP_029863|||http://purl.uniprot.org/annotation/VSP_029864|||http://purl.uniprot.org/annotation/VSP_029865
http://togogenome.org/gene/9606:B3GNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY97                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of enzymatic activity, no loss of B3GNT8-binding.|||Lumenal|||N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219170|||http://purl.uniprot.org/annotation/VSP_001791
http://togogenome.org/gene/9606:GADD45G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95257                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with E-77, E-80 and R-83.|||30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-77 and E-80.|||30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-77 and R-83.|||30-fold reduction in homodimerization affinity and 90% decrease in growth inhibition activity and ability to stop cell cycle; when associated with R-47, E-80 and R-83.|||Growth arrest and DNA damage-inducible protein GADD45 gamma|||Homodimerization|||Reduced growth inhibition activity; when associated with K-87.|||Reduced growth inhibition activity; when associated with K-89.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148336|||http://purl.uniprot.org/annotation/VAR_018888
http://togogenome.org/gene/9606:PSMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJT2|||http://purl.uniprot.org/uniprot/B4DXW9|||http://purl.uniprot.org/uniprot/Q5QPM7|||http://purl.uniprot.org/uniprot/Q92530                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization.|||Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-83.|||Abolishes interaction with FBXO7, but has no effect on homodimerization; when associated with E-90.|||Asymmetric dimethylarginine|||Disordered|||Important for homodimerization and interaction with FBXO7|||N-acetylalanine|||Omega-N-methylarginine|||PI31 proteasome regulator C-terminal|||PI31 proteasome regulator N-terminal|||Phosphoserine|||Pro residues|||Proteasome inhibitor PI31 subunit|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220920|||http://purl.uniprot.org/annotation/VAR_022153|||http://purl.uniprot.org/annotation/VAR_024564
http://togogenome.org/gene/9606:PLXNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIW2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with an autosomal dominant neurodevelopmental disorder; unknown pathological significance.|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||In DWOPNED.|||In DWOPNED; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Plexin-A1|||Probable disease-associated variant found in a patient with an autosomal dominant neurodevelopmental disorder.|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232745|||http://purl.uniprot.org/annotation/VAR_087499|||http://purl.uniprot.org/annotation/VAR_087500|||http://purl.uniprot.org/annotation/VAR_087501|||http://purl.uniprot.org/annotation/VAR_087502|||http://purl.uniprot.org/annotation/VAR_087503|||http://purl.uniprot.org/annotation/VAR_087504|||http://purl.uniprot.org/annotation/VAR_087505|||http://purl.uniprot.org/annotation/VAR_087506
http://togogenome.org/gene/9606:NDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99608|||http://purl.uniprot.org/uniprot/X5D982                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Necdin|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156740|||http://purl.uniprot.org/annotation/VAR_065889
http://togogenome.org/gene/9606:KRT84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSB2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type II cuticular Hb4|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063700|||http://purl.uniprot.org/annotation/VAR_018122|||http://purl.uniprot.org/annotation/VAR_018123|||http://purl.uniprot.org/annotation/VAR_018124|||http://purl.uniprot.org/annotation/VAR_030734|||http://purl.uniprot.org/annotation/VAR_030735
http://togogenome.org/gene/9606:WIPI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4P8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreasess interaction with ATG16L1.|||Impairs interaction with ATG16L1.|||Impairs preautophagosomal localization; when associated with T-242.|||Impairs preautophagosomal localization; when associated with T-243.|||In IDDSSA; altered autophagosome assembly shown in patient cells.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 5.|||L/FRRG motif|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat domain phosphoinositide-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051440|||http://purl.uniprot.org/annotation/VAR_082589|||http://purl.uniprot.org/annotation/VSP_016970|||http://purl.uniprot.org/annotation/VSP_016971|||http://purl.uniprot.org/annotation/VSP_016972|||http://purl.uniprot.org/annotation/VSP_016973|||http://purl.uniprot.org/annotation/VSP_016974
http://togogenome.org/gene/9606:BBS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3A9|||http://purl.uniprot.org/uniprot/Q96RK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 4 protein|||Disordered|||Found in patients with Bardet-Biedl syndrome carrying mutations in other BBS genes; uncertain pathological role.|||In BBS4.|||In a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS1; uncertain pathological role.|||In a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS12; uncertain pathological role.|||In isoform 2.|||In isoform 3.|||Interaction with PCM1|||Polar residues|||Required for localization to centrosomes|||TPR|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106263|||http://purl.uniprot.org/annotation/VAR_013170|||http://purl.uniprot.org/annotation/VAR_017049|||http://purl.uniprot.org/annotation/VAR_017050|||http://purl.uniprot.org/annotation/VAR_017051|||http://purl.uniprot.org/annotation/VAR_017052|||http://purl.uniprot.org/annotation/VAR_017053|||http://purl.uniprot.org/annotation/VAR_017054|||http://purl.uniprot.org/annotation/VAR_028722|||http://purl.uniprot.org/annotation/VAR_028723|||http://purl.uniprot.org/annotation/VAR_038894|||http://purl.uniprot.org/annotation/VAR_038895|||http://purl.uniprot.org/annotation/VAR_038896|||http://purl.uniprot.org/annotation/VAR_038897|||http://purl.uniprot.org/annotation/VAR_066287|||http://purl.uniprot.org/annotation/VAR_066288|||http://purl.uniprot.org/annotation/VAR_066289|||http://purl.uniprot.org/annotation/VSP_024410|||http://purl.uniprot.org/annotation/VSP_047507
http://togogenome.org/gene/9606:ABRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Z2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Actin-binding 1|||Actin-binding 2|||Actin-binding Rho-activating protein|||Basic and acidic residues|||Disordered|||Interaction with actin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247739
http://togogenome.org/gene/9606:SNX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAU9|||http://purl.uniprot.org/uniprot/E9PJV7|||http://purl.uniprot.org/uniprot/E9PLV3|||http://purl.uniprot.org/uniprot/Q92543                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PX|||PXA|||Polar residues|||Sorting nexin C-terminal|||Sorting nexin-19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213868|||http://purl.uniprot.org/annotation/VAR_057334|||http://purl.uniprot.org/annotation/VAR_060288|||http://purl.uniprot.org/annotation/VAR_060289|||http://purl.uniprot.org/annotation/VAR_060290|||http://purl.uniprot.org/annotation/VAR_060291|||http://purl.uniprot.org/annotation/VAR_060292|||http://purl.uniprot.org/annotation/VSP_057153|||http://purl.uniprot.org/annotation/VSP_057154|||http://purl.uniprot.org/annotation/VSP_057155
http://togogenome.org/gene/9606:CHCHD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MBW9|||http://purl.uniprot.org/uniprot/Q8WYQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  CHCH|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||In FTDALS2.|||In FTDALS2; results in disorganization of mitochondrial cristae.|||In IMMD; associated in cis with R-58 in a IMMD family; unknown pathological significance; does not affect mitochondrial structure and organization.|||In IMMD; associated in cis with S-15 in a IMMD family; causes mitochondrial fragmentation.|||In SMAJ.|||Mitochondrion|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254038|||http://purl.uniprot.org/annotation/VAR_071805|||http://purl.uniprot.org/annotation/VAR_071806|||http://purl.uniprot.org/annotation/VAR_073283|||http://purl.uniprot.org/annotation/VAR_073284|||http://purl.uniprot.org/annotation/VAR_073285
http://togogenome.org/gene/9606:AKAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RP22|||http://purl.uniprot.org/uniprot/Q13023                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein 6|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||PKA-RII subunit binding domain|||Phosphoserine|||Polar residues|||Spectrin 1|||Spectrin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064530|||http://purl.uniprot.org/annotation/VAR_028171|||http://purl.uniprot.org/annotation/VAR_028172|||http://purl.uniprot.org/annotation/VAR_028173|||http://purl.uniprot.org/annotation/VAR_028174|||http://purl.uniprot.org/annotation/VAR_028175|||http://purl.uniprot.org/annotation/VAR_028176|||http://purl.uniprot.org/annotation/VAR_035781|||http://purl.uniprot.org/annotation/VAR_035782|||http://purl.uniprot.org/annotation/VAR_035783|||http://purl.uniprot.org/annotation/VAR_035784|||http://purl.uniprot.org/annotation/VAR_050653|||http://purl.uniprot.org/annotation/VAR_050654|||http://purl.uniprot.org/annotation/VAR_050655|||http://purl.uniprot.org/annotation/VAR_050656|||http://purl.uniprot.org/annotation/VAR_050657|||http://purl.uniprot.org/annotation/VSP_054497|||http://purl.uniprot.org/annotation/VSP_054498
http://togogenome.org/gene/9606:IGFALS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35858|||http://purl.uniprot.org/uniprot/Q8TAY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In ACLSD.|||In isoform 2.|||Insulin-like growth factor-binding protein complex acid labile subunit|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020695|||http://purl.uniprot.org/annotation/PRO_5004314369|||http://purl.uniprot.org/annotation/VAR_022034|||http://purl.uniprot.org/annotation/VAR_022035|||http://purl.uniprot.org/annotation/VAR_050658|||http://purl.uniprot.org/annotation/VAR_050659|||http://purl.uniprot.org/annotation/VAR_072475|||http://purl.uniprot.org/annotation/VAR_072476|||http://purl.uniprot.org/annotation/VAR_072477|||http://purl.uniprot.org/annotation/VAR_072478|||http://purl.uniprot.org/annotation/VAR_072479|||http://purl.uniprot.org/annotation/VAR_072480|||http://purl.uniprot.org/annotation/VAR_072481|||http://purl.uniprot.org/annotation/VAR_072482|||http://purl.uniprot.org/annotation/VAR_072483|||http://purl.uniprot.org/annotation/VAR_074071|||http://purl.uniprot.org/annotation/VSP_044605
http://togogenome.org/gene/9606:GUK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16774|||http://purl.uniprot.org/uniprot/Q6IBG8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Guanylate kinase|||Guanylate kinase-like|||In isoform 2 and isoform 3.|||In isoform 3.|||Increases in kcat with GMP as substrate.|||Leads to aggregation. Increases in kcat with GMP as substrate.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170651|||http://purl.uniprot.org/annotation/VSP_043778|||http://purl.uniprot.org/annotation/VSP_047372
http://togogenome.org/gene/9606:KLHL31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H511                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 31|||N,N,N-trimethylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271035|||http://purl.uniprot.org/annotation/VAR_050050|||http://purl.uniprot.org/annotation/VAR_050051|||http://purl.uniprot.org/annotation/VAR_050052
http://togogenome.org/gene/9606:FAM83B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0W9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of interaction with EGFR. Loss of activation of EGFR.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM83B|||Required for interaction with RAF1 and for the function                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297562|||http://purl.uniprot.org/annotation/VAR_034638|||http://purl.uniprot.org/annotation/VAR_034639|||http://purl.uniprot.org/annotation/VAR_034640|||http://purl.uniprot.org/annotation/VAR_034641
http://togogenome.org/gene/9606:ZNF821                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXX1|||http://purl.uniprot.org/uniprot/A0A0C4DH12|||http://purl.uniprot.org/uniprot/O75541                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||In isoform 2.|||Polar residues|||Zinc finger protein 821                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317289|||http://purl.uniprot.org/annotation/VSP_030933
http://togogenome.org/gene/9606:MTARC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Z3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Decreased catalytic activity toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor.|||Decreased catalytic efficiency toward benzamidoxime; no effect on affinity for benzamidoxime; no effect on binding of the molybdenum cofactor.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||MOSC|||Mitochondrial amidoxime reducing component 2|||Mitochondrion|||N6-acetyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273340|||http://purl.uniprot.org/annotation/VAR_030133|||http://purl.uniprot.org/annotation/VAR_062275|||http://purl.uniprot.org/annotation/VAR_070777|||http://purl.uniprot.org/annotation/VSP_022513|||http://purl.uniprot.org/annotation/VSP_022514
http://togogenome.org/gene/9606:TBX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95935                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Engrailed homology 1 repressor|||In CAKUT2; results in decreased transcriptional repression through a dominant negative effect; does not affect nuclear localization; does not bind DNA; no effect on interaction with SIX1; no effect on interaction with TLE3.|||In CAKUT2; results in decreased transcriptional repression through a dominant negative effect; does not affect nuclear localization; no effect on DNA binding; no effect on interaction with SIX1; no effect on interaction with TLE3.|||Nuclear localization signal|||T-box|||T-box transcription factor TBX18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184446|||http://purl.uniprot.org/annotation/VAR_052263|||http://purl.uniprot.org/annotation/VAR_074629|||http://purl.uniprot.org/annotation/VAR_074630|||http://purl.uniprot.org/annotation/VAR_074631|||http://purl.uniprot.org/annotation/VAR_074632
http://togogenome.org/gene/9606:OR4K13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVS2|||http://purl.uniprot.org/uniprot/Q8NH42                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150556|||http://purl.uniprot.org/annotation/VAR_053172
http://togogenome.org/gene/9606:KRTAP5-9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26371                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184107|||http://purl.uniprot.org/annotation/VAR_053731|||http://purl.uniprot.org/annotation/VAR_053732
http://togogenome.org/gene/9606:OR1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVH4|||http://purl.uniprot.org/uniprot/Q9Y585                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150415|||http://purl.uniprot.org/annotation/VAR_022047|||http://purl.uniprot.org/annotation/VAR_034162|||http://purl.uniprot.org/annotation/VAR_034163|||http://purl.uniprot.org/annotation/VAR_062007
http://togogenome.org/gene/9606:NR4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8N6|||http://purl.uniprot.org/uniprot/P43354|||http://purl.uniprot.org/uniprot/Q53EL4                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Bipartite nuclear localization signal (NLS1)|||Disordered|||In IDLDP.|||In IDLDP; unknown pathological significance.|||In isoform 2.|||NR C4-type|||NR LBD|||Nuclear localization signal (NLS1)|||Nuclear receptor|||Nuclear receptor subfamily 4 group A member 2|||nuclear export sequence (NES1)|||nuclear export sequence (NES2)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053718|||http://purl.uniprot.org/annotation/VAR_087381|||http://purl.uniprot.org/annotation/VAR_087382|||http://purl.uniprot.org/annotation/VAR_087383|||http://purl.uniprot.org/annotation/VAR_087384|||http://purl.uniprot.org/annotation/VAR_087385|||http://purl.uniprot.org/annotation/VAR_087386|||http://purl.uniprot.org/annotation/VAR_087387|||http://purl.uniprot.org/annotation/VSP_056057
http://togogenome.org/gene/9606:COX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00403|||http://purl.uniprot.org/uniprot/U5Z487                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 2|||Cytochrome oxidase subunit II copper A binding|||Cytochrome oxidase subunit II transmembrane region profile|||Helical|||Helical; Name=I|||Helical; Name=II|||In MT-C4D; affect the stability of the COX complex.|||In colorectal cancer.|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183610|||http://purl.uniprot.org/annotation/VAR_008390|||http://purl.uniprot.org/annotation/VAR_008571|||http://purl.uniprot.org/annotation/VAR_008572|||http://purl.uniprot.org/annotation/VAR_008863|||http://purl.uniprot.org/annotation/VAR_011344|||http://purl.uniprot.org/annotation/VAR_011345|||http://purl.uniprot.org/annotation/VAR_035085
http://togogenome.org/gene/9606:MAN1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33908                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210308|||http://purl.uniprot.org/annotation/VAR_034102|||http://purl.uniprot.org/annotation/VSP_056372|||http://purl.uniprot.org/annotation/VSP_056373|||http://purl.uniprot.org/annotation/VSP_056374
http://togogenome.org/gene/9606:GMDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60547                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GDP-mannose 4,6 dehydratase|||In isoform 2.|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201705|||http://purl.uniprot.org/annotation/VSP_047324
http://togogenome.org/gene/9606:RFC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40937|||http://purl.uniprot.org/uniprot/Q59GW7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Disordered|||In isoform 2.|||N-acetylmethionine|||Replication factor C subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121751|||http://purl.uniprot.org/annotation/VAR_018749|||http://purl.uniprot.org/annotation/VSP_043067
http://togogenome.org/gene/9606:ASB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H765                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat and SOCS box protein 8|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066938
http://togogenome.org/gene/9606:SLC4A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5JJ20|||http://purl.uniprot.org/uniprot/Q9Y6R1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with CA2.|||Abolishes transporter activity.|||Abolishes transporter activity. Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; S-842 and T-844.|||Alters interaction with CA4.|||Band 3 cytoplasmic|||Basic and acidic residues|||Basic residues|||Bicarbonate transporter-like transmembrane|||CA2-binding|||Confers anion exchange activity; when associated with E-798; S-842; T-844 and R-847.|||Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; S-842 and R-847.|||Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; T-844 and R-847.|||Cytoplasmic|||Discontinuously helical|||Discontinuously helical; Name=10|||Discontinuously helical; Name=3|||Disordered|||Electrogenic sodium bicarbonate cotransporter 1|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In pRTA-OA; altered function.|||In pRTA-OA; decreased cotransporter activity; mediates electroneutral sodium/bicarbonate cotransport rather than electrogenic sodium/bicarbonate cotransport; no effect on cell membrane localization; significant loss of cotransporter activity when associated with S-530.|||In pRTA-OA; decreased cotransporter activity; no effect on localization to the basolateral membrane; significant loss of cotransporter activity when associated with S-529.|||In pRTA-OA; decreased localization to the basolateral membrane; mistargeting to the apical membrane probably explains the loss of the cotransporter activity.|||In pRTA-OA; loss of localization to the plasma membrane; the retention in the cytoplasm probably explains the loss of the cotransporter activity.|||In pRTA-OA; mistargeting and altered function.|||In pRTA-OA; mistargeting to the apical membrane and altered function.|||Interaction with CA4|||Loss of conductance regulation by cAMP; isoform 1.|||Loss of regulation by cAMP of the transporter stoichiometry. Abolishes interaction with CA2.|||Loss of regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2.|||Loss of regulation by cAMP of the transporter stoichiometry. Shifts transporter stoichiometry from 3:1 to 2:1.|||Mistargeting and altered function.|||Moderate reduction of the sodium-dependent ion transport activity.|||N-linked (GalNAc) asparagine|||No effect on regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2.|||No effect on the sodium-dependent ion transport activity.|||Partial loss of interaction with CA2.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Phosphotyrosine|||Polar residues|||Prevents membrane targeting.|||Prevents phosphorylation by PKA. Loss of regulation by cAMP of the transporter stoichiometry.|||Required for basolateral targeting|||Required for interaction with AHCYL1|||Severely reduces transporter activity.|||Severely reduces transporter activity. Confers anion exchange activity; when associated with SST-527--529-GFS; S-842; T-844 and R-847.|||Strong reduction of the sodium-dependent ion transport activity.|||Strongly reduces transporter activity.|||Targeting to apical membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079227|||http://purl.uniprot.org/annotation/VAR_024751|||http://purl.uniprot.org/annotation/VAR_024752|||http://purl.uniprot.org/annotation/VAR_024753|||http://purl.uniprot.org/annotation/VAR_024754|||http://purl.uniprot.org/annotation/VAR_024755|||http://purl.uniprot.org/annotation/VAR_024756|||http://purl.uniprot.org/annotation/VAR_071661|||http://purl.uniprot.org/annotation/VAR_071662|||http://purl.uniprot.org/annotation/VSP_016704|||http://purl.uniprot.org/annotation/VSP_016705|||http://purl.uniprot.org/annotation/VSP_016706|||http://purl.uniprot.org/annotation/VSP_016707|||http://purl.uniprot.org/annotation/VSP_016708|||http://purl.uniprot.org/annotation/VSP_041003
http://togogenome.org/gene/9606:GNGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63211                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(T) subunit gamma-T1|||Removed|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012605|||http://purl.uniprot.org/annotation/PRO_0000012606|||http://purl.uniprot.org/annotation/VAR_033949
http://togogenome.org/gene/9606:CREBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60519                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic motif|||Disordered|||Leucine-zipper|||bZIP|||cAMP-responsive element-binding protein-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318192
http://togogenome.org/gene/9606:C2orf72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCS6                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C2orf72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339300
http://togogenome.org/gene/9606:SERPINA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2W1|||http://purl.uniprot.org/uniprot/Q9UK55                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Essential for interaction with PROZ|||Heparin-binding|||Loss of inhibitory activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Protein Z-dependent protease inhibitor|||Reactive bond|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032482|||http://purl.uniprot.org/annotation/VAR_020325|||http://purl.uniprot.org/annotation/VAR_020326|||http://purl.uniprot.org/annotation/VAR_020327|||http://purl.uniprot.org/annotation/VAR_038833|||http://purl.uniprot.org/annotation/VAR_038834|||http://purl.uniprot.org/annotation/VAR_038835|||http://purl.uniprot.org/annotation/VAR_051940|||http://purl.uniprot.org/annotation/VAR_051941|||http://purl.uniprot.org/annotation/VAR_051942|||http://purl.uniprot.org/annotation/VAR_070192
http://togogenome.org/gene/9606:PGBD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||PiggyBac transposable element-derived protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288055
http://togogenome.org/gene/9606:TMEM63A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94886                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  CSC1-like protein 1|||Helical|||In HLD19; loss of mechanosensitive ion channel activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280725|||http://purl.uniprot.org/annotation/VAR_031191|||http://purl.uniprot.org/annotation/VAR_061813|||http://purl.uniprot.org/annotation/VAR_083043|||http://purl.uniprot.org/annotation/VAR_083044|||http://purl.uniprot.org/annotation/VAR_083045
http://togogenome.org/gene/9606:CDC40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60508                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In PCH15; in knockdown cells, unable to rescue higher intron retention levels and to restore normal cell viability, contrary to wild-type; reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells.|||Loss of isomerization. Can rescue splicing defects when transfected in knockout cells.|||Phosphoserine|||Polar residues|||Pre-mRNA-processing factor 17|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051142|||http://purl.uniprot.org/annotation/VAR_085515
http://togogenome.org/gene/9606:TBC1D8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQ40|||http://purl.uniprot.org/uniprot/O95759                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Disordered|||GRAM 1|||GRAM 2|||Glutamine finger|||In isoform 2.|||Rab-GAP TBC|||TBC1 domain family member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208033|||http://purl.uniprot.org/annotation/VAR_022128|||http://purl.uniprot.org/annotation/VAR_022129|||http://purl.uniprot.org/annotation/VAR_024654|||http://purl.uniprot.org/annotation/VAR_047500|||http://purl.uniprot.org/annotation/VAR_060542|||http://purl.uniprot.org/annotation/VSP_038340
http://togogenome.org/gene/9606:CDK15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q40                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 15|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085619|||http://purl.uniprot.org/annotation/VAR_042016|||http://purl.uniprot.org/annotation/VAR_042017|||http://purl.uniprot.org/annotation/VAR_042018|||http://purl.uniprot.org/annotation/VAR_042019|||http://purl.uniprot.org/annotation/VAR_042020|||http://purl.uniprot.org/annotation/VSP_023745|||http://purl.uniprot.org/annotation/VSP_038765|||http://purl.uniprot.org/annotation/VSP_047226|||http://purl.uniprot.org/annotation/VSP_059406|||http://purl.uniprot.org/annotation/VSP_059407|||http://purl.uniprot.org/annotation/VSP_059408
http://togogenome.org/gene/9606:HS3ST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y661                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 4|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085221|||http://purl.uniprot.org/annotation/VAR_069580
http://togogenome.org/gene/9606:DOC2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14183                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2 1|||C2 2|||Double C2-like domain-containing protein alpha|||In isoform 2.|||Interaction with UNC13D|||Interaction with UNC13D and DYNLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079965|||http://purl.uniprot.org/annotation/VAR_019656|||http://purl.uniprot.org/annotation/VSP_056977|||http://purl.uniprot.org/annotation/VSP_056978|||http://purl.uniprot.org/annotation/VSP_056979
http://togogenome.org/gene/9606:OTX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0D0|||http://purl.uniprot.org/uniprot/F1T0D1|||http://purl.uniprot.org/uniprot/P32243                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein OTX2|||In CPHD6; acts as a dominant inhibitor of the HESX1 gene.|||In CPHD6; unknown pathological significance; loss of transcriptional activity, when tested on bicoid binding sites; decreases transactivation mediated by the wild-type protein, when tested on bicoid binding sites; no effect on DNA-binding.|||In MCOPS5.|||In MCOPS5; does not affect the expression or nuclear localization of the protein but inhibits its DNA-binding activity as well as its transactivation capability; the protein is non-functional.|||In RDEOP.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049210|||http://purl.uniprot.org/annotation/VAR_029354|||http://purl.uniprot.org/annotation/VAR_029355|||http://purl.uniprot.org/annotation/VAR_029356|||http://purl.uniprot.org/annotation/VAR_065952|||http://purl.uniprot.org/annotation/VAR_065953|||http://purl.uniprot.org/annotation/VAR_073793|||http://purl.uniprot.org/annotation/VAR_078446|||http://purl.uniprot.org/annotation/VSP_021006
http://togogenome.org/gene/9606:RNPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In CPHD7; impairs binding to U12 and U6atac small nuclear RNAs; leads to a partial defect in the folding of RRM 2 domain and reduced stability of the full-length protein.|||In CPHD7; reduced expression due to nonsense-mediated mRNA decay; impairs binding to U12 and U6atac small nuclear RNAs.|||In isoform 2.|||Necessary for binding to m(7)G-capped U12 snRNA|||Necessary for interaction with PDCD7|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding region-containing protein 3|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311112|||http://purl.uniprot.org/annotation/VAR_081540|||http://purl.uniprot.org/annotation/VAR_081541|||http://purl.uniprot.org/annotation/VSP_053413
http://togogenome.org/gene/9606:RAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15153|||http://purl.uniprot.org/uniprot/V9H0H7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylasparagine; by botulinum toxin|||Abolishes in vitro prenylation.|||Cysteine methyl ester|||Effector region|||In IMD73A; dominant-negative mutant; binds GDP, but not GTP; inhibits oxidase activation and superoxide anion production in vitro.|||In IMD73B; gain-of-function variant; exhibits impaired GAP-mediated GTP hydrolysis, resulting in sustained GTP association and prolonged RAC2-driven activation of downstream effectors; when transfected into cells, shows increased basal reactive oxygen species production following stimulation by PMA compared to cells transfected with wild-type; increased interaction with PAK1, compared to wild-type.|||In IMD73B; unknown pathological significance; cells transfected with this variant show higher production of reactive oxygen species compared to wild-type; potential gain-of-function variant.|||In IMD73B; unknown pathological significance; increased interaction with PAK1 compared to wild-type; potential gain-of-function variant.|||In IMD73C; strong decrease in protein expression.|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230|||Ras-related C3 botulinum toxin substrate 2|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042046|||http://purl.uniprot.org/annotation/PRO_0000042047|||http://purl.uniprot.org/annotation/PRO_5004777124|||http://purl.uniprot.org/annotation/VAR_017452|||http://purl.uniprot.org/annotation/VAR_036569|||http://purl.uniprot.org/annotation/VAR_085472|||http://purl.uniprot.org/annotation/VAR_085473|||http://purl.uniprot.org/annotation/VAR_085474|||http://purl.uniprot.org/annotation/VAR_085475
http://togogenome.org/gene/9606:NNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PCX7|||http://purl.uniprot.org/uniprot/Q13423                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alanine dehydrogenase/pyridine nucleotide transhydrogenase NAD(H)-binding|||Cytoplasmic|||Helical|||In GCCD4.|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||NAD(P) transhydrogenase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001055|||http://purl.uniprot.org/annotation/VAR_068781|||http://purl.uniprot.org/annotation/VAR_068782|||http://purl.uniprot.org/annotation/VAR_068783|||http://purl.uniprot.org/annotation/VAR_068784|||http://purl.uniprot.org/annotation/VAR_068785|||http://purl.uniprot.org/annotation/VAR_068786|||http://purl.uniprot.org/annotation/VAR_068787|||http://purl.uniprot.org/annotation/VAR_068788|||http://purl.uniprot.org/annotation/VAR_068789|||http://purl.uniprot.org/annotation/VAR_068790|||http://purl.uniprot.org/annotation/VAR_068791
http://togogenome.org/gene/9606:ZFYVE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBF4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes PtdIns3P binding but has no effect on its localization to lipid droplets or its interaction with RAB18; when associated with S-654.|||Abolishes PtdIns3P binding but has no effect on its localization to lipid droplets or its interaction with RAB18; when associated with S-770.|||Disrupts its localization to lipid droplets.|||Drastically reduce PtdIns3P binding; when associated with A-617 and A-619. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738.|||Drastically reduce PtdIns3P binding; when associated with A-617 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738.|||Drastically reduce PtdIns3P binding; when associated with A-619 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738.|||Drastically reduce PtdIns3P binding; when associated with A-734 and A-736. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621.|||Drastically reduce PtdIns3P binding; when associated with A-734 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621.|||Drastically reduce PtdIns3P binding; when associated with A-736 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621.|||FYVE-type 1|||FYVE-type 2|||In isoform 2.|||In isoform 3.|||Partially restore PtdIns3P binding; when associated with R-733.|||Partially restored PtdIns3P binding; when associated with R-616.|||Required for localization in the lipid droplets|||Zinc finger FYVE domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098713|||http://purl.uniprot.org/annotation/VSP_008007|||http://purl.uniprot.org/annotation/VSP_056770
http://togogenome.org/gene/9606:BTNL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXG8|||http://purl.uniprot.org/uniprot/Q8N324                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin-like protein 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014542|||http://purl.uniprot.org/annotation/VAR_049841|||http://purl.uniprot.org/annotation/VSP_012720|||http://purl.uniprot.org/annotation/VSP_012721|||http://purl.uniprot.org/annotation/VSP_012722|||http://purl.uniprot.org/annotation/VSP_012723
http://togogenome.org/gene/9606:CMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRP2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||COX assembly mitochondrial protein 2 homolog|||Cx9C motif 1|||Cx9C motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192943|||http://purl.uniprot.org/annotation/VAR_033816
http://togogenome.org/gene/9606:POU3F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20264                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Homeobox|||In SNIBFIS.|||In SNIBFIS; mislocation in cytoplasm in addition to nuclear location; decreased transcriptional activation function; abolished homodimerization.|||In SNIBFIS; mislocation within the nucleus; decreased transcriptional activation function; decreased homodimerization.|||In SNIBFIS; no effect on nuclear location; decreased transcriptional activation function; no effect on homodimerization.|||In SNIBFIS; no effect on nuclear location; decreased transcriptional activation function; slightly decreased homodimerization.|||In SNIBFIS; no effect on nuclear location; increased transcriptional activation function; no effect on homodimerization.|||In SNIBFIS; no effect on nuclear location; no effect on transcriptional activation function; no effect on homodimerization.|||POU domain, class 3, transcription factor 3|||POU-specific|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100727|||http://purl.uniprot.org/annotation/VAR_083083|||http://purl.uniprot.org/annotation/VAR_083084|||http://purl.uniprot.org/annotation/VAR_083085|||http://purl.uniprot.org/annotation/VAR_083086|||http://purl.uniprot.org/annotation/VAR_083087|||http://purl.uniprot.org/annotation/VAR_083088|||http://purl.uniprot.org/annotation/VAR_083089|||http://purl.uniprot.org/annotation/VAR_083090|||http://purl.uniprot.org/annotation/VAR_083091
http://togogenome.org/gene/9606:VCX3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NNX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 10 AA tandem repeats of L-S-Q-E-S-[EQ]-V-E-E-P|||Basic residues|||Disordered|||Polar residues|||Variable charge X-linked protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184661
http://togogenome.org/gene/9606:TEX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYF3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SPGFX2.|||In isoform 2.|||In isoform 3.|||Testis-expressed protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296955|||http://purl.uniprot.org/annotation/VAR_034635|||http://purl.uniprot.org/annotation/VAR_034636|||http://purl.uniprot.org/annotation/VAR_073889|||http://purl.uniprot.org/annotation/VAR_073890|||http://purl.uniprot.org/annotation/VSP_027260|||http://purl.uniprot.org/annotation/VSP_027261
http://togogenome.org/gene/9606:LDB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z501|||http://purl.uniprot.org/uniprot/A0A0S2Z530|||http://purl.uniprot.org/uniprot/O75112                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In CMD1C.|||In CMD1C; unknown pathological significance.|||In MFM-ZASP.|||In MFM4.|||In isoform 2 and isoform 6.|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 4, isoform 5 and isoform 6.|||LIM domain-binding protein 3|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075767|||http://purl.uniprot.org/annotation/VAR_024008|||http://purl.uniprot.org/annotation/VAR_024009|||http://purl.uniprot.org/annotation/VAR_024010|||http://purl.uniprot.org/annotation/VAR_024011|||http://purl.uniprot.org/annotation/VAR_024012|||http://purl.uniprot.org/annotation/VAR_024013|||http://purl.uniprot.org/annotation/VAR_050146|||http://purl.uniprot.org/annotation/VAR_082846|||http://purl.uniprot.org/annotation/VAR_082847|||http://purl.uniprot.org/annotation/VAR_082848|||http://purl.uniprot.org/annotation/VAR_082849|||http://purl.uniprot.org/annotation/VAR_082850|||http://purl.uniprot.org/annotation/VAR_082851|||http://purl.uniprot.org/annotation/VAR_082852|||http://purl.uniprot.org/annotation/VAR_082853|||http://purl.uniprot.org/annotation/VAR_082854|||http://purl.uniprot.org/annotation/VAR_082855|||http://purl.uniprot.org/annotation/VAR_082856|||http://purl.uniprot.org/annotation/VAR_082857|||http://purl.uniprot.org/annotation/VAR_082858|||http://purl.uniprot.org/annotation/VSP_051897|||http://purl.uniprot.org/annotation/VSP_051898|||http://purl.uniprot.org/annotation/VSP_051899|||http://purl.uniprot.org/annotation/VSP_051900|||http://purl.uniprot.org/annotation/VSP_051901|||http://purl.uniprot.org/annotation/VSP_051902
http://togogenome.org/gene/9606:SOWAHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein SOWAHB|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317240|||http://purl.uniprot.org/annotation/VAR_048280|||http://purl.uniprot.org/annotation/VAR_059126
http://togogenome.org/gene/9606:CDH12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55289                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-12|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003791|||http://purl.uniprot.org/annotation/PRO_0000003792|||http://purl.uniprot.org/annotation/VAR_048505|||http://purl.uniprot.org/annotation/VAR_048506|||http://purl.uniprot.org/annotation/VAR_048507|||http://purl.uniprot.org/annotation/VSP_056449
http://togogenome.org/gene/9606:MORC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHJ4|||http://purl.uniprot.org/uniprot/Q14149|||http://purl.uniprot.org/uniprot/Q4VBZ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  About threefold increase in catalytic activity.|||CW-type|||Diffuse nuclear localization, possibly due to loss of DNA or nucleosome binding.|||Diffuse nuclear localization. Fails to form nuclear bodies in the presence of ATP.|||Disordered|||Fails to localize to PML nuclear bodies and activate TP53.|||Forms nuclear bodies, but rapidly diffuses throughout the nucleus under conditions of ATP depletion.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Loss of sumoylation; when associated with R-597; R-650; R-651 and R-740.|||Loss of sumoylation; when associated with R-597; R-650; R-651 and R-794.|||Loss of sumoylation; when associated with R-597; R-650; R-740 and R-794.|||Loss of sumoylation; when associated with R-597; R-651; R-740 and R-794.|||Loss of sumoylation; when associated with R-650; R-651; R-740 and R-794.|||MORC family CW-type zinc finger protein 3|||Nuclear matrix binding|||Phosphoserine|||Polar residues|||RNA binding|||Strong decrease of binding to NS1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096538
http://togogenome.org/gene/9606:TDRD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ19                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||RRM|||Tudor|||Tudor domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270754|||http://purl.uniprot.org/annotation/VAR_029817|||http://purl.uniprot.org/annotation/VAR_029818|||http://purl.uniprot.org/annotation/VSP_022216
http://togogenome.org/gene/9606:DMRTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor A2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333772
http://togogenome.org/gene/9606:PLEKHA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2H5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pleckstrin homology domain-containing family A member 6|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053884|||http://purl.uniprot.org/annotation/VAR_037145|||http://purl.uniprot.org/annotation/VAR_037146
http://togogenome.org/gene/9606:TCF21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43680                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||Transcription factor 21|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127464
http://togogenome.org/gene/9606:TAOK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL54                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of kinase activity. In isoform 1, excluded from the nucleus. No effect on microtubule-binding.|||Loss of kinase activity; No effect on MAP3K7-mediated activation of NF-kappa-B.|||No effect on kinase activity, nor on JNK activation, but severe reduction in nuclear localization and apoptotic membrane blebbing.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086733|||http://purl.uniprot.org/annotation/VSP_015967|||http://purl.uniprot.org/annotation/VSP_015968|||http://purl.uniprot.org/annotation/VSP_015969|||http://purl.uniprot.org/annotation/VSP_015970|||http://purl.uniprot.org/annotation/VSP_044894
http://togogenome.org/gene/9606:BATF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV37|||http://purl.uniprot.org/uniprot/Q8N1L9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic leucine zipper transcriptional factor ATF-like 2|||Basic motif|||Disordered|||In isoform 2.|||Leucine-zipper|||Polar residues|||Pro residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288681|||http://purl.uniprot.org/annotation/VAR_048443|||http://purl.uniprot.org/annotation/VSP_025752
http://togogenome.org/gene/9606:DHX57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P158                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||DEVH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Putative ATP-dependent RNA helicase DHX57|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233151|||http://purl.uniprot.org/annotation/VAR_033861|||http://purl.uniprot.org/annotation/VAR_052190|||http://purl.uniprot.org/annotation/VAR_052191|||http://purl.uniprot.org/annotation/VSP_018056|||http://purl.uniprot.org/annotation/VSP_018057|||http://purl.uniprot.org/annotation/VSP_018058|||http://purl.uniprot.org/annotation/VSP_018059|||http://purl.uniprot.org/annotation/VSP_018060
http://togogenome.org/gene/9606:DNAJC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3W2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DPH-type MB|||DnaJ homolog subfamily C member 24|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||J|||Loss of iron-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082622|||http://purl.uniprot.org/annotation/VAR_036397|||http://purl.uniprot.org/annotation/VSP_056274
http://togogenome.org/gene/9606:ODR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SWX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein odr-4 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304683|||http://purl.uniprot.org/annotation/VAR_035059|||http://purl.uniprot.org/annotation/VSP_028098|||http://purl.uniprot.org/annotation/VSP_028099|||http://purl.uniprot.org/annotation/VSP_028100|||http://purl.uniprot.org/annotation/VSP_044478
http://togogenome.org/gene/9606:KIDINS220                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULH0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In SINO; no effect on protein abundance.|||In SINO; no effect on protein abundance; no effect on subcellular localization.|||In VENARG.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KAP NTPase|||Kinase D-interacting substrate of 220 kDa|||Mediates interaction with CRKL|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322119|||http://purl.uniprot.org/annotation/VAR_039399|||http://purl.uniprot.org/annotation/VAR_039400|||http://purl.uniprot.org/annotation/VAR_048285|||http://purl.uniprot.org/annotation/VAR_077995|||http://purl.uniprot.org/annotation/VAR_077996|||http://purl.uniprot.org/annotation/VAR_086218|||http://purl.uniprot.org/annotation/VSP_031861|||http://purl.uniprot.org/annotation/VSP_031862|||http://purl.uniprot.org/annotation/VSP_031863|||http://purl.uniprot.org/annotation/VSP_031864|||http://purl.uniprot.org/annotation/VSP_031865|||http://purl.uniprot.org/annotation/VSP_031866|||http://purl.uniprot.org/annotation/VSP_031867
http://togogenome.org/gene/9606:TAS2R41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59536                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 41                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082295|||http://purl.uniprot.org/annotation/VAR_060211
http://togogenome.org/gene/9606:DKK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I1W660|||http://purl.uniprot.org/uniprot/O94907                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand                                                                                  ^@                                                                                  DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf N-terminal cysteine-rich|||Dickkopf-related protein 1|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007218|||http://purl.uniprot.org/annotation/PRO_5003653433
http://togogenome.org/gene/9606:SESN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58005                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C-terminal domain; mediates TORC1 regulation|||Cysteine sulfenic acid (-SOH) intermediate|||In isoform 2.|||In isoform 3.|||N-terminal domain; may mediate the alkylhydroperoxide reductase activity|||Sestrin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221183|||http://purl.uniprot.org/annotation/VAR_051958|||http://purl.uniprot.org/annotation/VAR_051959|||http://purl.uniprot.org/annotation/VSP_006063|||http://purl.uniprot.org/annotation/VSP_006064|||http://purl.uniprot.org/annotation/VSP_054563|||http://purl.uniprot.org/annotation/VSP_054564
http://togogenome.org/gene/9606:PDE4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43849|||http://purl.uniprot.org/uniprot/P78505|||http://purl.uniprot.org/uniprot/Q08493|||http://purl.uniprot.org/uniprot/Q32MM7|||http://purl.uniprot.org/uniprot/Q7KYS4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform PDE4C2.|||In isoform PDE4C3.|||PDEase|||Phosphoserine|||Polar residues|||Pro residues|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 4C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198811|||http://purl.uniprot.org/annotation/VAR_034374|||http://purl.uniprot.org/annotation/VAR_050473|||http://purl.uniprot.org/annotation/VAR_050474|||http://purl.uniprot.org/annotation/VAR_061497|||http://purl.uniprot.org/annotation/VSP_004574|||http://purl.uniprot.org/annotation/VSP_004575
http://togogenome.org/gene/9606:CFAP65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYZ8|||http://purl.uniprot.org/uniprot/B4DZ05|||http://purl.uniprot.org/uniprot/Q6ZU64                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abnormal spindle-like microcephaly-associated protein ASH|||Acidic residues|||Basic and acidic residues|||Cilia- and flagella-associated protein 65|||Disordered|||Helical|||In SPGF40.|||In SPGF40; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||MSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288805|||http://purl.uniprot.org/annotation/VAR_032500|||http://purl.uniprot.org/annotation/VAR_050726|||http://purl.uniprot.org/annotation/VAR_050727|||http://purl.uniprot.org/annotation/VAR_050728|||http://purl.uniprot.org/annotation/VAR_080903|||http://purl.uniprot.org/annotation/VAR_083169|||http://purl.uniprot.org/annotation/VAR_083170|||http://purl.uniprot.org/annotation/VAR_083171|||http://purl.uniprot.org/annotation/VAR_083172|||http://purl.uniprot.org/annotation/VAR_083173|||http://purl.uniprot.org/annotation/VAR_083174|||http://purl.uniprot.org/annotation/VAR_083656|||http://purl.uniprot.org/annotation/VAR_083657|||http://purl.uniprot.org/annotation/VSP_045221|||http://purl.uniprot.org/annotation/VSP_045222|||http://purl.uniprot.org/annotation/VSP_045223|||http://purl.uniprot.org/annotation/VSP_055631|||http://purl.uniprot.org/annotation/VSP_055632|||http://purl.uniprot.org/annotation/VSP_055633
http://togogenome.org/gene/9606:DMAC2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99766                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase subunit s, mitochondrial|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Mitochondrion|||N-terminal domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002538|||http://purl.uniprot.org/annotation/VAR_060296|||http://purl.uniprot.org/annotation/VSP_040059|||http://purl.uniprot.org/annotation/VSP_040060|||http://purl.uniprot.org/annotation/VSP_040061|||http://purl.uniprot.org/annotation/VSP_040062
http://togogenome.org/gene/9606:DPH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8W6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Diphthine--ammonia ligase|||In isoform 2.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282397|||http://purl.uniprot.org/annotation/VAR_031403|||http://purl.uniprot.org/annotation/VAR_031404|||http://purl.uniprot.org/annotation/VSP_042933
http://togogenome.org/gene/9606:HTR3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXA8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 3C|||Cytoplasmic|||Disordered|||Extracellular|||HA-stretch; determines single-channel conductance in 5-HT3 receptors|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In a colorectal cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312292|||http://purl.uniprot.org/annotation/VAR_037476|||http://purl.uniprot.org/annotation/VAR_037477|||http://purl.uniprot.org/annotation/VAR_037552
http://togogenome.org/gene/9606:RTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92541                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Loss of binding to single-stranded DNA.|||Phosphoserine|||Phosphothreonine|||Plus3|||Polar residues|||RNA polymerase-associated protein RTF1 homolog|||Reduced binding to single-stranded DNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255936
http://togogenome.org/gene/9606:RHBDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEB9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Enzyme inactivation. Reduces the cleavage of BIK and TSAP6. Increases TSAP6-mediated exosome secretion.|||Enzyme inactivation. Reduces the cleavage of BIK.|||Extracellular|||Helical|||In isoform 2.|||Nucleophile|||Rhomboid-related protein 4|||Ubiquitin-binding domain (UBD)|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254189|||http://purl.uniprot.org/annotation/VAR_034454|||http://purl.uniprot.org/annotation/VSP_021203|||http://purl.uniprot.org/annotation/VSP_021204
http://togogenome.org/gene/9606:OR3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVQ3|||http://purl.uniprot.org/uniprot/P47893                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150518|||http://purl.uniprot.org/annotation/VAR_062032
http://togogenome.org/gene/9606:VSTM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXK1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Important for CDC42-dependent filopodia induction|||N-linked (GlcNAc...) asparagine|||V-set and transmembrane domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340693
http://togogenome.org/gene/9606:ATPAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5M1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase mitochondrial F1 complex assembly factor 2|||Disordered|||In MC5DN1.|||Mitochondrion|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002418|||http://purl.uniprot.org/annotation/VAR_023386
http://togogenome.org/gene/9606:PRKAA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13131                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'-AMP-activated protein kinase catalytic subunit alpha-1|||AIS|||Activates the kinase activity.|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by ULK1|||Phosphothreonine|||Phosphothreonine; by LKB1 and CaMKK2|||Phosphothreonine; by ULK1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085589|||http://purl.uniprot.org/annotation/VAR_035622|||http://purl.uniprot.org/annotation/VAR_058401|||http://purl.uniprot.org/annotation/VSP_035431
http://togogenome.org/gene/9606:WDR41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5E0|||http://purl.uniprot.org/uniprot/Q9HAD4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||No effect on interaction with SMCR8.|||Reduces interaction with the C9ORF72-SMCR8 complex; when associated with R-445. No effect on interaction with SMCR8.|||Reduces interaction with the C9ORF72-SMCR8 complex; when associated with R-449. No effect on interaction with SMCR8.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 41                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051390|||http://purl.uniprot.org/annotation/VAR_023777|||http://purl.uniprot.org/annotation/VAR_031215|||http://purl.uniprot.org/annotation/VAR_031216|||http://purl.uniprot.org/annotation/VSP_054014
http://togogenome.org/gene/9606:UQCRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07919|||http://purl.uniprot.org/uniprot/Q567R0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acidic residues|||Cytochrome b-c1 complex subunit 6, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine|||Ubiquinol-cytochrome C reductase hinge                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035990|||http://purl.uniprot.org/annotation/PRO_5014309659|||http://purl.uniprot.org/annotation/VAR_034579
http://togogenome.org/gene/9606:FRYL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2C9F2R7|||http://purl.uniprot.org/uniprot/B3KXG5|||http://purl.uniprot.org/uniprot/O94915|||http://purl.uniprot.org/uniprot/Q6ZR29                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Breakpoint for insertion to form KMT2A/MLL1-AFF4 fusion protein|||Cell morphogenesis central region|||Cell morphogenesis protein C-terminal|||Cell morphogenesis protein N-terminal|||Disordered|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein furry C-terminal|||Protein furry homolog-like|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277619|||http://purl.uniprot.org/annotation/VAR_053832|||http://purl.uniprot.org/annotation/VAR_066994|||http://purl.uniprot.org/annotation/VSP_023038|||http://purl.uniprot.org/annotation/VSP_023039
http://togogenome.org/gene/9606:ZNF677                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XU0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 677                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233997|||http://purl.uniprot.org/annotation/VAR_052889|||http://purl.uniprot.org/annotation/VAR_052890
http://togogenome.org/gene/9606:CDK20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z562|||http://purl.uniprot.org/uniprot/A0A0S2Z5B6|||http://purl.uniprot.org/uniprot/Q8IZL9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 20|||Impairs CDK2 T-160 phosphorylation and activity.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085701|||http://purl.uniprot.org/annotation/VAR_024762|||http://purl.uniprot.org/annotation/VAR_024763|||http://purl.uniprot.org/annotation/VAR_024764|||http://purl.uniprot.org/annotation/VAR_041957|||http://purl.uniprot.org/annotation/VSP_016748|||http://purl.uniprot.org/annotation/VSP_016749|||http://purl.uniprot.org/annotation/VSP_016750|||http://purl.uniprot.org/annotation/VSP_016751|||http://purl.uniprot.org/annotation/VSP_016752|||http://purl.uniprot.org/annotation/VSP_043294
http://togogenome.org/gene/9606:STEAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZX6|||http://purl.uniprot.org/uniprot/Q658P3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  2-fold increase in Km for Fe(+3).|||2.5-fold increase in Km for FAD.|||2.5-fold increase in Km for Fe(+3).|||20-fold increase in Km for FAD.|||3-fold increase in Km for FAD.|||3-fold increase in Km for Fe(+3). 5-fold increase in Km for Fe(+3); when associated with F-229.|||3-fold increase in Km for Fe(+3). 5-fold increase in Km for Fe(+3); when associated with F-319.|||5-fold increase in Km for FAD.|||Cleavage; by RHBDL4/RHBDD1|||Cytoplasmic|||Disordered|||Ferric oxidoreductase|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-256.|||Inhibits glycosylation and does not inhibit RHBDL4/RHBDD1-induced cleavage; when associated with A-344.|||Loss of ferric-chelate reductase activity and heme b-binding.|||Loss of ferric-chelate reductase activity.|||Metalloreductase STEAP3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Strongly inhibits RHBDL4/RHBDD1-induced cleavage.|||Vesicular|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285171|||http://purl.uniprot.org/annotation/VAR_031975|||http://purl.uniprot.org/annotation/VSP_024829|||http://purl.uniprot.org/annotation/VSP_024830|||http://purl.uniprot.org/annotation/VSP_024831
http://togogenome.org/gene/9606:MCIDAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RGH6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In CILD42; reduced expression; reduced number of cilia and basal bodies.|||In CILD42; reduced number of cilia and basal bodies.|||Multicilin|||Necessary and sufficient for interaction with GMNN and sufficient for homodimerization|||Necessary and sufficient for its degradation during the cell cycle|||Necessary and sufficient for proper nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411076|||http://purl.uniprot.org/annotation/VAR_071800|||http://purl.uniprot.org/annotation/VAR_071801|||http://purl.uniprot.org/annotation/VAR_083455
http://togogenome.org/gene/9606:TBC1D23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In PCH11; unknown pathological significance.|||In isoform 2.|||May mediate the interaction with C17orf75, FAM91A1 and WDR11|||May mediate the interaction with FKBP15 and WASHC2; required for endosome to Golgi trafficking|||May mediate the interaction with WASHC1|||Phosphoserine|||Phosphothreonine|||Rab-GAP TBC|||Rhodanese|||TBC1 domain family member 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287497|||http://purl.uniprot.org/annotation/VAR_080040|||http://purl.uniprot.org/annotation/VSP_025519
http://togogenome.org/gene/9606:RBM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6Q4|||http://purl.uniprot.org/uniprot/E9PGM9|||http://purl.uniprot.org/uniprot/P78332                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a non-small cell lung cancer cell line.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein 6|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081760|||http://purl.uniprot.org/annotation/VAR_014226|||http://purl.uniprot.org/annotation/VAR_052216|||http://purl.uniprot.org/annotation/VSP_045202|||http://purl.uniprot.org/annotation/VSP_057401|||http://purl.uniprot.org/annotation/VSP_057402
http://togogenome.org/gene/9606:CCDC146                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYE0|||http://purl.uniprot.org/uniprot/Q96MS1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Coiled-coil domain-containing protein 146|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317252|||http://purl.uniprot.org/annotation/VAR_050742|||http://purl.uniprot.org/annotation/VAR_061583|||http://purl.uniprot.org/annotation/VAR_061584|||http://purl.uniprot.org/annotation/VSP_030926|||http://purl.uniprot.org/annotation/VSP_030927
http://togogenome.org/gene/9606:MRPS24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EL2                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Mitochondrion|||Small ribosomal subunit protein uS3m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273066|||http://purl.uniprot.org/annotation/VAR_030077
http://togogenome.org/gene/9606:MFSD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKY6|||http://purl.uniprot.org/uniprot/Q8NBP5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||Major facilitator superfamily (MFS) profile|||Major facilitator superfamily domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305025|||http://purl.uniprot.org/annotation/VAR_035152|||http://purl.uniprot.org/annotation/VAR_035153|||http://purl.uniprot.org/annotation/VAR_035966|||http://purl.uniprot.org/annotation/VAR_035967|||http://purl.uniprot.org/annotation/VAR_061383
http://togogenome.org/gene/9606:GLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06280|||http://purl.uniprot.org/uniprot/Q53Y83                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha galactosidase A C-terminal beta-sandwich|||Alpha-galactosidase|||Alpha-galactosidase A|||Decreased enzyme activity.|||Does not affect enzyme activity.|||In FD.|||In FD; atypical.|||In FD; atypical; loss of enzyme activity.|||In FD; decreased alpha-galactosidase activity.|||In FD; decreased enzyme activity.|||In FD; does not affect enzyme function.|||In FD; has 15% of wild-type activity.|||In FD; has 36% of wild-type activity.|||In FD; has 4% of wild-type activity.|||In FD; has 42% of wild-type activity.|||In FD; has 46% of wild-type activity.|||In FD; has 52% of wild-type activity.|||In FD; has 6% of wild-type activity.|||In FD; has no enzyme activity.|||In FD; loss of enzyme activity.|||In FD; mild.|||In FD; mild; does not significantly affect the enzyme activity but the mutant protein levels are decreased presumably in the ER of the cells.|||In FD; mild; loss of enzyme activity.|||In FD; severe.|||In FD; severe; with facial telangiectasias.|||In FD; unknown pathological significance.|||In FD; unknown pathological significance; decreased enzyme activity.|||In RNA edited version.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001004|||http://purl.uniprot.org/annotation/PRO_5014309532|||http://purl.uniprot.org/annotation/VAR_000431|||http://purl.uniprot.org/annotation/VAR_000432|||http://purl.uniprot.org/annotation/VAR_000433|||http://purl.uniprot.org/annotation/VAR_000434|||http://purl.uniprot.org/annotation/VAR_000435|||http://purl.uniprot.org/annotation/VAR_000436|||http://purl.uniprot.org/annotation/VAR_000437|||http://purl.uniprot.org/annotation/VAR_000438|||http://purl.uniprot.org/annotation/VAR_000439|||http://purl.uniprot.org/annotation/VAR_000440|||http://purl.uniprot.org/annotation/VAR_000441|||http://purl.uniprot.org/annotation/VAR_000442|||http://purl.uniprot.org/annotation/VAR_000443|||http://purl.uniprot.org/annotation/VAR_000444|||http://purl.uniprot.org/annotation/VAR_000445|||http://purl.uniprot.org/annotation/VAR_000446|||http://purl.uniprot.org/annotation/VAR_000447|||http://purl.uniprot.org/annotation/VAR_000448|||http://purl.uniprot.org/annotation/VAR_000449|||http://purl.uniprot.org/annotation/VAR_000450|||http://purl.uniprot.org/annotation/VAR_000451|||http://purl.uniprot.org/annotation/VAR_000452|||http://purl.uniprot.org/annotation/VAR_000453|||http://purl.uniprot.org/annotation/VAR_000454|||http://purl.uniprot.org/annotation/VAR_000455|||http://purl.uniprot.org/annotation/VAR_000456|||http://purl.uniprot.org/annotation/VAR_000457|||http://purl.uniprot.org/annotation/VAR_000458|||http://purl.uniprot.org/annotation/VAR_000459|||http://purl.uniprot.org/annotation/VAR_000460|||http://purl.uniprot.org/annotation/VAR_000461|||http://purl.uniprot.org/annotation/VAR_000462|||http://purl.uniprot.org/annotation/VAR_000463|||http://purl.uniprot.org/annotation/VAR_000464|||http://purl.uniprot.org/annotation/VAR_000465|||http://purl.uniprot.org/annotation/VAR_000466|||http://purl.uniprot.org/annotation/VAR_000467|||http://purl.uniprot.org/annotation/VAR_000468|||http://purl.uniprot.org/annotation/VAR_000469|||http://purl.uniprot.org/annotation/VAR_000470|||http://purl.uniprot.org/annotation/VAR_000471|||http://purl.uniprot.org/annotation/VAR_000472|||http://purl.uniprot.org/annotation/VAR_000473|||http://purl.uniprot.org/annotation/VAR_000474|||http://purl.uniprot.org/annotation/VAR_000475|||http://purl.uniprot.org/annotation/VAR_000476|||http://purl.uniprot.org/annotation/VAR_000477|||http://purl.uniprot.org/annotation/VAR_000478|||http://purl.uniprot.org/annotation/VAR_000479|||http://purl.uniprot.org/annotation/VAR_000480|||http://purl.uniprot.org/annotation/VAR_000481|||http://purl.uniprot.org/annotation/VAR_000482|||http://purl.uniprot.org/annotation/VAR_000483|||http://purl.uniprot.org/annotation/VAR_000484|||http://purl.uniprot.org/annotation/VAR_000485|||http://purl.uniprot.org/annotation/VAR_000486|||http://purl.uniprot.org/annotation/VAR_000487|||http://purl.uniprot.org/annotation/VAR_000488|||http://purl.uniprot.org/annotation/VAR_000489|||http://purl.uniprot.org/annotation/VAR_000490|||http://purl.uniprot.org/annotation/VAR_000491|||http://purl.uniprot.org/annotation/VAR_000492|||http://purl.uniprot.org/annotation/VAR_000493|||http://purl.uniprot.org/annotation/VAR_000494|||http://purl.uniprot.org/annotation/VAR_012362|||http://purl.uniprot.org/annotation/VAR_012363|||http://purl.uniprot.org/annotation/VAR_012364|||http://purl.uniprot.org/annotation/VAR_012365|||http://purl.uniprot.org/annotation/VAR_012366|||http://purl.uniprot.org/annotation/VAR_012367|||http://purl.uniprot.org/annotation/VAR_012368|||http://purl.uniprot.org/annotation/VAR_012369|||http://purl.uniprot.org/annotation/VAR_012370|||http://purl.uniprot.org/annotation/VAR_012371|||http://purl.uniprot.org/annotation/VAR_012372|||http://purl.uniprot.org/annotation/VAR_012373|||http://purl.uniprot.org/annotation/VAR_012374|||http://purl.uniprot.org/annotation/VAR_012375|||http://purl.uniprot.org/annotation/VAR_012376|||http://purl.uniprot.org/annotation/VAR_012377|||http://purl.uniprot.org/annotation/VAR_012378|||http://purl.uniprot.org/annotation/VAR_012379|||http://purl.uniprot.org/annotation/VAR_012380|||http://purl.uniprot.org/annotation/VAR_012381|||http://purl.uniprot.org/annotation/VAR_012382|||http://purl.uniprot.org/annotation/VAR_012383|||http://purl.uniprot.org/annotation/VAR_012384|||http://purl.uniprot.org/annotation/VAR_012385|||http://purl.uniprot.org/annotation/VAR_012386|||http://purl.uniprot.org/annotation/VAR_012387|||http://purl.uniprot.org/annotation/VAR_012388|||http://purl.uniprot.org/annotation/VAR_012389|||http://purl.uniprot.org/annotation/VAR_012390|||http://purl.uniprot.org/annotation/VAR_012391|||http://purl.uniprot.org/annotation/VAR_012392|||http://purl.uniprot.org/annotation/VAR_012393|||http://purl.uniprot.org/annotation/VAR_012394|||http://purl.uniprot.org/annotation/VAR_012395|||http://purl.uniprot.org/annotation/VAR_012396|||http://purl.uniprot.org/annotation/VAR_012397|||http://purl.uniprot.org/annotation/VAR_012398|||http://purl.uniprot.org/annotation/VAR_012399|||http://purl.uniprot.org/annotation/VAR_012400|||http://purl.uniprot.org/annotation/VAR_012401|||http://purl.uniprot.org/annotation/VAR_012402|||http://purl.uniprot.org/annotation/VAR_012403|||http://purl.uniprot.org/annotation/VAR_012404|||http://purl.uniprot.org/annotation/VAR_012405|||http://purl.uniprot.org/annotation/VAR_012406|||http://purl.uniprot.org/annotation/VAR_012407|||http://purl.uniprot.org/annotation/VAR_012408|||http://purl.uniprot.org/annotation/VAR_012409|||http://purl.uniprot.org/annotation/VAR_012410|||http://purl.uniprot.org/annotation/VAR_012411|||http://purl.uniprot.org/annotation/VAR_012412|||http://purl.uniprot.org/annotation/VAR_012413|||http://purl.uniprot.org/annotation/VAR_012414|||http://purl.uniprot.org/annotation/VAR_012415|||http://purl.uniprot.org/annotation/VAR_012416|||http://purl.uniprot.org/annotation/VAR_012418|||http://purl.uniprot.org/annotation/VAR_012419|||http://purl.uniprot.org/annotation/VAR_012420|||http://purl.uniprot.org/annotation/VAR_012421|||http://purl.uniprot.org/annotation/VAR_012422|||http://purl.uniprot.org/annotation/VAR_012423|||http://purl.uniprot.org/annotation/VAR_012424|||http://purl.uniprot.org/annotation/VAR_012425|||http://purl.uniprot.org/annotation/VAR_012426|||http://purl.uniprot.org/annotation/VAR_012427|||http://purl.uniprot.org/annotation/VAR_012429|||http://purl.uniprot.org/annotation/VAR_012430|||http://purl.uniprot.org/annotation/VAR_012431|||http://purl.uniprot.org/annotation/VAR_012432|||http://purl.uniprot.org/annotation/VAR_012433|||http://purl.uniprot.org/annotation/VAR_012434|||http://purl.uniprot.org/annotation/VAR_012435|||http://purl.uniprot.org/annotation/VAR_012436|||http://purl.uniprot.org/annotation/VAR_012437|||http://purl.uniprot.org/annotation/VAR_012438|||http://purl.uniprot.org/annotation/VAR_012439|||http://purl.uniprot.org/annotation/VAR_012440|||http://purl.uniprot.org/annotation/VAR_012441|||http://purl.uniprot.org/annotation/VAR_032290|||http://purl.uniprot.org/annotation/VAR_032291|||http://purl.uniprot.org/annotation/VAR_032292|||http://purl.uniprot.org/annotation/VAR_032293|||http://purl.uniprot.org/annotation/VAR_062550|||http://purl.uniprot.org/annotation/VAR_062551|||http://purl.uniprot.org/annotation/VAR_062552|||http://purl.uniprot.org/annotation/VAR_062553|||http://purl.uniprot.org/annotation/VAR_062554|||http://purl.uniprot.org/annotation/VAR_062555|||http://purl.uniprot.org/annotation/VAR_062556|||http://purl.uniprot.org/annotation/VAR_062557|||http://purl.uniprot.org/annotation/VAR_062558|||http://purl.uniprot.org/annotation/VAR_062559|||http://purl.uniprot.org/annotation/VAR_062560|||http://purl.uniprot.org/annotation/VAR_062561|||http://purl.uniprot.org/annotation/VAR_062562|||http://purl.uniprot.org/annotation/VAR_062563|||http://purl.uniprot.org/annotation/VAR_062564|||http://purl.uniprot.org/annotation/VAR_062565|||http://purl.uniprot.org/annotation/VAR_062566|||http://purl.uniprot.org/annotation/VAR_062567|||http://purl.uniprot.org/annotation/VAR_062568|||http://purl.uniprot.org/annotation/VAR_062569|||http://purl.uniprot.org/annotation/VAR_062570|||http://purl.uniprot.org/annotation/VAR_062571|||http://purl.uniprot.org/annotation/VAR_076478|||http://purl.uniprot.org/annotation/VAR_077365|||http://purl.uniprot.org/annotation/VAR_077366|||http://purl.uniprot.org/annotation/VAR_077367|||http://purl.uniprot.org/annotation/VAR_077368|||http://purl.uniprot.org/annotation/VAR_077369|||http://purl.uniprot.org/annotation/VAR_077370|||http://purl.uniprot.org/annotation/VAR_077371|||http://purl.uniprot.org/annotation/VAR_077372|||http://purl.uniprot.org/annotation/VAR_077373|||http://purl.uniprot.org/annotation/VAR_077374|||http://purl.uniprot.org/annotation/VAR_077375|||http://purl.uniprot.org/annotation/VAR_077376|||http://purl.uniprot.org/annotation/VAR_077377|||http://purl.uniprot.org/annotation/VAR_077378|||http://purl.uniprot.org/annotation/VAR_077379|||http://purl.uniprot.org/annotation/VAR_077380|||http://purl.uniprot.org/annotation/VAR_077381|||http://purl.uniprot.org/annotation/VAR_077382|||http://purl.uniprot.org/annotation/VAR_077383|||http://purl.uniprot.org/annotation/VAR_077384|||http://purl.uniprot.org/annotation/VAR_077385|||http://purl.uniprot.org/annotation/VAR_077386|||http://purl.uniprot.org/annotation/VAR_077387|||http://purl.uniprot.org/annotation/VAR_077388|||http://purl.uniprot.org/annotation/VAR_077389|||http://purl.uniprot.org/annotation/VAR_077390|||http://purl.uniprot.org/annotation/VAR_077391|||http://purl.uniprot.org/annotation/VAR_077392|||http://purl.uniprot.org/annotation/VAR_077393|||http://purl.uniprot.org/annotation/VAR_077394|||http://purl.uniprot.org/annotation/VAR_077395|||http://purl.uniprot.org/annotation/VAR_077396|||http://purl.uniprot.org/annotation/VAR_077397|||http://purl.uniprot.org/annotation/VAR_077398|||http://purl.uniprot.org/annotation/VAR_077399|||http://purl.uniprot.org/annotation/VAR_077400|||http://purl.uniprot.org/annotation/VAR_077401|||http://purl.uniprot.org/annotation/VAR_077402|||http://purl.uniprot.org/annotation/VAR_077403|||http://purl.uniprot.org/annotation/VAR_077404|||http://purl.uniprot.org/annotation/VAR_077405|||http://purl.uniprot.org/annotation/VAR_077406|||http://purl.uniprot.org/annotation/VAR_077407|||http://purl.uniprot.org/annotation/VAR_077408|||http://purl.uniprot.org/annotation/VAR_077409|||http://purl.uniprot.org/annotation/VAR_077410|||http://purl.uniprot.org/annotation/VAR_077411|||http://purl.uniprot.org/annotation/VAR_077412|||http://purl.uniprot.org/annotation/VAR_077413|||http://purl.uniprot.org/annotation/VAR_077414|||http://purl.uniprot.org/annotation/VAR_077415|||http://purl.uniprot.org/annotation/VAR_077416|||http://purl.uniprot.org/annotation/VAR_077417|||http://purl.uniprot.org/annotation/VAR_077418|||http://purl.uniprot.org/annotation/VAR_077419|||http://purl.uniprot.org/annotation/VAR_077420|||http://purl.uniprot.org/annotation/VAR_077421
http://togogenome.org/gene/9606:TP63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4N5|||http://purl.uniprot.org/uniprot/A0A0S2Z4N6|||http://purl.uniprot.org/uniprot/A0A141PNN3|||http://purl.uniprot.org/uniprot/A0A141PNN4|||http://purl.uniprot.org/uniprot/B7Z8X6|||http://purl.uniprot.org/uniprot/C9D7D0|||http://purl.uniprot.org/uniprot/Q9H3D4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination.|||Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-59.|||Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-62.|||Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-59 and A-62.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In ADULT syndrome.|||In ADULT syndrome; confers novel transcription activation capacity on isoform 6.|||In AEC.|||In EEC3 and RHS; does not decrease the transcriptional activity of the isoform 5 on a TP53 reporter system but disrupts the dominant-negative activity of isoform 2 and isoform 5 on the transcriptional activity of TP53.|||In EEC3 and SHFM4.|||In EEC3.|||In EEC3; abolishes transcription activation.|||In LMS.|||In OFC8.|||In POF21.|||In POF21; results in increased transcriptional activation in luciferase reporter assays.|||In POF21; results in increased transcriptional activation in luciferase reporter assays; affects oligomerization.|||In POF21; results in increased transcriptional activation in luciferase reporter assays; affects oligomerization; when expressed in mice, it results in accelerated oocyte loss via apoptosis.|||In POF21; unknown pathological significance; no effect on transcriptional activation in a luciferase reporter assay; does not affect oligomerization.|||In POF21; unknown pathological significance; results in increased transcriptional activation in a luciferase reporter assay; affects oligomerization.|||In RHS.|||In SHFM4.|||In cervical cancer.|||In colon cancer.|||In head and neck cancer.|||In isoform 11 and isoform 12.|||In isoform 2, isoform 4, isoform 6, isoform 8, isoform 10 and isoform 12.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7 and isoform 8.|||In isoform 9 and isoform 10.|||In lung carcinoma; somatic mutation.|||In ovarian cancer.|||Increased transcriptional activation in a luciferase reporter assay.|||Interaction with HIPK2|||No effect on transcriptional activation in a luciferase reporter assay.|||Oligomerization|||Polar residues|||SAM|||Transactivation inhibition|||Transcription activation|||Tumor protein 63|||p53 DNA-binding|||p53 tetramerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185729|||http://purl.uniprot.org/annotation/VAR_020866|||http://purl.uniprot.org/annotation/VAR_020867|||http://purl.uniprot.org/annotation/VAR_020868|||http://purl.uniprot.org/annotation/VAR_020869|||http://purl.uniprot.org/annotation/VAR_020870|||http://purl.uniprot.org/annotation/VAR_020871|||http://purl.uniprot.org/annotation/VAR_020872|||http://purl.uniprot.org/annotation/VAR_020873|||http://purl.uniprot.org/annotation/VAR_020874|||http://purl.uniprot.org/annotation/VAR_020875|||http://purl.uniprot.org/annotation/VAR_020876|||http://purl.uniprot.org/annotation/VAR_020877|||http://purl.uniprot.org/annotation/VAR_020878|||http://purl.uniprot.org/annotation/VAR_020879|||http://purl.uniprot.org/annotation/VAR_020880|||http://purl.uniprot.org/annotation/VAR_020881|||http://purl.uniprot.org/annotation/VAR_032736|||http://purl.uniprot.org/annotation/VAR_032737|||http://purl.uniprot.org/annotation/VAR_032738|||http://purl.uniprot.org/annotation/VAR_032739|||http://purl.uniprot.org/annotation/VAR_032740|||http://purl.uniprot.org/annotation/VAR_032741|||http://purl.uniprot.org/annotation/VAR_032742|||http://purl.uniprot.org/annotation/VAR_032743|||http://purl.uniprot.org/annotation/VAR_032744|||http://purl.uniprot.org/annotation/VAR_032745|||http://purl.uniprot.org/annotation/VAR_032746|||http://purl.uniprot.org/annotation/VAR_032747|||http://purl.uniprot.org/annotation/VAR_032748|||http://purl.uniprot.org/annotation/VAR_035126|||http://purl.uniprot.org/annotation/VAR_035127|||http://purl.uniprot.org/annotation/VAR_035128|||http://purl.uniprot.org/annotation/VAR_035129|||http://purl.uniprot.org/annotation/VAR_035130|||http://purl.uniprot.org/annotation/VAR_082924|||http://purl.uniprot.org/annotation/VAR_082925|||http://purl.uniprot.org/annotation/VAR_082926|||http://purl.uniprot.org/annotation/VAR_082927|||http://purl.uniprot.org/annotation/VAR_082928|||http://purl.uniprot.org/annotation/VAR_082929|||http://purl.uniprot.org/annotation/VAR_088375|||http://purl.uniprot.org/annotation/VAR_088376|||http://purl.uniprot.org/annotation/VAR_088377|||http://purl.uniprot.org/annotation/VAR_088378|||http://purl.uniprot.org/annotation/VAR_088379|||http://purl.uniprot.org/annotation/VAR_088380|||http://purl.uniprot.org/annotation/VAR_088381|||http://purl.uniprot.org/annotation/VAR_088382|||http://purl.uniprot.org/annotation/VAR_088383|||http://purl.uniprot.org/annotation/VAR_088384|||http://purl.uniprot.org/annotation/VAR_088385|||http://purl.uniprot.org/annotation/VAR_088386|||http://purl.uniprot.org/annotation/VSP_012465|||http://purl.uniprot.org/annotation/VSP_012466|||http://purl.uniprot.org/annotation/VSP_012467|||http://purl.uniprot.org/annotation/VSP_012468|||http://purl.uniprot.org/annotation/VSP_012469|||http://purl.uniprot.org/annotation/VSP_012470
http://togogenome.org/gene/9606:AFMID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HM1                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  HGGXW|||In isoform 2.|||Kynurenine formamidase|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248308|||http://purl.uniprot.org/annotation/VSP_038002
http://togogenome.org/gene/9606:SEC14L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3Z8|||http://purl.uniprot.org/uniprot/O76054                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||GOLD|||In isoform 2.|||In isoform 3.|||N6-succinyllysine|||SEC14-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210755|||http://purl.uniprot.org/annotation/VAR_024626|||http://purl.uniprot.org/annotation/VSP_042021|||http://purl.uniprot.org/annotation/VSP_045880
http://togogenome.org/gene/9606:FGD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z493|||http://purl.uniprot.org/uniprot/B7Z8F9|||http://purl.uniprot.org/uniprot/E9PJX4|||http://purl.uniprot.org/uniprot/F8W1R0|||http://purl.uniprot.org/uniprot/Q49A55|||http://purl.uniprot.org/uniprot/Q96M96                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Actin filament-binding|||Basic and acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 4|||FYVE-type|||In CMT4H.|||In CMT4H; found in patient's fibroblasts but absent from peripheral nerve where splicing defects and aberrant transcripts are detected.|||In isoform 2.|||In isoform 3.|||PH|||PH 1|||PH 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080947|||http://purl.uniprot.org/annotation/VAR_034957|||http://purl.uniprot.org/annotation/VAR_044321|||http://purl.uniprot.org/annotation/VSP_013078|||http://purl.uniprot.org/annotation/VSP_013079|||http://purl.uniprot.org/annotation/VSP_013080|||http://purl.uniprot.org/annotation/VSP_013081|||http://purl.uniprot.org/annotation/VSP_013082
http://togogenome.org/gene/9606:HNF4G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8Q4|||http://purl.uniprot.org/uniprot/Q14541                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Hepatocyte nuclear factor 4-gamma|||In isoform 2.|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053562|||http://purl.uniprot.org/annotation/VAR_009704|||http://purl.uniprot.org/annotation/VSP_037691
http://togogenome.org/gene/9606:SEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60896                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  26S proteasome complex subunit SEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122961|||http://purl.uniprot.org/annotation/VAR_012003
http://togogenome.org/gene/9606:PCBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61457                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In HPABH4D; increased proteolytic degradation; loss of HNF1B interaction; loss of HNF1B-coactivator activity.|||In HPABH4D; increased proteolytic degradation; reduced dehydratase activity; no impact on hydroxytetrahydrobiopterin-binding; reduced interaction with HNF1B; partial impact on HNF1B-coactivator activity.|||In HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity.|||In HPABH4D; when associated in cis with 27-E--T-104 del; unknown pathological significance; no impact on HNF1B interaction; no impact on HNF1B-coactivator activity.|||In HPABH4D; when associated in cis with Q-88; reduced protein levels; loss of HNF1B interaction; loss of HNF1B-coactivator activity.|||N-acetylalanine|||Pterin-4-alpha-carbinolamine dehydratase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063052|||http://purl.uniprot.org/annotation/VAR_005527|||http://purl.uniprot.org/annotation/VAR_005528|||http://purl.uniprot.org/annotation/VAR_005529|||http://purl.uniprot.org/annotation/VAR_005530|||http://purl.uniprot.org/annotation/VAR_084829|||http://purl.uniprot.org/annotation/VAR_084830|||http://purl.uniprot.org/annotation/VAR_084831
http://togogenome.org/gene/9606:KRTAP15-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI76                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 15-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223917|||http://purl.uniprot.org/annotation/VAR_047019
http://togogenome.org/gene/9606:PNPLA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41247                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DGA/G|||GXSXG|||In isoform 2.|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 4|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058460|||http://purl.uniprot.org/annotation/VAR_028068|||http://purl.uniprot.org/annotation/VAR_028069|||http://purl.uniprot.org/annotation/VAR_028070|||http://purl.uniprot.org/annotation/VAR_053816|||http://purl.uniprot.org/annotation/VSP_043089
http://togogenome.org/gene/9606:RALY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GL6|||http://purl.uniprot.org/uniprot/Q9UKM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Epitope (recognized by BKRF1 antibodies)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 1.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding protein Raly|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081746|||http://purl.uniprot.org/annotation/VAR_015223|||http://purl.uniprot.org/annotation/VAR_015224|||http://purl.uniprot.org/annotation/VAR_052215|||http://purl.uniprot.org/annotation/VSP_005804
http://togogenome.org/gene/9606:MMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08253                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  72 kDa type IV collagenase|||Activation peptide|||Collagen-binding|||Collagenase-like 1|||Collagenase-like 2|||Cysteine switch|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-II 3|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In MONA.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PEX|||Required for inhibitor TIMP2 binding|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028714|||http://purl.uniprot.org/annotation/PRO_0000028715|||http://purl.uniprot.org/annotation/PRO_0000391626|||http://purl.uniprot.org/annotation/VAR_020616|||http://purl.uniprot.org/annotation/VAR_020617|||http://purl.uniprot.org/annotation/VAR_032423|||http://purl.uniprot.org/annotation/VAR_032424|||http://purl.uniprot.org/annotation/VAR_032425|||http://purl.uniprot.org/annotation/VAR_036136|||http://purl.uniprot.org/annotation/VAR_036137|||http://purl.uniprot.org/annotation/VAR_036138|||http://purl.uniprot.org/annotation/VAR_054996|||http://purl.uniprot.org/annotation/VSP_044631|||http://purl.uniprot.org/annotation/VSP_045704
http://togogenome.org/gene/9606:DNAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Dynein axonemal intermediate chain 2|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114659|||http://purl.uniprot.org/annotation/VAR_033880|||http://purl.uniprot.org/annotation/VAR_061140|||http://purl.uniprot.org/annotation/VSP_036541
http://togogenome.org/gene/9606:ZC2HC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9B8|||http://purl.uniprot.org/uniprot/Q96GY0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC/C3H-type 1|||C2HC/C3H-type 2|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger C2HC domain-containing protein 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280246|||http://purl.uniprot.org/annotation/VAR_031102
http://togogenome.org/gene/9606:BOD1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYS8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Biorientation of chromosomes in cell division protein 1-like 2|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187033
http://togogenome.org/gene/9606:PPIL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PPIase cyclophilin-type|||Probable inactive peptidyl-prolyl cis-trans isomerase-like 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263755|||http://purl.uniprot.org/annotation/VAR_029620|||http://purl.uniprot.org/annotation/VSP_043036|||http://purl.uniprot.org/annotation/VSP_055658
http://togogenome.org/gene/9606:TUBGCP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RT7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 27 AA tandem repeats|||Disordered|||Gamma-tubulin complex component 6|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078131|||http://purl.uniprot.org/annotation/VAR_031594|||http://purl.uniprot.org/annotation/VAR_055852|||http://purl.uniprot.org/annotation/VAR_055853|||http://purl.uniprot.org/annotation/VAR_055854|||http://purl.uniprot.org/annotation/VAR_055855|||http://purl.uniprot.org/annotation/VAR_055856|||http://purl.uniprot.org/annotation/VAR_055857|||http://purl.uniprot.org/annotation/VAR_055858|||http://purl.uniprot.org/annotation/VSP_001624|||http://purl.uniprot.org/annotation/VSP_017208|||http://purl.uniprot.org/annotation/VSP_017209
http://togogenome.org/gene/9606:UHRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVR3|||http://purl.uniprot.org/uniprot/Q96T88                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity.|||Abolishes ability to bind hemimethylated DNA.|||Abolishes binding to histone H3.|||Abolishes specificity to hemimethylated DNA.|||Basic and acidic residues|||Decreased ability to bind DNA.|||Decreased affinity for DNA.|||Decreased binding to methylated DNA but does not affect ability to bind DNA.|||Diminishes phosphorylation by PKA.|||Disordered|||Disrupts the simultaneous binding to H3R2me0 and H3K9me3.|||Does not affect ability to bind DNA.|||Does not affect ability to bind histone H3 peptide.|||E3 ubiquitin-protein ligase UHRF1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone H3K4me0 binding|||Histone H3R2me0 binding|||Impaired binding to histone H3 without affecting the protein folding; when associated with A-142.|||Impaired binding to histone H3 without affecting the protein folding; when associated with A-153.|||Impaired binding to histone H3.|||In isoform 2.|||Linker|||Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability.|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on in vitro phosphorylation by PKA.|||PHD-type|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PKA|||Polar residues|||Prevents phosphorylation by CDK1 during M phase, leading to increased stability.|||RING-type|||Required for affinity and specificity for 5-mCpG sequence|||Required for formation of a 5-methylcytosine-binding pocket|||Required to confer preferential recognition of cytosine over thymine|||Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA|||Required to promote base flipping|||Slightly impaired binding to histone H3.|||Tudor-like 1|||Tudor-like 2|||Ubiquitin-like|||YDG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056144|||http://purl.uniprot.org/annotation/VAR_022554|||http://purl.uniprot.org/annotation/VAR_022555|||http://purl.uniprot.org/annotation/VAR_022556|||http://purl.uniprot.org/annotation/VAR_022557|||http://purl.uniprot.org/annotation/VAR_022558|||http://purl.uniprot.org/annotation/VSP_044394
http://togogenome.org/gene/9606:FAM120AOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T036                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein FAM120AOS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337248|||http://purl.uniprot.org/annotation/VAR_043677|||http://purl.uniprot.org/annotation/VAR_043678
http://togogenome.org/gene/9606:CD209                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R907|||http://purl.uniprot.org/uniprot/B4E2A8|||http://purl.uniprot.org/uniprot/M0R0P0|||http://purl.uniprot.org/uniprot/Q9NNX6|||http://purl.uniprot.org/uniprot/X6RB12                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X approximate tandem repeats|||C-type lectin|||CD209 antigen|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 11.|||In isoform 12.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 10, isoform 11 and isoform 12.|||In isoform 6, isoform 10, isoform 11 and isoform 12.|||In isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9.|||Loss of antigen internalization by endocytosis.|||Loss of binding to ICAM3 and HIV-1 gp120.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046595|||http://purl.uniprot.org/annotation/VAR_036689|||http://purl.uniprot.org/annotation/VAR_036690|||http://purl.uniprot.org/annotation/VAR_050104|||http://purl.uniprot.org/annotation/VAR_050105|||http://purl.uniprot.org/annotation/VSP_010037|||http://purl.uniprot.org/annotation/VSP_010038|||http://purl.uniprot.org/annotation/VSP_010039|||http://purl.uniprot.org/annotation/VSP_010040|||http://purl.uniprot.org/annotation/VSP_010041|||http://purl.uniprot.org/annotation/VSP_010042|||http://purl.uniprot.org/annotation/VSP_010043|||http://purl.uniprot.org/annotation/VSP_010044|||http://purl.uniprot.org/annotation/VSP_010047|||http://purl.uniprot.org/annotation/VSP_010048|||http://purl.uniprot.org/annotation/VSP_010049|||http://purl.uniprot.org/annotation/VSP_010050
http://togogenome.org/gene/9606:UGGT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D90|||http://purl.uniprot.org/uniprot/Q9NYU1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Glucosyltransferase|||In isoform 2.|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Prevents secretion from ER|||UDP-glucose:glycoprotein glucosyltransferase 2|||UGGT thioredoxin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012274|||http://purl.uniprot.org/annotation/PRO_5004164605|||http://purl.uniprot.org/annotation/VAR_030006|||http://purl.uniprot.org/annotation/VAR_030007|||http://purl.uniprot.org/annotation/VAR_030008|||http://purl.uniprot.org/annotation/VAR_055849|||http://purl.uniprot.org/annotation/VAR_055850|||http://purl.uniprot.org/annotation/VAR_055851|||http://purl.uniprot.org/annotation/VAR_061196|||http://purl.uniprot.org/annotation/VAR_061197|||http://purl.uniprot.org/annotation/VSP_056319|||http://purl.uniprot.org/annotation/VSP_056320
http://togogenome.org/gene/9606:TRIM45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8W5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Mutagenesis Site|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||E3 ubiquitin-protein ligase TRIM45|||Filamin|||In isoform 2.|||Loss of ubiquitination activity; when associated with A-94.|||Loss of ubiquitination activity; when associated with A-97.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056266|||http://purl.uniprot.org/annotation/VAR_019931|||http://purl.uniprot.org/annotation/VAR_019932|||http://purl.uniprot.org/annotation/VAR_019933|||http://purl.uniprot.org/annotation/VAR_044128|||http://purl.uniprot.org/annotation/VSP_012000
http://togogenome.org/gene/9606:NOL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRF4|||http://purl.uniprot.org/uniprot/B4DLW2|||http://purl.uniprot.org/uniprot/O94818                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleolar protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096935|||http://purl.uniprot.org/annotation/VSP_010080|||http://purl.uniprot.org/annotation/VSP_043344|||http://purl.uniprot.org/annotation/VSP_045836
http://togogenome.org/gene/9606:FAM53B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14153                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Protein FAM53B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189544|||http://purl.uniprot.org/annotation/VSP_009932|||http://purl.uniprot.org/annotation/VSP_009933
http://togogenome.org/gene/9606:IRS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P084|||http://purl.uniprot.org/uniprot/Q9Y4H2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IRS-type PTB|||Insulin receptor substrate 2|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by INSR|||Polar residues|||Pro residues|||YXXM motif 1|||YXXM motif 2|||YXXM motif 3|||YXXM motif 4|||YXXM motif 5|||YXXM motif 6|||YXXM motif 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084239|||http://purl.uniprot.org/annotation/VAR_014857|||http://purl.uniprot.org/annotation/VAR_021557|||http://purl.uniprot.org/annotation/VAR_021558|||http://purl.uniprot.org/annotation/VAR_033992|||http://purl.uniprot.org/annotation/VAR_033993
http://togogenome.org/gene/9606:SIMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRM7|||http://purl.uniprot.org/uniprot/Q8NDZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with CTBP1|||Interaction with SLF2|||Loss of interaction with SMC6; when associated with A-477, K-480 and K-481.|||Loss of interaction with SMC6; when associated with D-473, A-477 and K-480.|||Loss of interaction with SMC6; when associated with D-473, A-477 and K-481.|||Loss of interaction with SMC6; when associated with D-473, K-480 and K-481.|||NSE5-like domain|||Polar residues|||Required for inhibition of CAPN3 protease activity|||SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates|||SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates|||SUMO-interacting motif-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250581|||http://purl.uniprot.org/annotation/VAR_027568|||http://purl.uniprot.org/annotation/VAR_027569|||http://purl.uniprot.org/annotation/VAR_027570|||http://purl.uniprot.org/annotation/VAR_059603|||http://purl.uniprot.org/annotation/VSP_020671|||http://purl.uniprot.org/annotation/VSP_020672|||http://purl.uniprot.org/annotation/VSP_020673|||http://purl.uniprot.org/annotation/VSP_020674|||http://purl.uniprot.org/annotation/VSP_020675|||http://purl.uniprot.org/annotation/VSP_020676|||http://purl.uniprot.org/annotation/VSP_020677|||http://purl.uniprot.org/annotation/VSP_060886
http://togogenome.org/gene/9606:KRTAP3-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||3 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185167
http://togogenome.org/gene/9606:CD69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07108|||http://purl.uniprot.org/uniprot/Q53ZX0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Disordered|||Early activation antigen CD69|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046583
http://togogenome.org/gene/9606:TGM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95932                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SCA35; decreased protein stability.|||In SCA35; decreased transglutaminase activity; decreased protein stability.|||In SCA35; impairs transglutaminase activity.|||In isoform 2.|||Protein-glutamine gamma-glutamyltransferase 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213715|||http://purl.uniprot.org/annotation/VAR_013250|||http://purl.uniprot.org/annotation/VAR_065360|||http://purl.uniprot.org/annotation/VAR_065361|||http://purl.uniprot.org/annotation/VAR_072179|||http://purl.uniprot.org/annotation/VAR_072180|||http://purl.uniprot.org/annotation/VAR_072181|||http://purl.uniprot.org/annotation/VAR_080737|||http://purl.uniprot.org/annotation/VSP_015103|||http://purl.uniprot.org/annotation/VSP_015104
http://togogenome.org/gene/9606:RNF112                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  GB1/RHD3-type G|||Helical|||In isoform 2.|||Interaction with ZBTB16|||RING finger protein 112|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056301|||http://purl.uniprot.org/annotation/VSP_042377
http://togogenome.org/gene/9606:AKR1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04828                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value.|||70-fold decrease in progesterone reduction. No effect on DHT reduction.|||Aldo-keto reductase family 1 member C1|||Important for substrate specificity|||Lowers pKa of active site Tyr|||Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH.|||Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH.|||May be involved in the mediating step between the transformation of progesterone and the release of the cofactor|||No effect on progesterone reduction.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124633|||http://purl.uniprot.org/annotation/VAR_048214|||http://purl.uniprot.org/annotation/VAR_048215
http://togogenome.org/gene/9606:TMEM255A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JRV8|||http://purl.uniprot.org/uniprot/Q7Z4S8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Transmembrane protein 255A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266037|||http://purl.uniprot.org/annotation/VAR_029637|||http://purl.uniprot.org/annotation/VSP_021920|||http://purl.uniprot.org/annotation/VSP_021921|||http://purl.uniprot.org/annotation/VSP_046825|||http://purl.uniprot.org/annotation/VSP_046826
http://togogenome.org/gene/9606:MAT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP2|||http://purl.uniprot.org/uniprot/Q9NZL9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Methionine adenosyltransferase 2 subunit beta|||Phosphothreonine|||Removed|||Required for interaction with MAT2A|||RmlD-like substrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287520|||http://purl.uniprot.org/annotation/VAR_032318|||http://purl.uniprot.org/annotation/VSP_025534|||http://purl.uniprot.org/annotation/VSP_025535|||http://purl.uniprot.org/annotation/VSP_025536|||http://purl.uniprot.org/annotation/VSP_025537|||http://purl.uniprot.org/annotation/VSP_025538|||http://purl.uniprot.org/annotation/VSP_025539|||http://purl.uniprot.org/annotation/VSP_025540
http://togogenome.org/gene/9606:ZC3HAV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2W4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding to EXOSC5|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||N-acetylalanine|||N-terminal domain|||No effect on the structural inability to bind NAD(+); when associated with N-810.|||No effect on the structural inability to bind NAD(+); when associated with Y-830.|||Nuclear export signal|||Nuclear localization signal|||PARP catalytic|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Polar residues|||Removed|||WWE|||Zinc finger CCCH-type antiviral protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211343|||http://purl.uniprot.org/annotation/VAR_018454|||http://purl.uniprot.org/annotation/VAR_018455|||http://purl.uniprot.org/annotation/VAR_018456|||http://purl.uniprot.org/annotation/VAR_054319|||http://purl.uniprot.org/annotation/VSP_010268|||http://purl.uniprot.org/annotation/VSP_010269|||http://purl.uniprot.org/annotation/VSP_010270|||http://purl.uniprot.org/annotation/VSP_010271
http://togogenome.org/gene/9606:OR9Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGQ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150683|||http://purl.uniprot.org/annotation/VAR_053260
http://togogenome.org/gene/9606:SPINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00995                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  In PCTT and TCP; associated with disease susceptibility; risk factor also for acute pancreatitis; may confer susceptibility to fibrocalculous pancreatic diabetes.|||In PCTT.|||In PCTT; benign variant.|||Kazal-like|||Necessary for sperm binding|||Reactive bond for trypsin|||Serine protease inhibitor Kazal-type 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016557|||http://purl.uniprot.org/annotation/VAR_011688|||http://purl.uniprot.org/annotation/VAR_011689|||http://purl.uniprot.org/annotation/VAR_011690|||http://purl.uniprot.org/annotation/VAR_032011|||http://purl.uniprot.org/annotation/VAR_032012
http://togogenome.org/gene/9606:GPRC5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z831|||http://purl.uniprot.org/uniprot/Q9NZH0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor family C group 5 member B|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012965|||http://purl.uniprot.org/annotation/VSP_047585
http://togogenome.org/gene/9606:COX17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14061                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Strand                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cytochrome c oxidase copper chaperone|||Disordered|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213538
http://togogenome.org/gene/9606:TSPAN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVV6|||http://purl.uniprot.org/uniprot/O14817                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219241|||http://purl.uniprot.org/annotation/VAR_036616
http://togogenome.org/gene/9606:INPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49441                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Frequency not significantly different between lithium-treated bipolar patients and healthy controls.|||Inositol polyphosphate 1-phosphatase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142510|||http://purl.uniprot.org/annotation/VAR_019669|||http://purl.uniprot.org/annotation/VAR_049599
http://togogenome.org/gene/9606:KYAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K563|||http://purl.uniprot.org/uniprot/B7Z4W5|||http://purl.uniprot.org/uniprot/Q16773                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminotransferase class I/classII|||Disordered|||In isoform 2.|||In isoform 3.|||Kynurenine--oxoglutarate transaminase 1|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123942|||http://purl.uniprot.org/annotation/VSP_009875|||http://purl.uniprot.org/annotation/VSP_009876|||http://purl.uniprot.org/annotation/VSP_009877
http://togogenome.org/gene/9606:FXYD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0Q3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FXYD domain-containing ion transport regulator 6|||Helical|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010372|||http://purl.uniprot.org/annotation/VSP_045996
http://togogenome.org/gene/9606:PSG11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ72                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014918|||http://purl.uniprot.org/annotation/VAR_056076|||http://purl.uniprot.org/annotation/VAR_060365|||http://purl.uniprot.org/annotation/VAR_061325|||http://purl.uniprot.org/annotation/VAR_061326|||http://purl.uniprot.org/annotation/VSP_007876
http://togogenome.org/gene/9606:PLEKHM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWE6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PH 1|||PH 2|||Phorbol-ester/DAG-type|||Phosphoserine|||Pleckstrin homology domain-containing family M member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326034|||http://purl.uniprot.org/annotation/VSP_032511|||http://purl.uniprot.org/annotation/VSP_032512|||http://purl.uniprot.org/annotation/VSP_032513
http://togogenome.org/gene/9606:SLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6Q3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to membranes.|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-myristoyl glycine|||Polar residues|||Removed|||SH2|||SH3|||SLA C-terminal|||Src-like-adapter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022351|||http://purl.uniprot.org/annotation/VAR_051361|||http://purl.uniprot.org/annotation/VSP_007240|||http://purl.uniprot.org/annotation/VSP_007241|||http://purl.uniprot.org/annotation/VSP_018794
http://togogenome.org/gene/9606:ACTL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H568                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Actin-like protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286171|||http://purl.uniprot.org/annotation/VAR_032079|||http://purl.uniprot.org/annotation/VAR_032080
http://togogenome.org/gene/9606:THBD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07204                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||C-type lectin|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6; calcium-binding|||Extracellular|||Helical|||Improved overall glycosaminoglycan attachment, likely due to improved xylosyltransferase acceptor consensus sequence around Ser-492.|||In AHUS6.|||In AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation.|||In THPH12 and AHUS6; cells transfected with the mutant are less effective in converting C3b to iC3b on the cell surface after complement activation.|||Involved in alpha-L/beta-2 and alpha-M/beta-2 integrin binding|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Reduced glycosaminoglycan attachment.|||Thrombomodulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007771|||http://purl.uniprot.org/annotation/VAR_011368|||http://purl.uniprot.org/annotation/VAR_011369|||http://purl.uniprot.org/annotation/VAR_011370|||http://purl.uniprot.org/annotation/VAR_011371|||http://purl.uniprot.org/annotation/VAR_011372|||http://purl.uniprot.org/annotation/VAR_011373|||http://purl.uniprot.org/annotation/VAR_049011|||http://purl.uniprot.org/annotation/VAR_063223|||http://purl.uniprot.org/annotation/VAR_063224|||http://purl.uniprot.org/annotation/VAR_063673|||http://purl.uniprot.org/annotation/VAR_063674
http://togogenome.org/gene/9606:CFAP418                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NL8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 418|||Disordered|||In CORD16 and BBS21; does not affect interaction with FAM161A..|||In RP64; does not affect interaction with FAM161A..|||Required for interaction with FAM161A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271058|||http://purl.uniprot.org/annotation/VAR_033683|||http://purl.uniprot.org/annotation/VAR_067305|||http://purl.uniprot.org/annotation/VAR_067306
http://togogenome.org/gene/9606:RNF145                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9Y9|||http://purl.uniprot.org/uniprot/Q8NDT8|||http://purl.uniprot.org/uniprot/Q96MT1                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||RING finger protein 145|||RING-type|||RING-type; atypical|||YLYF motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294024|||http://purl.uniprot.org/annotation/VSP_037501|||http://purl.uniprot.org/annotation/VSP_043661|||http://purl.uniprot.org/annotation/VSP_043662|||http://purl.uniprot.org/annotation/VSP_044539
http://togogenome.org/gene/9606:SKIDA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1XH10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Polar residues|||SKI/DACH domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328529|||http://purl.uniprot.org/annotation/VSP_059383
http://togogenome.org/gene/9606:ECH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13011                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial|||Important for catalytic activity|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007417|||http://purl.uniprot.org/annotation/VAR_014927|||http://purl.uniprot.org/annotation/VAR_033913
http://togogenome.org/gene/9606:SPHK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53ZR5|||http://purl.uniprot.org/uniprot/Q9NYA1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CIB1.|||DAGKc|||In isoform 2.|||In isoform 3.|||Loss of binding to negatively charged membranes, diffuse cytosolic distribution.|||Loss of enzyme activity.|||Nuclear export signal 1|||Nuclear export signal 2|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor|||Sphingosine kinase 1|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181357|||http://purl.uniprot.org/annotation/VAR_082919|||http://purl.uniprot.org/annotation/VSP_035453|||http://purl.uniprot.org/annotation/VSP_047078
http://togogenome.org/gene/9606:IFT70B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4P2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Intraflagellar transport protein 70B|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333201|||http://purl.uniprot.org/annotation/VAR_043124|||http://purl.uniprot.org/annotation/VAR_043125
http://togogenome.org/gene/9606:GPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD30                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alanine aminotransferase 2|||Disordered|||In NEDSPM; loss of function mutation.|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247532|||http://purl.uniprot.org/annotation/VAR_073379|||http://purl.uniprot.org/annotation/VSP_020008
http://togogenome.org/gene/9606:CTSF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBX1                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin F|||In CLN13.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026202|||http://purl.uniprot.org/annotation/PRO_0000026203|||http://purl.uniprot.org/annotation/VAR_051513|||http://purl.uniprot.org/annotation/VAR_070159|||http://purl.uniprot.org/annotation/VAR_070160|||http://purl.uniprot.org/annotation/VAR_070161|||http://purl.uniprot.org/annotation/VAR_070162
http://togogenome.org/gene/9606:NRDE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7Z3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||Loss of interaction with MTREX associated with decreased RNAs stability; when associated with A-163; A-187 and E-189.|||Loss of interaction with MTREX associated with decreased RNAs stability; when associated with A-163; R-166 and A-187.|||Loss of interaction with MTREX associated with decreased RNAs stability; when associated with A-163; R-166 and E-189.|||Loss of interaction with MTREX associated with decreased RNAs stability; when associated with R-166; A-187 and E-189.|||MID/MTR4-interacting domain|||N-acetylalanine|||Nuclear exosome regulator NRDE2|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089907|||http://purl.uniprot.org/annotation/VAR_057813|||http://purl.uniprot.org/annotation/VAR_060343|||http://purl.uniprot.org/annotation/VAR_062239
http://togogenome.org/gene/9606:PPP1R3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7J1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  CBM21|||Disordered|||Glycogen-binding motif|||PP1-binding motif|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 3E|||Substrate-binding motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338638
http://togogenome.org/gene/9606:FEZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Engrailed homology 1 repressor|||Fez family zinc finger protein 1|||In HH22; partial loss of function.|||In isoform 2.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295114|||http://purl.uniprot.org/annotation/VAR_071918|||http://purl.uniprot.org/annotation/VSP_026732|||http://purl.uniprot.org/annotation/VSP_026733
http://togogenome.org/gene/9606:MSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35548                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Does not bind DNA but still suppresses OCFRE activation.|||Homeobox|||Homeobox protein MSX-2|||In CRS2.|||In CRS2; gain of function.|||In PFM1.|||In PFM1; loss of function.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049099|||http://purl.uniprot.org/annotation/VAR_003755|||http://purl.uniprot.org/annotation/VAR_010200|||http://purl.uniprot.org/annotation/VAR_010201|||http://purl.uniprot.org/annotation/VAR_010786|||http://purl.uniprot.org/annotation/VAR_010898|||http://purl.uniprot.org/annotation/VAR_071634
http://togogenome.org/gene/9606:MYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05976                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In CMYP14; no protein detected by western blot in patient muscle.|||In isoform MLC3.|||Myosin light chain 1/3, skeletal muscle isoform|||N,N,N-trimethylalanine|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198681|||http://purl.uniprot.org/annotation/VAR_082312|||http://purl.uniprot.org/annotation/VSP_038686
http://togogenome.org/gene/9606:ZNF625                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||Phosphotyrosine|||Polar residues|||Zinc finger protein 625                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234602|||http://purl.uniprot.org/annotation/VAR_052882|||http://purl.uniprot.org/annotation/VSP_046327
http://togogenome.org/gene/9606:H3C7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:UPK3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75631                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Found in a patient with unilateral multicystic kidney disease; unknown pathological significance.|||Found in patients with renal adysplasia; unknown pathological significance; normal targeting to the cell surface.|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Uroplakin-3a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022637|||http://purl.uniprot.org/annotation/VAR_020158|||http://purl.uniprot.org/annotation/VAR_044399|||http://purl.uniprot.org/annotation/VAR_044400|||http://purl.uniprot.org/annotation/VAR_044401|||http://purl.uniprot.org/annotation/VSP_030004
http://togogenome.org/gene/9606:ARMCX5-GPRASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-protein coupled receptor-associated sorting protein 2|||In DFNX7; requires 2 nucleotide substitutions.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239053|||http://purl.uniprot.org/annotation/VAR_049265|||http://purl.uniprot.org/annotation/VAR_081645
http://togogenome.org/gene/9606:SLC36A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2H8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||Loss amino acid:proton symporter activity. No effect on localization to the plasma membrane.|||N-linked (GlcNAc...) asparagine|||No effect on amino acid:proton symporter activity. No effect on localization to the plasma membrane.|||Polar residues|||Proton-coupled amino acid transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093825|||http://purl.uniprot.org/annotation/VAR_048122|||http://purl.uniprot.org/annotation/VSP_044390|||http://purl.uniprot.org/annotation/VSP_044391|||http://purl.uniprot.org/annotation/VSP_044392
http://togogenome.org/gene/9606:KCNH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L42                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 8|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054018|||http://purl.uniprot.org/annotation/VAR_055098|||http://purl.uniprot.org/annotation/VAR_055099|||http://purl.uniprot.org/annotation/VSP_057036|||http://purl.uniprot.org/annotation/VSP_057037|||http://purl.uniprot.org/annotation/VSP_057038|||http://purl.uniprot.org/annotation/VSP_057039
http://togogenome.org/gene/9606:SLC24A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Alpha-1|||Alpha-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium/potassium/calcium exchanger 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019370|||http://purl.uniprot.org/annotation/VAR_028024|||http://purl.uniprot.org/annotation/VAR_028025|||http://purl.uniprot.org/annotation/VAR_028026|||http://purl.uniprot.org/annotation/VAR_028027
http://togogenome.org/gene/9606:TTC7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPK7|||http://purl.uniprot.org/uniprot/G5E9G4|||http://purl.uniprot.org/uniprot/I6L9J2|||http://purl.uniprot.org/uniprot/Q9ULT0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In GIDID1.|||In GIDID1; reduced interaction with PI4KA.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 7 N-terminal|||Tetratricopeptide repeat protein 7A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106385|||http://purl.uniprot.org/annotation/VAR_016602|||http://purl.uniprot.org/annotation/VAR_052624|||http://purl.uniprot.org/annotation/VAR_069636|||http://purl.uniprot.org/annotation/VAR_075126|||http://purl.uniprot.org/annotation/VAR_075127|||http://purl.uniprot.org/annotation/VAR_075128|||http://purl.uniprot.org/annotation/VAR_075129|||http://purl.uniprot.org/annotation/VAR_075130|||http://purl.uniprot.org/annotation/VAR_075131|||http://purl.uniprot.org/annotation/VAR_075132|||http://purl.uniprot.org/annotation/VAR_075133|||http://purl.uniprot.org/annotation/VAR_075134|||http://purl.uniprot.org/annotation/VAR_075135|||http://purl.uniprot.org/annotation/VAR_075136|||http://purl.uniprot.org/annotation/VAR_075137|||http://purl.uniprot.org/annotation/VAR_075138|||http://purl.uniprot.org/annotation/VAR_075139|||http://purl.uniprot.org/annotation/VAR_075140|||http://purl.uniprot.org/annotation/VAR_075141|||http://purl.uniprot.org/annotation/VSP_039347|||http://purl.uniprot.org/annotation/VSP_039348|||http://purl.uniprot.org/annotation/VSP_057271
http://togogenome.org/gene/9606:EPHB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54762                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Disrupts interaction with GRB7 and ACP1.|||Eph LBD|||Ephrin type-B receptor 1|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a gastric adenocarcinoma sample; somatic mutation.|||In an ovarian undifferentiated carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Kinase-dead mutant. Unable to autophosphorylate, to interact with SH2 domain-containing interactors, to activate the MAPK/ERK and JUN signaling cascades. Not ubiquitinated by CBL.|||Loss of interaction with NCK1.|||Loss of interaction with SHC1 and SRC.|||Loss of interaction with SHC1.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016824|||http://purl.uniprot.org/annotation/VAR_011801|||http://purl.uniprot.org/annotation/VAR_011802|||http://purl.uniprot.org/annotation/VAR_011803|||http://purl.uniprot.org/annotation/VAR_011804|||http://purl.uniprot.org/annotation/VAR_011805|||http://purl.uniprot.org/annotation/VAR_042165|||http://purl.uniprot.org/annotation/VAR_042166|||http://purl.uniprot.org/annotation/VAR_042167|||http://purl.uniprot.org/annotation/VAR_042168|||http://purl.uniprot.org/annotation/VAR_042169|||http://purl.uniprot.org/annotation/VAR_042170|||http://purl.uniprot.org/annotation/VAR_042171|||http://purl.uniprot.org/annotation/VAR_058479|||http://purl.uniprot.org/annotation/VSP_056017|||http://purl.uniprot.org/annotation/VSP_056018|||http://purl.uniprot.org/annotation/VSP_056019
http://togogenome.org/gene/9606:ITGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05556                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CX3CL1-binding|||Cytoplasmic|||Disordered|||Does not interact with ITGB1BP1.|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Integrin beta-1|||Interaction with ITGB1BP1|||Interaction with TMEM182|||Loss of beta-1A interaction with FLNA and FLNB.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine; alternate|||No effect on cell surface location but impairs interaction with TNS3 and PEAK1.|||No effect on cell surface location but impairs interaction with TNS3 and PEAK1. Strongly reduces ITGB1BP1 binding; when associated with A-792.|||No effect on interaction with ACAP1.|||PSI|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces interaction with ACAP1.|||Reduces interaction with ITGB1BP1, but not with FERMT2 or TLN1. Inhibits fibronectin deposition and mineralized bone nodules formation.|||Signal for sorting from recycling endosomes; interaction with ACAP1|||Slightly reduces interaction with ACAP1.|||Strongly reduces ITGB1BP1 binding; when associated with A-795.|||Strongly reduces ITGB1BP1 binding; when associated with D-788.|||Strongly reduces ITGB1BP1 binding; when associated with D-790.|||Strongly reduces interaction with ACAP1 and ability to recycle; does not affect heterodimerization with ITGA5.|||VWFA|||in ADMIDAS binding site|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016334|||http://purl.uniprot.org/annotation/VSP_002741|||http://purl.uniprot.org/annotation/VSP_002742|||http://purl.uniprot.org/annotation/VSP_002743|||http://purl.uniprot.org/annotation/VSP_002744
http://togogenome.org/gene/9606:ECT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8V3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2-fold increase in GEF activity.|||BRCT 1|||BRCT 2|||Complete loss of GEF activity and failure to support cytokinesis.|||DH|||Diminishes its phosphorylation status.|||Diminishes its phosphorylation status. Reduces its interaction with PLK1 and Rho exchange activity. Does not change its subcellular localization. Does not inhibit anchorage-independent growth and invasion in cancer cells.|||Disordered|||Does not inhibit its Rho exchange activity. Increases interaction with RACGAP1. Does not inhibit anchorage-independent growth and invasion in cancer cells.|||Does not inhibit subcellular localization or homodimerization. Enhances its Rho exchange activity.|||Does not reduce its interaction with PLK1, change its subcellular localization and Rho exchange activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Inhibits activation of the transforming activity.|||Inhibits homodimerization. Increases binding with RhoA and GEF activity.|||Inhibits interaction with RACGAP1. Abolishes targeting to the central spindle.|||Inhibits its phosphorylation and anchorage-independent growth and invasion in cancer cells. Does not inhibit its GEF activity.|||Marked increase in GEF activity and rescues the cytokinesis defect caused by depletion of endogenous ECT2. When expressed in a cancer cell line, causes faster cell proliferation than the wild-type protein.|||More than 10-fold increase in GEF activity. Overexpression causes noticeable changes in interphase cell morphology such as cell rounding and formation of stress fibers, suggesting ectopic RHOA activation.|||More than 10-fold increase in GEF activity. Overexpression causes noticeable changes in interphase cell morphology such as cell rounding and formation of stress fibers, suggesting ectopic RhoA activation.|||N-acetylalanine|||No effect on GEF activity but severely decreases ECT2 activation by RHOA. Fails to rescue the cytokinesis defect caused by knockdown of endogenous ECT2 in contrast to the wild-type protein which rescues this defect.|||No effect on GEF activity but severely decreases ECT2 activation by RHOA. Localizes correctly but fails to rescue the cytokinesis defect caused by knockdown of endogenous ECT2 in contrast to the wild-type protein which rescues this defect.|||Nuclear localization signal|||PH|||Partially releases inhibition.|||Phosphoserine|||Phosphothreonine; by CDK1|||Phosphothreonine; by PKC/PRKCI|||Polar residues|||Protein ECT2|||Removed|||Shows both nuclear and cytoplasmic localization and activates its transforming activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080938|||http://purl.uniprot.org/annotation/VAR_035975|||http://purl.uniprot.org/annotation/VAR_047064|||http://purl.uniprot.org/annotation/VSP_041976|||http://purl.uniprot.org/annotation/VSP_041977|||http://purl.uniprot.org/annotation/VSP_041978
http://togogenome.org/gene/9606:ZNF30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17039                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047359|||http://purl.uniprot.org/annotation/VAR_047736|||http://purl.uniprot.org/annotation/VAR_047737|||http://purl.uniprot.org/annotation/VAR_047738|||http://purl.uniprot.org/annotation/VAR_047739|||http://purl.uniprot.org/annotation/VSP_040942|||http://purl.uniprot.org/annotation/VSP_040943|||http://purl.uniprot.org/annotation/VSP_040944
http://togogenome.org/gene/9606:C4orf51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J302                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C4orf51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392538
http://togogenome.org/gene/9606:STRA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPB8|||http://purl.uniprot.org/uniprot/Q9BX79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MCOPS9.|||In MCOPS9; also found in a family with isolated colobomatous microphthalmia; affects STRA6 cell surface expression and retinol uptake; requires 2 nucleotide substitutions.|||In MCOPS9; loss of tyrosine phosphorylation.|||In anophthalmia/microphthalmia.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with RBP1|||Loss of interaction with RBP1.|||Loss of tyrosine phosphorylation.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Receptor for retinol uptake STRA6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311228|||http://purl.uniprot.org/annotation/VAR_037168|||http://purl.uniprot.org/annotation/VAR_037169|||http://purl.uniprot.org/annotation/VAR_037170|||http://purl.uniprot.org/annotation/VAR_037171|||http://purl.uniprot.org/annotation/VAR_037172|||http://purl.uniprot.org/annotation/VAR_037173|||http://purl.uniprot.org/annotation/VAR_037174|||http://purl.uniprot.org/annotation/VAR_037175|||http://purl.uniprot.org/annotation/VAR_060203|||http://purl.uniprot.org/annotation/VAR_060204|||http://purl.uniprot.org/annotation/VAR_060205|||http://purl.uniprot.org/annotation/VAR_066849|||http://purl.uniprot.org/annotation/VSP_029437|||http://purl.uniprot.org/annotation/VSP_029438|||http://purl.uniprot.org/annotation/VSP_029439|||http://purl.uniprot.org/annotation/VSP_046776|||http://purl.uniprot.org/annotation/VSP_047497
http://togogenome.org/gene/9606:CTPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRF8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CTP synthase 2|||Disordered|||For GATase activity|||Glutamine amidotransferase type-1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247033
http://togogenome.org/gene/9606:NTN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3H6|||http://purl.uniprot.org/uniprot/B2RE43|||http://purl.uniprot.org/uniprot/Q9HB63                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||NTR|||Netrin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042116|||http://purl.uniprot.org/annotation/PRO_5002781549|||http://purl.uniprot.org/annotation/VAR_023548|||http://purl.uniprot.org/annotation/VSP_015745|||http://purl.uniprot.org/annotation/VSP_015746
http://togogenome.org/gene/9606:CAPN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC96                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-10|||Domain III 1|||Domain III 2|||In a colorectal cancer sample; somatic mutation.|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||In isoform G.|||In isoform H.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207725|||http://purl.uniprot.org/annotation/VAR_014437|||http://purl.uniprot.org/annotation/VAR_014438|||http://purl.uniprot.org/annotation/VAR_014439|||http://purl.uniprot.org/annotation/VAR_014440|||http://purl.uniprot.org/annotation/VAR_014441|||http://purl.uniprot.org/annotation/VAR_014442|||http://purl.uniprot.org/annotation/VAR_014443|||http://purl.uniprot.org/annotation/VAR_036049|||http://purl.uniprot.org/annotation/VSP_005232|||http://purl.uniprot.org/annotation/VSP_005233|||http://purl.uniprot.org/annotation/VSP_005234|||http://purl.uniprot.org/annotation/VSP_005235|||http://purl.uniprot.org/annotation/VSP_005236|||http://purl.uniprot.org/annotation/VSP_005237|||http://purl.uniprot.org/annotation/VSP_005238|||http://purl.uniprot.org/annotation/VSP_005239|||http://purl.uniprot.org/annotation/VSP_005240|||http://purl.uniprot.org/annotation/VSP_005241|||http://purl.uniprot.org/annotation/VSP_005242|||http://purl.uniprot.org/annotation/VSP_005243
http://togogenome.org/gene/9606:KCNK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDS2|||http://purl.uniprot.org/uniprot/Q9Y257                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No channel activity.|||Polar residues|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel|||Potassium channel subfamily K member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101750|||http://purl.uniprot.org/annotation/VAR_052426|||http://purl.uniprot.org/annotation/VAR_052427|||http://purl.uniprot.org/annotation/VAR_059842|||http://purl.uniprot.org/annotation/VSP_006692
http://togogenome.org/gene/9606:MFRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||FZ|||Found in a patient with high hyperopia; unknown pathological significance.|||Helical; Signal-anchor for type II membrane protein|||In NNO2.|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||Membrane frizzled-related protein|||N-linked (GlcNAc...) asparagine|||Polar residues|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228132|||http://purl.uniprot.org/annotation/VAR_025691|||http://purl.uniprot.org/annotation/VAR_025692|||http://purl.uniprot.org/annotation/VAR_025693|||http://purl.uniprot.org/annotation/VAR_025694|||http://purl.uniprot.org/annotation/VAR_025695|||http://purl.uniprot.org/annotation/VAR_025696|||http://purl.uniprot.org/annotation/VAR_071160|||http://purl.uniprot.org/annotation/VAR_075401|||http://purl.uniprot.org/annotation/VAR_075402|||http://purl.uniprot.org/annotation/VAR_075403|||http://purl.uniprot.org/annotation/VSP_055928|||http://purl.uniprot.org/annotation/VSP_055929
http://togogenome.org/gene/9606:LYPLAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWZ2                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Lysophospholipase-like protein 1|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227557|||http://purl.uniprot.org/annotation/VAR_025607|||http://purl.uniprot.org/annotation/VAR_060992|||http://purl.uniprot.org/annotation/VSP_017556
http://togogenome.org/gene/9606:STYXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3H6|||http://purl.uniprot.org/uniprot/Q9Y6J8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Confers phosphatase activity. Dephosphorylates G3BP1 at 'Ser-149'. Loss of interaction with G3BP1. Reduces arsenite-induced stress granule formation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Rhodanese|||Serine/threonine/tyrosine-interacting-like protein 1|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094837|||http://purl.uniprot.org/annotation/VSP_005175|||http://purl.uniprot.org/annotation/VSP_005176|||http://purl.uniprot.org/annotation/VSP_005177|||http://purl.uniprot.org/annotation/VSP_005178|||http://purl.uniprot.org/annotation/VSP_005179|||http://purl.uniprot.org/annotation/VSP_005180
http://togogenome.org/gene/9606:ANXA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ72                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067507|||http://purl.uniprot.org/annotation/VAR_030786
http://togogenome.org/gene/9606:HAPLN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UW8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Hyaluronan and proteoglycan link protein 4|||Ig-like C2-type|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013192
http://togogenome.org/gene/9606:GABRA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48169|||http://purl.uniprot.org/uniprot/X5D7F5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-4|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000441|||http://purl.uniprot.org/annotation/VAR_036032|||http://purl.uniprot.org/annotation/VAR_046552|||http://purl.uniprot.org/annotation/VAR_046553
http://togogenome.org/gene/9606:CLEC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNC9|||http://purl.uniprot.org/uniprot/O75596                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 3 member A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017374|||http://purl.uniprot.org/annotation/PRO_5014098589|||http://purl.uniprot.org/annotation/VAR_021259
http://togogenome.org/gene/9606:TMEM229A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXF0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Transmembrane protein 229A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000391848
http://togogenome.org/gene/9606:ACTR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H981                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-related protein 8|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089123|||http://purl.uniprot.org/annotation/VAR_028033|||http://purl.uniprot.org/annotation/VSP_040506|||http://purl.uniprot.org/annotation/VSP_040507|||http://purl.uniprot.org/annotation/VSP_040508
http://togogenome.org/gene/9606:RTN4IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWV3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In OPA10.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||Reticulon-4-interacting protein 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042114|||http://purl.uniprot.org/annotation/VAR_076369|||http://purl.uniprot.org/annotation/VSP_015742|||http://purl.uniprot.org/annotation/VSP_015743|||http://purl.uniprot.org/annotation/VSP_015744
http://togogenome.org/gene/9606:ACE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKH4|||http://purl.uniprot.org/uniprot/P12821                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished binding to chloride ion.|||Abolished dependence to chloride, leading to reduced peptidyl dipeptidase activity.|||Abolished dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394.|||Abolished dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394. Abolishes the second active site, preventing maturation of Cholecystokinin-5.|||Abolished dipeptidyl carboxypeptidase activity; when associated with 988-K--K-992. Abolished N-terminal active sites, leading to impaired ability to degrade the hemoregulatory peptide N-acetyl-SDKP (AcSDKP). In contrast, does not affect cleavage of other substrates, such as Cholecystokinin-5.|||Abolished peptidase activity, leading to increased levels of amyloid-beta; when associated with D-391.|||Abolished peptidase activity, leading to increased levels of amyloid-beta; when associated with D-989.|||Abolishes phosphorylation and decreases membrane retention.|||Angiotensin-converting enzyme|||Angiotensin-converting enzyme, soluble form|||Cleavage|||Cytoplasmic|||Decreased ability to cleave substance P and bradykinin. Reduced binding to captopril inhibitor.|||Decreased ability to cleave substance P and captopril inhibitor.|||Decreased dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394.|||Does not prevent cleavage and secretion of the soluble form, suggesting that processing can take place at different sites.|||Extracellular|||Helical|||In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-140 and D-368. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-140 and D-368. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-140 and D-368. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121 and D-368.|||In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-140 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-140 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-140 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121 and D-617.|||In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-121, D-368 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-121, D-368 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-103, D-368 and D-617.|||In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-140, D-368 and D-617. In ACE(t)g1 mutant; decreased N-glycosylation without affecting stability; when associated with D-140, D-368 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-103, D-368 and D-617.|||In ACE(t)g0 mutant; abolished N-glycosylation leading to impaired stability and degradation; when associated with D-121, D-140, D-368 and D-617. In ACE(t)g2 mutant; decreased N-glycosylation without affecting stability; when associated with D-140, D-368 and D-617. In ACE(t)g3 mutant; decreased N-glycosylation leading to impaired stability and degradation; when associated with D-121, D-368 and D-617.|||In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-318 and D-445.|||In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-318 and D-445. In Ndom1234569 mutant; does not affect dipeptidyl carboxypeptidase activity; when associated with D-318.|||In Ndom123456 mutant; abolished dipeptidyl carboxypeptidase activity; when associated with D-445 and D-509. In Ndom1234569 mutant; does not affect dipeptidyl carboxypeptidase activity; when associated with D-445.|||In isoform 4.|||In isoform Somatic-2.|||In isoform Testis-specific.|||Increased cleavage and secretion of the soluble form by generating a new cleavage site.|||Juxtamembrane stalk|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||No effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type.|||Not glycosylated|||Peptidase M2 1|||Peptidase M2 2|||Phosphoserine|||Proton acceptor 1|||Proton acceptor 2|||Proton donor 1|||Proton donor 2|||Strongly decreased dipeptidyl carboxypeptidase activity; when associated with 390-K--K-394. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028530|||http://purl.uniprot.org/annotation/PRO_0000028531|||http://purl.uniprot.org/annotation/PRO_5002803094|||http://purl.uniprot.org/annotation/VAR_011707|||http://purl.uniprot.org/annotation/VAR_011708|||http://purl.uniprot.org/annotation/VAR_011709|||http://purl.uniprot.org/annotation/VAR_014189|||http://purl.uniprot.org/annotation/VAR_014190|||http://purl.uniprot.org/annotation/VAR_014191|||http://purl.uniprot.org/annotation/VAR_014192|||http://purl.uniprot.org/annotation/VAR_020053|||http://purl.uniprot.org/annotation/VAR_023430|||http://purl.uniprot.org/annotation/VAR_023431|||http://purl.uniprot.org/annotation/VAR_023432|||http://purl.uniprot.org/annotation/VAR_023433|||http://purl.uniprot.org/annotation/VAR_023434|||http://purl.uniprot.org/annotation/VAR_029139|||http://purl.uniprot.org/annotation/VAR_029140|||http://purl.uniprot.org/annotation/VAR_029141|||http://purl.uniprot.org/annotation/VAR_029142|||http://purl.uniprot.org/annotation/VAR_034602|||http://purl.uniprot.org/annotation/VAR_035434|||http://purl.uniprot.org/annotation/VAR_054000|||http://purl.uniprot.org/annotation/VAR_054001|||http://purl.uniprot.org/annotation/VAR_074173|||http://purl.uniprot.org/annotation/VAR_082898|||http://purl.uniprot.org/annotation/VAR_082899|||http://purl.uniprot.org/annotation/VSP_029932|||http://purl.uniprot.org/annotation/VSP_029933|||http://purl.uniprot.org/annotation/VSP_035120|||http://purl.uniprot.org/annotation/VSP_035121|||http://purl.uniprot.org/annotation/VSP_054836|||http://purl.uniprot.org/annotation/VSP_054837
http://togogenome.org/gene/9606:NLRP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W24                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Increased tendency to form aggregates.|||Increased thermal stability of the Pyrin domain.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NACHT, LRR and PYD domains-containing protein 14|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080901|||http://purl.uniprot.org/annotation/VAR_024180|||http://purl.uniprot.org/annotation/VAR_031932|||http://purl.uniprot.org/annotation/VAR_031933|||http://purl.uniprot.org/annotation/VAR_031934|||http://purl.uniprot.org/annotation/VAR_031935|||http://purl.uniprot.org/annotation/VAR_031936|||http://purl.uniprot.org/annotation/VAR_031937|||http://purl.uniprot.org/annotation/VAR_031938|||http://purl.uniprot.org/annotation/VAR_031939|||http://purl.uniprot.org/annotation/VAR_031940|||http://purl.uniprot.org/annotation/VAR_031941|||http://purl.uniprot.org/annotation/VAR_031942|||http://purl.uniprot.org/annotation/VAR_031943|||http://purl.uniprot.org/annotation/VAR_031944|||http://purl.uniprot.org/annotation/VAR_036387|||http://purl.uniprot.org/annotation/VAR_053622|||http://purl.uniprot.org/annotation/VAR_053623
http://togogenome.org/gene/9606:AIDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BJ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Axin interactor, dorsalization-associated protein|||Axin-binding|||C2 Aida-type|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305277|||http://purl.uniprot.org/annotation/VSP_028322|||http://purl.uniprot.org/annotation/VSP_034661
http://togogenome.org/gene/9606:RAB4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20338                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  10-fold decrease in ZFYVE20 binding affinity.|||5-glutamyl serotonin|||Cysteine methyl ester|||Effector region|||Phosphoserine|||Phosphoserine; by CDK1|||Ras-related protein Rab-4A|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121093
http://togogenome.org/gene/9606:ARNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6P0|||http://purl.uniprot.org/uniprot/B0AZM1|||http://purl.uniprot.org/uniprot/P27540|||http://purl.uniprot.org/uniprot/Q53F30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aryl hydrocarbon receptor nuclear translocator|||BHLH|||Basic and acidic residues|||DNA-binding|||Diminishes DNA interaction.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates the transcription activity and dimerization of the AHR:ARNT complex|||N-acetylalanine|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphoserine|||Polar residues|||Removed|||Required for heterodimer formation with EPAS1|||Required for heterodimer formation with HIF1A|||Severely diminishes DNA interaction.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127118|||http://purl.uniprot.org/annotation/VAR_014819|||http://purl.uniprot.org/annotation/VAR_018906|||http://purl.uniprot.org/annotation/VAR_020189|||http://purl.uniprot.org/annotation/VAR_024280|||http://purl.uniprot.org/annotation/VSP_002092|||http://purl.uniprot.org/annotation/VSP_036532|||http://purl.uniprot.org/annotation/VSP_036533|||http://purl.uniprot.org/annotation/VSP_055030
http://togogenome.org/gene/9606:H4C7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99525                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding                                                                                  ^@                                                                                  Histone H4-like protein type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324392
http://togogenome.org/gene/9606:DDAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95865|||http://purl.uniprot.org/uniprot/V9HW53                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Chain                                                                                  ^@                                                                                  N(G),N(G)-dimethylarginine dimethylaminohydrolase 2|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171121
http://togogenome.org/gene/9606:OR2AT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWB1|||http://purl.uniprot.org/uniprot/A6NND4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AT4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310866
http://togogenome.org/gene/9606:DBT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T9W1|||http://purl.uniprot.org/uniprot/P11182                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In MSUD2.|||Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial|||Lipoyl-binding|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-lipoyllysine|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peripheral subunit-binding (PSBD)|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020489|||http://purl.uniprot.org/annotation/VAR_004978|||http://purl.uniprot.org/annotation/VAR_015099|||http://purl.uniprot.org/annotation/VAR_015100
http://togogenome.org/gene/9606:PELI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H716|||http://purl.uniprot.org/uniprot/Q9HAT8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to IRAK1.|||Abolishes binding to IRAK1; when associated with A-187.|||Abolishes binding to IRAK1; when associated with A-188.|||E3 ubiquitin-protein ligase pellino homolog 2|||FHA; atypical|||Helical|||Loss of IRAK1-polyubiquitination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194174
http://togogenome.org/gene/9606:CSHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1R0|||http://purl.uniprot.org/uniprot/A0A384N655|||http://purl.uniprot.org/uniprot/I6L999|||http://purl.uniprot.org/uniprot/Q14406                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chorionic somatomammotropin hormone-like 1|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032959|||http://purl.uniprot.org/annotation/PRO_5002092588|||http://purl.uniprot.org/annotation/PRO_5017328810|||http://purl.uniprot.org/annotation/VAR_059807|||http://purl.uniprot.org/annotation/VSP_040114|||http://purl.uniprot.org/annotation/VSP_040115|||http://purl.uniprot.org/annotation/VSP_040116
http://togogenome.org/gene/9606:UBAP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GYI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Pro residues|||UMA|||Ubiquitin-associated protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413688
http://togogenome.org/gene/9606:NOTCH2NLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3S9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Notch homolog 2 N-terminal-like protein A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337103|||http://purl.uniprot.org/annotation/VAR_043601|||http://purl.uniprot.org/annotation/VAR_043602|||http://purl.uniprot.org/annotation/VAR_043603|||http://purl.uniprot.org/annotation/VAR_043604|||http://purl.uniprot.org/annotation/VSP_033895|||http://purl.uniprot.org/annotation/VSP_033896
http://togogenome.org/gene/9606:TEKT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIF3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Tektin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184565|||http://purl.uniprot.org/annotation/VAR_034549|||http://purl.uniprot.org/annotation/VAR_053720
http://togogenome.org/gene/9606:NINL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2I6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||D-box|||Disordered|||Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 495-A--A-497.|||Disrupts binding to CDC20 and FZR1 and prevents ubiquitination and subsequent degradation of NINL; when associated with 633-A--A-636.|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||KEN box|||Ninein-like protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259714|||http://purl.uniprot.org/annotation/VAR_058509|||http://purl.uniprot.org/annotation/VAR_058510|||http://purl.uniprot.org/annotation/VAR_059700|||http://purl.uniprot.org/annotation/VAR_059701|||http://purl.uniprot.org/annotation/VAR_059702|||http://purl.uniprot.org/annotation/VAR_059703|||http://purl.uniprot.org/annotation/VAR_059704|||http://purl.uniprot.org/annotation/VAR_061688|||http://purl.uniprot.org/annotation/VAR_061689|||http://purl.uniprot.org/annotation/VSP_037883
http://togogenome.org/gene/9606:EPGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW88                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||Epigen|||Extracellular|||Helical|||In isoform 2, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 7.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045462|||http://purl.uniprot.org/annotation/VSP_036654|||http://purl.uniprot.org/annotation/VSP_036655|||http://purl.uniprot.org/annotation/VSP_036656|||http://purl.uniprot.org/annotation/VSP_036657|||http://purl.uniprot.org/annotation/VSP_036658
http://togogenome.org/gene/9606:CBX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QXZ6|||http://purl.uniprot.org/uniprot/O95503                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chromo|||Chromobox protein homolog 6|||Disordered|||Phosphoserine|||Reduced interaction with H3C15 and H3C1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080210
http://togogenome.org/gene/9606:MBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02686                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Citrulline|||Citrulline; in form C8|||Cleavage; by CTSG|||Deamidated glutamine|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4 and isoform 6.|||Induces experimental autoimmune encephalomyelitis (EAE) 1|||Induces experimental autoimmune encephalomyelitis (EAE) 2|||Myelin basic protein|||N-acetylalanine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by UHMK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Symmetric dimethylarginine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158990|||http://purl.uniprot.org/annotation/VSP_003308|||http://purl.uniprot.org/annotation/VSP_003309|||http://purl.uniprot.org/annotation/VSP_003310|||http://purl.uniprot.org/annotation/VSP_003311
http://togogenome.org/gene/9606:SF3B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUJ0|||http://purl.uniprot.org/uniprot/Q15427                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphotyrosine|||Pro residues|||RRM|||RRM 1|||RRM 2|||Removed|||Splicing factor 3B subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081955
http://togogenome.org/gene/9606:ZNF165                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49910|||http://purl.uniprot.org/uniprot/Q53Z40                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||SCAN box|||Zinc finger protein 165                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047436
http://togogenome.org/gene/9606:C17orf107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZR85                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C17orf107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342338
http://togogenome.org/gene/9606:ST3GAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V5F3|||http://purl.uniprot.org/uniprot/A0A7P0RGI5|||http://purl.uniprot.org/uniprot/Q11206|||http://purl.uniprot.org/uniprot/Q6IBE6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149262|||http://purl.uniprot.org/annotation/PRO_5014310484|||http://purl.uniprot.org/annotation/PRO_5029838108|||http://purl.uniprot.org/annotation/VSP_001784|||http://purl.uniprot.org/annotation/VSP_001785|||http://purl.uniprot.org/annotation/VSP_001786|||http://purl.uniprot.org/annotation/VSP_021104
http://togogenome.org/gene/9606:KIAA0319L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZA0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dyslexia-associated protein KIAA0319-like protein|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||MANSC|||N-linked (GlcNAc...) asparagine|||PKD 1|||PKD 2|||PKD 3|||PKD 4|||PKD 5|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329064|||http://purl.uniprot.org/annotation/VAR_042644|||http://purl.uniprot.org/annotation/VAR_042645|||http://purl.uniprot.org/annotation/VSP_032953|||http://purl.uniprot.org/annotation/VSP_032954|||http://purl.uniprot.org/annotation/VSP_032955
http://togogenome.org/gene/9606:LILRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N423                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 1, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Leukocyte immunoglobulin-like receptor subfamily B member 2|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014821|||http://purl.uniprot.org/annotation/VAR_016997|||http://purl.uniprot.org/annotation/VAR_016998|||http://purl.uniprot.org/annotation/VAR_016999|||http://purl.uniprot.org/annotation/VAR_017000|||http://purl.uniprot.org/annotation/VAR_047432|||http://purl.uniprot.org/annotation/VAR_047433|||http://purl.uniprot.org/annotation/VAR_047434|||http://purl.uniprot.org/annotation/VAR_047435|||http://purl.uniprot.org/annotation/VAR_061314|||http://purl.uniprot.org/annotation/VAR_061315|||http://purl.uniprot.org/annotation/VSP_061382|||http://purl.uniprot.org/annotation/VSP_061383|||http://purl.uniprot.org/annotation/VSP_061384|||http://purl.uniprot.org/annotation/VSP_061385
http://togogenome.org/gene/9606:FOXP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IT66|||http://purl.uniprot.org/uniprot/Q548T7|||http://purl.uniprot.org/uniprot/Q8N2P0|||http://purl.uniprot.org/uniprot/Q8TEA2|||http://purl.uniprot.org/uniprot/Q9H334                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Breakpoint for translocation to form PAX5-FOXP1|||C2H2-type|||CTBP1-binding|||Disordered|||Does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2.|||FOXP coiled-coil|||Fork-head|||Forkhead box protein P1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRLIAF; nuclear and cytoplasmic aggregation; loss of transcriptional repression activity; loss of ability to self-associate; loss of interaction with FOXP2.|||In MRLIAF; unknown pathological significance; does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||Leucine-zipper|||Likely benign variant; does not affect nuclear localization; no loss of transcriptional repression activity; no loss of ability to self-associate; no loss of interaction with FOXP2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091877|||http://purl.uniprot.org/annotation/VAR_065067|||http://purl.uniprot.org/annotation/VAR_065068|||http://purl.uniprot.org/annotation/VAR_065069|||http://purl.uniprot.org/annotation/VAR_065070|||http://purl.uniprot.org/annotation/VAR_065071|||http://purl.uniprot.org/annotation/VAR_065072|||http://purl.uniprot.org/annotation/VAR_065073|||http://purl.uniprot.org/annotation/VAR_065074|||http://purl.uniprot.org/annotation/VAR_065075|||http://purl.uniprot.org/annotation/VAR_075246|||http://purl.uniprot.org/annotation/VAR_075247|||http://purl.uniprot.org/annotation/VAR_075248|||http://purl.uniprot.org/annotation/VAR_075249|||http://purl.uniprot.org/annotation/VSP_001555|||http://purl.uniprot.org/annotation/VSP_001556|||http://purl.uniprot.org/annotation/VSP_043462|||http://purl.uniprot.org/annotation/VSP_043463|||http://purl.uniprot.org/annotation/VSP_046930|||http://purl.uniprot.org/annotation/VSP_057341
http://togogenome.org/gene/9606:TM9SF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QYR3|||http://purl.uniprot.org/uniprot/B4DH88|||http://purl.uniprot.org/uniprot/Q92544                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Phosphotyrosine|||Transmembrane 9 superfamily member|||Transmembrane 9 superfamily member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210178|||http://purl.uniprot.org/annotation/PRO_5007352952
http://togogenome.org/gene/9606:AGPAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15120                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-acyl-sn-glycerol-3-phosphate acyltransferase beta|||Cytoplasmic|||EGTR motif|||HXXXXD motif|||Helical|||In CGL1; 90% of wild-type 1-acyl-sn-glycerol-3-phosphate acyltransferase activity.|||In CGL1; reduced 1-acyl-sn-glycerol-3-phosphate acyltransferase activity.|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208192|||http://purl.uniprot.org/annotation/VAR_017325|||http://purl.uniprot.org/annotation/VAR_017326|||http://purl.uniprot.org/annotation/VAR_017327|||http://purl.uniprot.org/annotation/VAR_017328|||http://purl.uniprot.org/annotation/VSP_005071
http://togogenome.org/gene/9606:GNPAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15228                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dihydroxyacetone phosphate acyltransferase|||HXXXXD motif|||In RCDP2.|||In RCDP2; 70% reduction in activity.|||In RCDP2; complete loss of activity.|||In isoform 2.|||Microbody targeting signal|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195246|||http://purl.uniprot.org/annotation/VAR_006357|||http://purl.uniprot.org/annotation/VAR_006358|||http://purl.uniprot.org/annotation/VAR_025897|||http://purl.uniprot.org/annotation/VAR_030696|||http://purl.uniprot.org/annotation/VAR_030697|||http://purl.uniprot.org/annotation/VSP_056435
http://togogenome.org/gene/9606:RIC8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Synembryn-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235899|||http://purl.uniprot.org/annotation/VSP_018510|||http://purl.uniprot.org/annotation/VSP_018511|||http://purl.uniprot.org/annotation/VSP_018512|||http://purl.uniprot.org/annotation/VSP_018513|||http://purl.uniprot.org/annotation/VSP_039866
http://togogenome.org/gene/9606:SHOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXU9|||http://purl.uniprot.org/uniprot/Q6ZU10                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SPGF75.|||In SPGF75; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Protein shortage in chiasmata 1 ortholog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089719|||http://purl.uniprot.org/annotation/VAR_050829|||http://purl.uniprot.org/annotation/VAR_050830|||http://purl.uniprot.org/annotation/VAR_050831|||http://purl.uniprot.org/annotation/VAR_050832|||http://purl.uniprot.org/annotation/VAR_050833|||http://purl.uniprot.org/annotation/VAR_050834|||http://purl.uniprot.org/annotation/VAR_050835|||http://purl.uniprot.org/annotation/VAR_050836|||http://purl.uniprot.org/annotation/VAR_050837|||http://purl.uniprot.org/annotation/VAR_050838|||http://purl.uniprot.org/annotation/VAR_050839|||http://purl.uniprot.org/annotation/VAR_050840|||http://purl.uniprot.org/annotation/VAR_087416|||http://purl.uniprot.org/annotation/VAR_087417|||http://purl.uniprot.org/annotation/VAR_087418|||http://purl.uniprot.org/annotation/VAR_087419|||http://purl.uniprot.org/annotation/VSP_014747|||http://purl.uniprot.org/annotation/VSP_014748|||http://purl.uniprot.org/annotation/VSP_014749|||http://purl.uniprot.org/annotation/VSP_046641
http://togogenome.org/gene/9606:ZNF575                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XF7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Zinc finger protein 575                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047664
http://togogenome.org/gene/9606:GUF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N442                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  In DEE40.|||Mitochondrion|||Translation factor GUF1, mitochondrial|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256251|||http://purl.uniprot.org/annotation/VAR_028895|||http://purl.uniprot.org/annotation/VAR_028896|||http://purl.uniprot.org/annotation/VAR_077804
http://togogenome.org/gene/9606:DACT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFP1|||http://purl.uniprot.org/uniprot/Q96B18                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Dapper homolog 3|||Disordered|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264616
http://togogenome.org/gene/9606:COX5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL93|||http://purl.uniprot.org/uniprot/P10606                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 5B, mitochondrial|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006109
http://togogenome.org/gene/9606:PCDH17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14917                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004001|||http://purl.uniprot.org/annotation/VSP_021581|||http://purl.uniprot.org/annotation/VSP_021582
http://togogenome.org/gene/9606:NSA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQZ6|||http://purl.uniprot.org/uniprot/O95478|||http://purl.uniprot.org/uniprot/Q5J7U2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Phosphothreonine|||Ribosome biogenesis protein NSA2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122259|||http://purl.uniprot.org/annotation/VAR_051862
http://togogenome.org/gene/9606:INPP5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14642                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Inositol polyphosphate-5-phosphatase A|||Loss of membrane localization. No loss of enzyme activity.|||Loss of prenylation and membrane localization. No loss of enzyme activity.|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209719|||http://purl.uniprot.org/annotation/PRO_0000396780|||http://purl.uniprot.org/annotation/VAR_034006
http://togogenome.org/gene/9606:TEX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Important for interaction with piRNA|||Interaction with LIRE1|||Polar residues|||Testis-expressed protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325962
http://togogenome.org/gene/9606:EIF4E3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5X7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 4E type 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287697|||http://purl.uniprot.org/annotation/VSP_025602
http://togogenome.org/gene/9606:ST14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Y6                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In ARCI11.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Suppressor of tumorigenicity 14 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088712|||http://purl.uniprot.org/annotation/VAR_032847|||http://purl.uniprot.org/annotation/VAR_032848|||http://purl.uniprot.org/annotation/VAR_032849
http://togogenome.org/gene/9606:TLL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6L7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  CUB 1|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Peptidase M12A|||Polar residues|||Tolloid-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046036|||http://purl.uniprot.org/annotation/PRO_0000046037
http://togogenome.org/gene/9606:STX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43752                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Removed|||Required for interaction with VPS51|||Syntaxin-6|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210208|||http://purl.uniprot.org/annotation/VSP_054763
http://togogenome.org/gene/9606:TNPO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5L0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with SRSF1.|||Abolished interaction with SRSF1. In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-667, A-671, A-702, A-750 and A-751.|||Abolished interaction with SRSF1. In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-667, A-671, A-702, A-751 and A-758.|||Abolished interaction with SRSF1. In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-667, A-671, A-750, A-751 and A-758.|||Abolished interaction with SRSF1. In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-667, A-702, A-750, A-751 and A-758.|||Abolished interaction with SRSF1. In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-667, A-671, A-702, A-750, A-751 and A-758.|||Decreased interaction with GTP-bound Ran.|||In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-667, A-671, A-702, A-750 and A-758.|||In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-660, A-664, A-671, A-702, A-750, A-751 and A-758.|||In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-620, A-664, A-667, A-671, A-702, A-750, A-751 and A-758.|||In 9Ala; abolished interaction with SRSF1 and CPSF6 without affecting interaction with GTP-bound Ran; when associated with A-660, A-664, A-667, A-671, A-702, A-750, A-751 and A-758.|||In LGMDD2.|||In LGMDD2; induces relocalization to nuclear periphery; impaired ability to transport target proteins into the nucleus; induces resistance to HIV-1 infection.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Transportin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120781|||http://purl.uniprot.org/annotation/VAR_071822|||http://purl.uniprot.org/annotation/VAR_082591|||http://purl.uniprot.org/annotation/VAR_082592|||http://purl.uniprot.org/annotation/VAR_082593|||http://purl.uniprot.org/annotation/VSP_011178|||http://purl.uniprot.org/annotation/VSP_030174|||http://purl.uniprot.org/annotation/VSP_045494
http://togogenome.org/gene/9606:ZNF566                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRR6|||http://purl.uniprot.org/uniprot/Q969W8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 566                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047656|||http://purl.uniprot.org/annotation/VSP_043419
http://togogenome.org/gene/9606:CANT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVQ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect activity.|||Helical; Signal-anchor for type II membrane protein|||Important for dimer formation|||In DBQD1 and EDM7; severely affects activity.|||In DBQD1.|||In DBQD1; affects protein secretion.|||In DBQD1; affects protein stability and secretion.|||In DBQD1; severely affects activity.|||In EDM7; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Increases GDPase activity 2-fold and ADPase activity 5-fold. Forms dimer even at suboptimal Ca(2+) concentrations.|||Increases activity 5-fold.|||Interchain|||Loss of activity.|||Loss of dimer formation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on GDPase and ADPase activities. No effect on dimer formation; when associated with S-287.|||Reduces GDPase activity 1.3-fold and ADPase activity 2-fold. Severe loss of dimer formation; when associated with S-287.|||Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. No effect on dimer formation; when associated with S-287.|||Reduces GDPase activity 1.7-fold and ADPase activity 1.5-fold. Severe loss of dimer formation; when associated with S-287.|||Reduces GDPase activity 2-fold and ADPase activity 2.5-fold. No effect on dimer formation; when associated with S-287.|||Reduces GDPase and ADPase activities 1.3-fold.|||Reduces GDPase and ADPase activities 1.7-fold. Severe loss of dimer formation; when associated with S-287.|||Reduces activity by 95%.|||Reduces activity by 96%.|||Reduces activity by 98%.|||Reduces activity by 99%.|||Reduces activity by over 99.9%.|||Slightly reduced activity.|||Soluble calcium-activated nucleotidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209925|||http://purl.uniprot.org/annotation/VAR_062980|||http://purl.uniprot.org/annotation/VAR_062981|||http://purl.uniprot.org/annotation/VAR_062982|||http://purl.uniprot.org/annotation/VAR_068655|||http://purl.uniprot.org/annotation/VAR_068656|||http://purl.uniprot.org/annotation/VAR_068657|||http://purl.uniprot.org/annotation/VAR_068658|||http://purl.uniprot.org/annotation/VAR_068659|||http://purl.uniprot.org/annotation/VAR_068660|||http://purl.uniprot.org/annotation/VAR_068661|||http://purl.uniprot.org/annotation/VAR_068662|||http://purl.uniprot.org/annotation/VAR_068663|||http://purl.uniprot.org/annotation/VAR_068664|||http://purl.uniprot.org/annotation/VAR_080400|||http://purl.uniprot.org/annotation/VSP_013760|||http://purl.uniprot.org/annotation/VSP_013761|||http://purl.uniprot.org/annotation/VSP_054260
http://togogenome.org/gene/9606:S100A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4H2|||http://purl.uniprot.org/uniprot/P23297                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Strand                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||Protein S100-A1|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143961
http://togogenome.org/gene/9606:MT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25713                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-3|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197250
http://togogenome.org/gene/9606:CEP76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAP6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 76 kDa|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089501|||http://purl.uniprot.org/annotation/VSP_037610|||http://purl.uniprot.org/annotation/VSP_037611|||http://purl.uniprot.org/annotation/VSP_037612|||http://purl.uniprot.org/annotation/VSP_037613
http://togogenome.org/gene/9606:HLA-DMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1V0E3P2|||http://purl.uniprot.org/uniprot/P28068                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes targeting to endosomes and results in relocalization to the cell membrane.|||Beta-1|||Beta-2|||Connecting peptide|||Cytoplasmic|||Decreases the interaction with MHCII and peptide exchange.|||HLA class II histocompatibility antigen, DM beta chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DMB*01:01.|||In allele DMB*01:02 and allele DMB*01:06.|||In allele DMB*01:04 and allele DMB*01:05.|||In allele DMB*01:06.|||In allele DMB*01:07.|||Increases the interaction with MHCII and peptide exchange; when associated with N-49.|||Increases the interaction with MHCII and peptide exchange; when associated with Q-65.|||Lumenal|||N-linked (GlcNAc...) asparagine|||YXXZ motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018960|||http://purl.uniprot.org/annotation/PRO_5010666605|||http://purl.uniprot.org/annotation/VAR_016752|||http://purl.uniprot.org/annotation/VAR_016753|||http://purl.uniprot.org/annotation/VAR_016754|||http://purl.uniprot.org/annotation/VAR_016755|||http://purl.uniprot.org/annotation/VAR_050360|||http://purl.uniprot.org/annotation/VAR_050361|||http://purl.uniprot.org/annotation/VAR_050362
http://togogenome.org/gene/9606:VAMP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51809                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Longin|||N-acetylalanine; partial|||Phosphoserine|||Removed|||Vesicle-associated membrane protein 7|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206761|||http://purl.uniprot.org/annotation/VSP_017508|||http://purl.uniprot.org/annotation/VSP_017509
http://togogenome.org/gene/9606:LRRC73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B825|||http://purl.uniprot.org/uniprot/Q5JTD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252159
http://togogenome.org/gene/9606:STATH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02808                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Mass|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Hydrophobic; inhibits precipitation of calcium phosphate salts|||Hydroxyapatite-binding; inhibits crystal growth|||In isoform 2.|||Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-37|||Isoglutamyl lysine isopeptide (Lys-Gln); in form cyclo-statherin Q-39|||Phosphoserine|||Statherin|||With phosphorylated Ser-21 and Ser-22 and transglutamine cross-link.|||With phosphorylated Ser-21 and Ser-22.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022422|||http://purl.uniprot.org/annotation/VAR_069065|||http://purl.uniprot.org/annotation/VSP_045744
http://togogenome.org/gene/9606:PTPRO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16827                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase O|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025458|||http://purl.uniprot.org/annotation/VSP_035586|||http://purl.uniprot.org/annotation/VSP_043136|||http://purl.uniprot.org/annotation/VSP_054481|||http://purl.uniprot.org/annotation/VSP_054482
http://togogenome.org/gene/9606:CHRNA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36544                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mass|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  115-fold more potently inhibited by the alpha-conotoxin ImI; but no change in inhibition by the alpha-conotoxin ImII.|||Associated with receptor activation|||Cytoplasmic|||Essential for TMEM35A/NACHO-mediated proper subunit assembly and trafficking to cell membrane|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000366|||http://purl.uniprot.org/annotation/VSP_043019|||http://purl.uniprot.org/annotation/VSP_058107|||http://purl.uniprot.org/annotation/VSP_058108
http://togogenome.org/gene/9606:MYO1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00160|||http://purl.uniprot.org/uniprot/Q4LE34                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||Myosin motor|||Phosphoserine|||Probable disease-associated variant found in a patient with non-syndromic sensorineural hearing loss.|||SH3|||TH1|||Unconventional myosin-If                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123452|||http://purl.uniprot.org/annotation/VAR_056179|||http://purl.uniprot.org/annotation/VAR_079873
http://togogenome.org/gene/9606:WNT9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9ZGG3|||http://purl.uniprot.org/uniprot/O14904                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt|||Protein Wnt-9a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041455|||http://purl.uniprot.org/annotation/PRO_5003133039|||http://purl.uniprot.org/annotation/VAR_052956
http://togogenome.org/gene/9606:GNG12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBI6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012667|||http://purl.uniprot.org/annotation/PRO_0000012668
http://togogenome.org/gene/9606:NLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBE8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abrogates kinase activity.|||Basic residues|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Required for homodimerization and kinase activation and localization to the nucleus|||Required for interaction with TAB2|||Serine/threonine-protein kinase NLK|||Sufficient for interaction with DAPK3|||TQE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186336|||http://purl.uniprot.org/annotation/VAR_019549|||http://purl.uniprot.org/annotation/VAR_042273
http://togogenome.org/gene/9606:TMEM107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX40                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MKS13 and OFD16; does not affect subcellular location at ciliary transition zone; significantly decreases cilium assembly from patient's skin primary fibroblast; impairs protein localization to cilium from patient's skin primary fibroblast.|||In OFD16; does not affect subcellular location at ciliary transition zone.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254541|||http://purl.uniprot.org/annotation/VAR_079328|||http://purl.uniprot.org/annotation/VAR_079329|||http://purl.uniprot.org/annotation/VSP_021210|||http://purl.uniprot.org/annotation/VSP_021211|||http://purl.uniprot.org/annotation/VSP_021212|||http://purl.uniprot.org/annotation/VSP_021213
http://togogenome.org/gene/9606:ABCA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LE27|||http://purl.uniprot.org/uniprot/Q99758                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  150 Kda mature form|||ABC transporter|||ABC transporter 1|||ABC transporter 2|||Cleavage; by CTSL|||Decreases ATP hydrolysis activity of 13% compared to the wild-type.|||Decreases ATP hydrolysis activity of 15% compared to the wild-type.|||Decreases ATP hydrolysis activity of 18% compared to the wild-type.|||Decreases ATP hydrolysis activity of 36% compared to the wild-type.|||Decreases ATP hydrolysis activity of 56% compared to the wild-type.|||Does not affect N-glycosylation. Does not affect protein expression. Does not affect lamellar body membrane location.|||Does not affect lamellar body membrane location. Does not affect protein expression. Does not affect proteolytic processing.|||Does not affect protein oligomerization.|||Helical|||In SMDP3.|||In SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport.|||In SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity.|||In SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport.|||In SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport.|||In SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation.|||In SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro.|||In SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization.|||In SMDP3; unknown pathological significance.|||In SMDP3; unknown pathological significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death.|||In SMDP3; unknown pathological significance; does not affect protein oligomerization.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-124. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.|||Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-140. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location.|||Loss of proteolytic processing.|||N-linked (GlcNAc...) asparagine|||Phospholipid-transporting ATPase ABCA3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093293|||http://purl.uniprot.org/annotation/PRO_0000452297|||http://purl.uniprot.org/annotation/VAR_023497|||http://purl.uniprot.org/annotation/VAR_023498|||http://purl.uniprot.org/annotation/VAR_023499|||http://purl.uniprot.org/annotation/VAR_023500|||http://purl.uniprot.org/annotation/VAR_025061|||http://purl.uniprot.org/annotation/VAR_025062|||http://purl.uniprot.org/annotation/VAR_035728|||http://purl.uniprot.org/annotation/VAR_035729|||http://purl.uniprot.org/annotation/VAR_035730|||http://purl.uniprot.org/annotation/VAR_084240|||http://purl.uniprot.org/annotation/VAR_084241|||http://purl.uniprot.org/annotation/VAR_084242|||http://purl.uniprot.org/annotation/VAR_084243|||http://purl.uniprot.org/annotation/VAR_084244|||http://purl.uniprot.org/annotation/VAR_084245|||http://purl.uniprot.org/annotation/VAR_084246|||http://purl.uniprot.org/annotation/VAR_084247|||http://purl.uniprot.org/annotation/VAR_084248|||http://purl.uniprot.org/annotation/VAR_084249|||http://purl.uniprot.org/annotation/VAR_084250|||http://purl.uniprot.org/annotation/VAR_084251|||http://purl.uniprot.org/annotation/VAR_084252|||http://purl.uniprot.org/annotation/VAR_084253|||http://purl.uniprot.org/annotation/VAR_084254|||http://purl.uniprot.org/annotation/VAR_084255|||http://purl.uniprot.org/annotation/VAR_084256|||http://purl.uniprot.org/annotation/VAR_084257|||http://purl.uniprot.org/annotation/VAR_084258|||http://purl.uniprot.org/annotation/VSP_056262|||http://purl.uniprot.org/annotation/VSP_056263
http://togogenome.org/gene/9606:RPS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62280                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes S-acylation.|||Citrulline|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Small ribosomal subunit protein uS17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128509
http://togogenome.org/gene/9606:CACNA1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60840                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Binding to the beta subunit|||Cytoplasmic|||Dihydropyridine binding|||Disordered|||Extracellular|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In AIED and CSNB2A.|||In CSNB2A.|||In CSNB2A; increases the number of mutant channels open at physiologic membrane potential and allows for persistent Ca(2+) entry due to reduced channel inactivation resulting in a gain-of-function defect.|||In CSNB2A; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4 and isoform 6.|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Polar residues|||Voltage-dependent L-type calcium channel subunit alpha-1F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053950|||http://purl.uniprot.org/annotation/VAR_001504|||http://purl.uniprot.org/annotation/VAR_001505|||http://purl.uniprot.org/annotation/VAR_001506|||http://purl.uniprot.org/annotation/VAR_001507|||http://purl.uniprot.org/annotation/VAR_029376|||http://purl.uniprot.org/annotation/VAR_030807|||http://purl.uniprot.org/annotation/VAR_030808|||http://purl.uniprot.org/annotation/VAR_030809|||http://purl.uniprot.org/annotation/VAR_030810|||http://purl.uniprot.org/annotation/VAR_030811|||http://purl.uniprot.org/annotation/VAR_030812|||http://purl.uniprot.org/annotation/VAR_030813|||http://purl.uniprot.org/annotation/VAR_030814|||http://purl.uniprot.org/annotation/VAR_030815|||http://purl.uniprot.org/annotation/VAR_030816|||http://purl.uniprot.org/annotation/VAR_030817|||http://purl.uniprot.org/annotation/VAR_030818|||http://purl.uniprot.org/annotation/VAR_030819|||http://purl.uniprot.org/annotation/VAR_030820|||http://purl.uniprot.org/annotation/VAR_030821|||http://purl.uniprot.org/annotation/VAR_030822|||http://purl.uniprot.org/annotation/VAR_031822|||http://purl.uniprot.org/annotation/VAR_054818|||http://purl.uniprot.org/annotation/VAR_055662|||http://purl.uniprot.org/annotation/VAR_071433|||http://purl.uniprot.org/annotation/VSP_036785|||http://purl.uniprot.org/annotation/VSP_045172|||http://purl.uniprot.org/annotation/VSP_058923|||http://purl.uniprot.org/annotation/VSP_058924
http://togogenome.org/gene/9606:ARK2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A059NXK6|||http://purl.uniprot.org/uniprot/Q6ZSG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase ARK2C|||In isoform 2.|||RING-type|||RING-type; atypical|||Reduced binding to free ubiquitin and reduced E3 ubiquitin-protein ligase activity.|||Reduced binding to free ubiquitin.|||Reduced ubiquitin discharge.|||Ubiquitin binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245587|||http://purl.uniprot.org/annotation/VSP_045128
http://togogenome.org/gene/9606:KCNN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15554                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In DHS2.|||In DHS2; no effect on plasma membrane localization; increases calcium-activated potassium channel activity.|||Intermediate conductance calcium-activated potassium channel protein 4|||Loss of sensitivity to triarylmethanes.|||Phosphohistidine|||Pore-forming; Name=Segment H5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155017|||http://purl.uniprot.org/annotation/VAR_074485|||http://purl.uniprot.org/annotation/VAR_074486|||http://purl.uniprot.org/annotation/VAR_074487
http://togogenome.org/gene/9606:EYA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6K4|||http://purl.uniprot.org/uniprot/A6NCB9|||http://purl.uniprot.org/uniprot/B3KXR1|||http://purl.uniprot.org/uniprot/F8WB53|||http://purl.uniprot.org/uniprot/Q0P517|||http://purl.uniprot.org/uniprot/Q99502                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eyes absent homolog 1|||Found in a patient with congenital cataract.|||In ASA.|||In ASA; with cataract.|||In BOR1.|||In BOR1; with cataract.|||In BOS1.|||In isoform EYA1B.|||In isoform EYA1D.|||Loss of tyrosine phosphatase activity toward H2AX.|||Nucleophile|||Polar residues|||Pro residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218643|||http://purl.uniprot.org/annotation/VAR_005203|||http://purl.uniprot.org/annotation/VAR_005204|||http://purl.uniprot.org/annotation/VAR_016864|||http://purl.uniprot.org/annotation/VAR_016865|||http://purl.uniprot.org/annotation/VAR_016866|||http://purl.uniprot.org/annotation/VAR_016867|||http://purl.uniprot.org/annotation/VAR_016868|||http://purl.uniprot.org/annotation/VAR_016869|||http://purl.uniprot.org/annotation/VAR_024439|||http://purl.uniprot.org/annotation/VAR_044452|||http://purl.uniprot.org/annotation/VAR_064942|||http://purl.uniprot.org/annotation/VAR_064943|||http://purl.uniprot.org/annotation/VAR_064944|||http://purl.uniprot.org/annotation/VAR_064945|||http://purl.uniprot.org/annotation/VAR_064946|||http://purl.uniprot.org/annotation/VAR_064947|||http://purl.uniprot.org/annotation/VAR_070033|||http://purl.uniprot.org/annotation/VSP_001486|||http://purl.uniprot.org/annotation/VSP_045793|||http://purl.uniprot.org/annotation/VSP_045794
http://togogenome.org/gene/9606:MAD2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI95                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters interaction with REV3L and REV1. Loss of interaction with REV3L; when associated with A-63. No effect on interaction with REV1; when associated with A-124.|||Alters interaction with REV3L. Loss of interaction with REV3L; when associated with A-171.|||HORMA|||In FANCV; drastically reduced protein abundance.|||Induces structural changes that increase affinity for REV3L and REV1. No effect on interaction with REV1; when associated with A-171.|||Mediates interaction with REV1 and REV3L and homodimerization|||Mediates interaction with ipaB|||Mitotic spindle assembly checkpoint protein MAD2B|||Significantly prevents interaction with REV1; no effect on interaction with REV3L.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126119|||http://purl.uniprot.org/annotation/VAR_077981
http://togogenome.org/gene/9606:HIRIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HIRA-interacting protein 3|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083989|||http://purl.uniprot.org/annotation/VAR_028115|||http://purl.uniprot.org/annotation/VAR_051033|||http://purl.uniprot.org/annotation/VSP_003877|||http://purl.uniprot.org/annotation/VSP_046024|||http://purl.uniprot.org/annotation/VSP_046025
http://togogenome.org/gene/9606:OR5AS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD4|||http://purl.uniprot.org/uniprot/Q8N127                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150580|||http://purl.uniprot.org/annotation/VAR_034217|||http://purl.uniprot.org/annotation/VAR_034218
http://togogenome.org/gene/9606:PHF21B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z665|||http://purl.uniprot.org/uniprot/A0A0S2Z6R3|||http://purl.uniprot.org/uniprot/B1AHC5|||http://purl.uniprot.org/uniprot/Q96EK2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PHD finger protein 21B|||PHD-type|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226769|||http://purl.uniprot.org/annotation/VAR_051601|||http://purl.uniprot.org/annotation/VSP_017456|||http://purl.uniprot.org/annotation/VSP_043149
http://togogenome.org/gene/9606:LRRFIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y608                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DVL3-binding|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 5.|||Leucine-rich repeat flightless-interacting protein 2|||No change in LPS-induced NFKB activity.|||No change in LPS-induced NFKB activity. Interacts with MYD88 in an LPS-inducible manner.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduction in LPS-induced NFKB activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245246|||http://purl.uniprot.org/annotation/VAR_050001|||http://purl.uniprot.org/annotation/VSP_019674|||http://purl.uniprot.org/annotation/VSP_019675|||http://purl.uniprot.org/annotation/VSP_019676|||http://purl.uniprot.org/annotation/VSP_019677|||http://purl.uniprot.org/annotation/VSP_056969|||http://purl.uniprot.org/annotation/VSP_056970|||http://purl.uniprot.org/annotation/VSP_056971|||http://purl.uniprot.org/annotation/VSP_056972|||http://purl.uniprot.org/annotation/VSP_056973
http://togogenome.org/gene/9606:GDF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55107                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Growth/differentiation factor 10|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033844|||http://purl.uniprot.org/annotation/PRO_0000033845
http://togogenome.org/gene/9606:DCAF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66K64                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with DDB1, DDA1 and RBM39 in presence of indisulam.|||DDB1- and CUL4-associated factor 15|||Decreased interaction with DDA1 and RBM39 in presence of indisulam.|||Decreased interaction with DDB1, DDA1 and RBM39 in presence of indisulam.|||Decreased interaction with RBM39 in presence of indisulam, without affecting interaction with DDA1 and DDB1.|||Disordered|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314485
http://togogenome.org/gene/9606:SLC25A30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSR0|||http://purl.uniprot.org/uniprot/B3KTE8|||http://purl.uniprot.org/uniprot/Q5SVS4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Kidney mitochondrial carrier protein 1|||N-acetylserine|||Removed|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288916|||http://purl.uniprot.org/annotation/VSP_053984
http://togogenome.org/gene/9606:PLAA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y263                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||In NDMSBA.|||In NDMSBA; no effect on protein stability; no effect on subcellular localization; decreased function in positive regulation of cytosolic phospholipase A2 activity; in patient cells homozygous for the mutation.|||N6-acetyllysine|||PFU|||PUL|||Phospholipase A-2-activating protein|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051130|||http://purl.uniprot.org/annotation/VAR_079276|||http://purl.uniprot.org/annotation/VAR_079277
http://togogenome.org/gene/9606:ZMAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NC0                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Matrin-type|||N-acetylalanine|||Removed|||Zinc finger matrin-type protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047327
http://togogenome.org/gene/9606:PRSS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56730|||http://purl.uniprot.org/uniprot/Q96I80                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Charge relay system|||Disordered|||Kringle|||N-linked (GlcNAc...) asparagine|||Neurotrypsin|||Peptidase S1|||Pro residues|||Reactive bond homolog|||SRCR|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||Zymogen activation region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027663|||http://purl.uniprot.org/annotation/PRO_5004321914|||http://purl.uniprot.org/annotation/VAR_051835|||http://purl.uniprot.org/annotation/VAR_051836
http://togogenome.org/gene/9606:COL9A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20849                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen alpha-1(IX) chain|||Collagen-like 1|||Collagen-like 10|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Collagen-like 9|||Disordered|||In STL4.|||In isoform 2.|||In isoform 3.|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Nonhelical region (NC3)|||Nonhelical region (NC4)|||Pro residues|||Triple-helical region (COL1)|||Triple-helical region (COL2)|||Triple-helical region (COL3)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005765|||http://purl.uniprot.org/annotation/VAR_023326|||http://purl.uniprot.org/annotation/VAR_023327|||http://purl.uniprot.org/annotation/VAR_026463|||http://purl.uniprot.org/annotation/VAR_026464|||http://purl.uniprot.org/annotation/VAR_055668|||http://purl.uniprot.org/annotation/VAR_055669|||http://purl.uniprot.org/annotation/VAR_087538|||http://purl.uniprot.org/annotation/VAR_087539|||http://purl.uniprot.org/annotation/VSP_001141|||http://purl.uniprot.org/annotation/VSP_001142|||http://purl.uniprot.org/annotation/VSP_015250|||http://purl.uniprot.org/annotation/VSP_015251
http://togogenome.org/gene/9606:TRPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13507                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Binds to IP3R3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In SCA41; toxic gain of function effect.|||In isoform 2.|||Loss of inhibition by intracellular Ca(2+) and loss of Ca(2+)-induced thermostability.|||Loss of inhibition by intracellular Ca(2+) and loss of Ca(2+)-induced thermostability. Impaired extracellular Ca(2+) inhibition at a holding potential of -60 mV. No effect on activation by diacylglycerol (DAG) analog; when associated with A-525 and A-874.|||N-linked (GlcNAc...) asparagine|||No effect on inhibition by Ca(2+) or thermostability. No effect on activation by diacylglycerol (DAG) analog; when associated with A-874 and A-883.|||Retains robust Ca(2+) inhibition with moderate enhancement of thermostability in low-Ca(2+) conditions. No effect on activation by diacylglycerol (DAG) analog; when associated with A-525 and A-883.|||Short transient receptor potential channel 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215310|||http://purl.uniprot.org/annotation/VAR_073835|||http://purl.uniprot.org/annotation/VSP_061592
http://togogenome.org/gene/9606:ELOVL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTI6|||http://purl.uniprot.org/uniprot/B3KWH9|||http://purl.uniprot.org/uniprot/Q9NYP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Elongation of very long chain fatty acids protein 5|||Helical|||In SCA38.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282838|||http://purl.uniprot.org/annotation/VAR_072361|||http://purl.uniprot.org/annotation/VAR_072362|||http://purl.uniprot.org/annotation/VSP_045917|||http://purl.uniprot.org/annotation/VSP_045918|||http://purl.uniprot.org/annotation/VSP_045919
http://togogenome.org/gene/9606:SYVN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TM6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ligase activity.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase synoviolin|||HAF-H domain; necessary to form higher-order Hrd1 complexes|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with p53/TP53|||Involved in FAM8A1 interaction|||Loss of interaction with FAM8A1, HERPUD1, OS9 and UBE2J1, impaired degradation of immature core-glycosylated basigin/CD147.|||Lumenal|||Necessary and sufficient for SEL1L interaction|||No effect on interaction with FAM8A1, HERPUD1, OS9, SEL1L and UBE2J1.|||Phosphoserine|||Polar residues|||Pro residues|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280548|||http://purl.uniprot.org/annotation/VSP_023777|||http://purl.uniprot.org/annotation/VSP_023778
http://togogenome.org/gene/9606:SPATA45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q537H7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Spermatogenesis-associated protein 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285785|||http://purl.uniprot.org/annotation/VAR_060195
http://togogenome.org/gene/9606:NAT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KRQ7|||http://purl.uniprot.org/uniprot/J3KSE9|||http://purl.uniprot.org/uniprot/J3KT72|||http://purl.uniprot.org/uniprot/J3QL33|||http://purl.uniprot.org/uniprot/J3QQP3|||http://purl.uniprot.org/uniprot/Q9BTE0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha/beta-tubulin-N-acetyltransferase 9|||In isoform 2.|||N-acetyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286874|||http://purl.uniprot.org/annotation/VAR_032225|||http://purl.uniprot.org/annotation/VSP_025231
http://togogenome.org/gene/9606:CLSTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Calsyntenin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform CLSTN3beta.|||Lumenal|||May be associated with susceptibility to obesity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004026|||http://purl.uniprot.org/annotation/VAR_036114|||http://purl.uniprot.org/annotation/VAR_048583|||http://purl.uniprot.org/annotation/VAR_087903|||http://purl.uniprot.org/annotation/VSP_043748|||http://purl.uniprot.org/annotation/VSP_061880
http://togogenome.org/gene/9606:IBTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLE0|||http://purl.uniprot.org/uniprot/E7EPI0|||http://purl.uniprot.org/uniprot/Q9P2D0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||BTB|||BTB 1|||BTB 2|||Disordered|||In isoform 2.|||In isoform 3.|||Inhibitor of Bruton tyrosine kinase|||Phosphoserine|||Polar residues|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280276|||http://purl.uniprot.org/annotation/VAR_031106|||http://purl.uniprot.org/annotation/VAR_031107|||http://purl.uniprot.org/annotation/VSP_023600|||http://purl.uniprot.org/annotation/VSP_023601|||http://purl.uniprot.org/annotation/VSP_023602|||http://purl.uniprot.org/annotation/VSP_023604
http://togogenome.org/gene/9606:SDHAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with the iron-sulfur transfer complex composed of HSC20, HSPA9 and ISCU and reduces binding to SDHB.|||Basic and acidic residues|||Disordered|||In MC2DN2.|||In MC2DN2; abolishes binding to the iron-sulfur transfer complex formed by HSC20, HSPA9 and ICSU; prevents interaction with SDHB; leads to rapid degradation of SDHAF1.|||In MC2DN2; rapid degradation of SDHB by the LONP1 protease; increased levels of HIF1A and EPAS1/HIF2A which correlates with succinate accumulation.|||In MC2DN2; reduces but does not prevent interaction with HSC20 or SDHB.|||Interaction with SDHB|||LYR motif 1; required for interaction with HSC20|||LYR motif 2; not required for interaction with HSC20|||Retains reduced ability to interact with HSC20 and SDHB.|||Succinate dehydrogenase assembly factor 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327916|||http://purl.uniprot.org/annotation/VAR_058097|||http://purl.uniprot.org/annotation/VAR_058098|||http://purl.uniprot.org/annotation/VAR_081226|||http://purl.uniprot.org/annotation/VAR_081227|||http://purl.uniprot.org/annotation/VAR_085405|||http://purl.uniprot.org/annotation/VAR_085406
http://togogenome.org/gene/9606:DHX33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIS6|||http://purl.uniprot.org/uniprot/Q9H6R0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX33|||Critical for rDNA-binding|||DEAH box|||Disordered|||HA2; required for interaction with EIF3G and RPL26|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||No effect on inflammasome activation upon dsRNA-binding.|||Required for nucleolar location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055164|||http://purl.uniprot.org/annotation/VAR_057239|||http://purl.uniprot.org/annotation/VAR_057240|||http://purl.uniprot.org/annotation/VSP_016256
http://togogenome.org/gene/9606:GPR180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V85                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||Integral membrane protein GPR180|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239662|||http://purl.uniprot.org/annotation/VAR_035925
http://togogenome.org/gene/9606:NEU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQI0|||http://purl.uniprot.org/uniprot/Q99519                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Repeat|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  BNR 1|||BNR 2|||BNR 3|||BNR 4|||Correct sorting to the plasma membrane but no endocytosis and internalization.|||Does not affect sialidase activity.|||FRIP motif|||Helical|||In SIALIDOSIS.|||In SIALIDOSIS; infantile type 2; catalytically inactive.|||In SIALIDOSIS; infantile type 2; catalytically inactive; rapid intralysosomal degradation.|||In SIALIDOSIS; infantile type 2; unable to reach the lysosomes.|||In SIALIDOSIS; type 1 and juvenile type 2; catalytically inactive; retained in pre-lysosomal compartments.|||In SIALIDOSIS; type 1; mild mutation as residual activity is still measurable.|||In SIALIDOSIS; type 1; no enzyme activity and no transport to the lysosome.|||In SIALIDOSIS; type 1; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes.|||In SIALIDOSIS; type 1; normally processed.|||In SIALIDOSIS; type 1; partial transport and residual transport activity.|||In SIALIDOSIS; type 1; reduction in enzyme activity.|||In SIALIDOSIS; type 1; unable to reach the lysosomes.|||In SIALIDOSIS; type 2.|||In SIALIDOSIS; type 2; affects substrate binding or catalysis.|||In SIALIDOSIS; type 2; impaired enzyme folding.|||In SIALIDOSIS; type 2; less than 10% of activity.|||In SIALIDOSIS; type 2; less than 10% of activity; rapid intralysosomal degradation; impaired enzyme folding.|||In SIALIDOSIS; type 2; no enzyme activity; retained in the endoplasmic reticulum / Golgi or rapidly degraded in the lysosomes.|||In SIALIDOSIS; type 2; reduction in enzyme activity; rapid intralysosomal degradation.|||In SIALIDOSIS; type 2; unable to reach the lysosomes.|||Internalization signal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton acceptor|||Sialidase|||Sialidase-1|||Significant decrease in sialidase activity; absence of lysosomal localization; mislocalization to the endoplasmic reticulum.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012026|||http://purl.uniprot.org/annotation/VAR_012207|||http://purl.uniprot.org/annotation/VAR_012208|||http://purl.uniprot.org/annotation/VAR_012209|||http://purl.uniprot.org/annotation/VAR_012210|||http://purl.uniprot.org/annotation/VAR_012211|||http://purl.uniprot.org/annotation/VAR_012212|||http://purl.uniprot.org/annotation/VAR_012213|||http://purl.uniprot.org/annotation/VAR_012214|||http://purl.uniprot.org/annotation/VAR_012215|||http://purl.uniprot.org/annotation/VAR_012216|||http://purl.uniprot.org/annotation/VAR_012217|||http://purl.uniprot.org/annotation/VAR_012218|||http://purl.uniprot.org/annotation/VAR_012219|||http://purl.uniprot.org/annotation/VAR_012220|||http://purl.uniprot.org/annotation/VAR_012221|||http://purl.uniprot.org/annotation/VAR_012222|||http://purl.uniprot.org/annotation/VAR_012223|||http://purl.uniprot.org/annotation/VAR_012224|||http://purl.uniprot.org/annotation/VAR_012225|||http://purl.uniprot.org/annotation/VAR_012226|||http://purl.uniprot.org/annotation/VAR_017460|||http://purl.uniprot.org/annotation/VAR_017461|||http://purl.uniprot.org/annotation/VAR_018076|||http://purl.uniprot.org/annotation/VAR_018077|||http://purl.uniprot.org/annotation/VAR_049203|||http://purl.uniprot.org/annotation/VAR_079557|||http://purl.uniprot.org/annotation/VAR_079558|||http://purl.uniprot.org/annotation/VAR_079559|||http://purl.uniprot.org/annotation/VAR_079560|||http://purl.uniprot.org/annotation/VAR_079561|||http://purl.uniprot.org/annotation/VAR_079562|||http://purl.uniprot.org/annotation/VAR_079563|||http://purl.uniprot.org/annotation/VAR_079564|||http://purl.uniprot.org/annotation/VAR_079565|||http://purl.uniprot.org/annotation/VAR_079566|||http://purl.uniprot.org/annotation/VAR_079567|||http://purl.uniprot.org/annotation/VAR_079568
http://togogenome.org/gene/9606:EIF1AY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJH9|||http://purl.uniprot.org/uniprot/O14602                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Eukaryotic translation initiation factor 1A, Y-chromosomal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||S1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145102
http://togogenome.org/gene/9606:ILRUN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6K1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein ILRUN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089519|||http://purl.uniprot.org/annotation/VSP_017259
http://togogenome.org/gene/9606:VHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2F2|||http://purl.uniprot.org/uniprot/A0A0S2Z4K1|||http://purl.uniprot.org/uniprot/P40337                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 5 AA tandem repeats of G-[PAVG]-E-E-[DAYSLE]|||Acidic residues|||Disordered|||In ECYT2 and VHLD; type I.|||In ECYT2 and VHLD; type II.|||In ECYT2, pheochromocytoma and VHLD; type IIA.|||In ECYT2.|||In RCC; with paraneoplastic erythrocytosis; inhibits binding to HIF1AN.|||In VHLD.|||In VHLD; type I-II.|||In VHLD; type I-II; abolishes release from chaperonin complex and the interaction with Elongin BC complex.|||In VHLD; type I-II; common mutation.|||In VHLD; type I.|||In VHLD; type I; No effect on interaction with HIF1A nor on HIF1A degradation.|||In VHLD; type I; common mutation.|||In VHLD; type I; requires 2 nucleotide substitutions.|||In VHLD; type II and type 2C.|||In VHLD; type II.|||In VHLD; type IIA.|||In VHLD; with RCC.|||In cerebellar hemangioblastoma.|||In hemangioblastoma.|||In isoform 2.|||In isoform 3.|||In lung cancer.|||In pheochromocytoma and VHLD; type I.|||In pheochromocytoma and VHLD; type II.|||In pheochromocytoma and VHLD; type II; common mutation.|||In pheochromocytoma.|||In pheochromocytoma; likely benign variant.|||In pheochromocytoma; requires 2 nucleotide substitutions.|||Interaction with Elongin BC complex|||Involved in binding to CCT complex|||No interaction with HIF1A. No HIF1A degradation.|||von Hippel-Lindau disease tumor suppressor|||von Hippel-Lindau disease tumour suppressor alpha|||von Hippel-Lindau disease tumour suppressor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065809|||http://purl.uniprot.org/annotation/VAR_005670|||http://purl.uniprot.org/annotation/VAR_005671|||http://purl.uniprot.org/annotation/VAR_005672|||http://purl.uniprot.org/annotation/VAR_005673|||http://purl.uniprot.org/annotation/VAR_005674|||http://purl.uniprot.org/annotation/VAR_005675|||http://purl.uniprot.org/annotation/VAR_005676|||http://purl.uniprot.org/annotation/VAR_005677|||http://purl.uniprot.org/annotation/VAR_005678|||http://purl.uniprot.org/annotation/VAR_005679|||http://purl.uniprot.org/annotation/VAR_005680|||http://purl.uniprot.org/annotation/VAR_005681|||http://purl.uniprot.org/annotation/VAR_005682|||http://purl.uniprot.org/annotation/VAR_005683|||http://purl.uniprot.org/annotation/VAR_005684|||http://purl.uniprot.org/annotation/VAR_005685|||http://purl.uniprot.org/annotation/VAR_005686|||http://purl.uniprot.org/annotation/VAR_005687|||http://purl.uniprot.org/annotation/VAR_005688|||http://purl.uniprot.org/annotation/VAR_005689|||http://purl.uniprot.org/annotation/VAR_005690|||http://purl.uniprot.org/annotation/VAR_005691|||http://purl.uniprot.org/annotation/VAR_005692|||http://purl.uniprot.org/annotation/VAR_005693|||http://purl.uniprot.org/annotation/VAR_005694|||http://purl.uniprot.org/annotation/VAR_005695|||http://purl.uniprot.org/annotation/VAR_005696|||http://purl.uniprot.org/annotation/VAR_005697|||http://purl.uniprot.org/annotation/VAR_005698|||http://purl.uniprot.org/annotation/VAR_005699|||http://purl.uniprot.org/annotation/VAR_005700|||http://purl.uniprot.org/annotation/VAR_005701|||http://purl.uniprot.org/annotation/VAR_005702|||http://purl.uniprot.org/annotation/VAR_005703|||http://purl.uniprot.org/annotation/VAR_005704|||http://purl.uniprot.org/annotation/VAR_005705|||http://purl.uniprot.org/annotation/VAR_005706|||http://purl.uniprot.org/annotation/VAR_005707|||http://purl.uniprot.org/annotation/VAR_005708|||http://purl.uniprot.org/annotation/VAR_005709|||http://purl.uniprot.org/annotation/VAR_005710|||http://purl.uniprot.org/annotation/VAR_005711|||http://purl.uniprot.org/annotation/VAR_005712|||http://purl.uniprot.org/annotation/VAR_005713|||http://purl.uniprot.org/annotation/VAR_005714|||http://purl.uniprot.org/annotation/VAR_005715|||http://purl.uniprot.org/annotation/VAR_005716|||http://purl.uniprot.org/annotation/VAR_005717|||http://purl.uniprot.org/annotation/VAR_005718|||http://purl.uniprot.org/annotation/VAR_005719|||http://purl.uniprot.org/annotation/VAR_005720|||http://purl.uniprot.org/annotation/VAR_005722|||http://purl.uniprot.org/annotation/VAR_005723|||http://purl.uniprot.org/annotation/VAR_005724|||http://purl.uniprot.org/annotation/VAR_005725|||http://purl.uniprot.org/annotation/VAR_005726|||http://purl.uniprot.org/annotation/VAR_005727|||http://purl.uniprot.org/annotation/VAR_005728|||http://purl.uniprot.org/annotation/VAR_005729|||http://purl.uniprot.org/annotation/VAR_005730|||http://purl.uniprot.org/annotation/VAR_005731|||http://purl.uniprot.org/annotation/VAR_005732|||http://purl.uniprot.org/annotation/VAR_005733|||http://purl.uniprot.org/annotation/VAR_005734|||http://purl.uniprot.org/annotation/VAR_005735|||http://purl.uniprot.org/annotation/VAR_005736|||http://purl.uniprot.org/annotation/VAR_005737|||http://purl.uniprot.org/annotation/VAR_005738|||http://purl.uniprot.org/annotation/VAR_005739|||http://purl.uniprot.org/annotation/VAR_005740|||http://purl.uniprot.org/annotation/VAR_005741|||http://purl.uniprot.org/annotation/VAR_005742|||http://purl.uniprot.org/annotation/VAR_005743|||http://purl.uniprot.org/annotation/VAR_005744|||http://purl.uniprot.org/annotation/VAR_005746|||http://purl.uniprot.org/annotation/VAR_005747|||http://purl.uniprot.org/annotation/VAR_005748|||http://purl.uniprot.org/annotation/VAR_005749|||http://purl.uniprot.org/annotation/VAR_005750|||http://purl.uniprot.org/annotation/VAR_005751|||http://purl.uniprot.org/annotation/VAR_005752|||http://purl.uniprot.org/annotation/VAR_005753|||http://purl.uniprot.org/annotation/VAR_005754|||http://purl.uniprot.org/annotation/VAR_005755|||http://purl.uniprot.org/annotation/VAR_005756|||http://purl.uniprot.org/annotation/VAR_005757|||http://purl.uniprot.org/annotation/VAR_005758|||http://purl.uniprot.org/annotation/VAR_005759|||http://purl.uniprot.org/annotation/VAR_005760|||http://purl.uniprot.org/annotation/VAR_005761|||http://purl.uniprot.org/annotation/VAR_005762|||http://purl.uniprot.org/annotation/VAR_005763|||http://purl.uniprot.org/annotation/VAR_005764|||http://purl.uniprot.org/annotation/VAR_005765|||http://purl.uniprot.org/annotation/VAR_005766|||http://purl.uniprot.org/annotation/VAR_005767|||http://purl.uniprot.org/annotation/VAR_005768|||http://purl.uniprot.org/annotation/VAR_005769|||http://purl.uniprot.org/annotation/VAR_005770|||http://purl.uniprot.org/annotation/VAR_005771|||http://purl.uniprot.org/annotation/VAR_005772|||http://purl.uniprot.org/annotation/VAR_005773|||http://purl.uniprot.org/annotation/VAR_005774|||http://purl.uniprot.org/annotation/VAR_005775|||http://purl.uniprot.org/annotation/VAR_005776|||http://purl.uniprot.org/annotation/VAR_005777|||http://purl.uniprot.org/annotation/VAR_005778|||http://purl.uniprot.org/annotation/VAR_005779|||http://purl.uniprot.org/annotation/VAR_008097|||http://purl.uniprot.org/annotation/VAR_008098|||http://purl.uniprot.org/annotation/VAR_008099|||http://purl.uniprot.org/annotation/VAR_008100|||http://purl.uniprot.org/annotation/VAR_008101|||http://purl.uniprot.org/annotation/VAR_008102|||http://purl.uniprot.org/annotation/VAR_008103|||http://purl.uniprot.org/annotation/VAR_008104|||http://purl.uniprot.org/annotation/VAR_034562|||http://purl.uniprot.org/annotation/VAR_034987|||http://purl.uniprot.org/annotation/VAR_034988|||http://purl.uniprot.org/annotation/VAR_034989|||http://purl.uniprot.org/annotation/VAR_034990|||http://purl.uniprot.org/annotation/VAR_034991|||http://purl.uniprot.org/annotation/VAR_034992|||http://purl.uniprot.org/annotation/VAR_034993|||http://purl.uniprot.org/annotation/VAR_034994|||http://purl.uniprot.org/annotation/VAR_034995|||http://purl.uniprot.org/annotation/VAR_034996|||http://purl.uniprot.org/annotation/VAR_034997|||http://purl.uniprot.org/annotation/VAR_034998|||http://purl.uniprot.org/annotation/VAR_034999|||http://purl.uniprot.org/annotation/VAR_035000|||http://purl.uniprot.org/annotation/VAR_035001|||http://purl.uniprot.org/annotation/VAR_055087|||http://purl.uniprot.org/annotation/VSP_004488|||http://purl.uniprot.org/annotation/VSP_007740
http://togogenome.org/gene/9606:OR1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWA2|||http://purl.uniprot.org/uniprot/Q9P1Q5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150412|||http://purl.uniprot.org/annotation/VAR_020380|||http://purl.uniprot.org/annotation/VAR_034161|||http://purl.uniprot.org/annotation/VAR_047080
http://togogenome.org/gene/9606:SMARCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRP6|||http://purl.uniprot.org/uniprot/B7ZLQ5|||http://purl.uniprot.org/uniprot/P28370                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||No effect on neurite outgrowth.|||Phosphoserine|||Phosphotyrosine|||Probable global transcription activator SNF2L1|||SANT|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074351|||http://purl.uniprot.org/annotation/VAR_001242|||http://purl.uniprot.org/annotation/VAR_079028|||http://purl.uniprot.org/annotation/VSP_020406
http://togogenome.org/gene/9606:CILK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQG4|||http://purl.uniprot.org/uniprot/Q9UPZ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In ECO; significantly impairs kinase activity; decreased localization at the ciliary tips; impaired ciliogenesis; results in abnormally elongated cilia; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system; loss of nuclear localization.|||In EJM10; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system.|||In EJM10; unknown pathological significance.|||In EJM10; unknown pathological significance; impairs mitosis, cell-cycle exit and radial neuroblast migration, while promoting apoptosis, when tested in a heterologous system.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-36.|||Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-38.|||Loss of activity and autophosphorylation; when associated with R-33; R-36 and R-38.|||Loss of activity and autophosphorylation; when associated with R-34; R-36 and R-38.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with A-157.|||Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with F-159.|||Serine/threonine-protein kinase ICK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086007|||http://purl.uniprot.org/annotation/VAR_042001|||http://purl.uniprot.org/annotation/VAR_042002|||http://purl.uniprot.org/annotation/VAR_042003|||http://purl.uniprot.org/annotation/VAR_042004|||http://purl.uniprot.org/annotation/VAR_042005|||http://purl.uniprot.org/annotation/VAR_053931|||http://purl.uniprot.org/annotation/VAR_057994|||http://purl.uniprot.org/annotation/VAR_080554|||http://purl.uniprot.org/annotation/VAR_080555|||http://purl.uniprot.org/annotation/VAR_080556|||http://purl.uniprot.org/annotation/VAR_080557|||http://purl.uniprot.org/annotation/VAR_080558|||http://purl.uniprot.org/annotation/VSP_050752|||http://purl.uniprot.org/annotation/VSP_050753
http://togogenome.org/gene/9606:TNNC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63316|||http://purl.uniprot.org/uniprot/Q6FH91                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In CMD1Z.|||In CMH13; impairs protein kinase A dependent signaling from cardiac troponin I to troponin C.|||In CMH13; increases calcium sensitivity of the myofilaments.|||In CMH13; no changes in calcium sensitivity of the myofilaments.|||N-acetylmethionine|||Phosphoserine|||Troponin C, slow skeletal and cardiac muscles                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073697|||http://purl.uniprot.org/annotation/VAR_019776|||http://purl.uniprot.org/annotation/VAR_043988|||http://purl.uniprot.org/annotation/VAR_063070|||http://purl.uniprot.org/annotation/VAR_063071|||http://purl.uniprot.org/annotation/VAR_063072|||http://purl.uniprot.org/annotation/VAR_063073
http://togogenome.org/gene/9606:NEXMIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QGS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In XLID98.|||In XLID98; de novo dominant mutation found in females; disease phenotype includes epilepsy as a feature.|||Neurite extension and migration factor|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257844|||http://purl.uniprot.org/annotation/VAR_049529|||http://purl.uniprot.org/annotation/VAR_079039|||http://purl.uniprot.org/annotation/VAR_079040|||http://purl.uniprot.org/annotation/VAR_079041|||http://purl.uniprot.org/annotation/VAR_079042|||http://purl.uniprot.org/annotation/VAR_079043|||http://purl.uniprot.org/annotation/VAR_079044|||http://purl.uniprot.org/annotation/VAR_079045
http://togogenome.org/gene/9606:ADGRF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZF2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor F5|||Cleavage|||Cleavage; by autolysis|||Cleavage; by furin|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Ig-like 1|||Ig-like 2|||Ig-like 3|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012896|||http://purl.uniprot.org/annotation/VAR_024477|||http://purl.uniprot.org/annotation/VAR_025326|||http://purl.uniprot.org/annotation/VAR_055291|||http://purl.uniprot.org/annotation/VSP_010837|||http://purl.uniprot.org/annotation/VSP_010838|||http://purl.uniprot.org/annotation/VSP_039130
http://togogenome.org/gene/9606:ITGB1BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKP3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||CHORD 1|||CHORD 2|||CS|||Disordered|||In isoform 2.|||Integrin beta-1-binding protein 2|||SH2-binding|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084267|||http://purl.uniprot.org/annotation/VSP_056379
http://togogenome.org/gene/9606:FOXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32314                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein N2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091868|||http://purl.uniprot.org/annotation/VSP_035743|||http://purl.uniprot.org/annotation/VSP_035744
http://togogenome.org/gene/9606:KRT35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92764                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha5|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063692|||http://purl.uniprot.org/annotation/VAR_056019|||http://purl.uniprot.org/annotation/VAR_056020|||http://purl.uniprot.org/annotation/VAR_056021
http://togogenome.org/gene/9606:FBXL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKA1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes iron-binding and promotes its degradation.|||F-box|||F-box/LRR-repeat protein 5|||Hemerythrin-like|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||More than 90% loss of binding to IREB2/IRP2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119845|||http://purl.uniprot.org/annotation/VSP_008417
http://togogenome.org/gene/9606:PPDPFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWR9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Pancreatic progenitor cell differentiation and proliferation factor-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228102|||http://purl.uniprot.org/annotation/VSP_017651|||http://purl.uniprot.org/annotation/VSP_044862
http://togogenome.org/gene/9606:NEU4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR54|||http://purl.uniprot.org/uniprot/Q3KR05|||http://purl.uniprot.org/uniprot/Q8WWR8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BNR 1|||BNR 2|||BNR 3|||Disordered|||FRIP motif|||Impairs mitochondrial targeting.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Proton acceptor|||Sialidase|||Sialidase-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208906|||http://purl.uniprot.org/annotation/VAR_067458|||http://purl.uniprot.org/annotation/VSP_037491|||http://purl.uniprot.org/annotation/VSP_047123
http://togogenome.org/gene/9606:PCDH12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DMJDS1.|||In DMJDS1; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-12|||Protocadherin-12, secreted form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003996|||http://purl.uniprot.org/annotation/PRO_0000444041|||http://purl.uniprot.org/annotation/VAR_020368|||http://purl.uniprot.org/annotation/VAR_020369|||http://purl.uniprot.org/annotation/VAR_080385|||http://purl.uniprot.org/annotation/VAR_080386|||http://purl.uniprot.org/annotation/VAR_080387|||http://purl.uniprot.org/annotation/VAR_080388|||http://purl.uniprot.org/annotation/VAR_080389
http://togogenome.org/gene/9606:MASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48740                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||CUB 1|||CUB 2|||Charge relay system|||Cleavage; by autolysis|||EGF-like; calcium-binding|||Homodimerization|||In 3MC1.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with FCN2|||Interaction with MBL2|||Interchain (between heavy and light chains)|||Loss of interaction with FCN2, FCN3 and MBL2.|||Loss of interaction with FNC2 and FCN3 and partial loss of interaction with MBL2.|||Mannan-binding lectin serine protease 1|||Mannan-binding lectin serine protease 1 heavy chain|||Mannan-binding lectin serine protease 1 light chain|||N-linked (GlcNAc) asparagine|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No autoproteolytic processing.|||Partial loss of interaction with FCN2 and FCN3. No effect on interaction with MBL2.|||Partial loss of interaction with FCN2, FCN3 and MBL2.|||Peptidase S1|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027592|||http://purl.uniprot.org/annotation/PRO_0000027593|||http://purl.uniprot.org/annotation/PRO_0000027594|||http://purl.uniprot.org/annotation/VAR_051831|||http://purl.uniprot.org/annotation/VAR_051832|||http://purl.uniprot.org/annotation/VAR_051833|||http://purl.uniprot.org/annotation/VAR_078814|||http://purl.uniprot.org/annotation/VAR_082900|||http://purl.uniprot.org/annotation/VAR_082901|||http://purl.uniprot.org/annotation/VAR_082902|||http://purl.uniprot.org/annotation/VAR_082903|||http://purl.uniprot.org/annotation/VAR_082904|||http://purl.uniprot.org/annotation/VAR_082905|||http://purl.uniprot.org/annotation/VSP_036809|||http://purl.uniprot.org/annotation/VSP_036810|||http://purl.uniprot.org/annotation/VSP_036811|||http://purl.uniprot.org/annotation/VSP_036812|||http://purl.uniprot.org/annotation/VSP_036813
http://togogenome.org/gene/9606:TAF6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0D4|||http://purl.uniprot.org/uniprot/Q9Y6J9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Phosphoserine|||TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118879
http://togogenome.org/gene/9606:RASSF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK89                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Ras association domain-containing protein 10|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332284|||http://purl.uniprot.org/annotation/VAR_042999
http://togogenome.org/gene/9606:C1QTNF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0J0L9|||http://purl.uniprot.org/uniprot/Q9BXJ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C1q|||C1q 1|||C1q 2|||Complement C1q tumor necrosis factor-related protein 4|||Disordered|||Found in a patient with autosomal recessive retinitis pigmentosa; unknown pathological significance.|||Found in a patient with systemic lupus erythematosus; unknown pathological significance; inhibits TNF-mediated NF-kB activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003533|||http://purl.uniprot.org/annotation/PRO_5017253384|||http://purl.uniprot.org/annotation/VAR_081086|||http://purl.uniprot.org/annotation/VAR_081087
http://togogenome.org/gene/9606:ATP2C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR57|||http://purl.uniprot.org/uniprot/O75185                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Calcium-transporting ATPase type 2C member 2|||Cation-transporting P-type ATPase C-terminal|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||Interaction with ORAI1|||Loss of calcium-dependent ATPase activity.|||Loss of calcium-dependent ATPase activity. Has no effect on trafficking to the plasma membrane.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046207|||http://purl.uniprot.org/annotation/VAR_047935|||http://purl.uniprot.org/annotation/VAR_047936|||http://purl.uniprot.org/annotation/VAR_047937|||http://purl.uniprot.org/annotation/VAR_059137|||http://purl.uniprot.org/annotation/VAR_070929|||http://purl.uniprot.org/annotation/VSP_035989|||http://purl.uniprot.org/annotation/VSP_054679
http://togogenome.org/gene/9606:C3orf22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5N4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Uncharacterized protein C3orf22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234430|||http://purl.uniprot.org/annotation/VSP_056902
http://togogenome.org/gene/9606:NRROS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YC3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In SENEBAC; unknown pathological significance.|||Interchain (with C-? in TGFB1); in linked form|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Transforming growth factor beta activator LRRC33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042660|||http://purl.uniprot.org/annotation/VAR_083995|||http://purl.uniprot.org/annotation/VAR_083996
http://togogenome.org/gene/9606:GFY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L273                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Golgi-associated olfactory signaling regulator|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000424823
http://togogenome.org/gene/9606:ASB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y575                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 3|||In isoform 2.|||In isoform 3.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066926|||http://purl.uniprot.org/annotation/VSP_036392|||http://purl.uniprot.org/annotation/VSP_044606
http://togogenome.org/gene/9606:EXOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2C4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Mitochondrion|||No effect on catalytic activity.|||Nuclease EXOG, mitochondrial|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178669|||http://purl.uniprot.org/annotation/VAR_044320|||http://purl.uniprot.org/annotation/VSP_034506|||http://purl.uniprot.org/annotation/VSP_034507|||http://purl.uniprot.org/annotation/VSP_034508|||http://purl.uniprot.org/annotation/VSP_041214
http://togogenome.org/gene/9606:MAP1LC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H492                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished deconjugation of phosphatidylethanolamine (PE) by ATG4B, without affecting deconjugation by Legionella RavZ.|||Abolished deconjugation of phosphatidylethanolamine (PE) by Legionella RavZ, without affecting deconjugation by ATG4B.|||Abolished deconjugation of phosphatidylethanolamine (PE) by both Legionella RavZ and ATG4B.|||Cleavage; by ATG4B|||Decreases interaction with ATG13 and strongly reduces autophagosome formation.|||Decreases interaction with ATG13.|||Does not affect deconjugation of phosphatidylethanolamine (PE).|||Enhances binding to RETREG1.|||Important for interaction with ATG13 and for autophagosome formation|||In isoform 2.|||Increases interaction with ATG13 and strongly reduces autophagosome formation.|||Microtubule-associated proteins 1A/1B light chain 3A|||No processing of precursor.|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Phosphoserine; by PKA|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017192|||http://purl.uniprot.org/annotation/PRO_0000017193|||http://purl.uniprot.org/annotation/VSP_013660
http://togogenome.org/gene/9606:RPS19BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WX3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Active regulator of SIRT1|||Citrulline|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252393|||http://purl.uniprot.org/annotation/VAR_051330
http://togogenome.org/gene/9606:TMEM9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6P5|||http://purl.uniprot.org/uniprot/Q543A1|||http://purl.uniprot.org/uniprot/Q9NQ34                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034376|||http://purl.uniprot.org/annotation/PRO_5014309540|||http://purl.uniprot.org/annotation/VSP_055294
http://togogenome.org/gene/9606:ANKRD17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75179                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Acidic residues|||Ankyrin repeat domain-containing protein 17|||Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CAGS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||KH|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307917|||http://purl.uniprot.org/annotation/VAR_036711|||http://purl.uniprot.org/annotation/VAR_086093|||http://purl.uniprot.org/annotation/VAR_086094|||http://purl.uniprot.org/annotation/VAR_086095|||http://purl.uniprot.org/annotation/VAR_086096|||http://purl.uniprot.org/annotation/VAR_086097|||http://purl.uniprot.org/annotation/VAR_086099|||http://purl.uniprot.org/annotation/VAR_086100|||http://purl.uniprot.org/annotation/VAR_086101|||http://purl.uniprot.org/annotation/VAR_086102|||http://purl.uniprot.org/annotation/VAR_086103|||http://purl.uniprot.org/annotation/VAR_086104|||http://purl.uniprot.org/annotation/VAR_086105|||http://purl.uniprot.org/annotation/VSP_028859|||http://purl.uniprot.org/annotation/VSP_028860|||http://purl.uniprot.org/annotation/VSP_028861|||http://purl.uniprot.org/annotation/VSP_028862|||http://purl.uniprot.org/annotation/VSP_028863|||http://purl.uniprot.org/annotation/VSP_028864|||http://purl.uniprot.org/annotation/VSP_028865|||http://purl.uniprot.org/annotation/VSP_047048|||http://purl.uniprot.org/annotation/VSP_054757
http://togogenome.org/gene/9606:PANX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTT7|||http://purl.uniprot.org/uniprot/Q495U3|||http://purl.uniprot.org/uniprot/Q96RD6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 1 and isoform 2.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pannexin-2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208488|||http://purl.uniprot.org/annotation/VAR_036575|||http://purl.uniprot.org/annotation/VSP_002677|||http://purl.uniprot.org/annotation/VSP_039092
http://togogenome.org/gene/9606:PSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||PH|||PH and SEC7 domain-containing protein 2|||Phosphoserine|||Polar residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334162|||http://purl.uniprot.org/annotation/VAR_043346|||http://purl.uniprot.org/annotation/VAR_043347|||http://purl.uniprot.org/annotation/VAR_043348
http://togogenome.org/gene/9606:DLGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTP4|||http://purl.uniprot.org/uniprot/A8MXQ8|||http://purl.uniprot.org/uniprot/B7Z2J5|||http://purl.uniprot.org/uniprot/O14490|||http://purl.uniprot.org/uniprot/Q6IS01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disks large-associated protein 1|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Interaction with DYL2|||PDZ-binding|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174288|||http://purl.uniprot.org/annotation/VAR_053648|||http://purl.uniprot.org/annotation/VSP_006003|||http://purl.uniprot.org/annotation/VSP_006004|||http://purl.uniprot.org/annotation/VSP_006005|||http://purl.uniprot.org/annotation/VSP_006006|||http://purl.uniprot.org/annotation/VSP_043222|||http://purl.uniprot.org/annotation/VSP_043223|||http://purl.uniprot.org/annotation/VSP_043718|||http://purl.uniprot.org/annotation/VSP_043719|||http://purl.uniprot.org/annotation/VSP_043720|||http://purl.uniprot.org/annotation/VSP_043721|||http://purl.uniprot.org/annotation/VSP_043722|||http://purl.uniprot.org/annotation/VSP_043723
http://togogenome.org/gene/9606:YLPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49750|||http://purl.uniprot.org/uniprot/Q8NF45                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 1 and isoform 3.|||In isoform 3.|||Involved in interaction with PPP1CA|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||YLP motif-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066298|||http://purl.uniprot.org/annotation/VSP_059470|||http://purl.uniprot.org/annotation/VSP_059471|||http://purl.uniprot.org/annotation/VSP_059472
http://togogenome.org/gene/9606:BIRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13489                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 3|||Breakpoint for translocation to form BIRC3-MALT1|||CARD|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122349|||http://purl.uniprot.org/annotation/VAR_021069|||http://purl.uniprot.org/annotation/VAR_021070|||http://purl.uniprot.org/annotation/VAR_049536
http://togogenome.org/gene/9606:SPATA31A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31A6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297668
http://togogenome.org/gene/9606:ABTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969K4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat and BTB/POZ domain-containing protein 1|||BTB 1|||BTB 2|||In isoform 1.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248267|||http://purl.uniprot.org/annotation/VSP_052148|||http://purl.uniprot.org/annotation/VSP_052149|||http://purl.uniprot.org/annotation/VSP_052150|||http://purl.uniprot.org/annotation/VSP_052151|||http://purl.uniprot.org/annotation/VSP_052152|||http://purl.uniprot.org/annotation/VSP_052153
http://togogenome.org/gene/9606:OGFOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N543                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fe2OG dioxygenase|||In isoform 2.|||Loss of function.|||Nuclear localization signal|||Polar residues|||Prolyl 3-hydroxylase OGFOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288974|||http://purl.uniprot.org/annotation/VAR_032545|||http://purl.uniprot.org/annotation/VSP_025852
http://togogenome.org/gene/9606:HSPG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98160                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes BMP1-mediated cleavage of endorepellin.|||Basement membrane-specific heparan sulfate proteoglycan core protein|||Cleavage; by BMP1|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Endorepellin|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 13|||Ig-like C2-type 14|||Ig-like C2-type 15|||Ig-like C2-type 16|||Ig-like C2-type 17|||Ig-like C2-type 18|||Ig-like C2-type 19|||Ig-like C2-type 2|||Ig-like C2-type 20|||Ig-like C2-type 21|||Ig-like C2-type 22|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In SJS1.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LG3 peptide|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 1; first part|||Laminin EGF-like 1; second part|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4; truncated|||Laminin EGF-like 5; first part|||Laminin EGF-like 5; second part|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9; first part|||Laminin EGF-like 9; second part|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin IV type A 1|||Laminin IV type A 2|||Laminin IV type A 3|||Mediates motor neuron attachment|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (heparan sulfate) serine|||Retains proper folding. Reduced calcium ion binding.|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026696|||http://purl.uniprot.org/annotation/PRO_0000391621|||http://purl.uniprot.org/annotation/PRO_0000391622|||http://purl.uniprot.org/annotation/VAR_014122|||http://purl.uniprot.org/annotation/VAR_047979|||http://purl.uniprot.org/annotation/VAR_047980|||http://purl.uniprot.org/annotation/VAR_047981|||http://purl.uniprot.org/annotation/VAR_047982|||http://purl.uniprot.org/annotation/VAR_047983|||http://purl.uniprot.org/annotation/VAR_047984|||http://purl.uniprot.org/annotation/VAR_047985|||http://purl.uniprot.org/annotation/VAR_047986|||http://purl.uniprot.org/annotation/VAR_047987|||http://purl.uniprot.org/annotation/VAR_047988|||http://purl.uniprot.org/annotation/VAR_047989|||http://purl.uniprot.org/annotation/VAR_047990|||http://purl.uniprot.org/annotation/VAR_047991|||http://purl.uniprot.org/annotation/VAR_047992|||http://purl.uniprot.org/annotation/VAR_047993|||http://purl.uniprot.org/annotation/VAR_047994|||http://purl.uniprot.org/annotation/VAR_047995|||http://purl.uniprot.org/annotation/VAR_057051|||http://purl.uniprot.org/annotation/VAR_057052
http://togogenome.org/gene/9606:SLC6A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48066                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium- and chloride-dependent GABA transporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214784|||http://purl.uniprot.org/annotation/VSP_056539
http://togogenome.org/gene/9606:KIRREL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQV3|||http://purl.uniprot.org/uniprot/A0A0A0MRC1|||http://purl.uniprot.org/uniprot/Q6UWL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 5.|||Kin of IRRE-like protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015096|||http://purl.uniprot.org/annotation/PRO_5001967056|||http://purl.uniprot.org/annotation/PRO_5001967217|||http://purl.uniprot.org/annotation/VAR_056098|||http://purl.uniprot.org/annotation/VAR_056099|||http://purl.uniprot.org/annotation/VAR_056100|||http://purl.uniprot.org/annotation/VAR_056101|||http://purl.uniprot.org/annotation/VAR_067450|||http://purl.uniprot.org/annotation/VSP_011780|||http://purl.uniprot.org/annotation/VSP_011781|||http://purl.uniprot.org/annotation/VSP_011783|||http://purl.uniprot.org/annotation/VSP_011784|||http://purl.uniprot.org/annotation/VSP_011785
http://togogenome.org/gene/9606:TSSK1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0ZT98|||http://purl.uniprot.org/uniprot/Q9BXA7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Constitutively active.|||Disordered|||Loss of kinase activity.|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086766|||http://purl.uniprot.org/annotation/VAR_041235|||http://purl.uniprot.org/annotation/VAR_041236|||http://purl.uniprot.org/annotation/VAR_041237|||http://purl.uniprot.org/annotation/VAR_041238|||http://purl.uniprot.org/annotation/VAR_041239|||http://purl.uniprot.org/annotation/VAR_041240
http://togogenome.org/gene/9606:EMILIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXX0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen-like|||Disordered|||EMI|||EMILIN-2|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007817|||http://purl.uniprot.org/annotation/VAR_057528|||http://purl.uniprot.org/annotation/VAR_057529|||http://purl.uniprot.org/annotation/VAR_062003
http://togogenome.org/gene/9606:ARB2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUF8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cotranscriptional regulator FAM172A|||Disordered|||Found in a patient with CHARGES; unknown pathological significance.|||Found in patients with CHARGES; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Nucleophile|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320931|||http://purl.uniprot.org/annotation/VAR_039312|||http://purl.uniprot.org/annotation/VAR_080593|||http://purl.uniprot.org/annotation/VAR_080594|||http://purl.uniprot.org/annotation/VSP_031749|||http://purl.uniprot.org/annotation/VSP_043313|||http://purl.uniprot.org/annotation/VSP_043314
http://togogenome.org/gene/9606:CCT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48643                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HSNSP.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||T-complex protein 1 subunit epsilon                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128346|||http://purl.uniprot.org/annotation/VAR_030658|||http://purl.uniprot.org/annotation/VAR_052267|||http://purl.uniprot.org/annotation/VSP_054005|||http://purl.uniprot.org/annotation/VSP_054006
http://togogenome.org/gene/9606:GPLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80108                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol-glycan-specific phospholipase D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022047|||http://purl.uniprot.org/annotation/VAR_030743|||http://purl.uniprot.org/annotation/VAR_030744|||http://purl.uniprot.org/annotation/VAR_030745|||http://purl.uniprot.org/annotation/VAR_030746|||http://purl.uniprot.org/annotation/VAR_030747|||http://purl.uniprot.org/annotation/VAR_030748|||http://purl.uniprot.org/annotation/VAR_030749|||http://purl.uniprot.org/annotation/VAR_051278|||http://purl.uniprot.org/annotation/VSP_023261|||http://purl.uniprot.org/annotation/VSP_023262
http://togogenome.org/gene/9606:RAD51C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43502                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA repair protein RAD51 homolog 3|||In BROVCA3.|||In BROVCA3; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51.|||In FANCO; possibly hypomorphic allele; reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51.|||In isoform 2.|||Interaction with RAD51B, RAD51D and XRCC3|||Nuclear localization signal|||Partial loss of function.|||Phosphoserine|||Reduces interaction with BRCA2 and to a lesser extent with PALB2 and RAD51.|||Required for Holliday junction resolution activity|||Significant loss of function; abolishes Holliday junction resolution activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122941|||http://purl.uniprot.org/annotation/VAR_020518|||http://purl.uniprot.org/annotation/VAR_020519|||http://purl.uniprot.org/annotation/VAR_020520|||http://purl.uniprot.org/annotation/VAR_063837|||http://purl.uniprot.org/annotation/VAR_063838|||http://purl.uniprot.org/annotation/VAR_063839|||http://purl.uniprot.org/annotation/VAR_063840|||http://purl.uniprot.org/annotation/VAR_063841|||http://purl.uniprot.org/annotation/VAR_063842|||http://purl.uniprot.org/annotation/VAR_063843|||http://purl.uniprot.org/annotation/VAR_063844|||http://purl.uniprot.org/annotation/VAR_063845|||http://purl.uniprot.org/annotation/VAR_064032|||http://purl.uniprot.org/annotation/VAR_068014|||http://purl.uniprot.org/annotation/VAR_068015|||http://purl.uniprot.org/annotation/VAR_068016|||http://purl.uniprot.org/annotation/VAR_068017|||http://purl.uniprot.org/annotation/VAR_068018|||http://purl.uniprot.org/annotation/VAR_068019|||http://purl.uniprot.org/annotation/VAR_068020|||http://purl.uniprot.org/annotation/VSP_043656|||http://purl.uniprot.org/annotation/VSP_043657
http://togogenome.org/gene/9606:SPINT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5R1|||http://purl.uniprot.org/uniprot/Q6UDR6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Kunitz-type protease inhibitor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308327|||http://purl.uniprot.org/annotation/PRO_5017400789|||http://purl.uniprot.org/annotation/VAR_036795|||http://purl.uniprot.org/annotation/VAR_050068
http://togogenome.org/gene/9606:GMNC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCL1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region                                                                                  ^@                                                                                  Disordered|||Geminin coiled-coil domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346425
http://togogenome.org/gene/9606:CCNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclin-L2|||Cyclin-like 1|||Cyclin-like 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RS|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080487|||http://purl.uniprot.org/annotation/VSP_016130|||http://purl.uniprot.org/annotation/VSP_016131|||http://purl.uniprot.org/annotation/VSP_016132|||http://purl.uniprot.org/annotation/VSP_058301|||http://purl.uniprot.org/annotation/VSP_058302|||http://purl.uniprot.org/annotation/VSP_058303|||http://purl.uniprot.org/annotation/VSP_058304
http://togogenome.org/gene/9606:TSPAN18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SJ8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219268|||http://purl.uniprot.org/annotation/VAR_057279
http://togogenome.org/gene/9606:UBXN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68543                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||SEP|||UBX|||UBX domain-containing protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211031|||http://purl.uniprot.org/annotation/VSP_056306
http://togogenome.org/gene/9606:CNGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14028                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cyclic nucleotide-gated cation channel beta-1|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||IQ-like|||In RP45.|||In isoform 4.|||In isoform GARP2.|||In isoform RCNC2A.|||Loss of calcium/calmodulin modulation.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219323|||http://purl.uniprot.org/annotation/VAR_058691|||http://purl.uniprot.org/annotation/VAR_059225|||http://purl.uniprot.org/annotation/VAR_059226|||http://purl.uniprot.org/annotation/VAR_059227|||http://purl.uniprot.org/annotation/VAR_059228|||http://purl.uniprot.org/annotation/VAR_059229|||http://purl.uniprot.org/annotation/VAR_059230|||http://purl.uniprot.org/annotation/VAR_060491|||http://purl.uniprot.org/annotation/VSP_001110|||http://purl.uniprot.org/annotation/VSP_037921|||http://purl.uniprot.org/annotation/VSP_037922|||http://purl.uniprot.org/annotation/VSP_053421
http://togogenome.org/gene/9606:TRIM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQS5|||http://purl.uniprot.org/uniprot/Q8IYM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM22|||In isoform 2.|||Loss of E3 ubiquitin-protein ligase activity, reduces auto-ubiquitination and not affect nuclear bodies formation. Loss of antiviral activity; when associated with A-18.|||Loss of antiviral activity and not affect nuclear bodies formation; when associated with A-15.|||Nuclear localization signal|||RING-type|||Reduces formation of regular nuclear bodies.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056232|||http://purl.uniprot.org/annotation/VAR_052134|||http://purl.uniprot.org/annotation/VAR_052135|||http://purl.uniprot.org/annotation/VAR_052136|||http://purl.uniprot.org/annotation/VAR_052137|||http://purl.uniprot.org/annotation/VSP_012060
http://togogenome.org/gene/9606:SAMD9L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ATXPC and M7MLS1.|||In ATXPC; unknown pathological significance.|||In M7MLS1.|||In SCA49; results in motor and sensory impairments when expressed in zebrafish.|||In isoform 2.|||SAM|||Sterile alpha motif domain-containing protein 9-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279498|||http://purl.uniprot.org/annotation/VAR_030911|||http://purl.uniprot.org/annotation/VAR_030912|||http://purl.uniprot.org/annotation/VAR_030913|||http://purl.uniprot.org/annotation/VAR_030914|||http://purl.uniprot.org/annotation/VAR_077034|||http://purl.uniprot.org/annotation/VAR_077035|||http://purl.uniprot.org/annotation/VAR_085144|||http://purl.uniprot.org/annotation/VAR_085145|||http://purl.uniprot.org/annotation/VAR_085146|||http://purl.uniprot.org/annotation/VAR_087095|||http://purl.uniprot.org/annotation/VSP_027875
http://togogenome.org/gene/9606:SEMA4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0C4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dominant negative effect on myogenic differentiation|||Extracellular|||Helical|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||PSI|||Phosphoserine|||Pro residues|||Sema|||Semaphorin-4C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032325
http://togogenome.org/gene/9606:DEFB116                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KQ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 116|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045344|||http://purl.uniprot.org/annotation/VAR_048863
http://togogenome.org/gene/9606:WDR62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43379                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MCPH2.|||In MCPH2; the mutant protein does not localize to the spindle pole during mitosis.|||In MCPH2; uncertain pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281879|||http://purl.uniprot.org/annotation/VAR_031299|||http://purl.uniprot.org/annotation/VAR_031300|||http://purl.uniprot.org/annotation/VAR_031301|||http://purl.uniprot.org/annotation/VAR_055014|||http://purl.uniprot.org/annotation/VAR_055015|||http://purl.uniprot.org/annotation/VAR_057629|||http://purl.uniprot.org/annotation/VAR_063702|||http://purl.uniprot.org/annotation/VAR_063703|||http://purl.uniprot.org/annotation/VAR_065843|||http://purl.uniprot.org/annotation/VAR_065844|||http://purl.uniprot.org/annotation/VAR_065845|||http://purl.uniprot.org/annotation/VAR_082935|||http://purl.uniprot.org/annotation/VSP_024077|||http://purl.uniprot.org/annotation/VSP_024078|||http://purl.uniprot.org/annotation/VSP_024079|||http://purl.uniprot.org/annotation/VSP_024080|||http://purl.uniprot.org/annotation/VSP_039906
http://togogenome.org/gene/9606:PNMA8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 1.|||Paraneoplastic antigen-like protein 8B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325839|||http://purl.uniprot.org/annotation/VSP_059423|||http://purl.uniprot.org/annotation/VSP_059424
http://togogenome.org/gene/9606:PLAGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1YLA1|||http://purl.uniprot.org/uniprot/A1YLA2|||http://purl.uniprot.org/uniprot/Q9UM63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||In isoform 2.|||Zinc finger protein PLAGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047222|||http://purl.uniprot.org/annotation/VAR_052729|||http://purl.uniprot.org/annotation/VSP_028123
http://togogenome.org/gene/9606:GJC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFK1                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gap junction gamma-3 protein|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057874
http://togogenome.org/gene/9606:PRXL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRV4|||http://purl.uniprot.org/uniprot/A0A0A0MT35|||http://purl.uniprot.org/uniprot/A0A2P0CTB1|||http://purl.uniprot.org/uniprot/A0A2P0CU24|||http://purl.uniprot.org/uniprot/Q8TBF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||Phosphotyrosine|||Prostamide/prostaglandin F synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284637|||http://purl.uniprot.org/annotation/VSP_024581|||http://purl.uniprot.org/annotation/VSP_040901|||http://purl.uniprot.org/annotation/VSP_040903|||http://purl.uniprot.org/annotation/VSP_040904
http://togogenome.org/gene/9606:METTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBP6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished RNA methyltransferase activity.|||Abolished interaction with WDR4; when associated with D-143, D-151 and D-172.|||Abolished interaction with WDR4; when associated with D-40, D-143 and D-151.|||Abolished interaction with WDR4; when associated with D-40, D-143 and D-172.|||Abolished interaction with WDR4; when associated with D-40, D-151 and D-172.|||Abolished methyltransferase activity.|||Abolished methyltransferase activity. Abolished tRNA-binding; when associated with A-165, A-170, A-243 and A-246.|||Abolished phosphorylation; does not affect methyltransferase activity.|||Abolished tRNA-binding; when associated with A-165, A-167, A-243 and A-246.|||Abolished tRNA-binding; when associated with A-167, A-170, A-243 and A-246.|||Alpha6 helix|||AlphaC helix|||Disordered|||Does not affect methyltransferase activity.|||In isoform 2.|||Mimics phosphorylation; abolished affect methyltransferase activity.|||N-acetylalanine|||Phosphoserine; by PKB/AKT1 and RPS6KA3|||Removed|||Slightly reduced methyltransferase activity.|||Slightly reduced tRNA-binding. Abolished tRNA-binding; when associated with A-165, A-167, A-170 and A-243. Does not affect methyltransferase activity.|||Slightly reduced tRNA-binding. Abolished tRNA-binding; when associated with A-165, A-167, A-170 and A-246. Strongly reduced methyltransferase activity.|||Strongly reduced methyltransferase activity.|||tRNA (guanine-N(7)-)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171431|||http://purl.uniprot.org/annotation/VSP_044671|||http://purl.uniprot.org/annotation/VSP_044672
http://togogenome.org/gene/9606:WNK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J92                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished MAP3K15/ASK3-dependent phosphorylation.|||Abolished interaction with OXSR1/OSR1.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In PHA2B.|||In PHA2B; impaired interaction with KLHL3.|||In a metastatic melanoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with KLHL3|||Mimics phosphorylation without affecting WNK4 kinase activity.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||RFXV motif|||Serine/threonine-protein kinase WNK4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086824|||http://purl.uniprot.org/annotation/VAR_017588|||http://purl.uniprot.org/annotation/VAR_017589|||http://purl.uniprot.org/annotation/VAR_017590|||http://purl.uniprot.org/annotation/VAR_017591|||http://purl.uniprot.org/annotation/VAR_041330|||http://purl.uniprot.org/annotation/VAR_041331|||http://purl.uniprot.org/annotation/VAR_041332|||http://purl.uniprot.org/annotation/VAR_041333|||http://purl.uniprot.org/annotation/VAR_051685|||http://purl.uniprot.org/annotation/VAR_051686|||http://purl.uniprot.org/annotation/VAR_061748|||http://purl.uniprot.org/annotation/VSP_050648|||http://purl.uniprot.org/annotation/VSP_050649|||http://purl.uniprot.org/annotation/VSP_050650|||http://purl.uniprot.org/annotation/VSP_050651|||http://purl.uniprot.org/annotation/VSP_050652|||http://purl.uniprot.org/annotation/VSP_050653
http://togogenome.org/gene/9606:BCAP31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51572                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-164.|||Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-238.|||B-cell receptor-associated protein 31|||Cleavage; by caspase-8|||Cytoplasmic|||Di-lysine motif|||Helical|||In isoform 2.|||Lumenal|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142891|||http://purl.uniprot.org/annotation/VSP_043116
http://togogenome.org/gene/9606:SNX29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PX|||Phosphoserine|||Phosphothreonine|||RUN|||Sorting nexin-29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297565|||http://purl.uniprot.org/annotation/VSP_027281
http://togogenome.org/gene/9606:TAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHF0                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In HH10; has markedly reduced activity.|||In HH10; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; the patient also carries a mutation in HS6ST1.|||In isoform 2.|||In isoform 3.|||Methionine amide|||Neurokinin-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033565|||http://purl.uniprot.org/annotation/PRO_0000033566|||http://purl.uniprot.org/annotation/PRO_0000033567|||http://purl.uniprot.org/annotation/VAR_069176|||http://purl.uniprot.org/annotation/VAR_069969|||http://purl.uniprot.org/annotation/VSP_013186|||http://purl.uniprot.org/annotation/VSP_013187
http://togogenome.org/gene/9606:ANKH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCJ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in individuals of a consanguinous family with intellectual disability syndrome, deafness and ankylosis; likely pathogenic variant; localizes at the plasma membrane; loss-of-function.|||Helical|||In CCAL2.|||In CCAL2; sporadic.|||In CMDD.|||In isoform 2.|||Mineralization regulator ANKH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137467|||http://purl.uniprot.org/annotation/VAR_012192|||http://purl.uniprot.org/annotation/VAR_012193|||http://purl.uniprot.org/annotation/VAR_012194|||http://purl.uniprot.org/annotation/VAR_012195|||http://purl.uniprot.org/annotation/VAR_012196|||http://purl.uniprot.org/annotation/VAR_012197|||http://purl.uniprot.org/annotation/VAR_012198|||http://purl.uniprot.org/annotation/VAR_017556|||http://purl.uniprot.org/annotation/VAR_017557|||http://purl.uniprot.org/annotation/VAR_022606|||http://purl.uniprot.org/annotation/VAR_022607|||http://purl.uniprot.org/annotation/VAR_088435|||http://purl.uniprot.org/annotation/VSP_055824
http://togogenome.org/gene/9606:KLHL38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2WGJ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325809|||http://purl.uniprot.org/annotation/VAR_059437|||http://purl.uniprot.org/annotation/VAR_059438|||http://purl.uniprot.org/annotation/VAR_059439|||http://purl.uniprot.org/annotation/VAR_059440|||http://purl.uniprot.org/annotation/VAR_060485|||http://purl.uniprot.org/annotation/VAR_060486
http://togogenome.org/gene/9606:ERP27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DN0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Conserved PDIA3 binding in vivo and in vitro.|||Decreases somatostatin-14 binding.|||Endoplasmic reticulum resident protein 27|||Greatly reduces PDIA3 binding in vivo and in vitro.|||N-linked (GlcNAc...) asparagine|||PDIA3-binding site|||Prevents secretion from ER|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281118|||http://purl.uniprot.org/annotation/VAR_052582
http://togogenome.org/gene/9606:ZNF831                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPB2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Polar residues|||Pro residues|||Zinc finger protein 831                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236041|||http://purl.uniprot.org/annotation/VAR_026472|||http://purl.uniprot.org/annotation/VAR_026473|||http://purl.uniprot.org/annotation/VAR_069367
http://togogenome.org/gene/9606:CCDC28A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUJ5|||http://purl.uniprot.org/uniprot/Q8IWP9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Breakpoint for translocation to form NUP98-CCDC28A|||Coiled-coil domain-containing protein 28A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089411|||http://purl.uniprot.org/annotation/VAR_050744|||http://purl.uniprot.org/annotation/VAR_050745
http://togogenome.org/gene/9606:TBX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57082                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In ICPPS.|||In PAPPAS; also responsible for ischiocoxopodopatellar syndrome in heterozygous carriers; no detectable protein expression in homozygous patient cells.|||In isoform 2.|||Phosphoserine|||T-box|||T-box transcription factor TBX4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184433|||http://purl.uniprot.org/annotation/VAR_020251|||http://purl.uniprot.org/annotation/VAR_021983|||http://purl.uniprot.org/annotation/VAR_026745|||http://purl.uniprot.org/annotation/VAR_026746|||http://purl.uniprot.org/annotation/VAR_026772|||http://purl.uniprot.org/annotation/VAR_078493|||http://purl.uniprot.org/annotation/VAR_083526|||http://purl.uniprot.org/annotation/VSP_054002
http://togogenome.org/gene/9606:MTHFD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13995                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  50% decrease in NAD and NADP-dependent dehydrogenase specific activity. Reduced affinity for magnesium.|||80% decrease in NAD-dependent dehydrogenase specific activity. 18% decrease in NADP-dependent dehydrogenase specific activity. Reduced affinity for magnesium.|||82% decrease in NAD-dependent dehydrogenase specific activity. 65% decrease in NADP-dependent dehydrogenase specific activity. Reduced affinity for magnesium.|||84% decrease in NAD-dependent dehydrogenase specific activity. 36% increase in NADP-dependent dehydrogenase specific activity. Reduced affinity for magnesium.|||Almost complete loss of NAD-dependent dehydrogenase specific activity. 50% decrease in NADP-dependent dehydrogenase specific activity.|||Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial|||Complete loss of NAD and NADP-dependent dehydrogenase specific activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||Significant loss of NAD and NADP-dependent dehydrogenase specific activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034049|||http://purl.uniprot.org/annotation/VSP_056188
http://togogenome.org/gene/9606:IL2RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y5Z0|||http://purl.uniprot.org/uniprot/P01589|||http://purl.uniprot.org/uniprot/Q5W005                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In IMD41.|||In IMD41; the receptor does not localize to the plasma membrane.|||Interleukin-2 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011024|||http://purl.uniprot.org/annotation/PRO_5014105998|||http://purl.uniprot.org/annotation/PRO_5036466988|||http://purl.uniprot.org/annotation/VAR_019280|||http://purl.uniprot.org/annotation/VAR_074641|||http://purl.uniprot.org/annotation/VAR_074642
http://togogenome.org/gene/9606:MAN2C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN9|||http://purl.uniprot.org/uniprot/Q9NTJ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-mannosidase 2C1|||Glycoside hydrolase family 38 central|||In CDDG2; unknown pathological significance; has no effect on processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells.|||In CDDG2; unknown pathological significance; results in defective processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells.|||In CDDG2; unknown pathological significance; severely decreased mannosidase activity; results in defective processing of free oligosaccharides as shown by complementation assay in MAN2C1-deficient cells.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206907|||http://purl.uniprot.org/annotation/VAR_021914|||http://purl.uniprot.org/annotation/VAR_049211|||http://purl.uniprot.org/annotation/VAR_049212|||http://purl.uniprot.org/annotation/VAR_061192|||http://purl.uniprot.org/annotation/VAR_069180|||http://purl.uniprot.org/annotation/VAR_087012|||http://purl.uniprot.org/annotation/VAR_087013|||http://purl.uniprot.org/annotation/VAR_087014|||http://purl.uniprot.org/annotation/VSP_046375|||http://purl.uniprot.org/annotation/VSP_046395|||http://purl.uniprot.org/annotation/VSP_046895
http://togogenome.org/gene/9606:ND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03897|||http://purl.uniprot.org/uniprot/Q7GXZ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In LS and MC1DM1.|||In LS; unknown pathological significance; decrease in enzyme activity.|||In MC1DM1.|||NADH-ubiquinone oxidoreductase chain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117752|||http://purl.uniprot.org/annotation/VAR_008391|||http://purl.uniprot.org/annotation/VAR_008392|||http://purl.uniprot.org/annotation/VAR_008598|||http://purl.uniprot.org/annotation/VAR_035091|||http://purl.uniprot.org/annotation/VAR_035092|||http://purl.uniprot.org/annotation/VAR_064564|||http://purl.uniprot.org/annotation/VAR_084384
http://togogenome.org/gene/9606:RFPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75677                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||Increased cell proliferation, reduced apoptosis and lack of cyclin B1/CCNB1 and CDK1 degradation.|||Increased cell proliferation.|||No effect on cell proliferation.|||RING-type|||Reduced phosphorylation by CDK1.|||Reduced phosphorylation by PKC, increased cell proliferation, reduced apoptosis and lack of cyclin B1/CCNB1 and CDK1 degradation.|||Ret finger protein-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056030|||http://purl.uniprot.org/annotation/VAR_020115|||http://purl.uniprot.org/annotation/VAR_039572|||http://purl.uniprot.org/annotation/VAR_039573|||http://purl.uniprot.org/annotation/VAR_080854|||http://purl.uniprot.org/annotation/VAR_080855
http://togogenome.org/gene/9606:ADH1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RHZ6|||http://purl.uniprot.org/uniprot/P00325|||http://purl.uniprot.org/uniprot/V9HW50                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alcohol dehydrogenase-like C-terminal|||Alcohol dehydrogenase-like N-terminal|||All-trans-retinol dehydrogenase [NAD(+)] ADH1B|||Enoyl reductase (ER)|||In beta-3/Indianapolis; allele ADH1B*3; decreased NAD(H) binding.|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160661|||http://purl.uniprot.org/annotation/VAR_000426|||http://purl.uniprot.org/annotation/VAR_000427|||http://purl.uniprot.org/annotation/VAR_019322|||http://purl.uniprot.org/annotation/VAR_019323|||http://purl.uniprot.org/annotation/VSP_054847
http://togogenome.org/gene/9606:SCN10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Y9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||Helical; Voltage-sensor; Name=S4 of repeat I|||Helical; Voltage-sensor; Name=S4 of repeat II|||Helical; Voltage-sensor; Name=S4 of repeat III|||Helical; Voltage-sensor; Name=S4 of repeat IV|||I|||II|||III|||IQ|||IV|||In FEPS2; increases the excitability of small DRG neurons.|||N-linked (GlcNAc...) asparagine|||No gain in function in response to depolarization.|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Sodium channel protein type 10 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048507|||http://purl.uniprot.org/annotation/VAR_020605|||http://purl.uniprot.org/annotation/VAR_020606|||http://purl.uniprot.org/annotation/VAR_020607|||http://purl.uniprot.org/annotation/VAR_020608|||http://purl.uniprot.org/annotation/VAR_048696|||http://purl.uniprot.org/annotation/VAR_064748|||http://purl.uniprot.org/annotation/VAR_070878|||http://purl.uniprot.org/annotation/VAR_070879|||http://purl.uniprot.org/annotation/VAR_070880|||http://purl.uniprot.org/annotation/VAR_070881|||http://purl.uniprot.org/annotation/VAR_070882|||http://purl.uniprot.org/annotation/VAR_070883|||http://purl.uniprot.org/annotation/VAR_070884
http://togogenome.org/gene/9606:ZIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95409                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HPE5.|||In HPE5; 2-fold increase in luciferase activity.|||In HPE5; near-complete loss of luciferase activity.|||In HPE5; requires 2 nucleotide substitutions; 50% reduction of luciferase activity.|||Necessary for interaction with MDFIC and transcriptional activation or repression|||Phosphoserine|||Polar residues|||Zinc finger protein ZIC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047247|||http://purl.uniprot.org/annotation/VAR_008856|||http://purl.uniprot.org/annotation/VAR_023793|||http://purl.uniprot.org/annotation/VAR_023794|||http://purl.uniprot.org/annotation/VAR_023795|||http://purl.uniprot.org/annotation/VAR_023796|||http://purl.uniprot.org/annotation/VAR_058592|||http://purl.uniprot.org/annotation/VAR_058593|||http://purl.uniprot.org/annotation/VAR_058594|||http://purl.uniprot.org/annotation/VAR_058595|||http://purl.uniprot.org/annotation/VAR_058596|||http://purl.uniprot.org/annotation/VAR_058597|||http://purl.uniprot.org/annotation/VAR_058598|||http://purl.uniprot.org/annotation/VAR_058599|||http://purl.uniprot.org/annotation/VAR_058600|||http://purl.uniprot.org/annotation/VAR_058601|||http://purl.uniprot.org/annotation/VAR_058602|||http://purl.uniprot.org/annotation/VAR_058603|||http://purl.uniprot.org/annotation/VAR_058604|||http://purl.uniprot.org/annotation/VAR_058605|||http://purl.uniprot.org/annotation/VAR_058606|||http://purl.uniprot.org/annotation/VAR_058607|||http://purl.uniprot.org/annotation/VAR_058608|||http://purl.uniprot.org/annotation/VAR_058609|||http://purl.uniprot.org/annotation/VAR_058610
http://togogenome.org/gene/9606:SOCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15524|||http://purl.uniprot.org/uniprot/Q4JHT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Extended SH2 subdomain (ESS)|||In AISIMD; heterozygous T-cells show increased levels of STAT1 phosphorylation following treatment with IFNG, compared to control cells.|||In AISIMD; loss of inhibition of cytokine-induced STAT phosphorylation, including IFNG-induced STAT1 phosphorylation, IL2-induced STAT5 phosphorylation and IL4-induced STAT6 phosphorylation.|||In AISIMD; unknown pathological significance; when transfected into HEK293T cells, shows impaired suppression of IFNG-mediated gene expression compared to wild-type.|||Interaction with Elongin BC complex|||Kinase inhibitory region (KIR)|||Polar residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181235|||http://purl.uniprot.org/annotation/VAR_061808|||http://purl.uniprot.org/annotation/VAR_085947|||http://purl.uniprot.org/annotation/VAR_085948|||http://purl.uniprot.org/annotation/VAR_085949|||http://purl.uniprot.org/annotation/VAR_085950
http://togogenome.org/gene/9606:GNPDA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46926                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases catalytic efficiency.|||Decreases hexamer stability and catalytic efficiency.|||For ring-opening step|||Glucosamine-6-phosphate isomerase 1|||In isoform 2.|||N6-acetyllysine|||Phosphothreonine|||Proton acceptor; for enolization step|||Proton acceptor; for ring-opening step                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160122|||http://purl.uniprot.org/annotation/VSP_057011
http://togogenome.org/gene/9606:CREM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03060                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||In isoform 10, isoform 11 and isoform 19.|||In isoform 11 and isoform 12.|||In isoform 12 and isoform 11.|||In isoform 15.|||In isoform 16.|||In isoform 17 and isoform 18.|||In isoform 2, isoform 3, isoform 4, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 23, isoform 28 and isoform 29.|||In isoform 2, isoform 3, isoform 5, isoform 10, isoform 14, isoform 15, isoform 25 and isoform 28.|||In isoform 20.|||In isoform 21 and isoform 24.|||In isoform 22.|||In isoform 23.|||In isoform 25.|||In isoform 26.|||In isoform 3, isoform 6, isoform 7, isoform 18, isoform 20, isoform 21, isoform 23, isoform 28 and isoform 29.|||In isoform 4, isoform 13, isoform 14, isoform 22, isoform 23, isoform 27, isoform 28 and isoform 29.|||In isoform 4, isoform 27 and isoform 29.|||In isoform 5 and isoform 12.|||In isoform 6 and isoform 8.|||In isoform 7 and isoform 9.|||KID|||Leucine-zipper|||Phosphoserine|||bZIP|||cAMP-responsive element modulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076607|||http://purl.uniprot.org/annotation/VAR_055561|||http://purl.uniprot.org/annotation/VSP_059697|||http://purl.uniprot.org/annotation/VSP_059698|||http://purl.uniprot.org/annotation/VSP_059699|||http://purl.uniprot.org/annotation/VSP_059700|||http://purl.uniprot.org/annotation/VSP_059701|||http://purl.uniprot.org/annotation/VSP_059702|||http://purl.uniprot.org/annotation/VSP_059703|||http://purl.uniprot.org/annotation/VSP_059704|||http://purl.uniprot.org/annotation/VSP_059705|||http://purl.uniprot.org/annotation/VSP_059706|||http://purl.uniprot.org/annotation/VSP_059707|||http://purl.uniprot.org/annotation/VSP_059708|||http://purl.uniprot.org/annotation/VSP_059709|||http://purl.uniprot.org/annotation/VSP_059710|||http://purl.uniprot.org/annotation/VSP_059711|||http://purl.uniprot.org/annotation/VSP_059712|||http://purl.uniprot.org/annotation/VSP_059713|||http://purl.uniprot.org/annotation/VSP_059714|||http://purl.uniprot.org/annotation/VSP_059715|||http://purl.uniprot.org/annotation/VSP_059716|||http://purl.uniprot.org/annotation/VSP_059717
http://togogenome.org/gene/9606:C2orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P641                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C2orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326123|||http://purl.uniprot.org/annotation/VAR_050717|||http://purl.uniprot.org/annotation/VAR_050718|||http://purl.uniprot.org/annotation/VAR_050719
http://togogenome.org/gene/9606:SERPINA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDH1|||http://purl.uniprot.org/uniprot/P05154                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Does not change inhibition of thrombin, activated protein C/F5 and factor XI/F11 activities.|||Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin.|||Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Slightly reduces the rate of thrombin inhibition in the presence of heparin. Inhibits weakly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin.|||Does not change the rate of thrombin or activated protein C/F5 inhibition in the presence or absence of heparin. Strongly reduces the rate of thrombin inhibition in the presence of heparin.|||Does not inhibit thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin.|||In allele PCI*B.|||Increases inhibition of activated protein C/F5 and factor XI/F11 activities. Decreases inhibition of thrombin activity.|||Increases inhibition of thrombin activity.|||Increases inhibition of thrombin activity. Inhibits heterodimer formation with TMPRSS11E.|||Inhibits heterodimer formation with TMPRSS11E.|||Inhibits strongly thrombomodulin-enhanced rate of thrombin inhibition in presence of heparin.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Plasma serine protease inhibitor|||Reactive bond|||Removed in mature form|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032427|||http://purl.uniprot.org/annotation/PRO_0000414091|||http://purl.uniprot.org/annotation/VAR_007100|||http://purl.uniprot.org/annotation/VAR_007101|||http://purl.uniprot.org/annotation/VAR_013080|||http://purl.uniprot.org/annotation/VAR_013081|||http://purl.uniprot.org/annotation/VAR_013082|||http://purl.uniprot.org/annotation/VAR_013083|||http://purl.uniprot.org/annotation/VAR_013084|||http://purl.uniprot.org/annotation/VAR_013900
http://togogenome.org/gene/9606:HSCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYJ4|||http://purl.uniprot.org/uniprot/B0QYH2|||http://purl.uniprot.org/uniprot/Q8IWL3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-44 and S-58.|||Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-44 and S-61.|||Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-58 and S-61.|||Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-44; S-58 and S-61.|||Co-chaperone HscB C-terminal oligomerisation|||Does not interact with HSPA9. Does not inhibit interaction with ISCU.|||HscB tetracysteine metal binding motif|||Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic|||Iron-sulfur cluster co-chaperone protein HscB, mitochondrial|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007262|||http://purl.uniprot.org/annotation/PRO_0000446242|||http://purl.uniprot.org/annotation/VAR_048916|||http://purl.uniprot.org/annotation/VAR_048917
http://togogenome.org/gene/9606:DOCK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 4|||Disordered|||Found in a CNS cancer cell line.|||Found in a prostate cancer cell line.|||Found in colorectal cancer cell line.|||Found in prostate and ovarian cancer cell lines; abolishes ability to interact with CRK and to activate Rap1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189990|||http://purl.uniprot.org/annotation/VAR_015823|||http://purl.uniprot.org/annotation/VAR_015824|||http://purl.uniprot.org/annotation/VAR_015825|||http://purl.uniprot.org/annotation/VAR_015826|||http://purl.uniprot.org/annotation/VAR_015827|||http://purl.uniprot.org/annotation/VAR_015828|||http://purl.uniprot.org/annotation/VAR_015829|||http://purl.uniprot.org/annotation/VAR_015830|||http://purl.uniprot.org/annotation/VAR_015831|||http://purl.uniprot.org/annotation/VAR_015832|||http://purl.uniprot.org/annotation/VAR_057517|||http://purl.uniprot.org/annotation/VAR_057518|||http://purl.uniprot.org/annotation/VAR_057519|||http://purl.uniprot.org/annotation/VAR_057520|||http://purl.uniprot.org/annotation/VAR_057521|||http://purl.uniprot.org/annotation/VSP_007701|||http://purl.uniprot.org/annotation/VSP_007703|||http://purl.uniprot.org/annotation/VSP_007705|||http://purl.uniprot.org/annotation/VSP_007706
http://togogenome.org/gene/9606:OVOL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00110                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Polar residues|||Putative transcription factor ovo-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320622
http://togogenome.org/gene/9606:FGGY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C11                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FGGY carbohydrate kinase domain-containing protein|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326452|||http://purl.uniprot.org/annotation/VAR_040072|||http://purl.uniprot.org/annotation/VAR_059193|||http://purl.uniprot.org/annotation/VAR_059194|||http://purl.uniprot.org/annotation/VSP_032658|||http://purl.uniprot.org/annotation/VSP_032659|||http://purl.uniprot.org/annotation/VSP_033424|||http://purl.uniprot.org/annotation/VSP_045338|||http://purl.uniprot.org/annotation/VSP_054533
http://togogenome.org/gene/9606:RPAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes dephosphorylation of ERN1; when associated with 2-A--L-32 DEL.|||Abolishes dephosphorylation of ERN1; when associated with 275-G--E-612 DEL.|||Abolishes interaction with RNA polymerase II complex subunits; when associated with A-100.|||Abolishes interaction with RNA polymerase II complex subunits; when associated with A-105.|||Abolishes interaction with RNA polymerase II complex subunits; when associated with A-136.|||Abolishes interaction with RNA polymerase II complex subunits; when associated with A-140.|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2|||RTR1-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250648|||http://purl.uniprot.org/annotation/VSP_020680|||http://purl.uniprot.org/annotation/VSP_020681
http://togogenome.org/gene/9606:POTEB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BUK9|||http://purl.uniprot.org/uniprot/Q495V5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member B2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423303
http://togogenome.org/gene/9606:TLR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R933|||http://purl.uniprot.org/uniprot/Q9Y2C9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not inhibit homodimer formation.|||Extracellular|||Helical|||Impairs the ability to induce NF-kappa-B activation.|||In isoform 2.|||Inhibits homodimer formation.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034731|||http://purl.uniprot.org/annotation/VAR_057289|||http://purl.uniprot.org/annotation/VAR_057290|||http://purl.uniprot.org/annotation/VAR_057291|||http://purl.uniprot.org/annotation/VAR_057292|||http://purl.uniprot.org/annotation/VAR_057293|||http://purl.uniprot.org/annotation/VAR_057294|||http://purl.uniprot.org/annotation/VAR_057295|||http://purl.uniprot.org/annotation/VAR_057296|||http://purl.uniprot.org/annotation/VAR_057297|||http://purl.uniprot.org/annotation/VAR_063110|||http://purl.uniprot.org/annotation/VAR_066352|||http://purl.uniprot.org/annotation/VAR_066353|||http://purl.uniprot.org/annotation/VAR_066354|||http://purl.uniprot.org/annotation/VAR_066355|||http://purl.uniprot.org/annotation/VAR_066356|||http://purl.uniprot.org/annotation/VAR_066357|||http://purl.uniprot.org/annotation/VAR_066358|||http://purl.uniprot.org/annotation/VAR_066359|||http://purl.uniprot.org/annotation/VAR_066360|||http://purl.uniprot.org/annotation/VSP_056851
http://togogenome.org/gene/9606:TRIM33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN30|||http://purl.uniprot.org/uniprot/Q9UPN9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125.|||Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||B box-type 1|||B box-type 2|||Basic and acidic residues|||Breakpoint for translocation to form TRIM33-RET oncogene|||Bromo|||Disordered|||E3 ubiquitin-protein ligase TRIM33|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform Beta.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for E3 ubiquitin-protein ligase activity and repression of SMAD4 signaling and transcriptional repression|||Necessary for oligomerization|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056395|||http://purl.uniprot.org/annotation/VAR_024616|||http://purl.uniprot.org/annotation/VAR_029494|||http://purl.uniprot.org/annotation/VAR_042376|||http://purl.uniprot.org/annotation/VAR_042377|||http://purl.uniprot.org/annotation/VAR_042378|||http://purl.uniprot.org/annotation/VAR_042379|||http://purl.uniprot.org/annotation/VAR_042380|||http://purl.uniprot.org/annotation/VAR_042381|||http://purl.uniprot.org/annotation/VSP_005774
http://togogenome.org/gene/9606:DPP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2E4|||http://purl.uniprot.org/uniprot/B7Z299|||http://purl.uniprot.org/uniprot/E9PDL2|||http://purl.uniprot.org/uniprot/E9PF59|||http://purl.uniprot.org/uniprot/P42658|||http://purl.uniprot.org/uniprot/Q8IYG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Dipeptidyl aminopeptidase-like protein 6|||Dipeptidylpeptidase IV N-terminal|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In MRD33.|||In isoform DPPX-S.|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122409|||http://purl.uniprot.org/annotation/VAR_051579|||http://purl.uniprot.org/annotation/VAR_073680|||http://purl.uniprot.org/annotation/VSP_005365
http://togogenome.org/gene/9606:BUD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRD0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BUD13 homolog|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287688|||http://purl.uniprot.org/annotation/VAR_032343|||http://purl.uniprot.org/annotation/VAR_032344|||http://purl.uniprot.org/annotation/VAR_032345|||http://purl.uniprot.org/annotation/VAR_053908|||http://purl.uniprot.org/annotation/VSP_025590
http://togogenome.org/gene/9606:PPIAL4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2A2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433924
http://togogenome.org/gene/9606:MGAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09327                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188842
http://togogenome.org/gene/9606:CCND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP19|||http://purl.uniprot.org/uniprot/P30281|||http://purl.uniprot.org/uniprot/Q5T8J1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cyclin C-terminal|||Cyclin N-terminal|||Cyclin-like|||Disordered|||G1/S-specific cyclin-D3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080442|||http://purl.uniprot.org/annotation/VAR_014205|||http://purl.uniprot.org/annotation/VAR_020412|||http://purl.uniprot.org/annotation/VAR_033726|||http://purl.uniprot.org/annotation/VSP_042649|||http://purl.uniprot.org/annotation/VSP_046266|||http://purl.uniprot.org/annotation/VSP_046267
http://togogenome.org/gene/9606:VPREB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKI3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ig-like|||Pre-B lymphocyte protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015003|||http://purl.uniprot.org/annotation/VAR_049954
http://togogenome.org/gene/9606:CRISP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1I1|||http://purl.uniprot.org/uniprot/P54107                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine-rich secretory protein 1|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||SCP|||ShKT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006260|||http://purl.uniprot.org/annotation/PRO_5010036195|||http://purl.uniprot.org/annotation/VSP_006027|||http://purl.uniprot.org/annotation/VSP_006028
http://togogenome.org/gene/9606:TUT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYS8|||http://purl.uniprot.org/uniprot/Q96KX5|||http://purl.uniprot.org/uniprot/X6R3Q3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes inhibition of LIRE1 retrotransposition.|||Abolishes monouridylation activity.|||Acidic residues|||Basic and acidic residues|||CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Matrin-type|||PAP-associated 1|||PAP-associated 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sufficient for monouridylation activity|||Terminal uridylyltransferase 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150957|||http://purl.uniprot.org/annotation/VAR_053753|||http://purl.uniprot.org/annotation/VSP_013832|||http://purl.uniprot.org/annotation/VSP_013833|||http://purl.uniprot.org/annotation/VSP_013834|||http://purl.uniprot.org/annotation/VSP_013835|||http://purl.uniprot.org/annotation/VSP_013836|||http://purl.uniprot.org/annotation/VSP_013837|||http://purl.uniprot.org/annotation/VSP_013838|||http://purl.uniprot.org/annotation/VSP_013839|||http://purl.uniprot.org/annotation/VSP_013840
http://togogenome.org/gene/9606:SPOPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ16                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  BTB|||MATH|||Speckle-type POZ protein-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274588|||http://purl.uniprot.org/annotation/VAR_053719
http://togogenome.org/gene/9606:LDLR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01130                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold decreased affinity for LDLRAP1.|||3-fold decreased affinity for LDLRAP1.|||Abolishes interaction with ARRB2.|||Clustered O-linked oligosaccharides|||Cytoplasmic|||Decreased affinity for LDLRAP1.|||Disordered|||Does not affect receptor expression at the cell surface; does not affect LDL binding; does not affect LDL uptake and internalization.|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||Enhances interaction with ARRB2 and receptor internalization.|||Extracellular|||Found in a patient with hypercholesterolemia.|||Helical|||In Baltimore-1.|||In Bretagne-1.|||In Charlotte.|||In Chieti-3.|||In Denver-2.|||In El Salvador-1.|||In FHCL1.|||In FHCL1; Afrikaner-1/Maine; 65-70% of Afrikaner Americans.|||In FHCL1; Afrikaner-2; 20-30% of Afrikaners and 2% of FHCL1 Dutch.|||In FHCL1; Afrikaner-3; 5-10% of Afrikaners.|||In FHCL1; Algeria-1; unknown pathological significance.|||In FHCL1; Algeria-2; unknown pathological significance.|||In FHCL1; Algeria-3; unknown pathological significance.|||In FHCL1; Amsterdam; unknown pathological significance.|||In FHCL1; Cape Town-1; retards receptor transport from the endoplasmic reticulum to the cell surface.|||In FHCL1; Cincinnati-1; unknown pathological significance.|||In FHCL1; Cincinnati-3; unknown pathological significance.|||In FHCL1; Cincinnati-4; less than 2% receptor activity.|||In FHCL1; Durban-1.|||In FHCL1; French Canadian-2; 5% of French Canadians.|||In FHCL1; French Canadian-3/Mexico; 2% of French Canadians.|||In FHCL1; French Canadian-4.|||In FHCL1; Genoa.|||In FHCL1; Glasco.|||In FHCL1; Greece-2; unknown pathological significance.|||In FHCL1; Gujerat/Zambia/Belgian/Dutch/Sweden/Japan.|||In FHCL1; J.D.Bari/Syria; 2-fold decreased affinity for LDLRAP1.|||In FHCL1; Kuwait.|||In FHCL1; Lancashire; 6% of American English.|||In FHCL1; London-4.|||In FHCL1; New York-3.|||In FHCL1; Osaka-3.|||In FHCL1; Padova.|||In FHCL1; Paris-9; unknown pathological significance.|||In FHCL1; Philippines/Durban-2/Japan.|||In FHCL1; Picardie; unknown pathological significance.|||In FHCL1; Piscataway/Lithuania.|||In FHCL1; Pori; unknown pathological significance.|||In FHCL1; Puerto Rico.|||In FHCL1; San Francisco.|||In FHCL1; Sephardic/Safed; 10% of the Sephardic Jews.|||In FHCL1; Sicily.|||In FHCL1; Trieste.|||In FHCL1; Tulsa-2.|||In FHCL1; Turku.|||In FHCL1; does not affect receptor expression at the cell surface; does not affect LDL binding; results in impaired LDL uptake and internalization.|||In FHCL1; does not affect receptor expression at the cell surface; results in reduced LDL binding; results in reduced LDL uptake and internalization.|||In FHCL1; rare mutation; strongly reduced receptor activity.|||In FHCL1; results in defective LDL binding; does not affect receptor expression at the cell surface.|||In FHCL1; results in loss of receptor expression at the cell surface.|||In FHCL1; results in reduced receptor expression at the cell surface due to defective receptor recycling.|||In FHCL1; unknown pathological significance.|||In Germany.|||In Greece-1.|||In Issoire.|||In Italy-2.|||In London-5.|||In Mexico-1; leads to a defect in the intracellular transport of the receptor.|||In Mexico-2.|||In Mexico-3.|||In Miami-1.|||In Miami-2.|||In Milan.|||In Munster-1.|||In Munster-2.|||In Naples-1.|||In Naples-2.|||In Nevers.|||In New York-1.|||In New York-2.|||In New York-5.|||In North Platt.|||In Oklahoma.|||In Paris-4.|||In Paris-6.|||In Paris-7.|||In Portugal.|||In Rouen.|||In Russia-1.|||In Russia-2.|||In Saint Omer; retention in the ER.|||In Shreveport.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||Low-density lipoprotein receptor|||May contribute to familial hypercholesterolemia.|||N-linked (GlcNAc...) asparagine|||NPXY motif|||No change. Insensitive to MYLIP-triggered degradation; when associated with R-830. Insensitive to MYLIP-triggered degradation; when associated with R-816 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-816 and R-830.|||No change. No change; when associated with R-816 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-816; R-830 and A-839.|||No change. No change; when associated with R-816. No change; when associated with R-811 and R-816. Insensitive to MYLIP-triggered degradation; when associated with A-839. Insensitive to MYLIP-triggered degradation; when associated with R-816 and A-839. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-816 and A-839.|||No change. No change; when associated with R-830. No change; when associated with R-811 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-830 and A-839. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-830 and A-839.|||No effect on receptor internalization.|||Phosphothreonine|||Polar residues|||Required for MYLIP-triggered down-regulation of LDLR ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017312|||http://purl.uniprot.org/annotation/VAR_005304|||http://purl.uniprot.org/annotation/VAR_005305|||http://purl.uniprot.org/annotation/VAR_005306|||http://purl.uniprot.org/annotation/VAR_005307|||http://purl.uniprot.org/annotation/VAR_005308|||http://purl.uniprot.org/annotation/VAR_005309|||http://purl.uniprot.org/annotation/VAR_005310|||http://purl.uniprot.org/annotation/VAR_005311|||http://purl.uniprot.org/annotation/VAR_005312|||http://purl.uniprot.org/annotation/VAR_005313|||http://purl.uniprot.org/annotation/VAR_005314|||http://purl.uniprot.org/annotation/VAR_005315|||http://purl.uniprot.org/annotation/VAR_005316|||http://purl.uniprot.org/annotation/VAR_005317|||http://purl.uniprot.org/annotation/VAR_005318|||http://purl.uniprot.org/annotation/VAR_005319|||http://purl.uniprot.org/annotation/VAR_005320|||http://purl.uniprot.org/annotation/VAR_005321|||http://purl.uniprot.org/annotation/VAR_005322|||http://purl.uniprot.org/annotation/VAR_005323|||http://purl.uniprot.org/annotation/VAR_005324|||http://purl.uniprot.org/annotation/VAR_005325|||http://purl.uniprot.org/annotation/VAR_005326|||http://purl.uniprot.org/annotation/VAR_005327|||http://purl.uniprot.org/annotation/VAR_005328|||http://purl.uniprot.org/annotation/VAR_005329|||http://purl.uniprot.org/annotation/VAR_005330|||http://purl.uniprot.org/annotation/VAR_005331|||http://purl.uniprot.org/annotation/VAR_005332|||http://purl.uniprot.org/annotation/VAR_005333|||http://purl.uniprot.org/annotation/VAR_005334|||http://purl.uniprot.org/annotation/VAR_005335|||http://purl.uniprot.org/annotation/VAR_005336|||http://purl.uniprot.org/annotation/VAR_005337|||http://purl.uniprot.org/annotation/VAR_005338|||http://purl.uniprot.org/annotation/VAR_005339|||http://purl.uniprot.org/annotation/VAR_005340|||http://purl.uniprot.org/annotation/VAR_005341|||http://purl.uniprot.org/annotation/VAR_005342|||http://purl.uniprot.org/annotation/VAR_005343|||http://purl.uniprot.org/annotation/VAR_005344|||http://purl.uniprot.org/annotation/VAR_005345|||http://purl.uniprot.org/annotation/VAR_005346|||http://purl.uniprot.org/annotation/VAR_005347|||http://purl.uniprot.org/annotation/VAR_005348|||http://purl.uniprot.org/annotation/VAR_005349|||http://purl.uniprot.org/annotation/VAR_005350|||http://purl.uniprot.org/annotation/VAR_005351|||http://purl.uniprot.org/annotation/VAR_005352|||http://purl.uniprot.org/annotation/VAR_005353|||http://purl.uniprot.org/annotation/VAR_005354|||http://purl.uniprot.org/annotation/VAR_005355|||http://purl.uniprot.org/annotation/VAR_005356|||http://purl.uniprot.org/annotation/VAR_005357|||http://purl.uniprot.org/annotation/VAR_005358|||http://purl.uniprot.org/annotation/VAR_005359|||http://purl.uniprot.org/annotation/VAR_005360|||http://purl.uniprot.org/annotation/VAR_005361|||http://purl.uniprot.org/annotation/VAR_005362|||http://purl.uniprot.org/annotation/VAR_005363|||http://purl.uniprot.org/annotation/VAR_005364|||http://purl.uniprot.org/annotation/VAR_005365|||http://purl.uniprot.org/annotation/VAR_005366|||http://purl.uniprot.org/annotation/VAR_005367|||http://purl.uniprot.org/annotation/VAR_005368|||http://purl.uniprot.org/annotation/VAR_005369|||http://purl.uniprot.org/annotation/VAR_005370|||http://purl.uniprot.org/annotation/VAR_005371|||http://purl.uniprot.org/annotation/VAR_005372|||http://purl.uniprot.org/annotation/VAR_005373|||http://purl.uniprot.org/annotation/VAR_005374|||http://purl.uniprot.org/annotation/VAR_005375|||http://purl.uniprot.org/annotation/VAR_005376|||http://purl.uniprot.org/annotation/VAR_005377|||http://purl.uniprot.org/annotation/VAR_005378|||http://purl.uniprot.org/annotation/VAR_005379|||http://purl.uniprot.org/annotation/VAR_005380|||http://purl.uniprot.org/annotation/VAR_005381|||http://purl.uniprot.org/annotation/VAR_005382|||http://purl.uniprot.org/annotation/VAR_005383|||http://purl.uniprot.org/annotation/VAR_005384|||http://purl.uniprot.org/annotation/VAR_005385|||http://purl.uniprot.org/annotation/VAR_005386|||http://purl.uniprot.org/annotation/VAR_005387|||http://purl.uniprot.org/annotation/VAR_005388|||http://purl.uniprot.org/annotation/VAR_005389|||http://purl.uniprot.org/annotation/VAR_005390|||http://purl.uniprot.org/annotation/VAR_005391|||http://purl.uniprot.org/annotation/VAR_005392|||http://purl.uniprot.org/annotation/VAR_005393|||http://purl.uniprot.org/annotation/VAR_005394|||http://purl.uniprot.org/annotation/VAR_005395|||http://purl.uniprot.org/annotation/VAR_005396|||http://purl.uniprot.org/annotation/VAR_005397|||http://purl.uniprot.org/annotation/VAR_005398|||http://purl.uniprot.org/annotation/VAR_005399|||http://purl.uniprot.org/annotation/VAR_005400|||http://purl.uniprot.org/annotation/VAR_005401|||http://purl.uniprot.org/annotation/VAR_005402|||http://purl.uniprot.org/annotation/VAR_005403|||http://purl.uniprot.org/annotation/VAR_005404|||http://purl.uniprot.org/annotation/VAR_005405|||http://purl.uniprot.org/annotation/VAR_005406|||http://purl.uniprot.org/annotation/VAR_005407|||http://purl.uniprot.org/annotation/VAR_005408|||http://purl.uniprot.org/annotation/VAR_005409|||http://purl.uniprot.org/annotation/VAR_005410|||http://purl.uniprot.org/annotation/VAR_005412|||http://purl.uniprot.org/annotation/VAR_005413|||http://purl.uniprot.org/annotation/VAR_005414|||http://purl.uniprot.org/annotation/VAR_005415|||http://purl.uniprot.org/annotation/VAR_005416|||http://purl.uniprot.org/annotation/VAR_005417|||http://purl.uniprot.org/annotation/VAR_005418|||http://purl.uniprot.org/annotation/VAR_005419|||http://purl.uniprot.org/annotation/VAR_005420|||http://purl.uniprot.org/annotation/VAR_007979|||http://purl.uniprot.org/annotation/VAR_007980|||http://purl.uniprot.org/annotation/VAR_007981|||http://purl.uniprot.org/annotation/VAR_007982|||http://purl.uniprot.org/annotation/VAR_007983|||http://purl.uniprot.org/annotation/VAR_007984|||http://purl.uniprot.org/annotation/VAR_007985|||http://purl.uniprot.org/annotation/VAR_007986|||http://purl.uniprot.org/annotation/VAR_007987|||http://purl.uniprot.org/annotation/VAR_007988|||http://purl.uniprot.org/annotation/VAR_007989|||http://purl.uniprot.org/annotation/VAR_008995|||http://purl.uniprot.org/annotation/VAR_008996|||http://purl.uniprot.org/annotation/VAR_008997|||http://purl.uniprot.org/annotation/VAR_011862|||http://purl.uniprot.org/annotation/VAR_011863|||http://purl.uniprot.org/annotation/VAR_011864|||http://purl.uniprot.org/annotation/VAR_013949|||http://purl.uniprot.org/annotation/VAR_013950|||http://purl.uniprot.org/annotation/VAR_013951|||http://purl.uniprot.org/annotation/VAR_013952|||http://purl.uniprot.org/annotation/VAR_013953|||http://purl.uniprot.org/annotation/VAR_013954|||http://purl.uniprot.org/annotation/VAR_013955|||http://purl.uniprot.org/annotation/VAR_024519|||http://purl.uniprot.org/annotation/VAR_059375|||http://purl.uniprot.org/annotation/VAR_062371|||http://purl.uniprot.org/annotation/VAR_062372|||http://purl.uniprot.org/annotation/VAR_062373|||http://purl.uniprot.org/annotation/VAR_062374|||http://purl.uniprot.org/annotation/VAR_062375|||http://purl.uniprot.org/annotation/VAR_062376|||http://purl.uniprot.org/annotation/VAR_062377|||http://purl.uniprot.org/annotation/VAR_062378|||http://purl.uniprot.org/annotation/VAR_062379|||http://purl.uniprot.org/annotation/VAR_062380|||http://purl.uniprot.org/annotation/VAR_062381|||http://purl.uniprot.org/annotation/VAR_062382|||http://purl.uniprot.org/annotation/VAR_062383|||http://purl.uniprot.org/annotation/VAR_065780|||http://purl.uniprot.org/annotation/VAR_065781|||http://purl.uniprot.org/annotation/VAR_065782|||http://purl.uniprot.org/annotation/VAR_065783|||http://purl.uniprot.org/annotation/VAR_067196|||http://purl.uniprot.org/annotation/VAR_072827|||http://purl.uniprot.org/annotation/VAR_072828|||http://purl.uniprot.org/annotation/VAR_072829|||http://purl.uniprot.org/annotation/VAR_072830|||http://purl.uniprot.org/annotation/VAR_072831|||http://purl.uniprot.org/annotation/VAR_072832|||http://purl.uniprot.org/annotation/VAR_072833|||http://purl.uniprot.org/annotation/VAR_072834|||http://purl.uniprot.org/annotation/VAR_072835|||http://purl.uniprot.org/annotation/VAR_072836|||http://purl.uniprot.org/annotation/VAR_072837|||http://purl.uniprot.org/annotation/VAR_072838|||http://purl.uniprot.org/annotation/VAR_072839|||http://purl.uniprot.org/annotation/VAR_072840|||http://purl.uniprot.org/annotation/VAR_072841|||http://purl.uniprot.org/annotation/VAR_072842|||http://purl.uniprot.org/annotation/VAR_072843|||http://purl.uniprot.org/annotation/VAR_072844|||http://purl.uniprot.org/annotation/VAR_072845|||http://purl.uniprot.org/annotation/VAR_072846|||http://purl.uniprot.org/annotation/VAR_072847|||http://purl.uniprot.org/annotation/VAR_072848|||http://purl.uniprot.org/annotation/VAR_072849|||http://purl.uniprot.org/annotation/VAR_072850|||http://purl.uniprot.org/annotation/VAR_072851|||http://purl.uniprot.org/annotation/VAR_072852|||http://purl.uniprot.org/annotation/VAR_072853|||http://purl.uniprot.org/annotation/VAR_072854|||http://purl.uniprot.org/annotation/VAR_072855|||http://purl.uniprot.org/annotation/VAR_072856|||http://purl.uniprot.org/annotation/VAR_072857|||http://purl.uniprot.org/annotation/VAR_072858|||http://purl.uniprot.org/annotation/VAR_072859|||http://purl.uniprot.org/annotation/VAR_072860|||http://purl.uniprot.org/annotation/VAR_072861|||http://purl.uniprot.org/annotation/VSP_043053|||http://purl.uniprot.org/annotation/VSP_043054|||http://purl.uniprot.org/annotation/VSP_043595|||http://purl.uniprot.org/annotation/VSP_045525|||http://purl.uniprot.org/annotation/VSP_047413|||http://purl.uniprot.org/annotation/VSP_055014|||http://purl.uniprot.org/annotation/VSP_055015
http://togogenome.org/gene/9606:B4GALNT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76KP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1|||N-linked (GlcNAc...) asparagine|||PA14|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252370|||http://purl.uniprot.org/annotation/VAR_061096|||http://purl.uniprot.org/annotation/VAR_061097
http://togogenome.org/gene/9606:FAM90A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM90A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299592|||http://purl.uniprot.org/annotation/VAR_057778|||http://purl.uniprot.org/annotation/VAR_060154|||http://purl.uniprot.org/annotation/VAR_060155|||http://purl.uniprot.org/annotation/VAR_060293|||http://purl.uniprot.org/annotation/VAR_060294|||http://purl.uniprot.org/annotation/VAR_060295
http://togogenome.org/gene/9606:CDH18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RER2|||http://purl.uniprot.org/uniprot/Q13634                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-18|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003815|||http://purl.uniprot.org/annotation/PRO_0000003816|||http://purl.uniprot.org/annotation/PRO_5003087413|||http://purl.uniprot.org/annotation/VSP_042308
http://togogenome.org/gene/9606:MORN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDC4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN repeat-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279488|||http://purl.uniprot.org/annotation/VSP_023457
http://togogenome.org/gene/9606:SMDT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4I9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes calcium uptake into mitochondria.|||Abolishes regulation of calcium uptake into mitochondria.|||Essential MCU regulator, mitochondrial|||GXXXX[G/A/S]|||Helical|||Interaction with MAIP1|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296320|||http://purl.uniprot.org/annotation/VAR_034628
http://togogenome.org/gene/9606:TESK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFN2|||http://purl.uniprot.org/uniprot/Q96S53                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dual specificity testis-specific protein kinase 2|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086749|||http://purl.uniprot.org/annotation/VAR_041214|||http://purl.uniprot.org/annotation/VSP_004930|||http://purl.uniprot.org/annotation/VSP_004931
http://togogenome.org/gene/9606:NF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35240                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to AGAP2 and interaction with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.|||FERM|||In NF2.|||In NF2; also found in retinal hamartoma; severe.|||In NF2; also found in sporadic meningioma.|||In NF2; late onset.|||In NF2; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.|||In NF2; mild.|||In a breast cancer sample; somatic mutation.|||In breast ductal carcinoma.|||In isoform 10.|||In isoform 2.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8.|||In isoform 4 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||In melanoma.|||In sporadic meningioma.|||In sporadic meningioma; no effect on interaction with SCHIP1.|||In vestibular schwannoma.|||In vestibular schwannoma; changed interaction with SCHIP1.|||In vestibular schwannoma; loss of ability to interact with the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.|||Loss of phosphorylation. Significant accumulation in the nucleus and no effect on binding to DCAF1.|||Merlin|||No effect on phosphorylation. Defective nuclear accumulation. Significant decrease in binding to DCAF1 and in ability to inhibit cell proliferation.|||Phosphoserine|||Phosphoserine; by PAK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219412|||http://purl.uniprot.org/annotation/VAR_000809|||http://purl.uniprot.org/annotation/VAR_000810|||http://purl.uniprot.org/annotation/VAR_000811|||http://purl.uniprot.org/annotation/VAR_000812|||http://purl.uniprot.org/annotation/VAR_000813|||http://purl.uniprot.org/annotation/VAR_000814|||http://purl.uniprot.org/annotation/VAR_000815|||http://purl.uniprot.org/annotation/VAR_000816|||http://purl.uniprot.org/annotation/VAR_000817|||http://purl.uniprot.org/annotation/VAR_000818|||http://purl.uniprot.org/annotation/VAR_000819|||http://purl.uniprot.org/annotation/VAR_000820|||http://purl.uniprot.org/annotation/VAR_000821|||http://purl.uniprot.org/annotation/VAR_000822|||http://purl.uniprot.org/annotation/VAR_000823|||http://purl.uniprot.org/annotation/VAR_000824|||http://purl.uniprot.org/annotation/VAR_000825|||http://purl.uniprot.org/annotation/VAR_000826|||http://purl.uniprot.org/annotation/VAR_009123|||http://purl.uniprot.org/annotation/VAR_029041|||http://purl.uniprot.org/annotation/VAR_035848|||http://purl.uniprot.org/annotation/VAR_043011|||http://purl.uniprot.org/annotation/VAR_043012|||http://purl.uniprot.org/annotation/VAR_043013|||http://purl.uniprot.org/annotation/VAR_043014|||http://purl.uniprot.org/annotation/VAR_043015|||http://purl.uniprot.org/annotation/VAR_043016|||http://purl.uniprot.org/annotation/VAR_043017|||http://purl.uniprot.org/annotation/VAR_065227|||http://purl.uniprot.org/annotation/VSP_000492|||http://purl.uniprot.org/annotation/VSP_007040|||http://purl.uniprot.org/annotation/VSP_007041|||http://purl.uniprot.org/annotation/VSP_007042|||http://purl.uniprot.org/annotation/VSP_007043|||http://purl.uniprot.org/annotation/VSP_007044|||http://purl.uniprot.org/annotation/VSP_007045|||http://purl.uniprot.org/annotation/VSP_007046|||http://purl.uniprot.org/annotation/VSP_007047|||http://purl.uniprot.org/annotation/VSP_007048|||http://purl.uniprot.org/annotation/VSP_007049|||http://purl.uniprot.org/annotation/VSP_007050|||http://purl.uniprot.org/annotation/VSP_007051
http://togogenome.org/gene/9606:DNAH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXX0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Basic and acidic residues|||Disordered|||Dynein axonemal heavy chain 7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317666|||http://purl.uniprot.org/annotation/VAR_038580|||http://purl.uniprot.org/annotation/VAR_038581|||http://purl.uniprot.org/annotation/VAR_038582|||http://purl.uniprot.org/annotation/VAR_038583|||http://purl.uniprot.org/annotation/VAR_038584|||http://purl.uniprot.org/annotation/VAR_038585|||http://purl.uniprot.org/annotation/VAR_038586|||http://purl.uniprot.org/annotation/VAR_038587|||http://purl.uniprot.org/annotation/VAR_038588|||http://purl.uniprot.org/annotation/VAR_038589|||http://purl.uniprot.org/annotation/VAR_038590|||http://purl.uniprot.org/annotation/VAR_038591|||http://purl.uniprot.org/annotation/VAR_038592|||http://purl.uniprot.org/annotation/VAR_038593|||http://purl.uniprot.org/annotation/VAR_038594|||http://purl.uniprot.org/annotation/VAR_038595|||http://purl.uniprot.org/annotation/VAR_038596|||http://purl.uniprot.org/annotation/VAR_038597|||http://purl.uniprot.org/annotation/VAR_038598|||http://purl.uniprot.org/annotation/VSP_031131|||http://purl.uniprot.org/annotation/VSP_031132|||http://purl.uniprot.org/annotation/VSP_031133|||http://purl.uniprot.org/annotation/VSP_031134|||http://purl.uniprot.org/annotation/VSP_031135|||http://purl.uniprot.org/annotation/VSP_031136
http://togogenome.org/gene/9606:SLC1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43005                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Discontinuously helical|||Excitatory amino acid transporter 3|||Extracellular|||Helical|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In DCBXA; inhibits L-glutamate and L-cysteine transport activities.|||In DCBXA; reduces L-glutamate and L-cysteine transport activities; reduces cell membrane expression.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202065|||http://purl.uniprot.org/annotation/VAR_023308|||http://purl.uniprot.org/annotation/VAR_023309|||http://purl.uniprot.org/annotation/VAR_071953|||http://purl.uniprot.org/annotation/VAR_071954
http://togogenome.org/gene/9606:LSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H089                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CP-type G|||Disordered|||Large subunit GTPase 1 homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324553|||http://purl.uniprot.org/annotation/VAR_039826|||http://purl.uniprot.org/annotation/VAR_039827
http://togogenome.org/gene/9606:TCF7L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTL7|||http://purl.uniprot.org/uniprot/A0A994J711|||http://purl.uniprot.org/uniprot/C6ZRJ7|||http://purl.uniprot.org/uniprot/C6ZRK1|||http://purl.uniprot.org/uniprot/C6ZRK2|||http://purl.uniprot.org/uniprot/C6ZRK5|||http://purl.uniprot.org/uniprot/Q5VVR7|||http://purl.uniprot.org/uniprot/Q6FHW4|||http://purl.uniprot.org/uniprot/Q9NQB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes CTNNB1 binding.|||Abolishes CTNNB1 binding; when associated with A-24; A-26 and A-29.|||Abolishes CTNNB1 binding; when associated with A-24; A-28 and A-29.|||Basic and acidic residues|||CTNNB1-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 15 and isoform 16.|||In isoform 17.|||In isoform 2 and isoform 4.|||In isoform 3, isoform 7 and isoform 13.|||In isoform 4, isoform 5, isoform 7, isoform 13 and isoform 16.|||In isoform 6.|||In isoform 8, isoform 10, isoform 11, isoform 12, isoform 13, isoform 14, isoform 15 and isoform 16.|||In isoform 9, isoform 11, isoform 14 and isoform 15.|||Loss of sumoylation.|||Loss of sumoylation. No effect on localization to nuclear bodies.|||Mediates interaction with MAD2L2|||Nuclear localization signal|||Phosphothreonine; by NLK|||Polar residues|||Promoter-specific activation domain|||Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-201.|||Reduced phosphorylation by NLK and enhanced DNA-binding; when associated with V-212.|||Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-24; A-26 and A-28.|||Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-26; A-28 and A-29.|||Reduces CTNNB1 binding.|||Reduces transcription activation.|||Transcription factor 7-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048623|||http://purl.uniprot.org/annotation/VAR_035939|||http://purl.uniprot.org/annotation/VAR_047126|||http://purl.uniprot.org/annotation/VSP_006962|||http://purl.uniprot.org/annotation/VSP_006963|||http://purl.uniprot.org/annotation/VSP_006964|||http://purl.uniprot.org/annotation/VSP_006965|||http://purl.uniprot.org/annotation/VSP_006966|||http://purl.uniprot.org/annotation/VSP_006967|||http://purl.uniprot.org/annotation/VSP_006968|||http://purl.uniprot.org/annotation/VSP_006969|||http://purl.uniprot.org/annotation/VSP_006970|||http://purl.uniprot.org/annotation/VSP_006971|||http://purl.uniprot.org/annotation/VSP_006972|||http://purl.uniprot.org/annotation/VSP_045821|||http://purl.uniprot.org/annotation/VSP_045822|||http://purl.uniprot.org/annotation/VSP_053748|||http://purl.uniprot.org/annotation/VSP_053749|||http://purl.uniprot.org/annotation/VSP_053750
http://togogenome.org/gene/9606:DIS3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DIS3-like exonuclease 2|||Disordered|||Important for catalytic activity|||In PRLMNS.|||In PRLMNS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of exoribonuclease activity.|||N6-acetyllysine|||Phosphoserine|||Probable disease-associated variant found in a patient with Wilms tumor; does not suppress anchorage-independent cell growth.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314817|||http://purl.uniprot.org/annotation/VAR_038059|||http://purl.uniprot.org/annotation/VAR_067577|||http://purl.uniprot.org/annotation/VAR_067578|||http://purl.uniprot.org/annotation/VAR_067579|||http://purl.uniprot.org/annotation/VAR_079527|||http://purl.uniprot.org/annotation/VSP_030371|||http://purl.uniprot.org/annotation/VSP_030372|||http://purl.uniprot.org/annotation/VSP_030373|||http://purl.uniprot.org/annotation/VSP_030374|||http://purl.uniprot.org/annotation/VSP_030375|||http://purl.uniprot.org/annotation/VSP_030376|||http://purl.uniprot.org/annotation/VSP_030377|||http://purl.uniprot.org/annotation/VSP_030378
http://togogenome.org/gene/9606:INCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VD86                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interaction with CCNA1 and CCNA1/CDK2 complex; essential for CDK2 inhibitory activity|||Loss of phosphorylation site.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Protein INCA1|||Reduced phosphorylation.|||Reduced phosphorylation. Phosphorylation is almost abolished; when associated with A-191.|||Strongly reduced phosphorylation. Phosphorylation is almost abolished; when associated with A-182.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331513|||http://purl.uniprot.org/annotation/VSP_033235
http://togogenome.org/gene/9606:OPN1MW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04001|||http://purl.uniprot.org/uniprot/P0DN77|||http://purl.uniprot.org/uniprot/P0DN78                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CBD and BCM.|||In CBD.|||In COD5; results in protein misfolding and retention in the endoplasmic reticulum.|||Medium-wave-sensitive opsin 1|||Medium-wave-sensitive opsin 2|||Medium-wave-sensitive opsin 3|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Required for 11-cis-retinal regeneration                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197785|||http://purl.uniprot.org/annotation/PRO_0000435400|||http://purl.uniprot.org/annotation/PRO_0000435401|||http://purl.uniprot.org/annotation/VAR_004841|||http://purl.uniprot.org/annotation/VAR_064051|||http://purl.uniprot.org/annotation/VAR_064052|||http://purl.uniprot.org/annotation/VAR_064053
http://togogenome.org/gene/9606:AMZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D202|||http://purl.uniprot.org/uniprot/Q400G9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Archaemetzincin-1|||Disordered|||In isoform 2.|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159614|||http://purl.uniprot.org/annotation/VAR_024849|||http://purl.uniprot.org/annotation/VSP_055187|||http://purl.uniprot.org/annotation/VSP_055188
http://togogenome.org/gene/9606:EIF3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60228                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 3 subunit E|||N-acetylalanine|||PCI|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Promotes nuclear accumulation.|||Removed|||Sufficient for interaction with EPAS1|||Sufficient for interaction with MCM7|||Sufficient for interaction with TRIM27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123515|||http://purl.uniprot.org/annotation/VAR_046480
http://togogenome.org/gene/9606:ZNF48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVT1|||http://purl.uniprot.org/uniprot/Q96MX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Pro residues|||Zinc finger protein 48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234586|||http://purl.uniprot.org/annotation/VAR_052758|||http://purl.uniprot.org/annotation/VAR_052759|||http://purl.uniprot.org/annotation/VAR_059894
http://togogenome.org/gene/9606:ICA1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDH6|||http://purl.uniprot.org/uniprot/Q96Q33                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AH|||Disordered|||In isoform 2.|||Islet cell autoantigen 1-like protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076175|||http://purl.uniprot.org/annotation/VSP_017107
http://togogenome.org/gene/9606:SRPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78539                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  HYR|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi repeat-containing protein SRPX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022416|||http://purl.uniprot.org/annotation/VAR_005624|||http://purl.uniprot.org/annotation/VAR_005625|||http://purl.uniprot.org/annotation/VAR_005626|||http://purl.uniprot.org/annotation/VSP_004430|||http://purl.uniprot.org/annotation/VSP_043056|||http://purl.uniprot.org/annotation/VSP_045468|||http://purl.uniprot.org/annotation/VSP_046757
http://togogenome.org/gene/9606:ITGB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26010                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In isoform Short.|||Integrin beta-7|||Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphotyrosine; by Tyr-kinases|||VWFA|||in ADMIDAS binding site|||in ADMIDAS binding site and liganded-open conformation|||in ADMIDAS binding site and unliganded-closed conformation|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016352|||http://purl.uniprot.org/annotation/VAR_049637|||http://purl.uniprot.org/annotation/VSP_002753
http://togogenome.org/gene/9606:KIF21B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75037|||http://purl.uniprot.org/uniprot/Q2UVF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Interaction with TRIM3|||Kinesin motor|||Kinesin-like protein KIF21B|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125464|||http://purl.uniprot.org/annotation/VSP_016217|||http://purl.uniprot.org/annotation/VSP_045333
http://togogenome.org/gene/9606:LENG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVD1                                                                                  ^@                                                                                  Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:FMNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95466                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DAD|||Disordered|||FH2|||Formin-like protein 1|||GBD/FH3|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194890|||http://purl.uniprot.org/annotation/VSP_013977|||http://purl.uniprot.org/annotation/VSP_043845
http://togogenome.org/gene/9606:FBXO36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEA4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 36|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119928|||http://purl.uniprot.org/annotation/VAR_045626|||http://purl.uniprot.org/annotation/VSP_054336
http://togogenome.org/gene/9606:OR4F29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV92|||http://purl.uniprot.org/uniprot/Q6IEY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F3/4F16/4F29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150551
http://togogenome.org/gene/9606:SETD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTS1|||http://purl.uniprot.org/uniprot/Q9NVD3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished histone-lysine N-methyltransferase activity.|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform B.|||SET|||SET domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079509|||http://purl.uniprot.org/annotation/VAR_021948|||http://purl.uniprot.org/annotation/VAR_035988|||http://purl.uniprot.org/annotation/VSP_004146|||http://purl.uniprot.org/annotation/VSP_026578|||http://purl.uniprot.org/annotation/VSP_054087|||http://purl.uniprot.org/annotation/VSP_054088
http://togogenome.org/gene/9606:PDE6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51160                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'|||Cysteine methyl ester|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||GAF 1|||GAF 2|||In ACHM5.|||In ACHM5; decreases cGMP phosphodiesterase activity.|||In ACHM5; severely decreases cGMP phosphodiesterase activity.|||In COD4 and ACHM5; severely decreases cGMP phosphodiesterase activity.|||No effect on cGMP phosphodiesterase activity.|||PDEase|||Proton donor|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198831|||http://purl.uniprot.org/annotation/PRO_0000370788|||http://purl.uniprot.org/annotation/VAR_025470|||http://purl.uniprot.org/annotation/VAR_025471|||http://purl.uniprot.org/annotation/VAR_025472|||http://purl.uniprot.org/annotation/VAR_050475|||http://purl.uniprot.org/annotation/VAR_050476|||http://purl.uniprot.org/annotation/VAR_062408|||http://purl.uniprot.org/annotation/VAR_062409|||http://purl.uniprot.org/annotation/VAR_062410|||http://purl.uniprot.org/annotation/VAR_064744|||http://purl.uniprot.org/annotation/VAR_079307|||http://purl.uniprot.org/annotation/VAR_079308|||http://purl.uniprot.org/annotation/VAR_079309|||http://purl.uniprot.org/annotation/VAR_079310|||http://purl.uniprot.org/annotation/VAR_079311|||http://purl.uniprot.org/annotation/VAR_079312
http://togogenome.org/gene/9606:FOXG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55316                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with KDM5B.|||Basic and acidic residues|||Basic residues|||Disordered|||Fork-head|||Forkhead box protein G1|||Found in a patient with developmental delay with seizures and mild developmental delay; unknown pathological significance.|||In RTTCV.|||In RTTCV; the mutant protein extensively, although not fully, localizes in nuclear speckles, while the wild-type is more widely dispersed throughout the nucleus.|||Interaction with KDM5B|||Pro residues|||Probable disease-associated variant found in a patient with developmental delay.|||Required for interaction with TLE6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091835|||http://purl.uniprot.org/annotation/VAR_063885|||http://purl.uniprot.org/annotation/VAR_064395|||http://purl.uniprot.org/annotation/VAR_064396|||http://purl.uniprot.org/annotation/VAR_078715|||http://purl.uniprot.org/annotation/VAR_078716|||http://purl.uniprot.org/annotation/VAR_078717|||http://purl.uniprot.org/annotation/VAR_078718
http://togogenome.org/gene/9606:CHP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YKE7|||http://purl.uniprot.org/uniprot/Q99653                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcineurin B homologous protein 1|||Disordered|||Does not affect sodium:proton antiporter activity.|||Does not reduce calcium-binding, colocalization and interaction with SLC9A1.|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In SPAX9; decreased protein solubility; decreased protein location at the plasma membrane.|||Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-183.|||Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-147 and A-185.|||Inhibits translocation to the cytoplasm; when associated with A-143; A-145; A-183 and A-185.|||Inhibits translocation to the cytoplasm; when associated with A-143; A-147; A-183 and A-185.|||Inhibits translocation to the cytoplasm; when associated with A-145; A-147; A-183 and A-185.|||N-myristoyl glycine|||Necessary for association with microtubule and interaction with GAPDH|||Necessary for nuclear export signal|||Nuclear export signal 1|||Nuclear export signal 2|||Reduces calcium-binding and SLC9A1-dependent Na(+)/H(+) exchange activity. Does not reduce colocalization and interaction with SLC9A1. Reduces colocalization and interaction with SLC9A1; when associated with A-134.|||Reduces calcium-binding and SLC9A1-dependent Na(+)/H(+) exchange activity. Does not reduce colocalization and interaction with SLC9A1. Reduces colocalization and interaction with SLC9A1; when associated with A-175.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073843|||http://purl.uniprot.org/annotation/VAR_083033
http://togogenome.org/gene/9606:MRPS27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5EA06|||http://purl.uniprot.org/uniprot/Q6PKB3|||http://purl.uniprot.org/uniprot/Q92552                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Non-terminal Residue|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Confirmed at protein level.|||In isoform 2.|||Mitochondrion|||PPR|||PPR 1|||PPR 2|||Small ribosomal subunit protein mS27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087712|||http://purl.uniprot.org/annotation/VAR_047026|||http://purl.uniprot.org/annotation/VSP_054882
http://togogenome.org/gene/9606:VGLL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Transcription cofactor vestigial-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191349|||http://purl.uniprot.org/annotation/VSP_032166
http://togogenome.org/gene/9606:GSTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK4|||http://purl.uniprot.org/uniprot/B7Z1F9|||http://purl.uniprot.org/uniprot/P08263                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Confers ability to hydrolyze S-glutathionyl benzoate to glutathione and benzoic acid.|||Decreased isomerase activity.|||GST C-terminal|||GST N-terminal|||Glutathione S-transferase A1|||Glutathione S-transferase A1, N-terminally processed|||N-acetylalanine; in Glutathione S-transferase A1, N-terminally processed|||N-acetylmethionine|||N6-succinyllysine|||No significant effect on enzyme activity. Reduces protein stability.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185783|||http://purl.uniprot.org/annotation/PRO_0000423203|||http://purl.uniprot.org/annotation/VAR_033978|||http://purl.uniprot.org/annotation/VAR_049482|||http://purl.uniprot.org/annotation/VAR_049483
http://togogenome.org/gene/9606:TMEM87B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494BZZ8|||http://purl.uniprot.org/uniprot/Q96K49                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Found in restrictive cardiomyopathy; unknown pathological significance.|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 87B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291753|||http://purl.uniprot.org/annotation/PRO_5038633007|||http://purl.uniprot.org/annotation/VAR_078997|||http://purl.uniprot.org/annotation/VSP_026219
http://togogenome.org/gene/9606:CYP26A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43174                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 26A1|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051980|||http://purl.uniprot.org/annotation/VSP_045087
http://togogenome.org/gene/9606:CLSPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAW4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolished cleavage by caspase-7 (CASP7).|||Acidic patch|||Acidic residues|||Basic and acidic residues|||CKB motif 1|||CKB motif 2|||CKB motif 3|||Claspin|||Cleavage; by caspase-7|||Disordered|||Does not affect cleavage by caspase-7 (CASP7).|||Impairs interaction with CHEK1.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||No effect on interaction with CHEK1.|||PCNA-interacting protein (PIP)|||Phosphoserine|||Phosphothreonine; by CHEK1|||Polar residues|||Strongly decreases interaction with PCNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089875|||http://purl.uniprot.org/annotation/VAR_023439|||http://purl.uniprot.org/annotation/VAR_035674|||http://purl.uniprot.org/annotation/VAR_050867|||http://purl.uniprot.org/annotation/VAR_050868|||http://purl.uniprot.org/annotation/VSP_036033|||http://purl.uniprot.org/annotation/VSP_036034
http://togogenome.org/gene/9606:WDR73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5RKY8|||http://purl.uniprot.org/uniprot/Q6P4I2|||http://purl.uniprot.org/uniprot/Q6PJL8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307280|||http://purl.uniprot.org/annotation/VAR_035399
http://togogenome.org/gene/9606:USH2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75445                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with collagen IV.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 18|||Fibronectin type-III 19|||Fibronectin type-III 2|||Fibronectin type-III 20|||Fibronectin type-III 21|||Fibronectin type-III 22|||Fibronectin type-III 23|||Fibronectin type-III 24|||Fibronectin type-III 25|||Fibronectin type-III 26|||Fibronectin type-III 27|||Fibronectin type-III 28|||Fibronectin type-III 29|||Fibronectin type-III 3|||Fibronectin type-III 30|||Fibronectin type-III 31|||Fibronectin type-III 32|||Fibronectin type-III 33|||Fibronectin type-III 34|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Found in a family with autosomal recessive deafness; unknown pathological significance.|||Found in a patient with non-syndromic sensorineural hearing loss; unknown pathological significance.|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical|||In RP39 and USH2A.|||In RP39 and USH2A; benign variant.|||In RP39.|||In RP39; benign variant.|||In RP39; unknown pathological significance.|||In USH2A and RP39.|||In USH2A and RP39; associated with C-4115.|||In USH2A and RP39; associated with M-4425.|||In USH2A.|||In USH2A; abolishes interaction with collagen IV.|||In USH2A; benign variant.|||In USH2A; likely benign variant.|||In USH2A; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin G-like 1|||Laminin G-like 2|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Usherin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229804|||http://purl.uniprot.org/annotation/VAR_025760|||http://purl.uniprot.org/annotation/VAR_025761|||http://purl.uniprot.org/annotation/VAR_025762|||http://purl.uniprot.org/annotation/VAR_025763|||http://purl.uniprot.org/annotation/VAR_025764|||http://purl.uniprot.org/annotation/VAR_025765|||http://purl.uniprot.org/annotation/VAR_025766|||http://purl.uniprot.org/annotation/VAR_025767|||http://purl.uniprot.org/annotation/VAR_025768|||http://purl.uniprot.org/annotation/VAR_025769|||http://purl.uniprot.org/annotation/VAR_025770|||http://purl.uniprot.org/annotation/VAR_025771|||http://purl.uniprot.org/annotation/VAR_025772|||http://purl.uniprot.org/annotation/VAR_025773|||http://purl.uniprot.org/annotation/VAR_025774|||http://purl.uniprot.org/annotation/VAR_025775|||http://purl.uniprot.org/annotation/VAR_025776|||http://purl.uniprot.org/annotation/VAR_025777|||http://purl.uniprot.org/annotation/VAR_025778|||http://purl.uniprot.org/annotation/VAR_025779|||http://purl.uniprot.org/annotation/VAR_025780|||http://purl.uniprot.org/annotation/VAR_025781|||http://purl.uniprot.org/annotation/VAR_034064|||http://purl.uniprot.org/annotation/VAR_038362|||http://purl.uniprot.org/annotation/VAR_038363|||http://purl.uniprot.org/annotation/VAR_038364|||http://purl.uniprot.org/annotation/VAR_038365|||http://purl.uniprot.org/annotation/VAR_038366|||http://purl.uniprot.org/annotation/VAR_038367|||http://purl.uniprot.org/annotation/VAR_038368|||http://purl.uniprot.org/annotation/VAR_038369|||http://purl.uniprot.org/annotation/VAR_050087|||http://purl.uniprot.org/annotation/VAR_050088|||http://purl.uniprot.org/annotation/VAR_050089|||http://purl.uniprot.org/annotation/VAR_054557|||http://purl.uniprot.org/annotation/VAR_054558|||http://purl.uniprot.org/annotation/VAR_054559|||http://purl.uniprot.org/annotation/VAR_054560|||http://purl.uniprot.org/annotation/VAR_054561|||http://purl.uniprot.org/annotation/VAR_054562|||http://purl.uniprot.org/annotation/VAR_054563|||http://purl.uniprot.org/annotation/VAR_054564|||http://purl.uniprot.org/annotation/VAR_054565|||http://purl.uniprot.org/annotation/VAR_054566|||http://purl.uniprot.org/annotation/VAR_054567|||http://purl.uniprot.org/annotation/VAR_054568|||http://purl.uniprot.org/annotation/VAR_054569|||http://purl.uniprot.org/annotation/VAR_054570|||http://purl.uniprot.org/annotation/VAR_054571|||http://purl.uniprot.org/annotation/VAR_054572|||http://purl.uniprot.org/annotation/VAR_054573|||http://purl.uniprot.org/annotation/VAR_054574|||http://purl.uniprot.org/annotation/VAR_054575|||http://purl.uniprot.org/annotation/VAR_054576|||http://purl.uniprot.org/annotation/VAR_054577|||http://purl.uniprot.org/annotation/VAR_054578|||http://purl.uniprot.org/annotation/VAR_054579|||http://purl.uniprot.org/annotation/VAR_054580|||http://purl.uniprot.org/annotation/VAR_054581|||http://purl.uniprot.org/annotation/VAR_054582|||http://purl.uniprot.org/annotation/VAR_054583|||http://purl.uniprot.org/annotation/VAR_054584|||http://purl.uniprot.org/annotation/VAR_054585|||http://purl.uniprot.org/annotation/VAR_054586|||http://purl.uniprot.org/annotation/VAR_054587|||http://purl.uniprot.org/annotation/VAR_054588|||http://purl.uniprot.org/annotation/VAR_054589|||http://purl.uniprot.org/annotation/VAR_054590|||http://purl.uniprot.org/annotation/VAR_054591|||http://purl.uniprot.org/annotation/VAR_054592|||http://purl.uniprot.org/annotation/VAR_054593|||http://purl.uniprot.org/annotation/VAR_054594|||http://purl.uniprot.org/annotation/VAR_054595|||http://purl.uniprot.org/annotation/VAR_054596|||http://purl.uniprot.org/annotation/VAR_054597|||http://purl.uniprot.org/annotation/VAR_054598|||http://purl.uniprot.org/annotation/VAR_054599|||http://purl.uniprot.org/annotation/VAR_054600|||http://purl.uniprot.org/annotation/VAR_054601|||http://purl.uniprot.org/annotation/VAR_054602|||http://purl.uniprot.org/annotation/VAR_054603|||http://purl.uniprot.org/annotation/VAR_054604|||http://purl.uniprot.org/annotation/VAR_054605|||http://purl.uniprot.org/annotation/VAR_054606|||http://purl.uniprot.org/annotation/VAR_054607|||http://purl.uniprot.org/annotation/VAR_054608|||http://purl.uniprot.org/annotation/VAR_054609|||http://purl.uniprot.org/annotation/VAR_054610|||http://purl.uniprot.org/annotation/VAR_054611|||http://purl.uniprot.org/annotation/VAR_054612|||http://purl.uniprot.org/annotation/VAR_054613|||http://purl.uniprot.org/annotation/VAR_054614|||http://purl.uniprot.org/annotation/VAR_054615|||http://purl.uniprot.org/annotation/VAR_054616|||http://purl.uniprot.org/annotation/VAR_054617|||http://purl.uniprot.org/annotation/VAR_054618|||http://purl.uniprot.org/annotation/VAR_054619|||http://purl.uniprot.org/annotation/VAR_054620|||http://purl.uniprot.org/annotation/VAR_061350|||http://purl.uniprot.org/annotation/VAR_061351|||http://purl.uniprot.org/annotation/VAR_061352|||http://purl.uniprot.org/annotation/VAR_064761|||http://purl.uniprot.org/annotation/VAR_066665|||http://purl.uniprot.org/annotation/VAR_068354|||http://purl.uniprot.org/annotation/VAR_068355|||http://purl.uniprot.org/annotation/VAR_068356|||http://purl.uniprot.org/annotation/VAR_068357|||http://purl.uniprot.org/annotation/VAR_068358|||http://purl.uniprot.org/annotation/VAR_071996|||http://purl.uniprot.org/annotation/VAR_071997|||http://purl.uniprot.org/annotation/VAR_071998|||http://purl.uniprot.org/annotation/VAR_071999|||http://purl.uniprot.org/annotation/VAR_072000|||http://purl.uniprot.org/annotation/VAR_072001|||http://purl.uniprot.org/annotation/VAR_072002|||http://purl.uniprot.org/annotation/VAR_072003|||http://purl.uniprot.org/annotation/VAR_072004|||http://purl.uniprot.org/annotation/VAR_072005|||http://purl.uniprot.org/annotation/VAR_072006|||http://purl.uniprot.org/annotation/VAR_072007|||http://purl.uniprot.org/annotation/VAR_072008|||http://purl.uniprot.org/annotation/VAR_072009|||http://purl.uniprot.org/annotation/VAR_072010|||http://purl.uniprot.org/annotation/VAR_072011|||http://purl.uniprot.org/annotation/VAR_072012|||http://purl.uniprot.org/annotation/VAR_072013|||http://purl.uniprot.org/annotation/VAR_072014|||http://purl.uniprot.org/annotation/VAR_072015|||http://purl.uniprot.org/annotation/VAR_072016|||http://purl.uniprot.org/annotation/VAR_072017|||http://purl.uniprot.org/annotation/VAR_072018|||http://purl.uniprot.org/annotation/VAR_072019|||http://purl.uniprot.org/annotation/VAR_072020|||http://purl.uniprot.org/annotation/VAR_072021|||http://purl.uniprot.org/annotation/VAR_072022|||http://purl.uniprot.org/annotation/VAR_072023|||http://purl.uniprot.org/annotation/VAR_072024|||http://purl.uniprot.org/annotation/VAR_072025|||http://purl.uniprot.org/annotation/VAR_072026|||http://purl.uniprot.org/annotation/VAR_072027|||http://purl.uniprot.org/annotation/VAR_072028|||http://purl.uniprot.org/annotation/VAR_072029|||http://purl.uniprot.org/annotation/VAR_072030|||http://purl.uniprot.org/annotation/VAR_072031|||http://purl.uniprot.org/annotation/VAR_072032|||http://purl.uniprot.org/annotation/VAR_072033|||http://purl.uniprot.org/annotation/VAR_072034|||http://purl.uniprot.org/annotation/VAR_072035|||http://purl.uniprot.org/annotation/VAR_072036|||http://purl.uniprot.org/annotation/VAR_072037|||http://purl.uniprot.org/annotation/VAR_072038|||http://purl.uniprot.org/annotation/VAR_072039|||http://purl.uniprot.org/annotation/VAR_072040|||http://purl.uniprot.org/annotation/VAR_072041|||http://purl.uniprot.org/annotation/VAR_072042|||http://purl.uniprot.org/annotation/VAR_072043|||http://purl.uniprot.org/annotation/VAR_072044|||http://purl.uniprot.org/annotation/VAR_072045|||http://purl.uniprot.org/annotation/VAR_072046|||http://purl.uniprot.org/annotation/VAR_072047|||http://purl.uniprot.org/annotation/VAR_072048|||http://purl.uniprot.org/annotation/VAR_072049|||http://purl.uniprot.org/annotation/VAR_072050|||http://purl.uniprot.org/annotation/VAR_072051|||http://purl.uniprot.org/annotation/VAR_072052|||http://purl.uniprot.org/annotation/VAR_072053|||http://purl.uniprot.org/annotation/VAR_072054|||http://purl.uniprot.org/annotation/VAR_072055|||http://purl.uniprot.org/annotation/VAR_072056|||http://purl.uniprot.org/annotation/VAR_072057|||http://purl.uniprot.org/annotation/VAR_072058|||http://purl.uniprot.org/annotation/VAR_072059|||http://purl.uniprot.org/annotation/VAR_072060|||http://purl.uniprot.org/annotation/VAR_072061|||http://purl.uniprot.org/annotation/VAR_072062|||http://purl.uniprot.org/annotation/VAR_072063|||http://purl.uniprot.org/annotation/VAR_072064|||http://purl.uniprot.org/annotation/VAR_072065|||http://purl.uniprot.org/annotation/VAR_072066|||http://purl.uniprot.org/annotation/VAR_072067|||http://purl.uniprot.org/annotation/VAR_075587|||http://purl.uniprot.org/annotation/VAR_079508|||http://purl.uniprot.org/annotation/VAR_079509|||http://purl.uniprot.org/annotation/VAR_079877|||http://purl.uniprot.org/annotation/VSP_017771|||http://purl.uniprot.org/annotation/VSP_017772|||http://purl.uniprot.org/annotation/VSP_017773
http://togogenome.org/gene/9606:TYSND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2T9J0                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abrogates the self-cleaving activity of TYSND1.|||Charge relay system|||Cleavage|||In isoform 2.|||Peroxisomal leader peptide-processing protease|||Peroxisomal leader peptide-processing protease, 15 kDa form|||Peroxisomal leader peptide-processing protease, 45 kDa form|||Serine protease                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286124|||http://purl.uniprot.org/annotation/PRO_0000286125|||http://purl.uniprot.org/annotation/PRO_0000286126|||http://purl.uniprot.org/annotation/VAR_059758|||http://purl.uniprot.org/annotation/VSP_025000|||http://purl.uniprot.org/annotation/VSP_025001
http://togogenome.org/gene/9606:TSSK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6SA08                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Loss of kinase activity.|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086772|||http://purl.uniprot.org/annotation/VAR_041247|||http://purl.uniprot.org/annotation/VAR_041248|||http://purl.uniprot.org/annotation/VAR_041249|||http://purl.uniprot.org/annotation/VAR_041250|||http://purl.uniprot.org/annotation/VAR_041251|||http://purl.uniprot.org/annotation/VSP_023559|||http://purl.uniprot.org/annotation/VSP_023560
http://togogenome.org/gene/9606:NPY2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49146                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 2|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069928
http://togogenome.org/gene/9606:FTSJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QYX5|||http://purl.uniprot.org/uniprot/B3KN91|||http://purl.uniprot.org/uniprot/B7Z4K4|||http://purl.uniprot.org/uniprot/Q9UET6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In XLID9; severely decreases methylation of guanosine in tRNA(Phe) and cytidine in tRNA(Trp); methylation of cytidine in tRNA(Phe) appears normal.|||In isoform 2.|||Mononegavirus-type SAM-dependent 2'-O-MTase|||Phosphoserine|||Proton acceptor|||Required for binding to WDR6|||Ribosomal RNA methyltransferase FtsJ|||tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155575|||http://purl.uniprot.org/annotation/VAR_088175|||http://purl.uniprot.org/annotation/VSP_041419
http://togogenome.org/gene/9606:IFT46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Intraflagellar transport protein 46 homolog|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085516|||http://purl.uniprot.org/annotation/VAR_057533|||http://purl.uniprot.org/annotation/VSP_039859
http://togogenome.org/gene/9606:RNF103                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00237                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF103|||Helical|||Loss of E2-dependent ubiquitination.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056084
http://togogenome.org/gene/9606:MRPS33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1T3|||http://purl.uniprot.org/uniprot/Q3KRB4|||http://purl.uniprot.org/uniprot/Q9Y291                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||N-acetylserine|||Removed|||Small ribosomal subunit protein mS33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087727
http://togogenome.org/gene/9606:MIB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AX9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||E3 ubiquitin-protein ligase MIB2|||In isoform 10.|||In isoform 3.|||In isoform 4 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||MIB/HERC2 1|||MIB/HERC2 2|||N-acetylmethionine|||Phosphoserine|||RING-type 1|||RING-type 2|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055947|||http://purl.uniprot.org/annotation/VSP_014393|||http://purl.uniprot.org/annotation/VSP_014394|||http://purl.uniprot.org/annotation/VSP_014395|||http://purl.uniprot.org/annotation/VSP_014396|||http://purl.uniprot.org/annotation/VSP_035508|||http://purl.uniprot.org/annotation/VSP_035510|||http://purl.uniprot.org/annotation/VSP_035511|||http://purl.uniprot.org/annotation/VSP_035512|||http://purl.uniprot.org/annotation/VSP_045186
http://togogenome.org/gene/9606:SSTR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31391                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Somatostatin receptor type 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070127|||http://purl.uniprot.org/annotation/VAR_011703|||http://purl.uniprot.org/annotation/VAR_021560|||http://purl.uniprot.org/annotation/VAR_021561|||http://purl.uniprot.org/annotation/VAR_049441
http://togogenome.org/gene/9606:LRMDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2I8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich melanocyte differentiation-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089781|||http://purl.uniprot.org/annotation/VAR_033686
http://togogenome.org/gene/9606:PTGES3L-AARSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTE6                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Alanyl-tRNA editing protein Aarsd1|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277465|||http://purl.uniprot.org/annotation/VSP_023014|||http://purl.uniprot.org/annotation/VSP_043142
http://togogenome.org/gene/9606:L3MBTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W9S8|||http://purl.uniprot.org/uniprot/Q8NA19                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHHC-type|||Disordered|||In isoform 2.|||Lethal(3)malignant brain tumor-like protein 4|||MBT|||MBT 1|||MBT 2|||MBT 3|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337077|||http://purl.uniprot.org/annotation/VAR_060435|||http://purl.uniprot.org/annotation/VAR_060436|||http://purl.uniprot.org/annotation/VSP_033863|||http://purl.uniprot.org/annotation/VSP_033864
http://togogenome.org/gene/9606:FGF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVY3|||http://purl.uniprot.org/uniprot/P61328                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Fibroblast growth factor 12|||Gain of function, affects voltage dependence of SCN8A fast inactivation.|||In DEE47; increased function in positive regulation of SCN8A voltage-dependent sodium channel activity.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147604|||http://purl.uniprot.org/annotation/VAR_076507|||http://purl.uniprot.org/annotation/VSP_010222
http://togogenome.org/gene/9606:ANKRD34A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YU3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Abolishes methylation by N6AMT1.|||Ankyrin repeat domain-containing protein 34A|||Basic and acidic residues|||Disordered|||N5-methylglutamine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319100
http://togogenome.org/gene/9606:KRTAP19-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI72                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 19-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223907
http://togogenome.org/gene/9606:PNRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12796                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the interaction with the nuclear receptors; when associated with A-287.|||Abolishes the interaction with the nuclear receptors; when associated with A-290.|||Disordered|||In isoform 2.|||Nuclear localization signal|||Polar residues|||Proline-rich nuclear receptor coactivator 1|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058482|||http://purl.uniprot.org/annotation/VAR_051284|||http://purl.uniprot.org/annotation/VSP_055501
http://togogenome.org/gene/9606:HELZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2P0H7U5|||http://purl.uniprot.org/uniprot/B7ZLW2|||http://purl.uniprot.org/uniprot/P42694                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||DEAA box|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable helicase with zinc finger domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089185|||http://purl.uniprot.org/annotation/VAR_057273|||http://purl.uniprot.org/annotation/VAR_057274|||http://purl.uniprot.org/annotation/VAR_057275|||http://purl.uniprot.org/annotation/VSP_054493|||http://purl.uniprot.org/annotation/VSP_054494|||http://purl.uniprot.org/annotation/VSP_054495
http://togogenome.org/gene/9606:OSTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Osteopetrosis-associated transmembrane protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021963|||http://purl.uniprot.org/annotation/VAR_051257
http://togogenome.org/gene/9606:ZNF334                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1P4|||http://purl.uniprot.org/uniprot/Q9HCZ1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 334                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047537|||http://purl.uniprot.org/annotation/VAR_052813
http://togogenome.org/gene/9606:CYSLTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4ZKH2|||http://purl.uniprot.org/uniprot/Q5KU17|||http://purl.uniprot.org/uniprot/Q9NS75                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteinyl leukotriene receptor 2|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069303
http://togogenome.org/gene/9606:ULK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDG2|||http://purl.uniprot.org/uniprot/Q6PHR2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased kinase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of kinase activity. Does not promote GLI1 nuclear localization.|||MIT 1|||MIT 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250150|||http://purl.uniprot.org/annotation/VAR_057113|||http://purl.uniprot.org/annotation/VAR_059771|||http://purl.uniprot.org/annotation/VSP_038147|||http://purl.uniprot.org/annotation/VSP_038148|||http://purl.uniprot.org/annotation/VSP_039925|||http://purl.uniprot.org/annotation/VSP_057411
http://togogenome.org/gene/9606:ATAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X797|||http://purl.uniprot.org/uniprot/B7Z4Q7|||http://purl.uniprot.org/uniprot/Q5SQI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2-fold increase in activity.|||20% of wild-type acetyltransferase activity.|||Alpha-tubulin N-acetyltransferase 1|||Asymmetric dimethylarginine|||Crucial for catalytic activity|||Disordered|||In isoform 2.|||In isoform 3, isoform 6 and isoform 7.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 7.|||Loss of acetyltransferase activity.|||Marginal increase in activity.|||N-acetyltransferase|||N6-acetyllysine; by autocatalysis|||No effect on catalytic activity.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Reduced activity.|||Slight increase in activity.|||Strong reduction in acetyltransferase activity.|||Strong reduction in activity.|||Strong reduction in microtubule acetylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348066|||http://purl.uniprot.org/annotation/PRO_5012655192|||http://purl.uniprot.org/annotation/PRO_5014275537|||http://purl.uniprot.org/annotation/VSP_052899|||http://purl.uniprot.org/annotation/VSP_052900|||http://purl.uniprot.org/annotation/VSP_052901|||http://purl.uniprot.org/annotation/VSP_052902|||http://purl.uniprot.org/annotation/VSP_052903|||http://purl.uniprot.org/annotation/VSP_052904
http://togogenome.org/gene/9606:ADCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1T6|||http://purl.uniprot.org/uniprot/Q7Z695                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ABC1 atypical kinase-like|||Helical|||Protein kinase|||Proton acceptor|||Uncharacterized aarF domain-containing protein kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271792|||http://purl.uniprot.org/annotation/VAR_029992|||http://purl.uniprot.org/annotation/VAR_029993|||http://purl.uniprot.org/annotation/VAR_029994|||http://purl.uniprot.org/annotation/VAR_041418|||http://purl.uniprot.org/annotation/VAR_041419|||http://purl.uniprot.org/annotation/VAR_060990
http://togogenome.org/gene/9606:SAAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G1UCX3|||http://purl.uniprot.org/uniprot/Q96ER3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Phosphothreonine|||Protein SAAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279540|||http://purl.uniprot.org/annotation/VAR_053846|||http://purl.uniprot.org/annotation/VAR_053847
http://togogenome.org/gene/9606:NOM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5C9Z4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Loss of interaction with PPP1CA and loss of ability to relocalize PPP1CA to the nucleolus; when associated with A-308.|||Loss of interaction with PPP1CA and loss of ability to relocalize PPP1CA to the nucleolus; when associated with A-310.|||MI|||MIF4G|||Necessary for nucleolar localization and for targeting PPP1CA to the nucleolus|||Nucleolar MIF4G domain-containing protein 1|||Phosphoserine|||Required for efficient binding to PPP1CA and for targeting PPP1CA to the nucleolus                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286823|||http://purl.uniprot.org/annotation/VAR_032187|||http://purl.uniprot.org/annotation/VAR_032188|||http://purl.uniprot.org/annotation/VAR_032189|||http://purl.uniprot.org/annotation/VAR_032190|||http://purl.uniprot.org/annotation/VAR_053051|||http://purl.uniprot.org/annotation/VAR_061999
http://togogenome.org/gene/9606:ISCU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ30|||http://purl.uniprot.org/uniprot/B4DNC9|||http://purl.uniprot.org/uniprot/Q9H1K1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Cysteine persulfide|||Cysteine persulfide intermediate|||Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Slightly decreases the cysteine desulfurase activity in the presence of FXN; when associated with A-95. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN; when associated with A-95. Loss of the [2Fe-2S] cluster formation.|||Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Slightly decreases the cysteine desulfurase activity in the presence of FXN; when associated with A-95. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN; when associated with A.69. Loss of the [2Fe-2S] cluster formation.|||Does not affect ISC complex formation. Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Loss of iron-based stimulation of the cysteine desulfurase activity in the presence of FXN. Loss of the [2Fe-2S] cluster formation.|||Does not affect mitochondrial localization. Loss of iron-sulfur cluster biogenesis. Does not affect reductive cleavage of the ISCU2-bound-persulfide by FDX2.|||Does not affect the SDA complex formation. Abolishes desulfurase activity of SDA complex when zinc ion is bound. Activated by FXN when component of SDAU complex.|||Does not affect the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN.|||Does not affect the unstimulated cysteine desulfurase activity in the absence of FXN. Does not affect the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN. Does not affect the [2Fe-2S] cluster assembly.|||In isoform 2.|||Iron-sulfur cluster assembly enzyme ISCU|||Loss of iron-based stimulation of the cysteine desulfurase activity in the presence of FXN.|||Loss of phosphorylation. Does not affect phosphorylation.|||Mediates ISCU dimerization and de novo [2Fe-2S] cluster assembly|||Mitochondrion|||NIF system FeS cluster assembly NifU N-terminal|||Phosphoserine; by MTOR|||Slightly decrease the cysteine desulfurase activity in the presence of FXN. Does not affect iron based stimulation of the cysteine desulfurase activity in the presence of FXN.|||Stabilizes the D-state.|||Stabilizes the S-state.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019692|||http://purl.uniprot.org/annotation/VAR_060728|||http://purl.uniprot.org/annotation/VSP_013492
http://togogenome.org/gene/9606:SIPA1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43166                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||PDZ|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by PLK2|||Phosphothreonine|||Phosphothreonine; by PLK2|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated 1-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056746|||http://purl.uniprot.org/annotation/VAR_035549|||http://purl.uniprot.org/annotation/VAR_049152|||http://purl.uniprot.org/annotation/VSP_010917|||http://purl.uniprot.org/annotation/VSP_054774
http://togogenome.org/gene/9606:KRTAP4-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||26 X 5 AA repeats of C-C-[GRQVCH]-[SPT]-[VSTQR]|||3|||4|||5|||6|||7|||8|||9|||In allele KAP4.13.|||In allele KAP4.4-v1.|||Keratin-associated protein 4-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185172|||http://purl.uniprot.org/annotation/VAR_032772|||http://purl.uniprot.org/annotation/VAR_053459|||http://purl.uniprot.org/annotation/VAR_053460|||http://purl.uniprot.org/annotation/VAR_053461|||http://purl.uniprot.org/annotation/VAR_064559
http://togogenome.org/gene/9606:SPSB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BD6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RNF7 and CUL5.|||B30.2/SPRY|||Loss of phosphorylation.|||Phosphotyrosine; by MET|||SOCS box|||SPRY domain-containing SOCS box protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238472
http://togogenome.org/gene/9606:SLC9A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AI14                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=C/M3|||Helical; Name=D/M4|||Helical; Name=E/M5|||Helical; Name=F/M5A|||Helical; Name=G/M5B|||Helical; Name=H/M6|||Helical; Name=I/M7|||Helical; Name=J/M8|||Helical; Name=K/M9|||Helical; Name=M/M10|||N-linked (GlcNAc...) asparagine|||Name=A/M1|||Name=B/M2|||Name=L|||Sodium/hydrogen exchanger 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314665|||http://purl.uniprot.org/annotation/VAR_056209|||http://purl.uniprot.org/annotation/VAR_056210
http://togogenome.org/gene/9606:CERK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCT0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  15% decrease in catalytic activity and decreased stability.|||71% decrease in catalytic activity but no effect on substrate affinity.|||99% decrease in catalytic activity but no effect on substrate affinity.|||Ceramide kinase|||DAGKc|||Essential for enzyme activity|||In isoform 2.|||Phosphoserine|||Proton donor/acceptor|||Required for binding to sulfatide and phosphoinositides                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181354|||http://purl.uniprot.org/annotation/VAR_053685|||http://purl.uniprot.org/annotation/VAR_053686|||http://purl.uniprot.org/annotation/VAR_053687|||http://purl.uniprot.org/annotation/VSP_056944
http://togogenome.org/gene/9606:TSPY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CV99                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Testis-specific Y-encoded protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000408002
http://togogenome.org/gene/9606:AKR1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51857                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member D1|||In CBAS2.|||In CBAS2; decreases protein level; accumulates in inclusion bodies; acks of 5-beta-reductase activity.|||In CBAS2; decreases protein level; accumulates in inclusion bodies; decreases 5-beta-reductase activity.|||In CBAS2; decreases protein level; accumulates in inclusion bodies; lacks of 5-beta-reductase activity.|||In CBAS2; highly reduced KM and Vmax with cortisone as substrate. Increases KM and decreases kcat with testosterone as substrate. No change in NADPH affinity. More thermolabile in the absence of NADPH. Reduces 5-beta-reductase activity.|||In isoform 2.|||In isoform 3.|||Loss of activity.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124669|||http://purl.uniprot.org/annotation/VAR_033007|||http://purl.uniprot.org/annotation/VAR_033008|||http://purl.uniprot.org/annotation/VAR_044430|||http://purl.uniprot.org/annotation/VAR_044431|||http://purl.uniprot.org/annotation/VAR_081755|||http://purl.uniprot.org/annotation/VAR_081756|||http://purl.uniprot.org/annotation/VSP_042901|||http://purl.uniprot.org/annotation/VSP_042913
http://togogenome.org/gene/9606:ORM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02763                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-1-acid glycoprotein 1|||In allele ORM1*F2.|||In allele ORM1*S.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000170|||http://purl.uniprot.org/annotation/PRO_0000017860|||http://purl.uniprot.org/annotation/VAR_013840|||http://purl.uniprot.org/annotation/VAR_013841|||http://purl.uniprot.org/annotation/VAR_056166
http://togogenome.org/gene/9606:ZCCHC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DN1|||http://purl.uniprot.org/uniprot/Q8N3Z6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||CCHC-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Zinc finger CCHC domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150959|||http://purl.uniprot.org/annotation/VAR_054958|||http://purl.uniprot.org/annotation/VAR_054959|||http://purl.uniprot.org/annotation/VSP_013841|||http://purl.uniprot.org/annotation/VSP_013842
http://togogenome.org/gene/9606:SPINK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Kazal-like|||Pyrrolidone carboxylic acid|||Reactive bond|||Serine protease inhibitor Kazal-type 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016575|||http://purl.uniprot.org/annotation/VAR_034020
http://togogenome.org/gene/9606:HAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54257                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HAP1 N-terminal|||Huntingtin-associated protein 1|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||May influence the age-at-onset of Huntington disease; increases binding to mutated HTT; influences HTT degradation.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083894|||http://purl.uniprot.org/annotation/VAR_046736|||http://purl.uniprot.org/annotation/VAR_046737|||http://purl.uniprot.org/annotation/VAR_046738|||http://purl.uniprot.org/annotation/VAR_046739|||http://purl.uniprot.org/annotation/VAR_046741|||http://purl.uniprot.org/annotation/VAR_046742|||http://purl.uniprot.org/annotation/VAR_056906|||http://purl.uniprot.org/annotation/VAR_056907|||http://purl.uniprot.org/annotation/VAR_056908|||http://purl.uniprot.org/annotation/VAR_056909|||http://purl.uniprot.org/annotation/VAR_062817|||http://purl.uniprot.org/annotation/VSP_004277|||http://purl.uniprot.org/annotation/VSP_004278|||http://purl.uniprot.org/annotation/VSP_038754
http://togogenome.org/gene/9606:BAG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95817                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BAG|||BAG family molecular chaperone regulator 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In CMD1HH.|||In CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis.|||In MFM6; interferes with the differentiation of skeletal muscle cells; does not cause functional alterations in cardiomyocyte cells.|||N-acetylserine|||No functional consequences.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Significant loss of interaction with HSPA8.|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088868|||http://purl.uniprot.org/annotation/VAR_048344|||http://purl.uniprot.org/annotation/VAR_048345|||http://purl.uniprot.org/annotation/VAR_048346|||http://purl.uniprot.org/annotation/VAR_048347|||http://purl.uniprot.org/annotation/VAR_063089|||http://purl.uniprot.org/annotation/VAR_065479|||http://purl.uniprot.org/annotation/VAR_065480|||http://purl.uniprot.org/annotation/VAR_066777|||http://purl.uniprot.org/annotation/VAR_066778|||http://purl.uniprot.org/annotation/VAR_066779|||http://purl.uniprot.org/annotation/VAR_066780|||http://purl.uniprot.org/annotation/VAR_066781|||http://purl.uniprot.org/annotation/VAR_066782|||http://purl.uniprot.org/annotation/VAR_066783|||http://purl.uniprot.org/annotation/VAR_066784|||http://purl.uniprot.org/annotation/VAR_066785|||http://purl.uniprot.org/annotation/VAR_066786|||http://purl.uniprot.org/annotation/VAR_066787|||http://purl.uniprot.org/annotation/VAR_066788
http://togogenome.org/gene/9606:FYTTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||UAP56-binding motif|||UAP56-interacting factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287441|||http://purl.uniprot.org/annotation/VAR_062411|||http://purl.uniprot.org/annotation/VSP_038658|||http://purl.uniprot.org/annotation/VSP_038659|||http://purl.uniprot.org/annotation/VSP_038660|||http://purl.uniprot.org/annotation/VSP_038661
http://togogenome.org/gene/9606:PSG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ74                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014915|||http://purl.uniprot.org/annotation/VAR_033620|||http://purl.uniprot.org/annotation/VAR_049924|||http://purl.uniprot.org/annotation/VSP_041096|||http://purl.uniprot.org/annotation/VSP_041097
http://togogenome.org/gene/9606:PLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4B4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to the centrosome and ability to induce the G2/M arrest.|||Disordered|||Kinase defective mutant, abolishes activity.|||Kinase-defective mutant.|||POLO box 1|||POLO box 2|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086564|||http://purl.uniprot.org/annotation/VAR_021091|||http://purl.uniprot.org/annotation/VAR_021092|||http://purl.uniprot.org/annotation/VAR_021093|||http://purl.uniprot.org/annotation/VAR_021094|||http://purl.uniprot.org/annotation/VAR_021095|||http://purl.uniprot.org/annotation/VAR_021096|||http://purl.uniprot.org/annotation/VAR_062384
http://togogenome.org/gene/9606:RFX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48380                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||RFX-type winged-helix|||Transcription factor RFX3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215290|||http://purl.uniprot.org/annotation/VSP_007626|||http://purl.uniprot.org/annotation/VSP_007627|||http://purl.uniprot.org/annotation/VSP_015162|||http://purl.uniprot.org/annotation/VSP_015163
http://togogenome.org/gene/9606:CFAP54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N23                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 54|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324606|||http://purl.uniprot.org/annotation/VAR_056834|||http://purl.uniprot.org/annotation/VAR_056835|||http://purl.uniprot.org/annotation/VAR_056836|||http://purl.uniprot.org/annotation/VSP_057365|||http://purl.uniprot.org/annotation/VSP_057366
http://togogenome.org/gene/9606:THEMIS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1K5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CABIT 1|||CABIT 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Protein THEMIS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252378|||http://purl.uniprot.org/annotation/VAR_027846|||http://purl.uniprot.org/annotation/VAR_027847|||http://purl.uniprot.org/annotation/VSP_037964|||http://purl.uniprot.org/annotation/VSP_037965|||http://purl.uniprot.org/annotation/VSP_055714
http://togogenome.org/gene/9606:MMP26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J8YUH5|||http://purl.uniprot.org/uniprot/Q9NRE1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cysteine switch|||Matrix metalloproteinase-26|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028855|||http://purl.uniprot.org/annotation/PRO_0000028856|||http://purl.uniprot.org/annotation/VAR_033489|||http://purl.uniprot.org/annotation/VAR_033490
http://togogenome.org/gene/9606:RNF167                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6Y7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||Disordered|||Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1.|||E3 ubiquitin-protein ligase RNF167|||Found in a tumor sample; unknown pathological significance; abolished ability to regulate protein trafficking and localization.|||Found in a tumor sample; unknown pathological significance; impaired localization to endosomes.|||Found in a tumor sample; unknown pathological significance; impaired localization to lysosomes and ability to regulate lysosome positioning.|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PA|||Pro residues|||RING-type; atypical|||Reduced N-glycosylation. Abolished N-glycosylation; when associated with Q-33.|||Reduced N-glycosylation. Abolished N-glycosylation; when associated with Q-79.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245593|||http://purl.uniprot.org/annotation/VAR_026996|||http://purl.uniprot.org/annotation/VAR_086371|||http://purl.uniprot.org/annotation/VAR_086372|||http://purl.uniprot.org/annotation/VAR_086373|||http://purl.uniprot.org/annotation/VSP_061564
http://togogenome.org/gene/9606:ZNF735                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CB33                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Putative zinc finger protein 735                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000383475
http://togogenome.org/gene/9606:GPX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75715|||http://purl.uniprot.org/uniprot/V9HWN8                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Epididymal secretory glutathione peroxidase|||Glutathione peroxidase|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013076|||http://purl.uniprot.org/annotation/PRO_5014314729|||http://purl.uniprot.org/annotation/VAR_012040|||http://purl.uniprot.org/annotation/VAR_061206|||http://purl.uniprot.org/annotation/VSP_043046
http://togogenome.org/gene/9606:TERB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHR7                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Telomere repeats-binding bouquet formation protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263717|||http://purl.uniprot.org/annotation/VAR_029614|||http://purl.uniprot.org/annotation/VAR_076385|||http://purl.uniprot.org/annotation/VAR_076386
http://togogenome.org/gene/9606:CTSV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R717|||http://purl.uniprot.org/uniprot/O60911                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin L2|||Cathepsin propeptide inhibitor|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026277|||http://purl.uniprot.org/annotation/PRO_0000026278|||http://purl.uniprot.org/annotation/PRO_5018537672
http://togogenome.org/gene/9606:OR2H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCM6|||http://purl.uniprot.org/uniprot/Q9GZK4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-16*02.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150479|||http://purl.uniprot.org/annotation/VAR_010944|||http://purl.uniprot.org/annotation/VAR_053143
http://togogenome.org/gene/9606:ARL14EP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8R7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ARL14 effector protein|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251892|||http://purl.uniprot.org/annotation/VAR_033740
http://togogenome.org/gene/9606:PDGFRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16234                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CRK.|||Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-572.|||Abolishes interaction with SRC-family members and impairs internalization of the activated receptor; when associated with F-574.|||Basic and acidic residues|||Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In GIST sample; constitutively activated kinase.|||In GIST.|||In GISTPS; increased platelet-derived growth factor alpha-receptor activity; constitutively activated kinase.|||In GISTPS; unknown pathological significance.|||In a GIST sample; constitutively activated kinase.|||In a GIST sample; imatinib resistant, constitutively activated kinase.|||In a GIST sample; imatinib sensitive, constitutively activated kinase.|||In a glioblastoma multiforme sample; somatic mutation.|||In a hypereosinophilic syndrome sample; constitutively activated kinase.|||In a hypereosinophilic syndrome sample; does not lead to constitutive kinase activation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No effect on autophosphorylation and phosphorylation of PLCG1. Abolishes activation of phosphatidylinositol 3-kinase.|||Phosphotyrosine; by autocatalysis|||Platelet-derived growth factor receptor alpha|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly reduced interaction with PTPN11 and GRB2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016760|||http://purl.uniprot.org/annotation/VAR_034378|||http://purl.uniprot.org/annotation/VAR_042032|||http://purl.uniprot.org/annotation/VAR_042033|||http://purl.uniprot.org/annotation/VAR_042034|||http://purl.uniprot.org/annotation/VAR_042035|||http://purl.uniprot.org/annotation/VAR_042036|||http://purl.uniprot.org/annotation/VAR_042037|||http://purl.uniprot.org/annotation/VAR_066460|||http://purl.uniprot.org/annotation/VAR_066461|||http://purl.uniprot.org/annotation/VAR_066462|||http://purl.uniprot.org/annotation/VAR_066463|||http://purl.uniprot.org/annotation/VAR_066464|||http://purl.uniprot.org/annotation/VAR_066465|||http://purl.uniprot.org/annotation/VAR_066466|||http://purl.uniprot.org/annotation/VAR_066467|||http://purl.uniprot.org/annotation/VAR_066468|||http://purl.uniprot.org/annotation/VAR_066469|||http://purl.uniprot.org/annotation/VAR_066470|||http://purl.uniprot.org/annotation/VAR_066471|||http://purl.uniprot.org/annotation/VAR_066472|||http://purl.uniprot.org/annotation/VAR_066473|||http://purl.uniprot.org/annotation/VAR_066474|||http://purl.uniprot.org/annotation/VAR_066475|||http://purl.uniprot.org/annotation/VAR_083158|||http://purl.uniprot.org/annotation/VAR_083159|||http://purl.uniprot.org/annotation/VAR_083160|||http://purl.uniprot.org/annotation/VSP_007833|||http://purl.uniprot.org/annotation/VSP_007834|||http://purl.uniprot.org/annotation/VSP_042015|||http://purl.uniprot.org/annotation/VSP_042016
http://togogenome.org/gene/9606:NSUN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H649                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Catalytic mutant. Abolishes ability to methylate mt-tRNA(Met).|||In C2A; catalytic mutant. Abolishes ability to methylate mt-tRNA(Met).|||In COXPD48.|||In COXPD48; unknown pathological significance.|||Nucleophile|||tRNA (cytosine(34)-C(5))-methyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289230|||http://purl.uniprot.org/annotation/VAR_032605|||http://purl.uniprot.org/annotation/VAR_077445|||http://purl.uniprot.org/annotation/VAR_085049|||http://purl.uniprot.org/annotation/VAR_085050
http://togogenome.org/gene/9606:MACIR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GV9                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Macrophage immunometabolism regulator|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316776
http://togogenome.org/gene/9606:RRAGD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQL2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Decreased RPTOR-binding.|||Disordered|||In HOMG7; increased positive regulation of TORC1 signaling; increased phosphorylation of the downstream molecule S6K1.|||In isoform 2.|||Increased RPTOR-binding.|||Ras-related GTP-binding protein D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239953|||http://purl.uniprot.org/annotation/VAR_087904|||http://purl.uniprot.org/annotation/VAR_087905|||http://purl.uniprot.org/annotation/VAR_087906|||http://purl.uniprot.org/annotation/VAR_087907|||http://purl.uniprot.org/annotation/VAR_087908|||http://purl.uniprot.org/annotation/VAR_087909|||http://purl.uniprot.org/annotation/VSP_052078
http://togogenome.org/gene/9606:RGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2W5|||http://purl.uniprot.org/uniprot/B7Z915|||http://purl.uniprot.org/uniprot/B7ZB61|||http://purl.uniprot.org/uniprot/Q9NZL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform B.|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Ral guanine nucleotide dissociation stimulator-like 1|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068885|||http://purl.uniprot.org/annotation/VAR_035823|||http://purl.uniprot.org/annotation/VAR_035824|||http://purl.uniprot.org/annotation/VSP_001824
http://togogenome.org/gene/9606:UQCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z314|||http://purl.uniprot.org/uniprot/Q3KRB6|||http://purl.uniprot.org/uniprot/Q9NVA1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Ubiquinol-cytochrome c chaperone|||Ubiquinol-cytochrome c reductase complex assembly factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206560|||http://purl.uniprot.org/annotation/VAR_028047|||http://purl.uniprot.org/annotation/VAR_028048|||http://purl.uniprot.org/annotation/VAR_036612|||http://purl.uniprot.org/annotation/VSP_000855|||http://purl.uniprot.org/annotation/VSP_000856|||http://purl.uniprot.org/annotation/VSP_000857|||http://purl.uniprot.org/annotation/VSP_016027|||http://purl.uniprot.org/annotation/VSP_043406
http://togogenome.org/gene/9606:ARMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPT6|||http://purl.uniprot.org/uniprot/F5GZY1|||http://purl.uniprot.org/uniprot/Q9H993                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Damage-control phosphatase ARMT1|||Damage-control phosphatase ARMT1-like metal-binding|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||Subfamily III RTxK motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230795|||http://purl.uniprot.org/annotation/VAR_025791|||http://purl.uniprot.org/annotation/VAR_053090|||http://purl.uniprot.org/annotation/VAR_053091|||http://purl.uniprot.org/annotation/VAR_053092|||http://purl.uniprot.org/annotation/VAR_053093|||http://purl.uniprot.org/annotation/VAR_053094|||http://purl.uniprot.org/annotation/VAR_053095
http://togogenome.org/gene/9606:SLC37A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCC5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sugar phosphate exchanger 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309278|||http://purl.uniprot.org/annotation/VSP_029113|||http://purl.uniprot.org/annotation/VSP_029114|||http://purl.uniprot.org/annotation/VSP_029115
http://togogenome.org/gene/9606:PHF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y3N9|||http://purl.uniprot.org/uniprot/O95327|||http://purl.uniprot.org/uniprot/Q9UPP1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to H3K4me3; when associated with A-43. Abolishes binding to H3K4me3; when associated with A-65.|||Abolishes binding to H3K4me3; when associated with A-50.|||Abolishes histone methyltransferase activity.|||Basic and acidic residues|||Disordered|||Found in patients with autism spectrum disorders; unknown pathological significance.|||Histone lysine demethylase PHF8|||Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-120.|||Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-69.|||In MRXSSD; abolishes histone methyltransferase activity; reduces transcriptional activation activity.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||JmjC|||Linker|||PHD-type|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduces transcriptional activation activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059295|||http://purl.uniprot.org/annotation/VAR_062250|||http://purl.uniprot.org/annotation/VAR_076254|||http://purl.uniprot.org/annotation/VSP_014964|||http://purl.uniprot.org/annotation/VSP_014965|||http://purl.uniprot.org/annotation/VSP_043640|||http://purl.uniprot.org/annotation/VSP_054019|||http://purl.uniprot.org/annotation/VSP_054020|||http://purl.uniprot.org/annotation/VSP_054021
http://togogenome.org/gene/9606:C10orf53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6V4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||UPF0728 protein C10orf53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089794|||http://purl.uniprot.org/annotation/VSP_036509|||http://purl.uniprot.org/annotation/VSP_036867|||http://purl.uniprot.org/annotation/VSP_046396
http://togogenome.org/gene/9606:KLHDC7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch domain-containing protein 7B|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229000
http://togogenome.org/gene/9606:SLC25A28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TR30|||http://purl.uniprot.org/uniprot/Q96A46                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||Mitoferrin-2|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235255|||http://purl.uniprot.org/annotation/VSP_018413|||http://purl.uniprot.org/annotation/VSP_018414|||http://purl.uniprot.org/annotation/VSP_018415
http://togogenome.org/gene/9606:PRDX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTR2|||http://purl.uniprot.org/uniprot/P30048                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate|||Forms obligate homodimers under reducing and oxidizing conditions; does not form dodecamer rings under reducing conditions.|||Forms predominantly dodecamer rings.|||Impairs phosphorylation.|||In PPPCD.|||In SCAR32; absent protein, reduced glutathione peroxidase activity and reduced PRDX5 protein levels in patient fibroblasts.|||In SCAR32; unknown pathological significance.|||In SCAR32; unstable protein leading to its degradation, reduced glutathione peroxidase activity and reduced PRDX5 protein levels in patient fibroblasts.|||In isoform 2.|||Interchain (with C-108); in linked form|||Interchain (with C-229); in linked form|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Thioredoxin|||Thioredoxin-dependent peroxide reductase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023782|||http://purl.uniprot.org/annotation/VAR_025052|||http://purl.uniprot.org/annotation/VAR_025053|||http://purl.uniprot.org/annotation/VAR_025054|||http://purl.uniprot.org/annotation/VAR_059546|||http://purl.uniprot.org/annotation/VAR_087329|||http://purl.uniprot.org/annotation/VAR_087330|||http://purl.uniprot.org/annotation/VAR_087331|||http://purl.uniprot.org/annotation/VAR_087332|||http://purl.uniprot.org/annotation/VSP_054050
http://togogenome.org/gene/9606:MUC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q685J3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34|||35|||36|||37|||38|||39|||4|||40|||41|||42|||43|||44|||45|||46|||47|||48|||49|||5|||50|||51|||52|||53|||54|||55|||56|||57|||58|||59|||59 X approximate tandem repeats|||6|||7|||8|||9|||Cleavage|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Mucin-17|||N-linked (GlcNAc...) asparagine|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326254|||http://purl.uniprot.org/annotation/VAR_040047|||http://purl.uniprot.org/annotation/VAR_040048|||http://purl.uniprot.org/annotation/VAR_040049|||http://purl.uniprot.org/annotation/VAR_040050|||http://purl.uniprot.org/annotation/VAR_040051|||http://purl.uniprot.org/annotation/VAR_040052|||http://purl.uniprot.org/annotation/VAR_040053|||http://purl.uniprot.org/annotation/VAR_040054|||http://purl.uniprot.org/annotation/VAR_040055|||http://purl.uniprot.org/annotation/VAR_040056|||http://purl.uniprot.org/annotation/VAR_040057|||http://purl.uniprot.org/annotation/VAR_040058|||http://purl.uniprot.org/annotation/VAR_040059|||http://purl.uniprot.org/annotation/VAR_061489|||http://purl.uniprot.org/annotation/VAR_061490|||http://purl.uniprot.org/annotation/VAR_061491|||http://purl.uniprot.org/annotation/VAR_061492|||http://purl.uniprot.org/annotation/VAR_061493|||http://purl.uniprot.org/annotation/VAR_061494|||http://purl.uniprot.org/annotation/VAR_061495|||http://purl.uniprot.org/annotation/VSP_032648|||http://purl.uniprot.org/annotation/VSP_032649
http://togogenome.org/gene/9606:TMEM249                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2WGJ8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit TMEM249|||Cytoplasmic|||Disordered|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332223
http://togogenome.org/gene/9606:EDEM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV94                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 2|||In isoform 2.|||Loss of ERAD activity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012086|||http://purl.uniprot.org/annotation/VAR_012165|||http://purl.uniprot.org/annotation/VAR_055842|||http://purl.uniprot.org/annotation/VAR_055843|||http://purl.uniprot.org/annotation/VSP_013183
http://togogenome.org/gene/9606:ZNF316                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Zinc finger protein 316                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348942
http://togogenome.org/gene/9606:C5orf24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6I8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||UPF0461 protein C5orf24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295708|||http://purl.uniprot.org/annotation/VSP_027011
http://togogenome.org/gene/9606:STRIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Striatin-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187022|||http://purl.uniprot.org/annotation/VAR_049021|||http://purl.uniprot.org/annotation/VSP_014867|||http://purl.uniprot.org/annotation/VSP_014868
http://togogenome.org/gene/9606:CARD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||CARD|||Caspase recruitment domain-containing protein 6|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144079|||http://purl.uniprot.org/annotation/VAR_046689|||http://purl.uniprot.org/annotation/VAR_046690|||http://purl.uniprot.org/annotation/VAR_046691|||http://purl.uniprot.org/annotation/VAR_046692|||http://purl.uniprot.org/annotation/VAR_046693|||http://purl.uniprot.org/annotation/VAR_046694
http://togogenome.org/gene/9606:MYBPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ0|||http://purl.uniprot.org/uniprot/Q14324                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Myosin-binding protein C, fast-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072691|||http://purl.uniprot.org/annotation/VAR_014657|||http://purl.uniprot.org/annotation/VAR_014658|||http://purl.uniprot.org/annotation/VAR_014659|||http://purl.uniprot.org/annotation/VAR_056060|||http://purl.uniprot.org/annotation/VAR_056061|||http://purl.uniprot.org/annotation/VAR_061321|||http://purl.uniprot.org/annotation/VAR_061322
http://togogenome.org/gene/9606:HOXA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D182|||http://purl.uniprot.org/uniprot/B3KPN8|||http://purl.uniprot.org/uniprot/O43365                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A3|||In a breast cancer sample; somatic mutation.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200043|||http://purl.uniprot.org/annotation/VAR_036264|||http://purl.uniprot.org/annotation/VAR_036265
http://togogenome.org/gene/9606:VAMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15836|||http://purl.uniprot.org/uniprot/Q6FGG2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by C.botulinum neurotoxin type B (BoNT/B, botB)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)|||Abolished ubiquitination by RNF167; when associated with 66-R--R-68.|||Abolished ubiquitination by RNF167; when associated with R-77.|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Helical; Anchor for type IV membrane protein|||N-acetylserine|||Removed|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 3|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206728
http://togogenome.org/gene/9606:GAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GRB2-associated-binding protein 2|||Impaired interaction with 14-3-3 proteins and increased EGF-independent cell proliferation; when associated with A-210.|||Impaired interaction with 14-3-3 proteins and increased EGF-independent cell proliferation; when associated with A-391.|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050285|||http://purl.uniprot.org/annotation/VAR_020407|||http://purl.uniprot.org/annotation/VAR_053097|||http://purl.uniprot.org/annotation/VSP_038520
http://togogenome.org/gene/9606:FAM237A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTK4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Leucine amide|||Protein FAM237A|||Removed in the mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440611|||http://purl.uniprot.org/annotation/PRO_0000457709
http://togogenome.org/gene/9606:HCAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4Y1JWP1|||http://purl.uniprot.org/uniprot/Q9BXC0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Diminishes the response to L-lactate.|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hydroxycarboxylic acid receptor 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069586|||http://purl.uniprot.org/annotation/VAR_025151|||http://purl.uniprot.org/annotation/VAR_025152|||http://purl.uniprot.org/annotation/VAR_061218
http://togogenome.org/gene/9606:NUTM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NUT family member 2A|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266032|||http://purl.uniprot.org/annotation/VSP_034018|||http://purl.uniprot.org/annotation/VSP_034020
http://togogenome.org/gene/9606:KHSRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92945                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 12 AA imperfect repeats|||Disordered|||Far upstream element-binding protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||KH 1|||KH 2|||KH 3|||KH 4|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050137
http://togogenome.org/gene/9606:SLC38A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNN8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In FVH2.|||Solute carrier family 38 member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319593|||http://purl.uniprot.org/annotation/VAR_048125|||http://purl.uniprot.org/annotation/VAR_071252|||http://purl.uniprot.org/annotation/VAR_071253|||http://purl.uniprot.org/annotation/VAR_071254|||http://purl.uniprot.org/annotation/VAR_071255|||http://purl.uniprot.org/annotation/VAR_071256|||http://purl.uniprot.org/annotation/VAR_071257
http://togogenome.org/gene/9606:TMEM233                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 233                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394962
http://togogenome.org/gene/9606:ACIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQZ7|||http://purl.uniprot.org/uniprot/Q9UKV3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes cleavage by CASP3 and chromatin condensation activity.|||Acidic residues|||Apoptotic chromatin condensation inducer in the nucleus|||Basic and acidic residues|||Basic residues|||Cleavage; by caspase-3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphoserine; by SRPK2 and PKB/AKT1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAP|||Sufficient for interaction with RNPS1 and SAP18 and formation of the ASAP complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064436|||http://purl.uniprot.org/annotation/VAR_022031|||http://purl.uniprot.org/annotation/VAR_022032|||http://purl.uniprot.org/annotation/VAR_022033|||http://purl.uniprot.org/annotation/VAR_035777|||http://purl.uniprot.org/annotation/VAR_050632|||http://purl.uniprot.org/annotation/VAR_061547|||http://purl.uniprot.org/annotation/VSP_004025|||http://purl.uniprot.org/annotation/VSP_004026|||http://purl.uniprot.org/annotation/VSP_004028|||http://purl.uniprot.org/annotation/VSP_004029|||http://purl.uniprot.org/annotation/VSP_042204|||http://purl.uniprot.org/annotation/VSP_042205
http://togogenome.org/gene/9606:RUFY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7B1|||http://purl.uniprot.org/uniprot/Q96T51                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphorylation and endosomal targeting; when associated with F-389.|||Abolishes phosphorylation and endosomal targeting; when associated with F-400.|||Basic and acidic residues|||Disordered|||FYVE-type|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with RAB4|||Phosphoserine|||Phosphotyrosine|||RING-type|||RUN|||RUN and FYVE domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097530|||http://purl.uniprot.org/annotation/VAR_035985|||http://purl.uniprot.org/annotation/VAR_051327|||http://purl.uniprot.org/annotation/VSP_019785|||http://purl.uniprot.org/annotation/VSP_019786|||http://purl.uniprot.org/annotation/VSP_019787
http://togogenome.org/gene/9606:ADAM15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13444                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 15|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 2, isoform 11 and isoform 12.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 8.|||In isoform 6, isoform 7 and isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphotyrosine; by HCK and LCK|||Pro residues|||Reduces ADAM15-mediated T-cell aggregation.|||SH3-binding|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029082|||http://purl.uniprot.org/annotation/PRO_0000029083|||http://purl.uniprot.org/annotation/VAR_060315|||http://purl.uniprot.org/annotation/VAR_060316|||http://purl.uniprot.org/annotation/VAR_068970|||http://purl.uniprot.org/annotation/VSP_039524|||http://purl.uniprot.org/annotation/VSP_039525|||http://purl.uniprot.org/annotation/VSP_039526|||http://purl.uniprot.org/annotation/VSP_039527|||http://purl.uniprot.org/annotation/VSP_039528|||http://purl.uniprot.org/annotation/VSP_039529|||http://purl.uniprot.org/annotation/VSP_039530|||http://purl.uniprot.org/annotation/VSP_039531|||http://purl.uniprot.org/annotation/VSP_039532|||http://purl.uniprot.org/annotation/VSP_039533|||http://purl.uniprot.org/annotation/VSP_044695|||http://purl.uniprot.org/annotation/VSP_055143|||http://purl.uniprot.org/annotation/VSP_055144|||http://purl.uniprot.org/annotation/VSP_055145
http://togogenome.org/gene/9606:APH1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW43                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Gamma-secretase subunit APH-1B|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221052|||http://purl.uniprot.org/annotation/VAR_048315|||http://purl.uniprot.org/annotation/VSP_042945
http://togogenome.org/gene/9606:EPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G9JKG7|||http://purl.uniprot.org/uniprot/P01588                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Decreased erythrocyte proliferation; impaired EPOR dimerization following binding.|||Erythropoietin|||Found in a patient thought to have erythrocytosis, but had normal red cell mass; unknown pathological significance.|||In DBAL; loss of support of normal erythroid expansion or differentiation; reduced ability to promote EPOR dimer formation upon binding, resulting in reduced JAK2 activation and decreased STAT1 and STAT3 phosphorylation; mild decrease in affinity for EPOR; no effect on STAT5A phosphorylation.|||In ECYT5; unknown pathological significance.|||In a hepatocellular carcinoma.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000052|||http://purl.uniprot.org/annotation/CAR_000166|||http://purl.uniprot.org/annotation/CAR_000192|||http://purl.uniprot.org/annotation/PRO_0000008401|||http://purl.uniprot.org/annotation/PRO_5014304362|||http://purl.uniprot.org/annotation/VAR_009870|||http://purl.uniprot.org/annotation/VAR_009871|||http://purl.uniprot.org/annotation/VAR_078447|||http://purl.uniprot.org/annotation/VAR_080573|||http://purl.uniprot.org/annotation/VAR_080574|||http://purl.uniprot.org/annotation/VAR_080575|||http://purl.uniprot.org/annotation/VAR_080576|||http://purl.uniprot.org/annotation/VAR_080577
http://togogenome.org/gene/9606:HACD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P035                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CS|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313724|||http://purl.uniprot.org/annotation/VAR_037712|||http://purl.uniprot.org/annotation/VAR_037713|||http://purl.uniprot.org/annotation/VSP_056070
http://togogenome.org/gene/9606:DDHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPM6|||http://purl.uniprot.org/uniprot/O94830                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phospholipase activity. Loss of efficient targeting to the Golgi apparatus. No effect on PI(3)P-, PI(4)P-, PI(5)P-binding.|||DDHD|||Disordered|||In SPG54.|||In isoform 2.|||Loss of phospholipid binding and of Golgi/ERGIC localization; when associated with A-434 and A-435.|||Loss of phospholipid binding and of Golgi/ERGIC localization; when associated with A-434 and A-436.|||Loss of phospholipid binding and of Golgi/ERGIC localization; when associated with A-435 and A-436.|||Phospholipase DDHD2|||Phosphoserine|||SAM|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309330|||http://purl.uniprot.org/annotation/VAR_036930|||http://purl.uniprot.org/annotation/VAR_069574|||http://purl.uniprot.org/annotation/VSP_056087
http://togogenome.org/gene/9606:DCLRE1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H816                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5' exonuclease Apollo|||Abolishes interaction with TERF2.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with N-35.|||In Apm2; abolishes exonuclease activity and function on telomere maintenance. In Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with A-33.|||In Apm3; abolishes exonuclease activity and function on telomere maintenance. Impairs interaction with SPAG5.|||In DKCB8.|||In DKCB8; decreased interaction with TERF2.|||Slightly affects interaction with SPAG5.|||TBM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209119|||http://purl.uniprot.org/annotation/VAR_023292|||http://purl.uniprot.org/annotation/VAR_023293|||http://purl.uniprot.org/annotation/VAR_023294|||http://purl.uniprot.org/annotation/VAR_048891|||http://purl.uniprot.org/annotation/VAR_087866|||http://purl.uniprot.org/annotation/VAR_087867|||http://purl.uniprot.org/annotation/VAR_087868|||http://purl.uniprot.org/annotation/VAR_087869
http://togogenome.org/gene/9606:PFDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AQP2|||http://purl.uniprot.org/uniprot/Q9UHV9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Prefoldin subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124835
http://togogenome.org/gene/9606:ZNF793                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN11                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 793                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293699|||http://purl.uniprot.org/annotation/VAR_033107|||http://purl.uniprot.org/annotation/VAR_061967|||http://purl.uniprot.org/annotation/VSP_026564|||http://purl.uniprot.org/annotation/VSP_026565
http://togogenome.org/gene/9606:PIP4P1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T03                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CX5R motif|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues|||Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072579|||http://purl.uniprot.org/annotation/VSP_007815|||http://purl.uniprot.org/annotation/VSP_007816|||http://purl.uniprot.org/annotation/VSP_007817
http://togogenome.org/gene/9606:TBL1X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60907                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished homotetramerization, leading to a homodimer.|||Disordered|||Does not affect interaction with NCOR2 and GPS2.|||F-box-like|||F-box-like/WD repeat-containing protein TBL1X|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CHNG8.|||In CHNG8; unknown pathological significance.|||In CHNG8; unknown pathological significance; decreased protein expression.|||In CHNG8; unknown pathological significance; no effect on protein expression.|||In isoform 2.|||LisH|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Reduced interaction with NCOR2 and GPS2.|||Reduced interaction with NCOR2 and GPS2. Abolished ability to repress transcription.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051263|||http://purl.uniprot.org/annotation/VAR_083285|||http://purl.uniprot.org/annotation/VAR_083286|||http://purl.uniprot.org/annotation/VAR_083287|||http://purl.uniprot.org/annotation/VAR_083288|||http://purl.uniprot.org/annotation/VAR_083289|||http://purl.uniprot.org/annotation/VAR_083290|||http://purl.uniprot.org/annotation/VSP_036905
http://togogenome.org/gene/9606:SOWAHC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53LP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein SOWAHC|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274340
http://togogenome.org/gene/9606:RAB35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15286                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Destabilization of the intercellular bridge during cytokinesis. Strong reduction in fast recycling.|||Effector region|||In isoform 2.|||Loss of GTPase activity. Increased fast recycling.|||Loss of phosphorylation. No effect on binding to GDI1 and GDI2.|||O-(2-cholinephosphoryl)serine|||O-AMP-tyrosine|||Phosphomimetic mutant. Loss of binding to GDI1, GDI2, CHM and CHML.|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-35|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121245|||http://purl.uniprot.org/annotation/VSP_042918
http://togogenome.org/gene/9606:APOL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTP4|||http://purl.uniprot.org/uniprot/Q9BWW8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Apolipoprotein L6|||Basic and acidic residues|||Disordered|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137604|||http://purl.uniprot.org/annotation/VAR_053013
http://togogenome.org/gene/9606:PLS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14651                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding 1|||Actin-binding 2|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Calponin-homology (CH) 3|||Calponin-homology (CH) 4|||EF-hand 1|||EF-hand 2|||In DFNA76.|||N-acetylmethionine|||Plastin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073750|||http://purl.uniprot.org/annotation/VAR_048660|||http://purl.uniprot.org/annotation/VAR_048661|||http://purl.uniprot.org/annotation/VAR_083821|||http://purl.uniprot.org/annotation/VAR_083822|||http://purl.uniprot.org/annotation/VAR_083823|||http://purl.uniprot.org/annotation/VAR_083824
http://togogenome.org/gene/9606:NPAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2I2P5|||http://purl.uniprot.org/uniprot/Q99743                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Associated with non-Hodgkin's lymphoma and breast cancer risk.|||BHLH|||Disordered|||Neuronal PAS domain-containing protein 2|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||Pro residues|||Sufficient for heterodimer formation with BMAL1, E-box binding and for the effect of NADPH|||Susceptibility to seasonal affective disorder (SAD) and diurnal preference.|||axial binding residue|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127406|||http://purl.uniprot.org/annotation/VAR_029078|||http://purl.uniprot.org/annotation/VAR_029079
http://togogenome.org/gene/9606:CACNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06432                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Voltage-dependent calcium channel gamma-1 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164669|||http://purl.uniprot.org/annotation/VAR_012063
http://togogenome.org/gene/9606:KRTAP6-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI64                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 6-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223898
http://togogenome.org/gene/9606:TES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0U5|||http://purl.uniprot.org/uniprot/Q9UGI8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ACTL7A.|||Abolishes localization at focal adhesions.|||Disordered|||In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||PET|||Testin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075906|||http://purl.uniprot.org/annotation/VAR_050170|||http://purl.uniprot.org/annotation/VSP_003122
http://togogenome.org/gene/9606:CLIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXA5|||http://purl.uniprot.org/uniprot/P30622                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with tubulin. Abolishes localization at the microtubule plus end.|||Basic and acidic residues|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly domain-containing linker protein 1|||CCHC-type|||CLIP1 zinc knuckle|||Disordered|||Important for tubulin binding|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083527|||http://purl.uniprot.org/annotation/VAR_020398|||http://purl.uniprot.org/annotation/VAR_036446|||http://purl.uniprot.org/annotation/VAR_048672|||http://purl.uniprot.org/annotation/VAR_048673|||http://purl.uniprot.org/annotation/VAR_048674|||http://purl.uniprot.org/annotation/VAR_059206|||http://purl.uniprot.org/annotation/VSP_000765|||http://purl.uniprot.org/annotation/VSP_038201
http://togogenome.org/gene/9606:TRA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13595|||http://purl.uniprot.org/uniprot/Q549U1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 4.|||In isoform Short, isoform 3 and isoform 4.|||In isoform Short.|||Linker|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Removed|||Transformer-2 protein homolog alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081981|||http://purl.uniprot.org/annotation/VSP_005893|||http://purl.uniprot.org/annotation/VSP_005894|||http://purl.uniprot.org/annotation/VSP_005895|||http://purl.uniprot.org/annotation/VSP_057405
http://togogenome.org/gene/9606:ADD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35612|||http://purl.uniprot.org/uniprot/Q05DK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Beta-adducin|||Class II aldolase/adducin N-terminal|||Disordered|||In isoform 2, isoform 8 and isoform 9.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with calmodulin|||Phosphoserine|||Phosphoserine; by PKA and PKC|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218533|||http://purl.uniprot.org/annotation/VAR_014866|||http://purl.uniprot.org/annotation/VAR_014867|||http://purl.uniprot.org/annotation/VAR_014868|||http://purl.uniprot.org/annotation/VAR_025318|||http://purl.uniprot.org/annotation/VAR_048195|||http://purl.uniprot.org/annotation/VSP_000181|||http://purl.uniprot.org/annotation/VSP_000182|||http://purl.uniprot.org/annotation/VSP_000183|||http://purl.uniprot.org/annotation/VSP_017241|||http://purl.uniprot.org/annotation/VSP_017242|||http://purl.uniprot.org/annotation/VSP_017243|||http://purl.uniprot.org/annotation/VSP_017244|||http://purl.uniprot.org/annotation/VSP_017245|||http://purl.uniprot.org/annotation/VSP_017246|||http://purl.uniprot.org/annotation/VSP_043625|||http://purl.uniprot.org/annotation/VSP_055309
http://togogenome.org/gene/9606:EPHA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15375                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 7|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016818|||http://purl.uniprot.org/annotation/VAR_022105|||http://purl.uniprot.org/annotation/VAR_022106|||http://purl.uniprot.org/annotation/VAR_036090|||http://purl.uniprot.org/annotation/VAR_042150|||http://purl.uniprot.org/annotation/VAR_042151|||http://purl.uniprot.org/annotation/VAR_042152|||http://purl.uniprot.org/annotation/VSP_014380|||http://purl.uniprot.org/annotation/VSP_014381|||http://purl.uniprot.org/annotation/VSP_014382|||http://purl.uniprot.org/annotation/VSP_041943|||http://purl.uniprot.org/annotation/VSP_041944|||http://purl.uniprot.org/annotation/VSP_041945
http://togogenome.org/gene/9606:CC2D1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1N0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||C2|||Coiled-coil and C2 domain-containing protein 1A|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239609|||http://purl.uniprot.org/annotation/VAR_026670|||http://purl.uniprot.org/annotation/VAR_026671|||http://purl.uniprot.org/annotation/VAR_026672|||http://purl.uniprot.org/annotation/VSP_019242
http://togogenome.org/gene/9606:MC5R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33032                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  10% increase of binding to alpha-MSH.|||690% increase of binding to alpha-MSH.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melanocortin receptor 5|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069728|||http://purl.uniprot.org/annotation/VAR_013128
http://togogenome.org/gene/9606:SGIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with DPF motifs-containing proteins|||MHD|||Necessary and sufficient to mediate interaction with CANX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3-containing GRB2-like protein 3-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248395|||http://purl.uniprot.org/annotation/VAR_027297|||http://purl.uniprot.org/annotation/VAR_027298|||http://purl.uniprot.org/annotation/VAR_027299|||http://purl.uniprot.org/annotation/VAR_027300|||http://purl.uniprot.org/annotation/VSP_020273|||http://purl.uniprot.org/annotation/VSP_020274|||http://purl.uniprot.org/annotation/VSP_020275|||http://purl.uniprot.org/annotation/VSP_020276|||http://purl.uniprot.org/annotation/VSP_020277|||http://purl.uniprot.org/annotation/VSP_020278
http://togogenome.org/gene/9606:NDUFB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PH64|||http://purl.uniprot.org/uniprot/Q9Y6M9                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In MC1DN24.|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174306|||http://purl.uniprot.org/annotation/VAR_014484|||http://purl.uniprot.org/annotation/VAR_081460
http://togogenome.org/gene/9606:HSPA14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VDF9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Heat shock 70 kDa protein 14|||In a breast cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289946|||http://purl.uniprot.org/annotation/VAR_036347
http://togogenome.org/gene/9606:PHAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H814                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||Necessary for interaction with CBP80|||Necessary for poly U RNA-binding and snRNA export|||Nuclear export signal|||Nuclear localization signal|||Phosphorylated adapter RNA export protein|||Phosphoserine|||Phosphothreonine|||Removed|||Sufficient for poly U RNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239775|||http://purl.uniprot.org/annotation/VAR_051871
http://togogenome.org/gene/9606:ADAM29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD8|||http://purl.uniprot.org/uniprot/Q9UKF5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 9 AA approximate repeats|||Basic and acidic residues|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 29|||Disordered|||EGF-like|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In a cutaneous metastatic melanoma sample; somatic mutation; increases the adhesion of melanoma cells to collagens I and IV.|||In a melanoma cell line.|||In isoform Beta.|||In isoform Gamma.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029134|||http://purl.uniprot.org/annotation/PRO_0000029135|||http://purl.uniprot.org/annotation/PRO_5036300341|||http://purl.uniprot.org/annotation/VAR_036148|||http://purl.uniprot.org/annotation/VAR_036149|||http://purl.uniprot.org/annotation/VAR_066322|||http://purl.uniprot.org/annotation/VAR_066323|||http://purl.uniprot.org/annotation/VAR_066324|||http://purl.uniprot.org/annotation/VAR_066325|||http://purl.uniprot.org/annotation/VAR_066326|||http://purl.uniprot.org/annotation/VAR_066327|||http://purl.uniprot.org/annotation/VAR_066328|||http://purl.uniprot.org/annotation/VAR_066329|||http://purl.uniprot.org/annotation/VAR_066330|||http://purl.uniprot.org/annotation/VAR_066331|||http://purl.uniprot.org/annotation/VAR_066332|||http://purl.uniprot.org/annotation/VAR_066333|||http://purl.uniprot.org/annotation/VAR_066334|||http://purl.uniprot.org/annotation/VAR_066335|||http://purl.uniprot.org/annotation/VAR_066336|||http://purl.uniprot.org/annotation/VSP_005491|||http://purl.uniprot.org/annotation/VSP_005492|||http://purl.uniprot.org/annotation/VSP_005493
http://togogenome.org/gene/9606:HRH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5N1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Histamine H3 receptor|||In a Shy-Drager syndrome patient; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069690|||http://purl.uniprot.org/annotation/VAR_012235|||http://purl.uniprot.org/annotation/VSP_001881|||http://purl.uniprot.org/annotation/VSP_001882|||http://purl.uniprot.org/annotation/VSP_001883|||http://purl.uniprot.org/annotation/VSP_001884|||http://purl.uniprot.org/annotation/VSP_001885|||http://purl.uniprot.org/annotation/VSP_001886
http://togogenome.org/gene/9606:KIF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JKA9|||http://purl.uniprot.org/uniprot/Q9NS87                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Hyaluronan-mediated motility receptor C-terminal|||In BRDCS2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kinesin motor|||Kinesin-like protein KIF15|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328684|||http://purl.uniprot.org/annotation/VAR_042464|||http://purl.uniprot.org/annotation/VAR_042465|||http://purl.uniprot.org/annotation/VAR_042466|||http://purl.uniprot.org/annotation/VAR_042467|||http://purl.uniprot.org/annotation/VAR_087453|||http://purl.uniprot.org/annotation/VSP_032752|||http://purl.uniprot.org/annotation/VSP_032753|||http://purl.uniprot.org/annotation/VSP_032754|||http://purl.uniprot.org/annotation/VSP_032755
http://togogenome.org/gene/9606:WDR19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEZ3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CED4 and SLSN8.|||In NPHP13.|||In SLSN8.|||In SPGF72; unknown pathological significance; the mutant is absent from sperm neck and flagellum.|||In SRTD5.|||In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233156|||http://purl.uniprot.org/annotation/VAR_053424|||http://purl.uniprot.org/annotation/VAR_067312|||http://purl.uniprot.org/annotation/VAR_067313|||http://purl.uniprot.org/annotation/VAR_067314|||http://purl.uniprot.org/annotation/VAR_073673|||http://purl.uniprot.org/annotation/VAR_073674|||http://purl.uniprot.org/annotation/VAR_073675|||http://purl.uniprot.org/annotation/VAR_073676|||http://purl.uniprot.org/annotation/VAR_073677|||http://purl.uniprot.org/annotation/VAR_073678|||http://purl.uniprot.org/annotation/VAR_073679|||http://purl.uniprot.org/annotation/VAR_087243|||http://purl.uniprot.org/annotation/VSP_018073|||http://purl.uniprot.org/annotation/VSP_018074
http://togogenome.org/gene/9606:DNLZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SXM8                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant|||Transit Peptide|||Zinc Finger                                                                                  ^@                                                                                  DNL-type|||DNL-type zinc finger protein|||Disordered|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317166|||http://purl.uniprot.org/annotation/VAR_053993|||http://purl.uniprot.org/annotation/VAR_053994
http://togogenome.org/gene/9606:B4GALT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43286                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 5|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080545|||http://purl.uniprot.org/annotation/VAR_024468|||http://purl.uniprot.org/annotation/VAR_033538|||http://purl.uniprot.org/annotation/VAR_054022
http://togogenome.org/gene/9606:SNAP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60880                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)|||Decreased binding affinity for ZDHHC17.|||Decreased cleavage by BoNT/C, no change in cleavage by BoNT/A.|||Decreased cleavage by C.botulinum BoNT/C, no change in cleavage by C.botulinum BoNT/A (botA).|||Disordered|||In CMS18; interfers with calcium-induced fusion; inhibits exocytosis of catecholamine-containing vesicles.|||In isoform 2.|||Interaction with CENPF|||Interaction with ZDHHC17|||Mildly decreased binding affinity for ZDHHC17.|||No effect on ZDHHC17 binding.|||Not cleaved by BoNT/C.|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine|||Slight decrease in affinity for BoNT/A, increases kcat for BoNT/A.|||Small decrease in affinity for C.botulinum BoNT/A, increased efficiency of BoNT/C cleavage.|||Small decrease in affinity for C.botulinum BoNT/A.|||Synaptosomal-associated protein 25|||t-SNARE coiled-coil homology 1|||t-SNARE coiled-coil homology 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213587|||http://purl.uniprot.org/annotation/VAR_073698|||http://purl.uniprot.org/annotation/VSP_006186
http://togogenome.org/gene/9606:FCGR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y755|||http://purl.uniprot.org/uniprot/P08637                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by ADAM17|||Cytoplasmic|||Decreases the association with either CD247 or FCER1G.|||Decreases the association with either CD247 or FCER1G. Decreases cell surface expression.|||Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-212.|||Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-226 and A-228.|||Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-227 and A-228.|||Decreases the association with either CD247 or FCER1G. Strongly increases cell surface expression.|||Disrupts transmembrane anchoring.|||Enables membrane anchoring via glycosylphosphatidylinositol. Disrupts transmembrane anchoring.|||Enables membrane anchoring via glycosylphosphatidylinositol; disrupts transmembrane anchoring.|||Enables only transmembrane anchoring.|||Extracellular|||Has little effect on complex formation with CD247 or FCER1G.|||Has little effect on complex formation with CD247 or FCER1G. Decreases cell surface expression; when associated with A-226 and A-227.|||Has no effect on complex association with CD247 or FCER1G. Decreases cell surface expression; when associated with A-211 and A-212.|||Has no effect on complex formation with CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-211.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Impairs receptor shedding. Impairs the detachment of NK cells from opsonized target cells upon sequential activation.|||Impairs the interaction with S100A4.|||Important for receptor turnover|||In IMD20; loss of interaction with CD2.|||Loss of PKC-dependent phosphorylation. Abolishes pro-inflammatory cytokine production while enhancing cell degranulation.|||Low affinity immunoglobulin gamma Fc region receptor III-A|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC|||Phosphothreonine; by PKC|||Shows a higher binding capacity for IgG1, IgG3 and IgG4.|||Strongly decreases complex formation with CD247 or FCER1G.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015150|||http://purl.uniprot.org/annotation/PRO_5040055643|||http://purl.uniprot.org/annotation/VAR_003960|||http://purl.uniprot.org/annotation/VAR_008799|||http://purl.uniprot.org/annotation/VAR_008800|||http://purl.uniprot.org/annotation/VAR_058398|||http://purl.uniprot.org/annotation/VAR_058399|||http://purl.uniprot.org/annotation/VAR_058400
http://togogenome.org/gene/9606:GPAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNZ9|||http://purl.uniprot.org/uniprot/E9PE95|||http://purl.uniprot.org/uniprot/Q6NUI2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyltransferase|||Cytoplasmic|||Disordered|||Glycerol-3-phosphate acyltransferase 2, mitochondrial|||HXXXXD motif|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325853|||http://purl.uniprot.org/annotation/VSP_032450|||http://purl.uniprot.org/annotation/VSP_032451|||http://purl.uniprot.org/annotation/VSP_032452|||http://purl.uniprot.org/annotation/VSP_032453|||http://purl.uniprot.org/annotation/VSP_032454
http://togogenome.org/gene/9606:KIF2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PFA6|||http://purl.uniprot.org/uniprot/B0AZS5|||http://purl.uniprot.org/uniprot/O00139                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Globular|||In CDCBM3; results in abnormal cellular localization with predominant decoration of microtubules rather than diffuse punctiform cytoplasmic and nuclear distribution as observed for wild-type protein.|||In isoform 1 and isoform 2.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Kinesin motor|||Kinesin-like protein KIF2A|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125414|||http://purl.uniprot.org/annotation/VAR_070575|||http://purl.uniprot.org/annotation/VAR_070576|||http://purl.uniprot.org/annotation/VSP_028374|||http://purl.uniprot.org/annotation/VSP_028375|||http://purl.uniprot.org/annotation/VSP_028376|||http://purl.uniprot.org/annotation/VSP_047373
http://togogenome.org/gene/9606:FAM193B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPW0                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||FAM193 C-terminal|||Polar residues|||Pro residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:MKRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H000                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||E3 ubiquitin-protein ligase makorin-2|||In isoform 2.|||Makorin-type Cys-His|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055955|||http://purl.uniprot.org/annotation/VAR_052085|||http://purl.uniprot.org/annotation/VSP_055275
http://togogenome.org/gene/9606:UTP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Decreases degradation of p53/TP53.|||Disordered|||Phosphoserine|||Polar residues|||Promotes p53/TP53 degradation|||Represses p53/TP53 degradation|||U3 small nucleolar RNA-associated protein 25 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254149|||http://purl.uniprot.org/annotation/VAR_028827|||http://purl.uniprot.org/annotation/VAR_084648
http://togogenome.org/gene/9606:SHROOM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ASD1|||ASD2|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Shroom1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286061|||http://purl.uniprot.org/annotation/VAR_032061|||http://purl.uniprot.org/annotation/VSP_024962
http://togogenome.org/gene/9606:ZNF582                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NG8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Found in a patient with mild intellectual disability and eye movement disorder; unknown pathological significance.|||KRAB|||Zinc finger protein 582                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234591|||http://purl.uniprot.org/annotation/VAR_033578|||http://purl.uniprot.org/annotation/VAR_070557|||http://purl.uniprot.org/annotation/VAR_070558
http://togogenome.org/gene/9606:RDH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92781                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases androsterone dehydrogenase activity.|||Helical|||In FALBI.|||In FALBI; associated with macular dystrophy.|||In FALBI; decreased stability.|||In FALBI; decreased stability; loss of 11-cis retinol dehydrogenase activity.|||In FALBI; decreased stability; loss of 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region.|||In FALBI; loss of 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region.|||In FALBI; no effect on 11-cis retinol dehydrogenase activity; accumulates in the perinuclear region.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Retinol dehydrogenase 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054758|||http://purl.uniprot.org/annotation/VAR_009272|||http://purl.uniprot.org/annotation/VAR_009273|||http://purl.uniprot.org/annotation/VAR_009274|||http://purl.uniprot.org/annotation/VAR_016814|||http://purl.uniprot.org/annotation/VAR_016815|||http://purl.uniprot.org/annotation/VAR_016816|||http://purl.uniprot.org/annotation/VAR_016817|||http://purl.uniprot.org/annotation/VAR_016818|||http://purl.uniprot.org/annotation/VAR_016819|||http://purl.uniprot.org/annotation/VAR_016820|||http://purl.uniprot.org/annotation/VAR_016821|||http://purl.uniprot.org/annotation/VAR_016822|||http://purl.uniprot.org/annotation/VAR_016823|||http://purl.uniprot.org/annotation/VAR_052321|||http://purl.uniprot.org/annotation/VAR_052322|||http://purl.uniprot.org/annotation/VAR_068716|||http://purl.uniprot.org/annotation/VAR_068717|||http://purl.uniprot.org/annotation/VAR_068718|||http://purl.uniprot.org/annotation/VAR_068719|||http://purl.uniprot.org/annotation/VAR_075309|||http://purl.uniprot.org/annotation/VAR_081462|||http://purl.uniprot.org/annotation/VAR_081472
http://togogenome.org/gene/9606:E2F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00716                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin A/CDK2 binding|||DEF box|||Dimerization|||Disordered|||In isoform 2.|||Leucine-zipper|||Retinoblastoma protein binding|||Transactivation|||Transcription factor E2F3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219466|||http://purl.uniprot.org/annotation/VAR_014341|||http://purl.uniprot.org/annotation/VAR_014342|||http://purl.uniprot.org/annotation/VSP_045066|||http://purl.uniprot.org/annotation/VSP_045067|||http://purl.uniprot.org/annotation/VSP_045068
http://togogenome.org/gene/9606:PRR19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJB7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Proline-rich protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332273|||http://purl.uniprot.org/annotation/VSP_033371
http://togogenome.org/gene/9606:GLUD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL48|||http://purl.uniprot.org/uniprot/P00367                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ADP-ribosylcysteine|||Abolishes activation by ADP.|||Glutamate dehydrogenase 1, mitochondrial|||Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal|||In HHF6.|||In HHF6; abolishes inhibition by ATP; no effect on activation by ADP; Strongly reduces inhibition by GTP.|||In HHF6; diminished sensitivity to GTP.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces activity and inhibition by GTP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007206|||http://purl.uniprot.org/annotation/VAR_008666|||http://purl.uniprot.org/annotation/VAR_008667|||http://purl.uniprot.org/annotation/VAR_008668|||http://purl.uniprot.org/annotation/VAR_008669|||http://purl.uniprot.org/annotation/VAR_008670|||http://purl.uniprot.org/annotation/VAR_009270|||http://purl.uniprot.org/annotation/VAR_009271|||http://purl.uniprot.org/annotation/VAR_016760|||http://purl.uniprot.org/annotation/VAR_016761|||http://purl.uniprot.org/annotation/VAR_016762|||http://purl.uniprot.org/annotation/VAR_016763|||http://purl.uniprot.org/annotation/VAR_016764|||http://purl.uniprot.org/annotation/VAR_016765|||http://purl.uniprot.org/annotation/VSP_056244|||http://purl.uniprot.org/annotation/VSP_056523|||http://purl.uniprot.org/annotation/VSP_056524
http://togogenome.org/gene/9606:BTBD19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JJ37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||BTB/POZ domain-containing protein 19|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394239|||http://purl.uniprot.org/annotation/VSP_039226
http://togogenome.org/gene/9606:TSEN54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in familial late-onset hereditary ataxia; unknown pathological significance.|||In PCH2A and PCH4.|||In PCH2A.|||In PCH4.|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||tRNA-splicing endonuclease subunit Sen54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194029|||http://purl.uniprot.org/annotation/VAR_019459|||http://purl.uniprot.org/annotation/VAR_019461|||http://purl.uniprot.org/annotation/VAR_019462|||http://purl.uniprot.org/annotation/VAR_019463|||http://purl.uniprot.org/annotation/VAR_054812|||http://purl.uniprot.org/annotation/VAR_054813|||http://purl.uniprot.org/annotation/VAR_057721|||http://purl.uniprot.org/annotation/VAR_057722|||http://purl.uniprot.org/annotation/VAR_073350|||http://purl.uniprot.org/annotation/VAR_073351|||http://purl.uniprot.org/annotation/VSP_010988|||http://purl.uniprot.org/annotation/VSP_010989
http://togogenome.org/gene/9606:PRSS27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQR3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027506|||http://purl.uniprot.org/annotation/PRO_0000027507
http://togogenome.org/gene/9606:TNS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HR2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1142 and Q-1155.|||6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1142 and Q-1157.|||6-fold reduction in affinity for PtdIns(3,4,5)P3 and reduced IRS1 dephosphorylation but does not affect cell membrane localization or affinity for a tyrosine-phosphorylated peptide; when associated with Q-1155 and Q-1157.|||Basic and acidic residues|||C2 tensin-type|||Disordered|||Does not affect affinity for PtdIns(3,4,5)P3. Reduced affinity for tyrosine-phosphorylated peptide.|||Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1209 and Q-1212.|||Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1209 and Q-1214.|||Does not affect affinity for PtdIns(3,4,5)P3; when associated with Q-1212 and Q-1214.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of tyrosine-protein phosphatase activity. Reduced IRS1 degradation under catabolic conditions. Abolishes inhibition of AKT1 kinase activity. Does not affect disruption of SQSTM1-IRS1 interaction by TNS2. Reduced mTORC1 complex activation.|||Omega-N-methylarginine|||PTB|||Phorbol-ester/DAG-type|||Phosphatase tensin-type|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2|||Tensin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292987|||http://purl.uniprot.org/annotation/VAR_033043|||http://purl.uniprot.org/annotation/VAR_052547|||http://purl.uniprot.org/annotation/VSP_026457|||http://purl.uniprot.org/annotation/VSP_026458|||http://purl.uniprot.org/annotation/VSP_026460|||http://purl.uniprot.org/annotation/VSP_026461
http://togogenome.org/gene/9606:RGS17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphotyrosine|||Polar residues|||RGS|||Regulator of G-protein signaling 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204224
http://togogenome.org/gene/9606:CER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95813                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CTCK|||Cerberus|||Disordered|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006711|||http://purl.uniprot.org/annotation/VAR_021591|||http://purl.uniprot.org/annotation/VAR_021592|||http://purl.uniprot.org/annotation/VAR_021593
http://togogenome.org/gene/9606:MTCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6C9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished protein insertase activity.|||Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Hyperactive mutant with enhanced protein insertase activity.|||Mitochondrial carrier homolog 2|||Mitochondrial intermembrane|||N-acetylalanine|||Removed|||Solcar 1|||Solcar 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090637|||http://purl.uniprot.org/annotation/VAR_050128|||http://purl.uniprot.org/annotation/VAR_050129
http://togogenome.org/gene/9606:HLA-DQA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A173ADG5|||http://purl.uniprot.org/uniprot/P01909|||http://purl.uniprot.org/uniprot/Q8MH44                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DQ alpha 1 chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04 and allele DQA1*01:05.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07; requires 2 nucleotide substitutions.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*04:01 and allele DQA1*06:01.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05,allele DQA1*01:06 and allele DQA1*01:07.|||In allele DQA1*01:01, allele DQA1*01:02, allele DQA1*01:04, allele DQA1*01:05 and allele DQA1*01:07.|||In allele DQA1*01:01, allele DQA1*01:02,allele DQA1*01:03, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:06 and allele DQA1*01:07.|||In allele DQA1*01:01, allele DQA1*01:04, allele DQA1*01:05, allele DQA1*01:07, allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.|||In allele DQA1*01:02.|||In allele DQA1*01:03.|||In allele DQA1*01:04 and allele DQA1*01:05.|||In allele DQA1*01:04.|||In allele DQA1*01:06.|||In allele DQA1*01:07.|||In allele DQA1*02:01, allele DQA1*01:03, allele DQA1*06:01 and allele DQA1*06:02.|||In allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.|||In allele DQA1*02:01, allele DQA1*03:01, allele DQA1*03:02, allele DQA1*03:03, allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02.|||In allele DQA1*02:01.|||In allele DQA1*02:01; requires 2 nucleotide substitutions.|||In allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03.|||In allele DQA1*03:01, allele DQA1*03:02 and allele DQA1*03:03; requires 2 nucleotide substitutions.|||In allele DQA1*03:02 and allele DQA1*03:03.|||In allele DQA1*03:03.|||In allele DQA1*04:01, allele DQA1*04:02, allele DQA1*04:04, allele DQA1*06:01 and allele DQA1*06:02; requires 2 nucleotide substitutions.|||In allele DQA1*04:02.|||In allele DQA1*04:04.|||In allele DQA1*05:02.|||In allele DQA1*05:03, allele DQA1*05:06 and allele DQA1*05:07.|||In allele DQA1*05:04.|||In allele DQA1*05:05, allele DQA1*05:08 and allele DQA1*05:09.|||In allele DQA1*05:06.|||In allele DQA1*05:07.|||In allele DQA1*05:08.|||In allele DQA1*05:09.|||In allele DQA1*06:02.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018970|||http://purl.uniprot.org/annotation/PRO_5015052223|||http://purl.uniprot.org/annotation/VAR_014604|||http://purl.uniprot.org/annotation/VAR_033399|||http://purl.uniprot.org/annotation/VAR_033400|||http://purl.uniprot.org/annotation/VAR_033401|||http://purl.uniprot.org/annotation/VAR_033402|||http://purl.uniprot.org/annotation/VAR_033403|||http://purl.uniprot.org/annotation/VAR_033404|||http://purl.uniprot.org/annotation/VAR_033405|||http://purl.uniprot.org/annotation/VAR_033406|||http://purl.uniprot.org/annotation/VAR_033408|||http://purl.uniprot.org/annotation/VAR_033409|||http://purl.uniprot.org/annotation/VAR_033411|||http://purl.uniprot.org/annotation/VAR_033412|||http://purl.uniprot.org/annotation/VAR_033413|||http://purl.uniprot.org/annotation/VAR_050380|||http://purl.uniprot.org/annotation/VAR_050381|||http://purl.uniprot.org/annotation/VAR_050382|||http://purl.uniprot.org/annotation/VAR_050383|||http://purl.uniprot.org/annotation/VAR_050384|||http://purl.uniprot.org/annotation/VAR_050385|||http://purl.uniprot.org/annotation/VAR_050386|||http://purl.uniprot.org/annotation/VAR_050387|||http://purl.uniprot.org/annotation/VAR_050388|||http://purl.uniprot.org/annotation/VAR_060493|||http://purl.uniprot.org/annotation/VAR_060494|||http://purl.uniprot.org/annotation/VAR_060495|||http://purl.uniprot.org/annotation/VAR_060496|||http://purl.uniprot.org/annotation/VAR_060497|||http://purl.uniprot.org/annotation/VAR_060498|||http://purl.uniprot.org/annotation/VAR_060499|||http://purl.uniprot.org/annotation/VAR_060500|||http://purl.uniprot.org/annotation/VAR_060501|||http://purl.uniprot.org/annotation/VAR_060502|||http://purl.uniprot.org/annotation/VAR_060503|||http://purl.uniprot.org/annotation/VAR_060504|||http://purl.uniprot.org/annotation/VAR_060505|||http://purl.uniprot.org/annotation/VAR_060506|||http://purl.uniprot.org/annotation/VAR_060507|||http://purl.uniprot.org/annotation/VAR_060508|||http://purl.uniprot.org/annotation/VAR_060509|||http://purl.uniprot.org/annotation/VAR_060510|||http://purl.uniprot.org/annotation/VAR_060511|||http://purl.uniprot.org/annotation/VAR_060512|||http://purl.uniprot.org/annotation/VAR_060513|||http://purl.uniprot.org/annotation/VAR_060514|||http://purl.uniprot.org/annotation/VAR_060515|||http://purl.uniprot.org/annotation/VAR_060516|||http://purl.uniprot.org/annotation/VAR_060517|||http://purl.uniprot.org/annotation/VAR_060518|||http://purl.uniprot.org/annotation/VAR_060519|||http://purl.uniprot.org/annotation/VAR_060520|||http://purl.uniprot.org/annotation/VAR_060521|||http://purl.uniprot.org/annotation/VAR_060522|||http://purl.uniprot.org/annotation/VAR_060523|||http://purl.uniprot.org/annotation/VAR_060524|||http://purl.uniprot.org/annotation/VAR_060525|||http://purl.uniprot.org/annotation/VAR_060526|||http://purl.uniprot.org/annotation/VAR_060527|||http://purl.uniprot.org/annotation/VAR_060528|||http://purl.uniprot.org/annotation/VAR_060529|||http://purl.uniprot.org/annotation/VAR_060530|||http://purl.uniprot.org/annotation/VAR_060531|||http://purl.uniprot.org/annotation/VAR_060532|||http://purl.uniprot.org/annotation/VAR_060533
http://togogenome.org/gene/9606:VASP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0V4|||http://purl.uniprot.org/uniprot/P50552                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X 15 AA tandem repeats of L-[EQ]-[KR]-[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E|||Basic and acidic residues|||Disordered|||EVH2|||EVH2 block A|||EVH2 block B|||EVH2 block C|||Interferes with F-actin assembly; when associated with A-157 and A-239.|||KLKR|||Lower stability of tetramerization domain.|||N-acetylserine|||N6-acetyllysine|||No change in stability of tetramerization domain.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by PKA and PKG/PRKG1|||Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK1|||Phosphothreonine|||Phosphothreonine; by PKA, PKG/PRKG1 and AMPK|||Phosphotyrosine|||Polar residues|||Pro residues|||Promotes F-actin assembly; when associated with A-157 and A-239.|||Promotes F-actin assembly; when associated with A-157 and A-278. Interferes with F-actin assembly; when associated with A-157 and E-278.|||Promotes F-actin assembly; when associated with A-239 and A-278. Interferes with F-actin assembly; when associated with A-239 and E-278.|||Removed|||Vasodilator-stimulated phosphoprotein|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065767|||http://purl.uniprot.org/annotation/VAR_048929|||http://purl.uniprot.org/annotation/VAR_048930
http://togogenome.org/gene/9606:BRI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95415                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Membrane protein BRI3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064923|||http://purl.uniprot.org/annotation/VAR_033516|||http://purl.uniprot.org/annotation/VSP_060620|||http://purl.uniprot.org/annotation/VSP_060621
http://togogenome.org/gene/9606:PLA2R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZML4|||http://purl.uniprot.org/uniprot/Q13018                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin 1|||C-type lectin 2|||C-type lectin 3|||C-type lectin 4|||C-type lectin 5|||C-type lectin 6|||C-type lectin 7|||C-type lectin 8|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Fibronectin type-II|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Ricin B-type lectin|||Secretory phospholipase A2 receptor|||Soluble secretory phospholipase A2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311250|||http://purl.uniprot.org/annotation/PRO_5000144349|||http://purl.uniprot.org/annotation/PRO_5002866696|||http://purl.uniprot.org/annotation/VAR_037203|||http://purl.uniprot.org/annotation/VAR_037204|||http://purl.uniprot.org/annotation/VAR_037205|||http://purl.uniprot.org/annotation/VAR_037206|||http://purl.uniprot.org/annotation/VAR_037207|||http://purl.uniprot.org/annotation/VAR_037208|||http://purl.uniprot.org/annotation/VAR_037209|||http://purl.uniprot.org/annotation/VAR_061354|||http://purl.uniprot.org/annotation/VSP_029493|||http://purl.uniprot.org/annotation/VSP_029494
http://togogenome.org/gene/9606:NSUN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEA1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methylation of tRNA (Cys).|||Abolishes tRNA methyltransferase activity.|||Abolishes tRNA methyltransferase activity. Abolishes S-Adenosylmethionine binding.|||Abolishes tRNA methyltransferase activity. Does not affect S-Adenosylmethionine binding.|||Decreases substantially tRNA methyltransferase activity.|||Decreases subtantially tRNA methyltransferase activiry.|||Decreases tRNA methyltransferase activiry. Abolishes tRNA methyltransferase activiry; when associated with A-181.|||Does not impair target RNA binding. Abolishes tRNA (cytosine-5-)-methyltransferase activity.|||Dose not affect tRNA methyltransferase activity.|||Loss of S-Adenosylmethionine binding. Loss of tRNA methyltransferase activity.|||N6-acetyllysine|||Nucleophile|||PUA|||tRNA (cytosine(72)-C(5))-methyltransferase NSUN6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263114
http://togogenome.org/gene/9606:KCNH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKC0|||http://purl.uniprot.org/uniprot/B4DPJ3|||http://purl.uniprot.org/uniprot/J9JID4|||http://purl.uniprot.org/uniprot/Q9H252                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||PAC|||PAS|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 6|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054013|||http://purl.uniprot.org/annotation/VAR_053857|||http://purl.uniprot.org/annotation/VAR_053858|||http://purl.uniprot.org/annotation/VSP_000977|||http://purl.uniprot.org/annotation/VSP_000978|||http://purl.uniprot.org/annotation/VSP_000979|||http://purl.uniprot.org/annotation/VSP_000980
http://togogenome.org/gene/9606:SMARCB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12824                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X approximate tandem repeats|||DNA-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIV-1 integrase-binding|||In CSS3.|||In CSS3; patient with original diagnosis of Kleefstra syndrome; unknown pathological significance.|||In isoform B.|||Interaction with PPP1R15A|||MYC-binding|||Phosphoserine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205948|||http://purl.uniprot.org/annotation/VAR_068178|||http://purl.uniprot.org/annotation/VAR_068179|||http://purl.uniprot.org/annotation/VAR_076934|||http://purl.uniprot.org/annotation/VAR_076935|||http://purl.uniprot.org/annotation/VAR_080263|||http://purl.uniprot.org/annotation/VSP_004399
http://togogenome.org/gene/9606:NMNAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZQ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Abolished nicotinamide-nucleotide adenylyltransferase activity; abolished ability to promote mono-ADP-ribosylation of ribosomes.|||In isoform 2.|||Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2|||Reduces activity by 95%.|||S-palmitoyl cysteine|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135014|||http://purl.uniprot.org/annotation/VSP_015571
http://togogenome.org/gene/9606:STX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJX9|||http://purl.uniprot.org/uniprot/O14662                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 6.|||In isoform A.|||In isoform C and isoform D.|||In isoform C.|||In isoform E.|||Phosphoserine|||Syntaxin-16|||T-SNARE coiled-coil homology|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210226|||http://purl.uniprot.org/annotation/VSP_006348|||http://purl.uniprot.org/annotation/VSP_006349|||http://purl.uniprot.org/annotation/VSP_006350|||http://purl.uniprot.org/annotation/VSP_006351|||http://purl.uniprot.org/annotation/VSP_043849|||http://purl.uniprot.org/annotation/VSP_045073
http://togogenome.org/gene/9606:QPRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDH4|||http://purl.uniprot.org/uniprot/Q15274|||http://purl.uniprot.org/uniprot/V9HWJ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Forms dimers instead of hexamers.|||Important for hexamer formation|||Loss of activity.|||Nicotinate-nucleotide pyrophosphorylase [carboxylating]|||No effect on hexamer formation.|||Quinolinate phosphoribosyl transferase C-terminal|||Quinolinate phosphoribosyl transferase N-terminal|||Reduced activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155954|||http://purl.uniprot.org/annotation/PRO_5014314728|||http://purl.uniprot.org/annotation/VAR_021915|||http://purl.uniprot.org/annotation/VAR_050219
http://togogenome.org/gene/9606:ARL13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T892|||http://purl.uniprot.org/uniprot/Q3SXY8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 13B|||Abolishes sumoylation. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-276 and R-279.|||Basic and acidic residues|||Disordered|||Does not affect localization to cilia.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In JBTS8.|||In JBTS8; reduces binding to GTP.|||In JBTS8; the patient also manifests obesity as a feature; decreased localization to cilium.|||In a nephronophthisis (NPHP) patient.|||In isoform 2.|||In isoform 3.|||No effect. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-276 and R-329.|||No effect. Abolishes sumoylation; when associated with R-231; R-270; R-275; R-279 and R-329.|||No effect. Abolishes sumoylation; when associated with R-231; R-270; R-276; R-279 and R-329.|||No effect. Abolishes sumoylation; when associated with R-231; R-275; R-276; R-279 and R-329.|||No effect. Abolishes sumoylation; when associated with R-270; R-275; R-276; R-279 and R-329.|||Pro residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251137|||http://purl.uniprot.org/annotation/VAR_048319|||http://purl.uniprot.org/annotation/VAR_054371|||http://purl.uniprot.org/annotation/VAR_054372|||http://purl.uniprot.org/annotation/VAR_069190|||http://purl.uniprot.org/annotation/VAR_077496|||http://purl.uniprot.org/annotation/VSP_020733|||http://purl.uniprot.org/annotation/VSP_045421
http://togogenome.org/gene/9606:KCNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUL8|||http://purl.uniprot.org/uniprot/Q96KK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BTB|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Polar residues|||Potassium voltage-gated channel subfamily S member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054081|||http://purl.uniprot.org/annotation/VAR_020052|||http://purl.uniprot.org/annotation/VAR_053867
http://togogenome.org/gene/9606:EZH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8E9|||http://purl.uniprot.org/uniprot/Q15910|||http://purl.uniprot.org/uniprot/S4S3R8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates methyltransferase activity.|||Acidic residues|||Basic and acidic residues|||CXC|||Decreased histone methyltransferase activity.|||Disordered|||Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1.|||Found in a patient with B-cell lymphoma; increased hypertrimethylation of H3K27; changed substrate preferences; confers biochemical activity independent of H3K27 methylation state.|||Found in a patient with chronic myelomonocytic leukemia; somatic mutation; loss of histone methyltransferase activity.|||Found in a patient with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2.|||Found in a patient with myelodysplastic syndrome and myelodysplastic-myeloproliferative neoplasms; somatic mutation; loss of histone methyltransferase activity.|||Found in a patient with myeloid disorders; somatic mutation; loss of histone methyltransferase activity.|||Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation.|||Found in patients with follicular lymphoma; also in diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase EZH2|||Impaired CDK1- and CDK-2 mediated phosphorylation and subsequent gene silencing. Altered EZH2-mediated cell proliferation and migration.|||In WVS.|||In WVS; decreased histone methyltransferase activity.|||In WVS; unknown pathological significance.|||In a patient with chronic myelomonocytic leukemia.|||In a patient with diffuse large B-cell lymphoma; somatic mutation; changed substrate preferences; prefers substrates with greater methylation H3K27me0<me1<me2.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Interaction with CDYL|||Interaction with DNMT1, DNMT3A and DNMT3B|||Interaction with EED|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphothreonine; by CDK1 and CDK2|||Polar residues|||Reduced protein stability.|||Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1.|||SET|||Strongly decreases histone methyltransferase activity.|||Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213992|||http://purl.uniprot.org/annotation/VAR_055795|||http://purl.uniprot.org/annotation/VAR_067228|||http://purl.uniprot.org/annotation/VAR_067229|||http://purl.uniprot.org/annotation/VAR_067230|||http://purl.uniprot.org/annotation/VAR_067231|||http://purl.uniprot.org/annotation/VAR_067232|||http://purl.uniprot.org/annotation/VAR_067233|||http://purl.uniprot.org/annotation/VAR_067595|||http://purl.uniprot.org/annotation/VAR_067596|||http://purl.uniprot.org/annotation/VAR_067597|||http://purl.uniprot.org/annotation/VAR_078320|||http://purl.uniprot.org/annotation/VAR_078321|||http://purl.uniprot.org/annotation/VAR_078322|||http://purl.uniprot.org/annotation/VAR_078323|||http://purl.uniprot.org/annotation/VAR_078324|||http://purl.uniprot.org/annotation/VAR_078325|||http://purl.uniprot.org/annotation/VAR_078326|||http://purl.uniprot.org/annotation/VAR_078327|||http://purl.uniprot.org/annotation/VAR_078328|||http://purl.uniprot.org/annotation/VAR_078329|||http://purl.uniprot.org/annotation/VAR_078330|||http://purl.uniprot.org/annotation/VAR_078331|||http://purl.uniprot.org/annotation/VAR_078332|||http://purl.uniprot.org/annotation/VAR_078333|||http://purl.uniprot.org/annotation/VAR_078334|||http://purl.uniprot.org/annotation/VAR_078335|||http://purl.uniprot.org/annotation/VSP_038813|||http://purl.uniprot.org/annotation/VSP_038814|||http://purl.uniprot.org/annotation/VSP_038815|||http://purl.uniprot.org/annotation/VSP_038816
http://togogenome.org/gene/9606:MAIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||m-AAA protease-interacting protein 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301945|||http://purl.uniprot.org/annotation/VAR_034911
http://togogenome.org/gene/9606:TACR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21452                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Substance-K receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069893|||http://purl.uniprot.org/annotation/VAR_014680|||http://purl.uniprot.org/annotation/VAR_016159|||http://purl.uniprot.org/annotation/VAR_061221|||http://purl.uniprot.org/annotation/VAR_061222|||http://purl.uniprot.org/annotation/VAR_061223|||http://purl.uniprot.org/annotation/VAR_061224
http://togogenome.org/gene/9606:CZIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWV4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  CXXC motif containing zinc binding protein|||Disrupts protein folding and solubility; when associated with A-33; A-36 and A-67.|||Disrupts protein folding and solubility; when associated with A-33; A-36 and A-70.|||Disrupts protein folding and solubility; when associated with A-33; A-67 and A-70.|||Disrupts protein folding and solubility; when associated with A-36; A-67 and A-70.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264151
http://togogenome.org/gene/9606:LRSAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWE0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with TSG101.|||Abolishes ubiquitination of TSG101.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase LRSAM1|||In CMT2P; abolishes interaction with FUS.|||In CMT2P; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||PTAP motif 1|||PTAP motif 2|||Phosphoserine|||RING-type|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055923|||http://purl.uniprot.org/annotation/VAR_021051|||http://purl.uniprot.org/annotation/VAR_077460|||http://purl.uniprot.org/annotation/VAR_077461|||http://purl.uniprot.org/annotation/VSP_012660|||http://purl.uniprot.org/annotation/VSP_012661
http://togogenome.org/gene/9606:GDF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXG3|||http://purl.uniprot.org/uniprot/O60383                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found at higher frequency in mothers of dizygotic twins than in controls.|||Growth/differentiation factor 9|||In POF14; unknown pathological significance.|||In POF14; unknown pathological significance; also found at higher frequency in mothers of dizygotic twins than in controls.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CK|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033980|||http://purl.uniprot.org/annotation/PRO_0000033981|||http://purl.uniprot.org/annotation/VAR_058945|||http://purl.uniprot.org/annotation/VAR_058946|||http://purl.uniprot.org/annotation/VAR_058947|||http://purl.uniprot.org/annotation/VAR_066934|||http://purl.uniprot.org/annotation/VAR_066935|||http://purl.uniprot.org/annotation/VAR_066936|||http://purl.uniprot.org/annotation/VAR_066937|||http://purl.uniprot.org/annotation/VAR_066938|||http://purl.uniprot.org/annotation/VAR_066939|||http://purl.uniprot.org/annotation/VAR_066940|||http://purl.uniprot.org/annotation/VAR_066941
http://togogenome.org/gene/9606:RUSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-4 complex accessory subunit RUSC2|||Acidic residues|||Basic and acidic residues|||Disordered|||In MRT61; unknown pathological significance.|||Phosphoserine|||Polar residues|||RUN|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097534|||http://purl.uniprot.org/annotation/VAR_034653|||http://purl.uniprot.org/annotation/VAR_034654|||http://purl.uniprot.org/annotation/VAR_080461|||http://purl.uniprot.org/annotation/VAR_080462
http://togogenome.org/gene/9606:OR6T1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGN1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6T1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150638|||http://purl.uniprot.org/annotation/VAR_048049|||http://purl.uniprot.org/annotation/VAR_048050|||http://purl.uniprot.org/annotation/VAR_048051
http://togogenome.org/gene/9606:ZAR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NP61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Basic and acidic residues|||Disordered|||Protein ZAR1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332227
http://togogenome.org/gene/9606:COMMD3-BMI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35226|||http://purl.uniprot.org/uniprot/R4GMX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-174.|||Disordered|||Increases stimulation of RNF2 ubiquitin ligase activity; when associated with E-77.|||Increases stimulation of RNF2 ubiquitin ligase activity; when associated with N-73.|||Interaction with E4F1|||Interaction with PHC2|||Mildly decreases histone H2A ubiquitination. Strongly decreases histone H2A ubiquitination; when associated with A-62.|||Nuclear localization signal|||Polar residues|||Polycomb complex protein BMI-1|||RING-type|||Strongly decreases affinity for PHC2.|||Strongly decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-165.|||Strongly decreases histone H2A ubiquitination; when associated with A-64.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055987|||http://purl.uniprot.org/annotation/VAR_052087
http://togogenome.org/gene/9606:TRPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4N2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes inhibition by zinc allowing zinc ion influx.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CSNB1C.|||In a patient with night blindness started in the third decade; associated in cis with G-1438.|||In a patient with night blindness started in the third decade; associated in cis with T-962.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Reduces inhibition by zinc allowing zinc ion influx.|||Transient receptor potential cation channel subfamily M member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328930|||http://purl.uniprot.org/annotation/VAR_052370|||http://purl.uniprot.org/annotation/VAR_052371|||http://purl.uniprot.org/annotation/VAR_052372|||http://purl.uniprot.org/annotation/VAR_052373|||http://purl.uniprot.org/annotation/VAR_052374|||http://purl.uniprot.org/annotation/VAR_052375|||http://purl.uniprot.org/annotation/VAR_052376|||http://purl.uniprot.org/annotation/VAR_063173|||http://purl.uniprot.org/annotation/VAR_063174|||http://purl.uniprot.org/annotation/VAR_063175|||http://purl.uniprot.org/annotation/VAR_063176|||http://purl.uniprot.org/annotation/VAR_063177|||http://purl.uniprot.org/annotation/VAR_063178|||http://purl.uniprot.org/annotation/VAR_063179|||http://purl.uniprot.org/annotation/VAR_063180|||http://purl.uniprot.org/annotation/VAR_063181|||http://purl.uniprot.org/annotation/VAR_063182|||http://purl.uniprot.org/annotation/VAR_063183|||http://purl.uniprot.org/annotation/VAR_063184|||http://purl.uniprot.org/annotation/VAR_063185|||http://purl.uniprot.org/annotation/VAR_063186|||http://purl.uniprot.org/annotation/VAR_063187|||http://purl.uniprot.org/annotation/VAR_063188|||http://purl.uniprot.org/annotation/VAR_063189|||http://purl.uniprot.org/annotation/VAR_063190|||http://purl.uniprot.org/annotation/VAR_063191|||http://purl.uniprot.org/annotation/VSP_046786|||http://purl.uniprot.org/annotation/VSP_046787|||http://purl.uniprot.org/annotation/VSP_046788|||http://purl.uniprot.org/annotation/VSP_046789|||http://purl.uniprot.org/annotation/VSP_052748|||http://purl.uniprot.org/annotation/VSP_052749|||http://purl.uniprot.org/annotation/VSP_052750
http://togogenome.org/gene/9606:ASPM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWI2|||http://purl.uniprot.org/uniprot/Q8IZT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abnormal spindle-like microcephaly-associated protein|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||IQ 1|||IQ 10|||IQ 11|||IQ 12|||IQ 13|||IQ 14|||IQ 15|||IQ 16|||IQ 17|||IQ 18|||IQ 19|||IQ 2|||IQ 20|||IQ 21|||IQ 22|||IQ 23|||IQ 24|||IQ 25|||IQ 26|||IQ 27|||IQ 28|||IQ 29|||IQ 3|||IQ 30|||IQ 31|||IQ 32|||IQ 33|||IQ 34|||IQ 35|||IQ 36|||IQ 37|||IQ 38|||IQ 39|||IQ 4|||IQ 5|||IQ 6|||IQ 7|||IQ 8|||IQ 9|||In isoform 2.|||Phosphoserine|||Polar residues|||Sufficient for interaction with KATNA1:KATNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191332|||http://purl.uniprot.org/annotation/VAR_019084|||http://purl.uniprot.org/annotation/VAR_019085|||http://purl.uniprot.org/annotation/VAR_019086|||http://purl.uniprot.org/annotation/VAR_024369|||http://purl.uniprot.org/annotation/VAR_046758|||http://purl.uniprot.org/annotation/VAR_046759|||http://purl.uniprot.org/annotation/VAR_046760|||http://purl.uniprot.org/annotation/VAR_046761|||http://purl.uniprot.org/annotation/VAR_046762|||http://purl.uniprot.org/annotation/VAR_047263|||http://purl.uniprot.org/annotation/VAR_071930|||http://purl.uniprot.org/annotation/VAR_071931|||http://purl.uniprot.org/annotation/VSP_010680
http://togogenome.org/gene/9606:DDX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NKM7|||http://purl.uniprot.org/uniprot/Q96FC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent DNA helicase DDX11|||DEAH box|||Disordered|||Helicase ATP-binding|||In WBRS; impairs the helicase activity by perturbing its DNA binding and DNA-dependent ATPase activity; reduces binding to rDNA promoter and promotion of rDNA transcription.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of both DNA-dependent ATPase and ATP-dependent helicase activities.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055136|||http://purl.uniprot.org/annotation/VAR_024808|||http://purl.uniprot.org/annotation/VAR_024809|||http://purl.uniprot.org/annotation/VAR_024810|||http://purl.uniprot.org/annotation/VAR_052175|||http://purl.uniprot.org/annotation/VAR_052176|||http://purl.uniprot.org/annotation/VAR_052177|||http://purl.uniprot.org/annotation/VAR_052178|||http://purl.uniprot.org/annotation/VAR_069099|||http://purl.uniprot.org/annotation/VSP_016860|||http://purl.uniprot.org/annotation/VSP_016861|||http://purl.uniprot.org/annotation/VSP_016862|||http://purl.uniprot.org/annotation/VSP_016863|||http://purl.uniprot.org/annotation/VSP_016864|||http://purl.uniprot.org/annotation/VSP_016865
http://togogenome.org/gene/9606:KRT80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6KB66                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||In isoform 3.|||Keratin, type II cytoskeletal 80|||Linker 1|||Linker 12|||Phosphoserine|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314896|||http://purl.uniprot.org/annotation/VAR_049807|||http://purl.uniprot.org/annotation/VSP_030421|||http://purl.uniprot.org/annotation/VSP_030422|||http://purl.uniprot.org/annotation/VSP_030423
http://togogenome.org/gene/9606:NBEA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXQ8|||http://purl.uniprot.org/uniprot/Q8NFP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Disordered|||In NEDEGE.|||In NEDEGE; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Neurobeachin|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051089|||http://purl.uniprot.org/annotation/PRO_5002790421|||http://purl.uniprot.org/annotation/VAR_047658|||http://purl.uniprot.org/annotation/VAR_047659|||http://purl.uniprot.org/annotation/VAR_085275|||http://purl.uniprot.org/annotation/VAR_085276|||http://purl.uniprot.org/annotation/VAR_085278|||http://purl.uniprot.org/annotation/VAR_085279|||http://purl.uniprot.org/annotation/VAR_085280|||http://purl.uniprot.org/annotation/VAR_085281|||http://purl.uniprot.org/annotation/VAR_085282|||http://purl.uniprot.org/annotation/VAR_085283|||http://purl.uniprot.org/annotation/VAR_085284|||http://purl.uniprot.org/annotation/VAR_085285|||http://purl.uniprot.org/annotation/VAR_085286|||http://purl.uniprot.org/annotation/VAR_085366|||http://purl.uniprot.org/annotation/VSP_046397|||http://purl.uniprot.org/annotation/VSP_050538|||http://purl.uniprot.org/annotation/VSP_050539
http://togogenome.org/gene/9606:ICAM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14773|||http://purl.uniprot.org/uniprot/U5U6P8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In LW(B).|||In isoform 3.|||In isoform Short.|||Intercellular adhesion molecule 4|||Intercellular adhesion molecule N-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014796|||http://purl.uniprot.org/annotation/PRO_5014314237|||http://purl.uniprot.org/annotation/VAR_003912|||http://purl.uniprot.org/annotation/VAR_038721|||http://purl.uniprot.org/annotation/VSP_002519|||http://purl.uniprot.org/annotation/VSP_043229
http://togogenome.org/gene/9606:ZNF695                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW36                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; atypical|||C2H2-type 2; degenerate|||C2H2-type 3; atypical|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 1.|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 695                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233282|||http://purl.uniprot.org/annotation/VAR_057446|||http://purl.uniprot.org/annotation/VAR_057447|||http://purl.uniprot.org/annotation/VAR_061963|||http://purl.uniprot.org/annotation/VSP_018106|||http://purl.uniprot.org/annotation/VSP_018107|||http://purl.uniprot.org/annotation/VSP_018108|||http://purl.uniprot.org/annotation/VSP_018109|||http://purl.uniprot.org/annotation/VSP_038548|||http://purl.uniprot.org/annotation/VSP_038549
http://togogenome.org/gene/9606:DIABLO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBT2|||http://purl.uniprot.org/uniprot/A0A0S2Z5P6|||http://purl.uniprot.org/uniprot/A0A0S2Z5U7|||http://purl.uniprot.org/uniprot/K7X1S0|||http://purl.uniprot.org/uniprot/Q502X2|||http://purl.uniprot.org/uniprot/Q9NR28                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by PARL|||Diablo IAP-binding mitochondrial protein|||Diablo IAP-binding mitochondrial protein, cleaved form|||Disordered|||Helical|||IAP-binding|||In DFNA64; does not increase apoptotic activity compared to wild-type; enhances the degradation of mutant and wild-type protein via heterodimerization; cells expressing the mutant protein show increased susceptibility to calcium-induced loss of mitochondrial potential compared to wild-type, indicating increased sensitivity to mitochondrial stress and suggestive of mitochondrial dysfunction.|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021072|||http://purl.uniprot.org/annotation/PRO_0000458409|||http://purl.uniprot.org/annotation/VAR_066487|||http://purl.uniprot.org/annotation/VSP_004397|||http://purl.uniprot.org/annotation/VSP_042785
http://togogenome.org/gene/9606:TFAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01664                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper 1|||Leucine-zipper 2|||Phosphoserine|||Transcription factor AP-4|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127458|||http://purl.uniprot.org/annotation/VAR_059346
http://togogenome.org/gene/9606:THAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0W7                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  HCFC1-binding motif (HBM)|||THAP domain-containing protein 2|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068642|||http://purl.uniprot.org/annotation/VAR_034551
http://togogenome.org/gene/9606:CSTF2T                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0L4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1-1|||1-2; approximate|||1-3; approximate|||1-4; approximate|||1-5; approximate|||1-6|||1-7; approximate|||1-8; approximate|||1-9; approximate|||2-1|||2-2|||2-3|||2-4|||2-5; approximate|||2-6|||2-7; approximate|||2-8; approximate|||2-9; approximate|||9 X 5 AA tandem repeats of G-[AT]-G-[MI]-Q|||9 X 5 AA tandem repeats of M-E-T-R-[AG]|||Cleavage stimulation factor subunit 2 tau variant|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081534
http://togogenome.org/gene/9606:VIPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41587|||http://purl.uniprot.org/uniprot/X5D7Q6|||http://purl.uniprot.org/uniprot/X5DP12                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Vasoactive intestinal polypeptide receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012860|||http://purl.uniprot.org/annotation/PRO_5004953877|||http://purl.uniprot.org/annotation/PRO_5004955936|||http://purl.uniprot.org/annotation/VAR_011811|||http://purl.uniprot.org/annotation/VAR_011812|||http://purl.uniprot.org/annotation/VSP_056684|||http://purl.uniprot.org/annotation/VSP_056685
http://togogenome.org/gene/9606:OR1F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43749                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150431|||http://purl.uniprot.org/annotation/VAR_024086|||http://purl.uniprot.org/annotation/VAR_053121
http://togogenome.org/gene/9606:SPATA31F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY95|||http://purl.uniprot.org/uniprot/Q6ZU69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Protein SPATA31F1|||SPATA31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308581
http://togogenome.org/gene/9606:CCDC110                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EUS2|||http://purl.uniprot.org/uniprot/Q8TBZ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 110|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249076|||http://purl.uniprot.org/annotation/VAR_050729|||http://purl.uniprot.org/annotation/VAR_050730|||http://purl.uniprot.org/annotation/VAR_050731|||http://purl.uniprot.org/annotation/VAR_050732|||http://purl.uniprot.org/annotation/VAR_050733|||http://purl.uniprot.org/annotation/VAR_050734|||http://purl.uniprot.org/annotation/VAR_050735|||http://purl.uniprot.org/annotation/VAR_050736|||http://purl.uniprot.org/annotation/VAR_061577|||http://purl.uniprot.org/annotation/VSP_020365
http://togogenome.org/gene/9606:GPR143                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51810                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Delivered to both at the cell surface and in vesicles of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells; when associated with 329-A-A-330.|||Disordered|||Extracellular|||G-protein coupled receptor 143|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In NYS6.|||In OA1.|||In OA1; abnormal distribution of melanosomes; Not delivered at the cell surface of melanocytic and non-melanocytic cells.|||In OA1; not delivered at the cell surface of melanocytic and non-melanocytic cells.|||In OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum.|||In OA1; results in altered glycosylation pattern and subcellular localization consistent with protein retention in the endoplasmic reticulum; lacks G protein-activation abilities.|||Mostly delivered at the cell surface of melanocytic and non-melanocytic cells. Strongly delivered at the cell surface of melanocytic and non-melanocytic cells; when associated with 224-A-A-225.|||N-linked (GlcNAc...) asparagine|||Necessary for its G protein-activation ability and normal distribution of melanosomes|||Polar residues|||lysosomal/melanosomal membrane localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195086|||http://purl.uniprot.org/annotation/VAR_005507|||http://purl.uniprot.org/annotation/VAR_005508|||http://purl.uniprot.org/annotation/VAR_005509|||http://purl.uniprot.org/annotation/VAR_005510|||http://purl.uniprot.org/annotation/VAR_005511|||http://purl.uniprot.org/annotation/VAR_005513|||http://purl.uniprot.org/annotation/VAR_005514|||http://purl.uniprot.org/annotation/VAR_005515|||http://purl.uniprot.org/annotation/VAR_005516|||http://purl.uniprot.org/annotation/VAR_005517|||http://purl.uniprot.org/annotation/VAR_005518|||http://purl.uniprot.org/annotation/VAR_005519|||http://purl.uniprot.org/annotation/VAR_005520|||http://purl.uniprot.org/annotation/VAR_018130|||http://purl.uniprot.org/annotation/VAR_018131|||http://purl.uniprot.org/annotation/VAR_018132|||http://purl.uniprot.org/annotation/VAR_018133|||http://purl.uniprot.org/annotation/VAR_018134|||http://purl.uniprot.org/annotation/VAR_018135|||http://purl.uniprot.org/annotation/VAR_018136|||http://purl.uniprot.org/annotation/VAR_018137|||http://purl.uniprot.org/annotation/VAR_018138|||http://purl.uniprot.org/annotation/VAR_018139|||http://purl.uniprot.org/annotation/VAR_018140|||http://purl.uniprot.org/annotation/VAR_018141|||http://purl.uniprot.org/annotation/VAR_063264|||http://purl.uniprot.org/annotation/VAR_063265|||http://purl.uniprot.org/annotation/VAR_063266|||http://purl.uniprot.org/annotation/VAR_063267|||http://purl.uniprot.org/annotation/VAR_063268|||http://purl.uniprot.org/annotation/VAR_063269|||http://purl.uniprot.org/annotation/VAR_063270|||http://purl.uniprot.org/annotation/VAR_063271|||http://purl.uniprot.org/annotation/VAR_063272|||http://purl.uniprot.org/annotation/VAR_063273|||http://purl.uniprot.org/annotation/VAR_063274
http://togogenome.org/gene/9606:TMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||Transmembrane channel-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185382|||http://purl.uniprot.org/annotation/VAR_023360|||http://purl.uniprot.org/annotation/VAR_030621|||http://purl.uniprot.org/annotation/VAR_030622|||http://purl.uniprot.org/annotation/VAR_057281|||http://purl.uniprot.org/annotation/VAR_057282|||http://purl.uniprot.org/annotation/VAR_057283|||http://purl.uniprot.org/annotation/VAR_057284|||http://purl.uniprot.org/annotation/VSP_015279|||http://purl.uniprot.org/annotation/VSP_015281|||http://purl.uniprot.org/annotation/VSP_015282|||http://purl.uniprot.org/annotation/VSP_015283|||http://purl.uniprot.org/annotation/VSP_015284
http://togogenome.org/gene/9606:SH3GLB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW40|||http://purl.uniprot.org/uniprot/A0A140VJU5|||http://purl.uniprot.org/uniprot/Q9Y371                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with BAX.|||BAR|||Endophilin-B1|||In isoform 2.|||In isoform 3.|||Membrane-binding amphipathic helix|||N-acetylmethionine|||Phosphothreonine; by CDK5|||Reduced CDK5-mediated phosphorylation and impaired dimerization.|||Required for membrane binding|||SH3|||Spontaneous dimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146753|||http://purl.uniprot.org/annotation/VSP_009276|||http://purl.uniprot.org/annotation/VSP_044895
http://togogenome.org/gene/9606:TRPV4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBA0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Associated with lower sodium concentrations in serum; shows diminished response to hypotonic stress relative to wild-type.|||Cytoplasmic|||Decreased ATP-binding.|||Disordered|||Extracellular|||Found in a patient with spondyloepiphyseal dysplasia Maroteaux type.|||Found in a patient with spondyloepiphyseal dysplasia Maroteaux type; decreased protein stability; increased ATP-binding.|||Helical|||In BCYM3; results in a gain of function and a constitutive activation of the channel.|||In CMT2C and SPSMA; decreased protein stability; decreased ATP-binding.|||In CMT2C.|||In CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; decreases protein stability; causes increased cell death.|||In CMT2C; increased agonist-induced channel activity; causes increased cell death; no effect on protein stability and ATP-binding.|||In CMT2C; increased basal and agonist-induced channel activity, decreased protein stability; decreased ATP-binding; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death.|||In FDAB; poorly expressed on the cell surface; mutant channels show a significantly reduced response to agonists.|||In HMN8 and CMT2C; does not affect channel localization to plasma membrane; results in increased agonist-induced channel activity and increased basal intracellular calcium concentration; decreases ATP-binding; no effect on protein stability; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death.|||In HMN8 and CMT2C; increased agonist-induced channel activity and increased basal intracellular calcium concentration; slightly decreased protein stability and ATP-binding; decreases binding to membranes enriched in phosphatidylinositol-2,4-bisphosphate; causes increased cell death.|||In HMN8; loss of function mutation.|||In MTD and SMDK; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type.|||In MTD.|||In MTD; also found in a patient with spondyloepiphyseal dysplasia Maroteaux type.|||In MTD; decreased protein stability.|||In MTD; decreased protein stability; decreased ATP-binding.|||In MTD; decreased protein stability; no effect on ATP-binding.|||In MTD; impairs protein folding or stability.|||In MTD; lethal form.|||In MTD; lethal form; decreased protein stability; reduced ATP-binding.|||In MTD; no effect on protein stability; no effect on ATP-binding.|||In SMDK and PSTD.|||In SMDK.|||In SMDK; decreased protein stability; no effect on ATP-binding.|||In SMDK; slightly increased ATP-binding; slightly decreased protein stability.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||Interaction with calmodulin and ITPR3|||Loss of Ca(2+) dependent current potentiation.|||Loss of Ca(2+) influx. Loss of DDX3X translocation to the nucleus.|||Loss of calmodulin binding.|||Loss of calmodulin binding; when associated with 816-ELEEDE-821.|||Loss of calmodulin binding; when associated with A-828.|||Loss of interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate; when associated with P-299.|||No effect on channel activity. No effect on interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate.|||Phosphoserine|||Phosphotyrosine|||Pore-forming|||Selectivity filter|||Strongly decreased interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate. Loss of interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate; when associated with D-296.|||Transient receptor potential cation channel subfamily V member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215347|||http://purl.uniprot.org/annotation/VAR_052391|||http://purl.uniprot.org/annotation/VAR_054805|||http://purl.uniprot.org/annotation/VAR_054806|||http://purl.uniprot.org/annotation/VAR_062331|||http://purl.uniprot.org/annotation/VAR_062332|||http://purl.uniprot.org/annotation/VAR_062333|||http://purl.uniprot.org/annotation/VAR_062334|||http://purl.uniprot.org/annotation/VAR_062335|||http://purl.uniprot.org/annotation/VAR_063528|||http://purl.uniprot.org/annotation/VAR_063529|||http://purl.uniprot.org/annotation/VAR_063530|||http://purl.uniprot.org/annotation/VAR_063541|||http://purl.uniprot.org/annotation/VAR_064517|||http://purl.uniprot.org/annotation/VAR_064518|||http://purl.uniprot.org/annotation/VAR_064519|||http://purl.uniprot.org/annotation/VAR_064520|||http://purl.uniprot.org/annotation/VAR_064521|||http://purl.uniprot.org/annotation/VAR_064522|||http://purl.uniprot.org/annotation/VAR_064523|||http://purl.uniprot.org/annotation/VAR_064524|||http://purl.uniprot.org/annotation/VAR_064525|||http://purl.uniprot.org/annotation/VAR_064526|||http://purl.uniprot.org/annotation/VAR_064527|||http://purl.uniprot.org/annotation/VAR_064528|||http://purl.uniprot.org/annotation/VAR_064529|||http://purl.uniprot.org/annotation/VAR_064530|||http://purl.uniprot.org/annotation/VAR_064531|||http://purl.uniprot.org/annotation/VAR_064532|||http://purl.uniprot.org/annotation/VAR_064533|||http://purl.uniprot.org/annotation/VAR_064534|||http://purl.uniprot.org/annotation/VAR_064535|||http://purl.uniprot.org/annotation/VAR_064536|||http://purl.uniprot.org/annotation/VAR_064537|||http://purl.uniprot.org/annotation/VAR_064538|||http://purl.uniprot.org/annotation/VAR_064539|||http://purl.uniprot.org/annotation/VAR_064540|||http://purl.uniprot.org/annotation/VAR_067989|||http://purl.uniprot.org/annotation/VAR_067990|||http://purl.uniprot.org/annotation/VAR_067991|||http://purl.uniprot.org/annotation/VAR_067992|||http://purl.uniprot.org/annotation/VAR_067993|||http://purl.uniprot.org/annotation/VAR_068498|||http://purl.uniprot.org/annotation/VAR_068499|||http://purl.uniprot.org/annotation/VAR_068500|||http://purl.uniprot.org/annotation/VSP_013436|||http://purl.uniprot.org/annotation/VSP_013437|||http://purl.uniprot.org/annotation/VSP_026614|||http://purl.uniprot.org/annotation/VSP_026615
http://togogenome.org/gene/9606:CD1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A669KB34|||http://purl.uniprot.org/uniprot/P15813                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Antigen-presenting glycoprotein CD1d|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Internalization signal|||MHC class I-like antigen recognition-like|||N-linked (GlcNAc...) asparagine|||Strongly reduced internalization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014581|||http://purl.uniprot.org/annotation/PRO_5025611268|||http://purl.uniprot.org/annotation/VAR_010211
http://togogenome.org/gene/9606:KRT40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6A162                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cytoskeletal 40|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314857|||http://purl.uniprot.org/annotation/VAR_038078|||http://purl.uniprot.org/annotation/VAR_038079|||http://purl.uniprot.org/annotation/VAR_038080|||http://purl.uniprot.org/annotation/VAR_038081|||http://purl.uniprot.org/annotation/VAR_049787|||http://purl.uniprot.org/annotation/VAR_049788|||http://purl.uniprot.org/annotation/VAR_049789|||http://purl.uniprot.org/annotation/VAR_049790|||http://purl.uniprot.org/annotation/VAR_049791
http://togogenome.org/gene/9606:FBXO30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB52                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 30|||In a colorectal cancer sample; somatic mutation.|||TRAF-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119918|||http://purl.uniprot.org/annotation/VAR_020410|||http://purl.uniprot.org/annotation/VAR_024443|||http://purl.uniprot.org/annotation/VAR_036072|||http://purl.uniprot.org/annotation/VAR_049044
http://togogenome.org/gene/9606:PPFIBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDSMBA.|||In NEDSMBA; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Liprin-beta-1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191034|||http://purl.uniprot.org/annotation/VAR_017758|||http://purl.uniprot.org/annotation/VAR_087715|||http://purl.uniprot.org/annotation/VAR_087716|||http://purl.uniprot.org/annotation/VAR_087717|||http://purl.uniprot.org/annotation/VAR_087718|||http://purl.uniprot.org/annotation/VAR_087719|||http://purl.uniprot.org/annotation/VAR_087720|||http://purl.uniprot.org/annotation/VSP_009394|||http://purl.uniprot.org/annotation/VSP_009395|||http://purl.uniprot.org/annotation/VSP_009396|||http://purl.uniprot.org/annotation/VSP_009397|||http://purl.uniprot.org/annotation/VSP_009398|||http://purl.uniprot.org/annotation/VSP_009399|||http://purl.uniprot.org/annotation/VSP_009400
http://togogenome.org/gene/9606:NFE2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TN14|||http://purl.uniprot.org/uniprot/A0A8V8TPA8|||http://purl.uniprot.org/uniprot/Q16236                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with KEAP1.|||BZIP|||Basic and acidic residues|||Basic motif|||DLG motif|||Disordered|||ETGE motif|||In IMDDHH.|||In IMDDHH; increased protein abundance; increased positive regulation of transcription of target genes; changed cell redox homeostasis.|||In isoform 2 and isoform 3.|||In isoform 3.|||Leucine-zipper|||Loss of function; when associated with A-462; A-472; A-487; A-499 and A-569.|||Loss of function; when associated with A-462; A-472; A-487; A-499 and A-587.|||Loss of function; when associated with A-462; A-472; A-487; A-569 and A-587.|||Loss of function; when associated with A-462; A-472; A-499; A-569 and A-587.|||Loss of function; when associated with A-462; A-487; A-499; A-569 and A-587.|||Loss of function; when associated with A-472; A-487; A-499; A-569 and A-587.|||Loss of interaction with KEAP1.|||Mediates interaction with CHD6 and is necessary to activate transcription|||N-linked (Glc) (glycation) arginine|||N-linked (Glc) (glycation) lysine|||N6-acetyllysine; by CREBBP|||Nuclear factor erythroid 2-related factor 2|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076449|||http://purl.uniprot.org/annotation/VAR_020322|||http://purl.uniprot.org/annotation/VAR_032110|||http://purl.uniprot.org/annotation/VAR_032111|||http://purl.uniprot.org/annotation/VAR_080492|||http://purl.uniprot.org/annotation/VAR_080493|||http://purl.uniprot.org/annotation/VAR_080494|||http://purl.uniprot.org/annotation/VAR_080495|||http://purl.uniprot.org/annotation/VSP_025045|||http://purl.uniprot.org/annotation/VSP_046168
http://togogenome.org/gene/9606:SPRR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22528                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 12 AA approximate repeats|||3|||4|||5|||6|||6 X 8 AA approximate tandem repeats|||Cornifin-B|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149996|||http://purl.uniprot.org/annotation/VAR_002164|||http://purl.uniprot.org/annotation/VAR_002165|||http://purl.uniprot.org/annotation/VAR_002166|||http://purl.uniprot.org/annotation/VAR_021099
http://togogenome.org/gene/9606:NCAPG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XI2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Condensin-2 complex subunit G2|||HEAT|||In 3KS.|||In 3KS; leads to defects in mitotic chromosome compaction and organization; increases the number of micronuclei; increases cell death.|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255942|||http://purl.uniprot.org/annotation/VAR_053046|||http://purl.uniprot.org/annotation/VAR_053047|||http://purl.uniprot.org/annotation/VAR_083028|||http://purl.uniprot.org/annotation/VAR_083029|||http://purl.uniprot.org/annotation/VAR_083030|||http://purl.uniprot.org/annotation/VSP_021311
http://togogenome.org/gene/9606:IDH3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZN1|||http://purl.uniprot.org/uniprot/A0A087X2E5|||http://purl.uniprot.org/uniprot/O43837                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In RP46.|||In isoform A.|||In isoform C.|||Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial|||Isopropylmalate dehydrogenase-like|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014444|||http://purl.uniprot.org/annotation/VAR_022660|||http://purl.uniprot.org/annotation/VAR_049781|||http://purl.uniprot.org/annotation/VAR_054851|||http://purl.uniprot.org/annotation/VAR_056005|||http://purl.uniprot.org/annotation/VSP_002462|||http://purl.uniprot.org/annotation/VSP_041335
http://togogenome.org/gene/9606:MATCAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68EN5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished tyrosine carboxypeptidase activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Microtubule-associated tyrosine carboxypeptidase 1|||Nucleophile|||Reduced binding to microtubules.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320619|||http://purl.uniprot.org/annotation/VSP_031689|||http://purl.uniprot.org/annotation/VSP_031690|||http://purl.uniprot.org/annotation/VSP_031691
http://togogenome.org/gene/9606:TAFA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5A7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chemokine-like protein TAFA-5|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042732|||http://purl.uniprot.org/annotation/VSP_016068|||http://purl.uniprot.org/annotation/VSP_035191
http://togogenome.org/gene/9606:RAVER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PTBP1|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||RRM 1|||RRM 2|||RRM 3|||Removed|||Ribonucleoprotein PTB-binding 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081487|||http://purl.uniprot.org/annotation/VSP_017035|||http://purl.uniprot.org/annotation/VSP_017036|||http://purl.uniprot.org/annotation/VSP_040968|||http://purl.uniprot.org/annotation/VSP_040969
http://togogenome.org/gene/9606:C1orf56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Protein MENT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304969|||http://purl.uniprot.org/annotation/VSP_028157|||http://purl.uniprot.org/annotation/VSP_028158
http://togogenome.org/gene/9606:ACOT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14734                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 8|||Charge relay system|||Disordered|||Microbody targeting signal|||Reduces Acyl-CoA thioesterase activity and peroxisome proliferation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202152
http://togogenome.org/gene/9606:DYNC2H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCM8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Cytoplasmic dynein 2 heavy chain 1|||In SRTD3.|||In SRTD3; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Probable disease-associated variant found in short rib-polydactyly syndrome 3/6; digenic inheritance; the patient also carries a mutation in NEK1.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318743|||http://purl.uniprot.org/annotation/VAR_038862|||http://purl.uniprot.org/annotation/VAR_038863|||http://purl.uniprot.org/annotation/VAR_038864|||http://purl.uniprot.org/annotation/VAR_038865|||http://purl.uniprot.org/annotation/VAR_038866|||http://purl.uniprot.org/annotation/VAR_038867|||http://purl.uniprot.org/annotation/VAR_038868|||http://purl.uniprot.org/annotation/VAR_038869|||http://purl.uniprot.org/annotation/VAR_038870|||http://purl.uniprot.org/annotation/VAR_038871|||http://purl.uniprot.org/annotation/VAR_038872|||http://purl.uniprot.org/annotation/VAR_038873|||http://purl.uniprot.org/annotation/VAR_063242|||http://purl.uniprot.org/annotation/VAR_063243|||http://purl.uniprot.org/annotation/VAR_063244|||http://purl.uniprot.org/annotation/VAR_063245|||http://purl.uniprot.org/annotation/VAR_063246|||http://purl.uniprot.org/annotation/VAR_063247|||http://purl.uniprot.org/annotation/VAR_063248|||http://purl.uniprot.org/annotation/VAR_063249|||http://purl.uniprot.org/annotation/VAR_063250|||http://purl.uniprot.org/annotation/VAR_063251|||http://purl.uniprot.org/annotation/VAR_069591|||http://purl.uniprot.org/annotation/VAR_069592|||http://purl.uniprot.org/annotation/VAR_069593|||http://purl.uniprot.org/annotation/VAR_069594|||http://purl.uniprot.org/annotation/VAR_069595|||http://purl.uniprot.org/annotation/VAR_069596|||http://purl.uniprot.org/annotation/VAR_069597|||http://purl.uniprot.org/annotation/VAR_069598|||http://purl.uniprot.org/annotation/VAR_069599|||http://purl.uniprot.org/annotation/VAR_069600|||http://purl.uniprot.org/annotation/VAR_069601|||http://purl.uniprot.org/annotation/VAR_069602|||http://purl.uniprot.org/annotation/VAR_069603|||http://purl.uniprot.org/annotation/VAR_069604|||http://purl.uniprot.org/annotation/VAR_069605|||http://purl.uniprot.org/annotation/VAR_069606|||http://purl.uniprot.org/annotation/VAR_069607|||http://purl.uniprot.org/annotation/VAR_069608|||http://purl.uniprot.org/annotation/VAR_069609|||http://purl.uniprot.org/annotation/VAR_069610|||http://purl.uniprot.org/annotation/VAR_069611|||http://purl.uniprot.org/annotation/VAR_069612|||http://purl.uniprot.org/annotation/VAR_069613|||http://purl.uniprot.org/annotation/VAR_069614|||http://purl.uniprot.org/annotation/VAR_069615|||http://purl.uniprot.org/annotation/VAR_069616|||http://purl.uniprot.org/annotation/VSP_031282|||http://purl.uniprot.org/annotation/VSP_031283
http://togogenome.org/gene/9606:ZNF226                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBM0|||http://purl.uniprot.org/uniprot/Q9NYT6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 226                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047467|||http://purl.uniprot.org/annotation/VSP_046853|||http://purl.uniprot.org/annotation/VSP_046854
http://togogenome.org/gene/9606:GPR161                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQW8|||http://purl.uniprot.org/uniprot/Q8N6U8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 161|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069646|||http://purl.uniprot.org/annotation/VSP_010560|||http://purl.uniprot.org/annotation/VSP_010561|||http://purl.uniprot.org/annotation/VSP_035561|||http://purl.uniprot.org/annotation/VSP_044778|||http://purl.uniprot.org/annotation/VSP_044779|||http://purl.uniprot.org/annotation/VSP_045329|||http://purl.uniprot.org/annotation/VSP_046299
http://togogenome.org/gene/9606:NXPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58417|||http://purl.uniprot.org/uniprot/Q3LID8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  II|||III|||IV (linker domain)|||N-linked (GlcNAc...) asparagine|||Neurexophilin|||Neurexophilin-1|||V (Cys-rich)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020059|||http://purl.uniprot.org/annotation/PRO_5014309089
http://togogenome.org/gene/9606:GGH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92820                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Gamma-glutamyl hydrolase|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Nucleophile|||Proton donor|||Reduces activity 250-fold.|||Slightly reduced catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026539|||http://purl.uniprot.org/annotation/VAR_014697|||http://purl.uniprot.org/annotation/VAR_029230|||http://purl.uniprot.org/annotation/VAR_029231
http://togogenome.org/gene/9606:CCT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX11|||http://purl.uniprot.org/uniprot/P49368|||http://purl.uniprot.org/uniprot/Q59H77                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||T-complex protein 1 subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128321|||http://purl.uniprot.org/annotation/VAR_052265|||http://purl.uniprot.org/annotation/VSP_042026
http://togogenome.org/gene/9606:MAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Inhibits interaction with ZDHHC13 and ZDHHC17.|||Microtubule-associated protein 6|||Mn 1|||Mn 2|||Mn 3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344044|||http://purl.uniprot.org/annotation/VAR_044542|||http://purl.uniprot.org/annotation/VSP_034723|||http://purl.uniprot.org/annotation/VSP_054151
http://togogenome.org/gene/9606:LIPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK58                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Acyl-thioester intermediate|||BPL/LPL catalytic|||In NELABA.|||Lowers pKa of active site Cys|||Mislocalization to the cytosol; induces apoptotic cell death.|||Mitochondrion|||Putative lipoyltransferase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332305|||http://purl.uniprot.org/annotation/VAR_080037|||http://purl.uniprot.org/annotation/VAR_080038|||http://purl.uniprot.org/annotation/VAR_080039
http://togogenome.org/gene/9606:CLDND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHS1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Claudin domain-containing protein 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271020
http://togogenome.org/gene/9606:FBXO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Allows a rapid multiple mono-ubiquitination of the APC substrate, but strongly inhibits the slow ubiquitin chain elongation catalyzed by UBCH10|||Competitively blocks access of APC substrates to the D-box coreceptor formed by FZR1 and ANAPC10|||Decreases UBE2C-mediated ubiquitination.|||Degraded in similar manner to wild-type.|||Delays degradation.|||Disordered|||Does not affect inhibition of UBE2S-catalyzed chain elongation. Efficiently inhibits the degradation of PTTG1 at relatively high concentration. Reduces the competitive ability of FBXO5 to inhibit the association of PTTG1 to APC. Cannot compete with the APC substrate for APC binding. Decreases inhibition of CCNB1 ubiquitination by UBE2C.|||Does not affect protein stability.|||Does not affect protein stability; when associated with A-145.|||Does not affect protein stability; when associated with A-149.|||Does not affect the inhibitory activity against chain assembly; when associated with S-401.|||F-box|||F-box only protein 5|||Impairs CCNB1 ubiquitination by UBE2C; when associated with 339-K--L-345 del.|||Impairs CCNB1 ubiquitination by UBE2C; when associated with 356-Y--R-358 del.|||In isoform 2.|||Inhibits APC ubiquitin ligase activity|||Inhibits CCNB1 ubiquitination by UBE2C. Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with A-345; A-356 and A-358.|||Interaction with EVI5|||Loses inhibitory activity on UBE2S-catalyzed chain elongation.|||Loss of interaction with EVI5.|||Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145.|||Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149.|||Phosphoserine|||Reduced inhibition of APC. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly; when associated with S-401. Does not affect inhibition of UBE2S-catalyzed chain elongation. Reduces the competitive ability of FBXO5 to inhibit the association of securin to APC. Can still compete with the APC substrate for APC binding. Fails to inhibit ubiquitin chain assembly by UBE2C or mono-ubiquitination by UBE2D1. Largely abolishes the inhibitory activity against protein degradation. Fails to inactivate APC-FZR1 complex. Allows FBXO5 degradation in the absence of CDK4 inhibitor.|||Requires for efficient binding to CDC20|||Shows impaired interaction with BTRC.|||Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del.|||Sufficient for interaction with RPS6KA2; Prevents association of CDC20 with RPS6KA2|||Sufficient to suppress UBE2S activity; essential for interaction with UBE2S; competitively inhibits the rapide ubiquitin chain elongation by UBE2D1 which blocks UBE2D1 with APC; indispensable for recruitment and position of FBXO5 to the catalytic site of APC; abrogates the inhibition of ubiquitin chain assembly primarily catalyzed by UBE2S; inhibits the ubiquitination by either UBE2C or UBE2D1|||ZBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119881|||http://purl.uniprot.org/annotation/VAR_024440|||http://purl.uniprot.org/annotation/VAR_049038|||http://purl.uniprot.org/annotation/VSP_041362
http://togogenome.org/gene/9606:SDR39U1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6RWC2|||http://purl.uniprot.org/uniprot/Q86TZ5|||http://purl.uniprot.org/uniprot/Q9NRG7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DUF1731|||Disordered|||Epimerase family protein SDR39U1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279748|||http://purl.uniprot.org/annotation/VAR_057465|||http://purl.uniprot.org/annotation/VAR_057466|||http://purl.uniprot.org/annotation/VAR_060623|||http://purl.uniprot.org/annotation/VAR_060624|||http://purl.uniprot.org/annotation/VSP_060049|||http://purl.uniprot.org/annotation/VSP_060050
http://togogenome.org/gene/9606:PAPSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95340|||http://purl.uniprot.org/uniprot/Q5TB52                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-sulfurylase PUA-like|||Adenylyl-sulfate kinase|||Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2|||Decreased sulfate assimilation.|||In BCYM4; increases ubiquitin-dependent protein instability.|||In BCYM4; patient with premature pubarche and hyperandrogenism; decreased sulfate assimilation; increases ubiquitin-dependent protein instability.|||In BCYM4; reduced 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process.|||In isoform B.|||No effect on 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process.|||Sulfate adenylyltransferase|||Sulphate adenylyltransferase catalytic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105961|||http://purl.uniprot.org/annotation/VAR_022077|||http://purl.uniprot.org/annotation/VAR_029136|||http://purl.uniprot.org/annotation/VAR_029137|||http://purl.uniprot.org/annotation/VAR_029138|||http://purl.uniprot.org/annotation/VAR_063049|||http://purl.uniprot.org/annotation/VAR_073026|||http://purl.uniprot.org/annotation/VAR_073027|||http://purl.uniprot.org/annotation/VAR_073028|||http://purl.uniprot.org/annotation/VAR_073029|||http://purl.uniprot.org/annotation/VSP_001259
http://togogenome.org/gene/9606:PSME4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14997                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to acetylated histones.|||Bromodomain-like (BRDL)|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Proteasome activator complex subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280718|||http://purl.uniprot.org/annotation/VAR_031189|||http://purl.uniprot.org/annotation/VAR_031190|||http://purl.uniprot.org/annotation/VAR_059755|||http://purl.uniprot.org/annotation/VSP_023876|||http://purl.uniprot.org/annotation/VSP_023877|||http://purl.uniprot.org/annotation/VSP_023878|||http://purl.uniprot.org/annotation/VSP_023879
http://togogenome.org/gene/9606:PLXNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCM2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||PSI 1|||PSI 2|||PSI 3|||Plexin-A4|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240283|||http://purl.uniprot.org/annotation/VSP_019330|||http://purl.uniprot.org/annotation/VSP_019331|||http://purl.uniprot.org/annotation/VSP_019332|||http://purl.uniprot.org/annotation/VSP_019333|||http://purl.uniprot.org/annotation/VSP_019334
http://togogenome.org/gene/9606:TMEM151B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane protein 151B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307220|||http://purl.uniprot.org/annotation/VSP_028639|||http://purl.uniprot.org/annotation/VSP_028640
http://togogenome.org/gene/9606:DLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T3T9|||http://purl.uniprot.org/uniprot/Q6UY11                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein delta homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007534|||http://purl.uniprot.org/annotation/PRO_5004262741|||http://purl.uniprot.org/annotation/VAR_048977|||http://purl.uniprot.org/annotation/VSP_011767
http://togogenome.org/gene/9606:YTHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QR07|||http://purl.uniprot.org/uniprot/Q96MU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished binding to N6-methyladenosine (m6A)-containing RNAs.|||Abolishes RNA-binding and ability to influence alternative splice site selection.|||Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. Abolishes binding to m6A-containing mRNAs; when associated with A-377.|||Abolishes binding to N6-methyladenosine (m6A)-containing RNAs. Abolishes binding to m6A-containing mRNAs; when associated with A-428.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not affect ability to influence alternative splice site selection.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced binding affinity for N6-methyladenosine (m6A)-containing RNAs by 100-fold.|||Reduced binding affinity for N6-methyladenosine (m6A)-containing RNAs by 9-fold.|||Reduced binding to N6-methyladenosine (m6A)-containing RNAs.|||YTH|||YTH domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223076|||http://purl.uniprot.org/annotation/VAR_053746|||http://purl.uniprot.org/annotation/VSP_006818
http://togogenome.org/gene/9606:BLID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZY5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BH3-like|||BH3-like motif-containing cell death inducer|||Fails to induce apoptosis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301669|||http://purl.uniprot.org/annotation/VAR_056750
http://togogenome.org/gene/9606:PSMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99460                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 1|||Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||PC 1|||PC 10|||PC 2|||PC 3|||PC 4|||PC 5|||PC 6|||PC 7|||PC 8|||PC 9|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173801|||http://purl.uniprot.org/annotation/VSP_011475
http://togogenome.org/gene/9606:MMP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09238                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Motif|||Propeptide|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In a breast cancer sample; somatic mutation.|||Stromelysin-2|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028764|||http://purl.uniprot.org/annotation/PRO_0000028765|||http://purl.uniprot.org/annotation/VAR_020949|||http://purl.uniprot.org/annotation/VAR_020950|||http://purl.uniprot.org/annotation/VAR_020951|||http://purl.uniprot.org/annotation/VAR_020952|||http://purl.uniprot.org/annotation/VAR_020953|||http://purl.uniprot.org/annotation/VAR_020954|||http://purl.uniprot.org/annotation/VAR_020955|||http://purl.uniprot.org/annotation/VAR_036139
http://togogenome.org/gene/9606:ACAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTZ1|||http://purl.uniprot.org/uniprot/Q96P50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Acidic residues|||Arf-GAP|||Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 3|||C4-type|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000356159|||http://purl.uniprot.org/annotation/VSP_035992|||http://purl.uniprot.org/annotation/VSP_035993|||http://purl.uniprot.org/annotation/VSP_035994
http://togogenome.org/gene/9606:H2AC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93077                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 1-C|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055236
http://togogenome.org/gene/9606:DDX24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZR7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX24|||Basic and acidic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055029|||http://purl.uniprot.org/annotation/VAR_052162|||http://purl.uniprot.org/annotation/VSP_053881
http://togogenome.org/gene/9606:UBE4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14139                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In NEDHMS.|||In isoform 2.|||N6-acetyllysine|||Polar residues|||U-box|||Ubiquitin conjugation factor E4 A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194990|||http://purl.uniprot.org/annotation/VAR_086502|||http://purl.uniprot.org/annotation/VAR_086503|||http://purl.uniprot.org/annotation/VSP_013673
http://togogenome.org/gene/9606:SWT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXU9|||http://purl.uniprot.org/uniprot/Q5T5J6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PIN|||PINc|||Transcriptional protein SWT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251184|||http://purl.uniprot.org/annotation/VAR_027652|||http://purl.uniprot.org/annotation/VAR_027653|||http://purl.uniprot.org/annotation/VAR_027654|||http://purl.uniprot.org/annotation/VAR_027655
http://togogenome.org/gene/9606:CTLA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16410                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Cytotoxic T-lymphocyte protein 4|||Extracellular|||Helical|||Homodimerization|||Ig-like V-type|||Important for interaction with CD80 and CD86|||In IDAIL.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Increased risk for Graves disease, insulin-dependent diabetes mellitus, thyroid-associated orbitopathy, systemic lupus erythematosus and susceptibility to HBV infection.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by TXK and JAK2|||Strongly reduced interaction with CD80, CD86 and ICOSLG.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014734|||http://purl.uniprot.org/annotation/VAR_013577|||http://purl.uniprot.org/annotation/VAR_072681|||http://purl.uniprot.org/annotation/VSP_041284|||http://purl.uniprot.org/annotation/VSP_041285|||http://purl.uniprot.org/annotation/VSP_041286|||http://purl.uniprot.org/annotation/VSP_041287|||http://purl.uniprot.org/annotation/VSP_047238|||http://purl.uniprot.org/annotation/VSP_047239
http://togogenome.org/gene/9606:TTC38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5R3I4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Removed|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321530|||http://purl.uniprot.org/annotation/VAR_039344
http://togogenome.org/gene/9606:EPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Enhancer of polycomb homolog 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239295
http://togogenome.org/gene/9606:NLGN4X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4S1|||http://purl.uniprot.org/uniprot/B3KP11|||http://purl.uniprot.org/uniprot/Q8N0W4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Carboxylesterase type B|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with NRXN1|||N-linked (GlcNAc...) asparagine|||Neuroligin-4, X-linked|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008648|||http://purl.uniprot.org/annotation/VAR_036576|||http://purl.uniprot.org/annotation/VSP_013270
http://togogenome.org/gene/9606:TMPPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT21                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein with metallophosphoesterase domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322116|||http://purl.uniprot.org/annotation/VSP_031858
http://togogenome.org/gene/9606:IPO11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI26                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Importin N-terminal|||Importin-11|||In isoform 2.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120756|||http://purl.uniprot.org/annotation/VAR_050004|||http://purl.uniprot.org/annotation/VAR_050005|||http://purl.uniprot.org/annotation/VSP_041420
http://togogenome.org/gene/9606:SHISA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZ34                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Protein shisa-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395039|||http://purl.uniprot.org/annotation/VSP_059385
http://togogenome.org/gene/9606:KIR2DL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E3NZD8|||http://purl.uniprot.org/uniprot/P43628                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Immunoglobulin subtype|||In isoform 2.|||Killer cell immunoglobulin-like receptor 2DL3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015080|||http://purl.uniprot.org/annotation/PRO_5014303243|||http://purl.uniprot.org/annotation/VAR_010313|||http://purl.uniprot.org/annotation/VAR_010314|||http://purl.uniprot.org/annotation/VAR_010315|||http://purl.uniprot.org/annotation/VAR_010316|||http://purl.uniprot.org/annotation/VAR_010317|||http://purl.uniprot.org/annotation/VAR_015967|||http://purl.uniprot.org/annotation/VAR_015968|||http://purl.uniprot.org/annotation/VAR_015969|||http://purl.uniprot.org/annotation/VAR_015970|||http://purl.uniprot.org/annotation/VAR_049978|||http://purl.uniprot.org/annotation/VAR_049979|||http://purl.uniprot.org/annotation/VSP_007814
http://togogenome.org/gene/9606:CD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08571                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Monocyte differentiation antigen CD14, membrane-bound form|||Monocyte differentiation antigen CD14, urinary form|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Removed in mature form|||Required for response to bacterial lipopolysaccharide (LPS)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020884|||http://purl.uniprot.org/annotation/PRO_0000020885|||http://purl.uniprot.org/annotation/PRO_0000020886|||http://purl.uniprot.org/annotation/VAR_024302|||http://purl.uniprot.org/annotation/VAR_050771
http://togogenome.org/gene/9606:AHSA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V438|||http://purl.uniprot.org/uniprot/O95433                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activator of 90 kDa heat shock protein ATPase homolog 1|||Activator of Hsp90 ATPase homologue 1-like C-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphomimetic mutant. Increases the binding to HSP90AA1 resulting in TSC1 dissociation from HSP90AA1.|||Phosphoserine|||Phosphotyrosine; by ABL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215820|||http://purl.uniprot.org/annotation/VSP_055797
http://togogenome.org/gene/9606:SMC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR33|||http://purl.uniprot.org/uniprot/G8JLG1|||http://purl.uniprot.org/uniprot/Q14683|||http://purl.uniprot.org/uniprot/Q68EN4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In CDLS2.|||In CDLS2; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins.|||In CDLS2; unknown pathological significance.|||In DEE85.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by ATM and ATR|||Polar residues|||RecF/RecN/SMC N-terminal|||Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966.|||Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957.|||SMC hinge|||Structural maintenance of chromosomes protein 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118989|||http://purl.uniprot.org/annotation/VAR_026529|||http://purl.uniprot.org/annotation/VAR_026530|||http://purl.uniprot.org/annotation/VAR_052438|||http://purl.uniprot.org/annotation/VAR_062785|||http://purl.uniprot.org/annotation/VAR_062786|||http://purl.uniprot.org/annotation/VAR_062787|||http://purl.uniprot.org/annotation/VAR_062788|||http://purl.uniprot.org/annotation/VAR_062789|||http://purl.uniprot.org/annotation/VAR_062790|||http://purl.uniprot.org/annotation/VAR_062791|||http://purl.uniprot.org/annotation/VAR_062792|||http://purl.uniprot.org/annotation/VAR_062793|||http://purl.uniprot.org/annotation/VAR_062794|||http://purl.uniprot.org/annotation/VAR_062795|||http://purl.uniprot.org/annotation/VAR_062796|||http://purl.uniprot.org/annotation/VAR_062797|||http://purl.uniprot.org/annotation/VAR_062798|||http://purl.uniprot.org/annotation/VAR_062799|||http://purl.uniprot.org/annotation/VAR_062800|||http://purl.uniprot.org/annotation/VAR_062801|||http://purl.uniprot.org/annotation/VAR_062802|||http://purl.uniprot.org/annotation/VAR_062803|||http://purl.uniprot.org/annotation/VAR_064542|||http://purl.uniprot.org/annotation/VAR_064543|||http://purl.uniprot.org/annotation/VAR_078274|||http://purl.uniprot.org/annotation/VAR_078275|||http://purl.uniprot.org/annotation/VAR_078276|||http://purl.uniprot.org/annotation/VAR_078277|||http://purl.uniprot.org/annotation/VAR_078278|||http://purl.uniprot.org/annotation/VAR_083971|||http://purl.uniprot.org/annotation/VAR_083972|||http://purl.uniprot.org/annotation/VAR_083973|||http://purl.uniprot.org/annotation/VAR_083974|||http://purl.uniprot.org/annotation/VAR_083975|||http://purl.uniprot.org/annotation/VAR_083976|||http://purl.uniprot.org/annotation/VAR_083977|||http://purl.uniprot.org/annotation/VAR_083978
http://togogenome.org/gene/9606:ENDOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KNL5|||http://purl.uniprot.org/uniprot/Q14249                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  DNA/RNA non-specific endonuclease|||Endonuclease G, mitochondrial|||Essential for catalytic activity|||Essential for deoxyribonuclease activity|||Extracellular Endonuclease subunit A|||Interchain|||Loss of phosphorylation. Suppresses interaction with YWHAG and induction of autophagy; when associated with A-128.|||Loss of phosphorylation. Suppresses interaction with YWHAG and induction of autophagy; when associated with A-288.|||Mitochondrion|||Phosphomimetic mutant. No effect on its interaction with YWHAG. Enhances interaction with YWHAG; when associated with T-128.|||Phosphomimetic mutant. No effect on its interaction with YWHAG. Enhances interaction with YWHAG; when associated with T-288.|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by GSK3-beta|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019918|||http://purl.uniprot.org/annotation/VAR_031691
http://togogenome.org/gene/9606:IVNS1ABP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Y0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||In IMD70; uncertain pathological significance; strong decrease in protein expression.|||Influenza virus NS1A-binding protein|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Phosphoserine|||Polar residues|||Significant inhibition of interaction with AHR; partial decrease of AHR signaling induced by IVNS1ABP.|||Sufficient for AHR interaction and signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285077|||http://purl.uniprot.org/annotation/VAR_084531|||http://purl.uniprot.org/annotation/VAR_084532
http://togogenome.org/gene/9606:SPRED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z699                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In LGSS.|||KBD|||N-acetylserine|||N6-methyllysine|||Phosphoserine|||Removed|||Required for interaction with TESK1|||SPR|||Sprouty-related, EVH1 domain-containing protein 1|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076907|||http://purl.uniprot.org/annotation/VAR_064827|||http://purl.uniprot.org/annotation/VAR_064828
http://togogenome.org/gene/9606:OR52N4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGI2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52N4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150788|||http://purl.uniprot.org/annotation/VAR_034352|||http://purl.uniprot.org/annotation/VAR_034353|||http://purl.uniprot.org/annotation/VAR_053338|||http://purl.uniprot.org/annotation/VAR_053339
http://togogenome.org/gene/9606:UBQLNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Ubiquilin-like protein|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307791|||http://purl.uniprot.org/annotation/VAR_036652|||http://purl.uniprot.org/annotation/VAR_036653|||http://purl.uniprot.org/annotation/VAR_036654|||http://purl.uniprot.org/annotation/VAR_036655|||http://purl.uniprot.org/annotation/VAR_036656|||http://purl.uniprot.org/annotation/VAR_036657|||http://purl.uniprot.org/annotation/VAR_036658|||http://purl.uniprot.org/annotation/VAR_036659|||http://purl.uniprot.org/annotation/VSP_028833
http://togogenome.org/gene/9606:FRS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ7|||http://purl.uniprot.org/uniprot/O43559                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor receptor substrate 3|||IRS-type PTB|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087346|||http://purl.uniprot.org/annotation/VAR_033855
http://togogenome.org/gene/9606:PRRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14668|||http://purl.uniprot.org/uniprot/Q8NEK6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gla|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Transmembrane gamma-carboxyglutamic acid protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022541|||http://purl.uniprot.org/annotation/PRO_0000022542|||http://purl.uniprot.org/annotation/VAR_036268|||http://purl.uniprot.org/annotation/VSP_044789|||http://purl.uniprot.org/annotation/VSP_044790
http://togogenome.org/gene/9606:PGM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDQ8|||http://purl.uniprot.org/uniprot/B7Z6C2|||http://purl.uniprot.org/uniprot/P36871                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-D-phosphohexomutase alpha/beta/alpha|||In CDG1T; decreases mildly solubility.|||In CDG1T; decreases strongly solubility.|||In CDG1T; reduces mildly phosphoglucomutase activity.|||In CDG1T; reduces solubility; increases aggregation.|||In CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity.|||In CDG1T; strongly reduces phosphoglucomutase activity.|||In CDG1T; strongly reduces solubility; increases aggregation.|||In CDG1T; there is 7% enzyme residual phosphoglucomutase activity.|||In allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type.|||In allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type.|||In allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoglucomutase-1|||Phosphoserine|||Phosphoserine intermediate|||Phosphothreonine|||Phosphothreonine; by PAK1|||Phosphotyrosine|||via phosphate groupe                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147776|||http://purl.uniprot.org/annotation/VAR_006090|||http://purl.uniprot.org/annotation/VAR_006091|||http://purl.uniprot.org/annotation/VAR_006092|||http://purl.uniprot.org/annotation/VAR_034380|||http://purl.uniprot.org/annotation/VAR_050496|||http://purl.uniprot.org/annotation/VAR_062280|||http://purl.uniprot.org/annotation/VAR_069219|||http://purl.uniprot.org/annotation/VAR_071635|||http://purl.uniprot.org/annotation/VAR_071636|||http://purl.uniprot.org/annotation/VAR_071637|||http://purl.uniprot.org/annotation/VAR_071638|||http://purl.uniprot.org/annotation/VAR_071639|||http://purl.uniprot.org/annotation/VAR_071640|||http://purl.uniprot.org/annotation/VAR_071641|||http://purl.uniprot.org/annotation/VAR_071642|||http://purl.uniprot.org/annotation/VAR_071643|||http://purl.uniprot.org/annotation/VAR_071644|||http://purl.uniprot.org/annotation/VAR_071645|||http://purl.uniprot.org/annotation/VSP_004686|||http://purl.uniprot.org/annotation/VSP_045204
http://togogenome.org/gene/9606:ZNF624                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2J8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 624                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047695|||http://purl.uniprot.org/annotation/VAR_035592|||http://purl.uniprot.org/annotation/VAR_058001|||http://purl.uniprot.org/annotation/VSP_037538
http://togogenome.org/gene/9606:CTAGE6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||cTAGE family member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000384149
http://togogenome.org/gene/9606:SEPTIN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14141|||http://purl.uniprot.org/uniprot/Q541S4|||http://purl.uniprot.org/uniprot/Q548C9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform I.|||In isoform IV.|||In isoform V.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Septin-6|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173525|||http://purl.uniprot.org/annotation/VSP_006051|||http://purl.uniprot.org/annotation/VSP_006052|||http://purl.uniprot.org/annotation/VSP_006053|||http://purl.uniprot.org/annotation/VSP_006054
http://togogenome.org/gene/9606:CEP295NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||CEP295 N-terminal-like protein|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422183
http://togogenome.org/gene/9606:GMCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53SE7|||http://purl.uniprot.org/uniprot/Q96IK5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BTB|||Disordered|||Germ cell-less protein-like 1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087520
http://togogenome.org/gene/9606:PLBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHP8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Putative phospholipase B-like 2|||Putative phospholipase B-like 2 32 kDa form|||Putative phospholipase B-like 2 45 kDa form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286110|||http://purl.uniprot.org/annotation/PRO_0000314074|||http://purl.uniprot.org/annotation/PRO_0000314075|||http://purl.uniprot.org/annotation/VAR_032075|||http://purl.uniprot.org/annotation/VAR_062187|||http://purl.uniprot.org/annotation/VSP_055623
http://togogenome.org/gene/9606:METTL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JXM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Pro residues|||Probable methyltransferase-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343743|||http://purl.uniprot.org/annotation/VAR_044502
http://togogenome.org/gene/9606:ST6GALNAC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4F1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149278
http://togogenome.org/gene/9606:FEM1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||Found in a patient with polycystic ovary syndrome; unknown pathological significance.|||Phosphoserine|||Polar residues|||Protein fem-1 homolog A|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324525|||http://purl.uniprot.org/annotation/VAR_039809
http://togogenome.org/gene/9606:NIPSNAP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z3L7|||http://purl.uniprot.org/uniprot/Q9BS92                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N6-succinyllysine|||NIPSNAP|||Protein NipSnap homolog 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221154|||http://purl.uniprot.org/annotation/VAR_050277|||http://purl.uniprot.org/annotation/VAR_050278|||http://purl.uniprot.org/annotation/VAR_050279
http://togogenome.org/gene/9606:CAPSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWF8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Calcyphosin-like protein|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264473|||http://purl.uniprot.org/annotation/VAR_029631|||http://purl.uniprot.org/annotation/VAR_029632
http://togogenome.org/gene/9606:B3GAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPZ5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Region|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2|||Helical; Signal-anchor for type II membrane protein|||Interaction with galactose moiety of substrate glycoprotein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195172
http://togogenome.org/gene/9606:ARID1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 1B|||Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||Found in a patient with autism; unknown pathological significance.|||Found in a patient with short stature; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||LXXLL|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with short stature; de novo mutation.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200576|||http://purl.uniprot.org/annotation/VAR_036257|||http://purl.uniprot.org/annotation/VAR_067662|||http://purl.uniprot.org/annotation/VAR_067663|||http://purl.uniprot.org/annotation/VAR_067664|||http://purl.uniprot.org/annotation/VAR_067665|||http://purl.uniprot.org/annotation/VAR_067666|||http://purl.uniprot.org/annotation/VAR_067667|||http://purl.uniprot.org/annotation/VAR_067668|||http://purl.uniprot.org/annotation/VAR_067669|||http://purl.uniprot.org/annotation/VAR_067670|||http://purl.uniprot.org/annotation/VAR_067671|||http://purl.uniprot.org/annotation/VAR_067672|||http://purl.uniprot.org/annotation/VAR_067673|||http://purl.uniprot.org/annotation/VAR_067674|||http://purl.uniprot.org/annotation/VAR_067675|||http://purl.uniprot.org/annotation/VAR_067676|||http://purl.uniprot.org/annotation/VAR_067677|||http://purl.uniprot.org/annotation/VAR_067678|||http://purl.uniprot.org/annotation/VAR_067679|||http://purl.uniprot.org/annotation/VAR_067680|||http://purl.uniprot.org/annotation/VAR_067681|||http://purl.uniprot.org/annotation/VAR_067682|||http://purl.uniprot.org/annotation/VAR_067683|||http://purl.uniprot.org/annotation/VAR_067684|||http://purl.uniprot.org/annotation/VAR_067685|||http://purl.uniprot.org/annotation/VAR_067686|||http://purl.uniprot.org/annotation/VAR_067687|||http://purl.uniprot.org/annotation/VAR_067688|||http://purl.uniprot.org/annotation/VAR_067689|||http://purl.uniprot.org/annotation/VAR_067690|||http://purl.uniprot.org/annotation/VAR_067691|||http://purl.uniprot.org/annotation/VAR_067692|||http://purl.uniprot.org/annotation/VAR_067693|||http://purl.uniprot.org/annotation/VAR_077456|||http://purl.uniprot.org/annotation/VAR_077457|||http://purl.uniprot.org/annotation/VAR_077458|||http://purl.uniprot.org/annotation/VAR_077459|||http://purl.uniprot.org/annotation/VAR_078697|||http://purl.uniprot.org/annotation/VAR_078698|||http://purl.uniprot.org/annotation/VSP_061510|||http://purl.uniprot.org/annotation/VSP_061511|||http://purl.uniprot.org/annotation/VSP_061512
http://togogenome.org/gene/9606:DRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MC2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dynein regulatory complex protein 1|||In CILD21.|||In CILD21; multiple flagellar abnormalities are present in patient sperm.|||In SPGF80.|||In SPGF80; no protein detected in a homozygous patient sperm.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277881|||http://purl.uniprot.org/annotation/VAR_030625|||http://purl.uniprot.org/annotation/VAR_030626|||http://purl.uniprot.org/annotation/VAR_030627|||http://purl.uniprot.org/annotation/VAR_030628|||http://purl.uniprot.org/annotation/VAR_057758|||http://purl.uniprot.org/annotation/VAR_087935|||http://purl.uniprot.org/annotation/VAR_087936|||http://purl.uniprot.org/annotation/VAR_087937|||http://purl.uniprot.org/annotation/VAR_087938|||http://purl.uniprot.org/annotation/VAR_087939
http://togogenome.org/gene/9606:IRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14316                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Diminished acetylation by both CREBBP/p300 and PCAF. Greatly reduced enhancement of H4 promoter activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Greatly diminished acetylation by PCAF. Lesser loss of acetylation by CREBBP/p300. Loss of DNA binding and no enhancement of H4 promoter activity.|||IRF tryptophan pentad repeat|||In isoform 2.|||Interferon regulatory factor 2|||Little loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Greater loss of sumoylation; when associated with R-137. Further loss of sumoylation; when associated with R-293. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-137 and R-293.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Additional small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-296. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293.|||Some loss of sumoylation. Increases IRF2-mediation activation of ISRE and H4 promoters. Increased inhibition of IRF1-mediated transcription. Further small loss of sumoylation; when associated with R-166. Great loss of sumoylation; when associated with R-137. Abolishes sumoylation. Greatly increased activation of ISRE and H4 promoters and further increased ability to inhibit IRF1-mediated transcription; when associated with R-166 and R-293.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154549|||http://purl.uniprot.org/annotation/VSP_043965
http://togogenome.org/gene/9606:IL32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24001                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interleukin-32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021487|||http://purl.uniprot.org/annotation/VAR_005506|||http://purl.uniprot.org/annotation/VSP_022005|||http://purl.uniprot.org/annotation/VSP_022006|||http://purl.uniprot.org/annotation/VSP_022007|||http://purl.uniprot.org/annotation/VSP_043318|||http://purl.uniprot.org/annotation/VSP_045785|||http://purl.uniprot.org/annotation/VSP_047855|||http://purl.uniprot.org/annotation/VSP_047856
http://togogenome.org/gene/9606:C14orf119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWQ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C14orf119                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089929|||http://purl.uniprot.org/annotation/VAR_033744
http://togogenome.org/gene/9606:P2RY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51582                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes agonist-induced phosphorylation. Prevents agonist-induced desensitization and loss of cell surface receptors.|||Cytoplasmic|||Extracellular|||Greatly reduces agonist-induced desensitization and loss of cell surface receptors.|||Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-334.|||Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-339.|||Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-334 and A-339.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||No effect on agonist-induced phosphorylation, no functional effect.|||No effect.|||No functional effect.|||P2Y purinoceptor 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070020|||http://purl.uniprot.org/annotation/VAR_011854|||http://purl.uniprot.org/annotation/VAR_011855|||http://purl.uniprot.org/annotation/VAR_011856|||http://purl.uniprot.org/annotation/VAR_049429
http://togogenome.org/gene/9606:SCN4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35499                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with severe dystrophia myotonica 2; unknown pathological significance; the patient carries a disease-causing CCTG repeat expansion in CNBP; may act as a disease modifier; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IQ|||IV|||Important for inhibition by tetrodotoxin|||Important for rapid channel inactivation|||In CMS16; enhanced fast inactivation and slowed recovery from fast inactivation.|||In CMS16; leads to fast inactivation.|||In CMS16; leads to hyperpolarization of the steady-state fast inactivation, slow recovery from inactivation and reduces the channel ability to activate in response to repetitive stimulating pulses.|||In HOKPP2.|||In HOKPP2; also found in patients with severe fetal hypokinesia or congenital myopathy; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials.|||In HOKPP2; atypical phenotype with heat-induced myotonia and cold-induced paralysis with hypokalemia; changes the voltage-gated sodium channel activity; increases channel activation and slow inactivation at low temperature.|||In HOKPP2; changes the voltage-gated sodium channel activity; increases membrane hypoexcitability; increases channel activation and both fast and slow channel inactivation.|||In HOKPP2; increased depolarization tendency at normal and reduced extracellular potassium and reduced amplitude and rise time of action potentials.|||In HYPP and NKPP.|||In HYPP and PMC.|||In MYOSCN4A and PMC.|||In MYOSCN4A and PMC; severe.|||In MYOSCN4A.|||In MYOSCN4A; acetazolamide-responsive myotonia.|||In MYOSCN4A; also found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function.|||In MYOSCN4A; causes a hyperpolarizing shift of the activation curve; enhances channel slow inactivation.|||In MYOSCN4A; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability; decreases channel fast inactivation.|||In MYOSCN4A; enhances voltage-gated sodium channel activation inducing membrane hyperexcitability.|||In MYOSCN4A; fluctuating cold-induced and exercise-induced stiffness.|||In MYOSCN4A; highly variable severity.|||In MYOSCN4A; unusually severe and lethal phenotype with neonatal onset.|||In MYOSCN4A; variable phenotype ranging from mild to severe myotonia.|||In NKPP and HOKPP2; detected in a family where three affected members manifested hypokalemic periodic paralysis whereas five other patients had normokalemic periodic paralysis.|||In NKPP.|||In PMC and HYPP.|||In PMC, MYOSCN4A and HYPP.|||In PMC.|||In PMC; accelerates deactivation from the inactivated state and enhances the remobilization of gating charge.|||In PMC; changes the voltage-gated sodium channel activity; increases membrane hyperexcitability at low temperature; decreases channel activation, deactivation, fast inactivation and recovery delay from fast inactivation.|||In PMC; increases the extent of charge immobilization in response to strong depolarization.|||In PMC; without cold paralysis.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||N-linked (GlcNAc...) asparagine|||No significant effect on channel activity.|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; complete loss of sodium channel function.|||Probable disease-associated variant found in patients with severe fetal hypokinesia or congenital myopathy; impaired sodium channel function.|||Sodium channel protein type 4 subunit alpha|||Voltage-gated sodium channel activity is not affected and channel activation as well as fast and slow inactivation curves are normal. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048495|||http://purl.uniprot.org/annotation/VAR_001560|||http://purl.uniprot.org/annotation/VAR_001561|||http://purl.uniprot.org/annotation/VAR_001562|||http://purl.uniprot.org/annotation/VAR_001563|||http://purl.uniprot.org/annotation/VAR_001564|||http://purl.uniprot.org/annotation/VAR_001565|||http://purl.uniprot.org/annotation/VAR_001566|||http://purl.uniprot.org/annotation/VAR_001567|||http://purl.uniprot.org/annotation/VAR_001568|||http://purl.uniprot.org/annotation/VAR_001569|||http://purl.uniprot.org/annotation/VAR_001570|||http://purl.uniprot.org/annotation/VAR_001571|||http://purl.uniprot.org/annotation/VAR_001572|||http://purl.uniprot.org/annotation/VAR_001573|||http://purl.uniprot.org/annotation/VAR_001574|||http://purl.uniprot.org/annotation/VAR_001575|||http://purl.uniprot.org/annotation/VAR_017785|||http://purl.uniprot.org/annotation/VAR_017786|||http://purl.uniprot.org/annotation/VAR_017787|||http://purl.uniprot.org/annotation/VAR_017788|||http://purl.uniprot.org/annotation/VAR_017789|||http://purl.uniprot.org/annotation/VAR_017790|||http://purl.uniprot.org/annotation/VAR_017791|||http://purl.uniprot.org/annotation/VAR_017792|||http://purl.uniprot.org/annotation/VAR_017793|||http://purl.uniprot.org/annotation/VAR_017794|||http://purl.uniprot.org/annotation/VAR_017795|||http://purl.uniprot.org/annotation/VAR_022341|||http://purl.uniprot.org/annotation/VAR_037104|||http://purl.uniprot.org/annotation/VAR_037105|||http://purl.uniprot.org/annotation/VAR_037106|||http://purl.uniprot.org/annotation/VAR_037107|||http://purl.uniprot.org/annotation/VAR_054934|||http://purl.uniprot.org/annotation/VAR_054935|||http://purl.uniprot.org/annotation/VAR_054936|||http://purl.uniprot.org/annotation/VAR_054937|||http://purl.uniprot.org/annotation/VAR_054938|||http://purl.uniprot.org/annotation/VAR_054939|||http://purl.uniprot.org/annotation/VAR_054940|||http://purl.uniprot.org/annotation/VAR_054941|||http://purl.uniprot.org/annotation/VAR_054942|||http://purl.uniprot.org/annotation/VAR_054943|||http://purl.uniprot.org/annotation/VAR_054944|||http://purl.uniprot.org/annotation/VAR_054945|||http://purl.uniprot.org/annotation/VAR_054946|||http://purl.uniprot.org/annotation/VAR_054947|||http://purl.uniprot.org/annotation/VAR_054948|||http://purl.uniprot.org/annotation/VAR_054949|||http://purl.uniprot.org/annotation/VAR_054950|||http://purl.uniprot.org/annotation/VAR_054951|||http://purl.uniprot.org/annotation/VAR_054952|||http://purl.uniprot.org/annotation/VAR_064987|||http://purl.uniprot.org/annotation/VAR_065230|||http://purl.uniprot.org/annotation/VAR_065231|||http://purl.uniprot.org/annotation/VAR_074581|||http://purl.uniprot.org/annotation/VAR_074598|||http://purl.uniprot.org/annotation/VAR_075430|||http://purl.uniprot.org/annotation/VAR_075431|||http://purl.uniprot.org/annotation/VAR_075432|||http://purl.uniprot.org/annotation/VAR_075433|||http://purl.uniprot.org/annotation/VAR_075434|||http://purl.uniprot.org/annotation/VAR_075435|||http://purl.uniprot.org/annotation/VAR_075436|||http://purl.uniprot.org/annotation/VAR_075437|||http://purl.uniprot.org/annotation/VAR_079519
http://togogenome.org/gene/9606:ADH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40394                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  All-trans-retinol dehydrogenase [NAD(+)] ADH7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160691|||http://purl.uniprot.org/annotation/VAR_024364|||http://purl.uniprot.org/annotation/VSP_043093
http://togogenome.org/gene/9606:LCN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6JVE6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Epididymal-specific lipocalin-10|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017920|||http://purl.uniprot.org/annotation/VSP_040220
http://togogenome.org/gene/9606:SOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL29|||http://purl.uniprot.org/uniprot/G5E9P6|||http://purl.uniprot.org/uniprot/P04179|||http://purl.uniprot.org/uniprot/Q96AM7|||http://purl.uniprot.org/uniprot/Q9UG59                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Associated with a decreased susceptibility to diabetic nephropathy in Japanese and Chinese patients with type 2 diabetes.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment.|||Manganese/iron superoxide dismutase C-terminal|||Manganese/iron superoxide dismutase N-terminal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Reduced enzyme activity.|||Superoxide dismutase [Mn], mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032869|||http://purl.uniprot.org/annotation/VAR_007165|||http://purl.uniprot.org/annotation/VAR_016183|||http://purl.uniprot.org/annotation/VAR_019363|||http://purl.uniprot.org/annotation/VAR_019364|||http://purl.uniprot.org/annotation/VAR_019365|||http://purl.uniprot.org/annotation/VAR_025898|||http://purl.uniprot.org/annotation/VSP_042558|||http://purl.uniprot.org/annotation/VSP_053761|||http://purl.uniprot.org/annotation/VSP_053762
http://togogenome.org/gene/9606:KLHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7A1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119126
http://togogenome.org/gene/9606:RBBP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75884                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Involved in binding to RB1|||Loss of catalytic activity. Fails to block TGF-beta-mediated anti-proliferative signal in tumor cells.|||Serine hydrolase RBBP9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097180|||http://purl.uniprot.org/annotation/VSP_004374
http://togogenome.org/gene/9606:NR2C2AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WQ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nuclear receptor 2C2-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295585|||http://purl.uniprot.org/annotation/VSP_056072
http://togogenome.org/gene/9606:POU1F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28069                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Homeobox|||In CPHD1.|||In CPHD1; associated with less severe impairment of transactivation; has a similar DNA-binding affinity as the wild-type protein.|||In CPHD1; associated with severe impairment of transactivation; has a greatly reduced DNA-binding affinity as the wild-type protein.|||In CPHD1; loss of function.|||In CPHD1; reduces transactivation capacity on the GH1 gene; increases the functional binding on the GH1 promoter; increases the interaction with ELK1, LHX3 and PITX1.|||In CPHD1; reduces transactivation capacity on the PRL gene; increases instability of the protein.|||In CPHD1; transactivation capacity of this mutant is markedly decreased on the GH1; PRL, TSHB and POU1F1 genes; abolishes the functional interaction of POU1F1 on the PRL promoter with the coactivator CREBBP but not with the transcription factor LHX3; displays normal nuclear accumulation but a markedly decreased binding to a DNA response element.|||In isoform A.|||Increases the interaction with LHX3 and PITX1. No effect on the interaction with ELK1.|||Increases the interaction with LHX3. No effect on the interaction with ELK1.|||No effect on the interaction with ELK1, LHX3 and PITX1.|||POU-specific|||Pituitary-specific positive transcription factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100697|||http://purl.uniprot.org/annotation/VAR_003776|||http://purl.uniprot.org/annotation/VAR_003777|||http://purl.uniprot.org/annotation/VAR_003778|||http://purl.uniprot.org/annotation/VAR_003779|||http://purl.uniprot.org/annotation/VAR_003780|||http://purl.uniprot.org/annotation/VAR_003781|||http://purl.uniprot.org/annotation/VAR_010574|||http://purl.uniprot.org/annotation/VAR_010575|||http://purl.uniprot.org/annotation/VAR_010576|||http://purl.uniprot.org/annotation/VAR_015260|||http://purl.uniprot.org/annotation/VAR_049361|||http://purl.uniprot.org/annotation/VAR_063425|||http://purl.uniprot.org/annotation/VAR_063426|||http://purl.uniprot.org/annotation/VAR_063427|||http://purl.uniprot.org/annotation/VAR_075530|||http://purl.uniprot.org/annotation/VAR_075531|||http://purl.uniprot.org/annotation/VSP_002314
http://togogenome.org/gene/9606:TM4SF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CE8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Transmembrane 4 L6 family member 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219304
http://togogenome.org/gene/9606:TRIM51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||In isoform 2.|||RING-type|||Tripartite motif-containing protein 51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328724|||http://purl.uniprot.org/annotation/VSP_039765
http://togogenome.org/gene/9606:COPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53618                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coatomer subunit beta|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In BARMACS.|||N-acetylthreonine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193833|||http://purl.uniprot.org/annotation/VAR_085552
http://togogenome.org/gene/9606:CCNH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51946                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclin-H|||Disordered|||No effect on the transcriptional activity of the reconstituted TFIIH complex.|||Phosphoserine|||Phosphoserine; by CDK8|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080471|||http://purl.uniprot.org/annotation/VAR_013067|||http://purl.uniprot.org/annotation/VAR_013068|||http://purl.uniprot.org/annotation/VAR_013069|||http://purl.uniprot.org/annotation/VAR_013070
http://togogenome.org/gene/9606:MGME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQP7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Abolishes exonuclease activity.|||In MTDPS11; impaired exonuclease activity.|||Mitochondrial genome maintenance exonuclease 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079439|||http://purl.uniprot.org/annotation/VAR_033758|||http://purl.uniprot.org/annotation/VAR_069102
http://togogenome.org/gene/9606:CRKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46109                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with DOCK5.|||Crk-like protein|||Disordered|||Phosphotyrosine|||SH2|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079347
http://togogenome.org/gene/9606:TWF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12792                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADF-H 1|||ADF-H 2|||Disordered|||Found in a patient with isolated coloboma, increases interaction with ACTG1.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Twinfilin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214950|||http://purl.uniprot.org/annotation/VAR_082792|||http://purl.uniprot.org/annotation/VSP_017899|||http://purl.uniprot.org/annotation/VSP_038075
http://togogenome.org/gene/9606:TADA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BN2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Transcriptional adapter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316015|||http://purl.uniprot.org/annotation/VAR_038352
http://togogenome.org/gene/9606:LRRC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWI4|||http://purl.uniprot.org/uniprot/Q8TF66                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 15|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021605|||http://purl.uniprot.org/annotation/PRO_5002790184|||http://purl.uniprot.org/annotation/VAR_051101|||http://purl.uniprot.org/annotation/VAR_051102|||http://purl.uniprot.org/annotation/VSP_041130
http://togogenome.org/gene/9606:NFATC2IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCF5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||NFATC2-interacting protein|||Phosphoserine|||Phosphothreonine|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281008|||http://purl.uniprot.org/annotation/VAR_031208|||http://purl.uniprot.org/annotation/VSP_023931|||http://purl.uniprot.org/annotation/VSP_023932
http://togogenome.org/gene/9606:U2SURP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15042                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||CID|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Removed|||SURP motif|||U2 snRNP-associated SURP motif-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280070|||http://purl.uniprot.org/annotation/VSP_023522|||http://purl.uniprot.org/annotation/VSP_023523|||http://purl.uniprot.org/annotation/VSP_023524
http://togogenome.org/gene/9606:SLC20A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR38|||http://purl.uniprot.org/uniprot/B2RBR4|||http://purl.uniprot.org/uniprot/B4DJ71|||http://purl.uniprot.org/uniprot/Q08357                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-575.|||Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-91.|||Abolishes phosphate but not sodium uptake; when associated with Q-91 and Q-575.|||Abolishes sodium-dependent phosphate transport; no effect on retroviral receptor function.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs phosphate transport; no effect on retroviral receptor function.|||In IBGC1.|||In IBGC1; Impairs phosphate transport; no effect on retroviral receptor function.|||In IBGC1; loss of sodium-dependent phosphate transport but no effect on cell membrane localization.|||In IBGC1; substantially impaired phosphate transport.|||In IBGC1; unknown pathological significance.|||In IBGC1; unknown pathological significance; reduced sodium-dependent phosphate transport and cell membrane localization.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sodium-dependent phosphate transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341268|||http://purl.uniprot.org/annotation/VAR_067545|||http://purl.uniprot.org/annotation/VAR_067546|||http://purl.uniprot.org/annotation/VAR_067547|||http://purl.uniprot.org/annotation/VAR_067548|||http://purl.uniprot.org/annotation/VAR_067549|||http://purl.uniprot.org/annotation/VAR_067550|||http://purl.uniprot.org/annotation/VAR_072255|||http://purl.uniprot.org/annotation/VAR_072256|||http://purl.uniprot.org/annotation/VAR_072257|||http://purl.uniprot.org/annotation/VAR_072258|||http://purl.uniprot.org/annotation/VAR_072259|||http://purl.uniprot.org/annotation/VAR_072260|||http://purl.uniprot.org/annotation/VAR_072261|||http://purl.uniprot.org/annotation/VAR_072262|||http://purl.uniprot.org/annotation/VAR_072263|||http://purl.uniprot.org/annotation/VAR_072264|||http://purl.uniprot.org/annotation/VAR_072265|||http://purl.uniprot.org/annotation/VAR_075396|||http://purl.uniprot.org/annotation/VAR_075397|||http://purl.uniprot.org/annotation/VAR_075398|||http://purl.uniprot.org/annotation/VAR_088078
http://togogenome.org/gene/9606:LSM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylalanine|||Removed|||Sm|||U6 snRNA-associated Sm-like protein LSm7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125579
http://togogenome.org/gene/9606:BLTP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T938|||http://purl.uniprot.org/uniprot/Q2LD37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Bridge-like lipid transfer protein family member 1|||Bridge-like lipid transfer protein family member 1 C-terminal|||Disordered|||Helical|||In ALKKUCS.|||In ALKKUCS; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317555|||http://purl.uniprot.org/annotation/VAR_038547|||http://purl.uniprot.org/annotation/VAR_038548|||http://purl.uniprot.org/annotation/VAR_038549|||http://purl.uniprot.org/annotation/VAR_061241|||http://purl.uniprot.org/annotation/VAR_061242|||http://purl.uniprot.org/annotation/VAR_080684|||http://purl.uniprot.org/annotation/VAR_080685|||http://purl.uniprot.org/annotation/VAR_080686|||http://purl.uniprot.org/annotation/VAR_080687|||http://purl.uniprot.org/annotation/VAR_080688|||http://purl.uniprot.org/annotation/VAR_080689|||http://purl.uniprot.org/annotation/VAR_080690|||http://purl.uniprot.org/annotation/VAR_080691|||http://purl.uniprot.org/annotation/VAR_080692|||http://purl.uniprot.org/annotation/VAR_083180|||http://purl.uniprot.org/annotation/VAR_083181|||http://purl.uniprot.org/annotation/VAR_083182|||http://purl.uniprot.org/annotation/VAR_083183|||http://purl.uniprot.org/annotation/VSP_031023|||http://purl.uniprot.org/annotation/VSP_031024|||http://purl.uniprot.org/annotation/VSP_031025|||http://purl.uniprot.org/annotation/VSP_031026|||http://purl.uniprot.org/annotation/VSP_031027|||http://purl.uniprot.org/annotation/VSP_031028|||http://purl.uniprot.org/annotation/VSP_031029|||http://purl.uniprot.org/annotation/VSP_031030|||http://purl.uniprot.org/annotation/VSP_031031
http://togogenome.org/gene/9606:SPATS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q496A3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Spermatogenesis-associated serine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307694|||http://purl.uniprot.org/annotation/VAR_036631|||http://purl.uniprot.org/annotation/VSP_028787
http://togogenome.org/gene/9606:RRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15050                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Ribosome biogenesis regulatory protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185374|||http://purl.uniprot.org/annotation/VAR_020484|||http://purl.uniprot.org/annotation/VAR_051887|||http://purl.uniprot.org/annotation/VAR_051888
http://togogenome.org/gene/9606:PRPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK41|||http://purl.uniprot.org/uniprot/P11908                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Region|||Splice Variant                                                                                  ^@                                                                                  Binding of phosphoribosylpyrophosphate|||In isoform 2.|||Removed|||Ribose-phosphate pyrophosphokinase 2|||Ribose-phosphate pyrophosphokinase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141074|||http://purl.uniprot.org/annotation/VSP_027769
http://togogenome.org/gene/9606:ANAPC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUN5|||http://purl.uniprot.org/uniprot/C5H3H2|||http://purl.uniprot.org/uniprot/Q96DE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Turn                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 16|||Disordered|||N-acetylalanine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089816
http://togogenome.org/gene/9606:ING4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNL4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Citrulline|||Disordered|||Histone H3K4me3 binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Inhibitor of growth protein 4|||N6-acetyllysine|||PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212668|||http://purl.uniprot.org/annotation/VSP_012518|||http://purl.uniprot.org/annotation/VSP_012519|||http://purl.uniprot.org/annotation/VSP_041288|||http://purl.uniprot.org/annotation/VSP_041289|||http://purl.uniprot.org/annotation/VSP_041290|||http://purl.uniprot.org/annotation/VSP_041291|||http://purl.uniprot.org/annotation/VSP_041292|||http://purl.uniprot.org/annotation/VSP_041293
http://togogenome.org/gene/9606:EIF3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EK53|||http://purl.uniprot.org/uniprot/K7ERF1|||http://purl.uniprot.org/uniprot/Q9UBQ5|||http://purl.uniprot.org/uniprot/U3LUI4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 3 subunit K|||In isoform 2.|||N-acetylalanine|||PCI|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123546|||http://purl.uniprot.org/annotation/VSP_055475
http://togogenome.org/gene/9606:ZKSCAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234016|||http://purl.uniprot.org/annotation/VAR_033597|||http://purl.uniprot.org/annotation/VAR_033598|||http://purl.uniprot.org/annotation/VAR_057460|||http://purl.uniprot.org/annotation/VSP_018189|||http://purl.uniprot.org/annotation/VSP_018190
http://togogenome.org/gene/9606:IFI16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16666                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes TP53-mediated transcriptional activation; when associated with A-218.|||Abolishes TP53-mediated transcriptional activation; when associated with A-222.|||Abolishes TP53-mediated transcriptional activation; when associated with A-267.|||Abolishes TP53-mediated transcriptional activation; when associated with A-272.|||Basic and acidic residues|||Disordered|||Gamma-interferon-inducible protein 16|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HIN-200 1|||HIN-200 2|||Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734.|||Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759.|||Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759.|||Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759.|||Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759.|||Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759.|||Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759.|||Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform IFI16-beta.|||Interaction with TP53 C-terminus|||Interaction with TP53 core domain|||Minor effect on nuclear localization (mimics acetylated state).|||Mostly nuclear, minor cytoplasmic localization.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Predominant cytoplasmic localization.|||Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state).|||Predominant nuclear, some cytoplasmic localization.|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153723|||http://purl.uniprot.org/annotation/VAR_029486|||http://purl.uniprot.org/annotation/VAR_029487|||http://purl.uniprot.org/annotation/VAR_029488|||http://purl.uniprot.org/annotation/VAR_029489|||http://purl.uniprot.org/annotation/VAR_029490|||http://purl.uniprot.org/annotation/VAR_029491|||http://purl.uniprot.org/annotation/VAR_057582|||http://purl.uniprot.org/annotation/VSP_002675|||http://purl.uniprot.org/annotation/VSP_002676|||http://purl.uniprot.org/annotation/VSP_044691|||http://purl.uniprot.org/annotation/VSP_061846|||http://purl.uniprot.org/annotation/VSP_061847
http://togogenome.org/gene/9606:SRRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-acetylglycine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Serrate RNA effector molecule homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220965|||http://purl.uniprot.org/annotation/VSP_000324|||http://purl.uniprot.org/annotation/VSP_032502|||http://purl.uniprot.org/annotation/VSP_038122|||http://purl.uniprot.org/annotation/VSP_038123
http://togogenome.org/gene/9606:TERT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14746                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes oxidative stress-induced phosphorylation and RAN binding. Impaired nuclear export and enhanced antiapoptotic activity against ROS-dependent apoptosis induction. Impaired interaction with PTPN11. No dephosphorylation by PTPN11.|||Abolishes phosphorylation by DYRK2.|||Abolishes telomerase catalytic activity.|||About 75% reduction in telomerase activity, about 50% reduction in repeat extension rate and 5.2-fold increase in nucleotide incorporation fidelity. Little further reduction in activity and 13.5-fold increase in nucleotide incorporation fidelity; when associated with Y-866.|||About 75% reduction in telomerase activity, about 80% reduction in repeat reduction rate and 3.9-fold increase in nucleotide incorporation fidelity.|||About 80% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity, nor on TR interaction nor on protein levels.|||About 85% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction.|||About 90% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction.|||Associated with acute myeloid leukemia.|||Bipartite nuclear localization signal|||CP motif|||CTE|||Completely abolishes telomerase-mediated primer extension and reduced binding to short telomeric primers. Complete loss of catalytic activity but no further loss of binding to telomeric primers; when associated with 137-A--A-141.|||Defective in high-affinity TERC interactions.|||Disordered|||GQ motif|||In AA.|||In AA; abolishes telomerase catalytic activity but no effect on binding to TERC.|||In AA; associated with susceptibility to acute myeloid leukemia.|||In AA; non-severe; abolishes telomerase catalytic activity but little effect on binding to TERC.|||In AA; very severe; no effect on telomerase catalytic activity but shortened telomeres.|||In DKCA2; abolishes telomerase catalytic activity but no effect on binding to TERC.|||In DKCA2; severe; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC.|||In DKCA2; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC.|||In DKCB4; 50% reduction in telomerase activity.|||In DKCB4; no effect on telomerase catalytic activity and little effect on binding to TERC.|||In DKCB4; severe phenotype overlapping with Hoyeraal-Hreidarsson syndrome; very short telomeres and greatly reduced telomerase activity.|||In DKCB4; the mutant protein has 13% residual activity.|||In PFBMFT1 and AA; moderate.|||In PFBMFT1 and AA; severe and moderate; associated with disease susceptibility; shorter telomeres.|||In PFBMFT1, AA and DKCB4; severe and moderate; associated with susceptibility to acute myelogenous leukemia; the mutant protein has 36% residual activity.|||In PFBMFT1.|||In PFBMFT1; associated with Ile-791 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity; this mutation causes most if not all of the functional defects.|||In PFBMFT1; associated with Met-867 in cis on the same allele; the double mutant shows severe defects in telomere repeat addition processivity.|||In PFBMFT1; impaired telomerase activity.|||In PFBMFT1; moderate.|||In PFBMFT1; severe.|||In PFBMFT1; the mutant protein is demonstrated to cause decreased telomerase activity.|||In PFBMFT1; the mutant protein is demonstrated to cause severely compromised telomerase activity.|||In PFBMFT1; unknown pathological significance; impaired telomerase activity.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Increased incidence in sporadic acute myeloid leukemia.|||Linker|||Loss of telomerase activity.|||Loss of telomerase activity. In the absence of TR, no loss of binding to telomeric primers.|||Moderate reduction in telomerase activity, no change in repeat extension rate nor on nucleotide incorporation fidelity. Little further reduction in activity but 13.5-fold increase in nucleotide incorporation fidelity; when associated with M-867.|||Phosphoserine; by DYRK2|||Phosphoserine; by PKB/AKT1|||Phosphotyrosine; by SRC-type Tyr-kinases|||Primer grip sequence|||QFP motif|||RNA-interacting domain 1|||RNA-interacting domain 2|||Reduced catalytic activity and repeat addition processivity. Complete loss of catalytic activity but no loss of binding to telomeric primers; when associated with 930-A--A-934.|||Required for nucleotide incorporation and primer extension rate|||Required for oligomerization|||Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template|||Required for regulating specificity for telomeric DNA and for processivity for primer elongation|||Reverse transcriptase|||Severe reduction in telomerase activity, about 50% reduction in repeat extension rate and 2.2-fold increase in nucleotide incorporation fidelity. No further reduction in activity but 2.8-fold increase in nucleotide incorporation fidelity; when associated with Y-866.|||TFLY; involved in RNA binding|||Telomerase reverse transcriptase ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054925|||http://purl.uniprot.org/annotation/VAR_025149|||http://purl.uniprot.org/annotation/VAR_025150|||http://purl.uniprot.org/annotation/VAR_036863|||http://purl.uniprot.org/annotation/VAR_036864|||http://purl.uniprot.org/annotation/VAR_036865|||http://purl.uniprot.org/annotation/VAR_036866|||http://purl.uniprot.org/annotation/VAR_036867|||http://purl.uniprot.org/annotation/VAR_036868|||http://purl.uniprot.org/annotation/VAR_036869|||http://purl.uniprot.org/annotation/VAR_036870|||http://purl.uniprot.org/annotation/VAR_053726|||http://purl.uniprot.org/annotation/VAR_062535|||http://purl.uniprot.org/annotation/VAR_062536|||http://purl.uniprot.org/annotation/VAR_062537|||http://purl.uniprot.org/annotation/VAR_062538|||http://purl.uniprot.org/annotation/VAR_062539|||http://purl.uniprot.org/annotation/VAR_062540|||http://purl.uniprot.org/annotation/VAR_062541|||http://purl.uniprot.org/annotation/VAR_062542|||http://purl.uniprot.org/annotation/VAR_062543|||http://purl.uniprot.org/annotation/VAR_062544|||http://purl.uniprot.org/annotation/VAR_062780|||http://purl.uniprot.org/annotation/VAR_062781|||http://purl.uniprot.org/annotation/VAR_062782|||http://purl.uniprot.org/annotation/VAR_062783|||http://purl.uniprot.org/annotation/VAR_062784|||http://purl.uniprot.org/annotation/VAR_068792|||http://purl.uniprot.org/annotation/VAR_068793|||http://purl.uniprot.org/annotation/VAR_068794|||http://purl.uniprot.org/annotation/VAR_068795|||http://purl.uniprot.org/annotation/VAR_068796|||http://purl.uniprot.org/annotation/VAR_068797|||http://purl.uniprot.org/annotation/VAR_068798|||http://purl.uniprot.org/annotation/VAR_068799|||http://purl.uniprot.org/annotation/VAR_068800|||http://purl.uniprot.org/annotation/VAR_084996|||http://purl.uniprot.org/annotation/VSP_019587|||http://purl.uniprot.org/annotation/VSP_019588|||http://purl.uniprot.org/annotation/VSP_021727|||http://purl.uniprot.org/annotation/VSP_053369
http://togogenome.org/gene/9606:ERGIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2TJK5|||http://purl.uniprot.org/uniprot/Q9Y282                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes MARCHF2-mediated degradation.|||Cytoplasmic|||Endoplasmic reticulum vesicle transporter C-terminal|||Endoplasmic reticulum vesicle transporter N-terminal|||Endoplasmic reticulum-Golgi intermediate compartment protein 3|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||No effect on MARCHF2-mediated ubiquitination and degradation.|||Phosphoserine|||Reduces MARCHF2-mediated ubiquitination and degradation. No effect on interaction with MARCHF2. Reduces MARCHF2-mediated ubiquitination and degradation by 90%; when associated with R-8.|||Required for MARCHF2-mediated degradation|||Ubiquitinated; by MARCHF2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097640|||http://purl.uniprot.org/annotation/VAR_036553|||http://purl.uniprot.org/annotation/VAR_048939|||http://purl.uniprot.org/annotation/VSP_008652|||http://purl.uniprot.org/annotation/VSP_008653|||http://purl.uniprot.org/annotation/VSP_019208
http://togogenome.org/gene/9606:LETMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5D7|||http://purl.uniprot.org/uniprot/F8W1Z2|||http://purl.uniprot.org/uniprot/Q6P1Q0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||LETM1 domain-containing protein 1|||Letm1 RBD|||Mitochondrial intermembrane|||Required and sufficient for mitochondrial import                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310419|||http://purl.uniprot.org/annotation/VAR_037033|||http://purl.uniprot.org/annotation/VSP_029273|||http://purl.uniprot.org/annotation/VSP_029274|||http://purl.uniprot.org/annotation/VSP_029275|||http://purl.uniprot.org/annotation/VSP_029276|||http://purl.uniprot.org/annotation/VSP_029277|||http://purl.uniprot.org/annotation/VSP_029278|||http://purl.uniprot.org/annotation/VSP_029279|||http://purl.uniprot.org/annotation/VSP_045299
http://togogenome.org/gene/9606:FGFBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibroblast growth factor-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244264|||http://purl.uniprot.org/annotation/VAR_026888|||http://purl.uniprot.org/annotation/VAR_059288
http://togogenome.org/gene/9606:FNDC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2H6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Fibronectin type-III domain-containing protein 3A|||Helical|||In isoform 2.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087321|||http://purl.uniprot.org/annotation/VAR_059655|||http://purl.uniprot.org/annotation/VSP_037723|||http://purl.uniprot.org/annotation/VSP_037724
http://togogenome.org/gene/9606:OR6K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFU5|||http://purl.uniprot.org/uniprot/Q8NGY3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6K3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150630|||http://purl.uniprot.org/annotation/VAR_055066|||http://purl.uniprot.org/annotation/VAR_055067|||http://purl.uniprot.org/annotation/VAR_055068|||http://purl.uniprot.org/annotation/VAR_055069|||http://purl.uniprot.org/annotation/VAR_062052|||http://purl.uniprot.org/annotation/VAR_062053|||http://purl.uniprot.org/annotation/VAR_064741
http://togogenome.org/gene/9606:RIPPLY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57055                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Pro residues|||Protein ripply3|||Ripply homology domain|||WRPW motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080020|||http://purl.uniprot.org/annotation/VSP_004205
http://togogenome.org/gene/9606:OPRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZI64|||http://purl.uniprot.org/uniprot/P41146|||http://purl.uniprot.org/uniprot/Q8IXB0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes G protein-mediated inhibition of adenylate cyclase. Abolishes antagonist-mediated inhibition of G protein-mediated signaling.|||Abolishes G protein-mediated inhibition of adenylate cyclase. No effect on antagonist-mediated inhibition of G protein-mediated signaling.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs G protein-mediated inhibition of adenylate cyclase.|||Impairs ligand-mediated internalization.|||Important for G protein-mediated signaling|||In isoform 2.|||Mildly impairs G protein-mediated inhibition of adenylate cyclase. Abolishes antagonist-mediated inhibition of G protein-mediated signaling.|||N-linked (GlcNAc...) asparagine|||No effect on ligand-mediated internalization; when associated with A-337 and A-346.|||No effect on ligand-mediated internalization; when associated with A-337 and A-351.|||No effect on ligand-mediated internalization; when associated with A-346 and A-351.|||Nociceptin receptor|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069980|||http://purl.uniprot.org/annotation/VSP_001897
http://togogenome.org/gene/9606:UTP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TED0                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed|||U3 small nucleolar RNA-associated protein 15 homolog|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051321|||http://purl.uniprot.org/annotation/VAR_057621|||http://purl.uniprot.org/annotation/VAR_057622|||http://purl.uniprot.org/annotation/VAR_057623|||http://purl.uniprot.org/annotation/VSP_055255|||http://purl.uniprot.org/annotation/VSP_055256
http://togogenome.org/gene/9606:FOXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12952|||http://purl.uniprot.org/uniprot/Q498Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein L1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091859
http://togogenome.org/gene/9606:CHRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1Q0|||http://purl.uniprot.org/uniprot/P08172|||http://purl.uniprot.org/uniprot/Q6SL56|||http://purl.uniprot.org/uniprot/Q6SL59|||http://purl.uniprot.org/uniprot/Q86SJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes signaling via downstream effectors.|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for signaling|||Muscarinic acetylcholine receptor M2|||N-linked (GlcNAc...) asparagine|||Nearly abolishes signaling via downstream effectors.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced affinity for acetylcholine. Abolishes signaling via downstream effectors.|||Reduced affinity for acetylcholine. Reduces signaling via downstream effectors.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069021
http://togogenome.org/gene/9606:CST8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDQ4|||http://purl.uniprot.org/uniprot/O60676                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cystatin|||Cystatin-8|||N-linked (GlcNAc...) asparagine|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006653|||http://purl.uniprot.org/annotation/PRO_5035365861|||http://purl.uniprot.org/annotation/VAR_014527|||http://purl.uniprot.org/annotation/VAR_061130
http://togogenome.org/gene/9606:ANGPTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY76                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  ANGPTL4 C-terminal chain|||ANGPTL4 N-terminal chain|||Angiopoietin-related protein 4|||Associated with lower plasma levels of triglyceride and higher levels of HDL cholesterol; strongly reduced inactivation of lipoprotein lipase LPL; no effect on protein secretion and stability of monomers; abolishes accumulation of oligomers.|||Cleavage|||Decreased inactivation of lipoprotein lipase LPL.|||Fibrinogen C-terminal|||Impaired protein folding.|||In isoform 2.|||In isoform 3.|||Loss of inactivation of lipoprotein lipase LPL.|||Loss of proteolytic cleavage.|||Loss of proteolytic cleavage. Decreased ability to inactivate lipoprotein lipase LPL.|||Loss of proteolytic cleavage. No effect on the ability to inactivate lipoprotein lipase LPL.|||N-linked (GlcNAc...) asparagine|||No effect on protein folding.|||No effect on secretion and proteolytic cleavage. Loss of oligomerization; when associated with A-76.|||No effect on secretion and proteolytic cleavage. Loss of oligomerization; when associated with A-80.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009124|||http://purl.uniprot.org/annotation/PRO_0000446859|||http://purl.uniprot.org/annotation/PRO_0000446860|||http://purl.uniprot.org/annotation/VAR_020428|||http://purl.uniprot.org/annotation/VAR_032642|||http://purl.uniprot.org/annotation/VAR_032643|||http://purl.uniprot.org/annotation/VAR_032644|||http://purl.uniprot.org/annotation/VAR_032645|||http://purl.uniprot.org/annotation/VAR_032646|||http://purl.uniprot.org/annotation/VAR_032647|||http://purl.uniprot.org/annotation/VAR_032648|||http://purl.uniprot.org/annotation/VAR_032649|||http://purl.uniprot.org/annotation/VAR_032650|||http://purl.uniprot.org/annotation/VAR_032651|||http://purl.uniprot.org/annotation/VAR_032652|||http://purl.uniprot.org/annotation/VAR_032653|||http://purl.uniprot.org/annotation/VAR_032654|||http://purl.uniprot.org/annotation/VAR_032655|||http://purl.uniprot.org/annotation/VAR_032656|||http://purl.uniprot.org/annotation/VAR_032657|||http://purl.uniprot.org/annotation/VAR_032658|||http://purl.uniprot.org/annotation/VAR_032659|||http://purl.uniprot.org/annotation/VAR_032660|||http://purl.uniprot.org/annotation/VAR_032661|||http://purl.uniprot.org/annotation/VAR_032662|||http://purl.uniprot.org/annotation/VAR_032663|||http://purl.uniprot.org/annotation/VAR_032664|||http://purl.uniprot.org/annotation/VAR_032665|||http://purl.uniprot.org/annotation/VAR_032666|||http://purl.uniprot.org/annotation/VAR_032667|||http://purl.uniprot.org/annotation/VAR_032668|||http://purl.uniprot.org/annotation/VSP_047045|||http://purl.uniprot.org/annotation/VSP_055092
http://togogenome.org/gene/9606:SH2D4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H788                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||SH2|||SH2 domain-containing protein 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233133|||http://purl.uniprot.org/annotation/VAR_026055|||http://purl.uniprot.org/annotation/VAR_026056|||http://purl.uniprot.org/annotation/VAR_051350|||http://purl.uniprot.org/annotation/VAR_051351|||http://purl.uniprot.org/annotation/VSP_042784
http://togogenome.org/gene/9606:ZNF517                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AV05|||http://purl.uniprot.org/uniprot/B7ZLN6|||http://purl.uniprot.org/uniprot/Q6ZMY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 517                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047636|||http://purl.uniprot.org/annotation/VAR_057425
http://togogenome.org/gene/9606:VWC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Brorin|||Disordered|||Mediates cell adhesion|||VWFC 1|||VWFC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307159|||http://purl.uniprot.org/annotation/VAR_035371
http://togogenome.org/gene/9606:GSTK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FII1|||http://purl.uniprot.org/uniprot/Q9Y2Q3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DSBA-like thioredoxin|||Glutathione S-transferase kappa 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185891|||http://purl.uniprot.org/annotation/VSP_040025|||http://purl.uniprot.org/annotation/VSP_040978|||http://purl.uniprot.org/annotation/VSP_040979
http://togogenome.org/gene/9606:CYP2B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20813                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2B6|||In allele CYP2B6*10.|||In allele CYP2B6*11.|||In allele CYP2B6*12.|||In allele CYP2B6*14.|||In allele CYP2B6*15.|||In allele CYP2B6*2 and allele CYP2B6*10.|||In allele CYP2B6*3.|||In allele CYP2B6*4, allele CYP2B6*6, allele CYP2B6*7 and allele CYP2B6*13; slight decrease in activity.|||In allele CYP2B6*5 and allele CYP2B6*7.|||In allele CYP2B6*6, allele CYP2B6*7, allele CYP2B6*9 and allele CYP2B6*13.|||In allele CYP2B6*8 and allele CYP2B6*13.|||In isoform 2.|||Phosphoserine; by PKA|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051683|||http://purl.uniprot.org/annotation/VAR_016924|||http://purl.uniprot.org/annotation/VAR_016925|||http://purl.uniprot.org/annotation/VAR_016926|||http://purl.uniprot.org/annotation/VAR_016927|||http://purl.uniprot.org/annotation/VAR_016928|||http://purl.uniprot.org/annotation/VAR_016929|||http://purl.uniprot.org/annotation/VAR_016948|||http://purl.uniprot.org/annotation/VAR_023563|||http://purl.uniprot.org/annotation/VAR_023564|||http://purl.uniprot.org/annotation/VAR_023565|||http://purl.uniprot.org/annotation/VAR_023566|||http://purl.uniprot.org/annotation/VAR_023567|||http://purl.uniprot.org/annotation/VAR_024716|||http://purl.uniprot.org/annotation/VAR_025206|||http://purl.uniprot.org/annotation/VAR_025207|||http://purl.uniprot.org/annotation/VAR_025208|||http://purl.uniprot.org/annotation/VAR_025209|||http://purl.uniprot.org/annotation/VAR_025210|||http://purl.uniprot.org/annotation/VAR_033819|||http://purl.uniprot.org/annotation/VSP_055571|||http://purl.uniprot.org/annotation/VSP_055572
http://togogenome.org/gene/9606:CMPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EBM0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||UMP-CMP kinase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331524|||http://purl.uniprot.org/annotation/VAR_055997|||http://purl.uniprot.org/annotation/VSP_033238|||http://purl.uniprot.org/annotation/VSP_033239|||http://purl.uniprot.org/annotation/VSP_033240|||http://purl.uniprot.org/annotation/VSP_033241
http://togogenome.org/gene/9606:OTUD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2D3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished deubiquitinase activity.|||Basic and acidic residues|||Cys-loop|||Disordered|||Found in a family with an early age of onset of diabetes; unknown pathological significance; reduced the stability and catalytic activity.|||His-loop|||Impaired activity.|||N6-acetyllysine|||Nucleophile|||OTU|||OTU domain-containing protein 3|||Phosphoserine|||Polar residues|||UBA-like|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058103|||http://purl.uniprot.org/annotation/VAR_051258|||http://purl.uniprot.org/annotation/VAR_051259|||http://purl.uniprot.org/annotation/VAR_087061
http://togogenome.org/gene/9606:PARN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN69|||http://purl.uniprot.org/uniprot/O95453                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In DKCB6.|||In PFBMFT4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with poly(A)|||Loss of activity.|||Loss of dimerization. Loss of activity.|||Loss of function but does not abolish ability to bind RNA.|||Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs.|||Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+).|||Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+).|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Polar residues|||Poly(A)-specific ribonuclease PARN|||Poly(A)-specific ribonuclease RNA-binding|||R3H|||Reduced affinity for poly(A). Little effect on activity.|||Reduced affinity for poly(A). Loss of activity.|||Reduced affinity for poly(A). Strongly reduced activity.|||Strong reduction of phosphorylation by MAPKAPK2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212851|||http://purl.uniprot.org/annotation/VAR_073782|||http://purl.uniprot.org/annotation/VAR_073783|||http://purl.uniprot.org/annotation/VSP_042846|||http://purl.uniprot.org/annotation/VSP_042847|||http://purl.uniprot.org/annotation/VSP_057269
http://togogenome.org/gene/9606:MAP4K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12851                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CNH|||Disordered|||In isoform 2.|||Mitogen-activated protein kinase kinase kinase kinase 2|||PEST1|||PEST2|||PEST3|||Phosphoserine|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086275|||http://purl.uniprot.org/annotation/VSP_054134
http://togogenome.org/gene/9606:SYTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2A9|||http://purl.uniprot.org/uniprot/Q4VX76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Disordered|||In isoform 2.|||Polar residues|||RabBD|||Synaptotagmin-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311116|||http://purl.uniprot.org/annotation/VAR_037137|||http://purl.uniprot.org/annotation/VAR_037138|||http://purl.uniprot.org/annotation/VAR_037139|||http://purl.uniprot.org/annotation/VSP_029403
http://togogenome.org/gene/9606:SERTAD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||SERTA|||SERTA domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191615
http://togogenome.org/gene/9606:BCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAY6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Beta,beta-carotene 15,15'-dioxygenase|||Disordered|||In HCVAD; decreased beta-carotene 15,15'-monooxygenase activity; 90% decrease compared to wild-type; decreased catalytic efficiency; no effect on affinity for all-trans-beta-carotene.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143933|||http://purl.uniprot.org/annotation/VAR_048406|||http://purl.uniprot.org/annotation/VAR_048407|||http://purl.uniprot.org/annotation/VAR_058112
http://togogenome.org/gene/9606:NQO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPX6|||http://purl.uniprot.org/uniprot/P16083|||http://purl.uniprot.org/uniprot/Q5TD07                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Flavodoxin-like fold|||Loss of activity toward CB1954, no effect toward menadione.|||Phosphoserine|||Ribosyldihydronicotinamide dehydrogenase [quinone]                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071626|||http://purl.uniprot.org/annotation/VAR_021399|||http://purl.uniprot.org/annotation/VAR_021400|||http://purl.uniprot.org/annotation/VAR_021401|||http://purl.uniprot.org/annotation/VAR_021402|||http://purl.uniprot.org/annotation/VAR_021403
http://togogenome.org/gene/9606:MBLAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY36|||http://purl.uniprot.org/uniprot/Q68D91                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase MBLAC2|||In isoform 2.|||Loss of ZDHH20-catalyzed palmitoylation. Shows only a slight reduction in the Vmax and a small increase in the Km towards palmitoyl-CoA in comparison with wild-type.|||Loss of enzyme activity.|||Metallo-beta-lactamase|||N-acetylserine|||No effect on ZDHH20-catalyzed palmitoylation.|||No effect on enzyme activity.|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325935|||http://purl.uniprot.org/annotation/VAR_039956|||http://purl.uniprot.org/annotation/VSP_032490
http://togogenome.org/gene/9606:C1QTNF9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Complement C1q and tumor necrosis factor-related protein 9B|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348424|||http://purl.uniprot.org/annotation/VSP_035153|||http://purl.uniprot.org/annotation/VSP_035154
http://togogenome.org/gene/9606:SPA17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A172Q397|||http://purl.uniprot.org/uniprot/Q15506                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||IQ|||RIIa|||Sperm surface protein Sp17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181340
http://togogenome.org/gene/9606:PTGFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43088                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Prostaglandin F2-alpha receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070070|||http://purl.uniprot.org/annotation/VSP_042025|||http://purl.uniprot.org/annotation/VSP_053588|||http://purl.uniprot.org/annotation/VSP_053589|||http://purl.uniprot.org/annotation/VSP_053590|||http://purl.uniprot.org/annotation/VSP_053591|||http://purl.uniprot.org/annotation/VSP_053592|||http://purl.uniprot.org/annotation/VSP_053593|||http://purl.uniprot.org/annotation/VSP_053594|||http://purl.uniprot.org/annotation/VSP_053595|||http://purl.uniprot.org/annotation/VSP_053596|||http://purl.uniprot.org/annotation/VSP_053597
http://togogenome.org/gene/9606:TNFAIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03169                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Tumor necrosis factor alpha-induced protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118932|||http://purl.uniprot.org/annotation/VAR_020772|||http://purl.uniprot.org/annotation/VAR_020773|||http://purl.uniprot.org/annotation/VAR_020774|||http://purl.uniprot.org/annotation/VAR_038742
http://togogenome.org/gene/9606:ANXA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76027                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067505|||http://purl.uniprot.org/annotation/VAR_022814|||http://purl.uniprot.org/annotation/VAR_031212|||http://purl.uniprot.org/annotation/VAR_048255|||http://purl.uniprot.org/annotation/VAR_048256|||http://purl.uniprot.org/annotation/VAR_048257|||http://purl.uniprot.org/annotation/VAR_048258
http://togogenome.org/gene/9606:ZNF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17017                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047337|||http://purl.uniprot.org/annotation/VAR_054791|||http://purl.uniprot.org/annotation/VAR_057381
http://togogenome.org/gene/9606:CACTIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUQ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Splicing factor Cactin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231617|||http://purl.uniprot.org/annotation/VSP_017856
http://togogenome.org/gene/9606:CELF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5EA30|||http://purl.uniprot.org/uniprot/Q92879                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUGBP Elav-like family member 1|||Disordered|||Does not reduce RNA-binding; when associated with D-331 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472.|||Does not reduce RNA-binding; when associated with L-63 and D-331. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472.|||Does not reduce RNA-binding; when associated with L-63 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081538|||http://purl.uniprot.org/annotation/VSP_005784|||http://purl.uniprot.org/annotation/VSP_005785|||http://purl.uniprot.org/annotation/VSP_026787|||http://purl.uniprot.org/annotation/VSP_026788|||http://purl.uniprot.org/annotation/VSP_045043
http://togogenome.org/gene/9606:MS4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HJ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Membrane-spanning 4-domains subfamily A member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158632|||http://purl.uniprot.org/annotation/VSP_007109|||http://purl.uniprot.org/annotation/VSP_045798
http://togogenome.org/gene/9606:RNF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99496                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Decreases ubiquitin ligase activity on histone H2A.|||Disordered|||E3 ubiquitin-protein ligase RING2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In LUSYAM.|||In LUSYAM; unknown pathological significance.|||In isoform 2.|||Interaction with HIP2|||Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B|||Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A.|||Loss of ubiquitin ligase activity on histone H2A.|||Mildly decreases ubiquitin ligase activity on histone H2A.|||N-acetylserine|||Nearly abolishes ubiquitin ligase activity on histone H2A.|||No effect on ubiquitin ligase activity on histone H2A.|||Phosphoserine|||Polar residues|||RING-type|||Reduced interaction with CBX7.|||Removed|||Strong decrease in HIP2-binding; when associated with S-54.|||Strong decrease in HIP2-binding; when associated with W-51.|||Strongly decreases ubiquitin ligase activity on histone H2A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056038|||http://purl.uniprot.org/annotation/VAR_086207|||http://purl.uniprot.org/annotation/VAR_086208|||http://purl.uniprot.org/annotation/VSP_055439
http://togogenome.org/gene/9606:HES7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SCDO4.|||In isoform 2.|||Orange|||Pro residues|||Transcription factor HES-7|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252422|||http://purl.uniprot.org/annotation/VAR_064921|||http://purl.uniprot.org/annotation/VAR_064922|||http://purl.uniprot.org/annotation/VAR_064923|||http://purl.uniprot.org/annotation/VSP_047334
http://togogenome.org/gene/9606:TNFRSF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07011                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In IMD109; unknown pathological significance; contrary to wild-type, undetectable in patient's stimulated peripheral blood mononuclear cells; patient's cells show defective expansion, reduced expression of IFNG and perforin/PRF1 and impaired allospecific and EBV-specific cytotoxic activity, as well as reduced mitochondrial function.|||In a colorectal cancer sample; somatic mutation.|||Interaction with LRR-1|||N-linked (GlcNAc...) asparagine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034577|||http://purl.uniprot.org/annotation/VAR_018920|||http://purl.uniprot.org/annotation/VAR_018921|||http://purl.uniprot.org/annotation/VAR_018922|||http://purl.uniprot.org/annotation/VAR_035478|||http://purl.uniprot.org/annotation/VAR_088225
http://togogenome.org/gene/9606:GPR87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY21                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 87|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069595|||http://purl.uniprot.org/annotation/VAR_035760|||http://purl.uniprot.org/annotation/VAR_055921
http://togogenome.org/gene/9606:DYSF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75923                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Cytoplasmic|||Disordered|||Dysferlin|||Extracellular|||Fails to bind calcium.|||Found in patients with isolated hyperCKemia.|||Helical|||In LGMDR2 and MMD1; also found in patients with isolated hyperCKemia.|||In LGMDR2 and proximodistal myopathy.|||In LGMDR2 and proximodistal myopathy; unknown pathological significance.|||In LGMDR2.|||In LGMDR2; unknown pathological significance.|||In MMD1 and LGMDR2.|||In MMD1 and LGMDR2; Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2.|||In MMD1, LGMDR2 and proximodistal myopathy.|||In MMD1.|||In MMD1; dbNP:28939700.|||In a breast cancer sample; somatic mutation.|||In isoform 15.|||In isoform 2, isoform 5, isoform 7, isoform 8, isoform 11 and isoform 13.|||In isoform 3, isoform 5, isoform 6, isoform 7, isoform 9, isoform 11, isoform 12, isoform 13 and isoform 15.|||In isoform 4, isoform 6, isoform 7, isoform 10, isoform 12 and isoform 13.|||In isoform 8, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13 and isoform 14.|||In proximodistal myopathy.|||In pseudometabolic myopathy.|||Moderately increased calcium affinity.|||Phosphoserine|||Phosphothreonine|||Reduced calcium affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057879|||http://purl.uniprot.org/annotation/VAR_012308|||http://purl.uniprot.org/annotation/VAR_012309|||http://purl.uniprot.org/annotation/VAR_012310|||http://purl.uniprot.org/annotation/VAR_012311|||http://purl.uniprot.org/annotation/VAR_020308|||http://purl.uniprot.org/annotation/VAR_024853|||http://purl.uniprot.org/annotation/VAR_024854|||http://purl.uniprot.org/annotation/VAR_024855|||http://purl.uniprot.org/annotation/VAR_024856|||http://purl.uniprot.org/annotation/VAR_024857|||http://purl.uniprot.org/annotation/VAR_024858|||http://purl.uniprot.org/annotation/VAR_024859|||http://purl.uniprot.org/annotation/VAR_024860|||http://purl.uniprot.org/annotation/VAR_024861|||http://purl.uniprot.org/annotation/VAR_024862|||http://purl.uniprot.org/annotation/VAR_024863|||http://purl.uniprot.org/annotation/VAR_024864|||http://purl.uniprot.org/annotation/VAR_024865|||http://purl.uniprot.org/annotation/VAR_024866|||http://purl.uniprot.org/annotation/VAR_024867|||http://purl.uniprot.org/annotation/VAR_024868|||http://purl.uniprot.org/annotation/VAR_024869|||http://purl.uniprot.org/annotation/VAR_024870|||http://purl.uniprot.org/annotation/VAR_024871|||http://purl.uniprot.org/annotation/VAR_024872|||http://purl.uniprot.org/annotation/VAR_035893|||http://purl.uniprot.org/annotation/VAR_035894|||http://purl.uniprot.org/annotation/VAR_049055|||http://purl.uniprot.org/annotation/VAR_049056|||http://purl.uniprot.org/annotation/VAR_057834|||http://purl.uniprot.org/annotation/VAR_057835|||http://purl.uniprot.org/annotation/VAR_057836|||http://purl.uniprot.org/annotation/VAR_057837|||http://purl.uniprot.org/annotation/VAR_057838|||http://purl.uniprot.org/annotation/VAR_057839|||http://purl.uniprot.org/annotation/VAR_057840|||http://purl.uniprot.org/annotation/VAR_057841|||http://purl.uniprot.org/annotation/VAR_057842|||http://purl.uniprot.org/annotation/VAR_057843|||http://purl.uniprot.org/annotation/VAR_057844|||http://purl.uniprot.org/annotation/VAR_057845|||http://purl.uniprot.org/annotation/VAR_057846|||http://purl.uniprot.org/annotation/VAR_057847|||http://purl.uniprot.org/annotation/VAR_057848|||http://purl.uniprot.org/annotation/VAR_057849|||http://purl.uniprot.org/annotation/VAR_057850|||http://purl.uniprot.org/annotation/VAR_057851|||http://purl.uniprot.org/annotation/VAR_057852|||http://purl.uniprot.org/annotation/VAR_057853|||http://purl.uniprot.org/annotation/VAR_057854|||http://purl.uniprot.org/annotation/VAR_057855|||http://purl.uniprot.org/annotation/VAR_057856|||http://purl.uniprot.org/annotation/VAR_057857|||http://purl.uniprot.org/annotation/VAR_057858|||http://purl.uniprot.org/annotation/VAR_057859|||http://purl.uniprot.org/annotation/VAR_057860|||http://purl.uniprot.org/annotation/VAR_057861|||http://purl.uniprot.org/annotation/VAR_057862|||http://purl.uniprot.org/annotation/VAR_057863|||http://purl.uniprot.org/annotation/VAR_057864|||http://purl.uniprot.org/annotation/VAR_057865|||http://purl.uniprot.org/annotation/VAR_057866|||http://purl.uniprot.org/annotation/VAR_057867|||http://purl.uniprot.org/annotation/VAR_057868|||http://purl.uniprot.org/annotation/VAR_057869|||http://purl.uniprot.org/annotation/VAR_057870|||http://purl.uniprot.org/annotation/VAR_057871|||http://purl.uniprot.org/annotation/VAR_057872|||http://purl.uniprot.org/annotation/VAR_057873|||http://purl.uniprot.org/annotation/VAR_057874|||http://purl.uniprot.org/annotation/VAR_057875|||http://purl.uniprot.org/annotation/VAR_057876|||http://purl.uniprot.org/annotation/VAR_057877|||http://purl.uniprot.org/annotation/VAR_057878|||http://purl.uniprot.org/annotation/VAR_057879|||http://purl.uniprot.org/annotation/VAR_057880|||http://purl.uniprot.org/annotation/VAR_057881|||http://purl.uniprot.org/annotation/VAR_061170|||http://purl.uniprot.org/annotation/VSP_035924|||http://purl.uniprot.org/annotation/VSP_035925|||http://purl.uniprot.org/annotation/VSP_035926|||http://purl.uniprot.org/annotation/VSP_035927|||http://purl.uniprot.org/annotation/VSP_035928|||http://purl.uniprot.org/annotation/VSP_035929
http://togogenome.org/gene/9606:LRP2BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2M1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRP2-binding protein|||Sel1-like 1|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5|||Sel1-like 6|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315707|||http://purl.uniprot.org/annotation/VSP_030664
http://togogenome.org/gene/9606:ABHD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2K0                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||In PHARC.|||In PHARC; abolished monoacyglycerol lipase activity.|||In PHARC; unknown pathological significance.|||In PHARC; unknown pathological significance; abolished monoacyglycerol lipase activity.|||In isoform 2.|||In isoform 3.|||Loss of 2-arachidonoyglycerol hydrolase activity.|||Loss of lipase activity.|||Lysophosphatidylserine lipase ABHD12|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079413|||http://purl.uniprot.org/annotation/VAR_050630|||http://purl.uniprot.org/annotation/VAR_081587|||http://purl.uniprot.org/annotation/VAR_081588|||http://purl.uniprot.org/annotation/VAR_081589|||http://purl.uniprot.org/annotation/VAR_081590|||http://purl.uniprot.org/annotation/VAR_081591|||http://purl.uniprot.org/annotation/VAR_081592|||http://purl.uniprot.org/annotation/VAR_081593|||http://purl.uniprot.org/annotation/VAR_081594|||http://purl.uniprot.org/annotation/VSP_009097|||http://purl.uniprot.org/annotation/VSP_037372
http://togogenome.org/gene/9606:DHRS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTZ2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.|||Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.|||Dehydrogenase/reductase SDR family member 4|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal targeting signal|||Phosphoserine|||Proton acceptor|||Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054647|||http://purl.uniprot.org/annotation/VAR_057272|||http://purl.uniprot.org/annotation/VAR_061846|||http://purl.uniprot.org/annotation/VSP_008585|||http://purl.uniprot.org/annotation/VSP_008586|||http://purl.uniprot.org/annotation/VSP_031435|||http://purl.uniprot.org/annotation/VSP_031436|||http://purl.uniprot.org/annotation/VSP_031437|||http://purl.uniprot.org/annotation/VSP_031438|||http://purl.uniprot.org/annotation/VSP_031439|||http://purl.uniprot.org/annotation/VSP_044947
http://togogenome.org/gene/9606:EIF3I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13347|||http://purl.uniprot.org/uniprot/Q5U0F4                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Crosslink|||Mass|||Modified Residue|||Repeat                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 3 subunit I|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051036
http://togogenome.org/gene/9606:NCAPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMS0|||http://purl.uniprot.org/uniprot/B3KY03|||http://purl.uniprot.org/uniprot/Q15021                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes localization to the nucleus, while it only reduces chromosome binding.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Condensin complex subunit 1|||Condensin complex subunit 1 C-terminal|||Condensin complex subunit 1 N-terminal|||Disordered|||In MCPH21; found in two patients from a consanguineous family; unknown pathological significance.|||Interactions with SMC2 and SMC4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095035|||http://purl.uniprot.org/annotation/VAR_024421|||http://purl.uniprot.org/annotation/VAR_024422|||http://purl.uniprot.org/annotation/VAR_057511|||http://purl.uniprot.org/annotation/VAR_058713|||http://purl.uniprot.org/annotation/VAR_080953
http://togogenome.org/gene/9606:ANKRD44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6Z7|||http://purl.uniprot.org/uniprot/Q8N8A2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 26|||ANK 27|||ANK 28|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244572|||http://purl.uniprot.org/annotation/VSP_019600|||http://purl.uniprot.org/annotation/VSP_019601|||http://purl.uniprot.org/annotation/VSP_019602|||http://purl.uniprot.org/annotation/VSP_019603|||http://purl.uniprot.org/annotation/VSP_019604|||http://purl.uniprot.org/annotation/VSP_035965|||http://purl.uniprot.org/annotation/VSP_035966
http://togogenome.org/gene/9606:OR13C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWR7|||http://purl.uniprot.org/uniprot/Q8NGS9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150731|||http://purl.uniprot.org/annotation/VAR_060030|||http://purl.uniprot.org/annotation/VAR_060031
http://togogenome.org/gene/9606:ARHGAP26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z536|||http://purl.uniprot.org/uniprot/Q9UNA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In JMML; somatic mutation.|||In isoform 2.|||PH|||Polar residues|||Pro residues|||Rho GTPase-activating protein 26|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056718|||http://purl.uniprot.org/annotation/VAR_013623|||http://purl.uniprot.org/annotation/VSP_001659
http://togogenome.org/gene/9606:KCNA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22460                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||2 X 11 AA tandem repeat of D-[SP]-G-V-R-P-L-P-P-L-P|||Abolishes sumoylation; when associated with R-221.|||Abolishes sumoylation; when associated with R-536.|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with pulmonary arterial hypertension; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of DLG1 effect on channel current.|||PDZ-binding|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 5|||Pro residues|||Reduces sumoylation; when associated with N-220.|||Reduces sumoylation; when associated with N-535.|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053985|||http://purl.uniprot.org/annotation/VAR_035770|||http://purl.uniprot.org/annotation/VAR_053856|||http://purl.uniprot.org/annotation/VAR_054786|||http://purl.uniprot.org/annotation/VAR_079602|||http://purl.uniprot.org/annotation/VAR_079603|||http://purl.uniprot.org/annotation/VAR_079604|||http://purl.uniprot.org/annotation/VAR_079605|||http://purl.uniprot.org/annotation/VAR_079606|||http://purl.uniprot.org/annotation/VSP_037110
http://togogenome.org/gene/9606:ETS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K725|||http://purl.uniprot.org/uniprot/B4DW78|||http://purl.uniprot.org/uniprot/P14921                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation domain; required for transcription activation|||Disordered|||ETS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helix H4|||Helix H5|||Helix HI-1|||Helix HI-2|||In isoform 3.|||In isoform 5.|||In isoform Ets-1 p27.|||In isoform c-ETS-1B.|||N6-acetyllysine|||N6-acetyllysine; alternate|||PNT|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK|||Phosphotyrosine|||Protein C-ets-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204069|||http://purl.uniprot.org/annotation/VSP_001464|||http://purl.uniprot.org/annotation/VSP_043152|||http://purl.uniprot.org/annotation/VSP_046056|||http://purl.uniprot.org/annotation/VSP_055485|||http://purl.uniprot.org/annotation/VSP_055486
http://togogenome.org/gene/9606:ZNHIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43257                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HIT-type|||Impairs the p38 MAPK-mediated phosphorylation of ZNHIT1.|||In a colorectal cancer sample; somatic mutation.|||Interaction with NR1D2|||No change in the in vitro MAPK14/MAPK11-induced phosphorylation level of ZNHIT1.|||Nuclear localization signal|||Phosphothreonine; by MAPK11 and MAPK14|||Zinc finger HIT domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173546|||http://purl.uniprot.org/annotation/VAR_035719
http://togogenome.org/gene/9606:LRIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T3J3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with HP1 (CBX1/HP1-beta, CBX3/HP1-gamma and CBX5/HP1-alpha).|||Abolishes nuclear localization.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Ligand-dependent nuclear receptor-interacting factor 1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||PxVxL motif|||Slightly reduces nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250686|||http://purl.uniprot.org/annotation/VAR_027599|||http://purl.uniprot.org/annotation/VAR_027600|||http://purl.uniprot.org/annotation/VAR_050703|||http://purl.uniprot.org/annotation/VSP_020721
http://togogenome.org/gene/9606:TRAPPC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z392                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with congenital disorder of glycosylation; unknown pathological significance.|||In LGMDR18.|||In LGMDR18; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||N6-acetyllysine|||Trafficking protein particle complex subunit 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348072|||http://purl.uniprot.org/annotation/VAR_070158|||http://purl.uniprot.org/annotation/VAR_078126|||http://purl.uniprot.org/annotation/VAR_078127|||http://purl.uniprot.org/annotation/VAR_087914|||http://purl.uniprot.org/annotation/VSP_035095|||http://purl.uniprot.org/annotation/VSP_035096|||http://purl.uniprot.org/annotation/VSP_035097|||http://purl.uniprot.org/annotation/VSP_035098|||http://purl.uniprot.org/annotation/VSP_035099
http://togogenome.org/gene/9606:PDCD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14737                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Programmed cell death protein 5|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121545|||http://purl.uniprot.org/annotation/VSP_056203
http://togogenome.org/gene/9606:ZNF341                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504V9|||http://purl.uniprot.org/uniprot/Q9BYN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In HIES3; absence of the full-length protein in patient cells; loss of function in transcriptional STAT3 activation; loss of DNA binding; does not localize to the nucleus.|||In HIES3; absence of the full-length protein in patient cells; results in weak DNA binding in vitro; does not affect localization to the nucleus.|||In HIES3; decreased function in transcriptional STAT3 activation; severly reduced DNA binding in vitro; does not affect nuclear localization.|||In HIES3; does not localize to the nucleus.|||In isoform 2.|||Pro residues|||Zinc finger protein 341                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047541|||http://purl.uniprot.org/annotation/VAR_081880|||http://purl.uniprot.org/annotation/VAR_081881|||http://purl.uniprot.org/annotation/VAR_081882|||http://purl.uniprot.org/annotation/VAR_081883|||http://purl.uniprot.org/annotation/VSP_027218
http://togogenome.org/gene/9606:PGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJD8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Pepsin A-3|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026013|||http://purl.uniprot.org/annotation/PRO_0000026014
http://togogenome.org/gene/9606:LTC4S                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16873                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect leukotriene-C4 synthase activity but substantially increased KM for GSH.|||Helical|||Leukotriene C4 synthase|||Leukotriene-C4 synthaseactivity is reduced by 30%.|||Loss of leukotriene-C4 synthase activity.|||Lumenal|||Phosphoserine; by RPS6KB1|||Proton acceptor|||Proton donor|||Reduced leukotriene-C4 synthase activity by nearly 80%.|||Reduces Leukotriene-C4 synthase activity and increases the optimum for pH-dependent activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217748|||http://purl.uniprot.org/annotation/VAR_042736
http://togogenome.org/gene/9606:SLC7A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCU3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Solute carrier family 7 member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330725|||http://purl.uniprot.org/annotation/VAR_042716|||http://purl.uniprot.org/annotation/VAR_042717|||http://purl.uniprot.org/annotation/VAR_042718|||http://purl.uniprot.org/annotation/VAR_042719|||http://purl.uniprot.org/annotation/VSP_033067|||http://purl.uniprot.org/annotation/VSP_033068|||http://purl.uniprot.org/annotation/VSP_033069
http://togogenome.org/gene/9606:SCNM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In OFD19; the genetic variation producing this missense variant predominantly affects splicing and the resulting mRNA is predicted to undergo nonsense-mediated mRNA decay.|||In isoform 2.|||In isoform 3.|||Matrin-type|||Phosphoserine|||Required for interaction with LUC7L2|||Sodium channel modifier 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259635|||http://purl.uniprot.org/annotation/VAR_087730|||http://purl.uniprot.org/annotation/VSP_021489|||http://purl.uniprot.org/annotation/VSP_053982|||http://purl.uniprot.org/annotation/VSP_053983
http://togogenome.org/gene/9606:TRIM64                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 64                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331574
http://togogenome.org/gene/9606:CNTNAP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein-like 3B|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||In isoform 2.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339353|||http://purl.uniprot.org/annotation/VSP_034153|||http://purl.uniprot.org/annotation/VSP_034154|||http://purl.uniprot.org/annotation/VSP_034155|||http://purl.uniprot.org/annotation/VSP_034156
http://togogenome.org/gene/9606:CAPN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNR4|||http://purl.uniprot.org/uniprot/E7ESS6|||http://purl.uniprot.org/uniprot/O14815|||http://purl.uniprot.org/uniprot/Q6PIV8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-9|||Disordered|||Domain III|||Domain IV|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207722|||http://purl.uniprot.org/annotation/VAR_022188|||http://purl.uniprot.org/annotation/VAR_022189|||http://purl.uniprot.org/annotation/VAR_022190|||http://purl.uniprot.org/annotation/VAR_022191|||http://purl.uniprot.org/annotation/VAR_022192|||http://purl.uniprot.org/annotation/VAR_022193|||http://purl.uniprot.org/annotation/VAR_022194|||http://purl.uniprot.org/annotation/VAR_022195|||http://purl.uniprot.org/annotation/VAR_022196|||http://purl.uniprot.org/annotation/VAR_022197|||http://purl.uniprot.org/annotation/VAR_022198|||http://purl.uniprot.org/annotation/VAR_022199|||http://purl.uniprot.org/annotation/VSP_007553
http://togogenome.org/gene/9606:SRBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5C6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Phosphoserine|||Polar residues|||S1 RNA-binding domain-containing protein 1|||S1 motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284357|||http://purl.uniprot.org/annotation/VAR_056995|||http://purl.uniprot.org/annotation/VAR_056996|||http://purl.uniprot.org/annotation/VAR_056997|||http://purl.uniprot.org/annotation/VSP_024461
http://togogenome.org/gene/9606:SMG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPR3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes stimulation of RENT1 dephosphorylation.|||Basic and acidic residues|||Disordered|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG5|||PINc|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076322|||http://purl.uniprot.org/annotation/VAR_030828
http://togogenome.org/gene/9606:NAA40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UY6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5 times reduced N-alpha-acetyltransferase activity.|||Abolished N-alpha-acetyltransferase activity.|||Does not affect N-alpha-acetyltransferase activity.|||Essential for catalytic activity|||In isoform 2.|||In isoform 3.|||N-acetyltransferase|||N-alpha-acetyltransferase 40|||N-myristoyl glycine|||Reduced N-alpha-acetyltransferase activity.|||Removed|||Slightly reduced N-alpha-acetyltransferase activity.|||Strongly reduced N-alpha-acetyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284897|||http://purl.uniprot.org/annotation/VSP_054273|||http://purl.uniprot.org/annotation/VSP_054274
http://togogenome.org/gene/9606:HSPA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11142|||http://purl.uniprot.org/uniprot/Q53HF2|||http://purl.uniprot.org/uniprot/V9HW22                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of in vitro methylation by METTL21A.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heat shock cognate 71 kDa protein|||In isoform 2.|||Interaction with BAG1|||N-acetylserine|||N6,N6,N6-trimethyllysine; by METTL21A; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Nucleotide-binding domain (NBD)|||Omega-N-methylarginine|||Phosphoserine|||Removed|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078270|||http://purl.uniprot.org/annotation/VAR_049619|||http://purl.uniprot.org/annotation/VAR_049620|||http://purl.uniprot.org/annotation/VSP_002427
http://togogenome.org/gene/9606:SCGB2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75556                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mass|||Signal Peptide                                                                                  ^@                                                                                  Mammaglobin-B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036373
http://togogenome.org/gene/9606:ZCWPW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504Y3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CW-type|||Disordered|||Little effect on histone H3K4me3 binding.|||Loss of histone H3K4me3 binding.|||Loss of histone H3K4me3 binding; when associated with F-41.|||PWWP|||Reduced histone H3K4me3 binding.|||Significantly reduced histone H3K4me3 binding.|||Significantly reduced histone H3K4me3 binding. Loss of histone H3K4me3 binding; when associated with L-30 or M-30.|||Zinc finger CW-type PWWP domain protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286348|||http://purl.uniprot.org/annotation/VAR_051499
http://togogenome.org/gene/9606:CDHR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8M9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin-related family member 4|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319973|||http://purl.uniprot.org/annotation/VAR_039109|||http://purl.uniprot.org/annotation/VSP_031552|||http://purl.uniprot.org/annotation/VSP_031553
http://togogenome.org/gene/9606:CT45A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMU7|||http://purl.uniprot.org/uniprot/P0DMU8|||http://purl.uniprot.org/uniprot/P0DMV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A5|||Cancer/testis antigen family 45 member A6|||Cancer/testis antigen family 45 member A7|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308950|||http://purl.uniprot.org/annotation/PRO_0000433029|||http://purl.uniprot.org/annotation/PRO_0000433117
http://togogenome.org/gene/9606:HAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2N2G5|||http://purl.uniprot.org/uniprot/G3V1S7|||http://purl.uniprot.org/uniprot/Q8IYH3|||http://purl.uniprot.org/uniprot/Q92839                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hyaluronan synthase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197169|||http://purl.uniprot.org/annotation/VAR_047025
http://togogenome.org/gene/9606:GBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRX0|||http://purl.uniprot.org/uniprot/B4E1U2|||http://purl.uniprot.org/uniprot/Q6ZN66                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 6|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313811|||http://purl.uniprot.org/annotation/VAR_037750|||http://purl.uniprot.org/annotation/VAR_037751|||http://purl.uniprot.org/annotation/VAR_037752|||http://purl.uniprot.org/annotation/VAR_037753|||http://purl.uniprot.org/annotation/VAR_037754|||http://purl.uniprot.org/annotation/VSP_030155
http://togogenome.org/gene/9606:RGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCS9|||http://purl.uniprot.org/uniprot/O15211                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Ral guanine nucleotide dissociation stimulator-like 2|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068888|||http://purl.uniprot.org/annotation/VAR_051903|||http://purl.uniprot.org/annotation/VAR_051904|||http://purl.uniprot.org/annotation/VSP_055847|||http://purl.uniprot.org/annotation/VSP_055848|||http://purl.uniprot.org/annotation/VSP_055849
http://togogenome.org/gene/9606:KMT2E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZD2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with HCFC1.|||Basic and acidic residues|||Basic residues|||Disordered|||Fails to activate the cell cycle regulated element (CCRE) in the cyclin A promoter.|||HCFC1-binding motif (HBM)|||In ODLURO.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform NKp44L.|||Inactive histone-lysine N-methyltransferase 2E|||Loss of binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3).|||No effect on binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3).|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PHD-type|||Phosphoserine|||Polar residues|||Pro residues|||SET|||Severe reduction in the binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341419|||http://purl.uniprot.org/annotation/VAR_052656|||http://purl.uniprot.org/annotation/VAR_083126|||http://purl.uniprot.org/annotation/VAR_083127|||http://purl.uniprot.org/annotation/VAR_083128|||http://purl.uniprot.org/annotation/VAR_083129|||http://purl.uniprot.org/annotation/VAR_083130|||http://purl.uniprot.org/annotation/VAR_083131|||http://purl.uniprot.org/annotation/VAR_083132|||http://purl.uniprot.org/annotation/VAR_083133|||http://purl.uniprot.org/annotation/VAR_083134|||http://purl.uniprot.org/annotation/VAR_083135|||http://purl.uniprot.org/annotation/VAR_083136|||http://purl.uniprot.org/annotation/VAR_083137|||http://purl.uniprot.org/annotation/VSP_052803|||http://purl.uniprot.org/annotation/VSP_052804|||http://purl.uniprot.org/annotation/VSP_052805|||http://purl.uniprot.org/annotation/VSP_052806|||http://purl.uniprot.org/annotation/VSP_052807|||http://purl.uniprot.org/annotation/VSP_052808|||http://purl.uniprot.org/annotation/VSP_052809|||http://purl.uniprot.org/annotation/VSP_052810|||http://purl.uniprot.org/annotation/VSP_052811|||http://purl.uniprot.org/annotation/VSP_052812|||http://purl.uniprot.org/annotation/VSP_053834|||http://purl.uniprot.org/annotation/VSP_053835
http://togogenome.org/gene/9606:FANCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15287                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Fanconi anemia group G protein|||In FANCG; associated with a mild clinical phenotype; disruption of HES1-binding; no effect on FANCA-binding.|||In a colorectal cancer sample; somatic mutation.|||Loss of BRCA2-, FANCD2- and XRCC3-binding. No effect on complex formation with FANCA and FANCF.|||No effect on BRCA2-, FANCA-, FANCF-, nor XRCC3-binding.|||No effect on HES1-, nor FANCA-binding.|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106292|||http://purl.uniprot.org/annotation/VAR_017495|||http://purl.uniprot.org/annotation/VAR_020311|||http://purl.uniprot.org/annotation/VAR_021103|||http://purl.uniprot.org/annotation/VAR_021104|||http://purl.uniprot.org/annotation/VAR_021105|||http://purl.uniprot.org/annotation/VAR_021106|||http://purl.uniprot.org/annotation/VAR_021107|||http://purl.uniprot.org/annotation/VAR_021108|||http://purl.uniprot.org/annotation/VAR_035864
http://togogenome.org/gene/9606:NASP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49321|||http://purl.uniprot.org/uniprot/Q5T626                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Histone-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Nuclear autoantigenic sperm protein|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||TPR|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide SHNi-TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106299|||http://purl.uniprot.org/annotation/VAR_052619|||http://purl.uniprot.org/annotation/VSP_006551|||http://purl.uniprot.org/annotation/VSP_036616|||http://purl.uniprot.org/annotation/VSP_047028
http://togogenome.org/gene/9606:SERPINB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GU38|||http://purl.uniprot.org/uniprot/P50452                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Reactive bond|||Serpin|||Serpin B8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094111|||http://purl.uniprot.org/annotation/VAR_047110|||http://purl.uniprot.org/annotation/VAR_047111|||http://purl.uniprot.org/annotation/VAR_051947|||http://purl.uniprot.org/annotation/VAR_051948|||http://purl.uniprot.org/annotation/VSP_043097|||http://purl.uniprot.org/annotation/VSP_055135
http://togogenome.org/gene/9606:EPS15L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 3 AA repeats of D-P-F|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EH 1|||EH 2|||EH 3|||Epidermal growth factor receptor substrate 15-like 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with DAB2|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146118|||http://purl.uniprot.org/annotation/VSP_042200|||http://purl.uniprot.org/annotation/VSP_045429|||http://purl.uniprot.org/annotation/VSP_046904|||http://purl.uniprot.org/annotation/VSP_046905
http://togogenome.org/gene/9606:ZNF740                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Zinc finger protein 740                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251401
http://togogenome.org/gene/9606:ASPRV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53RT3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes production of active form of enzyme.|||Cytoplasmic|||Extracellular|||Helical|||In ADLI; impairs filaggrin cleavage.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase A2|||Retroviral-like aspartic protease 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271170|||http://purl.uniprot.org/annotation/PRO_0000271171|||http://purl.uniprot.org/annotation/PRO_0000271172|||http://purl.uniprot.org/annotation/VAR_051508|||http://purl.uniprot.org/annotation/VAR_084554|||http://purl.uniprot.org/annotation/VAR_084555|||http://purl.uniprot.org/annotation/VAR_084556|||http://purl.uniprot.org/annotation/VSP_061434
http://togogenome.org/gene/9606:PDHX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8C8MSB2|||http://purl.uniprot.org/uniprot/O00330                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Decreased DLD binding.|||Decreased interaction with DLD.|||Disordered|||In isoform 2.|||In isoform 3.|||Lipoyl-binding|||Mitochondrion|||Moderately decreased interaction with DLD.|||N6-acetyllysine|||N6-lipoyllysine|||N6-succinyllysine|||Peripheral subunit-binding (PSBD)|||Phosphoserine|||Pro residues|||Pyruvate dehydrogenase protein X component, mitochondrial|||Strongly decreased DLD binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020484|||http://purl.uniprot.org/annotation/VAR_046619|||http://purl.uniprot.org/annotation/VAR_046620|||http://purl.uniprot.org/annotation/VAR_046621|||http://purl.uniprot.org/annotation/VSP_045271|||http://purl.uniprot.org/annotation/VSP_053817
http://togogenome.org/gene/9606:MAD2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13257                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-195.|||Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-178 and D-195.|||Abolishes phosphorylation on serine residues; when associated with A-170 and A-178.|||Binds to the N and C-terminus of MAD1L1. Abolishes interaction with MAD1L1 and reduces interaction with CDC20; when associated with D-170 and D-178.|||HORMA|||In isoform 2.|||Leads to formation of the closed conformation; when associated with A-133.|||Leads to formation the closed conformation and homodimerization. Reduces binding to MAD1L1.|||Mitotic spindle assembly checkpoint protein MAD2A|||N-acetylalanine|||Phosphoserine|||Prevents aggregation and promotes formation of monomeric protein that slowly interconverts between the open and closed conformation.|||Prevents formation of the closed conformation and interaction with CDC20; when associated with A-133.|||Prevents interaction with CDC20 and leads to formation of the closed conformation; when associated with A-133.|||Reduces phosphorylation on serine residues; when associated with A-170. Abolishes phosphorylation on serine residues; when associated with A-170 and A-195.|||Reduces phosphorylation on serine residues; when associated with A-178. Abolishes phosphorylation on serine residues; when associated with A-178 and A-195.|||Removed|||Required for assuming the closed conformation and for interaction with CDC20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126117|||http://purl.uniprot.org/annotation/VSP_047644|||http://purl.uniprot.org/annotation/VSP_047645
http://togogenome.org/gene/9606:MRPL21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXI4|||http://purl.uniprot.org/uniprot/Q7Z2W9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Large ribosomal subunit protein bL21m|||Mitochondrion|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252442|||http://purl.uniprot.org/annotation/VSP_045633
http://togogenome.org/gene/9606:GAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13480|||http://purl.uniprot.org/uniprot/Q9HA84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRB2-associated-binding protein 1|||In DFNB26; results in dysregulation of MET-signaling pathway genes expression; does not affect interaction with METTL13.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylserine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050282|||http://purl.uniprot.org/annotation/VAR_025261|||http://purl.uniprot.org/annotation/VAR_036132|||http://purl.uniprot.org/annotation/VAR_036133|||http://purl.uniprot.org/annotation/VAR_053096|||http://purl.uniprot.org/annotation/VAR_080809|||http://purl.uniprot.org/annotation/VSP_017137
http://togogenome.org/gene/9606:RGPD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99666|||http://purl.uniprot.org/uniprot/V9HWE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RANBP2-like and GRIP domain-containing protein 5/6|||RanBD1|||RanBD1 1|||RanBD1 2|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204915|||http://purl.uniprot.org/annotation/VSP_038968|||http://purl.uniprot.org/annotation/VSP_038969
http://togogenome.org/gene/9606:LRRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRNT|||Leucine-rich repeat-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021618
http://togogenome.org/gene/9606:PRELID3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||PRELI domain containing protein 3B|||PRELI/MSF1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079429|||http://purl.uniprot.org/annotation/VSP_044840
http://togogenome.org/gene/9606:MUC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02505|||http://purl.uniprot.org/uniprot/Q9H3Q6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||32 X approximate tandem repeats, Ser/Thr-rich|||4|||5|||6|||7|||8|||9|||Disordered|||EGF-like|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||May be associated with Crohn disease.|||Mucin-3A|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158955|||http://purl.uniprot.org/annotation/VAR_030722|||http://purl.uniprot.org/annotation/VAR_030723|||http://purl.uniprot.org/annotation/VAR_030724|||http://purl.uniprot.org/annotation/VSP_023229|||http://purl.uniprot.org/annotation/VSP_023230|||http://purl.uniprot.org/annotation/VSP_023231|||http://purl.uniprot.org/annotation/VSP_023232|||http://purl.uniprot.org/annotation/VSP_023233|||http://purl.uniprot.org/annotation/VSP_023234|||http://purl.uniprot.org/annotation/VSP_023235
http://togogenome.org/gene/9606:TMEM255B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Pro residues|||Transmembrane protein 255B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266042
http://togogenome.org/gene/9606:CYP39A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTD2|||http://purl.uniprot.org/uniprot/B7Z786|||http://purl.uniprot.org/uniprot/Q9NYL5                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  10% decrease of 7-alpha hydroxylase activity.|||24-hydroxycholesterol 7-alpha-hydroxylase|||60% decrease of 7-alpha hydroxylase activity.|||Associated with elevated serum (24S)-hydroxycholesterol levels; 30% decrease of 7-alpha hydroxylase activity.|||Associated with elevated serum (24S)-hydroxycholesterol levels; impairs 7-alpha hydroxylase activity.|||Helical|||Impairs 7-alpha hydroxylase activity.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051992|||http://purl.uniprot.org/annotation/VAR_031609|||http://purl.uniprot.org/annotation/VAR_031610|||http://purl.uniprot.org/annotation/VAR_031611|||http://purl.uniprot.org/annotation/VAR_031612|||http://purl.uniprot.org/annotation/VAR_083092
http://togogenome.org/gene/9606:USP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94966                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CS 1|||CS 2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2 and isoform 4.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3, isoform 4, isoform 6 and isoform 7.|||In isoform 4 and isoform 6.|||In isoform 7.|||Lumenal|||MYND-type|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080646|||http://purl.uniprot.org/annotation/VAR_051528|||http://purl.uniprot.org/annotation/VSP_026708|||http://purl.uniprot.org/annotation/VSP_026709|||http://purl.uniprot.org/annotation/VSP_026710|||http://purl.uniprot.org/annotation/VSP_026711|||http://purl.uniprot.org/annotation/VSP_026712|||http://purl.uniprot.org/annotation/VSP_026713|||http://purl.uniprot.org/annotation/VSP_045891|||http://purl.uniprot.org/annotation/VSP_047057
http://togogenome.org/gene/9606:ASL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDL8|||http://purl.uniprot.org/uniprot/A0A0S2Z316|||http://purl.uniprot.org/uniprot/P04424                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10-fold reduction in activity.|||2-fold reduction in activity.|||Argininosuccinate lyase|||Argininosuccinate lyase C-terminal|||Fumarate lyase N-terminal|||In ARGINSA.|||In ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate.|||In ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression.|||In ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression.|||In ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation.|||In ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production.|||In ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity.|||In ARGINSA; loss of argininosuccinate lyase activity.|||In ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding.|||In ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression.|||In ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression.|||In ARGINSA; severe.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increases basicity of active site His|||N-acetylalanine|||N6-acetyllysine|||Proton acceptor|||Proton donor|||Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.|||Removed|||in chain A|||in chain B|||in chain C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137712|||http://purl.uniprot.org/annotation/VAR_000676|||http://purl.uniprot.org/annotation/VAR_000677|||http://purl.uniprot.org/annotation/VAR_000678|||http://purl.uniprot.org/annotation/VAR_000679|||http://purl.uniprot.org/annotation/VAR_017572|||http://purl.uniprot.org/annotation/VAR_017573|||http://purl.uniprot.org/annotation/VAR_017574|||http://purl.uniprot.org/annotation/VAR_036281|||http://purl.uniprot.org/annotation/VAR_036282|||http://purl.uniprot.org/annotation/VAR_043106|||http://purl.uniprot.org/annotation/VAR_043107|||http://purl.uniprot.org/annotation/VAR_043108|||http://purl.uniprot.org/annotation/VAR_043109|||http://purl.uniprot.org/annotation/VAR_043110|||http://purl.uniprot.org/annotation/VAR_043111|||http://purl.uniprot.org/annotation/VAR_043112|||http://purl.uniprot.org/annotation/VAR_072186|||http://purl.uniprot.org/annotation/VAR_072187|||http://purl.uniprot.org/annotation/VAR_072188|||http://purl.uniprot.org/annotation/VAR_072189|||http://purl.uniprot.org/annotation/VAR_072190|||http://purl.uniprot.org/annotation/VAR_072191|||http://purl.uniprot.org/annotation/VAR_072192|||http://purl.uniprot.org/annotation/VAR_072193|||http://purl.uniprot.org/annotation/VAR_072194|||http://purl.uniprot.org/annotation/VAR_072195|||http://purl.uniprot.org/annotation/VAR_072196|||http://purl.uniprot.org/annotation/VAR_072197|||http://purl.uniprot.org/annotation/VAR_072198|||http://purl.uniprot.org/annotation/VAR_072199|||http://purl.uniprot.org/annotation/VAR_072200|||http://purl.uniprot.org/annotation/VAR_072201|||http://purl.uniprot.org/annotation/VAR_072202|||http://purl.uniprot.org/annotation/VAR_072203|||http://purl.uniprot.org/annotation/VAR_072204|||http://purl.uniprot.org/annotation/VAR_072205|||http://purl.uniprot.org/annotation/VAR_072206|||http://purl.uniprot.org/annotation/VAR_072207|||http://purl.uniprot.org/annotation/VAR_072208|||http://purl.uniprot.org/annotation/VAR_072209|||http://purl.uniprot.org/annotation/VAR_072210|||http://purl.uniprot.org/annotation/VAR_072211|||http://purl.uniprot.org/annotation/VAR_072212|||http://purl.uniprot.org/annotation/VAR_072213|||http://purl.uniprot.org/annotation/VAR_072214|||http://purl.uniprot.org/annotation/VAR_072215|||http://purl.uniprot.org/annotation/VAR_072216|||http://purl.uniprot.org/annotation/VAR_072217|||http://purl.uniprot.org/annotation/VAR_072218|||http://purl.uniprot.org/annotation/VAR_072219|||http://purl.uniprot.org/annotation/VAR_072220|||http://purl.uniprot.org/annotation/VAR_072221|||http://purl.uniprot.org/annotation/VAR_072222|||http://purl.uniprot.org/annotation/VAR_072223|||http://purl.uniprot.org/annotation/VAR_072224|||http://purl.uniprot.org/annotation/VAR_072225|||http://purl.uniprot.org/annotation/VAR_072226|||http://purl.uniprot.org/annotation/VAR_072227|||http://purl.uniprot.org/annotation/VAR_072228|||http://purl.uniprot.org/annotation/VAR_075551|||http://purl.uniprot.org/annotation/VAR_075552|||http://purl.uniprot.org/annotation/VAR_085825|||http://purl.uniprot.org/annotation/VAR_085826|||http://purl.uniprot.org/annotation/VAR_085827|||http://purl.uniprot.org/annotation/VAR_085828|||http://purl.uniprot.org/annotation/VSP_047255|||http://purl.uniprot.org/annotation/VSP_047256
http://togogenome.org/gene/9606:TNKS1BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0C2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  182 kDa tankyrase-1-binding protein|||Acidic|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-methyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Tankyrase-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072437|||http://purl.uniprot.org/annotation/VAR_028141|||http://purl.uniprot.org/annotation/VAR_032615|||http://purl.uniprot.org/annotation/VSP_026000|||http://purl.uniprot.org/annotation/VSP_026001|||http://purl.uniprot.org/annotation/VSP_026002
http://togogenome.org/gene/9606:MYD88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSI9|||http://purl.uniprot.org/uniprot/A0A3B3ITY3|||http://purl.uniprot.org/uniprot/A0A3F2YP85|||http://purl.uniprot.org/uniprot/Q99836                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished interaction with E.coli TcpC without affecting ability to promote Toll-like receptor (TLR)-mediated cytokine production; when associated with S-203.|||Abolished interaction with E.coli TcpC without affecting ability to promote Toll-like receptor (TLR)-mediated cytokine production; when associated with S-280.|||Death|||Disordered|||Found in hematological malignancies; somatic mutation; unknown pathological significance.|||Found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation.|||Found in hematological malignancies; somatic mutation; unknown pathological significance; loss of NF-kappa-B complex activation; loss of interaction with IRAK4; reduces homooligomerization.|||Found in hematological malignancies; somatic mutation; unknown pathological significance; no effect on NF-kappaB complex activation.|||In IMD68; loss of NF-kappa-B complex activation.|||In IMD68; results in a loss of function; decreases NF-kappa-B complex activation.|||In IMD68; results in a loss of function; loss of NF-kappa-B complex activation.|||In Pococurante (Poc); abolished MYD88-dependent sensing of most Toll-like receptor (TLR) ligands.|||In WM1; found in hematological malignancies; somatic mutation; unknown pathological significance; constitutively activates NF-kappaB complex activation; gain-of-function mutation; does not affect interaction with IRAK4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Intermediate domain|||Myeloid differentiation primary response protein MyD88|||Phosphoserine|||Rare variant; unknown pathological significance; loss of NF-kappa-B complex activation; loss of interaction with IRAK4; reduces homooligomerization.|||Reduced interaction with TIRAP, and strongly reduced activity. Strongly reduced interaction with TIRAP; when associated with A-288.|||Slightly reduced activity, and reduced interaction with TIRAP. Strongly reduced interaction with TIRAP; when associated with A-196.|||Slightly reduced activity.|||Strongly reduced activity.|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096666|||http://purl.uniprot.org/annotation/VAR_047953|||http://purl.uniprot.org/annotation/VAR_047954|||http://purl.uniprot.org/annotation/VAR_072893|||http://purl.uniprot.org/annotation/VAR_072894|||http://purl.uniprot.org/annotation/VAR_072895|||http://purl.uniprot.org/annotation/VAR_072896|||http://purl.uniprot.org/annotation/VAR_073252|||http://purl.uniprot.org/annotation/VAR_073253|||http://purl.uniprot.org/annotation/VAR_073254|||http://purl.uniprot.org/annotation/VAR_073255|||http://purl.uniprot.org/annotation/VAR_073256|||http://purl.uniprot.org/annotation/VAR_073257|||http://purl.uniprot.org/annotation/VAR_073258|||http://purl.uniprot.org/annotation/VAR_073259|||http://purl.uniprot.org/annotation/VAR_073260|||http://purl.uniprot.org/annotation/VAR_073261|||http://purl.uniprot.org/annotation/VAR_073262|||http://purl.uniprot.org/annotation/VAR_073263|||http://purl.uniprot.org/annotation/VSP_038887|||http://purl.uniprot.org/annotation/VSP_043498|||http://purl.uniprot.org/annotation/VSP_043499|||http://purl.uniprot.org/annotation/VSP_043500|||http://purl.uniprot.org/annotation/VSP_053764|||http://purl.uniprot.org/annotation/VSP_053765
http://togogenome.org/gene/9606:HOXB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14652                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B2|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200114
http://togogenome.org/gene/9606:GAL3ST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A11                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Galactose-3-O-sulfotransferase 3|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085206|||http://purl.uniprot.org/annotation/VAR_053988|||http://purl.uniprot.org/annotation/VAR_053989
http://togogenome.org/gene/9606:VASH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJZ5|||http://purl.uniprot.org/uniprot/A8K4K8|||http://purl.uniprot.org/uniprot/Q86V25                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished tyrosine carboxypeptidase activity. No effect on binding to microtubule.|||Disordered|||Disrupted interaction with SVBP. Reduced tyrosine carboxypeptidase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||No effect on tyrosine carboxypeptidase activity.|||Phosphoserine|||Reduced tyrosine carboxypeptidase activity.|||Slightly reduced tyrosine carboxypeptidase activity.|||Strongly reduced tyrosine carboxypeptidase activity.|||Tubulinyl-Tyr carboxypeptidase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189982|||http://purl.uniprot.org/annotation/VSP_013328|||http://purl.uniprot.org/annotation/VSP_013329|||http://purl.uniprot.org/annotation/VSP_013330|||http://purl.uniprot.org/annotation/VSP_013331|||http://purl.uniprot.org/annotation/VSP_013332|||http://purl.uniprot.org/annotation/VSP_013333|||http://purl.uniprot.org/annotation/VSP_013334|||http://purl.uniprot.org/annotation/VSP_054104
http://togogenome.org/gene/9606:FAM72D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L9T8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM72D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340259
http://togogenome.org/gene/9606:SLC22A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15244                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol.|||Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.|||Decreased TEA uptake and YES1-mediated tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-241. Strong decrease in TEA uptake; when associated with F-377. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-377.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations|||Lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol.|||Lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol.|||Lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol.|||N-linked (GlcNAc...) asparagine|||No change in TEA and metformin uptake. No change in tyrosine phosphorylation.|||No change in TEA uptake.|||Proline-rich sequence|||Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-362.|||Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-362 and F-377.|||Solute carrier family 22 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320957|||http://purl.uniprot.org/annotation/VAR_039322|||http://purl.uniprot.org/annotation/VAR_039323|||http://purl.uniprot.org/annotation/VAR_039324|||http://purl.uniprot.org/annotation/VAR_039325|||http://purl.uniprot.org/annotation/VAR_039326|||http://purl.uniprot.org/annotation/VAR_039327|||http://purl.uniprot.org/annotation/VAR_039328|||http://purl.uniprot.org/annotation/VAR_039329|||http://purl.uniprot.org/annotation/VSP_031771|||http://purl.uniprot.org/annotation/VSP_031772|||http://purl.uniprot.org/annotation/VSP_031773|||http://purl.uniprot.org/annotation/VSP_031774
http://togogenome.org/gene/9606:JPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIC1|||http://purl.uniprot.org/uniprot/Q8WXH2|||http://purl.uniprot.org/uniprot/Q96HD8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Junctophilin-3|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159850|||http://purl.uniprot.org/annotation/VAR_032494|||http://purl.uniprot.org/annotation/VAR_032495|||http://purl.uniprot.org/annotation/VAR_032496|||http://purl.uniprot.org/annotation/VSP_002787|||http://purl.uniprot.org/annotation/VSP_002788
http://togogenome.org/gene/9606:RPL22L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5R6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Ribosomal protein eL22-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240632|||http://purl.uniprot.org/annotation/VAR_061771
http://togogenome.org/gene/9606:NWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q149M9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||NACHT|||NACHT domain- and WD repeat-containing protein 1|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308254|||http://purl.uniprot.org/annotation/VAR_036769|||http://purl.uniprot.org/annotation/VAR_036770|||http://purl.uniprot.org/annotation/VAR_036771|||http://purl.uniprot.org/annotation/VAR_036772|||http://purl.uniprot.org/annotation/VAR_036773|||http://purl.uniprot.org/annotation/VAR_036774|||http://purl.uniprot.org/annotation/VAR_036775|||http://purl.uniprot.org/annotation/VSP_028940|||http://purl.uniprot.org/annotation/VSP_028941|||http://purl.uniprot.org/annotation/VSP_040651|||http://purl.uniprot.org/annotation/VSP_040652
http://togogenome.org/gene/9606:KIAA0753                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2KHM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS38; unknown pathological significance.|||In OFD15.|||In SRTD21.|||In isoform 2.|||Necessary and sufficient for CEP20-binding|||Phosphoserine|||Polar residues|||Protein moonraker                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280109|||http://purl.uniprot.org/annotation/VAR_031065|||http://purl.uniprot.org/annotation/VAR_031066|||http://purl.uniprot.org/annotation/VAR_031067|||http://purl.uniprot.org/annotation/VAR_031068|||http://purl.uniprot.org/annotation/VAR_031069|||http://purl.uniprot.org/annotation/VAR_031070|||http://purl.uniprot.org/annotation/VAR_031071|||http://purl.uniprot.org/annotation/VAR_031072|||http://purl.uniprot.org/annotation/VAR_079381|||http://purl.uniprot.org/annotation/VAR_086266|||http://purl.uniprot.org/annotation/VAR_086267|||http://purl.uniprot.org/annotation/VAR_086268|||http://purl.uniprot.org/annotation/VSP_023539
http://togogenome.org/gene/9606:SLC39A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z534|||http://purl.uniprot.org/uniprot/Q15043                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased N-glycosylation.|||Extracellular|||HHHGHXHX-motif|||Helical|||In HCIN; loss of localization at the plasma membrane; loss of Zn uptake activity.|||In HMNDYT2; no effect on protein abundance; no effect on subcellular localization at the plasma membrane and within the cytoplasm; decreased manganese ion transmembrane transporter activity.|||In isoform 2.|||In isoform 3.|||Metal cation symporter ZIP14|||N-linked (GlcNAc...) asparagine|||XEXPHE-motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312194|||http://purl.uniprot.org/annotation/PRO_5014239317|||http://purl.uniprot.org/annotation/VAR_037450|||http://purl.uniprot.org/annotation/VAR_077004|||http://purl.uniprot.org/annotation/VAR_077005|||http://purl.uniprot.org/annotation/VAR_077006|||http://purl.uniprot.org/annotation/VAR_080794|||http://purl.uniprot.org/annotation/VSP_029728|||http://purl.uniprot.org/annotation/VSP_040139
http://togogenome.org/gene/9606:MRPL47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD33                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein uL29m|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030567|||http://purl.uniprot.org/annotation/VAR_052042|||http://purl.uniprot.org/annotation/VAR_052043|||http://purl.uniprot.org/annotation/VSP_035649|||http://purl.uniprot.org/annotation/VSP_035650
http://togogenome.org/gene/9606:APOA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02647                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  1|||10|||10 X approximate tandem repeats|||2|||3; half-length|||4|||5|||6|||7|||8|||9; half-length|||Apolipoprotein A-I|||Confirmed at protein level.|||In AMYL8.|||In AMYL8; also found in a family with amyloid polyneuropathy-nephropathy Iowa.|||In AMYL8; plasma level of HDL and apoA-I protein were significantly lower in the patient.|||In AMYL8; unknown pathological significance.|||In Baltimore.|||In Boston; no evidence of association with premature coronary heart disease; associated with decreased levels of HDL cholesterol; associated with decreased serum cellular cholesterol efflux; associated with decreased lecithin-cholesterol acyltransferase (LCAT) activity.|||In FHA2; missing protein expression.|||In FHA2; no protein expression.|||In Fukuoka.|||In Giessen.|||In HDL deficiency; with periorbital xanthelasmas; decreased protein abundance.|||In Hita.|||In Marburg/Munster-2.|||In Milano; no evidence of association with premature vascular disease; associated with decreased HDL levels and moderate increase in triglycerides; allows the formation of disulfide-linked homodimers via the introduced cysteine; assembles properly in HDL; alters protein structure; has no tendency to form fibrils and aggregates.|||In Munster-3A.|||In Munster-3B.|||In Munster-3C.|||In Munster-4.|||In Norway.|||In Oita; 60% of normal apoA-I and normal HDL cholesterol levels; rapidly cleared from plasma.|||In Tsushima.|||In Zaragoza.|||Methionine sulfoxide|||N-linked (Glc) (glycation) lysine|||Proapolipoprotein A-I|||Truncated apolipoprotein A-I|||With 1 methionine sulfoxide, oxidation at Met-110.|||With 1 methionine sulfoxide, oxidation at Met-136.|||With 2 methionine sulfoxides, oxidation at Met-110 and Met-136.|||Without methionine sulfoxide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001939|||http://purl.uniprot.org/annotation/PRO_0000001940|||http://purl.uniprot.org/annotation/PRO_0000425323|||http://purl.uniprot.org/annotation/VAR_000605|||http://purl.uniprot.org/annotation/VAR_000606|||http://purl.uniprot.org/annotation/VAR_000607|||http://purl.uniprot.org/annotation/VAR_000608|||http://purl.uniprot.org/annotation/VAR_000609|||http://purl.uniprot.org/annotation/VAR_000610|||http://purl.uniprot.org/annotation/VAR_000611|||http://purl.uniprot.org/annotation/VAR_000612|||http://purl.uniprot.org/annotation/VAR_000613|||http://purl.uniprot.org/annotation/VAR_000614|||http://purl.uniprot.org/annotation/VAR_000615|||http://purl.uniprot.org/annotation/VAR_000616|||http://purl.uniprot.org/annotation/VAR_000617|||http://purl.uniprot.org/annotation/VAR_000618|||http://purl.uniprot.org/annotation/VAR_000619|||http://purl.uniprot.org/annotation/VAR_000620|||http://purl.uniprot.org/annotation/VAR_000621|||http://purl.uniprot.org/annotation/VAR_000622|||http://purl.uniprot.org/annotation/VAR_000623|||http://purl.uniprot.org/annotation/VAR_000624|||http://purl.uniprot.org/annotation/VAR_000625|||http://purl.uniprot.org/annotation/VAR_014609|||http://purl.uniprot.org/annotation/VAR_016189|||http://purl.uniprot.org/annotation/VAR_017017|||http://purl.uniprot.org/annotation/VAR_021362|||http://purl.uniprot.org/annotation/VAR_025445|||http://purl.uniprot.org/annotation/VAR_074073|||http://purl.uniprot.org/annotation/VAR_083307|||http://purl.uniprot.org/annotation/VAR_083308|||http://purl.uniprot.org/annotation/VAR_083309|||http://purl.uniprot.org/annotation/VAR_083310|||http://purl.uniprot.org/annotation/VAR_083311|||http://purl.uniprot.org/annotation/VAR_083312
http://togogenome.org/gene/9606:FAM209B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JX69                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Protein FAM209B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236040|||http://purl.uniprot.org/annotation/VAR_033762|||http://purl.uniprot.org/annotation/VAR_050918|||http://purl.uniprot.org/annotation/VAR_061633
http://togogenome.org/gene/9606:KLHL41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60662                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||In NEM9.|||In isoform Short.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 41|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119088|||http://purl.uniprot.org/annotation/VAR_050046|||http://purl.uniprot.org/annotation/VAR_050047|||http://purl.uniprot.org/annotation/VAR_071823|||http://purl.uniprot.org/annotation/VAR_071824|||http://purl.uniprot.org/annotation/VSP_002819
http://togogenome.org/gene/9606:GAS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZT7|||http://purl.uniprot.org/uniprot/A0A384MR00|||http://purl.uniprot.org/uniprot/B7Z1U9|||http://purl.uniprot.org/uniprot/O95995                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein regulatory complex subunit 4|||Growth arrest-specific protein 8|||In CILD33; loss of localization to cilia; abnormal cilia with axonemal disorganization.|||In CILD33; the same mutation in the mouse sequence shows a moderate decrease in cilia motility.|||In isoform 2.|||Interaction with SMO|||Microtubule-binding|||Regulates microtubule-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220377|||http://purl.uniprot.org/annotation/VAR_016006|||http://purl.uniprot.org/annotation/VAR_049230|||http://purl.uniprot.org/annotation/VAR_080336|||http://purl.uniprot.org/annotation/VAR_080337|||http://purl.uniprot.org/annotation/VAR_080338|||http://purl.uniprot.org/annotation/VSP_054805
http://togogenome.org/gene/9606:PTMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFU3|||http://purl.uniprot.org/uniprot/F5GXR3|||http://purl.uniprot.org/uniprot/P20962                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||N-acetylserine|||N6-acetyllysine|||Parathymosin|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191632
http://togogenome.org/gene/9606:NECTIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92692                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform Alpha.|||Increased entry of HHV-1/Rid1 and HSV-2.|||Loss of entry of HHV-1/Rid1 and HSV-2. No effect on PRV entry.|||N-linked (GlcNAc...) asparagine|||Nectin-2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015136|||http://purl.uniprot.org/annotation/VSP_002628|||http://purl.uniprot.org/annotation/VSP_002629
http://togogenome.org/gene/9606:HPGD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15428                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  15-hydroxyprostaglandin dehydrogenase [NAD(+)]|||In COA; inactive.|||In DIGC.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss 15-hydroxyprostaglandin dehydrogenase activity.|||Loss of activity.|||Proton acceptor|||Reduced affinity for NAD and prostaglandin E2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054744|||http://purl.uniprot.org/annotation/VAR_006972|||http://purl.uniprot.org/annotation/VAR_046209|||http://purl.uniprot.org/annotation/VAR_060792|||http://purl.uniprot.org/annotation/VSP_043032|||http://purl.uniprot.org/annotation/VSP_045106|||http://purl.uniprot.org/annotation/VSP_045107|||http://purl.uniprot.org/annotation/VSP_045108|||http://purl.uniprot.org/annotation/VSP_045579
http://togogenome.org/gene/9606:PIRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C851                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoinositide-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347060
http://togogenome.org/gene/9606:ZNF813                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN06                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 813                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294363|||http://purl.uniprot.org/annotation/VAR_033167|||http://purl.uniprot.org/annotation/VAR_033168|||http://purl.uniprot.org/annotation/VAR_052905|||http://purl.uniprot.org/annotation/VAR_052906|||http://purl.uniprot.org/annotation/VAR_052907|||http://purl.uniprot.org/annotation/VAR_052908
http://togogenome.org/gene/9606:TBPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62380                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  TATA box-binding protein-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153992
http://togogenome.org/gene/9606:GLDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14DE1|||http://purl.uniprot.org/uniprot/Q6ZMI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by BMP1|||Cleavage; by furin-like protease|||Collagen-like 1|||Collagen-like 2|||Cytoplasmic|||Disordered|||Extracellular|||Gliomedin|||Gliomedin shedded ectodomain|||Helical; Signal-anchor for type II membrane protein|||In LCCS11; abolishes cell surface localization; abolishes interaction with NFASC.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246321|||http://purl.uniprot.org/annotation/PRO_0000434265|||http://purl.uniprot.org/annotation/VAR_027039|||http://purl.uniprot.org/annotation/VAR_050424|||http://purl.uniprot.org/annotation/VAR_061484|||http://purl.uniprot.org/annotation/VAR_078545|||http://purl.uniprot.org/annotation/VAR_078546|||http://purl.uniprot.org/annotation/VSP_019845
http://togogenome.org/gene/9606:RAB3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7G2|||http://purl.uniprot.org/uniprot/O95716                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||Loss of phosphorylation. Reduced binding of CHM and CHML binding.|||N-acetylalanine|||Phosphomimetic mutant. Loss of CHM and CHML binding.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3D|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121088|||http://purl.uniprot.org/annotation/VAR_051710
http://togogenome.org/gene/9606:SIAH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW03                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Zinc Finger                                                                                  ^@                                                                                  SIAH-type; degenerate|||Seven in absentia homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334701
http://togogenome.org/gene/9606:ARAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CH1|||http://purl.uniprot.org/uniprot/Q8WWN8|||http://purl.uniprot.org/uniprot/Q9H7C1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3|||C4-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Loss of PtdIns(3,4,5)P3 binding.|||PH|||PH 1|||PH 2|||PH 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Ras-associating|||Rho-GAP|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074215|||http://purl.uniprot.org/annotation/VAR_036180|||http://purl.uniprot.org/annotation/VAR_036181|||http://purl.uniprot.org/annotation/VAR_036182|||http://purl.uniprot.org/annotation/VAR_048330|||http://purl.uniprot.org/annotation/VSP_056214|||http://purl.uniprot.org/annotation/VSP_056215
http://togogenome.org/gene/9606:MAGEA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E962|||http://purl.uniprot.org/uniprot/P43364                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a family with intellectual disability; unknown pathological significance.|||In isoform 2.|||MAGE|||Melanoma-associated antigen 11|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156710|||http://purl.uniprot.org/annotation/VAR_053497|||http://purl.uniprot.org/annotation/VAR_080775|||http://purl.uniprot.org/annotation/VSP_018576
http://togogenome.org/gene/9606:RPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS36|||http://purl.uniprot.org/uniprot/P39023|||http://purl.uniprot.org/uniprot/Q96QL0                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein uL3|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on methylation by METTL18.|||Phosphoserine|||Rare variant found in a Diamond-Blackfan anemia patient; unknown pathological significance.|||Removed|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077227|||http://purl.uniprot.org/annotation/VAR_069220
http://togogenome.org/gene/9606:OR4P4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4P4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150566
http://togogenome.org/gene/9606:KRTCAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6L1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Keratinocyte-associated protein 2|||Lumenal|||Phosphothreonine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226992|||http://purl.uniprot.org/annotation/VAR_025531|||http://purl.uniprot.org/annotation/VSP_053439
http://togogenome.org/gene/9606:CLN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75503                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Ceroid-lipofuscinosis neuronal protein 5|||Ceroid-lipofuscinosis neuronal protein 5, secreted form|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In CLN5.|||In CLN5; Retained in the endoplasmic reticulum rather than reaching the lysosome.|||In CLN5; creates a new N-glycosylation site; retained in the endoplasmic reticulum rather than reaching the lysosome.|||In CLN5; loss of glycosylation; effectively transported to the lysosome.|||In CLN5; retained in the endoplasmic reticulum rather than reaching the lysosome.|||Loss of glycosylation. Effectively transported to the lysosome.|||Loss of glycosylation. Partially retained in the endoplasmic reticulum.|||Loss of glycosylation. Retained in the Golgi apparatus rather than reaching the lysosome.|||Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome.|||Lumenal|||Membrane-anchoring|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089860|||http://purl.uniprot.org/annotation/PRO_0000438009|||http://purl.uniprot.org/annotation/VAR_005137|||http://purl.uniprot.org/annotation/VAR_005138|||http://purl.uniprot.org/annotation/VAR_042700|||http://purl.uniprot.org/annotation/VAR_042701|||http://purl.uniprot.org/annotation/VAR_042702|||http://purl.uniprot.org/annotation/VAR_059031|||http://purl.uniprot.org/annotation/VAR_059032|||http://purl.uniprot.org/annotation/VAR_066895|||http://purl.uniprot.org/annotation/VAR_066896|||http://purl.uniprot.org/annotation/VAR_066897|||http://purl.uniprot.org/annotation/VAR_066898|||http://purl.uniprot.org/annotation/VAR_066899|||http://purl.uniprot.org/annotation/VAR_066900|||http://purl.uniprot.org/annotation/VAR_066901|||http://purl.uniprot.org/annotation/VAR_066902|||http://purl.uniprot.org/annotation/VAR_066903
http://togogenome.org/gene/9606:TRAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHG8|||http://purl.uniprot.org/uniprot/Q13114                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Interaction with glycoprotein N of Andes and New York hantaviruses|||Abolishes interaction with LTBR, CD40 and TANK.|||Abolishes interaction with RALGDS.|||Abolishes interaction with RNF216; when associated with A-441.|||Abolishes interaction with RNF216; when associated with A-443.|||Confers resistance to cleavage by enterovirus D68 protease 2A.|||Disordered|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IIAE5.|||In isoform 2.|||Loss of ubiquitination activity on ASC; when associated with A-68.|||Loss of ubiquitination activity on ASC; when associated with A-70.|||Loss of ubiquitination activity, impaired interaction with MAVS and IRF3. No effect on interaction with IKBKE, nor with DDX3X.|||MATH|||Phosphoserine|||RING-type|||Strong increase in both 'Lys-48' and 'Lys-63'-linked ubiquitination.|||TNF receptor-associated factor 3|||TRAF-type|||TRAF-type 1|||TRAF-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056401|||http://purl.uniprot.org/annotation/VAR_052149|||http://purl.uniprot.org/annotation/VAR_069081|||http://purl.uniprot.org/annotation/VSP_040040
http://togogenome.org/gene/9606:ADIPOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A54                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adiponectin receptor protein 1|||Basic and acidic residues|||Cytoplasmic|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with 161-S--S-167 and 229-G--G-231.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with 161-S--S-167 and 291-S--S-297.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with 229-G--G-231 and 291-S--S-297.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-208 and A-337.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-208 and A-341.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-191; A-337 and A-341.|||Decreases activation of AMPK in response to ADIPOQ binding; when associated with A-208; A-337 and A-341.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218827
http://togogenome.org/gene/9606:DEPDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75140                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished phosphorylation by PIM1; when associated with A-1002.|||Abolished phosphorylation by PIM1; when associated with A-1530.|||Basic and acidic residues|||DEP|||Disordered|||GATOR1 complex protein DEPDC5|||In FFEVF1; does not inhibit DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation.|||In FFEVF1; does not inhibit DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; inhibits slightly RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation.|||In FFEVF1; does not inhibit DEPDC5 signaling; stimulates slightly kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation.|||In FFEVF1; inhibits slightly DEPDC5 signaling; does not change kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation.|||In FFEVF1; inhibits slightly DEPDC5 signaling; stimulates slightly kinase activity of mTORC1; does not change association with the GATOR complex; does not change RRAGA/RRAGC and RRAGB/RRAGC heterodimer formation.|||In FFEVF1; unknown pathological significance.|||In isoform 1 and isoform 9.|||In isoform 1, isoform 4 and isoform 8.|||In isoform 2.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 6.|||In mutant AB; abolished interaction with NPRL2 and NPRL3; when associated with 185-G--G-189.|||In mutant AB; abolished interaction with NPRL2 and NPRL3; when associated with 371-G--G-375.|||In mutant P; strongly decreased interaction with RagA/RRAGA.|||No effect on interaction with KLHL22.|||No effect on ubiquitination. Loss of interaction with KLHL22 and ubiquitination; when associated with R-447, R-1065, R-1088 and R-1574.|||No effect on ubiquitination. Loss of interaction with KLHL22 and ubiquitination; when associated with R-447, R-710, R-1065 and R-1574.|||No effect on ubiquitination. Loss of interaction with KLHL22 and ubiquitination; when associated with R-447, R-710, R-1088 and R-1574.|||No effect on ubiquitination. Loss of interaction with KLHL22 and ubiquitination; when associated with R-710, R-1065, R-1088 and R-1574.|||No effect on ubiquitination. Loss of ubiquitination; when associated with R-447, R-710, R-1065 and R-1088.|||Phosphoserine|||Phosphoserine; by PIM1|||Phosphoserine; by PKB/AKT1 and PIM1|||Polar residues|||Strongly decreased interaction with RagA/RRAGA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079865|||http://purl.uniprot.org/annotation/VAR_024338|||http://purl.uniprot.org/annotation/VAR_053953|||http://purl.uniprot.org/annotation/VAR_053954|||http://purl.uniprot.org/annotation/VAR_069263|||http://purl.uniprot.org/annotation/VAR_069264|||http://purl.uniprot.org/annotation/VAR_069265|||http://purl.uniprot.org/annotation/VAR_069266|||http://purl.uniprot.org/annotation/VAR_072363|||http://purl.uniprot.org/annotation/VAR_072364|||http://purl.uniprot.org/annotation/VAR_072365|||http://purl.uniprot.org/annotation/VAR_072366|||http://purl.uniprot.org/annotation/VAR_077128|||http://purl.uniprot.org/annotation/VAR_077129|||http://purl.uniprot.org/annotation/VAR_077130|||http://purl.uniprot.org/annotation/VAR_077131|||http://purl.uniprot.org/annotation/VAR_077132|||http://purl.uniprot.org/annotation/VAR_077133|||http://purl.uniprot.org/annotation/VSP_014933|||http://purl.uniprot.org/annotation/VSP_014934|||http://purl.uniprot.org/annotation/VSP_014936|||http://purl.uniprot.org/annotation/VSP_014937|||http://purl.uniprot.org/annotation/VSP_014938|||http://purl.uniprot.org/annotation/VSP_014939|||http://purl.uniprot.org/annotation/VSP_014940|||http://purl.uniprot.org/annotation/VSP_014941
http://togogenome.org/gene/9606:OR52E4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGH9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52E4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150773|||http://purl.uniprot.org/annotation/VAR_024147|||http://purl.uniprot.org/annotation/VAR_024148|||http://purl.uniprot.org/annotation/VAR_034335|||http://purl.uniprot.org/annotation/VAR_034336|||http://purl.uniprot.org/annotation/VAR_034337|||http://purl.uniprot.org/annotation/VAR_062082
http://togogenome.org/gene/9606:LASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIC4|||http://purl.uniprot.org/uniprot/Q14847                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LIM and SH3 domain protein 1|||LIM zinc-binding|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||N6-succinyllysine|||Nebulin 1|||Nebulin 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075761|||http://purl.uniprot.org/annotation/VSP_016554|||http://purl.uniprot.org/annotation/VSP_054611
http://togogenome.org/gene/9606:PADI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2J8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Loss of enzyme activity.|||Mildly reduced enzyme activity.|||Nucleophile|||Protein-arginine deiminase type-2|||Reduced enzyme activity.|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220026|||http://purl.uniprot.org/annotation/VSP_056385
http://togogenome.org/gene/9606:OR10Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV63|||http://purl.uniprot.org/uniprot/Q8NGY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150721|||http://purl.uniprot.org/annotation/VAR_034297
http://togogenome.org/gene/9606:HUWE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6Z7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase HUWE1|||Found in patients with autism spectrum disorders; unknown pathological significance.|||Glycyl thioester intermediate|||HECT|||In MRXST.|||In MRXST; decreased protein levels in patient cells.|||In MRXST; increased protein levels in patient cells.|||In isoform 2.|||In isoform 3.|||Loss of activity.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||UBA|||UIM|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120340|||http://purl.uniprot.org/annotation/VAR_045670|||http://purl.uniprot.org/annotation/VAR_045671|||http://purl.uniprot.org/annotation/VAR_045672|||http://purl.uniprot.org/annotation/VAR_061986|||http://purl.uniprot.org/annotation/VAR_076253|||http://purl.uniprot.org/annotation/VAR_082247|||http://purl.uniprot.org/annotation/VAR_082248|||http://purl.uniprot.org/annotation/VAR_082249|||http://purl.uniprot.org/annotation/VAR_082250|||http://purl.uniprot.org/annotation/VAR_082251|||http://purl.uniprot.org/annotation/VAR_082252|||http://purl.uniprot.org/annotation/VAR_082253|||http://purl.uniprot.org/annotation/VAR_082254|||http://purl.uniprot.org/annotation/VAR_082255|||http://purl.uniprot.org/annotation/VAR_082256|||http://purl.uniprot.org/annotation/VAR_082257|||http://purl.uniprot.org/annotation/VAR_082258|||http://purl.uniprot.org/annotation/VAR_082259|||http://purl.uniprot.org/annotation/VAR_082260|||http://purl.uniprot.org/annotation/VAR_082261|||http://purl.uniprot.org/annotation/VAR_082262|||http://purl.uniprot.org/annotation/VAR_082263|||http://purl.uniprot.org/annotation/VAR_082264|||http://purl.uniprot.org/annotation/VSP_011146|||http://purl.uniprot.org/annotation/VSP_015272
http://togogenome.org/gene/9606:ATG16L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAA4|||http://purl.uniprot.org/uniprot/Q9H7Q5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues|||Protein Atg16l2|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337110|||http://purl.uniprot.org/annotation/VAR_043605|||http://purl.uniprot.org/annotation/VSP_033904|||http://purl.uniprot.org/annotation/VSP_033905
http://togogenome.org/gene/9606:SLCO1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYB5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gain of pH-sensitivity of E1S transport.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191054|||http://purl.uniprot.org/annotation/VSP_042882|||http://purl.uniprot.org/annotation/VSP_045278|||http://purl.uniprot.org/annotation/VSP_045279
http://togogenome.org/gene/9606:PHLDA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  14 X 2 AA repeats of P-H|||15 X 2 AA repeats of P-Q|||Basic and acidic residues|||Basic residues|||Disordered|||PH|||Pleckstrin homology-like domain family A member 1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053897
http://togogenome.org/gene/9606:PITX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99697                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In ASGD4.|||In RDC; results in 25% loss of transactivation activity.|||In RIEG1.|||In RIEG1; more than 100-fold reduction in DNA binding activity as well as no detectable transactivation activity.|||In RIEG1; more than 200% increase in transactivation activity.|||In isoform PTX2A.|||In isoform PTX2C.|||Nuclear localization signal|||OAR|||Phosphothreonine; by PKB/AKT2|||Pituitary homeobox 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049223|||http://purl.uniprot.org/annotation/VAR_003762|||http://purl.uniprot.org/annotation/VAR_003763|||http://purl.uniprot.org/annotation/VAR_003764|||http://purl.uniprot.org/annotation/VAR_003765|||http://purl.uniprot.org/annotation/VAR_003766|||http://purl.uniprot.org/annotation/VAR_035027|||http://purl.uniprot.org/annotation/VAR_035028|||http://purl.uniprot.org/annotation/VAR_035029|||http://purl.uniprot.org/annotation/VAR_058735|||http://purl.uniprot.org/annotation/VAR_058736|||http://purl.uniprot.org/annotation/VAR_058737|||http://purl.uniprot.org/annotation/VAR_058738|||http://purl.uniprot.org/annotation/VAR_058739|||http://purl.uniprot.org/annotation/VAR_058740|||http://purl.uniprot.org/annotation/VAR_082833|||http://purl.uniprot.org/annotation/VSP_002260|||http://purl.uniprot.org/annotation/VSP_002261
http://togogenome.org/gene/9606:MED23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DL5|||http://purl.uniprot.org/uniprot/Q9ULK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In MRT18; specifically impairs the response of JUN and FOS immediate early genes to serum mitogens by altering the interaction between enhancer-bound transcription factors TCF7L2 and ELK1 and the Mediator complex.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||Mediator of RNA polymerase II transcription subunit 23|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079358|||http://purl.uniprot.org/annotation/VAR_082644|||http://purl.uniprot.org/annotation/VSP_004034|||http://purl.uniprot.org/annotation/VSP_004035|||http://purl.uniprot.org/annotation/VSP_004036|||http://purl.uniprot.org/annotation/VSP_004037|||http://purl.uniprot.org/annotation/VSP_028380|||http://purl.uniprot.org/annotation/VSP_047860|||http://purl.uniprot.org/annotation/VSP_047861
http://togogenome.org/gene/9606:ADAM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13443                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cleavage; by furin-like protease|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 9|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029062|||http://purl.uniprot.org/annotation/VSP_011057|||http://purl.uniprot.org/annotation/VSP_011058
http://togogenome.org/gene/9606:KRBOX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JUW0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||KRAB|||KRAB domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233994|||http://purl.uniprot.org/annotation/VSP_018163|||http://purl.uniprot.org/annotation/VSP_018164|||http://purl.uniprot.org/annotation/VSP_018165
http://togogenome.org/gene/9606:WDR38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0D8|||http://purl.uniprot.org/uniprot/A0A087X0J1|||http://purl.uniprot.org/uniprot/B7ZW23|||http://purl.uniprot.org/uniprot/B7ZW24|||http://purl.uniprot.org/uniprot/B9EK65|||http://purl.uniprot.org/uniprot/Q5JTN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294440|||http://purl.uniprot.org/annotation/VAR_053431|||http://purl.uniprot.org/annotation/VAR_053432
http://togogenome.org/gene/9606:FCRL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVJ9|||http://purl.uniprot.org/uniprot/B4E0W2|||http://purl.uniprot.org/uniprot/Q96LA5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 2|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014761|||http://purl.uniprot.org/annotation/PRO_5002801054|||http://purl.uniprot.org/annotation/PRO_5002803718|||http://purl.uniprot.org/annotation/VAR_049873|||http://purl.uniprot.org/annotation/VSP_014111|||http://purl.uniprot.org/annotation/VSP_014112|||http://purl.uniprot.org/annotation/VSP_014113|||http://purl.uniprot.org/annotation/VSP_014114|||http://purl.uniprot.org/annotation/VSP_014115|||http://purl.uniprot.org/annotation/VSP_014116|||http://purl.uniprot.org/annotation/VSP_014117|||http://purl.uniprot.org/annotation/VSP_014118
http://togogenome.org/gene/9606:SNAPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92966                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||snRNA-activating protein complex subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072024|||http://purl.uniprot.org/annotation/VAR_051366
http://togogenome.org/gene/9606:BAALC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Brain and acute leukemia cytoplasmic protein|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with CAMK2A|||N-myristoyl glycine|||Polar residues|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248205|||http://purl.uniprot.org/annotation/VAR_056741|||http://purl.uniprot.org/annotation/VSP_060712|||http://purl.uniprot.org/annotation/VSP_060713|||http://purl.uniprot.org/annotation/VSP_060714|||http://purl.uniprot.org/annotation/VSP_060715|||http://purl.uniprot.org/annotation/VSP_060716|||http://purl.uniprot.org/annotation/VSP_060717|||http://purl.uniprot.org/annotation/VSP_060718|||http://purl.uniprot.org/annotation/VSP_060719
http://togogenome.org/gene/9606:CALCOCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1Z2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C-terminal AD (CTNNB1 binding site); interaction with CCAR1|||Calcium-binding and coiled-coil domain-containing protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with GATA1|||N-terminal AD (CTNNB1 binding site)|||Phosphoserine|||UBZ1-type|||p300 KIX-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308899|||http://purl.uniprot.org/annotation/VAR_036881|||http://purl.uniprot.org/annotation/VSP_029052|||http://purl.uniprot.org/annotation/VSP_029053|||http://purl.uniprot.org/annotation/VSP_041471|||http://purl.uniprot.org/annotation/VSP_041472
http://togogenome.org/gene/9606:SYN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14994|||http://purl.uniprot.org/uniprot/Q17R54|||http://purl.uniprot.org/uniprot/Q59EX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  A|||B; linker|||C; actin-binding and synaptic-vesicle binding|||Disordered|||E|||In patients affected by schizophrenia.|||J; Pro-rich linker|||Phosphoserine|||Phosphoserine; by CDK1 and MAPK|||Phosphoserine; by PKA and CaMK1|||Polar residues|||Pro residues|||Synapsin ATP-binding|||Synapsin pre-ATP-grasp|||Synapsin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183024|||http://purl.uniprot.org/annotation/VAR_068906
http://togogenome.org/gene/9606:GRIN2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8D9PH81|||http://purl.uniprot.org/uniprot/H0Y2V8|||http://purl.uniprot.org/uniprot/O15398|||http://purl.uniprot.org/uniprot/Q14957|||http://purl.uniprot.org/uniprot/Q8IW23                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency.|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||Functional determinant of NMDA receptors|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 2C|||Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Pore-forming|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011580|||http://purl.uniprot.org/annotation/PRO_5014092429|||http://purl.uniprot.org/annotation/PRO_5027151620|||http://purl.uniprot.org/annotation/PRO_5034207459|||http://purl.uniprot.org/annotation/VAR_037634|||http://purl.uniprot.org/annotation/VAR_079958|||http://purl.uniprot.org/annotation/VAR_079959|||http://purl.uniprot.org/annotation/VAR_079960|||http://purl.uniprot.org/annotation/VAR_079961|||http://purl.uniprot.org/annotation/VAR_079962|||http://purl.uniprot.org/annotation/VAR_079963|||http://purl.uniprot.org/annotation/VAR_079964|||http://purl.uniprot.org/annotation/VAR_079965|||http://purl.uniprot.org/annotation/VAR_079966|||http://purl.uniprot.org/annotation/VAR_079967|||http://purl.uniprot.org/annotation/VAR_079968|||http://purl.uniprot.org/annotation/VAR_079969|||http://purl.uniprot.org/annotation/VAR_079970|||http://purl.uniprot.org/annotation/VAR_079971|||http://purl.uniprot.org/annotation/VAR_079972|||http://purl.uniprot.org/annotation/VAR_079973|||http://purl.uniprot.org/annotation/VAR_079974
http://togogenome.org/gene/9606:CHMP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LBR1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes interaction with SPAST and VPS4A; when associated with A-188.|||Abolishes interaction with SPAST and VPS4A; when associated with A-192.|||Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-178 and R-181.|||Abolishes interaction with SPAST and no effect on interaction with VPS4A; when associated with R-181 and R-184.|||Abolishes interaction with SPAScT and no effect on interaction with VPS4A; when associated with R-178 and R-184.|||Abolishes interaction with VPS4B.|||Charged multivesicular body protein 1b|||Decreases interaction with SPAST.|||Diminishes interaction with VPS4B.|||Disordered|||Interaction with IST1|||Interaction with SPAST|||Interaction with VPS4A, MITD1 and STAMBP|||Interaction with VPS4B|||Interaction with VTA1|||MIT-interacting motif|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211454
http://togogenome.org/gene/9606:CHD1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRH8|||http://purl.uniprot.org/uniprot/A0A0A0MSH9|||http://purl.uniprot.org/uniprot/Q86WJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ATP-dependent chromatin remodeler activity.|||Abolishes ATPase activity.|||Abrogates chromatin remodeling activity. Prevents PARP2 removal from chromatin.|||Acidic residues|||Basic and acidic residues|||Chromodomain-helicase-DNA-binding protein 1-like|||DEAH box|||Decreased interaction with nucleosomes.|||Disordered|||Disrupts interaction with PARP1. Abolishes the release from auto-inhibition through macro domain binding to the N-terminal ATPase module. Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-307, E-308 and E-398; E-319, E-320, E-407 and E-422.|||Does not reduce interaction of the macro domain with the N-terminal ATPase module; when associated with E-750.|||Found in patients with cancer; loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity.|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity.|||Macro|||Omega-N-methylarginine|||Phosphoserine|||Reduced interaction with histones.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-307, E-308 and E-750.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-319, E-320, E-407 and E-750.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-319, E-320, E-422 and E-750.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-398 and E-750.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-407; E-422 and E-750.|||Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-750.|||Regulatory linker segment (RLS)|||Required for ATPase activity|||Strongly reduced interaction with the acidic patch of histones.|||Strongly reduces poly(ADP-ribose)-binding but not ATPase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332141|||http://purl.uniprot.org/annotation/VAR_042954|||http://purl.uniprot.org/annotation/VAR_042955|||http://purl.uniprot.org/annotation/VAR_042956|||http://purl.uniprot.org/annotation/VAR_042957|||http://purl.uniprot.org/annotation/VAR_042958|||http://purl.uniprot.org/annotation/VAR_086613|||http://purl.uniprot.org/annotation/VAR_086614|||http://purl.uniprot.org/annotation/VAR_086615|||http://purl.uniprot.org/annotation/VAR_086616|||http://purl.uniprot.org/annotation/VSP_033340|||http://purl.uniprot.org/annotation/VSP_033341|||http://purl.uniprot.org/annotation/VSP_033342|||http://purl.uniprot.org/annotation/VSP_055675
http://togogenome.org/gene/9606:KIF5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33176|||http://purl.uniprot.org/uniprot/Q6P164|||http://purl.uniprot.org/uniprot/V9HW29                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Globular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kinesin motor|||Kinesin-1 heavy chain|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125351
http://togogenome.org/gene/9606:MMP23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75900                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes processing of soluble form.|||Cleavage; by furin-like protease|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||Lumenal|||Matrix metalloproteinase-23|||Matrix metalloproteinase-23, soluble form|||N-linked (GlcNAc...) asparagine|||ShKT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259513|||http://purl.uniprot.org/annotation/PRO_0000259514|||http://purl.uniprot.org/annotation/PRO_0000259515|||http://purl.uniprot.org/annotation/VAR_028948|||http://purl.uniprot.org/annotation/VSP_021411|||http://purl.uniprot.org/annotation/VSP_021412
http://togogenome.org/gene/9606:VAT1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K288|||http://purl.uniprot.org/uniprot/Q9HCJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Enoyl reductase (ER)|||Phosphoserine|||Phosphothreonine|||Synaptic vesicle membrane protein VAT-1 homolog-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160922
http://togogenome.org/gene/9606:RANGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46060|||http://purl.uniprot.org/uniprot/Q9BSK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Abolishes RANGTPase activation.|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hydrophobic interaction with UBE2I|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Loss of cross-link to SUMO1. Abolishes association with nuclear pores during interphase, and with mitotic spindles during mitosis.|||N-acetylalanine|||N6-acetyllysine; alternate|||No effect on phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK2|||Ran GTPase-activating protein 1|||Ran-GTPase activating protein 1 C-terminal|||Removed|||SUMO conjugation|||Strongly decreased phosphorylation. No effect on sumoylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056737|||http://purl.uniprot.org/annotation/VAR_029240
http://togogenome.org/gene/9606:NPEPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDH3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Probable aminopeptidase NPEPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165828|||http://purl.uniprot.org/annotation/VAR_059756|||http://purl.uniprot.org/annotation/VAR_059757|||http://purl.uniprot.org/annotation/VSP_007251|||http://purl.uniprot.org/annotation/VSP_007252|||http://purl.uniprot.org/annotation/VSP_007253|||http://purl.uniprot.org/annotation/VSP_007254|||http://purl.uniprot.org/annotation/VSP_044526|||http://purl.uniprot.org/annotation/VSP_044527
http://togogenome.org/gene/9606:TULP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0I9|||http://purl.uniprot.org/uniprot/O00294|||http://purl.uniprot.org/uniprot/Q0QD38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In LCA15.|||In RP14.|||In RP14; abolishes RPE phagocytosis.|||In RP14; no effect on RPE phagocytosis.|||In RP14; unknown pathological significance.|||In isoform 2.|||Tubby C-terminal|||Tubby-related protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186466|||http://purl.uniprot.org/annotation/VAR_007941|||http://purl.uniprot.org/annotation/VAR_007942|||http://purl.uniprot.org/annotation/VAR_007943|||http://purl.uniprot.org/annotation/VAR_008274|||http://purl.uniprot.org/annotation/VAR_008275|||http://purl.uniprot.org/annotation/VAR_008276|||http://purl.uniprot.org/annotation/VAR_008277|||http://purl.uniprot.org/annotation/VAR_008278|||http://purl.uniprot.org/annotation/VAR_008279|||http://purl.uniprot.org/annotation/VAR_008280|||http://purl.uniprot.org/annotation/VAR_008281|||http://purl.uniprot.org/annotation/VAR_013310|||http://purl.uniprot.org/annotation/VAR_034575|||http://purl.uniprot.org/annotation/VAR_037584|||http://purl.uniprot.org/annotation/VAR_065500|||http://purl.uniprot.org/annotation/VAR_065501|||http://purl.uniprot.org/annotation/VAR_065502|||http://purl.uniprot.org/annotation/VAR_065503|||http://purl.uniprot.org/annotation/VSP_023031
http://togogenome.org/gene/9606:IGLON5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGN9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||IgLON family member 5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332301
http://togogenome.org/gene/9606:IER5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VY09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Immediate early response gene 5 protein|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190438|||http://purl.uniprot.org/annotation/VAR_028404|||http://purl.uniprot.org/annotation/VAR_028405|||http://purl.uniprot.org/annotation/VAR_028406|||http://purl.uniprot.org/annotation/VAR_028407|||http://purl.uniprot.org/annotation/VAR_028408
http://togogenome.org/gene/9606:H4C15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:ZNF182                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17025                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in a child with sporadic epilepsy; unknown pathological significance.|||In isoform 2.|||KRAB|||Zinc finger protein 182                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047345|||http://purl.uniprot.org/annotation/VAR_077837|||http://purl.uniprot.org/annotation/VSP_043078
http://togogenome.org/gene/9606:SBNO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KN83                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein strawberry notch homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314555|||http://purl.uniprot.org/annotation/VAR_037910|||http://purl.uniprot.org/annotation/VAR_037911|||http://purl.uniprot.org/annotation/VAR_037912|||http://purl.uniprot.org/annotation/VAR_037913|||http://purl.uniprot.org/annotation/VAR_057794|||http://purl.uniprot.org/annotation/VSP_030295|||http://purl.uniprot.org/annotation/VSP_030296|||http://purl.uniprot.org/annotation/VSP_030297|||http://purl.uniprot.org/annotation/VSP_030298
http://togogenome.org/gene/9606:ADAMTSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TH1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  ADAMTS-like protein 2|||Disordered|||In GPHYSD1.|||In GPHYSD1; leads to the reduced secretion of the mutated protein.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||PLAC|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249682|||http://purl.uniprot.org/annotation/VAR_046011|||http://purl.uniprot.org/annotation/VAR_054874|||http://purl.uniprot.org/annotation/VAR_054875|||http://purl.uniprot.org/annotation/VAR_054876|||http://purl.uniprot.org/annotation/VAR_054877|||http://purl.uniprot.org/annotation/VAR_066543|||http://purl.uniprot.org/annotation/VAR_066544|||http://purl.uniprot.org/annotation/VAR_066545|||http://purl.uniprot.org/annotation/VAR_066546|||http://purl.uniprot.org/annotation/VAR_066547|||http://purl.uniprot.org/annotation/VAR_066548|||http://purl.uniprot.org/annotation/VAR_066549|||http://purl.uniprot.org/annotation/VAR_066550|||http://purl.uniprot.org/annotation/VAR_066551|||http://purl.uniprot.org/annotation/VAR_066552|||http://purl.uniprot.org/annotation/VAR_066553
http://togogenome.org/gene/9606:ZFAND6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FIF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||AN1-type|||AN1-type zinc finger protein 6|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245235|||http://purl.uniprot.org/annotation/VSP_019652
http://togogenome.org/gene/9606:PRSS48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ1|||http://purl.uniprot.org/uniprot/Q7RTY5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000095975|||http://purl.uniprot.org/annotation/PRO_5007491737|||http://purl.uniprot.org/annotation/VAR_042920|||http://purl.uniprot.org/annotation/VAR_042921|||http://purl.uniprot.org/annotation/VAR_042922|||http://purl.uniprot.org/annotation/VSP_033287
http://togogenome.org/gene/9606:GLYCTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVS8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycerate kinase|||In D-GA; the mutant protein is not expressed and has no enzymatic activity.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287192|||http://purl.uniprot.org/annotation/VAR_032285|||http://purl.uniprot.org/annotation/VAR_032286|||http://purl.uniprot.org/annotation/VAR_061205|||http://purl.uniprot.org/annotation/VAR_065909|||http://purl.uniprot.org/annotation/VSP_025356|||http://purl.uniprot.org/annotation/VSP_025357|||http://purl.uniprot.org/annotation/VSP_025358|||http://purl.uniprot.org/annotation/VSP_025359|||http://purl.uniprot.org/annotation/VSP_025360|||http://purl.uniprot.org/annotation/VSP_025361|||http://purl.uniprot.org/annotation/VSP_025362|||http://purl.uniprot.org/annotation/VSP_025363|||http://purl.uniprot.org/annotation/VSP_025364|||http://purl.uniprot.org/annotation/VSP_025365
http://togogenome.org/gene/9606:CPM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14384                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%.|||5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability.|||Abolishes enzyme activity.|||Carboxypeptidase M|||Expressed on cell membrane. Released from membrane by PI-PLC.|||GPI-anchor amidated serine|||Little expression on cell membrane. Perinuclear localization. Not released from membrane by PI-PLC.|||N-linked (GlcNAc...) asparagine|||Probable structural role|||Proton donor/acceptor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004391|||http://purl.uniprot.org/annotation/PRO_0000251910|||http://purl.uniprot.org/annotation/VAR_048600|||http://purl.uniprot.org/annotation/VAR_048601
http://togogenome.org/gene/9606:BZW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LIC9|||http://purl.uniprot.org/uniprot/Q7L1Q6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||W2|||eIF5-mimic protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254609|||http://purl.uniprot.org/annotation/VSP_021266|||http://purl.uniprot.org/annotation/VSP_043568|||http://purl.uniprot.org/annotation/VSP_043569
http://togogenome.org/gene/9606:PA2G4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ80                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases in vitro phosphorylation by PKC.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RNA|||Loss of nucleolar localization.|||Loss of phosphorylation and interaction with ERBB3 and HUWE1.|||N-acetylserine|||Necessary for nucleolar localization|||No effect on in vitro phosphorylation by PKC.|||No effect on phosphorylation and loss of nucleolar localization.|||Only partial nucleolar localization.|||Phosphoserine|||Phosphoserine; by PKC/PRKCD|||Phosphothreonine|||Proliferation-associated protein 2G4|||RNA-binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148989|||http://purl.uniprot.org/annotation/VSP_057325
http://togogenome.org/gene/9606:PPP1R15B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSH1|||http://purl.uniprot.org/uniprot/Q5SWA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Found in a patient with isolated coloboma; unknown pathological significance.|||In MSSGM2; no effect on localization; increased protein abundance; loss of interaction with protein phosphatase catalytic subunit PP1; decreased dephosphorylation of EIF2S1.|||Phosphoserine|||Polar residues|||Protein phosphatase 1 regulatory subunit 15A/B C-terminal|||Protein phosphatase 1 regulatory subunit 15B|||Protein phosphatase 1 regulatory subunit 15B N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320520|||http://purl.uniprot.org/annotation/VAR_039196|||http://purl.uniprot.org/annotation/VAR_039197|||http://purl.uniprot.org/annotation/VAR_039198|||http://purl.uniprot.org/annotation/VAR_039199|||http://purl.uniprot.org/annotation/VAR_039200|||http://purl.uniprot.org/annotation/VAR_074072|||http://purl.uniprot.org/annotation/VAR_079851
http://togogenome.org/gene/9606:ZSWIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR11                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  SWIM-type|||Zinc finger SWIM domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223095|||http://purl.uniprot.org/annotation/VAR_020445
http://togogenome.org/gene/9606:BCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11274                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with FES and GRB2.|||Abolishes interaction with PDZK1.|||Binding to ABL SH2-domain|||Breakpoint cluster region protein|||Breakpoint for translocation to form BCR-ABL oncogene|||C2|||DH|||Disordered|||In a bladder transitional cell carcinoma sample; somatic mutation.|||In isoform 2.|||Kinase|||Loss of GAP activity. Loss of GAP activity; when associated with A-1202.|||Loss of GAP activity; when associated with A-1090.|||Loss of RHOAGEF activity.|||N-acetylmethionine|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FES|||Phosphotyrosine; by HCK|||Polar residues|||Reduces interaction with PDZK1. Abolishes interaction with DLG4. No effect on synaptic localization.|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080933|||http://purl.uniprot.org/annotation/VAR_031552|||http://purl.uniprot.org/annotation/VAR_031553|||http://purl.uniprot.org/annotation/VAR_031554|||http://purl.uniprot.org/annotation/VAR_041883|||http://purl.uniprot.org/annotation/VAR_041884|||http://purl.uniprot.org/annotation/VAR_041885|||http://purl.uniprot.org/annotation/VAR_041886|||http://purl.uniprot.org/annotation/VAR_041887|||http://purl.uniprot.org/annotation/VAR_041888|||http://purl.uniprot.org/annotation/VAR_041889|||http://purl.uniprot.org/annotation/VAR_041890|||http://purl.uniprot.org/annotation/VAR_041891|||http://purl.uniprot.org/annotation/VAR_041892|||http://purl.uniprot.org/annotation/VAR_041893|||http://purl.uniprot.org/annotation/VAR_041894|||http://purl.uniprot.org/annotation/VAR_041895|||http://purl.uniprot.org/annotation/VAR_041896|||http://purl.uniprot.org/annotation/VAR_041897|||http://purl.uniprot.org/annotation/VAR_051983|||http://purl.uniprot.org/annotation/VSP_024352
http://togogenome.org/gene/9606:RHOQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17081                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active. Interacts with PARD6 proteins and GOPC.|||Cysteine methyl ester|||Effector region|||Loss of interaction with GOPC.|||Removed in mature form|||Rho-related GTP-binding protein RhoQ|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198871|||http://purl.uniprot.org/annotation/PRO_0000281222
http://togogenome.org/gene/9606:POLR1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTY1|||http://purl.uniprot.org/uniprot/P0DPB5|||http://purl.uniprot.org/uniprot/P0DPB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerases I and III subunit RPAC2|||Disordered|||In TCS2.|||N-acetylmethionine|||Phosphoserine|||Protein POLR1D, isoform 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149316|||http://purl.uniprot.org/annotation/PRO_0000442287|||http://purl.uniprot.org/annotation/VAR_064892|||http://purl.uniprot.org/annotation/VAR_064893|||http://purl.uniprot.org/annotation/VAR_064894|||http://purl.uniprot.org/annotation/VAR_064895|||http://purl.uniprot.org/annotation/VAR_064896|||http://purl.uniprot.org/annotation/VAR_064897|||http://purl.uniprot.org/annotation/VAR_064898
http://togogenome.org/gene/9606:OR2T33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG76                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150507|||http://purl.uniprot.org/annotation/VAR_053159
http://togogenome.org/gene/9606:TIMM50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FCP1 homology|||Helical|||In MGCA9; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Mitochondrial import inner membrane translocase subunit TIM50|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043115|||http://purl.uniprot.org/annotation/VAR_078568|||http://purl.uniprot.org/annotation/VAR_078569|||http://purl.uniprot.org/annotation/VSP_016389|||http://purl.uniprot.org/annotation/VSP_047682|||http://purl.uniprot.org/annotation/VSP_047683
http://togogenome.org/gene/9606:TNFAIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13829                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CUL3 and induces abnormal actin stress fibers.|||BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2|||Disordered|||Does not affect phosphorylation level.|||Does not affect phosphorylation level; when associated with A-142.|||Does not affect phosphorylation level; when associated with A-237.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by CK2|||Slightly impairs phosphorylation level.|||Strongly impairs phosphorylation level.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191300|||http://purl.uniprot.org/annotation/VSP_056029
http://togogenome.org/gene/9606:PLEK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08567                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEP|||N6-acetyllysine|||PH 1|||PH 2|||Phosphoserine; by PKC|||Pleckstrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053859|||http://purl.uniprot.org/annotation/VAR_005524|||http://purl.uniprot.org/annotation/VAR_027797|||http://purl.uniprot.org/annotation/VAR_027798|||http://purl.uniprot.org/annotation/VAR_027799|||http://purl.uniprot.org/annotation/VAR_056666
http://togogenome.org/gene/9606:MEP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL91|||http://purl.uniprot.org/uniprot/Q16819                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Interchain|||MAM|||MATH|||Meprin A subunit alpha|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Peptidase M12A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028877|||http://purl.uniprot.org/annotation/PRO_0000028878|||http://purl.uniprot.org/annotation/VAR_020056|||http://purl.uniprot.org/annotation/VAR_021846|||http://purl.uniprot.org/annotation/VAR_033492|||http://purl.uniprot.org/annotation/VAR_033493|||http://purl.uniprot.org/annotation/VAR_051583
http://togogenome.org/gene/9606:CCHCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7G6|||http://purl.uniprot.org/uniprot/Q2TB68|||http://purl.uniprot.org/uniprot/Q769H0|||http://purl.uniprot.org/uniprot/Q8TD31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil alpha-helical rod protein 1|||Disordered|||In allele HCR*WWCC; associated with psoriasis.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089416|||http://purl.uniprot.org/annotation/VAR_017761|||http://purl.uniprot.org/annotation/VAR_017762|||http://purl.uniprot.org/annotation/VAR_017763|||http://purl.uniprot.org/annotation/VAR_017764|||http://purl.uniprot.org/annotation/VAR_017765|||http://purl.uniprot.org/annotation/VAR_017766|||http://purl.uniprot.org/annotation/VAR_017767|||http://purl.uniprot.org/annotation/VAR_017768|||http://purl.uniprot.org/annotation/VAR_017769|||http://purl.uniprot.org/annotation/VAR_017770|||http://purl.uniprot.org/annotation/VAR_017771|||http://purl.uniprot.org/annotation/VAR_017772|||http://purl.uniprot.org/annotation/VAR_017782|||http://purl.uniprot.org/annotation/VAR_017783|||http://purl.uniprot.org/annotation/VAR_017784|||http://purl.uniprot.org/annotation/VSP_038062|||http://purl.uniprot.org/annotation/VSP_047069
http://togogenome.org/gene/9606:QRFP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83859                                                                                  ^@                                                                                  Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Phenylalanine amide|||Pyrrolidone carboxylic acid|||QRF-amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010086|||http://purl.uniprot.org/annotation/PRO_0000010087|||http://purl.uniprot.org/annotation/VAR_049184
http://togogenome.org/gene/9606:EAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ELL-associated factor 1|||In isoform 2.|||Necessary for transactivation activity|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130334|||http://purl.uniprot.org/annotation/VSP_056193|||http://purl.uniprot.org/annotation/VSP_056194
http://togogenome.org/gene/9606:SMYD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN46|||http://purl.uniprot.org/uniprot/Q9H7B4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C-terminal domain; essential for histone methyltransferase activity, nuclear localization and mediates interaction with HSP90AA1|||Histone-lysine N-methyltransferase SMYD3|||In isoform 2.|||In isoform 3.|||MYND-type|||N-acetylmethionine|||Phosphothreonine|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218312|||http://purl.uniprot.org/annotation/VSP_012416|||http://purl.uniprot.org/annotation/VSP_012417|||http://purl.uniprot.org/annotation/VSP_035601
http://togogenome.org/gene/9606:ACOT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9L9                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal succinyl-coenzyme A thioesterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202149|||http://purl.uniprot.org/annotation/VAR_052300|||http://purl.uniprot.org/annotation/VAR_052301
http://togogenome.org/gene/9606:STX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13277|||http://purl.uniprot.org/uniprot/Q53YE2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with congenital cataract and developmental delay; unknown pathological significance.|||Helical|||Helical; Anchor for type IV membrane protein|||In DIAR12; loss of expression.|||In isoform 3.|||In isoform B.|||Syntaxin-3|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210199|||http://purl.uniprot.org/annotation/VAR_028189|||http://purl.uniprot.org/annotation/VAR_052246|||http://purl.uniprot.org/annotation/VAR_052247|||http://purl.uniprot.org/annotation/VAR_086135|||http://purl.uniprot.org/annotation/VAR_086136|||http://purl.uniprot.org/annotation/VSP_006340|||http://purl.uniprot.org/annotation/VSP_043187
http://togogenome.org/gene/9606:R3HCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3T6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||R3H|||R3H and coiled-coil domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307389|||http://purl.uniprot.org/annotation/VAR_035420|||http://purl.uniprot.org/annotation/VAR_035421|||http://purl.uniprot.org/annotation/VAR_035422|||http://purl.uniprot.org/annotation/VAR_035423|||http://purl.uniprot.org/annotation/VSP_058566
http://togogenome.org/gene/9606:CLCNKA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51800                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CBS 1|||CBS 2|||Calcium insensitive.|||Chloride channel protein ClC-Ka|||Cytoplasmic|||Helical|||In BARTS4B; a patient also carrying a mutation in CLCNKB.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094455|||http://purl.uniprot.org/annotation/VAR_014465|||http://purl.uniprot.org/annotation/VAR_019787|||http://purl.uniprot.org/annotation/VAR_019788|||http://purl.uniprot.org/annotation/VAR_030784|||http://purl.uniprot.org/annotation/VAR_033768|||http://purl.uniprot.org/annotation/VAR_048695|||http://purl.uniprot.org/annotation/VAR_059209|||http://purl.uniprot.org/annotation/VAR_061095|||http://purl.uniprot.org/annotation/VAR_063074|||http://purl.uniprot.org/annotation/VAR_068971|||http://purl.uniprot.org/annotation/VSP_044700|||http://purl.uniprot.org/annotation/VSP_045795
http://togogenome.org/gene/9606:SLC10A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5PT55                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sodium/bile acid cotransporter 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263745|||http://purl.uniprot.org/annotation/VAR_050230
http://togogenome.org/gene/9606:LENG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BZ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Leukocyte receptor cluster member 1|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254627|||http://purl.uniprot.org/annotation/VAR_051090
http://togogenome.org/gene/9606:NACC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BF6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region                                                                                  ^@                                                                                  BEN|||BTB|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nucleus accumbens-associated protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263668
http://togogenome.org/gene/9606:ALG10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5I7T1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Putative Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215448|||http://purl.uniprot.org/annotation/VAR_023753|||http://purl.uniprot.org/annotation/VAR_048217|||http://purl.uniprot.org/annotation/VAR_061002
http://togogenome.org/gene/9606:IL17RE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMZ3|||http://purl.uniprot.org/uniprot/Q8NFR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interleukin-17 receptor C/E N-terminal|||Interleukin-17 receptor E|||N-linked (GlcNAc...) asparagine|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309467|||http://purl.uniprot.org/annotation/PRO_5002803430|||http://purl.uniprot.org/annotation/VAR_036956|||http://purl.uniprot.org/annotation/VAR_036957|||http://purl.uniprot.org/annotation/VAR_036958|||http://purl.uniprot.org/annotation/VSP_029190|||http://purl.uniprot.org/annotation/VSP_029191|||http://purl.uniprot.org/annotation/VSP_029192|||http://purl.uniprot.org/annotation/VSP_029193|||http://purl.uniprot.org/annotation/VSP_029194|||http://purl.uniprot.org/annotation/VSP_029195|||http://purl.uniprot.org/annotation/VSP_029196
http://togogenome.org/gene/9606:EFNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43921                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Ephrin RBD|||Ephrin-A2|||GPI-anchor amidated asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008361|||http://purl.uniprot.org/annotation/PRO_0000008362
http://togogenome.org/gene/9606:HMGN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05204                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylserine; alternate|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In variant H17.|||N6-acetyllysine; alternate|||Non-histone chromosomal protein HMG-17|||Phosphoserine|||Phosphoserine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206697|||http://purl.uniprot.org/annotation/VAR_003716
http://togogenome.org/gene/9606:RWDD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57060                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Strand                                                                                  ^@                                                                                  Phosphoserine|||RWD|||RWD domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079504
http://togogenome.org/gene/9606:OR7C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWU6|||http://purl.uniprot.org/uniprot/O76099                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150646|||http://purl.uniprot.org/annotation/VAR_024111|||http://purl.uniprot.org/annotation/VAR_024112|||http://purl.uniprot.org/annotation/VAR_053232|||http://purl.uniprot.org/annotation/VAR_053233
http://togogenome.org/gene/9606:ZBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H171                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Polar residues|||RIP homotypic interaction motif (RHIM) 1|||RIP homotypic interaction motif (RHIM) 2|||Z-DNA-binding protein 1|||Z-binding 1|||Z-binding 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066564|||http://purl.uniprot.org/annotation/VAR_014316|||http://purl.uniprot.org/annotation/VAR_057030|||http://purl.uniprot.org/annotation/VAR_057031|||http://purl.uniprot.org/annotation/VAR_057032|||http://purl.uniprot.org/annotation/VAR_057033|||http://purl.uniprot.org/annotation/VAR_061728|||http://purl.uniprot.org/annotation/VAR_061729|||http://purl.uniprot.org/annotation/VAR_069138|||http://purl.uniprot.org/annotation/VSP_004078|||http://purl.uniprot.org/annotation/VSP_004079|||http://purl.uniprot.org/annotation/VSP_004080|||http://purl.uniprot.org/annotation/VSP_004081|||http://purl.uniprot.org/annotation/VSP_004082|||http://purl.uniprot.org/annotation/VSP_045405|||http://purl.uniprot.org/annotation/VSP_045406|||http://purl.uniprot.org/annotation/VSP_046081
http://togogenome.org/gene/9606:EMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCB8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Embigin|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014749|||http://purl.uniprot.org/annotation/VSP_055593
http://togogenome.org/gene/9606:PDE7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP56                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||PDEase|||Phosphoserine|||Proton donor|||cAMP-specific 3',5'-cyclic phosphodiesterase 7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198836
http://togogenome.org/gene/9606:DDX23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY11|||http://purl.uniprot.org/uniprot/Q9BUQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Probable ATP-dependent RNA helicase DDX23|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055128|||http://purl.uniprot.org/annotation/VSP_056575|||http://purl.uniprot.org/annotation/VSP_056576
http://togogenome.org/gene/9606:AURKC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQB9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aurora kinase C|||Disordered|||Impairs kinase activity, and keeps AURKC with the chromosomes until the end of mitosis.|||Impairs kinase activity.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with BIRC5|||Phosphothreonine; by PKA|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085660|||http://purl.uniprot.org/annotation/VAR_040385|||http://purl.uniprot.org/annotation/VAR_040386|||http://purl.uniprot.org/annotation/VAR_040387|||http://purl.uniprot.org/annotation/VSP_004872|||http://purl.uniprot.org/annotation/VSP_041095
http://togogenome.org/gene/9606:SLC35C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQH0|||http://purl.uniprot.org/uniprot/Q96A29                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  GDP-fucose transporter 1|||Helical|||In CDG2C.|||In CDG2C; does not rescue defective fucosylation in cells lacking GDP-fucose transport.|||In isoform 2.|||Sugar phosphate transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213391|||http://purl.uniprot.org/annotation/VAR_012347|||http://purl.uniprot.org/annotation/VAR_012348|||http://purl.uniprot.org/annotation/VAR_057302|||http://purl.uniprot.org/annotation/VAR_057303|||http://purl.uniprot.org/annotation/VSP_047116
http://togogenome.org/gene/9606:FAM81B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LP2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM81B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265122|||http://purl.uniprot.org/annotation/VAR_057968|||http://purl.uniprot.org/annotation/VAR_057969|||http://purl.uniprot.org/annotation/VAR_057970|||http://purl.uniprot.org/annotation/VAR_057971
http://togogenome.org/gene/9606:PHTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3S3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 3, isoform 4, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||PHTF|||Polar residues|||Protein PHTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318509|||http://purl.uniprot.org/annotation/VSP_031192|||http://purl.uniprot.org/annotation/VSP_031193|||http://purl.uniprot.org/annotation/VSP_031194|||http://purl.uniprot.org/annotation/VSP_046275|||http://purl.uniprot.org/annotation/VSP_046276|||http://purl.uniprot.org/annotation/VSP_057299|||http://purl.uniprot.org/annotation/VSP_057300
http://togogenome.org/gene/9606:MKI67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46013                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  16 X 122 AA approximate repeats|||Basic and acidic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform Short.|||K167R 1|||K167R 10|||K167R 11|||K167R 12|||K167R 13|||K167R 14|||K167R 15|||K167R 16|||K167R 2|||K167R 3|||K167R 4|||K167R 5|||K167R 6|||K167R 7|||K167R 8|||K167R 9|||N6-acetyllysine|||PP1-binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proliferation marker protein Ki-67                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084301|||http://purl.uniprot.org/annotation/VAR_014858|||http://purl.uniprot.org/annotation/VAR_014859|||http://purl.uniprot.org/annotation/VAR_020047|||http://purl.uniprot.org/annotation/VAR_021838|||http://purl.uniprot.org/annotation/VAR_024161|||http://purl.uniprot.org/annotation/VAR_024162|||http://purl.uniprot.org/annotation/VAR_024163|||http://purl.uniprot.org/annotation/VAR_024164|||http://purl.uniprot.org/annotation/VAR_024165|||http://purl.uniprot.org/annotation/VAR_024166|||http://purl.uniprot.org/annotation/VAR_024167|||http://purl.uniprot.org/annotation/VAR_029055|||http://purl.uniprot.org/annotation/VAR_029056|||http://purl.uniprot.org/annotation/VAR_029057|||http://purl.uniprot.org/annotation/VAR_029058|||http://purl.uniprot.org/annotation/VAR_029059|||http://purl.uniprot.org/annotation/VAR_029060|||http://purl.uniprot.org/annotation/VAR_029061|||http://purl.uniprot.org/annotation/VAR_029062|||http://purl.uniprot.org/annotation/VAR_029063|||http://purl.uniprot.org/annotation/VAR_029064|||http://purl.uniprot.org/annotation/VAR_029065|||http://purl.uniprot.org/annotation/VAR_029066|||http://purl.uniprot.org/annotation/VAR_029067|||http://purl.uniprot.org/annotation/VAR_029068|||http://purl.uniprot.org/annotation/VAR_029069|||http://purl.uniprot.org/annotation/VAR_029070|||http://purl.uniprot.org/annotation/VAR_029071|||http://purl.uniprot.org/annotation/VAR_029072|||http://purl.uniprot.org/annotation/VAR_029073|||http://purl.uniprot.org/annotation/VAR_029074|||http://purl.uniprot.org/annotation/VAR_033995|||http://purl.uniprot.org/annotation/VAR_033996|||http://purl.uniprot.org/annotation/VAR_033997|||http://purl.uniprot.org/annotation/VAR_061671|||http://purl.uniprot.org/annotation/VSP_004298
http://togogenome.org/gene/9606:TFEB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QYS6|||http://purl.uniprot.org/uniprot/P19484                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by Coxsackievirus B3 protease 3C|||Abolished ability to bind eltrombopag drug.|||Abolished alkylation, abolishing ability to prevent association with 14-3-3/YWHA adapters.|||Abolished nuclear export in response to nutrient availability.|||Abolished nuclear localization upon mTORC1 inactivation.|||Abolished recruitment to lysosomal membrane in response to nutrients, leading to constitutive nuclear localization.|||BHLH|||Disordered|||Does not affect interaction with 14-3-3/YWHA and subcellular localization.|||Does not affect nuclear localization.|||Does not affect recruitment to lysosomal membrane in response to nutrients.|||Impaired cleavage by Coxsackievirus B3 protease 3C.|||Impaired nuclear export in response to nutrient availability.|||Impaired phosphorylation by MTOR, leading to constitutive nuclear localization and transcription factor activity. Impaired nuclear export in response to nutrient availability.|||Impaired phosphorylation by MTOR, leading to reduced interaction with 14-3-3/YWHA and constitutive nuclear localization. Does not affect nuclear export in response to nutrient availability.|||In MutCom_1 mutant; abolished ability to bind eltrombopag drug; when associated with 248-A--A-254.|||In MutCom_1 mutant; abolished ability to bind eltrombopag drug; when associated with 271-A--A-274.|||In MutCom_2 mutant; does not affect ability to bind eltrombopag drug.|||In MutCom_3 mutant; does not affect ability to bind eltrombopag drug.|||In MutCom_4 mutant; does not affect ability to bind eltrombopag drug.|||In isoform 2.|||Leucine-zipper|||Mimics phosphorylation status; abolished translocation to the nucleus in response to starvation.|||Mimics phosphorylation; leading to increased interaction with 14-3-3/YWHA and impaired nuclear localization.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Pro residues|||S-(2,3-dicarboxypropyl)cysteine|||Strong transcription activation domain|||Transcription factor EB|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127473|||http://purl.uniprot.org/annotation/VSP_002159
http://togogenome.org/gene/9606:TIGAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ88                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.|||Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.|||Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.|||Fructose-2,6-bisphosphatase TIGAR|||Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.|||N6-acetyllysine|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179957
http://togogenome.org/gene/9606:TMEM81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P7N7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 81                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287876|||http://purl.uniprot.org/annotation/VAR_032353|||http://purl.uniprot.org/annotation/VAR_032354
http://togogenome.org/gene/9606:CUL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWT3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cullin-9|||DOC|||Disordered|||IBR-type|||In isoform 2.|||Phosphoserine|||Polar residues|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119815|||http://purl.uniprot.org/annotation/VAR_048844|||http://purl.uniprot.org/annotation/VAR_048845|||http://purl.uniprot.org/annotation/VSP_009573
http://togogenome.org/gene/9606:TRAPPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5R8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In a melanoma.|||Trafficking protein particle complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211562|||http://purl.uniprot.org/annotation/VAR_013028
http://togogenome.org/gene/9606:TLCD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MV1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N6-acetyllysine|||TLC|||TLC domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286701
http://togogenome.org/gene/9606:SEMA7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMH6|||http://purl.uniprot.org/uniprot/F5GYX3|||http://purl.uniprot.org/uniprot/O75326                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ITGB1-dependent enhancement of axon growth; when associated with E-269.|||Abolishes ITGB1-dependent enhancement of axon growth; when associated with K-267.|||Asymmetric dimethylarginine|||Cell attachment site|||Disordered|||GPI-anchor amidated alanine|||Ig-like|||Ig-like C2-type|||In PFIC11.|||In isoform 2.|||Interaction with integrins|||N-linked (GlcNAc...) asparagine|||Pro residues|||Removed in mature form|||Results in JMH-variant phenotype.|||Sema|||Semaphorin-7A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032347|||http://purl.uniprot.org/annotation/PRO_0000032348|||http://purl.uniprot.org/annotation/VAR_029282|||http://purl.uniprot.org/annotation/VAR_038836|||http://purl.uniprot.org/annotation/VAR_038837|||http://purl.uniprot.org/annotation/VAR_038838|||http://purl.uniprot.org/annotation/VAR_038839|||http://purl.uniprot.org/annotation/VAR_068679|||http://purl.uniprot.org/annotation/VAR_087326|||http://purl.uniprot.org/annotation/VSP_045349
http://togogenome.org/gene/9606:CCDC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KR35|||http://purl.uniprot.org/uniprot/Q8WUD4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 12|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076191
http://togogenome.org/gene/9606:VSTM2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N03                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Ig-like|||In isoform 2.|||In isoform 3.|||V-set and transmembrane domain-containing protein 2-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015164|||http://purl.uniprot.org/annotation/VSP_013380|||http://purl.uniprot.org/annotation/VSP_026512|||http://purl.uniprot.org/annotation/VSP_026513|||http://purl.uniprot.org/annotation/VSP_026514
http://togogenome.org/gene/9606:GPR176                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14439                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 176|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069656|||http://purl.uniprot.org/annotation/VSP_058845|||http://purl.uniprot.org/annotation/VSP_058846
http://togogenome.org/gene/9606:SHE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ18                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||SH2|||SH2 domain-containing adapter protein E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246775
http://togogenome.org/gene/9606:TSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWH7|||http://purl.uniprot.org/uniprot/H3BMQ0|||http://purl.uniprot.org/uniprot/P49815|||http://purl.uniprot.org/uniprot/X5D7Q2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes AMPK-mediated phosphorylation; when associated with A-1271.|||Abolishes AMPK-mediated phosphorylation; when associated with A-1387.|||Abolishes GAP activity.|||Basic and acidic residues|||Could be associated with TSC2.|||Decreased GTPase-activating protein activity.|||Disordered|||In FCORD2; somatic mutation; decreased function in negative regulation of TOR signaling; does not affect interaction with TSC1.|||In TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420; enhances ubiquitination by MYCBP2.|||In TSC2.|||In TSC2; Abolishes GAP activity.|||In TSC2; greatly reduces the ability to enhance the RHEBGTPase activity.|||In TSC2; impairs phosphorylation at S-1387, S-1418 and S-1420.|||In TSC2; impairs repression of EIF4EBP1 phosphorylation.|||In TSC2; unknown pathological significance.|||In isoform 2, isoform 6 and isoform 7.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Inhibits insulin-stimulated phosphorylation and activation of RPS6KB1; when associated with A-1462.|||Inhibits insulin-stimulated phosphorylation and activation of RPS6KB1; when associated with A-939.|||No effect.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by PKB/AKT1|||Phosphoserine; by RPS6KA1|||Phosphothreonine|||Phosphothreonine; by AMPK|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Rap-GAP|||Required for interaction with TSC1|||Tuberin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065654|||http://purl.uniprot.org/annotation/VAR_005646|||http://purl.uniprot.org/annotation/VAR_005647|||http://purl.uniprot.org/annotation/VAR_005648|||http://purl.uniprot.org/annotation/VAR_005649|||http://purl.uniprot.org/annotation/VAR_005650|||http://purl.uniprot.org/annotation/VAR_005651|||http://purl.uniprot.org/annotation/VAR_005652|||http://purl.uniprot.org/annotation/VAR_005653|||http://purl.uniprot.org/annotation/VAR_005654|||http://purl.uniprot.org/annotation/VAR_005655|||http://purl.uniprot.org/annotation/VAR_005656|||http://purl.uniprot.org/annotation/VAR_005657|||http://purl.uniprot.org/annotation/VAR_005658|||http://purl.uniprot.org/annotation/VAR_005659|||http://purl.uniprot.org/annotation/VAR_005660|||http://purl.uniprot.org/annotation/VAR_005661|||http://purl.uniprot.org/annotation/VAR_005662|||http://purl.uniprot.org/annotation/VAR_005663|||http://purl.uniprot.org/annotation/VAR_005664|||http://purl.uniprot.org/annotation/VAR_005665|||http://purl.uniprot.org/annotation/VAR_005666|||http://purl.uniprot.org/annotation/VAR_005667|||http://purl.uniprot.org/annotation/VAR_008019|||http://purl.uniprot.org/annotation/VAR_008020|||http://purl.uniprot.org/annotation/VAR_008021|||http://purl.uniprot.org/annotation/VAR_008022|||http://purl.uniprot.org/annotation/VAR_008023|||http://purl.uniprot.org/annotation/VAR_008024|||http://purl.uniprot.org/annotation/VAR_008025|||http://purl.uniprot.org/annotation/VAR_008026|||http://purl.uniprot.org/annotation/VAR_008027|||http://purl.uniprot.org/annotation/VAR_008028|||http://purl.uniprot.org/annotation/VAR_008029|||http://purl.uniprot.org/annotation/VAR_008030|||http://purl.uniprot.org/annotation/VAR_008031|||http://purl.uniprot.org/annotation/VAR_008032|||http://purl.uniprot.org/annotation/VAR_008033|||http://purl.uniprot.org/annotation/VAR_009415|||http://purl.uniprot.org/annotation/VAR_009416|||http://purl.uniprot.org/annotation/VAR_009417|||http://purl.uniprot.org/annotation/VAR_009418|||http://purl.uniprot.org/annotation/VAR_009419|||http://purl.uniprot.org/annotation/VAR_009420|||http://purl.uniprot.org/annotation/VAR_009421|||http://purl.uniprot.org/annotation/VAR_009422|||http://purl.uniprot.org/annotation/VAR_009423|||http://purl.uniprot.org/annotation/VAR_009424|||http://purl.uniprot.org/annotation/VAR_009425|||http://purl.uniprot.org/annotation/VAR_009426|||http://purl.uniprot.org/annotation/VAR_009427|||http://purl.uniprot.org/annotation/VAR_009428|||http://purl.uniprot.org/annotation/VAR_009429|||http://purl.uniprot.org/annotation/VAR_009430|||http://purl.uniprot.org/annotation/VAR_009431|||http://purl.uniprot.org/annotation/VAR_009432|||http://purl.uniprot.org/annotation/VAR_009433|||http://purl.uniprot.org/annotation/VAR_009434|||http://purl.uniprot.org/annotation/VAR_009435|||http://purl.uniprot.org/annotation/VAR_009436|||http://purl.uniprot.org/annotation/VAR_009437|||http://purl.uniprot.org/annotation/VAR_009438|||http://purl.uniprot.org/annotation/VAR_009439|||http://purl.uniprot.org/annotation/VAR_009440|||http://purl.uniprot.org/annotation/VAR_009441|||http://purl.uniprot.org/annotation/VAR_009442|||http://purl.uniprot.org/annotation/VAR_009443|||http://purl.uniprot.org/annotation/VAR_009444|||http://purl.uniprot.org/annotation/VAR_009445|||http://purl.uniprot.org/annotation/VAR_009446|||http://purl.uniprot.org/annotation/VAR_009447|||http://purl.uniprot.org/annotation/VAR_009448|||http://purl.uniprot.org/annotation/VAR_009449|||http://purl.uniprot.org/annotation/VAR_009450|||http://purl.uniprot.org/annotation/VAR_009451|||http://purl.uniprot.org/annotation/VAR_009452|||http://purl.uniprot.org/annotation/VAR_009453|||http://purl.uniprot.org/annotation/VAR_009454|||http://purl.uniprot.org/annotation/VAR_009455|||http://purl.uniprot.org/annotation/VAR_009456|||http://purl.uniprot.org/annotation/VAR_009457|||http://purl.uniprot.org/annotation/VAR_009458|||http://purl.uniprot.org/annotation/VAR_018600|||http://purl.uniprot.org/annotation/VAR_018601|||http://purl.uniprot.org/annotation/VAR_018602|||http://purl.uniprot.org/annotation/VAR_018603|||http://purl.uniprot.org/annotation/VAR_022919|||http://purl.uniprot.org/annotation/VAR_022920|||http://purl.uniprot.org/annotation/VAR_022921|||http://purl.uniprot.org/annotation/VAR_022922|||http://purl.uniprot.org/annotation/VAR_057014|||http://purl.uniprot.org/annotation/VAR_057015|||http://purl.uniprot.org/annotation/VAR_060584|||http://purl.uniprot.org/annotation/VAR_060585|||http://purl.uniprot.org/annotation/VAR_078847|||http://purl.uniprot.org/annotation/VSP_004470|||http://purl.uniprot.org/annotation/VSP_004471|||http://purl.uniprot.org/annotation/VSP_004472|||http://purl.uniprot.org/annotation/VSP_038355|||http://purl.uniprot.org/annotation/VSP_054163|||http://purl.uniprot.org/annotation/VSP_055896|||http://purl.uniprot.org/annotation/VSP_055897
http://togogenome.org/gene/9606:CD28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0L1|||http://purl.uniprot.org/uniprot/P10747                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||T-cell-specific surface glycoprotein CD28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014652|||http://purl.uniprot.org/annotation/PRO_5002803440|||http://purl.uniprot.org/annotation/VSP_002494|||http://purl.uniprot.org/annotation/VSP_002495|||http://purl.uniprot.org/annotation/VSP_002496|||http://purl.uniprot.org/annotation/VSP_002497|||http://purl.uniprot.org/annotation/VSP_002498|||http://purl.uniprot.org/annotation/VSP_002499|||http://purl.uniprot.org/annotation/VSP_047701
http://togogenome.org/gene/9606:CLEC12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK10|||http://purl.uniprot.org/uniprot/Q2HXU8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes tyrosine phosphorylation and inhibitory receptor activity. Abolishes interaction with PTPN6 and PTPN11. Abolishes protection against natural killer cell-mediated cytotoxicity.|||C-type lectin|||C-type lectin domain family 12 member B|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313581|||http://purl.uniprot.org/annotation/VAR_037670|||http://purl.uniprot.org/annotation/VAR_037671|||http://purl.uniprot.org/annotation/VSP_030034|||http://purl.uniprot.org/annotation/VSP_030035
http://togogenome.org/gene/9606:NCBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53F19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Complete loss of 7-methylguanosine-containing mRNA cap binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Minor loss of 7-methylguanosine-containing mRNA cap binding.|||Nuclear cap-binding protein subunit 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA recognition motif (RRM) domain|||WLDD motif; essential for 7-methylguanosine-containing mRNA cap binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308582|||http://purl.uniprot.org/annotation/VSP_028999
http://togogenome.org/gene/9606:IDO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQW0                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased indoleamine 2,3-dioxygenase activity.|||In isoform 2.|||Indoleamine 2,3-dioxygenase 2|||Loss of indoleamine 2,3-dioxygenase activity.|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285262|||http://purl.uniprot.org/annotation/VAR_032007|||http://purl.uniprot.org/annotation/VAR_073727|||http://purl.uniprot.org/annotation/VSP_024858|||http://purl.uniprot.org/annotation/VSP_024859
http://togogenome.org/gene/9606:LAMTOR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43504                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  N-acetylmethionine|||No change.|||No interaction with XABX14-154 (truncated form of HBX).|||Ragulator complex protein LAMTOR5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066007
http://togogenome.org/gene/9606:SNPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IRY9|||http://purl.uniprot.org/uniprot/O15079                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Syntaphilin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072030|||http://purl.uniprot.org/annotation/VSP_037438
http://togogenome.org/gene/9606:PPP2R5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15173                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Impaired trimer formation with PP2A subunits A/C, no effect on KLHL15-binding.|||In isoform Beta-2.|||Loss of KLHL15-binding and enhanced stability.|||Phosphoserine; by CLK2|||Pro residues|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071450|||http://purl.uniprot.org/annotation/VSP_005109
http://togogenome.org/gene/9606:ACP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4Z2|||http://purl.uniprot.org/uniprot/B7Z552|||http://purl.uniprot.org/uniprot/B7Z6L8|||http://purl.uniprot.org/uniprot/B7Z6T8|||http://purl.uniprot.org/uniprot/B7Z7D2|||http://purl.uniprot.org/uniprot/B7Z8T9|||http://purl.uniprot.org/uniprot/E9PHY0|||http://purl.uniprot.org/uniprot/E9PQY3|||http://purl.uniprot.org/uniprot/P11117                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Lysosomal acid phosphatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023960|||http://purl.uniprot.org/annotation/PRO_5002863963|||http://purl.uniprot.org/annotation/PRO_5002863976|||http://purl.uniprot.org/annotation/PRO_5002866771|||http://purl.uniprot.org/annotation/PRO_5003242846|||http://purl.uniprot.org/annotation/PRO_5014085666|||http://purl.uniprot.org/annotation/VAR_027801|||http://purl.uniprot.org/annotation/VAR_034394|||http://purl.uniprot.org/annotation/VAR_050519|||http://purl.uniprot.org/annotation/VSP_045629|||http://purl.uniprot.org/annotation/VSP_045630
http://togogenome.org/gene/9606:FGF16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43320                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Fibroblast growth factor 16|||In MF4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147613|||http://purl.uniprot.org/annotation/VAR_072396
http://togogenome.org/gene/9606:DYNLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63172                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Dynein light chain Tctex-type 1|||Interaction with GNB1|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195152
http://togogenome.org/gene/9606:ZNF232                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIR0|||http://purl.uniprot.org/uniprot/A0A8Q3SIT7|||http://purl.uniprot.org/uniprot/I3L4J6|||http://purl.uniprot.org/uniprot/Q9UNY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform Short.|||Polar residues|||SCAN box|||Zinc finger protein 232                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047472|||http://purl.uniprot.org/annotation/VAR_035573|||http://purl.uniprot.org/annotation/VSP_006906
http://togogenome.org/gene/9606:GPR37L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60883                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in siblings with a novel form of progressive myoclonus epilepsy; unknown pathological significance; no effect on expression levels, cell surface location, signaling activity or ubiquitination.|||G-protein coupled receptor 37-like 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012796|||http://purl.uniprot.org/annotation/VAR_047455|||http://purl.uniprot.org/annotation/VAR_047456|||http://purl.uniprot.org/annotation/VAR_047457|||http://purl.uniprot.org/annotation/VAR_080868
http://togogenome.org/gene/9606:FAM221B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8Z2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Protein FAM221B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309264|||http://purl.uniprot.org/annotation/VAR_061598|||http://purl.uniprot.org/annotation/VAR_061599|||http://purl.uniprot.org/annotation/VSP_035486|||http://purl.uniprot.org/annotation/VSP_035487|||http://purl.uniprot.org/annotation/VSP_036643|||http://purl.uniprot.org/annotation/VSP_036644
http://togogenome.org/gene/9606:CD99                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP69|||http://purl.uniprot.org/uniprot/P14209                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD99 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 3.|||In isoform II.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021726|||http://purl.uniprot.org/annotation/PRO_5001919112|||http://purl.uniprot.org/annotation/VAR_014733|||http://purl.uniprot.org/annotation/VAR_014734|||http://purl.uniprot.org/annotation/VSP_004324|||http://purl.uniprot.org/annotation/VSP_046315
http://togogenome.org/gene/9606:OR9G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH87                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150678|||http://purl.uniprot.org/annotation/VAR_032777|||http://purl.uniprot.org/annotation/VAR_032778|||http://purl.uniprot.org/annotation/VAR_032779|||http://purl.uniprot.org/annotation/VAR_032780|||http://purl.uniprot.org/annotation/VAR_032781|||http://purl.uniprot.org/annotation/VAR_034276|||http://purl.uniprot.org/annotation/VAR_053254|||http://purl.uniprot.org/annotation/VAR_053255|||http://purl.uniprot.org/annotation/VAR_053256|||http://purl.uniprot.org/annotation/VAR_060017|||http://purl.uniprot.org/annotation/VAR_060018|||http://purl.uniprot.org/annotation/VAR_060019|||http://purl.uniprot.org/annotation/VAR_060020|||http://purl.uniprot.org/annotation/VAR_060021
http://togogenome.org/gene/9606:KRT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35527                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In EPPK.|||In EPPK; with knuckle pads.|||Keratin, type I cytoskeletal 9|||Leads to aggregate formation.|||Linker 1|||Linker 12|||Phosphoserine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063640|||http://purl.uniprot.org/annotation/VAR_003822|||http://purl.uniprot.org/annotation/VAR_003823|||http://purl.uniprot.org/annotation/VAR_003824|||http://purl.uniprot.org/annotation/VAR_003825|||http://purl.uniprot.org/annotation/VAR_010499|||http://purl.uniprot.org/annotation/VAR_010500|||http://purl.uniprot.org/annotation/VAR_010501|||http://purl.uniprot.org/annotation/VAR_010502|||http://purl.uniprot.org/annotation/VAR_010503|||http://purl.uniprot.org/annotation/VAR_010504|||http://purl.uniprot.org/annotation/VAR_035438|||http://purl.uniprot.org/annotation/VAR_035439|||http://purl.uniprot.org/annotation/VAR_036805|||http://purl.uniprot.org/annotation/VAR_036806|||http://purl.uniprot.org/annotation/VAR_036807|||http://purl.uniprot.org/annotation/VAR_036808|||http://purl.uniprot.org/annotation/VAR_036809|||http://purl.uniprot.org/annotation/VAR_036810|||http://purl.uniprot.org/annotation/VAR_071977|||http://purl.uniprot.org/annotation/VAR_071978|||http://purl.uniprot.org/annotation/VAR_071979|||http://purl.uniprot.org/annotation/VAR_071980
http://togogenome.org/gene/9606:FBXW12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6X9E4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box/WD repeat-containing protein 12|||In isoform 2.|||In isoform 3.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051000|||http://purl.uniprot.org/annotation/VAR_057601|||http://purl.uniprot.org/annotation/VAR_057602|||http://purl.uniprot.org/annotation/VAR_057603|||http://purl.uniprot.org/annotation/VSP_042911|||http://purl.uniprot.org/annotation/VSP_044601
http://togogenome.org/gene/9606:CMTM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 4|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||MARVEL|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186103|||http://purl.uniprot.org/annotation/VSP_008260|||http://purl.uniprot.org/annotation/VSP_008261
http://togogenome.org/gene/9606:NIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z410|||http://purl.uniprot.org/uniprot/Q86X76                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  CN hydrolase|||Deaminated glutathione amidase|||In isoform 1.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Mitochondrion|||Nucleophile|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213251|||http://purl.uniprot.org/annotation/VSP_011544|||http://purl.uniprot.org/annotation/VSP_011545|||http://purl.uniprot.org/annotation/VSP_011546|||http://purl.uniprot.org/annotation/VSP_011547|||http://purl.uniprot.org/annotation/VSP_053711|||http://purl.uniprot.org/annotation/VSP_053712
http://togogenome.org/gene/9606:CST9L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJH1|||http://purl.uniprot.org/uniprot/Q9H4G1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cystatin|||Cystatin-9-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006656|||http://purl.uniprot.org/annotation/PRO_5018675981|||http://purl.uniprot.org/annotation/VAR_022079
http://togogenome.org/gene/9606:NUDT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Abolishes localization to peroxisomes.|||In isoform 2.|||Loss of decapping activity towards NAD-capped RNAs.|||Loss of homodimerization; when associated with A-281; A-283; A-284 and A-384.|||Loss of homodimerization; when associated with A-281; A-283; A-287 and A-384.|||Loss of homodimerization; when associated with A-281; A-284; A-287 and A-384.|||Loss of homodimerization; when associated with A-283; A-284; A-287 and A-384.|||Microbody targeting signal|||N6-succinyllysine|||NAD-capped RNA hydrolase NUDT12|||No effect on decapping activity towards NAD-capped RNAs. Loss of homodimerization; when associated with A-281; A-283; A-284 and A-287.|||Nudix box|||Nudix hydrolase|||Partial loss of decapping activity towards NAD-capped RNAs.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056956|||http://purl.uniprot.org/annotation/VAR_034157|||http://purl.uniprot.org/annotation/VAR_034158|||http://purl.uniprot.org/annotation/VSP_060395
http://togogenome.org/gene/9606:MIS18BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P0N0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Mis18-binding protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||SANT|||SANTA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197140|||http://purl.uniprot.org/annotation/VAR_050184|||http://purl.uniprot.org/annotation/VAR_050185|||http://purl.uniprot.org/annotation/VAR_050186|||http://purl.uniprot.org/annotation/VAR_050187|||http://purl.uniprot.org/annotation/VSP_014105
http://togogenome.org/gene/9606:PM20D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYS1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Xaa-Arg dipeptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286340|||http://purl.uniprot.org/annotation/VAR_032081
http://togogenome.org/gene/9606:CPPED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRF8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Catalytic|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Serine/threonine-protein phosphatase CPPED1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320556|||http://purl.uniprot.org/annotation/VAR_039204|||http://purl.uniprot.org/annotation/VAR_039205|||http://purl.uniprot.org/annotation/VAR_039206|||http://purl.uniprot.org/annotation/VAR_039207|||http://purl.uniprot.org/annotation/VSP_031658|||http://purl.uniprot.org/annotation/VSP_055218|||http://purl.uniprot.org/annotation/VSP_055219
http://togogenome.org/gene/9606:AOC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16853|||http://purl.uniprot.org/uniprot/Q9UEU7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469.|||Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469.|||Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394.|||Interchain|||Membrane primary amine oxidase|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Proton acceptor|||Schiff-base intermediate with substrate; via topaquinone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064102|||http://purl.uniprot.org/annotation/VAR_012064|||http://purl.uniprot.org/annotation/VAR_024343|||http://purl.uniprot.org/annotation/VAR_025027|||http://purl.uniprot.org/annotation/VAR_025028|||http://purl.uniprot.org/annotation/VAR_025029|||http://purl.uniprot.org/annotation/VAR_025030|||http://purl.uniprot.org/annotation/VAR_025031|||http://purl.uniprot.org/annotation/VAR_025032|||http://purl.uniprot.org/annotation/VAR_025033|||http://purl.uniprot.org/annotation/VAR_025034|||http://purl.uniprot.org/annotation/VAR_025035|||http://purl.uniprot.org/annotation/VAR_052603|||http://purl.uniprot.org/annotation/VAR_052604|||http://purl.uniprot.org/annotation/VAR_052605|||http://purl.uniprot.org/annotation/VSP_053751|||http://purl.uniprot.org/annotation/VSP_053752|||http://purl.uniprot.org/annotation/VSP_055201
http://togogenome.org/gene/9606:PCDH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2D9|||http://purl.uniprot.org/uniprot/B7ZM79|||http://purl.uniprot.org/uniprot/Q5VT82|||http://purl.uniprot.org/uniprot/Q9HC56|||http://purl.uniprot.org/uniprot/X5D7N0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003994|||http://purl.uniprot.org/annotation/PRO_5002708111|||http://purl.uniprot.org/annotation/PRO_5004955333|||http://purl.uniprot.org/annotation/PRO_5014568446|||http://purl.uniprot.org/annotation/PRO_5014587121|||http://purl.uniprot.org/annotation/VSP_035430
http://togogenome.org/gene/9606:ZNF250                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNS9|||http://purl.uniprot.org/uniprot/P15622                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||KRAB|||Zinc finger protein 250                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047483|||http://purl.uniprot.org/annotation/VSP_011039|||http://purl.uniprot.org/annotation/VSP_011040
http://togogenome.org/gene/9606:KCNC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03721                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased inhibition of channel closure by PKC.|||Decreased inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-9.|||Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-15 and D-21.|||Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-9; D-15 and D-21.|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||In isoform 3.|||Inactivation gate|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Potassium voltage-gated channel subfamily C member 4|||Selectivity filter|||Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-15.|||Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-21.|||Strong decrease of inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054058|||http://purl.uniprot.org/annotation/VAR_027505|||http://purl.uniprot.org/annotation/VAR_034051|||http://purl.uniprot.org/annotation/VAR_062185|||http://purl.uniprot.org/annotation/VSP_020581|||http://purl.uniprot.org/annotation/VSP_020582|||http://purl.uniprot.org/annotation/VSP_040033
http://togogenome.org/gene/9606:MMP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51511                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Matrix metalloproteinase-15|||N-linked (GlcNAc...) asparagine|||Or 45|||Phosphoserine|||Pro residues|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028808|||http://purl.uniprot.org/annotation/PRO_0000028809|||http://purl.uniprot.org/annotation/VAR_020055|||http://purl.uniprot.org/annotation/VAR_030523|||http://purl.uniprot.org/annotation/VAR_030524|||http://purl.uniprot.org/annotation/VAR_030525|||http://purl.uniprot.org/annotation/VAR_030526
http://togogenome.org/gene/9606:GUCA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02747                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Peptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Guanylin|||HMW-guanylin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013135|||http://purl.uniprot.org/annotation/PRO_0000013136|||http://purl.uniprot.org/annotation/VAR_062678
http://togogenome.org/gene/9606:H2BC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60814                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-K|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071828
http://togogenome.org/gene/9606:SYPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYR7|||http://purl.uniprot.org/uniprot/Q5VXT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Polar residues|||Synaptophysin-like protein 2|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179166|||http://purl.uniprot.org/annotation/VSP_014268
http://togogenome.org/gene/9606:UBOX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94941                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||In isoform 2.|||RING finger protein 37|||RING-type|||U-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056076|||http://purl.uniprot.org/annotation/VAR_046402|||http://purl.uniprot.org/annotation/VAR_046403|||http://purl.uniprot.org/annotation/VSP_042899
http://togogenome.org/gene/9606:DDX49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6V7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Probable ATP-dependent RNA helicase DDX49|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055052|||http://purl.uniprot.org/annotation/VAR_033858|||http://purl.uniprot.org/annotation/VAR_033859|||http://purl.uniprot.org/annotation/VAR_052167|||http://purl.uniprot.org/annotation/VSP_056367|||http://purl.uniprot.org/annotation/VSP_056368|||http://purl.uniprot.org/annotation/VSP_056369
http://togogenome.org/gene/9606:CTRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99895                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-C|||Found in a patient with chronic pancreatitis; unknown pathological significance.|||Found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type.|||Found in a patient with chronic pancreatitis; unknown pathological significance; catalytic activity comparable to that of wild type; the mutant undergoes proteolytic degradation during trypsin-mediated activation.|||Found in a patient with chronic pancreatitis; unknown pathological significance; mutant protein secretion, activity and trypsin-mediated degradation are comparable to those of wild-type.|||Found in a patient with chronic pancreatitis; unknown pathological significance; the mutant is not secreted.|||Found in patients with chronic pancreatitis; unknown pathological significance.|||In PCTT; associated with disease susceptibility; highly reduced catalytic efficiency.|||In PCTT; associated with disease susceptibility; impaired catalytic activity.|||In PCTT; associated with disease susceptibility; results in altered enzyme specificity and loss of activity.|||In PCTT; associated with disease susceptibility; results in reduced protein secretion and loss of activity.|||In PCTT; associated with susceptibility to disease; reduced protein secretion; impaired catalytic activity.|||In PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion and loss of activity.|||In PCTT; associated with susceptibility to disease; results in markedly reduced protein secretion.|||In PCTT; associated with susceptibility to disease; results in reduced secretion; normal activity; the mutant undergoes proteolytic degradation during trypsin-mediated activation.|||In PCTT; associated with susceptibility to disease; slightly reduced activity.|||In PCTT; associated with susceptibility to disease; the mutant is not secreted.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Rare variant that may be associated with susceptibility to pancreatitis; results in markedly reduced protein secretion.|||Rare variant; found in a patient with chronic pancreatitis; unknown pathological significance.|||Rare variant; results in impaired protein secretion.|||Rare variant; results in normal secretion and activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027713|||http://purl.uniprot.org/annotation/PRO_0000027714|||http://purl.uniprot.org/annotation/VAR_010928|||http://purl.uniprot.org/annotation/VAR_043516|||http://purl.uniprot.org/annotation/VAR_043517|||http://purl.uniprot.org/annotation/VAR_043518|||http://purl.uniprot.org/annotation/VAR_043519|||http://purl.uniprot.org/annotation/VAR_043520|||http://purl.uniprot.org/annotation/VAR_043521|||http://purl.uniprot.org/annotation/VAR_043522|||http://purl.uniprot.org/annotation/VAR_043523|||http://purl.uniprot.org/annotation/VAR_043524|||http://purl.uniprot.org/annotation/VAR_043525|||http://purl.uniprot.org/annotation/VAR_043526|||http://purl.uniprot.org/annotation/VAR_043527|||http://purl.uniprot.org/annotation/VAR_043528|||http://purl.uniprot.org/annotation/VAR_043529|||http://purl.uniprot.org/annotation/VAR_043530|||http://purl.uniprot.org/annotation/VAR_070520|||http://purl.uniprot.org/annotation/VAR_070521|||http://purl.uniprot.org/annotation/VAR_070522|||http://purl.uniprot.org/annotation/VAR_070523|||http://purl.uniprot.org/annotation/VAR_070524|||http://purl.uniprot.org/annotation/VAR_070525|||http://purl.uniprot.org/annotation/VAR_070526|||http://purl.uniprot.org/annotation/VAR_070527|||http://purl.uniprot.org/annotation/VAR_070528|||http://purl.uniprot.org/annotation/VAR_070529|||http://purl.uniprot.org/annotation/VAR_070530|||http://purl.uniprot.org/annotation/VAR_070531|||http://purl.uniprot.org/annotation/VAR_070532|||http://purl.uniprot.org/annotation/VAR_070533|||http://purl.uniprot.org/annotation/VAR_070534|||http://purl.uniprot.org/annotation/VAR_070535|||http://purl.uniprot.org/annotation/VAR_070536|||http://purl.uniprot.org/annotation/VAR_070537|||http://purl.uniprot.org/annotation/VAR_070538|||http://purl.uniprot.org/annotation/VAR_070539|||http://purl.uniprot.org/annotation/VAR_070540|||http://purl.uniprot.org/annotation/VAR_070541
http://togogenome.org/gene/9606:DNAJC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5X1|||http://purl.uniprot.org/uniprot/Q96DA6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||J|||Mitochondrial import inner membrane translocase subunit TIM14|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071100|||http://purl.uniprot.org/annotation/VSP_047119
http://togogenome.org/gene/9606:BPIFA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPI fold-containing family A member 3|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017187|||http://purl.uniprot.org/annotation/VAR_049754|||http://purl.uniprot.org/annotation/VAR_049755|||http://purl.uniprot.org/annotation/VSP_026471
http://togogenome.org/gene/9606:LMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S06                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lipase maturation factor 1|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000276739|||http://purl.uniprot.org/annotation/VAR_030487|||http://purl.uniprot.org/annotation/VAR_030488|||http://purl.uniprot.org/annotation/VAR_053829|||http://purl.uniprot.org/annotation/VAR_053830|||http://purl.uniprot.org/annotation/VSP_057388
http://togogenome.org/gene/9606:ALPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10696                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Alkaline phosphatase, germ cell type|||Disordered|||GPI-anchor amidated aspartate|||N-linked (GlcNAc...) asparagine|||Phosphoserine intermediate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024033|||http://purl.uniprot.org/annotation/PRO_0000024034|||http://purl.uniprot.org/annotation/VAR_027553|||http://purl.uniprot.org/annotation/VAR_027554|||http://purl.uniprot.org/annotation/VAR_027555
http://togogenome.org/gene/9606:NLRP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59046                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  FISNA|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||NACHT|||NACHT, LRR and PYD domains-containing protein 12|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080899|||http://purl.uniprot.org/annotation/VAR_053620|||http://purl.uniprot.org/annotation/VAR_053621|||http://purl.uniprot.org/annotation/VSP_005523|||http://purl.uniprot.org/annotation/VSP_005524|||http://purl.uniprot.org/annotation/VSP_009879|||http://purl.uniprot.org/annotation/VSP_016908|||http://purl.uniprot.org/annotation/VSP_016909|||http://purl.uniprot.org/annotation/VSP_016910|||http://purl.uniprot.org/annotation/VSP_054622|||http://purl.uniprot.org/annotation/VSP_055193
http://togogenome.org/gene/9606:IQCA1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCM1|||http://purl.uniprot.org/uniprot/E0ZS59                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||IQ|||IQ and AAA domain-containing protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341249
http://togogenome.org/gene/9606:SHLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V20                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Fails to interact with SHLD3 or MAD2L2.|||In isoform 2.|||Mediates interaction with SHLD1|||Shieldin complex subunit 2|||Sufficient for interaction with SHLD3 and MAD2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087161|||http://purl.uniprot.org/annotation/VAR_053997|||http://purl.uniprot.org/annotation/VAR_053998|||http://purl.uniprot.org/annotation/VAR_053999|||http://purl.uniprot.org/annotation/VSP_016165
http://togogenome.org/gene/9606:KLF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5W3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Interaction with WWP1|||Krueppel-like factor 2|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047162|||http://purl.uniprot.org/annotation/VAR_038830|||http://purl.uniprot.org/annotation/VAR_038831
http://togogenome.org/gene/9606:SPRY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43597                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CAV1.|||Abolishes interaction with GRB2.|||Basic and acidic residues|||Cleavage; by FAP|||Disordered|||In IGAN3; no effect on protein expression; negatively regulates ERK1 and ERK2 cascade.|||Inhibits cleavage by the prolyl endopeptidase FAP.|||Polar residues|||Protein sprouty homolog 2|||Required for interaction with CAV1|||Required for interaction with TESK1|||SPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076901|||http://purl.uniprot.org/annotation/VAR_024647|||http://purl.uniprot.org/annotation/VAR_076288
http://togogenome.org/gene/9606:SNX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SYF1|||http://purl.uniprot.org/uniprot/Q9UMY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||N-acetylserine|||PX|||Phosphoserine|||Phosphotyrosine|||Removed|||Sorting nexin-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213858|||http://purl.uniprot.org/annotation/VSP_060252|||http://purl.uniprot.org/annotation/VSP_060253
http://togogenome.org/gene/9606:AAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2I8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP2-associated protein kinase 1|||Clathrin-binding domain (CBD)|||Disordered|||Does not affect interaction with NOTCH1 but abolishes interaction with ESP15.|||In isoform 2.|||Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization.|||Inhibits autophosphorylation and phosphorylation of AP2M1. Does not affect NUMB localization. Does not interact with monoubiquitinated NOTCH1.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250578|||http://purl.uniprot.org/annotation/VAR_031129|||http://purl.uniprot.org/annotation/VAR_040348|||http://purl.uniprot.org/annotation/VAR_040349|||http://purl.uniprot.org/annotation/VAR_040350|||http://purl.uniprot.org/annotation/VAR_040351|||http://purl.uniprot.org/annotation/VAR_040352|||http://purl.uniprot.org/annotation/VAR_040353|||http://purl.uniprot.org/annotation/VAR_040354|||http://purl.uniprot.org/annotation/VSP_039459
http://togogenome.org/gene/9606:AIF1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Allograft inflammatory factor 1-like|||Disordered|||EF-hand 1|||EF-hand 2; degenerate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073870|||http://purl.uniprot.org/annotation/VSP_017150|||http://purl.uniprot.org/annotation/VSP_017151|||http://purl.uniprot.org/annotation/VSP_017152|||http://purl.uniprot.org/annotation/VSP_017153
http://togogenome.org/gene/9606:JUN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05412                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes activation of FASLG/CD95L transcription.|||Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-91.|||Abolishes interaction with FBXW7; when associated with A-63; A-73 and A-93.|||Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239.|||Abolishes the synergistic activity with SMAD3 to activate TGF-beta-mediated transcription.|||Basic motif|||Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-89; A-93; and A-286.|||Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-286.|||Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-89; and A-93.|||Complete loss of PAK2-mediated phosphorylation; when associated with A-2; A-8; A-93; and A-286.|||Complete loss of PAK2-mediated phosphorylation; when associated with A-8; A-89; A-93; and A-286.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Greatly reduced ATF7-mediated transcriptional activity; when associated with A-63. Abolishes interaction with FBXW7; when associated with A-63; A-91 and A-93.|||Greatly reduced ATF7-mediated transcriptional activity; when associated with A-73. Abolishes interaction with FBXW7; when associated with A-73; A-91 and A-93.|||Interaction with PAGE4|||Leucine-zipper|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for synergistic transcriptional activity with SMAD3|||Phosphoserine|||Phosphoserine; by DYRK2 and GSK3-beta|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK8 and PLK3|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Phosphothreonine; by PAK2|||Transcription factor Jun|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076429|||http://purl.uniprot.org/annotation/VAR_012070
http://togogenome.org/gene/9606:FHOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2V2M9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DAD|||Disordered|||FH1|||FH1/FH2 domain-containing protein 3|||FH2|||GBD/FH3|||In CMH28.|||In CMH28; unknown pathological significance.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283791|||http://purl.uniprot.org/annotation/VAR_055804|||http://purl.uniprot.org/annotation/VAR_085890|||http://purl.uniprot.org/annotation/VAR_085891|||http://purl.uniprot.org/annotation/VAR_085892|||http://purl.uniprot.org/annotation/VAR_085893|||http://purl.uniprot.org/annotation/VAR_085894|||http://purl.uniprot.org/annotation/VAR_085895|||http://purl.uniprot.org/annotation/VAR_085896|||http://purl.uniprot.org/annotation/VAR_085897|||http://purl.uniprot.org/annotation/VAR_085898|||http://purl.uniprot.org/annotation/VAR_085899|||http://purl.uniprot.org/annotation/VAR_085900|||http://purl.uniprot.org/annotation/VAR_085901|||http://purl.uniprot.org/annotation/VAR_085902|||http://purl.uniprot.org/annotation/VAR_085903|||http://purl.uniprot.org/annotation/VAR_085904|||http://purl.uniprot.org/annotation/VAR_085905|||http://purl.uniprot.org/annotation/VAR_085906|||http://purl.uniprot.org/annotation/VAR_085907|||http://purl.uniprot.org/annotation/VAR_085908|||http://purl.uniprot.org/annotation/VAR_085909|||http://purl.uniprot.org/annotation/VAR_085910|||http://purl.uniprot.org/annotation/VAR_085911|||http://purl.uniprot.org/annotation/VAR_085912|||http://purl.uniprot.org/annotation/VAR_085913|||http://purl.uniprot.org/annotation/VAR_085914|||http://purl.uniprot.org/annotation/VAR_085915|||http://purl.uniprot.org/annotation/VAR_085916|||http://purl.uniprot.org/annotation/VSP_024397|||http://purl.uniprot.org/annotation/VSP_024398|||http://purl.uniprot.org/annotation/VSP_044682|||http://purl.uniprot.org/annotation/VSP_044683
http://togogenome.org/gene/9606:PRDM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1, isoform 2 and isoform 5.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 2.|||In isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||PR domain zinc finger protein 10|||Phosphoserine|||Phosphothreonine|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047767|||http://purl.uniprot.org/annotation/VAR_019984|||http://purl.uniprot.org/annotation/VAR_054418|||http://purl.uniprot.org/annotation/VSP_035655|||http://purl.uniprot.org/annotation/VSP_035656|||http://purl.uniprot.org/annotation/VSP_036351|||http://purl.uniprot.org/annotation/VSP_036352|||http://purl.uniprot.org/annotation/VSP_036353
http://togogenome.org/gene/9606:H2BC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93079                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-H|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071833
http://togogenome.org/gene/9606:LLGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15334                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Lethal(2) giant larvae protein homolog 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232725|||http://purl.uniprot.org/annotation/VAR_058710|||http://purl.uniprot.org/annotation/VAR_058711
http://togogenome.org/gene/9606:FSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R366|||http://purl.uniprot.org/uniprot/Q9BTV5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  B30.2/SPRY|||COS|||Disordered|||Fibronectin type III and SPRY domain-containing protein 1|||Fibronectin type-III|||In mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-322.|||In mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-324.|||In mitosis, remained associated with microtubules; when associated with A-313; A-322 and A-324.|||In mitosis, remained associated with microtubules; when associated with A-317; A-322 and A-324.|||Omega-N-methylarginine|||Reduced ability to associate with microtubules; when associated with D-313; D-317 and D-324.|||Reduced ability to associate with microtubules; when associated with D-313; D-317 and E-322.|||Reduced ability to associate with microtubules; when associated with D-313; E-322 and D-324.|||Reduced ability to associate with microtubules; when associated with D-317; E-322 and D-324.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316537|||http://purl.uniprot.org/annotation/VAR_038385
http://togogenome.org/gene/9606:PRRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6L0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In BFIS2.|||In EKD1.|||In EKD1; may affect subcellular location, becoming predominantly cytoplasmic; impairs interaction with GRIA1 and SNAP25.|||In EKD1; no effect on location at the plasma membrane.|||In ICCA.|||In ICCA; may be produced at very low levels due to a premature stop codon in the mRNA, that could lead to nonsense-mediated mRNA decay.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich transmembrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307745|||http://purl.uniprot.org/annotation/VAR_067010|||http://purl.uniprot.org/annotation/VAR_067011|||http://purl.uniprot.org/annotation/VAR_067012|||http://purl.uniprot.org/annotation/VAR_067013|||http://purl.uniprot.org/annotation/VAR_067014|||http://purl.uniprot.org/annotation/VAR_067320|||http://purl.uniprot.org/annotation/VAR_067321|||http://purl.uniprot.org/annotation/VAR_067322|||http://purl.uniprot.org/annotation/VAR_067323|||http://purl.uniprot.org/annotation/VAR_067324|||http://purl.uniprot.org/annotation/VAR_067325|||http://purl.uniprot.org/annotation/VAR_067326|||http://purl.uniprot.org/annotation/VAR_067327|||http://purl.uniprot.org/annotation/VAR_068426|||http://purl.uniprot.org/annotation/VAR_080269|||http://purl.uniprot.org/annotation/VSP_028814|||http://purl.uniprot.org/annotation/VSP_028815
http://togogenome.org/gene/9606:PHOSPHO2-KLHL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBE8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242157
http://togogenome.org/gene/9606:ZNF672                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q499Z4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 672                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233991
http://togogenome.org/gene/9606:REEP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00765                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Receptor expression-enhancing protein 5|||Required for dimerization and maintaining endoplasmic reticulum morphology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101815|||http://purl.uniprot.org/annotation/VSP_056633
http://togogenome.org/gene/9606:VRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0TB08|||http://purl.uniprot.org/uniprot/Q99986                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by PLK3 and induction of Golgi fragmentation during mitosis. Strongly reduced autophosphorylation.|||Basic and acidic residues|||Disordered|||Does not abolish autophosphorylation.|||Does not affect phosphorylation at S-342.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphoserine; by PLK3|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase VRK1|||Strongly reduced autophosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086803
http://togogenome.org/gene/9606:CYP2U1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z449                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 2U1|||Helical|||In SPG56.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291756|||http://purl.uniprot.org/annotation/VAR_069575|||http://purl.uniprot.org/annotation/VAR_069576|||http://purl.uniprot.org/annotation/VAR_069577|||http://purl.uniprot.org/annotation/VAR_069578|||http://purl.uniprot.org/annotation/VSP_026222|||http://purl.uniprot.org/annotation/VSP_026223
http://togogenome.org/gene/9606:CEP57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XR8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 57 kDa|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Mediates interaction with microtubules|||Phosphoserine|||Polar residues|||centrosome localization domain (CLD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189532|||http://purl.uniprot.org/annotation/VAR_059839|||http://purl.uniprot.org/annotation/VSP_012262|||http://purl.uniprot.org/annotation/VSP_012263|||http://purl.uniprot.org/annotation/VSP_012264|||http://purl.uniprot.org/annotation/VSP_037839|||http://purl.uniprot.org/annotation/VSP_037840
http://togogenome.org/gene/9606:CXCL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95715                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-X-C motif chemokine 14|||D-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005115
http://togogenome.org/gene/9606:NUP85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW27                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In NPHS17; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP160.|||In NPHS17; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP160.|||In NPHS17; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Nuclear pore complex protein Nup85|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324187|||http://purl.uniprot.org/annotation/VAR_081364|||http://purl.uniprot.org/annotation/VAR_081365|||http://purl.uniprot.org/annotation/VAR_081366|||http://purl.uniprot.org/annotation/VSP_056079|||http://purl.uniprot.org/annotation/VSP_056080|||http://purl.uniprot.org/annotation/VSP_056081|||http://purl.uniprot.org/annotation/VSP_056082
http://togogenome.org/gene/9606:KDSR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06136                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3-ketodihydrosphingosine reductase|||Cytoplasmic|||Helical|||In EKVP4.|||In EKVP4; loss of 3-dehydrosphinganine reductase activity.|||In isoform 2.|||Lumenal|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031982|||http://purl.uniprot.org/annotation/VAR_079185|||http://purl.uniprot.org/annotation/VAR_079186|||http://purl.uniprot.org/annotation/VAR_079187|||http://purl.uniprot.org/annotation/VAR_079188|||http://purl.uniprot.org/annotation/VSP_056641
http://togogenome.org/gene/9606:MRPL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P015                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Large ribosomal subunit protein uL15m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257838
http://togogenome.org/gene/9606:ZNF658                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7Y5|||http://purl.uniprot.org/uniprot/Q5TYW1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19; degenerate|||C2H2-type 1; degenerate|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 658                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280433|||http://purl.uniprot.org/annotation/VAR_052888|||http://purl.uniprot.org/annotation/VSP_023671|||http://purl.uniprot.org/annotation/VSP_023672
http://togogenome.org/gene/9606:MDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5K1VW95|||http://purl.uniprot.org/uniprot/P40925|||http://purl.uniprot.org/uniprot/V9HWF2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DEE88; decreased protein expression; increased levels of glutamate and glycerol-3-phosphate.|||In isoform 2.|||In isoform 3.|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Malate dehydrogenase, cytoplasmic|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000113409|||http://purl.uniprot.org/annotation/VAR_083894|||http://purl.uniprot.org/annotation/VSP_042661|||http://purl.uniprot.org/annotation/VSP_045847
http://togogenome.org/gene/9606:STRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Stereocilin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022426|||http://purl.uniprot.org/annotation/VAR_051389
http://togogenome.org/gene/9606:APBB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ88|||http://purl.uniprot.org/uniprot/B4E2F2|||http://purl.uniprot.org/uniprot/G5E9Y1|||http://purl.uniprot.org/uniprot/Q5I0G1|||http://purl.uniprot.org/uniprot/Q92870                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with APP and gamma-secretase-dependent processing of the APP membrane-anchored C-terminal fragment C83.|||Amyloid beta precursor protein binding family B member 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PID|||PID 1|||PID 2|||Phosphoserine|||Polar residues|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076052|||http://purl.uniprot.org/annotation/VAR_069029|||http://purl.uniprot.org/annotation/VSP_040354|||http://purl.uniprot.org/annotation/VSP_040355|||http://purl.uniprot.org/annotation/VSP_044232|||http://purl.uniprot.org/annotation/VSP_045042
http://togogenome.org/gene/9606:NKX2-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2Z4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Nkx-2.4|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048935
http://togogenome.org/gene/9606:PCSK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ9|||http://purl.uniprot.org/uniprot/Q6UW60                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with HSPA5.|||P/Homo B|||Peptidase S8|||Proprotein convertase subtilisin/kexin type 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246778|||http://purl.uniprot.org/annotation/PRO_0000246779|||http://purl.uniprot.org/annotation/PRO_5007491838|||http://purl.uniprot.org/annotation/VAR_061772|||http://purl.uniprot.org/annotation/VSP_052097
http://togogenome.org/gene/9606:LUC7L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3C5|||http://purl.uniprot.org/uniprot/J3KPP4|||http://purl.uniprot.org/uniprot/O95232|||http://purl.uniprot.org/uniprot/Q86Y74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Luc7-like protein 3|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058013|||http://purl.uniprot.org/annotation/VSP_018136|||http://purl.uniprot.org/annotation/VSP_018137
http://togogenome.org/gene/9606:RIPK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T11|||http://purl.uniprot.org/uniprot/Q9H4D1                                                                                  ^@                                                                                  Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Site                                                                                  ^@                                                                                  Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  ANK|||Basic and acidic residues|||Disordered|||Protein kinase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RAP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62834                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Ras-related protein Rap-1A|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030199|||http://purl.uniprot.org/annotation/PRO_0000030200
http://togogenome.org/gene/9606:ARID4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29374|||http://purl.uniprot.org/uniprot/Q05CG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 4A|||Abolishes binding to trimethylated lysines.|||Acidic residues|||Basic and acidic residues|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform II.|||In isoform III.|||No effect on binding to trimethylated lysines.|||Phosphoserine|||Polar residues|||Retinoblastoma protein binding|||Significantly reduces affinity for trimethylated lysines.|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200580|||http://purl.uniprot.org/annotation/VAR_031566|||http://purl.uniprot.org/annotation/VAR_031567|||http://purl.uniprot.org/annotation/VAR_031568|||http://purl.uniprot.org/annotation/VSP_004371|||http://purl.uniprot.org/annotation/VSP_004372|||http://purl.uniprot.org/annotation/VSP_004373
http://togogenome.org/gene/9606:YDJC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MPS7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carbohydrate deacetylase|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328774|||http://purl.uniprot.org/annotation/VAR_042519|||http://purl.uniprot.org/annotation/VSP_032784|||http://purl.uniprot.org/annotation/VSP_032785|||http://purl.uniprot.org/annotation/VSP_032786|||http://purl.uniprot.org/annotation/VSP_032787
http://togogenome.org/gene/9606:BTAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14981|||http://purl.uniprot.org/uniprot/Q2M1V9|||http://purl.uniprot.org/uniprot/Q8N6J1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  DEGH box|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||TATA-binding protein-associated factor 172                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074311|||http://purl.uniprot.org/annotation/VSP_056510
http://togogenome.org/gene/9606:FAM3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K9B4|||http://purl.uniprot.org/uniprot/Q96BQ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  GG-type lectin|||Helical|||ILEI/PANDER|||N-linked (GlcNAc...) asparagine|||Protein FAM3D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008754|||http://purl.uniprot.org/annotation/VAR_053087|||http://purl.uniprot.org/annotation/VAR_053088
http://togogenome.org/gene/9606:LYZL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YUZ6|||http://purl.uniprot.org/uniprot/O75951                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lysozyme-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240640|||http://purl.uniprot.org/annotation/PRO_5014217361|||http://purl.uniprot.org/annotation/VAR_026819
http://togogenome.org/gene/9606:AP5M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EQ45|||http://purl.uniprot.org/uniprot/Q9H0R1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-5 complex subunit mu-1|||In isoform 2.|||MHD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193795|||http://purl.uniprot.org/annotation/VAR_055484|||http://purl.uniprot.org/annotation/VAR_055485|||http://purl.uniprot.org/annotation/VSP_008407|||http://purl.uniprot.org/annotation/VSP_008408
http://togogenome.org/gene/9606:REL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPL7|||http://purl.uniprot.org/uniprot/Q04864                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKA|||Proto-oncogene c-Rel|||RHD|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205165|||http://purl.uniprot.org/annotation/VSP_055857
http://togogenome.org/gene/9606:ATXN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15265|||http://purl.uniprot.org/uniprot/Q9UPD8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished cleavage by caspase-7 and attenuates formation of protein aggregates in SCA7 degeneration; when associated with N-266.|||Abolished cleavage by caspase-7 and attenuates formation of protein aggregates in SCA7 degeneration; when associated with N-344.|||Almost completely abolishes sumoylation.|||Ataxin-7|||Basic and acidic residues|||Cleavage; by caspase-7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 3.|||In isoform b.|||No effect on sumoylation.|||Polar residues|||Pro residues|||SCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064759|||http://purl.uniprot.org/annotation/VAR_011823|||http://purl.uniprot.org/annotation/VAR_011824|||http://purl.uniprot.org/annotation/VAR_020143|||http://purl.uniprot.org/annotation/VAR_053779|||http://purl.uniprot.org/annotation/VSP_007695|||http://purl.uniprot.org/annotation/VSP_044456
http://togogenome.org/gene/9606:SMG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86US8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes RNase activity.|||Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 140-E--E-146.|||Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 46-E--E-52.|||Basic and acidic residues|||Disordered|||EJC-binding motif 1; mediates interaction with the EJC|||EJC-binding motif 2; mediates interaction with the EJC|||Impaired nonsense-mediated RNA decay.|||Impaired nonsense-mediated RNA decay; when associated with A-1251.|||In isoform 2.|||In isoform 3.|||Interaction with telomeric DNA|||Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1251.|||Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1392.|||Omega-N-methylarginine|||PINc|||Phosphoserine|||Phosphothreonine|||Polar residues|||Telomerase-binding protein EST1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087069|||http://purl.uniprot.org/annotation/VAR_018499|||http://purl.uniprot.org/annotation/VAR_018500|||http://purl.uniprot.org/annotation/VAR_018501|||http://purl.uniprot.org/annotation/VAR_018502|||http://purl.uniprot.org/annotation/VAR_018503|||http://purl.uniprot.org/annotation/VAR_050978|||http://purl.uniprot.org/annotation/VAR_050979|||http://purl.uniprot.org/annotation/VAR_061648|||http://purl.uniprot.org/annotation/VSP_010360|||http://purl.uniprot.org/annotation/VSP_010361|||http://purl.uniprot.org/annotation/VSP_047157
http://togogenome.org/gene/9606:C19orf73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVV2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Putative uncharacterized protein C19orf73                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348438|||http://purl.uniprot.org/annotation/VAR_046164
http://togogenome.org/gene/9606:MTRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBK8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  FAD-binding FR-type|||Flavodoxin-like|||Hinge|||In HMAE.|||In isoform A.|||May increase risk for spina bifida.|||Methionine synthase reductase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021785|||http://purl.uniprot.org/annotation/VAR_012836|||http://purl.uniprot.org/annotation/VAR_012837|||http://purl.uniprot.org/annotation/VAR_012838|||http://purl.uniprot.org/annotation/VAR_012839|||http://purl.uniprot.org/annotation/VAR_012840|||http://purl.uniprot.org/annotation/VAR_012841|||http://purl.uniprot.org/annotation/VAR_012842|||http://purl.uniprot.org/annotation/VAR_012843|||http://purl.uniprot.org/annotation/VAR_014944|||http://purl.uniprot.org/annotation/VAR_015731|||http://purl.uniprot.org/annotation/VAR_034595|||http://purl.uniprot.org/annotation/VAR_034596|||http://purl.uniprot.org/annotation/VAR_034597|||http://purl.uniprot.org/annotation/VAR_034598|||http://purl.uniprot.org/annotation/VAR_034599|||http://purl.uniprot.org/annotation/VAR_056947|||http://purl.uniprot.org/annotation/VSP_060027
http://togogenome.org/gene/9606:HMOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09601|||http://purl.uniprot.org/uniprot/Q6FH11                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Heme oxygenase 1|||Heme oxygenase 1 soluble form|||Important for catalytic activity|||Inactive as a heme oxygenase but active as a peroxidase.|||No effect on catalytic activity, oligomerization and localization to the endoplasmic reticulum.|||Phosphoserine|||Polar residues|||Significant reduction in catalytic activity, reduced oligomerization, reduced endoplasmic reticulum localization with cytoplasmic mislocalization.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209687|||http://purl.uniprot.org/annotation/PRO_0000455621|||http://purl.uniprot.org/annotation/VAR_019165|||http://purl.uniprot.org/annotation/VAR_022156
http://togogenome.org/gene/9606:TYW3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPR3|||http://purl.uniprot.org/uniprot/Q96GE7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||tRNA wybutosine-synthesizing protein 3 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281842|||http://purl.uniprot.org/annotation/VAR_031292|||http://purl.uniprot.org/annotation/VAR_031293|||http://purl.uniprot.org/annotation/VSP_044477
http://togogenome.org/gene/9606:FIZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Flt3-interacting zinc finger protein 1|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046937|||http://purl.uniprot.org/annotation/VAR_060269
http://togogenome.org/gene/9606:ERMN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIZ1|||http://purl.uniprot.org/uniprot/Q8TAM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Binds actin|||Disordered|||Ermin|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314748|||http://purl.uniprot.org/annotation/VSP_036982
http://togogenome.org/gene/9606:RNF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBF6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphothreonine; by CK2|||RING-box protein 2|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056023|||http://purl.uniprot.org/annotation/VSP_008449|||http://purl.uniprot.org/annotation/VSP_041444|||http://purl.uniprot.org/annotation/VSP_044525
http://togogenome.org/gene/9606:GPAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDG5|||http://purl.uniprot.org/uniprot/Q53EU6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Glycerol-3-phosphate acyltransferase 3|||HXXXXD motif|||Helical|||Phospholipid/glycerol acyltransferase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291570
http://togogenome.org/gene/9606:RBFOX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2.|||Interaction with RNA|||Omega-N-methylarginine; alternate|||Polar residues|||Pro residues|||RNA binding protein fox-1 homolog 3|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349207|||http://purl.uniprot.org/annotation/VSP_056241
http://togogenome.org/gene/9606:NR3C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KQF5|||http://purl.uniprot.org/uniprot/E5KQF6|||http://purl.uniprot.org/uniprot/F1D8N4|||http://purl.uniprot.org/uniprot/P04150                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes expression of A-type isoforms.|||Abolishes expression of B-type isoforms.|||Abolishes expression of C-type isoforms; when associated with I-86 and I-90.|||Abolishes expression of C-type isoforms; when associated with I-86 and I-98.|||Abolishes expression of C-type isoforms; when associated with I-90 and I-98.|||Abolishes expression of D-type isoforms; when associated with I-316 and I-331.|||Abolishes expression of D-type isoforms; when associated with I-316 and I-336.|||Abolishes expression of D-type isoforms; when associated with I-331 and I-336.|||Abolishes phosphorylation and enhances transcriptional activation.|||Abolishes phosphorylation. Does not affect translocation to the nucleus following ligand stimulation. Increases protein half-life and transcriptional repressor activity. Alters repertoire of regulated genes. Increases cell death.|||Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-494 and A-495.|||Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-492; A-494 and A-495.|||Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-494. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-492 and A-494.|||Decrease in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-495. Complete loss in acetylation and in repression of its transcriptional activity by CLOCK-BMAL1 heterodimer; when associated with A-480; A-492 and A-495.|||Decreases dimerization and transactivation by dexamethasone; when associated with S-602.|||Decreases transactivation by dexamethasone by 95%.|||Disordered|||Does not affect the activity of isoform Alpha-C3.|||Does not affect translocation to the nucleus following ligand stimulation.|||Enhances transactivation activity; does not affect transrepression activity; may increase sensitivity to exogenously administered glucocorticoids; may contribute to central obesity in men and show lack of association with other risk factors for coronary heart disease and diabetes mellitus.|||Glucocorticoid receptor|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hinge|||In GCCR.|||In GCCR; alters interaction with NCOA2 and strongly reduces transcription activation; acts as dominant negative mutant.|||In GCCR; decreased DNA-binding and transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type.|||In GCCR; has 50% binding affinity.|||In GCCR; interferes with translocation to the nucleus and thereby strongly reduces transcription activation; is equally impaired in nuclear export; acts as dominant negative mutant.|||In GCCR; loss of DNA-binding and of transactivation activity; incomplete dexamethasone-induced translocation to the nucleus; no effect on dexamethasone-binding affinity compared with wild-type.|||In GCCR; loss of dexamethasone-binding, dexamethasone-induced translocation to the nucleus and of transactivation activity.|||In GCCR; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding.|||In GCCR; reduces transactivation of the glucocorticoid-inducible tumor virus promoter; reduces affinity for ligand; delays its nuclear translocation; acts as dominant negative mutant.|||In GCCR; unknown pathological significance; reduces transactivation activity; delays nuclear translocation; does not exert a dominant negative effect; impairs DNA binding.|||In GCCR; unknown pathological significance; reduces transactivation activity; enhances transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not exert a dominant negative effect; does not impair DNA binding.|||In GCCR; unknown pathological significance; reduces transactivation and transrepression activity; reduces affinity for ligand; delays nuclear translocation; does not impair DNA binding.|||In GCCR; unknown pathological significance; reduces transactivation; reduces affinity for ligand; exerts a dominant negative effect; does not impair DNA binding.|||In isoform 10.|||In isoform Alpha-2 and isoform Beta-2.|||In isoform Alpha-B and isoform Beta-B.|||In isoform Alpha-C1.|||In isoform Alpha-C2.|||In isoform Alpha-C3.|||In isoform Alpha-D1.|||In isoform Alpha-D2.|||In isoform Alpha-D3.|||In isoform Beta, isoform Beta-B, isoform Beta-2 and isoform GR-A beta.|||In isoform GR-A alpha and isoform GR-A beta.|||In pseudohermaphroditism; female with hypokalemia due to glucocorticoid resistance; 6-fold reduction in binding affinity compared with the wild-type receptor.|||Increases solubility. No effect on transactivation by dexamethasone.|||Interaction with CLOCK|||Interaction with CRY1|||Modulating|||N-acetylmethionine|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Polar residues|||Reduces activation mediated by ligand binding domain; when associated with A-585.|||Reduces activation mediated by ligand binding domain; when associated with A-590.|||Reduces activity of isoform Alpha-C3 by half.|||Reduces expression of target genes IGFBP1 and IRF8.|||Reduces transactivation activity; does not affect transrepression activity.|||Reduces transactivation by the ADA complex.|||Reduces transcription activation activity of isoform Alpha-C3 by half.|||Reduces transcription activation activity of isoform Alpha-C3 by half. Suppresses apoptosis-inducing activity of isoform Alpha-C3. Impairs recruitment of selected coregulators onto DNA binding sites.|||Required for high transcriptional activity of isoform Alpha-C3|||Slightly reduces sumoylation. Inhibits the stimulatory effect of RWDD3 on its transcriptional activity.|||Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277.|||Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293.|||Strongly reduces transactivation by the ADA complex.|||Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225.|||Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224.|||Strongly reduces transactivation by the ADA complex; when associated with L-235.|||Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225.|||Strongly reduces transactivation by the ADA complex; when associated with V-236.|||Variant of uncertain significance; associated in cis with A-321 and S-766 in one individual; doubles transactivation potential.|||Variant of uncertain significance; associated in cis with D-72 and A-321 in one individual; doubles transactivation potential.|||Variant of uncertain significance; associated in cis with D-72 and S-766 in one individual; doubles transactivation potential. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019937|||http://purl.uniprot.org/annotation/VAR_004675|||http://purl.uniprot.org/annotation/VAR_004676|||http://purl.uniprot.org/annotation/VAR_004677|||http://purl.uniprot.org/annotation/VAR_004678|||http://purl.uniprot.org/annotation/VAR_013472|||http://purl.uniprot.org/annotation/VAR_013473|||http://purl.uniprot.org/annotation/VAR_014140|||http://purl.uniprot.org/annotation/VAR_014622|||http://purl.uniprot.org/annotation/VAR_015628|||http://purl.uniprot.org/annotation/VAR_015629|||http://purl.uniprot.org/annotation/VAR_015630|||http://purl.uniprot.org/annotation/VAR_015631|||http://purl.uniprot.org/annotation/VAR_015632|||http://purl.uniprot.org/annotation/VAR_015633|||http://purl.uniprot.org/annotation/VAR_025014|||http://purl.uniprot.org/annotation/VAR_071935|||http://purl.uniprot.org/annotation/VAR_071936|||http://purl.uniprot.org/annotation/VAR_075797|||http://purl.uniprot.org/annotation/VAR_075798|||http://purl.uniprot.org/annotation/VAR_075799|||http://purl.uniprot.org/annotation/VAR_075800|||http://purl.uniprot.org/annotation/VAR_075801|||http://purl.uniprot.org/annotation/VAR_075802|||http://purl.uniprot.org/annotation/VAR_075803|||http://purl.uniprot.org/annotation/VAR_075804|||http://purl.uniprot.org/annotation/VAR_077143|||http://purl.uniprot.org/annotation/VAR_077144|||http://purl.uniprot.org/annotation/VAR_077145|||http://purl.uniprot.org/annotation/VSP_003703|||http://purl.uniprot.org/annotation/VSP_007363|||http://purl.uniprot.org/annotation/VSP_013340|||http://purl.uniprot.org/annotation/VSP_018773|||http://purl.uniprot.org/annotation/VSP_043908|||http://purl.uniprot.org/annotation/VSP_058312|||http://purl.uniprot.org/annotation/VSP_058313|||http://purl.uniprot.org/annotation/VSP_058314|||http://purl.uniprot.org/annotation/VSP_058315|||http://purl.uniprot.org/annotation/VSP_058316|||http://purl.uniprot.org/annotation/VSP_058317
http://togogenome.org/gene/9606:OPN1LW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04000                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In 62% of the population.|||In BCM.|||In CBP.|||Long-wave-sensitive opsin 1|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||O-linked (GlcNAc) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197802|||http://purl.uniprot.org/annotation/VAR_004842|||http://purl.uniprot.org/annotation/VAR_009298|||http://purl.uniprot.org/annotation/VAR_009299|||http://purl.uniprot.org/annotation/VAR_012010|||http://purl.uniprot.org/annotation/VAR_012011|||http://purl.uniprot.org/annotation/VAR_012012|||http://purl.uniprot.org/annotation/VAR_012014|||http://purl.uniprot.org/annotation/VAR_012015|||http://purl.uniprot.org/annotation/VAR_050612|||http://purl.uniprot.org/annotation/VAR_064054
http://togogenome.org/gene/9606:COPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61201|||http://purl.uniprot.org/uniprot/Q59EL2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  COP9 signalosome complex subunit 2|||In isoform 2.|||Mediates interaction with NIF3L1|||PCI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120968|||http://purl.uniprot.org/annotation/VSP_011884
http://togogenome.org/gene/9606:PIERCE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BRN8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Piercer of microtubule wall 2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423417
http://togogenome.org/gene/9606:SLF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L9F1|||http://purl.uniprot.org/uniprot/Q9BQI6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||BRCT 1|||BRCT 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||NSE5-like domain; mediates interaction with SLF2|||SMC5-SMC6 complex localization factor protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243906|||http://purl.uniprot.org/annotation/VAR_059120|||http://purl.uniprot.org/annotation/VSP_056914|||http://purl.uniprot.org/annotation/VSP_056915
http://togogenome.org/gene/9606:PARP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGN5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished formation of a complex with core nucleosome and HPF1, leading to abolished ability to catalyze serine ADP-ribosylation of histones.|||Abolished formation of a complex with core nucleosome and HPF1, leading to abolished ability to catalyze serine ADP-ribosylation of histones. Abolished DNA-induced ADP-ribosyltransferase activity. Abolished trapping at DNA damage sites upon binding to PARP inhibitors (PARPi).|||Abolished poly [ADP-ribose] polymerase activity without affecting localization to DNA damage sites.|||Abolished trapping at DNA damage sites upon binding to PARP inhibitors (PARPi).|||Basic and acidic residues|||Cleavage; by caspase-8|||Decreased poly [ADP-ribose] polymerase activity.|||Decreased poly [ADP-ribose] polymerase activity. Impaired formation of a complex with damaged DNA.|||Disordered|||Does not affect DNA-induced ADP-ribosyltransferase activity.|||Does not affect poly [ADP-ribose] polymerase activity.|||For poly [ADP-ribose] polymerase activity|||In PARP2-QFRD mutant; induces conformational change that bridges nucleosomes by binding to linker DNA ends and promotes interaction with HPF1.|||In isoform 2.|||Increased DNA-induced ADP-ribosyltransferase activity.|||N-terminal region (NTR)|||N6-acetyllysine|||Nuclear localization signal|||PARP alpha-helical|||PARP catalytic|||Phosphoserine|||Poly [ADP-ribose] polymerase 2|||Reduced DNA-induced ADP-ribosyltransferase activity.|||Reduced localization to the nucleus. Abolished localization to the nucleus; when associated with 21-A-A-22.|||Reduced localization to the nucleus. Abolished localization to the nucleus; when associated with 37-A-A-38.|||Reduced recruitment to DNA damage sites. Abolished DNA-induced ADP-ribosyltransferase activity.|||Reduced recruitment to DNA damage sites. Decreased poly [ADP-ribose] polymerase activity.|||Strongly reduced serine ADP-ribosylation, caused by abolished interaction with HPF1.|||WGR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211327|||http://purl.uniprot.org/annotation/VAR_019174|||http://purl.uniprot.org/annotation/VAR_019175|||http://purl.uniprot.org/annotation/VAR_019176|||http://purl.uniprot.org/annotation/VAR_019177|||http://purl.uniprot.org/annotation/VAR_019178|||http://purl.uniprot.org/annotation/VAR_050462|||http://purl.uniprot.org/annotation/VSP_004537
http://togogenome.org/gene/9606:C9orf152                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2L3|||http://purl.uniprot.org/uniprot/Q5JTZ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  TBC1|||Uncharacterized protein C9orf152                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229729
http://togogenome.org/gene/9606:LRRC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q50LG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 24|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231596
http://togogenome.org/gene/9606:PYURF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of interaction with NDUFAF5.|||Mitochondrion|||Protein preY, mitochondrial|||Reduces interaction with NDUFAF5.|||TRM112                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246315
http://togogenome.org/gene/9606:KRT6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48668                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In PPKNEFD; collapsed of the keratin filament network in a dose-dependent manner.|||In PPKNEFD; unknown pathological significance.|||Keratin, type II cytoskeletal 6C|||Linker 1|||Linker 12|||N-acetylalanine|||Phosphoserine|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063735|||http://purl.uniprot.org/annotation/VAR_035031|||http://purl.uniprot.org/annotation/VAR_035032|||http://purl.uniprot.org/annotation/VAR_035033|||http://purl.uniprot.org/annotation/VAR_071308|||http://purl.uniprot.org/annotation/VAR_071309
http://togogenome.org/gene/9606:PROC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPC8|||http://purl.uniprot.org/uniprot/P04070                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Activation peptide|||Charge relay system|||Cleavage; by thrombin|||Disordered|||EGF-like 1|||EGF-like 2|||Gain of function mutation; abolishes glycosylation at N-313; decreases its catalytic activity; significant loss of its protective effect on endothelial barrier function; increased activation by thrombin.|||Gla|||In Malakoff; low anticoagulant activity.|||In Marseille; low anticoagulant activity.|||In Paris; low anticoagulant activity.|||In THPH3.|||In THPH3; La Jolla-2/Osaka-7 and -8.|||In THPH3; London-1/Tochigi.|||In THPH3; Osaka-4.|||In THPH3; Osaka-6.|||In THPH3; Osaka-9.|||In THPH3; Vermont-1.|||In THPH3; Vermont-2.|||In THPH3; Vermont-3.|||In THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity.|||In THPH3; also found in patients with PROC deficiency; decrease in vitamin-K dependent serine protease activity; decreased Golgi localization.|||In THPH3; drastically reduced secretion; colocalizes with 26S proteasome.|||In THPH3; type II; Osaka-10; alters proteolytic processing so that S-42 is the N-terminus of the mature protein.|||In THPH4.|||In THPH4; Clamart.|||In THPH4; Hong Kong-2.|||In THPH4; Muenchen.|||In THPH4; drastically reduced secretion; colocalizes with 26S proteasome.|||In THPH4; neonatal purpura fulminans.|||In THPH4; no effect on secretion; no effect on catalytic activity in vitro.|||In Yonago; defective anticoagulant activity.|||In a patient with PROC deficiency; sporadic case.|||In isoform 2.|||In patients with PROC deficiency.|||In patients with PROC deficiency; La Jolla-1.|||In patients with PROC deficiency; La Jolla-3.|||In patients with PROC deficiency; Purmerend.|||In patients with PROC deficiency; St Louis-2.|||In patients with PROC deficiency; St Louis-3.|||In patients with PROC deficiency; abolishes Golgi localization.|||In patients with PROC deficiency; requires 2 nucleotide substitutions.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical; partial|||O-linked (GalNAc...) threonine|||Peptidase S1|||Phosphoserine; by FAM20C|||Vitamin K-dependent protein C|||Vitamin K-dependent protein C heavy chain|||Vitamin K-dependent protein C light chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028107|||http://purl.uniprot.org/annotation/PRO_0000028108|||http://purl.uniprot.org/annotation/PRO_0000028109|||http://purl.uniprot.org/annotation/PRO_0000028110|||http://purl.uniprot.org/annotation/PRO_0000028111|||http://purl.uniprot.org/annotation/VAR_006634|||http://purl.uniprot.org/annotation/VAR_006635|||http://purl.uniprot.org/annotation/VAR_006636|||http://purl.uniprot.org/annotation/VAR_006637|||http://purl.uniprot.org/annotation/VAR_006638|||http://purl.uniprot.org/annotation/VAR_006639|||http://purl.uniprot.org/annotation/VAR_006640|||http://purl.uniprot.org/annotation/VAR_006641|||http://purl.uniprot.org/annotation/VAR_006642|||http://purl.uniprot.org/annotation/VAR_006643|||http://purl.uniprot.org/annotation/VAR_006644|||http://purl.uniprot.org/annotation/VAR_006645|||http://purl.uniprot.org/annotation/VAR_006646|||http://purl.uniprot.org/annotation/VAR_006647|||http://purl.uniprot.org/annotation/VAR_006648|||http://purl.uniprot.org/annotation/VAR_006649|||http://purl.uniprot.org/annotation/VAR_006650|||http://purl.uniprot.org/annotation/VAR_006651|||http://purl.uniprot.org/annotation/VAR_006652|||http://purl.uniprot.org/annotation/VAR_006653|||http://purl.uniprot.org/annotation/VAR_006654|||http://purl.uniprot.org/annotation/VAR_006655|||http://purl.uniprot.org/annotation/VAR_006656|||http://purl.uniprot.org/annotation/VAR_006657|||http://purl.uniprot.org/annotation/VAR_006658|||http://purl.uniprot.org/annotation/VAR_006659|||http://purl.uniprot.org/annotation/VAR_006660|||http://purl.uniprot.org/annotation/VAR_006661|||http://purl.uniprot.org/annotation/VAR_006662|||http://purl.uniprot.org/annotation/VAR_006663|||http://purl.uniprot.org/annotation/VAR_006664|||http://purl.uniprot.org/annotation/VAR_006665|||http://purl.uniprot.org/annotation/VAR_006666|||http://purl.uniprot.org/annotation/VAR_006667|||http://purl.uniprot.org/annotation/VAR_006668|||http://purl.uniprot.org/annotation/VAR_006669|||http://purl.uniprot.org/annotation/VAR_006670|||http://purl.uniprot.org/annotation/VAR_006671|||http://purl.uniprot.org/annotation/VAR_006672|||http://purl.uniprot.org/annotation/VAR_006673|||http://purl.uniprot.org/annotation/VAR_006674|||http://purl.uniprot.org/annotation/VAR_006675|||http://purl.uniprot.org/annotation/VAR_006676|||http://purl.uniprot.org/annotation/VAR_006677|||http://purl.uniprot.org/annotation/VAR_006678|||http://purl.uniprot.org/annotation/VAR_006679|||http://purl.uniprot.org/annotation/VAR_006680|||http://purl.uniprot.org/annotation/VAR_006681|||http://purl.uniprot.org/annotation/VAR_006682|||http://purl.uniprot.org/annotation/VAR_006683|||http://purl.uniprot.org/annotation/VAR_006684|||http://purl.uniprot.org/annotation/VAR_006685|||http://purl.uniprot.org/annotation/VAR_006686|||http://purl.uniprot.org/annotation/VAR_006687|||http://purl.uniprot.org/annotation/VAR_006688|||http://purl.uniprot.org/annotation/VAR_006689|||http://purl.uniprot.org/annotation/VAR_006690|||http://purl.uniprot.org/annotation/VAR_006691|||http://purl.uniprot.org/annotation/VAR_006692|||http://purl.uniprot.org/annotation/VAR_006693|||http://purl.uniprot.org/annotation/VAR_006694|||http://purl.uniprot.org/annotation/VAR_006695|||http://purl.uniprot.org/annotation/VAR_006696|||http://purl.uniprot.org/annotation/VAR_006697|||http://purl.uniprot.org/annotation/VAR_006698|||http://purl.uniprot.org/annotation/VAR_006699|||http://purl.uniprot.org/annotation/VAR_006700|||http://purl.uniprot.org/annotation/VAR_006701|||http://purl.uniprot.org/annotation/VAR_006702|||http://purl.uniprot.org/annotation/VAR_006703|||http://purl.uniprot.org/annotation/VAR_006704|||http://purl.uniprot.org/annotation/VAR_006705|||http://purl.uniprot.org/annotation/VAR_006706|||http://purl.uniprot.org/annotation/VAR_006707|||http://purl.uniprot.org/annotation/VAR_006708|||http://purl.uniprot.org/annotation/VAR_006709|||http://purl.uniprot.org/annotation/VAR_006710|||http://purl.uniprot.org/annotation/VAR_055074|||http://purl.uniprot.org/annotation/VAR_073145|||http://purl.uniprot.org/annotation/VAR_073146|||http://purl.uniprot.org/annotation/VAR_073147|||http://purl.uniprot.org/annotation/VAR_074296|||http://purl.uniprot.org/annotation/VAR_074297|||http://purl.uniprot.org/annotation/VAR_074298|||http://purl.uniprot.org/annotation/VAR_074299|||http://purl.uniprot.org/annotation/VAR_074300|||http://purl.uniprot.org/annotation/VAR_074301|||http://purl.uniprot.org/annotation/VAR_074302|||http://purl.uniprot.org/annotation/VAR_074303|||http://purl.uniprot.org/annotation/VAR_074304|||http://purl.uniprot.org/annotation/VAR_074305|||http://purl.uniprot.org/annotation/VAR_074306|||http://purl.uniprot.org/annotation/VAR_074307|||http://purl.uniprot.org/annotation/VSP_054393|||http://purl.uniprot.org/annotation/VSP_054394
http://togogenome.org/gene/9606:ABCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUJ3|||http://purl.uniprot.org/uniprot/Q8IZY2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||Basic and acidic residues|||Disordered|||Extracellular|||Helical|||In AD9.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phospholipid-transporting ATPase ABCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250674|||http://purl.uniprot.org/annotation/VAR_027581|||http://purl.uniprot.org/annotation/VAR_027582|||http://purl.uniprot.org/annotation/VAR_027583|||http://purl.uniprot.org/annotation/VAR_027584|||http://purl.uniprot.org/annotation/VAR_027585|||http://purl.uniprot.org/annotation/VAR_027586|||http://purl.uniprot.org/annotation/VAR_027587|||http://purl.uniprot.org/annotation/VAR_027588|||http://purl.uniprot.org/annotation/VAR_027589|||http://purl.uniprot.org/annotation/VAR_060985|||http://purl.uniprot.org/annotation/VAR_081204|||http://purl.uniprot.org/annotation/VSP_020701|||http://purl.uniprot.org/annotation/VSP_020702
http://togogenome.org/gene/9606:BMAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKD3|||http://purl.uniprot.org/uniprot/A0A669KBF4|||http://purl.uniprot.org/uniprot/B2RCL8|||http://purl.uniprot.org/uniprot/O00327                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  2-2.5-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1.|||BHLH|||Basic and acidic residues|||Basic helix-loop-helix ARNT-like protein 1|||Disordered|||Enhanced PER1 reporter activity by CLOCK-BMAL1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired CLOCK binding.|||Important for interaction with CLOCK|||In isoform 8 and isoform 9.|||In isoform BMAL1A and isoform 9.|||In isoform BMAL1C.|||In isoform BMAL1D.|||In isoform BMAL1E.|||In isoform BMAL1F.|||In isoform MOP3.|||Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1.|||Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1; when associated with E-407.|||Interaction with CIART|||Interaction with E-box DNA|||N6-acetyllysine|||No effect on CLOCK binding.|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphomimetic mutant which severely impairs DNA binding and CLOCK-BMAL1 transcriptional activity.|||Phosphomimetic mutant with no effect on DNA binding or CLOCK-BMAL1 transcriptional activity.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by GSK3-beta|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127156|||http://purl.uniprot.org/annotation/VSP_002094|||http://purl.uniprot.org/annotation/VSP_002095|||http://purl.uniprot.org/annotation/VSP_002096|||http://purl.uniprot.org/annotation/VSP_002097|||http://purl.uniprot.org/annotation/VSP_002098|||http://purl.uniprot.org/annotation/VSP_002099|||http://purl.uniprot.org/annotation/VSP_002100|||http://purl.uniprot.org/annotation/VSP_002101|||http://purl.uniprot.org/annotation/VSP_002102|||http://purl.uniprot.org/annotation/VSP_035457
http://togogenome.org/gene/9606:SPDYC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MJ68                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Speedy protein C|||Speedy/Ringo box; Required for CDK-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234116
http://togogenome.org/gene/9606:PP2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MPX8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PPM-type phosphatase|||Protein phosphatase 2C-like domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320672|||http://purl.uniprot.org/annotation/VAR_039272|||http://purl.uniprot.org/annotation/VAR_039273|||http://purl.uniprot.org/annotation/VAR_039274|||http://purl.uniprot.org/annotation/VSP_031721|||http://purl.uniprot.org/annotation/VSP_031722|||http://purl.uniprot.org/annotation/VSP_031723|||http://purl.uniprot.org/annotation/VSP_031724
http://togogenome.org/gene/9606:MRPL43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4V4|||http://purl.uniprot.org/uniprot/Q8N983                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Large ribosomal subunit protein mL43|||Mitochondrion|||Ribosomal protein/NADH dehydrogenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030561|||http://purl.uniprot.org/annotation/VSP_011026|||http://purl.uniprot.org/annotation/VSP_011027|||http://purl.uniprot.org/annotation/VSP_011028|||http://purl.uniprot.org/annotation/VSP_011029|||http://purl.uniprot.org/annotation/VSP_011030|||http://purl.uniprot.org/annotation/VSP_054092|||http://purl.uniprot.org/annotation/VSP_054093
http://togogenome.org/gene/9606:HINT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX68                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Adenosine 5'-monophosphoramidase HINT2|||HIT|||Histidine triad motif|||Loss of adenosine phosphoramidase activity.|||Mitochondrion|||N6-acetyllysine|||Tele-AMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109786
http://togogenome.org/gene/9606:SLC25A52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L0B8|||http://purl.uniprot.org/uniprot/Q3SY17                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Mitochondrial nicotinamide adenine dinucleotide transporter SLC25A52|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271790|||http://purl.uniprot.org/annotation/VAR_060299
http://togogenome.org/gene/9606:TET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form KMT2A/MLL1-TET1 oncogene|||CXXC-type|||Disordered|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with DNA|||Loss of catalytic activity and loss of the ability to induce DNA demethylation; when associated with A-1674. When transfected in knockout cells, fails to restore pancreatic beta-cell specification, as shown by impaired NKX6.1, PAX6, PDX1 and INS expression; when associated with A-1674.|||Loss of catalytic activity and loss of the ability to induce DNA demethylation; when associated with Y-1672. When transfected in knockout cells, fails to restore pancreatic beta-cell specification, as shown by impaired NKX6.1, PAX6, PDX1 and INS expression; when associated with Y-1672.|||Methylcytosine dioxygenase TET1|||Phosphoserine|||Polar residues|||Sufficient for binding to genomic CpG islands                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251949|||http://purl.uniprot.org/annotation/VAR_027734|||http://purl.uniprot.org/annotation/VAR_027735|||http://purl.uniprot.org/annotation/VAR_027736|||http://purl.uniprot.org/annotation/VAR_027737|||http://purl.uniprot.org/annotation/VAR_027738|||http://purl.uniprot.org/annotation/VAR_080763|||http://purl.uniprot.org/annotation/VSP_061826|||http://purl.uniprot.org/annotation/VSP_061827|||http://purl.uniprot.org/annotation/VSP_061828|||http://purl.uniprot.org/annotation/VSP_061829
http://togogenome.org/gene/9606:GAGE12H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDE8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339404
http://togogenome.org/gene/9606:ESS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WEF8|||http://purl.uniprot.org/uniprot/Q96DF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Splicing factor ESS-2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079876|||http://purl.uniprot.org/annotation/VAR_015117|||http://purl.uniprot.org/annotation/VAR_015118|||http://purl.uniprot.org/annotation/VAR_015119
http://togogenome.org/gene/9606:FAM161A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B820                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In RP28.|||In isoform 2.|||In isoform 3.|||Protein FAM161A|||Required for interaction with CFAP418                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329052|||http://purl.uniprot.org/annotation/VAR_042630|||http://purl.uniprot.org/annotation/VAR_042631|||http://purl.uniprot.org/annotation/VAR_060180|||http://purl.uniprot.org/annotation/VAR_083934|||http://purl.uniprot.org/annotation/VSP_032935|||http://purl.uniprot.org/annotation/VSP_039126
http://togogenome.org/gene/9606:IQCJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1A5X6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||IQ|||IQ domain-containing protein J|||In isoform IQCJ-2.|||In isoform IQCJ-3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315661|||http://purl.uniprot.org/annotation/VSP_030597|||http://purl.uniprot.org/annotation/VSP_043259
http://togogenome.org/gene/9606:EBNA1BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C2Q8|||http://purl.uniprot.org/uniprot/Q6IB29|||http://purl.uniprot.org/uniprot/Q99848                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Probable rRNA-processing protein EBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119993|||http://purl.uniprot.org/annotation/VAR_024437
http://togogenome.org/gene/9606:EMCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4W5J1|||http://purl.uniprot.org/uniprot/Q9ULC0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Endomucin|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019290|||http://purl.uniprot.org/annotation/PRO_5014309452|||http://purl.uniprot.org/annotation/VSP_010826|||http://purl.uniprot.org/annotation/VSP_043264
http://togogenome.org/gene/9606:PGLYRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75594                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmuramoyl-L-alanine amidase|||N-linked (GlcNAc...) asparagine|||Peptidoglycan recognition protein 1|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023901|||http://purl.uniprot.org/annotation/VAR_050497
http://togogenome.org/gene/9606:RLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04808                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Connecting peptide|||In isoform 2.|||Interchain (between B and A chains)|||Relaxin A chain|||Relaxin B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016076|||http://purl.uniprot.org/annotation/PRO_0000016077|||http://purl.uniprot.org/annotation/PRO_0000016078|||http://purl.uniprot.org/annotation/VAR_011962|||http://purl.uniprot.org/annotation/VSP_002709|||http://purl.uniprot.org/annotation/VSP_002710
http://togogenome.org/gene/9606:OR10A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVZ2|||http://purl.uniprot.org/uniprot/P58181                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150685|||http://purl.uniprot.org/annotation/VAR_053262
http://togogenome.org/gene/9606:UVSSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2YD98|||http://purl.uniprot.org/uniprot/Q69YU2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs interaction with the TFIIH complex.|||Impairs transcription-coupled nucleotide excision repair ability.|||In UVSS3; mild phenotype; impairs transcription-coupled nucleotide excision repair ability.|||In isoform 2.|||Phosphoserine|||UV-stimulated scaffold protein A|||VHS-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317282|||http://purl.uniprot.org/annotation/VAR_038499|||http://purl.uniprot.org/annotation/VAR_038500|||http://purl.uniprot.org/annotation/VAR_067798|||http://purl.uniprot.org/annotation/VSP_030932
http://togogenome.org/gene/9606:ITLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fibrinogen C-terminal|||In isoform 2.|||Intelectin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009149|||http://purl.uniprot.org/annotation/VAR_019926|||http://purl.uniprot.org/annotation/VAR_049076|||http://purl.uniprot.org/annotation/VSP_055093
http://togogenome.org/gene/9606:CSTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3V096|||http://purl.uniprot.org/uniprot/B4DUD5|||http://purl.uniprot.org/uniprot/E7EWR4|||http://purl.uniprot.org/uniprot/P33240                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10; approximate|||11|||12 X 5 AA tandem repeats of M-E-A-R-[AG]|||12; approximate|||1; approximate|||2|||3|||4; approximate|||5; approximate|||6|||7|||8|||9|||Cleavage stimulation factor subunit 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RPO2TC1|||Interactions with CSTF3 and SYMPK|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081531|||http://purl.uniprot.org/annotation/VSP_014841
http://togogenome.org/gene/9606:ANK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12955|||http://purl.uniprot.org/uniprot/Q8NAK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin-3|||Basic and acidic residues|||Death|||Disordered|||Found in a patient with Gillessen-Kaesbach-Nishimura syndrome; unknown pathological significance.|||Found in a patient with autism; unknown pathological significance.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||UPA domain|||ZU5|||ZU5 1|||ZU5 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066886|||http://purl.uniprot.org/annotation/VAR_054333|||http://purl.uniprot.org/annotation/VAR_059115|||http://purl.uniprot.org/annotation/VAR_059116|||http://purl.uniprot.org/annotation/VAR_059117|||http://purl.uniprot.org/annotation/VAR_061013|||http://purl.uniprot.org/annotation/VAR_061014|||http://purl.uniprot.org/annotation/VAR_068702|||http://purl.uniprot.org/annotation/VAR_068703|||http://purl.uniprot.org/annotation/VAR_068704|||http://purl.uniprot.org/annotation/VAR_077912|||http://purl.uniprot.org/annotation/VSP_044348|||http://purl.uniprot.org/annotation/VSP_044349|||http://purl.uniprot.org/annotation/VSP_044350|||http://purl.uniprot.org/annotation/VSP_044351|||http://purl.uniprot.org/annotation/VSP_044352|||http://purl.uniprot.org/annotation/VSP_044353|||http://purl.uniprot.org/annotation/VSP_044354|||http://purl.uniprot.org/annotation/VSP_046885|||http://purl.uniprot.org/annotation/VSP_046886|||http://purl.uniprot.org/annotation/VSP_053753|||http://purl.uniprot.org/annotation/VSP_053754|||http://purl.uniprot.org/annotation/VSP_053755|||http://purl.uniprot.org/annotation/VSP_053756|||http://purl.uniprot.org/annotation/VSP_053757|||http://purl.uniprot.org/annotation/VSP_053758|||http://purl.uniprot.org/annotation/VSP_053759
http://togogenome.org/gene/9606:SH3BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFX7|||http://purl.uniprot.org/uniprot/Q9Y3L3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAR|||Disordered|||In isoform 2.|||Interaction with CD2AP|||Interaction with CGNL1|||Phosphoserine|||Phosphothreonine|||Pro residues|||Probable loss of the GTPase activator activity. Loss of function in cell migration.|||Rho-GAP|||SH3 domain-binding protein 1|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056723|||http://purl.uniprot.org/annotation/VAR_033450|||http://purl.uniprot.org/annotation/VAR_033451|||http://purl.uniprot.org/annotation/VSP_011373|||http://purl.uniprot.org/annotation/VSP_011374
http://togogenome.org/gene/9606:ZNF526                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9ZYJ3|||http://purl.uniprot.org/uniprot/Q8TF50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In DENNED; unknown pathological significance.|||Pro residues|||Zinc finger protein 526                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306875|||http://purl.uniprot.org/annotation/VAR_035331|||http://purl.uniprot.org/annotation/VAR_035332|||http://purl.uniprot.org/annotation/VAR_087342|||http://purl.uniprot.org/annotation/VAR_087343
http://togogenome.org/gene/9606:NAGLU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE4|||http://purl.uniprot.org/uniprot/P54802                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-N-acetylglucosaminidase 77 kDa form|||Alpha-N-acetylglucosaminidase 82 kDa form|||Alpha-N-acetylglucosaminidase C-terminal|||Alpha-N-acetylglucosaminidase N-terminal|||Alpha-N-acetylglucosaminidase tim-barrel|||In CMT2V.|||In MPS3B.|||In MPS3B; accounts for approximately 20% of MPS3B alleles in a Dutch patient group.|||In MPS3B; accounts for approximately 6% of mutations in Australasian patients with MPS3B.|||In MPS3B; accounts for approximately 6% of the mutant alleles in Australasian patients with MPS3B.|||In MPS3B; associated with a partially degraded polypeptide in a 16-hour chase experiment suggesting that L-48 NAGLU affects the processing and stability of the gene; some L-48 NAGLU is being correctly sorted to the lysosomal compartment.|||In MPS3B; decreases the enzyme activity markedly.|||In MPS3B; does not yield active enzyme.|||In MPS3B; no enzyme activity.|||In MPS3B; no enzyme activity; synthesizes a polypeptide with a molecular size similar to that of the wild-type.|||In MPS3B; produces 12.7% residual enzyme activity.|||In MPS3B; unknown pathological significance.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020728|||http://purl.uniprot.org/annotation/PRO_0000020729|||http://purl.uniprot.org/annotation/PRO_5007491720|||http://purl.uniprot.org/annotation/VAR_005007|||http://purl.uniprot.org/annotation/VAR_005008|||http://purl.uniprot.org/annotation/VAR_005009|||http://purl.uniprot.org/annotation/VAR_005010|||http://purl.uniprot.org/annotation/VAR_005011|||http://purl.uniprot.org/annotation/VAR_005012|||http://purl.uniprot.org/annotation/VAR_005013|||http://purl.uniprot.org/annotation/VAR_005014|||http://purl.uniprot.org/annotation/VAR_005015|||http://purl.uniprot.org/annotation/VAR_008979|||http://purl.uniprot.org/annotation/VAR_008980|||http://purl.uniprot.org/annotation/VAR_008981|||http://purl.uniprot.org/annotation/VAR_008982|||http://purl.uniprot.org/annotation/VAR_008983|||http://purl.uniprot.org/annotation/VAR_008984|||http://purl.uniprot.org/annotation/VAR_008985|||http://purl.uniprot.org/annotation/VAR_008986|||http://purl.uniprot.org/annotation/VAR_008987|||http://purl.uniprot.org/annotation/VAR_008988|||http://purl.uniprot.org/annotation/VAR_008989|||http://purl.uniprot.org/annotation/VAR_008990|||http://purl.uniprot.org/annotation/VAR_008991|||http://purl.uniprot.org/annotation/VAR_025489|||http://purl.uniprot.org/annotation/VAR_025490|||http://purl.uniprot.org/annotation/VAR_025491|||http://purl.uniprot.org/annotation/VAR_025492|||http://purl.uniprot.org/annotation/VAR_025493|||http://purl.uniprot.org/annotation/VAR_025494|||http://purl.uniprot.org/annotation/VAR_054699|||http://purl.uniprot.org/annotation/VAR_054700|||http://purl.uniprot.org/annotation/VAR_054701|||http://purl.uniprot.org/annotation/VAR_054702|||http://purl.uniprot.org/annotation/VAR_054703|||http://purl.uniprot.org/annotation/VAR_054704|||http://purl.uniprot.org/annotation/VAR_054705|||http://purl.uniprot.org/annotation/VAR_054706|||http://purl.uniprot.org/annotation/VAR_054707|||http://purl.uniprot.org/annotation/VAR_054708|||http://purl.uniprot.org/annotation/VAR_054709|||http://purl.uniprot.org/annotation/VAR_054710|||http://purl.uniprot.org/annotation/VAR_054711|||http://purl.uniprot.org/annotation/VAR_054712|||http://purl.uniprot.org/annotation/VAR_054713|||http://purl.uniprot.org/annotation/VAR_054714|||http://purl.uniprot.org/annotation/VAR_054715|||http://purl.uniprot.org/annotation/VAR_054716|||http://purl.uniprot.org/annotation/VAR_054717|||http://purl.uniprot.org/annotation/VAR_054718|||http://purl.uniprot.org/annotation/VAR_054719|||http://purl.uniprot.org/annotation/VAR_054720|||http://purl.uniprot.org/annotation/VAR_054721|||http://purl.uniprot.org/annotation/VAR_054722|||http://purl.uniprot.org/annotation/VAR_054723|||http://purl.uniprot.org/annotation/VAR_054724|||http://purl.uniprot.org/annotation/VAR_054725|||http://purl.uniprot.org/annotation/VAR_054726|||http://purl.uniprot.org/annotation/VAR_054727|||http://purl.uniprot.org/annotation/VAR_054728|||http://purl.uniprot.org/annotation/VAR_054729|||http://purl.uniprot.org/annotation/VAR_054730|||http://purl.uniprot.org/annotation/VAR_054731|||http://purl.uniprot.org/annotation/VAR_054732|||http://purl.uniprot.org/annotation/VAR_054733|||http://purl.uniprot.org/annotation/VAR_054734|||http://purl.uniprot.org/annotation/VAR_054735|||http://purl.uniprot.org/annotation/VAR_054736|||http://purl.uniprot.org/annotation/VAR_054737|||http://purl.uniprot.org/annotation/VAR_054738|||http://purl.uniprot.org/annotation/VAR_054739|||http://purl.uniprot.org/annotation/VAR_074607|||http://purl.uniprot.org/annotation/VAR_079424|||http://purl.uniprot.org/annotation/VAR_079425
http://togogenome.org/gene/9606:DUSP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1R2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Dual specificity protein phosphatase 15|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of phosphatase activity.|||N-myristoyl glycine|||Phosphocysteine intermediate|||Removed|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094824|||http://purl.uniprot.org/annotation/VSP_007292|||http://purl.uniprot.org/annotation/VSP_007293|||http://purl.uniprot.org/annotation/VSP_019228|||http://purl.uniprot.org/annotation/VSP_043107
http://togogenome.org/gene/9606:PGAM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J4Y8|||http://purl.uniprot.org/uniprot/Q96HS1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by PARL.|||Cleavage; by PARL|||Disordered|||Helical|||In isoform 2.|||Interaction with KEAP1|||Loss of interaction with KEAP1; when associated with A-79.|||Loss of interaction with KEAP1; when associated with A-80.|||Loss of phosphatase activity.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine|||Phosphoserine|||Serine/threonine-protein phosphatase PGAM5, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288782|||http://purl.uniprot.org/annotation/VSP_025761
http://togogenome.org/gene/9606:MAPK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A286YF97|||http://purl.uniprot.org/uniprot/F8W9R5|||http://purl.uniprot.org/uniprot/P53779|||http://purl.uniprot.org/uniprot/Q499Y8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 3.|||In isoform Alpha-1.|||Loss of palmitoylation.|||Mitogen-activated protein kinase 10|||Phosphothreonine; by MAP2K7|||Phosphotyrosine; by MAP2K4|||Polar residues|||Protein kinase|||Proton acceptor|||S-palmitoyl cysteine|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186277|||http://purl.uniprot.org/annotation/VSP_004839|||http://purl.uniprot.org/annotation/VSP_041911
http://togogenome.org/gene/9606:TAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6K3|||http://purl.uniprot.org/uniprot/Q15750                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MAP3K7.|||About 50% loss of IL-6 secretion after IL-1alpha stimulation.|||Complete loss of ITCH-mediated ubiquitination.|||Disordered|||In isoform 2.|||Loss of interaction with XIAP.|||Loss of phosphorylation site.|||O-linked (GlcNAc) serine|||PPM-type phosphatase|||Phosphoserine|||Phosphoserine; by MAPK14|||Phosphothreonine|||Phosphothreonine; by MAPK14|||Polar residues|||Required for interaction with MAP3K7|||TGF-beta-activated kinase 1 and MAP3K7-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057797|||http://purl.uniprot.org/annotation/VAR_039271|||http://purl.uniprot.org/annotation/VSP_042024
http://togogenome.org/gene/9606:PATL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-595 and A-625.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-595 and A-626.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-591; A-625 and A-626.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-520; A-595; A-625 and A-626.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-519; A-591; A-595; A-625 and A-626.|||In mut1; Abolishes RNA-binding, localization to P-body and interaction with the decapping machinery; when associated with A-520; A-591; A-595; A-625 and A-626.|||In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with A-527; A-530 and S-534.|||In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-527 and A-530.|||In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-527 and S-534.|||In mut2; Abolishes interaction with the decapping machinery and localization to P-body; when associated with S-523; A-530 and S-534.|||In mut3; does not affect neither RNA-binding,interaction with the decapping machinery, nor localization to P-body.|||Involved in RNA-binding|||Involved in nuclear foci localization|||Involved in nuclear speckle localization|||Loss of nuclear export; when associated with A-86, A-90 and A-93.|||Loss of nuclear export; when associated with A-86, A-90 and A-95.|||Loss of nuclear export; when associated with A-86, A-93 and A-95.|||Loss of nuclear export; when associated with A-90, A-93 and A-95.|||Nuclear export signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein PAT1 homolog 1|||Region A; interaction with DDX6/RCK|||Region C|||Region H|||Region N; interaction with decapping machinery                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320963|||http://purl.uniprot.org/annotation/VSP_031777|||http://purl.uniprot.org/annotation/VSP_031778|||http://purl.uniprot.org/annotation/VSP_040576|||http://purl.uniprot.org/annotation/VSP_040577
http://togogenome.org/gene/9606:SF3B5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWJ5                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site|||Strand                                                                                  ^@                                                                                  Interaction with RNA|||Interaction with SF3B1 and SF3B3|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Removed|||Splicing factor 3B subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220757
http://togogenome.org/gene/9606:BHLHE41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAT1|||http://purl.uniprot.org/uniprot/Q9C0J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes RXRA repression.|||Associated with short sleep phenotype; abolishes inhibition of CLOCK-BMAL1 and NPAS2/BMAL1 transactivation activities.|||Associated with short sleep phenotype; heterogeneous phenotype; increases inhibition of CLOCK-BMAL1 and NPAS2/BMAL1 transactivation activities.|||BHLH|||Basic and acidic residues|||Class E basic helix-loop-helix protein 41|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Necessary for interaction with RXRA and repressor activity towards RXRA|||Orange|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127147|||http://purl.uniprot.org/annotation/VAR_063259|||http://purl.uniprot.org/annotation/VAR_082585|||http://purl.uniprot.org/annotation/VAR_082586
http://togogenome.org/gene/9606:TMEM184A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Transmembrane protein 184A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300466|||http://purl.uniprot.org/annotation/VAR_060120|||http://purl.uniprot.org/annotation/VAR_062157
http://togogenome.org/gene/9606:ABI3BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7G0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Found in a patient with isolated coloboma; unknown pathological significance.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Target of Nesh-SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022472|||http://purl.uniprot.org/annotation/VAR_079855|||http://purl.uniprot.org/annotation/VSP_010860|||http://purl.uniprot.org/annotation/VSP_010861|||http://purl.uniprot.org/annotation/VSP_061186|||http://purl.uniprot.org/annotation/VSP_061187
http://togogenome.org/gene/9606:NCKAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14513                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nck-associated protein 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096711|||http://purl.uniprot.org/annotation/VAR_051220|||http://purl.uniprot.org/annotation/VAR_051221|||http://purl.uniprot.org/annotation/VAR_051222|||http://purl.uniprot.org/annotation/VAR_051223|||http://purl.uniprot.org/annotation/VAR_051224|||http://purl.uniprot.org/annotation/VAR_051225|||http://purl.uniprot.org/annotation/VAR_061686|||http://purl.uniprot.org/annotation/VSP_021601|||http://purl.uniprot.org/annotation/VSP_021602|||http://purl.uniprot.org/annotation/VSP_021603|||http://purl.uniprot.org/annotation/VSP_021604|||http://purl.uniprot.org/annotation/VSP_021605|||http://purl.uniprot.org/annotation/VSP_021606
http://togogenome.org/gene/9606:C20orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R5K4|||http://purl.uniprot.org/uniprot/Q9NUB4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Uncharacterized protein C20orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079466
http://togogenome.org/gene/9606:GDAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB36                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Found in a patient with hereditary motor neuropathy; unknown pathological significance.|||GST C-terminal|||GST N-terminal|||Ganglioside-induced differentiation-associated protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical|||Impairment in the ability to induce mitochondrial fragmentation.|||In CMT2K; dominant form.|||In CMT2K; dominant form; no effect on mitochondrial localization.|||In CMT2K; dominant form; unknown pathological significance.|||In CMT2K; dominant form;.|||In CMT2K; recessive form.|||In CMT2K; recessive form; unknown pathological significance.|||In CMT2RV; Abolishes mitochondrial fission.|||In CMT4A; no effect on mitochondrial localization but abolishes mitochondrial fission.|||In CMT4A; no effect on mitochondrial localization but impairment in the ability to induce mitochondrial fragmentation.|||In CMTRIA; no effect on mitochondrial localization but impairment in the ability to induce mitochondrial fragmentation.|||In isoform 2.|||N6-acetyllysine; alternate|||No effect on mitochondrial localization.|||Required for mitochondrial localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186038|||http://purl.uniprot.org/annotation/VAR_017184|||http://purl.uniprot.org/annotation/VAR_017185|||http://purl.uniprot.org/annotation/VAR_017186|||http://purl.uniprot.org/annotation/VAR_017187|||http://purl.uniprot.org/annotation/VAR_067086|||http://purl.uniprot.org/annotation/VAR_067087|||http://purl.uniprot.org/annotation/VAR_073297|||http://purl.uniprot.org/annotation/VAR_078265|||http://purl.uniprot.org/annotation/VAR_078266|||http://purl.uniprot.org/annotation/VAR_078267|||http://purl.uniprot.org/annotation/VAR_078268|||http://purl.uniprot.org/annotation/VAR_078269|||http://purl.uniprot.org/annotation/VAR_078270|||http://purl.uniprot.org/annotation/VAR_078271|||http://purl.uniprot.org/annotation/VAR_078272|||http://purl.uniprot.org/annotation/VAR_078273|||http://purl.uniprot.org/annotation/VSP_038393
http://togogenome.org/gene/9606:PRR15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1A1|||http://purl.uniprot.org/uniprot/Q8IV56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pro residues|||Proline-rich protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271109|||http://purl.uniprot.org/annotation/VAR_059710
http://togogenome.org/gene/9606:PTPN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6H6|||http://purl.uniprot.org/uniprot/Q15678                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FERM|||In a breast cancer sample; somatic mutation.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219437|||http://purl.uniprot.org/annotation/VAR_035849|||http://purl.uniprot.org/annotation/VAR_035850|||http://purl.uniprot.org/annotation/VAR_046995
http://togogenome.org/gene/9606:TNFRSF10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00220                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect on palmitoylation.|||No effect on palmitoylation. Loss of palmitoylation, decreased association with membranes, decreased oligomerization, decreased death-induced signaling complex assembly associated with decreased function in TRAIL-induced cell death; when associated with S-261 and S-262.|||No effect on palmitoylation. Loss of palmitoylation, decreased association with membranes, decreased oligomerization, decreased death-induced signaling complex assembly associated with decreased function in TRAIL-induced cell death; when associated with S-261 and S-263.|||No effect on palmitoylation. Loss of palmitoylation, decreased association with membranes, decreased oligomerization, decreased death-induced signaling complex assembly associated with decreased function in TRAIL-induced cell death; when associated with S-262 and S-263.|||Omega-N-methylarginine|||Phosphoserine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 10A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034579|||http://purl.uniprot.org/annotation/VAR_016149|||http://purl.uniprot.org/annotation/VAR_016150|||http://purl.uniprot.org/annotation/VAR_016151|||http://purl.uniprot.org/annotation/VAR_016152|||http://purl.uniprot.org/annotation/VAR_052349|||http://purl.uniprot.org/annotation/VAR_052350|||http://purl.uniprot.org/annotation/VAR_052351|||http://purl.uniprot.org/annotation/VAR_052352
http://togogenome.org/gene/9606:ZNF318                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUA4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with AR|||Matrin-type 1|||Matrin-type 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Zinc finger protein 318                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191807|||http://purl.uniprot.org/annotation/VAR_036056|||http://purl.uniprot.org/annotation/VAR_036057|||http://purl.uniprot.org/annotation/VAR_053759|||http://purl.uniprot.org/annotation/VAR_053760|||http://purl.uniprot.org/annotation/VAR_053761|||http://purl.uniprot.org/annotation/VAR_053762|||http://purl.uniprot.org/annotation/VAR_053763|||http://purl.uniprot.org/annotation/VAR_053764|||http://purl.uniprot.org/annotation/VSP_016592|||http://purl.uniprot.org/annotation/VSP_016593
http://togogenome.org/gene/9606:UBXN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00124                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Phosphoserine|||Polar residues|||UBX|||UBX domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211033|||http://purl.uniprot.org/annotation/VAR_052687|||http://purl.uniprot.org/annotation/VAR_052688|||http://purl.uniprot.org/annotation/VSP_004376|||http://purl.uniprot.org/annotation/VSP_015535
http://togogenome.org/gene/9606:CELSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||(3R)-3-hydroxyaspartate|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cadherin EGF LAG seven-pass G-type receptor 1|||Cytoplasmic|||Disordered|||Does not affect protein localization to the cell membrane.|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In LMPHM9.|||In LMPHM9; unknown pathological significance.|||In NTD; shows reduced protein localization to the cell membrane.|||In NTD; shows significantly reduced protein localization to the cell membrane.|||In isoform 2.|||Laminin EGF-like|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012914|||http://purl.uniprot.org/annotation/VAR_016094|||http://purl.uniprot.org/annotation/VAR_016095|||http://purl.uniprot.org/annotation/VAR_024479|||http://purl.uniprot.org/annotation/VAR_024480|||http://purl.uniprot.org/annotation/VAR_049464|||http://purl.uniprot.org/annotation/VAR_049465|||http://purl.uniprot.org/annotation/VAR_049466|||http://purl.uniprot.org/annotation/VAR_049467|||http://purl.uniprot.org/annotation/VAR_049468|||http://purl.uniprot.org/annotation/VAR_049469|||http://purl.uniprot.org/annotation/VAR_049470|||http://purl.uniprot.org/annotation/VAR_049471|||http://purl.uniprot.org/annotation/VAR_049472|||http://purl.uniprot.org/annotation/VAR_049473|||http://purl.uniprot.org/annotation/VAR_067213|||http://purl.uniprot.org/annotation/VAR_067214|||http://purl.uniprot.org/annotation/VAR_067215|||http://purl.uniprot.org/annotation/VAR_067216|||http://purl.uniprot.org/annotation/VAR_067217|||http://purl.uniprot.org/annotation/VAR_067218|||http://purl.uniprot.org/annotation/VAR_085932|||http://purl.uniprot.org/annotation/VAR_085933|||http://purl.uniprot.org/annotation/VAR_085934|||http://purl.uniprot.org/annotation/VAR_085935|||http://purl.uniprot.org/annotation/VAR_085936|||http://purl.uniprot.org/annotation/VAR_085937|||http://purl.uniprot.org/annotation/VAR_085938|||http://purl.uniprot.org/annotation/VAR_085939|||http://purl.uniprot.org/annotation/VAR_085940|||http://purl.uniprot.org/annotation/VSP_002011|||http://purl.uniprot.org/annotation/VSP_002012
http://togogenome.org/gene/9606:MSANTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1M0|||http://purl.uniprot.org/uniprot/Q6P1R3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Myb-like|||Myb/SANT-like DNA-binding|||Myb/SANT-like DNA-binding domain-containing protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274301|||http://purl.uniprot.org/annotation/VSP_022705|||http://purl.uniprot.org/annotation/VSP_022706
http://togogenome.org/gene/9606:NBPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H094                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Neuroblastoma breakpoint family member 3|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288038|||http://purl.uniprot.org/annotation/VAR_032374|||http://purl.uniprot.org/annotation/VAR_032375|||http://purl.uniprot.org/annotation/VAR_047965|||http://purl.uniprot.org/annotation/VAR_053909|||http://purl.uniprot.org/annotation/VSP_025625|||http://purl.uniprot.org/annotation/VSP_025626|||http://purl.uniprot.org/annotation/VSP_025627|||http://purl.uniprot.org/annotation/VSP_025628|||http://purl.uniprot.org/annotation/VSP_044705
http://togogenome.org/gene/9606:HEXIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MH2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Interaction with CCNT1, HEXIM1 and HEXIM2|||Interaction with P-TEFb|||Loss of interaction with P-TEFb.|||Phosphoserine|||Phosphothreonine|||Protein HEXIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305267
http://togogenome.org/gene/9606:GREM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H772                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CTCK|||Gremlin-2|||In STHAG9.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006720|||http://purl.uniprot.org/annotation/VAR_048876|||http://purl.uniprot.org/annotation/VAR_078067|||http://purl.uniprot.org/annotation/VAR_078068|||http://purl.uniprot.org/annotation/VAR_078069
http://togogenome.org/gene/9606:TNP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09430|||http://purl.uniprot.org/uniprot/Q4ZG82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Spermatid nuclear transition protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191417
http://togogenome.org/gene/9606:SLC30A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAD4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||His-rich loop; required for zinc transport|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Loss of zinc transporter activity.|||Loss of zinc transporter activity. No effect on localization to the trans-Golgi network.|||Lumenal|||Mediates homodimerization with SLC30A6|||N-acetylmethionine|||No effect on zinc ion transmembrane transporter activity. No effect on zinc ion import into Golgi. Loss of specificity for zinc ions as it can also transport cadmium ions.|||No effect on zinc transporter activity. No effect on localization to the trans-Golgi network.|||Proton-coupled zinc antiporter SLC30A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314293|||http://purl.uniprot.org/annotation/VSP_030254|||http://purl.uniprot.org/annotation/VSP_030255|||http://purl.uniprot.org/annotation/VSP_030256|||http://purl.uniprot.org/annotation/VSP_043673|||http://purl.uniprot.org/annotation/VSP_043674|||http://purl.uniprot.org/annotation/VSP_045115
http://togogenome.org/gene/9606:PLEKHG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0TW08|||http://purl.uniprot.org/uniprot/Q3KR16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of exchange activity.|||PH|||Pleckstrin homology domain-containing family G member 6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307912|||http://purl.uniprot.org/annotation/VAR_036710|||http://purl.uniprot.org/annotation/VSP_028856|||http://purl.uniprot.org/annotation/VSP_028857|||http://purl.uniprot.org/annotation/VSP_028858
http://togogenome.org/gene/9606:ABHD17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GS6                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Alpha/beta hydrolase domain-containing protein 17A|||Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity. No effect on its localization. No effect on NRAS plasma membrane localization.|||Phosphoserine|||Reduces catalytic activity. Loss of membrane localization. No effect on NRAS plasma membrane localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297509|||http://purl.uniprot.org/annotation/VSP_027268|||http://purl.uniprot.org/annotation/VSP_027269|||http://purl.uniprot.org/annotation/VSP_027270|||http://purl.uniprot.org/annotation/VSP_027271
http://togogenome.org/gene/9606:DHX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43143                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX15|||Abolished ATPase activity without affecting ability to activate the MAVS-dependent signaling to produce interferon-beta.|||Abolished ATPase activity.|||Abolished interaction with NKRF.|||Basic and acidic residues|||DEAH box|||Decreased, but not abolished interaction, with NKRF.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055139
http://togogenome.org/gene/9606:ELAVL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0R4J2E6|||http://purl.uniprot.org/uniprot/A0A494C0M6|||http://purl.uniprot.org/uniprot/A0A494C147|||http://purl.uniprot.org/uniprot/B1APY9|||http://purl.uniprot.org/uniprot/P26378                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by CARM1; alternate|||Disordered|||ELAV-like protein 4|||In isoform 1 and isoform 2.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Omega-N-methylarginine; by CARM1; alternate|||Phosphoserine|||Polar residues|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081583|||http://purl.uniprot.org/annotation/VAR_052204|||http://purl.uniprot.org/annotation/VAR_058091|||http://purl.uniprot.org/annotation/VAR_058092|||http://purl.uniprot.org/annotation/VSP_060279|||http://purl.uniprot.org/annotation/VSP_060280|||http://purl.uniprot.org/annotation/VSP_060281|||http://purl.uniprot.org/annotation/VSP_060282|||http://purl.uniprot.org/annotation/VSP_060283
http://togogenome.org/gene/9606:SLCO6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU7|||http://purl.uniprot.org/uniprot/C9J020|||http://purl.uniprot.org/uniprot/Q86UG4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2 and isoform 3.|||In isoform 3.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307642|||http://purl.uniprot.org/annotation/VAR_036622|||http://purl.uniprot.org/annotation/VAR_036623|||http://purl.uniprot.org/annotation/VAR_036624|||http://purl.uniprot.org/annotation/VAR_053680|||http://purl.uniprot.org/annotation/VSP_028753|||http://purl.uniprot.org/annotation/VSP_028754
http://togogenome.org/gene/9606:NDNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB73                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Fibronectin type-III 1|||Fibronectin type-III 2|||In HH25; loss of protein expression.|||In HH25; no effect on protein abundance; decreased secretion; loss of function in cellular response to fibroblast growth factor stimulus.|||In HH25; no effect on protein abundance; no effect on function in cellular response to fibroblast growth factor stimulus.|||N-linked (GlcNAc...) asparagine|||Protein NDNF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301965|||http://purl.uniprot.org/annotation/VAR_084037|||http://purl.uniprot.org/annotation/VAR_084038|||http://purl.uniprot.org/annotation/VAR_084039
http://togogenome.org/gene/9606:ENPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22413                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AMP-threonine intermediate|||Associated with T2D; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane.|||Cleavage|||Cytoplasmic|||Decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane.|||Di-leucine motif|||Disordered|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 1|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form|||Essential for catalytic activity|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In ARHR2 and GACI1.|||In ARHR2.|||In ARHR2; loss of activity.|||In ARHR2; unknown pathological significance.|||In COLED.|||In COLED; impaired homodimerization.|||In GACI1.|||In GACI1; decreased nucleotide phosphodiesterase activity; no effect on localization to plasma membrane.|||In GACI1; loss of nucleotide phosphodiesterase activity; loss of localization to plasma membrane.|||In GACI1; loss of nucleotide phosphodiesterase activity; no effect on localization to plasma membrane.|||In GACI1; unknown pathological significance.|||In OPLL.|||Linker|||N-linked (GlcNAc...) asparagine|||No effect on nucleotide phosphodiesterase activity; no effect on localization to plasma membrane.|||Nuclease|||Phosphodiesterase|||Phosphothreonine|||SMB 1|||SMB 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188564|||http://purl.uniprot.org/annotation/PRO_0000447133|||http://purl.uniprot.org/annotation/VAR_008873|||http://purl.uniprot.org/annotation/VAR_014141|||http://purl.uniprot.org/annotation/VAR_014142|||http://purl.uniprot.org/annotation/VAR_014143|||http://purl.uniprot.org/annotation/VAR_014144|||http://purl.uniprot.org/annotation/VAR_018514|||http://purl.uniprot.org/annotation/VAR_018515|||http://purl.uniprot.org/annotation/VAR_037432|||http://purl.uniprot.org/annotation/VAR_037433|||http://purl.uniprot.org/annotation/VAR_037434|||http://purl.uniprot.org/annotation/VAR_037435|||http://purl.uniprot.org/annotation/VAR_063719|||http://purl.uniprot.org/annotation/VAR_063720|||http://purl.uniprot.org/annotation/VAR_067910|||http://purl.uniprot.org/annotation/VAR_067911|||http://purl.uniprot.org/annotation/VAR_067912|||http://purl.uniprot.org/annotation/VAR_067913|||http://purl.uniprot.org/annotation/VAR_067914|||http://purl.uniprot.org/annotation/VAR_070782|||http://purl.uniprot.org/annotation/VAR_070783|||http://purl.uniprot.org/annotation/VAR_070784|||http://purl.uniprot.org/annotation/VAR_077255|||http://purl.uniprot.org/annotation/VAR_077256|||http://purl.uniprot.org/annotation/VAR_077257|||http://purl.uniprot.org/annotation/VAR_077258|||http://purl.uniprot.org/annotation/VAR_077259|||http://purl.uniprot.org/annotation/VAR_077260|||http://purl.uniprot.org/annotation/VAR_077261|||http://purl.uniprot.org/annotation/VAR_077262|||http://purl.uniprot.org/annotation/VAR_077263|||http://purl.uniprot.org/annotation/VAR_077264|||http://purl.uniprot.org/annotation/VAR_077265|||http://purl.uniprot.org/annotation/VAR_077266|||http://purl.uniprot.org/annotation/VAR_077267|||http://purl.uniprot.org/annotation/VAR_077268|||http://purl.uniprot.org/annotation/VAR_077269|||http://purl.uniprot.org/annotation/VAR_077270|||http://purl.uniprot.org/annotation/VAR_077271|||http://purl.uniprot.org/annotation/VAR_077272|||http://purl.uniprot.org/annotation/VAR_077273|||http://purl.uniprot.org/annotation/VAR_077274|||http://purl.uniprot.org/annotation/VAR_077275|||http://purl.uniprot.org/annotation/VAR_077276|||http://purl.uniprot.org/annotation/VAR_077277|||http://purl.uniprot.org/annotation/VAR_077278|||http://purl.uniprot.org/annotation/VAR_077279|||http://purl.uniprot.org/annotation/VAR_077280|||http://purl.uniprot.org/annotation/VAR_077281|||http://purl.uniprot.org/annotation/VAR_077282|||http://purl.uniprot.org/annotation/VAR_077283|||http://purl.uniprot.org/annotation/VAR_081644
http://togogenome.org/gene/9606:C22orf23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZE7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  UPF0193 protein EVG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221089|||http://purl.uniprot.org/annotation/VAR_057346
http://togogenome.org/gene/9606:STIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31948|||http://purl.uniprot.org/uniprot/V9HW72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||STI1|||STI1 1|||STI1 2|||Stress-induced-phosphoprotein 1|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106372|||http://purl.uniprot.org/annotation/VSP_055034|||http://purl.uniprot.org/annotation/VSP_055035
http://togogenome.org/gene/9606:PTX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A99                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Pentraxin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320645|||http://purl.uniprot.org/annotation/VAR_039249|||http://purl.uniprot.org/annotation/VAR_039250|||http://purl.uniprot.org/annotation/VAR_039251|||http://purl.uniprot.org/annotation/VAR_039252|||http://purl.uniprot.org/annotation/VAR_039253|||http://purl.uniprot.org/annotation/VAR_060084|||http://purl.uniprot.org/annotation/VAR_062130|||http://purl.uniprot.org/annotation/VSP_040203
http://togogenome.org/gene/9606:ARHGAP35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Enhances Rac GAP activity.|||FF 1|||FF 2|||FF 3|||FF 4|||Has GTPase activity, required for proper localization|||No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1221. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1236.|||No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1226. Abolishes phosphorylation by PRKCA; when associated with A-1126 and A-1236.|||No effect on total phosphorylation levels. No effect on inhibition of phospholipid binding by PRKCA phosphorylation. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1226.|||Phosphoserine|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine|||Phosphothreonine; by PKC/PRKCA|||Phosphotyrosine|||Phosphotyrosine; by ABL2 and PTK6|||Polar residues|||Pro residues|||Required for phospholipid binding and regulation of the substrate preference|||Rho GTPase-activating protein 35|||Rho-GAP|||pG1 pseudoGTPase|||pG2 pseudoGTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056730
http://togogenome.org/gene/9606:KCNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92953                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FFAT|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Potassium voltage-gated channel subfamily B member 2|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054048|||http://purl.uniprot.org/annotation/VAR_034050|||http://purl.uniprot.org/annotation/VAR_035774
http://togogenome.org/gene/9606:ETV5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41161                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Mass|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ETS|||ETS translocation variant 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204118|||http://purl.uniprot.org/annotation/VAR_048951|||http://purl.uniprot.org/annotation/VSP_055489
http://togogenome.org/gene/9606:ZP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05996                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage|||Cleavage; by ASTL|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Processed zona pellucida sperm-binding protein 2|||Removed in mature form|||ZP|||Zona pellucida sperm-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041689|||http://purl.uniprot.org/annotation/PRO_0000041690|||http://purl.uniprot.org/annotation/PRO_0000304559|||http://purl.uniprot.org/annotation/VAR_024705|||http://purl.uniprot.org/annotation/VSP_054508
http://togogenome.org/gene/9606:LRRC38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT99                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Repeat|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312418|||http://purl.uniprot.org/annotation/VAR_037504|||http://purl.uniprot.org/annotation/VAR_037505
http://togogenome.org/gene/9606:FTCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95954                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclodeaminase/cyclohydrolase|||For cyclodeaminase activity|||For formimidoyltransferase activity|||Formimidoyltransferase-cyclodeaminase|||Formiminotransferase C-subdomain|||Formiminotransferase N-subdomain|||In FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 57% wild-type activity.|||In FIGLU-URIA; mild phenotype; decreased glutamate formimidoyltransferase activity; 61% of wild-type activity.|||In isoform C.|||In isoform D.|||In isoform E.|||Linker|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087359|||http://purl.uniprot.org/annotation/VAR_015887|||http://purl.uniprot.org/annotation/VAR_015888|||http://purl.uniprot.org/annotation/VAR_015889|||http://purl.uniprot.org/annotation/VSP_004257|||http://purl.uniprot.org/annotation/VSP_004258|||http://purl.uniprot.org/annotation/VSP_004259|||http://purl.uniprot.org/annotation/VSP_004260
http://togogenome.org/gene/9606:PYM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRP8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Partner of Y14 and mago|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with MAGOH and RBM8A|||eIF2A-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287285|||http://purl.uniprot.org/annotation/VAR_032297|||http://purl.uniprot.org/annotation/VSP_025430
http://togogenome.org/gene/9606:TRIB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92519                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein kinase|||Tribbles homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131863|||http://purl.uniprot.org/annotation/VAR_042371
http://togogenome.org/gene/9606:NHLRC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG21                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  NHL 1|||NHL 2|||NHL-repeat-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395106
http://togogenome.org/gene/9606:KCND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0V9|||http://purl.uniprot.org/uniprot/Q9NZV8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with FLNC.|||BTB|||Causes a positive shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel.|||Cytoplasmic|||Decreases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Important for normal channel activation and inactivation, for interaction with KCNIP2, and probably other family members as well|||Increases pak current amplitude and causes a positive shift in the voltage-dependence of activation and steady-state inactivation. May increase the affinity for the closed-inactivated state of the channel.|||Increases peak current amplitude and causes a negative shift in the voltage-dependence of activation.|||Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation.|||Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.|||Increases peak current amplitude and slows the onset of inactivation at low voltage, but has no effect on the voltage-dependence of activation.|||Increases peak current amplitude but has a minor effect on the voltage-dependence of activation.|||Increases peak current amplitude but has no effect on the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.|||Interaction with KCNIP1|||Interaction with KCNIP1, KCNIP2, and other family members|||Loss of channel activity.|||May impair protein folding.|||No effect on peak current amplitude, but causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Potassium voltage-gated channel subfamily D member 2|||Probable disease-associated variant found in a family with atypical autism and severe epilepsy; disrupts potassium current inactivation.|||Required for dendritic targeting|||S4-S5 linker|||Selectivity filter|||Slightly increases peak current amplitude and causes a negative shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054064|||http://purl.uniprot.org/annotation/PRO_5014296867|||http://purl.uniprot.org/annotation/VAR_072076
http://togogenome.org/gene/9606:MAB21L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8X9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Protein mab-21-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286584
http://togogenome.org/gene/9606:CLDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57739                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-2|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||In OAZON; unknown pathological significance.|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144734|||http://purl.uniprot.org/annotation/VAR_085653
http://togogenome.org/gene/9606:TP53I11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14683|||http://purl.uniprot.org/uniprot/Q8N8U5|||http://purl.uniprot.org/uniprot/U3KQ32                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Tumor protein p53-inducible protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058142
http://togogenome.org/gene/9606:RAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBE9|||http://purl.uniprot.org/uniprot/B3KPD7|||http://purl.uniprot.org/uniprot/Q9Y5P3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Retinoic acid-induced protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097161|||http://purl.uniprot.org/annotation/VAR_046100|||http://purl.uniprot.org/annotation/VAR_046101|||http://purl.uniprot.org/annotation/VSP_047524
http://togogenome.org/gene/9606:RRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXD1|||http://purl.uniprot.org/uniprot/B4E0I8|||http://purl.uniprot.org/uniprot/E9PL69|||http://purl.uniprot.org/uniprot/P23921                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  ATP-cone|||Cysteine radical intermediate|||Important for electron transfer|||Important for hydrogen atom transfer|||Interacts with thioredoxin/glutaredoxin|||N6-acetyllysine|||Phosphothreonine|||Proton acceptor|||Redox-active|||Ribonucleoside-diphosphate reductase large subunit|||Ribonucleotide reductase large subunit|||Severely decreases interaction with AHCYL1 in the presence of dATP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187190|||http://purl.uniprot.org/annotation/VAR_052052|||http://purl.uniprot.org/annotation/VAR_052053
http://togogenome.org/gene/9606:AFAP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TED9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Actin filament-associated protein 1-like 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH 1|||PH 2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295239|||http://purl.uniprot.org/annotation/VSP_026856|||http://purl.uniprot.org/annotation/VSP_026857|||http://purl.uniprot.org/annotation/VSP_026858|||http://purl.uniprot.org/annotation/VSP_026859
http://togogenome.org/gene/9606:OR5F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95221                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150595|||http://purl.uniprot.org/annotation/VAR_034225|||http://purl.uniprot.org/annotation/VAR_053194|||http://purl.uniprot.org/annotation/VAR_062043
http://togogenome.org/gene/9606:XRCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43542|||http://purl.uniprot.org/uniprot/Q53XC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  DNA repair protein XRCC3|||In CMM6; risk factor for disease development.|||N-acetylmethionine|||RecA family profile 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122951|||http://purl.uniprot.org/annotation/VAR_013006|||http://purl.uniprot.org/annotation/VAR_020405|||http://purl.uniprot.org/annotation/VAR_029295|||http://purl.uniprot.org/annotation/VAR_029296
http://togogenome.org/gene/9606:PCDHA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003900|||http://purl.uniprot.org/annotation/VAR_048530|||http://purl.uniprot.org/annotation/VAR_048531|||http://purl.uniprot.org/annotation/VAR_048532|||http://purl.uniprot.org/annotation/VAR_048533|||http://purl.uniprot.org/annotation/VAR_048534|||http://purl.uniprot.org/annotation/VAR_059182|||http://purl.uniprot.org/annotation/VAR_061062|||http://purl.uniprot.org/annotation/VAR_061063|||http://purl.uniprot.org/annotation/VSP_000688|||http://purl.uniprot.org/annotation/VSP_000689
http://togogenome.org/gene/9606:COA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2R0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytochrome c oxidase assembly factor 3 homolog, mitochondrial|||Disordered|||Helical|||In MC4DN14; unknown pathological significance.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239438|||http://purl.uniprot.org/annotation/VAR_084180
http://togogenome.org/gene/9606:APH1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUG7|||http://purl.uniprot.org/uniprot/Q96BI3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Gamma-secretase subunit APH-1A|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impaired gamma-secretease assembly and reduced proteolytic activity of the gamma-secretase complex.|||In isoform 2.|||In isoform 3.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221050|||http://purl.uniprot.org/annotation/VSP_008355|||http://purl.uniprot.org/annotation/VSP_008356|||http://purl.uniprot.org/annotation/VSP_045424
http://togogenome.org/gene/9606:DCHS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MVP2; loss-of-function mutation; results in reduced protein levels; results in increased protein degradation.|||In MVP2; unknown pathological significance; has no significant effect on protein levels.|||In MVP2; unknown pathological significance; loss-of-function mutation; results in reduced protein levels; results in increased protein degradation.|||In VMLDS1.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004000|||http://purl.uniprot.org/annotation/VAR_036110|||http://purl.uniprot.org/annotation/VAR_048577|||http://purl.uniprot.org/annotation/VAR_048578|||http://purl.uniprot.org/annotation/VAR_048579|||http://purl.uniprot.org/annotation/VAR_061074|||http://purl.uniprot.org/annotation/VAR_070928|||http://purl.uniprot.org/annotation/VAR_075048|||http://purl.uniprot.org/annotation/VAR_075049|||http://purl.uniprot.org/annotation/VAR_075050
http://togogenome.org/gene/9606:ATP5MGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4Y8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative ATP synthase subunit g 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225013
http://togogenome.org/gene/9606:KPTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y664                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In MRT41; loss of localization to F-actin-rich regions; cytoplasmic accumulation at irregular perinuclear sites.|||In isoform 2.|||KICSTOR complex protein kaptin|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239234|||http://purl.uniprot.org/annotation/VAR_070974|||http://purl.uniprot.org/annotation/VSP_053990
http://togogenome.org/gene/9606:PCDHGB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003976|||http://purl.uniprot.org/annotation/VAR_048569|||http://purl.uniprot.org/annotation/VAR_048570|||http://purl.uniprot.org/annotation/VAR_061073|||http://purl.uniprot.org/annotation/VSP_008688|||http://purl.uniprot.org/annotation/VSP_008689
http://togogenome.org/gene/9606:PAX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23760                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form PAX3-NCOA1 oncogene|||Disordered|||Homeobox|||In CDHS.|||In WS1 and WS3.|||In WS1.|||In WS1; associated with H-271 in one family; unknown pathological significance.|||In WS1; associated with K-273 in one family.|||In WS1; associated with meningomyelocele.|||In WS1; important hearing loss.|||In WS1; originally classified as Waardenburg syndrome type 2.|||In WS1; results in decreased transcriptional activation of MITF; no effect on localization to nucleus; no effect on interaction with SOX10.|||In WS3.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform Pax3A.|||In isoform Pax3B.|||In isoform Pax3E.|||In isoform Pax3G.|||In isoform Pax3H.|||PAI subdomain|||Paired|||Paired box protein Pax-3|||Phosphoserine|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050178|||http://purl.uniprot.org/annotation/VAR_003790|||http://purl.uniprot.org/annotation/VAR_003791|||http://purl.uniprot.org/annotation/VAR_003792|||http://purl.uniprot.org/annotation/VAR_003793|||http://purl.uniprot.org/annotation/VAR_003794|||http://purl.uniprot.org/annotation/VAR_003795|||http://purl.uniprot.org/annotation/VAR_003796|||http://purl.uniprot.org/annotation/VAR_003797|||http://purl.uniprot.org/annotation/VAR_003798|||http://purl.uniprot.org/annotation/VAR_003799|||http://purl.uniprot.org/annotation/VAR_003800|||http://purl.uniprot.org/annotation/VAR_003801|||http://purl.uniprot.org/annotation/VAR_003802|||http://purl.uniprot.org/annotation/VAR_003803|||http://purl.uniprot.org/annotation/VAR_003804|||http://purl.uniprot.org/annotation/VAR_003805|||http://purl.uniprot.org/annotation/VAR_003806|||http://purl.uniprot.org/annotation/VAR_003807|||http://purl.uniprot.org/annotation/VAR_013619|||http://purl.uniprot.org/annotation/VAR_013640|||http://purl.uniprot.org/annotation/VAR_013641|||http://purl.uniprot.org/annotation/VAR_017533|||http://purl.uniprot.org/annotation/VAR_017534|||http://purl.uniprot.org/annotation/VAR_017535|||http://purl.uniprot.org/annotation/VAR_017536|||http://purl.uniprot.org/annotation/VAR_017537|||http://purl.uniprot.org/annotation/VAR_017538|||http://purl.uniprot.org/annotation/VAR_017539|||http://purl.uniprot.org/annotation/VAR_079619|||http://purl.uniprot.org/annotation/VAR_079620|||http://purl.uniprot.org/annotation/VAR_079621|||http://purl.uniprot.org/annotation/VSP_002355|||http://purl.uniprot.org/annotation/VSP_002356|||http://purl.uniprot.org/annotation/VSP_002357|||http://purl.uniprot.org/annotation/VSP_002358|||http://purl.uniprot.org/annotation/VSP_042004|||http://purl.uniprot.org/annotation/VSP_042005|||http://purl.uniprot.org/annotation/VSP_043634|||http://purl.uniprot.org/annotation/VSP_043635|||http://purl.uniprot.org/annotation/VSP_044915
http://togogenome.org/gene/9606:NAALAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNJ3|||http://purl.uniprot.org/uniprot/Q9Y3Q0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-acetylated-alpha-linked acidic dipeptidase 2|||N-linked (GlcNAc...) asparagine|||NAALADase|||Nucleophile; for NAALADase activity|||PA|||Peptidase M28|||Transferrin receptor-like dimerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174121|||http://purl.uniprot.org/annotation/VAR_034120|||http://purl.uniprot.org/annotation/VAR_034121|||http://purl.uniprot.org/annotation/VSP_054147|||http://purl.uniprot.org/annotation/VSP_054148
http://togogenome.org/gene/9606:HSPBAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K045|||http://purl.uniprot.org/uniprot/Q96EW2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HSPB1-associated protein 1|||In isoform 2.|||In isoform 3.|||Interaction with HSPB1|||JmjC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284113|||http://purl.uniprot.org/annotation/VAR_031703|||http://purl.uniprot.org/annotation/VSP_024442|||http://purl.uniprot.org/annotation/VSP_024443|||http://purl.uniprot.org/annotation/VSP_024444|||http://purl.uniprot.org/annotation/VSP_024445
http://togogenome.org/gene/9606:ZFP69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AA0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||SCAN box|||Zinc finger protein 69 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252161|||http://purl.uniprot.org/annotation/VAR_033583
http://togogenome.org/gene/9606:ATRNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0Y2|||http://purl.uniprot.org/uniprot/Q5VV63                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Attractin-like protein 1|||C-type lectin|||CUB|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||Extracellular|||Helical|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Laminin EGF-like 1|||Laminin EGF-like 2|||N-linked (GlcNAc...) asparagine|||PSI 1|||PSI 2|||PSI 3|||PSI 4|||PSI 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334650|||http://purl.uniprot.org/annotation/VAR_043446|||http://purl.uniprot.org/annotation/VSP_033718|||http://purl.uniprot.org/annotation/VSP_033719
http://togogenome.org/gene/9606:SMIM29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T20                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Small integral membrane protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019539|||http://purl.uniprot.org/annotation/VSP_059576
http://togogenome.org/gene/9606:TENT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RAF2|||http://purl.uniprot.org/uniprot/Q6PIY7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytically inactive.|||Disordered|||In isoform 2.|||Nuclear localization signal|||PAP-associated|||Phosphoserine|||Poly(A) RNA polymerase GLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341549|||http://purl.uniprot.org/annotation/VSP_034324
http://togogenome.org/gene/9606:TAS2R5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1U0|||http://purl.uniprot.org/uniprot/Q502V5|||http://purl.uniprot.org/uniprot/Q9NYW4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082212|||http://purl.uniprot.org/annotation/VAR_020203|||http://purl.uniprot.org/annotation/VAR_024184|||http://purl.uniprot.org/annotation/VAR_034537|||http://purl.uniprot.org/annotation/VAR_034538|||http://purl.uniprot.org/annotation/VAR_053343|||http://purl.uniprot.org/annotation/VAR_053344
http://togogenome.org/gene/9606:CT47A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:CNTNAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7T7|||http://purl.uniprot.org/uniprot/B2RCH4|||http://purl.uniprot.org/uniprot/Q9UHC6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein-like 2|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||In isoform 2.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||May be a risk factor for autism.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019506|||http://purl.uniprot.org/annotation/PRO_5002779571|||http://purl.uniprot.org/annotation/PRO_5014219317|||http://purl.uniprot.org/annotation/VAR_046227|||http://purl.uniprot.org/annotation/VAR_046228|||http://purl.uniprot.org/annotation/VAR_046229|||http://purl.uniprot.org/annotation/VAR_046230|||http://purl.uniprot.org/annotation/VAR_046231|||http://purl.uniprot.org/annotation/VAR_046232|||http://purl.uniprot.org/annotation/VAR_046233|||http://purl.uniprot.org/annotation/VAR_046234|||http://purl.uniprot.org/annotation/VAR_046235|||http://purl.uniprot.org/annotation/VAR_046236|||http://purl.uniprot.org/annotation/VAR_046237|||http://purl.uniprot.org/annotation/VAR_046238|||http://purl.uniprot.org/annotation/VAR_046239|||http://purl.uniprot.org/annotation/VAR_046240|||http://purl.uniprot.org/annotation/VAR_046241|||http://purl.uniprot.org/annotation/VAR_046242|||http://purl.uniprot.org/annotation/VAR_046243|||http://purl.uniprot.org/annotation/VAR_046244|||http://purl.uniprot.org/annotation/VAR_046245|||http://purl.uniprot.org/annotation/VAR_046246|||http://purl.uniprot.org/annotation/VAR_046247|||http://purl.uniprot.org/annotation/VAR_046248|||http://purl.uniprot.org/annotation/VSP_014976
http://togogenome.org/gene/9606:FAM110B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRT5|||http://purl.uniprot.org/uniprot/Q8TC76                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Centrosome-associated FAM110 C-terminal|||Centrosome-associated FAM110 N-terminal|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Protein FAM110B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285651|||http://purl.uniprot.org/annotation/VAR_036319
http://togogenome.org/gene/9606:CAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5Q0|||http://purl.uniprot.org/uniprot/P04040                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolished localization to peroxisomes.|||Catalase|||Catalase core|||Does not affect localization to peroxisomes.|||Microbody targeting signal; atypical|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084901
http://togogenome.org/gene/9606:SLC51A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UW1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In PFIC6; loss of expression in the colon of an homozygous patient.|||Organic solute transporter subunit alpha|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331543|||http://purl.uniprot.org/annotation/VAR_042895|||http://purl.uniprot.org/annotation/VAR_086189
http://togogenome.org/gene/9606:GOSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PCW1|||http://purl.uniprot.org/uniprot/O95249                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Golgi SNAP receptor complex member 1|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212542|||http://purl.uniprot.org/annotation/VSP_047326
http://togogenome.org/gene/9606:SDCCAG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SQ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates interaction with OFD1|||Phosphoserine|||Serologically defined colon cancer antigen 8|||Sufficient for homodimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076310|||http://purl.uniprot.org/annotation/VAR_051333|||http://purl.uniprot.org/annotation/VSP_016949|||http://purl.uniprot.org/annotation/VSP_016950|||http://purl.uniprot.org/annotation/VSP_016951|||http://purl.uniprot.org/annotation/VSP_016952|||http://purl.uniprot.org/annotation/VSP_016953
http://togogenome.org/gene/9606:CC2D1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0F9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2|||Coiled-coil and C2 domain-containing protein 1B|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288426|||http://purl.uniprot.org/annotation/VAR_062191|||http://purl.uniprot.org/annotation/VSP_025657|||http://purl.uniprot.org/annotation/VSP_025658|||http://purl.uniprot.org/annotation/VSP_025659|||http://purl.uniprot.org/annotation/VSP_025660|||http://purl.uniprot.org/annotation/VSP_025661|||http://purl.uniprot.org/annotation/VSP_025662|||http://purl.uniprot.org/annotation/VSP_025663
http://togogenome.org/gene/9606:NBPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3BBV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Neuroblastoma breakpoint family member 1|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5|||Olduvai 6|||Olduvai 7|||Olduvai 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288037|||http://purl.uniprot.org/annotation/VAR_032364|||http://purl.uniprot.org/annotation/VAR_032365|||http://purl.uniprot.org/annotation/VAR_032366|||http://purl.uniprot.org/annotation/VAR_032367|||http://purl.uniprot.org/annotation/VAR_032368|||http://purl.uniprot.org/annotation/VAR_032369|||http://purl.uniprot.org/annotation/VAR_032370|||http://purl.uniprot.org/annotation/VAR_032371|||http://purl.uniprot.org/annotation/VAR_032372|||http://purl.uniprot.org/annotation/VAR_032373|||http://purl.uniprot.org/annotation/VSP_059360
http://togogenome.org/gene/9606:SSH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYL5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abrogates phosphatase activity.|||Basic and acidic residues|||DEK-C|||Disordered|||Impairs stimulation of phosphatase activity by actin but does not affect basal activity.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with YWHAG|||N-acetylalanine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein phosphatase Slingshot homolog 1|||Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-937.|||Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-978.|||Removed|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094841|||http://purl.uniprot.org/annotation/VSP_016311|||http://purl.uniprot.org/annotation/VSP_016312|||http://purl.uniprot.org/annotation/VSP_016313|||http://purl.uniprot.org/annotation/VSP_016314|||http://purl.uniprot.org/annotation/VSP_016315|||http://purl.uniprot.org/annotation/VSP_016316|||http://purl.uniprot.org/annotation/VSP_016317|||http://purl.uniprot.org/annotation/VSP_016318|||http://purl.uniprot.org/annotation/VSP_016319
http://togogenome.org/gene/9606:PTEN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6KD01|||http://purl.uniprot.org/uniprot/P60484                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  60% reduction in phosphatase activity towards PtdIns(3,4,5)P3.|||700-fold reduction in phosphatase activity towards PtdIns(3,4,5)P3. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation.|||75% reduction in phosphatase activity towards PtdIns(3,4,5)P3.|||75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Modest reduction in phosphatase activity towards PtdIns(3,4)P2.|||85% reduction in phosphatase activity towards PtdIns(3,4,5)P3.|||Basic and acidic residues|||C2 tensin-type|||Constitutive interaction with DLC1 and interaction with p85 following EGF stimulation.|||Constitutive interaction with DLC1.|||Cytoplasmic; when associated with E-13. Shows less tumor suppressive ability; when associated with E-13.|||Decreased stability.|||Disordered|||Does not affect the ability to inhibit AKT/PKB activation.|||Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2.|||Does not reduce phosphatase activity towards PtdIns(3,4,5)P3.|||Expression is restricted to isoform alpha.|||Foun in a patient with macrocephaly, ventriculomegaly, vertebral anomalies, anal atresia, congenital cardiac disease, tracheoesophageal fistula, renal anomalies, radial dysplasia and other limb defects; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CWS1 and LDD; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In CWS1 and endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes.|||In CWS1 and glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In CWS1.|||In CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P3.|||In CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes.|||In CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In CWS1; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes.|||In CWS1; no lipid phosphatase activity but retains protein phosphatase activity; retains ability to inhibit focal adhesion formation.|||In CWS1; phosphatase-dead protein with neither lipid nor protein phosphatase activity.|||In CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4 but PtdIns(3,4,5)P3 phosphatase activity is similar to wild-type.|||In CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4.|||In CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes.|||In CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes; predominantly nuclear.|||In CWS1; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In GLM2; the patient also suffered from benign meningioma; not capable of inducing apoptosis; induced increased cell proliferation; led to high constitutive AKT1 activation which could not be increased further by stimulation with insulin.|||In HNSCC.|||In MCEPHAS.|||In a patient with prostate cancer; reduced phosphatase activity towards PtdIns(3,4,5); shifts its activity from phosphatidylinositol phosphate 3-phosphatase to phosphatidylinositol phosphate 5-phosphatase; disrupts PI3K/ATK signaling; reduced cell migration.|||In breast cancer; severely reduced protein phosphatase activity.|||In endometrial cancer; loss of protein phosphatase activity.|||In endometrial hyperplasia.|||In endometrial hyperplasia; loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains ability to bind phospholipid membranes.|||In endometrial hyperplasia; reduced phosphatase activity towards PtdIns(3,4,5)P3; mildly reduced tumor suppressor activity; reduced ability to inactivate AKT/PKB.|||In glioblastoma; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In glioblastoma; reduced tumor suppressor activity; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4; reduced ability to inactivate AKT/PKB; retains ability to bind phospholipid membranes.|||In glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4.|||In glioblastoma; severely reduced protein phosphatase activity; loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes.|||In glioma.|||In glioma; loss of protein phosphatase activity.|||In glioma; reduced tumor suppressor activity; fails to inactivate AKT/PKB.|||In glioma; retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes.|||In isoform 3.|||In isoform alpha.|||In malignant melanoma; somatic mutation.|||In multiple cancers.|||In one patient with clinical findings suggesting hamartoma tumor syndrome.|||In prostate cancer; no effect on protein phosphatase activity; reduced phosphatase activity towards Ins(1,3,4,5)P3 but retains PtdIns(3,4,5)P3 phosphatase activity.|||Loss of DLG1-, MAGI2-, MAGI3- and MAST2-binding. Decrease of protein stability.|||Loss of DLG1-, MAGI2-, MAGI3-, MAST1-, MAST2- and MAST3-binding.|||Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding.|||Loss of phosphatase activity towards Ins(1,3,4,5)P3.|||Loss of phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3.|||Loss of phosphatase activity towards Ins(1,3,4,5)P4.|||Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes.|||Loss of phosphatase activity towards Ins(1,3,4,5)P4; retains the ability to bind phospholipid membranes.|||Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation.|||N-acetylthreonine|||No effect on MAGI2-, MAST2- and DLG1-binding.|||No effect on interaction with DLC1 or p85.|||Nuclear. Cytoplasmic; when associated with E-289. Shows less tumor suppressive ability; when associated with E-289.|||PDZ domain-binding|||Phosphatase tensin-type|||Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by CK2 and PLK3|||Phosphoserine; by ROCK1 and CK2|||Phosphothreonine|||Phosphothreonine; by GSK3-beta and PLK3|||Phosphothreonine; by ROCK1 and CK2|||Phosphotyrosine; by FRK|||Polar residues|||Reduced phosphatase activity towards Ins(1,3,4,5)P4; retains PtdIns(3,4,5)P3 phosphatase activity.|||Reduced phosphatase activity towards Ins(1,3,4,5)P4; retains phosphatase activity towards PtdIns(3,4,5)P3.|||Reduced phosphatase activity towards PtdIns(3,4,5)P3, PtdIns(3,4)P2 and PtdIns(3)P.|||Reduces growth suppression activity and promotes anchorage-independent growth. Reduces binding to phospholipid membranes in vitro; phosphatase activity towards PtdIns(3,4,5)P3 is not affected.|||Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain; when associated with A-319.|||Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain; when associated with A-321.|||Reduces the growth suppression activity and cells show anchorage-independent growth. Reduces binding to phospholipid membranes in vitro. Phosphatase activity towards PtdIns(3,4,5)P3 is not affected.|||Removed|||Required for interaction with NOP53|||Retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes.|||Retains phosphatase activity towards Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3; retains the ability to bind phospholipid membranes.|||Significantly lower phosphatase activity, reduced protein stability and decreased growth-inhibitory effect.|||Tyrosine specific protein phosphatases ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215904|||http://purl.uniprot.org/annotation/VAR_007457|||http://purl.uniprot.org/annotation/VAR_007458|||http://purl.uniprot.org/annotation/VAR_007459|||http://purl.uniprot.org/annotation/VAR_007460|||http://purl.uniprot.org/annotation/VAR_007461|||http://purl.uniprot.org/annotation/VAR_007462|||http://purl.uniprot.org/annotation/VAR_007463|||http://purl.uniprot.org/annotation/VAR_007464|||http://purl.uniprot.org/annotation/VAR_007465|||http://purl.uniprot.org/annotation/VAR_007466|||http://purl.uniprot.org/annotation/VAR_007467|||http://purl.uniprot.org/annotation/VAR_007468|||http://purl.uniprot.org/annotation/VAR_007469|||http://purl.uniprot.org/annotation/VAR_007470|||http://purl.uniprot.org/annotation/VAR_007807|||http://purl.uniprot.org/annotation/VAR_007808|||http://purl.uniprot.org/annotation/VAR_008036|||http://purl.uniprot.org/annotation/VAR_008733|||http://purl.uniprot.org/annotation/VAR_008734|||http://purl.uniprot.org/annotation/VAR_008735|||http://purl.uniprot.org/annotation/VAR_008736|||http://purl.uniprot.org/annotation/VAR_008737|||http://purl.uniprot.org/annotation/VAR_008738|||http://purl.uniprot.org/annotation/VAR_008739|||http://purl.uniprot.org/annotation/VAR_008740|||http://purl.uniprot.org/annotation/VAR_008741|||http://purl.uniprot.org/annotation/VAR_008742|||http://purl.uniprot.org/annotation/VAR_008743|||http://purl.uniprot.org/annotation/VAR_011587|||http://purl.uniprot.org/annotation/VAR_011588|||http://purl.uniprot.org/annotation/VAR_011589|||http://purl.uniprot.org/annotation/VAR_018100|||http://purl.uniprot.org/annotation/VAR_018101|||http://purl.uniprot.org/annotation/VAR_018102|||http://purl.uniprot.org/annotation/VAR_018103|||http://purl.uniprot.org/annotation/VAR_018104|||http://purl.uniprot.org/annotation/VAR_018105|||http://purl.uniprot.org/annotation/VAR_018106|||http://purl.uniprot.org/annotation/VAR_025167|||http://purl.uniprot.org/annotation/VAR_026248|||http://purl.uniprot.org/annotation/VAR_026249|||http://purl.uniprot.org/annotation/VAR_026250|||http://purl.uniprot.org/annotation/VAR_026251|||http://purl.uniprot.org/annotation/VAR_026252|||http://purl.uniprot.org/annotation/VAR_026253|||http://purl.uniprot.org/annotation/VAR_026254|||http://purl.uniprot.org/annotation/VAR_026255|||http://purl.uniprot.org/annotation/VAR_026256|||http://purl.uniprot.org/annotation/VAR_026257|||http://purl.uniprot.org/annotation/VAR_026258|||http://purl.uniprot.org/annotation/VAR_026259|||http://purl.uniprot.org/annotation/VAR_026260|||http://purl.uniprot.org/annotation/VAR_026261|||http://purl.uniprot.org/annotation/VAR_026262|||http://purl.uniprot.org/annotation/VAR_026263|||http://purl.uniprot.org/annotation/VAR_026264|||http://purl.uniprot.org/annotation/VAR_026265|||http://purl.uniprot.org/annotation/VAR_026266|||http://purl.uniprot.org/annotation/VAR_026267|||http://purl.uniprot.org/annotation/VAR_026268|||http://purl.uniprot.org/annotation/VAR_026269|||http://purl.uniprot.org/annotation/VAR_026270|||http://purl.uniprot.org/annotation/VAR_026271|||http://purl.uniprot.org/annotation/VAR_026272|||http://purl.uniprot.org/annotation/VAR_026273|||http://purl.uniprot.org/annotation/VAR_026274|||http://purl.uniprot.org/annotation/VAR_026275|||http://purl.uniprot.org/annotation/VAR_026276|||http://purl.uniprot.org/annotation/VAR_026277|||http://purl.uniprot.org/annotation/VAR_026278|||http://purl.uniprot.org/annotation/VAR_026279|||http://purl.uniprot.org/annotation/VAR_026280|||http://purl.uniprot.org/annotation/VAR_026281|||http://purl.uniprot.org/annotation/VAR_032634|||http://purl.uniprot.org/annotation/VAR_032635|||http://purl.uniprot.org/annotation/VAR_032636|||http://purl.uniprot.org/annotation/VAR_032637|||http://purl.uniprot.org/annotation/VAR_076551|||http://purl.uniprot.org/annotation/VAR_076762|||http://purl.uniprot.org/annotation/VAR_076763|||http://purl.uniprot.org/annotation/VAR_078705|||http://purl.uniprot.org/annotation/VSP_055420|||http://purl.uniprot.org/annotation/VSP_055421|||http://purl.uniprot.org/annotation/VSP_055422|||http://purl.uniprot.org/annotation/VSP_055423
http://togogenome.org/gene/9606:C16orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C16orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296625|||http://purl.uniprot.org/annotation/VAR_034632
http://togogenome.org/gene/9606:DTX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase DTX1|||Polar residues|||Pro residues|||RING-type|||SH3-binding|||WWE 1|||WWE 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219080
http://togogenome.org/gene/9606:ZNF140                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKI0|||http://purl.uniprot.org/uniprot/P52738                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 140                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047423|||http://purl.uniprot.org/annotation/VAR_046562|||http://purl.uniprot.org/annotation/VSP_056436
http://togogenome.org/gene/9606:GGPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95749                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Geranylgeranyl pyrophosphate synthase|||In MDHLO; shows slightly decreased farnesyltranstransferase activity.|||In MDHLO; unknown pathological significance; shows no change in farnesyltranstransferase activity.|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123962|||http://purl.uniprot.org/annotation/VAR_086458|||http://purl.uniprot.org/annotation/VAR_086459|||http://purl.uniprot.org/annotation/VAR_086460|||http://purl.uniprot.org/annotation/VAR_086461|||http://purl.uniprot.org/annotation/VAR_086462|||http://purl.uniprot.org/annotation/VSP_056578
http://togogenome.org/gene/9606:LOC100129697                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZP14                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:MTPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58546|||http://purl.uniprot.org/uniprot/Q69YG1                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Myotrophin|||N-acetylcysteine|||N6-acetyllysine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067031
http://togogenome.org/gene/9606:CASP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14790                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-riboxanated arginine|||Abolished ADP-riboxanation by C.violaceum CopC.|||Abolishes binding to FLASH. Induces NF-kappa-B activation.|||Abolishes interaction with UBR2.|||Associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma.|||Caspase-8 subunit p10|||Caspase-8 subunit p18|||Cleavage; by CASP6|||Cleavage; by autocatalytic cleavage|||DED 1|||DED 2|||Impaired CDK1-mediated phosphorylation and enhanced apoptosis.|||In CASP8D.|||In isoform 2, isoform 4 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 9.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004628|||http://purl.uniprot.org/annotation/PRO_0000004629|||http://purl.uniprot.org/annotation/PRO_0000004630|||http://purl.uniprot.org/annotation/PRO_0000004631|||http://purl.uniprot.org/annotation/VAR_014204|||http://purl.uniprot.org/annotation/VAR_020127|||http://purl.uniprot.org/annotation/VAR_025816|||http://purl.uniprot.org/annotation/VSP_000808|||http://purl.uniprot.org/annotation/VSP_000809|||http://purl.uniprot.org/annotation/VSP_000810|||http://purl.uniprot.org/annotation/VSP_000811|||http://purl.uniprot.org/annotation/VSP_000812|||http://purl.uniprot.org/annotation/VSP_000813|||http://purl.uniprot.org/annotation/VSP_000814|||http://purl.uniprot.org/annotation/VSP_000815|||http://purl.uniprot.org/annotation/VSP_000816|||http://purl.uniprot.org/annotation/VSP_000817
http://togogenome.org/gene/9606:SLC10A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS43|||http://purl.uniprot.org/uniprot/P09131                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||P3 protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052343|||http://purl.uniprot.org/annotation/VAR_050229|||http://purl.uniprot.org/annotation/VSP_043669
http://togogenome.org/gene/9606:OR6C68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDL8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 6C68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309618
http://togogenome.org/gene/9606:LIAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0H4IV28|||http://purl.uniprot.org/uniprot/Q6ZQX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||20 X 10 AA approximate tandem repeat of A-L-K-G-F-H-P-D-P-E|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ATE1|||Lysine-rich domain|||Polar residues|||Protein LIAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340233|||http://purl.uniprot.org/annotation/VAR_044008|||http://purl.uniprot.org/annotation/VAR_044009|||http://purl.uniprot.org/annotation/VSP_034195|||http://purl.uniprot.org/annotation/VSP_034196|||http://purl.uniprot.org/annotation/VSP_034197|||http://purl.uniprot.org/annotation/VSP_034198
http://togogenome.org/gene/9606:CATSPERD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XM0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit delta|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287150|||http://purl.uniprot.org/annotation/VAR_032270|||http://purl.uniprot.org/annotation/VAR_032271|||http://purl.uniprot.org/annotation/VAR_061714|||http://purl.uniprot.org/annotation/VSP_025344|||http://purl.uniprot.org/annotation/VSP_025345|||http://purl.uniprot.org/annotation/VSP_025346
http://togogenome.org/gene/9606:RAB6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0N0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Effector region|||No GTP binding. No GTP binding; when associated with T-45.|||No GTP binding; when associated with G-25.|||O-AMP-tyrosine; by Legionella DrrA|||Ras-related protein Rab-6C|||Required for centrosome localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121117|||http://purl.uniprot.org/annotation/VAR_038161
http://togogenome.org/gene/9606:CYP3A7-CYP3A51P                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24462                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 3A7|||Has no effect on catalytic activity.|||In isoform 2.|||Increases catalytic activity.|||Reduces affinity for substrate and catalytic efficiency.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051790|||http://purl.uniprot.org/annotation/VAR_020124|||http://purl.uniprot.org/annotation/VAR_055564|||http://purl.uniprot.org/annotation/VSP_055577
http://togogenome.org/gene/9606:USP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBJ7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080660|||http://purl.uniprot.org/annotation/VAR_022055|||http://purl.uniprot.org/annotation/VAR_024590
http://togogenome.org/gene/9606:ASPDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6ND91                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aspartate dehydrogenase domain-containing protein|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300623|||http://purl.uniprot.org/annotation/VAR_062676|||http://purl.uniprot.org/annotation/VSP_038742|||http://purl.uniprot.org/annotation/VSP_038743
http://togogenome.org/gene/9606:ZNF773                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QYZ8|||http://purl.uniprot.org/uniprot/Q6PK81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 773                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285303|||http://purl.uniprot.org/annotation/VSP_024870
http://togogenome.org/gene/9606:TRIM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C029                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphorylation by RPS6KA5/MSK1. Reduced ubiquitination activity towards RNF187.|||Abolishes ubiquitination and stabilization of RNF187.|||Abolishes ubiquitination and stabilization of RNF187; when associated with A-29.|||Abolishes ubiquitination and stabilization of RNF187; when associated with A-32.|||B box-type|||B30.2/SPRY|||Complete loss of interaction with GYG1.|||Complete loss of substrate binding.|||E3 ubiquitin-protein ligase TRIM7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine; by RPS6KA5|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056204|||http://purl.uniprot.org/annotation/VAR_017399|||http://purl.uniprot.org/annotation/VAR_017400|||http://purl.uniprot.org/annotation/VAR_017401|||http://purl.uniprot.org/annotation/VAR_052125|||http://purl.uniprot.org/annotation/VAR_052126|||http://purl.uniprot.org/annotation/VSP_009018|||http://purl.uniprot.org/annotation/VSP_009019|||http://purl.uniprot.org/annotation/VSP_009020|||http://purl.uniprot.org/annotation/VSP_009021|||http://purl.uniprot.org/annotation/VSP_009022
http://togogenome.org/gene/9606:PEX11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96011                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Interaction with PEX19, PEX11G and FIS1 and peroxisome targeting|||N6-acetyllysine|||Peroxisomal membrane protein 11B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105967|||http://purl.uniprot.org/annotation/VSP_042860
http://togogenome.org/gene/9606:JUNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17275|||http://purl.uniprot.org/uniprot/Q5U079                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BZIP|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Leucine-zipper|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Transcription factor JunB|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076438|||http://purl.uniprot.org/annotation/VAR_021081
http://togogenome.org/gene/9606:ZNF511                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB15                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 1.|||Omega-N-methylarginine|||Zinc finger protein 511                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047629|||http://purl.uniprot.org/annotation/VSP_059997
http://togogenome.org/gene/9606:CENPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5T0|||http://purl.uniprot.org/uniprot/Q9H3R5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere protein H|||Centromere protein H C-terminal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089478|||http://purl.uniprot.org/annotation/VAR_036167
http://togogenome.org/gene/9606:CRNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBG3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cornulin|||Disordered|||EF-hand|||In ESCR.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305586|||http://purl.uniprot.org/annotation/VAR_048469|||http://purl.uniprot.org/annotation/VAR_048470|||http://purl.uniprot.org/annotation/VAR_048471
http://togogenome.org/gene/9606:ST6GALNAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDV1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149275|||http://purl.uniprot.org/annotation/VAR_055846|||http://purl.uniprot.org/annotation/VSP_013218|||http://purl.uniprot.org/annotation/VSP_013219
http://togogenome.org/gene/9606:COMMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N668                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 1|||In isoform 2.|||N-acetylalanine|||Reduces copper-induced fluorescence change.|||Removed|||Required for binding to PtdIns(4,5)P2|||Sufficient for interaction with SLC12A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077384|||http://purl.uniprot.org/annotation/VSP_055532
http://togogenome.org/gene/9606:SYNE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMZ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Interchain (C-563 in SUN2); alternate|||Interchain (with C-657 in SUN1); alternate|||KASH|||Nesprin-3|||Perinuclear space|||Spectrin 1|||Spectrin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281120|||http://purl.uniprot.org/annotation/VAR_031231|||http://purl.uniprot.org/annotation/VAR_031232|||http://purl.uniprot.org/annotation/VAR_031233|||http://purl.uniprot.org/annotation/VAR_031234|||http://purl.uniprot.org/annotation/VAR_068433|||http://purl.uniprot.org/annotation/VSP_023976|||http://purl.uniprot.org/annotation/VSP_023977|||http://purl.uniprot.org/annotation/VSP_023978
http://togogenome.org/gene/9606:C1orf159                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HA4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Uncharacterized protein C1orf159                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255250|||http://purl.uniprot.org/annotation/VSP_021280|||http://purl.uniprot.org/annotation/VSP_021281|||http://purl.uniprot.org/annotation/VSP_021282|||http://purl.uniprot.org/annotation/VSP_021283|||http://purl.uniprot.org/annotation/VSP_021284|||http://purl.uniprot.org/annotation/VSP_021285|||http://purl.uniprot.org/annotation/VSP_021286
http://togogenome.org/gene/9606:GATA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUF4|||http://purl.uniprot.org/uniprot/B6DU75|||http://purl.uniprot.org/uniprot/P43694                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||GATA-type|||GATA-type 1|||GATA-type 2|||In ASD2.|||In ASD2; decreased function resulting in reduced myocardial genes expression; fails to down-regulate endothelial and endocardial genes.|||In ASD2; unknown pathological significance.|||In AVSD4.|||In AVSD4; also in a patient with VSD1 and a patient with TOF.|||In TACHD; impairs the ability to bind and transactivate the promoter of AMH gene; abolishes interaction with ZFPM2.|||In TOF.|||In TOF; drastically diminished DNA-binding affinity; decreased transcriptional activity; no effect on subcellular location; completely disrupted interaction with TBX5.|||In TOF; slightly diminished DNA-binding affinity; decreased transcriptional activity; no effect on subcellular location; no effect on interaction with TBX5.|||In VSD1 and TOF; unknown pathological significance.|||In VSD1.|||In VSD1; significantly reduced activation of the NPPA promoter with the mutant protein compared to wild-type.|||In isoform 2.|||N6-methyllysine; by EZH2|||Polar residues|||Probable disease-associated variant found in patients with dilated cardiomyopathy; results in significantly reduced transactivation activity.|||Transcription factor GATA-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083413|||http://purl.uniprot.org/annotation/VAR_016204|||http://purl.uniprot.org/annotation/VAR_038195|||http://purl.uniprot.org/annotation/VAR_038196|||http://purl.uniprot.org/annotation/VAR_067605|||http://purl.uniprot.org/annotation/VAR_067606|||http://purl.uniprot.org/annotation/VAR_067607|||http://purl.uniprot.org/annotation/VAR_067608|||http://purl.uniprot.org/annotation/VAR_067609|||http://purl.uniprot.org/annotation/VAR_067610|||http://purl.uniprot.org/annotation/VAR_067611|||http://purl.uniprot.org/annotation/VAR_067612|||http://purl.uniprot.org/annotation/VAR_067613|||http://purl.uniprot.org/annotation/VAR_067614|||http://purl.uniprot.org/annotation/VAR_067615|||http://purl.uniprot.org/annotation/VAR_067616|||http://purl.uniprot.org/annotation/VAR_067617|||http://purl.uniprot.org/annotation/VAR_067618|||http://purl.uniprot.org/annotation/VAR_067619|||http://purl.uniprot.org/annotation/VAR_067620|||http://purl.uniprot.org/annotation/VAR_067621|||http://purl.uniprot.org/annotation/VAR_067622|||http://purl.uniprot.org/annotation/VAR_067623|||http://purl.uniprot.org/annotation/VAR_070670|||http://purl.uniprot.org/annotation/VAR_071514|||http://purl.uniprot.org/annotation/VAR_071515|||http://purl.uniprot.org/annotation/VAR_071516|||http://purl.uniprot.org/annotation/VAR_072111|||http://purl.uniprot.org/annotation/VAR_072112|||http://purl.uniprot.org/annotation/VAR_072113|||http://purl.uniprot.org/annotation/VAR_072114|||http://purl.uniprot.org/annotation/VSP_055082
http://togogenome.org/gene/9606:PTPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15257                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with the PP2A(D) complex.|||Disordered|||Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex.|||Impairs interaction with the PP2A(D) complex.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Removed|||Serine/threonine-protein phosphatase 2A activator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071524|||http://purl.uniprot.org/annotation/VAR_028101|||http://purl.uniprot.org/annotation/VAR_028102|||http://purl.uniprot.org/annotation/VAR_028103|||http://purl.uniprot.org/annotation/VSP_005122|||http://purl.uniprot.org/annotation/VSP_005123|||http://purl.uniprot.org/annotation/VSP_005124
http://togogenome.org/gene/9606:NEDD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15843                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  (Microbial infection) Deamidated glutamine|||Decreased interaction with B.pseudomallei Cif protein, leading to decreased deamidation.|||Decreased interaction with B.pseudomallei Cif protein, leading to slightly decreased deamidation.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Impaired ability to activate cullin-RING-based E3 ubiquitin-protein ligase complexes.|||Interaction with UBE1C|||N6-acetyllysine|||NEDD8|||Prevents adenylation by UBE1C.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042767|||http://purl.uniprot.org/annotation/PRO_0000042768
http://togogenome.org/gene/9606:ADAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH5|||http://purl.uniprot.org/uniprot/Q96M93                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  A to I editase|||Adenosine deaminase domain-containing protein 1|||DRBM|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309520|||http://purl.uniprot.org/annotation/VSP_029225|||http://purl.uniprot.org/annotation/VSP_029226
http://togogenome.org/gene/9606:HPS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TN06|||http://purl.uniprot.org/uniprot/A8K2E6|||http://purl.uniprot.org/uniprot/Q6P1K3|||http://purl.uniprot.org/uniprot/Q9NQG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BLOC-3 complex member HPS4|||Basic and acidic residues|||CCZ1/INTU/HPS4 third Longin|||CCZ1/INTU/HSP4 first Longin|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084052|||http://purl.uniprot.org/annotation/VAR_021836|||http://purl.uniprot.org/annotation/VAR_024158|||http://purl.uniprot.org/annotation/VAR_024159|||http://purl.uniprot.org/annotation/VAR_025006|||http://purl.uniprot.org/annotation/VAR_025007|||http://purl.uniprot.org/annotation/VSP_003880|||http://purl.uniprot.org/annotation/VSP_003881|||http://purl.uniprot.org/annotation/VSP_003882|||http://purl.uniprot.org/annotation/VSP_017082
http://togogenome.org/gene/9606:IL6R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTB5|||http://purl.uniprot.org/uniprot/A0N0L5|||http://purl.uniprot.org/uniprot/P08887                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  30% decrease of ligand-binding and IL6 signaling.|||30% decrease of ligand-binding and increase of IL6 signaling.|||30% increase of ligand-binding and 100% increase in IL6 signaling.|||50% Decrease of ligand-binding and 50% increase in IL6 signaling.|||50% decrease of ligand-binding and IL6 signaling.|||70% decrease of ligand-binding and no IL6 signaling.|||80% decrease of ligand-binding and no IL6 signaling.|||Abolishes cleavage by ADAM17.|||Cleavage; by ADAM10 and ADAM17|||Complete loss of ligand-binding.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like C2-type|||In HIES5; decreased STAT1 and STAT3 phosphorylation.|||In HIES5; unknown pathological significance; no effect on STAT1 and STAT3 phosphorylation.|||In isoform 2.|||Interleukin-6 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||No change of ligand-binding and IL6 signaling.|||No change of ligand-binding and no IL6 signaling.|||No effect on IL6R signaling.|||No effect on IL6R signaling; when associated with A-55, A-93, A-221 and A-245. Loss of cleavage by ADAM17; when associated with A-55, A-93, A-221 and A-245.|||No effect on cleavage or sIL6R levels. No effect on IL6R signaling; when associated with A-55, A-221, A-245 and A-350. Loss of cleavage by ADAM17; when associated with A-55, A-221, A-245 and A-350.|||No effect on cleavage or sIL6R levels. No effect on IL6R signaling; when associated with A-55, A-93, A-245 and A-350. Loss of cleavage by ADAM17; when associated with A-55, A-93, A-245 and A-350.|||Not glycosylated|||O-linked (GlcNAc) threonine|||Polar residues|||Reduces cleavage by ADAM17.|||Significantly associated with circulating levels of IL6 and soluble IL6R; increases cleavage by ADAM17.|||Slightly induces cleavage and sIL6R levels.No effect on IL6R signaling; when associated with A-55, A-93, A-221 and A-350. Loss of cleavage by ADAM17; when associated with A-55, A-93, A-221 and A-350.|||Soluble interleukin-6 receptor subunit alpha|||Strongly induces cleavage and sIL6R levels.|||Strongly induces cleavage and sIL6R levels. No effect on IL6R signaling; when associated with A-93, A-221, A-245 and A-350. Loss of cleavage by ADAM17; when associated with A-93, A-221, A-245 and A-350.|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010895|||http://purl.uniprot.org/annotation/PRO_0000450730|||http://purl.uniprot.org/annotation/PRO_5001831899|||http://purl.uniprot.org/annotation/PRO_5014296519|||http://purl.uniprot.org/annotation/VAR_021995|||http://purl.uniprot.org/annotation/VAR_049166|||http://purl.uniprot.org/annotation/VAR_084713|||http://purl.uniprot.org/annotation/VAR_084714|||http://purl.uniprot.org/annotation/VSP_001682|||http://purl.uniprot.org/annotation/VSP_001683
http://togogenome.org/gene/9606:DCST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1A1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DC-STAMP domain-containing protein 2|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278826|||http://purl.uniprot.org/annotation/VSP_023408|||http://purl.uniprot.org/annotation/VSP_023409
http://togogenome.org/gene/9606:OR4X2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVL5|||http://purl.uniprot.org/uniprot/Q8NGF9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 4X2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150571
http://togogenome.org/gene/9606:ZFP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCL3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 14 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047285
http://togogenome.org/gene/9606:EVL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EVH2|||EVH2 block A|||EVH2 block B|||EVH2 block C|||Ena/VASP-like protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 1 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KLKR|||Phosphoserine|||Polar residues|||Pro residues|||Required for interaction with ZDHHC17|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087104|||http://purl.uniprot.org/annotation/VAR_036464|||http://purl.uniprot.org/annotation/VAR_036465|||http://purl.uniprot.org/annotation/VSP_004044|||http://purl.uniprot.org/annotation/VSP_057322|||http://purl.uniprot.org/annotation/VSP_057323|||http://purl.uniprot.org/annotation/VSP_058778|||http://purl.uniprot.org/annotation/VSP_058779
http://togogenome.org/gene/9606:ZSCAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7L9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 3.|||In isoform 4.|||SCAN box|||Zinc finger and SCAN domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047749|||http://purl.uniprot.org/annotation/VAR_065095|||http://purl.uniprot.org/annotation/VSP_011947|||http://purl.uniprot.org/annotation/VSP_011948|||http://purl.uniprot.org/annotation/VSP_040201|||http://purl.uniprot.org/annotation/VSP_040202
http://togogenome.org/gene/9606:CCL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55773                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-C motif chemokine 23|||CCL23(19-99)|||CCL23(22-99)|||CCL23(27-99)|||CCL23(30-99)|||In isoform Long.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005229|||http://purl.uniprot.org/annotation/PRO_0000041847|||http://purl.uniprot.org/annotation/PRO_0000041848|||http://purl.uniprot.org/annotation/PRO_0000041849|||http://purl.uniprot.org/annotation/PRO_0000041850|||http://purl.uniprot.org/annotation/VAR_011916|||http://purl.uniprot.org/annotation/VSP_001063
http://togogenome.org/gene/9606:TCP11X2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9J9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  T-complex protein 11 X-linked protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000424012
http://togogenome.org/gene/9606:DERL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RGY0|||http://purl.uniprot.org/uniprot/Q9BUN8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Derlin-1|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Impaired ERAD substrate degradation.|||In isoform 2.|||Lumenal|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Reduces interaction with and proteolysis of XBP1 isoform 1.|||Removed|||SHP-box|||Significantly reduced binding to VCP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219042|||http://purl.uniprot.org/annotation/VAR_019516|||http://purl.uniprot.org/annotation/VSP_041329
http://togogenome.org/gene/9606:OR52I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGK6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150778|||http://purl.uniprot.org/annotation/VAR_034342
http://togogenome.org/gene/9606:LBHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQE6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LBH|||LBH domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284493|||http://purl.uniprot.org/annotation/VSP_024545
http://togogenome.org/gene/9606:CHMP4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H444                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Charged multivesicular body protein 4b|||Disordered|||In CTRCT31.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211489|||http://purl.uniprot.org/annotation/VAR_037579|||http://purl.uniprot.org/annotation/VAR_037580
http://togogenome.org/gene/9606:PAIP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Polar residues|||Polyadenylate-binding protein-interacting protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317294
http://togogenome.org/gene/9606:OR14C36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHC7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 14C36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150589|||http://purl.uniprot.org/annotation/VAR_062070|||http://purl.uniprot.org/annotation/VAR_062071|||http://purl.uniprot.org/annotation/VAR_062072
http://togogenome.org/gene/9606:MAPK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4K2|||http://purl.uniprot.org/uniprot/P45983                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protein kinase activity.|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 1, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Mitogen-activated protein kinase 8|||Phosphorylation blocked.|||Phosphoserine|||Phosphothreonine; by MAP2K7|||Phosphotyrosine; by MAP2K4|||Polar residues|||Protein kinase|||Proton acceptor|||S-nitrosocysteine|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186262|||http://purl.uniprot.org/annotation/VAR_042258|||http://purl.uniprot.org/annotation/VAR_042259|||http://purl.uniprot.org/annotation/VAR_050592|||http://purl.uniprot.org/annotation/VSP_004831|||http://purl.uniprot.org/annotation/VSP_004832|||http://purl.uniprot.org/annotation/VSP_004833|||http://purl.uniprot.org/annotation/VSP_054554
http://togogenome.org/gene/9606:ATG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQM6|||http://purl.uniprot.org/uniprot/O95352                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FAP motif|||Glycyl thioester intermediate|||Impairs conjugation activity; when associated with D-15 and D-16.|||Impairs conjugation activity; when associated with D-15 and D-17.|||Impairs conjugation activity; when associated with D-16 and D-17.|||In SCAR31.|||In SCAR31; in homozygous patient cells it results in diminished autophagic flux.|||In SCAR31; results in decreased LC3-I lipidation to form LC3-II.|||In SCAR31; results in severely decreased LC3-I lipidation to form LC3-II.|||In SCAR31; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of LC3-I lipidation to form LC3-II.|||N-acetylalanine|||Phosphoserine|||Removed|||THIF-type NAD/FAD binding fold|||Ubiquitin-like modifier-activating enzyme ATG7|||Ubiquitin-like modifier-activating enzyme Atg7 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212806|||http://purl.uniprot.org/annotation/VAR_053014|||http://purl.uniprot.org/annotation/VAR_085979|||http://purl.uniprot.org/annotation/VAR_085980|||http://purl.uniprot.org/annotation/VAR_085981|||http://purl.uniprot.org/annotation/VAR_085982|||http://purl.uniprot.org/annotation/VAR_085983|||http://purl.uniprot.org/annotation/VAR_085984|||http://purl.uniprot.org/annotation/VAR_085985|||http://purl.uniprot.org/annotation/VAR_085986|||http://purl.uniprot.org/annotation/VSP_013205|||http://purl.uniprot.org/annotation/VSP_045206|||http://purl.uniprot.org/annotation/VSP_045207
http://togogenome.org/gene/9606:LLPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Protein LLP homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274346
http://togogenome.org/gene/9606:PKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98161                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with PKD1.|||C-type lectin|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Does not affect auto-cleavage.|||Does not undergo auto-cleavage.|||Extracellular|||GPS|||Helical|||In PKD1.|||In PKD1; associated with M-2768.|||In PKD1; associated with S-2858.|||In PKD1; benign variant.|||In PKD1; does not undergo autoproteolytic cleavage.|||In PKD1; likely benign variant.|||In PKD1; unknown pathological significance.|||In PKD1; unknown pathological significance; nearly abolishes expression at the cell membrane.|||In a patient with polycystic kidney disease; does not affect autoproteolytic cleavage at the GPS domain.|||In isoform 2 and isoform 3.|||In isoform 2.|||LDL-receptor class A; atypical|||LRR 1|||LRR 2|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||PKD 1|||PKD 10|||PKD 11|||PKD 12|||PKD 13|||PKD 14|||PKD 15|||PKD 16|||PKD 17|||PKD 2|||PKD 3|||PKD 4|||PKD 5|||PKD 6|||PKD 7|||PKD 8|||PKD 9|||PLAT|||Phosphoserine; by PRKX; in vitro|||Polar residues|||Polycystin-1|||REJ|||WSC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024298|||http://purl.uniprot.org/annotation/VAR_005533|||http://purl.uniprot.org/annotation/VAR_005535|||http://purl.uniprot.org/annotation/VAR_005536|||http://purl.uniprot.org/annotation/VAR_005537|||http://purl.uniprot.org/annotation/VAR_005538|||http://purl.uniprot.org/annotation/VAR_005539|||http://purl.uniprot.org/annotation/VAR_005541|||http://purl.uniprot.org/annotation/VAR_005542|||http://purl.uniprot.org/annotation/VAR_005543|||http://purl.uniprot.org/annotation/VAR_005544|||http://purl.uniprot.org/annotation/VAR_005545|||http://purl.uniprot.org/annotation/VAR_005546|||http://purl.uniprot.org/annotation/VAR_005547|||http://purl.uniprot.org/annotation/VAR_010085|||http://purl.uniprot.org/annotation/VAR_010086|||http://purl.uniprot.org/annotation/VAR_010087|||http://purl.uniprot.org/annotation/VAR_010088|||http://purl.uniprot.org/annotation/VAR_010089|||http://purl.uniprot.org/annotation/VAR_010090|||http://purl.uniprot.org/annotation/VAR_010091|||http://purl.uniprot.org/annotation/VAR_010092|||http://purl.uniprot.org/annotation/VAR_010093|||http://purl.uniprot.org/annotation/VAR_010094|||http://purl.uniprot.org/annotation/VAR_010095|||http://purl.uniprot.org/annotation/VAR_010096|||http://purl.uniprot.org/annotation/VAR_010097|||http://purl.uniprot.org/annotation/VAR_010098|||http://purl.uniprot.org/annotation/VAR_010099|||http://purl.uniprot.org/annotation/VAR_010100|||http://purl.uniprot.org/annotation/VAR_011030|||http://purl.uniprot.org/annotation/VAR_011031|||http://purl.uniprot.org/annotation/VAR_011032|||http://purl.uniprot.org/annotation/VAR_011033|||http://purl.uniprot.org/annotation/VAR_011034|||http://purl.uniprot.org/annotation/VAR_011035|||http://purl.uniprot.org/annotation/VAR_011036|||http://purl.uniprot.org/annotation/VAR_011037|||http://purl.uniprot.org/annotation/VAR_011038|||http://purl.uniprot.org/annotation/VAR_011039|||http://purl.uniprot.org/annotation/VAR_011040|||http://purl.uniprot.org/annotation/VAR_011041|||http://purl.uniprot.org/annotation/VAR_011042|||http://purl.uniprot.org/annotation/VAR_011043|||http://purl.uniprot.org/annotation/VAR_011044|||http://purl.uniprot.org/annotation/VAR_011045|||http://purl.uniprot.org/annotation/VAR_011046|||http://purl.uniprot.org/annotation/VAR_011047|||http://purl.uniprot.org/annotation/VAR_011048|||http://purl.uniprot.org/annotation/VAR_011049|||http://purl.uniprot.org/annotation/VAR_011050|||http://purl.uniprot.org/annotation/VAR_011051|||http://purl.uniprot.org/annotation/VAR_011052|||http://purl.uniprot.org/annotation/VAR_011053|||http://purl.uniprot.org/annotation/VAR_011054|||http://purl.uniprot.org/annotation/VAR_011055|||http://purl.uniprot.org/annotation/VAR_011056|||http://purl.uniprot.org/annotation/VAR_011057|||http://purl.uniprot.org/annotation/VAR_011058|||http://purl.uniprot.org/annotation/VAR_011059|||http://purl.uniprot.org/annotation/VAR_011060|||http://purl.uniprot.org/annotation/VAR_011061|||http://purl.uniprot.org/annotation/VAR_011062|||http://purl.uniprot.org/annotation/VAR_011063|||http://purl.uniprot.org/annotation/VAR_011064|||http://purl.uniprot.org/annotation/VAR_011065|||http://purl.uniprot.org/annotation/VAR_011066|||http://purl.uniprot.org/annotation/VAR_011067|||http://purl.uniprot.org/annotation/VAR_011068|||http://purl.uniprot.org/annotation/VAR_011069|||http://purl.uniprot.org/annotation/VAR_011070|||http://purl.uniprot.org/annotation/VAR_011071|||http://purl.uniprot.org/annotation/VAR_012452|||http://purl.uniprot.org/annotation/VAR_012453|||http://purl.uniprot.org/annotation/VAR_012454|||http://purl.uniprot.org/annotation/VAR_012455|||http://purl.uniprot.org/annotation/VAR_012456|||http://purl.uniprot.org/annotation/VAR_012457|||http://purl.uniprot.org/annotation/VAR_012458|||http://purl.uniprot.org/annotation/VAR_012459|||http://purl.uniprot.org/annotation/VAR_012460|||http://purl.uniprot.org/annotation/VAR_012461|||http://purl.uniprot.org/annotation/VAR_012462|||http://purl.uniprot.org/annotation/VAR_012463|||http://purl.uniprot.org/annotation/VAR_012464|||http://purl.uniprot.org/annotation/VAR_012465|||http://purl.uniprot.org/annotation/VAR_012466|||http://purl.uniprot.org/annotation/VAR_012467|||http://purl.uniprot.org/annotation/VAR_012468|||http://purl.uniprot.org/annotation/VAR_012469|||http://purl.uniprot.org/annotation/VAR_012470|||http://purl.uniprot.org/annotation/VAR_012471|||http://purl.uniprot.org/annotation/VAR_013838|||http://purl.uniprot.org/annotation/VAR_013839|||http://purl.uniprot.org/annotation/VAR_014918|||http://purl.uniprot.org/annotation/VAR_056696|||http://purl.uniprot.org/annotation/VAR_056697|||http://purl.uniprot.org/annotation/VAR_056698|||http://purl.uniprot.org/annotation/VAR_056699|||http://purl.uniprot.org/annotation/VAR_056700|||http://purl.uniprot.org/annotation/VAR_056701|||http://purl.uniprot.org/annotation/VAR_056702|||http://purl.uniprot.org/annotation/VAR_056703|||http://purl.uniprot.org/annotation/VAR_056704|||http://purl.uniprot.org/annotation/VAR_058759|||http://purl.uniprot.org/annotation/VAR_058760|||http://purl.uniprot.org/annotation/VAR_058761|||http://purl.uniprot.org/annotation/VAR_058762|||http://purl.uniprot.org/annotation/VAR_058763|||http://purl.uniprot.org/annotation/VAR_058764|||http://purl.uniprot.org/annotation/VAR_058765|||http://purl.uniprot.org/annotation/VAR_058766|||http://purl.uniprot.org/annotation/VAR_058767|||http://purl.uniprot.org/annotation/VAR_058768|||http://purl.uniprot.org/annotation/VAR_058769|||http://purl.uniprot.org/annotation/VAR_058770|||http://purl.uniprot.org/annotation/VAR_058771|||http://purl.uniprot.org/annotation/VAR_058772|||http://purl.uniprot.org/annotation/VAR_058773|||http://purl.uniprot.org/annotation/VAR_058774|||http://purl.uniprot.org/annotation/VAR_058775|||http://purl.uniprot.org/annotation/VAR_058776|||http://purl.uniprot.org/annotation/VAR_058777|||http://purl.uniprot.org/annotation/VAR_058778|||http://purl.uniprot.org/annotation/VAR_058779|||http://purl.uniprot.org/annotation/VAR_058780|||http://purl.uniprot.org/annotation/VAR_058781|||http://purl.uniprot.org/annotation/VAR_058782|||http://purl.uniprot.org/annotation/VAR_058783|||http://purl.uniprot.org/annotation/VAR_058784|||http://purl.uniprot.org/annotation/VAR_058785|||http://purl.uniprot.org/annotation/VAR_058786|||http://purl.uniprot.org/annotation/VAR_058787|||http://purl.uniprot.org/annotation/VAR_058788|||http://purl.uniprot.org/annotation/VAR_058789|||http://purl.uniprot.org/annotation/VAR_058790|||http://purl.uniprot.org/annotation/VAR_058791|||http://purl.uniprot.org/annotation/VAR_058792|||http://purl.uniprot.org/annotation/VAR_058793|||http://purl.uniprot.org/annotation/VAR_058794|||http://purl.uniprot.org/annotation/VAR_058795|||http://purl.uniprot.org/annotation/VAR_058796|||http://purl.uniprot.org/annotation/VAR_058797|||http://purl.uniprot.org/annotation/VAR_058798|||http://purl.uniprot.org/annotation/VAR_058799|||http://purl.uniprot.org/annotation/VAR_058800|||http://purl.uniprot.org/annotation/VAR_058801|||http://purl.uniprot.org/annotation/VAR_058802|||http://purl.uniprot.org/annotation/VAR_058803|||http://purl.uniprot.org/annotation/VAR_058804|||http://purl.uniprot.org/annotation/VAR_058805|||http://purl.uniprot.org/annotation/VAR_058806|||http://purl.uniprot.org/annotation/VAR_058807|||http://purl.uniprot.org/annotation/VAR_058808|||http://purl.uniprot.org/annotation/VAR_058809|||http://purl.uniprot.org/annotation/VAR_058810|||http://purl.uniprot.org/annotation/VAR_058811|||http://purl.uniprot.org/annotation/VAR_058812|||http://purl.uniprot.org/annotation/VAR_058813|||http://purl.uniprot.org/annotation/VAR_058814|||http://purl.uniprot.org/annotation/VAR_058815|||http://purl.uniprot.org/annotation/VAR_058816|||http://purl.uniprot.org/annotation/VAR_058817|||http://purl.uniprot.org/annotation/VAR_058818|||http://purl.uniprot.org/annotation/VAR_058819|||http://purl.uniprot.org/annotation/VAR_064380|||http://purl.uniprot.org/annotation/VAR_064381|||http://purl.uniprot.org/annotation/VAR_064382|||http://purl.uniprot.org/annotation/VAR_064383|||http://purl.uniprot.org/annotation/VAR_064384|||http://purl.uniprot.org/annotation/VAR_064385|||http://purl.uniprot.org/annotation/VAR_064386|||http://purl.uniprot.org/annotation/VAR_064387|||http://purl.uniprot.org/annotation/VAR_064388|||http://purl.uniprot.org/annotation/VAR_064389|||http://purl.uniprot.org/annotation/VAR_064390|||http://purl.uniprot.org/annotation/VAR_064391|||http://purl.uniprot.org/annotation/VAR_064392|||http://purl.uniprot.org/annotation/VAR_064393|||http://purl.uniprot.org/annotation/VAR_068024|||http://purl.uniprot.org/annotation/VAR_068025|||http://purl.uniprot.org/annotation/VAR_068026|||http://purl.uniprot.org/annotation/VAR_068027|||http://purl.uniprot.org/annotation/VAR_068028|||http://purl.uniprot.org/annotation/VAR_068029|||http://purl.uniprot.org/annotation/VAR_068030|||http://purl.uniprot.org/annotation/VAR_068031|||http://purl.uniprot.org/annotation/VSP_009677|||http://purl.uniprot.org/annotation/VSP_009678
http://togogenome.org/gene/9606:MED29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUA7|||http://purl.uniprot.org/uniprot/Q9NX70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 29|||N-acetylalanine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288058|||http://purl.uniprot.org/annotation/VSP_056133|||http://purl.uniprot.org/annotation/VSP_056134
http://togogenome.org/gene/9606:SPEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4P9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||Disordered|||Essential for homodimerization and microtubule bundling activity|||In isoform 2.|||Sperm flagellar protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079421|||http://purl.uniprot.org/annotation/VSP_017219|||http://purl.uniprot.org/annotation/VSP_017220
http://togogenome.org/gene/9606:SLC4A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5M450|||http://purl.uniprot.org/uniprot/E9PFN4|||http://purl.uniprot.org/uniprot/Q9Y6M7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Band 3 cytoplasmic|||Basic and acidic residues|||Basic residues|||Bicarbonate transporter-like transmembrane|||CA2-binding|||Cytoplasmic|||Disordered|||Essential for cell membrane localization and transport activity|||Extracellular|||Helical|||In isoform 10, isoform 11 and isoform 14.|||In isoform 2, isoform 3, isoform 4, isoform 6, isoform 9, isoform 11, isoform 13 and isoform 14.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5, isoform 6, isoform 7, isoform 8 and isoform 13.|||In isoform 5.|||In isoform 6, isoform 9, isoform 10, isoform 11 and isoform 12.|||In isoform 7, isoform 8, isoform 13 and isoform 14.|||In isoform 8, isoform 10 and isoform 12.|||Loss of cell membrane localization. Significant reduction in transport activity.|||Loss of cell membrane localization. Unable to rescue phagocyte deficient acidification phenotype of SLC4A7 knockout.|||Loss of interaction with ATP6V1B1.|||Loss of interaction with CA2. Loss of regulation by CA2.|||N-linked (GlcNAc...) asparagine|||No effect on cell membrane localization. Unable to rescue phagocyte deficient acidification phenotype of SLC4A7 knockout.|||No effect on interaction with CA2. No effect on regulation by CA2.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sodium bicarbonate cotransporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079233|||http://purl.uniprot.org/annotation/VAR_055317|||http://purl.uniprot.org/annotation/VSP_047838|||http://purl.uniprot.org/annotation/VSP_047839|||http://purl.uniprot.org/annotation/VSP_047840|||http://purl.uniprot.org/annotation/VSP_047841|||http://purl.uniprot.org/annotation/VSP_047842|||http://purl.uniprot.org/annotation/VSP_047843|||http://purl.uniprot.org/annotation/VSP_047844|||http://purl.uniprot.org/annotation/VSP_047845|||http://purl.uniprot.org/annotation/VSP_047846|||http://purl.uniprot.org/annotation/VSP_047847|||http://purl.uniprot.org/annotation/VSP_047848|||http://purl.uniprot.org/annotation/VSP_047849
http://togogenome.org/gene/9606:TRIO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75962                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  30% decrease in nucleotide exchange activity.|||40% decrease in nucleotide exchange activity.|||50% decrease in nucleotide exchange activity.|||80% decrease in nucleotide exchange activity.|||90% decrease in nucleotide exchange activity.|||Basic and acidic residues|||CRAL-TRIO|||DH 1|||DH 2|||Disordered|||Expected to disrupt kinase activity. Causes reorganization of the actin cytoskeleton in the absence of NGF.|||Found in patient with severe intellectual disability; unknown pathological significance.|||Ig-like C2-type|||In MRD44.|||In MRD44; decreased activation of RAC1-mediated signaling; severely decreased neurite outgrowth.|||In MRD44; no effect on RAC1-mediated signaling; no effect on neurite outgrowth.|||In MRD44; severely decreased activation of RAC1-mediated signaling; severely decreased neurite outgrowth.|||In MRD44; unknown pathological significance.|||In MRD63; increased activation of RAC1-mediated signaling; increased neurite outgrowth.|||In MRD63; slightly increased occipitofrontal circumference; increased activation of RAC1-mediated signaling; increased lamellipodia formation.|||In MRD63; slightly increased occipitofrontal circumference; increased activation of RAC1-mediated signaling; increased neurite outgrowth.|||In MRD63; slightly increased occipitofrontal circumference; slightly increased RAC1-mediated signaling; slightly increased neurite outgrowth.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of nucleotide exchange activity.|||No change in nucleotide exchange activity.|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||SH3 1|||SH3 2|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Triple functional domain protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080978|||http://purl.uniprot.org/annotation/VAR_041899|||http://purl.uniprot.org/annotation/VAR_041900|||http://purl.uniprot.org/annotation/VAR_041901|||http://purl.uniprot.org/annotation/VAR_041902|||http://purl.uniprot.org/annotation/VAR_041903|||http://purl.uniprot.org/annotation/VAR_059802|||http://purl.uniprot.org/annotation/VAR_059803|||http://purl.uniprot.org/annotation/VAR_069371|||http://purl.uniprot.org/annotation/VAR_069372|||http://purl.uniprot.org/annotation/VAR_077093|||http://purl.uniprot.org/annotation/VAR_077094|||http://purl.uniprot.org/annotation/VAR_077095|||http://purl.uniprot.org/annotation/VAR_077096|||http://purl.uniprot.org/annotation/VAR_077097|||http://purl.uniprot.org/annotation/VAR_077098|||http://purl.uniprot.org/annotation/VAR_077099|||http://purl.uniprot.org/annotation/VAR_077100|||http://purl.uniprot.org/annotation/VAR_077101|||http://purl.uniprot.org/annotation/VAR_077102|||http://purl.uniprot.org/annotation/VAR_083915|||http://purl.uniprot.org/annotation/VAR_083916|||http://purl.uniprot.org/annotation/VAR_083917|||http://purl.uniprot.org/annotation/VAR_083918|||http://purl.uniprot.org/annotation/VAR_083919|||http://purl.uniprot.org/annotation/VAR_083920|||http://purl.uniprot.org/annotation/VAR_083921|||http://purl.uniprot.org/annotation/VAR_083922|||http://purl.uniprot.org/annotation/VSP_004467|||http://purl.uniprot.org/annotation/VSP_004468|||http://purl.uniprot.org/annotation/VSP_023306|||http://purl.uniprot.org/annotation/VSP_023307|||http://purl.uniprot.org/annotation/VSP_037860|||http://purl.uniprot.org/annotation/VSP_037861|||http://purl.uniprot.org/annotation/VSP_037862
http://togogenome.org/gene/9606:ALOX15B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15296                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes calcium-dependent association with membranes; when associated with A-39 and A-44.|||Abolishes calcium-dependent association with membranes; when associated with A-39 and A-85.|||Abolishes calcium-dependent association with membranes; when associated with A-44 and A-85.|||Changes the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with Y-602.|||Does not affect arachidonate 15-lipoxygenase activity; destabilizes the enzyme structure.|||Does not affect arachidonate 15-lipoxygenase activity; does not impact enzyme structure.|||In isoform B and isoform D.|||In isoform B.|||In isoform C.|||Lipoxygenase|||Loss of 15-lipoxygenase activity.|||No effect on the stereoselectivity of the oxygenation reaction. Completely changes the stereoselectivity of the oxygenation reaction to produce (8S)-HPETE instead of (15S)-HPETE; when associated with H-603.|||PLAT|||Polyunsaturated fatty acid lipoxygenase ALOX15B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220700|||http://purl.uniprot.org/annotation/VAR_024524|||http://purl.uniprot.org/annotation/VAR_024525|||http://purl.uniprot.org/annotation/VAR_061334|||http://purl.uniprot.org/annotation/VAR_083544|||http://purl.uniprot.org/annotation/VSP_003142|||http://purl.uniprot.org/annotation/VSP_003143|||http://purl.uniprot.org/annotation/VSP_003144|||http://purl.uniprot.org/annotation/VSP_003145
http://togogenome.org/gene/9606:SF3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DF2|||http://purl.uniprot.org/uniprot/Q15428                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||Matrin-type|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Pro residues|||Splicing factor 3A subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174315
http://togogenome.org/gene/9606:CALHM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XJ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 3|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186719|||http://purl.uniprot.org/annotation/VAR_081109
http://togogenome.org/gene/9606:GRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z392|||http://purl.uniprot.org/uniprot/P25098                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  50% reduction in phosphorylation of G-protein coupled receptor rhodopsin.|||60% reduction in phosphorylation of G-protein coupled receptor rhodopsin.|||85% reduction in phosphorylation of G-protein coupled receptor rhodopsin.|||95% reduction in phosphorylation of G-protein coupled receptor rhodopsin and beta-2 adrenergic receptor ADRB2. Does not affect binding to ADRB2. Not activated by receptor binding. No effect on phosphorylation of the non-receptor substrate tubulin.|||95% reduction in phosphorylation of G-protein coupled receptor rhodopsin.|||95% reduction in phosphorylation of G-protein coupled receptor rhodopsin. 60% reduction in phosphorylation of beta-2 adrenergic receptor ADRB2. Does not affect binding to ADRB2. Not activated by receptor binding. No effect on phosphorylation of the non-receptor substrate tubulin.|||95% reduction in phosphorylation of G-protein coupled receptor rhodopsin. 90% reduction in phosphorylation of beta-2 adrenergic receptor ADRB2. Does not affect binding to ADRB2. Not activated by receptor binding. No effect on phosphorylation of the non-receptor substrate tubulin.|||AGC-kinase C-terminal|||Beta-adrenergic receptor kinase 1|||In a colorectal adenocarcinoma sample; somatic mutation.|||N-terminal|||PH|||Phosphoserine|||Protein kinase|||Proton acceptor|||RGS|||Required for receptor phosphorylation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085627|||http://purl.uniprot.org/annotation/VAR_040378|||http://purl.uniprot.org/annotation/VAR_040379
http://togogenome.org/gene/9606:SNRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5P5|||http://purl.uniprot.org/uniprot/B4DHM9|||http://purl.uniprot.org/uniprot/E7EUC4|||http://purl.uniprot.org/uniprot/Q9NRH2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||SNF-related serine/threonine-protein kinase|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225605|||http://purl.uniprot.org/annotation/VAR_041096|||http://purl.uniprot.org/annotation/VAR_041097|||http://purl.uniprot.org/annotation/VAR_041098|||http://purl.uniprot.org/annotation/VAR_041099|||http://purl.uniprot.org/annotation/VAR_041100|||http://purl.uniprot.org/annotation/VSP_051959|||http://purl.uniprot.org/annotation/VSP_051960
http://togogenome.org/gene/9606:CHPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUD6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cholinephosphotransferase 1|||Cytoplasmic|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MCF-12A cell line.|||In isoform 2.|||Increases basicity of active site His|||Lumenal|||N-acetylalanine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289252|||http://purl.uniprot.org/annotation/VAR_032612|||http://purl.uniprot.org/annotation/VAR_032613|||http://purl.uniprot.org/annotation/VSP_025989|||http://purl.uniprot.org/annotation/VSP_025990
http://togogenome.org/gene/9606:CHML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26374                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Rab proteins geranylgeranyltransferase component A 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056689
http://togogenome.org/gene/9606:HTR1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28566                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 1E|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068933|||http://purl.uniprot.org/annotation/VAR_014165|||http://purl.uniprot.org/annotation/VAR_022061
http://togogenome.org/gene/9606:DRC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY82                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Dynein regulatory complex subunit 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279434|||http://purl.uniprot.org/annotation/VAR_030898|||http://purl.uniprot.org/annotation/VAR_030899|||http://purl.uniprot.org/annotation/VAR_030900|||http://purl.uniprot.org/annotation/VAR_030901|||http://purl.uniprot.org/annotation/VAR_050738|||http://purl.uniprot.org/annotation/VAR_055286|||http://purl.uniprot.org/annotation/VAR_061580|||http://purl.uniprot.org/annotation/VAR_061581|||http://purl.uniprot.org/annotation/VSP_023438
http://togogenome.org/gene/9606:WSCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TBF2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sialate:O-sulfotransferase 2|||WSC 1|||WSC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305065|||http://purl.uniprot.org/annotation/VAR_035161|||http://purl.uniprot.org/annotation/VSP_028211
http://togogenome.org/gene/9606:PAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7H5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with PINT87aa|||Phosphoserine|||Polar residues|||RNA polymerase II-associated factor 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326400|||http://purl.uniprot.org/annotation/VSP_032650|||http://purl.uniprot.org/annotation/VSP_032651|||http://purl.uniprot.org/annotation/VSP_032652|||http://purl.uniprot.org/annotation/VSP_055740|||http://purl.uniprot.org/annotation/VSP_055741
http://togogenome.org/gene/9606:RAP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61225                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Ras-related protein Rap-2b|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030215|||http://purl.uniprot.org/annotation/PRO_0000030216
http://togogenome.org/gene/9606:NPIPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UND3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear pore complex-interacting protein family member A1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076275|||http://purl.uniprot.org/annotation/VAR_034141
http://togogenome.org/gene/9606:IGSF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95976                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Immunoglobulin superfamily member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000065014|||http://purl.uniprot.org/annotation/VAR_039137|||http://purl.uniprot.org/annotation/VAR_039138|||http://purl.uniprot.org/annotation/VAR_039139
http://togogenome.org/gene/9606:CTXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60606                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Cortexin-1|||Disordered|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079500
http://togogenome.org/gene/9606:IFNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L0N195|||http://purl.uniprot.org/uniprot/P01562                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  In alpha-1B.|||Interferon alpha-1/13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016359|||http://purl.uniprot.org/annotation/PRO_5003946419|||http://purl.uniprot.org/annotation/VAR_013000|||http://purl.uniprot.org/annotation/VAR_024508|||http://purl.uniprot.org/annotation/VAR_025173
http://togogenome.org/gene/9606:HAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14929                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of activity after pulsatile shear stress.|||Histone acetyltransferase type B catalytic subunit|||In a colorectal cancer sample; somatic mutation.|||In isoform B.|||Interaction with histone H4 N-terminus|||N-acetylalanine|||N6-acetyllysine|||No loss of activity after pulsatile shear stress.|||Phosphoserine|||Phosphoserine; by AMPK|||Proton donor/acceptor|||Removed|||Strongly reduces HAT activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083902|||http://purl.uniprot.org/annotation/VAR_035997|||http://purl.uniprot.org/annotation/VSP_041129
http://togogenome.org/gene/9606:SLIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94813                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CTCK|||Cleavage|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7|||In isoform 2 and isoform 3.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRCT 3|||LRRCT 4|||LRRNT|||LRRNT 2|||LRRNT 3|||LRRNT 4|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Slit homolog 2 protein|||Slit homolog 2 protein C-product|||Slit homolog 2 protein N-product                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007725|||http://purl.uniprot.org/annotation/PRO_0000007726|||http://purl.uniprot.org/annotation/PRO_0000007727|||http://purl.uniprot.org/annotation/VAR_018098|||http://purl.uniprot.org/annotation/VAR_018099|||http://purl.uniprot.org/annotation/VSP_050035|||http://purl.uniprot.org/annotation/VSP_050036
http://togogenome.org/gene/9606:KLK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y337                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Disordered|||Kallikrein-5|||Major binding site for inhibitory zinc|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027939|||http://purl.uniprot.org/annotation/VAR_051853|||http://purl.uniprot.org/annotation/VAR_051854
http://togogenome.org/gene/9606:POLR2K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53803                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerases I, II, and III subunit RPABC4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159750
http://togogenome.org/gene/9606:ADARB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J4V7|||http://purl.uniprot.org/uniprot/P78563                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A to I editase|||Basic residues|||DRBM|||DRBM 1|||DRBM 2|||Disordered|||Double-stranded RNA-specific editase 1|||In NEDHYMS; decreased protein stability; strong decreased editing activity.|||In NEDHYMS; unknown pathological significance; altered ratio of alternative splicing.|||In NEDHYMS; unknown pathological significance; mild decreased editing activity.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||Interaction with substrate RNA|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171779|||http://purl.uniprot.org/annotation/VAR_070931|||http://purl.uniprot.org/annotation/VAR_083947|||http://purl.uniprot.org/annotation/VAR_083948|||http://purl.uniprot.org/annotation/VAR_083949|||http://purl.uniprot.org/annotation/VAR_083950|||http://purl.uniprot.org/annotation/VAR_083951|||http://purl.uniprot.org/annotation/VSP_000865|||http://purl.uniprot.org/annotation/VSP_000866|||http://purl.uniprot.org/annotation/VSP_019597|||http://purl.uniprot.org/annotation/VSP_041421
http://togogenome.org/gene/9606:SCAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95104                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CID|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||SR-related and CTD-associated factor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081943|||http://purl.uniprot.org/annotation/VAR_052234|||http://purl.uniprot.org/annotation/VSP_005879|||http://purl.uniprot.org/annotation/VSP_047351
http://togogenome.org/gene/9606:XKR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6D3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Cytoplasmic|||Extracellular|||Helical|||In 2DA; abolished cleavage by CASP3 and ability to promote phosphatidylserine exposure. Does not affect interaction with BSG but prevents homodimerization. Does not affect ability to promote myoblast differentiation.|||Phosphoserine|||Phosphothreonine|||XK-related protein 8|||XK-related protein 8, processed form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190792|||http://purl.uniprot.org/annotation/PRO_0000423984
http://togogenome.org/gene/9606:MAGED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5V3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20; approximate|||21|||22|||22 X 6 AA tandem repeats of W-[PQ]-X-P-X-X|||3|||4|||5|||6|||7|||8|||9|||Disordered|||In isoform 2.|||MAGE|||Melanoma-associated antigen D1|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156723|||http://purl.uniprot.org/annotation/VAR_060070|||http://purl.uniprot.org/annotation/VSP_009286
http://togogenome.org/gene/9606:FAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8JR05|||http://purl.uniprot.org/uniprot/A0A7P0T1I0|||http://purl.uniprot.org/uniprot/B3KU84|||http://purl.uniprot.org/uniprot/Q6V0I7|||http://purl.uniprot.org/uniprot/X2G5I7|||http://purl.uniprot.org/uniprot/X2GA70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 28|||Cadherin 29|||Cadherin 3|||Cadherin 30|||Cadherin 31|||Cadherin 32|||Cadherin 33|||Cadherin 34|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Helical|||In HKLLS2.|||In VMLDS2 and HKLLS2.|||In VMLDS2.|||In isoform 2.|||In isoform 3.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Necessary and sufficient for interaction with MPDZ|||Phosphoserine|||Protocadherin Fat 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324637|||http://purl.uniprot.org/annotation/PRO_5028117789|||http://purl.uniprot.org/annotation/VAR_039860|||http://purl.uniprot.org/annotation/VAR_039861|||http://purl.uniprot.org/annotation/VAR_039862|||http://purl.uniprot.org/annotation/VAR_039863|||http://purl.uniprot.org/annotation/VAR_039864|||http://purl.uniprot.org/annotation/VAR_039865|||http://purl.uniprot.org/annotation/VAR_039866|||http://purl.uniprot.org/annotation/VAR_048580|||http://purl.uniprot.org/annotation/VAR_048581|||http://purl.uniprot.org/annotation/VAR_070925|||http://purl.uniprot.org/annotation/VAR_070926|||http://purl.uniprot.org/annotation/VAR_070927|||http://purl.uniprot.org/annotation/VAR_071948|||http://purl.uniprot.org/annotation/VAR_071949|||http://purl.uniprot.org/annotation/VAR_071950|||http://purl.uniprot.org/annotation/VSP_032334|||http://purl.uniprot.org/annotation/VSP_032335|||http://purl.uniprot.org/annotation/VSP_032336|||http://purl.uniprot.org/annotation/VSP_032337|||http://purl.uniprot.org/annotation/VSP_032338
http://togogenome.org/gene/9606:CDKN1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49918                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 4 AA repeats of P-A-P-A|||Cyclin-dependent kinase inhibitor 1C|||Disordered|||In BWS.|||In BWS; unknown pathological significance.|||In IMAGE.|||In IMAGE; PCNA binding is disrupted.|||In a bladder cancer.|||In a breast cancer.|||In hepatocellular carcinomas.|||In isoform Short.|||In several cancers.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190087|||http://purl.uniprot.org/annotation/VAR_001404|||http://purl.uniprot.org/annotation/VAR_001405|||http://purl.uniprot.org/annotation/VAR_001406|||http://purl.uniprot.org/annotation/VAR_001407|||http://purl.uniprot.org/annotation/VAR_068848|||http://purl.uniprot.org/annotation/VAR_068849|||http://purl.uniprot.org/annotation/VAR_068850|||http://purl.uniprot.org/annotation/VAR_068851|||http://purl.uniprot.org/annotation/VAR_068852|||http://purl.uniprot.org/annotation/VAR_075200|||http://purl.uniprot.org/annotation/VAR_075201|||http://purl.uniprot.org/annotation/VAR_075202|||http://purl.uniprot.org/annotation/VAR_075203|||http://purl.uniprot.org/annotation/VAR_075204|||http://purl.uniprot.org/annotation/VAR_075205|||http://purl.uniprot.org/annotation/VSP_000867
http://togogenome.org/gene/9606:MRNIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NTE8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreases nuclear localization. Reduces nuclear localization and increases DNA damage accumulation and does not affect the association with the MRN complex; when associated with A-141 and A-154.|||Disordered|||Does not affect nuclear localization.|||Does not affect nuclear localization. Decreases weakly the association with the MRN complex. Reduces phosphorylation; when associated with A-115 and A-143.|||In isoform 2.|||In isoform 3.|||MRN complex-interacting protein|||Necessary for the association with the MRN complex|||Nuclear localization signal (NLS)|||Phosphoserine|||Polar residues|||Reduces nuclear localization and increases DNA damage accumulation and does not affect the association with the MRN complex; when associated with 148-A--A-151 and A-154.|||Reduces nuclear localization and increases DNA damage accumulation and does not affect the association with the MRN complex; when associated with A-141 and 148-A--A-151.|||Reduces nuclear localization and increases DNA damage accumulation. Decreases weakly the association with the MRN complex. Reduces phosphorylation; when associated with A-100 and A-143.|||Reduces phosphorylation; when associated with A-100 and A-115.|||Reduces the association with the MRN complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326119|||http://purl.uniprot.org/annotation/VAR_039990|||http://purl.uniprot.org/annotation/VAR_039991|||http://purl.uniprot.org/annotation/VAR_039992|||http://purl.uniprot.org/annotation/VAR_054030|||http://purl.uniprot.org/annotation/VSP_032560|||http://purl.uniprot.org/annotation/VSP_032561|||http://purl.uniprot.org/annotation/VSP_032562|||http://purl.uniprot.org/annotation/VSP_047227
http://togogenome.org/gene/9606:TMEM167B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0V7|||http://purl.uniprot.org/uniprot/Q9NRX6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Protein kish-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265081
http://togogenome.org/gene/9606:PPP2R3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5P8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EF-hand|||In isoform 2.|||Pro residues|||Serine/threonine-protein phosphatase 2A regulatory subunit B" subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071444|||http://purl.uniprot.org/annotation/VAR_035109|||http://purl.uniprot.org/annotation/VAR_055356|||http://purl.uniprot.org/annotation/VSP_037310
http://togogenome.org/gene/9606:ANKK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFD2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and protein kinase domain-containing protein 1|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085620|||http://purl.uniprot.org/annotation/VAR_025010|||http://purl.uniprot.org/annotation/VAR_036784|||http://purl.uniprot.org/annotation/VAR_036785|||http://purl.uniprot.org/annotation/VAR_036786|||http://purl.uniprot.org/annotation/VAR_036787|||http://purl.uniprot.org/annotation/VAR_040359|||http://purl.uniprot.org/annotation/VAR_040360|||http://purl.uniprot.org/annotation/VAR_040361|||http://purl.uniprot.org/annotation/VAR_040362|||http://purl.uniprot.org/annotation/VAR_040363|||http://purl.uniprot.org/annotation/VAR_040364|||http://purl.uniprot.org/annotation/VAR_040365|||http://purl.uniprot.org/annotation/VAR_040366|||http://purl.uniprot.org/annotation/VAR_040367|||http://purl.uniprot.org/annotation/VAR_040368|||http://purl.uniprot.org/annotation/VAR_040369|||http://purl.uniprot.org/annotation/VAR_040370|||http://purl.uniprot.org/annotation/VAR_040371|||http://purl.uniprot.org/annotation/VAR_040372|||http://purl.uniprot.org/annotation/VAR_040373|||http://purl.uniprot.org/annotation/VAR_040374
http://togogenome.org/gene/9606:GOLGA6L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7Z2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 6-like protein 1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326027
http://togogenome.org/gene/9606:RARB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KWP3|||http://purl.uniprot.org/uniprot/F1D8S6|||http://purl.uniprot.org/uniprot/P10826|||http://purl.uniprot.org/uniprot/Q3SB16|||http://purl.uniprot.org/uniprot/Q5QHG3|||http://purl.uniprot.org/uniprot/Q86UC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  As a heterodimer with RXRA, abolishes transcriptional repression on DR1 and reduces transcriptional activation on DR5.|||As a heterodimer with RXRA, abolishes transcriptional repression on DR1, reduces transcriptional activation on DR5 and binding affinity for DR1 and DR5 DNA elements.|||As a heterodimer with RXRA, reduces binding affinity for DR5 DNA element and no change in binding to DR1. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-367. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-120.|||As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces binding affinity for DR1 and DR5 DNA elements; when associated with E-366.|||As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-365 and E-366.|||As a heterodimer with RXRA, reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5. Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-366 and E-367.|||Disordered|||Greatly reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with I-222 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and S-232.|||Hinge|||In MCOPS12; increased transcriptional response to retinoic acid ligands.|||In MCOPS12; increases transcriptional response to retinoic acid.|||In a colorectal cancer sample; somatic mutation.|||In isoform Beta-2.|||In isoform Beta-4.|||Modulating|||NR C4-type|||NR LBD|||No effect on transcriptional activation in the absence of hormone.|||Nuclear receptor|||Phosphoserine|||Polar residues|||Reduced transcriptional activation in the absence of hormone. Even greater reduction in transcriptional activation in the absence of hormone; when associated with D-223 or S-232. Great reduction in transcriptional activation in the absence of hormone; when associated with D-223 and S-232.|||Reduced transcriptional activation in the absence of hormone. Some further reduction of transcriptional activity in the absence of hormone; when associated with I-222 or D-223. Great reduction in transcriptional activation in the absence of hormone; when associated with I-222 and D-223.|||Reduces transcriptional repression on DR1 and reduced transcriptional activation on DR5; when associated with V-123 and E-369.|||Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with E-369 and E-370.|||Reduces transcriptional repression on DR1 and reduces transcriptional activation on DR5; when associated with V-123 and E-370.|||Retinoic acid receptor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053467|||http://purl.uniprot.org/annotation/VAR_036060|||http://purl.uniprot.org/annotation/VAR_070780|||http://purl.uniprot.org/annotation/VAR_070781|||http://purl.uniprot.org/annotation/VAR_077141|||http://purl.uniprot.org/annotation/VAR_077142|||http://purl.uniprot.org/annotation/VSP_003634|||http://purl.uniprot.org/annotation/VSP_003635
http://togogenome.org/gene/9606:NPIPB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Nuclear pore complex-interacting protein family member B13|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343665
http://togogenome.org/gene/9606:BEAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B7T3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||Pro residues|||Protein BEAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322540|||http://purl.uniprot.org/annotation/VSP_031911|||http://purl.uniprot.org/annotation/VSP_046914
http://togogenome.org/gene/9606:MTMR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EF0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases catalytic activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increases catalytic activity.|||Myotubularin phosphatase|||Myotubularin-related protein 8|||Phosphocysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330034|||http://purl.uniprot.org/annotation/VAR_042688|||http://purl.uniprot.org/annotation/VAR_042689|||http://purl.uniprot.org/annotation/VSP_033007
http://togogenome.org/gene/9606:POLR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24928                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||2; approximate|||3|||30|||31|||32|||33|||34|||35|||36|||37|||38|||39|||4|||40|||41|||42|||43|||44|||45|||46|||47|||48|||49|||5|||50|||51; approximate|||52; approximate|||6|||7|||8|||9|||Asymmetric dimethylarginine; alternate; by CARM1|||Bridging helix|||C-terminal domain (CTD); 52 X 7 AA approximate tandem repeats of Y-[ST]-P-[STQ]-[ST]-P-[SRTEVKGN]|||DNA-directed RNA polymerase II subunit RPB1|||Decreases cell viability.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); by NEDD4|||Impairs ubiquitination, interaction with the TFIIH complex, and its degradation during transcription stress.|||In NEDHIB; mild.|||In NEDHIB; mild; decreased cell viability.|||In NEDHIB; mild; unknown pathological significance.|||In NEDHIB; mild; unknown pathological significance; decreased cell viability.|||In NEDHIB; moderate.|||In NEDHIB; moderate; unknown pathological significance.|||In NEDHIB; moderate; unknown pathological significance; no effect on cell viability.|||In NEDHIB; profound; decreased cell viability.|||In NEDHIB; severe; unknown pathological significance.|||In NEDHIB; severe; unknown pathological significance; no effect on cell viability.|||In NEDHIB; unknown pathological significance; no effect on cell viability.|||In isoform 2.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1887; R-1908 and R-1922.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1887; R-1908 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1873; R-1908; R-1922 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1859; R-1866; R-1887; R-1908; R-1922 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1838; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1859; R-1859; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R-1859; R-1866; R-1873; R-1887; R-1908; R-1922 and R-1936.|||Loss of acetylation and loss of regulation of growth-factor-induced gene expression; when associated with R.1838; R-1859; R-1866; R-1873; R-1887; R-1922 and R-1936.|||Misexpression of a variety of small nuclear RNAs and small nucleolar RNAs. Loss of interaction with TDRD3 and SMN1/SMN2.|||N-acetylmethionine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Omega-N-methylated arginine; by CARM1; in vitro|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Symmetric dimethylarginine; alternate; by PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073940|||http://purl.uniprot.org/annotation/VAR_051872|||http://purl.uniprot.org/annotation/VAR_082988|||http://purl.uniprot.org/annotation/VAR_082989|||http://purl.uniprot.org/annotation/VAR_082990|||http://purl.uniprot.org/annotation/VAR_082991|||http://purl.uniprot.org/annotation/VAR_082992|||http://purl.uniprot.org/annotation/VAR_082993|||http://purl.uniprot.org/annotation/VAR_082994|||http://purl.uniprot.org/annotation/VAR_082995|||http://purl.uniprot.org/annotation/VAR_082996|||http://purl.uniprot.org/annotation/VAR_082997|||http://purl.uniprot.org/annotation/VAR_082998|||http://purl.uniprot.org/annotation/VAR_082999|||http://purl.uniprot.org/annotation/VAR_083000|||http://purl.uniprot.org/annotation/VAR_083001|||http://purl.uniprot.org/annotation/VAR_083002|||http://purl.uniprot.org/annotation/VSP_056184|||http://purl.uniprot.org/annotation/VSP_056185
http://togogenome.org/gene/9606:TNKS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2K2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN; partial|||(3S)-3-hydroxyhistidine; by HIF1AN; partial|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||Enhanced hydroxylation by HIF1AN.|||HIF1AN-binding|||Loss of activity.|||PARP catalytic|||Polar residues|||Poly [ADP-ribose] polymerase tankyrase-2|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211334
http://togogenome.org/gene/9606:COIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38432                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  1-1|||1-2|||2 X 4 AA repeats of A-R-N-S|||2 X 4 AA repeats of S-L-P-A|||2-1|||2-2|||3-1|||3-2|||3-3|||3-4|||4 X 2 AA tandem repeats of R-G|||Basic and acidic residues|||Coilin|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired interaction with SMN.|||Phosphoserine|||Phosphoserine; by VRK1 and VRK2|||Phosphothreonine|||Polar residues|||Required for interaction with SMN|||Tudor; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058146
http://togogenome.org/gene/9606:AQP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41181                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MIAC; when associated with A-217.|||Abolishes interaction with MIAC; when associated with A-221.|||Aquaporin-2|||Cytoplasmic|||Discontinuously helical|||Disordered|||Does not affect interaction with MIAC; when associated with A-78.|||Does not affect interaction with MIAC; when associated with A-79.|||Expressed in the apical membrane.|||Extracellular|||Helical|||In NDI2.|||In NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus.|||In NDI2; loss of water channel activity.|||In NDI2; loss of water channel activity; mutant protein does not fold properly.|||In NDI2; mutant protein does not fold properly and is not functional.|||In NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane.|||In NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256.|||In NDI2; retained in the Golgi compartment.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||No effect on expression at the apical cell membrane.|||No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.|||Phosphoserine; by PKA|||Reduces interaction with MIAC.|||Retained in the endoplasmic reticulum.|||Retained in vesicles.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063934|||http://purl.uniprot.org/annotation/VAR_004401|||http://purl.uniprot.org/annotation/VAR_004402|||http://purl.uniprot.org/annotation/VAR_004403|||http://purl.uniprot.org/annotation/VAR_015239|||http://purl.uniprot.org/annotation/VAR_015240|||http://purl.uniprot.org/annotation/VAR_015241|||http://purl.uniprot.org/annotation/VAR_015242|||http://purl.uniprot.org/annotation/VAR_015243|||http://purl.uniprot.org/annotation/VAR_015244|||http://purl.uniprot.org/annotation/VAR_015245|||http://purl.uniprot.org/annotation/VAR_015246|||http://purl.uniprot.org/annotation/VAR_015247|||http://purl.uniprot.org/annotation/VAR_015248|||http://purl.uniprot.org/annotation/VAR_015249|||http://purl.uniprot.org/annotation/VAR_015250|||http://purl.uniprot.org/annotation/VAR_015251|||http://purl.uniprot.org/annotation/VAR_015252|||http://purl.uniprot.org/annotation/VAR_015253|||http://purl.uniprot.org/annotation/VAR_015254|||http://purl.uniprot.org/annotation/VAR_015255|||http://purl.uniprot.org/annotation/VAR_015256|||http://purl.uniprot.org/annotation/VAR_015257|||http://purl.uniprot.org/annotation/VAR_037577|||http://purl.uniprot.org/annotation/VAR_062585|||http://purl.uniprot.org/annotation/VAR_062586|||http://purl.uniprot.org/annotation/VAR_062587|||http://purl.uniprot.org/annotation/VAR_062588|||http://purl.uniprot.org/annotation/VAR_062589|||http://purl.uniprot.org/annotation/VAR_062590|||http://purl.uniprot.org/annotation/VAR_071370
http://togogenome.org/gene/9606:JKAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPC2|||http://purl.uniprot.org/uniprot/G3V2M4|||http://purl.uniprot.org/uniprot/Q9P055                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||JNK1/MAPK8-associated membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089903|||http://purl.uniprot.org/annotation/VSP_060708|||http://purl.uniprot.org/annotation/VSP_060709|||http://purl.uniprot.org/annotation/VSP_060710
http://togogenome.org/gene/9606:CCL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51671|||http://purl.uniprot.org/uniprot/Q6I9T4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine|||Chemokine interleukin-8-like|||Eotaxin|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005195|||http://purl.uniprot.org/annotation/PRO_5014205943|||http://purl.uniprot.org/annotation/VAR_001634|||http://purl.uniprot.org/annotation/VAR_001635|||http://purl.uniprot.org/annotation/VAR_001636|||http://purl.uniprot.org/annotation/VAR_001637|||http://purl.uniprot.org/annotation/VAR_048705
http://togogenome.org/gene/9606:MEST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1L9|||http://purl.uniprot.org/uniprot/B4DQW6|||http://purl.uniprot.org/uniprot/Q5EB52                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Mesoderm-specific transcript homolog protein|||N-linked (GlcNAc...) asparagine|||RVIALD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284418|||http://purl.uniprot.org/annotation/PRO_5014296876|||http://purl.uniprot.org/annotation/VSP_024532|||http://purl.uniprot.org/annotation/VSP_024533
http://togogenome.org/gene/9606:LDLRAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T700                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LDL-receptor class A 1|||LDL-receptor class A 2; atypical|||LDL-receptor class A 3; atypical|||Low-density lipoprotein receptor class A domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299376|||http://purl.uniprot.org/annotation/VSP_027617|||http://purl.uniprot.org/annotation/VSP_027618|||http://purl.uniprot.org/annotation/VSP_054532
http://togogenome.org/gene/9606:RASEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ41                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||Favors GTP association.|||Impairs nucleotide binding and perinuclear localization.|||In isoform 2.|||Phosphoserine|||Polar residues|||Ras and EF-hand domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299577|||http://purl.uniprot.org/annotation/VAR_034858|||http://purl.uniprot.org/annotation/VSP_027766|||http://purl.uniprot.org/annotation/VSP_027767
http://togogenome.org/gene/9606:TMCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFR1|||http://purl.uniprot.org/uniprot/O75069|||http://purl.uniprot.org/uniprot/Q8IW47                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Transmembrane and coiled-coil domains protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184597|||http://purl.uniprot.org/annotation/VSP_046245|||http://purl.uniprot.org/annotation/VSP_058939|||http://purl.uniprot.org/annotation/VSP_058940
http://togogenome.org/gene/9606:EDAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with increase in hair thickness; results in decreased downstream activity of NFKB1 48 hours after transfection into cells.|||Basic and acidic residues|||Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||In ECTD10A and ECTD10B; abolishes NF-kappa-B activation and reduces JNK activation.|||In ECTD10B.|||In ECTD10B; the mutant protein does not interact with EDARADD and is functionally inactive.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reduces activation of NF-kappa-B.|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member EDAR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034608|||http://purl.uniprot.org/annotation/VAR_013448|||http://purl.uniprot.org/annotation/VAR_013449|||http://purl.uniprot.org/annotation/VAR_013450|||http://purl.uniprot.org/annotation/VAR_020011|||http://purl.uniprot.org/annotation/VAR_054444|||http://purl.uniprot.org/annotation/VAR_054445|||http://purl.uniprot.org/annotation/VAR_054446|||http://purl.uniprot.org/annotation/VAR_054447|||http://purl.uniprot.org/annotation/VAR_054448|||http://purl.uniprot.org/annotation/VAR_054449|||http://purl.uniprot.org/annotation/VAR_054450|||http://purl.uniprot.org/annotation/VAR_054451|||http://purl.uniprot.org/annotation/VAR_054452|||http://purl.uniprot.org/annotation/VAR_054453|||http://purl.uniprot.org/annotation/VAR_064830|||http://purl.uniprot.org/annotation/VAR_064831|||http://purl.uniprot.org/annotation/VAR_064832|||http://purl.uniprot.org/annotation/VAR_064833|||http://purl.uniprot.org/annotation/VAR_064834|||http://purl.uniprot.org/annotation/VAR_077562|||http://purl.uniprot.org/annotation/VSP_054187
http://togogenome.org/gene/9606:SGSM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A6J3|||http://purl.uniprot.org/uniprot/O43147                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Loss of GTPase activator activity towards RAB32, RAB33B and RAB38.|||Phosphoserine|||Polar residues|||RUN|||Rab-GAP TBC|||Small G protein signaling modulator 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284662|||http://purl.uniprot.org/annotation/VAR_031795|||http://purl.uniprot.org/annotation/VAR_031796|||http://purl.uniprot.org/annotation/VAR_031797|||http://purl.uniprot.org/annotation/VAR_031798|||http://purl.uniprot.org/annotation/VAR_031799|||http://purl.uniprot.org/annotation/VAR_031800|||http://purl.uniprot.org/annotation/VSP_024594|||http://purl.uniprot.org/annotation/VSP_024595|||http://purl.uniprot.org/annotation/VSP_024596|||http://purl.uniprot.org/annotation/VSP_024597|||http://purl.uniprot.org/annotation/VSP_024598|||http://purl.uniprot.org/annotation/VSP_035964
http://togogenome.org/gene/9606:PEDS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Essential for catalytic activity|||Helical|||Histidine box-1|||Histidine box-2|||In isoform 2.|||Loss of plasmanylethanolamine desaturase activity.|||No effect on desaturase plasmanylethanolamine activity.|||No effect on plasmanylethanolamine desaturase activity.|||Plasmanylethanolamine desaturase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319993|||http://purl.uniprot.org/annotation/VAR_059732|||http://purl.uniprot.org/annotation/VSP_054091
http://togogenome.org/gene/9606:LOXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4K0                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Abolishes oxidase activity and oxidation of trimethylated 'Lys-4' of histone H3 but does not affect secretion, interaction with SNAI1, binding to the CDH1 promoter, repression of CDH1 transcription or ability to induce EMT.|||Does not affect ability to inhibit keratinocyte differentiation.|||Inhibits secretion.|||Loss of enzyme activity.|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog 2|||Lysyl-oxidase like|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018532|||http://purl.uniprot.org/annotation/VAR_024527|||http://purl.uniprot.org/annotation/VAR_050010
http://togogenome.org/gene/9606:PRDM16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 10|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; atypical|||C2H2-type 8|||C2H2-type 9|||Disordered|||Histone-lysine N-methyltransferase PRDM16|||In CMD1LL; unknown pathological significance.|||In LVNC8.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CTBP1, CTBP2 and ZNF516|||Mediates interaction with SKI and regulation of TGF-beta signaling|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047773|||http://purl.uniprot.org/annotation/VAR_031433|||http://purl.uniprot.org/annotation/VAR_031434|||http://purl.uniprot.org/annotation/VAR_070212|||http://purl.uniprot.org/annotation/VAR_070213|||http://purl.uniprot.org/annotation/VAR_070214|||http://purl.uniprot.org/annotation/VAR_070215|||http://purl.uniprot.org/annotation/VAR_070216|||http://purl.uniprot.org/annotation/VSP_006932|||http://purl.uniprot.org/annotation/VSP_038063|||http://purl.uniprot.org/annotation/VSP_038064|||http://purl.uniprot.org/annotation/VSP_038065
http://togogenome.org/gene/9606:PPP1R1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Protein phosphatase 1 regulatory subunit 1C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286443|||http://purl.uniprot.org/annotation/VSP_025061
http://togogenome.org/gene/9606:CLHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHS4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Clathrin heavy chain linker domain-containing protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325870|||http://purl.uniprot.org/annotation/VAR_039944|||http://purl.uniprot.org/annotation/VAR_039945|||http://purl.uniprot.org/annotation/VAR_039946|||http://purl.uniprot.org/annotation/VAR_039947|||http://purl.uniprot.org/annotation/VSP_032461
http://togogenome.org/gene/9606:LGI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0V4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich repeat LGI family member 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017708|||http://purl.uniprot.org/annotation/VAR_030536|||http://purl.uniprot.org/annotation/VAR_030537
http://togogenome.org/gene/9606:BET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15155|||http://purl.uniprot.org/uniprot/Q53XK0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BET1 homolog|||Cytoplasmic|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Phosphoserine|||T-SNARE coiled-coil homology|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206884|||http://purl.uniprot.org/annotation/VSP_056216
http://togogenome.org/gene/9606:NRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWG1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||Extracellular|||Helical; Note=Internal signal sequence|||N-linked (GlcNAc...) asparagine|||Neuregulin-4|||Pro-neuregulin-4, membrane-bound isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019485|||http://purl.uniprot.org/annotation/PRO_0000019486
http://togogenome.org/gene/9606:SPACA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YUZ7|||http://purl.uniprot.org/uniprot/E9PF91|||http://purl.uniprot.org/uniprot/Q05C28|||http://purl.uniprot.org/uniprot/Q8IXA5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lysozyme|||Cleavage; to produce processed form|||Cytoplasmic|||Extracellular|||Glycosyl hydrolases family 22 (GH22)|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Sperm acrosome membrane-associated protein 3, membrane form|||Sperm acrosome membrane-associated protein 3, processed form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256219|||http://purl.uniprot.org/annotation/PRO_0000256220|||http://purl.uniprot.org/annotation/VAR_028885|||http://purl.uniprot.org/annotation/VAR_028886|||http://purl.uniprot.org/annotation/VAR_050008|||http://purl.uniprot.org/annotation/VSP_021329
http://togogenome.org/gene/9606:PRKD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZL6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphorylation. Decreases substrate affinity and increases catalytic efficiency. Increases Ser-706 or/and Ser-710 phosphorylation. Increases NF-kappa-B activation in response to oxidative stress.|||Abolishes phosphorylation. Loss of Tyr-717 phosphorylation and any other tyrosine phosphorylation, and increases NF-kappa-B activation in response to oxidative stress; when associated with A-706.|||Abolishes phosphorylation. Loss of Tyr-717 phosphorylation and any other tyrosine phosphorylation, and increases NF-kappa-B activation in response to oxidative stress; when associated with A-710.|||Constitutive kinase activity; when associated with E-706 and E-710.|||Constitutive kinase activity; when associated with E-706 or with E-244 and E-706. when associated with E-710 or with E-244 and E-710. Increases Tyr-717 phosphorylation; when associated with E-710 or with E-710 and D-438.|||Constitutive kinase activity; when associated with E-710 or with E-244 and E-710. Increases Tyr-717 phosphorylation; when associated with E-710 or with E-710 and D-438.|||Disordered|||Important for ABL1-mediated Tyr-717 phosphorylation|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increase in ability to bind phorbol ester, slight increase in ability to bind DAG.|||Loss of kinase activity.|||Loss of phosphorylation. No effect on phosphorylation of Tyr-717 and on Ser-706 or/and Ser-710 phosphorylation.|||Loss of phosphorylation. No effect on the interaction with PRKCD. No effect on Ser-706 or/and Ser-710 phosphorylation.|||PH|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by CSNK1D and CSNK1E|||Phosphoserine; by PKC|||Phosphoserine; by autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Pro residues|||Protein kinase|||Proton acceptor|||Reduced catalytic activity. Severe reduction in Tyr-717 phosphorylation by ABL1 in response to oxidative stress. No effect on Ser-706 or/and Ser-710 phosphorylation and on NF-kappa-B activation in response to oxidative stress.|||Serine/threonine-protein kinase D2|||Slight increase in Tyr-717 phosphorylation. No effect on Ser-706 or/and Ser-710 phosphorylation. Increase in Tyr-717 phosphorylation; when associated with E-706 and E-710.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055716|||http://purl.uniprot.org/annotation/VAR_042330|||http://purl.uniprot.org/annotation/VAR_042331|||http://purl.uniprot.org/annotation/VAR_042332|||http://purl.uniprot.org/annotation/VAR_042333|||http://purl.uniprot.org/annotation/VAR_042334|||http://purl.uniprot.org/annotation/VAR_042335|||http://purl.uniprot.org/annotation/VAR_061531|||http://purl.uniprot.org/annotation/VSP_057279|||http://purl.uniprot.org/annotation/VSP_059398
http://togogenome.org/gene/9606:ZNF81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51508                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Found in a family with intellectual disability; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 81                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047395|||http://purl.uniprot.org/annotation/VAR_019939|||http://purl.uniprot.org/annotation/VAR_019940|||http://purl.uniprot.org/annotation/VAR_019941|||http://purl.uniprot.org/annotation/VAR_019942|||http://purl.uniprot.org/annotation/VAR_019943|||http://purl.uniprot.org/annotation/VAR_038806|||http://purl.uniprot.org/annotation/VAR_052765
http://togogenome.org/gene/9606:KRTAP26-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PEX3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 26-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223916|||http://purl.uniprot.org/annotation/VAR_053477|||http://purl.uniprot.org/annotation/VAR_053478
http://togogenome.org/gene/9606:IL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60568|||http://purl.uniprot.org/uniprot/Q0GK43                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  In FT-IL2-A and FT-IL2-B.|||In FT-IL2-B.|||Interleukin-2|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000051|||http://purl.uniprot.org/annotation/PRO_0000015484|||http://purl.uniprot.org/annotation/PRO_5014205719|||http://purl.uniprot.org/annotation/VAR_003967|||http://purl.uniprot.org/annotation/VAR_003968
http://togogenome.org/gene/9606:ALG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R5K5|||http://purl.uniprot.org/uniprot/Q9BVK2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In CDG1H.|||In PCLD3.|||In isoform 2.|||Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174162|||http://purl.uniprot.org/annotation/VAR_023480|||http://purl.uniprot.org/annotation/VAR_023481|||http://purl.uniprot.org/annotation/VAR_023482|||http://purl.uniprot.org/annotation/VAR_031596|||http://purl.uniprot.org/annotation/VAR_080918|||http://purl.uniprot.org/annotation/VAR_080919|||http://purl.uniprot.org/annotation/VSP_046291
http://togogenome.org/gene/9606:EFS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43281                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Divergent helix-loop-helix motif|||Embryonal Fyn-associated substrate|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform Efs2 and isoform 3.|||Phosphotyrosine; by SRC|||Pro residues|||SH3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086940|||http://purl.uniprot.org/annotation/VAR_035912|||http://purl.uniprot.org/annotation/VAR_054088|||http://purl.uniprot.org/annotation/VAR_054089|||http://purl.uniprot.org/annotation/VSP_004232|||http://purl.uniprot.org/annotation/VSP_054584
http://togogenome.org/gene/9606:PROZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22891                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||EGF-like 1|||EGF-like 2|||Gla|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Glc...) serine|||Peptidase S1|||Vitamin K-dependent protein Z                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028488|||http://purl.uniprot.org/annotation/PRO_0000028489|||http://purl.uniprot.org/annotation/VAR_013124|||http://purl.uniprot.org/annotation/VAR_013125|||http://purl.uniprot.org/annotation/VSP_005415
http://togogenome.org/gene/9606:ZDHHC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUE0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Palmitoyltransferase ZDHHC18|||Phosphoserine|||Pro residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212902|||http://purl.uniprot.org/annotation/VSP_056000
http://togogenome.org/gene/9606:WDR77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQA1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Methylosome protein WDR77|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051074|||http://purl.uniprot.org/annotation/VAR_042903|||http://purl.uniprot.org/annotation/VSP_056166
http://togogenome.org/gene/9606:EEPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L9B9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Endonuclease/exonuclease/phosphatase family domain-containing protein 1|||HhH|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317261|||http://purl.uniprot.org/annotation/VAR_056867|||http://purl.uniprot.org/annotation/VAR_056868|||http://purl.uniprot.org/annotation/VAR_060374
http://togogenome.org/gene/9606:ENTHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYW4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  ENTH|||ENTH domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312179|||http://purl.uniprot.org/annotation/VAR_037449
http://togogenome.org/gene/9606:CEACAM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLI3|||http://purl.uniprot.org/uniprot/P31997|||http://purl.uniprot.org/uniprot/Q0Z7S6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 8|||Does not affect the monomeric structure. Decreases heterodimerization with CEACAM6.|||Does not affect the monomeric structure. Loss of heterodimerization with CEACAM6.|||GPI-anchor amidated aspartate|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||Inhibits heterophilic cell adhesion.|||N-linked (GlcNAc...) asparagine|||No effect on heterophilic cell adhesion.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014572|||http://purl.uniprot.org/annotation/PRO_0000014573|||http://purl.uniprot.org/annotation/PRO_5002800897|||http://purl.uniprot.org/annotation/PRO_5014306893|||http://purl.uniprot.org/annotation/VAR_011721|||http://purl.uniprot.org/annotation/VAR_049849|||http://purl.uniprot.org/annotation/VAR_049850|||http://purl.uniprot.org/annotation/VAR_049851|||http://purl.uniprot.org/annotation/VAR_049852
http://togogenome.org/gene/9606:BCLAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2AJT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BCLAF1 and THRAP3 family member 3|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287434|||http://purl.uniprot.org/annotation/VSP_025458|||http://purl.uniprot.org/annotation/VSP_025459
http://togogenome.org/gene/9606:RHOBTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYZ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB 1|||BTB 2|||Disordered|||In DEE64.|||In DEE64; also found in a patient with Rett syndrome-like phenotype.|||In DEE64; decreased proteasomal degradation; does not affect interaction with CUL3.|||In DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3.|||In isoform 2.|||In isoform 3.|||Results in decreased interaction with CUL3.|||Rho-like|||Rho-related BTB domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198962|||http://purl.uniprot.org/annotation/VAR_079030|||http://purl.uniprot.org/annotation/VAR_080812|||http://purl.uniprot.org/annotation/VAR_080813|||http://purl.uniprot.org/annotation/VAR_080814|||http://purl.uniprot.org/annotation/VAR_080815|||http://purl.uniprot.org/annotation/VAR_080816|||http://purl.uniprot.org/annotation/VSP_054098|||http://purl.uniprot.org/annotation/VSP_054099
http://togogenome.org/gene/9606:ODAD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Outer dynein arm-docking complex subunit 4|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284507|||http://purl.uniprot.org/annotation/VAR_031758|||http://purl.uniprot.org/annotation/VAR_031759|||http://purl.uniprot.org/annotation/VSP_024548|||http://purl.uniprot.org/annotation/VSP_024549
http://togogenome.org/gene/9606:USP17L27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:FAM9C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Protein FAM9C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119034
http://togogenome.org/gene/9606:PAQR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXW6|||http://purl.uniprot.org/uniprot/Q8TEZ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Membrane progestin receptor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218840
http://togogenome.org/gene/9606:CSE1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKW7|||http://purl.uniprot.org/uniprot/P55060                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Exportin-2|||Importin N-terminal|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117287|||http://purl.uniprot.org/annotation/VAR_029327|||http://purl.uniprot.org/annotation/VAR_036558|||http://purl.uniprot.org/annotation/VAR_048836|||http://purl.uniprot.org/annotation/VSP_001222|||http://purl.uniprot.org/annotation/VSP_001223|||http://purl.uniprot.org/annotation/VSP_001224|||http://purl.uniprot.org/annotation/VSP_001225|||http://purl.uniprot.org/annotation/VSP_047203
http://togogenome.org/gene/9606:NME4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVT9|||http://purl.uniprot.org/uniprot/O00746                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Abolishes cardiolipin-containing membrane binding; decreases lipid transfer and pro-apoptotic activity; does not change phosphotransfer activity.|||In isoform 2.|||Mitochondrion|||Nucleoside diphosphate kinase, mitochondrial|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019432|||http://purl.uniprot.org/annotation/VSP_054743
http://togogenome.org/gene/9606:NAA25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CX7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-alpha-acetyltransferase 25, NatB auxiliary subunit|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294337|||http://purl.uniprot.org/annotation/VAR_033156|||http://purl.uniprot.org/annotation/VAR_035872|||http://purl.uniprot.org/annotation/VAR_054099|||http://purl.uniprot.org/annotation/VAR_054100|||http://purl.uniprot.org/annotation/VSP_026629|||http://purl.uniprot.org/annotation/VSP_026630
http://togogenome.org/gene/9606:MSTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14793|||http://purl.uniprot.org/uniprot/Q53S46                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage|||Decreases SMAD3 protein signal transduction; when associated with L-268.|||Decreases SMAD3 protein signal transduction; when associated with N-267.|||Growth/differentiation factor 8|||Increases SMAD3 protein signal transduction.|||Increases SMAD3 protein signal transduction; when associated with D-355.|||Increases SMAD3 protein signal transduction; when associated with M-316 and M-318.|||Increases SMAD3 protein signal transduction; when associated with Q-357.|||Increases SMAD3 protein signal transduction; when associated with Y-315 and M-316.|||Increases SMAD3 protein signal transduction; when associated with Y-315 and M-318.|||Interchain|||N-linked (GlcNAc...) asparagine|||Slightly decreased SMAD3 protein signal transduction.|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033950|||http://purl.uniprot.org/annotation/PRO_0000033951|||http://purl.uniprot.org/annotation/PRO_5014309552|||http://purl.uniprot.org/annotation/VAR_014475|||http://purl.uniprot.org/annotation/VAR_014476|||http://purl.uniprot.org/annotation/VAR_052575|||http://purl.uniprot.org/annotation/VAR_052576
http://togogenome.org/gene/9606:TNFSF12-TNFSF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YY99|||http://purl.uniprot.org/uniprot/O43508                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform TWE-PRIL.|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 12, membrane form|||Tumor necrosis factor ligand superfamily member 12, secreted form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034520|||http://purl.uniprot.org/annotation/PRO_0000034521|||http://purl.uniprot.org/annotation/VSP_045245
http://togogenome.org/gene/9606:AK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylate kinase isoenzyme 6|||In isoform 2.|||Induces homodimerization. Reduces adenylate kinase activity by 72% and ATPase activity by 76%. Significantly changes Cajal body organization in the nucleus, resulting in enhanced apoptosis and reduced proliferation.|||LID|||NMP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153896|||http://purl.uniprot.org/annotation/VSP_039714
http://togogenome.org/gene/9606:SENP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMM0|||http://purl.uniprot.org/uniprot/F8W6D9|||http://purl.uniprot.org/uniprot/Q9GZR1                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protease|||Sentrin-specific protease 6|||Ubiquitin-like protease family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101725|||http://purl.uniprot.org/annotation/VAR_016096|||http://purl.uniprot.org/annotation/VAR_029653|||http://purl.uniprot.org/annotation/VAR_029654|||http://purl.uniprot.org/annotation/VAR_029655|||http://purl.uniprot.org/annotation/VAR_051545|||http://purl.uniprot.org/annotation/VSP_005274
http://togogenome.org/gene/9606:MALRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYJ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||Helical|||LDL-receptor class A 1|||LDL-receptor class A 10|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class A 9|||MAM 1|||MAM 2|||MAM 3|||MAM 4|||MAM 5|||MAM 6|||MAM 7|||MAM 8|||MAM 9|||MAM and LDL-receptor class A domain-containing protein 1|||N-linked (GlcNAc...) asparagine|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328968|||http://purl.uniprot.org/annotation/VAR_042585|||http://purl.uniprot.org/annotation/VAR_042586|||http://purl.uniprot.org/annotation/VAR_042587|||http://purl.uniprot.org/annotation/VAR_042588|||http://purl.uniprot.org/annotation/VAR_042589|||http://purl.uniprot.org/annotation/VAR_042590|||http://purl.uniprot.org/annotation/VAR_042592|||http://purl.uniprot.org/annotation/VAR_042594|||http://purl.uniprot.org/annotation/VAR_042595|||http://purl.uniprot.org/annotation/VAR_042596|||http://purl.uniprot.org/annotation/VAR_042597|||http://purl.uniprot.org/annotation/VAR_042598|||http://purl.uniprot.org/annotation/VAR_042599|||http://purl.uniprot.org/annotation/VAR_075928|||http://purl.uniprot.org/annotation/VAR_075929|||http://purl.uniprot.org/annotation/VAR_075930
http://togogenome.org/gene/9606:SYCE1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MT33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region                                                                                  ^@                                                                                  Disordered|||Synaptonemal complex central element protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341221
http://togogenome.org/gene/9606:SAV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTQ1|||http://purl.uniprot.org/uniprot/Q9H4B6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  In a colon cancer cell line.|||Phosphoserine|||Phosphothreonine|||Protein salvador homolog 1|||SARAH|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076060|||http://purl.uniprot.org/annotation/VAR_015880
http://togogenome.org/gene/9606:ATAD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QE3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 5|||Abolishes RB1 binding. Abolishes RB1 binding; when associated with K-1432. Weakly detected after methyl methane-sulfonate (MMS) treatment. Expression detected after MMS treatment; when associated with K-1432. Weakly affects the RAD9A interaction after MMS exposure. No effect on the RAD9A interaction after MMS exposure; when associated with K-1432. Resists to DNA damage after MMS exposure; when associated with K-1432.|||Abolishes RB1 binding; when associated with G-1430. Expression detected after methyl methane-sulfonate (MMS) treatment; when associated with G-1430. No effect on the RAD9A interaction after MMS exposure; when associated with G-1430. Resists to DNA damage after MMS exposure; when associated with G-1430.|||Abolishes interaction with WDR48 and recruitment of RAD51 at site of stalled replication forks under replication stress. Reduces down-regulation of PCNA monoubiquitination but retains the ability to unload PCNA from chromatin.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with RAD51 and RFC5|||Interaction with WDR48|||LXCXE motif|||Loss of interaction with RAD51 and loading of RAD51 to stalled replication forks during replication stress. Loss of processing of stalled replication forks. Retains PCNA-unloading ability.|||No effect on the RAD9A interaction after MMS exposure. Resists to DNA damage after MMS exposure.|||Phosphoserine|||Polar residues|||Pro residues|||Results in defective PCNA removal from chromatin and recruitment of RAD51 at site of stalled replication forks under replication stress. Loss of processing of stalled replication forks. Retains interaction with PCNA and RFC4.|||Weakly affects the RAD9A interaction after MMS exposure.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317618|||http://purl.uniprot.org/annotation/VAR_038572|||http://purl.uniprot.org/annotation/VAR_038573|||http://purl.uniprot.org/annotation/VAR_038574|||http://purl.uniprot.org/annotation/VAR_038575|||http://purl.uniprot.org/annotation/VAR_038576|||http://purl.uniprot.org/annotation/VAR_038577|||http://purl.uniprot.org/annotation/VAR_079496|||http://purl.uniprot.org/annotation/VSP_031097
http://togogenome.org/gene/9606:C16orf82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHF3|||http://purl.uniprot.org/uniprot/Q7Z2V1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein TNT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072616
http://togogenome.org/gene/9606:GARNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH81|||http://purl.uniprot.org/uniprot/Q5VVW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CNH|||Disordered|||GTPase-activating Rap/Ran-GAP domain-like protein 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312215|||http://purl.uniprot.org/annotation/VAR_037456|||http://purl.uniprot.org/annotation/VAR_037457|||http://purl.uniprot.org/annotation/VSP_029740|||http://purl.uniprot.org/annotation/VSP_029741|||http://purl.uniprot.org/annotation/VSP_029742|||http://purl.uniprot.org/annotation/VSP_029743|||http://purl.uniprot.org/annotation/VSP_029744|||http://purl.uniprot.org/annotation/VSP_029745|||http://purl.uniprot.org/annotation/VSP_054875
http://togogenome.org/gene/9606:LRRC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N386                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||Leucine-rich repeat-containing protein 25|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021613|||http://purl.uniprot.org/annotation/VAR_051109|||http://purl.uniprot.org/annotation/VAR_061677
http://togogenome.org/gene/9606:PRDX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPQ2|||http://purl.uniprot.org/uniprot/Q06830                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  87% reduction in enzymatic activity.|||Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity.|||Basic and acidic residues|||Cysteine sulfenic acid (-SOH) intermediate|||Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interchain (with C-173); in linked form|||Interchain (with C-52); in linked form|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Peroxiredoxin-1|||Phosphoserine|||Phosphothreonine; by CDK1|||Removed|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135076|||http://purl.uniprot.org/annotation/VAR_025050
http://togogenome.org/gene/9606:ALDH4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30038                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial|||In HYRPRO2; allele ALDH4A1*3; loss of enzyme activity.|||In allele ALDH4A1*4.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Phosphoserine|||Proton acceptor|||Reduced affinity for NAD. No effect on enzyme activity.|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007173|||http://purl.uniprot.org/annotation/VAR_002259|||http://purl.uniprot.org/annotation/VAR_002260|||http://purl.uniprot.org/annotation/VAR_029337|||http://purl.uniprot.org/annotation/VAR_048903|||http://purl.uniprot.org/annotation/VSP_043785|||http://purl.uniprot.org/annotation/VSP_047732
http://togogenome.org/gene/9606:SNRPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08579                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a colorectal cancer sample; somatic mutation.|||N6-acetyllysine; alternate|||Phosphotyrosine|||Polar residues|||RRM 1|||RRM 2|||U2 small nuclear ribonucleoprotein B""" /id="PRO_0000081892                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/VAR_035487
http://togogenome.org/gene/9606:PPP3CB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z781|||http://purl.uniprot.org/uniprot/P16298                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||Does not affect catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Increases basal catalytic activity. Does not affect interaction with PPP3R1/calreticulin B and calmodulin.|||Increases catalytic activity independently of calmodulin. Does not affect interaction with PPP3R1/calreticulin B and calmodulin.|||Increases catalytic activity independently of calmodulin. Loss of interaction with calmodulin. Does not affect interaction with PPP3R1/calreticulin B.|||Increases catalytic efficiency towards NFATC1 and DARPP32 but not towards a peptide substrate. Does not affect cytoplasmic localization and activation by calmodulin.|||Loss of catalytic activity. Loss of interaction with PPP3R1/calreticulin B and calmodulin.|||Moderate loss of calmodulin-mediated activation. Probably prevents recognition of substrates.|||Modest increase in catalytic activity in absence of calmodulin.|||Modest increase in catalytic activity in absence of calmodulin. Does not affect interaction with calmodulin.|||N-acetylalanine|||Phosphoserine|||Proton donor|||Reduction of basal catalytic activity in absence of calmodulin.|||Removed|||SAPNY motif|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform|||Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates.|||Severe reduction of basal catalytic activity in absence of calmodulin. Severe loss of calmodulin-mediated activation. Probably prevents recognition of substrates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058825|||http://purl.uniprot.org/annotation/VSP_005096|||http://purl.uniprot.org/annotation/VSP_005097|||http://purl.uniprot.org/annotation/VSP_012617|||http://purl.uniprot.org/annotation/VSP_043803
http://togogenome.org/gene/9606:GK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG0|||http://purl.uniprot.org/uniprot/Q14410                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate kinase FGGY C-terminal|||Carbohydrate kinase FGGY N-terminal|||Glycerol kinase 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059536
http://togogenome.org/gene/9606:FAM234A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein FAM234A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247993|||http://purl.uniprot.org/annotation/VSP_020121|||http://purl.uniprot.org/annotation/VSP_020122
http://togogenome.org/gene/9606:MFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes GTP binding and GTPase activity. Loss of function in mitochondrial fusion.|||Abolishes GTPase activity. Abolishes dimerization.|||Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding.|||Acts as a dominant negative mutant; induces fragmentation of mitochondria.|||Causes mitochondrial clumping.|||Cytoplasmic|||Decreases GTPase activity and impairs mitochondrial fusion.|||Decreases GTPase activity.|||Decreases GTPase activity. Abolishes dimerization. Impairs mitochondrial fusion.|||Decreases GTPase activity. Impairs mitochondrial fusion.|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Helical; Name=1|||Helical; Name=2|||Impairs protein folding.|||Impairs protein folding. Decreases GTPase activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Induces a strong decrease in mitochondrial clustering.|||Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding.|||Loss of function in mitochondrial fusion. Abolishes dimerization. Decreases GTPase activity.|||Mildly decreases GTPase activity and impairs mitochondrial fusion.|||Mildly decreases GTPase activity.|||Mitochondrial intermembrane|||Mitofusin-1|||Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions|||Slightly decreases GTPase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127672|||http://purl.uniprot.org/annotation/VAR_018606|||http://purl.uniprot.org/annotation/VAR_036115|||http://purl.uniprot.org/annotation/VSP_010362|||http://purl.uniprot.org/annotation/VSP_010363|||http://purl.uniprot.org/annotation/VSP_010364
http://togogenome.org/gene/9606:TBC1D5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A6K1|||http://purl.uniprot.org/uniprot/Q92609                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes retromer displacement from endosome membrane; no effect on interaction with VPS29; when associated with A-169.|||Abolishes retromer displacement from endosome membrane; no effect on interaction with VPS29; when associated with A-204.|||Arginine finger|||Disordered|||Disrupts interaction with VPS29.|||Glutamine finger|||In isoform 2.|||LIR 1|||LIR 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-GAP TBC|||Required for interaction with ATG8 family proteins|||Required for interaction with retromer; involved in interaction with ATG8 family proteins|||TBC1 domain family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208028|||http://purl.uniprot.org/annotation/VAR_052536|||http://purl.uniprot.org/annotation/VSP_045039
http://togogenome.org/gene/9606:AARSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTE6                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Alanyl-tRNA editing protein Aarsd1|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277465|||http://purl.uniprot.org/annotation/VSP_023014|||http://purl.uniprot.org/annotation/VSP_043142
http://togogenome.org/gene/9606:RCCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NED2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  (3R)-3-hydroxyarginine|||Abolishes hydroxylation by KDM8.|||Interaction with KDM8|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337973|||http://purl.uniprot.org/annotation/VAR_043727
http://togogenome.org/gene/9606:DUSP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05923                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 2|||Loss of tyrosine phosphatase activity.|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094793
http://togogenome.org/gene/9606:NUDT19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXV4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Acyl-coenzyme A diphosphatase NUDT19|||Disordered|||Important for coenzyme A binding|||Microbody targeting signal|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324571|||http://purl.uniprot.org/annotation/VAR_039831
http://togogenome.org/gene/9606:MLYCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95822                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  110-fold reduction in catalytic activity.|||2-fold reduction in catalytic activity.|||3.5-fold reduction in catalytic activity.|||7-fold reduction in catalytic activity.|||Abolishes formation of disulfide-linked homotetramers. Abolishes the cooperative enzyme kinetics that are seen under oxidative conditions.|||Alpha-helical domain|||Catalytic domain|||Decreases catalytic activity. Increases affinity for malonyl-CoA.|||Does not abolish formation of disulfide-linked homotetramers. No effect on development of cooperative enzyme kinetics in response to oxidative conditions.|||Essential for catalytic activity|||In isoform Cytoplasmic+peroxisomal.|||Interchain|||Malonyl-CoA decarboxylase, mitochondrial|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021088|||http://purl.uniprot.org/annotation/VSP_047649
http://togogenome.org/gene/9606:ZFP62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Zinc finger protein 62 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047305|||http://purl.uniprot.org/annotation/VAR_064881|||http://purl.uniprot.org/annotation/VAR_064882|||http://purl.uniprot.org/annotation/VSP_010136|||http://purl.uniprot.org/annotation/VSP_045257
http://togogenome.org/gene/9606:P2RX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99571                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not change ATP-induced inward current. Does not change affinity for ATP.|||Does not change ATP-induced inward current; does not change affinity for ATP.|||Does not change protein expression; does not affect membrane subcellular location; increases ATP-induced inward current.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In isoform 2.|||In isoform 3.|||May influence susceptibility to multiple sclerosis in the presence of variants M-205 and S-361 in P2RX7; does not affect membrane subcellular location; reduces ATP-induced inward current; decreases affinity for ATP.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161553|||http://purl.uniprot.org/annotation/VAR_014942|||http://purl.uniprot.org/annotation/VAR_028307|||http://purl.uniprot.org/annotation/VAR_079856|||http://purl.uniprot.org/annotation/VAR_079857|||http://purl.uniprot.org/annotation/VAR_079858|||http://purl.uniprot.org/annotation/VSP_053812|||http://purl.uniprot.org/annotation/VSP_053813
http://togogenome.org/gene/9606:SQOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6N5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cysteine persulfide intermediate|||In SQORD; severely decreased sulfide:quinone oxidoreductase activity; severely reduced protein levels in patient cells.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Sulfide:quinone oxidoreductase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022408|||http://purl.uniprot.org/annotation/VAR_014959|||http://purl.uniprot.org/annotation/VAR_085241
http://togogenome.org/gene/9606:TMOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYL9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Phosphoserine|||Tropomodulin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186134
http://togogenome.org/gene/9606:CPSF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGF8|||http://purl.uniprot.org/uniprot/Q8N684                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Arg/Ser-rich domain|||Basic and acidic residues|||Cleavage and polyadenylation specificity factor subunit 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081527|||http://purl.uniprot.org/annotation/VSP_017194|||http://purl.uniprot.org/annotation/VSP_038975
http://togogenome.org/gene/9606:TTYH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H313                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein tweety homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312239|||http://purl.uniprot.org/annotation/VSP_029753|||http://purl.uniprot.org/annotation/VSP_029754|||http://purl.uniprot.org/annotation/VSP_029755|||http://purl.uniprot.org/annotation/VSP_029756|||http://purl.uniprot.org/annotation/VSP_029757|||http://purl.uniprot.org/annotation/VSP_029758|||http://purl.uniprot.org/annotation/VSP_029759|||http://purl.uniprot.org/annotation/VSP_029760
http://togogenome.org/gene/9606:AP1G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75843|||http://purl.uniprot.org/uniprot/Q86U03|||http://purl.uniprot.org/uniprot/Q86V28                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-1 complex subunit gamma-like 2|||Disordered|||Essential for ubiquitin-binding|||GAE|||Greatly diminishes interaction with ubiquitin; when associated with G-369.|||Greatly diminishes interaction with ubiquitin; when associated with G-372.|||Greatly diminishes interaction with ubiquitin; when associated with G-376.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193760|||http://purl.uniprot.org/annotation/VAR_024363
http://togogenome.org/gene/9606:PCDHGC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR81|||http://purl.uniprot.org/uniprot/Q9UN70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin C-terminal catenin-binding|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003985|||http://purl.uniprot.org/annotation/VSP_008698|||http://purl.uniprot.org/annotation/VSP_008699
http://togogenome.org/gene/9606:ZNF26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17031|||http://purl.uniprot.org/uniprot/V9HW07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047355
http://togogenome.org/gene/9606:KLHL29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BTB|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 29|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119086|||http://purl.uniprot.org/annotation/VSP_010403
http://togogenome.org/gene/9606:KCNJ10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78508                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||INTRAMEM|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 10|||Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In SESAMES.|||In SESAMES; important loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, does not form functional channels.|||In SESAMES; loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, does not form functional channels.|||In SESAMES; loss of localization to the basolateral membrane in kidney cells; in non-tubular cells, forms functional channels; important loss of MAGI1-binding when transfected in tubular MDCKII cells, but not in non-tubular HEK293T cells.|||In SESAMES; no effect on localization to the basolateral membrane in kidney cells.|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154953|||http://purl.uniprot.org/annotation/VAR_020339|||http://purl.uniprot.org/annotation/VAR_034018|||http://purl.uniprot.org/annotation/VAR_063059|||http://purl.uniprot.org/annotation/VAR_063060|||http://purl.uniprot.org/annotation/VAR_063061|||http://purl.uniprot.org/annotation/VAR_063062|||http://purl.uniprot.org/annotation/VAR_063063|||http://purl.uniprot.org/annotation/VAR_063064|||http://purl.uniprot.org/annotation/VAR_072746|||http://purl.uniprot.org/annotation/VAR_072747
http://togogenome.org/gene/9606:DNAJC25-GNG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1X3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 25|||Helical|||In isoform 2.|||In isoform 3.|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348569|||http://purl.uniprot.org/annotation/VSP_035180|||http://purl.uniprot.org/annotation/VSP_035181|||http://purl.uniprot.org/annotation/VSP_035182
http://togogenome.org/gene/9606:BRAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJG6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BRCA1-associated ATM activator 1|||Disordered|||HEAT 1|||HEAT 2|||In NEDCAS and RMFSL; unknown pathological significance.|||In NEDCAS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Required for interaction with NDFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255257|||http://purl.uniprot.org/annotation/VAR_031202|||http://purl.uniprot.org/annotation/VAR_061594|||http://purl.uniprot.org/annotation/VAR_081168|||http://purl.uniprot.org/annotation/VAR_081169|||http://purl.uniprot.org/annotation/VAR_081170|||http://purl.uniprot.org/annotation/VSP_021288|||http://purl.uniprot.org/annotation/VSP_021289|||http://purl.uniprot.org/annotation/VSP_021290|||http://purl.uniprot.org/annotation/VSP_021291
http://togogenome.org/gene/9606:LMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PK83|||http://purl.uniprot.org/uniprot/P25800                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Rhombotin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075894|||http://purl.uniprot.org/annotation/VSP_046664
http://togogenome.org/gene/9606:RNASEH2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDP1                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In AGS3.|||N-acetylmethionine|||Phosphoserine|||Ribonuclease H2 subunit C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248385|||http://purl.uniprot.org/annotation/VAR_027287|||http://purl.uniprot.org/annotation/VAR_027288|||http://purl.uniprot.org/annotation/VAR_070618|||http://purl.uniprot.org/annotation/VAR_070619|||http://purl.uniprot.org/annotation/VAR_070620|||http://purl.uniprot.org/annotation/VAR_070621|||http://purl.uniprot.org/annotation/VAR_070622
http://togogenome.org/gene/9606:RSRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arginine/serine-rich protein 1|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||No effect on interaction with spliceosome factors.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Reduces interaction with spliceosome factors.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297617|||http://purl.uniprot.org/annotation/VAR_034655|||http://purl.uniprot.org/annotation/VAR_034656|||http://purl.uniprot.org/annotation/VSP_027305|||http://purl.uniprot.org/annotation/VSP_027306|||http://purl.uniprot.org/annotation/VSP_027307
http://togogenome.org/gene/9606:TK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ES52|||http://purl.uniprot.org/uniprot/P04183                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  30-fold higher KM for thymidine.|||300-fold higher KM for thymidine.|||50-fold higher KM for thymidine.|||KEN box|||Loss of phosphorylation. Constant expression during cell cycle. No effect on ATP-induced tetramerization.|||N-acetylserine|||No effect on phosphorylation.|||Perturbes ATP-induced tetramerization. Retaines the enzymatic function with decreased thymidine affinity and catalytic efficiency.|||Phosphoserine|||Proton acceptor|||Removed|||Resistant to degradation in the mitotic exit phase.|||Thymidine kinase, cytosolic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174948
http://togogenome.org/gene/9606:MPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DW50|||http://purl.uniprot.org/uniprot/F5GX71|||http://purl.uniprot.org/uniprot/H3BPB8|||http://purl.uniprot.org/uniprot/H3BPP3|||http://purl.uniprot.org/uniprot/P34949|||http://purl.uniprot.org/uniprot/Q8NHZ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In CDG1B.|||In isoform 2.|||Mannose-6-phosphate isomerase|||N-acetylalanine|||Phosphomannose isomerase type I C-terminal|||Phosphomannose isomerase type I catalytic|||Phosphomannose isomerase type I helical insertion|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194235|||http://purl.uniprot.org/annotation/VAR_012338|||http://purl.uniprot.org/annotation/VAR_012339|||http://purl.uniprot.org/annotation/VAR_012340|||http://purl.uniprot.org/annotation/VAR_012345|||http://purl.uniprot.org/annotation/VAR_022516|||http://purl.uniprot.org/annotation/VAR_022517|||http://purl.uniprot.org/annotation/VAR_022518|||http://purl.uniprot.org/annotation/VAR_022519|||http://purl.uniprot.org/annotation/VAR_022520|||http://purl.uniprot.org/annotation/VAR_022521|||http://purl.uniprot.org/annotation/VAR_022522|||http://purl.uniprot.org/annotation/VAR_022523|||http://purl.uniprot.org/annotation/VAR_022524|||http://purl.uniprot.org/annotation/VSP_013357
http://togogenome.org/gene/9606:AMMECR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4V0|||http://purl.uniprot.org/uniprot/A0A0S2Z4X0|||http://purl.uniprot.org/uniprot/Q9Y4X0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMMECR1|||Disordered|||In MFHIEN; creates a novel nonuniform expression pattern in the nucleus.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear protein AMMECR1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142366|||http://purl.uniprot.org/annotation/VAR_078027|||http://purl.uniprot.org/annotation/VSP_008516|||http://purl.uniprot.org/annotation/VSP_017058|||http://purl.uniprot.org/annotation/VSP_044229
http://togogenome.org/gene/9606:ROPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAT0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interaction with RHPN1|||Phosphoserine|||RIIa|||Ropporin-1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307392|||http://purl.uniprot.org/annotation/VSP_028743|||http://purl.uniprot.org/annotation/VSP_028744
http://togogenome.org/gene/9606:BTBD18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein 18|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394237|||http://purl.uniprot.org/annotation/VAR_063155|||http://purl.uniprot.org/annotation/VAR_063156
http://togogenome.org/gene/9606:SPSB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJ21                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  B30.2/SPRY|||Disordered|||SOCS box|||SPRY domain-containing SOCS box protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278778|||http://purl.uniprot.org/annotation/VAR_052034
http://togogenome.org/gene/9606:GRM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5P7|||http://purl.uniprot.org/uniprot/P41594                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased constitutive signaling activity.|||Disordered|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 1.|||In isoform 3.|||Increased constitutive signaling activity.|||Metabotropic glutamate receptor 5|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012932|||http://purl.uniprot.org/annotation/PRO_5002725515|||http://purl.uniprot.org/annotation/VSP_002030|||http://purl.uniprot.org/annotation/VSP_047710
http://togogenome.org/gene/9606:USP22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPT9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Impairs its function as a positive modulator of androgen receptor transactivation; when associated with A-471.|||Impairs its function as a positive modulator of androgen receptor transactivation; when associated with A-479.|||In isoform 2.|||N6-acetyllysine|||Nucleophile|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080650|||http://purl.uniprot.org/annotation/VSP_036720
http://togogenome.org/gene/9606:ABCD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28288                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 3|||Abolishes localization to peroxisomes.|||Decreased ATP-binding affinity.|||Decreased ATPase activity.|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093309|||http://purl.uniprot.org/annotation/VAR_000091|||http://purl.uniprot.org/annotation/VSP_031187|||http://purl.uniprot.org/annotation/VSP_031188|||http://purl.uniprot.org/annotation/VSP_031189
http://togogenome.org/gene/9606:FBXO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AF1|||http://purl.uniprot.org/uniprot/Q9UK99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||ApaG|||Disordered|||F-box|||F-box only protein 3|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119877|||http://purl.uniprot.org/annotation/VAR_049037|||http://purl.uniprot.org/annotation/VSP_024395|||http://purl.uniprot.org/annotation/VSP_024396|||http://purl.uniprot.org/annotation/VSP_039614
http://togogenome.org/gene/9606:SKA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BD8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes microtubule binding; when associated with A-155 and A-236.|||Abolishes microtubule binding; when associated with A-155 and A-245.|||Abolishes microtubule binding; when associated with A-236 and A-245.|||Basic and acidic residues|||Disordered|||In isoform 2.|||Microtubule binding|||N-acetylalanine|||Phosphomimetic mutant which strongly reduces microtubule binding; when associated with D-185.|||Phosphomimetic mutant which strongly reduces microtubule binding; when associated with D-242.|||Removed|||Spindle and kinetochore-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273155|||http://purl.uniprot.org/annotation/VAR_030091|||http://purl.uniprot.org/annotation/VSP_037250
http://togogenome.org/gene/9606:FIGNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMB9|||http://purl.uniprot.org/uniprot/Q6ZP58                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fidgetin-like protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343702|||http://purl.uniprot.org/annotation/VAR_044425
http://togogenome.org/gene/9606:PRDM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gains the ability to sequentially mono-, di-, and tri-methylate both 'Lys-4' and 'Lys-36' of histone H3, albeit with lower efficiency when compared to PRDM9.|||Histone-lysine N-methyltransferase PRDM7|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||KRAB-related|||Polar residues|||SET|||Substantially increases histone-lysine N-methyltransferase activity. Gains the catalytic competency of PRDM9. Sequentially mono-, di-, and tri-methylates both 'Lys-4' and 'Lys-36' of histone H3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047763|||http://purl.uniprot.org/annotation/VAR_057461|||http://purl.uniprot.org/annotation/VAR_057462|||http://purl.uniprot.org/annotation/VAR_057463|||http://purl.uniprot.org/annotation/VSP_006930|||http://purl.uniprot.org/annotation/VSP_006931|||http://purl.uniprot.org/annotation/VSP_036349|||http://purl.uniprot.org/annotation/VSP_036350
http://togogenome.org/gene/9606:CDC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISD2|||http://purl.uniprot.org/uniprot/B2RCW0|||http://purl.uniprot.org/uniprot/Q13042                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell division cycle protein 16 homolog|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||TPR|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106267|||http://purl.uniprot.org/annotation/VSP_008427|||http://purl.uniprot.org/annotation/VSP_008428|||http://purl.uniprot.org/annotation/VSP_057270
http://togogenome.org/gene/9606:H3-3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4P9|||http://purl.uniprot.org/uniprot/P84243                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolished serotonylation by TGM2.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H2A/H2B/H3|||Histone H3.3|||In BRYLIB1 and BRYLIB2.|||In BRYLIB1 and BRYLIB2; unknown pathological significance.|||In BRYLIB1.|||In BRYLIB1; decreased protein abundance.|||In BRYLIB1; unknown pathological significance.|||In BRYLIB1; unknown pathological significance; decreased protein abundance; increased interaction with DAXX; not changed subcellular location.|||In BRYLIB1; unknown pathological significance; increased protein abundance.|||In BRYLIB1; unknown pathological significance; no effect on protein abundance.|||In BRYLIB2.|||In BRYLIB2; unknown pathological significance.|||In BRYLIB2; unknown pathological significance; decreased protein abundance.|||In BRYLIB2; unknown pathological significance; no effect on protein abundance.|||In GLM and BRYLIB2; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels.|||In GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels.|||In GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels.|||Interaction with ZMYND11|||Loss of interaction with DNAJC9, but not with other histone chaperones, such as ASF1A, MCCM2, NASP or SPT2.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||Probable disease-associated variant found in chondroblastoma and clear cell chondrosarcoma; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in giant cell tumors of bone; somatic mutation.|||Reduced binding of histone H1 to histone H3.3-containing nucleosomes.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221247|||http://purl.uniprot.org/annotation/VAR_079021|||http://purl.uniprot.org/annotation/VAR_079022|||http://purl.uniprot.org/annotation/VAR_079023|||http://purl.uniprot.org/annotation/VAR_079024|||http://purl.uniprot.org/annotation/VAR_079025|||http://purl.uniprot.org/annotation/VAR_087155|||http://purl.uniprot.org/annotation/VAR_087156|||http://purl.uniprot.org/annotation/VAR_087157|||http://purl.uniprot.org/annotation/VAR_087158|||http://purl.uniprot.org/annotation/VAR_087159|||http://purl.uniprot.org/annotation/VAR_087160|||http://purl.uniprot.org/annotation/VAR_087161|||http://purl.uniprot.org/annotation/VAR_087162|||http://purl.uniprot.org/annotation/VAR_087163|||http://purl.uniprot.org/annotation/VAR_087164|||http://purl.uniprot.org/annotation/VAR_087165|||http://purl.uniprot.org/annotation/VAR_087166|||http://purl.uniprot.org/annotation/VAR_087167|||http://purl.uniprot.org/annotation/VAR_087168|||http://purl.uniprot.org/annotation/VAR_087169|||http://purl.uniprot.org/annotation/VAR_087170|||http://purl.uniprot.org/annotation/VAR_087171|||http://purl.uniprot.org/annotation/VAR_087172|||http://purl.uniprot.org/annotation/VAR_087173|||http://purl.uniprot.org/annotation/VAR_087174|||http://purl.uniprot.org/annotation/VAR_087175|||http://purl.uniprot.org/annotation/VAR_087176|||http://purl.uniprot.org/annotation/VAR_087177|||http://purl.uniprot.org/annotation/VAR_087178|||http://purl.uniprot.org/annotation/VAR_087179|||http://purl.uniprot.org/annotation/VAR_087180|||http://purl.uniprot.org/annotation/VAR_087181|||http://purl.uniprot.org/annotation/VAR_087182|||http://purl.uniprot.org/annotation/VAR_087183|||http://purl.uniprot.org/annotation/VAR_087184|||http://purl.uniprot.org/annotation/VAR_087185|||http://purl.uniprot.org/annotation/VAR_087186|||http://purl.uniprot.org/annotation/VAR_087187|||http://purl.uniprot.org/annotation/VAR_087188|||http://purl.uniprot.org/annotation/VAR_087189|||http://purl.uniprot.org/annotation/VAR_087190|||http://purl.uniprot.org/annotation/VAR_087191|||http://purl.uniprot.org/annotation/VAR_087192|||http://purl.uniprot.org/annotation/VAR_087193
http://togogenome.org/gene/9606:TAFA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5A9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chemokine-like protein TAFA-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042721
http://togogenome.org/gene/9606:CYP20A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW02                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 20A1|||Helical|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318095|||http://purl.uniprot.org/annotation/VAR_059153|||http://purl.uniprot.org/annotation/VAR_059154|||http://purl.uniprot.org/annotation/VSP_055585
http://togogenome.org/gene/9606:PIGW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7B1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In GPIBD11; no effect on protein abundance; loss of function in GPI-anchored protein transport.|||In GPIBD11; reduced protein abundance; decreased function in GPI-anchored protein transport.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylinositol-glycan biosynthesis class W protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246282|||http://purl.uniprot.org/annotation/VAR_071933|||http://purl.uniprot.org/annotation/VAR_071934
http://togogenome.org/gene/9606:SMPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0T6|||http://purl.uniprot.org/uniprot/Q9NY59                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Region|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Endonuclease/exonuclease/phosphatase|||Helical|||Important for substrate recognition|||In isoform 2.|||Phosphoserine|||Polar residues|||Proton acceptor|||S-palmitoyl cysteine|||Sphingomyelin phosphodiesterase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075692|||http://purl.uniprot.org/annotation/VSP_054334
http://togogenome.org/gene/9606:RELL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUW5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||RELT-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323590
http://togogenome.org/gene/9606:EGR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH80|||http://purl.uniprot.org/uniprot/Q06889                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Early growth response protein 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047125|||http://purl.uniprot.org/annotation/VSP_045954
http://togogenome.org/gene/9606:ZNF43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSW2|||http://purl.uniprot.org/uniprot/P17038                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047376|||http://purl.uniprot.org/annotation/VAR_035569|||http://purl.uniprot.org/annotation/VAR_054794|||http://purl.uniprot.org/annotation/VSP_036734
http://togogenome.org/gene/9606:CA5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2D0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Transit Peptide                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 5B, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004237
http://togogenome.org/gene/9606:SUMO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EEV6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Propeptide|||Sequence Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Small ubiquitin-related modifier 4|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042710|||http://purl.uniprot.org/annotation/PRO_0000042711|||http://purl.uniprot.org/annotation/VAR_023740
http://togogenome.org/gene/9606:PSMB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49720                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylserine|||N6-acetyllysine|||Proteasome subunit beta type-3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148057|||http://purl.uniprot.org/annotation/VAR_034415
http://togogenome.org/gene/9606:CXCL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80162                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  C-X-C motif chemokine 6|||Small-inducible cytokine B6, N-processed variant 1|||Small-inducible cytokine B6, N-processed variant 2|||Small-inducible cytokine B6, N-processed variant 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005084|||http://purl.uniprot.org/annotation/PRO_0000005085|||http://purl.uniprot.org/annotation/PRO_0000005086|||http://purl.uniprot.org/annotation/PRO_0000005087
http://togogenome.org/gene/9606:NUPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NF83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Nuclear protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346768
http://togogenome.org/gene/9606:KHDC3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q587J8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes DNA double-strand break repair. Reduces the localization of the homologous recombination DNA repair pathway protein RAD51 to sites of DNA double-strand breaks. May exhibit a dominant negative effect on PARP1 activation, homologous recombination repair and ATM-CHK2 signaling. No effect on restart of stalled replication forks, nascent DNA stability, localization to DNA double-strand break repair sites or interaction with PARP1.|||Basic and acidic residues|||Decreases recruitment of RAD51 to DNA double-strand breaks, PARP1 activity and ATM-CHK2 signaling resulting in a decrease in DNA double-strand break repair.|||Disordered|||In HYDM2; unknown pathological significance.|||Involved in RNA binding|||KH domain-containing protein 3|||KH; atypical|||No effect on recruitment of RAD51 to DNA double-strand breaks, PARP1 activity, ATM-CHK2 signaling or DNA double-strand break repair.|||Phosphoserine|||Phosphothreonine; by ATM|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311967|||http://purl.uniprot.org/annotation/VAR_054052|||http://purl.uniprot.org/annotation/VAR_054053|||http://purl.uniprot.org/annotation/VAR_085059
http://togogenome.org/gene/9606:ENTPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5L3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  7% of wild-type ATPase activity, accumulates intracellularly.|||Abolishes ecto-ATPase activity, accumulates intracellularly.|||Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 2|||Extracellular|||Helical|||In isoform Short and isoform gamma.|||In isoform gamma.|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209906|||http://purl.uniprot.org/annotation/VAR_050307|||http://purl.uniprot.org/annotation/VSP_003610|||http://purl.uniprot.org/annotation/VSP_053548
http://togogenome.org/gene/9606:ZNF667                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5CZB4|||http://purl.uniprot.org/uniprot/Q5HYK9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 667                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251897|||http://purl.uniprot.org/annotation/VAR_027716|||http://purl.uniprot.org/annotation/VAR_027717|||http://purl.uniprot.org/annotation/VAR_047330
http://togogenome.org/gene/9606:MED18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUE0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Mediator of RNA polymerase II transcription subunit 18|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304742
http://togogenome.org/gene/9606:FKBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00688                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||N6-acetyllysine|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP3|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075307
http://togogenome.org/gene/9606:CFAP97D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RV13                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Sperm axonemal maintenance protein CFAP97D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392549
http://togogenome.org/gene/9606:HOXA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31267                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200067
http://togogenome.org/gene/9606:PCYOX1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBM8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prenylcysteine oxidase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280286|||http://purl.uniprot.org/annotation/VAR_031110|||http://purl.uniprot.org/annotation/VAR_031111|||http://purl.uniprot.org/annotation/VAR_050472|||http://purl.uniprot.org/annotation/VSP_039271|||http://purl.uniprot.org/annotation/VSP_039272
http://togogenome.org/gene/9606:LY6E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16553                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Abolishes inhibition of human coronaviruses entry.|||About 50% loss of viral entry enhancement.|||Complete loss of viral entry enhancement. Abolishes inhibition of human coronaviruses entry.|||GPI-anchor amidated serine|||Lymphocyte antigen 6E|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036138|||http://purl.uniprot.org/annotation/PRO_0000036139
http://togogenome.org/gene/9606:KCNK18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z418                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Interaction with YWHAH|||Interaction with calcineurin|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Phosphoserine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 18|||Restores sensitivity to extracellular protons.|||Strongly reduced current amplitude and localization to cell membrane. Strongly reduced current amplitude and localization to cell membrane; when associated with Q-70.|||Strongly reduced current amplitude and localization to cell membrane. Strongly reduced current amplitude and localization to cell membrane; when associated with Q-96.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312500|||http://purl.uniprot.org/annotation/VAR_037521|||http://purl.uniprot.org/annotation/VAR_037522|||http://purl.uniprot.org/annotation/VAR_037523|||http://purl.uniprot.org/annotation/VAR_037524|||http://purl.uniprot.org/annotation/VAR_037525|||http://purl.uniprot.org/annotation/VAR_037526|||http://purl.uniprot.org/annotation/VAR_064027
http://togogenome.org/gene/9606:SMCHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHR9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase activity domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BAMS and FSHD2; no change in protein abundance; strongly increased ATPase activity.|||In BAMS; has an increased ATPase activity.|||In BAMS; has an increased ATPase activity; no change in protein abundance.|||In BAMS; increased ATPase activity.|||In BAMS; no change in protein abundance.|||In BAMS; no change in protein abundance; does not affect ATPase activity.|||In BAMS; no change in protein abundance; slightly decreased ATPase activity.|||In BAMS; slightly decreased ATPase activity.|||In FSHD2.|||In FSHD2; abolished ATPase activity.|||In FSHD2; decreased ATPase activity.|||In FSHD2; decreased protein level in fibroblasts as compared to wild-type protein.|||In FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; abolished ATPase activity.|||In FSHD2; decreased protein level in fibroblasts as compared to wild-type protein; decreased ATPase activity.|||In FSHD2; does not affect ATPase activity.|||In FSHD2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||SMC hinge|||Structural maintenance of chromosomes flexible hinge domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332144|||http://purl.uniprot.org/annotation/VAR_042959|||http://purl.uniprot.org/annotation/VAR_042960|||http://purl.uniprot.org/annotation/VAR_051365|||http://purl.uniprot.org/annotation/VAR_069067|||http://purl.uniprot.org/annotation/VAR_069068|||http://purl.uniprot.org/annotation/VAR_069069|||http://purl.uniprot.org/annotation/VAR_069070|||http://purl.uniprot.org/annotation/VAR_069071|||http://purl.uniprot.org/annotation/VAR_069072|||http://purl.uniprot.org/annotation/VAR_078869|||http://purl.uniprot.org/annotation/VAR_078870|||http://purl.uniprot.org/annotation/VAR_078871|||http://purl.uniprot.org/annotation/VAR_078872|||http://purl.uniprot.org/annotation/VAR_078873|||http://purl.uniprot.org/annotation/VAR_078874|||http://purl.uniprot.org/annotation/VAR_078875|||http://purl.uniprot.org/annotation/VAR_078876|||http://purl.uniprot.org/annotation/VAR_078877|||http://purl.uniprot.org/annotation/VAR_078878|||http://purl.uniprot.org/annotation/VAR_078879|||http://purl.uniprot.org/annotation/VAR_078880|||http://purl.uniprot.org/annotation/VAR_078881|||http://purl.uniprot.org/annotation/VAR_078882|||http://purl.uniprot.org/annotation/VAR_078883|||http://purl.uniprot.org/annotation/VAR_078884|||http://purl.uniprot.org/annotation/VAR_078885|||http://purl.uniprot.org/annotation/VAR_078886|||http://purl.uniprot.org/annotation/VAR_078887|||http://purl.uniprot.org/annotation/VAR_078888|||http://purl.uniprot.org/annotation/VAR_078889|||http://purl.uniprot.org/annotation/VAR_078890|||http://purl.uniprot.org/annotation/VAR_078891|||http://purl.uniprot.org/annotation/VAR_078892|||http://purl.uniprot.org/annotation/VAR_078893|||http://purl.uniprot.org/annotation/VAR_078894|||http://purl.uniprot.org/annotation/VAR_078895|||http://purl.uniprot.org/annotation/VAR_078896|||http://purl.uniprot.org/annotation/VAR_078897|||http://purl.uniprot.org/annotation/VAR_078898|||http://purl.uniprot.org/annotation/VAR_078899|||http://purl.uniprot.org/annotation/VAR_078900|||http://purl.uniprot.org/annotation/VAR_078901|||http://purl.uniprot.org/annotation/VAR_078902|||http://purl.uniprot.org/annotation/VAR_078903|||http://purl.uniprot.org/annotation/VAR_078904|||http://purl.uniprot.org/annotation/VAR_078905|||http://purl.uniprot.org/annotation/VAR_078906|||http://purl.uniprot.org/annotation/VAR_078907|||http://purl.uniprot.org/annotation/VAR_078908|||http://purl.uniprot.org/annotation/VAR_078909|||http://purl.uniprot.org/annotation/VAR_080698|||http://purl.uniprot.org/annotation/VAR_080699|||http://purl.uniprot.org/annotation/VAR_080700|||http://purl.uniprot.org/annotation/VAR_080701|||http://purl.uniprot.org/annotation/VAR_080702|||http://purl.uniprot.org/annotation/VAR_080703|||http://purl.uniprot.org/annotation/VAR_080704|||http://purl.uniprot.org/annotation/VAR_080705|||http://purl.uniprot.org/annotation/VAR_080706|||http://purl.uniprot.org/annotation/VSP_033344|||http://purl.uniprot.org/annotation/VSP_033345|||http://purl.uniprot.org/annotation/VSP_033346|||http://purl.uniprot.org/annotation/VSP_033347|||http://purl.uniprot.org/annotation/VSP_033348
http://togogenome.org/gene/9606:CHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT33|||http://purl.uniprot.org/uniprot/O14646                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 5 AA repeats of H-S-D-H-R|||Abolishes DNA-binding.|||Basic and acidic residues|||Basic residues|||CHD1 helical C-terminal domain (CHCT)|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 1|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In PILBOS.|||In PILBOS; patient cells show a global increase of methylated histone binding.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080224|||http://purl.uniprot.org/annotation/VAR_055652|||http://purl.uniprot.org/annotation/VAR_080265|||http://purl.uniprot.org/annotation/VAR_080266|||http://purl.uniprot.org/annotation/VAR_080267|||http://purl.uniprot.org/annotation/VAR_080268|||http://purl.uniprot.org/annotation/VSP_038432
http://togogenome.org/gene/9606:LOC107985149                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNW8                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TMEM87A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BTS6|||http://purl.uniprot.org/uniprot/Q8NBN3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduced mechanosensitive channel activity in Tmem87a-expressing cells.|||Transmembrane protein 87A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270751|||http://purl.uniprot.org/annotation/PRO_5039375050|||http://purl.uniprot.org/annotation/VSP_022207|||http://purl.uniprot.org/annotation/VSP_022208|||http://purl.uniprot.org/annotation/VSP_022209
http://togogenome.org/gene/9606:RASGRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV61                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||Ras guanyl-releasing protein 3|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068883|||http://purl.uniprot.org/annotation/VAR_051901|||http://purl.uniprot.org/annotation/VSP_047371
http://togogenome.org/gene/9606:ACTMAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BKX5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Actin maturation protease|||Catalytically inactive, disrupts N-terminal cleavage of immature actin.|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Peptidase C39-like|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297659|||http://purl.uniprot.org/annotation/VSP_039884|||http://purl.uniprot.org/annotation/VSP_039885
http://togogenome.org/gene/9606:SAMD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZD0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250563|||http://purl.uniprot.org/annotation/VSP_020659
http://togogenome.org/gene/9606:C9orf85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MD7                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Removed|||Uncharacterized protein C9orf85                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089720|||http://purl.uniprot.org/annotation/VSP_014428|||http://purl.uniprot.org/annotation/VSP_014429|||http://purl.uniprot.org/annotation/VSP_014430
http://togogenome.org/gene/9606:NUP133                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUM0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In NPHS18; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus.|||In NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus.|||In NPHS18; loss of function in nephrogenesis; unable to rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP107.|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||N6-acetyllysine|||Nuclear pore complex protein Nup133|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204838|||http://purl.uniprot.org/annotation/VAR_030829|||http://purl.uniprot.org/annotation/VAR_030830|||http://purl.uniprot.org/annotation/VAR_030831|||http://purl.uniprot.org/annotation/VAR_035854|||http://purl.uniprot.org/annotation/VAR_035855|||http://purl.uniprot.org/annotation/VAR_081359|||http://purl.uniprot.org/annotation/VAR_081360|||http://purl.uniprot.org/annotation/VAR_081361
http://togogenome.org/gene/9606:RETREG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR51|||http://purl.uniprot.org/uniprot/Q8NC44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with ATG8 family proteins, induction of ER fragmentation and ER degradation.|||Disordered|||Helical|||LIR motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reticulophagy regulator 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089346|||http://purl.uniprot.org/annotation/PRO_5002788432|||http://purl.uniprot.org/annotation/VAR_022835|||http://purl.uniprot.org/annotation/VAR_033720
http://togogenome.org/gene/9606:APOBEC3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRW3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Required for interaction with human foamy virus protein Bet|||CMP/dCMP-type deaminase|||DNA dC->dU-editing enzyme APOBEC-3C|||No effect on Vif binding.|||Proton donor|||Remains sensitive to HIV-1 Vif but abolishes Vif binding.|||Resistant to HIV-1 Vif and abolishes Vif binding.|||Resistant to HIV-1 Vif and reduces Vif binding.|||Resistant to HIV-1 Vif.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171755
http://togogenome.org/gene/9606:AZI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6S1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  5-azacytidine-induced protein 2|||Homodimerization|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with TBK1 and IKBKE|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280602|||http://purl.uniprot.org/annotation/VSP_023817|||http://purl.uniprot.org/annotation/VSP_023818|||http://purl.uniprot.org/annotation/VSP_047087|||http://purl.uniprot.org/annotation/VSP_047088|||http://purl.uniprot.org/annotation/VSP_047089|||http://purl.uniprot.org/annotation/VSP_047090
http://togogenome.org/gene/9606:HCRTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43614|||http://purl.uniprot.org/uniprot/S4X0W3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes response to orexin-A.|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for responses to orexin|||N-linked (GlcNAc...) asparagine|||Orexin receptor type 2|||Required for response to orexin-A|||Strongly impairs response to orexin-A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069989|||http://purl.uniprot.org/annotation/VAR_044507|||http://purl.uniprot.org/annotation/VAR_044508|||http://purl.uniprot.org/annotation/VAR_044509|||http://purl.uniprot.org/annotation/VAR_044510
http://togogenome.org/gene/9606:CYB561                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTA1|||http://purl.uniprot.org/uniprot/J3QRH5|||http://purl.uniprot.org/uniprot/P49447                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b561|||Cytoplasmic|||Helical|||In ORTHYP2.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Transmembrane ascorbate-dependent reductase CYB561|||Vesicular|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000151027|||http://purl.uniprot.org/annotation/VAR_081730|||http://purl.uniprot.org/annotation/VAR_081731|||http://purl.uniprot.org/annotation/VSP_056950
http://togogenome.org/gene/9606:URI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94763                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Does not lead to dissociation of the URI1-PPP1CC complex. Enhances phosphorylation of RPS6KB1 after IGF1 stimulation. Confers a cell survival increase.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Phosphothreonine|||Polar residues|||Pro residues|||Unconventional prefoldin RPB5 interactor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097365|||http://purl.uniprot.org/annotation/VAR_056978|||http://purl.uniprot.org/annotation/VSP_032773|||http://purl.uniprot.org/annotation/VSP_042259|||http://purl.uniprot.org/annotation/VSP_044769|||http://purl.uniprot.org/annotation/VSP_044770
http://togogenome.org/gene/9606:DNAJB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNN2|||http://purl.uniprot.org/uniprot/Q9UDY4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Chaperone DnaJ C-terminal|||DnaJ homolog subfamily B member 4|||J|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071021
http://togogenome.org/gene/9606:ARRDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B67                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolishes interaction with ADRB2; when associated with E-48; E-52 and E-139.|||Abolishes interaction with ADRB2; when associated with E-48; E-52 and E-85.|||Abolishes interaction with ADRB2; when associated with E-48; E-85 and E-139.|||Abolishes interaction with ADRB2; when associated with E-52; E-85 and E-139.|||Abolishes interaction with NEDD4; when associated with 346-A--A-349.|||Arrestin domain-containing protein 3|||Disordered|||Nearly abolishes interaction with ADRB2; when associated with E-56; E-135 and E-153.|||Nearly abolishes interaction with ADRB2; when associated with E-56; E-58 and E-135.|||Nearly abolishes interaction with ADRB2; when associated with E-56; E-58 and E-153.|||Nearly abolishes interaction with ADRB2; when associated with E-58; E-135 and E-153.|||PPxY motif 1|||PPxY motif 2|||Strongly reduces interaction with NEDD4. Abolishes interaction with NEDD4; when associated with 391-A--A-394. Abolishes interaction with HGS; when associated with 391-A--A-394.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244349
http://togogenome.org/gene/9606:METTL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95568                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protein-L-histidine N-tele-methyltransferase activity.|||Basic and acidic residues|||Decreased localization to the nucleus.|||Disordered|||Histidine protein methyltransferase 1 homolog|||Loss of protein-L-histidine N-tele-methyltransferase activity.|||No effect on automethylation. Loss of protein-L-histidine N-tele-methyltransferase activity toward RPL3.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Tele-methylhistidine; by autocatalysis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247199|||http://purl.uniprot.org/annotation/VAR_027087|||http://purl.uniprot.org/annotation/VAR_027088|||http://purl.uniprot.org/annotation/VAR_027089|||http://purl.uniprot.org/annotation/VAR_054050|||http://purl.uniprot.org/annotation/VAR_054051
http://togogenome.org/gene/9606:MTX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYI7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Metaxin-3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337100|||http://purl.uniprot.org/annotation/VAR_043600|||http://purl.uniprot.org/annotation/VSP_033893|||http://purl.uniprot.org/annotation/VSP_033894|||http://purl.uniprot.org/annotation/VSP_036207|||http://purl.uniprot.org/annotation/VSP_036208|||http://purl.uniprot.org/annotation/VSP_046824
http://togogenome.org/gene/9606:HMX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein HMX3|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341382
http://togogenome.org/gene/9606:UBE2E3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969T4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||Loss of activity.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 E3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082474|||http://purl.uniprot.org/annotation/VAR_023392
http://togogenome.org/gene/9606:FKBPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIM3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes HSP90AB1 binding; when associated with A-287.|||Abolishes HSP90AB1 binding; when associated with A-291.|||Disordered|||FK506-binding protein-like|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289878|||http://purl.uniprot.org/annotation/VAR_061546
http://togogenome.org/gene/9606:ETV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41162                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ETS|||ETS translocation variant 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204114|||http://purl.uniprot.org/annotation/VSP_013351|||http://purl.uniprot.org/annotation/VSP_013352
http://togogenome.org/gene/9606:SLC13A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF27|||http://purl.uniprot.org/uniprot/Q8WWT9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In ARLIAK; severely decreased transport of succinate, 2-oxoglutarate and N-acetylaspartate.|||In ARLIAK; unable to transport succinate, 2-oxoglutarate and N-acetylaspartate.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Na(+)/dicarboxylate cotransporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000172492|||http://purl.uniprot.org/annotation/VAR_082121|||http://purl.uniprot.org/annotation/VAR_082122|||http://purl.uniprot.org/annotation/VSP_006123|||http://purl.uniprot.org/annotation/VSP_006124|||http://purl.uniprot.org/annotation/VSP_015291|||http://purl.uniprot.org/annotation/VSP_015292|||http://purl.uniprot.org/annotation/VSP_015293|||http://purl.uniprot.org/annotation/VSP_015294|||http://purl.uniprot.org/annotation/VSP_015295
http://togogenome.org/gene/9606:ITPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DER3|||http://purl.uniprot.org/uniprot/B4DGH1|||http://purl.uniprot.org/uniprot/Q14643|||http://purl.uniprot.org/uniprot/Q59H91                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with AHCYL1.|||Basic and acidic residues|||Creates a dileucine motif and recruits clathrin.|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In GLSP.|||In GLSP; alters calcium release of isoform 3.|||In SCA15.|||In SCA29.|||In isoform 2, isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4, isoform 5 and isoform 8.|||In isoform 3, isoform 4, isoform 6, isoform 7 and isoform 8.|||Inositol 1,4,5-trisphosphate receptor type 1|||Interaction with ERP44|||Ion transport|||Lumenal|||MIR|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||N-linked (GlcNAc...) asparagine|||No effect on interaction with AHCYL1.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RyR/IP3R Homology associated|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153920|||http://purl.uniprot.org/annotation/VAR_037005|||http://purl.uniprot.org/annotation/VAR_037006|||http://purl.uniprot.org/annotation/VAR_069567|||http://purl.uniprot.org/annotation/VAR_069569|||http://purl.uniprot.org/annotation/VAR_077462|||http://purl.uniprot.org/annotation/VAR_077463|||http://purl.uniprot.org/annotation/VAR_077464|||http://purl.uniprot.org/annotation/VAR_077465|||http://purl.uniprot.org/annotation/VAR_081167|||http://purl.uniprot.org/annotation/VSP_002687|||http://purl.uniprot.org/annotation/VSP_002688|||http://purl.uniprot.org/annotation/VSP_002689|||http://purl.uniprot.org/annotation/VSP_002690
http://togogenome.org/gene/9606:PNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H307                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with CTBP1 and shows moderate relief of CTBP1-mediated repression.|||Abolishes interaction with KRT18.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Necessary for interaction with PPIG|||Necessary for interaction with RNPS1|||Necessary for interactions with KRT8, KRT18 and KRT19|||Necessary for mediating alternative 5' splicing|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pinin|||Polar residues|||Removed|||Sufficient for PSAP complex assembly                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190242|||http://purl.uniprot.org/annotation/VAR_023368
http://togogenome.org/gene/9606:TMEM14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6G1                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 14A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221169|||http://purl.uniprot.org/annotation/VAR_052497
http://togogenome.org/gene/9606:RNLS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJW3|||http://purl.uniprot.org/uniprot/Q5VYX0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amine oxidase|||In isoform 2.|||Renalase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019588|||http://purl.uniprot.org/annotation/VAR_023310|||http://purl.uniprot.org/annotation/VSP_015211|||http://purl.uniprot.org/annotation/VSP_015212
http://togogenome.org/gene/9606:ERICH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P6B1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glutamate-rich protein 5|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294433|||http://purl.uniprot.org/annotation/VAR_033176|||http://purl.uniprot.org/annotation/VAR_033177|||http://purl.uniprot.org/annotation/VAR_033178|||http://purl.uniprot.org/annotation/VSP_046650
http://togogenome.org/gene/9606:CCDC191                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCU4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 191|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309221|||http://purl.uniprot.org/annotation/VAR_036913|||http://purl.uniprot.org/annotation/VAR_036914|||http://purl.uniprot.org/annotation/VSP_057041|||http://purl.uniprot.org/annotation/VSP_057042|||http://purl.uniprot.org/annotation/VSP_057043
http://togogenome.org/gene/9606:MED12L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXY0|||http://purl.uniprot.org/uniprot/Q86YW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In NIZIDS.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Mediator of RNA polymerase II transcription subunit 12-like protein|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313053|||http://purl.uniprot.org/annotation/VAR_037647|||http://purl.uniprot.org/annotation/VAR_037648|||http://purl.uniprot.org/annotation/VAR_037649|||http://purl.uniprot.org/annotation/VAR_037650|||http://purl.uniprot.org/annotation/VAR_037651|||http://purl.uniprot.org/annotation/VAR_084189|||http://purl.uniprot.org/annotation/VSP_029994|||http://purl.uniprot.org/annotation/VSP_029995|||http://purl.uniprot.org/annotation/VSP_029996|||http://purl.uniprot.org/annotation/VSP_029997
http://togogenome.org/gene/9606:PIDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB75                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Death|||Disordered|||In MRT75.|||In MRT75; loss of interaction with CRADD; loss of activation of CASP2 protein.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 7.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Loss of complex assembly with CRADD.|||Loss of complex assembly with CRADD. Loss of PIDDosome assembly. Loss of CASP2 activation.|||Loss of the proteolytic cleavage producing PIDD-C.|||Loss of the proteolytic cleavage producing PIDD-C. Unable to translocate to the nucleus upon DNA damage. No effect on the ability to activate CASP2. Complete loss of proteolytic cleavage; when associated with A-588.|||Loss of the proteolytic cleavage producing PIDD-CC.|||Loss of the proteolytic cleavage producing PIDD-CC. Loss of interaction with CRADD and of the ability to activate CASP2. No effect on translocation to the nucleus upon DNA damage. Complete loss of proteolytic cleavage; when associated with A-446.|||N-acetylalanine|||No effect on complex assembly with CRADD.|||No effect on the proteolytic cleavage producing PIDD-C.|||No effect on the proteolytic cleavage producing PIDD-CC.|||PIDD-C|||PIDD-CC|||PIDD-N|||Partial loss of complex assembly with CRADD.|||Partial loss of complex assembly with CRADD. Decreased PIDDosome assembly. Decreased CASP2 activation.|||Peptidase S68|||Phosphoserine|||Removed|||UPA domain|||ZU5 1|||ZU5 2|||p53-induced death domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245243|||http://purl.uniprot.org/annotation/PRO_0000445715|||http://purl.uniprot.org/annotation/PRO_0000445716|||http://purl.uniprot.org/annotation/PRO_0000445717|||http://purl.uniprot.org/annotation/VAR_028031|||http://purl.uniprot.org/annotation/VAR_080765|||http://purl.uniprot.org/annotation/VAR_087344|||http://purl.uniprot.org/annotation/VAR_087345|||http://purl.uniprot.org/annotation/VAR_087346|||http://purl.uniprot.org/annotation/VAR_087347|||http://purl.uniprot.org/annotation/VSP_019664|||http://purl.uniprot.org/annotation/VSP_019665|||http://purl.uniprot.org/annotation/VSP_019666|||http://purl.uniprot.org/annotation/VSP_019667|||http://purl.uniprot.org/annotation/VSP_019668|||http://purl.uniprot.org/annotation/VSP_019669|||http://purl.uniprot.org/annotation/VSP_019670|||http://purl.uniprot.org/annotation/VSP_019671|||http://purl.uniprot.org/annotation/VSP_019672|||http://purl.uniprot.org/annotation/VSP_019673
http://togogenome.org/gene/9606:SLC35A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQL8|||http://purl.uniprot.org/uniprot/A0A1W2PRT7|||http://purl.uniprot.org/uniprot/A0A1W2PSD1|||http://purl.uniprot.org/uniprot/Q9Y2D2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In AMRS.|||In isoform 2.|||In isoform 3.|||UDP-N-acetylglucosamine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213357|||http://purl.uniprot.org/annotation/VAR_087691|||http://purl.uniprot.org/annotation/VSP_012786|||http://purl.uniprot.org/annotation/VSP_054232|||http://purl.uniprot.org/annotation/VSP_054233
http://togogenome.org/gene/9606:BAZ2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIF8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bromo|||Bromodomain adjacent to zinc finger domain protein 2B|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||MBD|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211174|||http://purl.uniprot.org/annotation/VAR_055549|||http://purl.uniprot.org/annotation/VAR_055550|||http://purl.uniprot.org/annotation/VAR_055551|||http://purl.uniprot.org/annotation/VAR_055552|||http://purl.uniprot.org/annotation/VAR_055553|||http://purl.uniprot.org/annotation/VSP_000553|||http://purl.uniprot.org/annotation/VSP_000554|||http://purl.uniprot.org/annotation/VSP_037114|||http://purl.uniprot.org/annotation/VSP_037115
http://togogenome.org/gene/9606:FAM117A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C073                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein FAM117A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264988|||http://purl.uniprot.org/annotation/VSP_056129
http://togogenome.org/gene/9606:GALK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DW43|||http://purl.uniprot.org/uniprot/B7ZAX5|||http://purl.uniprot.org/uniprot/Q01415                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GHMP kinase C-terminal|||GHMP kinase N-terminal|||Galactokinase N-terminal|||In isoform 2.|||N-acetylgalactosamine kinase|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184647|||http://purl.uniprot.org/annotation/VAR_049123|||http://purl.uniprot.org/annotation/VSP_042897
http://togogenome.org/gene/9606:PSPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78330                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PSPHD; decreased L-phosphoserine phosphatase activity.|||Loss of L-phosphoserine phosphatase activity.|||N-acetylmethionine|||Nucleophile|||Phosphoserine phosphatase|||Proton donor|||Reduces L-phosphoserine phosphatase activity by about 25%.|||Reduces L-phosphoserine phosphatase activity by about 50%.|||Reduces L-phosphoserine phosphatase activity by about 75%.|||Reduces L-phosphoserine phosphatase activity by about 80%.|||Reduces L-phosphoserine phosphatase activity by about 95%.|||Reduces L-phosphoserine phosphatase activity by about 99%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156879|||http://purl.uniprot.org/annotation/VAR_022378|||http://purl.uniprot.org/annotation/VAR_022379|||http://purl.uniprot.org/annotation/VAR_084508
http://togogenome.org/gene/9606:NDST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8T3|||http://purl.uniprot.org/uniprot/P52848                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1|||Cytoplasmic|||For sulfotransferase activity|||Helical|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 1|||Heparan sulfate N-sulfotransferase 1|||Heparan sulphate-N-deacetylase|||In MRT46.|||In isoform 2.|||In isoform 3.|||Loss of heparan sulfate-glucosamine N-sulfotransferase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Sufficient for localization to Golgi membrane|||Sulfotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085210|||http://purl.uniprot.org/annotation/VAR_072646|||http://purl.uniprot.org/annotation/VAR_072647|||http://purl.uniprot.org/annotation/VAR_072648|||http://purl.uniprot.org/annotation/VAR_072649|||http://purl.uniprot.org/annotation/VSP_017397|||http://purl.uniprot.org/annotation/VSP_017398|||http://purl.uniprot.org/annotation/VSP_061518
http://togogenome.org/gene/9606:KRTAP2-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYT5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  11 X 5 AA repeats of C-C-[CDPQRWG]-[APRS]-[CIPSTVD]|||Keratin-associated protein 2-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331451
http://togogenome.org/gene/9606:CMTM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DZ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 5|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186105|||http://purl.uniprot.org/annotation/VSP_008262|||http://purl.uniprot.org/annotation/VSP_008263|||http://purl.uniprot.org/annotation/VSP_008264|||http://purl.uniprot.org/annotation/VSP_008265|||http://purl.uniprot.org/annotation/VSP_047120
http://togogenome.org/gene/9606:TMEM132E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEE7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNB99.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Transmembrane protein 132E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287103|||http://purl.uniprot.org/annotation/VAR_073717
http://togogenome.org/gene/9606:AKIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase-interacting protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064857|||http://purl.uniprot.org/annotation/VAR_021565|||http://purl.uniprot.org/annotation/VAR_050688|||http://purl.uniprot.org/annotation/VSP_013275|||http://purl.uniprot.org/annotation/VSP_013276
http://togogenome.org/gene/9606:GUCY2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51841                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Guanylate cyclase|||Helical|||In a breast cancer sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||Interchain|||Protein kinase|||Retinal guanylyl cyclase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012386|||http://purl.uniprot.org/annotation/VAR_009136|||http://purl.uniprot.org/annotation/VAR_009137|||http://purl.uniprot.org/annotation/VAR_030633|||http://purl.uniprot.org/annotation/VAR_030634|||http://purl.uniprot.org/annotation/VAR_030635|||http://purl.uniprot.org/annotation/VAR_036419|||http://purl.uniprot.org/annotation/VAR_042233|||http://purl.uniprot.org/annotation/VAR_042234|||http://purl.uniprot.org/annotation/VAR_042235|||http://purl.uniprot.org/annotation/VAR_042236|||http://purl.uniprot.org/annotation/VAR_042237|||http://purl.uniprot.org/annotation/VAR_042238|||http://purl.uniprot.org/annotation/VAR_042239|||http://purl.uniprot.org/annotation/VAR_042240|||http://purl.uniprot.org/annotation/VAR_042241|||http://purl.uniprot.org/annotation/VAR_042242|||http://purl.uniprot.org/annotation/VAR_042243|||http://purl.uniprot.org/annotation/VAR_069424
http://togogenome.org/gene/9606:H2AC20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16777                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 2-C|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055238
http://togogenome.org/gene/9606:KRTAP10-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60331                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||24 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185209|||http://purl.uniprot.org/annotation/VAR_017603|||http://purl.uniprot.org/annotation/VAR_047502|||http://purl.uniprot.org/annotation/VAR_047503|||http://purl.uniprot.org/annotation/VAR_047504
http://togogenome.org/gene/9606:DEFB107A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZN7                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006979
http://togogenome.org/gene/9606:OR4K5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN5|||http://purl.uniprot.org/uniprot/Q8NGD3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150555|||http://purl.uniprot.org/annotation/VAR_034200
http://togogenome.org/gene/9606:KSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVT5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||Kinase suppressor of Ras 1|||Loss of MAP2K1 mediated-BRAF-KSR1 dimerization.|||Loss of interaction with BRAF and MAP2K1 and severe decrease in MAP2K1 phosphorylation levels.|||Loss of the interaction with MAP2K1 resulting in loss of BRAF-KSR1 dimerization and BRAF activation. No effect on ATP binding or interaction with HSP90AA1, 14-3-3 and CDC37.|||Mediates association with membranes|||No effect on MAP2K1 mediated-BRAF-KSR1 dimerization and BRAF activation.|||No effect on MAP2K1 or MAP2K2 mediated-BRAF-KSR1 dimerization and BRAF activation.|||No effect on MAP2K1- or MAP2K2-mediated-BRAF-KSR1 dimerization and BRAF activation.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces interaction with BRAF and MAP2K1 and thus phosphorylation of MAP2K1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086229|||http://purl.uniprot.org/annotation/VAR_040658|||http://purl.uniprot.org/annotation/VAR_046048|||http://purl.uniprot.org/annotation/VAR_046049|||http://purl.uniprot.org/annotation/VSP_055655|||http://purl.uniprot.org/annotation/VSP_055656|||http://purl.uniprot.org/annotation/VSP_055657
http://togogenome.org/gene/9606:OR2A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVW2|||http://purl.uniprot.org/uniprot/O95047                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150454
http://togogenome.org/gene/9606:NRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60462|||http://purl.uniprot.org/uniprot/Q7Z3T9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||F5/8 type C|||F5/8 type C 1|||F5/8 type C 2|||Helical|||In isoform A0.|||In isoform A17 and isoform B0.|||In isoform B0 and isoform B5.|||In isoform s9.|||MAM|||N-linked (GlcNAc...) asparagine|||Neuropilin|||Neuropilin-2|||Or 22|||Polar residues|||Rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021863|||http://purl.uniprot.org/annotation/PRO_5004295229|||http://purl.uniprot.org/annotation/VAR_047754|||http://purl.uniprot.org/annotation/VAR_065167|||http://purl.uniprot.org/annotation/VAR_067537|||http://purl.uniprot.org/annotation/VAR_067538|||http://purl.uniprot.org/annotation/VSP_004341|||http://purl.uniprot.org/annotation/VSP_004342|||http://purl.uniprot.org/annotation/VSP_041160|||http://purl.uniprot.org/annotation/VSP_044908|||http://purl.uniprot.org/annotation/VSP_044909
http://togogenome.org/gene/9606:HM13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGU3|||http://purl.uniprot.org/uniprot/A0A0S2Z5V7|||http://purl.uniprot.org/uniprot/Q8TCT9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation; when associated with Q-10.|||Abolishes N-glycosylation; when associated with Q-20.|||Abolishes proteolysis of PSEN1.|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Lumenal|||Minor histocompatibility antigen H13|||N-linked (GlcNAc...) asparagine|||No effect on inhibitor binding; abolishes catalytic activity. Abolishes proteolysis of PSEN1. Abolishes proteolysis of XBP1 isoform 1 and increases interaction with XBP1 isoform 1.|||No effect on proteolysis of PSEN1.|||PAL|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073907|||http://purl.uniprot.org/annotation/VAR_014274|||http://purl.uniprot.org/annotation/VSP_005196|||http://purl.uniprot.org/annotation/VSP_015082|||http://purl.uniprot.org/annotation/VSP_015083
http://togogenome.org/gene/9606:ASCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50553                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Achaete-scute homolog 1|||Disordered|||N6-acetyllysine|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127126|||http://purl.uniprot.org/annotation/VAR_013179
http://togogenome.org/gene/9606:SLC52A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ40                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cell surface localization.|||Cytoplasmic|||Extracellular|||Helical|||In BVVLS1.|||In BVVLS1; loss of localization to cell membrane; loss of riboflavin transport.|||In BVVLS1; loss of localization to cell membrane; loss of riboflavin transport; does not affect protein abundance.|||In BVVLS1; loss of riboflavin transport; no effect on localization to cell membrane; does not affect protein abundance.|||In BVVLS1; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on cell surface localization.|||No effect on riboflavin transport; no effect on localization to cell membrane.|||Phosphoserine|||Solute carrier family 52, riboflavin transporter, member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042636|||http://purl.uniprot.org/annotation/VAR_053565|||http://purl.uniprot.org/annotation/VAR_053566|||http://purl.uniprot.org/annotation/VAR_053567|||http://purl.uniprot.org/annotation/VAR_053568|||http://purl.uniprot.org/annotation/VAR_053569|||http://purl.uniprot.org/annotation/VAR_063694|||http://purl.uniprot.org/annotation/VAR_063695|||http://purl.uniprot.org/annotation/VAR_063696|||http://purl.uniprot.org/annotation/VAR_063698|||http://purl.uniprot.org/annotation/VAR_063699|||http://purl.uniprot.org/annotation/VAR_063700|||http://purl.uniprot.org/annotation/VAR_063701|||http://purl.uniprot.org/annotation/VAR_077422|||http://purl.uniprot.org/annotation/VAR_077423|||http://purl.uniprot.org/annotation/VAR_077424|||http://purl.uniprot.org/annotation/VAR_077425|||http://purl.uniprot.org/annotation/VAR_077426|||http://purl.uniprot.org/annotation/VAR_077427|||http://purl.uniprot.org/annotation/VAR_077428|||http://purl.uniprot.org/annotation/VAR_077429|||http://purl.uniprot.org/annotation/VAR_077430|||http://purl.uniprot.org/annotation/VAR_077431|||http://purl.uniprot.org/annotation/VAR_077432|||http://purl.uniprot.org/annotation/VSP_003814|||http://purl.uniprot.org/annotation/VSP_003815
http://togogenome.org/gene/9606:SLC26A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40879                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chloride anion exchanger|||Cytoplasmic|||Extracellular|||Helical|||In DIAR1.|||Loss of interaction with NHERF4. No effect on localization to cell membrane or its exchanger activity.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||STAS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080161|||http://purl.uniprot.org/annotation/VAR_007428|||http://purl.uniprot.org/annotation/VAR_007429|||http://purl.uniprot.org/annotation/VAR_007430|||http://purl.uniprot.org/annotation/VAR_007431|||http://purl.uniprot.org/annotation/VAR_007432|||http://purl.uniprot.org/annotation/VAR_007433|||http://purl.uniprot.org/annotation/VAR_012777|||http://purl.uniprot.org/annotation/VAR_012778|||http://purl.uniprot.org/annotation/VAR_053660|||http://purl.uniprot.org/annotation/VAR_053661|||http://purl.uniprot.org/annotation/VAR_053662|||http://purl.uniprot.org/annotation/VAR_066062|||http://purl.uniprot.org/annotation/VAR_066063|||http://purl.uniprot.org/annotation/VAR_066064|||http://purl.uniprot.org/annotation/VAR_066065|||http://purl.uniprot.org/annotation/VAR_066066|||http://purl.uniprot.org/annotation/VAR_066067|||http://purl.uniprot.org/annotation/VAR_066068|||http://purl.uniprot.org/annotation/VAR_066069|||http://purl.uniprot.org/annotation/VAR_066070|||http://purl.uniprot.org/annotation/VAR_066071|||http://purl.uniprot.org/annotation/VAR_066072|||http://purl.uniprot.org/annotation/VAR_066073|||http://purl.uniprot.org/annotation/VAR_066074|||http://purl.uniprot.org/annotation/VAR_066075|||http://purl.uniprot.org/annotation/VAR_077354|||http://purl.uniprot.org/annotation/VAR_077355|||http://purl.uniprot.org/annotation/VAR_077356|||http://purl.uniprot.org/annotation/VAR_077357|||http://purl.uniprot.org/annotation/VAR_077358|||http://purl.uniprot.org/annotation/VAR_077359|||http://purl.uniprot.org/annotation/VAR_077360|||http://purl.uniprot.org/annotation/VAR_077361|||http://purl.uniprot.org/annotation/VAR_077362
http://togogenome.org/gene/9606:FAM20B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75063                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glycosaminoglycan xylosylkinase|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008745
http://togogenome.org/gene/9606:IQGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46940                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes neurite outgrowth promoting activity; when associated with A-1441.|||Abolishes neurite outgrowth promoting activity; when associated with A-1443.|||Basic and acidic residues|||C1|||C2|||Calponin-homology (CH)|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by PKC/PRKCE|||Phosphotyrosine|||Ras GTPase-activating-like protein IQGAP1|||Ras-GAP|||Removed|||Strongly enhances neurite outgrowth promoting activity; when associated with A-1441.|||Strongly enhances neurite outgrowth promoting activity; when associated with A-1443.|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056648|||http://purl.uniprot.org/annotation/VAR_049134
http://togogenome.org/gene/9606:EML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00423                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes tubulin binding; when associated with S-192; A-547; T-626; S-627; A-646 and A-786.|||Abolishes tubulin binding; when associated with S-192; S-194; A-547; S-627; A-646 and A-786.|||Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; A-646 and A-786.|||Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-646.|||Abolishes tubulin binding; when associated with S-192; S-194; A-547; T-626; S-627 and A-786.|||Abolishes tubulin binding; when associated with S-192; S-194; T-626; S-627; A-646 and A-786.|||Abolishes tubulin binding; when associated with S-194; A-547; T-626; S-627; A-646 and A-786.|||Disordered|||Echinoderm microtubule-associated protein-like 1|||In BH.|||In BH; decreased microtubule-binding.|||In isoform 3.|||No effect on tubulin binding. Does not disrupt self-association. Decreased association with microtubules.|||Phosphoserine|||Polar residues|||Tandem atypical propeller in EMLs|||WD 1|||WD 10|||WD 11|||WD 12|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050961|||http://purl.uniprot.org/annotation/VAR_031720|||http://purl.uniprot.org/annotation/VAR_031721|||http://purl.uniprot.org/annotation/VAR_031722|||http://purl.uniprot.org/annotation/VAR_071075|||http://purl.uniprot.org/annotation/VAR_071076|||http://purl.uniprot.org/annotation/VAR_081119|||http://purl.uniprot.org/annotation/VSP_024476
http://togogenome.org/gene/9606:PGPEP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFU8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Pyroglutamyl-peptidase 1-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334694|||http://purl.uniprot.org/annotation/VAR_043463|||http://purl.uniprot.org/annotation/VAR_043464|||http://purl.uniprot.org/annotation/VSP_053799
http://togogenome.org/gene/9606:TAS2R60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59551                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 60                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082351
http://togogenome.org/gene/9606:GPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13227                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with TBL1X.|||Abolishes interaction with sumoylated NR1H2 and NR5A2 proteins.|||Abolishes methylation.|||Abolishes sumoylation; when associated with R-45.|||Abolishes sumoylation; when associated with R-71.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Decreases methylation.|||Disordered|||Does not affect methylation.|||G protein pathway suppressor 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Omega-N-methylarginine; alternate|||Polar residues|||Strongly decreases methylation.|||Weakly affects interaction with sumoylated NR1H2 and NR5A2 proteins.|||interaction with SUMO                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087565|||http://purl.uniprot.org/annotation/VAR_021972|||http://purl.uniprot.org/annotation/VSP_057012
http://togogenome.org/gene/9606:CDCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation and interaction with YHWAE and YHWAZ.|||Abolishes phosphorylation, interaction with YHWAE and YHWAZ, and cytoplasmic localization.|||Basic and acidic residues|||Cell division cycle-associated protein 7|||Disordered|||Does not affect phosphorylation or interaction with YHWAE and YHWAZ.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ICF3.|||In ICF3; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increased phosphorylation, binding to YHWAE and YHWAZ, and cytoplasmic expression.|||Interaction with MYC|||Mediates transcriptional activity|||No effect on subcellular location.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Predominantly cytoplasmic.|||Predominantly cytoplasmic. Completely cytoplasmic with no nuclear expression; when associated with E-171.|||Predominantly cytoplasmic. Completely cytoplasmic with no nuclear expression; when associated with E-176.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249310|||http://purl.uniprot.org/annotation/VAR_076578|||http://purl.uniprot.org/annotation/VAR_076579|||http://purl.uniprot.org/annotation/VAR_076580|||http://purl.uniprot.org/annotation/VAR_076581|||http://purl.uniprot.org/annotation/VSP_020394|||http://purl.uniprot.org/annotation/VSP_020395|||http://purl.uniprot.org/annotation/VSP_020396|||http://purl.uniprot.org/annotation/VSP_020397|||http://purl.uniprot.org/annotation/VSP_054407|||http://purl.uniprot.org/annotation/VSP_054408
http://togogenome.org/gene/9606:TCAIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3R3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||T-cell activation inhibitor, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235340|||http://purl.uniprot.org/annotation/VAR_050720|||http://purl.uniprot.org/annotation/VSP_018469|||http://purl.uniprot.org/annotation/VSP_018470|||http://purl.uniprot.org/annotation/VSP_018471|||http://purl.uniprot.org/annotation/VSP_018472|||http://purl.uniprot.org/annotation/VSP_038421
http://togogenome.org/gene/9606:CEBPZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03701                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CCAAT/enhancer-binding protein zeta|||Disordered|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173470|||http://purl.uniprot.org/annotation/VAR_026043|||http://purl.uniprot.org/annotation/VAR_031399|||http://purl.uniprot.org/annotation/VAR_031400|||http://purl.uniprot.org/annotation/VAR_055622
http://togogenome.org/gene/9606:VPS13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q709C8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abnormal localization to the cytosol.|||Basic residues|||Chorein N-terminal|||Disordered|||FFAT|||In PARK23.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Intermembrane lipid transfer protein VPS13C|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Required for late endosome/lysosome localization|||Required for lipid droplet localization|||SHR-BD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262949|||http://purl.uniprot.org/annotation/VAR_029548|||http://purl.uniprot.org/annotation/VAR_029549|||http://purl.uniprot.org/annotation/VAR_029550|||http://purl.uniprot.org/annotation/VAR_029551|||http://purl.uniprot.org/annotation/VAR_029552|||http://purl.uniprot.org/annotation/VAR_029553|||http://purl.uniprot.org/annotation/VAR_029554|||http://purl.uniprot.org/annotation/VAR_029555|||http://purl.uniprot.org/annotation/VAR_029556|||http://purl.uniprot.org/annotation/VAR_053808|||http://purl.uniprot.org/annotation/VAR_074191|||http://purl.uniprot.org/annotation/VAR_076363|||http://purl.uniprot.org/annotation/VSP_052243|||http://purl.uniprot.org/annotation/VSP_052244|||http://purl.uniprot.org/annotation/VSP_052245
http://togogenome.org/gene/9606:FUOM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VDF0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Fucose mutarotase|||In isoform 2.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286553|||http://purl.uniprot.org/annotation/VSP_025080|||http://purl.uniprot.org/annotation/VSP_025081
http://togogenome.org/gene/9606:CKAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07065                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Cytoskeleton-associated protein 4|||Disordered|||Extracellular|||Helical|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by FAM20C|||Pro residues|||S-palmitoyl cysteine; by ZDHHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252417|||http://purl.uniprot.org/annotation/VAR_027853
http://togogenome.org/gene/9606:NANOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4D1|||http://purl.uniprot.org/uniprot/Q9H9S0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X repeats starting with a Trp in each unit|||Basic and acidic residues|||Decreased POU5F1 promoter DNA-binding and protein stability.|||Disordered|||Homeobox|||Homeobox protein NANOG|||In isoform 2.|||Increased POU5F1 promoter DNA-binding and protein stability.|||Inhibits POU5F1 promoter DNA-binding.|||No effect on POU5F1 promoter DNA-binding.|||No effect on POU5F1 promoter DNA-binding. Decreased protein stability.|||No effect on POU5F1 promoter DNA-binding. Increased protein stability.|||Polar residues|||Required for DNA-binding|||Sufficient for strong transactivation activity|||Sufficient for transactivation activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261418|||http://purl.uniprot.org/annotation/VAR_029384|||http://purl.uniprot.org/annotation/VSP_021688
http://togogenome.org/gene/9606:TIMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01033|||http://purl.uniprot.org/uniprot/Q6FGX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Decreases protein flexibility and increases affinity for MMP14.|||Involved in metalloproteinase-binding|||Metalloproteinase inhibitor 1|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||NTR|||Nearly abolishes metalloproteinase inhibition.|||Normal interaction with metalloproteinase.|||Phosphoserine; by FAM20C|||Reduced interaction with metalloproteinase.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000002|||http://purl.uniprot.org/annotation/CAR_000003|||http://purl.uniprot.org/annotation/PRO_0000034323|||http://purl.uniprot.org/annotation/PRO_5014310451
http://togogenome.org/gene/9606:GYS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54840                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Disordered|||Glycogen [starch] synthase, liver|||In GSD0.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by GSK3-alpha and GSK3-beta|||Phosphoserine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194768|||http://purl.uniprot.org/annotation/VAR_007860|||http://purl.uniprot.org/annotation/VAR_007861|||http://purl.uniprot.org/annotation/VAR_007862|||http://purl.uniprot.org/annotation/VAR_007863|||http://purl.uniprot.org/annotation/VAR_007864|||http://purl.uniprot.org/annotation/VAR_007865|||http://purl.uniprot.org/annotation/VAR_055885|||http://purl.uniprot.org/annotation/VAR_055886|||http://purl.uniprot.org/annotation/VAR_058848
http://togogenome.org/gene/9606:ZNF326                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRN4|||http://purl.uniprot.org/uniprot/Q5BKZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||C2H2 AKAP95-type|||C2H2 AKAP95-type 1|||C2H2 AKAP95-type 2|||DBIRD complex subunit ZNF326|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Mediates transcriptional activation|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075386|||http://purl.uniprot.org/annotation/VSP_014956|||http://purl.uniprot.org/annotation/VSP_043772
http://togogenome.org/gene/9606:PEAK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes homodimerization and interaction with CRK isoform CRK-II.|||Abolishes interaction with CRK isoform CRK-II. Abolishes inhibition of CRK-II-dependent membrane ruffling.|||Disordered|||Pro residues|||Protein PEAK3|||Strongly decreases homodimerization and interaction with CRK isoform CRK-II.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277808
http://togogenome.org/gene/9606:TMEM196                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Transmembrane protein 196                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317256|||http://purl.uniprot.org/annotation/VSP_030928|||http://purl.uniprot.org/annotation/VSP_030929|||http://purl.uniprot.org/annotation/VSP_039208
http://togogenome.org/gene/9606:CXCR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49682                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes CXCL10-induced chemotaxis. Reduces CXCL9- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11.|||Abolishes binding to CXCL10 and CXCL11 and CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-induced chemotaxis.|||Abolishes binding to CXCL10 and CXCL11 and CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced chemotaxis.|||Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis.|||Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces ligand-induced receptor internalization.|||Abolishes binding to CXCL10 and CXCL11. Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis.|||C-X-C chemokine receptor type 3|||Cytoplasmic|||Disordered|||Does not affect binding to CXCL9, CXCL10 and CXCL11 or activation.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11 or receptor internalization.|||Reduces binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis.|||Reduces binding to CXCL10 and CXCL11, and reduces CXCL10- and CXCL11-induced chemotaxis and activation. Does not affect CXCL9-induced chemotaxis and activation.|||Reduces binding to CXCL10 and CXCL9- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and CXCL10-induced chemotaxis.|||Reduces binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11.|||Reduces slightly CXCL9-, CXCL10- and CXCL11-induced chemotaxis.|||Reduces sulfation and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL10. Abolishes sulfation, binding to CXCL11, ligand-induced receptor internalization and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-29.|||Reduces sulfation, binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes sulfation, binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-27.|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069346|||http://purl.uniprot.org/annotation/VAR_016240|||http://purl.uniprot.org/annotation/VAR_016241|||http://purl.uniprot.org/annotation/VSP_015684|||http://purl.uniprot.org/annotation/VSP_015685
http://togogenome.org/gene/9606:RNASE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10153|||http://purl.uniprot.org/uniprot/W0UV60                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||C-linked (Man) tryptophan|||N-linked (GlcNAc...) asparagine|||Non-secretory ribonuclease|||Proton acceptor|||Proton donor|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000004|||http://purl.uniprot.org/annotation/PRO_0000030874|||http://purl.uniprot.org/annotation/PRO_5014206139|||http://purl.uniprot.org/annotation/VAR_013150|||http://purl.uniprot.org/annotation/VAR_059820
http://togogenome.org/gene/9606:ABLIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGA7|||http://purl.uniprot.org/uniprot/O94929                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding LIM protein 3|||Basic and acidic residues|||Disordered|||HP|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075702|||http://purl.uniprot.org/annotation/VAR_050143|||http://purl.uniprot.org/annotation/VSP_012126|||http://purl.uniprot.org/annotation/VSP_012127|||http://purl.uniprot.org/annotation/VSP_012128|||http://purl.uniprot.org/annotation/VSP_012129|||http://purl.uniprot.org/annotation/VSP_012130
http://togogenome.org/gene/9606:OR10H5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWE9|||http://purl.uniprot.org/uniprot/Q8NGA6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10H5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150706
http://togogenome.org/gene/9606:PLLP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y342                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||MARVEL|||Phosphoserine|||Plasmolipin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156813
http://togogenome.org/gene/9606:TAPBPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX59                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Ig-like C1-type|||Ig-like V-type|||In isoform beta.|||In isoform delta.|||In isoform epsilon.|||In isoform eta.|||In isoform gamma.|||In isoform zeta.|||Lumenal|||Tapasin-related protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014993|||http://purl.uniprot.org/annotation/VAR_033627|||http://purl.uniprot.org/annotation/VAR_056090|||http://purl.uniprot.org/annotation/VAR_071757|||http://purl.uniprot.org/annotation/VAR_071758|||http://purl.uniprot.org/annotation/VAR_071759|||http://purl.uniprot.org/annotation/VAR_071760|||http://purl.uniprot.org/annotation/VSP_057089|||http://purl.uniprot.org/annotation/VSP_057090|||http://purl.uniprot.org/annotation/VSP_057091|||http://purl.uniprot.org/annotation/VSP_057092|||http://purl.uniprot.org/annotation/VSP_057093|||http://purl.uniprot.org/annotation/VSP_057094|||http://purl.uniprot.org/annotation/VSP_057095|||http://purl.uniprot.org/annotation/VSP_057096
http://togogenome.org/gene/9606:OR5AC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZP5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150574|||http://purl.uniprot.org/annotation/VAR_034214
http://togogenome.org/gene/9606:CTDSP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14595                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2|||FCP1 homology|||Phosphoserine|||Proton donor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212574
http://togogenome.org/gene/9606:UCMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A067XJP8|||http://purl.uniprot.org/uniprot/A0A067XJX6|||http://purl.uniprot.org/uniprot/A0A067XKV3|||http://purl.uniprot.org/uniprot/Q8WVF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Ucma-N|||Unique cartilage matrix-associated protein|||Unique cartilage matrix-associated protein C-terminal fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019549|||http://purl.uniprot.org/annotation/PRO_0000347063|||http://purl.uniprot.org/annotation/PRO_0000347064|||http://purl.uniprot.org/annotation/PRO_5001647954|||http://purl.uniprot.org/annotation/PRO_5001649632|||http://purl.uniprot.org/annotation/PRO_5001649929
http://togogenome.org/gene/9606:ARHGEF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15013                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Basic and acidic residues|||DH|||Disordered|||Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance.|||In SNCV.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N5-methylglutamine|||Phosphoserine|||Polar residues|||Rho guanine nucleotide exchange factor 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080926|||http://purl.uniprot.org/annotation/VAR_019118|||http://purl.uniprot.org/annotation/VAR_038603|||http://purl.uniprot.org/annotation/VAR_057188|||http://purl.uniprot.org/annotation/VAR_073288|||http://purl.uniprot.org/annotation/VSP_010704|||http://purl.uniprot.org/annotation/VSP_040754|||http://purl.uniprot.org/annotation/VSP_040755|||http://purl.uniprot.org/annotation/VSP_040756|||http://purl.uniprot.org/annotation/VSP_040757
http://togogenome.org/gene/9606:KREMEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MU8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CUB|||Cytoplasmic|||Essential for apoptotic activity|||Extracellular|||Helical|||In ECTD13.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Kremen protein 1|||Kringle|||N-linked (GlcNAc...) asparagine|||WSC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021564|||http://purl.uniprot.org/annotation/VAR_078807|||http://purl.uniprot.org/annotation/VSP_003900|||http://purl.uniprot.org/annotation/VSP_015698|||http://purl.uniprot.org/annotation/VSP_034914
http://togogenome.org/gene/9606:OPN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1Y3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding of 11-cis retinal and all-trans retinal. No effect on G-alpha (i) protein signaling.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Opsin-3|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197813|||http://purl.uniprot.org/annotation/VAR_050613|||http://purl.uniprot.org/annotation/VAR_050614|||http://purl.uniprot.org/annotation/VSP_010209
http://togogenome.org/gene/9606:LYAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX58                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC LYAR-type 1|||C2HC LYAR-type 2|||Cell growth-regulating nucleolar protein|||Decreases the production of 28S rRNA and the formation of pre-60S particle.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084528|||http://purl.uniprot.org/annotation/VAR_023080|||http://purl.uniprot.org/annotation/VAR_023081
http://togogenome.org/gene/9606:NCAPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRG7|||http://purl.uniprot.org/uniprot/Q15003                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Condensin complex subunit 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MCPH23; impairs mitotic chromosome compaction.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095038|||http://purl.uniprot.org/annotation/VAR_027882|||http://purl.uniprot.org/annotation/VAR_080954|||http://purl.uniprot.org/annotation/VSP_055179
http://togogenome.org/gene/9606:GHRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBU3                                                                                  ^@                                                                                  Experimental Information|||Helix|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Lipid Binding|||Mass|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Ghrelin-27|||Ghrelin-27-C10, O-decanoylated form.|||Ghrelin-27-C8, O-octanoylated form.|||Ghrelin-28|||Ghrelin-28-C10, O-decanoylated form.|||Ghrelin-28-C10:1, O-decenoylated form.|||Ghrelin-28-C8, O-octanoylated form.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||Leucine amide|||O-decanoyl serine; alternate|||O-hexanoyl serine; alternate|||O-octanoyl serine; alternate|||Obestatin|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019202|||http://purl.uniprot.org/annotation/PRO_0000019203|||http://purl.uniprot.org/annotation/PRO_0000019204|||http://purl.uniprot.org/annotation/PRO_0000045140|||http://purl.uniprot.org/annotation/PRO_0000045141|||http://purl.uniprot.org/annotation/VAR_029135|||http://purl.uniprot.org/annotation/VAR_050095|||http://purl.uniprot.org/annotation/VSP_003245|||http://purl.uniprot.org/annotation/VSP_041437|||http://purl.uniprot.org/annotation/VSP_041438|||http://purl.uniprot.org/annotation/VSP_047642
http://togogenome.org/gene/9606:SLC33A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00400                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetyl-coenzyme A transporter 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CCHLND; the mutant protein is present at normal levels in patient fibroblasts; the mutant protein fails to localize normally to the Golgi apparatus and instead shows punctate staining in the cytoplasm.|||In SPG42; significant increase in the amount of nuclear phosphorylated SMAD1-SMAD5-SMAD8 protein complex; marked increase of the BMPR1A protein level; no change for BMPR2 protein level; decrease of BMPR1A degradation; Loss of homodimerization in the endoplasmic membrane; loss of acetyl-CoA transport activity.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076165|||http://purl.uniprot.org/annotation/VAR_035776|||http://purl.uniprot.org/annotation/VAR_050631|||http://purl.uniprot.org/annotation/VAR_054850|||http://purl.uniprot.org/annotation/VAR_067915
http://togogenome.org/gene/9606:PLEKHO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD55                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family O member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309483|||http://purl.uniprot.org/annotation/VAR_036964|||http://purl.uniprot.org/annotation/VSP_029212
http://togogenome.org/gene/9606:MAPKAPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16644                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory helix|||Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||Higher affinity toward PCH2.|||In MDPT3; decreased localization to the nucleus.|||In a glioblastoma multiforme sample; somatic mutation.|||In an ovarian endometrioid sample; somatic mutation.|||MAP kinase-activated protein kinase 3|||N-acetylmethionine|||Nuclear export signal (NES)|||Phosphoserine; by MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine; by MAPK14|||Polar residues|||Protein kinase|||Proton acceptor|||p38 MAPK-binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086293|||http://purl.uniprot.org/annotation/VAR_040755|||http://purl.uniprot.org/annotation/VAR_040756|||http://purl.uniprot.org/annotation/VAR_040757|||http://purl.uniprot.org/annotation/VAR_077085
http://togogenome.org/gene/9606:C2CD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4AC94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 domain-containing protein 3|||Disordered|||In OFD14.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311239|||http://purl.uniprot.org/annotation/VAR_037181|||http://purl.uniprot.org/annotation/VAR_037182|||http://purl.uniprot.org/annotation/VAR_037183|||http://purl.uniprot.org/annotation/VAR_037184|||http://purl.uniprot.org/annotation/VAR_037185|||http://purl.uniprot.org/annotation/VAR_037186|||http://purl.uniprot.org/annotation/VAR_037187|||http://purl.uniprot.org/annotation/VAR_071196|||http://purl.uniprot.org/annotation/VAR_075697|||http://purl.uniprot.org/annotation/VSP_029444|||http://purl.uniprot.org/annotation/VSP_029445|||http://purl.uniprot.org/annotation/VSP_029446|||http://purl.uniprot.org/annotation/VSP_029447|||http://purl.uniprot.org/annotation/VSP_029448|||http://purl.uniprot.org/annotation/VSP_034676|||http://purl.uniprot.org/annotation/VSP_034677|||http://purl.uniprot.org/annotation/VSP_034678|||http://purl.uniprot.org/annotation/VSP_034679
http://togogenome.org/gene/9606:STK24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR80|||http://purl.uniprot.org/uniprot/Q5U0E6|||http://purl.uniprot.org/uniprot/Q6P0Y1|||http://purl.uniprot.org/uniprot/Q9Y6E0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Cleavage; by caspase-3, caspase-7 and caspase-8|||Disordered|||In isoform A.|||Loss of activity and autophosphorylation.|||Loss of phosphorylation by PKA.|||Loss of proteolytic cleavage by caspases.|||N-acetylalanine|||Nuclear export signal (NES)|||Phosphoserine|||Phosphothreonine; by PKA|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 24|||Serine/threonine-protein kinase 24 12 kDa subunit|||Serine/threonine-protein kinase 24 36 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086711|||http://purl.uniprot.org/annotation/PRO_0000413618|||http://purl.uniprot.org/annotation/PRO_0000413619|||http://purl.uniprot.org/annotation/VAR_041148|||http://purl.uniprot.org/annotation/VAR_041149|||http://purl.uniprot.org/annotation/VSP_004874
http://togogenome.org/gene/9606:PUS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KMT5|||http://purl.uniprot.org/uniprot/E5KMT6|||http://purl.uniprot.org/uniprot/Q9Y606                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MLASA1.|||In MLASA1; unknown pathological significance.|||In MLASA1; unknown pathological significance; mild phenotype.|||In isoform 2.|||Loss of enzyme activity.|||Mitochondrion|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Pseudouridine synthase I TruA alpha/beta|||Pseudouridylate synthase 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057517|||http://purl.uniprot.org/annotation/VAR_021788|||http://purl.uniprot.org/annotation/VAR_036447|||http://purl.uniprot.org/annotation/VAR_086155|||http://purl.uniprot.org/annotation/VAR_086156|||http://purl.uniprot.org/annotation/VAR_086157|||http://purl.uniprot.org/annotation/VAR_086158|||http://purl.uniprot.org/annotation/VAR_086159|||http://purl.uniprot.org/annotation/VSP_020116
http://togogenome.org/gene/9606:HNRNPA2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22626                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  About 10-fold increase in interferon beta production.|||Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Does not affect hydrogel-binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoproteins A2/B1|||Impairs hydrogel-binding.|||In IBMPFD2.|||In isoform A2.|||N-acetylmethionine|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine; alternate|||Nuclear localization signal|||Nuclear targeting sequence|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RRM 1|||RRM 2|||Slightly affects hydrogel-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081836|||http://purl.uniprot.org/annotation/VAR_070591|||http://purl.uniprot.org/annotation/VSP_005830
http://togogenome.org/gene/9606:DMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13316                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cell attachment site|||Dentin matrix acidic phosphoprotein 1|||Disordered|||In isoform 2.|||In one individual with tumoral calcinosis.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021110|||http://purl.uniprot.org/annotation/VAR_030750|||http://purl.uniprot.org/annotation/VAR_030751|||http://purl.uniprot.org/annotation/VAR_030752|||http://purl.uniprot.org/annotation/VAR_033848|||http://purl.uniprot.org/annotation/VSP_004191
http://togogenome.org/gene/9606:JSRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Affecting excitation/contraction coupling in muscle fibers; the sensitivity of CACNA1S voltage sensor is shifted to higher depolarizing voltages in cells carrying this variant.|||Basic and acidic residues|||Disordered|||Junctional sarcoplasmic reticulum protein 1|||Mediates interaction with CACNA1S|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314025|||http://purl.uniprot.org/annotation/VAR_037838|||http://purl.uniprot.org/annotation/VAR_037839|||http://purl.uniprot.org/annotation/VAR_069019|||http://purl.uniprot.org/annotation/VAR_069020
http://togogenome.org/gene/9606:QDPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09417                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dihydropteridine reductase|||In HPABH4C.|||In HPABH4C; mild.|||In HPABH4C; severe.|||In isoform 2.|||N-acetylalanine|||N6-succinyllysine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054636|||http://purl.uniprot.org/annotation/VAR_006960|||http://purl.uniprot.org/annotation/VAR_006961|||http://purl.uniprot.org/annotation/VAR_006962|||http://purl.uniprot.org/annotation/VAR_006963|||http://purl.uniprot.org/annotation/VAR_006964|||http://purl.uniprot.org/annotation/VAR_006965|||http://purl.uniprot.org/annotation/VAR_006966|||http://purl.uniprot.org/annotation/VAR_006967|||http://purl.uniprot.org/annotation/VAR_006968|||http://purl.uniprot.org/annotation/VAR_006969|||http://purl.uniprot.org/annotation/VAR_006970|||http://purl.uniprot.org/annotation/VAR_006971|||http://purl.uniprot.org/annotation/VAR_008121|||http://purl.uniprot.org/annotation/VAR_008122|||http://purl.uniprot.org/annotation/VAR_013027|||http://purl.uniprot.org/annotation/VAR_021767|||http://purl.uniprot.org/annotation/VAR_021768|||http://purl.uniprot.org/annotation/VAR_021769|||http://purl.uniprot.org/annotation/VAR_021770|||http://purl.uniprot.org/annotation/VSP_054356
http://togogenome.org/gene/9606:NIBAN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT44|||http://purl.uniprot.org/uniprot/Q86XR2|||http://purl.uniprot.org/uniprot/Q8N894                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3, isoform 4 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||PH|||Protein Niban 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323759|||http://purl.uniprot.org/annotation/VAR_039583|||http://purl.uniprot.org/annotation/VAR_039584|||http://purl.uniprot.org/annotation/VAR_039585|||http://purl.uniprot.org/annotation/VAR_062126|||http://purl.uniprot.org/annotation/VSP_032126|||http://purl.uniprot.org/annotation/VSP_032127|||http://purl.uniprot.org/annotation/VSP_032128|||http://purl.uniprot.org/annotation/VSP_032129|||http://purl.uniprot.org/annotation/VSP_032130|||http://purl.uniprot.org/annotation/VSP_032131|||http://purl.uniprot.org/annotation/VSP_054124|||http://purl.uniprot.org/annotation/VSP_054125|||http://purl.uniprot.org/annotation/VSP_054126
http://togogenome.org/gene/9606:KCNIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6D7|||http://purl.uniprot.org/uniprot/B3KSZ5|||http://purl.uniprot.org/uniprot/Q9NS61                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2.|||In isoform 3, isoform 5, isoform 7 and isoform 9.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with KCND2|||Kv channel-interacting protein 2|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073821|||http://purl.uniprot.org/annotation/PRO_5015337443|||http://purl.uniprot.org/annotation/VSP_015049|||http://purl.uniprot.org/annotation/VSP_015050|||http://purl.uniprot.org/annotation/VSP_015051|||http://purl.uniprot.org/annotation/VSP_015052|||http://purl.uniprot.org/annotation/VSP_015053|||http://purl.uniprot.org/annotation/VSP_015054|||http://purl.uniprot.org/annotation/VSP_015055|||http://purl.uniprot.org/annotation/VSP_015056|||http://purl.uniprot.org/annotation/VSP_015057|||http://purl.uniprot.org/annotation/VSP_015058
http://togogenome.org/gene/9606:VTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9ZGG2|||http://purl.uniprot.org/uniprot/P04004                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Peptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69.|||Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76.|||Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69.|||Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76.|||Basic residues|||Cell attachment site|||Cleavage|||Disordered|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Heparin-binding|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine; by CK2; in vitro|||Polar residues|||SMB|||Somatomedin-B|||Sulfotyrosine|||Vitronectin|||Vitronectin V10 subunit|||Vitronectin V65 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036394|||http://purl.uniprot.org/annotation/PRO_0000036395|||http://purl.uniprot.org/annotation/PRO_0000036396|||http://purl.uniprot.org/annotation/PRO_0000036397|||http://purl.uniprot.org/annotation/PRO_5003133002|||http://purl.uniprot.org/annotation/VAR_012983|||http://purl.uniprot.org/annotation/VAR_012984|||http://purl.uniprot.org/annotation/VAR_012985
http://togogenome.org/gene/9606:OR4A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWJ2|||http://purl.uniprot.org/uniprot/Q8NH83                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150524|||http://purl.uniprot.org/annotation/VAR_031741|||http://purl.uniprot.org/annotation/VAR_062033|||http://purl.uniprot.org/annotation/VAR_062034
http://togogenome.org/gene/9606:PLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53350                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity. Abolishes checkpoint recovery.|||Abolishes interaction with CDC25C and reduces centrosomal localization.|||Abolishes kinase activity.|||Activation loop|||Basic and acidic residues|||D-box that targets the protein for proteasomal degradation in anaphase|||Disordered|||Does not interfere with FRY-binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Important for interaction with phosphorylated proteins|||In a lung squamous cell carcinoma sample; somatic mutation.|||In analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130.|||In analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67.|||In pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538.|||In pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540.|||Increases activity and restores recovery after DNA damage checkpoint.|||Increases activity. Results in a block in G1/S.|||Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337.|||Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340.|||Linker|||Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-427.|||Loss of kinase activity. No effect on RIOK2-binding.|||Loss of kinase activity. No effect on S-phase progression.|||N-acetylserine|||No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210.|||No effect on centrosomal localization, nor on S-phase progression; when asscociated with A-427. Loss of centrosomal localization and of S-phase progression; when associated with A- 415 and A-427.|||No effect on centrosomal localization, nor on S-phase progression; when associated with A-414. Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-415.|||POLO box 1|||POLO box 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by AURKA|||Protein kinase|||Proton acceptor|||Reduced catalytic activity, but no effect on affinity for ATP.|||Removed|||Serine/threonine-protein kinase PLK1|||Severe mitotic defects leading to prometaphase delay. Increased localization at kinetochores leading to increased levels of phosphorylated BUBR1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086556|||http://purl.uniprot.org/annotation/VAR_041018|||http://purl.uniprot.org/annotation/VAR_041019|||http://purl.uniprot.org/annotation/VAR_041020|||http://purl.uniprot.org/annotation/VAR_041021|||http://purl.uniprot.org/annotation/VAR_041022|||http://purl.uniprot.org/annotation/VAR_051659|||http://purl.uniprot.org/annotation/VAR_051660|||http://purl.uniprot.org/annotation/VAR_051661
http://togogenome.org/gene/9606:CLDN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15551|||http://purl.uniprot.org/uniprot/Q75L79                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-3|||Cytoplasmic|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144738
http://togogenome.org/gene/9606:TP53TG3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:AFG2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PGU6|||http://purl.uniprot.org/uniprot/Q8NB90                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||ATPase family gene 2 protein homolog A|||CDC48 N-terminal subdomain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDHSB.|||In NEDHSB; impaired maturation of pre-60S ribosome.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330583|||http://purl.uniprot.org/annotation/VAR_042703|||http://purl.uniprot.org/annotation/VAR_042704|||http://purl.uniprot.org/annotation/VAR_075775|||http://purl.uniprot.org/annotation/VAR_075776|||http://purl.uniprot.org/annotation/VAR_075777|||http://purl.uniprot.org/annotation/VAR_075778|||http://purl.uniprot.org/annotation/VAR_075779|||http://purl.uniprot.org/annotation/VAR_075780|||http://purl.uniprot.org/annotation/VAR_075781|||http://purl.uniprot.org/annotation/VAR_075782|||http://purl.uniprot.org/annotation/VAR_075783|||http://purl.uniprot.org/annotation/VAR_075784|||http://purl.uniprot.org/annotation/VAR_075785|||http://purl.uniprot.org/annotation/VAR_086543|||http://purl.uniprot.org/annotation/VSP_033046|||http://purl.uniprot.org/annotation/VSP_033047|||http://purl.uniprot.org/annotation/VSP_033048|||http://purl.uniprot.org/annotation/VSP_033049
http://togogenome.org/gene/9606:RRP36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EU6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Ribosomal RNA processing protein 36 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252157|||http://purl.uniprot.org/annotation/VAR_027786|||http://purl.uniprot.org/annotation/VSP_020884
http://togogenome.org/gene/9606:RBMY1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member A1|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081899|||http://purl.uniprot.org/annotation/VSP_042315|||http://purl.uniprot.org/annotation/VSP_042316
http://togogenome.org/gene/9606:OR5H6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW86|||http://purl.uniprot.org/uniprot/Q8NGV6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5H6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150597|||http://purl.uniprot.org/annotation/VAR_054343|||http://purl.uniprot.org/annotation/VAR_054344|||http://purl.uniprot.org/annotation/VAR_054345|||http://purl.uniprot.org/annotation/VAR_054346|||http://purl.uniprot.org/annotation/VAR_054347|||http://purl.uniprot.org/annotation/VAR_054348|||http://purl.uniprot.org/annotation/VAR_060008|||http://purl.uniprot.org/annotation/VAR_060009
http://togogenome.org/gene/9606:XRRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2D8|||http://purl.uniprot.org/uniprot/Q8TEH2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Polar residues|||X-ray radiation resistance-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318130|||http://purl.uniprot.org/annotation/VAR_038693|||http://purl.uniprot.org/annotation/VAR_051492|||http://purl.uniprot.org/annotation/VSP_044988|||http://purl.uniprot.org/annotation/VSP_044989|||http://purl.uniprot.org/annotation/VSP_052670|||http://purl.uniprot.org/annotation/VSP_052671|||http://purl.uniprot.org/annotation/VSP_052672|||http://purl.uniprot.org/annotation/VSP_052673|||http://purl.uniprot.org/annotation/VSP_052674
http://togogenome.org/gene/9606:PCDHB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003934|||http://purl.uniprot.org/annotation/VAR_021881|||http://purl.uniprot.org/annotation/VAR_048553|||http://purl.uniprot.org/annotation/VAR_059188|||http://purl.uniprot.org/annotation/VSP_055931
http://togogenome.org/gene/9606:ZNF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWJ4|||http://purl.uniprot.org/uniprot/E9PIH3|||http://purl.uniprot.org/uniprot/E9PJX9|||http://purl.uniprot.org/uniprot/F5H290|||http://purl.uniprot.org/uniprot/P17097                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Phosphoserine|||Zinc finger protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047330|||http://purl.uniprot.org/annotation/VAR_024191|||http://purl.uniprot.org/annotation/VAR_052744|||http://purl.uniprot.org/annotation/VAR_052745|||http://purl.uniprot.org/annotation/VSP_054822|||http://purl.uniprot.org/annotation/VSP_054823|||http://purl.uniprot.org/annotation/VSP_054824
http://togogenome.org/gene/9606:DCLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVM3|||http://purl.uniprot.org/uniprot/Q9C098                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252254|||http://purl.uniprot.org/annotation/VAR_040444|||http://purl.uniprot.org/annotation/VAR_040445|||http://purl.uniprot.org/annotation/VAR_040446|||http://purl.uniprot.org/annotation/VAR_040447|||http://purl.uniprot.org/annotation/VAR_040448|||http://purl.uniprot.org/annotation/VAR_040449|||http://purl.uniprot.org/annotation/VAR_040450|||http://purl.uniprot.org/annotation/VAR_040451
http://togogenome.org/gene/9606:STK36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW1|||http://purl.uniprot.org/uniprot/Q9NRP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In an ovarian endometrioid sample; somatic mutation.|||In an ovarian papillary serous adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||No effect on nuclear localization of GLI1 or GLI2 or on GLI-mediated transcription.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229020|||http://purl.uniprot.org/annotation/VAR_025727|||http://purl.uniprot.org/annotation/VAR_025728|||http://purl.uniprot.org/annotation/VAR_025729|||http://purl.uniprot.org/annotation/VAR_041177|||http://purl.uniprot.org/annotation/VAR_041178|||http://purl.uniprot.org/annotation/VAR_041179|||http://purl.uniprot.org/annotation/VAR_041180|||http://purl.uniprot.org/annotation/VAR_041181|||http://purl.uniprot.org/annotation/VAR_041182|||http://purl.uniprot.org/annotation/VAR_041183|||http://purl.uniprot.org/annotation/VAR_041184|||http://purl.uniprot.org/annotation/VAR_041185|||http://purl.uniprot.org/annotation/VAR_041186|||http://purl.uniprot.org/annotation/VAR_041187|||http://purl.uniprot.org/annotation/VAR_041188|||http://purl.uniprot.org/annotation/VAR_041189|||http://purl.uniprot.org/annotation/VAR_041190|||http://purl.uniprot.org/annotation/VAR_041191|||http://purl.uniprot.org/annotation/VAR_041192|||http://purl.uniprot.org/annotation/VAR_041193|||http://purl.uniprot.org/annotation/VAR_041194|||http://purl.uniprot.org/annotation/VAR_041195|||http://purl.uniprot.org/annotation/VAR_057112|||http://purl.uniprot.org/annotation/VAR_061747|||http://purl.uniprot.org/annotation/VSP_051983
http://togogenome.org/gene/9606:ATP5PO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48047                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase subunit O, mitochondrial|||Increased ATP levels.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002646|||http://purl.uniprot.org/annotation/VAR_011930
http://togogenome.org/gene/9606:LIG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGV9|||http://purl.uniprot.org/uniprot/A8K8Q4|||http://purl.uniprot.org/uniprot/P49917                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA ligase family profile|||Associated with resistance to multiple myeloma.|||BRCT|||BRCT 1|||BRCT 2|||DNA ligase 4|||Found in a patient with microcephalic primordial dwarfism; unknown pathological significance.|||In LIG4S and leukemia; impairs activity.|||In LIG4S.|||In RSSCID.|||N6-AMP-lysine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059576|||http://purl.uniprot.org/annotation/VAR_012774|||http://purl.uniprot.org/annotation/VAR_012775|||http://purl.uniprot.org/annotation/VAR_016771|||http://purl.uniprot.org/annotation/VAR_016772|||http://purl.uniprot.org/annotation/VAR_016773|||http://purl.uniprot.org/annotation/VAR_018808|||http://purl.uniprot.org/annotation/VAR_029352|||http://purl.uniprot.org/annotation/VAR_029353|||http://purl.uniprot.org/annotation/VAR_033884|||http://purl.uniprot.org/annotation/VAR_044123|||http://purl.uniprot.org/annotation/VAR_044124|||http://purl.uniprot.org/annotation/VAR_075826|||http://purl.uniprot.org/annotation/VAR_084970|||http://purl.uniprot.org/annotation/VAR_084971
http://togogenome.org/gene/9606:DPY19L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z388                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-acetylalanine|||Probable C-mannosyltransferase DPY19L4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311881
http://togogenome.org/gene/9606:PCIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4Z3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes formation of N(6),2'-O-dimethyladenosine cap (m6A(m)).|||Basic and acidic residues|||Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly reduced formation of N(6),2'-O-dimethyladenosine cap (m6A(m)).|||WW|||mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076087
http://togogenome.org/gene/9606:PCARE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in patients with pathologic myopia; unknown pathological significance.|||In RP54.|||In RP54; induces proteasomal degradation.|||In RP54; unknown pathological significance.|||N-myristoyl glycine|||Photoreceptor cilium actin regulator|||Polar residues|||Pro residues|||Probable disease-associated variant found in a family with sensorineural hearing loss and retinal degeneration; the retinal involvement is more severe in double homozygotes also carrying a CEP250 truncating variant.|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329078|||http://purl.uniprot.org/annotation/VAR_042646|||http://purl.uniprot.org/annotation/VAR_042647|||http://purl.uniprot.org/annotation/VAR_042648|||http://purl.uniprot.org/annotation/VAR_042649|||http://purl.uniprot.org/annotation/VAR_042650|||http://purl.uniprot.org/annotation/VAR_063395|||http://purl.uniprot.org/annotation/VAR_063396|||http://purl.uniprot.org/annotation/VAR_065267|||http://purl.uniprot.org/annotation/VAR_065268|||http://purl.uniprot.org/annotation/VAR_065269|||http://purl.uniprot.org/annotation/VAR_065270|||http://purl.uniprot.org/annotation/VAR_065271|||http://purl.uniprot.org/annotation/VAR_065272|||http://purl.uniprot.org/annotation/VAR_065273|||http://purl.uniprot.org/annotation/VAR_065274|||http://purl.uniprot.org/annotation/VAR_065275|||http://purl.uniprot.org/annotation/VAR_065276|||http://purl.uniprot.org/annotation/VAR_065277|||http://purl.uniprot.org/annotation/VAR_065278|||http://purl.uniprot.org/annotation/VAR_065279|||http://purl.uniprot.org/annotation/VAR_065280|||http://purl.uniprot.org/annotation/VAR_065281|||http://purl.uniprot.org/annotation/VAR_065282|||http://purl.uniprot.org/annotation/VAR_065283|||http://purl.uniprot.org/annotation/VAR_065284|||http://purl.uniprot.org/annotation/VAR_065285|||http://purl.uniprot.org/annotation/VAR_065286|||http://purl.uniprot.org/annotation/VAR_065287|||http://purl.uniprot.org/annotation/VAR_065288|||http://purl.uniprot.org/annotation/VAR_079609|||http://purl.uniprot.org/annotation/VAR_081751
http://togogenome.org/gene/9606:TBC1D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPX1|||http://purl.uniprot.org/uniprot/Q8IZP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3|||TBC1 domain family member 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208025|||http://purl.uniprot.org/annotation/PRO_0000300265|||http://purl.uniprot.org/annotation/VAR_063088|||http://purl.uniprot.org/annotation/VSP_056829|||http://purl.uniprot.org/annotation/VSP_056830
http://togogenome.org/gene/9606:MCM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AHB0|||http://purl.uniprot.org/uniprot/P33992                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DNA replication licensing factor MCM5|||In MGORS8.|||MCM|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194107|||http://purl.uniprot.org/annotation/VAR_014813|||http://purl.uniprot.org/annotation/VAR_014814|||http://purl.uniprot.org/annotation/VAR_014815|||http://purl.uniprot.org/annotation/VAR_079198
http://togogenome.org/gene/9606:RBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50120                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Retinol-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067395
http://togogenome.org/gene/9606:CCDC47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In THNS; loss-of-function variant affecting ER calcium ion homeostasis in patient cells; no protein detected by Western blot in patient cells.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PAT complex subunit CCDC47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235797|||http://purl.uniprot.org/annotation/VAR_081926|||http://purl.uniprot.org/annotation/VAR_081927|||http://purl.uniprot.org/annotation/VSP_018478
http://togogenome.org/gene/9606:NIPAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0D2K0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In ARCI6.|||In ARCI6; frequent mutation.|||In isoform 2.|||Magnesium transporter NIPA4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284447|||http://purl.uniprot.org/annotation/VAR_031736|||http://purl.uniprot.org/annotation/VAR_031737|||http://purl.uniprot.org/annotation/VAR_031738|||http://purl.uniprot.org/annotation/VAR_031739|||http://purl.uniprot.org/annotation/VAR_031740|||http://purl.uniprot.org/annotation/VAR_054120|||http://purl.uniprot.org/annotation/VAR_075461|||http://purl.uniprot.org/annotation/VSP_036122
http://togogenome.org/gene/9606:ATXN2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BUF6|||http://purl.uniprot.org/uniprot/Q8WWM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Ataxin-2-like protein|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with MPL|||N-acetylmethionine|||N6-acetyllysine|||No effect on localization to stress granules under stress conditions.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064754|||http://purl.uniprot.org/annotation/VSP_011587|||http://purl.uniprot.org/annotation/VSP_011588|||http://purl.uniprot.org/annotation/VSP_011589|||http://purl.uniprot.org/annotation/VSP_011590|||http://purl.uniprot.org/annotation/VSP_011591|||http://purl.uniprot.org/annotation/VSP_011592|||http://purl.uniprot.org/annotation/VSP_011593|||http://purl.uniprot.org/annotation/VSP_011594|||http://purl.uniprot.org/annotation/VSP_044243|||http://purl.uniprot.org/annotation/VSP_047122
http://togogenome.org/gene/9606:MGST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99735                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Microsomal glutathione S-transferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217740|||http://purl.uniprot.org/annotation/VAR_019997|||http://purl.uniprot.org/annotation/VSP_044538
http://togogenome.org/gene/9606:TEPSIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-4 complex accessory subunit Tepsin|||Basic and acidic residues|||Decreased interaction with AP4B1 in vitro.|||Decreased interaction with AP4B1 in vitro; when associated with A-476.|||Decreased interaction with AP4B1 in vitro; when associated with S-476.|||Decreased interaction with AP4B1 in vitro; when associated with S-477.|||Decreased interaction with AP4E1 in vitro.|||Disordered|||ENTH|||In isoform 2.|||Interaction with AP4B1|||Interaction with AP4E1|||Loss of interaction with AP4B1 in vitro.|||Loss of interaction with AP4B1 in vitro; when associated with I-473.|||Loss of interaction with AP4B1 in vitro; when associated with Q-474.|||Loss of interaction with AP4B1 in vitro; when associated with S-470.|||Loss of interaction with AP4B1 in vitro; when associated with S-471.|||Loss of interaction with AP4B1 n vitro.|||Loss of interaction with AP4E1 in vitro.|||No effect on interaction with AP4B1 in vitro.|||No effect on interaction with AP4B1 in vitro. Decreased interaction with AP4B1; when associated with D-474.|||No effect on interaction with AP4E1 in vitro.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286678|||http://purl.uniprot.org/annotation/VSP_025141|||http://purl.uniprot.org/annotation/VSP_025142
http://togogenome.org/gene/9606:TATDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93075                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Putative deoxyribonuclease TATDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201993|||http://purl.uniprot.org/annotation/VAR_047028|||http://purl.uniprot.org/annotation/VAR_047029|||http://purl.uniprot.org/annotation/VAR_047030
http://togogenome.org/gene/9606:COL20A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P218                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Collagen alpha-1(XX) chain|||Collagen-like 1|||Collagen-like 2|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013986|||http://purl.uniprot.org/annotation/VAR_055671|||http://purl.uniprot.org/annotation/VSP_038876|||http://purl.uniprot.org/annotation/VSP_038877|||http://purl.uniprot.org/annotation/VSP_038878
http://togogenome.org/gene/9606:RIBC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N443                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||RIB43A-like with coiled-coils protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254093|||http://purl.uniprot.org/annotation/VSP_021178|||http://purl.uniprot.org/annotation/VSP_021179|||http://purl.uniprot.org/annotation/VSP_044834|||http://purl.uniprot.org/annotation/VSP_044835
http://togogenome.org/gene/9606:SEC23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15436                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased interaction with MIA3; when associated with A-628.|||Decreased interaction with MIA3; when associated with A-678.|||Decreased interaction with MIA3; when associated with A-681.|||Decreased interaction with MIA3; when associated with K-672.|||Gelsolin-like|||In CLSD; loss of COPII vesicle coating; results in absence of incorporation of cargo proteins into vesicles.|||In isoform 2.|||N-acetylthreonine|||Phosphothreonine|||Protein transport protein Sec23A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205146|||http://purl.uniprot.org/annotation/VAR_031029|||http://purl.uniprot.org/annotation/VAR_031030|||http://purl.uniprot.org/annotation/VSP_056230
http://togogenome.org/gene/9606:AGAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0Z1|||http://purl.uniprot.org/uniprot/Q96P64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 4|||Basic and acidic residues|||C4-type|||Disordered|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284673|||http://purl.uniprot.org/annotation/VAR_031804
http://togogenome.org/gene/9606:CAV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51636|||http://purl.uniprot.org/uniprot/Q53X57                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Caveolin-2|||Cytoplasmic|||Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated phosphorylation and binding of RASA1, SRC and NCK1; when associated with A-19.|||Greatly reduced Src-mediated phosphorylation and binding of RASA1, SRC and NCK1. Completely eliminates Src-mediated tyrosine phosphorylation and binding to RASA1, SRC and NCK1; when associated with A-27.|||Helical|||In isoform Beta.|||In isoform C.|||Phosphoserine|||Phosphotyrosine; by SRC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004772|||http://purl.uniprot.org/annotation/VAR_012071|||http://purl.uniprot.org/annotation/VSP_018696|||http://purl.uniprot.org/annotation/VSP_038114|||http://purl.uniprot.org/annotation/VSP_038115
http://togogenome.org/gene/9606:GP1BB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13224                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In BSS.|||In isoform 2.|||Interchain (with C-500 or C-501 in GP1BA)|||LRR|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKA|||Phosphothreonine|||Platelet glycoprotein Ib beta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021345|||http://purl.uniprot.org/annotation/VAR_025000|||http://purl.uniprot.org/annotation/VAR_025001|||http://purl.uniprot.org/annotation/VSP_032671
http://togogenome.org/gene/9606:SLC9A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVB4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In AUTS16.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Normal protein expression. Does not affect endosomal localizatiion. Fails to alkalinizes endosomal lumen.|||Normal protein expression. Fails to alkalinizes endosomal lumen. Does not affect endosomal localizatiion.|||Sodium/hydrogen exchanger 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052367|||http://purl.uniprot.org/annotation/VAR_022114|||http://purl.uniprot.org/annotation/VAR_050232|||http://purl.uniprot.org/annotation/VAR_087549
http://togogenome.org/gene/9606:SEC22C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2N5|||http://purl.uniprot.org/uniprot/Q9BRL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Longin|||Lumenal|||Vesicle-trafficking protein SEC22c                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324161|||http://purl.uniprot.org/annotation/VSP_032161|||http://purl.uniprot.org/annotation/VSP_032162|||http://purl.uniprot.org/annotation/VSP_032163|||http://purl.uniprot.org/annotation/VSP_032164
http://togogenome.org/gene/9606:CCDC142                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RM4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 142|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311260|||http://purl.uniprot.org/annotation/VAR_037210|||http://purl.uniprot.org/annotation/VSP_029497|||http://purl.uniprot.org/annotation/VSP_029498
http://togogenome.org/gene/9606:SEMA3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15041                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with CHARGE syndrome; unknown pathological significance.|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032317|||http://purl.uniprot.org/annotation/VAR_080476|||http://purl.uniprot.org/annotation/VAR_080477|||http://purl.uniprot.org/annotation/VAR_080478|||http://purl.uniprot.org/annotation/VAR_080479|||http://purl.uniprot.org/annotation/VSP_046237
http://togogenome.org/gene/9606:IFNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C2Z6|||http://purl.uniprot.org/uniprot/Q8IZI9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  40 fold decrease in antiviral activity.|||43 fold decrease in antiviral activity.|||46 fold decrease in antiviral activity.|||51 fold decrease in antiviral activity.|||650 fold decrease in antiviral activity.|||68 fold decrease in antiviral activity.|||Interferon lambda-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015510|||http://purl.uniprot.org/annotation/PRO_5030649993|||http://purl.uniprot.org/annotation/VAR_063419|||http://purl.uniprot.org/annotation/VAR_063420
http://togogenome.org/gene/9606:PCCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05166                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-CoA binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||In PA-2.|||In PA-2; affects heteromeric and homomeric assembly.|||In PA-2; does not affect either heteromeric or homomeric assembly.|||In PA-2; does not affect either heteromeric or homomeric assembly; decreased thermostability affecting holoenzyme oligomerization; no effect on propionyl-CoA carboxylase activity.|||In PA-2; likely benign variant.|||In PA-2; no effect on affinity for propionyl-CoA; decreased reaction kinetics for the propionyl-CoA carboxylase activity; decreased thermostability affecting holoenzyme oligomerization.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Propionyl-CoA carboxylase beta chain, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000293|||http://purl.uniprot.org/annotation/VAR_000271|||http://purl.uniprot.org/annotation/VAR_000272|||http://purl.uniprot.org/annotation/VAR_000273|||http://purl.uniprot.org/annotation/VAR_000274|||http://purl.uniprot.org/annotation/VAR_000275|||http://purl.uniprot.org/annotation/VAR_000276|||http://purl.uniprot.org/annotation/VAR_000277|||http://purl.uniprot.org/annotation/VAR_000278|||http://purl.uniprot.org/annotation/VAR_000279|||http://purl.uniprot.org/annotation/VAR_000280|||http://purl.uniprot.org/annotation/VAR_000281|||http://purl.uniprot.org/annotation/VAR_009080|||http://purl.uniprot.org/annotation/VAR_009081|||http://purl.uniprot.org/annotation/VAR_009082|||http://purl.uniprot.org/annotation/VAR_009083|||http://purl.uniprot.org/annotation/VAR_009084|||http://purl.uniprot.org/annotation/VAR_009085|||http://purl.uniprot.org/annotation/VAR_009086|||http://purl.uniprot.org/annotation/VAR_023847|||http://purl.uniprot.org/annotation/VAR_023848|||http://purl.uniprot.org/annotation/VAR_023849|||http://purl.uniprot.org/annotation/VAR_023850|||http://purl.uniprot.org/annotation/VAR_023851|||http://purl.uniprot.org/annotation/VAR_023852|||http://purl.uniprot.org/annotation/VAR_023853|||http://purl.uniprot.org/annotation/VAR_023854|||http://purl.uniprot.org/annotation/VAR_023855|||http://purl.uniprot.org/annotation/VAR_023856|||http://purl.uniprot.org/annotation/VAR_023857|||http://purl.uniprot.org/annotation/VAR_023858|||http://purl.uniprot.org/annotation/VAR_048163|||http://purl.uniprot.org/annotation/VSP_042568
http://togogenome.org/gene/9606:RASL11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Ras-like protein family member 11B|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308365
http://togogenome.org/gene/9606:DNAJA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YX3|||http://purl.uniprot.org/uniprot/Q8WW22                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CR-type|||CXXCXGXG motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily A member 4|||In isoform 2.|||In isoform 3.|||J|||Phosphoserine|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071014|||http://purl.uniprot.org/annotation/PRO_0000396760|||http://purl.uniprot.org/annotation/VAR_069064|||http://purl.uniprot.org/annotation/VSP_038965|||http://purl.uniprot.org/annotation/VSP_045696
http://togogenome.org/gene/9606:ZC3H12C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Probable ribonuclease ZC3H12C|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337843|||http://purl.uniprot.org/annotation/VSP_054127
http://togogenome.org/gene/9606:BORCS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BLOC-1-related complex subunit 5|||Disordered|||In isoform 2.|||Loss of myristoylation and loss of localization to lysosomal membranes.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318596|||http://purl.uniprot.org/annotation/VAR_038840|||http://purl.uniprot.org/annotation/VAR_038841|||http://purl.uniprot.org/annotation/VSP_031254
http://togogenome.org/gene/9606:CARMIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Capping protein, Arp2/3 and myosin-I linker protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Necessary for localization at the cell membrane|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324608|||http://purl.uniprot.org/annotation/VAR_039845|||http://purl.uniprot.org/annotation/VSP_032305|||http://purl.uniprot.org/annotation/VSP_032306|||http://purl.uniprot.org/annotation/VSP_032307|||http://purl.uniprot.org/annotation/VSP_032308|||http://purl.uniprot.org/annotation/VSP_032309
http://togogenome.org/gene/9606:PPM1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49593                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with sclerosing cholangitis short stature hypothyroidism and abnormal tongue pigmentation; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057758|||http://purl.uniprot.org/annotation/VAR_024580|||http://purl.uniprot.org/annotation/VAR_036520|||http://purl.uniprot.org/annotation/VAR_036521|||http://purl.uniprot.org/annotation/VAR_050620|||http://purl.uniprot.org/annotation/VAR_086701|||http://purl.uniprot.org/annotation/VSP_056483|||http://purl.uniprot.org/annotation/VSP_056484
http://togogenome.org/gene/9606:TYW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV66                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Flavodoxin-like|||In isoform 2.|||Radical SAM core|||S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281826|||http://purl.uniprot.org/annotation/VAR_031288|||http://purl.uniprot.org/annotation/VAR_031289|||http://purl.uniprot.org/annotation/VAR_031290|||http://purl.uniprot.org/annotation/VSP_024066|||http://purl.uniprot.org/annotation/VSP_024067
http://togogenome.org/gene/9606:DUOXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9Q6|||http://purl.uniprot.org/uniprot/B5M0B7|||http://purl.uniprot.org/uniprot/B5M0B8|||http://purl.uniprot.org/uniprot/B5M0C0|||http://purl.uniprot.org/uniprot/Q1HG43                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dual oxidase maturation factor 1|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264241|||http://purl.uniprot.org/annotation/VAR_029630|||http://purl.uniprot.org/annotation/VAR_057753|||http://purl.uniprot.org/annotation/VSP_021890|||http://purl.uniprot.org/annotation/VSP_021891
http://togogenome.org/gene/9606:GJA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48165|||http://purl.uniprot.org/uniprot/X5D7G1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-8 protein|||Gap junction protein cysteine-rich|||Helical|||In CTRCT1.|||In CTRCT1; cataract with microcornea.|||In CTRCT1; decreased gap junction channel activity.|||In CTRCT1; nuclear progressive cataract.|||In CTRCT1; severely decreased gap junction channel activity; does not localize to the cell membrane.|||In CTRCT1; unknown pathological significance.|||In CTRCT1; unknown pathological significance; abolishes localization to the plasma membrane and function.|||In CTRCT1; zonular pulverulent and nuclear progressive cataract.|||In CTRCT1; zonular pulverulent.|||Likely benign variant; does not affect gap junctions formation and gap junctional currents.|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057830|||http://purl.uniprot.org/annotation/VAR_002005|||http://purl.uniprot.org/annotation/VAR_037642|||http://purl.uniprot.org/annotation/VAR_038797|||http://purl.uniprot.org/annotation/VAR_038798|||http://purl.uniprot.org/annotation/VAR_038799|||http://purl.uniprot.org/annotation/VAR_038800|||http://purl.uniprot.org/annotation/VAR_038801|||http://purl.uniprot.org/annotation/VAR_069579|||http://purl.uniprot.org/annotation/VAR_070021|||http://purl.uniprot.org/annotation/VAR_070022|||http://purl.uniprot.org/annotation/VAR_084810|||http://purl.uniprot.org/annotation/VAR_084811|||http://purl.uniprot.org/annotation/VAR_084812|||http://purl.uniprot.org/annotation/VAR_084813|||http://purl.uniprot.org/annotation/VAR_084814|||http://purl.uniprot.org/annotation/VAR_084815|||http://purl.uniprot.org/annotation/VAR_084816|||http://purl.uniprot.org/annotation/VAR_086591|||http://purl.uniprot.org/annotation/VAR_086592
http://togogenome.org/gene/9606:FAM131B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94871|||http://purl.uniprot.org/uniprot/Q86XD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM131B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253032|||http://purl.uniprot.org/annotation/VAR_053920|||http://purl.uniprot.org/annotation/VSP_041633|||http://purl.uniprot.org/annotation/VSP_046798
http://togogenome.org/gene/9606:CD274                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0GN75|||http://purl.uniprot.org/uniprot/Q9NZQ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Largely abrogates multimerization, in vitro.|||N-linked (GlcNAc...) asparagine|||Programmed cell death 1 ligand 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014553|||http://purl.uniprot.org/annotation/PRO_5004172848|||http://purl.uniprot.org/annotation/VSP_013735|||http://purl.uniprot.org/annotation/VSP_013736|||http://purl.uniprot.org/annotation/VSP_013737|||http://purl.uniprot.org/annotation/VSP_061953
http://togogenome.org/gene/9606:MT1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13640                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Alpha|||Beta|||In isoform 2.|||Metallothionein-1G|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197238|||http://purl.uniprot.org/annotation/VSP_017230
http://togogenome.org/gene/9606:UGT1A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5DSZ6|||http://purl.uniprot.org/uniprot/Q9HAW9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In allele UGT1A8*2.|||In allele UGT1A8*3; dramatic reduction in catalytic activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036007|||http://purl.uniprot.org/annotation/PRO_5009998737|||http://purl.uniprot.org/annotation/VAR_015543|||http://purl.uniprot.org/annotation/VAR_015544|||http://purl.uniprot.org/annotation/VAR_015545|||http://purl.uniprot.org/annotation/VAR_015546|||http://purl.uniprot.org/annotation/VAR_015547|||http://purl.uniprot.org/annotation/VAR_015549|||http://purl.uniprot.org/annotation/VAR_052463|||http://purl.uniprot.org/annotation/VAR_058585|||http://purl.uniprot.org/annotation/VAR_058586|||http://purl.uniprot.org/annotation/VAR_061871|||http://purl.uniprot.org/annotation/VSP_053964
http://togogenome.org/gene/9606:FAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVX9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Fatty acyl-CoA reductase 1|||Helical|||In CSPSD.|||In CSPSD; increased ether lipid biosynthetic process in patient cells; increased FAR1 protein levels in patient cells due to impaired down-regulation by plasmalogen.|||In PFCRD; results in a complete loss of enzyme activity.|||Necessary and sufficient for PEX19-mediated localization into peroxisome membrane|||Peroxisomal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261394|||http://purl.uniprot.org/annotation/VAR_053800|||http://purl.uniprot.org/annotation/VAR_072692|||http://purl.uniprot.org/annotation/VAR_072693|||http://purl.uniprot.org/annotation/VAR_085710|||http://purl.uniprot.org/annotation/VAR_085711|||http://purl.uniprot.org/annotation/VAR_085712|||http://purl.uniprot.org/annotation/VAR_085713
http://togogenome.org/gene/9606:OR6J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGC5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150628|||http://purl.uniprot.org/annotation/VAR_087850
http://togogenome.org/gene/9606:TRIP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PGG9|||http://purl.uniprot.org/uniprot/A0A6Q8PHK0|||http://purl.uniprot.org/uniprot/A0A994J4J0|||http://purl.uniprot.org/uniprot/A0A994J569|||http://purl.uniprot.org/uniprot/A0A994J755|||http://purl.uniprot.org/uniprot/H7C1L9|||http://purl.uniprot.org/uniprot/Q14669                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIP12|||Glycyl thioester intermediate|||HECT|||In CLABARS.|||In CLABARS; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||K-box|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173872|||http://purl.uniprot.org/annotation/VAR_080431|||http://purl.uniprot.org/annotation/VAR_080432|||http://purl.uniprot.org/annotation/VAR_080433|||http://purl.uniprot.org/annotation/VAR_080434|||http://purl.uniprot.org/annotation/VAR_080435|||http://purl.uniprot.org/annotation/VAR_080436|||http://purl.uniprot.org/annotation/VAR_080437|||http://purl.uniprot.org/annotation/VAR_080438|||http://purl.uniprot.org/annotation/VSP_044326|||http://purl.uniprot.org/annotation/VSP_044327|||http://purl.uniprot.org/annotation/VSP_044328|||http://purl.uniprot.org/annotation/VSP_044329
http://togogenome.org/gene/9606:CCDC172                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7W6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 172                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344513
http://togogenome.org/gene/9606:CD79A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11912                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT1|||B-cell antigen receptor complex-associated protein alpha chain|||Cytoplasmic|||Extracellular|||Helical|||ITAM|||Ig-like C2-type|||In isoform 2.|||Increased phosphorylation of Y-188; when associated with A-197 and A-203.|||Increased phosphorylation of Y-188; when associated with A-197 and V-209.|||Increased phosphorylation of Y-188; when associated with A-203 and V-209.|||Interchain (with C-136 in beta chain)|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases|||Phosphotyrosine; by Tyr-kinases|||Required for binding to BLNK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014558|||http://purl.uniprot.org/annotation/VSP_002476
http://togogenome.org/gene/9606:THAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBB0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  HCFC1-binding motif (HBM)|||In isoform 2.|||In isoform 3.|||THAP domain-containing protein 6|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068647|||http://purl.uniprot.org/annotation/VSP_039072|||http://purl.uniprot.org/annotation/VSP_054378
http://togogenome.org/gene/9606:NSFL1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FE8|||http://purl.uniprot.org/uniprot/Q9UNZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NSFL1 cofactor p47|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SEP|||UBX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210988|||http://purl.uniprot.org/annotation/VAR_017481|||http://purl.uniprot.org/annotation/VSP_009262|||http://purl.uniprot.org/annotation/VSP_009263|||http://purl.uniprot.org/annotation/VSP_041062
http://togogenome.org/gene/9606:MCAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVS2                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Malonyl-CoA-acyl carrier protein transacylase, mitochondrial|||Mitochondrion|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000589|||http://purl.uniprot.org/annotation/VAR_048183|||http://purl.uniprot.org/annotation/VSP_010517|||http://purl.uniprot.org/annotation/VSP_010518
http://togogenome.org/gene/9606:COX6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H6SG15|||http://purl.uniprot.org/uniprot/P12074                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 6A1, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006119
http://togogenome.org/gene/9606:TSPAN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75954                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219253
http://togogenome.org/gene/9606:ANKRD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3D2|||http://purl.uniprot.org/uniprot/Q9Y2G4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat domain-containing protein 6|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066901|||http://purl.uniprot.org/annotation/VAR_039114|||http://purl.uniprot.org/annotation/VAR_039115|||http://purl.uniprot.org/annotation/VAR_039116|||http://purl.uniprot.org/annotation/VAR_039117|||http://purl.uniprot.org/annotation/VAR_055506|||http://purl.uniprot.org/annotation/VSP_000270|||http://purl.uniprot.org/annotation/VSP_031591|||http://purl.uniprot.org/annotation/VSP_043189|||http://purl.uniprot.org/annotation/VSP_043190
http://togogenome.org/gene/9606:INSL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Q6                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Connecting peptide|||Insulin-like peptide INSL5 A chain|||Insulin-like peptide INSL5 B chain|||Interchain (between B and A chains)|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016163|||http://purl.uniprot.org/annotation/PRO_0000016164|||http://purl.uniprot.org/annotation/PRO_0000016165|||http://purl.uniprot.org/annotation/VAR_046099
http://togogenome.org/gene/9606:ZNF579                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAF0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Pro residues|||Zinc finger protein 579                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047669|||http://purl.uniprot.org/annotation/VAR_061956
http://togogenome.org/gene/9606:STAMBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK54|||http://purl.uniprot.org/uniprot/A0A804HIF8|||http://purl.uniprot.org/uniprot/O95630                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MICCAP.|||In isoform 2.|||Indirect zinc-binding|||Interaction with CHMP3|||Interaction with STAM|||JAMM motif|||MPN|||Phosphoserine|||Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization.|||STAM-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194869|||http://purl.uniprot.org/annotation/VAR_069806|||http://purl.uniprot.org/annotation/VAR_069807|||http://purl.uniprot.org/annotation/VAR_069808|||http://purl.uniprot.org/annotation/VAR_069809|||http://purl.uniprot.org/annotation/VAR_069810|||http://purl.uniprot.org/annotation/VAR_069811|||http://purl.uniprot.org/annotation/VSP_057197
http://togogenome.org/gene/9606:TNFSF13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5J7Q1|||http://purl.uniprot.org/uniprot/Q9Y275                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNF family profile|||Tumor necrosis factor ligand superfamily member 13b, membrane form|||Tumor necrosis factor ligand superfamily member 13b, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034528|||http://purl.uniprot.org/annotation/PRO_0000034529|||http://purl.uniprot.org/annotation/VAR_013483|||http://purl.uniprot.org/annotation/VSP_041183|||http://purl.uniprot.org/annotation/VSP_047591|||http://purl.uniprot.org/annotation/VSP_047592
http://togogenome.org/gene/9606:CSDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y534                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  CSD|||Cold shock domain-containing protein C2|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100351
http://togogenome.org/gene/9606:COPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXC6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  COP9 signalosome complex subunit 9|||Decreases interaction with CSN complex. Abolishes interaction with CSN complex; when associated with A-44.|||Does not abolish interaction with CSN complex. Abolishes interaction with CSN complex; when associated with A-51.|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332924|||http://purl.uniprot.org/annotation/VSP_037073|||http://purl.uniprot.org/annotation/VSP_037074|||http://purl.uniprot.org/annotation/VSP_037075
http://togogenome.org/gene/9606:SCARF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6Z5|||http://purl.uniprot.org/uniprot/Q14162                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Scavenger receptor class F member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007738|||http://purl.uniprot.org/annotation/PRO_5002725467|||http://purl.uniprot.org/annotation/VAR_047249|||http://purl.uniprot.org/annotation/VAR_047250|||http://purl.uniprot.org/annotation/VAR_047251|||http://purl.uniprot.org/annotation/VAR_047252|||http://purl.uniprot.org/annotation/VAR_047253|||http://purl.uniprot.org/annotation/VAR_047254|||http://purl.uniprot.org/annotation/VSP_039956|||http://purl.uniprot.org/annotation/VSP_039957|||http://purl.uniprot.org/annotation/VSP_039958|||http://purl.uniprot.org/annotation/VSP_039959|||http://purl.uniprot.org/annotation/VSP_039960|||http://purl.uniprot.org/annotation/VSP_039961
http://togogenome.org/gene/9606:SLC17A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2U7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Vesicular glutamate transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331611|||http://purl.uniprot.org/annotation/VAR_042904|||http://purl.uniprot.org/annotation/VSP_056110|||http://purl.uniprot.org/annotation/VSP_056111
http://togogenome.org/gene/9606:ADAM19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBU7|||http://purl.uniprot.org/uniprot/Q9H013                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 19|||Disordered|||EGF-like|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues|||Pro residues|||SH3-binding|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029102|||http://purl.uniprot.org/annotation/PRO_0000029103|||http://purl.uniprot.org/annotation/VAR_036146|||http://purl.uniprot.org/annotation/VAR_036147|||http://purl.uniprot.org/annotation/VAR_057066|||http://purl.uniprot.org/annotation/VAR_062670|||http://purl.uniprot.org/annotation/VSP_005481
http://togogenome.org/gene/9606:SPAG17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Q759                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In SPGF55; unknown pathological significance; decreased protein expression in homozygous patient sperm.|||In a colorectal cancer sample; somatic mutation.|||Polar residues|||Sperm-associated antigen 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331445|||http://purl.uniprot.org/annotation/VAR_042863|||http://purl.uniprot.org/annotation/VAR_042864|||http://purl.uniprot.org/annotation/VAR_042865|||http://purl.uniprot.org/annotation/VAR_042866|||http://purl.uniprot.org/annotation/VAR_042867|||http://purl.uniprot.org/annotation/VAR_085965
http://togogenome.org/gene/9606:DGKI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV00|||http://purl.uniprot.org/uniprot/E9PFX6|||http://purl.uniprot.org/uniprot/O75912|||http://purl.uniprot.org/uniprot/Q59GE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Basic residues|||DAGKc|||Diacylglycerol kinase iota|||Disordered|||PDZ-binding|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218466|||http://purl.uniprot.org/annotation/VAR_010190
http://togogenome.org/gene/9606:SPIDR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14159                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA repair-scaffolding protein|||Disordered|||In ODG9; changed double-strand break repair via homologous recombination.|||In ODG9; patient cells demonstrated a marked increase in mitomycin-induced chromosomal breaks compared to wild-type cells.|||In isoform 2.|||In isoform 3.|||Necessary for interaction with RAD51|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251720|||http://purl.uniprot.org/annotation/VAR_086691|||http://purl.uniprot.org/annotation/VAR_086692|||http://purl.uniprot.org/annotation/VSP_056652|||http://purl.uniprot.org/annotation/VSP_056653|||http://purl.uniprot.org/annotation/VSP_056654
http://togogenome.org/gene/9606:INAFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JVW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Pro residues|||Putative transmembrane protein INAFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394048
http://togogenome.org/gene/9606:INAVA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8N8P9|||http://purl.uniprot.org/uniprot/Q3KP66                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytohesin Ubiquitin Protein Inducing|||Decreases interaction with YWHAQ, cellular signaling pathway activation and cytokine secretion.|||Disordered|||In IBD29; decreases protein stability.|||In isoform 2.|||Innate immunity activator protein|||No effect on nuclear translocation upon induction by MDP. Abolishes nuclear translocation upon induction by MDP and slightly decreases NOD2-induced AP-1 and NF-kappaB activation and IL6 secretion; when associated with 164-A--A-170 and 335-A--A-338.|||No effect on nuclear translocation upon induction by MDP. Abolishes nuclear translocation upon induction by MDP and slightly decreases NOD2-induced AP-1 and NF-kappaB activation and IL6 secretion; when associated with 164-A--A-170 and 423-A--A-426.|||No effect on nuclear translocation upon induction by MDP. Abolishes nuclear translocation upon induction by MDP and slightly decreases NOD2-induced AP-1 and NF-kappaB activation and IL6 secretion; when associated with 335-A--A-338 and 423-A--A-426.|||Nuclear localization signal (NLS) 1|||Nuclear localization signal (NLS) 2|||Nuclear localization signal (NLS) 3|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251729|||http://purl.uniprot.org/annotation/VAR_030835|||http://purl.uniprot.org/annotation/VAR_080249|||http://purl.uniprot.org/annotation/VSP_046048
http://togogenome.org/gene/9606:FGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02671                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline; by P4HA1|||Alpha-chain polymerization, binding distal domain of another fibrin gamma chain|||Basic and acidic residues|||Cleavage; by hementin; to prevent blood coagulation|||Cleavage; by plasmin; to break down fibrin clots|||Cleavage; by thrombin; to release fibrinopeptide A|||Disordered|||Fibrinogen C-terminal|||Fibrinogen alpha chain|||Fibrinopeptide A|||In AMYL8.|||In Aarhus-1.|||In CAFBN; hypofibrinogenemia; heterozygous; decreased fibrinogen complex assembly; no effect on fibrinogen complex secretion.|||In CAFBN; hypofibrinogenemia; heterozygous; impaired fibrinogen complex assembly.|||In CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion.|||In Canterbury.|||In Caracas-2.|||In DYSFIBRIN; fibrinogen Dusart/Paris-5.|||In DYSFIBRIN; fibrinogen Metz 1/Hershey III.|||In Detroit-1.|||In Kyoto-2.|||In Lille-1.|||In Lima.|||In Munich-1; requires 2 nucleotide substitutions.|||In Rouen-1.|||In isoform 2.|||Interchain|||Interchain (with C-106 in beta chain)|||Interchain (with C-165 in gamma chain)|||Interchain (with C-223 in beta chain)|||Interchain (with C-49 in gamma chain)|||Interchain (with C-95 in beta chain)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; in variant Caracas-2|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009021|||http://purl.uniprot.org/annotation/PRO_0000009022|||http://purl.uniprot.org/annotation/VAR_002390|||http://purl.uniprot.org/annotation/VAR_002391|||http://purl.uniprot.org/annotation/VAR_002392|||http://purl.uniprot.org/annotation/VAR_002393|||http://purl.uniprot.org/annotation/VAR_002394|||http://purl.uniprot.org/annotation/VAR_002395|||http://purl.uniprot.org/annotation/VAR_002396|||http://purl.uniprot.org/annotation/VAR_002397|||http://purl.uniprot.org/annotation/VAR_002398|||http://purl.uniprot.org/annotation/VAR_002399|||http://purl.uniprot.org/annotation/VAR_002400|||http://purl.uniprot.org/annotation/VAR_002401|||http://purl.uniprot.org/annotation/VAR_010730|||http://purl.uniprot.org/annotation/VAR_010731|||http://purl.uniprot.org/annotation/VAR_010732|||http://purl.uniprot.org/annotation/VAR_011609|||http://purl.uniprot.org/annotation/VAR_011610|||http://purl.uniprot.org/annotation/VAR_011611|||http://purl.uniprot.org/annotation/VAR_014168|||http://purl.uniprot.org/annotation/VAR_072721|||http://purl.uniprot.org/annotation/VAR_072722|||http://purl.uniprot.org/annotation/VAR_072723|||http://purl.uniprot.org/annotation/VSP_001531|||http://purl.uniprot.org/annotation/VSP_001532
http://togogenome.org/gene/9606:PPP2CB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJS0|||http://purl.uniprot.org/uniprot/P62714                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Catalytically inactive. No effect on interaction with PPME1.|||Leucine methyl ester|||Phosphotyrosine|||Proton donor|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058845
http://togogenome.org/gene/9606:POLR3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DH01|||http://purl.uniprot.org/uniprot/Q9NVU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||DNA-directed RNA polymerase III subunit RPC5|||DNA-directed RNA polymerase III subunit RPC5 C-terminal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073970|||http://purl.uniprot.org/annotation/VAR_024623|||http://purl.uniprot.org/annotation/VSP_007064|||http://purl.uniprot.org/annotation/VSP_007065|||http://purl.uniprot.org/annotation/VSP_044710|||http://purl.uniprot.org/annotation/VSP_046374
http://togogenome.org/gene/9606:ZNF709                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N972                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 709                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230312
http://togogenome.org/gene/9606:EXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3'-5' exonuclease|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||piRNA biogenesis protein EXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337244|||http://purl.uniprot.org/annotation/VAR_043676|||http://purl.uniprot.org/annotation/VSP_033987|||http://purl.uniprot.org/annotation/VSP_054898
http://togogenome.org/gene/9606:ZSCAN26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCN4|||http://purl.uniprot.org/uniprot/A0A087X2F1|||http://purl.uniprot.org/uniprot/B3KTR1|||http://purl.uniprot.org/uniprot/B4DMT1|||http://purl.uniprot.org/uniprot/B4DVH3|||http://purl.uniprot.org/uniprot/Q16670                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||SCAN box|||Zinc finger and SCAN domain-containing protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307313|||http://purl.uniprot.org/annotation/VAR_035405|||http://purl.uniprot.org/annotation/VAR_059900|||http://purl.uniprot.org/annotation/VAR_059901|||http://purl.uniprot.org/annotation/VAR_059902|||http://purl.uniprot.org/annotation/VSP_028702
http://togogenome.org/gene/9606:CCL28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0Q3|||http://purl.uniprot.org/uniprot/D6RC73|||http://purl.uniprot.org/uniprot/Q9NRJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C-C motif chemokine|||C-C motif chemokine 28|||Chemokine interleukin-8-like|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005242|||http://purl.uniprot.org/annotation/PRO_5014205098|||http://purl.uniprot.org/annotation/VSP_047735
http://togogenome.org/gene/9606:TDO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48775                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||In HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization.|||Reduces enzyme activity by 90%.|||Reduces enzyme activity by 99%.|||Reduces enzyme activity.|||Tryptophan 2,3-dioxygenase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072399|||http://purl.uniprot.org/annotation/VAR_080251
http://togogenome.org/gene/9606:TTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRA3|||http://purl.uniprot.org/uniprot/A0A0A0MTS7|||http://purl.uniprot.org/uniprot/Q7Z3B7|||http://purl.uniprot.org/uniprot/Q8WZ42                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Disrupts catalytic activity.|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 100|||Fibronectin type-III 101|||Fibronectin type-III 102|||Fibronectin type-III 103|||Fibronectin type-III 104|||Fibronectin type-III 105|||Fibronectin type-III 106|||Fibronectin type-III 107|||Fibronectin type-III 108|||Fibronectin type-III 109|||Fibronectin type-III 11|||Fibronectin type-III 110|||Fibronectin type-III 111|||Fibronectin type-III 112|||Fibronectin type-III 113|||Fibronectin type-III 114|||Fibronectin type-III 115|||Fibronectin type-III 116|||Fibronectin type-III 117|||Fibronectin type-III 118|||Fibronectin type-III 119|||Fibronectin type-III 12|||Fibronectin type-III 120|||Fibronectin type-III 121|||Fibronectin type-III 122|||Fibronectin type-III 123|||Fibronectin type-III 124|||Fibronectin type-III 125|||Fibronectin type-III 126|||Fibronectin type-III 127|||Fibronectin type-III 128|||Fibronectin type-III 129|||Fibronectin type-III 13|||Fibronectin type-III 130|||Fibronectin type-III 131|||Fibronectin type-III 132|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 18|||Fibronectin type-III 19|||Fibronectin type-III 2|||Fibronectin type-III 20|||Fibronectin type-III 21|||Fibronectin type-III 22|||Fibronectin type-III 23|||Fibronectin type-III 24|||Fibronectin type-III 25|||Fibronectin type-III 26|||Fibronectin type-III 27|||Fibronectin type-III 28|||Fibronectin type-III 29|||Fibronectin type-III 3|||Fibronectin type-III 30|||Fibronectin type-III 31|||Fibronectin type-III 32|||Fibronectin type-III 33|||Fibronectin type-III 34|||Fibronectin type-III 35|||Fibronectin type-III 36|||Fibronectin type-III 37|||Fibronectin type-III 38|||Fibronectin type-III 39|||Fibronectin type-III 4|||Fibronectin type-III 40|||Fibronectin type-III 41|||Fibronectin type-III 42|||Fibronectin type-III 43|||Fibronectin type-III 44|||Fibronectin type-III 45|||Fibronectin type-III 46|||Fibronectin type-III 47|||Fibronectin type-III 48|||Fibronectin type-III 49|||Fibronectin type-III 5|||Fibronectin type-III 50|||Fibronectin type-III 51|||Fibronectin type-III 52|||Fibronectin type-III 53|||Fibronectin type-III 54|||Fibronectin type-III 55|||Fibronectin type-III 56|||Fibronectin type-III 57|||Fibronectin type-III 58|||Fibronectin type-III 59|||Fibronectin type-III 6|||Fibronectin type-III 60|||Fibronectin type-III 61|||Fibronectin type-III 62|||Fibronectin type-III 63|||Fibronectin type-III 64|||Fibronectin type-III 65|||Fibronectin type-III 66|||Fibronectin type-III 67|||Fibronectin type-III 68|||Fibronectin type-III 69|||Fibronectin type-III 7|||Fibronectin type-III 70|||Fibronectin type-III 71|||Fibronectin type-III 72|||Fibronectin type-III 73|||Fibronectin type-III 74|||Fibronectin type-III 75|||Fibronectin type-III 76|||Fibronectin type-III 77|||Fibronectin type-III 78|||Fibronectin type-III 79|||Fibronectin type-III 8|||Fibronectin type-III 80|||Fibronectin type-III 81|||Fibronectin type-III 82|||Fibronectin type-III 83|||Fibronectin type-III 84|||Fibronectin type-III 85|||Fibronectin type-III 86|||Fibronectin type-III 87|||Fibronectin type-III 88|||Fibronectin type-III 89|||Fibronectin type-III 9|||Fibronectin type-III 90|||Fibronectin type-III 91|||Fibronectin type-III 92|||Fibronectin type-III 93|||Fibronectin type-III 94|||Fibronectin type-III 95|||Fibronectin type-III 96|||Fibronectin type-III 97|||Fibronectin type-III 98|||Fibronectin type-III 99|||Ig-like|||Ig-like 1|||Ig-like 10|||Ig-like 100|||Ig-like 101|||Ig-like 102|||Ig-like 103|||Ig-like 104|||Ig-like 105|||Ig-like 106|||Ig-like 107|||Ig-like 108|||Ig-like 109|||Ig-like 11|||Ig-like 110|||Ig-like 111|||Ig-like 112|||Ig-like 113|||Ig-like 114|||Ig-like 115|||Ig-like 116|||Ig-like 117|||Ig-like 118|||Ig-like 119|||Ig-like 12|||Ig-like 120|||Ig-like 121|||Ig-like 122|||Ig-like 123|||Ig-like 124|||Ig-like 125|||Ig-like 126|||Ig-like 127|||Ig-like 128|||Ig-like 129|||Ig-like 13|||Ig-like 130|||Ig-like 131|||Ig-like 132|||Ig-like 133|||Ig-like 134|||Ig-like 135|||Ig-like 136|||Ig-like 137|||Ig-like 138|||Ig-like 139|||Ig-like 14|||Ig-like 140|||Ig-like 141|||Ig-like 142|||Ig-like 143|||Ig-like 144|||Ig-like 145|||Ig-like 146|||Ig-like 147|||Ig-like 148|||Ig-like 149|||Ig-like 15|||Ig-like 150|||Ig-like 151|||Ig-like 152|||Ig-like 16|||Ig-like 17|||Ig-like 18|||Ig-like 19|||Ig-like 2|||Ig-like 20|||Ig-like 21|||Ig-like 22|||Ig-like 23|||Ig-like 24|||Ig-like 25|||Ig-like 26|||Ig-like 27|||Ig-like 28|||Ig-like 29|||Ig-like 3|||Ig-like 30|||Ig-like 31|||Ig-like 32|||Ig-like 33|||Ig-like 34|||Ig-like 35|||Ig-like 36|||Ig-like 37|||Ig-like 38|||Ig-like 39|||Ig-like 4|||Ig-like 40|||Ig-like 41|||Ig-like 42|||Ig-like 43|||Ig-like 44|||Ig-like 45|||Ig-like 46|||Ig-like 47|||Ig-like 48|||Ig-like 49|||Ig-like 5|||Ig-like 50|||Ig-like 51|||Ig-like 52|||Ig-like 53|||Ig-like 54|||Ig-like 55|||Ig-like 56|||Ig-like 57|||Ig-like 58|||Ig-like 59|||Ig-like 6|||Ig-like 60|||Ig-like 61|||Ig-like 62|||Ig-like 63|||Ig-like 64|||Ig-like 65|||Ig-like 66|||Ig-like 67|||Ig-like 68|||Ig-like 69|||Ig-like 7|||Ig-like 70|||Ig-like 71|||Ig-like 72|||Ig-like 73|||Ig-like 74|||Ig-like 75|||Ig-like 76|||Ig-like 77|||Ig-like 78|||Ig-like 79|||Ig-like 8|||Ig-like 80|||Ig-like 81|||Ig-like 82|||Ig-like 83|||Ig-like 84|||Ig-like 85|||Ig-like 86|||Ig-like 87|||Ig-like 88|||Ig-like 89|||Ig-like 9|||Ig-like 90|||Ig-like 91|||Ig-like 92|||Ig-like 93|||Ig-like 94|||Ig-like 95|||Ig-like 96|||Ig-like 97|||Ig-like 98|||Ig-like 99|||In CMD1G.|||In CMD1G; affects interaction with TCAP/telethonin.|||In CMH9.|||In MFM9; disrupts NBR1-binding.|||In TMD.|||In a Wilms tumor; somatic mutation.|||In a bladder carcinoma sample; somatic mutation.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a head and neck squamous cell carcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In a renal chromophobe cancer sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3, isoform 9 and isoform 10.|||In isoform 4 and isoform 11.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 10.|||In isoform 9.|||No phosphorylation on tyrosine.|||PEVK 1|||PEVK 10|||PEVK 11|||PEVK 12|||PEVK 13|||PEVK 14|||PEVK 15|||PEVK 16|||PEVK 17|||PEVK 18|||PEVK 19|||PEVK 2|||PEVK 20|||PEVK 21|||PEVK 22|||PEVK 23|||PEVK 24|||PEVK 25|||PEVK 26|||PEVK 27|||PEVK 28|||PEVK 29|||PEVK 3|||PEVK 30|||PEVK 31|||PEVK 4|||PEVK 5|||PEVK 6|||PEVK 7|||PEVK 8|||PEVK 9|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Titin|||Z-repeat 1|||Z-repeat 2|||Z-repeat 3|||Z-repeat 4|||Z-repeat 5|||Z-repeat 6|||Z-repeat 7|||ZIS1|||ZIS5 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239311|||http://purl.uniprot.org/annotation/VAR_026634|||http://purl.uniprot.org/annotation/VAR_026635|||http://purl.uniprot.org/annotation/VAR_026636|||http://purl.uniprot.org/annotation/VAR_026685|||http://purl.uniprot.org/annotation/VAR_026686|||http://purl.uniprot.org/annotation/VAR_026687|||http://purl.uniprot.org/annotation/VAR_026688|||http://purl.uniprot.org/annotation/VAR_026689|||http://purl.uniprot.org/annotation/VAR_026690|||http://purl.uniprot.org/annotation/VAR_026691|||http://purl.uniprot.org/annotation/VAR_026692|||http://purl.uniprot.org/annotation/VAR_026693|||http://purl.uniprot.org/annotation/VAR_026694|||http://purl.uniprot.org/annotation/VAR_026695|||http://purl.uniprot.org/annotation/VAR_040078|||http://purl.uniprot.org/annotation/VAR_040079|||http://purl.uniprot.org/annotation/VAR_040080|||http://purl.uniprot.org/annotation/VAR_040081|||http://purl.uniprot.org/annotation/VAR_040082|||http://purl.uniprot.org/annotation/VAR_040083|||http://purl.uniprot.org/annotation/VAR_040084|||http://purl.uniprot.org/annotation/VAR_040085|||http://purl.uniprot.org/annotation/VAR_040086|||http://purl.uniprot.org/annotation/VAR_040087|||http://purl.uniprot.org/annotation/VAR_040088|||http://purl.uniprot.org/annotation/VAR_040089|||http://purl.uniprot.org/annotation/VAR_040090|||http://purl.uniprot.org/annotation/VAR_040091|||http://purl.uniprot.org/annotation/VAR_040092|||http://purl.uniprot.org/annotation/VAR_040093|||http://purl.uniprot.org/annotation/VAR_040094|||http://purl.uniprot.org/annotation/VAR_040095|||http://purl.uniprot.org/annotation/VAR_040096|||http://purl.uniprot.org/annotation/VAR_040097|||http://purl.uniprot.org/annotation/VAR_040098|||http://purl.uniprot.org/annotation/VAR_040099|||http://purl.uniprot.org/annotation/VAR_040100|||http://purl.uniprot.org/annotation/VAR_040101|||http://purl.uniprot.org/annotation/VAR_040102|||http://purl.uniprot.org/annotation/VAR_040103|||http://purl.uniprot.org/annotation/VAR_040104|||http://purl.uniprot.org/annotation/VAR_040105|||http://purl.uniprot.org/annotation/VAR_040106|||http://purl.uniprot.org/annotation/VAR_040107|||http://purl.uniprot.org/annotation/VAR_040108|||http://purl.uniprot.org/annotation/VAR_040109|||http://purl.uniprot.org/annotation/VAR_040110|||http://purl.uniprot.org/annotation/VAR_040111|||http://purl.uniprot.org/annotation/VAR_040112|||http://purl.uniprot.org/annotation/VAR_040113|||http://purl.uniprot.org/annotation/VAR_040114|||http://purl.uniprot.org/annotation/VAR_040115|||http://purl.uniprot.org/annotation/VAR_040116|||http://purl.uniprot.org/annotation/VAR_040117|||http://purl.uniprot.org/annotation/VAR_040118|||http://purl.uniprot.org/annotation/VAR_040119|||http://purl.uniprot.org/annotation/VAR_040120|||http://purl.uniprot.org/annotation/VAR_040121|||http://purl.uniprot.org/annotation/VAR_040122|||http://purl.uniprot.org/annotation/VAR_040123|||http://purl.uniprot.org/annotation/VAR_040124|||http://purl.uniprot.org/annotation/VAR_040125|||http://purl.uniprot.org/annotation/VAR_040126|||http://purl.uniprot.org/annotation/VAR_040127|||http://purl.uniprot.org/annotation/VAR_040128|||http://purl.uniprot.org/annotation/VAR_040129|||http://purl.uniprot.org/annotation/VAR_040130|||http://purl.uniprot.org/annotation/VAR_040131|||http://purl.uniprot.org/annotation/VAR_040132|||http://purl.uniprot.org/annotation/VAR_040133|||http://purl.uniprot.org/annotation/VAR_040134|||http://purl.uniprot.org/annotation/VAR_040135|||http://purl.uniprot.org/annotation/VAR_040136|||http://purl.uniprot.org/annotation/VAR_040137|||http://purl.uniprot.org/annotation/VAR_040138|||http://purl.uniprot.org/annotation/VAR_040139|||http://purl.uniprot.org/annotation/VAR_040140|||http://purl.uniprot.org/annotation/VAR_040141|||http://purl.uniprot.org/annotation/VAR_040142|||http://purl.uniprot.org/annotation/VAR_040143|||http://purl.uniprot.org/annotation/VAR_040144|||http://purl.uniprot.org/annotation/VAR_040145|||http://purl.uniprot.org/annotation/VAR_040146|||http://purl.uniprot.org/annotation/VAR_040147|||http://purl.uniprot.org/annotation/VAR_040148|||http://purl.uniprot.org/annotation/VAR_040149|||http://purl.uniprot.org/annotation/VAR_040150|||http://purl.uniprot.org/annotation/VAR_040151|||http://purl.uniprot.org/annotation/VAR_040152|||http://purl.uniprot.org/annotation/VAR_040153|||http://purl.uniprot.org/annotation/VAR_040154|||http://purl.uniprot.org/annotation/VAR_040155|||http://purl.uniprot.org/annotation/VAR_040156|||http://purl.uniprot.org/annotation/VAR_040157|||http://purl.uniprot.org/annotation/VAR_040158|||http://purl.uniprot.org/annotation/VAR_040159|||http://purl.uniprot.org/annotation/VAR_040160|||http://purl.uniprot.org/annotation/VAR_040161|||http://purl.uniprot.org/annotation/VAR_040162|||http://purl.uniprot.org/annotation/VAR_040163|||http://purl.uniprot.org/annotation/VAR_040164|||http://purl.uniprot.org/annotation/VAR_040165|||http://purl.uniprot.org/annotation/VAR_040166|||http://purl.uniprot.org/annotation/VAR_040167|||http://purl.uniprot.org/annotation/VAR_040168|||http://purl.uniprot.org/annotation/VAR_040169|||http://purl.uniprot.org/annotation/VAR_040170|||http://purl.uniprot.org/annotation/VAR_040171|||http://purl.uniprot.org/annotation/VAR_040172|||http://purl.uniprot.org/annotation/VAR_040173|||http://purl.uniprot.org/annotation/VAR_040174|||http://purl.uniprot.org/annotation/VAR_040175|||http://purl.uniprot.org/annotation/VAR_040176|||http://purl.uniprot.org/annotation/VAR_040177|||http://purl.uniprot.org/annotation/VAR_040178|||http://purl.uniprot.org/annotation/VAR_040179|||http://purl.uniprot.org/annotation/VAR_040180|||http://purl.uniprot.org/annotation/VAR_040181|||http://purl.uniprot.org/annotation/VAR_040182|||http://purl.uniprot.org/annotation/VAR_040183|||http://purl.uniprot.org/annotation/VAR_040184|||http://purl.uniprot.org/annotation/VAR_040185|||http://purl.uniprot.org/annotation/VAR_040186|||http://purl.uniprot.org/annotation/VAR_040187|||http://purl.uniprot.org/annotation/VAR_040188|||http://purl.uniprot.org/annotation/VAR_040189|||http://purl.uniprot.org/annotation/VAR_040190|||http://purl.uniprot.org/annotation/VAR_040191|||http://purl.uniprot.org/annotation/VAR_040192|||http://purl.uniprot.org/annotation/VAR_040193|||http://purl.uniprot.org/annotation/VAR_040194|||http://purl.uniprot.org/annotation/VAR_040195|||http://purl.uniprot.org/annotation/VAR_040196|||http://purl.uniprot.org/annotation/VAR_040197|||http://purl.uniprot.org/annotation/VAR_040198|||http://purl.uniprot.org/annotation/VAR_040199|||http://purl.uniprot.org/annotation/VAR_040200|||http://purl.uniprot.org/annotation/VAR_040201|||http://purl.uniprot.org/annotation/VAR_040202|||http://purl.uniprot.org/annotation/VAR_040203|||http://purl.uniprot.org/annotation/VAR_040204|||http://purl.uniprot.org/annotation/VAR_040205|||http://purl.uniprot.org/annotation/VAR_040206|||http://purl.uniprot.org/annotation/VAR_040207|||http://purl.uniprot.org/annotation/VAR_040208|||http://purl.uniprot.org/annotation/VAR_040209|||http://purl.uniprot.org/annotation/VAR_040210|||http://purl.uniprot.org/annotation/VAR_040211|||http://purl.uniprot.org/annotation/VAR_040212|||http://purl.uniprot.org/annotation/VAR_040213|||http://purl.uniprot.org/annotation/VAR_040214|||http://purl.uniprot.org/annotation/VAR_040215|||http://purl.uniprot.org/annotation/VAR_040216|||http://purl.uniprot.org/annotation/VAR_040217|||http://purl.uniprot.org/annotation/VAR_040218|||http://purl.uniprot.org/annotation/VAR_040219|||http://purl.uniprot.org/annotation/VAR_040220|||http://purl.uniprot.org/annotation/VAR_040221|||http://purl.uniprot.org/annotation/VAR_040222|||http://purl.uniprot.org/annotation/VAR_040223|||http://purl.uniprot.org/annotation/VAR_040224|||http://purl.uniprot.org/annotation/VAR_040225|||http://purl.uniprot.org/annotation/VAR_040226|||http://purl.uniprot.org/annotation/VAR_040227|||http://purl.uniprot.org/annotation/VAR_040228|||http://purl.uniprot.org/annotation/VAR_040229|||http://purl.uniprot.org/annotation/VAR_040230|||http://purl.uniprot.org/annotation/VAR_040231|||http://purl.uniprot.org/annotation/VAR_040232|||http://purl.uniprot.org/annotation/VAR_040233|||http://purl.uniprot.org/annotation/VAR_040234|||http://purl.uniprot.org/annotation/VAR_040235|||http://purl.uniprot.org/annotation/VAR_040236|||http://purl.uniprot.org/annotation/VAR_040237|||http://purl.uniprot.org/annotation/VAR_040238|||http://purl.uniprot.org/annotation/VAR_040239|||http://purl.uniprot.org/annotation/VAR_040240|||http://purl.uniprot.org/annotation/VAR_040241|||http://purl.uniprot.org/annotation/VAR_040242|||http://purl.uniprot.org/annotation/VAR_040243|||http://purl.uniprot.org/annotation/VAR_040244|||http://purl.uniprot.org/annotation/VAR_040245|||http://purl.uniprot.org/annotation/VAR_040246|||http://purl.uniprot.org/annotation/VAR_040247|||http://purl.uniprot.org/annotation/VAR_040248|||http://purl.uniprot.org/annotation/VAR_040249|||http://purl.uniprot.org/annotation/VAR_040250|||http://purl.uniprot.org/annotation/VAR_040251|||http://purl.uniprot.org/annotation/VAR_040252|||http://purl.uniprot.org/annotation/VAR_040253|||http://purl.uniprot.org/annotation/VAR_040254|||http://purl.uniprot.org/annotation/VAR_040255|||http://purl.uniprot.org/annotation/VAR_040256|||http://purl.uniprot.org/annotation/VAR_040257|||http://purl.uniprot.org/annotation/VAR_040258|||http://purl.uniprot.org/annotation/VAR_040259|||http://purl.uniprot.org/annotation/VAR_040260|||http://purl.uniprot.org/annotation/VAR_040261|||http://purl.uniprot.org/annotation/VAR_040262|||http://purl.uniprot.org/annotation/VAR_040263|||http://purl.uniprot.org/annotation/VAR_040264|||http://purl.uniprot.org/annotation/VAR_040265|||http://purl.uniprot.org/annotation/VAR_040266|||http://purl.uniprot.org/annotation/VAR_040267|||http://purl.uniprot.org/annotation/VAR_040268|||http://purl.uniprot.org/annotation/VAR_040269|||http://purl.uniprot.org/annotation/VAR_040270|||http://purl.uniprot.org/annotation/VAR_040271|||http://purl.uniprot.org/annotation/VAR_040272|||http://purl.uniprot.org/annotation/VAR_040273|||http://purl.uniprot.org/annotation/VAR_040274|||http://purl.uniprot.org/annotation/VAR_040275|||http://purl.uniprot.org/annotation/VAR_040276|||http://purl.uniprot.org/annotation/VAR_040277|||http://purl.uniprot.org/annotation/VAR_040278|||http://purl.uniprot.org/annotation/VAR_040279|||http://purl.uniprot.org/annotation/VAR_040280|||http://purl.uniprot.org/annotation/VAR_040281|||http://purl.uniprot.org/annotation/VAR_040282|||http://purl.uniprot.org/annotation/VAR_040283|||http://purl.uniprot.org/annotation/VAR_040284|||http://purl.uniprot.org/annotation/VAR_040285|||http://purl.uniprot.org/annotation/VAR_040286|||http://purl.uniprot.org/annotation/VAR_040287|||http://purl.uniprot.org/annotation/VAR_040288|||http://purl.uniprot.org/annotation/VAR_040289|||http://purl.uniprot.org/annotation/VAR_040290|||http://purl.uniprot.org/annotation/VAR_040291|||http://purl.uniprot.org/annotation/VAR_040292|||http://purl.uniprot.org/annotation/VAR_040293|||http://purl.uniprot.org/annotation/VAR_040294|||http://purl.uniprot.org/annotation/VAR_040295|||http://purl.uniprot.org/annotation/VAR_040296|||http://purl.uniprot.org/annotation/VAR_040297|||http://purl.uniprot.org/annotation/VAR_040298|||http://purl.uniprot.org/annotation/VAR_040299|||http://purl.uniprot.org/annotation/VAR_040300|||http://purl.uniprot.org/annotation/VAR_040301|||http://purl.uniprot.org/annotation/VAR_040302|||http://purl.uniprot.org/annotation/VAR_040303|||http://purl.uniprot.org/annotation/VAR_040304|||http://purl.uniprot.org/annotation/VAR_040305|||http://purl.uniprot.org/annotation/VAR_040306|||http://purl.uniprot.org/annotation/VAR_040307|||http://purl.uniprot.org/annotation/VAR_040308|||http://purl.uniprot.org/annotation/VAR_040309|||http://purl.uniprot.org/annotation/VAR_040310|||http://purl.uniprot.org/annotation/VAR_040311|||http://purl.uniprot.org/annotation/VAR_040312|||http://purl.uniprot.org/annotation/VAR_040313|||http://purl.uniprot.org/annotation/VAR_040314|||http://purl.uniprot.org/annotation/VAR_040315|||http://purl.uniprot.org/annotation/VAR_040316|||http://purl.uniprot.org/annotation/VAR_040317|||http://purl.uniprot.org/annotation/VAR_040318|||http://purl.uniprot.org/annotation/VAR_040319|||http://purl.uniprot.org/annotation/VAR_040320|||http://purl.uniprot.org/annotation/VAR_040321|||http://purl.uniprot.org/annotation/VAR_040322|||http://purl.uniprot.org/annotation/VAR_040323|||http://purl.uniprot.org/annotation/VAR_040324|||http://purl.uniprot.org/annotation/VAR_040325|||http://purl.uniprot.org/annotation/VAR_040326|||http://purl.uniprot.org/annotation/VAR_040327|||http://purl.uniprot.org/annotation/VAR_040328|||http://purl.uniprot.org/annotation/VAR_040329|||http://purl.uniprot.org/annotation/VAR_040330|||http://purl.uniprot.org/annotation/VAR_040331|||http://purl.uniprot.org/annotation/VAR_040332|||http://purl.uniprot.org/annotation/VAR_040333|||http://purl.uniprot.org/annotation/VAR_040334|||http://purl.uniprot.org/annotation/VAR_040335|||http://purl.uniprot.org/annotation/VAR_040336|||http://purl.uniprot.org/annotation/VAR_040337|||http://purl.uniprot.org/annotation/VAR_040338|||http://purl.uniprot.org/annotation/VAR_040339|||http://purl.uniprot.org/annotation/VAR_040340|||http://purl.uniprot.org/annotation/VAR_040341|||http://purl.uniprot.org/annotation/VAR_040342|||http://purl.uniprot.org/annotation/VAR_040343|||http://purl.uniprot.org/annotation/VAR_040344|||http://purl.uniprot.org/annotation/VAR_040345|||http://purl.uniprot.org/annotation/VAR_040346|||http://purl.uniprot.org/annotation/VAR_040347|||http://purl.uniprot.org/annotation/VAR_056081|||http://purl.uniprot.org/annotation/VAR_056082|||http://purl.uniprot.org/annotation/VAR_056083|||http://purl.uniprot.org/annotation/VAR_056084|||http://purl.uniprot.org/annotation/VAR_056085|||http://purl.uniprot.org/annotation/VAR_056086|||http://purl.uniprot.org/annotation/VAR_056087|||http://purl.uniprot.org/annotation/VAR_056088|||http://purl.uniprot.org/annotation/VAR_056089|||http://purl.uniprot.org/annotation/VAR_069432|||http://purl.uniprot.org/annotation/VAR_069433|||http://purl.uniprot.org/annotation/VAR_074293|||http://purl.uniprot.org/annotation/VAR_074294|||http://purl.uniprot.org/annotation/VSP_019138|||http://purl.uniprot.org/annotation/VSP_019139|||http://purl.uniprot.org/annotation/VSP_019140|||http://purl.uniprot.org/annotation/VSP_019141|||http://purl.uniprot.org/annotation/VSP_019142|||http://purl.uniprot.org/annotation/VSP_019143|||http://purl.uniprot.org/annotation/VSP_019144|||http://purl.uniprot.org/annotation/VSP_019145|||http://purl.uniprot.org/annotation/VSP_019146|||http://purl.uniprot.org/annotation/VSP_019147|||http://purl.uniprot.org/annotation/VSP_019148|||http://purl.uniprot.org/annotation/VSP_019149|||http://purl.uniprot.org/annotation/VSP_019150|||http://purl.uniprot.org/annotation/VSP_019151|||http://purl.uniprot.org/annotation/VSP_019152|||http://purl.uniprot.org/annotation/VSP_042903|||http://purl.uniprot.org/annotation/VSP_045929|||http://purl.uniprot.org/annotation/VSP_045930|||http://purl.uniprot.org/annotation/VSP_045931|||http://purl.uniprot.org/annotation/VSP_045932|||http://purl.uniprot.org/annotation/VSP_045933|||http://purl.uniprot.org/annotation/VSP_045934|||http://purl.uniprot.org/annotation/VSP_045935|||http://purl.uniprot.org/annotation/VSP_047142
http://togogenome.org/gene/9606:CIMAP1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXM7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein CIMAP1C|||STPGR 1|||STPGR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304785|||http://purl.uniprot.org/annotation/VAR_062204
http://togogenome.org/gene/9606:ZNF675                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD23                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 675                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304875|||http://purl.uniprot.org/annotation/VAR_057440|||http://purl.uniprot.org/annotation/VAR_060430|||http://purl.uniprot.org/annotation/VAR_060431
http://togogenome.org/gene/9606:CTSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E324|||http://purl.uniprot.org/uniprot/P10619|||http://purl.uniprot.org/uniprot/X6R5C5|||http://purl.uniprot.org/uniprot/X6R8A1                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carboxypeptidase|||In GSL.|||In GSL; loss of activity.|||In GSL; small amount of activity.|||In isoform 2.|||Inactivates the enzyme.|||Lysosomal protective protein|||Lysosomal protective protein 20 kDa chain|||Lysosomal protective protein 32 kDa chain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004274|||http://purl.uniprot.org/annotation/PRO_0000004275|||http://purl.uniprot.org/annotation/PRO_0000004276|||http://purl.uniprot.org/annotation/PRO_5002803780|||http://purl.uniprot.org/annotation/PRO_5004976082|||http://purl.uniprot.org/annotation/PRO_5040104872|||http://purl.uniprot.org/annotation/VAR_001385|||http://purl.uniprot.org/annotation/VAR_001386|||http://purl.uniprot.org/annotation/VAR_001387|||http://purl.uniprot.org/annotation/VAR_001388|||http://purl.uniprot.org/annotation/VAR_001389|||http://purl.uniprot.org/annotation/VAR_001390|||http://purl.uniprot.org/annotation/VAR_063018|||http://purl.uniprot.org/annotation/VAR_063019|||http://purl.uniprot.org/annotation/VAR_063020|||http://purl.uniprot.org/annotation/VAR_063021|||http://purl.uniprot.org/annotation/VAR_063022|||http://purl.uniprot.org/annotation/VAR_063023|||http://purl.uniprot.org/annotation/VSP_054832
http://togogenome.org/gene/9606:MGAT4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ53                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288593|||http://purl.uniprot.org/annotation/VAR_032446|||http://purl.uniprot.org/annotation/VAR_053913|||http://purl.uniprot.org/annotation/VSP_025716|||http://purl.uniprot.org/annotation/VSP_043231
http://togogenome.org/gene/9606:LOXL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JB6                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog 4|||Lysyl-oxidase like|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018535|||http://purl.uniprot.org/annotation/VAR_050012|||http://purl.uniprot.org/annotation/VAR_050013|||http://purl.uniprot.org/annotation/VAR_059431
http://togogenome.org/gene/9606:M1AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX03|||http://purl.uniprot.org/uniprot/Q8TC57                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SPGF48; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Meiosis 1 arrest protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349268|||http://purl.uniprot.org/annotation/VAR_046335|||http://purl.uniprot.org/annotation/VAR_046336|||http://purl.uniprot.org/annotation/VAR_085687|||http://purl.uniprot.org/annotation/VAR_085688|||http://purl.uniprot.org/annotation/VAR_085689|||http://purl.uniprot.org/annotation/VAR_085690|||http://purl.uniprot.org/annotation/VAR_085691|||http://purl.uniprot.org/annotation/VSP_035291|||http://purl.uniprot.org/annotation/VSP_035292|||http://purl.uniprot.org/annotation/VSP_035293|||http://purl.uniprot.org/annotation/VSP_035294|||http://purl.uniprot.org/annotation/VSP_055677
http://togogenome.org/gene/9606:SPARC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09486                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||Follistatin-like|||In OI17; decreased secretion of the protein; altered secretion of procollagen type I.|||In OI17; no effect on expression and secretion of the protein; altered secretion of procollagen type I.|||Kazal-like|||Loss of collagen binding.|||N-linked (GlcNAc...) asparagine|||SPARC|||Strongly reduced collagen binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020304|||http://purl.uniprot.org/annotation/VAR_050431|||http://purl.uniprot.org/annotation/VAR_059530|||http://purl.uniprot.org/annotation/VAR_075142|||http://purl.uniprot.org/annotation/VAR_075143
http://togogenome.org/gene/9606:TRIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15650                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ASCH|||Activating signal cointegrator 1|||C4-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||Mediates interaction with DDRGK1|||Mediates interaction with UFL1|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065631
http://togogenome.org/gene/9606:ANXA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12429                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A3|||N-acetylalanine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067477|||http://purl.uniprot.org/annotation/VAR_013914|||http://purl.uniprot.org/annotation/VAR_013915|||http://purl.uniprot.org/annotation/VAR_013916|||http://purl.uniprot.org/annotation/VAR_013917
http://togogenome.org/gene/9606:SFRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N474                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  FZ|||N-linked (GlcNAc...) asparagine|||NTR|||No effect on molecular weight.|||Reduced molecular weight.|||Secreted frizzled-related protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032538
http://togogenome.org/gene/9606:ALS2CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q60I27                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ALS2 C-terminal-like protein|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 6.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313849|||http://purl.uniprot.org/annotation/VAR_037791|||http://purl.uniprot.org/annotation/VAR_037792|||http://purl.uniprot.org/annotation/VAR_037793|||http://purl.uniprot.org/annotation/VAR_061554|||http://purl.uniprot.org/annotation/VSP_030168|||http://purl.uniprot.org/annotation/VSP_030169|||http://purl.uniprot.org/annotation/VSP_030170|||http://purl.uniprot.org/annotation/VSP_030171|||http://purl.uniprot.org/annotation/VSP_043859
http://togogenome.org/gene/9606:HTR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95264                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 3B|||Cytoplasmic|||Extracellular|||HA-stretch; determines single-channel conductance in 5-HT3 receptors|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reduced molecular weight and cell membrane expression.|||Reduced molecular weight. Very little expression in the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312289|||http://purl.uniprot.org/annotation/VAR_037472|||http://purl.uniprot.org/annotation/VAR_037473|||http://purl.uniprot.org/annotation/VAR_037474|||http://purl.uniprot.org/annotation/VAR_037475|||http://purl.uniprot.org/annotation/VSP_029796
http://togogenome.org/gene/9606:DRD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21918                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||D(1B) dopamine receptor|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs subcellular location.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069405|||http://purl.uniprot.org/annotation/VAR_003458|||http://purl.uniprot.org/annotation/VAR_003459|||http://purl.uniprot.org/annotation/VAR_003460|||http://purl.uniprot.org/annotation/VAR_003461|||http://purl.uniprot.org/annotation/VAR_011837|||http://purl.uniprot.org/annotation/VAR_024254|||http://purl.uniprot.org/annotation/VAR_029210|||http://purl.uniprot.org/annotation/VAR_029211|||http://purl.uniprot.org/annotation/VAR_029212|||http://purl.uniprot.org/annotation/VAR_029213|||http://purl.uniprot.org/annotation/VAR_029215|||http://purl.uniprot.org/annotation/VAR_061217
http://togogenome.org/gene/9606:WWC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AWC2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein WWC2|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309490|||http://purl.uniprot.org/annotation/VAR_036965|||http://purl.uniprot.org/annotation/VAR_036966|||http://purl.uniprot.org/annotation/VAR_036967|||http://purl.uniprot.org/annotation/VAR_036968|||http://purl.uniprot.org/annotation/VAR_062108|||http://purl.uniprot.org/annotation/VSP_029213|||http://purl.uniprot.org/annotation/VSP_029214|||http://purl.uniprot.org/annotation/VSP_029215|||http://purl.uniprot.org/annotation/VSP_029216|||http://purl.uniprot.org/annotation/VSP_029217|||http://purl.uniprot.org/annotation/VSP_029218|||http://purl.uniprot.org/annotation/VSP_029219
http://togogenome.org/gene/9606:GALNT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY85|||http://purl.uniprot.org/uniprot/Q8IUC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 13|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059130|||http://purl.uniprot.org/annotation/VAR_049242|||http://purl.uniprot.org/annotation/VSP_011218|||http://purl.uniprot.org/annotation/VSP_011219|||http://purl.uniprot.org/annotation/VSP_054411
http://togogenome.org/gene/9606:BCL2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92843                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BH1|||BH2|||BH4|||Bcl-2-like protein 2|||In isoform 3.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143066|||http://purl.uniprot.org/annotation/VAR_048418|||http://purl.uniprot.org/annotation/VSP_042064
http://togogenome.org/gene/9606:RABIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47224|||http://purl.uniprot.org/uniprot/Q53EV1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Guanine nucleotide exchange factor MSS4|||MSS4|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174174
http://togogenome.org/gene/9606:AKR7A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDN8|||http://purl.uniprot.org/uniprot/O95154                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aflatoxin B1 aldehyde reductase member 3|||Lowers pKa of active site Tyr|||NADP-dependent oxidoreductase|||Phosphoserine|||Phosphothreonine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070378|||http://purl.uniprot.org/annotation/VAR_017416|||http://purl.uniprot.org/annotation/VAR_017417|||http://purl.uniprot.org/annotation/VAR_017418
http://togogenome.org/gene/9606:ASAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43150                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2|||Disordered|||In isoform 2.|||Loss of Arf-GAP activity.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074198|||http://purl.uniprot.org/annotation/VAR_020307|||http://purl.uniprot.org/annotation/VSP_009722
http://togogenome.org/gene/9606:EFCAB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXU6|||http://purl.uniprot.org/uniprot/Q6NXP0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand calcium-binding domain-containing protein 12|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238660|||http://purl.uniprot.org/annotation/VAR_033697|||http://purl.uniprot.org/annotation/VAR_048667|||http://purl.uniprot.org/annotation/VAR_048668|||http://purl.uniprot.org/annotation/VAR_061089|||http://purl.uniprot.org/annotation/VAR_061090
http://togogenome.org/gene/9606:RIMBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6Z0|||http://purl.uniprot.org/uniprot/O15034                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RIMS-binding protein 2|||SH3|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221383|||http://purl.uniprot.org/annotation/VAR_057714|||http://purl.uniprot.org/annotation/VAR_057715|||http://purl.uniprot.org/annotation/VSP_009212|||http://purl.uniprot.org/annotation/VSP_009213|||http://purl.uniprot.org/annotation/VSP_009214|||http://purl.uniprot.org/annotation/VSP_009215|||http://purl.uniprot.org/annotation/VSP_009216
http://togogenome.org/gene/9606:KLLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2CW77                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding                                                                                  ^@                                                                                  Killin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347059
http://togogenome.org/gene/9606:SLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2G2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cleavage; by caspase-3|||Disordered|||Found in a patient with global developmental delay; unknown pathological significance.|||In a lung adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||STE20-like serine/threonine-protein kinase|||UVR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233239|||http://purl.uniprot.org/annotation/VAR_041080|||http://purl.uniprot.org/annotation/VAR_041081|||http://purl.uniprot.org/annotation/VAR_041082|||http://purl.uniprot.org/annotation/VAR_041083|||http://purl.uniprot.org/annotation/VAR_041084|||http://purl.uniprot.org/annotation/VAR_041085|||http://purl.uniprot.org/annotation/VAR_041086|||http://purl.uniprot.org/annotation/VAR_051666|||http://purl.uniprot.org/annotation/VAR_084656|||http://purl.uniprot.org/annotation/VSP_018100
http://togogenome.org/gene/9606:PRKX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51817                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Constitutive kinase activity; when associated with Q-93.|||Constitutive kinase activity; when associated with R-202.|||Disordered|||Increases the affinity for PRKAR2A and PRKAR2B.|||Loss of function.|||N-acetylmethionine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||cAMP-dependent protein kinase catalytic subunit PRKX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086582|||http://purl.uniprot.org/annotation/VAR_061744
http://togogenome.org/gene/9606:YBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDP4|||http://purl.uniprot.org/uniprot/Q9Y2T7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CSD|||Disordered|||Phosphothreonine|||Polar residues|||Required for cytoplasmic retention|||Required for mRNA-binding|||Y-box-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100225|||http://purl.uniprot.org/annotation/VAR_027916|||http://purl.uniprot.org/annotation/VAR_027917
http://togogenome.org/gene/9606:CSN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05814|||http://purl.uniprot.org/uniprot/W5RWE1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-casein|||Phosphoserine; in form 1-P, form 2-P, form 3-P, form 4-P and form 5-P|||Phosphoserine; in form 3-P, form 4-P and form 5-P|||Phosphoserine; in form 4-P and form 5-P|||Phosphothreonine; in form 5-P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004475|||http://purl.uniprot.org/annotation/PRO_5014315709
http://togogenome.org/gene/9606:UBD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8S6|||http://purl.uniprot.org/uniprot/O15205                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation by thioester intermediate formation with UBA6|||Decreases interaction with MAD2L1, no effect on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and moderately attenuates UBD-induced tumor formation in vivo; when associated with D-11. Complete loss of interaction with MAD2L1, no effect on the interaction with TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates UBD-induced tumor formation in vivo; when associated with D-11; D-75; D-77 and Q-79.|||Decreases interaction with MAD2L1, no effect on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and moderately attenuates UBD-induced tumor formation in vivo; when associated with D-75 and D-77. Complete loss of interaction with MAD2L1, no effect on the interaction with TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates UBD-induced tumor formation in vivo; when associated with D-11; Q-13; D-75 and D-77.|||Decreases interaction with MAD2L1, no effect on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and moderately attenuates UBD-induced tumor formation in vivo; when associated with D-75 and Q-79. Complete loss of interaction with MAD2L1, no effect on the interaction with TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates UBD-induced tumor formation in vivo; when associated with D-11; Q-13; D-75 and Q-79.|||Decreases interaction with MAD2L1, no effect on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and moderately attenuates UBD-induced tumor formation in vivo; when associated with D-77 and Q-79. Complete loss of interaction with MAD2L1, no effect on the interaction with TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates UBD-induced tumor formation in vivo; when associated with D-11; Q-13; D-77 and Q-79.|||Decreases interaction with MAD2L1, no effect on the interaction with HDAC6, UBA6, NUB1 and SQSTM1 and moderately attenuates UBD-induced tumor formation in vivo; when associated with Q-13. Complete loss of interaction with MAD2L1, no effect on the interaction with TP53/p53, HDAC6, UBA6, NUB1 and SQSTM1 and significantly attenuates UBD-induced tumor formation in vivo; when associated with Q-13; D-75; D-77 and Q-79.|||Impaired thioester formation-mediated activation by UBA6. Loss of interaction with UBA6 and SQSTM1. No effect on its interaction with MAD2L1, HDAC6 and NUB1.|||Ubiquitin D|||Ubiquitin-like|||Ubiquitin-like 1|||Ubiquitin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114893|||http://purl.uniprot.org/annotation/VAR_024273|||http://purl.uniprot.org/annotation/VAR_024274|||http://purl.uniprot.org/annotation/VAR_024275|||http://purl.uniprot.org/annotation/VAR_024276|||http://purl.uniprot.org/annotation/VAR_025401|||http://purl.uniprot.org/annotation/VAR_025402|||http://purl.uniprot.org/annotation/VAR_052693
http://togogenome.org/gene/9606:FBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22087                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Decreased acetylation; restores ability to methylate histone H2A; when associated with R-102 and 205-R-R-206.|||Decreased acetylation; restores ability to methylate histone H2A; when associated with R-102 and R-121.|||Decreased acetylation; restores ability to methylate histone H2A; when associated with R-121 and 205-R-R-206.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-102 and 205-Q-Q-206.|||Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-102 and Q-121.|||Mimics acetylation; impaired ability to methylate histone H2A; when associated with Q-121 and 205-Q-Q-206.|||N6-acetyllysine|||Phosphoserine|||rRNA 2'-O-methyltransferase fibrillarin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148507
http://togogenome.org/gene/9606:CDKN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2J7|||http://purl.uniprot.org/uniprot/Q16667                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase inhibitor 3|||Disordered|||In HCC; patient BX-01.|||In HCC; patient BX-05.|||In HCC; patient BX-10.|||In HCC; patient NT1.|||In HCC; patient NT4.|||In HCC; patient T9.|||In isoform 2.|||Interaction with CDK2|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094949|||http://purl.uniprot.org/annotation/VAR_013842|||http://purl.uniprot.org/annotation/VAR_013843|||http://purl.uniprot.org/annotation/VAR_013844|||http://purl.uniprot.org/annotation/VAR_013845|||http://purl.uniprot.org/annotation/VAR_013846|||http://purl.uniprot.org/annotation/VAR_013847|||http://purl.uniprot.org/annotation/VAR_013848|||http://purl.uniprot.org/annotation/VAR_013849|||http://purl.uniprot.org/annotation/VAR_013850|||http://purl.uniprot.org/annotation/VAR_051769|||http://purl.uniprot.org/annotation/VSP_036613
http://togogenome.org/gene/9606:MRPL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1L8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein uL14m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261134
http://togogenome.org/gene/9606:TMEM182                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZP80                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with ITGB1|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 182                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290226|||http://purl.uniprot.org/annotation/VAR_032773|||http://purl.uniprot.org/annotation/VSP_026134|||http://purl.uniprot.org/annotation/VSP_026135
http://togogenome.org/gene/9606:ZMYND15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H091                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||MYND-type|||Pro residues|||Zinc finger MYND domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218317|||http://purl.uniprot.org/annotation/VAR_052992|||http://purl.uniprot.org/annotation/VSP_042144|||http://purl.uniprot.org/annotation/VSP_047208
http://togogenome.org/gene/9606:SDF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRK5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  45 kDa calcium-binding protein|||Does not affect calcium-binding.|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inhibits calcium-binding.|||N-linked (GlcNAc...) asparagine|||Necessary for intracellular retention in Golgi apparatus lumen|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004156|||http://purl.uniprot.org/annotation/VAR_035461|||http://purl.uniprot.org/annotation/VAR_048659|||http://purl.uniprot.org/annotation/VSP_037484|||http://purl.uniprot.org/annotation/VSP_037485|||http://purl.uniprot.org/annotation/VSP_037486|||http://purl.uniprot.org/annotation/VSP_037487|||http://purl.uniprot.org/annotation/VSP_037488|||http://purl.uniprot.org/annotation/VSP_037489|||http://purl.uniprot.org/annotation/VSP_040559
http://togogenome.org/gene/9606:RARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KPZ0|||http://purl.uniprot.org/uniprot/H0UI22|||http://purl.uniprot.org/uniprot/Q5T160                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||DALR anticodon binding|||Found in a patient with complex IV deficiency and non-lethal infantile mitochondrial disease; unknown pathological significance.|||Found in a patient with late onset progressive myoclonus epilepsy; unknown pathological significance.|||Found in a patient with progressive myoclonus epilepsy and dementia; unknown pathological significance.|||Mitochondrion|||N6-acetyllysine|||Probable arginine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250731|||http://purl.uniprot.org/annotation/VAR_037800|||http://purl.uniprot.org/annotation/VAR_037801|||http://purl.uniprot.org/annotation/VAR_037802|||http://purl.uniprot.org/annotation/VAR_076278|||http://purl.uniprot.org/annotation/VAR_076279|||http://purl.uniprot.org/annotation/VAR_085046|||http://purl.uniprot.org/annotation/VAR_085047|||http://purl.uniprot.org/annotation/VAR_085048
http://togogenome.org/gene/9606:NPIPB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXF8|||http://purl.uniprot.org/uniprot/E9PJ23|||http://purl.uniprot.org/uniprot/E9PS57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nuclear pore complex-interacting protein family member B6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423921|||http://purl.uniprot.org/annotation/PRO_5002780446|||http://purl.uniprot.org/annotation/PRO_5003244200
http://togogenome.org/gene/9606:MUL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969V5                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ligase activity.|||Abolishes ligase activity. No effect on mitochondrial localization.|||Cytoplasmic|||Failure to reduce TP53 levels and abolishes ligase activity; when associated with S-302.|||Failure to reduce TP53 levels and abolishes ligase activity; when associated with S-305.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Mitochondrial intermembrane|||Mitochondrial ubiquitin ligase activator of NFKB 1|||Protein is targeted to the ER; when associated with A-260.|||Protein is targeted to the ER; when associated with A-261.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277660
http://togogenome.org/gene/9606:ZNF177                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13360                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 177                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047441|||http://purl.uniprot.org/annotation/VAR_031692|||http://purl.uniprot.org/annotation/VAR_031693|||http://purl.uniprot.org/annotation/VAR_057401|||http://purl.uniprot.org/annotation/VSP_044461|||http://purl.uniprot.org/annotation/VSP_045841|||http://purl.uniprot.org/annotation/VSP_045842
http://togogenome.org/gene/9606:C17orf67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P5P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C17orf67                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287179
http://togogenome.org/gene/9606:ST6GALNAC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5G9|||http://purl.uniprot.org/uniprot/Q969X2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314795|||http://purl.uniprot.org/annotation/VSP_030359|||http://purl.uniprot.org/annotation/VSP_055722
http://togogenome.org/gene/9606:COL14A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05707                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  4-hydroxyproline|||4-hydroxyproline; partial|||5-hydroxylysine; alternate|||5-hydroxylysine; partial|||Cell attachment site|||Collagen alpha-1(XIV) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC4)|||O-linked (Gal...) hydroxylysine; alternate|||O-linked (Gal...) hydroxylysine; partial|||Pro residues|||Triple-helical region 1 (COL2)|||Triple-helical region 2 (COL1)|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005785|||http://purl.uniprot.org/annotation/VAR_048772|||http://purl.uniprot.org/annotation/VAR_048773|||http://purl.uniprot.org/annotation/VAR_048774|||http://purl.uniprot.org/annotation/VAR_048775|||http://purl.uniprot.org/annotation/VAR_061113|||http://purl.uniprot.org/annotation/VSP_051653|||http://purl.uniprot.org/annotation/VSP_051654
http://togogenome.org/gene/9606:AQP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4U2|||http://purl.uniprot.org/uniprot/O14520|||http://purl.uniprot.org/uniprot/Q5T5M0|||http://purl.uniprot.org/uniprot/Q6P5T0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects water and glycerol transport.|||Aquaporin-7|||Cytoplasmic|||Decreased interaction with PLIN1.|||Decreased permeability to glycerol. Mildly decreased water permeability.|||Discontinuously helical|||Extracellular|||Helical|||Important for permeability to glycerol|||In isoform 2.|||NPA 1|||NPA 2|||Phosphoserine|||Strongly decreased permeability to glycerol. Mildly decreased water permeability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063958|||http://purl.uniprot.org/annotation/VAR_061343|||http://purl.uniprot.org/annotation/VAR_061344|||http://purl.uniprot.org/annotation/VAR_067253|||http://purl.uniprot.org/annotation/VAR_067254|||http://purl.uniprot.org/annotation/VAR_067255|||http://purl.uniprot.org/annotation/VSP_056249|||http://purl.uniprot.org/annotation/VSP_056250
http://togogenome.org/gene/9606:JMJD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S16                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||JmjC|||JmjC domain-containing protein 8|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344531|||http://purl.uniprot.org/annotation/VSP_034849
http://togogenome.org/gene/9606:LENEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5L5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Lens epithelial cell protein LEP503                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084403
http://togogenome.org/gene/9606:LIMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Associated with lower plasma levels of low-density lipoprotein cholesterol; reduces protein stability.|||Basic and acidic residues|||Disordered|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform Alpha and isoform 5.|||LIM domain and actin-binding protein 1|||LIM zinc-binding|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Required for interaction with MYO5B|||Required for interaction with NPC1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075730|||http://purl.uniprot.org/annotation/VAR_080864|||http://purl.uniprot.org/annotation/VSP_003116|||http://purl.uniprot.org/annotation/VSP_003117|||http://purl.uniprot.org/annotation/VSP_040136
http://togogenome.org/gene/9606:FPGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05932                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Expression is reduced by 1.86-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; Km of glutamic acid is increased 3.5-fold and apparent Vmax of it is reduced 3.4-fold; reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.32-fold increase in the EC(50) for folic acid; IC(50) of methotrexate is 1.84-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected; all results are for isoform 2 variant in comparison to the wild-type of it.|||Expression reduced by 2.11-fold; Vmax with methotrexate as substrate is significantly reduced resulting in significantly decreased intrinsic clearance of methotrexate; apparent Vmax for glutamic acid is reduced 5-fold; reaction velocity at 100 nmol/L of pemetrexed is significantly reduced and folic acid dose-response curve is shifted to the right which corresponds to 4.28-fold increase in the EC(50) for folic acid; IC(50) of methotrexate is 1.64-fold higher and accumulation of a lower ratio of long-chain methotrexate polyglutamates to short-chain polyglutamates is detected; all results are for isoform 2 variant in comparison to the wild-type of it.|||Folylpolyglutamate synthase, mitochondrial|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010097|||http://purl.uniprot.org/annotation/VAR_043929|||http://purl.uniprot.org/annotation/VAR_043930|||http://purl.uniprot.org/annotation/VAR_043931|||http://purl.uniprot.org/annotation/VAR_059305|||http://purl.uniprot.org/annotation/VAR_066016|||http://purl.uniprot.org/annotation/VAR_066017|||http://purl.uniprot.org/annotation/VAR_066018|||http://purl.uniprot.org/annotation/VSP_018733|||http://purl.uniprot.org/annotation/VSP_041959|||http://purl.uniprot.org/annotation/VSP_041960
http://togogenome.org/gene/9606:PDE12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6T1Q0|||http://purl.uniprot.org/uniprot/Q6L8Q7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2',5'-phosphodiesterase 12|||Disordered|||Endonuclease/exonuclease/phosphatase|||In isoform 2.|||Mitochondrion|||Phosphoserine|||Polar residues|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324312|||http://purl.uniprot.org/annotation/VAR_039698|||http://purl.uniprot.org/annotation/VSP_032202|||http://purl.uniprot.org/annotation/VSP_032203
http://togogenome.org/gene/9606:TMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5M5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane channel-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259602|||http://purl.uniprot.org/annotation/VAR_066557|||http://purl.uniprot.org/annotation/VAR_066558|||http://purl.uniprot.org/annotation/VAR_066559|||http://purl.uniprot.org/annotation/VAR_066560|||http://purl.uniprot.org/annotation/VSP_052201|||http://purl.uniprot.org/annotation/VSP_052202
http://togogenome.org/gene/9606:SH2B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7K6|||http://purl.uniprot.org/uniprot/F5GYM4|||http://purl.uniprot.org/uniprot/Q59H48|||http://purl.uniprot.org/uniprot/Q9UQQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Associated with susceptibility to CELIAC13 and T1D.|||Basic and acidic residues|||Disordered|||Found in a patient with isolated erythrocytosis; unknown pathological significance.|||PH|||Phosphoserine|||Polar residues|||SH2|||SH2B adapter protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084454|||http://purl.uniprot.org/annotation/VAR_024168|||http://purl.uniprot.org/annotation/VAR_046210|||http://purl.uniprot.org/annotation/VAR_080828|||http://purl.uniprot.org/annotation/VAR_080829
http://togogenome.org/gene/9606:PAGE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JUK9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||P antigen family member 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247360|||http://purl.uniprot.org/annotation/VAR_027097|||http://purl.uniprot.org/annotation/VAR_027098
http://togogenome.org/gene/9606:LPAR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5KU18|||http://purl.uniprot.org/uniprot/Q9H1C0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lysophosphatidic acid receptor 5|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069600
http://togogenome.org/gene/9606:PRKAG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGI9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5'-AMP-activated protein kinase subunit gamma-3|||AMPK pseudosubstrate|||Associated with increased glycogen content and metabolism in skeletal muscle; results in increased basal and AMP-activated AMPK activity.|||CBS 1|||CBS 2|||CBS 3|||CBS 4|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204384|||http://purl.uniprot.org/annotation/VAR_023484|||http://purl.uniprot.org/annotation/VAR_048251|||http://purl.uniprot.org/annotation/VAR_048252|||http://purl.uniprot.org/annotation/VAR_069470|||http://purl.uniprot.org/annotation/VAR_069471|||http://purl.uniprot.org/annotation/VAR_069472|||http://purl.uniprot.org/annotation/VAR_069473|||http://purl.uniprot.org/annotation/VAR_069474|||http://purl.uniprot.org/annotation/VAR_069475|||http://purl.uniprot.org/annotation/VAR_069476|||http://purl.uniprot.org/annotation/VAR_069477|||http://purl.uniprot.org/annotation/VAR_069478|||http://purl.uniprot.org/annotation/VAR_069479|||http://purl.uniprot.org/annotation/VAR_069480|||http://purl.uniprot.org/annotation/VAR_069481|||http://purl.uniprot.org/annotation/VAR_069482|||http://purl.uniprot.org/annotation/VAR_069483|||http://purl.uniprot.org/annotation/VAR_069484|||http://purl.uniprot.org/annotation/VAR_069485|||http://purl.uniprot.org/annotation/VAR_069486|||http://purl.uniprot.org/annotation/VSP_015587
http://togogenome.org/gene/9606:PPP3R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63098                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Site|||Strand                                                                                  ^@                                                                                  Calcineurin A binding|||Calcineurin subunit B type 1|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interaction with PxVP motif in substrates of the catalytic subunit|||N-myristoyl glycine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073484
http://togogenome.org/gene/9606:MICOS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XKP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||MICOS complex subunit MIC13|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289985
http://togogenome.org/gene/9606:GTF2H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13888                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||General transcription factor IIH subunit 2|||No effect on the transcriptional activity of the reconstituted TFIIH complex.|||Phosphotyrosine|||Reconstituted TFIIH complex lacks p62 and has no transcriptional activity.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119248|||http://purl.uniprot.org/annotation/VAR_011664|||http://purl.uniprot.org/annotation/VAR_011665
http://togogenome.org/gene/9606:RPS15A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62244                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  N6-succinyllysine|||Removed|||Small ribosomal subunit protein uS8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126602
http://togogenome.org/gene/9606:BEX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9J7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||His cluster|||Protein BEX5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229788
http://togogenome.org/gene/9606:SPAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07617                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Sperm-associated antigen 1|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106324|||http://purl.uniprot.org/annotation/VAR_054324|||http://purl.uniprot.org/annotation/VAR_054325|||http://purl.uniprot.org/annotation/VAR_054326|||http://purl.uniprot.org/annotation/VSP_054290|||http://purl.uniprot.org/annotation/VSP_054291
http://togogenome.org/gene/9606:ALMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34|||34 X 47 AA approximate tandem repeat|||4|||5|||6|||7|||8|||9|||ALMS motif|||Acidic residues|||Basic and acidic residues|||Centrosome-associated protein ALMS1|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225592|||http://purl.uniprot.org/annotation/VAR_025433|||http://purl.uniprot.org/annotation/VAR_025434|||http://purl.uniprot.org/annotation/VAR_025435|||http://purl.uniprot.org/annotation/VAR_025436|||http://purl.uniprot.org/annotation/VAR_056734|||http://purl.uniprot.org/annotation/VAR_059575|||http://purl.uniprot.org/annotation/VAR_059576|||http://purl.uniprot.org/annotation/VAR_059577|||http://purl.uniprot.org/annotation/VAR_059578|||http://purl.uniprot.org/annotation/VAR_080194|||http://purl.uniprot.org/annotation/VSP_017347|||http://purl.uniprot.org/annotation/VSP_017348|||http://purl.uniprot.org/annotation/VSP_017349
http://togogenome.org/gene/9606:GYG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46976                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycogenin-1|||Important for catalytic activity|||In GSD15; loss of autoglucosylation.|||In PGBM2.|||In isoform GN-1.|||In isoform GN-1S.|||Interaction with GYS1|||Loss of glucosylation.|||N-acetylthreonine|||O-linked (Glc...) tyrosine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215176|||http://purl.uniprot.org/annotation/VAR_063768|||http://purl.uniprot.org/annotation/VAR_072706|||http://purl.uniprot.org/annotation/VAR_072707|||http://purl.uniprot.org/annotation/VSP_001768|||http://purl.uniprot.org/annotation/VSP_001769
http://togogenome.org/gene/9606:DALRD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5D0E6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DALR anticodon-binding domain-containing protein 3|||In DEE86; severe reduction of tRNA(Arg) N(3)-methylcytidine modification.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315848|||http://purl.uniprot.org/annotation/VAR_038349|||http://purl.uniprot.org/annotation/VAR_084359|||http://purl.uniprot.org/annotation/VSP_030741|||http://purl.uniprot.org/annotation/VSP_030743|||http://purl.uniprot.org/annotation/VSP_030744|||http://purl.uniprot.org/annotation/VSP_030746
http://togogenome.org/gene/9606:CPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK13|||http://purl.uniprot.org/uniprot/A0A1B0GTB8|||http://purl.uniprot.org/uniprot/P23786                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Sequence Variant|||Topological Domain|||Transit Peptide                                                                                  ^@                                                                                  Associated with susceptibility to IIAE4; 3-fold decrease of affinity for L-carnitine; lower thermal stability compared to wild-type.|||Associated with susceptibility to IIAE4; no effect on activity; does not affect affinity for L-carnitine; lower thermal stability compared to wild-type.|||Carnitine O-palmitoyltransferase 2, mitochondrial|||Choline/carnitine acyltransferase|||Confirmed at protein level.|||In CPT2D.|||In CPT2D; hepatocardiomuscular form.|||In CPT2D; muscular form; frequent mutation.|||In CPT2D; muscular type.|||In CPT2DI and CPT2D; early-onset hepatocardiomuscular form.|||In CPT2DI; hepatocardiomuscular form.|||In a patient with IIAE4.|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Note=Mitochondrial inner membrane|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004424|||http://purl.uniprot.org/annotation/VAR_001391|||http://purl.uniprot.org/annotation/VAR_001392|||http://purl.uniprot.org/annotation/VAR_001393|||http://purl.uniprot.org/annotation/VAR_001394|||http://purl.uniprot.org/annotation/VAR_001395|||http://purl.uniprot.org/annotation/VAR_001396|||http://purl.uniprot.org/annotation/VAR_001397|||http://purl.uniprot.org/annotation/VAR_001398|||http://purl.uniprot.org/annotation/VAR_001399|||http://purl.uniprot.org/annotation/VAR_001400|||http://purl.uniprot.org/annotation/VAR_007966|||http://purl.uniprot.org/annotation/VAR_007967|||http://purl.uniprot.org/annotation/VAR_007968|||http://purl.uniprot.org/annotation/VAR_007969|||http://purl.uniprot.org/annotation/VAR_007970|||http://purl.uniprot.org/annotation/VAR_007971|||http://purl.uniprot.org/annotation/VAR_011741|||http://purl.uniprot.org/annotation/VAR_020540|||http://purl.uniprot.org/annotation/VAR_020541|||http://purl.uniprot.org/annotation/VAR_020542|||http://purl.uniprot.org/annotation/VAR_020543|||http://purl.uniprot.org/annotation/VAR_020544|||http://purl.uniprot.org/annotation/VAR_020545|||http://purl.uniprot.org/annotation/VAR_037976|||http://purl.uniprot.org/annotation/VAR_066567|||http://purl.uniprot.org/annotation/VAR_066568
http://togogenome.org/gene/9606:SLC22A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H015                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abrogates TEA transport activity.|||Cytoplasmic|||Decreased carnitine transport; decreased acetylcholine transport.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220497|||http://purl.uniprot.org/annotation/VAR_019528|||http://purl.uniprot.org/annotation/VAR_019529|||http://purl.uniprot.org/annotation/VAR_019530
http://togogenome.org/gene/9606:TSPAN33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UF1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282922
http://togogenome.org/gene/9606:ZIC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T25                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein ZIC 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047255|||http://purl.uniprot.org/annotation/VAR_079268|||http://purl.uniprot.org/annotation/VAR_079269
http://togogenome.org/gene/9606:EFHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JST6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DM10 1|||DM10 2|||DM10 3|||EF-hand|||EF-hand domain-containing family member C2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251703|||http://purl.uniprot.org/annotation/VAR_027698|||http://purl.uniprot.org/annotation/VAR_027699|||http://purl.uniprot.org/annotation/VAR_027700|||http://purl.uniprot.org/annotation/VAR_027701|||http://purl.uniprot.org/annotation/VAR_061086|||http://purl.uniprot.org/annotation/VSP_020766
http://togogenome.org/gene/9606:WNT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93097                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In DIAR9.|||In DIAR9; diminished staining for the intestinal stem cell marker OLFM4; enteroid cultures generated from patient intestinal epithelium cannot be expanded and do not survive multiple passages; shows a 10-fold increase in LEF1 mRNA and a 100-fold reduction in TLR4 expression compared to controls indicating alterations in canonical Wnt signaling and microbial pattern-recognition signaling.|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-2b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041413|||http://purl.uniprot.org/annotation/VAR_081727|||http://purl.uniprot.org/annotation/VAR_081728|||http://purl.uniprot.org/annotation/VSP_006794
http://togogenome.org/gene/9606:DNAJC5G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7S2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 5G|||In isoform 2.|||J|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071057|||http://purl.uniprot.org/annotation/VAR_033882|||http://purl.uniprot.org/annotation/VAR_033883|||http://purl.uniprot.org/annotation/VSP_056967|||http://purl.uniprot.org/annotation/VSP_056968
http://togogenome.org/gene/9606:INPPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15357                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity but not phosphorylation upon FCGR2A clustering.|||Abolishes interaction with SH3YL1.|||Abolishes interaction with p130Cas/BCAR1 and its ability to induce increased adhesion. Abolishes phosphorylation upon FCGR2A clustering.|||Associated with susceptibility to T2D.|||Basic and acidic residues|||Disordered|||In OPSMD.|||In isoform 2.|||Inducer a strong reduction of phosphorylation upon re-plating on collagen I.|||NPXY motif|||Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Pro residues|||Reduces PDGF-stimulated tyrosine phosphorylation and association with SHC1.|||SAM|||SH2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302870|||http://purl.uniprot.org/annotation/VAR_034980|||http://purl.uniprot.org/annotation/VAR_034981|||http://purl.uniprot.org/annotation/VAR_034982|||http://purl.uniprot.org/annotation/VAR_034983|||http://purl.uniprot.org/annotation/VAR_034984|||http://purl.uniprot.org/annotation/VAR_069586|||http://purl.uniprot.org/annotation/VAR_069587|||http://purl.uniprot.org/annotation/VAR_069588|||http://purl.uniprot.org/annotation/VAR_069589|||http://purl.uniprot.org/annotation/VSP_027985
http://togogenome.org/gene/9606:EIF4G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RU06|||http://purl.uniprot.org/uniprot/B2RU10|||http://purl.uniprot.org/uniprot/B4DSI9|||http://purl.uniprot.org/uniprot/O95065|||http://purl.uniprot.org/uniprot/Q04637|||http://purl.uniprot.org/uniprot/Q96I65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to EIF4A; when associated with A-767 and A-770.|||Abolishes binding to EIF4A; when associated with A-767 and A-775.|||Abolishes binding to EIF4A; when associated with A-770 and A-775.|||Abolishes binding to EIF4A; when associated with A-841 and A-842.|||Abolishes binding to EIF4A; when associated with A-850 and K-851.|||Abolishes binding to EIF4A; when associated with A-895 and A-92.|||Abolishes binding to EIF4A; when associated with A-895 and A-95.|||Abolishes binding to EIF4A; when associated with A-92 and A-95.|||Abolishes binding to EIF4A; when associated with A-973.|||Abolishes binding to EIF4A; when associated with A-976.|||Abolishes binding to EIF4E.|||Acidic residues|||Basic and acidic residues|||Cleavage; by enterovirus/rhinovirus protease 2A|||Cleavage; by foot-and-mouth disease virus leader protease|||Disordered|||EIF4A-binding|||EIF4E-binding|||Eukaryotic translation initiation factor 4 gamma 1|||Found in a patient with Parkinson disease; unknown pathological significance.|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||Found in patients with Parkinson disease; unknown pathological significance.|||In PARK18.|||In a colorectal cancer sample; somatic mutation.|||In isoform 7 and isoform 8.|||In isoform 9.|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E and isoform 7.|||Loss of PABPC1 binding.|||Loss of PABPC1 binding; when associated with 174-AAAAA-178.|||Loss of PABPC1 binding; when associated with 184-AAAA-187.|||MI|||MIF4G|||N-acetylmethionine|||N6-acetyllysine|||Necessary but not sufficient for MKNK1-binding|||Omega-N-methylarginine|||PABPC1-binding|||Phosphoserine|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced cleavage by protease 2A from human rhinovirus 2.|||Removed|||Slightly reduced binding to EIF4A; when associated with A-984.|||Slightly reduced binding to EIF4A; when associated with A-989.|||W2|||eIF3/EIF4A-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007786|||http://purl.uniprot.org/annotation/VAR_036117|||http://purl.uniprot.org/annotation/VAR_055704|||http://purl.uniprot.org/annotation/VAR_055705|||http://purl.uniprot.org/annotation/VAR_061147|||http://purl.uniprot.org/annotation/VAR_061148|||http://purl.uniprot.org/annotation/VAR_063040|||http://purl.uniprot.org/annotation/VAR_066571|||http://purl.uniprot.org/annotation/VAR_066572|||http://purl.uniprot.org/annotation/VAR_066573|||http://purl.uniprot.org/annotation/VAR_066574|||http://purl.uniprot.org/annotation/VAR_066575|||http://purl.uniprot.org/annotation/VAR_066576|||http://purl.uniprot.org/annotation/VAR_066577|||http://purl.uniprot.org/annotation/VAR_066578|||http://purl.uniprot.org/annotation/VAR_066579|||http://purl.uniprot.org/annotation/VAR_066580|||http://purl.uniprot.org/annotation/VAR_079031|||http://purl.uniprot.org/annotation/VSP_018720|||http://purl.uniprot.org/annotation/VSP_018721|||http://purl.uniprot.org/annotation/VSP_018722|||http://purl.uniprot.org/annotation/VSP_018723|||http://purl.uniprot.org/annotation/VSP_047396|||http://purl.uniprot.org/annotation/VSP_047397
http://togogenome.org/gene/9606:PEX11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8C6|||http://purl.uniprot.org/uniprot/B4DMF6|||http://purl.uniprot.org/uniprot/O75192                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||No effect on peroxisomal location.|||Peroxisomal membrane protein 11A|||Required for homodimerization, interaction with PEX11G, and peroxisomal localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105964|||http://purl.uniprot.org/annotation/VSP_054753
http://togogenome.org/gene/9606:STARD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2P6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHA|||In isoform 2.|||In isoform 3.|||Kinesin motor|||Phosphoserine|||Polar residues|||Reduced ATPase activity.|||Reduced ability to bind microtubules.|||START|||StAR-related lipid transfer protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220678|||http://purl.uniprot.org/annotation/VAR_037257|||http://purl.uniprot.org/annotation/VAR_037258|||http://purl.uniprot.org/annotation/VAR_037259|||http://purl.uniprot.org/annotation/VAR_037260|||http://purl.uniprot.org/annotation/VAR_037261|||http://purl.uniprot.org/annotation/VAR_037262|||http://purl.uniprot.org/annotation/VAR_037263|||http://purl.uniprot.org/annotation/VAR_037264|||http://purl.uniprot.org/annotation/VAR_037266|||http://purl.uniprot.org/annotation/VAR_059811|||http://purl.uniprot.org/annotation/VSP_029573|||http://purl.uniprot.org/annotation/VSP_029574|||http://purl.uniprot.org/annotation/VSP_029575|||http://purl.uniprot.org/annotation/VSP_029576|||http://purl.uniprot.org/annotation/VSP_029577
http://togogenome.org/gene/9606:RHOT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXI1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Causes constitutive activation inducing an aggregation of the mitochondrial network.|||Cytoplasmic|||EF-hand 1|||EF-hand 2|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Induces an aggregation of the mitochondrial network.|||Miro 1|||Miro 2|||Mitochondrial Rho GTPase 2|||Mitochondrial intermembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239318|||http://purl.uniprot.org/annotation/VAR_026637|||http://purl.uniprot.org/annotation/VAR_026638|||http://purl.uniprot.org/annotation/VSP_019162|||http://purl.uniprot.org/annotation/VSP_019163|||http://purl.uniprot.org/annotation/VSP_019164
http://togogenome.org/gene/9606:BPY2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14599                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Testis-specific basic protein Y 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184664
http://togogenome.org/gene/9606:OFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL37|||http://purl.uniprot.org/uniprot/O75665                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centriole and centriolar satellite protein OFD1|||Disordered|||In JBTS10; unknown pathological significance.|||In OFD1.|||In isoform 2.|||In isoform 3.|||Increased protein stability.|||LisH|||Loss of phosphorylation by PKA. Loss of cAMP-dependent interaction with TBC1D31. Loss of ubiquitin-mediated proteasomal degradation. Loss of function in cilium assembly. Dominant negative effect.|||Mediates homooligomerization|||Mediates the interaction with SDCCAG8|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058029|||http://purl.uniprot.org/annotation/VAR_013753|||http://purl.uniprot.org/annotation/VAR_013754|||http://purl.uniprot.org/annotation/VAR_015574|||http://purl.uniprot.org/annotation/VAR_030789|||http://purl.uniprot.org/annotation/VAR_058758|||http://purl.uniprot.org/annotation/VAR_069100|||http://purl.uniprot.org/annotation/VAR_075701|||http://purl.uniprot.org/annotation/VSP_004177|||http://purl.uniprot.org/annotation/VSP_004178|||http://purl.uniprot.org/annotation/VSP_023334
http://togogenome.org/gene/9606:USP17L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Inactive ubiquitin carboxyl-terminal hydrolase 17-like protein 4|||Polar residues|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331646
http://togogenome.org/gene/9606:ZNF570                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EP39|||http://purl.uniprot.org/uniprot/Q96NI8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 570                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047661|||http://purl.uniprot.org/annotation/PRO_5003904160|||http://purl.uniprot.org/annotation/VSP_055967
http://togogenome.org/gene/9606:CAPN15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75808                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-15|||Disordered|||In OGIN; unknown pathological significance.|||In isoform 2.|||Phosphoserine|||Pro residues|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||RanBP2-type 4|||RanBP2-type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278770|||http://purl.uniprot.org/annotation/VAR_085921|||http://purl.uniprot.org/annotation/VAR_085922|||http://purl.uniprot.org/annotation/VAR_085923|||http://purl.uniprot.org/annotation/VAR_085924|||http://purl.uniprot.org/annotation/VAR_085925|||http://purl.uniprot.org/annotation/VSP_023361|||http://purl.uniprot.org/annotation/VSP_023362
http://togogenome.org/gene/9606:PKHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08F94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Ciliary targeting sequence (CST)|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Fibrocystin|||Found in a patient affected by polycystic liver disease; unknown pathological significance.|||G8 1|||G8 2|||Helical|||IPT/TIG 10|||IPT/TIG 11|||IPT/TIG 12; atypical|||IPT/TIG 1; atypical|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||IPT/TIG 5|||IPT/TIG 6; atypical|||IPT/TIG 7|||IPT/TIG 8; atypical|||IPT/TIG 9|||In PKD4.|||In PKD4; common mutation; also found in a patient affected by polycystic liver disease.|||In PKD4; may affect splicing.|||In PKD4; unknown pathological significance.|||In a colorectal cancer sample and PKD4; somatic mutation; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In a patient with polycystic kidney disease.|||In isoform 2.|||Loss of protein convertase cleavage into a 85 kDa PTM fragment.|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal (NLS)|||PA14|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||PbH1 6|||PbH1 7|||PbH1 8|||PbH1 9|||Probable disease-associated variant found in a patient affected by polycystic liver disease.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022062|||http://purl.uniprot.org/annotation/VAR_014039|||http://purl.uniprot.org/annotation/VAR_014040|||http://purl.uniprot.org/annotation/VAR_014041|||http://purl.uniprot.org/annotation/VAR_014042|||http://purl.uniprot.org/annotation/VAR_014043|||http://purl.uniprot.org/annotation/VAR_014044|||http://purl.uniprot.org/annotation/VAR_014045|||http://purl.uniprot.org/annotation/VAR_014046|||http://purl.uniprot.org/annotation/VAR_014047|||http://purl.uniprot.org/annotation/VAR_014048|||http://purl.uniprot.org/annotation/VAR_014049|||http://purl.uniprot.org/annotation/VAR_014050|||http://purl.uniprot.org/annotation/VAR_014051|||http://purl.uniprot.org/annotation/VAR_014052|||http://purl.uniprot.org/annotation/VAR_014053|||http://purl.uniprot.org/annotation/VAR_014054|||http://purl.uniprot.org/annotation/VAR_014055|||http://purl.uniprot.org/annotation/VAR_014056|||http://purl.uniprot.org/annotation/VAR_014057|||http://purl.uniprot.org/annotation/VAR_014058|||http://purl.uniprot.org/annotation/VAR_014059|||http://purl.uniprot.org/annotation/VAR_014060|||http://purl.uniprot.org/annotation/VAR_014061|||http://purl.uniprot.org/annotation/VAR_014062|||http://purl.uniprot.org/annotation/VAR_014063|||http://purl.uniprot.org/annotation/VAR_018520|||http://purl.uniprot.org/annotation/VAR_018521|||http://purl.uniprot.org/annotation/VAR_018522|||http://purl.uniprot.org/annotation/VAR_018523|||http://purl.uniprot.org/annotation/VAR_018524|||http://purl.uniprot.org/annotation/VAR_018525|||http://purl.uniprot.org/annotation/VAR_018526|||http://purl.uniprot.org/annotation/VAR_018527|||http://purl.uniprot.org/annotation/VAR_018528|||http://purl.uniprot.org/annotation/VAR_018529|||http://purl.uniprot.org/annotation/VAR_018530|||http://purl.uniprot.org/annotation/VAR_018531|||http://purl.uniprot.org/annotation/VAR_018532|||http://purl.uniprot.org/annotation/VAR_018533|||http://purl.uniprot.org/annotation/VAR_018534|||http://purl.uniprot.org/annotation/VAR_018535|||http://purl.uniprot.org/annotation/VAR_018536|||http://purl.uniprot.org/annotation/VAR_018537|||http://purl.uniprot.org/annotation/VAR_018538|||http://purl.uniprot.org/annotation/VAR_018539|||http://purl.uniprot.org/annotation/VAR_018540|||http://purl.uniprot.org/annotation/VAR_018541|||http://purl.uniprot.org/annotation/VAR_018542|||http://purl.uniprot.org/annotation/VAR_018543|||http://purl.uniprot.org/annotation/VAR_018544|||http://purl.uniprot.org/annotation/VAR_018545|||http://purl.uniprot.org/annotation/VAR_018546|||http://purl.uniprot.org/annotation/VAR_018547|||http://purl.uniprot.org/annotation/VAR_018548|||http://purl.uniprot.org/annotation/VAR_018549|||http://purl.uniprot.org/annotation/VAR_018550|||http://purl.uniprot.org/annotation/VAR_018551|||http://purl.uniprot.org/annotation/VAR_018552|||http://purl.uniprot.org/annotation/VAR_018553|||http://purl.uniprot.org/annotation/VAR_018554|||http://purl.uniprot.org/annotation/VAR_018555|||http://purl.uniprot.org/annotation/VAR_018556|||http://purl.uniprot.org/annotation/VAR_018557|||http://purl.uniprot.org/annotation/VAR_018558|||http://purl.uniprot.org/annotation/VAR_018559|||http://purl.uniprot.org/annotation/VAR_018560|||http://purl.uniprot.org/annotation/VAR_018561|||http://purl.uniprot.org/annotation/VAR_018562|||http://purl.uniprot.org/annotation/VAR_018563|||http://purl.uniprot.org/annotation/VAR_018564|||http://purl.uniprot.org/annotation/VAR_018565|||http://purl.uniprot.org/annotation/VAR_018566|||http://purl.uniprot.org/annotation/VAR_018567|||http://purl.uniprot.org/annotation/VAR_018568|||http://purl.uniprot.org/annotation/VAR_018569|||http://purl.uniprot.org/annotation/VAR_018570|||http://purl.uniprot.org/annotation/VAR_018571|||http://purl.uniprot.org/annotation/VAR_018572|||http://purl.uniprot.org/annotation/VAR_018573|||http://purl.uniprot.org/annotation/VAR_018574|||http://purl.uniprot.org/annotation/VAR_018575|||http://purl.uniprot.org/annotation/VAR_018576|||http://purl.uniprot.org/annotation/VAR_018577|||http://purl.uniprot.org/annotation/VAR_018578|||http://purl.uniprot.org/annotation/VAR_018579|||http://purl.uniprot.org/annotation/VAR_018580|||http://purl.uniprot.org/annotation/VAR_018581|||http://purl.uniprot.org/annotation/VAR_018582|||http://purl.uniprot.org/annotation/VAR_018583|||http://purl.uniprot.org/annotation/VAR_018584|||http://purl.uniprot.org/annotation/VAR_018585|||http://purl.uniprot.org/annotation/VAR_018586|||http://purl.uniprot.org/annotation/VAR_018587|||http://purl.uniprot.org/annotation/VAR_018588|||http://purl.uniprot.org/annotation/VAR_018589|||http://purl.uniprot.org/annotation/VAR_018590|||http://purl.uniprot.org/annotation/VAR_018591|||http://purl.uniprot.org/annotation/VAR_018592|||http://purl.uniprot.org/annotation/VAR_018593|||http://purl.uniprot.org/annotation/VAR_018594|||http://purl.uniprot.org/annotation/VAR_018595|||http://purl.uniprot.org/annotation/VAR_018596|||http://purl.uniprot.org/annotation/VAR_018597|||http://purl.uniprot.org/annotation/VAR_018598|||http://purl.uniprot.org/annotation/VAR_018599|||http://purl.uniprot.org/annotation/VAR_027439|||http://purl.uniprot.org/annotation/VAR_027440|||http://purl.uniprot.org/annotation/VAR_027441|||http://purl.uniprot.org/annotation/VAR_027442|||http://purl.uniprot.org/annotation/VAR_027443|||http://purl.uniprot.org/annotation/VAR_036228|||http://purl.uniprot.org/annotation/VAR_036229|||http://purl.uniprot.org/annotation/VAR_036230|||http://purl.uniprot.org/annotation/VAR_036231|||http://purl.uniprot.org/annotation/VAR_051282|||http://purl.uniprot.org/annotation/VAR_066416|||http://purl.uniprot.org/annotation/VAR_066417|||http://purl.uniprot.org/annotation/VAR_066418|||http://purl.uniprot.org/annotation/VAR_066419|||http://purl.uniprot.org/annotation/VAR_066420|||http://purl.uniprot.org/annotation/VAR_066421|||http://purl.uniprot.org/annotation/VAR_066422|||http://purl.uniprot.org/annotation/VAR_066423|||http://purl.uniprot.org/annotation/VAR_066424|||http://purl.uniprot.org/annotation/VAR_066425|||http://purl.uniprot.org/annotation/VAR_066426|||http://purl.uniprot.org/annotation/VAR_066427|||http://purl.uniprot.org/annotation/VAR_066428|||http://purl.uniprot.org/annotation/VAR_066429|||http://purl.uniprot.org/annotation/VAR_066430|||http://purl.uniprot.org/annotation/VAR_066431|||http://purl.uniprot.org/annotation/VAR_066432|||http://purl.uniprot.org/annotation/VAR_066433|||http://purl.uniprot.org/annotation/VAR_066434|||http://purl.uniprot.org/annotation/VAR_066435|||http://purl.uniprot.org/annotation/VAR_066436|||http://purl.uniprot.org/annotation/VAR_066437|||http://purl.uniprot.org/annotation/VAR_066438|||http://purl.uniprot.org/annotation/VAR_066439|||http://purl.uniprot.org/annotation/VAR_066440|||http://purl.uniprot.org/annotation/VAR_066441|||http://purl.uniprot.org/annotation/VAR_066442|||http://purl.uniprot.org/annotation/VAR_066443|||http://purl.uniprot.org/annotation/VAR_066444|||http://purl.uniprot.org/annotation/VAR_066445|||http://purl.uniprot.org/annotation/VAR_066446|||http://purl.uniprot.org/annotation/VAR_075540|||http://purl.uniprot.org/annotation/VAR_080923|||http://purl.uniprot.org/annotation/VAR_080924|||http://purl.uniprot.org/annotation/VAR_080925|||http://purl.uniprot.org/annotation/VAR_080926|||http://purl.uniprot.org/annotation/VAR_080927|||http://purl.uniprot.org/annotation/VAR_080928|||http://purl.uniprot.org/annotation/VAR_080929|||http://purl.uniprot.org/annotation/VAR_080930|||http://purl.uniprot.org/annotation/VAR_080931|||http://purl.uniprot.org/annotation/VAR_080932|||http://purl.uniprot.org/annotation/VAR_080933|||http://purl.uniprot.org/annotation/VAR_080934|||http://purl.uniprot.org/annotation/VSP_003947|||http://purl.uniprot.org/annotation/VSP_003948
http://togogenome.org/gene/9606:CSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09919|||http://purl.uniprot.org/uniprot/Q6FH65|||http://purl.uniprot.org/uniprot/Q8N4W3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Granulocyte colony-stimulating factor|||In isoform 3.|||In isoform Short.|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015570|||http://purl.uniprot.org/annotation/PRO_5010141904|||http://purl.uniprot.org/annotation/PRO_5014312261|||http://purl.uniprot.org/annotation/VAR_013073|||http://purl.uniprot.org/annotation/VAR_013074|||http://purl.uniprot.org/annotation/VSP_002673|||http://purl.uniprot.org/annotation/VSP_045246
http://togogenome.org/gene/9606:S100A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FQ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1; degenerate|||EF-hand 2|||Protein S100-A16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144023
http://togogenome.org/gene/9606:NANS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  AFP-like|||In SEMDG.|||N6-acetyllysine|||Phosphoserine|||Removed|||Sialic acid synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097750|||http://purl.uniprot.org/annotation/VAR_013308|||http://purl.uniprot.org/annotation/VAR_076571|||http://purl.uniprot.org/annotation/VAR_076572|||http://purl.uniprot.org/annotation/VAR_076573|||http://purl.uniprot.org/annotation/VAR_076574|||http://purl.uniprot.org/annotation/VAR_076575|||http://purl.uniprot.org/annotation/VAR_076576|||http://purl.uniprot.org/annotation/VAR_076577
http://togogenome.org/gene/9606:MTERF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFP7|||http://purl.uniprot.org/uniprot/Q7Z6M4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Dimerization with NSUN4|||Disordered|||MTERF 1|||MTERF 2|||MTERF 3|||MTERF 4|||MTERF 5|||Mitochondrion|||Transcription termination factor 4, mitochondrial|||mTERF domain-containing protein 2 processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255461|||http://purl.uniprot.org/annotation/PRO_0000424341|||http://purl.uniprot.org/annotation/VAR_028865|||http://purl.uniprot.org/annotation/VAR_028866|||http://purl.uniprot.org/annotation/VAR_028867|||http://purl.uniprot.org/annotation/VAR_028868|||http://purl.uniprot.org/annotation/VAR_028869
http://togogenome.org/gene/9606:STC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76061|||http://purl.uniprot.org/uniprot/Q6FHC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Stanniocalcin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033303|||http://purl.uniprot.org/annotation/PRO_5014310441
http://togogenome.org/gene/9606:LRRC8E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSJ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alters channel anion selectivity.|||Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||Volume-regulated anion channel subunit LRRC8E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076250|||http://purl.uniprot.org/annotation/VAR_056930|||http://purl.uniprot.org/annotation/VAR_059695|||http://purl.uniprot.org/annotation/VAR_059696|||http://purl.uniprot.org/annotation/VAR_060437
http://togogenome.org/gene/9606:CHST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43916                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Motif|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 1|||Cell attachment site|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085182
http://togogenome.org/gene/9606:MYO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM54                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Decreased localization to autophagosomes.|||Disordered|||IQ|||In DFNA22.|||In DFNB37.|||In DFNHCM.|||In isoform 1.|||In isoform 2 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||Interaction with OPTN|||Interaction with TAX1BP1 and CALCOCO2/NDP52|||Interaction with TOM1|||Myosin N-terminal SH3-like|||Myosin motor|||Phosphoserine|||Phosphothreonine|||Required for binding calmodulin|||Responsible for slow ATPase activity|||SAH|||Three-helix bundle|||Unconventional myosin-VI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123464|||http://purl.uniprot.org/annotation/VAR_012110|||http://purl.uniprot.org/annotation/VAR_016209|||http://purl.uniprot.org/annotation/VAR_029988|||http://purl.uniprot.org/annotation/VSP_007985|||http://purl.uniprot.org/annotation/VSP_022332|||http://purl.uniprot.org/annotation/VSP_022333|||http://purl.uniprot.org/annotation/VSP_042208
http://togogenome.org/gene/9606:GNPTAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3T906                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes proteolytic cleavage by MBTPS1.|||Cleavage; by MBTPS1|||DMAP1-binding|||EF-hand|||Found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||Found in a patient with mucolipidosis type II or III; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||Found in a patient with mucolipidosis type II or III; unknown pathological significance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates.|||Helical|||In MLII and MLIIIA; no effect on protein abundance; decreased localization to the Golgi; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII.|||In MLII; abnormal protein cleavage into alpha and beta subunits; no effect on protein abundance; significantly decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase.|||In MLII; decreased protein abundance; no effect on localization to the Golgi; does not suppress protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; decreased protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; loss of Golgi localization; defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates.|||In MLII; no effect on protein abundance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; no loss of Golgi localization; no defects in protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; unknown pathological significance.|||In MLII; unknown pathological significance; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; unknown pathological significance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLII; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA.|||In MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; also found in patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; decreased localization to the Golgi; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates.|||In MLIIIA; no effect on protein abundance; loss of localization to the Golgi; defects in protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on protein abundance; loss of localization to the Golgi; loss of protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on protein abundance; no effect on localization to the Golgi.|||In MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates.|||In MLIIIA; no effect on protein cleavage into alpha and beta subunits; no effect on protein abundance; no effect on subcellular location in cis-Golgi apparatus; slightly affects UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; no effect on protein abundance; no effect on localization to the Golgi; no effect on protein cleavage into alpha and beta subunits; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity toward some substrates.|||In MLIIIA; patients with intermediate phenotype between MLII and MLIIIA; unknown pathological significance; no effect on protein abundance; decreased localization to the Golgi; loss of UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In MLIIIA; reduces protein cleavage into alpha and beta subunits; reduces protein abundance; no effect on subcellular location in Golgi apparatus; mildly affects UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase.|||In MLIIIA; significantly reduces protein cleavage into alpha and beta subunits; reduces protein abundance; significantly decreased localization to the Golgi; significantly reduces UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase.|||In MLIIIA; unknown pathological significance.|||In MLIIIA; unknown pathological significance; decreased localization to the Golgi; decreased protein cleavage into alpha and beta subunits; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; reduces protein abundance.|||In MLIIIA; unknown pathological significance; no effect on protein abundance; decreased protein cleavage into alpha and beta subunits; decreased retention in the Golgi; mistargeted to lysosomes and plasma membrane; decreased UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity.|||In isoform 2.|||LNR 1|||LNR 2|||May be a risk factor for stuttering.|||N-acetylglucosamine-1-phosphotransferase subunit alpha|||N-acetylglucosamine-1-phosphotransferase subunit beta|||N-linked (GlcNAc...) asparagine|||Partially cleaved by MBTPS1.|||Rare variant; found in individuals suffering from stuttering; unknown pathological significance. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225008|||http://purl.uniprot.org/annotation/PRO_0000225009|||http://purl.uniprot.org/annotation/VAR_025416|||http://purl.uniprot.org/annotation/VAR_025417|||http://purl.uniprot.org/annotation/VAR_027509|||http://purl.uniprot.org/annotation/VAR_027510|||http://purl.uniprot.org/annotation/VAR_027511|||http://purl.uniprot.org/annotation/VAR_053545|||http://purl.uniprot.org/annotation/VAR_062807|||http://purl.uniprot.org/annotation/VAR_062808|||http://purl.uniprot.org/annotation/VAR_062809|||http://purl.uniprot.org/annotation/VAR_062810|||http://purl.uniprot.org/annotation/VAR_062811|||http://purl.uniprot.org/annotation/VAR_062812|||http://purl.uniprot.org/annotation/VAR_062813|||http://purl.uniprot.org/annotation/VAR_062814|||http://purl.uniprot.org/annotation/VAR_062815|||http://purl.uniprot.org/annotation/VAR_070831|||http://purl.uniprot.org/annotation/VAR_070832|||http://purl.uniprot.org/annotation/VAR_070833|||http://purl.uniprot.org/annotation/VAR_070834|||http://purl.uniprot.org/annotation/VAR_073124|||http://purl.uniprot.org/annotation/VAR_073125|||http://purl.uniprot.org/annotation/VAR_073126|||http://purl.uniprot.org/annotation/VAR_073127|||http://purl.uniprot.org/annotation/VAR_073128|||http://purl.uniprot.org/annotation/VAR_073129|||http://purl.uniprot.org/annotation/VAR_073130|||http://purl.uniprot.org/annotation/VAR_073131|||http://purl.uniprot.org/annotation/VAR_073132|||http://purl.uniprot.org/annotation/VAR_073133|||http://purl.uniprot.org/annotation/VAR_073134|||http://purl.uniprot.org/annotation/VAR_073135|||http://purl.uniprot.org/annotation/VAR_073136|||http://purl.uniprot.org/annotation/VAR_073137|||http://purl.uniprot.org/annotation/VAR_073138|||http://purl.uniprot.org/annotation/VAR_073219|||http://purl.uniprot.org/annotation/VAR_073220|||http://purl.uniprot.org/annotation/VAR_073221|||http://purl.uniprot.org/annotation/VAR_074206|||http://purl.uniprot.org/annotation/VAR_074207|||http://purl.uniprot.org/annotation/VAR_074208|||http://purl.uniprot.org/annotation/VAR_074209|||http://purl.uniprot.org/annotation/VAR_079713|||http://purl.uniprot.org/annotation/VAR_079714|||http://purl.uniprot.org/annotation/VAR_079715|||http://purl.uniprot.org/annotation/VAR_079716|||http://purl.uniprot.org/annotation/VSP_017338|||http://purl.uniprot.org/annotation/VSP_017339
http://togogenome.org/gene/9606:PEMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBM1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||INTRAMEM|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to S-adenosyl-L-methionine.|||Cytoplasmic|||Helical|||Impairs binding to S-adenosyl-L-methionine.|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||Phosphatidylethanolamine N-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193920|||http://purl.uniprot.org/annotation/VAR_016093|||http://purl.uniprot.org/annotation/VAR_032771|||http://purl.uniprot.org/annotation/VAR_055372|||http://purl.uniprot.org/annotation/VAR_055373|||http://purl.uniprot.org/annotation/VAR_060083|||http://purl.uniprot.org/annotation/VAR_082891|||http://purl.uniprot.org/annotation/VSP_037311|||http://purl.uniprot.org/annotation/VSP_046034
http://togogenome.org/gene/9606:XPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01831|||http://purl.uniprot.org/uniprot/X5DRB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA repair protein complementing XP-C cells|||DNA-binding; preference for heteroduplex DNA|||DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complex|||Diminishes repair activity and impairs DNA binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In XP-C; diminishes repair activity and impairs DNA binding.|||In XP-C; mild.|||In XP-C; severe; does not affect interaction with KAT2A and transcription coactivator activity in absence of DNA damage.|||In isoform 2.|||In isoform 3.|||Interaction with CETN2|||Interaction with ERCC2 and GTF2H1|||Interaction with RAD23B|||Minimal sensor domain involved in damage recognition|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rad4 beta-hairpin|||Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; greatly reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites.|||Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci.|||Reduces DNA repair activity; abolishes single-stranded DNA binding; reduces binding to homoduplex DNA; reduces localization at DNA damaged foci; decreases recruitment of TFIIH complex to lesion sites.|||Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-851.|||Reduces NER activity and abolishes interaction with CETN2; when associated with A-848 and A-855.|||Reduces NER activity and abolishes interaction with CETN2; when associated with A-851 and A-855.|||Reduces nuclear mobility and impairs repair activity.|||Removed|||Slightly diminishes repair activity and slightly impairs DNA binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218293|||http://purl.uniprot.org/annotation/VAR_005846|||http://purl.uniprot.org/annotation/VAR_005847|||http://purl.uniprot.org/annotation/VAR_005848|||http://purl.uniprot.org/annotation/VAR_018894|||http://purl.uniprot.org/annotation/VAR_018895|||http://purl.uniprot.org/annotation/VAR_018896|||http://purl.uniprot.org/annotation/VAR_018897|||http://purl.uniprot.org/annotation/VAR_018898|||http://purl.uniprot.org/annotation/VAR_018899|||http://purl.uniprot.org/annotation/VAR_018900|||http://purl.uniprot.org/annotation/VAR_018901|||http://purl.uniprot.org/annotation/VAR_018902|||http://purl.uniprot.org/annotation/VAR_018903|||http://purl.uniprot.org/annotation/VAR_018904|||http://purl.uniprot.org/annotation/VAR_057475|||http://purl.uniprot.org/annotation/VAR_057476|||http://purl.uniprot.org/annotation/VAR_059963|||http://purl.uniprot.org/annotation/VAR_064039|||http://purl.uniprot.org/annotation/VSP_046344|||http://purl.uniprot.org/annotation/VSP_055890|||http://purl.uniprot.org/annotation/VSP_055891
http://togogenome.org/gene/9606:MAN2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16706                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-mannosidase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206902|||http://purl.uniprot.org/annotation/VAR_074182
http://togogenome.org/gene/9606:SCLY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQU4|||http://purl.uniprot.org/uniprot/B4DDP9|||http://purl.uniprot.org/uniprot/Q59FK2|||http://purl.uniprot.org/uniprot/Q96I15                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminotransferase class V|||Disordered|||In isoform 2.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||S-selanylcysteine intermediate|||Selenocysteine lyase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317012|||http://purl.uniprot.org/annotation/VAR_038464|||http://purl.uniprot.org/annotation/VAR_038465|||http://purl.uniprot.org/annotation/VAR_038466|||http://purl.uniprot.org/annotation/VSP_030854
http://togogenome.org/gene/9606:ATG4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTY5|||http://purl.uniprot.org/uniprot/Q96DT6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Cysteine protease ATG4C|||N-acetylmethionine|||Nucleophile|||Peptidase C54 catalytic|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215849
http://togogenome.org/gene/9606:TMEM116                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCL8|||http://purl.uniprot.org/uniprot/Q9BWF8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 116                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251195|||http://purl.uniprot.org/annotation/VAR_027659|||http://purl.uniprot.org/annotation/VSP_046987|||http://purl.uniprot.org/annotation/VSP_046988
http://togogenome.org/gene/9606:ABCB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUT2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||Abolish binding to ATP.|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial potassium channel ATP-binding subunit|||Mitochondrion|||Renders the protein unstable.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000251|||http://purl.uniprot.org/annotation/VAR_013331|||http://purl.uniprot.org/annotation/VAR_035733|||http://purl.uniprot.org/annotation/VAR_035734|||http://purl.uniprot.org/annotation/VSP_000026|||http://purl.uniprot.org/annotation/VSP_055297|||http://purl.uniprot.org/annotation/VSP_056744|||http://purl.uniprot.org/annotation/VSP_056745
http://togogenome.org/gene/9606:CDK16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK97|||http://purl.uniprot.org/uniprot/Q00536|||http://purl.uniprot.org/uniprot/Q9BRL4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CCNY.|||Abolishes phosphorylation by BRSK2. Abolishes effect on insulin secretion.|||Constitutively activated, due to loss of an inhibitory phosphorylation site. Increases interaction with CCNY.|||Cyclin-dependent kinase 16|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of kinase activity.|||Loss of kinase activity. Abolishes effect on insulin secretion.|||Phosphoserine|||Phosphoserine; by BRSK2|||Phosphoserine; by CDK5|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly reduces interaction with CCNY.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086484|||http://purl.uniprot.org/annotation/VSP_046134|||http://purl.uniprot.org/annotation/VSP_046342
http://togogenome.org/gene/9606:C16orf92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LL3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Fertilization-influencing membrane protein|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321511|||http://purl.uniprot.org/annotation/VSP_031783
http://togogenome.org/gene/9606:FRZB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9ZGF6|||http://purl.uniprot.org/uniprot/Q92765                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||FZ|||In OS1; associated with disease susceptibility; has diminished ability to antagonize Wnt signaling, in vitro.|||N-linked (GlcNAc...) asparagine|||NTR|||Polar residues|||Secreted frizzled-related protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032546|||http://purl.uniprot.org/annotation/PRO_5014302712|||http://purl.uniprot.org/annotation/VAR_014862|||http://purl.uniprot.org/annotation/VAR_021411
http://togogenome.org/gene/9606:LRRN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUT4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat neuronal protein 4|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021029|||http://purl.uniprot.org/annotation/VAR_025548|||http://purl.uniprot.org/annotation/VAR_051143
http://togogenome.org/gene/9606:PRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92954                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11; approximate|||12|||13|||14|||15|||16; approximate|||17|||18; approximate|||19; approximate|||20|||21|||22|||23|||24; approximate|||25|||26; approximate|||27|||28|||29|||2; approximate|||3|||30|||31|||32|||33; approximate|||34|||35; approximate|||36; approximate|||37; approximate|||38; approximate|||39|||40|||41|||42; approximate|||43; approximate|||44|||45; approximate|||46; approximate|||47; approximate|||48; approximate|||49|||4; approximate|||5|||50|||51; approximate|||52|||53; approximate|||54; approximate|||55; approximate|||56; approximate|||57|||58|||59 X 8 AA repeats of K-X-P-X-P-T-T-X|||59; approximate|||6; approximate|||7|||8|||9|||Alternate|||Basic and acidic residues|||Basic residues|||Cleavage; by subtilisin-like proprotein convertase 4|||Disordered|||Hemopexin 1|||Hemopexin 2|||In isoform B, isoform D and isoform E.|||In isoform C and isoform D.|||In isoform E.|||In isoform F.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues|||Pro residues|||Proteoglycan 4|||Proteoglycan 4 C-terminal part|||SMB 1|||SMB 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043232|||http://purl.uniprot.org/annotation/PRO_0000043233|||http://purl.uniprot.org/annotation/VAR_024023|||http://purl.uniprot.org/annotation/VAR_051559|||http://purl.uniprot.org/annotation/VAR_051560|||http://purl.uniprot.org/annotation/VAR_051561|||http://purl.uniprot.org/annotation/VSP_016467|||http://purl.uniprot.org/annotation/VSP_016468|||http://purl.uniprot.org/annotation/VSP_016469|||http://purl.uniprot.org/annotation/VSP_016470
http://togogenome.org/gene/9606:HLA-A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1PKY1|||http://purl.uniprot.org/uniprot/B2R7U3|||http://purl.uniprot.org/uniprot/P04439                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Allele A*01:01, allele A*23:01, allele A*24:02, allele A*26:01, allele A*29:02, allele A*36:01, allele A*43:01 and allele A*80:01.|||Allele A*80:01.|||Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Disordered|||Extracellular|||HLA class I histocompatibility antigen, A alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||Impairs binding to TAP1-TAP2 transporter, resulting in impaired presentation of intracellular peptides.|||Impairs the maturation of a peptide-receptive HLA-A*02-B2M complex.|||Impairs the recruitment of HLA-A*02 in the peptide-loading complex.|||In allele A*01:01 and allele A*36:01.|||In allele A*01:01, allele A*02:01, allele A*02:05, allele A*11:01, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01.|||In allele A*01:01, allele A*02:01, allele A*02:05, allele A*23:01, allele 24:02, allele A*25:01, allele A*26:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*36:01, allele A*43:01, allele A*74:01 and allele A*80:01.|||In allele A*01:01, allele A*11:01 and allele A*36:01.|||In allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*32:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01 and allele A*74:01.|||In allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*34:01, allele A*36:01, allele A*43:01, allele A*66:01 and allele A*80:01.|||In allele A*01:01, allele A*11:01, allele A*25:01, allele A*26:01, allele A*43:01 and allele A*66:01.|||In allele A*01:01, allele A*23:01, allele A*24:02 and allele A*80:01.|||In allele A*01:01, allele A*26:01, allele A*29:02, allele A*36:01, allele A*43:01 and allele A*80:01.|||In allele A*02:01 and allele A*02:05.|||In allele A*02:01 and allele A*02:05; requires 2 nucleotide substitutions.|||In allele A*02:01 and allele A*69:01.|||In allele A*02:01, allele A*02:05 and allele A*69:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele 24:02 and allele A*34:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02 and allele A*69:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 allele A*69:01, allele A*74:01 and allele A*80:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 and allele A*69:01; does not alter the affinity of VL9 peptide for HLA-E or HLA-E expression at the plasma membrane; decreases KLRD1-KLRC1 and KLRD1-KLRC2 receptor engagement and signaling.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*68:01, allele A*69:01 and allele A*74:01; results in inefficient T cell recognition of epitopes derived from influenza A virus..|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*68:01 and allele A*69:01.|||In allele A*02:01, allele A*02:05, allele A*23:01, allele A*24:02, allele A*69:01.|||In allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01.|||In allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01 and allele A*80:01.|||In allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01, allele A*74:01.|||In allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*29:02, allele A*32:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01, allele A*69:01 and allele A*74:01.|||In allele A*02:01, allele A*02:05, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*69:01.|||In allele A*02:01, allele A*02:05, allele A*68:01 and allele A*69:01.|||In allele A*02:05, allele A*11:01, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01 and allele A*69:01.|||In allele A*02:05, allele A*23:01 and allele 24:02.|||In allele A*02:05, allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*68:01.|||In allele A*02:05.|||In allele A*11:01 and allele A*24:02.|||In allele A*23:01 and allele 24:02.|||In allele A*23:01 and allele A*24:02.|||In allele A*23:01, allele 24:02 and allele A*80:01.|||In allele A*23:01, allele 24:02, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*68:01 and allele A*74:01.|||In allele A*23:01, allele 24:02.|||In allele A*23:01, allele A*24:02 and allele A*30:01.|||In allele A*23:01, allele A*24:02, allele A*25:01 and allele A*32:01.|||In allele A*23:01, allele A*24:02, allele A*25:01 and allele A*32:01; Bw4 motif RIALR is involved in the recognition of NK cell inhibitory receptor KIR3DL1.|||In allele A*23:01, allele A*25:01, allele A*26:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*74:01.|||In allele A*23:01, allele A*29:02, allele A*30:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*74:01 and allele A*80:01.|||In allele A*23:01.|||In allele A*25:01 and allele A*32:01; requires 2 nucleotide substitutions.|||In allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01 and allele A*74:01.|||In allele A*25:01, allele A*26:01, allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*74:01 and allele A*80:01.|||In allele A*25:01, allele A*26:01, allele A*31:01, allele A*32:01, allele A*33:01, allele A*34:01, allele A*43:01, allele A*66:01, allele A*74:01.|||In allele A*25:01, allele A*26:01, allele A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and allele A*69:01.|||In allele A*25:01, allele A*26:01, allele A*34:01, allele A*43:01 and allele A*66:01.|||In allele A*29:02 and allele A*43:01.|||In allele A*29:02, allele A*31:01 and allele A*33:01; requires 2 nucleotide substitutions.|||In allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01 and allele A*74:01.|||In allele A*29:02, allele A*31:01, allele A*32:01, allele A*33:01 and allele A*74:01; impairs VL9 peptide processing and HLA-E expression at the plasma membrane.|||In allele A*30:01 and allele A*31:01.|||In allele A*30:01.|||In allele A*30:01; requires 2 nucleotide substitutions.|||In allele A*31:01 and allele A*33:01.|||In allele A*32:01 and allele A*74:01.|||In allele A*33:01.|||In allele A*34:01.|||In allele A*68:01; impairs binding to CD8A and reduces recognition by antigen-specific CD8-positive T cells.|||In allele A*74:01.|||In allele A*80:01.|||In allele A*80:01; does not alter the affinity of VL9 peptide for HLA-E or HLA-E expression at the plasma membrane; facilitates KLRD1-KLRC1 and KLRD1-KLRC2 receptor engagement and signaling.|||In allele A*80:01; requires 2 nucleotide substitutions.|||In alleles A*01:01 and allele A*36:01.|||In alleles A*25:01, allele A*26:01, allele A*33:01, allele A*34:01, allele A*66:01, allele A*68:01 and allele A*69:01; requires 2 nucleotide substitutions.|||In alleles A*29:02 and allele A*43:01.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Sulfotyrosine|||VL9 epitope ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018815|||http://purl.uniprot.org/annotation/PRO_5002780129|||http://purl.uniprot.org/annotation/PRO_5015087079|||http://purl.uniprot.org/annotation/VAR_082315|||http://purl.uniprot.org/annotation/VAR_082316|||http://purl.uniprot.org/annotation/VAR_082317|||http://purl.uniprot.org/annotation/VAR_082318|||http://purl.uniprot.org/annotation/VAR_082319|||http://purl.uniprot.org/annotation/VAR_082320|||http://purl.uniprot.org/annotation/VAR_082321|||http://purl.uniprot.org/annotation/VAR_082322|||http://purl.uniprot.org/annotation/VAR_082323|||http://purl.uniprot.org/annotation/VAR_082324|||http://purl.uniprot.org/annotation/VAR_082325|||http://purl.uniprot.org/annotation/VAR_082326|||http://purl.uniprot.org/annotation/VAR_082327|||http://purl.uniprot.org/annotation/VAR_082328|||http://purl.uniprot.org/annotation/VAR_082329|||http://purl.uniprot.org/annotation/VAR_082330|||http://purl.uniprot.org/annotation/VAR_082331|||http://purl.uniprot.org/annotation/VAR_082332|||http://purl.uniprot.org/annotation/VAR_082333|||http://purl.uniprot.org/annotation/VAR_082334|||http://purl.uniprot.org/annotation/VAR_082335|||http://purl.uniprot.org/annotation/VAR_082336|||http://purl.uniprot.org/annotation/VAR_082337|||http://purl.uniprot.org/annotation/VAR_082338|||http://purl.uniprot.org/annotation/VAR_082339|||http://purl.uniprot.org/annotation/VAR_082340|||http://purl.uniprot.org/annotation/VAR_082341|||http://purl.uniprot.org/annotation/VAR_082342|||http://purl.uniprot.org/annotation/VAR_082343|||http://purl.uniprot.org/annotation/VAR_082344|||http://purl.uniprot.org/annotation/VAR_082345|||http://purl.uniprot.org/annotation/VAR_082346|||http://purl.uniprot.org/annotation/VAR_082347|||http://purl.uniprot.org/annotation/VAR_082348|||http://purl.uniprot.org/annotation/VAR_082349|||http://purl.uniprot.org/annotation/VAR_082350|||http://purl.uniprot.org/annotation/VAR_082351|||http://purl.uniprot.org/annotation/VAR_082352|||http://purl.uniprot.org/annotation/VAR_082353|||http://purl.uniprot.org/annotation/VAR_082354|||http://purl.uniprot.org/annotation/VAR_082355|||http://purl.uniprot.org/annotation/VAR_082356|||http://purl.uniprot.org/annotation/VAR_082357|||http://purl.uniprot.org/annotation/VAR_082358|||http://purl.uniprot.org/annotation/VAR_082359|||http://purl.uniprot.org/annotation/VAR_082360|||http://purl.uniprot.org/annotation/VAR_082361|||http://purl.uniprot.org/annotation/VAR_082362|||http://purl.uniprot.org/annotation/VAR_082363|||http://purl.uniprot.org/annotation/VAR_082364|||http://purl.uniprot.org/annotation/VAR_082365|||http://purl.uniprot.org/annotation/VAR_082366|||http://purl.uniprot.org/annotation/VAR_082367|||http://purl.uniprot.org/annotation/VAR_082368|||http://purl.uniprot.org/annotation/VAR_082369|||http://purl.uniprot.org/annotation/VAR_082370|||http://purl.uniprot.org/annotation/VAR_082371|||http://purl.uniprot.org/annotation/VAR_082372|||http://purl.uniprot.org/annotation/VAR_082373|||http://purl.uniprot.org/annotation/VAR_082374|||http://purl.uniprot.org/annotation/VAR_082375|||http://purl.uniprot.org/annotation/VAR_082376|||http://purl.uniprot.org/annotation/VAR_082377|||http://purl.uniprot.org/annotation/VAR_082378|||http://purl.uniprot.org/annotation/VAR_082379|||http://purl.uniprot.org/annotation/VAR_082380|||http://purl.uniprot.org/annotation/VAR_082381|||http://purl.uniprot.org/annotation/VAR_082382|||http://purl.uniprot.org/annotation/VAR_082383|||http://purl.uniprot.org/annotation/VAR_082384|||http://purl.uniprot.org/annotation/VAR_082385|||http://purl.uniprot.org/annotation/VAR_082386|||http://purl.uniprot.org/annotation/VAR_082387|||http://purl.uniprot.org/annotation/VAR_082388|||http://purl.uniprot.org/annotation/VAR_082389|||http://purl.uniprot.org/annotation/VAR_082390|||http://purl.uniprot.org/annotation/VAR_082391|||http://purl.uniprot.org/annotation/VAR_082392|||http://purl.uniprot.org/annotation/VAR_082393|||http://purl.uniprot.org/annotation/VAR_082394|||http://purl.uniprot.org/annotation/VAR_082395|||http://purl.uniprot.org/annotation/VAR_082396|||http://purl.uniprot.org/annotation/VAR_082397|||http://purl.uniprot.org/annotation/VAR_082398|||http://purl.uniprot.org/annotation/VAR_082399|||http://purl.uniprot.org/annotation/VAR_082400|||http://purl.uniprot.org/annotation/VAR_082401|||http://purl.uniprot.org/annotation/VAR_082402|||http://purl.uniprot.org/annotation/VAR_082403|||http://purl.uniprot.org/annotation/VAR_082404|||http://purl.uniprot.org/annotation/VAR_082405|||http://purl.uniprot.org/annotation/VAR_082406|||http://purl.uniprot.org/annotation/VAR_082407|||http://purl.uniprot.org/annotation/VSP_060391|||http://purl.uniprot.org/annotation/VSP_060392
http://togogenome.org/gene/9606:MTOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQ52|||http://purl.uniprot.org/uniprot/P42345                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Barely detectable kinase activity.|||Catalytic loop|||Disordered|||FAT|||FATC|||Found in a patient with focal epilepsy; unknown pathological significance.|||Found in a patient with non-lesional nocturnal frontal epilepsy; unknown pathological significance.|||Found in a renal cell carcinoma sample; somatic mutation.|||G-loop|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 21|||HEAT 22|||HEAT 23|||HEAT 24|||HEAT 25|||HEAT 26|||HEAT 27|||HEAT 28|||HEAT 29|||HEAT 3|||HEAT 30|||HEAT 31|||HEAT 32|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In FCORD2; also found in a colorectal adenocarcinoma sample; somatic mutation; increased TOR signaling.|||In FCORD2; somatic mutation.|||In FCORD2; somatic mutation; increased TOR signaling.|||In FCORD2; somatic mutation; increased TOR signaling; increased kinase activity.|||In FCORD2; somatic mutation; unknown pathological significance.|||In SKS.|||In SKS; results in increased mTOR signaling.|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||Increased mTOR kinase activity.|||Interaction with MLST8|||Interaction with NBN|||Kinase-dead mutant, loss of interaction with TM4SF5 and loss of lysosome membrane localization; when associated with E-2357.|||Kinase-dead mutant, loss of interaction with TM4SF5 and loss of lysosome membrane localization; when associated with I-2364.|||Mimics phosphorylation; leading to stronger phosphorylation of RPS6KB1; when associated with E-2164. Increased activity of the mTORC1 complex.|||N-acetylmethionine|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Phosphoserine; by TBK1|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by RPS6KB1|||Polar residues|||Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2159.|||Reduces mTORC1-associated S-2481 autophosphorylation; when associated with A-2164. Reduced activity of the mTORC1 complex.|||Serine/threonine-protein kinase mTOR|||Stronger phosphorylation of RPS6KB1; when associated with D-2159.|||Sufficient for interaction with the FKBP1A/rapamycin complex|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088808|||http://purl.uniprot.org/annotation/VAR_041537|||http://purl.uniprot.org/annotation/VAR_041538|||http://purl.uniprot.org/annotation/VAR_041539|||http://purl.uniprot.org/annotation/VAR_041540|||http://purl.uniprot.org/annotation/VAR_041541|||http://purl.uniprot.org/annotation/VAR_041542|||http://purl.uniprot.org/annotation/VAR_041543|||http://purl.uniprot.org/annotation/VAR_041544|||http://purl.uniprot.org/annotation/VAR_064733|||http://purl.uniprot.org/annotation/VAR_064734|||http://purl.uniprot.org/annotation/VAR_075072|||http://purl.uniprot.org/annotation/VAR_078824|||http://purl.uniprot.org/annotation/VAR_078825|||http://purl.uniprot.org/annotation/VAR_078826|||http://purl.uniprot.org/annotation/VAR_078827|||http://purl.uniprot.org/annotation/VAR_078828|||http://purl.uniprot.org/annotation/VAR_078829|||http://purl.uniprot.org/annotation/VAR_078830|||http://purl.uniprot.org/annotation/VAR_078831|||http://purl.uniprot.org/annotation/VAR_078832|||http://purl.uniprot.org/annotation/VAR_078833|||http://purl.uniprot.org/annotation/VAR_078834|||http://purl.uniprot.org/annotation/VAR_078835|||http://purl.uniprot.org/annotation/VAR_078836|||http://purl.uniprot.org/annotation/VAR_078837|||http://purl.uniprot.org/annotation/VAR_078838|||http://purl.uniprot.org/annotation/VAR_078839|||http://purl.uniprot.org/annotation/VAR_078840|||http://purl.uniprot.org/annotation/VAR_078841|||http://purl.uniprot.org/annotation/VAR_078842|||http://purl.uniprot.org/annotation/VAR_078843
http://togogenome.org/gene/9606:GMEB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQS0|||http://purl.uniprot.org/uniprot/Q9UKD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Glucocorticoid modulatory element-binding protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Phosphoserine|||SAND                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074092
http://togogenome.org/gene/9606:DCAF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61962                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 7|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051425|||http://purl.uniprot.org/annotation/VSP_054015
http://togogenome.org/gene/9606:SLC25A38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DW6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In SIDBA2.|||Mitochondrial glycine transporter|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291802|||http://purl.uniprot.org/annotation/VAR_032862|||http://purl.uniprot.org/annotation/VAR_058093|||http://purl.uniprot.org/annotation/VAR_058094|||http://purl.uniprot.org/annotation/VAR_058095|||http://purl.uniprot.org/annotation/VAR_058096
http://togogenome.org/gene/9606:PLAC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZF1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Placenta-specific gene 8 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186092
http://togogenome.org/gene/9606:NIBAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Protein Niban 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213120|||http://purl.uniprot.org/annotation/VAR_053533|||http://purl.uniprot.org/annotation/VAR_053534|||http://purl.uniprot.org/annotation/VAR_053535|||http://purl.uniprot.org/annotation/VAR_053536
http://togogenome.org/gene/9606:DYNC1LI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PHI6|||http://purl.uniprot.org/uniprot/Q9Y6G9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cytoplasmic dynein 1 light intermediate chain 1|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114666|||http://purl.uniprot.org/annotation/VAR_023325|||http://purl.uniprot.org/annotation/VAR_061141
http://togogenome.org/gene/9606:EEIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9C2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 NT-type|||Disordered|||Early estrogen-induced gene 1 protein|||In isoform 2.|||In isoform 3.|||Polar residues|||Required for interaction with TNFRSF11A/RANK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261634|||http://purl.uniprot.org/annotation/VSP_021744|||http://purl.uniprot.org/annotation/VSP_043857
http://togogenome.org/gene/9606:ELP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKA4|||http://purl.uniprot.org/uniprot/B4DXV1|||http://purl.uniprot.org/uniprot/Q9H9T3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Elongator complex protein 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetyltransferase|||N6-methyllysine|||No effect on tyrosine phosphorylation.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ALK|||Radical SAM core|||Small reduction in tyrosine phosphorylation.|||Substantial reduction in tyrosine phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283986|||http://purl.uniprot.org/annotation/VSP_024406|||http://purl.uniprot.org/annotation/VSP_055284|||http://purl.uniprot.org/annotation/VSP_055285|||http://purl.uniprot.org/annotation/VSP_055286
http://togogenome.org/gene/9606:TANGO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTB6|||http://purl.uniprot.org/uniprot/Q9C0B7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||Helical|||Phosphoserine|||Polar residues|||RNA polymerase II assembly factor Rtp1 C-terminal|||Transport and Golgi organization protein 6 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305059
http://togogenome.org/gene/9606:SPEGNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV53                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  IQ|||Ig-like 1|||Ig-like 2|||SPEG neighbor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000448232
http://togogenome.org/gene/9606:CMTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1G2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1|||Disordered|||G-patch|||Interaction with POLR2A|||N6-acetyllysine|||No effect.|||Phosphoserine|||Polar residues|||Proton acceptor|||Reduces both mRNA cap binding and catalytic activity of the enzyme.|||RrmJ-type SAM-dependent 2'-O-MTase|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251239
http://togogenome.org/gene/9606:P2RY10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00398                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Putative P2Y purinoceptor 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070034|||http://purl.uniprot.org/annotation/VAR_033481
http://togogenome.org/gene/9606:ZFP92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NM28                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 92 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328807
http://togogenome.org/gene/9606:GRPEL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAA5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  GrpE protein homolog 2, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013052|||http://purl.uniprot.org/annotation/VSP_057020|||http://purl.uniprot.org/annotation/VSP_057021
http://togogenome.org/gene/9606:PTPRZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFE7|||http://purl.uniprot.org/uniprot/P23471                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Alpha-carbonic anhydrase|||Ancestral active site|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (chondroitin sulfate) serine; alternate|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; alternate|||Phosphothreonine|||Polar residues|||Receptor-type tyrosine-protein phosphatase zeta|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025468|||http://purl.uniprot.org/annotation/VAR_038942|||http://purl.uniprot.org/annotation/VAR_038943|||http://purl.uniprot.org/annotation/VAR_038944|||http://purl.uniprot.org/annotation/VSP_054061|||http://purl.uniprot.org/annotation/VSP_054062
http://togogenome.org/gene/9606:NEURL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||NHR 1|||NHR 2|||NHR 3|||NHR 4|||NHR 5|||NHR 6|||Neuralized-like protein 4|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299105|||http://purl.uniprot.org/annotation/VAR_049527|||http://purl.uniprot.org/annotation/VSP_027563
http://togogenome.org/gene/9606:INA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16352                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Alpha-internexin|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In a breast cancer sample; somatic mutation.|||Linker 1|||Linker 2|||N6-acetyllysine|||Phosphoserine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063783|||http://purl.uniprot.org/annotation/VAR_033497|||http://purl.uniprot.org/annotation/VAR_036369|||http://purl.uniprot.org/annotation/VAR_049808
http://togogenome.org/gene/9606:CIMIP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6J272                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule inner protein 2A|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325900|||http://purl.uniprot.org/annotation/VSP_032470|||http://purl.uniprot.org/annotation/VSP_032471
http://togogenome.org/gene/9606:ADGRG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z303|||http://purl.uniprot.org/uniprot/E9PHI0|||http://purl.uniprot.org/uniprot/Q6ZMH4|||http://purl.uniprot.org/uniprot/Q96K78                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor G7|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012903|||http://purl.uniprot.org/annotation/PRO_5002866697|||http://purl.uniprot.org/annotation/PRO_5003245033|||http://purl.uniprot.org/annotation/VAR_049459|||http://purl.uniprot.org/annotation/VAR_049460|||http://purl.uniprot.org/annotation/VAR_055138
http://togogenome.org/gene/9606:NUDT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Diphosphoinositol polyphosphate phosphohydrolase 3-alpha|||Disordered|||Nudix box|||Nudix hydrolase|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057062
http://togogenome.org/gene/9606:MPP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2T1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with DLG1.|||Does not affect the interaction with DLG1.|||Guanylate kinase-like|||In isoform 2.|||L27 1|||L27 2|||MAGUK p55 subfamily member 7|||PDZ|||Phospho-regulated basic and hydrophobic (PRBH) motif|||Phosphoserine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320027|||http://purl.uniprot.org/annotation/VAR_039110|||http://purl.uniprot.org/annotation/VSP_056065|||http://purl.uniprot.org/annotation/VSP_056066|||http://purl.uniprot.org/annotation/VSP_056067
http://togogenome.org/gene/9606:TLCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||TLC|||TLC domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328990
http://togogenome.org/gene/9606:RORB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58EY0                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||NR LBD|||Nuclear receptor                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PCDHA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN75                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003906|||http://purl.uniprot.org/annotation/VSP_000695|||http://purl.uniprot.org/annotation/VSP_000696
http://togogenome.org/gene/9606:OR2T6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHC8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150501|||http://purl.uniprot.org/annotation/VAR_053152|||http://purl.uniprot.org/annotation/VAR_053153|||http://purl.uniprot.org/annotation/VAR_053154|||http://purl.uniprot.org/annotation/VAR_060001|||http://purl.uniprot.org/annotation/VAR_060002
http://togogenome.org/gene/9606:GRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM7|||http://purl.uniprot.org/uniprot/P07492                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gastrin-releasing peptide|||In isoform 2.|||In isoform 3.|||Methionine amide|||Neuromedin-C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003035|||http://purl.uniprot.org/annotation/PRO_0000003036|||http://purl.uniprot.org/annotation/PRO_0000003037|||http://purl.uniprot.org/annotation/PRO_5007491734|||http://purl.uniprot.org/annotation/VAR_027834|||http://purl.uniprot.org/annotation/VSP_000549|||http://purl.uniprot.org/annotation/VSP_000550
http://togogenome.org/gene/9606:TUBB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS31|||http://purl.uniprot.org/uniprot/B4E386|||http://purl.uniprot.org/uniprot/K7EJ64|||http://purl.uniprot.org/uniprot/Q9BUF5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||In FPVEPD; may affect microtubules stability.|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-6 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048255|||http://purl.uniprot.org/annotation/VAR_080406
http://togogenome.org/gene/9606:ATP5F1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36542|||http://purl.uniprot.org/uniprot/Q8TAS0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase subunit gamma, mitochondrial|||In isoform Heart.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002685|||http://purl.uniprot.org/annotation/VSP_000439
http://togogenome.org/gene/9606:SKIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8J1|||http://purl.uniprot.org/uniprot/A0A8V8TLC0|||http://purl.uniprot.org/uniprot/Q15477                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished helicase activity.|||DEVH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In THES2; abolished ATPase activity.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Superkiller complex protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102091|||http://purl.uniprot.org/annotation/VAR_035944|||http://purl.uniprot.org/annotation/VAR_035945|||http://purl.uniprot.org/annotation/VAR_055888|||http://purl.uniprot.org/annotation/VAR_055889|||http://purl.uniprot.org/annotation/VAR_055890|||http://purl.uniprot.org/annotation/VAR_055891|||http://purl.uniprot.org/annotation/VAR_060379|||http://purl.uniprot.org/annotation/VAR_060380|||http://purl.uniprot.org/annotation/VAR_060381|||http://purl.uniprot.org/annotation/VAR_060382|||http://purl.uniprot.org/annotation/VAR_067721
http://togogenome.org/gene/9606:C9orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C9orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295144|||http://purl.uniprot.org/annotation/VAR_033220|||http://purl.uniprot.org/annotation/VAR_033221|||http://purl.uniprot.org/annotation/VAR_033222|||http://purl.uniprot.org/annotation/VAR_033223
http://togogenome.org/gene/9606:IL12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29460                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Fibronectin type-III|||Ig-like C2-type|||Interchain (with C-96 in IL12A and C-73 in IL23A)|||Interleukin-12 subunit beta|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000187|||http://purl.uniprot.org/annotation/PRO_0000010930|||http://purl.uniprot.org/annotation/VAR_020001|||http://purl.uniprot.org/annotation/VAR_049170
http://togogenome.org/gene/9606:SLC15A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2CQT6|||http://purl.uniprot.org/uniprot/P46059                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished peptide transporter activity.|||Cytoplasmic|||Does not affect peptide transporter activity.|||Extracellular|||Extracellular domain (ECD)|||Helical|||N-linked (GlcNAc...) asparagine|||Nearly abolished peptide transporter activity.|||Reduced peptide transporter activity.|||Solute carrier family 15 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064304|||http://purl.uniprot.org/annotation/VAR_020456|||http://purl.uniprot.org/annotation/VAR_020457|||http://purl.uniprot.org/annotation/VAR_020458|||http://purl.uniprot.org/annotation/VAR_022147|||http://purl.uniprot.org/annotation/VAR_022148|||http://purl.uniprot.org/annotation/VAR_022149|||http://purl.uniprot.org/annotation/VAR_029321|||http://purl.uniprot.org/annotation/VAR_029322|||http://purl.uniprot.org/annotation/VAR_029323|||http://purl.uniprot.org/annotation/VAR_029324
http://togogenome.org/gene/9606:PIK3C2G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLY6|||http://purl.uniprot.org/uniprot/F5H369|||http://purl.uniprot.org/uniprot/O75747                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||C2|||C2 PI3K-type|||Catalytic loop|||G-loop|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088799|||http://purl.uniprot.org/annotation/VAR_056676|||http://purl.uniprot.org/annotation/VAR_056677|||http://purl.uniprot.org/annotation/VAR_060323|||http://purl.uniprot.org/annotation/VAR_060324|||http://purl.uniprot.org/annotation/VAR_060325
http://togogenome.org/gene/9606:RTN4RL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GPI-anchor amidated cysteine|||Important for interaction with MAG|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Reticulon-4 receptor-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046048|||http://purl.uniprot.org/annotation/PRO_0000046049|||http://purl.uniprot.org/annotation/VSP_047767|||http://purl.uniprot.org/annotation/VSP_047768
http://togogenome.org/gene/9606:PRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV00|||http://purl.uniprot.org/uniprot/O14744                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Beta barrel|||Critical for specifying symmetric addition of methyl groups|||Dimerization|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4.|||Increased MAPK1/MAPK3 phosphorylation in response to EGF.|||N-acetylalanine; in Protein arginine N-methyltransferase 5, N-terminally processed|||PRMT5 TIM barrel|||PRMT5 arginine-N-methyltransferase|||PRMT5 oligomerisation|||Protein arginine N-methyltransferase 5|||Protein arginine N-methyltransferase 5, N-terminally processed|||Proton donor/acceptor|||Removed; alternate|||SAM-dependent MTase PRMT-type|||TIM barrel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212342|||http://purl.uniprot.org/annotation/PRO_0000417602|||http://purl.uniprot.org/annotation/VSP_043382|||http://purl.uniprot.org/annotation/VSP_054685|||http://purl.uniprot.org/annotation/VSP_054768
http://togogenome.org/gene/9606:SMYD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRG4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes methyltransferase activity on p53/TP53.|||Abolishes methyltransferase activity.|||In isoform 2.|||MYND-type|||N-lysine methyltransferase SMYD2|||No effect on methyltransferase activity on p53/TP53.|||Phosphoserine|||Reduces methyltransferase activity on p53/TP53.|||SET|||Slightly reduces methyltransferase activity on p53/TP53.|||Strongly reduces methyltransferase activity on p53/TP53.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218309|||http://purl.uniprot.org/annotation/VAR_023442|||http://purl.uniprot.org/annotation/VAR_052991|||http://purl.uniprot.org/annotation/VSP_056005
http://togogenome.org/gene/9606:MYH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13535                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In CACOV and DA7.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-8|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123413|||http://purl.uniprot.org/annotation/VAR_019810|||http://purl.uniprot.org/annotation/VAR_030207|||http://purl.uniprot.org/annotation/VAR_030208|||http://purl.uniprot.org/annotation/VAR_030209|||http://purl.uniprot.org/annotation/VAR_050202|||http://purl.uniprot.org/annotation/VAR_050203|||http://purl.uniprot.org/annotation/VAR_050204
http://togogenome.org/gene/9606:EHMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GV09|||http://purl.uniprot.org/uniprot/Q9H9B1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Abolishes binding to histone H3K9me.|||Abolishes binding to methylated RELAK310me1, histone H3K9me1 and H3K9me2.|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone H3K9me binding|||Histone-lysine N-methyltransferase EHMT1|||In KLEFS1.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with histone H3|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pre-SET|||Removed|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186067|||http://purl.uniprot.org/annotation/VAR_027642|||http://purl.uniprot.org/annotation/VAR_036345|||http://purl.uniprot.org/annotation/VAR_036346|||http://purl.uniprot.org/annotation/VAR_069183|||http://purl.uniprot.org/annotation/VSP_002222|||http://purl.uniprot.org/annotation/VSP_002223|||http://purl.uniprot.org/annotation/VSP_002224|||http://purl.uniprot.org/annotation/VSP_002225|||http://purl.uniprot.org/annotation/VSP_040717|||http://purl.uniprot.org/annotation/VSP_040718
http://togogenome.org/gene/9606:ZNF438                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T427|||http://purl.uniprot.org/uniprot/Q7Z4V0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger protein 438                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245847|||http://purl.uniprot.org/annotation/VAR_027013|||http://purl.uniprot.org/annotation/VAR_035580|||http://purl.uniprot.org/annotation/VAR_061946|||http://purl.uniprot.org/annotation/VSP_019799|||http://purl.uniprot.org/annotation/VSP_019800
http://togogenome.org/gene/9606:CAB39L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WE6|||http://purl.uniprot.org/uniprot/Q9H9S4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Calcium-binding protein 39-like|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209826
http://togogenome.org/gene/9606:SRD5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18405                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  3-oxo-5-alpha-steroid 4-dehydrogenase 1|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213674
http://togogenome.org/gene/9606:PSMB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8D7|||http://purl.uniprot.org/uniprot/P28065                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Impairs correct processing at the consensus site.|||In PRAAS3; digenic inheritance; patient also carries a mutation in PSMB4; patients' cells show reduction of proteasome content and cysteine-type endopeptidase activity of the proteasome.|||In isoform LMP2.S.|||N6-acetyllysine|||Nucleophile|||Proteasome subunit beta type-9|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026619|||http://purl.uniprot.org/annotation/PRO_0000026620|||http://purl.uniprot.org/annotation/VAR_013578|||http://purl.uniprot.org/annotation/VAR_051551|||http://purl.uniprot.org/annotation/VAR_051552|||http://purl.uniprot.org/annotation/VAR_051553|||http://purl.uniprot.org/annotation/VAR_075258|||http://purl.uniprot.org/annotation/VSP_005288
http://togogenome.org/gene/9606:WDR76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFX7|||http://purl.uniprot.org/uniprot/Q9H967                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 76                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242691|||http://purl.uniprot.org/annotation/VAR_026862|||http://purl.uniprot.org/annotation/VAR_026863
http://togogenome.org/gene/9606:FKBP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7YQ73|||http://purl.uniprot.org/uniprot/O95302                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PPIase FKBP-type|||PPIase FKBP-type 1|||PPIase FKBP-type 2|||PPIase FKBP-type 3|||PPIase FKBP-type 4|||Peptidyl-prolyl cis-trans isomerase FKBP9|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045760|||http://purl.uniprot.org/annotation/VSP_054825|||http://purl.uniprot.org/annotation/VSP_054826
http://togogenome.org/gene/9606:CFDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0H5APX3|||http://purl.uniprot.org/uniprot/A0A0H5AUJ9|||http://purl.uniprot.org/uniprot/Q9UEE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||BCNT-C|||Basic and acidic residues|||Craniofacial development protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hydrophilic|||In isoform 2.|||N6-methyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212494|||http://purl.uniprot.org/annotation/VAR_048408|||http://purl.uniprot.org/annotation/VSP_016242
http://togogenome.org/gene/9606:HOXC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43248                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein Hox-C11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200192|||http://purl.uniprot.org/annotation/VAR_031850|||http://purl.uniprot.org/annotation/VAR_034002
http://togogenome.org/gene/9606:OLAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV23                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||S-acyl fatty acid synthase thioesterase, medium chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180358|||http://purl.uniprot.org/annotation/VSP_040022
http://togogenome.org/gene/9606:KL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UEF7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycosyl hydrolase-1 1|||Glycosyl hydrolase-1 2|||Helical|||In HFTC3; impairs the ability to form a ternary complex with FGF23 and FGFR1c; impairs KL-dependent FGF23 signaling.|||In a colorectal cancer sample; somatic mutation.|||In allele KL-VS; associated with S-370.|||In allele KL-VS; associated with V-352.|||In isoform 2.|||Klotho|||Klotho peptide|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042243|||http://purl.uniprot.org/annotation/PRO_0000042244|||http://purl.uniprot.org/annotation/VAR_023582|||http://purl.uniprot.org/annotation/VAR_023583|||http://purl.uniprot.org/annotation/VAR_023584|||http://purl.uniprot.org/annotation/VAR_023585|||http://purl.uniprot.org/annotation/VAR_036449|||http://purl.uniprot.org/annotation/VAR_049295|||http://purl.uniprot.org/annotation/VAR_064554|||http://purl.uniprot.org/annotation/VSP_015824|||http://purl.uniprot.org/annotation/VSP_015825
http://togogenome.org/gene/9606:SLC6A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23975                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In OI; loss of function.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sodium-dependent noradrenaline transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214748|||http://purl.uniprot.org/annotation/VAR_010022|||http://purl.uniprot.org/annotation/VAR_011756|||http://purl.uniprot.org/annotation/VAR_011757|||http://purl.uniprot.org/annotation/VAR_011758|||http://purl.uniprot.org/annotation/VAR_011759|||http://purl.uniprot.org/annotation/VAR_011760|||http://purl.uniprot.org/annotation/VAR_011761|||http://purl.uniprot.org/annotation/VAR_011762|||http://purl.uniprot.org/annotation/VAR_011763|||http://purl.uniprot.org/annotation/VAR_011764|||http://purl.uniprot.org/annotation/VAR_011765|||http://purl.uniprot.org/annotation/VAR_011766|||http://purl.uniprot.org/annotation/VAR_014800|||http://purl.uniprot.org/annotation/VAR_020048|||http://purl.uniprot.org/annotation/VAR_021861|||http://purl.uniprot.org/annotation/VAR_029157|||http://purl.uniprot.org/annotation/VSP_044479|||http://purl.uniprot.org/annotation/VSP_054119
http://togogenome.org/gene/9606:CHD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCK8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATPase activity.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 8|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In IDDAM.|||In IDDAM; unknown pathological significance.|||In isoform 2.|||Interaction with FAM124B|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080233|||http://purl.uniprot.org/annotation/VAR_069573|||http://purl.uniprot.org/annotation/VAR_078704|||http://purl.uniprot.org/annotation/VSP_017270
http://togogenome.org/gene/9606:TMEM92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXU6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues|||Transmembrane protein 92                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251709|||http://purl.uniprot.org/annotation/VAR_027703|||http://purl.uniprot.org/annotation/VAR_027704|||http://purl.uniprot.org/annotation/VAR_061715
http://togogenome.org/gene/9606:ACTR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GD5|||http://purl.uniprot.org/uniprot/Q9P1U1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 3B|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342358|||http://purl.uniprot.org/annotation/VAR_048188|||http://purl.uniprot.org/annotation/VSP_034418|||http://purl.uniprot.org/annotation/VSP_041474
http://togogenome.org/gene/9606:SAMD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGI4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||SAM|||Sterile alpha motif domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311361
http://togogenome.org/gene/9606:HDAC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZH6|||http://purl.uniprot.org/uniprot/Q9BRX7|||http://purl.uniprot.org/uniprot/Q9NSW6|||http://purl.uniprot.org/uniprot/Q9UBN7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||Acidic residues|||Disordered|||Histone deacetylase 1|||Histone deacetylase 2|||Histone deacetylase 6|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces histone deacetylase activity. Abolishes HDAC6-mediated deacetylation of alpha-tubulin. Abolishes HDAC6-mediated deacetylation of alpha-tubulin; when associated with A-216.|||Reduces histone deacetylase activity. Does not affect HDAC6-mediated deacetylation of alpha-tubulin. Abolishes HDAC6-mediated deacetylation of alpha-tubulin; when associated with A-611.|||UBP-type|||Ubiquitin binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114703|||http://purl.uniprot.org/annotation/VAR_046300|||http://purl.uniprot.org/annotation/VAR_068962|||http://purl.uniprot.org/annotation/VSP_044576
http://togogenome.org/gene/9606:ARF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61204                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor 3|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207386|||http://purl.uniprot.org/annotation/VSP_056935
http://togogenome.org/gene/9606:NUTM2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L443                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||NUT family member 2F|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337995|||http://purl.uniprot.org/annotation/VAR_068009|||http://purl.uniprot.org/annotation/VAR_068010
http://togogenome.org/gene/9606:ZNF454                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9F8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 454                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047600|||http://purl.uniprot.org/annotation/VAR_033568|||http://purl.uniprot.org/annotation/VAR_059919
http://togogenome.org/gene/9606:SURF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15526                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In CMT4K; unknown pathological significance.|||In MC4DN1.|||In MC4DN1; benign variant.|||In MC4DN1; reduced protein stability.|||In MC4DN1; unknown pathological significance.|||In MC4DN1; unknown pathological significance; reduces protein stability; impairs complex IV assembly.|||In MC4DN1; unknown pathological significance; reduces protein stability; impairs complex IV assembly; .|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Surfeit locus protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215652|||http://purl.uniprot.org/annotation/VAR_007450|||http://purl.uniprot.org/annotation/VAR_007451|||http://purl.uniprot.org/annotation/VAR_007452|||http://purl.uniprot.org/annotation/VAR_015258|||http://purl.uniprot.org/annotation/VAR_015259|||http://purl.uniprot.org/annotation/VAR_036340|||http://purl.uniprot.org/annotation/VAR_068648|||http://purl.uniprot.org/annotation/VAR_068649|||http://purl.uniprot.org/annotation/VAR_068650|||http://purl.uniprot.org/annotation/VAR_068651|||http://purl.uniprot.org/annotation/VAR_068652|||http://purl.uniprot.org/annotation/VAR_068653|||http://purl.uniprot.org/annotation/VAR_068654|||http://purl.uniprot.org/annotation/VAR_068682|||http://purl.uniprot.org/annotation/VAR_076315|||http://purl.uniprot.org/annotation/VAR_083393|||http://purl.uniprot.org/annotation/VAR_083394|||http://purl.uniprot.org/annotation/VAR_083395|||http://purl.uniprot.org/annotation/VAR_083396|||http://purl.uniprot.org/annotation/VAR_083397|||http://purl.uniprot.org/annotation/VSP_034817
http://togogenome.org/gene/9606:HDAC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQL6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by PKC.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not affect phosphorylation by PKC.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase|||Histone deacetylase 5|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||No effect.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1|||Phosphothreonine; by PKC|||Polar residues|||Pro residues|||Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259.|||Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2.|||Reduces CaMK-dependent nuclear export.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114701|||http://purl.uniprot.org/annotation/VAR_055903|||http://purl.uniprot.org/annotation/VAR_055904|||http://purl.uniprot.org/annotation/VSP_002081|||http://purl.uniprot.org/annotation/VSP_039180
http://togogenome.org/gene/9606:CYB5D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUJ1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Neuferricin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312321|||http://purl.uniprot.org/annotation/VAR_037487|||http://purl.uniprot.org/annotation/VAR_037488|||http://purl.uniprot.org/annotation/VSP_045028
http://togogenome.org/gene/9606:USF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15853                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform USF2A-delta-H.|||In isoform USF2B.|||In isoform USF2c.|||Leucine-zipper|||Upstream stimulatory factor 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127500|||http://purl.uniprot.org/annotation/VSP_002164|||http://purl.uniprot.org/annotation/VSP_002165|||http://purl.uniprot.org/annotation/VSP_047804
http://togogenome.org/gene/9606:ARSF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54793                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase F|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033427|||http://purl.uniprot.org/annotation/VAR_058846
http://togogenome.org/gene/9606:MEX3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L020                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||KH 1|||KH 2|||Phosphoserine|||Pro residues|||RING-type|||RNA-binding protein MEX3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281013
http://togogenome.org/gene/9606:GNA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29992                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Deamidated glutamine; by Photorhabdus PAU_02230|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-11|||In HHC2; induces a decrease in sensitivity to changes in extracellular calcium concentrations.|||In HYPOC2.|||In HYPOC2; induces an increase in sensitivity to changes in extracellular calcium concentrations.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203746|||http://purl.uniprot.org/annotation/VAR_070165|||http://purl.uniprot.org/annotation/VAR_070166|||http://purl.uniprot.org/annotation/VAR_070167|||http://purl.uniprot.org/annotation/VAR_070168|||http://purl.uniprot.org/annotation/VAR_070169|||http://purl.uniprot.org/annotation/VAR_070170
http://togogenome.org/gene/9606:RAD9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99638                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by ABL1.|||Cell cycle checkpoint control protein RAD9A|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-380.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-387.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-380 and A-387.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-375; A-380 and A-387.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-341; A-375; A-380 and A-387.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-328; A-341; A-375; A-380 and A-387.|||Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-277; A-328; A-341; A-375; A-380 and A-387.|||Disordered|||Phosphoserine|||Phosphotyrosine|||Possesses 3'-5' exonuclease activity|||Sufficient for interaction with ABL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225000|||http://purl.uniprot.org/annotation/VAR_025410|||http://purl.uniprot.org/annotation/VAR_025411|||http://purl.uniprot.org/annotation/VAR_025412|||http://purl.uniprot.org/annotation/VAR_025413|||http://purl.uniprot.org/annotation/VAR_051724
http://togogenome.org/gene/9606:RPL31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62899                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein eL31|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153763|||http://purl.uniprot.org/annotation/VSP_042572|||http://purl.uniprot.org/annotation/VSP_043224
http://togogenome.org/gene/9606:ATP6V0A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In DRTA3.|||Polar residues|||V-type proton ATPase 116 kDa subunit a 4|||Vacuolar                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119219|||http://purl.uniprot.org/annotation/VAR_017255|||http://purl.uniprot.org/annotation/VAR_017256|||http://purl.uniprot.org/annotation/VAR_017257|||http://purl.uniprot.org/annotation/VAR_020992|||http://purl.uniprot.org/annotation/VAR_020993|||http://purl.uniprot.org/annotation/VAR_020994|||http://purl.uniprot.org/annotation/VAR_020995|||http://purl.uniprot.org/annotation/VAR_020996|||http://purl.uniprot.org/annotation/VAR_066612|||http://purl.uniprot.org/annotation/VAR_066613
http://togogenome.org/gene/9606:ITPRIPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIP1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Inositol 1,4,5-trisphosphate receptor-interacting protein-like 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336093|||http://purl.uniprot.org/annotation/VAR_043549|||http://purl.uniprot.org/annotation/VAR_043550
http://togogenome.org/gene/9606:PNPLA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6Z6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DGA/G|||GXGXXG|||GXSXG|||In isoform 2.|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 5|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292021|||http://purl.uniprot.org/annotation/VAR_032932|||http://purl.uniprot.org/annotation/VAR_032933|||http://purl.uniprot.org/annotation/VAR_032934|||http://purl.uniprot.org/annotation/VSP_026373
http://togogenome.org/gene/9606:TMEM165                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC07                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alters subcellular location.|||Cytoplasmic|||Disordered|||Helical|||In CDG2K; accumulates in Golgi compartment; displays decreased affinity for Ca(2+) ions; does not affect the affinity for Mn(2+) ions.|||In CDG2K; alters subcellular location; displays decreased affinity for Ca(2+) ions; does not affect the affinity for Mn(2+) ions.|||In CDG2K; alters subcellular location; does not affect the affinity for Ca(2+) and Mn(2+) ions.|||In CDG2K; does not affect the affinity for Ca(2+) and Mn(2+) ions.|||In isoform 2.|||Lumenal|||No effect on subcellular location.|||Putative divalent cation/proton antiporter TMEM165                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247334|||http://purl.uniprot.org/annotation/VAR_068446|||http://purl.uniprot.org/annotation/VAR_068447|||http://purl.uniprot.org/annotation/VAR_068448|||http://purl.uniprot.org/annotation/VAR_088436|||http://purl.uniprot.org/annotation/VSP_056691
http://togogenome.org/gene/9606:CNN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDF4|||http://purl.uniprot.org/uniprot/B4DUT8|||http://purl.uniprot.org/uniprot/Q99439                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Calponin-2|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||Disordered|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204773|||http://purl.uniprot.org/annotation/VSP_042941
http://togogenome.org/gene/9606:TMOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28289                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Tropomodulin-1|||Tropomyosin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186128|||http://purl.uniprot.org/annotation/VSP_056863|||http://purl.uniprot.org/annotation/VSP_056864
http://togogenome.org/gene/9606:CCDC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G8IFA7|||http://purl.uniprot.org/uniprot/Q9H0W5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 8|||Decreased interaction with ANKRA2.|||Disordered|||Phosphoserine|||PxLPxI/L motif; mediates interaction with ANKRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089401|||http://purl.uniprot.org/annotation/VAR_020272|||http://purl.uniprot.org/annotation/VAR_061587|||http://purl.uniprot.org/annotation/VAR_061588
http://togogenome.org/gene/9606:AMPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01433                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP deaminase 2|||Disordered|||In PCH9.|||In isoform 5.|||In isoform Ex1A-2-3.|||In isoform Ex1B-3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194407|||http://purl.uniprot.org/annotation/VAR_069105|||http://purl.uniprot.org/annotation/VAR_071158|||http://purl.uniprot.org/annotation/VAR_071159|||http://purl.uniprot.org/annotation/VAR_071193|||http://purl.uniprot.org/annotation/VSP_001271|||http://purl.uniprot.org/annotation/VSP_001272|||http://purl.uniprot.org/annotation/VSP_001273|||http://purl.uniprot.org/annotation/VSP_045975
http://togogenome.org/gene/9606:SAP30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75446                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abolishes zinc-binding.|||Atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP30|||Interaction with NCOR1|||Interaction with SIN3A|||Phosphoserine|||Phosphothreonine|||Retains zinc-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097582
http://togogenome.org/gene/9606:ERMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMD3|||http://purl.uniprot.org/uniprot/Q7Z2K6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum metallopeptidase 1|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259492|||http://purl.uniprot.org/annotation/VAR_028945|||http://purl.uniprot.org/annotation/VSP_056121|||http://purl.uniprot.org/annotation/VSP_056122
http://togogenome.org/gene/9606:CCDC198                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL43|||http://purl.uniprot.org/uniprot/E9PSE9|||http://purl.uniprot.org/uniprot/F5GWJ3|||http://purl.uniprot.org/uniprot/Q9NVL8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Factor associated with metabolism and energy|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089913|||http://purl.uniprot.org/annotation/VAR_024310
http://togogenome.org/gene/9606:SUPT16H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5B9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||FACT complex subunit SPT16|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NEDDFAC; unknown pathological significance.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245169|||http://purl.uniprot.org/annotation/VAR_086185|||http://purl.uniprot.org/annotation/VAR_086186|||http://purl.uniprot.org/annotation/VAR_086187|||http://purl.uniprot.org/annotation/VAR_086188
http://togogenome.org/gene/9606:MED17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVC6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In MCPHSBA.|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079359|||http://purl.uniprot.org/annotation/VAR_057781|||http://purl.uniprot.org/annotation/VAR_063126|||http://purl.uniprot.org/annotation/VAR_065066|||http://purl.uniprot.org/annotation/VSP_028115|||http://purl.uniprot.org/annotation/VSP_028116
http://togogenome.org/gene/9606:PKHD1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WI1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibrocystin-L|||G8 1|||G8 2|||Helical|||IPT/TIG 1|||IPT/TIG 10|||IPT/TIG 11|||IPT/TIG 12|||IPT/TIG 13|||IPT/TIG 14|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||IPT/TIG 5|||IPT/TIG 6|||IPT/TIG 7|||IPT/TIG 8|||IPT/TIG 9|||O-linked (GalNAc...) threonine|||PA14|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||PbH1 6|||PbH1 7|||PbH1 8|||PbH1 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318572|||http://purl.uniprot.org/annotation/VAR_038760|||http://purl.uniprot.org/annotation/VAR_038761|||http://purl.uniprot.org/annotation/VAR_038762|||http://purl.uniprot.org/annotation/VAR_038763|||http://purl.uniprot.org/annotation/VAR_038764|||http://purl.uniprot.org/annotation/VAR_038765|||http://purl.uniprot.org/annotation/VAR_038766|||http://purl.uniprot.org/annotation/VAR_038767|||http://purl.uniprot.org/annotation/VAR_038768|||http://purl.uniprot.org/annotation/VAR_038769|||http://purl.uniprot.org/annotation/VAR_038770|||http://purl.uniprot.org/annotation/VAR_038771|||http://purl.uniprot.org/annotation/VAR_038772|||http://purl.uniprot.org/annotation/VAR_038773|||http://purl.uniprot.org/annotation/VAR_038774
http://togogenome.org/gene/9606:BCL2L11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRE7|||http://purl.uniprot.org/uniprot/A0A0C4DH20|||http://purl.uniprot.org/uniprot/O43521                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes induction of apoptosis. Abolishes interaction with BAX and BCL2; in isoform Bim-alpha3 and isoform BimS. Loses the ability to induce the conformationally active form of BAX.|||Apoptosis Bim N-terminal|||BH3|||Bcl-2-like protein 11|||Disordered|||In isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3.|||In isoform Bim-alpha4.|||In isoform Bim-alpha5 and isoform Bim-alpha6.|||In isoform Bim-beta1, isoform Bim-beta2 and isoform Bim-beta6.|||In isoform Bim-beta1.|||In isoform Bim-beta2 and isoform Bim-beta6.|||In isoform Bim-beta3.|||In isoform Bim-beta4.|||In isoform Bim-beta5 and isoform Bim-beta7.|||In isoform Bim-gamma.|||In isoform BimA.|||In isoform BimABC, isoform BimL, isoform Bim-alpha2, isoform Bim-gamma, isoform Bim-beta6 and isoform Bim-beta7.|||In isoform BimAC and isoform BimABC.|||In isoform BimS, isoform Bim-alpha3, isoform Bim-alpha6 and isoform Bim-alpha4.|||Phosphoserine|||Phosphoserine; by MAPK|||Polar residues|||Retains the ability to induce apoptosis. Abolishes interaction with BAX; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BCL2.|||Retains the ability to induce apoptosis. Abolishes interaction with BCL2; in isoform Bim-alpha3 and isoform BimS. No effect on interaction with BAX.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143109|||http://purl.uniprot.org/annotation/VSP_000535|||http://purl.uniprot.org/annotation/VSP_035608|||http://purl.uniprot.org/annotation/VSP_035609|||http://purl.uniprot.org/annotation/VSP_035610|||http://purl.uniprot.org/annotation/VSP_035611|||http://purl.uniprot.org/annotation/VSP_035612|||http://purl.uniprot.org/annotation/VSP_035613|||http://purl.uniprot.org/annotation/VSP_035614|||http://purl.uniprot.org/annotation/VSP_035615|||http://purl.uniprot.org/annotation/VSP_035616|||http://purl.uniprot.org/annotation/VSP_035617|||http://purl.uniprot.org/annotation/VSP_035618|||http://purl.uniprot.org/annotation/VSP_035619|||http://purl.uniprot.org/annotation/VSP_035620|||http://purl.uniprot.org/annotation/VSP_042865|||http://purl.uniprot.org/annotation/VSP_042866
http://togogenome.org/gene/9606:HEATR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4Q2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT repeat-containing protein 3|||In DBA21; severe decrease of protein levels in patient cells; bone marrow patient cells show abnormal acceleration of erythrocyte maturation suggesting impaired function; affects function in RPL5 nuclear import as shown in patient cells.|||In DBA21; severe decrease of protein levels in patient cells; results in impaired biogenesis of 60S ribosomal subunits.|||In DBA21; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050821|||http://purl.uniprot.org/annotation/VAR_033989|||http://purl.uniprot.org/annotation/VAR_087794|||http://purl.uniprot.org/annotation/VAR_087795|||http://purl.uniprot.org/annotation/VAR_087796|||http://purl.uniprot.org/annotation/VAR_087797|||http://purl.uniprot.org/annotation/VSP_009640|||http://purl.uniprot.org/annotation/VSP_009641|||http://purl.uniprot.org/annotation/VSP_009642
http://togogenome.org/gene/9606:DEFB130A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP73|||http://purl.uniprot.org/uniprot/P0DP74                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 130A|||Beta-defensin 130B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045369|||http://purl.uniprot.org/annotation/PRO_0000440984
http://togogenome.org/gene/9606:PNRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes the interaction with DCP1A.|||Abolishes the interaction with the nuclear receptors but not decapping enzyme; when associated with A-101.|||Abolishes the interaction with the nuclear receptors but not decapping enzyme; when associated with A-104.|||Disordered|||In isoform 2.|||Polar residues|||Proline-rich nuclear receptor coactivator 2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058485|||http://purl.uniprot.org/annotation/VSP_037463
http://togogenome.org/gene/9606:PTBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26599                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polypyrimidine tract-binding protein 1|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081737|||http://purl.uniprot.org/annotation/VSP_061652|||http://purl.uniprot.org/annotation/VSP_061653
http://togogenome.org/gene/9606:GALNT16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68VJ8|||http://purl.uniprot.org/uniprot/Q8N428                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||Polypeptide N-acetylgalactosaminyltransferase 16|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059135|||http://purl.uniprot.org/annotation/VAR_055848|||http://purl.uniprot.org/annotation/VAR_061195|||http://purl.uniprot.org/annotation/VSP_011231
http://togogenome.org/gene/9606:NDUFA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43678                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2|||Redox-active|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118789|||http://purl.uniprot.org/annotation/VAR_036174|||http://purl.uniprot.org/annotation/VSP_045479
http://togogenome.org/gene/9606:KRTAP4-11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||27 X 5 AA repeats of C-C-[GIKRQVHEL]-[SPTR]-[STVQRMC]|||3|||4|||5|||6|||7|||8|||9|||In allele KAP4.14.|||Keratin-associated protein 4-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185180|||http://purl.uniprot.org/annotation/VAR_064553
http://togogenome.org/gene/9606:WNT7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56706                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered linker|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-7b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041444
http://togogenome.org/gene/9606:BCAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54687                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Branched-chain-amino-acid aminotransferase, cytosolic|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000103292|||http://purl.uniprot.org/annotation/VAR_019614|||http://purl.uniprot.org/annotation/VAR_047681|||http://purl.uniprot.org/annotation/VAR_047682|||http://purl.uniprot.org/annotation/VSP_042651|||http://purl.uniprot.org/annotation/VSP_042652|||http://purl.uniprot.org/annotation/VSP_043560|||http://purl.uniprot.org/annotation/VSP_046057
http://togogenome.org/gene/9606:SNX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95219                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location.|||Disordered|||In isoform 2.|||N-acetylmethionine|||PX|||Phosphoserine|||Sorting nexin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213842|||http://purl.uniprot.org/annotation/VSP_056665
http://togogenome.org/gene/9606:TMEM248                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWD8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Transmembrane protein 248                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295126|||http://purl.uniprot.org/annotation/VSP_026736|||http://purl.uniprot.org/annotation/VSP_026737
http://togogenome.org/gene/9606:TMSB4Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14604                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Thymosin beta-4, Y-chromosomal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045921
http://togogenome.org/gene/9606:ZC3HC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with SKP1.|||C3HC-type|||Disordered|||Does not strongly affect phosphorylation status; when associated with F-105.|||Does not strongly affect phosphorylation status; when associated with F-137.|||F-box-like|||In isoform 2.|||In isoform 3.|||Induces a complete cytoplasmic redistribution.|||Induces a partial cytoplasmic redistribution.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Strongly reduces phosphorylation and induces the formation of a constitutive SCF(NIPA) E3 complex that degrades CCNB1 at G2/M phase and delays mitotic entry.|||Zinc finger C3HC-type protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096849|||http://purl.uniprot.org/annotation/VAR_023312|||http://purl.uniprot.org/annotation/VAR_023313|||http://purl.uniprot.org/annotation/VSP_015217|||http://purl.uniprot.org/annotation/VSP_015218
http://togogenome.org/gene/9606:KLK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43240                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Kallikrein-10|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027953|||http://purl.uniprot.org/annotation/VAR_027979|||http://purl.uniprot.org/annotation/VAR_027980
http://togogenome.org/gene/9606:ZNF841                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN19                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16; degenerate|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Zinc finger protein 841                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334677|||http://purl.uniprot.org/annotation/VSP_033755|||http://purl.uniprot.org/annotation/VSP_040752
http://togogenome.org/gene/9606:CCDC42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M95                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 42|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234498|||http://purl.uniprot.org/annotation/VAR_026282|||http://purl.uniprot.org/annotation/VAR_057786|||http://purl.uniprot.org/annotation/VAR_057787|||http://purl.uniprot.org/annotation/VSP_055651
http://togogenome.org/gene/9606:TBXT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15178                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In NTD; unknown pathological significance.|||In SAVA; reduced DNA binding activity; increased cell growth; altered expression of genes involved in ossification and notochord maintenance.|||In isoform 2.|||Polar residues|||T-box|||T-box transcription factor T                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184414|||http://purl.uniprot.org/annotation/VAR_020250|||http://purl.uniprot.org/annotation/VAR_021982|||http://purl.uniprot.org/annotation/VAR_024656|||http://purl.uniprot.org/annotation/VAR_032457|||http://purl.uniprot.org/annotation/VAR_032458|||http://purl.uniprot.org/annotation/VAR_063239|||http://purl.uniprot.org/annotation/VAR_071251|||http://purl.uniprot.org/annotation/VAR_082154|||http://purl.uniprot.org/annotation/VSP_044795
http://togogenome.org/gene/9606:DNAJC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IAH1|||http://purl.uniprot.org/uniprot/Q9UKB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||DnaJ homolog subfamily C member 12|||In HPANBH4; decreased protein levels in patient cells.|||In isoform B.|||J|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071066|||http://purl.uniprot.org/annotation/VAR_048913|||http://purl.uniprot.org/annotation/VAR_048914|||http://purl.uniprot.org/annotation/VAR_078797|||http://purl.uniprot.org/annotation/VSP_001295|||http://purl.uniprot.org/annotation/VSP_001296
http://togogenome.org/gene/9606:OR4N2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVT2|||http://purl.uniprot.org/uniprot/Q8NGD1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150563|||http://purl.uniprot.org/annotation/VAR_034207|||http://purl.uniprot.org/annotation/VAR_048032|||http://purl.uniprot.org/annotation/VAR_048033
http://togogenome.org/gene/9606:OR2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV98|||http://purl.uniprot.org/uniprot/Q13607                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150469|||http://purl.uniprot.org/annotation/VAR_053136|||http://purl.uniprot.org/annotation/VAR_053137
http://togogenome.org/gene/9606:NT5C1B-RDH14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P26                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytosolic 5'-nucleotidase 1B|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144796|||http://purl.uniprot.org/annotation/VSP_010201|||http://purl.uniprot.org/annotation/VSP_010202|||http://purl.uniprot.org/annotation/VSP_010203
http://togogenome.org/gene/9606:TCL1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95988                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  T-cell leukemia/lymphoma protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184490|||http://purl.uniprot.org/annotation/VAR_020467
http://togogenome.org/gene/9606:MANSC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHS7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||MANSC|||MANSC domain-containing protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349176
http://togogenome.org/gene/9606:RFPL4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWI9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||RING-type|||Ret finger protein-like 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274600|||http://purl.uniprot.org/annotation/VAR_044525
http://togogenome.org/gene/9606:ASIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78348                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acid-sensing ion channel 1|||Complete loss in the shift of pH for both activation and desensitization by the spider venom psalmotoxin-1.|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||Important for channel desensitizing|||Important for channel gating|||Important for interaction with the spider venom psalmotoxin-1|||In isoform 1.|||In isoform 3.|||Key residue for defining the pH sensitivity of ASIC1 (isoform 1)|||Large decrease in response to pH 6.5 solutions.|||Loss of phosphorylation.|||N-linked (GlcNAc...) asparagine|||No effect on phosphorylation.|||Phosphoserine|||Phosphoserine; by PKA|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181294|||http://purl.uniprot.org/annotation/VSP_015596|||http://purl.uniprot.org/annotation/VSP_045298
http://togogenome.org/gene/9606:KRTAP5-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75690                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184106|||http://purl.uniprot.org/annotation/VAR_062156
http://togogenome.org/gene/9606:OR10K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV65|||http://purl.uniprot.org/uniprot/Q6IF99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150712|||http://purl.uniprot.org/annotation/VAR_053283
http://togogenome.org/gene/9606:GNS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBC5|||http://purl.uniprot.org/uniprot/P15586|||http://purl.uniprot.org/uniprot/Q7Z3X3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||In MPS3D.|||In isoform 2.|||N-acetylglucosamine-6-sulfatase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033413|||http://purl.uniprot.org/annotation/VAR_064070|||http://purl.uniprot.org/annotation/VAR_064071|||http://purl.uniprot.org/annotation/VAR_064072|||http://purl.uniprot.org/annotation/VAR_064073|||http://purl.uniprot.org/annotation/VSP_056486
http://togogenome.org/gene/9606:CRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50238                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine-rich protein 1|||LIM zinc-binding|||N6-acetyllysine|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075707
http://togogenome.org/gene/9606:TRIM27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8R9|||http://purl.uniprot.org/uniprot/P14373                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity; when associated with A-16.|||Abolished E3 ubiquitin-protein ligase activity; when associated with A-31.|||B box-type|||B30.2/SPRY|||Breakpoint for translocation to form the TRIM27/RET oncogene|||In isoform Beta.|||RING-type|||Zinc finger protein RFP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056240|||http://purl.uniprot.org/annotation/VSP_010896|||http://purl.uniprot.org/annotation/VSP_010897
http://togogenome.org/gene/9606:AKTIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8T0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AKT-interacting protein|||Disordered|||Impairs interaction with FHIP1B, HOOK1, HOOK2 and HOOK3.|||In isoform 2.|||Phosphoserine|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082609|||http://purl.uniprot.org/annotation/VSP_037631
http://togogenome.org/gene/9606:SERPINB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LPD5|||http://purl.uniprot.org/uniprot/A9UKE9|||http://purl.uniprot.org/uniprot/B4DKT7|||http://purl.uniprot.org/uniprot/F5GYW9|||http://purl.uniprot.org/uniprot/Q96P15                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  In allele B and allele C.|||In allele B and allele D.|||In allele D.|||In allele D; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3.|||RCL|||Reactive bond|||Serpin|||Serpin B11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094117|||http://purl.uniprot.org/annotation/VAR_012472|||http://purl.uniprot.org/annotation/VAR_012473|||http://purl.uniprot.org/annotation/VAR_057177|||http://purl.uniprot.org/annotation/VAR_060331|||http://purl.uniprot.org/annotation/VAR_060332|||http://purl.uniprot.org/annotation/VAR_060333|||http://purl.uniprot.org/annotation/VAR_060334|||http://purl.uniprot.org/annotation/VAR_064572|||http://purl.uniprot.org/annotation/VSP_040670|||http://purl.uniprot.org/annotation/VSP_040671
http://togogenome.org/gene/9606:TCTE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JU00                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein regulatory complex subunit 5|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326525|||http://purl.uniprot.org/annotation/VAR_040073|||http://purl.uniprot.org/annotation/VAR_040074|||http://purl.uniprot.org/annotation/VAR_040075
http://togogenome.org/gene/9606:CDH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULB4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-9|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003779|||http://purl.uniprot.org/annotation/PRO_0000003780|||http://purl.uniprot.org/annotation/VAR_029799|||http://purl.uniprot.org/annotation/VAR_029800
http://togogenome.org/gene/9606:SLC39A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTL8|||http://purl.uniprot.org/uniprot/Q9NY26                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect membrane localization. Decreases zinc uptake.|||Does not affect membrane localization; when associated with A-158. Decreases zinc uptake; when associated with A-158.|||Does not affect membrane localization; when associated with A-160. Decreases zinc uptake; when associated with A-160.|||Extracellular|||Helical|||In isoform 2.|||Zinc transporter ZIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068763|||http://purl.uniprot.org/annotation/VSP_056522
http://togogenome.org/gene/9606:CENPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49450                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CATD|||Disordered|||Histone H3-like centromeric protein A|||Impaired mitotic chromosome congression and chromosome segregation; when associated with A-17.|||Impaired mitotic chromosome congression and chromosome segregation; when associated with A-19.|||Impairs interaction with HJURP, association with chromatin and localization at centromeres.|||Impairs retention at centromeres, but not targeting to centromeres.|||Important for flexibility of DNA ends that protrude from nucleosomes|||In isoform 2.|||Induces a delay at the terminal stage of cytokinesis and chromosome misalignment during mitosis due to a defect in kinetochore attachment to microtubules.|||N,N,N-trimethylglycine|||No effect on interaction with HJURP. Impairs localization at centromeres.|||No effect on location at centromeres. Abolishes location at centromeres; when associated with G-104.|||Phosphoserine|||Phosphoserine; by AURKA and AURKB|||Reduces location at centromeres. Abolishes location at centromeres; when associated with C-112.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221373|||http://purl.uniprot.org/annotation/VSP_020430
http://togogenome.org/gene/9606:HSD17B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37059                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase type 2|||Helical; Signal-anchor for type II membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054570|||http://purl.uniprot.org/annotation/VAR_018852
http://togogenome.org/gene/9606:DOHH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU89                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Decreased iron-binding. Loss of iron-binding; when associated with L-86.|||Deoxyhypusine hydroxylase|||HEAT-like PBS-type 1|||HEAT-like PBS-type 2|||HEAT-like PBS-type 3|||HEAT-like PBS-type 4|||HEAT-like PBS-type 5|||In NEDMVIC.|||In NEDMVIC; unknown pathological significance.|||Loss of deoxyhypusine monooxygenase activity. Loss of iron-binding.|||Loss of deoxyhypusine monooxygenase activity. No effect on iron-binding.|||Loss of iron-binding.|||N-acetylmethionine|||No effect on iron-binding. Loss of iron-binding; when associated with L-237.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248575|||http://purl.uniprot.org/annotation/VAR_087785|||http://purl.uniprot.org/annotation/VAR_087786|||http://purl.uniprot.org/annotation/VAR_087787|||http://purl.uniprot.org/annotation/VAR_087788|||http://purl.uniprot.org/annotation/VAR_087789
http://togogenome.org/gene/9606:OXNAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JLB7|||http://purl.uniprot.org/uniprot/Q96HP4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  FAD-binding FR-type|||Oxidoreductase NAD-binding domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299571|||http://purl.uniprot.org/annotation/VAR_034855|||http://purl.uniprot.org/annotation/VAR_034856|||http://purl.uniprot.org/annotation/VAR_034857
http://togogenome.org/gene/9606:FHL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13643|||http://purl.uniprot.org/uniprot/Q96C98                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Four and a half LIM domains protein 3|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||N-acetylserine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075740
http://togogenome.org/gene/9606:RPRD1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CID|||Complete loss of binding to POLR2ACTD in vivo.|||Disordered|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Regulation of nuclear pre-mRNA domain-containing protein 1B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079441
http://togogenome.org/gene/9606:DPRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFQ7                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Divergent paired-related homeobox|||Homeobox                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311326
http://togogenome.org/gene/9606:VPS33B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z577|||http://purl.uniprot.org/uniprot/Q9H267                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disrupts interaction with VIPAS39.|||Disrupts interaction with VIPAS39; no effect on interaction with STX7; impairs localization to VIPAS39-containing endosomal compartment.|||In ARCS1.|||In ARCS1; effect on interaction with VIPAS39 is reported conflictingly but disrupts colocalization with VIPAS39 at cytoplasmic organelle; impairs localization to VIPAS39-containing endosomal compartment; and induces fragmentation of the VIPAS39-containing endosomal compartment; no effect on interaction with STX7 and association with the HOPS complex.|||In ARCS1; no effect on interaction with VIPAS39; impairs localization to VIPAS39-containing endosomal compartment.|||In KDIDAR; disrupts vesicular trafficking of LH3 to intracellular collagen; does not affect interaction with VIPAS39; decreased interaction with RAB25 and RAB11A.|||In PFIC12; disrupts colocalization with VIPAS39 at cytoplasmic organelle; decreased protein expression.|||In isoform 2.|||N-acetylalanine|||No effect on interaction with VIPAS39 and STX7; impairs localization to VIPAS39-containing endosomal compartment.|||No effect on interaction with VIPAS39; no effect on interaction with STX7 and association with the HOPS complex; impairs localization to VIPAS39-containing endosomal compartment.|||Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-382 and E-511.|||Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-382 and E-517.|||Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-133; E-511 and E-517.|||Reduces phosphorylation activity, but does not impair phagolysosomal fusion in M.tuberculosis-infected macrophages; when associated with E-382; E-511 and E-517.|||Removed|||Vacuolar protein sorting-associated protein 33B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206305|||http://purl.uniprot.org/annotation/VAR_013828|||http://purl.uniprot.org/annotation/VAR_018983|||http://purl.uniprot.org/annotation/VAR_057330|||http://purl.uniprot.org/annotation/VAR_057901|||http://purl.uniprot.org/annotation/VAR_087658|||http://purl.uniprot.org/annotation/VAR_087659|||http://purl.uniprot.org/annotation/VAR_087660|||http://purl.uniprot.org/annotation/VSP_056567
http://togogenome.org/gene/9606:BZW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6E2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Reduced interaction with EIF2S2.|||Reduced interaction with EIF3C.|||W2|||eIF5-mimic protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254618|||http://purl.uniprot.org/annotation/VAR_033642|||http://purl.uniprot.org/annotation/VSP_055568|||http://purl.uniprot.org/annotation/VSP_055569
http://togogenome.org/gene/9606:VPS25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRG1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to CHMP6.|||Vacuolar protein-sorting-associated protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215216|||http://purl.uniprot.org/annotation/VAR_048940
http://togogenome.org/gene/9606:BGLAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02818                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  4-carboxyglutamate|||4-carboxyglutamate; partial|||Gla|||Not hydroxylated|||Osteocalcin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011086|||http://purl.uniprot.org/annotation/PRO_0000011087|||http://purl.uniprot.org/annotation/VAR_038743
http://togogenome.org/gene/9606:CDH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLF0|||http://purl.uniprot.org/uniprot/P22223                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-3|||Cytoplasmic|||Extracellular|||Helical|||In EEMS.|||In HJMD.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003745|||http://purl.uniprot.org/annotation/PRO_0000003746|||http://purl.uniprot.org/annotation/VAR_015422|||http://purl.uniprot.org/annotation/VAR_031929|||http://purl.uniprot.org/annotation/VAR_031930|||http://purl.uniprot.org/annotation/VAR_031931|||http://purl.uniprot.org/annotation/VAR_033010|||http://purl.uniprot.org/annotation/VSP_024820
http://togogenome.org/gene/9606:MOSPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75425                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MSP|||Motile sperm domain-containing protein 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213465|||http://purl.uniprot.org/annotation/VSP_014053|||http://purl.uniprot.org/annotation/VSP_014054|||http://purl.uniprot.org/annotation/VSP_014055|||http://purl.uniprot.org/annotation/VSP_044522
http://togogenome.org/gene/9606:FXYD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58549                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FXYD domain-containing ion transport regulator 7|||Helical|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148190
http://togogenome.org/gene/9606:TEX50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTY4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Testis-expressed protein 50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5008408626
http://togogenome.org/gene/9606:PLXNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75051                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-A2|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232747|||http://purl.uniprot.org/annotation/VAR_056722|||http://purl.uniprot.org/annotation/VAR_058201|||http://purl.uniprot.org/annotation/VAR_059554|||http://purl.uniprot.org/annotation/VAR_059555|||http://purl.uniprot.org/annotation/VAR_059556|||http://purl.uniprot.org/annotation/VAR_059557|||http://purl.uniprot.org/annotation/VSP_017967|||http://purl.uniprot.org/annotation/VSP_017968|||http://purl.uniprot.org/annotation/VSP_017969
http://togogenome.org/gene/9606:ZNF705B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CI00                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||KRAB|||Putative zinc finger protein 705B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000399466
http://togogenome.org/gene/9606:CBR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75828                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carbonyl reductase [NADPH] 3|||Decreased carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone and isatin.|||Increased carbonyl reductase (NADPH) activity; exhibits a 2-fold higher Vmax with menadione; higher Vmax with NADP(H); does not affect Km for menadione.|||Modest increase in carbonyl reductase (NADPH) activity toward 1,2-naphthoquinone.|||N-acetylserine|||Phosphoserine|||Proton acceptor|||Removed|||Significant decreased of the Km value for isatin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054608|||http://purl.uniprot.org/annotation/VAR_033868|||http://purl.uniprot.org/annotation/VAR_033869|||http://purl.uniprot.org/annotation/VAR_033870|||http://purl.uniprot.org/annotation/VAR_033871|||http://purl.uniprot.org/annotation/VAR_033872|||http://purl.uniprot.org/annotation/VAR_033873
http://togogenome.org/gene/9606:TAS2R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q502V6|||http://purl.uniprot.org/uniprot/Q9NYW7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082188|||http://purl.uniprot.org/annotation/VAR_020198|||http://purl.uniprot.org/annotation/VAR_020199|||http://purl.uniprot.org/annotation/VAR_053340
http://togogenome.org/gene/9606:RAB40A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXH6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Ras-related protein Rab-40A|||Removed in mature form|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121257|||http://purl.uniprot.org/annotation/PRO_0000370830|||http://purl.uniprot.org/annotation/VAR_034435
http://togogenome.org/gene/9606:DLX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07687|||http://purl.uniprot.org/uniprot/Q53QU7|||http://purl.uniprot.org/uniprot/X5D7D8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DLX-2|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049023|||http://purl.uniprot.org/annotation/VSP_054287|||http://purl.uniprot.org/annotation/VSP_054288
http://togogenome.org/gene/9606:MRPL27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0M9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein bL27m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181229|||http://purl.uniprot.org/annotation/VAR_052023
http://togogenome.org/gene/9606:LYPD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWN5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GPI-anchor amidated alanine|||In isoform 2.|||Ly6/PLAUR domain-containing protein 5|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226763|||http://purl.uniprot.org/annotation/PRO_0000226764|||http://purl.uniprot.org/annotation/VAR_052704|||http://purl.uniprot.org/annotation/VAR_059885|||http://purl.uniprot.org/annotation/VAR_059886|||http://purl.uniprot.org/annotation/VSP_017447
http://togogenome.org/gene/9606:GIMAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7X0|||http://purl.uniprot.org/uniprot/Q9NUV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AIG1-type G|||Disordered|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 4|||IQ|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190987|||http://purl.uniprot.org/annotation/VAR_017306
http://togogenome.org/gene/9606:APEH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13798                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acylamino-acid-releasing enzyme|||Charge relay system|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122430|||http://purl.uniprot.org/annotation/VAR_051580
http://togogenome.org/gene/9606:ITIH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06033                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Aspartate 1-(chondroitin 4-sulfate)-ester|||In isoform 2.|||Inter-alpha-trypsin inhibitor heavy chain H3|||N-linked (GlcNAc...) asparagine|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016529|||http://purl.uniprot.org/annotation/PRO_0000016530|||http://purl.uniprot.org/annotation/PRO_0000016531|||http://purl.uniprot.org/annotation/VAR_049647|||http://purl.uniprot.org/annotation/VAR_049648|||http://purl.uniprot.org/annotation/VAR_049649|||http://purl.uniprot.org/annotation/VAR_049650|||http://purl.uniprot.org/annotation/VAR_049651|||http://purl.uniprot.org/annotation/VAR_061275|||http://purl.uniprot.org/annotation/VSP_029842
http://togogenome.org/gene/9606:KIRREL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN67|||http://purl.uniprot.org/uniprot/Q96J84                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In NPHS23; decreased localization to cell membrane due to intracellular retention; affects integrity of podocyte cell-cell junctions and leads to altered cellular permeability.|||In NPHS23; unknown pathological significance; affects integrity of podocyte cell-cell junctions and leads to altered cellular permeability.|||In isoform 2.|||In isoform 3.|||Kin of IRRE-like protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by FYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015093|||http://purl.uniprot.org/annotation/PRO_5014567681|||http://purl.uniprot.org/annotation/VAR_059428|||http://purl.uniprot.org/annotation/VAR_085245|||http://purl.uniprot.org/annotation/VAR_085246|||http://purl.uniprot.org/annotation/VSP_011732|||http://purl.uniprot.org/annotation/VSP_011733
http://togogenome.org/gene/9606:HNRNPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52597                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding; when associated with A-120.|||Decreases affinity for RNA oligonucleotide 100-fold.|||Drastically effects folding of RRM2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein F|||Heterogeneous nuclear ribonucleoprotein F, N-terminally processed|||Interaction with RNA|||Little disruption of binding RNA.|||Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding; when associated with A-180.|||Loss of RNA-binding.|||Minimal effect on affinity for RNA oligonucleotide.|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F, N-terminally processed|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein F; alternate|||N6-acetyllysine; alternate|||No effect on affinity for RNA oligonucleotide.|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||RRM 3|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081852|||http://purl.uniprot.org/annotation/PRO_0000367114|||http://purl.uniprot.org/annotation/VAR_027999
http://togogenome.org/gene/9606:DMTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMJ8|||http://purl.uniprot.org/uniprot/Q9Y222                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-D-binding Myb-like transcription factor 1|||Disordered|||H-T-H motif|||HTH myb-type|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Interaction with CCND1, CCND2 and CCND3|||Interaction with CCND2|||Myb-like 1|||Myb-like 2|||Required for DNA-binding|||Required for transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323729|||http://purl.uniprot.org/annotation/VAR_039577|||http://purl.uniprot.org/annotation/VSP_032089|||http://purl.uniprot.org/annotation/VSP_032090|||http://purl.uniprot.org/annotation/VSP_032091|||http://purl.uniprot.org/annotation/VSP_032092|||http://purl.uniprot.org/annotation/VSP_032093|||http://purl.uniprot.org/annotation/VSP_041063
http://togogenome.org/gene/9606:KCNV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDN2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In RCD3B.|||In RCD3B; loss of interaction with KCNB1.|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily V member 2|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054094|||http://purl.uniprot.org/annotation/VAR_027632|||http://purl.uniprot.org/annotation/VAR_027633|||http://purl.uniprot.org/annotation/VAR_027634|||http://purl.uniprot.org/annotation/VAR_027635|||http://purl.uniprot.org/annotation/VAR_027636|||http://purl.uniprot.org/annotation/VAR_027637|||http://purl.uniprot.org/annotation/VAR_027638|||http://purl.uniprot.org/annotation/VAR_087564
http://togogenome.org/gene/9606:OR4C15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2C9F2M4|||http://purl.uniprot.org/uniprot/Q8NGM1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150535
http://togogenome.org/gene/9606:KDELR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43731                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||ER lumen protein-retaining receptor 3|||Helical|||Important for recycling of cargo proteins with the sequence motif K-D-E-L from the Golgi to the endoplasmic reticulum|||In isoform 2.|||Interaction with the K-D-E-L motif on target proteins|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194158|||http://purl.uniprot.org/annotation/VAR_014506|||http://purl.uniprot.org/annotation/VSP_022856
http://togogenome.org/gene/9606:FABP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7DVW5|||http://purl.uniprot.org/uniprot/Q01469                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein 5|||Loss of ligand-induced nuclear import; when associated with A-24 and A-33.|||Loss of ligand-induced nuclear import; when associated with A-24 and A-34.|||Loss of ligand-induced nuclear import; when associated with A-33 and A-34.|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067377
http://togogenome.org/gene/9606:PLOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00469                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fe2OG dioxygenase|||Found in a patient with congenital hydrocephalus; unknown pathological significance.|||In BRKS2.|||In BRKS2; phenotype characterized by mild to severe osteogenesis imperfecta with or without postnatal contractures.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine|||Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024683|||http://purl.uniprot.org/annotation/VAR_022164|||http://purl.uniprot.org/annotation/VAR_022165|||http://purl.uniprot.org/annotation/VAR_022166|||http://purl.uniprot.org/annotation/VAR_069531|||http://purl.uniprot.org/annotation/VAR_083432|||http://purl.uniprot.org/annotation/VAR_083433|||http://purl.uniprot.org/annotation/VSP_013467|||http://purl.uniprot.org/annotation/VSP_057221|||http://purl.uniprot.org/annotation/VSP_057222
http://togogenome.org/gene/9606:UBE2J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y385                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of stress-dependent phosphorylation. Loss of cell recovery for ER stress.|||Cytoplasmic|||Disordered|||Glycyl thioester intermediate|||Helical; Anchor for type IV membrane protein|||Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER.|||Lumenal|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Polar residues|||UBC core|||Ubiquitin-conjugating enzyme E2 J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082594|||http://purl.uniprot.org/annotation/VAR_019689|||http://purl.uniprot.org/annotation/VAR_019690
http://togogenome.org/gene/9606:WNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56703                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Proto-oncogene Wnt-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041416
http://togogenome.org/gene/9606:USP40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVE5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080670|||http://purl.uniprot.org/annotation/VAR_017123|||http://purl.uniprot.org/annotation/VAR_017124|||http://purl.uniprot.org/annotation/VAR_059753|||http://purl.uniprot.org/annotation/VSP_008595|||http://purl.uniprot.org/annotation/VSP_008596|||http://purl.uniprot.org/annotation/VSP_012819|||http://purl.uniprot.org/annotation/VSP_040938
http://togogenome.org/gene/9606:TTC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YS0|||http://purl.uniprot.org/uniprot/Q86TA5|||http://purl.uniprot.org/uniprot/Q8TEM7|||http://purl.uniprot.org/uniprot/Q96N46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||S1 motif|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide repeat protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106399|||http://purl.uniprot.org/annotation/VSP_013480|||http://purl.uniprot.org/annotation/VSP_013481|||http://purl.uniprot.org/annotation/VSP_047107
http://togogenome.org/gene/9606:CD300H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K2S4Q6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein CD300H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5014029141|||http://purl.uniprot.org/annotation/VSP_059910|||http://purl.uniprot.org/annotation/VSP_059911
http://togogenome.org/gene/9606:STON1-GTF2A1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYG5|||http://purl.uniprot.org/uniprot/Q3MIM1|||http://purl.uniprot.org/uniprot/Q53S48|||http://purl.uniprot.org/uniprot/Q9Y6Q2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||MHD|||Polar residues|||SHD|||Stonin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185736|||http://purl.uniprot.org/annotation/VAR_020183|||http://purl.uniprot.org/annotation/VAR_020184|||http://purl.uniprot.org/annotation/VAR_020185|||http://purl.uniprot.org/annotation/VAR_052156|||http://purl.uniprot.org/annotation/VSP_045845|||http://purl.uniprot.org/annotation/VSP_045846
http://togogenome.org/gene/9606:NDUFAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14561                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl carrier protein, mitochondrial|||Carrier|||Mitochondrion|||N6-acetyllysine|||O-(pantetheine 4'-phosphoryl)serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000561
http://togogenome.org/gene/9606:IFT81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYA0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes tubulin-binding and impaired ciliogenesis; when associated with 113-E-E-114.|||Abolishes tubulin-binding and impaired ciliogenesis; when associated with 73-E--E-75.|||CH (calponin-homology)-like region|||In SRTD19.|||In SRTD19; unknown pathological significance.|||In isoform 2.|||In isoform CDV-1.|||Intraflagellar transport protein 81 homolog|||N-acetylserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020916|||http://purl.uniprot.org/annotation/VAR_080485|||http://purl.uniprot.org/annotation/VAR_080487|||http://purl.uniprot.org/annotation/VAR_080488|||http://purl.uniprot.org/annotation/VAR_080793|||http://purl.uniprot.org/annotation/VSP_018784|||http://purl.uniprot.org/annotation/VSP_050695|||http://purl.uniprot.org/annotation/VSP_050696
http://togogenome.org/gene/9606:MCMDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXX4|||http://purl.uniprot.org/uniprot/Q4G0Z9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||MCM|||MCM AAA-lid|||Minichromosome maintenance domain-containing protein 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255258|||http://purl.uniprot.org/annotation/VAR_028861|||http://purl.uniprot.org/annotation/VAR_028862|||http://purl.uniprot.org/annotation/VAR_028863|||http://purl.uniprot.org/annotation/VSP_038998|||http://purl.uniprot.org/annotation/VSP_038999|||http://purl.uniprot.org/annotation/VSP_039000|||http://purl.uniprot.org/annotation/VSP_039001
http://togogenome.org/gene/9606:TBC1D3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPX1|||http://purl.uniprot.org/uniprot/Q8IZP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3|||TBC1 domain family member 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208025|||http://purl.uniprot.org/annotation/PRO_0000300265|||http://purl.uniprot.org/annotation/VAR_063088|||http://purl.uniprot.org/annotation/VSP_056829|||http://purl.uniprot.org/annotation/VSP_056830
http://togogenome.org/gene/9606:RBPJL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QPV1|||http://purl.uniprot.org/uniprot/Q9UBG7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Beta-trefoil DNA-binding|||DNA-binding|||Disordered|||IPT/TIG|||In isoform 2.|||RBP-J/Cbf11/Cbf12 DNA binding|||Recombining binding protein suppressor of hairless-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208570|||http://purl.uniprot.org/annotation/VSP_039150
http://togogenome.org/gene/9606:COPS7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBW8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  COP9 signalosome complex subunit 7a|||Disordered|||N-acetylserine|||PCI|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120996
http://togogenome.org/gene/9606:NKAIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNZ0|||http://purl.uniprot.org/uniprot/Q5VXU1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Breakpoint for interstitial deletion to form SUSP1-NKAIN2|||Helical|||In isoform 2.|||In isoform 3.|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265088|||http://purl.uniprot.org/annotation/VSP_021902|||http://purl.uniprot.org/annotation/VSP_029298
http://togogenome.org/gene/9606:TPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17752                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ACT|||In isoform 2.|||Phosphoserine; by PKA|||Tryptophan 5-hydroxylase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205568|||http://purl.uniprot.org/annotation/VSP_000546
http://togogenome.org/gene/9606:AGBL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEM8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic carboxypeptidase 3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283751|||http://purl.uniprot.org/annotation/VAR_031573|||http://purl.uniprot.org/annotation/VAR_031574|||http://purl.uniprot.org/annotation/VAR_031575|||http://purl.uniprot.org/annotation/VSP_024370|||http://purl.uniprot.org/annotation/VSP_024371|||http://purl.uniprot.org/annotation/VSP_024372|||http://purl.uniprot.org/annotation/VSP_024373|||http://purl.uniprot.org/annotation/VSP_040423
http://togogenome.org/gene/9606:SEC24C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53992                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Gelsolin-like|||In isoform 2.|||Loss of packaging into COPII-coated vesicles of the IxM motif-containing cargos GOSR2 and STX5.|||Phosphothreonine|||Polar residues|||Pro residues|||Protein transport protein Sec24C|||Zinc finger-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205156|||http://purl.uniprot.org/annotation/VAR_057174|||http://purl.uniprot.org/annotation/VAR_058690|||http://purl.uniprot.org/annotation/VSP_056516
http://togogenome.org/gene/9606:RPS4X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R491|||http://purl.uniprot.org/uniprot/P62701                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||RNA-binding S4|||Removed|||S4 RNA-binding|||Small ribosomal subunit protein eS4, X isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130805
http://togogenome.org/gene/9606:BAHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAH|||Basic and acidic residues|||Basic residues|||Bromo adjacent homology domain-containing 1 protein|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287918|||http://purl.uniprot.org/annotation/VAR_032359|||http://purl.uniprot.org/annotation/VAR_032360|||http://purl.uniprot.org/annotation/VAR_032361|||http://purl.uniprot.org/annotation/VSP_025623|||http://purl.uniprot.org/annotation/VSP_025624
http://togogenome.org/gene/9606:LAIR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ISS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Ig-like C2-type|||In isoform 2.|||Leukocyte-associated immunoglobulin-like receptor 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250685|||http://purl.uniprot.org/annotation/VAR_049882|||http://purl.uniprot.org/annotation/VAR_049883|||http://purl.uniprot.org/annotation/VAR_049884|||http://purl.uniprot.org/annotation/VSP_020720
http://togogenome.org/gene/9606:FGF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09038                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to integrin ITGAV:ITGB3 and suppresses FGF2 signaling with loss of ERK1/2 activation and reduced ability to induce DNA synthesis, cell migration and angiogenesis. Acts as a potent antagonist of FGF2-mediated angiogenesis.|||Basic and acidic residues|||Cell attachment site; atypical|||Disordered|||Fibroblast growth factor 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Heparin-binding|||Important for interaction with integrin|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No effect on integrin binding.|||Omega-N-methylarginine; alternate|||Or 93, or 124, or 125, or 131, or 161|||Phosphotyrosine; by TEC|||Reduces binding to integrin ITGAV:ITGB3 and suppresses FGF2 signaling with reduced ERK1/2 activation and reduced ability to induce DNA synthesis, cell migration and angiogenesis. Acts as a potent antagonist of FGF2-mediated angiogenesis.|||Symmetric dimethylarginine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008932|||http://purl.uniprot.org/annotation/PRO_0000008933|||http://purl.uniprot.org/annotation/VSP_037383|||http://purl.uniprot.org/annotation/VSP_037384|||http://purl.uniprot.org/annotation/VSP_037385|||http://purl.uniprot.org/annotation/VSP_038236|||http://purl.uniprot.org/annotation/VSP_038237
http://togogenome.org/gene/9606:IFT20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Splice Variant                                                                                  ^@                                                                                  IFT57-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Intraflagellar transport protein 20 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249303|||http://purl.uniprot.org/annotation/VSP_020390|||http://purl.uniprot.org/annotation/VSP_020391|||http://purl.uniprot.org/annotation/VSP_046026
http://togogenome.org/gene/9606:SEMA5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13591|||http://purl.uniprot.org/uniprot/X5DR95                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with autism spectrum disorder.|||Sema|||Semaphorin-5A|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032335|||http://purl.uniprot.org/annotation/PRO_5004954996|||http://purl.uniprot.org/annotation/VAR_030294|||http://purl.uniprot.org/annotation/VAR_030295|||http://purl.uniprot.org/annotation/VAR_078706
http://togogenome.org/gene/9606:PCDH18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYG2|||http://purl.uniprot.org/uniprot/Q9HCL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with DAB1|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin-18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004002|||http://purl.uniprot.org/annotation/PRO_5004257363|||http://purl.uniprot.org/annotation/VSP_035648
http://togogenome.org/gene/9606:KRTAP21-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI58                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Keratin-associated protein 21-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223912|||http://purl.uniprot.org/annotation/VAR_036563
http://togogenome.org/gene/9606:PODNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3M0|||http://purl.uniprot.org/uniprot/Q6PEZ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||Podocan-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311187|||http://purl.uniprot.org/annotation/VAR_037151|||http://purl.uniprot.org/annotation/VSP_043973|||http://purl.uniprot.org/annotation/VSP_043974
http://togogenome.org/gene/9606:DNAJB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWX2|||http://purl.uniprot.org/uniprot/Q8TBM8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with HSPA8/Hsc70.|||Cytoplasmic|||Disordered|||DnaJ homolog subfamily B member 14|||Helical|||In isoform 2.|||J|||Lumenal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281478|||http://purl.uniprot.org/annotation/VSP_024006|||http://purl.uniprot.org/annotation/VSP_024007
http://togogenome.org/gene/9606:SMIM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KF7|||http://purl.uniprot.org/uniprot/V9GYF9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Small integral membrane protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089550
http://togogenome.org/gene/9606:PPP1CA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJS9|||http://purl.uniprot.org/uniprot/P62136                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor|||Removed|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase PP1-alpha catalytic subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058774|||http://purl.uniprot.org/annotation/VSP_043377|||http://purl.uniprot.org/annotation/VSP_046754
http://togogenome.org/gene/9606:RAB7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51149                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RILP and localization to late endosomal/lysosomal compartments.|||Abolishes interaction with RILP and reduces its localization to late endosomal/lysosomal compartments.|||Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. No loss of interaction with CLN5. No loss of interaction with PRPH. Reduced interaction with VPS13A. Inhibits SARS-CoV-2 infection.|||Cysteine methyl ester|||Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-182.|||Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RILP and localization to late endosomal/lysosomal compartments; when associated with A-183.|||Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. No loss of interaction with CLN5 and VPS13A. Increases interaction with PRPH. Inhibits SARS-CoV-2 infection.|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CMT2B; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH.|||In CMT2B; increases GTP hydrolysis; decreases affinity for GTP and GDP; does not affect interaction with NTRK1; results in higher levels of NTRK1 and MAPK1/MAPK3 phosphorylation after NGF stimulation consistent with enhanced MAPK signaling; increases interaction with PRPH.|||N-acetylthreonine|||Phosphoserine|||Ras-related protein Rab-7a|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121121|||http://purl.uniprot.org/annotation/VAR_018722|||http://purl.uniprot.org/annotation/VAR_018723|||http://purl.uniprot.org/annotation/VAR_037886|||http://purl.uniprot.org/annotation/VAR_037887|||http://purl.uniprot.org/annotation/VAR_037888
http://togogenome.org/gene/9606:CTU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BSW6|||http://purl.uniprot.org/uniprot/Q2VPK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytoplasmic tRNA 2-thiolation protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylcysteine|||Phosphoserine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289175|||http://purl.uniprot.org/annotation/VAR_032595|||http://purl.uniprot.org/annotation/VAR_032596|||http://purl.uniprot.org/annotation/VAR_032597|||http://purl.uniprot.org/annotation/VAR_062244|||http://purl.uniprot.org/annotation/VSP_025950|||http://purl.uniprot.org/annotation/VSP_039378
http://togogenome.org/gene/9606:UNC119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EN86|||http://purl.uniprot.org/uniprot/Q13432                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GMP phosphodiesterase delta subunit|||Impairs interaction with LCK.|||In IMD13; impairs interaction with LCK; impairs LCK activation; induces LCK mislocalization.|||In isoform B.|||Loss of phosphorylation; when associated with A-37 and A-39.|||Loss of phosphorylation; when associated with A-37 and A-41.|||Loss of phosphorylation; when associated with A-39 and A-41.|||Phosphoserine; by CK2|||Polar residues|||Protein unc-119 homolog A|||Required for centrosome localization|||Required for midbody localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221212|||http://purl.uniprot.org/annotation/VAR_071184|||http://purl.uniprot.org/annotation/VSP_004545
http://togogenome.org/gene/9606:FAM13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94988                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 2.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM13A|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058920|||http://purl.uniprot.org/annotation/VAR_049019|||http://purl.uniprot.org/annotation/VSP_039152|||http://purl.uniprot.org/annotation/VSP_039153|||http://purl.uniprot.org/annotation/VSP_039154|||http://purl.uniprot.org/annotation/VSP_039155|||http://purl.uniprot.org/annotation/VSP_039156|||http://purl.uniprot.org/annotation/VSP_039157|||http://purl.uniprot.org/annotation/VSP_039158
http://togogenome.org/gene/9606:CAPZA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KX2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  F-actin-capping protein subunit alpha-3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208631
http://togogenome.org/gene/9606:UNC93B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1C4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein unc-93 homolog B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190040|||http://purl.uniprot.org/annotation/VAR_059850
http://togogenome.org/gene/9606:TRPM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2W7|||http://purl.uniprot.org/uniprot/W8DTH1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glycosylation.|||Abolishes multimerization and channel activity. Reduces cell surface expression.|||Cytoplasmic|||Epitope; activates specific cytotoxic T lymphocytes|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Ion transport|||N-linked (GlcNAc...) (complex) asparagine|||No effect on glycosylation or ability to form functional channels.|||No effect on glycosylation or channel activity.|||TRPM SLOG|||Transient receptor potential cation channel subfamily M member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215333|||http://purl.uniprot.org/annotation/VAR_052383|||http://purl.uniprot.org/annotation/VAR_052384|||http://purl.uniprot.org/annotation/VAR_052385|||http://purl.uniprot.org/annotation/VAR_052386|||http://purl.uniprot.org/annotation/VAR_052387|||http://purl.uniprot.org/annotation/VAR_059837|||http://purl.uniprot.org/annotation/VSP_012330|||http://purl.uniprot.org/annotation/VSP_012332|||http://purl.uniprot.org/annotation/VSP_012333|||http://purl.uniprot.org/annotation/VSP_053268|||http://purl.uniprot.org/annotation/VSP_054505|||http://purl.uniprot.org/annotation/VSP_054506|||http://purl.uniprot.org/annotation/VSP_054507
http://togogenome.org/gene/9606:NOP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46087                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211818|||http://purl.uniprot.org/annotation/VAR_030938|||http://purl.uniprot.org/annotation/VSP_023494|||http://purl.uniprot.org/annotation/VSP_045308|||http://purl.uniprot.org/annotation/VSP_045309
http://togogenome.org/gene/9606:FBXL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKT7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decrease in binding efficiency with CRY2 and of CRY2 ubiquitination efficiency, loss of binding with CRY1.|||Disordered|||F-box|||F-box/LRR-repeat protein 3|||In IDDSFAS.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Loss of binding with CRY1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119842|||http://purl.uniprot.org/annotation/VAR_082209|||http://purl.uniprot.org/annotation/VAR_082210
http://togogenome.org/gene/9606:ISOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AB3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Isochorismatase domain-containing protein 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268671|||http://purl.uniprot.org/annotation/VSP_022000|||http://purl.uniprot.org/annotation/VSP_038741
http://togogenome.org/gene/9606:SIRPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1W8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C1-type 1|||Ig-like C1-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Signal-regulatory protein gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014957|||http://purl.uniprot.org/annotation/VAR_049936|||http://purl.uniprot.org/annotation/VAR_049937|||http://purl.uniprot.org/annotation/VSP_007027|||http://purl.uniprot.org/annotation/VSP_007028|||http://purl.uniprot.org/annotation/VSP_026960
http://togogenome.org/gene/9606:EAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWJ3|||http://purl.uniprot.org/uniprot/Q96CJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ELL-associated factor 2|||In isoform 2.|||Necessary for interaction with ELL|||Necessary for interaction with TCEA1 and transactivation activity|||Necessary for transactivation activity|||Phosphoserine|||Polar residues|||Transcription elongation factor Eaf N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130337|||http://purl.uniprot.org/annotation/VSP_015310
http://togogenome.org/gene/9606:CD83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX61|||http://purl.uniprot.org/uniprot/Q01151                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD83 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014657|||http://purl.uniprot.org/annotation/VAR_033609
http://togogenome.org/gene/9606:NSMF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7L5|||http://purl.uniprot.org/uniprot/Q6X4W1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In HH9; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in FGFR1.|||In HH9; sporadic case.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||Localizes both in the cytoplasm and the nucleus.|||Localizes predominantly in the cytoplasm.|||N-myristoyl glycine|||NMDA receptor synaptonuclear signaling and neuronal migration factor|||Necessary and sufficient to elicit dendritic processes and synaptic contacts|||Nuclear localization signal|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096778|||http://purl.uniprot.org/annotation/VAR_023003|||http://purl.uniprot.org/annotation/VAR_059699|||http://purl.uniprot.org/annotation/VAR_069967|||http://purl.uniprot.org/annotation/VSP_014759|||http://purl.uniprot.org/annotation/VSP_014760|||http://purl.uniprot.org/annotation/VSP_014761|||http://purl.uniprot.org/annotation/VSP_014762|||http://purl.uniprot.org/annotation/VSP_014763
http://togogenome.org/gene/9606:UPRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRR5|||http://purl.uniprot.org/uniprot/A8KAF9|||http://purl.uniprot.org/uniprot/Q96BW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Uracil phosphoribosyltransferase homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254535|||http://purl.uniprot.org/annotation/VSP_021205|||http://purl.uniprot.org/annotation/VSP_021206|||http://purl.uniprot.org/annotation/VSP_021207|||http://purl.uniprot.org/annotation/VSP_021208|||http://purl.uniprot.org/annotation/VSP_021209
http://togogenome.org/gene/9606:MCUB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWR8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Calcium uniporter regulatory subunit MCUb, mitochondrial|||Helical|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282980|||http://purl.uniprot.org/annotation/VAR_031443|||http://purl.uniprot.org/annotation/VAR_031444|||http://purl.uniprot.org/annotation/VAR_060149
http://togogenome.org/gene/9606:ZDHHC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8X9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Mediates interaction with IRF3 and STING1|||No effect on the regulation of STING1-mediated innate immune response.|||Palmitoyltransferase ZDHHC11|||Polar residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212883|||http://purl.uniprot.org/annotation/VAR_021998|||http://purl.uniprot.org/annotation/VAR_024704|||http://purl.uniprot.org/annotation/VAR_052975|||http://purl.uniprot.org/annotation/VSP_055997|||http://purl.uniprot.org/annotation/VSP_055998|||http://purl.uniprot.org/annotation/VSP_055999
http://togogenome.org/gene/9606:OSBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969R2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Oxysterol-binding protein 2|||PH|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100366|||http://purl.uniprot.org/annotation/VAR_053546|||http://purl.uniprot.org/annotation/VSP_054520|||http://purl.uniprot.org/annotation/VSP_054886|||http://purl.uniprot.org/annotation/VSP_054887|||http://purl.uniprot.org/annotation/VSP_055262|||http://purl.uniprot.org/annotation/VSP_055263|||http://purl.uniprot.org/annotation/VSP_055751|||http://purl.uniprot.org/annotation/VSP_055752
http://togogenome.org/gene/9606:SPINT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49223                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Kunitz-type protease inhibitor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016887|||http://purl.uniprot.org/annotation/VAR_059443
http://togogenome.org/gene/9606:CITED4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RK1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Cbp/p300-interacting transactivator 4|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233309
http://togogenome.org/gene/9606:COX7A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24310|||http://purl.uniprot.org/uniprot/Q6FGI7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7A1, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006149
http://togogenome.org/gene/9606:TSPYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0U9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Testis-specific Y-encoded-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185670|||http://purl.uniprot.org/annotation/VAR_016229|||http://purl.uniprot.org/annotation/VAR_016230|||http://purl.uniprot.org/annotation/VAR_046722
http://togogenome.org/gene/9606:ANKRD66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2M5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 66|||Basic residues|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421258
http://togogenome.org/gene/9606:MINDY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0A6                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Probable ubiquitin carboxyl-terminal hydrolase MINDY-4|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320590|||http://purl.uniprot.org/annotation/VAR_039212|||http://purl.uniprot.org/annotation/VAR_039213|||http://purl.uniprot.org/annotation/VAR_039214|||http://purl.uniprot.org/annotation/VAR_039215|||http://purl.uniprot.org/annotation/VAR_039216|||http://purl.uniprot.org/annotation/VAR_039217|||http://purl.uniprot.org/annotation/VAR_062248
http://togogenome.org/gene/9606:IQCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSY6|||http://purl.uniprot.org/uniprot/B4DIF4|||http://purl.uniprot.org/uniprot/Q86XH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATPase AAA-type core|||Basic residues|||Disordered|||Dynein regulatory complex protein 11|||IQ|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283572|||http://purl.uniprot.org/annotation/VAR_031495|||http://purl.uniprot.org/annotation/VAR_060983|||http://purl.uniprot.org/annotation/VAR_060984|||http://purl.uniprot.org/annotation/VSP_024327|||http://purl.uniprot.org/annotation/VSP_024330|||http://purl.uniprot.org/annotation/VSP_024331|||http://purl.uniprot.org/annotation/VSP_047012
http://togogenome.org/gene/9606:FZD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL33|||http://purl.uniprot.org/uniprot/B4E236|||http://purl.uniprot.org/uniprot/O60353                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-6|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In NDNC1; also found in a patient with neural tube defects; the mutant protein localizes to the lysosomes compared to wild-type.|||In a patient with neural tube defects.|||In isoform 2.|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012994|||http://purl.uniprot.org/annotation/VAR_047440|||http://purl.uniprot.org/annotation/VAR_047441|||http://purl.uniprot.org/annotation/VAR_047442|||http://purl.uniprot.org/annotation/VAR_066398|||http://purl.uniprot.org/annotation/VAR_066963|||http://purl.uniprot.org/annotation/VAR_066964|||http://purl.uniprot.org/annotation/VAR_066965|||http://purl.uniprot.org/annotation/VAR_066966|||http://purl.uniprot.org/annotation/VAR_066967|||http://purl.uniprot.org/annotation/VAR_066968|||http://purl.uniprot.org/annotation/VAR_066969|||http://purl.uniprot.org/annotation/VSP_044291
http://togogenome.org/gene/9606:PSMA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25787                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Proteasome subunit alpha type-2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124077|||http://purl.uniprot.org/annotation/VAR_036278
http://togogenome.org/gene/9606:PMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1K2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polyamine-modulated factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248237|||http://purl.uniprot.org/annotation/VAR_034147|||http://purl.uniprot.org/annotation/VAR_034148|||http://purl.uniprot.org/annotation/VSP_044638|||http://purl.uniprot.org/annotation/VSP_052136|||http://purl.uniprot.org/annotation/VSP_052137|||http://purl.uniprot.org/annotation/VSP_052138|||http://purl.uniprot.org/annotation/VSP_052139|||http://purl.uniprot.org/annotation/VSP_052140
http://togogenome.org/gene/9606:RBM18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H35                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Probable RNA-binding protein 18|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254122
http://togogenome.org/gene/9606:ADAMTS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFZ4|||http://purl.uniprot.org/uniprot/Q9UKP4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 7|||Basic and acidic residues|||Cysteine switch|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Polar residues|||Pro residues|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029176|||http://purl.uniprot.org/annotation/PRO_0000029177|||http://purl.uniprot.org/annotation/VAR_046112|||http://purl.uniprot.org/annotation/VAR_046113|||http://purl.uniprot.org/annotation/VAR_046114|||http://purl.uniprot.org/annotation/VAR_046115|||http://purl.uniprot.org/annotation/VAR_046116
http://togogenome.org/gene/9606:THOC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W42                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In BBIS; localizes to the cytoplasm and not to the nucleus.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||THO complex subunit 6 homolog|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233158|||http://purl.uniprot.org/annotation/VAR_069779|||http://purl.uniprot.org/annotation/VSP_018078|||http://purl.uniprot.org/annotation/VSP_018079
http://togogenome.org/gene/9606:MMP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14780                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  67 kDa matrix metalloproteinase-9|||82 kDa matrix metalloproteinase-9|||Activation peptide|||Basic and acidic residues|||Cleavage; by MMP3|||Cysteine switch|||Disordered|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-II 3|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Loss of activity.|||May be associated with susceptibility to IDD.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028754|||http://purl.uniprot.org/annotation/PRO_0000028755|||http://purl.uniprot.org/annotation/PRO_0000028756|||http://purl.uniprot.org/annotation/PRO_0000028757|||http://purl.uniprot.org/annotation/VAR_013780|||http://purl.uniprot.org/annotation/VAR_013781|||http://purl.uniprot.org/annotation/VAR_013782|||http://purl.uniprot.org/annotation/VAR_014742|||http://purl.uniprot.org/annotation/VAR_020054|||http://purl.uniprot.org/annotation/VAR_024595|||http://purl.uniprot.org/annotation/VAR_025165|||http://purl.uniprot.org/annotation/VAR_025166|||http://purl.uniprot.org/annotation/VAR_037004
http://togogenome.org/gene/9606:RNF182                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6D2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RNF182|||Helical|||In a colorectal cancer sample; somatic mutation.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261620|||http://purl.uniprot.org/annotation/VAR_035959|||http://purl.uniprot.org/annotation/VAR_035960
http://togogenome.org/gene/9606:TMEM207                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWW9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Loss of WWOX-binding.|||Transmembrane protein 207                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317525|||http://purl.uniprot.org/annotation/VAR_051436
http://togogenome.org/gene/9606:DHH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43323                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cholesterol glycine ester|||Cleavage; by autolysis|||Desert hedgehog protein|||Desert hedgehog protein N-product|||Essential for auto-cleavage|||In GDMN; unknown pathological significance.|||In GDMN; unknown pathological significance; Reduces cleavage efficiency in in vitro time course.|||In SRXY7.|||Involved in auto-cleavage|||Involved in cholesterol transfer|||Loss of palmitoylation.|||N-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013244|||http://purl.uniprot.org/annotation/PRO_0000013245|||http://purl.uniprot.org/annotation/VAR_054873|||http://purl.uniprot.org/annotation/VAR_086512|||http://purl.uniprot.org/annotation/VAR_086513
http://togogenome.org/gene/9606:BPHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AI2|||http://purl.uniprot.org/uniprot/Q86W56|||http://purl.uniprot.org/uniprot/Q86WA6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  <0.1% of wild type activity.|||A-domain|||AB hydrolase-1|||Abolished poly(ADP-ribose) glycohydrolase activity.|||Abolishes nuclear targeting; when associated with A-12.|||Abolishes nuclear targeting; when associated with G-13.|||Basic and acidic residues|||Binding of alpha-amino group of substrate|||Catalytic|||Charge relay system|||Complete loss of activity.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect.|||Nuclear localization signal|||Nucleophile|||PIP-box (PCNA interacting peptide)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Poly(ADP-ribose) glycohydrolase|||Reduced poly(ADP-ribose) glycohydrolase activity.|||Reduces hydrolase activity.|||Valacyclovir hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017841|||http://purl.uniprot.org/annotation/PRO_0000066602|||http://purl.uniprot.org/annotation/VSP_009115|||http://purl.uniprot.org/annotation/VSP_011769|||http://purl.uniprot.org/annotation/VSP_011770|||http://purl.uniprot.org/annotation/VSP_044674|||http://purl.uniprot.org/annotation/VSP_044675|||http://purl.uniprot.org/annotation/VSP_044676|||http://purl.uniprot.org/annotation/VSP_044677
http://togogenome.org/gene/9606:SPINK13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9E8LN18|||http://purl.uniprot.org/uniprot/Q1W4C9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serine protease inhibitor Kazal-type 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344510|||http://purl.uniprot.org/annotation/PRO_5038475156|||http://purl.uniprot.org/annotation/VSP_034842
http://togogenome.org/gene/9606:ISM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6H9L7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  AMOP|||Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Isthmin-2|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000072090|||http://purl.uniprot.org/annotation/VAR_035365|||http://purl.uniprot.org/annotation/VAR_035366|||http://purl.uniprot.org/annotation/VSP_028610|||http://purl.uniprot.org/annotation/VSP_028611|||http://purl.uniprot.org/annotation/VSP_028612|||http://purl.uniprot.org/annotation/VSP_029679|||http://purl.uniprot.org/annotation/VSP_029680|||http://purl.uniprot.org/annotation/VSP_029681
http://togogenome.org/gene/9606:TFAP2E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6VUC0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  H-S-H (helix-span-helix), dimerization|||PPxY motif|||Phosphoserine; by PKA|||Transcription factor AP-2-epsilon                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309516
http://togogenome.org/gene/9606:GRAMD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRAM|||GRAM domain-containing protein 2A|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287454
http://togogenome.org/gene/9606:DDR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCQ1|||http://purl.uniprot.org/uniprot/A0A0A0MSX3|||http://purl.uniprot.org/uniprot/Q08345|||http://purl.uniprot.org/uniprot/Q96T61|||http://purl.uniprot.org/uniprot/Q96T62                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PTPN11.|||Confers over 20-fold resistance to the ability of an inhibitor to inhibit autophosphorylation.|||Cytoplasmic|||DS-like domain|||Disordered|||Epithelial discoidin domain-containing receptor 1|||Extracellular|||F5/8 type C|||Helical|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibits collagen-induced phosphorylation.|||Loss of kinase activity. Complete loss of the collagen-independent constitutive activation; when associated with Q-211.|||N-linked (GlcNAc...) asparagine|||PPxY motif|||Phosphorylates in response to collagen, but at lower levels compared to wild-type. No activation in the absence of collagen.|||Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-379.|||Phosphorylates in response to collagen, but at lower levels compared to wild-type. Phosphorylates in response to collagen, but at lower levels compared to wild-type; when associated with A-393.|||Phosphorylates regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation.|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor|||Sustained phosphorylation regardless of collagen presence, collagen addition does not alter significantly the levels of constitutive phosphorylation. Located intracellularly and at the cell surface. Displays a reduced rate of receptor internalization, which is not altered in the presence of collagen. Able to bind collagen as wild-type. Exhibits enhanced collagen-independent receptor dimerization. Complete loss of the collagen-independent constitutive activation; when associated with A-655.|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016742|||http://purl.uniprot.org/annotation/PRO_5004321943|||http://purl.uniprot.org/annotation/PRO_5014214302|||http://purl.uniprot.org/annotation/PRO_5014506438|||http://purl.uniprot.org/annotation/VAR_041492|||http://purl.uniprot.org/annotation/VAR_041493|||http://purl.uniprot.org/annotation/VAR_041494|||http://purl.uniprot.org/annotation/VAR_041495|||http://purl.uniprot.org/annotation/VAR_041496|||http://purl.uniprot.org/annotation/VAR_041497|||http://purl.uniprot.org/annotation/VAR_049716|||http://purl.uniprot.org/annotation/VSP_002953|||http://purl.uniprot.org/annotation/VSP_036916|||http://purl.uniprot.org/annotation/VSP_036917|||http://purl.uniprot.org/annotation/VSP_038057|||http://purl.uniprot.org/annotation/VSP_043582
http://togogenome.org/gene/9606:OR2V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHB1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2V1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312488
http://togogenome.org/gene/9606:CEPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TRF3|||http://purl.uniprot.org/uniprot/Q9Y6K0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity.|||Basic and acidic residues|||Choline/ethanolaminephosphotransferase 1|||Disordered|||Does not affect either the enzyme activity or the diacylglycerol specificity.|||Helical|||Increases basicity of active site His|||Induces a reduction in both cholinephosphotransferase and ethanolaminephosphotransferase activities.|||Induces a reduction in cholinephosphotransferase activity and abolishes ethanolaminephosphotransferase activity.|||Induces a strong reduction in enzyme activity and alters diacylglycerol specificity.|||Induces a strong reduction in enzyme activity without altering diacylglycerol specificity.|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine|||Phosphothreonine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289245
http://togogenome.org/gene/9606:FGD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFF2|||http://purl.uniprot.org/uniprot/B7ZM68|||http://purl.uniprot.org/uniprot/Q6ZNL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 5|||FYVE-type|||In isoform 2.|||PH|||PH 1|||PH 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080950|||http://purl.uniprot.org/annotation/VAR_059799|||http://purl.uniprot.org/annotation/VAR_059800|||http://purl.uniprot.org/annotation/VAR_059801|||http://purl.uniprot.org/annotation/VSP_013088
http://togogenome.org/gene/9606:PPP2R2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2T4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071428|||http://purl.uniprot.org/annotation/VSP_036457|||http://purl.uniprot.org/annotation/VSP_036458|||http://purl.uniprot.org/annotation/VSP_043380
http://togogenome.org/gene/9606:NUAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60285                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with PPP1CB and ability to regulate myosin PP1 activity.|||Abolishes kinase activity and ability to induce senescence.|||Abrogates phosphorylation by PKB/AKT1. Does not affect ability to induce senescence.|||Basic and acidic residues|||Disordered|||GILK motif|||In isoform 2.|||N-acetylmethionine|||NUAK family SNF1-like kinase 1|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex. Abolishes ability to induce senescence.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086453|||http://purl.uniprot.org/annotation/VAR_017246|||http://purl.uniprot.org/annotation/VAR_040963|||http://purl.uniprot.org/annotation/VSP_014236|||http://purl.uniprot.org/annotation/VSP_014237
http://togogenome.org/gene/9606:ZNF785                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8V0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 785                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345630|||http://purl.uniprot.org/annotation/VAR_076389|||http://purl.uniprot.org/annotation/VAR_076390|||http://purl.uniprot.org/annotation/VSP_034965
http://togogenome.org/gene/9606:ARPC4-TTLL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYG9                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PHLDA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology-like domain family A member 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053900
http://togogenome.org/gene/9606:LGI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N145                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In IDDMDS.|||In IDDMDS; severely reduced secretion due to retention of the mutant in the Golgi apparatus.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich repeat LGI family member 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017710|||http://purl.uniprot.org/annotation/VAR_053488|||http://purl.uniprot.org/annotation/VAR_087683|||http://purl.uniprot.org/annotation/VAR_087684|||http://purl.uniprot.org/annotation/VAR_087685|||http://purl.uniprot.org/annotation/VSP_056297
http://togogenome.org/gene/9606:SLC2A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95528                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with lower insulin level.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In ATORS.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 2, facilitated glucose transporter member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050379|||http://purl.uniprot.org/annotation/VAR_024652|||http://purl.uniprot.org/annotation/VAR_029335|||http://purl.uniprot.org/annotation/VAR_029535|||http://purl.uniprot.org/annotation/VAR_029536|||http://purl.uniprot.org/annotation/VAR_029537|||http://purl.uniprot.org/annotation/VAR_042417|||http://purl.uniprot.org/annotation/VAR_042418|||http://purl.uniprot.org/annotation/VAR_042419|||http://purl.uniprot.org/annotation/VAR_042420|||http://purl.uniprot.org/annotation/VAR_042421|||http://purl.uniprot.org/annotation/VAR_042422|||http://purl.uniprot.org/annotation/VAR_042423|||http://purl.uniprot.org/annotation/VAR_042424
http://togogenome.org/gene/9606:EDNRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25101                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Endothelin-1 receptor|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In MFDA.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012721|||http://purl.uniprot.org/annotation/VAR_035758|||http://purl.uniprot.org/annotation/VAR_073788|||http://purl.uniprot.org/annotation/VAR_073789|||http://purl.uniprot.org/annotation/VSP_011059|||http://purl.uniprot.org/annotation/VSP_011060|||http://purl.uniprot.org/annotation/VSP_011061|||http://purl.uniprot.org/annotation/VSP_011062|||http://purl.uniprot.org/annotation/VSP_011063|||http://purl.uniprot.org/annotation/VSP_045578
http://togogenome.org/gene/9606:ZNF322                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6U7Q0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10; degenerate|||C2H2-type 11; degenerate|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Phosphoserine|||Zinc finger protein 322                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047529
http://togogenome.org/gene/9606:C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13671                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||C-linked (Man) tryptophan; partial|||C5b-binding domain|||CCP 1|||CCP 2|||Complement component C6|||EGF-like|||Factor I module (FIM) 1|||Factor I module (FIM) 2|||In allotype C6 A.|||Kazal-like 1|||Kazal-like 2|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) threonine|||Sushi 1|||Sushi 2|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023579|||http://purl.uniprot.org/annotation/VAR_006056|||http://purl.uniprot.org/annotation/VAR_027647|||http://purl.uniprot.org/annotation/VAR_027648
http://togogenome.org/gene/9606:STT3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46977                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||DK motif|||DXD motif 1|||DXD motif 2|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A|||Helical|||Important for catalytic activity|||In CDG1WAD.|||In CDG1WAD; partial loss of function, when tested in a heterologous system; does not affect expression levels.|||In CDG1WAD; unknown pathological significance; partial loss of function, when tested in a heterologous system.|||In CDG1WAD; unknown pathological significance; partial loss of function, when tested in a heterologous system; does not affect expression levels.|||In CDG1WAR; affects activity resulting in hypoglycosylation of STT3A-specific substrates.|||In isoform 2.|||Interacts with target acceptor peptide in protein substrate|||Lumenal|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||SVSE motif|||WWDYG motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072290|||http://purl.uniprot.org/annotation/VAR_070944|||http://purl.uniprot.org/annotation/VAR_086762|||http://purl.uniprot.org/annotation/VAR_086763|||http://purl.uniprot.org/annotation/VAR_086764|||http://purl.uniprot.org/annotation/VAR_086765|||http://purl.uniprot.org/annotation/VAR_086766|||http://purl.uniprot.org/annotation/VAR_086767|||http://purl.uniprot.org/annotation/VAR_086768|||http://purl.uniprot.org/annotation/VSP_055106
http://togogenome.org/gene/9606:CAVIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NZI2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Caveolae-associated protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Leucine-zipper 1|||Leucine-zipper 2|||Leucine-zipper 3|||N-acetylmethionine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Required for homotrimerization and for interaction with CAVIN2 and CAVIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097094|||http://purl.uniprot.org/annotation/VAR_034416|||http://purl.uniprot.org/annotation/VAR_035982|||http://purl.uniprot.org/annotation/VSP_051624|||http://purl.uniprot.org/annotation/VSP_051625
http://togogenome.org/gene/9606:OR5M9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK6|||http://purl.uniprot.org/uniprot/Q8NGP3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150607|||http://purl.uniprot.org/annotation/VAR_034230
http://togogenome.org/gene/9606:MAEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP0|||http://purl.uniprot.org/uniprot/E9JVC4|||http://purl.uniprot.org/uniprot/Q96JY0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HMG box|||In isoform 2.|||In isoform 3.|||Maelstrom|||Protein maelstrom homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232501|||http://purl.uniprot.org/annotation/VAR_034103|||http://purl.uniprot.org/annotation/VSP_036660|||http://purl.uniprot.org/annotation/VSP_036661|||http://purl.uniprot.org/annotation/VSP_036662
http://togogenome.org/gene/9606:SPATA19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5L4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||Phosphoserine|||Spermatogenesis-associated protein 19, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251609|||http://purl.uniprot.org/annotation/VAR_027697
http://togogenome.org/gene/9606:LGSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TDP6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GS beta-grasp|||GS catalytic|||In isoform 2.|||In isoform 3.|||Lengsin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153282|||http://purl.uniprot.org/annotation/VAR_054552|||http://purl.uniprot.org/annotation/VAR_054553|||http://purl.uniprot.org/annotation/VAR_054554|||http://purl.uniprot.org/annotation/VSP_036480|||http://purl.uniprot.org/annotation/VSP_036481|||http://purl.uniprot.org/annotation/VSP_036482|||http://purl.uniprot.org/annotation/VSP_036483
http://togogenome.org/gene/9606:DEFB125                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4E8|||http://purl.uniprot.org/uniprot/Q8N687                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 125|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006996|||http://purl.uniprot.org/annotation/PRO_0000006997|||http://purl.uniprot.org/annotation/PRO_5005122720|||http://purl.uniprot.org/annotation/VAR_061134
http://togogenome.org/gene/9606:HDGFL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Hepatoma-derived growth factor-related protein 3|||Nuclear localization signal|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191703
http://togogenome.org/gene/9606:SLC25A15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y619                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Does not affect ornithine-ornithine exchange. Does not affect substrate specificity.|||Exhibits an altered substrate specificity. Favors the transport of L-arginine and L-lysine with respect to that of L-ornithine.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In HHHS.|||In HHHS; abolishes ornithine/ornithine exchange.|||In HHHS; does not affect mitochondrial localization.|||In HHHS; exhibits very low transport activity despite normal insertion in the liposomal membrane.|||In HHHS; incapable of catalyzing homo-exchanges of ornithine, arginine, lysine and citrulline.|||In HHHS; maintains a residual transport activity of 10%. Not detected at mitochondrion membrane.|||In HHHS; maintains a residual transport activity of 35%.|||In HHHS; requires 2 nucleotide substitutions; unknown pathological significance.|||Incapable of catalyzing homo-exchanges of ornithine, arginine, lysine and citrulline.|||Mitochondrial ornithine transporter 1|||Reduced ornithine-ornithine exchange. Does not affect substrate specificity.|||Reduced uptake rate for ornithine transport. Favors the transport of L-arginine and L-lysine with respect to that of L-ornithine.|||Solcar 1|||Solcar 2|||Solcar 3|||Substrate specificities are markedly altered. Vmax value is 14-fold lower for ornithine as substrate.|||Substrate specificities are markedly altered. Vmax value is 14-fold lower for ornithine as substrate. Decreased strongly L-ornithine transport but not L-arginine and L-lysine transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090650|||http://purl.uniprot.org/annotation/VAR_012757|||http://purl.uniprot.org/annotation/VAR_012758|||http://purl.uniprot.org/annotation/VAR_012759|||http://purl.uniprot.org/annotation/VAR_012760|||http://purl.uniprot.org/annotation/VAR_012761|||http://purl.uniprot.org/annotation/VAR_012762|||http://purl.uniprot.org/annotation/VAR_012763|||http://purl.uniprot.org/annotation/VAR_012764|||http://purl.uniprot.org/annotation/VAR_058948|||http://purl.uniprot.org/annotation/VAR_058949|||http://purl.uniprot.org/annotation/VAR_058950|||http://purl.uniprot.org/annotation/VAR_058951|||http://purl.uniprot.org/annotation/VAR_058952|||http://purl.uniprot.org/annotation/VAR_058953|||http://purl.uniprot.org/annotation/VAR_058954|||http://purl.uniprot.org/annotation/VAR_058955|||http://purl.uniprot.org/annotation/VAR_058956|||http://purl.uniprot.org/annotation/VAR_087078
http://togogenome.org/gene/9606:CFAP70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSW1|||http://purl.uniprot.org/uniprot/A0A8I5KZ08|||http://purl.uniprot.org/uniprot/Q5T0N1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 70|||Disordered|||In SPGF41; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291913|||http://purl.uniprot.org/annotation/VAR_032877|||http://purl.uniprot.org/annotation/VAR_032878|||http://purl.uniprot.org/annotation/VAR_083155|||http://purl.uniprot.org/annotation/VSP_026289|||http://purl.uniprot.org/annotation/VSP_026291|||http://purl.uniprot.org/annotation/VSP_054461|||http://purl.uniprot.org/annotation/VSP_054462
http://togogenome.org/gene/9606:TMEM239                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW34                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 239                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413694|||http://purl.uniprot.org/annotation/VSP_053737
http://togogenome.org/gene/9606:ACOT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL42|||http://purl.uniprot.org/uniprot/Q86TX2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Sequence Variant                                                                                  ^@                                                                                  Acyl-CoA thioester hydrolase/bile acid-CoA amino acid N-acetyltransferase|||Acyl-coenzyme A thioesterase 1|||BAAT/Acyl-CoA thioester hydrolase C-terminal|||Charge relay system|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202155|||http://purl.uniprot.org/annotation/VAR_059830
http://togogenome.org/gene/9606:RUNDC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NL0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RUN|||RUN domain-containing protein 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336049|||http://purl.uniprot.org/annotation/VAR_043473|||http://purl.uniprot.org/annotation/VAR_043474|||http://purl.uniprot.org/annotation/VAR_043475|||http://purl.uniprot.org/annotation/VSP_033803|||http://purl.uniprot.org/annotation/VSP_033804|||http://purl.uniprot.org/annotation/VSP_033805|||http://purl.uniprot.org/annotation/VSP_033806|||http://purl.uniprot.org/annotation/VSP_033807
http://togogenome.org/gene/9606:ADAMTSL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A669KBE7|||http://purl.uniprot.org/uniprot/B7ZMJ3|||http://purl.uniprot.org/uniprot/Q6UY14|||http://purl.uniprot.org/uniprot/Q9UFG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ADAMTS-like protein 4|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||PLAC|||Polar residues|||Pro residues|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257966|||http://purl.uniprot.org/annotation/PRO_5002867183|||http://purl.uniprot.org/annotation/PRO_5025334078|||http://purl.uniprot.org/annotation/VAR_061918|||http://purl.uniprot.org/annotation/VAR_061919|||http://purl.uniprot.org/annotation/VSP_052183|||http://purl.uniprot.org/annotation/VSP_052184|||http://purl.uniprot.org/annotation/VSP_055759
http://togogenome.org/gene/9606:RALB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11234                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Confers resistance to GGTI-induced pancreatic cancer cell apoptosis, but not to GGTI-dependent inhibition of anchorage-independent proliferation.|||Cysteine methyl ester|||Disordered|||Effector region|||Impaired abscission, the last step of cytokinesis, as shown by the accumulation of bridged cells. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23.|||Impaired abscission, the last step of cytokinesis. No effect on cytokinesis; when associated with V-23.|||Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with 1-M--S-11 or N-49. No effect on cytokinesis; when associated with R-38, W-48 or E-49. No effect on interaction with EXOC2 and EXOC8. Decreased interaction with EXOC2 and EXOC8; when associated with R-38 or W-48.|||In isoform 2.|||In isoform 3.|||Loss of GTPase activity.|||Loss of geranylgeranylation and membrane localization.|||No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with V-23.|||No effect on cytokinesis. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23.|||Ras-related protein Ral-B|||Reduces the binding affinity to EXOC2 effector.|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082698|||http://purl.uniprot.org/annotation/PRO_0000281349|||http://purl.uniprot.org/annotation/VSP_055843|||http://purl.uniprot.org/annotation/VSP_055844
http://togogenome.org/gene/9606:ALKBH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXW9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4|||Fe2OG dioxygenase|||In isoform 2.|||Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-171.|||Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-254.|||Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-171 and A-254.|||N-acetylalanine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239281|||http://purl.uniprot.org/annotation/VAR_061004|||http://purl.uniprot.org/annotation/VSP_019128|||http://purl.uniprot.org/annotation/VSP_036841
http://togogenome.org/gene/9606:ASCL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R2M9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  BHLH|||Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RIMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIU4|||http://purl.uniprot.org/uniprot/A0A8Q3SJ53|||http://purl.uniprot.org/uniprot/A0A994J503|||http://purl.uniprot.org/uniprot/A0A994J5M6|||http://purl.uniprot.org/uniprot/A0A994J7W6|||http://purl.uniprot.org/uniprot/F8W6W8|||http://purl.uniprot.org/uniprot/Q9UQ26                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In CRSDS.|||In isoform 1 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||RabBD|||Regulating synaptic membrane exocytosis protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190201|||http://purl.uniprot.org/annotation/VAR_084549|||http://purl.uniprot.org/annotation/VAR_084550|||http://purl.uniprot.org/annotation/VAR_084551|||http://purl.uniprot.org/annotation/VAR_084552|||http://purl.uniprot.org/annotation/VSP_040864|||http://purl.uniprot.org/annotation/VSP_040865|||http://purl.uniprot.org/annotation/VSP_040866|||http://purl.uniprot.org/annotation/VSP_040867|||http://purl.uniprot.org/annotation/VSP_040868|||http://purl.uniprot.org/annotation/VSP_040869|||http://purl.uniprot.org/annotation/VSP_040870|||http://purl.uniprot.org/annotation/VSP_040871|||http://purl.uniprot.org/annotation/VSP_040872|||http://purl.uniprot.org/annotation/VSP_040873|||http://purl.uniprot.org/annotation/VSP_040874|||http://purl.uniprot.org/annotation/VSP_040875|||http://purl.uniprot.org/annotation/VSP_044661|||http://purl.uniprot.org/annotation/VSP_044662
http://togogenome.org/gene/9606:HAGH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16775                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Hydroxyacylglutathione hydrolase, mitochondrial|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192342|||http://purl.uniprot.org/annotation/VSP_037929|||http://purl.uniprot.org/annotation/VSP_055199|||http://purl.uniprot.org/annotation/VSP_055200
http://togogenome.org/gene/9606:GTF2IRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PFE2|||http://purl.uniprot.org/uniprot/Q9UHL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytoplasmic localization.|||Disordered|||GTF2I-like 1|||GTF2I-like 2|||GTF2I-like 3|||GTF2I-like 4|||GTF2I-like 5|||General transcription factor II-I repeat domain-containing protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083870|||http://purl.uniprot.org/annotation/VAR_013446|||http://purl.uniprot.org/annotation/VSP_003873|||http://purl.uniprot.org/annotation/VSP_043425
http://togogenome.org/gene/9606:DDR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16832                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes collagen binding.|||Abolishes kinase activity.|||Cytoplasmic|||Discoidin domain-containing receptor 2|||Disordered|||Extracellular|||F5/8 type C|||Helical|||In SEMD-SL.|||In SEMD-SL; abolishes collagen binding.|||In SEMD-SL; causes retention in an intracellular compartment and thereby abolishes signaling in response collagen binding.|||In WRCN; increased autophosphorylation in patient fibroblasts.|||In a lung large cell carcinoma sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC and autocatalysis|||Promotes autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-741.|||Protein kinase|||Proton acceptor|||Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-736 and F-740.|||Reduces autophosphorylation. Abolishes phosphorylation by SRC; when associated with F-740 and F-741.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016746|||http://purl.uniprot.org/annotation/VAR_041498|||http://purl.uniprot.org/annotation/VAR_041499|||http://purl.uniprot.org/annotation/VAR_041500|||http://purl.uniprot.org/annotation/VAR_041501|||http://purl.uniprot.org/annotation/VAR_063050|||http://purl.uniprot.org/annotation/VAR_063051|||http://purl.uniprot.org/annotation/VAR_063052|||http://purl.uniprot.org/annotation/VAR_065719|||http://purl.uniprot.org/annotation/VAR_075417|||http://purl.uniprot.org/annotation/VAR_081931|||http://purl.uniprot.org/annotation/VAR_081932
http://togogenome.org/gene/9606:CSNK1G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXA3|||http://purl.uniprot.org/uniprot/Q9HCP0|||http://purl.uniprot.org/uniprot/U3KQB3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Casein kinase I isoform gamma-1|||Disordered|||In isoform 1S.|||Loss of kinase activity.|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with non-syndromic early-onset epilepsy associated with severe developmental delay and microcephaly.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192839|||http://purl.uniprot.org/annotation/VAR_042084|||http://purl.uniprot.org/annotation/VAR_042085|||http://purl.uniprot.org/annotation/VAR_078686|||http://purl.uniprot.org/annotation/VSP_004748
http://togogenome.org/gene/9606:UBE2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RAH7|||http://purl.uniprot.org/uniprot/P61077                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes affect lysine reactivity.|||Activity is restricted HECT-type and not RING-containing E3 ubiquitin-protein ligases. Exhibits ubiquitin transfer with ARIH1 and PRKN.|||Does not affect lysine reactivity.|||Glycyl thioester intermediate|||Has intermediate lysine reactivity.|||In isoform 2.|||In isoform 3.|||Loss of function.|||Strongly impairs lysine reactivity but retains some ability to transfer ubiquitin to BRCA1.|||UBC core|||Ubiquitin-conjugating enzyme E2 D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082466|||http://purl.uniprot.org/annotation/VSP_038096|||http://purl.uniprot.org/annotation/VSP_038097
http://togogenome.org/gene/9606:SGCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92629                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Delta-sarcoglycan|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In CMD1L.|||In LGMDR6.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175245|||http://purl.uniprot.org/annotation/VAR_010396|||http://purl.uniprot.org/annotation/VAR_010429|||http://purl.uniprot.org/annotation/VAR_013181|||http://purl.uniprot.org/annotation/VSP_039245|||http://purl.uniprot.org/annotation/VSP_039246|||http://purl.uniprot.org/annotation/VSP_039247
http://togogenome.org/gene/9606:TFDP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Acidic residues|||Critical for repression of E2F activity|||DCB1|||DCB2|||DEF box|||Disordered|||Involved in negatively regulating E2F activity|||No effect on down-regulation of E2F transcriptional activity; when associated R-112.|||No effect on down-regulation of E2F transcriptional activity; when associated with or without R-112.|||No effect on down-regulation of E2F transcriptional activity; when associated with or without R-161 or with V-164.|||Polar residues|||Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; N-131 and E-145.|||Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and E-145.|||Restores enhanced E2F-mediated transcriptional activity; when associated with K-121; Y-130 and N-131.|||Restores enhanced E2F-mediated transcriptional activity; when associated with Y-130; N-131 and E-145.|||Transcription factor Dp family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305940
http://togogenome.org/gene/9606:EPHX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6B9                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Transmembrane                                                                                  ^@                                                                                  Epoxide hydrolase 3|||Helical|||Loss of catalytic activity.|||No effect on catalytic activity.|||Nucleophile|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264232
http://togogenome.org/gene/9606:ZNF107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYK5|||http://purl.uniprot.org/uniprot/A0A0B4J2G0|||http://purl.uniprot.org/uniprot/Q8WVL4|||http://purl.uniprot.org/uniprot/Q9UII5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Non-terminal Residue|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; atypical|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17; atypical|||C2H2-type 18; atypical|||C2H2-type 19; atypical|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; atypical|||C2H2-type 7|||C2H2-type 8; atypical|||C2H2-type 9; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 107                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047681
http://togogenome.org/gene/9606:SEC31B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Pro residues|||Protein transport protein Sec31B|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8; interaction with SEC13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295153|||http://purl.uniprot.org/annotation/VAR_033228|||http://purl.uniprot.org/annotation/VAR_033229|||http://purl.uniprot.org/annotation/VAR_033230|||http://purl.uniprot.org/annotation/VAR_033231|||http://purl.uniprot.org/annotation/VAR_033232|||http://purl.uniprot.org/annotation/VAR_033233|||http://purl.uniprot.org/annotation/VAR_033234|||http://purl.uniprot.org/annotation/VAR_053415|||http://purl.uniprot.org/annotation/VAR_053416|||http://purl.uniprot.org/annotation/VSP_026757|||http://purl.uniprot.org/annotation/VSP_026758|||http://purl.uniprot.org/annotation/VSP_026759|||http://purl.uniprot.org/annotation/VSP_026760|||http://purl.uniprot.org/annotation/VSP_026761|||http://purl.uniprot.org/annotation/VSP_026762|||http://purl.uniprot.org/annotation/VSP_026763
http://togogenome.org/gene/9606:OLIG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Oligodendrocyte transcription factor 3|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127417
http://togogenome.org/gene/9606:SH2D6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXG6                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||SH2                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ZNF185                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPM4|||http://purl.uniprot.org/uniprot/O15231                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7 and isoform 8.|||In isoform 9.|||LIM zinc-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 185                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075911|||http://purl.uniprot.org/annotation/VSP_039898|||http://purl.uniprot.org/annotation/VSP_039899|||http://purl.uniprot.org/annotation/VSP_039900|||http://purl.uniprot.org/annotation/VSP_039901|||http://purl.uniprot.org/annotation/VSP_039902|||http://purl.uniprot.org/annotation/VSP_043405|||http://purl.uniprot.org/annotation/VSP_045080|||http://purl.uniprot.org/annotation/VSP_045081|||http://purl.uniprot.org/annotation/VSP_047205|||http://purl.uniprot.org/annotation/VSP_047206|||http://purl.uniprot.org/annotation/VSP_054773
http://togogenome.org/gene/9606:C18orf32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCD1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Necessary for its localzation to the endoplasmic reticulum and lipid droplets|||UPF0729 protein C18orf32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321908|||http://purl.uniprot.org/annotation/VAR_039374
http://togogenome.org/gene/9606:ST8SIA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5F7|||http://purl.uniprot.org/uniprot/F5H8D1|||http://purl.uniprot.org/uniprot/O15466                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-2,8-sialyltransferase 8E|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149296|||http://purl.uniprot.org/annotation/VSP_056664
http://togogenome.org/gene/9606:TGFB1I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43294                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CBLC and enhancement of CBLCE3 ubiquitin-protein ligase activity.|||Disordered|||In isoform 2.|||Interaction with PTK2/FAK1|||Interaction with PTK2B/PYK2|||LD motif 1|||LD motif 2|||LD motif 3|||LD motif 4|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Loss of AR coactivation; when associated with S-369.|||Loss of AR coactivation; when associated with S-372.|||Loss of AR coactivation; when associated with S-428.|||Loss of AR coactivation; when associated with S-431.|||Loss of interaction with AR; when associated with 338-A--A-342.|||Loss of interaction with AR; when associated with 456-A--A-460.|||N-acetylmethionine|||No effect on interaction with CBLC.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FAK2 and FYN|||Polar residues|||Prevents phosphorylation by FAK2 and FYN. Prevents interaction with CSK.|||Transcription activation|||Transforming growth factor beta-1-induced transcript 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291582|||http://purl.uniprot.org/annotation/VAR_032831|||http://purl.uniprot.org/annotation/VSP_026183
http://togogenome.org/gene/9606:KIF4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95239|||http://purl.uniprot.org/uniprot/Q59HG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes chromatin localization; in association with A-1106 and A-1110.|||Abolishes chromatin localization; in association with A-1106 and A-1112.|||Abolishes chromatin localization; in association with A-1110 and A-1112.|||Basic and acidic residues|||CRD; required for [4Fe-4S] cluster binding and localization to the spindle midzone and midbody during anaphase and telophase|||Chromosome-associated kinesin KIF4A|||Diffuse localization and does not localize to the spindle midzone or midbody during anaphase and telophase. Does not affect the interaction with PRC1.|||Disordered|||Globular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Kinesin motor|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Required for the interaction with PRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125437|||http://purl.uniprot.org/annotation/VAR_021828|||http://purl.uniprot.org/annotation/VAR_049693|||http://purl.uniprot.org/annotation/VAR_049694|||http://purl.uniprot.org/annotation/VSP_013375|||http://purl.uniprot.org/annotation/VSP_013376
http://togogenome.org/gene/9606:LIN28B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN17                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||CCHC-type 1|||CCHC-type 2|||CSD|||Disordered|||In isoform 2.|||Nucleolar localization signal|||Phosphoserine|||Polar residues|||Protein lin-28 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253793|||http://purl.uniprot.org/annotation/VSP_027207
http://togogenome.org/gene/9606:FBXL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H469                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 15|||Interaction with SMURF1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119931
http://togogenome.org/gene/9606:CDYL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y232                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes CoA-binding and ability to inhibit histone crotonylation.|||Acetyl-CoA-binding domain|||Chromo|||Chromodomain Y-like protein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with EZH2|||N6,N6,N6-trimethyllysine; by EHMT2; alternate|||N6,N6-dimethyllysine; by EHMT2; alternate|||N6-methyllysine; by EHMT2; alternate|||No impact on recruitment to DNA double strand breaks.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080221|||http://purl.uniprot.org/annotation/VAR_032936|||http://purl.uniprot.org/annotation/VAR_032937|||http://purl.uniprot.org/annotation/VAR_032938|||http://purl.uniprot.org/annotation/VAR_032939|||http://purl.uniprot.org/annotation/VSP_026382|||http://purl.uniprot.org/annotation/VSP_026383|||http://purl.uniprot.org/annotation/VSP_026384|||http://purl.uniprot.org/annotation/VSP_041025
http://togogenome.org/gene/9606:TMCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PC87|||http://purl.uniprot.org/uniprot/O94876                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Transmembrane and coiled-coil domains protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184595|||http://purl.uniprot.org/annotation/VAR_047918|||http://purl.uniprot.org/annotation/VSP_053924|||http://purl.uniprot.org/annotation/VSP_053925
http://togogenome.org/gene/9606:PDIA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPU5|||http://purl.uniprot.org/uniprot/Q15084                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  25% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-58 and S-193.|||50% decrease in enzyme activity; when associated with S-55. 90% decrease in enzyme activity; when associated with S-193. Abolishes enzyme activity; when associated with S-55; S-190 and S-193.|||50% decrease in enzyme activity; when associated with S-58. Abolishes enzyme activity; when associated with S-58; S-190 and S-193.|||90% decrease in enzyme activity; when associated with S-58. 25% decrease in enzyme activity; when associated with S-190. Abolishes enzyme activity; when associated with S-55; S-58 and S-190.|||Accelerates dephosphorylation of ERN1; when associated with A-193.|||Accelerates dephosphorylation of ERN1; when associated with A-58.|||Contributes to redox potential value|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lowers pKa of C-terminal Cys of first active site|||Lowers pKa of C-terminal Cys of second active site|||Nucleophile|||Phosphoserine|||Phosphoserine; by FAM20C|||Prevents secretion from ER|||Protein disulfide-isomerase A6|||Redox-active|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034236|||http://purl.uniprot.org/annotation/PRO_5017277959|||http://purl.uniprot.org/annotation/VAR_022152|||http://purl.uniprot.org/annotation/VSP_021803|||http://purl.uniprot.org/annotation/VSP_054370|||http://purl.uniprot.org/annotation/VSP_055173|||http://purl.uniprot.org/annotation/VSP_055174
http://togogenome.org/gene/9606:GPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43304                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Found in patients with type 2 diabetes; unknown pathological significance.|||Glycerol-3-phosphate dehydrogenase, mitochondrial|||In isoform 2.|||Mitochondrion|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010429|||http://purl.uniprot.org/annotation/VAR_025215|||http://purl.uniprot.org/annotation/VAR_049113|||http://purl.uniprot.org/annotation/VAR_049114|||http://purl.uniprot.org/annotation/VAR_083484|||http://purl.uniprot.org/annotation/VAR_083485|||http://purl.uniprot.org/annotation/VAR_083486|||http://purl.uniprot.org/annotation/VSP_017134
http://togogenome.org/gene/9606:KCNJ15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99712                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 15|||Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In a breast cancer sample; somatic mutation.|||Pore-forming|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154972|||http://purl.uniprot.org/annotation/VAR_019728|||http://purl.uniprot.org/annotation/VAR_025523|||http://purl.uniprot.org/annotation/VAR_036427
http://togogenome.org/gene/9606:MIDEAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1C7CYX1|||http://purl.uniprot.org/uniprot/Q6PJG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||C2H2-type|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Mitotic deacetylase-associated SANT domain protein|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259764|||http://purl.uniprot.org/annotation/VAR_050182|||http://purl.uniprot.org/annotation/VAR_050183|||http://purl.uniprot.org/annotation/VAR_061361
http://togogenome.org/gene/9606:RPS20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60866                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Enhanced readthrough on the poly(A)-stall sequences; when associated with R-4.|||Enhanced readthrough on the poly(A)-stall sequences; when associated with R-8.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein uS10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146683|||http://purl.uniprot.org/annotation/VSP_042724
http://togogenome.org/gene/9606:ANO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y532|||http://purl.uniprot.org/uniprot/B7Z9Z0|||http://purl.uniprot.org/uniprot/Q32M45                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin dimerisation|||Anoctamin-4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288650|||http://purl.uniprot.org/annotation/VAR_032453|||http://purl.uniprot.org/annotation/VSP_025741|||http://purl.uniprot.org/annotation/VSP_025742|||http://purl.uniprot.org/annotation/VSP_025743
http://togogenome.org/gene/9606:SIAH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUQ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to degrade DCC.|||Decreased activity.|||Decreased activity; when associated with L-66.|||Decreased activity; when associated with T-68.|||Disordered|||E3 ubiquitin-protein ligase SIAH1|||Impaired ATM mediated phosphorylation, but normal interaction with HIPK2 and HIPK2 subsequent proteasomal degradation.|||Impairs CTNNB1 degradation.|||In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-226.|||In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-237.|||In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-226 and A-237.|||In B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-253.|||In B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-265.|||In BURHAS.|||In BURHAS; loss of function in Wnt signaling pathway.|||In C; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-233.|||In D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-214 and A-215.|||In D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-231 and A-232.|||In D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-214; A-215; A-231 and A-232.|||In E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-142.|||In E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-151.|||In isoform 2.|||In isoform 3.|||Loss of function.|||Loss of function; when associated with A-55 and A-59.|||Loss of function; when associated with A-55 and S-72.|||Loss of function; when associated with A-59 and S-72.|||Loss of function; when associated with S-44.|||Loss of function; when associated with Y-59.|||No effect.|||Phosphoserine; by ATM and ATR|||RING-type|||Reduced interaction with HIPK2 and HIPK2 subsequent proteasomal degradation.|||SBD|||SIAH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056163|||http://purl.uniprot.org/annotation/VAR_085780|||http://purl.uniprot.org/annotation/VAR_085781|||http://purl.uniprot.org/annotation/VAR_085782|||http://purl.uniprot.org/annotation/VAR_085783|||http://purl.uniprot.org/annotation/VAR_085784|||http://purl.uniprot.org/annotation/VSP_010166|||http://purl.uniprot.org/annotation/VSP_029210|||http://purl.uniprot.org/annotation/VSP_029211
http://togogenome.org/gene/9606:ZNF587                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SQ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 587                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233987|||http://purl.uniprot.org/annotation/VSP_046842
http://togogenome.org/gene/9606:GYS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13807                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycogen [starch] synthase, muscle|||In NIDDM.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by AMPK and PKA|||Phosphoserine; by CK2|||Phosphoserine; by GSK3-alpha and GSK3-beta|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194763|||http://purl.uniprot.org/annotation/VAR_007859|||http://purl.uniprot.org/annotation/VAR_014727|||http://purl.uniprot.org/annotation/VAR_014728|||http://purl.uniprot.org/annotation/VAR_014729|||http://purl.uniprot.org/annotation/VAR_014730|||http://purl.uniprot.org/annotation/VAR_014731|||http://purl.uniprot.org/annotation/VAR_014732|||http://purl.uniprot.org/annotation/VAR_037958|||http://purl.uniprot.org/annotation/VSP_042745
http://togogenome.org/gene/9606:DAPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIK4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes apoptotic activity.|||Autoinhibitory domain|||Calmodulin-binding|||Death-associated protein kinase 2|||Disordered|||In isoform 2.|||Interaction with YWHAE is increased.|||Interaction with YWHAE is reduced.|||Leucine-zipper|||Loss of Ca(2+)-calmodulin independent phosphorylation, increase in apoptotic activity.|||Loss of activity, apoptotic function and of autophosphorylation.|||Loss of ca(2+)-calmodulin binding, increase in activity, loss of autophosphorylation.|||No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity.|||No effect on interaction with YWHAE.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by PKB/AKT1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085912|||http://purl.uniprot.org/annotation/VAR_040436|||http://purl.uniprot.org/annotation/VAR_040437|||http://purl.uniprot.org/annotation/VSP_042057
http://togogenome.org/gene/9606:CRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7D6VM04|||http://purl.uniprot.org/uniprot/A8K118|||http://purl.uniprot.org/uniprot/B7Z824|||http://purl.uniprot.org/uniprot/B7Z826|||http://purl.uniprot.org/uniprot/F5H0L2|||http://purl.uniprot.org/uniprot/P82279                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with EPB41L5. No effection on interaction wtih PALS1.|||Abolishes interaction with PALS1. Not required for interaction with EPB41L5.|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16; calcium-binding|||EGF-like 17|||EGF-like 18|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8|||EGF-like 9|||Extracellular|||Found in a patient with Leber congenital amaurosis; unknown pathological significance.|||Found in a patient with early-onset retinal dystrophy; unknown pathological significance.|||Found in patients with retinitis pigmentosa; unknown pathological significance; heterozygous.|||Helical|||In LCA8 and RP12.|||In LCA8.|||In LCA8; also early onset RP without preservation of the paraarteriolar retinal pigment epithelium.|||In LCA8; also found in patients with early-onset rod-cone retinal dystrophy.|||In LCA8; unknown pathological significance.|||In PPCRA.|||In RP12 and LCA8.|||In RP12 and LCA8; without preservation of the paraarteriolar retinal pigment epithelium.|||In RP12.|||In RP12; located on the same allele as H-837.|||In RP12; located on the same allele as T-1354.|||In RP12; unknown pathological significance.|||In RP12; without preservation of the paraarteriolar retinal pigment epithelium.|||In early-onset retinal dystrophy; probable disease-associated variant.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with EPB41L5|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in patients with early-onset retinal dystrophy.|||Probable disease-associated variant found in patients with rod-cone retinal dystrophy.|||Protein crumbs homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007500|||http://purl.uniprot.org/annotation/PRO_5002722711|||http://purl.uniprot.org/annotation/PRO_5027906953|||http://purl.uniprot.org/annotation/VAR_011641|||http://purl.uniprot.org/annotation/VAR_011642|||http://purl.uniprot.org/annotation/VAR_011643|||http://purl.uniprot.org/annotation/VAR_011644|||http://purl.uniprot.org/annotation/VAR_011645|||http://purl.uniprot.org/annotation/VAR_011646|||http://purl.uniprot.org/annotation/VAR_011647|||http://purl.uniprot.org/annotation/VAR_011648|||http://purl.uniprot.org/annotation/VAR_011649|||http://purl.uniprot.org/annotation/VAR_022941|||http://purl.uniprot.org/annotation/VAR_022942|||http://purl.uniprot.org/annotation/VAR_022943|||http://purl.uniprot.org/annotation/VAR_022944|||http://purl.uniprot.org/annotation/VAR_022945|||http://purl.uniprot.org/annotation/VAR_022946|||http://purl.uniprot.org/annotation/VAR_022947|||http://purl.uniprot.org/annotation/VAR_022948|||http://purl.uniprot.org/annotation/VAR_022949|||http://purl.uniprot.org/annotation/VAR_022950|||http://purl.uniprot.org/annotation/VAR_022951|||http://purl.uniprot.org/annotation/VAR_022952|||http://purl.uniprot.org/annotation/VAR_022953|||http://purl.uniprot.org/annotation/VAR_022954|||http://purl.uniprot.org/annotation/VAR_022955|||http://purl.uniprot.org/annotation/VAR_022956|||http://purl.uniprot.org/annotation/VAR_022957|||http://purl.uniprot.org/annotation/VAR_022958|||http://purl.uniprot.org/annotation/VAR_022959|||http://purl.uniprot.org/annotation/VAR_022960|||http://purl.uniprot.org/annotation/VAR_022961|||http://purl.uniprot.org/annotation/VAR_022962|||http://purl.uniprot.org/annotation/VAR_022963|||http://purl.uniprot.org/annotation/VAR_022964|||http://purl.uniprot.org/annotation/VAR_022965|||http://purl.uniprot.org/annotation/VAR_022966|||http://purl.uniprot.org/annotation/VAR_022967|||http://purl.uniprot.org/annotation/VAR_022968|||http://purl.uniprot.org/annotation/VAR_022969|||http://purl.uniprot.org/annotation/VAR_022970|||http://purl.uniprot.org/annotation/VAR_022971|||http://purl.uniprot.org/annotation/VAR_022972|||http://purl.uniprot.org/annotation/VAR_022973|||http://purl.uniprot.org/annotation/VAR_022974|||http://purl.uniprot.org/annotation/VAR_022975|||http://purl.uniprot.org/annotation/VAR_022976|||http://purl.uniprot.org/annotation/VAR_022977|||http://purl.uniprot.org/annotation/VAR_022978|||http://purl.uniprot.org/annotation/VAR_022979|||http://purl.uniprot.org/annotation/VAR_022980|||http://purl.uniprot.org/annotation/VAR_022981|||http://purl.uniprot.org/annotation/VAR_022982|||http://purl.uniprot.org/annotation/VAR_022983|||http://purl.uniprot.org/annotation/VAR_064180|||http://purl.uniprot.org/annotation/VAR_064181|||http://purl.uniprot.org/annotation/VAR_067125|||http://purl.uniprot.org/annotation/VAR_067126|||http://purl.uniprot.org/annotation/VAR_067127|||http://purl.uniprot.org/annotation/VAR_067128|||http://purl.uniprot.org/annotation/VAR_067129|||http://purl.uniprot.org/annotation/VAR_067130|||http://purl.uniprot.org/annotation/VAR_067131|||http://purl.uniprot.org/annotation/VAR_067132|||http://purl.uniprot.org/annotation/VAR_067133|||http://purl.uniprot.org/annotation/VAR_067134|||http://purl.uniprot.org/annotation/VAR_067135|||http://purl.uniprot.org/annotation/VAR_067136|||http://purl.uniprot.org/annotation/VAR_067137|||http://purl.uniprot.org/annotation/VAR_067138|||http://purl.uniprot.org/annotation/VAR_067139|||http://purl.uniprot.org/annotation/VAR_067140|||http://purl.uniprot.org/annotation/VAR_067141|||http://purl.uniprot.org/annotation/VAR_067142|||http://purl.uniprot.org/annotation/VAR_067143|||http://purl.uniprot.org/annotation/VAR_067144|||http://purl.uniprot.org/annotation/VAR_067145|||http://purl.uniprot.org/annotation/VAR_067146|||http://purl.uniprot.org/annotation/VAR_067147|||http://purl.uniprot.org/annotation/VAR_067148|||http://purl.uniprot.org/annotation/VAR_067149|||http://purl.uniprot.org/annotation/VAR_067150|||http://purl.uniprot.org/annotation/VAR_067151|||http://purl.uniprot.org/annotation/VAR_067152|||http://purl.uniprot.org/annotation/VAR_067153|||http://purl.uniprot.org/annotation/VAR_067154|||http://purl.uniprot.org/annotation/VAR_067155|||http://purl.uniprot.org/annotation/VAR_067156|||http://purl.uniprot.org/annotation/VAR_067157|||http://purl.uniprot.org/annotation/VAR_067158|||http://purl.uniprot.org/annotation/VAR_067159|||http://purl.uniprot.org/annotation/VAR_068363|||http://purl.uniprot.org/annotation/VAR_079622|||http://purl.uniprot.org/annotation/VAR_079623|||http://purl.uniprot.org/annotation/VAR_079624|||http://purl.uniprot.org/annotation/VAR_079625|||http://purl.uniprot.org/annotation/VAR_079626|||http://purl.uniprot.org/annotation/VAR_079627|||http://purl.uniprot.org/annotation/VAR_079628|||http://purl.uniprot.org/annotation/VAR_079629|||http://purl.uniprot.org/annotation/VAR_082818|||http://purl.uniprot.org/annotation/VSP_014724|||http://purl.uniprot.org/annotation/VSP_014725|||http://purl.uniprot.org/annotation/VSP_014726|||http://purl.uniprot.org/annotation/VSP_014727|||http://purl.uniprot.org/annotation/VSP_014728|||http://purl.uniprot.org/annotation/VSP_014729|||http://purl.uniprot.org/annotation/VSP_045332
http://togogenome.org/gene/9606:SLC23A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 23 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165975|||http://purl.uniprot.org/annotation/VAR_053451|||http://purl.uniprot.org/annotation/VAR_053452|||http://purl.uniprot.org/annotation/VAR_053453|||http://purl.uniprot.org/annotation/VAR_062111|||http://purl.uniprot.org/annotation/VSP_006813|||http://purl.uniprot.org/annotation/VSP_006814
http://togogenome.org/gene/9606:INSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51460                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Turn                                                                                  ^@                                                                                  C peptide like|||Found in a male with undermasculinised genitalia and intra-abdominal testes; unknown pathological significance.|||In CRYPTO.|||In isoform 2.|||Insulin-like 3 A chain|||Insulin-like 3 B chain|||Interchain (between B and A chains)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016140|||http://purl.uniprot.org/annotation/PRO_0000016141|||http://purl.uniprot.org/annotation/PRO_0000016142|||http://purl.uniprot.org/annotation/VAR_013231|||http://purl.uniprot.org/annotation/VAR_013232|||http://purl.uniprot.org/annotation/VAR_013233|||http://purl.uniprot.org/annotation/VAR_013234|||http://purl.uniprot.org/annotation/VAR_013235|||http://purl.uniprot.org/annotation/VAR_013236|||http://purl.uniprot.org/annotation/VAR_013237|||http://purl.uniprot.org/annotation/VAR_017122|||http://purl.uniprot.org/annotation/VSP_045526
http://togogenome.org/gene/9606:XKRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PP77                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||XK-related protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190772|||http://purl.uniprot.org/annotation/VSP_037520
http://togogenome.org/gene/9606:EIF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56537                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 6|||In isoform 2.|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153734|||http://purl.uniprot.org/annotation/VSP_046747
http://togogenome.org/gene/9606:PEX26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R100|||http://purl.uniprot.org/uniprot/A0A0S2Z5M7|||http://purl.uniprot.org/uniprot/Q7Z2D7|||http://purl.uniprot.org/uniprot/Q7Z412                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In PBD-CG8; impaired protein import into peroxisome; decreased interaction with PEX6; does not affect localization to peroxisomal membrane.|||In PBD7A.|||In PBD7B and PBD-CG8; neonatal adrenoleukodystrophy; impaired protein import into peroxisome; affects the interaction with PEX6.|||In PBD7B; infantile Refsum disease.|||In isoform 2.|||Peroxisomal matrix|||Peroxisome assembly protein 26|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058340|||http://purl.uniprot.org/annotation/VAR_018647|||http://purl.uniprot.org/annotation/VAR_018648|||http://purl.uniprot.org/annotation/VAR_018649|||http://purl.uniprot.org/annotation/VAR_034146|||http://purl.uniprot.org/annotation/VAR_087137|||http://purl.uniprot.org/annotation/VAR_087138|||http://purl.uniprot.org/annotation/VAR_087139|||http://purl.uniprot.org/annotation/VSP_053499
http://togogenome.org/gene/9606:SRFBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Serum response factor-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320006
http://togogenome.org/gene/9606:PRSS37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1T9|||http://purl.uniprot.org/uniprot/B7ZMK3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Peptidase S1|||Probable inactive serine protease 37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326070|||http://purl.uniprot.org/annotation/PRO_5002864121|||http://purl.uniprot.org/annotation/VAR_039985
http://togogenome.org/gene/9606:STOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2F5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Polar residues|||Storkhead-box protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313629|||http://purl.uniprot.org/annotation/VSP_030072|||http://purl.uniprot.org/annotation/VSP_030073
http://togogenome.org/gene/9606:TOLLIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR28|||http://purl.uniprot.org/uniprot/F2Z2Y8|||http://purl.uniprot.org/uniprot/Q6FIE9|||http://purl.uniprot.org/uniprot/Q8N8J5|||http://purl.uniprot.org/uniprot/Q9H0E2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AIM1|||AIM2|||C2|||CUE|||In isoform 2.|||N-acetylalanine|||Reduced interaction with TOM1.|||Reduced interaction with TOM1; when associated with Ala-12.|||Reduced interaction with TOM1; when associated with Ala-20.|||Reduced interaction with TOM1; when associated with Ala-23.|||Reduced interaction with TOM1; when associated with Ala-9.|||Removed|||Toll-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072625|||http://purl.uniprot.org/annotation/VAR_034557|||http://purl.uniprot.org/annotation/VAR_079499|||http://purl.uniprot.org/annotation/VSP_056301
http://togogenome.org/gene/9606:ZP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12836                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||P-type|||Processed zona pellucida sperm-binding protein 4|||Removed in mature form|||ZP|||Zona pellucida sperm-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041727|||http://purl.uniprot.org/annotation/PRO_0000041728|||http://purl.uniprot.org/annotation/PRO_0000304578|||http://purl.uniprot.org/annotation/VAR_052997|||http://purl.uniprot.org/annotation/VAR_052998
http://togogenome.org/gene/9606:EMC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R9N3|||http://purl.uniprot.org/uniprot/A0A0S2Z598|||http://purl.uniprot.org/uniprot/Q5J8M3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||ER membrane protein complex subunit 4|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylthreonine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251914|||http://purl.uniprot.org/annotation/VAR_053775|||http://purl.uniprot.org/annotation/VSP_020798|||http://purl.uniprot.org/annotation/VSP_020799|||http://purl.uniprot.org/annotation/VSP_037374|||http://purl.uniprot.org/annotation/VSP_037375
http://togogenome.org/gene/9606:ZNF576                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H609                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Zinc finger protein 576                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047667|||http://purl.uniprot.org/annotation/VAR_023956
http://togogenome.org/gene/9606:CAPRIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14444                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690 and K-695.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-640, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-633, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-626, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-619, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-616, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-612, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-608, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished ability to undergo liquid-liquid phase separation for the formation of a membraneless compartment; when associated with K-612, K-616, K-619, K-626, K-633, K-640, K-660, K-667, K-676, K-684, K-688, K-690, K-695 and K-698.|||Abolished interaction with G3BP1 and ability to promote stress granule formation.|||Abolished interaction with G3BP1.|||Acidic residues|||Asymmetric dimethylarginine; alternate|||Caprin-1|||Decreased ability to undergo liquid-liquid phase separation.|||Disordered|||Does not affect ability to undergo liquid-liquid phase separation.|||G3BP1-binding|||In isoform 2.|||Increased interaction with G3BP1.|||Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-633.|||Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-690.|||Major reduction in MYC and CCND2 RNA-binding; when associated with A-633 and A-690.|||N-acetylproline|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine; by EPHA4|||Polar residues|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087549|||http://purl.uniprot.org/annotation/VAR_042425|||http://purl.uniprot.org/annotation/VAR_042426|||http://purl.uniprot.org/annotation/VAR_042427|||http://purl.uniprot.org/annotation/VSP_032687
http://togogenome.org/gene/9606:S100A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31151                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||N-acetylserine|||Protein S100-A7|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143990|||http://purl.uniprot.org/annotation/VAR_039118
http://togogenome.org/gene/9606:MTERF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AM1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||Transcription termination factor 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255464|||http://purl.uniprot.org/annotation/VAR_034113|||http://purl.uniprot.org/annotation/VAR_034114|||http://purl.uniprot.org/annotation/VAR_053787|||http://purl.uniprot.org/annotation/VAR_053788
http://togogenome.org/gene/9606:CERT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5P4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ceramide transfer; when associated with A-499.|||Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity.|||Ceramide transfer protein|||Disordered|||FFAT|||Found in a patient with intellectual disability.|||Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA and MOSPD2.|||In MRD34.|||In MRD34; associated with authism and epilepsy.|||In isoform 2.|||In isoform 3.|||No effect on ceramide transfer activity.|||PH|||Phosphoserine|||Phosphoserine; by PKD|||Phosphotyrosine|||Polar residues|||Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588.|||Reduces ceramide transfer.|||START                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220665|||http://purl.uniprot.org/annotation/VAR_061815|||http://purl.uniprot.org/annotation/VAR_069403|||http://purl.uniprot.org/annotation/VAR_073721|||http://purl.uniprot.org/annotation/VAR_078652|||http://purl.uniprot.org/annotation/VSP_006276|||http://purl.uniprot.org/annotation/VSP_041022
http://togogenome.org/gene/9606:DBN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16643                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ADF-H|||Basic and acidic residues|||Decreased binding to ZMYND8.|||Disordered|||Drebrin|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of binding to ZMYND8. Loss of ZMYND8 cytoplasmic localization.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080008|||http://purl.uniprot.org/annotation/VAR_035910|||http://purl.uniprot.org/annotation/VAR_035911|||http://purl.uniprot.org/annotation/VAR_047365|||http://purl.uniprot.org/annotation/VAR_047366|||http://purl.uniprot.org/annotation/VSP_028175|||http://purl.uniprot.org/annotation/VSP_053443
http://togogenome.org/gene/9606:VCAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13611|||http://purl.uniprot.org/uniprot/Q59FG9|||http://purl.uniprot.org/uniprot/Q6MZK8|||http://purl.uniprot.org/uniprot/Q86W61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-type lectin|||Cleavage; by ADAMTS15|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||GAG-alpha (glucosaminoglycan attachment domain)|||GAG-beta|||Ig-like|||Ig-like V-type|||In isoform V1 and isoform V3.|||In isoform V1.|||In isoform V2.|||In isoform V3.|||In isoform Vint.|||Link|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Polar residues|||Sushi|||Versican core protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017522|||http://purl.uniprot.org/annotation/PRO_5014588811|||http://purl.uniprot.org/annotation/VAR_020214|||http://purl.uniprot.org/annotation/VAR_020215|||http://purl.uniprot.org/annotation/VAR_020216|||http://purl.uniprot.org/annotation/VAR_021958|||http://purl.uniprot.org/annotation/VAR_021959|||http://purl.uniprot.org/annotation/VAR_021960|||http://purl.uniprot.org/annotation/VAR_031632|||http://purl.uniprot.org/annotation/VAR_031633|||http://purl.uniprot.org/annotation/VSP_003082|||http://purl.uniprot.org/annotation/VSP_003083|||http://purl.uniprot.org/annotation/VSP_003084|||http://purl.uniprot.org/annotation/VSP_003085|||http://purl.uniprot.org/annotation/VSP_003086
http://togogenome.org/gene/9606:TSPAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AKP1|||http://purl.uniprot.org/uniprot/B2RD31|||http://purl.uniprot.org/uniprot/O60636                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219236|||http://purl.uniprot.org/annotation/VAR_052328|||http://purl.uniprot.org/annotation/VSP_047734
http://togogenome.org/gene/9606:LRRIQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN5|||http://purl.uniprot.org/uniprot/Q96JM4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||IQ 3|||In isoform 2.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||Leucine-rich repeat and IQ domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313625|||http://purl.uniprot.org/annotation/VAR_037672|||http://purl.uniprot.org/annotation/VAR_037673|||http://purl.uniprot.org/annotation/VAR_037674|||http://purl.uniprot.org/annotation/VSP_030065
http://togogenome.org/gene/9606:STIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G0XQ39|||http://purl.uniprot.org/uniprot/Q13586                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes activation of CRAC channels.|||Abolishes colocalization with ORAI1 and activation of CRAC channels.|||Constitutive activation of CRAC channels.|||Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels.|||Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108.|||Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110.|||Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||In IMD10.|||In STRMK and TAM1.|||In STRMK; autosomal dominant; promotes constitutive activation of the Ca(2+) release-activated Ca(2+) (CRAC) channel.|||In TAM1; increases store-operated Ca(2+) influx.|||In TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired.|||In isoform 2.|||Increases Ca(2+) influx even when Ca(2+) stores are not depleted.|||Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel.|||Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted.|||Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.|||Microtubule tip localization signal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with autosomal recessive hypomaturation enamel malformations, nail dysplasia and frequent throat infections.|||Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel.|||Reduces activation of CRAC channels.|||SAM|||SOAR/CAD|||Stromal interaction molecule 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033326|||http://purl.uniprot.org/annotation/PRO_5014091417|||http://purl.uniprot.org/annotation/VAR_061878|||http://purl.uniprot.org/annotation/VAR_069892|||http://purl.uniprot.org/annotation/VAR_069893|||http://purl.uniprot.org/annotation/VAR_069894|||http://purl.uniprot.org/annotation/VAR_069895|||http://purl.uniprot.org/annotation/VAR_069896|||http://purl.uniprot.org/annotation/VAR_071476|||http://purl.uniprot.org/annotation/VAR_071477|||http://purl.uniprot.org/annotation/VAR_074037|||http://purl.uniprot.org/annotation/VAR_075619|||http://purl.uniprot.org/annotation/VAR_075620|||http://purl.uniprot.org/annotation/VAR_075621|||http://purl.uniprot.org/annotation/VAR_075622|||http://purl.uniprot.org/annotation/VAR_075623|||http://purl.uniprot.org/annotation/VSP_055150|||http://purl.uniprot.org/annotation/VSP_055151
http://togogenome.org/gene/9606:FRAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CSPG 1|||CSPG 10|||CSPG 11|||CSPG 12|||CSPG 2|||CSPG 3|||CSPG 4|||CSPG 5|||CSPG 6|||CSPG 7|||CSPG 8|||CSPG 9|||Calx-beta 1|||Calx-beta 2|||Calx-beta 3|||Calx-beta 4|||Calx-beta 5|||Cytoplasmic|||Extracellular|||Extracellular matrix organizing protein FRAS1|||FU 1|||FU 10|||FU 11|||FU 12|||FU 13|||FU 14|||FU 2|||FU 3|||FU 4|||FU 5|||FU 6|||FU 7|||FU 8|||FU 9|||Helical|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010120|||http://purl.uniprot.org/annotation/VAR_055807|||http://purl.uniprot.org/annotation/VAR_055808|||http://purl.uniprot.org/annotation/VAR_055809|||http://purl.uniprot.org/annotation/VAR_055810|||http://purl.uniprot.org/annotation/VAR_055811|||http://purl.uniprot.org/annotation/VAR_055812|||http://purl.uniprot.org/annotation/VAR_055813|||http://purl.uniprot.org/annotation/VAR_055814|||http://purl.uniprot.org/annotation/VAR_055815|||http://purl.uniprot.org/annotation/VAR_055816|||http://purl.uniprot.org/annotation/VAR_055817|||http://purl.uniprot.org/annotation/VAR_055818|||http://purl.uniprot.org/annotation/VAR_069150|||http://purl.uniprot.org/annotation/VAR_069151|||http://purl.uniprot.org/annotation/VAR_069152|||http://purl.uniprot.org/annotation/VAR_069153|||http://purl.uniprot.org/annotation/VSP_011287|||http://purl.uniprot.org/annotation/VSP_011288|||http://purl.uniprot.org/annotation/VSP_011289|||http://purl.uniprot.org/annotation/VSP_011290|||http://purl.uniprot.org/annotation/VSP_011291|||http://purl.uniprot.org/annotation/VSP_011292|||http://purl.uniprot.org/annotation/VSP_011293|||http://purl.uniprot.org/annotation/VSP_011294|||http://purl.uniprot.org/annotation/VSP_011295|||http://purl.uniprot.org/annotation/VSP_011299|||http://purl.uniprot.org/annotation/VSP_046232
http://togogenome.org/gene/9606:H1-7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK96|||http://purl.uniprot.org/uniprot/Q75WM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Testis-specific H1 histone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343414|||http://purl.uniprot.org/annotation/VAR_044371|||http://purl.uniprot.org/annotation/VAR_044372|||http://purl.uniprot.org/annotation/VAR_044373|||http://purl.uniprot.org/annotation/VAR_044374|||http://purl.uniprot.org/annotation/VAR_044375|||http://purl.uniprot.org/annotation/VAR_047359
http://togogenome.org/gene/9606:CHST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LGC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 3|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In SEDCJD.|||In SEDCJD; decreased chondroitin sulfate biosynthetic process.|||In SEDCJD; loss of chondroitin 6-sulfotransferase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085188|||http://purl.uniprot.org/annotation/VAR_021413|||http://purl.uniprot.org/annotation/VAR_021414|||http://purl.uniprot.org/annotation/VAR_021415|||http://purl.uniprot.org/annotation/VAR_047856|||http://purl.uniprot.org/annotation/VAR_047857|||http://purl.uniprot.org/annotation/VAR_047858|||http://purl.uniprot.org/annotation/VAR_047859
http://togogenome.org/gene/9606:MYOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15172                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In CMYP17.|||In CMYP17; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Myoblast determination protein 1|||N6-methyllysine; by EHMT2|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127360|||http://purl.uniprot.org/annotation/VAR_036392|||http://purl.uniprot.org/annotation/VAR_036393|||http://purl.uniprot.org/annotation/VAR_084715|||http://purl.uniprot.org/annotation/VAR_084716
http://togogenome.org/gene/9606:YOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes deubiquitinase activity without affecting interaction with VCP. Specifically blocks a step in the course of dislocation and/or degradation of endoplasmic reticulum-resident proteins destined for proteasomal degradation. Prevents the macroautophagy of damaged lysosome membranes decorated with K48-linked ubiquitin chains.|||C2H2-type|||Cys-loop|||Disordered|||Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-292.|||Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-295.|||His-loop|||In isoform 2.|||Nucleophile|||OTU|||Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-336.|||Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-342.|||S2 site|||UBX-like|||Ubiquitin thioesterase OTU1|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282356|||http://purl.uniprot.org/annotation/VSP_024122
http://togogenome.org/gene/9606:NT5DC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H857                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5'-nucleotidase domain-containing protein 2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247224|||http://purl.uniprot.org/annotation/VAR_034143|||http://purl.uniprot.org/annotation/VSP_019951|||http://purl.uniprot.org/annotation/VSP_019952|||http://purl.uniprot.org/annotation/VSP_019953
http://togogenome.org/gene/9606:GOLPH3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4A5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Beta-hairpin required for oligomerization|||Disordered|||Golgi phosphoprotein 3-like|||In isoform 2.|||Loss of binding to coatomer.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324135|||http://purl.uniprot.org/annotation/VSP_055229
http://togogenome.org/gene/9606:SMARCD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Z9|||http://purl.uniprot.org/uniprot/Q6STE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DM2|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3|||SWIB/MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071988|||http://purl.uniprot.org/annotation/VAR_020884|||http://purl.uniprot.org/annotation/VSP_012498
http://togogenome.org/gene/9606:NOC2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3T9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Nucleolar complex protein 2 homolog|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121048|||http://purl.uniprot.org/annotation/VAR_028145|||http://purl.uniprot.org/annotation/VAR_028146|||http://purl.uniprot.org/annotation/VAR_050289
http://togogenome.org/gene/9606:TMEM121B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Transmembrane protein 121B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089466|||http://purl.uniprot.org/annotation/VSP_045398
http://togogenome.org/gene/9606:CDY2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Chromo|||Disordered|||Polar residues|||Testis-specific chromodomain protein Y 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080220
http://togogenome.org/gene/9606:ABCC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J65                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 12|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253578|||http://purl.uniprot.org/annotation/VAR_028392|||http://purl.uniprot.org/annotation/VAR_028393|||http://purl.uniprot.org/annotation/VAR_028394|||http://purl.uniprot.org/annotation/VAR_028395|||http://purl.uniprot.org/annotation/VAR_028396|||http://purl.uniprot.org/annotation/VAR_028397|||http://purl.uniprot.org/annotation/VAR_028398|||http://purl.uniprot.org/annotation/VAR_028399|||http://purl.uniprot.org/annotation/VAR_028400|||http://purl.uniprot.org/annotation/VAR_048139|||http://purl.uniprot.org/annotation/VAR_048140|||http://purl.uniprot.org/annotation/VSP_021084|||http://purl.uniprot.org/annotation/VSP_021085|||http://purl.uniprot.org/annotation/VSP_021086|||http://purl.uniprot.org/annotation/VSP_021087|||http://purl.uniprot.org/annotation/VSP_021088|||http://purl.uniprot.org/annotation/VSP_021089|||http://purl.uniprot.org/annotation/VSP_021090|||http://purl.uniprot.org/annotation/VSP_021091|||http://purl.uniprot.org/annotation/VSP_021092
http://togogenome.org/gene/9606:FYB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decrease in phosphorylation and interaction with LCP2. Significant decrease in phosphorylation and loss of interaction with LCP2; when associated with F-491.|||Decrease in phosphorylation and interaction with LCP2. Significant decrease in phosphorylation and loss of interaction with LCP2; when associated with F-587.|||Disordered|||FYN-binding protein 2|||In isoform 2.|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2-binding; to LCP2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304583|||http://purl.uniprot.org/annotation/VAR_035041|||http://purl.uniprot.org/annotation/VSP_028031|||http://purl.uniprot.org/annotation/VSP_028032
http://togogenome.org/gene/9606:KCTD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3F6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 3|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||PCNA-binding|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247421|||http://purl.uniprot.org/annotation/VSP_019978|||http://purl.uniprot.org/annotation/VSP_019979|||http://purl.uniprot.org/annotation/VSP_019980
http://togogenome.org/gene/9606:ARL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36404                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 2|||Does not inhibit the interaction with TBCD and rescues the TBCD-induced microtubule destruction.|||Does not inhibit the interaction with TBCD and rescues the TBCD-induced microtubule destruction. Reduces interaction with ARL2BP. Inhibits accumulation of STAT3 in the nucleus.|||Does not reduce interaction with ARL2BP.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In MRCS1; decreased interaction with UNC119; decreased interaction with ARL2BP; changed cellular respiration; decreased ATP production.|||In isoform 2.|||Induces cell cycle arrest, reduces ability to form microtubules and centrosome fragmentation. Inhibits the interaction with TBCD and does not rescue the TBCD-induced microtubule destruction. Interacts with ARL2BP and PDE6D.|||N-myristoyl glycine|||Phosphoserine|||Reduces interaction with ARL2BP.|||Reduces interaction with ARL2BP. Inhibits the interaction with TBCD and rescues the TBCD-induced microtubule destruction.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207453|||http://purl.uniprot.org/annotation/VAR_028056|||http://purl.uniprot.org/annotation/VAR_085165|||http://purl.uniprot.org/annotation/VSP_047278
http://togogenome.org/gene/9606:F13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00488                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cleavage; by thrombin; to produce active factor XIII-A|||Coagulation factor XIII A chain|||Disordered|||Higher specific activity.|||In FA13AD.|||In FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; decreased intracellular protein abundance; decreased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; decreased intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; decreased alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin gamma chain cross-linking activity; decreased rate of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; decreased intracellular protein abundance; loss of protein-glutamine gamma-glutamyltransferase activity; loss of alpha-2-antiplasmin to fibrin cross-linking activity; decreased rate of fibrin gamma chain cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; loss of fibrin alpha chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; mild; no effect on intracellular protein abundance; no effect on protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; no effect on intracellular protein abundance; increased protein-glutamine gamma-glutamyltransferase activity; no effect on alpha-2-antiplasmin to fibrin cross-linking activity; no effect on fibrin alpha chain and gamma chain cross-linking activity; decreased clot fiber thickness.|||In FA13AD; unknown pathological significance.|||In allele F13A*1A, allele F13A*2A and allele F13*(2)A.|||In allele F13A*2A and allele F13A*2B.|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033646|||http://purl.uniprot.org/annotation/PRO_0000033647|||http://purl.uniprot.org/annotation/VAR_007471|||http://purl.uniprot.org/annotation/VAR_007472|||http://purl.uniprot.org/annotation/VAR_007473|||http://purl.uniprot.org/annotation/VAR_007474|||http://purl.uniprot.org/annotation/VAR_013927|||http://purl.uniprot.org/annotation/VAR_013928|||http://purl.uniprot.org/annotation/VAR_013929|||http://purl.uniprot.org/annotation/VAR_020910|||http://purl.uniprot.org/annotation/VAR_020911|||http://purl.uniprot.org/annotation/VAR_060545|||http://purl.uniprot.org/annotation/VAR_074280|||http://purl.uniprot.org/annotation/VAR_074281|||http://purl.uniprot.org/annotation/VAR_074282|||http://purl.uniprot.org/annotation/VAR_074283|||http://purl.uniprot.org/annotation/VAR_074284|||http://purl.uniprot.org/annotation/VAR_074285|||http://purl.uniprot.org/annotation/VAR_074286|||http://purl.uniprot.org/annotation/VAR_074287|||http://purl.uniprot.org/annotation/VAR_074288|||http://purl.uniprot.org/annotation/VAR_074289|||http://purl.uniprot.org/annotation/VAR_074290|||http://purl.uniprot.org/annotation/VAR_074291|||http://purl.uniprot.org/annotation/VAR_077619|||http://purl.uniprot.org/annotation/VAR_077620|||http://purl.uniprot.org/annotation/VAR_077621|||http://purl.uniprot.org/annotation/VAR_077622|||http://purl.uniprot.org/annotation/VAR_077623|||http://purl.uniprot.org/annotation/VAR_077624|||http://purl.uniprot.org/annotation/VAR_077625
http://togogenome.org/gene/9606:MANEAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VSG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glycoprotein endo-alpha-1,2-mannosidase-like protein|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282320|||http://purl.uniprot.org/annotation/VSP_024116|||http://purl.uniprot.org/annotation/VSP_024117|||http://purl.uniprot.org/annotation/VSP_024118|||http://purl.uniprot.org/annotation/VSP_024119
http://togogenome.org/gene/9606:TAF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15544                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Transcription initiation factor TFIID subunit 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118902|||http://purl.uniprot.org/annotation/VAR_016333|||http://purl.uniprot.org/annotation/VAR_052261|||http://purl.uniprot.org/annotation/VSP_044936
http://togogenome.org/gene/9606:KLK15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6B7HBY5|||http://purl.uniprot.org/uniprot/M0R0D7|||http://purl.uniprot.org/uniprot/Q6UBM2|||http://purl.uniprot.org/uniprot/Q9H2R5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kallikrein-15|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027960|||http://purl.uniprot.org/annotation/PRO_0000027961|||http://purl.uniprot.org/annotation/PRO_5010142576|||http://purl.uniprot.org/annotation/PRO_5012994573|||http://purl.uniprot.org/annotation/PRO_5033879268|||http://purl.uniprot.org/annotation/VAR_020179|||http://purl.uniprot.org/annotation/VAR_036298|||http://purl.uniprot.org/annotation/VSP_005404|||http://purl.uniprot.org/annotation/VSP_005405|||http://purl.uniprot.org/annotation/VSP_005406|||http://purl.uniprot.org/annotation/VSP_005407|||http://purl.uniprot.org/annotation/VSP_054621
http://togogenome.org/gene/9606:MUTYH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KP25|||http://purl.uniprot.org/uniprot/E5KP26|||http://purl.uniprot.org/uniprot/E5KP27|||http://purl.uniprot.org/uniprot/E5KP28|||http://purl.uniprot.org/uniprot/E9PM53|||http://purl.uniprot.org/uniprot/Q9UIF7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Adenine DNA glycosylase|||Decreased function in DNA repair.|||Disordered|||Does not affect DNA glycosylase activity.|||Does not affect DNA glycosylase activity; does not affect function in DNA repair.|||Does not affect function in DNA repair.|||Does not affect function.|||Found in a case of sporadic lung cancer; unknown pathological significance; loss of function in DNA repair.|||Found in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair.|||Found in multiple polyposis and sporadic colorectal cancer cases; unknown pathological significance; does not affect DNA glycosylase activity; does not affect function in DNA repair.|||Found in patient with multiple polyposis; unknown pathological significance; does not affect function in DNA repair.|||Found in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair.|||Found in sporadic hepatocellular carcinoma; unknown pathological significance; loss of function in DNA repair.|||In FAP2.|||In FAP2; also found in a case of sporadic colorectal cancer; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair.|||In FAP2; also found in a case of sporadic colorectal cancer; unknown pathological significance; decreased function in DNA repair.|||In FAP2; also found in a patient with multiple polyps; unknown pathological significance; does not affect function in DNA repair.|||In FAP2; also found in multiple polyposis and colorectal cancer cases; loss of DNA glycosylase activity; loss of function in DNA repair.|||In FAP2; also found in multiple polyposis and colorectal cancer cases; loss of function in DNA repair.|||In FAP2; also found in multiple polyposis case; unknown pathological significance; reduced DNA glycosylase activity; no effect on function in DNA repair.|||In FAP2; also found in multiple polyposis cases; loss of DNA glycosylase activity; loss of function in DNA repair.|||In FAP2; also found in multiple polyposis cases; loss of function in DNA repair.|||In FAP2; also found in multiple polyposis cases; unknown pathological significance; does not affect DNA glycosylase activity; slightly decreased function in DNA repair.|||In FAP2; also found in multiple polyposis, colorectal and lung cancer cases; unknown pathological significance; decreased function in DNA repair.|||In FAP2; also found in patient with multiple polyps and in a family with non-polyposis colorectal cancer-like syndrome; unknown pathological significance; does not affect function in DNA repair.|||In FAP2; decreased function in DNA repair.|||In FAP2; found also in sporadic colorectal cancer cases; unknown pathological significance; decreased function in DNA repair.|||In FAP2; loss of DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair.|||In FAP2; loss of DNA glycosylase activity; loss of DNA binding; loss of function in DNA repair.|||In FAP2; loss of DNA glycosylase activity; loss of function in DNA repair.|||In FAP2; loss of function in DNA repair.|||In FAP2; reduced DNA glycosylase activity.|||In FAP2; reduced DNA glycosylase activity; decreased DNA binding; decreased function in DNA repair.|||In FAP2; reduced DNA glycosylase activity; decreased DNA binding; loss of function in DNA repair.|||In FAP2; unknown pathological significance.|||In FAP2; unknown pathological significance; does not affect function in DNA repair.|||In GASC; sporadic; decreased function in DNA repair.|||In GASC; sporadic; unknown pathological significance; does not affect function in DNA repair.|||In isoform Alpha-2 and isoform Gamma-2.|||In isoform Alpha-3 and isoform Gamma-3.|||In isoform Beta-1, isoform Gamma-2 and isoform Gamma-3.|||Likely benign variant; does not affect DNA glycosylase activity.|||Likely benign variant; does not affect DNA glycosylase activity; does not affect function in DNA repair.|||Loss of DNA glycosylase activity.|||Nudix box|||Nudix hydrolase|||Polar residues|||Probable disease-associated variant found in a case of familial colorectal cancer; no significant effect on DNA glycosylase activity; slightly decreased function in DNA repair.|||Probable disease-associated variant found in multiple polyposis cases; decreased function in DNA repair.|||Proton donor/acceptor|||Reduced DNA glycosylase activity; decreased function in DNA repair.|||Transition state stabilizer ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102239|||http://purl.uniprot.org/annotation/VAR_018872|||http://purl.uniprot.org/annotation/VAR_018873|||http://purl.uniprot.org/annotation/VAR_018874|||http://purl.uniprot.org/annotation/VAR_018875|||http://purl.uniprot.org/annotation/VAR_018876|||http://purl.uniprot.org/annotation/VAR_018877|||http://purl.uniprot.org/annotation/VAR_018878|||http://purl.uniprot.org/annotation/VAR_026045|||http://purl.uniprot.org/annotation/VAR_026046|||http://purl.uniprot.org/annotation/VAR_026047|||http://purl.uniprot.org/annotation/VAR_026048|||http://purl.uniprot.org/annotation/VAR_026049|||http://purl.uniprot.org/annotation/VAR_026050|||http://purl.uniprot.org/annotation/VAR_026051|||http://purl.uniprot.org/annotation/VAR_048262|||http://purl.uniprot.org/annotation/VAR_064938|||http://purl.uniprot.org/annotation/VAR_064939|||http://purl.uniprot.org/annotation/VAR_064940|||http://purl.uniprot.org/annotation/VAR_064941|||http://purl.uniprot.org/annotation/VAR_077640|||http://purl.uniprot.org/annotation/VAR_077641|||http://purl.uniprot.org/annotation/VAR_077642|||http://purl.uniprot.org/annotation/VAR_077643|||http://purl.uniprot.org/annotation/VAR_077644|||http://purl.uniprot.org/annotation/VAR_077645|||http://purl.uniprot.org/annotation/VAR_077646|||http://purl.uniprot.org/annotation/VAR_077647|||http://purl.uniprot.org/annotation/VAR_077648|||http://purl.uniprot.org/annotation/VAR_077649|||http://purl.uniprot.org/annotation/VAR_077650|||http://purl.uniprot.org/annotation/VAR_077651|||http://purl.uniprot.org/annotation/VAR_077652|||http://purl.uniprot.org/annotation/VAR_077653|||http://purl.uniprot.org/annotation/VAR_077654|||http://purl.uniprot.org/annotation/VAR_077655|||http://purl.uniprot.org/annotation/VAR_077656|||http://purl.uniprot.org/annotation/VAR_077657|||http://purl.uniprot.org/annotation/VAR_077658|||http://purl.uniprot.org/annotation/VAR_077659|||http://purl.uniprot.org/annotation/VAR_077660|||http://purl.uniprot.org/annotation/VAR_077661|||http://purl.uniprot.org/annotation/VAR_077662|||http://purl.uniprot.org/annotation/VAR_077663|||http://purl.uniprot.org/annotation/VAR_077664|||http://purl.uniprot.org/annotation/VAR_077665|||http://purl.uniprot.org/annotation/VAR_077666|||http://purl.uniprot.org/annotation/VAR_077667|||http://purl.uniprot.org/annotation/VAR_077668|||http://purl.uniprot.org/annotation/VAR_077669|||http://purl.uniprot.org/annotation/VAR_077670|||http://purl.uniprot.org/annotation/VAR_077671|||http://purl.uniprot.org/annotation/VAR_077672|||http://purl.uniprot.org/annotation/VAR_077673|||http://purl.uniprot.org/annotation/VAR_077674|||http://purl.uniprot.org/annotation/VAR_077675|||http://purl.uniprot.org/annotation/VAR_077676|||http://purl.uniprot.org/annotation/VAR_077677|||http://purl.uniprot.org/annotation/VAR_077678|||http://purl.uniprot.org/annotation/VAR_077679|||http://purl.uniprot.org/annotation/VAR_077680|||http://purl.uniprot.org/annotation/VAR_077681|||http://purl.uniprot.org/annotation/VSP_010548|||http://purl.uniprot.org/annotation/VSP_010549|||http://purl.uniprot.org/annotation/VSP_010550
http://togogenome.org/gene/9606:LSM12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MHD2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AD|||In isoform 2.|||N-acetylalanine|||Phosphothreonine|||Protein LSM12|||Removed|||Required for NAADP and TPCN2 binding|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305126|||http://purl.uniprot.org/annotation/VAR_035166|||http://purl.uniprot.org/annotation/VAR_062209|||http://purl.uniprot.org/annotation/VSP_028241
http://togogenome.org/gene/9606:GDPGP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNW5                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  GDP-D-glucose phosphorylase 1|||Tele-GMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336750|||http://purl.uniprot.org/annotation/VAR_043555|||http://purl.uniprot.org/annotation/VAR_043556|||http://purl.uniprot.org/annotation/VAR_043557
http://togogenome.org/gene/9606:NDUFAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5U1|||http://purl.uniprot.org/uniprot/Q8N183                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In MC1DN10.|||In MC1DN10; patient cells homozygous for the variant do not express detectable amounts of protein; complex I assembly is altered and activity is severely reduced in patient cells compared to control.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020054|||http://purl.uniprot.org/annotation/VAR_081422|||http://purl.uniprot.org/annotation/VAR_081423|||http://purl.uniprot.org/annotation/VAR_081424
http://togogenome.org/gene/9606:SLC25A45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR90|||http://purl.uniprot.org/uniprot/Q8N413                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291826|||http://purl.uniprot.org/annotation/VAR_032866|||http://purl.uniprot.org/annotation/VAR_050135|||http://purl.uniprot.org/annotation/VSP_026246|||http://purl.uniprot.org/annotation/VSP_026247|||http://purl.uniprot.org/annotation/VSP_026248
http://togogenome.org/gene/9606:PLAGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPG8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Zinc finger protein PLAGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047223
http://togogenome.org/gene/9606:COMMD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX08                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077401|||http://purl.uniprot.org/annotation/VAR_048814
http://togogenome.org/gene/9606:TRPM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YLN8|||http://purl.uniprot.org/uniprot/Q96QT4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-type protein kinase|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||Loss of kinase activity.|||Mutant channels are functional but show increased susceptibility to inhibition by intracellular magnesium concentrations compared to wild-type channels.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pore-forming|||Probable disease-associated variant found in a patient with hypomagnesemia and secondary hypocalcemia; de novo variant; causes severely reduced Mg(2+) uptake in transfected cells.|||Proton acceptor|||Transient receptor potential cation channel subfamily M member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215331|||http://purl.uniprot.org/annotation/VAR_019967|||http://purl.uniprot.org/annotation/VAR_042395|||http://purl.uniprot.org/annotation/VAR_042396|||http://purl.uniprot.org/annotation/VAR_042397|||http://purl.uniprot.org/annotation/VAR_042398|||http://purl.uniprot.org/annotation/VAR_042399|||http://purl.uniprot.org/annotation/VAR_042400|||http://purl.uniprot.org/annotation/VAR_042401|||http://purl.uniprot.org/annotation/VAR_042402|||http://purl.uniprot.org/annotation/VAR_042403|||http://purl.uniprot.org/annotation/VAR_042404|||http://purl.uniprot.org/annotation/VAR_042405|||http://purl.uniprot.org/annotation/VAR_042406|||http://purl.uniprot.org/annotation/VAR_052381|||http://purl.uniprot.org/annotation/VAR_052382|||http://purl.uniprot.org/annotation/VAR_086707
http://togogenome.org/gene/9606:ATAD3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVI7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 3A|||Decrease in S100B-binding.|||Disordered|||Helical|||In HAYOS.|||In PHRINL.|||In PHRINL; decreased protein levels in patient cells.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of S100B-binding; when associated with S-341.|||Loss of S100B-binding; when associated with S-345.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylserine|||N6-acetyllysine|||No effect on homooligomerization. Immediate fragmentation of the mitochondrial network.|||Phosphoserine|||Removed|||Required for interaction with the inner surface of the mitochondrial outer membrane|||S100B-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084799|||http://purl.uniprot.org/annotation/VAR_023526|||http://purl.uniprot.org/annotation/VAR_055468|||http://purl.uniprot.org/annotation/VAR_082788|||http://purl.uniprot.org/annotation/VAR_082789|||http://purl.uniprot.org/annotation/VAR_083867|||http://purl.uniprot.org/annotation/VAR_083868|||http://purl.uniprot.org/annotation/VAR_083869|||http://purl.uniprot.org/annotation/VSP_015636|||http://purl.uniprot.org/annotation/VSP_044145
http://togogenome.org/gene/9606:TAS2R14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYV8                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082255|||http://purl.uniprot.org/annotation/VAR_053347|||http://purl.uniprot.org/annotation/VAR_062085
http://togogenome.org/gene/9606:SPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13103                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Phosphoserine|||Secreted phosphoprotein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022403|||http://purl.uniprot.org/annotation/VAR_025698
http://togogenome.org/gene/9606:NCAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWD4|||http://purl.uniprot.org/uniprot/P13591                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||GPI-anchor amidated asparagine|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015009|||http://purl.uniprot.org/annotation/PRO_5001831984|||http://purl.uniprot.org/annotation/VAR_049960|||http://purl.uniprot.org/annotation/VAR_049961|||http://purl.uniprot.org/annotation/VAR_049962|||http://purl.uniprot.org/annotation/VAR_061331|||http://purl.uniprot.org/annotation/VSP_034818|||http://purl.uniprot.org/annotation/VSP_034819|||http://purl.uniprot.org/annotation/VSP_034820|||http://purl.uniprot.org/annotation/VSP_034821|||http://purl.uniprot.org/annotation/VSP_034822|||http://purl.uniprot.org/annotation/VSP_034823|||http://purl.uniprot.org/annotation/VSP_034824|||http://purl.uniprot.org/annotation/VSP_034825
http://togogenome.org/gene/9606:HLA-E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4E9D3W4|||http://purl.uniprot.org/uniprot/A8K8M6|||http://purl.uniprot.org/uniprot/O19682|||http://purl.uniprot.org/uniprot/P13747                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the recognition by KLRD1-KLRC1.|||Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Disordered|||Extracellular|||HLA class I histocompatibility antigen, alpha chain E|||Has no impact on the affinity for KLRD1-KLRC1.|||Helical|||Ig-like|||Ig-like C1-type|||Immunoglobulin C1-set|||Impairs folding.|||Impairs the recognition by KLRD1-KLRC1.|||In allele E*01:01.|||In allele E*01:04.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Reduces the affinity for KLRD1-KLRC1.|||Soluble HLA class I histocompatibility antigen, alpha chain E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018882|||http://purl.uniprot.org/annotation/PRO_0000445757|||http://purl.uniprot.org/annotation/PRO_5002725500|||http://purl.uniprot.org/annotation/PRO_5035407262|||http://purl.uniprot.org/annotation/VAR_016651|||http://purl.uniprot.org/annotation/VAR_016652|||http://purl.uniprot.org/annotation/VAR_059510
http://togogenome.org/gene/9606:ZNG1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J3G2|||http://purl.uniprot.org/uniprot/Q8IUF1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  CXCC motif|||CobW C-terminal|||CobW/HypB/UreG nucleotide-binding|||Disordered|||Zinc-regulated GTPase metalloprotein activator 1B|||psi-PxLVp motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316813
http://togogenome.org/gene/9606:DIDO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to H3K4me3.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Death-inducer obliterator 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear localization signal|||Omega-N-methylarginine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||TFIIS central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059324|||http://purl.uniprot.org/annotation/VAR_028310|||http://purl.uniprot.org/annotation/VAR_028311|||http://purl.uniprot.org/annotation/VAR_057093|||http://purl.uniprot.org/annotation/VAR_057094|||http://purl.uniprot.org/annotation/VAR_057095|||http://purl.uniprot.org/annotation/VAR_057096|||http://purl.uniprot.org/annotation/VAR_061740|||http://purl.uniprot.org/annotation/VSP_007209|||http://purl.uniprot.org/annotation/VSP_007210|||http://purl.uniprot.org/annotation/VSP_007211|||http://purl.uniprot.org/annotation/VSP_007212|||http://purl.uniprot.org/annotation/VSP_017225|||http://purl.uniprot.org/annotation/VSP_017226
http://togogenome.org/gene/9606:ENSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43768                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Alpha-endosulfine|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 4, isoform 6 and isoform 9.|||In isoform 3, isoform 7 and isoform 9.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 8.|||Mimicks a phosphorylated state and impairs interaction with SNCA.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by GWL|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146758|||http://purl.uniprot.org/annotation/VSP_001443|||http://purl.uniprot.org/annotation/VSP_037063|||http://purl.uniprot.org/annotation/VSP_037064|||http://purl.uniprot.org/annotation/VSP_037065|||http://purl.uniprot.org/annotation/VSP_037066|||http://purl.uniprot.org/annotation/VSP_037067
http://togogenome.org/gene/9606:PTTG1IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPZ0|||http://purl.uniprot.org/uniprot/P53801                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphotyrosine|||Pituitary tumor-transforming gene 1 protein-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022184|||http://purl.uniprot.org/annotation/PRO_5014567686
http://togogenome.org/gene/9606:FAM156A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDB6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein FAM156A/FAM156B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244468
http://togogenome.org/gene/9606:INO80B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C086                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||HIT-type|||INO80 complex subunit B|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173554|||http://purl.uniprot.org/annotation/VAR_055083
http://togogenome.org/gene/9606:VMAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NL98                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Vimentin-type intermediate filament-associated coiled-coil protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319066
http://togogenome.org/gene/9606:OR1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S0|||http://purl.uniprot.org/uniprot/Q8NH94                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150442|||http://purl.uniprot.org/annotation/VAR_047141|||http://purl.uniprot.org/annotation/VAR_047142|||http://purl.uniprot.org/annotation/VAR_047143|||http://purl.uniprot.org/annotation/VAR_047144
http://togogenome.org/gene/9606:CIRBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6W5Y5|||http://purl.uniprot.org/uniprot/K7EPM4|||http://purl.uniprot.org/uniprot/K7EQR7|||http://purl.uniprot.org/uniprot/Q14011|||http://purl.uniprot.org/uniprot/Q53XX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cold-inducible RNA-binding protein|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081503|||http://purl.uniprot.org/annotation/VSP_056402|||http://purl.uniprot.org/annotation/VSP_056403|||http://purl.uniprot.org/annotation/VSP_056895
http://togogenome.org/gene/9606:ADH1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00326                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alcohol dehydrogenase 1C|||In allele ADH3*2/gamma-2.|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160664|||http://purl.uniprot.org/annotation/VAR_000428|||http://purl.uniprot.org/annotation/VAR_000429|||http://purl.uniprot.org/annotation/VAR_023992|||http://purl.uniprot.org/annotation/VAR_023993|||http://purl.uniprot.org/annotation/VAR_023994
http://togogenome.org/gene/9606:OPN1MW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04001|||http://purl.uniprot.org/uniprot/P0DN77|||http://purl.uniprot.org/uniprot/P0DN78                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CBD and BCM.|||In CBD.|||In COD5; results in protein misfolding and retention in the endoplasmic reticulum.|||Medium-wave-sensitive opsin 1|||Medium-wave-sensitive opsin 2|||Medium-wave-sensitive opsin 3|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Required for 11-cis-retinal regeneration                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197785|||http://purl.uniprot.org/annotation/PRO_0000435400|||http://purl.uniprot.org/annotation/PRO_0000435401|||http://purl.uniprot.org/annotation/VAR_004841|||http://purl.uniprot.org/annotation/VAR_064051|||http://purl.uniprot.org/annotation/VAR_064052|||http://purl.uniprot.org/annotation/VAR_064053
http://togogenome.org/gene/9606:KRT72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||In isoform 3.|||Keratin, type II cytoskeletal 72|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314877|||http://purl.uniprot.org/annotation/VAR_038087|||http://purl.uniprot.org/annotation/VAR_038088|||http://purl.uniprot.org/annotation/VAR_038089|||http://purl.uniprot.org/annotation/VAR_038090|||http://purl.uniprot.org/annotation/VAR_061298|||http://purl.uniprot.org/annotation/VSP_030416|||http://purl.uniprot.org/annotation/VSP_045280
http://togogenome.org/gene/9606:FBXO43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G163                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 43|||Impairs ubiquitination and degradation in response to calcium.|||In OZEMA12 and SPGF64; reduced protein abundance; failed to significantly upregulate CCNB1; the variant does not rescue the mouse knockdown oocyte phenotype compared to wild-type protein.|||In SPGF64; unknown pathological significance.|||Phosphoserine|||Phosphothreonine|||Polar residues|||ZBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247233|||http://purl.uniprot.org/annotation/VAR_061168|||http://purl.uniprot.org/annotation/VAR_061169|||http://purl.uniprot.org/annotation/VAR_086815|||http://purl.uniprot.org/annotation/VAR_086816|||http://purl.uniprot.org/annotation/VAR_086817|||http://purl.uniprot.org/annotation/VAR_086818|||http://purl.uniprot.org/annotation/VAR_086819|||http://purl.uniprot.org/annotation/VAR_086820
http://togogenome.org/gene/9606:NGEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDI2|||http://purl.uniprot.org/uniprot/Q8N5V2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DH|||Disordered|||Ephexin-1|||In isoform 2 and isoform 3.|||In isoform 2.|||PH|||Phosphotyrosine|||Polar residues|||Regulatory region; modulates activity toward RHOA, RAC1 and CDC42|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248388|||http://purl.uniprot.org/annotation/VAR_027289|||http://purl.uniprot.org/annotation/VAR_027290|||http://purl.uniprot.org/annotation/VSP_020259|||http://purl.uniprot.org/annotation/VSP_020260|||http://purl.uniprot.org/annotation/VSP_020261
http://togogenome.org/gene/9606:SPRR2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RM1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA tandem repeats of [PS]-K-C-P-[EQ]-[PS]-C-P-P|||Disordered|||Small proline-rich protein 2F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150012
http://togogenome.org/gene/9606:PCDHA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003892|||http://purl.uniprot.org/annotation/VAR_048526|||http://purl.uniprot.org/annotation/VSP_000679|||http://purl.uniprot.org/annotation/VSP_000680|||http://purl.uniprot.org/annotation/VSP_008704|||http://purl.uniprot.org/annotation/VSP_008705
http://togogenome.org/gene/9606:OR4F5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH21                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 4F5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150547
http://togogenome.org/gene/9606:TALDO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37837                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Confers fructose-6-phosphate aldolase activity.|||In TALDOD.|||In isoform 2.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Schiff-base intermediate with substrate|||Transaldolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173564|||http://purl.uniprot.org/annotation/VAR_011511|||http://purl.uniprot.org/annotation/VAR_086514|||http://purl.uniprot.org/annotation/VSP_061595
http://togogenome.org/gene/9606:MATR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0R4J2E8|||http://purl.uniprot.org/uniprot/B3KM87|||http://purl.uniprot.org/uniprot/B4DF66|||http://purl.uniprot.org/uniprot/P43243|||http://purl.uniprot.org/uniprot/Q9H4N1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In ALS21.|||In ALS21; results in increased interaction with TARDBP.|||In ALS21; unknown pathological significance.|||In isoform 2.|||Matrin-3|||Matrin-type|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081622|||http://purl.uniprot.org/annotation/VAR_063421|||http://purl.uniprot.org/annotation/VAR_071078|||http://purl.uniprot.org/annotation/VAR_071079|||http://purl.uniprot.org/annotation/VAR_071080|||http://purl.uniprot.org/annotation/VAR_074067|||http://purl.uniprot.org/annotation/VAR_074068|||http://purl.uniprot.org/annotation/VAR_074069|||http://purl.uniprot.org/annotation/VAR_074070|||http://purl.uniprot.org/annotation/VAR_078513|||http://purl.uniprot.org/annotation/VSP_042624
http://togogenome.org/gene/9606:RBAK-RBAKDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYG8                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||KRAB                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:C6orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M1T2K5|||http://purl.uniprot.org/uniprot/Q6UXA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C6orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019541|||http://purl.uniprot.org/annotation/PRO_5004017483|||http://purl.uniprot.org/annotation/VAR_022907|||http://purl.uniprot.org/annotation/VAR_022908|||http://purl.uniprot.org/annotation/VAR_022909|||http://purl.uniprot.org/annotation/VAR_022910|||http://purl.uniprot.org/annotation/VAR_028732|||http://purl.uniprot.org/annotation/VAR_028733|||http://purl.uniprot.org/annotation/VAR_028734|||http://purl.uniprot.org/annotation/VAR_050801|||http://purl.uniprot.org/annotation/VAR_050802|||http://purl.uniprot.org/annotation/VAR_054399
http://togogenome.org/gene/9606:CADM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFZ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule 4|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291980|||http://purl.uniprot.org/annotation/VAR_032906
http://togogenome.org/gene/9606:LRCH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C5D9|||http://purl.uniprot.org/uniprot/O75427                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat and calponin homology domain-containing protein 4|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084480|||http://purl.uniprot.org/annotation/VAR_051135
http://togogenome.org/gene/9606:GANAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIW2|||http://purl.uniprot.org/uniprot/B4DSM6|||http://purl.uniprot.org/uniprot/B4DZ53|||http://purl.uniprot.org/uniprot/E9PKU7|||http://purl.uniprot.org/uniprot/F5H6X6|||http://purl.uniprot.org/uniprot/Q14697|||http://purl.uniprot.org/uniprot/V9HWJ0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient affected by polycystic liver disease; unknown pathological significance.|||Found in a patient affected by polycystic liver disease; unknown pathological significance; the patient carried additional PKHD1 variant; the mutation results in significantly reduced alpha-glucosidase activity; dbNP:rs753910059.|||Found in a patient with polycystic liver disease; unknown pathological significance.|||Found in a patient with polycystic liver disease; unknown pathological significance; no apparent effect on the endoplasmic reticulum localization.|||Glycoside hydrolase family 31 N-terminal|||In PKD3; fails to promote PKD1 and PKD2 localization to the cell surface.|||In PKD3; unknown pathological significance; no apparent effect on the endoplasmic reticulum localization.|||In isoform 2.|||In isoform 3.|||Likely benign variant; no effect on PKD1 and PKD2 localization to the cell surface.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||Neutral alpha-glucosidase AB|||No effect on PKD1 and PKD2 localization to the cell surface.|||Nucleophile|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018571|||http://purl.uniprot.org/annotation/PRO_5004776912|||http://purl.uniprot.org/annotation/VAR_022086|||http://purl.uniprot.org/annotation/VAR_024529|||http://purl.uniprot.org/annotation/VAR_050272|||http://purl.uniprot.org/annotation/VAR_077088|||http://purl.uniprot.org/annotation/VAR_077089|||http://purl.uniprot.org/annotation/VAR_077090|||http://purl.uniprot.org/annotation/VAR_077091|||http://purl.uniprot.org/annotation/VAR_077092|||http://purl.uniprot.org/annotation/VAR_080920|||http://purl.uniprot.org/annotation/VAR_080921|||http://purl.uniprot.org/annotation/VAR_080922|||http://purl.uniprot.org/annotation/VAR_085221|||http://purl.uniprot.org/annotation/VAR_085222|||http://purl.uniprot.org/annotation/VAR_085223|||http://purl.uniprot.org/annotation/VAR_085224|||http://purl.uniprot.org/annotation/VSP_010674|||http://purl.uniprot.org/annotation/VSP_039976|||http://purl.uniprot.org/annotation/VSP_039977
http://togogenome.org/gene/9606:CD164L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWJ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD164 sialomucin-like 2 protein|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045779|||http://purl.uniprot.org/annotation/VAR_057508|||http://purl.uniprot.org/annotation/VSP_017031
http://togogenome.org/gene/9606:GADL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQY3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic amino acid decarboxylase GADL1|||In isoform 2.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312224|||http://purl.uniprot.org/annotation/VSP_036227
http://togogenome.org/gene/9606:MARCHF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX47                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase MARCHF5|||Helical|||Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-65.|||Loss of E3 ubiquitin ligase activity. Formation of highly interconnected mitochondria and perinuclear accumulation; when associated with S-68.|||Loss of ubiquitin ligase activity, formation of highly interconnected mitochondria, change in mitochondria morphology that in turns triggers senescence, and perinuclear accumulation.|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271769
http://togogenome.org/gene/9606:S100A7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SG5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Protein S100-A7A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143991|||http://purl.uniprot.org/annotation/VAR_048468|||http://purl.uniprot.org/annotation/VAR_061048
http://togogenome.org/gene/9606:PROB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EW31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Proline-rich basic protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413693
http://togogenome.org/gene/9606:ID4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47928                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  DNA-binding protein inhibitor ID-4|||Disordered|||Pro residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127250
http://togogenome.org/gene/9606:SEC11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YKT4|||http://purl.uniprot.org/uniprot/P67812                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-terminal short (CTS) helix|||Charge relay system|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity.|||Loss of catalytic activity. Slight reduction in protein stability.|||Lumenal|||Moderate reduction in catalytic activity. Reduces protein stability.|||No effect on catalytic activity or protein stability.|||Signal peptidase complex catalytic subunit SEC11A|||Slight reduction in catalytic activity; when associated with D-97.|||Slight reduction in catalytic activity; when associated with R-116.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109543|||http://purl.uniprot.org/annotation/VSP_055052|||http://purl.uniprot.org/annotation/VSP_055053|||http://purl.uniprot.org/annotation/VSP_055054|||http://purl.uniprot.org/annotation/VSP_055055
http://togogenome.org/gene/9606:PARD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEW0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation by AURKA.|||Basic and acidic residues|||Delayed epithelial tight junction assembly.|||Disordered|||In NTD; reduces interaction with PRKCA, disrupts tight junction formation in epithelial cells.|||In NTD; reduces interaction with PRKCA; increases phosphorylation; disrupts tight junction formation in epithelial cells.|||In NTD; unknown pathological significance.|||In isoform 10.|||In isoform 2, isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 5, isoform 6, isoform 7, isoform 9 and isoform 11.|||In isoform 3, isoform 6, isoform 7, isoform 9 and isoform 10.|||In isoform 4, isoform 5 and isoform 7.|||In isoform 5.|||In isoform 8, isoform 9 and isoform 10.|||Interaction with FRMD4A|||Interaction with PRKCI and PRKCZ|||N6-acetyllysine|||PDZ 1|||PDZ 2|||PDZ 3|||Partitioning defective 3 homolog|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185069|||http://purl.uniprot.org/annotation/VAR_015663|||http://purl.uniprot.org/annotation/VAR_050453|||http://purl.uniprot.org/annotation/VAR_079846|||http://purl.uniprot.org/annotation/VAR_079847|||http://purl.uniprot.org/annotation/VAR_079848|||http://purl.uniprot.org/annotation/VSP_007462|||http://purl.uniprot.org/annotation/VSP_007463|||http://purl.uniprot.org/annotation/VSP_007464|||http://purl.uniprot.org/annotation/VSP_007465|||http://purl.uniprot.org/annotation/VSP_007466|||http://purl.uniprot.org/annotation/VSP_007467|||http://purl.uniprot.org/annotation/VSP_007468|||http://purl.uniprot.org/annotation/VSP_007469|||http://purl.uniprot.org/annotation/VSP_007470|||http://purl.uniprot.org/annotation/VSP_007471
http://togogenome.org/gene/9606:PTCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D273|||http://purl.uniprot.org/uniprot/O75127                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||PPR|||PPR 1|||PPR 2|||PPR 3|||PPR 4|||PPR 5|||PPR 6|||PPR 7|||PPR 8|||PPR 9|||Pentacotripeptide-repeat region of PRORP|||Pentatricopeptide repeat-containing protein 1, mitochondrial|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097089|||http://purl.uniprot.org/annotation/VAR_052936|||http://purl.uniprot.org/annotation/VAR_052937
http://togogenome.org/gene/9606:DLX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56178|||http://purl.uniprot.org/uniprot/Q53Y73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DLX-5|||In SHFM1D.|||In isoform 2.|||Phosphoserine; by MAPK14; in vitro|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049031|||http://purl.uniprot.org/annotation/VAR_033874|||http://purl.uniprot.org/annotation/VAR_067413|||http://purl.uniprot.org/annotation/VSP_056884
http://togogenome.org/gene/9606:WDR89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FK6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 89                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254036
http://togogenome.org/gene/9606:BLOC1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78537                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Splice Variant                                                                                  ^@                                                                                  Biogenesis of lysosome-related organelles complex 1 subunit 1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156331|||http://purl.uniprot.org/annotation/VSP_040954
http://togogenome.org/gene/9606:OLFML2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68BL7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Cleavage|||Disordered|||In isoform 2.|||In isoform 3.|||Olfactomedin-like|||Olfactomedin-like protein 2A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311428|||http://purl.uniprot.org/annotation/VAR_037250|||http://purl.uniprot.org/annotation/VAR_037251|||http://purl.uniprot.org/annotation/VSP_029565|||http://purl.uniprot.org/annotation/VSP_029566|||http://purl.uniprot.org/annotation/VSP_029567
http://togogenome.org/gene/9606:KLF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13118                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Krueppel-like factor 10|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047177|||http://purl.uniprot.org/annotation/VAR_052716|||http://purl.uniprot.org/annotation/VSP_042653|||http://purl.uniprot.org/annotation/VSP_047482|||http://purl.uniprot.org/annotation/VSP_047483|||http://purl.uniprot.org/annotation/VSP_047484|||http://purl.uniprot.org/annotation/VSP_047485
http://togogenome.org/gene/9606:SLC6A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48029|||http://purl.uniprot.org/uniprot/Q59EV7|||http://purl.uniprot.org/uniprot/X5D9C4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  65.0% of wild type creatine transporter activity.|||78.0% of wild type creatine transporter activity.|||82.0% of wild type creatine transporter activity.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CCDS1.|||In CCDS1; decreased creatine transporter activity.|||In CCDS1; decreased creatine transporter activity; no effect on cell membrane localization.|||In CCDS1; unknown pathological significance; 35.0% of wild type creatine transporter activity.|||In CCDS1; unknown pathological significance; loss of creatine transporter activity; no effect on cell membrane localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No effect on creatine transporter activity.|||Phosphoserine|||Phosphothreonine|||Sodium- and chloride-dependent creatine transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214774|||http://purl.uniprot.org/annotation/VAR_020525|||http://purl.uniprot.org/annotation/VAR_020526|||http://purl.uniprot.org/annotation/VAR_020527|||http://purl.uniprot.org/annotation/VAR_020528|||http://purl.uniprot.org/annotation/VAR_020529|||http://purl.uniprot.org/annotation/VAR_034483|||http://purl.uniprot.org/annotation/VAR_063707|||http://purl.uniprot.org/annotation/VAR_063708|||http://purl.uniprot.org/annotation/VAR_063709|||http://purl.uniprot.org/annotation/VAR_063710|||http://purl.uniprot.org/annotation/VAR_070563|||http://purl.uniprot.org/annotation/VAR_071791|||http://purl.uniprot.org/annotation/VAR_071792|||http://purl.uniprot.org/annotation/VAR_071793|||http://purl.uniprot.org/annotation/VAR_071794|||http://purl.uniprot.org/annotation/VAR_074262|||http://purl.uniprot.org/annotation/VAR_074263|||http://purl.uniprot.org/annotation/VAR_074264|||http://purl.uniprot.org/annotation/VAR_074265|||http://purl.uniprot.org/annotation/VAR_074266|||http://purl.uniprot.org/annotation/VAR_074267|||http://purl.uniprot.org/annotation/VAR_074268|||http://purl.uniprot.org/annotation/VAR_074269|||http://purl.uniprot.org/annotation/VAR_074270|||http://purl.uniprot.org/annotation/VAR_074271|||http://purl.uniprot.org/annotation/VAR_075562|||http://purl.uniprot.org/annotation/VAR_075563|||http://purl.uniprot.org/annotation/VAR_075564|||http://purl.uniprot.org/annotation/VAR_075565|||http://purl.uniprot.org/annotation/VAR_075566|||http://purl.uniprot.org/annotation/VAR_075567|||http://purl.uniprot.org/annotation/VAR_086684|||http://purl.uniprot.org/annotation/VAR_086685|||http://purl.uniprot.org/annotation/VAR_086686|||http://purl.uniprot.org/annotation/VSP_043916|||http://purl.uniprot.org/annotation/VSP_043917|||http://purl.uniprot.org/annotation/VSP_043918|||http://purl.uniprot.org/annotation/VSP_043919|||http://purl.uniprot.org/annotation/VSP_043920|||http://purl.uniprot.org/annotation/VSP_046316
http://togogenome.org/gene/9606:MYO15A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Actin-binding|||Associated with moderately severe sensorineural hearing loss (DFNB3) in a Smith-Magenis syndrome patient.|||Basic and acidic residues|||Disordered|||FERM|||IQ 1|||IQ 2|||IQ 3|||In DFNB3.|||In DFNB3; Indian family.|||In DFNB3; family from Bengkala.|||In isoform 2.|||MyTH4 1|||MyTH4 2|||Myosin motor|||Neck or regulatory domain|||Polar residues|||Pro residues|||SH3|||Tail|||Unconventional myosin-XV                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123474|||http://purl.uniprot.org/annotation/VAR_010303|||http://purl.uniprot.org/annotation/VAR_010304|||http://purl.uniprot.org/annotation/VAR_037959|||http://purl.uniprot.org/annotation/VAR_037960|||http://purl.uniprot.org/annotation/VAR_037961|||http://purl.uniprot.org/annotation/VAR_037962|||http://purl.uniprot.org/annotation/VAR_037963|||http://purl.uniprot.org/annotation/VAR_037964|||http://purl.uniprot.org/annotation/VAR_071648|||http://purl.uniprot.org/annotation/VSP_056655|||http://purl.uniprot.org/annotation/VSP_056656
http://togogenome.org/gene/9606:C20orf144                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQM9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C20orf144                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079467|||http://purl.uniprot.org/annotation/VAR_050921
http://togogenome.org/gene/9606:TTLL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EMB2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Decreased binding to microtubules and polyglutamylase activity.|||Disordered|||Essential for specifying initiation versus elongation step of the polyglutamylase activity|||In CORD19.|||In isoform 2.|||In isoform 3.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL5|||c-MTBD region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223341|||http://purl.uniprot.org/annotation/VAR_057895|||http://purl.uniprot.org/annotation/VAR_057896|||http://purl.uniprot.org/annotation/VAR_057897|||http://purl.uniprot.org/annotation/VAR_057898|||http://purl.uniprot.org/annotation/VAR_057899|||http://purl.uniprot.org/annotation/VAR_057900|||http://purl.uniprot.org/annotation/VAR_071327|||http://purl.uniprot.org/annotation/VSP_037453|||http://purl.uniprot.org/annotation/VSP_037454|||http://purl.uniprot.org/annotation/VSP_037455|||http://purl.uniprot.org/annotation/VSP_037456|||http://purl.uniprot.org/annotation/VSP_037457
http://togogenome.org/gene/9606:TNFRSF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20333                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Seems to be associated with hyperandrogenism, polycystic ovary syndrome (PCOS) and systemic lupus erythematosus.|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 1b, membrane form|||Tumor necrosis factor-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034548|||http://purl.uniprot.org/annotation/PRO_0000034549|||http://purl.uniprot.org/annotation/VAR_015434|||http://purl.uniprot.org/annotation/VAR_015435|||http://purl.uniprot.org/annotation/VAR_017176|||http://purl.uniprot.org/annotation/VAR_017177|||http://purl.uniprot.org/annotation/VAR_017178|||http://purl.uniprot.org/annotation/VAR_017179|||http://purl.uniprot.org/annotation/VAR_017180|||http://purl.uniprot.org/annotation/VAR_017181|||http://purl.uniprot.org/annotation/VSP_011826|||http://purl.uniprot.org/annotation/VSP_011827
http://togogenome.org/gene/9606:EPS8L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6S3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Epidermal growth factor receptor kinase substrate 8-like protein 2|||In isoform 2.|||In isoform 3.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239084|||http://purl.uniprot.org/annotation/VSP_019092|||http://purl.uniprot.org/annotation/VSP_054144
http://togogenome.org/gene/9606:ARFGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP61                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosylation factor GTPase-activating protein 3|||Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074193|||http://purl.uniprot.org/annotation/VAR_013447|||http://purl.uniprot.org/annotation/VAR_036177|||http://purl.uniprot.org/annotation/VAR_055523|||http://purl.uniprot.org/annotation/VAR_055524|||http://purl.uniprot.org/annotation/VAR_055525|||http://purl.uniprot.org/annotation/VAR_055526|||http://purl.uniprot.org/annotation/VAR_055527|||http://purl.uniprot.org/annotation/VSP_046888
http://togogenome.org/gene/9606:PDX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52945                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Nuclear localization signal|||Pancreas/duodenum homeobox protein 1|||Phosphoserine; by HIPK2|||Phosphothreonine; by PASK|||Pro residues|||Risk factor for type 2 diabetes.|||Transactivation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049147|||http://purl.uniprot.org/annotation/VAR_009309|||http://purl.uniprot.org/annotation/VAR_009310|||http://purl.uniprot.org/annotation/VAR_009311|||http://purl.uniprot.org/annotation/VAR_009312|||http://purl.uniprot.org/annotation/VAR_009313
http://togogenome.org/gene/9606:ZNF468                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VIY5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 468                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280412|||http://purl.uniprot.org/annotation/VAR_031141|||http://purl.uniprot.org/annotation/VAR_031142|||http://purl.uniprot.org/annotation/VSP_023659
http://togogenome.org/gene/9606:SUSD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVN2|||http://purl.uniprot.org/uniprot/Q96L08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi|||Sushi domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251973|||http://purl.uniprot.org/annotation/VAR_027744|||http://purl.uniprot.org/annotation/VAR_035663|||http://purl.uniprot.org/annotation/VSP_020833|||http://purl.uniprot.org/annotation/VSP_020834
http://togogenome.org/gene/9606:HSP90AB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGL0|||http://purl.uniprot.org/uniprot/P08238|||http://purl.uniprot.org/uniprot/Q6PK50                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleaved under oxidative stress|||Decreases interaction with NOS3 and SRC. impairs resists LPS-induced tyrosine phosphorylation. Does not block LPS-induced pp60src phosphorylation.|||Decreases the signal of SMYD2-dependent HSP90AB1 methylation. Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-531. Diminishes dimerized form; when associated with A-531. Reduces interaction with STIP1 or CDC37; when associated with A-531.|||Disordered|||Heat shock protein HSP 90-beta|||Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-574. Diminishes dimerized form; when associated with A-574. Reduces interaction with STIP1 or CDC37; when associated with A-574.|||Histidine kinase/HSP90-like ATPase|||Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2.|||Increases the binding affinity for AHR; when associated with A-226. Increases AHR transcription activity; when associated with A-226.|||Increases the binding affinity for AHR; when associated with A-255. Increases AHR transcription activity; when associated with A-255.|||Interaction with AHSA1|||Interaction with BIRC2|||Interaction with NR1D1|||Interaction with NR3C1|||Interaction with TP53|||N6-acetyllysine|||N6-malonyllysine|||N6-methylated lysine|||N6-methylated lysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on the interaction with AHR; when associated with E-226.|||No effect on the interaction with AHR; when associated with E-255.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by PLK2 and PLK3|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Reduced ATPase activity and client protein activation.|||Removed|||S-nitrosocysteine|||Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2.|||TPR repeat-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000062917|||http://purl.uniprot.org/annotation/VAR_049624
http://togogenome.org/gene/9606:MAP2K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4QPA9|||http://purl.uniprot.org/uniprot/B4DFY5|||http://purl.uniprot.org/uniprot/Q02750                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by anthrax lethal factor|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 1|||In CFC3.|||In MEL; somatic mutation.|||In MEL; somatic mutation; results in increased MAPK signal transduction.|||In isoform 2.|||Increases interaction with KSR1 and BRAF.|||Increases interaction with KSR1 and BRAF; when associated with L-220.|||Increases interaction with KSR1 and BRAF; when associated with w-219.|||Loss of catalytic activity. No effect on BRAF-KSR1 dimerization; when associated with A-218.|||Loss of catalytic activity. No effect on BRAF-KSR1 dimerization; when associated with A-222.|||Loss of catalytic activity. No effect on BRAF-KSR1 or BRAF-KSR2 dimerization.|||Loss of catalytic activity. Strongly reduces phosphorylation upon UV irradiation.|||Loss of interaction with BRAF and KSR1. Loss of BRAF-KSR1 dimerization.|||No effect on BRAF-KSR1 dimerization; when associated with D-218.|||No effect on BRAF-KSR1 dimerization; when associated with D-222.|||No loss of activity.|||Phosphoserine; by BRAF and RAF1|||Phosphoserine; by PAK|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Protein kinase|||Proton acceptor|||RAF1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086365|||http://purl.uniprot.org/annotation/VAR_035093|||http://purl.uniprot.org/annotation/VAR_035094|||http://purl.uniprot.org/annotation/VAR_069780|||http://purl.uniprot.org/annotation/VAR_084452|||http://purl.uniprot.org/annotation/VAR_084453|||http://purl.uniprot.org/annotation/VAR_084454|||http://purl.uniprot.org/annotation/VSP_040500
http://togogenome.org/gene/9606:GNAI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63096                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||Abolishes switch to an activated conformation and dissociation from beta and gamma subunits upon GTP binding. Abolishes interaction with RGS family members.|||Deamidated glutamine; by Photorhabdus PAU_02230|||Enhances interaction (inactive GDP-bound) with RGS14.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-1|||In NEDHISB.|||In NEDHISB; loss of GTP binding.|||In NEDHISB; unknown pathological significance.|||In isoform 2.|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203671|||http://purl.uniprot.org/annotation/VAR_087204|||http://purl.uniprot.org/annotation/VAR_087205|||http://purl.uniprot.org/annotation/VAR_087206|||http://purl.uniprot.org/annotation/VAR_087207|||http://purl.uniprot.org/annotation/VAR_087208|||http://purl.uniprot.org/annotation/VAR_087209|||http://purl.uniprot.org/annotation/VAR_087210|||http://purl.uniprot.org/annotation/VAR_087211|||http://purl.uniprot.org/annotation/VAR_087212|||http://purl.uniprot.org/annotation/VAR_087213|||http://purl.uniprot.org/annotation/VAR_087214|||http://purl.uniprot.org/annotation/VAR_087215|||http://purl.uniprot.org/annotation/VAR_087216|||http://purl.uniprot.org/annotation/VAR_087217|||http://purl.uniprot.org/annotation/VAR_087218|||http://purl.uniprot.org/annotation/VAR_087219|||http://purl.uniprot.org/annotation/VSP_045215
http://togogenome.org/gene/9606:RAET1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6H3X3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GPI-anchor amidated glycine|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||MHC class I alpha-1 like|||MHC class I alpha-2 like|||N-linked (GlcNAc...) asparagine|||Reduced cell surface expression.|||Removed in mature form|||UL-16 binding protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019022|||http://purl.uniprot.org/annotation/PRO_0000429932|||http://purl.uniprot.org/annotation/VAR_033449|||http://purl.uniprot.org/annotation/VSP_051621|||http://purl.uniprot.org/annotation/VSP_051622|||http://purl.uniprot.org/annotation/VSP_059264
http://togogenome.org/gene/9606:RPS27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42677                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Disordered|||Phosphoserine|||Removed|||Small ribosomal subunit protein eS27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149051
http://togogenome.org/gene/9606:AVPI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T686                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Arginine vasopressin-induced protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282402|||http://purl.uniprot.org/annotation/VAR_031405
http://togogenome.org/gene/9606:RPS3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3M5|||http://purl.uniprot.org/uniprot/P61247                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyltyrosine|||Decreased ADP-ribosylation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Removed|||Small ribosomal subunit protein eS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153524
http://togogenome.org/gene/9606:MYL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10916|||http://purl.uniprot.org/uniprot/Q6IB42                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Deamidated asparagine|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In CMH10.|||In CMH10; decrease calcium binding affinity.|||In CMH10; impairs calcium binding; bind calcium upon phosphorylation.|||In CMH10; some patients present with mid-left ventricular chamber thickening; significantly decrease calcium binding affinity; loss of phosphorylation.|||In CMH10; with mid-left ventricular chamber thickening; decrease calcium binding affinity.|||In CMH10; with mid-left ventricular chamber thickening; decrease calcium binding affinity; large increase in its calcium binding affinity upon phosphorylation.|||Myosin regulatory light chain 2, ventricular/cardiac muscle isoform|||N,N,N-trimethylalanine|||Phosphoserine|||Phosphoserine; by ZIPK/DAPK3|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198727|||http://purl.uniprot.org/annotation/VAR_004601|||http://purl.uniprot.org/annotation/VAR_004602|||http://purl.uniprot.org/annotation/VAR_004603|||http://purl.uniprot.org/annotation/VAR_004604|||http://purl.uniprot.org/annotation/VAR_004605|||http://purl.uniprot.org/annotation/VAR_019844|||http://purl.uniprot.org/annotation/VAR_029449
http://togogenome.org/gene/9606:TMPRSS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-1|||1-10|||1-11|||1-12|||1-2|||1-3|||1-4|||1-5|||1-6|||1-7|||1-8|||1-9; approximate|||13 X 5 AA repeats of A-S-P-A-[GLQR]|||2-1; approximate|||2-2|||2-3|||2-4|||4 X 5 AA repeats of T-P-P-G-R|||Abolishes autocleavage. Abolishes PRSS8 cleavage and activation. Increases localization to the cell surface. No effect on glycosylation.|||Abolishes autocleavage. Abolishes serine protease activity including PRSS8 cleavage and activation. Increases localization to the cell surface. No effect on glycosylation.|||Charge relay system|||Cleavage; by autolysis; required for cell surface localization and secretion|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||LDL-receptor class A|||Loss of localization to the cell surface even in the presence of the inhibitor SPINT2. Reduces PRSS8 cleavage and activation. No effect on interaction with SPINT2.|||N-linked (GlcNAc...) asparagine|||No effect on autocleavage.|||No effect on autocleavage. No effect on PRSS8 cleavage and activation.|||Peptidase S1|||Polar residues|||Reduces autocleavage. Loss of localization to the cell surface even in the presence of the inhibitor SPINT2. Reduces PRSS8 cleavage and activation. No effect on interaction with SPINT2.|||Required for autocleavage and PRSS8 cleavage|||SRCR|||Significantly reduces autocleavage and cleavage of substrates. Abolishes phosphorylation when inhibited by SPINT2/HAI-2, also reduces localization to the cell surface and is instead localized to the endoplasmic reticulum.|||Transmembrane protease serine 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088698|||http://purl.uniprot.org/annotation/VAR_081354|||http://purl.uniprot.org/annotation/VAR_081355|||http://purl.uniprot.org/annotation/VSP_013099|||http://purl.uniprot.org/annotation/VSP_013100|||http://purl.uniprot.org/annotation/VSP_013101|||http://purl.uniprot.org/annotation/VSP_013102|||http://purl.uniprot.org/annotation/VSP_013103|||http://purl.uniprot.org/annotation/VSP_013104
http://togogenome.org/gene/9606:AMY2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19961                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Modified Residue|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Alpha-amylase 2B|||In isoform 2.|||Nucleophile|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001402|||http://purl.uniprot.org/annotation/VSP_056932|||http://purl.uniprot.org/annotation/VSP_056933
http://togogenome.org/gene/9606:SAR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6B6                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  GTP-binding protein SAR1b|||In CMRD.|||In CMRD; loss of GDP/GTP-binding.|||In CMRD; reduced affinity for GDP/GTP.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206261|||http://purl.uniprot.org/annotation/VAR_016806|||http://purl.uniprot.org/annotation/VAR_016807|||http://purl.uniprot.org/annotation/VAR_016808|||http://purl.uniprot.org/annotation/VAR_059051|||http://purl.uniprot.org/annotation/VAR_059052
http://togogenome.org/gene/9606:ARHGAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98171                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||F-BAR|||In isoform 2.|||Phosphoserine|||Rho GTPase-activating protein 4|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056701|||http://purl.uniprot.org/annotation/VAR_028413|||http://purl.uniprot.org/annotation/VSP_042902
http://togogenome.org/gene/9606:HECTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV18|||http://purl.uniprot.org/uniprot/B4DIQ2|||http://purl.uniprot.org/uniprot/Q5U5R9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Phosphoserine|||Probable E3 ubiquitin-protein ligase HECTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240851|||http://purl.uniprot.org/annotation/VAR_026836|||http://purl.uniprot.org/annotation/VSP_044965|||http://purl.uniprot.org/annotation/VSP_044966
http://togogenome.org/gene/9606:A2ML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2U0|||http://purl.uniprot.org/uniprot/B3KVV6                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-2-macroglobulin|||Alpha-2-macroglobulin bait region|||Alpha-2-macroglobulin-like protein 1|||Alpha-macroglobulin receptor-binding|||Bait region|||In isoform 2.|||Isoglutamyl cysteine thioester (Cys-Gln)|||May be a risk factor for otitis media.|||N-linked (GlcNAc...) asparagine|||Risk factor for otitis media.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318074|||http://purl.uniprot.org/annotation/VAR_055463|||http://purl.uniprot.org/annotation/VAR_055464|||http://purl.uniprot.org/annotation/VAR_055465|||http://purl.uniprot.org/annotation/VAR_055466|||http://purl.uniprot.org/annotation/VAR_059083|||http://purl.uniprot.org/annotation/VAR_059084|||http://purl.uniprot.org/annotation/VAR_071854|||http://purl.uniprot.org/annotation/VAR_071855|||http://purl.uniprot.org/annotation/VAR_071856|||http://purl.uniprot.org/annotation/VAR_081009|||http://purl.uniprot.org/annotation/VAR_081010|||http://purl.uniprot.org/annotation/VAR_081011|||http://purl.uniprot.org/annotation/VAR_081012|||http://purl.uniprot.org/annotation/VAR_081013|||http://purl.uniprot.org/annotation/VAR_081014|||http://purl.uniprot.org/annotation/VAR_081015|||http://purl.uniprot.org/annotation/VSP_057135
http://togogenome.org/gene/9606:DEFB135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KP9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 135                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045362
http://togogenome.org/gene/9606:OXTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9L7|||http://purl.uniprot.org/uniprot/P30559                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Oxytocin receptor|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069998|||http://purl.uniprot.org/annotation/VAR_031570|||http://purl.uniprot.org/annotation/VAR_031571
http://togogenome.org/gene/9606:GPHB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RPU1|||http://purl.uniprot.org/uniprot/Q86YW7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Glycoprotein hormone beta-5|||Glycoprotein hormone subunit beta|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011761|||http://purl.uniprot.org/annotation/PRO_5014227021
http://togogenome.org/gene/9606:PLCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXT2|||http://purl.uniprot.org/uniprot/B7ZM61|||http://purl.uniprot.org/uniprot/Q9P212                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1|||Abolishes interaction with HRAS.|||Basic and acidic residues|||C2|||Decreases 17.5-fold the affinity for HRAS.|||Disordered|||In NPHS3.|||In NPHS3; gives rise to focal segmental glomerulosclerosis rather than diffuse mesangial sclerosis.|||In isoform 2.|||Increases 1.4-fold the affinity for HRAS.|||Increases 2.8-fold the affinity for HRAS.|||Loss of the phospholipase C enzymatic activity. Still activates HRAS and the MAP kinase pathway.|||No effect on HRAS-binding.|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues|||Ras-GEF|||Ras-associating|||Ras-associating 1|||Ras-associating 2|||Reduces HRAS-binding.|||Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256238|||http://purl.uniprot.org/annotation/VAR_029883|||http://purl.uniprot.org/annotation/VAR_031843|||http://purl.uniprot.org/annotation/VAR_031844|||http://purl.uniprot.org/annotation/VAR_031845|||http://purl.uniprot.org/annotation/VAR_031846|||http://purl.uniprot.org/annotation/VAR_031847|||http://purl.uniprot.org/annotation/VAR_087600|||http://purl.uniprot.org/annotation/VAR_087601|||http://purl.uniprot.org/annotation/VSP_021335|||http://purl.uniprot.org/annotation/VSP_021336
http://togogenome.org/gene/9606:POLR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95602                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bridging helix|||DNA-directed RNA polymerase I subunit RPA1|||Disordered|||In AFDCIN.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073923|||http://purl.uniprot.org/annotation/VAR_047493|||http://purl.uniprot.org/annotation/VAR_047494|||http://purl.uniprot.org/annotation/VAR_047495|||http://purl.uniprot.org/annotation/VAR_047496|||http://purl.uniprot.org/annotation/VAR_047497|||http://purl.uniprot.org/annotation/VAR_047498|||http://purl.uniprot.org/annotation/VAR_047499|||http://purl.uniprot.org/annotation/VAR_073964|||http://purl.uniprot.org/annotation/VAR_073965
http://togogenome.org/gene/9606:METTL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1A3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protein-L-histidine N-pros-methyltransferase activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein-L-histidine N-pros-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317490|||http://purl.uniprot.org/annotation/VSP_030997
http://togogenome.org/gene/9606:WRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14191                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X 27 AA tandem repeats of H-L-S-P-N-D-N-E-N-D-T-S-Y-V-I-E-S-D-E-D-L-E-M-E-M-L-K|||3'-5' exonuclease|||Abolished interaction with XRCC5 and XRCC6.|||Abolishes exonuclease activity.|||Acidic residues|||Associated with a higher risk of myocardial infarction.|||Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HRDC|||Helicase ATP-binding|||Helicase C-terminal|||In WRN.|||In a colorectal cancer sample; somatic mutation.|||Interaction with DNA|||Interaction with WRNIP1|||KBM 1|||KBM 2|||Loss of DNA binding.|||N-acetylserine|||No effect on exonuclease activity.|||Phosphoserine|||Reduces affinity for DNA about 20-fold. Loss of DNA binding; when associated with A-987.|||Reduces affinity for DNA about 4-fold.|||Reduces affinity for DNA about 8-fold.|||Reduces affinity for DNA about 8-fold. Loss of DNA binding; when associated with A-993.|||Reduces exonuclease activity.|||Removed|||Strongly reduces exonuclease activity.|||XLM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205045|||http://purl.uniprot.org/annotation/VAR_006904|||http://purl.uniprot.org/annotation/VAR_006905|||http://purl.uniprot.org/annotation/VAR_006906|||http://purl.uniprot.org/annotation/VAR_007903|||http://purl.uniprot.org/annotation/VAR_014913|||http://purl.uniprot.org/annotation/VAR_014914|||http://purl.uniprot.org/annotation/VAR_017453|||http://purl.uniprot.org/annotation/VAR_017454|||http://purl.uniprot.org/annotation/VAR_017455|||http://purl.uniprot.org/annotation/VAR_017456|||http://purl.uniprot.org/annotation/VAR_017457|||http://purl.uniprot.org/annotation/VAR_017458|||http://purl.uniprot.org/annotation/VAR_017459|||http://purl.uniprot.org/annotation/VAR_018941|||http://purl.uniprot.org/annotation/VAR_018942|||http://purl.uniprot.org/annotation/VAR_018943|||http://purl.uniprot.org/annotation/VAR_018944|||http://purl.uniprot.org/annotation/VAR_018945|||http://purl.uniprot.org/annotation/VAR_018946|||http://purl.uniprot.org/annotation/VAR_018947|||http://purl.uniprot.org/annotation/VAR_020450|||http://purl.uniprot.org/annotation/VAR_020451|||http://purl.uniprot.org/annotation/VAR_026588|||http://purl.uniprot.org/annotation/VAR_026589|||http://purl.uniprot.org/annotation/VAR_036318|||http://purl.uniprot.org/annotation/VAR_054162|||http://purl.uniprot.org/annotation/VAR_057124
http://togogenome.org/gene/9606:BCKDK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14874                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Histidine kinase|||In BCKDKD.|||In BCKDKD; complete loss of kinase activity.|||In BCKDKD; partial loss of kinase activity.|||In isoform 2 and isoform 3.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by autocatalysis|||[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023452|||http://purl.uniprot.org/annotation/VAR_069037|||http://purl.uniprot.org/annotation/VAR_072184|||http://purl.uniprot.org/annotation/VAR_072185|||http://purl.uniprot.org/annotation/VSP_054604|||http://purl.uniprot.org/annotation/VSP_054605
http://togogenome.org/gene/9606:SOCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14508                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Increased protein half-life.|||Increased protein half-life; reduced interaction with AREL1.|||Interaction with AREL1|||No effect on protein half-life.|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181238|||http://purl.uniprot.org/annotation/VAR_052032
http://togogenome.org/gene/9606:POLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMQ1|||http://purl.uniprot.org/uniprot/P09884                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cleavage|||CysA-type|||CysB motif|||DNA polymerase alpha catalytic subunit|||DNA polymerase alpha catalytic subunit N-terminal|||DNA-binding|||DNA-directed DNA polymerase family B exonuclease|||DNA-directed DNA polymerase family B multifunctional|||Disordered|||In VEODS; decreased protein abundance; may alter splicing.|||In VEODS; no effect on protein abundance; decreased DNA replication.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Zinc finger DNA-directed DNA polymerase family B alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046428|||http://purl.uniprot.org/annotation/VAR_048877|||http://purl.uniprot.org/annotation/VAR_083194|||http://purl.uniprot.org/annotation/VAR_083195|||http://purl.uniprot.org/annotation/VAR_083196
http://togogenome.org/gene/9606:CARD19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LW7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes the NF-kappa-B inhibitory activity.|||CARD|||Caspase recruitment domain-containing protein 19|||In isoform 2.|||Phosphoserine|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064927|||http://purl.uniprot.org/annotation/VSP_014723
http://togogenome.org/gene/9606:TMEM38A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6F2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical;Name=1|||Helical;Name=2|||Helical;Name=3|||Helical;Name=4|||Helical;Name=5|||Helical;Name=6|||Helical;Name=7|||Lumenal|||Trimeric intracellular cation channel type A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271068
http://togogenome.org/gene/9606:TRIM49B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Putative tripartite motif-containing protein 49B|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328997|||http://purl.uniprot.org/annotation/VAR_042601
http://togogenome.org/gene/9606:ESD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ2|||http://purl.uniprot.org/uniprot/P10768                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1.3% of wild-type activity.|||3% of wild-type activity.|||4.3% of wild-type activity.|||62% increase in activity.|||83% of wild-type activity.|||9% of wild-type activity.|||Charge relay system|||In allele ESD*2.|||Loss of activity.|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Removed|||S-formylglutathione hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210339|||http://purl.uniprot.org/annotation/VAR_005202|||http://purl.uniprot.org/annotation/VAR_022275
http://togogenome.org/gene/9606:ZNF85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03923|||http://purl.uniprot.org/uniprot/Q49A12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 85                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047398|||http://purl.uniprot.org/annotation/VAR_033552|||http://purl.uniprot.org/annotation/VAR_033553|||http://purl.uniprot.org/annotation/VAR_033554|||http://purl.uniprot.org/annotation/VAR_047515|||http://purl.uniprot.org/annotation/VAR_061932|||http://purl.uniprot.org/annotation/VAR_061933|||http://purl.uniprot.org/annotation/VAR_061934|||http://purl.uniprot.org/annotation/VSP_035771|||http://purl.uniprot.org/annotation/VSP_042154|||http://purl.uniprot.org/annotation/VSP_042155
http://togogenome.org/gene/9606:CCDC61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6R9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein CCDC61|||Disordered|||Head domain|||In isoform 2.|||Loss of dimerization.|||Loss of microtubule-binding; when associated with E-259, E-263, E-266 and E-268.|||Loss of microtubule-binding; when associated with E-259, E-263, E-266 and E-270.|||Loss of microtubule-binding; when associated with E-259, E-263, E-268 and E-270.|||Loss of microtubule-binding; when associated with E-259, E-266, E-268 and E-270.|||Loss of microtubule-binding; when associated with E-263, E-266, E-268 and E-270.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311255|||http://purl.uniprot.org/annotation/VSP_053741
http://togogenome.org/gene/9606:TCEA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTX4|||http://purl.uniprot.org/uniprot/B7Z4W0|||http://purl.uniprot.org/uniprot/P23193                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||TFIIS N-terminal|||TFIIS central|||TFIIS-type|||Transcription elongation factor A protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121446|||http://purl.uniprot.org/annotation/VSP_006409
http://togogenome.org/gene/9606:DNAJC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75937                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||DnaJ homolog subfamily C member 8|||Essential for polyglutamine aggregation suppression|||J|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071060
http://togogenome.org/gene/9606:NFE2L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4A8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||Leucine-zipper|||Nuclear factor erythroid 2-related factor 3|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076452|||http://purl.uniprot.org/annotation/VAR_055562
http://togogenome.org/gene/9606:IL4I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolished L-amino-acid oxidase activity.|||Disordered|||In an ovarian cancer; decreased L-amino-acid oxidase activity.|||In isoform 2.|||Increased L-amino-acid oxidase activity.|||L-amino-acid oxidase|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001710|||http://purl.uniprot.org/annotation/VAR_048260|||http://purl.uniprot.org/annotation/VAR_083941|||http://purl.uniprot.org/annotation/VAR_083942|||http://purl.uniprot.org/annotation/VSP_017173
http://togogenome.org/gene/9606:IPO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT38|||http://purl.uniprot.org/uniprot/Q8TEX9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||Importin N-terminal|||Importin-4|||In isoform 2.|||N-acetylmethionine|||TOG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120748|||http://purl.uniprot.org/annotation/VAR_030758|||http://purl.uniprot.org/annotation/VAR_030759|||http://purl.uniprot.org/annotation/VSP_009339
http://togogenome.org/gene/9606:HRNR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YZ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Hornerin|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||S-100-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144038|||http://purl.uniprot.org/annotation/VAR_048494|||http://purl.uniprot.org/annotation/VAR_048495|||http://purl.uniprot.org/annotation/VAR_048496|||http://purl.uniprot.org/annotation/VAR_048497|||http://purl.uniprot.org/annotation/VAR_048498|||http://purl.uniprot.org/annotation/VAR_048499|||http://purl.uniprot.org/annotation/VAR_059174|||http://purl.uniprot.org/annotation/VAR_059175|||http://purl.uniprot.org/annotation/VAR_059176|||http://purl.uniprot.org/annotation/VAR_061053|||http://purl.uniprot.org/annotation/VAR_061054|||http://purl.uniprot.org/annotation/VAR_061055|||http://purl.uniprot.org/annotation/VAR_061056
http://togogenome.org/gene/9606:TCP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAT8|||http://purl.uniprot.org/uniprot/Q8WWU5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||T-complex protein 11 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324298|||http://purl.uniprot.org/annotation/VAR_039692|||http://purl.uniprot.org/annotation/VAR_039693|||http://purl.uniprot.org/annotation/VSP_032185|||http://purl.uniprot.org/annotation/VSP_032186|||http://purl.uniprot.org/annotation/VSP_045217|||http://purl.uniprot.org/annotation/VSP_047124|||http://purl.uniprot.org/annotation/VSP_047125|||http://purl.uniprot.org/annotation/VSP_047126
http://togogenome.org/gene/9606:ADISSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Adipose-secreted signaling protein|||In isoform 2.|||N-acetylalanine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079419|||http://purl.uniprot.org/annotation/VSP_040293
http://togogenome.org/gene/9606:SCNN1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R812|||http://purl.uniprot.org/uniprot/P51168                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amiloride-sensitive sodium channel subunit beta|||Associated with hypertension in South African Black.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||In BESC1.|||In BESC1; decreased channel activity.|||In BESC1; increased channel activity.|||In LIDLS1.|||In LIDLS1; constitutive channel activation.|||In PHA1B2.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181268|||http://purl.uniprot.org/annotation/VAR_007127|||http://purl.uniprot.org/annotation/VAR_007128|||http://purl.uniprot.org/annotation/VAR_007129|||http://purl.uniprot.org/annotation/VAR_014891|||http://purl.uniprot.org/annotation/VAR_014892|||http://purl.uniprot.org/annotation/VAR_015836|||http://purl.uniprot.org/annotation/VAR_015837|||http://purl.uniprot.org/annotation/VAR_015838|||http://purl.uniprot.org/annotation/VAR_015839|||http://purl.uniprot.org/annotation/VAR_015840|||http://purl.uniprot.org/annotation/VAR_015841|||http://purl.uniprot.org/annotation/VAR_026519|||http://purl.uniprot.org/annotation/VAR_026520|||http://purl.uniprot.org/annotation/VAR_026521|||http://purl.uniprot.org/annotation/VAR_026522|||http://purl.uniprot.org/annotation/VAR_036480|||http://purl.uniprot.org/annotation/VAR_036481|||http://purl.uniprot.org/annotation/VAR_036482|||http://purl.uniprot.org/annotation/VAR_062401|||http://purl.uniprot.org/annotation/VAR_062402|||http://purl.uniprot.org/annotation/VAR_062403|||http://purl.uniprot.org/annotation/VAR_062404|||http://purl.uniprot.org/annotation/VAR_062405|||http://purl.uniprot.org/annotation/VAR_062406|||http://purl.uniprot.org/annotation/VAR_062407|||http://purl.uniprot.org/annotation/VSP_007724
http://togogenome.org/gene/9606:PAGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75459                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||P antigen family member 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148347|||http://purl.uniprot.org/annotation/VAR_027767
http://togogenome.org/gene/9606:KRTAP9-9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYP9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 5 AA repeats of C-C-[RQVGE]-[SPSTNQ]-[TASL]|||2|||3|||4|||5|||6|||7|||8|||9|||In isoform 2 and isoform 3.|||In isoform 3.|||Keratin-associated protein 9-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185193|||http://purl.uniprot.org/annotation/VAR_060047|||http://purl.uniprot.org/annotation/VAR_060048|||http://purl.uniprot.org/annotation/VSP_028981|||http://purl.uniprot.org/annotation/VSP_054315
http://togogenome.org/gene/9606:OR56A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWL6|||http://purl.uniprot.org/uniprot/Q8NH54                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 56A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150794|||http://purl.uniprot.org/annotation/VAR_024152
http://togogenome.org/gene/9606:LCORL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSW0|||http://purl.uniprot.org/uniprot/Q8N3X6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH psq-type|||In isoform 2.|||In isoform 3.|||Ligand-dependent nuclear receptor corepressor-like protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310463|||http://purl.uniprot.org/annotation/VSP_029287|||http://purl.uniprot.org/annotation/VSP_029288|||http://purl.uniprot.org/annotation/VSP_029289
http://togogenome.org/gene/9606:SORBS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTX5|||http://purl.uniprot.org/uniprot/Q9BX66                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Has a protective role in both obesity and diabetes.|||In a breast cancer sample; somatic mutation.|||In isoform 11.|||In isoform 12.|||In isoform 2.|||In isoform 3, isoform 4, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12.|||In isoform 3.|||In isoform 4 and isoform 10.|||In isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 4, isoform 5, isoform 6, isoform 8, isoform 9, isoform 10 and isoform 12.|||In isoform 4, isoform 6, isoform 8, isoform 9 and isoform 12.|||In isoform 4, isoform 7, isoform 8, isoform 10 and isoform 12.|||In isoform 4, isoform 7, isoform 9 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 12.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SoHo|||Sorbin and SH3 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072185|||http://purl.uniprot.org/annotation/VAR_019653|||http://purl.uniprot.org/annotation/VAR_019654|||http://purl.uniprot.org/annotation/VAR_035661|||http://purl.uniprot.org/annotation/VAR_047652|||http://purl.uniprot.org/annotation/VAR_047653|||http://purl.uniprot.org/annotation/VAR_047654|||http://purl.uniprot.org/annotation/VSP_039210|||http://purl.uniprot.org/annotation/VSP_041193|||http://purl.uniprot.org/annotation/VSP_041194|||http://purl.uniprot.org/annotation/VSP_050895|||http://purl.uniprot.org/annotation/VSP_050896|||http://purl.uniprot.org/annotation/VSP_050898|||http://purl.uniprot.org/annotation/VSP_050899|||http://purl.uniprot.org/annotation/VSP_050900|||http://purl.uniprot.org/annotation/VSP_050901|||http://purl.uniprot.org/annotation/VSP_050902|||http://purl.uniprot.org/annotation/VSP_050903|||http://purl.uniprot.org/annotation/VSP_050904|||http://purl.uniprot.org/annotation/VSP_050905|||http://purl.uniprot.org/annotation/VSP_050906|||http://purl.uniprot.org/annotation/VSP_050907|||http://purl.uniprot.org/annotation/VSP_050908|||http://purl.uniprot.org/annotation/VSP_050909|||http://purl.uniprot.org/annotation/VSP_050910|||http://purl.uniprot.org/annotation/VSP_050911|||http://purl.uniprot.org/annotation/VSP_050912|||http://purl.uniprot.org/annotation/VSP_050913
http://togogenome.org/gene/9606:GOLGA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBA6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Breakpoint for translocation to form RET-GOLGA5 oncogene|||Cytoplasmic|||Dimethylated arginine|||Disordered|||Golgin subfamily A member 5|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Lumenal|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190061|||http://purl.uniprot.org/annotation/VAR_055859|||http://purl.uniprot.org/annotation/VAR_055860|||http://purl.uniprot.org/annotation/VSP_007731|||http://purl.uniprot.org/annotation/VSP_007732
http://togogenome.org/gene/9606:CRISP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RD74|||http://purl.uniprot.org/uniprot/P16562                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine-rich secretory protein 2|||In isoform 2.|||SCP|||ShKT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006264|||http://purl.uniprot.org/annotation/VAR_048832|||http://purl.uniprot.org/annotation/VSP_053891
http://togogenome.org/gene/9606:TRIM32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13049                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin ligase activity and ability to activate ULK1.|||B box-type|||E3 ubiquitin-protein ligase TRIM32|||In BBS11.|||In LGMDR8.|||In a patient with Bardet-Biedl syndrome; unknown pathological significance.|||N-acetylalanine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Phosphoserine|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056246|||http://purl.uniprot.org/annotation/VAR_018725|||http://purl.uniprot.org/annotation/VAR_038807|||http://purl.uniprot.org/annotation/VAR_038808|||http://purl.uniprot.org/annotation/VAR_038809|||http://purl.uniprot.org/annotation/VAR_042939|||http://purl.uniprot.org/annotation/VAR_042940|||http://purl.uniprot.org/annotation/VAR_066295
http://togogenome.org/gene/9606:ALDH16A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ83                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aldehyde dehydrogenase family 16 member A1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312986|||http://purl.uniprot.org/annotation/VAR_037638|||http://purl.uniprot.org/annotation/VAR_037639|||http://purl.uniprot.org/annotation/VSP_029982|||http://purl.uniprot.org/annotation/VSP_029983|||http://purl.uniprot.org/annotation/VSP_043280
http://togogenome.org/gene/9606:SERPINB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48594|||http://purl.uniprot.org/uniprot/Q9BYF7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site                                                                                  ^@                                                                                  N-acetylmethionine|||Reactive bond|||Serpin|||Serpin B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094104
http://togogenome.org/gene/9606:CA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUH8|||http://purl.uniprot.org/uniprot/P23280                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase|||Carbonic anhydrase 6|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004241|||http://purl.uniprot.org/annotation/PRO_5025097294|||http://purl.uniprot.org/annotation/VAR_028268|||http://purl.uniprot.org/annotation/VAR_028269|||http://purl.uniprot.org/annotation/VAR_028270|||http://purl.uniprot.org/annotation/VAR_028271|||http://purl.uniprot.org/annotation/VAR_033712|||http://purl.uniprot.org/annotation/VAR_061093|||http://purl.uniprot.org/annotation/VSP_045435|||http://purl.uniprot.org/annotation/VSP_046668
http://togogenome.org/gene/9606:ATP13A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y635|||http://purl.uniprot.org/uniprot/Q9H7F0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Helical|||Impairs the transport activity.|||In PPH5.|||In PPH5; unknown pathological significance.|||In isoform 2.|||Lumenal|||P5B-type ATPase N-terminal|||Phosphoserine|||Polyamine-transporting ATPase 13A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046425|||http://purl.uniprot.org/annotation/VAR_087461|||http://purl.uniprot.org/annotation/VAR_087462|||http://purl.uniprot.org/annotation/VSP_007314|||http://purl.uniprot.org/annotation/VSP_007315|||http://purl.uniprot.org/annotation/VSP_007316|||http://purl.uniprot.org/annotation/VSP_036300
http://togogenome.org/gene/9606:HSDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXM5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Inactive hydroxysteroid dehydrogenase-like protein 1|||N-acetylalanine|||Removed|||Required for mitochondria translocation|||Restores the oxidoreductase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313671|||http://purl.uniprot.org/annotation/VAR_037693|||http://purl.uniprot.org/annotation/VAR_037694|||http://purl.uniprot.org/annotation/VSP_042823
http://togogenome.org/gene/9606:DOK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PRA3|||http://purl.uniprot.org/uniprot/Q18PE1|||http://purl.uniprot.org/uniprot/Q8N1M3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Does not affect AChR clusters number or complexity.|||IRS-type PTB|||In CMS10.|||In CMS10; reduced stimulation of MUSK autophosphorylation when associated with A-174; results in a significant reduction of AChR clusters.|||In CMS10; results in a decrease of branched, c-shaped and perforated AChR clusters.|||In CMS10; results in a significant reduction of AChR clusters.|||In CMS10; results in reduced stimulation of MUSK autophosphorylation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Polar residues|||Protein Dok-7|||Reduced stimulation of MUSK autophosphorylation.|||Reduced stimulation of MUSK autophosphorylation; when associated with Q-158.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250371|||http://purl.uniprot.org/annotation/VAR_027544|||http://purl.uniprot.org/annotation/VAR_027545|||http://purl.uniprot.org/annotation/VAR_027546|||http://purl.uniprot.org/annotation/VAR_027547|||http://purl.uniprot.org/annotation/VAR_027548|||http://purl.uniprot.org/annotation/VAR_027549|||http://purl.uniprot.org/annotation/VAR_027550|||http://purl.uniprot.org/annotation/VAR_027551|||http://purl.uniprot.org/annotation/VAR_031246|||http://purl.uniprot.org/annotation/VAR_050508|||http://purl.uniprot.org/annotation/VAR_068750|||http://purl.uniprot.org/annotation/VAR_068751|||http://purl.uniprot.org/annotation/VAR_068752|||http://purl.uniprot.org/annotation/VAR_068753|||http://purl.uniprot.org/annotation/VAR_068754|||http://purl.uniprot.org/annotation/VAR_068755|||http://purl.uniprot.org/annotation/VAR_068756|||http://purl.uniprot.org/annotation/VAR_068757|||http://purl.uniprot.org/annotation/VAR_068758|||http://purl.uniprot.org/annotation/VAR_068759|||http://purl.uniprot.org/annotation/VAR_068760|||http://purl.uniprot.org/annotation/VAR_068761|||http://purl.uniprot.org/annotation/VAR_068762|||http://purl.uniprot.org/annotation/VAR_068763|||http://purl.uniprot.org/annotation/VAR_068764|||http://purl.uniprot.org/annotation/VAR_068765|||http://purl.uniprot.org/annotation/VAR_068766|||http://purl.uniprot.org/annotation/VAR_068767|||http://purl.uniprot.org/annotation/VAR_068768|||http://purl.uniprot.org/annotation/VAR_068769|||http://purl.uniprot.org/annotation/VAR_068770|||http://purl.uniprot.org/annotation/VAR_068771|||http://purl.uniprot.org/annotation/VAR_068772|||http://purl.uniprot.org/annotation/VAR_068773|||http://purl.uniprot.org/annotation/VAR_068774|||http://purl.uniprot.org/annotation/VSP_020633|||http://purl.uniprot.org/annotation/VSP_020634|||http://purl.uniprot.org/annotation/VSP_020635|||http://purl.uniprot.org/annotation/VSP_047252|||http://purl.uniprot.org/annotation/VSP_047253
http://togogenome.org/gene/9606:FKBP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y680                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||In isoform 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP7|||Retention in the endoplasmic reticulum                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025513|||http://purl.uniprot.org/annotation/VSP_041018|||http://purl.uniprot.org/annotation/VSP_059387|||http://purl.uniprot.org/annotation/VSP_059388
http://togogenome.org/gene/9606:RRP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RRP15-like protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273213|||http://purl.uniprot.org/annotation/VAR_030112|||http://purl.uniprot.org/annotation/VAR_030113|||http://purl.uniprot.org/annotation/VAR_053813
http://togogenome.org/gene/9606:POU3F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20265                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In isoform N-OCT 5A.|||In isoform N-OCT 5B.|||POU domain, class 3, transcription factor 2|||POU-specific|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013495|||http://purl.uniprot.org/annotation/VSP_018749|||http://purl.uniprot.org/annotation/VSP_018750
http://togogenome.org/gene/9606:TM6SF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8A7|||http://purl.uniprot.org/uniprot/Q9BZW4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Associated with higher circulating levels of alanine transaminase with lower levels of low-density lipoprotein-cholesterol (LDL-C), triglycerides and alkaline phosphatase in 3 independent populations; reduces protein expression by 46%.|||Disordered|||EXPERA 1|||EXPERA 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Transmembrane 6 superfamily member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181835|||http://purl.uniprot.org/annotation/VAR_062153|||http://purl.uniprot.org/annotation/VSP_040282
http://togogenome.org/gene/9606:TRIM63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Q1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||B box-type|||COS|||Disordered|||E3 ubiquitin-protein ligase TRIM63|||In isoform 2.|||Interaction with TTN|||Loss of SUMO2-binding.|||RING-type|||Rare variant; found in a patient with hypertrophic cardiomyopathy; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056290|||http://purl.uniprot.org/annotation/VAR_020116|||http://purl.uniprot.org/annotation/VAR_074092|||http://purl.uniprot.org/annotation/VAR_074093|||http://purl.uniprot.org/annotation/VAR_074094|||http://purl.uniprot.org/annotation/VAR_074095|||http://purl.uniprot.org/annotation/VAR_074096|||http://purl.uniprot.org/annotation/VAR_074097|||http://purl.uniprot.org/annotation/VAR_074098|||http://purl.uniprot.org/annotation/VAR_074099|||http://purl.uniprot.org/annotation/VAR_074100|||http://purl.uniprot.org/annotation/VAR_074101|||http://purl.uniprot.org/annotation/VAR_074102|||http://purl.uniprot.org/annotation/VAR_074103|||http://purl.uniprot.org/annotation/VAR_074104|||http://purl.uniprot.org/annotation/VAR_086949|||http://purl.uniprot.org/annotation/VSP_055443
http://togogenome.org/gene/9606:RGP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92546                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  RAB6A-GEF complex partner protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050741
http://togogenome.org/gene/9606:PRDX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13162|||http://purl.uniprot.org/uniprot/V9HW63                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate|||Interchain (with C-124); in linked form|||Interchain (with C-245); in linked form|||Peroxiredoxin-4|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135098|||http://purl.uniprot.org/annotation/PRO_5014314731
http://togogenome.org/gene/9606:CCNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75909                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-K|||Disordered|||In IDDHDF; contrary to the wild-type protein, does not rescue morpholino knockdown phenotype in zebrafish.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080478|||http://purl.uniprot.org/annotation/VAR_081570|||http://purl.uniprot.org/annotation/VSP_010830|||http://purl.uniprot.org/annotation/VSP_035970|||http://purl.uniprot.org/annotation/VSP_035971|||http://purl.uniprot.org/annotation/VSP_035972|||http://purl.uniprot.org/annotation/VSP_035973
http://togogenome.org/gene/9606:PPM1J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JR12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289058|||http://purl.uniprot.org/annotation/VAR_032566|||http://purl.uniprot.org/annotation/VAR_032567|||http://purl.uniprot.org/annotation/VSP_025882|||http://purl.uniprot.org/annotation/VSP_025883
http://togogenome.org/gene/9606:VPS41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49754                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||CHCR|||Disordered|||Disrupts interaction with ARL8B; impairs lysosomal localization and degradation of endocytosed cargo.|||In SCAR29; decreased protein abundance.|||In SCAR29; decreased protein abundance; cannot form a functional HOPS complex; causes a kinetic defect in the endosome-lysosome fusion process.|||In SCAR29; loss of expression; cannot form a functional HOPS complex.|||In SCAR29; unknown pathological significance; decreased protein abundance.|||In SCAR29; unknown pathological significance; no effect on protein expression.|||In isoform 2.|||In isoform 3.|||Interaction with ARL8B|||RING-type; atypical|||Vacuolar protein sorting-associated protein 41 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212823|||http://purl.uniprot.org/annotation/VAR_047914|||http://purl.uniprot.org/annotation/VAR_047915|||http://purl.uniprot.org/annotation/VAR_047916|||http://purl.uniprot.org/annotation/VAR_085704|||http://purl.uniprot.org/annotation/VAR_085705|||http://purl.uniprot.org/annotation/VAR_085706|||http://purl.uniprot.org/annotation/VAR_085707|||http://purl.uniprot.org/annotation/VAR_085708|||http://purl.uniprot.org/annotation/VSP_006751|||http://purl.uniprot.org/annotation/VSP_006752|||http://purl.uniprot.org/annotation/VSP_054169
http://togogenome.org/gene/9606:SCUBE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JP65|||http://purl.uniprot.org/uniprot/Q6ZS56|||http://purl.uniprot.org/uniprot/Q86TI6|||http://purl.uniprot.org/uniprot/Q8IWY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CUB|||Disordered|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||N-linked (GlcNAc...) asparagine|||Polar residues|||Signal peptide, CUB and EGF-like domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254648|||http://purl.uniprot.org/annotation/PRO_5002625355|||http://purl.uniprot.org/annotation/PRO_5004300924|||http://purl.uniprot.org/annotation/VAR_028850|||http://purl.uniprot.org/annotation/VAR_028851
http://togogenome.org/gene/9606:CRNKL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JY65|||http://purl.uniprot.org/uniprot/Q69YP1|||http://purl.uniprot.org/uniprot/Q9BZJ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Crooked neck-like protein 1|||Disordered|||HAT 1|||HAT 10|||HAT 11|||HAT 12|||HAT 13|||HAT 14|||HAT 15|||HAT 16|||HAT 17|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||HAT 9|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Mediates interaction with HSP90|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205719|||http://purl.uniprot.org/annotation/VAR_024995|||http://purl.uniprot.org/annotation/VAR_049318|||http://purl.uniprot.org/annotation/VAR_049319|||http://purl.uniprot.org/annotation/VAR_049320|||http://purl.uniprot.org/annotation/VAR_049321|||http://purl.uniprot.org/annotation/VSP_002058|||http://purl.uniprot.org/annotation/VSP_002059|||http://purl.uniprot.org/annotation/VSP_002060|||http://purl.uniprot.org/annotation/VSP_002061|||http://purl.uniprot.org/annotation/VSP_002062
http://togogenome.org/gene/9606:TXLNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUQ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gamma-taxilin|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189426|||http://purl.uniprot.org/annotation/VAR_019809|||http://purl.uniprot.org/annotation/VSP_039391
http://togogenome.org/gene/9606:BOD1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y9Y2|||http://purl.uniprot.org/uniprot/Q8NFC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  A.T hook|||Acidic residues|||Basic and acidic residues|||Biorientation of chromosomes in cell division protein 1-like 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187027|||http://purl.uniprot.org/annotation/VAR_035220|||http://purl.uniprot.org/annotation/VAR_035221|||http://purl.uniprot.org/annotation/VAR_035222|||http://purl.uniprot.org/annotation/VAR_035223|||http://purl.uniprot.org/annotation/VAR_035224|||http://purl.uniprot.org/annotation/VAR_035225|||http://purl.uniprot.org/annotation/VAR_035226|||http://purl.uniprot.org/annotation/VAR_035227|||http://purl.uniprot.org/annotation/VAR_036124|||http://purl.uniprot.org/annotation/VAR_061166
http://togogenome.org/gene/9606:CDH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55286                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-8|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003773|||http://purl.uniprot.org/annotation/PRO_0000003774
http://togogenome.org/gene/9606:MPDZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75970                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In HYC2.|||In HYC2; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||L27|||Loss of interaction with CAMK2A.|||Multiple PDZ domain protein|||Omega-N-methylarginine|||PDZ 1|||PDZ 10|||PDZ 11|||PDZ 12|||PDZ 13|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ 7|||PDZ 8|||PDZ 9|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094594|||http://purl.uniprot.org/annotation/VAR_056115|||http://purl.uniprot.org/annotation/VAR_056116|||http://purl.uniprot.org/annotation/VAR_056117|||http://purl.uniprot.org/annotation/VAR_056118|||http://purl.uniprot.org/annotation/VAR_056119|||http://purl.uniprot.org/annotation/VAR_056120|||http://purl.uniprot.org/annotation/VAR_081122|||http://purl.uniprot.org/annotation/VAR_081123|||http://purl.uniprot.org/annotation/VAR_081124|||http://purl.uniprot.org/annotation/VAR_081125|||http://purl.uniprot.org/annotation/VSP_040450|||http://purl.uniprot.org/annotation/VSP_040451
http://togogenome.org/gene/9606:TIFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CG3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by ALPK1 and subsequent TIFA-mediated NF-kappa-B activation.|||Disordered|||FHA|||In RKN: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with 88-A-A-89.|||In RKN: Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with A-51.|||Loss of binding to TRAF6 and activation of NF-kappa-B and JNK pathways.|||Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with A-66.|||Loss of homooligomerization and activation of NF-kappa-B and JNK pathways; when associated with E-50.|||Phosphothreonine; by ALPK1|||TRAF-interacting protein with FHA domain-containing protein A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320689|||http://purl.uniprot.org/annotation/VAR_051422
http://togogenome.org/gene/9606:TGFBR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3QNQ0|||http://purl.uniprot.org/uniprot/D2JYI1|||http://purl.uniprot.org/uniprot/P37173                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes kinase activity, TGF-beta signaling and interaction with DAXX.|||Cytoplasmic|||Extracellular|||Helical|||In HNPCC6.|||In LDS2.|||In LDS2; has a negative effect on TGF-beta signaling.|||In a breast tumor.|||In a breast tumor; signaling of TGF-beta significantly inhibited.|||In a colorectal cancer sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In esophageal cancer.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein kinase|||Proton acceptor|||Sufficient for interaction with CLU|||TGF-beta receptor type-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024426|||http://purl.uniprot.org/annotation/PRO_5003033108|||http://purl.uniprot.org/annotation/PRO_5010102791|||http://purl.uniprot.org/annotation/VAR_008156|||http://purl.uniprot.org/annotation/VAR_015816|||http://purl.uniprot.org/annotation/VAR_017606|||http://purl.uniprot.org/annotation/VAR_020510|||http://purl.uniprot.org/annotation/VAR_022351|||http://purl.uniprot.org/annotation/VAR_022352|||http://purl.uniprot.org/annotation/VAR_022353|||http://purl.uniprot.org/annotation/VAR_022354|||http://purl.uniprot.org/annotation/VAR_022355|||http://purl.uniprot.org/annotation/VAR_022356|||http://purl.uniprot.org/annotation/VAR_022357|||http://purl.uniprot.org/annotation/VAR_022358|||http://purl.uniprot.org/annotation/VAR_022359|||http://purl.uniprot.org/annotation/VAR_022360|||http://purl.uniprot.org/annotation/VAR_022361|||http://purl.uniprot.org/annotation/VAR_022362|||http://purl.uniprot.org/annotation/VAR_028063|||http://purl.uniprot.org/annotation/VAR_029760|||http://purl.uniprot.org/annotation/VAR_029761|||http://purl.uniprot.org/annotation/VAR_036070|||http://purl.uniprot.org/annotation/VAR_041414|||http://purl.uniprot.org/annotation/VAR_041415|||http://purl.uniprot.org/annotation/VAR_041416|||http://purl.uniprot.org/annotation/VAR_041417|||http://purl.uniprot.org/annotation/VAR_066723|||http://purl.uniprot.org/annotation/VAR_066724|||http://purl.uniprot.org/annotation/VAR_066725|||http://purl.uniprot.org/annotation/VAR_066726|||http://purl.uniprot.org/annotation/VAR_066727|||http://purl.uniprot.org/annotation/VAR_066728|||http://purl.uniprot.org/annotation/VAR_066729|||http://purl.uniprot.org/annotation/VAR_066730|||http://purl.uniprot.org/annotation/VAR_066731|||http://purl.uniprot.org/annotation/VAR_076167|||http://purl.uniprot.org/annotation/VAR_076168|||http://purl.uniprot.org/annotation/VAR_076169|||http://purl.uniprot.org/annotation/VAR_076170|||http://purl.uniprot.org/annotation/VAR_076171|||http://purl.uniprot.org/annotation/VSP_012157|||http://purl.uniprot.org/annotation/VSP_061513|||http://purl.uniprot.org/annotation/VSP_061514
http://togogenome.org/gene/9606:UBA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41226                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1-1|||1-2|||2 approximate repeats|||Found in a small consanguineous family with learning disability; unknown pathological significance.|||Glycyl thioester intermediate|||Phosphoserine|||Ubiquitin-like modifier-activating enzyme 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194937|||http://purl.uniprot.org/annotation/VAR_047793|||http://purl.uniprot.org/annotation/VAR_052434|||http://purl.uniprot.org/annotation/VAR_080759
http://togogenome.org/gene/9606:NR1H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6ZGS9|||http://purl.uniprot.org/uniprot/Q96RI1                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates SUMO1-mediated inhibition of ligand-induced transcactivation at ABCB11/BSEP and NR0B2/SHP promoters; when associated with R-132 and A-291.|||Abrogates SUMO1-mediated inhibition of ligand-induced transcactivation at ABCB11/BSEP and NR0B2/SHP promoters; when associated with R-132 and R-289.|||Abrogates SUMO1-mediated inhibition of ligand-induced transcactivation at ABCB11/BSEP and NR0B2/SHP promoters; when associated with R-289 and A-291.|||As a heterodimer with RXRA, impaired transcriptional activity.|||Bile acid receptor|||Decreases transcriptional activation SC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, impairs interaction with RXRA and enhances interaction with SETD7, decreases association with ABCB11/BSEP promoter.|||Decreases transcriptional activation SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on interaction with RXRA and SETD7, decreases association with ABCB11/BSEP promoter.|||Decreases transcriptional activation SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on interaction with RXRA and SETD7.|||Decreases transcriptional activation SLC51A/OSTA, SLC51B/OSTB and ABCB11/BSEP, no effect on interaction with RXRA and impairs interaction with SETD7.|||Decreases transcriptional activation of SLC51B/OSTB, no effect on SLC51A/OSTA and ABCB11/BSEP, impairs interaction with RXRA and SETD7.|||Decreases transcriptional activation of SLC51B/OSTB, no effect on SLC51A/OSTA and ABCB11/BSEP, no effect on interaction with RXRA and SETD7.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Impairs ligand-dependent transactivation activity, impairs interaction with PPARGC1A; when associated with A-145.|||Impairs ligand-dependent transactivation activity, impairs interaction with PPARGC1A; when associated with A-164.|||Impairs transcriptional activation of ABCB11/BSEP.|||In PFIC5; loss of isoform 4 transcription regulatory region sequence-specific DNA binding activity; loss of isoform 4 function in regulation of transcription DNA-templated.|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||N6-acetyllysine; by EP300|||N6-methyllysine; by SETD7|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine; by PKC/PRKCZ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053538|||http://purl.uniprot.org/annotation/VAR_077017|||http://purl.uniprot.org/annotation/VSP_003665|||http://purl.uniprot.org/annotation/VSP_010135|||http://purl.uniprot.org/annotation/VSP_044547
http://togogenome.org/gene/9606:SLC22A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y226                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||May be associated with a reduced risk for gout; variant carriers have lower serum urate levels and increased renal urate excretion; results in strongly reduced urate transport; no change in SLC22A13/OAT10 protein levels; no change in cellular localization.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230782|||http://purl.uniprot.org/annotation/VAR_025787|||http://purl.uniprot.org/annotation/VAR_025788|||http://purl.uniprot.org/annotation/VAR_086737|||http://purl.uniprot.org/annotation/VSP_017830
http://togogenome.org/gene/9606:LY6G6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7Z1|||http://purl.uniprot.org/uniprot/O95867                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||Lymphocyte antigen 6 complex locus protein G6c|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036176|||http://purl.uniprot.org/annotation/PRO_0000323019|||http://purl.uniprot.org/annotation/PRO_5014275541|||http://purl.uniprot.org/annotation/VAR_039541
http://togogenome.org/gene/9606:RSL24D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHA3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Probable ribosome biogenesis protein RLP24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136896
http://togogenome.org/gene/9606:ANGEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNK9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Protein angel homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218581|||http://purl.uniprot.org/annotation/VAR_056239|||http://purl.uniprot.org/annotation/VAR_056240|||http://purl.uniprot.org/annotation/VAR_061374
http://togogenome.org/gene/9606:INMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95050                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Indolethylamine N-methyltransferase|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159712|||http://purl.uniprot.org/annotation/VAR_011616|||http://purl.uniprot.org/annotation/VAR_011617|||http://purl.uniprot.org/annotation/VAR_036991|||http://purl.uniprot.org/annotation/VAR_036992|||http://purl.uniprot.org/annotation/VAR_036993|||http://purl.uniprot.org/annotation/VAR_036994|||http://purl.uniprot.org/annotation/VAR_061373|||http://purl.uniprot.org/annotation/VSP_045922
http://togogenome.org/gene/9606:EIF4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38919                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase activity is not increased by the presence of CASC3. Does not prevent EJC formation. Prevents the EJC disassembly.|||DEAD box|||Decreased interaction with CWC22.|||Eukaryotic initiation factor 4A-III|||Eukaryotic initiation factor 4A-III, N-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In RCPS.|||Loss of CWC22-binding and loss of incorporation into EJCs.|||Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-270.|||Loss of CWC22-binding and loss of incorporation into EJCs; when associated with K-273.|||Loss of incorporation into EJCs; when associated with K-401.|||Loss of incorporation into EJCs; when associated with R-402.|||N-acetylalanine; in Eukaryotic initiation factor 4A-III, N-terminally processed|||N-acetylmethionine|||N6-acetyllysine|||No effect on interaction with CWC22.|||Phosphoserine|||Phosphothreonine|||Q motif|||Reduced incorporation into EJCs.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054942|||http://purl.uniprot.org/annotation/PRO_0000423267|||http://purl.uniprot.org/annotation/VAR_071090
http://togogenome.org/gene/9606:ZMAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MD47|||http://purl.uniprot.org/uniprot/Q5H9K5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||In isoform 2.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Polar residues|||Zinc finger matrin-type protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311348|||http://purl.uniprot.org/annotation/VAR_053766|||http://purl.uniprot.org/annotation/VAR_062159|||http://purl.uniprot.org/annotation/VSP_029533
http://togogenome.org/gene/9606:MRPL41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXM3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL41|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273228
http://togogenome.org/gene/9606:C11orf68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3H3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1.|||In isoform 3.|||Omega-N-methylarginine|||UPF0696 protein C11orf68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228117|||http://purl.uniprot.org/annotation/VAR_060319|||http://purl.uniprot.org/annotation/VSP_059970|||http://purl.uniprot.org/annotation/VSP_059971
http://togogenome.org/gene/9606:SRSF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13243|||http://purl.uniprot.org/uniprot/Q86U32                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform SRP40-2.|||In isoform SRP40-4.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RRM|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081927|||http://purl.uniprot.org/annotation/VAR_014713|||http://purl.uniprot.org/annotation/VSP_005863|||http://purl.uniprot.org/annotation/VSP_005864|||http://purl.uniprot.org/annotation/VSP_005865
http://togogenome.org/gene/9606:IFT25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y547                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Strand                                                                                  ^@                                                                                  Intraflagellar transport protein 25 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058531
http://togogenome.org/gene/9606:API5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDR3|||http://purl.uniprot.org/uniprot/Q9BZZ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM-like and Heat-like helical repeats|||Apoptosis inhibitor 5|||Disordered|||In isoform 1.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Leucine-zipper|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064634|||http://purl.uniprot.org/annotation/VAR_021519|||http://purl.uniprot.org/annotation/VAR_021520|||http://purl.uniprot.org/annotation/VAR_021521|||http://purl.uniprot.org/annotation/VSP_039761|||http://purl.uniprot.org/annotation/VSP_039762|||http://purl.uniprot.org/annotation/VSP_041969|||http://purl.uniprot.org/annotation/VSP_041970|||http://purl.uniprot.org/annotation/VSP_041971|||http://purl.uniprot.org/annotation/VSP_041972|||http://purl.uniprot.org/annotation/VSP_043289|||http://purl.uniprot.org/annotation/VSP_057412
http://togogenome.org/gene/9606:KLHDC8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYD2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch 7|||Kelch domain-containing protein 8A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229001
http://togogenome.org/gene/9606:LGALS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUM7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413535|||http://purl.uniprot.org/annotation/VAR_065877
http://togogenome.org/gene/9606:FOXD4L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4-like 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091825
http://togogenome.org/gene/9606:FNTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49354                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||PFTA 1|||PFTA 2|||PFTA 3|||PFTA 4|||PFTA 5|||Phosphoserine|||Pro residues|||Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha|||Reduced activity.|||Reduced catalytic efficiency.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119746|||http://purl.uniprot.org/annotation/VSP_036468
http://togogenome.org/gene/9606:OR6Y1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGX8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6Y1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150641|||http://purl.uniprot.org/annotation/VAR_062055
http://togogenome.org/gene/9606:SLC46A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NT5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  2-fold reduction of methotrexate uptake.|||8-fold reduction of methotrexate uptake.|||Abolished N-glycosylation without affecting localization to the cell membrane; when associated with Q-58.|||Abolished N-glycosylation without affecting localization to the cell membrane; when associated with Q-68.|||Abolished folate uptake.|||Abolished methotrexate uptake.|||Abolished proton-coupled folate transport at pH 5.5 and pH 7.5.|||Abolished proton-coupled folate transport at pH 5.5, while it displays strong proton-coupled folate transporter activity at pH 7.5.|||Abolished proton-coupled folate transport.|||Abolished sensitivity to myricetin inhibitor.|||Abolishes folate uptake.|||About 90% loss of transport function.|||Complete loss of transport function.|||Cytoplasmic|||Decreased folate uptake at low folate concentration, while folate uptake is not affected at high folate concentration.|||Decreased methotrexate uptake at low concentration.|||Decreased proton-coupled folate transport.|||Displays a lower affinity for folate substrate associated with a higher rate of conformational change.|||Does not affect folate uptake.|||Does not affect methotrexate uptake at low concentration.|||Does not affect methotrexate uptake.|||Extracellular|||Helical; Name=TM1|||Helical; Name=TM10|||Helical; Name=TM11|||Helical; Name=TM12|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||Helical; Name=TM6|||Helical; Name=TM7|||Helical; Name=TM8|||Helical; Name=TM9|||In HFM; abolishes folate uptake.|||In HFM; decreased folate uptake.|||In HFM; locks the protein into an inward-open conformation, leading to decreased folate uptake; does not affect localization to the cell membrane.|||In HFM; loss of function measured as methotrexate uptake.|||In HFM; loss-of-function mutation; targeted to the plasma membrane but has significantly impaired folate transport activity.|||In HFM; reduces folate uptake to 13% of normal levels.|||In HFM; strongly decreased folate and methotrexate uptake.|||In isoform 2.|||Loss of methotrexate uptake.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton-coupled folate transporter|||Slightly decreased proton-coupled folate transport.|||Strongly decreased folate and methotrexate uptake, while it still binds pemetrexed.|||reversibly protonated residue during proton transport                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084851|||http://purl.uniprot.org/annotation/VAR_032825|||http://purl.uniprot.org/annotation/VAR_032826|||http://purl.uniprot.org/annotation/VAR_032827|||http://purl.uniprot.org/annotation/VAR_032828|||http://purl.uniprot.org/annotation/VAR_032829|||http://purl.uniprot.org/annotation/VAR_050302|||http://purl.uniprot.org/annotation/VAR_058210|||http://purl.uniprot.org/annotation/VAR_067960|||http://purl.uniprot.org/annotation/VAR_067961|||http://purl.uniprot.org/annotation/VAR_067962|||http://purl.uniprot.org/annotation/VAR_067963|||http://purl.uniprot.org/annotation/VAR_085918|||http://purl.uniprot.org/annotation/VAR_085919|||http://purl.uniprot.org/annotation/VAR_085920|||http://purl.uniprot.org/annotation/VSP_016053
http://togogenome.org/gene/9606:FOXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00409                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein N3|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091869|||http://purl.uniprot.org/annotation/VAR_049163|||http://purl.uniprot.org/annotation/VSP_001551
http://togogenome.org/gene/9606:RPL27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61353                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  KOW|||Large ribosomal subunit protein eL27|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126077
http://togogenome.org/gene/9606:ADGRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60241                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor B2|||Cleavage; by furin|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Inhibits autoproteolytic cleavage.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphotyrosine|||Polar residues|||Probable disease-associated variant found in a patient with progressive spastic paraparesis and other neurological symptoms; enhances receptor surface expression; increases the constitutive signaling activity; does not affect interaction with GNAZ; promotes enhanced interaction with GNAI1; decreases interaction with SH3GL2.|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012864|||http://purl.uniprot.org/annotation/VAR_079840|||http://purl.uniprot.org/annotation/VSP_037045|||http://purl.uniprot.org/annotation/VSP_037046|||http://purl.uniprot.org/annotation/VSP_037047
http://togogenome.org/gene/9606:WDR90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KV7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 17|||WD 18|||WD 19|||WD 2|||WD 20|||WD 21|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 90                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341412|||http://purl.uniprot.org/annotation/VAR_044060|||http://purl.uniprot.org/annotation/VAR_044061|||http://purl.uniprot.org/annotation/VAR_044062|||http://purl.uniprot.org/annotation/VAR_044063|||http://purl.uniprot.org/annotation/VAR_044064|||http://purl.uniprot.org/annotation/VAR_044065|||http://purl.uniprot.org/annotation/VSP_034290|||http://purl.uniprot.org/annotation/VSP_034294|||http://purl.uniprot.org/annotation/VSP_034298|||http://purl.uniprot.org/annotation/VSP_034300|||http://purl.uniprot.org/annotation/VSP_034303|||http://purl.uniprot.org/annotation/VSP_034306|||http://purl.uniprot.org/annotation/VSP_041087|||http://purl.uniprot.org/annotation/VSP_041088
http://togogenome.org/gene/9606:CYP2D6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C1ID52|||http://purl.uniprot.org/uniprot/P10635|||http://purl.uniprot.org/uniprot/Q5Y7H2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol.|||Basic and acidic residues|||Cytochrome P450 2D6|||Disordered|||Helical|||In allele CYP2D6*10 and allele CYP2D6*14; poor debrisquone metabolism.|||In allele CYP2D6*12; impaired metabolism of sparteine.|||In allele CYP2D6*14; poor debrisquone metabolism.|||In allele CYP2D6*17; poor debrisquone metabolism.|||In allele CYP2D6*2, allele CYP2D6*10, allele CYP2D6*12, allele CYP2D6*14, allele CYP2D6*17, allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46; impaired metabolism of sparteine.|||In allele CYP2D6*2, allele CYP2D6*12, allele CYP2D6*14, allele CYP2D6*17, allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46; significantly reduced monooxygenase activity toward anandamide; slight decrease of monooxygenase activity towards bufuralol.|||In allele CYP2D6*21 and allele CYP2D6*46.|||In allele CYP2D6*22.|||In allele CYP2D6*23.|||In allele CYP2D6*24.|||In allele CYP2D6*25.|||In allele CYP2D6*26.|||In allele CYP2D6*27.|||In allele CYP2D6*33.|||In allele CYP2D6*35.|||In allele CYP2D6*45A, allele CYP2D6*45B and allele CYP2D6*46.|||In allele CYP2D6*6B and allele CYP2D6*6C.|||In allele CYP2D6*7; loss of activity.|||In allele CYP2D6*87.|||In allele CYP2D6*88.|||In allele CYP2D6*89; >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol.|||In allele CYP2D6*9.|||In allele CYP2D6*90.|||In allele CYP2D6*91.|||In allele CYP2D6*93; >90% decrease of monooxygenase activity towards dextromethorphan and bufuralol.|||In allele CYP2D6*94.|||In allele CYP2D6*97.|||In allele CYP2D6*98.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051731|||http://purl.uniprot.org/annotation/PRO_5004264737|||http://purl.uniprot.org/annotation/VAR_001256|||http://purl.uniprot.org/annotation/VAR_008336|||http://purl.uniprot.org/annotation/VAR_008337|||http://purl.uniprot.org/annotation/VAR_008338|||http://purl.uniprot.org/annotation/VAR_008339|||http://purl.uniprot.org/annotation/VAR_008340|||http://purl.uniprot.org/annotation/VAR_008341|||http://purl.uniprot.org/annotation/VAR_008347|||http://purl.uniprot.org/annotation/VAR_008348|||http://purl.uniprot.org/annotation/VAR_008366|||http://purl.uniprot.org/annotation/VAR_008367|||http://purl.uniprot.org/annotation/VAR_008368|||http://purl.uniprot.org/annotation/VAR_008369|||http://purl.uniprot.org/annotation/VAR_008370|||http://purl.uniprot.org/annotation/VAR_008371|||http://purl.uniprot.org/annotation/VAR_008372|||http://purl.uniprot.org/annotation/VAR_008373|||http://purl.uniprot.org/annotation/VAR_008374|||http://purl.uniprot.org/annotation/VAR_014633|||http://purl.uniprot.org/annotation/VAR_024720|||http://purl.uniprot.org/annotation/VAR_024721|||http://purl.uniprot.org/annotation/VAR_024722|||http://purl.uniprot.org/annotation/VAR_024723|||http://purl.uniprot.org/annotation/VAR_024724|||http://purl.uniprot.org/annotation/VAR_024725|||http://purl.uniprot.org/annotation/VAR_024726|||http://purl.uniprot.org/annotation/VAR_045679|||http://purl.uniprot.org/annotation/VAR_045680|||http://purl.uniprot.org/annotation/VAR_045681|||http://purl.uniprot.org/annotation/VAR_059150|||http://purl.uniprot.org/annotation/VAR_059151|||http://purl.uniprot.org/annotation/VAR_072764|||http://purl.uniprot.org/annotation/VAR_072765|||http://purl.uniprot.org/annotation/VAR_072766|||http://purl.uniprot.org/annotation/VAR_072767|||http://purl.uniprot.org/annotation/VAR_072768|||http://purl.uniprot.org/annotation/VAR_072769|||http://purl.uniprot.org/annotation/VAR_072770|||http://purl.uniprot.org/annotation/VAR_072771|||http://purl.uniprot.org/annotation/VAR_072772|||http://purl.uniprot.org/annotation/VAR_072773|||http://purl.uniprot.org/annotation/VAR_072774|||http://purl.uniprot.org/annotation/VAR_072775|||http://purl.uniprot.org/annotation/VAR_072776|||http://purl.uniprot.org/annotation/VAR_072777|||http://purl.uniprot.org/annotation/VAR_072778|||http://purl.uniprot.org/annotation/VAR_072779|||http://purl.uniprot.org/annotation/VAR_072780|||http://purl.uniprot.org/annotation/VAR_072781|||http://purl.uniprot.org/annotation/VAR_072782|||http://purl.uniprot.org/annotation/VSP_044486
http://togogenome.org/gene/9606:CNKSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL25|||http://purl.uniprot.org/uniprot/G3V160|||http://purl.uniprot.org/uniprot/Q53GM7|||http://purl.uniprot.org/uniprot/Q969H4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  CRIC|||Connector enhancer of kinase suppressor of ras 1|||Disordered|||In isoform 2.|||No interaction with Rho.|||PDZ|||PH|||Phosphoserine|||Polar residues|||Pro residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089969|||http://purl.uniprot.org/annotation/VAR_057790|||http://purl.uniprot.org/annotation/VSP_010886
http://togogenome.org/gene/9606:P3H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVL6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fe2OG dioxygenase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Prolyl 3-hydroxylase 3|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240360|||http://purl.uniprot.org/annotation/VAR_050443|||http://purl.uniprot.org/annotation/VAR_050444|||http://purl.uniprot.org/annotation/VAR_050445|||http://purl.uniprot.org/annotation/VAR_050446|||http://purl.uniprot.org/annotation/VAR_050447|||http://purl.uniprot.org/annotation/VSP_019352
http://togogenome.org/gene/9606:WRNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S55                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ATPase WRNIP1|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of ATPase activity.|||Loss of affinity for ubiquitin.|||N6-acetyllysine; alternate|||Normal affinity for ubiquitin.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduced affinity for ubiquitin.|||UBZ4-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084785|||http://purl.uniprot.org/annotation/VSP_051781|||http://purl.uniprot.org/annotation/VSP_051782|||http://purl.uniprot.org/annotation/VSP_051783
http://togogenome.org/gene/9606:RABEPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8A0|||http://purl.uniprot.org/uniprot/A0A0S2Z4Z5|||http://purl.uniprot.org/uniprot/Q7Z6M1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Phosphoserine|||Rab9 effector protein with kelch motifs                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280616|||http://purl.uniprot.org/annotation/VAR_031175|||http://purl.uniprot.org/annotation/VAR_031176|||http://purl.uniprot.org/annotation/VAR_031177|||http://purl.uniprot.org/annotation/VAR_031178|||http://purl.uniprot.org/annotation/VAR_031179|||http://purl.uniprot.org/annotation/VAR_050058|||http://purl.uniprot.org/annotation/VAR_050059|||http://purl.uniprot.org/annotation/VSP_023828
http://togogenome.org/gene/9606:VAMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75379|||http://purl.uniprot.org/uniprot/Q6IAZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Phosphoserine|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 4|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206731|||http://purl.uniprot.org/annotation/VSP_006326
http://togogenome.org/gene/9606:TTC23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W5X9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Tetratricopeptide repeat protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289548|||http://purl.uniprot.org/annotation/VSP_026017|||http://purl.uniprot.org/annotation/VSP_026018
http://togogenome.org/gene/9606:SPATA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEY3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Spermatogenesis-associated protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072101|||http://purl.uniprot.org/annotation/VAR_051369
http://togogenome.org/gene/9606:SPANXC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Polar residues|||Sperm protein associated with the nucleus on the X chromosome C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189551|||http://purl.uniprot.org/annotation/VAR_032024
http://togogenome.org/gene/9606:CLUAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNW5|||http://purl.uniprot.org/uniprot/Q96AJ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Clusterin-associated protein 1|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239451|||http://purl.uniprot.org/annotation/VAR_050869|||http://purl.uniprot.org/annotation/VAR_050870|||http://purl.uniprot.org/annotation/VSP_019229
http://togogenome.org/gene/9606:NDUFB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96000                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In MC1DN35; decreased protein abundance; decreased CHCHD4-mediated oxidation; loss of mitochondrial localization; retained in the cytosol; loss of function in mitochondrial respiratory chain complex I assembly.|||In isoform 2.|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118830|||http://purl.uniprot.org/annotation/VAR_084767|||http://purl.uniprot.org/annotation/VSP_056555
http://togogenome.org/gene/9606:IGF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05019|||http://purl.uniprot.org/uniprot/Q13429|||http://purl.uniprot.org/uniprot/Q59GC5|||http://purl.uniprot.org/uniprot/Q5U743                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  A|||B|||Basic and acidic residues|||C|||D|||Disordered|||Dominant-negative mutant, no effect on IGFR1-binding, defective in integrin-binding and the formation of ternary complex with integrins and IGFR1, defective in inducing IGF1 signaling and cell proliferation, and suppresses activation of IGF1R by insulin and tumorigenesis in vivo; when associated with E-84.|||Dominant-negative mutant, no effect on IGFR1-binding, defective in integrin-binding and the formation of ternary complex with integrins and IGFR1, defective in inducing IGF1 signaling and cell proliferation, and suppresses activation of IGF1R by insulin and tumorigenesis in vivo; when associated with E-85.|||E peptide|||Found in a patient with primordial dwarfism; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Insulin-like|||Insulin-like growth factor I|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015663|||http://purl.uniprot.org/annotation/PRO_0000015664|||http://purl.uniprot.org/annotation/PRO_0000015665|||http://purl.uniprot.org/annotation/PRO_5004252488|||http://purl.uniprot.org/annotation/PRO_5014102473|||http://purl.uniprot.org/annotation/PRO_5014310167|||http://purl.uniprot.org/annotation/VAR_013945|||http://purl.uniprot.org/annotation/VAR_056113|||http://purl.uniprot.org/annotation/VAR_075825|||http://purl.uniprot.org/annotation/VSP_039637|||http://purl.uniprot.org/annotation/VSP_043317|||http://purl.uniprot.org/annotation/VSP_047399
http://togogenome.org/gene/9606:ZBTB44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BY22|||http://purl.uniprot.org/uniprot/Q8NCP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger and BTB domain-containing protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274608|||http://purl.uniprot.org/annotation/VAR_030336|||http://purl.uniprot.org/annotation/VSP_022834|||http://purl.uniprot.org/annotation/VSP_022835|||http://purl.uniprot.org/annotation/VSP_022836|||http://purl.uniprot.org/annotation/VSP_022837
http://togogenome.org/gene/9606:LOXL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58215                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Disordered|||Found in patients with Stickler syndrome; unknown pathological significance.|||Impaired ability to mediate deacetylation of STAT3.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-214; A-345 and A-459.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-376 and A-446.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-376 and A-492.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-446 and A-492.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-214 and A-345.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-214 and A-459.|||Impaired ability to mediate deacetylation of STAT3; when associated with A-83; A-345 and A-459.|||In isoform 2.|||In isoform 3.|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog 3|||Lysyl-oxidase like|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018533|||http://purl.uniprot.org/annotation/VAR_050011|||http://purl.uniprot.org/annotation/VAR_077909|||http://purl.uniprot.org/annotation/VSP_054417|||http://purl.uniprot.org/annotation/VSP_054418
http://togogenome.org/gene/9606:CALB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05937                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calbindin|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||In isoform 2.|||Interaction with RANBP9|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073472|||http://purl.uniprot.org/annotation/VSP_055508
http://togogenome.org/gene/9606:ROCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2P9DU05|||http://purl.uniprot.org/uniprot/O75116|||http://purl.uniprot.org/uniprot/Q14DU5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes cleavage by granzyme B.|||Cleavage; by granzyme B|||Disordered|||In a metastatic melanoma sample; somatic mutation.|||Interaction with NPM1|||Interaction with PPP1R12A|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by ROCK2|||Phosphotyrosine; by SRC|||Polar residues|||Protein kinase|||Proton acceptor|||REM-1|||RHOA binding|||Rho-associated protein kinase 2|||RhoBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086625|||http://purl.uniprot.org/annotation/VAR_041062|||http://purl.uniprot.org/annotation/VAR_041063|||http://purl.uniprot.org/annotation/VAR_041064|||http://purl.uniprot.org/annotation/VAR_057110
http://togogenome.org/gene/9606:IL13RA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78552                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||In isoform 2.|||Interleukin-13 receptor subunit alpha-1|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010939|||http://purl.uniprot.org/annotation/VSP_055587|||http://purl.uniprot.org/annotation/VSP_055588
http://togogenome.org/gene/9606:LRPAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30533                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-2-macroglobulin receptor-associated protein|||Basic and acidic residues|||Disordered|||LDL receptor binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Prevents secretion from ER|||Reduces competition with MAPT for binding to LRP1; when associated with A-290.|||Reduces competition with MAPT for binding to LRP1; when associated with A-304.|||Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-307.|||Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-341.|||Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-307 and A-341.|||Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-302; A-307 and A-341.|||Strongly reduced interaction with LRP1; when associated with A-283; A-293; A-302; A-307 and A-341.|||Strongly reduced interaction with LRP1; when associated with A-291; A-293; A-302; A-307 and A-341.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020724|||http://purl.uniprot.org/annotation/VAR_011821|||http://purl.uniprot.org/annotation/VAR_050660
http://togogenome.org/gene/9606:PLA2G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ20                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic residues|||Disordered|||Group 3 secretory phospholipase A2|||Impairs PGE2 synthesis. Impairs PGD2 synthesis. Impairs mast cell degranulation. Impairs neurite outgrowth.|||Loss of glycosylation.|||N-linked (GlcNAc...) asparagine|||Phospholipase A2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022992|||http://purl.uniprot.org/annotation/VAR_020288|||http://purl.uniprot.org/annotation/VAR_024555|||http://purl.uniprot.org/annotation/VAR_024556|||http://purl.uniprot.org/annotation/VAR_024557|||http://purl.uniprot.org/annotation/VAR_034366|||http://purl.uniprot.org/annotation/VAR_056581
http://togogenome.org/gene/9606:BANF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H503                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Barrier-to-autointegration factor-like protein|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221030|||http://purl.uniprot.org/annotation/VAR_013693|||http://purl.uniprot.org/annotation/VAR_024372|||http://purl.uniprot.org/annotation/VSP_046080
http://togogenome.org/gene/9606:LAMA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQS9|||http://purl.uniprot.org/uniprot/A0A0A0MTC7|||http://purl.uniprot.org/uniprot/Q16363|||http://purl.uniprot.org/uniprot/Q5D044                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||Domain II and I|||In CMD1JJ; loss of integrin-binding capacity.|||In isoform 2.|||In isoform 3.|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4; truncated|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin subunit alpha-4|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017060|||http://purl.uniprot.org/annotation/PRO_5001974392|||http://purl.uniprot.org/annotation/PRO_5004254017|||http://purl.uniprot.org/annotation/PRO_5014506434|||http://purl.uniprot.org/annotation/VAR_025550|||http://purl.uniprot.org/annotation/VAR_025551|||http://purl.uniprot.org/annotation/VAR_025552|||http://purl.uniprot.org/annotation/VAR_056140|||http://purl.uniprot.org/annotation/VAR_056141|||http://purl.uniprot.org/annotation/VAR_056142|||http://purl.uniprot.org/annotation/VAR_056143|||http://purl.uniprot.org/annotation/VAR_056144|||http://purl.uniprot.org/annotation/VAR_061348|||http://purl.uniprot.org/annotation/VAR_069708|||http://purl.uniprot.org/annotation/VSP_017542|||http://purl.uniprot.org/annotation/VSP_038853|||http://purl.uniprot.org/annotation/VSP_038854
http://togogenome.org/gene/9606:FGF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVY2|||http://purl.uniprot.org/uniprot/P21781                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fibroblast growth factor|||Fibroblast growth factor 7|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008965|||http://purl.uniprot.org/annotation/PRO_5031603812|||http://purl.uniprot.org/annotation/VAR_049063|||http://purl.uniprot.org/annotation/VAR_071038|||http://purl.uniprot.org/annotation/VSP_055090
http://togogenome.org/gene/9606:NXPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95156                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  II|||III|||IV (linker domain)|||N-linked (GlcNAc...) asparagine|||Neurexophilin-2|||V (Cys-rich)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020063
http://togogenome.org/gene/9606:TGIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15583                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  CTBP-binding motif|||Disordered|||Homeobox protein TGIF1|||Homeobox; TALE-type|||In HPE4.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049318|||http://purl.uniprot.org/annotation/VAR_009961|||http://purl.uniprot.org/annotation/VAR_009962|||http://purl.uniprot.org/annotation/VAR_009963|||http://purl.uniprot.org/annotation/VAR_009964|||http://purl.uniprot.org/annotation/VAR_020151|||http://purl.uniprot.org/annotation/VAR_023803|||http://purl.uniprot.org/annotation/VAR_047363|||http://purl.uniprot.org/annotation/VAR_061268|||http://purl.uniprot.org/annotation/VSP_013020|||http://purl.uniprot.org/annotation/VSP_013021|||http://purl.uniprot.org/annotation/VSP_043108|||http://purl.uniprot.org/annotation/VSP_043109|||http://purl.uniprot.org/annotation/VSP_046848
http://togogenome.org/gene/9606:FCRLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6BAA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fc receptor-like B|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332992|||http://purl.uniprot.org/annotation/VSP_033419|||http://purl.uniprot.org/annotation/VSP_033420|||http://purl.uniprot.org/annotation/VSP_033421|||http://purl.uniprot.org/annotation/VSP_033422|||http://purl.uniprot.org/annotation/VSP_033423
http://togogenome.org/gene/9606:KRTAP6-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI66                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 6-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223899
http://togogenome.org/gene/9606:MDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTM1|||http://purl.uniprot.org/uniprot/G3XAL0|||http://purl.uniprot.org/uniprot/P40926                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In DEE51; decreased protein abundance; strong decrease in malate dehydrogenase activity; severe defects in aerobic respiration, when assayed in a heterologous system.|||In DEE51; severe defects in aerobic respiration, when assayed in a heterologous system.|||In isoform 2.|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||Malate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-307.|||No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-314.|||No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-307 and R-314.|||No activation of enzyme activity on treatment with TSA or NAM; when associated with R-301; R-307 and R-314.|||O-linked (GlcNAc) serine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018628|||http://purl.uniprot.org/annotation/VAR_047787|||http://purl.uniprot.org/annotation/VAR_078001|||http://purl.uniprot.org/annotation/VAR_078002|||http://purl.uniprot.org/annotation/VAR_078003|||http://purl.uniprot.org/annotation/VSP_055312
http://togogenome.org/gene/9606:GPR68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5B2|||http://purl.uniprot.org/uniprot/Q15743                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Failed to stimulate IP formation at pH 6.8, activity is restored at more acid pH.|||Found in a renal cell carcinoma case; somatic mutation.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In AI2A6.|||N-linked (GlcNAc...) asparagine|||No effect on pH-sensing activity.|||Ovarian cancer G-protein coupled receptor 1|||Severe loss pH-sensing activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070113|||http://purl.uniprot.org/annotation/VAR_058714|||http://purl.uniprot.org/annotation/VAR_064716|||http://purl.uniprot.org/annotation/VAR_077874
http://togogenome.org/gene/9606:SERPINF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF3|||http://purl.uniprot.org/uniprot/P36955                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Confirmed at protein level.|||Disordered|||N-linked (GlcNAc...) (complex) asparagine|||O-glycosylated at one site|||Phosphoserine; by CK2|||Phosphoserine; by PKA|||Pigment epithelium-derived factor|||Pyrrolidone carboxylic acid|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032508|||http://purl.uniprot.org/annotation/PRO_5007491844|||http://purl.uniprot.org/annotation/VAR_009126|||http://purl.uniprot.org/annotation/VAR_025500
http://togogenome.org/gene/9606:PDE10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B1UZR0|||http://purl.uniprot.org/uniprot/Q9Y233                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GAF 1|||GAF 2|||In ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding.|||In IOLOD; decreased protein abundance.|||In isoform PDE10A2.|||Loss of activity and of zinc binding.|||PDEase|||Phosphothreonine|||Proton donor|||Reduces activity 1000-fold.|||cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198843|||http://purl.uniprot.org/annotation/VAR_008797|||http://purl.uniprot.org/annotation/VAR_047822|||http://purl.uniprot.org/annotation/VAR_047823|||http://purl.uniprot.org/annotation/VAR_076798|||http://purl.uniprot.org/annotation/VAR_076799|||http://purl.uniprot.org/annotation/VAR_076800|||http://purl.uniprot.org/annotation/VAR_076801|||http://purl.uniprot.org/annotation/VSP_004601
http://togogenome.org/gene/9606:ZNF354A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60765|||http://purl.uniprot.org/uniprot/V9HWI2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Polar residues|||Zinc finger protein 354A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047238
http://togogenome.org/gene/9606:CUEDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AHX0|||http://purl.uniprot.org/uniprot/Q9NWM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  CUE|||CUE domain-containing protein 1|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079559|||http://purl.uniprot.org/annotation/VAR_021951|||http://purl.uniprot.org/annotation/VAR_033765|||http://purl.uniprot.org/annotation/VAR_050933|||http://purl.uniprot.org/annotation/VSP_010316
http://togogenome.org/gene/9606:UNC45A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3U1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with HSP90AB1; when associated with D-40. No effect on interaction with PGR.|||Abolishes interaction with HSP90AB1; when associated with D-77. No effect on interaction with PGR.|||Abolishes interaction with HSP90AB1; when associated with E-33. No effect on interaction with PGR.|||Abolishes interaction with HSP90AB1; when associated with E-70. No effect on interaction with PGR.|||Disordered|||In OOHE; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphothreonine|||Protein unc-45 homolog A|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249888|||http://purl.uniprot.org/annotation/VAR_052629|||http://purl.uniprot.org/annotation/VAR_086010|||http://purl.uniprot.org/annotation/VAR_086011|||http://purl.uniprot.org/annotation/VAR_086012|||http://purl.uniprot.org/annotation/VAR_086013|||http://purl.uniprot.org/annotation/VAR_086014|||http://purl.uniprot.org/annotation/VAR_086015|||http://purl.uniprot.org/annotation/VAR_086016|||http://purl.uniprot.org/annotation/VSP_020584|||http://purl.uniprot.org/annotation/VSP_020585
http://togogenome.org/gene/9606:CFAP141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU69                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270966
http://togogenome.org/gene/9606:DPEP2NB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RQF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||DPEP2 neighbor protein|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444871
http://togogenome.org/gene/9606:BTN2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7KYR7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin subfamily 2 member A1|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014529|||http://purl.uniprot.org/annotation/VAR_049825|||http://purl.uniprot.org/annotation/VAR_049826|||http://purl.uniprot.org/annotation/VAR_049827|||http://purl.uniprot.org/annotation/VAR_049828|||http://purl.uniprot.org/annotation/VAR_061303|||http://purl.uniprot.org/annotation/VAR_061304|||http://purl.uniprot.org/annotation/VSP_012708|||http://purl.uniprot.org/annotation/VSP_035843|||http://purl.uniprot.org/annotation/VSP_035844|||http://purl.uniprot.org/annotation/VSP_043165|||http://purl.uniprot.org/annotation/VSP_043166|||http://purl.uniprot.org/annotation/VSP_044249|||http://purl.uniprot.org/annotation/VSP_045005|||http://purl.uniprot.org/annotation/VSP_045006
http://togogenome.org/gene/9606:CEP295                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ALMS motif|||Basic and acidic residues|||Centrosomal protein of 295 kDa|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Necessary for centriole targeting and microtubule association|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324595|||http://purl.uniprot.org/annotation/VAR_059337|||http://purl.uniprot.org/annotation/VAR_059338|||http://purl.uniprot.org/annotation/VAR_059339|||http://purl.uniprot.org/annotation/VAR_059340|||http://purl.uniprot.org/annotation/VAR_059341|||http://purl.uniprot.org/annotation/VAR_059342|||http://purl.uniprot.org/annotation/VAR_059343|||http://purl.uniprot.org/annotation/VSP_032288|||http://purl.uniprot.org/annotation/VSP_032289|||http://purl.uniprot.org/annotation/VSP_032290|||http://purl.uniprot.org/annotation/VSP_032291
http://togogenome.org/gene/9606:NOS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0S0A6|||http://purl.uniprot.org/uniprot/P29474                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||FAD-binding FR-type|||Flavodoxin-like|||Found in a colorectal cancer sample; somatic mutation.|||In isoform eNOS13B.|||In isoform eNOS13C.|||Interaction with NOSIP|||N-myristoyl glycine|||Nitric oxide synthase 3|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by CDK5|||Phosphothreonine|||Phosphothreonine; by AMPK|||Pro residues|||Reduced nitrite (NO) production.|||Removed|||S-palmitoyl cysteine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170943|||http://purl.uniprot.org/annotation/VAR_008037|||http://purl.uniprot.org/annotation/VAR_031218|||http://purl.uniprot.org/annotation/VAR_031219|||http://purl.uniprot.org/annotation/VAR_031220|||http://purl.uniprot.org/annotation/VAR_031221|||http://purl.uniprot.org/annotation/VAR_036303|||http://purl.uniprot.org/annotation/VAR_036304|||http://purl.uniprot.org/annotation/VAR_061377|||http://purl.uniprot.org/annotation/VSP_042625|||http://purl.uniprot.org/annotation/VSP_042626|||http://purl.uniprot.org/annotation/VSP_045495|||http://purl.uniprot.org/annotation/VSP_045496
http://togogenome.org/gene/9606:ISYNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK73|||http://purl.uniprot.org/uniprot/Q9NPH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreases activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Inositol-3-phosphate synthase 1|||Myo-inositol-1-phosphate synthase GAPDH-like|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324628|||http://purl.uniprot.org/annotation/VSP_032324|||http://purl.uniprot.org/annotation/VSP_046065
http://togogenome.org/gene/9606:EBF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4W6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C5-type|||Disordered|||IPT/TIG|||In HADDS; according to PubMed:28017373 shows significant loss of transcriptional activator activity while according to PubMed:28017370 shows partial loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding.|||In HADDS; loss of transcriptional activator activity.|||In HADDS; partial loss of transcriptional activator activity.|||In HADDS; significant loss of transcriptional activator activity.|||In HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin binding.|||In HADDS; significant loss of transcriptional activator activity; localizes both in the cytoplasm and the nucleus; decreased chromatin-binding.|||In isoform Short.|||Interaction with DNA|||Transcription factor COE3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107832|||http://purl.uniprot.org/annotation/VAR_078033|||http://purl.uniprot.org/annotation/VAR_078034|||http://purl.uniprot.org/annotation/VAR_078035|||http://purl.uniprot.org/annotation/VAR_078036|||http://purl.uniprot.org/annotation/VAR_078037|||http://purl.uniprot.org/annotation/VAR_078038|||http://purl.uniprot.org/annotation/VAR_078039|||http://purl.uniprot.org/annotation/VAR_078040|||http://purl.uniprot.org/annotation/VAR_078041|||http://purl.uniprot.org/annotation/VAR_078042|||http://purl.uniprot.org/annotation/VSP_001113|||http://purl.uniprot.org/annotation/VSP_001114
http://togogenome.org/gene/9606:TMEM267                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VDI3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 267                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281921
http://togogenome.org/gene/9606:UXT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBK9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Causes dislocation from the centrosome; when associated with L-50.|||Causes dislocation from the centrosome; when associated with L-59.|||In isoform 1.|||Protein UXT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065751|||http://purl.uniprot.org/annotation/VSP_059081
http://togogenome.org/gene/9606:OSCAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV17|||http://purl.uniprot.org/uniprot/A0A087X1R2|||http://purl.uniprot.org/uniprot/A0A0A0MR14|||http://purl.uniprot.org/uniprot/A0A0A0MRF2|||http://purl.uniprot.org/uniprot/Q8IYS5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Ig-like|||Ig-like 1|||Ig-like 2|||Immunoglobulin subtype|||In isoform 2, isoform 3 and isoform 6.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 6.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Osteoclast-associated immunoglobulin-like receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310951|||http://purl.uniprot.org/annotation/PRO_5001967220|||http://purl.uniprot.org/annotation/PRO_5001974155|||http://purl.uniprot.org/annotation/PRO_5014013272|||http://purl.uniprot.org/annotation/PRO_5014013292|||http://purl.uniprot.org/annotation/VAR_037108|||http://purl.uniprot.org/annotation/VAR_047393|||http://purl.uniprot.org/annotation/VSP_029352|||http://purl.uniprot.org/annotation/VSP_029353|||http://purl.uniprot.org/annotation/VSP_029354|||http://purl.uniprot.org/annotation/VSP_029355
http://togogenome.org/gene/9606:ZDHHC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUH5                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Abolishes SNAP25 and HTT binding.|||Abolishes SNAP25 binding.|||Abolishes palmitoyltransferase activity.|||Cytoplasmic|||DHHC|||Decreased binding affinity for SNAP25.|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Mildly decreased binding affinity for SNAP25.|||Necessary and sufficient for interaction with DNAJC5 and SNAP25|||No effect on SNAP25 binding.|||Palmitoyltransferase ZDHHC17|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212900|||http://purl.uniprot.org/annotation/VAR_052978|||http://purl.uniprot.org/annotation/VSP_010021|||http://purl.uniprot.org/annotation/VSP_010022|||http://purl.uniprot.org/annotation/VSP_010023|||http://purl.uniprot.org/annotation/VSP_010024|||http://purl.uniprot.org/annotation/VSP_010025
http://togogenome.org/gene/9606:STX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2W9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Syntaxin-18|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210231|||http://purl.uniprot.org/annotation/VAR_052250|||http://purl.uniprot.org/annotation/VAR_052251|||http://purl.uniprot.org/annotation/VAR_052252
http://togogenome.org/gene/9606:CDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3D6|||http://purl.uniprot.org/uniprot/I6L9I5|||http://purl.uniprot.org/uniprot/P06493                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abnormal cell cycle exhibiting only M-phase without completing either karyokinesis or cytokinesis.|||Constitutive polyubiquitination.|||Cyclin-dependent kinase 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CAK|||Phosphothreonine; by PKMYT1|||Phosphotyrosine|||Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCD|||Phosphotyrosine; by PKR|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085724|||http://purl.uniprot.org/annotation/VSP_021375
http://togogenome.org/gene/9606:HAUS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6D7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  HAUS augmin-like complex subunit 4|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089901|||http://purl.uniprot.org/annotation/VSP_007851|||http://purl.uniprot.org/annotation/VSP_007852|||http://purl.uniprot.org/annotation/VSP_007853
http://togogenome.org/gene/9606:UNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0B0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Disordered|||Phosphoserine|||Polar residues|||RING finger protein unkempt homolog|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213899
http://togogenome.org/gene/9606:G3BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic disordered region|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform B.|||N6-succinyllysine|||NTF2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RG-rich region|||RRM|||Ras GTPase-activating protein-binding protein 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194800|||http://purl.uniprot.org/annotation/VAR_036128|||http://purl.uniprot.org/annotation/VSP_003605
http://togogenome.org/gene/9606:PSMA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAA3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Proteasome subunit alpha-type 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124149|||http://purl.uniprot.org/annotation/VSP_005285|||http://purl.uniprot.org/annotation/VSP_018602
http://togogenome.org/gene/9606:PNO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||KH|||N-acetylmethionine|||RNA-binding protein PNO1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270540|||http://purl.uniprot.org/annotation/VAR_029814|||http://purl.uniprot.org/annotation/VAR_029815
http://togogenome.org/gene/9606:TTC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A3L6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tetratricopeptide repeat protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307771|||http://purl.uniprot.org/annotation/VAR_036643|||http://purl.uniprot.org/annotation/VAR_036644|||http://purl.uniprot.org/annotation/VAR_036645
http://togogenome.org/gene/9606:ITGA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN28|||http://purl.uniprot.org/uniprot/P53708                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||Helical|||In RHDA1; the mutant does not localize at the cell membrane.|||In RHDA1; unknown pathological significance.|||Integrin alpha-2|||Integrin alpha-8|||Integrin alpha-8 heavy chain|||Integrin alpha-8 light chain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016310|||http://purl.uniprot.org/annotation/PRO_0000016311|||http://purl.uniprot.org/annotation/PRO_0000016312|||http://purl.uniprot.org/annotation/PRO_5002803433|||http://purl.uniprot.org/annotation/VAR_018673|||http://purl.uniprot.org/annotation/VAR_018674|||http://purl.uniprot.org/annotation/VAR_018675|||http://purl.uniprot.org/annotation/VAR_018676|||http://purl.uniprot.org/annotation/VAR_018677|||http://purl.uniprot.org/annotation/VAR_018678|||http://purl.uniprot.org/annotation/VAR_034682|||http://purl.uniprot.org/annotation/VAR_071106|||http://purl.uniprot.org/annotation/VAR_071107
http://togogenome.org/gene/9606:MN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10571                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In CEBALID.|||In CEBALID; increased protein aggregation; decreased protein degradation via the ubiquitin-proteasome pathway; loss of interaction with RING1; decreased interaction with ZBTB24; no effect on nuclear localization.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Transcriptional activator MN1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096521|||http://purl.uniprot.org/annotation/VAR_047533|||http://purl.uniprot.org/annotation/VAR_083776|||http://purl.uniprot.org/annotation/VAR_083777|||http://purl.uniprot.org/annotation/VAR_083778|||http://purl.uniprot.org/annotation/VAR_083779|||http://purl.uniprot.org/annotation/VAR_083780|||http://purl.uniprot.org/annotation/VAR_083781|||http://purl.uniprot.org/annotation/VAR_083782
http://togogenome.org/gene/9606:THRSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92748                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Thyroid hormone-inducible hepatic protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123773
http://togogenome.org/gene/9606:RNF212                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495C1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Probable E3 SUMO-protein ligase RNF212|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274612|||http://purl.uniprot.org/annotation/VAR_059815|||http://purl.uniprot.org/annotation/VSP_022839|||http://purl.uniprot.org/annotation/VSP_022840|||http://purl.uniprot.org/annotation/VSP_022841|||http://purl.uniprot.org/annotation/VSP_022842|||http://purl.uniprot.org/annotation/VSP_022843|||http://purl.uniprot.org/annotation/VSP_022844|||http://purl.uniprot.org/annotation/VSP_046301
http://togogenome.org/gene/9606:DHX37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY37                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Impairs the catalytic activity of the helicase.|||In NEDBAVC; unknown pathological significance.|||In NEDBAVC; unknown pathological significance; requires 2 nucleotide substitutions.|||In SRXY11.|||In SRXY11; unknown pathological significance.|||Pro residues|||Probable ATP-dependent RNA helicase DHX37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055172|||http://purl.uniprot.org/annotation/VAR_052185|||http://purl.uniprot.org/annotation/VAR_052186|||http://purl.uniprot.org/annotation/VAR_052187|||http://purl.uniprot.org/annotation/VAR_052188|||http://purl.uniprot.org/annotation/VAR_052189|||http://purl.uniprot.org/annotation/VAR_061826|||http://purl.uniprot.org/annotation/VAR_083628|||http://purl.uniprot.org/annotation/VAR_083629|||http://purl.uniprot.org/annotation/VAR_083630|||http://purl.uniprot.org/annotation/VAR_083631|||http://purl.uniprot.org/annotation/VAR_083632|||http://purl.uniprot.org/annotation/VAR_083633|||http://purl.uniprot.org/annotation/VAR_083634|||http://purl.uniprot.org/annotation/VAR_083635|||http://purl.uniprot.org/annotation/VAR_083636|||http://purl.uniprot.org/annotation/VAR_083637|||http://purl.uniprot.org/annotation/VAR_083638|||http://purl.uniprot.org/annotation/VAR_083639|||http://purl.uniprot.org/annotation/VAR_083640|||http://purl.uniprot.org/annotation/VAR_083641|||http://purl.uniprot.org/annotation/VAR_083642|||http://purl.uniprot.org/annotation/VAR_083643|||http://purl.uniprot.org/annotation/VAR_083644
http://togogenome.org/gene/9606:EQTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ60                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Equatorin|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286593|||http://purl.uniprot.org/annotation/VAR_032136|||http://purl.uniprot.org/annotation/VAR_032137|||http://purl.uniprot.org/annotation/VAR_056727|||http://purl.uniprot.org/annotation/VSP_025109|||http://purl.uniprot.org/annotation/VSP_025110|||http://purl.uniprot.org/annotation/VSP_042157
http://togogenome.org/gene/9606:ZNF76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36508                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||3 X 12 AA approximate repeats|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||Zinc finger protein 76                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047386|||http://purl.uniprot.org/annotation/VAR_033546|||http://purl.uniprot.org/annotation/VAR_033547|||http://purl.uniprot.org/annotation/VAR_033548|||http://purl.uniprot.org/annotation/VSP_006894
http://togogenome.org/gene/9606:KRBOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JBD0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||KRAB|||KRAB domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000404593|||http://purl.uniprot.org/annotation/VSP_040580
http://togogenome.org/gene/9606:GRAPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QRP9|||http://purl.uniprot.org/uniprot/Q8TC17                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GRB2-related adapter protein-like|||In isoform 2.|||SH2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344236|||http://purl.uniprot.org/annotation/VSP_039172
http://togogenome.org/gene/9606:TIGIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495A1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abrogates interaction with PVR, cell clustering and PVR signaling.|||Cytoplasmic|||Extracellular|||Helical|||Homodimerization|||ITIM motif|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||T-cell immunoreceptor with Ig and ITIM domains                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299405|||http://purl.uniprot.org/annotation/VAR_056079|||http://purl.uniprot.org/annotation/VSP_027634|||http://purl.uniprot.org/annotation/VSP_027635
http://togogenome.org/gene/9606:DDX17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5H1ZRQ2|||http://purl.uniprot.org/uniprot/Q59F66|||http://purl.uniprot.org/uniprot/Q92841                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEAD box|||DEAD-box RNA helicase Q|||Decreased CD44 alternative splicing.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||Impaired sumoylation and decreased stability. Impairs interaction with HDAC1, but not with HDAC2, nor HDAC3. No effect on EP300-, ESR1-, DDX5- and YAP1-binding.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with YAP1|||Loss of helicase activity. Loss of splicing regulation in the estrogen signaling pathway. Reduced CD44 alternative splicing regulation. Does not promote ZCH3HAV1-mediated RNA degradation.|||Loss of helicase activity. No effect on ESR1 coactivation.|||N6-acetyllysine; by EP300|||No effect on HDAC1-, HDAC2- nor HDAC3-binding, decreased ESR1 coactivation, strongly decreased TP53 coactivation. Complete loss of lysine acetylation, decreased stability, loss of ESR1 and TP53 coactivation and loss of HDAC1- and HDAC3-binding, no effect on HDAC2-binding; when associated with 108-R-R-109.|||No effect on HDAC1-, HDAC2- nor HDAC3-binding, small decrease in ESR1 coactivation, decreased TP53 coactivation. Complete loss of lysine acetylation, decreased stability, loss of ESR1 and TP53 coactivation and loss of HDAC1- and HDAC3-binding, no effect on HDAC2-binding; when associated with R-121.|||No effect on transcription activation, when assayed in luciferase reporter gene assays using MDM2 or FOS promoters, either alone or in the presence of EP300 and KAT2B.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Probable ATP-dependent RNA helicase DDX17|||Q motif|||RNA helicase|||Small decrease in CD44 alternative splicing.|||Transactivation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054993|||http://purl.uniprot.org/annotation/PRO_5029464524|||http://purl.uniprot.org/annotation/VSP_042527|||http://purl.uniprot.org/annotation/VSP_042528|||http://purl.uniprot.org/annotation/VSP_042529
http://togogenome.org/gene/9606:DEDD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AQP5|||http://purl.uniprot.org/uniprot/O75618                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DED|||Death effector domain-containing protein|||Disordered|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191274|||http://purl.uniprot.org/annotation/VSP_003846
http://togogenome.org/gene/9606:NUDT18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVK8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  8-oxo-dGDP phosphatase NUDT18|||In isoform 2.|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324567|||http://purl.uniprot.org/annotation/VSP_032276|||http://purl.uniprot.org/annotation/VSP_032277
http://togogenome.org/gene/9606:PDK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15119                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Histidine kinase|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||Phosphotyrosine|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023440|||http://purl.uniprot.org/annotation/VAR_042296|||http://purl.uniprot.org/annotation/VSP_042549
http://togogenome.org/gene/9606:MAFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Q3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In MCTO.|||Leucine-zipper|||Polar residues|||Transcription factor MafB|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076494|||http://purl.uniprot.org/annotation/VAR_067979|||http://purl.uniprot.org/annotation/VAR_067980|||http://purl.uniprot.org/annotation/VAR_067981|||http://purl.uniprot.org/annotation/VAR_067982|||http://purl.uniprot.org/annotation/VAR_067983|||http://purl.uniprot.org/annotation/VAR_067984|||http://purl.uniprot.org/annotation/VAR_067985|||http://purl.uniprot.org/annotation/VAR_067986|||http://purl.uniprot.org/annotation/VAR_067987|||http://purl.uniprot.org/annotation/VAR_067988
http://togogenome.org/gene/9606:GABBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7R0|||http://purl.uniprot.org/uniprot/C9J342|||http://purl.uniprot.org/uniprot/Q59HG8|||http://purl.uniprot.org/uniprot/Q5SUJ9|||http://purl.uniprot.org/uniprot/Q8IW08|||http://purl.uniprot.org/uniprot/Q9UBS5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes signaling via G-proteins. Abolishes antagonist binding.|||Cytoplasmic|||Decreases signaling via G-proteins.|||Disordered|||Extracellular|||G-protein coupled receptors family 3 profile|||Gamma-aminobutyric acid type B receptor subunit 1|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 1B.|||In isoform 1C.|||In isoform 1D.|||In isoform 1E.|||Interaction with ATF4|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues|||Pro residues|||Slightly decreases signaling via G-proteins.|||Strongly reduces signaling via G-proteins. Abolishes antagonist binding.|||Strongly reduces signaling via G-proteins. No effect on antagonist binding.|||Strongly reduces signaling via G-proteins. Strongly reduces antagonist binding.|||Sushi|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012949|||http://purl.uniprot.org/annotation/PRO_5004310329|||http://purl.uniprot.org/annotation/PRO_5014275535|||http://purl.uniprot.org/annotation/PRO_5014309961|||http://purl.uniprot.org/annotation/PRO_5040213691|||http://purl.uniprot.org/annotation/VAR_010146|||http://purl.uniprot.org/annotation/VAR_010147|||http://purl.uniprot.org/annotation/VAR_049279|||http://purl.uniprot.org/annotation/VSP_002037|||http://purl.uniprot.org/annotation/VSP_002038|||http://purl.uniprot.org/annotation/VSP_002039|||http://purl.uniprot.org/annotation/VSP_002040
http://togogenome.org/gene/9606:ARRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49407                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with AP2B1.|||Basic and acidic residues|||Beta-arrestin-1|||Constitutive active; enables phosphorylation-independent binding to GPCRs.|||Disordered|||In isoform 1B.|||Interaction with CHRM2|||Interaction with SRC|||Interaction with TRAF6|||Phosphoserine; by GRK5|||Phosphotyrosine|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205194|||http://purl.uniprot.org/annotation/VSP_000322
http://togogenome.org/gene/9606:SIRT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXA8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes desuccinylation and deglutarylation activity.|||Abolishes enzyme activity.|||Deacetylase sirtuin-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increases the KM for desuccinylation.|||Increases the KM for desuccinylation. Does not affect deacetylase activity.|||Mitochondrion|||NAD-dependent protein deacylase sirtuin-5, mitochondrial|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110266|||http://purl.uniprot.org/annotation/VAR_029042|||http://purl.uniprot.org/annotation/VAR_051980|||http://purl.uniprot.org/annotation/VSP_008730|||http://purl.uniprot.org/annotation/VSP_008731|||http://purl.uniprot.org/annotation/VSP_042291|||http://purl.uniprot.org/annotation/VSP_042292
http://togogenome.org/gene/9606:PHOX2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14813                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In CFEOM2.|||May be involved in congenital central hypoventilation syndrome.|||Paired mesoderm homeobox protein 2A|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049259|||http://purl.uniprot.org/annotation/VAR_019014|||http://purl.uniprot.org/annotation/VAR_019016
http://togogenome.org/gene/9606:LRRC71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8H7|||http://purl.uniprot.org/uniprot/Q8N4P6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 71|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284542|||http://purl.uniprot.org/annotation/VAR_031773|||http://purl.uniprot.org/annotation/VAR_031774|||http://purl.uniprot.org/annotation/VAR_059593|||http://purl.uniprot.org/annotation/VSP_024560|||http://purl.uniprot.org/annotation/VSP_024561|||http://purl.uniprot.org/annotation/VSP_024562
http://togogenome.org/gene/9606:SLC35E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K37                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Solute carrier family 35 member E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071941|||http://purl.uniprot.org/annotation/VSP_010139|||http://purl.uniprot.org/annotation/VSP_010140|||http://purl.uniprot.org/annotation/VSP_010141|||http://purl.uniprot.org/annotation/VSP_031351
http://togogenome.org/gene/9606:PRH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV42|||http://purl.uniprot.org/uniprot/F1T0A8|||http://purl.uniprot.org/uniprot/P02810                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Decreased phosphorylation by FAM20C; when associated with A-24.|||Decreased phosphorylation by FAM20C; when associated with A-38.|||Disordered|||In allele PRH1-DB.|||In allele PRH1-PA and allele PRH1-DB.|||In allele PRH1-PA; interferes with proteolytic cleavage at Arg-122.|||In allele PRH1-PIF, allele PRH1-PA and allele PRH1-DB.|||In allele PRH2-2.|||In allele PRH2-3.|||Inhibits hydroxyapatite formation, binds to hydroxyapatite and calcium|||O-linked (GlcA) serine; alternate|||Peptide P-C|||Phosphoserine; alternate|||Phosphoserine; by FAM20C|||Phosphoserine; by FAM20C; alternate|||Polar residues|||Pro residues|||Pyrrolidone carboxylic acid|||Salivary acidic proline-rich phosphoprotein 1/2|||Salivary acidic proline-rich phosphoprotein 3/4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022137|||http://purl.uniprot.org/annotation/PRO_0000022138|||http://purl.uniprot.org/annotation/PRO_0000022139|||http://purl.uniprot.org/annotation/PRO_5014218800|||http://purl.uniprot.org/annotation/VAR_005563|||http://purl.uniprot.org/annotation/VAR_005564|||http://purl.uniprot.org/annotation/VAR_005565|||http://purl.uniprot.org/annotation/VAR_023240|||http://purl.uniprot.org/annotation/VAR_023241|||http://purl.uniprot.org/annotation/VAR_023242
http://togogenome.org/gene/9606:MUC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||Disordered|||Mucin-7|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc) serine; by GALNT13|||O-linked (GalNAc) threonine; by GALNT13|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239228|||http://purl.uniprot.org/annotation/VAR_050451
http://togogenome.org/gene/9606:TRAIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished ability to regulate nuclear envelope breakdown to anaphase.|||Abolished accumulation in nucleolus.|||Abolished interaction with PCNA and localization to DNA damage sites.|||Abolished interaction with PCNA.|||Abolished sumoylation and localization to the nucleus; when associated with A-127, A-205, A-247 and A-462.|||Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-205 and A-247.|||Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-205 and A-462.|||Abolished sumoylation and localization to the nucleus; when associated with A-80, A-127, A-247 and A-462.|||Abolished sumoylation and localization to the nucleus; when associated with A-80, A-205, A-247 and A-462.|||E3 ubiquitin-protein ligase TRAIP|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In SCKL9; abolished localization to the nucleolus.|||Interaction with CYLD|||PIP-box|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056191|||http://purl.uniprot.org/annotation/VAR_076530
http://togogenome.org/gene/9606:EEF1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68104|||http://purl.uniprot.org/uniprot/Q6IPS9                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  5-glutamyl glycerylphosphorylethanolamine|||Abolishes methylation by EEF1AKMT2.|||Abolishes methylation by EEF1AKMT3.|||Abolishes phosphorylation by PASK.|||Elongation factor 1-alpha 1|||G1|||G2|||G3|||G4|||G5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ubiquitination in response to ribosome stalling caused by ternatin-4.|||N,N,N-trimethylglycine|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3|||N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT4|||N6,N6,N6-trimethyllysine; by EEF1AKMT1|||N6,N6,N6-trimethyllysine; by EEF1AKMT2|||N6,N6-dimethyllysine|||N6,N6-dimethyllysine; alternate; by EEF1AKMT3|||N6,N6-dimethyllysine; alternate; by EEF1AKMT4|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate; by EEF1AKMT3|||N6-methyllysine; alternate; by EEF1AKMT4|||N6-succinyllysine; alternate|||No effect on methylation by EEF1AKMT2.|||No effect on methylation by EEF1AKMT2. Abolishes EEF1AKMT4-mediated methylation.|||No effect on methylation by EEF1AKMT2. Abolishes methylation by METTL13.|||Phosphoserine; by TGFBR1|||Phosphothreonine; by PASK|||Removed|||Resistant to inhibition by plitidepsin and ternatin-4. No effect on SARS-CoV-2 proteins translation.|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090885
http://togogenome.org/gene/9606:ZNF337                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5C0|||http://purl.uniprot.org/uniprot/Q6ZUQ0|||http://purl.uniprot.org/uniprot/Q9Y3M9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 337                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047540|||http://purl.uniprot.org/annotation/VAR_024213|||http://purl.uniprot.org/annotation/VAR_052814|||http://purl.uniprot.org/annotation/VSP_055949
http://togogenome.org/gene/9606:C6orf163                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TEZ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Uncharacterized protein C6orf163                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271361
http://togogenome.org/gene/9606:SH3RF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase SH3RF3|||Interaction with RAC1|||Phosphoserine|||Polar residues|||RING-type|||Reduced JNK activation. Significant loss of interaction with RAC1; alone or when associated with N-403 and A-406.|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||Significant loss of interaction with RAC1; alone or when associated with P-404 and A-406.|||Significant loss of interaction with RAC1; when associated with N-403 and P-404.|||Significant reduction in autoubiquitination; when associated with A-73.|||Significant reduction in autoubiquitination; when associated with A-75.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284883
http://togogenome.org/gene/9606:MYH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12882                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Found in a renal cell carcinoma sample; somatic mutation.|||IQ|||In a breast cancer sample; somatic mutation.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-1|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123391|||http://purl.uniprot.org/annotation/VAR_030193|||http://purl.uniprot.org/annotation/VAR_030194|||http://purl.uniprot.org/annotation/VAR_030195|||http://purl.uniprot.org/annotation/VAR_036003|||http://purl.uniprot.org/annotation/VAR_036004|||http://purl.uniprot.org/annotation/VAR_036005|||http://purl.uniprot.org/annotation/VAR_054159|||http://purl.uniprot.org/annotation/VAR_064735
http://togogenome.org/gene/9606:CCDC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P6D6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307715|||http://purl.uniprot.org/annotation/VAR_050748|||http://purl.uniprot.org/annotation/VAR_050749|||http://purl.uniprot.org/annotation/VAR_069401
http://togogenome.org/gene/9606:HOXC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09630                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-C6|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200174|||http://purl.uniprot.org/annotation/VSP_002392
http://togogenome.org/gene/9606:VIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09327|||http://purl.uniprot.org/uniprot/Q53F91                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-604. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-604.|||Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-725.|||Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-604 and F-725.|||Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-555; F-604 and F-725.|||Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-461; F-555; F-604 and F-725.|||Core|||Does not reduce binding to PIP2.|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||Gelsolin-like 6|||HP|||Headpiece|||In isoform 2.|||Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 125-A--S-129.|||Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 86-N--E-91.|||Inhibits actin-severing activity. Does not inhibit actin-capping activity.|||Inhibits actin-severing activity. Does not inhibit actin-nucleation and actin-capping activities.|||Inhibits activities regarding actin capping and actin severing.|||Inhibits activities regarding actin capping, actin severing and actin bundling.|||LPA/PIP2-binding site 1|||LPA/PIP2-binding site 2|||LPA/PIP2-binding site 3|||Necessary for homodimerization|||Phosphoserine|||Reduces actin-severing activity and interaction with PLCG1. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-324; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-324; F-461; F-555; F-604 and F-725.|||Reduces activities regarding actin capping and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-81 and F-256.|||Reduces activities regarding actin capping and actin severing. Does not reduce lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-60; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-60; F-81 and F-256.|||Reduces activities regarding actin nucleating and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-256.|||Reduces activities regarding actin nucleation and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-81.|||Reduces binding to PIP2.|||Reduces interaction with F-actin.|||Reduces the Ca(2+)-dependent actin-severing activity.|||Removed|||Villin-1 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218727|||http://purl.uniprot.org/annotation/VAR_054502|||http://purl.uniprot.org/annotation/VSP_054436|||http://purl.uniprot.org/annotation/VSP_054437
http://togogenome.org/gene/9606:VWDE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2E2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||VWFD|||von Willebrand factor D and EGF domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329441|||http://purl.uniprot.org/annotation/VAR_047871|||http://purl.uniprot.org/annotation/VAR_047872|||http://purl.uniprot.org/annotation/VAR_047873|||http://purl.uniprot.org/annotation/VAR_047874|||http://purl.uniprot.org/annotation/VAR_071061|||http://purl.uniprot.org/annotation/VSP_055465
http://togogenome.org/gene/9606:GAPDHS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K1|||http://purl.uniprot.org/uniprot/O14556                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activates thiol group during catalysis|||Disordered|||Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding|||Glyceraldehyde-3-phosphate dehydrogenase, testis-specific|||Nucleophile|||Pro residues|||Testis-specific N-terminal extension                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145502|||http://purl.uniprot.org/annotation/VAR_049219
http://togogenome.org/gene/9606:FAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLR2|||http://purl.uniprot.org/uniprot/Q12884                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Antiplasmin-cleaving enzyme FAP, soluble form|||Charge relay system|||Cleavage|||Cytoplasmic|||Decreased plasma membrane expression; loss of homodimerization and dipeptidyl peptidase activity; mislocalized with the calnexin in the endoplasmic reticulum; causes induction of the unfolded protein response (UPR).|||Dipeptidylpeptidase IV N-terminal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Inhibits endopeptidase activity. Increases dipeptidyl peptidase activity.|||Inhibits endopeptidase activity. No change in dipeptidyl peptidase activity.|||N-linked (GlcNAc...) asparagine|||Peptidase S9 prolyl oligopeptidase catalytic|||Prolyl endopeptidase FAP|||Reduces dipeptidyl peptidase and endopeptidase activities.|||Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-203.|||Reduces dipeptidyl peptidase and endopeptidase activities. Does not inhibit cell adhesion, migration and invasion. Inhibits dipeptidyl peptidase and endopeptidase activities; when associated with A-204.|||Reduces dipeptidyl peptidase and gelatinolytic activities. Does not inhibit cell adhesion, migration and invasion.|||Strongly reduces endopeptidase activity. No change in dipeptidyl peptidase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122424|||http://purl.uniprot.org/annotation/PRO_0000430643|||http://purl.uniprot.org/annotation/VAR_071264|||http://purl.uniprot.org/annotation/VSP_005367
http://togogenome.org/gene/9606:DIP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3H2|||http://purl.uniprot.org/uniprot/Q96IB4|||http://purl.uniprot.org/uniprot/Q9P265                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Basic and acidic residues|||DMAP1-binding|||Disco-interacting protein 2 homolog B|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318736|||http://purl.uniprot.org/annotation/VAR_038861
http://togogenome.org/gene/9606:SRMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3Y6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Loss of kinase activity.|||Loss of kinase activity. Exhibits a diffused cytoplasmic localization. No effect on interaction with KHDRBS1 or VIM but abolishes tyrosine phosphorylation of both substrates.|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Significant reduction in phosphorylation.|||Tyrosine-protein kinase Srms                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088160|||http://purl.uniprot.org/annotation/VAR_041831|||http://purl.uniprot.org/annotation/VAR_041832|||http://purl.uniprot.org/annotation/VAR_041833|||http://purl.uniprot.org/annotation/VAR_041834|||http://purl.uniprot.org/annotation/VAR_041835|||http://purl.uniprot.org/annotation/VAR_041836|||http://purl.uniprot.org/annotation/VAR_041837|||http://purl.uniprot.org/annotation/VAR_041838|||http://purl.uniprot.org/annotation/VAR_041839|||http://purl.uniprot.org/annotation/VAR_041840|||http://purl.uniprot.org/annotation/VAR_051700|||http://purl.uniprot.org/annotation/VAR_051701|||http://purl.uniprot.org/annotation/VAR_051702
http://togogenome.org/gene/9606:ZSCAN20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17040                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||SCAN box|||Zinc finger and SCAN domain-containing protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047360|||http://purl.uniprot.org/annotation/VAR_054799|||http://purl.uniprot.org/annotation/VAR_054800|||http://purl.uniprot.org/annotation/VSP_036735|||http://purl.uniprot.org/annotation/VSP_036736|||http://purl.uniprot.org/annotation/VSP_036737|||http://purl.uniprot.org/annotation/VSP_036738|||http://purl.uniprot.org/annotation/VSP_036739
http://togogenome.org/gene/9606:NXNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ03                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nucleoredoxin-like protein 2|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229735|||http://purl.uniprot.org/annotation/VAR_025755|||http://purl.uniprot.org/annotation/VSP_039844
http://togogenome.org/gene/9606:HEATR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AI08                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT repeat-containing protein 6|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337173|||http://purl.uniprot.org/annotation/VAR_043670|||http://purl.uniprot.org/annotation/VAR_043671
http://togogenome.org/gene/9606:KIAA1328                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Protein hinderin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312298|||http://purl.uniprot.org/annotation/VAR_037483|||http://purl.uniprot.org/annotation/VSP_029809|||http://purl.uniprot.org/annotation/VSP_029810|||http://purl.uniprot.org/annotation/VSP_029811|||http://purl.uniprot.org/annotation/VSP_029812|||http://purl.uniprot.org/annotation/VSP_029813|||http://purl.uniprot.org/annotation/VSP_029814|||http://purl.uniprot.org/annotation/VSP_029815
http://togogenome.org/gene/9606:SLC39A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCX7|||http://purl.uniprot.org/uniprot/B4DZZ8|||http://purl.uniprot.org/uniprot/Q92504                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||In AGM9.|||In AGM9; decreased zinc ion transporter activity; does not affect localization to endoplasmic reticulum.|||In AGM9; unknown pathological significance.|||Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release.|||Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-275.|||Loss of phosphorylation in response to Zn(2+) treatment and of cytosolic Zn(2+) release; when associated with A-276.|||Phosphoserine; by CK2|||Pros-methylhistidine|||Zinc transporter SLC39A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213688|||http://purl.uniprot.org/annotation/VAR_050034|||http://purl.uniprot.org/annotation/VAR_050035|||http://purl.uniprot.org/annotation/VAR_050036|||http://purl.uniprot.org/annotation/VAR_086723|||http://purl.uniprot.org/annotation/VAR_086724|||http://purl.uniprot.org/annotation/VAR_086725|||http://purl.uniprot.org/annotation/VAR_086726|||http://purl.uniprot.org/annotation/VAR_086727|||http://purl.uniprot.org/annotation/VAR_086728|||http://purl.uniprot.org/annotation/VAR_086729
http://togogenome.org/gene/9606:MRPS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15235                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||Small ribosomal subunit protein uS12m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030606|||http://purl.uniprot.org/annotation/VAR_051820
http://togogenome.org/gene/9606:CFAP92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein CFAP92                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320679|||http://purl.uniprot.org/annotation/VSP_031739
http://togogenome.org/gene/9606:FAM236D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTK5|||http://purl.uniprot.org/uniprot/A0A1B0GUG4|||http://purl.uniprot.org/uniprot/P0DP71                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Protein FAM236C|||Protein FAM236D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440653|||http://purl.uniprot.org/annotation/PRO_0000440959
http://togogenome.org/gene/9606:ACOT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y305                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 9, mitochondrial|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053812|||http://purl.uniprot.org/annotation/VAR_062668|||http://purl.uniprot.org/annotation/VSP_036419|||http://purl.uniprot.org/annotation/VSP_036420|||http://purl.uniprot.org/annotation/VSP_041093
http://togogenome.org/gene/9606:APOBEC3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0MJ49|||http://purl.uniprot.org/uniprot/B7ZLZ1|||http://purl.uniprot.org/uniprot/P31941                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Altered deaminase activity and restriction activity towards genetic invaders.|||Altered deaminase activity.|||CMP/dCMP-type deaminase|||DNA dC->dU-editing enzyme APOBEC-3A|||In isoform 2.|||No effect on deaminase activity despite an altered restriction activity towards genetic invaders.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171752|||http://purl.uniprot.org/annotation/VAR_048721|||http://purl.uniprot.org/annotation/VSP_041723
http://togogenome.org/gene/9606:FAM219A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 7.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM219A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089676|||http://purl.uniprot.org/annotation/VSP_035492|||http://purl.uniprot.org/annotation/VSP_035493|||http://purl.uniprot.org/annotation/VSP_035494|||http://purl.uniprot.org/annotation/VSP_035495|||http://purl.uniprot.org/annotation/VSP_035496
http://togogenome.org/gene/9606:MORN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T089                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN repeat-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247454|||http://purl.uniprot.org/annotation/VAR_027105|||http://purl.uniprot.org/annotation/VAR_051199|||http://purl.uniprot.org/annotation/VSP_019994|||http://purl.uniprot.org/annotation/VSP_019995
http://togogenome.org/gene/9606:HAPLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10915                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Hyaluronan and proteoglycan link protein 1|||Ig-like V-type|||In a colorectal cancer sample; somatic mutation.|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013177|||http://purl.uniprot.org/annotation/PRO_0000013178|||http://purl.uniprot.org/annotation/VAR_036168|||http://purl.uniprot.org/annotation/VAR_049316
http://togogenome.org/gene/9606:PITPNM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZ72|||http://purl.uniprot.org/uniprot/Q9UF51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDHD|||Disordered|||In isoform 2.|||In isoform 3.|||Membrane-associated phosphatidylinositol transfer protein 2|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232741|||http://purl.uniprot.org/annotation/VAR_053584|||http://purl.uniprot.org/annotation/VAR_062131|||http://purl.uniprot.org/annotation/VSP_017961|||http://purl.uniprot.org/annotation/VSP_017962|||http://purl.uniprot.org/annotation/VSP_017963
http://togogenome.org/gene/9606:GLIPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48060                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Glioma pathogenesis-related protein 1|||Helical|||In isoform 2.|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006270|||http://purl.uniprot.org/annotation/VAR_048833|||http://purl.uniprot.org/annotation/VAR_061128|||http://purl.uniprot.org/annotation/VSP_043902
http://togogenome.org/gene/9606:RAB40C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S21                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with RNF7 and CUL5.|||Abolishes interaction with RNF7.|||Disordered|||In isoform 2.|||Polar residues|||Ras-related protein Rab-40C|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121261|||http://purl.uniprot.org/annotation/VSP_055835
http://togogenome.org/gene/9606:RGS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41220                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Changes specificity and confers GNAI1 binding; when associated with D-184. Strongly increases affinity for GNAI1 and GNAI3; when associated with D-184 and K-191.|||Changes specificity and confers GNAI1 binding; when associated with D-184. Strongly increases affinity for GNAI1 and GNAI3; when associated with S-106 and K-191.|||Decreases GTPase accelerating function but has no effect on translation inhibitory activity, suggesting that its role in translation is independent of its effects on G proteins.|||Disordered|||Impairs association with plasma membrane.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Likely benign variant; no effect on down-regulation of angiotensin-activated signaling pathway.|||Loss of isoform 1 expression.|||Loss of isoform 2 expression.|||Loss of isoform 3 expression.|||Loss of isoform 4 expression.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with E-86; L-87; S-90; K-102; F-105; I-110; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; K-102; F-105; I-110; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; F-105; I-110; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and E-111.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; I-110; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; S-90; K-102; F-105; I-110; E-111 and L-114.|||Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; L-87; S-90; K-102; F-105; I-110; E-111 and L-114.|||Necessary for membrane association|||Necessary to inhibit protein synthesis|||RGS|||Rare variant; unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; decreased RGS2 protein abundance.|||Rare variant; unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; reduced interaction with GNAQ.|||Regulator of G-protein signaling 2|||Strongly increases affinity for GNAI1 and GNAI3; when associated with S-106 and D-184.|||Unknown pathological significance; decreased down-regulation of angiotensin-activated signaling pathway; reduced localization at the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204178|||http://purl.uniprot.org/annotation/VAR_079238|||http://purl.uniprot.org/annotation/VAR_079239|||http://purl.uniprot.org/annotation/VAR_079240|||http://purl.uniprot.org/annotation/VAR_079241|||http://purl.uniprot.org/annotation/VAR_079242|||http://purl.uniprot.org/annotation/VAR_079243|||http://purl.uniprot.org/annotation/VAR_079244|||http://purl.uniprot.org/annotation/VAR_079245|||http://purl.uniprot.org/annotation/VAR_079246|||http://purl.uniprot.org/annotation/VAR_079247|||http://purl.uniprot.org/annotation/VAR_079248|||http://purl.uniprot.org/annotation/VAR_079249|||http://purl.uniprot.org/annotation/VAR_079250|||http://purl.uniprot.org/annotation/VAR_079251|||http://purl.uniprot.org/annotation/VAR_079252|||http://purl.uniprot.org/annotation/VAR_079253|||http://purl.uniprot.org/annotation/VSP_041296|||http://purl.uniprot.org/annotation/VSP_041297|||http://purl.uniprot.org/annotation/VSP_041298
http://togogenome.org/gene/9606:ARHGAP31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8S0MHV1|||http://purl.uniprot.org/uniprot/Q2M1Z3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 31|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320114|||http://purl.uniprot.org/annotation/VAR_039122|||http://purl.uniprot.org/annotation/VAR_039123|||http://purl.uniprot.org/annotation/VAR_039124|||http://purl.uniprot.org/annotation/VAR_039125|||http://purl.uniprot.org/annotation/VAR_039126|||http://purl.uniprot.org/annotation/VAR_065919
http://togogenome.org/gene/9606:LCE1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T753                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1E|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235328|||http://purl.uniprot.org/annotation/VAR_060066|||http://purl.uniprot.org/annotation/VAR_062117
http://togogenome.org/gene/9606:THNSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYQ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||Threonine synthase-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185646|||http://purl.uniprot.org/annotation/VAR_052545|||http://purl.uniprot.org/annotation/VAR_052546|||http://purl.uniprot.org/annotation/VAR_058869|||http://purl.uniprot.org/annotation/VAR_061893
http://togogenome.org/gene/9606:CLPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK11|||http://purl.uniprot.org/uniprot/Q9H078                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Autoinhibitory|||Cleavage; by PARL|||Clp ATPase C-terminal|||Decreased ATP hydrolysis activity. Loss of ATP-dependent protein disaggregase activity.|||In MGCA7A.|||In MGCA7A; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity.|||In MGCA7B.|||In MGCA7B; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; not changed mitochondrial respiration.|||In MGCA7B; increased ATP hydrolysis activity; severely decreased ATP-dependent protein disaggregase activity.|||In MGCA7B; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity.|||In MGCA7B; unknown pathological significance.|||In MGCA7B; unknown pathological significance; requires 2 nucleotide substitutions.|||In SCN9.|||In SCN9; decreased granulocyte differentiation; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; decreased mitochondrial respiration.|||In SCN9; decreased granulocyte differentiation; decreased ATP hydrolysis activity; decreased ATP-dependent protein disaggregase activity; does not render cells more sensitive to ER stress-induced apoptosis.|||In SCN9; decreased granulocyte differentiation; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity; decreased mitochondrial respiration.|||In SCN9; decreased granulocyte differentiation; loss of ATP hydrolysis activity; loss of ATP-dependent protein disaggregase activity; does not render cells more sensitive to ER stress-induced apoptosis.|||In SCN9; decreased mitochondrial respiration.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of ATP hydrolysis activity at pH 8.0. No effect on ATP hydrolysis activity at pH 6.8. Loss of ATP-dependent protein disaggregase activity at pH 8.0 and 6.8.|||Loss of ATP hydrolysis activity. Loss of ATP-dependent protein disaggregase activity.|||Mitochondrial disaggregase|||Mitochondrial disaggregase, cleaved form|||Mitochondrion|||N6-acetyllysine|||No effect on ATP hydrolysis activity. Loss of ATP-dependent protein disaggregase activity.|||No effect on ATPase activity but shows decreased disaggregase activity.|||Normal ATP hydrolysis activity; normal ATP-dependent protein disaggregase activity.|||Regulatory; slows ATPase and disaggregase activities|||Severely decreased ATP hydrolysis activity. Loss of ATP-dependent protein disaggregase activity.|||Shows higher order assembly but disaggregase activity is severely impaired by 70-80%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191239|||http://purl.uniprot.org/annotation/PRO_0000458241|||http://purl.uniprot.org/annotation/VAR_048740|||http://purl.uniprot.org/annotation/VAR_073397|||http://purl.uniprot.org/annotation/VAR_073398|||http://purl.uniprot.org/annotation/VAR_073399|||http://purl.uniprot.org/annotation/VAR_073400|||http://purl.uniprot.org/annotation/VAR_073401|||http://purl.uniprot.org/annotation/VAR_073402|||http://purl.uniprot.org/annotation/VAR_073403|||http://purl.uniprot.org/annotation/VAR_073404|||http://purl.uniprot.org/annotation/VAR_073405|||http://purl.uniprot.org/annotation/VAR_073406|||http://purl.uniprot.org/annotation/VAR_073407|||http://purl.uniprot.org/annotation/VAR_073408|||http://purl.uniprot.org/annotation/VAR_087351|||http://purl.uniprot.org/annotation/VAR_087352|||http://purl.uniprot.org/annotation/VAR_087353|||http://purl.uniprot.org/annotation/VAR_087354|||http://purl.uniprot.org/annotation/VAR_087355|||http://purl.uniprot.org/annotation/VAR_087356|||http://purl.uniprot.org/annotation/VAR_087357|||http://purl.uniprot.org/annotation/VAR_087358|||http://purl.uniprot.org/annotation/VAR_087359|||http://purl.uniprot.org/annotation/VAR_087360|||http://purl.uniprot.org/annotation/VAR_087361|||http://purl.uniprot.org/annotation/VAR_087362|||http://purl.uniprot.org/annotation/VAR_087363|||http://purl.uniprot.org/annotation/VAR_087364|||http://purl.uniprot.org/annotation/VSP_001106|||http://purl.uniprot.org/annotation/VSP_044725|||http://purl.uniprot.org/annotation/VSP_044726|||http://purl.uniprot.org/annotation/VSP_057397
http://togogenome.org/gene/9606:AFF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51826|||http://purl.uniprot.org/uniprot/Q8NAP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AF4/FMR2 family member 3|||Basic and acidic residues|||Disordered|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In KINS.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215916|||http://purl.uniprot.org/annotation/VAR_030805|||http://purl.uniprot.org/annotation/VAR_030806|||http://purl.uniprot.org/annotation/VAR_080758|||http://purl.uniprot.org/annotation/VAR_085675|||http://purl.uniprot.org/annotation/VAR_085676|||http://purl.uniprot.org/annotation/VAR_085677|||http://purl.uniprot.org/annotation/VAR_085678|||http://purl.uniprot.org/annotation/VAR_085679|||http://purl.uniprot.org/annotation/VAR_085680|||http://purl.uniprot.org/annotation/VSP_041120
http://togogenome.org/gene/9606:OR2C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N628                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150466|||http://purl.uniprot.org/annotation/VAR_025540|||http://purl.uniprot.org/annotation/VAR_025541|||http://purl.uniprot.org/annotation/VAR_046378|||http://purl.uniprot.org/annotation/VAR_062016
http://togogenome.org/gene/9606:PPP1R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41236                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Phosphothreonine; by GSK3|||Polar residues|||Protein phosphatase inhibitor 2|||Removed|||Required for binding PPP1CC|||Required for binding PPP1CC catalytic center, displacing metal ions and inhibition of PPP1CC catalytic activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071481
http://togogenome.org/gene/9606:MSRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ68                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate|||Impaired subcellular location.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitochondrial peptide methionine sulfoxide reductase|||Mitochondrion|||N-myristoyl glycine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Redox-active; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138626|||http://purl.uniprot.org/annotation/VSP_041405|||http://purl.uniprot.org/annotation/VSP_041406|||http://purl.uniprot.org/annotation/VSP_041407|||http://purl.uniprot.org/annotation/VSP_042132
http://togogenome.org/gene/9606:ICMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60725                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Protein-S-isoprenylcysteine O-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209894
http://togogenome.org/gene/9606:PIGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQA9|||http://purl.uniprot.org/uniprot/O95427                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GPI ethanolamine phosphate transferase 1|||GPI ethanolamine phosphate transferase 1 C-terminal|||Helical|||In MCAHS1.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246198|||http://purl.uniprot.org/annotation/VAR_053573|||http://purl.uniprot.org/annotation/VAR_053574|||http://purl.uniprot.org/annotation/VAR_053575|||http://purl.uniprot.org/annotation/VAR_053576|||http://purl.uniprot.org/annotation/VAR_053577|||http://purl.uniprot.org/annotation/VAR_053578|||http://purl.uniprot.org/annotation/VAR_066402
http://togogenome.org/gene/9606:LOC101059915                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GWI6                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:WDR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61964                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone H3 binding.|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with histone H3|||Loss of interaction with RBBP5 and reduced ability to stimulate KMT2A methyltransferase activity in association with RBBP5 and ASH2L.|||N-acetylalanine|||N6-acetyllysine|||Polar residues|||Reduced interaction with RBBP5 and reduced ability to stimulate KMT2A methyltransferase activity in association with RBBP5 and ASH2L.|||Removed|||Significant decrease in interaction with KMT2A.|||Strongly reduced affinity for histone H3.|||Strongly reduced affinity for histone H3. No effect on interaction with KMT2A.|||Strongly reduced affinity for histone H3. Significant decrease in interaction with KMT2A.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051350|||http://purl.uniprot.org/annotation/VAR_081531
http://togogenome.org/gene/9606:BACH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD60; impairs protein stability; the mutant is unsoluble and forms multiple aggregates.|||In IMD60; unknown pathological significance; severely decreased localization in the nucleus; the mutant aggregates in the cytoplasm.|||Interchain; redox-active|||Leads to nuclear accumulation.|||Leucine-zipper|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Polar residues|||Transcription regulator protein BACH2|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076456|||http://purl.uniprot.org/annotation/VAR_033535|||http://purl.uniprot.org/annotation/VAR_082216|||http://purl.uniprot.org/annotation/VAR_082217
http://togogenome.org/gene/9606:SNCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G4Y816|||http://purl.uniprot.org/uniprot/Q16143                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3; approximate|||4|||4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)|||Acidic residues|||Beta-synuclein|||Disordered|||Phosphoserine; by BARK1, CK2 and GRK5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184035
http://togogenome.org/gene/9606:KCNJ5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5J6E2W8|||http://purl.uniprot.org/uniprot/P48544                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in aldosterone-producing adrenal adenoma samples; somatic mutation.|||Found in aldosterone-producing adrenal adenoma samples; somatic mutation; results in loss of channel selectivity and membrane depolarization.|||Found in patients with hypertension with ACTH-dependent aldosterone hypersecretion; unknown pathological significance; no effect on channel function.|||G protein-activated inward rectifier potassium channel 4|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In HALD3; also found in aldosterone-producing adrenal adenoma samples; results in loss of channel selectivity and membrane depolarization; increases expression of CYP11B2 and its transcriptional regulators NR4A2 and ATF2; increases aldosterone and hybrid steroids 18-oxocortisol and 18-hydroxycortisol synthesis; increases STAR expression and phosphorylation.|||In HALD3; detected as germline mutation in a kindred with severe primary aldosteronism and adrenocortical hyperplasia; also found as somatic mutation in aldosterone-producing adrenal adenoma samples; results in loss of channel selectivity and membrane depolarization.|||In HALD3; loss of channel selectivity.|||In HALD3; results in a profound alteration of channel function with loss of channel selectivity and membrane depolarization.|||In HALD3; results in alteration of channel function with reduced channel selectivity and membrane depolarization; increases expression of CYP11B2 and its transcriptional regulator NR4A2.|||In LQT13.|||Inward rectifier potassium channel C-terminal|||Phosphoserine|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Probable disease-associated variant found in patients with hypertension with ACTH-dependent aldosterone hypersecretion; loss of channel selectivity.|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154934|||http://purl.uniprot.org/annotation/VAR_063107|||http://purl.uniprot.org/annotation/VAR_063766|||http://purl.uniprot.org/annotation/VAR_065929|||http://purl.uniprot.org/annotation/VAR_065930|||http://purl.uniprot.org/annotation/VAR_065931|||http://purl.uniprot.org/annotation/VAR_065932|||http://purl.uniprot.org/annotation/VAR_065933|||http://purl.uniprot.org/annotation/VAR_067090|||http://purl.uniprot.org/annotation/VAR_069182|||http://purl.uniprot.org/annotation/VAR_077577|||http://purl.uniprot.org/annotation/VAR_077578|||http://purl.uniprot.org/annotation/VAR_077579|||http://purl.uniprot.org/annotation/VAR_077580
http://togogenome.org/gene/9606:KIFC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5U4|||http://purl.uniprot.org/uniprot/B7Z808|||http://purl.uniprot.org/uniprot/B7Z896|||http://purl.uniprot.org/uniprot/F5H3M2|||http://purl.uniprot.org/uniprot/H3BMZ5|||http://purl.uniprot.org/uniprot/Q9BVG8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kinesin motor|||Kinesin-like protein KIFC3|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125431|||http://purl.uniprot.org/annotation/VAR_028114|||http://purl.uniprot.org/annotation/VSP_021018|||http://purl.uniprot.org/annotation/VSP_022361|||http://purl.uniprot.org/annotation/VSP_022362|||http://purl.uniprot.org/annotation/VSP_043724|||http://purl.uniprot.org/annotation/VSP_057224
http://togogenome.org/gene/9606:DEFA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01523                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Mutagenesis Site|||Peptide|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Defensin alpha 5|||Disrupts homodimer-formation. Reduced interaction with B.antracis lef/lethal factor and reduced killing of S.aureus. Reduced enhancement of S.flexneri infection.|||Does not disrupt homodimer-formation. Reduced enhancement of S.flexneri infection. Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-71. Reduced induction of IL-8 secretion; when associated with A-71.|||Does not impair antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with K-75. Reduced induction of IL-8 secretion; when associated with K-75.|||Does not impair antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with K-94. Reduced induction of IL-8 secretion; when associated with K-90.|||Enhanced antibacterial activity against both E.coli and S.aureus.|||Enhanced antibacterial activity against both E.coli and S.aureus. Disrupts homodimerization. Enhanced membrane binding and membrane disintegration abilities, as well further increased antibacterial activity; when associated with R-69.|||Enhanced antibacterial activity against both E.coli and S.aureus. Enhanced membrane binding and membrane disintegration abilities, as well as further increased antibacterial activity; when associated with R-83.|||HD5(23-94)|||HD5(29-94)|||HD5(56-94)|||HD5(63-94)|||Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-75. Reduced induction of IL-8 secretion; when associated with A-75.|||Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-94. Reduced induction of IL-8 secretion; when associated with A-94.|||Impairs antimicrobial activity against S. aureus; when associated with K-71. Reduced induction of IL-8 secretion; when associated with K-71.|||Impairs antimicrobial activity against S. aureus; when associated with K-90. Reduced induction of IL-8 secretion; when associated with K-90.|||Impairs antimicrobial activity against S.aureus.|||Increased interaction with B.antracis lef/lethal factor.|||Prohibits tetramer formation; when associated with S-67.|||Prohibits tetramer formation; when associated with S-72.|||Prohibits tetramer formation; when associated with S-92.|||Prohibits tetramer formation; when associated with S-93.|||Reduced interaction with B.antracis lef/lethal factor and decreased bactericidal activity against E.coli and S.aureus. Reduced enhancement of S.flexneri infection.|||Reduced interaction with B.antracis lef/lethal factor. Reduced enhancement of S.flexneri infection.|||Reduced killing of S.aureus and E.coli. Impairs antimicrobial activity against E.coli, E.aerogenes, S.aureus and B.cereus; when associated with A-90. Reduced induction of IL-8 secretion; when associated with A-90.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006787|||http://purl.uniprot.org/annotation/PRO_0000417387|||http://purl.uniprot.org/annotation/PRO_0000417388|||http://purl.uniprot.org/annotation/PRO_0000417389|||http://purl.uniprot.org/annotation/PRO_0000417390|||http://purl.uniprot.org/annotation/VAR_059245
http://togogenome.org/gene/9606:ANP32A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5U2|||http://purl.uniprot.org/uniprot/P39687                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acidic leucine-rich nuclear phosphoprotein 32 family member A|||Acidic residues|||Complete loss of phosphorylation; when associated with A-158.|||Complete loss of phosphorylation; when associated with A-204.|||Disordered|||Interaction with E4F1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Loss of interaction with influenza virus APB2.|||Necessary for tumor-suppressive function|||No loss of phosphorylation.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||U2A'/phosphoprotein 32 family A C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137592
http://togogenome.org/gene/9606:SIGLEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZZ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of sialic acid recognition capacity.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 11|||Ig-like C2-type 12|||Ig-like C2-type 13|||Ig-like C2-type 14|||Ig-like C2-type 15|||Ig-like C2-type 16|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sialoadhesin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014968|||http://purl.uniprot.org/annotation/VAR_014136|||http://purl.uniprot.org/annotation/VAR_014137|||http://purl.uniprot.org/annotation/VAR_014138|||http://purl.uniprot.org/annotation/VAR_021926|||http://purl.uniprot.org/annotation/VAR_021927|||http://purl.uniprot.org/annotation/VAR_024502|||http://purl.uniprot.org/annotation/VAR_049943|||http://purl.uniprot.org/annotation/VAR_049944|||http://purl.uniprot.org/annotation/VAR_049945|||http://purl.uniprot.org/annotation/VSP_002571|||http://purl.uniprot.org/annotation/VSP_002572
http://togogenome.org/gene/9606:STARD3NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95772                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FFAT|||Helical|||In isoform 2.|||Loss of interaction with MOSPD2.|||MENTAL|||N-acetylmethionine|||Phosphoserine|||STARD3 N-terminal-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021666|||http://purl.uniprot.org/annotation/VSP_018819
http://togogenome.org/gene/9606:PTH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A98                                                                                  ^@                                                                                  Helix|||Molecule Processing|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide                                                                                  ^@                                                                                  Helix|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Tuberoinfundibular peptide of 39 residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045942|||http://purl.uniprot.org/annotation/PRO_0000045943
http://togogenome.org/gene/9606:AGBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH9|||http://purl.uniprot.org/uniprot/Q5U5Z8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic carboxypeptidase 2|||Cytosolic carboxypeptidase N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleophile|||Peptidase M14 carboxypeptidase A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283748|||http://purl.uniprot.org/annotation/VAR_031572|||http://purl.uniprot.org/annotation/VAR_046637|||http://purl.uniprot.org/annotation/VAR_046638|||http://purl.uniprot.org/annotation/VAR_046639|||http://purl.uniprot.org/annotation/VAR_046640|||http://purl.uniprot.org/annotation/VSP_024360|||http://purl.uniprot.org/annotation/VSP_024361
http://togogenome.org/gene/9606:C1QC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAA7|||http://purl.uniprot.org/uniprot/A0A8Q3SIZ0|||http://purl.uniprot.org/uniprot/P02747                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||C1q|||Collagen-like|||Complement C1q subcomponent subunit C|||Disordered|||In C1QD3.|||Interchain|||O-linked (Gal...) hydroxylysine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003524|||http://purl.uniprot.org/annotation/PRO_5014214276|||http://purl.uniprot.org/annotation/VAR_008542
http://togogenome.org/gene/9606:ZNF543                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08ER8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 543                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286809|||http://purl.uniprot.org/annotation/VAR_032171|||http://purl.uniprot.org/annotation/VAR_032172|||http://purl.uniprot.org/annotation/VAR_032173|||http://purl.uniprot.org/annotation/VAR_032174|||http://purl.uniprot.org/annotation/VAR_032175|||http://purl.uniprot.org/annotation/VAR_032176
http://togogenome.org/gene/9606:OR2A25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVV5|||http://purl.uniprot.org/uniprot/A4D2G3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293718|||http://purl.uniprot.org/annotation/VAR_054664|||http://purl.uniprot.org/annotation/VAR_054665
http://togogenome.org/gene/9606:PRSS57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZMF6|||http://purl.uniprot.org/uniprot/Q6UWY2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Decreases enzyme activity tenfold.|||Decreases enzyme activity tenfold. Decreases enzyme activity twentyfold; when associated with A-215.|||Decreases enzyme activity tenfold. Decreases enzyme activity twentyfold; when associated with G-236.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 57                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295853|||http://purl.uniprot.org/annotation/PRO_5002864138|||http://purl.uniprot.org/annotation/VAR_051839
http://togogenome.org/gene/9606:TOMM40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96008                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrial import receptor subunit TOM40 homolog|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051523|||http://purl.uniprot.org/annotation/VSP_008589|||http://purl.uniprot.org/annotation/VSP_008590
http://togogenome.org/gene/9606:ZZEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43149                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DOC|||Disordered|||EF-hand|||In isoform 2.|||In isoform 3.|||Loss of histone H3 binding.|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||ZZ-type 1|||ZZ-type 2|||Zinc finger ZZ-type and EF-hand domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289000|||http://purl.uniprot.org/annotation/VAR_032551|||http://purl.uniprot.org/annotation/VAR_032552|||http://purl.uniprot.org/annotation/VAR_032553|||http://purl.uniprot.org/annotation/VAR_032554|||http://purl.uniprot.org/annotation/VAR_032555|||http://purl.uniprot.org/annotation/VAR_032556|||http://purl.uniprot.org/annotation/VAR_032557|||http://purl.uniprot.org/annotation/VAR_032558|||http://purl.uniprot.org/annotation/VAR_032559|||http://purl.uniprot.org/annotation/VAR_032560|||http://purl.uniprot.org/annotation/VSP_025870|||http://purl.uniprot.org/annotation/VSP_025871|||http://purl.uniprot.org/annotation/VSP_036989|||http://purl.uniprot.org/annotation/VSP_042268|||http://purl.uniprot.org/annotation/VSP_042269|||http://purl.uniprot.org/annotation/VSP_042270
http://togogenome.org/gene/9606:RILP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NA2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments.|||Abolishes interaction with RAB7A and localization to late endosomal/lysosomal compartments.|||Disordered|||In isoform 2.|||Necessary for interaction with RAB7A and RAB34, lysosomal distribution and morphology|||Phosphoserine|||Phosphothreonine|||RH1|||RH2|||Rab-interacting lysosomal protein|||Reduces dimerization, interaction with RAB7A and localization to late endosomal/lysosomal compartments.|||Strongly reduces dimerization and localization to late endosomal/lysosomal compartments.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097339|||http://purl.uniprot.org/annotation/VAR_034417|||http://purl.uniprot.org/annotation/VAR_051321|||http://purl.uniprot.org/annotation/VSP_016043|||http://purl.uniprot.org/annotation/VSP_016044
http://togogenome.org/gene/9606:CES5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT32|||http://purl.uniprot.org/uniprot/V9HWK3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acyl-ester intermediate|||Carboxylesterase 5A|||Carboxylesterase type B|||Carboxylic ester hydrolase|||Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308591|||http://purl.uniprot.org/annotation/PRO_5005149329|||http://purl.uniprot.org/annotation/VAR_036836|||http://purl.uniprot.org/annotation/VAR_036837|||http://purl.uniprot.org/annotation/VAR_036838|||http://purl.uniprot.org/annotation/VAR_036839|||http://purl.uniprot.org/annotation/VAR_036840|||http://purl.uniprot.org/annotation/VSP_029005|||http://purl.uniprot.org/annotation/VSP_029006|||http://purl.uniprot.org/annotation/VSP_043296
http://togogenome.org/gene/9606:MTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4K7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Localized in the mitochondria|||Mitochondrial ribosome-associated GTPase 2|||Not localized in the mitochondria|||OBG-type G|||Obg                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205429|||http://purl.uniprot.org/annotation/VAR_033983|||http://purl.uniprot.org/annotation/VAR_049299|||http://purl.uniprot.org/annotation/VAR_049300|||http://purl.uniprot.org/annotation/VSP_056672
http://togogenome.org/gene/9606:DBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMT0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein DBX1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302843
http://togogenome.org/gene/9606:VCPKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H867                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Loss of methyltransferase activity.|||N-acetylalanine|||Phosphoserine|||Protein N-lysine methyltransferase METTL21D|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089937|||http://purl.uniprot.org/annotation/VAR_059621|||http://purl.uniprot.org/annotation/VSP_008814|||http://purl.uniprot.org/annotation/VSP_008815|||http://purl.uniprot.org/annotation/VSP_008816|||http://purl.uniprot.org/annotation/VSP_026586|||http://purl.uniprot.org/annotation/VSP_026587|||http://purl.uniprot.org/annotation/VSP_043258
http://togogenome.org/gene/9606:PLEKHN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q494U1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with C1QBP|||Loss of myristoylation, reduced protein stability, morphological alterations in mitochondria but no effect on its mitochondrial localization. Loss of cell membrane localization leading to localization to intracellular organelles.|||Loss of phosphorylation and interaction with C1QBP; when associated with F-302.|||Loss of phosphorylation and interaction with C1QBP; when associated with F-456.|||N-myristoyl glycine|||PH 1|||PH 2|||Phosphoserine|||Phosphotyrosine|||Pleckstrin homology domain-containing family N member 1|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309363|||http://purl.uniprot.org/annotation/VAR_036946|||http://purl.uniprot.org/annotation/VSP_059838|||http://purl.uniprot.org/annotation/VSP_059839|||http://purl.uniprot.org/annotation/VSP_059840
http://togogenome.org/gene/9606:MBIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS73                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with MAP3K12|||Leucine-zipper 1|||Leucine-zipper 2|||MAP3K12-binding inhibitory protein 1|||N6-acetyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096269|||http://purl.uniprot.org/annotation/VAR_018449|||http://purl.uniprot.org/annotation/VAR_034093|||http://purl.uniprot.org/annotation/VSP_010265|||http://purl.uniprot.org/annotation/VSP_010266|||http://purl.uniprot.org/annotation/VSP_040134
http://togogenome.org/gene/9606:NTF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20783                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurotrophin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019659|||http://purl.uniprot.org/annotation/PRO_0000019660|||http://purl.uniprot.org/annotation/VAR_012084|||http://purl.uniprot.org/annotation/VSP_043353
http://togogenome.org/gene/9606:VOPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J827|||http://purl.uniprot.org/uniprot/C9JVH1|||http://purl.uniprot.org/uniprot/Q96AW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect binding to WWOX.|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Pro residues|||Reduces binding to WWOX.|||WW domain binding protein VOPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325917|||http://purl.uniprot.org/annotation/PRO_5011977146|||http://purl.uniprot.org/annotation/VSP_043867|||http://purl.uniprot.org/annotation/VSP_043868|||http://purl.uniprot.org/annotation/VSP_055723
http://togogenome.org/gene/9606:SMC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXX5|||http://purl.uniprot.org/uniprot/E9PD53|||http://purl.uniprot.org/uniprot/Q58F29|||http://purl.uniprot.org/uniprot/Q9NTJ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Pro residues|||RecF/RecN/SMC N-terminal|||SMC hinge|||Structural maintenance of chromosomes protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119006|||http://purl.uniprot.org/annotation/VAR_052439|||http://purl.uniprot.org/annotation/VAR_052440|||http://purl.uniprot.org/annotation/VAR_059843|||http://purl.uniprot.org/annotation/VSP_007245
http://togogenome.org/gene/9606:NOL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SY16                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes kinase activity and rRNA processing.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Polynucleotide 5'-hydroxyl-kinase NOL9|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096939|||http://purl.uniprot.org/annotation/VAR_054777|||http://purl.uniprot.org/annotation/VAR_054778|||http://purl.uniprot.org/annotation/VAR_054779|||http://purl.uniprot.org/annotation/VAR_056955
http://togogenome.org/gene/9606:ADGRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZF6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor G4|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070335|||http://purl.uniprot.org/annotation/VAR_055929|||http://purl.uniprot.org/annotation/VAR_059329|||http://purl.uniprot.org/annotation/VAR_059330|||http://purl.uniprot.org/annotation/VAR_059331|||http://purl.uniprot.org/annotation/VAR_059332|||http://purl.uniprot.org/annotation/VSP_038170|||http://purl.uniprot.org/annotation/VSP_038171|||http://purl.uniprot.org/annotation/VSP_038172|||http://purl.uniprot.org/annotation/VSP_038173|||http://purl.uniprot.org/annotation/VSP_038174|||http://purl.uniprot.org/annotation/VSP_038175|||http://purl.uniprot.org/annotation/VSP_038176
http://togogenome.org/gene/9606:C7orf57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H7J8|||http://purl.uniprot.org/uniprot/Q86XB5|||http://purl.uniprot.org/uniprot/Q8NEG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Uncharacterized protein C7orf57                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310991|||http://purl.uniprot.org/annotation/VAR_056813|||http://purl.uniprot.org/annotation/VSP_046991|||http://purl.uniprot.org/annotation/VSP_046992|||http://purl.uniprot.org/annotation/VSP_046993
http://togogenome.org/gene/9606:STXBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61764                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with Lennox-Gastaut syndrome; unknown pathological significance.|||In DEE4.|||In DEE4; may alter protein structure.|||In DEE4; reduced thermostability; decreased binding to STX1A.|||In isoform 2.|||No effect on subcellular location.|||Phosphoserine|||Probable disease-associated variant found in a patient with epileptic encephalopathy.|||Syntaxin-binding protein 1|||Variant of uncertain significance; expressed at low levels compared with wild-type; no effect on subcellular location.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206277|||http://purl.uniprot.org/annotation/VAR_046205|||http://purl.uniprot.org/annotation/VAR_046206|||http://purl.uniprot.org/annotation/VAR_046207|||http://purl.uniprot.org/annotation/VAR_046208|||http://purl.uniprot.org/annotation/VAR_071814|||http://purl.uniprot.org/annotation/VAR_071815|||http://purl.uniprot.org/annotation/VAR_071816|||http://purl.uniprot.org/annotation/VAR_073148|||http://purl.uniprot.org/annotation/VAR_073149|||http://purl.uniprot.org/annotation/VAR_073150|||http://purl.uniprot.org/annotation/VAR_073151|||http://purl.uniprot.org/annotation/VAR_073152|||http://purl.uniprot.org/annotation/VAR_073153|||http://purl.uniprot.org/annotation/VAR_073154|||http://purl.uniprot.org/annotation/VAR_078218|||http://purl.uniprot.org/annotation/VAR_078631|||http://purl.uniprot.org/annotation/VAR_078632|||http://purl.uniprot.org/annotation/VAR_078633|||http://purl.uniprot.org/annotation/VAR_078634|||http://purl.uniprot.org/annotation/VAR_078635|||http://purl.uniprot.org/annotation/VAR_078636|||http://purl.uniprot.org/annotation/VAR_078757|||http://purl.uniprot.org/annotation/VAR_078758|||http://purl.uniprot.org/annotation/VAR_078759|||http://purl.uniprot.org/annotation/VSP_006713
http://togogenome.org/gene/9606:SYF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95926                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Pre-mRNA-splicing factor SYF2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250376|||http://purl.uniprot.org/annotation/VAR_062162|||http://purl.uniprot.org/annotation/VSP_054802
http://togogenome.org/gene/9606:RAB11FIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WKZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the interaction with RAB11A and RAB4A, homooligomerization and subcellular location.|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A.|||FIP-RBD|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recycling|||Phosphoserine|||Polar residues|||Pro residues|||Rab11 family-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097304|||http://purl.uniprot.org/annotation/VAR_022447|||http://purl.uniprot.org/annotation/VAR_056977|||http://purl.uniprot.org/annotation/VAR_059714|||http://purl.uniprot.org/annotation/VAR_069365|||http://purl.uniprot.org/annotation/VSP_013726|||http://purl.uniprot.org/annotation/VSP_013727|||http://purl.uniprot.org/annotation/VSP_013728|||http://purl.uniprot.org/annotation/VSP_013729|||http://purl.uniprot.org/annotation/VSP_013730|||http://purl.uniprot.org/annotation/VSP_013731|||http://purl.uniprot.org/annotation/VSP_013732
http://togogenome.org/gene/9606:ARL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0F7                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 6|||In BBS3.|||In BBS3; abrogates the GTP-binding ability without affecting GDP-binding/dissociating properties; increased proteasomal degradation.|||In BBS3; abrogates the GTP-binding ability; increased proteasomal degradation.|||In BBS3; locked in a GDP-bound state that differs from its wild-type counterpart which is mainly GTP-bound; increased proteasomal degradation.|||In RP55.|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207472|||http://purl.uniprot.org/annotation/VAR_027643|||http://purl.uniprot.org/annotation/VAR_027644|||http://purl.uniprot.org/annotation/VAR_027645|||http://purl.uniprot.org/annotation/VAR_027646|||http://purl.uniprot.org/annotation/VAR_064184|||http://purl.uniprot.org/annotation/VAR_071405|||http://purl.uniprot.org/annotation/VSP_040511
http://togogenome.org/gene/9606:KCTD16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8W2|||http://purl.uniprot.org/uniprot/Q68DU8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD16|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248593
http://togogenome.org/gene/9606:F2RL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by thrombin or trypsin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||No effect on receptor activation.|||No proteolytic cleavage (by thrombin or trypsin).|||Polar residues|||Proteinase-activated receptor 4|||Removed for receptor activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012762|||http://purl.uniprot.org/annotation/PRO_0000012763|||http://purl.uniprot.org/annotation/VAR_012852|||http://purl.uniprot.org/annotation/VAR_012853|||http://purl.uniprot.org/annotation/VAR_028300|||http://purl.uniprot.org/annotation/VAR_028301
http://togogenome.org/gene/9606:ZNF599                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NL3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||De novo variant found in a patient with intellectual disability.|||In isoform 2.|||KRAB|||Zinc finger protein 599                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234592|||http://purl.uniprot.org/annotation/VAR_065087|||http://purl.uniprot.org/annotation/VSP_018385|||http://purl.uniprot.org/annotation/VSP_018386
http://togogenome.org/gene/9606:CARMIL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIB7|||http://purl.uniprot.org/uniprot/A0A8Q3SII9|||http://purl.uniprot.org/uniprot/Q6F5E8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CARMIL C-terminal|||CARMIL pleckstrin homology|||Capping protein, Arp2/3 and myosin-I linker protein 2|||Disordered|||In IMD58.|||In IMD58; decreased protein expression in patient's cells.|||In IMD58; decreased protein expression in patient's leukocytes; no effect on homodimerization.|||In IMD58; no detectable protein expression in patient's leukocytes; no effect on homodimerization.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1021.|||Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1023.|||Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing.|||Necessary for localization at the cell membrane|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Tropomodulin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325817|||http://purl.uniprot.org/annotation/VAR_081149|||http://purl.uniprot.org/annotation/VAR_081150|||http://purl.uniprot.org/annotation/VAR_081151|||http://purl.uniprot.org/annotation/VAR_081152|||http://purl.uniprot.org/annotation/VAR_081153|||http://purl.uniprot.org/annotation/VSP_047857|||http://purl.uniprot.org/annotation/VSP_047858
http://togogenome.org/gene/9606:MAP3K6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95382                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In an ovarian endometrioid cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Mitogen-activated protein kinase kinase kinase 6|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086251|||http://purl.uniprot.org/annotation/VAR_032832|||http://purl.uniprot.org/annotation/VAR_032833|||http://purl.uniprot.org/annotation/VAR_032834|||http://purl.uniprot.org/annotation/VAR_035629|||http://purl.uniprot.org/annotation/VAR_046050|||http://purl.uniprot.org/annotation/VAR_046051|||http://purl.uniprot.org/annotation/VAR_046052|||http://purl.uniprot.org/annotation/VAR_046053|||http://purl.uniprot.org/annotation/VAR_046054|||http://purl.uniprot.org/annotation/VAR_046055|||http://purl.uniprot.org/annotation/VAR_046056|||http://purl.uniprot.org/annotation/VAR_046057|||http://purl.uniprot.org/annotation/VSP_026201|||http://purl.uniprot.org/annotation/VSP_026202|||http://purl.uniprot.org/annotation/VSP_026203|||http://purl.uniprot.org/annotation/VSP_026204
http://togogenome.org/gene/9606:LSMEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8F7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Leucine-rich single-pass membrane protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309272|||http://purl.uniprot.org/annotation/VSP_029104
http://togogenome.org/gene/9606:NHLRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6VVB1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase NHLRC1|||In EPM2.|||In EPM2; does not significantly alters the subcellular location as compared to the wild-type.|||In EPM2; loss of interaction with EPM2A.|||In EPM2; loss of interaction with EPM2A; increased levels of PPP1R3C and glycogen.|||In EPM2; severely reduced interaction with EPM2A; increased levels of PPP1R3C and glycogen.|||In EPM2; significantly alters the distribution of the protein; a great majority of cells expressing the mutant form formed perinuclear inclusion when compared with the wild-type form.|||In EPM2; the mutant protein targeted exclusively nucleus as compared to predominantly cytoplasmic and partially nuclear localization of the wild-type protein.|||Loss of interaction with EP2MA.|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055980|||http://purl.uniprot.org/annotation/VAR_019482|||http://purl.uniprot.org/annotation/VAR_019483|||http://purl.uniprot.org/annotation/VAR_019484|||http://purl.uniprot.org/annotation/VAR_019485|||http://purl.uniprot.org/annotation/VAR_019486|||http://purl.uniprot.org/annotation/VAR_019487|||http://purl.uniprot.org/annotation/VAR_019488|||http://purl.uniprot.org/annotation/VAR_046387|||http://purl.uniprot.org/annotation/VAR_046388|||http://purl.uniprot.org/annotation/VAR_046389|||http://purl.uniprot.org/annotation/VAR_046390|||http://purl.uniprot.org/annotation/VAR_046391|||http://purl.uniprot.org/annotation/VAR_046392|||http://purl.uniprot.org/annotation/VAR_046393|||http://purl.uniprot.org/annotation/VAR_046394|||http://purl.uniprot.org/annotation/VAR_046395|||http://purl.uniprot.org/annotation/VAR_046396|||http://purl.uniprot.org/annotation/VAR_046397|||http://purl.uniprot.org/annotation/VAR_046398|||http://purl.uniprot.org/annotation/VAR_046399|||http://purl.uniprot.org/annotation/VAR_046400|||http://purl.uniprot.org/annotation/VAR_046401|||http://purl.uniprot.org/annotation/VAR_070793|||http://purl.uniprot.org/annotation/VAR_070794
http://togogenome.org/gene/9606:GEMIN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWZ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Gem-associated protein 8|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087155|||http://purl.uniprot.org/annotation/VAR_051011
http://togogenome.org/gene/9606:C9orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ63                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes binding to SNRNP200.|||Basic and acidic residues|||Decreases binding to SNRNP200.|||Disordered|||Interaction with SNRNP200|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Splicing factor C9orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227523|||http://purl.uniprot.org/annotation/VAR_050828
http://togogenome.org/gene/9606:RAB11FIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXF6|||http://purl.uniprot.org/uniprot/Q9UFM0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  C2|||Disordered|||FIP-RBD|||Phosphoserine|||Polar residues|||Pro residues|||Rab11 family-interacting protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097307
http://togogenome.org/gene/9606:ARL4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56559                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 4C|||Cytoplasmic localization.|||Cytoplasmic localization. Increases GDP-form.|||Does not interact with alpha tubulin.|||Does not interact with alpha tubulin. Activates transferrin transport from early endosome to recycling endosome.|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207462|||http://purl.uniprot.org/annotation/VSP_055120
http://togogenome.org/gene/9606:RXRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JKR7|||http://purl.uniprot.org/uniprot/A0A0S2Z570|||http://purl.uniprot.org/uniprot/B7Z7J5|||http://purl.uniprot.org/uniprot/P28702|||http://purl.uniprot.org/uniprot/Q5STP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hinge|||In isoform 2.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Omega-N-methylarginine|||Polar residues|||Pro residues|||Retinoic acid receptor RXR-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053572|||http://purl.uniprot.org/annotation/VSP_045587
http://togogenome.org/gene/9606:ACRV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26436                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||2-1|||2-2|||2-3|||2-4|||3 X 5 AA repeats of S-E-H-[GA]-S|||3-1|||3-2|||3-3|||3-4|||3-5|||3-6|||3-7|||3-8|||3-9|||4 X 4 AA repeats of S-G-E-H|||9 X 5 AA repeats of [SV]-G-E-Q-[PSA]|||Acrosomal protein SP-10|||Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 7.|||In isoform 4, isoform 5, isoform 8 and isoform 9.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020760|||http://purl.uniprot.org/annotation/VAR_050680|||http://purl.uniprot.org/annotation/VSP_004120|||http://purl.uniprot.org/annotation/VSP_004121|||http://purl.uniprot.org/annotation/VSP_004122|||http://purl.uniprot.org/annotation/VSP_004123|||http://purl.uniprot.org/annotation/VSP_004124|||http://purl.uniprot.org/annotation/VSP_004125|||http://purl.uniprot.org/annotation/VSP_004126|||http://purl.uniprot.org/annotation/VSP_004127|||http://purl.uniprot.org/annotation/VSP_004128
http://togogenome.org/gene/9606:OR7G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW43|||http://purl.uniprot.org/uniprot/Q8NG99                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150651|||http://purl.uniprot.org/annotation/VAR_024113
http://togogenome.org/gene/9606:ZBTB20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCW4|||http://purl.uniprot.org/uniprot/Q9HC78                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In PRIMS; does not affect subcellular location; strongly reduced DNA binding; reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele.|||In PRIMS; strongly reduced DNA binding; reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele.|||In PRIMS; strongly reduced DNA binding; strongly reduced ability to repress transcription; dominant-negative effect of the mutant on the wild-type allele.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger and BTB domain-containing protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047733|||http://purl.uniprot.org/annotation/VAR_072583|||http://purl.uniprot.org/annotation/VAR_072584|||http://purl.uniprot.org/annotation/VAR_072585|||http://purl.uniprot.org/annotation/VAR_072586|||http://purl.uniprot.org/annotation/VSP_032503
http://togogenome.org/gene/9606:GHDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2G8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Disordered|||GH3 domain-containing protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||N5-methylglutamine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021593|||http://purl.uniprot.org/annotation/VSP_010835|||http://purl.uniprot.org/annotation/VSP_010836|||http://purl.uniprot.org/annotation/VSP_044831
http://togogenome.org/gene/9606:COPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35606                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coatomer subunit beta'|||Disordered|||In MCPH19; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050912|||http://purl.uniprot.org/annotation/VAR_080601|||http://purl.uniprot.org/annotation/VSP_056165
http://togogenome.org/gene/9606:ATF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0Z421|||http://purl.uniprot.org/uniprot/A8K383|||http://purl.uniprot.org/uniprot/P18850                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Almost complete loss of RNF186-mediated ubiquitination.|||BZIP|||Basic motif|||Cleavage; by MBTPS1|||Cyclic AMP-dependent transcription factor ATF-6 alpha|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Signal-anchor for type II membrane protein|||In ACHM7.|||In ACHM7; reduced ATF6-mediated unfolded protein response.|||Interaction with THBS4|||Leucine-zipper|||Loss of glycosylation at Asn-472 and increase of Golgi translocation rate.|||Loss of glycosylation at Asn-584 and increase of Golgi translocation rate. Higher increase in Golgi translocation rate; when associated with Ile-645.|||Loss of glycosylation at Asn-643 and increase of Golgi translocation rate. Higher increase in Golgi translocation rate; when associated with Ile-586.|||Loss of proteolytic cleavage; when associated with F-391.|||Loss of proteolytic cleavage; when associated with L-394.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Processed cyclic AMP-dependent transcription factor ATF-6 alpha|||Reduces proteolytic cleavage.|||Transcription activation|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076589|||http://purl.uniprot.org/annotation/PRO_0000296200|||http://purl.uniprot.org/annotation/VAR_022455|||http://purl.uniprot.org/annotation/VAR_022456|||http://purl.uniprot.org/annotation/VAR_022457|||http://purl.uniprot.org/annotation/VAR_022458|||http://purl.uniprot.org/annotation/VAR_075681|||http://purl.uniprot.org/annotation/VAR_075682
http://togogenome.org/gene/9606:DDX39B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCM3|||http://purl.uniprot.org/uniprot/Q13838                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||DEAD-box RNA helicase Q|||DECD box|||Decreased ATPase activity and loss of helicase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Increased ATPase activity and loss of helicase activity.|||Loss of ATPase and helicase activity.|||N-acetylalanine|||N6-acetyllysine; alternate|||No effect on ATPase activity.|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed|||Spliceosome RNA helicase DDX39B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055071|||http://purl.uniprot.org/annotation/VSP_026347
http://togogenome.org/gene/9606:SLC35E4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA|||Helical|||In isoform 2.|||Solute carrier family 35 member E4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298927|||http://purl.uniprot.org/annotation/VSP_027480|||http://purl.uniprot.org/annotation/VSP_027481
http://togogenome.org/gene/9606:NCAPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IBW4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Condensin-2 complex subunit H2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326241|||http://purl.uniprot.org/annotation/VSP_032636|||http://purl.uniprot.org/annotation/VSP_032637|||http://purl.uniprot.org/annotation/VSP_032638|||http://purl.uniprot.org/annotation/VSP_032639
http://togogenome.org/gene/9606:HLTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGA6|||http://purl.uniprot.org/uniprot/A8K5B6|||http://purl.uniprot.org/uniprot/Q05BZ6|||http://purl.uniprot.org/uniprot/Q14527                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DEGH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIRAN|||Helicase ATP-binding|||Helicase C-terminal|||Helicase-like transcription factor|||In isoform 2.|||Interaction with SP1 and SP3|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by JAK2|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030722|||http://purl.uniprot.org/annotation/VAR_029265|||http://purl.uniprot.org/annotation/VAR_052121|||http://purl.uniprot.org/annotation/VAR_052122|||http://purl.uniprot.org/annotation/VSP_018873
http://togogenome.org/gene/9606:DIPK1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P6D2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Divergent protein kinase domain 1C|||Helical|||In isoform 2.|||Lumenal|||May mediate ER retention                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286707|||http://purl.uniprot.org/annotation/VSP_025146
http://togogenome.org/gene/9606:EPB41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7Y3|||http://purl.uniprot.org/uniprot/P11171|||http://purl.uniprot.org/uniprot/Q1WWM3|||http://purl.uniprot.org/uniprot/Q29RX4|||http://purl.uniprot.org/uniprot/Q59F12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||Hydrophilic|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 7.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60.|||Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphotyrosine|||Phosphotyrosine; by EGFR|||Polar residues|||Protein 4.1|||Spectrin--actin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219390|||http://purl.uniprot.org/annotation/VAR_009122|||http://purl.uniprot.org/annotation/VSP_000468|||http://purl.uniprot.org/annotation/VSP_000469|||http://purl.uniprot.org/annotation/VSP_000470|||http://purl.uniprot.org/annotation/VSP_000471|||http://purl.uniprot.org/annotation/VSP_000472|||http://purl.uniprot.org/annotation/VSP_000473|||http://purl.uniprot.org/annotation/VSP_012872|||http://purl.uniprot.org/annotation/VSP_012873
http://togogenome.org/gene/9606:EPB41L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRA8|||http://purl.uniprot.org/uniprot/A8K968|||http://purl.uniprot.org/uniprot/Q9Y2J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Band 4.1-like protein 3|||Band 4.1-like protein 3, N-terminally processed|||Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||Hydrophilic|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N-acetylthreonine; in Band 4.1-like protein 3, N-terminally processed|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed; alternate|||Spectrin--actin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219399|||http://purl.uniprot.org/annotation/PRO_0000423194|||http://purl.uniprot.org/annotation/VAR_048353|||http://purl.uniprot.org/annotation/VAR_048354|||http://purl.uniprot.org/annotation/VAR_048355|||http://purl.uniprot.org/annotation/VSP_000482|||http://purl.uniprot.org/annotation/VSP_000483|||http://purl.uniprot.org/annotation/VSP_000484|||http://purl.uniprot.org/annotation/VSP_000485|||http://purl.uniprot.org/annotation/VSP_000486|||http://purl.uniprot.org/annotation/VSP_054819|||http://purl.uniprot.org/annotation/VSP_054820
http://togogenome.org/gene/9606:PHYKPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUZ5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5-phosphohydroxy-L-lysine phospho-lyase|||In PHLU.|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287667|||http://purl.uniprot.org/annotation/VAR_048233|||http://purl.uniprot.org/annotation/VAR_069543|||http://purl.uniprot.org/annotation/VAR_069544|||http://purl.uniprot.org/annotation/VSP_025584|||http://purl.uniprot.org/annotation/VSP_025585
http://togogenome.org/gene/9606:PXDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92626                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Cleavage; by FURIN|||Disordered|||Does not affect protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315 and S-1316.|||Does not affect protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315 and S-1319.|||Does not affect the proteolytic processing.|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In ASGD7.|||In isoform 2.|||Interchain (with C-1315); in homotrimer|||Interchain (with C-736); in homotrimer|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||LRRNT|||Loss of bromide oxidation. Loss of tubulogenesis. Does not induce angiogenesis.|||Loss of peroxidase activity. Does not affect oligomerization. Loss of peroxidase activity; when associated with E-823. Does not support the formation of collagen IV cross-links; when associated with W-823. Reduces the proteolytic processing; when associated with W-823. Loss of collagen IV cross-link; when associated with W-823.|||Loss of peroxidase activity. Does not affect oligomerization. Loss of peroxidase activity; when associated with E-826. Does not support the formation of collagen IV cross-links; when associated with E-826. Reduces the proteolytic processing; when associated with E-826. Loss of collagen IV cross-link; when associated with E-826.|||Loss of protein homooligomerization. Loss of protein homooligomerization; when associated with S-1315. Does not affect peroxidase activity; when associated with S-1315. Retains the ability to support the collagen IV cross-links; when associated with S-1315. Slightly reduces proteolysis; when associated with S-1315.|||Loss of protein homooligomerization. Loss of protein homooligomerization; when associated with S-1316 and S-1319. Loss of protein homooligomerization; when associated with S-736. Does not affect peroxydase activity; when associated with S-736. Affects cell surface location; when associated with S-736. Slightly reduces proteolysis; when associated with S-736.|||Loss of proteolytic cleavage. Decreases the formation of sulfilimine cross-links in collagen IV. Reduces the proteolytic processing. Affects collagen IV cross-linking.|||N-linked (GlcNAc...) asparagine|||PXDN active fragment|||Peroxidasin homolog|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||Required in homotrimerization|||Transition state stabilizer|||VWFC|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319619|||http://purl.uniprot.org/annotation/PRO_0000455175|||http://purl.uniprot.org/annotation/VAR_039048|||http://purl.uniprot.org/annotation/VAR_050487|||http://purl.uniprot.org/annotation/VAR_071389|||http://purl.uniprot.org/annotation/VSP_031516|||http://purl.uniprot.org/annotation/VSP_031517
http://togogenome.org/gene/9606:MKX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox protein Mohawk|||Homeobox; TALE-type|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268856|||http://purl.uniprot.org/annotation/VAR_033875
http://togogenome.org/gene/9606:TFG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BK6|||http://purl.uniprot.org/uniprot/Q92734                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form TRK-T3|||Disordered|||In HMSNO; does not affect interaction with PDCD6.|||In SPG57; causes mitochondrial fragmentation.|||In SPG57; defective self-assembly into an oligomeric complex; impaired interaction with PDCD6; causes mitochondrial fragmentation.|||In SPG57; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-acetylmethionine|||Omega-N-methylarginine|||PB1|||Phosphoserine|||Polar residues|||Protein TFG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072500|||http://purl.uniprot.org/annotation/VAR_035668|||http://purl.uniprot.org/annotation/VAR_054322|||http://purl.uniprot.org/annotation/VAR_054323|||http://purl.uniprot.org/annotation/VAR_068917|||http://purl.uniprot.org/annotation/VAR_070986|||http://purl.uniprot.org/annotation/VAR_078075|||http://purl.uniprot.org/annotation/VAR_082155|||http://purl.uniprot.org/annotation/VSP_047131|||http://purl.uniprot.org/annotation/VSP_057414|||http://purl.uniprot.org/annotation/VSP_057415
http://togogenome.org/gene/9606:TIMM13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5L4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit Tim13|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193623
http://togogenome.org/gene/9606:CYB5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43169                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||Cytochrome b5 type B|||Disordered|||Helical|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006471|||http://purl.uniprot.org/annotation/PRO_0000006472
http://togogenome.org/gene/9606:OR1M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGA1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150447
http://togogenome.org/gene/9606:BLTP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14667                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Bridge-like lipid transfer protein family member 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Transmembrane domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248587|||http://purl.uniprot.org/annotation/VAR_027352|||http://purl.uniprot.org/annotation/VAR_027353|||http://purl.uniprot.org/annotation/VAR_052706|||http://purl.uniprot.org/annotation/VSP_020317|||http://purl.uniprot.org/annotation/VSP_020318|||http://purl.uniprot.org/annotation/VSP_020319|||http://purl.uniprot.org/annotation/VSP_020320|||http://purl.uniprot.org/annotation/VSP_020321|||http://purl.uniprot.org/annotation/VSP_020322
http://togogenome.org/gene/9606:CCDC136                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JN2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 136|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300639|||http://purl.uniprot.org/annotation/VAR_034880|||http://purl.uniprot.org/annotation/VAR_034881|||http://purl.uniprot.org/annotation/VSP_027840|||http://purl.uniprot.org/annotation/VSP_027841|||http://purl.uniprot.org/annotation/VSP_027842|||http://purl.uniprot.org/annotation/VSP_027843|||http://purl.uniprot.org/annotation/VSP_027844|||http://purl.uniprot.org/annotation/VSP_027845
http://togogenome.org/gene/9606:ZC3HAV1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Polar residues|||Removed|||Zinc finger CCCH-type antiviral protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331459|||http://purl.uniprot.org/annotation/VSP_033210|||http://purl.uniprot.org/annotation/VSP_033211
http://togogenome.org/gene/9606:TRPC4AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEL6                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Interaction with TNFRSF1A|||N-acetylalanine|||Removed|||Short transient receptor potential channel 4-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072641|||http://purl.uniprot.org/annotation/VSP_003982|||http://purl.uniprot.org/annotation/VSP_054231
http://togogenome.org/gene/9606:GPR19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15760|||http://purl.uniprot.org/uniprot/Q6IBH2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069538|||http://purl.uniprot.org/annotation/VAR_024256
http://togogenome.org/gene/9606:SKI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12755                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In SGS.|||Phosphoserine|||Polar residues|||Ski oncogene                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129382|||http://purl.uniprot.org/annotation/VAR_071170|||http://purl.uniprot.org/annotation/VAR_071171|||http://purl.uniprot.org/annotation/VAR_071172|||http://purl.uniprot.org/annotation/VAR_071173|||http://purl.uniprot.org/annotation/VAR_071174|||http://purl.uniprot.org/annotation/VAR_071175|||http://purl.uniprot.org/annotation/VAR_071176|||http://purl.uniprot.org/annotation/VAR_071177|||http://purl.uniprot.org/annotation/VAR_071178|||http://purl.uniprot.org/annotation/VAR_071179|||http://purl.uniprot.org/annotation/VAR_071180|||http://purl.uniprot.org/annotation/VAR_071181|||http://purl.uniprot.org/annotation/VAR_071182|||http://purl.uniprot.org/annotation/VAR_071183|||http://purl.uniprot.org/annotation/VAR_071659|||http://purl.uniprot.org/annotation/VAR_071660
http://togogenome.org/gene/9606:CD52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31358|||http://purl.uniprot.org/uniprot/V9HWN9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  CAMPATH-1 antigen|||GPI-anchor amidated serine|||Helical|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020904|||http://purl.uniprot.org/annotation/PRO_0000020905|||http://purl.uniprot.org/annotation/PRO_5014314734|||http://purl.uniprot.org/annotation/VAR_014838|||http://purl.uniprot.org/annotation/VAR_050775
http://togogenome.org/gene/9606:NHSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P206                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Uncharacterized protein KIAA1522                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311246|||http://purl.uniprot.org/annotation/VAR_037190|||http://purl.uniprot.org/annotation/VAR_037191|||http://purl.uniprot.org/annotation/VAR_037192|||http://purl.uniprot.org/annotation/VAR_037193|||http://purl.uniprot.org/annotation/VAR_037194|||http://purl.uniprot.org/annotation/VAR_037195|||http://purl.uniprot.org/annotation/VSP_040217|||http://purl.uniprot.org/annotation/VSP_041634|||http://purl.uniprot.org/annotation/VSP_043215
http://togogenome.org/gene/9606:CCNY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8E4|||http://purl.uniprot.org/uniprot/Q8ND76                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-Y|||Cyclin-like|||In isoform 2.|||In isoform 3.|||Induces a diffuse cytoplasmic localization.|||N-myristoyl glycine|||No effect on subcellular location.|||Phosphoserine|||Phosphoserine; by CDK14|||Phosphothreonine|||Phosphothreonine; by CDK14|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080514|||http://purl.uniprot.org/annotation/VSP_014833|||http://purl.uniprot.org/annotation/VSP_014834
http://togogenome.org/gene/9606:CLEC19A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GV53                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  C-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5008408650
http://togogenome.org/gene/9606:NCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Y3|||http://purl.uniprot.org/uniprot/P16333                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cytoplasmic protein NCK1|||In isoform 2.|||N-acetylalanine|||No effect on RASA1-binding.|||No effect on RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229.|||Phosphoserine|||Phosphotyrosine|||Removed|||SH2|||SH3|||SH3 1|||SH3 2|||SH3 3|||Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-143 and K-229.|||Small decrease in RASA1-binding. Almost complete loss of RASA1-binding; when associated with K-38 and K-229.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096766|||http://purl.uniprot.org/annotation/VAR_051228|||http://purl.uniprot.org/annotation/VSP_043122
http://togogenome.org/gene/9606:SPTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02549                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||In Cagliari.|||In EL2 and HPP; Saint-Louis.|||In EL2.|||In EL2; Alexandria.|||In EL2; Anastasia.|||In EL2; Barcelona.|||In EL2; Clichy.|||In EL2; Corbeil.|||In EL2; Culoz.|||In EL2; Genova.|||In EL2; Jendouba.|||In EL2; Lograno.|||In EL2; Lyon.|||In EL2; Marseille.|||In EL2; Nigerian.|||In EL2; Ponte de Sor.|||In EL2; Tunis.|||In HPP.|||In isoform 2.|||Phosphoserine|||SH3|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin alpha chain, erythrocytic 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073452|||http://purl.uniprot.org/annotation/VAR_001324|||http://purl.uniprot.org/annotation/VAR_001325|||http://purl.uniprot.org/annotation/VAR_001326|||http://purl.uniprot.org/annotation/VAR_001327|||http://purl.uniprot.org/annotation/VAR_001328|||http://purl.uniprot.org/annotation/VAR_001329|||http://purl.uniprot.org/annotation/VAR_001330|||http://purl.uniprot.org/annotation/VAR_001331|||http://purl.uniprot.org/annotation/VAR_001332|||http://purl.uniprot.org/annotation/VAR_001333|||http://purl.uniprot.org/annotation/VAR_001334|||http://purl.uniprot.org/annotation/VAR_001335|||http://purl.uniprot.org/annotation/VAR_001336|||http://purl.uniprot.org/annotation/VAR_001337|||http://purl.uniprot.org/annotation/VAR_001338|||http://purl.uniprot.org/annotation/VAR_001339|||http://purl.uniprot.org/annotation/VAR_001340|||http://purl.uniprot.org/annotation/VAR_001341|||http://purl.uniprot.org/annotation/VAR_001342|||http://purl.uniprot.org/annotation/VAR_001343|||http://purl.uniprot.org/annotation/VAR_001344|||http://purl.uniprot.org/annotation/VAR_001345|||http://purl.uniprot.org/annotation/VAR_001346|||http://purl.uniprot.org/annotation/VAR_001347|||http://purl.uniprot.org/annotation/VAR_001348|||http://purl.uniprot.org/annotation/VAR_001349|||http://purl.uniprot.org/annotation/VAR_001350|||http://purl.uniprot.org/annotation/VAR_001351|||http://purl.uniprot.org/annotation/VAR_038506|||http://purl.uniprot.org/annotation/VAR_038507|||http://purl.uniprot.org/annotation/VAR_038508|||http://purl.uniprot.org/annotation/VAR_038509|||http://purl.uniprot.org/annotation/VAR_038510|||http://purl.uniprot.org/annotation/VAR_038511|||http://purl.uniprot.org/annotation/VAR_038512|||http://purl.uniprot.org/annotation/VAR_059199|||http://purl.uniprot.org/annotation/VAR_059200|||http://purl.uniprot.org/annotation/VAR_059201|||http://purl.uniprot.org/annotation/VSP_037662
http://togogenome.org/gene/9606:IFI27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40305                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Complete loss of TRIM21-mediated ubiquitination.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased pro-apoptotic activity; when associated with D-56.|||Increased pro-apoptotic activity; when associated with D-96.|||Interferon alpha-inducible protein 27, mitochondrial|||Mediates interaction with SKP2 and hepatitis C virus non-structural protein NS5A|||Mitochondrion|||Required for hepatitis C virus non-structural protein NS5A degradation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147372|||http://purl.uniprot.org/annotation/VAR_028066|||http://purl.uniprot.org/annotation/VSP_059907|||http://purl.uniprot.org/annotation/VSP_059908|||http://purl.uniprot.org/annotation/VSP_059909
http://togogenome.org/gene/9606:KLHL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2G3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 14|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119117|||http://purl.uniprot.org/annotation/VSP_041342|||http://purl.uniprot.org/annotation/VSP_041343
http://togogenome.org/gene/9606:MBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J7H0|||http://purl.uniprot.org/uniprot/A8K654|||http://purl.uniprot.org/uniprot/B4DI41|||http://purl.uniprot.org/uniprot/B4DUR3|||http://purl.uniprot.org/uniprot/Q9UIS9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to methylated DNA.|||Abolishes interaction with ATF7IP and subsequent transcription repression activity.|||Basic and acidic residues|||Basic residues|||CXXC-type|||CXXC-type 1|||CXXC-type 2|||CXXC-type 3|||Disordered|||Disrupts tertiary structure and abolishes DNA binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 10.|||In isoform 11.|||In isoform 2 and isoform 12.|||In isoform 2 and isoform 8.|||In isoform 2, isoform 4, isoform 6, isoform 8 and isoform 11.|||In isoform 4 and isoform 7.|||In isoform 5 and isoform 10.|||In isoform 6.|||In isoform 9.|||MBD|||Methyl-CpG-binding domain protein 1|||No loss of binding to methylated DNA.|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues|||Reduces binding to methylated DNA.|||Strongly reduces binding to methylated DNA.|||Transcriptional repression domain (TRD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096258|||http://purl.uniprot.org/annotation/VAR_019513|||http://purl.uniprot.org/annotation/VSP_011064|||http://purl.uniprot.org/annotation/VSP_011065|||http://purl.uniprot.org/annotation/VSP_011066|||http://purl.uniprot.org/annotation/VSP_011068|||http://purl.uniprot.org/annotation/VSP_011069|||http://purl.uniprot.org/annotation/VSP_011070|||http://purl.uniprot.org/annotation/VSP_011071|||http://purl.uniprot.org/annotation/VSP_042812|||http://purl.uniprot.org/annotation/VSP_054736|||http://purl.uniprot.org/annotation/VSP_054737|||http://purl.uniprot.org/annotation/VSP_054738|||http://purl.uniprot.org/annotation/VSP_054739
http://togogenome.org/gene/9606:TAOK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1Q8|||http://purl.uniprot.org/uniprot/Q9H2K8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||Inhibits activation of the p38/MAPK14 stress-activated MAPK cascade in response to DNA damage.|||Loss of serine/threonine-protein kinase activity.|||N6-acetyllysine|||No autophosphorylation and no kinase activity; when associated with A-181.|||No autophosphorylation and no kinase activity; when associated with F-183.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TAO3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086737|||http://purl.uniprot.org/annotation/VAR_023691|||http://purl.uniprot.org/annotation/VAR_041205|||http://purl.uniprot.org/annotation/VAR_041206|||http://purl.uniprot.org/annotation/VAR_041207
http://togogenome.org/gene/9606:RBCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYM8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-282.|||Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-285.|||Disordered|||IBR-type|||In PGBM1.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with IRF3|||Interaction with RNF31|||Interaction with TAB2|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||RING-type 1|||RING-type 2; atypical|||RanBP-type and C3HC4-type zinc finger-containing protein 1|||RanBP2-type|||TRIAD supradomain|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056295|||http://purl.uniprot.org/annotation/VAR_071385|||http://purl.uniprot.org/annotation/VAR_071386|||http://purl.uniprot.org/annotation/VSP_005766|||http://purl.uniprot.org/annotation/VSP_005767|||http://purl.uniprot.org/annotation/VSP_005768
http://togogenome.org/gene/9606:AIMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNK3|||http://purl.uniprot.org/uniprot/Q12904                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminoacyl tRNA synthase complex-interacting multifunctional protein 1|||Basic and acidic residues|||Disordered|||Endothelial monocyte-activating polypeptide 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Interaction with HSP90B1|||N-acetylalanine|||N6-succinyllysine|||Phosphoserine|||Removed|||Required for endothelial cell death|||Required for endothelial cell migration|||Required for fibroblast proliferation|||TRNA-binding|||tRNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019242|||http://purl.uniprot.org/annotation/PRO_0000223394|||http://purl.uniprot.org/annotation/VAR_025212|||http://purl.uniprot.org/annotation/VAR_029156|||http://purl.uniprot.org/annotation/VAR_050124|||http://purl.uniprot.org/annotation/VSP_042197
http://togogenome.org/gene/9606:FOXP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Cleavage|||Cleavage; by PCSK1 or PCSK2|||Decrease in nuclear export; when associated with A-242 and A-246.|||Decrease in nuclear export; when associated with A-242 and A-248.|||Decrease in nuclear export; when associated with A-246 and A-248.|||Decrease in nuclear export; when associated with A-69, A-71 and A-74.|||Decrease in nuclear export; when associated with A-69, A-71 and A-76.|||Decrease in nuclear export; when associated with A-69, A-74 and A-76.|||Decrease in nuclear export; when associated with A-71, A-74 and A-76.|||Decrease in phosphorylation, significant decrease in transcriptional repressor activity and reduced interaction with PP1CA, PP1CB and PP1CG. Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-422.|||Disordered|||Disrupts dimerization but does not affect DNA-binding; when associated with Q-348. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and P-372.|||Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and T-370.|||Essential for transcriptional repressor activity and for interaction with KAT5 and HDAC7|||Fork-head|||Forkhead box protein P3|||Forkhead box protein P3 41 kDa form|||Forkhead box protein P3, C-terminally processed|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In IPEX.|||In IPEX; mild phenotype; no loss of protein expression.|||In IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373.|||In IPEX; no effect on dimerization.|||In IPEX; no loss of protein expression.|||In IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347.|||In IPEX; significantly reduces dimerization.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with IKZF4|||Interaction with RUNX1|||Interaction with ZFP90|||LXXLL motif|||Leucine-zipper|||Loss of interaction with RORA.|||Loss of nuclear localization.|||N6-acetyllysine|||N6-acetyllysine; alternate|||No loss of DNA-binding. Disrupts dimerization but does not affect DNA-binding; when associated with T-370. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with T-370 and P-372.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK2|||Polar residues|||Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-418.|||Slight increase in transcriptional repressor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091886|||http://purl.uniprot.org/annotation/PRO_0000432430|||http://purl.uniprot.org/annotation/PRO_0000432431|||http://purl.uniprot.org/annotation/PRO_0000432432|||http://purl.uniprot.org/annotation/VAR_011330|||http://purl.uniprot.org/annotation/VAR_011331|||http://purl.uniprot.org/annotation/VAR_011332|||http://purl.uniprot.org/annotation/VAR_011333|||http://purl.uniprot.org/annotation/VAR_023569|||http://purl.uniprot.org/annotation/VAR_078971|||http://purl.uniprot.org/annotation/VAR_078972|||http://purl.uniprot.org/annotation/VAR_078973|||http://purl.uniprot.org/annotation/VAR_078974|||http://purl.uniprot.org/annotation/VAR_078975|||http://purl.uniprot.org/annotation/VAR_078976|||http://purl.uniprot.org/annotation/VSP_015796|||http://purl.uniprot.org/annotation/VSP_036418|||http://purl.uniprot.org/annotation/VSP_047859
http://togogenome.org/gene/9606:DYRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92630                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes protein serine/threonine kinase activity.|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 2|||Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination.|||Impaired nuclear translocation.|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by MAP3K10|||Phosphothreonine; by ATM|||Phosphothreonine; by MAP3K10|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085936|||http://purl.uniprot.org/annotation/VAR_040458|||http://purl.uniprot.org/annotation/VAR_040459|||http://purl.uniprot.org/annotation/VAR_040460|||http://purl.uniprot.org/annotation/VAR_040461|||http://purl.uniprot.org/annotation/VAR_040462|||http://purl.uniprot.org/annotation/VAR_040463|||http://purl.uniprot.org/annotation/VSP_026115
http://togogenome.org/gene/9606:ZNF239                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16600                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Zinc finger protein 239                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047480|||http://purl.uniprot.org/annotation/VAR_024205|||http://purl.uniprot.org/annotation/VAR_024206|||http://purl.uniprot.org/annotation/VAR_025536
http://togogenome.org/gene/9606:GPR61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G4XH66|||http://purl.uniprot.org/uniprot/Q9BZJ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect subcellular location.|||Extracellular|||G-protein coupled receptor 61|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069578
http://togogenome.org/gene/9606:PDRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKN4|||http://purl.uniprot.org/uniprot/Q9NUG6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  p53 and DNA damage-regulated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058277
http://togogenome.org/gene/9606:CD1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRL5|||http://purl.uniprot.org/uniprot/P15812                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||Ig-like|||In allele CD1E*02, allele CD1E*05 and CD1E*06.|||In allele CD1E*03.|||In allele CD1E*04; impairs localization to late endosomal compartments and lipid antigen presentation.|||In allele CD1E*05.|||In isoform 13.|||In isoform 2, isoform 4, isoform 6, isoform 7, isoform 9 and isoform 12.|||In isoform 3 and isoform 10.|||In isoform 4, isoform 7, isoform 11 and isoform 12.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12.|||N-linked (GlcNAc...) asparagine|||Removed in sCD1e|||T-cell surface glycoprotein CD1e, membrane-associated|||T-cell surface glycoprotein CD1e, soluble                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014582|||http://purl.uniprot.org/annotation/PRO_0000379780|||http://purl.uniprot.org/annotation/PRO_0000379781|||http://purl.uniprot.org/annotation/PRO_5002645950|||http://purl.uniprot.org/annotation/VAR_010191|||http://purl.uniprot.org/annotation/VAR_010192|||http://purl.uniprot.org/annotation/VAR_010193|||http://purl.uniprot.org/annotation/VAR_056035|||http://purl.uniprot.org/annotation/VAR_058324|||http://purl.uniprot.org/annotation/VAR_058325|||http://purl.uniprot.org/annotation/VSP_037708|||http://purl.uniprot.org/annotation/VSP_037709|||http://purl.uniprot.org/annotation/VSP_037710|||http://purl.uniprot.org/annotation/VSP_037711|||http://purl.uniprot.org/annotation/VSP_037712|||http://purl.uniprot.org/annotation/VSP_037713|||http://purl.uniprot.org/annotation/VSP_046961
http://togogenome.org/gene/9606:OR9Q2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW85|||http://purl.uniprot.org/uniprot/Q8NGE9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9Q2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150684|||http://purl.uniprot.org/annotation/VAR_062061
http://togogenome.org/gene/9606:AVPR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37288|||http://purl.uniprot.org/uniprot/X5D2B0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine|||Vasopressin V1a receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070197|||http://purl.uniprot.org/annotation/VAR_022065
http://togogenome.org/gene/9606:KRTAP2-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7H8|||http://purl.uniprot.org/uniprot/Q9BYR9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  10 X 5 AA repeats of C-C-[CDPQRWG]-[APRS]-[CIPSTVD]|||10 X 5 AA repeats of C-C-[CDPQRW]-[ADPRS]-[CIPSTV]|||Keratin-associated protein 2-3|||Keratin-associated protein 2-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185162|||http://purl.uniprot.org/annotation/PRO_0000331452
http://togogenome.org/gene/9606:FCER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K3W4U1|||http://purl.uniprot.org/uniprot/P06734                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Low affinity immunoglobulin epsilon Fc receptor membrane-bound form|||Low affinity immunoglobulin epsilon Fc receptor soluble form|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017391|||http://purl.uniprot.org/annotation/PRO_0000017392|||http://purl.uniprot.org/annotation/VAR_035387|||http://purl.uniprot.org/annotation/VAR_035388|||http://purl.uniprot.org/annotation/VAR_069800
http://togogenome.org/gene/9606:COG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z652|||http://purl.uniprot.org/uniprot/P83436                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Non-terminal Residue|||Sequence Variant                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213518|||http://purl.uniprot.org/annotation/VAR_048762
http://togogenome.org/gene/9606:NMNAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AN62|||http://purl.uniprot.org/uniprot/Q9HAN9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytidyltransferase-like|||Disordered|||In LCA9.|||In LCA9; does not affect nuclear localization.|||In LCA9; does not affect nuclear localization; results in significantly reduced enzymatic activity.|||In LCA9; results in significantly reduced enzymatic activity.|||In LCA9; results in significantly reduced enzymatic activity; the mutant localizes to the cytoplasm.|||Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135012|||http://purl.uniprot.org/annotation/VAR_068856|||http://purl.uniprot.org/annotation/VAR_068857|||http://purl.uniprot.org/annotation/VAR_068858|||http://purl.uniprot.org/annotation/VAR_068859|||http://purl.uniprot.org/annotation/VAR_068860|||http://purl.uniprot.org/annotation/VAR_068861|||http://purl.uniprot.org/annotation/VAR_068862|||http://purl.uniprot.org/annotation/VAR_068863|||http://purl.uniprot.org/annotation/VAR_068864|||http://purl.uniprot.org/annotation/VAR_068865|||http://purl.uniprot.org/annotation/VAR_068866|||http://purl.uniprot.org/annotation/VAR_068867|||http://purl.uniprot.org/annotation/VAR_068868|||http://purl.uniprot.org/annotation/VAR_068869|||http://purl.uniprot.org/annotation/VAR_068870|||http://purl.uniprot.org/annotation/VAR_068871|||http://purl.uniprot.org/annotation/VAR_068872|||http://purl.uniprot.org/annotation/VAR_068873|||http://purl.uniprot.org/annotation/VAR_068874|||http://purl.uniprot.org/annotation/VAR_068875|||http://purl.uniprot.org/annotation/VAR_068876|||http://purl.uniprot.org/annotation/VAR_068877|||http://purl.uniprot.org/annotation/VAR_068878|||http://purl.uniprot.org/annotation/VAR_068879|||http://purl.uniprot.org/annotation/VAR_068880|||http://purl.uniprot.org/annotation/VAR_068881|||http://purl.uniprot.org/annotation/VAR_068882|||http://purl.uniprot.org/annotation/VAR_068883
http://togogenome.org/gene/9606:ZNF768                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BS42|||http://purl.uniprot.org/uniprot/Q9H5H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Increases protein stability.|||No effect on protein stability.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Zinc finger protein 768                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304408|||http://purl.uniprot.org/annotation/VAR_035024|||http://purl.uniprot.org/annotation/VAR_052900
http://togogenome.org/gene/9606:IDH3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15384|||http://purl.uniprot.org/uniprot/P51553                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.|||Complete loss of the activation of the heterotetramer and the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||In isoform 2.|||Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial|||Isopropylmalate dehydrogenase-like|||Mitochondrion|||No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||No effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.|||No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.|||No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.|||Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by ADP.|||Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014449|||http://purl.uniprot.org/annotation/VSP_046771
http://togogenome.org/gene/9606:DYNLL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FJ2                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Dynein light chain 2, cytoplasmic|||Interaction with myosin V motor complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195132
http://togogenome.org/gene/9606:PMFBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBY8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SPGF31.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Polyamine-modulated factor 1-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304619|||http://purl.uniprot.org/annotation/VAR_035042|||http://purl.uniprot.org/annotation/VAR_035043|||http://purl.uniprot.org/annotation/VAR_035044|||http://purl.uniprot.org/annotation/VAR_035045|||http://purl.uniprot.org/annotation/VAR_056974|||http://purl.uniprot.org/annotation/VAR_069056|||http://purl.uniprot.org/annotation/VAR_081140|||http://purl.uniprot.org/annotation/VAR_081141|||http://purl.uniprot.org/annotation/VAR_081142|||http://purl.uniprot.org/annotation/VAR_081143|||http://purl.uniprot.org/annotation/VAR_082886|||http://purl.uniprot.org/annotation/VSP_060104|||http://purl.uniprot.org/annotation/VSP_060105|||http://purl.uniprot.org/annotation/VSP_060106|||http://purl.uniprot.org/annotation/VSP_060107|||http://purl.uniprot.org/annotation/VSP_060108
http://togogenome.org/gene/9606:ZNF92                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IZS8|||http://purl.uniprot.org/uniprot/Q03936|||http://purl.uniprot.org/uniprot/V9HVY7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15; degenerate|||C2H2-type 16; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 92                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047401|||http://purl.uniprot.org/annotation/VAR_024843|||http://purl.uniprot.org/annotation/VAR_052766|||http://purl.uniprot.org/annotation/VAR_052767|||http://purl.uniprot.org/annotation/VSP_016964|||http://purl.uniprot.org/annotation/VSP_016965
http://togogenome.org/gene/9606:CEP78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MST6|||http://purl.uniprot.org/uniprot/Q5JTW2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 78 kDa|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291952|||http://purl.uniprot.org/annotation/VSP_026321|||http://purl.uniprot.org/annotation/VSP_026322|||http://purl.uniprot.org/annotation/VSP_026323
http://togogenome.org/gene/9606:DMBT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJ76|||http://purl.uniprot.org/uniprot/Q9UGM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||Deleted in malignant brain tumors 1 protein|||Disordered|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In a glioma cell line.|||In a glioma sample; glioblastoma multiforme; somatic mutation.|||In a glioma sample; pilocytic astrocytoma.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Requires 2 nucleotide substitutions.|||SRCR|||SRCR 1|||SRCR 10|||SRCR 11|||SRCR 12|||SRCR 13|||SRCR 14|||SRCR 2|||SRCR 3|||SRCR 4|||SRCR 5|||SRCR 6|||SRCR 7|||SRCR 8|||SRCR 9|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045387|||http://purl.uniprot.org/annotation/PRO_5022722009|||http://purl.uniprot.org/annotation/VAR_024788|||http://purl.uniprot.org/annotation/VAR_024789|||http://purl.uniprot.org/annotation/VAR_024790|||http://purl.uniprot.org/annotation/VAR_024791|||http://purl.uniprot.org/annotation/VAR_024792|||http://purl.uniprot.org/annotation/VAR_024793|||http://purl.uniprot.org/annotation/VAR_024794|||http://purl.uniprot.org/annotation/VAR_024795|||http://purl.uniprot.org/annotation/VAR_024796|||http://purl.uniprot.org/annotation/VAR_024797|||http://purl.uniprot.org/annotation/VAR_024798|||http://purl.uniprot.org/annotation/VAR_024799|||http://purl.uniprot.org/annotation/VAR_024800|||http://purl.uniprot.org/annotation/VAR_024801|||http://purl.uniprot.org/annotation/VAR_024802|||http://purl.uniprot.org/annotation/VAR_024803|||http://purl.uniprot.org/annotation/VAR_024804|||http://purl.uniprot.org/annotation/VAR_024805|||http://purl.uniprot.org/annotation/VAR_024806|||http://purl.uniprot.org/annotation/VAR_024807|||http://purl.uniprot.org/annotation/VAR_044417|||http://purl.uniprot.org/annotation/VAR_044418|||http://purl.uniprot.org/annotation/VAR_052994|||http://purl.uniprot.org/annotation/VAR_052995|||http://purl.uniprot.org/annotation/VAR_057981|||http://purl.uniprot.org/annotation/VAR_057982|||http://purl.uniprot.org/annotation/VAR_057983|||http://purl.uniprot.org/annotation/VAR_057984|||http://purl.uniprot.org/annotation/VAR_057985|||http://purl.uniprot.org/annotation/VAR_057986|||http://purl.uniprot.org/annotation/VAR_080764|||http://purl.uniprot.org/annotation/VSP_016846|||http://purl.uniprot.org/annotation/VSP_016847|||http://purl.uniprot.org/annotation/VSP_016848|||http://purl.uniprot.org/annotation/VSP_016849|||http://purl.uniprot.org/annotation/VSP_016850|||http://purl.uniprot.org/annotation/VSP_034653|||http://purl.uniprot.org/annotation/VSP_034654|||http://purl.uniprot.org/annotation/VSP_034655|||http://purl.uniprot.org/annotation/VSP_034656|||http://purl.uniprot.org/annotation/VSP_053979|||http://purl.uniprot.org/annotation/VSP_053980|||http://purl.uniprot.org/annotation/VSP_053981
http://togogenome.org/gene/9606:SZRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z422                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||SUZ|||SUZ domain-containing protein 1|||SUZ-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303068|||http://purl.uniprot.org/annotation/VSP_027995|||http://purl.uniprot.org/annotation/VSP_027996|||http://purl.uniprot.org/annotation/VSP_027997|||http://purl.uniprot.org/annotation/VSP_055690
http://togogenome.org/gene/9606:UBTFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CB47                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HMG box 1|||HMG box 2|||Polar residues|||Upstream-binding factor 1-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000386640
http://togogenome.org/gene/9606:CTAGE8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG41|||http://purl.uniprot.org/uniprot/Q8IX94                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||cTAGE family member 4|||cTAGE family member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189540|||http://purl.uniprot.org/annotation/PRO_0000395454
http://togogenome.org/gene/9606:CUL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z600|||http://purl.uniprot.org/uniprot/Q13618                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cullin family profile|||Cullin-3|||Disordered|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||In NEDAUS.|||In NEDAUS; decreases interaction with KEAP1.|||In PHA2E.|||In isoform 2.|||In isoform 3.|||Interaction with KLHL18|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119793|||http://purl.uniprot.org/annotation/VAR_017194|||http://purl.uniprot.org/annotation/VAR_017195|||http://purl.uniprot.org/annotation/VAR_048839|||http://purl.uniprot.org/annotation/VAR_067532|||http://purl.uniprot.org/annotation/VAR_067533|||http://purl.uniprot.org/annotation/VAR_078688|||http://purl.uniprot.org/annotation/VAR_085407|||http://purl.uniprot.org/annotation/VAR_085408|||http://purl.uniprot.org/annotation/VSP_008824|||http://purl.uniprot.org/annotation/VSP_008825
http://togogenome.org/gene/9606:TWSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZX9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Twisted gastrulation protein homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278808|||http://purl.uniprot.org/annotation/VSP_042538|||http://purl.uniprot.org/annotation/VSP_042539
http://togogenome.org/gene/9606:CDKN2AIPNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HQ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to XRN2.|||CDKN2AIP N-terminal-like protein|||In isoform 2.|||N-acetylmethionine|||XRN2-binding (XTBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325926|||http://purl.uniprot.org/annotation/VSP_032486
http://togogenome.org/gene/9606:TNFSF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5JXL4|||http://purl.uniprot.org/uniprot/Q9UNG2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Tumor necrosis factor ligand superfamily member 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185506
http://togogenome.org/gene/9606:NLRP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WX94                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In HYDM1.|||In HYDM1; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||NACHT|||NACHT, LRR and PYD domains-containing protein 7|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080895|||http://purl.uniprot.org/annotation/VAR_026710|||http://purl.uniprot.org/annotation/VAR_026711|||http://purl.uniprot.org/annotation/VAR_026712|||http://purl.uniprot.org/annotation/VAR_026713|||http://purl.uniprot.org/annotation/VAR_026714|||http://purl.uniprot.org/annotation/VAR_059035|||http://purl.uniprot.org/annotation/VAR_059036|||http://purl.uniprot.org/annotation/VAR_059037|||http://purl.uniprot.org/annotation/VAR_059038|||http://purl.uniprot.org/annotation/VAR_059039|||http://purl.uniprot.org/annotation/VAR_059040|||http://purl.uniprot.org/annotation/VAR_060103|||http://purl.uniprot.org/annotation/VAR_085072|||http://purl.uniprot.org/annotation/VAR_085073|||http://purl.uniprot.org/annotation/VAR_085074|||http://purl.uniprot.org/annotation/VAR_085075|||http://purl.uniprot.org/annotation/VAR_085076|||http://purl.uniprot.org/annotation/VAR_085077|||http://purl.uniprot.org/annotation/VAR_085078|||http://purl.uniprot.org/annotation/VSP_016906|||http://purl.uniprot.org/annotation/VSP_016907
http://togogenome.org/gene/9606:ERO1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alternate|||ERO1-like protein beta|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on catalytic activity when DTT is used as an electron donor; when associated with A-90. Loss of catalytic activity when P4HB is used as an electron donor; when associated with A-90.|||No effect on catalytic activity when DTT is used as an electron donor; when associated with A-95. Loss of catalytic activity when P4HB is used as an electron donor; when associated with A-95.|||Redox-active|||Redox-active; alternate|||Slightly decrease in activity. Significant increased activity; when associated with A-130.|||Small increase in activity. Significant increased activity; when associated with A-130.|||Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein, but loss of homodimerization with A-396 mutated protein. Loss of catalytic activity when DTT or P4HB are used as an electron donor; when associated with A-393.|||Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein. Loss of catalytic activity when DTT or P4HB are used as an electron donor; when associated with A-396.|||Strong decrease in P4HB-binding. Efficient homodimerization with both wild-type and A-390 mutated protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008418|||http://purl.uniprot.org/annotation/VAR_019492|||http://purl.uniprot.org/annotation/VAR_028012|||http://purl.uniprot.org/annotation/VSP_056988
http://togogenome.org/gene/9606:IQCF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTL0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  IQ 1|||IQ 2|||IQ domain-containing protein F5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345956
http://togogenome.org/gene/9606:SHOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In NSLH1; creates a N-myristoylation site, resulting in myristoylation of the protein and aberrant targeting to the plasma membrane.|||In NSLH1; significantly decreases ERK1/2 activity; does not affect cytoplasm and nucleus localization; does not affect SHOC2-MRAS-RAF1 complex assembly; impairs interaction with phosphatase 1c.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat protein SHOC-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097737|||http://purl.uniprot.org/annotation/VAR_060199|||http://purl.uniprot.org/annotation/VAR_074030|||http://purl.uniprot.org/annotation/VSP_038188
http://togogenome.org/gene/9606:HSPA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5I0|||http://purl.uniprot.org/uniprot/B3KTT5|||http://purl.uniprot.org/uniprot/P0DMV8|||http://purl.uniprot.org/uniprot/P0DMV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of in vitro methylation by METTL21A.|||Disordered|||Heat shock 70 kDa protein 1A|||Heat shock 70 kDa protein 1B|||In isoform 2.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by METTL21A; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||No loss of acetylation and ATPase activity. Exhibits normal protein refolding activity during the early phase but exhibits defects in ubiquitin-mediated protein degradation during the later phase.|||Nucleotide-binding domain (NBD)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Reduces affinity for ADP.|||Removed|||Significant loss of acetylation and ATPase activity. Decreased binding to HOPX and HSP90 and increased binding to STUB1 and NAA10. Impaired capacity for protein refolding during the early phase after stress but shows normal protein degradation activity in the late phase.|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078249|||http://purl.uniprot.org/annotation/PRO_0000433115|||http://purl.uniprot.org/annotation/VAR_029053|||http://purl.uniprot.org/annotation/VAR_029054|||http://purl.uniprot.org/annotation/VAR_032152|||http://purl.uniprot.org/annotation/VAR_032153|||http://purl.uniprot.org/annotation/VSP_044427
http://togogenome.org/gene/9606:SPANXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VSR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Sperm protein associated with the nucleus on the X chromosome N1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285538
http://togogenome.org/gene/9606:ADGRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6QNK2|||http://purl.uniprot.org/uniprot/Q9NSM3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes G-protein coupled receptor activity; does not affect subcellular location.|||Adhesion G-protein coupled receptor D1|||Cytoplasmic|||Decreases cell surface location; abolishes G-protein coupled receptor activity.|||Disordered|||Does not affect membrane trafficking and basal activity.|||Does not affect membrane trafficking. Abolishes receptor activity.|||Does not affect subcellular location.|||Does not affect subcellular location; decreases G-protein coupled receptor activity.|||Does not affect subcellular location; does not change G-protein coupled receptor activity.|||Does not affect subcellular location; increases G-protein coupled receptor activity.|||Does not change G-protein coupled receptor activity.|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No effect on G-protein coupled receptor activity; does not affect subcellular location.|||Pentraxin (PTX)|||Reduces cell membrane location; decreases G-protein coupled receptor activity.|||Stachel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012905|||http://purl.uniprot.org/annotation/VAR_049461|||http://purl.uniprot.org/annotation/VAR_049462|||http://purl.uniprot.org/annotation/VAR_077698|||http://purl.uniprot.org/annotation/VAR_077699|||http://purl.uniprot.org/annotation/VAR_077700|||http://purl.uniprot.org/annotation/VAR_077701|||http://purl.uniprot.org/annotation/VAR_077702|||http://purl.uniprot.org/annotation/VAR_077703|||http://purl.uniprot.org/annotation/VAR_077704|||http://purl.uniprot.org/annotation/VAR_077705|||http://purl.uniprot.org/annotation/VAR_077706|||http://purl.uniprot.org/annotation/VAR_077707|||http://purl.uniprot.org/annotation/VAR_077708|||http://purl.uniprot.org/annotation/VAR_077709|||http://purl.uniprot.org/annotation/VAR_077710|||http://purl.uniprot.org/annotation/VAR_077711|||http://purl.uniprot.org/annotation/VAR_077712|||http://purl.uniprot.org/annotation/VAR_077713|||http://purl.uniprot.org/annotation/VAR_077714|||http://purl.uniprot.org/annotation/VAR_077715|||http://purl.uniprot.org/annotation/VAR_077716|||http://purl.uniprot.org/annotation/VAR_077717|||http://purl.uniprot.org/annotation/VAR_077718|||http://purl.uniprot.org/annotation/VAR_077719|||http://purl.uniprot.org/annotation/VAR_077720|||http://purl.uniprot.org/annotation/VAR_077721|||http://purl.uniprot.org/annotation/VAR_077722|||http://purl.uniprot.org/annotation/VAR_077723|||http://purl.uniprot.org/annotation/VAR_077724|||http://purl.uniprot.org/annotation/VAR_077725|||http://purl.uniprot.org/annotation/VAR_077726|||http://purl.uniprot.org/annotation/VAR_077727|||http://purl.uniprot.org/annotation/VAR_077728|||http://purl.uniprot.org/annotation/VAR_077729|||http://purl.uniprot.org/annotation/VAR_077730|||http://purl.uniprot.org/annotation/VAR_077731|||http://purl.uniprot.org/annotation/VAR_077732|||http://purl.uniprot.org/annotation/VAR_077733|||http://purl.uniprot.org/annotation/VAR_077734|||http://purl.uniprot.org/annotation/VAR_077735|||http://purl.uniprot.org/annotation/VAR_077736|||http://purl.uniprot.org/annotation/VAR_077737|||http://purl.uniprot.org/annotation/VAR_077738|||http://purl.uniprot.org/annotation/VAR_077739|||http://purl.uniprot.org/annotation/VAR_077740|||http://purl.uniprot.org/annotation/VAR_077741|||http://purl.uniprot.org/annotation/VAR_077742|||http://purl.uniprot.org/annotation/VAR_077743|||http://purl.uniprot.org/annotation/VAR_077744|||http://purl.uniprot.org/annotation/VAR_077745|||http://purl.uniprot.org/annotation/VAR_077746|||http://purl.uniprot.org/annotation/VAR_077747|||http://purl.uniprot.org/annotation/VAR_077748|||http://purl.uniprot.org/annotation/VAR_077749|||http://purl.uniprot.org/annotation/VAR_077750|||http://purl.uniprot.org/annotation/VAR_077751|||http://purl.uniprot.org/annotation/VAR_077752|||http://purl.uniprot.org/annotation/VAR_077753|||http://purl.uniprot.org/annotation/VAR_077754|||http://purl.uniprot.org/annotation/VAR_077755|||http://purl.uniprot.org/annotation/VAR_077756|||http://purl.uniprot.org/annotation/VAR_077757|||http://purl.uniprot.org/annotation/VAR_077758|||http://purl.uniprot.org/annotation/VAR_077759|||http://purl.uniprot.org/annotation/VAR_077760|||http://purl.uniprot.org/annotation/VAR_077761|||http://purl.uniprot.org/annotation/VAR_077762|||http://purl.uniprot.org/annotation/VAR_077763|||http://purl.uniprot.org/annotation/VAR_077764|||http://purl.uniprot.org/annotation/VAR_077765|||http://purl.uniprot.org/annotation/VAR_077766|||http://purl.uniprot.org/annotation/VAR_077767|||http://purl.uniprot.org/annotation/VAR_077768|||http://purl.uniprot.org/annotation/VAR_077769|||http://purl.uniprot.org/annotation/VAR_077770|||http://purl.uniprot.org/annotation/VAR_077771|||http://purl.uniprot.org/annotation/VAR_077772|||http://purl.uniprot.org/annotation/VAR_077773|||http://purl.uniprot.org/annotation/VAR_077774|||http://purl.uniprot.org/annotation/VAR_077775|||http://purl.uniprot.org/annotation/VAR_077776|||http://purl.uniprot.org/annotation/VAR_077777|||http://purl.uniprot.org/annotation/VAR_077778|||http://purl.uniprot.org/annotation/VAR_077779|||http://purl.uniprot.org/annotation/VAR_077780|||http://purl.uniprot.org/annotation/VAR_077781|||http://purl.uniprot.org/annotation/VAR_077782|||http://purl.uniprot.org/annotation/VAR_077783|||http://purl.uniprot.org/annotation/VAR_077784|||http://purl.uniprot.org/annotation/VAR_077785|||http://purl.uniprot.org/annotation/VAR_077786|||http://purl.uniprot.org/annotation/VAR_077787|||http://purl.uniprot.org/annotation/VAR_077788|||http://purl.uniprot.org/annotation/VAR_077789|||http://purl.uniprot.org/annotation/VAR_077790|||http://purl.uniprot.org/annotation/VAR_077791|||http://purl.uniprot.org/annotation/VAR_077792|||http://purl.uniprot.org/annotation/VAR_077793|||http://purl.uniprot.org/annotation/VAR_077794|||http://purl.uniprot.org/annotation/VAR_077795|||http://purl.uniprot.org/annotation/VAR_077796|||http://purl.uniprot.org/annotation/VAR_077797|||http://purl.uniprot.org/annotation/VAR_077798|||http://purl.uniprot.org/annotation/VAR_077799|||http://purl.uniprot.org/annotation/VAR_077800|||http://purl.uniprot.org/annotation/VSP_012787|||http://purl.uniprot.org/annotation/VSP_012788|||http://purl.uniprot.org/annotation/VSP_012789|||http://purl.uniprot.org/annotation/VSP_012790|||http://purl.uniprot.org/annotation/VSP_053678
http://togogenome.org/gene/9606:KCNA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16322                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Motif|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Potassium voltage-gated channel subfamily A member 10|||S-palmitoyl cysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308275|||http://purl.uniprot.org/annotation/VAR_036778|||http://purl.uniprot.org/annotation/VAR_036779|||http://purl.uniprot.org/annotation/VAR_036780
http://togogenome.org/gene/9606:RPS6KA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75582                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Decreases kinase activity by 60% in response to PMA and UV-C.|||Disordered|||In isoform 2.|||In isoform 3.|||Inactivates the N-terminal kinase domain.|||Loss of kinase activity, and blocks phosphorylation of S-212; S-376 and S-381 in response to PMA and UV-C.|||Loss of kinase activity, and decreases the phosphorylation of S-360 and T-581.|||Loss of kinase activity.|||Phosphoserine|||Phosphoserine; by MAPK1, MAPK3 and MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine; by MAPK1, MAPK3 and MAPK14|||Polar residues|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Ribosomal protein S6 kinase alpha-5|||Strongly reduces phosphorylation of T-581 in response to PMA and UV-C.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086207|||http://purl.uniprot.org/annotation/VAR_040634|||http://purl.uniprot.org/annotation/VAR_040635|||http://purl.uniprot.org/annotation/VAR_040636|||http://purl.uniprot.org/annotation/VAR_051634|||http://purl.uniprot.org/annotation/VSP_041837|||http://purl.uniprot.org/annotation/VSP_041838|||http://purl.uniprot.org/annotation/VSP_057410
http://togogenome.org/gene/9606:LMBR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0Y9|||http://purl.uniprot.org/uniprot/A0A0S2Z6E3|||http://purl.uniprot.org/uniprot/Q6UX01                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with LGB|||LCN1-binding|||Protein LMBR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053910|||http://purl.uniprot.org/annotation/VSP_016892|||http://purl.uniprot.org/annotation/VSP_016893|||http://purl.uniprot.org/annotation/VSP_016894|||http://purl.uniprot.org/annotation/VSP_016895|||http://purl.uniprot.org/annotation/VSP_016896
http://togogenome.org/gene/9606:FST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19883                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Follistatin|||Follistatin-like 1|||Follistatin-like 2|||Follistatin-like 3|||Found in patients with orofacial clefting; unknown pathological significance.|||In isoform 2.|||Kazal-like 1|||Kazal-like 2|||Kazal-like 3|||N-linked (GlcNAc...) asparagine|||TB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010103|||http://purl.uniprot.org/annotation/VAR_049091|||http://purl.uniprot.org/annotation/VAR_085164|||http://purl.uniprot.org/annotation/VSP_001565
http://togogenome.org/gene/9606:PRSS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQE7                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||N-linked (GlcNAc...) asparagine|||Thymus-specific serine protease                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027320|||http://purl.uniprot.org/annotation/VAR_051826|||http://purl.uniprot.org/annotation/VAR_051827
http://togogenome.org/gene/9606:PIGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92535                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In GPIBD16; decreased function in GPI-anchor biosynthesis as indicated by reduced surface expression of various GPI-anchored proteins.|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058431|||http://purl.uniprot.org/annotation/VAR_011360|||http://purl.uniprot.org/annotation/VAR_080520|||http://purl.uniprot.org/annotation/VAR_080521|||http://purl.uniprot.org/annotation/VAR_080522
http://togogenome.org/gene/9606:FAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2M0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with monoubiquitinated FANCD2; when associated with A-44.|||Abolishes interaction with monoubiquitinated FANCD2; when associated with A-47.|||Basic and acidic residues|||D-box|||Disordered|||Fanconi-associated nuclease 1|||In KMIN.|||In KMIN; partially complement cell survival upon exposure to mitomycin C.|||In isoform 2.|||KEN box|||Loss of nuclease activity.|||Loss of nuclease activity. Loss of nuclease activity; when associated with A-864; A-975 and A-977.|||Loss of nuclease activity; when associated with A-864; A-960 and A-975.|||Loss of nuclease activity; when associated with A-864; A-960 and A-977.|||Loss of nuclease activity; when associated with A-960; A-975 and A-977.|||Phosphoserine|||Still localized to sites of DNA damage but the strength of the signal is diminished.|||Strongly reduced affinity for sites that have a 5'-terminal phosphate anchor at a flap of 1 nucleotide; when associated with A-706.|||Strongly reduced affinity for sites that have a 5'-terminal phosphate anchor at a flap of 1 nucleotide; when associated with A-952.|||UBZ4-type|||VRR-NUC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311224|||http://purl.uniprot.org/annotation/VAR_037167|||http://purl.uniprot.org/annotation/VAR_068958|||http://purl.uniprot.org/annotation/VAR_068959|||http://purl.uniprot.org/annotation/VAR_068960|||http://purl.uniprot.org/annotation/VAR_068961|||http://purl.uniprot.org/annotation/VSP_029429|||http://purl.uniprot.org/annotation/VSP_029430
http://togogenome.org/gene/9606:DCAF12L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU92                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 12-like protein 1|||Disordered|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306848|||http://purl.uniprot.org/annotation/VAR_035323
http://togogenome.org/gene/9606:GPR26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDV2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 26|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||No effect on constitutive activity.|||No effect on constitutive activity; when associated with A-104. No effect on constitutive activity; when associated with Q-104.|||No effect on constitutive activity; when associated with E-236.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069545
http://togogenome.org/gene/9606:PLCXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUJ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PI-PLC X domain-containing protein 1|||PI-PLC X-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304804
http://togogenome.org/gene/9606:MFAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55083                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Fibrinogen C-terminal|||In isoform 2.|||Microfibril-associated glycoprotein 4|||Moderate reduction in its interaction with COL1A1. Significant reduction in its interaction with ELN.|||N-linked (GlcNAc...) asparagine|||No effect on its interaction with COL1A1 and ELN.|||Significant reduction in its interaction with COL1A1 and ELN.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009134|||http://purl.uniprot.org/annotation/VAR_069073|||http://purl.uniprot.org/annotation/VSP_045831
http://togogenome.org/gene/9606:SVBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N300                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Decreased VASH1 tyrosine carboxypeptidase activity on alpha-tubulin.|||Decreased interaction with VASH1. Almost abolished VASH1 tyrosine carboxypeptidase activity on alpha-tubulin. Strongly decreased interaction with VASH2. Decreased VASH2 tyrosine carboxypeptidase activity on alpha-tubulin.|||Disordered|||In NEDAHM; probably not expressed at protein level; impaired VASH1 secretion and solubility.|||No effect on VASH1 tyrosine carboxypeptidase activity on alpha-tubulin.|||No effect on interaction with VASH2. No effect on VASH2 tyrosine carboxypeptidase activity on alpha-tubulin.|||Slightly decreased interaction with VASH1. Decreased VASH1 tyrosine carboxypeptidase activity on alpha-tubulin. No effect on interaction with VASH2. No effect on VASH2 tyrosine carboxypeptidase activity on alpha-tubulin.|||Small vasohibin-binding protein|||Strongly decreased VASH1 tyrosine carboxypeptidase activity on alpha-tubulin.|||Strongly decreased interaction with VASH1. Decreased VASH1 tyrosine carboxypeptidase activity on alpha-tubulin. Disrupted interaction with VASH2. Decreased VASH2 tyrosine carboxypeptidase activity on alpha-tubulin.|||Strongly decreased interaction with VASH1. Decreased VASH1 tyrosine carboxypeptidase activity on alpha-tubulin. Strongly decreased interaction with VASH2. Decreased VASH2 tyrosine carboxypeptidase activity on alpha-tubulin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233663|||http://purl.uniprot.org/annotation/VAR_083027
http://togogenome.org/gene/9606:SP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6BEB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Pro residues|||Transcription factor Sp5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047146|||http://purl.uniprot.org/annotation/VAR_052713
http://togogenome.org/gene/9606:NLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYT8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Mitochondrion|||N6-acetyllysine|||Neurolysin, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028575|||http://purl.uniprot.org/annotation/VAR_024594|||http://purl.uniprot.org/annotation/VAR_054002|||http://purl.uniprot.org/annotation/VAR_054003|||http://purl.uniprot.org/annotation/VAR_054004|||http://purl.uniprot.org/annotation/VAR_062224
http://togogenome.org/gene/9606:PTPRE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2Z9|||http://purl.uniprot.org/uniprot/P23469|||http://purl.uniprot.org/uniprot/Q96P81                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphotyrosine|||Receptor-type tyrosine-protein phosphatase epsilon|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025439|||http://purl.uniprot.org/annotation/PRO_5004322538|||http://purl.uniprot.org/annotation/VSP_007778|||http://purl.uniprot.org/annotation/VSP_038490
http://togogenome.org/gene/9606:NEMF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60524                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished ability to mediate CAT tailing.|||Acidic residues|||Basic and acidic residues|||Disordered|||In IDDSAPN.|||In IDDSAPN; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosome quality control complex subunit NEMF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097642|||http://purl.uniprot.org/annotation/VAR_034488|||http://purl.uniprot.org/annotation/VAR_085459|||http://purl.uniprot.org/annotation/VAR_085460|||http://purl.uniprot.org/annotation/VAR_085461|||http://purl.uniprot.org/annotation/VAR_085462|||http://purl.uniprot.org/annotation/VSP_008396|||http://purl.uniprot.org/annotation/VSP_010462|||http://purl.uniprot.org/annotation/VSP_041064|||http://purl.uniprot.org/annotation/VSP_041065|||http://purl.uniprot.org/annotation/VSP_041066
http://togogenome.org/gene/9606:TRIM50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLG2|||http://purl.uniprot.org/uniprot/Q86XT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM50|||In isoform Beta.|||N6-acetyllysine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056274|||http://purl.uniprot.org/annotation/VAR_020491|||http://purl.uniprot.org/annotation/VAR_085709|||http://purl.uniprot.org/annotation/VSP_012088
http://togogenome.org/gene/9606:YIF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BJH7|||http://purl.uniprot.org/uniprot/Q9H5F7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In KABAMAS; decreased protein abundance.|||In KABAMAS; loss of expression.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Protein YIF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307258|||http://purl.uniprot.org/annotation/VAR_035385|||http://purl.uniprot.org/annotation/VAR_085531|||http://purl.uniprot.org/annotation/VAR_085532|||http://purl.uniprot.org/annotation/VSP_028650|||http://purl.uniprot.org/annotation/VSP_028651|||http://purl.uniprot.org/annotation/VSP_028652|||http://purl.uniprot.org/annotation/VSP_028653|||http://purl.uniprot.org/annotation/VSP_028654|||http://purl.uniprot.org/annotation/VSP_028655|||http://purl.uniprot.org/annotation/VSP_046823
http://togogenome.org/gene/9606:GARIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ4|||http://purl.uniprot.org/uniprot/Q8TC56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bipartite nuclear localization signal|||Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285643|||http://purl.uniprot.org/annotation/VAR_032036|||http://purl.uniprot.org/annotation/VAR_032037|||http://purl.uniprot.org/annotation/VAR_032038
http://togogenome.org/gene/9606:NFIX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHW2|||http://purl.uniprot.org/uniprot/Q14938                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Asymmetric dimethylarginine|||CTF/NF-I|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MALNS.|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4 and isoform 6.|||In isoform 5.|||Nuclear factor 1 X-type|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100203|||http://purl.uniprot.org/annotation/VAR_068720|||http://purl.uniprot.org/annotation/VAR_068721|||http://purl.uniprot.org/annotation/VAR_077571|||http://purl.uniprot.org/annotation/VAR_077572|||http://purl.uniprot.org/annotation/VAR_077573|||http://purl.uniprot.org/annotation/VAR_077574|||http://purl.uniprot.org/annotation/VSP_003558|||http://purl.uniprot.org/annotation/VSP_003559|||http://purl.uniprot.org/annotation/VSP_003560|||http://purl.uniprot.org/annotation/VSP_003561|||http://purl.uniprot.org/annotation/VSP_003562
http://togogenome.org/gene/9606:IL6ST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0N0L2|||http://purl.uniprot.org/uniprot/P40189|||http://purl.uniprot.org/uniprot/Q17RA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with increased levels of soluble IL6RB in blood serum.|||Box 1 motif|||Cytoplasmic|||Disordered|||Does not induce ligand-independent activation.|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Found in patient with lung cancer; unknown pathological significance.|||Helical|||Ig-like C2-type|||In HIES4A; results in impaired cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, OSM and LIF and a weak response to IL-27.|||In HIES4A; results in impaired cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, OSM, LIF and a weak response to IL-27.|||In HIES4B; results in defective cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, IL-27, OSM but not LIF.|||In HIES4B; results in defective cytokine-mediated signaling pathway.|||In HIES4B; results in impaired cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, IL-27 and reduced response to OSM, CNTF and LIF.|||In IMD94; results in constitutively active IL6-mediated signaling and constitutive phosphorylation of STAT3 in patient cells.|||In STWS2; results in impaired cytokine-mediated signaling pathway with loss of response to IL-6, IL-11, IL-27, OSM and LIF; does not localize to the cell membrane.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increases cell surface expression.|||Induces ligand-independent activation.|||Interleukin-6 receptor subunit beta|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Refractory to inhibition by SOCS3.|||Results in impaired cytokine-mediated signaling pathway with loss of response to IL-6 and IL-11. Weak response to IL-27, OSM and LIF.|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010899|||http://purl.uniprot.org/annotation/PRO_5001967426|||http://purl.uniprot.org/annotation/PRO_5014308179|||http://purl.uniprot.org/annotation/VAR_036165|||http://purl.uniprot.org/annotation/VAR_047782|||http://purl.uniprot.org/annotation/VAR_047783|||http://purl.uniprot.org/annotation/VAR_047784|||http://purl.uniprot.org/annotation/VAR_047785|||http://purl.uniprot.org/annotation/VAR_047786|||http://purl.uniprot.org/annotation/VAR_074654|||http://purl.uniprot.org/annotation/VAR_083197|||http://purl.uniprot.org/annotation/VAR_083198|||http://purl.uniprot.org/annotation/VAR_086950|||http://purl.uniprot.org/annotation/VAR_086951|||http://purl.uniprot.org/annotation/VAR_086952|||http://purl.uniprot.org/annotation/VAR_086953|||http://purl.uniprot.org/annotation/VAR_086954|||http://purl.uniprot.org/annotation/VAR_086955|||http://purl.uniprot.org/annotation/VSP_001684|||http://purl.uniprot.org/annotation/VSP_001685|||http://purl.uniprot.org/annotation/VSP_043716
http://togogenome.org/gene/9606:IRGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J7NNX4|||http://purl.uniprot.org/uniprot/Q6NXR0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||IRG-type G|||Interferon-inducible GTPase 5|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285265|||http://purl.uniprot.org/annotation/VAR_032008
http://togogenome.org/gene/9606:HSD3B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14060                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1|||Helical|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087774|||http://purl.uniprot.org/annotation/VAR_000005|||http://purl.uniprot.org/annotation/VAR_014174|||http://purl.uniprot.org/annotation/VAR_014175|||http://purl.uniprot.org/annotation/VAR_048096|||http://purl.uniprot.org/annotation/VAR_048097|||http://purl.uniprot.org/annotation/VAR_048098
http://togogenome.org/gene/9606:SMIM15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3B0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Small integral membrane protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326075|||http://purl.uniprot.org/annotation/VAR_039986
http://togogenome.org/gene/9606:KRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35908                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In IBS.|||In IBS; unknown pathological significance.|||Keratin, type II cytoskeletal 2 epidermal|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063715|||http://purl.uniprot.org/annotation/VAR_003865|||http://purl.uniprot.org/annotation/VAR_003866|||http://purl.uniprot.org/annotation/VAR_003867|||http://purl.uniprot.org/annotation/VAR_009185|||http://purl.uniprot.org/annotation/VAR_009186|||http://purl.uniprot.org/annotation/VAR_009187|||http://purl.uniprot.org/annotation/VAR_010514|||http://purl.uniprot.org/annotation/VAR_010515|||http://purl.uniprot.org/annotation/VAR_010516|||http://purl.uniprot.org/annotation/VAR_017829|||http://purl.uniprot.org/annotation/VAR_031082|||http://purl.uniprot.org/annotation/VAR_031083|||http://purl.uniprot.org/annotation/VAR_031084|||http://purl.uniprot.org/annotation/VAR_031085|||http://purl.uniprot.org/annotation/VAR_031086|||http://purl.uniprot.org/annotation/VAR_058293|||http://purl.uniprot.org/annotation/VAR_058294|||http://purl.uniprot.org/annotation/VAR_086330
http://togogenome.org/gene/9606:C1orf115                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7X2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Required for drug-induced death protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265073
http://togogenome.org/gene/9606:PDZD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVR9|||http://purl.uniprot.org/uniprot/B3KW03|||http://purl.uniprot.org/uniprot/Q17RL8|||http://purl.uniprot.org/uniprot/Q76G19                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||PDZ|||PDZ domain-containing protein 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055921|||http://purl.uniprot.org/annotation/VAR_035952|||http://purl.uniprot.org/annotation/VSP_054521
http://togogenome.org/gene/9606:ADNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DHZ8|||http://purl.uniprot.org/uniprot/Q9H2P0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Activity-dependent neuroprotector homeobox protein|||Asymmetric dimethylarginine|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; atypical|||C2H2-type 6; atypical|||C2H2-type 7|||C2H2-type 8; atypical|||C2H2-type 9; atypical|||Disordered|||Found in a patient with autism; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox|||N6-acetyllysine; alternate|||Neuroprotective peptide (NAP)|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048807|||http://purl.uniprot.org/annotation/VAR_078696
http://togogenome.org/gene/9606:OR56B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH76                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 56B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150798|||http://purl.uniprot.org/annotation/VAR_024153
http://togogenome.org/gene/9606:LDB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6E1WJ75|||http://purl.uniprot.org/uniprot/Q86U70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ESR1.|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||LIM domain-binding protein 1|||LIM interaction|||LIM interaction domain (LID)|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084384|||http://purl.uniprot.org/annotation/VAR_036366|||http://purl.uniprot.org/annotation/VSP_027830|||http://purl.uniprot.org/annotation/VSP_027831|||http://purl.uniprot.org/annotation/VSP_027832
http://togogenome.org/gene/9606:SORL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92673                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects the nuclear location of the C-terminal fragment generated by PSEN1.|||BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||Cell attachment site|||Cytoplasmic|||DXXLL motif involved in the interaction with GGA1|||EGF-like|||Endocytosis signal|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||In AD; unknown pathological significance.|||In AD; unknown pathological significance; loss of interaction with APP amyloid-beta peptides, hence reduced turnover of APP amyloid-beta peptides in cells.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||LDL-receptor class A 1|||LDL-receptor class A 10|||LDL-receptor class A 11|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class A 9|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||Loss of interaction with GGA1 and PACS1. No effect on interaction with APP. Affects subcellular location, by causing increased localization to recycling endosomes. Increased APP processing by alpha-secretase, resulting in increased levels of soluble APP-alpha and C83 APP fragments. Decreased APP processing by beta-secretase, resulting in reduced levels of C99 APP fragment.|||Loss of interaction with GGA1 and PACS1. No effect on interaction with APP. Affects subcellular location, increasing localization at the cell surface, possibly due to drastically decreased endocytosis. Impaired Golgi apparatus - endosome sorting. Increased amyloidogenic APP processing by beta-secretase, resulting in increased levels of soluble APP-beta and amyloid-beta protein 40 and 42. Loss of APOA5 internalization.|||Loss of propeptide cleavage.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on endocytosis.|||No effect on endocytosis. Affects LPL sorting to endosomes.|||No effect on endocytosis. Decreased Golgi apparatus - endosome sorting.|||No effect on the interaction with HSPA12A.|||Phosphoserine|||Phosphoserine; by ROCK2|||Potential nuclear localization signal for the C-terminal fragment generated by PSEN1|||Removed in mature form|||Required for efficient Golgi apparatus - endosome sorting|||Required for interaction with GGA1 and GGA2|||Sortilin-related receptor|||Strong decrease in interaction with HSPA12A.|||Strong reduction in Golgi apparatus - endosome sorting. Loss of interaction with AP-1 complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033164|||http://purl.uniprot.org/annotation/PRO_0000033165|||http://purl.uniprot.org/annotation/VAR_020360|||http://purl.uniprot.org/annotation/VAR_034508|||http://purl.uniprot.org/annotation/VAR_034509|||http://purl.uniprot.org/annotation/VAR_036371|||http://purl.uniprot.org/annotation/VAR_036372|||http://purl.uniprot.org/annotation/VAR_036373|||http://purl.uniprot.org/annotation/VAR_070012|||http://purl.uniprot.org/annotation/VAR_070013|||http://purl.uniprot.org/annotation/VAR_070014|||http://purl.uniprot.org/annotation/VAR_070015|||http://purl.uniprot.org/annotation/VAR_070016
http://togogenome.org/gene/9606:ATP2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14983|||http://purl.uniprot.org/uniprot/Q7Z675                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In BROD.|||In isoform 3.|||In isoform SERCA1A and isoform 3.|||Interaction with PLN|||Phosphoserine|||Phosphothreonine|||Sarcoplasmic/endoplasmic reticulum calcium ATPase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046187|||http://purl.uniprot.org/annotation/VAR_015588|||http://purl.uniprot.org/annotation/VSP_000355|||http://purl.uniprot.org/annotation/VSP_054770
http://togogenome.org/gene/9606:FOLR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14207                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Folate receptor beta|||GPI-anchor amidated asparagine|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008806|||http://purl.uniprot.org/annotation/PRO_0000008807|||http://purl.uniprot.org/annotation/VAR_036408
http://togogenome.org/gene/9606:GPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78333                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glypican-5|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Removed in mature form|||Secreted glypican-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012319|||http://purl.uniprot.org/annotation/PRO_0000012320|||http://purl.uniprot.org/annotation/PRO_0000333849|||http://purl.uniprot.org/annotation/VAR_024228
http://togogenome.org/gene/9606:RBM12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In SCZD19; associated with disease susceptibility.|||Phosphoserine|||Pro residues|||RNA-binding protein 12|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081770|||http://purl.uniprot.org/annotation/VAR_052217|||http://purl.uniprot.org/annotation/VAR_052218|||http://purl.uniprot.org/annotation/VAR_078980
http://togogenome.org/gene/9606:NR6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8S0|||http://purl.uniprot.org/uniprot/F1DAM1|||http://purl.uniprot.org/uniprot/Q15406                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 6 group A member 1|||Polar residues|||Sufficient for interaction with UIMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053741|||http://purl.uniprot.org/annotation/VSP_003720|||http://purl.uniprot.org/annotation/VSP_003721|||http://purl.uniprot.org/annotation/VSP_025927
http://togogenome.org/gene/9606:POU5F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2IYK3|||http://purl.uniprot.org/uniprot/F2Z381|||http://purl.uniprot.org/uniprot/M1S623|||http://purl.uniprot.org/uniprot/Q01860                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  9aaTAD|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Homeobox|||In isoform B.|||POU domain, class 5, transcription factor 1|||POU-specific|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100747|||http://purl.uniprot.org/annotation/VAR_003774|||http://purl.uniprot.org/annotation/VAR_003775|||http://purl.uniprot.org/annotation/VAR_046203|||http://purl.uniprot.org/annotation/VAR_046204|||http://purl.uniprot.org/annotation/VSP_002333
http://togogenome.org/gene/9606:TMA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2S6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic and acidic residues|||Disordered|||Translation machinery-associated protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235681
http://togogenome.org/gene/9606:GRXCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFK2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glutaredoxin domain-containing cysteine-rich protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349191|||http://purl.uniprot.org/annotation/VAR_060192
http://togogenome.org/gene/9606:RGS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43566                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GoLoco|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Necessary for interaction with RABGEF1|||Phosphoserine|||Polar residues|||RBD 1|||RBD 2|||RGS|||Regulator of G-protein signaling 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204217|||http://purl.uniprot.org/annotation/VSP_027577|||http://purl.uniprot.org/annotation/VSP_027578|||http://purl.uniprot.org/annotation/VSP_027579|||http://purl.uniprot.org/annotation/VSP_029426|||http://purl.uniprot.org/annotation/VSP_037959
http://togogenome.org/gene/9606:CLIC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FIC5|||http://purl.uniprot.org/uniprot/Q9Y696                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chloride intracellular channel protein 4|||GST C-terminal|||Helical; Note=After insertion into the membrane|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Required for insertion into the membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144210
http://togogenome.org/gene/9606:PALM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDB9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Paralemmin-3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332171|||http://purl.uniprot.org/annotation/PRO_0000332172|||http://purl.uniprot.org/annotation/VAR_053804
http://togogenome.org/gene/9606:SESTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTX3|||http://purl.uniprot.org/uniprot/Q86VW0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CRAL-TRIO|||SEC14 domain and spectrin repeat-containing protein 1|||Spectrin 1|||Spectrin 2|||Spectrin 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309479|||http://purl.uniprot.org/annotation/VAR_036963|||http://purl.uniprot.org/annotation/VAR_051919
http://togogenome.org/gene/9606:CRTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UUV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form the MECT1-MAML2 and MAML2-MECT1 fusion proteins|||CREB-regulated transcription coactivator 1|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by SIK1 and SIK2|||Phosphothreonine|||Polar residues|||Pro residues|||Required for ubiquitination and degradation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096354|||http://purl.uniprot.org/annotation/VAR_053934|||http://purl.uniprot.org/annotation/VAR_053935|||http://purl.uniprot.org/annotation/VAR_053936|||http://purl.uniprot.org/annotation/VSP_051749|||http://purl.uniprot.org/annotation/VSP_051750|||http://purl.uniprot.org/annotation/VSP_051751
http://togogenome.org/gene/9606:TXNDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY8|||http://purl.uniprot.org/uniprot/Q86VQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||22 X 15 AA approximate tandem repeat of Q-P-K-X-G-D-I-P-K-S-[PS]-E-[KE]-X-I|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120153|||http://purl.uniprot.org/annotation/VAR_022762|||http://purl.uniprot.org/annotation/VAR_022763|||http://purl.uniprot.org/annotation/VAR_022764|||http://purl.uniprot.org/annotation/VAR_022765|||http://purl.uniprot.org/annotation/VAR_057351|||http://purl.uniprot.org/annotation/VAR_057352|||http://purl.uniprot.org/annotation/VSP_014328|||http://purl.uniprot.org/annotation/VSP_053684
http://togogenome.org/gene/9606:CAMTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Y1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Basic and acidic residues|||CG-1|||Calmodulin-binding transcription activator 1|||Disordered|||Found in patients with late onset progressive myoclonus epilepsy; unknown pathological significance.|||IPT/TIG|||IQ 1|||IQ 2|||IQ 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235820|||http://purl.uniprot.org/annotation/VAR_047824|||http://purl.uniprot.org/annotation/VAR_047825|||http://purl.uniprot.org/annotation/VAR_047826|||http://purl.uniprot.org/annotation/VAR_085043|||http://purl.uniprot.org/annotation/VSP_035936|||http://purl.uniprot.org/annotation/VSP_035937|||http://purl.uniprot.org/annotation/VSP_043842|||http://purl.uniprot.org/annotation/VSP_043843|||http://purl.uniprot.org/annotation/VSP_046358|||http://purl.uniprot.org/annotation/VSP_046359
http://togogenome.org/gene/9606:DUSP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51452                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 3|||In isoform 2.|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094795|||http://purl.uniprot.org/annotation/VSP_056284
http://togogenome.org/gene/9606:PARP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59ER9|||http://purl.uniprot.org/uniprot/Q8IXQ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||Loss of ADP ribosylation activity and interaction with DTX3L.|||Macro|||Macro 1|||Macro 2|||No defect in ADP ribosylation and interaction with DTX3L.|||No defect in ubiquitin ADP ribosylation and the interaction with DTX3L.|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP9|||Reduces ADP ribosylation activity and interaction with DTX3L.|||Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-147.|||Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-346.|||Severe reduction in ubiquitin ADP ribosylation. No effect on the interaction with DTX3L and on DTX3LE3 ligase activity. Increases DNA repair.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211339|||http://purl.uniprot.org/annotation/VAR_056654|||http://purl.uniprot.org/annotation/VAR_056655|||http://purl.uniprot.org/annotation/VAR_056656|||http://purl.uniprot.org/annotation/VAR_056657|||http://purl.uniprot.org/annotation/VSP_008505|||http://purl.uniprot.org/annotation/VSP_046086|||http://purl.uniprot.org/annotation/VSP_046087
http://togogenome.org/gene/9606:TP53RK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S44                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EKC/KEOPS complex subunit TP53RK|||In GAMOS4.|||In GAMOS4; abolished interaction with TPRKB.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088190|||http://purl.uniprot.org/annotation/VAR_014427|||http://purl.uniprot.org/annotation/VAR_030870|||http://purl.uniprot.org/annotation/VAR_041881|||http://purl.uniprot.org/annotation/VAR_041882|||http://purl.uniprot.org/annotation/VAR_080371|||http://purl.uniprot.org/annotation/VAR_080372|||http://purl.uniprot.org/annotation/VAR_080373
http://togogenome.org/gene/9606:LRRC31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N629|||http://purl.uniprot.org/uniprot/Q6UY01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 31|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229922|||http://purl.uniprot.org/annotation/VAR_034085|||http://purl.uniprot.org/annotation/VAR_051111|||http://purl.uniprot.org/annotation/VAR_051112|||http://purl.uniprot.org/annotation/VSP_017797|||http://purl.uniprot.org/annotation/VSP_017798|||http://purl.uniprot.org/annotation/VSP_017799|||http://purl.uniprot.org/annotation/VSP_055910|||http://purl.uniprot.org/annotation/VSP_055911
http://togogenome.org/gene/9606:RAB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61106                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||N-acetylalanine|||Ras-related protein Rab-14|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121185|||http://purl.uniprot.org/annotation/VAR_012986
http://togogenome.org/gene/9606:PRPF40A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75400                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FF 1|||FF 2|||FF 3|||FF 4|||FF 5|||FF 6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 5.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA-processing factor 40 homolog A|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076085|||http://purl.uniprot.org/annotation/VSP_008047|||http://purl.uniprot.org/annotation/VSP_008048|||http://purl.uniprot.org/annotation/VSP_040781|||http://purl.uniprot.org/annotation/VSP_040782|||http://purl.uniprot.org/annotation/VSP_040783
http://togogenome.org/gene/9606:NR2E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6ZGT9|||http://purl.uniprot.org/uniprot/Q9Y466                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 2 group E member 1|||Required for transcriptional repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053592|||http://purl.uniprot.org/annotation/VSP_054639
http://togogenome.org/gene/9606:ABHD14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUJ0                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Protein ABHD14A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282285|||http://purl.uniprot.org/annotation/VAR_031390|||http://purl.uniprot.org/annotation/VAR_031391
http://togogenome.org/gene/9606:LYZL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YUZ8|||http://purl.uniprot.org/uniprot/Q6UWQ5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lysozyme|||Disordered|||Glycosyl hydrolases family 22 (GH22)|||In isoform 2.|||Lysozyme-like protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240635|||http://purl.uniprot.org/annotation/VAR_026817|||http://purl.uniprot.org/annotation/VSP_019402
http://togogenome.org/gene/9606:BMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13497                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein 1|||CUB 1|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||Disordered|||Doesn't abolish secretion.|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||In OI13; leads to a protein with deficient procollagen IC-terminal propeptide proteolytic activity.|||In OI13; partial loss of activity.|||In OI13; the mutation leads to severely reduced post-translational N-glycosylation of the protein and impairs protein secretion; leads to both reduced secretion and subsequent reduced processing of the substrates CHRD and COL1A1.|||In a breast cancer sample; somatic mutation.|||In isoform BMP1-1.|||In isoform BMP1-4.|||In isoform BMP1-5.|||In isoform BMP1-6.|||In isoform BMP1-7.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Peptidase M12A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028889|||http://purl.uniprot.org/annotation/PRO_0000028890|||http://purl.uniprot.org/annotation/VAR_036141|||http://purl.uniprot.org/annotation/VAR_051584|||http://purl.uniprot.org/annotation/VAR_067224|||http://purl.uniprot.org/annotation/VAR_069096|||http://purl.uniprot.org/annotation/VAR_072248|||http://purl.uniprot.org/annotation/VSP_005461|||http://purl.uniprot.org/annotation/VSP_005462|||http://purl.uniprot.org/annotation/VSP_005463|||http://purl.uniprot.org/annotation/VSP_005464|||http://purl.uniprot.org/annotation/VSP_005465|||http://purl.uniprot.org/annotation/VSP_005466|||http://purl.uniprot.org/annotation/VSP_005467|||http://purl.uniprot.org/annotation/VSP_005468|||http://purl.uniprot.org/annotation/VSP_005469|||http://purl.uniprot.org/annotation/VSP_005470
http://togogenome.org/gene/9606:RSU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15404                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||N-acetylserine|||Ras suppressor protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097499|||http://purl.uniprot.org/annotation/VSP_043831
http://togogenome.org/gene/9606:PPARD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8S7|||http://purl.uniprot.org/uniprot/Q03181                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||NR C4-type|||NR LBD|||Nuclear receptor|||Peroxisome proliferator-activated receptor delta|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053486|||http://purl.uniprot.org/annotation/VSP_010133|||http://purl.uniprot.org/annotation/VSP_010134|||http://purl.uniprot.org/annotation/VSP_043787|||http://purl.uniprot.org/annotation/VSP_046104
http://togogenome.org/gene/9606:MRPL58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14197                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL62|||Mitochondrion|||N5-methylglutamine|||Strongly impairs peptide release activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030339|||http://purl.uniprot.org/annotation/VAR_020045|||http://purl.uniprot.org/annotation/VAR_024604|||http://purl.uniprot.org/annotation/VAR_061767
http://togogenome.org/gene/9606:ANGPTL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI99                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Angiopoietin-related protein 6|||Disordered|||Fibrinogen C-terminal|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009128
http://togogenome.org/gene/9606:INPP5E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||13 X 4 AA repeats of P-X-X-P|||2|||3|||4|||5|||6|||7|||8|||9|||Abolishes farnesylation-dependent interaction with PDE6D.|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In JBTS1.|||In JBTS1; associated with W-512; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In JBTS1; associated with W-515; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In JBTS1; reduced levels of protein in patients' fibroblasts; significant number of cells from patients have shorter or no cilia.|||In JBTS1; severe reduction of phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In JBTS1; slightly reduced phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In JBTS1; unknown pathological significance.|||In isoform 2.|||Phosphatidylinositol polyphosphate 5-phosphatase type IV|||Phosphoserine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209747|||http://purl.uniprot.org/annotation/PRO_0000431688|||http://purl.uniprot.org/annotation/VAR_047078|||http://purl.uniprot.org/annotation/VAR_063012|||http://purl.uniprot.org/annotation/VAR_063013|||http://purl.uniprot.org/annotation/VAR_063014|||http://purl.uniprot.org/annotation/VAR_063015|||http://purl.uniprot.org/annotation/VAR_063016|||http://purl.uniprot.org/annotation/VAR_063017|||http://purl.uniprot.org/annotation/VAR_076892|||http://purl.uniprot.org/annotation/VAR_077247|||http://purl.uniprot.org/annotation/VAR_077248|||http://purl.uniprot.org/annotation/VAR_077249|||http://purl.uniprot.org/annotation/VAR_077250|||http://purl.uniprot.org/annotation/VAR_077251|||http://purl.uniprot.org/annotation/VAR_077252|||http://purl.uniprot.org/annotation/VAR_077253|||http://purl.uniprot.org/annotation/VAR_077254|||http://purl.uniprot.org/annotation/VAR_081790|||http://purl.uniprot.org/annotation/VSP_009799
http://togogenome.org/gene/9606:ZMYM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K126|||http://purl.uniprot.org/uniprot/Q9UBW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Breakpoint for translocation to form ZMYM2-FGFR1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NECRC.|||In NECRC; does not localize to the nucleus; decreased interaction with FOXP1 and FOXP2.|||In NECRC; does not localize to the nucleus; loss of interaction with FOXP1 and FOXP2.|||In isoform 2.|||Likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus.|||Likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; no effect on localization to the nucleus; no effect on transcriptional repression activity.|||Likely benign variant; found in a patient with congenital anomalies of the kidney and urinary tract; requires 2 nucleotide substitutions; no effect on localization to the nucleus.|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||MYM-type 5|||MYM-type 6|||MYM-type 7|||MYM-type 8|||Phosphoserine|||Phosphothreonine|||Polar residues|||TRASH|||Zinc finger MYM-type protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191382|||http://purl.uniprot.org/annotation/VAR_086274|||http://purl.uniprot.org/annotation/VAR_086275|||http://purl.uniprot.org/annotation/VAR_086276|||http://purl.uniprot.org/annotation/VAR_086277|||http://purl.uniprot.org/annotation/VAR_086278|||http://purl.uniprot.org/annotation/VAR_086279|||http://purl.uniprot.org/annotation/VAR_086280|||http://purl.uniprot.org/annotation/VAR_086281|||http://purl.uniprot.org/annotation/VAR_086282|||http://purl.uniprot.org/annotation/VAR_086283|||http://purl.uniprot.org/annotation/VAR_086284|||http://purl.uniprot.org/annotation/VAR_086285|||http://purl.uniprot.org/annotation/VAR_086286|||http://purl.uniprot.org/annotation/VAR_086287|||http://purl.uniprot.org/annotation/VAR_086288|||http://purl.uniprot.org/annotation/VSP_039065|||http://purl.uniprot.org/annotation/VSP_039066|||http://purl.uniprot.org/annotation/VSP_039067
http://togogenome.org/gene/9606:IGSF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969P0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EWI motif|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Immunoglobulin superfamily member 8|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226247|||http://purl.uniprot.org/annotation/VSP_017429|||http://purl.uniprot.org/annotation/VSP_017430|||http://purl.uniprot.org/annotation/VSP_017431
http://togogenome.org/gene/9606:SSBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04837                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Found in a patient with a systemic mitochondrial disorder; unknown pathological significance; impaired multimerization; reduced ability to stimulate POLG-dependent DNA synthesis in vitro; mtDNA depletion without any detectable energetic defects.|||In OPA13.|||In OPA13; may impair dimerization and tetramerization.|||In OPA13; reduced ability to stimulate POLG-dependent DNA synthesis in vitro.|||In mtSSB45-1; decreased POLG polymerase activity and increased unwinding of double-stranded DNA by the helicase TWNK, in vitro.|||In mtSSB45-2; decreased unwinding of double-stranded DNA by the helicase TWNK, in vitro.|||In mtSSBalpha1; decreased POLG polymerase activity, in vitro. No effect on unwinding of double-stranded DNA by the helicase TWNK.|||In mtSSBloop12; decreased unwinding of double-stranded DNA by the helicase TWNK and increased binding to single-stranded DNA, in vitro.|||In mtSSBloop23; reduced ability to open template DNA and decreased POLG polymerase activity, in vitro. Also displays decreased unwinding of double-stranded DNA by the helicase TWNK and increased binding to single-stranded DNA.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||SSB|||Single-stranded DNA-binding protein, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033263|||http://purl.uniprot.org/annotation/VAR_084732|||http://purl.uniprot.org/annotation/VAR_084733|||http://purl.uniprot.org/annotation/VAR_084734|||http://purl.uniprot.org/annotation/VAR_084735|||http://purl.uniprot.org/annotation/VAR_084736|||http://purl.uniprot.org/annotation/VAR_084737|||http://purl.uniprot.org/annotation/VAR_084738
http://togogenome.org/gene/9606:C11orf97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C11orf97                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440043
http://togogenome.org/gene/9606:CCR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51685                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 8|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069288|||http://purl.uniprot.org/annotation/VAR_049384|||http://purl.uniprot.org/annotation/VSP_056340
http://togogenome.org/gene/9606:TEX13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YWL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Putative testis-expressed protein 13C|||RanBP2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000435874
http://togogenome.org/gene/9606:HGFAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RAR4|||http://purl.uniprot.org/uniprot/Q04756                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Fibronectin type-I|||Fibronectin type-II|||Hepatocyte growth factor activator long chain|||Hepatocyte growth factor activator short chain|||Interchain (between short and long chains)|||Kringle|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027911|||http://purl.uniprot.org/annotation/PRO_0000027912|||http://purl.uniprot.org/annotation/PRO_0000027913|||http://purl.uniprot.org/annotation/PRO_5003087349|||http://purl.uniprot.org/annotation/VAR_024294|||http://purl.uniprot.org/annotation/VAR_024295|||http://purl.uniprot.org/annotation/VAR_033651|||http://purl.uniprot.org/annotation/VAR_033652|||http://purl.uniprot.org/annotation/VAR_051851
http://togogenome.org/gene/9606:EXOSC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDZ9|||http://purl.uniprot.org/uniprot/Q15024                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exoribonuclease phosphorolytic|||Exosome complex component RRP42|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139963|||http://purl.uniprot.org/annotation/VAR_014923|||http://purl.uniprot.org/annotation/VAR_032765
http://togogenome.org/gene/9606:EDARADD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Death|||Disordered|||Ectodysplasin-A receptor-associated adapter protein|||In ECTD11A.|||In ECTD11A; severely impairs NF-kappa-B activation and acted in a dominant-negative manner.|||In ECTD11B; impairs the interaction with EDAR and severely inhibits NF-kappa-B activity.|||In ECTD11B; may reduce binding to EDAR; impairs NF-kappa-B activation by about 50%.|||In isoform B.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086928|||http://purl.uniprot.org/annotation/VAR_013482|||http://purl.uniprot.org/annotation/VAR_050963|||http://purl.uniprot.org/annotation/VAR_054509|||http://purl.uniprot.org/annotation/VAR_054510|||http://purl.uniprot.org/annotation/VAR_064835|||http://purl.uniprot.org/annotation/VAR_064836|||http://purl.uniprot.org/annotation/VSP_003861
http://togogenome.org/gene/9606:LGALS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47929                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076940
http://togogenome.org/gene/9606:C19orf25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFG5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphotyrosine|||UPF0449 protein C19orf25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252420|||http://purl.uniprot.org/annotation/VSP_020961
http://togogenome.org/gene/9606:AARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTZ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Alanine--tRNA ligase, mitochondrial|||Found in patient with leukoencephalopathy; unknown pathological significance.|||In COXPD8.|||In LKENP.|||In LKENP; deleterious only under stress conditions.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250725|||http://purl.uniprot.org/annotation/VAR_027609|||http://purl.uniprot.org/annotation/VAR_027610|||http://purl.uniprot.org/annotation/VAR_057357|||http://purl.uniprot.org/annotation/VAR_065956|||http://purl.uniprot.org/annotation/VAR_065957|||http://purl.uniprot.org/annotation/VAR_071837|||http://purl.uniprot.org/annotation/VAR_071838|||http://purl.uniprot.org/annotation/VAR_071839|||http://purl.uniprot.org/annotation/VAR_071840|||http://purl.uniprot.org/annotation/VAR_071841|||http://purl.uniprot.org/annotation/VAR_071842|||http://purl.uniprot.org/annotation/VAR_071843
http://togogenome.org/gene/9606:OSBPL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXB5|||http://purl.uniprot.org/uniprot/Q9NX98                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Omega-N-methylarginine|||Oxysterol-binding protein-related protein 10|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100380|||http://purl.uniprot.org/annotation/VAR_022100|||http://purl.uniprot.org/annotation/VSP_042930
http://togogenome.org/gene/9606:RMDN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96TC7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||FFAT|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces interaction with MOSPD2.|||Regulator of microtubule dynamics protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287510|||http://purl.uniprot.org/annotation/VAR_049029|||http://purl.uniprot.org/annotation/VSP_025531
http://togogenome.org/gene/9606:VAPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0L0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alters interaction with ZFYVE27 and prevents binding to the FFAT motif in target proteins; when associated with D-94.|||Alters interaction with ZFYVE27 and prevents binding to the FFAT motif in target proteins; when associated with D-96.|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Impairs the interaction of the MSP domain with the phosphorylated FFAT motif of STARD3. Does not affect its ability to interact with the conventional FFAT motif of OSBPL1A.|||In isoform 2.|||Interchain|||Involved in binding the phosphorylated serine of the phospho-FFAT motif|||MSP|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Vesicle-associated membrane protein-associated protein A|||phosphorylated FFAT motif binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213470|||http://purl.uniprot.org/annotation/VAR_050440|||http://purl.uniprot.org/annotation/VAR_050441|||http://purl.uniprot.org/annotation/VSP_038648
http://togogenome.org/gene/9606:KANK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63ZY3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  20-fold decrease in binding to KIF21A.|||26-fold decrease in binding to KIF21A.|||33-fold decrease in binding to KIF21A.|||4-fold decrease in binding to KIF21A.|||ANK 0; degenerate|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||Impairs phosphorylation; when associated with 510-A--A-512.|||Impairs phosphorylation; when associated with A-515.|||In NPHS16; increased interaction with ARHGDIA; loss of function in regulation of the Rho signaling pathway; no effect on cytoplasmic localization; loss of function in podocytes migration.|||In NPHS16; loss of function in regulation of the Rho signaling pathway; no effect on cytoplasmic localization; decreased function in podocytes migration.|||In PPKWH.|||In isoform 2.|||In isoform 3.|||Interaction with AIFM1|||Interaction with NCOA1|||KN motif and ankyrin repeat domain-containing protein 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240840|||http://purl.uniprot.org/annotation/VAR_048304|||http://purl.uniprot.org/annotation/VAR_048305|||http://purl.uniprot.org/annotation/VAR_072431|||http://purl.uniprot.org/annotation/VAR_080959|||http://purl.uniprot.org/annotation/VAR_080960|||http://purl.uniprot.org/annotation/VSP_019427|||http://purl.uniprot.org/annotation/VSP_019428|||http://purl.uniprot.org/annotation/VSP_019429
http://togogenome.org/gene/9606:MAK16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXY0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Protein MAK16 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203794|||http://purl.uniprot.org/annotation/VAR_023076
http://togogenome.org/gene/9606:LIPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y234                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  BPL/LPL catalytic|||In LIPT1D.|||Lipoyltransferase 1, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017856|||http://purl.uniprot.org/annotation/VAR_073669|||http://purl.uniprot.org/annotation/VAR_073670|||http://purl.uniprot.org/annotation/VAR_073671
http://togogenome.org/gene/9606:TMED6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW62                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GOLD|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010393
http://togogenome.org/gene/9606:RPL30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62888                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein eL30|||N6-acetyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146120
http://togogenome.org/gene/9606:ANKHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Acidic residues|||Ankyrin repeat and KH domain-containing protein 1|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||KH|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306326|||http://purl.uniprot.org/annotation/VAR_035291|||http://purl.uniprot.org/annotation/VAR_035292|||http://purl.uniprot.org/annotation/VAR_035293|||http://purl.uniprot.org/annotation/VAR_048281|||http://purl.uniprot.org/annotation/VSP_028452|||http://purl.uniprot.org/annotation/VSP_028453|||http://purl.uniprot.org/annotation/VSP_028454|||http://purl.uniprot.org/annotation/VSP_028455|||http://purl.uniprot.org/annotation/VSP_028456|||http://purl.uniprot.org/annotation/VSP_028457|||http://purl.uniprot.org/annotation/VSP_028458|||http://purl.uniprot.org/annotation/VSP_044231
http://togogenome.org/gene/9606:SH3GL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z376|||http://purl.uniprot.org/uniprot/Q99962                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Strand                                                                                  ^@                                                                                  BAR|||Binds and tubulates liposomes|||Disordered|||Endophilin-A1|||Loss of tubulation of liposomes, no effect on liposome binding.|||Membrane-binding amphipathic helix|||No effect. Indol ring not associated with the membrane.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 and S-66.|||Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 or with S-63 and Q-70.|||Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-66 or with S-66 and Q-70.|||Required for dimerization upon membrane association|||SH3|||Vesiculation of liposomes, no effect on liposome binding, indol ring located in hydrophobic core of the membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146747
http://togogenome.org/gene/9606:ZNF536                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EQN6|||http://purl.uniprot.org/uniprot/O15090                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger protein 536                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271041
http://togogenome.org/gene/9606:XKR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GH73|||http://purl.uniprot.org/uniprot/Q96KT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Pro residues|||XK-related protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190785|||http://purl.uniprot.org/annotation/VSP_014663
http://togogenome.org/gene/9606:GTF2E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29084                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||TFIIE beta|||Transcription initiation factor IIE subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211226|||http://purl.uniprot.org/annotation/VAR_039003|||http://purl.uniprot.org/annotation/VAR_052281|||http://purl.uniprot.org/annotation/VAR_076893|||http://purl.uniprot.org/annotation/VAR_076894
http://togogenome.org/gene/9606:CYP3A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08684|||http://purl.uniprot.org/uniprot/Q6GRK0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome P450 3A4|||Helical|||In VDDR3; 10-fold increased activity towards calcitriol; no effect in protein abundance; decreased activity for non-vitamin D substrates.|||In allele CYP3A4*10.|||In allele CYP3A4*11; unstable form.|||In allele CYP3A4*12; has an altered testosterone hydroxylase activity.|||In allele CYP3A4*13; lack of expression.|||In allele CYP3A4*14.|||In allele CYP3A4*15.|||In allele CYP3A4*16.|||In allele CYP3A4*17; exhibits lower turnover numbers for testosterone and chlorpyrifos.|||In allele CYP3A4*18; exhibits higher turnover numbers for testosterone and chlorpyrifos.|||In allele CYP3A4*19.|||In allele CYP3A4*2; exhibits a lower intrinsic clearance toward nifedipine.|||In allele CYP3A4*3.|||In allele CYP3A4*4; significant decrease in catalytic efficiency.|||In allele CYP3A4*5.|||In allele CYP3A4*7.|||In allele CYP3A4*8.|||In allele CYP3A4*9.|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051786|||http://purl.uniprot.org/annotation/VAR_008363|||http://purl.uniprot.org/annotation/VAR_008364|||http://purl.uniprot.org/annotation/VAR_011597|||http://purl.uniprot.org/annotation/VAR_011598|||http://purl.uniprot.org/annotation/VAR_011599|||http://purl.uniprot.org/annotation/VAR_011600|||http://purl.uniprot.org/annotation/VAR_011601|||http://purl.uniprot.org/annotation/VAR_011602|||http://purl.uniprot.org/annotation/VAR_011603|||http://purl.uniprot.org/annotation/VAR_011604|||http://purl.uniprot.org/annotation/VAR_011605|||http://purl.uniprot.org/annotation/VAR_011606|||http://purl.uniprot.org/annotation/VAR_011607|||http://purl.uniprot.org/annotation/VAR_011608|||http://purl.uniprot.org/annotation/VAR_014322|||http://purl.uniprot.org/annotation/VAR_014323|||http://purl.uniprot.org/annotation/VAR_014324|||http://purl.uniprot.org/annotation/VAR_037547|||http://purl.uniprot.org/annotation/VAR_037548|||http://purl.uniprot.org/annotation/VAR_037549|||http://purl.uniprot.org/annotation/VAR_037550|||http://purl.uniprot.org/annotation/VAR_084337
http://togogenome.org/gene/9606:CNR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34972                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes agonist-induced inhibitory effect on adenylate cyclase. No effect on ligand binding.|||Abolishes ligand binding and agonist-induced inhibitory effect on adenylate cyclase.|||Affects cannabinoid agonist binding; when associated with A-109.|||Basic and acidic residues|||Cannabinoid receptor 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||High incidence in Japanese depressed subjects.|||Loss of ligand binding. Alters agonist-induced inhibitory effect on adenylate cyclase.|||N-linked (GlcNAc...) asparagine|||No effect on agonist binding.|||No effect on agonist binding. Affects cannabinoid agonist binding; when associated with G-112.|||No effect on ligand binding. Alters agonist-induced inhibitory effect on adenylate cyclase.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069323|||http://purl.uniprot.org/annotation/VAR_029209|||http://purl.uniprot.org/annotation/VAR_054310
http://togogenome.org/gene/9606:PGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20142                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Gastricsin|||In isoform 2.|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026056|||http://purl.uniprot.org/annotation/PRO_0000026057|||http://purl.uniprot.org/annotation/VSP_042312
http://togogenome.org/gene/9606:MAPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RXH5|||http://purl.uniprot.org/uniprot/P27361|||http://purl.uniprot.org/uniprot/Q9BWJ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of ubiquitination by TRIM15; when associated with R-168.|||Complete loss of ubiquitination by TRIM15; when associated with R-302.|||Disordered|||In isoform 2.|||In isoform 3.|||Mitogen-activated protein kinase 3|||N-acetylalanine|||Phosphothreonine|||Phosphothreonine; by MAP2K1 and MAP2K2|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by MAP2K1 and MAP2K2|||Protein kinase|||Proton acceptor|||Removed|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186251|||http://purl.uniprot.org/annotation/VAR_042253|||http://purl.uniprot.org/annotation/VSP_041906|||http://purl.uniprot.org/annotation/VSP_041907
http://togogenome.org/gene/9606:TAC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UU9                                                                                  ^@                                                                                  Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Endokinin-A|||Endokinin-A/B|||Endokinin-C|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leucine amide|||Methionine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320011|||http://purl.uniprot.org/annotation/PRO_0000320012|||http://purl.uniprot.org/annotation/PRO_0000320013|||http://purl.uniprot.org/annotation/PRO_5000063346|||http://purl.uniprot.org/annotation/PRO_5000063347|||http://purl.uniprot.org/annotation/VSP_052676|||http://purl.uniprot.org/annotation/VSP_052677|||http://purl.uniprot.org/annotation/VSP_052680|||http://purl.uniprot.org/annotation/VSP_052681
http://togogenome.org/gene/9606:SGTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EQ0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat                                                                                  ^@                                                                                  N6-acetyllysine|||Phosphoserine|||Small glutamine-rich tetratricopeptide repeat-containing protein beta|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106368
http://togogenome.org/gene/9606:BMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14692                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bms1-type G|||Disordered|||G1|||G2|||G3|||G4|||G5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In ACC; fibroblasts show CDKN1A-mediated G1/S phase transition defect with a significantly reduced cell proliferation rate compared to controls; in vitro scratch assay reveal an increased cell migration rate.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosome biogenesis protein BMS1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195004|||http://purl.uniprot.org/annotation/VAR_057503|||http://purl.uniprot.org/annotation/VAR_057504|||http://purl.uniprot.org/annotation/VAR_057505|||http://purl.uniprot.org/annotation/VAR_057506|||http://purl.uniprot.org/annotation/VAR_057507|||http://purl.uniprot.org/annotation/VAR_072539
http://togogenome.org/gene/9606:OR2K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFP3|||http://purl.uniprot.org/uniprot/Q8NGT1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150485
http://togogenome.org/gene/9606:C21orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58505                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Uncharacterized protein C21orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079521|||http://purl.uniprot.org/annotation/VSP_003827|||http://purl.uniprot.org/annotation/VSP_003828|||http://purl.uniprot.org/annotation/VSP_057984
http://togogenome.org/gene/9606:TAS1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7J9|||http://purl.uniprot.org/uniprot/Q7RTX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Taste receptor type 1 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012954|||http://purl.uniprot.org/annotation/PRO_5002724685|||http://purl.uniprot.org/annotation/VAR_036707|||http://purl.uniprot.org/annotation/VAR_036708|||http://purl.uniprot.org/annotation/VAR_036709|||http://purl.uniprot.org/annotation/VSP_012418|||http://purl.uniprot.org/annotation/VSP_012420|||http://purl.uniprot.org/annotation/VSP_012421|||http://purl.uniprot.org/annotation/VSP_012422
http://togogenome.org/gene/9606:SPC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBM1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Interaction with the C-terminus of SPBC24|||Interaction with the N-terminus of SPBC24|||Interaction with the NDC80-NUF2 subcomplex|||Kinetochore protein Spc25|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249565
http://togogenome.org/gene/9606:PRR20E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86478|||http://purl.uniprot.org/uniprot/P86479|||http://purl.uniprot.org/uniprot/P86480|||http://purl.uniprot.org/uniprot/P86481|||http://purl.uniprot.org/uniprot/P86496                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 20A|||Proline-rich protein 20B|||Proline-rich protein 20C|||Proline-rich protein 20D|||Proline-rich protein 20E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336092|||http://purl.uniprot.org/annotation/PRO_0000393890|||http://purl.uniprot.org/annotation/PRO_0000393891|||http://purl.uniprot.org/annotation/PRO_0000393892|||http://purl.uniprot.org/annotation/PRO_0000393893
http://togogenome.org/gene/9606:PTPRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M9MML4|||http://purl.uniprot.org/uniprot/P08575                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In IMD105.|||In IMD105; associated with lack of surface expression.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 8.|||Loss of activity. Abolishes interaction with SKAP1.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Protein tyrosine phosphatase receptor type N-terminal|||Receptor-type tyrosine-protein phosphatase C|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025470|||http://purl.uniprot.org/annotation/PRO_5004100983|||http://purl.uniprot.org/annotation/VAR_020303|||http://purl.uniprot.org/annotation/VAR_021205|||http://purl.uniprot.org/annotation/VAR_035653|||http://purl.uniprot.org/annotation/VAR_035654|||http://purl.uniprot.org/annotation/VAR_036860|||http://purl.uniprot.org/annotation/VAR_051763|||http://purl.uniprot.org/annotation/VAR_051764|||http://purl.uniprot.org/annotation/VAR_051765|||http://purl.uniprot.org/annotation/VAR_087537|||http://purl.uniprot.org/annotation/VSP_059409|||http://purl.uniprot.org/annotation/VSP_059833|||http://purl.uniprot.org/annotation/VSP_059834|||http://purl.uniprot.org/annotation/VSP_059835|||http://purl.uniprot.org/annotation/VSP_059836|||http://purl.uniprot.org/annotation/VSP_059837
http://togogenome.org/gene/9606:TNFRSF11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00300                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Abolishes dimerization.|||Death 1|||Death 2|||Decreases inhibition of osteoclast differentiation.|||In PDB5.|||Involved in dimerization|||N-linked (GlcNAc...) asparagine|||Reduces affinity for TNFSF11. Decreases inhibition of osteoclast differentiation.|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 11B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034587|||http://purl.uniprot.org/annotation/VAR_013439|||http://purl.uniprot.org/annotation/VAR_018957|||http://purl.uniprot.org/annotation/VAR_019413
http://togogenome.org/gene/9606:ZNF354C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y25                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 354C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280408|||http://purl.uniprot.org/annotation/VAR_031138|||http://purl.uniprot.org/annotation/VAR_031139|||http://purl.uniprot.org/annotation/VAR_031140
http://togogenome.org/gene/9606:EIF4EBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13541                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Turn                                                                                  ^@                                                                                  Abolishes eIF4E-binding. Increased ubiquitination by the BCR(KLHL25) complex.|||Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-65.|||Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-46 and A-70.|||Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-37; A-65 and A-70.|||Abolishes phosphorylation by MTOR and increased ubiquitination by the BCR(KLHL25) complex; when associated with A-46; A-65 and A-70.|||Basic and acidic residues|||Disordered|||Does not affect ubiquitination by the BCR(KLHL25) complex.|||Eukaryotic translation initiation factor 4E-binding protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ubiquitination by the BCR(KLHL25) complex.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphoserine; by DYRK2, MAPK1, MAPK3 and MTOR|||Phosphothreonine|||Phosphothreonine; by MTOR|||Phosphotyrosine|||Polar residues|||Reduced interaction with RPTOR.|||Removed|||TOS motif|||YXXXXLphi motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190513
http://togogenome.org/gene/9606:CALCOCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13137                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates interaction with MAPLC3A, MAPLC3B and GABARAPL2.|||Abrogates the interaction with MAP1LC3C.|||CLIR|||Calcium-binding and coiled-coil domain-containing protein 2|||Disordered|||Does not affect interaction with MYO6.|||Fails interact with MYO6 and to promote maturation of autophagosomes.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with LGALS8|||Interaction with MYO6|||LIR-like|||Phosphoserine|||Prevents interaction with LGALS8.|||Severely reduced affinity for LGALS8.|||Severely reduces affinity for LGALS8.|||UBZ1-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312337|||http://purl.uniprot.org/annotation/VAR_037489|||http://purl.uniprot.org/annotation/VAR_037490|||http://purl.uniprot.org/annotation/VAR_037491|||http://purl.uniprot.org/annotation/VAR_037492|||http://purl.uniprot.org/annotation/VAR_037493|||http://purl.uniprot.org/annotation/VSP_044728|||http://purl.uniprot.org/annotation/VSP_046766|||http://purl.uniprot.org/annotation/VSP_046767|||http://purl.uniprot.org/annotation/VSP_047414
http://togogenome.org/gene/9606:RPE65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16518                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreasing protein levels. Loss of enzymatic activity.|||Decreasing protein levels. Loss of enzymatic activity. Significantly decreased protein stability.|||Does not affect isomerohydrolase activity.|||In LCA2 and RP20.|||In LCA2 and RP20; severely decreased retinol isomerase activity.|||In LCA2.|||In LCA2; benign variant; no effect on retinol isomerase activity.|||In LCA2; reduced protein levels; decreased function in the retinoid cycle.|||In LCA2; severely decreased retinol isomerase activity.|||In LCA2; unknown pathological significance.|||In RP20 and LCA2.|||In RP20 and LCA2; reduced protein levels; decreased function in the retinoid cycle.|||In RP20.|||In RP20; likely benign variant; very mild decrease of retinol isomerase activity.|||In RP20; uncertain pathological significance.|||In RP20; unknown pathological significance.|||In RP87; unknown pathological significance; does not affect protein abundance; does not affect subcellular localization; does not affect isomerization activity; may cause abnormal splicing mRNAs thereby decreasing protein levels.|||Increased isomerohydrolase activity.|||Loss of enzymatic activity.|||Loss of enzymatic activity. No palmitoylation. Loss of membrane association.|||N-acetylserine|||N6-acetyllysine|||No effect on retinol isomerase activity.|||No loss of enzymatic activity. No effect on palmitoylation. No loss of membrane association.|||Phosphoserine|||Phosphothreonine|||Removed|||Retinoid isomerohydrolase|||S-palmitoyl cysteine; in membrane form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143943|||http://purl.uniprot.org/annotation/VAR_017126|||http://purl.uniprot.org/annotation/VAR_017127|||http://purl.uniprot.org/annotation/VAR_017128|||http://purl.uniprot.org/annotation/VAR_017129|||http://purl.uniprot.org/annotation/VAR_017130|||http://purl.uniprot.org/annotation/VAR_017131|||http://purl.uniprot.org/annotation/VAR_017132|||http://purl.uniprot.org/annotation/VAR_017133|||http://purl.uniprot.org/annotation/VAR_017134|||http://purl.uniprot.org/annotation/VAR_017135|||http://purl.uniprot.org/annotation/VAR_017136|||http://purl.uniprot.org/annotation/VAR_017137|||http://purl.uniprot.org/annotation/VAR_017138|||http://purl.uniprot.org/annotation/VAR_017139|||http://purl.uniprot.org/annotation/VAR_017140|||http://purl.uniprot.org/annotation/VAR_017141|||http://purl.uniprot.org/annotation/VAR_017142|||http://purl.uniprot.org/annotation/VAR_018151|||http://purl.uniprot.org/annotation/VAR_034477|||http://purl.uniprot.org/annotation/VAR_037619|||http://purl.uniprot.org/annotation/VAR_060808|||http://purl.uniprot.org/annotation/VAR_060809|||http://purl.uniprot.org/annotation/VAR_060810|||http://purl.uniprot.org/annotation/VAR_060811|||http://purl.uniprot.org/annotation/VAR_060812|||http://purl.uniprot.org/annotation/VAR_060813|||http://purl.uniprot.org/annotation/VAR_060814|||http://purl.uniprot.org/annotation/VAR_060815|||http://purl.uniprot.org/annotation/VAR_060816|||http://purl.uniprot.org/annotation/VAR_060817|||http://purl.uniprot.org/annotation/VAR_060818|||http://purl.uniprot.org/annotation/VAR_060819|||http://purl.uniprot.org/annotation/VAR_060820|||http://purl.uniprot.org/annotation/VAR_060821|||http://purl.uniprot.org/annotation/VAR_060822|||http://purl.uniprot.org/annotation/VAR_060823|||http://purl.uniprot.org/annotation/VAR_060824|||http://purl.uniprot.org/annotation/VAR_067160|||http://purl.uniprot.org/annotation/VAR_067161|||http://purl.uniprot.org/annotation/VAR_067162|||http://purl.uniprot.org/annotation/VAR_067163|||http://purl.uniprot.org/annotation/VAR_067164|||http://purl.uniprot.org/annotation/VAR_067757|||http://purl.uniprot.org/annotation/VAR_070172|||http://purl.uniprot.org/annotation/VAR_070173|||http://purl.uniprot.org/annotation/VAR_071672|||http://purl.uniprot.org/annotation/VAR_080043|||http://purl.uniprot.org/annotation/VAR_081684|||http://purl.uniprot.org/annotation/VAR_083292|||http://purl.uniprot.org/annotation/VAR_083293|||http://purl.uniprot.org/annotation/VAR_083294|||http://purl.uniprot.org/annotation/VAR_083295|||http://purl.uniprot.org/annotation/VAR_083296|||http://purl.uniprot.org/annotation/VAR_083297|||http://purl.uniprot.org/annotation/VAR_083298|||http://purl.uniprot.org/annotation/VAR_083299|||http://purl.uniprot.org/annotation/VAR_083300
http://togogenome.org/gene/9606:CENPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07199                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolishes N-terminal methylation.|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Homodimerization|||Major centromere autoantigen B|||N,N,N-trimethylglycine; alternate|||N,N-dimethylglycine; alternate|||N-methylglycine; alternate|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126125
http://togogenome.org/gene/9606:GRWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glutamate-rich WD repeat-containing protein 1|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051011|||http://purl.uniprot.org/annotation/VAR_046334
http://togogenome.org/gene/9606:TOPAZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9V7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein TOPAZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320600|||http://purl.uniprot.org/annotation/VAR_039224|||http://purl.uniprot.org/annotation/VAR_039225|||http://purl.uniprot.org/annotation/VAR_039226|||http://purl.uniprot.org/annotation/VAR_039227|||http://purl.uniprot.org/annotation/VAR_039228|||http://purl.uniprot.org/annotation/VAR_039229|||http://purl.uniprot.org/annotation/VAR_039230
http://togogenome.org/gene/9606:FUNDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVP5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes phosphorylation by SRC.|||Cytoplasmic|||Does not affect interaction with MAP1 LC3 family proteins.|||FUN14 domain-containing protein 1|||Helical|||Impairs interaction with MAP1 LC3 family proteins.|||Mitochondrial intermembrane|||Phosphoserine|||Phosphotyrosine; by SRC|||YXXL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271345|||http://purl.uniprot.org/annotation/VAR_074638
http://togogenome.org/gene/9606:TCF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8M7|||http://purl.uniprot.org/uniprot/Q9Y242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FHA|||PHD-type|||Phosphoserine|||Pro residues|||Transcription factor 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059327|||http://purl.uniprot.org/annotation/VAR_017741|||http://purl.uniprot.org/annotation/VAR_017742|||http://purl.uniprot.org/annotation/VAR_051604
http://togogenome.org/gene/9606:ABHD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB40                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  (Lyso)-N-acylphosphatidylethanolamine lipase|||AB hydrolase-1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080864|||http://purl.uniprot.org/annotation/VSP_056924|||http://purl.uniprot.org/annotation/VSP_056925
http://togogenome.org/gene/9606:RFC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40938                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Replication factor C subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121761|||http://purl.uniprot.org/annotation/VAR_018750|||http://purl.uniprot.org/annotation/VSP_044920
http://togogenome.org/gene/9606:ELOVL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW60                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Elongation of very long chain fatty acids protein 1|||Helical|||In IKSHD; loss of fatty acid elongase activity.|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207536|||http://purl.uniprot.org/annotation/VAR_083193|||http://purl.uniprot.org/annotation/VSP_045436
http://togogenome.org/gene/9606:SLFN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7P3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes endoribonuclease activity.|||C-terminally truncated SLFN14 endoribonuclease|||In BDPLT20.|||In BDPLT20; the mutation results in strongly reduced protein stability.|||In BDPLT20; the mutation results in weakly reduced protein stability.|||In isoform 2.|||Protein SLFN14|||Reduces endoribonuclease activity.|||Required for endoribonuclease activity|||Required for ribosome binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342339|||http://purl.uniprot.org/annotation/PRO_0000436153|||http://purl.uniprot.org/annotation/VAR_044177|||http://purl.uniprot.org/annotation/VAR_044178|||http://purl.uniprot.org/annotation/VAR_044179|||http://purl.uniprot.org/annotation/VAR_044180|||http://purl.uniprot.org/annotation/VAR_044181|||http://purl.uniprot.org/annotation/VAR_044182|||http://purl.uniprot.org/annotation/VAR_075786|||http://purl.uniprot.org/annotation/VAR_075787|||http://purl.uniprot.org/annotation/VAR_075788|||http://purl.uniprot.org/annotation/VAR_076796|||http://purl.uniprot.org/annotation/VSP_034414
http://togogenome.org/gene/9606:NDUFAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P032                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  In MC1DN15.|||In MC1DN15; results in altered complex I assembly.|||N-myristoyl glycine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 4|||Phosphoserine|||Reduces interaction with calmodulin. Does not promote MMP-9 secretion.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220988|||http://purl.uniprot.org/annotation/VAR_044329|||http://purl.uniprot.org/annotation/VAR_081426
http://togogenome.org/gene/9606:ARHGAP45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVA9|||http://purl.uniprot.org/uniprot/B3KXW7|||http://purl.uniprot.org/uniprot/F5H1R4|||http://purl.uniprot.org/uniprot/K7ES92|||http://purl.uniprot.org/uniprot/K7ES98|||http://purl.uniprot.org/uniprot/Q8IYN3|||http://purl.uniprot.org/uniprot/Q92619                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||F-BAR|||In allele HA-1H; induction of CTL recognition for epitope HA-1.|||In isoform 2.|||Minor histocompatibility antigen HA-1|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 45|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330312|||http://purl.uniprot.org/annotation/PRO_0000330313|||http://purl.uniprot.org/annotation/VAR_042693|||http://purl.uniprot.org/annotation/VAR_042694|||http://purl.uniprot.org/annotation/VAR_042695|||http://purl.uniprot.org/annotation/VAR_042696|||http://purl.uniprot.org/annotation/VAR_042697|||http://purl.uniprot.org/annotation/VSP_044707
http://togogenome.org/gene/9606:KCNE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IAE6|||http://purl.uniprot.org/uniprot/Q9Y6H6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases current 4-fold in KCNH2/KCNE3 channel.|||Disordered|||Found in some patients with periodic paralysis; unknown pathological significance; alters voltage dependence, lowers current and diminishes open probability in KCNC4/KCNE3 channel; lowers current in KCNQ1/KCNE3 channel.|||Helical|||In BRGDA6; also in a patient suffering from drug-induced torsades de pointes; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144289|||http://purl.uniprot.org/annotation/VAR_015064|||http://purl.uniprot.org/annotation/VAR_058635|||http://purl.uniprot.org/annotation/VAR_058636|||http://purl.uniprot.org/annotation/VAR_058637
http://togogenome.org/gene/9606:FGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09769|||http://purl.uniprot.org/uniprot/P78453                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Strongly increased catalytic activity. Functions as oncogene.|||Tyrosine-protein kinase Fgr                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088091|||http://purl.uniprot.org/annotation/VAR_041700|||http://purl.uniprot.org/annotation/VAR_041701
http://togogenome.org/gene/9606:EVC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UK5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In EVC.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Limbin|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084363|||http://purl.uniprot.org/annotation/VAR_017209|||http://purl.uniprot.org/annotation/VAR_017210|||http://purl.uniprot.org/annotation/VAR_017211|||http://purl.uniprot.org/annotation/VAR_035933|||http://purl.uniprot.org/annotation/VAR_035934|||http://purl.uniprot.org/annotation/VAR_051089|||http://purl.uniprot.org/annotation/VSP_008848|||http://purl.uniprot.org/annotation/VSP_008849
http://togogenome.org/gene/9606:ZSCAN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5P9VN71|||http://purl.uniprot.org/uniprot/I3L1J3|||http://purl.uniprot.org/uniprot/Q96SZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||N5-methylglutamine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047452|||http://purl.uniprot.org/annotation/VSP_039221|||http://purl.uniprot.org/annotation/VSP_054601|||http://purl.uniprot.org/annotation/VSP_054602
http://togogenome.org/gene/9606:TRIM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C037                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ligase activity.|||B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM4|||In isoform Beta and isoform Gamma.|||In isoform Gamma.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056200|||http://purl.uniprot.org/annotation/VAR_046715|||http://purl.uniprot.org/annotation/VAR_046716|||http://purl.uniprot.org/annotation/VSP_010197|||http://purl.uniprot.org/annotation/VSP_010198|||http://purl.uniprot.org/annotation/VSP_010199
http://togogenome.org/gene/9606:SERPINI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDY9|||http://purl.uniprot.org/uniprot/O75830                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Reactive bond|||Serpin|||Serpin I2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032525|||http://purl.uniprot.org/annotation/PRO_5002803508|||http://purl.uniprot.org/annotation/VAR_024357|||http://purl.uniprot.org/annotation/VAR_051957
http://togogenome.org/gene/9606:PDE3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2E5|||http://purl.uniprot.org/uniprot/Q13370                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Helical|||In isoform 2.|||Interaction with PIK3R6|||Interaction with RAPGEF3|||Loss of interaction with PIK3R6.|||Loss of interaction with RAPGEF3.|||PDEase|||Phosphoserine|||Phosphoserine; by PKB/AKT1 or PKB/AKT2|||Polar residues|||Proton donor|||cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198802|||http://purl.uniprot.org/annotation/VAR_031462|||http://purl.uniprot.org/annotation/VSP_054138
http://togogenome.org/gene/9606:ZNF385A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PM9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 2.|||In isoform 2 and isoform 3.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Necessary for binding to ITPR1, CEBPA and p53/TP53 mRNAs|||Phosphoserine|||Phosphothreonine|||Zinc finger protein 385A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047554|||http://purl.uniprot.org/annotation/VSP_047448|||http://purl.uniprot.org/annotation/VSP_047449
http://togogenome.org/gene/9606:MAGEB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||MAGE|||Melanoma-associated antigen B6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156717
http://togogenome.org/gene/9606:DPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZG8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  2-(3-amino-3-carboxypropyl)histidine synthase subunit 1|||Disordered|||In DEDSSH1; impairs diphthamide modification of elongation factor 2.|||In DEDSSH1; impairs diphthamide modification of elongation factor 2..|||In DEDSSH1; normal diphthamide modification of elongation factor 2.|||In breast and ovarian cancer.|||In breast and ovarian cancer; requires 2 nucleotide substitutions.|||In isoform 1 and isoform 5.|||In isoform 2.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307882|||http://purl.uniprot.org/annotation/VAR_036702|||http://purl.uniprot.org/annotation/VAR_036703|||http://purl.uniprot.org/annotation/VAR_036704|||http://purl.uniprot.org/annotation/VAR_036705|||http://purl.uniprot.org/annotation/VAR_055706|||http://purl.uniprot.org/annotation/VAR_059255|||http://purl.uniprot.org/annotation/VAR_076413|||http://purl.uniprot.org/annotation/VAR_086296|||http://purl.uniprot.org/annotation/VAR_086297|||http://purl.uniprot.org/annotation/VAR_086298|||http://purl.uniprot.org/annotation/VAR_087452|||http://purl.uniprot.org/annotation/VSP_061760|||http://purl.uniprot.org/annotation/VSP_061761|||http://purl.uniprot.org/annotation/VSP_061762|||http://purl.uniprot.org/annotation/VSP_061763
http://togogenome.org/gene/9606:BTNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJV4|||http://purl.uniprot.org/uniprot/F8WBA1|||http://purl.uniprot.org/uniprot/Q9UIR0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Butyrophilin-like protein 2|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||Ig-like V-type 3|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014537|||http://purl.uniprot.org/annotation/VAR_021171|||http://purl.uniprot.org/annotation/VAR_029128|||http://purl.uniprot.org/annotation/VAR_033602|||http://purl.uniprot.org/annotation/VAR_033603|||http://purl.uniprot.org/annotation/VAR_033604|||http://purl.uniprot.org/annotation/VAR_033605|||http://purl.uniprot.org/annotation/VAR_033606|||http://purl.uniprot.org/annotation/VAR_033607|||http://purl.uniprot.org/annotation/VAR_049837|||http://purl.uniprot.org/annotation/VAR_049838|||http://purl.uniprot.org/annotation/VAR_061307|||http://purl.uniprot.org/annotation/VAR_061308|||http://purl.uniprot.org/annotation/VSP_027184|||http://purl.uniprot.org/annotation/VSP_027185|||http://purl.uniprot.org/annotation/VSP_027186|||http://purl.uniprot.org/annotation/VSP_027187|||http://purl.uniprot.org/annotation/VSP_027188|||http://purl.uniprot.org/annotation/VSP_027189|||http://purl.uniprot.org/annotation/VSP_027190|||http://purl.uniprot.org/annotation/VSP_027191
http://togogenome.org/gene/9606:N4BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75113                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Abolished ability to degrade HIV-1 mRNAs.|||Abolished ability to interact with ubiquitin.|||Abolished cleavage by MALT1.|||Cleavage|||Cleavage; by CASP8|||Cleavage; by MALT1|||CoCUN|||Disordered|||KH-like|||NEDD4-binding protein 1|||Phosphoserine|||Phosphothreonine|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096680
http://togogenome.org/gene/9606:GDF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95390                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by BMP1|||Cleavage; by FURIN|||Growth/differentiation factor 11|||In VHO; loss of proteolytic cleavage of N-terminal propeptide; markedly reduced function in the activation of SMAD protein signal transduction.|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033986|||http://purl.uniprot.org/annotation/PRO_0000033987|||http://purl.uniprot.org/annotation/VAR_085163
http://togogenome.org/gene/9606:COG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS45|||http://purl.uniprot.org/uniprot/J3KNI1|||http://purl.uniprot.org/uniprot/Q8N8L9|||http://purl.uniprot.org/uniprot/Q9H9E3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 4|||D domain|||Disordered|||E domain; essential for proper cell surface glycosylation|||In CDG2J; severe defects in glycosylation.|||In SWILS; delayed anterograde vesicular trafficking from the ER to the Golgi and accelerated retrograde vesicular recycling from the Golgi to the ER, leading to a decrease in Golgi volume, as well as morphologic abnormalities with collapse of the Golgi stacks in affected fibroblasts; altered decorin/DCNGolgi-dependent glycosylation; no effect on protein expression.|||In isoform 2.|||In isoform 3.|||Interaction with SCFD1|||Interaction with STX5|||N-acetylalanine|||Phosphoserine|||Removed|||Severe defects in glycosylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213504|||http://purl.uniprot.org/annotation/VAR_058009|||http://purl.uniprot.org/annotation/VAR_063767|||http://purl.uniprot.org/annotation/VAR_081564|||http://purl.uniprot.org/annotation/VSP_001127|||http://purl.uniprot.org/annotation/VSP_001128|||http://purl.uniprot.org/annotation/VSP_037551
http://togogenome.org/gene/9606:ARF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84077                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor 1|||Important for the stable binding to the membranes|||In PVNH8.|||In PVNH8; decreased interaction with GGA3.|||In PVNH8; unknown pathological significance.|||Inhibits GTP hydrolysis. Coatomer proteins recruitment to the Golgi membrane and formation of coated vesicles are normal. However, Golgi transport is severely reduced due to impaired vesicle uncoating.|||N-acetylglycine; alternate|||N-myristoyl glycine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207378|||http://purl.uniprot.org/annotation/VAR_081272|||http://purl.uniprot.org/annotation/VAR_081273|||http://purl.uniprot.org/annotation/VAR_081274
http://togogenome.org/gene/9606:MVD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53602                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  15-fold inflation in KM for mevalonate diphosphate.|||Diphosphomevalonate decarboxylase|||In POROK7.|||In POROK7; 1000-fold diminution in diphosphomevalonate decarboxylase activity.|||In POROK7; unknown pathological significance.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087012|||http://purl.uniprot.org/annotation/VAR_051605|||http://purl.uniprot.org/annotation/VAR_075052|||http://purl.uniprot.org/annotation/VAR_075053|||http://purl.uniprot.org/annotation/VAR_075054|||http://purl.uniprot.org/annotation/VAR_075055|||http://purl.uniprot.org/annotation/VAR_075056|||http://purl.uniprot.org/annotation/VAR_075057|||http://purl.uniprot.org/annotation/VAR_075058|||http://purl.uniprot.org/annotation/VAR_075059|||http://purl.uniprot.org/annotation/VAR_075060|||http://purl.uniprot.org/annotation/VAR_075061
http://togogenome.org/gene/9606:TMEM276                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTL5|||http://purl.uniprot.org/uniprot/P0DTL6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 1.|||In isoform 4 and isoform 2.|||In isoform 4.|||RING-type; degenerate|||TRAF-type|||Transmembrane protein 276|||Zinc finger TRAF-type-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328852|||http://purl.uniprot.org/annotation/PRO_0000456471|||http://purl.uniprot.org/annotation/VSP_061632|||http://purl.uniprot.org/annotation/VSP_061633|||http://purl.uniprot.org/annotation/VSP_061634|||http://purl.uniprot.org/annotation/VSP_061635
http://togogenome.org/gene/9606:WDR24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S15                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Zinc Finger                                                                                  ^@                                                                                  Abolished interaction with WDR59 and assembly of the GATOR2 complex; when associated with E-451.|||Abolished interaction with WDR59 and assembly of the GATOR2 complex; when associated with E-632-633-E.|||Abolished phosphorylation by AMPK.|||C4-type|||GATOR2 complex protein WDR24|||Impaired amino-acid-mediated mTORC1 activation.|||Mimics phosphorylation, leading to inhibit mTORC1 activation.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||RING-type; atypical|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051375
http://togogenome.org/gene/9606:FRMD4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNA2|||http://purl.uniprot.org/uniprot/Q6PEW6|||http://purl.uniprot.org/uniprot/Q9Y2L6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FERM|||FERM domain-containing protein 4B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Necessary for adherens junction and tight junction localization|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219446|||http://purl.uniprot.org/annotation/VSP_040895
http://togogenome.org/gene/9606:ZMYM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GXA6|||http://purl.uniprot.org/uniprot/B4DSJ9|||http://purl.uniprot.org/uniprot/Q5SVZ6|||http://purl.uniprot.org/uniprot/Q9H5R2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HAT C-terminal dimerisation|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||Polar residues|||TRASH|||TTF-type|||Zinc finger MYM-type protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191377|||http://purl.uniprot.org/annotation/VAR_034589|||http://purl.uniprot.org/annotation/VAR_053767|||http://purl.uniprot.org/annotation/VAR_053768
http://togogenome.org/gene/9606:SLC17A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Dileucine internalization motif|||Disordered|||Helical|||In ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity.|||In ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity.|||In ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity.|||In ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity.|||In SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity.|||In SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity.|||In isoform 2.|||Localizes in vesicular structures mainly concentrated in the perinuclear region.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sialin|||Targeted to plasma membrane.|||Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220947|||http://purl.uniprot.org/annotation/VAR_018684|||http://purl.uniprot.org/annotation/VAR_018685|||http://purl.uniprot.org/annotation/VAR_018686|||http://purl.uniprot.org/annotation/VAR_018687|||http://purl.uniprot.org/annotation/VAR_018688|||http://purl.uniprot.org/annotation/VAR_018689|||http://purl.uniprot.org/annotation/VAR_034746|||http://purl.uniprot.org/annotation/VAR_087626|||http://purl.uniprot.org/annotation/VSP_010482|||http://purl.uniprot.org/annotation/VSP_010483
http://togogenome.org/gene/9606:CDK19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUB1|||http://purl.uniprot.org/uniprot/I6W807|||http://purl.uniprot.org/uniprot/Q9BWU1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 19|||Disordered|||In DEE87.|||In DEE87; decreased protein kinase activity.|||In DEE87; fails to rescue neurologic phenotypes in a Drosophila model system.|||In DEE87; fails to rescue neurologic phenotypes in a Drosophila model system; increased protein kinase activity.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085713|||http://purl.uniprot.org/annotation/VAR_084392|||http://purl.uniprot.org/annotation/VAR_084393|||http://purl.uniprot.org/annotation/VAR_084394|||http://purl.uniprot.org/annotation/VAR_084395|||http://purl.uniprot.org/annotation/VAR_084396|||http://purl.uniprot.org/annotation/VAR_084397|||http://purl.uniprot.org/annotation/VAR_084398|||http://purl.uniprot.org/annotation/VAR_084399|||http://purl.uniprot.org/annotation/VSP_015857
http://togogenome.org/gene/9606:VPS26B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0F5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Phosphoserine|||Vacuolar protein sorting-associated protein 26B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247089
http://togogenome.org/gene/9606:CT47A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:HBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D1MGQ2|||http://purl.uniprot.org/uniprot/P69905                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by N.americanus apr-2|||Causes alpha-thalassemia.|||Globin family profile|||Hemoglobin subunit alpha|||Hemopressin|||In Adana; unstable; causes alpha-thalassemia.|||In Aichi; slightly unstable.|||In Al-Ain Abu Dhabi.|||In Anantharaj.|||In Ann Arbor; unstable.|||In Atago; O(2) affinity up.|||In Attleboro; O(2) affinity up.|||In Auckland; unstable.|||In Aztec.|||In Bari.|||In Bassett; markedly reduced oxygen affinity.|||In Beijing.|||In Bibba; unstable; causes alpha-thalassemia.|||In Boghe.|||In Bourmedes.|||In Broomfield.|||In Campinas.|||In Catonsville.|||In Cemenelum; O(2) affinity up.|||In Chad.|||In Chapel Hill.|||In Charolles.|||In Chiapas.|||In Chicago.|||In ChongQing; O(2) affinity up.|||In Clinic; unstable; causes alpha-thalassemia.|||In Contaldo; unstable.|||In Cordele; unstable.|||In Dallas; O(2) affinity up.|||In Daneskgah-Teheran.|||In Davenport.|||In Denmark Hill; O(2) affinity up.|||In Duan.|||In Dunn; O(2) affinity up.|||In Etobicoke; O(2) affinity up.|||In Evans; unstable.|||In Evanston; O(2) affinity up.|||In Ferndown; O(2) affinity up.|||In Fontainebleau.|||In Fort Worth.|||In Fort de France; O(2) affinity up.|||In Fukutomi; O(2) affinity up.|||In G-Pest.|||In G-Philadelphia.|||In Garden State.|||In Godavari; O(2) affinity up.|||In Grady.|||In Guizhou.|||In HBH; hemoglobin Aghia Sophia.|||In Hanamaki; O(2) affinity up.|||In Handa; O(2) affinity up.|||In Handsworth.|||In Harbin; slightly unstable.|||In Hasharon/Sinai; unstable.|||In Hekinan.|||In Hikoshima/Shimonoseki.|||In Hirosaki; unstable.|||In Hobart.|||In Hopkins-II; unstable.|||In Inkster; O(2) affinity up.|||In Iwata; unstable.|||In J-Abidjan.|||In J-Anatolia.|||In J-Buda.|||In J-Cape Town; O(2) affinity up.|||In J-Habana.|||In J-Kurosh.|||In J-Medellin.|||In J-Meerut/J-Birmingham.|||In J-Nyanza.|||In J-Paris 1/J-Aljezur.|||In J-Rovigo; unstable.|||In J-Tashikuergan.|||In J-Tongariki.|||In J-Toronto.|||In Jackson.|||In Kanagawa; O(2) affinity up.|||In Karachi.|||In Kawachi; O(2) affinity up.|||In Kokura; also in Umi/Michigan; unstable.|||In Kurdistan.|||In Kurosaki.|||In L-Persian Gulf.|||In Le Lamentin.|||In Legnano; O(2) affinity up.|||In Lille.|||In Loire; O(2) affinity up.|||In Luxembourg; unstable.|||In M-Boston/M-Osaka; O(2) affinity down.|||In Manitoba; slightly unstable.|||In Melusine.|||In Milledgeville; O(2) affinity up.|||In Miyano; O(2) affinity up.|||In Moabit; unstable.|||In Montefiore; O(2) affinity up.|||In Montgomery.|||In Nigeria.|||In Noko.|||In Nouakchott.|||In Nunobiki; O(2) affinity up.|||In O-Padova.|||In Ottawa/Siam.|||In Owari.|||In Ozieri.|||In Pavie.|||In Persepolis.|||In Petah Tikva; unstable; causes alpha-thalassemia.|||In Phnom Penh.|||In Plasencia; family with moderate microcytosis and hypochromia.|||In Pontoise; unstable.|||In Port Huron.|||In Port Phillip; unstable.|||In Prato; unstable.|||In Q-Iran.|||In Queens/Ogi.|||In Questembert; highly unstable; causes alpha-thalassemia.|||In Quong Sze; causes alpha-thalassemia.|||In Ravenscourt Park; causes alpha-thalassemia.|||In Reims; slightly unstable.|||In Rouen/Ethiopia; O(2) affinity up.|||In Russ.|||In Savaria.|||In Sawara; O(2) affinity up.|||In Setif; unstable.|||In Shenyang; unstable.|||In Singapore.|||In Spanish town.|||In Stanleyville-2.|||In Suan-Dok; unstable; causes alpha-thalassemia.|||In Sun Prairie; unstable.|||In Suresnes; O(2) affinity up.|||In Swan River.|||In Thailand.|||In Thionville; O(2) affinity down.|||In Tokoname; O(2) affinity up.|||In Tottori; unstable.|||In Toyama.|||In Tunis-Bizerte; unstable; causes alpha-thalassemia.|||In Turriff.|||In Twin Peaks.|||In Ube-4.|||In Val de Marne; O(2) affinity up.|||In West One.|||In Westmead.|||In Woodville; O(2) affinity up.|||In Yuda; O(2) affinity down.|||In Zaire.|||In Zambia.|||N-linked (Glc) (glycation) lysine|||N-linked (Glc) (glycation) lysine; alternate|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Not glycated|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||distal binding residue|||proximal binding residue ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052653|||http://purl.uniprot.org/annotation/PRO_0000455882|||http://purl.uniprot.org/annotation/VAR_002719|||http://purl.uniprot.org/annotation/VAR_002720|||http://purl.uniprot.org/annotation/VAR_002721|||http://purl.uniprot.org/annotation/VAR_002722|||http://purl.uniprot.org/annotation/VAR_002723|||http://purl.uniprot.org/annotation/VAR_002724|||http://purl.uniprot.org/annotation/VAR_002725|||http://purl.uniprot.org/annotation/VAR_002726|||http://purl.uniprot.org/annotation/VAR_002727|||http://purl.uniprot.org/annotation/VAR_002728|||http://purl.uniprot.org/annotation/VAR_002729|||http://purl.uniprot.org/annotation/VAR_002730|||http://purl.uniprot.org/annotation/VAR_002731|||http://purl.uniprot.org/annotation/VAR_002732|||http://purl.uniprot.org/annotation/VAR_002733|||http://purl.uniprot.org/annotation/VAR_002734|||http://purl.uniprot.org/annotation/VAR_002735|||http://purl.uniprot.org/annotation/VAR_002736|||http://purl.uniprot.org/annotation/VAR_002737|||http://purl.uniprot.org/annotation/VAR_002738|||http://purl.uniprot.org/annotation/VAR_002739|||http://purl.uniprot.org/annotation/VAR_002740|||http://purl.uniprot.org/annotation/VAR_002741|||http://purl.uniprot.org/annotation/VAR_002742|||http://purl.uniprot.org/annotation/VAR_002743|||http://purl.uniprot.org/annotation/VAR_002744|||http://purl.uniprot.org/annotation/VAR_002745|||http://purl.uniprot.org/annotation/VAR_002746|||http://purl.uniprot.org/annotation/VAR_002747|||http://purl.uniprot.org/annotation/VAR_002748|||http://purl.uniprot.org/annotation/VAR_002749|||http://purl.uniprot.org/annotation/VAR_002750|||http://purl.uniprot.org/annotation/VAR_002751|||http://purl.uniprot.org/annotation/VAR_002752|||http://purl.uniprot.org/annotation/VAR_002753|||http://purl.uniprot.org/annotation/VAR_002754|||http://purl.uniprot.org/annotation/VAR_002755|||http://purl.uniprot.org/annotation/VAR_002756|||http://purl.uniprot.org/annotation/VAR_002757|||http://purl.uniprot.org/annotation/VAR_002758|||http://purl.uniprot.org/annotation/VAR_002759|||http://purl.uniprot.org/annotation/VAR_002760|||http://purl.uniprot.org/annotation/VAR_002761|||http://purl.uniprot.org/annotation/VAR_002762|||http://purl.uniprot.org/annotation/VAR_002763|||http://purl.uniprot.org/annotation/VAR_002764|||http://purl.uniprot.org/annotation/VAR_002765|||http://purl.uniprot.org/annotation/VAR_002766|||http://purl.uniprot.org/annotation/VAR_002767|||http://purl.uniprot.org/annotation/VAR_002768|||http://purl.uniprot.org/annotation/VAR_002769|||http://purl.uniprot.org/annotation/VAR_002770|||http://purl.uniprot.org/annotation/VAR_002771|||http://purl.uniprot.org/annotation/VAR_002772|||http://purl.uniprot.org/annotation/VAR_002773|||http://purl.uniprot.org/annotation/VAR_002774|||http://purl.uniprot.org/annotation/VAR_002775|||http://purl.uniprot.org/annotation/VAR_002776|||http://purl.uniprot.org/annotation/VAR_002777|||http://purl.uniprot.org/annotation/VAR_002778|||http://purl.uniprot.org/annotation/VAR_002779|||http://purl.uniprot.org/annotation/VAR_002780|||http://purl.uniprot.org/annotation/VAR_002781|||http://purl.uniprot.org/annotation/VAR_002782|||http://purl.uniprot.org/annotation/VAR_002783|||http://purl.uniprot.org/annotation/VAR_002784|||http://purl.uniprot.org/annotation/VAR_002785|||http://purl.uniprot.org/annotation/VAR_002786|||http://purl.uniprot.org/annotation/VAR_002787|||http://purl.uniprot.org/annotation/VAR_002788|||http://purl.uniprot.org/annotation/VAR_002789|||http://purl.uniprot.org/annotation/VAR_002790|||http://purl.uniprot.org/annotation/VAR_002791|||http://purl.uniprot.org/annotation/VAR_002792|||http://purl.uniprot.org/annotation/VAR_002793|||http://purl.uniprot.org/annotation/VAR_002794|||http://purl.uniprot.org/annotation/VAR_002795|||http://purl.uniprot.org/annotation/VAR_002796|||http://purl.uniprot.org/annotation/VAR_002797|||http://purl.uniprot.org/annotation/VAR_002798|||http://purl.uniprot.org/annotation/VAR_002799|||http://purl.uniprot.org/annotation/VAR_002800|||http://purl.uniprot.org/annotation/VAR_002801|||http://purl.uniprot.org/annotation/VAR_002802|||http://purl.uniprot.org/annotation/VAR_002803|||http://purl.uniprot.org/annotation/VAR_002804|||http://purl.uniprot.org/annotation/VAR_002805|||http://purl.uniprot.org/annotation/VAR_002806|||http://purl.uniprot.org/annotation/VAR_002807|||http://purl.uniprot.org/annotation/VAR_002808|||http://purl.uniprot.org/annotation/VAR_002809|||http://purl.uniprot.org/annotation/VAR_002810|||http://purl.uniprot.org/annotation/VAR_002811|||http://purl.uniprot.org/annotation/VAR_002812|||http://purl.uniprot.org/annotation/VAR_002813|||http://purl.uniprot.org/annotation/VAR_002814|||http://purl.uniprot.org/annotation/VAR_002815|||http://purl.uniprot.org/annotation/VAR_002816|||http://purl.uniprot.org/annotation/VAR_002817|||http://purl.uniprot.org/annotation/VAR_002818|||http://purl.uniprot.org/annotation/VAR_002819|||http://purl.uniprot.org/annotation/VAR_002820|||http://purl.uniprot.org/annotation/VAR_002821|||http://purl.uniprot.org/annotation/VAR_002822|||http://purl.uniprot.org/annotation/VAR_002823|||http://purl.uniprot.org/annotation/VAR_002824|||http://purl.uniprot.org/annotation/VAR_002825|||http://purl.uniprot.org/annotation/VAR_002826|||http://purl.uniprot.org/annotation/VAR_002827|||http://purl.uniprot.org/annotation/VAR_002828|||http://purl.uniprot.org/annotation/VAR_002829|||http://purl.uniprot.org/annotation/VAR_002830|||http://purl.uniprot.org/annotation/VAR_002831|||http://purl.uniprot.org/annotation/VAR_002832|||http://purl.uniprot.org/annotation/VAR_002833|||http://purl.uniprot.org/annotation/VAR_002834|||http://purl.uniprot.org/annotation/VAR_002835|||http://purl.uniprot.org/annotation/VAR_002836|||http://purl.uniprot.org/annotation/VAR_002837|||http://purl.uniprot.org/annotation/VAR_002838|||http://purl.uniprot.org/annotation/VAR_002839|||http://purl.uniprot.org/annotation/VAR_002840|||http://purl.uniprot.org/annotation/VAR_002841|||http://purl.uniprot.org/annotation/VAR_002842|||http://purl.uniprot.org/annotation/VAR_002843|||http://purl.uniprot.org/annotation/VAR_002844|||http://purl.uniprot.org/annotation/VAR_002845|||http://purl.uniprot.org/annotation/VAR_002846|||http://purl.uniprot.org/annotation/VAR_002847|||http://purl.uniprot.org/annotation/VAR_002848|||http://purl.uniprot.org/annotation/VAR_002849|||http://purl.uniprot.org/annotation/VAR_002850|||http://purl.uniprot.org/annotation/VAR_002851|||http://purl.uniprot.org/annotation/VAR_002852|||http://purl.uniprot.org/annotation/VAR_002853|||http://purl.uniprot.org/annotation/VAR_002854|||http://purl.uniprot.org/annotation/VAR_002855|||http://purl.uniprot.org/annotation/VAR_012662|||http://purl.uniprot.org/annotation/VAR_020775|||http://purl.uniprot.org/annotation/VAR_025002|||http://purl.uniprot.org/annotation/VAR_025387|||http://purl.uniprot.org/annotation/VAR_025388|||http://purl.uniprot.org/annotation/VAR_025389|||http://purl.uniprot.org/annotation/VAR_025390|||http://purl.uniprot.org/annotation/VAR_025391|||http://purl.uniprot.org/annotation/VAR_025392|||http://purl.uniprot.org/annotation/VAR_035242|||http://purl.uniprot.org/annotation/VAR_038149|||http://purl.uniprot.org/annotation/VAR_038150|||http://purl.uniprot.org/annotation/VAR_049272|||http://purl.uniprot.org/annotation/VAR_066401
http://togogenome.org/gene/9606:THUMPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP37|||http://purl.uniprot.org/uniprot/Q969Z2|||http://purl.uniprot.org/uniprot/Q9BTF0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||THUMP|||THUMP domain-containing protein 2|||UPF0020                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072532|||http://purl.uniprot.org/annotation/VSP_041645|||http://purl.uniprot.org/annotation/VSP_041646
http://togogenome.org/gene/9606:UPK1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75841                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Uroplakin-1b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219289|||http://purl.uniprot.org/annotation/VAR_028780
http://togogenome.org/gene/9606:DHRS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75911                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Proton acceptor|||Short-chain dehydrogenase/reductase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054644|||http://purl.uniprot.org/annotation/VAR_067443|||http://purl.uniprot.org/annotation/VSP_013256|||http://purl.uniprot.org/annotation/VSP_013257
http://togogenome.org/gene/9606:NPAS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUM7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic motif; degenerate|||Decreased transcription factor activity due to impaired interaction with ARNT2.|||Decreased transcription factor activity.|||Disordered|||Does not affect the transcription factor activity.|||Helix-loop-helix motif|||In isoform 2.|||Likely benign variant; does not affect the transcription factor activity.|||Neuronal PAS domain-containing protein 4|||PAC|||PAS 1|||PAS 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248222|||http://purl.uniprot.org/annotation/VAR_076845|||http://purl.uniprot.org/annotation/VAR_076846|||http://purl.uniprot.org/annotation/VAR_076847|||http://purl.uniprot.org/annotation/VAR_076848|||http://purl.uniprot.org/annotation/VAR_076849|||http://purl.uniprot.org/annotation/VAR_076850|||http://purl.uniprot.org/annotation/VAR_076851|||http://purl.uniprot.org/annotation/VAR_076852|||http://purl.uniprot.org/annotation/VAR_076853|||http://purl.uniprot.org/annotation/VAR_076854|||http://purl.uniprot.org/annotation/VAR_076855|||http://purl.uniprot.org/annotation/VAR_076856|||http://purl.uniprot.org/annotation/VAR_076857|||http://purl.uniprot.org/annotation/VAR_076858|||http://purl.uniprot.org/annotation/VSP_056596|||http://purl.uniprot.org/annotation/VSP_056597
http://togogenome.org/gene/9606:ITGAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11215                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 2.|||Influences susceptibility to SLE.|||Integrin alpha-M|||N-linked (GlcNAc...) asparagine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016289|||http://purl.uniprot.org/annotation/VAR_043870|||http://purl.uniprot.org/annotation/VAR_043871|||http://purl.uniprot.org/annotation/VAR_043872|||http://purl.uniprot.org/annotation/VAR_043873|||http://purl.uniprot.org/annotation/VSP_047365
http://togogenome.org/gene/9606:NBPF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRP3|||http://purl.uniprot.org/uniprot/Q8N660                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Neuroblastoma breakpoint family member 15|||Olduvai|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5|||Olduvai 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288049|||http://purl.uniprot.org/annotation/VAR_032383
http://togogenome.org/gene/9606:SSR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J365|||http://purl.uniprot.org/uniprot/Q9UNL2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Translocon-associated protein subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191690|||http://purl.uniprot.org/annotation/VSP_056195
http://togogenome.org/gene/9606:PTGER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34995                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Prostaglandin E2 receptor EP1 subtype                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070050|||http://purl.uniprot.org/annotation/VAR_017190|||http://purl.uniprot.org/annotation/VAR_029216|||http://purl.uniprot.org/annotation/VAR_029217
http://togogenome.org/gene/9606:ALDH6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02252                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In MMSDHD; unknown pathological significance.|||In isoform 2.|||Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007189|||http://purl.uniprot.org/annotation/VAR_010244|||http://purl.uniprot.org/annotation/VAR_088433|||http://purl.uniprot.org/annotation/VAR_088434|||http://purl.uniprot.org/annotation/VSP_055067
http://togogenome.org/gene/9606:ERBB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21860                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In FERLK; risk factor for erythroleukemia; results in increased ERBB-mediated signaling; results in a block of erythroid differentiation and increased cell proliferation.|||In VSCN1; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane.|||In VSCN1; unknown pathological significance; some decrease in ERBB2 phosphorylation upon NG1 treatment, compared to wild-type; does not affect the subcellular localization at the cell membrane.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Receptor tyrosine-protein kinase erbB-3|||Strongly reduced autophosphorylation.|||Strongly reduced tyrosine phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016672|||http://purl.uniprot.org/annotation/VAR_042101|||http://purl.uniprot.org/annotation/VAR_042102|||http://purl.uniprot.org/annotation/VAR_042103|||http://purl.uniprot.org/annotation/VAR_042104|||http://purl.uniprot.org/annotation/VAR_042105|||http://purl.uniprot.org/annotation/VAR_042106|||http://purl.uniprot.org/annotation/VAR_042107|||http://purl.uniprot.org/annotation/VAR_042108|||http://purl.uniprot.org/annotation/VAR_042109|||http://purl.uniprot.org/annotation/VAR_042110|||http://purl.uniprot.org/annotation/VAR_042111|||http://purl.uniprot.org/annotation/VAR_042112|||http://purl.uniprot.org/annotation/VAR_049710|||http://purl.uniprot.org/annotation/VAR_049711|||http://purl.uniprot.org/annotation/VAR_081641|||http://purl.uniprot.org/annotation/VAR_086108|||http://purl.uniprot.org/annotation/VAR_086109|||http://purl.uniprot.org/annotation/VAR_086110|||http://purl.uniprot.org/annotation/VAR_086111|||http://purl.uniprot.org/annotation/VSP_002893|||http://purl.uniprot.org/annotation/VSP_002894|||http://purl.uniprot.org/annotation/VSP_041661|||http://purl.uniprot.org/annotation/VSP_041662|||http://purl.uniprot.org/annotation/VSP_041663|||http://purl.uniprot.org/annotation/VSP_041664
http://togogenome.org/gene/9606:L1TD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7N2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||LINE-1 type transposase domain-containing protein 1|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307217|||http://purl.uniprot.org/annotation/VAR_035377|||http://purl.uniprot.org/annotation/VAR_035378|||http://purl.uniprot.org/annotation/VAR_035379|||http://purl.uniprot.org/annotation/VAR_035380|||http://purl.uniprot.org/annotation/VAR_035381|||http://purl.uniprot.org/annotation/VAR_035382|||http://purl.uniprot.org/annotation/VAR_051094
http://togogenome.org/gene/9606:FOXC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99958                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein C2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In LPHDST.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091808|||http://purl.uniprot.org/annotation/VAR_018418|||http://purl.uniprot.org/annotation/VAR_060950
http://togogenome.org/gene/9606:CHMP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD42                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Charged multivesicular body protein 1a|||Disordered|||In isoform 2.|||MIT-interacting motif|||N-acetylmethionine|||No effect on interaction with IST1; when associated with L-194.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211448|||http://purl.uniprot.org/annotation/VSP_051716
http://togogenome.org/gene/9606:PDLIM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4N4|||http://purl.uniprot.org/uniprot/P50479                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LIM zinc-binding|||PDZ|||PDZ and LIM domain protein 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075873|||http://purl.uniprot.org/annotation/VAR_035205|||http://purl.uniprot.org/annotation/VAR_035206|||http://purl.uniprot.org/annotation/VAR_035207|||http://purl.uniprot.org/annotation/VAR_050167|||http://purl.uniprot.org/annotation/VSP_003124
http://togogenome.org/gene/9606:GABRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PBQ7|||http://purl.uniprot.org/uniprot/P47869                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with epilepsy; unknown pathological significance.|||Gamma-aminobutyric acid receptor subunit alpha-2|||Helical|||In DEE78; impaired GABA-gated chloride ion channel activity.|||In DEE78; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000433|||http://purl.uniprot.org/annotation/PRO_5022262638|||http://purl.uniprot.org/annotation/VAR_083186|||http://purl.uniprot.org/annotation/VAR_083187|||http://purl.uniprot.org/annotation/VAR_083188|||http://purl.uniprot.org/annotation/VAR_083189|||http://purl.uniprot.org/annotation/VAR_083190|||http://purl.uniprot.org/annotation/VAR_083191|||http://purl.uniprot.org/annotation/VAR_083192|||http://purl.uniprot.org/annotation/VSP_054277|||http://purl.uniprot.org/annotation/VSP_054278
http://togogenome.org/gene/9606:KRTAP13-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SY46                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 10 AA approximate repeats|||Keratin-associated protein 13-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185202
http://togogenome.org/gene/9606:CATIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7H3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Ciliogenesis-associated TTC17-interacting protein|||Disordered|||In SPGF54; reduces the protein stability. Increases the kinetics of actin polymerisation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309187|||http://purl.uniprot.org/annotation/VAR_085385
http://togogenome.org/gene/9606:OR51B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H340                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51B6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150748|||http://purl.uniprot.org/annotation/VAR_053312|||http://purl.uniprot.org/annotation/VAR_053313|||http://purl.uniprot.org/annotation/VAR_053314|||http://purl.uniprot.org/annotation/VAR_053315|||http://purl.uniprot.org/annotation/VAR_053316|||http://purl.uniprot.org/annotation/VAR_053317|||http://purl.uniprot.org/annotation/VAR_053318|||http://purl.uniprot.org/annotation/VAR_053319|||http://purl.uniprot.org/annotation/VAR_053320|||http://purl.uniprot.org/annotation/VAR_053321|||http://purl.uniprot.org/annotation/VAR_053322|||http://purl.uniprot.org/annotation/VAR_060035|||http://purl.uniprot.org/annotation/VAR_060036
http://togogenome.org/gene/9606:ORC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5N6                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolished DNA binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MGORS3.|||Origin recognition complex subunit 6|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127097|||http://purl.uniprot.org/annotation/VAR_029283|||http://purl.uniprot.org/annotation/VAR_029284|||http://purl.uniprot.org/annotation/VAR_065487
http://togogenome.org/gene/9606:PRIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49643                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA primase large subunit|||Decreases RNA primer di-nucleotide formation about 5-fold. Does not affect the ratio between the di-nucleotide and its extension products.|||Decreases primase affinity for POLA1 by 10-fold.|||Decreases primase affinity for POLA1 by 30-fold.|||Decreases primase affinity for POLA1 by 40-fold.|||Disordered|||In isoform 2.|||Interacts with PRIM1|||Interdomain linker|||Phosphothreonine|||RNA:DNA duplex-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046768|||http://purl.uniprot.org/annotation/VAR_051506|||http://purl.uniprot.org/annotation/VAR_059742|||http://purl.uniprot.org/annotation/VAR_059743|||http://purl.uniprot.org/annotation/VAR_059744|||http://purl.uniprot.org/annotation/VAR_059745|||http://purl.uniprot.org/annotation/VAR_059747|||http://purl.uniprot.org/annotation/VAR_059748|||http://purl.uniprot.org/annotation/VSP_015111|||http://purl.uniprot.org/annotation/VSP_015112
http://togogenome.org/gene/9606:TRAPPC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48553                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In NEDMISS; unable to rescue intra-Golgi vesicle-mediated transport defects in gene-null cells.|||In isoform 2.|||Phosphoserine|||Trafficking protein particle complex subunit 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193509|||http://purl.uniprot.org/annotation/VAR_009514|||http://purl.uniprot.org/annotation/VAR_009515|||http://purl.uniprot.org/annotation/VAR_009516|||http://purl.uniprot.org/annotation/VAR_084045|||http://purl.uniprot.org/annotation/VSP_056589|||http://purl.uniprot.org/annotation/VSP_056590
http://togogenome.org/gene/9606:CYP4F8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98187                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4F8|||Helical|||No effect on U-44069 and 9,11-diazo-prostadienoic acid (U-51605) hydroxylation; loss of 20:4n-6 or 22:5n-6 oxidation.|||No effect on U-44069 and U-51605 hydroxylation. 20:4n-6 hydroxylation shifted from C-18 to C-19.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051855|||http://purl.uniprot.org/annotation/VAR_038347|||http://purl.uniprot.org/annotation/VAR_038348
http://togogenome.org/gene/9606:USP38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB14                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Loss of binding to LSD1/KDM1A.|||Loss of deubiquitinating activity; when associated with A-454.|||Loss of deubiquitinating activity; when associated with A-857.|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080668|||http://purl.uniprot.org/annotation/VSP_054486
http://togogenome.org/gene/9606:ASRGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L266                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation by autocleavage. Abolishes enzyme activity.|||Found in a large family with early-onset recessive retinal degeneration; abolishes autocleavage resulting in loss of enzymatic activity; increased protein aggregation; changes protein localization that becomes perinuclear, does not change ligand affinity for L-aspartic acid beta-hydroxamate.|||In isoform 2.|||Isoaspartyl peptidase/L-asparaginase alpha chain|||Isoaspartyl peptidase/L-asparaginase beta chain|||N-acetylmethionine|||Nucleophile|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305204|||http://purl.uniprot.org/annotation/PRO_0000420556|||http://purl.uniprot.org/annotation/VAR_081118|||http://purl.uniprot.org/annotation/VSP_028287
http://togogenome.org/gene/9606:PIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13526                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Loss of binding to phosphorylated target proteins, including to phosphorylated RBBP8/CtIP; decrease in DNA repair of double-strand breaks by homologous recombination less efficient than that observed with wild-type protein. Abolishes interaction with IRAK3/IRAK-M. Abolishes IL33-mediated increase of IRAK3/IRAK-M protein levels.|||Loss of peptidyl-prolyl cis/trans isomerase activity, nuclear localization and cellular function.|||Loss of peptidyl-prolyl cis/trans isomerase activity. No effect on the interaction with IRAK3/IRAK-M. Abolishes IL33-mediated increase of IRAK3/IRAK-M protein levels.|||Loss of peptidyl-prolyl cis/trans isomerase activity; decrease in DNA repair of double-strand breaks by homologous recombination slightly less efficient than that observed with wild-type protein. No effect on RBBP8/CtIP.|||N6-acetyllysine|||Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1|||Phosphoserine|||Phosphoserine; by DAPK1|||Polar residues|||PpiC|||Reduced affinity for KIF20B.|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193435
http://togogenome.org/gene/9606:ZNF780B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6R6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22; degenerate|||C2H2-type 23; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 780B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263088
http://togogenome.org/gene/9606:MRPL20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYC9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein bL20m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248279|||http://purl.uniprot.org/annotation/VSP_056084
http://togogenome.org/gene/9606:MYH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In CMYP6.|||In isoform 2.|||In one patient with familial myopathy; unknown pathological significance.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-2|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123393|||http://purl.uniprot.org/annotation/VAR_032630|||http://purl.uniprot.org/annotation/VAR_032631|||http://purl.uniprot.org/annotation/VAR_032632|||http://purl.uniprot.org/annotation/VAR_032633|||http://purl.uniprot.org/annotation/VSP_056291
http://togogenome.org/gene/9606:HPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK9|||http://purl.uniprot.org/uniprot/B7Z1L4|||http://purl.uniprot.org/uniprot/P05981                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Interchain (between non-catalytic and catalytic chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Serine protease hepsin catalytic chain|||Serine protease hepsin non-catalytic chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027841|||http://purl.uniprot.org/annotation/PRO_0000027842
http://togogenome.org/gene/9606:VPS72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15906                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Almost abolishes interaction with H2AZ1 and H2BC11. Abolishes interaction with H2AZ1 and H2BC11 and exchange of H2A for H2AZ1 in nucleosomes; when associated with A-29--37-A.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly decreases interaction with H2AZ1 and H2BC11. Abolishes interaction with H2AZ1 and H2BC11 and exchange of H2A for H2AZ1 in nucleosomes; when associated with A-43--46-A.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Pro residues|||Vacuolar protein sorting-associated protein 72 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066283|||http://purl.uniprot.org/annotation/VAR_035803|||http://purl.uniprot.org/annotation/VSP_047566
http://togogenome.org/gene/9606:WASF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T8P4|||http://purl.uniprot.org/uniprot/Q9UPY6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding protein WASF3|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188996|||http://purl.uniprot.org/annotation/VAR_052953|||http://purl.uniprot.org/annotation/VSP_054517
http://togogenome.org/gene/9606:GCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0Z4|||http://purl.uniprot.org/uniprot/Q96CN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||GRIP|||GRIP and coiled-coil domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190072|||http://purl.uniprot.org/annotation/VAR_020157|||http://purl.uniprot.org/annotation/VAR_021902|||http://purl.uniprot.org/annotation/VAR_049259|||http://purl.uniprot.org/annotation/VAR_049260|||http://purl.uniprot.org/annotation/VAR_049261|||http://purl.uniprot.org/annotation/VAR_049262
http://togogenome.org/gene/9606:FASTKD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAST kinase domain-containing protein 2, mitochondrial|||In COXPD44.|||In COXPD44; decreased mitochondrial large ribosomal subunit assembly.|||In COXPD44; unknown pathological significance.|||In isoform 2.|||Mitochondrion|||Phosphoserine|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050783|||http://purl.uniprot.org/annotation/VAR_053889|||http://purl.uniprot.org/annotation/VAR_053890|||http://purl.uniprot.org/annotation/VAR_084340|||http://purl.uniprot.org/annotation/VAR_084341|||http://purl.uniprot.org/annotation/VAR_084342|||http://purl.uniprot.org/annotation/VAR_084343|||http://purl.uniprot.org/annotation/VSP_017186|||http://purl.uniprot.org/annotation/VSP_017187
http://togogenome.org/gene/9606:MAGEB16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A368                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen B16|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311928|||http://purl.uniprot.org/annotation/VAR_037350|||http://purl.uniprot.org/annotation/VAR_037351|||http://purl.uniprot.org/annotation/VAR_037352|||http://purl.uniprot.org/annotation/VAR_037353|||http://purl.uniprot.org/annotation/VAR_037354
http://togogenome.org/gene/9606:AFF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51816                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AF4/FMR2 family member 2|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215912|||http://purl.uniprot.org/annotation/VAR_028217|||http://purl.uniprot.org/annotation/VSP_000211|||http://purl.uniprot.org/annotation/VSP_000212|||http://purl.uniprot.org/annotation/VSP_000213|||http://purl.uniprot.org/annotation/VSP_000214|||http://purl.uniprot.org/annotation/VSP_000215|||http://purl.uniprot.org/annotation/VSP_000216|||http://purl.uniprot.org/annotation/VSP_043237|||http://purl.uniprot.org/annotation/VSP_043238
http://togogenome.org/gene/9606:CEP104                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60308                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centrosomal protein of 104 kDa|||Disordered|||HEAT 1|||HEAT 2|||In MRT77.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050763|||http://purl.uniprot.org/annotation/VAR_020042|||http://purl.uniprot.org/annotation/VAR_034036|||http://purl.uniprot.org/annotation/VAR_087591|||http://purl.uniprot.org/annotation/VSP_014364|||http://purl.uniprot.org/annotation/VSP_014365|||http://purl.uniprot.org/annotation/VSP_014366|||http://purl.uniprot.org/annotation/VSP_014367
http://togogenome.org/gene/9606:OARD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J5P1|||http://purl.uniprot.org/uniprot/C9JXC3|||http://purl.uniprot.org/uniprot/Q9Y530                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribose glycohydrolase OARD1|||Abolishes enzyme activity and ability to form a stable covalent adduct with the ADP-ribosylated substrate.|||Abolishes enzyme activity without affecting ability to form a stable covalent adduct with the ADP-ribosylated substrate.|||Abolishes enzyme activity.|||Macro|||N-acetylalanine|||No effect.|||Nucleophile|||Phosphoserine|||Probable disease-associated variant found in a family with severe neurodegeneration.|||Proton acceptor|||Reduced catalytic activity. No effect on affinity towards substrate.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089529|||http://purl.uniprot.org/annotation/VAR_081206
http://togogenome.org/gene/9606:KIAA1755                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JYT7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein KIAA1755                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317284|||http://purl.uniprot.org/annotation/VAR_038501|||http://purl.uniprot.org/annotation/VAR_038502|||http://purl.uniprot.org/annotation/VAR_038503|||http://purl.uniprot.org/annotation/VAR_038504|||http://purl.uniprot.org/annotation/VAR_038505
http://togogenome.org/gene/9606:SLC41A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GZ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Solute carrier family 41 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295592|||http://purl.uniprot.org/annotation/VAR_033296|||http://purl.uniprot.org/annotation/VAR_046667|||http://purl.uniprot.org/annotation/VSP_026934|||http://purl.uniprot.org/annotation/VSP_026935|||http://purl.uniprot.org/annotation/VSP_026936|||http://purl.uniprot.org/annotation/VSP_026937|||http://purl.uniprot.org/annotation/VSP_026938|||http://purl.uniprot.org/annotation/VSP_035505|||http://purl.uniprot.org/annotation/VSP_035506|||http://purl.uniprot.org/annotation/VSP_043676|||http://purl.uniprot.org/annotation/VSP_054059|||http://purl.uniprot.org/annotation/VSP_054060
http://togogenome.org/gene/9606:MRPS21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82921|||http://purl.uniprot.org/uniprot/Q99768                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Small ribosomal subunit protein bS21m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178413|||http://purl.uniprot.org/annotation/VAR_024610|||http://purl.uniprot.org/annotation/VAR_051825
http://togogenome.org/gene/9606:SYNGR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43761                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||MARVEL|||N-acetylmethionine|||Synaptogyrin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183996
http://togogenome.org/gene/9606:APOBEC3H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZI3|||http://purl.uniprot.org/uniprot/B7TQM3|||http://purl.uniprot.org/uniprot/B7TQM4|||http://purl.uniprot.org/uniprot/B7TQM9|||http://purl.uniprot.org/uniprot/Q6NTF7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||DNA dC->dU-editing enzyme APOBEC-3H|||Decreases protein stability.|||In allele A3H-Var; haplotype 2; allele presenting a higher expression and more effective in retrotransposons and HIV-1 restriction.|||In allele A3H-Var; haplotype 2; allele presenting a higher expression and which is more effective in retrotransposons and HIV-1 restriction; increases protein stability.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Proton donor|||Reduces the ability to inhibit the retrotransposition of LINE-1 elements.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291663|||http://purl.uniprot.org/annotation/VAR_032835|||http://purl.uniprot.org/annotation/VAR_032836|||http://purl.uniprot.org/annotation/VAR_032837|||http://purl.uniprot.org/annotation/VAR_032838|||http://purl.uniprot.org/annotation/VAR_032839|||http://purl.uniprot.org/annotation/VAR_065622|||http://purl.uniprot.org/annotation/VAR_067444|||http://purl.uniprot.org/annotation/VSP_035034|||http://purl.uniprot.org/annotation/VSP_039975|||http://purl.uniprot.org/annotation/VSP_047044
http://togogenome.org/gene/9606:KIRREL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PRX9|||http://purl.uniprot.org/uniprot/Q8IZU9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with intellectual disability; unknown pathological significance.|||Found in patients with intellectual disability; unknown pathological significance.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In isoform 2.|||Kin of IRRE-like protein 3|||N-linked (GlcNAc...) asparagine|||Processed kin of IRRE-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015098|||http://purl.uniprot.org/annotation/PRO_0000435799|||http://purl.uniprot.org/annotation/PRO_5003242958|||http://purl.uniprot.org/annotation/VAR_054828|||http://purl.uniprot.org/annotation/VAR_054829|||http://purl.uniprot.org/annotation/VAR_054830|||http://purl.uniprot.org/annotation/VSP_011799|||http://purl.uniprot.org/annotation/VSP_011800
http://togogenome.org/gene/9606:FAM222B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ88|||http://purl.uniprot.org/uniprot/B3KTH5|||http://purl.uniprot.org/uniprot/Q8WU58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM222B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274245|||http://purl.uniprot.org/annotation/VAR_050900|||http://purl.uniprot.org/annotation/VAR_050901
http://togogenome.org/gene/9606:MPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40238                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with thrombocytosis; results in altered MPL expression.|||Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In CAMT.|||In CAMT; loss of function.|||In CAMT; loss of function; loss of membrane localization, impaired glycosylation.|||In MMM; somatic mutation; requires 2 nucleotide substitutions.|||In THCYT2 and MMM; somatic mutation in myelofibrosis with myeloid metaplasia; results in cytokine-independent growth and thrombopoietin hypersensitivity; results in constitutive activation of JAK-STAT signaling pathway.|||In THCYT2; activating mutation; induces MPL autonomous dimerization and signal activation in the absence of the ligand.|||In THCYT2; gain of function; loss of membrane localization, impaired glycosylation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Thrombopoietin receptor|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010987|||http://purl.uniprot.org/annotation/VAR_011988|||http://purl.uniprot.org/annotation/VAR_011989|||http://purl.uniprot.org/annotation/VAR_049173|||http://purl.uniprot.org/annotation/VAR_049174|||http://purl.uniprot.org/annotation/VAR_067559|||http://purl.uniprot.org/annotation/VAR_067560|||http://purl.uniprot.org/annotation/VAR_067561|||http://purl.uniprot.org/annotation/VAR_073030|||http://purl.uniprot.org/annotation/VAR_073031|||http://purl.uniprot.org/annotation/VAR_073032|||http://purl.uniprot.org/annotation/VAR_073033|||http://purl.uniprot.org/annotation/VAR_073034|||http://purl.uniprot.org/annotation/VAR_073035|||http://purl.uniprot.org/annotation/VAR_073036|||http://purl.uniprot.org/annotation/VAR_073037|||http://purl.uniprot.org/annotation/VAR_073038|||http://purl.uniprot.org/annotation/VAR_073039|||http://purl.uniprot.org/annotation/VSP_001734|||http://purl.uniprot.org/annotation/VSP_001735
http://togogenome.org/gene/9606:GATD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2D5|||http://purl.uniprot.org/uniprot/A0A140VKB0|||http://purl.uniprot.org/uniprot/F2Z2Q0|||http://purl.uniprot.org/uniprot/P0DPI2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Putative glutamine amidotransferase-like class 1 domain-containing protein 3B, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008544|||http://purl.uniprot.org/annotation/PRO_5002107040|||http://purl.uniprot.org/annotation/PRO_5003294196|||http://purl.uniprot.org/annotation/PRO_5007491755|||http://purl.uniprot.org/annotation/VAR_020441|||http://purl.uniprot.org/annotation/VAR_027921|||http://purl.uniprot.org/annotation/VSP_001454|||http://purl.uniprot.org/annotation/VSP_059660
http://togogenome.org/gene/9606:PTPN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E105|||http://purl.uniprot.org/uniprot/Q05209                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Basic and acidic residues|||Decreases enzyme activity.|||Disordered|||In colon cancer.|||In isoform 2.|||In isoform 3.|||Interaction with TGFB1I1|||Loss of phosphorylation site.|||N-acetylmethionine|||Nearly abolishes enzyme activity.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094771|||http://purl.uniprot.org/annotation/VAR_006385|||http://purl.uniprot.org/annotation/VAR_019512|||http://purl.uniprot.org/annotation/VAR_020297|||http://purl.uniprot.org/annotation/VAR_057129|||http://purl.uniprot.org/annotation/VSP_046274|||http://purl.uniprot.org/annotation/VSP_054168
http://togogenome.org/gene/9606:HR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43593                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C6-type|||Disordered|||In ALUNC.|||In ALUNC; affects binding to thyroid hormone receptor; Markedly diminished histone demethylase activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||JmjC|||LXXLL motif 1|||LXXLL motif 2|||Lysine-specific demethylase hairless|||Markedly diminishes histone demethylase activity.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083890|||http://purl.uniprot.org/annotation/VAR_005265|||http://purl.uniprot.org/annotation/VAR_005266|||http://purl.uniprot.org/annotation/VAR_005267|||http://purl.uniprot.org/annotation/VAR_016222|||http://purl.uniprot.org/annotation/VAR_027806|||http://purl.uniprot.org/annotation/VAR_027807|||http://purl.uniprot.org/annotation/VAR_035927|||http://purl.uniprot.org/annotation/VAR_061664|||http://purl.uniprot.org/annotation/VSP_004276
http://togogenome.org/gene/9606:ADAM12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6G4|||http://purl.uniprot.org/uniprot/O43184|||http://purl.uniprot.org/uniprot/Q5JRP2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 12|||Disordered|||EGF-like|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphotyrosine; by SRC|||Polar residues|||SH3-binding; class I|||SH3-binding; class II|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029078|||http://purl.uniprot.org/annotation/PRO_0000029079|||http://purl.uniprot.org/annotation/PRO_5002724661|||http://purl.uniprot.org/annotation/PRO_5040104221|||http://purl.uniprot.org/annotation/VAR_036143|||http://purl.uniprot.org/annotation/VAR_036144|||http://purl.uniprot.org/annotation/VAR_036145|||http://purl.uniprot.org/annotation/VAR_038542|||http://purl.uniprot.org/annotation/VAR_066310|||http://purl.uniprot.org/annotation/VAR_066311|||http://purl.uniprot.org/annotation/VSP_005476|||http://purl.uniprot.org/annotation/VSP_005477|||http://purl.uniprot.org/annotation/VSP_031001|||http://purl.uniprot.org/annotation/VSP_031002|||http://purl.uniprot.org/annotation/VSP_031003
http://togogenome.org/gene/9606:MAGEA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43355                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes HLA-A1 binding.|||Disordered|||In a breast cancer sample; somatic mutation.|||MAGE|||Melanoma-associated antigen 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156701|||http://purl.uniprot.org/annotation/VAR_004283|||http://purl.uniprot.org/annotation/VAR_011737|||http://purl.uniprot.org/annotation/VAR_036581|||http://purl.uniprot.org/annotation/VAR_053491
http://togogenome.org/gene/9606:GLIS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z689|||http://purl.uniprot.org/uniprot/Q1PHJ8|||http://purl.uniprot.org/uniprot/Q8NEA6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger protein GLIS3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047211|||http://purl.uniprot.org/annotation/VAR_031062|||http://purl.uniprot.org/annotation/VAR_047148|||http://purl.uniprot.org/annotation/VAR_047149|||http://purl.uniprot.org/annotation/VSP_038299
http://togogenome.org/gene/9606:RAB5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51148                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Effector region|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Loss of phosphorylation. No effect on GDI1, GDI2, CHML and CHM binding.|||Phosphomimetic mutant. Loss of GDI1, GDI2, CHML and CHM binding.|||Phosphoserine; by LRRK2|||Polar residues|||Ras-related protein Rab-5C|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121110|||http://purl.uniprot.org/annotation/VAR_036414|||http://purl.uniprot.org/annotation/VSP_046035
http://togogenome.org/gene/9606:RGS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57771                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||RGS|||Regulator of G-protein signaling 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204199|||http://purl.uniprot.org/annotation/VSP_036421
http://togogenome.org/gene/9606:ARL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4G2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 14|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281147|||http://purl.uniprot.org/annotation/VAR_055521|||http://purl.uniprot.org/annotation/VAR_055522
http://togogenome.org/gene/9606:RPL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36578                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL4|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129350
http://togogenome.org/gene/9606:ZFP37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Q3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||KRAB|||Phosphoserine|||Zinc finger protein 37 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047293|||http://purl.uniprot.org/annotation/VAR_058701|||http://purl.uniprot.org/annotation/VSP_037941|||http://purl.uniprot.org/annotation/VSP_055044
http://togogenome.org/gene/9606:LCE3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 3A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235333|||http://purl.uniprot.org/annotation/VAR_053484
http://togogenome.org/gene/9606:CLPTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3H2|||http://purl.uniprot.org/uniprot/O96005                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Putative lipid scramblase CLPTM1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245096|||http://purl.uniprot.org/annotation/VAR_071064|||http://purl.uniprot.org/annotation/VSP_055525|||http://purl.uniprot.org/annotation/VSP_055526
http://togogenome.org/gene/9606:AGFG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z444|||http://purl.uniprot.org/uniprot/P52594                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Arf-GAP domain and FG repeat-containing protein 1|||C4-type|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204904|||http://purl.uniprot.org/annotation/VSP_017600|||http://purl.uniprot.org/annotation/VSP_017601|||http://purl.uniprot.org/annotation/VSP_046186
http://togogenome.org/gene/9606:DGAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Diacylglycerol O-acyltransferase 2|||Disordered|||Found in patients with Charcot-Marie-Tooth disease; unknown pathological significance.|||Helical|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249045|||http://purl.uniprot.org/annotation/VAR_033864|||http://purl.uniprot.org/annotation/VAR_033865|||http://purl.uniprot.org/annotation/VAR_077236|||http://purl.uniprot.org/annotation/VSP_020356
http://togogenome.org/gene/9606:OR52L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGH7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150783|||http://purl.uniprot.org/annotation/VAR_055078|||http://purl.uniprot.org/annotation/VAR_055079|||http://purl.uniprot.org/annotation/VAR_055080|||http://purl.uniprot.org/annotation/VAR_055081|||http://purl.uniprot.org/annotation/VAR_055082
http://togogenome.org/gene/9606:LCA5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95447                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Lebercilin-like protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079507|||http://purl.uniprot.org/annotation/VAR_021947|||http://purl.uniprot.org/annotation/VAR_042739
http://togogenome.org/gene/9606:PAM16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In SMDMDM.|||J-like|||Mitochondrial import inner membrane translocase subunit TIM16|||No effect on protein translocation into mitochondria in a heterologous system.|||Partial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of protein translocation into mitochondria in a heterologous system; when associated with G-92. Loss of DNAJC19-binding; when associated with G-92. Complete loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity; when associated with G-92.|||Partial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of protein translocation into mitochondria in a heterologous system; when associated with G-93. Partial loss of DNAJC19-binding. Loss of DNAJC19-binding; when associated with G-93. Partial loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity. Complete loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity; when associated with G-93.|||Phosphoserine|||Substantial loss of protein translocation into mitochondria in a heterologous system.|||Substantial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of DNAJC19-binding. Partial loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214078|||http://purl.uniprot.org/annotation/VAR_013764|||http://purl.uniprot.org/annotation/VAR_073419
http://togogenome.org/gene/9606:OR2AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG84                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150474|||http://purl.uniprot.org/annotation/VAR_055051|||http://purl.uniprot.org/annotation/VAR_055052
http://togogenome.org/gene/9606:IFI27L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2X8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Interferon alpha-inducible protein 27-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008740
http://togogenome.org/gene/9606:ORM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19652                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-1-acid glycoprotein 2|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000171|||http://purl.uniprot.org/annotation/PRO_0000017861|||http://purl.uniprot.org/annotation/VAR_014667|||http://purl.uniprot.org/annotation/VAR_050172|||http://purl.uniprot.org/annotation/VAR_050173|||http://purl.uniprot.org/annotation/VAR_050174|||http://purl.uniprot.org/annotation/VAR_050175
http://togogenome.org/gene/9606:ATMIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43313                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ATM interactor|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2; degenerate|||Disordered|||In isoform 2.|||Polar residues|||Required for formation of RAD51 foci                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050756|||http://purl.uniprot.org/annotation/VAR_050681|||http://purl.uniprot.org/annotation/VAR_050682|||http://purl.uniprot.org/annotation/VSP_035820
http://togogenome.org/gene/9606:PILRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Greatly diminishes interaction with PTPN6.|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Paired immunoglobulin-like type 2 receptor alpha|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226821|||http://purl.uniprot.org/annotation/VAR_056062|||http://purl.uniprot.org/annotation/VAR_060361|||http://purl.uniprot.org/annotation/VSP_017500|||http://purl.uniprot.org/annotation/VSP_017501|||http://purl.uniprot.org/annotation/VSP_017502
http://togogenome.org/gene/9606:PKIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61925                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site|||Strand                                                                                  ^@                                                                                  Disordered|||Important for inhibition|||N-acetylthreonine|||Polar residues|||Removed|||cAMP-dependent protein kinase inhibitor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154532
http://togogenome.org/gene/9606:MEF2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z417|||http://purl.uniprot.org/uniprot/A0A0S2Z453|||http://purl.uniprot.org/uniprot/A0A0S2Z454|||http://purl.uniprot.org/uniprot/A0A0S2Z4C8|||http://purl.uniprot.org/uniprot/A0A0S2Z4N0|||http://purl.uniprot.org/uniprot/A0A8I5KVQ4|||http://purl.uniprot.org/uniprot/A8K720|||http://purl.uniprot.org/uniprot/Q02078                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cleavage at sites 1 and 2 by caspase 3. Increased cleavage at site 3 by caspase 3.|||Abolishes cleavage at sites 2 and 3 by caspase 7.|||Abolishes sumoylation. No change in subcellular location nor in DNA binding. Loss of transcriptional repression.|||Beta domain|||Cleavage|||Decreased MEF2A protein level.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Greatly reduced p38-mediated phosphorylation. Abolishes P38-mediated transcriptional activation; when associated with A-312.|||Greatly reduced p38-mediated phosphorylation. Abolishes p38-mediated transcriptional activation; when associated with A-319.|||Holliday junction regulator protein family C-terminal|||In isoform 7.|||In isoform 8.|||In isoform MEFA, isoform RSRFC9, isoform 6 and isoform 7.|||In isoform RSRFC4 and isoform RSRFC9.|||In isoform RSRFC4, isoform RSRFC9, isoform 5, isoform 6 and isoform 8.|||Loss of nuclear localization; 66% decrease in transcription activation; loss of synergistic activation by MEF2A and GATA1 through a dominant-negative mechanism.|||Loss of sumoylation.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2A|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on p38-mediated phosphorylation.|||No effect on p38-mediated transcriptional activity.|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CK2|||Phosphoserine; by MAPK|||Phosphoserine; by MAPK14|||Phosphoserine; by MAPK7|||Phosphothreonine|||Phosphothreonine; by MAPK7 and MAPK14|||Phosphothreonine; by NLK|||Polar residues|||Pro residues|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-269.|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-270.|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-273.|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-275.|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-277.|||Reduced p38 alpha- and beta2-mediated transcriptional activity; when associated with A-278.|||Required for interaction with MAPKs|||Rescues sumoylation.|||Slightly increased MEF2A protein level.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199428|||http://purl.uniprot.org/annotation/VAR_017743|||http://purl.uniprot.org/annotation/VAR_038407|||http://purl.uniprot.org/annotation/VAR_038408|||http://purl.uniprot.org/annotation/VAR_038409|||http://purl.uniprot.org/annotation/VSP_006240|||http://purl.uniprot.org/annotation/VSP_006241|||http://purl.uniprot.org/annotation/VSP_006242|||http://purl.uniprot.org/annotation/VSP_043338|||http://purl.uniprot.org/annotation/VSP_046018|||http://purl.uniprot.org/annotation/VSP_046019
http://togogenome.org/gene/9606:SPINK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58062                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016565
http://togogenome.org/gene/9606:SLC66A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MC27|||http://purl.uniprot.org/uniprot/Q8N755                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Solute carrier family 66 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232512|||http://purl.uniprot.org/annotation/VSP_054623
http://togogenome.org/gene/9606:BAG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95429                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with HSP70.|||BAG|||BAG family molecular chaperone regulator 4|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Reduces interaction with HSP70.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088870|||http://purl.uniprot.org/annotation/VSP_042741
http://togogenome.org/gene/9606:CALML3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27482                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Strand                                                                                  ^@                                                                                  Calmodulin-like protein 3|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073547
http://togogenome.org/gene/9606:METTL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJ78                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  12S rRNA N4-methylcytidine (m4C) methyltransferase|||Abolished methylation of 12S rRNA position C839.|||Absence of methylation of 12S rRNA position C839 and decreased methylation at position C841.|||Decreased methylation of 12S rRNA positions C839 and C841.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308332|||http://purl.uniprot.org/annotation/VAR_036801|||http://purl.uniprot.org/annotation/VAR_036802|||http://purl.uniprot.org/annotation/VAR_059446|||http://purl.uniprot.org/annotation/VSP_028970|||http://purl.uniprot.org/annotation/VSP_028971|||http://purl.uniprot.org/annotation/VSP_028972|||http://purl.uniprot.org/annotation/VSP_028973|||http://purl.uniprot.org/annotation/VSP_028974|||http://purl.uniprot.org/annotation/VSP_028975
http://togogenome.org/gene/9606:GRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13255|||http://purl.uniprot.org/uniprot/Q59HC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In SCA44; enhances G-protein coupled glutamate receptor signaling pathway.|||In SCAR13.|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform Beta.|||Interchain|||Metabotropic glutamate receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012922|||http://purl.uniprot.org/annotation/VAR_024482|||http://purl.uniprot.org/annotation/VAR_028184|||http://purl.uniprot.org/annotation/VAR_028185|||http://purl.uniprot.org/annotation/VAR_028186|||http://purl.uniprot.org/annotation/VAR_028187|||http://purl.uniprot.org/annotation/VAR_028188|||http://purl.uniprot.org/annotation/VAR_036194|||http://purl.uniprot.org/annotation/VAR_055875|||http://purl.uniprot.org/annotation/VAR_080186|||http://purl.uniprot.org/annotation/VAR_080187|||http://purl.uniprot.org/annotation/VAR_081782|||http://purl.uniprot.org/annotation/VSP_002024|||http://purl.uniprot.org/annotation/VSP_002025|||http://purl.uniprot.org/annotation/VSP_055127|||http://purl.uniprot.org/annotation/VSP_055128
http://togogenome.org/gene/9606:CHST7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS84                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Carbohydrate sulfotransferase 7|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085198
http://togogenome.org/gene/9606:SNTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMZ2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Sentan                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342516
http://togogenome.org/gene/9606:CHRNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02708|||http://purl.uniprot.org/uniprot/Q53SH4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acetylcholine receptor subunit alpha|||Associated with receptor activation|||Changed acetylcholine-gated cation-selective channel activity.|||Cytoplasmic|||Extracellular|||Helical|||In CMS1A.|||In CMS1A; causes increased channel opening in absence of ACh; prolonged opening in presence of ACh; increased affinity for ACh and enhanced desensitization.|||In CMS1A; increases the rate of channel opening and slows the rate of channel closing but has no effect on agonist binding.|||In CMS1B; abnormally slow channel opening and closing resulting in abnormally brief current.|||In CMS1B; fewer and shorter ion channel activations with decreased channel opening rate and increased channel closing rate.|||In CMS1B; markedly reduced protein expression.|||In CMS1B; mutant channel shows an approximately 30-fold decrease of ACh binding affinity for the second of 2 closed-state binding sites but only a 2-fold decrease in gating efficiency.|||In LMPS.|||In isoform 2.|||Increased length of channel opening.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000305|||http://purl.uniprot.org/annotation/PRO_5011946766|||http://purl.uniprot.org/annotation/VAR_000282|||http://purl.uniprot.org/annotation/VAR_000283|||http://purl.uniprot.org/annotation/VAR_000284|||http://purl.uniprot.org/annotation/VAR_000285|||http://purl.uniprot.org/annotation/VAR_000286|||http://purl.uniprot.org/annotation/VAR_021206|||http://purl.uniprot.org/annotation/VAR_021207|||http://purl.uniprot.org/annotation/VAR_021208|||http://purl.uniprot.org/annotation/VAR_021209|||http://purl.uniprot.org/annotation/VAR_038599|||http://purl.uniprot.org/annotation/VAR_038600|||http://purl.uniprot.org/annotation/VAR_038601|||http://purl.uniprot.org/annotation/VAR_043904|||http://purl.uniprot.org/annotation/VSP_061499
http://togogenome.org/gene/9606:DGAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75907                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished diacylglycerol O-acyltransferase activity.|||Amphipathic helix (AH)|||Cytoplasmic|||Decreased diacylglycerol O-acyltransferase activity.|||Diacylglycerol O-acyltransferase 1|||Disordered|||Does not affect diacylglycerol O-acyltransferase activity.|||Extracellular loop 1 (EL1)|||FYXDWWN motif|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Important for catalytic activity|||In DIAR7; unknown pathological significance.|||Intracellular loop 1 (IL1)|||Intracellular loop 2 (IL2)|||Involved in homomerization|||Lumenal|||MBOAT fold|||Phosphoserine|||Reduced diacylglycerol O-acyltransferase activity.|||Slightly decreased diacylglycerol O-acyltransferase activity.|||Strongly reduced diacylglycerol O-acyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207654|||http://purl.uniprot.org/annotation/VAR_082141
http://togogenome.org/gene/9606:NEIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FI4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Endonuclease 8-like 1|||Found in a patient with childhood-onset nephrotic syndrome, focal segmental glomerulosclerosis and end-stage renal disease; unknown pathological significance.|||Found in a patient with childhood-onset steroid-resistant nephrotic syndrome; unknown pathological significance.|||Found in a patient with nephrotic syndrome also carrying mutation P-159 in MYO1E.|||In RNA edited version.|||Loss of glycosylase activity.|||Loss of glycosylase and AP lyase activity.|||Proton donor|||Proton donor; for beta-elimination activity|||Proton donor; for delta-elimination activity|||Removed|||Schiff-base intermediate with DNA|||Strongly reduced glycosylase activity. Has little effect on AP lyase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170905|||http://purl.uniprot.org/annotation/VAR_020580|||http://purl.uniprot.org/annotation/VAR_020581|||http://purl.uniprot.org/annotation/VAR_020582|||http://purl.uniprot.org/annotation/VAR_020583|||http://purl.uniprot.org/annotation/VAR_020584|||http://purl.uniprot.org/annotation/VAR_065018|||http://purl.uniprot.org/annotation/VAR_065963|||http://purl.uniprot.org/annotation/VAR_065964|||http://purl.uniprot.org/annotation/VAR_087607|||http://purl.uniprot.org/annotation/VAR_087608
http://togogenome.org/gene/9606:IKZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y4D3|||http://purl.uniprot.org/uniprot/A0A2R8YFR0|||http://purl.uniprot.org/uniprot/A0A8V8TNQ0|||http://purl.uniprot.org/uniprot/C9JTB0|||http://purl.uniprot.org/uniprot/Q13422                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to DNA and has diffuse nuclear localization.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||DNA-binding protein Ikaros|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In CVID13; abolishes binding to DNA; has diffuse nuclear localization.|||In CVID13; decreases binding to pericentromeric heterochromatin DNA; has diffuse nuclear localization.|||In isoform Ik2.|||In isoform Ik3 and isoform Ik4.|||In isoform Ik4.|||In isoform Ik5.|||In isoform Ik6.|||In isoform Ik7 and isoform Ikx.|||In isoform Ikx.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for binding PP1CC|||Required for both high-affinity DNA binding and pericentromeric heterochromatin localization|||Required for both pericentromeric heterochromatin localization and DNA binding|||Required for both pericentromeric heterochromatin localization and complete DNA binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047094|||http://purl.uniprot.org/annotation/VAR_076401|||http://purl.uniprot.org/annotation/VAR_076402|||http://purl.uniprot.org/annotation/VAR_076403|||http://purl.uniprot.org/annotation/VAR_076404|||http://purl.uniprot.org/annotation/VAR_076405|||http://purl.uniprot.org/annotation/VSP_006847|||http://purl.uniprot.org/annotation/VSP_006848|||http://purl.uniprot.org/annotation/VSP_006849|||http://purl.uniprot.org/annotation/VSP_006850|||http://purl.uniprot.org/annotation/VSP_006851|||http://purl.uniprot.org/annotation/VSP_006852|||http://purl.uniprot.org/annotation/VSP_053404|||http://purl.uniprot.org/annotation/VSP_053405
http://togogenome.org/gene/9606:IFNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0W0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon kappa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016410|||http://purl.uniprot.org/annotation/VAR_021303|||http://purl.uniprot.org/annotation/VAR_032710
http://togogenome.org/gene/9606:HDAC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2SVS4|||http://purl.uniprot.org/uniprot/P56524                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone deacetylase activity.|||Abolishes sumoylation and reduces the histone deacetylase activity.|||Basic and acidic residues|||Contributes to catalysis|||Decreased interaction with ANKRA2.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Histone deacetylase|||Histone deacetylase 4|||Histone deacetylase glutamine rich N-terminal|||In NEDCHF.|||In NEDCHF; decreased interaction with YWHAB.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with MEF2A|||Loss of interaction with ANKRA2.|||May affect interaction with ANKRA2.|||No effect on interaction with ANKRA2.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by CaMK4|||Phosphoserine; by CaMK4 and SIK1|||Polar residues|||PxLPxI/L motif; mediates interaction with ANKRA2 and 14-3-3 proteins|||Reduces CaMK-dependent nuclear export.|||Reduces phosphorylation and its subsequent nuclear export.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114699|||http://purl.uniprot.org/annotation/VAR_036042|||http://purl.uniprot.org/annotation/VAR_071965|||http://purl.uniprot.org/annotation/VAR_087034|||http://purl.uniprot.org/annotation/VAR_087035|||http://purl.uniprot.org/annotation/VAR_087036|||http://purl.uniprot.org/annotation/VAR_087037|||http://purl.uniprot.org/annotation/VSP_057290|||http://purl.uniprot.org/annotation/VSP_057291
http://togogenome.org/gene/9606:ADCY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J1J0|||http://purl.uniprot.org/uniprot/Q08828                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 1|||Cytoplasmic|||Disordered|||Guanylate cyclase|||Helical|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195682|||http://purl.uniprot.org/annotation/VAR_029186|||http://purl.uniprot.org/annotation/VAR_029187|||http://purl.uniprot.org/annotation/VAR_048246
http://togogenome.org/gene/9606:SCAMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969E2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||Secretory carrier-associated membrane protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191259|||http://purl.uniprot.org/annotation/VAR_061783|||http://purl.uniprot.org/annotation/VSP_026446|||http://purl.uniprot.org/annotation/VSP_026447
http://togogenome.org/gene/9606:MAOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21397|||http://purl.uniprot.org/uniprot/Q49A63|||http://purl.uniprot.org/uniprot/Q53YE7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amine oxidase|||Amine oxidase [flavin-containing] A|||Complete loss of activity.|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Important for catalytic activity|||Important for substrate specificity|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with membrane phospholipid headgroups|||Mitochondrial intermembrane|||N-acetylmethionine|||No loss of activity.|||Phosphoserine|||Probable disease-associated variant found in a family with Brunner syndrome-like behavioral disturbances; reduced activity.|||S-8alpha-FAD cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099850|||http://purl.uniprot.org/annotation/VAR_014795|||http://purl.uniprot.org/annotation/VAR_014796|||http://purl.uniprot.org/annotation/VAR_036545|||http://purl.uniprot.org/annotation/VAR_064573|||http://purl.uniprot.org/annotation/VAR_071963|||http://purl.uniprot.org/annotation/VSP_045173
http://togogenome.org/gene/9606:QRFPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z3L3|||http://purl.uniprot.org/uniprot/Q96P65                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Pyroglutamylated RF-amide peptide receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070097|||http://purl.uniprot.org/annotation/VAR_049437|||http://purl.uniprot.org/annotation/VAR_049438|||http://purl.uniprot.org/annotation/VAR_049439
http://togogenome.org/gene/9606:C1orf127                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLG7|||http://purl.uniprot.org/uniprot/G8JLG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5003510497
http://togogenome.org/gene/9606:RNF34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTM5|||http://purl.uniprot.org/uniprot/Q969K3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Cleavage; by caspase-3|||Disordered|||E3 ubiquitin-protein ligase RNF34|||FYVE-type|||In isoform 2.|||Loss of E3 ubiquitin protein ligase activity.|||Phosphoserine|||Polar residues|||RING-type|||SAP 1|||SAP 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056072|||http://purl.uniprot.org/annotation/VSP_038341
http://togogenome.org/gene/9606:OR2AG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWC6|||http://purl.uniprot.org/uniprot/A6NM03                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AG2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312343|||http://purl.uniprot.org/annotation/VAR_037497|||http://purl.uniprot.org/annotation/VAR_037498|||http://purl.uniprot.org/annotation/VAR_037499|||http://purl.uniprot.org/annotation/VAR_037500
http://togogenome.org/gene/9606:ANKS4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8V4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Acidic residues|||Ankyrin repeat and SAM domain-containing protein 4B|||Decreased interaction with USH1C.|||Decreased localization to microvilli.|||Disordered|||Mediates interaction with MYO7B|||Mediates localization to microvilli|||PDZ-binding; mediates interaction with USH1C|||Phosphoserine|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066996
http://togogenome.org/gene/9606:PRAMEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60811                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156976|||http://purl.uniprot.org/annotation/VAR_034400|||http://purl.uniprot.org/annotation/VAR_034401|||http://purl.uniprot.org/annotation/VAR_034402|||http://purl.uniprot.org/annotation/VAR_034403|||http://purl.uniprot.org/annotation/VAR_034404|||http://purl.uniprot.org/annotation/VAR_034405|||http://purl.uniprot.org/annotation/VAR_034406|||http://purl.uniprot.org/annotation/VAR_034407|||http://purl.uniprot.org/annotation/VAR_034408|||http://purl.uniprot.org/annotation/VAR_034409|||http://purl.uniprot.org/annotation/VAR_034410|||http://purl.uniprot.org/annotation/VAR_034411|||http://purl.uniprot.org/annotation/VAR_034412|||http://purl.uniprot.org/annotation/VAR_034413|||http://purl.uniprot.org/annotation/VAR_053606|||http://purl.uniprot.org/annotation/VAR_060093
http://togogenome.org/gene/9606:CX3CR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49238                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with a markedly reduced risk of acute coronary artery disease; associated with higher risk of developing ARMD12; chemotaxis of monocytes of individuals with homozygous Ile-249 and Met-280 genotypes is impaired in the presence of bound CX3CR1 protein.|||Associated with higher risk of developing ARMD12; impaired antifungal innate immune response; chemotaxis of monocytes of individuals with homozygous Met-280 and Ile-249 genotypes is impaired in the presence of bound CX3CR1 protein.|||CX3C chemokine receptor 1|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069326|||http://purl.uniprot.org/annotation/VAR_010041|||http://purl.uniprot.org/annotation/VAR_010042|||http://purl.uniprot.org/annotation/VAR_010043|||http://purl.uniprot.org/annotation/VAR_010044|||http://purl.uniprot.org/annotation/VAR_022062|||http://purl.uniprot.org/annotation/VAR_049386|||http://purl.uniprot.org/annotation/VSP_009681|||http://purl.uniprot.org/annotation/VSP_009682|||http://purl.uniprot.org/annotation/VSP_044595
http://togogenome.org/gene/9606:POLR2H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52434                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerases I, II, and III subunit RPABC3|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||N-acetylalanine|||Non-specific ssDNA binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073997|||http://purl.uniprot.org/annotation/VSP_055017|||http://purl.uniprot.org/annotation/VSP_055018|||http://purl.uniprot.org/annotation/VSP_055019
http://togogenome.org/gene/9606:TJAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTD0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Tight junction-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072550|||http://purl.uniprot.org/annotation/VSP_015999|||http://purl.uniprot.org/annotation/VSP_016000|||http://purl.uniprot.org/annotation/VSP_016001|||http://purl.uniprot.org/annotation/VSP_016002
http://togogenome.org/gene/9606:TOB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14106                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein Tob2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143815|||http://purl.uniprot.org/annotation/VSP_055557
http://togogenome.org/gene/9606:PIANP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||O-linked (GalNAc...) threonine|||PILR alpha-associated neural protein|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285964|||http://purl.uniprot.org/annotation/VSP_024939
http://togogenome.org/gene/9606:CCL19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IBD6|||http://purl.uniprot.org/uniprot/Q99731                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine|||C-C motif chemokine 19|||Chemokine interleukin-8-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005214|||http://purl.uniprot.org/annotation/PRO_5014205945
http://togogenome.org/gene/9606:MBOAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T53                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes ability to acylate ghrelin.|||Cytoplasmic|||Does not affect octanoyltransferase activity.|||Ghrelin O-acyltransferase|||Helical|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273024|||http://purl.uniprot.org/annotation/VAR_030069|||http://purl.uniprot.org/annotation/VAR_059434|||http://purl.uniprot.org/annotation/VSP_032958|||http://purl.uniprot.org/annotation/VSP_032959
http://togogenome.org/gene/9606:RBPMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRY4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Important for homodimerization|||In isoform 2.|||N-acetylserine|||No effect on homodimerization. No effect on function in gastrointestinal smooth muscle cell differentiation.|||RNA-binding protein with multiple splicing 2|||RRM|||Removed|||Strongly reduces homodimerization and interaction with EEF2. Strongly reduces NOG mRNA binding. Loss of function in gastrointestinal smooth muscle cell differentiation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274909|||http://purl.uniprot.org/annotation/VSP_056896
http://togogenome.org/gene/9606:TMEFF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Kazal-like 1|||Kazal-like 2|||N-linked (GlcNAc...) (complex) asparagine; atypical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for shedding|||Tomoregulin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016587|||http://purl.uniprot.org/annotation/VSP_014312|||http://purl.uniprot.org/annotation/VSP_014313|||http://purl.uniprot.org/annotation/VSP_024973|||http://purl.uniprot.org/annotation/VSP_024974
http://togogenome.org/gene/9606:AMER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  APC membrane recruitment protein 2|||Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281885|||http://purl.uniprot.org/annotation/VAR_031303|||http://purl.uniprot.org/annotation/VAR_036448|||http://purl.uniprot.org/annotation/VSP_024089
http://togogenome.org/gene/9606:C8orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX44|||http://purl.uniprot.org/uniprot/Q8NAV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DUF4657|||Disordered|||In isoform 2.|||Pro residues|||Uncharacterized protein C8orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285640|||http://purl.uniprot.org/annotation/VSP_024876
http://togogenome.org/gene/9606:STXBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFX7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylserine|||Removed|||Syntaxin-binding protein 6|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206782|||http://purl.uniprot.org/annotation/VSP_008071|||http://purl.uniprot.org/annotation/VSP_008072|||http://purl.uniprot.org/annotation/VSP_008073
http://togogenome.org/gene/9606:LIMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Interaction with EGLN1/PHD2|||Interaction with RB1|||LIM domain-containing protein 1|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Mediates nuclear export|||Necessary for nuclear localization|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075801|||http://purl.uniprot.org/annotation/VAR_021993|||http://purl.uniprot.org/annotation/VAR_050147
http://togogenome.org/gene/9606:SMTNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MU46                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Calmodulin-binding|||Calponin-homology (CH)|||Disordered|||Phosphoserine|||Polar residues|||Smoothelin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317275
http://togogenome.org/gene/9606:TMEM225                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GV28                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||RVxF|||Transmembrane protein 225                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339350|||http://purl.uniprot.org/annotation/VAR_051260|||http://purl.uniprot.org/annotation/VAR_061690
http://togogenome.org/gene/9606:ALKBH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BT7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alkylated DNA repair protein alkB homolog 8|||Basic and acidic residues|||Disordered|||Fe2OG dioxygenase|||In MRT71; missing tRNA wobble uridine modification.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Methyltransferase domain|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337125|||http://purl.uniprot.org/annotation/VAR_083119|||http://purl.uniprot.org/annotation/VSP_033925|||http://purl.uniprot.org/annotation/VSP_033926|||http://purl.uniprot.org/annotation/VSP_033927|||http://purl.uniprot.org/annotation/VSP_033928|||http://purl.uniprot.org/annotation/VSP_039159
http://togogenome.org/gene/9606:HHIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QV1                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes SHH binding.|||EGF-like 1|||EGF-like 2|||Hedgehog-interacting protein|||In isoform 2.|||Interaction with SHH zinc binding site|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007623|||http://purl.uniprot.org/annotation/VAR_021518|||http://purl.uniprot.org/annotation/VSP_013192|||http://purl.uniprot.org/annotation/VSP_013193
http://togogenome.org/gene/9606:HORMAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG9|||http://purl.uniprot.org/uniprot/Q86X24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HORMA|||HORMA domain-containing protein 1|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284664|||http://purl.uniprot.org/annotation/VAR_031801|||http://purl.uniprot.org/annotation/VSP_024600|||http://purl.uniprot.org/annotation/VSP_024601|||http://purl.uniprot.org/annotation/VSP_024602|||http://purl.uniprot.org/annotation/VSP_024603
http://togogenome.org/gene/9606:GNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13823|||http://purl.uniprot.org/uniprot/Q5T0F3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CP-type G|||Diffused nuclear localization, loss of nucleolar localization.|||Disordered|||Loss of GTP-binding. Efficient localization to the nucleus, but excluded from nucleoli.|||Loss of GTP-binding. Punctate pattern throughout the nucleus, including nucleoli.|||N-acetylmethionine|||No effect on GTP-binding, nor on nucleolar localization.|||No effect on nucleolar localization Predominantly cytoplasmic, with some nucleolar staining; when associated with 682-AAA-684. Strong nucleolar localization, with some cytoplasmic staining; when associated with 724-AAA-726. Diffused localization to both cytoplasm and nucleus; when associated with 682-AAA-684 and 724-AAA-726.|||No effect on nucleolar localization.|||No effect on nucleolar localization. Predominantly cytoplasmic, with some nucleolar staining; when associated with 711-AAA-713. Diffused localization to both cytoplasm and nucleus; when associated with 711-AAA-713 and 724-AAA-726.|||No effect on nucleolar localization. Strong nucleolar localization, with some cytoplasmic staining; when associated with 711-AAA-713. Diffused localization to both cytoplasm and nucleus; when associated with 682-AAA-684 and 711-AAA-713.|||No effect on nucleolar localization; when associated with A-463.|||No effect on nucleolar localization; when associated with A-475.|||Nucleolar GTP-binding protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215806|||http://purl.uniprot.org/annotation/VAR_050291
http://togogenome.org/gene/9606:PNLIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16233                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In PNLIPD; loss of function in lipid catabolic process; the mutant is not secreted.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT|||Pancreatic triacylglycerol lipase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017785|||http://purl.uniprot.org/annotation/VAR_078977
http://togogenome.org/gene/9606:ACSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9T3|||http://purl.uniprot.org/uniprot/B4E0R0|||http://purl.uniprot.org/uniprot/E7EPM6|||http://purl.uniprot.org/uniprot/P33121                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3'-nitrotyrosine|||AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||Long-chain-fatty-acid--CoA ligase 1|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193104|||http://purl.uniprot.org/annotation/VSP_009604|||http://purl.uniprot.org/annotation/VSP_054391
http://togogenome.org/gene/9606:S100B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4C5|||http://purl.uniprot.org/uniprot/P04271                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Strand|||Turn                                                                                  ^@                                                                                  Blocked amino end (Ser); alternate|||EF-hand|||EF-hand 1|||EF-hand 2|||N-acetylserine; alternate|||Protein S100-B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143966
http://togogenome.org/gene/9606:OR8B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGG8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150655|||http://purl.uniprot.org/annotation/VAR_047145|||http://purl.uniprot.org/annotation/VAR_047146
http://togogenome.org/gene/9606:ZBTB26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Zinc finger and BTB domain-containing protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047739|||http://purl.uniprot.org/annotation/VAR_052916
http://togogenome.org/gene/9606:ESX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N693                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 9 AA tandem repeats of P-P-x-x-P-x-P-P-x|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein ESX1|||Homeobox protein ESX1-C|||Homeobox protein ESX1-N|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048876|||http://purl.uniprot.org/annotation/PRO_0000386625|||http://purl.uniprot.org/annotation/PRO_0000386626|||http://purl.uniprot.org/annotation/VAR_059352
http://togogenome.org/gene/9606:DDX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTA4|||http://purl.uniprot.org/uniprot/P17844                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNA helicase activity.|||Abolishes sumoylation, abolishes interaction with HDAC1, increases TP53 coactivation and promotes polyubiquitination.|||Abolishes sumoylation.|||Basic and acidic residues|||Binds to the tau stem-loop-containing RNA. Inhibits tau exon 10 inclusion and RNA cleavage. Does not inhibit interaction with RBM4.|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Probable ATP-dependent RNA helicase DDX5|||Q motif|||Transactivation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054991|||http://purl.uniprot.org/annotation/VAR_029241|||http://purl.uniprot.org/annotation/VSP_056154
http://togogenome.org/gene/9606:ARMCX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9R4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||Armadillo repeat-containing X-linked protein 4|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191370|||http://purl.uniprot.org/annotation/VAR_024761|||http://purl.uniprot.org/annotation/VSP_060248|||http://purl.uniprot.org/annotation/VSP_060249|||http://purl.uniprot.org/annotation/VSP_060250|||http://purl.uniprot.org/annotation/VSP_060251
http://togogenome.org/gene/9606:SLC35G4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7Q5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA 1|||EamA 2|||Helical|||Putative solute carrier family 35 member G4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342675|||http://purl.uniprot.org/annotation/VAR_061556
http://togogenome.org/gene/9606:FBXO39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4B4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119935|||http://purl.uniprot.org/annotation/VAR_024444|||http://purl.uniprot.org/annotation/VAR_024445|||http://purl.uniprot.org/annotation/VAR_024446|||http://purl.uniprot.org/annotation/VAR_049050|||http://purl.uniprot.org/annotation/VAR_049051
http://togogenome.org/gene/9606:CPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N679|||http://purl.uniprot.org/uniprot/P16870                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase E|||In BDVS.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004384|||http://purl.uniprot.org/annotation/PRO_0000004385|||http://purl.uniprot.org/annotation/PRO_5017279394|||http://purl.uniprot.org/annotation/VAR_036011|||http://purl.uniprot.org/annotation/VAR_048599|||http://purl.uniprot.org/annotation/VAR_085993|||http://purl.uniprot.org/annotation/VAR_085994|||http://purl.uniprot.org/annotation/VSP_040959
http://togogenome.org/gene/9606:NMRAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P622|||http://purl.uniprot.org/uniprot/Q9HBL8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Does not impair binding to NADPH; maintains the dimerization properties as the wild type; does not affect binding to ASS1; does not affect perinuclear localization.|||Impairs binding to NADPH; abolishes the ability to dimerize; enhances binding to ASS1; reduces perinuclear localization.|||Impairs binding to NADPH; enhances binding to ASS1; reduces perinuclear localization.|||Interaction with ASS1|||NmrA-like|||NmrA-like family domain-containing protein 1|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278204|||http://purl.uniprot.org/annotation/VAR_030689|||http://purl.uniprot.org/annotation/VAR_030690
http://togogenome.org/gene/9606:EPDR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J80|||http://purl.uniprot.org/uniprot/Q9UM22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Mammalian ependymin-related protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008351|||http://purl.uniprot.org/annotation/PRO_5004324155|||http://purl.uniprot.org/annotation/VSP_031976|||http://purl.uniprot.org/annotation/VSP_046829
http://togogenome.org/gene/9606:PMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RH45|||http://purl.uniprot.org/uniprot/P02689                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Disordered|||In CMT1G.|||Myelin P2 protein|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067388|||http://purl.uniprot.org/annotation/VAR_081897|||http://purl.uniprot.org/annotation/VAR_081898|||http://purl.uniprot.org/annotation/VAR_081899
http://togogenome.org/gene/9606:MLF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1F4|||http://purl.uniprot.org/uniprot/Q15773|||http://purl.uniprot.org/uniprot/Q5U0N1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||Myeloid leukemia factor 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220754|||http://purl.uniprot.org/annotation/VAR_036429
http://togogenome.org/gene/9606:TFRC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TM46|||http://purl.uniprot.org/uniprot/A8K6Q8|||http://purl.uniprot.org/uniprot/B7Z2I6|||http://purl.uniprot.org/uniprot/G3V0E5|||http://purl.uniprot.org/uniprot/P02786                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1.27-fold increase of the endocytic uptake of the receptor.|||16% binding to transferrin.|||2-fold increase of the endocytic uptake of the receptor.|||20-fold reduced affinity for transferrin receptor. No binding to HFE.|||20-fold reduced affinity for transferrin. No binding to HFE.|||5% binding to transferrin.|||57% binding to transferrin.|||>5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE.|||Cell attachment site; required for binding to transferrin|||Cleavage; by trypsin; to produce soluble form|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In IMD46; increases protein expression; increases cell surface expression on T and B cells; increases soluble form level; impairs receptor internalization; impairs transferrin transport; impairs T and B cell proliferation as well as B cell class-switching; interacts with STEAP3; doesn't affect receptor internalization in erythroid precursor cells.|||Interchain|||Large effect on affinity for transferrin. 4-fold reduced affinity for HFE.|||Ligand-binding|||Mediates interaction with SH3BP4|||N-linked (GlcNAc...) asparagine|||No binding to transferrin.|||No effect on binding to transferrin. >10-fold reduced affinity for HFE.|||No influence on endocytic uptake of the receptor.|||No significant effect on binding to transferrin nor HFE.|||O-linked (GalNAc...) threonine|||Only 14% as active as wild-type receptor.|||Only 16% as active as wild-type receptor.|||Only 19% as active as wild-type receptor.|||Only 20% as active as wild-type receptor.|||Only 35% as active as wild-type receptor.|||Only 48% as active as wild-type receptor.|||Only 80% as active as wild-type receptor.|||Only 88% as active as wild-type receptor.|||PA|||Peptidase M28|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine|||Stop-transfer sequence|||Transferrin receptor protein 1|||Transferrin receptor protein 1, serum form|||Transferrin receptor-like dimerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000072|||http://purl.uniprot.org/annotation/CAR_000173|||http://purl.uniprot.org/annotation/PRO_0000174132|||http://purl.uniprot.org/annotation/PRO_0000292265|||http://purl.uniprot.org/annotation/VAR_012737|||http://purl.uniprot.org/annotation/VAR_051806|||http://purl.uniprot.org/annotation/VAR_051807|||http://purl.uniprot.org/annotation/VAR_051808|||http://purl.uniprot.org/annotation/VAR_076365
http://togogenome.org/gene/9606:TRAM1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N609                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||TLC|||Translocating chain-associated membrane protein 1-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313706
http://togogenome.org/gene/9606:TINAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSC1|||http://purl.uniprot.org/uniprot/Q9UJW2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Alternate|||Cleavage; by furin|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SMB|||Tubulointerstitial nephritis antigen                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050600|||http://purl.uniprot.org/annotation/VAR_047091|||http://purl.uniprot.org/annotation/VAR_047092|||http://purl.uniprot.org/annotation/VAR_047093|||http://purl.uniprot.org/annotation/VAR_047094|||http://purl.uniprot.org/annotation/VAR_047095|||http://purl.uniprot.org/annotation/VSP_050567|||http://purl.uniprot.org/annotation/VSP_050568
http://togogenome.org/gene/9606:CYP2W1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAV3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Associated with increased colorectal cancer risk.|||Cytochrome P450 2W1|||Loss of glycosylation.|||N-linked (GlcNAc...) asparagine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051782|||http://purl.uniprot.org/annotation/VAR_027413|||http://purl.uniprot.org/annotation/VAR_071912|||http://purl.uniprot.org/annotation/VAR_071913|||http://purl.uniprot.org/annotation/VAR_071914|||http://purl.uniprot.org/annotation/VAR_071915
http://togogenome.org/gene/9606:TRAPPC6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75865                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Trafficking protein particle complex subunit 6A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244539|||http://purl.uniprot.org/annotation/VSP_019585|||http://purl.uniprot.org/annotation/VSP_047016|||http://purl.uniprot.org/annotation/VSP_047017
http://togogenome.org/gene/9606:AKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK05|||http://purl.uniprot.org/uniprot/B4DN86|||http://purl.uniprot.org/uniprot/Q92667                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  A-kinase anchor protein 1, mitochondrial|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||KH|||Mitochondrion|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016659|||http://purl.uniprot.org/annotation/VAR_024512|||http://purl.uniprot.org/annotation/VAR_049676|||http://purl.uniprot.org/annotation/VAR_049677|||http://purl.uniprot.org/annotation/VAR_049678|||http://purl.uniprot.org/annotation/VSP_002845|||http://purl.uniprot.org/annotation/VSP_002846
http://togogenome.org/gene/9606:STK26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P289                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished serine/threonine-protein kinase activity.|||Disordered|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086404|||http://purl.uniprot.org/annotation/VAR_040844|||http://purl.uniprot.org/annotation/VAR_040845|||http://purl.uniprot.org/annotation/VAR_040846|||http://purl.uniprot.org/annotation/VSP_041469|||http://purl.uniprot.org/annotation/VSP_041470
http://togogenome.org/gene/9606:CCDC153                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q494R4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 153|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342650|||http://purl.uniprot.org/annotation/VAR_044322|||http://purl.uniprot.org/annotation/VSP_034518
http://togogenome.org/gene/9606:GPR32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NIL6|||http://purl.uniprot.org/uniprot/O75388                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069552|||http://purl.uniprot.org/annotation/VAR_011860
http://togogenome.org/gene/9606:RAB15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V562|||http://purl.uniprot.org/uniprot/G5EMR8|||http://purl.uniprot.org/uniprot/P59190                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||In isoform 2.|||Ras-related protein Rab-15|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121188|||http://purl.uniprot.org/annotation/VSP_010420
http://togogenome.org/gene/9606:SLAMF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A28                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SLAM family member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042233|||http://purl.uniprot.org/annotation/VAR_023580|||http://purl.uniprot.org/annotation/VAR_032812|||http://purl.uniprot.org/annotation/VAR_032813|||http://purl.uniprot.org/annotation/VAR_032814|||http://purl.uniprot.org/annotation/VSP_015819|||http://purl.uniprot.org/annotation/VSP_015820
http://togogenome.org/gene/9606:TSGA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Testis-specific gene 13 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286344
http://togogenome.org/gene/9606:OLIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Oligodendrocyte transcription factor 1|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127411
http://togogenome.org/gene/9606:CLEC2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHP7|||http://purl.uniprot.org/uniprot/W8JXM2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 2 member D|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315285|||http://purl.uniprot.org/annotation/VAR_038172|||http://purl.uniprot.org/annotation/VAR_038173|||http://purl.uniprot.org/annotation/VSP_039676|||http://purl.uniprot.org/annotation/VSP_039678|||http://purl.uniprot.org/annotation/VSP_039680|||http://purl.uniprot.org/annotation/VSP_039681|||http://purl.uniprot.org/annotation/VSP_039682|||http://purl.uniprot.org/annotation/VSP_039683
http://togogenome.org/gene/9606:NCOA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59EE8|||http://purl.uniprot.org/uniprot/Q9Y6Q9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes acetylation by CREBBP.|||Acetyltransferase|||Asymmetric dimethylarginine|||BHLH|||Basic and acidic residues|||Disordered|||Does not affect acetylation by CREBBP.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||Interaction with CREBBP|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; by CREBBP|||Nuclear receptor coactivator 3|||PAS|||Phosphoserine|||Phosphoserine; by CK1|||Polar residues|||Removed|||Strongly reduces acetylation by CREBBP.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094406|||http://purl.uniprot.org/annotation/VAR_013831|||http://purl.uniprot.org/annotation/VAR_013832|||http://purl.uniprot.org/annotation/VAR_013833|||http://purl.uniprot.org/annotation/VAR_013834|||http://purl.uniprot.org/annotation/VAR_053527|||http://purl.uniprot.org/annotation/VAR_053528|||http://purl.uniprot.org/annotation/VAR_053529|||http://purl.uniprot.org/annotation/VAR_060695|||http://purl.uniprot.org/annotation/VAR_060696|||http://purl.uniprot.org/annotation/VAR_060697|||http://purl.uniprot.org/annotation/VAR_060698|||http://purl.uniprot.org/annotation/VSP_003405|||http://purl.uniprot.org/annotation/VSP_003406|||http://purl.uniprot.org/annotation/VSP_003407|||http://purl.uniprot.org/annotation/VSP_003408
http://togogenome.org/gene/9606:PKP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99569                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Plakophilin-4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064289|||http://purl.uniprot.org/annotation/VSP_006737
http://togogenome.org/gene/9606:IFIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09913|||http://purl.uniprot.org/uniprot/Q05DN2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Abolishes RNA-binding.|||Disordered|||Interferon-induced protein with tetratricopeptide repeats 2|||N-acetylserine|||Removed|||Significantly impairs RNA-binding; when associated with Glu-255.|||Significantly impairs RNA-binding; when associated with Glu-259.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106347|||http://purl.uniprot.org/annotation/VAR_014490|||http://purl.uniprot.org/annotation/VAR_052615|||http://purl.uniprot.org/annotation/VAR_052616
http://togogenome.org/gene/9606:SHROOM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z682|||http://purl.uniprot.org/uniprot/F5H3B6|||http://purl.uniprot.org/uniprot/Q13796|||http://purl.uniprot.org/uniprot/Q68DU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  ASD1|||ASD2|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein Shroom2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064650|||http://purl.uniprot.org/annotation/VAR_024250|||http://purl.uniprot.org/annotation/VAR_036577|||http://purl.uniprot.org/annotation/VAR_053896|||http://purl.uniprot.org/annotation/VAR_053897
http://togogenome.org/gene/9606:KLHL25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0H3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272308|||http://purl.uniprot.org/annotation/VAR_050041|||http://purl.uniprot.org/annotation/VAR_050042
http://togogenome.org/gene/9606:SNRPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62306                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  N-acetylserine|||Removed|||Sm|||Small nuclear ribonucleoprotein F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125536
http://togogenome.org/gene/9606:PPP4R3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IN85|||http://purl.uniprot.org/uniprot/Q8N6W1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 5.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 3A|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254598|||http://purl.uniprot.org/annotation/VSP_021252|||http://purl.uniprot.org/annotation/VSP_021253|||http://purl.uniprot.org/annotation/VSP_021256
http://togogenome.org/gene/9606:AJM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J069                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Apical junction component 1 homolog|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392544
http://togogenome.org/gene/9606:GAGE10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337202|||http://purl.uniprot.org/annotation/VAR_085737|||http://purl.uniprot.org/annotation/VAR_085738
http://togogenome.org/gene/9606:E2F4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16254                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEF box|||Dimerization|||Disordered|||HCFC1-binding-motif (HBM)|||Interaction with RBL1 and RBL2|||Leucine-zipper|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||Transactivation|||Transcription factor E2F4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219468|||http://purl.uniprot.org/annotation/VAR_014024|||http://purl.uniprot.org/annotation/VAR_014936
http://togogenome.org/gene/9606:GPSM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIF1|||http://purl.uniprot.org/uniprot/P81274                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes interaction with INSC; when associated with E-228.|||Abolishes location at mitotic spindle poles; when associated with A-228.|||Abolishes location at mitotic spindle poles; when associated with A-243.|||G-protein-signaling modulator 2|||GoLoco 1|||GoLoco 2|||GoLoco 3|||GoLoco 4|||Important for interaction with NUMA1; INSC and FRMPD1|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by PKG|||Phosphothreonine|||Strongly reduces interaction with INSC. Abolishes interaction with INSC; when associated with R-290.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106358
http://togogenome.org/gene/9606:PECR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY49                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to peroxisomes.|||In isoform 2.|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal trans-2-enoyl-CoA reductase|||Phosphoserine|||Phosphotyrosine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054740|||http://purl.uniprot.org/annotation/VAR_021535|||http://purl.uniprot.org/annotation/VAR_021536|||http://purl.uniprot.org/annotation/VSP_013260
http://togogenome.org/gene/9606:TBCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15814                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-CAP/cofactor C-like|||Disordered|||Inhibits stimulation of tubulin GTPase activity.|||N-acetylmethionine|||Phosphoserine|||Tubulin-specific chaperone C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080046|||http://purl.uniprot.org/annotation/VAR_020448|||http://purl.uniprot.org/annotation/VAR_024653|||http://purl.uniprot.org/annotation/VAR_026822|||http://purl.uniprot.org/annotation/VAR_026823|||http://purl.uniprot.org/annotation/VAR_026824|||http://purl.uniprot.org/annotation/VAR_067423
http://togogenome.org/gene/9606:RCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14257                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||In isoform 2.|||Phosphothreonine|||Prevents secretion from ER|||Reticulocalbin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004148|||http://purl.uniprot.org/annotation/VSP_055139
http://togogenome.org/gene/9606:AZIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTF6|||http://purl.uniprot.org/uniprot/O14977                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Antizyme inhibitor 1|||N6-(pyridoxal phosphate)lysine|||Not modified|||Orn/DAP/Arg decarboxylase 2 C-terminal|||Orn/DAP/Arg decarboxylase 2 N-terminal|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149992
http://togogenome.org/gene/9606:KRTAP24-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI83                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 10 AA repeats of Y-[ILR]-[SVPC]-[NRTS]-[SNTG]-X-[QHRP]-[PSY]-[QSL]-[SRK]|||Keratin-associated protein 24-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223915
http://togogenome.org/gene/9606:CPLX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7G2                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Propeptide|||Region                                                                                  ^@                                                                                  Complexin-4|||Cysteine methyl ester|||Disordered|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240235|||http://purl.uniprot.org/annotation/PRO_0000240236
http://togogenome.org/gene/9606:FCHO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0JRZ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binds preferentially to larger liposomes.|||Disordered|||F-BAR|||F-BAR domain only protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interchain (with C-147)|||Interchain (with C-273)|||MHD|||Mediates dimerization and binding to membranes enriched in Pi(4,5)-P2 and induces their tubulation|||Mediates interaction with DAB2, EPS15, EPS15R and ITSN1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266005|||http://purl.uniprot.org/annotation/VAR_029636|||http://purl.uniprot.org/annotation/VSP_021910|||http://purl.uniprot.org/annotation/VSP_021911|||http://purl.uniprot.org/annotation/VSP_044812
http://togogenome.org/gene/9606:NOSTRIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVI9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  F-BAR|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nostrin|||Phosphoserine|||REM-1|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289089|||http://purl.uniprot.org/annotation/VAR_032569|||http://purl.uniprot.org/annotation/VSP_025884|||http://purl.uniprot.org/annotation/VSP_025885|||http://purl.uniprot.org/annotation/VSP_044995
http://togogenome.org/gene/9606:ZNF93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35789|||http://purl.uniprot.org/uniprot/Q6NS90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 93                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047402|||http://purl.uniprot.org/annotation/VAR_052768|||http://purl.uniprot.org/annotation/VSP_016988|||http://purl.uniprot.org/annotation/VSP_016989
http://togogenome.org/gene/9606:REPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7D3|||http://purl.uniprot.org/uniprot/Q96D71                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||EH|||EH 1|||EH 2|||In NBIA7; primary fibroblasts from patients, who are compound heterozygous with E-113, show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface.|||In NBIA7; primary fibroblasts from patients, who are compound heterozygous with L-78, show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Interaction with RALBP1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||RalBP1-associated Eps domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073829|||http://purl.uniprot.org/annotation/VAR_080634|||http://purl.uniprot.org/annotation/VAR_080635|||http://purl.uniprot.org/annotation/VSP_007953|||http://purl.uniprot.org/annotation/VSP_007954|||http://purl.uniprot.org/annotation/VSP_007955
http://togogenome.org/gene/9606:GLRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35754                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutaredoxin|||Glutaredoxin-1|||N-acetylalanine|||N6-succinyllysine|||Redox-active|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141600|||http://purl.uniprot.org/annotation/VAR_049189
http://togogenome.org/gene/9606:GPR101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P66                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In PITA2.|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 101                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069601|||http://purl.uniprot.org/annotation/VAR_049398|||http://purl.uniprot.org/annotation/VAR_049399|||http://purl.uniprot.org/annotation/VAR_072691
http://togogenome.org/gene/9606:NUDT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBG1|||http://purl.uniprot.org/uniprot/A0A0C4DGJ4|||http://purl.uniprot.org/uniprot/Q9NZJ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Diphosphoinositol polyphosphate phosphohydrolase 2|||Diphosphoinositol polyphosphate phosphohydrolase NUDT4B|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||Nudix box|||Nudix hydrolase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057058|||http://purl.uniprot.org/annotation/PRO_0000444882|||http://purl.uniprot.org/annotation/VSP_014269|||http://purl.uniprot.org/annotation/VSP_014270
http://togogenome.org/gene/9606:MMRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8L6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Disordered|||EMI|||In a colorectal cancer sample; somatic mutation.|||Multimerin-2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007822|||http://purl.uniprot.org/annotation/VAR_019801|||http://purl.uniprot.org/annotation/VAR_019802|||http://purl.uniprot.org/annotation/VAR_036362|||http://purl.uniprot.org/annotation/VAR_053076|||http://purl.uniprot.org/annotation/VAR_053077
http://togogenome.org/gene/9606:SPESP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW49                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Sperm equatorial segment protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042707|||http://purl.uniprot.org/annotation/VAR_023738|||http://purl.uniprot.org/annotation/VAR_031430|||http://purl.uniprot.org/annotation/VAR_056994
http://togogenome.org/gene/9606:CPXCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N123                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  CPX chromosomal region candidate gene 1 protein|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305343|||http://purl.uniprot.org/annotation/VAR_035218|||http://purl.uniprot.org/annotation/VAR_035219
http://togogenome.org/gene/9606:TUBA1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1K5|||http://purl.uniprot.org/uniprot/F5H5D3|||http://purl.uniprot.org/uniprot/Q9BQE3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Site                                                                                  ^@                                                                                  3'-nitrotyrosine|||Detyrosinated tubulin alpha-1C chain|||Disordered|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Tubulin alpha-1C chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048112|||http://purl.uniprot.org/annotation/PRO_0000437394
http://togogenome.org/gene/9606:AP2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94973                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP-2 complex subunit alpha-2|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193732|||http://purl.uniprot.org/annotation/VSP_035762|||http://purl.uniprot.org/annotation/VSP_035763|||http://purl.uniprot.org/annotation/VSP_035764
http://togogenome.org/gene/9606:SEPTIN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5S0|||http://purl.uniprot.org/uniprot/Q9NVA2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||G1 motif|||G3 motif|||G4 motif|||High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Septin-11|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173542|||http://purl.uniprot.org/annotation/VSP_038320
http://togogenome.org/gene/9606:PCGF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35227                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In TPFS.|||Nuclear localization signal|||Phosphothreonine|||Polar residues|||Polycomb group RING finger protein 2|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055984|||http://purl.uniprot.org/annotation/VAR_082085|||http://purl.uniprot.org/annotation/VAR_082086
http://togogenome.org/gene/9606:ZNF267                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14586                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 267                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047494|||http://purl.uniprot.org/annotation/VAR_057414|||http://purl.uniprot.org/annotation/VAR_059907
http://togogenome.org/gene/9606:RETNLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ08                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interchain|||Resistin-like beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030345|||http://purl.uniprot.org/annotation/VAR_051791
http://togogenome.org/gene/9606:CTCF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFL0|||http://purl.uniprot.org/uniprot/P49711                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in an endometrial carcinoma sample; no effect on its nuclear localization; loss of its ability to inhibit cell proliferation; unknown pathological significance.|||Found in an endometrial carcinoma sample; no effect on its nuclear localization; no loss of its ability to inhibit cell proliferation; unknown pathological significance.|||Found in an endometrial carcinoma sample; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRD21.|||In a Wilms' tumor.|||In a breast tumor.|||In a prostate tumor.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcriptional repressor CTCF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047228|||http://purl.uniprot.org/annotation/VAR_013141|||http://purl.uniprot.org/annotation/VAR_013142|||http://purl.uniprot.org/annotation/VAR_013143|||http://purl.uniprot.org/annotation/VAR_013144|||http://purl.uniprot.org/annotation/VAR_070776|||http://purl.uniprot.org/annotation/VAR_079374|||http://purl.uniprot.org/annotation/VAR_079375|||http://purl.uniprot.org/annotation/VAR_079376|||http://purl.uniprot.org/annotation/VAR_079377|||http://purl.uniprot.org/annotation/VSP_045350
http://togogenome.org/gene/9606:UCHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09936|||http://purl.uniprot.org/uniprot/V9HW74                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  10000-fold decrease in enzymatic activity; no change in affinity for ubiquitin ethyl ester.|||2-fold increase in affinity for ubiquitin ethyl ester, slight reduction in enzymatic activity.|||6-fold decrease in affinity for ubiquitin ethyl ester; 97.5% decrease in enzymatic activity.|||Abolishes enzymatic activity.|||Almost complete loss of activity.|||Important for enzyme activity|||In PARK5; impaired enzymatic hydrolase activity; has about a 50% reduction in catalytic activity compared to wild-type protein.|||In SPG79A.|||In SPG79A; unknown pathological significance.|||In SPG79B; decreased protein abundance.|||In SPG79B; has decreased binding to ubiquitin and significantly decreased hydrolase activity compared to wild-type.|||In SPG79B; increased hydrolase activity; decreased protein abundance.|||Interaction with ubiquitin|||May be associated with reduced risk for sporadic Parkinson disease; it confers protection from oxidative stress when expressed at physiological levels in neuroblastoma cells and primary cortical neurons; loss of dimerization ability; impaired ligase activity.|||No effect on enzymatic parameters.|||Nucleophile|||Phosphoserine|||Proton donor|||Removed in mature form|||S-farnesyl cysteine|||Susceptible to oxidation|||Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site|||Ubiquitin carboxyl-terminal hydrolase isozyme L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211055|||http://purl.uniprot.org/annotation/PRO_0000414311|||http://purl.uniprot.org/annotation/VAR_015677|||http://purl.uniprot.org/annotation/VAR_015678|||http://purl.uniprot.org/annotation/VAR_070875|||http://purl.uniprot.org/annotation/VAR_078119|||http://purl.uniprot.org/annotation/VAR_078120|||http://purl.uniprot.org/annotation/VAR_087898|||http://purl.uniprot.org/annotation/VAR_087899|||http://purl.uniprot.org/annotation/VAR_087900|||http://purl.uniprot.org/annotation/VAR_087901|||http://purl.uniprot.org/annotation/VAR_087902
http://togogenome.org/gene/9606:TAF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15543                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Histone-fold|||In MRT60; impairs interaction with TAF11.|||Transcription initiation factor TFIID subunit 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118910|||http://purl.uniprot.org/annotation/VAR_079046|||http://purl.uniprot.org/annotation/VAR_079047
http://togogenome.org/gene/9606:CD84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIB8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of dimerization.|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphotyrosine|||Phosphotyrosine; by FES|||Phosphotyrosine; by LYN|||Reduced tyrosine phosphorylation and reduced binding of SH2D1B. Loss of phosphorylation and loss of binding of SH2D1A and SH2D1B; when associated with F-279.|||Reduced tyrosine phosphorylation, reduced binding of SH2D1B and loss of binding of SH2D1A.|||SLAM family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252029|||http://purl.uniprot.org/annotation/VSP_020848|||http://purl.uniprot.org/annotation/VSP_020849|||http://purl.uniprot.org/annotation/VSP_020850|||http://purl.uniprot.org/annotation/VSP_020851|||http://purl.uniprot.org/annotation/VSP_020852|||http://purl.uniprot.org/annotation/VSP_020853|||http://purl.uniprot.org/annotation/VSP_020854|||http://purl.uniprot.org/annotation/VSP_020855|||http://purl.uniprot.org/annotation/VSP_020856
http://togogenome.org/gene/9606:DNAJC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99615                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 7|||Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-409.|||Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-333 and A-409.|||In isoform 2.|||J|||N-acetylalanine|||Phosphoserine|||Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333.|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071058|||http://purl.uniprot.org/annotation/VSP_044279
http://togogenome.org/gene/9606:BRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7A8|||http://purl.uniprot.org/uniprot/P25440|||http://purl.uniprot.org/uniprot/X5CF57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Bromo|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 2|||Disordered|||In a gastric adenocarcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of homodimerization.|||N-acetylmethionine|||NET|||Nuclear localization signal|||Partial loss of homodimerization; when associated with A-154.|||Partial loss of homodimerization; when associated with A-182.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211180|||http://purl.uniprot.org/annotation/VAR_022132|||http://purl.uniprot.org/annotation/VAR_029300|||http://purl.uniprot.org/annotation/VAR_029301|||http://purl.uniprot.org/annotation/VAR_041904|||http://purl.uniprot.org/annotation/VAR_041905|||http://purl.uniprot.org/annotation/VAR_041906|||http://purl.uniprot.org/annotation/VAR_041907|||http://purl.uniprot.org/annotation/VAR_041908|||http://purl.uniprot.org/annotation/VAR_041909|||http://purl.uniprot.org/annotation/VAR_041910|||http://purl.uniprot.org/annotation/VAR_041911|||http://purl.uniprot.org/annotation/VAR_041912|||http://purl.uniprot.org/annotation/VSP_022600|||http://purl.uniprot.org/annotation/VSP_055028|||http://purl.uniprot.org/annotation/VSP_055029
http://togogenome.org/gene/9606:LMX1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLH2|||http://purl.uniprot.org/uniprot/O60663|||http://purl.uniprot.org/uniprot/Q6ISE0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In FSGS10.|||In FSGS10; decreased transcriptional activity.|||In NPS.|||In isoform 2 and isoform 3.|||In isoform 3.|||LIM homeobox transcription factor 1-beta|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||Loss of transcriptional activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075828|||http://purl.uniprot.org/annotation/VAR_004198|||http://purl.uniprot.org/annotation/VAR_004199|||http://purl.uniprot.org/annotation/VAR_004200|||http://purl.uniprot.org/annotation/VAR_004201|||http://purl.uniprot.org/annotation/VAR_004202|||http://purl.uniprot.org/annotation/VAR_004203|||http://purl.uniprot.org/annotation/VAR_004204|||http://purl.uniprot.org/annotation/VAR_004205|||http://purl.uniprot.org/annotation/VAR_015190|||http://purl.uniprot.org/annotation/VAR_015191|||http://purl.uniprot.org/annotation/VAR_015192|||http://purl.uniprot.org/annotation/VAR_015193|||http://purl.uniprot.org/annotation/VAR_015194|||http://purl.uniprot.org/annotation/VAR_015195|||http://purl.uniprot.org/annotation/VAR_015196|||http://purl.uniprot.org/annotation/VAR_015197|||http://purl.uniprot.org/annotation/VAR_015198|||http://purl.uniprot.org/annotation/VAR_015201|||http://purl.uniprot.org/annotation/VAR_015202|||http://purl.uniprot.org/annotation/VAR_015203|||http://purl.uniprot.org/annotation/VAR_015204|||http://purl.uniprot.org/annotation/VAR_015205|||http://purl.uniprot.org/annotation/VAR_015206|||http://purl.uniprot.org/annotation/VAR_015207|||http://purl.uniprot.org/annotation/VAR_015208|||http://purl.uniprot.org/annotation/VAR_015209|||http://purl.uniprot.org/annotation/VAR_015210|||http://purl.uniprot.org/annotation/VAR_015211|||http://purl.uniprot.org/annotation/VAR_015212|||http://purl.uniprot.org/annotation/VAR_015213|||http://purl.uniprot.org/annotation/VAR_047755|||http://purl.uniprot.org/annotation/VAR_085231|||http://purl.uniprot.org/annotation/VAR_085232|||http://purl.uniprot.org/annotation/VSP_003113|||http://purl.uniprot.org/annotation/VSP_046472
http://togogenome.org/gene/9606:RNF115                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4L5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF115|||Loss of autoubiquitination.|||Loss of autoubiquitination; when associated with R-26.|||Loss of autoubiquitination; when associated with R-32.|||N-acetylalanine|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056314|||http://purl.uniprot.org/annotation/VAR_052105
http://togogenome.org/gene/9606:RBM15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate; by PRMT1|||Basic and acidic residues|||Breakpoint for translocation to form RBM15-MKL1|||Decreased methylation by PRMT1, leading to decreased ubiquitination by CNOT4.|||Decreased, but not abolished methylation by PRMT1.|||Disordered|||Disrupts interaction with SETD1B.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Omega-N-methylarginine; alternate; by PRMT1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding protein 15|||RRM 1|||RRM 2|||RRM 3|||SPOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081777|||http://purl.uniprot.org/annotation/VSP_005811|||http://purl.uniprot.org/annotation/VSP_005812|||http://purl.uniprot.org/annotation/VSP_053877
http://togogenome.org/gene/9606:NME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTW7|||http://purl.uniprot.org/uniprot/P15531                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a neuroblastoma sample; increased motility of carcinoma cells.|||In isoform 2.|||Increased motility of carcinoma cells.|||Limited increase in motility of carcinoma cells.|||Loss of activity.|||Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells.|||No loss of activity or substrate binding.|||Nucleoside diphosphate kinase A|||Nucleoside diphosphate kinase-like|||Phosphoserine|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137114|||http://purl.uniprot.org/annotation/VAR_004625|||http://purl.uniprot.org/annotation/VSP_036707
http://togogenome.org/gene/9606:ANGPTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5C1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  ANGPTL3(17-221)|||ANGPTL3(17-224)|||Abolishes effect on plasma triglyceride level; when associated with 62-I-N-63.|||Abolishes effect on plasma triglyceride level; when associated with N-65.|||Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-63.|||Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-65.|||Abolishes protein secretion; associated with low plasma triglyceride level.|||Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-221 and S-224.|||Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-221 and S-235.|||Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-224 and S-235.|||Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with S-221; S-224 and S-235.|||Angiopoietin-related protein 3|||Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro.|||Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein secretion.|||Common allele in African americans; associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein folding.|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc) threonine|||Required for inhibition of LPL lipase activity|||Sufficient to inhibit LIPG/EL phospholipase activity|||Sufficient to inhibit LPL lipase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009122|||http://purl.uniprot.org/annotation/PRO_0000435903|||http://purl.uniprot.org/annotation/PRO_0000435904|||http://purl.uniprot.org/annotation/VAR_049071|||http://purl.uniprot.org/annotation/VAR_067283|||http://purl.uniprot.org/annotation/VAR_075670|||http://purl.uniprot.org/annotation/VAR_075671|||http://purl.uniprot.org/annotation/VAR_075672|||http://purl.uniprot.org/annotation/VAR_075673|||http://purl.uniprot.org/annotation/VAR_075674|||http://purl.uniprot.org/annotation/VAR_075675|||http://purl.uniprot.org/annotation/VAR_075676|||http://purl.uniprot.org/annotation/VAR_075677|||http://purl.uniprot.org/annotation/VAR_075678|||http://purl.uniprot.org/annotation/VAR_075679|||http://purl.uniprot.org/annotation/VAR_075680
http://togogenome.org/gene/9606:IQCJ-SCHIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU38                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||IQ|||IQCJ-SCHIP1 readthrough transcript protein|||In isoform IQCJ-SCHIP1-2.|||Phosphoserine|||Polar residues|||Required for interaction with ankyrins                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000442334|||http://purl.uniprot.org/annotation/VSP_059227
http://togogenome.org/gene/9606:BTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3I5|||http://purl.uniprot.org/uniprot/A0A0S2Z437|||http://purl.uniprot.org/uniprot/P35070                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Betacellulin|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Probetacellulin|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007490|||http://purl.uniprot.org/annotation/PRO_0000007491|||http://purl.uniprot.org/annotation/PRO_0000300685|||http://purl.uniprot.org/annotation/PRO_5006608195|||http://purl.uniprot.org/annotation/PRO_5014239327|||http://purl.uniprot.org/annotation/VAR_029307|||http://purl.uniprot.org/annotation/VAR_029308|||http://purl.uniprot.org/annotation/VAR_061151
http://togogenome.org/gene/9606:SPTLC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15270                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates.|||Decreased catalytic activity with L-serine and palmitoyl-CoA as substrates. Does not affect the negative regulation by OMRDL3 and ceramides.|||Helical|||In HSAN1C; complete loss of normal activity as measured by lack of formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine.|||In HSAN1C; late onset; slightly increased activity with L-serine as substrate; highly increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine.|||In HSAN1C; partial loss of normal activity as measured by reduced formation of sphinganine; affects enzymatic affinity resulting in the accumulation of the alternative metabolite 1-deoxy-sphinganine.|||In HSAN1C; reduced activity with L-serine as substrate; increased activity toward L-alanine resulting in the accumulation of 1-deoxy-sphinganine.|||Loss of catalytic activity with L-serine and palmitoyl-CoA as substrates.|||Loss of negative regulation by OMRDL3 and ceramides.|||N6-(pyridoxal phosphate)lysine|||Reduces the dimerization propensity with SPTLC1; reduces the dimerization propensity with SPTLC1; when associated with A-305. Does not impair enzymatic activity; when associated with A-304 and A-305.|||Reduces the dimerization propensity with SPTLC1; when associated with A-302 and A-304. Does not impair enzymatic activity; when associated with A-302 and A-304.|||Serine palmitoyltransferase 2|||Some decrease in catalytic activity with L-serine and palmitoyl-CoA as substrates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163858|||http://purl.uniprot.org/annotation/VAR_064798|||http://purl.uniprot.org/annotation/VAR_064799|||http://purl.uniprot.org/annotation/VAR_064800|||http://purl.uniprot.org/annotation/VAR_069525|||http://purl.uniprot.org/annotation/VAR_081286
http://togogenome.org/gene/9606:TMEM205                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW68                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 205                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317501
http://togogenome.org/gene/9606:ACADL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28330                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Long-chain specific acyl-CoA dehydrogenase, mitochondrial|||Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000509|||http://purl.uniprot.org/annotation/VAR_000328|||http://purl.uniprot.org/annotation/VAR_000329
http://togogenome.org/gene/9606:SPIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56A73                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Histone H3K4me3 and H3R8me2a binding|||Spindlin-4|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313794
http://togogenome.org/gene/9606:USP35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2H5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of catalytic activity.|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080665|||http://purl.uniprot.org/annotation/VAR_057042|||http://purl.uniprot.org/annotation/VSP_040291
http://togogenome.org/gene/9606:FBXO8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5D1|||http://purl.uniprot.org/uniprot/Q8IXA8|||http://purl.uniprot.org/uniprot/Q9NRD0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 8|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120218|||http://purl.uniprot.org/annotation/VAR_036157|||http://purl.uniprot.org/annotation/VAR_071118|||http://purl.uniprot.org/annotation/VAR_071119|||http://purl.uniprot.org/annotation/VSP_055885
http://togogenome.org/gene/9606:KCND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK17                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In BRGDA9; unknown pathological significance; does not affect the electrophysiological properties of the channel.|||In BRGDA9; unknown pathological significance; gain of function mutation.|||In SCA19.|||In SCA19; loss of channel activity.|||In SCA19; results in reduced channel activity consistent with impaired cell surface expression of the mutant protein.|||In SCA19; unknown pathological significance; causes reduced channel activity.|||In SCA19; unknown pathological significance; results in impaired cell surface expression.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with KCNIP2|||Mediates dendritic targeting|||Phosphoserine|||Phosphoserine; by CaMK2D|||Phosphothreonine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily D member 3|||Pro residues|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054068|||http://purl.uniprot.org/annotation/VAR_035775|||http://purl.uniprot.org/annotation/VAR_067694|||http://purl.uniprot.org/annotation/VAR_067695|||http://purl.uniprot.org/annotation/VAR_067696|||http://purl.uniprot.org/annotation/VAR_070785|||http://purl.uniprot.org/annotation/VAR_070786|||http://purl.uniprot.org/annotation/VAR_070787|||http://purl.uniprot.org/annotation/VAR_070788|||http://purl.uniprot.org/annotation/VAR_070789|||http://purl.uniprot.org/annotation/VAR_070790|||http://purl.uniprot.org/annotation/VAR_070791|||http://purl.uniprot.org/annotation/VAR_073831|||http://purl.uniprot.org/annotation/VAR_079709|||http://purl.uniprot.org/annotation/VSP_008826
http://togogenome.org/gene/9606:FKBP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PAR0|||http://purl.uniprot.org/uniprot/Q9NYL4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025519|||http://purl.uniprot.org/annotation/VSP_043037
http://togogenome.org/gene/9606:CDC25C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX61|||http://purl.uniprot.org/uniprot/P30307                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MARK3. Reduces phosphorylation of S-216 by MARK3.|||Disordered|||Facilitates nuclear exclusion.|||HIV-1 Vpr binding site|||In isoform 2 and isoform 5.|||In isoform 4 and isoform 5.|||Loss of phosphorylation. Severely impairs PLK1-binding.|||M-phase inducer phosphatase 3|||Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus.|||N-acetylserine|||No effect on HIV-1 Vpr binding.|||No effect on interaction with MARK3.|||No effect on interaction with MARK3. Abolishes phosphorylation by MARK3.|||Partial loss of HIV-1 Vpr binding.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CHEK1, CHEK2, BRSK1, MAPK14 AND MARK3|||Phosphoserine; by PLK3|||Phosphothreonine|||Polar residues|||Reduces phosphorylation by MARK3 and CHEK1.|||Removed|||Rhodanese                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198647|||http://purl.uniprot.org/annotation/VAR_020146|||http://purl.uniprot.org/annotation/VAR_027922|||http://purl.uniprot.org/annotation/VAR_027923|||http://purl.uniprot.org/annotation/VAR_027924|||http://purl.uniprot.org/annotation/VSP_000863|||http://purl.uniprot.org/annotation/VSP_000864
http://togogenome.org/gene/9606:H3C12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:TAMM41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BW9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In COXPD56; unknown pathological significance; compared to wild-type, only partly rescues the growth defect in deficient yeast, when tested on respiratory media at 36 degrees Celsius.|||In COXPD56; unknown pathological significance; contrary to wild-type, unable to complement the growth defect in deficient yeast.|||In isoform 2.|||In isoform 3.|||Phosphatidate cytidylyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248354|||http://purl.uniprot.org/annotation/VAR_027276|||http://purl.uniprot.org/annotation/VAR_053649|||http://purl.uniprot.org/annotation/VAR_087807|||http://purl.uniprot.org/annotation/VAR_087808|||http://purl.uniprot.org/annotation/VAR_087809|||http://purl.uniprot.org/annotation/VSP_053905|||http://purl.uniprot.org/annotation/VSP_053906|||http://purl.uniprot.org/annotation/VSP_055724|||http://purl.uniprot.org/annotation/VSP_055725
http://togogenome.org/gene/9606:CYP4A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02928                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Associated with hypertension; significantly reduced arachidonic acid and lauric acid metabolizing activity.|||Cytochrome P450 4A11|||In CYP4A11V.|||In isoform 2.|||Loss of activity.|||Loss of covalent heme binding.|||Phosphoserine|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003579|||http://purl.uniprot.org/annotation/PRO_0000003580|||http://purl.uniprot.org/annotation/VAR_001257|||http://purl.uniprot.org/annotation/VAR_019160|||http://purl.uniprot.org/annotation/VAR_044377|||http://purl.uniprot.org/annotation/VAR_048452|||http://purl.uniprot.org/annotation/VSP_034595
http://togogenome.org/gene/9606:LMF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Lipase maturation factor 2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324510|||http://purl.uniprot.org/annotation/VAR_039803|||http://purl.uniprot.org/annotation/VAR_039804|||http://purl.uniprot.org/annotation/VSP_032254|||http://purl.uniprot.org/annotation/VSP_032255
http://togogenome.org/gene/9606:FTH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02794                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Ferritin heavy chain|||Ferritin heavy chain, N-terminally processed|||Ferritin-like diiron|||N-acetylmethionine|||N-acetylthreonine; in Ferritin heavy chain, N-terminally processed|||No effect on iron binding but the oxidation rate is severely reduced; when associated with Q-87.|||Phosphoserine|||Reduces iron binding and oxidation rate; when associated with A-28. No effect on iron binding but the oxidation rate is severely reduced; when associated with A-108.|||Reduces iron binding and oxidation rate; when associated with Q-87.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201048|||http://purl.uniprot.org/annotation/PRO_0000424472
http://togogenome.org/gene/9606:PIK3C2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUF7|||http://purl.uniprot.org/uniprot/O00750|||http://purl.uniprot.org/uniprot/Q4LE65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Activation loop|||C2|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||Interaction with GRB2|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088798
http://togogenome.org/gene/9606:DDX53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TM3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  DEAD box|||Found in a renal cell carcinoma case; somatic mutation.|||Helicase ATP-binding|||Helicase C-terminal|||KH|||Probable ATP-dependent RNA helicase DDX53|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054973|||http://purl.uniprot.org/annotation/VAR_052168|||http://purl.uniprot.org/annotation/VAR_052169|||http://purl.uniprot.org/annotation/VAR_052170|||http://purl.uniprot.org/annotation/VAR_064707
http://togogenome.org/gene/9606:CXXC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0U4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CXXC-type|||CXXC-type zinc finger protein 1|||Complete loss of DNA binding activity. No effect on localization in nuclear speckles.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079743|||http://purl.uniprot.org/annotation/VSP_040132
http://togogenome.org/gene/9606:ENTPD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQZ7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 7|||Helical|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274419|||http://purl.uniprot.org/annotation/VAR_030287
http://togogenome.org/gene/9606:ZNF680                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEM1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 680                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234000|||http://purl.uniprot.org/annotation/VAR_027892|||http://purl.uniprot.org/annotation/VAR_027893|||http://purl.uniprot.org/annotation/VAR_027894|||http://purl.uniprot.org/annotation/VSP_043114|||http://purl.uniprot.org/annotation/VSP_043115
http://togogenome.org/gene/9606:KCNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95069|||http://purl.uniprot.org/uniprot/Q6ZW95|||http://purl.uniprot.org/uniprot/U3N6F0|||http://purl.uniprot.org/uniprot/U3N834                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Essential for chloroform and halothane sensitivity|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interchain|||Mimics non-phosphorylated state and has no effect on leak channel activity.|||N-linked (GlcNAc...) asparagine|||Phosphomimetic mutant which causes switch to voltage-dependent outward rectifier channel activity.|||Phosphoserine; by PKA|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel|||Potassium channel subfamily K member 2|||Required for basal channel activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101742|||http://purl.uniprot.org/annotation/VSP_024428|||http://purl.uniprot.org/annotation/VSP_024429|||http://purl.uniprot.org/annotation/VSP_047567|||http://purl.uniprot.org/annotation/VSP_047568
http://togogenome.org/gene/9606:SYT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Helical|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Synaptotagmin-9|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183962|||http://purl.uniprot.org/annotation/VAR_036390|||http://purl.uniprot.org/annotation/VAR_065760|||http://purl.uniprot.org/annotation/VAR_065761|||http://purl.uniprot.org/annotation/VAR_065762
http://togogenome.org/gene/9606:CYB561D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQS1|||http://purl.uniprot.org/uniprot/Q8N8Q1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b561|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lumenal|||Probable transmembrane reductase CYB561D1|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000151034|||http://purl.uniprot.org/annotation/VSP_038649|||http://purl.uniprot.org/annotation/VSP_038650|||http://purl.uniprot.org/annotation/VSP_041162|||http://purl.uniprot.org/annotation/VSP_046985|||http://purl.uniprot.org/annotation/VSP_046986
http://togogenome.org/gene/9606:NMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30419                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished glycine- and lysine-myristoyltransferase activities.|||Disordered|||Glycylpeptide N-tetradecanoyltransferase 1|||In isoform Short.|||Phosphoserine|||Reduced activity.|||Reduced glycine N-myristoyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064221|||http://purl.uniprot.org/annotation/VAR_050286|||http://purl.uniprot.org/annotation/VSP_003570
http://togogenome.org/gene/9606:PDCD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IUD7|||http://purl.uniprot.org/uniprot/Q14690                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||N-acetylalanine|||Phosphoserine|||Protein RRP5 homolog|||Removed|||S1 motif|||S1 motif 1|||S1 motif 10|||S1 motif 11|||S1 motif 12|||S1 motif 2|||S1 motif 3|||S1 motif 4|||S1 motif 5|||S1 motif 6|||S1 motif 7|||S1 motif 8|||S1 motif 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205762|||http://purl.uniprot.org/annotation/VAR_014930|||http://purl.uniprot.org/annotation/VAR_031669|||http://purl.uniprot.org/annotation/VAR_031670|||http://purl.uniprot.org/annotation/VAR_054485|||http://purl.uniprot.org/annotation/VAR_054486|||http://purl.uniprot.org/annotation/VAR_054487|||http://purl.uniprot.org/annotation/VAR_076436
http://togogenome.org/gene/9606:SMG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0W8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In NEDITPO; unknown pathological significance.|||In isoform 2.|||N-acetylserine|||Nonsense-mediated mRNA decay factor SMG9|||Phosphoserine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289163|||http://purl.uniprot.org/annotation/VAR_087655|||http://purl.uniprot.org/annotation/VSP_025946
http://togogenome.org/gene/9606:KIF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Kinesin motor|||Kinesin-like protein KIF19|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278245|||http://purl.uniprot.org/annotation/VAR_030719|||http://purl.uniprot.org/annotation/VAR_049703|||http://purl.uniprot.org/annotation/VAR_059371|||http://purl.uniprot.org/annotation/VAR_061283|||http://purl.uniprot.org/annotation/VSP_023207|||http://purl.uniprot.org/annotation/VSP_023208|||http://purl.uniprot.org/annotation/VSP_023209
http://togogenome.org/gene/9606:DLG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4H2|||http://purl.uniprot.org/uniprot/B7Z647|||http://purl.uniprot.org/uniprot/B9EGL1|||http://purl.uniprot.org/uniprot/P78352                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disks large homolog 4|||Disordered|||Guanylate kinase-like|||In MRD62.|||In isoform 2.|||In isoform 3.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094560|||http://purl.uniprot.org/annotation/PRO_5014300259|||http://purl.uniprot.org/annotation/VAR_083773|||http://purl.uniprot.org/annotation/VAR_083774|||http://purl.uniprot.org/annotation/VSP_014929|||http://purl.uniprot.org/annotation/VSP_047247
http://togogenome.org/gene/9606:YJU2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1U2|||http://purl.uniprot.org/uniprot/P13994                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||Probable splicing factor YJU2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064401|||http://purl.uniprot.org/annotation/VAR_053854|||http://purl.uniprot.org/annotation/VAR_053855
http://togogenome.org/gene/9606:BIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RHU4|||http://purl.uniprot.org/uniprot/Q9NQY0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BAR|||Basic and acidic residues|||Bridging integrator 3|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192955|||http://purl.uniprot.org/annotation/VSP_013465
http://togogenome.org/gene/9606:GLI4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10075                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger protein GLI4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047267|||http://purl.uniprot.org/annotation/VAR_052734
http://togogenome.org/gene/9606:RGPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||Phosphothreonine|||Polar residues|||RANBP2-like and GRIP domain-containing protein 1|||RanBD1 1|||RanBD1 2|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204919
http://togogenome.org/gene/9606:APOO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUR5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||MICOS complex subunit MIC26|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254646|||http://purl.uniprot.org/annotation/VSP_023333
http://togogenome.org/gene/9606:B4GALT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60909                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080533|||http://purl.uniprot.org/annotation/VAR_020487|||http://purl.uniprot.org/annotation/VAR_054021|||http://purl.uniprot.org/annotation/VSP_014103|||http://purl.uniprot.org/annotation/VSP_014104|||http://purl.uniprot.org/annotation/VSP_043010
http://togogenome.org/gene/9606:KRT33B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14525                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha3-II|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063689
http://togogenome.org/gene/9606:MUC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3S8TMF2|||http://purl.uniprot.org/uniprot/Q02817                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  1|||10A|||10B|||11A|||11B|||12|||13|||14|||15|||16|||2|||3|||4|||5|||6|||7A|||7B|||8A|||8B|||9A|||9B|||Approximate repeats|||CTCK|||Cleavage; by autolysis; in vitro|||Decreased binding to Cu(1+) without affecting binding to Cu(2+). Abolished binding to Cu(1+); when associated with L-146 and L-154.|||Decreased binding to Cu(1+) without affecting binding to Cu(2+). Abolished binding to Cu(1+); when associated with L-146 and V-326.|||Decreased binding to Cu(1+) without affecting binding to Cu(2+). Abolished binding to Cu(1+); when associated with L-154 and V-326.|||Decreased binding to Cu(2+).|||Disordered|||Does not abolish homodimerization. Does not abolish ability to form filaments; when associated with A-1130.|||Impaired formation of intermolecular disulfide bonds; inducing a mixture of monomers and homodimers. Does not abolish ability to form filaments; when associated with A-1088.|||Interchain|||Mucin-2|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc) serine|||O-linked (GalNAc) threonine|||Phosphoserine|||Polar residues|||Pro residues|||Slightly Decreased binding to Cu(2+).|||TIL|||VWFC|||VWFC 1|||VWFC 2|||VWFD|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019281|||http://purl.uniprot.org/annotation/PRO_5019111801|||http://purl.uniprot.org/annotation/VAR_056582|||http://purl.uniprot.org/annotation/VAR_056583|||http://purl.uniprot.org/annotation/VAR_056584|||http://purl.uniprot.org/annotation/VAR_059531|||http://purl.uniprot.org/annotation/VAR_059532|||http://purl.uniprot.org/annotation/VAR_059533|||http://purl.uniprot.org/annotation/VAR_059534|||http://purl.uniprot.org/annotation/VAR_059535|||http://purl.uniprot.org/annotation/VAR_059536|||http://purl.uniprot.org/annotation/VAR_059537|||http://purl.uniprot.org/annotation/VAR_061487
http://togogenome.org/gene/9606:HNRNPA0                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13151                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein A0|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081826
http://togogenome.org/gene/9606:UBIAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Z9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In SCCD.|||In SCCD; does not affect coenzyme Q10 synthesis.|||In SCCD; reduced menaquinone-4 (MK-4) synthesis.|||In SCCD; reduced menaquinone-4 (MK-4) synthesis; does not affect coenzyme Q10 synthesis.|||In isoform 2.|||N-acetylalanine|||Removed|||UbiA prenyltransferase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242627|||http://purl.uniprot.org/annotation/VAR_043713|||http://purl.uniprot.org/annotation/VAR_043714|||http://purl.uniprot.org/annotation/VAR_043715|||http://purl.uniprot.org/annotation/VAR_043716|||http://purl.uniprot.org/annotation/VAR_043717|||http://purl.uniprot.org/annotation/VAR_043718|||http://purl.uniprot.org/annotation/VAR_043719|||http://purl.uniprot.org/annotation/VAR_043720|||http://purl.uniprot.org/annotation/VAR_043721|||http://purl.uniprot.org/annotation/VAR_043722|||http://purl.uniprot.org/annotation/VAR_043723|||http://purl.uniprot.org/annotation/VAR_043724|||http://purl.uniprot.org/annotation/VAR_064337|||http://purl.uniprot.org/annotation/VAR_064338|||http://purl.uniprot.org/annotation/VAR_064339|||http://purl.uniprot.org/annotation/VAR_064340|||http://purl.uniprot.org/annotation/VAR_064341|||http://purl.uniprot.org/annotation/VAR_064342|||http://purl.uniprot.org/annotation/VAR_064343|||http://purl.uniprot.org/annotation/VAR_069267|||http://purl.uniprot.org/annotation/VSP_019455|||http://purl.uniprot.org/annotation/VSP_019456
http://togogenome.org/gene/9606:FNDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4ZHG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type III domain-containing protein 1|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284831|||http://purl.uniprot.org/annotation/VAR_031826|||http://purl.uniprot.org/annotation/VAR_031827|||http://purl.uniprot.org/annotation/VAR_031828|||http://purl.uniprot.org/annotation/VAR_031829|||http://purl.uniprot.org/annotation/VAR_031830|||http://purl.uniprot.org/annotation/VAR_031831|||http://purl.uniprot.org/annotation/VAR_031832|||http://purl.uniprot.org/annotation/VAR_031833|||http://purl.uniprot.org/annotation/VAR_063225|||http://purl.uniprot.org/annotation/VSP_024663
http://togogenome.org/gene/9606:EVX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03828                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox even-skipped homolog protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048872
http://togogenome.org/gene/9606:TEX22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J3V5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Testis-expressed protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410917
http://togogenome.org/gene/9606:GPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3TZU2|||http://purl.uniprot.org/uniprot/P06744                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased enzymatic activity.|||Disordered|||Glucose-6-phosphate isomerase|||In HA-GPID.|||In HA-GPID; GPIBari and Mola.|||In HA-GPID; GPIElyria.|||In HA-GPID; GPIFukuoka and Kinki.|||In HA-GPID; GPIIwate.|||In HA-GPID; GPIKinki.|||In HA-GPID; GPIMatsumoto.|||In HA-GPID; GPIMount Scopus.|||In HA-GPID; GPINarita and Morcone.|||In HA-GPID; GPISarcina.|||In HA-GPID; Strongly reduced glucose-6-phosphate isomerase activity.|||In HA-GPID; severe form with neurological deficits; GPIHomburg.|||In HA-GPID; severe form; GPICalden.|||In HA-GPID; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Proton donor|||Removed|||Retained full enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180537|||http://purl.uniprot.org/annotation/VAR_002516|||http://purl.uniprot.org/annotation/VAR_002517|||http://purl.uniprot.org/annotation/VAR_002518|||http://purl.uniprot.org/annotation/VAR_002519|||http://purl.uniprot.org/annotation/VAR_002520|||http://purl.uniprot.org/annotation/VAR_002521|||http://purl.uniprot.org/annotation/VAR_002522|||http://purl.uniprot.org/annotation/VAR_002523|||http://purl.uniprot.org/annotation/VAR_002524|||http://purl.uniprot.org/annotation/VAR_002525|||http://purl.uniprot.org/annotation/VAR_002526|||http://purl.uniprot.org/annotation/VAR_002527|||http://purl.uniprot.org/annotation/VAR_002528|||http://purl.uniprot.org/annotation/VAR_002529|||http://purl.uniprot.org/annotation/VAR_002530|||http://purl.uniprot.org/annotation/VAR_002531|||http://purl.uniprot.org/annotation/VAR_002532|||http://purl.uniprot.org/annotation/VAR_002533|||http://purl.uniprot.org/annotation/VAR_002534|||http://purl.uniprot.org/annotation/VAR_002535|||http://purl.uniprot.org/annotation/VAR_002536|||http://purl.uniprot.org/annotation/VAR_002537|||http://purl.uniprot.org/annotation/VAR_002538|||http://purl.uniprot.org/annotation/VAR_018816|||http://purl.uniprot.org/annotation/VAR_033943|||http://purl.uniprot.org/annotation/VAR_082092|||http://purl.uniprot.org/annotation/VAR_082093|||http://purl.uniprot.org/annotation/VSP_043475|||http://purl.uniprot.org/annotation/VSP_043476
http://togogenome.org/gene/9606:RBM19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4C8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Probable RNA-binding protein 19|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||RRM 5|||RRM 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081781|||http://purl.uniprot.org/annotation/VAR_023114|||http://purl.uniprot.org/annotation/VAR_023115|||http://purl.uniprot.org/annotation/VAR_023116|||http://purl.uniprot.org/annotation/VAR_023117|||http://purl.uniprot.org/annotation/VAR_057246|||http://purl.uniprot.org/annotation/VAR_059822
http://togogenome.org/gene/9606:NREP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16612                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Accelerates protein degradation and reduces glioma cell migration.|||Basic and acidic residues|||Disordered|||In isoform 2.|||Neuronal regeneration-related protein|||Phosphoserine|||Reduces protein degradation and induces glioma cell migration.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057937|||http://purl.uniprot.org/annotation/VAR_051238|||http://purl.uniprot.org/annotation/VSP_043013
http://togogenome.org/gene/9606:IMPG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYL3|||http://purl.uniprot.org/uniprot/Q17R60                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like|||Found in a patient with vitelliform macular dystrophy; unknown pathological significance.|||Heparin- and hyaluronan-binding|||In RP91.|||In RP91; unknown pathological significance.|||In VMD4.|||In VMD4; unknown pathological significance.|||In isoform 2.|||Interphotoreceptor matrix proteoglycan 1|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||SEA|||SEA 1|||SEA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252238|||http://purl.uniprot.org/annotation/PRO_5001832091|||http://purl.uniprot.org/annotation/VAR_027793|||http://purl.uniprot.org/annotation/VAR_027794|||http://purl.uniprot.org/annotation/VAR_051069|||http://purl.uniprot.org/annotation/VAR_051070|||http://purl.uniprot.org/annotation/VAR_051071|||http://purl.uniprot.org/annotation/VAR_051072|||http://purl.uniprot.org/annotation/VAR_072668|||http://purl.uniprot.org/annotation/VAR_072669|||http://purl.uniprot.org/annotation/VAR_072670|||http://purl.uniprot.org/annotation/VAR_082192|||http://purl.uniprot.org/annotation/VAR_086246|||http://purl.uniprot.org/annotation/VAR_086247|||http://purl.uniprot.org/annotation/VSP_055981|||http://purl.uniprot.org/annotation/VSP_055982|||http://purl.uniprot.org/annotation/VSP_055983
http://togogenome.org/gene/9606:MEMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y316                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ERBB2.|||Diminishes interaction with ERBB2.|||In isoform 2.|||In isoform 3.|||Phosphotyrosine|||Protein MEMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134394|||http://purl.uniprot.org/annotation/VSP_041092|||http://purl.uniprot.org/annotation/VSP_047693
http://togogenome.org/gene/9606:SDF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IBU4|||http://purl.uniprot.org/uniprot/Q99470                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  MIR|||MIR 1|||MIR 2|||MIR 3|||Stromal cell-derived factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031955|||http://purl.uniprot.org/annotation/PRO_5014310485|||http://purl.uniprot.org/annotation/VAR_051913
http://togogenome.org/gene/9606:PAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504Q3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Exonuclease|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Linker|||Loss of exonuclease activity.|||PAN2-PAN3 deadenylation complex catalytic subunit PAN2|||Phosphoserine|||USP|||WD 1|||WD 2|||WD 3|||WD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280521|||http://purl.uniprot.org/annotation/VAR_031162|||http://purl.uniprot.org/annotation/VAR_031163|||http://purl.uniprot.org/annotation/VAR_036359|||http://purl.uniprot.org/annotation/VSP_023748|||http://purl.uniprot.org/annotation/VSP_023749
http://togogenome.org/gene/9606:ZNF548                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEK5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 548                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242160|||http://purl.uniprot.org/annotation/VAR_026845|||http://purl.uniprot.org/annotation/VAR_026846|||http://purl.uniprot.org/annotation/VSP_019453
http://togogenome.org/gene/9606:TMEM143                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMT0|||http://purl.uniprot.org/uniprot/B4DPF8|||http://purl.uniprot.org/uniprot/Q96AN5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Transmembrane protein 143                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285958|||http://purl.uniprot.org/annotation/VAR_032058|||http://purl.uniprot.org/annotation/VSP_024930|||http://purl.uniprot.org/annotation/VSP_024931|||http://purl.uniprot.org/annotation/VSP_024932
http://togogenome.org/gene/9606:DUSP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13202                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dual specificity protein phosphatase 8|||Phosphocysteine intermediate|||Pro residues|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094810
http://togogenome.org/gene/9606:PATE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C8F1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  Prostate and testis expressed protein 4|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000354971
http://togogenome.org/gene/9606:LRRC37A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QTJ5|||http://purl.uniprot.org/uniprot/O60309                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRC37A/B like protein 1 C-terminal|||Leucine-rich repeat-containing protein 37A3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076244|||http://purl.uniprot.org/annotation/VAR_051088|||http://purl.uniprot.org/annotation/VAR_061672
http://togogenome.org/gene/9606:KRTAP10-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60369                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||18 X 5 AA repeats of C-C-X(3)|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185211|||http://purl.uniprot.org/annotation/VAR_047850|||http://purl.uniprot.org/annotation/VAR_047851
http://togogenome.org/gene/9606:RAB22A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL26                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Constitutive GTPase activity. Impairs normal protein trafficking through early endosomes.|||Disordered|||Effector region|||Loss of GTPase activity.|||Ras-related protein Rab-22A|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121209
http://togogenome.org/gene/9606:PRSS56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW18                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Disordered|||In MCOP6.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 56                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000408091|||http://purl.uniprot.org/annotation/VAR_065076|||http://purl.uniprot.org/annotation/VAR_065077|||http://purl.uniprot.org/annotation/VAR_069226|||http://purl.uniprot.org/annotation/VAR_069227|||http://purl.uniprot.org/annotation/VAR_069228|||http://purl.uniprot.org/annotation/VAR_069229|||http://purl.uniprot.org/annotation/VAR_069230
http://togogenome.org/gene/9606:MLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12872                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Motilin|||Motilin-associated peptide|||Promotilin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019184|||http://purl.uniprot.org/annotation/PRO_0000019185|||http://purl.uniprot.org/annotation/PRO_0000342171|||http://purl.uniprot.org/annotation/VAR_020372|||http://purl.uniprot.org/annotation/VSP_045484|||http://purl.uniprot.org/annotation/VSP_047653
http://togogenome.org/gene/9606:BMP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K694|||http://purl.uniprot.org/uniprot/M9VUD0|||http://purl.uniprot.org/uniprot/P22003                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Bone morphogenetic protein 5|||Disordered|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Polar residues|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033866|||http://purl.uniprot.org/annotation/PRO_0000033867|||http://purl.uniprot.org/annotation/VAR_047054|||http://purl.uniprot.org/annotation/VAR_061896|||http://purl.uniprot.org/annotation/VSP_056841
http://togogenome.org/gene/9606:PPCDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BQB0|||http://purl.uniprot.org/uniprot/H3BRQ0|||http://purl.uniprot.org/uniprot/H3BSE3|||http://purl.uniprot.org/uniprot/H3BU63|||http://purl.uniprot.org/uniprot/Q96CD2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Flavoprotein|||In isoform 2.|||Loss of activity.|||Phosphopantothenoylcysteine decarboxylase|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182030|||http://purl.uniprot.org/annotation/VAR_068974|||http://purl.uniprot.org/annotation/VSP_044802
http://togogenome.org/gene/9606:MRPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y399                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In COXPD36; results in impaired assembly of the small mitoribosomal subunit and impaired mitochondrial translation in patient cells.|||Small ribosomal subunit protein uS2m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134343|||http://purl.uniprot.org/annotation/VAR_020128|||http://purl.uniprot.org/annotation/VAR_034479|||http://purl.uniprot.org/annotation/VAR_034480|||http://purl.uniprot.org/annotation/VAR_080787|||http://purl.uniprot.org/annotation/VAR_080788|||http://purl.uniprot.org/annotation/VAR_080789
http://togogenome.org/gene/9606:UFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61960                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished ability to be activated by UBA5.|||Confers resistance to cleavage.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||In HLD14; decreased ability to form thioester bonds with UBA5 and UFC1; decreased protein ufmylation; does not affect the cellular response to endoplasmic reticulum stress.|||In isoform 2.|||Removed in mature form|||Slightly reduced interaction with UFM1.|||Ubiquitin-fold modifier 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042122|||http://purl.uniprot.org/annotation/PRO_0000042123|||http://purl.uniprot.org/annotation/VAR_081218|||http://purl.uniprot.org/annotation/VSP_041186
http://togogenome.org/gene/9606:ARHGEF28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1W1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PTK2/FAK1; required for regulation of axonal branching and synapse formation|||Interaction with microtubules|||Mediates cytoplasmic retention and interaction with MAPK8IP1|||Mediates cytoplasmic retention and interaction with YWHAH|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||RNA-binding|||Rho guanine nucleotide exchange factor 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324119|||http://purl.uniprot.org/annotation/VAR_039657|||http://purl.uniprot.org/annotation/VAR_039658|||http://purl.uniprot.org/annotation/VAR_039659|||http://purl.uniprot.org/annotation/VAR_039660|||http://purl.uniprot.org/annotation/VAR_039661|||http://purl.uniprot.org/annotation/VAR_039662|||http://purl.uniprot.org/annotation/VAR_039663|||http://purl.uniprot.org/annotation/VAR_039664|||http://purl.uniprot.org/annotation/VSP_032140|||http://purl.uniprot.org/annotation/VSP_032141|||http://purl.uniprot.org/annotation/VSP_032142|||http://purl.uniprot.org/annotation/VSP_032143|||http://purl.uniprot.org/annotation/VSP_032144|||http://purl.uniprot.org/annotation/VSP_044737|||http://purl.uniprot.org/annotation/VSP_044738
http://togogenome.org/gene/9606:SLC26A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RACGAP1|||N-linked (GlcNAc...) asparagine|||Not a cause of male infertility.|||Polar residues|||STAS|||Testis anion transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322586|||http://purl.uniprot.org/annotation/VAR_039464|||http://purl.uniprot.org/annotation/VAR_039465|||http://purl.uniprot.org/annotation/VAR_039466|||http://purl.uniprot.org/annotation/VAR_039467|||http://purl.uniprot.org/annotation/VAR_070058|||http://purl.uniprot.org/annotation/VAR_070059|||http://purl.uniprot.org/annotation/VAR_070060|||http://purl.uniprot.org/annotation/VSP_052704|||http://purl.uniprot.org/annotation/VSP_052705|||http://purl.uniprot.org/annotation/VSP_052706|||http://purl.uniprot.org/annotation/VSP_052707|||http://purl.uniprot.org/annotation/VSP_052708
http://togogenome.org/gene/9606:CCSER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7U1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Serine-rich coiled-coil domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309461|||http://purl.uniprot.org/annotation/VAR_036952|||http://purl.uniprot.org/annotation/VAR_036953|||http://purl.uniprot.org/annotation/VAR_036954|||http://purl.uniprot.org/annotation/VAR_036955|||http://purl.uniprot.org/annotation/VSP_029180|||http://purl.uniprot.org/annotation/VSP_029181|||http://purl.uniprot.org/annotation/VSP_040287|||http://purl.uniprot.org/annotation/VSP_054560
http://togogenome.org/gene/9606:HHLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JL84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HERV-H LTR-associating protein 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394219|||http://purl.uniprot.org/annotation/VSP_039212
http://togogenome.org/gene/9606:FADS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Q0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||Cytoplasmic|||Disordered|||Fatty acid desaturase 3|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307108|||http://purl.uniprot.org/annotation/VAR_035341|||http://purl.uniprot.org/annotation/VAR_035342
http://togogenome.org/gene/9606:TP53I3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FA7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased enzyme activity.|||Loss of enzyme activity.|||N-acetylmethionine|||Quinone oxidoreductase PIG3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160917|||http://purl.uniprot.org/annotation/VAR_033032|||http://purl.uniprot.org/annotation/VAR_048201|||http://purl.uniprot.org/annotation/VSP_015783|||http://purl.uniprot.org/annotation/VSP_015784
http://togogenome.org/gene/9606:EFCAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein regulatory complex protein 8|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253544|||http://purl.uniprot.org/annotation/VSP_021055|||http://purl.uniprot.org/annotation/VSP_021056|||http://purl.uniprot.org/annotation/VSP_021057|||http://purl.uniprot.org/annotation/VSP_043273|||http://purl.uniprot.org/annotation/VSP_043274
http://togogenome.org/gene/9606:IRAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12912                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Inositol 1,4,5-triphosphate receptor associated 2|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Processed inositol 1,4,5-triphosphate receptor associated 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084483|||http://purl.uniprot.org/annotation/PRO_0000296244|||http://purl.uniprot.org/annotation/VAR_054545|||http://purl.uniprot.org/annotation/VAR_054546|||http://purl.uniprot.org/annotation/VAR_054547|||http://purl.uniprot.org/annotation/VAR_054548|||http://purl.uniprot.org/annotation/VSP_036471
http://togogenome.org/gene/9606:EMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54851                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Epithelial membrane protein 2|||Helical|||In NPHS10; decreased amount of CAV1.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164658|||http://purl.uniprot.org/annotation/VAR_071478|||http://purl.uniprot.org/annotation/VAR_071479
http://togogenome.org/gene/9606:ZNF217                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75362                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 217                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047460|||http://purl.uniprot.org/annotation/VAR_035572|||http://purl.uniprot.org/annotation/VAR_052795|||http://purl.uniprot.org/annotation/VAR_061939
http://togogenome.org/gene/9606:PHACTR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z339|||http://purl.uniprot.org/uniprot/Q96KR7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphatase and actin regulator 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||RPEL|||RPEL 1|||RPEL 2|||RPEL 3|||RPEL 4|||Required for PP1CA binding and inhibition of PP1 activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126638|||http://purl.uniprot.org/annotation/VAR_021969|||http://purl.uniprot.org/annotation/VSP_009091|||http://purl.uniprot.org/annotation/VSP_009092|||http://purl.uniprot.org/annotation/VSP_044546
http://togogenome.org/gene/9606:RNASE10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GAN6|||http://purl.uniprot.org/uniprot/W0UTC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Inactive ribonuclease-like protein 10|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045963|||http://purl.uniprot.org/annotation/PRO_5004798302|||http://purl.uniprot.org/annotation/VAR_052198|||http://purl.uniprot.org/annotation/VSP_053579
http://togogenome.org/gene/9606:OR10G7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWF3|||http://purl.uniprot.org/uniprot/Q8NGN6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10G7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150699|||http://purl.uniprot.org/annotation/VAR_024126|||http://purl.uniprot.org/annotation/VAR_034285|||http://purl.uniprot.org/annotation/VAR_048060|||http://purl.uniprot.org/annotation/VAR_048061|||http://purl.uniprot.org/annotation/VAR_048062|||http://purl.uniprot.org/annotation/VAR_048063|||http://purl.uniprot.org/annotation/VAR_048064
http://togogenome.org/gene/9606:KAT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92831                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Complete loss of acetyl-lysine binding.|||Disordered|||Found in a patient with isolated coloboma; unknown pathological significance.|||Histone acetyltransferase KAT2B|||N-acetyltransferase|||Polar residues|||Pro residues|||Proton donor/acceptor|||Reduced acetyl-lysine binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211208|||http://purl.uniprot.org/annotation/VAR_034372|||http://purl.uniprot.org/annotation/VAR_079852
http://togogenome.org/gene/9606:MANEA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SRI9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Catalytic|||Cytoplasmic|||Glycoprotein endo-alpha-1,2-mannosidase|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282315|||http://purl.uniprot.org/annotation/VAR_036242
http://togogenome.org/gene/9606:LMX1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in autosomal recessive sensorineural hearing loss; unknown pathological significance.|||Homeobox|||In DFNA7.|||In DFNA7; unknown pathological significance.|||In isoform LMX1A-4AB.|||LIM homeobox transcription factor 1-alpha|||LIM zinc-binding 1|||LIM zinc-binding 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075825|||http://purl.uniprot.org/annotation/VAR_083732|||http://purl.uniprot.org/annotation/VAR_083733|||http://purl.uniprot.org/annotation/VAR_083734|||http://purl.uniprot.org/annotation/VAR_083735|||http://purl.uniprot.org/annotation/VSP_003112
http://togogenome.org/gene/9606:TRIM43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056265
http://togogenome.org/gene/9606:PRR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16378                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Proline-rich protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022115|||http://purl.uniprot.org/annotation/VAR_027926|||http://purl.uniprot.org/annotation/VAR_027927|||http://purl.uniprot.org/annotation/VSP_044635
http://togogenome.org/gene/9606:ANKRD13D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 13D|||Basic and acidic residues|||Disordered|||In isoform 1.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UIM 1|||UIM 2|||UIM 3|||UIM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240651|||http://purl.uniprot.org/annotation/VSP_061475|||http://purl.uniprot.org/annotation/VSP_061476
http://togogenome.org/gene/9606:SH3TC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWX8|||http://purl.uniprot.org/uniprot/Q8TE82                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||N-acetylmethionine|||Phosphotyrosine|||SH3|||SH3 domain and tetratricopeptide repeat-containing protein 1|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106355|||http://purl.uniprot.org/annotation/VAR_021934|||http://purl.uniprot.org/annotation/VAR_034127|||http://purl.uniprot.org/annotation/VAR_034128|||http://purl.uniprot.org/annotation/VAR_035866|||http://purl.uniprot.org/annotation/VAR_035867
http://togogenome.org/gene/9606:FUT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2L2|||http://purl.uniprot.org/uniprot/Q10981                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Galactoside alpha-(1,2)-fucosyltransferase 2|||Helical|||Helical; Signal-anchor for type II membrane protein|||In allele Sej; non-secretor phenotype.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012140|||http://purl.uniprot.org/annotation/VAR_003422|||http://purl.uniprot.org/annotation/VAR_003423|||http://purl.uniprot.org/annotation/VAR_003424|||http://purl.uniprot.org/annotation/VAR_003425|||http://purl.uniprot.org/annotation/VAR_022187
http://togogenome.org/gene/9606:CKM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R892|||http://purl.uniprot.org/uniprot/P06732                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Creatine kinase M-type|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211975|||http://purl.uniprot.org/annotation/VAR_018680|||http://purl.uniprot.org/annotation/VAR_018681|||http://purl.uniprot.org/annotation/VAR_018682|||http://purl.uniprot.org/annotation/VAR_049675
http://togogenome.org/gene/9606:NAP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2V4|||http://purl.uniprot.org/uniprot/F5H4R6|||http://purl.uniprot.org/uniprot/F8W543|||http://purl.uniprot.org/uniprot/P55209                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Impaired binding to histones and ability to mediate histone chaperone activity.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-acetylmethionine|||N6-acetyllysine|||NAP1L motif|||Nuclear localization signal|||Nucleosome assembly protein 1-like 1|||Phosphoserine|||Phosphothreonine|||Removed|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185652|||http://purl.uniprot.org/annotation/PRO_0000393943|||http://purl.uniprot.org/annotation/VSP_053909|||http://purl.uniprot.org/annotation/VSP_057357|||http://purl.uniprot.org/annotation/VSP_057358
http://togogenome.org/gene/9606:ZNF445                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59923                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||SCAN box|||Zinc finger protein 445                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047594|||http://purl.uniprot.org/annotation/VAR_052832
http://togogenome.org/gene/9606:PGLYRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PD5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes amidase activity.|||Deamidated asparagine|||Disordered|||Important for catalytic activity; essential for amidase activity and zinc hydrate coordination|||In isoform 2.|||N-acetylmuramoyl-L-alanine amidase|||N-linked (GlcNAc...) asparagine|||No effect on amidase activity.|||Phosphoserine|||Reduced amidase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023920|||http://purl.uniprot.org/annotation/VAR_050498|||http://purl.uniprot.org/annotation/VAR_050499|||http://purl.uniprot.org/annotation/VAR_050500|||http://purl.uniprot.org/annotation/VAR_050501|||http://purl.uniprot.org/annotation/VAR_050502|||http://purl.uniprot.org/annotation/VAR_055231|||http://purl.uniprot.org/annotation/VSP_008964
http://togogenome.org/gene/9606:MAPK8IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUQ9|||http://purl.uniprot.org/uniprot/Q9UQF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes KNS2 binding.|||Abolishes MAPK9 interaction.|||Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 1|||D-box 1|||D-box 2|||Disordered|||In T2D; risk factor.|||Interaction with MAP3K7|||Interaction with VRK2|||JNK-binding domain (JBD)|||Minimal inhibitory domain (MID)|||No effect on KNS2 binding.|||PID|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK8, MAPK9 and MAPK10|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220628|||http://purl.uniprot.org/annotation/VAR_012243|||http://purl.uniprot.org/annotation/VAR_049664|||http://purl.uniprot.org/annotation/VAR_049665
http://togogenome.org/gene/9606:SH3TC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A514TP98|||http://purl.uniprot.org/uniprot/Q8TF17                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In CMT4C.|||In CMT4C; unknown pathological significance.|||In MNMN.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 domain and tetratricopeptide repeat-containing protein 2|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106356|||http://purl.uniprot.org/annotation/VAR_018267|||http://purl.uniprot.org/annotation/VAR_018268|||http://purl.uniprot.org/annotation/VAR_018269|||http://purl.uniprot.org/annotation/VAR_018270|||http://purl.uniprot.org/annotation/VAR_052622|||http://purl.uniprot.org/annotation/VAR_052623|||http://purl.uniprot.org/annotation/VAR_064421|||http://purl.uniprot.org/annotation/VAR_087587|||http://purl.uniprot.org/annotation/VAR_087588|||http://purl.uniprot.org/annotation/VSP_009881|||http://purl.uniprot.org/annotation/VSP_009882|||http://purl.uniprot.org/annotation/VSP_009883|||http://purl.uniprot.org/annotation/VSP_009884|||http://purl.uniprot.org/annotation/VSP_009885|||http://purl.uniprot.org/annotation/VSP_009886|||http://purl.uniprot.org/annotation/VSP_054499
http://togogenome.org/gene/9606:ABRAXAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15018                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-231.|||BRISC complex subunit Abraxas 2|||Basic and acidic residues|||Disordered|||Important for interaction with BBRC36 and other subunits of the BRISC complex|||Important for interaction with SHMT2|||MPN|||Phosphoserine|||Reduces interaction with SHMT2, but has no effect on interaction with BRCC3.|||Slightly reduces interaction with BBRC36. Abolishes interaction with SHMT2. Strongly reduces interactions with BABAM2 and BABAM1.|||Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with R-220. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with R-220 and Y-241.|||Strongly reduces interaction with BBRC3; SHMT2; BABAM2 and BABAM1; when associated with Y-231. Abolishes interaction with BRCC3 and strongly reduces interaction with SHMT2; BABAM2 and BABAM1; when associated with Y-231 and Y-241.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050725
http://togogenome.org/gene/9606:CXorf65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein CXorf65                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346434|||http://purl.uniprot.org/annotation/VAR_045896
http://togogenome.org/gene/9606:PATE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UY27                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Prostate and testis expressed protein 2|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263607|||http://purl.uniprot.org/annotation/VSP_035810
http://togogenome.org/gene/9606:RNASEH2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75792                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In AGS4.|||In AGS4; strongly impairs enzyme activity but not interaction with RNASEH2B and RNASEH2C.|||Loss of enzyme activity.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RNase H type-2|||Reduced enzyme activity.|||Ribonuclease H2 subunit A|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111710|||http://purl.uniprot.org/annotation/VAR_024617|||http://purl.uniprot.org/annotation/VAR_027377|||http://purl.uniprot.org/annotation/VAR_027378|||http://purl.uniprot.org/annotation/VAR_070623|||http://purl.uniprot.org/annotation/VAR_070624|||http://purl.uniprot.org/annotation/VAR_070625|||http://purl.uniprot.org/annotation/VAR_070626|||http://purl.uniprot.org/annotation/VAR_070627|||http://purl.uniprot.org/annotation/VAR_070628|||http://purl.uniprot.org/annotation/VAR_070629|||http://purl.uniprot.org/annotation/VAR_070630|||http://purl.uniprot.org/annotation/VAR_070631|||http://purl.uniprot.org/annotation/VAR_070632
http://togogenome.org/gene/9606:H1-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22492                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1t|||Important for nucleosome binding properties|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195910|||http://purl.uniprot.org/annotation/VAR_049310|||http://purl.uniprot.org/annotation/VAR_049311|||http://purl.uniprot.org/annotation/VAR_049312
http://togogenome.org/gene/9606:OR11G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWS8|||http://purl.uniprot.org/uniprot/Q8NGC1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150723|||http://purl.uniprot.org/annotation/VAR_047237|||http://purl.uniprot.org/annotation/VAR_047238
http://togogenome.org/gene/9606:C22orf31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95567                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C22orf31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254057|||http://purl.uniprot.org/annotation/VAR_028808|||http://purl.uniprot.org/annotation/VAR_028809
http://togogenome.org/gene/9606:PCDHB16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRJ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003944|||http://purl.uniprot.org/annotation/VAR_026478|||http://purl.uniprot.org/annotation/VAR_026479|||http://purl.uniprot.org/annotation/VAR_055587|||http://purl.uniprot.org/annotation/VAR_061068|||http://purl.uniprot.org/annotation/VAR_061069
http://togogenome.org/gene/9606:PRR23C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Pro residues|||Proline-rich protein 23C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332250
http://togogenome.org/gene/9606:TNFSF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50591|||http://purl.uniprot.org/uniprot/Q6IBA9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Polar residues|||TNF family profile|||Tumor necrosis factor ligand superfamily member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185503|||http://purl.uniprot.org/annotation/VAR_052584|||http://purl.uniprot.org/annotation/VAR_052585|||http://purl.uniprot.org/annotation/VSP_043507|||http://purl.uniprot.org/annotation/VSP_043508
http://togogenome.org/gene/9606:ZNF398                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7S8|||http://purl.uniprot.org/uniprot/A0A090N8F2|||http://purl.uniprot.org/uniprot/B4DXA9|||http://purl.uniprot.org/uniprot/Q8TD17                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||KRAB-related|||Polar residues|||Zinc finger protein 398                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047565|||http://purl.uniprot.org/annotation/VAR_052817|||http://purl.uniprot.org/annotation/VAR_052818|||http://purl.uniprot.org/annotation/VSP_006926
http://togogenome.org/gene/9606:CTNNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDY0|||http://purl.uniprot.org/uniprot/B4DKT9|||http://purl.uniprot.org/uniprot/B4DU00|||http://purl.uniprot.org/uniprot/P35221                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by CK1.|||Abolishes phosphorylation by CK1. No effect on phosphorylation by CK2.|||Abolishes phosphorylation by CK2. No effect on phosphorylation by CK1.|||Basic and acidic residues|||Catenin alpha-1|||Disordered|||Enhances phosphorylation by CK1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MDPT2; no effect on VCL-binding.|||In isoform 2.|||In isoform 3.|||Interaction with JUP and CTNNB1|||Interaction with alpha-actinin|||Involved in homodimerization|||N-acetylthreonine|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphothreonine; by CK1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064261|||http://purl.uniprot.org/annotation/PRO_5002800893|||http://purl.uniprot.org/annotation/VAR_022303|||http://purl.uniprot.org/annotation/VAR_022304|||http://purl.uniprot.org/annotation/VAR_076586|||http://purl.uniprot.org/annotation/VAR_076587|||http://purl.uniprot.org/annotation/VAR_076588|||http://purl.uniprot.org/annotation/VAR_076589|||http://purl.uniprot.org/annotation/VSP_017494|||http://purl.uniprot.org/annotation/VSP_047810
http://togogenome.org/gene/9606:ATP6V0E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15342                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||V-type proton ATPase subunit e 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071740
http://togogenome.org/gene/9606:KRT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13645                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In AEI1.|||In AEI1; requires 2 nucleotide substitutions.|||In EHK.|||In EHK; also found in a patient with hyperkeratotic epidermal nevi due to genetic mosaicism.|||In EHK; mild phenotype.|||In EHK; severe phenotype.|||In IHL; unknown pathological significance.|||Interchain|||Keratin, type I cytoskeletal 10|||Linker 1|||Linker 12|||Phosphoserine|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063642|||http://purl.uniprot.org/annotation/VAR_003826|||http://purl.uniprot.org/annotation/VAR_003827|||http://purl.uniprot.org/annotation/VAR_003828|||http://purl.uniprot.org/annotation/VAR_003829|||http://purl.uniprot.org/annotation/VAR_003830|||http://purl.uniprot.org/annotation/VAR_003831|||http://purl.uniprot.org/annotation/VAR_003832|||http://purl.uniprot.org/annotation/VAR_003833|||http://purl.uniprot.org/annotation/VAR_010505|||http://purl.uniprot.org/annotation/VAR_010506|||http://purl.uniprot.org/annotation/VAR_010507|||http://purl.uniprot.org/annotation/VAR_010508|||http://purl.uniprot.org/annotation/VAR_010509|||http://purl.uniprot.org/annotation/VAR_010510|||http://purl.uniprot.org/annotation/VAR_010511|||http://purl.uniprot.org/annotation/VAR_033145|||http://purl.uniprot.org/annotation/VAR_058202|||http://purl.uniprot.org/annotation/VAR_060723|||http://purl.uniprot.org/annotation/VAR_071985|||http://purl.uniprot.org/annotation/VAR_087806
http://togogenome.org/gene/9606:CENPM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSP4                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand                                                                                  ^@                                                                                  Centromere protein M|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058224|||http://purl.uniprot.org/annotation/VSP_010259|||http://purl.uniprot.org/annotation/VSP_010260|||http://purl.uniprot.org/annotation/VSP_017725|||http://purl.uniprot.org/annotation/VSP_017726|||http://purl.uniprot.org/annotation/VSP_046189
http://togogenome.org/gene/9606:MSI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHE8|||http://purl.uniprot.org/uniprot/Q96DH6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form MSI2/HOXA9 fusion protein|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA-binding protein Musashi homolog 2|||RRM|||RRM 1|||RRM 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081652|||http://purl.uniprot.org/annotation/VSP_011168|||http://purl.uniprot.org/annotation/VSP_011169|||http://purl.uniprot.org/annotation/VSP_011170|||http://purl.uniprot.org/annotation/VSP_011171
http://togogenome.org/gene/9606:NCMAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1S8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Noncompact myelin-associated protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265078
http://togogenome.org/gene/9606:ZNF366                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N895                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with CTBP1 and in part relieves transcription repression; when associated with A-590.|||Abolishes interaction with CTBP1 and in part relieves transcription repression; when associated with A-592.|||Abolishes interaction with CTBP1. Abolishes interaction with CTBP1; when associated with A-648.|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Decreases interaction with CTBP1; when associated with A-645.|||Decreases interaction with CTBP1; when associated with A-647.|||Disordered|||Interaction with NRIP1|||No effect on interaction with CTBP1. Abolishes interaction with CTBP1; when associated with A-593.|||PXDLS|||Zinc finger protein 366                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047548|||http://purl.uniprot.org/annotation/VAR_033564
http://togogenome.org/gene/9606:ZNF142                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0N7C4|||http://purl.uniprot.org/uniprot/P52746                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 31|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDISHM.|||Phosphoserine|||Polar residues|||Zinc finger protein 142                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047425|||http://purl.uniprot.org/annotation/VAR_047230|||http://purl.uniprot.org/annotation/VAR_047231|||http://purl.uniprot.org/annotation/VAR_047232|||http://purl.uniprot.org/annotation/VAR_082094|||http://purl.uniprot.org/annotation/VAR_082095|||http://purl.uniprot.org/annotation/VAR_082096|||http://purl.uniprot.org/annotation/VAR_082097
http://togogenome.org/gene/9606:GTPBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2CFK9|||http://purl.uniprot.org/uniprot/Q9BZE4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GTP-binding protein 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||OBG-type G|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195023|||http://purl.uniprot.org/annotation/VAR_068801|||http://purl.uniprot.org/annotation/VSP_056146|||http://purl.uniprot.org/annotation/VSP_056147
http://togogenome.org/gene/9606:SLC35A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BS91                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||UDP-sugar transporter protein SLC35A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309355|||http://purl.uniprot.org/annotation/VAR_036945
http://togogenome.org/gene/9606:PLIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FHZ7|||http://purl.uniprot.org/uniprot/Q99541                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished phosphorylation at Tyr-232 by isoform 1 of CHKA (CHKalpha2).|||Disordered|||N-acetylalanine|||Perilipin-2|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099888|||http://purl.uniprot.org/annotation/VAR_061506
http://togogenome.org/gene/9606:MARCHF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0Z6|||http://purl.uniprot.org/uniprot/Q8TCQ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase MARCHF1|||Helical|||In isoform 2.|||Polar residues|||RING-CH-type|||RING-type|||Responsible for down-regulation of CD86 and MHC class II cell surface expression|||Responsible for low stability                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274365|||http://purl.uniprot.org/annotation/VSP_022724|||http://purl.uniprot.org/annotation/VSP_022725
http://togogenome.org/gene/9606:SIPA1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWP0|||http://purl.uniprot.org/uniprot/O60292                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with bilateral congenital cataracts; unknown pathological significance; lack of normal basal actin stress fiber formation; absence of SIPA1L3 and F-actin colocalization.|||N6-acetyllysine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated 1-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056752|||http://purl.uniprot.org/annotation/VAR_025476|||http://purl.uniprot.org/annotation/VAR_025477|||http://purl.uniprot.org/annotation/VAR_075045
http://togogenome.org/gene/9606:CT55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUE5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cancer/testis antigen 55|||Disordered|||In SPGFX7; protein undetectable in patient spermatozoa.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079739|||http://purl.uniprot.org/annotation/VAR_088387|||http://purl.uniprot.org/annotation/VSP_014465
http://togogenome.org/gene/9606:SCG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13521                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Manserin|||O-glycosylated at one site|||Phosphoserine|||Secretogranin-2|||Secretoneurin|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005452|||http://purl.uniprot.org/annotation/PRO_0000005453|||http://purl.uniprot.org/annotation/PRO_0000005454|||http://purl.uniprot.org/annotation/PRO_0000432735|||http://purl.uniprot.org/annotation/VAR_031555|||http://purl.uniprot.org/annotation/VAR_031556|||http://purl.uniprot.org/annotation/VAR_031557|||http://purl.uniprot.org/annotation/VAR_031558|||http://purl.uniprot.org/annotation/VAR_031559|||http://purl.uniprot.org/annotation/VAR_048755
http://togogenome.org/gene/9606:VAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99536                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Removed|||Synaptic vesicle membrane protein VAT-1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160918|||http://purl.uniprot.org/annotation/VSP_055794|||http://purl.uniprot.org/annotation/VSP_055795
http://togogenome.org/gene/9606:BRMS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5PSV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Breast cancer metastasis-suppressor 1-like protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305309|||http://purl.uniprot.org/annotation/VSP_055547
http://togogenome.org/gene/9606:EMX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04741                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein EMX1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048866|||http://purl.uniprot.org/annotation/VSP_022145|||http://purl.uniprot.org/annotation/VSP_022146
http://togogenome.org/gene/9606:SLIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75094                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CTCK|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRCT 3|||LRRCT 4|||LRRNT|||LRRNT 2|||LRRNT 3|||LRRNT 4|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Slit homolog 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007732|||http://purl.uniprot.org/annotation/VAR_020168|||http://purl.uniprot.org/annotation/VAR_021905|||http://purl.uniprot.org/annotation/VAR_024265|||http://purl.uniprot.org/annotation/VAR_049004|||http://purl.uniprot.org/annotation/VAR_049005|||http://purl.uniprot.org/annotation/VAR_049006|||http://purl.uniprot.org/annotation/VSP_009714|||http://purl.uniprot.org/annotation/VSP_009715|||http://purl.uniprot.org/annotation/VSP_054798
http://togogenome.org/gene/9606:NECTIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K4PZ75|||http://purl.uniprot.org/uniprot/Q96NY8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In EDSS1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nectin-4|||Polar residues|||Processed poliovirus receptor-related protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297673|||http://purl.uniprot.org/annotation/PRO_0000311086|||http://purl.uniprot.org/annotation/PRO_5014305667|||http://purl.uniprot.org/annotation/VAR_034669|||http://purl.uniprot.org/annotation/VAR_064189|||http://purl.uniprot.org/annotation/VSP_056819|||http://purl.uniprot.org/annotation/VSP_056820
http://togogenome.org/gene/9606:C3AR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2H7|||http://purl.uniprot.org/uniprot/Q16581                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C3a anaphylatoxin chemotactic receptor|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Phosphoserine|||Phosphothreonine|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069202|||http://purl.uniprot.org/annotation/VAR_019164
http://togogenome.org/gene/9606:STK32C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW0|||http://purl.uniprot.org/uniprot/B7Z7J1|||http://purl.uniprot.org/uniprot/H0Y349|||http://purl.uniprot.org/uniprot/H0Y431|||http://purl.uniprot.org/uniprot/Q86UX6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with global developmental delay; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 32C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232415|||http://purl.uniprot.org/annotation/VAR_025900|||http://purl.uniprot.org/annotation/VAR_035637|||http://purl.uniprot.org/annotation/VAR_041170|||http://purl.uniprot.org/annotation/VAR_041171|||http://purl.uniprot.org/annotation/VAR_084657|||http://purl.uniprot.org/annotation/VSP_051998
http://togogenome.org/gene/9606:ARHGDIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QQX2|||http://purl.uniprot.org/uniprot/P52565|||http://purl.uniprot.org/uniprot/V9HWE8                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NPHS8; produces mislocalization into the nucleus, hyperactivation of Rho-GTPases RHOA, RAC1 and CDC42 and impaired cell motility.|||In isoform 2.|||Loss of RHOA interaction; when associated with A-185.|||Loss of RHOA interaction; when associated with A-45.|||Loss of interaction with NGFR.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Removed|||Rho GDP-dissociation inhibitor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219013|||http://purl.uniprot.org/annotation/VAR_069814|||http://purl.uniprot.org/annotation/VSP_046699
http://togogenome.org/gene/9606:KCNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with KCND2|||Kv channel-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073818|||http://purl.uniprot.org/annotation/VSP_015043|||http://purl.uniprot.org/annotation/VSP_015044|||http://purl.uniprot.org/annotation/VSP_041511|||http://purl.uniprot.org/annotation/VSP_047687
http://togogenome.org/gene/9606:EVPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLH8|||http://purl.uniprot.org/uniprot/K7EKI0|||http://purl.uniprot.org/uniprot/Q92817                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  4 X 4 AA tandem repeats of K-G-S-P|||Basic and acidic residues|||Central fibrous rod domain|||Disordered|||Envoplakin|||Globular 1|||Globular 2|||Phosphoserine|||Plectin 1|||Plectin 2|||Plectin 3|||Plectin 4|||Plectin 5|||Plectin 6|||Plectin 7|||Polar residues|||SH3|||Spectrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078147|||http://purl.uniprot.org/annotation/VAR_024579|||http://purl.uniprot.org/annotation/VAR_033863|||http://purl.uniprot.org/annotation/VAR_057698|||http://purl.uniprot.org/annotation/VAR_057699
http://togogenome.org/gene/9606:LRRIQ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6PVS8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  IQ|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Leucine-rich repeat and IQ domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311194|||http://purl.uniprot.org/annotation/VAR_037154|||http://purl.uniprot.org/annotation/VAR_037155|||http://purl.uniprot.org/annotation/VAR_037156|||http://purl.uniprot.org/annotation/VAR_051136|||http://purl.uniprot.org/annotation/VAR_051137|||http://purl.uniprot.org/annotation/VAR_051138|||http://purl.uniprot.org/annotation/VAR_051139|||http://purl.uniprot.org/annotation/VSP_029408|||http://purl.uniprot.org/annotation/VSP_029409|||http://purl.uniprot.org/annotation/VSP_029410|||http://purl.uniprot.org/annotation/VSP_029411
http://togogenome.org/gene/9606:QRICH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L3Z9|||http://purl.uniprot.org/uniprot/Q2TAL8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CARD|||DUF3504|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In VERBRAS; decreased QRICH1 protein expression; decreased growth plate chondrocyte hypertrophic differentiation; unknown pathological significance.|||In VERBRAS; unknown pathological significance.|||N-acetylmethionine|||Phosphoserine|||Transcriptional regulator QRICH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269853|||http://purl.uniprot.org/annotation/VAR_080962|||http://purl.uniprot.org/annotation/VAR_084455|||http://purl.uniprot.org/annotation/VAR_084456|||http://purl.uniprot.org/annotation/VAR_084457
http://togogenome.org/gene/9606:NIP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y221                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  60S ribosome subunit biogenesis protein NIP7 homolog|||C-terminal domain|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-terminal domain|||PUA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218773|||http://purl.uniprot.org/annotation/VAR_036488|||http://purl.uniprot.org/annotation/VSP_012094
http://togogenome.org/gene/9606:H2AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75409                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Huntingtin-interacting protein M|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254087|||http://purl.uniprot.org/annotation/VAR_028810
http://togogenome.org/gene/9606:MEI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TIA1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with non-obstructive azoospermia; unknown pathological significance.|||Found in patients with non-obstructive azoospermia; unknown pathological significance.|||In HYDM3; the variant leads to a normally spliced transcript and two abnormal isoforms.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Meiosis inhibitor protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000347264|||http://purl.uniprot.org/annotation/VAR_046037|||http://purl.uniprot.org/annotation/VAR_046038|||http://purl.uniprot.org/annotation/VAR_051184|||http://purl.uniprot.org/annotation/VAR_081145|||http://purl.uniprot.org/annotation/VAR_082605|||http://purl.uniprot.org/annotation/VAR_087425|||http://purl.uniprot.org/annotation/VAR_087426|||http://purl.uniprot.org/annotation/VSP_052883|||http://purl.uniprot.org/annotation/VSP_052884|||http://purl.uniprot.org/annotation/VSP_052885|||http://purl.uniprot.org/annotation/VSP_052886|||http://purl.uniprot.org/annotation/VSP_052887|||http://purl.uniprot.org/annotation/VSP_052888|||http://purl.uniprot.org/annotation/VSP_052889|||http://purl.uniprot.org/annotation/VSP_052890|||http://purl.uniprot.org/annotation/VSP_052891
http://togogenome.org/gene/9606:BPIFB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4F0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPI fold-containing family B member 2|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017164|||http://purl.uniprot.org/annotation/VAR_024515|||http://purl.uniprot.org/annotation/VAR_036550|||http://purl.uniprot.org/annotation/VAR_049740
http://togogenome.org/gene/9606:CLDND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0R4J2F2|||http://purl.uniprot.org/uniprot/Q9NY35                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Claudin domain-containing protein 1|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164694|||http://purl.uniprot.org/annotation/VSP_013156|||http://purl.uniprot.org/annotation/VSP_013157|||http://purl.uniprot.org/annotation/VSP_046865
http://togogenome.org/gene/9606:RBMY1J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQ82|||http://purl.uniprot.org/uniprot/Q15415                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member F/J|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314164|||http://purl.uniprot.org/annotation/VSP_030217|||http://purl.uniprot.org/annotation/VSP_030218
http://togogenome.org/gene/9606:RSPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UC2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphothreonine; by MAPK1|||Polar residues|||Radial spoke head protein 3 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313741|||http://purl.uniprot.org/annotation/VAR_037720|||http://purl.uniprot.org/annotation/VAR_037721|||http://purl.uniprot.org/annotation/VAR_037722|||http://purl.uniprot.org/annotation/VAR_037723|||http://purl.uniprot.org/annotation/VAR_037724|||http://purl.uniprot.org/annotation/VAR_037725|||http://purl.uniprot.org/annotation/VSP_030128
http://togogenome.org/gene/9606:ACAA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNP8|||http://purl.uniprot.org/uniprot/P42765                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-ketoacyl-CoA thiolase, mitochondrial|||Acyl-thioester intermediate|||Decreased acyl-CoA hydrolase activity.|||Decreased acyl-CoA hydrolase activity; when associated with A-382.|||Decreased acyl-CoA hydrolase activity; when associated with S-92.|||Increases nucleophilicity of active site Cys|||Mitochondrion; not cleaved|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Proton donor/acceptor|||Thiolase C-terminal|||Thiolase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223299|||http://purl.uniprot.org/annotation/VAR_052577
http://togogenome.org/gene/9606:OR5K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NET4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5K3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310455|||http://purl.uniprot.org/annotation/VAR_037044
http://togogenome.org/gene/9606:YAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K0KVU2|||http://purl.uniprot.org/uniprot/P46937|||http://purl.uniprot.org/uniprot/Q86T74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of interaction with TEAD1.|||Disordered|||Enhanced interaction with TP73.|||In YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-109; A-127 and A-164.|||In YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-109 and A-127.|||In YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-127 and A-164.|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 8.|||In isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 7 and isoform 9.|||Loss of interaction with ERBB4, loss of transcriptional coactivation function toward CTF and reduced interaction with PRRG4; when associated with A-199.|||Loss of interaction with ERBB4, loss of transcriptional coactivation function toward CTF and reduced interaction with PRRG4; when associated with A-202.|||Loss of interaction with TEAD1, TEAD2, TEAD3 and TEAD4. Loss of transcriptional coactivation activity towards TEAD1, TEAD2, TEAD3 and TEAD4 but no effect on its activity towards RUNX2 and ERBB4. Abolishes suppression of ciliogenesis.|||Loss of interaction with TEAD1.|||Loss of phosphorylation by LATS1.|||No change in interaction with TEAD4. Reduced interaction with TEAD4 and transforming ability; when associated with A-84 and A-85.|||No effect on interaction with PRRG4.|||No effect on phosphorylation but loss of interaction with YWHAB.|||No phosphorylation by ABL1 and partial loss of binding to TP73.|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by LATS1 and LATS2|||Phosphoserine; by MAPK8 and MAPK9|||Phosphothreonine|||Phosphothreonine; by MAPK8 and MAPK9|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||Reduced interaction with PRRG4; when associated with A-258.|||Reduced interaction with PRRG4; when associated with A-261.|||Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-84.|||Reduced interaction with TEAD4 and transforming ability; when associated with A-80 and A-85.|||Reduced phosphorylation by LATS2, loss of phosphorylation by LATS1, loss of interaction with YWHAB, decreased interaction with ERBB4 and increased nuclear localization and transcriptional coactivation activity toward ERBB4. In YAP-4SA; prevents phosphorylation by LATS1 and LATS2, promoting retention in the nucleus; when associated with A-61; A-109; A-127 and A-164.|||Significantly decreased phosphorylation at S-127 and decreased interaction with YWHAB.|||Transactivation domain|||Transcriptional coactivator YAP1|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076071|||http://purl.uniprot.org/annotation/VAR_071125|||http://purl.uniprot.org/annotation/VAR_071126|||http://purl.uniprot.org/annotation/VAR_071127|||http://purl.uniprot.org/annotation/VAR_071128|||http://purl.uniprot.org/annotation/VSP_039053|||http://purl.uniprot.org/annotation/VSP_039054|||http://purl.uniprot.org/annotation/VSP_039055|||http://purl.uniprot.org/annotation/VSP_045190|||http://purl.uniprot.org/annotation/VSP_053483
http://togogenome.org/gene/9606:NANP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBE9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N-acylneuraminate-9-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083938
http://togogenome.org/gene/9606:ARHGEF10L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTL3|||http://purl.uniprot.org/uniprot/Q5VXI4|||http://purl.uniprot.org/uniprot/Q9HCE6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DH|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Rho guanine nucleotide exchange factor 10-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342361|||http://purl.uniprot.org/annotation/VAR_044183|||http://purl.uniprot.org/annotation/VAR_044184|||http://purl.uniprot.org/annotation/VAR_044185|||http://purl.uniprot.org/annotation/VAR_044186|||http://purl.uniprot.org/annotation/VAR_061794|||http://purl.uniprot.org/annotation/VSP_034420|||http://purl.uniprot.org/annotation/VSP_034421|||http://purl.uniprot.org/annotation/VSP_034422|||http://purl.uniprot.org/annotation/VSP_034423|||http://purl.uniprot.org/annotation/VSP_034424|||http://purl.uniprot.org/annotation/VSP_034425|||http://purl.uniprot.org/annotation/VSP_034426
http://togogenome.org/gene/9606:DCP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZD4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||mRNA-decapping enzyme 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000402799|||http://purl.uniprot.org/annotation/VAR_047395|||http://purl.uniprot.org/annotation/VAR_047396|||http://purl.uniprot.org/annotation/VAR_047397|||http://purl.uniprot.org/annotation/VAR_047398|||http://purl.uniprot.org/annotation/VSP_056044
http://togogenome.org/gene/9606:PCYOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHG3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prenylcysteine oxidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023298|||http://purl.uniprot.org/annotation/VAR_050469|||http://purl.uniprot.org/annotation/VAR_050470|||http://purl.uniprot.org/annotation/VAR_050471|||http://purl.uniprot.org/annotation/VSP_056701
http://togogenome.org/gene/9606:PCSK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBP7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1.5 kDa decrease of the apparent molecular mass of pro-PCSK9 and PCSK9 and no effect on processing and secretion.|||Associated with lower plasma levels of low-density lipoprotein cholesterol.|||Associated with lower plasma levels of low-density lipoprotein cholesterol; more extensive cleavage by furin and PCSK5.|||Associated with lower plasma levels of low-density lipoprotein cholesterol; reduced phosphorylation at Ser-47.|||Associated with reduced phosphorylation at Ser-47.|||C-terminal domain|||Charge relay system|||Cleavage; by autolysis|||Cleavage; by furin and PCSK5|||Does not affect multimerization or zymogen processing.|||Found in a patient associated with autosomal dominant hypercholesterolemia; unknown pathological significance.|||Found in patients with familial hypercholesterolemia carrying a homozygous LDLR mutation; acts as a disease modifier resulting in a mild phenotype.|||In FHCL3.|||In FHCL3; complete loss of cleavage by furin and PCSK5; reduces glycosylation levels; no effect on protein sulfation and phosphorylation; no effect on protein sulfation but inhibits phosphorylation when associated with Y-374; highly reduces LDL uptake when associated with Y-374.|||In FHCL3; partial loss of cleavage by furin and PCSK5.|||In FHCL3; partial loss of cleavage by furin and PCSK5; no effect on protein sulfation but inhibits phosphorylation when associated with S-218; highly increases LDL uptake when associated with S-218.|||In isoform 2.|||Increases interaction with ANXA2.|||Inhibitor I9|||N-linked (GlcNAc...) asparagine|||No effect on interaction with ANXA2.|||Peptidase S8|||Phosphoserine; by FAM20C|||Proprotein convertase subtilisin/kexin type 9|||Remains in the endoplasmic reticulum and is not secreted.|||Sulfotyrosine|||This variant seems to have a modifier effect on LDLR mutation and familial hypercholesterolemia.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027120|||http://purl.uniprot.org/annotation/PRO_0000027121|||http://purl.uniprot.org/annotation/VAR_017197|||http://purl.uniprot.org/annotation/VAR_017198|||http://purl.uniprot.org/annotation/VAR_017199|||http://purl.uniprot.org/annotation/VAR_017200|||http://purl.uniprot.org/annotation/VAR_017201|||http://purl.uniprot.org/annotation/VAR_021336|||http://purl.uniprot.org/annotation/VAR_021337|||http://purl.uniprot.org/annotation/VAR_021338|||http://purl.uniprot.org/annotation/VAR_021339|||http://purl.uniprot.org/annotation/VAR_021340|||http://purl.uniprot.org/annotation/VAR_021341|||http://purl.uniprot.org/annotation/VAR_025451|||http://purl.uniprot.org/annotation/VAR_025452|||http://purl.uniprot.org/annotation/VAR_025453|||http://purl.uniprot.org/annotation/VAR_025454|||http://purl.uniprot.org/annotation/VAR_025455|||http://purl.uniprot.org/annotation/VAR_025456|||http://purl.uniprot.org/annotation/VAR_025457|||http://purl.uniprot.org/annotation/VAR_025458|||http://purl.uniprot.org/annotation/VAR_025459|||http://purl.uniprot.org/annotation/VAR_058520|||http://purl.uniprot.org/annotation/VAR_058521|||http://purl.uniprot.org/annotation/VAR_058522|||http://purl.uniprot.org/annotation/VAR_058523|||http://purl.uniprot.org/annotation/VAR_058524|||http://purl.uniprot.org/annotation/VAR_058525|||http://purl.uniprot.org/annotation/VAR_058526|||http://purl.uniprot.org/annotation/VAR_058527|||http://purl.uniprot.org/annotation/VAR_058528|||http://purl.uniprot.org/annotation/VAR_058529|||http://purl.uniprot.org/annotation/VAR_058530|||http://purl.uniprot.org/annotation/VAR_058531|||http://purl.uniprot.org/annotation/VAR_058532|||http://purl.uniprot.org/annotation/VAR_058533|||http://purl.uniprot.org/annotation/VAR_058534|||http://purl.uniprot.org/annotation/VAR_058535|||http://purl.uniprot.org/annotation/VAR_058536|||http://purl.uniprot.org/annotation/VAR_058537|||http://purl.uniprot.org/annotation/VAR_067282|||http://purl.uniprot.org/annotation/VAR_067351|||http://purl.uniprot.org/annotation/VAR_073657|||http://purl.uniprot.org/annotation/VSP_008844|||http://purl.uniprot.org/annotation/VSP_008845|||http://purl.uniprot.org/annotation/VSP_008846
http://togogenome.org/gene/9606:TYROBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43914|||http://purl.uniprot.org/uniprot/X6RGC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-41 and L-45.|||Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-41 and L-49.|||Does not significantly alter the formation of homotrimers or homotetramers; when associated with L-45 and L-49.|||Extracellular|||Found in patients with early-onset Alzheimer disease; unknown pathological significance.|||Found in patients with early-onset Alzheimer disease; unknown pathological significance; associated in cis with E-2 in some patients.|||Found in patients with early-onset Alzheimer disease; unknown pathological significance; associated in cis with L-55 in some patients.|||Found in patients with early-onset Alzheimer disease; unknown pathological significance; causes reduced expression; also leads to reduced expression of TREM2.|||Helical|||ITAM|||Important for interaction with transmembrane receptors|||In isoform 2.|||In isoform 3.|||Interchain|||Phosphotyrosine|||Polar residues|||Reduced cell surface expression of KIR2DS1. Severely impairs formation of homotrimers and homotetramers. Abolishes interaction with TREM2 and stabilization of TREM2-CTF. Impairs the expression of KLRD1-KLRC2 on the cell surface.|||Reduced interaction with KLRC2 and KIR2DS3. Reduces homotrimer formation and increases homotetramer formation.|||Reduces formation of homotrimers and homotetramers.|||Severely impairs formation of homotrimers and homotetramers.|||TYRO protein tyrosine kinase-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022603|||http://purl.uniprot.org/annotation/PRO_5004976519|||http://purl.uniprot.org/annotation/VAR_011985|||http://purl.uniprot.org/annotation/VAR_081398|||http://purl.uniprot.org/annotation/VAR_081399|||http://purl.uniprot.org/annotation/VAR_081400|||http://purl.uniprot.org/annotation/VAR_081401|||http://purl.uniprot.org/annotation/VAR_081402|||http://purl.uniprot.org/annotation/VAR_081403|||http://purl.uniprot.org/annotation/VAR_081404|||http://purl.uniprot.org/annotation/VAR_081405|||http://purl.uniprot.org/annotation/VSP_012909|||http://purl.uniprot.org/annotation/VSP_046066
http://togogenome.org/gene/9606:ATXN7L3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Ataxin-7-like protein 3B|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392529
http://togogenome.org/gene/9606:SLC18A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16572                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Has normal transporter activity. Loss of activity; when associated with N-398.|||Has normal transporter activity. Retains the transporter activity; when associated with E-398.|||Helical|||Important for transporter activity|||In CMS21.|||Loss of activity.|||Lumenal, vesicle|||Mediates interaction with SEC14L1|||N-linked (GlcNAc...) asparagine|||Vesicular acetylcholine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127517|||http://purl.uniprot.org/annotation/VAR_020034|||http://purl.uniprot.org/annotation/VAR_020035|||http://purl.uniprot.org/annotation/VAR_024638|||http://purl.uniprot.org/annotation/VAR_029152|||http://purl.uniprot.org/annotation/VAR_078030|||http://purl.uniprot.org/annotation/VAR_078031
http://togogenome.org/gene/9606:PRDM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPI0|||http://purl.uniprot.org/uniprot/Q9UKN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; atypical|||Disordered|||PR domain zinc finger protein 4|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047760
http://togogenome.org/gene/9606:ZIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PE6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger imprinted 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047775|||http://purl.uniprot.org/annotation/VAR_024222|||http://purl.uniprot.org/annotation/VAR_024223|||http://purl.uniprot.org/annotation/VAR_024224|||http://purl.uniprot.org/annotation/VAR_024225|||http://purl.uniprot.org/annotation/VAR_033599|||http://purl.uniprot.org/annotation/VAR_052933
http://togogenome.org/gene/9606:TESC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BS2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Calcineurin B homologous protein 3|||Disordered|||EF-hand|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073859|||http://purl.uniprot.org/annotation/VSP_035518|||http://purl.uniprot.org/annotation/VSP_035519|||http://purl.uniprot.org/annotation/VSP_045287
http://togogenome.org/gene/9606:MICAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94851                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Blocks FAD binding and abolishes catalytic activity.|||Calponin-homology (CH)|||Disordered|||In MICAL-2NLSMut; abolishes nuclear localization.|||In isoform 1, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4, isoform 6 and isoform 2.|||In isoform 4.|||In isoform 6 and isoform 2.|||Interaction with MAPK1|||LIM zinc-binding|||Monooxygenase domain|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Pro residues|||[F-actin]-monooxygenase MICAL2|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075844|||http://purl.uniprot.org/annotation/VAR_020257|||http://purl.uniprot.org/annotation/VAR_021992|||http://purl.uniprot.org/annotation/VAR_024523|||http://purl.uniprot.org/annotation/VAR_050155|||http://purl.uniprot.org/annotation/VAR_050156|||http://purl.uniprot.org/annotation/VAR_050157|||http://purl.uniprot.org/annotation/VAR_056936|||http://purl.uniprot.org/annotation/VAR_056937|||http://purl.uniprot.org/annotation/VAR_056938|||http://purl.uniprot.org/annotation/VAR_056939|||http://purl.uniprot.org/annotation/VAR_056940|||http://purl.uniprot.org/annotation/VAR_061684|||http://purl.uniprot.org/annotation/VSP_061291|||http://purl.uniprot.org/annotation/VSP_061292|||http://purl.uniprot.org/annotation/VSP_061293|||http://purl.uniprot.org/annotation/VSP_061294|||http://purl.uniprot.org/annotation/VSP_061295|||http://purl.uniprot.org/annotation/VSP_061296|||http://purl.uniprot.org/annotation/VSP_061297|||http://purl.uniprot.org/annotation/VSP_061298|||http://purl.uniprot.org/annotation/VSP_061299
http://togogenome.org/gene/9606:TBC1D8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0IIM8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||In NPHS20; exhibits intracellular vesicular localization; rescues only partially glomerular filtration defects in tbc1d8b knockout fish; reduced podocyte migration; defective vesicular trafficking in podocytes.|||In NPHS20; rescues only partially glomerular filtration defects in tbc1d8b knockout fish; defective vesicular trafficking in podocytes.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Rab-GAP TBC|||TBC1 domain family member 8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337183|||http://purl.uniprot.org/annotation/VAR_082286|||http://purl.uniprot.org/annotation/VAR_082287|||http://purl.uniprot.org/annotation/VSP_033953|||http://purl.uniprot.org/annotation/VSP_033954|||http://purl.uniprot.org/annotation/VSP_043710
http://togogenome.org/gene/9606:COMMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBI1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077389|||http://purl.uniprot.org/annotation/VAR_061121
http://togogenome.org/gene/9606:CBFA2T3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75081                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form type-1 RUNX1-CBFA2T3 fusion protein|||Breakpoint for translocation to form type-2 RUNX1-CBFA2T3 fusion protein|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with HIF1A|||Interaction with ZBTB33|||Loss of interaction with PRKAR2A.|||MYND-type|||Mediates interaction with PDE7A (in isoform 2)|||Mediates interaction with PRKAR2A|||Mediates localization to the nucleus|||Nervy homology region 2 (NHR2); essential for down-regulation of PFKFB3, PFKFB4 and PDK1 expression|||Nervy homology region 3 (NHR3); essential for down-regulation of PFKFB3, PFKFB4 and PDK1 expression|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein CBFA2T3|||Required for nucleolar targeting (in isoform 1)|||TAFH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307173|||http://purl.uniprot.org/annotation/VAR_035374|||http://purl.uniprot.org/annotation/VAR_035447|||http://purl.uniprot.org/annotation/VAR_035448|||http://purl.uniprot.org/annotation/VAR_035449|||http://purl.uniprot.org/annotation/VSP_028620|||http://purl.uniprot.org/annotation/VSP_028621|||http://purl.uniprot.org/annotation/VSP_028622|||http://purl.uniprot.org/annotation/VSP_028623|||http://purl.uniprot.org/annotation/VSP_028624
http://togogenome.org/gene/9606:GPAA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43292                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased function in GPI-anchor attachment to protein.|||Glycosylphosphatidylinositol anchor attachment 1 protein|||Helical|||In GPIBD15.|||In GPIBD15; results in low amounts of GPI-anchored proteins on cell surface.|||In GPIBD15; unknown pathological significance; requires 2 nucleotide substitutions.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on function in GPI-anchor attachment to protein.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087554|||http://purl.uniprot.org/annotation/VAR_080543|||http://purl.uniprot.org/annotation/VAR_080544|||http://purl.uniprot.org/annotation/VAR_080545|||http://purl.uniprot.org/annotation/VAR_080546|||http://purl.uniprot.org/annotation/VAR_080547|||http://purl.uniprot.org/annotation/VAR_080548|||http://purl.uniprot.org/annotation/VSP_009542
http://togogenome.org/gene/9606:SNRNP48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEG0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CHHC U11-48K-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||U11/U12 small nuclear ribonucleoprotein 48 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089544|||http://purl.uniprot.org/annotation/VAR_033678|||http://purl.uniprot.org/annotation/VAR_050812|||http://purl.uniprot.org/annotation/VSP_014640|||http://purl.uniprot.org/annotation/VSP_014641
http://togogenome.org/gene/9606:CTAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75638                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cancer/testis antigen 2|||Disordered|||In isoform LAGE-1A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218923|||http://purl.uniprot.org/annotation/VAR_007855|||http://purl.uniprot.org/annotation/VAR_007856|||http://purl.uniprot.org/annotation/VAR_057512|||http://purl.uniprot.org/annotation/VSP_004301
http://togogenome.org/gene/9606:SELP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16109|||http://purl.uniprot.org/uniprot/Q5R341|||http://purl.uniprot.org/uniprot/Q6NUL9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to ischemic stroke.|||C-type lectin|||Cytoplasmic|||EGF-like|||Endocytosis signal|||Extracellular|||Helical|||Impairs interaction with SELPLG. Abolishes cell rolling on glycan ligands.|||Interaction with SNX17|||N-linked (GlcNAc...) asparagine|||P-selectin|||Reduced frequency in patients with myocardial infarction.|||S-palmitoyl cysteine; alternate|||S-stearoyl cysteine; alternate|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017498|||http://purl.uniprot.org/annotation/VAR_004192|||http://purl.uniprot.org/annotation/VAR_004193|||http://purl.uniprot.org/annotation/VAR_004194|||http://purl.uniprot.org/annotation/VAR_004195|||http://purl.uniprot.org/annotation/VAR_013910|||http://purl.uniprot.org/annotation/VAR_013911|||http://purl.uniprot.org/annotation/VAR_013912|||http://purl.uniprot.org/annotation/VAR_013913|||http://purl.uniprot.org/annotation/VAR_019381|||http://purl.uniprot.org/annotation/VAR_019382|||http://purl.uniprot.org/annotation/VAR_019383|||http://purl.uniprot.org/annotation/VAR_019384|||http://purl.uniprot.org/annotation/VAR_019385|||http://purl.uniprot.org/annotation/VAR_019386|||http://purl.uniprot.org/annotation/VAR_019387|||http://purl.uniprot.org/annotation/VAR_019388|||http://purl.uniprot.org/annotation/VAR_019389
http://togogenome.org/gene/9606:CCDC174                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PII3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 174|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251956|||http://purl.uniprot.org/annotation/VAR_061573
http://togogenome.org/gene/9606:NBPF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAX3|||http://purl.uniprot.org/uniprot/Q96M43                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Neuroblastoma breakpoint family member 4|||Olduvai|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288039
http://togogenome.org/gene/9606:SSTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30874                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Almost abolishes expression. Abolishes membrane localization.|||Cytoplasmic|||Expression levels reduced by 40%. No significant change in ligand binding capacity or affinity. Reduced G protein-mediated cAMP signaling but no effect on G protein-mediated calcium release.|||Expression levels reduced by 50%. Significantly reduced ligand binding capacity but increased affinity. Reduced G protein-mediated cAMP release but no effect on G-protein mediated calcium release.|||Expression levels reduced by 60%.|||Expression levels reduced by 80%.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for ligand binding|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine|||Slightly reduced expression levels. No significant change in ligand binding capacity or affinity. No significant change in G protein-mediated cAMP or calcium release.|||Slightly reduced expression levels. Remains localized in membrane. Abolishes ligand binding and G protein-mediated calcium release.|||Slightly reduced expression levels. Significantly reduced ligand binding capacity but increased affinity. Reduced G protein-mediated cAMP release but no effect on G protein-mediated calcium release.|||Somatostatin receptor type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070120|||http://purl.uniprot.org/annotation/VSP_001922
http://togogenome.org/gene/9606:PTGES3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYT3|||http://purl.uniprot.org/uniprot/B3KUY2|||http://purl.uniprot.org/uniprot/Q15185                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||CS|||Cleavage; by caspase-7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||PXLE motif|||Phosphoserine|||Prostaglandin E synthase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218952|||http://purl.uniprot.org/annotation/VSP_055363|||http://purl.uniprot.org/annotation/VSP_055364|||http://purl.uniprot.org/annotation/VSP_055365
http://togogenome.org/gene/9606:KCNK13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB14                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101762|||http://purl.uniprot.org/annotation/VAR_034052|||http://purl.uniprot.org/annotation/VAR_052429
http://togogenome.org/gene/9606:CCDC167                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0B6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Transmembrane                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 167|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308550
http://togogenome.org/gene/9606:FOXF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12946                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein F1|||In ACDMPV.|||In ACDMPV; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091832|||http://purl.uniprot.org/annotation/VAR_071016|||http://purl.uniprot.org/annotation/VAR_071017|||http://purl.uniprot.org/annotation/VAR_071018|||http://purl.uniprot.org/annotation/VAR_071019|||http://purl.uniprot.org/annotation/VAR_071020|||http://purl.uniprot.org/annotation/VAR_071021|||http://purl.uniprot.org/annotation/VAR_071022|||http://purl.uniprot.org/annotation/VAR_071023|||http://purl.uniprot.org/annotation/VAR_071024|||http://purl.uniprot.org/annotation/VAR_071025|||http://purl.uniprot.org/annotation/VAR_071026|||http://purl.uniprot.org/annotation/VAR_071027|||http://purl.uniprot.org/annotation/VAR_071028|||http://purl.uniprot.org/annotation/VAR_071029|||http://purl.uniprot.org/annotation/VAR_071030|||http://purl.uniprot.org/annotation/VAR_071031|||http://purl.uniprot.org/annotation/VAR_071032|||http://purl.uniprot.org/annotation/VAR_071033|||http://purl.uniprot.org/annotation/VAR_071034|||http://purl.uniprot.org/annotation/VAR_071035|||http://purl.uniprot.org/annotation/VAR_071036|||http://purl.uniprot.org/annotation/VAR_076592
http://togogenome.org/gene/9606:AFP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02771                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Albumin 1|||Albumin 2|||Albumin 3|||Alpha-fetoprotein|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000070|||http://purl.uniprot.org/annotation/PRO_0000001097|||http://purl.uniprot.org/annotation/VAR_012049|||http://purl.uniprot.org/annotation/VAR_033928
http://togogenome.org/gene/9606:DUSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DU40|||http://purl.uniprot.org/uniprot/P28562                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 1|||Loss of phosphatase activity.|||Phosphocysteine intermediate|||Phosphoserine; by MAPK1 and MAPK3|||Rhodanese|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094790|||http://purl.uniprot.org/annotation/VAR_025201|||http://purl.uniprot.org/annotation/VAR_025202
http://togogenome.org/gene/9606:GLI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10070|||http://purl.uniprot.org/uniprot/Q1PSW9|||http://purl.uniprot.org/uniprot/Q59FV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CJS.|||In CJS; loss of DNA-binding; loss of transcription factor activity.|||In CJS; unknown pathological significance; decreased transcription factor activity.|||In HPE9; unknown pathological significance.|||In isoform 1, isoform 2, isoform 3 and isoform 4.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Likely benign variant; associated with N-1520 in Culler-Jones syndrome; decreased transcription factor activity when associated with N-1520.|||Likely benign variant; associated with V-1352 in Culler-Jones syndrome; decreased transcription factor activity when associated with V-1352.|||N6-acetyllysine; by EP300|||No effect on transcription factor activity.|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine|||Polar residues|||Zinc finger protein GLI2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000354050|||http://purl.uniprot.org/annotation/VAR_032975|||http://purl.uniprot.org/annotation/VAR_032976|||http://purl.uniprot.org/annotation/VAR_032977|||http://purl.uniprot.org/annotation/VAR_032978|||http://purl.uniprot.org/annotation/VAR_047303|||http://purl.uniprot.org/annotation/VAR_047304|||http://purl.uniprot.org/annotation/VAR_047305|||http://purl.uniprot.org/annotation/VAR_047306|||http://purl.uniprot.org/annotation/VAR_047307|||http://purl.uniprot.org/annotation/VAR_071700|||http://purl.uniprot.org/annotation/VAR_075214|||http://purl.uniprot.org/annotation/VAR_075215|||http://purl.uniprot.org/annotation/VAR_075216|||http://purl.uniprot.org/annotation/VAR_075217|||http://purl.uniprot.org/annotation/VAR_075218|||http://purl.uniprot.org/annotation/VSP_006877|||http://purl.uniprot.org/annotation/VSP_006878|||http://purl.uniprot.org/annotation/VSP_006879|||http://purl.uniprot.org/annotation/VSP_035708
http://togogenome.org/gene/9606:OR51G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVF5|||http://purl.uniprot.org/uniprot/Q8NGK1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150754|||http://purl.uniprot.org/annotation/VAR_034318|||http://purl.uniprot.org/annotation/VAR_053324|||http://purl.uniprot.org/annotation/VAR_053325|||http://purl.uniprot.org/annotation/VAR_053326|||http://purl.uniprot.org/annotation/VAR_062080
http://togogenome.org/gene/9606:CCDC50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVM0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 50|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066307|||http://purl.uniprot.org/annotation/VAR_050754|||http://purl.uniprot.org/annotation/VAR_050755|||http://purl.uniprot.org/annotation/VSP_014985
http://togogenome.org/gene/9606:ZNF559                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTS4|||http://purl.uniprot.org/uniprot/A0A0A0MTT2|||http://purl.uniprot.org/uniprot/B3KPL8|||http://purl.uniprot.org/uniprot/B4DP29|||http://purl.uniprot.org/uniprot/Q3LIC1|||http://purl.uniprot.org/uniprot/Q9BR84                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 559                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047649|||http://purl.uniprot.org/annotation/VAR_033576|||http://purl.uniprot.org/annotation/VSP_047039|||http://purl.uniprot.org/annotation/VSP_047040
http://togogenome.org/gene/9606:OSGEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPF4                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In GAMOS3.|||In GAMOS3; reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs.|||In GAMOS3; strongly reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs.|||tRNA N6-adenosine threonylcarbamoyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096984|||http://purl.uniprot.org/annotation/VAR_080357|||http://purl.uniprot.org/annotation/VAR_080358|||http://purl.uniprot.org/annotation/VAR_080359|||http://purl.uniprot.org/annotation/VAR_080360|||http://purl.uniprot.org/annotation/VAR_080361|||http://purl.uniprot.org/annotation/VAR_080362|||http://purl.uniprot.org/annotation/VAR_080363|||http://purl.uniprot.org/annotation/VAR_080364|||http://purl.uniprot.org/annotation/VAR_080365|||http://purl.uniprot.org/annotation/VAR_080366|||http://purl.uniprot.org/annotation/VAR_080367|||http://purl.uniprot.org/annotation/VAR_080368|||http://purl.uniprot.org/annotation/VAR_080369|||http://purl.uniprot.org/annotation/VAR_080370
http://togogenome.org/gene/9606:ZNF212                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8N3|||http://purl.uniprot.org/uniprot/B3KQE6|||http://purl.uniprot.org/uniprot/Q9UDV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 212                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047456|||http://purl.uniprot.org/annotation/VAR_052794
http://togogenome.org/gene/9606:CYRIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUQ9                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with RAC1.|||CYFIP-related Rac1 interactor B|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||N-myristoyl glycine|||No effect on interaction with RAC1. Almost abolishes interaction with RAC1; when associated with D-161.|||Removed|||Strongly decreases interaction with RAC1. Almost abolishes interaction with RAC1; when associated with D-150.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187060|||http://purl.uniprot.org/annotation/VAR_019704|||http://purl.uniprot.org/annotation/VSP_056503
http://togogenome.org/gene/9606:USP45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RBV3|||http://purl.uniprot.org/uniprot/Q70EL2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytically inactive. Loss of ability to deubiquitinate ERCC1. Loss of interaction with SPDL1 and ability to deubiquitinate SPDL1.|||Disordered|||In LCA19; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with ERCC1|||Loss of protein expression.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||Significant reduction in interaction with ERCC1.|||Significant reduction in interaction with ERCC1. Complete loss of ability to interact with and deubiquitinate ERCC1; when associated with A-25.|||Significant reduction in interaction with ERCC1. Complete loss of ability to interact with and deubiquitinate ERCC1; when associated with A-26.|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280561|||http://purl.uniprot.org/annotation/VAR_031167|||http://purl.uniprot.org/annotation/VAR_031168|||http://purl.uniprot.org/annotation/VAR_060663|||http://purl.uniprot.org/annotation/VAR_083031|||http://purl.uniprot.org/annotation/VAR_083032|||http://purl.uniprot.org/annotation/VSP_023789|||http://purl.uniprot.org/annotation/VSP_023790|||http://purl.uniprot.org/annotation/VSP_023791|||http://purl.uniprot.org/annotation/VSP_023792|||http://purl.uniprot.org/annotation/VSP_023793
http://togogenome.org/gene/9606:ASZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWH4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1|||Disordered|||In isoform 2.|||Phosphoserine|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066969|||http://purl.uniprot.org/annotation/VAR_024175|||http://purl.uniprot.org/annotation/VSP_056918
http://togogenome.org/gene/9606:PIP4K2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78356                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylserine|||N6-acetyllysine|||PIPK|||Phosphatidylinositol 5-phosphate 4-kinase type-2 beta|||Phosphoserine|||Phosphothreonine|||Removed|||Required for interaction with PIP5K1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185470|||http://purl.uniprot.org/annotation/VSP_010384|||http://purl.uniprot.org/annotation/VSP_010385
http://togogenome.org/gene/9606:ZNF79                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2B0|||http://purl.uniprot.org/uniprot/B4DY65|||http://purl.uniprot.org/uniprot/B7ZAB8|||http://purl.uniprot.org/uniprot/F5H032|||http://purl.uniprot.org/uniprot/Q15937                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 79                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047388|||http://purl.uniprot.org/annotation/VAR_024841|||http://purl.uniprot.org/annotation/VAR_024842|||http://purl.uniprot.org/annotation/VAR_059896
http://togogenome.org/gene/9606:MRPL55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7F7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein mL55|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273099|||http://purl.uniprot.org/annotation/VAR_030082|||http://purl.uniprot.org/annotation/VAR_052045|||http://purl.uniprot.org/annotation/VSP_022477
http://togogenome.org/gene/9606:EIF3CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5ME19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit C-like protein|||N6-acetyllysine|||PCI|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422825
http://togogenome.org/gene/9606:CACNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C184|||http://purl.uniprot.org/uniprot/Q08289|||http://purl.uniprot.org/uniprot/Q59H42|||http://purl.uniprot.org/uniprot/Q5VVH1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In BRGDA4; unknown pathological significance; affects channel activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2a and isoform 2f.|||In isoform 2b and isoform 2cN4.|||In isoform 2c and isoform 2cN2.|||In isoform 2e.|||In isoform 2f and isoform 2g.|||In isoform 2h, isoform 2cN2 and isoform 2cN4.|||Phosphoserine|||Phosphothreonine; by CaMK2D|||Polar residues|||Reduces binding to RRAD; when associated with A-298 and A-374.|||Reduces binding to RRAD; when associated with A-298 and A-376.|||Reduces binding to RRAD; when associated with A-374 and A-376.|||Required for CaMK2D-binding|||SH3|||Voltage-dependent L-type calcium channel subunit beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144051|||http://purl.uniprot.org/annotation/VAR_036350|||http://purl.uniprot.org/annotation/VAR_044041|||http://purl.uniprot.org/annotation/VSP_000626|||http://purl.uniprot.org/annotation/VSP_000627|||http://purl.uniprot.org/annotation/VSP_000628|||http://purl.uniprot.org/annotation/VSP_000629|||http://purl.uniprot.org/annotation/VSP_000630|||http://purl.uniprot.org/annotation/VSP_000631
http://togogenome.org/gene/9606:MAGEB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZ81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen B5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156716
http://togogenome.org/gene/9606:SPPL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLZ2|||http://purl.uniprot.org/uniprot/Q8TCT8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Loss of intramembrane-cleaving activity toward FASLG, ITM2B, TNF and the simian foamy virus envelope glycoprotein gp130.|||Lumenal|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||PA|||PAL|||Signal peptide peptidase-like 2A|||YXXo lysosomal targeting motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073910|||http://purl.uniprot.org/annotation/PRO_5036483279|||http://purl.uniprot.org/annotation/VAR_051790
http://togogenome.org/gene/9606:CEP72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P209                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 72 kDa|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089499|||http://purl.uniprot.org/annotation/VAR_050798|||http://purl.uniprot.org/annotation/VAR_050799|||http://purl.uniprot.org/annotation/VAR_050800|||http://purl.uniprot.org/annotation/VSP_037835|||http://purl.uniprot.org/annotation/VSP_037836
http://togogenome.org/gene/9606:TNIK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKE5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In isoform 2, isoform 5, isoform 6 and isoform 8.|||In isoform 3, isoform 5, isoform 7 and isoform 8.|||In isoform 4, isoform 6, isoform 7 and isoform 8.|||Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation.|||Loss of autophosphorylation.|||Mediates interaction with NEDD4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||TRAF2 and NCK-interacting protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086761|||http://purl.uniprot.org/annotation/VAR_041231|||http://purl.uniprot.org/annotation/VAR_041232|||http://purl.uniprot.org/annotation/VAR_041233|||http://purl.uniprot.org/annotation/VSP_004889|||http://purl.uniprot.org/annotation/VSP_004890|||http://purl.uniprot.org/annotation/VSP_004891
http://togogenome.org/gene/9606:N4BP2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TBK1|||http://purl.uniprot.org/uniprot/Q9UQP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||NEDD4-binding protein 2-like 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318958|||http://purl.uniprot.org/annotation/VSP_031319
http://togogenome.org/gene/9606:STIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR87|||http://purl.uniprot.org/uniprot/B7ZLW5|||http://purl.uniprot.org/uniprot/E9PSF2|||http://purl.uniprot.org/uniprot/Q15468|||http://purl.uniprot.org/uniprot/Q5T0C7|||http://purl.uniprot.org/uniprot/Q7Z626                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MCPH7.|||In isoform 2.|||Interaction with CENPJ|||Interaction with RBM14|||N-acetylmethionine|||PIN1-binding|||Phosphoserine|||Polar residues|||SCL-interrupting locus protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271332|||http://purl.uniprot.org/annotation/VAR_029870|||http://purl.uniprot.org/annotation/VAR_029871|||http://purl.uniprot.org/annotation/VAR_029872|||http://purl.uniprot.org/annotation/VAR_051386|||http://purl.uniprot.org/annotation/VAR_072404|||http://purl.uniprot.org/annotation/VSP_022301
http://togogenome.org/gene/9606:COX7A2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14548|||http://purl.uniprot.org/uniprot/Q6FGA0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7A-related protein, mitochondrial|||Helical|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006154
http://togogenome.org/gene/9606:SCFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVM8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed|||Sec1 family domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206287|||http://purl.uniprot.org/annotation/VAR_019616|||http://purl.uniprot.org/annotation/VSP_047070|||http://purl.uniprot.org/annotation/VSP_047071
http://togogenome.org/gene/9606:CALY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYX4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuron-specific vesicular protein calcyon                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164368|||http://purl.uniprot.org/annotation/VSP_034473|||http://purl.uniprot.org/annotation/VSP_034474|||http://purl.uniprot.org/annotation/VSP_034475
http://togogenome.org/gene/9606:SYNPO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E258|||http://purl.uniprot.org/uniprot/Q9UMS6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin binding|||Basic and acidic residues|||Disordered|||F-actin binding|||F-actin bundling activity|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with ACTN2|||Interaction with BAG3|||Interaction with FLNC|||Interaction with VPS18|||Interaction with YWHAB|||Interaction with ZYX|||Nuclear localization signal|||PDZ|||PPPY motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Synaptopodin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187673|||http://purl.uniprot.org/annotation/VAR_019670|||http://purl.uniprot.org/annotation/VAR_057256|||http://purl.uniprot.org/annotation/VAR_057257|||http://purl.uniprot.org/annotation/VAR_057258|||http://purl.uniprot.org/annotation/VSP_041222|||http://purl.uniprot.org/annotation/VSP_041223|||http://purl.uniprot.org/annotation/VSP_053771|||http://purl.uniprot.org/annotation/VSP_058887
http://togogenome.org/gene/9606:C1orf43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWL3|||http://purl.uniprot.org/uniprot/X6R6S3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Protein C1orf43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089256|||http://purl.uniprot.org/annotation/VSP_014417|||http://purl.uniprot.org/annotation/VSP_014418|||http://purl.uniprot.org/annotation/VSP_014419|||http://purl.uniprot.org/annotation/VSP_014420|||http://purl.uniprot.org/annotation/VSP_014421
http://togogenome.org/gene/9606:HINFP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQA5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes DNA-Binding.|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Histone H4 transcription factor|||In isoform 2.|||Interaction with NPAT|||Required for activation of histone H4 transcription and contributes to DNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047218|||http://purl.uniprot.org/annotation/VAR_019424|||http://purl.uniprot.org/annotation/VAR_026547|||http://purl.uniprot.org/annotation/VAR_026548|||http://purl.uniprot.org/annotation/VAR_038793|||http://purl.uniprot.org/annotation/VSP_044719|||http://purl.uniprot.org/annotation/VSP_044720
http://togogenome.org/gene/9606:GBGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J7Q0Z1|||http://purl.uniprot.org/uniprot/Q8N5D6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Found in FORS blood group carriers; reactivates Forssman antigen synthesis and expression in erythrocytes.|||Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157295|||http://purl.uniprot.org/annotation/VAR_022452|||http://purl.uniprot.org/annotation/VAR_025068|||http://purl.uniprot.org/annotation/VAR_025069|||http://purl.uniprot.org/annotation/VAR_025070|||http://purl.uniprot.org/annotation/VAR_025071|||http://purl.uniprot.org/annotation/VAR_025072|||http://purl.uniprot.org/annotation/VAR_025073|||http://purl.uniprot.org/annotation/VAR_025074|||http://purl.uniprot.org/annotation/VAR_085166|||http://purl.uniprot.org/annotation/VSP_013750|||http://purl.uniprot.org/annotation/VSP_055375
http://togogenome.org/gene/9606:PTPN23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DST5|||http://purl.uniprot.org/uniprot/Q9H3S7                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 2 AA approximate tandem repeats of P-Q|||Abolishes interaction with CHMP4B; when associated with D-202.|||Abolishes interaction with UBAP1.|||BRO1|||Basic and acidic residues|||Disordered|||His|||In NEDBASS.|||In NEDBASS; unknown pathological significance.|||In NEDBASS; when associated in cis with H-1017; unknown pathological significance.|||In NEDBASS; when associated in cis with R-583; unknown pathological significance.|||Nearly abolishes interaction with CHMP4B. Abolishes interaction with CHMP4B; when associated with D-206.|||Omega-N-methylarginine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TPR 1|||TPR 2|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094777|||http://purl.uniprot.org/annotation/VAR_022682|||http://purl.uniprot.org/annotation/VAR_022683|||http://purl.uniprot.org/annotation/VAR_084289|||http://purl.uniprot.org/annotation/VAR_084290|||http://purl.uniprot.org/annotation/VAR_084291|||http://purl.uniprot.org/annotation/VAR_084292|||http://purl.uniprot.org/annotation/VAR_084293|||http://purl.uniprot.org/annotation/VAR_084294|||http://purl.uniprot.org/annotation/VAR_084295|||http://purl.uniprot.org/annotation/VAR_084296|||http://purl.uniprot.org/annotation/VAR_084297|||http://purl.uniprot.org/annotation/VAR_084298|||http://purl.uniprot.org/annotation/VAR_084299|||http://purl.uniprot.org/annotation/VAR_084300|||http://purl.uniprot.org/annotation/VAR_084301|||http://purl.uniprot.org/annotation/VAR_084302|||http://purl.uniprot.org/annotation/VAR_084303|||http://purl.uniprot.org/annotation/VAR_084304
http://togogenome.org/gene/9606:CHODL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFS2|||http://purl.uniprot.org/uniprot/Q9H9P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Chondrolectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017415|||http://purl.uniprot.org/annotation/VSP_017275|||http://purl.uniprot.org/annotation/VSP_017276|||http://purl.uniprot.org/annotation/VSP_043300
http://togogenome.org/gene/9606:ADAM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C3I4|||http://purl.uniprot.org/uniprot/Q08AL8|||http://purl.uniprot.org/uniprot/Q9P0K1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interactions with YWHAB and YWHAZ; when associated with A-834.|||Abolishes interactions with YWHAB and YWHAZ; when associated with A-857.|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 22|||Disordered|||EGF-like|||Extracellular|||Helical|||In DEE61; unknown pathological significance; loss of interaction with LGI1; no effect on DLG4-binding, nor on subcellular location.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029112|||http://purl.uniprot.org/annotation/PRO_0000029113|||http://purl.uniprot.org/annotation/PRO_5014306701|||http://purl.uniprot.org/annotation/PRO_5033014662|||http://purl.uniprot.org/annotation/VAR_020057|||http://purl.uniprot.org/annotation/VAR_051589|||http://purl.uniprot.org/annotation/VAR_051590|||http://purl.uniprot.org/annotation/VAR_080496|||http://purl.uniprot.org/annotation/VSP_005482|||http://purl.uniprot.org/annotation/VSP_005483|||http://purl.uniprot.org/annotation/VSP_005484
http://togogenome.org/gene/9606:HRH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35367                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Histamine H1 receptor|||Important for agonist binding|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069676|||http://purl.uniprot.org/annotation/VAR_033476|||http://purl.uniprot.org/annotation/VAR_035761|||http://purl.uniprot.org/annotation/VAR_049410
http://togogenome.org/gene/9606:POM121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cisternal side|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Nuclear envelope pore membrane protein POM 121|||Phosphoserine|||Polar residues|||Pore side|||Pro residues|||Required for targeting to the nucleus and nuclear pore complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346773|||http://purl.uniprot.org/annotation/VAR_045905|||http://purl.uniprot.org/annotation/VSP_035010|||http://purl.uniprot.org/annotation/VSP_035011
http://togogenome.org/gene/9606:TPSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZJ3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Tryptase delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027483|||http://purl.uniprot.org/annotation/PRO_0000027484|||http://purl.uniprot.org/annotation/VAR_016870|||http://purl.uniprot.org/annotation/VAR_016871|||http://purl.uniprot.org/annotation/VAR_016872|||http://purl.uniprot.org/annotation/VSP_008319
http://togogenome.org/gene/9606:RPL7L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DKI1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Ribosomal protein uL30-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000104659|||http://purl.uniprot.org/annotation/VSP_056504
http://togogenome.org/gene/9606:ZFP64                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQX0|||http://purl.uniprot.org/uniprot/Q9NTW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6, isoform 1 and isoform 2.|||In isoform 6.|||Phosphoserine|||Polar residues|||Zinc finger protein 64                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047308|||http://purl.uniprot.org/annotation/VAR_028019|||http://purl.uniprot.org/annotation/VAR_028020|||http://purl.uniprot.org/annotation/VAR_035564|||http://purl.uniprot.org/annotation/VAR_035565|||http://purl.uniprot.org/annotation/VAR_082942|||http://purl.uniprot.org/annotation/VAR_082943|||http://purl.uniprot.org/annotation/VSP_007285|||http://purl.uniprot.org/annotation/VSP_007286|||http://purl.uniprot.org/annotation/VSP_038213|||http://purl.uniprot.org/annotation/VSP_038214|||http://purl.uniprot.org/annotation/VSP_046896|||http://purl.uniprot.org/annotation/VSP_046897|||http://purl.uniprot.org/annotation/VSP_046898|||http://purl.uniprot.org/annotation/VSP_060092
http://togogenome.org/gene/9606:EXOC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60645|||http://purl.uniprot.org/uniprot/Q69YP2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue                                                                                  ^@                                                                                  Exocyst complex component 3|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118925
http://togogenome.org/gene/9606:ZSCAN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAM6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||SCAN box|||Zinc finger and SCAN domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047751|||http://purl.uniprot.org/annotation/VAR_052926
http://togogenome.org/gene/9606:CCL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C1Q1|||http://purl.uniprot.org/uniprot/D0EI67|||http://purl.uniprot.org/uniprot/P13501                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Antagonist of the chemokine receptors CCR1 and CCR3.|||C-C motif chemokine|||C-C motif chemokine 5|||Chemokine interleukin-8-like|||Cleavage; by DPP4|||Methionine sulfoxide|||No effect on inhibition of activity by tick evasin-4.|||O-glycosylated.|||O-linked (GalNAc...) serine; partial|||RANTES(3-68)|||RANTES(4-68)|||Reduced inhibition of activity by tick evasin-4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005175|||http://purl.uniprot.org/annotation/PRO_0000005176|||http://purl.uniprot.org/annotation/PRO_0000005177|||http://purl.uniprot.org/annotation/PRO_5014205493|||http://purl.uniprot.org/annotation/PRO_5019782608|||http://purl.uniprot.org/annotation/VAR_043043
http://togogenome.org/gene/9606:TDRD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60522                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4|||Tudor 5|||Tudor 6|||Tudor 7|||Tudor 8|||Tudor domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183167|||http://purl.uniprot.org/annotation/VAR_029050|||http://purl.uniprot.org/annotation/VAR_029051|||http://purl.uniprot.org/annotation/VAR_029052|||http://purl.uniprot.org/annotation/VAR_052423|||http://purl.uniprot.org/annotation/VSP_044801
http://togogenome.org/gene/9606:RAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62826                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes steric hindrance that traps the essential Q-69 in an unreactive position, and causes slow GTP hydrolysis in wild-type. Loss of one hydrogen bond with the gamma phosphate group of bound GTP.|||Blocks DNA replication; when associated with L-69.|||Decreased acetylation.|||Essential for GTP hydrolysis|||GTP-binding nuclear protein Ran|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5.|||Has low binding affinity for GTP and GDP. Decreases nuclear import of proteins and RNA. Stabilizes the interaction with RCC1. No effect on nuclear location during interphase. Loss of activity in triggering microtubule assembly at mitotic chromosomes.|||Interaction with RANBP1|||Loss of normal mitotic chromosome segregation and defective mitotic spindle orientation.|||Loss of normal mitotic chromosome segregation and formation of sister chromatid bridges.|||Mimics acetylation; enhances the nuclear export of RELA/p65.|||Minor effect on the interaction with the alpha phosphate group of bound GTP.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No effect on GTPase activity. Abolishes interaction with RANBP1.|||Phosphothreonine|||Probable loss of interaction with NUTF2. Loss of transport to the nucleus.|||Removed|||Strongly decreased GTPase activity. Probably locked in the GTP-bound form. Loss of interaction with NUTF2. Decreases nuclear location and leads to cytoplasmic location during interphase. Loss of function in importin-mediated protein nuclear import. High activity in triggering microtubule assembly at mitotic chromosomes. Blocks DNA replication; when associated with V-19.|||Strongly decreases the relase of bound GDP.|||Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208696
http://togogenome.org/gene/9606:DGKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6T7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  DAGKc|||Diacylglycerol kinase beta|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine|||Required for association with membranes and function in neurite spine formation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218457|||http://purl.uniprot.org/annotation/VAR_048858|||http://purl.uniprot.org/annotation/VSP_021898|||http://purl.uniprot.org/annotation/VSP_021899
http://togogenome.org/gene/9606:OR52N5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK9|||http://purl.uniprot.org/uniprot/Q8NH56                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 52N5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150789|||http://purl.uniprot.org/annotation/VAR_047147
http://togogenome.org/gene/9606:LCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80188                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neutrophil gelatinase-associated lipocalin|||Pyrrolidone carboxylic acid|||Strongly reduced affinity for catecholate-type ferric siderophores; when associated with A-145.|||Strongly reduced affinity for catecholate-type ferric siderophores; when associated with A-154.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017933|||http://purl.uniprot.org/annotation/VSP_039780
http://togogenome.org/gene/9606:FAM25C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3EWG3|||http://purl.uniprot.org/uniprot/B3EWG5|||http://purl.uniprot.org/uniprot/B3EWG6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM25A|||Protein FAM25C|||Protein FAM25G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270919|||http://purl.uniprot.org/annotation/PRO_0000416047|||http://purl.uniprot.org/annotation/PRO_0000416048|||http://purl.uniprot.org/annotation/VAR_054062
http://togogenome.org/gene/9606:AQP12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXF9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-12A|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||NPA 1|||NPA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063971
http://togogenome.org/gene/9606:CLEC14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 14 member A|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017377
http://togogenome.org/gene/9606:OR2L13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW96|||http://purl.uniprot.org/uniprot/Q8N349                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2L13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150490|||http://purl.uniprot.org/annotation/VAR_053148|||http://purl.uniprot.org/annotation/VAR_062025
http://togogenome.org/gene/9606:LRFN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type-III domain-containing protein 2|||Loss of DLG1-, DLG3- and DLG4-binding.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014838|||http://purl.uniprot.org/annotation/VAR_049894
http://togogenome.org/gene/9606:PKN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16512                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes Serine/threonine-protein kinase activity.|||Abolishes cleavage by caspase-3 and formation of 70 kDa fragment.|||Abolishes cleavage by caspase-3 and formation of AF1 fragment.|||Abolishes cleavage by caspase-3 and formation of AF3 fragment.|||Abolishes interaction with bacterial SspH1.|||C2|||Cleavage; by caspase-3|||Decreases interaction with bacterial SspH1.|||Disordered|||Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Polar residues|||Protein kinase|||Proton acceptor|||REM-1 1|||REM-1 2|||REM-1 3|||Removed|||Serine/threonine-protein kinase N1|||Substantial reduction of autophosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055719|||http://purl.uniprot.org/annotation/VAR_014937|||http://purl.uniprot.org/annotation/VAR_042337|||http://purl.uniprot.org/annotation/VAR_042338|||http://purl.uniprot.org/annotation/VAR_042339|||http://purl.uniprot.org/annotation/VAR_042340|||http://purl.uniprot.org/annotation/VAR_042341|||http://purl.uniprot.org/annotation/VAR_042342|||http://purl.uniprot.org/annotation/VAR_042343|||http://purl.uniprot.org/annotation/VAR_042344|||http://purl.uniprot.org/annotation/VAR_042345|||http://purl.uniprot.org/annotation/VSP_038143|||http://purl.uniprot.org/annotation/VSP_039213|||http://purl.uniprot.org/annotation/VSP_039214
http://togogenome.org/gene/9606:MEGF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6BM72                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||EMI|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Multiple epidermal growth factor-like domains protein 11|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309735|||http://purl.uniprot.org/annotation/VAR_036990|||http://purl.uniprot.org/annotation/VAR_059261|||http://purl.uniprot.org/annotation/VAR_059262|||http://purl.uniprot.org/annotation/VAR_059263|||http://purl.uniprot.org/annotation/VAR_059264|||http://purl.uniprot.org/annotation/VAR_059265|||http://purl.uniprot.org/annotation/VSP_029246|||http://purl.uniprot.org/annotation/VSP_029247|||http://purl.uniprot.org/annotation/VSP_029248|||http://purl.uniprot.org/annotation/VSP_029249|||http://purl.uniprot.org/annotation/VSP_029250|||http://purl.uniprot.org/annotation/VSP_029251|||http://purl.uniprot.org/annotation/VSP_029252
http://togogenome.org/gene/9606:TOMM70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94826                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Mitochondrial import receptor subunit TOM70|||Mitochondrial intermembrane|||N-acetylalanine|||N6-acetyllysine|||No effect on interaction with HSP90AA1.|||Omega-N-methylarginine|||Phosphoserine|||Removed|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Unable to induce IRF3 activation upon Sendai virus infection. Loss of interaction with HSPA8 and HSP90AA1. No effect on mitochondrial location.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106336
http://togogenome.org/gene/9606:COL1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02452                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyproline|||4-hydroxyproline|||5-hydroxylysine|||5-hydroxylysine; alternate|||Allysine|||C-terminal propeptide|||Cell attachment site|||Cleavage; by collagenase|||Cleavage; by procollagen C-endopeptidase|||Cleavage; by procollagen N-endopeptidase|||Collagen alpha-1(I) chain|||Disordered|||Fibrillar collagen NC1|||Found in a patient with isolated osteopenia and vascular rupture; unknown pathological significance.|||Found in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure.|||Found in a patient with mild osteogenesis imperfecta; uncertain pathological significance.|||In CAFYD.|||In EDSCL1.|||In OI.|||In OI1 and OI2; mild to moderate form.|||In OI1 and OIEDS1; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls.|||In OI1.|||In OI1; de novo mutation; unknown pathological significance.|||In OI1; mild form.|||In OI1; mild phenotype.|||In OI1; patient diagnosed with OI1/OI4.|||In OI1; the patient also has mutation Glu-1219; unknown pathological significance.|||In OI2 and OI3; extremely severe form.|||In OI2 and OI3; moderate to lethal form.|||In OI2, OI3 and OI4; mild to lethal form.|||In OI2.|||In OI2; impaired pro-alpha chain association.|||In OI2; lethal form.|||In OI2; mild to moderate form.|||In OI2; rare variant; unknown pathological significance.|||In OI2; results in slow procollagen cleavage by N-proteinase.|||In OI3 and OI2.|||In OI3 and OI4.|||In OI3 and OI4; mild form.|||In OI3 and OIEDS1; small decrease of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls.|||In OI3.|||In OI3; mild to moderate form.|||In OI3; severe form.|||In OI3; severe.|||In OI4, OI2 and OI3.|||In OI4.|||In OI4; mild form.|||In OI; moderate form.|||In OIEDS1.|||In OIEDS1; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls.|||In OIEDS1; affects dimer formation, helix stability and organization of collagen fibrils.|||In OIEDS1; decreased N-terminal propeptide processing.|||In OIEDS1; severely decreased cleavage of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls.|||In OIEDS1; small decrease of N-terminal propeptide; affects collagen fibril organization; collagen dermal fibrils in patients have smaller diameters than in age-matched controls.|||Interchain|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Nonhelical region (C-terminal)|||Nonhelical region (N-terminal)|||O-linked (Gal...) hydroxylysine; alternate|||Phosphoserine|||Pro residues|||Pyrrolidone carboxylic acid|||Triple-helical region|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005719|||http://purl.uniprot.org/annotation/PRO_0000005720|||http://purl.uniprot.org/annotation/PRO_0000005721|||http://purl.uniprot.org/annotation/VAR_001642|||http://purl.uniprot.org/annotation/VAR_001643|||http://purl.uniprot.org/annotation/VAR_001644|||http://purl.uniprot.org/annotation/VAR_001645|||http://purl.uniprot.org/annotation/VAR_001646|||http://purl.uniprot.org/annotation/VAR_001647|||http://purl.uniprot.org/annotation/VAR_001648|||http://purl.uniprot.org/annotation/VAR_001649|||http://purl.uniprot.org/annotation/VAR_001650|||http://purl.uniprot.org/annotation/VAR_001651|||http://purl.uniprot.org/annotation/VAR_001652|||http://purl.uniprot.org/annotation/VAR_001653|||http://purl.uniprot.org/annotation/VAR_001654|||http://purl.uniprot.org/annotation/VAR_001655|||http://purl.uniprot.org/annotation/VAR_001656|||http://purl.uniprot.org/annotation/VAR_001657|||http://purl.uniprot.org/annotation/VAR_001658|||http://purl.uniprot.org/annotation/VAR_001660|||http://purl.uniprot.org/annotation/VAR_001661|||http://purl.uniprot.org/annotation/VAR_001662|||http://purl.uniprot.org/annotation/VAR_001663|||http://purl.uniprot.org/annotation/VAR_001664|||http://purl.uniprot.org/annotation/VAR_001665|||http://purl.uniprot.org/annotation/VAR_001666|||http://purl.uniprot.org/annotation/VAR_001667|||http://purl.uniprot.org/annotation/VAR_001668|||http://purl.uniprot.org/annotation/VAR_001669|||http://purl.uniprot.org/annotation/VAR_001670|||http://purl.uniprot.org/annotation/VAR_001671|||http://purl.uniprot.org/annotation/VAR_001672|||http://purl.uniprot.org/annotation/VAR_001673|||http://purl.uniprot.org/annotation/VAR_001674|||http://purl.uniprot.org/annotation/VAR_001676|||http://purl.uniprot.org/annotation/VAR_001677|||http://purl.uniprot.org/annotation/VAR_001678|||http://purl.uniprot.org/annotation/VAR_001679|||http://purl.uniprot.org/annotation/VAR_001680|||http://purl.uniprot.org/annotation/VAR_001681|||http://purl.uniprot.org/annotation/VAR_001682|||http://purl.uniprot.org/annotation/VAR_001683|||http://purl.uniprot.org/annotation/VAR_001684|||http://purl.uniprot.org/annotation/VAR_001685|||http://purl.uniprot.org/annotation/VAR_001686|||http://purl.uniprot.org/annotation/VAR_001687|||http://purl.uniprot.org/annotation/VAR_001688|||http://purl.uniprot.org/annotation/VAR_001689|||http://purl.uniprot.org/annotation/VAR_001690|||http://purl.uniprot.org/annotation/VAR_001691|||http://purl.uniprot.org/annotation/VAR_001692|||http://purl.uniprot.org/annotation/VAR_001693|||http://purl.uniprot.org/annotation/VAR_001694|||http://purl.uniprot.org/annotation/VAR_001695|||http://purl.uniprot.org/annotation/VAR_001696|||http://purl.uniprot.org/annotation/VAR_001697|||http://purl.uniprot.org/annotation/VAR_001698|||http://purl.uniprot.org/annotation/VAR_001699|||http://purl.uniprot.org/annotation/VAR_001700|||http://purl.uniprot.org/annotation/VAR_001701|||http://purl.uniprot.org/annotation/VAR_001702|||http://purl.uniprot.org/annotation/VAR_001703|||http://purl.uniprot.org/annotation/VAR_001704|||http://purl.uniprot.org/annotation/VAR_001705|||http://purl.uniprot.org/annotation/VAR_001707|||http://purl.uniprot.org/annotation/VAR_001708|||http://purl.uniprot.org/annotation/VAR_001709|||http://purl.uniprot.org/annotation/VAR_001710|||http://purl.uniprot.org/annotation/VAR_001711|||http://purl.uniprot.org/annotation/VAR_001712|||http://purl.uniprot.org/annotation/VAR_001713|||http://purl.uniprot.org/annotation/VAR_001714|||http://purl.uniprot.org/annotation/VAR_001715|||http://purl.uniprot.org/annotation/VAR_001716|||http://purl.uniprot.org/annotation/VAR_001717|||http://purl.uniprot.org/annotation/VAR_001718|||http://purl.uniprot.org/annotation/VAR_001719|||http://purl.uniprot.org/annotation/VAR_001720|||http://purl.uniprot.org/annotation/VAR_001721|||http://purl.uniprot.org/annotation/VAR_001722|||http://purl.uniprot.org/annotation/VAR_001723|||http://purl.uniprot.org/annotation/VAR_001724|||http://purl.uniprot.org/annotation/VAR_001725|||http://purl.uniprot.org/annotation/VAR_001726|||http://purl.uniprot.org/annotation/VAR_001727|||http://purl.uniprot.org/annotation/VAR_001728|||http://purl.uniprot.org/annotation/VAR_001729|||http://purl.uniprot.org/annotation/VAR_001730|||http://purl.uniprot.org/annotation/VAR_001731|||http://purl.uniprot.org/annotation/VAR_001732|||http://purl.uniprot.org/annotation/VAR_001733|||http://purl.uniprot.org/annotation/VAR_001734|||http://purl.uniprot.org/annotation/VAR_001735|||http://purl.uniprot.org/annotation/VAR_001736|||http://purl.uniprot.org/annotation/VAR_001737|||http://purl.uniprot.org/annotation/VAR_008118|||http://purl.uniprot.org/annotation/VAR_013579|||http://purl.uniprot.org/annotation/VAR_030013|||http://purl.uniprot.org/annotation/VAR_030014|||http://purl.uniprot.org/annotation/VAR_030015|||http://purl.uniprot.org/annotation/VAR_030016|||http://purl.uniprot.org/annotation/VAR_030017|||http://purl.uniprot.org/annotation/VAR_033097|||http://purl.uniprot.org/annotation/VAR_033778|||http://purl.uniprot.org/annotation/VAR_033779|||http://purl.uniprot.org/annotation/VAR_033780|||http://purl.uniprot.org/annotation/VAR_033781|||http://purl.uniprot.org/annotation/VAR_063290|||http://purl.uniprot.org/annotation/VAR_063291|||http://purl.uniprot.org/annotation/VAR_063292|||http://purl.uniprot.org/annotation/VAR_063293|||http://purl.uniprot.org/annotation/VAR_063294|||http://purl.uniprot.org/annotation/VAR_063295|||http://purl.uniprot.org/annotation/VAR_063296|||http://purl.uniprot.org/annotation/VAR_063297|||http://purl.uniprot.org/annotation/VAR_063298|||http://purl.uniprot.org/annotation/VAR_063299|||http://purl.uniprot.org/annotation/VAR_063300|||http://purl.uniprot.org/annotation/VAR_063301|||http://purl.uniprot.org/annotation/VAR_063302|||http://purl.uniprot.org/annotation/VAR_063303|||http://purl.uniprot.org/annotation/VAR_063304|||http://purl.uniprot.org/annotation/VAR_063305|||http://purl.uniprot.org/annotation/VAR_063306|||http://purl.uniprot.org/annotation/VAR_063307|||http://purl.uniprot.org/annotation/VAR_063308|||http://purl.uniprot.org/annotation/VAR_063309|||http://purl.uniprot.org/annotation/VAR_063310|||http://purl.uniprot.org/annotation/VAR_063311|||http://purl.uniprot.org/annotation/VAR_063312|||http://purl.uniprot.org/annotation/VAR_063313|||http://purl.uniprot.org/annotation/VAR_063314|||http://purl.uniprot.org/annotation/VAR_063315|||http://purl.uniprot.org/annotation/VAR_063316|||http://purl.uniprot.org/annotation/VAR_063317|||http://purl.uniprot.org/annotation/VAR_063318|||http://purl.uniprot.org/annotation/VAR_063319|||http://purl.uniprot.org/annotation/VAR_063320|||http://purl.uniprot.org/annotation/VAR_063321|||http://purl.uniprot.org/annotation/VAR_063322|||http://purl.uniprot.org/annotation/VAR_063323|||http://purl.uniprot.org/annotation/VAR_063324|||http://purl.uniprot.org/annotation/VAR_063325|||http://purl.uniprot.org/annotation/VAR_063326|||http://purl.uniprot.org/annotation/VAR_063327|||http://purl.uniprot.org/annotation/VAR_063328|||http://purl.uniprot.org/annotation/VAR_063329|||http://purl.uniprot.org/annotation/VAR_063330|||http://purl.uniprot.org/annotation/VAR_063331|||http://purl.uniprot.org/annotation/VAR_063332|||http://purl.uniprot.org/annotation/VAR_063333|||http://purl.uniprot.org/annotation/VAR_063334|||http://purl.uniprot.org/annotation/VAR_063335|||http://purl.uniprot.org/annotation/VAR_063336|||http://purl.uniprot.org/annotation/VAR_063337|||http://purl.uniprot.org/annotation/VAR_063338|||http://purl.uniprot.org/annotation/VAR_063339|||http://purl.uniprot.org/annotation/VAR_063340|||http://purl.uniprot.org/annotation/VAR_063341|||http://purl.uniprot.org/annotation/VAR_063342|||http://purl.uniprot.org/annotation/VAR_066385|||http://purl.uniprot.org/annotation/VAR_074158|||http://purl.uniprot.org/annotation/VAR_074159|||http://purl.uniprot.org/annotation/VAR_085148|||http://purl.uniprot.org/annotation/VAR_085149|||http://purl.uniprot.org/annotation/VAR_085150|||http://purl.uniprot.org/annotation/VAR_085151|||http://purl.uniprot.org/annotation/VAR_085152
http://togogenome.org/gene/9606:TRMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXH9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Trm1 methyltransferase|||tRNA (guanine(26)-N(2))-dimethyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147671|||http://purl.uniprot.org/annotation/VSP_016720
http://togogenome.org/gene/9606:SLC9A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAH2|||http://purl.uniprot.org/uniprot/P19634                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes membrane localization.|||Abolishes plasma membrane localization. Reduces greatly sodium:proton antiporter activity.|||Abolishes sodium:proton antiporter activity.|||Almost complete loss of activity.|||Almost complete loss of activity. Reduces membrane localization.|||Cation/H+ exchanger|||Channel pore-lining|||Confers pH-dependent PI(4,5)P2 binding|||Cytoplasmic|||Decreases sodium:proton antiporter activity by 50%; when associated with A-577.|||Decreases sodium:proton antiporter activity by 50%; when associated with A-578.|||Disordered|||Does not affect membrane localization. Abolishes sodium:proton antiporter activity.|||Does not affect membrane localization. Decreases sodium:proton antiporter activity. Reduces Vmax and Km for Na(+) and a slightly reduced Vmax and Km for Li(+). Decreases sodium:proton antiporter activity; when associated with Q-217. Reduces Vmax for Na(+) and Li(+); when associated with Q-217.|||Does not affect membrane localization. Does not affect sodium:proton antiporter activity.|||Does not affect membrane localization. Does not affect sodium:proton antiporter activity. Decreases sodium:proton antiporter activity; when associated with N-226. Reduces Vmax for Na(+) and Li(+); when associated with D-226.|||Does not affect plasma membrane localization.|||Does not affect sodium:proton antiporter activity.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In LIKNS; causes reduced expression of the mutant protein; hypoglycosylated; does not localize properly at the plasma membrane; small residual activity.|||In LIKNS; unknown pathological significance.|||In isoform 2.|||Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane.|||Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane. Abolishes interaction with TESC.|||Interaction with CALM1|||Interaction with CHP2|||Interaction with PPP3CA|||Interaction with TESC|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||PI(4,5)P2-binding region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces activity.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-518.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-522.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-526.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-527.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-530.|||Reduces interaction with CHP1 and the exchange activity; when associated with Q-531.|||Sodium/hydrogen exchanger 1|||Sodium/hydrogen exchanger regulatory region|||Strongly reduced interaction with CHP2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052347|||http://purl.uniprot.org/annotation/VAR_050231|||http://purl.uniprot.org/annotation/VAR_073439|||http://purl.uniprot.org/annotation/VAR_082153|||http://purl.uniprot.org/annotation/VSP_022101|||http://purl.uniprot.org/annotation/VSP_022102
http://togogenome.org/gene/9606:AMBRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6T1|||http://purl.uniprot.org/uniprot/Q9C0C7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolished cleavage by caspases without affecting cleavage by calpains.|||Abolished interaction with DDB1.|||Abolished interaction with LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C).|||Abolished interaction with PPP2CA and MYC, leading to decreased MYC dephosphorylation; when associated with 1206-A--A-1208. Abolished interaction with PPP2CA and FOXO3, leading to decreased FOXO3 dephosphorylation; when associated with 1206-A--A-1208.|||Abolished interaction with PPP2CA and MYC, leading to decreased MYC dephosphorylation; when associated with 275-A--A-277. Abolished interaction with PPP2CA and FOXO3, leading to decreased FOXO3 dephosphorylation; when associated with 275-A--A-277.|||Abolished interaction with TRAF6.|||Abolished phosphorylation by CHUK/IKKA, leading to impaired interaction with ATG8 family proteins and reduced mitophagic activity.|||Activating molecule in BECN1-regulated autophagy protein 1|||Asymmetric dimethylarginine|||Cleavage; by caspase-6, caspase-7 and caspase-8|||Disordered|||Does not affect interaction with TRAF6.|||Found in a child with spina bifida; unknown pathological significance; reduced induction of autophagy.|||Found in a fetus with anencephaly and spina bifida; unknown pathological significance; does not impair induction of autophagy.|||Found in a fetus with encephalocele and spina bifida; unknown pathological significance; reduced induction of autophagy.|||Found in a fetus with encephalocele; unknown pathological significance; reduced induction of autophagy.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired phosphorylation by MTOR, leading to strong induction of autophagy. Does not affect interaction with DDB1.|||In TAT1 mutant; abolished interaction with DYNLL1 and DYNLL2, leading to constitutive induction of autophagy.|||In TAT2 mutant; abolished interaction with DYNLL1 and DYNLL2, leading to constitutive induction of autophagy.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Interaction with DDB1|||LIR|||Phospho-mimetic mutant; abolished ability to promote autophagy. Does not affect interaction with DDB1.|||Phospho-mimetic mutant; increased interaction with ATG8 family proteins and increased mitophagic activity.|||Phosphoserine|||Phosphoserine; by IKKA|||Phosphoserine; by MTOR|||Polar residues|||Pro residues|||PxP motif 1|||PxP motif 2|||TQT motif 1|||TQT motif 2|||WD|||WD 1|||WD 2|||WD 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315703|||http://purl.uniprot.org/annotation/VAR_085051|||http://purl.uniprot.org/annotation/VAR_085052|||http://purl.uniprot.org/annotation/VAR_085053|||http://purl.uniprot.org/annotation/VAR_085054|||http://purl.uniprot.org/annotation/VAR_085055|||http://purl.uniprot.org/annotation/VSP_030654|||http://purl.uniprot.org/annotation/VSP_030655|||http://purl.uniprot.org/annotation/VSP_030656|||http://purl.uniprot.org/annotation/VSP_030657|||http://purl.uniprot.org/annotation/VSP_045989|||http://purl.uniprot.org/annotation/VSP_045990
http://togogenome.org/gene/9606:SFTPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNP6|||http://purl.uniprot.org/uniprot/Q8IWL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  4-hydroxyproline|||C-type lectin|||Collagen-like|||Disordered|||In ILD1.|||In ILD1; impaired secretion.|||In ILD1; unknown pathological significance; impaired secretion.|||In allele 6A and allele 6A(5).|||In allele 6A(2).|||In isoform 2.|||Interchain|||May be associated with susceptibility to idiopathic pulmonary fibrosis in smokers; allele 6A(4) and allele 6A(5); does not affect secretion.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Pulmonary surfactant-associated protein A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017457|||http://purl.uniprot.org/annotation/PRO_5002803728|||http://purl.uniprot.org/annotation/VAR_004184|||http://purl.uniprot.org/annotation/VAR_012231|||http://purl.uniprot.org/annotation/VAR_012232|||http://purl.uniprot.org/annotation/VAR_012233|||http://purl.uniprot.org/annotation/VAR_021292|||http://purl.uniprot.org/annotation/VAR_063517|||http://purl.uniprot.org/annotation/VAR_086118|||http://purl.uniprot.org/annotation/VAR_086119|||http://purl.uniprot.org/annotation/VAR_086120|||http://purl.uniprot.org/annotation/VAR_086121|||http://purl.uniprot.org/annotation/VSP_046802
http://togogenome.org/gene/9606:CCL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00175                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-C motif chemokine 24|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005232|||http://purl.uniprot.org/annotation/VAR_018404|||http://purl.uniprot.org/annotation/VAR_048710|||http://purl.uniprot.org/annotation/VAR_048711|||http://purl.uniprot.org/annotation/VAR_048712
http://togogenome.org/gene/9606:METTL25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6Q8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Probable methyltransferase-like protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252148|||http://purl.uniprot.org/annotation/VAR_027779
http://togogenome.org/gene/9606:SORT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99523                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abrogates interaction with GGA1 and impairs localization to the Golgi.|||Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795.|||Abrogates propeptide cleavage.|||BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||BNR 7|||BNR 8|||BNR 9|||Cytoplasmic|||DXXLL motif involved in the interaction with GGA1|||Endocytosis signal|||Extracellular|||Golgi to endosome transport and interactions with GGA1 and GGA2|||Helical|||In isoform 2.|||Interactions with LRPAP1 and NGFB|||Intrachain binding of the propeptide and the extracellular domain|||Loss of palmitoylation. Decreased recycling from endosomes to the Golgi apparatus. Increased lysosomal degradation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduces endocytosis and Golgi to endosome sorting; when associated with A-792.|||Reduces endocytosis and Golgi to endosome sorting; when associated with A-795.|||Reduces interaction with GGA1.|||Removed in mature form|||S-palmitoyl cysteine|||Sortilin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033162|||http://purl.uniprot.org/annotation/PRO_0000033163|||http://purl.uniprot.org/annotation/VAR_053681|||http://purl.uniprot.org/annotation/VSP_046239|||http://purl.uniprot.org/annotation/VSP_046240
http://togogenome.org/gene/9606:CISD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ45                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes absorption in the 300-500 nm range.|||CDGSH iron-sulfur domain-containing protein 1|||Cytoplasmic|||Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster; when associated with Cys-87.|||Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster; when associated with Ile-55. Markedly decreases the transfer rate of the [2Fe-2S] cluster. Abolishes iron transfer to the mitochondrial matrix.|||Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Does not affect absorption in the 300-500 nm range. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster.|||Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical; Signal-anchor for type III membrane protein|||N-acetylserine|||N6-acetyllysine; alternate|||Removed|||Schiff-base intermediate with pyridoxal 5'-phosphate|||Slighly reduces the transfer rate of the [2Fe-2S] cluster.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089803
http://togogenome.org/gene/9606:CHTOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3Y2                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chromatin target of PRMT1 protein|||Disordered|||GAR motif; involved in 5hmC binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with PRMT1|||Loss of 5hmc binding; when associated with A-195; A-197; A-199 and A-201.|||Loss of 5hmc binding; when associated with A-195; A-197; A-199 and A-203.|||Loss of 5hmc binding; when associated with A-195; A-197; A-201 and A-203.|||Loss of 5hmc binding; when associated with A-195; A-199; A-201 and A-203.|||Loss of 5hmc binding; when associated with A-197; A-199; A-201 and A-203.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089263|||http://purl.uniprot.org/annotation/VSP_017277|||http://purl.uniprot.org/annotation/VSP_040496
http://togogenome.org/gene/9606:HTRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92743                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||IGFBP N-terminal|||In CADASIL2.|||In CADASIL2; loss of proteolytic activity.|||In CADASIL2; partial loss of proteolytic activity.|||In CADASIL2; unknown pathological significance; small decrease, if any, in proteolytic activity.|||In CARASIL; has 21 to 50% normal protease activity; is unable to suppress TGF-beta activity.|||Involved in trimer stabilization|||Kazal-like|||Loss of activity.|||PDZ|||Serine protease|||Serine protease HTRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026943|||http://purl.uniprot.org/annotation/VAR_063148|||http://purl.uniprot.org/annotation/VAR_063149|||http://purl.uniprot.org/annotation/VAR_076371|||http://purl.uniprot.org/annotation/VAR_076372|||http://purl.uniprot.org/annotation/VAR_076373|||http://purl.uniprot.org/annotation/VAR_076374|||http://purl.uniprot.org/annotation/VAR_076375|||http://purl.uniprot.org/annotation/VAR_076376|||http://purl.uniprot.org/annotation/VAR_076377|||http://purl.uniprot.org/annotation/VAR_076378|||http://purl.uniprot.org/annotation/VAR_076379|||http://purl.uniprot.org/annotation/VAR_076380|||http://purl.uniprot.org/annotation/VAR_076381|||http://purl.uniprot.org/annotation/VAR_076382
http://togogenome.org/gene/9606:DHFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ76|||http://purl.uniprot.org/uniprot/B4DM58|||http://purl.uniprot.org/uniprot/P00374                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DHFR|||Decreases affinity for NADP and dihydrofolate over 10-fold.|||Dihydrofolate reductase|||In DHFRD.|||In isoform 2.|||Increases affinity for dihydrofolate about 15-fold. No effect on affinity for NADPH.|||Increases affinity for dihydrofolate about 2-fold. No effect on affinity for NADPH.|||Increases affinity for dihydrofolate about 3-fold. No effect on affinity for NADPH.|||Increases affinity for dihydrofolate about 3-fold. Reduces affinity for NADPH about 3-fold.|||Reduces catalytic rate 2-fold. Reduces affinity for dihydrofolate 9-fold; when associated with R-32.|||Reduces catalytic rate 5-fold. Reduces affinity for dihydrofolate 9-fold; when associated with E-36.|||Strongly decreased affinity for methotrexate. Decreases catalytic rate constant 200-fold. Decreases affinity for NADP and dihydrofolate over 10-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186362|||http://purl.uniprot.org/annotation/VAR_065818|||http://purl.uniprot.org/annotation/VAR_065819|||http://purl.uniprot.org/annotation/VSP_056352
http://togogenome.org/gene/9606:XAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GPH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Polar residues|||TRAF-type|||XIAP-associated factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329028|||http://purl.uniprot.org/annotation/VAR_042616|||http://purl.uniprot.org/annotation/VAR_042617|||http://purl.uniprot.org/annotation/VAR_042618|||http://purl.uniprot.org/annotation/VAR_042619|||http://purl.uniprot.org/annotation/VSP_032918|||http://purl.uniprot.org/annotation/VSP_032919|||http://purl.uniprot.org/annotation/VSP_032920|||http://purl.uniprot.org/annotation/VSP_032921|||http://purl.uniprot.org/annotation/VSP_032922|||http://purl.uniprot.org/annotation/VSP_032923
http://togogenome.org/gene/9606:BCL7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z3H6|||http://purl.uniprot.org/uniprot/Q9BQE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  B-cell CLL/lymphoma 7 protein family member B|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239829|||http://purl.uniprot.org/annotation/VSP_019276|||http://purl.uniprot.org/annotation/VSP_019277|||http://purl.uniprot.org/annotation/VSP_019278|||http://purl.uniprot.org/annotation/VSP_019279|||http://purl.uniprot.org/annotation/VSP_045923
http://togogenome.org/gene/9606:GAREM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75VX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CABIT|||Disordered|||GRB2-associated and regulator of MAPK protein 2|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340253|||http://purl.uniprot.org/annotation/VSP_034201|||http://purl.uniprot.org/annotation/VSP_047321|||http://purl.uniprot.org/annotation/VSP_047322
http://togogenome.org/gene/9606:NEK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51956|||http://purl.uniprot.org/uniprot/Q6ZN64                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with VAV2|||N-acetylmethionine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086423|||http://purl.uniprot.org/annotation/VAR_033906|||http://purl.uniprot.org/annotation/VAR_040908|||http://purl.uniprot.org/annotation/VAR_040909|||http://purl.uniprot.org/annotation/VAR_040910|||http://purl.uniprot.org/annotation/VAR_040911|||http://purl.uniprot.org/annotation/VAR_040912|||http://purl.uniprot.org/annotation/VAR_040913|||http://purl.uniprot.org/annotation/VAR_040914|||http://purl.uniprot.org/annotation/VSP_035427
http://togogenome.org/gene/9606:IL10RB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08334                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to HBV infection; higher cell surface levels.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Interleukin-10 receptor subunit beta|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011014|||http://purl.uniprot.org/annotation/VAR_020666
http://togogenome.org/gene/9606:FAM199X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QYU2|||http://purl.uniprot.org/uniprot/Q6PEV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein FAM199X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251210|||http://purl.uniprot.org/annotation/VSP_020747
http://togogenome.org/gene/9606:IL17C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0M4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interleukin-17C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015429|||http://purl.uniprot.org/annotation/VAR_049598
http://togogenome.org/gene/9606:HES3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Orange|||Pro residues|||Transcription factor HES-3|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269174
http://togogenome.org/gene/9606:SLU7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95391                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes nuclear localization.|||Basic and acidic residues|||Bipartite nuclear localization signal|||CCHC-type|||Disordered|||Does not affect nuclear localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133.|||Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128.|||Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133.|||Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133.|||N-acetylserine|||Phosphoserine|||Pre-mRNA-splicing factor SLU7|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289194|||http://purl.uniprot.org/annotation/VAR_032598|||http://purl.uniprot.org/annotation/VAR_032599
http://togogenome.org/gene/9606:KLRC4-KLRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26718                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Inhibits association with the HCST signaling dimer.|||N-linked (GlcNAc...) asparagine|||NKG2-D type II integral membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046665|||http://purl.uniprot.org/annotation/VAR_013295|||http://purl.uniprot.org/annotation/VAR_030738
http://togogenome.org/gene/9606:PRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04554|||http://purl.uniprot.org/uniprot/Q1LZN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic nuclear protein HPI1|||Basic nuclear protein HPI2|||Basic nuclear protein HPS1|||Basic nuclear protein HPS2|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Removed|||Sperm histone HP2|||Sperm histone HP3|||Sperm histone HP4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025758|||http://purl.uniprot.org/annotation/PRO_0000025759|||http://purl.uniprot.org/annotation/PRO_0000025760|||http://purl.uniprot.org/annotation/PRO_0000025761|||http://purl.uniprot.org/annotation/PRO_0000025762|||http://purl.uniprot.org/annotation/PRO_0000025763|||http://purl.uniprot.org/annotation/PRO_0000025764|||http://purl.uniprot.org/annotation/VSP_054786
http://togogenome.org/gene/9606:MBNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUK0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Muscleblind-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089180|||http://purl.uniprot.org/annotation/VSP_006431|||http://purl.uniprot.org/annotation/VSP_006432|||http://purl.uniprot.org/annotation/VSP_006433|||http://purl.uniprot.org/annotation/VSP_006434|||http://purl.uniprot.org/annotation/VSP_015935|||http://purl.uniprot.org/annotation/VSP_044309
http://togogenome.org/gene/9606:SCAPER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||In IDDRP; unknown pathological significance.|||In isoform 3.|||Loss of CCNA2/CDK2 complex-binding.|||No effect on CCNA2/CDK2 complex-binding.|||Phosphoserine|||Polar residues|||S phase cyclin A-associated protein in the endoplasmic reticulum                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047513|||http://purl.uniprot.org/annotation/VAR_019978|||http://purl.uniprot.org/annotation/VAR_052806|||http://purl.uniprot.org/annotation/VAR_059910|||http://purl.uniprot.org/annotation/VAR_081681|||http://purl.uniprot.org/annotation/VAR_081682|||http://purl.uniprot.org/annotation/VSP_046503
http://togogenome.org/gene/9606:ADCY8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K3|||http://purl.uniprot.org/uniprot/P40145|||http://purl.uniprot.org/uniprot/Q4F7X0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 8|||Cytoplasmic|||Disordered|||Essential for CALM1 interaction|||Essential for autoinhibition maintenance|||Essential for autoinhibition maintenance by promoting interaction of the N and C termini|||Guanylate cyclase|||Helical|||In a colorectal cancer sample; somatic mutation.|||Involved in AKAP5 and PRKAR2A interaction|||Involved in CALM1 interaction|||Involved in ORAI1, STIM1, PPP2CA and PPP2R1A interaction|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Required for both calcium stimulation and maintenance of autoinhibition                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195705|||http://purl.uniprot.org/annotation/VAR_029188|||http://purl.uniprot.org/annotation/VAR_036328
http://togogenome.org/gene/9606:YPEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60688                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Nuclear localization signal|||Protein yippee-like 1|||Yippee                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212381
http://togogenome.org/gene/9606:FBN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35556                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 20; calcium-binding|||EGF-like 21; calcium-binding|||EGF-like 22; calcium-binding|||EGF-like 23; calcium-binding|||EGF-like 24; calcium-binding|||EGF-like 25; calcium-binding|||EGF-like 26; calcium-binding|||EGF-like 27; calcium-binding|||EGF-like 28; calcium-binding|||EGF-like 29; calcium-binding|||EGF-like 3|||EGF-like 30; calcium-binding|||EGF-like 31; calcium-binding|||EGF-like 32; calcium-binding|||EGF-like 33; calcium-binding|||EGF-like 34; calcium-binding|||EGF-like 35; calcium-binding|||EGF-like 36; calcium-binding|||EGF-like 37; calcium-binding|||EGF-like 38; calcium-binding|||EGF-like 39; calcium-binding|||EGF-like 40; calcium-binding|||EGF-like 41; calcium-binding|||EGF-like 42; calcium-binding|||EGF-like 43; calcium-binding|||EGF-like 44; calcium-binding|||EGF-like 45; calcium-binding|||EGF-like 46; calcium-binding|||EGF-like 47; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibrillin-2|||Found in a renal cell carcinoma case; somatic mutation.|||In CCA.|||In CCA; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25.|||In EOMD.|||In isoform 2.|||Interaction with MFAP4|||N-linked (GlcNAc...) asparagine|||O-linked (Glc) serine|||O-linked (Glc) threonine|||Placensin|||Pro residues|||TB 1|||TB 2|||TB 3|||TB 4|||TB 5|||TB 6|||TB 7|||TB 8|||TB 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007584|||http://purl.uniprot.org/annotation/PRO_0000436887|||http://purl.uniprot.org/annotation/PRO_0000436888|||http://purl.uniprot.org/annotation/VAR_002349|||http://purl.uniprot.org/annotation/VAR_002350|||http://purl.uniprot.org/annotation/VAR_002351|||http://purl.uniprot.org/annotation/VAR_010739|||http://purl.uniprot.org/annotation/VAR_010740|||http://purl.uniprot.org/annotation/VAR_010741|||http://purl.uniprot.org/annotation/VAR_014664|||http://purl.uniprot.org/annotation/VAR_015851|||http://purl.uniprot.org/annotation/VAR_016143|||http://purl.uniprot.org/annotation/VAR_054979|||http://purl.uniprot.org/annotation/VAR_054980|||http://purl.uniprot.org/annotation/VAR_054981|||http://purl.uniprot.org/annotation/VAR_054982|||http://purl.uniprot.org/annotation/VAR_054983|||http://purl.uniprot.org/annotation/VAR_054984|||http://purl.uniprot.org/annotation/VAR_054985|||http://purl.uniprot.org/annotation/VAR_054986|||http://purl.uniprot.org/annotation/VAR_054987|||http://purl.uniprot.org/annotation/VAR_054988|||http://purl.uniprot.org/annotation/VAR_054989|||http://purl.uniprot.org/annotation/VAR_054990|||http://purl.uniprot.org/annotation/VAR_055415|||http://purl.uniprot.org/annotation/VAR_055416|||http://purl.uniprot.org/annotation/VAR_055417|||http://purl.uniprot.org/annotation/VAR_058364|||http://purl.uniprot.org/annotation/VAR_058365|||http://purl.uniprot.org/annotation/VAR_058366|||http://purl.uniprot.org/annotation/VAR_058367|||http://purl.uniprot.org/annotation/VAR_058368|||http://purl.uniprot.org/annotation/VAR_058369|||http://purl.uniprot.org/annotation/VAR_058370|||http://purl.uniprot.org/annotation/VAR_058371|||http://purl.uniprot.org/annotation/VAR_058372|||http://purl.uniprot.org/annotation/VAR_058373|||http://purl.uniprot.org/annotation/VAR_058374|||http://purl.uniprot.org/annotation/VAR_058375|||http://purl.uniprot.org/annotation/VAR_064705|||http://purl.uniprot.org/annotation/VAR_072651|||http://purl.uniprot.org/annotation/VAR_072652|||http://purl.uniprot.org/annotation/VAR_072653|||http://purl.uniprot.org/annotation/VAR_072654|||http://purl.uniprot.org/annotation/VAR_072655|||http://purl.uniprot.org/annotation/VAR_072656|||http://purl.uniprot.org/annotation/VAR_074052|||http://purl.uniprot.org/annotation/VAR_076482|||http://purl.uniprot.org/annotation/VSP_037369|||http://purl.uniprot.org/annotation/VSP_037370|||http://purl.uniprot.org/annotation/VSP_037371
http://togogenome.org/gene/9606:CDRT15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T59                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CMT1A duplicated region transcript 15 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314905|||http://purl.uniprot.org/annotation/VAR_038121
http://togogenome.org/gene/9606:MRPL28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13084                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein bL28m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030506|||http://purl.uniprot.org/annotation/VAR_052024|||http://purl.uniprot.org/annotation/VAR_054219|||http://purl.uniprot.org/annotation/VAR_061806
http://togogenome.org/gene/9606:UBALD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYN6                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylserine|||Removed|||UBA-like domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239028
http://togogenome.org/gene/9606:TMEM214                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUQ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||Transmembrane protein 214                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321897|||http://purl.uniprot.org/annotation/VAR_039370|||http://purl.uniprot.org/annotation/VSP_041155
http://togogenome.org/gene/9606:CKS1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61024                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  Cyclin-dependent kinases regulatory subunit 1|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206235
http://togogenome.org/gene/9606:FAM117B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1L5|||http://purl.uniprot.org/uniprot/Q7Z3M2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM117B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299533|||http://purl.uniprot.org/annotation/VSP_027729|||http://purl.uniprot.org/annotation/VSP_027730
http://togogenome.org/gene/9606:FKBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02790                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased catalytic activity toward TRPC1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Interaction with tubulin|||N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate|||N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial|||N6-acetyllysine|||Omega-N-methylarginine|||PPIase FKBP-type 1|||PPIase FKBP-type 2|||Peptidyl-prolyl cis-trans isomerase FKBP4|||Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CK2|||Phosphotyrosine|||Polar residues|||Removed; alternate|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075318|||http://purl.uniprot.org/annotation/PRO_0000391468|||http://purl.uniprot.org/annotation/VAR_050624
http://togogenome.org/gene/9606:GOLGA6L9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEM1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Golgin subfamily A member 6-like protein 9|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334675|||http://purl.uniprot.org/annotation/VSP_033754
http://togogenome.org/gene/9606:RASA4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GXT2                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  C2|||Disordered|||Polar residues|||Ras-GAP                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:NPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z491|||http://purl.uniprot.org/uniprot/A0A0S2Z4G7|||http://purl.uniprot.org/uniprot/A0A140VJQ2|||http://purl.uniprot.org/uniprot/P06748                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylserine|||Abolishes phosphorylation by PLK2 and impairs centriole duplication.|||Acidic residues|||Basic and acidic residues|||Breakpoint for translocation to form NPM1-MLF1|||Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268.|||Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276.|||Complete destabilization of the structure; when associated with A-290.|||Disordered|||Does not affect phosphorylation by PLK2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263.|||Increase in the stabilization of the structure and partial delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-267.|||Increase in the stabilization of the structure.|||Interaction between pentamers|||Mimicks phosphorylation state, inducing accumulation of centrioles.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Necessary for interaction with APEX1|||No change in the sumoylation level.|||Nuclear localization signal|||Nucleophosmin|||Nucleophosmin C-terminal|||Nucleoplasmin core|||Partial destabilization of the structure.|||Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288.|||Partial loss of phosphorylation.|||Partial loss of phosphorylation. Does not affect phosphorylation by PLK2.|||Partial loss of phosphorylation; when associated with A-237.|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphoserine; by PLK1 and PLK2|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by CDK1, CDK2 and CDK6|||Phosphotyrosine|||Polar residues|||Required for interaction with SENP3|||Required for nucleolar localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219481|||http://purl.uniprot.org/annotation/VSP_003616|||http://purl.uniprot.org/annotation/VSP_043599
http://togogenome.org/gene/9606:MYG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB07                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Catalytically inactive.|||Loss of RNase activity and gained single stranded DNase activity.|||Loss of mitochondrial location.|||MYG1 exonuclease|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213483|||http://purl.uniprot.org/annotation/VAR_059854|||http://purl.uniprot.org/annotation/VAR_083553
http://togogenome.org/gene/9606:POLR2M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CAP1|||http://purl.uniprot.org/uniprot/P0CAP2|||http://purl.uniprot.org/uniprot/Q6EEV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerase II subunit GRINL1A|||DNA-directed RNA polymerase II subunit GRINL1A, isoforms 4/5|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 9.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9 and isoform 3.|||In isoform 9.|||Myocardial zonula adherens protein|||No effect on DYNLL1-binding.|||No effect on DYNLL1-binding; when associated with G-436.|||No effect on DYNLL1-binding; when associated with G-448.|||Polar residues|||Required for DYNLL1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326233|||http://purl.uniprot.org/annotation/PRO_0000376013|||http://purl.uniprot.org/annotation/PRO_5000089546|||http://purl.uniprot.org/annotation/VAR_054029|||http://purl.uniprot.org/annotation/VAR_055453|||http://purl.uniprot.org/annotation/VSP_032624|||http://purl.uniprot.org/annotation/VSP_037387|||http://purl.uniprot.org/annotation/VSP_037388|||http://purl.uniprot.org/annotation/VSP_037389|||http://purl.uniprot.org/annotation/VSP_037390|||http://purl.uniprot.org/annotation/VSP_037391|||http://purl.uniprot.org/annotation/VSP_037392|||http://purl.uniprot.org/annotation/VSP_037393|||http://purl.uniprot.org/annotation/VSP_037394|||http://purl.uniprot.org/annotation/VSP_037395|||http://purl.uniprot.org/annotation/VSP_037396|||http://purl.uniprot.org/annotation/VSP_037397|||http://purl.uniprot.org/annotation/VSP_037398
http://togogenome.org/gene/9606:CSK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3B6|||http://purl.uniprot.org/uniprot/B2R6Q4|||http://purl.uniprot.org/uniprot/P41240                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Decreases activity by two-thirds and alters conformation.|||Interaction with PTPN22|||N-acetylserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Strong decrease of phosphorylation by PRKACA (catalytic subunit of PKA).|||Tyrosine-protein kinase CSK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088070|||http://purl.uniprot.org/annotation/VAR_025203|||http://purl.uniprot.org/annotation/VAR_025204|||http://purl.uniprot.org/annotation/VAR_025205|||http://purl.uniprot.org/annotation/VAR_041678
http://togogenome.org/gene/9606:ARC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LC44                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Activity-regulated cytoskeleton-associated protein|||Complete loss of RNF216-mediated ubiquitination; when associated by A-268.|||Complete loss of RNF216-mediated ubiquitination; when associated by A-269.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with DNM2|||Interaction with SH3GL1 or SH3GL3|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273285
http://togogenome.org/gene/9606:JPH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Junctophilin-4|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159852
http://togogenome.org/gene/9606:LHCGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22888                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In FMPP.|||In FMPP; cells expressing the mutation display up to a 12-fold increase in basal cAMP production compared with cells expressing the same number of cell surface wild-type receptor indicating constitutive activation of the mutant receptor.|||In LHR; Leydig cell hypoplasia type 1.|||In LHR; Leydig cell hypoplasia type 1; abolishes signal transduction.|||In LHR; Leydig cell hypoplasia type 1; completely devoided of hormone-induced cAMP reporter gene activation; although initial translocation to the endoplasmic reticulum is normal translocation is halted or misrouted and the mutant does not reach the cell surface and cannot bind hormone.|||In LHR; Leydig cell hypoplasia type 1; exhibits a marked impairment of human chorionic gonadotropin binding; shows the absence of the glycosylated cell surface form; the mutant receptor is retained in the endoplasmic reticulum; mutant receptors do not migrate to the cell surface.|||In LHR; Leydig cell hypoplasia type 1; micropenis.|||In LHR; Leydig cell hypoplasia type 1; shows reduced cAMP production and ligand binding; receptor trafficking is not affected by the mutation.|||In LHR; Leydig cell hypoplasia type 2.|||In LHR; reveals a marked impairment of human chorionic gonadotropin binding and signal transduction.|||In Leydig cell tumor; somatic mutation; causes receptor activation and precocious puberty.|||In a breast cancer sample; somatic mutation.|||In isoform Short.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRNT|||Loss of palmitoylation.|||Lutropin-choriogonadotropic hormone receptor|||May be associated with earlier age of onset of breast cancer and poor prognosis.|||N-linked (GlcNAc...) asparagine|||No change in intracellular cAMP accumulation.|||Reduces intracellular cAMP accumulation.|||S-palmitoyl cysteine|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012780|||http://purl.uniprot.org/annotation/VAR_003549|||http://purl.uniprot.org/annotation/VAR_003550|||http://purl.uniprot.org/annotation/VAR_003551|||http://purl.uniprot.org/annotation/VAR_003552|||http://purl.uniprot.org/annotation/VAR_003553|||http://purl.uniprot.org/annotation/VAR_003554|||http://purl.uniprot.org/annotation/VAR_003555|||http://purl.uniprot.org/annotation/VAR_003556|||http://purl.uniprot.org/annotation/VAR_003557|||http://purl.uniprot.org/annotation/VAR_003558|||http://purl.uniprot.org/annotation/VAR_003559|||http://purl.uniprot.org/annotation/VAR_003560|||http://purl.uniprot.org/annotation/VAR_003561|||http://purl.uniprot.org/annotation/VAR_003562|||http://purl.uniprot.org/annotation/VAR_003563|||http://purl.uniprot.org/annotation/VAR_010154|||http://purl.uniprot.org/annotation/VAR_010155|||http://purl.uniprot.org/annotation/VAR_010156|||http://purl.uniprot.org/annotation/VAR_010157|||http://purl.uniprot.org/annotation/VAR_010158|||http://purl.uniprot.org/annotation/VAR_010159|||http://purl.uniprot.org/annotation/VAR_010160|||http://purl.uniprot.org/annotation/VAR_010161|||http://purl.uniprot.org/annotation/VAR_010162|||http://purl.uniprot.org/annotation/VAR_010163|||http://purl.uniprot.org/annotation/VAR_010164|||http://purl.uniprot.org/annotation/VAR_035764|||http://purl.uniprot.org/annotation/VAR_055922|||http://purl.uniprot.org/annotation/VAR_060737|||http://purl.uniprot.org/annotation/VAR_062336|||http://purl.uniprot.org/annotation/VAR_062337|||http://purl.uniprot.org/annotation/VAR_062338|||http://purl.uniprot.org/annotation/VAR_062339|||http://purl.uniprot.org/annotation/VSP_001962
http://togogenome.org/gene/9606:RFLNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5W9                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Refilin-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264631
http://togogenome.org/gene/9606:DRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13474                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Dystrophin-related protein 2|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spectrin 1|||Spectrin 2|||WW|||ZZ-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076083|||http://purl.uniprot.org/annotation/VAR_033898|||http://purl.uniprot.org/annotation/VSP_042662
http://togogenome.org/gene/9606:PAIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AE6|||http://purl.uniprot.org/uniprot/Q9BPZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Ataxin-2 C-terminal|||Disordered|||PABPC1-interacting motif-1 (PAM1)|||PABPC1-interacting motif-2 (PAM2)|||Polar residues|||Polyadenylate-binding protein-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058179
http://togogenome.org/gene/9606:LPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B1RVA9|||http://purl.uniprot.org/uniprot/P06858                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Charge relay system|||Essential for determining substrate specificity|||Impaired heparin-binding; when associated with N-430 and N-432.|||Impaired heparin-binding; when associated with N-430 and N-437.|||Impaired heparin-binding; when associated with N-432 and N-437.|||Important for heparin binding|||Important for interaction with lipoprotein particles|||In FCHL3 and HLPP1; associated with disease susceptibility; loss of activity; frequent mutation.|||In FCHL3; associated with disease susceptibility; has approximately 80% of the specific activity of wild-type enzyme.|||In HLPP1 and hyperlipidemia; synthesized as a catalytically inactive form; total amount is almost equal to that of the normal enzyme; non-releasable by heparin due to the abnormal structure of the mutant protein.|||In HLPP1.|||In HLPP1; 2.0% of activity.|||In HLPP1; 3.2% of activity.|||In HLPP1; 5% of full activity.|||In HLPP1; Bethesda; loss of activity and abnormal heparin binding.|||In HLPP1; Nijmegen; loss of activity.|||In HLPP1; affects the protein folding.|||In HLPP1; almost complete loss of enzyme activity.|||In HLPP1; approximately 6% of normal LPL activity and 40% of LPL mass are detected in the patient's postheparin plasma; results in the production of a functionally inactive enzyme.|||In HLPP1; complete loss of enzyme activity.|||In HLPP1; decreased protein secretion; loss of interaction with GPIHBP1; decreased lipoprotein lipase activity.|||In HLPP1; decreases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct.|||In HLPP1; decreases the specific activity of the enzyme; reduces the secretion of the mutant protein significantly; the total LPL mass is reduced compared to that of the wild-type construct.|||In HLPP1; decreases the specific activity of the enzyme; the total LPL mass is reduced compared to that of the wild-type construct.|||In HLPP1; gives rise to a 80% decrease in specific catalytic activity.|||In HLPP1; has 48% of normal activity in vitro; decreased levels of activity account for by the lower protein mass levels of the mutants rather than by decreased enzymatic activities; loss of interaction with GPIHBP1.|||In HLPP1; has no effect on the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct.|||In HLPP1; increases the specific activity of the enzyme; has a mild effect on the secretion of the mutant enzyme; the total LPL mass is reduced compared to that of the wild-type construct.|||In HLPP1; lacks both triolein and tributyrin esterase activities.|||In HLPP1; loss of activity.|||In HLPP1; mild hypertriglyceridemia; partial activity.|||In HLPP1; no enzyme activity.|||In HLPP1; produces an inactive protein which is not secreted into the media.|||In HLPP1; results in a moderate reduction in catalytic activity.|||In HLPP1; severely decreased lipoprotein lipase activity; decreased secretion.|||In HLPP1; synthesized as a catalytically inactive form.|||In HLPP1; the LPL mass level is approximately 67% of the normal; the activity is 32% of the nornal.|||Interaction with GPIHBP1|||Lipoprotein lipase|||Loss of both triglyceride hydrolase and phospholipase activity.|||Loss of enzyme activity with triolein and tributyrin.|||Loss of enzyme activity.|||Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with 420-A-A-421.|||Loss of interaction with lipoprotein particles, but no effect on interaction with GPIHBP1; when associated with A-417.|||Loss of triglyceride hydrolase activity while phospholipase activity remains intact.|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity.|||Nucleophile|||PLAT|||Reduced triglyceride hydrolase activity and increased phospholipase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017775|||http://purl.uniprot.org/annotation/PRO_5014204238|||http://purl.uniprot.org/annotation/VAR_004211|||http://purl.uniprot.org/annotation/VAR_004212|||http://purl.uniprot.org/annotation/VAR_004213|||http://purl.uniprot.org/annotation/VAR_004214|||http://purl.uniprot.org/annotation/VAR_004215|||http://purl.uniprot.org/annotation/VAR_004216|||http://purl.uniprot.org/annotation/VAR_004217|||http://purl.uniprot.org/annotation/VAR_004218|||http://purl.uniprot.org/annotation/VAR_004219|||http://purl.uniprot.org/annotation/VAR_004220|||http://purl.uniprot.org/annotation/VAR_004221|||http://purl.uniprot.org/annotation/VAR_004222|||http://purl.uniprot.org/annotation/VAR_004223|||http://purl.uniprot.org/annotation/VAR_004224|||http://purl.uniprot.org/annotation/VAR_004225|||http://purl.uniprot.org/annotation/VAR_004226|||http://purl.uniprot.org/annotation/VAR_004227|||http://purl.uniprot.org/annotation/VAR_004228|||http://purl.uniprot.org/annotation/VAR_004229|||http://purl.uniprot.org/annotation/VAR_004230|||http://purl.uniprot.org/annotation/VAR_004231|||http://purl.uniprot.org/annotation/VAR_004232|||http://purl.uniprot.org/annotation/VAR_004233|||http://purl.uniprot.org/annotation/VAR_004234|||http://purl.uniprot.org/annotation/VAR_004235|||http://purl.uniprot.org/annotation/VAR_004236|||http://purl.uniprot.org/annotation/VAR_004237|||http://purl.uniprot.org/annotation/VAR_004238|||http://purl.uniprot.org/annotation/VAR_004239|||http://purl.uniprot.org/annotation/VAR_004240|||http://purl.uniprot.org/annotation/VAR_004241|||http://purl.uniprot.org/annotation/VAR_004242|||http://purl.uniprot.org/annotation/VAR_004243|||http://purl.uniprot.org/annotation/VAR_004244|||http://purl.uniprot.org/annotation/VAR_004245|||http://purl.uniprot.org/annotation/VAR_004246|||http://purl.uniprot.org/annotation/VAR_011948|||http://purl.uniprot.org/annotation/VAR_011949|||http://purl.uniprot.org/annotation/VAR_011950|||http://purl.uniprot.org/annotation/VAR_011951|||http://purl.uniprot.org/annotation/VAR_011952|||http://purl.uniprot.org/annotation/VAR_049819|||http://purl.uniprot.org/annotation/VAR_057914|||http://purl.uniprot.org/annotation/VAR_057915|||http://purl.uniprot.org/annotation/VAR_057916|||http://purl.uniprot.org/annotation/VAR_057917|||http://purl.uniprot.org/annotation/VAR_057918|||http://purl.uniprot.org/annotation/VAR_057919|||http://purl.uniprot.org/annotation/VAR_057920|||http://purl.uniprot.org/annotation/VAR_057921|||http://purl.uniprot.org/annotation/VAR_057922|||http://purl.uniprot.org/annotation/VAR_057923|||http://purl.uniprot.org/annotation/VAR_057924|||http://purl.uniprot.org/annotation/VAR_057925|||http://purl.uniprot.org/annotation/VAR_057926|||http://purl.uniprot.org/annotation/VAR_057927|||http://purl.uniprot.org/annotation/VAR_057928|||http://purl.uniprot.org/annotation/VAR_057929|||http://purl.uniprot.org/annotation/VAR_057930|||http://purl.uniprot.org/annotation/VAR_057931|||http://purl.uniprot.org/annotation/VAR_057932|||http://purl.uniprot.org/annotation/VAR_057933|||http://purl.uniprot.org/annotation/VAR_057934|||http://purl.uniprot.org/annotation/VAR_057935|||http://purl.uniprot.org/annotation/VAR_057936|||http://purl.uniprot.org/annotation/VAR_057937|||http://purl.uniprot.org/annotation/VAR_057938|||http://purl.uniprot.org/annotation/VAR_057939|||http://purl.uniprot.org/annotation/VAR_057940|||http://purl.uniprot.org/annotation/VAR_057941|||http://purl.uniprot.org/annotation/VAR_057942|||http://purl.uniprot.org/annotation/VAR_057943|||http://purl.uniprot.org/annotation/VAR_057944|||http://purl.uniprot.org/annotation/VAR_057945|||http://purl.uniprot.org/annotation/VAR_077541
http://togogenome.org/gene/9606:PRND                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7U7M2|||http://purl.uniprot.org/uniprot/Q9UKY0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cu(2+) binding|||Flexible tail|||GPI-anchor amidated glycine|||Globular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Prion-like protein doppel|||Prion/Doppel protein beta-ribbon|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025745|||http://purl.uniprot.org/annotation/PRO_0000025746|||http://purl.uniprot.org/annotation/VAR_013765|||http://purl.uniprot.org/annotation/VAR_013766|||http://purl.uniprot.org/annotation/VAR_013767|||http://purl.uniprot.org/annotation/VAR_013769|||http://purl.uniprot.org/annotation/VAR_013770|||http://purl.uniprot.org/annotation/VAR_013771|||http://purl.uniprot.org/annotation/VAR_013772|||http://purl.uniprot.org/annotation/VAR_013773
http://togogenome.org/gene/9606:PRAMEF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60813                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156985
http://togogenome.org/gene/9606:LMAN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAT1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 3.|||L-type lectin-like|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein ERGIC-53-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017663|||http://purl.uniprot.org/annotation/VAR_049771|||http://purl.uniprot.org/annotation/VAR_049772|||http://purl.uniprot.org/annotation/VSP_013143
http://togogenome.org/gene/9606:BHLHA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Class A basic helix-loop-helix protein 9|||Disordered|||In CCSPD; unknown pathological significance; requires 2 nucleotide substitutions.|||In MSSD; completely abolishes the transcription activation with the dimerization partners TCF3, TCF4 and TCF12.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341377|||http://purl.uniprot.org/annotation/VAR_073333|||http://purl.uniprot.org/annotation/VAR_073334|||http://purl.uniprot.org/annotation/VAR_073335|||http://purl.uniprot.org/annotation/VAR_077086
http://togogenome.org/gene/9606:SNAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43623                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to KPNA2 and impairs binding to KPNB1, IPO7 and TMPO1; when associated with E-192.|||Abolishes binding to KPNA2 and impairs binding to KPNB1, IPO7 and TMPO1; when associated with E-196.|||Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-166.|||Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-175.|||Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-225.|||Abolishes binding to KPNA2, KPNB1 and IPO7 and impairs binding to TMPO1; when associated with E-229.|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; atypical|||Disordered|||In a patient with neural tube defects.|||Increases protein stability and half-life, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-100.|||Increases protein stability and half-life, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-104.|||Increases protein stability, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-92.|||Increases protein stability, nuclear accumulation and repressor activity on E-cadherin/CDH1 promoter; when associated with A-96.|||Increases protein stability. Does not affect repressor activity on E-cadherin/CDH1 promoter.|||Polar residues|||SNAG domain|||Zinc finger protein SNAI2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047032|||http://purl.uniprot.org/annotation/VAR_009873|||http://purl.uniprot.org/annotation/VAR_069163|||http://purl.uniprot.org/annotation/VAR_069164
http://togogenome.org/gene/9606:SPAG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75391                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||R3H|||Removed|||Sperm-associated antigen 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072097
http://togogenome.org/gene/9606:ALX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95076                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein aristaless-like 3|||In FND1.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048812|||http://purl.uniprot.org/annotation/VAR_047475|||http://purl.uniprot.org/annotation/VAR_063226|||http://purl.uniprot.org/annotation/VAR_063227|||http://purl.uniprot.org/annotation/VAR_063228|||http://purl.uniprot.org/annotation/VAR_063229
http://togogenome.org/gene/9606:HP1BP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SSJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H15 1|||H15 2|||H15 3|||Heterochromatin protein 1-binding protein 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||PxVxL motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339642|||http://purl.uniprot.org/annotation/VSP_034168|||http://purl.uniprot.org/annotation/VSP_034169|||http://purl.uniprot.org/annotation/VSP_034170|||http://purl.uniprot.org/annotation/VSP_034171
http://togogenome.org/gene/9606:KIF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIL4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125435|||http://purl.uniprot.org/annotation/VAR_049687|||http://purl.uniprot.org/annotation/VAR_049688|||http://purl.uniprot.org/annotation/VAR_059369|||http://purl.uniprot.org/annotation/VAR_061280|||http://purl.uniprot.org/annotation/VSP_002867
http://togogenome.org/gene/9606:PNMA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL41                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||CCHC-type|||Disordered|||In isoform 2.|||Paraneoplastic antigen Ma3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280215|||http://purl.uniprot.org/annotation/VAR_057701|||http://purl.uniprot.org/annotation/VAR_057702|||http://purl.uniprot.org/annotation/VSP_023571
http://togogenome.org/gene/9606:HDGFL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4V5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hepatoma-derived growth factor-related protein 2|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interaction with DPF3/BAF45C isoform 2|||Loss of interaction with SMARCA4, SMARCC1, SMARCD1 and DPF3/BAF45C isoform 2.|||Loss of interaction with histone H3K36me2.|||PWWP|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317643|||http://purl.uniprot.org/annotation/VSP_031116|||http://purl.uniprot.org/annotation/VSP_047329
http://togogenome.org/gene/9606:EHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZN3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes ATP-binding and localizes to cytoplasm.|||Abolishes interaction with RAB11FIP2.|||Abolishes sumoylation and localization to tubular structures of the ERC, impairs fast recycling activity from the ERC, no effect on homooligomerization; when associated with R-511.|||Abolishes sumoylation localization to tubular structures of the ERC, impairs fast recycling activity from the ERC, no effect on homooligomerization;; when associated with R-315.|||Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 3|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Greatly reduces oligomerization and interaction with RAB11FIP2.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146112|||http://purl.uniprot.org/annotation/VSP_056606|||http://purl.uniprot.org/annotation/VSP_056607
http://togogenome.org/gene/9606:XCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47992                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Lymphotactin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005248
http://togogenome.org/gene/9606:DNPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULA0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aspartyl aminopeptidase|||In isoform 2.|||N-acetylmethionine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173451|||http://purl.uniprot.org/annotation/VSP_060753
http://togogenome.org/gene/9606:RICTOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6R327                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes deubiquitination by USP9X and increases interaction with MTOR. No effect on interaction with SIN1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Interaction with NBN|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by GSK3-alpha and GSK3-beta|||Phosphothreonine; by RPS6KB1|||Rapamycin-insensitive companion of mTOR|||Reduced GSK3-mediated phosphorylation, reduced interaction with FBXW7, reduced FBXW7-mediated ubiquitination and increased stability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308179|||http://purl.uniprot.org/annotation/VAR_051320|||http://purl.uniprot.org/annotation/VSP_038362|||http://purl.uniprot.org/annotation/VSP_038363|||http://purl.uniprot.org/annotation/VSP_052581
http://togogenome.org/gene/9606:OGFOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTF4|||http://purl.uniprot.org/uniprot/Q6N063                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2|||Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288978|||http://purl.uniprot.org/annotation/VSP_025855|||http://purl.uniprot.org/annotation/VSP_025856|||http://purl.uniprot.org/annotation/VSP_025857|||http://purl.uniprot.org/annotation/VSP_025858|||http://purl.uniprot.org/annotation/VSP_025859
http://togogenome.org/gene/9606:PRELID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N945                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PRELI domain-containing protein 2|||PRELI/MSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307773|||http://purl.uniprot.org/annotation/VAR_053910|||http://purl.uniprot.org/annotation/VSP_028824|||http://purl.uniprot.org/annotation/VSP_028825|||http://purl.uniprot.org/annotation/VSP_044841
http://togogenome.org/gene/9606:GLT8D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1C3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glycosyltransferase 8 domain-containing protein 2|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271382|||http://purl.uniprot.org/annotation/VAR_049247
http://togogenome.org/gene/9606:CPED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0V7|||http://purl.uniprot.org/uniprot/Q9H6Q5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cadherin-like and PC-esterase domain-containing protein 1|||Cadherin-like beta sandwich|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317732|||http://purl.uniprot.org/annotation/VAR_038664|||http://purl.uniprot.org/annotation/VAR_038665|||http://purl.uniprot.org/annotation/VAR_038666|||http://purl.uniprot.org/annotation/VAR_038667|||http://purl.uniprot.org/annotation/VSP_031140|||http://purl.uniprot.org/annotation/VSP_031141
http://togogenome.org/gene/9606:NNAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITN5|||http://purl.uniprot.org/uniprot/Q16517                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform Beta.|||Neuronatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096882|||http://purl.uniprot.org/annotation/VSP_004331
http://togogenome.org/gene/9606:TRIM59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWR1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Molecule Processing|||Region|||Site|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||Helical|||RING-type|||Tripartite motif-containing protein 59                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249679
http://togogenome.org/gene/9606:TRDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJV0|||http://purl.uniprot.org/uniprot/H9ME53|||http://purl.uniprot.org/uniprot/Q13061|||http://purl.uniprot.org/uniprot/Q8IVK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Aspartyl beta-hydroxylase/Triadin|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In CARDAR; results in intracellular retention and degradation of the mutant protein.|||In isoform 2.|||In isoform 3.|||Interchain|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Triadin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065626|||http://purl.uniprot.org/annotation/VAR_057008|||http://purl.uniprot.org/annotation/VAR_057009|||http://purl.uniprot.org/annotation/VAR_057010|||http://purl.uniprot.org/annotation/VAR_057011|||http://purl.uniprot.org/annotation/VAR_057012|||http://purl.uniprot.org/annotation/VAR_057013|||http://purl.uniprot.org/annotation/VAR_065263|||http://purl.uniprot.org/annotation/VAR_065264|||http://purl.uniprot.org/annotation/VAR_065265|||http://purl.uniprot.org/annotation/VAR_067350|||http://purl.uniprot.org/annotation/VSP_045561|||http://purl.uniprot.org/annotation/VSP_045562|||http://purl.uniprot.org/annotation/VSP_045563|||http://purl.uniprot.org/annotation/VSP_045564|||http://purl.uniprot.org/annotation/VSP_045565
http://togogenome.org/gene/9606:TAFAZZIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4E6|||http://purl.uniprot.org/uniprot/A0A0S2Z4F4|||http://purl.uniprot.org/uniprot/A0A0S2Z4K0|||http://purl.uniprot.org/uniprot/A0A0S2Z4K9|||http://purl.uniprot.org/uniprot/A6XNE1|||http://purl.uniprot.org/uniprot/Q16635                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Motif|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  HXXXXD motif|||Helical|||In BTHS.|||In BTHS; abolishes catalytic activity.|||In BTHS; does not affect mitochondrial localization.|||In BTHS; unstable protein.|||In isoform 1, isoform 2, isoform 5 and isoform 6.|||In isoform 2, isoform 6, isoform 8 and isoform 9.|||In isoform 4.|||In isoform 5, isoform 6, isoform 7 and isoform 9.|||Mitochondrial intermembrane|||Mitochondrial targeting sequence|||Phospholipid/glycerol acyltransferase|||Tafazzin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220928|||http://purl.uniprot.org/annotation/VAR_014110|||http://purl.uniprot.org/annotation/VAR_014111|||http://purl.uniprot.org/annotation/VAR_014112|||http://purl.uniprot.org/annotation/VAR_068434|||http://purl.uniprot.org/annotation/VAR_084500|||http://purl.uniprot.org/annotation/VAR_084501|||http://purl.uniprot.org/annotation/VAR_084502|||http://purl.uniprot.org/annotation/VAR_084503|||http://purl.uniprot.org/annotation/VAR_084504|||http://purl.uniprot.org/annotation/VAR_084505|||http://purl.uniprot.org/annotation/VAR_084506|||http://purl.uniprot.org/annotation/VSP_061365|||http://purl.uniprot.org/annotation/VSP_061366|||http://purl.uniprot.org/annotation/VSP_061367|||http://purl.uniprot.org/annotation/VSP_061368
http://togogenome.org/gene/9606:AKAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75969|||http://purl.uniprot.org/uniprot/V9HWD4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  A-kinase anchor 110kDa C-terminal|||A-kinase anchor protein 3|||Abolishes interaction with ROPN1.|||Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RII binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064526|||http://purl.uniprot.org/annotation/VAR_036428|||http://purl.uniprot.org/annotation/VAR_055488|||http://purl.uniprot.org/annotation/VAR_055489|||http://purl.uniprot.org/annotation/VAR_055490|||http://purl.uniprot.org/annotation/VAR_055491|||http://purl.uniprot.org/annotation/VAR_055492|||http://purl.uniprot.org/annotation/VAR_059112|||http://purl.uniprot.org/annotation/VAR_060730|||http://purl.uniprot.org/annotation/VAR_061000
http://togogenome.org/gene/9606:OR8K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH51                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8K3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150672|||http://purl.uniprot.org/annotation/VAR_024123|||http://purl.uniprot.org/annotation/VAR_034273|||http://purl.uniprot.org/annotation/VAR_034274
http://togogenome.org/gene/9606:SCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09683                                                                                  ^@                                                                                  Helix|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Phosphoserine|||Secretin|||Valine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011423|||http://purl.uniprot.org/annotation/PRO_0000011424|||http://purl.uniprot.org/annotation/PRO_0000011425
http://togogenome.org/gene/9606:ATP13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD20                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||A-domain; part 1|||A-domain; part 2|||Arm-like|||Cytoplasmic|||Disordered|||Endoplasmic reticulum transmembrane helix translocase|||Extracellular|||Found in a patient with intellectual disability; unknown pathological significance.|||Helical|||In isoform B.|||In isoform C.|||Loss of ATPase activity.|||N-acetylalanine|||N-domain|||N-linked (GlcNAc...) asparagine|||P-domain; part 1|||P-domain; part 2|||P-domain; part 3|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046421|||http://purl.uniprot.org/annotation/VAR_084651|||http://purl.uniprot.org/annotation/VSP_000433|||http://purl.uniprot.org/annotation/VSP_000434|||http://purl.uniprot.org/annotation/VSP_000435
http://togogenome.org/gene/9606:TIGD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNK0|||http://purl.uniprot.org/uniprot/Q4W5G0|||http://purl.uniprot.org/uniprot/V9HWD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Tigger transposable element-derived protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271088|||http://purl.uniprot.org/annotation/VAR_053036
http://togogenome.org/gene/9606:WDR17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZU2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||WD 1|||WD 10|||WD 11|||WD 12|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051364|||http://purl.uniprot.org/annotation/VAR_047399|||http://purl.uniprot.org/annotation/VAR_047400|||http://purl.uniprot.org/annotation/VAR_047401|||http://purl.uniprot.org/annotation/VAR_047402|||http://purl.uniprot.org/annotation/VAR_047403|||http://purl.uniprot.org/annotation/VAR_062101|||http://purl.uniprot.org/annotation/VSP_047201|||http://purl.uniprot.org/annotation/VSP_047202
http://togogenome.org/gene/9606:PATE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXA2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Prostate and testis expressed protein 1|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315325|||http://purl.uniprot.org/annotation/VAR_052699|||http://purl.uniprot.org/annotation/VAR_052700|||http://purl.uniprot.org/annotation/VSP_030533
http://togogenome.org/gene/9606:PLA2G4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZI4|||http://purl.uniprot.org/uniprot/P47712                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-577.|||7-fold reduced phospholipase and lysophospholipase activities. 100-fold reduced phospholipase and lysophospholipase activities; when associated with A-195.|||Abolishes both phospholipase and lysophospholipase activities.|||Abolishes phospholipase activity.|||Abolishes phospholipiase activity.|||Basic and acidic residues|||C2|||Cytosolic phospholipase A2|||Decreases agonist-stimulated release of arachidonic acid. Reduces phospholipase A2 activity; when associated with A-437; A-454 and A-727.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs binding to ceramide-1-phosphate.|||Impairs phosphoinositide-stimulated phospholipase A2 activity.|||Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-543.|||Impairs phosphoinositide-stimulated phospholipase A2 activity.; when associated with A-541 and A-544.|||Impairs phosphoinositide-stimulated phospholipase A2 activity; when associated with A-543 and A-544.|||Impairs phospholipase A2 and lysophospholipase activities in the absence of phosphoinositides. Has full activity in the presence of phosphoinositides.|||In GURDP; decreased protein expression, if any, in platelets from homozygous patients.|||In GURDP; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||No effect on phospholipase activity.|||No effect on phospholipase activity; when associated with A-139 and A-141.|||No effect on phospholipase activity; when associated with A-139 and A-151.|||No effect on phospholipase activity; when associated with A-141 and A-151.|||No effect on phospholipase activity; when associated with A-324.|||No effect on phospholipase activity; when associated with A-331.|||No effect on phospholipase activity; when associated with A-620.|||No effect on phospholipase activity; when associated with A-634.|||No effect on phospholipase or lysophospholipase activity.|||Nucleophile|||PLA2c|||Phospholipid binding|||Phosphoserine|||Phosphoserine; by MAPK|||Phosphothreonine|||Proton acceptor|||Reduces phospholipase A2 activity; when associated with A-437; A-455 and A-505.|||Reduces phospholipase A2 activity; when associated with A-437; A-505 and A-727.|||Reduces phospholipase A2 activity; when associated with A-454; A-505 and A-727.|||Reduces phospholipase activity 200-fold.|||Reduces phospholipase activity 2000-fold.|||Reduces phospholipase activity 300-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187262|||http://purl.uniprot.org/annotation/VAR_018424|||http://purl.uniprot.org/annotation/VAR_018760|||http://purl.uniprot.org/annotation/VAR_029276|||http://purl.uniprot.org/annotation/VAR_035826|||http://purl.uniprot.org/annotation/VAR_062128|||http://purl.uniprot.org/annotation/VAR_070778|||http://purl.uniprot.org/annotation/VAR_070779|||http://purl.uniprot.org/annotation/VAR_082091
http://togogenome.org/gene/9606:PRKCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RTI5|||http://purl.uniprot.org/uniprot/Q02156                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes activity and S-729 phosphorylation.|||Abolishes phosphorylation by PDK1, and S-729 phosphorylation.|||C2|||Disordered|||Enhances T-566 dephosphorylation.|||In a colorectal cancer sample; somatic mutation.|||Interaction with actin|||No effect on S-729 phosphorylation.|||No effect on activity; no effect on S-729 phosphorylation.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK11 and MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Protein kinase C epsilon type|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055697|||http://purl.uniprot.org/annotation/VAR_035466|||http://purl.uniprot.org/annotation/VAR_042307|||http://purl.uniprot.org/annotation/VAR_042308|||http://purl.uniprot.org/annotation/VAR_042309|||http://purl.uniprot.org/annotation/VAR_050559
http://togogenome.org/gene/9606:SNU13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55769|||http://purl.uniprot.org/uniprot/Q6FHM6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Abolishes U4 snRNA-binding.|||Important for U4 snRNA-binding|||Interaction with U4 snRNA and U4atac snRNA|||N-acetylmethionine|||N-acetylthreonine; in NHP2-like protein 1, N-terminally processed|||N6-acetyllysine|||NHP2-like protein 1|||NHP2-like protein 1, N-terminally processed|||Phosphoserine|||Reduces U4 snRNA-binding by about 50%.|||Removed; alternate|||Ribosomal protein eL8/eL30/eS12/Gadd45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136778|||http://purl.uniprot.org/annotation/PRO_0000423260|||http://purl.uniprot.org/annotation/VAR_034155
http://togogenome.org/gene/9606:PPP6R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BXH2|||http://purl.uniprot.org/uniprot/Q5H9R7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein phosphatase 6 regulatory subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046100|||http://purl.uniprot.org/annotation/VAR_057720|||http://purl.uniprot.org/annotation/VSP_017140|||http://purl.uniprot.org/annotation/VSP_017141|||http://purl.uniprot.org/annotation/VSP_017142|||http://purl.uniprot.org/annotation/VSP_017143|||http://purl.uniprot.org/annotation/VSP_017144
http://togogenome.org/gene/9606:MME                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08473                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In CMT2T; decrease of protein expression.|||In CMT2T; late-onset form; results in reduction of neprilysin activity.|||In CMT2T; results in reduction of neprilysin activity.|||In CMT2T; unknown pathological significance.|||In SCA43.|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Neprilysin|||Peptidase M13|||Phosphoserine|||Proton donor|||Removed|||Stop-transfer sequence                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078213|||http://purl.uniprot.org/annotation/VAR_077684|||http://purl.uniprot.org/annotation/VAR_077685|||http://purl.uniprot.org/annotation/VAR_077686|||http://purl.uniprot.org/annotation/VAR_077687|||http://purl.uniprot.org/annotation/VAR_077688|||http://purl.uniprot.org/annotation/VAR_077689|||http://purl.uniprot.org/annotation/VAR_077690|||http://purl.uniprot.org/annotation/VAR_077691
http://togogenome.org/gene/9606:GNG13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2W3                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012671|||http://purl.uniprot.org/annotation/PRO_0000012672
http://togogenome.org/gene/9606:CCDC180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZK1|||http://purl.uniprot.org/uniprot/Q9P1Z9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 180|||DUF4455|||Disordered|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315233|||http://purl.uniprot.org/annotation/VAR_038151|||http://purl.uniprot.org/annotation/VAR_038152|||http://purl.uniprot.org/annotation/VAR_038153|||http://purl.uniprot.org/annotation/VAR_038154|||http://purl.uniprot.org/annotation/VAR_038155|||http://purl.uniprot.org/annotation/VAR_038156|||http://purl.uniprot.org/annotation/VAR_038157|||http://purl.uniprot.org/annotation/VAR_061250|||http://purl.uniprot.org/annotation/VSP_059687
http://togogenome.org/gene/9606:TBCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYF5|||http://purl.uniprot.org/uniprot/Q8TEA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In IHPRF3.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a head & Neck squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||Protein kinase|||Rab-GAP TBC|||Rhodanese|||TBC domain-containing protein kinase-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273278|||http://purl.uniprot.org/annotation/VAR_030123|||http://purl.uniprot.org/annotation/VAR_030124|||http://purl.uniprot.org/annotation/VAR_041380|||http://purl.uniprot.org/annotation/VAR_041381|||http://purl.uniprot.org/annotation/VAR_041382|||http://purl.uniprot.org/annotation/VAR_041383|||http://purl.uniprot.org/annotation/VAR_041384|||http://purl.uniprot.org/annotation/VAR_041385|||http://purl.uniprot.org/annotation/VAR_041386|||http://purl.uniprot.org/annotation/VAR_041387|||http://purl.uniprot.org/annotation/VAR_077816|||http://purl.uniprot.org/annotation/VAR_077817|||http://purl.uniprot.org/annotation/VSP_052274|||http://purl.uniprot.org/annotation/VSP_052275
http://togogenome.org/gene/9606:RDH13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVA3|||http://purl.uniprot.org/uniprot/Q8NBN7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylserine|||Phosphoserine|||Proton acceptor|||Removed|||Retinol dehydrogenase 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054768|||http://purl.uniprot.org/annotation/PRO_5002788453|||http://purl.uniprot.org/annotation/VSP_040383
http://togogenome.org/gene/9606:DYTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2CJ06                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dystrotelin|||Polar residues|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298934|||http://purl.uniprot.org/annotation/VAR_050960|||http://purl.uniprot.org/annotation/VAR_050961
http://togogenome.org/gene/9606:IL15RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS77|||http://purl.uniprot.org/uniprot/G8CVM3|||http://purl.uniprot.org/uniprot/Q13261                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4, isoform 6 and isoform 8.|||In isoform 5 and isoform 6.|||In isoform 7 and isoform 8.|||In isoform 9.|||Interleukin-15 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues|||Soluble interleukin-15 receptor subunit alpha|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011044|||http://purl.uniprot.org/annotation/PRO_0000333855|||http://purl.uniprot.org/annotation/PRO_5003509020|||http://purl.uniprot.org/annotation/VAR_020967|||http://purl.uniprot.org/annotation/VSP_012623|||http://purl.uniprot.org/annotation/VSP_012624|||http://purl.uniprot.org/annotation/VSP_012625|||http://purl.uniprot.org/annotation/VSP_012626|||http://purl.uniprot.org/annotation/VSP_055406
http://togogenome.org/gene/9606:EFCAB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU69                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||EF-hand calcium-binding domain-containing protein 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315836|||http://purl.uniprot.org/annotation/VAR_038343|||http://purl.uniprot.org/annotation/VAR_038344|||http://purl.uniprot.org/annotation/VAR_038345|||http://purl.uniprot.org/annotation/VAR_048644|||http://purl.uniprot.org/annotation/VAR_048645|||http://purl.uniprot.org/annotation/VAR_048646|||http://purl.uniprot.org/annotation/VSP_030732|||http://purl.uniprot.org/annotation/VSP_030733|||http://purl.uniprot.org/annotation/VSP_030734|||http://purl.uniprot.org/annotation/VSP_030735|||http://purl.uniprot.org/annotation/VSP_047184|||http://purl.uniprot.org/annotation/VSP_047185|||http://purl.uniprot.org/annotation/VSP_047186|||http://purl.uniprot.org/annotation/VSP_055510
http://togogenome.org/gene/9606:RET                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07949                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes GFRAL-mediated MAPK1/MAPK2 phosphorylation.|||Breakpoint for translocation to form PCM1-RET; RET-CCDC6; RET-GOLGA5; RET-TRIM24 and RET-TRIM33 oncogenes|||Breakpoint for translocation to form the TRIM27/RET oncogene|||Cadherin|||Cleavage; by caspase-3|||Cytoplasmic|||Extracellular|||Extracellular cell-membrane anchored RET cadherin 120 kDa fragment|||Found in a patient with congenital central hypoventilation syndrome; unknown pathological significance.|||Found in patients with Hirschsprung disease; unknown pathological significance.|||Found in two patients with Hirschsprung disease.|||Helical|||Impaired cleavage by caspase-3 and loss of induced cell death.|||In HSCR1, pheochromocytoma, MTC and MEN2A; familial form.|||In HSCR1.|||In HSCR1; also in a colorectal cancer sample; somatic mutation.|||In HSCR1; familial form.|||In HSCR1; sporadic form.|||In HSCR1; unknown pathological significance.|||In MEN2A and HSCR1.|||In MEN2A and MTC; familial and sporadic forms.|||In MEN2A and MTC; familial form.|||In MEN2A and pheochromocytoma.|||In MEN2A, HSCR1 and MTC; familial and sporadic forms.|||In MEN2A, MTC and HSCR1.|||In MEN2A, MTC and HSCR1; familial and sporadic forms.|||In MEN2A, pheochromocytoma and MTC; familial form.|||In MEN2A, pheochromocytoma and MTC; familial form; also found as somatic mutation in a sporadic thyroid carcinoma.|||In MEN2A.|||In MEN2B and MTC; familial form.|||In MEN2B and MTC; sporadic form; somatic mutation; also found in a patient with renal agenesis.|||In MEN2B; somatic mutation in sporadic medullary thyroid carcinoma; requires 2 nucleotide substitutions.|||In MTC, MEN2A and HSCR1; familial and sporadic forms.|||In MTC; familial and sporadic forms.|||In MTC; familial form.|||In MTC; sporadic form.|||In a bladder transitional cell carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a patient with renal agenesis; unknown pathological significance; constitutively phosphorylated.|||In a patient with renal agenesis; unknown pathological significance; constitutively phosphorylated; expressed only the immature intracellular form.|||In a patient with renal agenesis; unknown pathological significance; prevents phosphorylation in response to GDNF.|||In isoform 2.|||In thyroid carcinoma; somatic mutation.|||Loss of induced cell death, but increased cell aggregation.|||Loss of kinase activity. No effect on interaction with and dissociation from CBLC and CD2AP.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proto-oncogene tyrosine-protein kinase receptor Ret|||Proton acceptor|||Soluble RET kinase fragment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024450|||http://purl.uniprot.org/annotation/PRO_0000415292|||http://purl.uniprot.org/annotation/PRO_0000415293|||http://purl.uniprot.org/annotation/VAR_006295|||http://purl.uniprot.org/annotation/VAR_006296|||http://purl.uniprot.org/annotation/VAR_006297|||http://purl.uniprot.org/annotation/VAR_006298|||http://purl.uniprot.org/annotation/VAR_006299|||http://purl.uniprot.org/annotation/VAR_006300|||http://purl.uniprot.org/annotation/VAR_006301|||http://purl.uniprot.org/annotation/VAR_006302|||http://purl.uniprot.org/annotation/VAR_006303|||http://purl.uniprot.org/annotation/VAR_006304|||http://purl.uniprot.org/annotation/VAR_006305|||http://purl.uniprot.org/annotation/VAR_006306|||http://purl.uniprot.org/annotation/VAR_006307|||http://purl.uniprot.org/annotation/VAR_006308|||http://purl.uniprot.org/annotation/VAR_006309|||http://purl.uniprot.org/annotation/VAR_006310|||http://purl.uniprot.org/annotation/VAR_006311|||http://purl.uniprot.org/annotation/VAR_006312|||http://purl.uniprot.org/annotation/VAR_006313|||http://purl.uniprot.org/annotation/VAR_006314|||http://purl.uniprot.org/annotation/VAR_006315|||http://purl.uniprot.org/annotation/VAR_006316|||http://purl.uniprot.org/annotation/VAR_006317|||http://purl.uniprot.org/annotation/VAR_006318|||http://purl.uniprot.org/annotation/VAR_006319|||http://purl.uniprot.org/annotation/VAR_006320|||http://purl.uniprot.org/annotation/VAR_006321|||http://purl.uniprot.org/annotation/VAR_006322|||http://purl.uniprot.org/annotation/VAR_006323|||http://purl.uniprot.org/annotation/VAR_006324|||http://purl.uniprot.org/annotation/VAR_006325|||http://purl.uniprot.org/annotation/VAR_006326|||http://purl.uniprot.org/annotation/VAR_006327|||http://purl.uniprot.org/annotation/VAR_006328|||http://purl.uniprot.org/annotation/VAR_006329|||http://purl.uniprot.org/annotation/VAR_006330|||http://purl.uniprot.org/annotation/VAR_006331|||http://purl.uniprot.org/annotation/VAR_006332|||http://purl.uniprot.org/annotation/VAR_006334|||http://purl.uniprot.org/annotation/VAR_006335|||http://purl.uniprot.org/annotation/VAR_006336|||http://purl.uniprot.org/annotation/VAR_006337|||http://purl.uniprot.org/annotation/VAR_006338|||http://purl.uniprot.org/annotation/VAR_006339|||http://purl.uniprot.org/annotation/VAR_006340|||http://purl.uniprot.org/annotation/VAR_006341|||http://purl.uniprot.org/annotation/VAR_006342|||http://purl.uniprot.org/annotation/VAR_006343|||http://purl.uniprot.org/annotation/VAR_006345|||http://purl.uniprot.org/annotation/VAR_006346|||http://purl.uniprot.org/annotation/VAR_006347|||http://purl.uniprot.org/annotation/VAR_006348|||http://purl.uniprot.org/annotation/VAR_006349|||http://purl.uniprot.org/annotation/VAR_008966|||http://purl.uniprot.org/annotation/VAR_009459|||http://purl.uniprot.org/annotation/VAR_009460|||http://purl.uniprot.org/annotation/VAR_009461|||http://purl.uniprot.org/annotation/VAR_009462|||http://purl.uniprot.org/annotation/VAR_009463|||http://purl.uniprot.org/annotation/VAR_009464|||http://purl.uniprot.org/annotation/VAR_009465|||http://purl.uniprot.org/annotation/VAR_009466|||http://purl.uniprot.org/annotation/VAR_009467|||http://purl.uniprot.org/annotation/VAR_009468|||http://purl.uniprot.org/annotation/VAR_009469|||http://purl.uniprot.org/annotation/VAR_009470|||http://purl.uniprot.org/annotation/VAR_009471|||http://purl.uniprot.org/annotation/VAR_009472|||http://purl.uniprot.org/annotation/VAR_009473|||http://purl.uniprot.org/annotation/VAR_009474|||http://purl.uniprot.org/annotation/VAR_009475|||http://purl.uniprot.org/annotation/VAR_009476|||http://purl.uniprot.org/annotation/VAR_009477|||http://purl.uniprot.org/annotation/VAR_009478|||http://purl.uniprot.org/annotation/VAR_009479|||http://purl.uniprot.org/annotation/VAR_009480|||http://purl.uniprot.org/annotation/VAR_009481|||http://purl.uniprot.org/annotation/VAR_009482|||http://purl.uniprot.org/annotation/VAR_009483|||http://purl.uniprot.org/annotation/VAR_009484|||http://purl.uniprot.org/annotation/VAR_009485|||http://purl.uniprot.org/annotation/VAR_009486|||http://purl.uniprot.org/annotation/VAR_009487|||http://purl.uniprot.org/annotation/VAR_009488|||http://purl.uniprot.org/annotation/VAR_009489|||http://purl.uniprot.org/annotation/VAR_009490|||http://purl.uniprot.org/annotation/VAR_009491|||http://purl.uniprot.org/annotation/VAR_009492|||http://purl.uniprot.org/annotation/VAR_009493|||http://purl.uniprot.org/annotation/VAR_011582|||http://purl.uniprot.org/annotation/VAR_012743|||http://purl.uniprot.org/annotation/VAR_012744|||http://purl.uniprot.org/annotation/VAR_012745|||http://purl.uniprot.org/annotation/VAR_018153|||http://purl.uniprot.org/annotation/VAR_018154|||http://purl.uniprot.org/annotation/VAR_018155|||http://purl.uniprot.org/annotation/VAR_018156|||http://purl.uniprot.org/annotation/VAR_018157|||http://purl.uniprot.org/annotation/VAR_035711|||http://purl.uniprot.org/annotation/VAR_035712|||http://purl.uniprot.org/annotation/VAR_041762|||http://purl.uniprot.org/annotation/VAR_041763|||http://purl.uniprot.org/annotation/VAR_041764|||http://purl.uniprot.org/annotation/VAR_041765|||http://purl.uniprot.org/annotation/VAR_041766|||http://purl.uniprot.org/annotation/VAR_041767|||http://purl.uniprot.org/annotation/VAR_044392|||http://purl.uniprot.org/annotation/VAR_044393|||http://purl.uniprot.org/annotation/VAR_044394|||http://purl.uniprot.org/annotation/VAR_044395|||http://purl.uniprot.org/annotation/VAR_044396|||http://purl.uniprot.org/annotation/VAR_044397|||http://purl.uniprot.org/annotation/VAR_044398|||http://purl.uniprot.org/annotation/VAR_067101|||http://purl.uniprot.org/annotation/VAR_067102|||http://purl.uniprot.org/annotation/VAR_067103|||http://purl.uniprot.org/annotation/VAR_067104|||http://purl.uniprot.org/annotation/VAR_067105|||http://purl.uniprot.org/annotation/VAR_067106|||http://purl.uniprot.org/annotation/VAR_067107|||http://purl.uniprot.org/annotation/VAR_067108|||http://purl.uniprot.org/annotation/VAR_067109|||http://purl.uniprot.org/annotation/VAR_067110|||http://purl.uniprot.org/annotation/VAR_067111|||http://purl.uniprot.org/annotation/VAR_067112|||http://purl.uniprot.org/annotation/VAR_067113|||http://purl.uniprot.org/annotation/VAR_067114|||http://purl.uniprot.org/annotation/VAR_067115|||http://purl.uniprot.org/annotation/VAR_067116|||http://purl.uniprot.org/annotation/VAR_067117|||http://purl.uniprot.org/annotation/VAR_067118|||http://purl.uniprot.org/annotation/VAR_067119|||http://purl.uniprot.org/annotation/VAR_067120|||http://purl.uniprot.org/annotation/VAR_067121|||http://purl.uniprot.org/annotation/VAR_067122|||http://purl.uniprot.org/annotation/VAR_067123|||http://purl.uniprot.org/annotation/VAR_067124|||http://purl.uniprot.org/annotation/VSP_040735
http://togogenome.org/gene/9606:NUDT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG26|||http://purl.uniprot.org/uniprot/Q96KB3|||http://purl.uniprot.org/uniprot/Q9BW91                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ADP-ribose pyrophosphatase, mitochondrial|||Disordered|||In isoform 2.|||Mitochondrion|||Nudix box|||Nudix hydrolase|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019950|||http://purl.uniprot.org/annotation/PRO_5004321917|||http://purl.uniprot.org/annotation/VSP_010552
http://togogenome.org/gene/9606:MOCOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EN8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In XAN2.|||MOSC|||Molybdenum cofactor sulfurase|||N6-(pyridoxal phosphate)lysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249952|||http://purl.uniprot.org/annotation/VAR_027528|||http://purl.uniprot.org/annotation/VAR_027529|||http://purl.uniprot.org/annotation/VAR_027530|||http://purl.uniprot.org/annotation/VAR_027531|||http://purl.uniprot.org/annotation/VAR_027532|||http://purl.uniprot.org/annotation/VAR_027533|||http://purl.uniprot.org/annotation/VAR_027534|||http://purl.uniprot.org/annotation/VAR_027535|||http://purl.uniprot.org/annotation/VAR_027536|||http://purl.uniprot.org/annotation/VAR_027537|||http://purl.uniprot.org/annotation/VAR_027538|||http://purl.uniprot.org/annotation/VAR_045899
http://togogenome.org/gene/9606:ZFTRAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTL6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 4 and isoform 2.|||In isoform 4.|||RING-type; degenerate|||TRAF-type|||Zinc finger TRAF-type-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328852|||http://purl.uniprot.org/annotation/VSP_061632|||http://purl.uniprot.org/annotation/VSP_061633|||http://purl.uniprot.org/annotation/VSP_061634|||http://purl.uniprot.org/annotation/VSP_061635
http://togogenome.org/gene/9606:P2RY8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VZ1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070031
http://togogenome.org/gene/9606:HIPK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL1|||http://purl.uniprot.org/uniprot/Q8NE63                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeodomain-interacting protein kinase 4|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232401|||http://purl.uniprot.org/annotation/VAR_030578|||http://purl.uniprot.org/annotation/VAR_040554|||http://purl.uniprot.org/annotation/VAR_040555|||http://purl.uniprot.org/annotation/VAR_040556|||http://purl.uniprot.org/annotation/VAR_040557|||http://purl.uniprot.org/annotation/VAR_040558|||http://purl.uniprot.org/annotation/VAR_040559|||http://purl.uniprot.org/annotation/VAR_040560
http://togogenome.org/gene/9606:CRACR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSW2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand calcium-binding domain-containing protein 4B|||Failure to localize to the Golgi membrane.|||GDP-binding mutant with reduced GTPase activity and protein stability. Reduced ability to activate JNK signaling pathway. Failure to localize to the microtubule organizing center and Golgi apparatus membrane, instead shows a predominant localization to the cytoplasm.|||GTP-binding mutant with reduced GTPase activity but increased protein stability. Increased ability to activate JNK signaling pathway. No effect on its localization to the microtubule organizing center or Golgi apparatus membrane.|||GTP/GDP-binding defective mutant with reduced GTPase activity and protein stability. Failure to localize to the microtubule organizing center and Golgi apparatus membrane, instead shows a predominant localization to the cytoplasm.|||In EF2MUT; enhanced STIM1 clustering and elevated cytoplasmic Ca2+, thereby causing cell death in T-cells. Loss of calcium-binding. Can rescue JNK phosphorylation when expressed in CRACR2A-depleted T-cells. No effect on its localization to the Golgi membrane.|||In isoform 1.|||Loss of calcium-binding and interaction with the dynein-dynactin complex; when associated with A-63; A-65 and A-97.|||Loss of calcium-binding and interaction with the dynein-dynactin complex; when associated with A-63; A-65 and A-99.|||Loss of calcium-binding and interaction with the dynein-dynactin complex; when associated with A-63; A-97 and A-99.|||Loss of calcium-binding and interaction with the dynein-dynactin complex; when associated with A-65; A-97 and A-99.|||Proline-rich domain (PRD) which mediates interaction with VAV1|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283046|||http://purl.uniprot.org/annotation/VAR_031483|||http://purl.uniprot.org/annotation/VAR_031484|||http://purl.uniprot.org/annotation/VAR_031485|||http://purl.uniprot.org/annotation/VAR_031486|||http://purl.uniprot.org/annotation/VAR_031487|||http://purl.uniprot.org/annotation/VAR_031488|||http://purl.uniprot.org/annotation/VSP_060977|||http://purl.uniprot.org/annotation/VSP_060978
http://togogenome.org/gene/9606:TUBB2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13885                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CDCBM5; abolishes coassembly with tubulin subunits and incorporation into the microtubule polymer network.|||In CDCBM5; reduces coassembly with tubulin subunits and incorporation into the microtubule polymer network.|||In a colorectal cancer sample; somatic mutation.|||MREI motif|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta-2A chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262648|||http://purl.uniprot.org/annotation/VAR_036197|||http://purl.uniprot.org/annotation/VAR_071168|||http://purl.uniprot.org/annotation/VAR_071169
http://togogenome.org/gene/9606:AP3B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GYB0|||http://purl.uniprot.org/uniprot/Q13367                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP-3 complex subunit beta-2|||Acidic residues|||Basic and acidic residues|||Clathrin/coatomer adaptor adaptin-like N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193748|||http://purl.uniprot.org/annotation/VSP_043905|||http://purl.uniprot.org/annotation/VSP_054918|||http://purl.uniprot.org/annotation/VSP_054919
http://togogenome.org/gene/9606:SEPTIN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3D0|||http://purl.uniprot.org/uniprot/B4DNE4|||http://purl.uniprot.org/uniprot/G3V1Q4|||http://purl.uniprot.org/uniprot/Q16181                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||Interaction with SEPTIN12|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Septin-7|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173528|||http://purl.uniprot.org/annotation/VSP_022202
http://togogenome.org/gene/9606:PCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35558                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished both phosphoenolpyruvate carboxykinase and protein kinase activities.|||Abolished phosphorylation by AKT1, interaction with INSIG proteins (INSIG1 and INSIG2) and ability to regulate lipogenesis.|||Abolishes acetylation and increases protein stability; when associated with R-70 and R-594.|||Abolishes acetylation and increases protein stability; when associated with R-70 and R-71.|||Abolishes acetylation and increases protein stability; when associated with R-71 and R-594.|||In PCKDC; decreased phosphoenolpyruvate carboxykinase activity.|||In PCKDC; decreased stability; no effect on phosphoenolpyruvate carboxykinase activity.|||In PCKDC; unknown pathological significance; decreased phosphoenolpyruvate carboxykinase activity.|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; by p300/EP300|||Omega-loop|||Phosphoenolpyruvate carboxykinase, cytosolic [GTP]|||Phosphomimetic mutant, promotes the serine protein kinase activity by reducing the binding affinity to oxaloacetate.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000103627|||http://purl.uniprot.org/annotation/VAR_015575|||http://purl.uniprot.org/annotation/VAR_021072|||http://purl.uniprot.org/annotation/VAR_021073|||http://purl.uniprot.org/annotation/VAR_021074|||http://purl.uniprot.org/annotation/VAR_021075|||http://purl.uniprot.org/annotation/VAR_021076|||http://purl.uniprot.org/annotation/VAR_021077|||http://purl.uniprot.org/annotation/VAR_021078|||http://purl.uniprot.org/annotation/VAR_042444|||http://purl.uniprot.org/annotation/VAR_079633|||http://purl.uniprot.org/annotation/VAR_079634|||http://purl.uniprot.org/annotation/VAR_079635|||http://purl.uniprot.org/annotation/VSP_057073|||http://purl.uniprot.org/annotation/VSP_057074
http://togogenome.org/gene/9606:ZNF276                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L9I3|||http://purl.uniprot.org/uniprot/Q8N554                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||May increase breast cancer risk.|||Polar residues|||ZAD|||Zinc finger protein 276                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047323|||http://purl.uniprot.org/annotation/VAR_019125|||http://purl.uniprot.org/annotation/VAR_019126|||http://purl.uniprot.org/annotation/VAR_032708|||http://purl.uniprot.org/annotation/VAR_032709|||http://purl.uniprot.org/annotation/VSP_026104
http://togogenome.org/gene/9606:RFTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14699|||http://purl.uniprot.org/uniprot/Q8N5I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of association with membranes. Same effect; when associated with S-3.|||N-myristoyl glycine|||Partially affects association with membranes. Loss of association with membranes; when associated with A-2.|||Phosphoserine|||Polar residues|||Raftlin|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050718|||http://purl.uniprot.org/annotation/VAR_051317|||http://purl.uniprot.org/annotation/VAR_061699
http://togogenome.org/gene/9606:DNASE1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13609                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Bipartite nuclear localization signal|||Deoxyribonuclease gamma|||Essential for enzymatic activity|||In a breast cancer sample; somatic mutation.|||In a breast cancer sample; somatic mutation; diminishes enzymatic activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Not required for free DNA-nuclease activity but required for activity towards liposome-coated DNA|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007288|||http://purl.uniprot.org/annotation/VAR_036079|||http://purl.uniprot.org/annotation/VAR_036080|||http://purl.uniprot.org/annotation/VAR_036081|||http://purl.uniprot.org/annotation/VAR_059249|||http://purl.uniprot.org/annotation/VAR_061137|||http://purl.uniprot.org/annotation/VAR_076797|||http://purl.uniprot.org/annotation/VSP_047251
http://togogenome.org/gene/9606:UNC80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2C7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In IHPRF2.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||In isoform 5 and isoform 7.|||In isoform 7.|||Phosphoserine|||Polar residues|||Protein unc-80 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089348|||http://purl.uniprot.org/annotation/VAR_033656|||http://purl.uniprot.org/annotation/VAR_060196|||http://purl.uniprot.org/annotation/VAR_075874|||http://purl.uniprot.org/annotation/VAR_075875|||http://purl.uniprot.org/annotation/VSP_031528|||http://purl.uniprot.org/annotation/VSP_036741|||http://purl.uniprot.org/annotation/VSP_036742|||http://purl.uniprot.org/annotation/VSP_036743|||http://purl.uniprot.org/annotation/VSP_036744|||http://purl.uniprot.org/annotation/VSP_036745|||http://purl.uniprot.org/annotation/VSP_036746|||http://purl.uniprot.org/annotation/VSP_054289
http://togogenome.org/gene/9606:BRD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXI2|||http://purl.uniprot.org/uniprot/Q9H8M2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Bromodomain-containing protein 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone H4K5ac H4K8ac and histone H4K5bu H4K8bu binding|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239219|||http://purl.uniprot.org/annotation/VAR_033635|||http://purl.uniprot.org/annotation/VAR_033636|||http://purl.uniprot.org/annotation/VAR_059143|||http://purl.uniprot.org/annotation/VSP_019112|||http://purl.uniprot.org/annotation/VSP_019113|||http://purl.uniprot.org/annotation/VSP_019114|||http://purl.uniprot.org/annotation/VSP_019115|||http://purl.uniprot.org/annotation/VSP_037493|||http://purl.uniprot.org/annotation/VSP_037494|||http://purl.uniprot.org/annotation/VSP_043234
http://togogenome.org/gene/9606:LYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12980                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||Protein lyl-1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127262
http://togogenome.org/gene/9606:LTO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV07                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Protein LTO1 homolog|||Removed|||deca-GX3 motif; required for interaction with YAE1 and the CIA complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058075|||http://purl.uniprot.org/annotation/VAR_062231
http://togogenome.org/gene/9606:RNF141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVD5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  N-myristoyl glycine|||RING finger protein 141|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056101
http://togogenome.org/gene/9606:RBMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z499|||http://purl.uniprot.org/uniprot/P29558                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 4.|||Phosphothreonine|||Polar residues|||RNA-binding motif, single-stranded-interacting protein 1|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081798|||http://purl.uniprot.org/annotation/VSP_011930|||http://purl.uniprot.org/annotation/VSP_037790|||http://purl.uniprot.org/annotation/VSP_037791
http://togogenome.org/gene/9606:TLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEF9|||http://purl.uniprot.org/uniprot/Q04724|||http://purl.uniprot.org/uniprot/Q59EF7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes HESX1 binding.|||Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK1|||Polar residues|||Pro residues|||Q domain|||SP domain|||Transducin-like enhancer protein 1|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051276
http://togogenome.org/gene/9606:MPST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJX3|||http://purl.uniprot.org/uniprot/P25325                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-mercaptopyruvate sulfurtransferase|||Cysteine persulfide intermediate|||Hinge|||In isoform 2.|||Interchain (with C-264); redox-active|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Removed|||Rhodanese|||Rhodanese 1|||Rhodanese 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139398|||http://purl.uniprot.org/annotation/VSP_055027
http://togogenome.org/gene/9606:ANKLE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK|||Ankyrin repeat and LEM domain-containing protein 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type III membrane protein|||In MCPH16.|||In MCPH16; unknown pathological significance.|||In MCPH16; unknown pathological significance; severe loss of VRK1 nuclear localization in non-dividing cells.|||In isoform 2.|||In isoform 3.|||LEM|||Lumenal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280242|||http://purl.uniprot.org/annotation/VAR_031097|||http://purl.uniprot.org/annotation/VAR_031098|||http://purl.uniprot.org/annotation/VAR_031099|||http://purl.uniprot.org/annotation/VAR_076205|||http://purl.uniprot.org/annotation/VAR_083604|||http://purl.uniprot.org/annotation/VAR_083605|||http://purl.uniprot.org/annotation/VAR_083606|||http://purl.uniprot.org/annotation/VAR_083607|||http://purl.uniprot.org/annotation/VAR_083608|||http://purl.uniprot.org/annotation/VAR_083609|||http://purl.uniprot.org/annotation/VAR_083610|||http://purl.uniprot.org/annotation/VAR_083611|||http://purl.uniprot.org/annotation/VAR_083612|||http://purl.uniprot.org/annotation/VSP_023574|||http://purl.uniprot.org/annotation/VSP_023575|||http://purl.uniprot.org/annotation/VSP_044173
http://togogenome.org/gene/9606:RPAIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTT3|||http://purl.uniprot.org/uniprot/Q86UA6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes sumoylation; when associated with R-114 and R-121.|||Abolishes sumoylation; when associated with R-121 and R-142.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Induces a strong decrease in sumoylation; when associated with N-103. Abolishes sumoylation; when associated with R-114 and R-142.|||Mediates nuclear export|||Phosphoserine|||RIP-type|||RPA-interacting protein|||RPA-interacting protein N-terminal|||Sumoylated and increases total protein sumoylation levels.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076299|||http://purl.uniprot.org/annotation/VAR_023947|||http://purl.uniprot.org/annotation/VSP_016402|||http://purl.uniprot.org/annotation/VSP_016403|||http://purl.uniprot.org/annotation/VSP_016404|||http://purl.uniprot.org/annotation/VSP_016405|||http://purl.uniprot.org/annotation/VSP_016406|||http://purl.uniprot.org/annotation/VSP_016407|||http://purl.uniprot.org/annotation/VSP_016408|||http://purl.uniprot.org/annotation/VSP_016409|||http://purl.uniprot.org/annotation/VSP_016410|||http://purl.uniprot.org/annotation/VSP_045356|||http://purl.uniprot.org/annotation/VSP_046795
http://togogenome.org/gene/9606:DSTYK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XUX3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dual serine/threonine and tyrosine protein kinase|||In CAKUT1.|||In CAKUT1; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No change.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233118|||http://purl.uniprot.org/annotation/VAR_057101|||http://purl.uniprot.org/annotation/VAR_071324|||http://purl.uniprot.org/annotation/VAR_071325|||http://purl.uniprot.org/annotation/VAR_071326|||http://purl.uniprot.org/annotation/VSP_018030|||http://purl.uniprot.org/annotation/VSP_018031|||http://purl.uniprot.org/annotation/VSP_018032|||http://purl.uniprot.org/annotation/VSP_018033|||http://purl.uniprot.org/annotation/VSP_018034
http://togogenome.org/gene/9606:NUP205                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92621                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In NPHS13; abrogates interaction with NUP93.|||N-acetylalanine|||Nuclear pore complex protein Nup205|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204859|||http://purl.uniprot.org/annotation/VAR_050567|||http://purl.uniprot.org/annotation/VAR_050568|||http://purl.uniprot.org/annotation/VAR_076471
http://togogenome.org/gene/9606:BTG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY30                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In OZEMA8.|||In OZEMA8; loss-of-function variant resulting in impaired maternal mRNA decay in fertilized oocytes from the affected individual; abolishes the interaction with CNOT7.|||In isoform 2.|||Protein BTG4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143810|||http://purl.uniprot.org/annotation/VAR_084759|||http://purl.uniprot.org/annotation/VAR_084760|||http://purl.uniprot.org/annotation/VSP_053851
http://togogenome.org/gene/9606:SQSTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13501                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  75% decrease in MAP1LC3B-binding.|||Abolished ability to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes.|||Basic and acidic residues|||Breakpoint for translocation to form the NUP214-SQSTM1 fusion protein|||Confirmed at protein level.|||Decreased activation of NF-kappa-B.|||Decreased ubiquitination by the BCR(KEAP1) complex, leading to decreased sequestering activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In FTDALS3.|||In FTDALS3; likely benign variant.|||In PDB3 and FTDALS3.|||In PDB3 and FTDALS3; loss of polyubiquitin-binding and increased activation of NF-kappa-B.|||In PDB3 and FTDALS3; no effect on polyubiquitin-binding.|||In PDB3.|||In PDB3; loss of polyubiquitin-binding.|||In isoform 2.|||Interaction with GABRR3|||Interaction with KEAP1|||Interaction with LCK|||Interaction with NTRK1|||Interaction with PAWR|||Interaction with PRKCZ and dimerization|||LIM protein-binding (LB)|||LIR|||Loss of interaction with PRKCI. Alters dimerization.|||Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69.|||Loss of polyubiquitin-binding.|||MAP1LC3B-binding|||N-acetylalanine|||No effect on MAP1LC3B-binding.|||No effect on interaction with LCK.|||No effect on interaction with PRKCI.|||No effect on interaction with PRKCZ.|||No effect on interactions with PRKCZ and PRKCI.|||No effect on interactions with PRKCZ, PRKCI and NBR1. Loss of localization in cytoplasmic inclusion bodies. Loss of dimerization; when associated with A-7.|||No effect on polyubiquitin-binding.|||PB1|||Partial loss of polyubiquitin-binding. Loss of localization to cytoplasmic inclusion bodies.|||Phosphoserine|||Phosphoserine; by ULK1 and TBK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Sequestosome-1|||Strong decrease in MAP1LC3B-binding, disrupts interaction with GABARAP.|||Strongly decreased interaction with KEAP1.|||TRAF6-binding|||UBA|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072176|||http://purl.uniprot.org/annotation/VAR_023590|||http://purl.uniprot.org/annotation/VAR_023591|||http://purl.uniprot.org/annotation/VAR_023592|||http://purl.uniprot.org/annotation/VAR_023593|||http://purl.uniprot.org/annotation/VAR_023594|||http://purl.uniprot.org/annotation/VAR_023595|||http://purl.uniprot.org/annotation/VAR_023596|||http://purl.uniprot.org/annotation/VAR_023597|||http://purl.uniprot.org/annotation/VAR_023598|||http://purl.uniprot.org/annotation/VAR_061707|||http://purl.uniprot.org/annotation/VAR_068915|||http://purl.uniprot.org/annotation/VAR_073899|||http://purl.uniprot.org/annotation/VAR_073900|||http://purl.uniprot.org/annotation/VAR_073901|||http://purl.uniprot.org/annotation/VAR_073902|||http://purl.uniprot.org/annotation/VAR_073903|||http://purl.uniprot.org/annotation/VAR_073904|||http://purl.uniprot.org/annotation/VAR_073905|||http://purl.uniprot.org/annotation/VAR_073906|||http://purl.uniprot.org/annotation/VAR_073907|||http://purl.uniprot.org/annotation/VAR_073908|||http://purl.uniprot.org/annotation/VAR_073909|||http://purl.uniprot.org/annotation/VAR_073910|||http://purl.uniprot.org/annotation/VAR_073911|||http://purl.uniprot.org/annotation/VAR_073912|||http://purl.uniprot.org/annotation/VAR_073913|||http://purl.uniprot.org/annotation/VAR_073914|||http://purl.uniprot.org/annotation/VAR_073915|||http://purl.uniprot.org/annotation/VAR_073916|||http://purl.uniprot.org/annotation/VAR_073917|||http://purl.uniprot.org/annotation/VAR_073918|||http://purl.uniprot.org/annotation/VAR_073919|||http://purl.uniprot.org/annotation/VAR_073920|||http://purl.uniprot.org/annotation/VAR_073921|||http://purl.uniprot.org/annotation/VAR_073922|||http://purl.uniprot.org/annotation/VAR_073923|||http://purl.uniprot.org/annotation/VAR_073924|||http://purl.uniprot.org/annotation/VAR_073925|||http://purl.uniprot.org/annotation/VAR_073926|||http://purl.uniprot.org/annotation/VAR_073927|||http://purl.uniprot.org/annotation/VAR_073928|||http://purl.uniprot.org/annotation/VAR_073929|||http://purl.uniprot.org/annotation/VAR_073930|||http://purl.uniprot.org/annotation/VAR_073931|||http://purl.uniprot.org/annotation/VAR_073932|||http://purl.uniprot.org/annotation/VAR_073933|||http://purl.uniprot.org/annotation/VAR_073934|||http://purl.uniprot.org/annotation/VAR_073935|||http://purl.uniprot.org/annotation/VAR_073936|||http://purl.uniprot.org/annotation/VAR_073937|||http://purl.uniprot.org/annotation/VSP_015841
http://togogenome.org/gene/9606:MTHFSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN17|||http://purl.uniprot.org/uniprot/Q2M296                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Methenyltetrahydrofolate synthase domain-containing protein|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295871|||http://purl.uniprot.org/annotation/VAR_033373|||http://purl.uniprot.org/annotation/VAR_033374|||http://purl.uniprot.org/annotation/VAR_033375|||http://purl.uniprot.org/annotation/VAR_068902|||http://purl.uniprot.org/annotation/VAR_068903|||http://purl.uniprot.org/annotation/VSP_027115|||http://purl.uniprot.org/annotation/VSP_044492
http://togogenome.org/gene/9606:TMEM213                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRL7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Transmembrane protein 213                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337054|||http://purl.uniprot.org/annotation/VSP_039555|||http://purl.uniprot.org/annotation/VSP_039556|||http://purl.uniprot.org/annotation/VSP_039557
http://togogenome.org/gene/9606:ACOT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00154                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cytosolic acyl coenzyme A thioester hydrolase|||Disordered|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053806|||http://purl.uniprot.org/annotation/VSP_000151|||http://purl.uniprot.org/annotation/VSP_000152|||http://purl.uniprot.org/annotation/VSP_000153|||http://purl.uniprot.org/annotation/VSP_000154|||http://purl.uniprot.org/annotation/VSP_000155|||http://purl.uniprot.org/annotation/VSP_000156|||http://purl.uniprot.org/annotation/VSP_047094
http://togogenome.org/gene/9606:UTP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75691                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Decreases nucleolar localization.|||Disordered|||Does not decrease nucleolar localization.|||HEAT 1|||HEAT 2|||In a breast cancer sample; somatic mutation.|||Inhibits nucleolar but not nuclear localization.|||Inhibits nucleolar localization and decreases nuclear localization.|||Nuclear localization signal|||Nucleolar localization signal|||Phosphoserine|||Phosphothreonine|||Small subunit processome component 20 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080011|||http://purl.uniprot.org/annotation/VAR_022162|||http://purl.uniprot.org/annotation/VAR_022163|||http://purl.uniprot.org/annotation/VAR_036274|||http://purl.uniprot.org/annotation/VAR_036275|||http://purl.uniprot.org/annotation/VAR_055135|||http://purl.uniprot.org/annotation/VAR_055136
http://togogenome.org/gene/9606:FCHSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94868                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ITSN1 and location at clathrin-coated pits; when associated with S-576.|||Abolishes interaction with ITSN1 and location at clathrin-coated pits; when associated with S-607.|||Abolishes interaction with ITSN1.|||Disordered|||F-BAR|||F-BAR and double SH3 domains protein 2|||Impaired recruitment to the cell membrane.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increased recruitment to the cell membrane.|||Loss of ability to promote actin polymerization; when associated with A-478.|||Loss of ability to promote actin polymerization; when associated with A-480.|||Loss of ability to promote actin polymerization; when associated with A-521.|||Loss of ability to promote actin polymerization; when associated with A-524.|||Phosphoserine|||Polar residues|||Pro residues|||Required and sufficient for location at clathrin-coated pits|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278214|||http://purl.uniprot.org/annotation/VSP_023167|||http://purl.uniprot.org/annotation/VSP_023168|||http://purl.uniprot.org/annotation/VSP_023169
http://togogenome.org/gene/9606:TUBG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B4Z394|||http://purl.uniprot.org/uniprot/Q9NRH3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine; by BRSK1|||Tubulin gamma-2 chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048468|||http://purl.uniprot.org/annotation/VAR_020418
http://togogenome.org/gene/9606:AP5S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUS5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  AP-5 complex subunit sigma-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079423
http://togogenome.org/gene/9606:SKP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63208                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||Interaction with the F-box domain of F-box proteins|||Phosphothreonine|||Removed|||S-phase kinase-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187251|||http://purl.uniprot.org/annotation/VSP_007555
http://togogenome.org/gene/9606:CDC42EP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14613                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CRIB|||Cdc42 effector protein 2|||Disordered|||N-acetylserine|||No binding with CDC42; no induced pseudopodia formation.|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212648|||http://purl.uniprot.org/annotation/VAR_023001|||http://purl.uniprot.org/annotation/VAR_023002
http://togogenome.org/gene/9606:POM121L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||POM121-like protein 2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292039
http://togogenome.org/gene/9606:H3C8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:TASOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein TASOR|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295728|||http://purl.uniprot.org/annotation/VAR_033350|||http://purl.uniprot.org/annotation/VAR_033351|||http://purl.uniprot.org/annotation/VAR_033352|||http://purl.uniprot.org/annotation/VAR_055092|||http://purl.uniprot.org/annotation/VAR_059595|||http://purl.uniprot.org/annotation/VSP_027030|||http://purl.uniprot.org/annotation/VSP_027031|||http://purl.uniprot.org/annotation/VSP_027032|||http://purl.uniprot.org/annotation/VSP_027033|||http://purl.uniprot.org/annotation/VSP_027034
http://togogenome.org/gene/9606:CYS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q717R9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Ciliary targeting motif|||Cystin-1|||Disordered|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261177
http://togogenome.org/gene/9606:SLC16A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15375                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Monocarboxylate transporter 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211399|||http://purl.uniprot.org/annotation/VSP_056660|||http://purl.uniprot.org/annotation/VSP_056661
http://togogenome.org/gene/9606:IZUMO1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6ND01                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with IZUMO1.|||GPI-anchor amidated serine|||Important for interaction with IZUMO1|||In isoform 2.|||Mildly decreases interaction with IZUMO1.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes interaction with IZUMO1.|||Sperm-egg fusion protein Juno                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332987|||http://purl.uniprot.org/annotation/PRO_0000429472|||http://purl.uniprot.org/annotation/VSP_040470
http://togogenome.org/gene/9606:PIK3IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FE7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kringle|||N-linked (GlcNAc...) (complex) asparagine|||O-linked (GalNAc...) serine|||Phosphoinositide-3-kinase-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280347|||http://purl.uniprot.org/annotation/VAR_031121|||http://purl.uniprot.org/annotation/VSP_023638|||http://purl.uniprot.org/annotation/VSP_023639|||http://purl.uniprot.org/annotation/VSP_023640|||http://purl.uniprot.org/annotation/VSP_043368|||http://purl.uniprot.org/annotation/VSP_053370
http://togogenome.org/gene/9606:SNRNP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  U11/U12 small nuclear ribonucleoprotein 25 kDa protein|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114924
http://togogenome.org/gene/9606:EIF1AD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9N8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Probable RNA-binding protein EIF1AD|||S1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314151|||http://purl.uniprot.org/annotation/VAR_037851|||http://purl.uniprot.org/annotation/VAR_037852
http://togogenome.org/gene/9606:ZNF444                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Y2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||SCAN box|||Zinc finger protein 444                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047593|||http://purl.uniprot.org/annotation/VSP_008798
http://togogenome.org/gene/9606:CABP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0K2|||http://purl.uniprot.org/uniprot/Q9NPB3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcium-binding protein 2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In DFNB93.|||In isoform S-CaBP2.|||N-myristoyl glycine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073517|||http://purl.uniprot.org/annotation/VAR_063087|||http://purl.uniprot.org/annotation/VAR_080405|||http://purl.uniprot.org/annotation/VSP_000734
http://togogenome.org/gene/9606:SRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DU24|||http://purl.uniprot.org/uniprot/P11831                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Involved in dimerization|||MADS-box|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by dsDNA kinase|||Serum response factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000181|||http://purl.uniprot.org/annotation/CAR_000196|||http://purl.uniprot.org/annotation/PRO_0000199423
http://togogenome.org/gene/9606:PSMC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2M0|||http://purl.uniprot.org/uniprot/P43686                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  26S proteasome regulatory subunit 6B|||AAA+ ATPase|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084686|||http://purl.uniprot.org/annotation/VSP_000022
http://togogenome.org/gene/9606:ENY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPA8                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Splice Variant|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Transcription and mRNA export factor ENY2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314130|||http://purl.uniprot.org/annotation/VSP_046891
http://togogenome.org/gene/9606:ZNF700                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVH9|||http://purl.uniprot.org/uniprot/Q9H0M5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 700                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233280|||http://purl.uniprot.org/annotation/VAR_033591|||http://purl.uniprot.org/annotation/VAR_052897
http://togogenome.org/gene/9606:KCNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IRL4|||http://purl.uniprot.org/uniprot/A9LNM6|||http://purl.uniprot.org/uniprot/Q6UVM3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated potassium channel BK alpha subunit|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In DEE57; decreased protein abundance; loss of chloride-activated potassium channel activity; loss of potassium selectivity.|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Pore-forming|||Potassium channel|||Potassium channel subfamily T member 2|||RCK N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312503|||http://purl.uniprot.org/annotation/VAR_037527|||http://purl.uniprot.org/annotation/VAR_037528|||http://purl.uniprot.org/annotation/VAR_037529|||http://purl.uniprot.org/annotation/VAR_080867|||http://purl.uniprot.org/annotation/VSP_029852|||http://purl.uniprot.org/annotation/VSP_029853|||http://purl.uniprot.org/annotation/VSP_029854|||http://purl.uniprot.org/annotation/VSP_029855|||http://purl.uniprot.org/annotation/VSP_029856|||http://purl.uniprot.org/annotation/VSP_029857
http://togogenome.org/gene/9606:FLII                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13045                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||In isoform 2.|||In isoform 3.|||Interaction with ACTL6A|||Interaction with LRRFIP1 and LRRFIP2|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-acetylmethionine|||N6-acetyllysine|||No change in ESR1 binding but reduced binding to ACTL6A and reduced coactivator function.|||No change in binding to ACTL6A or in coactivator function.|||Phosphoserine|||Phosphoserine; by SGK3|||Phosphothreonine; by SGK3|||Protein flightless-1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218750|||http://purl.uniprot.org/annotation/VAR_029258|||http://purl.uniprot.org/annotation/VSP_044686|||http://purl.uniprot.org/annotation/VSP_044687|||http://purl.uniprot.org/annotation/VSP_046887
http://togogenome.org/gene/9606:FAM187B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17R55                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protein FAM187B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284626|||http://purl.uniprot.org/annotation/VAR_031790|||http://purl.uniprot.org/annotation/VAR_031791|||http://purl.uniprot.org/annotation/VAR_031792
http://togogenome.org/gene/9606:CGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYZ4|||http://purl.uniprot.org/uniprot/P01215|||http://purl.uniprot.org/uniprot/Q6I9S8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Glycoprotein hormones alpha chain|||Increases from 1 to 3 the number of FSH binding a single FSHR receptor.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000036|||http://purl.uniprot.org/annotation/CAR_000037|||http://purl.uniprot.org/annotation/PRO_0000011640|||http://purl.uniprot.org/annotation/PRO_5005391042|||http://purl.uniprot.org/annotation/PRO_5014205941
http://togogenome.org/gene/9606:NDUFA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2Y9D025|||http://purl.uniprot.org/uniprot/P56556                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Complex 1 LYR protein|||In MC1DN33.|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174302|||http://purl.uniprot.org/annotation/VAR_014483|||http://purl.uniprot.org/annotation/VAR_081470|||http://purl.uniprot.org/annotation/VAR_081471
http://togogenome.org/gene/9606:HOXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CA4|||http://purl.uniprot.org/uniprot/Q9GZZ0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200201|||http://purl.uniprot.org/annotation/VAR_034003
http://togogenome.org/gene/9606:PDCD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZ42|||http://purl.uniprot.org/uniprot/A0A087WZ38|||http://purl.uniprot.org/uniprot/O75340|||http://purl.uniprot.org/uniprot/Q53FC3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11.|||Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. Does not affect interaction with TFG and SEC31A.|||Abolishes the interaction with SEC31A, PDCD6IP, ANXA7 and ANXA11.|||Does not affect interaction with SEC31A. Does not affect interaction with PDCD6IP.|||Does not affect interaction with SEC31A. Reduces the interaction with HEBP2, PDCD6IP and ANXA7.|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Impairs interaction with ANXA11.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increases interaction with PDCD6IP and ANXA7. Impairs interaction with ANXA11. Augments stauroporine-induced cell death.|||Increases interaction with PDCD6IP. Impairs interaction with ANAX7 and ANXA11.|||Increases interaction with PDCD6IP. Impairs interaction with ANXA11.|||Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114.|||Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47.|||N-acetylalanine|||Programmed cell death protein 6|||Removed|||Slightly reduced interaction with SEC31A. Does not affect interaction with PDCD6IP.|||Strongly impaired interaction with SEC31A and TFG. Does not affect interaction with PDCD6IP.|||Strongly impaired interaction with SEC31A. Slightly reduced interaction with PDCD6IP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073729|||http://purl.uniprot.org/annotation/VAR_035459|||http://purl.uniprot.org/annotation/VSP_045113|||http://purl.uniprot.org/annotation/VSP_045542
http://togogenome.org/gene/9606:SMPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MPD7; unknown pathological significance.|||Small muscular protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071978|||http://purl.uniprot.org/annotation/VAR_087073|||http://purl.uniprot.org/annotation/VAR_087074|||http://purl.uniprot.org/annotation/VAR_087075|||http://purl.uniprot.org/annotation/VAR_087076
http://togogenome.org/gene/9606:KLC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P597                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Kinesin light chain 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230785|||http://purl.uniprot.org/annotation/VSP_017831|||http://purl.uniprot.org/annotation/VSP_017832
http://togogenome.org/gene/9606:CHERP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||CID|||Calcium homeostasis endoplasmic reticulum protein|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SURP motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299492|||http://purl.uniprot.org/annotation/VAR_034833
http://togogenome.org/gene/9606:LOC124903767                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6K4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Putative uncharacterized protein MGC34800                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329444
http://togogenome.org/gene/9606:TMIE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEW7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNB6.|||Transmembrane inner ear expressed protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022555|||http://purl.uniprot.org/annotation/VAR_021524|||http://purl.uniprot.org/annotation/VAR_021525|||http://purl.uniprot.org/annotation/VAR_021526
http://togogenome.org/gene/9606:HSFX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK21|||http://purl.uniprot.org/uniprot/Q9UBD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||HSF-type DNA-binding|||Heat shock transcription factor, X-linked|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339188
http://togogenome.org/gene/9606:SAMHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H15|||http://purl.uniprot.org/uniprot/Q9Y3Z3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Phosphothreonine|||Abolished ability to restrict infection by viruses.|||Abolished ability to restrict infection by viruses. Abolishes dNTPase activity; when associated with A-312 and A-366. Does not affect ability to promote DNA end resection at stalled replication forks; when associated with A-312.|||Abolished dNTPase activity without affecting homotetramerization.|||Abolished dNTPase activity without affecting homotetramerization. Abolished ability to restrict infection by viruses.|||Abolished dNTPase activity without affecting homotetramerization. Abolished dNTPase activity; when associated with A-319.|||Abolished homotetramerization and dNTPase activity.|||Abolishes dNTPase activity; when associated with A-149.|||Abolishes dNTPase activity; when associated with A-312 and A-315.|||Abolishes dNTPase activity; when associated with A-315 and A-366. Does not affect ability to promote DNA end resection at stalled replication forks; when associated with A-315.|||Abolishes dNTPase activity; when associated with A-370.|||Abolishes dNTPase activity; when associated with G-374.|||Abolishes proteasomal degradation triggered by the viral accessory protein vpx.|||Abolishes zinc binding and dNTPase activity. Does not affect ability to promote DNA end resection at stalled replication forks.|||Basic and acidic residues|||Decreases dNTPase activity. Impairs homotetramerization and nearly abolishes dNTPase activity; when associated with E-451.|||Deoxynucleoside triphosphate triphosphohydrolase SAMHD1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD|||Impaired ability to promote DNA end resection at stalled replication forks. Promotes dNTPase activity and ability to restrict infection by viruses.|||Impaired homotetramerization and slightly reduced dNTPase activity. Impaired homotetramerization and reduced dNTPase activity A-330.|||Impaired homotetramerization and slightly reduced dNTPase activity. Impaired homotetramerization and reduced dNTPase activity; when associated with A-358.|||Impairs homotetramerization and abolishes dNTPase activity.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-352 and A-376.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-352 and A-377.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-376 and A-377.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-534 and D-540.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-537 and A-534.|||Impairs homotetramerization and abolishes dNTPase activity; when associated with A-537 and D-540.|||Impairs homotetramerization and nearly abolishes dNTPase activity.|||Impairs homotetramerization and nearly abolishes dNTPase activity. Abolished ability to restrict infection by viruses.|||Impairs homotetramerization and nearly abolishes dNTPase activity; when associated with E-145.|||Impairs homotetramerization and nearly abolishes dNTPase activity; when associated with K-145.|||Impairs homotetramerization and nearly abolishes dNTPase activity; when associated with K-364.|||Impairs homotetramerization and nearly abolishes dNTPase activity; when associated with R-361.|||In AGS5 and CHBL2; loss of function in defense response to virus; decreased oligomerization; decreased ability to restrict LINE-1 retrotransposon activity.|||In AGS5.|||In AGS5; Does not affect dNTP regulation, while affecting ability to promote DNA end resection at stalled replication forks.|||In AGS5; does not affect oligomerization; decreased ability to restrict LINE-1 retrotransposon activity; does not affect localization to nucleus.|||In AGS5; loss of function in defense response to virus; decreased oligomerization.|||In AGS5; loss of function in defense response to virus; decreased oligomerization; does not affect localization to nucleus; novel localization to the cytoplasm.|||In AGS5; loss of function in defense response to virus; does not affect oligomerization; decreased ability to restrict LINE-1 retrotransposon activity.|||In AGS5; loss of function in defense response to virus; loss of oligomerization.|||In AGS5; loss of function in defense response to virus; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity.|||In AGS5; loss of oligomerization.|||In AGS5; loss of oligomerization; decreased ability to restrict LINE-1 retrotransposon activity.|||In isoform 3.|||In isoform 4.|||Increased stability of the tetramer and increased deoxynucleoside triphosphate (dNTPase) activity; when associated with F-77 and F-80 and R-111.|||Increased stability of the tetramer and increased deoxynucleoside triphosphate (dNTPase) activity; when associated with F-77 and F-80.|||Increased stability of the tetramer and increased deoxynucleoside triphosphate (dNTPase) activity; when associated with F-77 and R-111.|||Loss of dNTPase activity.|||Loss of function in defense response to virus.|||Loss of function in defense response to virus. Does not affect oligomerization. Retains dNTPase activity.|||Loss of function in defense response to virus. Loss of dNTPase activity. Does not affect oligomerization.|||Loss of phosphorylation by human cytomegalovirus/HCMV kinase UL97.|||Mimicks phosphorylation state, retains ability to promote DNA end resection at stalled replication forks. Induces large conformational changes that impair homotetramerization, leading to reduced dNTPase activity and decreased ability to restrict infection by viruses.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Promotes ability to restrict infection by viruses.|||SAM|||in other chain ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153732|||http://purl.uniprot.org/annotation/VAR_058481|||http://purl.uniprot.org/annotation/VAR_058482|||http://purl.uniprot.org/annotation/VAR_058483|||http://purl.uniprot.org/annotation/VAR_058484|||http://purl.uniprot.org/annotation/VAR_058485|||http://purl.uniprot.org/annotation/VAR_058486|||http://purl.uniprot.org/annotation/VAR_058487|||http://purl.uniprot.org/annotation/VAR_058488|||http://purl.uniprot.org/annotation/VAR_058489|||http://purl.uniprot.org/annotation/VAR_070633|||http://purl.uniprot.org/annotation/VAR_070634|||http://purl.uniprot.org/annotation/VAR_078239|||http://purl.uniprot.org/annotation/VAR_078240|||http://purl.uniprot.org/annotation/VAR_080530|||http://purl.uniprot.org/annotation/VSP_046561|||http://purl.uniprot.org/annotation/VSP_046562
http://togogenome.org/gene/9606:ACY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03154|||http://purl.uniprot.org/uniprot/V9HWA0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost abolishes enzyme activity.|||Aminoacylase-1|||Decreased protein stability. Loss of enzyme activity.|||In ACY1D.|||In ACY1D; loss of activity.|||In ACY1D; slightly reduced activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Peptidase M20 dimerisation|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185236|||http://purl.uniprot.org/annotation/VAR_020452|||http://purl.uniprot.org/annotation/VAR_026104|||http://purl.uniprot.org/annotation/VAR_026105|||http://purl.uniprot.org/annotation/VAR_036076|||http://purl.uniprot.org/annotation/VAR_043113|||http://purl.uniprot.org/annotation/VAR_043114|||http://purl.uniprot.org/annotation/VAR_051805|||http://purl.uniprot.org/annotation/VAR_065562|||http://purl.uniprot.org/annotation/VAR_065563|||http://purl.uniprot.org/annotation/VSP_046876|||http://purl.uniprot.org/annotation/VSP_046877|||http://purl.uniprot.org/annotation/VSP_046878
http://togogenome.org/gene/9606:OR4C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN0|||http://purl.uniprot.org/uniprot/Q8NH72                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150531|||http://purl.uniprot.org/annotation/VAR_034191
http://togogenome.org/gene/9606:OBI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0B1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of E3 ubiquitin transferase activity. No effect on association with ORC complex.|||ORC ubiquitin ligase 1|||Phosphoserine|||Polar residues|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055876
http://togogenome.org/gene/9606:ARFGEF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TH69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Brefeldin A-inhibited guanine nucleotide-exchange protein 3|||Disordered|||Helical|||Phosphoserine|||Polar residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286671|||http://purl.uniprot.org/annotation/VAR_032154|||http://purl.uniprot.org/annotation/VAR_032155|||http://purl.uniprot.org/annotation/VAR_032156|||http://purl.uniprot.org/annotation/VAR_051925
http://togogenome.org/gene/9606:RGPD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W705|||http://purl.uniprot.org/uniprot/O14715                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||Phosphoserine|||Phosphothreonine|||Polar residues|||RANBP2-like and GRIP domain-containing protein 8|||RanBD1 1|||RanBD1 2|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204917
http://togogenome.org/gene/9606:BCAR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTS3|||http://purl.uniprot.org/uniprot/B3KNL6|||http://purl.uniprot.org/uniprot/B3KP06|||http://purl.uniprot.org/uniprot/O75815                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with BCAR1 and SRC.|||Abolishes localization to focal adhesions. Reduces interaction with PTPRA.|||Breast cancer anti-estrogen resistance protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||Mediates the interaction with BCAR1/p130CAS|||N-acetylalanine|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Ras-GEF|||Removed|||Required for interaction with NEDD9|||SH2|||Weakens interaction with BCAR1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230284|||http://purl.uniprot.org/annotation/VAR_050689|||http://purl.uniprot.org/annotation/VAR_050690|||http://purl.uniprot.org/annotation/VSP_017814|||http://purl.uniprot.org/annotation/VSP_046716|||http://purl.uniprot.org/annotation/VSP_046717
http://togogenome.org/gene/9606:CYBC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQA9                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b-245 chaperone 1|||Helical|||In CGD5; loss of protein expression; decreased PMA-induced oxidative burst in neutrophils.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281418|||http://purl.uniprot.org/annotation/VAR_084696|||http://purl.uniprot.org/annotation/VSP_046335
http://togogenome.org/gene/9606:USO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60763                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Acidic residues|||Decreased association with Golgi membranes.|||Disordered|||General vesicular transport factor p115|||Globular head|||In isoform 2.|||Loss of phosphorylation. Promotes association with Golgi membranes.|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065774|||http://purl.uniprot.org/annotation/VSP_039120|||http://purl.uniprot.org/annotation/VSP_039121
http://togogenome.org/gene/9606:ARSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHX8|||http://purl.uniprot.org/uniprot/A0A804HJF6|||http://purl.uniprot.org/uniprot/A1L484|||http://purl.uniprot.org/uniprot/B7Z1M0|||http://purl.uniprot.org/uniprot/B7Z6V4|||http://purl.uniprot.org/uniprot/F5GYY5|||http://purl.uniprot.org/uniprot/F5H324|||http://purl.uniprot.org/uniprot/P51690                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase L|||Helical|||In CDPX1.|||In CDPX1; no effect on arylsulfatase activity, protein stability and localization to the Golgi apparatus.|||In CDPX1; significant loss of arylsulfatase activity; no effect on protein stability and localization to the Golgi apparatus.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033425|||http://purl.uniprot.org/annotation/PRO_5002636474|||http://purl.uniprot.org/annotation/PRO_5040028606|||http://purl.uniprot.org/annotation/VAR_007307|||http://purl.uniprot.org/annotation/VAR_007308|||http://purl.uniprot.org/annotation/VAR_007309|||http://purl.uniprot.org/annotation/VAR_007310|||http://purl.uniprot.org/annotation/VAR_007311|||http://purl.uniprot.org/annotation/VAR_007312|||http://purl.uniprot.org/annotation/VAR_023570|||http://purl.uniprot.org/annotation/VAR_023571|||http://purl.uniprot.org/annotation/VAR_023572|||http://purl.uniprot.org/annotation/VAR_037974|||http://purl.uniprot.org/annotation/VAR_037975
http://togogenome.org/gene/9606:MFSD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Abolishes export of sphingosine-1-phosphate.|||Disordered|||Does not affect export of sphingosine-1-phosphate.|||Helical|||Pro residues|||Sphingosine-1-phosphate transporter MFSD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341260
http://togogenome.org/gene/9606:UCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Uridine-cytidine kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164455|||http://purl.uniprot.org/annotation/VSP_014262
http://togogenome.org/gene/9606:FOXD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Fork-head|||Forkhead box protein D3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091817
http://togogenome.org/gene/9606:EXTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92935                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Exostosin-like 1|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149653|||http://purl.uniprot.org/annotation/VAR_012830|||http://purl.uniprot.org/annotation/VAR_049228
http://togogenome.org/gene/9606:TMEM19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HH6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284794|||http://purl.uniprot.org/annotation/VSP_024659|||http://purl.uniprot.org/annotation/VSP_024660
http://togogenome.org/gene/9606:CCDC93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q567U6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 93|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Sufficient for interaction with CCDC22|||Sufficient for interaction with WASHC2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234604|||http://purl.uniprot.org/annotation/VAR_035499|||http://purl.uniprot.org/annotation/VAR_054108|||http://purl.uniprot.org/annotation/VAR_054109|||http://purl.uniprot.org/annotation/VAR_054110|||http://purl.uniprot.org/annotation/VAR_054111
http://togogenome.org/gene/9606:ERP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30040|||http://purl.uniprot.org/uniprot/V9HW71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  ERp29 N-terminal|||Endoplasmic reticulum resident protein 29|||Endoplasmic reticulum resident protein 29 C-terminal|||In isoform 2.|||Phosphotyrosine; by PKDCC|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021197|||http://purl.uniprot.org/annotation/PRO_5014314727|||http://purl.uniprot.org/annotation/VSP_045680|||http://purl.uniprot.org/annotation/VSP_045681
http://togogenome.org/gene/9606:CCDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020862|||http://purl.uniprot.org/annotation/VSP_054551
http://togogenome.org/gene/9606:SUPT4H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63272                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Interaction with SUPT5H|||N-acetylalanine|||Removed|||Transcription elongation factor SPT4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210325
http://togogenome.org/gene/9606:POGLUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ97|||http://purl.uniprot.org/uniprot/Q8NBL1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Glycosyl transferase CAP10|||In DDD4.|||In LGMDR21; reduced glucosyltransferase and xylosyltransferase activities; impaired Notch signaling.|||Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates|||Loss of O-glucosyltransferase activity.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 1|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246685|||http://purl.uniprot.org/annotation/VAR_027041|||http://purl.uniprot.org/annotation/VAR_027042|||http://purl.uniprot.org/annotation/VAR_077954|||http://purl.uniprot.org/annotation/VAR_077955|||http://purl.uniprot.org/annotation/VAR_077956|||http://purl.uniprot.org/annotation/VAR_077957
http://togogenome.org/gene/9606:BEND5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5N0|||http://purl.uniprot.org/uniprot/Q7L4P6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BEN|||BEN domain-containing protein 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274279|||http://purl.uniprot.org/annotation/VSP_022695
http://togogenome.org/gene/9606:SFXN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4A7                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-acetylserine|||N6-acetyllysine|||Removed|||Sideroflexin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000177041|||http://purl.uniprot.org/annotation/VSP_014608|||http://purl.uniprot.org/annotation/VSP_014609|||http://purl.uniprot.org/annotation/VSP_014610
http://togogenome.org/gene/9606:METTL21A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JES0|||http://purl.uniprot.org/uniprot/Q8WXB1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Disordered|||In isoform 2.|||Protein N-lysine methyltransferase METTL21A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292033|||http://purl.uniprot.org/annotation/VAR_032935|||http://purl.uniprot.org/annotation/VSP_026379|||http://purl.uniprot.org/annotation/VSP_026380
http://togogenome.org/gene/9606:GALNT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNN1|||http://purl.uniprot.org/uniprot/Q9HCQ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 9|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059120|||http://purl.uniprot.org/annotation/VSP_011206
http://togogenome.org/gene/9606:PTCHD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW05                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 4|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320640|||http://purl.uniprot.org/annotation/VSP_056623|||http://purl.uniprot.org/annotation/VSP_056624|||http://purl.uniprot.org/annotation/VSP_056625|||http://purl.uniprot.org/annotation/VSP_058427|||http://purl.uniprot.org/annotation/VSP_058428
http://togogenome.org/gene/9606:PRRC2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X974|||http://purl.uniprot.org/uniprot/P48634                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2 X type B repeats|||2-1|||2-2|||3 X 50 AA type C repeats|||3-1|||3-2|||3-3|||4 X 57 AA type A repeats|||Asymmetric dimethylarginine|||BAT2 N-terminal|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein PRRC2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064829|||http://purl.uniprot.org/annotation/VAR_023215|||http://purl.uniprot.org/annotation/VAR_023216|||http://purl.uniprot.org/annotation/VAR_023217|||http://purl.uniprot.org/annotation/VAR_023218|||http://purl.uniprot.org/annotation/VAR_023219|||http://purl.uniprot.org/annotation/VAR_023220|||http://purl.uniprot.org/annotation/VAR_023221|||http://purl.uniprot.org/annotation/VAR_023222|||http://purl.uniprot.org/annotation/VAR_023223|||http://purl.uniprot.org/annotation/VAR_023224|||http://purl.uniprot.org/annotation/VAR_023225|||http://purl.uniprot.org/annotation/VAR_023226|||http://purl.uniprot.org/annotation/VAR_023227|||http://purl.uniprot.org/annotation/VAR_023228|||http://purl.uniprot.org/annotation/VAR_035796|||http://purl.uniprot.org/annotation/VAR_035797|||http://purl.uniprot.org/annotation/VAR_045992|||http://purl.uniprot.org/annotation/VAR_045993|||http://purl.uniprot.org/annotation/VAR_045994|||http://purl.uniprot.org/annotation/VAR_045995|||http://purl.uniprot.org/annotation/VAR_045996|||http://purl.uniprot.org/annotation/VAR_045997|||http://purl.uniprot.org/annotation/VAR_045998|||http://purl.uniprot.org/annotation/VAR_056742|||http://purl.uniprot.org/annotation/VSP_015099|||http://purl.uniprot.org/annotation/VSP_015100|||http://purl.uniprot.org/annotation/VSP_015101|||http://purl.uniprot.org/annotation/VSP_015102|||http://purl.uniprot.org/annotation/VSP_030865
http://togogenome.org/gene/9606:KRTAP4-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||26 X 5 AA repeats of C-C-[GRQVCHIEK]-[SPTR]-[VSTQYC]|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 4-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185173|||http://purl.uniprot.org/annotation/VAR_057648|||http://purl.uniprot.org/annotation/VAR_063826|||http://purl.uniprot.org/annotation/VAR_064560|||http://purl.uniprot.org/annotation/VAR_064561|||http://purl.uniprot.org/annotation/VAR_064562
http://togogenome.org/gene/9606:FETUB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PG08|||http://purl.uniprot.org/uniprot/Q5J875|||http://purl.uniprot.org/uniprot/Q9UGM5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cystatin fetuin-B-type|||Cystatin fetuin-B-type 1|||Cystatin fetuin-B-type 2|||Disordered|||Fetuin-B|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008899|||http://purl.uniprot.org/annotation/PRO_5003245178|||http://purl.uniprot.org/annotation/PRO_5004257817|||http://purl.uniprot.org/annotation/VAR_024449|||http://purl.uniprot.org/annotation/VAR_049061|||http://purl.uniprot.org/annotation/VAR_049062|||http://purl.uniprot.org/annotation/VSP_047135
http://togogenome.org/gene/9606:CEP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L269|||http://purl.uniprot.org/uniprot/I3L2N4|||http://purl.uniprot.org/uniprot/I3L4V2|||http://purl.uniprot.org/uniprot/I3NI25|||http://purl.uniprot.org/uniprot/Q96NB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein 20|||Disordered|||In isoform 2.|||LisH|||Loss of homooligomerization and loss of localization to centrosomes and pericentriolar satellites; when associated with A-49.|||Loss of homooligomerization and loss of localization to centrosomes and pericentriolar satellites; when associated with A-76.|||Loss of interaction with KIAA0753; when associated with A-76.|||Necessary and sufficient for homooligomerization and localization to centrosomes and pericentriolar satellites|||No effect on interaction with KIAA0753.|||Phosphoserine|||Strongly decreased interaction with KIAA0753; when associated with A-49. Loss of interaction with KIAA0753; when associated with Q-53.|||Strongly decreased interaction with KIAA0753; when associated with A-76.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264465|||http://purl.uniprot.org/annotation/VSP_056998
http://togogenome.org/gene/9606:TMEM150B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC51                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Modulator of macroautophagy TMEM150B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349284|||http://purl.uniprot.org/annotation/VAR_046343
http://togogenome.org/gene/9606:H6PD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95479                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  6-phosphogluconolactonase|||GDH/6PGL endoplasmic bifunctional protein|||Hexose-6-phosphate dehydrogenase|||In CORTRD1; loss of glucose-6-phosphate dehydrogenase activity.|||In CORTRD1; no effect on protein abundance; decreased glucose-6-phosphate dehydrogenase activity.|||In CORTRD1; unknown pathological significance; no effect on glucose-6-phosphate dehydrogenase activity; however an effect was originally observed.|||In isoform 2.|||Linker|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Proton acceptor|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010442|||http://purl.uniprot.org/annotation/VAR_026487|||http://purl.uniprot.org/annotation/VAR_049117|||http://purl.uniprot.org/annotation/VAR_049118|||http://purl.uniprot.org/annotation/VAR_049119|||http://purl.uniprot.org/annotation/VAR_049120|||http://purl.uniprot.org/annotation/VAR_069193|||http://purl.uniprot.org/annotation/VAR_083053|||http://purl.uniprot.org/annotation/VAR_083054|||http://purl.uniprot.org/annotation/VAR_083055|||http://purl.uniprot.org/annotation/VAR_083056|||http://purl.uniprot.org/annotation/VSP_060485
http://togogenome.org/gene/9606:KRTAP10-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60410                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||19 X 5 AA repeats of C-C-X(3)|||2|||3|||4|||5|||6|||7|||8|||9|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Keratin-associated protein 10-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185216|||http://purl.uniprot.org/annotation/VAR_028234|||http://purl.uniprot.org/annotation/VAR_036560|||http://purl.uniprot.org/annotation/VAR_036561
http://togogenome.org/gene/9606:FMNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DAD|||Disordered|||FH2|||Formin-like protein 2|||GBD/FH3|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289093|||http://purl.uniprot.org/annotation/VAR_032570|||http://purl.uniprot.org/annotation/VAR_032571|||http://purl.uniprot.org/annotation/VSP_025887
http://togogenome.org/gene/9606:DEFB119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GRG0|||http://purl.uniprot.org/uniprot/Q8N690                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 119|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006987|||http://purl.uniprot.org/annotation/PRO_5005143664|||http://purl.uniprot.org/annotation/VSP_029871|||http://purl.uniprot.org/annotation/VSP_043188
http://togogenome.org/gene/9606:OR4Q3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW32|||http://purl.uniprot.org/uniprot/Q8NH05                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4Q3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150567|||http://purl.uniprot.org/annotation/VAR_053176|||http://purl.uniprot.org/annotation/VAR_053177
http://togogenome.org/gene/9606:LACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV20                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Decreased acetylation; does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages.|||Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-52 and A-265.|||Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-52 and A-89.|||Does not affect ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages; when associated with A-89 and A-265.|||Impaired ability to promote pattern recognition receptor (PRR)-induced cytokines in macrophages.|||In JUVAR; reduced NOD2-induced signaling.|||In JUVAR; unknown pathological significance.|||May influence susceptibility to juvenile rheumatoid arthritis; increased adenosine deaminase activity and decreased adenosine phosphorylase activity; reduced ability to promote pattern recognition receptor (PRR)-induced cytokines; reduced NOD2-induced signaling; does not change interaction with FASN.|||N6-acetyllysine|||Purine nucleoside phosphorylase LACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163187|||http://purl.uniprot.org/annotation/VAR_052943|||http://purl.uniprot.org/annotation/VAR_073274|||http://purl.uniprot.org/annotation/VAR_083278|||http://purl.uniprot.org/annotation/VAR_083279
http://togogenome.org/gene/9606:OR2W1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVA1|||http://purl.uniprot.org/uniprot/Q9Y3N9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-15*02.|||In allele 6M1-15*03.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2W1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150511|||http://purl.uniprot.org/annotation/VAR_010953|||http://purl.uniprot.org/annotation/VAR_010954
http://togogenome.org/gene/9606:NIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XUU0|||http://purl.uniprot.org/uniprot/Q8N4C6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||Important for interaction with CEP170|||In SCKL7; does not disrupt protein expression or localization or affect mitotic functions in an obvious way.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 9.|||In isoform 6.|||In isoform 8.|||Ninein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096844|||http://purl.uniprot.org/annotation/VAR_019453|||http://purl.uniprot.org/annotation/VAR_019454|||http://purl.uniprot.org/annotation/VAR_019455|||http://purl.uniprot.org/annotation/VAR_051235|||http://purl.uniprot.org/annotation/VAR_051236|||http://purl.uniprot.org/annotation/VAR_069083|||http://purl.uniprot.org/annotation/VAR_069084|||http://purl.uniprot.org/annotation/VSP_010950|||http://purl.uniprot.org/annotation/VSP_010952|||http://purl.uniprot.org/annotation/VSP_010953|||http://purl.uniprot.org/annotation/VSP_010954|||http://purl.uniprot.org/annotation/VSP_010955|||http://purl.uniprot.org/annotation/VSP_010956|||http://purl.uniprot.org/annotation/VSP_010957|||http://purl.uniprot.org/annotation/VSP_010958|||http://purl.uniprot.org/annotation/VSP_010960|||http://purl.uniprot.org/annotation/VSP_040039
http://togogenome.org/gene/9606:NTRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04629|||http://purl.uniprot.org/uniprot/X5DR71                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with GGA3.|||Breakpoint for translocation to form TRK and TRK-T3|||Breakpoint for translocation to form TRK-T1|||Cytoplasmic|||DXXLL|||Extracellular|||Helical|||High affinity nerve growth factor receptor|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In CIPA.|||In CIPA; aberrantly processed; shows diminished autophosphorylation in neuronal cells.|||In CIPA; abolishes autophosphorylation.|||In CIPA; following transfection in neuroblastoma cells and NGF treatment, decreased percentage of cells differentiated into neuronal phenotype and reduced neurite length compared with wild-type; slightly decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal and NGF-induced autophosphorylation; small reduction in NGF-stimulated calcium flux.|||In CIPA; following transfection in neuroblastoma cells and NGF treatment, loss of differentiation into neuronal phenotype; partially decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux.|||In CIPA; following transfection in neuroblastoma cells and NGF treatment, small decrease in the percentage of cells differentiated into neuronal phenotype, but in differentiated cells, the average neurite length is comparable to wild-type; no effect on N-glycosylation, subcellular location, nor on basal and NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux.|||In CIPA; loss of function.|||In CIPA; loss of function; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells.|||In CIPA; loss of protein.|||In CIPA; might impair the function of the enzyme without compromising autophosphorylation.|||In CIPA; no effect on N-glycosylation, nor on subcellular location; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux.|||In CIPA; partially decreased N-glycosylation; reduced expression at the plasma membrane; reduced basal autophosphorylation and complete loss of NGF-induced autophosphorylation; loss of NGF-stimulated calcium flux.|||In CIPA; processed as wild-type but shows significantly diminished autophosphorylation in both neuronal and non-neuronal cells.|||In CIPA; unknown pathological significance; following transfection in neuroblastoma cells and NGF treatment, no effect on neurite outgrowth, nor neurite length; no effect on N-glycosylation, subcellular location, basal and NGF-induced autophosphorylation, nor on NGF-stimulated calcium flux.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 3.|||In isoform TrkA-I, isoform 3 and isoform TrkA-III.|||In isoform TrkA-III.|||Interaction with PLCG1|||Interaction with SHC1|||Interaction with SQSTM1|||LRR 1|||LRR 2|||LRRCT|||Loss of interaction with PLCG1 and altered phosphorylation of PLCG1. Altered neurite outgrowth and altered activation of the MAPK pathway; when associated with F-496.|||Loss of interaction with SHC1 and altered phosphorylation of SHC1. Altered neurite outgrowth and altered activation of the MAPK pathway; when associated with F-791.|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with GGA3.|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016724|||http://purl.uniprot.org/annotation/PRO_5004955970|||http://purl.uniprot.org/annotation/VAR_004103|||http://purl.uniprot.org/annotation/VAR_009623|||http://purl.uniprot.org/annotation/VAR_009624|||http://purl.uniprot.org/annotation/VAR_009625|||http://purl.uniprot.org/annotation/VAR_009626|||http://purl.uniprot.org/annotation/VAR_009627|||http://purl.uniprot.org/annotation/VAR_009628|||http://purl.uniprot.org/annotation/VAR_009629|||http://purl.uniprot.org/annotation/VAR_009630|||http://purl.uniprot.org/annotation/VAR_009631|||http://purl.uniprot.org/annotation/VAR_009632|||http://purl.uniprot.org/annotation/VAR_009633|||http://purl.uniprot.org/annotation/VAR_009634|||http://purl.uniprot.org/annotation/VAR_009635|||http://purl.uniprot.org/annotation/VAR_009636|||http://purl.uniprot.org/annotation/VAR_041461|||http://purl.uniprot.org/annotation/VAR_041462|||http://purl.uniprot.org/annotation/VAR_041463|||http://purl.uniprot.org/annotation/VAR_041464|||http://purl.uniprot.org/annotation/VAR_041465|||http://purl.uniprot.org/annotation/VAR_041466|||http://purl.uniprot.org/annotation/VAR_041467|||http://purl.uniprot.org/annotation/VAR_041468|||http://purl.uniprot.org/annotation/VAR_041469|||http://purl.uniprot.org/annotation/VAR_049714|||http://purl.uniprot.org/annotation/VAR_068480|||http://purl.uniprot.org/annotation/VAR_068481|||http://purl.uniprot.org/annotation/VAR_068482|||http://purl.uniprot.org/annotation/VAR_077472|||http://purl.uniprot.org/annotation/VAR_077473|||http://purl.uniprot.org/annotation/VAR_077474|||http://purl.uniprot.org/annotation/VAR_077475|||http://purl.uniprot.org/annotation/VAR_077476|||http://purl.uniprot.org/annotation/VAR_077477|||http://purl.uniprot.org/annotation/VAR_077478|||http://purl.uniprot.org/annotation/VAR_077479|||http://purl.uniprot.org/annotation/VAR_077480|||http://purl.uniprot.org/annotation/VAR_079399|||http://purl.uniprot.org/annotation/VAR_079400|||http://purl.uniprot.org/annotation/VAR_079401|||http://purl.uniprot.org/annotation/VAR_079402|||http://purl.uniprot.org/annotation/VAR_079403|||http://purl.uniprot.org/annotation/VAR_079404|||http://purl.uniprot.org/annotation/VAR_079405|||http://purl.uniprot.org/annotation/VAR_079406|||http://purl.uniprot.org/annotation/VSP_002899|||http://purl.uniprot.org/annotation/VSP_041905|||http://purl.uniprot.org/annotation/VSP_042152
http://togogenome.org/gene/9606:UGT2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTE5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000450721|||http://purl.uniprot.org/annotation/VSP_060686
http://togogenome.org/gene/9606:ASMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46597|||http://purl.uniprot.org/uniprot/X5D784                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acetylserotonin O-methyltransferase|||Acetylserotonin O-methyltransferase dimerisation|||Found in a patient with bipolar disorder; unknown pathological significance; reduced enzyme activity.|||Found in patients with neuropsychiatric disorders; unknown pathological significance; nearly abolishes enzyme activity.|||In isoform 2.|||In isoform 3.|||Nearly abolishes enzyme activity.|||No effect on enzyme activity.|||O-methyltransferase|||Proton acceptor|||Proton donor/acceptor|||Reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083982|||http://purl.uniprot.org/annotation/VAR_045991|||http://purl.uniprot.org/annotation/VAR_069111|||http://purl.uniprot.org/annotation/VAR_069112|||http://purl.uniprot.org/annotation/VAR_069114|||http://purl.uniprot.org/annotation/VAR_069115|||http://purl.uniprot.org/annotation/VAR_069116|||http://purl.uniprot.org/annotation/VAR_069117|||http://purl.uniprot.org/annotation/VAR_069118|||http://purl.uniprot.org/annotation/VAR_069119|||http://purl.uniprot.org/annotation/VAR_069120|||http://purl.uniprot.org/annotation/VAR_069121|||http://purl.uniprot.org/annotation/VAR_069122|||http://purl.uniprot.org/annotation/VAR_069123|||http://purl.uniprot.org/annotation/VAR_069125|||http://purl.uniprot.org/annotation/VAR_069126|||http://purl.uniprot.org/annotation/VAR_069127|||http://purl.uniprot.org/annotation/VAR_069128|||http://purl.uniprot.org/annotation/VAR_069129|||http://purl.uniprot.org/annotation/VAR_069130|||http://purl.uniprot.org/annotation/VAR_069131|||http://purl.uniprot.org/annotation/VAR_069132|||http://purl.uniprot.org/annotation/VSP_004284|||http://purl.uniprot.org/annotation/VSP_004285
http://togogenome.org/gene/9606:SLC28A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3L5|||http://purl.uniprot.org/uniprot/B7Z3L6|||http://purl.uniprot.org/uniprot/B7Z533|||http://purl.uniprot.org/uniprot/O00337                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Changed pyrimidine- and adenosine-specific:sodium symporter activity. Decreased specificity for pyrimidine nucleosides enabling also the transport of inosine. Loss of specificity for pyrimidine nucleosides; when associated with M-319 and T-352.|||Changed pyrimidine- and adenosine-specific:sodium symporter activity. Loss of specificity for pyrimidine nucleosides; when associated with G-318 and M-319.|||Changed pyrimidine- and adenosine-specific:sodium symporter activity. Loss of specificity for pyrimidine nucleosides; when associated with G-318 and T-352.|||Concentrative nucleoside transporter C-terminal|||Concentrative nucleoside transporter N-terminal|||Cytoplasmic|||Extracellular|||Helical|||In URCTU; changed N-glycosylation; increased protein degradation; affects urinary excretion of uridine and cytidine.|||In URCTU; no effect on localization to the cell membrane; loss of pyrimidine- and adenosine-specific:sodium symporter activity; affects urinary excretion of uridine and cytidine.|||In allele A.|||In allele B.|||In alleles B and C.|||In isoform 2.|||Loss of pyrimidine- and adenosine-specific:sodium symporter activity.|||N-linked (GlcNAc...) asparagine|||No effect on localization to the apical plasma membrane. Loss of pyrimidine- and adenosine-specific:sodium symporter activity. Probably due to sodium uncoupling in the nucleoside translocation cycle.|||Nucleoside transporter/FeoB GTPase Gate|||Sodium/nucleoside cotransporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070446|||http://purl.uniprot.org/annotation/VAR_009499|||http://purl.uniprot.org/annotation/VAR_009500|||http://purl.uniprot.org/annotation/VAR_009501|||http://purl.uniprot.org/annotation/VAR_009502|||http://purl.uniprot.org/annotation/VAR_009503|||http://purl.uniprot.org/annotation/VAR_057194|||http://purl.uniprot.org/annotation/VAR_057195|||http://purl.uniprot.org/annotation/VAR_057196|||http://purl.uniprot.org/annotation/VAR_061802|||http://purl.uniprot.org/annotation/VAR_082636|||http://purl.uniprot.org/annotation/VSP_037221|||http://purl.uniprot.org/annotation/VSP_037222
http://togogenome.org/gene/9606:ARHGEF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12774                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 5|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080916|||http://purl.uniprot.org/annotation/VSP_035175
http://togogenome.org/gene/9606:IREB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48200                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NDCAMA; may drastically decrease protein expression level.|||In isoform 2.|||Iron-responsive element-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076684|||http://purl.uniprot.org/annotation/VAR_058410|||http://purl.uniprot.org/annotation/VAR_082271|||http://purl.uniprot.org/annotation/VAR_082272|||http://purl.uniprot.org/annotation/VSP_056823|||http://purl.uniprot.org/annotation/VSP_056824
http://togogenome.org/gene/9606:ENAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased phosphorylation by FAM20C.|||Disordered|||Enamelin|||In AI1B and AI1C; decreased phosphorylation by FAM20C.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021174|||http://purl.uniprot.org/annotation/VAR_020105|||http://purl.uniprot.org/annotation/VAR_024311|||http://purl.uniprot.org/annotation/VAR_024312|||http://purl.uniprot.org/annotation/VAR_024313|||http://purl.uniprot.org/annotation/VAR_047076|||http://purl.uniprot.org/annotation/VAR_073665
http://togogenome.org/gene/9606:ZNF224                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZL3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 224                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047465|||http://purl.uniprot.org/annotation/VAR_021891|||http://purl.uniprot.org/annotation/VAR_024204|||http://purl.uniprot.org/annotation/VAR_047061|||http://purl.uniprot.org/annotation/VAR_047062|||http://purl.uniprot.org/annotation/VAR_047063|||http://purl.uniprot.org/annotation/VAR_061941
http://togogenome.org/gene/9606:TEX44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53QW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Testis-expressed protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309182|||http://purl.uniprot.org/annotation/VAR_036894|||http://purl.uniprot.org/annotation/VAR_036895|||http://purl.uniprot.org/annotation/VAR_036896|||http://purl.uniprot.org/annotation/VAR_036897
http://togogenome.org/gene/9606:SLC45A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2W3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In IDDNPF; no effect on protein abundance; decreased glucose transport activity.|||In IDDNPF; no effect on protein abundance; no effect on glucose transport activity.|||Phosphothreonine|||Pro residues|||Proton-associated sugar transporter A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122514|||http://purl.uniprot.org/annotation/VAR_079344|||http://purl.uniprot.org/annotation/VAR_079345|||http://purl.uniprot.org/annotation/VAR_079346
http://togogenome.org/gene/9606:CELA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08218|||http://purl.uniprot.org/uniprot/Q6ISP9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 2B|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027695|||http://purl.uniprot.org/annotation/PRO_0000027696|||http://purl.uniprot.org/annotation/PRO_5004274827|||http://purl.uniprot.org/annotation/VAR_044534|||http://purl.uniprot.org/annotation/VAR_044535|||http://purl.uniprot.org/annotation/VAR_044536|||http://purl.uniprot.org/annotation/VAR_044537
http://togogenome.org/gene/9606:CEP170                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SW79                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 170 kDa|||Disordered|||FHA|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with CCDC61|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Targeting to centrosomes|||Targeting to microtubules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282887|||http://purl.uniprot.org/annotation/VAR_031437|||http://purl.uniprot.org/annotation/VSP_024240|||http://purl.uniprot.org/annotation/VSP_024241|||http://purl.uniprot.org/annotation/VSP_024242
http://togogenome.org/gene/9606:RTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7F2|||http://purl.uniprot.org/uniprot/O75298|||http://purl.uniprot.org/uniprot/Q6GMT0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In SPG12.|||In isoform RTN2-B.|||In isoform RTN2-C.|||Phosphoserine|||Polar residues|||Reticulon|||Reticulon-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030351|||http://purl.uniprot.org/annotation/VAR_053632|||http://purl.uniprot.org/annotation/VAR_067562|||http://purl.uniprot.org/annotation/VSP_005649|||http://purl.uniprot.org/annotation/VSP_018870
http://togogenome.org/gene/9606:LIPM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYY2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||In isoform 2.|||Lipase member M|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286829|||http://purl.uniprot.org/annotation/VAR_032191|||http://purl.uniprot.org/annotation/VAR_059382|||http://purl.uniprot.org/annotation/VSP_056261
http://togogenome.org/gene/9606:SPG21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZD8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AB hydrolase-1|||Abolishes interaction with CD4.|||In isoform 2.|||Maspardin|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227980|||http://purl.uniprot.org/annotation/VSP_041512
http://togogenome.org/gene/9606:PWWP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with HDAC1 and MTA1|||Interaction with the H2A.Z/H2AZ1|||Loss of interaction with H3K36me3.|||No effect on interaction with H3K36me3.|||PWWP|||PWWP domain-containing protein 2A|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311363|||http://purl.uniprot.org/annotation/VSP_029547|||http://purl.uniprot.org/annotation/VSP_029548|||http://purl.uniprot.org/annotation/VSP_054064|||http://purl.uniprot.org/annotation/VSP_054065
http://togogenome.org/gene/9606:DCUN1D5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP84|||http://purl.uniprot.org/uniprot/Q9BTE7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Affects nucleus localization.|||DCN1-like protein 5|||DCUN1|||Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and R-219. Does not affect localization at nucleus; when associated with A-195 and R-219.|||Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with R-219 and A-225. Does not affect localization at nucleus; when associated with R-219 and A-225.|||Loss of interaction with RBX1, CUL1 and CAND1.|||Loss of interaction with RBX1, CUL1 and CAND1. Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and A-225. Does not affect localization at nucleus; when associated with A-195 and A-225.|||Loss of interaction with RBX1, CUL1, CUL2, CUL3 and CAND1. Does not affect interaction with UBE2M and NEDD8. Fails to augment Cul3 neddylation beyond basal levels.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254171
http://togogenome.org/gene/9606:VPS39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JC1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  CHCR|||CNH|||In isoform 2.|||Vam6/Vps39-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065901|||http://purl.uniprot.org/annotation/VSP_004075
http://togogenome.org/gene/9606:FUT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q11130                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-(1,3)-fucosyltransferase 7|||Cytoplasmic|||Found in patients with ulcerative colitis; loss of alpha-(1,3)-fucosyltransferase activity.|||Helical; Signal-anchor for type II membrane protein|||Impairs glycosylation. Impairs glycosylation; when associated with Q-291. Does not affect SELP and SELL binding on SELPLG. Does not affect SELP and SELL binding on SELPLG; when associated with Q-291. Abolishes alpha-(1,3)-fucosyltransferase activity. Abolishes alpha-(1,3)-fucosyltransferase activity; when associated with Q-291. Fails to synthetises sLe(x) antigens or to generate SELE binding. Fails to synthetises sLe(x) antigens or to generate SELE binding; when associated with Q-291. Does not affect sLe(x) antigens synthesis or SELE binding only in presence of SELPLG and GCNT1; when associated with Q-291.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Slightly affects glycosylation. Impairs glycosylation; when associated with Q-81. Does not affect SELP and SELL binding on SELPLG. Does not affect SELP and SELL binding on SELPLG; when associated with Q-81. Abolishes alpha-(1,3)-fucosyltransferase activity. Abolishes alpha-(1,3)-fucosyltransferase activity; when associated with Q-81. Fails to synthetises sLe(x) antigens or to generate SELE binding. Fails to synthetises sLe(x) antigens or to generate SELE binding; when associated with Q-81. Does not affect sLe(x) antigens synthesis or SELE binding only in presence of SELPLG and GCNT1; when associated with Q-81.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221113|||http://purl.uniprot.org/annotation/VAR_079131
http://togogenome.org/gene/9606:CLASRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQS2|||http://purl.uniprot.org/uniprot/Q8N2M8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||CLK4-associating serine/arginine rich protein|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Suppressor of white apricot N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081945|||http://purl.uniprot.org/annotation/VAR_016809|||http://purl.uniprot.org/annotation/VAR_035490|||http://purl.uniprot.org/annotation/VSP_013894|||http://purl.uniprot.org/annotation/VSP_013895|||http://purl.uniprot.org/annotation/VSP_055717
http://togogenome.org/gene/9606:NAPEPLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ20                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost no change in activity.|||Disordered|||Impairs binding to bile acids resulting in loss of activity.|||Impairs homodimerization resulting in loss of activity; when associated with S-158.|||Impairs homodimerization resulting in loss of activity; when associated with S-159.|||Loss of activity.|||N-acetylmethionine|||N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318159|||http://purl.uniprot.org/annotation/VAR_038694|||http://purl.uniprot.org/annotation/VAR_038695
http://togogenome.org/gene/9606:ZNF513                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8E2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In RP58; cannot bind to promoters of retinal-specific genes.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Zinc finger protein 513                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047632|||http://purl.uniprot.org/annotation/VAR_064926|||http://purl.uniprot.org/annotation/VSP_035624|||http://purl.uniprot.org/annotation/VSP_035625
http://togogenome.org/gene/9606:DCX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K340|||http://purl.uniprot.org/uniprot/O43602                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||In LISX1 and SBHX.|||In LISX1 and SBHX; decreased tubulin binding.|||In LISX1.|||In SBH.|||In SBHX.|||In SBHX; mild.|||In epilepsy; resistant partial seizures; related to 'cryptogenic' epilepsy.|||In isoform 2.|||Neuronal migration protein doublecortin|||Phosphoserine; by CDK5|||Phosphoserine; by CK2|||Phosphoserine; by CK2, MARK1 and PKA|||Phosphoserine; by DYRK2|||Phosphoserine; by MAPK|||Phosphoserine; by MARK1 and PKA|||Phosphoserine; by PKC|||Phosphothreonine; by CDK5|||Phosphothreonine; by MAPK|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and MAPK|||Phosphotyrosine; by ABL|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079833|||http://purl.uniprot.org/annotation/VAR_007819|||http://purl.uniprot.org/annotation/VAR_007820|||http://purl.uniprot.org/annotation/VAR_007821|||http://purl.uniprot.org/annotation/VAR_007822|||http://purl.uniprot.org/annotation/VAR_007823|||http://purl.uniprot.org/annotation/VAR_007824|||http://purl.uniprot.org/annotation/VAR_007825|||http://purl.uniprot.org/annotation/VAR_007826|||http://purl.uniprot.org/annotation/VAR_007827|||http://purl.uniprot.org/annotation/VAR_007828|||http://purl.uniprot.org/annotation/VAR_007829|||http://purl.uniprot.org/annotation/VAR_007830|||http://purl.uniprot.org/annotation/VAR_007831|||http://purl.uniprot.org/annotation/VAR_007832|||http://purl.uniprot.org/annotation/VAR_007833|||http://purl.uniprot.org/annotation/VAR_007834|||http://purl.uniprot.org/annotation/VAR_007835|||http://purl.uniprot.org/annotation/VAR_007836|||http://purl.uniprot.org/annotation/VAR_007837|||http://purl.uniprot.org/annotation/VAR_007838|||http://purl.uniprot.org/annotation/VAR_007839|||http://purl.uniprot.org/annotation/VAR_007840|||http://purl.uniprot.org/annotation/VAR_007841|||http://purl.uniprot.org/annotation/VAR_007842|||http://purl.uniprot.org/annotation/VAR_010202|||http://purl.uniprot.org/annotation/VAR_010536|||http://purl.uniprot.org/annotation/VAR_026022|||http://purl.uniprot.org/annotation/VAR_026023|||http://purl.uniprot.org/annotation/VAR_026024|||http://purl.uniprot.org/annotation/VAR_026025|||http://purl.uniprot.org/annotation/VAR_026026|||http://purl.uniprot.org/annotation/VAR_026027|||http://purl.uniprot.org/annotation/VAR_026028|||http://purl.uniprot.org/annotation/VAR_026029|||http://purl.uniprot.org/annotation/VAR_026030|||http://purl.uniprot.org/annotation/VAR_026031|||http://purl.uniprot.org/annotation/VAR_026032|||http://purl.uniprot.org/annotation/VAR_026033|||http://purl.uniprot.org/annotation/VAR_026034|||http://purl.uniprot.org/annotation/VAR_026035|||http://purl.uniprot.org/annotation/VAR_026036|||http://purl.uniprot.org/annotation/VAR_026037|||http://purl.uniprot.org/annotation/VAR_026038|||http://purl.uniprot.org/annotation/VAR_077482|||http://purl.uniprot.org/annotation/VSP_058155
http://togogenome.org/gene/9606:RNF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBP0|||http://purl.uniprot.org/uniprot/Q8N5U6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity and ability to monoubiquitinate RPS2/us5 and RPS3/us3.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF10|||In isoform 2.|||Interaction with MEOX2|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259585|||http://purl.uniprot.org/annotation/VAR_028967|||http://purl.uniprot.org/annotation/VAR_028968|||http://purl.uniprot.org/annotation/VSP_021478
http://togogenome.org/gene/9606:H2AC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FTV9|||http://purl.uniprot.org/uniprot/P0C0S8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055235
http://togogenome.org/gene/9606:OR11H6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP4|||http://purl.uniprot.org/uniprot/Q8NGC7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11H6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150726|||http://purl.uniprot.org/annotation/VAR_024130|||http://purl.uniprot.org/annotation/VAR_034299|||http://purl.uniprot.org/annotation/VAR_034300|||http://purl.uniprot.org/annotation/VAR_034301|||http://purl.uniprot.org/annotation/VAR_034302|||http://purl.uniprot.org/annotation/VAR_034303|||http://purl.uniprot.org/annotation/VAR_034304
http://togogenome.org/gene/9606:PCDHB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5E2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003926|||http://purl.uniprot.org/annotation/VAR_020367|||http://purl.uniprot.org/annotation/VAR_033708|||http://purl.uniprot.org/annotation/VAR_033709|||http://purl.uniprot.org/annotation/VAR_059183|||http://purl.uniprot.org/annotation/VAR_059184|||http://purl.uniprot.org/annotation/VAR_059185
http://togogenome.org/gene/9606:ZNF708                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17019                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Phosphoserine|||Zinc finger protein 708                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047706|||http://purl.uniprot.org/annotation/VAR_054795|||http://purl.uniprot.org/annotation/VAR_054796|||http://purl.uniprot.org/annotation/VAR_054797|||http://purl.uniprot.org/annotation/VAR_054798
http://togogenome.org/gene/9606:CBX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5B2|||http://purl.uniprot.org/uniprot/O00257                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with YWHAZ and YWHAE; impairs interaction with PCGF6 and BMI1; no effect on interaction with RNF2.|||Basic and acidic residues|||Basic residues|||Chromo|||Disordered|||E3 SUMO-protein ligase CBX4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Interaction with BMI1|||Interaction with RNF2|||Involved in interaction with H3C15 and H3C1|||Involved in interaction with H3C15 and RNF2|||N6-acetyllysine; alternate|||No effect on ZNF131 sumoylation.|||Phosphoserine|||Phosphothreonine; by HIPK2|||Polar residues|||Reduced interaction with H3C15, H3C1 and RNF2.|||Small decrease in ZNF131 sumoylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080206|||http://purl.uniprot.org/annotation/VSP_041599
http://togogenome.org/gene/9606:TATDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SGD3|||http://purl.uniprot.org/uniprot/Q6P1N9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Deoxyribonuclease TATDN1|||In isoform 2.|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313590|||http://purl.uniprot.org/annotation/VSP_030045
http://togogenome.org/gene/9606:SCGB3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L6B3|||http://purl.uniprot.org/uniprot/Q96PL1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Interchain|||Secretoglobin family 3A member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036381|||http://purl.uniprot.org/annotation/PRO_5014308668|||http://purl.uniprot.org/annotation/VAR_036185
http://togogenome.org/gene/9606:CTNND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJU1|||http://purl.uniprot.org/uniprot/B4DRK2|||http://purl.uniprot.org/uniprot/E7EPC8|||http://purl.uniprot.org/uniprot/Q9UQB3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Catenin delta-2|||Disordered|||Found in patients with autism; unknown pathological significance; has no effect on Wnt signaling.|||Has no effect on Wnt signaling.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Probable disease-associated variant found in autism; hypomorphic variant affecting Wnt signaling.|||Probable disease-associated variant found in autism; hypomorphic variant affecting dendritic spines development and maintenance; results in reduced interaction with CTNNB1.|||Probable disease-associated variant found in autism; loss-of-function variant affecting dendritic spines development and maintenance; results in reduced interaction with CTNNB1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064299|||http://purl.uniprot.org/annotation/VAR_036162|||http://purl.uniprot.org/annotation/VAR_062270|||http://purl.uniprot.org/annotation/VAR_062271|||http://purl.uniprot.org/annotation/VAR_062272|||http://purl.uniprot.org/annotation/VAR_073387|||http://purl.uniprot.org/annotation/VAR_073388|||http://purl.uniprot.org/annotation/VAR_073389|||http://purl.uniprot.org/annotation/VAR_073390|||http://purl.uniprot.org/annotation/VAR_073391|||http://purl.uniprot.org/annotation/VAR_073392|||http://purl.uniprot.org/annotation/VAR_073393|||http://purl.uniprot.org/annotation/VAR_073394|||http://purl.uniprot.org/annotation/VAR_073395|||http://purl.uniprot.org/annotation/VSP_006746
http://togogenome.org/gene/9606:ATP6V1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36543                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In ARCL2C.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphotyrosine|||Removed|||V-type proton ATPase subunit E 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117295|||http://purl.uniprot.org/annotation/VAR_036565|||http://purl.uniprot.org/annotation/VAR_078604|||http://purl.uniprot.org/annotation/VAR_078605|||http://purl.uniprot.org/annotation/VSP_042925|||http://purl.uniprot.org/annotation/VSP_044589
http://togogenome.org/gene/9606:KRT16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08779                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Mass|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mass|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In FNEPPK1 and PC1.|||In PC1.|||In PC1; late onset.|||In PC1; requires 2 nucleotide substitutions.|||Keratin, type I cytoskeletal 16|||Linker 1|||Linker 12|||Rare variant; found as somatic mutation in a patient with localized epidermolytic hyperkeratosis in the right palm and the right sole; unknown pathological significance.|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063662|||http://purl.uniprot.org/annotation/VAR_003846|||http://purl.uniprot.org/annotation/VAR_009183|||http://purl.uniprot.org/annotation/VAR_009184|||http://purl.uniprot.org/annotation/VAR_012854|||http://purl.uniprot.org/annotation/VAR_012855|||http://purl.uniprot.org/annotation/VAR_012856|||http://purl.uniprot.org/annotation/VAR_013837|||http://purl.uniprot.org/annotation/VAR_017065|||http://purl.uniprot.org/annotation/VAR_017066|||http://purl.uniprot.org/annotation/VAR_017067|||http://purl.uniprot.org/annotation/VAR_035440|||http://purl.uniprot.org/annotation/VAR_072436|||http://purl.uniprot.org/annotation/VAR_072437|||http://purl.uniprot.org/annotation/VAR_072438|||http://purl.uniprot.org/annotation/VAR_072439|||http://purl.uniprot.org/annotation/VAR_072440
http://togogenome.org/gene/9606:NDUFAF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L592                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||Loss of function.|||Mitochondrion|||Probable disease-associated variant found in patients with pathologic myopia; may decrease mitochondrial complex I activity; decreases the production of ATP; decreases reactive oxygen species production.|||Protein arginine methyltransferase NDUFAF7, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315672|||http://purl.uniprot.org/annotation/VAR_038274|||http://purl.uniprot.org/annotation/VAR_079608|||http://purl.uniprot.org/annotation/VSP_030606|||http://purl.uniprot.org/annotation/VSP_030607
http://togogenome.org/gene/9606:LYRM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MSI8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  LYR motif-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345398
http://togogenome.org/gene/9606:GINS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5L0|||http://purl.uniprot.org/uniprot/A0A0S2Z5L4|||http://purl.uniprot.org/uniprot/A0A0S2Z5P2|||http://purl.uniprot.org/uniprot/Q9BRX5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Mass|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mass|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA replication complex GINS protein PSF3|||GINS subunit|||In isoform 2.|||In isoform 3.|||Not essential for folding and stability of GINS complex, but may regulate accessibility to the central complex pore|||This is the measured mass for the GINS complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327615|||http://purl.uniprot.org/annotation/VSP_032737|||http://purl.uniprot.org/annotation/VSP_046694
http://togogenome.org/gene/9606:TOR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JU69|||http://purl.uniprot.org/uniprot/Q8N2E6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Lysine amide|||N-linked (GlcNAc...) asparagine|||Prosalusin|||Salusin-alpha|||Salusin-beta|||Torsin-2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228825|||http://purl.uniprot.org/annotation/PRO_0000228826|||http://purl.uniprot.org/annotation/PRO_0000228827|||http://purl.uniprot.org/annotation/PRO_0000228828|||http://purl.uniprot.org/annotation/PRO_0000228829|||http://purl.uniprot.org/annotation/VAR_055661|||http://purl.uniprot.org/annotation/VSP_017703|||http://purl.uniprot.org/annotation/VSP_017704|||http://purl.uniprot.org/annotation/VSP_035631|||http://purl.uniprot.org/annotation/VSP_035632
http://togogenome.org/gene/9606:SLC35C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6R4|||http://purl.uniprot.org/uniprot/Q9NQQ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 35 member C2|||Sugar phosphate transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213399|||http://purl.uniprot.org/annotation/VSP_009229|||http://purl.uniprot.org/annotation/VSP_056729
http://togogenome.org/gene/9606:PHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2T1|||http://purl.uniprot.org/uniprot/E7EX82|||http://purl.uniprot.org/uniprot/Q8NDX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HD1|||In isoform 2.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 3|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076290|||http://purl.uniprot.org/annotation/VSP_016763|||http://purl.uniprot.org/annotation/VSP_016764|||http://purl.uniprot.org/annotation/VSP_016765|||http://purl.uniprot.org/annotation/VSP_016766|||http://purl.uniprot.org/annotation/VSP_016767|||http://purl.uniprot.org/annotation/VSP_016768|||http://purl.uniprot.org/annotation/VSP_016769|||http://purl.uniprot.org/annotation/VSP_016770|||http://purl.uniprot.org/annotation/VSP_016771
http://togogenome.org/gene/9606:MARCHF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0T0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Almost complete loss of ebolavirus restriction.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase MARCHF8|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||RING-CH-type|||Strong loss of catalytic activity; when associated with S-80, S-123 and S-126.|||Strong loss of catalytic activity; when associated with S-80, S-83 and S-123.|||Strong loss of catalytic activity; when associated with S-80, S-83 and S-126.|||Strong loss of catalytic activity; when associated with S-83, S-123 and S-126.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274370|||http://purl.uniprot.org/annotation/VAR_030266|||http://purl.uniprot.org/annotation/VAR_030267|||http://purl.uniprot.org/annotation/VSP_055697
http://togogenome.org/gene/9606:SIX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95475|||http://purl.uniprot.org/uniprot/Q6P051                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with bilateral asymmetric microphthalmia, cataract and nystagmus; unknown pathological significance.|||Homeobox|||Homeobox protein SIX6|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049307|||http://purl.uniprot.org/annotation/VAR_026241|||http://purl.uniprot.org/annotation/VAR_031631
http://togogenome.org/gene/9606:C11orf16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ32                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Uncharacterized protein C11orf16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089832|||http://purl.uniprot.org/annotation/VAR_056827|||http://purl.uniprot.org/annotation/VAR_056828|||http://purl.uniprot.org/annotation/VSP_039850
http://togogenome.org/gene/9606:SCN7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01118                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine; by PKA|||Polar residues|||Pore-forming|||Sodium channel protein type 7 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048499|||http://purl.uniprot.org/annotation/VAR_024410|||http://purl.uniprot.org/annotation/VAR_055641|||http://purl.uniprot.org/annotation/VAR_055642|||http://purl.uniprot.org/annotation/VAR_055643|||http://purl.uniprot.org/annotation/VAR_055644|||http://purl.uniprot.org/annotation/VAR_055645|||http://purl.uniprot.org/annotation/VAR_063120|||http://purl.uniprot.org/annotation/VAR_063121
http://togogenome.org/gene/9606:SEC61B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60468                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes S-acylation.|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylproline|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein transport protein Sec61 subunit beta|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157254
http://togogenome.org/gene/9606:C3orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H4A9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Uncharacterized membrane protein C3orf80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413691
http://togogenome.org/gene/9606:STMN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ72                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||S-palmitoyl cysteine|||SLD|||Stathmin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182402|||http://purl.uniprot.org/annotation/VSP_056525
http://togogenome.org/gene/9606:CCDC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4L8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 24|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233666|||http://purl.uniprot.org/annotation/VSP_018148
http://togogenome.org/gene/9606:HNRNPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14866|||http://purl.uniprot.org/uniprot/Q6NTA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-fold increase in RNA-binding affinity.|||15-fold decrease in RNA-binding affinity; when associated with A-174.|||4-fold increase in RNA-binding affinity.|||6-fold decrease in RNA-binding affinity.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein L|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CaMK4|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||Significant decrease in RNA-binding affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081862|||http://purl.uniprot.org/annotation/VSP_044301
http://togogenome.org/gene/9606:DNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51530                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes ability to resect DNA in present of BLM.|||Abolishes ability to unwind DNA, while it does not affect ability to resect DNA.|||DNA replication ATP-dependent helicase/nuclease DNA2|||Helicase activity|||In PEOA6; the mutant protein has a complete loss of nuclease activity and severely impaired helicase activity; consistent with a loss of function mutation.|||In PEOA6; the mutant protein has decreased nuclease activity (30% of wild-type) and enhanced helicase activity; consistent with a loss of function mutation.|||In PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclease activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080712|||http://purl.uniprot.org/annotation/VAR_069905|||http://purl.uniprot.org/annotation/VAR_069906|||http://purl.uniprot.org/annotation/VAR_069907|||http://purl.uniprot.org/annotation/VSP_021869|||http://purl.uniprot.org/annotation/VSP_021870|||http://purl.uniprot.org/annotation/VSP_021871|||http://purl.uniprot.org/annotation/VSP_044185
http://togogenome.org/gene/9606:FABP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07148|||http://purl.uniprot.org/uniprot/Q05CP7|||http://purl.uniprot.org/uniprot/Q6FGL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, liver|||Increases the binding for cholesterol; increases high density lipoprotein (HDL)- and low density lipoprotein (LDL)-mediated cholesterol uptake.|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067334|||http://purl.uniprot.org/annotation/VAR_014662|||http://purl.uniprot.org/annotation/VAR_022093
http://togogenome.org/gene/9606:SMIM21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSN8|||http://purl.uniprot.org/uniprot/Q3B7S5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340722
http://togogenome.org/gene/9606:R3HCC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384DVK4|||http://purl.uniprot.org/uniprot/A8K931|||http://purl.uniprot.org/uniprot/Q4KMT0|||http://purl.uniprot.org/uniprot/Q4KMY3|||http://purl.uniprot.org/uniprot/Q7Z5L2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein R3HCC1L|||Disordered|||EJC-binding motif; may mediate interaction with the EJC|||In isoform 2.|||In isoform 3.|||Loss of interaction with the EJC.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087487|||http://purl.uniprot.org/annotation/VAR_023092|||http://purl.uniprot.org/annotation/VAR_023093|||http://purl.uniprot.org/annotation/VAR_056898|||http://purl.uniprot.org/annotation/VAR_056899|||http://purl.uniprot.org/annotation/VAR_056900|||http://purl.uniprot.org/annotation/VAR_056901|||http://purl.uniprot.org/annotation/VAR_061652|||http://purl.uniprot.org/annotation/VSP_014919|||http://purl.uniprot.org/annotation/VSP_014920|||http://purl.uniprot.org/annotation/VSP_014921
http://togogenome.org/gene/9606:H2BC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58876|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-C/E/F/G/I|||Histone H2B type 1-D|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/PRO_0000071827|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:GBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0R5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 3|||In isoform 2.|||Promotes ubiquitination and degradation by S. flexneri IpaH9.8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261159|||http://purl.uniprot.org/annotation/VAR_029082|||http://purl.uniprot.org/annotation/VAR_029083|||http://purl.uniprot.org/annotation/VAR_029084|||http://purl.uniprot.org/annotation/VAR_054136|||http://purl.uniprot.org/annotation/VAR_054137|||http://purl.uniprot.org/annotation/VAR_054138|||http://purl.uniprot.org/annotation/VSP_044360|||http://purl.uniprot.org/annotation/VSP_044361
http://togogenome.org/gene/9606:KDM4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QZ60|||http://purl.uniprot.org/uniprot/Q9H3R0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes lysine-specific histone demethylase activity.|||C2HC pre-PHD-type|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||JmjC|||JmjN|||Lysine-specific demethylase 4C|||PHD-type 1|||PHD-type 2|||Polar residues|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183177|||http://purl.uniprot.org/annotation/VAR_020340|||http://purl.uniprot.org/annotation/VAR_024681|||http://purl.uniprot.org/annotation/VAR_024682|||http://purl.uniprot.org/annotation/VAR_049660|||http://purl.uniprot.org/annotation/VAR_049661|||http://purl.uniprot.org/annotation/VAR_049662|||http://purl.uniprot.org/annotation/VAR_049663|||http://purl.uniprot.org/annotation/VSP_018311|||http://purl.uniprot.org/annotation/VSP_045462|||http://purl.uniprot.org/annotation/VSP_045463|||http://purl.uniprot.org/annotation/VSP_046113
http://togogenome.org/gene/9606:FADS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95864                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-CoA 6-desaturase|||Cytochrome b5 heme-binding|||Cytoplasmic|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307101|||http://purl.uniprot.org/annotation/VSP_028568|||http://purl.uniprot.org/annotation/VSP_028569|||http://purl.uniprot.org/annotation/VSP_054809
http://togogenome.org/gene/9606:PLPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43688                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Loss of lipid phosphatase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phospholipid phosphatase 2|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220909|||http://purl.uniprot.org/annotation/VAR_061541|||http://purl.uniprot.org/annotation/VSP_037765|||http://purl.uniprot.org/annotation/VSP_047366
http://togogenome.org/gene/9606:CLEC16A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2KHT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FPL|||In isoform 2.|||In isoform 3.|||Polar residues|||Protein CLEC16A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274476|||http://purl.uniprot.org/annotation/VAR_030288|||http://purl.uniprot.org/annotation/VSP_022745|||http://purl.uniprot.org/annotation/VSP_022746|||http://purl.uniprot.org/annotation/VSP_022747|||http://purl.uniprot.org/annotation/VSP_022748|||http://purl.uniprot.org/annotation/VSP_022749|||http://purl.uniprot.org/annotation/VSP_022750
http://togogenome.org/gene/9606:RNF113A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15541                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Cells are hypersensitive to DNA damage by alkylating agents.|||Disordered|||E3 ubiquitin-protein ligase RNF113A|||Important for interaction with CXCR4|||Important for interaction with SNRNP200/BRR2|||Loss of E3 ubiquitin ligase activity.|||N-acetylalanine|||Phosphoserine|||RING-type|||Removed|||Strongly decreased interaction with CXCR4. Abolishes the ability to promote CXCR4 degradation.|||Strongly decreased interaction with SNRNP200/BRR2.|||Strongly reduced E3 ubiquitin ligase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056087
http://togogenome.org/gene/9606:RSPRY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||Disordered|||In SEMDFA.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||RING finger and SPRY domain-containing protein 1|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278786|||http://purl.uniprot.org/annotation/VAR_075873|||http://purl.uniprot.org/annotation/VSP_023382|||http://purl.uniprot.org/annotation/VSP_023383
http://togogenome.org/gene/9606:UBE2Z                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H832                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||In isoform 2.|||Phosphoserine|||UBC core|||Ubiquitin-conjugating enzyme E2 Z                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280515|||http://purl.uniprot.org/annotation/VSP_023747
http://togogenome.org/gene/9606:ACADSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3P9|||http://purl.uniprot.org/uniprot/P45954                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Decreased acyl-CoA dehydrogenase activity.|||In SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity.|||In isoform 2.|||Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.|||Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000519|||http://purl.uniprot.org/annotation/VAR_013010|||http://purl.uniprot.org/annotation/VAR_014749|||http://purl.uniprot.org/annotation/VAR_048177|||http://purl.uniprot.org/annotation/VAR_048178|||http://purl.uniprot.org/annotation/VAR_048179|||http://purl.uniprot.org/annotation/VSP_055778
http://togogenome.org/gene/9606:OR5M10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEU7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150608|||http://purl.uniprot.org/annotation/VAR_053201|||http://purl.uniprot.org/annotation/VAR_053202
http://togogenome.org/gene/9606:YEATS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULM3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to histone H3 crotonylated at 'Lys-27' (H3K27cr).|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone H3K27cr binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced binding to histone H3 crotonylated at 'Lys-27' (H3K27cr).|||Strongly reduced binding to histone H3 crotonylated at 'Lys-27' (H3K27cr).|||YEATS|||YEATS domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076366|||http://purl.uniprot.org/annotation/VAR_051494|||http://purl.uniprot.org/annotation/VAR_051495|||http://purl.uniprot.org/annotation/VAR_051496
http://togogenome.org/gene/9606:CD33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20138|||http://purl.uniprot.org/uniprot/Q546G0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to PTPN6 and PTPN11. Increases binding of red blood cells.|||Complete loss of phosphorylation by LCK.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 3.|||In isoform CD33m.|||More than 50% loss of phosphorylation by LCK.|||Myeloid cell surface antigen CD33|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by LCK|||Polar residues|||Reduces binding to PTPN6.|||Significant loss of binding to peripheral blood granulocytes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014878|||http://purl.uniprot.org/annotation/PRO_5014309577|||http://purl.uniprot.org/annotation/VAR_028260|||http://purl.uniprot.org/annotation/VAR_028261|||http://purl.uniprot.org/annotation/VAR_028262|||http://purl.uniprot.org/annotation/VAR_028263|||http://purl.uniprot.org/annotation/VAR_028264|||http://purl.uniprot.org/annotation/VAR_049904|||http://purl.uniprot.org/annotation/VAR_049905|||http://purl.uniprot.org/annotation/VAR_049906|||http://purl.uniprot.org/annotation/VAR_049907|||http://purl.uniprot.org/annotation/VAR_049908|||http://purl.uniprot.org/annotation/VAR_061319|||http://purl.uniprot.org/annotation/VSP_045364|||http://purl.uniprot.org/annotation/VSP_046172
http://togogenome.org/gene/9606:DCTD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32321                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||Deoxycytidylate deaminase|||In isoform 2.|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171691|||http://purl.uniprot.org/annotation/VSP_038094
http://togogenome.org/gene/9606:STRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43815                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Caveolin-binding|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Striatin|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051232|||http://purl.uniprot.org/annotation/VSP_023495|||http://purl.uniprot.org/annotation/VSP_023496
http://togogenome.org/gene/9606:PDF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBH1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Hydrophobic dimerization interface|||Mitochondrion|||Peptide deformylase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006729|||http://purl.uniprot.org/annotation/VAR_060122
http://togogenome.org/gene/9606:PDE1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z226|||http://purl.uniprot.org/uniprot/B7Z7A2|||http://purl.uniprot.org/uniprot/P54750|||http://purl.uniprot.org/uniprot/Q9Y633                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A|||In isoform 2, isoform 6 and isoform 7.|||In isoform 3, isoform 8 and isoform 9.|||In isoform 4, isoform 6 and isoform 8.|||In isoform 5, isoform 7 and isoform 9.|||PDEase|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198785|||http://purl.uniprot.org/annotation/VSP_004547|||http://purl.uniprot.org/annotation/VSP_004548|||http://purl.uniprot.org/annotation/VSP_004549|||http://purl.uniprot.org/annotation/VSP_004550
http://togogenome.org/gene/9606:TBC1D3I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXS9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431606
http://togogenome.org/gene/9606:MCTP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4G1|||http://purl.uniprot.org/uniprot/Q6DN14                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||C2 3|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Multiple C2 and transmembrane domain-containing protein 1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294471|||http://purl.uniprot.org/annotation/VAR_033189|||http://purl.uniprot.org/annotation/VSP_026655|||http://purl.uniprot.org/annotation/VSP_026656|||http://purl.uniprot.org/annotation/VSP_026657|||http://purl.uniprot.org/annotation/VSP_026658|||http://purl.uniprot.org/annotation/VSP_026659|||http://purl.uniprot.org/annotation/VSP_026660|||http://purl.uniprot.org/annotation/VSP_026661
http://togogenome.org/gene/9606:COQ7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99807                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  1|||2|||2 X approximate tandem repeats|||5-demethoxyubiquinone hydroxylase, mitochondrial|||In COQ10D8.|||In isoform 2.|||Mitochondrion|||Reduces nuclear localization. Increases level of reactive oxygen species (ROS).|||Required for nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079251|||http://purl.uniprot.org/annotation/VAR_055148|||http://purl.uniprot.org/annotation/VAR_076370|||http://purl.uniprot.org/annotation/VSP_039068
http://togogenome.org/gene/9606:NKD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969F2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates myristoylation and membrane association and impairs delivery of TGFA to the cell surface.|||Basic and acidic residues|||Disordered|||EF-hand|||In isoform 2.|||Interaction with DVL1, DVL2 and DVL3|||Interaction with TGFA|||N-myristoyl glycine|||Pro residues|||Protein naked cuticle homolog 2|||Removed|||Targeting to the basolateral cell membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301993|||http://purl.uniprot.org/annotation/VAR_034934|||http://purl.uniprot.org/annotation/VSP_027900|||http://purl.uniprot.org/annotation/VSP_027901
http://togogenome.org/gene/9606:KGD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82909                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Alpha-ketoglutarate dehydrogenase component 4|||Disordered|||N-acetylmethionine|||N6-succinyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087733
http://togogenome.org/gene/9606:PLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUH9|||http://purl.uniprot.org/uniprot/Q9NYY3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Impairs localization to the centrosome and centriole duplication; when associated with A-629 and M-631.|||Impairs localization to the centrosome and centriole duplication; when associated with F-503 and A-631.|||Impairs localization to the centrosome and centriole duplication; when associated with F-503 and M-631.|||In a lung adenocarcinoma sample; somatic mutation.|||In an ovarian Endometrioid carcinoma sample; somatic mutation.|||Loss of kinase activity.|||POLO box|||POLO box 1|||POLO box 2|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086561|||http://purl.uniprot.org/annotation/VAR_041023|||http://purl.uniprot.org/annotation/VAR_041024|||http://purl.uniprot.org/annotation/VAR_041025|||http://purl.uniprot.org/annotation/VAR_041026
http://togogenome.org/gene/9606:MICU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes homooligomerization.|||Abolishes interaction with EMRE/SMDT1 while maintaining interaction with MICU2SO.|||Abolishes interchain disulfide bond and heterodimer formation with MICU2.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-242 and A-421.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-242 and A-432.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-231; A-421 and A-432.|||Abolishes mitochondrial Ca(2+) uptake; when associated with A-242; A-421 and A-432.|||C-helix region|||Calcium uptake protein 1, mitochondrial|||Disordered|||EF-hand 1|||EF-hand 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Interchain (with C-413 in MICU2)|||Loss of function; when associated with A-421.|||Mitochondrial intermembrane|||Mitochondrion|||Polybasic region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322990|||http://purl.uniprot.org/annotation/VSP_031979|||http://purl.uniprot.org/annotation/VSP_031980|||http://purl.uniprot.org/annotation/VSP_031981|||http://purl.uniprot.org/annotation/VSP_039890|||http://purl.uniprot.org/annotation/VSP_039891|||http://purl.uniprot.org/annotation/VSP_039892
http://togogenome.org/gene/9606:TET2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158SIU0|||http://purl.uniprot.org/uniprot/Q6N021                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In IMD75; loss of methylcytosine dioxygenase activity.|||In IMD75; loss of protein expression; loss of methylcytosine dioxygenase activity.|||In a chronic myelomonocytic leukemia sample.|||In a chronic myelomonocytic leukemia sample; somatic mutation.|||In a myelodysplastic syndrome.|||In a myelodysplastic syndrome; somatic mutation in a chronic myelomonocytic leukemia sample.|||In a myelodysplastic syndrome; somatic mutation.|||In a myelodysplastic syndrome; somatic mutation; loss of 5-methylcytosine demethylase activity in vivo; no effect on interaction with DCAF1, nor on monoubiquitination, when tested in a heterologous system.|||In a myelodysplatic/myeloproliferative disorder and a chronic myelomonocytic leukemia sample.|||In a myeloproliferative disorder; somatic mutation.|||In a myeloproliferative disorder; somatic mutation; also in a patient with systemic mastocytosis associated with chronic myelomonocytic leukemia.|||In a polycythemia vera sample; somatic mutation.|||In a primary acute myeloid leukemia sample; somatic mutation; reduces enzyme activity.|||In a refractory anemia sample; loss of monoubiquitination, chromatin binding and 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||In a refractory anemia with excess blasts sample.|||In a refractory anemia with ringed sideroblasts sample.|||In a secondary acute myeloid leukemia sample; somatic mutation; loss of enzyme activity.|||In an acute myeloid leukemia sample; somatic mutation.|||In an essential thrombocythemia sample.|||In chronic myelomonocytic leukemia and acute myeloid leukemia samples.|||In chronic myelomonocytic leukemia samples; loss of monoubiquitination, chromatin binding and 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||In chronic myelomonocytic leukemia samples; no effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||In isoform 2.|||In isoform 3.|||In myelodysplastic syndromes, myeloproliferative disorders and chronic myelomonocytic leukemia; somatic mutation in acute myeloid leukemia and chronic myelomonocytic leukemia samples.|||In myelodysplastic syndromes; refractory cytopenia with multilineage dysplasia and ringed sideroblasts; somatic mutation in a patient.|||In myelodysplastic/myeloproliferative disorders.|||In myelodysplastic/myeloproliferative disorders; a patient positive for mutation F-617 in JAK2.|||In myelodysplastic/myeloproliferative disorders; no effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||In myeloproliferative disorders.|||In primary myelofibrosis and chronic myelomonocytic leukemia samples; loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||In refractory anemia with ringed sideroblasts; somatic mutation in an acute myeloid leukemia sample.|||Interaction with DNA|||Loss of enzyme activity.|||Loss of enzyme activity. Still able to enhance histone H2BGlcNAcylation by OGT; when associated with A-1384. Loss of enzyme activity; when associated with V-1384.|||Loss of enzyme activity. Still able to enhance histone H2BGlcNAcylation by OGT; when associated with Y-1382.|||Loss of enzyme activity; when associated with E-1299.|||Loss of enzyme activity; when associated with Y-1382.|||Loss of interaction with DCAF1, monoubiquitination and of 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||Loss of monoubiquitination and of 5-methylcytosine demethylase activity in vivo. No effect on interaction with DCAF1, when tested in a heterologous system.|||Methylcytosine dioxygenase TET1-3 oxygenase|||Methylcytosine dioxygenase TET2|||Near loss of enzyme activity.|||No effect on interaction with DCAF1, monoubiquitination, nor on 5-methylcytosine demethylase activity in vivo, when tested in a heterologous system.|||Phosphoserine|||Polar residues|||Pro residues|||Reduces enzyme activity; when associated with A-1290.|||Reduces enzyme activity; when associated with A-1295.|||Requires 2 nucleotide substitutions.|||Slightly reduces enzyme activity.|||Strongly reduced enzyme activity. Slightly decreased affinity for DNA. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324588|||http://purl.uniprot.org/annotation/VAR_039841|||http://purl.uniprot.org/annotation/VAR_039842|||http://purl.uniprot.org/annotation/VAR_039843|||http://purl.uniprot.org/annotation/VAR_039844|||http://purl.uniprot.org/annotation/VAR_058130|||http://purl.uniprot.org/annotation/VAR_058131|||http://purl.uniprot.org/annotation/VAR_058132|||http://purl.uniprot.org/annotation/VAR_058133|||http://purl.uniprot.org/annotation/VAR_058134|||http://purl.uniprot.org/annotation/VAR_058135|||http://purl.uniprot.org/annotation/VAR_058136|||http://purl.uniprot.org/annotation/VAR_058137|||http://purl.uniprot.org/annotation/VAR_058138|||http://purl.uniprot.org/annotation/VAR_058139|||http://purl.uniprot.org/annotation/VAR_058140|||http://purl.uniprot.org/annotation/VAR_058141|||http://purl.uniprot.org/annotation/VAR_058142|||http://purl.uniprot.org/annotation/VAR_058143|||http://purl.uniprot.org/annotation/VAR_058144|||http://purl.uniprot.org/annotation/VAR_058145|||http://purl.uniprot.org/annotation/VAR_058146|||http://purl.uniprot.org/annotation/VAR_058147|||http://purl.uniprot.org/annotation/VAR_058148|||http://purl.uniprot.org/annotation/VAR_058149|||http://purl.uniprot.org/annotation/VAR_058150|||http://purl.uniprot.org/annotation/VAR_058151|||http://purl.uniprot.org/annotation/VAR_058152|||http://purl.uniprot.org/annotation/VAR_058153|||http://purl.uniprot.org/annotation/VAR_058154|||http://purl.uniprot.org/annotation/VAR_058155|||http://purl.uniprot.org/annotation/VAR_058156|||http://purl.uniprot.org/annotation/VAR_058157|||http://purl.uniprot.org/annotation/VAR_058158|||http://purl.uniprot.org/annotation/VAR_058159|||http://purl.uniprot.org/annotation/VAR_058160|||http://purl.uniprot.org/annotation/VAR_058161|||http://purl.uniprot.org/annotation/VAR_058162|||http://purl.uniprot.org/annotation/VAR_058163|||http://purl.uniprot.org/annotation/VAR_058164|||http://purl.uniprot.org/annotation/VAR_058165|||http://purl.uniprot.org/annotation/VAR_058166|||http://purl.uniprot.org/annotation/VAR_058167|||http://purl.uniprot.org/annotation/VAR_058168|||http://purl.uniprot.org/annotation/VAR_058169|||http://purl.uniprot.org/annotation/VAR_058170|||http://purl.uniprot.org/annotation/VAR_058171|||http://purl.uniprot.org/annotation/VAR_058172|||http://purl.uniprot.org/annotation/VAR_058173|||http://purl.uniprot.org/annotation/VAR_058174|||http://purl.uniprot.org/annotation/VAR_058175|||http://purl.uniprot.org/annotation/VAR_058176|||http://purl.uniprot.org/annotation/VAR_058177|||http://purl.uniprot.org/annotation/VAR_058178|||http://purl.uniprot.org/annotation/VAR_058179|||http://purl.uniprot.org/annotation/VAR_058180|||http://purl.uniprot.org/annotation/VAR_058181|||http://purl.uniprot.org/annotation/VAR_058182|||http://purl.uniprot.org/annotation/VAR_058183|||http://purl.uniprot.org/annotation/VAR_058184|||http://purl.uniprot.org/annotation/VAR_058185|||http://purl.uniprot.org/annotation/VAR_058186|||http://purl.uniprot.org/annotation/VAR_058187|||http://purl.uniprot.org/annotation/VAR_058188|||http://purl.uniprot.org/annotation/VAR_058189|||http://purl.uniprot.org/annotation/VAR_058190|||http://purl.uniprot.org/annotation/VAR_058191|||http://purl.uniprot.org/annotation/VAR_058192|||http://purl.uniprot.org/annotation/VAR_058193|||http://purl.uniprot.org/annotation/VAR_058194|||http://purl.uniprot.org/annotation/VAR_058195|||http://purl.uniprot.org/annotation/VAR_058196|||http://purl.uniprot.org/annotation/VAR_058197|||http://purl.uniprot.org/annotation/VAR_058198|||http://purl.uniprot.org/annotation/VAR_085544|||http://purl.uniprot.org/annotation/VAR_085545|||http://purl.uniprot.org/annotation/VSP_032282|||http://purl.uniprot.org/annotation/VSP_032283|||http://purl.uniprot.org/annotation/VSP_032284|||http://purl.uniprot.org/annotation/VSP_032285
http://togogenome.org/gene/9606:TBRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3YBR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FYR C-terminal|||FYR N-terminal|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Removed|||Transforming growth factor beta regulator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274218|||http://purl.uniprot.org/annotation/VSP_022644|||http://purl.uniprot.org/annotation/VSP_022645
http://togogenome.org/gene/9606:COQ8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI60                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  AAAS motif|||Abolishes binding ADP or ATP.|||Atypical kinase COQ8A, mitochondrial|||Disordered|||Does not affect selectivity for binding ADP or ATP.|||Does not affect selectivity for binding ADP or ATP. Impaired multi-subunit COQ enzyme complex.|||Does not impair homodimerization.|||Enables autophosphorylation but inhibits coenzyme Q biosynthesis in vivo.|||Helical|||Impaired binding ADP or ATP.|||Impaired homodimerization.|||In COQ10D4.|||In COQ10D4; decreased stability.|||In COQ10D4; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KxGQ motif|||Mitochondrion|||Protein kinase|||Proton acceptor|||Slightly affects selectivity for binding ADP or ATP.|||Slightly impaired homodimerization.|||Strongly impairs binding ADP or ATP. Impaired multi-subunit COQ enzyme complex.|||Strongly impairs homodimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000262|||http://purl.uniprot.org/annotation/VAR_020319|||http://purl.uniprot.org/annotation/VAR_044402|||http://purl.uniprot.org/annotation/VAR_044403|||http://purl.uniprot.org/annotation/VAR_044404|||http://purl.uniprot.org/annotation/VAR_044405|||http://purl.uniprot.org/annotation/VAR_044406|||http://purl.uniprot.org/annotation/VAR_044407|||http://purl.uniprot.org/annotation/VAR_044408|||http://purl.uniprot.org/annotation/VAR_045576|||http://purl.uniprot.org/annotation/VAR_072622|||http://purl.uniprot.org/annotation/VAR_072623|||http://purl.uniprot.org/annotation/VAR_072624|||http://purl.uniprot.org/annotation/VAR_072625|||http://purl.uniprot.org/annotation/VAR_072626|||http://purl.uniprot.org/annotation/VAR_072627|||http://purl.uniprot.org/annotation/VAR_076860|||http://purl.uniprot.org/annotation/VSP_022351|||http://purl.uniprot.org/annotation/VSP_022352|||http://purl.uniprot.org/annotation/VSP_022353
http://togogenome.org/gene/9606:TPM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P67936                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Tropomyosin alpha-4 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205635|||http://purl.uniprot.org/annotation/VAR_036535|||http://purl.uniprot.org/annotation/VSP_006611
http://togogenome.org/gene/9606:RTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYW3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Retrotransposon Gag-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259629|||http://purl.uniprot.org/annotation/VAR_051319
http://togogenome.org/gene/9606:AGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKV8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||4-hydroxyproline|||Abrogates RNA cleavage but does not affect binding to siRNA or translational repression.|||Abrogates RNA cleavage but does not affect binding to siRNA.|||Abrogates RNA cleavage.|||Abrogates RNA cleavage. Binds siRNA.|||Disordered|||Impairs RNA cleavage.|||In LESKRES.|||In LESKRES; complete loss of function. Changes in the subcellular location pattern. Diffuse location into the cytoplasm. Does not bind mRNA. Abolishes interaction with DICER1. Abolishes phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387.|||In LESKRES; impairs shRNA-mediated silencing. Decreased phosphorylation of the C-terminal serine cluster. Increased binding to mRNA targets.|||In LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of a C-terminal serine cluster. Does not affect phosphorylation of Ser-387.|||In LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Decreased phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387.|||In LESKRES; impairs shRNA-mediated silencing. Does not affect targeting to P-bodies. Increases binding to mRNA targets. Does not affect interaction with DICER1. Does not affect phosphorylation of the C-terminal serine cluster. Does not affect phosphorylation of Ser-387.|||In isoform 2.|||Interaction with GW182 family members|||Interaction with guide RNA|||No effect on RNA cleavage.|||No effect on binding to the 7-methylguanosine cap of mRNA or inhibition of translation.|||No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation and abolishes interaction with TNRC6C; when associated with V-470.|||No effect on miRNA-binding or target mRNA cleavage. Abrogates binding to the 7-methylguanosine cap of mRNA and prevents inhibition of translation. Abolishes interaction with TNRC6C; when associated with V-505.|||No effect.|||PAZ|||Phosphoserine|||Piwi|||Pro residues|||Protein argonaute-2|||Reduced protein stability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194057|||http://purl.uniprot.org/annotation/VAR_085417|||http://purl.uniprot.org/annotation/VAR_085418|||http://purl.uniprot.org/annotation/VAR_085419|||http://purl.uniprot.org/annotation/VAR_085420|||http://purl.uniprot.org/annotation/VAR_085421|||http://purl.uniprot.org/annotation/VAR_085422|||http://purl.uniprot.org/annotation/VAR_085423|||http://purl.uniprot.org/annotation/VAR_085424|||http://purl.uniprot.org/annotation/VAR_085425|||http://purl.uniprot.org/annotation/VAR_085426|||http://purl.uniprot.org/annotation/VAR_085427|||http://purl.uniprot.org/annotation/VSP_037001
http://togogenome.org/gene/9606:CBLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDV7|||http://purl.uniprot.org/uniprot/Q75N03                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||E3 ubiquitin-protein ligase Hakai|||HYB domain|||Hakai C2H2 zinc finger|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284048|||http://purl.uniprot.org/annotation/VSP_054879
http://togogenome.org/gene/9606:IRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35568                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not affect IRS1 stability.|||GRB2-binding|||IRS-type PTB|||Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-527 and A-636.|||Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-527 and A-639.|||Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-636 and A-639.|||Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-527; A-636 and A-639.|||Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-312; A-527; A-636 and A-639.|||In T2D.|||Induces IRS1 degradation.|||Insulin receptor substrate 1|||Loss of phosphorylation by SIK2.|||May contribute to insulin resistance by impairing metabolic signaling through PI3K-dependent pathways.|||Mediates interaction with PHIP|||PH|||Phosphoserine|||Phosphoserine; by AMPK and SIK2|||Phosphoserine; by CK2|||Phosphoserine; by IKKB, MAPK8 and RPS6KB1|||Phosphoserine; by RPS6KB1|||Phosphoserine; by RPS6KB1 and PKC/PRKCQ|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by INSR|||Polar residues|||Pro residues|||YXXM motif 1|||YXXM motif 2|||YXXM motif 3|||YXXM motif 4|||YXXM motif 5|||YXXM motif 6|||YXXM motif 7|||YXXM motif 8|||YXXM motif 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084236|||http://purl.uniprot.org/annotation/VAR_005299|||http://purl.uniprot.org/annotation/VAR_005300|||http://purl.uniprot.org/annotation/VAR_005301|||http://purl.uniprot.org/annotation/VAR_005302|||http://purl.uniprot.org/annotation/VAR_005303|||http://purl.uniprot.org/annotation/VAR_014853|||http://purl.uniprot.org/annotation/VAR_014854|||http://purl.uniprot.org/annotation/VAR_014855|||http://purl.uniprot.org/annotation/VAR_014856|||http://purl.uniprot.org/annotation/VAR_021837|||http://purl.uniprot.org/annotation/VAR_025320
http://togogenome.org/gene/9606:SPANXA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS26                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Sperm protein associated with the nucleus on the X chromosome A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189549
http://togogenome.org/gene/9606:GPAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UL3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Glycerol-3-phosphate acyltransferase 4|||HXXXXD motif|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024703
http://togogenome.org/gene/9606:SEPTIN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5ME97|||http://purl.uniprot.org/uniprot/B7Z277|||http://purl.uniprot.org/uniprot/B7Z371|||http://purl.uniprot.org/uniprot/E7EW69|||http://purl.uniprot.org/uniprot/Q59H84|||http://purl.uniprot.org/uniprot/Q9H9P7|||http://purl.uniprot.org/uniprot/Q9P0V9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  G1 motif|||G3 motif|||G4 motif|||In isoform 2.|||In isoform 3.|||Septin-10|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173538|||http://purl.uniprot.org/annotation/VAR_051936|||http://purl.uniprot.org/annotation/VSP_014091|||http://purl.uniprot.org/annotation/VSP_041479
http://togogenome.org/gene/9606:IFT52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y366                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In SRTD16.|||Intraflagellar transport protein 52 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084167|||http://purl.uniprot.org/annotation/VAR_077805
http://togogenome.org/gene/9606:SEMG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  2 X 60 AA tandem repeats, type 1|||2-1|||2-2|||3-1|||3-2|||Abrogates binding to EPPIN and do not inhibit spem motility.|||Alpha-inhibin-31|||Alpha-inhibin-92|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with EPPIN|||Interchain|||Less common genetic variant.|||Polar residues|||Pyrrolidone carboxylic acid|||Repeat-rich region|||Semenogelin-1|||Seminal basic protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032351|||http://purl.uniprot.org/annotation/PRO_0000032352|||http://purl.uniprot.org/annotation/PRO_0000032353|||http://purl.uniprot.org/annotation/PRO_0000032354|||http://purl.uniprot.org/annotation/VAR_005610|||http://purl.uniprot.org/annotation/VAR_022679|||http://purl.uniprot.org/annotation/VAR_053650|||http://purl.uniprot.org/annotation/VAR_053651|||http://purl.uniprot.org/annotation/VSP_004385
http://togogenome.org/gene/9606:PCDHB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LNH7|||http://purl.uniprot.org/uniprot/B4DSB6|||http://purl.uniprot.org/uniprot/Q9Y5E3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003924|||http://purl.uniprot.org/annotation/VAR_021879|||http://purl.uniprot.org/annotation/VAR_033705|||http://purl.uniprot.org/annotation/VAR_033706|||http://purl.uniprot.org/annotation/VAR_033707|||http://purl.uniprot.org/annotation/VAR_070665|||http://purl.uniprot.org/annotation/VAR_070666
http://togogenome.org/gene/9606:PDZK1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13113                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||PDZK1-interacting protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058282
http://togogenome.org/gene/9606:DNAJC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99543                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 2|||DnaJ homolog subfamily C member 2, N-terminally processed|||Epitope (recognized by CD8(+) cytotoxic T-lymphocytes)|||In isoform 2.|||J|||Loss of function.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Removed; alternate|||SANT 1|||SANT 2|||ZRF1-UBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071123|||http://purl.uniprot.org/annotation/PRO_0000425752|||http://purl.uniprot.org/annotation/VSP_023562
http://togogenome.org/gene/9606:KCTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14681|||http://purl.uniprot.org/uniprot/Q8IYY2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD2|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191287
http://togogenome.org/gene/9606:SMO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99835                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CRJS; constitutive activation of the smoothened signaling pathway.|||In basal cell carcinoma and ameloblastoma samples; somatic mutation; constitutive activation of the smoothened signaling pathway.|||In basal cell carcinoma samples; somatic mutation.|||Interaction with BBS5 and BBS7|||Interaction with DLG5|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein smoothened|||Required for interaction with PRKACA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013015|||http://purl.uniprot.org/annotation/VAR_007848|||http://purl.uniprot.org/annotation/VAR_007849|||http://purl.uniprot.org/annotation/VAR_037891|||http://purl.uniprot.org/annotation/VAR_077087
http://togogenome.org/gene/9606:CFAP53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M91                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 53|||In HTX6; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089407|||http://purl.uniprot.org/annotation/VAR_050746|||http://purl.uniprot.org/annotation/VAR_050747|||http://purl.uniprot.org/annotation/VAR_077590
http://togogenome.org/gene/9606:PPP1R13L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUF5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RelA-associated inhibitor|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066966
http://togogenome.org/gene/9606:AGAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 5|||Basic and acidic residues|||C4-type; degenerate|||Disordered|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349205
http://togogenome.org/gene/9606:GLS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C201|||http://purl.uniprot.org/uniprot/O94925|||http://purl.uniprot.org/uniprot/Q68D38                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Cleavage; by MPP|||Decreased enzyme activity.|||Disordered|||Glutaminase EF-hand|||Glutaminase kidney isoform, mitochondrial 65 kDa chain|||Glutaminase kidney isoform, mitochondrial 68 kDa chain|||Highly mobile activation loop|||In CASGID; increased enzyme activity.|||In DEE71.|||In GDPAG; loss of enzyme activity.|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||No effect on catalytic activity. Loss of inhibition by BPTES.|||No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.|||No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011622|||http://purl.uniprot.org/annotation/PRO_0000447412|||http://purl.uniprot.org/annotation/VAR_049188|||http://purl.uniprot.org/annotation/VAR_081971|||http://purl.uniprot.org/annotation/VAR_081972|||http://purl.uniprot.org/annotation/VAR_081973|||http://purl.uniprot.org/annotation/VAR_081974|||http://purl.uniprot.org/annotation/VSP_001765|||http://purl.uniprot.org/annotation/VSP_001766|||http://purl.uniprot.org/annotation/VSP_001767
http://togogenome.org/gene/9606:FAM162B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6X4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Protein FAM162B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254639|||http://purl.uniprot.org/annotation/VAR_053782
http://togogenome.org/gene/9606:UQCRQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14949                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 8|||Helical|||In MC3DN4.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193544|||http://purl.uniprot.org/annotation/VAR_045911
http://togogenome.org/gene/9606:TSHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01222                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CHNG4.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Thyrotropin subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011746|||http://purl.uniprot.org/annotation/PRO_0000011747|||http://purl.uniprot.org/annotation/VAR_054769|||http://purl.uniprot.org/annotation/VAR_087375|||http://purl.uniprot.org/annotation/VAR_087376|||http://purl.uniprot.org/annotation/VSP_053387
http://togogenome.org/gene/9606:FBXO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK22                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Acidic residues|||Disordered|||F-box|||F-box only protein 2|||FBA|||Important for carbohydrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119875|||http://purl.uniprot.org/annotation/VAR_049036
http://togogenome.org/gene/9606:CCDC89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N998                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 89|||Disordered|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271024
http://togogenome.org/gene/9606:ZNF563                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TA94                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 563                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047653|||http://purl.uniprot.org/annotation/VSP_016381|||http://purl.uniprot.org/annotation/VSP_016382
http://togogenome.org/gene/9606:PFN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35080                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform IIb.|||N-acetylalanine|||Profilin-2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199575|||http://purl.uniprot.org/annotation/VSP_005217
http://togogenome.org/gene/9606:ZNF324                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75467                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Nuclear localization signal|||Zinc finger protein 324A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047533
http://togogenome.org/gene/9606:RCAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R612|||http://purl.uniprot.org/uniprot/Q14206                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calcipressin-2|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211417|||http://purl.uniprot.org/annotation/VSP_026923
http://togogenome.org/gene/9606:P2RY13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPV8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070040|||http://purl.uniprot.org/annotation/VAR_028299|||http://purl.uniprot.org/annotation/VSP_036226
http://togogenome.org/gene/9606:NSUN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE18                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleophile|||Polar residues|||Putative methyltransferase NSUN7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289238|||http://purl.uniprot.org/annotation/VAR_032610|||http://purl.uniprot.org/annotation/VAR_059790|||http://purl.uniprot.org/annotation/VSP_025976|||http://purl.uniprot.org/annotation/VSP_025977|||http://purl.uniprot.org/annotation/VSP_025978|||http://purl.uniprot.org/annotation/VSP_025979
http://togogenome.org/gene/9606:MED13L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71F56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MRFACD.|||In MRFACD; unknown pathological significance.|||In a patient with dextro-looped transposition of the great arteries; unknown pathological significance.|||LXXLL motif 1|||LXXLL motif 2|||Leucine-zipper|||Mediator of RNA polymerase II transcription subunit 13-like|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076352|||http://purl.uniprot.org/annotation/VAR_024024|||http://purl.uniprot.org/annotation/VAR_024025|||http://purl.uniprot.org/annotation/VAR_024026|||http://purl.uniprot.org/annotation/VAR_076332
http://togogenome.org/gene/9606:COX7B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF08                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7B2, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006161|||http://purl.uniprot.org/annotation/VAR_026231
http://togogenome.org/gene/9606:CP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PL27|||http://purl.uniprot.org/uniprot/P00450                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Ceruloplasmin|||F5/8 type A 1|||F5/8 type A 2|||F5/8 type A 3|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Plastocyanin-like|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||Reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease.|||Retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease.|||type 1 copper site|||type 2 copper site|||type 3 copper site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002912|||http://purl.uniprot.org/annotation/PRO_5014296989|||http://purl.uniprot.org/annotation/VAR_025655|||http://purl.uniprot.org/annotation/VAR_025656|||http://purl.uniprot.org/annotation/VAR_025657|||http://purl.uniprot.org/annotation/VAR_025658|||http://purl.uniprot.org/annotation/VAR_025659|||http://purl.uniprot.org/annotation/VAR_025660|||http://purl.uniprot.org/annotation/VAR_032815
http://togogenome.org/gene/9606:TST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKQ2|||http://purl.uniprot.org/uniprot/Q16762                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteine persulfide intermediate|||Hinge|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine|||Removed|||Rhodanese|||Rhodanese 1|||Rhodanese 2|||Thiosulfate sulfurtransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139395|||http://purl.uniprot.org/annotation/VAR_051799|||http://purl.uniprot.org/annotation/VAR_051800
http://togogenome.org/gene/9606:ANLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5D9|||http://purl.uniprot.org/uniprot/Q9NQW6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates interaction with CD2AP.|||Abrogates ubiquitin-mediated proteolysis; when associated with A-41.|||Abrogates ubiquitin-mediated proteolysis; when associated with A-44.|||Anillin|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In FSGS8.|||In FSGS8; results in decreased interaction with CD2AP.|||In isoform 2.|||Interaction with CD2AP|||Interaction with F-actin|||Localization to the cleavage furrow|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for ubiquitination                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227965|||http://purl.uniprot.org/annotation/VAR_025661|||http://purl.uniprot.org/annotation/VAR_025662|||http://purl.uniprot.org/annotation/VAR_072418|||http://purl.uniprot.org/annotation/VAR_072419|||http://purl.uniprot.org/annotation/VSP_017617
http://togogenome.org/gene/9606:MKKS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Has a modifier effect on BBS; causes a mislocalization of the protein; fails to associate with centrosome.|||In BBS6.|||In BBS6; atypical mild phenotype consisting of retinitis pigmentosa and polydactyly without other signs of Bardet-Biedl syndrome; results in decreased interaction with BBS12.|||In BBS6; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Tyr-84 mutant; localizes properly to the centrosome.|||In BBS6; fails to associate with centrosome.|||In BBS6; found in a patient also carrying A-155 in TMEM237; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Y-84 mutant; greatly reduces the ability to interact with BBS12.|||In BBS6; increases MKKS protein degradation; fails to associate with centrosome; the mutant is highly polyubiquitinated and rapidly degraded by the ubiquitin-proteasome protein degradation pathway.|||In BBS6; increases MKKS protein degradation; localizes properly to the centrosome.|||In BBS6; moderately affects interaction with BBS2; greatly reduces the ability to interact with BBS12.|||In BBS6; unknown pathological significance.|||In MKKS and BBS6; associated with Y-84 in MKKS; unknown pathological significance; increases MKKS protein degradation; no effect on ciliogenesis; disrupts import to the nucleus; no effect on interaction with SMARCC1; may affect modulation of SMARCC1 subcellular location.|||In MKKS and BBS6; causes both increased MKKS protein degradation and reduced solubility relative to wild-type and Tyr-84 mutant; the mutant is immobilized at the centrosome even in the absence of proteasome inhibition; the mutant is also highly polyubiquitinated; no effect on import to the nucleus.|||In MKKS; associated with S-242; decreased interaction with BBS12; no effect on ciliogenesis; disrupts import to the nucleus; no effect on interaction with SMARCC1; may affect modulation of SMARCC1 subcellular location.|||In a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS12; uncertain pathological role.|||Molecular chaperone MKKS|||No effect on import to the nucleus.|||Substrate-binding apical domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128415|||http://purl.uniprot.org/annotation/VAR_009864|||http://purl.uniprot.org/annotation/VAR_009865|||http://purl.uniprot.org/annotation/VAR_009866|||http://purl.uniprot.org/annotation/VAR_009867|||http://purl.uniprot.org/annotation/VAR_009868|||http://purl.uniprot.org/annotation/VAR_009869|||http://purl.uniprot.org/annotation/VAR_009882|||http://purl.uniprot.org/annotation/VAR_009883|||http://purl.uniprot.org/annotation/VAR_009884|||http://purl.uniprot.org/annotation/VAR_013161|||http://purl.uniprot.org/annotation/VAR_017035|||http://purl.uniprot.org/annotation/VAR_017036|||http://purl.uniprot.org/annotation/VAR_017037|||http://purl.uniprot.org/annotation/VAR_017038|||http://purl.uniprot.org/annotation/VAR_017039|||http://purl.uniprot.org/annotation/VAR_017040|||http://purl.uniprot.org/annotation/VAR_017041|||http://purl.uniprot.org/annotation/VAR_017042|||http://purl.uniprot.org/annotation/VAR_038898|||http://purl.uniprot.org/annotation/VAR_038899|||http://purl.uniprot.org/annotation/VAR_038900|||http://purl.uniprot.org/annotation/VAR_038901|||http://purl.uniprot.org/annotation/VAR_038902|||http://purl.uniprot.org/annotation/VAR_038903|||http://purl.uniprot.org/annotation/VAR_066262|||http://purl.uniprot.org/annotation/VAR_066263|||http://purl.uniprot.org/annotation/VAR_066264|||http://purl.uniprot.org/annotation/VAR_066265|||http://purl.uniprot.org/annotation/VAR_077208|||http://purl.uniprot.org/annotation/VAR_080223
http://togogenome.org/gene/9606:MAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21145                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform B.|||In isoform C.|||In isoform D.|||MARVEL|||Myelin and lymphocyte protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156805|||http://purl.uniprot.org/annotation/VSP_003162|||http://purl.uniprot.org/annotation/VSP_003163|||http://purl.uniprot.org/annotation/VSP_003164
http://togogenome.org/gene/9606:STK39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UEW8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to WNK1 and SLC12A2/NKCC1.|||Abolished serine/threonine-protein kinase activity.|||Basic and acidic residues|||Caspase cleavage related site|||Decreased binding to SLC12A2/NKCC1.|||Disordered|||Does not affect activation by WNK kinases.|||Does not greatly affect the kinase activity.|||In isoform 2.|||Interaction with RELT|||Mimics phosphorylation; promoting kinase activity independently of WNK kinases.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine|||Phosphothreonine; by WNK1|||Prevents phosphorylation and activation by WNK kinases.|||Protein kinase|||Proton acceptor|||STE20/SPS1-related proline-alanine-rich protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086722|||http://purl.uniprot.org/annotation/VSP_055889
http://togogenome.org/gene/9606:TNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A499FJ16|||http://purl.uniprot.org/uniprot/B3KXJ4|||http://purl.uniprot.org/uniprot/C9J1X3|||http://purl.uniprot.org/uniprot/Q07912                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activated CDC42 kinase 1|||CRIB|||Constantly active kinase.|||Disordered|||EBD domain|||Found in patients with childhood-onset epilepsy; unknown pathological significance; loss of interaction with NEDD4 and NEDD4L; increased protein abundance.|||In a gastric adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region.|||In a lung adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates; no effect on subcellular localization to perinuclear region.|||In an ovarian endometrioid cancer sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Y-284 leading to activation of AKT1; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on catalytic activity itself as the purified kinase domain has activity in vitro comparable to wild-type protein; no effect on subcellular localization to perinuclear region.|||In an ovarian mucinous carcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region.|||In isoform 2.|||In isoform 3.|||Increased autophosphorylation at Y-284.|||Loss of autophosphorylation at Y-284.|||Mig-6|||No effect on autophosphorylation at Y-284.|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by SRC and autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Required for interaction with NEDD4|||Required for interaction with SRC|||SAM-like domain|||SH3|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088058|||http://purl.uniprot.org/annotation/VAR_032792|||http://purl.uniprot.org/annotation/VAR_032793|||http://purl.uniprot.org/annotation/VAR_032794|||http://purl.uniprot.org/annotation/VAR_032795|||http://purl.uniprot.org/annotation/VAR_032796|||http://purl.uniprot.org/annotation/VAR_032797|||http://purl.uniprot.org/annotation/VAR_032798|||http://purl.uniprot.org/annotation/VAR_032799|||http://purl.uniprot.org/annotation/VAR_032800|||http://purl.uniprot.org/annotation/VAR_032801|||http://purl.uniprot.org/annotation/VAR_032802|||http://purl.uniprot.org/annotation/VAR_057115|||http://purl.uniprot.org/annotation/VAR_076966|||http://purl.uniprot.org/annotation/VSP_008655|||http://purl.uniprot.org/annotation/VSP_008656|||http://purl.uniprot.org/annotation/VSP_037284|||http://purl.uniprot.org/annotation/VSP_037285|||http://purl.uniprot.org/annotation/VSP_037286
http://togogenome.org/gene/9606:NAA35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K874|||http://purl.uniprot.org/uniprot/Q5VZE5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-alpha-acetyltransferase 35, NatC auxiliary subunit|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308614|||http://purl.uniprot.org/annotation/VSP_056098|||http://purl.uniprot.org/annotation/VSP_056099
http://togogenome.org/gene/9606:SCGB1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95968                                                                                  ^@                                                                                  Chain|||Experimental Information|||Mass|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Mass|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 1D member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036378
http://togogenome.org/gene/9606:RBMXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75526                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Pro residues|||RNA-binding motif protein, X-linked-like-2|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281737|||http://purl.uniprot.org/annotation/VAR_055334|||http://purl.uniprot.org/annotation/VAR_055335|||http://purl.uniprot.org/annotation/VAR_055336|||http://purl.uniprot.org/annotation/VAR_061833
http://togogenome.org/gene/9606:ADGRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXM8|||http://purl.uniprot.org/uniprot/Q5T601                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor F1|||Cytoplasmic|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012891|||http://purl.uniprot.org/annotation/PRO_5004229225|||http://purl.uniprot.org/annotation/VAR_055928|||http://purl.uniprot.org/annotation/VSP_039588|||http://purl.uniprot.org/annotation/VSP_039589
http://togogenome.org/gene/9606:PUM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14671                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenine-nucleotide binding in RNA target|||B and inds cytosine-nucleotide in RNA target.|||Basic and acidic residues|||Changes the specificity for RNA; when associated with 1043-SN-1044.|||Changes the specificity for RNA; when associated with E-1047.|||Decreased RNA-binding activity.|||Disordered|||Does not affect RNA-binding activity.|||Guanine-nucleotide binding in RNA target|||In SCA47; decreased post-transcriptional repression of E2F3 and ATXN1.|||In SCA47; results in reduced PUM1 protein levels and decreased post-transcriptional repression of E2F3 and ATXN1.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 4.|||N-acetylserine|||Non-specific-nucleotide binding in RNA target|||Omega-N-methylarginine|||PUM-HD|||Phospho-mimic mutant; persistent RNA-binding activity in quiescent cells.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pumilio 1|||Pumilio 2|||Pumilio 3|||Pumilio 4|||Pumilio 5|||Pumilio 6|||Pumilio 7|||Pumilio 8|||Pumilio homolog 1|||Removed|||Specifically binds cytosine-nucleotide in RNA target.|||Specifically binds guanine-nucleotide in RNA target.|||Specifically binds uracil-nucleotide in RNA target.|||Uracil-nucleotide binding in RNA target                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075917|||http://purl.uniprot.org/annotation/VAR_080784|||http://purl.uniprot.org/annotation/VAR_080785|||http://purl.uniprot.org/annotation/VAR_080786|||http://purl.uniprot.org/annotation/VSP_017059|||http://purl.uniprot.org/annotation/VSP_017060|||http://purl.uniprot.org/annotation/VSP_017061|||http://purl.uniprot.org/annotation/VSP_053703|||http://purl.uniprot.org/annotation/VSP_053704
http://togogenome.org/gene/9606:ABHD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUJ1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||In isoform 2.|||In isoform 3.|||Loss of palmitoyl-(protein) hydrolase activity.|||Mitochondrion|||Palmitoyl-protein thioesterase ABHD10, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280733|||http://purl.uniprot.org/annotation/VAR_031194|||http://purl.uniprot.org/annotation/VSP_056093|||http://purl.uniprot.org/annotation/VSP_056742|||http://purl.uniprot.org/annotation/VSP_056743
http://togogenome.org/gene/9606:TUBA3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PEY2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Variant|||Site                                                                                  ^@                                                                                  3'-nitrotyrosine|||Detyrosinated tubulin alpha-3E chain|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Tubulin alpha-3E chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293649|||http://purl.uniprot.org/annotation/PRO_0000437400|||http://purl.uniprot.org/annotation/VAR_052667|||http://purl.uniprot.org/annotation/VAR_052668|||http://purl.uniprot.org/annotation/VAR_052669|||http://purl.uniprot.org/annotation/VAR_054640|||http://purl.uniprot.org/annotation/VAR_054641
http://togogenome.org/gene/9606:HIPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAE4|||http://purl.uniprot.org/uniprot/Q9H422                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeodomain-interacting protein kinase 3|||In isoform 2.|||Interaction with AR|||Interaction with FAS|||Interaction with UBL1|||Loss of kinase activity and impaired activation of SF1.|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Required for localization to nuclear speckles|||SUMO interaction motifs (SIM); required for nuclear localization and kinase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085998|||http://purl.uniprot.org/annotation/VAR_040549|||http://purl.uniprot.org/annotation/VAR_040550|||http://purl.uniprot.org/annotation/VAR_040551|||http://purl.uniprot.org/annotation/VAR_040552|||http://purl.uniprot.org/annotation/VAR_040553|||http://purl.uniprot.org/annotation/VAR_051627|||http://purl.uniprot.org/annotation/VSP_013140
http://togogenome.org/gene/9606:CT45A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMU7|||http://purl.uniprot.org/uniprot/P0DMU8|||http://purl.uniprot.org/uniprot/P0DMV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A5|||Cancer/testis antigen family 45 member A6|||Cancer/testis antigen family 45 member A7|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308950|||http://purl.uniprot.org/annotation/PRO_0000433029|||http://purl.uniprot.org/annotation/PRO_0000433117
http://togogenome.org/gene/9606:BPIFB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59826|||http://purl.uniprot.org/uniprot/Q14DE0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPI fold-containing family B member 3|||Lipid-binding serum glycoprotein C-terminal|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017170|||http://purl.uniprot.org/annotation/PRO_5014306934|||http://purl.uniprot.org/annotation/VAR_049742|||http://purl.uniprot.org/annotation/VAR_049743|||http://purl.uniprot.org/annotation/VAR_049744|||http://purl.uniprot.org/annotation/VAR_049745|||http://purl.uniprot.org/annotation/VAR_049746
http://togogenome.org/gene/9606:SLCO1B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP78|||http://purl.uniprot.org/uniprot/Q9NPD5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In a colorectal cancer sample; somatic mutation.|||In isoform SLCO1B3-2.|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 1B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191053|||http://purl.uniprot.org/annotation/VAR_024645|||http://purl.uniprot.org/annotation/VAR_036410|||http://purl.uniprot.org/annotation/VAR_036411|||http://purl.uniprot.org/annotation/VAR_053672|||http://purl.uniprot.org/annotation/VAR_053673|||http://purl.uniprot.org/annotation/VAR_062150|||http://purl.uniprot.org/annotation/VSP_056615|||http://purl.uniprot.org/annotation/VSP_056616|||http://purl.uniprot.org/annotation/VSP_056617
http://togogenome.org/gene/9606:KANK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NY19                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||In isoform 1.|||KN motif and ankyrin repeat domain-containing protein 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244582|||http://purl.uniprot.org/annotation/VAR_026909|||http://purl.uniprot.org/annotation/VAR_026910|||http://purl.uniprot.org/annotation/VAR_026911|||http://purl.uniprot.org/annotation/VSP_061119
http://togogenome.org/gene/9606:SLX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSI2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform B.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Ribosome biogenesis protein SLX9 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079528|||http://purl.uniprot.org/annotation/VAR_021949|||http://purl.uniprot.org/annotation/VSP_003831
http://togogenome.org/gene/9606:FGF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVZ8|||http://purl.uniprot.org/uniprot/A0A9L9PX77|||http://purl.uniprot.org/uniprot/A0A9L9PXK7|||http://purl.uniprot.org/uniprot/Q92915                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibroblast growth factor 14|||In SCA27A.|||In a colorectal cancer.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147610|||http://purl.uniprot.org/annotation/VAR_022735|||http://purl.uniprot.org/annotation/VAR_022736|||http://purl.uniprot.org/annotation/VAR_082821|||http://purl.uniprot.org/annotation/VAR_087533|||http://purl.uniprot.org/annotation/VSP_029051
http://togogenome.org/gene/9606:PON2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15165                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Associated with elevated mean fasting plasma glucose level.|||In isoform 1.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Not cleaved|||Proton acceptor|||Serum paraoxonase/arylesterase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223287|||http://purl.uniprot.org/annotation/VAR_006045|||http://purl.uniprot.org/annotation/VAR_006046|||http://purl.uniprot.org/annotation/VAR_020786|||http://purl.uniprot.org/annotation/VSP_004533|||http://purl.uniprot.org/annotation/VSP_040715
http://togogenome.org/gene/9606:TRAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60296                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HAP1 N-terminal|||In isoform 2.|||Interaction with HGS|||Phosphoserine|||Polar residues|||Pro residues|||Trafficking kinesin-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064538|||http://purl.uniprot.org/annotation/VAR_014201|||http://purl.uniprot.org/annotation/VAR_014434|||http://purl.uniprot.org/annotation/VAR_051458|||http://purl.uniprot.org/annotation/VSP_053418|||http://purl.uniprot.org/annotation/VSP_053419
http://togogenome.org/gene/9606:ZNF804A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z570                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Zinc finger protein 804A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232518|||http://purl.uniprot.org/annotation/VAR_025943|||http://purl.uniprot.org/annotation/VAR_025944|||http://purl.uniprot.org/annotation/VAR_025945|||http://purl.uniprot.org/annotation/VAR_025946|||http://purl.uniprot.org/annotation/VAR_025947|||http://purl.uniprot.org/annotation/VAR_035599|||http://purl.uniprot.org/annotation/VAR_054133|||http://purl.uniprot.org/annotation/VAR_054134|||http://purl.uniprot.org/annotation/VAR_054135
http://togogenome.org/gene/9606:EXOC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YP36|||http://purl.uniprot.org/uniprot/B2RDH5|||http://purl.uniprot.org/uniprot/B3KXY5|||http://purl.uniprot.org/uniprot/B7Z6G5|||http://purl.uniprot.org/uniprot/E7EW84|||http://purl.uniprot.org/uniprot/Q8TAG9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Exocyst complex component 6|||Exocyst complex subunit Sec15 C-terminal|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118951|||http://purl.uniprot.org/annotation/VAR_044522|||http://purl.uniprot.org/annotation/VAR_044523|||http://purl.uniprot.org/annotation/VAR_044524|||http://purl.uniprot.org/annotation/VSP_047160
http://togogenome.org/gene/9606:ZSWIM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7M6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||SWIM-type|||Zinc finger SWIM domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223101
http://togogenome.org/gene/9606:CCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29279|||http://purl.uniprot.org/uniprot/Q5M8T4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CCN family member 2|||CTCK|||Heparin-binding|||IGFBP N-terminal|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TSP type-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014402|||http://purl.uniprot.org/annotation/PRO_5014309868|||http://purl.uniprot.org/annotation/VAR_027925|||http://purl.uniprot.org/annotation/VSP_002460
http://togogenome.org/gene/9606:SYT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 1.|||Polar residues|||Synaptotagmin-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183959|||http://purl.uniprot.org/annotation/VAR_046952|||http://purl.uniprot.org/annotation/VAR_046953|||http://purl.uniprot.org/annotation/VAR_061834|||http://purl.uniprot.org/annotation/VAR_082921|||http://purl.uniprot.org/annotation/VAR_082922|||http://purl.uniprot.org/annotation/VSP_040846|||http://purl.uniprot.org/annotation/VSP_040847
http://togogenome.org/gene/9606:RANBP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60518                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||N-acetylalanine|||Ran-GTP binding|||Ran-binding protein 6|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120779
http://togogenome.org/gene/9606:CMYA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3K9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Amphipathic helix H1|||Amphipathic helix H2|||Amphipathic helix H3|||B-box coiled-coil; BBC|||B30.2/SPRY|||Basic and acidic residues|||Basic residues|||Cardiomyopathy-associated protein 5|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Phosphoserine|||Polar residues|||Required for RYR2 clustering                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328722|||http://purl.uniprot.org/annotation/VAR_042471|||http://purl.uniprot.org/annotation/VAR_042472|||http://purl.uniprot.org/annotation/VAR_042473|||http://purl.uniprot.org/annotation/VAR_042474|||http://purl.uniprot.org/annotation/VAR_042475|||http://purl.uniprot.org/annotation/VAR_042476|||http://purl.uniprot.org/annotation/VAR_042477|||http://purl.uniprot.org/annotation/VAR_042478|||http://purl.uniprot.org/annotation/VAR_042479|||http://purl.uniprot.org/annotation/VAR_042480|||http://purl.uniprot.org/annotation/VAR_042481|||http://purl.uniprot.org/annotation/VAR_042482|||http://purl.uniprot.org/annotation/VAR_042483|||http://purl.uniprot.org/annotation/VAR_042484|||http://purl.uniprot.org/annotation/VAR_042485|||http://purl.uniprot.org/annotation/VAR_042486|||http://purl.uniprot.org/annotation/VAR_042487|||http://purl.uniprot.org/annotation/VAR_042488|||http://purl.uniprot.org/annotation/VAR_042489|||http://purl.uniprot.org/annotation/VAR_042490|||http://purl.uniprot.org/annotation/VAR_042491|||http://purl.uniprot.org/annotation/VAR_042492|||http://purl.uniprot.org/annotation/VAR_042493|||http://purl.uniprot.org/annotation/VAR_042494|||http://purl.uniprot.org/annotation/VAR_042495|||http://purl.uniprot.org/annotation/VAR_042496|||http://purl.uniprot.org/annotation/VAR_042497|||http://purl.uniprot.org/annotation/VAR_061611
http://togogenome.org/gene/9606:ZNF131                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52739                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||No effect on sumoylation. Complete loss of CBX4 sumoylation; when associated with R-477 and R-601.|||No effect on sumoylation; when associated with R-242 and R-281.|||No effect on sumoylation; when associated with R-281 and R-289.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Significant loss of sumoylation. Complete loss of CBX4 sumoylation; when associated with R-477 and R-610.|||Small loss of sumoylation. Complete loss of CBX4 sumoylation; when associated with R-601 and R-610.|||Zinc finger protein 131                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047413|||http://purl.uniprot.org/annotation/VSP_016923
http://togogenome.org/gene/9606:GCNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0V5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Defines the adult i phenotype.|||Helical; Signal-anchor for type II membrane protein|||In CTRCT13; unknown pathological significance.|||In isoform B.|||In isoform C.|||Lumenal|||N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395119|||http://purl.uniprot.org/annotation/VAR_073827|||http://purl.uniprot.org/annotation/VAR_073828|||http://purl.uniprot.org/annotation/VAR_073829|||http://purl.uniprot.org/annotation/VAR_073830|||http://purl.uniprot.org/annotation/VAR_084818|||http://purl.uniprot.org/annotation/VSP_058347|||http://purl.uniprot.org/annotation/VSP_058348
http://togogenome.org/gene/9606:CNTNAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78357                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein 1|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||In CHN3.|||In LCCS7 and CHN3.|||In LCCS7.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019503|||http://purl.uniprot.org/annotation/VAR_050267|||http://purl.uniprot.org/annotation/VAR_078818|||http://purl.uniprot.org/annotation/VAR_078819|||http://purl.uniprot.org/annotation/VAR_078820|||http://purl.uniprot.org/annotation/VAR_078821|||http://purl.uniprot.org/annotation/VAR_078822|||http://purl.uniprot.org/annotation/VAR_078823|||http://purl.uniprot.org/annotation/VAR_081766|||http://purl.uniprot.org/annotation/VAR_081767|||http://purl.uniprot.org/annotation/VAR_081768|||http://purl.uniprot.org/annotation/VAR_081769|||http://purl.uniprot.org/annotation/VAR_081770|||http://purl.uniprot.org/annotation/VAR_081771|||http://purl.uniprot.org/annotation/VAR_081772
http://togogenome.org/gene/9606:LRRC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H756                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||Leucine-rich repeat-containing protein 19|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021610
http://togogenome.org/gene/9606:OR6A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW91|||http://purl.uniprot.org/uniprot/O95222                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150619|||http://purl.uniprot.org/annotation/VAR_053217
http://togogenome.org/gene/9606:LHFPL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG04|||http://purl.uniprot.org/uniprot/Q6ICI0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||LHFPL tetraspan subfamily member 7 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337008
http://togogenome.org/gene/9606:SPATA31A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313018
http://togogenome.org/gene/9606:COL28A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2UY09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Basic and acidic residues|||Collagen alpha-1(XXVIII) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000074667|||http://purl.uniprot.org/annotation/VAR_038566|||http://purl.uniprot.org/annotation/VAR_038567|||http://purl.uniprot.org/annotation/VAR_038568|||http://purl.uniprot.org/annotation/VAR_038569|||http://purl.uniprot.org/annotation/VAR_038570|||http://purl.uniprot.org/annotation/VAR_038571|||http://purl.uniprot.org/annotation/VAR_061117|||http://purl.uniprot.org/annotation/VSP_031091|||http://purl.uniprot.org/annotation/VSP_031092|||http://purl.uniprot.org/annotation/VSP_031093|||http://purl.uniprot.org/annotation/VSP_031094
http://togogenome.org/gene/9606:TRMT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z2W7|||http://purl.uniprot.org/uniprot/Q8IZ69                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||RRM|||tRNA (uracil-5-)-methyltransferase homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081614|||http://purl.uniprot.org/annotation/VAR_033721|||http://purl.uniprot.org/annotation/VAR_035482|||http://purl.uniprot.org/annotation/VSP_011322|||http://purl.uniprot.org/annotation/VSP_011323
http://togogenome.org/gene/9606:AMH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03971                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Abolishes AMH signaling.|||Abolishes AMH signaling. Does not induce regression of the Muellerian duct.|||Cleavage|||Decreases AMH signaling.|||Disordered|||In PMDS1.|||Interchain|||Little effect on AMH signaling.|||Muellerian-inhibiting factor|||N-linked (GlcNAc...) asparagine|||Pro residues|||Shows a slight decrease in AMH signaling. Affects slightly Mullerian duct regression.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033747|||http://purl.uniprot.org/annotation/PRO_0000454649|||http://purl.uniprot.org/annotation/VAR_007483|||http://purl.uniprot.org/annotation/VAR_007484|||http://purl.uniprot.org/annotation/VAR_007485|||http://purl.uniprot.org/annotation/VAR_007486|||http://purl.uniprot.org/annotation/VAR_007487|||http://purl.uniprot.org/annotation/VAR_007488|||http://purl.uniprot.org/annotation/VAR_007489|||http://purl.uniprot.org/annotation/VAR_007490|||http://purl.uniprot.org/annotation/VAR_007491|||http://purl.uniprot.org/annotation/VAR_007492|||http://purl.uniprot.org/annotation/VAR_031027|||http://purl.uniprot.org/annotation/VAR_031028|||http://purl.uniprot.org/annotation/VAR_065100
http://togogenome.org/gene/9606:SFXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NB2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylmethionine|||Sideroflexin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000177035
http://togogenome.org/gene/9606:ATP8B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60423                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Phospholipid-transporting ATPase IK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046367|||http://purl.uniprot.org/annotation/VAR_055544|||http://purl.uniprot.org/annotation/VAR_055545|||http://purl.uniprot.org/annotation/VSP_039716|||http://purl.uniprot.org/annotation/VSP_043554|||http://purl.uniprot.org/annotation/VSP_043555
http://togogenome.org/gene/9606:PPP1R14C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAE6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by ILK1|||Polar residues|||Protein phosphatase 1 regulatory subunit 14C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071494|||http://purl.uniprot.org/annotation/VAR_025547
http://togogenome.org/gene/9606:HYAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12891                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  EGF-like|||GPI-anchor amidated glycine|||Hyaluronidase-2|||N-linked (GlcNAc...) asparagine|||Proton donor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012099|||http://purl.uniprot.org/annotation/PRO_0000012100|||http://purl.uniprot.org/annotation/VAR_028170|||http://purl.uniprot.org/annotation/VAR_061193
http://togogenome.org/gene/9606:DHRS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJE2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Splice Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 12|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312175|||http://purl.uniprot.org/annotation/VSP_029724|||http://purl.uniprot.org/annotation/VSP_029725|||http://purl.uniprot.org/annotation/VSP_029726|||http://purl.uniprot.org/annotation/VSP_029727
http://togogenome.org/gene/9606:XIRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q702N8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform B.|||In isoform C.|||Interaction with CTNNB1|||Interaction with FLNC|||Interaction with VASP|||Phosphoserine|||Polar residues|||Pro residues|||Xin 1|||Xin 10|||Xin 11|||Xin 12|||Xin 13|||Xin 14|||Xin 15|||Xin 16|||Xin 17|||Xin 2|||Xin 3|||Xin 4|||Xin 5|||Xin 6|||Xin 7|||Xin 8|||Xin 9|||Xin actin-binding repeat-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316983|||http://purl.uniprot.org/annotation/VAR_038439|||http://purl.uniprot.org/annotation/VAR_038440|||http://purl.uniprot.org/annotation/VAR_038441|||http://purl.uniprot.org/annotation/VAR_038442|||http://purl.uniprot.org/annotation/VAR_038443|||http://purl.uniprot.org/annotation/VAR_038444|||http://purl.uniprot.org/annotation/VAR_038445|||http://purl.uniprot.org/annotation/VAR_038446|||http://purl.uniprot.org/annotation/VAR_038447|||http://purl.uniprot.org/annotation/VAR_038448|||http://purl.uniprot.org/annotation/VAR_061722|||http://purl.uniprot.org/annotation/VAR_061723|||http://purl.uniprot.org/annotation/VAR_061724|||http://purl.uniprot.org/annotation/VAR_061725|||http://purl.uniprot.org/annotation/VSP_030843|||http://purl.uniprot.org/annotation/VSP_030844|||http://purl.uniprot.org/annotation/VSP_030845
http://togogenome.org/gene/9606:BCOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BZ37|||http://purl.uniprot.org/uniprot/H7C231|||http://purl.uniprot.org/uniprot/Q6W2J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-509.|||Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-507 and A-511.|||Abolishes interaction with BCL6 and inhibits BCL6 corepression activity; when associated with A-509 and A-511.|||BCL-6 corepressor|||BCL-6 corepressor PCGF1 binding|||BCL-6 corepressor non-ankyrin-repeat|||Basic and acidic residues|||Diminishes interaction with BCL6.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MCOPS2.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with BCL6|||N6-acetyllysine|||Necessary and sufficient for interaction with PCGF1|||Phosphoserine|||Polar residues|||Slightly inhibits interaction with PCGF1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066978|||http://purl.uniprot.org/annotation/VAR_020921|||http://purl.uniprot.org/annotation/VSP_012554|||http://purl.uniprot.org/annotation/VSP_012555|||http://purl.uniprot.org/annotation/VSP_012556|||http://purl.uniprot.org/annotation/VSP_012557
http://togogenome.org/gene/9606:OR2T29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH02                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150506
http://togogenome.org/gene/9606:GTF3C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BY84|||http://purl.uniprot.org/uniprot/Q9Y5Q8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||General transcription factor 3C polypeptide 5|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed|||Transcription factor IIIC subunit 5 HTH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209715|||http://purl.uniprot.org/annotation/VAR_053727|||http://purl.uniprot.org/annotation/VSP_010355|||http://purl.uniprot.org/annotation/VSP_035196
http://togogenome.org/gene/9606:FOXD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12950                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091821|||http://purl.uniprot.org/annotation/VAR_028177|||http://purl.uniprot.org/annotation/VAR_028178|||http://purl.uniprot.org/annotation/VAR_028179
http://togogenome.org/gene/9606:RING1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8F2|||http://purl.uniprot.org/uniprot/Q06587                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RING1|||In isoform 2.|||Necessary for interaction with CBX2|||Necessary for transcriptional repression|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056384|||http://purl.uniprot.org/annotation/VAR_076618|||http://purl.uniprot.org/annotation/VSP_017694
http://togogenome.org/gene/9606:KMT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03164                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||A.T hook 1|||A.T hook 2|||A.T hook 3|||Abolished auto-methylation.|||Abolishes DNA-binding and increases CpG methylation of the HOXA9 promoter region. Does not lead to the development of leukemia when overexpressed in mice as gene fusion with MLLT3.|||Abolishes cleavage by TASP1; when associated with 2666-A-A-2667.|||Abolishes interaction with histone H3K4me3.|||Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding.|||Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874.|||Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878.|||Basic and acidic residues|||Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-KNL1 oncogenes|||Breakpoint for translocation to form KMT2A-AFF4 fusion protein|||Breakpoint for translocation to form KMT2A-CENPK oncogene|||Breakpoint for translocation to form KMT2A-FRYL fusion protein|||Breakpoint for translocation to form KMT2A-GAS7 oncogene|||Breakpoint for translocation to form KMT2A-LPP|||Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene|||Bromo; divergent|||C2HC pre-PHD-type|||CXXC-type|||Cleavage; by TASP1, site 1|||Cleavage; by TASP1, site 2|||Decreases affinity for histone H3K4me3.|||Decreases binding affinity for PPIE.|||Disordered|||Disrupts interaction with ASH2L and RBBP5 and nearly abolishes histone methyltransferase activity.|||Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869.|||Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872.|||FYR C-terminal|||FYR N-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase 2A|||Impairs DNA-binding.|||Impairs methyltransferase activity toward unmodified or monomethylated H3K4me.|||Impairs zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding.|||Important for WDR5-recognition and binding|||In isoform 2.|||In isoform 3.|||Increased interaction with WDR5.|||Integrase domain-binding motif 1 (IBM1)|||Integrase domain-binding motif 2 (IBM2)|||Interaction with histone H3K4me3|||Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with I-3861.|||Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with L-3867.|||Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with T-3861.|||Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with V-3867.|||Loss of interaction with MEN1.|||Loss of interaction with PSIP1; when associated with A-148.|||Loss of interaction with PSIP1; when associated with Q-144 and A-148.|||Loss of interaction with PSIP1; when associated with Q-146 and A-148.|||Loss of interaction with the WRAD complex and WDR5.|||Loss of the histone H3 methyltransferase activity. Abolishes interaction with S-adenosyl-L-methionine.|||MLL cleavage product C180|||MLL cleavage product N320|||May perturb protein folding and thereby decrease binding affinity for PPIE.|||Menin-binding motif (MBM)|||Mildly decreases DNA-binding.|||N6-acetyllysine|||No effect on DNA-binding.|||No effect on stability or DNA-binding.|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4|||Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-136.|||Phosphomimetic mutant. Significant increase in interaction with PSIP1; when associated with D-142.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Post-SET|||Pro residues|||Reduced interaction with MEN1.|||Reduced interaction with MEN1; when associated with E-24.|||Reduced interaction with MEN1; when associated with E-25.|||Reduced interaction with PSIP1.|||Reduced interaction with PSIP1. Loss of interaction with PSIP1; when associated with A-149 or Q-144 and Q-146.|||Reduced interaction with PSIP1; when associated with A-129 or A-132.|||Reduced interaction with PSIP1; when associated with A-133.|||Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720.|||S-methylcysteine; by autocatalysis|||SET|||Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity.|||Slight decrease in interaction with WDR5.|||Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867.|||Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871.|||Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me.|||WDR5 interaction motif (WIN)|||Weakly affects interaction with PSIP1 whereas significantly decreases interaction of KMT2A-MEN1 complex with PSIP1. Reduced interaction with PSIP1; when associated with A-133. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124876|||http://purl.uniprot.org/annotation/PRO_0000390949|||http://purl.uniprot.org/annotation/PRO_0000390950|||http://purl.uniprot.org/annotation/VAR_021317|||http://purl.uniprot.org/annotation/VAR_021318|||http://purl.uniprot.org/annotation/VAR_021319|||http://purl.uniprot.org/annotation/VAR_021320|||http://purl.uniprot.org/annotation/VAR_021321|||http://purl.uniprot.org/annotation/VAR_021322|||http://purl.uniprot.org/annotation/VAR_021323|||http://purl.uniprot.org/annotation/VAR_021324|||http://purl.uniprot.org/annotation/VAR_052652|||http://purl.uniprot.org/annotation/VSP_006666|||http://purl.uniprot.org/annotation/VSP_046879
http://togogenome.org/gene/9606:SPARCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZB68|||http://purl.uniprot.org/uniprot/Q14515|||http://purl.uniprot.org/uniprot/Q8N4S1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||Follistatin-like|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one additional site|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||SPARC-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020312|||http://purl.uniprot.org/annotation/PRO_5014312249|||http://purl.uniprot.org/annotation/VAR_016107|||http://purl.uniprot.org/annotation/VAR_056578|||http://purl.uniprot.org/annotation/VAR_058849|||http://purl.uniprot.org/annotation/VSP_056678
http://togogenome.org/gene/9606:PRMT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVM4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SBIDDS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Protein arginine N-methyltransferase 7|||SAM-dependent MTase PRMT-type 1|||SAM-dependent MTase PRMT-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212335|||http://purl.uniprot.org/annotation/VAR_076329|||http://purl.uniprot.org/annotation/VAR_076330|||http://purl.uniprot.org/annotation/VAR_076331|||http://purl.uniprot.org/annotation/VSP_005213|||http://purl.uniprot.org/annotation/VSP_005214|||http://purl.uniprot.org/annotation/VSP_037253|||http://purl.uniprot.org/annotation/VSP_037254|||http://purl.uniprot.org/annotation/VSP_037255
http://togogenome.org/gene/9606:ZBED4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75132                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BED-type 1|||BED-type 2|||BED-type 3|||BED-type 4|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Required for homodimerization and nuclear accumulation|||Zinc finger BED domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066563|||http://purl.uniprot.org/annotation/VAR_027809
http://togogenome.org/gene/9606:CSNK2A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEV1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Casein kinase II subunit alpha 3|||In a lung carcinoma sample; somatic mutation; shows greater kinase activity, provides a cell growth advantage and increases its interaction with the PML tumor suppressor protein and PML degradation.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422194|||http://purl.uniprot.org/annotation/VAR_069225
http://togogenome.org/gene/9606:TROAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12815                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 33 AA approximate tandem repeats|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Tastin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065636|||http://purl.uniprot.org/annotation/VSP_042820|||http://purl.uniprot.org/annotation/VSP_042821|||http://purl.uniprot.org/annotation/VSP_055063
http://togogenome.org/gene/9606:DZIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSP1|||http://purl.uniprot.org/uniprot/Q86YF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Cilium assembly protein DZIP1|||Disordered|||In MVP3; decreased protein stability.|||In SPGF47; decreased protein abundance; changed ciliary basal body organization; loss of sperm flagellum assembly.|||In SPGF47; decreased protein abundance; loss of sperm flagellum assembly.|||In isoform 2.|||In isoform 3.|||Mediates interaction with GDI2 and RAB8A|||Mediates interaction with GLI3 and localization to the cilium basal body|||Mediates interaction with PCM1|||Phosphoserine; by PLK1|||Polar residues|||Required for interaction with DAZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047106|||http://purl.uniprot.org/annotation/VAR_019456|||http://purl.uniprot.org/annotation/VAR_052710|||http://purl.uniprot.org/annotation/VAR_052711|||http://purl.uniprot.org/annotation/VAR_085517|||http://purl.uniprot.org/annotation/VAR_085518|||http://purl.uniprot.org/annotation/VAR_085519|||http://purl.uniprot.org/annotation/VSP_010962|||http://purl.uniprot.org/annotation/VSP_010963|||http://purl.uniprot.org/annotation/VSP_010964|||http://purl.uniprot.org/annotation/VSP_010965
http://togogenome.org/gene/9606:SGK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBY8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increased activation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine; by PDPK1|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086646|||http://purl.uniprot.org/annotation/VAR_041074|||http://purl.uniprot.org/annotation/VAR_041075|||http://purl.uniprot.org/annotation/VAR_083966|||http://purl.uniprot.org/annotation/VSP_060876|||http://purl.uniprot.org/annotation/VSP_060877
http://togogenome.org/gene/9606:FBRSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibrosin-1-like protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321962|||http://purl.uniprot.org/annotation/VAR_039390
http://togogenome.org/gene/9606:CDSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G8JLG2|||http://purl.uniprot.org/uniprot/Q15517                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Corneodesmosin|||Disordered|||In allele 1.11, allele 1.21, allele 1.31, allele 1.32, allele 1.51, allele 1.52, allele 2.11, allele 2.21, allele 2.22 and allele 2.23.|||In allele 1.21.|||In allele 1.31 and allele 1.32.|||In allele 1.32.|||In allele 1.51.|||In allele 2.11, allele 2.21, allele 2.22 and allele 2.23.|||In allele 2.11.|||In allele 2.21, allele 2.22 and allele 2.23.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020912|||http://purl.uniprot.org/annotation/PRO_5014574465|||http://purl.uniprot.org/annotation/VAR_022615|||http://purl.uniprot.org/annotation/VAR_022616|||http://purl.uniprot.org/annotation/VAR_022617|||http://purl.uniprot.org/annotation/VAR_022618|||http://purl.uniprot.org/annotation/VAR_022619|||http://purl.uniprot.org/annotation/VAR_022620|||http://purl.uniprot.org/annotation/VAR_022621|||http://purl.uniprot.org/annotation/VAR_022637|||http://purl.uniprot.org/annotation/VAR_022638|||http://purl.uniprot.org/annotation/VAR_022639|||http://purl.uniprot.org/annotation/VAR_022640|||http://purl.uniprot.org/annotation/VAR_022641|||http://purl.uniprot.org/annotation/VAR_046010
http://togogenome.org/gene/9606:TEAD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15561                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Important loss of interaction with YAP1 and complete loss of transforming ability.|||In isoform 2.|||In isoform 3.|||Loss of interaction with YAP1 and also activation by YAP1.|||Polar residues|||Pro residues|||Reduced interaction with YAP1.|||Reduced transforming ability.|||TEA|||Transcriptional enhancer factor TEF-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205937|||http://purl.uniprot.org/annotation/VAR_052279|||http://purl.uniprot.org/annotation/VSP_043099|||http://purl.uniprot.org/annotation/VSP_045657
http://togogenome.org/gene/9606:MRPL45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WU62|||http://purl.uniprot.org/uniprot/A0A087X2D5|||http://purl.uniprot.org/uniprot/B4DEF8                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Tim44-like                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:UBTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R886|||http://purl.uniprot.org/uniprot/B3KMW8|||http://purl.uniprot.org/uniprot/Q8WUN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Ubiquitin domain-containing protein 2|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244332|||http://purl.uniprot.org/annotation/VAR_052694
http://togogenome.org/gene/9606:CLCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S66                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Chloride channel CLIC-like protein 1|||Disordered|||Helical|||In RP32; reduces ion channel activity; no impact on interaction with CALR; no impact on ER localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297682|||http://purl.uniprot.org/annotation/VAR_034673|||http://purl.uniprot.org/annotation/VAR_083125|||http://purl.uniprot.org/annotation/VSP_027347|||http://purl.uniprot.org/annotation/VSP_027348|||http://purl.uniprot.org/annotation/VSP_027349
http://togogenome.org/gene/9606:DSTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60981|||http://purl.uniprot.org/uniprot/V9HWA6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADF-H|||Destrin|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214918|||http://purl.uniprot.org/annotation/VAR_036459|||http://purl.uniprot.org/annotation/VSP_043069
http://togogenome.org/gene/9606:SELENOT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62341                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Non standard residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Mutagenesis Site|||Non standard residue|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec)|||Helical|||Increases ROS levels induced by neurotoxins.|||Selenocysteine|||Thioredoxin reductase-like selenoprotein T                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032290
http://togogenome.org/gene/9606:RASGEF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9B8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-terminal Ras-GEF|||Ras-GEF|||Ras-GEF domain-containing family member 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297635|||http://purl.uniprot.org/annotation/VSP_027312
http://togogenome.org/gene/9606:NPR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4A5|||http://purl.uniprot.org/uniprot/P17342|||http://purl.uniprot.org/uniprot/Q60I31                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Atrial natriuretic peptide receptor 3|||Cytoplasmic|||Extracellular|||Helical|||In BOMOS; loss of localization at the plasma membrane.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine|||Receptor ligand binding region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012370|||http://purl.uniprot.org/annotation/PRO_5002725502|||http://purl.uniprot.org/annotation/PRO_5014310238|||http://purl.uniprot.org/annotation/VAR_086244|||http://purl.uniprot.org/annotation/VAR_086245|||http://purl.uniprot.org/annotation/VSP_001812|||http://purl.uniprot.org/annotation/VSP_045901|||http://purl.uniprot.org/annotation/VSP_045902
http://togogenome.org/gene/9606:GPR153                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0I9QQ03|||http://purl.uniprot.org/uniprot/Q6NV75                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues|||Pro residues|||Probable G-protein coupled receptor 153                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069637|||http://purl.uniprot.org/annotation/VAR_023741
http://togogenome.org/gene/9606:MYL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01449                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin regulatory light chain 2, atrial isoform|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198725
http://togogenome.org/gene/9606:ZNF200                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP91|||http://purl.uniprot.org/uniprot/P98182                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger protein 200                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047449|||http://purl.uniprot.org/annotation/VAR_052790|||http://purl.uniprot.org/annotation/VSP_036037|||http://purl.uniprot.org/annotation/VSP_046734
http://togogenome.org/gene/9606:C19orf38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein HIDE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341217
http://togogenome.org/gene/9606:STAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AI02|||http://purl.uniprot.org/uniprot/Q6MZM3|||http://purl.uniprot.org/uniprot/Q6MZP3|||http://purl.uniprot.org/uniprot/Q8N3U4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cohesin subunit SA-2|||Disordered|||In HPE13 and MKMS; patient cells show decreased protein abundance; increased sister chromatid cohesion.|||In HPE13.|||In MKMS.|||In MKMS; loss of interaction with RAD21; loss of interaction with cohesin complex.|||In MKMS; unknown pathological significance.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||SCD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120185|||http://purl.uniprot.org/annotation/VAR_060114|||http://purl.uniprot.org/annotation/VAR_082294|||http://purl.uniprot.org/annotation/VAR_082295|||http://purl.uniprot.org/annotation/VAR_082296|||http://purl.uniprot.org/annotation/VAR_082297|||http://purl.uniprot.org/annotation/VAR_082298|||http://purl.uniprot.org/annotation/VAR_082300|||http://purl.uniprot.org/annotation/VAR_083967|||http://purl.uniprot.org/annotation/VAR_083968|||http://purl.uniprot.org/annotation/VAR_083969|||http://purl.uniprot.org/annotation/VAR_083970|||http://purl.uniprot.org/annotation/VSP_041119
http://togogenome.org/gene/9606:CSN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07498                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cleavage; by chymosin/rennin|||Kappa-casein|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; alternate|||Phosphothreonine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004498|||http://purl.uniprot.org/annotation/VAR_026338|||http://purl.uniprot.org/annotation/VAR_026339|||http://purl.uniprot.org/annotation/VAR_026340
http://togogenome.org/gene/9606:ARF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84085                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor 5|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207396
http://togogenome.org/gene/9606:ZNF460                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14592                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 460                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047499|||http://purl.uniprot.org/annotation/VSP_055954
http://togogenome.org/gene/9606:LIMS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW19|||http://purl.uniprot.org/uniprot/P0CW20                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LIM and senescent cell antigen-like-containing domain protein 3|||LIM and senescent cell antigen-like-containing domain protein 4|||LIM zinc-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266013|||http://purl.uniprot.org/annotation/PRO_0000409553|||http://purl.uniprot.org/annotation/VSP_054392
http://togogenome.org/gene/9606:LIN7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAP6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Kinase interacting site|||L27|||PDZ|||Protein lin-7 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189626|||http://purl.uniprot.org/annotation/VSP_042156
http://togogenome.org/gene/9606:FBXL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P050                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box and leucine-rich protein 22|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247149|||http://purl.uniprot.org/annotation/VAR_033940
http://togogenome.org/gene/9606:CEACAM20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UY09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Carcinoembryonic antigen-related cell adhesion molecule 20|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014577|||http://purl.uniprot.org/annotation/VAR_056030|||http://purl.uniprot.org/annotation/VAR_056031|||http://purl.uniprot.org/annotation/VAR_056032|||http://purl.uniprot.org/annotation/VAR_056033|||http://purl.uniprot.org/annotation/VAR_056034|||http://purl.uniprot.org/annotation/VAR_059385|||http://purl.uniprot.org/annotation/VAR_061312|||http://purl.uniprot.org/annotation/VSP_059367|||http://purl.uniprot.org/annotation/VSP_059368|||http://purl.uniprot.org/annotation/VSP_059369
http://togogenome.org/gene/9606:DSCAML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384DVL8|||http://purl.uniprot.org/uniprot/Q8TD84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule DSCAML1|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014748|||http://purl.uniprot.org/annotation/VAR_035512|||http://purl.uniprot.org/annotation/VAR_035513|||http://purl.uniprot.org/annotation/VSP_014978
http://togogenome.org/gene/9606:PALB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YC2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates the interaction with BRCA1; decreases double-stranded DNA break-initiated homologous recombination; reduces PALB2 and RAD51 localization to ionizing radiation-induced foci; may weaken homooligomerization.|||Basic and acidic residues|||ChAM (Chromatin-association motif); required for chromatin association, mediates nucleosome association|||DNA-binding (with the preference D loop > dsDNA > ssDNA)|||Decreases double-stranded DNA break-initiated homologous recombination.|||Disordered|||In BC; abrogates the interaction with BRCA1; abrogates double-stranded DNA break-initiated homologous recombination; abrogates PALB2 and RAD51 localization to ionizing radiation-induced foci; may weaken homooligomerization.|||Interaction with BRCA1|||Interaction with RAD51|||Interaction with RAD51, BRCA2 and POLH|||Loss of interaction with BRCA1 but no effect on interaction with BRCA2.|||May be associated with breast cancer susceptibility.|||May be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR.|||May be associated with breast cancer susceptibility; reduces interaction with BRCA2, RAD51C, RAD51 and XRCC3; decreases double-stranded DNA break-initiated homologous recombination; increases sensitivity to IR.|||Partner and localizer of BRCA2|||Phosphoserine|||Polar residues|||Required for interaction with POLH and POLH DNA synthesis stimulation|||Required for its oligomerization and is important for its focal concentration at DNA damage sites|||Unstable and promotes protein degradation; reduces interaction with RAD51C and RAD51.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252391|||http://purl.uniprot.org/annotation/VAR_032959|||http://purl.uniprot.org/annotation/VAR_054150|||http://purl.uniprot.org/annotation/VAR_066361|||http://purl.uniprot.org/annotation/VAR_066362|||http://purl.uniprot.org/annotation/VAR_066363|||http://purl.uniprot.org/annotation/VAR_066364|||http://purl.uniprot.org/annotation/VAR_066365|||http://purl.uniprot.org/annotation/VAR_066366|||http://purl.uniprot.org/annotation/VAR_066367|||http://purl.uniprot.org/annotation/VAR_066368|||http://purl.uniprot.org/annotation/VAR_066369|||http://purl.uniprot.org/annotation/VAR_066370|||http://purl.uniprot.org/annotation/VAR_066371|||http://purl.uniprot.org/annotation/VAR_066372|||http://purl.uniprot.org/annotation/VAR_066373|||http://purl.uniprot.org/annotation/VAR_066374|||http://purl.uniprot.org/annotation/VAR_066375|||http://purl.uniprot.org/annotation/VAR_066376|||http://purl.uniprot.org/annotation/VAR_066377|||http://purl.uniprot.org/annotation/VAR_066378|||http://purl.uniprot.org/annotation/VAR_066379|||http://purl.uniprot.org/annotation/VAR_066380|||http://purl.uniprot.org/annotation/VAR_066381|||http://purl.uniprot.org/annotation/VAR_066382|||http://purl.uniprot.org/annotation/VAR_066383|||http://purl.uniprot.org/annotation/VAR_066384|||http://purl.uniprot.org/annotation/VAR_079842|||http://purl.uniprot.org/annotation/VAR_079843|||http://purl.uniprot.org/annotation/VAR_079844|||http://purl.uniprot.org/annotation/VAR_079845
http://togogenome.org/gene/9606:GPATCH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRK1|||http://purl.uniprot.org/uniprot/A8KAG1|||http://purl.uniprot.org/uniprot/E9PAV9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-patch                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:LRBA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494BZW2|||http://purl.uniprot.org/uniprot/A0A8V8TKR0|||http://purl.uniprot.org/uniprot/P50851                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Disordered|||Helical|||In CVID8.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Lipopolysaccharide-responsive and beige-like anchor protein|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051068|||http://purl.uniprot.org/annotation/VAR_022028|||http://purl.uniprot.org/annotation/VAR_035883|||http://purl.uniprot.org/annotation/VAR_035884|||http://purl.uniprot.org/annotation/VAR_035885|||http://purl.uniprot.org/annotation/VAR_057605|||http://purl.uniprot.org/annotation/VAR_057606|||http://purl.uniprot.org/annotation/VAR_057607|||http://purl.uniprot.org/annotation/VAR_057608|||http://purl.uniprot.org/annotation/VAR_057609|||http://purl.uniprot.org/annotation/VAR_057610|||http://purl.uniprot.org/annotation/VAR_068690|||http://purl.uniprot.org/annotation/VSP_038225|||http://purl.uniprot.org/annotation/VSP_038226
http://togogenome.org/gene/9606:PRPF38A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAV1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Loss of interaction with MFAP1.|||N-terminal protein interaction domain|||Phosphoserine|||Pre-mRNA-splicing factor 38A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287272|||http://purl.uniprot.org/annotation/VSP_025424
http://togogenome.org/gene/9606:ATP6V1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5K8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  V-type proton ATPase subunit D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144231
http://togogenome.org/gene/9606:TMEM130                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3G9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PKD|||Transmembrane protein 130                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278276|||http://purl.uniprot.org/annotation/VAR_030740|||http://purl.uniprot.org/annotation/VSP_023257|||http://purl.uniprot.org/annotation/VSP_023258
http://togogenome.org/gene/9606:MIER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N344                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ELM2|||Mesoderm induction early response protein 2|||Phosphoserine|||Polar residues|||SANT|||Unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313678|||http://purl.uniprot.org/annotation/VAR_037695|||http://purl.uniprot.org/annotation/VAR_037696|||http://purl.uniprot.org/annotation/VAR_037697|||http://purl.uniprot.org/annotation/VAR_037698|||http://purl.uniprot.org/annotation/VAR_078065
http://togogenome.org/gene/9606:PRAMEF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTA0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290162
http://togogenome.org/gene/9606:ABCC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95255                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 6|||Associated with lower plasma triglycerides and higher plasma HDL cholesterol.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in patient with putative diagnosis of PEX; uncertain pathological significance.|||Found in patient with putative diagnosis of PEX; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type.|||Found in patient with putative diagnosis of PEX; uncertain pathological significance; mutant protein is retained in the cytoplasm.|||Found in patient with putative diagnosis of PXE; uncertain pathological significance.|||Found in patient with putative diagnosis of PXE; uncertain pathological significance; localization comparable to wild-type.|||Found in patient with putative diagnosis of PXE; uncertain pathological significance; loss-of-function mutation; localization comparable to wild-type.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=16|||Helical; Name=17|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In GACI2 and PXE; autosomal recessive.|||In GACI2.|||In PXE.|||In PXE; affects protein expression and trafficking; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein.|||In PXE; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein.|||In PXE; autosomal dominant and autosomal recessive.|||In PXE; autosomal dominant and autosomal recessive; abolishes LTC4 and NEM-GS transport.|||In PXE; autosomal dominant and autosomal recessive; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein.|||In PXE; autosomal dominant.|||In PXE; autosomal dominant; abolishes LTC4 and NEM-GS transport.|||In PXE; autosomal dominant; abolishes LTC4 and NEM-GS transport; does not affect plasma membrane localization; does not increase extracellular pyrophosphate levels.|||In PXE; autosomal dominant; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein.|||In PXE; autosomal recessive.|||In PXE; autosomal recessive; affects protein expression and trafficking.|||In PXE; autosomal recessive; affects protein expression and trafficking; expression is reduced to less than 10%, when compared with the WT protein.|||In PXE; autosomal recessive; protein level is 15-20% that of the WT proteins; maturation of glycan chains is not affected indicating normal trafficking from the endoplasmic reticulum to the cell membrane.|||In PXE; does not change protein biosynthesis and folding.|||In PXE; loss-of-function variant; localization comparable to wild-type.|||In PXE; protein level is 15-20% that of the WT proteins; maturation of glycan chains is not affected indicating normal trafficking from the endoplasmic reticulum to the cell membrane.|||In PXE; pseudodominant.|||In PXE; putative autosomal dominant.|||In PXE; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093366|||http://purl.uniprot.org/annotation/VAR_011490|||http://purl.uniprot.org/annotation/VAR_011491|||http://purl.uniprot.org/annotation/VAR_011492|||http://purl.uniprot.org/annotation/VAR_011493|||http://purl.uniprot.org/annotation/VAR_011494|||http://purl.uniprot.org/annotation/VAR_011495|||http://purl.uniprot.org/annotation/VAR_013363|||http://purl.uniprot.org/annotation/VAR_013364|||http://purl.uniprot.org/annotation/VAR_013365|||http://purl.uniprot.org/annotation/VAR_013366|||http://purl.uniprot.org/annotation/VAR_013367|||http://purl.uniprot.org/annotation/VAR_013368|||http://purl.uniprot.org/annotation/VAR_013369|||http://purl.uniprot.org/annotation/VAR_013370|||http://purl.uniprot.org/annotation/VAR_013371|||http://purl.uniprot.org/annotation/VAR_013372|||http://purl.uniprot.org/annotation/VAR_013373|||http://purl.uniprot.org/annotation/VAR_013374|||http://purl.uniprot.org/annotation/VAR_013375|||http://purl.uniprot.org/annotation/VAR_013376|||http://purl.uniprot.org/annotation/VAR_013377|||http://purl.uniprot.org/annotation/VAR_013378|||http://purl.uniprot.org/annotation/VAR_013379|||http://purl.uniprot.org/annotation/VAR_013380|||http://purl.uniprot.org/annotation/VAR_013381|||http://purl.uniprot.org/annotation/VAR_013382|||http://purl.uniprot.org/annotation/VAR_013383|||http://purl.uniprot.org/annotation/VAR_013384|||http://purl.uniprot.org/annotation/VAR_013385|||http://purl.uniprot.org/annotation/VAR_013386|||http://purl.uniprot.org/annotation/VAR_013387|||http://purl.uniprot.org/annotation/VAR_013388|||http://purl.uniprot.org/annotation/VAR_013389|||http://purl.uniprot.org/annotation/VAR_013390|||http://purl.uniprot.org/annotation/VAR_013391|||http://purl.uniprot.org/annotation/VAR_013392|||http://purl.uniprot.org/annotation/VAR_013393|||http://purl.uniprot.org/annotation/VAR_013394|||http://purl.uniprot.org/annotation/VAR_055477|||http://purl.uniprot.org/annotation/VAR_059108|||http://purl.uniprot.org/annotation/VAR_060988|||http://purl.uniprot.org/annotation/VAR_067840|||http://purl.uniprot.org/annotation/VAR_067841|||http://purl.uniprot.org/annotation/VAR_067842|||http://purl.uniprot.org/annotation/VAR_067843|||http://purl.uniprot.org/annotation/VAR_067844|||http://purl.uniprot.org/annotation/VAR_067845|||http://purl.uniprot.org/annotation/VAR_067846|||http://purl.uniprot.org/annotation/VAR_067847|||http://purl.uniprot.org/annotation/VAR_067848|||http://purl.uniprot.org/annotation/VAR_067849|||http://purl.uniprot.org/annotation/VAR_067850|||http://purl.uniprot.org/annotation/VAR_067851|||http://purl.uniprot.org/annotation/VAR_067852|||http://purl.uniprot.org/annotation/VAR_067853|||http://purl.uniprot.org/annotation/VAR_067854|||http://purl.uniprot.org/annotation/VAR_067855|||http://purl.uniprot.org/annotation/VAR_067856|||http://purl.uniprot.org/annotation/VAR_067857|||http://purl.uniprot.org/annotation/VAR_067858|||http://purl.uniprot.org/annotation/VAR_067859|||http://purl.uniprot.org/annotation/VAR_067860|||http://purl.uniprot.org/annotation/VAR_067861|||http://purl.uniprot.org/annotation/VAR_067862|||http://purl.uniprot.org/annotation/VAR_067863|||http://purl.uniprot.org/annotation/VAR_067864|||http://purl.uniprot.org/annotation/VAR_067865|||http://purl.uniprot.org/annotation/VAR_067866|||http://purl.uniprot.org/annotation/VAR_067867|||http://purl.uniprot.org/annotation/VAR_067868|||http://purl.uniprot.org/annotation/VAR_067869|||http://purl.uniprot.org/annotation/VAR_067870|||http://purl.uniprot.org/annotation/VAR_067871|||http://purl.uniprot.org/annotation/VAR_067872|||http://purl.uniprot.org/annotation/VAR_067873|||http://purl.uniprot.org/annotation/VAR_067874|||http://purl.uniprot.org/annotation/VAR_067875|||http://purl.uniprot.org/annotation/VAR_067876|||http://purl.uniprot.org/annotation/VAR_067877|||http://purl.uniprot.org/annotation/VAR_067878|||http://purl.uniprot.org/annotation/VAR_067879|||http://purl.uniprot.org/annotation/VAR_067880|||http://purl.uniprot.org/annotation/VAR_067881|||http://purl.uniprot.org/annotation/VAR_067882|||http://purl.uniprot.org/annotation/VAR_067883|||http://purl.uniprot.org/annotation/VAR_067884|||http://purl.uniprot.org/annotation/VAR_067885|||http://purl.uniprot.org/annotation/VAR_067886|||http://purl.uniprot.org/annotation/VAR_067887|||http://purl.uniprot.org/annotation/VAR_067888|||http://purl.uniprot.org/annotation/VAR_067889|||http://purl.uniprot.org/annotation/VAR_067890|||http://purl.uniprot.org/annotation/VAR_067891|||http://purl.uniprot.org/annotation/VAR_067892|||http://purl.uniprot.org/annotation/VAR_067893|||http://purl.uniprot.org/annotation/VAR_067894|||http://purl.uniprot.org/annotation/VAR_067895|||http://purl.uniprot.org/annotation/VAR_067896|||http://purl.uniprot.org/annotation/VAR_067897|||http://purl.uniprot.org/annotation/VAR_067898|||http://purl.uniprot.org/annotation/VAR_067899|||http://purl.uniprot.org/annotation/VAR_067900|||http://purl.uniprot.org/annotation/VAR_067901|||http://purl.uniprot.org/annotation/VAR_067902|||http://purl.uniprot.org/annotation/VAR_067903|||http://purl.uniprot.org/annotation/VAR_067904|||http://purl.uniprot.org/annotation/VAR_067905|||http://purl.uniprot.org/annotation/VAR_067906|||http://purl.uniprot.org/annotation/VAR_067907|||http://purl.uniprot.org/annotation/VAR_067908|||http://purl.uniprot.org/annotation/VAR_067909|||http://purl.uniprot.org/annotation/VAR_072803|||http://purl.uniprot.org/annotation/VAR_072804|||http://purl.uniprot.org/annotation/VAR_072805|||http://purl.uniprot.org/annotation/VAR_072806|||http://purl.uniprot.org/annotation/VAR_072807|||http://purl.uniprot.org/annotation/VAR_072808|||http://purl.uniprot.org/annotation/VAR_072809|||http://purl.uniprot.org/annotation/VAR_072810|||http://purl.uniprot.org/annotation/VAR_072811|||http://purl.uniprot.org/annotation/VAR_072812|||http://purl.uniprot.org/annotation/VAR_072813|||http://purl.uniprot.org/annotation/VSP_047315|||http://purl.uniprot.org/annotation/VSP_047316|||http://purl.uniprot.org/annotation/VSP_057077|||http://purl.uniprot.org/annotation/VSP_057078
http://togogenome.org/gene/9606:RPS26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62854                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In DBA10.|||Phosphoserine|||Pro residues|||Removed|||Small ribosomal subunit protein eS26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204509|||http://purl.uniprot.org/annotation/VAR_063580|||http://purl.uniprot.org/annotation/VAR_063581
http://togogenome.org/gene/9606:BICD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G01                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with RAB6A|||Polar residues|||Protein bicaudal D homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205357|||http://purl.uniprot.org/annotation/VAR_069060|||http://purl.uniprot.org/annotation/VSP_007961|||http://purl.uniprot.org/annotation/VSP_007962|||http://purl.uniprot.org/annotation/VSP_007963|||http://purl.uniprot.org/annotation/VSP_007964|||http://purl.uniprot.org/annotation/VSP_045637|||http://purl.uniprot.org/annotation/VSP_045638
http://togogenome.org/gene/9606:MYOZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Myozenin-1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111095
http://togogenome.org/gene/9606:PROM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R879|||http://purl.uniprot.org/uniprot/Q8N271                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prominin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331239|||http://purl.uniprot.org/annotation/PRO_5002781818|||http://purl.uniprot.org/annotation/VAR_042749|||http://purl.uniprot.org/annotation/VSP_033148|||http://purl.uniprot.org/annotation/VSP_033149
http://togogenome.org/gene/9606:AMY1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DTE7|||http://purl.uniprot.org/uniprot/P0DTE8|||http://purl.uniprot.org/uniprot/P0DUB6|||http://purl.uniprot.org/uniprot/Q6NSB3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-amylase|||Alpha-amylase 1A|||Alpha-amylase 1B|||Alpha-amylase 1C|||Alpha-amylase C-terminal|||Deamidated asparagine; partial|||Deamidated asparagine; partial; alternate|||Glycosyl hydrolase family 13 catalytic|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor|||Pyrrolidone carboxylic acid|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001401|||http://purl.uniprot.org/annotation/PRO_0000450820|||http://purl.uniprot.org/annotation/PRO_0000450821|||http://purl.uniprot.org/annotation/PRO_5013198096
http://togogenome.org/gene/9606:GZMK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49863                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Granzyme K|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027415|||http://purl.uniprot.org/annotation/PRO_0000027416
http://togogenome.org/gene/9606:DAZAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15038                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with NEDD4. Abolishes NEDD4-mediated ubiquitination.|||Abolishes ubiquitin-mediated degradation. Does not affect nuclear localization.|||DAZ-associated protein 2|||Disordered|||Does not affect ubiquitin-mediated degradation. Abolishes nuclear localization with the protein located in the cytoplasm.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of phosphorylation by HIPK2.|||PPAY|||Phosphoserine; by HIPK2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079788|||http://purl.uniprot.org/annotation/VAR_061639|||http://purl.uniprot.org/annotation/VSP_042773|||http://purl.uniprot.org/annotation/VSP_045678|||http://purl.uniprot.org/annotation/VSP_045679|||http://purl.uniprot.org/annotation/VSP_046764|||http://purl.uniprot.org/annotation/VSP_055181
http://togogenome.org/gene/9606:UBE2H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IU20|||http://purl.uniprot.org/uniprot/A4D1L5|||http://purl.uniprot.org/uniprot/P62256                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||In isoform 2.|||N6-acetyllysine|||UBC core|||Ubiquitin-conjugating enzyme E2 H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082486|||http://purl.uniprot.org/annotation/VSP_044580
http://togogenome.org/gene/9606:ARFRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13795                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-related protein 1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207487|||http://purl.uniprot.org/annotation/VAR_036559|||http://purl.uniprot.org/annotation/VSP_043531|||http://purl.uniprot.org/annotation/VSP_057570|||http://purl.uniprot.org/annotation/VSP_057571|||http://purl.uniprot.org/annotation/VSP_057572
http://togogenome.org/gene/9606:SLC25A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DX16|||http://purl.uniprot.org/uniprot/D9HTE9|||http://purl.uniprot.org/uniprot/P53007                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In CMS23; reduced rates of citrate transport.|||In D2L2AD.|||In D2L2AD; abolishes citrate transport.|||In D2L2AD; disease phenotype may include decreased activity of mitochondrial respiratory chain complex V.|||In D2L2AD; no protein detected by Western blot in patient fibroblasts; severely reduced rates of citrate transport.|||In D2L2AD; reduced rates of citrate transport.|||In D2L2AD; severely reduced rates of citrate transport.|||In D2L2AD; unknown pathological significance; very mild decrease of citrate transport rates.|||Phosphoserine|||Removed in mature form|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Tricarboxylate transport protein, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019262|||http://purl.uniprot.org/annotation/PRO_0000456575|||http://purl.uniprot.org/annotation/VAR_069490|||http://purl.uniprot.org/annotation/VAR_069491|||http://purl.uniprot.org/annotation/VAR_069492|||http://purl.uniprot.org/annotation/VAR_069493|||http://purl.uniprot.org/annotation/VAR_069494|||http://purl.uniprot.org/annotation/VAR_069495|||http://purl.uniprot.org/annotation/VAR_069496|||http://purl.uniprot.org/annotation/VAR_069497|||http://purl.uniprot.org/annotation/VAR_077511|||http://purl.uniprot.org/annotation/VAR_081661|||http://purl.uniprot.org/annotation/VAR_081662|||http://purl.uniprot.org/annotation/VAR_081663|||http://purl.uniprot.org/annotation/VAR_081664|||http://purl.uniprot.org/annotation/VAR_081665|||http://purl.uniprot.org/annotation/VAR_081666|||http://purl.uniprot.org/annotation/VAR_081667|||http://purl.uniprot.org/annotation/VAR_081668|||http://purl.uniprot.org/annotation/VAR_081669|||http://purl.uniprot.org/annotation/VAR_081670
http://togogenome.org/gene/9606:CRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02741                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-reactive protein|||C-reactive protein(1-205)|||In isoform 2.|||Pentraxin (PTX)|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023526|||http://purl.uniprot.org/annotation/PRO_0000023527|||http://purl.uniprot.org/annotation/VSP_004656
http://togogenome.org/gene/9606:HEATR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WZ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT repeat-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254129|||http://purl.uniprot.org/annotation/VAR_028817|||http://purl.uniprot.org/annotation/VAR_028818|||http://purl.uniprot.org/annotation/VAR_028819
http://togogenome.org/gene/9606:EIF5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60841|||http://purl.uniprot.org/uniprot/Q8N5A0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by viral protease 3C of poliovirus, Coxsackievirus B3 and Human rhinovirus 14|||Acidic residues|||Basic and acidic residues|||Disordered|||Disruption of contacts with eIF1A (EIF1AX); when associated with 1188-E-E-1189 and 1218-R-R-1219.|||Disruption of contacts with eIF1A (EIF1AX); when associated with 1188-E-R-1189 and E-1199.|||Disruption of contacts with eIF1A (EIF1AX); when associated with E-1199 and 1218-R-R-1219.|||Disruption of contacts with the Met-tRNA acceptor stem; when associated with A-1105.|||Disruption of contacts with the Met-tRNA acceptor stem; when associated with A-1174.|||Eukaryotic translation initiation factor 5B|||G1|||G2|||G3|||G4|||G5|||Loss of activity in vivo. Partial activity in vitro.|||Loss of activity in vivo. Retains full activity in vitro.|||Loss of activity; both in vivo and in vitro.|||Loss of activity; both in vivo and in vitro. Loss of EIF5B release from the 80S initiation complex, certainly due to loss of ability to hydrolyze GTP.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137294|||http://purl.uniprot.org/annotation/VAR_055954|||http://purl.uniprot.org/annotation/VAR_055955|||http://purl.uniprot.org/annotation/VAR_060587
http://togogenome.org/gene/9606:DPH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2P9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Diphthine methyl ester synthase|||In NEDSFF; decreased function in diphthamide biosynthesis shown in a yeast assay system.|||In NEDSFF; loss of function in diphthamide biosynthesis shown in a yeast assay system.|||In NEDSFF; results in multisystem abnormalities in a homozygous mouse knockin model; decreased function in diphthamide biosynthesis shown in a yeast assay system.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156133|||http://purl.uniprot.org/annotation/VAR_087842|||http://purl.uniprot.org/annotation/VAR_087843|||http://purl.uniprot.org/annotation/VAR_087844|||http://purl.uniprot.org/annotation/VSP_008508|||http://purl.uniprot.org/annotation/VSP_008509|||http://purl.uniprot.org/annotation/VSP_008510|||http://purl.uniprot.org/annotation/VSP_008511|||http://purl.uniprot.org/annotation/VSP_043444
http://togogenome.org/gene/9606:INSYN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2T9L4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Inhibitory synaptic factor 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337045
http://togogenome.org/gene/9606:ELAVL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRX1|||http://purl.uniprot.org/uniprot/Q12926                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ELAV-like protein 2|||In isoform 2.|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081579|||http://purl.uniprot.org/annotation/VSP_005788
http://togogenome.org/gene/9606:PEX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00628|||http://purl.uniprot.org/uniprot/Q6FGN1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Impaired binding to cargo proteins containing a PTS2 peroxisomal targeting signal.|||Impaired interaction with PEX5, leading to decreased peroxisomal import of proteins containing a PTS2 peroxisomal targeting signal.|||In PBD9B.|||In RCDP1.|||In RCDP1; unknown pathological significance.|||In isoform 2.|||Peroxisomal targeting signal 2 receptor|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051116|||http://purl.uniprot.org/annotation/VAR_007725|||http://purl.uniprot.org/annotation/VAR_007726|||http://purl.uniprot.org/annotation/VAR_016810|||http://purl.uniprot.org/annotation/VSP_056393
http://togogenome.org/gene/9606:IL1R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27930                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Contains proteolytic cleavage site|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform Short.|||Interleukin-1 receptor type 2, membrane form|||Interleukin-1 receptor type 2, soluble form|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015439|||http://purl.uniprot.org/annotation/PRO_0000415348|||http://purl.uniprot.org/annotation/VAR_019132|||http://purl.uniprot.org/annotation/VAR_019133|||http://purl.uniprot.org/annotation/VSP_042222
http://togogenome.org/gene/9606:SULT1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43704                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Proton acceptor|||Reduces Vmax with p-nitrophenol as substrate; binds to adenosine 3',5'-bisphosphate with a dissociation constant (Kd) value increases 4-fold compared with wild-type; binds to PAPS with a dissociation constant (Kd) value similar to wild-type.|||Sulfotransferase 1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085161|||http://purl.uniprot.org/annotation/VAR_085176
http://togogenome.org/gene/9606:EME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Crossover junction endonuclease EME1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223630|||http://purl.uniprot.org/annotation/VAR_025337|||http://purl.uniprot.org/annotation/VAR_025338|||http://purl.uniprot.org/annotation/VAR_025339|||http://purl.uniprot.org/annotation/VAR_055708|||http://purl.uniprot.org/annotation/VAR_055709|||http://purl.uniprot.org/annotation/VAR_055710|||http://purl.uniprot.org/annotation/VSP_017284
http://togogenome.org/gene/9606:ZFAND4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8Q5|||http://purl.uniprot.org/uniprot/J3KPC0|||http://purl.uniprot.org/uniprot/Q86WR3|||http://purl.uniprot.org/uniprot/Q86XD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  AN1-type|||AN1-type zinc finger protein 4|||Disordered|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269892|||http://purl.uniprot.org/annotation/VAR_053773|||http://purl.uniprot.org/annotation/VAR_053774|||http://purl.uniprot.org/annotation/VAR_062163
http://togogenome.org/gene/9606:CAPZA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47755                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  F-actin-capping protein subunit alpha-2|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208627|||http://purl.uniprot.org/annotation/VSP_053871|||http://purl.uniprot.org/annotation/VSP_053872
http://togogenome.org/gene/9606:R3HDM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D70                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||R3H|||R3H domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281431
http://togogenome.org/gene/9606:SAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10523                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In CSNBO1.|||In RP96.|||Phosphothreonine|||S-arrestin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205186|||http://purl.uniprot.org/annotation/VAR_008263|||http://purl.uniprot.org/annotation/VAR_008264|||http://purl.uniprot.org/annotation/VAR_008265|||http://purl.uniprot.org/annotation/VAR_008266|||http://purl.uniprot.org/annotation/VAR_008267|||http://purl.uniprot.org/annotation/VAR_008268|||http://purl.uniprot.org/annotation/VAR_033524|||http://purl.uniprot.org/annotation/VAR_048333|||http://purl.uniprot.org/annotation/VAR_088068|||http://purl.uniprot.org/annotation/VAR_088069|||http://purl.uniprot.org/annotation/VAR_088070|||http://purl.uniprot.org/annotation/VAR_088071|||http://purl.uniprot.org/annotation/VAR_088072
http://togogenome.org/gene/9606:LRTM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N967                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat and transmembrane domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263686|||http://purl.uniprot.org/annotation/VAR_061679
http://togogenome.org/gene/9606:FRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14331                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Nuclear localization signal|||Protein FRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220767|||http://purl.uniprot.org/annotation/VAR_049105
http://togogenome.org/gene/9606:H2BC26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N257                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 3-B|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071837
http://togogenome.org/gene/9606:CHUK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15111                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  (Microbial infection) O-acetylthreonine; by Yersinia YopJ|||Full activation.|||Inhibitor of nuclear factor kappa-B kinase subunit alpha|||Leucine-zipper|||Loss of autophosphorylation.|||Loss of kinase activity.|||Loss of phosphorylation and decrease of kinase activity.|||Loss of phosphorylation and of activity.|||NEMO-binding|||No change in phosphorylation.|||Phosphoserine; by MAP3K14|||Phosphoserine; by SGK1|||Phosphothreonine; by PKB/AKT1 and SGK1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086011|||http://purl.uniprot.org/annotation/VAR_021359|||http://purl.uniprot.org/annotation/VAR_040565|||http://purl.uniprot.org/annotation/VAR_040566
http://togogenome.org/gene/9606:MYPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX60|||http://purl.uniprot.org/uniprot/Q86TC9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||In CMD1KK and CMH22; results in sarcomere disorganization and premature cell death.|||In CMD1KK.|||In CMD1KK; results in sarcomere disorganization and premature cell death.|||In CMD1KK; unknown pathological significance.|||In CMH22 and CMD1KK; perturbs MYPN nuclear shuttling and leads to disruption of intercalated disks.|||In CMH22.|||In isoform 2.|||Interaction with ACTN|||Interaction with CARP|||Interaction with NEB|||Myopalladin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240489|||http://purl.uniprot.org/annotation/VAR_026727|||http://purl.uniprot.org/annotation/VAR_026728|||http://purl.uniprot.org/annotation/VAR_026729|||http://purl.uniprot.org/annotation/VAR_049911|||http://purl.uniprot.org/annotation/VAR_049912|||http://purl.uniprot.org/annotation/VAR_049913|||http://purl.uniprot.org/annotation/VAR_069642|||http://purl.uniprot.org/annotation/VAR_069643|||http://purl.uniprot.org/annotation/VAR_069644|||http://purl.uniprot.org/annotation/VAR_069645|||http://purl.uniprot.org/annotation/VAR_069646|||http://purl.uniprot.org/annotation/VAR_069647|||http://purl.uniprot.org/annotation/VAR_069648|||http://purl.uniprot.org/annotation/VAR_069649|||http://purl.uniprot.org/annotation/VAR_069650|||http://purl.uniprot.org/annotation/VAR_069651|||http://purl.uniprot.org/annotation/VAR_069652|||http://purl.uniprot.org/annotation/VAR_069653|||http://purl.uniprot.org/annotation/VAR_069654|||http://purl.uniprot.org/annotation/VAR_069655|||http://purl.uniprot.org/annotation/VAR_069656|||http://purl.uniprot.org/annotation/VAR_069657|||http://purl.uniprot.org/annotation/VAR_069658|||http://purl.uniprot.org/annotation/VAR_069659|||http://purl.uniprot.org/annotation/VAR_069660|||http://purl.uniprot.org/annotation/VAR_069661|||http://purl.uniprot.org/annotation/VAR_069662|||http://purl.uniprot.org/annotation/VAR_069663|||http://purl.uniprot.org/annotation/VAR_074186|||http://purl.uniprot.org/annotation/VSP_019384|||http://purl.uniprot.org/annotation/VSP_019385
http://togogenome.org/gene/9606:ZAP70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43403                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes kinase activity.|||Decreases interaction with phosphorylated CD247; when associated with K-190.|||Decreases interaction with phosphorylated CD247; when associated with K-37.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs kinase activity.|||In ADMIO2; decreases interaction with phosphorylated CD247; decreases ZAP70 phosphorylation; no effect on subcellular localization of CD69 at the cell surface.|||In ADMIO2; no effect on interaction with phosphorylated CD247; increases TCR-induced Y-319 and Y-493 phosphorylation of ZAP70 and phosphorylation of LAT and LCP2; increases subcellular localization of CD69 at the cell surface; weakly decreases autoinhibition conformation.|||In IMD48.|||In a head and neck squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Increased constitutive kinase activity.|||Increased constitutive kinase activity; when associated with F-315.|||Increased constitutive kinase activity; when associated with F-315. About 80% loss of TCR-induced NFAT activation.|||Increased constitutive kinase activity; when associated with F-319.|||Increased constitutive kinase activity; when associated with F-319. About 75% loss of CD247/CD3Z-binding in stimulated TCR and complete loss of VAV1 interaction.|||Increased kinase activity after activation by LCK.|||Increases constitutive kinase activity on LAT phosphorylation, strongly increases subcellular localization of CD69 at the cell surface and decreases autoinhibition conformation.|||Increases kinase activity.|||Increases strongly constitutive kinase activity on LAT phosphorylation.|||Induces constitutive TCR stimulation-independent NFAT induction.|||Interdomain A|||Interdomain B|||N6-acetyllysine|||No effect on ubiquitination.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LCK|||Polar residues|||Protein kinase|||Proton acceptor|||SH2 1|||SH2 2|||Strongly decreased ubiquitination.|||Tyrosine-protein kinase ZAP-70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088168|||http://purl.uniprot.org/annotation/VAR_006351|||http://purl.uniprot.org/annotation/VAR_015538|||http://purl.uniprot.org/annotation/VAR_038688|||http://purl.uniprot.org/annotation/VAR_041846|||http://purl.uniprot.org/annotation/VAR_041847|||http://purl.uniprot.org/annotation/VAR_041848|||http://purl.uniprot.org/annotation/VAR_041849|||http://purl.uniprot.org/annotation/VAR_065623|||http://purl.uniprot.org/annotation/VAR_065624|||http://purl.uniprot.org/annotation/VAR_065625|||http://purl.uniprot.org/annotation/VAR_065626|||http://purl.uniprot.org/annotation/VAR_077137|||http://purl.uniprot.org/annotation/VAR_077138|||http://purl.uniprot.org/annotation/VSP_031156|||http://purl.uniprot.org/annotation/VSP_031157|||http://purl.uniprot.org/annotation/VSP_031158
http://togogenome.org/gene/9606:INTS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9B9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Integrator complex subunit 5|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259541
http://togogenome.org/gene/9606:SDHAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX18                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In PGL2; abolishes interaction with SDHA and flavination of SDHA.|||Mitochondrion|||Succinate dehydrogenase assembly factor 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294357|||http://purl.uniprot.org/annotation/VAR_058705
http://togogenome.org/gene/9606:TIMM23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SRD1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial import inner membrane translocase subunit Tim23B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349114|||http://purl.uniprot.org/annotation/VSP_060625
http://togogenome.org/gene/9606:CFP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4I5|||http://purl.uniprot.org/uniprot/P27918                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Decreases Complement C3 beta chain binding.|||Disordered|||In PFD; type I.|||In PFD; type II.|||In PFD; type II; decreases expression, inhibits oligomerization and fails to stimulate bacteriolysis; does not affect binding to Complement C3 beta chain.|||In PFD; type II; inhibits secretion and oligomerization.|||In PFD; type II; significantly decreases Complement C3 beta chain binding.|||In PFD; type III; significantly decreases Complement C3 beta chain binding.|||In a breast cancer sample; somatic mutation.|||Inhibits oligomerization.|||Inhibits oligomerization; when associated with A-47 and A-275.|||Inhibits oligomerization; when associated with A-47 and A-58.|||Inhibits oligomerization; when associated with A-58 and A-275.|||Interaction with Complement C3 beta chain|||N-linked (GlcNAc...) (complex) asparagine|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||Properdin|||Significantly decreases Complement C3 beta chain binding.|||Slightly decreases Complement C3 beta chain binding.|||TSP type-1 0|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035863|||http://purl.uniprot.org/annotation/PRO_5014239315|||http://purl.uniprot.org/annotation/VAR_002002|||http://purl.uniprot.org/annotation/VAR_002003|||http://purl.uniprot.org/annotation/VAR_002004|||http://purl.uniprot.org/annotation/VAR_013139|||http://purl.uniprot.org/annotation/VAR_020395|||http://purl.uniprot.org/annotation/VAR_020396|||http://purl.uniprot.org/annotation/VAR_020397|||http://purl.uniprot.org/annotation/VAR_035813|||http://purl.uniprot.org/annotation/VAR_083038|||http://purl.uniprot.org/annotation/VAR_083039
http://togogenome.org/gene/9606:GABRD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K496|||http://purl.uniprot.org/uniprot/O14764                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with childhood onset epileptic encephalopathy; unknown pathological significance.|||Gamma-aminobutyric acid receptor subunit delta|||Helical|||In GEFSP5; reduced receptor current amplitudes.|||In GEFSP5; unknown pathological significance; does not affect receptor current amplitudes.|||Is a risk factor for epilepsy; reduced receptor current amplitudes.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000468|||http://purl.uniprot.org/annotation/PRO_5022272397|||http://purl.uniprot.org/annotation/VAR_043151|||http://purl.uniprot.org/annotation/VAR_043152|||http://purl.uniprot.org/annotation/VAR_043153|||http://purl.uniprot.org/annotation/VAR_078225|||http://purl.uniprot.org/annotation/VAR_079270
http://togogenome.org/gene/9606:PAPOLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWT3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with RNA|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Poly(A) polymerase gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051624|||http://purl.uniprot.org/annotation/VSP_054379
http://togogenome.org/gene/9606:MEOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50221                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein MOX-1|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049195|||http://purl.uniprot.org/annotation/VAR_049584|||http://purl.uniprot.org/annotation/VSP_043340|||http://purl.uniprot.org/annotation/VSP_046700
http://togogenome.org/gene/9606:GRIN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A890YTL4|||http://purl.uniprot.org/uniprot/Q12879|||http://purl.uniprot.org/uniprot/Q547U9|||http://purl.uniprot.org/uniprot/Q59EW6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Changed glutamate-gated calcium ion channel activity characterized by accelerated response activation time and increased desensitization.|||Changed glutamate-gated calcium ion channel activity characterized by increased desensitization.|||Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course.|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Found in a cutaneous malignant melanoma sample.|||Found in a cutaneous malignant melanoma sample; somatic mutation.|||Found in a cutaneous malignant melanoma sample; somatic mutation; also found in a patient with benign epilepsy with centrotemporal spike.|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with autism; unknown pathological significance.|||Found in a patient with continuous spike-wave discharges during slow-wave sleep; also found in a patient with drug-resistant focal epilepsy; also found in a cutaneous malignant melanoma sample as somatic mutation; unknown pathological significance.|||Found in a patient with neonatal onset epileptic encephalopathy; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||Functional determinant of NMDA receptors|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 2A|||Helical|||In FESD.|||In FESD; affects receptor kinetics.|||In FESD; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability.|||In FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by affected receptor kinetics.|||In FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and decreased open probability.|||In FESD; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency.|||In FESD; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by drastically decreased glutamate agonist potency, decreased glycine agonist potency, reduced amplitude of current response, shortened synaptic-like response time course, decreased channel open probability and enhanced sensitivity to negative allosteric modulators.|||In FESD; decreased protein abundance; decreased localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol.|||In FESD; decreased protein abundance; loss of localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased glycine potency.|||In FESD; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol.|||In FESD; gain-of-function characterized by enhanced agonist potency, reduced sensitivity to endogenous negative inhibitors, prolonged synaptic-like response time course, increased single-channel mean open time and increased channel open probability.|||In FESD; increase in receptor response to agonists; decrease in the actions of endogenous negative modulators; increase in channel open probability; prolonged deactivation time course.|||In FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency.|||In FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency with delay in rise time and slower deactivation time course.|||In FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency.|||In FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency and decreased open probability.|||In FESD; no effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency.|||In FESD; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity.|||In FESD; results in reduced high-affinity zinc mediated inhibition.|||In FESD; the mutant receptor has decreased calcium permeability; shows a dominant-negative effect.|||In FESD; unknown pathological significance.|||In isoform 2.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||No effect on localization to the cell membrane. Changed glutamate-gated calcium ion channel activity characterized by decreased response amplitude and changed desensitization without effect on response rise time or deactivation time course.|||No effect on localization to the cell membrane. Changed glutamate-gated calcium ion channel activity characterized by increased desensitization.|||No effect on localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate potency.|||PDZ-binding|||Phosphoserine|||Polar residues|||Pore-forming|||Probable disease-associated variant found in a patient with schizophrenia. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011573|||http://purl.uniprot.org/annotation/PRO_5014309654|||http://purl.uniprot.org/annotation/PRO_5033113188|||http://purl.uniprot.org/annotation/VAR_010938|||http://purl.uniprot.org/annotation/VAR_065899|||http://purl.uniprot.org/annotation/VAR_067725|||http://purl.uniprot.org/annotation/VAR_067726|||http://purl.uniprot.org/annotation/VAR_067727|||http://purl.uniprot.org/annotation/VAR_067728|||http://purl.uniprot.org/annotation/VAR_067729|||http://purl.uniprot.org/annotation/VAR_067730|||http://purl.uniprot.org/annotation/VAR_067731|||http://purl.uniprot.org/annotation/VAR_067732|||http://purl.uniprot.org/annotation/VAR_067733|||http://purl.uniprot.org/annotation/VAR_067734|||http://purl.uniprot.org/annotation/VAR_067735|||http://purl.uniprot.org/annotation/VAR_067736|||http://purl.uniprot.org/annotation/VAR_067737|||http://purl.uniprot.org/annotation/VAR_067738|||http://purl.uniprot.org/annotation/VAR_067739|||http://purl.uniprot.org/annotation/VAR_067740|||http://purl.uniprot.org/annotation/VAR_067741|||http://purl.uniprot.org/annotation/VAR_067742|||http://purl.uniprot.org/annotation/VAR_067743|||http://purl.uniprot.org/annotation/VAR_067744|||http://purl.uniprot.org/annotation/VAR_067745|||http://purl.uniprot.org/annotation/VAR_067746|||http://purl.uniprot.org/annotation/VAR_067747|||http://purl.uniprot.org/annotation/VAR_067748|||http://purl.uniprot.org/annotation/VAR_067749|||http://purl.uniprot.org/annotation/VAR_067750|||http://purl.uniprot.org/annotation/VAR_067751|||http://purl.uniprot.org/annotation/VAR_067752|||http://purl.uniprot.org/annotation/VAR_067753|||http://purl.uniprot.org/annotation/VAR_069382|||http://purl.uniprot.org/annotation/VAR_069383|||http://purl.uniprot.org/annotation/VAR_070345|||http://purl.uniprot.org/annotation/VAR_070346|||http://purl.uniprot.org/annotation/VAR_070347|||http://purl.uniprot.org/annotation/VAR_070348|||http://purl.uniprot.org/annotation/VAR_070349|||http://purl.uniprot.org/annotation/VAR_070350|||http://purl.uniprot.org/annotation/VAR_070351|||http://purl.uniprot.org/annotation/VAR_070352|||http://purl.uniprot.org/annotation/VAR_070353|||http://purl.uniprot.org/annotation/VAR_070354|||http://purl.uniprot.org/annotation/VAR_070355|||http://purl.uniprot.org/annotation/VAR_070356|||http://purl.uniprot.org/annotation/VAR_070357|||http://purl.uniprot.org/annotation/VAR_070358|||http://purl.uniprot.org/annotation/VAR_070359|||http://purl.uniprot.org/annotation/VAR_070360|||http://purl.uniprot.org/annotation/VAR_070361|||http://purl.uniprot.org/annotation/VAR_070362|||http://purl.uniprot.org/annotation/VAR_070363|||http://purl.uniprot.org/annotation/VAR_070364|||http://purl.uniprot.org/annotation/VAR_070365|||http://purl.uniprot.org/annotation/VAR_070366|||http://purl.uniprot.org/annotation/VAR_070367|||http://purl.uniprot.org/annotation/VAR_070368|||http://purl.uniprot.org/annotation/VAR_070369|||http://purl.uniprot.org/annotation/VAR_070370|||http://purl.uniprot.org/annotation/VAR_070371|||http://purl.uniprot.org/annotation/VAR_070372|||http://purl.uniprot.org/annotation/VAR_070373|||http://purl.uniprot.org/annotation/VAR_070374|||http://purl.uniprot.org/annotation/VAR_071624|||http://purl.uniprot.org/annotation/VAR_071625|||http://purl.uniprot.org/annotation/VAR_071626|||http://purl.uniprot.org/annotation/VAR_071627|||http://purl.uniprot.org/annotation/VAR_071628|||http://purl.uniprot.org/annotation/VAR_072750|||http://purl.uniprot.org/annotation/VAR_078109|||http://purl.uniprot.org/annotation/VAR_078110|||http://purl.uniprot.org/annotation/VAR_078111|||http://purl.uniprot.org/annotation/VAR_078690|||http://purl.uniprot.org/annotation/VAR_079929|||http://purl.uniprot.org/annotation/VAR_079930|||http://purl.uniprot.org/annotation/VAR_079931|||http://purl.uniprot.org/annotation/VAR_079932|||http://purl.uniprot.org/annotation/VAR_079933|||http://purl.uniprot.org/annotation/VAR_079934|||http://purl.uniprot.org/annotation/VAR_079935|||http://purl.uniprot.org/annotation/VAR_079936|||http://purl.uniprot.org/annotation/VAR_079937|||http://purl.uniprot.org/annotation/VAR_079938|||http://purl.uniprot.org/annotation/VAR_079939|||http://purl.uniprot.org/annotation/VAR_079940|||http://purl.uniprot.org/annotation/VAR_079941|||http://purl.uniprot.org/annotation/VAR_079942|||http://purl.uniprot.org/annotation/VSP_044300
http://togogenome.org/gene/9606:ATOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00244                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Copper transport protein ATOX1|||HMA|||Has no overall effect on Cu(+)-bridged heterodimer formation with ATP7A.|||Impairs Cu(+)-bridged heterodimer formation with ATP7A.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212537
http://togogenome.org/gene/9606:KLK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92876                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Cleavage; by autolysis|||In isoform 2.|||In isoform 3.|||Kallikrein-6|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027940|||http://purl.uniprot.org/annotation/PRO_0000027941|||http://purl.uniprot.org/annotation/VAR_061776|||http://purl.uniprot.org/annotation/VSP_034403|||http://purl.uniprot.org/annotation/VSP_034404|||http://purl.uniprot.org/annotation/VSP_034405
http://togogenome.org/gene/9606:MYCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12524                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Leucine-zipper|||Pro residues|||Protein L-Myc|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127333|||http://purl.uniprot.org/annotation/VAR_027802|||http://purl.uniprot.org/annotation/VSP_015539|||http://purl.uniprot.org/annotation/VSP_015540|||http://purl.uniprot.org/annotation/VSP_053766
http://togogenome.org/gene/9606:XPO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V2Y6|||http://purl.uniprot.org/uniprot/A0A7I2V461|||http://purl.uniprot.org/uniprot/A0A7I2V6B9|||http://purl.uniprot.org/uniprot/B3KWD0|||http://purl.uniprot.org/uniprot/O14980                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-554.|||Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-554. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525.|||Abolishes Ran binding activity both in absence or presence of cargo.|||Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo.|||Does not abolish Ran binding activity and nuclear export complex formation.|||Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568.|||Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572.|||Does not abolish Rex-mediated mRNA export.|||Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export.|||Enhances Ran binding activity and does not abolish nuclear export complex formation. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-561. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-568 and A-572.|||Enhances Ran binding activity and does not abolish nuclear export complex formation. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-583. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-553.|||Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-590. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-513 and A-554.|||Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590.|||Enhances Ran binding activity; when associated with A-590.|||Exportin-1|||Exportin-1 C-terminal|||HEAT 1|||HEAT 10|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Importin N-terminal|||Interaction with HIV-1 Rev|||Interaction with RANBP3|||Interaction with Ran and nuclear export complex formation|||N6-acetyllysine|||Necessary for HTLV-1 Rex multimerization|||Necessary for HTLV-1 Rex-mediated mRNA export|||Partially abolishes Ran binding activity and does not abolish nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-561. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-513.|||Partially restores Ran binding activity in presence of cargo.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export.|||Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with S-414. Abolishes Rex multimerization; when associated with S-414.|||Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with T-411. Abolishes Rex multimerization; when associated with T-411.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204705
http://togogenome.org/gene/9606:SLC25A53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9E4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271791
http://togogenome.org/gene/9606:PLCB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00722|||http://purl.uniprot.org/uniprot/Q59F77|||http://purl.uniprot.org/uniprot/Q9BVT6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In isoform 2.|||In isoform 3.|||PI-PLC X-box|||PI-PLC Y-box|||PLC-beta PH|||Phosphoserine|||Polar residues|||Strongly reduces interaction with RAC1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088489|||http://purl.uniprot.org/annotation/VAR_047509|||http://purl.uniprot.org/annotation/VAR_047510|||http://purl.uniprot.org/annotation/VAR_047511|||http://purl.uniprot.org/annotation/VAR_047512|||http://purl.uniprot.org/annotation/VAR_047513|||http://purl.uniprot.org/annotation/VSP_035770|||http://purl.uniprot.org/annotation/VSP_054490
http://togogenome.org/gene/9606:IL17RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In IMD51; results in complete loss of expression and loss-of-function.|||In isoform 2.|||Interleukin-17 receptor A|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011030|||http://purl.uniprot.org/annotation/VAR_027966|||http://purl.uniprot.org/annotation/VAR_027967|||http://purl.uniprot.org/annotation/VAR_049176|||http://purl.uniprot.org/annotation/VAR_083722|||http://purl.uniprot.org/annotation/VSP_053496
http://togogenome.org/gene/9606:EFHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2CKC5|||http://purl.uniprot.org/uniprot/Q5JVL4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Associated with susceptibility to JAE1.|||Basic and acidic residues|||Benign variant; no effect on cell death; binds to CACNA1E.|||DM10|||DM10 1|||DM10 2|||DM10 3|||Disordered|||EF-hand|||EF-hand domain-containing protein 1|||In EJM1.|||In EJM1; associated with H-221; reduces substantially the cell death effect; reduces partly the calcium influx; binds to CACNA1E.|||In EJM1; associated with T-77; reduces substantially the cell death effect; reduces partly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration.|||In EJM1; no effect on protein expression; defective mitotic spindle organization; defective cytokinesis.|||In EJM1; no effect on protein expression; no effect on the spindle pole localization; defective mitotic spindle organization; defective cytokinesis.|||In EJM1; reduces substantially the cell death effect; reduces partly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration.|||In EJM1; uncertain pathological significance; also found at homozygosity in neonatal intractable epilepsy; reduces substantially the cell death effect; reduces significantly the calcium influx; normally binds to CACNA1E; does not affect subcellular location; results in impaired cell migration.|||In EJM1; unknown pathological significance.|||In a sporadic case of unclassified epilepsy.|||In isoform 2.|||In isoform 3.|||No effect on cell death; binds to CACNA1E as the wild type protein; does not affect subcellular location.|||No effect on cell death; normally binds to CACNA1E; does not affect subcellular location.|||Required for its localization in the mitotic spindle and interaction with alpha-tubulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073877|||http://purl.uniprot.org/annotation/VAR_023619|||http://purl.uniprot.org/annotation/VAR_023620|||http://purl.uniprot.org/annotation/VAR_023621|||http://purl.uniprot.org/annotation/VAR_023622|||http://purl.uniprot.org/annotation/VAR_023623|||http://purl.uniprot.org/annotation/VAR_023624|||http://purl.uniprot.org/annotation/VAR_023625|||http://purl.uniprot.org/annotation/VAR_023626|||http://purl.uniprot.org/annotation/VAR_026531|||http://purl.uniprot.org/annotation/VAR_043154|||http://purl.uniprot.org/annotation/VAR_043155|||http://purl.uniprot.org/annotation/VAR_043156|||http://purl.uniprot.org/annotation/VAR_043157|||http://purl.uniprot.org/annotation/VAR_043158|||http://purl.uniprot.org/annotation/VAR_043159|||http://purl.uniprot.org/annotation/VAR_048666|||http://purl.uniprot.org/annotation/VAR_072108|||http://purl.uniprot.org/annotation/VAR_072109|||http://purl.uniprot.org/annotation/VAR_072110|||http://purl.uniprot.org/annotation/VAR_079772|||http://purl.uniprot.org/annotation/VAR_079773|||http://purl.uniprot.org/annotation/VAR_079774|||http://purl.uniprot.org/annotation/VAR_079775|||http://purl.uniprot.org/annotation/VAR_079776|||http://purl.uniprot.org/annotation/VAR_079777|||http://purl.uniprot.org/annotation/VAR_079778|||http://purl.uniprot.org/annotation/VAR_079779|||http://purl.uniprot.org/annotation/VAR_079780|||http://purl.uniprot.org/annotation/VAR_079781|||http://purl.uniprot.org/annotation/VAR_079782|||http://purl.uniprot.org/annotation/VAR_079783|||http://purl.uniprot.org/annotation/VSP_015894|||http://purl.uniprot.org/annotation/VSP_015895|||http://purl.uniprot.org/annotation/VSP_046107
http://togogenome.org/gene/9606:P4HA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prolyl 4-hydroxylase subunit alpha-3|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317766|||http://purl.uniprot.org/annotation/VAR_038675|||http://purl.uniprot.org/annotation/VSP_031146|||http://purl.uniprot.org/annotation/VSP_031147|||http://purl.uniprot.org/annotation/VSP_054131
http://togogenome.org/gene/9606:PRCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42785                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Lysosomal Pro-X carboxypeptidase|||N-linked (GlcNAc...) asparagine|||SKS domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027308|||http://purl.uniprot.org/annotation/PRO_0000027309|||http://purl.uniprot.org/annotation/VAR_020464|||http://purl.uniprot.org/annotation/VAR_029329|||http://purl.uniprot.org/annotation/VSP_045799
http://togogenome.org/gene/9606:USP17L19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RCP7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421093
http://togogenome.org/gene/9606:CGB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQF0|||http://purl.uniprot.org/uniprot/P0DN87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Choriogonadotropin subunit beta 7|||Disordered|||Glycoprotein hormone subunit beta|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000436152|||http://purl.uniprot.org/annotation/PRO_5002521323
http://togogenome.org/gene/9606:PABIR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN12|||http://purl.uniprot.org/uniprot/G1UD80|||http://purl.uniprot.org/uniprot/Q7Z309                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 5.|||In isoform 5.|||N-acetylalanine|||Omega-N-methylarginine|||PABIR family member 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254545|||http://purl.uniprot.org/annotation/VSP_021215|||http://purl.uniprot.org/annotation/VSP_021216|||http://purl.uniprot.org/annotation/VSP_021217|||http://purl.uniprot.org/annotation/VSP_021218
http://togogenome.org/gene/9606:UROD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06132                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  25-30% of wild-type activity.|||5-10% of wild-type activity.|||In FPCT and HEP.|||In FPCT and HEP; requires 2 nucleotide substitutions; nearly normal activity.|||In FPCT.|||In FPCT; activity < 2%.|||In FPCT; decrease of activity.|||In FPCT; insoluble protein.|||In FPCT; significant decrease of activity.|||In HEP and FPCT; nearly normal activity.|||In HEP.|||In HEP; mild form.|||In HEP; mild phenotype; strong decrease of activity.|||In HEP; relative activity of 17% and 60% of wild-type towards uroporphyrinogen I and III respectively.|||In HEP; relative activity of 65% of wild-type towards uroporphyrinogen III.|||N-acetylmethionine|||No activity. Unable to bind substrate.|||Transition state stabilizer|||Uroporphyrinogen decarboxylase|||Very low activity. Binds substrate with similar geometry as wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187569|||http://purl.uniprot.org/annotation/VAR_007714|||http://purl.uniprot.org/annotation/VAR_007715|||http://purl.uniprot.org/annotation/VAR_007716|||http://purl.uniprot.org/annotation/VAR_007717|||http://purl.uniprot.org/annotation/VAR_007910|||http://purl.uniprot.org/annotation/VAR_007911|||http://purl.uniprot.org/annotation/VAR_007912|||http://purl.uniprot.org/annotation/VAR_007913|||http://purl.uniprot.org/annotation/VAR_007914|||http://purl.uniprot.org/annotation/VAR_007915|||http://purl.uniprot.org/annotation/VAR_007916|||http://purl.uniprot.org/annotation/VAR_007917|||http://purl.uniprot.org/annotation/VAR_009103|||http://purl.uniprot.org/annotation/VAR_009104|||http://purl.uniprot.org/annotation/VAR_009105|||http://purl.uniprot.org/annotation/VAR_009106|||http://purl.uniprot.org/annotation/VAR_009107|||http://purl.uniprot.org/annotation/VAR_009108|||http://purl.uniprot.org/annotation/VAR_010985|||http://purl.uniprot.org/annotation/VAR_010986|||http://purl.uniprot.org/annotation/VAR_010987|||http://purl.uniprot.org/annotation/VAR_010988|||http://purl.uniprot.org/annotation/VAR_022567|||http://purl.uniprot.org/annotation/VAR_022568|||http://purl.uniprot.org/annotation/VAR_022569|||http://purl.uniprot.org/annotation/VAR_022570|||http://purl.uniprot.org/annotation/VAR_022571|||http://purl.uniprot.org/annotation/VAR_022572|||http://purl.uniprot.org/annotation/VAR_022573|||http://purl.uniprot.org/annotation/VAR_022574|||http://purl.uniprot.org/annotation/VAR_022575|||http://purl.uniprot.org/annotation/VAR_022576|||http://purl.uniprot.org/annotation/VAR_022577|||http://purl.uniprot.org/annotation/VAR_022578|||http://purl.uniprot.org/annotation/VAR_060683|||http://purl.uniprot.org/annotation/VAR_060684|||http://purl.uniprot.org/annotation/VAR_060685|||http://purl.uniprot.org/annotation/VAR_060686|||http://purl.uniprot.org/annotation/VAR_065558|||http://purl.uniprot.org/annotation/VAR_065559|||http://purl.uniprot.org/annotation/VAR_067457
http://togogenome.org/gene/9606:JAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57087                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In IBGC8.|||In IBGC8; loss of localization to the plasma membrane; mainly retained in the cytoplasm.|||In IBGC8; loss of protein expression.|||In isoform 2.|||In isoform 3.|||Junctional adhesion molecule B|||N-linked (GlcNAc...) asparagine|||No effect on binding of JAM3 or integrin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015069|||http://purl.uniprot.org/annotation/VAR_049973|||http://purl.uniprot.org/annotation/VAR_083943|||http://purl.uniprot.org/annotation/VAR_083944|||http://purl.uniprot.org/annotation/VAR_083945|||http://purl.uniprot.org/annotation/VAR_083946|||http://purl.uniprot.org/annotation/VSP_045153|||http://purl.uniprot.org/annotation/VSP_047352
http://togogenome.org/gene/9606:MACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN28                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Metastasis-associated in colon cancer protein 1|||Phosphoserine|||SH3|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329032|||http://purl.uniprot.org/annotation/VAR_042620|||http://purl.uniprot.org/annotation/VAR_042621|||http://purl.uniprot.org/annotation/VAR_042622|||http://purl.uniprot.org/annotation/VAR_042623|||http://purl.uniprot.org/annotation/VAR_042624
http://togogenome.org/gene/9606:MRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCY5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 1.|||In isoform 2.|||In isoform 3.|||Melanocortin-2 receptor accessory protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096570|||http://purl.uniprot.org/annotation/VSP_003862|||http://purl.uniprot.org/annotation/VSP_003863|||http://purl.uniprot.org/annotation/VSP_003864|||http://purl.uniprot.org/annotation/VSP_021020
http://togogenome.org/gene/9606:TLE6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJM9|||http://purl.uniprot.org/uniprot/Q9H808                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In OZEMA15; almost complete loss of phosphorylation and reduced interaction with KHDC3L and OOEP.|||In OZEMA15; unknown pathological significance.|||In isoform 2.|||Phosphoserine; by PKA|||Polar residues|||Transducin-like enhancer protein 6|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051286|||http://purl.uniprot.org/annotation/VAR_076246|||http://purl.uniprot.org/annotation/VAR_084162|||http://purl.uniprot.org/annotation/VAR_084163|||http://purl.uniprot.org/annotation/VAR_084164|||http://purl.uniprot.org/annotation/VAR_084165|||http://purl.uniprot.org/annotation/VAR_084166|||http://purl.uniprot.org/annotation/VAR_084167|||http://purl.uniprot.org/annotation/VAR_084168|||http://purl.uniprot.org/annotation/VAR_084169|||http://purl.uniprot.org/annotation/VAR_084170|||http://purl.uniprot.org/annotation/VAR_084171|||http://purl.uniprot.org/annotation/VSP_047216
http://togogenome.org/gene/9606:RPGRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KN7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RPGR.|||Basic and acidic residues|||C2|||Decreases interaction with RPGR.|||Disordered|||Does not affect the interaction with NPHP4.|||Found in a patient associated with LCA6.|||Found in a patient with LCA6.|||Found in patients with primary open angle glaucoma and juvenile open angle glaucoma; affects the interaction with NPHP4.|||Impairs interaction with NPHP4.|||In CORD13.|||In LCA6.|||In LCA6; no effect on interaction with RPGR.|||In a patient with normal tension glaucoma and a patient with primary open angle glaucoma; affects the interaction with NPHP4.|||In a patient with normal tension glaucoma.|||In a patient with primary open angle glaucoma and a patient with juvenile open angle glaucoma; affects the interaction with NPHP4.|||In a patient with primary open angle glaucoma who also carries variant K-352 in MYOC; affects the interaction with NPHP4.|||In a patient with primary open angle glaucoma.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||Interaction with RPGR|||Nearly abolishes interaction with RPGR; when associated with A-1121 and A-1174.|||Nearly abolishes interaction with RPGR; when associated with A-1121 and A-1245.|||Nearly abolishes interaction with RPGR; when associated with A-1174 and A-1245.|||No effect on interaction with RPGR.|||Polar residues|||X-linked retinitis pigmentosa GTPase regulator-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097432|||http://purl.uniprot.org/annotation/VAR_017830|||http://purl.uniprot.org/annotation/VAR_017831|||http://purl.uniprot.org/annotation/VAR_017832|||http://purl.uniprot.org/annotation/VAR_017833|||http://purl.uniprot.org/annotation/VAR_017834|||http://purl.uniprot.org/annotation/VAR_017835|||http://purl.uniprot.org/annotation/VAR_017836|||http://purl.uniprot.org/annotation/VAR_057772|||http://purl.uniprot.org/annotation/VAR_057773|||http://purl.uniprot.org/annotation/VAR_057774|||http://purl.uniprot.org/annotation/VAR_065720|||http://purl.uniprot.org/annotation/VAR_065721|||http://purl.uniprot.org/annotation/VAR_065722|||http://purl.uniprot.org/annotation/VAR_065723|||http://purl.uniprot.org/annotation/VAR_065724|||http://purl.uniprot.org/annotation/VAR_065725|||http://purl.uniprot.org/annotation/VAR_065726|||http://purl.uniprot.org/annotation/VAR_065727|||http://purl.uniprot.org/annotation/VAR_065728|||http://purl.uniprot.org/annotation/VAR_065729|||http://purl.uniprot.org/annotation/VAR_065730|||http://purl.uniprot.org/annotation/VAR_065731|||http://purl.uniprot.org/annotation/VAR_065732|||http://purl.uniprot.org/annotation/VAR_065733|||http://purl.uniprot.org/annotation/VAR_065734|||http://purl.uniprot.org/annotation/VAR_065735|||http://purl.uniprot.org/annotation/VAR_065736|||http://purl.uniprot.org/annotation/VAR_065737|||http://purl.uniprot.org/annotation/VAR_065738|||http://purl.uniprot.org/annotation/VAR_067184|||http://purl.uniprot.org/annotation/VAR_067185|||http://purl.uniprot.org/annotation/VAR_067186|||http://purl.uniprot.org/annotation/VAR_067187|||http://purl.uniprot.org/annotation/VAR_067188|||http://purl.uniprot.org/annotation/VAR_076792|||http://purl.uniprot.org/annotation/VAR_076823|||http://purl.uniprot.org/annotation/VSP_009519|||http://purl.uniprot.org/annotation/VSP_009520|||http://purl.uniprot.org/annotation/VSP_009521|||http://purl.uniprot.org/annotation/VSP_009522|||http://purl.uniprot.org/annotation/VSP_009523|||http://purl.uniprot.org/annotation/VSP_009524|||http://purl.uniprot.org/annotation/VSP_009525|||http://purl.uniprot.org/annotation/VSP_009526|||http://purl.uniprot.org/annotation/VSP_009527
http://togogenome.org/gene/9606:CXCL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48061                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Mass|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-45 and S-46.|||55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-45 and S-48.|||55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-46 and S-48.|||Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor.|||Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-57. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-57.|||Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-86. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-86.|||Greatly impaired CXCR4 activation.|||Greatly impaired chemotactic activity and enhanced inhibition by heparin.|||Impaired CXCR4 activation ability, but only slightly impaired binding to the receptor.|||Impaired CXCR4 activation.|||Impaired CXCR4 activation. Loss of integrin activation; when associated with E-45 or E-64.|||Important for dimer formation|||Important for integrin interaction and activation|||In isoform 7.|||In isoform Alpha.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma.|||In isoform Theta.|||Loss of chemotactic activity.|||Loss of heparin-binding capacity.|||Loss of integrin activation; when associated with E-45 or E-48.|||Loss of integrin activation; when associated with E-48 or E-64.|||No effect on CXCR4 activation.|||No effect on CXCR4 activation. Impaired dimer formation, leading to increased chemotactic activity. Eliminates the pH dependence of dimerization.|||No effect on anti-HIV-1 and chemotactic activities.|||No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-34.|||No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-35.|||No significant effect on CXCR4 binding or activation.|||No significant effect on dimerization in neutral pH. Eliminates the pH dependence of dimerization.|||Receptor activation motif|||Receptor and heparin binding|||Receptor binding|||Reduced dimerization in neutral pH. Eliminates the pH dependence of dimerization.|||SDF-1-alpha(3-67)|||SDF-1-beta(3-72)|||Significantly decreased anti-HIV-1 and chemotactic activities.|||Significantly decreased chemotactic activity.|||Significantly impaired CXCR4 activation ability, but only slightly impaired binding to the receptor.|||Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and N-69.|||Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and Q-68.|||Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-68 and N-69.|||Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-62; Q-68 and N-69.|||Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with Q-48; Q-62; Q-68 and N-69.|||Slightly impaired binding and activation of CXCR4.|||Slightly impaired chemotactic activity and enhanced inhibition by heparin. Greatly impaired chemotactic activity; when associated with Q-29.|||Slightly impaired chemotactic activity, no effect on inhibition by heparin.|||Stromal cell-derived factor 1|||The measured range is 22-89.|||The measured range is 22-93.|||The measured range is 24-88.|||The measured range is 24-93.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005109|||http://purl.uniprot.org/annotation/PRO_0000005110|||http://purl.uniprot.org/annotation/PRO_0000005111|||http://purl.uniprot.org/annotation/VSP_001056|||http://purl.uniprot.org/annotation/VSP_041209|||http://purl.uniprot.org/annotation/VSP_042118|||http://purl.uniprot.org/annotation/VSP_042119|||http://purl.uniprot.org/annotation/VSP_042120|||http://purl.uniprot.org/annotation/VSP_054781
http://togogenome.org/gene/9606:NUP58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVL2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 2 AA repeats of F-G|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleoporin p58/p45|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204892|||http://purl.uniprot.org/annotation/VAR_050570|||http://purl.uniprot.org/annotation/VAR_050571|||http://purl.uniprot.org/annotation/VSP_007946|||http://purl.uniprot.org/annotation/VSP_007947|||http://purl.uniprot.org/annotation/VSP_045658
http://togogenome.org/gene/9606:PCDHAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNA7|||http://purl.uniprot.org/uniprot/Q9H158                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||Polar residues|||Protocadherin alpha-C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003910|||http://purl.uniprot.org/annotation/PRO_5014298338|||http://purl.uniprot.org/annotation/VAR_048540|||http://purl.uniprot.org/annotation/VSP_000699|||http://purl.uniprot.org/annotation/VSP_000700
http://togogenome.org/gene/9606:OR6K6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGW6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6K6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150631|||http://purl.uniprot.org/annotation/VAR_057551|||http://purl.uniprot.org/annotation/VAR_057552|||http://purl.uniprot.org/annotation/VAR_057553|||http://purl.uniprot.org/annotation/VAR_057554|||http://purl.uniprot.org/annotation/VAR_057555|||http://purl.uniprot.org/annotation/VAR_057556|||http://purl.uniprot.org/annotation/VAR_057557|||http://purl.uniprot.org/annotation/VAR_057558|||http://purl.uniprot.org/annotation/VAR_057559|||http://purl.uniprot.org/annotation/VAR_057560
http://togogenome.org/gene/9606:TUFM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384ME17|||http://purl.uniprot.org/uniprot/P49411                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Elongation factor Tu, mitochondrial|||G1|||G2|||G3|||G4|||G5|||In COXPD4.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007462|||http://purl.uniprot.org/annotation/VAR_031902
http://togogenome.org/gene/9606:APBA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96018                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Amyloid-beta A4 precursor protein-binding family A member 3|||Disordered|||N-acetylmethionine|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Polar residues|||Required for interaction with NECAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064620|||http://purl.uniprot.org/annotation/VAR_011822|||http://purl.uniprot.org/annotation/VAR_020134|||http://purl.uniprot.org/annotation/VAR_047952|||http://purl.uniprot.org/annotation/VAR_050666
http://togogenome.org/gene/9606:SLC10A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RA41|||http://purl.uniprot.org/uniprot/Q14973                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreased function in taurocholate transport.|||Decreased transport of taurocholate and cholate; decreased transport of estron sulfate; decreased expression at the cell membrane due to intracellular retention.|||Decreased transport of taurocholate and cholate; decreased transport of estron sulfate; does not affect localization to the cell membrane.|||Helical|||Hepatic sodium/bile acid cotransporter|||In FHCA2.|||In FHCA2; associated with resistance to hepatitis B virus infection and chronic hepatitis; unable to transport taurocholate and cholate; does not affect uptake of estrone sulfate; does not affect localization to the cell membrane.|||In FHCA2; decreased function in taurocholate transport.|||In FHCA2; loss of function in taurocholate transport; loss of localization to the cell membrane due to intracellular retention.|||Loss of function in taurocholate transport.|||N-linked (GlcNAc...) asparagine|||Severely decreased function in taurocholate transport.|||Slightly decreased function in taurocholate transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052335|||http://purl.uniprot.org/annotation/VAR_022113|||http://purl.uniprot.org/annotation/VAR_085560|||http://purl.uniprot.org/annotation/VAR_085561|||http://purl.uniprot.org/annotation/VAR_085562|||http://purl.uniprot.org/annotation/VAR_085563|||http://purl.uniprot.org/annotation/VAR_085564|||http://purl.uniprot.org/annotation/VAR_085565|||http://purl.uniprot.org/annotation/VAR_085566|||http://purl.uniprot.org/annotation/VAR_085567|||http://purl.uniprot.org/annotation/VAR_085568|||http://purl.uniprot.org/annotation/VAR_085569|||http://purl.uniprot.org/annotation/VAR_085570|||http://purl.uniprot.org/annotation/VAR_085571|||http://purl.uniprot.org/annotation/VAR_085572|||http://purl.uniprot.org/annotation/VAR_085573|||http://purl.uniprot.org/annotation/VAR_085574|||http://purl.uniprot.org/annotation/VAR_085575|||http://purl.uniprot.org/annotation/VAR_085576|||http://purl.uniprot.org/annotation/VAR_085577|||http://purl.uniprot.org/annotation/VAR_085578|||http://purl.uniprot.org/annotation/VAR_085579|||http://purl.uniprot.org/annotation/VAR_085580|||http://purl.uniprot.org/annotation/VAR_085581|||http://purl.uniprot.org/annotation/VAR_085582
http://togogenome.org/gene/9606:RHPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  BRO1|||Disordered|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||REM-1|||Rhophilin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218895
http://togogenome.org/gene/9606:LRIG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9K080|||http://purl.uniprot.org/uniprot/Q6UXM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeats and immunoglobulin-like domains protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014831|||http://purl.uniprot.org/annotation/PRO_5002997948|||http://purl.uniprot.org/annotation/VSP_015097
http://togogenome.org/gene/9606:C14orf180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN93|||http://purl.uniprot.org/uniprot/J3KNP8|||http://purl.uniprot.org/uniprot/Q8N912                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Nutritionally-regulated adipose and cardiac enriched protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326052
http://togogenome.org/gene/9606:GAPVD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGD8|||http://purl.uniprot.org/uniprot/F8W9S7|||http://purl.uniprot.org/uniprot/Q14C86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GTPase-activating protein and VPS9 domain-containing protein 1|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Ras-GAP|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324771|||http://purl.uniprot.org/annotation/VSP_032358|||http://purl.uniprot.org/annotation/VSP_032359|||http://purl.uniprot.org/annotation/VSP_032360|||http://purl.uniprot.org/annotation/VSP_032361|||http://purl.uniprot.org/annotation/VSP_032362
http://togogenome.org/gene/9606:JADE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFT8|||http://purl.uniprot.org/uniprot/B3KPL2|||http://purl.uniprot.org/uniprot/B4DFY8|||http://purl.uniprot.org/uniprot/G3XAA4|||http://purl.uniprot.org/uniprot/Q9NQC1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||E3 ubiquitin-protein ligase Jade-2|||In isoform 2.|||In isoform 3.|||Loss of E3 ubiquitin-protein ligase activity on KDM1A.|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059308|||http://purl.uniprot.org/annotation/VAR_053778|||http://purl.uniprot.org/annotation/VSP_021050|||http://purl.uniprot.org/annotation/VSP_021051
http://togogenome.org/gene/9606:SLC17A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14916                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Increased urate transport.|||N-linked (GlcNAc...) asparagine|||Sodium-dependent phosphate transport protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220936|||http://purl.uniprot.org/annotation/VAR_050060|||http://purl.uniprot.org/annotation/VAR_050061|||http://purl.uniprot.org/annotation/VSP_035012
http://togogenome.org/gene/9606:PILRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKJ0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Paired immunoglobulin-like type 2 receptor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226822|||http://purl.uniprot.org/annotation/VAR_059406|||http://purl.uniprot.org/annotation/VAR_059407|||http://purl.uniprot.org/annotation/VSP_017503|||http://purl.uniprot.org/annotation/VSP_017504
http://togogenome.org/gene/9606:SCARF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||Extracellular|||Helical|||In VDEGS.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Scavenger receptor class F member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007739|||http://purl.uniprot.org/annotation/VAR_015148|||http://purl.uniprot.org/annotation/VAR_015149|||http://purl.uniprot.org/annotation/VAR_015150|||http://purl.uniprot.org/annotation/VAR_015151|||http://purl.uniprot.org/annotation/VAR_035837|||http://purl.uniprot.org/annotation/VAR_055776|||http://purl.uniprot.org/annotation/VAR_055777|||http://purl.uniprot.org/annotation/VAR_059274|||http://purl.uniprot.org/annotation/VAR_065302|||http://purl.uniprot.org/annotation/VSP_042462
http://togogenome.org/gene/9606:PROK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC23                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In HH4.|||In HH4; no effect on intracellular calcium mobilization.|||In HH4; phenotype consistent with Kallmann syndrome.|||In HH4; phenotype consistent with Kallmann syndrome; impaired calcium mobilization.|||In HH4; totally abolished intracellular calcium mobilization.|||In isoform 2.|||Prokineticin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025809|||http://purl.uniprot.org/annotation/VAR_030955|||http://purl.uniprot.org/annotation/VAR_030956|||http://purl.uniprot.org/annotation/VAR_069970|||http://purl.uniprot.org/annotation/VAR_072177|||http://purl.uniprot.org/annotation/VAR_072178|||http://purl.uniprot.org/annotation/VAR_072991|||http://purl.uniprot.org/annotation/VSP_005219
http://togogenome.org/gene/9606:ANP32D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95626                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic leucine-rich nuclear phosphoprotein 32 family member D|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137598|||http://purl.uniprot.org/annotation/VAR_027832
http://togogenome.org/gene/9606:EIF2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14232                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In VWM1.|||In isoform 2.|||N6-acetyllysine|||Translation initiation factor eIF-2B subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156055|||http://purl.uniprot.org/annotation/VAR_015404|||http://purl.uniprot.org/annotation/VAR_068450|||http://purl.uniprot.org/annotation/VSP_055469|||http://purl.uniprot.org/annotation/VSP_055470
http://togogenome.org/gene/9606:SRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPP4|||http://purl.uniprot.org/uniprot/Q86TD4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sarcalumenin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045426|||http://purl.uniprot.org/annotation/PRO_5002790047|||http://purl.uniprot.org/annotation/VSP_060762|||http://purl.uniprot.org/annotation/VSP_060763
http://togogenome.org/gene/9606:PSMD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNM6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 13|||In isoform 2.|||N6-acetyllysine|||PCI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173867|||http://purl.uniprot.org/annotation/VAR_024591|||http://purl.uniprot.org/annotation/VAR_031094|||http://purl.uniprot.org/annotation/VAR_031095|||http://purl.uniprot.org/annotation/VAR_057050|||http://purl.uniprot.org/annotation/VSP_041067
http://togogenome.org/gene/9606:DELE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14154                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Propeptide|||Region|||Repeat|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Cleavage; by OMA1|||DAP3-binding cell death enhancer 1|||DAP3-binding cell death enhancer 1 short form|||Disordered|||Extended MTS|||Mitochondrion|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050721|||http://purl.uniprot.org/annotation/PRO_0000450308|||http://purl.uniprot.org/annotation/PRO_0000459060|||http://purl.uniprot.org/annotation/VAR_018272|||http://purl.uniprot.org/annotation/VAR_018273|||http://purl.uniprot.org/annotation/VAR_028197|||http://purl.uniprot.org/annotation/VAR_028198|||http://purl.uniprot.org/annotation/VAR_055940
http://togogenome.org/gene/9606:WEE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C1S8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In OZEMA5; decreased WEE2 phosphorylation at serine residues; decreased CDK1/CDC2 phosphorylation at 'Y-15'.|||In a gastric adenocarcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Wee1-like protein kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248079|||http://purl.uniprot.org/annotation/VAR_041304|||http://purl.uniprot.org/annotation/VAR_041305|||http://purl.uniprot.org/annotation/VAR_041306|||http://purl.uniprot.org/annotation/VAR_041307|||http://purl.uniprot.org/annotation/VAR_041308|||http://purl.uniprot.org/annotation/VAR_080992
http://togogenome.org/gene/9606:FAM47B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA70                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Protein FAM47B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187038
http://togogenome.org/gene/9606:FLRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6E1VY70|||http://purl.uniprot.org/uniprot/Q9NZU1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane protein FLRT1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021278
http://togogenome.org/gene/9606:NDUFAF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TEU4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Arginine-hydroxylase NDUFAF5, mitochondrial|||In MC1DN16.|||In isoform 2.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307213|||http://purl.uniprot.org/annotation/VAR_035376|||http://purl.uniprot.org/annotation/VAR_054119|||http://purl.uniprot.org/annotation/VAR_067956|||http://purl.uniprot.org/annotation/VAR_076864|||http://purl.uniprot.org/annotation/VSP_028637
http://togogenome.org/gene/9606:HPDL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IR7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  4-hydroxyphenylpyruvate dioxygenase-like protein|||In NEDSWMA.|||In NEDSWMA; unknown pathological significance.|||In NEDSWMA; unknown pathological significance; decreased protein abundance.|||In SPG83.|||In SPG83; unknown pathological significance.|||VOC 1|||VOC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271119|||http://purl.uniprot.org/annotation/VAR_085125|||http://purl.uniprot.org/annotation/VAR_085126|||http://purl.uniprot.org/annotation/VAR_085127|||http://purl.uniprot.org/annotation/VAR_085128|||http://purl.uniprot.org/annotation/VAR_085129|||http://purl.uniprot.org/annotation/VAR_085130|||http://purl.uniprot.org/annotation/VAR_085131|||http://purl.uniprot.org/annotation/VAR_085132|||http://purl.uniprot.org/annotation/VAR_085133|||http://purl.uniprot.org/annotation/VAR_085134|||http://purl.uniprot.org/annotation/VAR_085135|||http://purl.uniprot.org/annotation/VAR_085136|||http://purl.uniprot.org/annotation/VAR_085137|||http://purl.uniprot.org/annotation/VAR_085523
http://togogenome.org/gene/9606:OMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47874                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||Olfactory marker protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058043|||http://purl.uniprot.org/annotation/VAR_051254|||http://purl.uniprot.org/annotation/VAR_051255
http://togogenome.org/gene/9606:KLF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3GC14|||http://purl.uniprot.org/uniprot/Q99612                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Found in gastric cancer samples; somatic mutation.|||Found in prostate cancer samples; somatic mutation; does not up-regulates CDKN1A in a p53-independent manner and significantly reduces cell proliferation.|||In isoform 2.|||In isoform 3.|||Krueppel-like factor 6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047171|||http://purl.uniprot.org/annotation/VAR_065136|||http://purl.uniprot.org/annotation/VAR_065137|||http://purl.uniprot.org/annotation/VAR_065138|||http://purl.uniprot.org/annotation/VAR_065139|||http://purl.uniprot.org/annotation/VAR_065140|||http://purl.uniprot.org/annotation/VAR_065141|||http://purl.uniprot.org/annotation/VAR_065142|||http://purl.uniprot.org/annotation/VAR_065143|||http://purl.uniprot.org/annotation/VSP_015715|||http://purl.uniprot.org/annotation/VSP_045808
http://togogenome.org/gene/9606:SLC7A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92536                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Polar residues|||Y+L amino acid transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341477
http://togogenome.org/gene/9606:ERG28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FII3|||http://purl.uniprot.org/uniprot/Q86TW5|||http://purl.uniprot.org/uniprot/Q9UKR5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Transmembrane                                                                                  ^@                                                                                  Ergosterol biosynthetic protein 28 homolog|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193903
http://togogenome.org/gene/9606:CHKA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35790                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished acetylation by KAT5, leading to prevent conversion into a tyrosine-protein kinase.|||Abolished interaction with PLIN2 and PLIN3.|||Abolished phosphorylation by AMPK, preventing localization to lipid droplets and subsequent acetylation by KAT5.|||Choline kinase alpha|||Disordered|||Does not affect interaction with PLIN2 and PLIN3.|||In NEDMIMS.|||In NEDMIMS; a functional model in yeast shows reduced choline kinase activity.|||In isoform 2.|||Mimics acetylation; promoting monomerization, leading to decreased choline kinase activity. Increased lipolysis of lipid droplets.|||Mimics phosphorylation; promoting localization to lipid droplets.|||N6-acetyllysine|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206219|||http://purl.uniprot.org/annotation/VAR_054863|||http://purl.uniprot.org/annotation/VAR_054864|||http://purl.uniprot.org/annotation/VAR_087712|||http://purl.uniprot.org/annotation/VAR_087713|||http://purl.uniprot.org/annotation/VAR_087714|||http://purl.uniprot.org/annotation/VSP_009683
http://togogenome.org/gene/9606:TMOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZR1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Tropomodulin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186131|||http://purl.uniprot.org/annotation/VAR_052399|||http://purl.uniprot.org/annotation/VSP_041506
http://togogenome.org/gene/9606:ADAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCV1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A to I editase|||Adenosine deaminase domain-containing protein 2|||DRBM|||Disordered|||Found in a patient with non-obstructive azoospermia; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309524|||http://purl.uniprot.org/annotation/VAR_036976|||http://purl.uniprot.org/annotation/VAR_055650|||http://purl.uniprot.org/annotation/VAR_087421|||http://purl.uniprot.org/annotation/VSP_029230|||http://purl.uniprot.org/annotation/VSP_029231
http://togogenome.org/gene/9606:IDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGD7|||http://purl.uniprot.org/uniprot/P22304                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Iduronate 2-sulfatase 14 kDa chain|||Iduronate 2-sulfatase 42 kDa chain|||In MPS2.|||In MPS2; intermediate form.|||In MPS2; intermediate form; deleterious mutation; residual activity of 7.5% of the wild-type.|||In MPS2; intermediate form; mutation A-489 confirmed as causative of MPS2.|||In MPS2; intermediate to severe forms.|||In MPS2; intermediate/severe form.|||In MPS2; intermediate/severe form; higher affinity for the artificial substrate; poor transport to lysosomes.|||In MPS2; mild form.|||In MPS2; mild form; increase in enzyme activity observed in transfected cells.|||In MPS2; mild to severe forms.|||In MPS2; mild to severe forms; greatly reduced activity; poor transport to lysosomes.|||In MPS2; mild/intermediate form.|||In MPS2; mild/severe form.|||In MPS2; no significant enzyme activity.|||In MPS2; severe form.|||In MPS2; severe form; deleterious mutation confirmed.|||In MPS2; severe form; deleterious mutation; results in an inactive enzyme.|||In MPS2; severe form; total absence of residual activity; poor transport to lysosomes.|||In MPS2; severe from.|||In MPS2; severe.|||In MPS2; severe/intermediate form; greatly reduced activity; poor transport to lysosomes.|||In MPS2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033428|||http://purl.uniprot.org/annotation/PRO_0000033429|||http://purl.uniprot.org/annotation/PRO_0000033430|||http://purl.uniprot.org/annotation/VAR_007313|||http://purl.uniprot.org/annotation/VAR_007314|||http://purl.uniprot.org/annotation/VAR_007315|||http://purl.uniprot.org/annotation/VAR_007316|||http://purl.uniprot.org/annotation/VAR_007317|||http://purl.uniprot.org/annotation/VAR_007318|||http://purl.uniprot.org/annotation/VAR_007319|||http://purl.uniprot.org/annotation/VAR_007320|||http://purl.uniprot.org/annotation/VAR_007321|||http://purl.uniprot.org/annotation/VAR_007322|||http://purl.uniprot.org/annotation/VAR_007323|||http://purl.uniprot.org/annotation/VAR_007324|||http://purl.uniprot.org/annotation/VAR_007325|||http://purl.uniprot.org/annotation/VAR_007326|||http://purl.uniprot.org/annotation/VAR_007327|||http://purl.uniprot.org/annotation/VAR_007328|||http://purl.uniprot.org/annotation/VAR_007329|||http://purl.uniprot.org/annotation/VAR_007330|||http://purl.uniprot.org/annotation/VAR_007331|||http://purl.uniprot.org/annotation/VAR_007332|||http://purl.uniprot.org/annotation/VAR_007333|||http://purl.uniprot.org/annotation/VAR_007334|||http://purl.uniprot.org/annotation/VAR_007335|||http://purl.uniprot.org/annotation/VAR_007336|||http://purl.uniprot.org/annotation/VAR_007337|||http://purl.uniprot.org/annotation/VAR_007338|||http://purl.uniprot.org/annotation/VAR_007339|||http://purl.uniprot.org/annotation/VAR_007340|||http://purl.uniprot.org/annotation/VAR_007341|||http://purl.uniprot.org/annotation/VAR_007342|||http://purl.uniprot.org/annotation/VAR_007343|||http://purl.uniprot.org/annotation/VAR_007344|||http://purl.uniprot.org/annotation/VAR_007345|||http://purl.uniprot.org/annotation/VAR_007346|||http://purl.uniprot.org/annotation/VAR_007347|||http://purl.uniprot.org/annotation/VAR_007348|||http://purl.uniprot.org/annotation/VAR_007349|||http://purl.uniprot.org/annotation/VAR_007350|||http://purl.uniprot.org/annotation/VAR_007351|||http://purl.uniprot.org/annotation/VAR_007352|||http://purl.uniprot.org/annotation/VAR_007353|||http://purl.uniprot.org/annotation/VAR_007354|||http://purl.uniprot.org/annotation/VAR_007355|||http://purl.uniprot.org/annotation/VAR_007356|||http://purl.uniprot.org/annotation/VAR_007357|||http://purl.uniprot.org/annotation/VAR_007358|||http://purl.uniprot.org/annotation/VAR_007359|||http://purl.uniprot.org/annotation/VAR_007360|||http://purl.uniprot.org/annotation/VAR_007361|||http://purl.uniprot.org/annotation/VAR_007362|||http://purl.uniprot.org/annotation/VAR_007363|||http://purl.uniprot.org/annotation/VAR_007364|||http://purl.uniprot.org/annotation/VAR_007365|||http://purl.uniprot.org/annotation/VAR_007366|||http://purl.uniprot.org/annotation/VAR_007367|||http://purl.uniprot.org/annotation/VAR_007368|||http://purl.uniprot.org/annotation/VAR_007369|||http://purl.uniprot.org/annotation/VAR_007370|||http://purl.uniprot.org/annotation/VAR_007371|||http://purl.uniprot.org/annotation/VAR_007372|||http://purl.uniprot.org/annotation/VAR_007373|||http://purl.uniprot.org/annotation/VAR_007374|||http://purl.uniprot.org/annotation/VAR_007375|||http://purl.uniprot.org/annotation/VAR_007376|||http://purl.uniprot.org/annotation/VAR_007377|||http://purl.uniprot.org/annotation/VAR_007378|||http://purl.uniprot.org/annotation/VAR_007379|||http://purl.uniprot.org/annotation/VAR_007380|||http://purl.uniprot.org/annotation/VAR_007381|||http://purl.uniprot.org/annotation/VAR_007382|||http://purl.uniprot.org/annotation/VAR_007383|||http://purl.uniprot.org/annotation/VAR_007384|||http://purl.uniprot.org/annotation/VAR_007385|||http://purl.uniprot.org/annotation/VAR_007386|||http://purl.uniprot.org/annotation/VAR_007387|||http://purl.uniprot.org/annotation/VAR_008134|||http://purl.uniprot.org/annotation/VAR_008135|||http://purl.uniprot.org/annotation/VAR_008136|||http://purl.uniprot.org/annotation/VAR_008998|||http://purl.uniprot.org/annotation/VAR_008999|||http://purl.uniprot.org/annotation/VAR_009000|||http://purl.uniprot.org/annotation/VAR_009001|||http://purl.uniprot.org/annotation/VAR_009002|||http://purl.uniprot.org/annotation/VAR_009003|||http://purl.uniprot.org/annotation/VAR_026914|||http://purl.uniprot.org/annotation/VAR_026915|||http://purl.uniprot.org/annotation/VAR_026916|||http://purl.uniprot.org/annotation/VAR_026917|||http://purl.uniprot.org/annotation/VAR_026918|||http://purl.uniprot.org/annotation/VAR_026919|||http://purl.uniprot.org/annotation/VAR_026920|||http://purl.uniprot.org/annotation/VAR_026921|||http://purl.uniprot.org/annotation/VAR_026922|||http://purl.uniprot.org/annotation/VAR_026923|||http://purl.uniprot.org/annotation/VAR_026924|||http://purl.uniprot.org/annotation/VAR_026925|||http://purl.uniprot.org/annotation/VAR_026926|||http://purl.uniprot.org/annotation/VAR_026927|||http://purl.uniprot.org/annotation/VAR_026928|||http://purl.uniprot.org/annotation/VAR_026929|||http://purl.uniprot.org/annotation/VAR_026930|||http://purl.uniprot.org/annotation/VAR_026931|||http://purl.uniprot.org/annotation/VAR_026932|||http://purl.uniprot.org/annotation/VAR_026933|||http://purl.uniprot.org/annotation/VAR_026934|||http://purl.uniprot.org/annotation/VAR_026935|||http://purl.uniprot.org/annotation/VAR_026936|||http://purl.uniprot.org/annotation/VAR_026937|||http://purl.uniprot.org/annotation/VAR_026938|||http://purl.uniprot.org/annotation/VAR_026939|||http://purl.uniprot.org/annotation/VAR_026940|||http://purl.uniprot.org/annotation/VAR_026941|||http://purl.uniprot.org/annotation/VAR_026942|||http://purl.uniprot.org/annotation/VAR_026943|||http://purl.uniprot.org/annotation/VAR_026944|||http://purl.uniprot.org/annotation/VAR_026945|||http://purl.uniprot.org/annotation/VAR_026946|||http://purl.uniprot.org/annotation/VAR_026947|||http://purl.uniprot.org/annotation/VAR_026948|||http://purl.uniprot.org/annotation/VAR_026949|||http://purl.uniprot.org/annotation/VAR_026950|||http://purl.uniprot.org/annotation/VAR_026951|||http://purl.uniprot.org/annotation/VAR_026952|||http://purl.uniprot.org/annotation/VAR_026953|||http://purl.uniprot.org/annotation/VAR_026954|||http://purl.uniprot.org/annotation/VAR_026955|||http://purl.uniprot.org/annotation/VAR_026956|||http://purl.uniprot.org/annotation/VAR_026957|||http://purl.uniprot.org/annotation/VAR_026958|||http://purl.uniprot.org/annotation/VAR_026959|||http://purl.uniprot.org/annotation/VAR_026960|||http://purl.uniprot.org/annotation/VAR_026961|||http://purl.uniprot.org/annotation/VAR_026962|||http://purl.uniprot.org/annotation/VSP_006301|||http://purl.uniprot.org/annotation/VSP_006302|||http://purl.uniprot.org/annotation/VSP_039116|||http://purl.uniprot.org/annotation/VSP_039117
http://togogenome.org/gene/9606:OR4D5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD9|||http://purl.uniprot.org/uniprot/Q8NGN0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150539
http://togogenome.org/gene/9606:OGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0R3|||http://purl.uniprot.org/uniprot/P20774|||http://purl.uniprot.org/uniprot/Q7Z532                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Repeat|||Signal Peptide                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Mimecan|||N-linked (GlcNAc...) (keratan sulfate) asparagine|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032760|||http://purl.uniprot.org/annotation/PRO_5004295239|||http://purl.uniprot.org/annotation/PRO_5014297550
http://togogenome.org/gene/9606:PDZD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXQ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PDZ|||PDZ domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271215|||http://purl.uniprot.org/annotation/VSP_022286|||http://purl.uniprot.org/annotation/VSP_022287|||http://purl.uniprot.org/annotation/VSP_053798
http://togogenome.org/gene/9606:SVIL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6I8PIX7|||http://purl.uniprot.org/uniprot/O95425|||http://purl.uniprot.org/uniprot/Q569J5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Gelsolin-like 1|||Gelsolin-like 2|||Gelsolin-like 3|||Gelsolin-like 4|||Gelsolin-like 5|||HP|||In MFM10; decreased protein abundance.|||In isoform 2 and isoform SV4.|||In isoform 2.|||In isoform SV3.|||Interaction with MYLK|||Interaction with NEB|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Strongly increased affinity for F-actin.|||Supervillin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218740|||http://purl.uniprot.org/annotation/VAR_020791|||http://purl.uniprot.org/annotation/VAR_020792|||http://purl.uniprot.org/annotation/VAR_024691|||http://purl.uniprot.org/annotation/VAR_057467|||http://purl.uniprot.org/annotation/VAR_057468|||http://purl.uniprot.org/annotation/VAR_057469|||http://purl.uniprot.org/annotation/VAR_058308|||http://purl.uniprot.org/annotation/VAR_085140|||http://purl.uniprot.org/annotation/VSP_012425|||http://purl.uniprot.org/annotation/VSP_012426|||http://purl.uniprot.org/annotation/VSP_053768
http://togogenome.org/gene/9606:CYLC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14093|||http://purl.uniprot.org/uniprot/Q6PEJ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X approximate tandem repeats|||31 X 3 AA repeats of K-K-X|||Basic and acidic residues|||Cylicin N-terminal|||Cylicin-2|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079755|||http://purl.uniprot.org/annotation/VAR_020100|||http://purl.uniprot.org/annotation/VAR_020101|||http://purl.uniprot.org/annotation/VAR_020102|||http://purl.uniprot.org/annotation/VAR_050938|||http://purl.uniprot.org/annotation/VAR_050939
http://togogenome.org/gene/9606:USP16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5T5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of enzyme activity.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080643|||http://purl.uniprot.org/annotation/VAR_020388|||http://purl.uniprot.org/annotation/VSP_036713|||http://purl.uniprot.org/annotation/VSP_036714|||http://purl.uniprot.org/annotation/VSP_036715|||http://purl.uniprot.org/annotation/VSP_036716
http://togogenome.org/gene/9606:ARVCF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00192                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 10|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Disordered|||In isoform Short.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with RNA-binding proteins DDX5, HNRNPH2 and SRSF1 and with mRNAs|||Splicing regulator ARVCF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064294|||http://purl.uniprot.org/annotation/VAR_020408|||http://purl.uniprot.org/annotation/VAR_024692|||http://purl.uniprot.org/annotation/VAR_033529|||http://purl.uniprot.org/annotation/VAR_033530|||http://purl.uniprot.org/annotation/VAR_033531|||http://purl.uniprot.org/annotation/VAR_033532|||http://purl.uniprot.org/annotation/VAR_053812|||http://purl.uniprot.org/annotation/VSP_006739
http://togogenome.org/gene/9606:OR5V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV99|||http://purl.uniprot.org/uniprot/Q9UGF6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5V1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150617|||http://purl.uniprot.org/annotation/VAR_053211|||http://purl.uniprot.org/annotation/VAR_053212|||http://purl.uniprot.org/annotation/VAR_064740
http://togogenome.org/gene/9606:MGST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14880                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes S-acylation; when associated with S-150.|||Abolishes S-acylation; when associated with S-151.|||Cytoplasmic|||Glutathione S-transferase 3, mitochondrial|||Helical|||Mitochondrial intermembrane|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217741|||http://purl.uniprot.org/annotation/VAR_012061|||http://purl.uniprot.org/annotation/VAR_012062
http://togogenome.org/gene/9606:MAP2K7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV95|||http://purl.uniprot.org/uniprot/O14733                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by anthrax lethal factor|||D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 7|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAP3K|||Phosphothreonine; by MAP3K|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086388|||http://purl.uniprot.org/annotation/VAR_029890|||http://purl.uniprot.org/annotation/VAR_040825|||http://purl.uniprot.org/annotation/VAR_040826|||http://purl.uniprot.org/annotation/VAR_040827|||http://purl.uniprot.org/annotation/VAR_040828|||http://purl.uniprot.org/annotation/VAR_040829|||http://purl.uniprot.org/annotation/VSP_004883|||http://purl.uniprot.org/annotation/VSP_022309|||http://purl.uniprot.org/annotation/VSP_022310
http://togogenome.org/gene/9606:GNAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11488                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||Abolishes myristoylation, interaction with UNC119 and localization.|||Basic and acidic residues|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(t) subunit alpha-1|||In CSNB1G.|||In CSNBAD3.|||Interaction with RHO|||N-myristoyl glycine|||Phosphotyrosine; by SRC|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203737|||http://purl.uniprot.org/annotation/VAR_009279|||http://purl.uniprot.org/annotation/VAR_073798|||http://purl.uniprot.org/annotation/VAR_073799
http://togogenome.org/gene/9606:RALBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15311                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of ATP-binding and transport-associated ATPase activity.|||Mediates association with membranes and could form transmembrane domains|||Mediates interaction with RALA and RALB|||Mediates interaction with REPS1 and REPS2|||N-acetylthreonine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||RalA-binding protein 1|||Removed|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056733|||http://purl.uniprot.org/annotation/VAR_049147
http://togogenome.org/gene/9606:RPS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62241|||http://purl.uniprot.org/uniprot/Q5JR94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein eS8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122240|||http://purl.uniprot.org/annotation/VAR_051861
http://togogenome.org/gene/9606:BACE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Z0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-secretase 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of autoproteolytic cleavage.|||N-linked (GlcNAc...) asparagine|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025945|||http://purl.uniprot.org/annotation/PRO_0000025946|||http://purl.uniprot.org/annotation/VSP_038023|||http://purl.uniprot.org/annotation/VSP_038024|||http://purl.uniprot.org/annotation/VSP_038025|||http://purl.uniprot.org/annotation/VSP_038026|||http://purl.uniprot.org/annotation/VSP_038027
http://togogenome.org/gene/9606:ASPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U10                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  60 kDa lysophospholipase|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Acyl-ester intermediate|||Asparaginase|||Asparaginase/glutaminase|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324163|||http://purl.uniprot.org/annotation/VAR_059131|||http://purl.uniprot.org/annotation/VAR_059132|||http://purl.uniprot.org/annotation/VAR_059133|||http://purl.uniprot.org/annotation/VSP_040740
http://togogenome.org/gene/9606:SNX22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTF9|||http://purl.uniprot.org/uniprot/Q96L94                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PX|||Sorting nexin-22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213871|||http://purl.uniprot.org/annotation/VSP_056595
http://togogenome.org/gene/9606:CCNDBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95273                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-D1-binding protein 1|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with RPLP0|||Interaction with TCF3|||N-acetylalanine|||Removed|||Required for interaction with CCND1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323372|||http://purl.uniprot.org/annotation/VSP_032012|||http://purl.uniprot.org/annotation/VSP_032013|||http://purl.uniprot.org/annotation/VSP_032014|||http://purl.uniprot.org/annotation/VSP_032015|||http://purl.uniprot.org/annotation/VSP_032016
http://togogenome.org/gene/9606:TMPRSS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z247|||http://purl.uniprot.org/uniprot/F5GX83|||http://purl.uniprot.org/uniprot/F5GYA3|||http://purl.uniprot.org/uniprot/F5H0U3|||http://purl.uniprot.org/uniprot/F5H2M3|||http://purl.uniprot.org/uniprot/Q0P513|||http://purl.uniprot.org/uniprot/Q0P514|||http://purl.uniprot.org/uniprot/Q9H3S3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In patients with sporadic hearing loss.|||In patients with sporadic hearing loss; no detectable proteolytic activity in a yeast-based protease assay.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Reduced proteolytic activity in a yeast-based protease assay.|||SRCR|||Transmembrane protease serine 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088694|||http://purl.uniprot.org/annotation/VAR_038005|||http://purl.uniprot.org/annotation/VAR_038006|||http://purl.uniprot.org/annotation/VAR_038007|||http://purl.uniprot.org/annotation/VAR_038008|||http://purl.uniprot.org/annotation/VAR_038009|||http://purl.uniprot.org/annotation/VAR_038010|||http://purl.uniprot.org/annotation/VAR_038011
http://togogenome.org/gene/9606:MYL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NY64|||http://purl.uniprot.org/uniprot/P24844                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||Myosin regulatory light polypeptide 9|||N-acetylserine|||Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1, DAPK2 and ZIPK/DAPK3|||Phosphothreonine; by MLCK, CIT and ROCK2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198735|||http://purl.uniprot.org/annotation/VSP_042834
http://togogenome.org/gene/9606:ANKMY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MBY4|||http://purl.uniprot.org/uniprot/J3KPY5|||http://purl.uniprot.org/uniprot/J3KQ21|||http://purl.uniprot.org/uniprot/Q6GPI0|||http://purl.uniprot.org/uniprot/Q9P2S6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and MYND domain-containing protein 1|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MORN 1|||MORN 2|||MORN 3|||MYND-type|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066894|||http://purl.uniprot.org/annotation/VAR_048264|||http://purl.uniprot.org/annotation/VAR_048265|||http://purl.uniprot.org/annotation/VAR_048266|||http://purl.uniprot.org/annotation/VAR_048267|||http://purl.uniprot.org/annotation/VAR_048268|||http://purl.uniprot.org/annotation/VSP_007442|||http://purl.uniprot.org/annotation/VSP_007443|||http://purl.uniprot.org/annotation/VSP_007444|||http://purl.uniprot.org/annotation/VSP_007445|||http://purl.uniprot.org/annotation/VSP_039104
http://togogenome.org/gene/9606:SART3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15020                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with disseminated superficial actinic porokeratosis; unknown pathological significance.|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates interaction with PRPF3|||N-acetylalanine|||Necessary and sufficient for U6 snRNA binding|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||Removed|||Required for interaction with USP4|||Required for nuclear localization|||Squamous cell carcinoma antigen recognized by T-cells 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223313|||http://purl.uniprot.org/annotation/VAR_038683|||http://purl.uniprot.org/annotation/VAR_038684|||http://purl.uniprot.org/annotation/VAR_038802|||http://purl.uniprot.org/annotation/VSP_017248|||http://purl.uniprot.org/annotation/VSP_017249|||http://purl.uniprot.org/annotation/VSP_017250|||http://purl.uniprot.org/annotation/VSP_017251|||http://purl.uniprot.org/annotation/VSP_057284
http://togogenome.org/gene/9606:CACNA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00975                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Binding to the beta subunit|||Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Found in a family with myoclonus and dystonia; also found in a sporadic case; unknown pathological significance; single-channel currents of the mutant are smaller than wild-type, likely due to channel stabilization in the lower current amplitude open state; voltage-dependent activation and inactivation as well as ion selectivity are unchanged.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In NEDNEH.|||In isoform Alpha-1B-2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Voltage-dependent N-type calcium channel subunit alpha-1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053921|||http://purl.uniprot.org/annotation/VAR_048741|||http://purl.uniprot.org/annotation/VAR_048742|||http://purl.uniprot.org/annotation/VAR_048743|||http://purl.uniprot.org/annotation/VAR_061100|||http://purl.uniprot.org/annotation/VAR_061101|||http://purl.uniprot.org/annotation/VAR_073432|||http://purl.uniprot.org/annotation/VAR_083051|||http://purl.uniprot.org/annotation/VSP_000882
http://togogenome.org/gene/9606:SURF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15527                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphothreonine|||Surfeit locus protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072319|||http://purl.uniprot.org/annotation/VAR_014785|||http://purl.uniprot.org/annotation/VAR_057001
http://togogenome.org/gene/9606:POU2AF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8SAS4|||http://purl.uniprot.org/uniprot/Q8IXP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes interaction with POU2F3.|||Disordered|||OCA|||POU domain class 2-associating factor 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263611
http://togogenome.org/gene/9606:AADAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4W5N8|||http://purl.uniprot.org/uniprot/Q8N5Z0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aminotransferase class I/classII|||Disordered|||In isoform 2.|||Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial|||Mitochondrion|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020602|||http://purl.uniprot.org/annotation/VAR_061005|||http://purl.uniprot.org/annotation/VSP_009874
http://togogenome.org/gene/9606:HELQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDG4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished ATPase and DNA helicase activity.|||Abolished double-stranded DNA-binding.|||Abolishes ATPase and DNA helicase activity.|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Helicase POLQ-like|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329060|||http://purl.uniprot.org/annotation/VAR_042643|||http://purl.uniprot.org/annotation/VAR_055892|||http://purl.uniprot.org/annotation/VAR_055893|||http://purl.uniprot.org/annotation/VAR_055894|||http://purl.uniprot.org/annotation/VAR_061213|||http://purl.uniprot.org/annotation/VSP_032941|||http://purl.uniprot.org/annotation/VSP_032942|||http://purl.uniprot.org/annotation/VSP_032943|||http://purl.uniprot.org/annotation/VSP_032944|||http://purl.uniprot.org/annotation/VSP_032947|||http://purl.uniprot.org/annotation/VSP_032948
http://togogenome.org/gene/9606:BMP8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34820                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Bone morphogenetic protein 8B|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033882|||http://purl.uniprot.org/annotation/PRO_0000033883|||http://purl.uniprot.org/annotation/VAR_014474|||http://purl.uniprot.org/annotation/VSP_056842|||http://purl.uniprot.org/annotation/VSP_056843
http://togogenome.org/gene/9606:ATP11C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB49                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cleavage; by CASP3|||Cleavage; by CASP3 and CASP7|||Cleavage; by CASP3, CASP6 and CASP7|||Cytoplasmic|||Decreases ATPase activity.|||Decreases ATPase flippase activity.|||Decreases sorting to endosomal compartments in response to ca(2+) signaling.|||Di-leucine motif|||Extracellular|||Has minor effect on ATPase flippase activity.|||Has no effect on ATPase flippase activity.|||Has no effect on endoplasmic reticulum to plasma membrane trafficking. Impairs ATPase flippase activity.|||Has no effect on sorting to endosomal compartments in response to ca(2+) signaling.|||Helical|||Impairs ATPase flippase activity.|||Impairs caspase-mediated cleavage; when associated with A-442 and A-448.|||Impairs caspase-mediated cleavage; when associated with A-442 and A-484.|||Impairs caspase-mediated cleavage; when associated with A-448 and A-484.|||Impairs endoplasmic reticulum to plasma membrane trafficking.|||Impairs sorting to endosomal compartments in response to ca(2+) signaling.|||In HACXL; decreased phosphatidylserine translocation from the outer to the inner leaflet of erythrocytes cell membrane.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Localizes to endosomal compartments in the absence of ca(2+) signaling.|||Phospholipid-transporting ATPase IG|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046373|||http://purl.uniprot.org/annotation/VAR_021827|||http://purl.uniprot.org/annotation/VAR_036501|||http://purl.uniprot.org/annotation/VAR_036502|||http://purl.uniprot.org/annotation/VAR_055546|||http://purl.uniprot.org/annotation/VAR_061036|||http://purl.uniprot.org/annotation/VAR_081016|||http://purl.uniprot.org/annotation/VSP_007309|||http://purl.uniprot.org/annotation/VSP_013373|||http://purl.uniprot.org/annotation/VSP_013374
http://togogenome.org/gene/9606:DPAGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HI18|||http://purl.uniprot.org/uniprot/Q9H3H5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Helical; Name=Helix 1|||Helical; Name=Helix 10|||Helical; Name=Helix 2|||Helical; Name=Helix 3|||Helical; Name=Helix 4|||Helical; Name=Helix 5|||Helical; Name=Helix 6|||Helical; Name=Helix 7|||Helical; Name=Helix 8|||Helical; Name=Helix 9|||Impairs protein stability.|||In CDG1J; strongly reduced enzyme activity.|||In CMS13; increased enzyme activity.|||In CMS13; mildly reduced enzyme activity.|||In CMS13; strongly reduced enzyme activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||Lumenal|||Mildly reduced enzyme activity.|||N-linked (GlcNAc...) asparagine|||No significant effect on enzyme activity.|||Reduced enzyme activity.|||Reduces binding to inhibitor. Nearly abolishes enzyme activity.|||Strongly reduced enzyme activity.|||UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000108761|||http://purl.uniprot.org/annotation/VAR_011391|||http://purl.uniprot.org/annotation/VAR_017243|||http://purl.uniprot.org/annotation/VAR_036422|||http://purl.uniprot.org/annotation/VAR_068810|||http://purl.uniprot.org/annotation/VAR_068811|||http://purl.uniprot.org/annotation/VAR_068812|||http://purl.uniprot.org/annotation/VAR_068813|||http://purl.uniprot.org/annotation/VAR_068814|||http://purl.uniprot.org/annotation/VAR_068815|||http://purl.uniprot.org/annotation/VSP_001803|||http://purl.uniprot.org/annotation/VSP_008886
http://togogenome.org/gene/9606:P2RX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93086                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161555|||http://purl.uniprot.org/annotation/VSP_004503|||http://purl.uniprot.org/annotation/VSP_035587|||http://purl.uniprot.org/annotation/VSP_035588
http://togogenome.org/gene/9606:GALR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60755                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Galanin receptor type 3|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069469|||http://purl.uniprot.org/annotation/VAR_049387|||http://purl.uniprot.org/annotation/VAR_059322
http://togogenome.org/gene/9606:PTER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphotriesterase-related protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205364|||http://purl.uniprot.org/annotation/VAR_051610|||http://purl.uniprot.org/annotation/VSP_038342
http://togogenome.org/gene/9606:POMGNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAT1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Fibronectin type-III|||Helical; Signal-anchor for type II membrane protein|||In MDDGA8.|||In MDDGC8; no effect on protein expression; unchanged localization to the endoplasmic reticulum; decreased protein O-GlcNAc transferase catalytic activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249014|||http://purl.uniprot.org/annotation/VAR_068967|||http://purl.uniprot.org/annotation/VAR_081560|||http://purl.uniprot.org/annotation/VAR_081561|||http://purl.uniprot.org/annotation/VAR_081562|||http://purl.uniprot.org/annotation/VAR_081563
http://togogenome.org/gene/9606:WT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19544|||http://purl.uniprot.org/uniprot/Q6PI38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Abolishes sumoylation; when associated with R-177.|||Abolishes sumoylation; when associated with R-77.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Found in a mesothelioma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with target DNA|||In DDS and NPHS4.|||In DDS and WT1.|||In DDS, WT1, MEACHS and NPHS4.|||In DDS.|||In FS.|||In NPHS4.|||In RNA edited version.|||In WT1, DDS and MEACHS.|||In WT1.|||In a patient with hypospadias.|||In isoform 2, isoform 3, isoform 8 and isoform 9.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 6 and isoform 9.|||In isoform 7 and isoform 8.|||KTS motif|||Polar residues|||Pro residues|||Reduced RNA binding.|||Strongly reduced binding of DNA and RNA.|||Wilm's tumour protein N-terminal|||Wilms tumor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047131|||http://purl.uniprot.org/annotation/PRO_5004279522|||http://purl.uniprot.org/annotation/VAR_007739|||http://purl.uniprot.org/annotation/VAR_007740|||http://purl.uniprot.org/annotation/VAR_007741|||http://purl.uniprot.org/annotation/VAR_007742|||http://purl.uniprot.org/annotation/VAR_007743|||http://purl.uniprot.org/annotation/VAR_007744|||http://purl.uniprot.org/annotation/VAR_007745|||http://purl.uniprot.org/annotation/VAR_007746|||http://purl.uniprot.org/annotation/VAR_007747|||http://purl.uniprot.org/annotation/VAR_007748|||http://purl.uniprot.org/annotation/VAR_007749|||http://purl.uniprot.org/annotation/VAR_007750|||http://purl.uniprot.org/annotation/VAR_007751|||http://purl.uniprot.org/annotation/VAR_007752|||http://purl.uniprot.org/annotation/VAR_015053|||http://purl.uniprot.org/annotation/VAR_015054|||http://purl.uniprot.org/annotation/VAR_015055|||http://purl.uniprot.org/annotation/VAR_015056|||http://purl.uniprot.org/annotation/VAR_015057|||http://purl.uniprot.org/annotation/VAR_015058|||http://purl.uniprot.org/annotation/VAR_015059|||http://purl.uniprot.org/annotation/VAR_015060|||http://purl.uniprot.org/annotation/VAR_015061|||http://purl.uniprot.org/annotation/VAR_015062|||http://purl.uniprot.org/annotation/VAR_043798|||http://purl.uniprot.org/annotation/VAR_043799|||http://purl.uniprot.org/annotation/VAR_043800|||http://purl.uniprot.org/annotation/VAR_043801|||http://purl.uniprot.org/annotation/VAR_043802|||http://purl.uniprot.org/annotation/VAR_043803|||http://purl.uniprot.org/annotation/VAR_043804|||http://purl.uniprot.org/annotation/VAR_043805|||http://purl.uniprot.org/annotation/VAR_043806|||http://purl.uniprot.org/annotation/VAR_043807|||http://purl.uniprot.org/annotation/VAR_043808|||http://purl.uniprot.org/annotation/VAR_043809|||http://purl.uniprot.org/annotation/VAR_043810|||http://purl.uniprot.org/annotation/VAR_043811|||http://purl.uniprot.org/annotation/VAR_043812|||http://purl.uniprot.org/annotation/VAR_058021|||http://purl.uniprot.org/annotation/VSP_006866|||http://purl.uniprot.org/annotation/VSP_006867|||http://purl.uniprot.org/annotation/VSP_037582|||http://purl.uniprot.org/annotation/VSP_037583|||http://purl.uniprot.org/annotation/VSP_037584
http://togogenome.org/gene/9606:BCL2L10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YMD5|||http://purl.uniprot.org/uniprot/Q9HD36                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes Ca(2+) binding.|||Abolishes Ca(2+) binding; when associated with N-133.|||Abolishes Ca(2+) binding; when associated with R-131.|||Abolishes interaction with NME2.|||Abolishes ubiquitination. No effect on localization to the mitochondria. No effect on interaction with BCL2L11, BIK, BBC3 or PMAIP1.|||BH1|||BH2|||Bcl-2 Bcl-2 homology region 1-3|||Bcl-2-like protein 10|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Reduces interaction with BECN1 and BCL2L11.|||Required for Ca(2+) binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143068|||http://purl.uniprot.org/annotation/VAR_047113
http://togogenome.org/gene/9606:SOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU8|||http://purl.uniprot.org/uniprot/P08294                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Extracellular superoxide dismutase [Cu-Zn]|||N-linked (Glc) (glycation) lysine; in vitro|||N-linked (GlcNAc...) asparagine|||Not glycated|||Superoxide dismutase [Cu-Zn]|||Superoxide dismutase copper/zinc binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032855|||http://purl.uniprot.org/annotation/PRO_5007491787|||http://purl.uniprot.org/annotation/VAR_014705|||http://purl.uniprot.org/annotation/VAR_020776|||http://purl.uniprot.org/annotation/VAR_020777
http://togogenome.org/gene/9606:POLD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15054                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of PCNA binding.|||DNA polymerase delta subunit 3|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||No effect on sumoylation.|||PIP-box|||Partial loss of PCNA binding (60% of wild-type) and strong decrease of PCNA stimulation of Pol-delta4 polymerase activity.|||Partially loss of sumoylation. Complete loss of SUMO3-sumoylation; when associated with R-285.|||Partially loss of sumoylation. Complete loss of sumoylation; when associated with R-433.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186047|||http://purl.uniprot.org/annotation/VAR_064745|||http://purl.uniprot.org/annotation/VAR_064746|||http://purl.uniprot.org/annotation/VSP_054149|||http://purl.uniprot.org/annotation/VSP_054150
http://togogenome.org/gene/9606:TMEM59L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK28                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Microbody targeting signal|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 59-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003000
http://togogenome.org/gene/9606:ESRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3TZN9|||http://purl.uniprot.org/uniprot/Q6NXG1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Epithelial splicing regulatory protein 1|||In DFNB109; hypomorphic mutation affecting alternative splicing in patient-derived induced pluripotent stem cells and other cell-based assays.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||Omega-N-methylarginine|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273046|||http://purl.uniprot.org/annotation/VAR_030073|||http://purl.uniprot.org/annotation/VAR_080811|||http://purl.uniprot.org/annotation/VSP_022464|||http://purl.uniprot.org/annotation/VSP_022465|||http://purl.uniprot.org/annotation/VSP_022466|||http://purl.uniprot.org/annotation/VSP_022467
http://togogenome.org/gene/9606:ZNF875                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EPW3|||http://purl.uniprot.org/uniprot/P10072|||http://purl.uniprot.org/uniprot/Q7Z6E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 875                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047270|||http://purl.uniprot.org/annotation/VAR_047404|||http://purl.uniprot.org/annotation/VAR_047405|||http://purl.uniprot.org/annotation/VAR_047406|||http://purl.uniprot.org/annotation/VSP_035755
http://togogenome.org/gene/9606:GNG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60262                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7|||N-acetylserine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012635|||http://purl.uniprot.org/annotation/PRO_0000012636
http://togogenome.org/gene/9606:TCEAL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9L2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239211
http://togogenome.org/gene/9606:CCDC70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSX1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 70|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234432|||http://purl.uniprot.org/annotation/VAR_026238|||http://purl.uniprot.org/annotation/VAR_050763
http://togogenome.org/gene/9606:DOLK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z597|||http://purl.uniprot.org/uniprot/Q9UPQ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes dolichol kinase activity.|||CTP-binding|||Cytoplasmic|||Dolichol kinase|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In CDG1M; 2% residual dolichol kinase activity; fails to complement the temperature-sensitive phenotype of DK1-deficient yeast cells.|||In CDG1M; 4% residual dolichol kinase activity; fails to complement the temperature-sensitive phenotype of DK1-deficient yeast cells.|||Lumenal|||No effect on dolichol kinase activity.|||Reduces dolichol kinase activity.|||Reduces dolichol kinase activity. Significant reduction in binding affinity for CTP.|||Reduces dolichol kinase activity. Significant reduction in binding affinity for CTP; when associated with A-471.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072595|||http://purl.uniprot.org/annotation/VAR_032851|||http://purl.uniprot.org/annotation/VAR_032852|||http://purl.uniprot.org/annotation/VAR_049709
http://togogenome.org/gene/9606:DEFB130B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP73|||http://purl.uniprot.org/uniprot/P0DP74                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 130A|||Beta-defensin 130B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045369|||http://purl.uniprot.org/annotation/PRO_0000440984
http://togogenome.org/gene/9606:NUP210L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU65                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BIG2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nuclear pore membrane glycoprotein 210-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236048|||http://purl.uniprot.org/annotation/VAR_050574|||http://purl.uniprot.org/annotation/VSP_053811
http://togogenome.org/gene/9606:STRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3F4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Serine-threonine kinase receptor-associated protein|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051230|||http://purl.uniprot.org/annotation/VSP_056873
http://togogenome.org/gene/9606:LAMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQV4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||Lysosome-associated membrane glycoprotein 3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223695|||http://purl.uniprot.org/annotation/VAR_025343|||http://purl.uniprot.org/annotation/VAR_030827
http://togogenome.org/gene/9606:TMEM258                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61165                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylmethionine|||Transmembrane protein 258                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221142
http://togogenome.org/gene/9606:CNPY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B7I2                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein canopy homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314015
http://togogenome.org/gene/9606:TRIM38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00635                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM38|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056256|||http://purl.uniprot.org/annotation/VAR_013513
http://togogenome.org/gene/9606:ALDH1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTJ7|||http://purl.uniprot.org/uniprot/P30837                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase|||Aldehyde dehydrogenase X, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007172|||http://purl.uniprot.org/annotation/VAR_002257|||http://purl.uniprot.org/annotation/VAR_002258|||http://purl.uniprot.org/annotation/VAR_029891|||http://purl.uniprot.org/annotation/VAR_029892
http://togogenome.org/gene/9606:SERPINB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50453                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Site                                                                                  ^@                                                                                  Chain|||Modified Residue|||Site                                                                                  ^@                                                                                  N-acetylmethionine|||Reactive bond|||Serpin B9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094113
http://togogenome.org/gene/9606:CACNB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTK1|||http://purl.uniprot.org/uniprot/A0A1B0GTP5|||http://purl.uniprot.org/uniprot/A0A1B0GTX8|||http://purl.uniprot.org/uniprot/H0Y476|||http://purl.uniprot.org/uniprot/O00305                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase/L-type calcium channel beta subunit|||In EA5; associated with susceptibility to EIG9.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||Voltage-dependent L-type calcium channel subunit beta-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144060|||http://purl.uniprot.org/annotation/VAR_013669|||http://purl.uniprot.org/annotation/VSP_000635|||http://purl.uniprot.org/annotation/VSP_043192|||http://purl.uniprot.org/annotation/VSP_043193
http://togogenome.org/gene/9606:SLC50A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXX5|||http://purl.uniprot.org/uniprot/Q5SR67|||http://purl.uniprot.org/uniprot/Q9BRV3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||Mediates interaction with TRPV2|||MtN3/slv 1|||MtN3/slv 2|||Sugar transporter SWEET1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345116|||http://purl.uniprot.org/annotation/VSP_034916|||http://purl.uniprot.org/annotation/VSP_034917|||http://purl.uniprot.org/annotation/VSP_034918
http://togogenome.org/gene/9606:CENPJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8P1|||http://purl.uniprot.org/uniprot/F6VUX8|||http://purl.uniprot.org/uniprot/Q9HC77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-589.|||Abolishes phosphorylation by PLK2 and procentriole formation; when associated with A-595.|||Alpha/beta-tubulin binding|||Basic and acidic residues|||Centromere protein J|||Centromere protein J C-terminal|||Decreases interaction with alpha/beta-tubulin; disrupts association with microtubule distal tip; no effect on association with microtubule lattice; when associated with A-375.|||Decreases interaction with alpha/beta-tubulin; disrupts association with microtubule distal tip; no effect on association with microtubule lattice; when associated with A-385.|||Decreases interaction with alpha/beta-tubulin; disrupts association with microtubule distal tip; no effect on association with microtubule lattice; when associated with E-377.|||Decreases interaction with alpha/beta-tubulin; disrupts association with microtubule distal tip; no effect on association with microtubule lattice; when associated with E-378.|||Decreases interaction with alpha/beta-tubulin; when associated with A-338 and A-339.|||Decreases interaction with alpha/beta-tubulin; when associated with A-338 and A-341.|||Decreases interaction with alpha/beta-tubulin; when associated with A-339 and A-341.|||Disordered|||In MCPH6; reduced interaction with STIL.|||In isoform 2.|||Interaction with STIL|||Phosphoserine|||Phosphoserine; by PLK2|||Phosphoserine; by PLK2 and PLK4|||Polar residues|||Slightly decreases interaction with alpha/beta-tubulin; causes overly long daughter centrioles and enhances ciliary length; when associated with A-343.|||Slightly decreases interaction with alpha/beta-tubulin; causes overly long daughter centrioles and enhances ciliary length; when associated with A-344.|||Strongly decreases interaction with alpha/beta-tubulin; causes shorter centrioles and doublet microtubules in cilia.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089480|||http://purl.uniprot.org/annotation/VAR_032427|||http://purl.uniprot.org/annotation/VAR_032428|||http://purl.uniprot.org/annotation/VAR_032429|||http://purl.uniprot.org/annotation/VAR_032430|||http://purl.uniprot.org/annotation/VAR_032431|||http://purl.uniprot.org/annotation/VAR_032432|||http://purl.uniprot.org/annotation/VAR_032433|||http://purl.uniprot.org/annotation/VSP_056831|||http://purl.uniprot.org/annotation/VSP_056832
http://togogenome.org/gene/9606:CERKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49MI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Ceramide kinase-like protein|||DAGKc|||Disordered|||In RP26.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Loss of nuclear localization; in isoform 2.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Only cytoplasmic.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181356|||http://purl.uniprot.org/annotation/VAR_053688|||http://purl.uniprot.org/annotation/VAR_053689|||http://purl.uniprot.org/annotation/VAR_065182|||http://purl.uniprot.org/annotation/VSP_016653|||http://purl.uniprot.org/annotation/VSP_016654|||http://purl.uniprot.org/annotation/VSP_016655|||http://purl.uniprot.org/annotation/VSP_016656|||http://purl.uniprot.org/annotation/VSP_016657|||http://purl.uniprot.org/annotation/VSP_016658|||http://purl.uniprot.org/annotation/VSP_016659|||http://purl.uniprot.org/annotation/VSP_016660|||http://purl.uniprot.org/annotation/VSP_042663
http://togogenome.org/gene/9606:RUBCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PY84|||http://purl.uniprot.org/uniprot/Q8N4U6|||http://purl.uniprot.org/uniprot/Q92622                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912, G-915 and L-920.|||Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912, L-920 and G-923.|||Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-912,G-915 and G-923.|||Disrupts interaction with Rab7, translocation to cytoplasm; when associated with G-915, L-920 and G-923.|||Disrupts interaction with YWHAB.|||In isoform 2.|||In isoform 3.|||Interaction with BECN1|||Interaction with CARD9|||Interaction with CYBA|||Interaction with PIK3C3|||Interaction with Rab7|||Interaction with UVRAG|||Interaction with YWHAB|||Phosphoserine|||Polar residues|||RUN|||Run domain Beclin-1-interacting and cysteine-rich domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050736|||http://purl.uniprot.org/annotation/VSP_039160|||http://purl.uniprot.org/annotation/VSP_039161|||http://purl.uniprot.org/annotation/VSP_039471|||http://purl.uniprot.org/annotation/VSP_039472|||http://purl.uniprot.org/annotation/VSP_039473
http://togogenome.org/gene/9606:HMGXB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z641|||http://purl.uniprot.org/uniprot/Q9UGU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DUF4171|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||HMG domain-containing protein 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048542|||http://purl.uniprot.org/annotation/VAR_049559
http://togogenome.org/gene/9606:HSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULV5                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation. Greatly reduced sumoylation. Greatly increased transactivational activity.|||Abolishes sumoylation. 10-fold increased in transactivational activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Heat shock factor protein 4|||Hydrophobic repeat HR-A/B|||Hydrophobic repeat HR-C|||In CTRCT5; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair.|||In CTRCT5; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction.|||In CTRCT5; sporadic.|||In CTRCT5; sporadic; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair.|||In CTRCT5; unknown pathological significance; decreased binding to the DNASE2B promoter and decreased DNASE2B expression; impaired RAD51 induction and UVC-induced DNA damage repair.|||In isoform HSF4A.|||Interactions with DUSP26, MAPK1 and MAPK2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124571|||http://purl.uniprot.org/annotation/VAR_017558|||http://purl.uniprot.org/annotation/VAR_017559|||http://purl.uniprot.org/annotation/VAR_017560|||http://purl.uniprot.org/annotation/VAR_017561|||http://purl.uniprot.org/annotation/VAR_029018|||http://purl.uniprot.org/annotation/VSP_002418
http://togogenome.org/gene/9606:FMN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBL1|||http://purl.uniprot.org/uniprot/Q9NZ56                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with SPIRE1.|||Basic and acidic residues|||Blocks accumulation in the nucleus in response to DNA damage.|||Disordered|||FH1|||FH2|||Formin-2|||Important for interaction with SPIRE1|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Strongly reduces interaction with SPIRE1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194888|||http://purl.uniprot.org/annotation/VAR_033932|||http://purl.uniprot.org/annotation/VAR_049094|||http://purl.uniprot.org/annotation/VAR_059290|||http://purl.uniprot.org/annotation/VSP_056095
http://togogenome.org/gene/9606:RSAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA92                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrion|||Radical S-adenosyl methionine domain-containing protein 1, mitochondrial|||Radical SAM core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284609|||http://purl.uniprot.org/annotation/VAR_031777|||http://purl.uniprot.org/annotation/VAR_031778|||http://purl.uniprot.org/annotation/VAR_061126|||http://purl.uniprot.org/annotation/VSP_056130|||http://purl.uniprot.org/annotation/VSP_056131|||http://purl.uniprot.org/annotation/VSP_056132
http://togogenome.org/gene/9606:DDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV24|||http://purl.uniprot.org/uniprot/A0A0S2Z3N4|||http://purl.uniprot.org/uniprot/P20711|||http://purl.uniprot.org/uniprot/Q53Y41                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X approximate tandem repeats|||Aromatic-L-amino-acid decarboxylase|||In AADCD.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146939|||http://purl.uniprot.org/annotation/VAR_014788|||http://purl.uniprot.org/annotation/VAR_014789|||http://purl.uniprot.org/annotation/VAR_014790|||http://purl.uniprot.org/annotation/VAR_019214|||http://purl.uniprot.org/annotation/VAR_019215|||http://purl.uniprot.org/annotation/VAR_019216|||http://purl.uniprot.org/annotation/VAR_019217|||http://purl.uniprot.org/annotation/VAR_019309|||http://purl.uniprot.org/annotation/VAR_046137|||http://purl.uniprot.org/annotation/VAR_046138|||http://purl.uniprot.org/annotation/VAR_046139|||http://purl.uniprot.org/annotation/VAR_046140|||http://purl.uniprot.org/annotation/VAR_046141|||http://purl.uniprot.org/annotation/VAR_046142|||http://purl.uniprot.org/annotation/VAR_046143|||http://purl.uniprot.org/annotation/VAR_046144|||http://purl.uniprot.org/annotation/VSP_046569|||http://purl.uniprot.org/annotation/VSP_046570|||http://purl.uniprot.org/annotation/VSP_047175|||http://purl.uniprot.org/annotation/VSP_047176
http://togogenome.org/gene/9606:VPS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPR6|||http://purl.uniprot.org/uniprot/Q8N3P4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||RING-type; atypical|||Vacuolar protein sorting-associated protein 8 central|||Vacuolar protein sorting-associated protein 8 homolog|||WD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278267|||http://purl.uniprot.org/annotation/VAR_030730|||http://purl.uniprot.org/annotation/VAR_030731|||http://purl.uniprot.org/annotation/VAR_030732|||http://purl.uniprot.org/annotation/VAR_030733|||http://purl.uniprot.org/annotation/VSP_023249|||http://purl.uniprot.org/annotation/VSP_023250
http://togogenome.org/gene/9606:PREP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAH7|||http://purl.uniprot.org/uniprot/P48147                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||N-acetylmethionine|||N6-acetyllysine|||Peptidase S9 prolyl oligopeptidase catalytic|||Peptidase S9A N-terminal|||Prolyl endopeptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122401|||http://purl.uniprot.org/annotation/VAR_047790|||http://purl.uniprot.org/annotation/VAR_047791
http://togogenome.org/gene/9606:PPP1R21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMI0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In NEDHFBA.|||In NEDHFBA; unknown pathological significance.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphothreonine|||Protein phosphatase 1 regulatory subunit 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286098|||http://purl.uniprot.org/annotation/VAR_082035|||http://purl.uniprot.org/annotation/VAR_082036|||http://purl.uniprot.org/annotation/VAR_084655|||http://purl.uniprot.org/annotation/VAR_085954|||http://purl.uniprot.org/annotation/VSP_024984|||http://purl.uniprot.org/annotation/VSP_024985|||http://purl.uniprot.org/annotation/VSP_024986|||http://purl.uniprot.org/annotation/VSP_024987|||http://purl.uniprot.org/annotation/VSP_043216
http://togogenome.org/gene/9606:VSIR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7M9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||V-type immunoglobulin domain-containing suppressor of T-cell activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014765|||http://purl.uniprot.org/annotation/VAR_028036
http://togogenome.org/gene/9606:BRWD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6RI45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo 1|||Bromo 2|||Bromodomain and WD repeat-containing protein 3|||Disordered|||In XLID93; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283089|||http://purl.uniprot.org/annotation/VAR_031491|||http://purl.uniprot.org/annotation/VAR_036940|||http://purl.uniprot.org/annotation/VSP_024303|||http://purl.uniprot.org/annotation/VSP_024304|||http://purl.uniprot.org/annotation/VSP_024305|||http://purl.uniprot.org/annotation/VSP_024306|||http://purl.uniprot.org/annotation/VSP_024307
http://togogenome.org/gene/9606:CDHR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV98|||http://purl.uniprot.org/uniprot/Q58EZ6|||http://purl.uniprot.org/uniprot/Q9HBB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4 X 31 AA approximate tandem repeats|||4; truncated|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin-related family member 5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Loss of binding to CDHR2.|||Loss of interaction with USH1C.|||Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organization|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004012|||http://purl.uniprot.org/annotation/PRO_5002803889|||http://purl.uniprot.org/annotation/PRO_5004252054|||http://purl.uniprot.org/annotation/VAR_017920|||http://purl.uniprot.org/annotation/VAR_017921|||http://purl.uniprot.org/annotation/VAR_059192|||http://purl.uniprot.org/annotation/VAR_060412|||http://purl.uniprot.org/annotation/VAR_060413|||http://purl.uniprot.org/annotation/VSP_050692|||http://purl.uniprot.org/annotation/VSP_050693
http://togogenome.org/gene/9606:MPND                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N594|||http://purl.uniprot.org/uniprot/W4VSR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||JAMM motif|||MPN|||MPN domain-containing protein|||N-acetylalanine|||Phosphoserine|||RAMA|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278804|||http://purl.uniprot.org/annotation/VSP_023400|||http://purl.uniprot.org/annotation/VSP_023401
http://togogenome.org/gene/9606:TENT5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWP2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases substantially the interaction with PLK4. Weakens binding to PLK4; when associated with E-230 and E-321.|||Decreases substantially the interaction with PLK4. Weakens binding to PLK4; when associated with E-230 and E-321. Abolishes the inhibitory effect of TENT5C on the cell viability; when associated with E-320 and E-321.|||Does not affect colocalization with PLK4 in centrosome. Increases cell viability.|||Loss of poly(a) polymerase activity.|||Slightly decreases the binding to PLK4; when associated with E-320. Abolishes the inhibitory effect of TENT5C on the cell viability; when associated with P-144 and E-320.|||Slightly decreases the binding to PLK4; when associated with E-321. Abolishes the inhibitory effect of TENT5C on the cell viability; when associated with P-144 and E-321.|||Terminal nucleotidyltransferase 5C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259933|||http://purl.uniprot.org/annotation/VAR_060132
http://togogenome.org/gene/9606:TMEM154                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Transmembrane protein 154                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284503|||http://purl.uniprot.org/annotation/VAR_031755
http://togogenome.org/gene/9606:THADA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YHU6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||tRNA (32-2'-O)-methyltransferase regulator THADA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344057|||http://purl.uniprot.org/annotation/VAR_054070|||http://purl.uniprot.org/annotation/VAR_054071|||http://purl.uniprot.org/annotation/VAR_054072|||http://purl.uniprot.org/annotation/VAR_054073|||http://purl.uniprot.org/annotation/VAR_054074|||http://purl.uniprot.org/annotation/VAR_054075|||http://purl.uniprot.org/annotation/VAR_054076|||http://purl.uniprot.org/annotation/VSP_034730|||http://purl.uniprot.org/annotation/VSP_034731|||http://purl.uniprot.org/annotation/VSP_034732|||http://purl.uniprot.org/annotation/VSP_034733|||http://purl.uniprot.org/annotation/VSP_034734|||http://purl.uniprot.org/annotation/VSP_034735|||http://purl.uniprot.org/annotation/VSP_054421|||http://purl.uniprot.org/annotation/VSP_054422
http://togogenome.org/gene/9606:DENND6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWF6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||N6-methyllysine|||Phosphoserine|||Protein DENND6A|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289116
http://togogenome.org/gene/9606:ZNF717                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J5W8|||http://purl.uniprot.org/uniprot/C9JVC3|||http://purl.uniprot.org/uniprot/Q9BY31                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16; degenerate|||C2H2-type 17; degenerate|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 717                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333738
http://togogenome.org/gene/9606:CBY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV5|||http://purl.uniprot.org/uniprot/Q8NA61                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Protein chibby homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307291|||http://purl.uniprot.org/annotation/VAR_054064|||http://purl.uniprot.org/annotation/VSP_028673|||http://purl.uniprot.org/annotation/VSP_028674
http://togogenome.org/gene/9606:TBC1D10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E244|||http://purl.uniprot.org/uniprot/B7ZVY9|||http://purl.uniprot.org/uniprot/Q9BXI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Basic and acidic residues|||Binding to the PDZ domain of EBP50|||Disordered|||Glutamine finger|||In isoform 2.|||Loss of activity. No effect on subcellular location.|||Loss of interaction with EBP50 and impaired subcellular localization.|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 10A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208035|||http://purl.uniprot.org/annotation/VAR_052541|||http://purl.uniprot.org/annotation/VSP_043119
http://togogenome.org/gene/9606:SLC35G5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KT7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA 1|||EamA 2|||Helical|||Solute carrier family 35 member G5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269556|||http://purl.uniprot.org/annotation/VAR_059579|||http://purl.uniprot.org/annotation/VAR_059580
http://togogenome.org/gene/9606:MRPL50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5N7                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein mL50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261659|||http://purl.uniprot.org/annotation/VAR_029474|||http://purl.uniprot.org/annotation/VSP_056091
http://togogenome.org/gene/9606:LYVE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R672|||http://purl.uniprot.org/uniprot/Q9Y5Y7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Link|||Lymphatic vessel endothelial hyaluronic acid receptor 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252133|||http://purl.uniprot.org/annotation/PRO_5014298307|||http://purl.uniprot.org/annotation/VAR_027763|||http://purl.uniprot.org/annotation/VAR_027764|||http://purl.uniprot.org/annotation/VAR_027765
http://togogenome.org/gene/9606:REG3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW15                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lectin|||EPN|||In isoform 2.|||Regenerating islet-derived protein 3-gamma 15 kDa form|||Regenerating islet-derived protein 3-gamma 16.5 kDa form|||Sufficient to activate EXTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017434|||http://purl.uniprot.org/annotation/PRO_0000422751|||http://purl.uniprot.org/annotation/PRO_0000422752|||http://purl.uniprot.org/annotation/VSP_045169
http://togogenome.org/gene/9606:TP53AIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||p53-regulated apoptosis-inducing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300813|||http://purl.uniprot.org/annotation/VAR_059735|||http://purl.uniprot.org/annotation/VSP_027865|||http://purl.uniprot.org/annotation/VSP_027866|||http://purl.uniprot.org/annotation/VSP_027867|||http://purl.uniprot.org/annotation/VSP_027868
http://togogenome.org/gene/9606:KMO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K693|||http://purl.uniprot.org/uniprot/O15229                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes NADPH oxidase activity.|||Abolishes kynurenine 3-monooxygenase activity.|||Decreases to 30% NADPH oxidase activity.|||Decreases to 50% NADPH oxidase activity.|||FAD-binding|||Helical|||In isoform 2.|||In isoform 3.|||Kynurenine 3-monooxygenase|||N-linked (GlcNAc...) asparagine|||Not glycosylted. Reduces to 80% kynurenine 3-monooxygenase activity.|||Strongly decreases kynurenine 3-monooxygenase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229742|||http://purl.uniprot.org/annotation/VAR_030845|||http://purl.uniprot.org/annotation/VSP_051972|||http://purl.uniprot.org/annotation/VSP_051973
http://togogenome.org/gene/9606:KRTAP5-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8G9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184104|||http://purl.uniprot.org/annotation/VAR_062155
http://togogenome.org/gene/9606:MTRF1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMX1|||http://purl.uniprot.org/uniprot/Q9UGC7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  GGQ|||GGQ domain|||Impaired mitochondrial peptide chain release factor activity.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N5-methylglutamine|||Peptide chain release factor 1-like, mitochondrial|||Prokaryotic-type class I peptide chain release factors                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330944|||http://purl.uniprot.org/annotation/VAR_042725|||http://purl.uniprot.org/annotation/VAR_042726|||http://purl.uniprot.org/annotation/VAR_042727|||http://purl.uniprot.org/annotation/VAR_042728|||http://purl.uniprot.org/annotation/VSP_033139|||http://purl.uniprot.org/annotation/VSP_033140|||http://purl.uniprot.org/annotation/VSP_033141|||http://purl.uniprot.org/annotation/VSP_033142
http://togogenome.org/gene/9606:SECISBP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93073                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of binding to SELV and TXNRD1 SECIS elements.|||Phosphoserine|||Polar residues|||Selenocysteine insertion sequence-binding protein 2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050739|||http://purl.uniprot.org/annotation/VSP_016342
http://togogenome.org/gene/9606:SLC4A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBS3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases the water flux across the plasma membrane.|||Extracellular|||Helical|||In CDPD.|||In CHED.|||In CHED; affects protein processing and folding.|||In CHED; affects protein processing and transport to the cell surface.|||In CHED; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED mutant.|||In CHED; affects protein processing; the mutant protein is retained intracellularly; coexpression with wild-type protein partially rescues the cell surface trafficking of CHED2 mutant.|||In CHED; deafness not assessed.|||In CHED; does not facilitate water flux across the plasma membrane; decreases proton flux with or without cotransport of ammonia; does not affect protein processing.|||In FECD4; affects protein processing and transport to the cell surface; the mutant protein is retained intracellularly; coexpression with wild-type protein does not rescue the cell surface trafficking of FECD4 mutant.|||In FECD4; decreases cell surface expression; abolishes functional activity.|||In FECD4; decreases cell surface expression; highly reduces functional activity.|||In FECD4; does not interfere with post-translational processing; the mutant protein partially localizes to the cytoplasm.|||In FECD4; interferes with post-translational processing; the mutant protein localizes to the cytoplasm.|||In FECD4; interferes with post-translational processing; the mutant protein partially localizes to the cytoplasm.|||In FECD4; slightly decreases cell surface expression; reduces.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 4 member 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079236|||http://purl.uniprot.org/annotation/VAR_015521|||http://purl.uniprot.org/annotation/VAR_015522|||http://purl.uniprot.org/annotation/VAR_015523|||http://purl.uniprot.org/annotation/VAR_015524|||http://purl.uniprot.org/annotation/VAR_030662|||http://purl.uniprot.org/annotation/VAR_030663|||http://purl.uniprot.org/annotation/VAR_030664|||http://purl.uniprot.org/annotation/VAR_030665|||http://purl.uniprot.org/annotation/VAR_034944|||http://purl.uniprot.org/annotation/VAR_034945|||http://purl.uniprot.org/annotation/VAR_034946|||http://purl.uniprot.org/annotation/VAR_034947|||http://purl.uniprot.org/annotation/VAR_034948|||http://purl.uniprot.org/annotation/VAR_034949|||http://purl.uniprot.org/annotation/VAR_034950|||http://purl.uniprot.org/annotation/VAR_034951|||http://purl.uniprot.org/annotation/VAR_034952|||http://purl.uniprot.org/annotation/VAR_034953|||http://purl.uniprot.org/annotation/VAR_034954|||http://purl.uniprot.org/annotation/VAR_047806|||http://purl.uniprot.org/annotation/VAR_047807|||http://purl.uniprot.org/annotation/VAR_047808|||http://purl.uniprot.org/annotation/VAR_047809|||http://purl.uniprot.org/annotation/VAR_047810|||http://purl.uniprot.org/annotation/VAR_047811|||http://purl.uniprot.org/annotation/VAR_047812|||http://purl.uniprot.org/annotation/VAR_047813|||http://purl.uniprot.org/annotation/VAR_063713|||http://purl.uniprot.org/annotation/VAR_063714|||http://purl.uniprot.org/annotation/VAR_063715|||http://purl.uniprot.org/annotation/VAR_063716|||http://purl.uniprot.org/annotation/VAR_063717|||http://purl.uniprot.org/annotation/VAR_063718|||http://purl.uniprot.org/annotation/VAR_064422|||http://purl.uniprot.org/annotation/VAR_064423|||http://purl.uniprot.org/annotation/VAR_064424|||http://purl.uniprot.org/annotation/VAR_064425|||http://purl.uniprot.org/annotation/VAR_064426|||http://purl.uniprot.org/annotation/VAR_064427|||http://purl.uniprot.org/annotation/VAR_064428|||http://purl.uniprot.org/annotation/VAR_064978|||http://purl.uniprot.org/annotation/VAR_064979|||http://purl.uniprot.org/annotation/VAR_064980|||http://purl.uniprot.org/annotation/VAR_064981|||http://purl.uniprot.org/annotation/VAR_064982|||http://purl.uniprot.org/annotation/VAR_064983|||http://purl.uniprot.org/annotation/VAR_064984|||http://purl.uniprot.org/annotation/VAR_064985|||http://purl.uniprot.org/annotation/VAR_067272|||http://purl.uniprot.org/annotation/VAR_074015|||http://purl.uniprot.org/annotation/VAR_075537|||http://purl.uniprot.org/annotation/VAR_075538|||http://purl.uniprot.org/annotation/VAR_075539|||http://purl.uniprot.org/annotation/VSP_061106|||http://purl.uniprot.org/annotation/VSP_061107|||http://purl.uniprot.org/annotation/VSP_061108|||http://purl.uniprot.org/annotation/VSP_061109
http://togogenome.org/gene/9606:HOGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XE5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-fold decrease in kcat and a nearly 8-fold increase in KM.|||2.5-fold decrease in kcat and 4.2 fold increase in KM.|||25-fold increase in KM.|||4-hydroxy-2-oxoglutarate aldolase, mitochondrial|||6-fold increase in KM.|||7-fold increase in KM.|||In HP3.|||In isoform 2.|||Involved in proton transfer during cleavage|||Mitochondrion|||No change in activity.|||No enzymatic activity.|||Schiff-base intermediate with substrate|||Significant loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273346|||http://purl.uniprot.org/annotation/VAR_064035|||http://purl.uniprot.org/annotation/VAR_064036|||http://purl.uniprot.org/annotation/VAR_064037|||http://purl.uniprot.org/annotation/VSP_022515
http://togogenome.org/gene/9606:DNAAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5Z4|||http://purl.uniprot.org/uniprot/Q8WXU2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CS|||Dynein axonemal assembly factor 4|||In isoform 2.|||In isoform 3.|||Mediates interaction with ESR1 and STUB1|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106284|||http://purl.uniprot.org/annotation/VAR_017383|||http://purl.uniprot.org/annotation/VAR_017384|||http://purl.uniprot.org/annotation/VAR_017385|||http://purl.uniprot.org/annotation/VAR_017386|||http://purl.uniprot.org/annotation/VAR_026214|||http://purl.uniprot.org/annotation/VAR_026215|||http://purl.uniprot.org/annotation/VSP_011822|||http://purl.uniprot.org/annotation/VSP_011823|||http://purl.uniprot.org/annotation/VSP_041379
http://togogenome.org/gene/9606:FAM124B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5Z6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Protein FAM124B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286384|||http://purl.uniprot.org/annotation/VAR_060151|||http://purl.uniprot.org/annotation/VSP_025042|||http://purl.uniprot.org/annotation/VSP_025043
http://togogenome.org/gene/9606:ADORA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30542                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adenosine receptor A1|||Cytoplasmic|||Extracellular|||Found in a family with early-onset autosomal recessive parkinsonism and intellectual disability; unknown pathological significance; does not affect protein abundance; does not affect expression at the cell surface.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068991|||http://purl.uniprot.org/annotation/VAR_035754|||http://purl.uniprot.org/annotation/VAR_044138|||http://purl.uniprot.org/annotation/VAR_044139|||http://purl.uniprot.org/annotation/VAR_044140|||http://purl.uniprot.org/annotation/VAR_044141|||http://purl.uniprot.org/annotation/VAR_078549|||http://purl.uniprot.org/annotation/VSP_034401|||http://purl.uniprot.org/annotation/VSP_034402
http://togogenome.org/gene/9606:KDM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5P8|||http://purl.uniprot.org/uniprot/A0A0S2Z5T1|||http://purl.uniprot.org/uniprot/Q8N371                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bifunctional peptidase and arginyl-hydroxylase JMJD5|||Fails to cleave H3C1.|||In isoform 2.|||In isoform 3.|||Interaction with RCCD1|||JmjC|||Loss of H3K36me2 demethylase activity.|||Loss of L-arginyl 3-hydroxylase activity toward RPS6.|||Loss of L-arginyl 3-hydroxylase activity toward RPS6. Loss of peptidase activity toward methylated histones.|||Loss of L-arginyl 3-hydroxylase activity toward RPS6. Loss of peptidase activity toward methylated histones; when associated with A-323 and A-400. No effect on its regulatory function on the circadian clock or CRY1 stability.|||Loss of interaction with H3C1. Fails to cleave H3C1.|||Loss of peptidase activity toward methylated histones.|||Loss of peptidase activity toward methylated histones; when associated with A-321 and A-323.|||Loss of peptidase activity toward methylated histones; when associated with A-321 and A-400.|||No effect on L-arginyl 3-hydroxylase activity toward RPS6.|||Reduces L-arginyl 3-hydroxylase activity toward RPS6 substrate.|||Reduces L-arginyl 3-hydroxylase activity toward RPS6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292010|||http://purl.uniprot.org/annotation/VAR_032928|||http://purl.uniprot.org/annotation/VSP_026370|||http://purl.uniprot.org/annotation/VSP_039893
http://togogenome.org/gene/9606:FAM107B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H098                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Protein FAM107B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230774|||http://purl.uniprot.org/annotation/VSP_037527
http://togogenome.org/gene/9606:PLPPR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6T4P5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 3|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317529|||http://purl.uniprot.org/annotation/VAR_038544|||http://purl.uniprot.org/annotation/VAR_038545|||http://purl.uniprot.org/annotation/VSP_031004|||http://purl.uniprot.org/annotation/VSP_031005|||http://purl.uniprot.org/annotation/VSP_031006
http://togogenome.org/gene/9606:UBQLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||12 X 3 AA tandem repeats of P-X-X|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||In ALS15.|||In ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1 and FAF2; increases translocation of HNRNPA1 to the cytoplasm; adversely affects ERAD.|||In ALS15; leads to defective ubiquitin-mediated proteasomal degradation; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm.|||In ALS15; reduces binding to HNRNPA1; increases translocation of HNRNPA1 to the cytoplasm.|||In ALS15; uncertain pathological significance.|||N-acetylalanine|||Polar residues|||Probable disease-associated variant found in a patient with frontotemporal dementia.|||Removed|||STI1 1|||STI1 2|||STI1 3|||STI1 4|||UBA|||Ubiquilin-2|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211011|||http://purl.uniprot.org/annotation/VAR_052680|||http://purl.uniprot.org/annotation/VAR_066562|||http://purl.uniprot.org/annotation/VAR_066563|||http://purl.uniprot.org/annotation/VAR_066564|||http://purl.uniprot.org/annotation/VAR_066565|||http://purl.uniprot.org/annotation/VAR_066566|||http://purl.uniprot.org/annotation/VAR_068892|||http://purl.uniprot.org/annotation/VAR_068893|||http://purl.uniprot.org/annotation/VAR_068894|||http://purl.uniprot.org/annotation/VAR_068895|||http://purl.uniprot.org/annotation/VAR_068896|||http://purl.uniprot.org/annotation/VAR_068897
http://togogenome.org/gene/9606:RABL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3YEC7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||Interaction with CDKN2A|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rab-like protein 6|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274223|||http://purl.uniprot.org/annotation/VAR_030210|||http://purl.uniprot.org/annotation/VSP_022646|||http://purl.uniprot.org/annotation/VSP_022647|||http://purl.uniprot.org/annotation/VSP_022648|||http://purl.uniprot.org/annotation/VSP_022649|||http://purl.uniprot.org/annotation/VSP_042559|||http://purl.uniprot.org/annotation/VSP_042560
http://togogenome.org/gene/9606:TTC36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLP5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332179|||http://purl.uniprot.org/annotation/VAR_042972|||http://purl.uniprot.org/annotation/VSP_055760
http://togogenome.org/gene/9606:FAM170B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM170B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310494|||http://purl.uniprot.org/annotation/VAR_037062
http://togogenome.org/gene/9606:CD3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07766                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITAM|||Ig-like|||NUMB-binding region|||Phosphotyrosine|||T-cell surface glycoprotein CD3 epsilon chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014607
http://togogenome.org/gene/9606:DISP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MBM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Polar residues|||Protein dispatched homolog 2|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310696|||http://purl.uniprot.org/annotation/VAR_037078|||http://purl.uniprot.org/annotation/VAR_037079|||http://purl.uniprot.org/annotation/VAR_037080|||http://purl.uniprot.org/annotation/VAR_037081|||http://purl.uniprot.org/annotation/VAR_037082
http://togogenome.org/gene/9606:SUCLG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53597                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MTDPS9.|||In MTDPS9; with progressive liver disease and recurrent hepatic failure.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial|||Tele-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033340|||http://purl.uniprot.org/annotation/VAR_065120|||http://purl.uniprot.org/annotation/VAR_065121|||http://purl.uniprot.org/annotation/VAR_065157|||http://purl.uniprot.org/annotation/VAR_076432
http://togogenome.org/gene/9606:NDUFB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17568                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||N-myristoyl glycine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118811|||http://purl.uniprot.org/annotation/VAR_050591
http://togogenome.org/gene/9606:CLYBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0X4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes citramalyl-CoA lyase activity.|||Citramalyl-CoA lyase, mitochondrial|||In isoform 2.|||Loss of the protein product; reduction of circulating vitamin B12.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286389|||http://purl.uniprot.org/annotation/VAR_032099|||http://purl.uniprot.org/annotation/VAR_032100|||http://purl.uniprot.org/annotation/VAR_032101|||http://purl.uniprot.org/annotation/VAR_073420|||http://purl.uniprot.org/annotation/VSP_034643
http://togogenome.org/gene/9606:ZBTB7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95365                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Decreased transcription repressor activity, dominant negative effect. Increased glycolysis and cell proliferation, dominant negative effect. No effect on nuclear localization.|||Decreased transcription repressor activity. Acts as a dominant negative. No effect on nuclear localization.|||Decreased transcription repressor activity. No effect on nuclear localization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MNDLFH.|||In MNDLFH; unknown pathological significance.|||Increased proteasomal degradation. No effect on nuclear localization.|||Loss of sumoylation with SUMO1. May decrease interaction with transcriptional corepressors.|||Mediates interaction with KHDRBS1|||Mediates interaction with RELA|||Mediates interaction with SMAD4|||No effect on sumoylation with SUMO1. Decreased transcription repression activity. No effect on promoter binding.|||No effect on sumoylation with SUMO1. No effect on promoter binding.|||No effect on sumoylation with SUMO1. No effect on promoter binding. No effect on nuclear localization.|||No effect on transcription repressor activity. No effect on nuclear localization.|||Phosphoserine|||Zinc finger and BTB domain-containing protein 7A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047715|||http://purl.uniprot.org/annotation/VAR_086968|||http://purl.uniprot.org/annotation/VAR_086969|||http://purl.uniprot.org/annotation/VAR_086970|||http://purl.uniprot.org/annotation/VAR_086971|||http://purl.uniprot.org/annotation/VAR_086972|||http://purl.uniprot.org/annotation/VAR_086973
http://togogenome.org/gene/9606:MDFI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AKB6|||http://purl.uniprot.org/uniprot/Q99750                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||MDFI|||MyoD family inhibitor|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096324
http://togogenome.org/gene/9606:TBC1D7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPB9|||http://purl.uniprot.org/uniprot/Q9P0N9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished formation of the TSC-TBC complex; when associated with 81-A--A-84.|||Abolished formation of the TSC-TBC complex; when associated with A-121. Abolished interaction with TSC1 and TSC2; when associated with 94-A-A-95.|||Abolished interaction with TSC1.|||Abolished interaction with TSC1. Abolished interaction with TSC1 and TSC2; when associated with A-81--A-84.|||Decreased interaction with TSC1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Rab-GAP TBC|||TBC1 domain family member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208031|||http://purl.uniprot.org/annotation/VAR_052537|||http://purl.uniprot.org/annotation/VAR_052538|||http://purl.uniprot.org/annotation/VSP_041480|||http://purl.uniprot.org/annotation/VSP_044186|||http://purl.uniprot.org/annotation/VSP_044892
http://togogenome.org/gene/9606:GIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FC3|||http://purl.uniprot.org/uniprot/Q9Y2X7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ARF GTPase-activating protein GIT1|||Arf-GAP|||C4-type|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with ARHGEF7|||Interaction with IKBKG|||Interaction with MAPK1|||Interaction with NCK2 and GRIN3A|||Interaction with PCLO|||Interaction with PTK2/FAK1|||Interaction with PXN and TGFB1I1|||Interaction with gamma-tubulin and localization to the centrosome|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Required for localization at synapses|||When transfected to cells, increased number of multinucleated cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074200|||http://purl.uniprot.org/annotation/VSP_009666|||http://purl.uniprot.org/annotation/VSP_009667|||http://purl.uniprot.org/annotation/VSP_040984
http://togogenome.org/gene/9606:PARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L3T8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  In DEE75; unknown pathological significance.|||Mitochondrion|||Probable proline--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035818|||http://purl.uniprot.org/annotation/VAR_034527|||http://purl.uniprot.org/annotation/VAR_052644|||http://purl.uniprot.org/annotation/VAR_082149|||http://purl.uniprot.org/annotation/VAR_082617|||http://purl.uniprot.org/annotation/VAR_082618|||http://purl.uniprot.org/annotation/VAR_082619|||http://purl.uniprot.org/annotation/VAR_082620|||http://purl.uniprot.org/annotation/VAR_082621
http://togogenome.org/gene/9606:CORO1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coronin-1C|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050926|||http://purl.uniprot.org/annotation/VSP_047727|||http://purl.uniprot.org/annotation/VSP_047728
http://togogenome.org/gene/9606:NKX1-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UD57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||NK1 transcription factor-related protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325972
http://togogenome.org/gene/9606:IRS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14654                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CRK-binding|||Disordered|||GRB2-binding|||IRS-type PTB|||In CHNG9.|||In a colorectal cancer sample; somatic mutation.|||Insulin receptor substrate 4|||No effect. Reduces interaction with CRK by 50%; when associated with F-700. Abolishes interaction with CRK; when associated with F-700; F-743 and F-779.|||No effect. Reduces interaction with CRK by 50%; when associated with F-717. Abolishes interaction with CRK; when associated with F-717; F-743 and F-779.|||No effect. Reduces interaction with CRK by 50%; when associated with F-743. Abolishes interaction with CRK; when associated with F-700; F-717 and F-743.|||No effect. Reduces interaction with CRK by 50%; when associated with F-779. Abolishes interaction with CRK; when associated with F-700; F-717 and F-779.|||PH|||Phosphotyrosine|||Polar residues|||Pro residues|||YXXM motif 1|||YXXM motif 2|||YXXM motif 3|||YXXM motif 4|||YXXM motif 5|||YXXM motif 6|||YXXM motif 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314678|||http://purl.uniprot.org/annotation/VAR_038042|||http://purl.uniprot.org/annotation/VAR_038043|||http://purl.uniprot.org/annotation/VAR_038044|||http://purl.uniprot.org/annotation/VAR_051078|||http://purl.uniprot.org/annotation/VAR_051079|||http://purl.uniprot.org/annotation/VAR_051080|||http://purl.uniprot.org/annotation/VAR_061669|||http://purl.uniprot.org/annotation/VAR_083291
http://togogenome.org/gene/9606:ATPAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TC12                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase mitochondrial F1 complex assembly factor 1|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318915|||http://purl.uniprot.org/annotation/VAR_038906|||http://purl.uniprot.org/annotation/VSP_045437|||http://purl.uniprot.org/annotation/VSP_045438
http://togogenome.org/gene/9606:KIAA1614                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein KIAA1614                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313645|||http://purl.uniprot.org/annotation/VAR_037682|||http://purl.uniprot.org/annotation/VAR_037683|||http://purl.uniprot.org/annotation/VAR_037684|||http://purl.uniprot.org/annotation/VAR_037685|||http://purl.uniprot.org/annotation/VAR_063118|||http://purl.uniprot.org/annotation/VSP_030081
http://togogenome.org/gene/9606:OR4F6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV96|||http://purl.uniprot.org/uniprot/Q8NGB9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150548
http://togogenome.org/gene/9606:SPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16150                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD43 cytoplasmic tail|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Leukosialin|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphothreonine|||Reduced nuclear localization. Loss of nuclear localization; when associated with 282-P-G-283.|||Reduced nuclear localization. Loss of nuclear localization; when associated with 295-P-G-296.|||Required for interaction with EZR, MSN and RDX and for co-localization to microvilli                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021588|||http://purl.uniprot.org/annotation/PRO_0000443406|||http://purl.uniprot.org/annotation/VAR_051091|||http://purl.uniprot.org/annotation/VAR_051092
http://togogenome.org/gene/9606:PLEK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYT0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  DEP|||N-acetylmethionine|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053862|||http://purl.uniprot.org/annotation/VAR_050504
http://togogenome.org/gene/9606:TPRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W33                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein adipocyte-associated 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076099|||http://purl.uniprot.org/annotation/VSP_016932|||http://purl.uniprot.org/annotation/VSP_016933|||http://purl.uniprot.org/annotation/VSP_016934|||http://purl.uniprot.org/annotation/VSP_016935
http://togogenome.org/gene/9606:SCML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MBT 1|||MBT 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||Sex comb on midleg-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097628|||http://purl.uniprot.org/annotation/VSP_010277
http://togogenome.org/gene/9606:AGRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C6SUN5|||http://purl.uniprot.org/uniprot/O00253                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Abolishes inhibition of cAMP production in response to melanocortin receptor stimulation.|||Agouti|||Agouti-related protein|||Cleavage is blocked.|||Cleavage; by PCSK1|||Interaction with melanocortin receptors|||May play a role in obesity in an age-dependent manner; apparently no effect on activity.|||No effect on cleavage.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001034|||http://purl.uniprot.org/annotation/PRO_0000434044|||http://purl.uniprot.org/annotation/PRO_5014302140|||http://purl.uniprot.org/annotation/VAR_015385
http://togogenome.org/gene/9606:BASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80723                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Brain acid soluble protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142895|||http://purl.uniprot.org/annotation/VAR_048396|||http://purl.uniprot.org/annotation/VSP_037994
http://togogenome.org/gene/9606:LAMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2D6|||http://purl.uniprot.org/uniprot/Q9Y6N6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||Domain II and I|||In OCCM.|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; first part|||Laminin EGF-like 5; second part|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin IV type A|||Laminin N-terminal|||Laminin subunit gamma-3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017079|||http://purl.uniprot.org/annotation/PRO_5004311064|||http://purl.uniprot.org/annotation/VAR_056145|||http://purl.uniprot.org/annotation/VAR_056146|||http://purl.uniprot.org/annotation/VAR_056147|||http://purl.uniprot.org/annotation/VAR_056148|||http://purl.uniprot.org/annotation/VAR_056149|||http://purl.uniprot.org/annotation/VAR_066404
http://togogenome.org/gene/9606:ITGA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23229                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by PLAU in invasive prostate cancer|||Cytoplasmic|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 7.|||In isoform 9.|||In isoform Alpha-6X1A and isoform Alpha-6X1B.|||In isoform Alpha-6X1A, isoform Alpha-6X2A, isoform Alpha-6X1X2A, isoform 7 and isoform 9.|||In isoform Alpha-6X2A, isoform Alpha-6X2B and isoform 7.|||Integrin alpha-6|||Integrin alpha-6 heavy chain|||Integrin alpha-6 light chain|||Interaction with HPS5|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Processed integrin alpha-6|||S-palmitoyl cysteine; by DHHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016258|||http://purl.uniprot.org/annotation/PRO_0000016259|||http://purl.uniprot.org/annotation/PRO_0000016260|||http://purl.uniprot.org/annotation/PRO_0000425742|||http://purl.uniprot.org/annotation/VSP_002723|||http://purl.uniprot.org/annotation/VSP_002724|||http://purl.uniprot.org/annotation/VSP_002725|||http://purl.uniprot.org/annotation/VSP_036406|||http://purl.uniprot.org/annotation/VSP_036407
http://togogenome.org/gene/9606:FGFR1OP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVK5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form FGFR1OP2-FGFR1|||Disordered|||FGFR1 oncogene partner 2|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299041|||http://purl.uniprot.org/annotation/VSP_027538|||http://purl.uniprot.org/annotation/VSP_027539|||http://purl.uniprot.org/annotation/VSP_027540
http://togogenome.org/gene/9606:ODC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXF8|||http://purl.uniprot.org/uniprot/P11926                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  25% decrease of in vitro nitrosylation level.|||In BABS.|||In BABS; gain-of-function variant resulting in increased putrescine biosynthesis as indicated by higher amount of putrescine in patient red blood cells compared to controls; increased ODC1 protein levels in patient red blood cells.|||N6-(pyridoxal phosphate)lysine|||Orn/DAP/Arg decarboxylase 2 C-terminal|||Orn/DAP/Arg decarboxylase 2 N-terminal|||Ornithine decarboxylase|||Phosphoserine; by CK2|||Proton donor; shared with dimeric partner|||S-nitrosocysteine; in inhibited form|||Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149891|||http://purl.uniprot.org/annotation/VAR_085000|||http://purl.uniprot.org/annotation/VAR_085001
http://togogenome.org/gene/9606:TGM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08188                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by CTSL|||N-acetylalanine|||Phosphothreonine|||Phosphotyrosine|||Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain|||Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033652|||http://purl.uniprot.org/annotation/PRO_0000033653|||http://purl.uniprot.org/annotation/VAR_040067|||http://purl.uniprot.org/annotation/VAR_040068|||http://purl.uniprot.org/annotation/VAR_040069|||http://purl.uniprot.org/annotation/VAR_040070|||http://purl.uniprot.org/annotation/VAR_040071|||http://purl.uniprot.org/annotation/VAR_055360
http://togogenome.org/gene/9606:IFT88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL7|||http://purl.uniprot.org/uniprot/B3KX42|||http://purl.uniprot.org/uniprot/Q13099                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 3.|||In isoform 3.|||Intraflagellar transport protein 88 homolog|||Polar residues|||TPR|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106391|||http://purl.uniprot.org/annotation/VAR_046464|||http://purl.uniprot.org/annotation/VAR_046465|||http://purl.uniprot.org/annotation/VAR_046466|||http://purl.uniprot.org/annotation/VSP_060641|||http://purl.uniprot.org/annotation/VSP_060642
http://togogenome.org/gene/9606:LINS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG48                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In MRT27; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Protein Lines homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317749|||http://purl.uniprot.org/annotation/VAR_038668|||http://purl.uniprot.org/annotation/VAR_038669|||http://purl.uniprot.org/annotation/VAR_038670|||http://purl.uniprot.org/annotation/VAR_038671|||http://purl.uniprot.org/annotation/VAR_038672|||http://purl.uniprot.org/annotation/VAR_038673|||http://purl.uniprot.org/annotation/VAR_038674|||http://purl.uniprot.org/annotation/VAR_078341|||http://purl.uniprot.org/annotation/VSP_031142|||http://purl.uniprot.org/annotation/VSP_031143|||http://purl.uniprot.org/annotation/VSP_031144|||http://purl.uniprot.org/annotation/VSP_031145
http://togogenome.org/gene/9606:PERM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SV97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||PGC-1 and ERR-induced regulator in muscle protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299540|||http://purl.uniprot.org/annotation/VSP_027731|||http://purl.uniprot.org/annotation/VSP_053677
http://togogenome.org/gene/9606:ME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48163                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for activity|||In isoform 2.|||N-acetylmethionine|||NADP-dependent malic enzyme|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160192|||http://purl.uniprot.org/annotation/VSP_057051
http://togogenome.org/gene/9606:GPRASP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G protein-coupled receptor associated sorting protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334662|||http://purl.uniprot.org/annotation/VAR_049266|||http://purl.uniprot.org/annotation/VAR_049267
http://togogenome.org/gene/9606:SMPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60906                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Important for substrate recognition|||Proton acceptor|||Sphingomyelin phosphodiesterase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075686|||http://purl.uniprot.org/annotation/VAR_024181|||http://purl.uniprot.org/annotation/VAR_050305|||http://purl.uniprot.org/annotation/VAR_050306
http://togogenome.org/gene/9606:PPP1R17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8N7|||http://purl.uniprot.org/uniprot/O96001                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphothreonine; by PKG/PRKG1|||Protein phosphatase 1 regulatory subunit 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083869|||http://purl.uniprot.org/annotation/VAR_027838|||http://purl.uniprot.org/annotation/VAR_051025|||http://purl.uniprot.org/annotation/VSP_042736
http://togogenome.org/gene/9606:GREM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XAA7|||http://purl.uniprot.org/uniprot/B3KTR9|||http://purl.uniprot.org/uniprot/O60565                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CTCK|||Disordered|||Gremlin|||Gremlin-1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006714|||http://purl.uniprot.org/annotation/PRO_5014212459|||http://purl.uniprot.org/annotation/VSP_013321
http://togogenome.org/gene/9606:CUL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14999                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cullin-7|||DOC|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||In 3M1.|||In 3M1; impairs the ability to interact with RBX1, thus hampers the assembly of polyubiquitin chains.|||In 3M1; requires 2 nucleotide substitutions.|||In 3M1; unknown pathological significance.|||In isoform 2.|||Interaction with TP53|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119802|||http://purl.uniprot.org/annotation/VAR_026121|||http://purl.uniprot.org/annotation/VAR_026122|||http://purl.uniprot.org/annotation/VAR_026123|||http://purl.uniprot.org/annotation/VAR_026124|||http://purl.uniprot.org/annotation/VAR_048841|||http://purl.uniprot.org/annotation/VAR_048842|||http://purl.uniprot.org/annotation/VAR_048843|||http://purl.uniprot.org/annotation/VAR_071120|||http://purl.uniprot.org/annotation/VSP_046105|||http://purl.uniprot.org/annotation/VSP_046106
http://togogenome.org/gene/9606:UNC79                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SHN5|||http://purl.uniprot.org/uniprot/Q9P2D8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Protein unc-79 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315618|||http://purl.uniprot.org/annotation/VAR_038260|||http://purl.uniprot.org/annotation/VAR_038261|||http://purl.uniprot.org/annotation/VAR_038262|||http://purl.uniprot.org/annotation/VAR_038263|||http://purl.uniprot.org/annotation/VSP_030583|||http://purl.uniprot.org/annotation/VSP_030584
http://togogenome.org/gene/9606:CFAP36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G28                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 36|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278638|||http://purl.uniprot.org/annotation/VAR_030795|||http://purl.uniprot.org/annotation/VAR_030796|||http://purl.uniprot.org/annotation/VAR_050725|||http://purl.uniprot.org/annotation/VSP_023338
http://togogenome.org/gene/9606:USP24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPU5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proton acceptor|||UBA|||USP|||Ubiquitin carboxyl-terminal hydrolase 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080652|||http://purl.uniprot.org/annotation/VAR_047154|||http://purl.uniprot.org/annotation/VAR_047155|||http://purl.uniprot.org/annotation/VAR_047156|||http://purl.uniprot.org/annotation/VAR_047157
http://togogenome.org/gene/9606:TSPYL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY4|||http://purl.uniprot.org/uniprot/Q8N831                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Testis-specific Y-encoded-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307279|||http://purl.uniprot.org/annotation/VAR_035395|||http://purl.uniprot.org/annotation/VAR_035396|||http://purl.uniprot.org/annotation/VAR_035397|||http://purl.uniprot.org/annotation/VAR_035398
http://togogenome.org/gene/9606:NOVA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNW9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KH 1|||KH 2|||KH 3|||Loss of alternative splicing regulation.|||RNA-binding protein Nova-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050119
http://togogenome.org/gene/9606:FBXO34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 34|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119926|||http://purl.uniprot.org/annotation/VAR_021489|||http://purl.uniprot.org/annotation/VAR_021490|||http://purl.uniprot.org/annotation/VAR_049047|||http://purl.uniprot.org/annotation/VAR_049048
http://togogenome.org/gene/9606:IGF2BP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00425                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Insulin-like growth factor 2 mRNA-binding protein 3|||KH 1|||KH 2|||KH 3|||KH 4|||Loss of interaction with m6A-modified mRNA; when associated with 422-E-E-423. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 422-E-E-423.|||Loss of interaction with m6A-modified mRNA; when associated with 505-E-E-506. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 505-E-E-506.|||Partial reduction in interaction with m6A-modified mRNA; when associated with E-213. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; 422-E-E-423 and 505-E-E-506.|||Partial reduction in interaction with m6A-modified mRNA; when associated with E-294. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-294; 422-E-E-423 and 505-E-E-506.|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282538|||http://purl.uniprot.org/annotation/VSP_024172
http://togogenome.org/gene/9606:ECD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95905                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic region required for transactivation activity|||Acidic residues|||Decreases transactivation activity.|||Disordered|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-572 and A-579.|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-572 and A-584.|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-518, A-579 and A-584.|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-505, A-572, A-579 and A-584.|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-503, A-518, A-572, A-579 and A-584.|||Greatly impairs in vitro phosphorylation by CK2 and impairs cell cycle regulation activity; when associated with A-505, A-518, A-572, A-579 and A-584.|||In isoform 2.|||In isoform 3.|||Increases transactivation activity.|||Involved in nuclear export|||Phosphoserine|||Protein ecdysoneless homolog|||Transcription activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220844|||http://purl.uniprot.org/annotation/VAR_012191|||http://purl.uniprot.org/annotation/VAR_051970|||http://purl.uniprot.org/annotation/VAR_051971|||http://purl.uniprot.org/annotation/VAR_051972|||http://purl.uniprot.org/annotation/VAR_051973|||http://purl.uniprot.org/annotation/VSP_045670|||http://purl.uniprot.org/annotation/VSP_045671
http://togogenome.org/gene/9606:RCE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P5W4|||http://purl.uniprot.org/uniprot/Q9Y256                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  CAAX prenyl protease 2|||Helical|||In a breast cancer sample; somatic mutation.|||N-acetylalanine|||Proton donor/acceptor|||Removed|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194830|||http://purl.uniprot.org/annotation/VAR_036407
http://togogenome.org/gene/9606:NT5DC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UY8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5'-nucleotidase domain-containing protein 3|||Disordered|||In isoform 2.|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326247|||http://purl.uniprot.org/annotation/VAR_040043|||http://purl.uniprot.org/annotation/VSP_032643|||http://purl.uniprot.org/annotation/VSP_032644
http://togogenome.org/gene/9606:WAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TM35|||http://purl.uniprot.org/uniprot/P42768                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Actin nucleation-promoting factor WAS|||CRIB|||Disordered|||Found in a patient with THC1; unknown pathological significance.|||GRSGPLPPXP motif 1|||GRSGPLPPXP motif 2|||In THC1.|||In WAS and THC1.|||In WAS.|||In WAS; attenuated form.|||In WAS; found in a patient with MRT52.|||In WAS; mild form.|||In WAS; moderate form.|||In WAS; severe form.|||In XLN; a constitutively activating mutation.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphotyrosine; by FYN and HCK|||Polar residues|||Pro residues|||Removed|||WH1|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188990|||http://purl.uniprot.org/annotation/VAR_005823|||http://purl.uniprot.org/annotation/VAR_005824|||http://purl.uniprot.org/annotation/VAR_005825|||http://purl.uniprot.org/annotation/VAR_005826|||http://purl.uniprot.org/annotation/VAR_005827|||http://purl.uniprot.org/annotation/VAR_005828|||http://purl.uniprot.org/annotation/VAR_005829|||http://purl.uniprot.org/annotation/VAR_005830|||http://purl.uniprot.org/annotation/VAR_005831|||http://purl.uniprot.org/annotation/VAR_005832|||http://purl.uniprot.org/annotation/VAR_005833|||http://purl.uniprot.org/annotation/VAR_005834|||http://purl.uniprot.org/annotation/VAR_005835|||http://purl.uniprot.org/annotation/VAR_005836|||http://purl.uniprot.org/annotation/VAR_005837|||http://purl.uniprot.org/annotation/VAR_005838|||http://purl.uniprot.org/annotation/VAR_005839|||http://purl.uniprot.org/annotation/VAR_008105|||http://purl.uniprot.org/annotation/VAR_008106|||http://purl.uniprot.org/annotation/VAR_008107|||http://purl.uniprot.org/annotation/VAR_008108|||http://purl.uniprot.org/annotation/VAR_008109|||http://purl.uniprot.org/annotation/VAR_008110|||http://purl.uniprot.org/annotation/VAR_012710|||http://purl.uniprot.org/annotation/VAR_012711|||http://purl.uniprot.org/annotation/VAR_022806|||http://purl.uniprot.org/annotation/VAR_022807|||http://purl.uniprot.org/annotation/VAR_033255|||http://purl.uniprot.org/annotation/VAR_033256|||http://purl.uniprot.org/annotation/VAR_033257|||http://purl.uniprot.org/annotation/VAR_074020
http://togogenome.org/gene/9606:MESD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14696                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chaperone domain|||Disordered|||Escort domain|||In OI20.|||In isoform 2.|||LRP chaperone MESD|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096443|||http://purl.uniprot.org/annotation/VAR_083534|||http://purl.uniprot.org/annotation/VSP_055492|||http://purl.uniprot.org/annotation/VSP_055493
http://togogenome.org/gene/9606:ZDHHC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N966                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||Lumenal|||Palmitoyltransferase ZDHHC22|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212911
http://togogenome.org/gene/9606:OSTC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUD3|||http://purl.uniprot.org/uniprot/Q9NRP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Oligosaccharyltransferase complex subunit OSTC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320602|||http://purl.uniprot.org/annotation/VAR_039231|||http://purl.uniprot.org/annotation/VSP_047376
http://togogenome.org/gene/9606:STX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z425|||http://purl.uniprot.org/uniprot/Q12846                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Interaction with CENPF|||Phosphoserine|||Phosphothreonine|||Required for neurite tip localization|||Syntaxin-4|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210202|||http://purl.uniprot.org/annotation/VSP_054603
http://togogenome.org/gene/9606:DCANP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF63                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Dendritic cell nuclear protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229790|||http://purl.uniprot.org/annotation/VAR_025758|||http://purl.uniprot.org/annotation/VAR_025759
http://togogenome.org/gene/9606:CPA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1M2|||http://purl.uniprot.org/uniprot/B2RCS8|||http://purl.uniprot.org/uniprot/Q8WXQ8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase A5|||In isoform 2.|||In isoform 3.|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004361|||http://purl.uniprot.org/annotation/PRO_0000004362|||http://purl.uniprot.org/annotation/VAR_017191|||http://purl.uniprot.org/annotation/VAR_017192|||http://purl.uniprot.org/annotation/VAR_017193|||http://purl.uniprot.org/annotation/VAR_048596|||http://purl.uniprot.org/annotation/VSP_008806|||http://purl.uniprot.org/annotation/VSP_008807|||http://purl.uniprot.org/annotation/VSP_044866
http://togogenome.org/gene/9606:ANO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75V66                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin-5|||Cytoplasmic|||Extracellular|||Helical|||In GDD.|||In GDD; unknown pathological significance.|||In LGMDR12.|||In LGMDR12; unknown pathological significance.|||In MMD3 and LGMDR12; unknown pathological significance.|||In MMD3; unknown pathological significance.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191755|||http://purl.uniprot.org/annotation/VAR_023524|||http://purl.uniprot.org/annotation/VAR_023525|||http://purl.uniprot.org/annotation/VAR_052339|||http://purl.uniprot.org/annotation/VAR_052340|||http://purl.uniprot.org/annotation/VAR_063582|||http://purl.uniprot.org/annotation/VAR_063583|||http://purl.uniprot.org/annotation/VAR_068247|||http://purl.uniprot.org/annotation/VAR_068248|||http://purl.uniprot.org/annotation/VAR_076476|||http://purl.uniprot.org/annotation/VAR_076477|||http://purl.uniprot.org/annotation/VAR_080271|||http://purl.uniprot.org/annotation/VAR_080272|||http://purl.uniprot.org/annotation/VAR_080273|||http://purl.uniprot.org/annotation/VAR_080274|||http://purl.uniprot.org/annotation/VAR_080275|||http://purl.uniprot.org/annotation/VAR_080276|||http://purl.uniprot.org/annotation/VAR_080277|||http://purl.uniprot.org/annotation/VAR_080278|||http://purl.uniprot.org/annotation/VAR_080279|||http://purl.uniprot.org/annotation/VAR_080280|||http://purl.uniprot.org/annotation/VAR_080281|||http://purl.uniprot.org/annotation/VAR_080282|||http://purl.uniprot.org/annotation/VAR_080283|||http://purl.uniprot.org/annotation/VAR_080284|||http://purl.uniprot.org/annotation/VAR_080285|||http://purl.uniprot.org/annotation/VAR_080286|||http://purl.uniprot.org/annotation/VAR_080287|||http://purl.uniprot.org/annotation/VAR_080288|||http://purl.uniprot.org/annotation/VAR_080289|||http://purl.uniprot.org/annotation/VAR_080290|||http://purl.uniprot.org/annotation/VAR_080291|||http://purl.uniprot.org/annotation/VAR_080292|||http://purl.uniprot.org/annotation/VAR_080293|||http://purl.uniprot.org/annotation/VAR_080294|||http://purl.uniprot.org/annotation/VAR_080295|||http://purl.uniprot.org/annotation/VAR_080296|||http://purl.uniprot.org/annotation/VAR_080297|||http://purl.uniprot.org/annotation/VAR_080298|||http://purl.uniprot.org/annotation/VAR_080301
http://togogenome.org/gene/9606:GAB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2WGN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||GRB2-associated-binding protein 4|||PH|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271192|||http://purl.uniprot.org/annotation/VAR_053098
http://togogenome.org/gene/9606:PSMB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28074                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity.|||Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108.|||Displays resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with V-109.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Proteasome subunit beta type-5|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026589|||http://purl.uniprot.org/annotation/PRO_0000026590|||http://purl.uniprot.org/annotation/VAR_051549|||http://purl.uniprot.org/annotation/VSP_041263|||http://purl.uniprot.org/annotation/VSP_045686
http://togogenome.org/gene/9606:POLR2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15514                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073981
http://togogenome.org/gene/9606:TCEAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239206|||http://purl.uniprot.org/annotation/VAR_034546|||http://purl.uniprot.org/annotation/VAR_034547
http://togogenome.org/gene/9606:TTC39A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY6|||http://purl.uniprot.org/uniprot/A0A7P0T922|||http://purl.uniprot.org/uniprot/B7Z4W9|||http://purl.uniprot.org/uniprot/F6WE04|||http://purl.uniprot.org/uniprot/Q5SRH9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 39A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291996|||http://purl.uniprot.org/annotation/VSP_026348|||http://purl.uniprot.org/annotation/VSP_026349|||http://purl.uniprot.org/annotation/VSP_026350|||http://purl.uniprot.org/annotation/VSP_026351|||http://purl.uniprot.org/annotation/VSP_026352|||http://purl.uniprot.org/annotation/VSP_026353|||http://purl.uniprot.org/annotation/VSP_047198
http://togogenome.org/gene/9606:RDH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ELF7|||http://purl.uniprot.org/uniprot/Q9NYR8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Proton acceptor|||Retinol dehydrogenase 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305972|||http://purl.uniprot.org/annotation/VAR_035232|||http://purl.uniprot.org/annotation/VAR_035233
http://togogenome.org/gene/9606:PYDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/W6CW81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Pyrin|||Pyrin domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000445598
http://togogenome.org/gene/9606:THUMPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV44                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  THUMP|||tRNA (guanine(6)-N2)-methyltransferase THUMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259769|||http://purl.uniprot.org/annotation/VAR_028976
http://togogenome.org/gene/9606:MOB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70IA6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||MOB kinase activator 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193568|||http://purl.uniprot.org/annotation/VSP_012298|||http://purl.uniprot.org/annotation/VSP_012299|||http://purl.uniprot.org/annotation/VSP_044472
http://togogenome.org/gene/9606:ADPRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LIE5|||http://purl.uniprot.org/uniprot/W0NWJ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcineurin-like phosphoesterase|||In isoform 2.|||Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286567|||http://purl.uniprot.org/annotation/VAR_032125|||http://purl.uniprot.org/annotation/VAR_032126|||http://purl.uniprot.org/annotation/VSP_025092|||http://purl.uniprot.org/annotation/VSP_025093
http://togogenome.org/gene/9606:RNF216                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8N1|||http://purl.uniprot.org/uniprot/Q9NWF9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates ubiquitin chain formation activity.|||Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF216|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||IBR-type|||In GDHS.|||In isoform 2.|||In isoform 3.|||Mild reduced activity.|||Phosphoserine|||Phosphoserine; by MAPK1|||Polar residues|||RING-type|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056293|||http://purl.uniprot.org/annotation/VAR_070048|||http://purl.uniprot.org/annotation/VAR_070049|||http://purl.uniprot.org/annotation/VSP_012443|||http://purl.uniprot.org/annotation/VSP_012444
http://togogenome.org/gene/9606:DIRAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HU8                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||GTP-binding protein Di-Ras2|||Phosphoserine|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191650|||http://purl.uniprot.org/annotation/PRO_0000370777
http://togogenome.org/gene/9606:BRCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38398                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with BRIP1.|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Breast cancer type 1 susceptibility protein|||Could be associated with cancer susceptibility; major splicing aberration identified with this mutant.|||Could be associated with cancer susceptibility; multifactorial likelihood analysis provides evidence for pathogenicity.|||Disordered|||Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity.|||Does not abolish ABRAXAS1 binding, but abolishes formation of a heterotetramer with ABRAXAS1.|||Does not abolish ABRAXAS1 binding, but impairs formation of a heterotetramer with ABRAXAS1.|||Found in breast and ovarian cancer patients; unknown pathological significance.|||Found in breast cancer; unknown pathological significance.|||Found in breast-ovarian cancer patients; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs formation of a heterotetramer with ABRAXAS1.|||In BC and BROVCA1.|||In BC and FANCS; unknown pathological significance; Decreased localization to DNA damage sites and reduced interaction with UIMC1/RAP80.|||In BC and ovarian cancer; no interaction with BAP1.|||In BC and ovarian cancer; unknown pathological significance; decreased interaction with PALB2.|||In BC, BROVCA1 and OC; unknown pathological significance.|||In BC, ovarian cancer and FANCS; impairs protein stability; functionally impaired in vitro.|||In BC.|||In BC; abolishes ACACA binding.|||In BC; alters protein stability and abolishes ACACA and BRIP1 binding.|||In BC; no interaction with BAP1.|||In BC; strongly reduced transcription transactivation; abolishes interaction with BRIP1 and RBBP8.|||In BC; unknown pathological significance.|||In BC; unknown pathological significance; functionally impaired in vitro.|||In BC; unknown pathological significance; functionally neutral in vitro.|||In BC; unknown pathological significance; functionally neutral in vitro; no effect on in vitro phosphorylation by ATR.|||In BC; unknown pathological significance; strongly reduces affinity for a BRIP1 phosphopeptide; functionally impaired in vitro.|||In BROVCA1.|||In BROVCA1; unknown pathological significance.|||In FANCS.|||In a breast cancer sample; somatic mutation.|||In a patient with sporadic breast cancer; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In ovarian cancer.|||In ovarian cancer; unknown pathological significance.|||In ovarian cancer; unknown pathological significance; abolishes ACACA binding and strongly reduces BRIP1 binding.|||In some patients with sporadic breast cancer; unknown pathological significance.|||Inhibition of the infrared-induced G2 arrest. Reduces phosphorylation by ATR.|||Interaction with PALB2|||Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR.|||Mildly reduces affinity for a BRIP1 phosphopeptide.|||N-acetylmethionine|||No change in infrared S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR.|||No effect on affinity for a BRIP1 phosphopeptide.|||No effect on in vitro phosphorylation by ATR.|||No effect on interaction with BAP1.|||No ubiquitination of RBBP8. No restoration RBBP8-mediated focus formation or G2/M checkpoint control upon DNA damage.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by ATM and ATR|||Phosphoserine; by ATR; in vitro|||Phosphoserine; by CHEK2|||Phosphothreonine; by ATR; in vitro|||Polar residues|||RING-type|||Reduces in vitro phosphorylation by ATR.|||Slightly reduces affinity for a BRIP1 phosphopeptide.|||Strongly reduces affinity for a BRIP1 phosphopeptide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055830|||http://purl.uniprot.org/annotation/VAR_007754|||http://purl.uniprot.org/annotation/VAR_007755|||http://purl.uniprot.org/annotation/VAR_007756|||http://purl.uniprot.org/annotation/VAR_007757|||http://purl.uniprot.org/annotation/VAR_007758|||http://purl.uniprot.org/annotation/VAR_007759|||http://purl.uniprot.org/annotation/VAR_007760|||http://purl.uniprot.org/annotation/VAR_007761|||http://purl.uniprot.org/annotation/VAR_007762|||http://purl.uniprot.org/annotation/VAR_007763|||http://purl.uniprot.org/annotation/VAR_007764|||http://purl.uniprot.org/annotation/VAR_007765|||http://purl.uniprot.org/annotation/VAR_007766|||http://purl.uniprot.org/annotation/VAR_007767|||http://purl.uniprot.org/annotation/VAR_007768|||http://purl.uniprot.org/annotation/VAR_007769|||http://purl.uniprot.org/annotation/VAR_007770|||http://purl.uniprot.org/annotation/VAR_007771|||http://purl.uniprot.org/annotation/VAR_007772|||http://purl.uniprot.org/annotation/VAR_007773|||http://purl.uniprot.org/annotation/VAR_007774|||http://purl.uniprot.org/annotation/VAR_007775|||http://purl.uniprot.org/annotation/VAR_007776|||http://purl.uniprot.org/annotation/VAR_007777|||http://purl.uniprot.org/annotation/VAR_007778|||http://purl.uniprot.org/annotation/VAR_007779|||http://purl.uniprot.org/annotation/VAR_007780|||http://purl.uniprot.org/annotation/VAR_007781|||http://purl.uniprot.org/annotation/VAR_007782|||http://purl.uniprot.org/annotation/VAR_007783|||http://purl.uniprot.org/annotation/VAR_007784|||http://purl.uniprot.org/annotation/VAR_007785|||http://purl.uniprot.org/annotation/VAR_007786|||http://purl.uniprot.org/annotation/VAR_007787|||http://purl.uniprot.org/annotation/VAR_007788|||http://purl.uniprot.org/annotation/VAR_007789|||http://purl.uniprot.org/annotation/VAR_007790|||http://purl.uniprot.org/annotation/VAR_007791|||http://purl.uniprot.org/annotation/VAR_007792|||http://purl.uniprot.org/annotation/VAR_007793|||http://purl.uniprot.org/annotation/VAR_007794|||http://purl.uniprot.org/annotation/VAR_007795|||http://purl.uniprot.org/annotation/VAR_007796|||http://purl.uniprot.org/annotation/VAR_007797|||http://purl.uniprot.org/annotation/VAR_007798|||http://purl.uniprot.org/annotation/VAR_007799|||http://purl.uniprot.org/annotation/VAR_008759|||http://purl.uniprot.org/annotation/VAR_008760|||http://purl.uniprot.org/annotation/VAR_008761|||http://purl.uniprot.org/annotation/VAR_008762|||http://purl.uniprot.org/annotation/VAR_008763|||http://purl.uniprot.org/annotation/VAR_008764|||http://purl.uniprot.org/annotation/VAR_008765|||http://purl.uniprot.org/annotation/VAR_019944|||http://purl.uniprot.org/annotation/VAR_019945|||http://purl.uniprot.org/annotation/VAR_019946|||http://purl.uniprot.org/annotation/VAR_020110|||http://purl.uniprot.org/annotation/VAR_020111|||http://purl.uniprot.org/annotation/VAR_020112|||http://purl.uniprot.org/annotation/VAR_020679|||http://purl.uniprot.org/annotation/VAR_020680|||http://purl.uniprot.org/annotation/VAR_020681|||http://purl.uniprot.org/annotation/VAR_020682|||http://purl.uniprot.org/annotation/VAR_020683|||http://purl.uniprot.org/annotation/VAR_020684|||http://purl.uniprot.org/annotation/VAR_020685|||http://purl.uniprot.org/annotation/VAR_020686|||http://purl.uniprot.org/annotation/VAR_020687|||http://purl.uniprot.org/annotation/VAR_020688|||http://purl.uniprot.org/annotation/VAR_020689|||http://purl.uniprot.org/annotation/VAR_020690|||http://purl.uniprot.org/annotation/VAR_020691|||http://purl.uniprot.org/annotation/VAR_020692|||http://purl.uniprot.org/annotation/VAR_020693|||http://purl.uniprot.org/annotation/VAR_020694|||http://purl.uniprot.org/annotation/VAR_020695|||http://purl.uniprot.org/annotation/VAR_020696|||http://purl.uniprot.org/annotation/VAR_020697|||http://purl.uniprot.org/annotation/VAR_020698|||http://purl.uniprot.org/annotation/VAR_020699|||http://purl.uniprot.org/annotation/VAR_020700|||http://purl.uniprot.org/annotation/VAR_020701|||http://purl.uniprot.org/annotation/VAR_020702|||http://purl.uniprot.org/annotation/VAR_020704|||http://purl.uniprot.org/annotation/VAR_021913|||http://purl.uniprot.org/annotation/VAR_035947|||http://purl.uniprot.org/annotation/VAR_035948|||http://purl.uniprot.org/annotation/VAR_035949|||http://purl.uniprot.org/annotation/VAR_052077|||http://purl.uniprot.org/annotation/VAR_052078|||http://purl.uniprot.org/annotation/VAR_052079|||http://purl.uniprot.org/annotation/VAR_052080|||http://purl.uniprot.org/annotation/VAR_063212|||http://purl.uniprot.org/annotation/VAR_063899|||http://purl.uniprot.org/annotation/VAR_063900|||http://purl.uniprot.org/annotation/VAR_063901|||http://purl.uniprot.org/annotation/VAR_063902|||http://purl.uniprot.org/annotation/VAR_063903|||http://purl.uniprot.org/annotation/VAR_063904|||http://purl.uniprot.org/annotation/VAR_063905|||http://purl.uniprot.org/annotation/VAR_063906|||http://purl.uniprot.org/annotation/VAR_063907|||http://purl.uniprot.org/annotation/VAR_063908|||http://purl.uniprot.org/annotation/VAR_063909|||http://purl.uniprot.org/annotation/VAR_063910|||http://purl.uniprot.org/annotation/VAR_070458|||http://purl.uniprot.org/annotation/VAR_070459|||http://purl.uniprot.org/annotation/VAR_070460|||http://purl.uniprot.org/annotation/VAR_070461|||http://purl.uniprot.org/annotation/VAR_070462|||http://purl.uniprot.org/annotation/VAR_070463|||http://purl.uniprot.org/annotation/VAR_070464|||http://purl.uniprot.org/annotation/VAR_070465|||http://purl.uniprot.org/annotation/VAR_070466|||http://purl.uniprot.org/annotation/VAR_070467|||http://purl.uniprot.org/annotation/VAR_070468|||http://purl.uniprot.org/annotation/VAR_070469|||http://purl.uniprot.org/annotation/VAR_070470|||http://purl.uniprot.org/annotation/VAR_070471|||http://purl.uniprot.org/annotation/VAR_070472|||http://purl.uniprot.org/annotation/VAR_070473|||http://purl.uniprot.org/annotation/VAR_070474|||http://purl.uniprot.org/annotation/VAR_070475|||http://purl.uniprot.org/annotation/VAR_070476|||http://purl.uniprot.org/annotation/VAR_070477|||http://purl.uniprot.org/annotation/VAR_070478|||http://purl.uniprot.org/annotation/VAR_070479|||http://purl.uniprot.org/annotation/VAR_070480|||http://purl.uniprot.org/annotation/VAR_070481|||http://purl.uniprot.org/annotation/VAR_070482|||http://purl.uniprot.org/annotation/VAR_070483|||http://purl.uniprot.org/annotation/VAR_070484|||http://purl.uniprot.org/annotation/VAR_070485|||http://purl.uniprot.org/annotation/VAR_070486|||http://purl.uniprot.org/annotation/VAR_070487|||http://purl.uniprot.org/annotation/VAR_070488|||http://purl.uniprot.org/annotation/VAR_070489|||http://purl.uniprot.org/annotation/VAR_070490|||http://purl.uniprot.org/annotation/VAR_070491|||http://purl.uniprot.org/annotation/VAR_070492|||http://purl.uniprot.org/annotation/VAR_070493|||http://purl.uniprot.org/annotation/VAR_070494|||http://purl.uniprot.org/annotation/VAR_070495|||http://purl.uniprot.org/annotation/VAR_070496|||http://purl.uniprot.org/annotation/VAR_070497|||http://purl.uniprot.org/annotation/VAR_070498|||http://purl.uniprot.org/annotation/VAR_070499|||http://purl.uniprot.org/annotation/VAR_070500|||http://purl.uniprot.org/annotation/VAR_070501|||http://purl.uniprot.org/annotation/VAR_070502|||http://purl.uniprot.org/annotation/VAR_070503|||http://purl.uniprot.org/annotation/VAR_070504|||http://purl.uniprot.org/annotation/VAR_070505|||http://purl.uniprot.org/annotation/VAR_070506|||http://purl.uniprot.org/annotation/VAR_070507|||http://purl.uniprot.org/annotation/VAR_070508|||http://purl.uniprot.org/annotation/VAR_070509|||http://purl.uniprot.org/annotation/VAR_070510|||http://purl.uniprot.org/annotation/VAR_070511|||http://purl.uniprot.org/annotation/VAR_070512|||http://purl.uniprot.org/annotation/VAR_070513|||http://purl.uniprot.org/annotation/VAR_070514|||http://purl.uniprot.org/annotation/VAR_070515|||http://purl.uniprot.org/annotation/VAR_070516|||http://purl.uniprot.org/annotation/VAR_070517|||http://purl.uniprot.org/annotation/VAR_070518|||http://purl.uniprot.org/annotation/VAR_070519|||http://purl.uniprot.org/annotation/VAR_075666|||http://purl.uniprot.org/annotation/VAR_079607|||http://purl.uniprot.org/annotation/VAR_080693|||http://purl.uniprot.org/annotation/VSP_035396|||http://purl.uniprot.org/annotation/VSP_035398|||http://purl.uniprot.org/annotation/VSP_035399|||http://purl.uniprot.org/annotation/VSP_043797|||http://purl.uniprot.org/annotation/VSP_043798|||http://purl.uniprot.org/annotation/VSP_047891|||http://purl.uniprot.org/annotation/VSP_055404|||http://purl.uniprot.org/annotation/VSP_057569
http://togogenome.org/gene/9606:KCNRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5I3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  BTB|||In isoform 2.|||Potassium channel regulatory protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238945|||http://purl.uniprot.org/annotation/VSP_019018|||http://purl.uniprot.org/annotation/VSP_019021
http://togogenome.org/gene/9606:DENND4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75064                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  DENN domain-containing protein 4B|||Disordered|||MABP|||PPR 1|||PPR 2|||Phosphoserine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304678
http://togogenome.org/gene/9606:NUP188                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SRE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with syndromic developmental delay; unknown pathological significance.|||In SANDSTEF.|||In SANDSTEF; undetectable protein expression; loss of nuclear localization.|||In isoform 2.|||N-acetylalanine|||Nucleoporin NUP188|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299172|||http://purl.uniprot.org/annotation/VAR_034792|||http://purl.uniprot.org/annotation/VAR_034793|||http://purl.uniprot.org/annotation/VAR_083845|||http://purl.uniprot.org/annotation/VAR_083846|||http://purl.uniprot.org/annotation/VAR_083847|||http://purl.uniprot.org/annotation/VAR_083848|||http://purl.uniprot.org/annotation/VAR_085785|||http://purl.uniprot.org/annotation/VSP_027585
http://togogenome.org/gene/9606:ZSCAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||Pro residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047748|||http://purl.uniprot.org/annotation/VSP_011953|||http://purl.uniprot.org/annotation/VSP_011954
http://togogenome.org/gene/9606:PYGM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11217                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycogen phosphorylase, muscle form|||In GSD5.|||In GSD5; common in Japanese patients.|||In GSD5; rare mutation.|||In isoform 2.|||Involved in the association of subunits|||May be involved in allosteric control|||N-acetylserine|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Phosphoserine; by PHK; in form phosphorylase A|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188529|||http://purl.uniprot.org/annotation/VAR_003431|||http://purl.uniprot.org/annotation/VAR_003432|||http://purl.uniprot.org/annotation/VAR_003433|||http://purl.uniprot.org/annotation/VAR_003434|||http://purl.uniprot.org/annotation/VAR_014002|||http://purl.uniprot.org/annotation/VAR_014003|||http://purl.uniprot.org/annotation/VAR_014004|||http://purl.uniprot.org/annotation/VAR_014005|||http://purl.uniprot.org/annotation/VAR_014006|||http://purl.uniprot.org/annotation/VAR_014007|||http://purl.uniprot.org/annotation/VAR_014008|||http://purl.uniprot.org/annotation/VAR_014009|||http://purl.uniprot.org/annotation/VAR_014010|||http://purl.uniprot.org/annotation/VAR_014011|||http://purl.uniprot.org/annotation/VAR_014012|||http://purl.uniprot.org/annotation/VAR_014013|||http://purl.uniprot.org/annotation/VAR_014014|||http://purl.uniprot.org/annotation/VAR_014015|||http://purl.uniprot.org/annotation/VAR_061198|||http://purl.uniprot.org/annotation/VAR_085195|||http://purl.uniprot.org/annotation/VSP_043047
http://togogenome.org/gene/9606:ITGA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08514                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3.|||In BDPLT16; results in abnormal membrane ruffling and cytoplasmic protrusions as well as defective proplatelet formation.|||In GT1 and BDPLT16; results in low surface expression of the mutant protein.|||In GT1.|||In GT1; abolishes the binding function of alpha-IIb/beta-3 for soluble ligands without disturbing alpha-IIb/beta-3 expression; functional defect is likely caused by its allosteric effect rather than by a defect in the ligand-binding site itself.|||In GT1; alteres the conformation of heterodimers such that they were neither recognized by the heterodimer-specific antibody A2A9 nor able to undergo further intracellular processing or transport to the cell surface.|||In GT1; alters the heterodimer conformation thus impairing their intracellular transport.|||In GT1; associated with abrogation of alpha-IIb/beta-3 complex formation.|||In GT1; cells co-transfected with mutated alpha-IIb and wild-type beta-3 scarcely expressed the alpha-IIb/beta-3 complex.|||In GT1; disrupts the structural conformation and the ligand binding properties of the heterodimeric complex; in addition the mutation appears to confer susceptibility to proteolysis.|||In GT1; expression of mutant subunit alpha-IIb/bet-3 is 11% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum.|||In GT1; expression of mutant subunit alpha-IIb/bet-3 is 28% of control; mutant pro-alpha-IIb subunit is retained in the endoplasmic reticulum.|||In GT1; impairs surface expression of alpha-IIb/beta-3 and abrogates ligand binding to the activated integrin.|||In GT1; impairs surface expression of alpha-IIb/beta-3.|||In GT1; marked reduction in the rate of surface expression.|||In GT1; much reduced surface expression of alpha-IIb/beta-3 and a block in the maturation of pro-alpha-IIb.|||In GT1; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface.|||In GT1; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein.|||In GT1; type I.|||In GT1; type I; impairs surface expression of alpha-IIb/beta-3.|||In GT1; type II.|||In GT1; type II; the rate of subunit maturation and the surface exposure of glycoprotein IIb/beta-3 are strongly reduced.|||In alloantigen HPA-3B.|||In isoform 2.|||In isoform 3.|||Integrin alpha-IIb|||Integrin alpha-IIb heavy chain|||Integrin alpha-IIb light chain, form 1|||Integrin alpha-IIb light chain, form 2|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) serine; in variant S-874|||Pyrrolidone carboxylic acid; in light chain form 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016275|||http://purl.uniprot.org/annotation/PRO_0000016276|||http://purl.uniprot.org/annotation/PRO_0000016277|||http://purl.uniprot.org/annotation/PRO_0000292348|||http://purl.uniprot.org/annotation/VAR_003979|||http://purl.uniprot.org/annotation/VAR_003980|||http://purl.uniprot.org/annotation/VAR_003981|||http://purl.uniprot.org/annotation/VAR_003982|||http://purl.uniprot.org/annotation/VAR_003983|||http://purl.uniprot.org/annotation/VAR_009885|||http://purl.uniprot.org/annotation/VAR_009886|||http://purl.uniprot.org/annotation/VAR_009887|||http://purl.uniprot.org/annotation/VAR_009888|||http://purl.uniprot.org/annotation/VAR_014176|||http://purl.uniprot.org/annotation/VAR_014177|||http://purl.uniprot.org/annotation/VAR_030445|||http://purl.uniprot.org/annotation/VAR_030446|||http://purl.uniprot.org/annotation/VAR_030447|||http://purl.uniprot.org/annotation/VAR_030448|||http://purl.uniprot.org/annotation/VAR_030449|||http://purl.uniprot.org/annotation/VAR_030450|||http://purl.uniprot.org/annotation/VAR_030451|||http://purl.uniprot.org/annotation/VAR_030452|||http://purl.uniprot.org/annotation/VAR_030453|||http://purl.uniprot.org/annotation/VAR_030454|||http://purl.uniprot.org/annotation/VAR_030455|||http://purl.uniprot.org/annotation/VAR_030456|||http://purl.uniprot.org/annotation/VAR_030457|||http://purl.uniprot.org/annotation/VAR_030458|||http://purl.uniprot.org/annotation/VAR_030459|||http://purl.uniprot.org/annotation/VAR_030460|||http://purl.uniprot.org/annotation/VAR_030461|||http://purl.uniprot.org/annotation/VAR_030462|||http://purl.uniprot.org/annotation/VAR_030463|||http://purl.uniprot.org/annotation/VAR_030464|||http://purl.uniprot.org/annotation/VAR_030465|||http://purl.uniprot.org/annotation/VAR_030466|||http://purl.uniprot.org/annotation/VAR_030467|||http://purl.uniprot.org/annotation/VAR_030468|||http://purl.uniprot.org/annotation/VAR_054820|||http://purl.uniprot.org/annotation/VAR_054821|||http://purl.uniprot.org/annotation/VAR_069917|||http://purl.uniprot.org/annotation/VAR_069918|||http://purl.uniprot.org/annotation/VAR_069919|||http://purl.uniprot.org/annotation/VSP_002736|||http://purl.uniprot.org/annotation/VSP_002737
http://togogenome.org/gene/9606:SKA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSP0|||http://purl.uniprot.org/uniprot/Q8WVK7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Ska2 N-terminal|||Spindle and kinetochore-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266035|||http://purl.uniprot.org/annotation/VSP_047348|||http://purl.uniprot.org/annotation/VSP_047349
http://togogenome.org/gene/9606:PHYH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14832                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In RD.|||In RD; total loss of activity.|||In isoform 2.|||N6-succinyllysine|||Peroxisome|||Phosphoserine|||Phytanoyl-CoA dioxygenase, peroxisomal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024053|||http://purl.uniprot.org/annotation/VAR_005525|||http://purl.uniprot.org/annotation/VAR_005526|||http://purl.uniprot.org/annotation/VAR_012980|||http://purl.uniprot.org/annotation/VAR_017482|||http://purl.uniprot.org/annotation/VAR_017483|||http://purl.uniprot.org/annotation/VAR_017484|||http://purl.uniprot.org/annotation/VAR_017485|||http://purl.uniprot.org/annotation/VAR_017486|||http://purl.uniprot.org/annotation/VAR_017487|||http://purl.uniprot.org/annotation/VAR_017488|||http://purl.uniprot.org/annotation/VAR_017489|||http://purl.uniprot.org/annotation/VAR_017490|||http://purl.uniprot.org/annotation/VAR_017491|||http://purl.uniprot.org/annotation/VAR_017492|||http://purl.uniprot.org/annotation/VAR_017493|||http://purl.uniprot.org/annotation/VAR_018619|||http://purl.uniprot.org/annotation/VAR_018631|||http://purl.uniprot.org/annotation/VAR_050528|||http://purl.uniprot.org/annotation/VSP_046289
http://togogenome.org/gene/9606:MALSU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EH3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Mitochondrial assembly of ribosomal large subunit protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228108
http://togogenome.org/gene/9606:SLC46A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY10                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Solute carrier family 46 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065659|||http://purl.uniprot.org/annotation/VAR_021050
http://togogenome.org/gene/9606:EEF1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43324                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-terminal|||Disrupts interaction with EPRS1.|||Disrupts interaction with MARS1.|||Eukaryotic translation elongation factor 1 epsilon-1|||GST C-terminal|||In isoform 2.|||Linker|||N-acetylalanine|||N-terminal|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221132|||http://purl.uniprot.org/annotation/VSP_045088
http://togogenome.org/gene/9606:ZNF343                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZQ2|||http://purl.uniprot.org/uniprot/Q6P1L6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Polar residues|||Zinc finger protein 343                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047543|||http://purl.uniprot.org/annotation/VAR_059912|||http://purl.uniprot.org/annotation/VSP_016028|||http://purl.uniprot.org/annotation/VSP_016029|||http://purl.uniprot.org/annotation/VSP_016030
http://togogenome.org/gene/9606:ZNF136                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0J2|||http://purl.uniprot.org/uniprot/B4DS70|||http://purl.uniprot.org/uniprot/P52737                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Phosphoserine|||Zinc finger protein 136                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047420|||http://purl.uniprot.org/annotation/VAR_033555
http://togogenome.org/gene/9606:C6orf89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWU4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Bombesin receptor-activated protein C6orf89|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237621|||http://purl.uniprot.org/annotation/VSP_018598|||http://purl.uniprot.org/annotation/VSP_058111
http://togogenome.org/gene/9606:SHISAL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWV7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Protein shisa-like-2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317720|||http://purl.uniprot.org/annotation/VSP_031139
http://togogenome.org/gene/9606:CCDC54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEL0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 54|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286668|||http://purl.uniprot.org/annotation/VAR_032151
http://togogenome.org/gene/9606:OR6C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW15|||http://purl.uniprot.org/uniprot/A6NF89                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310457|||http://purl.uniprot.org/annotation/VAR_037048
http://togogenome.org/gene/9606:LHX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPM6                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx6|||Required for interaction with LDB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075794|||http://purl.uniprot.org/annotation/VSP_003109|||http://purl.uniprot.org/annotation/VSP_037745|||http://purl.uniprot.org/annotation/VSP_042073|||http://purl.uniprot.org/annotation/VSP_046043
http://togogenome.org/gene/9606:SPATA31D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332290
http://togogenome.org/gene/9606:DNAJB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI2|||http://purl.uniprot.org/uniprot/Q8NHS0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Turn                                                                                  ^@                                                                                  DnaJ homolog subfamily B member 8|||J|||Significant loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071029|||http://purl.uniprot.org/annotation/VAR_033881
http://togogenome.org/gene/9606:HEMGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hemogen|||Necessary for nuclear localization|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245361
http://togogenome.org/gene/9606:ATRIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXE1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATR-interacting protein|||Abolishes interaction with ATR and its recruitment to sites of DNA damage.|||Disordered|||EEXXXDL motif|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CINP|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064740|||http://purl.uniprot.org/annotation/VAR_050683|||http://purl.uniprot.org/annotation/VAR_050684|||http://purl.uniprot.org/annotation/VSP_010501|||http://purl.uniprot.org/annotation/VSP_010504|||http://purl.uniprot.org/annotation/VSP_047011
http://togogenome.org/gene/9606:CFAP97D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7J0                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TENM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW8|||http://purl.uniprot.org/uniprot/Q9P273                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||Extracellular|||Helical|||In MCOPS15.|||In MCOPS15; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Polar residues|||Teneurin N-terminal|||Teneurin-3|||YD 1|||YD 10|||YD 11|||YD 12|||YD 13|||YD 14|||YD 15|||YD 16|||YD 17|||YD 18|||YD 19|||YD 2|||YD 20|||YD 21|||YD 22|||YD 23|||YD 3|||YD 4|||YD 5|||YD 6|||YD 7|||YD 8|||YD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259505|||http://purl.uniprot.org/annotation/VAR_053796|||http://purl.uniprot.org/annotation/VAR_083250|||http://purl.uniprot.org/annotation/VAR_083251|||http://purl.uniprot.org/annotation/VAR_083252
http://togogenome.org/gene/9606:ACP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15309                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Greatly reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate.|||Important for substrate specificity|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PAPf39|||Prostatic acid phosphatase|||Proton donor|||Reduced enzyme activity, marked decrease in structural stability, and increased binding of the inhibitor, L(+)-tartrate.|||Required for homodimerization|||Required for structural stability                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023963|||http://purl.uniprot.org/annotation/PRO_0000411250|||http://purl.uniprot.org/annotation/VAR_047960|||http://purl.uniprot.org/annotation/VAR_047961|||http://purl.uniprot.org/annotation/VAR_047962|||http://purl.uniprot.org/annotation/VAR_047963|||http://purl.uniprot.org/annotation/VAR_047964|||http://purl.uniprot.org/annotation/VSP_036023|||http://purl.uniprot.org/annotation/VSP_053360
http://togogenome.org/gene/9606:FHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9A1|||http://purl.uniprot.org/uniprot/Q13642|||http://purl.uniprot.org/uniprot/Q5JXI2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Four and a half LIM domains protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In EDMD6.|||In EDMD6; drastically reduced protein levels in muscle.|||In RBMX1A.|||In RBMX1A; the mutant protein initiates aggregation of the FHL1 protein causing reducing bodies formation; dominant-negative effect.|||In RBMX1A; unknown pathological significance.|||In RBMX1B.|||In RBMX1B; unknown pathological significance.|||In SPM.|||In XMPMA.|||In XMPMA; unknown pathological significance.|||In isoform 1, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075735|||http://purl.uniprot.org/annotation/VAR_042603|||http://purl.uniprot.org/annotation/VAR_042604|||http://purl.uniprot.org/annotation/VAR_042605|||http://purl.uniprot.org/annotation/VAR_045999|||http://purl.uniprot.org/annotation/VAR_046000|||http://purl.uniprot.org/annotation/VAR_046001|||http://purl.uniprot.org/annotation/VAR_046002|||http://purl.uniprot.org/annotation/VAR_075350|||http://purl.uniprot.org/annotation/VAR_075351|||http://purl.uniprot.org/annotation/VAR_075352|||http://purl.uniprot.org/annotation/VAR_075353|||http://purl.uniprot.org/annotation/VAR_075354|||http://purl.uniprot.org/annotation/VAR_075355|||http://purl.uniprot.org/annotation/VAR_075356|||http://purl.uniprot.org/annotation/VAR_075357|||http://purl.uniprot.org/annotation/VAR_075358|||http://purl.uniprot.org/annotation/VAR_075359|||http://purl.uniprot.org/annotation/VAR_076566|||http://purl.uniprot.org/annotation/VAR_082844|||http://purl.uniprot.org/annotation/VAR_082845|||http://purl.uniprot.org/annotation/VSP_010693|||http://purl.uniprot.org/annotation/VSP_010694|||http://purl.uniprot.org/annotation/VSP_043162|||http://purl.uniprot.org/annotation/VSP_043404
http://togogenome.org/gene/9606:MILR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6M3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Allergin-1|||Cytoplasmic|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307364|||http://purl.uniprot.org/annotation/VSP_040765|||http://purl.uniprot.org/annotation/VSP_040766
http://togogenome.org/gene/9606:GTSF1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1H1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CHHC U11-48K-type 1|||CHHC U11-48K-type 2|||Disordered|||Gametocyte-specific factor 1-like|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221619|||http://purl.uniprot.org/annotation/VAR_052549|||http://purl.uniprot.org/annotation/VSP_047166
http://togogenome.org/gene/9606:RIOK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ89|||http://purl.uniprot.org/uniprot/B4E1Q4|||http://purl.uniprot.org/uniprot/O14730                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreases autophosphorylation (in vitro); abolishes inhibition of TNF-alpha-induced NF-kappaB activation; no effect on interaction with IRF3; fails to activate IFN-beta promoter and IRF3 phosphorylation.|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||RIO kinase|||Serine/threonine-protein kinase RIO3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213529|||http://purl.uniprot.org/annotation/VAR_042355|||http://purl.uniprot.org/annotation/VAR_042356|||http://purl.uniprot.org/annotation/VAR_042357|||http://purl.uniprot.org/annotation/VSP_012164
http://togogenome.org/gene/9606:ST3GAL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNP4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lactosylceramide alpha-2,3-sialyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149302|||http://purl.uniprot.org/annotation/VAR_025510|||http://purl.uniprot.org/annotation/VSP_033686|||http://purl.uniprot.org/annotation/VSP_033687|||http://purl.uniprot.org/annotation/VSP_033688
http://togogenome.org/gene/9606:CRISPLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK80|||http://purl.uniprot.org/uniprot/Q9H0B8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine-rich secretory protein LCCL domain-containing 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LCCL|||LCCL 1|||LCCL 2|||N-linked (GlcNAc...) asparagine|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248149|||http://purl.uniprot.org/annotation/PRO_5007491752|||http://purl.uniprot.org/annotation/VAR_027256|||http://purl.uniprot.org/annotation/VAR_027257|||http://purl.uniprot.org/annotation/VAR_074672|||http://purl.uniprot.org/annotation/VSP_020178|||http://purl.uniprot.org/annotation/VSP_020179|||http://purl.uniprot.org/annotation/VSP_020180|||http://purl.uniprot.org/annotation/VSP_020181|||http://purl.uniprot.org/annotation/VSP_020182|||http://purl.uniprot.org/annotation/VSP_020183
http://togogenome.org/gene/9606:CSPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1MSJ5|||http://purl.uniprot.org/uniprot/Q9H688                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosome and spindle pole-associated protein 1|||Disordered|||In isoform 1.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293464|||http://purl.uniprot.org/annotation/VAR_033045|||http://purl.uniprot.org/annotation/VAR_047014|||http://purl.uniprot.org/annotation/VSP_026475|||http://purl.uniprot.org/annotation/VSP_026476|||http://purl.uniprot.org/annotation/VSP_040072
http://togogenome.org/gene/9606:TRPC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y210                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Constitutively activates channel.|||Cytoplasmic|||Decreases calcium ion transport.|||Disordered|||Extracellular|||Helical|||In FSGS2.|||In FSGS2; decreases calcium ion transport.|||In FSGS2; decreases calcium ion transport; does not change localization at cell membrane; does not affect homodimer formation.|||In FSGS2; increases calcium ion transport.|||In FSGS2; increases cation channel activity; does not change plasma membrane expression; increases calcium ion transport.|||In FSGS2; increases cation channel activity; does not change plasma membrane expression; significantly reduces the ratio of cell-surface to total expression; increases calcium ion transport.|||In FSGS2; increases cation channel activity; does not change the outward peak current; increases significantly the inward peak current amplitude; increases calcium ion transport.|||In FSGS2; unknown pathological significance.|||In FSGS2; unknown pathological significance; decreases calcium ion transport.|||In FSGS2; unknown pathological significance; requires 2 nucleotide substitutions; decreases calcium ion transport.|||In isoform 2.|||In isoform 3.|||Increases calcium ion transport.|||Increases calcium transport. Increases calcium ion transport.|||Increases cation channel activity. Increases significantly inward and outward currents and does not show channel inactivation. Increases calcium ion transport.|||N-linked (GlcNAc...) asparagine|||No effect on RNF24-binding; when associated with A-125; A-127 and A-128.|||No effect on RNF24-binding; when associated with A-125; A-127 and A-130.|||No effect on RNF24-binding; when associated with A-125; A-128 and A-130.|||No effect on RNF24-binding; when associated with A-127; A-128 and A-130.|||Phosphoserine|||Short transient receptor potential channel 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215322|||http://purl.uniprot.org/annotation/VAR_026730|||http://purl.uniprot.org/annotation/VAR_026731|||http://purl.uniprot.org/annotation/VAR_026732|||http://purl.uniprot.org/annotation/VAR_026733|||http://purl.uniprot.org/annotation/VAR_026734|||http://purl.uniprot.org/annotation/VAR_038419|||http://purl.uniprot.org/annotation/VAR_061861|||http://purl.uniprot.org/annotation/VAR_067247|||http://purl.uniprot.org/annotation/VAR_067248|||http://purl.uniprot.org/annotation/VAR_067249|||http://purl.uniprot.org/annotation/VAR_079784|||http://purl.uniprot.org/annotation/VAR_079785|||http://purl.uniprot.org/annotation/VAR_079786|||http://purl.uniprot.org/annotation/VAR_079787|||http://purl.uniprot.org/annotation/VAR_079788|||http://purl.uniprot.org/annotation/VAR_079789|||http://purl.uniprot.org/annotation/VAR_079790|||http://purl.uniprot.org/annotation/VAR_079791|||http://purl.uniprot.org/annotation/VAR_079792|||http://purl.uniprot.org/annotation/VAR_079793|||http://purl.uniprot.org/annotation/VSP_006572|||http://purl.uniprot.org/annotation/VSP_006573
http://togogenome.org/gene/9606:NHERF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ61|||http://purl.uniprot.org/uniprot/Q86UT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF4|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058292|||http://purl.uniprot.org/annotation/VSP_051786|||http://purl.uniprot.org/annotation/VSP_051787|||http://purl.uniprot.org/annotation/VSP_051788|||http://purl.uniprot.org/annotation/VSP_051789|||http://purl.uniprot.org/annotation/VSP_051790|||http://purl.uniprot.org/annotation/VSP_051791
http://togogenome.org/gene/9606:CCR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0Q1|||http://purl.uniprot.org/uniprot/P51679                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 4|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069245|||http://purl.uniprot.org/annotation/VAR_010669|||http://purl.uniprot.org/annotation/VAR_010670
http://togogenome.org/gene/9606:SGSH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51688                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Does not affect enzyme activity; cells transfected with the mutant enzyme contain a 62 kDa precursor and a 56 kDa mature form as cells transfected with the wild-type enzyme.|||In MPS3A.|||In MPS3A; associated with a slowly progressive clinical phenotype; rapidly degraded but small amounts of the mutant protein are correctly transported to the lysosome; low but significant residual enzymatic activity.|||In MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme.|||In MPS3A; intermediate.|||In MPS3A; intermediate/severe; common mutation in Italy.|||In MPS3A; intermediate/severe; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum.|||In MPS3A; severe.|||In MPS3A; severe; common mutation in Western Europe and Australia.|||In MPS3A; severe; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme.|||In MPS3A; shows 3.3% activity of the expressed wild-type enzyme; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells.|||In MPS3A; the mutant enzyme retains 8% residual activity.|||In MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells.|||In MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum.|||In MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the mutant protein shows instability in the lysosomes.|||In MPS3A; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||N-sulphoglucosamine sulphohydrolase|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033433|||http://purl.uniprot.org/annotation/VAR_007388|||http://purl.uniprot.org/annotation/VAR_007389|||http://purl.uniprot.org/annotation/VAR_007390|||http://purl.uniprot.org/annotation/VAR_007391|||http://purl.uniprot.org/annotation/VAR_007392|||http://purl.uniprot.org/annotation/VAR_007393|||http://purl.uniprot.org/annotation/VAR_007394|||http://purl.uniprot.org/annotation/VAR_007395|||http://purl.uniprot.org/annotation/VAR_007396|||http://purl.uniprot.org/annotation/VAR_007397|||http://purl.uniprot.org/annotation/VAR_007398|||http://purl.uniprot.org/annotation/VAR_007399|||http://purl.uniprot.org/annotation/VAR_007400|||http://purl.uniprot.org/annotation/VAR_007401|||http://purl.uniprot.org/annotation/VAR_007402|||http://purl.uniprot.org/annotation/VAR_007403|||http://purl.uniprot.org/annotation/VAR_007404|||http://purl.uniprot.org/annotation/VAR_007405|||http://purl.uniprot.org/annotation/VAR_007406|||http://purl.uniprot.org/annotation/VAR_007407|||http://purl.uniprot.org/annotation/VAR_007408|||http://purl.uniprot.org/annotation/VAR_007409|||http://purl.uniprot.org/annotation/VAR_007410|||http://purl.uniprot.org/annotation/VAR_007411|||http://purl.uniprot.org/annotation/VAR_007412|||http://purl.uniprot.org/annotation/VAR_007413|||http://purl.uniprot.org/annotation/VAR_007414|||http://purl.uniprot.org/annotation/VAR_007415|||http://purl.uniprot.org/annotation/VAR_007416|||http://purl.uniprot.org/annotation/VAR_007417|||http://purl.uniprot.org/annotation/VAR_007418|||http://purl.uniprot.org/annotation/VAR_007419|||http://purl.uniprot.org/annotation/VAR_007420|||http://purl.uniprot.org/annotation/VAR_007421|||http://purl.uniprot.org/annotation/VAR_007422|||http://purl.uniprot.org/annotation/VAR_007423|||http://purl.uniprot.org/annotation/VAR_007424|||http://purl.uniprot.org/annotation/VAR_052517|||http://purl.uniprot.org/annotation/VAR_054670|||http://purl.uniprot.org/annotation/VAR_054671|||http://purl.uniprot.org/annotation/VAR_054672|||http://purl.uniprot.org/annotation/VAR_054673|||http://purl.uniprot.org/annotation/VAR_054674|||http://purl.uniprot.org/annotation/VAR_054675|||http://purl.uniprot.org/annotation/VAR_054676|||http://purl.uniprot.org/annotation/VAR_054677|||http://purl.uniprot.org/annotation/VAR_054678|||http://purl.uniprot.org/annotation/VAR_054679|||http://purl.uniprot.org/annotation/VAR_054680|||http://purl.uniprot.org/annotation/VAR_054681|||http://purl.uniprot.org/annotation/VAR_054682|||http://purl.uniprot.org/annotation/VAR_054683|||http://purl.uniprot.org/annotation/VAR_054684|||http://purl.uniprot.org/annotation/VAR_054685|||http://purl.uniprot.org/annotation/VAR_054686|||http://purl.uniprot.org/annotation/VAR_054687|||http://purl.uniprot.org/annotation/VAR_054688|||http://purl.uniprot.org/annotation/VAR_054689|||http://purl.uniprot.org/annotation/VAR_054690|||http://purl.uniprot.org/annotation/VAR_054691|||http://purl.uniprot.org/annotation/VAR_054692|||http://purl.uniprot.org/annotation/VAR_054693|||http://purl.uniprot.org/annotation/VAR_054694|||http://purl.uniprot.org/annotation/VAR_054695|||http://purl.uniprot.org/annotation/VAR_054696|||http://purl.uniprot.org/annotation/VAR_054697|||http://purl.uniprot.org/annotation/VAR_054698|||http://purl.uniprot.org/annotation/VAR_061884|||http://purl.uniprot.org/annotation/VAR_079426|||http://purl.uniprot.org/annotation/VAR_079427
http://togogenome.org/gene/9606:TIGD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DDE-1 1|||DDE-1 2|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||In isoform 2.|||Pro residues|||Tigger transposable element-derived protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272618|||http://purl.uniprot.org/annotation/VAR_030043|||http://purl.uniprot.org/annotation/VSP_042796
http://togogenome.org/gene/9606:ICAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13598|||http://purl.uniprot.org/uniprot/Q6FHE2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Intercellular adhesion molecule 2|||Intercellular adhesion molecule N-terminal|||N-linked (GlcNAc...) asparagine|||Required for interaction with EZR, MSN and RDX and co-localization to microvilli                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014790|||http://purl.uniprot.org/annotation/PRO_5014310454|||http://purl.uniprot.org/annotation/VAR_014655|||http://purl.uniprot.org/annotation/VAR_014656|||http://purl.uniprot.org/annotation/VAR_021920
http://togogenome.org/gene/9606:DTWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5C7                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DXTW|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Removed|||tRNA-uridine aminocarboxypropyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308212|||http://purl.uniprot.org/annotation/VAR_036757|||http://purl.uniprot.org/annotation/VAR_036758|||http://purl.uniprot.org/annotation/VAR_036759|||http://purl.uniprot.org/annotation/VSP_028922|||http://purl.uniprot.org/annotation/VSP_028923
http://togogenome.org/gene/9606:PFDN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99471                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Prefoldin subunit 5|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153661|||http://purl.uniprot.org/annotation/VSP_043103|||http://purl.uniprot.org/annotation/VSP_043104
http://togogenome.org/gene/9606:ORAI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Causes redox sensitivity with channel activity inhibited by hydrogen peroxide.|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Protein orai-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234395
http://togogenome.org/gene/9606:PPP1R3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQK1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  CBM21|||Found in a patient with progressive myoclonic epilepsy type 2 also carrying two mutations in EPM2B.|||Interaction with EPM2A|||No effect on interaction with EPM2A; when associated with A-85.|||No effect on interaction with EPM2A; when associated with A-87.|||No interaction with EPM2A; when associated with A-247.|||No interaction with EPM2A; when associated with A-250.|||PP1-binding motif|||Protein phosphatase 1 regulatory subunit 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285927|||http://purl.uniprot.org/annotation/VAR_059775|||http://purl.uniprot.org/annotation/VAR_067339
http://togogenome.org/gene/9606:SENP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4L4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Loss of enzymatic activity.|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Protease|||Sentrin-specific protease 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101721|||http://purl.uniprot.org/annotation/VAR_051544
http://togogenome.org/gene/9606:MST1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E058|||http://purl.uniprot.org/uniprot/G9JXB8|||http://purl.uniprot.org/uniprot/Q04912                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||In NPCA3.|||In NPCA3; unknown pathological significance.|||In isoform Delta-RON.|||In isoform RON-1.|||In isoform RON-2 and isoform RON-4.|||In isoform RON-2 and isoform RON-5.|||In isoform RON-3.|||Macrophage-stimulating protein receptor|||Macrophage-stimulating protein receptor alpha chain|||Macrophage-stimulating protein receptor beta chain|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Sema|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024452|||http://purl.uniprot.org/annotation/PRO_0000024453|||http://purl.uniprot.org/annotation/PRO_0000024454|||http://purl.uniprot.org/annotation/PRO_5003522923|||http://purl.uniprot.org/annotation/VAR_006350|||http://purl.uniprot.org/annotation/VAR_024577|||http://purl.uniprot.org/annotation/VAR_029238|||http://purl.uniprot.org/annotation/VAR_029239|||http://purl.uniprot.org/annotation/VAR_041768|||http://purl.uniprot.org/annotation/VAR_041769|||http://purl.uniprot.org/annotation/VAR_041770|||http://purl.uniprot.org/annotation/VAR_041771|||http://purl.uniprot.org/annotation/VAR_041772|||http://purl.uniprot.org/annotation/VAR_041773|||http://purl.uniprot.org/annotation/VAR_041774|||http://purl.uniprot.org/annotation/VAR_041775|||http://purl.uniprot.org/annotation/VAR_041776|||http://purl.uniprot.org/annotation/VAR_041777|||http://purl.uniprot.org/annotation/VAR_041778|||http://purl.uniprot.org/annotation/VAR_061749|||http://purl.uniprot.org/annotation/VAR_076928|||http://purl.uniprot.org/annotation/VAR_076929|||http://purl.uniprot.org/annotation/VAR_076930|||http://purl.uniprot.org/annotation/VAR_076931|||http://purl.uniprot.org/annotation/VSP_005007|||http://purl.uniprot.org/annotation/VSP_038919|||http://purl.uniprot.org/annotation/VSP_038920|||http://purl.uniprot.org/annotation/VSP_038921|||http://purl.uniprot.org/annotation/VSP_038922|||http://purl.uniprot.org/annotation/VSP_038923|||http://purl.uniprot.org/annotation/VSP_038924|||http://purl.uniprot.org/annotation/VSP_038925
http://togogenome.org/gene/9606:IQCF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXL9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  IQ 1|||IQ 2|||IQ domain-containing protein F2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282559
http://togogenome.org/gene/9606:ZNF211                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTK1|||http://purl.uniprot.org/uniprot/Q13398                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||KRAB|||Polar residues|||Zinc finger protein 211                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047455|||http://purl.uniprot.org/annotation/VAR_047278|||http://purl.uniprot.org/annotation/VAR_057402|||http://purl.uniprot.org/annotation/VSP_035702|||http://purl.uniprot.org/annotation/VSP_035703|||http://purl.uniprot.org/annotation/VSP_035704|||http://purl.uniprot.org/annotation/VSP_035705|||http://purl.uniprot.org/annotation/VSP_035706|||http://purl.uniprot.org/annotation/VSP_045643|||http://purl.uniprot.org/annotation/VSP_046769
http://togogenome.org/gene/9606:C19orf84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L1E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Uncharacterized protein C19orf84                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425555
http://togogenome.org/gene/9606:STAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49675|||http://purl.uniprot.org/uniprot/Q6IBK0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In AH1.|||In AH1; partial loss of activity.|||Mitochondrion|||Phosphoserine; by PKA|||START|||Steroidogenic acute regulatory protein, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033316|||http://purl.uniprot.org/annotation/VAR_005627|||http://purl.uniprot.org/annotation/VAR_005628|||http://purl.uniprot.org/annotation/VAR_014236|||http://purl.uniprot.org/annotation/VAR_014237|||http://purl.uniprot.org/annotation/VAR_014238|||http://purl.uniprot.org/annotation/VAR_014239|||http://purl.uniprot.org/annotation/VAR_014240|||http://purl.uniprot.org/annotation/VAR_014241|||http://purl.uniprot.org/annotation/VAR_014242|||http://purl.uniprot.org/annotation/VAR_034520
http://togogenome.org/gene/9606:PROSER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3WKY3|||http://purl.uniprot.org/uniprot/A0A8Q3WKY6|||http://purl.uniprot.org/uniprot/A0A8Q3WKY7|||http://purl.uniprot.org/uniprot/Q2NL68                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||Proline and serine-rich protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299482|||http://purl.uniprot.org/annotation/VAR_056845|||http://purl.uniprot.org/annotation/VAR_061631|||http://purl.uniprot.org/annotation/VSP_027698|||http://purl.uniprot.org/annotation/VSP_027699|||http://purl.uniprot.org/annotation/VSP_027700|||http://purl.uniprot.org/annotation/VSP_027701|||http://purl.uniprot.org/annotation/VSP_027702|||http://purl.uniprot.org/annotation/VSP_027703
http://togogenome.org/gene/9606:CD63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08962                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Motif|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD63 antigen|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Lysosomal targeting motif|||N-linked (GlcNAc...) asparagine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219216|||http://purl.uniprot.org/annotation/VSP_045300|||http://purl.uniprot.org/annotation/VSP_046996
http://togogenome.org/gene/9606:ZCRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1V1|||http://purl.uniprot.org/uniprot/Q8TBF4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CCHC-type|||Disordered|||Phosphoserine|||RRM|||Zinc finger CCHC-type and RNA-binding motif-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252373|||http://purl.uniprot.org/annotation/VAR_027845
http://togogenome.org/gene/9606:FBXO16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX29                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 16|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119896|||http://purl.uniprot.org/annotation/VAR_020409|||http://purl.uniprot.org/annotation/VAR_024442|||http://purl.uniprot.org/annotation/VAR_049041|||http://purl.uniprot.org/annotation/VSP_045600
http://togogenome.org/gene/9606:CHCHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BP2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Small ribosomal subunit protein mS37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129158
http://togogenome.org/gene/9606:CEACAM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40199                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 6|||GPI-anchor amidated glycine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||Inhibits homophilic and heterophilic cell adhesion.|||Inhibits homophilic cell adhesion. No effect on heterophilic cell adhesion.|||Inhibits homophilic cell adhesion. Reduces heterophilic cell adhesion.|||Loss of homodimerization and heterodimerization with CEACAM8.|||N-linked (GlcNAc...) asparagine|||No effect on homodimerization. Reduces heterodimerization with CEACAM8.|||No effect on homophilic and heterophilic cell adhesion.|||No effect on homophilic cell adhesion. Inhibits heterophilic cell adhesion.|||No effect on homophilic cell adhesion. Reduces heterophilic cell adhesion.|||Reduces homodimerization. Loss of heterodimerization with CEACAM8.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014568|||http://purl.uniprot.org/annotation/PRO_0000014569|||http://purl.uniprot.org/annotation/VAR_034680
http://togogenome.org/gene/9606:TMED4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W7F7|||http://purl.uniprot.org/uniprot/Q7Z7H5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Motif|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane emp24 domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010387|||http://purl.uniprot.org/annotation/PRO_5003385513|||http://purl.uniprot.org/annotation/VSP_035698|||http://purl.uniprot.org/annotation/VSP_035699|||http://purl.uniprot.org/annotation/VSP_035700
http://togogenome.org/gene/9606:GPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9Y4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  GPN-loop GTPase 2|||Gly-Pro-Asn (GPN)-loop; involved in dimer interface|||N-acetylalanine|||Removed|||Stabilizes the phosphate intermediate; shared with dimeric partner                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247829|||http://purl.uniprot.org/annotation/VAR_027153|||http://purl.uniprot.org/annotation/VAR_027154
http://togogenome.org/gene/9606:NTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95631                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||In MRMV4; changed localization; exclusively detected in the cytoplasm.|||In a neuroblastoma sample.|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||NTR|||Netrin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017082|||http://purl.uniprot.org/annotation/VAR_014279|||http://purl.uniprot.org/annotation/VAR_014280|||http://purl.uniprot.org/annotation/VAR_082026|||http://purl.uniprot.org/annotation/VAR_082027|||http://purl.uniprot.org/annotation/VAR_082028
http://togogenome.org/gene/9606:KCNK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2YDA1|||http://purl.uniprot.org/uniprot/Q9NYG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix 1|||Helical; Name=Pore helix 2|||In FHEIG; gain-of-function variant resulting in highly increased basal potassium currents; impaired sensitivity to arachidonic acid.|||In isoform 2.|||Increases basal level of channel activity and decreases further activation by pressure, but has little effect on further activation by arachidonic acid.|||Interchain|||N-linked (GlcNAc...) asparagine|||Potassium channel|||Potassium channel subfamily K member 4|||Pro residues|||Selectivity filter 1|||Selectivity filter 2|||Strongly increases basal level of channel activity, decreases further activation by pressure and abolishes further activation by arachidonic acid.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101747|||http://purl.uniprot.org/annotation/VAR_020206|||http://purl.uniprot.org/annotation/VAR_082119|||http://purl.uniprot.org/annotation/VAR_082120|||http://purl.uniprot.org/annotation/VSP_006689
http://togogenome.org/gene/9606:TMEM134                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6X4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Transmembrane protein 134                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279485|||http://purl.uniprot.org/annotation/VSP_023452|||http://purl.uniprot.org/annotation/VSP_023453|||http://purl.uniprot.org/annotation/VSP_023454
http://togogenome.org/gene/9606:ABCD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14678                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||Decreases ATPase activity. Reduces synthesis of adenosylcobalamin and methylcobalamin.|||Decreases interaction with LMBD1. Decreases colocalization with LMBD1. Decreases cobalamin transport activity.|||Decreases interaction with LMBD1. Decreases colocalization with LMBD1. Decreases cobalamin transport activity. Reduces synthesis of adenosylcobalamin and methylcobalamin.|||Decreases interaction with LMBD1. Reduces synthesis of adenosylcobalamin and methylcobalamin.|||Decreases of ATPase activity. Decreases cobalamin transport activity.|||Does not affect ATPase activity. Does not affect cobalamin transport activity.|||Does not affect ATPase nor cobalamin transport activities.|||Helical|||In MAHCJ; decreases interaction with LMBD1. Does not affect lysosomal subcellular location. Decreases ATPase activity.|||In MAHCJ; does not affect ATPase activity. Loss of cobalamin transport activity. Decreases interaction with LMBD1. Does not affect lysosomal subcellular location.|||In MAHCJ; strong decrease of ATPase activity. Strong decrease of cobalamin transport activity.|||Loss of ATPase activity. Loss of cobalamin transport activity.|||Lysosomal cobalamin transporter ABCD4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093312|||http://purl.uniprot.org/annotation/VAR_020222|||http://purl.uniprot.org/annotation/VAR_020778|||http://purl.uniprot.org/annotation/VAR_048134|||http://purl.uniprot.org/annotation/VAR_048135|||http://purl.uniprot.org/annotation/VAR_069097|||http://purl.uniprot.org/annotation/VAR_084972|||http://purl.uniprot.org/annotation/VAR_084973
http://togogenome.org/gene/9606:RPS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46782                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylmethionine; in 40S ribosomal protein S5; alternate|||N-acetylthreonine; in 40S ribosomal protein S5, N-terminally processed|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed; alternate|||Small ribosomal subunit protein uS7|||Small ribosomal subunit protein uS7, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124526|||http://purl.uniprot.org/annotation/PRO_0000370369
http://togogenome.org/gene/9606:ANTXRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U7XUX1|||http://purl.uniprot.org/uniprot/A6NF34                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anthrax toxin receptor-like|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332166|||http://purl.uniprot.org/annotation/PRO_5016171740|||http://purl.uniprot.org/annotation/VAR_042963
http://togogenome.org/gene/9606:SIGLEC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15389                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014944|||http://purl.uniprot.org/annotation/VAR_014249|||http://purl.uniprot.org/annotation/VAR_014250|||http://purl.uniprot.org/annotation/VAR_014251|||http://purl.uniprot.org/annotation/VAR_020087|||http://purl.uniprot.org/annotation/VAR_049929
http://togogenome.org/gene/9606:NAA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSU3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Interaction with NAA15|||N-acetyltransferase|||N-alpha-acetyltransferase 11|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305009|||http://purl.uniprot.org/annotation/VAR_048164|||http://purl.uniprot.org/annotation/VAR_048165
http://togogenome.org/gene/9606:PBX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40426|||http://purl.uniprot.org/uniprot/Q96AL5                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox; TALE-type|||In isoform 5.|||In isoform PBX3b and isoform PBX3d.|||In isoform PBX3c and isoform PBX3d.|||PBC|||PBC-A|||PBC-B|||Pre-B-cell leukemia transcription factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049239|||http://purl.uniprot.org/annotation/VSP_002275|||http://purl.uniprot.org/annotation/VSP_002276|||http://purl.uniprot.org/annotation/VSP_002277|||http://purl.uniprot.org/annotation/VSP_046311
http://togogenome.org/gene/9606:LRRC69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNQ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Leucine-rich repeat-containing protein 69                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336072|||http://purl.uniprot.org/annotation/VAR_043481|||http://purl.uniprot.org/annotation/VSP_033810
http://togogenome.org/gene/9606:STAT5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N5W4|||http://purl.uniprot.org/uniprot/A8K6I5|||http://purl.uniprot.org/uniprot/K7EK35|||http://purl.uniprot.org/uniprot/P42229|||http://purl.uniprot.org/uniprot/Q59GY7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by JAK2|||SH2|||Signal transducer and activator of transcription 5A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182423|||http://purl.uniprot.org/annotation/VAR_052073|||http://purl.uniprot.org/annotation/VSP_053332
http://togogenome.org/gene/9606:H1-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16403                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylserine|||Abolishes methylation.|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.2|||N-acetylserine; partial|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-crotonyllysine; alternate|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT1 and EHMT2|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195906|||http://purl.uniprot.org/annotation/VAR_003618|||http://purl.uniprot.org/annotation/VAR_049304|||http://purl.uniprot.org/annotation/VAR_049305
http://togogenome.org/gene/9606:DBNDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9R9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dysbindin domain-containing protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292438|||http://purl.uniprot.org/annotation/VSP_026214|||http://purl.uniprot.org/annotation/VSP_037541
http://togogenome.org/gene/9606:UBE2L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14933                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||In isoform 2.|||UBC core|||Ubiquitin/ISG15-conjugating enzyme E2 L6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082478|||http://purl.uniprot.org/annotation/VSP_037344
http://togogenome.org/gene/9606:ARHGAP11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4F7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Rho GTPase-activating protein 11A|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000267213|||http://purl.uniprot.org/annotation/VAR_035546|||http://purl.uniprot.org/annotation/VSP_054102|||http://purl.uniprot.org/annotation/VSP_054103|||http://purl.uniprot.org/annotation/VSP_055370
http://togogenome.org/gene/9606:SLC25A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHV9|||http://purl.uniprot.org/uniprot/B4DPV4|||http://purl.uniprot.org/uniprot/P16260                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090616
http://togogenome.org/gene/9606:CRYZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08257                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Quinone oxidoreductase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160906|||http://purl.uniprot.org/annotation/VAR_022913|||http://purl.uniprot.org/annotation/VAR_022914|||http://purl.uniprot.org/annotation/VAR_048200|||http://purl.uniprot.org/annotation/VSP_042927|||http://purl.uniprot.org/annotation/VSP_042928|||http://purl.uniprot.org/annotation/VSP_046425
http://togogenome.org/gene/9606:FRMPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CM0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the interaction with ARHGEF7. Mutant overexpression in cultured neurons does not induce a significant increase in spine density contrary to wild type.|||Abolishes the interaction with DLG1, DLG2, DLG3 and DLG4/PSD95. Reduces protein localization to dendritic spines.|||Abolishes the interaction with DLG4/PSD95. Reduces protein localization to dendritic spines.|||Basic and acidic residues|||Disordered|||FERM|||FERM and PDZ domain-containing protein 4|||In XLID104.|||Nearly abolishes interaction with GPSM2; when associated with 1010-A-A-1011.|||Nearly abolishes interaction with GPSM2; when associated with A-990.|||PDZ|||Polar residues|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307132|||http://purl.uniprot.org/annotation/VAR_077481
http://togogenome.org/gene/9606:AGPAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRZ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  1-acyl-sn-glycerol-3-phosphate acyltransferase delta|||HXXXXD motif|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208197|||http://purl.uniprot.org/annotation/VSP_056928|||http://purl.uniprot.org/annotation/VSP_056929
http://togogenome.org/gene/9606:ARMC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3E5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In JBTS30; unknown pathological significance.|||In isoform 2.|||LisH|||LisH domain-containing protein ARMC9|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280595|||http://purl.uniprot.org/annotation/VAR_031170|||http://purl.uniprot.org/annotation/VAR_031171|||http://purl.uniprot.org/annotation/VAR_031172|||http://purl.uniprot.org/annotation/VAR_056739|||http://purl.uniprot.org/annotation/VAR_069411|||http://purl.uniprot.org/annotation/VAR_080497|||http://purl.uniprot.org/annotation/VAR_080498|||http://purl.uniprot.org/annotation/VAR_080499|||http://purl.uniprot.org/annotation/VAR_080500|||http://purl.uniprot.org/annotation/VAR_080501|||http://purl.uniprot.org/annotation/VAR_080502|||http://purl.uniprot.org/annotation/VSP_023804
http://togogenome.org/gene/9606:INTS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Integrator complex subunit 12|||PHD-type|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059312|||http://purl.uniprot.org/annotation/VAR_049629
http://togogenome.org/gene/9606:ELF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1W9|||http://purl.uniprot.org/uniprot/A8K443|||http://purl.uniprot.org/uniprot/Q9UKW6                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ETS|||ETS-related transcription factor Elf-5|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||PNT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204092|||http://purl.uniprot.org/annotation/VSP_014510|||http://purl.uniprot.org/annotation/VSP_014511|||http://purl.uniprot.org/annotation/VSP_014512|||http://purl.uniprot.org/annotation/VSP_054662
http://togogenome.org/gene/9606:IL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13007                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interleukin-24|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015386|||http://purl.uniprot.org/annotation/VAR_011974|||http://purl.uniprot.org/annotation/VAR_013097|||http://purl.uniprot.org/annotation/VAR_013098|||http://purl.uniprot.org/annotation/VSP_042673|||http://purl.uniprot.org/annotation/VSP_042674|||http://purl.uniprot.org/annotation/VSP_043915
http://togogenome.org/gene/9606:SVOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4V2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Phosphoserine|||Synaptic vesicle 2-related protein|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279452
http://togogenome.org/gene/9606:PRUNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A088AWP5|||http://purl.uniprot.org/uniprot/B4DJW7|||http://purl.uniprot.org/uniprot/B4DSQ3|||http://purl.uniprot.org/uniprot/D6RTK6|||http://purl.uniprot.org/uniprot/G8XWS8|||http://purl.uniprot.org/uniprot/Q5JUB8|||http://purl.uniprot.org/uniprot/Q8WUY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CRAL-TRIO|||DHH motif|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||Polar residues|||Protein prune homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089701|||http://purl.uniprot.org/annotation/VAR_069436|||http://purl.uniprot.org/annotation/VSP_039339|||http://purl.uniprot.org/annotation/VSP_039340|||http://purl.uniprot.org/annotation/VSP_039341|||http://purl.uniprot.org/annotation/VSP_039342|||http://purl.uniprot.org/annotation/VSP_039343
http://togogenome.org/gene/9606:TOP1MT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYD2|||http://purl.uniprot.org/uniprot/E5KMK7|||http://purl.uniprot.org/uniprot/Q969P6                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  DNA topoisomerase I eukaryotic-type|||DNA topoisomerase I, mitochondrial|||Disordered|||In isoform 2.|||Interaction with DNA|||Mitochondrion|||O-(3'-phospho-DNA)-tyrosine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034797|||http://purl.uniprot.org/annotation/VAR_021863|||http://purl.uniprot.org/annotation/VAR_052593|||http://purl.uniprot.org/annotation/VSP_044783
http://togogenome.org/gene/9606:RPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXK4|||http://purl.uniprot.org/uniprot/P46781                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Removed|||S4 RNA-binding|||Small ribosomal subunit protein uS4|||Small ribosomal subunit protein uS4 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132689|||http://purl.uniprot.org/annotation/VAR_036543
http://togogenome.org/gene/9606:EML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95834                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Echinoderm microtubule-associated protein-like 2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Tandem atypical propeller in EMLs|||WD 1|||WD 10|||WD 11|||WD 12|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050962|||http://purl.uniprot.org/annotation/VAR_022026|||http://purl.uniprot.org/annotation/VAR_024697|||http://purl.uniprot.org/annotation/VAR_031723|||http://purl.uniprot.org/annotation/VAR_031724|||http://purl.uniprot.org/annotation/VAR_035879|||http://purl.uniprot.org/annotation/VSP_042541|||http://purl.uniprot.org/annotation/VSP_047538
http://togogenome.org/gene/9606:CARD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by HIV-1 protease|||Abolished cleavage by HIV-1 protease, leading to prevent formation of the CARD8 inflammasome and subsequent pyroptosis.|||Abolished formation of inflammasome filaments.|||Abolished formation of inflammasome filaments. Abolished ability to induce pyroptosis.|||Abolished formation of inflammasome filaments. Reduced ability to induce pyroptosis.|||Abolished interaction with DPP9, without affecting autocatalytic cleavage.|||Basic and acidic residues|||CARD|||Caspase recruitment domain-containing protein 8|||Caspase recruitment domain-containing protein 8, C-terminus|||Caspase recruitment domain-containing protein 8, N-terminus|||Cleavage; by autolysis|||Complete loss of autocatalytic cleavage. Abolished ability to form the CARD8 inflammasome and trigger pyroptosis. Abolished sensitivity to Val-boroPro. Does not affect interaction with DPP9.|||Disordered|||Does not affect autocatalytic cleavage; does not affect interaction with DPP9; impaired interaction with the C-terminal fragment of CARD8 in the ternary complex.|||Does not affect cleavage by HIV-1 protease.|||Does not affect sensitivity to Val-boroPro.|||FIIND|||In IBD30.|||In IBD30; unknown pathological significance.|||In isoform 1 and isoform 2.|||In isoform 3 and isoform 2.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Increased autocalalytic cleavage.|||Inhibits homodimer formation.|||No effect on autocatalytic cleavage.|||Partial loss of autocatalytic cleavage.|||Polar residues|||Severe loss of autocatalytic cleavage.|||UPA|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144080|||http://purl.uniprot.org/annotation/PRO_0000452847|||http://purl.uniprot.org/annotation/PRO_0000452848|||http://purl.uniprot.org/annotation/VAR_048606|||http://purl.uniprot.org/annotation/VAR_061079|||http://purl.uniprot.org/annotation/VAR_084560|||http://purl.uniprot.org/annotation/VAR_084561|||http://purl.uniprot.org/annotation/VAR_084562|||http://purl.uniprot.org/annotation/VSP_061068|||http://purl.uniprot.org/annotation/VSP_061069|||http://purl.uniprot.org/annotation/VSP_061070|||http://purl.uniprot.org/annotation/VSP_061071|||http://purl.uniprot.org/annotation/VSP_061072|||http://purl.uniprot.org/annotation/VSP_061073|||http://purl.uniprot.org/annotation/VSP_061074
http://togogenome.org/gene/9606:PTPRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18433                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes integrin-mediated interaction with BCAR1 and BCAR3 and reduces interaction between BCAR1 and CRK and, BCAR1 and SRC. Abolishes integrin-induced SRC-mediated tyrosine phosphorylation of BCAR1. Abolishes integrin-mediated recruitment of BCAR1, BCAR3, CRK and PTPRA to focal adhesions. Reduces integrin-mediated activation and membrane recruitment of RAC1 and CDC42.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Receptor-type tyrosine-protein phosphatase alpha|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025433|||http://purl.uniprot.org/annotation/VAR_057134|||http://purl.uniprot.org/annotation/VSP_059405
http://togogenome.org/gene/9606:CFAP119                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4V9|||http://purl.uniprot.org/uniprot/H3BTQ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 119|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321842|||http://purl.uniprot.org/annotation/VSP_031807|||http://purl.uniprot.org/annotation/VSP_031808|||http://purl.uniprot.org/annotation/VSP_045828|||http://purl.uniprot.org/annotation/VSP_045829
http://togogenome.org/gene/9606:SARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49591|||http://purl.uniprot.org/uniprot/Q0VGA5|||http://purl.uniprot.org/uniprot/Q5T5C7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DNA binding.|||Abolishes enzyme activity.|||Abolishes nuclear localization.|||Abolishes nuclear localization; when associated with A-482 and A-485.|||Abolishes nuclear localization; when associated with A-482 and A-493.|||Abolishes nuclear localization; when associated with A-485 and A-493.|||Abolishes nuclear location. Decreases enzyme activity. Retains nuclear location and abolishes enzyme activity; when associated with R-378.|||Aminoacyl-transfer RNA synthetases class-II family profile|||Basic and acidic residues|||Catalytically inactive. Loss of serine binding. No effect on nuclear location.|||Decreased enzyme activity. Abolishes DNA binding.|||Disordered|||Important for serine binding|||In NEDMAS; impaired serine-activation of enzyme resulting in a significant decrease in the first step of the aminoacylation reaction; reduced protein stability; reduced protein expression.|||In NEDMAS; reduced protein stability resulting in a significant decrease in cellular enzyme activity.|||Interaction with tRNA|||Mildly decreased enzyme activity. Nearly abolishes DNA binding.|||Moderately decreased enzyme activity.|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Retains nuclear location and abolishes enzyme activity; when associated with V-383.|||Serine--tRNA ligase, cytoplasmic|||Strongly decreased enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122191|||http://purl.uniprot.org/annotation/VAR_078434|||http://purl.uniprot.org/annotation/VAR_087457
http://togogenome.org/gene/9606:DCAF12L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VW00                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 12-like protein 2|||Disordered|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306850|||http://purl.uniprot.org/annotation/VAR_062104
http://togogenome.org/gene/9606:VDAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y277                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Beta stranded|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||N-acetylcysteine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Voltage-dependent anion-selective channel protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050512|||http://purl.uniprot.org/annotation/VSP_005079
http://togogenome.org/gene/9606:HOXA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31269                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Breakpoint for translocation to form MSI2/HOXA9 fusion protein|||Breakpoint for translocation to form the NUP98-HOXA9 fusion protein|||Disordered|||Homeobox|||Homeobox protein Hox-A9|||Results in loss of methylation.|||Symmetric dimethylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200081
http://togogenome.org/gene/9606:FRMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y4L9|||http://purl.uniprot.org/uniprot/Q8N878                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||FERM domain-containing protein 1|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247364|||http://purl.uniprot.org/annotation/VAR_027099|||http://purl.uniprot.org/annotation/VAR_027100|||http://purl.uniprot.org/annotation/VSP_041267
http://togogenome.org/gene/9606:CIAPIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BT65|||http://purl.uniprot.org/uniprot/Q6FI81                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anamorsin|||Cx2C motif 1|||Cx2C motif 2|||Fe-S binding site A|||Fe-S binding site B|||In isoform 2.|||In isoform 3.|||Linker|||Methyltransferase type 11|||N-terminal SAM-like domain|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079288|||http://purl.uniprot.org/annotation/VAR_033747|||http://purl.uniprot.org/annotation/VAR_033748|||http://purl.uniprot.org/annotation/VSP_012360|||http://purl.uniprot.org/annotation/VSP_012361
http://togogenome.org/gene/9606:MYZAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CAP1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 4 and isoform 9.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9 and isoform 3.|||In isoform 9.|||Myocardial zonula adherens protein|||No effect on DYNLL1-binding.|||No effect on DYNLL1-binding; when associated with G-436.|||No effect on DYNLL1-binding; when associated with G-448.|||Required for DYNLL1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000376013|||http://purl.uniprot.org/annotation/VAR_055453|||http://purl.uniprot.org/annotation/VSP_037389|||http://purl.uniprot.org/annotation/VSP_037390|||http://purl.uniprot.org/annotation/VSP_037391|||http://purl.uniprot.org/annotation/VSP_037392|||http://purl.uniprot.org/annotation/VSP_037393|||http://purl.uniprot.org/annotation/VSP_037394|||http://purl.uniprot.org/annotation/VSP_037395|||http://purl.uniprot.org/annotation/VSP_037396|||http://purl.uniprot.org/annotation/VSP_037397|||http://purl.uniprot.org/annotation/VSP_037398
http://togogenome.org/gene/9606:IPO9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Importin N-terminal|||Importin-9|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120754
http://togogenome.org/gene/9606:VPS26A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLT1|||http://purl.uniprot.org/uniprot/O75436                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with VPS35 and endosomal subcellular location.|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Vacuolar protein sorting-associated protein 26A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073007|||http://purl.uniprot.org/annotation/VSP_044910
http://togogenome.org/gene/9606:OR2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A1/2A42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150459
http://togogenome.org/gene/9606:ZBTB40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR52|||http://purl.uniprot.org/uniprot/F8WAI8|||http://purl.uniprot.org/uniprot/Q1RMZ5|||http://purl.uniprot.org/uniprot/Q9NUA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047745|||http://purl.uniprot.org/annotation/VAR_052920|||http://purl.uniprot.org/annotation/VAR_052921|||http://purl.uniprot.org/annotation/VAR_052922|||http://purl.uniprot.org/annotation/VAR_052923|||http://purl.uniprot.org/annotation/VSP_007757|||http://purl.uniprot.org/annotation/VSP_007758|||http://purl.uniprot.org/annotation/VSP_007759
http://togogenome.org/gene/9606:SMIM10L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMW3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Small integral membrane protein 10-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433231
http://togogenome.org/gene/9606:NOTCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46531                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN|||(3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Cleavage; by ADAM17|||Cleavage; by furin-like protease|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 10|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 20|||EGF-like 21; calcium-binding|||EGF-like 22|||EGF-like 23; calcium-binding|||EGF-like 24|||EGF-like 25; calcium-binding|||EGF-like 26|||EGF-like 27|||EGF-like 28|||EGF-like 29|||EGF-like 3|||EGF-like 30|||EGF-like 31; calcium-binding|||EGF-like 32; calcium-binding|||EGF-like 33|||EGF-like 34|||EGF-like 35|||EGF-like 36|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Extracellular|||Formation of an artifactual disulfide bond with PSEN1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HIF1AN-binding|||Helical|||In AOS5.|||Interaction with DLL4|||Interaction with PSEN1|||LNR 1|||LNR 2|||LNR 3|||Loss of proteolytic cleavage by gamma-secretase.|||N-linked (GlcNAc...) asparagine|||Neurogenic locus notch homolog protein 1|||Notch 1 extracellular truncation|||Notch 1 intracellular domain|||O-linked (Fuc) serine|||O-linked (Fuc...) threonine|||O-linked (Fuc...) threonine; alternate|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; alternate|||O-linked (Glc...) serine|||O-linked (GlcNAc) serine|||O-linked (GlcNAc...) threonine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007674|||http://purl.uniprot.org/annotation/PRO_0000007675|||http://purl.uniprot.org/annotation/PRO_0000007676|||http://purl.uniprot.org/annotation/VAR_034898|||http://purl.uniprot.org/annotation/VAR_046618|||http://purl.uniprot.org/annotation/VAR_048990|||http://purl.uniprot.org/annotation/VAR_071960|||http://purl.uniprot.org/annotation/VAR_071961|||http://purl.uniprot.org/annotation/VAR_071962
http://togogenome.org/gene/9606:SYT15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQS2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Synaptotagmin-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183980|||http://purl.uniprot.org/annotation/VSP_008643|||http://purl.uniprot.org/annotation/VSP_008644|||http://purl.uniprot.org/annotation/VSP_008645|||http://purl.uniprot.org/annotation/VSP_008646
http://togogenome.org/gene/9606:CLIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15247                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal|||Chloride intracellular channel protein 2|||Foot loop|||GST C-terminal|||Helical; Note=After insertion into the membrane|||In MRXS32; results in stimulation of RYR channels activity with channels remaining open for longer times; the mutation may impair insertion of the protein into the membrane to form a functioning ion channel.|||In soluble form|||Joint loop|||N-terminal|||Required for insertion into the membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144205|||http://purl.uniprot.org/annotation/VAR_068898
http://togogenome.org/gene/9606:GALNT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5C5|||http://purl.uniprot.org/uniprot/Q96FL9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Polypeptide N-acetylgalactosaminyltransferase 14|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059133|||http://purl.uniprot.org/annotation/VAR_033948|||http://purl.uniprot.org/annotation/VSP_011221|||http://purl.uniprot.org/annotation/VSP_011222|||http://purl.uniprot.org/annotation/VSP_045121
http://togogenome.org/gene/9606:KCTD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD6|||Interaction with ANK1 isoform Mu17|||Interaction with CUL3|||Interaction with USP21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251248
http://togogenome.org/gene/9606:ARMC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BXQ8|||http://purl.uniprot.org/uniprot/Q8N2F6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ARM|||Armadillo repeat-containing|||Armadillo repeat-containing protein 10|||Disordered|||Helical|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297707|||http://purl.uniprot.org/annotation/VAR_034681|||http://purl.uniprot.org/annotation/VSP_027361|||http://purl.uniprot.org/annotation/VSP_027362|||http://purl.uniprot.org/annotation/VSP_043290|||http://purl.uniprot.org/annotation/VSP_047404
http://togogenome.org/gene/9606:FAAP24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5V6|||http://purl.uniprot.org/uniprot/K7EKQ4|||http://purl.uniprot.org/uniprot/Q9BTP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DisA/LigA helix-hairpin-helix motif|||Fanconi anemia core complex-associated protein 24|||Fanconi anemia core complex-associated protein 24 pseudonuclease|||RuvA domain 2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270961|||http://purl.uniprot.org/annotation/VAR_029828|||http://purl.uniprot.org/annotation/VAR_029829|||http://purl.uniprot.org/annotation/VAR_050989
http://togogenome.org/gene/9606:ZNF608                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPE6|||http://purl.uniprot.org/uniprot/Q9ULD9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 608                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280420|||http://purl.uniprot.org/annotation/VAR_031148|||http://purl.uniprot.org/annotation/VSP_023664
http://togogenome.org/gene/9606:PARP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1T0|||http://purl.uniprot.org/uniprot/G5E9U9|||http://purl.uniprot.org/uniprot/Q9H0J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosyl aspartic acid|||ADP-ribosylcysteine|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||PARP catalytic|||Phosphoserine|||Polar residues|||Protein mono-ADP-ribosyltransferase PARP12|||WWE|||WWE 1|||WWE 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211341|||http://purl.uniprot.org/annotation/VAR_050463|||http://purl.uniprot.org/annotation/VAR_050464|||http://purl.uniprot.org/annotation/VAR_050465
http://togogenome.org/gene/9606:CARTPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16568                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  CART(1-39)|||CART(42-89)|||Cocaine- and amphetamine-regulated transcript protein|||Cosegregates with obesity phenotype in a large family.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004433|||http://purl.uniprot.org/annotation/PRO_0000004434|||http://purl.uniprot.org/annotation/PRO_0000004435|||http://purl.uniprot.org/annotation/VAR_012199|||http://purl.uniprot.org/annotation/VAR_012200|||http://purl.uniprot.org/annotation/VAR_053022
http://togogenome.org/gene/9606:MAPRE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPY8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  APC-binding|||Acidic residues|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||In isoform 2.|||Loss of localization of CAMSAP2 stretches to the Golgi apparatus; when associated with A-226.|||Loss of localization of CAMSAP2 stretches to the Golgi apparatus; when associated with A-234.|||Microtubule-associated protein RP/EB family member 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213428|||http://purl.uniprot.org/annotation/VSP_012947
http://togogenome.org/gene/9606:ATP1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13637|||http://purl.uniprot.org/uniprot/Q53ES0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AHC2 and DEE99; strong decrease in ATPase activity.|||In AHC2.|||In AHC2; decreased ATPase activity.|||In AHC2; no effect on ATPase activity.|||In AHC2; strong decrease in ATPase activity.|||In CAPOS.|||In DEE99.|||In DEE99; decreased affinity for sodium ions; decreased affinity for potassium ions.|||In DEE99; decreased sodium/potassium-exchanging ATPase activity.|||In DYT12.|||In DYT12; there is a drastic 40- to 50-fold reduction in Na(+) affinity in the mutant protein.|||In isoform 2.|||In isoform 3.|||Interaction with phosphoinositide-3 kinase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine|||Probable disease-associated variant found in a patient with tonic-clonic seizures associated with profound developmental delay and paroxysmal movement disorder.|||Sodium/potassium-transporting ATPase subunit alpha-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046298|||http://purl.uniprot.org/annotation/VAR_026735|||http://purl.uniprot.org/annotation/VAR_026736|||http://purl.uniprot.org/annotation/VAR_026737|||http://purl.uniprot.org/annotation/VAR_026738|||http://purl.uniprot.org/annotation/VAR_026739|||http://purl.uniprot.org/annotation/VAR_026740|||http://purl.uniprot.org/annotation/VAR_068935|||http://purl.uniprot.org/annotation/VAR_068936|||http://purl.uniprot.org/annotation/VAR_068937|||http://purl.uniprot.org/annotation/VAR_068938|||http://purl.uniprot.org/annotation/VAR_068939|||http://purl.uniprot.org/annotation/VAR_068940|||http://purl.uniprot.org/annotation/VAR_068941|||http://purl.uniprot.org/annotation/VAR_068942|||http://purl.uniprot.org/annotation/VAR_068943|||http://purl.uniprot.org/annotation/VAR_068944|||http://purl.uniprot.org/annotation/VAR_068945|||http://purl.uniprot.org/annotation/VAR_068946|||http://purl.uniprot.org/annotation/VAR_068947|||http://purl.uniprot.org/annotation/VAR_068948|||http://purl.uniprot.org/annotation/VAR_068949|||http://purl.uniprot.org/annotation/VAR_068950|||http://purl.uniprot.org/annotation/VAR_068951|||http://purl.uniprot.org/annotation/VAR_068952|||http://purl.uniprot.org/annotation/VAR_068953|||http://purl.uniprot.org/annotation/VAR_070767|||http://purl.uniprot.org/annotation/VAR_070768|||http://purl.uniprot.org/annotation/VAR_070769|||http://purl.uniprot.org/annotation/VAR_070770|||http://purl.uniprot.org/annotation/VAR_070771|||http://purl.uniprot.org/annotation/VAR_070772|||http://purl.uniprot.org/annotation/VAR_070773|||http://purl.uniprot.org/annotation/VAR_070774|||http://purl.uniprot.org/annotation/VAR_078699|||http://purl.uniprot.org/annotation/VAR_086446|||http://purl.uniprot.org/annotation/VAR_086447|||http://purl.uniprot.org/annotation/VAR_086448|||http://purl.uniprot.org/annotation/VAR_086449|||http://purl.uniprot.org/annotation/VAR_086450|||http://purl.uniprot.org/annotation/VAR_086451|||http://purl.uniprot.org/annotation/VAR_086452|||http://purl.uniprot.org/annotation/VAR_086453|||http://purl.uniprot.org/annotation/VAR_086454|||http://purl.uniprot.org/annotation/VAR_086455|||http://purl.uniprot.org/annotation/VAR_086456|||http://purl.uniprot.org/annotation/VAR_086457|||http://purl.uniprot.org/annotation/VSP_046956|||http://purl.uniprot.org/annotation/VSP_046957
http://togogenome.org/gene/9606:KLRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12918                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Killer cell lectin-like receptor subfamily B member 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260000|||http://purl.uniprot.org/annotation/VAR_028981
http://togogenome.org/gene/9606:MYOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z421|||http://purl.uniprot.org/uniprot/Q99972                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by CAPN2|||Completely blocks endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226.|||Decreases protein stability.|||Disordered|||Impairs endoproteolytic processing.|||Impairs endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and released a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226.|||In GLC1A and GLC3A; the GLC3A patient also carries mutation H-368 in CYP1B1 suggesting digenic inheritance.|||In GLC1A.|||In GLC1A; forms homomultimeric complexes that migrate at molecular weights larger than their wild-type counterparts; these mutant complexes remain sequestered intracellularly.|||In GLC1A; heterozygote specific phenotype.|||In GLC1A; incomplete penetrance; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum.|||In GLC1A; induces stress fiber formation in only 5% of cells.|||In GLC1A; inhibits endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum.|||In GLC1A; no effect on protein stability.|||In GLC1A; severe form.|||In GLC1A; severe form; inhibits endoproteolytic processing; produced the highest inhibition of the endoproteolytic processing; mainly accumulates as insoluble aggregates inside the endoplasmic reticulum; inhibits neurite outgrowth.|||In GLC1A; unknown pathological significance.|||In GLC1A; unknown pathological significance; no significant effect on protein stability.|||Loss of higher molecular weight isoform.|||Microbody targeting signal|||Myocilin|||Myocilin, C-terminal fragment|||Myocilin, N-terminal fragment|||N-linked (GlcNAc...) asparagine|||No effect on protein stability.|||Olfactomedin-like|||Reduced processing.|||Reduced processing. Impairs endoproteolytic processing; when associated with A-229 or A-230. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-229 or A-230.|||Slightly decreased protein stability.|||Slightly increases endoproteolytic processing.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020084|||http://purl.uniprot.org/annotation/PRO_0000428749|||http://purl.uniprot.org/annotation/PRO_0000428750|||http://purl.uniprot.org/annotation/PRO_5006608283|||http://purl.uniprot.org/annotation/VAR_005468|||http://purl.uniprot.org/annotation/VAR_005469|||http://purl.uniprot.org/annotation/VAR_005470|||http://purl.uniprot.org/annotation/VAR_005471|||http://purl.uniprot.org/annotation/VAR_005472|||http://purl.uniprot.org/annotation/VAR_005473|||http://purl.uniprot.org/annotation/VAR_005474|||http://purl.uniprot.org/annotation/VAR_005475|||http://purl.uniprot.org/annotation/VAR_005476|||http://purl.uniprot.org/annotation/VAR_005477|||http://purl.uniprot.org/annotation/VAR_008969|||http://purl.uniprot.org/annotation/VAR_008970|||http://purl.uniprot.org/annotation/VAR_009665|||http://purl.uniprot.org/annotation/VAR_009666|||http://purl.uniprot.org/annotation/VAR_009667|||http://purl.uniprot.org/annotation/VAR_009668|||http://purl.uniprot.org/annotation/VAR_009669|||http://purl.uniprot.org/annotation/VAR_009670|||http://purl.uniprot.org/annotation/VAR_009671|||http://purl.uniprot.org/annotation/VAR_009672|||http://purl.uniprot.org/annotation/VAR_009673|||http://purl.uniprot.org/annotation/VAR_009674|||http://purl.uniprot.org/annotation/VAR_009675|||http://purl.uniprot.org/annotation/VAR_009676|||http://purl.uniprot.org/annotation/VAR_009677|||http://purl.uniprot.org/annotation/VAR_009678|||http://purl.uniprot.org/annotation/VAR_009679|||http://purl.uniprot.org/annotation/VAR_009680|||http://purl.uniprot.org/annotation/VAR_009681|||http://purl.uniprot.org/annotation/VAR_009682|||http://purl.uniprot.org/annotation/VAR_009683|||http://purl.uniprot.org/annotation/VAR_009684|||http://purl.uniprot.org/annotation/VAR_009685|||http://purl.uniprot.org/annotation/VAR_009686|||http://purl.uniprot.org/annotation/VAR_009687|||http://purl.uniprot.org/annotation/VAR_009688|||http://purl.uniprot.org/annotation/VAR_009689|||http://purl.uniprot.org/annotation/VAR_009690|||http://purl.uniprot.org/annotation/VAR_009691|||http://purl.uniprot.org/annotation/VAR_009692|||http://purl.uniprot.org/annotation/VAR_009693|||http://purl.uniprot.org/annotation/VAR_009694|||http://purl.uniprot.org/annotation/VAR_009695|||http://purl.uniprot.org/annotation/VAR_009696|||http://purl.uniprot.org/annotation/VAR_009697|||http://purl.uniprot.org/annotation/VAR_009698|||http://purl.uniprot.org/annotation/VAR_009699|||http://purl.uniprot.org/annotation/VAR_009700|||http://purl.uniprot.org/annotation/VAR_014943|||http://purl.uniprot.org/annotation/VAR_054269|||http://purl.uniprot.org/annotation/VAR_054270|||http://purl.uniprot.org/annotation/VAR_054271|||http://purl.uniprot.org/annotation/VAR_054272|||http://purl.uniprot.org/annotation/VAR_054273|||http://purl.uniprot.org/annotation/VAR_054274|||http://purl.uniprot.org/annotation/VAR_054275|||http://purl.uniprot.org/annotation/VAR_054276|||http://purl.uniprot.org/annotation/VAR_054277|||http://purl.uniprot.org/annotation/VAR_054278|||http://purl.uniprot.org/annotation/VAR_054279|||http://purl.uniprot.org/annotation/VAR_054280|||http://purl.uniprot.org/annotation/VAR_054281|||http://purl.uniprot.org/annotation/VAR_054282|||http://purl.uniprot.org/annotation/VAR_054283|||http://purl.uniprot.org/annotation/VAR_054284|||http://purl.uniprot.org/annotation/VAR_054285|||http://purl.uniprot.org/annotation/VAR_054286|||http://purl.uniprot.org/annotation/VAR_054287|||http://purl.uniprot.org/annotation/VAR_054288|||http://purl.uniprot.org/annotation/VAR_054289|||http://purl.uniprot.org/annotation/VAR_054290|||http://purl.uniprot.org/annotation/VAR_054291|||http://purl.uniprot.org/annotation/VAR_054292|||http://purl.uniprot.org/annotation/VAR_054293|||http://purl.uniprot.org/annotation/VAR_054294|||http://purl.uniprot.org/annotation/VAR_054295|||http://purl.uniprot.org/annotation/VAR_054296|||http://purl.uniprot.org/annotation/VAR_054297|||http://purl.uniprot.org/annotation/VAR_054298|||http://purl.uniprot.org/annotation/VAR_054299|||http://purl.uniprot.org/annotation/VAR_054300|||http://purl.uniprot.org/annotation/VAR_054301|||http://purl.uniprot.org/annotation/VAR_054302|||http://purl.uniprot.org/annotation/VAR_054303|||http://purl.uniprot.org/annotation/VAR_054304|||http://purl.uniprot.org/annotation/VAR_054305|||http://purl.uniprot.org/annotation/VAR_054306|||http://purl.uniprot.org/annotation/VAR_054307|||http://purl.uniprot.org/annotation/VAR_054308|||http://purl.uniprot.org/annotation/VAR_054309
http://togogenome.org/gene/9606:LST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00453                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 11 and isoform 13.|||In isoform 12.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6, isoform 7, isoform 10 and isoform 13.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Leukocyte-specific transcript 1 protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084507|||http://purl.uniprot.org/annotation/VSP_046459|||http://purl.uniprot.org/annotation/VSP_047367|||http://purl.uniprot.org/annotation/VSP_050577|||http://purl.uniprot.org/annotation/VSP_050578|||http://purl.uniprot.org/annotation/VSP_050579|||http://purl.uniprot.org/annotation/VSP_050580|||http://purl.uniprot.org/annotation/VSP_050581|||http://purl.uniprot.org/annotation/VSP_050582|||http://purl.uniprot.org/annotation/VSP_050583|||http://purl.uniprot.org/annotation/VSP_050584|||http://purl.uniprot.org/annotation/VSP_050586|||http://purl.uniprot.org/annotation/VSP_050587
http://togogenome.org/gene/9606:GFER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55789                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||ERV/ALR sulfhydryl oxidase|||FAD-linked sulfhydryl oxidase ALR|||In MPMCD; less stable than the wild-type protein within the mitochondria, increased rate of dissociation of FAD by about 45-fold.|||In isoform 2.|||Interchain (with C-204)|||Interchain (with C-95)|||Phosphoserine|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208548|||http://purl.uniprot.org/annotation/VAR_061994|||http://purl.uniprot.org/annotation/VAR_063435|||http://purl.uniprot.org/annotation/VSP_040393
http://togogenome.org/gene/9606:NKX6-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C056                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-6.2|||In SPAX8; loss of protein expression.|||In SPAX8; unknown pathological significance.|||Repressor domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300635|||http://purl.uniprot.org/annotation/VAR_034878|||http://purl.uniprot.org/annotation/VAR_079480|||http://purl.uniprot.org/annotation/VAR_079481
http://togogenome.org/gene/9606:CACNA2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZS8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cache|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Interchain (between alpha-2-3 and delta-3 chains)|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||VWFA|||Voltage-dependent calcium channel subunit alpha-2-3|||Voltage-dependent calcium channel subunit alpha-2/delta-3|||Voltage-dependent calcium channel subunit delta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304646|||http://purl.uniprot.org/annotation/PRO_0000304647|||http://purl.uniprot.org/annotation/PRO_0000304648|||http://purl.uniprot.org/annotation/VSP_028064|||http://purl.uniprot.org/annotation/VSP_028065|||http://purl.uniprot.org/annotation/VSP_028066|||http://purl.uniprot.org/annotation/VSP_028067
http://togogenome.org/gene/9606:RAB3GAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J9AUI2|||http://purl.uniprot.org/uniprot/B9A6J2|||http://purl.uniprot.org/uniprot/Q15042                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In WARBM1; abolishes GEF activity towards RAB18; loss of RAB18 membrane association; no effect on GAP activity; no effect on GAP activity towards the RAB3 proteins RAB5A or RAB43.|||In isoform 2.|||In isoform 3.|||Loss of function.|||No effect.|||Phosphoserine|||Phosphothreonine|||Rab3 GTPase-activating protein catalytic subunit|||Rab3GAP catalytic subunit C-terminal|||Rab3GAP catalytic subunit conserved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191655|||http://purl.uniprot.org/annotation/VAR_051716|||http://purl.uniprot.org/annotation/VAR_086019|||http://purl.uniprot.org/annotation/VAR_086020|||http://purl.uniprot.org/annotation/VSP_054068|||http://purl.uniprot.org/annotation/VSP_054475|||http://purl.uniprot.org/annotation/VSP_054476
http://togogenome.org/gene/9606:GHSR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92847                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Growth hormone secretagogue receptor type 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In GHDP; affects cell-surface expression; impairs constitutive activity; does not affect the ability to respond to ghrelin.|||In GHDP; results in partial loss of constitutive activity of the receptor; does not affect response to ghrelin; does not affect receptor cell-surface expression.|||In isoform 1B.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069479|||http://purl.uniprot.org/annotation/VAR_032705|||http://purl.uniprot.org/annotation/VAR_049389|||http://purl.uniprot.org/annotation/VAR_073173|||http://purl.uniprot.org/annotation/VSP_001916|||http://purl.uniprot.org/annotation/VSP_001917
http://togogenome.org/gene/9606:COPS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN01|||http://purl.uniprot.org/uniprot/Q9UNS2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  COP9 signalosome complex subunit 3|||Disordered|||In isoform 2.|||N-acetylalanine|||PCI|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120978|||http://purl.uniprot.org/annotation/VSP_044271
http://togogenome.org/gene/9606:ATP13A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4D4|||http://purl.uniprot.org/uniprot/Q8NBS1|||http://purl.uniprot.org/uniprot/Q9NQ11                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Abolishes glycosylation.|||Autophosphorylated but displays limited spermine-induced ATPase activity and lacks spermine-induced dephosphorylation.|||Cytoplasmic|||Disordered|||Helical|||In KRS; decreased ATPase activity; no effect on stability; no effect on location.|||In KRS; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location; impaired autophagosome-lysosome fusion; impaired degradation of protein aggregates.|||In KRS; decreased protein stability; loss of autophosphorylation; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of lysosomal membrane location; impaired autophagosome-lysosome fusion; impaired degradation of protein aggregates.|||In KRS; found in two affected brothers also carrying C-481 in FBXO7; decreased protein stability; increased degradation by proteasome; novel location to endoplasmic reticulum; loss of ATPase activity; loss of autophosphorylation.|||In KRS; no effect on stability; no effect on location; decreased ATPase activity.|||In KRS; some patients manifest neuropathologic findings suggestive of neuronal ceroid lipofuscinosis.|||In KRS; the mutant protein is retained in the endoplasmic reticulum.|||In KRS; unknown pathological significance.|||In KRS; unknown pathological significance; associated in cis with Phe-441 in one individual.|||In KRS; unknown pathological significance; associated in cis with Thr-1069 in one individual.|||In SPG78; no effect on protein stability; loss of autophosphorylation; loss of lysosomal location; loss of ATPase activity.|||In a patient with early onset Parkinson disease and KRS; decreased ATPase activity; no effect on autophosphorylation; no effect on stability; no effect on location.|||In isoform B and isoform 3.|||In isoform B.|||Loss of ATPase function, autophosphorylation and protection against mitochondrial stress.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on lipid binding.|||Phosphoserine|||Polar residues|||Polyamine-transporting ATPase 13A2|||Reduced spermine-induced ATPase activity and lack of spermine-induced dephosphorylation.|||Reduced spermine-induced ATPase activity.|||Reduces lipid binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046423|||http://purl.uniprot.org/annotation/VAR_058451|||http://purl.uniprot.org/annotation/VAR_058452|||http://purl.uniprot.org/annotation/VAR_058453|||http://purl.uniprot.org/annotation/VAR_058454|||http://purl.uniprot.org/annotation/VAR_058455|||http://purl.uniprot.org/annotation/VAR_058456|||http://purl.uniprot.org/annotation/VAR_058457|||http://purl.uniprot.org/annotation/VAR_058458|||http://purl.uniprot.org/annotation/VAR_058459|||http://purl.uniprot.org/annotation/VAR_058460|||http://purl.uniprot.org/annotation/VAR_058461|||http://purl.uniprot.org/annotation/VAR_066019|||http://purl.uniprot.org/annotation/VAR_066020|||http://purl.uniprot.org/annotation/VAR_066021|||http://purl.uniprot.org/annotation/VAR_070194|||http://purl.uniprot.org/annotation/VAR_078055|||http://purl.uniprot.org/annotation/VAR_078056|||http://purl.uniprot.org/annotation/VAR_083537|||http://purl.uniprot.org/annotation/VAR_083538|||http://purl.uniprot.org/annotation/VSP_007310|||http://purl.uniprot.org/annotation/VSP_007311|||http://purl.uniprot.org/annotation/VSP_007312
http://togogenome.org/gene/9606:SCUBE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX30                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CUB|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In SSFSC2.|||In SSFSC2; decreased homodimerization; does not affect heterodimerization with SCUBE1 or SCUBE2; does not affect localization to the cell surface.|||In SSFSC2; loss of stimulation of BMP signaling; does not affect localization to the cell surface.|||In SSFSC2; loss of stimulation of BMP signaling; does not localize to the cell surface due to impaired secretion.|||In SSFSC2; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Signal peptide, CUB and EGF-like domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250616|||http://purl.uniprot.org/annotation/VAR_048994|||http://purl.uniprot.org/annotation/VAR_085320|||http://purl.uniprot.org/annotation/VAR_085321|||http://purl.uniprot.org/annotation/VAR_085322|||http://purl.uniprot.org/annotation/VAR_085323|||http://purl.uniprot.org/annotation/VAR_085324|||http://purl.uniprot.org/annotation/VSP_052167
http://togogenome.org/gene/9606:CALCRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16602                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcitonin gene-related peptide type 1 receptor|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In LMPHM8; unknown pathological significance; decreased function in adenylate cyclase-modulating G protein-coupled receptor signaling pathway; decreased interaction with RAMP2; decreased protein levels at the cell membrane.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Strongly reduced affinity for adrenomedullin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012811|||http://purl.uniprot.org/annotation/VAR_049453|||http://purl.uniprot.org/annotation/VAR_049454|||http://purl.uniprot.org/annotation/VAR_054822|||http://purl.uniprot.org/annotation/VAR_083775
http://togogenome.org/gene/9606:HMG20A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMG1|||http://purl.uniprot.org/uniprot/Q9NP66                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HMG box|||High mobility group protein 20A|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238649|||http://purl.uniprot.org/annotation/VSP_018621|||http://purl.uniprot.org/annotation/VSP_018622
http://togogenome.org/gene/9606:DKK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6SYF8|||http://purl.uniprot.org/uniprot/Q9UBP4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf N-terminal cysteine-rich|||Dickkopf-related protein 3|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007222|||http://purl.uniprot.org/annotation/PRO_5003342009|||http://purl.uniprot.org/annotation/VAR_030787|||http://purl.uniprot.org/annotation/VAR_057516
http://togogenome.org/gene/9606:EPHA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54764                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold reduced affinity for EFNB2; when associated with A-40.|||10-fold reduced affinity for EFNB2; when associated with A-42.|||Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 4|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a bladder carcinoma NOS sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016807|||http://purl.uniprot.org/annotation/VAR_042135|||http://purl.uniprot.org/annotation/VAR_042136|||http://purl.uniprot.org/annotation/VAR_042137|||http://purl.uniprot.org/annotation/VAR_049721|||http://purl.uniprot.org/annotation/VSP_056016
http://togogenome.org/gene/9606:QPCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16769                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity.|||Glutaminyl-peptide cyclotransferase|||Greatly lowers activity.|||In isoform 2.|||Lowers activity by approximately 30%.|||Lowers activity by approximately 35%.|||Lowers activity by approximately 40%.|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Reduces activity by 87%.|||Reduces activity by 96%.|||Reduces activity by 99%.|||Reduces activity by about 50%.|||Reduces activity by about 98%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022195|||http://purl.uniprot.org/annotation/VAR_005569|||http://purl.uniprot.org/annotation/VAR_053956|||http://purl.uniprot.org/annotation/VAR_053957|||http://purl.uniprot.org/annotation/VSP_038487
http://togogenome.org/gene/9606:RHOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61586|||http://purl.uniprot.org/uniprot/Q9BVT0                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosylasparagine; by botulinum toxin|||(Microbial infection) Cleavage; by yopT|||(Microbial infection) N6-stearoyl lysine|||(Microbial infection) O-AMP-threonine; by Vibrio VopS|||(Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate|||(Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate|||(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate|||(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate|||5-glutamyl serotonin|||Abolished monoglucosylation by C.difficile toxin TcdA. Abolished O-GlcNAcylation by C.novyi toxin TcdA.|||Abolishes AMPylation by Haemophilus IbpA.|||Abolishes interaction with DGKQ.|||Causes constitutive activation.|||Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT.|||Cysteine methyl ester|||Decreased Rho protein signal transduction. Decreased substrate adhesion-dependent cell spreading. Decreased stress fibers assembly. Decreased cytoplasmic microtubule organization.|||Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In 3KR mutant; abolished stearoylation in response to S.flexneri infection.|||In EDFAOB; somatic mosaic variant; decreased Rho protein signal transduction; decreased substrate adhesion-dependent cell spreading; decreased number of stress fibers assembly; decreased cytoplasmic microtubule organization.|||In EDFAOB; somatic mosaic variant; decreased Rho protein signal transduction; decreased substrate adhesion-dependent cell spreading; decreased stress fibers assembly; decreased cytoplasmic microtubule organization.|||Increased Rho protein signal transduction. Constitutively active.|||Phosphoserine; by PKG/PRKG1|||Reduced FBXL19-mediated ubiquitination and subsequent degradation.|||Removed in mature form|||S-geranylgeranyl cysteine|||Switch II region; involved in RAP1GDS1 isoform 2 binding|||Transforming protein RhoA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030411|||http://purl.uniprot.org/annotation/PRO_0000030412|||http://purl.uniprot.org/annotation/VAR_083545|||http://purl.uniprot.org/annotation/VAR_083546
http://togogenome.org/gene/9606:USP17L25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:TRPV5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YY98|||http://purl.uniprot.org/uniprot/Q9NQA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with S100A10|||Involved in Ca(2+)-dependent inactivation|||Ion transport|||Loss of glycosylation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Pore-forming|||Transient receptor potential cation channel subfamily V member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215350|||http://purl.uniprot.org/annotation/VAR_022247|||http://purl.uniprot.org/annotation/VAR_022248|||http://purl.uniprot.org/annotation/VAR_022249|||http://purl.uniprot.org/annotation/VAR_022250|||http://purl.uniprot.org/annotation/VSP_057199|||http://purl.uniprot.org/annotation/VSP_057200
http://togogenome.org/gene/9606:NPY5R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15761                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 5|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069939
http://togogenome.org/gene/9606:JDP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Jun dimerization protein 2|||Leucine-zipper|||Phosphothreonine; by MAPK8|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331130|||http://purl.uniprot.org/annotation/VAR_042738|||http://purl.uniprot.org/annotation/VSP_047128
http://togogenome.org/gene/9606:CCR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51677|||http://purl.uniprot.org/uniprot/Q8TDP4|||http://purl.uniprot.org/uniprot/Q8TDP5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-C chemokine receptor type 3|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069239|||http://purl.uniprot.org/annotation/VAR_010668|||http://purl.uniprot.org/annotation/VAR_020067|||http://purl.uniprot.org/annotation/VAR_049382|||http://purl.uniprot.org/annotation/VSP_046704
http://togogenome.org/gene/9606:NKTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30414                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Arg/Ser tandem repeat-rich|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||NK-tumor recognition protein|||PPIase cyclophilin-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064217|||http://purl.uniprot.org/annotation/VAR_051773|||http://purl.uniprot.org/annotation/VAR_051774|||http://purl.uniprot.org/annotation/VAR_061765|||http://purl.uniprot.org/annotation/VAR_061766
http://togogenome.org/gene/9606:SRGAP2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJJ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not improve solubility; when associated with R-108, R-205, R-235 and R-250.|||Does not improve solubility; when associated with R-73, R-108, R-205 and R-235.|||Does not improve solubility; when associated with R-73, R-108, R-205 and R-250.|||Does not improve solubility; when associated with R-73, R-108, R-235 and R-250.|||Does not improve solubility; when associated with R-73, R-205, R-235 and R-250.|||F-BAR|||SLIT-ROBO Rho GTPase-activating protein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000418193
http://togogenome.org/gene/9606:MBD3L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NE82                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative methyl-CpG-binding domain protein 3-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349233
http://togogenome.org/gene/9606:TARBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15633                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  DRBM 1|||DRBM 2|||DRBM 3|||In isoform 2.|||Phosphoserine|||RISC-loading complex subunit TARBP2|||Sufficient for interaction with DICER1|||Sufficient for interaction with PRKRA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065622|||http://purl.uniprot.org/annotation/VAR_046992|||http://purl.uniprot.org/annotation/VSP_035584
http://togogenome.org/gene/9606:SYBU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4D2|||http://purl.uniprot.org/uniprot/Q9NX95                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Sufficient for interaction with KIF5B|||Sufficient for interaction with STX1A|||Syntabulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050798|||http://purl.uniprot.org/annotation/VSP_019718|||http://purl.uniprot.org/annotation/VSP_019719|||http://purl.uniprot.org/annotation/VSP_019720|||http://purl.uniprot.org/annotation/VSP_019721|||http://purl.uniprot.org/annotation/VSP_019722
http://togogenome.org/gene/9606:C15orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5M9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Mitochondrion|||Polar residues|||Uncharacterized protein C15orf62, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332136
http://togogenome.org/gene/9606:LRP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DS68|||http://purl.uniprot.org/uniprot/Q86VZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LDL-receptor class A|||Low-density lipoprotein receptor-related protein 11|||MANSC|||N-linked (GlcNAc...) asparagine|||PKD|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017337|||http://purl.uniprot.org/annotation/VAR_025537|||http://purl.uniprot.org/annotation/VAR_025538|||http://purl.uniprot.org/annotation/VAR_056002|||http://purl.uniprot.org/annotation/VAR_056003|||http://purl.uniprot.org/annotation/VSP_017535|||http://purl.uniprot.org/annotation/VSP_017536
http://togogenome.org/gene/9606:GARIN5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Golgi-associated RAB2 interactor protein 5A|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334697|||http://purl.uniprot.org/annotation/VAR_043465|||http://purl.uniprot.org/annotation/VSP_033760
http://togogenome.org/gene/9606:TMEM80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7W9|||http://purl.uniprot.org/uniprot/Q96HE8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Pro residues|||Transmembrane protein 80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287873|||http://purl.uniprot.org/annotation/VSP_059531|||http://purl.uniprot.org/annotation/VSP_059532
http://togogenome.org/gene/9606:CD302                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT00|||http://purl.uniprot.org/uniprot/Q8IX05                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||CD302 antigen|||Cytoplasmic|||Extracellular|||Helical|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252332|||http://purl.uniprot.org/annotation/PRO_5001831886|||http://purl.uniprot.org/annotation/VAR_050101|||http://purl.uniprot.org/annotation/VSP_044258|||http://purl.uniprot.org/annotation/VSP_044259
http://togogenome.org/gene/9606:IL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22301|||http://purl.uniprot.org/uniprot/Q6FGW4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  About 80% loss of IL10RA binding.|||In a family affected by Crohn disease; decreases secretion thereby reducing the anti-inflammatory effect.|||Interleukin family protein|||Interleukin-10|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015360|||http://purl.uniprot.org/annotation/PRO_5014310430|||http://purl.uniprot.org/annotation/VAR_015883
http://togogenome.org/gene/9606:SDE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ49                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage|||Disordered|||In isoform 2.|||In isoform 3.|||No binding to PCNA; no cleavage at Gly-77.|||No cleavage at Gly-77.|||No effect on cleavage at Gly-77.|||PIP-box|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAP|||Splicing regulator SDE2|||UBL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286084|||http://purl.uniprot.org/annotation/PRO_0000442521|||http://purl.uniprot.org/annotation/VAR_032068|||http://purl.uniprot.org/annotation/VSP_024981|||http://purl.uniprot.org/annotation/VSP_024982
http://togogenome.org/gene/9606:SLC25A29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8R3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||Mitochondrial basic amino acids transporter|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090632|||http://purl.uniprot.org/annotation/VSP_046286|||http://purl.uniprot.org/annotation/VSP_046287|||http://purl.uniprot.org/annotation/VSP_055335
http://togogenome.org/gene/9606:PLA2G6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60733                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  85/88 kDa calcium-independent phospholipase A2|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 9|||Abolishes phospholipase and lysophospholipase activities.|||Calmodulin-binding (1-9-14 motif)|||Calmodulin-binding (IQ motif)|||DGA/G|||GXGXXG|||GXSXG|||Helical|||In NBIA2A and NBIA2B; significantly reduces phospholipase and lysophospholipase activities.|||In NBIA2A.|||In NBIA2A; complete loss of phospholipase and lysophospholipase activities.|||In NBIA2A; significantly reduces phospholipase and lysophospholipase activities.|||In NBIA2B.|||In NBIA2B; increases phospholipase, lysophospholipase and thioesterase activities.|||In PARK14; has no effect on phospholipase, lysophospholipase and thioesterase activities.|||In isoform Ankyrin-iPLA2-1.|||In isoform Ankyrin-iPLA2-2.|||In isoform SH-iPLA2.|||Nucleophile|||PNPLA|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067037|||http://purl.uniprot.org/annotation/VAR_018961|||http://purl.uniprot.org/annotation/VAR_018962|||http://purl.uniprot.org/annotation/VAR_018963|||http://purl.uniprot.org/annotation/VAR_018964|||http://purl.uniprot.org/annotation/VAR_018965|||http://purl.uniprot.org/annotation/VAR_029371|||http://purl.uniprot.org/annotation/VAR_029372|||http://purl.uniprot.org/annotation/VAR_029373|||http://purl.uniprot.org/annotation/VAR_029374|||http://purl.uniprot.org/annotation/VAR_037903|||http://purl.uniprot.org/annotation/VAR_062530|||http://purl.uniprot.org/annotation/VAR_062531|||http://purl.uniprot.org/annotation/VAR_070600|||http://purl.uniprot.org/annotation/VAR_070601|||http://purl.uniprot.org/annotation/VAR_079753|||http://purl.uniprot.org/annotation/VAR_083527|||http://purl.uniprot.org/annotation/VAR_083528|||http://purl.uniprot.org/annotation/VAR_083529|||http://purl.uniprot.org/annotation/VAR_083530|||http://purl.uniprot.org/annotation/VAR_083531|||http://purl.uniprot.org/annotation/VSP_000277|||http://purl.uniprot.org/annotation/VSP_000278|||http://purl.uniprot.org/annotation/VSP_000279|||http://purl.uniprot.org/annotation/VSP_000280|||http://purl.uniprot.org/annotation/VSP_000281|||http://purl.uniprot.org/annotation/VSP_000282
http://togogenome.org/gene/9606:ZNG1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60748|||http://purl.uniprot.org/uniprot/Q5RIA9|||http://purl.uniprot.org/uniprot/Q5RIB3|||http://purl.uniprot.org/uniprot/Q5RIB5|||http://purl.uniprot.org/uniprot/Q6NVZ8|||http://purl.uniprot.org/uniprot/Q9H2J8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CXCC motif|||CobW C-terminal|||CobW/HypB/UreG nucleotide-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Zinc-regulated GTPase metalloprotein activator 1E|||psi-PxLVp motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317239|||http://purl.uniprot.org/annotation/VAR_067710|||http://purl.uniprot.org/annotation/VAR_067711|||http://purl.uniprot.org/annotation/VSP_033808|||http://purl.uniprot.org/annotation/VSP_040475|||http://purl.uniprot.org/annotation/VSP_040476
http://togogenome.org/gene/9606:DENND2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUF6|||http://purl.uniprot.org/uniprot/Q9ULE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DENN domain-containing protein 2A|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242682|||http://purl.uniprot.org/annotation/VAR_026856|||http://purl.uniprot.org/annotation/VAR_026857|||http://purl.uniprot.org/annotation/VAR_026858|||http://purl.uniprot.org/annotation/VSP_019466|||http://purl.uniprot.org/annotation/VSP_019467
http://togogenome.org/gene/9606:WFS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4V6|||http://purl.uniprot.org/uniprot/O76024                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In CTRCT41.|||In DFNA6.|||In DFNA6; also found in a patient with type 2 diabetes; unknown pathological significance.|||In DFNA6; benign variant.|||In DFNA6; unknown pathological significance.|||In WFS1.|||In WFS1; greatly reduces protein expression compared to wild-type.|||In WFS1; mild form.|||In WFSL.|||In WFSL; greatly reduces protein expression compared to wild-type.|||In WFSL; mildly decreases protein expression compared to wild-type.|||Interaction with ATP6V1A|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Wolframin|||Wolframin EF-hand|||Wolframin OB-fold|||Wolframin cysteine-rich                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065963|||http://purl.uniprot.org/annotation/VAR_005840|||http://purl.uniprot.org/annotation/VAR_005841|||http://purl.uniprot.org/annotation/VAR_005842|||http://purl.uniprot.org/annotation/VAR_005843|||http://purl.uniprot.org/annotation/VAR_005844|||http://purl.uniprot.org/annotation/VAR_005845|||http://purl.uniprot.org/annotation/VAR_009109|||http://purl.uniprot.org/annotation/VAR_009110|||http://purl.uniprot.org/annotation/VAR_009111|||http://purl.uniprot.org/annotation/VAR_009112|||http://purl.uniprot.org/annotation/VAR_009113|||http://purl.uniprot.org/annotation/VAR_009114|||http://purl.uniprot.org/annotation/VAR_009115|||http://purl.uniprot.org/annotation/VAR_009116|||http://purl.uniprot.org/annotation/VAR_009117|||http://purl.uniprot.org/annotation/VAR_009118|||http://purl.uniprot.org/annotation/VAR_009119|||http://purl.uniprot.org/annotation/VAR_010602|||http://purl.uniprot.org/annotation/VAR_010603|||http://purl.uniprot.org/annotation/VAR_010604|||http://purl.uniprot.org/annotation/VAR_011305|||http://purl.uniprot.org/annotation/VAR_011306|||http://purl.uniprot.org/annotation/VAR_011307|||http://purl.uniprot.org/annotation/VAR_011308|||http://purl.uniprot.org/annotation/VAR_011309|||http://purl.uniprot.org/annotation/VAR_011310|||http://purl.uniprot.org/annotation/VAR_011311|||http://purl.uniprot.org/annotation/VAR_011312|||http://purl.uniprot.org/annotation/VAR_011313|||http://purl.uniprot.org/annotation/VAR_011314|||http://purl.uniprot.org/annotation/VAR_014034|||http://purl.uniprot.org/annotation/VAR_014035|||http://purl.uniprot.org/annotation/VAR_014036|||http://purl.uniprot.org/annotation/VAR_014037|||http://purl.uniprot.org/annotation/VAR_014038|||http://purl.uniprot.org/annotation/VAR_014995|||http://purl.uniprot.org/annotation/VAR_014996|||http://purl.uniprot.org/annotation/VAR_024554|||http://purl.uniprot.org/annotation/VAR_029499|||http://purl.uniprot.org/annotation/VAR_029500|||http://purl.uniprot.org/annotation/VAR_029501|||http://purl.uniprot.org/annotation/VAR_029502|||http://purl.uniprot.org/annotation/VAR_029503|||http://purl.uniprot.org/annotation/VAR_029504|||http://purl.uniprot.org/annotation/VAR_029505|||http://purl.uniprot.org/annotation/VAR_029506|||http://purl.uniprot.org/annotation/VAR_032791|||http://purl.uniprot.org/annotation/VAR_032962|||http://purl.uniprot.org/annotation/VAR_032963|||http://purl.uniprot.org/annotation/VAR_032964|||http://purl.uniprot.org/annotation/VAR_032965|||http://purl.uniprot.org/annotation/VAR_032966|||http://purl.uniprot.org/annotation/VAR_032967|||http://purl.uniprot.org/annotation/VAR_032968|||http://purl.uniprot.org/annotation/VAR_032969|||http://purl.uniprot.org/annotation/VAR_068343|||http://purl.uniprot.org/annotation/VAR_068344|||http://purl.uniprot.org/annotation/VAR_068345|||http://purl.uniprot.org/annotation/VAR_068346|||http://purl.uniprot.org/annotation/VAR_068347|||http://purl.uniprot.org/annotation/VAR_070935|||http://purl.uniprot.org/annotation/VAR_074210|||http://purl.uniprot.org/annotation/VAR_074211|||http://purl.uniprot.org/annotation/VAR_074212|||http://purl.uniprot.org/annotation/VAR_074213|||http://purl.uniprot.org/annotation/VAR_074214|||http://purl.uniprot.org/annotation/VAR_080401
http://togogenome.org/gene/9606:DUSP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNI6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Dual specificity protein phosphatase 12|||N-acetylmethionine|||Phosphocysteine intermediate|||Phosphoserine|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094818|||http://purl.uniprot.org/annotation/VAR_033899
http://togogenome.org/gene/9606:MAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27816                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||17 X 14 AA tandem repeats|||2|||26 residues 1|||26 residues 2|||3|||4|||5|||6|||7|||8; truncated|||9|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Microtubule-associated protein 4|||N-acetylalanine|||No change in microtubule binding; no change in microtubule polymerization activity.|||No change in microtubule binding; reduced microtubule polymerization activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3|||Tau/MAP 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072751|||http://purl.uniprot.org/annotation/VAR_020361|||http://purl.uniprot.org/annotation/VAR_020362|||http://purl.uniprot.org/annotation/VAR_039566|||http://purl.uniprot.org/annotation/VAR_039567|||http://purl.uniprot.org/annotation/VAR_039568|||http://purl.uniprot.org/annotation/VAR_039569|||http://purl.uniprot.org/annotation/VAR_039570|||http://purl.uniprot.org/annotation/VAR_039571|||http://purl.uniprot.org/annotation/VSP_003200|||http://purl.uniprot.org/annotation/VSP_032065|||http://purl.uniprot.org/annotation/VSP_032066|||http://purl.uniprot.org/annotation/VSP_032067|||http://purl.uniprot.org/annotation/VSP_032068|||http://purl.uniprot.org/annotation/VSP_032069|||http://purl.uniprot.org/annotation/VSP_032070|||http://purl.uniprot.org/annotation/VSP_032071|||http://purl.uniprot.org/annotation/VSP_032072|||http://purl.uniprot.org/annotation/VSP_032073|||http://purl.uniprot.org/annotation/VSP_032074|||http://purl.uniprot.org/annotation/VSP_032075|||http://purl.uniprot.org/annotation/VSP_032076|||http://purl.uniprot.org/annotation/VSP_032077|||http://purl.uniprot.org/annotation/VSP_032078|||http://purl.uniprot.org/annotation/VSP_032079|||http://purl.uniprot.org/annotation/VSP_043240|||http://purl.uniprot.org/annotation/VSP_043241
http://togogenome.org/gene/9606:KLHL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM8|||http://purl.uniprot.org/uniprot/B4DX37|||http://purl.uniprot.org/uniprot/Q6JEL2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BACK|||BTB|||In SPGF11; results in impaired self-association.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 10|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119112|||http://purl.uniprot.org/annotation/VAR_069357|||http://purl.uniprot.org/annotation/VAR_069358
http://togogenome.org/gene/9606:ERICH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMI5|||http://purl.uniprot.org/uniprot/Q86X53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glutamate-rich protein 1|||In a colorectal cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087029|||http://purl.uniprot.org/annotation/VAR_035915|||http://purl.uniprot.org/annotation/VAR_050974
http://togogenome.org/gene/9606:DEFB104A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTQ1                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-defensin 104                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006973|||http://purl.uniprot.org/annotation/VAR_024767
http://togogenome.org/gene/9606:UBA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVT1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||Impairs ubiquitin activation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Ubiquitin-like modifier-activating enzyme 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277797|||http://purl.uniprot.org/annotation/VAR_030594|||http://purl.uniprot.org/annotation/VSP_023083|||http://purl.uniprot.org/annotation/VSP_023084|||http://purl.uniprot.org/annotation/VSP_023085|||http://purl.uniprot.org/annotation/VSP_023086|||http://purl.uniprot.org/annotation/VSP_023087
http://togogenome.org/gene/9606:TNR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L306|||http://purl.uniprot.org/uniprot/Q92752                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||Fibrinogen C-terminal|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||In NEDSTO.|||In NEDSTO; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Tenascin-R                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007747|||http://purl.uniprot.org/annotation/VAR_021479|||http://purl.uniprot.org/annotation/VAR_021906|||http://purl.uniprot.org/annotation/VAR_021907|||http://purl.uniprot.org/annotation/VAR_030737|||http://purl.uniprot.org/annotation/VAR_055780|||http://purl.uniprot.org/annotation/VAR_086584|||http://purl.uniprot.org/annotation/VAR_086585|||http://purl.uniprot.org/annotation/VAR_086586|||http://purl.uniprot.org/annotation/VAR_086587|||http://purl.uniprot.org/annotation/VAR_086588|||http://purl.uniprot.org/annotation/VAR_086589|||http://purl.uniprot.org/annotation/VSP_012993
http://togogenome.org/gene/9606:TRIM60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495X7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 60                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249189
http://togogenome.org/gene/9606:PEBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S96                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Important for secretion|||N-linked (GlcNAc...) (complex) asparagine|||Phosphatidylethanolamine-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023279|||http://purl.uniprot.org/annotation/VAR_050467|||http://purl.uniprot.org/annotation/VAR_050468
http://togogenome.org/gene/9606:ZNF484                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JVG2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 484                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233986|||http://purl.uniprot.org/annotation/VAR_033570|||http://purl.uniprot.org/annotation/VSP_043079|||http://purl.uniprot.org/annotation/VSP_044922
http://togogenome.org/gene/9606:TCEANC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5F6|||http://purl.uniprot.org/uniprot/B4DG85|||http://purl.uniprot.org/uniprot/Q8N8B7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||TFIIS N-terminal|||TFIIS central|||Transcription elongation factor A N-terminal and central domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259659|||http://purl.uniprot.org/annotation/VAR_028970|||http://purl.uniprot.org/annotation/VSP_039895
http://togogenome.org/gene/9606:CIDEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRY9|||http://purl.uniprot.org/uniprot/Q96AQ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CIDE-N|||Does not affect ability to mediate lipid droplet fusion.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lipid transferase CIDEC|||Required for liquid-liquid phase separation (LLPS)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144722|||http://purl.uniprot.org/annotation/VSP_012738|||http://purl.uniprot.org/annotation/VSP_012739|||http://purl.uniprot.org/annotation/VSP_012740|||http://purl.uniprot.org/annotation/VSP_045051
http://togogenome.org/gene/9606:ADGRE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48960                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor E5|||Adhesion G protein-coupled receptor E5 subunit alpha|||Adhesion G protein-coupled receptor E5 subunit beta|||Cleavage|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012868|||http://purl.uniprot.org/annotation/PRO_0000296235|||http://purl.uniprot.org/annotation/PRO_0000296236|||http://purl.uniprot.org/annotation/VAR_017760|||http://purl.uniprot.org/annotation/VSP_009411|||http://purl.uniprot.org/annotation/VSP_009412
http://togogenome.org/gene/9606:HSPA4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE7|||http://purl.uniprot.org/uniprot/B4DXT2|||http://purl.uniprot.org/uniprot/B4DZR0|||http://purl.uniprot.org/uniprot/E9PDE8|||http://purl.uniprot.org/uniprot/O95757                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heat shock 70 kDa protein 4L|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078280|||http://purl.uniprot.org/annotation/VAR_025405|||http://purl.uniprot.org/annotation/VAR_031214|||http://purl.uniprot.org/annotation/VAR_055966
http://togogenome.org/gene/9606:NDUFA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15239|||http://purl.uniprot.org/uniprot/Q6IBB5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC1DN12.|||In a colorectal cancer sample; somatic mutation.|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118817|||http://purl.uniprot.org/annotation/VAR_014485|||http://purl.uniprot.org/annotation/VAR_035099|||http://purl.uniprot.org/annotation/VAR_035100|||http://purl.uniprot.org/annotation/VAR_036173
http://togogenome.org/gene/9606:MAP3K13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43283                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic|||Basic and acidic residues|||Disordered|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kinase inactive. Fails to activate NF-kappa-B.|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 13|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086264|||http://purl.uniprot.org/annotation/VAR_030577|||http://purl.uniprot.org/annotation/VAR_040708|||http://purl.uniprot.org/annotation/VAR_040709|||http://purl.uniprot.org/annotation/VAR_040710|||http://purl.uniprot.org/annotation/VAR_051640|||http://purl.uniprot.org/annotation/VSP_036562|||http://purl.uniprot.org/annotation/VSP_036563|||http://purl.uniprot.org/annotation/VSP_036564|||http://purl.uniprot.org/annotation/VSP_036565|||http://purl.uniprot.org/annotation/VSP_036566|||http://purl.uniprot.org/annotation/VSP_036567|||http://purl.uniprot.org/annotation/VSP_036568|||http://purl.uniprot.org/annotation/VSP_036569
http://togogenome.org/gene/9606:GNB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14775                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Guanine nucleotide-binding protein subunit beta-5|||In LADCI; severe, but incomplete loss of activation of RGS9 GTPase activator activity, affecting the deactivation of D(2) dopamine receptor-mediated signaling; decreased stability; decreased RGS9 stabilization.|||In isoform 2 and isoform 3.|||In isoform 3.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127705|||http://purl.uniprot.org/annotation/VAR_049270|||http://purl.uniprot.org/annotation/VAR_077994|||http://purl.uniprot.org/annotation/VSP_008765|||http://purl.uniprot.org/annotation/VSP_039101
http://togogenome.org/gene/9606:RALYL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT61|||http://purl.uniprot.org/uniprot/Q86SE5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||RNA-binding Raly-like protein|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299525|||http://purl.uniprot.org/annotation/VSP_027725|||http://purl.uniprot.org/annotation/VSP_027726|||http://purl.uniprot.org/annotation/VSP_054067
http://togogenome.org/gene/9606:RSC1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92681                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Involved in post-transcriptional down-regulation of SLC5A1|||Polar residues|||Regulatory solute carrier protein family 1 member 1|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324150|||http://purl.uniprot.org/annotation/VAR_039679|||http://purl.uniprot.org/annotation/VAR_039680|||http://purl.uniprot.org/annotation/VAR_039681
http://togogenome.org/gene/9606:BARHL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  BarH-like 2 homeobox protein|||Basic and acidic residues|||Disordered|||Homeobox|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048829
http://togogenome.org/gene/9606:MYMX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AxLyCxL|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CFZS2; skeletal muscle cells derived from the patient show abnormal myoblast fusion involved in skeletal muscle regeneration.|||Protein myomixer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5010077027|||http://purl.uniprot.org/annotation/VAR_087573
http://togogenome.org/gene/9606:SATL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VE3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetyltransferase|||Polar residues|||Spermidine/spermine N(1)-acetyltransferase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282928|||http://purl.uniprot.org/annotation/VAR_031438|||http://purl.uniprot.org/annotation/VSP_024253|||http://purl.uniprot.org/annotation/VSP_024254
http://togogenome.org/gene/9606:GJC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IBV7|||http://purl.uniprot.org/uniprot/Q5T442                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Associated with lymphedema in a small family.|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction gamma-2 protein|||Gap junction protein cysteine-rich|||Helical|||In HLD2.|||In LMPHM3.|||In SPG44; does not form functional homotypic channels.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057842|||http://purl.uniprot.org/annotation/VAR_023754|||http://purl.uniprot.org/annotation/VAR_023755|||http://purl.uniprot.org/annotation/VAR_023756|||http://purl.uniprot.org/annotation/VAR_063172|||http://purl.uniprot.org/annotation/VAR_063876|||http://purl.uniprot.org/annotation/VAR_063877|||http://purl.uniprot.org/annotation/VAR_063878|||http://purl.uniprot.org/annotation/VAR_063879|||http://purl.uniprot.org/annotation/VAR_063880|||http://purl.uniprot.org/annotation/VAR_063881
http://togogenome.org/gene/9606:FANCD2OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PS1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  FANCD2 opposite strand protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235343
http://togogenome.org/gene/9606:NADK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95544|||http://purl.uniprot.org/uniprot/Q6PJ22                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||NAD kinase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120713|||http://purl.uniprot.org/annotation/VAR_034119|||http://purl.uniprot.org/annotation/VSP_047312|||http://purl.uniprot.org/annotation/VSP_047313|||http://purl.uniprot.org/annotation/VSP_047314
http://togogenome.org/gene/9606:AWAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58HT5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Acyl-CoA wax alcohol acyltransferase 1|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249051
http://togogenome.org/gene/9606:HEPACAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CZ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hepatic and glial cell adhesion molecule|||Ig-like C2-type|||Ig-like V-type|||In MLC2A.|||In MLC2B.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298777|||http://purl.uniprot.org/annotation/VAR_034731|||http://purl.uniprot.org/annotation/VAR_065849|||http://purl.uniprot.org/annotation/VAR_065850|||http://purl.uniprot.org/annotation/VAR_065851|||http://purl.uniprot.org/annotation/VAR_065852|||http://purl.uniprot.org/annotation/VAR_065853|||http://purl.uniprot.org/annotation/VAR_065854|||http://purl.uniprot.org/annotation/VAR_065855|||http://purl.uniprot.org/annotation/VAR_065856|||http://purl.uniprot.org/annotation/VAR_065857|||http://purl.uniprot.org/annotation/VAR_065858|||http://purl.uniprot.org/annotation/VAR_065859|||http://purl.uniprot.org/annotation/VAR_065860|||http://purl.uniprot.org/annotation/VSP_052497|||http://purl.uniprot.org/annotation/VSP_052498
http://togogenome.org/gene/9606:AARD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LEZ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Alanine and arginine-rich domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337036|||http://purl.uniprot.org/annotation/VAR_043570
http://togogenome.org/gene/9606:DPEP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK16|||http://purl.uniprot.org/uniprot/Q9H4B8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Dipeptidase 3|||Disordered|||GPI-anchor amidated serine|||Interchain|||Loss of zinc binding.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231609|||http://purl.uniprot.org/annotation/PRO_0000231610
http://togogenome.org/gene/9606:P2RY11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G91                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070035|||http://purl.uniprot.org/annotation/VAR_020074
http://togogenome.org/gene/9606:FMO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49326                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Dimethylated arginine|||Flavin-containing monooxygenase 5|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147665|||http://purl.uniprot.org/annotation/VAR_015370|||http://purl.uniprot.org/annotation/VAR_022308|||http://purl.uniprot.org/annotation/VAR_022309|||http://purl.uniprot.org/annotation/VSP_042729|||http://purl.uniprot.org/annotation/VSP_042730|||http://purl.uniprot.org/annotation/VSP_045616|||http://purl.uniprot.org/annotation/VSP_045617
http://togogenome.org/gene/9606:POPDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBV1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In LGMDR26; causes aberrant modulation of the mechano-gated potassium channel KCNK2, when tested in a heterologous system.|||In LGMDR26; decreased protein expression in muscle; causes a slightly abnormal modulation of the mechano-gated potassium channel KCNK2, when tested in a heterologous system.|||N-linked (GlcNAc...) asparagine|||Popeye domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046795|||http://purl.uniprot.org/annotation/VAR_053602|||http://purl.uniprot.org/annotation/VAR_084034|||http://purl.uniprot.org/annotation/VAR_084035|||http://purl.uniprot.org/annotation/VAR_084036
http://togogenome.org/gene/9606:PLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14939                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Catalytic|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform PLD2B.|||In isoform PLD2C.|||PH|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||PX|||Phospholipase D2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218805|||http://purl.uniprot.org/annotation/VAR_036503|||http://purl.uniprot.org/annotation/VAR_051704|||http://purl.uniprot.org/annotation/VAR_051705|||http://purl.uniprot.org/annotation/VAR_051706|||http://purl.uniprot.org/annotation/VAR_051707|||http://purl.uniprot.org/annotation/VAR_059774|||http://purl.uniprot.org/annotation/VAR_061750|||http://purl.uniprot.org/annotation/VSP_005027|||http://purl.uniprot.org/annotation/VSP_054769
http://togogenome.org/gene/9606:GSC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56915                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein goosecoid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048885
http://togogenome.org/gene/9606:MFSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3U5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Dileucine internalization motif|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Major facilitator superfamily domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273382|||http://purl.uniprot.org/annotation/VAR_030138|||http://purl.uniprot.org/annotation/VAR_030139|||http://purl.uniprot.org/annotation/VAR_030140|||http://purl.uniprot.org/annotation/VAR_059466|||http://purl.uniprot.org/annotation/VSP_022537|||http://purl.uniprot.org/annotation/VSP_022538|||http://purl.uniprot.org/annotation/VSP_037578|||http://purl.uniprot.org/annotation/VSP_037579|||http://purl.uniprot.org/annotation/VSP_047667|||http://purl.uniprot.org/annotation/VSP_047668
http://togogenome.org/gene/9606:GNL3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DU1|||http://purl.uniprot.org/uniprot/Q9NVN8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||CP-type G|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Guanine nucleotide-binding protein-like 3-like protein|||Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization.|||Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35.|||Loss of nucleolar localization. No effect on nuclear localization.|||Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20.|||Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20.|||Required for nucleolar localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284381|||http://purl.uniprot.org/annotation/VAR_049495
http://togogenome.org/gene/9606:SLC8B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6J4K2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolished ability to prevent calcium overload.|||Cytoplasmic|||Extracellular|||Has no effect on calcium:sodium antiporter activity.|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Lithium-selective; displays markedly reduced calcium:sodium antiporter activity while retaining almost normal calcium:lithium antiporter activity.|||Lithium-selective; displays markedly reduced calcium:sodium antiporter activity while retaining normal calcium:lithium antiporter activity.|||Lithium-selective; displays reduced calcium:sodium antiporter activity while retaining almost normal calcium:lithium antiporter activity.|||Mitochondrial sodium/calcium exchanger protein|||Mitochondrion|||N-linked (GlcNAc...) asparagine|||Non-selective; displays reduction of both calcium:sodium and calcium:lithium antiporter activities.|||Non-selective; displays similar reduction of calcium:sodium and calcium:lithium antiporter activities.|||Phosphomimetic mutant; prevents calcium overload.|||Phosphoserine; by PKA|||Sodium-selective; has little effect on calcium:sodium antiporter activity while displaying markedly reduced calcium:lithium antiporter activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045756|||http://purl.uniprot.org/annotation/VAR_050224|||http://purl.uniprot.org/annotation/VAR_050225|||http://purl.uniprot.org/annotation/VSP_016996
http://togogenome.org/gene/9606:POLE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56282                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA polymerase epsilon subunit 2|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071562|||http://purl.uniprot.org/annotation/VAR_044379|||http://purl.uniprot.org/annotation/VAR_044380|||http://purl.uniprot.org/annotation/VAR_044381|||http://purl.uniprot.org/annotation/VSP_042551|||http://purl.uniprot.org/annotation/VSP_043796
http://togogenome.org/gene/9606:TMEM79                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSE2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||May be associated with atopic dermatitis.|||Transmembrane protein 79                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254118|||http://purl.uniprot.org/annotation/VAR_028815
http://togogenome.org/gene/9606:PTPRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28827                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like C2-type|||In isoform 2.|||MAM|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase mu|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025448|||http://purl.uniprot.org/annotation/VAR_046634|||http://purl.uniprot.org/annotation/VSP_046677
http://togogenome.org/gene/9606:NETO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDF5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 1 and isoform 2.|||In isoform 1.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Neuropilin and tolloid-like protein 1|||PDZ-binding|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021799|||http://purl.uniprot.org/annotation/VAR_051230|||http://purl.uniprot.org/annotation/VAR_051231|||http://purl.uniprot.org/annotation/VSP_012853|||http://purl.uniprot.org/annotation/VSP_012854|||http://purl.uniprot.org/annotation/VSP_012855
http://togogenome.org/gene/9606:TXNL4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX01                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Thioredoxin-like protein 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218289
http://togogenome.org/gene/9606:ESYT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0FGR8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes calcium binding; when associated with A-401.|||Abolishes calcium binding; when associated with A-413.|||Abolishes location at the cell membrane.|||Basic and acidic residues|||Basic residues|||C2 1|||C2 2|||C2 3|||Cytoplasmic|||Disordered|||Extended synaptotagmin-2|||Helical|||Impairs binding of the third calcium ion, but has no effect on the binding of the other two calcium ions.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD|||Strongly reduces calcium binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278258|||http://purl.uniprot.org/annotation/VAR_030725|||http://purl.uniprot.org/annotation/VAR_030726|||http://purl.uniprot.org/annotation/VSP_023236|||http://purl.uniprot.org/annotation/VSP_023238|||http://purl.uniprot.org/annotation/VSP_023239|||http://purl.uniprot.org/annotation/VSP_023240|||http://purl.uniprot.org/annotation/VSP_023241|||http://purl.uniprot.org/annotation/VSP_023242|||http://purl.uniprot.org/annotation/VSP_038324
http://togogenome.org/gene/9606:ZNF888                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CJ79                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 888                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000404597
http://togogenome.org/gene/9606:CCDC82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7C3|||http://purl.uniprot.org/uniprot/Q8N4S0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil|||Coiled-coil domain-containing protein 82|||DUF4211|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234288|||http://purl.uniprot.org/annotation/VAR_026164|||http://purl.uniprot.org/annotation/VAR_026165|||http://purl.uniprot.org/annotation/VAR_050764|||http://purl.uniprot.org/annotation/VSP_035403|||http://purl.uniprot.org/annotation/VSP_035404
http://togogenome.org/gene/9606:THNSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YJ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform SOFAT.|||N6-(pyridoxal phosphate)lysine|||Threonine synthase-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306407|||http://purl.uniprot.org/annotation/VAR_054635|||http://purl.uniprot.org/annotation/VAR_054636|||http://purl.uniprot.org/annotation/VAR_054637|||http://purl.uniprot.org/annotation/VAR_054638|||http://purl.uniprot.org/annotation/VSP_028468|||http://purl.uniprot.org/annotation/VSP_028469|||http://purl.uniprot.org/annotation/VSP_028470|||http://purl.uniprot.org/annotation/VSP_041659|||http://purl.uniprot.org/annotation/VSP_041660
http://togogenome.org/gene/9606:NFKBIE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00221|||http://purl.uniprot.org/uniprot/Q7LC14|||http://purl.uniprot.org/uniprot/Q96F31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||NF-kappa-B inhibitor epsilon|||No degradation.|||No effect.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067007|||http://purl.uniprot.org/annotation/VAR_046631|||http://purl.uniprot.org/annotation/VAR_046632
http://togogenome.org/gene/9606:DRICH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PGQ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Aspartate-rich protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319592|||http://purl.uniprot.org/annotation/VAR_039014
http://togogenome.org/gene/9606:ILDR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin-like domain-containing receptor 1|||In DFNB42; loss of interaction with MARVELD2; loss of tight junction location.|||In DFNB42; no effect on interaction with MARVELD2; loss of tight junction location.|||In DFNB42; uncertain pathological significance; no effect on interaction with MARVELD2; no effect on tight junction location.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245304|||http://purl.uniprot.org/annotation/VAR_065352|||http://purl.uniprot.org/annotation/VAR_065353|||http://purl.uniprot.org/annotation/VAR_065354|||http://purl.uniprot.org/annotation/VAR_079750|||http://purl.uniprot.org/annotation/VAR_085556|||http://purl.uniprot.org/annotation/VAR_085557|||http://purl.uniprot.org/annotation/VSP_019679|||http://purl.uniprot.org/annotation/VSP_019680|||http://purl.uniprot.org/annotation/VSP_019681|||http://purl.uniprot.org/annotation/VSP_019682|||http://purl.uniprot.org/annotation/VSP_019683|||http://purl.uniprot.org/annotation/VSP_019684|||http://purl.uniprot.org/annotation/VSP_019685|||http://purl.uniprot.org/annotation/VSP_019686|||http://purl.uniprot.org/annotation/VSP_019687
http://togogenome.org/gene/9606:ISOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CN7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  Isochorismatase domain-containing protein 1|||N6-succinyllysine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268664
http://togogenome.org/gene/9606:ZFYVE21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ24                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Diffuse cytoplasmic localization.|||FYVE-type|||In isoform 2.|||PH-like|||Zinc finger FYVE domain-containing protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098720|||http://purl.uniprot.org/annotation/VSP_013794
http://togogenome.org/gene/9606:HSPE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61604                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Strand                                                                                  ^@                                                                                  10 kDa heat shock protein, mitochondrial|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174917
http://togogenome.org/gene/9606:LRR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AWA7|||http://purl.uniprot.org/uniprot/Q96L50                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CUL2 and RBX1.|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084447|||http://purl.uniprot.org/annotation/VAR_051095|||http://purl.uniprot.org/annotation/VAR_051096|||http://purl.uniprot.org/annotation/VSP_008363|||http://purl.uniprot.org/annotation/VSP_008364
http://togogenome.org/gene/9606:PHKA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46019                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||In GSD9A.|||In GSD9A; type 1 and type 2.|||In GSD9A; type 1.|||In GSD9A; type 2.|||Phosphorylase b kinase regulatory subunit alpha, liver isoform|||Phosphoserine|||Polar residues|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057730|||http://purl.uniprot.org/annotation/VAR_006177|||http://purl.uniprot.org/annotation/VAR_006178|||http://purl.uniprot.org/annotation/VAR_006179|||http://purl.uniprot.org/annotation/VAR_006180|||http://purl.uniprot.org/annotation/VAR_006181|||http://purl.uniprot.org/annotation/VAR_006182|||http://purl.uniprot.org/annotation/VAR_006183|||http://purl.uniprot.org/annotation/VAR_006184|||http://purl.uniprot.org/annotation/VAR_006185|||http://purl.uniprot.org/annotation/VAR_006186|||http://purl.uniprot.org/annotation/VAR_012269|||http://purl.uniprot.org/annotation/VAR_012270|||http://purl.uniprot.org/annotation/VAR_012271|||http://purl.uniprot.org/annotation/VAR_012272|||http://purl.uniprot.org/annotation/VAR_012273|||http://purl.uniprot.org/annotation/VAR_012274|||http://purl.uniprot.org/annotation/VAR_012275|||http://purl.uniprot.org/annotation/VAR_012276|||http://purl.uniprot.org/annotation/VAR_012277|||http://purl.uniprot.org/annotation/VAR_024563|||http://purl.uniprot.org/annotation/VAR_050518|||http://purl.uniprot.org/annotation/VAR_062393|||http://purl.uniprot.org/annotation/VAR_062394|||http://purl.uniprot.org/annotation/VAR_062395|||http://purl.uniprot.org/annotation/VAR_062396|||http://purl.uniprot.org/annotation/VAR_062397|||http://purl.uniprot.org/annotation/VAR_062398
http://togogenome.org/gene/9606:ADPRHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HI13|||http://purl.uniprot.org/uniprot/Q8NDY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Inactive ADP-ribosyltransferase ARH2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277606|||http://purl.uniprot.org/annotation/VAR_048890|||http://purl.uniprot.org/annotation/VSP_023036
http://togogenome.org/gene/9606:LAPTM4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VI4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to NEDD4; when associated with A-296. Increases localization to cell membrane; when associated with A-296. Retains association with HGS and enhances PIP5K1C interaction; when associated with A-296. Does not affect EGFR degradation; when associated with A-296.|||Abolishes binding to NEDD4; when associated with A-312. Increases localization to cell membrane; when associated with A-312. Retains association with HGS and enhances PIP5K1C interaction; when associated with A-312. Does not affect EGFR degradation; when associated with A-312.|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Lysosomal-associated transmembrane protein 4B|||Required for NEDD4 interaction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249721|||http://purl.uniprot.org/annotation/VSP_059831
http://togogenome.org/gene/9606:OR5AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGF4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150578|||http://purl.uniprot.org/annotation/VAR_053180
http://togogenome.org/gene/9606:LDHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHM4|||http://purl.uniprot.org/uniprot/P07195|||http://purl.uniprot.org/uniprot/Q5U077                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with MP31.|||In LDHBD.|||In LDHBD; inactive.|||In LDHBD; slightly decreased activity.|||L-lactate dehydrogenase B chain|||Lactate/malate dehydrogenase C-terminal|||Lactate/malate dehydrogenase N-terminal|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168459|||http://purl.uniprot.org/annotation/VAR_004173|||http://purl.uniprot.org/annotation/VAR_004174|||http://purl.uniprot.org/annotation/VAR_004175|||http://purl.uniprot.org/annotation/VAR_004176|||http://purl.uniprot.org/annotation/VAR_004177|||http://purl.uniprot.org/annotation/VAR_004178|||http://purl.uniprot.org/annotation/VAR_004179|||http://purl.uniprot.org/annotation/VAR_011634|||http://purl.uniprot.org/annotation/VAR_011635|||http://purl.uniprot.org/annotation/VAR_011636|||http://purl.uniprot.org/annotation/VAR_011637|||http://purl.uniprot.org/annotation/VAR_011638|||http://purl.uniprot.org/annotation/VAR_049758
http://togogenome.org/gene/9606:SOX12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15370                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HMG box|||Required for transcriptional activation activity and synergistic coactivation of transcriptional activity with POU3F2|||Transcription factor SOX-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048754
http://togogenome.org/gene/9606:PCDH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSR3|||http://purl.uniprot.org/uniprot/Q9P2E7|||http://purl.uniprot.org/uniprot/X5D999                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin cytoplasmic C-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003995|||http://purl.uniprot.org/annotation/PRO_5004955355|||http://purl.uniprot.org/annotation/VSP_054404|||http://purl.uniprot.org/annotation/VSP_054405
http://togogenome.org/gene/9606:CNTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N815                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin N-terminal domain-containing protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313715|||http://purl.uniprot.org/annotation/VAR_037708|||http://purl.uniprot.org/annotation/VSP_030111
http://togogenome.org/gene/9606:TRIM49C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CI26                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 49C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000399992
http://togogenome.org/gene/9606:XAGE1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD64                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform D.|||Phosphoserine|||X antigen family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148349|||http://purl.uniprot.org/annotation/VSP_001596
http://togogenome.org/gene/9606:SERPINF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08697                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Alpha-2-antiplasmin|||Cleavage; by prolyl endopeptidase FAP, antiplasmin-cleaving enzyme FAP soluble form|||Disordered|||In APLID.|||In APLID; variant Okinawa; probably blocks intracellular transport of alpha-2-plasmin inhibitor.|||In isoform 2.|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-322 in alpha-fibrinogen)|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reactive bond for chymotrypsin|||Reactive bond for plasmin|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032511|||http://purl.uniprot.org/annotation/PRO_0000032512|||http://purl.uniprot.org/annotation/VAR_013252|||http://purl.uniprot.org/annotation/VAR_013253|||http://purl.uniprot.org/annotation/VAR_013254|||http://purl.uniprot.org/annotation/VAR_013255|||http://purl.uniprot.org/annotation/VAR_013256|||http://purl.uniprot.org/annotation/VAR_047951|||http://purl.uniprot.org/annotation/VAR_051956|||http://purl.uniprot.org/annotation/VAR_061792|||http://purl.uniprot.org/annotation/VSP_043833|||http://purl.uniprot.org/annotation/VSP_043834
http://togogenome.org/gene/9606:ALDH3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51648                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase family 3 member A2|||Cytoplasmic|||Decreased enzyme activity with dodecanal and hexadecanal. No effect on enzyme activity with octanal.|||Decreased enzyme activity with dodecanal. Strongly decreased enzyme activity with hexadecanal. No effect on enzyme activity with octanal.|||Helical|||In SLS.|||In SLS; 4% of activity.|||In SLS; 8% of activity.|||In SLS; common mutation in Europeans; severe loss of enzymatic activity.|||In SLS; mild reduction of activity; the underlying nucleotide substitution affects transcript stability.|||In SLS; severe loss of activity.|||In isoform 2.|||Loss of enzyme activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056473|||http://purl.uniprot.org/annotation/VAR_002249|||http://purl.uniprot.org/annotation/VAR_002250|||http://purl.uniprot.org/annotation/VAR_002251|||http://purl.uniprot.org/annotation/VAR_002252|||http://purl.uniprot.org/annotation/VAR_002253|||http://purl.uniprot.org/annotation/VAR_002254|||http://purl.uniprot.org/annotation/VAR_002255|||http://purl.uniprot.org/annotation/VAR_002256|||http://purl.uniprot.org/annotation/VAR_017510|||http://purl.uniprot.org/annotation/VAR_017511|||http://purl.uniprot.org/annotation/VAR_017512|||http://purl.uniprot.org/annotation/VAR_017513|||http://purl.uniprot.org/annotation/VAR_017514|||http://purl.uniprot.org/annotation/VAR_017515|||http://purl.uniprot.org/annotation/VAR_017516|||http://purl.uniprot.org/annotation/VAR_017517|||http://purl.uniprot.org/annotation/VAR_017518|||http://purl.uniprot.org/annotation/VAR_017519|||http://purl.uniprot.org/annotation/VAR_017520|||http://purl.uniprot.org/annotation/VAR_017521|||http://purl.uniprot.org/annotation/VAR_017522|||http://purl.uniprot.org/annotation/VAR_017523|||http://purl.uniprot.org/annotation/VAR_017524|||http://purl.uniprot.org/annotation/VAR_017525|||http://purl.uniprot.org/annotation/VAR_017526|||http://purl.uniprot.org/annotation/VAR_017527|||http://purl.uniprot.org/annotation/VAR_017528|||http://purl.uniprot.org/annotation/VSP_001283
http://togogenome.org/gene/9606:ATP2B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J5M1|||http://purl.uniprot.org/uniprot/Q16720                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Calmodulin-binding subdomain A|||Calmodulin-binding subdomain B|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impaired ATPase activity.|||In SCAX1; the mutant protein is expressed at the plasma membrane but shows impaired extrusion of intracellular calcium with prolonged retention of cytoplasmic calcium compared to wild-type under physiologic conditions.|||In SCAX1; the mutant protein is expressed at the plasma membrane, but shows impaired extrusion of intracellular calcium.|||In an aldosterone-producing adenoma sample; somatic mutation; increases intracellular calcium concentration that leads to autonomous aldosterone secretion.|||In isoform XA and isoform ZA.|||In isoform XE and isoform ZE.|||In isoform XG and isoform ZG.|||In isoform ZA, isoform ZB, isoform ZE and isoform ZG.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046218|||http://purl.uniprot.org/annotation/VAR_027928|||http://purl.uniprot.org/annotation/VAR_069308|||http://purl.uniprot.org/annotation/VAR_084697|||http://purl.uniprot.org/annotation/VAR_084698|||http://purl.uniprot.org/annotation/VSP_000392|||http://purl.uniprot.org/annotation/VSP_000393|||http://purl.uniprot.org/annotation/VSP_000394|||http://purl.uniprot.org/annotation/VSP_000395
http://togogenome.org/gene/9606:FOXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55317                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fork-head|||Hepatocyte nuclear factor 3-alpha|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091792|||http://purl.uniprot.org/annotation/VAR_013457|||http://purl.uniprot.org/annotation/VAR_013458|||http://purl.uniprot.org/annotation/VAR_015183|||http://purl.uniprot.org/annotation/VAR_015184|||http://purl.uniprot.org/annotation/VAR_015185|||http://purl.uniprot.org/annotation/VAR_055835|||http://purl.uniprot.org/annotation/VSP_055094
http://togogenome.org/gene/9606:OST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C6T2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases interaction with STT3A, STT3B and RPN1.|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4|||Helical|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328638
http://togogenome.org/gene/9606:HSP90B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14625|||http://purl.uniprot.org/uniprot/V9HWP2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Endoplasmin|||Histidine kinase/HSP90-like ATPase|||Important for ATP hydrolysis|||Interchain|||N-linked (GlcNAc...) asparagine|||N6-(2-hydroxyisobutyryl)lysine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013598|||http://purl.uniprot.org/annotation/PRO_5014314735
http://togogenome.org/gene/9606:PPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2U2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In SCFAI; decreased inorganic diphosphatase activity.|||In SCFI and SCFAI; loss of function in regulation of mitochondrial membrane potential; decreased inorganic diphosphatase activity.|||In SCFI.|||In SCFI; decreased inorganic diphosphatase activity.|||In SCFI; loss of function in regulation of mitochondrial membrane potential.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inorganic pyrophosphatase 2, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025411|||http://purl.uniprot.org/annotation/VAR_019723|||http://purl.uniprot.org/annotation/VAR_077866|||http://purl.uniprot.org/annotation/VAR_077867|||http://purl.uniprot.org/annotation/VAR_077868|||http://purl.uniprot.org/annotation/VAR_077869|||http://purl.uniprot.org/annotation/VAR_077870|||http://purl.uniprot.org/annotation/VAR_077871|||http://purl.uniprot.org/annotation/VAR_077872|||http://purl.uniprot.org/annotation/VAR_077873|||http://purl.uniprot.org/annotation/VSP_011649|||http://purl.uniprot.org/annotation/VSP_011650|||http://purl.uniprot.org/annotation/VSP_011651|||http://purl.uniprot.org/annotation/VSP_011652|||http://purl.uniprot.org/annotation/VSP_046256
http://togogenome.org/gene/9606:GSDME                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FVA8|||http://purl.uniprot.org/uniprot/O60443                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage by CASP3 or granzyme B. Abolishes pyroptosis induction.|||Abolishes cleavage by CASP3. Abolishes pyroptosis induction.|||Cleavage; by CASP3 or granzyme B|||Disrupts plasma membrane targeting and induction of necrotic activity; when associated with A-39 and/or A-41.|||Disrupts plasma membrane targeting and induction of necrotic activity; when associated with A-40 and/or A-41.|||Gasdermin PUB|||Gasdermin pore forming|||Gasdermin-E|||Gasdermin-E, C-terminal|||Gasdermin-E, N-terminal|||In a breast carcinoma sample; somatic mutation; reduced ability to induce pyroptosis.|||In a colon adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis.|||In a lung cancer adenocarcinoma sample; somatic mutation; reduced ability to induce pyroptosis.|||In a melanoma sample; somatic mutation; reduced ability to induce pyroptosis.|||In an uterine corpus endometrioid carcinoma sample; somatic mutation; reduced ability to induce pyroptosis.|||In isoform 2.|||In isoform 3.|||Low spontaneous pyroptosis-inducing activity.|||Membrane targeting domain|||No effect on plasma membrane targeting. Decreases induction of necrotic activity. Disrupts plasma membrane targeting and induction of necrotic activity; when associated with A-40.|||No effect on plasma membrane targeting. No effect on induction of cytotoxivity. Disrupts plasma membrane targeting and induction of necrotic activity; when associated with A-2 or A-39 and A-41.|||No spontaneous pyroptosis-inducing activity.|||S-(2-succinyl)cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148178|||http://purl.uniprot.org/annotation/PRO_0000442786|||http://purl.uniprot.org/annotation/PRO_0000442787|||http://purl.uniprot.org/annotation/VAR_030824|||http://purl.uniprot.org/annotation/VAR_030825|||http://purl.uniprot.org/annotation/VAR_053102|||http://purl.uniprot.org/annotation/VAR_083903|||http://purl.uniprot.org/annotation/VAR_083904|||http://purl.uniprot.org/annotation/VAR_083905|||http://purl.uniprot.org/annotation/VAR_083906|||http://purl.uniprot.org/annotation/VAR_083907|||http://purl.uniprot.org/annotation/VAR_083908|||http://purl.uniprot.org/annotation/VAR_083909|||http://purl.uniprot.org/annotation/VAR_083910|||http://purl.uniprot.org/annotation/VAR_083911|||http://purl.uniprot.org/annotation/VSP_004190|||http://purl.uniprot.org/annotation/VSP_044276
http://togogenome.org/gene/9606:RGS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2A0|||http://purl.uniprot.org/uniprot/B7Z2N1|||http://purl.uniprot.org/uniprot/P49758|||http://purl.uniprot.org/uniprot/Q2M3K2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  DEP|||Diminishes interaction with GNB5.|||G protein gamma|||In isoform 12.|||In isoform 13.|||In isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 2, isoform 10 and isoform 12.|||In isoform 3 and isoform 9.|||In isoform 5 and isoform 6.|||In isoform 6, isoform 7, isoform 9, isoform 10 and isoform 11.|||In isoform 8 and isoform 11.|||Loss of interaction with GNB5.|||RGS|||Regulator of G-protein signaling 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204192|||http://purl.uniprot.org/annotation/VSP_035845|||http://purl.uniprot.org/annotation/VSP_035846|||http://purl.uniprot.org/annotation/VSP_035847|||http://purl.uniprot.org/annotation/VSP_035848|||http://purl.uniprot.org/annotation/VSP_035849|||http://purl.uniprot.org/annotation/VSP_035850|||http://purl.uniprot.org/annotation/VSP_047806|||http://purl.uniprot.org/annotation/VSP_047807|||http://purl.uniprot.org/annotation/VSP_047808|||http://purl.uniprot.org/annotation/VSP_047809
http://togogenome.org/gene/9606:SPATA17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L03                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  IQ 1|||IQ 2|||IQ 3|||Spermatogenesis-associated protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265933|||http://purl.uniprot.org/annotation/VAR_051382
http://togogenome.org/gene/9606:CLPTM1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KA5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Lipid scramblase CLPTM1L|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331300|||http://purl.uniprot.org/annotation/VAR_042754|||http://purl.uniprot.org/annotation/VAR_042755|||http://purl.uniprot.org/annotation/VSP_033157
http://togogenome.org/gene/9606:SHC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S5L8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CH1|||CH2|||Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-424 and F-465.|||Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-413; F-424 and F-465.|||Completely reduces the phosphorylation and interaction with MUSK; when associated with Q-315.|||Disordered|||In isoform 2.|||PID|||Phosphorylation is markedly decreased. Completely reduces the phosphorylation and interaction with MUSK; when associated with K-549.|||Phosphotyrosine|||Polar residues|||Remains phosphorylated. Contains a residual phosphorylation; when associated with 374-F-F-375. Reduced the phosphorylation in presence of MUSK; when associated with 374-F-F-375 and 424. Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-413 and F-424. Retains the ability to bind MUSK. Retains the ability to bind MUSK; when associated with 374-F-F-375. Retains the ability to bind MUSK; when associated with 374-F-F-375 and F-424. Retains the ability to bind MUSK; when associated with 374-F-F-375; F-403; F-413 and F-424.|||Remains phosphorylated. Contains a residual phosphorylation; when associated with F-465. Retains the ability to bind MUSK. Reduced the phosphorylation in presence of MUSK; when associated with F-424 and F-465. Completely abolishes the phosphorylation in presence of MUSK; when associated with F-403; F-413; F-424 and F-465. Retains the ability to bind MUSK; when associated with F-465. Retains the ability to bind MUSK; when associated with F-424 and F-465. Retains the ability to bind MUSK; when associated with F-403; F-413; F-424 and F-465.|||SH2|||SHC-transforming protein 4|||Significantly decreased GRB2 interaction. Reduced the phosphorylation in presence of MUSK; when associated with 374-F-F-375 and F-465. Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-413 and F-465.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337200|||http://purl.uniprot.org/annotation/VAR_043672|||http://purl.uniprot.org/annotation/VAR_043673|||http://purl.uniprot.org/annotation/VAR_043674|||http://purl.uniprot.org/annotation/VAR_043675|||http://purl.uniprot.org/annotation/VSP_033965|||http://purl.uniprot.org/annotation/VSP_033966
http://togogenome.org/gene/9606:WBP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2W2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In VCTRL.|||In VCTRL; unknown pathological significance.|||Interaction with PP1|||Loss of PQBP1-binding; when associated with A-192 and A-197.|||Loss of PQBP1-binding; when associated with A-192 and A-198.|||Loss of PQBP1-binding; when associated with A-197 and A-198.|||N6-acetyllysine|||Omega-N-methylarginine|||PGR|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Required for nuclear import|||WW domain-binding protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065945|||http://purl.uniprot.org/annotation/VAR_085325|||http://purl.uniprot.org/annotation/VAR_085326|||http://purl.uniprot.org/annotation/VAR_085327|||http://purl.uniprot.org/annotation/VAR_085328
http://togogenome.org/gene/9606:CRYAA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02489                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Alpha-crystallin A chain|||Alpha-crystallin A(1-162)|||Alpha-crystallin A(1-168)|||Alpha-crystallin A(1-172)|||Deamidated asparagine; partial|||Deamidated glutamine; partial|||Impairs chaperone activity.|||In CTRCT9.|||In CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus.|||In CTRCT9; decreases oligomer formation.|||In CTRCT9; delays HSP70 expression increase in response to heat shock.|||In CTRCT9; forms inclusion bodies, decreases chaperone activity, decreases protein stability at 45 degrees Celsius and increases protein aggregate formation in response to DTT in vitro.|||In CTRCT9; reduces protein solubility.|||In CTRCT9; results in protein aggregation in the cytoplasm.|||In CTRCT9; reverse phase-high-performance liquid chromatography suggests an increased hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme.|||In CTRCT9; unknown pathological significance.|||In CTRCT9; unknown pathological significance; reduced chaperone-like activity in vitro.|||In CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity.|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Required for complex formation with BFSP1 and BFSP2; during homooligomerization, mediates the association of 2 dimers to form a tetramer|||Susceptible to oxidation|||With 1 phosphate group.|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125865|||http://purl.uniprot.org/annotation/PRO_0000226639|||http://purl.uniprot.org/annotation/PRO_0000423503|||http://purl.uniprot.org/annotation/PRO_0000423504|||http://purl.uniprot.org/annotation/VAR_003819|||http://purl.uniprot.org/annotation/VAR_036564|||http://purl.uniprot.org/annotation/VAR_038375|||http://purl.uniprot.org/annotation/VAR_046892|||http://purl.uniprot.org/annotation/VAR_046893|||http://purl.uniprot.org/annotation/VAR_070032|||http://purl.uniprot.org/annotation/VAR_084768|||http://purl.uniprot.org/annotation/VAR_084769|||http://purl.uniprot.org/annotation/VAR_084770|||http://purl.uniprot.org/annotation/VAR_084771|||http://purl.uniprot.org/annotation/VAR_084772|||http://purl.uniprot.org/annotation/VAR_084773|||http://purl.uniprot.org/annotation/VAR_084774|||http://purl.uniprot.org/annotation/VAR_084775|||http://purl.uniprot.org/annotation/VAR_084776|||http://purl.uniprot.org/annotation/VAR_084777|||http://purl.uniprot.org/annotation/VAR_084778|||http://purl.uniprot.org/annotation/VAR_084779|||http://purl.uniprot.org/annotation/VAR_084780|||http://purl.uniprot.org/annotation/VAR_084781
http://togogenome.org/gene/9606:CAPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN77|||http://purl.uniprot.org/uniprot/P17655|||http://purl.uniprot.org/uniprot/Q59EF6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anchors to the small subunit|||Calpain catalytic|||Calpain-2 catalytic subunit|||Disordered|||Domain III|||Domain IV|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||Linker|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026487|||http://purl.uniprot.org/annotation/PRO_0000026488|||http://purl.uniprot.org/annotation/VAR_014435|||http://purl.uniprot.org/annotation/VAR_014436|||http://purl.uniprot.org/annotation/VAR_021404|||http://purl.uniprot.org/annotation/VAR_021405|||http://purl.uniprot.org/annotation/VAR_021406|||http://purl.uniprot.org/annotation/VAR_021407|||http://purl.uniprot.org/annotation/VSP_043027|||http://purl.uniprot.org/annotation/VSP_043028
http://togogenome.org/gene/9606:C14orf39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1H7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In SPGF52; does not affect protein expression; impairs polycomplex formation between SIX6OS1 and SYCE1.|||Phosphoserine|||Protein SIX6OS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089888|||http://purl.uniprot.org/annotation/VAR_056983|||http://purl.uniprot.org/annotation/VAR_056984|||http://purl.uniprot.org/annotation/VAR_059715|||http://purl.uniprot.org/annotation/VAR_085225
http://togogenome.org/gene/9606:CDK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z537|||http://purl.uniprot.org/uniprot/Q15131                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 10|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085809|||http://purl.uniprot.org/annotation/VAR_041983|||http://purl.uniprot.org/annotation/VAR_041984|||http://purl.uniprot.org/annotation/VAR_041985|||http://purl.uniprot.org/annotation/VAR_041986|||http://purl.uniprot.org/annotation/VSP_021642|||http://purl.uniprot.org/annotation/VSP_021643|||http://purl.uniprot.org/annotation/VSP_021644|||http://purl.uniprot.org/annotation/VSP_054969|||http://purl.uniprot.org/annotation/VSP_054970|||http://purl.uniprot.org/annotation/VSP_054971|||http://purl.uniprot.org/annotation/VSP_054972|||http://purl.uniprot.org/annotation/VSP_054973
http://togogenome.org/gene/9606:TMEM252                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6L7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 252                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089707
http://togogenome.org/gene/9606:MAGEE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCI5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Interaction with DTNA|||MAGE 1|||MAGE 2|||Melanoma-associated antigen E1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156729|||http://purl.uniprot.org/annotation/VAR_036585|||http://purl.uniprot.org/annotation/VAR_036586|||http://purl.uniprot.org/annotation/VAR_060071|||http://purl.uniprot.org/annotation/VAR_076263
http://togogenome.org/gene/9606:ACTRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDG2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-related protein T1|||Found in a patient with Bazex syndrome; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255656|||http://purl.uniprot.org/annotation/VAR_080907|||http://purl.uniprot.org/annotation/VAR_080908
http://togogenome.org/gene/9606:RTL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NET4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Retrotransposon Gag-like protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259627|||http://purl.uniprot.org/annotation/VAR_051318
http://togogenome.org/gene/9606:ANKDD1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHY2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and death domain-containing protein 1B|||Death                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332160
http://togogenome.org/gene/9606:MRPS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60783                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In COXPD38.|||Small ribosomal subunit protein uS14m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131013|||http://purl.uniprot.org/annotation/VAR_082116
http://togogenome.org/gene/9606:ZMYND8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVZ6|||http://purl.uniprot.org/uniprot/A6H8Y8|||http://purl.uniprot.org/uniprot/Q2HXV5|||http://purl.uniprot.org/uniprot/Q569J9|||http://purl.uniprot.org/uniprot/Q9ULU4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Decreases binding to DBN1.|||Decreases interaction with histone H3K4me0 and histone H4K16ac.|||Decreases interaction with histone H3K4me0.|||Decreases interaction with histone H4ac.|||Disordered|||Found in a patient with syndromic intellectual disability; probable disease-associated variant.|||Found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with DBN1.|||Found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with GATAD2A.|||Found in a patient with syndromic intellectual disability; probable disease-associated variant; does not affect interaction with DBN1.|||Found in a patient with syndromic intellectual disability; probable disease-associated variant; does not affect interaction with GATAD2A.|||Found in two patients with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with GATAD2A.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 15 and isoform 18.|||In isoform 19.|||In isoform 2, isoform 3, isoform 4, isoform 6, isoform 9, isoform 12, isoform 13, isoform 14, isoform 15, isoform 16, isoform 21, isoform 22 and isoform 23.|||In isoform 2.|||In isoform 20.|||In isoform 22.|||In isoform 23.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18, isoform 20, isoform 21 and isoform 23.|||In isoform 5, isoform 7, isoform 8, isoform 10, isoform 12, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 18 and isoform 22.|||In isoform 6, isoform 7, isoform 8, isoform 9, isoform 11, isoform 13, isoform 16, isoform 19, isoform 22 and isoform 23.|||In isoform 8 and isoform 17.|||Increases interaction with histone H3K4me0.|||Interaction with PRKCB1|||Interaction with histone H3K14ac|||Interaction with histone H3K4me0|||Loss of binding to DBN1.|||Loss of binding to DBN1. Loss of cytoplasmic localization.|||MYND-type|||MYND-type zinc finger-containing chromatin reader ZMYND8|||N6-acetyllysine; alternate|||PHD-type|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with syndromic intellectual disability; probable disease-associated variant; disrupts interaction with DBN1.|||Required for homodimerization|||Required for interaction with CCNT1|||Required for interaction with histone H3 and histone H4|||Required for recruitment to DNA damage sites and for interaction with the NuRD complex, CHD4, HDAC1, HDAC2 and KDM1A|||Severely decreases interaction with histone H3.1K36me2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211209|||http://purl.uniprot.org/annotation/VAR_055559|||http://purl.uniprot.org/annotation/VAR_087647|||http://purl.uniprot.org/annotation/VAR_087648|||http://purl.uniprot.org/annotation/VAR_087649|||http://purl.uniprot.org/annotation/VAR_087650|||http://purl.uniprot.org/annotation/VAR_087651|||http://purl.uniprot.org/annotation/VAR_087652|||http://purl.uniprot.org/annotation/VAR_087653|||http://purl.uniprot.org/annotation/VAR_087654|||http://purl.uniprot.org/annotation/VSP_000563|||http://purl.uniprot.org/annotation/VSP_000564|||http://purl.uniprot.org/annotation/VSP_000565|||http://purl.uniprot.org/annotation/VSP_000566|||http://purl.uniprot.org/annotation/VSP_000567|||http://purl.uniprot.org/annotation/VSP_000568|||http://purl.uniprot.org/annotation/VSP_000570|||http://purl.uniprot.org/annotation/VSP_017096|||http://purl.uniprot.org/annotation/VSP_053400|||http://purl.uniprot.org/annotation/VSP_054810|||http://purl.uniprot.org/annotation/VSP_054811|||http://purl.uniprot.org/annotation/VSP_054812|||http://purl.uniprot.org/annotation/VSP_054814
http://togogenome.org/gene/9606:C12orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VSD7|||http://purl.uniprot.org/uniprot/Q8NA57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C12orf50|||Zinc-finger CCCH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295234|||http://purl.uniprot.org/annotation/VAR_033266|||http://purl.uniprot.org/annotation/VAR_033267
http://togogenome.org/gene/9606:SSH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK64|||http://purl.uniprot.org/uniprot/F5H527|||http://purl.uniprot.org/uniprot/Q76I76                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abrogates phosphatase activity.|||Basic and acidic residues|||DEK-C|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase Slingshot homolog 2|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094843|||http://purl.uniprot.org/annotation/VAR_051758|||http://purl.uniprot.org/annotation/VAR_051759|||http://purl.uniprot.org/annotation/VAR_051760|||http://purl.uniprot.org/annotation/VSP_016321|||http://purl.uniprot.org/annotation/VSP_016322|||http://purl.uniprot.org/annotation/VSP_016323|||http://purl.uniprot.org/annotation/VSP_016324|||http://purl.uniprot.org/annotation/VSP_016325
http://togogenome.org/gene/9606:KRCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPI7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Lysine-rich coiled-coil protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306396
http://togogenome.org/gene/9606:KRTAP9-7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTY7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||17 X 5 AA repeats of C-C-[VGSREQH]-[SQTPN]-[STPAI]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332259|||http://purl.uniprot.org/annotation/VAR_042995|||http://purl.uniprot.org/annotation/VAR_042996
http://togogenome.org/gene/9606:LGI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4S7|||http://purl.uniprot.org/uniprot/A0A0S2Z4X3|||http://purl.uniprot.org/uniprot/A0A0S2Z5G1|||http://purl.uniprot.org/uniprot/A0A1B0GUD3|||http://purl.uniprot.org/uniprot/O95970                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects glycosylation; when associated with Q-192 and Q-277. Loss of protein secretion; when associated with Q-192 and Q-277.|||Affects glycosylation; when associated with Q-192 and Q-422. Loss of protein secretion; when associated with Q-192 and Q-422.|||Affects glycosylation; when associated with Q-277 and Q-422. Loss of protein secretion; when associated with Q-277 and Q-422.|||EAR|||EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||EAR 7|||In ETL1.|||In ETL1; loss of protein secretion.|||In ETL1; loss of protein secretion; does not affect glycosylation status of the protein.|||In ETL1; loss of protein secretion; protein is retained in the endoplasmic reticulum; does not affect glycosylation status of the protein.|||In ETL1; probably affects signal sequence processing and secretion.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich glioma-inactivated protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017705|||http://purl.uniprot.org/annotation/PRO_5006608254|||http://purl.uniprot.org/annotation/PRO_5006608272|||http://purl.uniprot.org/annotation/PRO_5008408736|||http://purl.uniprot.org/annotation/PRO_5014239316|||http://purl.uniprot.org/annotation/VAR_015771|||http://purl.uniprot.org/annotation/VAR_015772|||http://purl.uniprot.org/annotation/VAR_015773|||http://purl.uniprot.org/annotation/VAR_015774|||http://purl.uniprot.org/annotation/VAR_023008|||http://purl.uniprot.org/annotation/VAR_023009|||http://purl.uniprot.org/annotation/VAR_058538|||http://purl.uniprot.org/annotation/VAR_058539|||http://purl.uniprot.org/annotation/VAR_058540|||http://purl.uniprot.org/annotation/VAR_058541|||http://purl.uniprot.org/annotation/VAR_058542|||http://purl.uniprot.org/annotation/VAR_058543|||http://purl.uniprot.org/annotation/VAR_058544|||http://purl.uniprot.org/annotation/VAR_058545|||http://purl.uniprot.org/annotation/VAR_058546|||http://purl.uniprot.org/annotation/VAR_058547|||http://purl.uniprot.org/annotation/VAR_058548|||http://purl.uniprot.org/annotation/VSP_007678|||http://purl.uniprot.org/annotation/VSP_007679|||http://purl.uniprot.org/annotation/VSP_038234
http://togogenome.org/gene/9606:C20orf203                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBC4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C20orf203                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394501
http://togogenome.org/gene/9606:ABCB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRK6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family B member 10, mitochondrial|||Does not affect ATPase activity; when associated with L-224 and G-582. Activated by Zn (II) mesoporphyrin; when associated with L-224 and G-582.|||Does not affect ATPase activity; when associated with S-215 and L-224. Activated by Zn (II) mesoporphyrin; when associated with S-215 and L-224.|||Does not affect ATPase activity; when associated withS-215 and G-582. Activated by Zn (II) mesoporphyrin; when associated with S-215 and G-582.|||Does not rescue hemoglobin and heme biosynthetic process.|||Helical|||In a breast cancer sample; somatic mutation.|||Increases hemoglobin biosynthetic process.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||S-glutathionyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000255|||http://purl.uniprot.org/annotation/VAR_013702|||http://purl.uniprot.org/annotation/VAR_031435|||http://purl.uniprot.org/annotation/VAR_035735|||http://purl.uniprot.org/annotation/VAR_048133
http://togogenome.org/gene/9606:GEMIN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXD5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AD|||Gem-associated protein 6|||Phosphoserine|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087460|||http://purl.uniprot.org/annotation/VAR_020391
http://togogenome.org/gene/9606:ASCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1I8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Activating signal cointegrator 1 complex subunit 2|||Basic and acidic residues|||CUE|||Decreases ubiquitin binding.|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of ubiquitin binding.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064689|||http://purl.uniprot.org/annotation/VAR_019464|||http://purl.uniprot.org/annotation/VAR_025512|||http://purl.uniprot.org/annotation/VAR_025513|||http://purl.uniprot.org/annotation/VAR_025514|||http://purl.uniprot.org/annotation/VAR_050675|||http://purl.uniprot.org/annotation/VAR_050676|||http://purl.uniprot.org/annotation/VAR_050677|||http://purl.uniprot.org/annotation/VAR_050678|||http://purl.uniprot.org/annotation/VSP_011009|||http://purl.uniprot.org/annotation/VSP_011010|||http://purl.uniprot.org/annotation/VSP_011011|||http://purl.uniprot.org/annotation/VSP_045878|||http://purl.uniprot.org/annotation/VSP_045879
http://togogenome.org/gene/9606:SLC52A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWF4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Riboflavin transport is unaffected.|||Solute carrier family 52, riboflavin transporter, member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042632|||http://purl.uniprot.org/annotation/VAR_028361|||http://purl.uniprot.org/annotation/VAR_028362|||http://purl.uniprot.org/annotation/VAR_028363|||http://purl.uniprot.org/annotation/VAR_079006|||http://purl.uniprot.org/annotation/VSP_039888|||http://purl.uniprot.org/annotation/VSP_039889
http://togogenome.org/gene/9606:TMC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT65|||http://purl.uniprot.org/uniprot/A0A087WVI4|||http://purl.uniprot.org/uniprot/Q7Z404                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||TMC|||Transmembrane channel-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289468|||http://purl.uniprot.org/annotation/VAR_032621|||http://purl.uniprot.org/annotation/VAR_032622|||http://purl.uniprot.org/annotation/VSP_026011|||http://purl.uniprot.org/annotation/VSP_026012|||http://purl.uniprot.org/annotation/VSP_026013
http://togogenome.org/gene/9606:ZBTB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8U5|||http://purl.uniprot.org/uniprot/Q96C00                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Polar residues|||Zinc finger and BTB domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047723|||http://purl.uniprot.org/annotation/VAR_061981
http://togogenome.org/gene/9606:GTF2H2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1K8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||General transcription factor IIH subunit 2-like protein|||Phosphotyrosine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332132
http://togogenome.org/gene/9606:CYP46A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6A2                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cholesterol 24-hydroxylase|||Helical|||In isoform 2.|||In isoform 3.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051994|||http://purl.uniprot.org/annotation/VSP_053858|||http://purl.uniprot.org/annotation/VSP_053859|||http://purl.uniprot.org/annotation/VSP_053860
http://togogenome.org/gene/9606:COA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WW8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Motif|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase assembly factor 5|||In MC4DN9.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325876|||http://purl.uniprot.org/annotation/VAR_065499
http://togogenome.org/gene/9606:RACK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL35|||http://purl.uniprot.org/uniprot/P63244                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302.|||Decreased binding to PTK2/FAK1; when associated with A-127.|||Decreased binding to PTK2/FAK1; when associated with A-130.|||Decreased binding to PTK2/FAK1; when associated with A-57.|||Decreased binding to PTK2/FAK1; when associated with A-60.|||Enhanced translation of mRNAs containing poly-A leaders.|||In DEmut; abolishes association with the ribosome and ability to initiate the ribosome quality control (RQC).|||N-acetylmethionine|||N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed|||N6-acetyllysine|||No effect on binding to SRC.|||No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation.|||No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246.|||No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-246 and F-302.|||Phosphoserine; by viral VacV B1 kinase|||Phosphothreonine|||Phosphothreonine; by viral VacV B1 kinase|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Removed; alternate|||Small ribosomal subunit protein RACK1|||Small ribosomal subunit protein RACK1, N-terminally processed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127731|||http://purl.uniprot.org/annotation/PRO_0000424480
http://togogenome.org/gene/9606:TTC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGH8|||http://purl.uniprot.org/uniprot/A0A0C4DGX9|||http://purl.uniprot.org/uniprot/A0A0C4DGY3|||http://purl.uniprot.org/uniprot/B3KSL8|||http://purl.uniprot.org/uniprot/Q8TAM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In BBS8.|||In RP51.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Polar residues|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tetratricopeptide repeat protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106388|||http://purl.uniprot.org/annotation/VAR_017247|||http://purl.uniprot.org/annotation/VAR_063705|||http://purl.uniprot.org/annotation/VSP_007821|||http://purl.uniprot.org/annotation/VSP_007822|||http://purl.uniprot.org/annotation/VSP_007823|||http://purl.uniprot.org/annotation/VSP_041151|||http://purl.uniprot.org/annotation/VSP_041152
http://togogenome.org/gene/9606:EMILIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NT22                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EMI|||EMILIN-3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007819|||http://purl.uniprot.org/annotation/VAR_053075|||http://purl.uniprot.org/annotation/VSP_055481
http://togogenome.org/gene/9606:TGIF2LX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUE1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox protein TGIF2LX|||Homeobox; TALE-type|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049324|||http://purl.uniprot.org/annotation/VAR_017867
http://togogenome.org/gene/9606:SPEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKD0|||http://purl.uniprot.org/uniprot/Q9C093                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In SPGF43; loss of protein expression; changed sperm axoneme assembly.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with IFT20|||Sperm flagellar protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299029|||http://purl.uniprot.org/annotation/VAR_034766|||http://purl.uniprot.org/annotation/VAR_034767|||http://purl.uniprot.org/annotation/VAR_034768|||http://purl.uniprot.org/annotation/VAR_034769|||http://purl.uniprot.org/annotation/VAR_034770|||http://purl.uniprot.org/annotation/VAR_034771|||http://purl.uniprot.org/annotation/VAR_034772|||http://purl.uniprot.org/annotation/VAR_034773|||http://purl.uniprot.org/annotation/VAR_051376|||http://purl.uniprot.org/annotation/VAR_051377|||http://purl.uniprot.org/annotation/VAR_083842|||http://purl.uniprot.org/annotation/VAR_083843|||http://purl.uniprot.org/annotation/VSP_027521|||http://purl.uniprot.org/annotation/VSP_027522|||http://purl.uniprot.org/annotation/VSP_027523|||http://purl.uniprot.org/annotation/VSP_027524|||http://purl.uniprot.org/annotation/VSP_027525
http://togogenome.org/gene/9606:CMTM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CKLF-like MARVEL transmembrane domain-containing protein 2|||Disordered|||Helical|||In isoform 2.|||MARVEL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186098|||http://purl.uniprot.org/annotation/VAR_022154|||http://purl.uniprot.org/annotation/VSP_047061
http://togogenome.org/gene/9606:NDUFC2-KCTD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUM3|||http://purl.uniprot.org/uniprot/E9PQ53                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||NADH dehydrogenase [ubiquinone] 1 subunit C2, isoform 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422827
http://togogenome.org/gene/9606:DNAJA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60884                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  CR-type|||CXXCXGXG motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily A member 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||J|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071011|||http://purl.uniprot.org/annotation/PRO_0000393942
http://togogenome.org/gene/9606:ZC3H10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K80                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to pri-MIR143.|||Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Omega-N-methylarginine|||Pro residues|||Reduces binding to pri-MIR143.|||Zinc finger CCCH domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281145
http://togogenome.org/gene/9606:RPL32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62910                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL32|||N6-succinyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131113
http://togogenome.org/gene/9606:MORF4L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15014                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abrogates both transcriptional activation and repression by MORF4L2.|||Basic and acidic residues|||Disordered|||MRG|||Mortality factor 4-like protein 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088768
http://togogenome.org/gene/9606:OR4K17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVZ4                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  G-protein coupled receptors family 1 profile|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ZDHHC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEX5|||http://purl.uniprot.org/uniprot/A0A804HJ40|||http://purl.uniprot.org/uniprot/Q9H6R6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Lipid Binding|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes palmitoylation, leading to impaired homooligomeization and decreased catalytic activity; when associated with 328-A-A-329.|||Abolishes palmitoylation, leading to impaired homooligomeization and decreased catalytic activity; when associated with A-343.|||Cytoplasmic|||DHHC|||Di-lysine motif|||Does not affect localization to the endoplasmic reticulum.|||Helical|||Impaired localization to the endoplasmic reticulum.|||In isoform 2.|||Lumenal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC6|||S-palmitoyl cysteine|||S-palmitoyl cysteine intermediate|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212871|||http://purl.uniprot.org/annotation/VAR_052974|||http://purl.uniprot.org/annotation/VSP_006938
http://togogenome.org/gene/9606:SPOCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92563                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine; by FAM20C|||Testican-2|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026701|||http://purl.uniprot.org/annotation/VAR_022020|||http://purl.uniprot.org/annotation/VSP_045668|||http://purl.uniprot.org/annotation/VSP_045669
http://togogenome.org/gene/9606:GARIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCB4|||http://purl.uniprot.org/uniprot/B3KQ44|||http://purl.uniprot.org/uniprot/B4DXH7|||http://purl.uniprot.org/uniprot/Q8IYT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi associated RAB2 interactor protein-like Rab2B-binding|||Golgi-associated RAB2 interactor protein 4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261630|||http://purl.uniprot.org/annotation/VAR_029464|||http://purl.uniprot.org/annotation/VAR_029465|||http://purl.uniprot.org/annotation/VAR_029466|||http://purl.uniprot.org/annotation/VAR_029467|||http://purl.uniprot.org/annotation/VAR_029468
http://togogenome.org/gene/9606:PLEKHH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULM0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||In isoform 2.|||MyTH4|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin homology domain-containing family H member 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310948|||http://purl.uniprot.org/annotation/VAR_037094|||http://purl.uniprot.org/annotation/VAR_037095|||http://purl.uniprot.org/annotation/VAR_037096|||http://purl.uniprot.org/annotation/VAR_037097|||http://purl.uniprot.org/annotation/VAR_037098|||http://purl.uniprot.org/annotation/VAR_037099|||http://purl.uniprot.org/annotation/VSP_029347|||http://purl.uniprot.org/annotation/VSP_029348|||http://purl.uniprot.org/annotation/VSP_029349
http://togogenome.org/gene/9606:TCF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GW91|||http://purl.uniprot.org/uniprot/A0A1B0GWD5|||http://purl.uniprot.org/uniprot/B3KVA4|||http://purl.uniprot.org/uniprot/E9PH57|||http://purl.uniprot.org/uniprot/H3BPJ7|||http://purl.uniprot.org/uniprot/H3BTP3|||http://purl.uniprot.org/uniprot/P15884                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||BHLH|||Basic and acidic residues|||Class A specific domain|||Disordered|||Essential for MYOD1 inhibition|||In PTHS.|||In PTHS; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner.|||In PTHS; loss of function.|||In PTHS; loss of function; also expressed in the nucleus with a pattern indistinguishable from the wild-type; does not have a major impact on homodimer formation; affects transcriptional activity in a context-dependent manner.|||In PTHS; loss of function; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner.|||In PTHS; mislocalized to small spherical punctae that are dispersed throughout the nucleus; can attenuate homo- and heterodimer formation; affects transcriptional activity in a context-dependent manner.|||In isoform 11.|||In isoform 13, isoform C- and isoform C-delta.|||In isoform A-, isoform B-delta, isoform B+delta and isoform C-delta.|||In isoform A-.|||In isoform B+delta, isoform SEF2-1A, isoform SEF2-1D, isoform 11 and isoform 13.|||In isoform D-.|||In isoform E-.|||In isoform F-.|||In isoform G- and isoform 11.|||In isoform G-.|||In isoform H-.|||In isoform I-.|||In isoform SEF2-1A.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a family with symmetrical acral keratoderma.|||Transcription factor 4|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127256|||http://purl.uniprot.org/annotation/VAR_034704|||http://purl.uniprot.org/annotation/VAR_034705|||http://purl.uniprot.org/annotation/VAR_049545|||http://purl.uniprot.org/annotation/VAR_058632|||http://purl.uniprot.org/annotation/VAR_058633|||http://purl.uniprot.org/annotation/VAR_058634|||http://purl.uniprot.org/annotation/VAR_066839|||http://purl.uniprot.org/annotation/VAR_066840|||http://purl.uniprot.org/annotation/VAR_066841|||http://purl.uniprot.org/annotation/VAR_066970|||http://purl.uniprot.org/annotation/VAR_066971|||http://purl.uniprot.org/annotation/VAR_066972|||http://purl.uniprot.org/annotation/VAR_066973|||http://purl.uniprot.org/annotation/VAR_066974|||http://purl.uniprot.org/annotation/VAR_078644|||http://purl.uniprot.org/annotation/VAR_079726|||http://purl.uniprot.org/annotation/VSP_002111|||http://purl.uniprot.org/annotation/VSP_002112|||http://purl.uniprot.org/annotation/VSP_030819|||http://purl.uniprot.org/annotation/VSP_044334|||http://purl.uniprot.org/annotation/VSP_044335|||http://purl.uniprot.org/annotation/VSP_044336|||http://purl.uniprot.org/annotation/VSP_044337|||http://purl.uniprot.org/annotation/VSP_044338|||http://purl.uniprot.org/annotation/VSP_044339|||http://purl.uniprot.org/annotation/VSP_044340|||http://purl.uniprot.org/annotation/VSP_045149|||http://purl.uniprot.org/annotation/VSP_045150|||http://purl.uniprot.org/annotation/VSP_045151|||http://purl.uniprot.org/annotation/VSP_047081|||http://purl.uniprot.org/annotation/VSP_047082|||http://purl.uniprot.org/annotation/VSP_047083|||http://purl.uniprot.org/annotation/VSP_054279|||http://purl.uniprot.org/annotation/VSP_057364
http://togogenome.org/gene/9606:RFLNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||Pro residues|||Refilin-A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274331|||http://purl.uniprot.org/annotation/VSP_022713
http://togogenome.org/gene/9606:BAZ2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VU39|||http://purl.uniprot.org/uniprot/Q9UIF9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||A.T hook 4|||Basic and acidic residues|||Bromo|||Bromodomain adjacent to zinc finger domain protein 2A|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 3.|||MBD|||N6-acetyllysine|||N6-acetyllysine; by KAT8|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211172|||http://purl.uniprot.org/annotation/VAR_055548|||http://purl.uniprot.org/annotation/VSP_019111|||http://purl.uniprot.org/annotation/VSP_037960|||http://purl.uniprot.org/annotation/VSP_037961
http://togogenome.org/gene/9606:LANCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV70                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LanC-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285251|||http://purl.uniprot.org/annotation/VSP_024855
http://togogenome.org/gene/9606:FGG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ6|||http://purl.uniprot.org/uniprot/P02679                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by hementin; to prevent blood coagulation|||Cleavage; by plasmin; to break down fibrin clots|||Disordered|||Fibrinogen C-terminal|||Fibrinogen gamma chain|||Gamma-chain polymerization, binding amino end of another fibrin alpha chain|||In Asahi; impaired polymerization.|||In Baltimore-3; impaired polymerization.|||In Bern-1; impaired polymerization.|||In CAFBN; hypofibrinogenemia; heterozygous.|||In CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; decreased fibrinogen complex secretion.|||In CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; impaired fibrinogen complex secretion.|||In CAFBN; hypofibrinogenemia; heterozygous; no effect on fibrinogen complex assembly; no effect on fibrinogen complex secretion.|||In DYSFIBRIN; fibrinogen Baltimore-1; impaired polymerization.|||In DYSFIBRIN; fibrinogen Bergamo-2/Essen/Haifa/Osaka-3/Perugia/Saga/Barcelona-3/Barcelona-4.|||In DYSFIBRIN; fibrinogen Milano-1; impaired polymerization.|||In DYSFIBRIN; fibrinogen Philadelphia.|||In Hillsborough; prolonged thrombin clotting time.|||In Kyoto-1; causes accelerated cleavage by plasmin.|||In Kyoto-3; impaired polymerization.|||In Milano-12.|||In Milano-7; impaired polymerization.|||In Nagoya-1; impaired polymerization.|||In Osaka-5.|||In Paris-1; impaired polymerization.|||In Tochigi/Osaka-2/Milano-5/Villajoyosa.|||In Vlissingen; defective calcium binding and impaired polymerization.|||In isoform Gamma-A.|||Interchain (with C-110 in beta chain)|||Interchain (with C-180 in alpha chain)|||Interchain (with C-227 in beta chain)|||Interchain (with C-34)|||Interchain (with C-35)|||Interchain (with C-64 in alpha chain)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-432)|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-424)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine; in variant Asahi|||Phosphoserine; by FAM20C|||Platelet aggregation and Staphylococcus clumping|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009099|||http://purl.uniprot.org/annotation/PRO_5007491731|||http://purl.uniprot.org/annotation/VAR_002409|||http://purl.uniprot.org/annotation/VAR_002410|||http://purl.uniprot.org/annotation/VAR_002411|||http://purl.uniprot.org/annotation/VAR_002412|||http://purl.uniprot.org/annotation/VAR_002413|||http://purl.uniprot.org/annotation/VAR_002414|||http://purl.uniprot.org/annotation/VAR_002415|||http://purl.uniprot.org/annotation/VAR_002416|||http://purl.uniprot.org/annotation/VAR_002417|||http://purl.uniprot.org/annotation/VAR_002418|||http://purl.uniprot.org/annotation/VAR_002419|||http://purl.uniprot.org/annotation/VAR_002420|||http://purl.uniprot.org/annotation/VAR_002421|||http://purl.uniprot.org/annotation/VAR_002422|||http://purl.uniprot.org/annotation/VAR_014170|||http://purl.uniprot.org/annotation/VAR_014171|||http://purl.uniprot.org/annotation/VAR_015853|||http://purl.uniprot.org/annotation/VAR_033930|||http://purl.uniprot.org/annotation/VAR_049066|||http://purl.uniprot.org/annotation/VAR_072621|||http://purl.uniprot.org/annotation/VAR_072726|||http://purl.uniprot.org/annotation/VAR_072727|||http://purl.uniprot.org/annotation/VAR_072728|||http://purl.uniprot.org/annotation/VAR_072729|||http://purl.uniprot.org/annotation/VSP_001537
http://togogenome.org/gene/9606:CD72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21854|||http://purl.uniprot.org/uniprot/Q5TLG3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B-cell differentiation antigen CD72|||C-type lectin|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by LYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046585|||http://purl.uniprot.org/annotation/VAR_033729
http://togogenome.org/gene/9606:THAP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ7|||http://purl.uniprot.org/uniprot/O43422                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  52 kDa repressor of the inhibitor of the protein kinase|||Basic and acidic residues|||Disordered|||In isoform Short.|||Phosphoserine|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068634|||http://purl.uniprot.org/annotation/VSP_004355|||http://purl.uniprot.org/annotation/VSP_004356
http://togogenome.org/gene/9606:OLFML2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWE8|||http://purl.uniprot.org/uniprot/F2Z3N3|||http://purl.uniprot.org/uniprot/Q68BL8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Olfactomedin-like protein 2B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311426|||http://purl.uniprot.org/annotation/PRO_5002803623|||http://purl.uniprot.org/annotation/PRO_5003290161|||http://purl.uniprot.org/annotation/VAR_037248|||http://purl.uniprot.org/annotation/VAR_037249|||http://purl.uniprot.org/annotation/VSP_029564
http://togogenome.org/gene/9606:MED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15648                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Enhances interaction with ESR1.|||Enhances protein stability; when associated with A-1032.|||Enhances protein stability; when associated with A-1457.|||Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649.|||Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608.|||Impairs interaction with ESR2; when associated with A-604; A-607 and A-645.|||Impairs interaction with ESR2; when associated with A-604; A-607 and A-648.|||Impairs interaction with ESR2; when associated with A-604; A-645 and A-648.|||Impairs interaction with ESR2; when associated with A-607; A-645 and A-648.|||In isoform 2.|||Increased interaction with PSIP1; when associated with D-886 and D-887.|||Increased interaction with PSIP1; when associated with D-887 or D-887 and D-889.|||Integrase domain-binding motif (IBM)|||Interaction with ESR1|||Interaction with GATA1|||Interaction with PPARGC1A and THRA|||Interaction with THRA|||Interaction with TP53|||Interaction with VDR|||Interaction with the Mediator complex|||Interaction with the Mediator complex and THRA|||LXXLL motif 1|||LXXLL motif 2|||Mediator of RNA polymerase II transcription subunit 1|||N6-acetyllysine|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-886 or D-886 and D-889.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by MAPK1 or MAPK3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058552|||http://purl.uniprot.org/annotation/VAR_034938|||http://purl.uniprot.org/annotation/VAR_053955|||http://purl.uniprot.org/annotation/VSP_027906|||http://purl.uniprot.org/annotation/VSP_027907
http://togogenome.org/gene/9606:TAS2R46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59540                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082318|||http://purl.uniprot.org/annotation/VAR_062091
http://togogenome.org/gene/9606:GPRIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60269                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||G protein-regulated inducer of neurite outgrowth 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050759|||http://purl.uniprot.org/annotation/VAR_051017|||http://purl.uniprot.org/annotation/VAR_051018|||http://purl.uniprot.org/annotation/VAR_059660|||http://purl.uniprot.org/annotation/VAR_059661|||http://purl.uniprot.org/annotation/VAR_059662|||http://purl.uniprot.org/annotation/VAR_059663|||http://purl.uniprot.org/annotation/VAR_059664|||http://purl.uniprot.org/annotation/VAR_061656|||http://purl.uniprot.org/annotation/VAR_061657|||http://purl.uniprot.org/annotation/VAR_061658|||http://purl.uniprot.org/annotation/VAR_061659|||http://purl.uniprot.org/annotation/VAR_061660|||http://purl.uniprot.org/annotation/VAR_061661|||http://purl.uniprot.org/annotation/VAR_061662
http://togogenome.org/gene/9606:DLG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FY1|||http://purl.uniprot.org/uniprot/Q92796                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disks large homolog 3|||Disordered|||Guanylate kinase-like|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094557|||http://purl.uniprot.org/annotation/VAR_036591|||http://purl.uniprot.org/annotation/VSP_035940|||http://purl.uniprot.org/annotation/VSP_035941|||http://purl.uniprot.org/annotation/VSP_035942|||http://purl.uniprot.org/annotation/VSP_043717
http://togogenome.org/gene/9606:ALDOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09972                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Fructose-bisphosphate aldolase C|||N6-acetyllysine|||Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Schiff-base intermediate with dihydroxyacetone-P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216947
http://togogenome.org/gene/9606:PDE6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16499                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||GAF 1|||GAF 2|||In RP43.|||N-acetylglycine|||PDEase|||Polar residues|||Proton donor|||Removed|||Removed in mature form|||Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198828|||http://purl.uniprot.org/annotation/PRO_0000396697|||http://purl.uniprot.org/annotation/VAR_006049|||http://purl.uniprot.org/annotation/VAR_025460|||http://purl.uniprot.org/annotation/VAR_025461|||http://purl.uniprot.org/annotation/VAR_025462|||http://purl.uniprot.org/annotation/VAR_025463|||http://purl.uniprot.org/annotation/VAR_025464|||http://purl.uniprot.org/annotation/VAR_025465|||http://purl.uniprot.org/annotation/VAR_025466|||http://purl.uniprot.org/annotation/VAR_025467|||http://purl.uniprot.org/annotation/VAR_025468|||http://purl.uniprot.org/annotation/VAR_025469|||http://purl.uniprot.org/annotation/VAR_047730|||http://purl.uniprot.org/annotation/VAR_047731
http://togogenome.org/gene/9606:ZNF397                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NF99                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||SCAN box|||Zinc finger protein 397                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047564|||http://purl.uniprot.org/annotation/VSP_006924|||http://purl.uniprot.org/annotation/VSP_006925|||http://purl.uniprot.org/annotation/VSP_042491|||http://purl.uniprot.org/annotation/VSP_042492
http://togogenome.org/gene/9606:GRIA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8D9PH77|||http://purl.uniprot.org/uniprot/A0A994J6J2|||http://purl.uniprot.org/uniprot/P48058|||http://purl.uniprot.org/uniprot/Q1WWK6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutamate receptor|||Glutamate receptor 4|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||In NEDSGA.|||In NEDSGA; unknown pathological significance.|||In isoform 2.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC/PRKCG|||Receptor ligand binding region|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011538|||http://purl.uniprot.org/annotation/PRO_5027154789|||http://purl.uniprot.org/annotation/PRO_5034636123|||http://purl.uniprot.org/annotation/PRO_5040530506|||http://purl.uniprot.org/annotation/VAR_080751|||http://purl.uniprot.org/annotation/VAR_080752|||http://purl.uniprot.org/annotation/VAR_080753|||http://purl.uniprot.org/annotation/VAR_080754|||http://purl.uniprot.org/annotation/VAR_080755|||http://purl.uniprot.org/annotation/VSP_042742|||http://purl.uniprot.org/annotation/VSP_042743
http://togogenome.org/gene/9606:CWC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KQK1|||http://purl.uniprot.org/uniprot/A0A8I5KRF5|||http://purl.uniprot.org/uniprot/D6REK3|||http://purl.uniprot.org/uniprot/Q6UX04                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In RPSKA.|||In isoform 2.|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||PPIase cyclophilin-type|||Phosphoserine|||Removed|||Spliceosome-associated protein CWC27 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313647|||http://purl.uniprot.org/annotation/VAR_037686|||http://purl.uniprot.org/annotation/VAR_078981|||http://purl.uniprot.org/annotation/VAR_078982|||http://purl.uniprot.org/annotation/VAR_078983|||http://purl.uniprot.org/annotation/VAR_078984|||http://purl.uniprot.org/annotation/VSP_030082|||http://purl.uniprot.org/annotation/VSP_030083
http://togogenome.org/gene/9606:UNKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PDK2|||http://purl.uniprot.org/uniprot/Q9H9P5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||In isoform 1 and isoform 2.|||In isoform 1 and isoform 3.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||No effects on the interaction with RAC1 or SMARCD2; when associated with A-639.|||No effects on the interaction with RAC1 or SMARCD2; when associated with A-670.|||Polar residues|||Pro residues|||Putative E3 ubiquitin-protein ligase UNKL|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278667|||http://purl.uniprot.org/annotation/VSP_039432|||http://purl.uniprot.org/annotation/VSP_039433|||http://purl.uniprot.org/annotation/VSP_039434|||http://purl.uniprot.org/annotation/VSP_039435|||http://purl.uniprot.org/annotation/VSP_039436|||http://purl.uniprot.org/annotation/VSP_039437|||http://purl.uniprot.org/annotation/VSP_039438|||http://purl.uniprot.org/annotation/VSP_039439|||http://purl.uniprot.org/annotation/VSP_039440|||http://purl.uniprot.org/annotation/VSP_039441|||http://purl.uniprot.org/annotation/VSP_039442|||http://purl.uniprot.org/annotation/VSP_039443
http://togogenome.org/gene/9606:CFC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG36                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Cryptic family protein 1B|||EGF-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395408
http://togogenome.org/gene/9606:DPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94777                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Dolichol phosphate-mannose biosynthesis regulatory protein|||Helical|||In CDG1U.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220873|||http://purl.uniprot.org/annotation/VAR_033895|||http://purl.uniprot.org/annotation/VAR_069745
http://togogenome.org/gene/9606:SNX21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z632|||http://purl.uniprot.org/uniprot/Q05DJ0|||http://purl.uniprot.org/uniprot/Q8WY78|||http://purl.uniprot.org/uniprot/Q969T3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PX|||Sorting nexin-21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213870|||http://purl.uniprot.org/annotation/VAR_052482|||http://purl.uniprot.org/annotation/VSP_045048|||http://purl.uniprot.org/annotation/VSP_045049|||http://purl.uniprot.org/annotation/VSP_047115
http://togogenome.org/gene/9606:NOXO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K832|||http://purl.uniprot.org/uniprot/Q8NFA2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Induces interaction with NOXA1 in vitro.|||Loss of ability to activate NOX1 associated with loss of lipid-binding and plasma membrane localization.|||Loss of ability to activate NOX3 and interact with CYBA. Induces interaction with NOXA1 in vitro.|||Loss of intramolecular interaction.|||NADPH oxidase organizer 1|||PX|||Proline-rich region; mediates mutually exclusive interactions with itself and NOXA1|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227594|||http://purl.uniprot.org/annotation/VSP_017560|||http://purl.uniprot.org/annotation/VSP_017561
http://togogenome.org/gene/9606:IGFBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22692                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||IGFBP N-terminal|||In isoform 2.|||Insulin-like growth factor-binding protein 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014382|||http://purl.uniprot.org/annotation/VAR_011906|||http://purl.uniprot.org/annotation/VSP_057034
http://togogenome.org/gene/9606:ALKAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXT8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  ALK and LTK ligand 1|||Disordered|||In isoform 2.|||Reduced affinity for receptor tyrosine kinase LTK.|||Slightly reduced affinity for receptor tyrosine kinase LTK.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317192|||http://purl.uniprot.org/annotation/VSP_055085
http://togogenome.org/gene/9606:ECI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42126                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Enoyl-CoA delta isomerase 1, mitochondrial|||Important for catalytic activity|||In isoform 2.|||Loss of activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007420|||http://purl.uniprot.org/annotation/VSP_001358
http://togogenome.org/gene/9606:H2AC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FI13                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 2-A|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055232
http://togogenome.org/gene/9606:SLC5A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY91                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Probable glucose sensor protein SLC5A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105376|||http://purl.uniprot.org/annotation/VAR_021997|||http://purl.uniprot.org/annotation/VAR_052489
http://togogenome.org/gene/9606:POLM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP87                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT|||DNA-directed DNA/RNA polymerase mu|||Disordered|||In isoform 2.|||In isoform 3.|||Involved in ssDNA binding|||Phosphoserine|||Responsible for the low discrimination between dNTP and rNTP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218787|||http://purl.uniprot.org/annotation/VAR_022287|||http://purl.uniprot.org/annotation/VAR_022288|||http://purl.uniprot.org/annotation/VAR_022289|||http://purl.uniprot.org/annotation/VAR_022290|||http://purl.uniprot.org/annotation/VSP_055288|||http://purl.uniprot.org/annotation/VSP_055289|||http://purl.uniprot.org/annotation/VSP_055290|||http://purl.uniprot.org/annotation/VSP_055291
http://togogenome.org/gene/9606:MXD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW11                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with SIN3A and SIN3B|||Max dimerization protein 3|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253707|||http://purl.uniprot.org/annotation/VAR_049546|||http://purl.uniprot.org/annotation/VSP_021109|||http://purl.uniprot.org/annotation/VSP_021110|||http://purl.uniprot.org/annotation/VSP_057220
http://togogenome.org/gene/9606:TMEM44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2T9K0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Transmembrane protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284544|||http://purl.uniprot.org/annotation/VAR_031775|||http://purl.uniprot.org/annotation/VAR_066998|||http://purl.uniprot.org/annotation/VAR_066999|||http://purl.uniprot.org/annotation/VSP_024565|||http://purl.uniprot.org/annotation/VSP_024569|||http://purl.uniprot.org/annotation/VSP_024571|||http://purl.uniprot.org/annotation/VSP_039211|||http://purl.uniprot.org/annotation/VSP_046357
http://togogenome.org/gene/9606:WDR55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1J0|||http://purl.uniprot.org/uniprot/Q9H6Y2                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237598|||http://purl.uniprot.org/annotation/VAR_037056|||http://purl.uniprot.org/annotation/VAR_037057|||http://purl.uniprot.org/annotation/VAR_037058|||http://purl.uniprot.org/annotation/VAR_037059|||http://purl.uniprot.org/annotation/VSP_037275
http://togogenome.org/gene/9606:FSTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZW2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand|||Follistatin-related protein 4|||Ig-like 1|||Ig-like 2|||In isoform 2.|||In isoform 3.|||Kazal-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251925|||http://purl.uniprot.org/annotation/VAR_027727|||http://purl.uniprot.org/annotation/VAR_027728|||http://purl.uniprot.org/annotation/VSP_020800|||http://purl.uniprot.org/annotation/VSP_020801|||http://purl.uniprot.org/annotation/VSP_020802
http://togogenome.org/gene/9606:OTOL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHN0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  5-hydroxylysine|||Basic and acidic residues|||C1q|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Disordered|||Hydroxyproline|||N-linked (GlcNAc...) asparagine|||O-linked (Gal...) hydroxylysine|||Otolin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332215|||http://purl.uniprot.org/annotation/VAR_042975
http://togogenome.org/gene/9606:C8G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07360                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Complement component C8 gamma chain|||Interchain (with C-194 in C8-alpha chain)|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017881|||http://purl.uniprot.org/annotation/VAR_014668|||http://purl.uniprot.org/annotation/VAR_014669|||http://purl.uniprot.org/annotation/VAR_044319
http://togogenome.org/gene/9606:CDK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00526                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 3|||In a glioblastoma multiforme sample; somatic mutation.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085776|||http://purl.uniprot.org/annotation/VAR_021101|||http://purl.uniprot.org/annotation/VAR_021102|||http://purl.uniprot.org/annotation/VAR_041973|||http://purl.uniprot.org/annotation/VAR_041974|||http://purl.uniprot.org/annotation/VAR_041975
http://togogenome.org/gene/9606:HBEGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99075                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Heparin-binding EGF-like growth factor|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Or 72, or 73, or 76, or 81|||Plays a critical role in diphtheria toxin binding and toxin sensitivity|||Proheparin-binding EGF-like growth factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007611|||http://purl.uniprot.org/annotation/PRO_0000007612|||http://purl.uniprot.org/annotation/PRO_0000007613|||http://purl.uniprot.org/annotation/PRO_0000302803
http://togogenome.org/gene/9606:TINAGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6SDV2|||http://purl.uniprot.org/uniprot/Q9GZM7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alternate|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal|||SMB|||Tubulointerstitial nephritis antigen-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026482|||http://purl.uniprot.org/annotation/VAR_051514|||http://purl.uniprot.org/annotation/VSP_013094|||http://purl.uniprot.org/annotation/VSP_013095|||http://purl.uniprot.org/annotation/VSP_013096|||http://purl.uniprot.org/annotation/VSP_013097|||http://purl.uniprot.org/annotation/VSP_013098|||http://purl.uniprot.org/annotation/VSP_043712
http://togogenome.org/gene/9606:DIPK1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ97|||http://purl.uniprot.org/uniprot/A0A087WZK6|||http://purl.uniprot.org/uniprot/A0A087X2C2|||http://purl.uniprot.org/uniprot/Q5T7M9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Divergent protein kinase domain 1A|||FAM69 N-terminal|||Helical|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282423|||http://purl.uniprot.org/annotation/VSP_024140|||http://purl.uniprot.org/annotation/VSP_024141
http://togogenome.org/gene/9606:GABBR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NIL8|||http://purl.uniprot.org/uniprot/O75899                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 3 profile|||Gamma-aminobutyric acid type B receptor subunit 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs interaction with GABBR1. Decreases signaling via G-proteins.|||In DEE59; full signaling activity in the absence of GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression.|||In DEE59; increased basal signaling activity and no stimulation by GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression.|||In DEE59; unknown pathological significance.|||In NDPLHS; increased basal signaling activity and only weak stimulation by GABA agonist; no effect on cell surface expression.|||In NDPLHS; increased basal signaling activity and only weak stimulation by GABA agonist; when injected into Xenopus tadpoles, causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals; no effect on cell surface expression.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012952|||http://purl.uniprot.org/annotation/PRO_5014305221|||http://purl.uniprot.org/annotation/VAR_010148|||http://purl.uniprot.org/annotation/VAR_010149|||http://purl.uniprot.org/annotation/VAR_049280|||http://purl.uniprot.org/annotation/VAR_079029|||http://purl.uniprot.org/annotation/VAR_080569|||http://purl.uniprot.org/annotation/VAR_080570|||http://purl.uniprot.org/annotation/VAR_080571|||http://purl.uniprot.org/annotation/VAR_080572
http://togogenome.org/gene/9606:POTEE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S8J3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Actin-like|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||POTE ankyrin domain family member E|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066914|||http://purl.uniprot.org/annotation/VSP_011969|||http://purl.uniprot.org/annotation/VSP_011970|||http://purl.uniprot.org/annotation/VSP_011971|||http://purl.uniprot.org/annotation/VSP_011972|||http://purl.uniprot.org/annotation/VSP_011973
http://togogenome.org/gene/9606:CFAP251                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 251|||Disordered|||In SPGF33.|||In isoform 2.|||In isoform 3.|||Polar residues|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296255|||http://purl.uniprot.org/annotation/VAR_034623|||http://purl.uniprot.org/annotation/VAR_034624|||http://purl.uniprot.org/annotation/VAR_034625|||http://purl.uniprot.org/annotation/VAR_060044|||http://purl.uniprot.org/annotation/VAR_081181|||http://purl.uniprot.org/annotation/VSP_027165|||http://purl.uniprot.org/annotation/VSP_027166|||http://purl.uniprot.org/annotation/VSP_027167|||http://purl.uniprot.org/annotation/VSP_027168
http://togogenome.org/gene/9606:TUBA3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPH8|||http://purl.uniprot.org/uniprot/Q1ZYQ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  3'-nitrotyrosine|||Detyrosinated tubulin alpha-3D chain|||In KTCN9; loss of protein.|||Involved in polymerization|||MREC motif|||N6-acetyllysine|||Phosphoserine|||Tubulin alpha-3D chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444671|||http://purl.uniprot.org/annotation/PRO_0000444672|||http://purl.uniprot.org/annotation/VAR_080471
http://togogenome.org/gene/9606:TTLL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVT0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Inactive polyglycylase TTLL10|||Polar residues|||Pro residues|||Recovers polyglycylase activity; when associated with N-448.|||Recovers polyglycylase activity; when associated with T-467.|||TTL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324520|||http://purl.uniprot.org/annotation/VAR_039806|||http://purl.uniprot.org/annotation/VAR_039807|||http://purl.uniprot.org/annotation/VAR_039808|||http://purl.uniprot.org/annotation/VAR_058480|||http://purl.uniprot.org/annotation/VSP_032262|||http://purl.uniprot.org/annotation/VSP_032263|||http://purl.uniprot.org/annotation/VSP_032264
http://togogenome.org/gene/9606:NPC1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFX6|||http://purl.uniprot.org/uniprot/Q9UHC9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with LIMA1.|||Associated with low LDL-C content and protection against coronary heart disease.|||Cytoplasmic|||Does not affect interaction with LIMA1.|||Extracellular|||Found in a non-responder to ezetimibe treatment.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||NPC1-like intracellular cholesterol transporter 1|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023266|||http://purl.uniprot.org/annotation/PRO_5002178504|||http://purl.uniprot.org/annotation/VAR_023369|||http://purl.uniprot.org/annotation/VAR_023370|||http://purl.uniprot.org/annotation/VAR_056659|||http://purl.uniprot.org/annotation/VAR_056660|||http://purl.uniprot.org/annotation/VAR_080844|||http://purl.uniprot.org/annotation/VAR_080845|||http://purl.uniprot.org/annotation/VAR_080846|||http://purl.uniprot.org/annotation/VAR_080847|||http://purl.uniprot.org/annotation/VAR_080848|||http://purl.uniprot.org/annotation/VAR_080849|||http://purl.uniprot.org/annotation/VAR_080850|||http://purl.uniprot.org/annotation/VAR_080851|||http://purl.uniprot.org/annotation/VAR_080852|||http://purl.uniprot.org/annotation/VAR_080853|||http://purl.uniprot.org/annotation/VSP_015312|||http://purl.uniprot.org/annotation/VSP_015313|||http://purl.uniprot.org/annotation/VSP_015314|||http://purl.uniprot.org/annotation/VSP_054503
http://togogenome.org/gene/9606:CRELD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJJ0|||http://purl.uniprot.org/uniprot/Q96HD1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CXXC|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||FU 1|||FU 2|||Helical|||In AVSD2; associated with disease susceptibility.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein disulfide isomerase CRELD1|||Redox-active|||protein disulfide-isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042781|||http://purl.uniprot.org/annotation/PRO_5032556255|||http://purl.uniprot.org/annotation/VAR_023764|||http://purl.uniprot.org/annotation/VAR_023765|||http://purl.uniprot.org/annotation/VAR_023766|||http://purl.uniprot.org/annotation/VAR_023767|||http://purl.uniprot.org/annotation/VAR_046653|||http://purl.uniprot.org/annotation/VAR_046654|||http://purl.uniprot.org/annotation/VSP_016091
http://togogenome.org/gene/9606:ITGB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLD8|||http://purl.uniprot.org/uniprot/P16144                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calx-beta|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||In JEB5A.|||In JEB5B.|||In JEB5B; abolishes interaction with PLEC and reduces interaction with COL17A1.|||In isoform Beta-4A, isoform Beta-4B and isoform Beta-4D.|||In isoform Beta-4B.|||In isoform Beta-4D.|||In isoform Beta-4E.|||Integrin beta|||Integrin beta-4|||Involved in NRG1- and IGF1-binding|||N-linked (GlcNAc...) asparagine|||PSI|||Palmitoylated on several cysteines|||Phosphoserine|||Phosphothreonine|||VWFA|||in ADMIDAS binding site|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016346|||http://purl.uniprot.org/annotation/PRO_5002866680|||http://purl.uniprot.org/annotation/VAR_004006|||http://purl.uniprot.org/annotation/VAR_004007|||http://purl.uniprot.org/annotation/VAR_004008|||http://purl.uniprot.org/annotation/VAR_004009|||http://purl.uniprot.org/annotation/VAR_004010|||http://purl.uniprot.org/annotation/VAR_004011|||http://purl.uniprot.org/annotation/VAR_010652|||http://purl.uniprot.org/annotation/VAR_011292|||http://purl.uniprot.org/annotation/VAR_011293|||http://purl.uniprot.org/annotation/VAR_011294|||http://purl.uniprot.org/annotation/VAR_011295|||http://purl.uniprot.org/annotation/VAR_011296|||http://purl.uniprot.org/annotation/VAR_011297|||http://purl.uniprot.org/annotation/VAR_011298|||http://purl.uniprot.org/annotation/VAR_011299|||http://purl.uniprot.org/annotation/VAR_011300|||http://purl.uniprot.org/annotation/VAR_011301|||http://purl.uniprot.org/annotation/VAR_027803|||http://purl.uniprot.org/annotation/VAR_027804|||http://purl.uniprot.org/annotation/VAR_055971|||http://purl.uniprot.org/annotation/VSP_002747|||http://purl.uniprot.org/annotation/VSP_002748|||http://purl.uniprot.org/annotation/VSP_002749|||http://purl.uniprot.org/annotation/VSP_002750|||http://purl.uniprot.org/annotation/VSP_002751
http://togogenome.org/gene/9606:MRPS28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z563|||http://purl.uniprot.org/uniprot/Q9Y2Q9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In COXPD47; strong decrease in mitochondrial translation and in oxidative phosphorylation biogenesis; this phenotype could be reversed in patient's fibroblasts by transfection with the wild-type protein.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Small ribosomal subunit protein bS1m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087714|||http://purl.uniprot.org/annotation/VAR_052047|||http://purl.uniprot.org/annotation/VAR_084507
http://togogenome.org/gene/9606:MOGAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VF5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  2-acylglycerol O-acyltransferase 3|||Catalitically inactive. No 2-acylglycerol O-acyltransferase neither diacylglycerol O-acyltransferase activities.|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Reduces 60% 2-acylglycerol O-acyltransferase activity. No effect on diacylglycerol O-acyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249067|||http://purl.uniprot.org/annotation/VSP_020361|||http://purl.uniprot.org/annotation/VSP_020362|||http://purl.uniprot.org/annotation/VSP_020363
http://togogenome.org/gene/9606:TIAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW11|||http://purl.uniprot.org/uniprot/Q8IVF5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-myristoyl glycine|||PDZ|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||RBD|||Removed|||Rho guanine nucleotide exchange factor TIAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317467|||http://purl.uniprot.org/annotation/VAR_038534|||http://purl.uniprot.org/annotation/VAR_038535|||http://purl.uniprot.org/annotation/VAR_051994|||http://purl.uniprot.org/annotation/VAR_051995|||http://purl.uniprot.org/annotation/VAR_051996|||http://purl.uniprot.org/annotation/VSP_030971|||http://purl.uniprot.org/annotation/VSP_030972|||http://purl.uniprot.org/annotation/VSP_030974|||http://purl.uniprot.org/annotation/VSP_030975
http://togogenome.org/gene/9606:APOD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05090                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Apolipoprotein D|||Interchain (with C-29 in APOA2)|||N-linked (GlcNAc...) (complex) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017872|||http://purl.uniprot.org/annotation/VAR_011931|||http://purl.uniprot.org/annotation/VAR_011932|||http://purl.uniprot.org/annotation/VAR_011933
http://togogenome.org/gene/9606:ZMYM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3Z7|||http://purl.uniprot.org/uniprot/Q14202                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||MYM-type 5|||MYM-type 6|||MYM-type 7|||MYM-type 8|||MYM-type 9|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TRASH|||Zinc finger MYM-type protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191378|||http://purl.uniprot.org/annotation/VSP_004492|||http://purl.uniprot.org/annotation/VSP_043262|||http://purl.uniprot.org/annotation/VSP_043263
http://togogenome.org/gene/9606:ERCC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W1GSK9|||http://purl.uniprot.org/uniprot/A0A804HKF9|||http://purl.uniprot.org/uniprot/B4DXD8|||http://purl.uniprot.org/uniprot/Q92889                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished acetylation by KAT5, leading to decreased interaction with ERCC1.|||Basic and acidic residues|||DNA repair endonuclease XPF|||Disordered|||ERCC4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase-like|||HhH2, dimerization with ERCC1|||In FANCQ.|||In FANCQ; disruption of interstrand cross-link repair activity; no effect on protein stability.|||In XFEPS.|||In XP-F.|||In XP-F; mild; significant residual repair activity.|||In XPF/CS.|||In isoform 2.|||Leucine-zipper 1|||Leucine-zipper 2|||Mimics acetylation; promoting interaction with ERCC1.|||N6-acetyllysine|||Nuclear localization signal|||Nuclease|||Phosphoserine|||Rare functional variant; causes mild disruption of interstrand cross-link repair activity; partial loss of protein stability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198853|||http://purl.uniprot.org/annotation/VAR_005849|||http://purl.uniprot.org/annotation/VAR_005850|||http://purl.uniprot.org/annotation/VAR_008200|||http://purl.uniprot.org/annotation/VAR_008201|||http://purl.uniprot.org/annotation/VAR_008202|||http://purl.uniprot.org/annotation/VAR_008203|||http://purl.uniprot.org/annotation/VAR_008204|||http://purl.uniprot.org/annotation/VAR_008205|||http://purl.uniprot.org/annotation/VAR_008206|||http://purl.uniprot.org/annotation/VAR_008207|||http://purl.uniprot.org/annotation/VAR_013395|||http://purl.uniprot.org/annotation/VAR_013396|||http://purl.uniprot.org/annotation/VAR_013397|||http://purl.uniprot.org/annotation/VAR_013398|||http://purl.uniprot.org/annotation/VAR_013399|||http://purl.uniprot.org/annotation/VAR_013408|||http://purl.uniprot.org/annotation/VAR_014769|||http://purl.uniprot.org/annotation/VAR_014770|||http://purl.uniprot.org/annotation/VAR_014771|||http://purl.uniprot.org/annotation/VAR_014772|||http://purl.uniprot.org/annotation/VAR_019201|||http://purl.uniprot.org/annotation/VAR_034802|||http://purl.uniprot.org/annotation/VAR_057477|||http://purl.uniprot.org/annotation/VAR_057478|||http://purl.uniprot.org/annotation/VAR_057479|||http://purl.uniprot.org/annotation/VAR_070086|||http://purl.uniprot.org/annotation/VAR_070087|||http://purl.uniprot.org/annotation/VAR_070088|||http://purl.uniprot.org/annotation/VAR_070089|||http://purl.uniprot.org/annotation/VAR_072084|||http://purl.uniprot.org/annotation/VAR_072085|||http://purl.uniprot.org/annotation/VAR_072086|||http://purl.uniprot.org/annotation/VAR_072087|||http://purl.uniprot.org/annotation/VSP_056341|||http://purl.uniprot.org/annotation/VSP_056342
http://togogenome.org/gene/9606:ZNF774                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NX45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 774                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263653|||http://purl.uniprot.org/annotation/VAR_029596|||http://purl.uniprot.org/annotation/VAR_029597|||http://purl.uniprot.org/annotation/VAR_029598
http://togogenome.org/gene/9606:LAMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13753                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Domain II and I|||In isoform Short.|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4; first part|||Laminin EGF-like 4; second part|||Laminin EGF-like 5|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8; truncated|||Laminin IV type A|||Laminin subunit gamma-2|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017077|||http://purl.uniprot.org/annotation/VAR_020304|||http://purl.uniprot.org/annotation/VAR_022017|||http://purl.uniprot.org/annotation/VAR_050081|||http://purl.uniprot.org/annotation/VAR_050082|||http://purl.uniprot.org/annotation/VAR_050083|||http://purl.uniprot.org/annotation/VAR_050084|||http://purl.uniprot.org/annotation/VAR_050085|||http://purl.uniprot.org/annotation/VSP_003040
http://togogenome.org/gene/9606:RPA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13156                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||OB|||Replication protein A 30 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097280|||http://purl.uniprot.org/annotation/VAR_019170
http://togogenome.org/gene/9606:DFFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZS0|||http://purl.uniprot.org/uniprot/O76075|||http://purl.uniprot.org/uniprot/Q96P72|||http://purl.uniprot.org/uniprot/Q96P73|||http://purl.uniprot.org/uniprot/Q96P74                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CIDE-N|||DNA fragmentation factor subunit beta|||In isoform Beta.|||In isoform Delta.|||In isoform Gamma.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144713|||http://purl.uniprot.org/annotation/VAR_009305|||http://purl.uniprot.org/annotation/VAR_048737|||http://purl.uniprot.org/annotation/VSP_001080|||http://purl.uniprot.org/annotation/VSP_001081|||http://purl.uniprot.org/annotation/VSP_001082|||http://purl.uniprot.org/annotation/VSP_001083|||http://purl.uniprot.org/annotation/VSP_001084
http://togogenome.org/gene/9606:PDPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15530                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-fold increase in kinase activity.|||3-phosphoinositide-dependent protein kinase 1|||Abolishes phosphorylation by MAP3K5; when associated with A-394.|||Abolishes phosphorylation by MAP3K5; when associated with A-398.|||Abolishes phosphorylation by MELK.|||Disordered|||Enhanced kinase activity towards PKB.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||No PDGF-dependent translocation to the membrane.|||No activation.|||No effect.|||PH|||PIF-pocket|||Phosphoserine|||Phosphoserine; by MAP3K5|||Phosphoserine; by PKC/PRKCQ|||Phosphoserine; by autocatalysis|||Phosphothreonine; by MELK|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SRC and INSR|||Polar residues|||Protein kinase|||Proton acceptor|||Reduction in basal activity.|||Slight reduction in pervanadate-stimulated tyrosine phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086500|||http://purl.uniprot.org/annotation/VSP_004894|||http://purl.uniprot.org/annotation/VSP_004895|||http://purl.uniprot.org/annotation/VSP_041902|||http://purl.uniprot.org/annotation/VSP_044796
http://togogenome.org/gene/9606:BUB1B-PAK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQU5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with F-566.|||CRIB|||Complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with A-165.|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||In isoform 2.|||Linker|||Phosphoserine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086476|||http://purl.uniprot.org/annotation/VAR_019993|||http://purl.uniprot.org/annotation/VAR_019994|||http://purl.uniprot.org/annotation/VAR_019995|||http://purl.uniprot.org/annotation/VAR_035631|||http://purl.uniprot.org/annotation/VAR_040972|||http://purl.uniprot.org/annotation/VAR_040973|||http://purl.uniprot.org/annotation/VAR_040974|||http://purl.uniprot.org/annotation/VAR_040975|||http://purl.uniprot.org/annotation/VAR_040976|||http://purl.uniprot.org/annotation/VAR_040977|||http://purl.uniprot.org/annotation/VAR_051655|||http://purl.uniprot.org/annotation/VAR_051656|||http://purl.uniprot.org/annotation/VAR_051657|||http://purl.uniprot.org/annotation/VSP_056733
http://togogenome.org/gene/9606:GABRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18505|||http://purl.uniprot.org/uniprot/X5DNL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in 1.1% of population and in some schizophrenic patients.|||Gamma-aminobutyric acid receptor subunit beta-1|||Helical|||In DEE45.|||In DEE45; no effect on localization to the plasma membrane; increased GABA-gated chloride ion channel activity; increased single channel burst duration.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000456|||http://purl.uniprot.org/annotation/PRO_5022269976|||http://purl.uniprot.org/annotation/VAR_000302|||http://purl.uniprot.org/annotation/VAR_035441|||http://purl.uniprot.org/annotation/VAR_077104|||http://purl.uniprot.org/annotation/VAR_077105|||http://purl.uniprot.org/annotation/VSP_055900|||http://purl.uniprot.org/annotation/VSP_055901
http://togogenome.org/gene/9606:KRTAP19-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4W3                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 19-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223905
http://togogenome.org/gene/9606:PPFIA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J8YUZ5|||http://purl.uniprot.org/uniprot/B3KN22|||http://purl.uniprot.org/uniprot/B4DIS5|||http://purl.uniprot.org/uniprot/O75335                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 2.|||In isoform 2.|||Liprin-alpha-4|||Phosphoserine|||Polar residues|||Pro residues|||SAM|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191032|||http://purl.uniprot.org/annotation/VSP_053668|||http://purl.uniprot.org/annotation/VSP_053669|||http://purl.uniprot.org/annotation/VSP_053670
http://togogenome.org/gene/9606:ACVR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27037                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Activin receptor type-2A|||Cytoplasmic|||Extracellular|||Found in a clear cell renal carcinoma case; somatic mutation.|||Helical|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024398|||http://purl.uniprot.org/annotation/VAR_032809|||http://purl.uniprot.org/annotation/VAR_032810|||http://purl.uniprot.org/annotation/VAR_064692|||http://purl.uniprot.org/annotation/VSP_054689
http://togogenome.org/gene/9606:SKIC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YL19|||http://purl.uniprot.org/uniprot/Q9GZS3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmethionine|||N-acetylthreonine; in WD repeat-containing protein 61, N-terminally processed|||Removed; alternate|||Superkiller complex protein 8|||Superkiller complex protein 8, N-terminally processed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245851|||http://purl.uniprot.org/annotation/PRO_0000425748
http://togogenome.org/gene/9606:ITGA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13797|||http://purl.uniprot.org/uniprot/Q8N6H6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In a breast cancer sample; somatic mutation.|||Integrin alpha-2|||Integrin alpha-9|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016316|||http://purl.uniprot.org/annotation/PRO_5001426252|||http://purl.uniprot.org/annotation/VAR_036073|||http://purl.uniprot.org/annotation/VAR_055091
http://togogenome.org/gene/9606:PI15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43692                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Peptidase inhibitor 15|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287622|||http://purl.uniprot.org/annotation/PRO_0000287623
http://togogenome.org/gene/9606:MBD3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHZ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Interacts with MBD3|||Methyl-CpG-binding domain protein 3-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096253
http://togogenome.org/gene/9606:PRKACG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22612                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||In BDPLT19; patient platelets show impaired activation.|||N-myristoyl glycine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Removed|||cAMP-dependent protein kinase catalytic subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086064|||http://purl.uniprot.org/annotation/VAR_033902|||http://purl.uniprot.org/annotation/VAR_040595|||http://purl.uniprot.org/annotation/VAR_072672
http://togogenome.org/gene/9606:CLTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09497                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Clathrin light chain B|||Disordered|||In isoform Non-brain.|||Involved in binding clathrin heavy chain|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205771|||http://purl.uniprot.org/annotation/VSP_001098
http://togogenome.org/gene/9606:MYH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35579                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||In DFNA17.|||In DFNA17; unknown pathological significance.|||In MATINS.|||In MATINS; likely benign variant.|||In MATINS; results in reduced protein levels.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Mediates interaction with LIMCH1|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-9|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123416|||http://purl.uniprot.org/annotation/VAR_010791|||http://purl.uniprot.org/annotation/VAR_010792|||http://purl.uniprot.org/annotation/VAR_010793|||http://purl.uniprot.org/annotation/VAR_010794|||http://purl.uniprot.org/annotation/VAR_010795|||http://purl.uniprot.org/annotation/VAR_010796|||http://purl.uniprot.org/annotation/VAR_010797|||http://purl.uniprot.org/annotation/VAR_018308|||http://purl.uniprot.org/annotation/VAR_018309|||http://purl.uniprot.org/annotation/VAR_018310|||http://purl.uniprot.org/annotation/VAR_018311|||http://purl.uniprot.org/annotation/VAR_018312|||http://purl.uniprot.org/annotation/VAR_018313|||http://purl.uniprot.org/annotation/VAR_018314|||http://purl.uniprot.org/annotation/VAR_018315|||http://purl.uniprot.org/annotation/VAR_018316|||http://purl.uniprot.org/annotation/VAR_018317|||http://purl.uniprot.org/annotation/VAR_018318|||http://purl.uniprot.org/annotation/VAR_030385|||http://purl.uniprot.org/annotation/VAR_036006|||http://purl.uniprot.org/annotation/VAR_044226|||http://purl.uniprot.org/annotation/VAR_044227|||http://purl.uniprot.org/annotation/VAR_044228|||http://purl.uniprot.org/annotation/VAR_083825|||http://purl.uniprot.org/annotation/VSP_035409|||http://purl.uniprot.org/annotation/VSP_035410
http://togogenome.org/gene/9606:HPS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BLOC-2 complex member HPS5|||Basic and acidic residues|||Disordered|||In HPS5.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084054|||http://purl.uniprot.org/annotation/VAR_015513|||http://purl.uniprot.org/annotation/VAR_062285|||http://purl.uniprot.org/annotation/VAR_062286|||http://purl.uniprot.org/annotation/VSP_007035
http://togogenome.org/gene/9606:VWA3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3D8|||http://purl.uniprot.org/uniprot/Q502W6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SCAR22.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Polar residues|||VWFA|||von Willebrand factor A domain-containing protein 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337040|||http://purl.uniprot.org/annotation/VAR_043571|||http://purl.uniprot.org/annotation/VAR_043572|||http://purl.uniprot.org/annotation/VAR_043573|||http://purl.uniprot.org/annotation/VAR_043574|||http://purl.uniprot.org/annotation/VAR_043575|||http://purl.uniprot.org/annotation/VAR_043576|||http://purl.uniprot.org/annotation/VAR_057022|||http://purl.uniprot.org/annotation/VAR_075091|||http://purl.uniprot.org/annotation/VAR_076433|||http://purl.uniprot.org/annotation/VSP_033834|||http://purl.uniprot.org/annotation/VSP_033835|||http://purl.uniprot.org/annotation/VSP_033836|||http://purl.uniprot.org/annotation/VSP_033837|||http://purl.uniprot.org/annotation/VSP_033838|||http://purl.uniprot.org/annotation/VSP_033839|||http://purl.uniprot.org/annotation/VSP_033840|||http://purl.uniprot.org/annotation/VSP_033841|||http://purl.uniprot.org/annotation/VSP_033842|||http://purl.uniprot.org/annotation/VSP_033843|||http://purl.uniprot.org/annotation/VSP_033844
http://togogenome.org/gene/9606:WASHC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X256|||http://purl.uniprot.org/uniprot/B7ZKT9|||http://purl.uniprot.org/uniprot/Q2M389                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MRT43; reduced expression of the protein; alters the WASH complex.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||Sufficient for interaction with WASHC5|||WASH complex subunit 4|||WASH complex subunit 4 N-terminal|||WASH complex subunit 7 C-terminal|||WASH complex subunit 7 central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282575|||http://purl.uniprot.org/annotation/VAR_031417|||http://purl.uniprot.org/annotation/VAR_031418|||http://purl.uniprot.org/annotation/VAR_057825|||http://purl.uniprot.org/annotation/VAR_071384|||http://purl.uniprot.org/annotation/VSP_024208|||http://purl.uniprot.org/annotation/VSP_024209
http://togogenome.org/gene/9606:DDX60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3G9HN97|||http://purl.uniprot.org/uniprot/Q6B0F7|||http://purl.uniprot.org/uniprot/Q8IY21                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DEVH box|||Helicase ATP-binding|||Helicase C-terminal|||Probable ATP-dependent RNA helicase DDX60                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318154|||http://purl.uniprot.org/annotation/VAR_055895|||http://purl.uniprot.org/annotation/VAR_055896
http://togogenome.org/gene/9606:FBXO11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HK63|||http://purl.uniprot.org/uniprot/Q86XK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 11|||Found in a lymphoma cell line; diminishes ubiquitin-mediated degradation of BCL6.|||Found in a patient with lymphoma.|||Found in a patient with lymphoma; almost abolishes ubiquitin-mediated degradation of BCL6.|||Found in a patient with lymphoma; strongly diminishes ubiquitin-mediated degradation of BCL6.|||Found in a patient with severe intellectual disability and muscular hypotonia; unknown pathological significance.|||Greatly reduced ability to bind PRDM1 and reduced proteolysis of PRDM1.|||In IDDFBA.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PbH1 1|||PbH1 10|||PbH1 11|||PbH1 12|||PbH1 13|||PbH1 14|||PbH1 15|||PbH1 16|||PbH1 17|||PbH1 18|||PbH1 19|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||PbH1 6|||PbH1 7|||PbH1 8|||PbH1 9|||Polar residues|||Pro residues|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273574|||http://purl.uniprot.org/annotation/VAR_024441|||http://purl.uniprot.org/annotation/VAR_070073|||http://purl.uniprot.org/annotation/VAR_070074|||http://purl.uniprot.org/annotation/VAR_070075|||http://purl.uniprot.org/annotation/VAR_070076|||http://purl.uniprot.org/annotation/VAR_070077|||http://purl.uniprot.org/annotation/VAR_081341|||http://purl.uniprot.org/annotation/VAR_081342|||http://purl.uniprot.org/annotation/VAR_081343|||http://purl.uniprot.org/annotation/VAR_081344|||http://purl.uniprot.org/annotation/VAR_081345|||http://purl.uniprot.org/annotation/VAR_081346|||http://purl.uniprot.org/annotation/VAR_081347|||http://purl.uniprot.org/annotation/VAR_081348|||http://purl.uniprot.org/annotation/VAR_081349|||http://purl.uniprot.org/annotation/VAR_081350|||http://purl.uniprot.org/annotation/VAR_081351|||http://purl.uniprot.org/annotation/VAR_081352|||http://purl.uniprot.org/annotation/VAR_081353|||http://purl.uniprot.org/annotation/VSP_008860|||http://purl.uniprot.org/annotation/VSP_008861|||http://purl.uniprot.org/annotation/VSP_008862|||http://purl.uniprot.org/annotation/VSP_008863|||http://purl.uniprot.org/annotation/VSP_008864|||http://purl.uniprot.org/annotation/VSP_008865|||http://purl.uniprot.org/annotation/VSP_022573|||http://purl.uniprot.org/annotation/VSP_022574
http://togogenome.org/gene/9606:DPPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6W0C5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Developmental pluripotency-associated protein 3|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239265|||http://purl.uniprot.org/annotation/VAR_030533
http://togogenome.org/gene/9606:AMELY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99218                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Amelogenin, Y isoform|||Disordered|||In isoform 1.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001200|||http://purl.uniprot.org/annotation/VSP_017077
http://togogenome.org/gene/9606:HEY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TF93|||http://purl.uniprot.org/uniprot/Q9UBP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  BHLH|||Disordered|||Hairy/enhancer-of-split related with YRPW motif protein 2|||Impairs transcriptional repression.|||In a patient with atrioventricular septal defects.|||Orange|||Polar residues|||Transcriptional repression and interaction with NCOR1 and SIN3A|||YRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245515|||http://purl.uniprot.org/annotation/VAR_026974|||http://purl.uniprot.org/annotation/VAR_026975|||http://purl.uniprot.org/annotation/VAR_026976|||http://purl.uniprot.org/annotation/VAR_026977
http://togogenome.org/gene/9606:OAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04181                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decreased protein abundance.|||In HOGA.|||In HOGA; decreased protein abundance.|||In HOGA; loss of protein stability; loss of ornithine aminotransferase activity.|||In HOGA; loss of protein stability; loss of ornithine aminotransferase activityx.|||In HOGA; may affect protein stability; loss of ornithine aminotransferase activity.|||In HOGA; mistargeted, accumulates in cytoplasm.|||In HOGA; no effect on protein abundance.|||In HOGA; no effect on protein abundance; loss of ornithine aminotransferase activity.|||In HOGA; no effect on protein stability; increased ornithine aminotransferase activity.|||In isoform 2.|||Mitochondrion; in hepatic form|||Mitochondrion; in renal form|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Ornithine aminotransferase, hepatic form|||Ornithine aminotransferase, renal form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001262|||http://purl.uniprot.org/annotation/PRO_0000001263|||http://purl.uniprot.org/annotation/VAR_000565|||http://purl.uniprot.org/annotation/VAR_000566|||http://purl.uniprot.org/annotation/VAR_000567|||http://purl.uniprot.org/annotation/VAR_000568|||http://purl.uniprot.org/annotation/VAR_000569|||http://purl.uniprot.org/annotation/VAR_000570|||http://purl.uniprot.org/annotation/VAR_000571|||http://purl.uniprot.org/annotation/VAR_000572|||http://purl.uniprot.org/annotation/VAR_000573|||http://purl.uniprot.org/annotation/VAR_000574|||http://purl.uniprot.org/annotation/VAR_000575|||http://purl.uniprot.org/annotation/VAR_000576|||http://purl.uniprot.org/annotation/VAR_000577|||http://purl.uniprot.org/annotation/VAR_000578|||http://purl.uniprot.org/annotation/VAR_000579|||http://purl.uniprot.org/annotation/VAR_000580|||http://purl.uniprot.org/annotation/VAR_000581|||http://purl.uniprot.org/annotation/VAR_000582|||http://purl.uniprot.org/annotation/VAR_000583|||http://purl.uniprot.org/annotation/VAR_000584|||http://purl.uniprot.org/annotation/VAR_000585|||http://purl.uniprot.org/annotation/VAR_000586|||http://purl.uniprot.org/annotation/VAR_015648|||http://purl.uniprot.org/annotation/VAR_071924|||http://purl.uniprot.org/annotation/VAR_071925|||http://purl.uniprot.org/annotation/VAR_071926|||http://purl.uniprot.org/annotation/VAR_071927|||http://purl.uniprot.org/annotation/VAR_071928|||http://purl.uniprot.org/annotation/VAR_071929|||http://purl.uniprot.org/annotation/VSP_043085
http://togogenome.org/gene/9606:KIF13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1H9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHA|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Kinesin motor|||Kinesin-like protein KIF13A|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125446|||http://purl.uniprot.org/annotation/VAR_029389|||http://purl.uniprot.org/annotation/VAR_049699|||http://purl.uniprot.org/annotation/VSP_002870|||http://purl.uniprot.org/annotation/VSP_021724|||http://purl.uniprot.org/annotation/VSP_021725|||http://purl.uniprot.org/annotation/VSP_021726|||http://purl.uniprot.org/annotation/VSP_045584|||http://purl.uniprot.org/annotation/VSP_045585
http://togogenome.org/gene/9606:SLC44A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A088QCU6|||http://purl.uniprot.org/uniprot/Q8IWA5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Choline transporter-like protein 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191717|||http://purl.uniprot.org/annotation/VAR_023404|||http://purl.uniprot.org/annotation/VSP_015431|||http://purl.uniprot.org/annotation/VSP_041792
http://togogenome.org/gene/9606:FRMD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUT3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FERM|||FERM domain-containing protein 7|||In NYS1.|||In NYS1; decreased RAC1 activity.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259532|||http://purl.uniprot.org/annotation/VAR_028951|||http://purl.uniprot.org/annotation/VAR_028952|||http://purl.uniprot.org/annotation/VAR_028953|||http://purl.uniprot.org/annotation/VAR_028954|||http://purl.uniprot.org/annotation/VAR_028955|||http://purl.uniprot.org/annotation/VAR_028956|||http://purl.uniprot.org/annotation/VAR_028957|||http://purl.uniprot.org/annotation/VAR_028958|||http://purl.uniprot.org/annotation/VAR_028959|||http://purl.uniprot.org/annotation/VAR_028960|||http://purl.uniprot.org/annotation/VAR_028961|||http://purl.uniprot.org/annotation/VAR_028962|||http://purl.uniprot.org/annotation/VAR_062650|||http://purl.uniprot.org/annotation/VAR_062651|||http://purl.uniprot.org/annotation/VAR_062652|||http://purl.uniprot.org/annotation/VAR_062653|||http://purl.uniprot.org/annotation/VAR_062654|||http://purl.uniprot.org/annotation/VAR_062655|||http://purl.uniprot.org/annotation/VAR_062656|||http://purl.uniprot.org/annotation/VAR_062657|||http://purl.uniprot.org/annotation/VAR_062658|||http://purl.uniprot.org/annotation/VAR_062659|||http://purl.uniprot.org/annotation/VAR_062660|||http://purl.uniprot.org/annotation/VAR_072102|||http://purl.uniprot.org/annotation/VAR_072103|||http://purl.uniprot.org/annotation/VAR_072104|||http://purl.uniprot.org/annotation/VAR_072105|||http://purl.uniprot.org/annotation/VAR_072106|||http://purl.uniprot.org/annotation/VSP_038722
http://togogenome.org/gene/9606:MREG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N565                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cholesterol-binding sequence motif|||In isoform 2.|||Melanoregulin|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292175|||http://purl.uniprot.org/annotation/VAR_053923|||http://purl.uniprot.org/annotation/VSP_026387
http://togogenome.org/gene/9606:SEMA3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99985                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032311|||http://purl.uniprot.org/annotation/VAR_020346|||http://purl.uniprot.org/annotation/VAR_051928|||http://purl.uniprot.org/annotation/VSP_055886|||http://purl.uniprot.org/annotation/VSP_055887|||http://purl.uniprot.org/annotation/VSP_055888
http://togogenome.org/gene/9606:NXF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Repeat                                                                                  ^@                                                                                  Has no effect on FG-nucleoporin binding.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||NTF2|||Nuclear RNA export factor 2|||Phosphoserine|||RRM|||Suppresses FG-nucleoporin binding.|||TAP-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220533
http://togogenome.org/gene/9606:MAGEA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43357                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolished recognition by the DCX(DCAF12) complex and ubiquitination.|||Abolishes HLA-A1 binding.|||Disordered|||MAGE|||Melanoma-associated antigen 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156703
http://togogenome.org/gene/9606:GLRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23415|||http://purl.uniprot.org/uniprot/Q14C71                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes potentiation of channel activity by Zn(2+).|||Abolishes sensitivity of channel activity to potentiation or inhibition by Zn(2+); when associated with F-137.|||Abolishes sensitivity of channel activity to potentiation or inhibition by Zn(2+); when associated with K-222.|||Cytoplasmic|||Decreases channel conductance; the mutant channel requires much higher glycine concentrations for activation.|||Disordered|||Extracellular|||Glycine receptor subunit alpha-1|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||In HKPX1.|||In HKPX1; abolishes expression at the cell membrane.|||In HKPX1; abolishes expression at the cell membrane; requires much higher glycine levels for channel activation.|||In HKPX1; decreases unitary channel conductance and requires much higher glycine concentrations for activation.|||In HKPX1; displays leak currents in the absence of glycine due to spontaneous channel opening.|||In HKPX1; high leak currents in the absence of glycine due to spontaneous channel opening.|||In HKPX1; impairs expression at the cell membrane; requires much higher glycine levels for channel activation.|||In HKPX1; requires much higher glycine levels for channel activation and displays an increased rate of desensitization.|||In HKPX1; requires much higher glycine levels for channel activation.|||In HKPX1; strongly increases sensitivity to extracellular glycine; high leak currents in the absence of glycine due to spontaneous channel opening.|||In isoform b.|||Increased single-channel conductance. No effect on glycine sensitivity, but decreased rate of activation.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Strongly decreases potentiation of channel activity by Zn(2+).|||Strongly decreases sensitivity to inhibition by Zn(2+).|||The mutant channel requires much higher glycine concentrations for activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000412|||http://purl.uniprot.org/annotation/VAR_000296|||http://purl.uniprot.org/annotation/VAR_000297|||http://purl.uniprot.org/annotation/VAR_000298|||http://purl.uniprot.org/annotation/VAR_000299|||http://purl.uniprot.org/annotation/VAR_000300|||http://purl.uniprot.org/annotation/VAR_000301|||http://purl.uniprot.org/annotation/VAR_010112|||http://purl.uniprot.org/annotation/VAR_010113|||http://purl.uniprot.org/annotation/VAR_010114|||http://purl.uniprot.org/annotation/VAR_075418|||http://purl.uniprot.org/annotation/VAR_075419|||http://purl.uniprot.org/annotation/VAR_075420|||http://purl.uniprot.org/annotation/VAR_075421|||http://purl.uniprot.org/annotation/VAR_075422|||http://purl.uniprot.org/annotation/VAR_075423|||http://purl.uniprot.org/annotation/VAR_075424|||http://purl.uniprot.org/annotation/VAR_075425|||http://purl.uniprot.org/annotation/VAR_075426|||http://purl.uniprot.org/annotation/VSP_021142
http://togogenome.org/gene/9606:RAB8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61006                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||Loss of interaction with MICALL1.|||Loss of phosphorylation. No effect on the binding of GDP or GTP. Localizes primarily to the Golgi complex but does not affect membrane localization.|||Phosphomimetic mutant. No effect on the binding of GDP or GTP. Loss of GDI1, GDI2, CHM, CHML, RABGGTA, RABGGTB, RAB3IP, TBC1D15, and INPP5B binding. Increases localization to the cell membrane.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Probable constitutively active mutant locked in the active GTP-bound form. Stimulates interaction with MICALL1.|||Ras-related protein Rab-8A|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121130|||http://purl.uniprot.org/annotation/PRO_0000370793|||http://purl.uniprot.org/annotation/VSP_056399
http://togogenome.org/gene/9606:RHCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1L3H056|||http://purl.uniprot.org/uniprot/A0A220QMN8|||http://purl.uniprot.org/uniprot/P18577                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ammonium transporter AmtB-like|||Associated with altered expression of E antigen.|||Blood group Rh(CE) polypeptide|||Found in antigen RhEFM.|||Found in antigen RhEKH.|||Helical|||In C(W)/Rh8 antigen.|||In C(X)/Rh9 antigen.|||In C/Rh2 antigen.|||In E/Rh5 antigen.|||In VS antigen.|||In isoform 1d.|||In isoform 1h.|||In isoform 2e.|||In isoform 4g.|||In isoform 8a.|||In isoform 8e.|||In isoform 8h.|||In isoform RHIV.|||In isoform RHVI and isoform 1c.|||In isoform RHVI and isoform 7a.|||In isoform RHVIII.|||In isoform RhPI-Alpha.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168189|||http://purl.uniprot.org/annotation/VAR_006911|||http://purl.uniprot.org/annotation/VAR_006912|||http://purl.uniprot.org/annotation/VAR_006913|||http://purl.uniprot.org/annotation/VAR_006914|||http://purl.uniprot.org/annotation/VAR_006915|||http://purl.uniprot.org/annotation/VAR_006916|||http://purl.uniprot.org/annotation/VAR_006917|||http://purl.uniprot.org/annotation/VAR_006918|||http://purl.uniprot.org/annotation/VAR_013301|||http://purl.uniprot.org/annotation/VAR_013302|||http://purl.uniprot.org/annotation/VAR_013303|||http://purl.uniprot.org/annotation/VAR_055260|||http://purl.uniprot.org/annotation/VAR_055261|||http://purl.uniprot.org/annotation/VAR_055262|||http://purl.uniprot.org/annotation/VAR_055263|||http://purl.uniprot.org/annotation/VAR_055264|||http://purl.uniprot.org/annotation/VAR_055265|||http://purl.uniprot.org/annotation/VAR_055266|||http://purl.uniprot.org/annotation/VAR_055267|||http://purl.uniprot.org/annotation/VAR_055268|||http://purl.uniprot.org/annotation/VAR_055269|||http://purl.uniprot.org/annotation/VAR_057987|||http://purl.uniprot.org/annotation/VAR_057988|||http://purl.uniprot.org/annotation/VAR_057989|||http://purl.uniprot.org/annotation/VSP_005701|||http://purl.uniprot.org/annotation/VSP_005702|||http://purl.uniprot.org/annotation/VSP_005703|||http://purl.uniprot.org/annotation/VSP_005704|||http://purl.uniprot.org/annotation/VSP_005705|||http://purl.uniprot.org/annotation/VSP_037505|||http://purl.uniprot.org/annotation/VSP_037506|||http://purl.uniprot.org/annotation/VSP_037507|||http://purl.uniprot.org/annotation/VSP_037508|||http://purl.uniprot.org/annotation/VSP_037509|||http://purl.uniprot.org/annotation/VSP_037510|||http://purl.uniprot.org/annotation/VSP_037511|||http://purl.uniprot.org/annotation/VSP_037512|||http://purl.uniprot.org/annotation/VSP_037513|||http://purl.uniprot.org/annotation/VSP_037514|||http://purl.uniprot.org/annotation/VSP_038405|||http://purl.uniprot.org/annotation/VSP_038406
http://togogenome.org/gene/9606:ARMCX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH62                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||Armadillo repeat-containing X-linked protein 3|||Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191366
http://togogenome.org/gene/9606:FSCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEG1|||http://purl.uniprot.org/uniprot/B3KTA3|||http://purl.uniprot.org/uniprot/Q16658                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes axon growth cone collapse in response to NGF.|||Decreased actin-binding and actin-bundling activity; when associated with E-271 and E-353.|||Decreased actin-binding and actin-bundling activity; when associated with E-271 and E-358.|||Decreased actin-binding and actin-bundling activity; when associated with E-353 and E-358.|||Decreased actin-binding and loss of actin-bundling activity; when associated with E-22 and E-398. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-100 and E-109.|||Decreased actin-binding and loss of actin-bundling activity; when associated with E-22 and E-43.|||Decreased actin-binding and loss of actin-bundling activity; when associated with E-43 and E-398. Decreased actin-binding and loss of actin-bundling activity; when associated with E-43; E-100 and E-109.|||Decreased actin-bundling activity.|||Decreases actin-bundling activity.|||Fascin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of phosphorylation.|||Mildly decreased actin-binding and actin-bundling activity; when associated with E-100 and E-109.|||Mildly decreased actin-binding and actin-bundling activity; when associated with E-100 and E-247. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-43 and E-100.|||Mildly decreased actin-binding and actin-bundling activity; when associated with E-109 and E-247. Decreased actin-binding and loss of actin-bundling activity; when associated with E-22; E-43 and E-109.|||N-acetylthreonine|||N6-acetyllysine|||No significant effect on actin-binding and actin-bundling activity; when associated with 150-E-E-151.|||No significant effect on actin-binding and actin-bundling activity; when associated with E-313.|||No significant effect on actin-binding and actin-bundling activity; when associated with E-341 and E-348.|||No significant effect on actin-binding and actin-bundling activity; when associated with E-341 and Q-464.|||No significant effect on actin-binding and actin-bundling activity; when associated with E-348 and Q-464.|||Phosphomimetic mutant that strongly decreases actin-bundling activity.|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Removed|||Strongly decreases actin-bundling activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219379
http://togogenome.org/gene/9606:LCN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDV4|||http://purl.uniprot.org/uniprot/Q6JVE5|||http://purl.uniprot.org/uniprot/Q8IW14                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Epididymal-specific lipocalin-12|||Lipocalin/cytosolic fatty-acid binding|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017922|||http://purl.uniprot.org/annotation/PRO_5014312161|||http://purl.uniprot.org/annotation/PRO_5017285723
http://togogenome.org/gene/9606:AGT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0ZBE2|||http://purl.uniprot.org/uniprot/B2R5S1|||http://purl.uniprot.org/uniprot/P01019                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Angiotensin 1-4|||Angiotensin 1-5|||Angiotensin 1-7|||Angiotensin 1-9|||Angiotensin-1|||Angiotensin-2|||Angiotensin-3|||Angiotensin-4|||Angiotensinogen|||Associated with essential hypertension and pre-eclampsia.|||Associated with hypertension.|||Associated with susceptibility to hypertension.|||Associated with susceptibility to hypertension; alters the structure, glycosylation and secretion of angiotensinogen.|||Associated with susceptibility to pre-eclampsia; alters the reactions with renin and angiotensin-converting enzyme.|||Beta-decarboxylated aspartate; in form angiotensin-A|||In RTD.|||N-linked (GlcNAc...) asparagine|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032456|||http://purl.uniprot.org/annotation/PRO_0000032457|||http://purl.uniprot.org/annotation/PRO_0000032458|||http://purl.uniprot.org/annotation/PRO_0000032459|||http://purl.uniprot.org/annotation/PRO_0000420659|||http://purl.uniprot.org/annotation/PRO_0000420660|||http://purl.uniprot.org/annotation/PRO_0000420661|||http://purl.uniprot.org/annotation/PRO_0000420662|||http://purl.uniprot.org/annotation/PRO_0000420663|||http://purl.uniprot.org/annotation/PRO_5002781493|||http://purl.uniprot.org/annotation/PRO_5014298172|||http://purl.uniprot.org/annotation/VAR_007093|||http://purl.uniprot.org/annotation/VAR_007094|||http://purl.uniprot.org/annotation/VAR_007095|||http://purl.uniprot.org/annotation/VAR_007096|||http://purl.uniprot.org/annotation/VAR_007097|||http://purl.uniprot.org/annotation/VAR_014573|||http://purl.uniprot.org/annotation/VAR_022933|||http://purl.uniprot.org/annotation/VAR_029166|||http://purl.uniprot.org/annotation/VAR_029167|||http://purl.uniprot.org/annotation/VAR_035431|||http://purl.uniprot.org/annotation/VAR_035432|||http://purl.uniprot.org/annotation/VAR_035433|||http://purl.uniprot.org/annotation/VAR_051939
http://togogenome.org/gene/9606:OTOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Proton channel OTOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313816|||http://purl.uniprot.org/annotation/VAR_037755|||http://purl.uniprot.org/annotation/VAR_037756|||http://purl.uniprot.org/annotation/VAR_037757|||http://purl.uniprot.org/annotation/VAR_037758|||http://purl.uniprot.org/annotation/VAR_037759
http://togogenome.org/gene/9606:PPP1R9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1I0|||http://purl.uniprot.org/uniprot/B7ZLX4|||http://purl.uniprot.org/uniprot/Q9ULJ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Actin-binding|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with TGN38|||Interaction with protein phosphatase 1|||Neurabin-1|||PDZ|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071507|||http://purl.uniprot.org/annotation/VAR_051746|||http://purl.uniprot.org/annotation/VSP_005121|||http://purl.uniprot.org/annotation/VSP_011139|||http://purl.uniprot.org/annotation/VSP_044469|||http://purl.uniprot.org/annotation/VSP_044470|||http://purl.uniprot.org/annotation/VSP_044471|||http://purl.uniprot.org/annotation/VSP_053808
http://togogenome.org/gene/9606:MT1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04732                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Alpha|||Beta|||In isoform 2.|||Metallothionein-1E|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197236|||http://purl.uniprot.org/annotation/VSP_041603
http://togogenome.org/gene/9606:DNAJC28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 28|||J|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071139
http://togogenome.org/gene/9606:PITPNC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic phosphatidylinositol transfer protein 1|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287530|||http://purl.uniprot.org/annotation/VSP_025545
http://togogenome.org/gene/9606:UBL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||UBA|||Ubiquitin-like|||Ubiquitin-like protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211021
http://togogenome.org/gene/9606:BAIAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQB8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E146.|||Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E147.|||Abolishes actin-bundling and filopodia formation; when associated with E-142; E-146 and E147.|||Abolishes actin-bundling and filopodia formation; when associated with E-143; E-146 and E147.|||Brain-specific angiogenesis inhibitor 1-associated protein 2|||Disordered|||IMD|||Impairs the SH3 domain and abolishes the interaction with EPS8.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||Loss of interaction with CDC42. Loss of stimulation of neurite growth.|||Loss of interaction with ENAH and no induction of filopodia; when associated with A-427.|||Loss of interaction with ENAH and no induction of filopodia; when associated with A-428.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064816|||http://purl.uniprot.org/annotation/VAR_050686|||http://purl.uniprot.org/annotation/VSP_015502|||http://purl.uniprot.org/annotation/VSP_015503|||http://purl.uniprot.org/annotation/VSP_015504|||http://purl.uniprot.org/annotation/VSP_015505|||http://purl.uniprot.org/annotation/VSP_015506
http://togogenome.org/gene/9606:ZNF304                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EQD3|||http://purl.uniprot.org/uniprot/M0QZ59|||http://purl.uniprot.org/uniprot/Q2T9G7|||http://purl.uniprot.org/uniprot/Q2T9G8|||http://purl.uniprot.org/uniprot/Q9HCX3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 304                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047523|||http://purl.uniprot.org/annotation/VAR_019979|||http://purl.uniprot.org/annotation/VAR_033563
http://togogenome.org/gene/9606:NTS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30990|||http://purl.uniprot.org/uniprot/Q6FH20                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Cleavage; by ACE and MME|||Cleavage; by MME|||Large neuromedin N|||Neuromedin N|||Neurotensin|||Neurotensin/neuromedin N|||Pyrrolidone carboxylic acid|||Tail peptide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019522|||http://purl.uniprot.org/annotation/PRO_0000019523|||http://purl.uniprot.org/annotation/PRO_0000019524|||http://purl.uniprot.org/annotation/PRO_0000019525|||http://purl.uniprot.org/annotation/PRO_5014310431
http://togogenome.org/gene/9606:KCNMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZL8|||http://purl.uniprot.org/uniprot/A0A1W2PP94|||http://purl.uniprot.org/uniprot/A0A1W2PPY5|||http://purl.uniprot.org/uniprot/A0A1W2PQK5|||http://purl.uniprot.org/uniprot/A0A1W2PQU4|||http://purl.uniprot.org/uniprot/A0A1W2PR56|||http://purl.uniprot.org/uniprot/A0A1W2PR62|||http://purl.uniprot.org/uniprot/A0A1W2PRN5|||http://purl.uniprot.org/uniprot/B7ZMF5|||http://purl.uniprot.org/uniprot/D5MRH1|||http://purl.uniprot.org/uniprot/Q12791|||http://purl.uniprot.org/uniprot/Q59FH2|||http://purl.uniprot.org/uniprot/Q5SVJ7|||http://purl.uniprot.org/uniprot/S4R453                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activated at more negative voltages. No effect on inhibition by HMIMP.|||Activated at more negative voltages. Slower rate of inactivation. Impaired inhibition by HMIMP. No effect on channel inhibition by Iberiotoxin.|||Basic and acidic residues|||Calcium bowl|||Calcium-activated potassium channel BK alpha subunit|||Calcium-activated potassium channel subunit alpha-1|||Cytoplasmic|||Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-118 and A-121.|||Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-119 and A-121.|||Disordered|||Extracellular|||Found in a patient with epilepsy; unknown pathological significance; no effect on voltage-dependent sensitivity.|||Found in a patient with epileptic encephalopathy; unknown pathological significance; no effect on voltage-dependent sensitivity.|||Found in patient with epilepsy; unknown pathological significance.|||Helical|||Helical; Name=Segment S0|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Heme-binding motif|||In CADEDS.|||In LIWAS; loss of voltage-gated potassium channel activity.|||In PNKD3 and EIG16; increased sensitivity to voltage-dependent activation resulting in increased channel activity; no change in calcium sensitivity.|||In PNKD3.|||In PNKD3; may have a synergistic effect with ethanol in the triggering of symptoms.|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Induces reduction in the coupling between calcium and channel opening.|||Ion transport|||Loss of function.|||Loss of heme-induced channel inhibition.|||No effect in the coupling between calcium and channel opening.|||No effect on activation voltage. No effect on inhibition by HMIMP.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pore-forming; Name=P region|||RCK N-terminal|||S-palmitoyl cysteine|||Segment S10|||Segment S7|||Segment S8|||Segment S9|||Selectivity for potassium                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054132|||http://purl.uniprot.org/annotation/VAR_023821|||http://purl.uniprot.org/annotation/VAR_079156|||http://purl.uniprot.org/annotation/VAR_079157|||http://purl.uniprot.org/annotation/VAR_083204|||http://purl.uniprot.org/annotation/VAR_083205|||http://purl.uniprot.org/annotation/VAR_083206|||http://purl.uniprot.org/annotation/VAR_083554|||http://purl.uniprot.org/annotation/VAR_083555|||http://purl.uniprot.org/annotation/VSP_009952|||http://purl.uniprot.org/annotation/VSP_009953|||http://purl.uniprot.org/annotation/VSP_009954|||http://purl.uniprot.org/annotation/VSP_009955|||http://purl.uniprot.org/annotation/VSP_009956|||http://purl.uniprot.org/annotation/VSP_009957|||http://purl.uniprot.org/annotation/VSP_009958
http://togogenome.org/gene/9606:MFSD14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SR56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Hippocampus abundant transcript-like protein 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239229|||http://purl.uniprot.org/annotation/VAR_055401|||http://purl.uniprot.org/annotation/VSP_056692|||http://purl.uniprot.org/annotation/VSP_056693|||http://purl.uniprot.org/annotation/VSP_056694
http://togogenome.org/gene/9606:LYZL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YUZ5|||http://purl.uniprot.org/uniprot/Q96KX0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||Lysozyme-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240638|||http://purl.uniprot.org/annotation/PRO_5014217360
http://togogenome.org/gene/9606:SPRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BIV9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Shadow of prion protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320166|||http://purl.uniprot.org/annotation/PRO_5000096015|||http://purl.uniprot.org/annotation/VAR_039152
http://togogenome.org/gene/9606:DHRS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWP2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 11|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045490|||http://purl.uniprot.org/annotation/VSP_016987|||http://purl.uniprot.org/annotation/VSP_059104
http://togogenome.org/gene/9606:ANXA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07355                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes heat stress-induced cell surface localization.|||Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A2|||Decreases interaction with PCSK9. Strongly decreases interaction with PCSK9; when associated with K-88.|||Does not affect interaction with PCSK9.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on interaction with PCSK9.|||Phosphoserine|||Phosphoserine; by PKC|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Removed|||S100A10-binding site|||Slightly decreases interaction with PCSK9.|||Stronger interaction with S100A4.|||Strongly decreases interaction with PCSK9.|||Strongly decreases interaction with PCSK9; when associated with 77-A--A-80.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067470|||http://purl.uniprot.org/annotation/VAR_012982|||http://purl.uniprot.org/annotation/VSP_038091
http://togogenome.org/gene/9606:SIGLECL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLS6|||http://purl.uniprot.org/uniprot/Q8N7X8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||SIGLEC family-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332128
http://togogenome.org/gene/9606:PCBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57723                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||KH 1|||KH 2|||KH 3|||Poly(rC)-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050094|||http://purl.uniprot.org/annotation/VAR_049681|||http://purl.uniprot.org/annotation/VSP_010016
http://togogenome.org/gene/9606:LRRC75A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZMA3|||http://purl.uniprot.org/uniprot/Q8NAA5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 75A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286624|||http://purl.uniprot.org/annotation/VSP_025134|||http://purl.uniprot.org/annotation/VSP_025135
http://togogenome.org/gene/9606:STBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95210                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes GYS2- and glycogen-binding, and leads to rapid degradation.|||Abolishes interaction with GABARAPL1.|||CBM20|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LIR|||Phosphoserine|||Polar residues|||Starch-binding domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087476
http://togogenome.org/gene/9606:BOLA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3K6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  BolA-like protein 2|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201236|||http://purl.uniprot.org/annotation/VSP_010092|||http://purl.uniprot.org/annotation/VSP_010093
http://togogenome.org/gene/9606:GFOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B7J2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Glucose-fructose oxidoreductase domain-containing protein 2|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282972|||http://purl.uniprot.org/annotation/VAR_054433|||http://purl.uniprot.org/annotation/VSP_024262|||http://purl.uniprot.org/annotation/VSP_055185|||http://purl.uniprot.org/annotation/VSP_055186
http://togogenome.org/gene/9606:AKIRIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53H80|||http://purl.uniprot.org/uniprot/Q9NW35                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolished association with the 20S and 26S proteasomes.|||Akirin-2|||Disordered|||Nuclear localization signal|||Phosphoserine|||SYVS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089555
http://togogenome.org/gene/9606:C1orf162                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEQ5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Transmembrane protein C1orf162                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304787|||http://purl.uniprot.org/annotation/VAR_035106|||http://purl.uniprot.org/annotation/VSP_028124
http://togogenome.org/gene/9606:RNF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCQ4|||http://purl.uniprot.org/uniprot/Q99942                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF5|||Helical|||Loss of E3 ubiquitin-protein ligase activity.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240393
http://togogenome.org/gene/9606:HABP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14520                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Cleavage|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Hyaluronan-binding protein 2 27 kDa light chain|||Hyaluronan-binding protein 2 27 kDa light chain alternate form|||Hyaluronan-binding protein 2 50 kDa heavy chain|||Hyaluronan-binding protein 2 50 kDa heavy chain alternate form|||In NMTC5; associated with disease susceptibility; variant Marburg I; could be a prominent risk predictor of carotid stenosis; impairs the pro-urokinase activating potency; increased cell migration and increased cell proliferation; dominant negative effect.|||In isoform 2.|||Interchain (between heavy and light chains)|||Kringle|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Variant Marburg II.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027899|||http://purl.uniprot.org/annotation/PRO_0000027900|||http://purl.uniprot.org/annotation/PRO_0000027901|||http://purl.uniprot.org/annotation/PRO_0000027902|||http://purl.uniprot.org/annotation/VAR_023399|||http://purl.uniprot.org/annotation/VAR_023400|||http://purl.uniprot.org/annotation/VAR_023401|||http://purl.uniprot.org/annotation/VSP_044583
http://togogenome.org/gene/9606:ARTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4W7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Artemin|||Disordered|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240286|||http://purl.uniprot.org/annotation/PRO_0000240287|||http://purl.uniprot.org/annotation/VAR_026718|||http://purl.uniprot.org/annotation/VSP_019335|||http://purl.uniprot.org/annotation/VSP_019336
http://togogenome.org/gene/9606:OR2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGH3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150468|||http://purl.uniprot.org/annotation/VAR_057537|||http://purl.uniprot.org/annotation/VAR_057538|||http://purl.uniprot.org/annotation/VAR_057539
http://togogenome.org/gene/9606:PSCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43653                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Prostate stem cell antigen|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036162|||http://purl.uniprot.org/annotation/PRO_0000036163|||http://purl.uniprot.org/annotation/VAR_020173|||http://purl.uniprot.org/annotation/VAR_080777
http://togogenome.org/gene/9606:TOP6BL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXL1|||http://purl.uniprot.org/uniprot/Q8N6T0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In HYDM4; unknown pathological significance.|||In isoform 1 and isoform 2.|||In isoform 1.|||In isoform 2.|||Polar residues|||Type 2 DNA topoisomerase 6 subunit B-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296622|||http://purl.uniprot.org/annotation/VAR_082606|||http://purl.uniprot.org/annotation/VSP_058330|||http://purl.uniprot.org/annotation/VSP_058331|||http://purl.uniprot.org/annotation/VSP_058332
http://togogenome.org/gene/9606:HK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J753|||http://purl.uniprot.org/uniprot/A8K7J7|||http://purl.uniprot.org/uniprot/B3KXY9|||http://purl.uniprot.org/uniprot/P19367|||http://purl.uniprot.org/uniprot/P78542|||http://purl.uniprot.org/uniprot/Q59FD4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Hexokinase 1|||Hexokinase 2|||Hexokinase C-terminal|||Hexokinase N-terminal|||Hexokinase large subdomain 1|||Hexokinase large subdomain 2|||Hexokinase small subdomain 1|||Hexokinase small subdomain 2|||Hexokinase-1|||In HK deficiency.|||In HK deficiency; HKUtrecht.|||In HMSNR.|||In NEDVIBA.|||In NEDVIBA; no effect on the affinity for glucose or ATP; no effect on thermal stability.|||In RP79; unknown pathological significance; no effect on hexokinase activity; no effect on protein abundance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial-binding peptide (MBP)|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197585|||http://purl.uniprot.org/annotation/VAR_009878|||http://purl.uniprot.org/annotation/VAR_023780|||http://purl.uniprot.org/annotation/VAR_023781|||http://purl.uniprot.org/annotation/VAR_078923|||http://purl.uniprot.org/annotation/VAR_083222|||http://purl.uniprot.org/annotation/VAR_083223|||http://purl.uniprot.org/annotation/VAR_083224|||http://purl.uniprot.org/annotation/VAR_083225|||http://purl.uniprot.org/annotation/VAR_087589|||http://purl.uniprot.org/annotation/VSP_002071|||http://purl.uniprot.org/annotation/VSP_002072|||http://purl.uniprot.org/annotation/VSP_002073
http://togogenome.org/gene/9606:RPUSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ73                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pseudouridylate synthase RPUSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300819|||http://purl.uniprot.org/annotation/VSP_055372
http://togogenome.org/gene/9606:DCAF4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXM0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 4-like protein 1|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288902
http://togogenome.org/gene/9606:VEGFD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43915                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Repeat|||Signal Peptide|||Strand                                                                                  ^@                                                                                  1; approximate|||2|||3|||4|||4 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-C|||Interchain|||N-linked (GlcNAc...) asparagine|||Or 99 (in a minor form)|||Vascular endothelial growth factor D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023408|||http://purl.uniprot.org/annotation/PRO_0000023409|||http://purl.uniprot.org/annotation/PRO_0000023410
http://togogenome.org/gene/9606:EPHA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MU00|||http://purl.uniprot.org/uniprot/B7ZKJ3|||http://purl.uniprot.org/uniprot/B7ZKW7|||http://purl.uniprot.org/uniprot/F8VP57|||http://purl.uniprot.org/uniprot/F8W9W0|||http://purl.uniprot.org/uniprot/P54756|||http://purl.uniprot.org/uniprot/Q59FT4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-A receptor 5|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016812|||http://purl.uniprot.org/annotation/VAR_042138|||http://purl.uniprot.org/annotation/VAR_042139|||http://purl.uniprot.org/annotation/VAR_042140|||http://purl.uniprot.org/annotation/VAR_042141|||http://purl.uniprot.org/annotation/VAR_042142|||http://purl.uniprot.org/annotation/VAR_042143|||http://purl.uniprot.org/annotation/VAR_042144|||http://purl.uniprot.org/annotation/VAR_042145|||http://purl.uniprot.org/annotation/VAR_042146|||http://purl.uniprot.org/annotation/VAR_042147|||http://purl.uniprot.org/annotation/VAR_042148|||http://purl.uniprot.org/annotation/VAR_045912|||http://purl.uniprot.org/annotation/VSP_002999|||http://purl.uniprot.org/annotation/VSP_039118|||http://purl.uniprot.org/annotation/VSP_039119
http://togogenome.org/gene/9606:PICK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRD5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  AH|||Abolishes interaction with GRIA2, but not with PRKCA.|||Abolishes interaction with other proteins, but not with itself.|||Acidic residues|||Disordered|||In isoform 2.|||PDZ|||PRKCA-binding protein|||Phosphothreonine|||S-palmitoyl cysteine; by DHHC8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058427|||http://purl.uniprot.org/annotation/VSP_054902|||http://purl.uniprot.org/annotation/VSP_054903
http://togogenome.org/gene/9606:MC2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01718                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adrenocorticotropic hormone receptor|||Cytoplasmic|||Extracellular|||Found in a glucocorticoid deficiency patient carrying also mutation I-74.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In GCCD1.|||In GCCD1; complete loss of activity.|||In GCCD1; partial loss of ACTIVITY.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069054|||http://purl.uniprot.org/annotation/VAR_003509|||http://purl.uniprot.org/annotation/VAR_003510|||http://purl.uniprot.org/annotation/VAR_003511|||http://purl.uniprot.org/annotation/VAR_003512|||http://purl.uniprot.org/annotation/VAR_003513|||http://purl.uniprot.org/annotation/VAR_010702|||http://purl.uniprot.org/annotation/VAR_010703|||http://purl.uniprot.org/annotation/VAR_015095|||http://purl.uniprot.org/annotation/VAR_015096|||http://purl.uniprot.org/annotation/VAR_015295|||http://purl.uniprot.org/annotation/VAR_049369|||http://purl.uniprot.org/annotation/VAR_064986
http://togogenome.org/gene/9606:SLC9A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXD1|||http://purl.uniprot.org/uniprot/Q96T83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cation/H+ exchanger|||Cytoplasmic|||Disordered|||Helical|||In MRX108; probable gain-of-function variant; affects the regulation of trans-Golgi network/post-Golgi pH homeostasis, causing alkalinization of these compartments compared to wild-type, hence affecting its own glycosylation and that of exported cargo proteins; no effect on subcellular location in the Golgi apparatus and plasma membrane.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Required for trans-Golgi network localization|||Sodium/hydrogen exchanger|||Sodium/hydrogen exchanger 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052363|||http://purl.uniprot.org/annotation/PRO_5001832041|||http://purl.uniprot.org/annotation/VAR_082101
http://togogenome.org/gene/9606:CARD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWT7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CARD|||Caspase recruitment domain-containing protein 10|||Disordered|||In IMD89; unknown pathological significance; decreased protein expression compared to wild type when transfected in HEK293T cells.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144084|||http://purl.uniprot.org/annotation/VAR_028116|||http://purl.uniprot.org/annotation/VAR_086467|||http://purl.uniprot.org/annotation/VSP_055523|||http://purl.uniprot.org/annotation/VSP_055524
http://togogenome.org/gene/9606:VPS35L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT69|||http://purl.uniprot.org/uniprot/Q7Z3J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In RTSC3; does not interact with VPS29.|||In isoform 2.|||Phosphoserine|||Polar residues|||VPS35 endosomal protein-sorting factor-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311352|||http://purl.uniprot.org/annotation/VAR_037230|||http://purl.uniprot.org/annotation/VAR_037231|||http://purl.uniprot.org/annotation/VAR_037232|||http://purl.uniprot.org/annotation/VAR_085197|||http://purl.uniprot.org/annotation/VSP_029536|||http://purl.uniprot.org/annotation/VSP_029537|||http://purl.uniprot.org/annotation/VSP_029538
http://togogenome.org/gene/9606:OR2A42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A1/2A42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150459
http://togogenome.org/gene/9606:SFTPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07988                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  In SMDP1.|||Interchain|||N-linked (GlcNAc...) asparagine|||Pulmonary surfactant-associated protein B|||Requires 2 nucleotide substitutions.|||Saposin A-type|||Saposin B-type 1|||Saposin B-type 2|||Saposin B-type 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031647|||http://purl.uniprot.org/annotation/PRO_0000031648|||http://purl.uniprot.org/annotation/PRO_0000031649|||http://purl.uniprot.org/annotation/VAR_006948|||http://purl.uniprot.org/annotation/VAR_006949|||http://purl.uniprot.org/annotation/VAR_006950|||http://purl.uniprot.org/annotation/VAR_013099|||http://purl.uniprot.org/annotation/VAR_013100|||http://purl.uniprot.org/annotation/VAR_036856
http://togogenome.org/gene/9606:SMIM17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DL12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Small integral membrane protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421255
http://togogenome.org/gene/9606:NPPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5LCN7|||http://purl.uniprot.org/uniprot/P23582                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CNP-22|||CNP-29|||CNP-53|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001553|||http://purl.uniprot.org/annotation/PRO_0000001554|||http://purl.uniprot.org/annotation/PRO_0000001555|||http://purl.uniprot.org/annotation/PRO_0000001556|||http://purl.uniprot.org/annotation/VAR_014583
http://togogenome.org/gene/9606:ANKRD13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS27|||http://purl.uniprot.org/uniprot/Q86YJ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 13B|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Polar residues|||Pro residues|||UIM 1|||UIM 2|||UIM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240643|||http://purl.uniprot.org/annotation/VSP_019404
http://togogenome.org/gene/9606:SUFU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A223LX15|||http://purl.uniprot.org/uniprot/Q9UMX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding.|||Abolishes ubiquitination by the SCF(FBXL17) complex.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-159.|||Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-380.|||Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-159 and R-380.|||In JBTS32; decreased stability; forms cytoplasmic aggregates; decreased interaction with GLI3; no effect on interaction with GLI1; decreased repression of the hedgehog/smoothened signaling pathway.|||In JBTS32; decreased stability; no effect on nuclear and cytoplasmic localization; decreased interaction with GLI3; no effect on interaction with GLI1; decreased repression of the hedgehog/smoothened signaling pathway.|||In isoform 2.|||In isoform 3.|||Increased interaction with FBXL17 and ubiquitination by the SCF(FBXL17) complex.|||N6-acetyllysine|||No effect on down-regulation of GLI1 activity.|||Phosphomimetic mutant; decreased interaction with FBXL17 and ubiquitination by the SCF(FBXL17) complex.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Suppressor of fused C-terminal|||Suppressor of fused homolog|||Suppressor of fused-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072302|||http://purl.uniprot.org/annotation/VAR_021566|||http://purl.uniprot.org/annotation/VAR_021567|||http://purl.uniprot.org/annotation/VAR_080418|||http://purl.uniprot.org/annotation/VAR_080419|||http://purl.uniprot.org/annotation/VAR_080420|||http://purl.uniprot.org/annotation/VAR_080421|||http://purl.uniprot.org/annotation/VAR_080422|||http://purl.uniprot.org/annotation/VAR_080423|||http://purl.uniprot.org/annotation/VAR_080424|||http://purl.uniprot.org/annotation/VAR_080425|||http://purl.uniprot.org/annotation/VAR_080426|||http://purl.uniprot.org/annotation/VAR_080427|||http://purl.uniprot.org/annotation/VAR_080428|||http://purl.uniprot.org/annotation/VSP_013278|||http://purl.uniprot.org/annotation/VSP_013279|||http://purl.uniprot.org/annotation/VSP_013280
http://togogenome.org/gene/9606:TAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWG9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of interaction with TAF10.|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription initiation factor TFIID subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245528|||http://purl.uniprot.org/annotation/VAR_052254|||http://purl.uniprot.org/annotation/VAR_052255|||http://purl.uniprot.org/annotation/VAR_052256|||http://purl.uniprot.org/annotation/VAR_052257
http://togogenome.org/gene/9606:PSG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00889                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014913|||http://purl.uniprot.org/annotation/VAR_011723|||http://purl.uniprot.org/annotation/VAR_011724|||http://purl.uniprot.org/annotation/VAR_011725|||http://purl.uniprot.org/annotation/VAR_011726|||http://purl.uniprot.org/annotation/VAR_011727|||http://purl.uniprot.org/annotation/VAR_011728|||http://purl.uniprot.org/annotation/VAR_011729|||http://purl.uniprot.org/annotation/VAR_011730|||http://purl.uniprot.org/annotation/VAR_011731|||http://purl.uniprot.org/annotation/VAR_011732|||http://purl.uniprot.org/annotation/VAR_011733|||http://purl.uniprot.org/annotation/VAR_011735|||http://purl.uniprot.org/annotation/VAR_049922|||http://purl.uniprot.org/annotation/VAR_049923|||http://purl.uniprot.org/annotation/VAR_061324|||http://purl.uniprot.org/annotation/VSP_039344
http://togogenome.org/gene/9606:NAXD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T9D8|||http://purl.uniprot.org/uniprot/Q8IW45                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent (S)-NAD(P)H-hydrate dehydratase|||In PEBEL2; decreased reaction kinetics for ATP-dependent NAD(P)H-hydrate dehydratase activity; decreased affinity for (6S)-NADHX; changed ATP-dependent NAD(P)H-hydrate dehydratase activity; thermostability assays show that activity is lost at temperatures above 30 degrees Celsius.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||YjeF C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337021|||http://purl.uniprot.org/annotation/VAR_043564|||http://purl.uniprot.org/annotation/VAR_043565|||http://purl.uniprot.org/annotation/VAR_043566|||http://purl.uniprot.org/annotation/VAR_082224|||http://purl.uniprot.org/annotation/VAR_082225|||http://purl.uniprot.org/annotation/VSP_033829|||http://purl.uniprot.org/annotation/VSP_033830|||http://purl.uniprot.org/annotation/VSP_042012
http://togogenome.org/gene/9606:ARMC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NXE6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||Abolished histidine methylation by METTL9.|||Armadillo repeat-containing protein 6|||Does not affect histidine methylation by METTL9.|||In isoform 2.|||Phosphoserine|||Pros-methylhistidine|||Strongly reduced histidine methylation by METTL9.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242660|||http://purl.uniprot.org/annotation/VSP_040103
http://togogenome.org/gene/9606:KDM1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y6H0|||http://purl.uniprot.org/uniprot/Q8NB78                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CW-type|||Disordered|||GLYR1-binding|||Histone H3-binding|||In isoform 2.|||In isoform 4.|||Loss of demethylase activity.|||Loss of demethylase activity. Defective in the binding of FAD.|||Lysine-specific histone demethylase 2|||No effect on DNA or nucleosome binding.|||Normal demethylase activity.|||Phosphoserine|||Reduced demethylase activity.|||SWIRM|||Strongly reduced demethylase activity. Loss of enzymatic activity; when associated with 273-G--S-278.|||Strongly reduced demethylase activity. Loss of enzymatic activity; when associated with 285-A--A-287.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247336|||http://purl.uniprot.org/annotation/VSP_019963|||http://purl.uniprot.org/annotation/VSP_019964|||http://purl.uniprot.org/annotation/VSP_019965
http://togogenome.org/gene/9606:ZNF618                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7W0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Polar residues|||Zinc finger protein 618                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286811|||http://purl.uniprot.org/annotation/VSP_025179|||http://purl.uniprot.org/annotation/VSP_025180|||http://purl.uniprot.org/annotation/VSP_025181|||http://purl.uniprot.org/annotation/VSP_025182|||http://purl.uniprot.org/annotation/VSP_025183|||http://purl.uniprot.org/annotation/VSP_055968
http://togogenome.org/gene/9606:MAST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A669KBJ4|||http://purl.uniprot.org/uniprot/Q6P0Q8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||In a breast mucinous carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||Microtubule-associated serine/threonine-protein kinase 2|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086312|||http://purl.uniprot.org/annotation/VAR_040771|||http://purl.uniprot.org/annotation/VAR_040772|||http://purl.uniprot.org/annotation/VAR_040773|||http://purl.uniprot.org/annotation/VAR_040774|||http://purl.uniprot.org/annotation/VAR_040775|||http://purl.uniprot.org/annotation/VAR_040776|||http://purl.uniprot.org/annotation/VAR_040777|||http://purl.uniprot.org/annotation/VAR_040778|||http://purl.uniprot.org/annotation/VAR_040779|||http://purl.uniprot.org/annotation/VAR_040780|||http://purl.uniprot.org/annotation/VAR_040781|||http://purl.uniprot.org/annotation/VAR_040782|||http://purl.uniprot.org/annotation/VAR_040783|||http://purl.uniprot.org/annotation/VAR_040784|||http://purl.uniprot.org/annotation/VAR_040785|||http://purl.uniprot.org/annotation/VAR_051645|||http://purl.uniprot.org/annotation/VSP_051698|||http://purl.uniprot.org/annotation/VSP_051699|||http://purl.uniprot.org/annotation/VSP_051700
http://togogenome.org/gene/9606:TAF1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUE8|||http://purl.uniprot.org/uniprot/Q15572                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TATA box-binding protein-associated factor RNA polymerase I subunit C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118863|||http://purl.uniprot.org/annotation/VAR_023245|||http://purl.uniprot.org/annotation/VAR_023246|||http://purl.uniprot.org/annotation/VAR_023247|||http://purl.uniprot.org/annotation/VAR_023248|||http://purl.uniprot.org/annotation/VAR_023249|||http://purl.uniprot.org/annotation/VAR_023250|||http://purl.uniprot.org/annotation/VAR_023251|||http://purl.uniprot.org/annotation/VAR_023252|||http://purl.uniprot.org/annotation/VAR_023253|||http://purl.uniprot.org/annotation/VAR_023254|||http://purl.uniprot.org/annotation/VAR_023255|||http://purl.uniprot.org/annotation/VAR_057261|||http://purl.uniprot.org/annotation/VAR_057262|||http://purl.uniprot.org/annotation/VAR_058966|||http://purl.uniprot.org/annotation/VSP_015153|||http://purl.uniprot.org/annotation/VSP_015154|||http://purl.uniprot.org/annotation/VSP_015156|||http://purl.uniprot.org/annotation/VSP_038086|||http://purl.uniprot.org/annotation/VSP_038087
http://togogenome.org/gene/9606:CASP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42574                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-riboxanated arginine|||Abolished ADP-riboxanation by C.violaceum CopC.|||Caspase-3 subunit p12|||Caspase-3 subunit p17|||In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-28 and A-175.|||In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-9 and A-175.|||In P3-D3A mutant; abolished cleavage and activation, leading to prevent thiol protease activity; when associated with A-9 and A-28.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||S-nitrosocysteine; in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004569|||http://purl.uniprot.org/annotation/PRO_0000004570|||http://purl.uniprot.org/annotation/PRO_0000004571|||http://purl.uniprot.org/annotation/PRO_0000004572|||http://purl.uniprot.org/annotation/VAR_001401|||http://purl.uniprot.org/annotation/VAR_048616
http://togogenome.org/gene/9606:TMEM231                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6L2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In JBTS20.|||In MKS11.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 231                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317520|||http://purl.uniprot.org/annotation/VAR_038543|||http://purl.uniprot.org/annotation/VAR_069044|||http://purl.uniprot.org/annotation/VAR_070456|||http://purl.uniprot.org/annotation/VSP_042387|||http://purl.uniprot.org/annotation/VSP_042388
http://togogenome.org/gene/9606:IFITM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNB3                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In OI5; correlates with reduced expression and barely detectable secretion of SERPINF1.|||Interferon-induced transmembrane protein 5|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305103|||http://purl.uniprot.org/annotation/VAR_062170|||http://purl.uniprot.org/annotation/VAR_071889
http://togogenome.org/gene/9606:HIF1AN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Hypoxia-inducible factor 1-alpha inhibitor|||Impairs dimer formation, leading to loss of HIF1AAsn hydroxylation activity. No stimulation of 2-oxoglutarate turnover; when associated with A-201.|||Important for dimer formation|||Interaction with VHL|||JmjC|||Loss of HIF1AAsn hydroxylation activity and slight stimulation of 2-oxoglutarate turnover; when associated with G-201.|||Loss of HIF1AAsn hydroxylation activity. Slightly stimulates 2-oxoglutarate turnover.|||N-acetylalanine|||No effect on Asp hydroxylation ability.|||No effect on dimer formation and HIF1AAsn hydroxylation activity.|||No impact on HIF1AAsn hydroxylation activity. Loss of Asp hydroxylation ability. Strongly stimulates 2-oxoglutarate turnover. Loss of HIF1AAsn hydroxylation activity and slight stimulation of 2-oxoglutarate turnover; when associated with R-296.|||Prevents suppression of HIFCAD activity.|||Prevents suppression of HIFCAD activity. Strongly stimulates 2-oxoglutarate turnover. No stimulation of 2-oxoglutarate turnover; when associated with R-340.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083974|||http://purl.uniprot.org/annotation/VAR_051028
http://togogenome.org/gene/9606:GORASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes mitotic phosphorylation; when associated with A-222.|||Abolishes mitotic phosphorylation; when associated with A-225.|||Abolishes myristoylation. Loss of its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. No effect on ER stress-induced relocalization from Golgi to ER.|||Abolishes organelle clustering; when associated with A-59.|||Abolishes organelle clustering; when associated with S-100.|||Dimethylated arginine|||Disordered|||Enhances homodimerization. Loss of ER stress-induced relocalization from Golgi to ER.|||GRASP|||Golgi reassembly-stacking protein 2|||Important for membrane binding|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation and its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. Inhibits ER stress-mediated disruption of homodimerization. Loss of ER stress-induced relocalization from Golgi to ER.|||Loss of phosphorylation. Does not inhibit ER stress-mediated disruption of homodimerization.|||N-myristoyl glycine|||PDZ GRASP-type 1|||PDZ GRASP-type 2|||Phosphomimetic mutant. No disruption of homodimerization.|||Phosphomimetic mutant. No loss of its ability to mediate unconventional (ER/Golgi-independent) trafficking of CFTR to the cell membrane. Disrupts homodimerization. No loss of ER stress-induced relocalization from Golgi to ER.|||Phosphomimetic mutant. Partial disruption of homodimerization.|||Phosphomimetic mutation that decreases the ability to promote organelle clustering.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087545|||http://purl.uniprot.org/annotation/VAR_051013|||http://purl.uniprot.org/annotation/VSP_011300|||http://purl.uniprot.org/annotation/VSP_054364
http://togogenome.org/gene/9606:LTB4R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E292|||http://purl.uniprot.org/uniprot/Q9NPC1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Leukotriene B4 receptor 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069711
http://togogenome.org/gene/9606:RABGAP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKD7|||http://purl.uniprot.org/uniprot/B7ZAP0|||http://purl.uniprot.org/uniprot/F1LJ00|||http://purl.uniprot.org/uniprot/F5H8L0|||http://purl.uniprot.org/uniprot/Q5R372|||http://purl.uniprot.org/uniprot/Q9Y3L8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Arginine finger|||Basic and acidic residues|||Disordered|||Glutamine finger|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab GTPase-activating protein 1-like|||Rab GTPase-activating protein 1-like, isoform 10|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348054|||http://purl.uniprot.org/annotation/PRO_0000417613|||http://purl.uniprot.org/annotation/VAR_052533|||http://purl.uniprot.org/annotation/VSP_035087|||http://purl.uniprot.org/annotation/VSP_052912|||http://purl.uniprot.org/annotation/VSP_052913|||http://purl.uniprot.org/annotation/VSP_052914|||http://purl.uniprot.org/annotation/VSP_052915|||http://purl.uniprot.org/annotation/VSP_052916|||http://purl.uniprot.org/annotation/VSP_052917|||http://purl.uniprot.org/annotation/VSP_052918|||http://purl.uniprot.org/annotation/VSP_052919|||http://purl.uniprot.org/annotation/VSP_052920|||http://purl.uniprot.org/annotation/VSP_052921|||http://purl.uniprot.org/annotation/VSP_052922|||http://purl.uniprot.org/annotation/VSP_052923|||http://purl.uniprot.org/annotation/VSP_052924
http://togogenome.org/gene/9606:CALML5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53H37|||http://purl.uniprot.org/uniprot/Q9NZT1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Calmodulin-like protein 5|||Confirmed at protein level.|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073854|||http://purl.uniprot.org/annotation/VAR_047545|||http://purl.uniprot.org/annotation/VAR_047546
http://togogenome.org/gene/9606:ACSM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CK6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A synthetase ACSM2B, mitochondrial|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306094
http://togogenome.org/gene/9606:S1PR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95977                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Sphingosine 1-phosphate receptor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069431|||http://purl.uniprot.org/annotation/VAR_022066
http://togogenome.org/gene/9606:OR8G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVX6|||http://purl.uniprot.org/uniprot/Q15617                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150662|||http://purl.uniprot.org/annotation/VAR_034260
http://togogenome.org/gene/9606:ZBTB38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAP3|||http://purl.uniprot.org/uniprot/Q9H6F0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||Basic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Found in patients with pathologic myopia; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CBFA2T3|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047742|||http://purl.uniprot.org/annotation/VAR_052917|||http://purl.uniprot.org/annotation/VAR_052918|||http://purl.uniprot.org/annotation/VAR_052919|||http://purl.uniprot.org/annotation/VAR_079610
http://togogenome.org/gene/9606:KRT38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76015                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha8|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063695|||http://purl.uniprot.org/annotation/VAR_055137
http://togogenome.org/gene/9606:GIMAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7V4|||http://purl.uniprot.org/uniprot/B4DH95|||http://purl.uniprot.org/uniprot/Q6P9H5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AIG1-type G|||Disordered|||GTPase IMAP family member 6|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333011|||http://purl.uniprot.org/annotation/VAR_043037|||http://purl.uniprot.org/annotation/VAR_043038|||http://purl.uniprot.org/annotation/VAR_043039|||http://purl.uniprot.org/annotation/VAR_049533|||http://purl.uniprot.org/annotation/VSP_033436|||http://purl.uniprot.org/annotation/VSP_045595|||http://purl.uniprot.org/annotation/VSP_045596
http://togogenome.org/gene/9606:ATP2B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23634                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Calmodulin-binding subdomain A|||Calmodulin-binding subdomain B|||Cytoplasmic|||Decreased calcium transport activity.|||Disordered|||Extracellular|||Helical|||In isoform XA, isoform XK, isoform ZA and isoform ZK.|||In isoform XB and isoform ZB.|||In isoform XK and isoform ZK.|||In isoform ZA, isoform ZK, isoform ZB and isoform ZD.|||Mildly decreased calcium transport activity.|||Phosphoserine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 4|||Strongly decreased calcium transport activity. Slowed decomposition of the phosphorylated intermediate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046220|||http://purl.uniprot.org/annotation/VSP_000402|||http://purl.uniprot.org/annotation/VSP_000403|||http://purl.uniprot.org/annotation/VSP_000404|||http://purl.uniprot.org/annotation/VSP_000405
http://togogenome.org/gene/9606:SDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PBI9|||http://purl.uniprot.org/uniprot/P34741                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage of ectodomain|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Neurexin/syndecan/glycophorin C|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphoserine|||Phosphoserine; by FAM20C|||Syndecan-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033503|||http://purl.uniprot.org/annotation/VAR_034675|||http://purl.uniprot.org/annotation/VAR_034676
http://togogenome.org/gene/9606:ARMH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RUU6|||http://purl.uniprot.org/uniprot/Q86TY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Armadillo-like helical domain-containing protein 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252152|||http://purl.uniprot.org/annotation/PRO_5002781890|||http://purl.uniprot.org/annotation/VAR_027782|||http://purl.uniprot.org/annotation/VAR_027783|||http://purl.uniprot.org/annotation/VAR_027784|||http://purl.uniprot.org/annotation/VAR_027785|||http://purl.uniprot.org/annotation/VSP_020881|||http://purl.uniprot.org/annotation/VSP_020882|||http://purl.uniprot.org/annotation/VSP_020883
http://togogenome.org/gene/9606:SLC37A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57057                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Glucose-6-phosphate exchanger SLC37A1|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199890|||http://purl.uniprot.org/annotation/VAR_017110|||http://purl.uniprot.org/annotation/VAR_017111
http://togogenome.org/gene/9606:HMGB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26583                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cysteine sulfonic acid (-SO3H)|||Cysteine sulfonic acid (-SO3H); alternate|||Disordered|||HMG box 1|||HMG box 2|||High mobility group protein B2|||In disulfide HMGB2; alternate|||N6-acetyllysine|||Phosphoserine|||Required for chemotactic activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048534
http://togogenome.org/gene/9606:DLEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1B5Y4|||http://purl.uniprot.org/uniprot/Q9Y238                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Deleted in lung and esophageal cancer protein 1|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079929|||http://purl.uniprot.org/annotation/VAR_035908|||http://purl.uniprot.org/annotation/VAR_056860|||http://purl.uniprot.org/annotation/VAR_056861|||http://purl.uniprot.org/annotation/VAR_056862|||http://purl.uniprot.org/annotation/VAR_056863|||http://purl.uniprot.org/annotation/VAR_056864|||http://purl.uniprot.org/annotation/VSP_051847|||http://purl.uniprot.org/annotation/VSP_051848|||http://purl.uniprot.org/annotation/VSP_051849|||http://purl.uniprot.org/annotation/VSP_051850
http://togogenome.org/gene/9606:EPRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07814                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||3 X 57 AA approximate repeats|||Abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment. Abolishes interaction with SYNCRIP.|||Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G.|||Almost complete loss of prolyl-tRNA ligase activity.|||Basic and acidic residues|||Bifunctional glutamate/proline--tRNA ligase|||Charged|||Disordered|||Glutamate--tRNA ligase|||In HLD15.|||In HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly.|||In HLD15; unknown pathological significance.|||In HLD15; unknown pathological significance; small decrease in aminoacylation activity.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone.|||Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP.|||Not active in translation inhibition, abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by RPS6KB1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proline--tRNA ligase|||WHEP-TRS 1|||WHEP-TRS 2|||WHEP-TRS 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119743|||http://purl.uniprot.org/annotation/VAR_037288|||http://purl.uniprot.org/annotation/VAR_037289|||http://purl.uniprot.org/annotation/VAR_037290|||http://purl.uniprot.org/annotation/VAR_037291|||http://purl.uniprot.org/annotation/VAR_037292|||http://purl.uniprot.org/annotation/VAR_037293|||http://purl.uniprot.org/annotation/VAR_037294|||http://purl.uniprot.org/annotation/VAR_057358|||http://purl.uniprot.org/annotation/VAR_080800|||http://purl.uniprot.org/annotation/VAR_080801|||http://purl.uniprot.org/annotation/VAR_080802|||http://purl.uniprot.org/annotation/VAR_080803
http://togogenome.org/gene/9606:RAB17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0T7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Effector region|||In isoform 2.|||Phosphoserine|||Ras-related protein Rab-17|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121191|||http://purl.uniprot.org/annotation/VAR_022102|||http://purl.uniprot.org/annotation/VAR_051711|||http://purl.uniprot.org/annotation/VAR_051712|||http://purl.uniprot.org/annotation/VSP_056400
http://togogenome.org/gene/9606:PNCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2M8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcium/calmodulin-dependent protein kinase type 1B|||Calmodulin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086079|||http://purl.uniprot.org/annotation/VAR_040598|||http://purl.uniprot.org/annotation/VSP_012634|||http://purl.uniprot.org/annotation/VSP_012635|||http://purl.uniprot.org/annotation/VSP_039091|||http://purl.uniprot.org/annotation/VSP_043373
http://togogenome.org/gene/9606:MLLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03111                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Acylated histone binding|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Protein ENL|||YEATS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215938
http://togogenome.org/gene/9606:TGFB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM40|||http://purl.uniprot.org/uniprot/B3KVH9|||http://purl.uniprot.org/uniprot/P10600                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Cell attachment site|||Disordered|||In LDS5; hypomorphic mutation; results in impaired TGF-beta signaling.|||In isoform 2.|||Interchain|||Latency-associated peptide|||N-linked (GlcNAc...) asparagine|||N5-methylglutamine|||TGF-beta family profile|||Transforming growth factor beta|||Transforming growth factor beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033796|||http://purl.uniprot.org/annotation/PRO_0000033797|||http://purl.uniprot.org/annotation/PRO_5014297005|||http://purl.uniprot.org/annotation/VAR_016315|||http://purl.uniprot.org/annotation/VAR_070924|||http://purl.uniprot.org/annotation/VSP_056285
http://togogenome.org/gene/9606:TLR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR97                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes activation of NF-kappa-B.|||Abolishes responses to both ssRNA and chemical ligands.|||Cytoplasmic|||Extracellular|||Helical|||In IMD98; gain-of-function variant resulting in increased NF-kappa-B activation measured in a reporter assay.|||In IMD98; increased NF-kappa-B activation measured in a reporter assay; results in increased TLR8 protein degradation.|||In isoform 2.|||Increases activation of NF-kappa-B.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||Monomeric and inactive.|||N-linked (GlcNAc...) asparagine|||Strongly decreases activation of NF-kappa-B.|||TIR|||Toll-like receptor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034735|||http://purl.uniprot.org/annotation/VAR_024667|||http://purl.uniprot.org/annotation/VAR_052363|||http://purl.uniprot.org/annotation/VAR_087088|||http://purl.uniprot.org/annotation/VAR_087089|||http://purl.uniprot.org/annotation/VAR_087090|||http://purl.uniprot.org/annotation/VAR_087091|||http://purl.uniprot.org/annotation/VSP_053412
http://togogenome.org/gene/9606:DAZ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  DAZ 1|||DAZ 10|||DAZ 11|||DAZ 12|||DAZ 2|||DAZ 3|||DAZ 4|||DAZ 5|||DAZ 6|||DAZ 7|||DAZ 8|||DAZ 9|||Deleted in azoospermia protein 3|||Disordered|||In isoform 2.|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081556|||http://purl.uniprot.org/annotation/VSP_040218
http://togogenome.org/gene/9606:LOC102724334                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57053                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type F-S|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071838
http://togogenome.org/gene/9606:CCDC166                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW27                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 166|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000412224
http://togogenome.org/gene/9606:TSPAN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95859                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Impairs interaction with ADAM10; when associated with S-12 and S-83.|||Impairs interaction with ADAM10; when associated with S-9 and S-12.|||Impairs interaction with ADAM10; when associated with S-9 and S-83.|||In EVR5.|||In isoform 2.|||S-palmitoyl cysteine|||Tetraspanin-12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219257|||http://purl.uniprot.org/annotation/VAR_062253|||http://purl.uniprot.org/annotation/VAR_063576|||http://purl.uniprot.org/annotation/VAR_063577|||http://purl.uniprot.org/annotation/VAR_063578|||http://purl.uniprot.org/annotation/VAR_063579|||http://purl.uniprot.org/annotation/VAR_068899|||http://purl.uniprot.org/annotation/VAR_068900|||http://purl.uniprot.org/annotation/VAR_068901|||http://purl.uniprot.org/annotation/VSP_038525
http://togogenome.org/gene/9606:RAB26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively activated.|||Disordered|||Effector region|||In isoform 2.|||Inactive, constitutively GDP-bound. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane.|||Inactive, due to loss of GNP binding. Abolishes location at Golgi membranes. Impairs transport of ADRA2A and ADRA2B from the Golgi to the cell membrane.|||Polar residues|||Ras-related protein Rab-26|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121218|||http://purl.uniprot.org/annotation/VSP_056879
http://togogenome.org/gene/9606:SLC19A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZV2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for pyridoxine transport|||Extracellular|||Helical|||In THMD2.|||N-linked (GlcNAc...) asparagine|||Significant decrease in pyridoxine transport.|||Thiamine transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232656|||http://purl.uniprot.org/annotation/VAR_025992|||http://purl.uniprot.org/annotation/VAR_025993|||http://purl.uniprot.org/annotation/VAR_052405|||http://purl.uniprot.org/annotation/VAR_061864
http://togogenome.org/gene/9606:TSNARE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RHT3|||http://purl.uniprot.org/uniprot/Q6P186|||http://purl.uniprot.org/uniprot/Q96NA8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology|||t-SNARE domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065668|||http://purl.uniprot.org/annotation/VAR_051461|||http://purl.uniprot.org/annotation/VAR_051462|||http://purl.uniprot.org/annotation/VAR_051463|||http://purl.uniprot.org/annotation/VAR_055146|||http://purl.uniprot.org/annotation/VSP_056304
http://togogenome.org/gene/9606:FABP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51161                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Gastrotropin|||In isoform 2.|||May be associated with type 2 diabetes obese individuals.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067380|||http://purl.uniprot.org/annotation/VAR_039578|||http://purl.uniprot.org/annotation/VAR_039579|||http://purl.uniprot.org/annotation/VAR_039580|||http://purl.uniprot.org/annotation/VSP_038039
http://togogenome.org/gene/9606:CCR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R734|||http://purl.uniprot.org/uniprot/P51686                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 9|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069291|||http://purl.uniprot.org/annotation/VAR_020068|||http://purl.uniprot.org/annotation/VAR_029208|||http://purl.uniprot.org/annotation/VSP_020286
http://togogenome.org/gene/9606:NMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A250SI41|||http://purl.uniprot.org/uniprot/Q5H8A3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Asparagine amide|||Neuromedin-S                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262480|||http://purl.uniprot.org/annotation/PRO_0000262481|||http://purl.uniprot.org/annotation/PRO_0000262482|||http://purl.uniprot.org/annotation/PRO_0000262483|||http://purl.uniprot.org/annotation/PRO_0000262484|||http://purl.uniprot.org/annotation/PRO_5011528102|||http://purl.uniprot.org/annotation/VAR_029495
http://togogenome.org/gene/9606:SRSF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05519                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  1|||10|||10 X 8 AA approximate repeats of R-R-S-R-S-R-S-R|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Serine/arginine-rich splicing factor 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081939|||http://purl.uniprot.org/annotation/VSP_043376
http://togogenome.org/gene/9606:NCOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J5B8|||http://purl.uniprot.org/uniprot/H0Y459|||http://purl.uniprot.org/uniprot/O75376|||http://purl.uniprot.org/uniprot/Q6PGR4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CORNR box 1|||CORNR box 2|||CORNR box 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HTH myb-type|||ID1|||ID2|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with C1D|||Interaction with ETO|||Interaction with SIN3A/B|||Interaction with ZBTB33 and HEXIM1|||Myb-like|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear receptor corepressor 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with RARA in the absence of its ligand|||SANT|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055617|||http://purl.uniprot.org/annotation/VSP_010207|||http://purl.uniprot.org/annotation/VSP_010208|||http://purl.uniprot.org/annotation/VSP_046468|||http://purl.uniprot.org/annotation/VSP_046469|||http://purl.uniprot.org/annotation/VSP_046470
http://togogenome.org/gene/9606:CLEC4E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULY5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 4 member E|||Confers specificity for glucose/mannose-type carbohydrates|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Impairs binding to trehalose-6,6'-dimycolate.|||Impairs trehalose-6,6'-dimycolate (TDM)-induced NF-kappa-B activation.|||N-linked (GlcNAc...) asparagine|||Reduces trehalose-6,6'-dimycolate (TDM)-induced NF-kappa-B activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046619
http://togogenome.org/gene/9606:IQGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7U6|||http://purl.uniprot.org/uniprot/B7Z7X2|||http://purl.uniprot.org/uniprot/Q13576|||http://purl.uniprot.org/uniprot/Q59HA3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||IQ 1|||IQ 2|||IQ 3|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Ras GTPase-activating-like protein IQGAP2|||Ras-GAP|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056650|||http://purl.uniprot.org/annotation/VAR_055823|||http://purl.uniprot.org/annotation/VAR_055824|||http://purl.uniprot.org/annotation/VAR_055825|||http://purl.uniprot.org/annotation/VAR_055826|||http://purl.uniprot.org/annotation/VAR_055827|||http://purl.uniprot.org/annotation/VAR_055828|||http://purl.uniprot.org/annotation/VAR_055829|||http://purl.uniprot.org/annotation/VAR_059292|||http://purl.uniprot.org/annotation/VAR_062958|||http://purl.uniprot.org/annotation/VAR_062959|||http://purl.uniprot.org/annotation/VAR_062960|||http://purl.uniprot.org/annotation/VAR_069434|||http://purl.uniprot.org/annotation/VAR_069435|||http://purl.uniprot.org/annotation/VSP_010629|||http://purl.uniprot.org/annotation/VSP_010630|||http://purl.uniprot.org/annotation/VSP_010631|||http://purl.uniprot.org/annotation/VSP_055149
http://togogenome.org/gene/9606:KLRC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43908                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In allele NKG2-F*02.|||NKG2-F type II integral membrane protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046673|||http://purl.uniprot.org/annotation/VAR_013406|||http://purl.uniprot.org/annotation/VAR_013407
http://togogenome.org/gene/9606:MBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11226                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Associated with low serum mannose-binding protein (MBP) concentrations and recurrent infections.|||Associated with low serum mannose-binding protein (MBP) concentrations; associated with protection against tuberculosis caused by Mycobacterium africanum.|||C-type lectin|||Collagen-like|||Disordered|||Hydroxyproline|||In 0.05% of European and African populations.|||In Chinese.|||Mannose-binding protein C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017401|||http://purl.uniprot.org/annotation/VAR_004182|||http://purl.uniprot.org/annotation/VAR_004183|||http://purl.uniprot.org/annotation/VAR_008543|||http://purl.uniprot.org/annotation/VAR_013294|||http://purl.uniprot.org/annotation/VAR_050119
http://togogenome.org/gene/9606:NOPCHAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5I9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||NOP protein chaperone 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263623|||http://purl.uniprot.org/annotation/VAR_056833|||http://purl.uniprot.org/annotation/VAR_060438
http://togogenome.org/gene/9606:AK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M32                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Adenylate kinase|||Adenylate kinase 7|||DPY-30|||In SPGF27; loss of protein expression in sperm cells, no effect in airway epithelial cells.|||LID|||NMP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158952|||http://purl.uniprot.org/annotation/VAR_017059|||http://purl.uniprot.org/annotation/VAR_057950|||http://purl.uniprot.org/annotation/VAR_080917
http://togogenome.org/gene/9606:GAGE12F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76087|||http://purl.uniprot.org/uniprot/P0CL80|||http://purl.uniprot.org/uniprot/P0CL81|||http://purl.uniprot.org/uniprot/P0CL82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12F|||G antigen 12G|||G antigen 12I|||G antigen 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148345|||http://purl.uniprot.org/annotation/PRO_0000311978|||http://purl.uniprot.org/annotation/PRO_0000407492|||http://purl.uniprot.org/annotation/PRO_0000407493|||http://purl.uniprot.org/annotation/VSP_040953
http://togogenome.org/gene/9606:EAPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56P03                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||E2F-associated phosphoprotein|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086904|||http://purl.uniprot.org/annotation/VAR_031915
http://togogenome.org/gene/9606:GSTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09488|||http://purl.uniprot.org/uniprot/X5D932|||http://purl.uniprot.org/uniprot/X5DR03                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Changes the properties of the enzyme toward some substrates.|||GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 1|||In allele GSTM1B.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Reduces catalytic activity 10-fold.|||Reduces catalytic activity 100-fold.|||Reduces catalytic activity by half.|||Removed|||Slight increase of catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185816|||http://purl.uniprot.org/annotation/VAR_003617|||http://purl.uniprot.org/annotation/VAR_014497|||http://purl.uniprot.org/annotation/VSP_036618
http://togogenome.org/gene/9606:SPDYE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLX3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Speedy protein E4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349195
http://togogenome.org/gene/9606:PERP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In EKVP7; patient cells show a change in the subcellular location pattern; does not associate with cell membrane; diffuse location into the cytoplasm.|||In OLMS2.|||In OLMS2; keratinocytes from patient show normal PERP membrane localization.|||p53 apoptosis effector related to PMP-22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226994|||http://purl.uniprot.org/annotation/VAR_052341|||http://purl.uniprot.org/annotation/VAR_070891|||http://purl.uniprot.org/annotation/VAR_085248|||http://purl.uniprot.org/annotation/VAR_085249|||http://purl.uniprot.org/annotation/VAR_085250
http://togogenome.org/gene/9606:IL19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHD0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Interleukin-19|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015379|||http://purl.uniprot.org/annotation/VAR_013077|||http://purl.uniprot.org/annotation/VSP_046253|||http://purl.uniprot.org/annotation/VSP_057193
http://togogenome.org/gene/9606:B3GALT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MS93|||http://purl.uniprot.org/uniprot/Q9Y2C3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyltransferase 5|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219164|||http://purl.uniprot.org/annotation/VAR_020460|||http://purl.uniprot.org/annotation/VAR_033536|||http://purl.uniprot.org/annotation/VAR_049347
http://togogenome.org/gene/9606:CR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VPA4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Complement component receptor 1-like protein|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317776|||http://purl.uniprot.org/annotation/VAR_038677|||http://purl.uniprot.org/annotation/VAR_038678|||http://purl.uniprot.org/annotation/VAR_038679|||http://purl.uniprot.org/annotation/VAR_038680|||http://purl.uniprot.org/annotation/VAR_038681|||http://purl.uniprot.org/annotation/VSP_031151|||http://purl.uniprot.org/annotation/VSP_031152|||http://purl.uniprot.org/annotation/VSP_031153
http://togogenome.org/gene/9606:FDX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4F2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||Disordered|||Ferredoxin-2, mitochondrial|||In MEOAL; strongly reduced protein expression in muscle in affected homozygous patients compared to control individuals.|||In MEOAL; unknown pathological significance; expressed at low levels in fibroblasts and muscles from a homozygous patient.|||In isoform 2.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325952|||http://purl.uniprot.org/annotation/VAR_082099|||http://purl.uniprot.org/annotation/VAR_082100|||http://purl.uniprot.org/annotation/VSP_056826
http://togogenome.org/gene/9606:ZRANB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGI0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Abolished binding to 'Lys-29'- and 'Lys-33'-linked ubiquitin.|||Abolished binding to 'Lys-33'-linked diubiquitin.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with 14-LV-15; A-90; 94-LV-95; A-155 and 159-LV-160.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; 94-LV-95; A-155 and 159-LV-160.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95 and 159-LV-160.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95; and A-155.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; A-155 and 159-LV-160.|||Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; A-90; 94-LV-95; A-155 and 159-LV-160.|||Abolishes the deubiquitinating activity but not the binding to ubiquitin chains.|||Disordered|||Does not affect binding to 'Lys-29'- and 'Lys-33'-linked ubiquitin.|||Nucleophile|||OTU|||Polar residues|||Proton acceptor|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||Strongly reduced binding to 'Lys-29'- and 'Lys-33'-linked ubiquitin.|||Strongly reduced binding to 'Lys-33'-linked diubiquitin.|||TRAF-binding|||Ubiquitin thioesterase ZRANB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065595
http://togogenome.org/gene/9606:SLC25A36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEA9|||http://purl.uniprot.org/uniprot/Q96CQ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291797|||http://purl.uniprot.org/annotation/VSP_026240|||http://purl.uniprot.org/annotation/VSP_026241|||http://purl.uniprot.org/annotation/VSP_026242|||http://purl.uniprot.org/annotation/VSP_035517
http://togogenome.org/gene/9606:PLAAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL19                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Cytoplasmic|||Essential for its ability regulate keratinocyte differentiation|||Helical|||In isoform 2.|||Interaction with TGM1|||LRAT|||Lumenal|||Phospholipase A and acyltransferase 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152490|||http://purl.uniprot.org/annotation/VAR_049480|||http://purl.uniprot.org/annotation/VAR_049481|||http://purl.uniprot.org/annotation/VSP_041496
http://togogenome.org/gene/9606:ZNRF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with RSPO1 and prevents subsequent membrane clearance.|||Basic residues|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase ZNRF3|||Extracellular|||Helical|||In isoform 2.|||Polar residues|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277806|||http://purl.uniprot.org/annotation/VSP_044043
http://togogenome.org/gene/9606:SPMIP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein SPMIP9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304989|||http://purl.uniprot.org/annotation/VAR_035142
http://togogenome.org/gene/9606:ELP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6Q8PGW3|||http://purl.uniprot.org/uniprot/B3KNB2|||http://purl.uniprot.org/uniprot/B4E3I9|||http://purl.uniprot.org/uniprot/F5H2T0|||http://purl.uniprot.org/uniprot/O95163|||http://purl.uniprot.org/uniprot/Q4LE38|||http://purl.uniprot.org/uniprot/Q8N516                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Disruption of dimer formation, reduced protein stability and reduced interaction with ELP2 and ELP3. Does not affect binding to tRNA.|||Elongator complex protein 1|||In HSAN3; mild phenotype; phosphorylation is reduced; does not affect interaction with ELP2; reduced interaction with ELP3; does not affect dimerization.|||In HSAN3; reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization.|||Mediates dimerization|||Phosphoserine|||Polar residues|||Reduced interaction with ELP2; does not affect interaction with ELP3; does not affect dimerization.|||Required for binding to tRNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084177|||http://purl.uniprot.org/annotation/VAR_011327|||http://purl.uniprot.org/annotation/VAR_047476|||http://purl.uniprot.org/annotation/VAR_047477|||http://purl.uniprot.org/annotation/VAR_047478|||http://purl.uniprot.org/annotation/VAR_047479|||http://purl.uniprot.org/annotation/VAR_047480|||http://purl.uniprot.org/annotation/VAR_047481|||http://purl.uniprot.org/annotation/VAR_047482|||http://purl.uniprot.org/annotation/VAR_047483|||http://purl.uniprot.org/annotation/VAR_047484|||http://purl.uniprot.org/annotation/VAR_047485|||http://purl.uniprot.org/annotation/VAR_047486|||http://purl.uniprot.org/annotation/VAR_047487|||http://purl.uniprot.org/annotation/VAR_085681
http://togogenome.org/gene/9606:CAPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDI5|||http://purl.uniprot.org/uniprot/B4DWH5|||http://purl.uniprot.org/uniprot/P07384                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-1 catalytic subunit|||Cleavage; for 75 kDa form|||Cleavage; for 78 kDa form|||Domain III|||Domain IV|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In SPG76.|||Linker|||N-acetylserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207694|||http://purl.uniprot.org/annotation/VAR_021085|||http://purl.uniprot.org/annotation/VAR_021086|||http://purl.uniprot.org/annotation/VAR_021087|||http://purl.uniprot.org/annotation/VAR_021088|||http://purl.uniprot.org/annotation/VAR_077899
http://togogenome.org/gene/9606:TAFA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3H0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chemokine-like protein TAFA-2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042723|||http://purl.uniprot.org/annotation/VSP_016066
http://togogenome.org/gene/9606:GPR50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13585                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Higher fasting circulating triglyceride levels.|||Lower fasting circulating triglyceride levels.|||Melatonin-related receptor|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069878|||http://purl.uniprot.org/annotation/VAR_062254|||http://purl.uniprot.org/annotation/VAR_062255|||http://purl.uniprot.org/annotation/VAR_062256
http://togogenome.org/gene/9606:CTDSPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15194                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||CTD small phosphatase-like protein|||Disordered|||FCP1 homology|||In isoform 2.|||Proton donor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212569|||http://purl.uniprot.org/annotation/VAR_019683|||http://purl.uniprot.org/annotation/VAR_019684|||http://purl.uniprot.org/annotation/VAR_019685|||http://purl.uniprot.org/annotation/VSP_011541
http://togogenome.org/gene/9606:TAFA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5A8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chemokine-like protein TAFA-3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042726|||http://purl.uniprot.org/annotation/VSP_016067
http://togogenome.org/gene/9606:CDC14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RQX7|||http://purl.uniprot.org/uniprot/B4DY86|||http://purl.uniprot.org/uniprot/Q59EF4|||http://purl.uniprot.org/uniprot/Q9UNH5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A|||B|||Disordered|||Dual specificity protein phosphatase CDC14A|||In DFNB32.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inappropriate nucleolar localization; when associated with A-362.|||Inappropriate nucleolar localization; when associated with A-364.|||Linker|||Loss of phosphatase activity.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094876|||http://purl.uniprot.org/annotation/VAR_019957|||http://purl.uniprot.org/annotation/VAR_019958|||http://purl.uniprot.org/annotation/VAR_035655|||http://purl.uniprot.org/annotation/VAR_081127|||http://purl.uniprot.org/annotation/VAR_081128|||http://purl.uniprot.org/annotation/VAR_081129|||http://purl.uniprot.org/annotation/VAR_081130|||http://purl.uniprot.org/annotation/VAR_081131|||http://purl.uniprot.org/annotation/VAR_081132|||http://purl.uniprot.org/annotation/VAR_081133|||http://purl.uniprot.org/annotation/VSP_012035|||http://purl.uniprot.org/annotation/VSP_012036|||http://purl.uniprot.org/annotation/VSP_012037|||http://purl.uniprot.org/annotation/VSP_012322|||http://purl.uniprot.org/annotation/VSP_012323|||http://purl.uniprot.org/annotation/VSP_047597
http://togogenome.org/gene/9606:EXOSC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5RKV6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Exosome complex component MTR3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287478
http://togogenome.org/gene/9606:NEURL1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MQ27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase NEURL1B|||In isoform 2.|||In isoform 3.|||NHR 1|||NHR 2|||Phosphothreonine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349382|||http://purl.uniprot.org/annotation/VSP_044404|||http://purl.uniprot.org/annotation/VSP_044405
http://togogenome.org/gene/9606:TRIM65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJ69                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||B box-type|||B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM65|||N-acetylalanine|||Phosphoserine|||Pro residues|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249191|||http://purl.uniprot.org/annotation/VAR_057224|||http://purl.uniprot.org/annotation/VAR_057225|||http://purl.uniprot.org/annotation/VAR_060245|||http://purl.uniprot.org/annotation/VAR_060246
http://togogenome.org/gene/9606:NME5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4L9|||http://purl.uniprot.org/uniprot/P56597                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant                                                                                  ^@                                                                                  In CILD48; unknown pathological significance.|||Nucleoside diphosphate kinase homolog 5|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137125|||http://purl.uniprot.org/annotation/VAR_087812
http://togogenome.org/gene/9606:CIMAP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L1A8|||http://purl.uniprot.org/uniprot/A8MYP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule associated protein 1B|||Disordered|||In isoform 2.|||Polar residues|||STPGR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346440|||http://purl.uniprot.org/annotation/VSP_034995|||http://purl.uniprot.org/annotation/VSP_034996|||http://purl.uniprot.org/annotation/VSP_034997
http://togogenome.org/gene/9606:ADGRG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E148|||http://purl.uniprot.org/uniprot/Q8IZF4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor G5|||Cleavage; by autolysis|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012894|||http://purl.uniprot.org/annotation/PRO_5002803723
http://togogenome.org/gene/9606:HSPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAH6|||http://purl.uniprot.org/uniprot/Q16082                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Heat shock protein beta-2|||SHSP|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125933|||http://purl.uniprot.org/annotation/VAR_016316
http://togogenome.org/gene/9606:NLGN4Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHI3|||http://purl.uniprot.org/uniprot/Q8NFZ3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carboxylesterase type B|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Interaction with NRXN1|||N-linked (GlcNAc...) asparagine|||Neuroligin-4, Y-linked|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008649|||http://purl.uniprot.org/annotation/VSP_007537|||http://purl.uniprot.org/annotation/VSP_044852|||http://purl.uniprot.org/annotation/VSP_044853|||http://purl.uniprot.org/annotation/VSP_044854|||http://purl.uniprot.org/annotation/VSP_044855
http://togogenome.org/gene/9606:SSX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60224                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||KRAB-related|||Polar residues|||Protein SSX4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181831|||http://purl.uniprot.org/annotation/VSP_054114|||http://purl.uniprot.org/annotation/VSP_054115
http://togogenome.org/gene/9606:WNT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96014                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041465
http://togogenome.org/gene/9606:KLHL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY78|||http://purl.uniprot.org/uniprot/Q68DU9|||http://purl.uniprot.org/uniprot/Q7Z330|||http://purl.uniprot.org/uniprot/Q9P2G9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 8|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119108|||http://purl.uniprot.org/annotation/VAR_030012|||http://purl.uniprot.org/annotation/VSP_054443
http://togogenome.org/gene/9606:PJVK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0ZLH3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In DFNB59.|||In DFNB59; causes hypervulnerability to sound.|||In DFNB59; unknown pathological significance.|||Pejvakin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249042|||http://purl.uniprot.org/annotation/VAR_027387|||http://purl.uniprot.org/annotation/VAR_027388|||http://purl.uniprot.org/annotation/VAR_053103|||http://purl.uniprot.org/annotation/VAR_068891|||http://purl.uniprot.org/annotation/VAR_083912|||http://purl.uniprot.org/annotation/VAR_083913|||http://purl.uniprot.org/annotation/VAR_083914
http://togogenome.org/gene/9606:TAF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXI2|||http://purl.uniprot.org/uniprot/Q7Z7C8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Bromodomain associated|||Disordered|||Histone-fold; involved in forming hexamer structure in TFIID complex|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Transcription initiation factor TFIID subunit 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315396|||http://purl.uniprot.org/annotation/VSP_030548|||http://purl.uniprot.org/annotation/VSP_030549
http://togogenome.org/gene/9606:H2AC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KPC7|||http://purl.uniprot.org/uniprot/Q96KK5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1-H|||Histone H2A/H2B/H3|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230200
http://togogenome.org/gene/9606:RASSF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8G8|||http://purl.uniprot.org/uniprot/Q8NHQ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Phosphothreonine|||Ras association domain-containing protein 8|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089840|||http://purl.uniprot.org/annotation/VSP_014248
http://togogenome.org/gene/9606:FANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC84                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Fibronectin type 3 and ankyrin repeat domains protein 1|||Fibronectin type-III|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066990|||http://purl.uniprot.org/annotation/VAR_024176|||http://purl.uniprot.org/annotation/VAR_027896|||http://purl.uniprot.org/annotation/VAR_048296|||http://purl.uniprot.org/annotation/VAR_048297|||http://purl.uniprot.org/annotation/VSP_013568|||http://purl.uniprot.org/annotation/VSP_013569
http://togogenome.org/gene/9606:NBEAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS30                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Disordered|||In isoform 1.|||Neurobeachin-like protein 1|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051094|||http://purl.uniprot.org/annotation/VSP_039337|||http://purl.uniprot.org/annotation/VSP_039338
http://togogenome.org/gene/9606:PLEKHA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K727|||http://purl.uniprot.org/uniprot/Q9HB19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PH|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin homology domain-containing family A member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053876|||http://purl.uniprot.org/annotation/VAR_061516
http://togogenome.org/gene/9606:MAP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CN5|||http://purl.uniprot.org/uniprot/Q49MG5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Microtubule-associated protein 9|||N-acetylserine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247753|||http://purl.uniprot.org/annotation/VAR_027151|||http://purl.uniprot.org/annotation/VAR_051152|||http://purl.uniprot.org/annotation/VAR_051153|||http://purl.uniprot.org/annotation/VAR_051154|||http://purl.uniprot.org/annotation/VSP_020037|||http://purl.uniprot.org/annotation/VSP_020038
http://togogenome.org/gene/9606:GNRH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43555                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycine amide|||GnRH-associated peptide 2|||Gonadoliberin-2|||In isoform 2.|||In isoform 3.|||Progonadoliberin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012456|||http://purl.uniprot.org/annotation/PRO_0000012457|||http://purl.uniprot.org/annotation/PRO_0000012458|||http://purl.uniprot.org/annotation/VAR_053109|||http://purl.uniprot.org/annotation/VSP_001825|||http://purl.uniprot.org/annotation/VSP_001826
http://togogenome.org/gene/9606:CYP26B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ER08|||http://purl.uniprot.org/uniprot/Q9NR63                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 26B1|||In RHFCA.|||In isoform 2.|||In isoform 3.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051985|||http://purl.uniprot.org/annotation/VAR_024383|||http://purl.uniprot.org/annotation/VAR_038722|||http://purl.uniprot.org/annotation/VAR_038723|||http://purl.uniprot.org/annotation/VAR_038724|||http://purl.uniprot.org/annotation/VAR_038725|||http://purl.uniprot.org/annotation/VAR_038726|||http://purl.uniprot.org/annotation/VAR_038727|||http://purl.uniprot.org/annotation/VAR_038728|||http://purl.uniprot.org/annotation/VAR_038729|||http://purl.uniprot.org/annotation/VAR_067923|||http://purl.uniprot.org/annotation/VAR_067924|||http://purl.uniprot.org/annotation/VAR_075982|||http://purl.uniprot.org/annotation/VSP_042967|||http://purl.uniprot.org/annotation/VSP_042968
http://togogenome.org/gene/9606:PAPPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTA8|||http://purl.uniprot.org/uniprot/Q13219|||http://purl.uniprot.org/uniprot/Q7Z613                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Interchain|||Interchain (with C-169 in PRG2 proform)|||Interchain (with C-51 in PRG2 proform)|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||Or C-583 with C-612|||Or C-587 with C-600|||Pappalysin-1|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029245|||http://purl.uniprot.org/annotation/PRO_0000029246|||http://purl.uniprot.org/annotation/VAR_011419|||http://purl.uniprot.org/annotation/VAR_018726|||http://purl.uniprot.org/annotation/VAR_057091|||http://purl.uniprot.org/annotation/VAR_057092
http://togogenome.org/gene/9606:PTPRS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13332|||http://purl.uniprot.org/uniprot/Q59FX6|||http://purl.uniprot.org/uniprot/Q8NHS7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NTRK3.|||Abolishes interaction with NTRK3; when associated with A-100.|||Abolishes interaction with NTRK3; when associated with A-97.|||Cleavage|||Cytoplasmic|||Decreases interaction with NTRK3.|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Important for binding to glycosaminoglycan chains|||In a colorectal cancer sample; somatic mutation.|||In isoform PTPS-F4-7 and isoform 3.|||In isoform PTPS-MEA, isoform 2 and isoform 3.|||In isoform PTPS-MEB, isoform 2 and isoform 3.|||In isoform PTPS-MEC and isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Receptor-type tyrosine-protein phosphatase S|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025462|||http://purl.uniprot.org/annotation/PRO_5014312258|||http://purl.uniprot.org/annotation/VAR_035649|||http://purl.uniprot.org/annotation/VAR_047277|||http://purl.uniprot.org/annotation/VSP_050021|||http://purl.uniprot.org/annotation/VSP_050022|||http://purl.uniprot.org/annotation/VSP_050023|||http://purl.uniprot.org/annotation/VSP_050024|||http://purl.uniprot.org/annotation/VSP_050025|||http://purl.uniprot.org/annotation/VSP_050026|||http://purl.uniprot.org/annotation/VSP_050027
http://togogenome.org/gene/9606:TYMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBL3|||http://purl.uniprot.org/uniprot/E5KRG5|||http://purl.uniprot.org/uniprot/P19971                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Disordered|||In MTDPS1.|||In isoform 2.|||Phosphothreonine|||Pyrimidine nucleoside phosphorylase C-terminal|||R-A-L-X-X-A-L-V-L|||R-V-A-A-A-L-X(5,6)-L-G-R|||Reduced catalytic activity.|||Thymidine phosphorylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035874|||http://purl.uniprot.org/annotation/PRO_0000035875|||http://purl.uniprot.org/annotation/VAR_007643|||http://purl.uniprot.org/annotation/VAR_007644|||http://purl.uniprot.org/annotation/VAR_007645|||http://purl.uniprot.org/annotation/VAR_007646|||http://purl.uniprot.org/annotation/VAR_007647|||http://purl.uniprot.org/annotation/VAR_007648|||http://purl.uniprot.org/annotation/VAR_016777|||http://purl.uniprot.org/annotation/VSP_045556
http://togogenome.org/gene/9606:DLGAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15398                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disks large-associated protein 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174299|||http://purl.uniprot.org/annotation/VAR_023774|||http://purl.uniprot.org/annotation/VAR_057718|||http://purl.uniprot.org/annotation/VAR_057719|||http://purl.uniprot.org/annotation/VAR_062147|||http://purl.uniprot.org/annotation/VSP_015550|||http://purl.uniprot.org/annotation/VSP_045341
http://togogenome.org/gene/9606:YPEL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61236                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein yippee-like 3|||Yippee                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212389|||http://purl.uniprot.org/annotation/VSP_037276
http://togogenome.org/gene/9606:BIVM-ERCC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FZ7|||http://purl.uniprot.org/uniprot/R4GMW8                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||XPG N-terminal|||XPG-I                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:GRIN3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60391|||http://purl.uniprot.org/uniprot/Q5F0I5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 3B|||Helical|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011570|||http://purl.uniprot.org/annotation/PRO_5027165552|||http://purl.uniprot.org/annotation/VAR_019676|||http://purl.uniprot.org/annotation/VAR_019677|||http://purl.uniprot.org/annotation/VAR_019678|||http://purl.uniprot.org/annotation/VAR_019679|||http://purl.uniprot.org/annotation/VAR_019680|||http://purl.uniprot.org/annotation/VAR_061188|||http://purl.uniprot.org/annotation/VAR_079909|||http://purl.uniprot.org/annotation/VAR_079910|||http://purl.uniprot.org/annotation/VAR_079911|||http://purl.uniprot.org/annotation/VAR_079912|||http://purl.uniprot.org/annotation/VAR_079913|||http://purl.uniprot.org/annotation/VAR_079914|||http://purl.uniprot.org/annotation/VAR_079915|||http://purl.uniprot.org/annotation/VAR_079916|||http://purl.uniprot.org/annotation/VAR_079917|||http://purl.uniprot.org/annotation/VAR_079918|||http://purl.uniprot.org/annotation/VAR_079919|||http://purl.uniprot.org/annotation/VAR_079920|||http://purl.uniprot.org/annotation/VAR_079921|||http://purl.uniprot.org/annotation/VAR_079922|||http://purl.uniprot.org/annotation/VAR_079923|||http://purl.uniprot.org/annotation/VAR_079924|||http://purl.uniprot.org/annotation/VAR_079925|||http://purl.uniprot.org/annotation/VAR_079926|||http://purl.uniprot.org/annotation/VAR_079927|||http://purl.uniprot.org/annotation/VAR_079928
http://togogenome.org/gene/9606:NFXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1Q2B0|||http://purl.uniprot.org/uniprot/Q6ZNB6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||NF-X1-type 1|||NF-X1-type 10|||NF-X1-type 2|||NF-X1-type 3|||NF-X1-type 4|||NF-X1-type 5|||NF-X1-type 6|||NF-X1-type 7|||NF-X1-type 8|||NF-X1-type 9|||NF-X1-type zinc finger protein NFXL1|||Phosphoserine|||Polar residues|||RING-type|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278827|||http://purl.uniprot.org/annotation/VAR_030869|||http://purl.uniprot.org/annotation/VSP_023410|||http://purl.uniprot.org/annotation/VSP_023411
http://togogenome.org/gene/9606:IMMP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0S9|||http://purl.uniprot.org/uniprot/Q96T52                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial inner membrane protease subunit 2|||Peptidase S26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259577|||http://purl.uniprot.org/annotation/VSP_021474|||http://purl.uniprot.org/annotation/VSP_021475
http://togogenome.org/gene/9606:JPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VZ3|||http://purl.uniprot.org/uniprot/Q9BR39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Cleavage; by calpain|||Cytoplasmic|||Disordered|||Does not affect protein conformation as shown by circular dichroism.|||Helical|||Helical; Anchor for type IV membrane protein|||In CMD2E; unknown pathological significance.|||In CMH17.|||In CMH17; modifies the secondary structure of the protein which is more flexible but does not undergo structural transition upon binding to membrane lipids; increases the affinity for phosphatidylserine; affects intracellular calcium handling and homeostasis.|||In CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis.|||In CMH17; results in vacuolization of intracellular structures and cardiomyocyte hypertrophy; affects intracellular calcium handling and homeostasis. Greatly reduced phosphorylation. Increased myotube diameter. Reduced RYR1 activity and EC gain. Disruption of interaction with TRPC3.|||In CMH17; unknown pathological significance.|||In isoform 2.|||Junctophilin-2|||Junctophilin-2 N-terminal fragment|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a patient with atrial fibrillation.|||Probable disease-associated variant found in a patient with dilated cardiomyopathy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159847|||http://purl.uniprot.org/annotation/PRO_0000446375|||http://purl.uniprot.org/annotation/VAR_053447|||http://purl.uniprot.org/annotation/VAR_065471|||http://purl.uniprot.org/annotation/VAR_065472|||http://purl.uniprot.org/annotation/VAR_065473|||http://purl.uniprot.org/annotation/VAR_065474|||http://purl.uniprot.org/annotation/VAR_065475|||http://purl.uniprot.org/annotation/VAR_081287|||http://purl.uniprot.org/annotation/VAR_081288|||http://purl.uniprot.org/annotation/VAR_081289|||http://purl.uniprot.org/annotation/VAR_081290|||http://purl.uniprot.org/annotation/VAR_086117|||http://purl.uniprot.org/annotation/VSP_002785|||http://purl.uniprot.org/annotation/VSP_002786
http://togogenome.org/gene/9606:ZGRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YA3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRF-type|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Protein ZGRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286626|||http://purl.uniprot.org/annotation/VAR_032147|||http://purl.uniprot.org/annotation/VAR_032148|||http://purl.uniprot.org/annotation/VAR_032149|||http://purl.uniprot.org/annotation/VAR_037862|||http://purl.uniprot.org/annotation/VAR_037863|||http://purl.uniprot.org/annotation/VAR_037864|||http://purl.uniprot.org/annotation/VSP_053232|||http://purl.uniprot.org/annotation/VSP_053233|||http://purl.uniprot.org/annotation/VSP_053234|||http://purl.uniprot.org/annotation/VSP_053235|||http://purl.uniprot.org/annotation/VSP_053236|||http://purl.uniprot.org/annotation/VSP_053237|||http://purl.uniprot.org/annotation/VSP_053238|||http://purl.uniprot.org/annotation/VSP_053239|||http://purl.uniprot.org/annotation/VSP_053240|||http://purl.uniprot.org/annotation/VSP_053241|||http://purl.uniprot.org/annotation/VSP_053242|||http://purl.uniprot.org/annotation/VSP_053243|||http://purl.uniprot.org/annotation/VSP_053244
http://togogenome.org/gene/9606:HTR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50406                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068974
http://togogenome.org/gene/9606:ADRA2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18825|||http://purl.uniprot.org/uniprot/Q4W594                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-2C adrenergic receptor|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Implicated in catechol agonist binding and receptor activation|||Implicated in ligand binding|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069105|||http://purl.uniprot.org/annotation/VAR_012747
http://togogenome.org/gene/9606:PLP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04941                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Proteolipid protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156819|||http://purl.uniprot.org/annotation/VAR_011924|||http://purl.uniprot.org/annotation/VSP_041602
http://togogenome.org/gene/9606:ENPP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AMP-threonine intermediate|||Bis(5'-adenosyl)-triphosphatase ENPP4|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324795|||http://purl.uniprot.org/annotation/VAR_039884|||http://purl.uniprot.org/annotation/VAR_039885|||http://purl.uniprot.org/annotation/VAR_039886
http://togogenome.org/gene/9606:OR5B17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVL8|||http://purl.uniprot.org/uniprot/Q8NGF7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5B17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150588|||http://purl.uniprot.org/annotation/VAR_034219|||http://purl.uniprot.org/annotation/VAR_053193
http://togogenome.org/gene/9606:LECT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14960                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Leukocyte cell-derived chemotaxin-2|||No metalloendopeptidase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017364|||http://purl.uniprot.org/annotation/VAR_011386
http://togogenome.org/gene/9606:SOX30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXW7|||http://purl.uniprot.org/uniprot/O94993                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HMG box|||In isoform 2.|||Polar residues|||Pro residues|||Transcription factor SOX-30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048773|||http://purl.uniprot.org/annotation/VAR_024485|||http://purl.uniprot.org/annotation/VAR_049563|||http://purl.uniprot.org/annotation/VSP_002205|||http://purl.uniprot.org/annotation/VSP_002206
http://togogenome.org/gene/9606:PCDHA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Polar residues|||Protocadherin alpha-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003902|||http://purl.uniprot.org/annotation/VAR_048535|||http://purl.uniprot.org/annotation/VAR_048536|||http://purl.uniprot.org/annotation/VAR_048537|||http://purl.uniprot.org/annotation/VSP_000690|||http://purl.uniprot.org/annotation/VSP_000691|||http://purl.uniprot.org/annotation/VSP_000692
http://togogenome.org/gene/9606:TEX36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJZ8|||http://purl.uniprot.org/uniprot/E9PJL2|||http://purl.uniprot.org/uniprot/Q5VZQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Domain of unknown function with conserved HDNR motif|||Polar residues|||Testis-expressed protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244088|||http://purl.uniprot.org/annotation/VAR_059615
http://togogenome.org/gene/9606:ATP5F1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25705|||http://purl.uniprot.org/uniprot/V9HW26                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase alpha subunit C-terminal|||ATP synthase subunit alpha, mitochondrial|||ATPase F1/V1/A1 complex alpha/beta subunit N-terminal|||ATPase F1/V1/A1 complex alpha/beta subunit nucleotide-binding|||In COXPD22.|||In MC5DN4.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphothreonine|||Required for activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002424|||http://purl.uniprot.org/annotation/VAR_048369|||http://purl.uniprot.org/annotation/VAR_069769|||http://purl.uniprot.org/annotation/VAR_071982|||http://purl.uniprot.org/annotation/VSP_045129|||http://purl.uniprot.org/annotation/VSP_054688
http://togogenome.org/gene/9606:LHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQE6|||http://purl.uniprot.org/uniprot/P01229                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Glycoprotein hormone subunit beta|||In HH23; lack of receptor binding.|||Lutropin subunit beta|||May be implicated in female infertility.|||More effective in stimulating IP3 but not cAMP production.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000045|||http://purl.uniprot.org/annotation/PRO_0000011726|||http://purl.uniprot.org/annotation/PRO_5010030581|||http://purl.uniprot.org/annotation/VAR_003189|||http://purl.uniprot.org/annotation/VAR_014589|||http://purl.uniprot.org/annotation/VAR_014590|||http://purl.uniprot.org/annotation/VAR_015672|||http://purl.uniprot.org/annotation/VAR_015673|||http://purl.uniprot.org/annotation/VAR_034098
http://togogenome.org/gene/9606:COLEC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWP8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  C-type lectin|||Collagen-like|||Collectin-11|||Disordered|||In 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis.|||In 3MC2; unknown pathological significance.|||In isoform 10.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform 9.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315044|||http://purl.uniprot.org/annotation/VAR_038143|||http://purl.uniprot.org/annotation/VAR_065901|||http://purl.uniprot.org/annotation/VAR_065902|||http://purl.uniprot.org/annotation/VAR_065903|||http://purl.uniprot.org/annotation/VAR_078813|||http://purl.uniprot.org/annotation/VSP_030463|||http://purl.uniprot.org/annotation/VSP_030464|||http://purl.uniprot.org/annotation/VSP_030465|||http://purl.uniprot.org/annotation/VSP_030466|||http://purl.uniprot.org/annotation/VSP_030467|||http://purl.uniprot.org/annotation/VSP_030468|||http://purl.uniprot.org/annotation/VSP_030469|||http://purl.uniprot.org/annotation/VSP_030470|||http://purl.uniprot.org/annotation/VSP_030471|||http://purl.uniprot.org/annotation/VSP_045532
http://togogenome.org/gene/9606:FOXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16676                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Decreased activation of transcription from PGF and C3 promoters.|||Disordered|||Fork-head|||Forkhead box protein D1|||Increased activation of transcription from the C3 promoter but no effect on the PGF promoter.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091811|||http://purl.uniprot.org/annotation/VAR_077596|||http://purl.uniprot.org/annotation/VAR_077597|||http://purl.uniprot.org/annotation/VAR_077598|||http://purl.uniprot.org/annotation/VAR_077599|||http://purl.uniprot.org/annotation/VAR_077600|||http://purl.uniprot.org/annotation/VAR_077601|||http://purl.uniprot.org/annotation/VAR_077602|||http://purl.uniprot.org/annotation/VAR_077603|||http://purl.uniprot.org/annotation/VAR_077604|||http://purl.uniprot.org/annotation/VAR_077605|||http://purl.uniprot.org/annotation/VAR_077606|||http://purl.uniprot.org/annotation/VAR_077607
http://togogenome.org/gene/9606:P3R3URF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWA1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||PIK3R3 upstream open reading frame protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000446328
http://togogenome.org/gene/9606:GPN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  GPN-loop GTPase 3|||Gly-Pro-Asn (GPN)-loop; involved in dimer interface|||In isoform 2.|||In isoform 3.|||Stabilizes the phosphate intermediate; shared with dimeric partner                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304790|||http://purl.uniprot.org/annotation/VAR_035107|||http://purl.uniprot.org/annotation/VAR_035108|||http://purl.uniprot.org/annotation/VSP_028125|||http://purl.uniprot.org/annotation/VSP_047327
http://togogenome.org/gene/9606:RBM28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R753|||http://purl.uniprot.org/uniprot/Q9NW13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ANES.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RNA-binding protein 28|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081785|||http://purl.uniprot.org/annotation/VAR_045654|||http://purl.uniprot.org/annotation/VAR_045655|||http://purl.uniprot.org/annotation/VSP_046111
http://togogenome.org/gene/9606:ANAPC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYG5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 11|||Greatly reduces autoubiquitination activity; in isoform 1.|||In isoform 2.|||RING-type|||Slightly reduces autoubiquitination activity; in isoform 1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055747|||http://purl.uniprot.org/annotation/VSP_012347
http://togogenome.org/gene/9606:ING1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFW2|||http://purl.uniprot.org/uniprot/Q9UK53                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K4me3 binding|||In HNSCC.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibitor of growth protein 1|||PBR|||PHD-type|||Unable to stimulate DNA repair after UV irradiation or promote DNA-damage-induced apoptosis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212661|||http://purl.uniprot.org/annotation/VAR_017420|||http://purl.uniprot.org/annotation/VAR_017421|||http://purl.uniprot.org/annotation/VAR_017422|||http://purl.uniprot.org/annotation/VAR_047097|||http://purl.uniprot.org/annotation/VSP_009126|||http://purl.uniprot.org/annotation/VSP_009127|||http://purl.uniprot.org/annotation/VSP_009128|||http://purl.uniprot.org/annotation/VSP_009129
http://togogenome.org/gene/9606:PPARGC1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 9.|||In isoform B4, isoform B4-8a and isoform B4-3ext.|||In isoform B4-3ext.|||In isoform B4-8a and isoform 8a.|||In isoform B5 and isoform B5-NT.|||In isoform NT-7a and isoform B5-NT.|||Interaction with PPARG|||LXXLL motif|||Mediates interaction with RNF34|||N6-acetyllysine|||Peroxisome proliferator-activated receptor gamma coactivator 1-alpha|||Phosphoserine; by AMPK|||Phosphothreonine; by AMPK|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081732|||http://purl.uniprot.org/annotation/VAR_018450|||http://purl.uniprot.org/annotation/VAR_018451|||http://purl.uniprot.org/annotation/VSP_047684|||http://purl.uniprot.org/annotation/VSP_047685|||http://purl.uniprot.org/annotation/VSP_053724|||http://purl.uniprot.org/annotation/VSP_053725|||http://purl.uniprot.org/annotation/VSP_053726|||http://purl.uniprot.org/annotation/VSP_053727|||http://purl.uniprot.org/annotation/VSP_053728|||http://purl.uniprot.org/annotation/VSP_053729|||http://purl.uniprot.org/annotation/VSP_053770
http://togogenome.org/gene/9606:MFSD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A286YF73|||http://purl.uniprot.org/uniprot/A0A286YFM2|||http://purl.uniprot.org/uniprot/Q8NHS3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased chloride channel activity.|||Dileucine internalization motif|||Disordered|||Extracellular|||Helical|||In CCMD and CLN7; endolysosomal localization; decreased chloride channel activity.|||In CLN7.|||In CLN7; decreased chloride channel activity.|||In CLN7; due to a deletion-insertion mutation at nucleotide level; endolysosomal localization; decreased chloride channel activity.|||In CLN7; endolysosomal localization; decreased chloride channel activity.|||In CLN7; lysosomal localization.|||In isoform 2.|||Major facilitator superfamily (MFS) profile|||Major facilitator superfamily domain-containing protein 8|||Mistargeted to the plasma membrane.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311232|||http://purl.uniprot.org/annotation/VAR_037176|||http://purl.uniprot.org/annotation/VAR_037177|||http://purl.uniprot.org/annotation/VAR_037178|||http://purl.uniprot.org/annotation/VAR_037179|||http://purl.uniprot.org/annotation/VAR_037180|||http://purl.uniprot.org/annotation/VAR_058427|||http://purl.uniprot.org/annotation/VAR_058428|||http://purl.uniprot.org/annotation/VAR_058429|||http://purl.uniprot.org/annotation/VAR_058430|||http://purl.uniprot.org/annotation/VAR_058431|||http://purl.uniprot.org/annotation/VAR_058432|||http://purl.uniprot.org/annotation/VAR_058433|||http://purl.uniprot.org/annotation/VAR_066915|||http://purl.uniprot.org/annotation/VAR_066916|||http://purl.uniprot.org/annotation/VAR_066917|||http://purl.uniprot.org/annotation/VAR_066918|||http://purl.uniprot.org/annotation/VAR_066919|||http://purl.uniprot.org/annotation/VAR_072673|||http://purl.uniprot.org/annotation/VAR_072674|||http://purl.uniprot.org/annotation/VSP_057054|||http://purl.uniprot.org/annotation/VSP_057055|||http://purl.uniprot.org/annotation/VSP_057056|||http://purl.uniprot.org/annotation/VSP_057057
http://togogenome.org/gene/9606:GSK3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49841|||http://purl.uniprot.org/uniprot/Q6FI27                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished serine/threonine-protein kinase activity.|||Abolishes activity toward AXIN1.|||Disordered|||Glycogen synthase kinase-3 beta|||In isoform 2.|||Loss of phosphorylation; abolished inhibition of activity, leading to constitutively active.|||Phosphoserine|||Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Prevents the phosphorylation of phosphate-primed glycogen synthase.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085980|||http://purl.uniprot.org/annotation/VSP_004790
http://togogenome.org/gene/9606:RHBDD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3P4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Rhomboid domain-containing protein 3|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079569|||http://purl.uniprot.org/annotation/VAR_021952|||http://purl.uniprot.org/annotation/VAR_051582
http://togogenome.org/gene/9606:CMIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY22                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  C-Maf-inducing protein|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317628|||http://purl.uniprot.org/annotation/VSP_031108|||http://purl.uniprot.org/annotation/VSP_031109|||http://purl.uniprot.org/annotation/VSP_031110|||http://purl.uniprot.org/annotation/VSP_031111
http://togogenome.org/gene/9606:SPDYA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTT5|||http://purl.uniprot.org/uniprot/Q5MJ70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1.|||Loss of CDK2 activation; when associated with N-97.|||Loss of CDK2 activation; when associated with Q-135.|||Phosphoserine|||Phosphothreonine|||Speedy protein A|||Speedy/Ringo box; Required for CDK-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234112|||http://purl.uniprot.org/annotation/VSP_052027|||http://purl.uniprot.org/annotation/VSP_052028
http://togogenome.org/gene/9606:SDK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58EX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Pro residues|||Protein sidekick-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226978|||http://purl.uniprot.org/annotation/VAR_080771|||http://purl.uniprot.org/annotation/VSP_017522|||http://purl.uniprot.org/annotation/VSP_017523|||http://purl.uniprot.org/annotation/VSP_017524|||http://purl.uniprot.org/annotation/VSP_017525
http://togogenome.org/gene/9606:ZNF555                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEP9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2 and isoform 3.|||In isoform 2.|||KRAB|||Zinc finger protein 555                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234588|||http://purl.uniprot.org/annotation/VAR_026295|||http://purl.uniprot.org/annotation/VAR_054223|||http://purl.uniprot.org/annotation/VAR_054224|||http://purl.uniprot.org/annotation/VAR_054225|||http://purl.uniprot.org/annotation/VSP_018382|||http://purl.uniprot.org/annotation/VSP_018383|||http://purl.uniprot.org/annotation/VSP_018384
http://togogenome.org/gene/9606:SLC10A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EP9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by thrombin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Sodium/bile acid cotransporter 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263742
http://togogenome.org/gene/9606:CRYBB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43320|||http://purl.uniprot.org/uniprot/R4UMM2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-crystallin B2|||Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||C-terminal arm|||Connecting peptide|||In CTRCT3.|||In CTRCT3; unknown pathological significance.|||N-acetylalanine|||N-terminal arm|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057553|||http://purl.uniprot.org/annotation/VAR_038431|||http://purl.uniprot.org/annotation/VAR_084787|||http://purl.uniprot.org/annotation/VAR_084788|||http://purl.uniprot.org/annotation/VAR_084789|||http://purl.uniprot.org/annotation/VAR_084790|||http://purl.uniprot.org/annotation/VAR_084791
http://togogenome.org/gene/9606:CARF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIA7|||http://purl.uniprot.org/uniprot/Q8N187                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Calcium-responsive transcription factor|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076172|||http://purl.uniprot.org/annotation/VSP_016785|||http://purl.uniprot.org/annotation/VSP_016786|||http://purl.uniprot.org/annotation/VSP_016787|||http://purl.uniprot.org/annotation/VSP_055713
http://togogenome.org/gene/9606:LRRC49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7G0|||http://purl.uniprot.org/uniprot/Q8IUZ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||Leucine-rich repeat-containing protein 49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233034|||http://purl.uniprot.org/annotation/VSP_044747|||http://purl.uniprot.org/annotation/VSP_046801|||http://purl.uniprot.org/annotation/VSP_055653
http://togogenome.org/gene/9606:RAB3GAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2M9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MARTS1; abolishes GEF activity towards RAB18.|||In MARTS1; may cause exon skipping.|||In WARBM2.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Rab3 GTPase-activating protein non-catalytic subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191662|||http://purl.uniprot.org/annotation/VAR_021588|||http://purl.uniprot.org/annotation/VAR_021589|||http://purl.uniprot.org/annotation/VAR_029881|||http://purl.uniprot.org/annotation/VAR_066675|||http://purl.uniprot.org/annotation/VAR_086021|||http://purl.uniprot.org/annotation/VSP_013311|||http://purl.uniprot.org/annotation/VSP_013312
http://togogenome.org/gene/9606:PSMB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49721                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmethionine|||Proteasome subunit beta type-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148043
http://togogenome.org/gene/9606:MAML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92585                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Mastermind-like protein 1|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Required for interaction with NOTCH proteins                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129493|||http://purl.uniprot.org/annotation/VAR_029010|||http://purl.uniprot.org/annotation/VAR_061335
http://togogenome.org/gene/9606:PDXDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHL7|||http://purl.uniprot.org/uniprot/Q6P996|||http://purl.uniprot.org/uniprot/Q86XE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pyridoxal-dependent decarboxylase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297677|||http://purl.uniprot.org/annotation/VAR_059252|||http://purl.uniprot.org/annotation/VSP_027341|||http://purl.uniprot.org/annotation/VSP_027342|||http://purl.uniprot.org/annotation/VSP_027343|||http://purl.uniprot.org/annotation/VSP_055731|||http://purl.uniprot.org/annotation/VSP_055732|||http://purl.uniprot.org/annotation/VSP_055733|||http://purl.uniprot.org/annotation/VSP_055734
http://togogenome.org/gene/9606:BMPR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAE3|||http://purl.uniprot.org/uniprot/O00238                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein receptor type-1B|||Cytoplasmic|||Disordered|||Extracellular|||GS|||Helical|||In AMD3; mouse BMPR1B construct containing this mutation shows loss of GDF5-dependent receptor activation, chicken BMPR1B construct containing this mutation does not show reduced chondrocyte differentiation, mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization.|||In AMD3; unknown pathological significance; mouse BMPR1B construct containing this mutation shows reduced GDF5-dependent receptor activation, mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization.|||In BDA1D; acts in a dominant-negative manner.|||In BDA2; in animal models loss of kinase activity and loss of positive regulation of chondrocyte differentiation.|||In BDA2; in animal models no effect on kinase activity but strongly decreased positive regulation of chondrocyte differentiation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In brachydactyly type C and BDA2; with also additional features of symphalangism-1.|||In isoform 2.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024412|||http://purl.uniprot.org/annotation/VAR_023819|||http://purl.uniprot.org/annotation/VAR_023820|||http://purl.uniprot.org/annotation/VAR_037967|||http://purl.uniprot.org/annotation/VAR_041401|||http://purl.uniprot.org/annotation/VAR_041402|||http://purl.uniprot.org/annotation/VAR_041403|||http://purl.uniprot.org/annotation/VAR_041404|||http://purl.uniprot.org/annotation/VAR_041405|||http://purl.uniprot.org/annotation/VAR_075520|||http://purl.uniprot.org/annotation/VAR_075521|||http://purl.uniprot.org/annotation/VAR_076406|||http://purl.uniprot.org/annotation/VSP_045100
http://togogenome.org/gene/9606:ADAMTS19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1X7SBR9|||http://purl.uniprot.org/uniprot/Q8TE59                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 19|||Basic and acidic residues|||Cysteine switch|||Disintegrin|||Disordered|||In CVDP2.|||In CVDP2; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Pro residues|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029202|||http://purl.uniprot.org/annotation/PRO_0000029203|||http://purl.uniprot.org/annotation/PRO_5010852630|||http://purl.uniprot.org/annotation/VAR_024599|||http://purl.uniprot.org/annotation/VAR_036154|||http://purl.uniprot.org/annotation/VAR_057087|||http://purl.uniprot.org/annotation/VAR_087790|||http://purl.uniprot.org/annotation/VAR_087791|||http://purl.uniprot.org/annotation/VAR_087792
http://togogenome.org/gene/9606:RUSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GQ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||Phosphothreonine|||RUS family member 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282930|||http://purl.uniprot.org/annotation/VAR_031439|||http://purl.uniprot.org/annotation/VAR_036485|||http://purl.uniprot.org/annotation/VSP_024255|||http://purl.uniprot.org/annotation/VSP_024256
http://togogenome.org/gene/9606:PPFIA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7Y5|||http://purl.uniprot.org/uniprot/G3V200|||http://purl.uniprot.org/uniprot/H0YHK3|||http://purl.uniprot.org/uniprot/O75334|||http://purl.uniprot.org/uniprot/Q4LE62                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4 and isoform 5.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 7.|||In isoform 8.|||Liprin-alpha-2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191027|||http://purl.uniprot.org/annotation/VSP_043819|||http://purl.uniprot.org/annotation/VSP_043820|||http://purl.uniprot.org/annotation/VSP_043821|||http://purl.uniprot.org/annotation/VSP_043822|||http://purl.uniprot.org/annotation/VSP_043823|||http://purl.uniprot.org/annotation/VSP_046718|||http://purl.uniprot.org/annotation/VSP_046719|||http://purl.uniprot.org/annotation/VSP_046720|||http://purl.uniprot.org/annotation/VSP_046721|||http://purl.uniprot.org/annotation/VSP_046722|||http://purl.uniprot.org/annotation/VSP_046723
http://togogenome.org/gene/9606:MRPS35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82673                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondrion|||Small ribosomal subunit protein mS35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046055|||http://purl.uniprot.org/annotation/VAR_052051|||http://purl.uniprot.org/annotation/VSP_054096|||http://purl.uniprot.org/annotation/VSP_054097
http://togogenome.org/gene/9606:TTC21B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0TA66|||http://purl.uniprot.org/uniprot/A0A7P0TB61|||http://purl.uniprot.org/uniprot/A8KA77|||http://purl.uniprot.org/uniprot/Q7Z4L5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a frameshift mutation and variant M-501 in BBS12; hypomorphic variant in vitro.|||Found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a frameshift mutation and variant P-34 in BBS10; hypomorphic variant in vitro.|||Found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries a homozygous frameshift mutation in BBS7; hypomorphic variant in vitro.|||Found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patient also carries two mutations in BBS6; hypomorphic variant in vitro.|||Found in a patient with Bardet-Biedl syndrome; probably acts as disease modifier; the patients also carries two mutations in BBS1; functionally null mutation in vitro.|||Found in a patient with Meckel-Gruber like syndrome also carrying L-222 on the same allele and variant G-1183 in RPGRIP1L; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber like syndrome also carrying variant C-671 in BBS7; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber like syndrome also carrying variant V-280 on the same allele and variant G-1183 in RPGRIP1L; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber like syndrome carrying variant D-559 in BBS1 and a variant in CC2D2A; unknown pathological significance; functionally null mutation in vitro.|||Found in a patient with Meckel-Gruber like syndrome; also found in patients with Bardet-Bied syndrome; also found in a patient with nephronophthisis with extra-renal features; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber like syndrome; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber syndrome also carrying C-347 on the same allele; unknown pathological significance; functionally null mutation in vitro.|||Found in a patient with Meckel-Gruber syndrome also carrying N-1041 on the same allele; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber syndrome also carrying a homozygous variant in CC2D2A; also found in a patient with short-rib thoracic dysplasia without polydactyly compoud heterozygous for causative mutations in IFT81; probably acts as disease modifier; functionally null mutation in vitro.|||Found in a patient with Meckel-Gruber syndrome also carrying a mutation in CC2D2A; unknown pathological significance; hypomorphic variant in vitro.|||Found in a patient with Meckel-Gruber syndrome; unknown pathological significance; functionally null mutation in vitro.|||Functionally null mutation in vitro.|||Hypomorphic variant in vitro.|||In JBTS11.|||In JBTS11; functionally null mutation in vitro.|||In JBTS11; hypomorphic variant in vitro.|||In NPHP12; also found in a patient with Bardet-Biedl syndrome carrying two variants in BBS4; hypomorphic variant in vitro.|||In NPHP12; hypomorphic variant in vitro.|||In NPHP12; unknown pathological significance; functionally null mutation in vitro.|||In NPHP12; with extra-renal features; functionally null mutation in vitro.|||In SRTD4 and NPHP12; also found in a patient with Bardet-Biedl syndrome carrying variants L-159 and T-346 in BBS12; also found in a patient with Meckel-Gruber syndrome carrying a homozygous variant in TMEM216; hypomorphic variant in vitro.|||In SRTD4; functionally null mutation in vitro.|||In isoform 2.|||TPR|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 17|||TPR 18|||TPR 19|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 21B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291917|||http://purl.uniprot.org/annotation/VAR_032888|||http://purl.uniprot.org/annotation/VAR_032889|||http://purl.uniprot.org/annotation/VAR_032890|||http://purl.uniprot.org/annotation/VAR_032891|||http://purl.uniprot.org/annotation/VAR_032892|||http://purl.uniprot.org/annotation/VAR_065514|||http://purl.uniprot.org/annotation/VAR_065515|||http://purl.uniprot.org/annotation/VAR_065516|||http://purl.uniprot.org/annotation/VAR_065517|||http://purl.uniprot.org/annotation/VAR_065518|||http://purl.uniprot.org/annotation/VAR_065519|||http://purl.uniprot.org/annotation/VAR_065520|||http://purl.uniprot.org/annotation/VAR_065521|||http://purl.uniprot.org/annotation/VAR_065522|||http://purl.uniprot.org/annotation/VAR_065523|||http://purl.uniprot.org/annotation/VAR_065524|||http://purl.uniprot.org/annotation/VAR_065525|||http://purl.uniprot.org/annotation/VAR_065526|||http://purl.uniprot.org/annotation/VAR_065527|||http://purl.uniprot.org/annotation/VAR_065528|||http://purl.uniprot.org/annotation/VAR_065529|||http://purl.uniprot.org/annotation/VAR_065530|||http://purl.uniprot.org/annotation/VAR_065531|||http://purl.uniprot.org/annotation/VAR_065532|||http://purl.uniprot.org/annotation/VAR_065533|||http://purl.uniprot.org/annotation/VAR_065534|||http://purl.uniprot.org/annotation/VAR_065535|||http://purl.uniprot.org/annotation/VAR_065536|||http://purl.uniprot.org/annotation/VAR_065537|||http://purl.uniprot.org/annotation/VAR_065538|||http://purl.uniprot.org/annotation/VAR_065539|||http://purl.uniprot.org/annotation/VAR_065540|||http://purl.uniprot.org/annotation/VAR_065541|||http://purl.uniprot.org/annotation/VAR_065542|||http://purl.uniprot.org/annotation/VAR_065543|||http://purl.uniprot.org/annotation/VAR_065544|||http://purl.uniprot.org/annotation/VAR_065545|||http://purl.uniprot.org/annotation/VAR_065546|||http://purl.uniprot.org/annotation/VAR_065547|||http://purl.uniprot.org/annotation/VAR_065548|||http://purl.uniprot.org/annotation/VAR_065549|||http://purl.uniprot.org/annotation/VAR_065550|||http://purl.uniprot.org/annotation/VAR_065551|||http://purl.uniprot.org/annotation/VAR_065552|||http://purl.uniprot.org/annotation/VAR_065553|||http://purl.uniprot.org/annotation/VAR_068172|||http://purl.uniprot.org/annotation/VSP_026306|||http://purl.uniprot.org/annotation/VSP_026307
http://togogenome.org/gene/9606:TMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82094|||http://purl.uniprot.org/uniprot/Q6PII6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with Elongin BC complex|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly reduced the ubiquitination directing activity of the protein.|||TATA element modulatory factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072589|||http://purl.uniprot.org/annotation/VAR_024284|||http://purl.uniprot.org/annotation/VAR_051439|||http://purl.uniprot.org/annotation/VAR_051440|||http://purl.uniprot.org/annotation/VAR_051441|||http://purl.uniprot.org/annotation/VSP_037411
http://togogenome.org/gene/9606:ZNF112                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VG01|||http://purl.uniprot.org/uniprot/Q9UJU3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 112                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047469|||http://purl.uniprot.org/annotation/VAR_057377|||http://purl.uniprot.org/annotation/VAR_057378|||http://purl.uniprot.org/annotation/VAR_057379|||http://purl.uniprot.org/annotation/VAR_057380|||http://purl.uniprot.org/annotation/VAR_060414|||http://purl.uniprot.org/annotation/VAR_060415|||http://purl.uniprot.org/annotation/VAR_060416|||http://purl.uniprot.org/annotation/VSP_039929
http://togogenome.org/gene/9606:SSR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51571                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Lumenal|||Translocon-associated protein subunit delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033292|||http://purl.uniprot.org/annotation/VAR_064161
http://togogenome.org/gene/9606:CCT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50990|||http://purl.uniprot.org/uniprot/Q7Z759                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||T-complex protein 1 subunit theta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128373|||http://purl.uniprot.org/annotation/VAR_052270|||http://purl.uniprot.org/annotation/VAR_052271|||http://purl.uniprot.org/annotation/VSP_054691|||http://purl.uniprot.org/annotation/VSP_054692
http://togogenome.org/gene/9606:MSMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08118                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-microseminoprotein|||In isoform PSP57.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019268|||http://purl.uniprot.org/annotation/VAR_011935|||http://purl.uniprot.org/annotation/VAR_011936|||http://purl.uniprot.org/annotation/VAR_011937|||http://purl.uniprot.org/annotation/VAR_011938|||http://purl.uniprot.org/annotation/VAR_011939|||http://purl.uniprot.org/annotation/VAR_011940|||http://purl.uniprot.org/annotation/VAR_011941|||http://purl.uniprot.org/annotation/VAR_011942|||http://purl.uniprot.org/annotation/VAR_011943|||http://purl.uniprot.org/annotation/VSP_003275|||http://purl.uniprot.org/annotation/VSP_003276
http://togogenome.org/gene/9606:HIGD1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MV81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||HIG1|||HIG1 domain family member 1C|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342673
http://togogenome.org/gene/9606:TPRKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EKC/KEOPS complex subunit TPRKB|||In GAMOS5.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279220|||http://purl.uniprot.org/annotation/VAR_080355|||http://purl.uniprot.org/annotation/VAR_080356|||http://purl.uniprot.org/annotation/VSP_023414|||http://purl.uniprot.org/annotation/VSP_023415
http://togogenome.org/gene/9606:FAM162A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A26|||http://purl.uniprot.org/uniprot/Q9H2P1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein FAM162A|||Required for proapoptotic activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254635|||http://purl.uniprot.org/annotation/VAR_028849
http://togogenome.org/gene/9606:EFNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52798                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ephrin RBD|||Ephrin-A4|||GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008373|||http://purl.uniprot.org/annotation/PRO_0000008374|||http://purl.uniprot.org/annotation/VSP_001448|||http://purl.uniprot.org/annotation/VSP_046707
http://togogenome.org/gene/9606:C5orf34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MH7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Uncharacterized protein C5orf34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295897|||http://purl.uniprot.org/annotation/VAR_035618
http://togogenome.org/gene/9606:ABHD17C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCB6                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Alpha/beta hydrolase domain-containing protein 17C|||Charge relay system|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297513|||http://purl.uniprot.org/annotation/VSP_027273
http://togogenome.org/gene/9606:RNASE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12724                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Eosinophil cationic protein|||Loss of in vitro formation of amyloid-like aggregates.|||May be involved in LPS- and LTA-binding|||May be involved in LPS-binding|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Proton donor|||Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030862|||http://purl.uniprot.org/annotation/VAR_013149|||http://purl.uniprot.org/annotation/VAR_014109|||http://purl.uniprot.org/annotation/VAR_029017
http://togogenome.org/gene/9606:GHITM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3K2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Growth hormone-inducible transmembrane protein|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179119
http://togogenome.org/gene/9606:NRGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92686                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Peptide|||Region|||Site                                                                                  ^@                                                                                  Citrulline; partial|||Collagen-like|||Crucial for interaction with calmodulin|||Disordered|||IQ|||N-acetylmethionine|||NEUG(55-78)|||Neurogranin|||Omega-N-methylarginine|||Phosphoserine; by PHK and PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159591|||http://purl.uniprot.org/annotation/PRO_0000377703
http://togogenome.org/gene/9606:KATNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7S5|||http://purl.uniprot.org/uniprot/O75449                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Abolishes ATP dependent microtubule severing activity and localization to spindle poles.|||Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308.|||Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309.|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with KATNB1|||Interaction with dynein and NDEL1|||Interaction with microtubules|||Katanin p60 ATPase-containing subunit A1|||Phosphoserine|||Phosphoserine; by DYRK2|||Phosphothreonine; by DYRK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084594|||http://purl.uniprot.org/annotation/VSP_012948|||http://purl.uniprot.org/annotation/VSP_012949|||http://purl.uniprot.org/annotation/VSP_012950
http://togogenome.org/gene/9606:MAP3K20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D4Q8H0|||http://purl.uniprot.org/uniprot/Q9NYL2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished association with BTRC without affecting protein stability.|||Acidic residues|||Basic and acidic residues|||C-terminal domain (CTD)|||Disordered|||In CNM6; decrease of protein abundance.|||In CNM6; unknown pathological significance.|||In SFMMP; mild destabilization of the protein.|||In SFMMP; produces protein aggregation.|||In an ovarian endometrioid sample; somatic mutation.|||In isoform 3.|||In isoform ZAKbeta.|||Leucine-zipper|||Loss of autophosphorylation activity.|||Loss of kinase activity. Does not affect ability to activate EIF2AK4/GCN2 in response to mild ribosome collision.|||Mimics phosphorylation; impaired ribosome-binding.|||Mitogen-activated protein kinase kinase kinase 20|||N-acetylserine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||SAM|||Sensing domain (S)|||Slight loss of autophosphorylation activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086338|||http://purl.uniprot.org/annotation/VAR_022827|||http://purl.uniprot.org/annotation/VAR_040806|||http://purl.uniprot.org/annotation/VAR_040807|||http://purl.uniprot.org/annotation/VAR_040808|||http://purl.uniprot.org/annotation/VAR_040809|||http://purl.uniprot.org/annotation/VAR_040810|||http://purl.uniprot.org/annotation/VAR_040811|||http://purl.uniprot.org/annotation/VAR_040812|||http://purl.uniprot.org/annotation/VAR_076448|||http://purl.uniprot.org/annotation/VAR_080563|||http://purl.uniprot.org/annotation/VAR_080564|||http://purl.uniprot.org/annotation/VAR_082158|||http://purl.uniprot.org/annotation/VAR_087102|||http://purl.uniprot.org/annotation/VSP_051741|||http://purl.uniprot.org/annotation/VSP_051742|||http://purl.uniprot.org/annotation/VSP_051743|||http://purl.uniprot.org/annotation/VSP_051744
http://togogenome.org/gene/9606:A4GALT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5J1|||http://purl.uniprot.org/uniprot/Q9NPC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha 1,4-glycosyltransferase|||Cytoplasmic|||DXD motif|||Helical|||Helical; Signal-anchor for type II membrane protein|||In individuals with NOR polyagglutination syndrome; causes the synthesis of both Gal(alpha1-4)Gal and Gal(alpha1-4)GalNAc moieties.|||In p individuals.|||In p individuals; complete loss of activity.|||In p individuals; partial loss of activity.|||Lactosylceramide 4-alpha-galactosyltransferase|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080578|||http://purl.uniprot.org/annotation/VAR_014296|||http://purl.uniprot.org/annotation/VAR_014297|||http://purl.uniprot.org/annotation/VAR_017507|||http://purl.uniprot.org/annotation/VAR_017508|||http://purl.uniprot.org/annotation/VAR_017509|||http://purl.uniprot.org/annotation/VAR_022320|||http://purl.uniprot.org/annotation/VAR_080910
http://togogenome.org/gene/9606:ANKRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRN9|||http://purl.uniprot.org/uniprot/Q5T457|||http://purl.uniprot.org/uniprot/Q9GZV1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 2|||Disordered|||In isoform 2.|||Loss of interaction and phosphorylation by PKB/AKT2, loss of translocation to the nucleus and loss of function in myocyte differentiation.|||May mediate interaction with PML, p53/TP53 and YBX1|||Phosphoserine; by PKB/AKT2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066897|||http://purl.uniprot.org/annotation/VAR_042498|||http://purl.uniprot.org/annotation/VSP_000269
http://togogenome.org/gene/9606:SHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98077                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  CH1|||Disordered|||PID|||Phosphotyrosine|||Pro residues|||SH2|||SHC-transforming protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097732
http://togogenome.org/gene/9606:ZFPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX07                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||CCHC FOG-type 1|||CCHC FOG-type 2|||CCHC FOG-type 3|||CCHC FOG-type 4|||CCHC FOG-type 5|||Disordered|||Interaction with CTBP2|||Interaction with TACC3|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein ZFPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221041|||http://purl.uniprot.org/annotation/VAR_057491
http://togogenome.org/gene/9606:COL16A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07092                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Collagen alpha-1(XVI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Disordered|||In isoform 2.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region 1 (NC1)|||Nonhelical region 10 (NC10)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Nonhelical region 4 (NC4)|||Nonhelical region 5 (NC5)|||Nonhelical region 6 (NC6)|||Nonhelical region 7 (NC7)|||Nonhelical region 8 (NC8)|||Nonhelical region 9 (NC9)|||Pro residues|||Triple-helical region 1 (COL1) with 2 imperfections|||Triple-helical region 2 (COL2) with 2 imperfections|||Triple-helical region 3 (COL3)|||Triple-helical region 4 (COL4) with 2 imperfections|||Triple-helical region 5 (COL5) with 3 imperfections|||Triple-helical region 6 (COL6) with 1 imperfection|||Triple-helical region 7 (COL7) with 1 imperfection|||Triple-helical region 8 (COL8) with 1 imperfection|||Triple-helical region 9 (COL9) with 3 imperfections                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005792|||http://purl.uniprot.org/annotation/VAR_031440|||http://purl.uniprot.org/annotation/VAR_048778|||http://purl.uniprot.org/annotation/VAR_048779|||http://purl.uniprot.org/annotation/VSP_024259|||http://purl.uniprot.org/annotation/VSP_024260
http://togogenome.org/gene/9606:OXGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R986|||http://purl.uniprot.org/uniprot/Q96P68                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  2-oxoglutarate receptor 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069994
http://togogenome.org/gene/9606:GKN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XP6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BRICHOS|||Gastrokine-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252104|||http://purl.uniprot.org/annotation/VAR_051012
http://togogenome.org/gene/9606:SHQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CS|||Disordered|||In DYT35; results in decreased H/ACA small nucleolar ribonucleoproteins production when expressed in a heterologous system.|||In NEDDS; results in decreased H/ACA small nucleolar ribonucleoproteins production when expressed in a heterologous system.|||In NEDDS; unknown pathological significance.|||In isoform 2.|||Polar residues|||Protein SHQ1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302822|||http://purl.uniprot.org/annotation/VAR_034962|||http://purl.uniprot.org/annotation/VAR_034963|||http://purl.uniprot.org/annotation/VAR_087400|||http://purl.uniprot.org/annotation/VAR_087401|||http://purl.uniprot.org/annotation/VAR_087402|||http://purl.uniprot.org/annotation/VAR_087403|||http://purl.uniprot.org/annotation/VSP_056105
http://togogenome.org/gene/9606:ACAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15027                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  3'-nitrotyrosine|||ANK 1|||ANK 2|||ANK 3|||Almost abolishes membrane binding.|||Arf-GAP|||Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1|||BAR|||C4-type|||Disordered|||Enhances interaction with ITGB1.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Loss of GAP activity. No effect on GULP1 binding or association with endosomal tubules when coexpressed with PIP5K1C.|||Loss of binding to PIP2 and PIP3. Loss of association with endosomal tubules when coexpressed with PIP5K1C.|||Loss of phosphorylation at S-554, interaction with ITGB1 and ITGB1-dependent cell migration.|||Loss of phosphorylation by PKB, interaction with ITGB1 and ITGB1-dependent cell migration.|||No effect on interaction with ITGB1.|||PH|||Phosphoserine; by PKB|||Preserves membrane binding and ability to tubulate liposomes.|||Prevents interaction with ITGB1 when S-554 is not phosphorylated|||Reduced membrane binding and ability to induce liposome tubulation.|||Required for formation of endosomal tubules when overexpressed with PIP5K1C|||Required for interaction with GULP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074209|||http://purl.uniprot.org/annotation/VAR_036178|||http://purl.uniprot.org/annotation/VAR_036179|||http://purl.uniprot.org/annotation/VAR_048328|||http://purl.uniprot.org/annotation/VAR_048329
http://togogenome.org/gene/9606:ANKRD36B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2N9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat domain-containing protein 36B|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243912|||http://purl.uniprot.org/annotation/VAR_057818|||http://purl.uniprot.org/annotation/VAR_060687|||http://purl.uniprot.org/annotation/VAR_060688|||http://purl.uniprot.org/annotation/VSP_039666|||http://purl.uniprot.org/annotation/VSP_039667|||http://purl.uniprot.org/annotation/VSP_039668|||http://purl.uniprot.org/annotation/VSP_039669|||http://purl.uniprot.org/annotation/VSP_039670|||http://purl.uniprot.org/annotation/VSP_039671
http://togogenome.org/gene/9606:C2CD4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 calcium-dependent domain-containing protein 4B|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324306|||http://purl.uniprot.org/annotation/VAR_039696|||http://purl.uniprot.org/annotation/VAR_039697
http://togogenome.org/gene/9606:TMEM132D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14C87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287100|||http://purl.uniprot.org/annotation/VAR_032264|||http://purl.uniprot.org/annotation/VAR_053887|||http://purl.uniprot.org/annotation/VAR_053888|||http://purl.uniprot.org/annotation/VSP_025307|||http://purl.uniprot.org/annotation/VSP_025308
http://togogenome.org/gene/9606:SPIRE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KIND|||Phosphoserine|||Polar residues|||Protein spire homolog 2|||Spir-box|||WH2 1|||WH2 2|||WH2 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320023|||http://purl.uniprot.org/annotation/VSP_031568|||http://purl.uniprot.org/annotation/VSP_031569|||http://purl.uniprot.org/annotation/VSP_031570|||http://purl.uniprot.org/annotation/VSP_031571|||http://purl.uniprot.org/annotation/VSP_031572
http://togogenome.org/gene/9606:PRR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQA4|||http://purl.uniprot.org/uniprot/P79522|||http://purl.uniprot.org/uniprot/Q96QB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||In isoform 2.|||Pro residues|||Proline-rich protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213889|||http://purl.uniprot.org/annotation/VAR_052963|||http://purl.uniprot.org/annotation/VSP_012818
http://togogenome.org/gene/9606:TNFSF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43557                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Tumor necrosis factor ligand superfamily member 14, membrane form|||Tumor necrosis factor ligand superfamily member 14, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034532|||http://purl.uniprot.org/annotation/PRO_0000034533|||http://purl.uniprot.org/annotation/VAR_027677|||http://purl.uniprot.org/annotation/VAR_027678|||http://purl.uniprot.org/annotation/VAR_027679|||http://purl.uniprot.org/annotation/VSP_006452
http://togogenome.org/gene/9606:ZNF516                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2YDX2|||http://purl.uniprot.org/uniprot/Q92618                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mediates promoter DNA-binding and activation of transcription|||Polar residues|||Pro residues|||Zinc finger protein 516                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047634|||http://purl.uniprot.org/annotation/VAR_052852|||http://purl.uniprot.org/annotation/VAR_052853
http://togogenome.org/gene/9606:POLR1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15446                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerase I subunit RPA34|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228120|||http://purl.uniprot.org/annotation/VAR_051875|||http://purl.uniprot.org/annotation/VAR_051876|||http://purl.uniprot.org/annotation/VAR_051877|||http://purl.uniprot.org/annotation/VAR_051878|||http://purl.uniprot.org/annotation/VAR_051879|||http://purl.uniprot.org/annotation/VAR_051880|||http://purl.uniprot.org/annotation/VSP_017673
http://togogenome.org/gene/9606:RPS27A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDW1|||http://purl.uniprot.org/uniprot/P62979                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosylthreonine|||ADP-ribosylglycine|||Abolished monoubiquitination by RNF25, leading to impaired ability to rescue stalled ribosomes; when associated with R-107. Abolished deubiquitination by USP16, without affecting maturation of the 40S ribosomal complex.|||Abolished monoubiquitination by RNF25, leading to impaired ability to rescue stalled ribosomes; when associated with R-113.|||Abolishes HLTF-mediated polyubiquitination of PCNA.|||C4-type|||Disordered|||Essential for function|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interacts with activating enzyme|||Loss of ADP-ribosylation.|||Loss of DTX3L-mediated polyubiquitination of histone H3 and H4.|||N6-acetyllysine|||No effect on ADP-ribosylation, when associated with K-72.|||No effect on ADP-ribosylation, when associated with K-74.|||No effect on ADP-ribosylation.|||No effect on HLTF-mediated polyubiquitination of PCNA.|||Phosphomimetic mutant that binds and activates PRKN.|||Phosphomimetic mutant that can recruit PRKN to mitochondria.|||Phosphoserine; by PINK1|||Prevents phosphorylation in case of mitophagy. Impaired translocation of PRKN to mitochondria.|||Small ribosomal subunit protein eS31|||Ubiquitin|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000396477|||http://purl.uniprot.org/annotation/PRO_0000396478
http://togogenome.org/gene/9606:MOSMO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHV5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Modulator of smoothened protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271082|||http://purl.uniprot.org/annotation/VSP_054465|||http://purl.uniprot.org/annotation/VSP_054466
http://togogenome.org/gene/9606:CEP112                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GYE8|||http://purl.uniprot.org/uniprot/Q8N8E3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 112 kDa|||DUF4485|||In SPGF44; no protein detected in patient cells.|||In SPGF44; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234508|||http://purl.uniprot.org/annotation/VAR_050752|||http://purl.uniprot.org/annotation/VAR_084997|||http://purl.uniprot.org/annotation/VAR_084998|||http://purl.uniprot.org/annotation/VAR_084999|||http://purl.uniprot.org/annotation/VSP_018338|||http://purl.uniprot.org/annotation/VSP_018339
http://togogenome.org/gene/9606:ZNF449                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9G9|||http://purl.uniprot.org/uniprot/Q7Z3P1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||In isoform 2.|||In isoform 3.|||SCAN box|||Zinc finger protein 449                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047597|||http://purl.uniprot.org/annotation/VSP_011949|||http://purl.uniprot.org/annotation/VSP_011950|||http://purl.uniprot.org/annotation/VSP_011951|||http://purl.uniprot.org/annotation/VSP_011952
http://togogenome.org/gene/9606:ZNF35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13682                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Globular domain|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047366
http://togogenome.org/gene/9606:H2AC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FTV9|||http://purl.uniprot.org/uniprot/B2R5B3|||http://purl.uniprot.org/uniprot/P0C0S8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055235
http://togogenome.org/gene/9606:GGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gametogenetin|||In isoform 2.|||In isoform 3.|||Interaction with GGNBP1|||Interactions with ZNF403/GGNBP2 and OAZ3|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239342|||http://purl.uniprot.org/annotation/VSP_019166|||http://purl.uniprot.org/annotation/VSP_019167|||http://purl.uniprot.org/annotation/VSP_019168|||http://purl.uniprot.org/annotation/VSP_019169|||http://purl.uniprot.org/annotation/VSP_019170
http://togogenome.org/gene/9606:CCKBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PIC8|||http://purl.uniprot.org/uniprot/P32239                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Gastrin/cholecystokinin type B receptor|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069474|||http://purl.uniprot.org/annotation/VAR_014684|||http://purl.uniprot.org/annotation/VAR_014685|||http://purl.uniprot.org/annotation/VAR_014686|||http://purl.uniprot.org/annotation/VAR_014687|||http://purl.uniprot.org/annotation/VAR_049388|||http://purl.uniprot.org/annotation/VSP_033444|||http://purl.uniprot.org/annotation/VSP_033445
http://togogenome.org/gene/9606:TCIRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13488                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In OPTB1.|||In isoform Short.|||V-type proton ATPase 116 kDa subunit a 3|||Vacuolar                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119218|||http://purl.uniprot.org/annotation/VAR_019569|||http://purl.uniprot.org/annotation/VAR_019570|||http://purl.uniprot.org/annotation/VAR_020988|||http://purl.uniprot.org/annotation/VAR_020989|||http://purl.uniprot.org/annotation/VAR_020990|||http://purl.uniprot.org/annotation/VAR_020991|||http://purl.uniprot.org/annotation/VAR_054340|||http://purl.uniprot.org/annotation/VAR_054341|||http://purl.uniprot.org/annotation/VSP_000345
http://togogenome.org/gene/9606:OR10Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGQ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150714|||http://purl.uniprot.org/annotation/VAR_024129|||http://purl.uniprot.org/annotation/VAR_062065
http://togogenome.org/gene/9606:ENTREP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P81408|||http://purl.uniprot.org/uniprot/Q9Y6J7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Protein ENTREP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079261|||http://purl.uniprot.org/annotation/VAR_035684|||http://purl.uniprot.org/annotation/VAR_037876|||http://purl.uniprot.org/annotation/VAR_056842|||http://purl.uniprot.org/annotation/VSP_038926|||http://purl.uniprot.org/annotation/VSP_046728|||http://purl.uniprot.org/annotation/VSP_046729
http://togogenome.org/gene/9606:NEUROD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW56|||http://purl.uniprot.org/uniprot/Q9HD90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BHLH|||Disordered|||Neurogenic differentiation factor 4|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127390|||http://purl.uniprot.org/annotation/VAR_012979
http://togogenome.org/gene/9606:TTC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T04|||http://purl.uniprot.org/uniprot/Q8N0Z6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  In NEDCAFD; likely pathogenic.|||In NEDCAFD; likely pathogenic; decreased TTC5 transcript levels.|||In NEDCAFD; unknown pathological significance.|||Loss of interaction with 28S rRNA of ribosome-coding tubulin, when associated with E-285. No change in interaction with N-terminal MREI motif of beta-tubulin nascent chain, when associated with E-285. Loss of tubulin autoregulation and accurate mitosis, when associated with E-285.|||Loss of interaction with 28S rRNA of ribosome-coding tubulin, when associated with E-287. No change in interaction with N-terminal MREI motif of beta-tubulin nascent chain, when associated with E-287. Loss of tubulin autoregulation and accurate mitosis, when associated with E-287.|||Loss of interaction with N-terminal MREI motif of beta-tubulin nascent chain. Loss of interaction with 28S rRNA of ribosome-coding tubulin. Loss of tubulin autoregulation and accurate mitosis.|||Mediates interaction with 28S rRNA of ribosome-coding tubulin|||Mediates interaction with N-terminal MREI motif of beta-tubulin nascent chain|||No change in interaction with 28S rRNA of ribosome-coding tubulin.|||No change in interaction with N-terminal MREI motif of beta-tubulin nascent chain.|||Nuclear export signal|||Partial loss of interaction with N-terminal MREI motif of beta-tubulin nascent chain. Loss of interaction with N-terminal MREI motif of beta-tubulin nascent chain; when associated with A-259.|||Partial loss of interaction with N-terminal MREI motif of beta-tubulin nascent chain. Loss of interaction with N-terminal MREI motif of beta-tubulin nascent chain; when associated with D-225.|||Phosphoserine; by ATM|||Phosphoserine; by CHEK2|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Tetratricopeptide repeat protein 5|||Tetratricopeptide repeat protein 5 OB fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106381|||http://purl.uniprot.org/annotation/VAR_034131|||http://purl.uniprot.org/annotation/VAR_055293|||http://purl.uniprot.org/annotation/VAR_085226|||http://purl.uniprot.org/annotation/VAR_085227|||http://purl.uniprot.org/annotation/VAR_085228|||http://purl.uniprot.org/annotation/VAR_085229
http://togogenome.org/gene/9606:ARHGEF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2K6|||http://purl.uniprot.org/uniprot/E9PMR6|||http://purl.uniprot.org/uniprot/Q9NZN5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form KMT2A/MLL1-ARHGEF12 oncogene|||DH|||Disordered|||In isoform 2.|||N-acetylserine|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||RGSL|||Removed|||Rho guanine nucleotide exchange factor 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080930|||http://purl.uniprot.org/annotation/VAR_020191|||http://purl.uniprot.org/annotation/VSP_008131
http://togogenome.org/gene/9606:KCNJ16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K434|||http://purl.uniprot.org/uniprot/Q8N538|||http://purl.uniprot.org/uniprot/Q9NPI9                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Motif|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In HKTD.|||In HKTD; when coexpressed with KCNJ10 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type.|||In HKTD; when coexpressed with KCNJ10 or KCNJ15 in Xenopus oocytes, it results in decreased channel expression at the surface and reduced potassium current amplitude compared to the wild-type.|||Inward rectifier potassium channel 16|||Inward rectifier potassium channel C-terminal|||Phosphoserine|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154975|||http://purl.uniprot.org/annotation/VAR_024510|||http://purl.uniprot.org/annotation/VAR_085941|||http://purl.uniprot.org/annotation/VAR_085942|||http://purl.uniprot.org/annotation/VAR_085943|||http://purl.uniprot.org/annotation/VAR_085944|||http://purl.uniprot.org/annotation/VAR_085945|||http://purl.uniprot.org/annotation/VAR_085946
http://togogenome.org/gene/9606:EXD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K948|||http://purl.uniprot.org/uniprot/Q86TX3|||http://purl.uniprot.org/uniprot/Q9NVH0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3'-5' exonuclease|||Abolished exodeoxyribonuclease activity.|||Abolished exonuclease activity.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Exonuclease 3'-5' domain-containing protein 2|||Helical|||Impaired exonuclease activity.|||In isoform 2.|||Loss of 3'-5' exonuclease activity. Impaired ability to stabilize and restart stalled replication forks in response to replication stress.|||Mitochondrial intermembrane|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089924|||http://purl.uniprot.org/annotation/VAR_050980|||http://purl.uniprot.org/annotation/VAR_050981|||http://purl.uniprot.org/annotation/VSP_044367
http://togogenome.org/gene/9606:LURAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LR2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 2|||Leucine rich adaptor protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271078
http://togogenome.org/gene/9606:ALG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92685                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase|||Helical|||In CDG1D.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080566|||http://purl.uniprot.org/annotation/VAR_010306|||http://purl.uniprot.org/annotation/VAR_037805|||http://purl.uniprot.org/annotation/VAR_037806|||http://purl.uniprot.org/annotation/VSP_042738
http://togogenome.org/gene/9606:SETD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Repeat|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Histone H3K4 binding|||Histone-lysine N-methyltransferase SETD7|||Increases near-attack conformations.|||Induces a reduction in methyltransferase activity toward TAF10 but an increased methyltransferase activity for H3 and p53/TP53.|||MORN 1|||MORN 2|||MORN 3|||SET|||Significantly reduces the catalytic activity.|||Significantly reduces the monomethyltransferase activity but increases the dimethyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186054
http://togogenome.org/gene/9606:PDE7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13946                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A|||In isoform PDE7A2.|||In isoform PDE7A3.|||PDEase|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198833|||http://purl.uniprot.org/annotation/VAR_056661|||http://purl.uniprot.org/annotation/VSP_004593|||http://purl.uniprot.org/annotation/VSP_038645|||http://purl.uniprot.org/annotation/VSP_038646
http://togogenome.org/gene/9606:ZNF414                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IQ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger protein 414                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242163|||http://purl.uniprot.org/annotation/VAR_026847|||http://purl.uniprot.org/annotation/VAR_026848|||http://purl.uniprot.org/annotation/VSP_045351
http://togogenome.org/gene/9606:MFSD6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWD5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Major facilitator superfamily domain-containing protein 6-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321944|||http://purl.uniprot.org/annotation/VAR_039389
http://togogenome.org/gene/9606:BRINP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0B6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BMP/retinoic acid-inducible neural-specific protein 2|||In isoform 2.|||MACPF|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045770|||http://purl.uniprot.org/annotation/VAR_049022|||http://purl.uniprot.org/annotation/VAR_049023|||http://purl.uniprot.org/annotation/VSP_017026
http://togogenome.org/gene/9606:DPPA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L190                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Developmental pluripotency-associated protein 4|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239268|||http://purl.uniprot.org/annotation/VAR_060372|||http://purl.uniprot.org/annotation/VAR_060373
http://togogenome.org/gene/9606:SNX31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9S9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PX|||Sorting nexin-31|||Strongly decreases interaction with CCDC22, CCDC93, VPS26C and VPS35L.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331603|||http://purl.uniprot.org/annotation/VAR_042900|||http://purl.uniprot.org/annotation/VAR_042901|||http://purl.uniprot.org/annotation/VAR_042902|||http://purl.uniprot.org/annotation/VSP_033261|||http://purl.uniprot.org/annotation/VSP_033262
http://togogenome.org/gene/9606:NDUFAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU61                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In MC1DN18.|||In isoform b.|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281154|||http://purl.uniprot.org/annotation/VAR_058491|||http://purl.uniprot.org/annotation/VAR_058492|||http://purl.uniprot.org/annotation/VAR_081425|||http://purl.uniprot.org/annotation/VSP_041086
http://togogenome.org/gene/9606:ARHGEF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR80|||http://purl.uniprot.org/uniprot/Q9NTG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ABR (APC-binding region) domain|||DH|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||PH|||Polar residues|||Rho guanine nucleotide exchange factor 4|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080914|||http://purl.uniprot.org/annotation/VAR_035970|||http://purl.uniprot.org/annotation/VAR_035971|||http://purl.uniprot.org/annotation/VAR_057187|||http://purl.uniprot.org/annotation/VSP_011617|||http://purl.uniprot.org/annotation/VSP_011618|||http://purl.uniprot.org/annotation/VSP_037119
http://togogenome.org/gene/9606:C11orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFU1|||http://purl.uniprot.org/uniprot/Q6NUJ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Uncharacterized protein C11orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320195
http://togogenome.org/gene/9606:ODAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF7|||http://purl.uniprot.org/uniprot/A0A5F9ZH22|||http://purl.uniprot.org/uniprot/B7Z7A1|||http://purl.uniprot.org/uniprot/B7Z7Y0|||http://purl.uniprot.org/uniprot/Q5T2S8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 10|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Disordered|||In CILD23; no effect on subcellular location, markedly reduced ciliary beat frequency and amplitude or complete immotility in most, but not all, respiratory cilia.|||In isoform 2.|||N6-methyllysine|||Outer dynein arm-docking complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243931|||http://purl.uniprot.org/annotation/VAR_033514|||http://purl.uniprot.org/annotation/VAR_050672|||http://purl.uniprot.org/annotation/VAR_050673|||http://purl.uniprot.org/annotation/VAR_070228|||http://purl.uniprot.org/annotation/VSP_056695|||http://purl.uniprot.org/annotation/VSP_056696
http://togogenome.org/gene/9606:PRKAR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2W3|||http://purl.uniprot.org/uniprot/A0A0S2Z472|||http://purl.uniprot.org/uniprot/A0A9L9PY56|||http://purl.uniprot.org/uniprot/A8KAH7|||http://purl.uniprot.org/uniprot/P13861                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Dimerization and phosphorylation|||Disordered|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Removed|||cAMP-dependent protein kinase type II-alpha regulatory subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205385|||http://purl.uniprot.org/annotation/VSP_056821
http://togogenome.org/gene/9606:STX1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61266                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In GEFSP9.|||In GEFSP9; loss of function mutation.|||In isoform 2.|||Phosphoserine|||Syntaxin-1B|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210192|||http://purl.uniprot.org/annotation/VAR_072675|||http://purl.uniprot.org/annotation/VAR_072676|||http://purl.uniprot.org/annotation/VSP_047681
http://togogenome.org/gene/9606:TMEM62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P6H9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254136
http://togogenome.org/gene/9606:MYADML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||MARVEL 1|||MARVEL 2|||Myeloid-associated differentiation marker-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332206
http://togogenome.org/gene/9606:WNT10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2K8FR47|||http://purl.uniprot.org/uniprot/Q9GZT5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Found in a patient with dental anomalies; unknown pathological significance.|||Found in patients with dental anomalies; unknown pathological significance.|||In OODD and STHAG4.|||In OODD and STHAG4; also found in patients with an unclassified form of ectodermal dysplasia.|||In OODD.|||In OODD; unknown pathological significance.|||In SSPS.|||In STHAG4 and OODD; unknown pathological significance.|||In STHAG4.|||In STHAG4; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Phosphothreonine|||Probable disease-associated variant found in patients with an unclassified form of ectodermal dysplasia.|||Protein Wnt|||Protein Wnt-10a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041460|||http://purl.uniprot.org/annotation/PRO_5014681491|||http://purl.uniprot.org/annotation/VAR_013239|||http://purl.uniprot.org/annotation/VAR_062510|||http://purl.uniprot.org/annotation/VAR_062511|||http://purl.uniprot.org/annotation/VAR_064837|||http://purl.uniprot.org/annotation/VAR_064838|||http://purl.uniprot.org/annotation/VAR_064839|||http://purl.uniprot.org/annotation/VAR_069171|||http://purl.uniprot.org/annotation/VAR_069172|||http://purl.uniprot.org/annotation/VAR_069173|||http://purl.uniprot.org/annotation/VAR_069174|||http://purl.uniprot.org/annotation/VAR_069175|||http://purl.uniprot.org/annotation/VAR_077446|||http://purl.uniprot.org/annotation/VAR_077447|||http://purl.uniprot.org/annotation/VAR_077448|||http://purl.uniprot.org/annotation/VAR_077449|||http://purl.uniprot.org/annotation/VAR_077450|||http://purl.uniprot.org/annotation/VAR_077451|||http://purl.uniprot.org/annotation/VAR_077452|||http://purl.uniprot.org/annotation/VAR_077453|||http://purl.uniprot.org/annotation/VAR_077454|||http://purl.uniprot.org/annotation/VAR_077455|||http://purl.uniprot.org/annotation/VAR_079418|||http://purl.uniprot.org/annotation/VAR_079419|||http://purl.uniprot.org/annotation/VAR_079420|||http://purl.uniprot.org/annotation/VAR_079421|||http://purl.uniprot.org/annotation/VAR_086718|||http://purl.uniprot.org/annotation/VAR_086719|||http://purl.uniprot.org/annotation/VAR_086720|||http://purl.uniprot.org/annotation/VAR_086721
http://togogenome.org/gene/9606:FUNDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWH2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||FUN14 domain-containing protein 2|||Helical|||Mitochondrial intermembrane|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314615
http://togogenome.org/gene/9606:U2AF1L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C3H1-type 1|||C3H1-type 2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylalanine|||RRM|||Removed|||Splicing factor U2AF 26 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309740|||http://purl.uniprot.org/annotation/VSP_029264|||http://purl.uniprot.org/annotation/VSP_029265
http://togogenome.org/gene/9606:AQP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29972                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aquaporin-1|||Cytoplasmic|||Extracellular|||Helical; Name=Helix 1|||Helical; Name=Helix 2|||Helical; Name=Helix 3|||Helical; Name=Helix 4|||Helical; Name=Helix 5|||Helical; Name=Helix 6|||Helical; Name=Helix B|||Helical; Name=Helix E|||Hg(2+)-sensitive residue|||In Co(A-B+) antigen.|||In Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Phosphoserine|||Phosphotyrosine|||Removed|||Substrate discrimination                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063920|||http://purl.uniprot.org/annotation/VAR_004400|||http://purl.uniprot.org/annotation/VAR_013279|||http://purl.uniprot.org/annotation/VAR_022318|||http://purl.uniprot.org/annotation/VSP_046109|||http://purl.uniprot.org/annotation/VSP_046110|||http://purl.uniprot.org/annotation/VSP_046679|||http://purl.uniprot.org/annotation/VSP_046680|||http://purl.uniprot.org/annotation/VSP_046681
http://togogenome.org/gene/9606:CDK5RAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRG9|||http://purl.uniprot.org/uniprot/B3KVI2|||http://purl.uniprot.org/uniprot/B9EG74|||http://purl.uniprot.org/uniprot/Q7Z3M0|||http://purl.uniprot.org/uniprot/Q96SN8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CDK5 regulatory subunit-associated protein 2|||Centrosomin N-terminal motif 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CDK5R1|||Interaction with MAPRE1|||Interaction with NCKAP5L|||Interaction with PCNT and AKAP9|||Loss of interaction with MAPRE1.|||No effect on centrosomal attachment, Golgi localization and loss of interaction to CALM1; when associated with A-1865.|||No effect on centrosomal attachment, Golgi localization and loss of interaction with CALM1; when associated with A-1869.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for centrosomal attachment, Golgi localization and CALM1 interaction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089835|||http://purl.uniprot.org/annotation/VAR_017443|||http://purl.uniprot.org/annotation/VAR_017444|||http://purl.uniprot.org/annotation/VAR_032426|||http://purl.uniprot.org/annotation/VAR_056831|||http://purl.uniprot.org/annotation/VAR_056832|||http://purl.uniprot.org/annotation/VAR_059616|||http://purl.uniprot.org/annotation/VSP_007563|||http://purl.uniprot.org/annotation/VSP_007564|||http://purl.uniprot.org/annotation/VSP_007565
http://togogenome.org/gene/9606:HBQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1K0GUV5|||http://purl.uniprot.org/uniprot/P09105                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit theta-1|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052846
http://togogenome.org/gene/9606:RFPL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLU0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||RING-type; degenerate|||Ret finger protein-like 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300811
http://togogenome.org/gene/9606:TLR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y7Z4|||http://purl.uniprot.org/uniprot/O60602                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In 10% of the population; abolishes flagellin signaling; associated with resistance to SLEB1.|||LRR 1|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKD/PRKD1|||Phosphotyrosine|||TIR|||Toll-like receptor 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034729|||http://purl.uniprot.org/annotation/PRO_5015331698|||http://purl.uniprot.org/annotation/VAR_018398|||http://purl.uniprot.org/annotation/VAR_018399|||http://purl.uniprot.org/annotation/VAR_018400|||http://purl.uniprot.org/annotation/VAR_032455|||http://purl.uniprot.org/annotation/VAR_032456|||http://purl.uniprot.org/annotation/VAR_047454|||http://purl.uniprot.org/annotation/VAR_061856|||http://purl.uniprot.org/annotation/VAR_061857|||http://purl.uniprot.org/annotation/VAR_061858|||http://purl.uniprot.org/annotation/VAR_070457
http://togogenome.org/gene/9606:UQCC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVI0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome c reductase complex assembly factor 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349243
http://togogenome.org/gene/9606:CRHR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3SXS2|||http://purl.uniprot.org/uniprot/B3TIK8|||http://purl.uniprot.org/uniprot/G3CIS4|||http://purl.uniprot.org/uniprot/K9J956|||http://purl.uniprot.org/uniprot/P34998                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Corticotropin-releasing factor receptor 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for antagonist binding|||Important for peptide agonist binding|||In isoform 5.|||In isoform CRF-R2, isoform CRF-R3 and isoform CRF-R4.|||In isoform CRF-R3.|||In isoform CRF-R4.|||Increases antagonist binding.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes antagonist binding.|||Phosphoserine; by PKA|||Slightly reduces antagonist binding.|||Strongly reduces antagonist binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012814|||http://purl.uniprot.org/annotation/PRO_5003443057|||http://purl.uniprot.org/annotation/PRO_5014101180|||http://purl.uniprot.org/annotation/PRO_5040053599|||http://purl.uniprot.org/annotation/VSP_001996|||http://purl.uniprot.org/annotation/VSP_001997|||http://purl.uniprot.org/annotation/VSP_001998|||http://purl.uniprot.org/annotation/VSP_045434
http://togogenome.org/gene/9606:NPFFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804CC06|||http://purl.uniprot.org/uniprot/A0PJM9|||http://purl.uniprot.org/uniprot/Q9Y5X5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neuropeptide FF receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069915|||http://purl.uniprot.org/annotation/VSP_001907|||http://purl.uniprot.org/annotation/VSP_001908|||http://purl.uniprot.org/annotation/VSP_001909|||http://purl.uniprot.org/annotation/VSP_001910|||http://purl.uniprot.org/annotation/VSP_001911
http://togogenome.org/gene/9606:ITIH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8B6|||http://purl.uniprot.org/uniprot/P19827                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to CUB domain of TNFAIP6.|||Aspartate 1-(chondroitin 4-sulfate)-ester|||Hyaluronan-binding|||In allele ITIH1*2 and allele ITIH1*3.|||In allele ITIH1*2.|||In isoform 2.|||In isoform 3.|||Inter-alpha-trypsin inhibitor heavy chain H1|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phagocytosis uptake signal|||Phosphoserine|||Phosphothreonine|||S-linked (Hex...) cysteine|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000138|||http://purl.uniprot.org/annotation/CAR_000139|||http://purl.uniprot.org/annotation/CAR_000213|||http://purl.uniprot.org/annotation/PRO_0000016506|||http://purl.uniprot.org/annotation/PRO_0000016507|||http://purl.uniprot.org/annotation/PRO_0000016508|||http://purl.uniprot.org/annotation/VAR_004019|||http://purl.uniprot.org/annotation/VAR_004020|||http://purl.uniprot.org/annotation/VAR_011873|||http://purl.uniprot.org/annotation/VAR_011874|||http://purl.uniprot.org/annotation/VAR_011875|||http://purl.uniprot.org/annotation/VSP_045419|||http://purl.uniprot.org/annotation/VSP_045420
http://togogenome.org/gene/9606:SLC46A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3Q1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Lysosomal proton-coupled steroid conjugate and bile acid symporter SLC46A3|||N-linked (GlcNAc...) asparagine|||Tyrosine-based lysosomal-sorting motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307253|||http://purl.uniprot.org/annotation/VSP_028648|||http://purl.uniprot.org/annotation/VSP_028649
http://togogenome.org/gene/9606:MRTO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Phosphoserine|||mRNA turnover protein 4 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154816
http://togogenome.org/gene/9606:PTGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14914                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Markedly decreases the catalytic efficiency toward 15-oxoprostaglandin E2 and (3E)-3-nonen-2-one.|||Markedly decreases the catalytic efficiency toward 15-oxoprostaglandin E2.|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Prostaglandin reductase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218065|||http://purl.uniprot.org/annotation/VAR_023111|||http://purl.uniprot.org/annotation/VSP_044652
http://togogenome.org/gene/9606:APOL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95236                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Apolipoprotein L3|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137602|||http://purl.uniprot.org/annotation/VAR_047488|||http://purl.uniprot.org/annotation/VAR_053007|||http://purl.uniprot.org/annotation/VSP_000293|||http://purl.uniprot.org/annotation/VSP_000294
http://togogenome.org/gene/9606:ZNF674                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HHU7|||http://purl.uniprot.org/uniprot/Q2M3X9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Rare variant found in patients with X-linked intellectual disability; unknown pathological significance.|||Zinc finger protein 674                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233995|||http://purl.uniprot.org/annotation/VAR_026152|||http://purl.uniprot.org/annotation/VAR_026153|||http://purl.uniprot.org/annotation/VAR_046997|||http://purl.uniprot.org/annotation/VSP_044562
http://togogenome.org/gene/9606:EREG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14944                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||Epiregulin|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Proepiregulin|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007556|||http://purl.uniprot.org/annotation/PRO_0000007557|||http://purl.uniprot.org/annotation/PRO_0000007558|||http://purl.uniprot.org/annotation/PRO_0000302800|||http://purl.uniprot.org/annotation/VAR_033827|||http://purl.uniprot.org/annotation/VAR_035833
http://togogenome.org/gene/9606:ZNF782                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMW2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 782                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263075|||http://purl.uniprot.org/annotation/VAR_029578|||http://purl.uniprot.org/annotation/VAR_029579|||http://purl.uniprot.org/annotation/VAR_052901|||http://purl.uniprot.org/annotation/VAR_052902
http://togogenome.org/gene/9606:LAX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||In isoform 3.|||Lymphocyte transmembrane adapter 1|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083329|||http://purl.uniprot.org/annotation/VSP_016641|||http://purl.uniprot.org/annotation/VSP_046972
http://togogenome.org/gene/9606:SULF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWU5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Basic and acidic residues|||Catalytic domain; necessary for arylsulfatase activity|||Cleavage; by furin|||Disordered|||Extracellular sulfatase Sulf-2|||Extracellular sulfatase Sulf-2 secreted form|||Hydrophilic domain; necessary for endoglucosamine-6-sulfatase activity|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of arylsulfatase activity.|||N-linked (GlcNAc...) asparagine|||No effect on N-acetylglucosamine-6-sulfatase activity. Significant loss of N-acetylglucosamine-6-sulfatase activity; when associated with 180-A--A-182.|||No effect on N-acetylglucosamine-6-sulfatase activity. Significant loss of N-acetylglucosamine-6-sulfatase activity; when associated with 402-A--A-404.|||Nucleophile|||O-linked (Xyl...) (chondroitin sulfate) serine|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033440|||http://purl.uniprot.org/annotation/PRO_0000457759|||http://purl.uniprot.org/annotation/VAR_036494|||http://purl.uniprot.org/annotation/VAR_036495|||http://purl.uniprot.org/annotation/VAR_052518|||http://purl.uniprot.org/annotation/VAR_061885|||http://purl.uniprot.org/annotation/VSP_013362
http://togogenome.org/gene/9606:RPL36A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83881                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein eL42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149117
http://togogenome.org/gene/9606:FOXK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P85037                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FHA|||Fork-head|||Forkhead box protein K1|||In isoform 2.|||Interaction with SIN3A and SIN3B|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced DNA-binding and ability to repress transcription without affecting interaction with SRF. No effect on interaction with DVL2.|||Reduced interaction with BAP1.|||Removed|||Required for interaction with FOXO4 and MEF2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261667|||http://purl.uniprot.org/annotation/VSP_052239|||http://purl.uniprot.org/annotation/VSP_052240
http://togogenome.org/gene/9606:TM2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLL2|||http://purl.uniprot.org/uniprot/E7EPS7|||http://purl.uniprot.org/uniprot/H0YNS4|||http://purl.uniprot.org/uniprot/Q9BRN9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TM2 domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298989|||http://purl.uniprot.org/annotation/PRO_5002800872|||http://purl.uniprot.org/annotation/PRO_5003219444|||http://purl.uniprot.org/annotation/PRO_5003546767|||http://purl.uniprot.org/annotation/VSP_027496
http://togogenome.org/gene/9606:RPL19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTE4|||http://purl.uniprot.org/uniprot/P84098                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Large ribosomal subunit protein eL19|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131169
http://togogenome.org/gene/9606:BVES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE79                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Blood vessel epicardial substance|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In LGMDR25; reduces membrane localization of BVES and POPDC2; decreases by 50% affinity for cAMP; disrupts enhancement of KCKN2 surface expression; increases KCKN2 outward currents; no effect on total protein levels.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for interaction with CAV3|||Required for interaction with KCNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046791|||http://purl.uniprot.org/annotation/VAR_017155|||http://purl.uniprot.org/annotation/VAR_053600|||http://purl.uniprot.org/annotation/VAR_075625
http://togogenome.org/gene/9606:KRTAP20-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI63                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Keratin-associated protein 20-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223910|||http://purl.uniprot.org/annotation/VAR_036562
http://togogenome.org/gene/9606:GABRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99928                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with MRT52; unknown pathological significance.|||Gamma-aminobutyric acid receptor subunit gamma-3|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000481|||http://purl.uniprot.org/annotation/VAR_033957|||http://purl.uniprot.org/annotation/VSP_047543|||http://purl.uniprot.org/annotation/VSP_047544
http://togogenome.org/gene/9606:PPIAL4F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B759|||http://purl.uniprot.org/uniprot/P0DN26                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4E|||Peptidyl-prolyl cis-trans isomerase A-like 4F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433925|||http://purl.uniprot.org/annotation/PRO_0000433926
http://togogenome.org/gene/9606:ADAMTS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75173                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 4|||Cysteine switch|||Disintegrin|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Spacer|||TSP type-1|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029164|||http://purl.uniprot.org/annotation/PRO_0000029165|||http://purl.uniprot.org/annotation/VAR_022450|||http://purl.uniprot.org/annotation/VAR_030636|||http://purl.uniprot.org/annotation/VAR_030637|||http://purl.uniprot.org/annotation/VAR_030638|||http://purl.uniprot.org/annotation/VAR_030639|||http://purl.uniprot.org/annotation/VAR_030640|||http://purl.uniprot.org/annotation/VAR_030641|||http://purl.uniprot.org/annotation/VAR_057073|||http://purl.uniprot.org/annotation/VSP_057293
http://togogenome.org/gene/9606:RPLP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05387                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein P2|||N-acetylmethionine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157640
http://togogenome.org/gene/9606:OR51M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNI9|||http://purl.uniprot.org/uniprot/Q9H341                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150760|||http://purl.uniprot.org/annotation/VAR_070593|||http://purl.uniprot.org/annotation/VAR_070594|||http://purl.uniprot.org/annotation/VAR_070595|||http://purl.uniprot.org/annotation/VAR_070596|||http://purl.uniprot.org/annotation/VAR_070597|||http://purl.uniprot.org/annotation/VAR_070598
http://togogenome.org/gene/9606:OTUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUV5|||http://purl.uniprot.org/uniprot/Q96FW1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to deubiquitinate DEPTOR. Does not affect ability to deubiquitinate RPTOR; when associated with A-91 and A-265.|||Abolished ability to deubiquitinate RPTOR.|||Abolishes ability to inhibit RNF168; when associated with A-88 and S-91. Does not affect ability to deubiquitinate RPTOR; when associated with A-88 and A-91.|||Abolishes hydrolase activity in vitro.|||Abolishes hydrolase activity in vitro. Abolishes ability to inhibit RNF168; when associated with S-91 and A-265.|||Abolishes hydrolase activity in vitro. Does not affect ability to inhibit RNF168. Does not affect ability to deubiquitinate DEPTOR. Abolishes ability to inhibit RNF168; when associated with E-88 and A-265.|||Abolishes only ubiquitin-vinylsulfone adduct formation.|||Does not affect ability to deubiquitinate DEPTOR.|||Does not affect ability to inhibit UBE2N/UBC13.|||Does not affect activity in DNA repair and ability to inhibit UBE2N/UBC13.|||Fails to inhibit ubiquitin conjugation by UBE2N/UBC13.|||Free ubiquitin binding|||Impairs inhibition of UBE2N/UBC13.|||In isoform 2.|||Interacts with free ubiquitin|||N-acetylalanine|||No effect on RNF128.|||Nucleophile|||OTU|||Phosphoserine|||Phosphotyrosine; by SRC|||Prevents RNF128 autoubiquitination, and stabilizes RNF128 in vivo. Abolishes both ubiquitin-binding and adduct formation with ubiquitin-vinylsulfone. Does not affect ability to deubiquitinate RPTOR; when associated with A-88 and A-265.|||Removed|||Required for proximal ubiquitin-binding|||Slightly improves ability to cleave 'K63'-linked ubiquitin.|||Ubiquitin thioesterase OTUB1|||Ubiquitin-conjugating enzyme E2 binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221008|||http://purl.uniprot.org/annotation/VSP_009464
http://togogenome.org/gene/9606:CLUH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75153                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Clu|||Clustered mitochondria protein homolog|||Disordered|||Phosphoserine|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123553|||http://purl.uniprot.org/annotation/VAR_034008
http://togogenome.org/gene/9606:AHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In XIGIS.|||In XIGIS; does not affect nuclear localization.|||In XIGIS; impaired nuclear localization.|||In XIGIS; unknown pathological significance.|||In XIGIS; unknown pathological significance; does not affect nuclear localization.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription factor Gibbin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313824|||http://purl.uniprot.org/annotation/VAR_037765|||http://purl.uniprot.org/annotation/VAR_086657|||http://purl.uniprot.org/annotation/VAR_086658|||http://purl.uniprot.org/annotation/VAR_086659|||http://purl.uniprot.org/annotation/VAR_086660|||http://purl.uniprot.org/annotation/VAR_086661|||http://purl.uniprot.org/annotation/VAR_086662|||http://purl.uniprot.org/annotation/VAR_086663|||http://purl.uniprot.org/annotation/VAR_086664|||http://purl.uniprot.org/annotation/VAR_086665|||http://purl.uniprot.org/annotation/VAR_086666|||http://purl.uniprot.org/annotation/VAR_086667|||http://purl.uniprot.org/annotation/VAR_086668|||http://purl.uniprot.org/annotation/VAR_086669|||http://purl.uniprot.org/annotation/VAR_086670|||http://purl.uniprot.org/annotation/VAR_086671|||http://purl.uniprot.org/annotation/VAR_086672|||http://purl.uniprot.org/annotation/VAR_086673|||http://purl.uniprot.org/annotation/VAR_086674|||http://purl.uniprot.org/annotation/VAR_086675|||http://purl.uniprot.org/annotation/VAR_086676|||http://purl.uniprot.org/annotation/VAR_086677|||http://purl.uniprot.org/annotation/VAR_086678|||http://purl.uniprot.org/annotation/VAR_086679|||http://purl.uniprot.org/annotation/VAR_086680|||http://purl.uniprot.org/annotation/VAR_086681|||http://purl.uniprot.org/annotation/VAR_086682|||http://purl.uniprot.org/annotation/VAR_086683
http://togogenome.org/gene/9606:CYTH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43739                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes autoinhibition and increases guanine-nucleotide exchange activity.|||C-terminal autoinhibitory region|||Cytohesin-3|||In isoform 2.|||PH|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120200|||http://purl.uniprot.org/annotation/VSP_006039
http://togogenome.org/gene/9606:USP53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J9FKG6|||http://purl.uniprot.org/uniprot/Q70EK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In PFIC7.|||In PFIC7; unknown pathological significance.|||Inactive ubiquitin carboxyl-terminal hydrolase 53|||Polar residues|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080681|||http://purl.uniprot.org/annotation/VAR_051541|||http://purl.uniprot.org/annotation/VAR_086693|||http://purl.uniprot.org/annotation/VAR_086694|||http://purl.uniprot.org/annotation/VAR_086695|||http://purl.uniprot.org/annotation/VAR_086696|||http://purl.uniprot.org/annotation/VAR_086697|||http://purl.uniprot.org/annotation/VAR_086698|||http://purl.uniprot.org/annotation/VAR_086699|||http://purl.uniprot.org/annotation/VAR_086700
http://togogenome.org/gene/9606:ATF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18848                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  4-hydroxyproline|||Abolished phosphorylation by CK2 leading to increased stability.|||Abolished phosphorylation by RPS6KA3/RSK2.|||Abolished phosphorylation on the betaTrCP degron motif, interaction with BTRC and subsequent ubiquitination.|||Basic motif|||BetaTrCP degron motif|||Cyclic AMP-dependent transcription factor ATF-4|||Decreased acetylation without affecting ubiquitination by SCF(BTRC).|||Disordered|||Does not affect phosphorylation by CK2.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Increased stability in low oxygen conditions; when associated with A-156, A-162, A-164 and A-167.|||Increased stability in low oxygen conditions; when associated with A-156, A-162, A-164 and A-174.|||Increased stability in low oxygen conditions; when associated with A-156, A-162, A-167 and A-174.|||Increased stability in low oxygen conditions; when associated with A-156, A-164, A-167 and A-174.|||Increased stability in low oxygen conditions; when associated with A-162, A-164, A-167 and A-174.|||Interaction with GABBR1|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by RPS6KA3|||Phosphothreonine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076584|||http://purl.uniprot.org/annotation/VAR_014768|||http://purl.uniprot.org/annotation/VAR_028253|||http://purl.uniprot.org/annotation/VAR_029259
http://togogenome.org/gene/9606:SLC1A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15758|||http://purl.uniprot.org/uniprot/Q59ES3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neutral amino acid transporter B(0)|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202082|||http://purl.uniprot.org/annotation/VAR_013517|||http://purl.uniprot.org/annotation/VAR_020439|||http://purl.uniprot.org/annotation/VSP_046354|||http://purl.uniprot.org/annotation/VSP_046851
http://togogenome.org/gene/9606:PIP5KL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9C9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285758|||http://purl.uniprot.org/annotation/VSP_024904
http://togogenome.org/gene/9606:ZNF805                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5CZA5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 805                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304624|||http://purl.uniprot.org/annotation/VAR_057454|||http://purl.uniprot.org/annotation/VSP_040823
http://togogenome.org/gene/9606:DEF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN54                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Differentially expressed in FDCP 8 homolog|||Disordered|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||N-acetylmethionine|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321913|||http://purl.uniprot.org/annotation/VAR_061485|||http://purl.uniprot.org/annotation/VSP_031821|||http://purl.uniprot.org/annotation/VSP_031822|||http://purl.uniprot.org/annotation/VSP_031823|||http://purl.uniprot.org/annotation/VSP_031824|||http://purl.uniprot.org/annotation/VSP_037523|||http://purl.uniprot.org/annotation/VSP_047179
http://togogenome.org/gene/9606:WBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75554                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with SNRNP200|||Matrin-type|||Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11.|||Phosphoserine|||Polar residues|||WW 1|||WW 2|||WW domain-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076065|||http://purl.uniprot.org/annotation/VAR_036352|||http://purl.uniprot.org/annotation/VSP_056413
http://togogenome.org/gene/9606:WDCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6R7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with HCK|||Loss of interaction with HCK; when associated with P-543.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD repeat and coiled-coil-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299501|||http://purl.uniprot.org/annotation/VAR_034834|||http://purl.uniprot.org/annotation/VAR_035876|||http://purl.uniprot.org/annotation/VSP_027712|||http://purl.uniprot.org/annotation/VSP_027713|||http://purl.uniprot.org/annotation/VSP_027714|||http://purl.uniprot.org/annotation/VSP_027715
http://togogenome.org/gene/9606:DLGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95886                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disks large-associated protein 3|||Disordered|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174294|||http://purl.uniprot.org/annotation/VAR_079371
http://togogenome.org/gene/9606:EIF3H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15372|||http://purl.uniprot.org/uniprot/Q6IB98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 3 subunit H|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MPN|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213961
http://togogenome.org/gene/9606:CACNG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UF02                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Voltage-dependent calcium channel gamma-5 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164681
http://togogenome.org/gene/9606:MAJIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KP22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 1.|||In isoform 2.|||Membrane-anchored junction protein|||Nuclear|||Perinuclear space|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325832|||http://purl.uniprot.org/annotation/VSP_058060|||http://purl.uniprot.org/annotation/VSP_058061|||http://purl.uniprot.org/annotation/VSP_058062|||http://purl.uniprot.org/annotation/VSP_058063
http://togogenome.org/gene/9606:ARHGEF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3C7|||http://purl.uniprot.org/uniprot/Q15052|||http://purl.uniprot.org/uniprot/Q8N4Q3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||DH|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho guanine nucleotide exchange factor 6|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080917|||http://purl.uniprot.org/annotation/VAR_051981|||http://purl.uniprot.org/annotation/VSP_015782
http://togogenome.org/gene/9606:SPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by prohormone convertase 2|||Disordered|||Glutamine amide|||Spexin|||Spexin-1|||Spexin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042159|||http://purl.uniprot.org/annotation/PRO_0000363216|||http://purl.uniprot.org/annotation/PRO_0000363217|||http://purl.uniprot.org/annotation/PRO_0000430213|||http://purl.uniprot.org/annotation/PRO_0000430214|||http://purl.uniprot.org/annotation/PRO_0000430215
http://togogenome.org/gene/9606:SMARCAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DESH box|||Disordered|||HARP 1|||HARP 2|||Helicase ATP-binding|||Helicase C-terminal|||In SIOD.|||In SIOD; abolishes annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage.|||In SIOD; impairs without abolishing annealing helicase activity; no effect on specific binding to fork DNA; no effect on recruitment to sites of DNA damage.|||In a breast cancer sample; somatic mutation.|||Loss of interaction with RPA2 and impaired recruitment by the RPA complex to sites of DNA damage.|||Mediates interaction with RPA2|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074348|||http://purl.uniprot.org/annotation/VAR_021363|||http://purl.uniprot.org/annotation/VAR_021364|||http://purl.uniprot.org/annotation/VAR_021366|||http://purl.uniprot.org/annotation/VAR_021367|||http://purl.uniprot.org/annotation/VAR_021368|||http://purl.uniprot.org/annotation/VAR_021369|||http://purl.uniprot.org/annotation/VAR_021370|||http://purl.uniprot.org/annotation/VAR_021371|||http://purl.uniprot.org/annotation/VAR_021372|||http://purl.uniprot.org/annotation/VAR_021373|||http://purl.uniprot.org/annotation/VAR_021374|||http://purl.uniprot.org/annotation/VAR_021375|||http://purl.uniprot.org/annotation/VAR_021376|||http://purl.uniprot.org/annotation/VAR_021377|||http://purl.uniprot.org/annotation/VAR_021378|||http://purl.uniprot.org/annotation/VAR_021379|||http://purl.uniprot.org/annotation/VAR_021380|||http://purl.uniprot.org/annotation/VAR_021381|||http://purl.uniprot.org/annotation/VAR_021382|||http://purl.uniprot.org/annotation/VAR_036026|||http://purl.uniprot.org/annotation/VAR_038370
http://togogenome.org/gene/9606:OC90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02509                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Otoconin-90|||Phospholipase A2-like 1|||Phospholipase A2-like 2|||Phospholipase A2-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022993|||http://purl.uniprot.org/annotation/VSP_059516
http://togogenome.org/gene/9606:CFAP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6A4                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296398
http://togogenome.org/gene/9606:KIF20B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q89                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PIN1|||Kinesin motor|||Kinesin-like protein KIF20B|||Necessary and sufficient for interaction with SHTN1|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274053|||http://purl.uniprot.org/annotation/VAR_030181|||http://purl.uniprot.org/annotation/VAR_030182|||http://purl.uniprot.org/annotation/VAR_030183|||http://purl.uniprot.org/annotation/VAR_030184|||http://purl.uniprot.org/annotation/VAR_030185|||http://purl.uniprot.org/annotation/VAR_030186|||http://purl.uniprot.org/annotation/VAR_030187|||http://purl.uniprot.org/annotation/VAR_030188|||http://purl.uniprot.org/annotation/VAR_030189|||http://purl.uniprot.org/annotation/VAR_075704|||http://purl.uniprot.org/annotation/VAR_075705|||http://purl.uniprot.org/annotation/VSP_022618|||http://purl.uniprot.org/annotation/VSP_022619|||http://purl.uniprot.org/annotation/VSP_022620|||http://purl.uniprot.org/annotation/VSP_022621|||http://purl.uniprot.org/annotation/VSP_022622
http://togogenome.org/gene/9606:CAMK2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TN60|||http://purl.uniprot.org/uniprot/A0A8V8TN65|||http://purl.uniprot.org/uniprot/A0A8V8TN88|||http://purl.uniprot.org/uniprot/A0A8V8TNA1|||http://purl.uniprot.org/uniprot/A0A8V8TNA7|||http://purl.uniprot.org/uniprot/A0A8V8TPJ8|||http://purl.uniprot.org/uniprot/A0A8V8TPY4|||http://purl.uniprot.org/uniprot/A0A994J516|||http://purl.uniprot.org/uniprot/A0A994J5B0|||http://purl.uniprot.org/uniprot/D6R938|||http://purl.uniprot.org/uniprot/E9PBG7|||http://purl.uniprot.org/uniprot/E9PF82|||http://purl.uniprot.org/uniprot/Q13557                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type II subunit delta|||Calmodulin-binding|||Disordered|||In isoform Delta 11.|||In isoform Delta 12.|||In isoform Delta 3 and isoform Delta 7.|||In isoform Delta 4 and isoform Delta 8.|||In isoform Delta 6, isoform Delta 7, isoform Delta 8, isoform Delta 10 and isoform Delta 12.|||In isoform Delta 9 and isoform Delta 10.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086099|||http://purl.uniprot.org/annotation/VAR_028196|||http://purl.uniprot.org/annotation/VAR_040602|||http://purl.uniprot.org/annotation/VAR_040603|||http://purl.uniprot.org/annotation/VSP_023095|||http://purl.uniprot.org/annotation/VSP_023096|||http://purl.uniprot.org/annotation/VSP_023097|||http://purl.uniprot.org/annotation/VSP_023098|||http://purl.uniprot.org/annotation/VSP_023099|||http://purl.uniprot.org/annotation/VSP_041820
http://togogenome.org/gene/9606:NLRP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCA1|||http://purl.uniprot.org/uniprot/Q96MN2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||NACHT|||NACHT, LRR and PYD domains-containing protein 4|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080889|||http://purl.uniprot.org/annotation/VAR_020007|||http://purl.uniprot.org/annotation/VAR_024179|||http://purl.uniprot.org/annotation/VAR_024827|||http://purl.uniprot.org/annotation/VAR_024828|||http://purl.uniprot.org/annotation/VAR_024829|||http://purl.uniprot.org/annotation/VAR_032764|||http://purl.uniprot.org/annotation/VSP_003916|||http://purl.uniprot.org/annotation/VSP_044007
http://togogenome.org/gene/9606:SYT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQA0|||http://purl.uniprot.org/uniprot/P21579                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||In BAGOS.|||N-linked (GlcNAc...) asparagine|||Phospholipid binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine|||Synaptotagmin-1|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183936|||http://purl.uniprot.org/annotation/VAR_072911|||http://purl.uniprot.org/annotation/VAR_081536|||http://purl.uniprot.org/annotation/VAR_081537|||http://purl.uniprot.org/annotation/VAR_081538|||http://purl.uniprot.org/annotation/VAR_081539
http://togogenome.org/gene/9606:TRERF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05GC8|||http://purl.uniprot.org/uniprot/Q96PN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||ELM2|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||Interaction with CREBBP|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SANT|||Transcriptional-regulating factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197134|||http://purl.uniprot.org/annotation/VAR_050197|||http://purl.uniprot.org/annotation/VAR_050198|||http://purl.uniprot.org/annotation/VAR_050199|||http://purl.uniprot.org/annotation/VAR_050200|||http://purl.uniprot.org/annotation/VAR_061362|||http://purl.uniprot.org/annotation/VSP_015644|||http://purl.uniprot.org/annotation/VSP_015645|||http://purl.uniprot.org/annotation/VSP_015646
http://togogenome.org/gene/9606:C2CD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE2|||http://purl.uniprot.org/uniprot/Q53TS8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Cation channel sperm-associated targeting subunit tau|||Disordered|||In SPGF68; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076174|||http://purl.uniprot.org/annotation/VAR_024769|||http://purl.uniprot.org/annotation/VAR_035787|||http://purl.uniprot.org/annotation/VAR_086977|||http://purl.uniprot.org/annotation/VSP_061598|||http://purl.uniprot.org/annotation/VSP_061599|||http://purl.uniprot.org/annotation/VSP_061600|||http://purl.uniprot.org/annotation/VSP_061601|||http://purl.uniprot.org/annotation/VSP_061602
http://togogenome.org/gene/9606:HTR5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2N2|||http://purl.uniprot.org/uniprot/P47898                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 5A|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068969|||http://purl.uniprot.org/annotation/VAR_035753
http://togogenome.org/gene/9606:MRPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09001                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In COXPD9.|||Large ribosomal subunit protein uL3m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077253|||http://purl.uniprot.org/annotation/VAR_020108|||http://purl.uniprot.org/annotation/VAR_066676
http://togogenome.org/gene/9606:TBCCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVR7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C-CAP/cofactor C-like|||In isoform 2.|||TBCC domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304944|||http://purl.uniprot.org/annotation/VAR_035123|||http://purl.uniprot.org/annotation/VSP_054000|||http://purl.uniprot.org/annotation/VSP_054001
http://togogenome.org/gene/9606:GCGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47871                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes expression at cell surface and glucagon binding.|||Abolishes glucagon binding.|||Abolishes glucagon binding. Strongly reduces expression at the cell surface.|||Causes the formation of an artifactual disulfide bond that abolishes glucagon binding; when associated with C-113.|||Causes the formation of an artifactual disulfide bond that abolishes glucagon binding; when associated with C-209.|||Causes the formation of an artifactual disulfide bond that interferes with glucagon binding; when associated with C-130.|||Causes the formation of an artifactual disulfide bond that interferes with glucagon binding; when associated with C-210.|||Cytoplasmic|||Disordered|||Extracellular|||Glucagon receptor|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for allosteric inhibitor binding|||In MVAH.|||In MVAH; abolishes glucagon binding.|||In MVAH; loss of glucagon-elicited cAMP production; no effect on localization to the cell membrane.|||In MVAH; when associated in cis with H-225; decreased glucagon binding and decreased glucagon-elicited cAMP production; no effect on localization to the cell membrane.|||In MVAH; when associated in cis with M-368; decreased glucagon binding and decreased glucagon-elicited cAMP production; decreased localization to the cell membrane.|||Loss of synthetic antagonist binding.|||N-linked (GlcNAc...) asparagine|||No effect on affinity for glucagon.|||No effect on glucagon-elicited cAMP production.|||Phosphoserine|||Strongly decreases affinity for synthetic antagonist.|||Strongly reduced affinity for glucagon.|||Strongly reduced affinity for glucagon. Increased constitutive signaling via G-proteins.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012832|||http://purl.uniprot.org/annotation/VAR_003581|||http://purl.uniprot.org/annotation/VAR_014837|||http://purl.uniprot.org/annotation/VAR_033966|||http://purl.uniprot.org/annotation/VAR_069815|||http://purl.uniprot.org/annotation/VAR_085613|||http://purl.uniprot.org/annotation/VAR_085614|||http://purl.uniprot.org/annotation/VAR_085615|||http://purl.uniprot.org/annotation/VAR_085616|||http://purl.uniprot.org/annotation/VAR_085617|||http://purl.uniprot.org/annotation/VAR_085618|||http://purl.uniprot.org/annotation/VAR_085619|||http://purl.uniprot.org/annotation/VAR_085620|||http://purl.uniprot.org/annotation/VAR_085621|||http://purl.uniprot.org/annotation/VAR_085622|||http://purl.uniprot.org/annotation/VAR_085623|||http://purl.uniprot.org/annotation/VAR_085624|||http://purl.uniprot.org/annotation/VAR_085625
http://togogenome.org/gene/9606:CHRDL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WN34                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chordin-like protein 2|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||VWFC 1|||VWFC 2|||VWFC 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005371|||http://purl.uniprot.org/annotation/VAR_055651|||http://purl.uniprot.org/annotation/VSP_013512|||http://purl.uniprot.org/annotation/VSP_013513|||http://purl.uniprot.org/annotation/VSP_013514|||http://purl.uniprot.org/annotation/VSP_013515|||http://purl.uniprot.org/annotation/VSP_013516|||http://purl.uniprot.org/annotation/VSP_013517|||http://purl.uniprot.org/annotation/VSP_013518|||http://purl.uniprot.org/annotation/VSP_013519
http://togogenome.org/gene/9606:ADAM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTL6|||http://purl.uniprot.org/uniprot/Q9H2U9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Detected in a melanoma cell line.|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 7|||Extracellular|||Helical|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to collagen IV and laminin-1; increases cell migration capabilities compared to wild-type.|||In a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to collagen IV.|||In a cutaneous metastatic melanoma sample; somatic mutation; does not affect cell growth but conferes reduced cell adhesion to laminin-1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029052|||http://purl.uniprot.org/annotation/PRO_0000029053|||http://purl.uniprot.org/annotation/PRO_5036073205|||http://purl.uniprot.org/annotation/VAR_046728|||http://purl.uniprot.org/annotation/VAR_046729|||http://purl.uniprot.org/annotation/VAR_046730|||http://purl.uniprot.org/annotation/VAR_046731|||http://purl.uniprot.org/annotation/VAR_046732|||http://purl.uniprot.org/annotation/VAR_046733|||http://purl.uniprot.org/annotation/VAR_046734|||http://purl.uniprot.org/annotation/VAR_066296|||http://purl.uniprot.org/annotation/VAR_066297|||http://purl.uniprot.org/annotation/VAR_066298|||http://purl.uniprot.org/annotation/VAR_066299|||http://purl.uniprot.org/annotation/VAR_066300|||http://purl.uniprot.org/annotation/VAR_066301|||http://purl.uniprot.org/annotation/VAR_066302|||http://purl.uniprot.org/annotation/VAR_066303|||http://purl.uniprot.org/annotation/VAR_066304|||http://purl.uniprot.org/annotation/VAR_066305|||http://purl.uniprot.org/annotation/VAR_066306|||http://purl.uniprot.org/annotation/VAR_066307|||http://purl.uniprot.org/annotation/VAR_066308|||http://purl.uniprot.org/annotation/VSP_056602|||http://purl.uniprot.org/annotation/VSP_056603
http://togogenome.org/gene/9606:HROB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Homologous recombination OB-fold protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288092|||http://purl.uniprot.org/annotation/VAR_032393|||http://purl.uniprot.org/annotation/VSP_025651|||http://purl.uniprot.org/annotation/VSP_025652|||http://purl.uniprot.org/annotation/VSP_025653|||http://purl.uniprot.org/annotation/VSP_025654|||http://purl.uniprot.org/annotation/VSP_025655|||http://purl.uniprot.org/annotation/VSP_047077
http://togogenome.org/gene/9606:KDM5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR42|||http://purl.uniprot.org/uniprot/Q9BY66                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARID|||Abolishes enzymatic activity; when associated with A-534.|||Abolishes enzymatic activity; when associated with A-536.|||Basic and acidic residues|||C5HC2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||JmjC|||JmjN|||Lysine-specific demethylase 5D|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200588|||http://purl.uniprot.org/annotation/VAR_032991|||http://purl.uniprot.org/annotation/VSP_000317|||http://purl.uniprot.org/annotation/VSP_043320
http://togogenome.org/gene/9606:FCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75636|||http://purl.uniprot.org/uniprot/Q6UXM4|||http://purl.uniprot.org/uniprot/Q6UY50                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Collagen-like|||Disordered|||Fibrinogen C-terminal|||Ficolin-3|||Hydroxyproline|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009142|||http://purl.uniprot.org/annotation/PRO_5014310683|||http://purl.uniprot.org/annotation/VSP_001541
http://togogenome.org/gene/9606:MAGEB17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen B17|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332218
http://togogenome.org/gene/9606:GLRX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK1|||http://purl.uniprot.org/uniprot/O76003                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutaredoxin 1|||Glutaredoxin 2|||Glutaredoxin-3|||Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with S-159.|||Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with S-261.|||Loss of 2Fe-2S-binding; when associated with S-159. Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with 299-D-A-300.|||Loss of 2Fe-2S-binding; when associated with S-261. Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with 197-D-A-198.|||N-acetylalanine|||Phosphoserine|||Removed|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120019|||http://purl.uniprot.org/annotation/VAR_016875|||http://purl.uniprot.org/annotation/VAR_016876
http://togogenome.org/gene/9606:RABGEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3R3|||http://purl.uniprot.org/uniprot/B3KMF1|||http://purl.uniprot.org/uniprot/Q9UJ41                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with ubiquitinated proteins|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Rab5 GDP/GTP exchange factor|||Reduces affinity for ubiquitin 3-fold.|||Strongly reduced activity.|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191315|||http://purl.uniprot.org/annotation/VSP_060130|||http://purl.uniprot.org/annotation/VSP_060131
http://togogenome.org/gene/9606:RIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5UIP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with ERCC6|||Interaction with condensed chromosomes in telophase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Telomere-associated protein RIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097333|||http://purl.uniprot.org/annotation/VAR_022788|||http://purl.uniprot.org/annotation/VAR_022789|||http://purl.uniprot.org/annotation/VAR_022790|||http://purl.uniprot.org/annotation/VAR_022791|||http://purl.uniprot.org/annotation/VAR_022792|||http://purl.uniprot.org/annotation/VAR_022793|||http://purl.uniprot.org/annotation/VAR_022794|||http://purl.uniprot.org/annotation/VAR_035983|||http://purl.uniprot.org/annotation/VAR_035984|||http://purl.uniprot.org/annotation/VSP_014431
http://togogenome.org/gene/9606:ASB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXK3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 13|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066949|||http://purl.uniprot.org/annotation/VSP_000272|||http://purl.uniprot.org/annotation/VSP_000273
http://togogenome.org/gene/9606:LHFPL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7J7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||LHFPL tetraspan subfamily member 4 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285961
http://togogenome.org/gene/9606:C1orf210                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||N-linked (GlcNAc...) asparagine|||Type III endosome membrane protein TEMP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271010|||http://purl.uniprot.org/annotation/VAR_033655
http://togogenome.org/gene/9606:DGKQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC1|||http://purl.uniprot.org/uniprot/P52824|||http://purl.uniprot.org/uniprot/Q59FF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes translocation to the plasma membrane.|||Basic and acidic residues|||DAGKc|||Decreased diacylglycerol kinase activity.|||Diacylglycerol kinase theta|||Disordered|||LXXLL motif 1|||LXXLL motif 2|||Loss of diacylglycerol kinase activity.|||Loss of diacylglycerol kinase activity. Loss of function is synaptic endocytosis.|||Loss of diacylglycerol kinase activity. No effect on translocation to the plasma membrane.|||No effect on diacylglycerol kinase activity.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phorbol-ester/DAG-type 3|||Phosphoserine|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218467|||http://purl.uniprot.org/annotation/VAR_058478
http://togogenome.org/gene/9606:OR56A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWQ5|||http://purl.uniprot.org/uniprot/A0A2C9F2M6|||http://purl.uniprot.org/uniprot/Q8NGH8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 56A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150795
http://togogenome.org/gene/9606:LCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13796                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation and reduces the cell surface expression of CD69 and IL2RA. Reduces association with the actin cytoskeleton.|||Actin-binding 1|||Actin-binding 2|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Calponin-homology (CH) 3|||Calponin-homology (CH) 4|||EF-hand 1|||EF-hand 2|||Found in a patient with isolated coloboma; increases interaction with actin.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Plastin-2|||Promotes association with the actin cytoskeleton.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073743|||http://purl.uniprot.org/annotation/VAR_001371|||http://purl.uniprot.org/annotation/VAR_024398|||http://purl.uniprot.org/annotation/VAR_030826|||http://purl.uniprot.org/annotation/VAR_079850|||http://purl.uniprot.org/annotation/VSP_056450|||http://purl.uniprot.org/annotation/VSP_056451
http://togogenome.org/gene/9606:FAM47E-STBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Protein FAM47E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326074|||http://purl.uniprot.org/annotation/VSP_040931|||http://purl.uniprot.org/annotation/VSP_040932|||http://purl.uniprot.org/annotation/VSP_040933|||http://purl.uniprot.org/annotation/VSP_040934
http://togogenome.org/gene/9606:ARSK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWY0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase K|||In MPS10; mutant protein is not detected by Western blot in transfected cells; severely decreased glucuronate-2-sulfatase activity.|||In MPS10; no effect on protein abundance; decreased glucuronate-2-sulfatase activity.|||Loss of arylsulfatase and glucuronate-2-sulfatase activity.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042219|||http://purl.uniprot.org/annotation/VAR_052516|||http://purl.uniprot.org/annotation/VAR_086963|||http://purl.uniprot.org/annotation/VAR_086964
http://togogenome.org/gene/9606:MSH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15457                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In SPGF2 and POF20.|||In SPGF2.|||In SPGF2; severely decreased MSH4 transcript and protein levels in testicular tissue from a homozygous patient.|||In SPGF2; unknown pathological significance.|||MutS protein homolog 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115197|||http://purl.uniprot.org/annotation/VAR_018831|||http://purl.uniprot.org/annotation/VAR_018832|||http://purl.uniprot.org/annotation/VAR_018833|||http://purl.uniprot.org/annotation/VAR_018834|||http://purl.uniprot.org/annotation/VAR_018835|||http://purl.uniprot.org/annotation/VAR_018836|||http://purl.uniprot.org/annotation/VAR_087408|||http://purl.uniprot.org/annotation/VAR_087409|||http://purl.uniprot.org/annotation/VAR_087410|||http://purl.uniprot.org/annotation/VAR_087411|||http://purl.uniprot.org/annotation/VAR_087412|||http://purl.uniprot.org/annotation/VAR_087413|||http://purl.uniprot.org/annotation/VAR_087414
http://togogenome.org/gene/9606:FCAMR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S2|||http://purl.uniprot.org/uniprot/Q8WWV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||High affinity immunoglobulin alpha and immunoglobulin mu Fc receptor|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates immunoglobulin Fc fragment-binding|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331483|||http://purl.uniprot.org/annotation/VSP_033227|||http://purl.uniprot.org/annotation/VSP_033228|||http://purl.uniprot.org/annotation/VSP_033229|||http://purl.uniprot.org/annotation/VSP_033230|||http://purl.uniprot.org/annotation/VSP_033231|||http://purl.uniprot.org/annotation/VSP_033232
http://togogenome.org/gene/9606:PLAAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWW9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Cytoplasmic|||Helical|||LRAT|||Loss of N-acyltransferase activity.|||Lumenal|||Phospholipase A and acyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152483
http://togogenome.org/gene/9606:PKP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y446                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Disordered|||In isoform PKP3b.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Plakophilin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064287|||http://purl.uniprot.org/annotation/VSP_053646
http://togogenome.org/gene/9606:MEIKIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXM9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Meiosis-specific kinetochore protein|||POLO box domain (PBD)-binding|||Required for localization to kinetochores                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432390
http://togogenome.org/gene/9606:TP53TG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:PRR35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG20                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Proline-rich protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326184
http://togogenome.org/gene/9606:ZNF32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17041                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||Zinc finger protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047361
http://togogenome.org/gene/9606:CCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0R1|||http://purl.uniprot.org/uniprot/P10147                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  C-C motif chemokine|||C-C motif chemokine 3|||Chemokine interleukin-8-like|||Involved in GAG binding|||MIP-1-alpha(4-69)|||Reduces heparin binding.|||Reduces self-association.|||Reduces self-association; in BB-10010: Improved pharmaceutical properties.|||Slightly reduces heparin binding.|||Strongly reduces heparin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005156|||http://purl.uniprot.org/annotation/PRO_0000005157|||http://purl.uniprot.org/annotation/PRO_5014205097|||http://purl.uniprot.org/annotation/VAR_048701
http://togogenome.org/gene/9606:SP110                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo|||Disordered|||HSR|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3, isoform 4, isoform 5 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||May be associated with increased susceptibility to tuberculosis.|||Nuclear hormone receptor interaction|||Nuclear localization signal|||PHD-type|||Phosphoserine|||Polar residues|||Pro residues|||SAND|||Sp110 nuclear body protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074101|||http://purl.uniprot.org/annotation/VAR_027170|||http://purl.uniprot.org/annotation/VAR_027171|||http://purl.uniprot.org/annotation/VAR_027172|||http://purl.uniprot.org/annotation/VAR_027173|||http://purl.uniprot.org/annotation/VAR_027174|||http://purl.uniprot.org/annotation/VAR_027175|||http://purl.uniprot.org/annotation/VAR_027176|||http://purl.uniprot.org/annotation/VAR_027177|||http://purl.uniprot.org/annotation/VAR_027178|||http://purl.uniprot.org/annotation/VAR_027179|||http://purl.uniprot.org/annotation/VAR_027180|||http://purl.uniprot.org/annotation/VAR_027181|||http://purl.uniprot.org/annotation/VAR_036029|||http://purl.uniprot.org/annotation/VAR_036030|||http://purl.uniprot.org/annotation/VAR_047051|||http://purl.uniprot.org/annotation/VAR_047052|||http://purl.uniprot.org/annotation/VSP_005991|||http://purl.uniprot.org/annotation/VSP_005992|||http://purl.uniprot.org/annotation/VSP_005994|||http://purl.uniprot.org/annotation/VSP_005995|||http://purl.uniprot.org/annotation/VSP_005996|||http://purl.uniprot.org/annotation/VSP_005997|||http://purl.uniprot.org/annotation/VSP_006000|||http://purl.uniprot.org/annotation/VSP_006001|||http://purl.uniprot.org/annotation/VSP_006002|||http://purl.uniprot.org/annotation/VSP_035593|||http://purl.uniprot.org/annotation/VSP_046079
http://togogenome.org/gene/9606:TUBB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCM7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Acidic residues|||Disordered|||In OZEMA2; decreased alpha/beta-tubulin heterodimer assembly; does not affect function in meiotic spindle assembly.|||In OZEMA2; decreased alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly.|||In OZEMA2; loss of alpha/beta-tubulin heterodimer assembly; loss of function in meiotic spindle assembly.|||In OZEMA2; loss of function in meiotic spindle assembly and oocyte maturation; when expressed in mouse oocytes it leads to abnormal spindle structure and maturation arrest.|||In OZEMA2; loss of function in meiotic spindle assembly.|||In OZEMA2; loss of function in oocyte maturation; decreased alpha/beta-tubulin heterodimer assembly.|||In OZEMA2; loss of function in oocyte maturation; loss of function in meiotic spindle assembly; decreased alpha/beta-tubulin heterodimer assembly.|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-8 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320631|||http://purl.uniprot.org/annotation/VAR_039240|||http://purl.uniprot.org/annotation/VAR_076898|||http://purl.uniprot.org/annotation/VAR_076899|||http://purl.uniprot.org/annotation/VAR_076900|||http://purl.uniprot.org/annotation/VAR_076901|||http://purl.uniprot.org/annotation/VAR_076902|||http://purl.uniprot.org/annotation/VAR_076903|||http://purl.uniprot.org/annotation/VAR_076904|||http://purl.uniprot.org/annotation/VAR_076905|||http://purl.uniprot.org/annotation/VAR_076906|||http://purl.uniprot.org/annotation/VAR_076907|||http://purl.uniprot.org/annotation/VAR_076908|||http://purl.uniprot.org/annotation/VAR_076909|||http://purl.uniprot.org/annotation/VAR_076910|||http://purl.uniprot.org/annotation/VAR_076911|||http://purl.uniprot.org/annotation/VAR_087566|||http://purl.uniprot.org/annotation/VAR_087567
http://togogenome.org/gene/9606:CLDN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56747                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-6|||Cytoplasmic|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144748|||http://purl.uniprot.org/annotation/VAR_017151
http://togogenome.org/gene/9606:CIMAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCI5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule-associated protein 3|||Found in patients with severe ciliopathies and left-right asymmetry defects; inhibits AURKA activity.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284526|||http://purl.uniprot.org/annotation/VAR_031767|||http://purl.uniprot.org/annotation/VAR_031768|||http://purl.uniprot.org/annotation/VAR_066484|||http://purl.uniprot.org/annotation/VSP_024557|||http://purl.uniprot.org/annotation/VSP_042040
http://togogenome.org/gene/9606:TANC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EK39|||http://purl.uniprot.org/uniprot/Q9C0D5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein TANC1|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316959|||http://purl.uniprot.org/annotation/VAR_038435|||http://purl.uniprot.org/annotation/VAR_038436|||http://purl.uniprot.org/annotation/VAR_038437|||http://purl.uniprot.org/annotation/VAR_061022|||http://purl.uniprot.org/annotation/VSP_030828
http://togogenome.org/gene/9606:NELFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFX9|||http://purl.uniprot.org/uniprot/Q9H3P2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||HDAg|||In isoform 2.|||NELF-C/D-binding|||Negative elongation factor A|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNAPII-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219126|||http://purl.uniprot.org/annotation/VAR_059459|||http://purl.uniprot.org/annotation/VSP_035589
http://togogenome.org/gene/9606:DHX38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92620                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In RP84.|||In RP84; unknown pathological significance.|||In isoform 2.|||N-acetylglycine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055147|||http://purl.uniprot.org/annotation/VAR_015518|||http://purl.uniprot.org/annotation/VAR_081338|||http://purl.uniprot.org/annotation/VAR_081339|||http://purl.uniprot.org/annotation/VSP_056045
http://togogenome.org/gene/9606:IL12RB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42701                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||In IMD30.|||In isoform 2.|||In isoform 3.|||Interleukin-12 receptor subunit beta-1|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010917|||http://purl.uniprot.org/annotation/VAR_011986|||http://purl.uniprot.org/annotation/VAR_011987|||http://purl.uniprot.org/annotation/VAR_015577|||http://purl.uniprot.org/annotation/VAR_021281|||http://purl.uniprot.org/annotation/VAR_021282|||http://purl.uniprot.org/annotation/VAR_021283|||http://purl.uniprot.org/annotation/VAR_021284|||http://purl.uniprot.org/annotation/VAR_021285|||http://purl.uniprot.org/annotation/VSP_001715|||http://purl.uniprot.org/annotation/VSP_037043|||http://purl.uniprot.org/annotation/VSP_037044
http://togogenome.org/gene/9606:IL21R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBE5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||C-linked (Man) tryptophan|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In IMD56; loss of function mutation.|||In IMD56; loss of function mutation; the mutation results in defective trafficking of the protein, with misfolding, impaired processing and abnormal subcellular distribution rather than proper expression at the plasma membrane.|||Interleukin-21 receptor|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010881|||http://purl.uniprot.org/annotation/VAR_014360|||http://purl.uniprot.org/annotation/VAR_014361|||http://purl.uniprot.org/annotation/VAR_014362|||http://purl.uniprot.org/annotation/VAR_069898|||http://purl.uniprot.org/annotation/VAR_069899
http://togogenome.org/gene/9606:HFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2PYH4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In POF9.|||In isoform 2.|||Probable ATP-dependent DNA helicase HFM1|||SEC63                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324393|||http://purl.uniprot.org/annotation/VAR_039799|||http://purl.uniprot.org/annotation/VAR_039800|||http://purl.uniprot.org/annotation/VAR_049338|||http://purl.uniprot.org/annotation/VAR_071262|||http://purl.uniprot.org/annotation/VAR_071263|||http://purl.uniprot.org/annotation/VSP_032249|||http://purl.uniprot.org/annotation/VSP_032250|||http://purl.uniprot.org/annotation/VSP_032251
http://togogenome.org/gene/9606:TMEM238                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JI98                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Transmembrane protein 238                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413540
http://togogenome.org/gene/9606:ADD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FL4|||http://purl.uniprot.org/uniprot/Q59EK1|||http://purl.uniprot.org/uniprot/Q5VU08|||http://purl.uniprot.org/uniprot/Q9UEY8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Class II aldolase/adducin N-terminal|||Cleavage by asparagine endopeptidase (AEP)|||Disordered|||Gamma-adducin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CPSQ3; decreased actin capping activity; increased fibroblast proliferation and migration; decreased colocalization with alpha subunit ADD1.|||In isoform 1.|||Interaction with calmodulin|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218536|||http://purl.uniprot.org/annotation/VAR_076996|||http://purl.uniprot.org/annotation/VSP_000188
http://togogenome.org/gene/9606:MMGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4V1                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||ER membrane protein complex subunit 5|||Helical|||In isoform 2.|||Lumenal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286435|||http://purl.uniprot.org/annotation/VSP_036488
http://togogenome.org/gene/9606:ACO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99798                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Aconitate hydratase, mitochondrial|||Disordered|||In ICRD.|||In ICRD; functional expression studies in yeast show that the mutant has decreased function under growth conditions requiring the TCA cycle and the glyoxylate shunt.|||In OPA9.|||In a breast cancer sample; somatic mutation.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000541|||http://purl.uniprot.org/annotation/VAR_033297|||http://purl.uniprot.org/annotation/VAR_036572|||http://purl.uniprot.org/annotation/VAR_067543|||http://purl.uniprot.org/annotation/VAR_073435|||http://purl.uniprot.org/annotation/VAR_073436|||http://purl.uniprot.org/annotation/VAR_073437|||http://purl.uniprot.org/annotation/VAR_073438
http://togogenome.org/gene/9606:HS2ST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LGA3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate 2-O-sulfotransferase 1|||In NFSRA.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207674|||http://purl.uniprot.org/annotation/VAR_085252|||http://purl.uniprot.org/annotation/VAR_085253|||http://purl.uniprot.org/annotation/VAR_085254|||http://purl.uniprot.org/annotation/VSP_014062|||http://purl.uniprot.org/annotation/VSP_014063|||http://purl.uniprot.org/annotation/VSP_014064
http://togogenome.org/gene/9606:HACL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXR1|||http://purl.uniprot.org/uniprot/Q9UJ83                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  2-hydroxyacyl-CoA lyase 1|||Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-455.|||Does not affect subcellular localization. Abolishes lyase activity. Does not affect subcellular localization, abolishes lyase activity, does not affect oligomerisation and does not bind TTP; when associated with S-456.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Microbody targeting signal|||N6-succinyllysine|||Phosphoserine|||Thiamine pyrophosphate binding|||Thiamine pyrophosphate enzyme N-terminal TPP-binding|||Thiamine pyrophosphate enzyme TPP-binding|||Thiamine pyrophosphate enzyme central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090816|||http://purl.uniprot.org/annotation/VSP_054191|||http://purl.uniprot.org/annotation/VSP_054192|||http://purl.uniprot.org/annotation/VSP_054749|||http://purl.uniprot.org/annotation/VSP_054750
http://togogenome.org/gene/9606:RNGTT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSJ8|||http://purl.uniprot.org/uniprot/O60942|||http://purl.uniprot.org/uniprot/Q7Z3R6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||GTase|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with POLR2A|||Loss of GTase activity.|||N6-GMP-lysine intermediate|||No effect on GTase activity.|||Phosphocysteine intermediate|||Pro residues|||Strongly reduced GTase activity.|||TPase|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||mRNA capping enzyme C-terminal|||mRNA-capping enzyme                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210108|||http://purl.uniprot.org/annotation/VAR_046481|||http://purl.uniprot.org/annotation/VSP_003202|||http://purl.uniprot.org/annotation/VSP_003203|||http://purl.uniprot.org/annotation/VSP_003204
http://togogenome.org/gene/9606:OR2J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZK6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150482|||http://purl.uniprot.org/annotation/VAR_019066
http://togogenome.org/gene/9606:FAM171A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM171A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328771
http://togogenome.org/gene/9606:FKRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9S5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects the tetramer assembly. Decreases the ribitol-5-phosphate transferase activity of about 80%.|||Cytoplasmic|||Decrease in ribitol-5-phosphate transferase activity. Does not affect protein expression. Loss of ribitol-5-phosphate transferase activity.|||Does not affect protein expression. Loss of ribitol-5-phosphate transferase activity.|||Helical|||In MDDGA5; severe Walker-Warburg syndrome.|||In MDDGB5 and MDDGC5.|||In MDDGB5.|||In MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI.|||In MDDGB5; severe form; brain involvement; intellectual disability and cerebellar cysts on cranial MRI; affects tetramer assembly; decreases the ribitol 5-phosphate transferase activity of about 95%..|||In MDDGB5; strongly reduced secretion to the medium; localizes mainly to the ER compartment.|||In MDDGB5; unknown pathological significance.|||In MDDGC5 and MDDGA5; muscle-eye-brain disease, decrease in ribitol-5-phosphate transferase activity..|||In MDDGC5.|||In MDDGC5; reduced secretion to the medium; localizes mainly to the Golgi apparatus; affects tetramer assembly; decreases the ribitol-5-phosphate transferase activity of about 50%..|||In MDDGC5; unknown pathological significance.|||Interchain|||Lumenal|||N-linked (GlcNAc...) asparagine|||Ribitol 5-phosphate transferase FKRP|||Zinc finger loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204723|||http://purl.uniprot.org/annotation/VAR_018280|||http://purl.uniprot.org/annotation/VAR_018281|||http://purl.uniprot.org/annotation/VAR_018282|||http://purl.uniprot.org/annotation/VAR_018283|||http://purl.uniprot.org/annotation/VAR_018284|||http://purl.uniprot.org/annotation/VAR_018285|||http://purl.uniprot.org/annotation/VAR_018286|||http://purl.uniprot.org/annotation/VAR_018287|||http://purl.uniprot.org/annotation/VAR_018288|||http://purl.uniprot.org/annotation/VAR_018289|||http://purl.uniprot.org/annotation/VAR_018290|||http://purl.uniprot.org/annotation/VAR_018291|||http://purl.uniprot.org/annotation/VAR_018292|||http://purl.uniprot.org/annotation/VAR_018293|||http://purl.uniprot.org/annotation/VAR_018294|||http://purl.uniprot.org/annotation/VAR_018295|||http://purl.uniprot.org/annotation/VAR_019272|||http://purl.uniprot.org/annotation/VAR_022850|||http://purl.uniprot.org/annotation/VAR_022851|||http://purl.uniprot.org/annotation/VAR_022852|||http://purl.uniprot.org/annotation/VAR_022853|||http://purl.uniprot.org/annotation/VAR_022854|||http://purl.uniprot.org/annotation/VAR_022855|||http://purl.uniprot.org/annotation/VAR_022856|||http://purl.uniprot.org/annotation/VAR_065055|||http://purl.uniprot.org/annotation/VAR_065056|||http://purl.uniprot.org/annotation/VAR_065057|||http://purl.uniprot.org/annotation/VAR_065058|||http://purl.uniprot.org/annotation/VAR_065059|||http://purl.uniprot.org/annotation/VAR_065060|||http://purl.uniprot.org/annotation/VAR_065061|||http://purl.uniprot.org/annotation/VAR_065062|||http://purl.uniprot.org/annotation/VAR_065063|||http://purl.uniprot.org/annotation/VAR_081096
http://togogenome.org/gene/9606:OR2M2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWI7|||http://purl.uniprot.org/uniprot/Q96R28                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2M2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150491|||http://purl.uniprot.org/annotation/VAR_034179|||http://purl.uniprot.org/annotation/VAR_059990|||http://purl.uniprot.org/annotation/VAR_059991|||http://purl.uniprot.org/annotation/VAR_062026
http://togogenome.org/gene/9606:PHKG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6U2|||http://purl.uniprot.org/uniprot/Q16816                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding (domain-C)|||Calmodulin-binding (domain-N)|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086508|||http://purl.uniprot.org/annotation/VAR_040994|||http://purl.uniprot.org/annotation/VAR_040995|||http://purl.uniprot.org/annotation/VSP_044716
http://togogenome.org/gene/9606:TRADD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15628                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolished GlcNAcylation by E.coli NleB1. Abolished ability to self-oligomerize. Strongly reduced GlcNAcylation by S.typhimurium Ssek1; when associated with A-245.|||Death|||Disordered|||In isoform 2.|||Interaction with KRT14 and KRT18|||Nuclear export signal|||Nuclear localization signal|||Strongly reduced GlcNAcylation by S.typhimurium Ssek1; when associated with A-235.|||Tumor necrosis factor receptor type 1-associated DEATH domain protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065602|||http://purl.uniprot.org/annotation/VSP_056526
http://togogenome.org/gene/9606:EPHB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WCM8|||http://purl.uniprot.org/uniprot/J3KQU5|||http://purl.uniprot.org/uniprot/O15197                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Eph LBD|||Ephrin type-B receptor 6|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Protein kinase|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016837|||http://purl.uniprot.org/annotation/PRO_5014571689|||http://purl.uniprot.org/annotation/VAR_019139|||http://purl.uniprot.org/annotation/VAR_019140|||http://purl.uniprot.org/annotation/VAR_019141|||http://purl.uniprot.org/annotation/VAR_019142|||http://purl.uniprot.org/annotation/VAR_036091|||http://purl.uniprot.org/annotation/VAR_036092|||http://purl.uniprot.org/annotation/VAR_036093|||http://purl.uniprot.org/annotation/VAR_036094|||http://purl.uniprot.org/annotation/VAR_042190|||http://purl.uniprot.org/annotation/VAR_042191|||http://purl.uniprot.org/annotation/VAR_042192|||http://purl.uniprot.org/annotation/VAR_042193|||http://purl.uniprot.org/annotation/VAR_042194|||http://purl.uniprot.org/annotation/VAR_042195|||http://purl.uniprot.org/annotation/VAR_042196|||http://purl.uniprot.org/annotation/VAR_042197|||http://purl.uniprot.org/annotation/VAR_042198|||http://purl.uniprot.org/annotation/VAR_042199|||http://purl.uniprot.org/annotation/VSP_037496|||http://purl.uniprot.org/annotation/VSP_037497|||http://purl.uniprot.org/annotation/VSP_037498
http://togogenome.org/gene/9606:PIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H611                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA helicase PIF1|||Disordered|||Hydrolyzes ATP in the presence of both magnesium and single-stranded DNA; weak activity in the presence of RNA or double-stranded DNA; No unwinding activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of ATPase activity. Lower activity for single-stranded DNA.|||PINT|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089980|||http://purl.uniprot.org/annotation/VAR_033206|||http://purl.uniprot.org/annotation/VSP_026715|||http://purl.uniprot.org/annotation/VSP_026716|||http://purl.uniprot.org/annotation/VSP_026717|||http://purl.uniprot.org/annotation/VSP_047457
http://togogenome.org/gene/9606:MCCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z693|||http://purl.uniprot.org/uniprot/Q68D27|||http://purl.uniprot.org/uniprot/Q96RQ3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  ATP-grasp|||Biotin carboxylation|||Biotinyl-binding|||In MCC1D.|||In MCC1D; associated with a reduction of wild-type residual activity.|||In MCC1D; asymptomatic form.|||In MCC1D; clinically asymptomatic form.|||In MCC1D; mild form.|||In MCC1D; severe form.|||In MCC1D; shows no residual activity.|||In MCC1D; shows some wild-type residual activity.|||In MCC1D; unknown pathological significance.|||Lipoyl-binding|||Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-biotinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002833|||http://purl.uniprot.org/annotation/VAR_012785|||http://purl.uniprot.org/annotation/VAR_012786|||http://purl.uniprot.org/annotation/VAR_012787|||http://purl.uniprot.org/annotation/VAR_012788|||http://purl.uniprot.org/annotation/VAR_012789|||http://purl.uniprot.org/annotation/VAR_012790|||http://purl.uniprot.org/annotation/VAR_012791|||http://purl.uniprot.org/annotation/VAR_038631|||http://purl.uniprot.org/annotation/VAR_067197|||http://purl.uniprot.org/annotation/VAR_067198|||http://purl.uniprot.org/annotation/VAR_072486|||http://purl.uniprot.org/annotation/VAR_072487|||http://purl.uniprot.org/annotation/VAR_072488|||http://purl.uniprot.org/annotation/VAR_072489|||http://purl.uniprot.org/annotation/VAR_072490|||http://purl.uniprot.org/annotation/VAR_072491|||http://purl.uniprot.org/annotation/VAR_072492|||http://purl.uniprot.org/annotation/VAR_072493|||http://purl.uniprot.org/annotation/VAR_072494|||http://purl.uniprot.org/annotation/VAR_072495|||http://purl.uniprot.org/annotation/VAR_072496|||http://purl.uniprot.org/annotation/VAR_072497|||http://purl.uniprot.org/annotation/VAR_072498|||http://purl.uniprot.org/annotation/VAR_072499|||http://purl.uniprot.org/annotation/VAR_072500|||http://purl.uniprot.org/annotation/VAR_072501|||http://purl.uniprot.org/annotation/VAR_072502|||http://purl.uniprot.org/annotation/VAR_072503|||http://purl.uniprot.org/annotation/VAR_072504|||http://purl.uniprot.org/annotation/VAR_072505|||http://purl.uniprot.org/annotation/VAR_072506|||http://purl.uniprot.org/annotation/VAR_077284|||http://purl.uniprot.org/annotation/VAR_077285|||http://purl.uniprot.org/annotation/VAR_077286|||http://purl.uniprot.org/annotation/VAR_077287|||http://purl.uniprot.org/annotation/VAR_077288|||http://purl.uniprot.org/annotation/VAR_077289|||http://purl.uniprot.org/annotation/VAR_077290|||http://purl.uniprot.org/annotation/VAR_079752
http://togogenome.org/gene/9606:SLX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY92                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||Disordered|||Does not modify the functional properties of the protein.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with MUS81|||Interaction with PLK1 and TERF2-TERF2IP|||Interaction with SLX1|||Interaction with SLX4IP, ERCC4/XPF and MSH2|||Likely benign variant; does not modify the functional properties of the protein.|||Phosphoserine|||Polar residues|||Requires 2 nucleotide substitutions.|||Structure-specific endonuclease subunit SLX4|||UBZ4-type 1|||UBZ4-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186219|||http://purl.uniprot.org/annotation/VAR_019326|||http://purl.uniprot.org/annotation/VAR_019327|||http://purl.uniprot.org/annotation/VAR_019729|||http://purl.uniprot.org/annotation/VAR_046337|||http://purl.uniprot.org/annotation/VAR_046338|||http://purl.uniprot.org/annotation/VAR_068982|||http://purl.uniprot.org/annotation/VAR_068983|||http://purl.uniprot.org/annotation/VAR_068984|||http://purl.uniprot.org/annotation/VAR_068985|||http://purl.uniprot.org/annotation/VAR_068986|||http://purl.uniprot.org/annotation/VAR_068987|||http://purl.uniprot.org/annotation/VAR_068988|||http://purl.uniprot.org/annotation/VAR_068989|||http://purl.uniprot.org/annotation/VAR_068990|||http://purl.uniprot.org/annotation/VAR_068991|||http://purl.uniprot.org/annotation/VAR_068992|||http://purl.uniprot.org/annotation/VAR_068993|||http://purl.uniprot.org/annotation/VAR_068994|||http://purl.uniprot.org/annotation/VAR_068995|||http://purl.uniprot.org/annotation/VAR_068996|||http://purl.uniprot.org/annotation/VAR_068997|||http://purl.uniprot.org/annotation/VAR_068998|||http://purl.uniprot.org/annotation/VAR_068999|||http://purl.uniprot.org/annotation/VAR_069000|||http://purl.uniprot.org/annotation/VAR_069001|||http://purl.uniprot.org/annotation/VAR_069002|||http://purl.uniprot.org/annotation/VAR_069003|||http://purl.uniprot.org/annotation/VAR_069004|||http://purl.uniprot.org/annotation/VAR_069005|||http://purl.uniprot.org/annotation/VAR_069006|||http://purl.uniprot.org/annotation/VAR_069007|||http://purl.uniprot.org/annotation/VAR_069008|||http://purl.uniprot.org/annotation/VAR_069009|||http://purl.uniprot.org/annotation/VAR_069010|||http://purl.uniprot.org/annotation/VAR_069011|||http://purl.uniprot.org/annotation/VAR_069012|||http://purl.uniprot.org/annotation/VAR_069013|||http://purl.uniprot.org/annotation/VAR_069014|||http://purl.uniprot.org/annotation/VAR_069015|||http://purl.uniprot.org/annotation/VAR_069016|||http://purl.uniprot.org/annotation/VAR_069017|||http://purl.uniprot.org/annotation/VSP_035295|||http://purl.uniprot.org/annotation/VSP_035296
http://togogenome.org/gene/9606:RMI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E14                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RMI1, TOP3A and BLM.|||According to PubMed:18923083, abolishes interaction with RMI1, TOP3A and BLM. According to PubMed:18923082, does not affect interaction with RMI1 and TOP3A.|||According to PubMed:18923083, does not affect interaction with RMI1, TOP3A and BLM. According to PubMed:18923082, affects interaction with BLM and the BMI complex.|||Disordered|||Does not affect interaction with RMI1, TOP3A and BLM.|||In isoform 2.|||N-acetylalanine|||OB|||Phosphoserine|||RecQ-mediated genome instability protein 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297577|||http://purl.uniprot.org/annotation/VSP_027287
http://togogenome.org/gene/9606:SH2D2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5UBZ2|||http://purl.uniprot.org/uniprot/Q5UBZ3|||http://purl.uniprot.org/uniprot/Q9NP31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||SH2|||SH2 domain-containing protein 2A|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097726|||http://purl.uniprot.org/annotation/VAR_024349|||http://purl.uniprot.org/annotation/VAR_056986|||http://purl.uniprot.org/annotation/VSP_003965|||http://purl.uniprot.org/annotation/VSP_003966|||http://purl.uniprot.org/annotation/VSP_046378
http://togogenome.org/gene/9606:ANKS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXP1|||http://purl.uniprot.org/uniprot/Q68DC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  3-hydroxyasparagine|||ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SAM domain-containing protein 6|||Disordered|||Essential for ANKS3 interaction|||In NPHP16.|||In isoform 2.|||In isoform 3.|||Loss of interaction with ANKS3.|||Phosphoserine|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067065|||http://purl.uniprot.org/annotation/VAR_034794|||http://purl.uniprot.org/annotation/VAR_070105|||http://purl.uniprot.org/annotation/VAR_070106|||http://purl.uniprot.org/annotation/VAR_070107|||http://purl.uniprot.org/annotation/VAR_070108|||http://purl.uniprot.org/annotation/VAR_070109|||http://purl.uniprot.org/annotation/VAR_070110|||http://purl.uniprot.org/annotation/VSP_016496|||http://purl.uniprot.org/annotation/VSP_016497|||http://purl.uniprot.org/annotation/VSP_016498
http://togogenome.org/gene/9606:C9orf57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0N0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Uncharacterized protein C9orf57                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227549|||http://purl.uniprot.org/annotation/VSP_056909
http://togogenome.org/gene/9606:PSKH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11801                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Loss of autophosphorylation.|||N-myristoyl glycine|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||Serine/threonine-protein kinase H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086167|||http://purl.uniprot.org/annotation/VAR_040614
http://togogenome.org/gene/9606:NBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5R6|||http://purl.uniprot.org/uniprot/Q14596                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ATG8 family protein-binding|||About 2-fold weaker interaction with ubiquitin than WT.|||About 3-fold weaker interaction with ubiquitin than WT.|||Acidic residues|||Complete loss of interaction with ubiquitin.|||Disordered|||In isoform 2.|||Loss of interaction ATG8 family proteins.|||Loss of interaction with SQSTM1.|||Loss of phosphorylation by GSK3A.|||Next to BRCA1 gene 1 protein|||No effect on interaction with SQSTM1.|||PB1|||Phosphoserine|||Phosphothreonine; by GSK3-alpha|||UBA|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096746|||http://purl.uniprot.org/annotation/VAR_016106|||http://purl.uniprot.org/annotation/VSP_004314
http://togogenome.org/gene/9606:LPAR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBY5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lysophosphatidic acid receptor 3|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069433|||http://purl.uniprot.org/annotation/VAR_049415
http://togogenome.org/gene/9606:WDR27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRH5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306831|||http://purl.uniprot.org/annotation/VAR_035317|||http://purl.uniprot.org/annotation/VAR_035318|||http://purl.uniprot.org/annotation/VAR_035319|||http://purl.uniprot.org/annotation/VAR_035320|||http://purl.uniprot.org/annotation/VAR_035321|||http://purl.uniprot.org/annotation/VSP_028510|||http://purl.uniprot.org/annotation/VSP_028511|||http://purl.uniprot.org/annotation/VSP_028512|||http://purl.uniprot.org/annotation/VSP_040796|||http://purl.uniprot.org/annotation/VSP_040797
http://togogenome.org/gene/9606:B4GAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43505                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-glucuronyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In MDDGA13; no effect on Golgi localization; loss of beta-1,4-glucuronyltransferase activity.|||In Mut2; mislocalization to the endoplasmic reticulum.|||In Mut3; mislocalization to the endoplasmic reticulum.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080555|||http://purl.uniprot.org/annotation/VAR_025019|||http://purl.uniprot.org/annotation/VAR_069989|||http://purl.uniprot.org/annotation/VAR_069990
http://togogenome.org/gene/9606:SNAPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RC42|||http://purl.uniprot.org/uniprot/Q16533                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||SNAPC3-binding|||SNAPC4-binding|||snRNA-activating protein complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072017
http://togogenome.org/gene/9606:CFAP68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5F2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089829|||http://purl.uniprot.org/annotation/VAR_050861|||http://purl.uniprot.org/annotation/VAR_050862|||http://purl.uniprot.org/annotation/VAR_054163
http://togogenome.org/gene/9606:IFNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GUN5|||http://purl.uniprot.org/uniprot/P01563                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In allele alpha-2A.|||In allele alpha-2C.|||Interferon alpha-2|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000049|||http://purl.uniprot.org/annotation/PRO_0000016360|||http://purl.uniprot.org/annotation/PRO_5031403293|||http://purl.uniprot.org/annotation/VAR_004012|||http://purl.uniprot.org/annotation/VAR_013001|||http://purl.uniprot.org/annotation/VAR_036329|||http://purl.uniprot.org/annotation/VAR_055972
http://togogenome.org/gene/9606:HLA-DRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JMH6|||http://purl.uniprot.org/uniprot/P01903                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Almost no change in down-regulation of MHCII. No ubiquitination and complete loss of down-regulation of MHCII; when associated with 'R-254' of HLA-DRB.|||Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Decreases the affinity of the interaction with TCR by more than five-fold.|||Decreases the interaction with CD4.|||Decreases the interaction with HLA-DM complex and peptide exchange.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HLA class II histocompatibility antigen, DR alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||Impairs the interaction with HLA-DM complex and peptide exchange.|||Impairs the interaction with HLA-DM complex, CLIP dissociation and peptide exchange.|||In allele DRA*01:01.|||Increases the interaction with HLA-DM complex and peptide exchange.|||Increases the interaction with HLA-DM complex and peptide exchange. Decreases the affinity of the interaction with TCR by more than five-fold.|||N-linked (GlcNAc...) asparagine|||Pathogen-derived peptide antigen|||Self- and pathogen-derived peptide antigen|||Self-peptide antigen                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018947|||http://purl.uniprot.org/annotation/PRO_5014514161|||http://purl.uniprot.org/annotation/VAR_004399|||http://purl.uniprot.org/annotation/VAR_035241
http://togogenome.org/gene/9606:GPBAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDU6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled bile acid receptor 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069500
http://togogenome.org/gene/9606:KIF4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYE2|||http://purl.uniprot.org/uniprot/Q2VIQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CRD; required for [4Fe-4S] cluster binding and localization to the spindle midzone and midbody during anaphase and telophase|||Chromosome-associated kinesin KIF4B|||Disordered|||Globular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with PRC1|||Kinesin motor|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301666|||http://purl.uniprot.org/annotation/VAR_049695|||http://purl.uniprot.org/annotation/VAR_049696|||http://purl.uniprot.org/annotation/VAR_049697|||http://purl.uniprot.org/annotation/VAR_061281
http://togogenome.org/gene/9606:FAM204A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8W3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Protein FAM204A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089808
http://togogenome.org/gene/9606:GAGE2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NT46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395445
http://togogenome.org/gene/9606:SAA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35542                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Confirmed at protein level.|||Disordered|||N-linked (GlcNAc...) asparagine; partial|||Serum amyloid A-4 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031583|||http://purl.uniprot.org/annotation/VAR_051893
http://togogenome.org/gene/9606:ACSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0E8|||http://purl.uniprot.org/uniprot/Q6DKJ3|||http://purl.uniprot.org/uniprot/Q96FY7|||http://purl.uniprot.org/uniprot/Q9NR19                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Acetyl-coenzyme A synthetase N-terminal|||Acetyl-coenzyme A synthetase, cytoplasmic|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208423|||http://purl.uniprot.org/annotation/VSP_046376
http://togogenome.org/gene/9606:OR8I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Y5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8I2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150668|||http://purl.uniprot.org/annotation/VAR_034266|||http://purl.uniprot.org/annotation/VAR_034267
http://togogenome.org/gene/9606:KRT6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04259                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In PC4.|||Keratin, type II cytoskeletal 6B|||Linker 1|||Linker 12|||N-acetylalanine|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063732|||http://purl.uniprot.org/annotation/VAR_021265|||http://purl.uniprot.org/annotation/VAR_021266|||http://purl.uniprot.org/annotation/VAR_021267|||http://purl.uniprot.org/annotation/VAR_023062
http://togogenome.org/gene/9606:NTNG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CW9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||In NEDBASH; abolished cell surface expression.|||In NEDBASH; almost abolished cell surface expression.|||In NEDBASH; highly decreased cell surface expression.|||In isoform 2.|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin N-terminal|||N-linked (GlcNAc...) asparagine|||NGL discriminant loop I|||NGL discriminant loop II|||NGL discriminant loop III|||Netrin-G2|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017095|||http://purl.uniprot.org/annotation/PRO_0000017096|||http://purl.uniprot.org/annotation/VAR_047847|||http://purl.uniprot.org/annotation/VAR_083458|||http://purl.uniprot.org/annotation/VAR_083459|||http://purl.uniprot.org/annotation/VAR_083460|||http://purl.uniprot.org/annotation/VAR_083461|||http://purl.uniprot.org/annotation/VAR_083462|||http://purl.uniprot.org/annotation/VAR_083463|||http://purl.uniprot.org/annotation/VAR_083464|||http://purl.uniprot.org/annotation/VSP_013147|||http://purl.uniprot.org/annotation/VSP_013148
http://togogenome.org/gene/9606:NFU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMS0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Alters protein structure. Increases likelihood of existing as monomer. Decreases ability to receive a Fe/S clusters from donor proteins. Decreases delivery rates of [2Fe-2S] cluster to target proteins.|||In MMDS1; alters protein structure; increases likelihood of existing as monomer; decreases ability to receive a Fe/S clusters from donor proteins; decreases delivery rates of [2Fe-2S] cluster to target proteins.|||In MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes.|||In MMDS1; patient's skeletal muscles and fibroblasts show deficiency of mitochondrial respiratory chain complexes; increases homodimerization; unable to receive a Fe/S clusters from donor proteins; changes delivery rates of [2Fe-2S] cluster to target proteins.|||In MMDS1; patient's skin fibroblasts show deficiency of lipoic acid synthase and reduced lipoic acid content.|||In MMDS1; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||NFU1 iron-sulfur cluster scaffold homolog, mitochondrial|||NifU                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166191|||http://purl.uniprot.org/annotation/VAR_044429|||http://purl.uniprot.org/annotation/VAR_066639|||http://purl.uniprot.org/annotation/VAR_079757|||http://purl.uniprot.org/annotation/VAR_079758|||http://purl.uniprot.org/annotation/VAR_079759|||http://purl.uniprot.org/annotation/VAR_079760|||http://purl.uniprot.org/annotation/VSP_041224|||http://purl.uniprot.org/annotation/VSP_041225
http://togogenome.org/gene/9606:ARPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15145                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124042
http://togogenome.org/gene/9606:SLC38A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Solute carrier family 38 member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318975|||http://purl.uniprot.org/annotation/VAR_038927|||http://purl.uniprot.org/annotation/VAR_048126|||http://purl.uniprot.org/annotation/VSP_031323|||http://purl.uniprot.org/annotation/VSP_031324|||http://purl.uniprot.org/annotation/VSP_031325|||http://purl.uniprot.org/annotation/VSP_031326|||http://purl.uniprot.org/annotation/VSP_031327
http://togogenome.org/gene/9606:CPLX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PUV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Complexin-2|||Disordered|||Interaction with the SNARE complex|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144875
http://togogenome.org/gene/9606:NOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RA73|||http://purl.uniprot.org/uniprot/G3XAL1|||http://purl.uniprot.org/uniprot/Q9Y239                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Mutagenesis Site|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished interaction with ubiquitin without affecting interaction with RIPK2.|||Abolishes activation of NF-kappa-B. Abolished interaction with ubiquitin and RIPK2.|||Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2.|||Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2.|||Abolishes caspase-9 activation.|||Abolishes interaction with RIPK2/RICK.|||CARD|||Does not associate with cell membrane.|||Does not associate with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).|||In isoform 2.|||In isoform 3.|||Increased binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) in tetrapeptide-containing muropeptides (MurNAc-TetraDAP or TetraDAP).|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of activation by sphingosine-1-phosphate.|||NACHT|||No effect on activation of NF-kappa-B. Abolishes interaction with RIPK2.|||No effect on association with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).|||Nucleotide-binding oligomerization domain-containing protein 1|||Reduced NF-kappa-B activation in response to ligand binding.|||Reduced binding affinity for NLRP10.|||Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).|||Reduces caspase-9 activation. Reduced binding affinity for NLRP10. Does not associate with cell membrane. Reduced NF-kappa-B activation in response to ligand binding.|||S-palmitoyl cysteine|||Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-567.|||Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-952.|||Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-567 and S-952.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144077|||http://purl.uniprot.org/annotation/VAR_020371|||http://purl.uniprot.org/annotation/VAR_053624|||http://purl.uniprot.org/annotation/VAR_053625|||http://purl.uniprot.org/annotation/VAR_053626|||http://purl.uniprot.org/annotation/VAR_053627|||http://purl.uniprot.org/annotation/VSP_055825|||http://purl.uniprot.org/annotation/VSP_055826|||http://purl.uniprot.org/annotation/VSP_061942
http://togogenome.org/gene/9606:PNLIPRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54315                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Inactive pancreatic lipase-related protein 1|||Nucleophile|||PLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017790|||http://purl.uniprot.org/annotation/VAR_014915|||http://purl.uniprot.org/annotation/VAR_022082|||http://purl.uniprot.org/annotation/VAR_022659|||http://purl.uniprot.org/annotation/VAR_036379|||http://purl.uniprot.org/annotation/VAR_049820|||http://purl.uniprot.org/annotation/VSP_014097|||http://purl.uniprot.org/annotation/VSP_014098|||http://purl.uniprot.org/annotation/VSP_014099|||http://purl.uniprot.org/annotation/VSP_014100
http://togogenome.org/gene/9606:MLNR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43193                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform B.|||Motilin receptor|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069860|||http://purl.uniprot.org/annotation/VSP_001894
http://togogenome.org/gene/9606:TGIF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN2                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Decrease of phosphorylation. Strong decrease of phosphorylation; when associated with V-182.|||Decrease of phosphorylation. Strong decrease of phosphorylation; when associated with V-186.|||Disordered|||Homeobox protein TGIF2|||Homeobox; TALE-type|||In isoform 2.|||Phosphothreonine|||Repressive function                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049321|||http://purl.uniprot.org/annotation/VSP_047346|||http://purl.uniprot.org/annotation/VSP_047347
http://togogenome.org/gene/9606:TTBK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ55|||http://purl.uniprot.org/uniprot/Q8IWY7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes serine/threonine-protein kinase activity.|||Disordered|||Found in a patient with SCA11; unknown pathological significance.|||Impaired serine/threonine-protein kinase activity.|||In a lung small cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Leads to inactivation/destabilization of the protein.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Tau-tubulin kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234342|||http://purl.uniprot.org/annotation/VAR_041261|||http://purl.uniprot.org/annotation/VAR_041262|||http://purl.uniprot.org/annotation/VAR_041263|||http://purl.uniprot.org/annotation/VAR_041264|||http://purl.uniprot.org/annotation/VAR_041265|||http://purl.uniprot.org/annotation/VAR_041266|||http://purl.uniprot.org/annotation/VAR_041267|||http://purl.uniprot.org/annotation/VAR_041268|||http://purl.uniprot.org/annotation/VAR_041269|||http://purl.uniprot.org/annotation/VAR_041270|||http://purl.uniprot.org/annotation/VAR_041271|||http://purl.uniprot.org/annotation/VAR_069052|||http://purl.uniprot.org/annotation/VAR_069053|||http://purl.uniprot.org/annotation/VAR_076383|||http://purl.uniprot.org/annotation/VAR_076384|||http://purl.uniprot.org/annotation/VSP_018272|||http://purl.uniprot.org/annotation/VSP_018273|||http://purl.uniprot.org/annotation/VSP_018274|||http://purl.uniprot.org/annotation/VSP_018275
http://togogenome.org/gene/9606:TM4SF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53R12                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage of the first 13 residues.|||Cleavage|||Cytoplasmic|||Helical|||Inverts transmembrane topology.|||Inverts transmembrane topology. Induces cleavage of CREB3L1.|||Lumenal|||No effect on cleavage of the first 13 residues.|||No effect on glycosylation upon ceramide treatment.|||Reduces glycosylation upon ceramide treatment. Abolishes glycosylation upon ceramide treatment; when associated with Q-132 and Q-148.|||Reduces glycosylation upon ceramide treatment. Abolishes glycosylation upon ceramide treatment; when associated with Q-132 and Q-163.|||Transmembrane 4 L6 family member 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251228|||http://purl.uniprot.org/annotation/VAR_027673
http://togogenome.org/gene/9606:CASP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2CIS9|||http://purl.uniprot.org/uniprot/P31944                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Propeptide                                                                                  ^@                                                                                  Caspase family p10|||Caspase family p20|||Caspase-14 subunit p10, mature form|||Caspase-14 subunit p17, mature form|||Caspase-14 subunit p20, intermediate form|||Caspase-14 subunit p8, intermediate form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004652|||http://purl.uniprot.org/annotation/PRO_0000004654|||http://purl.uniprot.org/annotation/PRO_0000432793|||http://purl.uniprot.org/annotation/PRO_0000432794|||http://purl.uniprot.org/annotation/PRO_0000432795|||http://purl.uniprot.org/annotation/PRO_0000432796
http://togogenome.org/gene/9606:THOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI27                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In XLID12.|||In XLID12; normal amounts of mutant protein; normal amounts of other THO complex subunits.|||In XLID12; reduced amounts of mutant protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life.|||In XLID12; reduced amounts of protein; reduced amounts of other THO complex subunits; the mutant protein has a significantly shorter half-life.|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||THO complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072523|||http://purl.uniprot.org/annotation/VAR_075718|||http://purl.uniprot.org/annotation/VAR_075719|||http://purl.uniprot.org/annotation/VAR_075720|||http://purl.uniprot.org/annotation/VAR_075721|||http://purl.uniprot.org/annotation/VSP_008588
http://togogenome.org/gene/9606:SALL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In DRRS.|||In isoform SALL4B.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sal-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047026|||http://purl.uniprot.org/annotation/VAR_016042|||http://purl.uniprot.org/annotation/VAR_016043|||http://purl.uniprot.org/annotation/VAR_033054|||http://purl.uniprot.org/annotation/VSP_046525
http://togogenome.org/gene/9606:OR9A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150676|||http://purl.uniprot.org/annotation/VAR_053253
http://togogenome.org/gene/9606:CCDC175                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C221                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 175                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259927|||http://purl.uniprot.org/annotation/VAR_050871|||http://purl.uniprot.org/annotation/VAR_050872|||http://purl.uniprot.org/annotation/VAR_050873|||http://purl.uniprot.org/annotation/VAR_050874
http://togogenome.org/gene/9606:RHOF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBH0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||N-acetylmethionine|||Removed in mature form|||Rho-related GTP-binding protein RhoF|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198865|||http://purl.uniprot.org/annotation/PRO_0000281216|||http://purl.uniprot.org/annotation/VSP_013571|||http://purl.uniprot.org/annotation/VSP_013572
http://togogenome.org/gene/9606:RAB2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUD4|||http://purl.uniprot.org/uniprot/Q8WUD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Effector region|||In isoform 2.|||Phosphoserine|||Ras-related protein Rab-2B|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121071|||http://purl.uniprot.org/annotation/VAR_051709|||http://purl.uniprot.org/annotation/VSP_055829
http://togogenome.org/gene/9606:TSPAN15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95858                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219263
http://togogenome.org/gene/9606:DEFB105B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1I4|||http://purl.uniprot.org/uniprot/B2RU30|||http://purl.uniprot.org/uniprot/Q8NG35                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 105                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006975|||http://purl.uniprot.org/annotation/PRO_5005122712|||http://purl.uniprot.org/annotation/PRO_5034019771
http://togogenome.org/gene/9606:BRPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HI52|||http://purl.uniprot.org/uniprot/A0A804HKY8|||http://purl.uniprot.org/uniprot/P55201                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bromo|||C2H2-type|||C2HC pre-PHD-type|||Disordered|||In IDDDFP.|||In IDDDFP; decreased histone H3-K23 acetylation; changed cytoplasmic localization; no effect on expression and assembly of the MOZ/MORF complex.|||In IDDDFP; decreased histone H3-K23 acetylation; increased localization to the nucleus; decreased expression and assembly of the MOZ/MORF complex.|||In IDDDFP; no effect on histone H3-K23 acetylation; increased aggregation in the cytoplasm; no effect on expression and assembly of the MOZ/MORF complex.|||In IDDDFP; no effect on histone H3-K23 acetylation; no effect on expression and assembly of the MOZ/MORF complex.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KAT6A and KAT6B|||Interaction with MEAF6 and ING5|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||PWWP|||Peregrin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for RUNX1 and RUNX2 transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211187|||http://purl.uniprot.org/annotation/VAR_028232|||http://purl.uniprot.org/annotation/VAR_048430|||http://purl.uniprot.org/annotation/VAR_078076|||http://purl.uniprot.org/annotation/VAR_078077|||http://purl.uniprot.org/annotation/VAR_078078|||http://purl.uniprot.org/annotation/VAR_078079|||http://purl.uniprot.org/annotation/VAR_078080|||http://purl.uniprot.org/annotation/VAR_078081|||http://purl.uniprot.org/annotation/VAR_078082|||http://purl.uniprot.org/annotation/VSP_037955|||http://purl.uniprot.org/annotation/VSP_037956|||http://purl.uniprot.org/annotation/VSP_037957
http://togogenome.org/gene/9606:PLCD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3E9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3|||Acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Substrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306821|||http://purl.uniprot.org/annotation/VAR_035316
http://togogenome.org/gene/9606:PLCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15111                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||In isoform 2.|||Inactive phospholipase C-like protein 1|||Interaction with GABA A beta subunit|||Interaction with PPP1C|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319414|||http://purl.uniprot.org/annotation/VAR_038993|||http://purl.uniprot.org/annotation/VAR_038994|||http://purl.uniprot.org/annotation/VAR_038995|||http://purl.uniprot.org/annotation/VAR_038996|||http://purl.uniprot.org/annotation/VAR_038997|||http://purl.uniprot.org/annotation/VAR_038998|||http://purl.uniprot.org/annotation/VSP_031475
http://togogenome.org/gene/9606:NCR3LG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D85                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C1-type|||Ig-like V-type|||Interaction with NCR3|||N-linked (GlcNAc...) asparagine|||Natural cytotoxicity triggering receptor 3 ligand 1|||Polar residues|||Retroviral-Gag-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000390564
http://togogenome.org/gene/9606:CLGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKG2|||http://purl.uniprot.org/uniprot/O14967                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||2-4|||Acidic residues|||Basic and acidic residues|||Calmegin|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Interaction with PPIB|||Lumenal|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004210|||http://purl.uniprot.org/annotation/PRO_5007356952|||http://purl.uniprot.org/annotation/VAR_024400|||http://purl.uniprot.org/annotation/VAR_033776|||http://purl.uniprot.org/annotation/VAR_048590|||http://purl.uniprot.org/annotation/VSP_055517|||http://purl.uniprot.org/annotation/VSP_055518
http://togogenome.org/gene/9606:KPNA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60684                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Disordered|||IBB|||Importin subunit alpha-7|||N-acetylmethionine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120729
http://togogenome.org/gene/9606:SNX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJM0|||http://purl.uniprot.org/uniprot/Q8N5Z3|||http://purl.uniprot.org/uniprot/Q9Y5X0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes vacuolization induced by overexpression.|||Basic and acidic residues|||Disordered|||In OPTB8.|||In OPTB8; increased expression, produces extensive cytoplasmic vacuolation and impairs bone resorptive function.|||In isoform 2.|||PX|||Polar residues|||Reduced vacuolization induced by overexpression.|||Required for interaction with ATP6V1D|||Slightly reduced vacuolization induced by overexpression.|||Sorting nexin-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213854|||http://purl.uniprot.org/annotation/VAR_046098|||http://purl.uniprot.org/annotation/VAR_069299|||http://purl.uniprot.org/annotation/VAR_069300|||http://purl.uniprot.org/annotation/VAR_069301|||http://purl.uniprot.org/annotation/VAR_069302|||http://purl.uniprot.org/annotation/VSP_045920
http://togogenome.org/gene/9606:PRAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2F6|||http://purl.uniprot.org/uniprot/D3DTV9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Putative protein PRAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000430950
http://togogenome.org/gene/9606:MMP13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45452|||http://purl.uniprot.org/uniprot/Q53H33                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Activation peptide|||Collagenase 3|||Cysteine switch|||Disordered|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In MANDP1.|||In MDST.|||In SEMDM; abnormal intracellular autoactivation and autodegradation within the ER/Golgi resulting in the secretion of small and inactive fragments.|||Interaction with TIMP2|||Interaction with collagen|||N-linked (GlcNAc...) asparagine|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028788|||http://purl.uniprot.org/annotation/PRO_0000028789|||http://purl.uniprot.org/annotation/PRO_5004248824|||http://purl.uniprot.org/annotation/VAR_011971|||http://purl.uniprot.org/annotation/VAR_020534|||http://purl.uniprot.org/annotation/VAR_032753|||http://purl.uniprot.org/annotation/VAR_063432|||http://purl.uniprot.org/annotation/VAR_063433|||http://purl.uniprot.org/annotation/VAR_063434|||http://purl.uniprot.org/annotation/VAR_073418
http://togogenome.org/gene/9606:AKAP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Z7|||http://purl.uniprot.org/uniprot/E7EMD6|||http://purl.uniprot.org/uniprot/O43572                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  A-kinase anchor protein 10, mitochondrial|||Associated with increased basal heart rate and decreased heart rate variability.|||Basic and acidic residues|||Disordered|||Mitochondrion|||PKA-RII subunit binding|||Phosphoserine|||RGS|||RGS 1|||RGS 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030404|||http://purl.uniprot.org/annotation/VAR_024607|||http://purl.uniprot.org/annotation/VAR_024608
http://togogenome.org/gene/9606:SUV39H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43463                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes methylation of histone H3.|||Abolishes methyltransferase activity.|||Chromo|||Histone-lysine N-methyltransferase SUV39H1|||In isoform 2.|||Interaction with SIRT1|||Loss of SIRT1-mediated up-regulation of enzymatic activity.|||Mediates interaction with MECOM|||N6-acetyllysine|||Phosphoserine|||Post-SET|||Pre-SET|||SET|||Significant loss of enzymatic activity.|||Strongly increases methylation of histone H3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186057|||http://purl.uniprot.org/annotation/VSP_054286
http://togogenome.org/gene/9606:ZBTB45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K62                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Pro residues|||Zinc finger and BTB domain-containing protein 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047619|||http://purl.uniprot.org/annotation/VAR_052924
http://togogenome.org/gene/9606:GTDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4AE62                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycosyltransferase-like domain-containing protein 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311088|||http://purl.uniprot.org/annotation/VAR_037136|||http://purl.uniprot.org/annotation/VSP_029378|||http://purl.uniprot.org/annotation/VSP_029379|||http://purl.uniprot.org/annotation/VSP_057596|||http://purl.uniprot.org/annotation/VSP_057597|||http://purl.uniprot.org/annotation/VSP_057598|||http://purl.uniprot.org/annotation/VSP_057599
http://togogenome.org/gene/9606:SPECC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DW07|||http://purl.uniprot.org/uniprot/B4E2A4|||http://purl.uniprot.org/uniprot/Q5M775                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Cytospin-B|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254033|||http://purl.uniprot.org/annotation/VAR_028800|||http://purl.uniprot.org/annotation/VAR_053055|||http://purl.uniprot.org/annotation/VAR_053056|||http://purl.uniprot.org/annotation/VSP_021162|||http://purl.uniprot.org/annotation/VSP_021163|||http://purl.uniprot.org/annotation/VSP_021164|||http://purl.uniprot.org/annotation/VSP_021165
http://togogenome.org/gene/9606:PGGHG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R1Z9|||http://purl.uniprot.org/uniprot/Q32M88                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Disordered|||Glycoside hydrolase family 65 central catalytic|||In isoform 2.|||Polar residues|||Protein-glucosylgalactosylhydroxylysine glucosidase|||Proton donor|||Significantly impairs catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329004|||http://purl.uniprot.org/annotation/VSP_032895|||http://purl.uniprot.org/annotation/VSP_032896
http://togogenome.org/gene/9606:CCDC187                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP49                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 187|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000435396|||http://purl.uniprot.org/annotation/VSP_058066
http://togogenome.org/gene/9606:TBL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12788                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Removed|||Transducin beta-like protein 3|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051272|||http://purl.uniprot.org/annotation/VAR_014479|||http://purl.uniprot.org/annotation/VAR_054320|||http://purl.uniprot.org/annotation/VAR_054321
http://togogenome.org/gene/9606:REC114                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YKR2|||http://purl.uniprot.org/uniprot/Q7Z4M0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In OZEMA10; unknown pathological significance; decreases protein level; does not affect interaction with MEI4 and IHO1; decreases MEI4 stability.|||Meiotic recombination protein REC114|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321518|||http://purl.uniprot.org/annotation/VAR_050893|||http://purl.uniprot.org/annotation/VAR_085251
http://togogenome.org/gene/9606:B3GNT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7M8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Loss of enzymatic activity, no loss of B3GNT2-binding and activation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306381|||http://purl.uniprot.org/annotation/VAR_049348
http://togogenome.org/gene/9606:KRTAP5-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q701N4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184100
http://togogenome.org/gene/9606:FER1L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2WGJ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||Cytoplasmic|||Disordered|||Extracellular|||Fer-1-like protein 6|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323674|||http://purl.uniprot.org/annotation/VAR_039558
http://togogenome.org/gene/9606:CRYZL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95825                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Quinone oxidoreductase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160913|||http://purl.uniprot.org/annotation/VAR_027835|||http://purl.uniprot.org/annotation/VSP_055792|||http://purl.uniprot.org/annotation/VSP_055793
http://togogenome.org/gene/9606:NPHS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP85                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant|||Topological Domain                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||In NPHS2.|||In NPHS2; requires 2 nucleotide substitutions.|||In NPHS2; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Podocin|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094035|||http://purl.uniprot.org/annotation/VAR_010231|||http://purl.uniprot.org/annotation/VAR_010232|||http://purl.uniprot.org/annotation/VAR_010233|||http://purl.uniprot.org/annotation/VAR_010234|||http://purl.uniprot.org/annotation/VAR_010235|||http://purl.uniprot.org/annotation/VAR_010236|||http://purl.uniprot.org/annotation/VAR_071212|||http://purl.uniprot.org/annotation/VAR_071213|||http://purl.uniprot.org/annotation/VAR_071214|||http://purl.uniprot.org/annotation/VAR_071215|||http://purl.uniprot.org/annotation/VAR_071216|||http://purl.uniprot.org/annotation/VAR_071217|||http://purl.uniprot.org/annotation/VAR_071218|||http://purl.uniprot.org/annotation/VAR_071219|||http://purl.uniprot.org/annotation/VAR_071220|||http://purl.uniprot.org/annotation/VAR_071221|||http://purl.uniprot.org/annotation/VAR_071222|||http://purl.uniprot.org/annotation/VAR_071223|||http://purl.uniprot.org/annotation/VAR_071224|||http://purl.uniprot.org/annotation/VAR_071225|||http://purl.uniprot.org/annotation/VAR_071226|||http://purl.uniprot.org/annotation/VAR_071227|||http://purl.uniprot.org/annotation/VAR_071228|||http://purl.uniprot.org/annotation/VAR_071229|||http://purl.uniprot.org/annotation/VAR_071230|||http://purl.uniprot.org/annotation/VAR_071231|||http://purl.uniprot.org/annotation/VAR_071232|||http://purl.uniprot.org/annotation/VAR_071233|||http://purl.uniprot.org/annotation/VAR_071234|||http://purl.uniprot.org/annotation/VAR_071235|||http://purl.uniprot.org/annotation/VAR_071236|||http://purl.uniprot.org/annotation/VAR_071237|||http://purl.uniprot.org/annotation/VAR_071238|||http://purl.uniprot.org/annotation/VAR_071239|||http://purl.uniprot.org/annotation/VAR_071240|||http://purl.uniprot.org/annotation/VAR_071241|||http://purl.uniprot.org/annotation/VAR_071242|||http://purl.uniprot.org/annotation/VAR_071243|||http://purl.uniprot.org/annotation/VAR_072134|||http://purl.uniprot.org/annotation/VAR_072135|||http://purl.uniprot.org/annotation/VAR_072136|||http://purl.uniprot.org/annotation/VAR_072137|||http://purl.uniprot.org/annotation/VAR_072138|||http://purl.uniprot.org/annotation/VAR_072139|||http://purl.uniprot.org/annotation/VAR_072140|||http://purl.uniprot.org/annotation/VAR_072141|||http://purl.uniprot.org/annotation/VAR_072142|||http://purl.uniprot.org/annotation/VAR_072143|||http://purl.uniprot.org/annotation/VAR_072144|||http://purl.uniprot.org/annotation/VAR_072145|||http://purl.uniprot.org/annotation/VAR_072146|||http://purl.uniprot.org/annotation/VAR_072147|||http://purl.uniprot.org/annotation/VAR_072148|||http://purl.uniprot.org/annotation/VAR_072149|||http://purl.uniprot.org/annotation/VAR_072150|||http://purl.uniprot.org/annotation/VAR_072151|||http://purl.uniprot.org/annotation/VAR_072152|||http://purl.uniprot.org/annotation/VAR_072153|||http://purl.uniprot.org/annotation/VAR_072154|||http://purl.uniprot.org/annotation/VAR_072155|||http://purl.uniprot.org/annotation/VAR_072156|||http://purl.uniprot.org/annotation/VAR_072157|||http://purl.uniprot.org/annotation/VAR_072158|||http://purl.uniprot.org/annotation/VAR_072159|||http://purl.uniprot.org/annotation/VAR_072160|||http://purl.uniprot.org/annotation/VAR_075617|||http://purl.uniprot.org/annotation/VAR_075618|||http://purl.uniprot.org/annotation/VAR_079808|||http://purl.uniprot.org/annotation/VAR_079809|||http://purl.uniprot.org/annotation/VAR_079810|||http://purl.uniprot.org/annotation/VAR_079811|||http://purl.uniprot.org/annotation/VAR_087597|||http://purl.uniprot.org/annotation/VAR_087598|||http://purl.uniprot.org/annotation/VAR_087599|||http://purl.uniprot.org/annotation/VSP_000499
http://togogenome.org/gene/9606:REXO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ95|||http://purl.uniprot.org/uniprot/B4E331|||http://purl.uniprot.org/uniprot/Q9GZR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Exonuclease|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||RNA exonuclease 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131703|||http://purl.uniprot.org/annotation/VAR_023067|||http://purl.uniprot.org/annotation/VAR_023068|||http://purl.uniprot.org/annotation/VSP_014796|||http://purl.uniprot.org/annotation/VSP_014797
http://togogenome.org/gene/9606:NUP107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57740                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Disordered|||In GAMOS7; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased protein amount detected by Western blot in patient cells; affects exon 4 splicing resulting in decreased levels of wild-type mature transcript; impairs assembly of nuclear pore complex.|||In GAMOS7; unknown pathological significance.|||In NPHS11; decreased function in nephrogenesis; unable to fully rescue morpholino-induced nephrogenesis defects in Xenopus; decreased interaction with NUP133.|||In NPHS11; decreased interaction with NUP133; changed localization to the nuclear pore with relocalization to the cytoplasm.|||In NPHS11; no effect on interaction with NUP133; no effect on localization to the nuclear pore.|||In NPHS11; unknown pathological significance.|||In ODG6.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Nuclear pore complex protein Nup107|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204831|||http://purl.uniprot.org/annotation/VAR_076358|||http://purl.uniprot.org/annotation/VAR_076359|||http://purl.uniprot.org/annotation/VAR_078571|||http://purl.uniprot.org/annotation/VAR_081356|||http://purl.uniprot.org/annotation/VAR_081357|||http://purl.uniprot.org/annotation/VAR_081358|||http://purl.uniprot.org/annotation/VAR_082054|||http://purl.uniprot.org/annotation/VSP_054262|||http://purl.uniprot.org/annotation/VSP_054263|||http://purl.uniprot.org/annotation/VSP_054264
http://togogenome.org/gene/9606:KRTAP1-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYS1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  15 X 5 AA repeats of C-C-[QEPVRC]-[TPIVLE]-[SRHVP]|||Keratin-associated protein 1-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185161
http://togogenome.org/gene/9606:JCHAIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01591                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Immunoglobulin J chain|||Interchain (with heavy chain)|||N-linked (GlcNAc...) (complex) asparagine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000167|||http://purl.uniprot.org/annotation/PRO_0000084174
http://togogenome.org/gene/9606:SRARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEQ6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Steroid receptor-associated and regulated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247124|||http://purl.uniprot.org/annotation/VAR_033654|||http://purl.uniprot.org/annotation/VAR_035491|||http://purl.uniprot.org/annotation/VAR_035492
http://togogenome.org/gene/9606:DCTPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H773                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Loss of dCTP diphosphatase activity.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||dCTP pyrophosphatase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291769
http://togogenome.org/gene/9606:CRCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75575                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase III subunit RPC9|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079335|||http://purl.uniprot.org/annotation/VSP_007538|||http://purl.uniprot.org/annotation/VSP_043249|||http://purl.uniprot.org/annotation/VSP_046273
http://togogenome.org/gene/9606:AKAP8L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  A-kinase anchor protein 8-like|||Acidic residues|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||C2H2 AKAP95-type 1|||C2H2 AKAP95-type 2|||Disordered|||In isoform 2.|||N6-acetyllysine|||Nuclear export signal (NES)|||Nuclear localization signal|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Pro residues|||Sufficient for activation of CTE-mediated expression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075384|||http://purl.uniprot.org/annotation/VAR_068822|||http://purl.uniprot.org/annotation/VSP_044426
http://togogenome.org/gene/9606:SERHL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK89|||http://purl.uniprot.org/uniprot/Q9H4I8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AB hydrolase-1|||In isoform 2.|||In isoform 3.|||Serine hydrolase-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097692|||http://purl.uniprot.org/annotation/VAR_021962|||http://purl.uniprot.org/annotation/VAR_051334|||http://purl.uniprot.org/annotation/VAR_051335|||http://purl.uniprot.org/annotation/VSP_003968|||http://purl.uniprot.org/annotation/VSP_003969|||http://purl.uniprot.org/annotation/VSP_003970
http://togogenome.org/gene/9606:PCMTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z927|||http://purl.uniprot.org/uniprot/Q96MG8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AdoMet binding motif|||BC-box|||Basic and acidic residues|||CUL-box|||Disordered|||In isoform 2.|||N-myristoyl glycine|||Protein-L-isoaspartate O-methyltransferase domain-containing protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111925|||http://purl.uniprot.org/annotation/VAR_060401|||http://purl.uniprot.org/annotation/VSP_061574
http://togogenome.org/gene/9606:ZNF284                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VY69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 284                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280403|||http://purl.uniprot.org/annotation/VAR_031135|||http://purl.uniprot.org/annotation/VAR_059909
http://togogenome.org/gene/9606:GPR83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYM4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 83|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012803|||http://purl.uniprot.org/annotation/VAR_047079|||http://purl.uniprot.org/annotation/VSP_061501
http://togogenome.org/gene/9606:TAS2R19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59542                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082328|||http://purl.uniprot.org/annotation/VAR_053354|||http://purl.uniprot.org/annotation/VAR_053355
http://togogenome.org/gene/9606:CTNNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K141|||http://purl.uniprot.org/uniprot/Q8WW10|||http://purl.uniprot.org/uniprot/Q9UI47                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Catenin alpha-3|||Disordered|||In ARVD13.|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064266|||http://purl.uniprot.org/annotation/VAR_053369|||http://purl.uniprot.org/annotation/VAR_062093|||http://purl.uniprot.org/annotation/VAR_070998|||http://purl.uniprot.org/annotation/VSP_051852|||http://purl.uniprot.org/annotation/VSP_051853
http://togogenome.org/gene/9606:CDC42SE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Lipid Binding|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-62.|||Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-66.|||Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-38.|||Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-41.|||Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-38 and A-41.|||CDC42 small effector protein 1|||CRIB|||Disordered|||In isoform 2.|||Mediates phosphoinositide-binding|||Prevents targeting to the activated TCR.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334629|||http://purl.uniprot.org/annotation/VSP_033717
http://togogenome.org/gene/9606:DNM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50570|||http://purl.uniprot.org/uniprot/Q8N1K8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Dynamin-2|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In CMT2M.|||In CMTDIB.|||In CMTDIB; may affect binding to vesicles and membranes in favor of binding to microtubules; may affect receptor-mediated endocytosis.|||In CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex.|||In CNM1.|||In CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex.|||In CNM1; centronuclear myopathy with cataracts.|||In CNM1; reduced association with the centrosome.|||In CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex.|||In CNM1; severe.|||In CNM1; severe; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex.|||In LCCS5; hypomorphic mutation impacting on endocytosis.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||N6-acetyllysine|||PH|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206570|||http://purl.uniprot.org/annotation/VAR_031961|||http://purl.uniprot.org/annotation/VAR_031962|||http://purl.uniprot.org/annotation/VAR_031963|||http://purl.uniprot.org/annotation/VAR_031964|||http://purl.uniprot.org/annotation/VAR_031965|||http://purl.uniprot.org/annotation/VAR_031966|||http://purl.uniprot.org/annotation/VAR_031967|||http://purl.uniprot.org/annotation/VAR_039041|||http://purl.uniprot.org/annotation/VAR_039042|||http://purl.uniprot.org/annotation/VAR_039043|||http://purl.uniprot.org/annotation/VAR_039044|||http://purl.uniprot.org/annotation/VAR_062574|||http://purl.uniprot.org/annotation/VAR_062575|||http://purl.uniprot.org/annotation/VAR_062576|||http://purl.uniprot.org/annotation/VAR_068365|||http://purl.uniprot.org/annotation/VAR_068366|||http://purl.uniprot.org/annotation/VAR_068367|||http://purl.uniprot.org/annotation/VAR_068368|||http://purl.uniprot.org/annotation/VAR_068369|||http://purl.uniprot.org/annotation/VAR_068370|||http://purl.uniprot.org/annotation/VAR_068371|||http://purl.uniprot.org/annotation/VAR_068372|||http://purl.uniprot.org/annotation/VAR_068373|||http://purl.uniprot.org/annotation/VAR_068425|||http://purl.uniprot.org/annotation/VAR_070163|||http://purl.uniprot.org/annotation/VAR_070164|||http://purl.uniprot.org/annotation/VSP_001325|||http://purl.uniprot.org/annotation/VSP_044280|||http://purl.uniprot.org/annotation/VSP_047534
http://togogenome.org/gene/9606:LYPLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1K9|||http://purl.uniprot.org/uniprot/B4DP64|||http://purl.uniprot.org/uniprot/O75608|||http://purl.uniprot.org/uniprot/Q6IAQ1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-protein thioesterase 1|||Charge relay system|||In isoform 2.|||Loss of thioesterase and lysophospholipase activity.|||N6-acetyllysine|||Phospholipase/carboxylesterase/thioesterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102267|||http://purl.uniprot.org/annotation/VAR_060991|||http://purl.uniprot.org/annotation/VSP_009196
http://togogenome.org/gene/9606:RNF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased E3 ubiquitin-protein ligase activity without affecting binding to UBE2D2.|||Decreased E3 ubiquitin-protein ligase activity, increased binding to UBE2D2.|||Decreased binding to UBE2D2.|||Disordered|||E3 ubiquitin-protein ligase RNF25|||Phosphoserine|||Polar residues|||RING-type|||RWD|||Reduced activation of NF-kappa-B.|||Strongly reduced E3 ubiquitin-protein ligase activity, slightly reduced binding to UBE2D2.|||Strongly reduced activation of NF-kappa-B.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056066
http://togogenome.org/gene/9606:RCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3I4|||http://purl.uniprot.org/uniprot/A0A0S2Z404|||http://purl.uniprot.org/uniprot/P18754|||http://purl.uniprot.org/uniprot/Q5T081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes N-terminal methylation.|||Abolishes interaction with Ran and impairs chromosome localization.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Decreases KPNA4 binding. Strongly decreases KPNA4 binding; when associated with A-21.|||Decreases KPNA4 binding. Strongly decreases KPNA4 binding; when associated with A-9.|||Disordered|||Does not abolish N-terminal methylation.|||In isoform 2.|||N,N,N-trimethylserine; alternate|||N,N-dimethylserine; alternate|||N-methylserine; alternate|||Phosphomimetic mutant. Decreases KPNA4 binding by about 10%.|||Phosphoserine|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||Regulator of chromosome condensation|||Removed|||Strongly impairs N-terminal methylation and subcellular localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206628|||http://purl.uniprot.org/annotation/VSP_041122
http://togogenome.org/gene/9606:ANKRD13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6S4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 13C|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240645|||http://purl.uniprot.org/annotation/VAR_026825|||http://purl.uniprot.org/annotation/VSP_019406|||http://purl.uniprot.org/annotation/VSP_019407|||http://purl.uniprot.org/annotation/VSP_019408
http://togogenome.org/gene/9606:BTN2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVV5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin subfamily 2 member A2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014530|||http://purl.uniprot.org/annotation/VAR_049829|||http://purl.uniprot.org/annotation/VSP_012712|||http://purl.uniprot.org/annotation/VSP_012713|||http://purl.uniprot.org/annotation/VSP_043561|||http://purl.uniprot.org/annotation/VSP_043562|||http://purl.uniprot.org/annotation/VSP_043563|||http://purl.uniprot.org/annotation/VSP_043564|||http://purl.uniprot.org/annotation/VSP_044861
http://togogenome.org/gene/9606:SMARCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GM5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CSS11.|||In CSS11; does not affect the interaction with SMARCC1 and SMARCA4.|||In CSS11; unknown pathological significance; does not affect the interaction with SMARCC1 and SMARCA4.|||In isoform 2.|||Interaction with ESR1, NR1H4, NR3C1, PGR and SMARCA4|||Interaction with SMARCC1 and SMARCC2|||N6-acetyllysine|||Necessary for GR/NR3C1-mediated remodeling and transcription from chromatin; required for GR/NR3C1 interaction with the BRG1/SMARCA4 complex in vivo|||Phosphothreonine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1|||SWIB/MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071983|||http://purl.uniprot.org/annotation/VAR_083801|||http://purl.uniprot.org/annotation/VAR_083802|||http://purl.uniprot.org/annotation/VAR_083803|||http://purl.uniprot.org/annotation/VAR_083804|||http://purl.uniprot.org/annotation/VAR_083805|||http://purl.uniprot.org/annotation/VSP_004179
http://togogenome.org/gene/9606:SIRT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRC8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes deacylase and deacetylase activities and activation of pre-rRNA synthesis. Abolished histone desuccinylase activity; when associated with A-111.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Catalytically inactive mutant; abolishes activation of pre-rRNA synthesis. Abolishes deacetylation of DDB1. Abolished histone desuccinylase activity; when associated with Y-187.|||Deacetylase sirtuin-type|||Decreased methylation; does not affect histone deacetylase activity.|||Disordered|||In isoform 2.|||In isoform 3.|||Mimics methylation status; impaired histone deacetylase activity.|||NAD-dependent protein deacetylase sirtuin-7|||Omega-N-methylarginine; alternate|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110271|||http://purl.uniprot.org/annotation/VSP_008736|||http://purl.uniprot.org/annotation/VSP_008737|||http://purl.uniprot.org/annotation/VSP_044396|||http://purl.uniprot.org/annotation/VSP_044397
http://togogenome.org/gene/9606:MTMR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13614                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GRAM|||In CMT4B1.|||In isoform 2.|||Loss of activity.|||Loss of homodimerization and interaction with SBF1.|||Myotubularin phosphatase|||Myotubularin-related protein 2|||No effect.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Reduces homodimerization and interaction with SBF1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094934|||http://purl.uniprot.org/annotation/VAR_047255|||http://purl.uniprot.org/annotation/VAR_047256|||http://purl.uniprot.org/annotation/VAR_047947|||http://purl.uniprot.org/annotation/VSP_044933
http://togogenome.org/gene/9606:TMEM219                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XT9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Insulin-like growth factor-binding protein 3 receptor|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329049
http://togogenome.org/gene/9606:ACTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68133                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Actin, alpha skeletal muscle|||Actin, alpha skeletal muscle, intermediate form|||In CMYP2A.|||In CMYP2A; formation of rod-like structure.|||In CMYP2A; found in a patient with a rare combination of CMYP2A and dilated cardiomyopathy.|||In CMYP2A; no effect on actin structure; higher sensitivity to calcium.|||In CMYP2A; requires 2 nucleotide substitutions.|||In CMYP2A; results in sequestration of sarcomeric and Z line proteins into intranuclear aggregates; there is some evidence of muscle regeneration suggesting a compensatory effect.|||In CMYP2A; some patients have core lesions on muscle biopsy.|||In CMYP2B.|||In CMYP2C.|||In CMYP2C; results in decreased motility due to abnormal interactions between actin and tropomyosin with tropomyosin stabilized in the 'off' position; the mutant protein incorporates into actin filaments and does not result in increased actin aggregation or disruption of the sarcomere.|||In SHPM; no effect on cytoskeleton structure.|||Interaction with alpha-actinin|||Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1|||Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N6-malonyllysine|||N6-methyllysine|||Removed|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000442803|||http://purl.uniprot.org/annotation/PRO_0000442804|||http://purl.uniprot.org/annotation/VAR_011680|||http://purl.uniprot.org/annotation/VAR_011681|||http://purl.uniprot.org/annotation/VAR_011682|||http://purl.uniprot.org/annotation/VAR_011683|||http://purl.uniprot.org/annotation/VAR_011684|||http://purl.uniprot.org/annotation/VAR_011685|||http://purl.uniprot.org/annotation/VAR_011686|||http://purl.uniprot.org/annotation/VAR_011687|||http://purl.uniprot.org/annotation/VAR_013470|||http://purl.uniprot.org/annotation/VAR_013471|||http://purl.uniprot.org/annotation/VAR_015579|||http://purl.uniprot.org/annotation/VAR_015580|||http://purl.uniprot.org/annotation/VAR_015581|||http://purl.uniprot.org/annotation/VAR_015582|||http://purl.uniprot.org/annotation/VAR_015583|||http://purl.uniprot.org/annotation/VAR_015584|||http://purl.uniprot.org/annotation/VAR_015585|||http://purl.uniprot.org/annotation/VAR_015586|||http://purl.uniprot.org/annotation/VAR_015587|||http://purl.uniprot.org/annotation/VAR_032917|||http://purl.uniprot.org/annotation/VAR_032918|||http://purl.uniprot.org/annotation/VAR_032919|||http://purl.uniprot.org/annotation/VAR_062424|||http://purl.uniprot.org/annotation/VAR_062425|||http://purl.uniprot.org/annotation/VAR_062426|||http://purl.uniprot.org/annotation/VAR_062427|||http://purl.uniprot.org/annotation/VAR_062428|||http://purl.uniprot.org/annotation/VAR_062429|||http://purl.uniprot.org/annotation/VAR_062430|||http://purl.uniprot.org/annotation/VAR_062431|||http://purl.uniprot.org/annotation/VAR_062432|||http://purl.uniprot.org/annotation/VAR_062433|||http://purl.uniprot.org/annotation/VAR_062434|||http://purl.uniprot.org/annotation/VAR_062435|||http://purl.uniprot.org/annotation/VAR_062436|||http://purl.uniprot.org/annotation/VAR_062437|||http://purl.uniprot.org/annotation/VAR_062438|||http://purl.uniprot.org/annotation/VAR_062439|||http://purl.uniprot.org/annotation/VAR_062440|||http://purl.uniprot.org/annotation/VAR_062441|||http://purl.uniprot.org/annotation/VAR_062442|||http://purl.uniprot.org/annotation/VAR_062443|||http://purl.uniprot.org/annotation/VAR_062444|||http://purl.uniprot.org/annotation/VAR_062445|||http://purl.uniprot.org/annotation/VAR_062446|||http://purl.uniprot.org/annotation/VAR_062447|||http://purl.uniprot.org/annotation/VAR_062448|||http://purl.uniprot.org/annotation/VAR_062449|||http://purl.uniprot.org/annotation/VAR_062450|||http://purl.uniprot.org/annotation/VAR_062451|||http://purl.uniprot.org/annotation/VAR_062452|||http://purl.uniprot.org/annotation/VAR_062453|||http://purl.uniprot.org/annotation/VAR_062454|||http://purl.uniprot.org/annotation/VAR_062455|||http://purl.uniprot.org/annotation/VAR_062456|||http://purl.uniprot.org/annotation/VAR_062457|||http://purl.uniprot.org/annotation/VAR_062458|||http://purl.uniprot.org/annotation/VAR_062459|||http://purl.uniprot.org/annotation/VAR_062460|||http://purl.uniprot.org/annotation/VAR_062461|||http://purl.uniprot.org/annotation/VAR_062462|||http://purl.uniprot.org/annotation/VAR_062463|||http://purl.uniprot.org/annotation/VAR_062464|||http://purl.uniprot.org/annotation/VAR_062465|||http://purl.uniprot.org/annotation/VAR_062466|||http://purl.uniprot.org/annotation/VAR_062467|||http://purl.uniprot.org/annotation/VAR_062468|||http://purl.uniprot.org/annotation/VAR_062469|||http://purl.uniprot.org/annotation/VAR_062470|||http://purl.uniprot.org/annotation/VAR_062471|||http://purl.uniprot.org/annotation/VAR_062472|||http://purl.uniprot.org/annotation/VAR_062473|||http://purl.uniprot.org/annotation/VAR_062474|||http://purl.uniprot.org/annotation/VAR_062475|||http://purl.uniprot.org/annotation/VAR_062476|||http://purl.uniprot.org/annotation/VAR_062477|||http://purl.uniprot.org/annotation/VAR_062478|||http://purl.uniprot.org/annotation/VAR_062479|||http://purl.uniprot.org/annotation/VAR_076426|||http://purl.uniprot.org/annotation/VAR_076427|||http://purl.uniprot.org/annotation/VAR_076428|||http://purl.uniprot.org/annotation/VAR_083589|||http://purl.uniprot.org/annotation/VAR_083590|||http://purl.uniprot.org/annotation/VAR_085717
http://togogenome.org/gene/9606:VANGL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4L6|||http://purl.uniprot.org/uniprot/Q9ULK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In NTD.|||In NTD; the mutant protein has diminished interaction with DVL1 compared to wild-type.|||In NTD; the mutation protein completely abrogates interaction with DVL1 compared to wild-type.|||Polar residues|||Vang-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186195|||http://purl.uniprot.org/annotation/VAR_067221|||http://purl.uniprot.org/annotation/VAR_067222|||http://purl.uniprot.org/annotation/VAR_067223
http://togogenome.org/gene/9606:FERMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AC8|||http://purl.uniprot.org/uniprot/Q54A15|||http://purl.uniprot.org/uniprot/Q9BQL6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FERM|||Fermitin family homolog 1|||In KNDLRS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219452|||http://purl.uniprot.org/annotation/VAR_014398|||http://purl.uniprot.org/annotation/VAR_014399|||http://purl.uniprot.org/annotation/VAR_048368|||http://purl.uniprot.org/annotation/VAR_061035|||http://purl.uniprot.org/annotation/VAR_066942|||http://purl.uniprot.org/annotation/VAR_066943|||http://purl.uniprot.org/annotation/VAR_066944|||http://purl.uniprot.org/annotation/VAR_066945|||http://purl.uniprot.org/annotation/VSP_003809|||http://purl.uniprot.org/annotation/VSP_003810|||http://purl.uniprot.org/annotation/VSP_003811|||http://purl.uniprot.org/annotation/VSP_009224|||http://purl.uniprot.org/annotation/VSP_009225
http://togogenome.org/gene/9606:CDCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8Z0|||http://purl.uniprot.org/uniprot/B7Z5Q5|||http://purl.uniprot.org/uniprot/E9PEI0|||http://purl.uniprot.org/uniprot/Q69YH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with PPP1CC but not subcellular location.|||Basic and acidic residues|||Basic residues|||Cell division cycle-associated protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PP1-binding|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287695|||http://purl.uniprot.org/annotation/VAR_032350|||http://purl.uniprot.org/annotation/VAR_032351|||http://purl.uniprot.org/annotation/VSP_025598|||http://purl.uniprot.org/annotation/VSP_025599
http://togogenome.org/gene/9606:H4C13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:TBX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8P2|||http://purl.uniprot.org/uniprot/Q96SF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphothreonine|||Polar residues|||T-box|||T-box transcription factor TBX15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184444|||http://purl.uniprot.org/annotation/VAR_055341|||http://purl.uniprot.org/annotation/VSP_040036
http://togogenome.org/gene/9606:FOXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58012|||http://purl.uniprot.org/uniprot/Q53ZD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein L2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In BPES.|||In BPES; diffuse nuclear localization as wild type; normal transactivation activity.|||In BPES; diffuse nuclear localization; increased transactivation activity.|||In BPES; diffuse nuclear localization; normal transcriptional activation.|||In BPES; nuclear aggregation and cytoplasmic mislocalization; impaired transactivation activity.|||In BPES; nuclear aggregation; impaired transactivation activity.|||In BPES; nuclear and cytoplasmic aggregation; impaired transactivation activity.|||In BPES; nuclear and cytoplasmic aggregation; normal transactivation activity.|||In BPES; significant higher cytoplasmic retention compared to the wild-type protein.|||In BPES; sporadic.|||In BPES; sporadic; nuclear aggregation; normal transactivation activity.|||In BPES; sporadic; nuclear and cytoplasmic aggregation; impaired transactivation activity.|||In BPES; type I.|||In BPES; type II.|||In BPES; type II; diffuse nuclear localization as wild type; impaired transactivation activity.|||In POF3.|||In POF3; does not affect nuclear localization; reduces transcriptional activation of OSR2.|||In granulosa-cell tumors of the ovary; not commonly found in other tumor types.|||Phosphoserine|||Pro residues|||Results in reduced sumoylation. Loss of transcriptional repression activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091861|||http://purl.uniprot.org/annotation/VAR_010782|||http://purl.uniprot.org/annotation/VAR_015181|||http://purl.uniprot.org/annotation/VAR_015182|||http://purl.uniprot.org/annotation/VAR_016883|||http://purl.uniprot.org/annotation/VAR_016884|||http://purl.uniprot.org/annotation/VAR_016885|||http://purl.uniprot.org/annotation/VAR_016886|||http://purl.uniprot.org/annotation/VAR_016887|||http://purl.uniprot.org/annotation/VAR_021196|||http://purl.uniprot.org/annotation/VAR_021197|||http://purl.uniprot.org/annotation/VAR_021198|||http://purl.uniprot.org/annotation/VAR_021199|||http://purl.uniprot.org/annotation/VAR_021200|||http://purl.uniprot.org/annotation/VAR_021201|||http://purl.uniprot.org/annotation/VAR_021202|||http://purl.uniprot.org/annotation/VAR_021203|||http://purl.uniprot.org/annotation/VAR_021204|||http://purl.uniprot.org/annotation/VAR_025306|||http://purl.uniprot.org/annotation/VAR_037303|||http://purl.uniprot.org/annotation/VAR_046490|||http://purl.uniprot.org/annotation/VAR_046491|||http://purl.uniprot.org/annotation/VAR_046492|||http://purl.uniprot.org/annotation/VAR_046493|||http://purl.uniprot.org/annotation/VAR_046494|||http://purl.uniprot.org/annotation/VAR_046495|||http://purl.uniprot.org/annotation/VAR_046496|||http://purl.uniprot.org/annotation/VAR_046497|||http://purl.uniprot.org/annotation/VAR_046498|||http://purl.uniprot.org/annotation/VAR_062545|||http://purl.uniprot.org/annotation/VAR_062546|||http://purl.uniprot.org/annotation/VAR_062547|||http://purl.uniprot.org/annotation/VAR_062548|||http://purl.uniprot.org/annotation/VAR_062549|||http://purl.uniprot.org/annotation/VAR_078138
http://togogenome.org/gene/9606:DAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51398                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein mS29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087717|||http://purl.uniprot.org/annotation/VAR_061811|||http://purl.uniprot.org/annotation/VSP_042790|||http://purl.uniprot.org/annotation/VSP_044639
http://togogenome.org/gene/9606:PLA2G2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14555                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Catalytically inactive but does not affect integrin binding. Impairs leukotriene B4 synthesis in activated neutrophils.|||Complete loss of bactericidal activity; when associated with E-27 and E-30.|||Complete loss of bactericidal activity; when associated with E-27 and E-35.|||Impairs bactericidal activity; when associated with D-138.|||Impairs bactericidal activity; when associated with E-122.|||Impairs bactericidal activity; when associated with E-127.|||Impairs bactericidal activity; when associated with E-128.|||Impairs bactericidal activity; when associated with E-135.|||Impairs bactericidal activity; when associated with E-57.|||Impairs bactericidal activity; when associated with E-72 and E-73.|||Impairs bactericidal activity; when associated with E-72 and E-77.|||Impairs bactericidal activity; when associated with E-73 and E-77.|||Important for integrin binding|||Moderately reduced integrin binding. Greatly reduced integrin binding but no effect on catalytic activity; when associated with E-120.|||Moderately reduced integrin binding. Greatly reduced integrin binding but no effect on catalytic activity; when associated with E-94.|||No effect on integrin binding.|||No effect on integrin binding; when associated with K-68.|||No effect on integrin binding; when associated with S-49.|||Phospholipase A2, membrane associated|||Reduces bactericidal activity to 18% against B.subtilis and to 12% against S.aureus. Complete loss of bactericidal activity; when associated with E-87 and E-99.|||Reduces bactericidal activity to 20% against B.subtilis and to 10% against S.aureus. Complete loss of bactericidal activity; when associated with E-99 and E-104.|||Reduces bactericidal activity to 20% against B.subtilis and to 4% against S.aureus. Complete loss of bactericidal activity; when associated with E-30 and E-35.|||Reduces bactericidal activity to 25% against B.subtilis and to 10% against S.aureus. Complete loss of bactericidal activity; when associated with E-87 and E-104.|||Slightly reduced integrin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022750|||http://purl.uniprot.org/annotation/VAR_018953
http://togogenome.org/gene/9606:TAGLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI15                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Calponin-homology (CH)|||Calponin-like|||Disordered|||Phosphoserine|||Transgelin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204788
http://togogenome.org/gene/9606:KRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12035                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In MECD2.|||Keratin, type II cytoskeletal 3|||Linker 1|||Linker 12|||N6,N6-dimethyllysine|||Phosphoserine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063716|||http://purl.uniprot.org/annotation/VAR_003868|||http://purl.uniprot.org/annotation/VAR_031327|||http://purl.uniprot.org/annotation/VAR_056023|||http://purl.uniprot.org/annotation/VAR_061297
http://togogenome.org/gene/9606:RB1CC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDY2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FFAT|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RB1-inducible coiled-coil protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097183|||http://purl.uniprot.org/annotation/VAR_023776|||http://purl.uniprot.org/annotation/VAR_033031|||http://purl.uniprot.org/annotation/VAR_051309|||http://purl.uniprot.org/annotation/VAR_051310|||http://purl.uniprot.org/annotation/VAR_051311|||http://purl.uniprot.org/annotation/VAR_051312|||http://purl.uniprot.org/annotation/VSP_040097
http://togogenome.org/gene/9606:MPHOSPH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99549                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Abolishes interaction with histone H3K9me3 and prevents recruitment of the HUSH complex to heterochromatin. Impaired ability to mediate silencing of unintegrated retroviral DNA.|||Basic and acidic residues|||Chromo|||Disordered|||Histone H3K9me3 binding|||In STA mutant; fails to dissociate from chromatin during early mitosis; when associated with A-149; A-164 and A-385.|||In STA mutant; fails to dissociate from chromatin during early mitosis; when associated with A-149; A-164; and A-334.|||In STA mutant; fails to dissociate from chromatin during early mitosis; when associated with A-149; A-334 and A-385.|||In STA mutant; fails to dissociate from chromatin during early mitosis; when associated with A-164; A-334 and A-385.|||In isoform 2.|||Interaction with histone H3K9me3|||Interaction with humanin|||M-phase phosphoprotein 8|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Phosphothreonine; by CDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080244|||http://purl.uniprot.org/annotation/VSP_031523
http://togogenome.org/gene/9606:GGT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKN3|||http://purl.uniprot.org/uniprot/J3KPJ0|||http://purl.uniprot.org/uniprot/Q6P531|||http://purl.uniprot.org/uniprot/Q6ZPD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Glutathione hydrolase 6 heavy chain|||Glutathione hydrolase 6 light chain|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314954|||http://purl.uniprot.org/annotation/PRO_0000314955|||http://purl.uniprot.org/annotation/VAR_038138|||http://purl.uniprot.org/annotation/VAR_038139|||http://purl.uniprot.org/annotation/VSP_030451
http://togogenome.org/gene/9606:AP3S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59780                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP-3 complex subunit sigma-2|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193817|||http://purl.uniprot.org/annotation/VSP_053673|||http://purl.uniprot.org/annotation/VSP_053674
http://togogenome.org/gene/9606:EPB41L4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8X1|||http://purl.uniprot.org/uniprot/Q8NEH8|||http://purl.uniprot.org/uniprot/Q9HCS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Band 4.1-like protein 4A|||Basic and acidic residues|||Disordered|||FERM|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219401|||http://purl.uniprot.org/annotation/VAR_055537
http://togogenome.org/gene/9606:KDM5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITA8|||http://purl.uniprot.org/uniprot/Q9UGL1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARID|||Abolishes interaction with histone H3. Decreases by 28% demethylase activity and repression of tumor suppressor genes expression.|||Abolishes interaction with histone H3. Decreases by 44% demethylase activity and repression of tumor suppressor genes expression; when associated with A-328.|||Abolishes lysine-specific histone demethylase activity.|||Almost abolishes interaction with histone H3. Decreases by 44% demethylase activity and repression of tumor suppressor genes expression; when associated with A-325.|||C5HC2|||Decreases interaction with histone H3.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs transcription repression ability and interaction with HDAC4.|||In MRT65.|||In isoform 2.|||JmjC|||JmjN|||Lysine-specific demethylase 5B|||N6-acetyllysine|||No effect on interaction with histone H3.|||PHD-type|||PHD-type 1|||PHD-type 2|||PHD-type 3|||Phosphoserine|||Polar residues|||Slightly decreases interaction with histone H3.|||Slightly decreases interaction with histone H3. Decreases by 21% demethylase activity and repression of tumor suppressor genes expression.|||Slightly impairs transcription repression ability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292412|||http://purl.uniprot.org/annotation/VAR_081276|||http://purl.uniprot.org/annotation/VAR_081277|||http://purl.uniprot.org/annotation/VSP_026408
http://togogenome.org/gene/9606:CYP4A22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZX9|||http://purl.uniprot.org/uniprot/A5PKT5|||http://purl.uniprot.org/uniprot/A5PL05|||http://purl.uniprot.org/uniprot/Q5TCH4|||http://purl.uniprot.org/uniprot/Q5TCH5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||Cytochrome P450 4A22|||Disordered|||Helical|||In allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||In allele CYP4A22*2 and CYP4A22*3.|||In allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||In allele CYP4A22*4, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||In allele CYP4A22*6, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13 and allele CYP4A22*15.|||In allele CYP4A22*7, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||In allele CYP4A22*8, allele CYP4A22*11, allele CYP4A22*14 and allele CYP4A22*15.|||In allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15.|||In isoform 2.|||Phosphoserine|||Polar residues|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343408|||http://purl.uniprot.org/annotation/PRO_0000343409|||http://purl.uniprot.org/annotation/VAR_044349|||http://purl.uniprot.org/annotation/VAR_044350|||http://purl.uniprot.org/annotation/VAR_044351|||http://purl.uniprot.org/annotation/VAR_044352|||http://purl.uniprot.org/annotation/VAR_044353|||http://purl.uniprot.org/annotation/VAR_044354|||http://purl.uniprot.org/annotation/VAR_044355|||http://purl.uniprot.org/annotation/VAR_044356|||http://purl.uniprot.org/annotation/VAR_044357|||http://purl.uniprot.org/annotation/VAR_044358|||http://purl.uniprot.org/annotation/VAR_044359|||http://purl.uniprot.org/annotation/VAR_044360|||http://purl.uniprot.org/annotation/VAR_044361|||http://purl.uniprot.org/annotation/VAR_061045|||http://purl.uniprot.org/annotation/VSP_034584
http://togogenome.org/gene/9606:PDE1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX78|||http://purl.uniprot.org/uniprot/B4DK72|||http://purl.uniprot.org/uniprot/Q01064|||http://purl.uniprot.org/uniprot/Q7Z364                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B|||In isoform PDE1B2.|||PDEase|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198789|||http://purl.uniprot.org/annotation/VSP_038643|||http://purl.uniprot.org/annotation/VSP_038644
http://togogenome.org/gene/9606:PAQR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXK6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Membrane progestin receptor gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218843|||http://purl.uniprot.org/annotation/VAR_031436
http://togogenome.org/gene/9606:KLHL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6TDP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||Interaction with F-actin|||Interaction with PDZK1|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 17|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119119
http://togogenome.org/gene/9606:PSORS1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X9A6|||http://purl.uniprot.org/uniprot/Q9UIG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Pro residues|||Psoriasis susceptibility 1 candidate gene 2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022159|||http://purl.uniprot.org/annotation/PRO_5010708192|||http://purl.uniprot.org/annotation/VAR_017395|||http://purl.uniprot.org/annotation/VAR_017396|||http://purl.uniprot.org/annotation/VAR_063104
http://togogenome.org/gene/9606:DLX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60479                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DLX-3|||Interaction with DNA|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049026
http://togogenome.org/gene/9606:YWHAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31946|||http://purl.uniprot.org/uniprot/V9HWD6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  14-3-3|||14-3-3 protein beta/alpha|||14-3-3 protein beta/alpha, N-terminally processed|||3'-nitrotyrosine|||Found in a renal cell carcinoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform Short.|||Interaction with phosphoserine on interacting protein|||N-acetylmethionine|||N-acetylmethionine; in 14-3-3 protein beta/alpha; alternate|||N-acetylthreonine; in 14-3-3 protein beta/alpha, N-terminally processed|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000003|||http://purl.uniprot.org/annotation/PRO_0000367900|||http://purl.uniprot.org/annotation/VAR_064762|||http://purl.uniprot.org/annotation/VSP_018632
http://togogenome.org/gene/9606:BLMH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13867                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bleomycin hydrolase|||N-acetylmethionine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050550|||http://purl.uniprot.org/annotation/VAR_010896
http://togogenome.org/gene/9606:HAUS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CS2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Splice Variant                                                                                  ^@                                                                                  HAUS augmin-like complex subunit 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089395|||http://purl.uniprot.org/annotation/VSP_010781
http://togogenome.org/gene/9606:POU2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YLL6|||http://purl.uniprot.org/uniprot/P09086                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||POU domain, class 2, transcription factor 2|||POU-specific|||Polar residues|||Pro residues|||Suppresses DNA-binding ability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100714|||http://purl.uniprot.org/annotation/VSP_002324|||http://purl.uniprot.org/annotation/VSP_002325|||http://purl.uniprot.org/annotation/VSP_007848|||http://purl.uniprot.org/annotation/VSP_007849|||http://purl.uniprot.org/annotation/VSP_032187
http://togogenome.org/gene/9606:PBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5V0|||http://purl.uniprot.org/uniprot/P40424|||http://purl.uniprot.org/uniprot/Q53YC7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form TCF3-PBX1 oncogene|||Disordered|||Homeobox|||Homeobox; TALE-type|||In CAKUTHED; unknown pathological significance.|||In isoform 3.|||In isoform PBX1b.|||PBC|||PBC-A|||PBC-B|||Polar residues|||Pre-B-cell leukemia transcription factor 1|||Required for binding to the NFIL3 promoter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049235|||http://purl.uniprot.org/annotation/VAR_068904|||http://purl.uniprot.org/annotation/VAR_079369|||http://purl.uniprot.org/annotation/VSP_002271|||http://purl.uniprot.org/annotation/VSP_002272|||http://purl.uniprot.org/annotation/VSP_044499
http://togogenome.org/gene/9606:MGRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60291                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase MGRN1|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Loss of TSG101-binding and drastic reduction of TSG101-ubiquitination.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RING-type|||Removed|||Required for TSG101-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246687|||http://purl.uniprot.org/annotation/VSP_019853|||http://purl.uniprot.org/annotation/VSP_036462
http://togogenome.org/gene/9606:TTLL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14166                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases expression of IFNB1 mRNA following infection with Sendai virus.|||Disordered|||TTL|||Tubulin--tyrosine ligase-like protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212446|||http://purl.uniprot.org/annotation/VAR_052413|||http://purl.uniprot.org/annotation/VAR_052414|||http://purl.uniprot.org/annotation/VAR_052415|||http://purl.uniprot.org/annotation/VAR_052416
http://togogenome.org/gene/9606:EPPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58107                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||Epiplakin|||Interaction with KRT14|||Interaction with KRT5|||Phosphoserine|||Phosphothreonine|||Plectin 1|||Plectin 10|||Plectin 11|||Plectin 12|||Plectin 13|||Plectin 14|||Plectin 15|||Plectin 16|||Plectin 17|||Plectin 18|||Plectin 19|||Plectin 2|||Plectin 20|||Plectin 21|||Plectin 22|||Plectin 23|||Plectin 24|||Plectin 25|||Plectin 26|||Plectin 27|||Plectin 28|||Plectin 29|||Plectin 3|||Plectin 30|||Plectin 31|||Plectin 32|||Plectin 33|||Plectin 34|||Plectin 35|||Plectin 36|||Plectin 37|||Plectin 38|||Plectin 39|||Plectin 4|||Plectin 40|||Plectin 41|||Plectin 42|||Plectin 43|||Plectin 44|||Plectin 45|||Plectin 46|||Plectin 47|||Plectin 48|||Plectin 49|||Plectin 5|||Plectin 50|||Plectin 51|||Plectin 52|||Plectin 53|||Plectin 54|||Plectin 55|||Plectin 56|||Plectin 57|||Plectin 58|||Plectin 59|||Plectin 6|||Plectin 60|||Plectin 61|||Plectin 62|||Plectin 63|||Plectin 64|||Plectin 65|||Plectin 7|||Plectin 8|||Plectin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078145|||http://purl.uniprot.org/annotation/VAR_081533
http://togogenome.org/gene/9606:TSPAN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41732                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In XLID58.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219248|||http://purl.uniprot.org/annotation/VAR_009259|||http://purl.uniprot.org/annotation/VAR_037905|||http://purl.uniprot.org/annotation/VAR_037906
http://togogenome.org/gene/9606:UGT1A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19224|||http://purl.uniprot.org/uniprot/Q5DSZ8|||http://purl.uniprot.org/uniprot/Q5DT01                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In allele UGT1A6*2 and allele UGT1A6*4.|||In allele UGT1A6*2, allele UGT1A6*3 and allele UGT1A6*4.|||In allele UGT1A6*2.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036005|||http://purl.uniprot.org/annotation/PRO_5009998740|||http://purl.uniprot.org/annotation/VAR_014784|||http://purl.uniprot.org/annotation/VAR_015559|||http://purl.uniprot.org/annotation/VAR_024685|||http://purl.uniprot.org/annotation/VAR_026628|||http://purl.uniprot.org/annotation/VAR_026629|||http://purl.uniprot.org/annotation/VSP_045779|||http://purl.uniprot.org/annotation/VSP_053962
http://togogenome.org/gene/9606:F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13726                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Tissue factor|||WKS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033638|||http://purl.uniprot.org/annotation/VAR_012008|||http://purl.uniprot.org/annotation/VAR_014298|||http://purl.uniprot.org/annotation/VAR_014299|||http://purl.uniprot.org/annotation/VAR_052280|||http://purl.uniprot.org/annotation/VSP_041896|||http://purl.uniprot.org/annotation/VSP_041897
http://togogenome.org/gene/9606:SHISAL2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKW6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein shisa-like-2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317723|||http://purl.uniprot.org/annotation/VAR_053995|||http://purl.uniprot.org/annotation/VAR_053996
http://togogenome.org/gene/9606:CD163L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 10|||SRCR 11|||SRCR 12|||SRCR 2|||SRCR 3|||SRCR 4|||SRCR 5|||SRCR 6|||SRCR 7|||SRCR 8|||SRCR 9|||Scavenger receptor cysteine-rich type 1 protein M160                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045392|||http://purl.uniprot.org/annotation/VAR_057206|||http://purl.uniprot.org/annotation/VAR_057207|||http://purl.uniprot.org/annotation/VAR_057208|||http://purl.uniprot.org/annotation/VAR_057209|||http://purl.uniprot.org/annotation/VAR_059810|||http://purl.uniprot.org/annotation/VSP_016875|||http://purl.uniprot.org/annotation/VSP_016876|||http://purl.uniprot.org/annotation/VSP_016877|||http://purl.uniprot.org/annotation/VSP_047557
http://togogenome.org/gene/9606:TEX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z669|||http://purl.uniprot.org/uniprot/Q8N6V9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Testis-expressed protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244481|||http://purl.uniprot.org/annotation/VSP_055381
http://togogenome.org/gene/9606:COPS7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1P5|||http://purl.uniprot.org/uniprot/J3KQ34|||http://purl.uniprot.org/uniprot/J3KQ41|||http://purl.uniprot.org/uniprot/Q6ZTQ7|||http://purl.uniprot.org/uniprot/Q9H9Q2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||COP9 signalosome complex subunit 7b|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||PCI|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120999|||http://purl.uniprot.org/annotation/VSP_011913|||http://purl.uniprot.org/annotation/VSP_040266
http://togogenome.org/gene/9606:GPR132                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNW8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased IP1 accumulation at any pH.|||Decreased basal activity at alkaline pH and loss of proton-sensing activity at low pH.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No change in basal activity.|||Probable G-protein coupled receptor 132                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069461|||http://purl.uniprot.org/annotation/VSP_008404|||http://purl.uniprot.org/annotation/VSP_054592
http://togogenome.org/gene/9606:RBM42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTD8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Necessary for interaction with HNRNPK|||Phosphoserine|||Pro residues|||RNA-binding protein 42|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307750|||http://purl.uniprot.org/annotation/VSP_028817|||http://purl.uniprot.org/annotation/VSP_028818|||http://purl.uniprot.org/annotation/VSP_037256
http://togogenome.org/gene/9606:COMMD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4G1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 6|||Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-24.|||Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-41.|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077398|||http://purl.uniprot.org/annotation/VAR_048813|||http://purl.uniprot.org/annotation/VSP_026593
http://togogenome.org/gene/9606:ANAPC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMX6|||http://purl.uniprot.org/uniprot/Q69YV3                                                                                  ^@                                                                                  Compositionally Biased Region|||Experimental Information|||Non-terminal Residue|||Region|||Repeat                                                                                  ^@                                                                                  Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||TPR                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:SLC25A34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIV7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291789
http://togogenome.org/gene/9606:INIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRY2|||http://purl.uniprot.org/uniprot/X6R8P6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SOSS complex subunit C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279419|||http://purl.uniprot.org/annotation/VSP_023423|||http://purl.uniprot.org/annotation/VSP_023424
http://togogenome.org/gene/9606:MFAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55001                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform A'.|||In isoform B.|||Microfibrillar-associated protein 2|||Or 19|||Polar residues|||Pyrrolidone carboxylic acid|||ShKT|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018682|||http://purl.uniprot.org/annotation/VSP_042779|||http://purl.uniprot.org/annotation/VSP_042780
http://togogenome.org/gene/9606:PRRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8D6|||http://purl.uniprot.org/uniprot/Q99946                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Pro residues|||Proline-rich transmembrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135697|||http://purl.uniprot.org/annotation/VAR_036212|||http://purl.uniprot.org/annotation/VSP_003808
http://togogenome.org/gene/9606:SDSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GA7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  Loss of enzyme activity.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Serine dehydratase-like|||Strongly increased enzyme activity towards threonine.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264624
http://togogenome.org/gene/9606:ZNF559-ZNF177                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13360                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 177                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047441|||http://purl.uniprot.org/annotation/VAR_031692|||http://purl.uniprot.org/annotation/VAR_031693|||http://purl.uniprot.org/annotation/VAR_057401|||http://purl.uniprot.org/annotation/VSP_044461|||http://purl.uniprot.org/annotation/VSP_045841|||http://purl.uniprot.org/annotation/VSP_045842
http://togogenome.org/gene/9606:FFAR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0PUW7|||http://purl.uniprot.org/uniprot/O14843                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes activation by propionate.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Free fatty acid receptor 3|||G-protein coupled receptors family 1 profile|||Gain of SCFA-independent constitutive G protein-coupled receptor activity.|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of SCFA-induced G protein-coupled receptor activity.|||N-linked (GlcNAc...) asparagine|||Partial loss of SCFA-induced G protein-coupled receptor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069569|||http://purl.uniprot.org/annotation/VAR_062854|||http://purl.uniprot.org/annotation/VAR_062855|||http://purl.uniprot.org/annotation/VAR_062856|||http://purl.uniprot.org/annotation/VAR_062857|||http://purl.uniprot.org/annotation/VAR_062858|||http://purl.uniprot.org/annotation/VAR_062962
http://togogenome.org/gene/9606:CEP44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0F1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Binds with microtubules and centrioles|||Centrosomal protein of 44 kDa|||Disordered|||In isoform 2.|||Loss of binding to microtubules and location to centrioles.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293722|||http://purl.uniprot.org/annotation/VAR_033116|||http://purl.uniprot.org/annotation/VSP_041378
http://togogenome.org/gene/9606:TMEM161B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6T3|||http://purl.uniprot.org/uniprot/B7Z6X1|||http://purl.uniprot.org/uniprot/E9PCX5|||http://purl.uniprot.org/uniprot/Q8NDZ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Integrase catalytic|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 161B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288089|||http://purl.uniprot.org/annotation/VSP_025647|||http://purl.uniprot.org/annotation/VSP_025648|||http://purl.uniprot.org/annotation/VSP_025649|||http://purl.uniprot.org/annotation/VSP_025650
http://togogenome.org/gene/9606:DYDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IM9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  DPY30 domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247559|||http://purl.uniprot.org/annotation/VAR_048889
http://togogenome.org/gene/9606:PBK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KB5|||http://purl.uniprot.org/uniprot/V9HWH0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decrease in the binding to DLG1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Loss of activity.|||Lymphokine-activated killer T-cell-originated protein kinase|||N-acetylmethionine|||PDZ-interaction|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||TP53-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086763|||http://purl.uniprot.org/annotation/VAR_021162|||http://purl.uniprot.org/annotation/VAR_041234|||http://purl.uniprot.org/annotation/VAR_051676|||http://purl.uniprot.org/annotation/VSP_055269
http://togogenome.org/gene/9606:LRRC58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 58|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312017
http://togogenome.org/gene/9606:FOXM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SFF0|||http://purl.uniprot.org/uniprot/A0A2P9DTZ1|||http://purl.uniprot.org/uniprot/A0A2P9DTZ8|||http://purl.uniprot.org/uniprot/A8K591|||http://purl.uniprot.org/uniprot/Q08050|||http://purl.uniprot.org/uniprot/Q53Y49                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein M1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CHEK2|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues|||Prevents phosphorylation by CDK1 and subsequent binding of POLO box domains of PLK1; when associated with A-611.|||Prevents phosphorylation by CDK1 and subsequent binding of POLO box domains of PLK1; when associated with A-693.|||Prevents phosphorylation by PLK1 and impairs transcription activity; when associated with A-730.|||Prevents phosphorylation by PLK1 and impairs transcription activity; when associated with A-739.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091863|||http://purl.uniprot.org/annotation/VAR_020024|||http://purl.uniprot.org/annotation/VAR_025239|||http://purl.uniprot.org/annotation/VAR_025240|||http://purl.uniprot.org/annotation/VAR_025241|||http://purl.uniprot.org/annotation/VAR_025242|||http://purl.uniprot.org/annotation/VSP_001547|||http://purl.uniprot.org/annotation/VSP_001548
http://togogenome.org/gene/9606:GOT1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHS2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N6-(pyridoxal phosphate)lysine|||Putative aspartate aminotransferase, cytoplasmic 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332999
http://togogenome.org/gene/9606:KRTAP12-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60328                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 5 AA approximate repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 12-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185198|||http://purl.uniprot.org/annotation/VAR_017592
http://togogenome.org/gene/9606:PSMD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15008                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PCI|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173838|||http://purl.uniprot.org/annotation/VSP_047711|||http://purl.uniprot.org/annotation/VSP_055177|||http://purl.uniprot.org/annotation/VSP_055178
http://togogenome.org/gene/9606:NKAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5F7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRXSHD.|||In MRXSHD; unknown pathological significance.|||N6-acetyllysine|||NF-kappa-B-activating protein|||Necessary for interaction with CIR1|||Necessary for interaction with HDAC3 and transcriptional repression|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259645|||http://purl.uniprot.org/annotation/VAR_053799|||http://purl.uniprot.org/annotation/VAR_083895|||http://purl.uniprot.org/annotation/VAR_083896|||http://purl.uniprot.org/annotation/VAR_083897|||http://purl.uniprot.org/annotation/VAR_083898|||http://purl.uniprot.org/annotation/VAR_083899
http://togogenome.org/gene/9606:PPIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62937|||http://purl.uniprot.org/uniprot/V9HWF5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  200-fold decrease of sensitivity to CsA. Reduced ability to stimulate MAPK/ERK phosphorylation.|||75-fold decrease of sensitivity to CsA.|||Acetylation-mimetic mutant; no effect on its interaction with TARDBP.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||Loss of ability to stimulate MAPK/ERK phosphorylation.|||Loss of acetylation and interaction with TARDBP.|||Loss of peptidyl-prolyl cis-trans isomerase activity and interaction with HCVNS5A. Loss of ability to stimulate MAPK/ERK phosphorylation.|||Loss of peptidyl-prolyl cis-trans isomerase activity.|||Loss of peptidyl-prolyl cis-trans isomerase activity. No loss of its interaction with BSG/CD147 or its ability to induce leukocyte chemotaxis. No effect on its interaction with MAP3K5/ASK1. Loss of its ability to negatively regulate oxidative stress-induced apoptosis mediated by MAP3K5/ASK1. Reduced interaction with TARDBP. No loss of interaction with influenza A virus matrix protein 1 or its ability to inhibit viral replication.|||N-acetylmethionine|||N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on peptidyl-prolyl cis-trans isomerase activity.|||No effect on peptidyl-prolyl cis-trans isomerase activity. Reduced interaction with BSG/CD147 and ability to induce leukocyte chemotaxis.|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A|||Peptidyl-prolyl cis-trans isomerase A, N-terminally processed|||Phosphoserine|||Phosphothreonine|||Reduced ability to stimulate MAPK/ERK phosphorylation.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064115|||http://purl.uniprot.org/annotation/PRO_0000423240|||http://purl.uniprot.org/annotation/VSP_056050
http://togogenome.org/gene/9606:MS4A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXJ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Membrane-spanning 4-domains subfamily A member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158648|||http://purl.uniprot.org/annotation/VAR_057653|||http://purl.uniprot.org/annotation/VSP_044899
http://togogenome.org/gene/9606:ZNF589                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||KRAB|||Phosphoserine|||Zinc finger protein 589                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306325|||http://purl.uniprot.org/annotation/VAR_035290|||http://purl.uniprot.org/annotation/VAR_052871|||http://purl.uniprot.org/annotation/VSP_028449|||http://purl.uniprot.org/annotation/VSP_028450|||http://purl.uniprot.org/annotation/VSP_028451
http://togogenome.org/gene/9606:BSND                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU50|||http://purl.uniprot.org/uniprot/Q8WZ55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  38% reduction in palmitoylation. Abolishes palmitoylation; when associated with S-56.|||74% reduction in palmitoylation. Abolishes palmitoylation; when associated with S-54.|||Barttin|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In BARTS4A; atypical.|||In BARTS4A; completely abolishes CLCNKA activation.|||In BARTS4A; completely abolishes CLCNKA activation; mutated protein fails to increase surface expression of CLCNKA; intracellular localization; probably retained in the ER.|||In BARTS4A; increases CLCNKA currents over those obtained with wild-type; still activates CLCNKA to an extent similar to that of wild-type; intracellular but some plasma membrane localization as well.|||Phosphoserine|||S-palmitoyl cysteine|||Stimulation of CLCNKA and CLCNKB currents enhanced; intense localization in the plasma membrane with no intracellular localization observed.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064999|||http://purl.uniprot.org/annotation/VAR_019783|||http://purl.uniprot.org/annotation/VAR_019784|||http://purl.uniprot.org/annotation/VAR_019785|||http://purl.uniprot.org/annotation/VAR_019786|||http://purl.uniprot.org/annotation/VAR_061564
http://togogenome.org/gene/9606:TNFRSF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92956                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cis interactions with BTLA.|||Cytoplasmic|||Does not affect cis interactions with BTLA.|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034590|||http://purl.uniprot.org/annotation/VAR_013007|||http://purl.uniprot.org/annotation/VAR_013440|||http://purl.uniprot.org/annotation/VAR_018955|||http://purl.uniprot.org/annotation/VAR_018956|||http://purl.uniprot.org/annotation/VSP_054186
http://togogenome.org/gene/9606:UGT2B28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY64                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 2B28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036046|||http://purl.uniprot.org/annotation/VAR_059847|||http://purl.uniprot.org/annotation/VAR_060661|||http://purl.uniprot.org/annotation/VAR_060662|||http://purl.uniprot.org/annotation/VSP_006710|||http://purl.uniprot.org/annotation/VSP_006711
http://togogenome.org/gene/9606:CTRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GPI1                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Chymotrypsin B2 chain A|||Chymotrypsin B2 chain B|||Chymotrypsin B2 chain C|||Chymotrypsinogen B2|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285870|||http://purl.uniprot.org/annotation/PRO_0000285871|||http://purl.uniprot.org/annotation/PRO_0000285872|||http://purl.uniprot.org/annotation/PRO_0000285873|||http://purl.uniprot.org/annotation/VAR_062766
http://togogenome.org/gene/9606:ARID3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 3B|||Acidic residues|||Asymmetric dimethylarginine|||Disordered|||Impairs binding to RB1.|||In isoform 3.|||In isoform 4.|||Interaction with ARID3A|||Interaction with RB1|||N-acetylmethionine|||Phosphoserine|||Polar residues|||REKLES                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295162|||http://purl.uniprot.org/annotation/VSP_026773|||http://purl.uniprot.org/annotation/VSP_026774|||http://purl.uniprot.org/annotation/VSP_039860
http://togogenome.org/gene/9606:SLC29A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased adenosine transport at pH 5.5.|||Decreased adenosine transport at pH 5.5. Partial loss of acidic pH-dependent activity resulting in emergence of adenosine transport at pH 7.4. Decreased nucleoside transport at pH 5.5; when associated with A-219. Complete loss of acidic pH-dependent activity resulting in full nucleoside transport at pH 7.4 as observed at pH 5.5; when associated with A-219.|||Decreased adenosine transport at pH 5.5. Partial loss of acidic pH-dependent activity resulting in emergence of adenosine transport at pH 7.4. Decreased nucleoside transport at pH 5.5; when associated with A-447. Complete loss of acidic pH-dependent activity resulting in full nucleoside transport at pH 7.4 as observed at pH 5.5; when associated with A-447.|||Decreased adenosine transport at pH5.5.|||Dileucine internalization motif|||Disordered|||Equilibrative nucleoside transporter 3|||Extracellular|||Helical|||Important for acidic pH-dependent nucleoside transporter activity. Acts as pH sensor|||In HLAS.|||In HLAS; almost total loss of nucleoside transport.|||In HLAS; partially retained in the endoplasmic reticulum; results in reduced nucleoside transport.|||In HLAS; results in reduced nucleoside transport.|||In isoform 2.|||Localization at the cell surface; when associated with A-31.|||Localization at the cell surface; when associated with A-32.|||Loss of adenosine transport at pH 5.5.|||N-linked (GlcNAc...) asparagine|||No change in adenosine transport at pH 5.5.|||No change in adenosine transport at pH5.5.|||No change in adenosine transport.|||Partial loss of acidic pH-dependent activity resulting in moderate emergence of adenosine transport at pH 7.4. Partial loss of acidic pH-dependent activity resulting in moderate emergence of adenosine transport at pH 7.4; when associated with D-219.|||Phosphoserine|||Polar residues|||Results in impaired nucleoside transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209343|||http://purl.uniprot.org/annotation/VAR_018662|||http://purl.uniprot.org/annotation/VAR_018663|||http://purl.uniprot.org/annotation/VAR_018664|||http://purl.uniprot.org/annotation/VAR_018665|||http://purl.uniprot.org/annotation/VAR_018666|||http://purl.uniprot.org/annotation/VAR_057884|||http://purl.uniprot.org/annotation/VAR_057885|||http://purl.uniprot.org/annotation/VAR_067801|||http://purl.uniprot.org/annotation/VAR_067802|||http://purl.uniprot.org/annotation/VAR_067803|||http://purl.uniprot.org/annotation/VAR_067804|||http://purl.uniprot.org/annotation/VAR_067805|||http://purl.uniprot.org/annotation/VAR_067806|||http://purl.uniprot.org/annotation/VAR_067807|||http://purl.uniprot.org/annotation/VAR_067808|||http://purl.uniprot.org/annotation/VAR_067809|||http://purl.uniprot.org/annotation/VSP_037436
http://togogenome.org/gene/9606:CEP162                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TB80                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 162 kDa|||Disordered|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295628|||http://purl.uniprot.org/annotation/VAR_033301|||http://purl.uniprot.org/annotation/VAR_033302|||http://purl.uniprot.org/annotation/VAR_051293|||http://purl.uniprot.org/annotation/VAR_051294|||http://purl.uniprot.org/annotation/VSP_026953
http://togogenome.org/gene/9606:MSRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZV6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Non standard residue|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Non standard residue|||Strand|||Turn                                                                                  ^@                                                                                  Methionine-R-sulfoxide reductase B1|||MsrB|||Nucleophile|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140321
http://togogenome.org/gene/9606:HINT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPU2|||http://purl.uniprot.org/uniprot/P49773                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Adenosine 5'-monophosphoramidase HINT1|||Approximately 10-fold increased affinity for tryptamine adenosine phosphoramidate.|||Approximately 30-fold increased affinity for tryptamine adenosine phosphoramidate.|||Approximately 50-fold increased affinity for tryptamine adenosine phosphoramidate.|||HIT|||Histidine triad motif|||In NMAN; loss of homodimerization; significant decrease in adenosine 5'-monophosphoramidase activity; approximately 40-fold increased affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity.|||In NMAN; negligible protein expression due to post-translational degradation; loss of homodimerization; significant decrease in adenosine 5'-monophosphoramidase activity; reduced SUMO-specific isopeptidase activity.|||In NMAN; negligible protein expression due to post-translational degradation; no effect on homodimerization; no effect on adenosine 5'-monophosphoramidase; no effect on affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity.|||In NMAN; no effect on homodimerization; no effect on adenosine 5'-monophosphoramidase activity; no effect on affinity for tryptamine adenosine phosphoramidate; loss of SUMO-specific isopeptidase activity.|||In NMAN; no mutant protein is detected due to post-translational degradation; no effect on SUMO-specific isopeptidase activity.|||In NMAN; the enzyme has no residual activity although the mutant protein is expressed at normal levels; no effect on homodimerization; loss of SUMO-specific isopeptidase activity.|||Loss of SUMO-specific isopeptidase activity.|||Loss of dimerization. Strongly reduced adenosine 5'-monophosphoramidase activity. A 110-fold increased affinity for 3-indolepropionic acyl-adenylate and a 100-fold increased affinity for tryptamine adenosine phosphoramidate monoester.|||Loss of dimerization. Strongly reduced adenosine 5'-monophosphoramidase activity. A 128-fold increased affinity for 3-indolepropionic acyl-adenylate and a 1000-fold increased affinity for tryptamine adenosine phosphoramidate monoester.|||N-acetylalanine|||N6-acetyllysine|||Nearly abolishes adenosine 5'-monophosphoramidase activity.|||Nearly abolishes adenosine 5'-monophosphoramidase activity. A 3-fold increased affinity for 3-indolepropionic acyl-adenylate and a 2-fold increased affinity for tryptamine adenosine phosphoramidate monoester.|||No effect on SUMO-specific isopeptidase activity.|||No effect on affinity for 3-indolepropionic acyl-adenylate but a 13.8-fold increased affinity for tryptamine adenosine phosphoramidate monoester.|||No significant effect on affinity for 3-indolepropionic acyl-adenylate and tryptamine adenosine phosphoramidate monoester.|||Phosphoserine|||Reduced SUMO-specific isopeptidase activity.|||Reduces adenosine 5'-monophosphoramidase activity.|||Removed|||Tele-AMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109781|||http://purl.uniprot.org/annotation/VAR_069212|||http://purl.uniprot.org/annotation/VAR_069213|||http://purl.uniprot.org/annotation/VAR_069214|||http://purl.uniprot.org/annotation/VAR_069215|||http://purl.uniprot.org/annotation/VAR_069216|||http://purl.uniprot.org/annotation/VAR_069217
http://togogenome.org/gene/9606:TRAF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00463                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Interaction with EIF2AK2/PKR|||MATH|||RING-type|||TNF receptor-associated factor 5|||TRAF-type 1|||TRAF-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056405|||http://purl.uniprot.org/annotation/VAR_020117|||http://purl.uniprot.org/annotation/VAR_052151|||http://purl.uniprot.org/annotation/VAR_052152|||http://purl.uniprot.org/annotation/VAR_071060|||http://purl.uniprot.org/annotation/VSP_055449|||http://purl.uniprot.org/annotation/VSP_055450
http://togogenome.org/gene/9606:FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXL6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation.|||Abrogates kinase activity.|||Basic and acidic residues|||Cleavage; by MBTPS1|||Cytoplasmic|||Disordered|||Extracellular serine/threonine protein kinase FAM20C|||Helical; Signal-anchor for type II membrane protein|||Impaired secretion.|||Impaired secretion. Loss of ability to promote osteoblast differentiation; when associated with A-89.|||Impaired secretion. Loss of ability to promote osteoblast differentiation; when associated with A-92.|||Impaired secretion; when associated with A-101 and A-335.|||Impaired secretion; when associated with A-101 and A-470.|||Impaired secretion; when associated with A-335 and A-470.|||In RNS.|||In RNS; mild non-lethal form; decreased protein kinase activity.|||In RNS; mild non-lethal form; decreased protein kinase activity; FAM20A is still able to increase remaining protein kinase activity.|||In isoform 2.|||Interchain|||Kinase domain|||Loss of membrane localization with more efficient secretion and loss of propeptide cleavage. Reduced oligomerization.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on homodimer formation. Complete disruption of homodimer formation but no effect on secretion; when associated with S-46.|||No effect on homodimer formation. Complete disruption of homodimer formation but no effect on secretion; when associated with S-48.|||No effect on secretion or activity.|||No effect on secretion.|||Phosphoserine|||Reduced kinase activity.|||Strongly reduced kinase activity.|||Unable to bind manganese. Abrogates kinase activity. Loss of ERO1A phosphorylation. Loss of autophosphorylation. Loss of ability to promote osteoblast differentiation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008747|||http://purl.uniprot.org/annotation/PRO_0000433883|||http://purl.uniprot.org/annotation/VAR_037530|||http://purl.uniprot.org/annotation/VAR_037531|||http://purl.uniprot.org/annotation/VAR_037532|||http://purl.uniprot.org/annotation/VAR_037533|||http://purl.uniprot.org/annotation/VAR_073660|||http://purl.uniprot.org/annotation/VAR_073661|||http://purl.uniprot.org/annotation/VAR_073662|||http://purl.uniprot.org/annotation/VAR_073663|||http://purl.uniprot.org/annotation/VAR_073664|||http://purl.uniprot.org/annotation/VSP_040834
http://togogenome.org/gene/9606:EHBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK17|||http://purl.uniprot.org/uniprot/A8K930|||http://purl.uniprot.org/uniprot/Q8NDI1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BMERB|||Basic and acidic residues|||C2 NT-type|||CAAX motif|||Calponin-homology (CH)|||Disordered|||EH domain-binding protein 1|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285202|||http://purl.uniprot.org/annotation/VAR_031992|||http://purl.uniprot.org/annotation/VAR_035913|||http://purl.uniprot.org/annotation/VSP_024834|||http://purl.uniprot.org/annotation/VSP_024835
http://togogenome.org/gene/9606:IRF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2USB5|||http://purl.uniprot.org/uniprot/B7Z1M2|||http://purl.uniprot.org/uniprot/Q13568                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished nuclear translocation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||IRF tryptophan pentad repeat|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interferon regulatory factor 5|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by IKKB|||Phosphoserine; by TBK1|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154558|||http://purl.uniprot.org/annotation/VSP_041375|||http://purl.uniprot.org/annotation/VSP_043924|||http://purl.uniprot.org/annotation/VSP_043925|||http://purl.uniprot.org/annotation/VSP_044822|||http://purl.uniprot.org/annotation/VSP_053330|||http://purl.uniprot.org/annotation/VSP_053331
http://togogenome.org/gene/9606:DYNLRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFR2|||http://purl.uniprot.org/uniprot/Q9NP97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Dynein light chain roadblock-type 1|||In isoform 2.|||N-acetylalanine|||Polar residues|||Removed|||Roadblock/LAMTOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220955|||http://purl.uniprot.org/annotation/VAR_049124|||http://purl.uniprot.org/annotation/VAR_049125|||http://purl.uniprot.org/annotation/VSP_007236|||http://purl.uniprot.org/annotation/VSP_007237
http://togogenome.org/gene/9606:ZNF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR55|||http://purl.uniprot.org/uniprot/B4DLS2|||http://purl.uniprot.org/uniprot/P17027                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047351|||http://purl.uniprot.org/annotation/VAR_024195|||http://purl.uniprot.org/annotation/VSP_055936
http://togogenome.org/gene/9606:C1S                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WCZ6|||http://purl.uniprot.org/uniprot/P09871                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||CUB|||CUB 1|||CUB 2|||Charge relay system|||Complement C1s subcomponent|||Complement C1s subcomponent heavy chain|||Complement C1s subcomponent light chain|||EGF-like; calcium-binding|||In EDSPD2.|||In EDSPD2; unknown pathological significance.|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027586|||http://purl.uniprot.org/annotation/PRO_0000027587|||http://purl.uniprot.org/annotation/PRO_0000027588|||http://purl.uniprot.org/annotation/VAR_014565|||http://purl.uniprot.org/annotation/VAR_033643|||http://purl.uniprot.org/annotation/VAR_033644|||http://purl.uniprot.org/annotation/VAR_077120|||http://purl.uniprot.org/annotation/VAR_077121
http://togogenome.org/gene/9606:JMJD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9V9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  2-oxoglutarate and iron-dependent oxygenase JMJD4|||In isoform 2.|||JmjC|||Loss of interaction with ETF1 and its ability to hydroxylate ETF1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291959|||http://purl.uniprot.org/annotation/VAR_032898|||http://purl.uniprot.org/annotation/VAR_032899|||http://purl.uniprot.org/annotation/VAR_032900|||http://purl.uniprot.org/annotation/VAR_032901|||http://purl.uniprot.org/annotation/VSP_026324
http://togogenome.org/gene/9606:NRN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q496H8                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated alanine|||Neuritin-like protein|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319429|||http://purl.uniprot.org/annotation/PRO_0000319430
http://togogenome.org/gene/9606:KBTBD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCT8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch repeat and BTB domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324766|||http://purl.uniprot.org/annotation/VAR_050055|||http://purl.uniprot.org/annotation/VSP_032354|||http://purl.uniprot.org/annotation/VSP_032355
http://togogenome.org/gene/9606:MAPRE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15691                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Turn                                                                                  ^@                                                                                  APC-binding|||Abolished acetylation by KAT2B/PCAF, impairing kinetochore-microtubule interactions during mitosis.|||Abolished crotonylation by KAT5.|||Calponin-homology (CH)|||DCTN1-binding|||Disordered|||EB1 C-terminal|||Interaction with APC|||Interaction with CDK5RAP2|||Interaction with MTUS2/TIP150|||Loss of binding to microtubules.|||Microtubule-associated protein RP/EB family member 1|||N-acetylalanine|||N6-acetyllysine|||N6-crotonyllysine|||No effect.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213416
http://togogenome.org/gene/9606:LONRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1L5Z9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||LON peptidase N-terminal domain and RING finger protein 2|||Lon N-terminal|||Polar residues|||RING-type|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277670|||http://purl.uniprot.org/annotation/VAR_030590|||http://purl.uniprot.org/annotation/VAR_035953|||http://purl.uniprot.org/annotation/VAR_054639|||http://purl.uniprot.org/annotation/VSP_023079
http://togogenome.org/gene/9606:SPIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01892                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates DNA-binding.|||Disordered|||ETS|||In isoform 2.|||In isoform 3.|||No effect on transcriptional activation.|||Reduces interaction with IRF4 and transcriptional activation.|||TAD1 (Acidic)|||TAD2|||Transcription factor Spi-B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204136|||http://purl.uniprot.org/annotation/VAR_061150|||http://purl.uniprot.org/annotation/VSP_001479|||http://purl.uniprot.org/annotation/VSP_001480|||http://purl.uniprot.org/annotation/VSP_045124|||http://purl.uniprot.org/annotation/VSP_045125
http://togogenome.org/gene/9606:LKAAEAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD35                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Protein LKAAEAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329279|||http://purl.uniprot.org/annotation/VAR_042651|||http://purl.uniprot.org/annotation/VAR_077877|||http://purl.uniprot.org/annotation/VSP_032961
http://togogenome.org/gene/9606:PXK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG95|||http://purl.uniprot.org/uniprot/B4DID9|||http://purl.uniprot.org/uniprot/B4DJD8|||http://purl.uniprot.org/uniprot/B4DJS8|||http://purl.uniprot.org/uniprot/E9PD56|||http://purl.uniprot.org/uniprot/Q7Z7A4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||No effect on subcellular location.|||PX|||PX domain-containing protein kinase-like protein|||Polar residues|||Pro residues|||Protein kinase|||Results in redistribution of protein from cytoplasm throughout entire cell.|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086592|||http://purl.uniprot.org/annotation/VAR_033911|||http://purl.uniprot.org/annotation/VAR_033912|||http://purl.uniprot.org/annotation/VAR_041362|||http://purl.uniprot.org/annotation/VAR_041363|||http://purl.uniprot.org/annotation/VSP_051907|||http://purl.uniprot.org/annotation/VSP_051908|||http://purl.uniprot.org/annotation/VSP_051909|||http://purl.uniprot.org/annotation/VSP_051910|||http://purl.uniprot.org/annotation/VSP_051911|||http://purl.uniprot.org/annotation/VSP_051912|||http://purl.uniprot.org/annotation/VSP_051913
http://togogenome.org/gene/9606:SHH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15465                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Mass|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Mass|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes palmitoylation.|||Cardin-Weintraub|||Cholesterol glycine ester|||Cleavage; by autolysis|||Disordered|||Essential for auto-cleavage|||In HPE3 and SMMCI.|||In HPE3.|||In HPE3; familial.|||In HPE3; familial; in the mouse sequence shows no change in activities at different temperatures.|||In HPE3; familial; the same mutation in the mouse sequence moderately reduces Ptch1 binding in vitro and signaling potency in chicken embryo neural plate explant assays compared with wild-type sequence.|||In HPE3; sporadic.|||In HPE3; sporadic; in the mouse sequence does not affect signaling activity in any of Shh signaling assays and causes no apparent defects in cholesterol-mediated autoprocessing reactions.|||In HPE3; the same mutation in the mouse sequence causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells; causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius; drastically reduces signaling potency in chicken embryo neural plate explant assays.|||In HPE3; the same mutation in the mouse sequence causes a failure of Shh processing leading to retention of the immature glycosylated protein within the endoplasmic reticulum of transfected cells; causes a temperature-dependent conformational change that allows Shh to bind Ptch1 at 4 or 32 degrees Celsius but not at 37 degrees Celsius; the mutation drastically reduces signaling potency in chicken embryo neural plate explant assays.|||In HPE3; the same mutation in the mouse sequence introduces a cleavage site for a furin-like protease resulting in abnormal protein processing; cleavage at this site removes 11 amino acids from the N-terminal domain and reduces affinity of Shh for Ptch1 and signaling potency in assays using chicken embryo neural plate explants and mouse C3H10T1/2 stem cells.|||In HPE3; unknown pathological significance.|||In SMMCI.|||In ocular coloboma.|||Involved in auto-cleavage|||Involved in cholesterol transfer|||N-linked (GlcNAc...) asparagine|||N-palmitoyl cysteine|||Sonic hedgehog protein|||Sonic hedgehog protein N-product|||Sonic hedgehog protein N-product: Membrane-bound product, purified from insect cells.|||Sonic hedgehog protein N-product: soluble product, purified from insect cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013208|||http://purl.uniprot.org/annotation/PRO_0000013209|||http://purl.uniprot.org/annotation/VAR_003619|||http://purl.uniprot.org/annotation/VAR_003620|||http://purl.uniprot.org/annotation/VAR_003621|||http://purl.uniprot.org/annotation/VAR_009163|||http://purl.uniprot.org/annotation/VAR_009164|||http://purl.uniprot.org/annotation/VAR_009165|||http://purl.uniprot.org/annotation/VAR_009166|||http://purl.uniprot.org/annotation/VAR_009167|||http://purl.uniprot.org/annotation/VAR_009168|||http://purl.uniprot.org/annotation/VAR_009169|||http://purl.uniprot.org/annotation/VAR_009170|||http://purl.uniprot.org/annotation/VAR_009171|||http://purl.uniprot.org/annotation/VAR_009172|||http://purl.uniprot.org/annotation/VAR_009173|||http://purl.uniprot.org/annotation/VAR_009174|||http://purl.uniprot.org/annotation/VAR_009175|||http://purl.uniprot.org/annotation/VAR_009176|||http://purl.uniprot.org/annotation/VAR_009177|||http://purl.uniprot.org/annotation/VAR_017883|||http://purl.uniprot.org/annotation/VAR_017884|||http://purl.uniprot.org/annotation/VAR_023804|||http://purl.uniprot.org/annotation/VAR_023805|||http://purl.uniprot.org/annotation/VAR_023806|||http://purl.uniprot.org/annotation/VAR_023807|||http://purl.uniprot.org/annotation/VAR_023808|||http://purl.uniprot.org/annotation/VAR_023809|||http://purl.uniprot.org/annotation/VAR_023810|||http://purl.uniprot.org/annotation/VAR_023811|||http://purl.uniprot.org/annotation/VAR_023812|||http://purl.uniprot.org/annotation/VAR_023813|||http://purl.uniprot.org/annotation/VAR_039888|||http://purl.uniprot.org/annotation/VAR_039889|||http://purl.uniprot.org/annotation/VAR_039890|||http://purl.uniprot.org/annotation/VAR_039891|||http://purl.uniprot.org/annotation/VAR_039892|||http://purl.uniprot.org/annotation/VAR_039893|||http://purl.uniprot.org/annotation/VAR_039894|||http://purl.uniprot.org/annotation/VAR_062592|||http://purl.uniprot.org/annotation/VAR_062593|||http://purl.uniprot.org/annotation/VAR_062594|||http://purl.uniprot.org/annotation/VAR_062595|||http://purl.uniprot.org/annotation/VAR_062596|||http://purl.uniprot.org/annotation/VAR_062597|||http://purl.uniprot.org/annotation/VAR_062598|||http://purl.uniprot.org/annotation/VAR_062599|||http://purl.uniprot.org/annotation/VAR_062600|||http://purl.uniprot.org/annotation/VAR_062601|||http://purl.uniprot.org/annotation/VAR_062602|||http://purl.uniprot.org/annotation/VAR_062603|||http://purl.uniprot.org/annotation/VAR_062604|||http://purl.uniprot.org/annotation/VAR_062605|||http://purl.uniprot.org/annotation/VAR_062606|||http://purl.uniprot.org/annotation/VAR_062607|||http://purl.uniprot.org/annotation/VAR_062608|||http://purl.uniprot.org/annotation/VAR_062609|||http://purl.uniprot.org/annotation/VAR_062610|||http://purl.uniprot.org/annotation/VAR_062611|||http://purl.uniprot.org/annotation/VAR_062612|||http://purl.uniprot.org/annotation/VAR_062613|||http://purl.uniprot.org/annotation/VAR_062614|||http://purl.uniprot.org/annotation/VAR_062615|||http://purl.uniprot.org/annotation/VAR_062616|||http://purl.uniprot.org/annotation/VAR_062617|||http://purl.uniprot.org/annotation/VAR_062618|||http://purl.uniprot.org/annotation/VAR_062619|||http://purl.uniprot.org/annotation/VAR_062620|||http://purl.uniprot.org/annotation/VAR_062621|||http://purl.uniprot.org/annotation/VAR_062622|||http://purl.uniprot.org/annotation/VAR_062623|||http://purl.uniprot.org/annotation/VAR_062624|||http://purl.uniprot.org/annotation/VAR_062625|||http://purl.uniprot.org/annotation/VAR_062626|||http://purl.uniprot.org/annotation/VAR_062627|||http://purl.uniprot.org/annotation/VAR_062628|||http://purl.uniprot.org/annotation/VAR_062629|||http://purl.uniprot.org/annotation/VAR_062630|||http://purl.uniprot.org/annotation/VAR_062631|||http://purl.uniprot.org/annotation/VAR_062632|||http://purl.uniprot.org/annotation/VAR_062633|||http://purl.uniprot.org/annotation/VAR_062634|||http://purl.uniprot.org/annotation/VAR_062635|||http://purl.uniprot.org/annotation/VAR_062636|||http://purl.uniprot.org/annotation/VAR_062637|||http://purl.uniprot.org/annotation/VAR_062638|||http://purl.uniprot.org/annotation/VAR_062639|||http://purl.uniprot.org/annotation/VAR_062640|||http://purl.uniprot.org/annotation/VAR_062641|||http://purl.uniprot.org/annotation/VAR_062642|||http://purl.uniprot.org/annotation/VAR_062643|||http://purl.uniprot.org/annotation/VAR_062644|||http://purl.uniprot.org/annotation/VAR_062645|||http://purl.uniprot.org/annotation/VAR_062646|||http://purl.uniprot.org/annotation/VAR_062647|||http://purl.uniprot.org/annotation/VAR_062648
http://togogenome.org/gene/9606:FXR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51114                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to PAK1.|||Abolished phosphorylation by PAK1, leading to impaired activity.|||Agenet-like 1|||Agenet-like 2|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Does not affect binding to PAK1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||KH 1|||KH 2|||Mimics phosphorylation state; leading to increased activity.|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding RGG-box|||RNA-binding protein FXR1|||Reduced binding to PAK1.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050106|||http://purl.uniprot.org/annotation/VAR_014890|||http://purl.uniprot.org/annotation/VAR_016077|||http://purl.uniprot.org/annotation/VAR_036050|||http://purl.uniprot.org/annotation/VSP_019709|||http://purl.uniprot.org/annotation/VSP_019710|||http://purl.uniprot.org/annotation/VSP_019711
http://togogenome.org/gene/9606:CLCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51788                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CBS 1|||CBS 2|||Chloride channel protein 2|||Cytoplasmic|||Disordered|||Found in a patient with childhood absence epilepsy; unknown pathological significance.|||Helical|||In EIG11; associated with disease susceptibility; the mutant channel has accelerated deactivation rates compared to wild-type, but normal activation and peak current.|||In EJM8; associated with disease susceptibility; the mutant channel has accelerated deactivation rates compared to wild-type, but normal activation and peak current.|||In HALD2; increased voltage-gated chloride currents due to higher channel open probabilities at physiological cell membrane potentials.|||In HALD2; increased voltage-gated chloride currents due to higher channel open probabilities at physiological cell membrane potentials; increased aldosterone synthase expression.|||In HALD2; increased voltage-gated chloride currents due to higher channel open probabilitiesat at physiological cell membrane potentials.|||In HALD2; increased voltage-gated chloride currents; increased aldosterone synthase expression.|||In JAE2; unknown pathological significance.|||In LKPAT; decreased voltage-gated chloride channel activity; does not affect protein expression; does not affect localization at the cell membrane.|||In LKPAT; loss of function mutation; the mutant protein is restricted to the endoplasmic reticulum and hardly reached the plasma membrane; lower amounts of the mutant protein compared to wild-type.|||In LKPAT; loss of function mutation; the mutant protein is restricted to the endoplasmic reticulum and hardly reaches the plasma membrane; lower amounts of the mutant protein compared to wild-type.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||No effect.|||Note=Loop between two helices|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces channel activity.|||Removed|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3|||Slightly faster channel activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094433|||http://purl.uniprot.org/annotation/VAR_015989|||http://purl.uniprot.org/annotation/VAR_054550|||http://purl.uniprot.org/annotation/VAR_054551|||http://purl.uniprot.org/annotation/VAR_057886|||http://purl.uniprot.org/annotation/VAR_057887|||http://purl.uniprot.org/annotation/VAR_057888|||http://purl.uniprot.org/annotation/VAR_057889|||http://purl.uniprot.org/annotation/VAR_057890|||http://purl.uniprot.org/annotation/VAR_057891|||http://purl.uniprot.org/annotation/VAR_057892|||http://purl.uniprot.org/annotation/VAR_057893|||http://purl.uniprot.org/annotation/VAR_057894|||http://purl.uniprot.org/annotation/VAR_058426|||http://purl.uniprot.org/annotation/VAR_070976|||http://purl.uniprot.org/annotation/VAR_070977|||http://purl.uniprot.org/annotation/VAR_081154|||http://purl.uniprot.org/annotation/VAR_081155|||http://purl.uniprot.org/annotation/VAR_081156|||http://purl.uniprot.org/annotation/VAR_081157|||http://purl.uniprot.org/annotation/VAR_081158|||http://purl.uniprot.org/annotation/VAR_081159|||http://purl.uniprot.org/annotation/VAR_088252|||http://purl.uniprot.org/annotation/VSP_007831|||http://purl.uniprot.org/annotation/VSP_007832|||http://purl.uniprot.org/annotation/VSP_036455|||http://purl.uniprot.org/annotation/VSP_036456|||http://purl.uniprot.org/annotation/VSP_045457|||http://purl.uniprot.org/annotation/VSP_045458
http://togogenome.org/gene/9606:NARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43776                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asparagine--tRNA ligase, cytoplasmic|||Disordered|||In NEDMILEG; decreased asparagine-tRNA ligase activity in patient cells.|||In NEDMILEG; unable to rescue growth defects in a yeast complementation assay.|||In NEDMILEG; unknown pathological significance.|||In NEDMILG.|||In NEDMILG; decreased protein levels in patient cells; decreased asparagine-tRNA ligase activity in patient cells.|||In NEDMILG; unknown pathological significance.|||In NEDMILG; unknown pathological significance; decreased protein levels in patient cells.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000176496|||http://purl.uniprot.org/annotation/VAR_085100|||http://purl.uniprot.org/annotation/VAR_085101|||http://purl.uniprot.org/annotation/VAR_085102|||http://purl.uniprot.org/annotation/VAR_085103|||http://purl.uniprot.org/annotation/VAR_085104|||http://purl.uniprot.org/annotation/VAR_085105|||http://purl.uniprot.org/annotation/VAR_085106|||http://purl.uniprot.org/annotation/VAR_085107|||http://purl.uniprot.org/annotation/VAR_085108|||http://purl.uniprot.org/annotation/VAR_085109|||http://purl.uniprot.org/annotation/VAR_085110|||http://purl.uniprot.org/annotation/VAR_085111|||http://purl.uniprot.org/annotation/VAR_085112|||http://purl.uniprot.org/annotation/VSP_056201|||http://purl.uniprot.org/annotation/VSP_056202
http://togogenome.org/gene/9606:ZNF638                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K583|||http://purl.uniprot.org/uniprot/Q14966                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Involved in localization to nuclear speckles|||Matrin-type|||Phosphoserine|||Polar residues|||RRM|||RRM 1|||RRM 2|||Zinc finger protein 638                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082011|||http://purl.uniprot.org/annotation/VAR_023069|||http://purl.uniprot.org/annotation/VAR_023070|||http://purl.uniprot.org/annotation/VAR_023071|||http://purl.uniprot.org/annotation/VAR_023072|||http://purl.uniprot.org/annotation/VAR_052238|||http://purl.uniprot.org/annotation/VSP_014801|||http://purl.uniprot.org/annotation/VSP_014802|||http://purl.uniprot.org/annotation/VSP_014803|||http://purl.uniprot.org/annotation/VSP_014804|||http://purl.uniprot.org/annotation/VSP_014805|||http://purl.uniprot.org/annotation/VSP_014806|||http://purl.uniprot.org/annotation/VSP_059342|||http://purl.uniprot.org/annotation/VSP_059343
http://togogenome.org/gene/9606:MMP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N119                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cysteine switch|||Disordered|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In HTX7.|||In HTX7; found associated with K-215.|||In HTX7; found associated with W-31.|||In HTX7; unknown pathological significance.|||Matrix metalloproteinase-21|||N-linked (GlcNAc...) asparagine|||Pro residues|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028839|||http://purl.uniprot.org/annotation/PRO_0000028840|||http://purl.uniprot.org/annotation/VAR_019393|||http://purl.uniprot.org/annotation/VAR_022291|||http://purl.uniprot.org/annotation/VAR_022292|||http://purl.uniprot.org/annotation/VAR_022293|||http://purl.uniprot.org/annotation/VAR_022294|||http://purl.uniprot.org/annotation/VAR_032824|||http://purl.uniprot.org/annotation/VAR_057803|||http://purl.uniprot.org/annotation/VAR_057804|||http://purl.uniprot.org/annotation/VAR_076319|||http://purl.uniprot.org/annotation/VAR_076320|||http://purl.uniprot.org/annotation/VAR_076321|||http://purl.uniprot.org/annotation/VAR_076322|||http://purl.uniprot.org/annotation/VAR_076323|||http://purl.uniprot.org/annotation/VAR_076324|||http://purl.uniprot.org/annotation/VAR_076325|||http://purl.uniprot.org/annotation/VAR_076326|||http://purl.uniprot.org/annotation/VAR_076327
http://togogenome.org/gene/9606:GCM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP62                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chorion-specific transcription factor GCMa|||Disordered|||GCM|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126647
http://togogenome.org/gene/9606:ACKR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25106                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Atypical chemokine receptor 3|||C-terminal cytoplasmic tail|||Cytoplasmic|||Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with A-145.|||Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with V-147.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In OCABSN; no effect on protein levels and cell membrane location; lower binding affinity for CXCL12.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070101|||http://purl.uniprot.org/annotation/VAR_027477|||http://purl.uniprot.org/annotation/VAR_085335
http://togogenome.org/gene/9606:ANKZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZS4|||http://purl.uniprot.org/uniprot/Q9H8Y5                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Abolished ability to cleave polypeptidyl-tRNAs.|||Abolishes interaction with VCP.|||Basic and acidic residues|||C2H2-type|||Disordered|||Found in a patient with infantile-onset inflammatory bowel disease; unknown pathological significance.|||Found in a patient with infantile-onset inflammatory bowel disease; unknown pathological significance; decreased function in cellular response to hydrogen peroxide; decreased protein abundance; does not affect interaction with VCP.|||Found in a patient with infantile-onset inflammatory bowel disease; unknown pathological significance; decreased function in cellular response to hydrogen peroxide; does not affect protein abundance; does not affect interaction with VCP.|||Phosphoserine|||Phosphothreonine|||Polar residues|||VCP/p97-interacting motif (VIM)|||VLRF1|||Vms1-associating treble clef|||tRNA endonuclease ANKZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247278|||http://purl.uniprot.org/annotation/VAR_048269|||http://purl.uniprot.org/annotation/VAR_048270|||http://purl.uniprot.org/annotation/VAR_079136|||http://purl.uniprot.org/annotation/VAR_079137|||http://purl.uniprot.org/annotation/VAR_079138|||http://purl.uniprot.org/annotation/VAR_079139
http://togogenome.org/gene/9606:SCGB1D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XE38                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 1D member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036380
http://togogenome.org/gene/9606:RNF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43567                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ER stress-induced JNK activation and apoptosis.|||Abolishes ER stress-induced JNK activation and apoptosis. Abolishes interaction with ERN1. Does not affect localization to endoplasmic reticulum.|||Abolishes ER stress-induced JNK activation and apoptosis. Disrupts localization to endoplasmic reticulum.|||Acidic residues|||Complete loss of E3 ligase activity; when associated with A-258.|||Complete loss of E3 ligase activity; when associated with A-260.|||Cytoplasmic|||Disordered|||Drastically reduces E3 ligase activity.|||E3 ubiquitin-protein ligase RNF13|||Found in a tumor sample; unknown pathological significance; abolished ability to regulate protein trafficking and localization.|||Found in a tumor sample; unknown pathological significance; abolished localization to endosomes.|||Helical|||In DEE73.|||In DEE73; gain-of-function variant; increased ER stress-induced apoptosis.|||In isoform 2.|||Loss of glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on ER stress-induced JNK activation and apoptosis.|||No effect on ER stress-induced JNK activation and apoptosis. No effect on interaction with ERN1.|||No effect on glycosylation.|||PA|||Polar residues|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056054|||http://purl.uniprot.org/annotation/VAR_082117|||http://purl.uniprot.org/annotation/VAR_082118|||http://purl.uniprot.org/annotation/VAR_086368|||http://purl.uniprot.org/annotation/VAR_086369|||http://purl.uniprot.org/annotation/VAR_086370|||http://purl.uniprot.org/annotation/VSP_055430|||http://purl.uniprot.org/annotation/VSP_055431
http://togogenome.org/gene/9606:H2AZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C0S5                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand                                                                                  ^@                                                                                  Abolishes interaction with VPS72; when associated with I-83 and N-93.|||Decreased acetylation by KAT2A.|||Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with I-83. Abolishes interaction with VPS72; when associated with I-83 and IG-101.|||Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with N-93. Abolishes interaction with VPS72; when associated with N-93 and IG-101.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone H2A.Z|||M6 cassette|||Monoisotopic, not modified.|||N6-acetyllysine; alternate|||N6-lactoyllysine|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||No effect on interaction with VPS72.|||Removed|||Required for interaction with INCENP|||Required for interaction with PWWP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055297
http://togogenome.org/gene/9606:DNASE1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49184                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Deoxyribonuclease-1-like 1|||Essential for enzymatic activity|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007284|||http://purl.uniprot.org/annotation/VAR_048869
http://togogenome.org/gene/9606:OR13C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGS8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150734|||http://purl.uniprot.org/annotation/VAR_024132|||http://purl.uniprot.org/annotation/VAR_024133|||http://purl.uniprot.org/annotation/VAR_024134|||http://purl.uniprot.org/annotation/VAR_024135|||http://purl.uniprot.org/annotation/VAR_034306|||http://purl.uniprot.org/annotation/VAR_053299|||http://purl.uniprot.org/annotation/VAR_053300|||http://purl.uniprot.org/annotation/VAR_060032|||http://purl.uniprot.org/annotation/VAR_060033|||http://purl.uniprot.org/annotation/VAR_060034
http://togogenome.org/gene/9606:PCDHGA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-A11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003968|||http://purl.uniprot.org/annotation/VAR_033711|||http://purl.uniprot.org/annotation/VSP_008679|||http://purl.uniprot.org/annotation/VSP_008680|||http://purl.uniprot.org/annotation/VSP_008681
http://togogenome.org/gene/9606:PRR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K699|||http://purl.uniprot.org/uniprot/P85299                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with RICTOR|||Phosphoserine|||Polar residues|||Proline-rich protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308162|||http://purl.uniprot.org/annotation/VAR_062230|||http://purl.uniprot.org/annotation/VSP_001646|||http://purl.uniprot.org/annotation/VSP_001648|||http://purl.uniprot.org/annotation/VSP_028884|||http://purl.uniprot.org/annotation/VSP_028885|||http://purl.uniprot.org/annotation/VSP_045883
http://togogenome.org/gene/9606:TNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRZ4|||http://purl.uniprot.org/uniprot/A8K4N4|||http://purl.uniprot.org/uniprot/B7Z8K2|||http://purl.uniprot.org/uniprot/Q15025                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to polyubiquitin ('K-63'-linked and linear).|||Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In patients with gastrointestinal diffuse large cell lymphoma.|||In patients with gastrointestinal diffuse large cell lymphoma; somatic mutation.|||In patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation.|||Interaction with Nef|||Interaction with Shigella flexneri ipah9.8|||Nuclear localization signal|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for inhibitory activity of TNF-induced NF-kappa-B activation|||TNFAIP3-interacting protein 1|||Ubiquitin-binding domain (UBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096691|||http://purl.uniprot.org/annotation/VAR_051453|||http://purl.uniprot.org/annotation/VAR_051454|||http://purl.uniprot.org/annotation/VAR_051455|||http://purl.uniprot.org/annotation/VAR_051456|||http://purl.uniprot.org/annotation/VAR_051457|||http://purl.uniprot.org/annotation/VAR_067965|||http://purl.uniprot.org/annotation/VAR_067966|||http://purl.uniprot.org/annotation/VAR_067967|||http://purl.uniprot.org/annotation/VAR_067968|||http://purl.uniprot.org/annotation/VSP_003913|||http://purl.uniprot.org/annotation/VSP_045296|||http://purl.uniprot.org/annotation/VSP_055208|||http://purl.uniprot.org/annotation/VSP_055209|||http://purl.uniprot.org/annotation/VSP_055210|||http://purl.uniprot.org/annotation/VSP_055211|||http://purl.uniprot.org/annotation/VSP_055212|||http://purl.uniprot.org/annotation/VSP_055213|||http://purl.uniprot.org/annotation/VSP_055214
http://togogenome.org/gene/9606:DCTN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00399                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Modified Residue|||Strand                                                                                  ^@                                                                                  Dynactin subunit 6|||Phosphothreonine; by CDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079830
http://togogenome.org/gene/9606:ATP7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A669KB88|||http://purl.uniprot.org/uniprot/B7ZLR3|||http://purl.uniprot.org/uniprot/B7ZLR4|||http://purl.uniprot.org/uniprot/E7ET55|||http://purl.uniprot.org/uniprot/P35670                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Altered copper-induced relocalization.|||Basic and acidic residues|||Copper-transporting ATPase 2|||Cytoplasmic|||Decreased copper transport activity with no effect on ATPase activity.|||Decreased copper transport activity; no effect on ATPase activity.|||Decreased copper transport rates; no effect on ATPase activity.|||Disordered|||Does not affect copper-induced relocalization.|||Extracellular|||HMA|||HMA 1|||HMA 2|||HMA 3|||HMA 4|||HMA 5|||HMA 6|||Helical|||In WD.|||In WD; affects copper-induced relocalization; the mutant is constitutively trafficked to the basolateral membrane instead of staying in the TGN under low copper conditions; does not affect interaction with COMMD1.|||In WD; also found in a patient with hypoceruloplasminemia without clinical manifestations of WD in the central nervous system or liver; a liver biopsy of the patient with hypoceruloplasminemia shows no copper or iron accumulation in Kupffer cells or hepatocytes; due to a nucleotide substitution that also results in out-of-frame partial skipping of exon 6, stop gain and reduced expression of the truncated protein; variant R-645 has no effect on protein localization; no effect on copper transport; does not affect interaction with COMMD1.|||In WD; common mutation.|||In WD; common mutation; decreased copper transport activity; loss of ATPase activity; cannot form an acylphosphate intermediate during catalysis; does not alter the folding of the nucleotide-binding domain; decreased stability; does not localize to late endosomes.|||In WD; common mutation; decreased copper transport activity; no effect on ATPase activity.|||In WD; copper ion transmembrane transporter activity.|||In WD; decreased copper ion transmembrane transporter activity.|||In WD; decreased copper transport activity.|||In WD; decreased copper transport activity; decreased ATPase activity; does not affect interaction with COMMD1.|||In WD; decreased copper transport activity; decreased ATPase activity; increased interaction with COMMD1; decreased localization to trans-Golgi network; increased degradation.|||In WD; decreased copper transport activity; increased ATPase activity.|||In WD; decreased copper transport activity; increased ATPase activity; decreased localization to TGN and reduced capacity to redistribute to cytoplasmic vesicles under high-copper levels.|||In WD; decreased copper transport activity; increased ATPase activity; decreased localization to the TGN.|||In WD; decreased copper transport activity; increased ATPase activity; does not affect interaction with COMMD1.|||In WD; decreased copper transport activity; increased ATPase activity; no effect on localization.|||In WD; decreased copper transport activity; loss of ATPase activity.|||In WD; decreased copper transport activity; no effect on ATPase activity.|||In WD; decreased copper transport activity; no effect on ATPase activity; decreased localization to the TGN.|||In WD; does not bind ATP; the mutant is stable and is properly targeted to the TGN.|||In WD; increased interaction with COMMD1; decreased localization to trans-Glogi network.|||In WD; increased protein degradation; the mutant has a diffuse cytoplasmic localization pattern and is absent from TGN under conditions of low-copper levels.|||In WD; likely benign variant.|||In WD; loss of copper transport activity.|||In WD; loss of copper transport activity; increased ATPase activity; does not affect localization to late endosomes.|||In WD; loss of copper transport activity; loss of ATPase activity.|||In WD; loss of copper transport activity; no effect on ATPase activity.|||In WD; marked impairment in copper transport.|||In WD; moderate impairment in copper transport.|||In WD; most common mutation; decreased copper transport activity; extensively localized throughout the cell in the distribution pattern of the endoplasmic reticulum.|||In WD; no effect on copper transport activity; normally localized to TGN network but unable to redistribute to cytoplasmic vesicles in response to copper.|||In WD; possible decreased copper transport activity; increased ATPase activity.|||In WD; unknown pathological significance.|||In WD; unknown pathological significance; does not affect interaction with COMMD1.|||In WD; unknown pathological significance; increased interaction with COMMD1.|||In WD; unknown pathological significance; localized at the TGN as the wild-type under conditions of low-copper levels.|||In WD; unknown pathological significance; no effect on copper transport activity.|||In WD; unknown pathological significance; no effect on copper transport activity; decreased localization to TGN and reduced capacity to redistribute to cytoplasmic vesicles under high-copper levels.|||In WD; unknown pathological significance; no effect on copper transport activity; does not affect interaction with COMMD1.|||In WD; unknown pathological significance; no effect on protein abundance; altered copper-induced relocalization; no effect on copper transport activity.|||In WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; may have an effect on copper transport activity; no effect on ATPase activity; does not affect interaction with COMMD1.|||In WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; no effect on copper transport activity.|||In WD; unknown pathological significance; no effect on protein abundance; no effect on protein localization; no effect on copper transport activity; does not affect interaction with COMMD1.|||In WD; yeast complementation assays show that the variant does not rescue iron-uptake deficiency of yeast mutant ccc2.|||In WD; yeast complementation assays show that the variant fully rescue iron-uptake deficiency of yeast mutant ccc2.|||In WD; yeast complementation assays show that the variant intermediately rescue iron-uptake deficiency of yeast mutant ccc2.|||In WD; yeast complementation assays show that the variant mildly rescue iron-uptake deficiency of yeast mutant ccc2.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Individuals heterozygous for Wilson disease mutations on the R-875 background may manifest the disease phenotype under conditions of copper deficiency; affects protein folding; localized to the ER and absent from TGN under low copper conditions; in response to high copper levels it relocalizes to vesicles and properly cycle back to TGN.|||Loss of ATPase activity. Cannot form an acylphosphate intermediate during catalysis. Does not alter folding of the nucleotide-binding domain.|||Loss of copper transport activity.|||No effect on copper transport activity.|||Phosphoserine|||Polar residues|||WND/140 kDa ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046314|||http://purl.uniprot.org/annotation/PRO_0000296199|||http://purl.uniprot.org/annotation/VAR_000703|||http://purl.uniprot.org/annotation/VAR_000704|||http://purl.uniprot.org/annotation/VAR_000705|||http://purl.uniprot.org/annotation/VAR_000706|||http://purl.uniprot.org/annotation/VAR_000707|||http://purl.uniprot.org/annotation/VAR_000708|||http://purl.uniprot.org/annotation/VAR_000710|||http://purl.uniprot.org/annotation/VAR_000711|||http://purl.uniprot.org/annotation/VAR_000712|||http://purl.uniprot.org/annotation/VAR_000713|||http://purl.uniprot.org/annotation/VAR_000714|||http://purl.uniprot.org/annotation/VAR_000715|||http://purl.uniprot.org/annotation/VAR_000716|||http://purl.uniprot.org/annotation/VAR_000717|||http://purl.uniprot.org/annotation/VAR_000719|||http://purl.uniprot.org/annotation/VAR_000720|||http://purl.uniprot.org/annotation/VAR_000721|||http://purl.uniprot.org/annotation/VAR_000722|||http://purl.uniprot.org/annotation/VAR_000723|||http://purl.uniprot.org/annotation/VAR_000724|||http://purl.uniprot.org/annotation/VAR_000725|||http://purl.uniprot.org/annotation/VAR_000726|||http://purl.uniprot.org/annotation/VAR_000727|||http://purl.uniprot.org/annotation/VAR_000728|||http://purl.uniprot.org/annotation/VAR_000729|||http://purl.uniprot.org/annotation/VAR_000730|||http://purl.uniprot.org/annotation/VAR_000731|||http://purl.uniprot.org/annotation/VAR_000732|||http://purl.uniprot.org/annotation/VAR_000733|||http://purl.uniprot.org/annotation/VAR_000734|||http://purl.uniprot.org/annotation/VAR_000735|||http://purl.uniprot.org/annotation/VAR_000736|||http://purl.uniprot.org/annotation/VAR_000737|||http://purl.uniprot.org/annotation/VAR_000738|||http://purl.uniprot.org/annotation/VAR_000739|||http://purl.uniprot.org/annotation/VAR_000740|||http://purl.uniprot.org/annotation/VAR_000741|||http://purl.uniprot.org/annotation/VAR_000742|||http://purl.uniprot.org/annotation/VAR_000743|||http://purl.uniprot.org/annotation/VAR_000744|||http://purl.uniprot.org/annotation/VAR_000745|||http://purl.uniprot.org/annotation/VAR_000746|||http://purl.uniprot.org/annotation/VAR_000747|||http://purl.uniprot.org/annotation/VAR_000748|||http://purl.uniprot.org/annotation/VAR_000749|||http://purl.uniprot.org/annotation/VAR_000750|||http://purl.uniprot.org/annotation/VAR_000751|||http://purl.uniprot.org/annotation/VAR_000752|||http://purl.uniprot.org/annotation/VAR_000753|||http://purl.uniprot.org/annotation/VAR_000754|||http://purl.uniprot.org/annotation/VAR_000755|||http://purl.uniprot.org/annotation/VAR_000756|||http://purl.uniprot.org/annotation/VAR_000757|||http://purl.uniprot.org/annotation/VAR_000758|||http://purl.uniprot.org/annotation/VAR_000759|||http://purl.uniprot.org/annotation/VAR_000760|||http://purl.uniprot.org/annotation/VAR_000761|||http://purl.uniprot.org/annotation/VAR_000762|||http://purl.uniprot.org/annotation/VAR_000763|||http://purl.uniprot.org/annotation/VAR_000764|||http://purl.uniprot.org/annotation/VAR_000765|||http://purl.uniprot.org/annotation/VAR_000766|||http://purl.uniprot.org/annotation/VAR_000767|||http://purl.uniprot.org/annotation/VAR_000768|||http://purl.uniprot.org/annotation/VAR_000769|||http://purl.uniprot.org/annotation/VAR_000770|||http://purl.uniprot.org/annotation/VAR_000771|||http://purl.uniprot.org/annotation/VAR_000772|||http://purl.uniprot.org/annotation/VAR_000773|||http://purl.uniprot.org/annotation/VAR_000774|||http://purl.uniprot.org/annotation/VAR_000775|||http://purl.uniprot.org/annotation/VAR_000776|||http://purl.uniprot.org/annotation/VAR_000777|||http://purl.uniprot.org/annotation/VAR_000778|||http://purl.uniprot.org/annotation/VAR_000779|||http://purl.uniprot.org/annotation/VAR_000781|||http://purl.uniprot.org/annotation/VAR_000782|||http://purl.uniprot.org/annotation/VAR_000783|||http://purl.uniprot.org/annotation/VAR_000784|||http://purl.uniprot.org/annotation/VAR_000785|||http://purl.uniprot.org/annotation/VAR_000786|||http://purl.uniprot.org/annotation/VAR_000787|||http://purl.uniprot.org/annotation/VAR_000788|||http://purl.uniprot.org/annotation/VAR_000789|||http://purl.uniprot.org/annotation/VAR_000790|||http://purl.uniprot.org/annotation/VAR_000791|||http://purl.uniprot.org/annotation/VAR_009004|||http://purl.uniprot.org/annotation/VAR_009005|||http://purl.uniprot.org/annotation/VAR_009006|||http://purl.uniprot.org/annotation/VAR_009007|||http://purl.uniprot.org/annotation/VAR_009008|||http://purl.uniprot.org/annotation/VAR_009009|||http://purl.uniprot.org/annotation/VAR_009010|||http://purl.uniprot.org/annotation/VAR_009011|||http://purl.uniprot.org/annotation/VAR_009012|||http://purl.uniprot.org/annotation/VAR_009013|||http://purl.uniprot.org/annotation/VAR_009014|||http://purl.uniprot.org/annotation/VAR_009015|||http://purl.uniprot.org/annotation/VAR_009016|||http://purl.uniprot.org/annotation/VAR_009017|||http://purl.uniprot.org/annotation/VAR_009018|||http://purl.uniprot.org/annotation/VAR_009019|||http://purl.uniprot.org/annotation/VAR_009020|||http://purl.uniprot.org/annotation/VAR_009021|||http://purl.uniprot.org/annotation/VAR_009022|||http://purl.uniprot.org/annotation/VAR_009023|||http://purl.uniprot.org/annotation/VAR_009024|||http://purl.uniprot.org/annotation/VAR_009025|||http://purl.uniprot.org/annotation/VAR_009026|||http://purl.uniprot.org/annotation/VAR_009027|||http://purl.uniprot.org/annotation/VAR_009028|||http://purl.uniprot.org/annotation/VAR_009029|||http://purl.uniprot.org/annotation/VAR_009030|||http://purl.uniprot.org/annotation/VAR_009031|||http://purl.uniprot.org/annotation/VAR_009032|||http://purl.uniprot.org/annotation/VAR_010009|||http://purl.uniprot.org/annotation/VAR_010010|||http://purl.uniprot.org/annotation/VAR_010011|||http://purl.uniprot.org/annotation/VAR_010012|||http://purl.uniprot.org/annotation/VAR_010013|||http://purl.uniprot.org/annotation/VAR_010014|||http://purl.uniprot.org/annotation/VAR_010015|||http://purl.uniprot.org/annotation/VAR_010017|||http://purl.uniprot.org/annotation/VAR_010018|||http://purl.uniprot.org/annotation/VAR_010019|||http://purl.uniprot.org/annotation/VAR_010020|||http://purl.uniprot.org/annotation/VAR_010021|||http://purl.uniprot.org/annotation/VAR_023010|||http://purl.uniprot.org/annotation/VAR_023011|||http://purl.uniprot.org/annotation/VAR_023012|||http://purl.uniprot.org/annotation/VAR_023013|||http://purl.uniprot.org/annotation/VAR_023014|||http://purl.uniprot.org/annotation/VAR_023015|||http://purl.uniprot.org/annotation/VAR_023016|||http://purl.uniprot.org/annotation/VAR_023017|||http://purl.uniprot.org/annotation/VAR_023018|||http://purl.uniprot.org/annotation/VAR_023019|||http://purl.uniprot.org/annotation/VAR_023020|||http://purl.uniprot.org/annotation/VAR_023021|||http://purl.uniprot.org/annotation/VAR_023022|||http://purl.uniprot.org/annotation/VAR_023023|||http://purl.uniprot.org/annotation/VAR_023024|||http://purl.uniprot.org/annotation/VAR_023025|||http://purl.uniprot.org/annotation/VAR_023026|||http://purl.uniprot.org/annotation/VAR_023027|||http://purl.uniprot.org/annotation/VAR_023028|||http://purl.uniprot.org/annotation/VAR_023029|||http://purl.uniprot.org/annotation/VAR_023030|||http://purl.uniprot.org/annotation/VAR_023031|||http://purl.uniprot.org/annotation/VAR_023032|||http://purl.uniprot.org/annotation/VAR_023033|||http://purl.uniprot.org/annotation/VAR_023034|||http://purl.uniprot.org/annotation/VAR_023035|||http://purl.uniprot.org/annotation/VAR_023036|||http://purl.uniprot.org/annotation/VAR_023037|||http://purl.uniprot.org/annotation/VAR_023038|||http://purl.uniprot.org/annotation/VAR_023039|||http://purl.uniprot.org/annotation/VAR_023040|||http://purl.uniprot.org/annotation/VAR_023041|||http://purl.uniprot.org/annotation/VAR_023042|||http://purl.uniprot.org/annotation/VAR_023043|||http://purl.uniprot.org/annotation/VAR_023044|||http://purl.uniprot.org/annotation/VAR_023045|||http://purl.uniprot.org/annotation/VAR_044453|||http://purl.uniprot.org/annotation/VAR_044454|||http://purl.uniprot.org/annotation/VAR_044455|||http://purl.uniprot.org/annotation/VAR_044456|||http://purl.uniprot.org/annotation/VAR_044457|||http://purl.uniprot.org/annotation/VAR_044458|||http://purl.uniprot.org/annotation/VAR_044459|||http://purl.uniprot.org/annotation/VAR_044460|||http://purl.uniprot.org/annotation/VAR_044461|||http://purl.uniprot.org/annotation/VAR_044462|||http://purl.uniprot.org/annotation/VAR_044463|||http://purl.uniprot.org/annotation/VAR_044464|||http://purl.uniprot.org/annotation/VAR_044465|||http://purl.uniprot.org/annotation/VAR_044466|||http://purl.uniprot.org/annotation/VAR_044468|||http://purl.uniprot.org/annotation/VAR_044469|||http://purl.uniprot.org/annotation/VAR_044470|||http://purl.uniprot.org/annotation/VAR_044471|||http://purl.uniprot.org/annotation/VAR_044472|||http://purl.uniprot.org/annotation/VAR_044473|||http://purl.uniprot.org/annotation/VAR_044474|||http://purl.uniprot.org/annotation/VAR_044476|||http://purl.uniprot.org/annotation/VAR_044477|||http://purl.uniprot.org/annotation/VAR_044478|||http://purl.uniprot.org/annotation/VAR_044479|||http://purl.uniprot.org/annotation/VAR_044480|||http://purl.uniprot.org/annotation/VAR_044481|||http://purl.uniprot.org/annotation/VAR_044483|||http://purl.uniprot.org/annotation/VAR_044484|||http://purl.uniprot.org/annotation/VAR_044485|||http://purl.uniprot.org/annotation/VAR_044486|||http://purl.uniprot.org/annotation/VAR_044487|||http://purl.uniprot.org/annotation/VAR_044488|||http://purl.uniprot.org/annotation/VAR_044489|||http://purl.uniprot.org/annotation/VAR_044490|||http://purl.uniprot.org/annotation/VAR_044491|||http://purl.uniprot.org/annotation/VAR_044492|||http://purl.uniprot.org/annotation/VAR_044493|||http://purl.uniprot.org/annotation/VAR_044494|||http://purl.uniprot.org/annotation/VAR_044495|||http://purl.uniprot.org/annotation/VAR_058925|||http://purl.uniprot.org/annotation/VAR_058926|||http://purl.uniprot.org/annotation/VAR_058927|||http://purl.uniprot.org/annotation/VAR_058928|||http://purl.uniprot.org/annotation/VAR_058929|||http://purl.uniprot.org/annotation/VAR_058930|||http://purl.uniprot.org/annotation/VAR_058931|||http://purl.uniprot.org/annotation/VAR_058932|||http://purl.uniprot.org/annotation/VAR_058933|||http://purl.uniprot.org/annotation/VAR_058934|||http://purl.uniprot.org/annotation/VAR_058935|||http://purl.uniprot.org/annotation/VAR_058936|||http://purl.uniprot.org/annotation/VAR_058937|||http://purl.uniprot.org/annotation/VAR_067335|||http://purl.uniprot.org/annotation/VAR_067336|||http://purl.uniprot.org/annotation/VAR_067337|||http://purl.uniprot.org/annotation/VAR_067338|||http://purl.uniprot.org/annotation/VAR_075336|||http://purl.uniprot.org/annotation/VAR_075337|||http://purl.uniprot.org/annotation/VAR_075338|||http://purl.uniprot.org/annotation/VAR_075339|||http://purl.uniprot.org/annotation/VAR_075340|||http://purl.uniprot.org/annotation/VAR_076693|||http://purl.uniprot.org/annotation/VAR_076694|||http://purl.uniprot.org/annotation/VAR_076695|||http://purl.uniprot.org/annotation/VAR_076696|||http://purl.uniprot.org/annotation/VAR_076697|||http://purl.uniprot.org/annotation/VAR_076698|||http://purl.uniprot.org/annotation/VAR_076699|||http://purl.uniprot.org/annotation/VAR_076700|||http://purl.uniprot.org/annotation/VAR_076701|||http://purl.uniprot.org/annotation/VAR_076702|||http://purl.uniprot.org/annotation/VAR_076703|||http://purl.uniprot.org/annotation/VAR_076704|||http://purl.uniprot.org/annotation/VAR_076705|||http://purl.uniprot.org/annotation/VAR_076706|||http://purl.uniprot.org/annotation/VAR_076707|||http://purl.uniprot.org/annotation/VAR_076708|||http://purl.uniprot.org/annotation/VAR_076709|||http://purl.uniprot.org/annotation/VAR_076710|||http://purl.uniprot.org/annotation/VAR_076711|||http://purl.uniprot.org/annotation/VAR_076729|||http://purl.uniprot.org/annotation/VAR_076730|||http://purl.uniprot.org/annotation/VAR_076731|||http://purl.uniprot.org/annotation/VAR_076732|||http://purl.uniprot.org/annotation/VAR_076733|||http://purl.uniprot.org/annotation/VAR_076734|||http://purl.uniprot.org/annotation/VAR_076735|||http://purl.uniprot.org/annotation/VAR_076736|||http://purl.uniprot.org/annotation/VAR_076737|||http://purl.uniprot.org/annotation/VAR_076738|||http://purl.uniprot.org/annotation/VAR_076739|||http://purl.uniprot.org/annotation/VAR_076740|||http://purl.uniprot.org/annotation/VAR_076741|||http://purl.uniprot.org/annotation/VAR_076742|||http://purl.uniprot.org/annotation/VAR_076743|||http://purl.uniprot.org/annotation/VAR_076744|||http://purl.uniprot.org/annotation/VAR_076745|||http://purl.uniprot.org/annotation/VAR_076746|||http://purl.uniprot.org/annotation/VAR_076747|||http://purl.uniprot.org/annotation/VAR_076748|||http://purl.uniprot.org/annotation/VAR_076749|||http://purl.uniprot.org/annotation/VAR_076750|||http://purl.uniprot.org/annotation/VAR_076751|||http://purl.uniprot.org/annotation/VAR_076752|||http://purl.uniprot.org/annotation/VAR_076765|||http://purl.uniprot.org/annotation/VAR_076766|||http://purl.uniprot.org/annotation/VAR_076767|||http://purl.uniprot.org/annotation/VAR_076768|||http://purl.uniprot.org/annotation/VAR_076769|||http://purl.uniprot.org/annotation/VAR_076770|||http://purl.uniprot.org/annotation/VAR_076771|||http://purl.uniprot.org/annotation/VAR_076772|||http://purl.uniprot.org/annotation/VAR_076773|||http://purl.uniprot.org/annotation/VAR_076774|||http://purl.uniprot.org/annotation/VAR_076793|||http://purl.uniprot.org/annotation/VAR_076794|||http://purl.uniprot.org/annotation/VAR_076795|||http://purl.uniprot.org/annotation/VAR_076810|||http://purl.uniprot.org/annotation/VAR_076811|||http://purl.uniprot.org/annotation/VAR_076812|||http://purl.uniprot.org/annotation/VAR_076813|||http://purl.uniprot.org/annotation/VAR_076814|||http://purl.uniprot.org/annotation/VAR_076815|||http://purl.uniprot.org/annotation/VAR_076816|||http://purl.uniprot.org/annotation/VAR_076817|||http://purl.uniprot.org/annotation/VAR_076818|||http://purl.uniprot.org/annotation/VAR_076819|||http://purl.uniprot.org/annotation/VAR_076970|||http://purl.uniprot.org/annotation/VAR_076971|||http://purl.uniprot.org/annotation/VAR_076972|||http://purl.uniprot.org/annotation/VAR_076973|||http://purl.uniprot.org/annotation/VAR_077616|||http://purl.uniprot.org/annotation/VAR_077617|||http://purl.uniprot.org/annotation/VAR_077618|||http://purl.uniprot.org/annotation/VAR_079550|||http://purl.uniprot.org/annotation/VAR_079551|||http://purl.uniprot.org/annotation/VSP_000426|||http://purl.uniprot.org/annotation/VSP_000427|||http://purl.uniprot.org/annotation/VSP_016559|||http://purl.uniprot.org/annotation/VSP_016560|||http://purl.uniprot.org/annotation/VSP_059175
http://togogenome.org/gene/9606:KRT23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC04|||http://purl.uniprot.org/uniprot/Q9C075                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||Keratin, type I cytoskeletal 23|||Linker 1|||Linker 12|||Polar residues|||Rod-like helical tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063677|||http://purl.uniprot.org/annotation/VAR_031608|||http://purl.uniprot.org/annotation/VAR_049785|||http://purl.uniprot.org/annotation/VSP_055662
http://togogenome.org/gene/9606:NEB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20929|||http://purl.uniprot.org/uniprot/Q05C45|||http://purl.uniprot.org/uniprot/Q96MF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In AMC6.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Interaction with SVIL|||Nebulin|||Nebulin 1|||Nebulin 10|||Nebulin 100|||Nebulin 101|||Nebulin 102|||Nebulin 103|||Nebulin 104|||Nebulin 105|||Nebulin 106|||Nebulin 107|||Nebulin 108|||Nebulin 109|||Nebulin 11|||Nebulin 110|||Nebulin 111|||Nebulin 112|||Nebulin 113|||Nebulin 114|||Nebulin 115|||Nebulin 116|||Nebulin 117|||Nebulin 118|||Nebulin 119|||Nebulin 12|||Nebulin 120|||Nebulin 121|||Nebulin 122|||Nebulin 123|||Nebulin 124|||Nebulin 125|||Nebulin 126|||Nebulin 127|||Nebulin 128|||Nebulin 129|||Nebulin 13|||Nebulin 130|||Nebulin 131|||Nebulin 132|||Nebulin 133|||Nebulin 134|||Nebulin 135|||Nebulin 136|||Nebulin 137|||Nebulin 138|||Nebulin 139|||Nebulin 14|||Nebulin 140|||Nebulin 141|||Nebulin 142|||Nebulin 143|||Nebulin 144|||Nebulin 145|||Nebulin 146|||Nebulin 147|||Nebulin 148|||Nebulin 149|||Nebulin 15|||Nebulin 150|||Nebulin 151|||Nebulin 152|||Nebulin 153|||Nebulin 154|||Nebulin 155|||Nebulin 156|||Nebulin 157|||Nebulin 158|||Nebulin 159|||Nebulin 16|||Nebulin 160|||Nebulin 161|||Nebulin 162|||Nebulin 163|||Nebulin 164|||Nebulin 165|||Nebulin 166|||Nebulin 167|||Nebulin 168|||Nebulin 169|||Nebulin 17|||Nebulin 170|||Nebulin 171|||Nebulin 172|||Nebulin 173|||Nebulin 174|||Nebulin 175|||Nebulin 176|||Nebulin 177|||Nebulin 178|||Nebulin 18|||Nebulin 19|||Nebulin 2|||Nebulin 20|||Nebulin 21|||Nebulin 22|||Nebulin 23|||Nebulin 24|||Nebulin 25|||Nebulin 26|||Nebulin 27|||Nebulin 28|||Nebulin 29|||Nebulin 3|||Nebulin 30|||Nebulin 31|||Nebulin 32|||Nebulin 33|||Nebulin 34|||Nebulin 35|||Nebulin 36|||Nebulin 37|||Nebulin 38|||Nebulin 39|||Nebulin 4|||Nebulin 40|||Nebulin 41|||Nebulin 42|||Nebulin 43|||Nebulin 44|||Nebulin 45|||Nebulin 46|||Nebulin 47|||Nebulin 48|||Nebulin 49|||Nebulin 5|||Nebulin 50|||Nebulin 51|||Nebulin 52|||Nebulin 53|||Nebulin 54|||Nebulin 55|||Nebulin 56|||Nebulin 57|||Nebulin 58|||Nebulin 59|||Nebulin 6|||Nebulin 60|||Nebulin 61|||Nebulin 62|||Nebulin 63|||Nebulin 64|||Nebulin 65|||Nebulin 66|||Nebulin 67|||Nebulin 68|||Nebulin 69|||Nebulin 7|||Nebulin 70|||Nebulin 71|||Nebulin 72|||Nebulin 73|||Nebulin 74|||Nebulin 75|||Nebulin 76|||Nebulin 77|||Nebulin 78|||Nebulin 79|||Nebulin 8|||Nebulin 80|||Nebulin 81|||Nebulin 82|||Nebulin 83|||Nebulin 84|||Nebulin 85|||Nebulin 86|||Nebulin 87|||Nebulin 88|||Nebulin 89|||Nebulin 9|||Nebulin 90|||Nebulin 91|||Nebulin 92|||Nebulin 93|||Nebulin 94|||Nebulin 95|||Nebulin 96|||Nebulin 97|||Nebulin 98|||Nebulin 99|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096775|||http://purl.uniprot.org/annotation/VAR_021888|||http://purl.uniprot.org/annotation/VAR_024240|||http://purl.uniprot.org/annotation/VAR_047692|||http://purl.uniprot.org/annotation/VAR_047693|||http://purl.uniprot.org/annotation/VAR_047694|||http://purl.uniprot.org/annotation/VAR_047695|||http://purl.uniprot.org/annotation/VAR_047696|||http://purl.uniprot.org/annotation/VAR_047697|||http://purl.uniprot.org/annotation/VAR_047698|||http://purl.uniprot.org/annotation/VAR_047699|||http://purl.uniprot.org/annotation/VAR_047700|||http://purl.uniprot.org/annotation/VAR_047701|||http://purl.uniprot.org/annotation/VAR_047702|||http://purl.uniprot.org/annotation/VAR_047703|||http://purl.uniprot.org/annotation/VAR_047704|||http://purl.uniprot.org/annotation/VAR_047705|||http://purl.uniprot.org/annotation/VAR_047706|||http://purl.uniprot.org/annotation/VAR_047707|||http://purl.uniprot.org/annotation/VAR_047708|||http://purl.uniprot.org/annotation/VAR_047709|||http://purl.uniprot.org/annotation/VAR_056953|||http://purl.uniprot.org/annotation/VAR_056954|||http://purl.uniprot.org/annotation/VAR_085714|||http://purl.uniprot.org/annotation/VAR_085715|||http://purl.uniprot.org/annotation/VAR_085716|||http://purl.uniprot.org/annotation/VSP_054444|||http://purl.uniprot.org/annotation/VSP_054445|||http://purl.uniprot.org/annotation/VSP_054446|||http://purl.uniprot.org/annotation/VSP_054447|||http://purl.uniprot.org/annotation/VSP_054448
http://togogenome.org/gene/9606:TGM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PF1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain                                                                                  ^@                                                                                  Protein-glutamine gamma-glutamyltransferase Z                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213716
http://togogenome.org/gene/9606:ZNF547                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVP9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 547                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047644|||http://purl.uniprot.org/annotation/VSP_016347|||http://purl.uniprot.org/annotation/VSP_016348
http://togogenome.org/gene/9606:ZNF496                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger protein 496                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047617|||http://purl.uniprot.org/annotation/VSP_038755
http://togogenome.org/gene/9606:SLC35F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1Q4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Pro residues|||Solute carrier family 35 member F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307307|||http://purl.uniprot.org/annotation/VSP_057263
http://togogenome.org/gene/9606:ENG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6Y5|||http://purl.uniprot.org/uniprot/F5GX88|||http://purl.uniprot.org/uniprot/P17813|||http://purl.uniprot.org/uniprot/Q5T9B9|||http://purl.uniprot.org/uniprot/Q96CG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Disordered|||Endoglin|||Essential for interaction with GDF2|||Extracellular|||Found in a family with hereditary hemorrhagic talagiectasia; unknown pathological significance.|||Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance.|||Helical|||Impairs protein folding, but does not abolish interaction with GDF2.|||Impairs protein folding. Impairs protein folding; when associated with C-350.|||Impairs protein folding. Impairs protein folding; when associated with C-382.|||In HHT1.|||In HHT1; impairs protein folding; abolishes expression at the cell surface.|||In HHT1; impairs protein folding; nearly abolishes expression at the cell surface.|||In HHT1; impairs protein folding; strongly reduces expression at the cell surface.|||In isoform Short.|||Interchain|||Loss of dimerization via ZP domain.|||Loss of interaction with ARRB2.|||Loss of interaction with GDF2.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with GDF2.|||OR1, C-terminal part|||OR1, N-terminal part|||OR2|||Phosphoserine; by TGFBR1|||Polar residues|||Required for interaction with GDF2|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021156|||http://purl.uniprot.org/annotation/PRO_5010140462|||http://purl.uniprot.org/annotation/PRO_5014312584|||http://purl.uniprot.org/annotation/VAR_005192|||http://purl.uniprot.org/annotation/VAR_005193|||http://purl.uniprot.org/annotation/VAR_005194|||http://purl.uniprot.org/annotation/VAR_005195|||http://purl.uniprot.org/annotation/VAR_005196|||http://purl.uniprot.org/annotation/VAR_005197|||http://purl.uniprot.org/annotation/VAR_009120|||http://purl.uniprot.org/annotation/VAR_009121|||http://purl.uniprot.org/annotation/VAR_014764|||http://purl.uniprot.org/annotation/VAR_026774|||http://purl.uniprot.org/annotation/VAR_026775|||http://purl.uniprot.org/annotation/VAR_026776|||http://purl.uniprot.org/annotation/VAR_026777|||http://purl.uniprot.org/annotation/VAR_026778|||http://purl.uniprot.org/annotation/VAR_026779|||http://purl.uniprot.org/annotation/VAR_026780|||http://purl.uniprot.org/annotation/VAR_026781|||http://purl.uniprot.org/annotation/VAR_026782|||http://purl.uniprot.org/annotation/VAR_026783|||http://purl.uniprot.org/annotation/VAR_037140|||http://purl.uniprot.org/annotation/VAR_070279|||http://purl.uniprot.org/annotation/VAR_070280|||http://purl.uniprot.org/annotation/VAR_070281|||http://purl.uniprot.org/annotation/VAR_070282|||http://purl.uniprot.org/annotation/VAR_070283|||http://purl.uniprot.org/annotation/VAR_070284|||http://purl.uniprot.org/annotation/VAR_070285|||http://purl.uniprot.org/annotation/VAR_070286|||http://purl.uniprot.org/annotation/VAR_070287|||http://purl.uniprot.org/annotation/VAR_070288|||http://purl.uniprot.org/annotation/VAR_070289|||http://purl.uniprot.org/annotation/VAR_070290|||http://purl.uniprot.org/annotation/VAR_070291|||http://purl.uniprot.org/annotation/VAR_070292|||http://purl.uniprot.org/annotation/VAR_070293|||http://purl.uniprot.org/annotation/VAR_070294|||http://purl.uniprot.org/annotation/VAR_070295|||http://purl.uniprot.org/annotation/VAR_070296|||http://purl.uniprot.org/annotation/VAR_070297|||http://purl.uniprot.org/annotation/VAR_070298|||http://purl.uniprot.org/annotation/VAR_070299|||http://purl.uniprot.org/annotation/VAR_070300|||http://purl.uniprot.org/annotation/VAR_070301|||http://purl.uniprot.org/annotation/VAR_070302|||http://purl.uniprot.org/annotation/VAR_070303|||http://purl.uniprot.org/annotation/VAR_070304|||http://purl.uniprot.org/annotation/VAR_070305|||http://purl.uniprot.org/annotation/VAR_070306|||http://purl.uniprot.org/annotation/VAR_070307|||http://purl.uniprot.org/annotation/VSP_004233
http://togogenome.org/gene/9606:PHF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Interaction with SIN3A|||PBR|||PHD finger protein 12|||PHD-type 1|||PHD-type 2; atypical|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059302|||http://purl.uniprot.org/annotation/VSP_051767|||http://purl.uniprot.org/annotation/VSP_051768|||http://purl.uniprot.org/annotation/VSP_051769|||http://purl.uniprot.org/annotation/VSP_051770|||http://purl.uniprot.org/annotation/VSP_051771|||http://purl.uniprot.org/annotation/VSP_051772
http://togogenome.org/gene/9606:MARK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V2E3|||http://purl.uniprot.org/uniprot/A0A7I2V3B9|||http://purl.uniprot.org/uniprot/A0A7I2V639|||http://purl.uniprot.org/uniprot/A0A7I2YQF7|||http://purl.uniprot.org/uniprot/H0YNV4|||http://purl.uniprot.org/uniprot/P27448|||http://purl.uniprot.org/uniprot/Q86U11                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In VIPB.|||In isoform 2 and isoform 6.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||KA1|||MAP/microtubule affinity-regulating kinase 3|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Phosphothreonine; by PKC/PRKCZ|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086304|||http://purl.uniprot.org/annotation/VAR_040765|||http://purl.uniprot.org/annotation/VAR_046763|||http://purl.uniprot.org/annotation/VAR_080189|||http://purl.uniprot.org/annotation/VAR_080778|||http://purl.uniprot.org/annotation/VSP_004943|||http://purl.uniprot.org/annotation/VSP_004944|||http://purl.uniprot.org/annotation/VSP_004945|||http://purl.uniprot.org/annotation/VSP_041582|||http://purl.uniprot.org/annotation/VSP_043197|||http://purl.uniprot.org/annotation/VSP_043198
http://togogenome.org/gene/9606:SLC16A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect subcellular localization. Abolishes tryptophan import activity.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Monocarboxylate transporter 10|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314253|||http://purl.uniprot.org/annotation/VAR_037874
http://togogenome.org/gene/9606:SCRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VDG4|||http://purl.uniprot.org/uniprot/Q0VDG5                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Secernin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262559|||http://purl.uniprot.org/annotation/VAR_034487|||http://purl.uniprot.org/annotation/VAR_053611|||http://purl.uniprot.org/annotation/VAR_069467|||http://purl.uniprot.org/annotation/VSP_042720
http://togogenome.org/gene/9606:C17orf75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||Protein Njmu-R1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096865
http://togogenome.org/gene/9606:NGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0M8W9|||http://purl.uniprot.org/uniprot/Q9NPG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Turn                                                                                  ^@                                                                                  Globin|||Globin family profile|||Neuroglobin|||Redox-active|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053390
http://togogenome.org/gene/9606:C4orf19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein C4orf19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286561|||http://purl.uniprot.org/annotation/VAR_032118|||http://purl.uniprot.org/annotation/VAR_032119|||http://purl.uniprot.org/annotation/VAR_050770
http://togogenome.org/gene/9606:WDR36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI36                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In GLC1G.|||In GLC1G; unknown pathological significance.|||In GLC1G; unknown pathological significance; requires 2 nucleotide substitutions.|||Phosphoserine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051386|||http://purl.uniprot.org/annotation/VAR_024700|||http://purl.uniprot.org/annotation/VAR_025963|||http://purl.uniprot.org/annotation/VAR_025964|||http://purl.uniprot.org/annotation/VAR_025965|||http://purl.uniprot.org/annotation/VAR_025966|||http://purl.uniprot.org/annotation/VAR_025967|||http://purl.uniprot.org/annotation/VAR_025968|||http://purl.uniprot.org/annotation/VAR_025969|||http://purl.uniprot.org/annotation/VAR_025970|||http://purl.uniprot.org/annotation/VAR_053430|||http://purl.uniprot.org/annotation/VAR_077608|||http://purl.uniprot.org/annotation/VAR_077609|||http://purl.uniprot.org/annotation/VAR_077610|||http://purl.uniprot.org/annotation/VAR_077611|||http://purl.uniprot.org/annotation/VAR_077612|||http://purl.uniprot.org/annotation/VAR_077613|||http://purl.uniprot.org/annotation/VAR_077614|||http://purl.uniprot.org/annotation/VAR_077615
http://togogenome.org/gene/9606:SRSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01130|||http://purl.uniprot.org/uniprot/Q53FN0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Serine/arginine-rich splicing factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081918|||http://purl.uniprot.org/annotation/VSP_056153
http://togogenome.org/gene/9606:STOML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BST3|||http://purl.uniprot.org/uniprot/Q53HB6|||http://purl.uniprot.org/uniprot/Q9UBI4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Band 7|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor for type III membrane protein|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Plasma membrane localization.|||SCP2|||Stomatin-like protein 1|||Tyrosine-type lysosomal sorting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094029|||http://purl.uniprot.org/annotation/VSP_012654|||http://purl.uniprot.org/annotation/VSP_054648|||http://purl.uniprot.org/annotation/VSP_054649|||http://purl.uniprot.org/annotation/VSP_054650
http://togogenome.org/gene/9606:ARHGEF35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Rho guanine nucleotide exchange factor 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348462
http://togogenome.org/gene/9606:CCDC74B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LY2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 74B|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274375|||http://purl.uniprot.org/annotation/VAR_030269|||http://purl.uniprot.org/annotation/VAR_030270|||http://purl.uniprot.org/annotation/VSP_022730
http://togogenome.org/gene/9606:LYG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1E2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Lysozyme g-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012023
http://togogenome.org/gene/9606:PRKG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJM3|||http://purl.uniprot.org/uniprot/B4DLF9|||http://purl.uniprot.org/uniprot/B7ZA25|||http://purl.uniprot.org/uniprot/Q13237                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Cyclic nucleotide-binding|||Disordered|||In AMD4; decreased protein abundance; unable to phosphorylate RAF1 in response to FGF2 and to inhibit FGF2-induced MAPK signaling; unable to suppress SOX9-induced COL2A1 expression; unable to upregulate COL10A1.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Reduces cGMP binding affinity; when associated with A-412.|||Reduces cGMP binding affinity; when associated with A-415.|||Removed|||cGMP-binding, high affinity; cAMP-binding, low affinity|||cGMP-binding, high affinity; cAMP-binding, moderate affinity|||cGMP-dependent protein kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086123|||http://purl.uniprot.org/annotation/VAR_040608|||http://purl.uniprot.org/annotation/VAR_040609|||http://purl.uniprot.org/annotation/VAR_051633|||http://purl.uniprot.org/annotation/VAR_086537|||http://purl.uniprot.org/annotation/VSP_055121
http://togogenome.org/gene/9606:HYLS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M11                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Centriolar and ciliogenesis-associated protein HYLS1|||In HLS1; altered subcellular localization, becomes localized to nuclear structures.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284925|||http://purl.uniprot.org/annotation/VAR_031866|||http://purl.uniprot.org/annotation/VAR_031867
http://togogenome.org/gene/9606:HABP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JVS0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases sumoylation; when associated with R-213 or R-276. Abolishes sumoylation; when associated with R-213 and R-276.|||Decreases sumoylation; when associated with R-336. Abolishes sumoylation; when associated with R-213 and R-336.|||Decreases sumoylation; when associated with R-336. Abolishes sumoylation; when associated with R-276 and R-336.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Intracellular hyaluronan-binding protein 4|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257972|||http://purl.uniprot.org/annotation/VSP_052194
http://togogenome.org/gene/9606:GCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5QJB7|||http://purl.uniprot.org/uniprot/B3KR21|||http://purl.uniprot.org/uniprot/Q8IWJ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreases RAB6A binding affinity by 2-fold. Strongly decreases RAB9A binding affinity. Strongly decreases RAB6A or RAB9A binding affinity and abolishes Golgi localization; when associated with A-1588.|||Disordered|||GRIP|||GRIP and coiled-coil domain-containing protein 2|||In isoform 2.|||Mediates interaction with RAB6A|||Mediates interaction with RAB9A|||N-acetylmethionine|||No effect on interaction with RAB6A and RAB9A.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Slightly decreases RAB6A binding affinity. Decreases RAB9A binding affinity by 2-fold. Strongly decreases RAB6A or RAB9A binding affinity and abolishes Golgi localization; when associated with A-1595.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190074|||http://purl.uniprot.org/annotation/VAR_016101|||http://purl.uniprot.org/annotation/VAR_046635|||http://purl.uniprot.org/annotation/VSP_040106|||http://purl.uniprot.org/annotation/VSP_040107
http://togogenome.org/gene/9606:BRPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bromo|||Bromodomain and PHD finger-containing protein 3|||C2HC pre-PHD-type|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PWWP|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211188|||http://purl.uniprot.org/annotation/VAR_048431|||http://purl.uniprot.org/annotation/VAR_061042|||http://purl.uniprot.org/annotation/VSP_055549|||http://purl.uniprot.org/annotation/VSP_055550
http://togogenome.org/gene/9606:ACBD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5Q0|||http://purl.uniprot.org/uniprot/A0A0S2Z5W7|||http://purl.uniprot.org/uniprot/A0A0S2Z5Y4|||http://purl.uniprot.org/uniprot/B4DJP3|||http://purl.uniprot.org/uniprot/K7EM05|||http://purl.uniprot.org/uniprot/Q8NC06                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  ACB|||Acyl-CoA-binding domain-containing protein 4|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214032|||http://purl.uniprot.org/annotation/VAR_055478|||http://purl.uniprot.org/annotation/VAR_059109|||http://purl.uniprot.org/annotation/VSP_014088|||http://purl.uniprot.org/annotation/VSP_014089|||http://purl.uniprot.org/annotation/VSP_014090
http://togogenome.org/gene/9606:RTKN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||REM-1|||Rhotekin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309326|||http://purl.uniprot.org/annotation/VAR_050516|||http://purl.uniprot.org/annotation/VAR_050517|||http://purl.uniprot.org/annotation/VSP_029135|||http://purl.uniprot.org/annotation/VSP_029136|||http://purl.uniprot.org/annotation/VSP_029137|||http://purl.uniprot.org/annotation/VSP_029138|||http://purl.uniprot.org/annotation/VSP_029139
http://togogenome.org/gene/9606:RPS4Y1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22090                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  S4 RNA-binding|||Small ribosomal subunit protein eS4, Y isoform 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130812
http://togogenome.org/gene/9606:OR5T1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVL6|||http://purl.uniprot.org/uniprot/Q8NG75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5T1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150613|||http://purl.uniprot.org/annotation/VAR_034233|||http://purl.uniprot.org/annotation/VAR_053210
http://togogenome.org/gene/9606:YIPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ENM8|||http://purl.uniprot.org/uniprot/Q9BWQ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||Polar residues|||Protein YIPF2|||Removed|||Yip1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000241454
http://togogenome.org/gene/9606:NHLRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z658|||http://purl.uniprot.org/uniprot/Q8NBF2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In FINCA; unknown pathological significance; decreases protein stability.|||In isoform 2.|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||NHL repeat-containing protein 2|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313808|||http://purl.uniprot.org/annotation/VAR_037749|||http://purl.uniprot.org/annotation/VAR_081171|||http://purl.uniprot.org/annotation/VSP_030153
http://togogenome.org/gene/9606:ARL5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y689                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 5A|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207467|||http://purl.uniprot.org/annotation/VSP_041017
http://togogenome.org/gene/9606:GSTP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09211|||http://purl.uniprot.org/uniprot/V9HWE9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase P|||In allele GSTP1*B and allele GSTP1*C.|||In allele GSTP1*C.|||N6-acetyllysine|||N6-succinyllysine|||Phosphothreonine|||Phosphotyrosine; by EGFR|||Reduces affinity for glutathione. Slightly reduced catalytic activity.|||Reduces catalytic activity about 50-fold.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185900|||http://purl.uniprot.org/annotation/VAR_014499|||http://purl.uniprot.org/annotation/VAR_014500|||http://purl.uniprot.org/annotation/VAR_049493
http://togogenome.org/gene/9606:CYP2C8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10632                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2C8|||In allele CYP2C8*10; reduces enzymatic activity with paclitaxel as substrate; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In allele CYP2C8*12; increases enzymatic activity with paclitaxel as substrate; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In allele CYP2C8*13; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In allele CYP2C8*14; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel.|||In allele CYP2C8*2; only found in African-Americans; increases intrinsic clearance of paclitaxel; decreases affinity for amodiaquine; increases enzymatic activity with amodiaquine as substrate.|||In allele CYP2C8*3; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate.|||In allele CYP2C8*4; reduces enzymatic activity with paclitaxel as substrate; decreases affinity for amodiaquine.|||In allele CYP2C8*6; no effect on affinity or enzymatic activity with paclitaxel as substrate; decreases affinity for amodiaquine; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In allele CYP2C8*8; increases affinity for paclitaxel; reduces enzymatic activity with paclitaxel as substrate; decreases intrinsic clearance of paclitaxel; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In allele CYP2C8*9; increases enzymatic activity with paclitaxel as substrate; reduces enzymatic activity with amodiaquine as substrate; decreases intrinsic clearance of amodiaquine.|||In isoform 2.|||Phosphoserine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051699|||http://purl.uniprot.org/annotation/VAR_001250|||http://purl.uniprot.org/annotation/VAR_001251|||http://purl.uniprot.org/annotation/VAR_001252|||http://purl.uniprot.org/annotation/VAR_001253|||http://purl.uniprot.org/annotation/VAR_011754|||http://purl.uniprot.org/annotation/VAR_012238|||http://purl.uniprot.org/annotation/VAR_012239|||http://purl.uniprot.org/annotation/VAR_012240|||http://purl.uniprot.org/annotation/VAR_016947|||http://purl.uniprot.org/annotation/VAR_018958|||http://purl.uniprot.org/annotation/VAR_075541|||http://purl.uniprot.org/annotation/VAR_075542|||http://purl.uniprot.org/annotation/VAR_075543|||http://purl.uniprot.org/annotation/VAR_075544|||http://purl.uniprot.org/annotation/VAR_075545|||http://purl.uniprot.org/annotation/VAR_075546|||http://purl.uniprot.org/annotation/VAR_075547|||http://purl.uniprot.org/annotation/VSP_043306|||http://purl.uniprot.org/annotation/VSP_043307
http://togogenome.org/gene/9606:ODF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J8Z1C3|||http://purl.uniprot.org/uniprot/B3KSD5|||http://purl.uniprot.org/uniprot/B4DUU0|||http://purl.uniprot.org/uniprot/B4DX03|||http://purl.uniprot.org/uniprot/B4DX85|||http://purl.uniprot.org/uniprot/Q5BJF6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 10.|||In isoform 2, isoform 3, isoform 5 and isoform 8.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 9.|||In isoform 5, isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Outer dense fiber protein 2|||Phosphoserine|||Phosphoserine; by TSSK4|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299455|||http://purl.uniprot.org/annotation/VAR_034821|||http://purl.uniprot.org/annotation/VSP_027665|||http://purl.uniprot.org/annotation/VSP_027666|||http://purl.uniprot.org/annotation/VSP_027667|||http://purl.uniprot.org/annotation/VSP_027668|||http://purl.uniprot.org/annotation/VSP_027669|||http://purl.uniprot.org/annotation/VSP_042070|||http://purl.uniprot.org/annotation/VSP_042071|||http://purl.uniprot.org/annotation/VSP_042072|||http://purl.uniprot.org/annotation/VSP_044946
http://togogenome.org/gene/9606:PDS5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTI5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||Basic and acidic residues|||Disordered|||HEAT|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sister chromatid cohesion protein PDS5 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287424|||http://purl.uniprot.org/annotation/VSP_052396|||http://purl.uniprot.org/annotation/VSP_052397|||http://purl.uniprot.org/annotation/VSP_052398|||http://purl.uniprot.org/annotation/VSP_052399|||http://purl.uniprot.org/annotation/VSP_052400|||http://purl.uniprot.org/annotation/VSP_052401|||http://purl.uniprot.org/annotation/VSP_052402
http://togogenome.org/gene/9606:PDIK1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N165                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PDIK1L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086494
http://togogenome.org/gene/9606:ABCA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N139                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 6|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250672|||http://purl.uniprot.org/annotation/VAR_027576|||http://purl.uniprot.org/annotation/VAR_027577|||http://purl.uniprot.org/annotation/VAR_027578|||http://purl.uniprot.org/annotation/VAR_027579|||http://purl.uniprot.org/annotation/VAR_027580|||http://purl.uniprot.org/annotation/VSP_020695|||http://purl.uniprot.org/annotation/VSP_020696|||http://purl.uniprot.org/annotation/VSP_020697|||http://purl.uniprot.org/annotation/VSP_020698
http://togogenome.org/gene/9606:UBA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZZ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to activate UFM1.|||Abolished interaction with UFM1 and GABARAPL2.|||Abolished interaction with UFM1 and decreased interaction with GABARAPL2.|||Abolished interaction with UFM1.|||Decreased interaction with UFM1 without affecting interaction with GABARAPL2.|||Forms a stable intermediate complex.|||Glycyl thioester intermediate|||Impaired ability to activate UFM1 via a trans-binding mechanism.|||Impaired ability to activate UFM1.|||Impaired homodimerization and ability to activate UFM1 via a trans-binding mechanism.|||In DEE44; abolishes UFM1 activating enzyme activity.|||In DEE44; no effect on UFM1 activating enzyme activity.|||In DEE44; reduces UFM1 activating enzyme activity.|||In DEE44; reduces UFM1 activating enzyme activity; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation.|||In DEE44; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation.|||In SCAR24; delocalizes protein to the nucleus; activates degradation through the ubiquitin proteasome pathway; decreases protein stability; disrupts interaction with UFM1.|||In SCAR24; does not affect cytoplasm localization; decreases protein stability; does not affect interaction with UFM1.|||In isoform 2.|||Phosphoserine|||UFM1-interacting sequence (UIS)|||Ubiquitin-like modifier-activating enzyme 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194970|||http://purl.uniprot.org/annotation/VAR_077153|||http://purl.uniprot.org/annotation/VAR_077154|||http://purl.uniprot.org/annotation/VAR_077155|||http://purl.uniprot.org/annotation/VAR_077156|||http://purl.uniprot.org/annotation/VAR_077157|||http://purl.uniprot.org/annotation/VAR_077158|||http://purl.uniprot.org/annotation/VAR_077159|||http://purl.uniprot.org/annotation/VAR_080409|||http://purl.uniprot.org/annotation/VSP_038528
http://togogenome.org/gene/9606:AQP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55064                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aquaporin-5|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||In PPKB; retains the ability to traffic to the cell membrane.|||Increased location at the cell membrane.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||No effect on location at the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063951|||http://purl.uniprot.org/annotation/VAR_070442|||http://purl.uniprot.org/annotation/VAR_070443|||http://purl.uniprot.org/annotation/VAR_070444|||http://purl.uniprot.org/annotation/VAR_070445|||http://purl.uniprot.org/annotation/VAR_070446
http://togogenome.org/gene/9606:PLOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60568|||http://purl.uniprot.org/uniprot/Q9UG85                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Accessory region|||Decreased lysyl hydroxylase activity and loss of glycosyltransferase activity.|||Decreased lysyl hydroxylase and glycosyltransferase activity.|||Fe2OG dioxygenase|||Important for dimerization|||In BCARD; generates a new glycosylation site; decreases protein stability; strongly decreases lysyl hydroxylase activity and nearly abolishes glycosyltransferase activity.|||In BCARD; unknown pathological significance.|||Loss of dimerization. Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity.|||Loss of dimerization. Loss of lysyl hydroxylase activity and no effect on glycosyltransferase activity.|||Loss of glucosyltransferase activity. Loss of galactosyltransferase activity.|||Loss of lysyl hydroxylase activity and decreased glycosyltransferase activity.|||Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3|||N-linked (GlcNAc...) asparagine|||Nearly abolishes glucosyltransferase activity. Nearly abolishes galactosyltransferase activity.|||No effect on dimerization, lysyl hydroxylase and glycosyltransferase activity.|||Reduced glucosyltransferase activity.|||Required for glycosyltransferase activity|||Strongly decreased lysyl hydroxylase activity. No effect on glycosyltransferase activity.|||Strongly reduced glucosyltransferase activity. Strongly reduced galactosyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024686|||http://purl.uniprot.org/annotation/VAR_012075|||http://purl.uniprot.org/annotation/VAR_051708|||http://purl.uniprot.org/annotation/VAR_054913|||http://purl.uniprot.org/annotation/VAR_082150
http://togogenome.org/gene/9606:MIDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504T8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Midnolin|||Polar residues|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287536
http://togogenome.org/gene/9606:TCTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57738                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||T-cell leukemia translocation-altered gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072470
http://togogenome.org/gene/9606:CPAMD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0S9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Kazal-like|||Polar residues|||Pro residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:CBS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2D6|||http://purl.uniprot.org/uniprot/P35520|||http://purl.uniprot.org/uniprot/Q9NTF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Associated with 1/3 to 2/3 the enzyme activity of the wild-type.|||Basic and acidic residues|||CBS|||Cystathionine beta-synthase|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In CBSD.|||In CBSD; 4% of activity; stable.|||In CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation.|||In CBSD; common mutation in Irish population; loss of activity.|||In CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates.|||In CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation.|||In CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation.|||In CBSD; decreased cystathionine beta-synthase activity; increased aggregation.|||In CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation.|||In CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation.|||In CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; has 36% of wild-type enzyme activity.|||In CBSD; has significantly decreased levels of enzyme activity.|||In CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; linked with C-369.|||In CBSD; linked with Q-125; loss of activity.|||In CBSD; linked with S-307.|||In CBSD; linked with V-114; 18% of activity.|||In CBSD; loss of activity.|||In CBSD; loss of cystathionine beta-synthase activity.|||In CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation.|||In CBSD; loss of expression.|||In CBSD; mild form.|||In CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability.|||In CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure.|||In CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates.|||In CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates.|||In CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure.|||In CBSD; moderate form.|||In CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation.|||In CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity.|||In CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet.|||In CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation.|||In CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation.|||In CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation.|||In CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure.|||In CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure.|||In CBSD; protein expression is comparable to wild-type; loss of activity.|||In CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure.|||In CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity.|||In CBSD; severe form.|||In CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates.|||In CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation.|||In CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation.|||In CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure.|||Reduced heme content and cystathionine beta-synthase activity.|||axial binding residue ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167133|||http://purl.uniprot.org/annotation/VAR_002171|||http://purl.uniprot.org/annotation/VAR_002172|||http://purl.uniprot.org/annotation/VAR_002173|||http://purl.uniprot.org/annotation/VAR_002174|||http://purl.uniprot.org/annotation/VAR_002175|||http://purl.uniprot.org/annotation/VAR_002176|||http://purl.uniprot.org/annotation/VAR_002177|||http://purl.uniprot.org/annotation/VAR_002178|||http://purl.uniprot.org/annotation/VAR_002179|||http://purl.uniprot.org/annotation/VAR_002180|||http://purl.uniprot.org/annotation/VAR_002181|||http://purl.uniprot.org/annotation/VAR_002182|||http://purl.uniprot.org/annotation/VAR_002183|||http://purl.uniprot.org/annotation/VAR_002184|||http://purl.uniprot.org/annotation/VAR_002185|||http://purl.uniprot.org/annotation/VAR_002186|||http://purl.uniprot.org/annotation/VAR_002187|||http://purl.uniprot.org/annotation/VAR_002188|||http://purl.uniprot.org/annotation/VAR_002189|||http://purl.uniprot.org/annotation/VAR_002190|||http://purl.uniprot.org/annotation/VAR_002191|||http://purl.uniprot.org/annotation/VAR_002192|||http://purl.uniprot.org/annotation/VAR_002193|||http://purl.uniprot.org/annotation/VAR_002194|||http://purl.uniprot.org/annotation/VAR_008049|||http://purl.uniprot.org/annotation/VAR_008050|||http://purl.uniprot.org/annotation/VAR_008051|||http://purl.uniprot.org/annotation/VAR_008052|||http://purl.uniprot.org/annotation/VAR_008053|||http://purl.uniprot.org/annotation/VAR_008054|||http://purl.uniprot.org/annotation/VAR_008055|||http://purl.uniprot.org/annotation/VAR_008056|||http://purl.uniprot.org/annotation/VAR_008057|||http://purl.uniprot.org/annotation/VAR_008058|||http://purl.uniprot.org/annotation/VAR_008059|||http://purl.uniprot.org/annotation/VAR_008060|||http://purl.uniprot.org/annotation/VAR_008061|||http://purl.uniprot.org/annotation/VAR_008062|||http://purl.uniprot.org/annotation/VAR_008063|||http://purl.uniprot.org/annotation/VAR_008064|||http://purl.uniprot.org/annotation/VAR_008065|||http://purl.uniprot.org/annotation/VAR_008066|||http://purl.uniprot.org/annotation/VAR_008067|||http://purl.uniprot.org/annotation/VAR_008068|||http://purl.uniprot.org/annotation/VAR_008069|||http://purl.uniprot.org/annotation/VAR_008070|||http://purl.uniprot.org/annotation/VAR_008071|||http://purl.uniprot.org/annotation/VAR_008072|||http://purl.uniprot.org/annotation/VAR_008073|||http://purl.uniprot.org/annotation/VAR_008074|||http://purl.uniprot.org/annotation/VAR_008075|||http://purl.uniprot.org/annotation/VAR_008076|||http://purl.uniprot.org/annotation/VAR_008077|||http://purl.uniprot.org/annotation/VAR_008078|||http://purl.uniprot.org/annotation/VAR_008079|||http://purl.uniprot.org/annotation/VAR_008080|||http://purl.uniprot.org/annotation/VAR_008081|||http://purl.uniprot.org/annotation/VAR_008082|||http://purl.uniprot.org/annotation/VAR_008083|||http://purl.uniprot.org/annotation/VAR_008084|||http://purl.uniprot.org/annotation/VAR_008085|||http://purl.uniprot.org/annotation/VAR_008086|||http://purl.uniprot.org/annotation/VAR_008087|||http://purl.uniprot.org/annotation/VAR_008088|||http://purl.uniprot.org/annotation/VAR_008089|||http://purl.uniprot.org/annotation/VAR_008090|||http://purl.uniprot.org/annotation/VAR_008091|||http://purl.uniprot.org/annotation/VAR_008092|||http://purl.uniprot.org/annotation/VAR_008093|||http://purl.uniprot.org/annotation/VAR_021790|||http://purl.uniprot.org/annotation/VAR_021791|||http://purl.uniprot.org/annotation/VAR_021792|||http://purl.uniprot.org/annotation/VAR_021793|||http://purl.uniprot.org/annotation/VAR_021794|||http://purl.uniprot.org/annotation/VAR_021795|||http://purl.uniprot.org/annotation/VAR_021796|||http://purl.uniprot.org/annotation/VAR_021797|||http://purl.uniprot.org/annotation/VAR_021798|||http://purl.uniprot.org/annotation/VAR_021799|||http://purl.uniprot.org/annotation/VAR_021800|||http://purl.uniprot.org/annotation/VAR_021801|||http://purl.uniprot.org/annotation/VAR_021802|||http://purl.uniprot.org/annotation/VAR_021803|||http://purl.uniprot.org/annotation/VAR_046921|||http://purl.uniprot.org/annotation/VAR_046922|||http://purl.uniprot.org/annotation/VAR_046923|||http://purl.uniprot.org/annotation/VAR_046924|||http://purl.uniprot.org/annotation/VAR_046925|||http://purl.uniprot.org/annotation/VAR_046926|||http://purl.uniprot.org/annotation/VAR_046927|||http://purl.uniprot.org/annotation/VAR_046928|||http://purl.uniprot.org/annotation/VAR_046929|||http://purl.uniprot.org/annotation/VAR_046930|||http://purl.uniprot.org/annotation/VAR_046931|||http://purl.uniprot.org/annotation/VAR_046932|||http://purl.uniprot.org/annotation/VAR_046933|||http://purl.uniprot.org/annotation/VAR_046934|||http://purl.uniprot.org/annotation/VAR_046935|||http://purl.uniprot.org/annotation/VAR_046936|||http://purl.uniprot.org/annotation/VAR_046937|||http://purl.uniprot.org/annotation/VAR_046938|||http://purl.uniprot.org/annotation/VAR_066098|||http://purl.uniprot.org/annotation/VAR_066099|||http://purl.uniprot.org/annotation/VAR_066100|||http://purl.uniprot.org/annotation/VAR_066101|||http://purl.uniprot.org/annotation/VAR_066102|||http://purl.uniprot.org/annotation/VAR_066103|||http://purl.uniprot.org/annotation/VAR_074590|||http://purl.uniprot.org/annotation/VAR_074591|||http://purl.uniprot.org/annotation/VAR_074592|||http://purl.uniprot.org/annotation/VAR_074593|||http://purl.uniprot.org/annotation/VAR_074594|||http://purl.uniprot.org/annotation/VAR_074595|||http://purl.uniprot.org/annotation/VSP_001217
http://togogenome.org/gene/9606:MAMSTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||MEF2-activating motif and SAP domain-containing transcriptional regulator|||MEF2-binding|||Polar residues|||Pro residues|||SAP|||Transcription activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319981|||http://purl.uniprot.org/annotation/VSP_031554|||http://purl.uniprot.org/annotation/VSP_031555
http://togogenome.org/gene/9606:RNPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4A4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Aminopeptidase B|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Removed|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095088|||http://purl.uniprot.org/annotation/VAR_051566
http://togogenome.org/gene/9606:SERPINE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07093                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glia-derived nexin|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032504|||http://purl.uniprot.org/annotation/VAR_036027|||http://purl.uniprot.org/annotation/VAR_051955|||http://purl.uniprot.org/annotation/VSP_038367|||http://purl.uniprot.org/annotation/VSP_043668
http://togogenome.org/gene/9606:ATG2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Autophagy-related protein 2 homolog B|||Chorein N-terminal|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Strongly reduced interaction with WDR45/WIPI4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089909|||http://purl.uniprot.org/annotation/VAR_021523|||http://purl.uniprot.org/annotation/VAR_023096|||http://purl.uniprot.org/annotation/VAR_045956
http://togogenome.org/gene/9606:SSUH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2M2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 1.|||In isoform 3.|||Probable disease-associated variant found in patients with dentin dysplasia; decreased protein abundance; no effect on nuclear localization.|||Protein SSUH2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260082|||http://purl.uniprot.org/annotation/VAR_033659|||http://purl.uniprot.org/annotation/VAR_078099|||http://purl.uniprot.org/annotation/VSP_061237|||http://purl.uniprot.org/annotation/VSP_061238
http://togogenome.org/gene/9606:PTH1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03431|||http://purl.uniprot.org/uniprot/Q0VGD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes hormone binding and homodimerization.|||Abolishes hormone binding. No effect on homodimerization.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for interaction with G proteins|||In BOCD.|||In MCDJ.|||In MCDJ; constitutively activated.|||In MCDJ; constitutively activated; constitutively increases adenylate cyclase-activating G-protein coupled receptor signaling pathway; decreases the degree of N-glycosylation; does not affect homodimerization.|||In MCDJ; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant.|||N-linked (GlcNAc...) asparagine|||Parathyroid hormone/parathyroid hormone-related peptide receptor|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012845|||http://purl.uniprot.org/annotation/PRO_5004178874|||http://purl.uniprot.org/annotation/VAR_003582|||http://purl.uniprot.org/annotation/VAR_003583|||http://purl.uniprot.org/annotation/VAR_016062|||http://purl.uniprot.org/annotation/VAR_016063|||http://purl.uniprot.org/annotation/VAR_016064|||http://purl.uniprot.org/annotation/VAR_038811
http://togogenome.org/gene/9606:MYF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13349                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In EORVA; decreased transcriptional activity and impaired nuclear localization.|||Myogenic factor 5|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127344|||http://purl.uniprot.org/annotation/VAR_081557
http://togogenome.org/gene/9606:KDM4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6B0I6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||JmjC|||JmjN|||Lysine-specific demethylase 4D|||Polar residues|||PolyADP-ribosyl glutamic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234376|||http://purl.uniprot.org/annotation/VAR_026225|||http://purl.uniprot.org/annotation/VAR_057882|||http://purl.uniprot.org/annotation/VAR_057883
http://togogenome.org/gene/9606:CMBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DG6                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  70% inhibition of enzymatic activity.|||97% inhibition of enzymatic activity.|||Carboxymethylenebutenolidase homolog|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308188|||http://purl.uniprot.org/annotation/VAR_036751
http://togogenome.org/gene/9606:TM4SF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14894                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disrupts arginine-binding.|||Extracellular|||Helical|||Interaction with MTOR and CASTOR1|||N-linked (GlcNAc...) asparagine|||Transmembrane 4 L6 family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219303
http://togogenome.org/gene/9606:RPL26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61254                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL24|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130787
http://togogenome.org/gene/9606:GNAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19087|||http://purl.uniprot.org/uniprot/Q5T697                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||Basic and acidic residues|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(t) subunit alpha-2|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203740|||http://purl.uniprot.org/annotation/VAR_014783|||http://purl.uniprot.org/annotation/VAR_047623|||http://purl.uniprot.org/annotation/VAR_047624
http://togogenome.org/gene/9606:KCNAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43448                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Voltage-gated potassium channel subunit beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148750
http://togogenome.org/gene/9606:ETV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ERX2|||http://purl.uniprot.org/uniprot/O00321|||http://purl.uniprot.org/uniprot/Q3KNT2                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ETS|||ETS translocation variant 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204112|||http://purl.uniprot.org/annotation/VAR_071062|||http://purl.uniprot.org/annotation/VSP_055488
http://togogenome.org/gene/9606:RPP30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78346                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Ribonuclease P protein subunit p30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140031|||http://purl.uniprot.org/annotation/VAR_051870|||http://purl.uniprot.org/annotation/VSP_045673
http://togogenome.org/gene/9606:OR52A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWD2|||http://purl.uniprot.org/uniprot/Q9H2C5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150766
http://togogenome.org/gene/9606:OXCT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYC2                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  5-glutamyl coenzyme A thioester intermediate|||Mitochondrion|||Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002416|||http://purl.uniprot.org/annotation/VAR_059134|||http://purl.uniprot.org/annotation/VAR_059135
http://togogenome.org/gene/9606:ZNF569                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ELU1|||http://purl.uniprot.org/uniprot/Q5MCW4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 569                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047659|||http://purl.uniprot.org/annotation/VAR_035589|||http://purl.uniprot.org/annotation/VAR_035590|||http://purl.uniprot.org/annotation/VSP_055966
http://togogenome.org/gene/9606:PGAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15259                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  In GSD10.|||Phosphoglycerate mutase 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179829|||http://purl.uniprot.org/annotation/VAR_006088|||http://purl.uniprot.org/annotation/VAR_006089|||http://purl.uniprot.org/annotation/VAR_013103
http://togogenome.org/gene/9606:CD300LB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4G0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with TYROBP, and strongly reduces activation properties.|||CMRF35-like molecule 7|||Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Interaction with TYROBP|||No effect on interaction with TYROBP, but strongly reduces activation properties.|||Phosphotyrosine; by FYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320130
http://togogenome.org/gene/9606:DAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAW0|||http://purl.uniprot.org/uniprot/P98082                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SH3KBP1.|||Basic and acidic residues|||DPF 1|||DPF 2|||Disabled homolog 2|||Disordered|||Greatly reduced binding to MYO6.|||Impairs TGF-beta receptor signaling, no effect on interaction with SMAD2.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||PID|||Phosphoserine|||Phosphoserine; in mitosis|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||Required for interaction with CSK|||Required for interaction with GRB2 and CSK|||Required for interaction with MYO6|||Required for localization to clathrin-coated pits|||Sufficient for interaction with GRB2|||Sufficient for interaction with SH3KBP1 SH3 domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079770|||http://purl.uniprot.org/annotation/VAR_031705|||http://purl.uniprot.org/annotation/VAR_050942|||http://purl.uniprot.org/annotation/VSP_004181|||http://purl.uniprot.org/annotation/VSP_038401
http://togogenome.org/gene/9606:USP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8N5|||http://purl.uniprot.org/uniprot/P40818                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with spastic paraplegia; unknown pathological significance.|||Impairs deubiquitination activity and leads to endosome membrane accumulation.|||In PITA4; somatic mutation; unknown pathological significance.|||In PITA4; somatic mutation; unknown pathological significance; localizes to nucleus instead of cytoplasm.|||In isoform 2.|||MIT|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proton acceptor|||Rhodanese|||SH3-binding|||USP|||Ubiquitin carboxyl-terminal hydrolase 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080627|||http://purl.uniprot.org/annotation/VAR_017796|||http://purl.uniprot.org/annotation/VAR_017797|||http://purl.uniprot.org/annotation/VAR_051525|||http://purl.uniprot.org/annotation/VAR_077850|||http://purl.uniprot.org/annotation/VAR_079717|||http://purl.uniprot.org/annotation/VAR_079718|||http://purl.uniprot.org/annotation/VAR_079719|||http://purl.uniprot.org/annotation/VAR_079720|||http://purl.uniprot.org/annotation/VAR_079721|||http://purl.uniprot.org/annotation/VSP_054594|||http://purl.uniprot.org/annotation/VSP_054595
http://togogenome.org/gene/9606:ATF7IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNI7|||http://purl.uniprot.org/uniprot/B3KQF8|||http://purl.uniprot.org/uniprot/Q6VMQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with MBD1 and subsequent transcriptional repression.|||Abolishes the interaction with SUMO.|||Activating transcription factor 7-interacting protein 1|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Interaction with MBD1|||Interaction with SETDB1|||Interaction with SUMO|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281780|||http://purl.uniprot.org/annotation/VAR_031283|||http://purl.uniprot.org/annotation/VAR_031284|||http://purl.uniprot.org/annotation/VAR_031285|||http://purl.uniprot.org/annotation/VSP_024035|||http://purl.uniprot.org/annotation/VSP_024038|||http://purl.uniprot.org/annotation/VSP_024039|||http://purl.uniprot.org/annotation/VSP_055912
http://togogenome.org/gene/9606:SLC22A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSA0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-63.|||No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-99.|||No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-63 and Q-99.|||No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface location; when associated with Q-56; Q-63 and Q-99.|||Reduced cell surface expression and estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-52; A-83; A-305 and A-469.|||Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-305 and A-469.|||Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-83 and A-469.|||Slightly reduced estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-52; A-83 and A-305.|||Slightly reduced estrone 3-sulfate transport. Reduced cell surface expression and estrone 3-sulfate transport; when associated with A-47; A-83; A-305 and A-469.|||Solute carrier family 22 member 11|||Strongly reduced cell surface expression and estrone 3-sulfate transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234435|||http://purl.uniprot.org/annotation/VAR_053962|||http://purl.uniprot.org/annotation/VSP_018319
http://togogenome.org/gene/9606:PITPNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48739                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Loss of phosphatidylcholine transfer activity but no effect on phosphatidylinositol transfer activity. Not inhibited by N-ethylmaleimide. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells.|||Loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells.|||Loss of phosphatidylinositol transfer activity. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells.|||N6-acetyllysine|||No effect on phosphatidylinositol transfer activity.|||Phosphatidylinositol transfer protein beta isoform|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191643|||http://purl.uniprot.org/annotation/VSP_012762|||http://purl.uniprot.org/annotation/VSP_055132
http://togogenome.org/gene/9606:ZNF816-ZNF321P                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0X1KG74|||http://purl.uniprot.org/uniprot/Q8N8H1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  KRAB|||Putative protein ZNF321                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294249
http://togogenome.org/gene/9606:SPANXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS26                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||Sperm protein associated with the nucleus on the X chromosome A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189549
http://togogenome.org/gene/9606:EIF4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60842                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEAD box|||Disordered|||Eukaryotic initiation factor 4A-I|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054933|||http://purl.uniprot.org/annotation/VSP_046032
http://togogenome.org/gene/9606:CADPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM57|||http://purl.uniprot.org/uniprot/Q86UW7|||http://purl.uniprot.org/uniprot/X5DNG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||C2|||Calcium-dependent secretion activator 2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with DRD2|||MHD1|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053868|||http://purl.uniprot.org/annotation/VAR_024786|||http://purl.uniprot.org/annotation/VSP_016815|||http://purl.uniprot.org/annotation/VSP_016816|||http://purl.uniprot.org/annotation/VSP_016817|||http://purl.uniprot.org/annotation/VSP_016818
http://togogenome.org/gene/9606:COX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00395|||http://purl.uniprot.org/uniprot/U5YWV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1'-histidyl-3'-tyrosine (His-Tyr)|||Cytochrome c oxidase subunit 1|||Cytochrome oxidase subunit I profile|||Found in two patients with acquired idiopathic sideroblastic anemia.|||Helical|||Helical; Name=I|||Helical; Name=II|||Helical; Name=III|||Helical; Name=IV|||Helical; Name=IX|||Helical; Name=V|||Helical; Name=VI|||Helical; Name=VII|||Helical; Name=VIII|||Helical; Name=X|||Helical; Name=XI|||Helical; Name=XII|||In CRC; displays steady-state catalytic activity linked to proton pumping that is approximately 34% of wild-type; an intrinsic proton leak is find in the enzyme, which will lead to decreased overall energy-conversion efficiency of the respiratory chain, perturbing transport processes such as protein, ion and metabolite trafficking.|||In CRC; the mutant is probably not expressed, indicating that the amino acid substitution results in a severely altered overall structure of the enzyme.|||In LHON; secondary mutation; does not seem to directly cause the disease.|||In MT-C4D.|||In MT-C4D; significant decrease in enzyme activity.|||Mitochondrial intermembrane|||Mitochondrial matrix|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183345|||http://purl.uniprot.org/annotation/VAR_008385|||http://purl.uniprot.org/annotation/VAR_008386|||http://purl.uniprot.org/annotation/VAR_008387|||http://purl.uniprot.org/annotation/VAR_008566|||http://purl.uniprot.org/annotation/VAR_008567|||http://purl.uniprot.org/annotation/VAR_008568|||http://purl.uniprot.org/annotation/VAR_008569|||http://purl.uniprot.org/annotation/VAR_008570|||http://purl.uniprot.org/annotation/VAR_011342|||http://purl.uniprot.org/annotation/VAR_011343|||http://purl.uniprot.org/annotation/VAR_033055|||http://purl.uniprot.org/annotation/VAR_033056|||http://purl.uniprot.org/annotation/VAR_064154|||http://purl.uniprot.org/annotation/VAR_064155
http://togogenome.org/gene/9606:MEIS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YNA8|||http://purl.uniprot.org/uniprot/Q49A38|||http://purl.uniprot.org/uniprot/Q99687                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Meis3|||Homeobox; TALE-type|||In isoform 2.|||In isoform 3.|||MEIS N-terminal|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049110|||http://purl.uniprot.org/annotation/PRO_5003546239|||http://purl.uniprot.org/annotation/VSP_012892|||http://purl.uniprot.org/annotation/VSP_012893
http://togogenome.org/gene/9606:SPATA32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282906|||http://purl.uniprot.org/annotation/VAR_060279
http://togogenome.org/gene/9606:SRRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK53|||http://purl.uniprot.org/uniprot/Q9UQ35                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Serine/arginine repetitive matrix protein 2|||Spt5 C-terminal|||Sufficient for RNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248154|||http://purl.uniprot.org/annotation/VAR_027259|||http://purl.uniprot.org/annotation/VAR_027260|||http://purl.uniprot.org/annotation/VAR_048868|||http://purl.uniprot.org/annotation/VSP_020184|||http://purl.uniprot.org/annotation/VSP_020185|||http://purl.uniprot.org/annotation/VSP_020186|||http://purl.uniprot.org/annotation/VSP_020187
http://togogenome.org/gene/9606:SMIM12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L0R6D7|||http://purl.uniprot.org/uniprot/Q96EX1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299478
http://togogenome.org/gene/9606:TNNI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19429|||http://purl.uniprot.org/uniprot/Q6FGX2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Disordered|||In CMD1FF.|||In CMD2A.|||In CMH7 and RCM1.|||In CMH7.|||In RCM1.|||Involved in TNI-TNT interactions|||Involved in binding TNC|||Involved in binding TNC and actin|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PAK3|||Phosphoserine; by PKA and PKD/PRKD1|||Phosphoserine; by PKC/PRKCE|||Phosphothreonine|||Phosphothreonine; by STK4/MST1|||Phosphotyrosine|||Removed|||Risk factor for CMH7.|||Troponin I, cardiac muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186151|||http://purl.uniprot.org/annotation/VAR_007603|||http://purl.uniprot.org/annotation/VAR_007604|||http://purl.uniprot.org/annotation/VAR_016078|||http://purl.uniprot.org/annotation/VAR_016079|||http://purl.uniprot.org/annotation/VAR_016080|||http://purl.uniprot.org/annotation/VAR_016081|||http://purl.uniprot.org/annotation/VAR_016082|||http://purl.uniprot.org/annotation/VAR_016083|||http://purl.uniprot.org/annotation/VAR_016084|||http://purl.uniprot.org/annotation/VAR_016085|||http://purl.uniprot.org/annotation/VAR_019872|||http://purl.uniprot.org/annotation/VAR_019873|||http://purl.uniprot.org/annotation/VAR_019874|||http://purl.uniprot.org/annotation/VAR_019875|||http://purl.uniprot.org/annotation/VAR_019876|||http://purl.uniprot.org/annotation/VAR_029453|||http://purl.uniprot.org/annotation/VAR_029454|||http://purl.uniprot.org/annotation/VAR_042745|||http://purl.uniprot.org/annotation/VAR_042746|||http://purl.uniprot.org/annotation/VAR_043989|||http://purl.uniprot.org/annotation/VAR_063548|||http://purl.uniprot.org/annotation/VAR_063549|||http://purl.uniprot.org/annotation/VAR_067264
http://togogenome.org/gene/9606:NAA80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IAP1|||http://purl.uniprot.org/uniprot/Q93015                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In NAA80mut; abolished acetyltransferase activity; when associated with F-83, D-151 and F-183.|||In NAA80mut; abolished acetyltransferase activity; when associated with F-83, Q-148 and D-151.|||In NAA80mut; abolished acetyltransferase activity; when associated with F-83, Q-148 and F-183.|||In NAA80mut; abolished acetyltransferase activity; when associated with Q-148, D-151 and F-183.|||In isoform 2.|||In non-small cell lung cancer cell lines.|||N-acetyltransferase|||N-alpha-acetyltransferase 80|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074536|||http://purl.uniprot.org/annotation/VAR_014224|||http://purl.uniprot.org/annotation/VAR_014225|||http://purl.uniprot.org/annotation/VSP_037187
http://togogenome.org/gene/9606:CGB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQP8|||http://purl.uniprot.org/uniprot/P0DN86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Choriogonadotropin subunit beta 3|||Disordered|||Glycoprotein hormone subunit beta|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Pro residues|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000042|||http://purl.uniprot.org/annotation/CAR_000043|||http://purl.uniprot.org/annotation/PRO_0000011676|||http://purl.uniprot.org/annotation/PRO_5014227020|||http://purl.uniprot.org/annotation/VAR_003188|||http://purl.uniprot.org/annotation/VAR_014585|||http://purl.uniprot.org/annotation/VAR_014586|||http://purl.uniprot.org/annotation/VAR_014587|||http://purl.uniprot.org/annotation/VAR_015231|||http://purl.uniprot.org/annotation/VAR_015232|||http://purl.uniprot.org/annotation/VAR_015233|||http://purl.uniprot.org/annotation/VAR_015234|||http://purl.uniprot.org/annotation/VAR_015235|||http://purl.uniprot.org/annotation/VSP_038396
http://togogenome.org/gene/9606:SCGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76038                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||Secretagogin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073636|||http://purl.uniprot.org/annotation/VAR_042710
http://togogenome.org/gene/9606:CAMLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49069                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to GET3.|||Cytoplasmic|||Disordered|||Guided entry of tail-anchored proteins factor CAMLG|||Helical|||Lumenal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089291|||http://purl.uniprot.org/annotation/VAR_024297|||http://purl.uniprot.org/annotation/VAR_050710
http://togogenome.org/gene/9606:SYT17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BN78|||http://purl.uniprot.org/uniprot/H3BRH9|||http://purl.uniprot.org/uniprot/Q9BSW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Disordered|||Phosphoserine|||Polar residues|||Synaptotagmin-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311936
http://togogenome.org/gene/9606:NDUFS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00217                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||In MC1DN2.|||In MC1DN2; decrease in enzyme activity; impaired assembly of complex I.|||In MC1DN2; unknown pathological significance.|||In MC1DN2; unknown pathological significance; decrease in enzyme activity; impaired assembly of complex I.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020012|||http://purl.uniprot.org/annotation/VAR_019538|||http://purl.uniprot.org/annotation/VAR_019539|||http://purl.uniprot.org/annotation/VAR_081440|||http://purl.uniprot.org/annotation/VAR_081441|||http://purl.uniprot.org/annotation/VAR_081442|||http://purl.uniprot.org/annotation/VAR_081443|||http://purl.uniprot.org/annotation/VAR_081444|||http://purl.uniprot.org/annotation/VAR_083603
http://togogenome.org/gene/9606:TRIB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMM9|||http://purl.uniprot.org/uniprot/J3KR25|||http://purl.uniprot.org/uniprot/Q96RU7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||Interaction with DDIT3/CHOP|||Phosphoserine|||Protein kinase|||Tribbles homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131866|||http://purl.uniprot.org/annotation/VAR_023965|||http://purl.uniprot.org/annotation/VAR_042372|||http://purl.uniprot.org/annotation/VAR_042373|||http://purl.uniprot.org/annotation/VAR_042374|||http://purl.uniprot.org/annotation/VAR_042375
http://togogenome.org/gene/9606:CT47A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:ABHD14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IU4|||http://purl.uniprot.org/uniprot/V9HW87                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  AB hydrolase-1|||Abolished protein-lysine deacetylase activity in vitro.|||Charge relay system|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Putative protein-lysine deacylase ABHD14B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065038|||http://purl.uniprot.org/annotation/VSP_008058
http://togogenome.org/gene/9606:C2orf68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7T9J5|||http://purl.uniprot.org/uniprot/Q2NKX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||UPF0561 protein C2orf68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328785|||http://purl.uniprot.org/annotation/VSP_032792|||http://purl.uniprot.org/annotation/VSP_032793
http://togogenome.org/gene/9606:IARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSE4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Found in a patient with Leigh syndrome; unknown pathological significance.|||In CAGSSS; unknown pathological significance.|||Isoleucine--tRNA ligase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233335|||http://purl.uniprot.org/annotation/VAR_034526|||http://purl.uniprot.org/annotation/VAR_059862|||http://purl.uniprot.org/annotation/VAR_072590|||http://purl.uniprot.org/annotation/VAR_072591|||http://purl.uniprot.org/annotation/VAR_083400|||http://purl.uniprot.org/annotation/VAR_083401|||http://purl.uniprot.org/annotation/VAR_083402|||http://purl.uniprot.org/annotation/VAR_083403|||http://purl.uniprot.org/annotation/VAR_083404|||http://purl.uniprot.org/annotation/VAR_084826|||http://purl.uniprot.org/annotation/VAR_084827|||http://purl.uniprot.org/annotation/VAR_084828
http://togogenome.org/gene/9606:UTS2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Urotensin-2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070193|||http://purl.uniprot.org/annotation/VAR_035768|||http://purl.uniprot.org/annotation/VAR_049451
http://togogenome.org/gene/9606:SLCO3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIG8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kazal-like|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Solute carrier organic anion transporter family member 3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191064|||http://purl.uniprot.org/annotation/VAR_054853|||http://purl.uniprot.org/annotation/VSP_036833|||http://purl.uniprot.org/annotation/VSP_036834|||http://purl.uniprot.org/annotation/VSP_036835|||http://purl.uniprot.org/annotation/VSP_036836|||http://purl.uniprot.org/annotation/VSP_036837|||http://purl.uniprot.org/annotation/VSP_036838
http://togogenome.org/gene/9606:CHRNA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C4IXS7|||http://purl.uniprot.org/uniprot/Q9GZZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  11-fold increase in inhibition of the AChR composed of subunits CHRNA9 and CHRNA10 by the conotoxin GEXXA, and no change in activity on mAChR composed of subunits CHRNA9 and CHRNA10 by the competitive conotoxin Vc1A.|||Associated with receptor activation|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-10|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000376|||http://purl.uniprot.org/annotation/VAR_048172
http://togogenome.org/gene/9606:LAMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13473                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||First lumenal domain|||Helical|||Hinge|||Impairs binding and subsequent lysosomal degradation of target proteins, such as GAPDH.|||Important for binding and subsequent lysosomal degradation of target proteins|||In DAND.|||In isoform LAMP-2B.|||In isoform LAMP-2C.|||Lumenal|||Lysosome-associated membrane glycoprotein 2|||N-linked (GlcNAc...) (polylactosaminoglycan) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Second lumenal domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017110|||http://purl.uniprot.org/annotation/VAR_011992|||http://purl.uniprot.org/annotation/VAR_026230|||http://purl.uniprot.org/annotation/VSP_003044|||http://purl.uniprot.org/annotation/VSP_042519
http://togogenome.org/gene/9606:HS3ST3B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y662                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 3B1|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085219
http://togogenome.org/gene/9606:ADAMTS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQW6|||http://purl.uniprot.org/uniprot/Q59FE5|||http://purl.uniprot.org/uniprot/Q6ZN14|||http://purl.uniprot.org/uniprot/Q9H324                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 10|||ADAMTS/ADAMTS-like Spacer 1|||ADAMTS/ADAMTS-like cysteine-rich|||Disintegrin|||Disordered|||In WMS1; shows consistent and significantly diminished protein secretion.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029184|||http://purl.uniprot.org/annotation/PRO_0000029185|||http://purl.uniprot.org/annotation/PRO_5014015964|||http://purl.uniprot.org/annotation/VAR_054439|||http://purl.uniprot.org/annotation/VAR_054440|||http://purl.uniprot.org/annotation/VAR_054441|||http://purl.uniprot.org/annotation/VSP_054707
http://togogenome.org/gene/9606:WIPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJZ9|||http://purl.uniprot.org/uniprot/O43516|||http://purl.uniprot.org/uniprot/Q2YDC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Binds actin|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||WAS/WASL-interacting protein family member 1|||WH2|||XRSGPXPPXP motif 1|||XRSGPXPPXP motif 2|||XRSGPXPPXP motif 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065941|||http://purl.uniprot.org/annotation/VAR_010295|||http://purl.uniprot.org/annotation/VAR_046526|||http://purl.uniprot.org/annotation/VSP_012964|||http://purl.uniprot.org/annotation/VSP_012965|||http://purl.uniprot.org/annotation/VSP_012966
http://togogenome.org/gene/9606:FCRL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DN72                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fc receptor-like protein 6|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphorylation implicated in interaction with PTPN11. Loss of interaction with PTPN11, PTPN6 and INPPL1.|||N-linked (GlcNAc...) asparagine|||No change of phosphorylation implicated in interaction with PTPN11. Loss of interaction with INPPD5, INPPL1 and GRB2.|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280213|||http://purl.uniprot.org/annotation/VAR_031090|||http://purl.uniprot.org/annotation/VSP_023565|||http://purl.uniprot.org/annotation/VSP_023566|||http://purl.uniprot.org/annotation/VSP_023567|||http://purl.uniprot.org/annotation/VSP_023568|||http://purl.uniprot.org/annotation/VSP_023569|||http://purl.uniprot.org/annotation/VSP_023570
http://togogenome.org/gene/9606:SMAD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DB7|||http://purl.uniprot.org/uniprot/Q99717                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Disordered|||Loss of phosphorylation and interaction with SMAD4.|||MH1|||MH2|||Mothers against decapentaplegic homolog 5|||N-acetylthreonine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090865
http://togogenome.org/gene/9606:KNDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HHZ0|||http://purl.uniprot.org/uniprot/A0A804HID6|||http://purl.uniprot.org/uniprot/A0A804HIZ4|||http://purl.uniprot.org/uniprot/Q76NI1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||KIND|||KIND 1|||KIND 2|||Kinase non-catalytic C-lobe domain-containing protein 1|||N-terminal Ras-GEF|||Phosphoserine|||Polar residues|||Pro residues|||Ras-GEF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307141|||http://purl.uniprot.org/annotation/VAR_035358|||http://purl.uniprot.org/annotation/VAR_035359|||http://purl.uniprot.org/annotation/VAR_035360|||http://purl.uniprot.org/annotation/VAR_051902|||http://purl.uniprot.org/annotation/VAR_061786|||http://purl.uniprot.org/annotation/VSP_028595|||http://purl.uniprot.org/annotation/VSP_028598
http://togogenome.org/gene/9606:POPDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues|||Popeye domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046793|||http://purl.uniprot.org/annotation/VAR_053601|||http://purl.uniprot.org/annotation/VSP_008743
http://togogenome.org/gene/9606:TRHDE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKU6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Thyrotropin-releasing hormone-degrading ectoenzyme|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095118
http://togogenome.org/gene/9606:EXOSC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQT5|||http://purl.uniprot.org/uniprot/Q9NYS3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exosome complex component RRP40|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In PCH1B.|||In isoform 2.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087131|||http://purl.uniprot.org/annotation/VAR_054098|||http://purl.uniprot.org/annotation/VAR_068505|||http://purl.uniprot.org/annotation/VAR_068506|||http://purl.uniprot.org/annotation/VAR_068507|||http://purl.uniprot.org/annotation/VAR_068508|||http://purl.uniprot.org/annotation/VAR_074169|||http://purl.uniprot.org/annotation/VSP_043457
http://togogenome.org/gene/9606:ZWILCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H900                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Protein zwilch homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314800|||http://purl.uniprot.org/annotation/VAR_038055|||http://purl.uniprot.org/annotation/VSP_030365
http://togogenome.org/gene/9606:CCNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG0|||http://purl.uniprot.org/uniprot/P78396                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-A1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080333|||http://purl.uniprot.org/annotation/VSP_034392|||http://purl.uniprot.org/annotation/VSP_044257
http://togogenome.org/gene/9606:TAAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1P5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070146|||http://purl.uniprot.org/annotation/VSP_016301
http://togogenome.org/gene/9606:RAP1GAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TL16|||http://purl.uniprot.org/uniprot/Q684P5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes GAP activity.|||Abolishes phosphorylation by PKG/PRKG1.|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKG/PRKG1; in vitro|||Phosphothreonine|||Polar residues|||Rap-GAP|||Rap1 GTPase-activating protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312716|||http://purl.uniprot.org/annotation/VAR_037553|||http://purl.uniprot.org/annotation/VSP_029888|||http://purl.uniprot.org/annotation/VSP_029889
http://togogenome.org/gene/9606:DHFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  DHFR|||Dihydrofolate reductase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186368|||http://purl.uniprot.org/annotation/VAR_061135
http://togogenome.org/gene/9606:ATP6V0D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8Y2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  V-type proton ATPase subunit d 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285657|||http://purl.uniprot.org/annotation/VAR_032039|||http://purl.uniprot.org/annotation/VAR_032040
http://togogenome.org/gene/9606:FAM83A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Protein FAM83A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286813|||http://purl.uniprot.org/annotation/VAR_032178|||http://purl.uniprot.org/annotation/VSP_025187|||http://purl.uniprot.org/annotation/VSP_025188|||http://purl.uniprot.org/annotation/VSP_025189|||http://purl.uniprot.org/annotation/VSP_025190|||http://purl.uniprot.org/annotation/VSP_025191
http://togogenome.org/gene/9606:MTA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6RRE2|||http://purl.uniprot.org/uniprot/Q9BTC8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BAH|||Disordered|||ELM2|||GATA-type; atypical|||In isoform 2.|||Metastasis-associated protein MTA3|||Phosphoserine|||Phosphothreonine|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083498|||http://purl.uniprot.org/annotation/VSP_001603|||http://purl.uniprot.org/annotation/VSP_001604
http://togogenome.org/gene/9606:GCSH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23434                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Glycine cleavage system H protein, mitochondrial|||Lipoyl-binding|||Mitochondrion|||N6-lipoyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010723|||http://purl.uniprot.org/annotation/VAR_018846|||http://purl.uniprot.org/annotation/VAR_018847
http://togogenome.org/gene/9606:CNTROB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N137                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrobin|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Pro residues|||Required for centrosome localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076240|||http://purl.uniprot.org/annotation/VAR_024787|||http://purl.uniprot.org/annotation/VAR_050877|||http://purl.uniprot.org/annotation/VSP_016836|||http://purl.uniprot.org/annotation/VSP_016837|||http://purl.uniprot.org/annotation/VSP_016838|||http://purl.uniprot.org/annotation/VSP_016839|||http://purl.uniprot.org/annotation/VSP_016840|||http://purl.uniprot.org/annotation/VSP_016841
http://togogenome.org/gene/9606:NPTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y639                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like 1|||Ig-like 2|||Ig-like 3|||In isoform 1 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Narpin; mediates binding with FGFR1 and has antidepressant-like activity|||Neuroplastin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394470|||http://purl.uniprot.org/annotation/VSP_039251|||http://purl.uniprot.org/annotation/VSP_039252|||http://purl.uniprot.org/annotation/VSP_039253
http://togogenome.org/gene/9606:LRRC40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9A6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 40|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226257|||http://purl.uniprot.org/annotation/VAR_034088|||http://purl.uniprot.org/annotation/VAR_034089
http://togogenome.org/gene/9606:PLA2G1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04054                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Phospholipase A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022739|||http://purl.uniprot.org/annotation/PRO_0000022740|||http://purl.uniprot.org/annotation/VAR_011911|||http://purl.uniprot.org/annotation/VAR_011912|||http://purl.uniprot.org/annotation/VAR_011913
http://togogenome.org/gene/9606:TPSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Helical|||In allele gamma-II.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Tryptase gamma|||Tryptase gamma heavy chain|||Tryptase gamma light chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027498|||http://purl.uniprot.org/annotation/PRO_0000027499|||http://purl.uniprot.org/annotation/PRO_0000027500|||http://purl.uniprot.org/annotation/VAR_012097|||http://purl.uniprot.org/annotation/VAR_012098|||http://purl.uniprot.org/annotation/VAR_012099|||http://purl.uniprot.org/annotation/VAR_012100|||http://purl.uniprot.org/annotation/VAR_012101|||http://purl.uniprot.org/annotation/VAR_025012|||http://purl.uniprot.org/annotation/VAR_061773
http://togogenome.org/gene/9606:PTCHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NR3|||http://purl.uniprot.org/uniprot/X5DNX9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a patient with intellectual disability; unknown pathological significance.|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 1|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280040|||http://purl.uniprot.org/annotation/VAR_064872|||http://purl.uniprot.org/annotation/VAR_064873|||http://purl.uniprot.org/annotation/VAR_064874|||http://purl.uniprot.org/annotation/VAR_064875|||http://purl.uniprot.org/annotation/VAR_064876|||http://purl.uniprot.org/annotation/VAR_064877|||http://purl.uniprot.org/annotation/VAR_064878|||http://purl.uniprot.org/annotation/VAR_064879|||http://purl.uniprot.org/annotation/VAR_064880|||http://purl.uniprot.org/annotation/VAR_075876|||http://purl.uniprot.org/annotation/VAR_075877|||http://purl.uniprot.org/annotation/VAR_075878|||http://purl.uniprot.org/annotation/VSP_023511|||http://purl.uniprot.org/annotation/VSP_023512|||http://purl.uniprot.org/annotation/VSP_023513
http://togogenome.org/gene/9606:COL6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5H7|||http://purl.uniprot.org/uniprot/P12109                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||C-terminal globular domain|||Cell attachment site|||Collagen alpha-1(VI) chain|||Disordered|||In BTHLM1 and UCMD1.|||In BTHLM1.|||In UCMD1.|||In UCMD1; fibroblasts with the mutation assembled and secreted normal collagen VI microfibrils; cell adhesion of heterozygous Arg-284 fibroblasts is markedly decreased but can be rescued by the addition of normal collagen VI.|||N-linked (GlcNAc...) asparagine|||N-terminal globular domain|||Probable disease-associated variant found in a patient with limb-girdle muscular dystrophy.|||Triple-helical region|||VWFA|||VWFA 1|||VWFA 2|||VWFA 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005758|||http://purl.uniprot.org/annotation/PRO_5036334048|||http://purl.uniprot.org/annotation/VAR_013580|||http://purl.uniprot.org/annotation/VAR_013581|||http://purl.uniprot.org/annotation/VAR_013582|||http://purl.uniprot.org/annotation/VAR_048763|||http://purl.uniprot.org/annotation/VAR_048764|||http://purl.uniprot.org/annotation/VAR_058213|||http://purl.uniprot.org/annotation/VAR_058214|||http://purl.uniprot.org/annotation/VAR_058215|||http://purl.uniprot.org/annotation/VAR_058216|||http://purl.uniprot.org/annotation/VAR_058217|||http://purl.uniprot.org/annotation/VAR_058218|||http://purl.uniprot.org/annotation/VAR_058219|||http://purl.uniprot.org/annotation/VAR_058220|||http://purl.uniprot.org/annotation/VAR_058221|||http://purl.uniprot.org/annotation/VAR_058222|||http://purl.uniprot.org/annotation/VAR_058223|||http://purl.uniprot.org/annotation/VAR_058224|||http://purl.uniprot.org/annotation/VAR_081097
http://togogenome.org/gene/9606:TRMT9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P272                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a child with sporadic epilepsy; unknown pathological significance.|||In isoform 2.|||Phosphoserine|||Probable tRNA methyltransferase 9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328792|||http://purl.uniprot.org/annotation/VAR_056243|||http://purl.uniprot.org/annotation/VAR_056244|||http://purl.uniprot.org/annotation/VAR_056245|||http://purl.uniprot.org/annotation/VAR_061378|||http://purl.uniprot.org/annotation/VAR_061379|||http://purl.uniprot.org/annotation/VAR_061380|||http://purl.uniprot.org/annotation/VAR_061381|||http://purl.uniprot.org/annotation/VAR_077832|||http://purl.uniprot.org/annotation/VSP_059378|||http://purl.uniprot.org/annotation/VSP_059379
http://togogenome.org/gene/9606:AMOTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY63                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Angiomotin-like protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190670|||http://purl.uniprot.org/annotation/VAR_033498|||http://purl.uniprot.org/annotation/VSP_015710
http://togogenome.org/gene/9606:SGCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4P5|||http://purl.uniprot.org/uniprot/A0A2R8Y5J3|||http://purl.uniprot.org/uniprot/A0A2R8YGQ3|||http://purl.uniprot.org/uniprot/B4DP78|||http://purl.uniprot.org/uniprot/C9JR67|||http://purl.uniprot.org/uniprot/E9PEH6|||http://purl.uniprot.org/uniprot/O43556                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dystroglycan-type cadherin-like|||Epsilon-sarcoglycan|||Extracellular|||Helical|||In DYT11.|||In DYT11; affects protein stability; the mutant undergoes endoplasmic reticulum-associated degradation.|||In DYT11; results in gain-of-glycosylation; the mutant is targeted to the plasma membrane at reduced levels compared to wild-type.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031677|||http://purl.uniprot.org/annotation/VAR_026750|||http://purl.uniprot.org/annotation/VAR_058088|||http://purl.uniprot.org/annotation/VAR_058089|||http://purl.uniprot.org/annotation/VAR_066732|||http://purl.uniprot.org/annotation/VAR_066733|||http://purl.uniprot.org/annotation/VAR_066734|||http://purl.uniprot.org/annotation/VAR_066735|||http://purl.uniprot.org/annotation/VAR_066736|||http://purl.uniprot.org/annotation/VAR_066737|||http://purl.uniprot.org/annotation/VAR_066738|||http://purl.uniprot.org/annotation/VAR_066739|||http://purl.uniprot.org/annotation/VAR_066740|||http://purl.uniprot.org/annotation/VAR_066741|||http://purl.uniprot.org/annotation/VAR_066742|||http://purl.uniprot.org/annotation/VAR_066743|||http://purl.uniprot.org/annotation/VSP_045092|||http://purl.uniprot.org/annotation/VSP_045093|||http://purl.uniprot.org/annotation/VSP_054079
http://togogenome.org/gene/9606:PPP1R37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75864                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Phosphoserine|||Pro residues|||Protein phosphatase 1 regulatory subunit 37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320939|||http://purl.uniprot.org/annotation/VSP_031754|||http://purl.uniprot.org/annotation/VSP_031755
http://togogenome.org/gene/9606:CLK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAZ1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK4|||Loss of function.|||Phosphoserine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085873|||http://purl.uniprot.org/annotation/VAR_040414|||http://purl.uniprot.org/annotation/VAR_040415
http://togogenome.org/gene/9606:SP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG40                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Phosphoserine|||Transcription factor Sp9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395450
http://togogenome.org/gene/9606:CLASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TRF6|||http://purl.uniprot.org/uniprot/Q7Z460                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CLIP-associating protein 1|||Disordered|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with CLIP2|||Interaction with PHLDB2 and RSN|||Interaction with microtubules, MAPRE1 and MAPRE3|||Localization to kinetochores|||Phosphoserine|||Phosphothreonine|||Polar residues|||TOG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089847|||http://purl.uniprot.org/annotation/VAR_053818|||http://purl.uniprot.org/annotation/VSP_022386|||http://purl.uniprot.org/annotation/VSP_022387|||http://purl.uniprot.org/annotation/VSP_022388|||http://purl.uniprot.org/annotation/VSP_022389|||http://purl.uniprot.org/annotation/VSP_054412|||http://purl.uniprot.org/annotation/VSP_054413|||http://purl.uniprot.org/annotation/VSP_054414|||http://purl.uniprot.org/annotation/VSP_057272
http://togogenome.org/gene/9606:DHRS7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ8|||http://purl.uniprot.org/uniprot/Q6IAN0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dehydrogenase/reductase SDR family member 7B|||Helical|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312105
http://togogenome.org/gene/9606:BDKRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30411                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B2 bradykinin receptor|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by GRK6|||Phosphothreonine|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069190|||http://purl.uniprot.org/annotation/VAR_003457|||http://purl.uniprot.org/annotation/VAR_012284|||http://purl.uniprot.org/annotation/VSP_001865
http://togogenome.org/gene/9606:OR2T4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH00                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150499|||http://purl.uniprot.org/annotation/VAR_062027
http://togogenome.org/gene/9606:NEMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14524                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  A; required for its colocalization with lamins at the nuclear envelope|||B; required for interaction with RAN-GTP|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nuclear envelope integral membrane protein 1|||Phosphoserine|||Required for nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050744|||http://purl.uniprot.org/annotation/VAR_057817|||http://purl.uniprot.org/annotation/VSP_011896
http://togogenome.org/gene/9606:IL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14005|||http://purl.uniprot.org/uniprot/Q9UME6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes proteolytic cleavage.|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interaction with GRIN2A|||Interaction with HTLV-1 tax|||Interaction with PPP1R12A, PPP1R12B and PPP1R12C|||Interleukin-16|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Polar residues|||Pro residues|||Pro-interleukin-16|||Reduces nuclear localization of pro-interleukin-16; when associated with 780-AA-781.|||Reduces nuclear localization of pro-interleukin-16; when associated with 797-AGLANA-802.|||Reduces phosphorylation and nuclear localization.|||Reduces phosphorylation. Enhances nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015412|||http://purl.uniprot.org/annotation/PRO_0000377543|||http://purl.uniprot.org/annotation/VAR_019203|||http://purl.uniprot.org/annotation/VAR_019204|||http://purl.uniprot.org/annotation/VAR_019205|||http://purl.uniprot.org/annotation/VAR_034013|||http://purl.uniprot.org/annotation/VAR_053372|||http://purl.uniprot.org/annotation/VAR_058310|||http://purl.uniprot.org/annotation/VSP_037458|||http://purl.uniprot.org/annotation/VSP_037459|||http://purl.uniprot.org/annotation/VSP_057192
http://togogenome.org/gene/9606:GBP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8V2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  C-terminal tail; required for its localization to cytoplasmic vesicle|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 7|||Interaction with the CYBA-CYBB complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313654|||http://purl.uniprot.org/annotation/VAR_037687|||http://purl.uniprot.org/annotation/VAR_037688
http://togogenome.org/gene/9606:IL26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GUW8|||http://purl.uniprot.org/uniprot/Q9NPH9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Interleukin family protein|||Interleukin-26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015387|||http://purl.uniprot.org/annotation/PRO_5034190431
http://togogenome.org/gene/9606:HJURP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Holliday junction recognition protein|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation by AKT1 and binding to YWHAG.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287433|||http://purl.uniprot.org/annotation/VAR_056912|||http://purl.uniprot.org/annotation/VAR_056913|||http://purl.uniprot.org/annotation/VAR_056914|||http://purl.uniprot.org/annotation/VAR_056915|||http://purl.uniprot.org/annotation/VAR_056916|||http://purl.uniprot.org/annotation/VAR_057946|||http://purl.uniprot.org/annotation/VAR_057947|||http://purl.uniprot.org/annotation/VAR_057948|||http://purl.uniprot.org/annotation/VAR_057949|||http://purl.uniprot.org/annotation/VSP_037467|||http://purl.uniprot.org/annotation/VSP_037468
http://togogenome.org/gene/9606:SPATA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0S9|||http://purl.uniprot.org/uniprot/B4DID4|||http://purl.uniprot.org/uniprot/Q9UM82                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with CYLD.|||Disordered|||PIM motif|||PUB|||Phosphoserine|||Reduced interaction with CYLD.|||Spermatogenesis-associated protein 2|||Strongly reduced interaction with RNF31/HOIP.|||Weak or no effect on interaction with CYLD.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072100|||http://purl.uniprot.org/annotation/VAR_051368
http://togogenome.org/gene/9606:PROCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCQ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Protein PROCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336063|||http://purl.uniprot.org/annotation/VAR_043476|||http://purl.uniprot.org/annotation/VAR_043477|||http://purl.uniprot.org/annotation/VSP_033988|||http://purl.uniprot.org/annotation/VSP_053931|||http://purl.uniprot.org/annotation/VSP_053932
http://togogenome.org/gene/9606:MTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KQR6|||http://purl.uniprot.org/uniprot/A0A8I5KZ76|||http://purl.uniprot.org/uniprot/Q13496                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Disrupts interaction with DES.|||Disrupts interaction with DES. Does not affect lipid phosphatase activity.|||Does not affect interaction with DES.|||GRAM|||In CNMX.|||In CNMX; dramatic decrease in phosphatase activity.|||In CNMX; greatly reduced binding to PI(3,5)P2; abolishes interaction with MTMR12; does not translocate to the late endosome following EGF stimulation; shows normal EGFR degradation.|||In CNMX; mild to moderate; abolishes interaction with DES, but not with MTMR12; reduces MTMR12 protein levels in myotubes.|||In CNMX; mild.|||In CNMX; mild; reduced binding to PI(3,5)P2.|||In CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2; abolishes interaction with MTMR12.|||In CNMX; severe.|||In CNMX; severe; dramatic decrease in phosphatase activity.|||In CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES and MTMR12.|||In CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation.|||In CNMX; severe; loss of activity.|||In CNMX; severe; loss of activity; abolishes interaction with DES and MTMR12.|||In CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES or MTMR12.|||In CNMX; very mild.|||In isoform 2.|||Lacks activity toward PI3P. Does not affect interaction with DES or MTMR12.|||Localizes to plasma membrane extensions. Does not affect interaction with DES.|||Loss of activity.|||Myotubularin|||Myotubularin phosphatase|||No effect on subcellular location.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Produces an unstable protein.|||Reduced response to PI5P.|||Reduces MTMR12 protein levels in myotubes.|||Tyrosine specific protein phosphatases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094930|||http://purl.uniprot.org/annotation/VAR_006386|||http://purl.uniprot.org/annotation/VAR_006387|||http://purl.uniprot.org/annotation/VAR_006388|||http://purl.uniprot.org/annotation/VAR_006389|||http://purl.uniprot.org/annotation/VAR_006390|||http://purl.uniprot.org/annotation/VAR_006391|||http://purl.uniprot.org/annotation/VAR_006392|||http://purl.uniprot.org/annotation/VAR_006393|||http://purl.uniprot.org/annotation/VAR_006394|||http://purl.uniprot.org/annotation/VAR_006395|||http://purl.uniprot.org/annotation/VAR_006396|||http://purl.uniprot.org/annotation/VAR_006397|||http://purl.uniprot.org/annotation/VAR_006398|||http://purl.uniprot.org/annotation/VAR_006399|||http://purl.uniprot.org/annotation/VAR_006400|||http://purl.uniprot.org/annotation/VAR_006401|||http://purl.uniprot.org/annotation/VAR_006402|||http://purl.uniprot.org/annotation/VAR_006403|||http://purl.uniprot.org/annotation/VAR_006404|||http://purl.uniprot.org/annotation/VAR_006405|||http://purl.uniprot.org/annotation/VAR_006406|||http://purl.uniprot.org/annotation/VAR_006407|||http://purl.uniprot.org/annotation/VAR_006408|||http://purl.uniprot.org/annotation/VAR_006409|||http://purl.uniprot.org/annotation/VAR_009217|||http://purl.uniprot.org/annotation/VAR_009218|||http://purl.uniprot.org/annotation/VAR_009219|||http://purl.uniprot.org/annotation/VAR_009220|||http://purl.uniprot.org/annotation/VAR_009221|||http://purl.uniprot.org/annotation/VAR_009222|||http://purl.uniprot.org/annotation/VAR_018227|||http://purl.uniprot.org/annotation/VAR_018228|||http://purl.uniprot.org/annotation/VAR_018229|||http://purl.uniprot.org/annotation/VAR_018230|||http://purl.uniprot.org/annotation/VAR_018231|||http://purl.uniprot.org/annotation/VAR_018232|||http://purl.uniprot.org/annotation/VAR_018233|||http://purl.uniprot.org/annotation/VAR_018234|||http://purl.uniprot.org/annotation/VAR_018235|||http://purl.uniprot.org/annotation/VAR_018236|||http://purl.uniprot.org/annotation/VAR_018237|||http://purl.uniprot.org/annotation/VAR_018238|||http://purl.uniprot.org/annotation/VAR_018239|||http://purl.uniprot.org/annotation/VAR_018240|||http://purl.uniprot.org/annotation/VAR_018241|||http://purl.uniprot.org/annotation/VAR_018242|||http://purl.uniprot.org/annotation/VAR_018243|||http://purl.uniprot.org/annotation/VAR_018244|||http://purl.uniprot.org/annotation/VAR_018245|||http://purl.uniprot.org/annotation/VAR_018246|||http://purl.uniprot.org/annotation/VAR_018247|||http://purl.uniprot.org/annotation/VAR_018248|||http://purl.uniprot.org/annotation/VAR_018249|||http://purl.uniprot.org/annotation/VAR_018250|||http://purl.uniprot.org/annotation/VAR_018251|||http://purl.uniprot.org/annotation/VAR_018252|||http://purl.uniprot.org/annotation/VAR_018253|||http://purl.uniprot.org/annotation/VAR_018254|||http://purl.uniprot.org/annotation/VAR_018255|||http://purl.uniprot.org/annotation/VAR_018256|||http://purl.uniprot.org/annotation/VAR_068846|||http://purl.uniprot.org/annotation/VSP_056208
http://togogenome.org/gene/9606:ZC3H15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type 1|||C3H1-type 2|||Disordered|||In isoform 2.|||Phosphoserine|||Required for interaction with DRG1|||Zinc finger CCCH domain-containing protein 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324642|||http://purl.uniprot.org/annotation/VAR_039867|||http://purl.uniprot.org/annotation/VAR_052969|||http://purl.uniprot.org/annotation/VSP_055992|||http://purl.uniprot.org/annotation/VSP_055993|||http://purl.uniprot.org/annotation/VSP_055994
http://togogenome.org/gene/9606:ECHDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DC8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Enoyl-CoA hydratase domain-containing protein 3, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333215|||http://purl.uniprot.org/annotation/VAR_043126|||http://purl.uniprot.org/annotation/VAR_043127|||http://purl.uniprot.org/annotation/VAR_043128|||http://purl.uniprot.org/annotation/VSP_033491
http://togogenome.org/gene/9606:FBXL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UF56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box/LRR-repeat protein 17|||Impaired ability to bind substrate proteins.|||In isoform 2 and isoform 3.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119865|||http://purl.uniprot.org/annotation/VAR_081000|||http://purl.uniprot.org/annotation/VSP_009476|||http://purl.uniprot.org/annotation/VSP_037034
http://togogenome.org/gene/9606:CEACAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13688|||http://purl.uniprot.org/uniprot/Q3KRG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Carcinoembryonic antigen-related cell adhesion molecule 1|||Cytoplasmic|||Decreases the binding to ANXA2.|||Disordered|||Doesn't affect cell surface expression. Impairs phosphorylation.|||Essential for interaction with PTPN11 and PTPN6|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||Impairs interaction with HAVCR2.|||Impairs phosphorylation; when associated with F-493.|||Impairs phosphorylation; when associated with F-520.|||In isoform 10.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 11.|||In isoform 7.|||In isoform 8, isoform 9 and isoform 11.|||In isoform 9.|||Interaction with FLNA|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by INSR, SRC and LCK|||Phosphotyrosine; by SRC, LCK, INSR and EGFR|||Polar residues|||Pyrrolidone carboxylic acid|||Required for homophilic binding|||Required for interaction with PTPN11 and PTPN6 and for control of phosphorylation level                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014562|||http://purl.uniprot.org/annotation/VAR_049844|||http://purl.uniprot.org/annotation/VAR_049845|||http://purl.uniprot.org/annotation/VAR_049846|||http://purl.uniprot.org/annotation/VAR_049847|||http://purl.uniprot.org/annotation/VSP_002478|||http://purl.uniprot.org/annotation/VSP_002479|||http://purl.uniprot.org/annotation/VSP_002480|||http://purl.uniprot.org/annotation/VSP_002481|||http://purl.uniprot.org/annotation/VSP_002482|||http://purl.uniprot.org/annotation/VSP_002483|||http://purl.uniprot.org/annotation/VSP_009227|||http://purl.uniprot.org/annotation/VSP_010938|||http://purl.uniprot.org/annotation/VSP_012222|||http://purl.uniprot.org/annotation/VSP_040571|||http://purl.uniprot.org/annotation/VSP_040572|||http://purl.uniprot.org/annotation/VSP_040573|||http://purl.uniprot.org/annotation/VSP_040574|||http://purl.uniprot.org/annotation/VSP_040575
http://togogenome.org/gene/9606:TECTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75443                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Alpha-tectorin|||GPI-anchor amidated asparagine|||In DFNA12.|||In DFNA12; postlingual and progressive.|||In DFNA12; prelingual and stable deafness.|||In DFNA12; progressive deafness with late onset.|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||NIDO|||Removed in mature form|||TIL 1|||TIL 2|||TIL 3|||VWFC|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041735|||http://purl.uniprot.org/annotation/PRO_0000041736|||http://purl.uniprot.org/annotation/VAR_018968|||http://purl.uniprot.org/annotation/VAR_018969|||http://purl.uniprot.org/annotation/VAR_018970|||http://purl.uniprot.org/annotation/VAR_018971|||http://purl.uniprot.org/annotation/VAR_018972|||http://purl.uniprot.org/annotation/VAR_018973|||http://purl.uniprot.org/annotation/VAR_018974|||http://purl.uniprot.org/annotation/VAR_018975|||http://purl.uniprot.org/annotation/VAR_018976|||http://purl.uniprot.org/annotation/VAR_018977|||http://purl.uniprot.org/annotation/VAR_018978|||http://purl.uniprot.org/annotation/VAR_036423|||http://purl.uniprot.org/annotation/VAR_036424|||http://purl.uniprot.org/annotation/VAR_036425|||http://purl.uniprot.org/annotation/VAR_057500|||http://purl.uniprot.org/annotation/VAR_057501|||http://purl.uniprot.org/annotation/VAR_059965|||http://purl.uniprot.org/annotation/VAR_066076|||http://purl.uniprot.org/annotation/VAR_066077|||http://purl.uniprot.org/annotation/VAR_066078|||http://purl.uniprot.org/annotation/VAR_066079|||http://purl.uniprot.org/annotation/VAR_066080|||http://purl.uniprot.org/annotation/VAR_066081|||http://purl.uniprot.org/annotation/VAR_066082|||http://purl.uniprot.org/annotation/VAR_066083|||http://purl.uniprot.org/annotation/VAR_066084|||http://purl.uniprot.org/annotation/VAR_066085|||http://purl.uniprot.org/annotation/VAR_066086|||http://purl.uniprot.org/annotation/VAR_066087|||http://purl.uniprot.org/annotation/VAR_066088|||http://purl.uniprot.org/annotation/VAR_066089|||http://purl.uniprot.org/annotation/VAR_066090|||http://purl.uniprot.org/annotation/VAR_066091|||http://purl.uniprot.org/annotation/VAR_066092|||http://purl.uniprot.org/annotation/VAR_066093|||http://purl.uniprot.org/annotation/VAR_066094|||http://purl.uniprot.org/annotation/VAR_066095|||http://purl.uniprot.org/annotation/VAR_066096|||http://purl.uniprot.org/annotation/VAR_066097
http://togogenome.org/gene/9606:UNC5CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H8YHX0|||http://purl.uniprot.org/uniprot/Q8IV45                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||Interaction with RELA and NFKB1|||Peptidase S68|||UNC5C-like protein|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309567|||http://purl.uniprot.org/annotation/VAR_036979
http://togogenome.org/gene/9606:FAM217A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXS0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM217A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089540|||http://purl.uniprot.org/annotation/VAR_023207|||http://purl.uniprot.org/annotation/VAR_056801|||http://purl.uniprot.org/annotation/VAR_056802|||http://purl.uniprot.org/annotation/VAR_056803|||http://purl.uniprot.org/annotation/VAR_056804
http://togogenome.org/gene/9606:OR2T11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH01                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150503|||http://purl.uniprot.org/annotation/VAR_053155|||http://purl.uniprot.org/annotation/VAR_053156
http://togogenome.org/gene/9606:GOLGA8M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BSY2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8M|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420860|||http://purl.uniprot.org/annotation/VSP_044751|||http://purl.uniprot.org/annotation/VSP_044752|||http://purl.uniprot.org/annotation/VSP_044753|||http://purl.uniprot.org/annotation/VSP_044754|||http://purl.uniprot.org/annotation/VSP_053442
http://togogenome.org/gene/9606:RASGRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV60|||http://purl.uniprot.org/uniprot/Q7LDG7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||In BDPLT18.|||In BDPLT18; lack of mutant protein in platelets from a patient homozygous for the mutation.|||In BDPLT18; loss of guanyl-nucleotide exchange factor activity.|||In BDPLT18; prevents Rap1 activation upon calcium stimulation; reduces platelet adhesion and spreading.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-myristoyl glycine|||N-terminal Ras-GEF|||Phorbol-ester/DAG-type|||Phosphoserine|||RAS guanyl-releasing protein 2|||Ras-GEF|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315608|||http://purl.uniprot.org/annotation/VAR_038257|||http://purl.uniprot.org/annotation/VAR_071474|||http://purl.uniprot.org/annotation/VAR_079614|||http://purl.uniprot.org/annotation/VAR_079615|||http://purl.uniprot.org/annotation/VAR_079616|||http://purl.uniprot.org/annotation/VAR_079617|||http://purl.uniprot.org/annotation/VAR_079618|||http://purl.uniprot.org/annotation/VSP_030574|||http://purl.uniprot.org/annotation/VSP_030575|||http://purl.uniprot.org/annotation/VSP_030576|||http://purl.uniprot.org/annotation/VSP_054132
http://togogenome.org/gene/9606:RAB40AL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C0E4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Sequence Variant                                                                                  ^@                                                                                  Ras-related protein Rab-40A-like|||Renders the protein unstable and disrupts its cytoplasmic localization.|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121258|||http://purl.uniprot.org/annotation/VAR_068916
http://togogenome.org/gene/9606:MYO1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0I1T2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||IQ|||In allele HA-2M; the HA-2V allele constitute the HA-2 epitope while HA-2M is not recognized by HA-2 cytotoxic T lymphocytes.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Minor histocompatibility antigen HA-2|||Myosin motor|||N-acetylmethionine|||No effect on membrane localization.|||No effect on membrane localization; when associated with K-883.|||No effect on membrane localization; when associated with R-885.|||No effect on membrane localization; when associated with R-903.|||No effect on membrane localization; when associated with R-906.|||Reduced membrane association.|||TH1|||Unconventional myosin-Ig                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340316|||http://purl.uniprot.org/annotation/PRO_0000340317|||http://purl.uniprot.org/annotation/VAR_044013|||http://purl.uniprot.org/annotation/VAR_044014|||http://purl.uniprot.org/annotation/VAR_044015|||http://purl.uniprot.org/annotation/VAR_050212|||http://purl.uniprot.org/annotation/VSP_034208|||http://purl.uniprot.org/annotation/VSP_034209|||http://purl.uniprot.org/annotation/VSP_034210|||http://purl.uniprot.org/annotation/VSP_034211|||http://purl.uniprot.org/annotation/VSP_034212
http://togogenome.org/gene/9606:RHOXF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHV9                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in infertile men; unknown pathological significance; no effect on induction of target genes expression.|||Homeobox|||Nuclear localization signal|||Rhox homeobox family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049245|||http://purl.uniprot.org/annotation/VAR_049587|||http://purl.uniprot.org/annotation/VAR_077002
http://togogenome.org/gene/9606:TRAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4K3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Interaction with TANK|||Interaction with TAX1BP1|||Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation.|||Loss of SUMO1-modification and c-myb-mediated transcriptional repressive activation. Loss of TRAF3IP2-mediated 'Lys-63'-linked polyubiquitination.|||Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis.|||Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-122.|||Loss of TRAF6 homodimerization and partially impaired polyubiquitin synthesis. Loss of TRAF6 homodimerization and impaired polyubiquitin synthesis; when associated with A-88.|||Loss of interaction with UBE2N.|||Loss of interaction with UBE2N. Has no effect on TRAF3IP2-mediated 'Lys-63'-linked polyubiquitination.|||Loss of ligase activity, autoubiquitination and signaling capacity.|||MATH|||Partially impaired polyubiquitin synthesis.|||RING-type|||TNF receptor-associated factor 6|||TRAF-type 1|||TRAF-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056407
http://togogenome.org/gene/9606:LMAN2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DI83|||http://purl.uniprot.org/uniprot/B4DVH1|||http://purl.uniprot.org/uniprot/B4E308|||http://purl.uniprot.org/uniprot/Q9H0V9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endoplasmic reticulum retention signal|||Helical|||In MRT52; no effect on general protein glycosylation.|||In isoform 2.|||In isoform 3.|||L-type lectin-like|||Loss of ER retention.|||Lumenal|||N-linked (GlcNAc...) (high mannose) asparagine|||VIP36-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017668|||http://purl.uniprot.org/annotation/VAR_076429|||http://purl.uniprot.org/annotation/VSP_017940|||http://purl.uniprot.org/annotation/VSP_054439|||http://purl.uniprot.org/annotation/VSP_054440
http://togogenome.org/gene/9606:RNF152                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8N0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RNF152|||Helical|||Necessary for interaction with RRAGA|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056111
http://togogenome.org/gene/9606:DSG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SJ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein-4|||Extracellular|||Helical|||In HYPT6.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003855|||http://purl.uniprot.org/annotation/PRO_0000003856|||http://purl.uniprot.org/annotation/VAR_021291|||http://purl.uniprot.org/annotation/VAR_024387|||http://purl.uniprot.org/annotation/VAR_033700|||http://purl.uniprot.org/annotation/VAR_048514|||http://purl.uniprot.org/annotation/VSP_012907
http://togogenome.org/gene/9606:PALS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658X5|||http://purl.uniprot.org/uniprot/Q8N3R9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 2.|||Increases interaction with CRB1.|||Interaction with LIN7C|||Interaction with PARD6B|||L27 1|||L27 2|||PDZ|||Phosphoserine|||Protein PALS1|||Reduces binding to Drosophila crb and causes incorrect PALS1 localization and cell polarity.|||Required for the correct localization of PALS1 and PATJ at cell-cell contacts and the normal formation of tight junctions and adherens junctions|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094580|||http://purl.uniprot.org/annotation/VSP_014002
http://togogenome.org/gene/9606:LRCOL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCL2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Leucine-rich colipase-like protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346758
http://togogenome.org/gene/9606:PRR15L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJT1|||http://purl.uniprot.org/uniprot/Q9BU68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Proline-rich protein 15-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294352
http://togogenome.org/gene/9606:PRAMEF26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGN4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348940
http://togogenome.org/gene/9606:B3GALT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Z6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyltransferase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219145
http://togogenome.org/gene/9606:WDR48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2L1|||http://purl.uniprot.org/uniprot/Q8TAF3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased interaction with RAD51AP1.|||Disordered|||Does not affect interaction with RAD51AP1.|||Found in a patient with spastic paraplegia; unknown pathological significance.|||Impaired binding to PHLPP1. Defective in stabilizing PHLPP1.|||Impaired binding to USP12; when associated with Ala-119.|||Impaired binding to USP12; when associated with Ala-172.|||Impaired binding to USP12; when associated with Ala-256.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275 and A-318. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275 and A-318.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-318 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-272, A-275, A-318 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-230, A-274, A-275, A-318 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-168, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-168, A-272, A-274, A-275, A-318 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-168, A-230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-168, A-230, A-272, A-274, A-275, A-318 and A-363.|||In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363.|||In UAF1(3A); impaired DNA-binding; when associated with A-30 and A-168. In UAF1(3A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30 and A-168. In UAF1(11A); impaired DNA-binding; when associated with A-30, A-117, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-117, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363.|||In UAF1(3A); impaired DNA-binding; when associated with A-30 and A-50. In UAF1(3A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30 and A-50. In UAF1(11A); impaired DNA-binding; when associated with A-30, A-50, A-117, A-161, A-230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-30, A-50, A-117, A-161, A-230, A-272, A-274, A-275, A-318 and A-363.|||In UAF1(3A); impaired DNA-binding; when associated with A-50 and A-168. In UAF1(3A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-50 and A-168. In UAF1(11A); impaired DNA-binding; when associated with A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363. In UAF1(11A); does not affect ability to promote USP1-mediated deubiquitination of FANCD2 and stimulate RAD51-mediated homologous recombination, because of DNA-binding mediated by RAD51AP1; when associated with A-50, A-117, A-161, A-168, A-230, A-272, A-274, A-275, A-318 and A-363.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphothreonine|||Phosphotyrosine|||Strongly reduces interaction with USP12 or USP46 and abolishes stimulation of their enzyme activity; when associated with A-256 and D-272.|||Strongly reduces interaction with USP12 or USP46 and abolishes stimulation of their enzyme activity; when associated with E-214 and A-256.|||Strongly reduces interaction with USP12 or USP46 and abolishes stimulation of their enzyme activity; when associated with E-214 and D-272. Impaired binding to USP12; when associated with Ala-77.|||Strongly reduces interaction with USP46 and abolishes stimulation of USP46 enzyme activity.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD repeat-containing protein 48 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051399|||http://purl.uniprot.org/annotation/VAR_077846|||http://purl.uniprot.org/annotation/VSP_016776|||http://purl.uniprot.org/annotation/VSP_016777|||http://purl.uniprot.org/annotation/VSP_037623|||http://purl.uniprot.org/annotation/VSP_037624|||http://purl.uniprot.org/annotation/VSP_037625|||http://purl.uniprot.org/annotation/VSP_037626
http://togogenome.org/gene/9606:BACE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3K2|||http://purl.uniprot.org/uniprot/B7Z3Z4|||http://purl.uniprot.org/uniprot/P56817|||http://purl.uniprot.org/uniprot/Q5W9H2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Almost abolishes beta-cleaved soluble APP production.|||Basic and acidic residues|||Beta-secretase 1|||Cytoplasmic|||DXXLL|||Decreases beta-cleaved soluble APP production.|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Impairs endocytosis and produces a delayed retrograde transport to the trans-Golgi network and delivery to the lysosmes, decreasinf its degradation. Disrupts location to late endosomes and lysosomes. Locates mainly at the cell surface. No effect on degradation regulated by GGA3. Effects on protein stability and defective internalization increases; when associated with R-501.|||In isoform 5 and isoform 6.|||In isoform B, isoform D and isoform 6.|||In isoform C and isoform D.|||Inhibits ubiquitination. No effect on endocytosis rate. Induced protein stability and acculmulation in early and late endosomes, lysosomes and cell membrane. Effects on protein stability and defective internalization increases; when associated with A-499-500-A.|||Interaction with RTN3|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||No effect on endocytosis form the cell surface. Decreases recycling from endosomes to the cell surface.|||No effect on endocytosis from the cell surface. Increases recycling from endosomes to the cell surface.|||Peptidase A1|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025939|||http://purl.uniprot.org/annotation/PRO_0000025940|||http://purl.uniprot.org/annotation/VAR_051509|||http://purl.uniprot.org/annotation/VAR_060692|||http://purl.uniprot.org/annotation/VSP_005222|||http://purl.uniprot.org/annotation/VSP_005223|||http://purl.uniprot.org/annotation/VSP_047092|||http://purl.uniprot.org/annotation/VSP_047093
http://togogenome.org/gene/9606:SNCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37840                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3; approximate|||4|||4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)|||Abolishes osmotic stress-induced phosphorylation.|||Acidic residues|||Alpha-synuclein|||Disordered|||Does not affect polymerization into amyloid fibrils.|||Impairs copper-binding.|||Impairs polymerization into amyloid fibrils.|||In PARK1 and DLB; significant increase in binding to negatively charged phospholipid liposomes; increases oligomerization.|||In PARK1; no effect on oligomerization.|||In PARK1; no effect on osmotic stress-induced phosphorylation; increases oligomerization.|||In PARK1; no effect on protein structure; no effect on phosphorylation of the protein; no effect on membrane- and lipid-binding; increases oligomerization; increases fibril formation; increases secretion of the protein; impairs copper-binding.|||In isoform 2-4.|||In isoform 2-5.|||Increases oligomerization.|||Interaction with SERF1A|||N-acetylmethionine|||No effect on oligomerization.|||No effect on osmotic stress-induced phosphorylation.|||Phosphoserine|||Phosphoserine; by BARK1, PLK2, CK2, CK1 and GRK5|||Phosphotyrosine; by FYN|||Reduces polymerization into amyloid fibrils.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184022|||http://purl.uniprot.org/annotation/VAR_007454|||http://purl.uniprot.org/annotation/VAR_007957|||http://purl.uniprot.org/annotation/VAR_022703|||http://purl.uniprot.org/annotation/VAR_070171|||http://purl.uniprot.org/annotation/VSP_006363|||http://purl.uniprot.org/annotation/VSP_006364
http://togogenome.org/gene/9606:BICRAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AI39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BRD4-interacting chromatin-remodeling complex-associated protein-like|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248602
http://togogenome.org/gene/9606:PRR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T870                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Proline-rich protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334688
http://togogenome.org/gene/9606:ANAPC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3Z6|||http://purl.uniprot.org/uniprot/Q9BS18                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 13|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253980
http://togogenome.org/gene/9606:KIFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCS7|||http://purl.uniprot.org/uniprot/Q9BW19                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Kinesin motor|||Kinesin-like protein KIFC1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125428|||http://purl.uniprot.org/annotation/VAR_012650
http://togogenome.org/gene/9606:FAM216B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7L0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM216B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263728|||http://purl.uniprot.org/annotation/VAR_033743
http://togogenome.org/gene/9606:ZNF749                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43361                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17; atypical|||C2H2-type 18|||C2H2-type 19; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||N6-acetyllysine|||Zinc finger protein 749                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274397|||http://purl.uniprot.org/annotation/VAR_030278|||http://purl.uniprot.org/annotation/VAR_030279|||http://purl.uniprot.org/annotation/VAR_030280
http://togogenome.org/gene/9606:MRPS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82912                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrion|||Small ribosomal subunit protein uS11m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030602|||http://purl.uniprot.org/annotation/VAR_052054|||http://purl.uniprot.org/annotation/VAR_052055|||http://purl.uniprot.org/annotation/VSP_005719|||http://purl.uniprot.org/annotation/VSP_005720
http://togogenome.org/gene/9606:TMEM43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2F9|||http://purl.uniprot.org/uniprot/Q9BTV4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In ARVD5.|||In AUNA3; decreased protein stability; reduced passive conductance current in cochlear glia-like supporting cells; does not affect interactions with GJB2 and GJB4.|||In EDMD7; the mutant protein forms predominantly monomers with very few dimers indicating a defect in oligomerization; overexpression in HeLa cells results in abnormal nuclear structures and decreased nuclear localization of both EMD and SUN2 with mislocalization of EMD to the endoplasmic reticulum.|||In EDMD7; the mutant protein is able to form oligomers; overexpression in HeLa cells results in abnormal nuclear structures and decreased nuclear localization of both EMD and SUN2 with mislocalization of EMD to the endoplasmic reticulum.|||N-acetylalanine|||Nuclear|||Perinuclear space|||Removed|||Transmembrane protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284498|||http://purl.uniprot.org/annotation/VAR_031751|||http://purl.uniprot.org/annotation/VAR_031752|||http://purl.uniprot.org/annotation/VAR_031753|||http://purl.uniprot.org/annotation/VAR_031754|||http://purl.uniprot.org/annotation/VAR_044438|||http://purl.uniprot.org/annotation/VAR_069794|||http://purl.uniprot.org/annotation/VAR_069795|||http://purl.uniprot.org/annotation/VAR_087154
http://togogenome.org/gene/9606:ELOA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Activation domain|||BC-box|||Basic and acidic residues|||Disordered|||Elongin-A2|||In a colorectal cancer sample; somatic mutation.|||Interacting with Elongin BC complex|||Polar residues|||TFIIS N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086963|||http://purl.uniprot.org/annotation/VAR_035914|||http://purl.uniprot.org/annotation/VAR_050965|||http://purl.uniprot.org/annotation/VAR_050966|||http://purl.uniprot.org/annotation/VAR_050967|||http://purl.uniprot.org/annotation/VAR_061646
http://togogenome.org/gene/9606:DPYD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12882                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  4Fe-4S ferredoxin-type 1|||4Fe-4S ferredoxin-type 2|||4Fe-4S ferredoxin-type 3|||Dihydropyrimidine dehydrogenase [NADP(+)]|||In DPYDD; allele DPYD*8; loss of activity.|||In DPYDD; allele DPYD*9A and allele DPYD*9B; loss of activity.|||In DPYDD; allele DPYD*9B; 25% of activity.|||In allele DPYD*10; low activity.|||In allele DPYD*4.|||In allele DPYD*5.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021114|||http://purl.uniprot.org/annotation/PRO_0000021115|||http://purl.uniprot.org/annotation/VAR_005173|||http://purl.uniprot.org/annotation/VAR_005174|||http://purl.uniprot.org/annotation/VAR_005175|||http://purl.uniprot.org/annotation/VAR_005176|||http://purl.uniprot.org/annotation/VAR_005177|||http://purl.uniprot.org/annotation/VAR_005178|||http://purl.uniprot.org/annotation/VAR_014760|||http://purl.uniprot.org/annotation/VAR_054034|||http://purl.uniprot.org/annotation/VSP_044929|||http://purl.uniprot.org/annotation/VSP_044930
http://togogenome.org/gene/9606:SUN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAQ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Nuclear|||Perinuclear space|||SUN|||SUN domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312220|||http://purl.uniprot.org/annotation/VAR_037458|||http://purl.uniprot.org/annotation/VAR_037459|||http://purl.uniprot.org/annotation/VSP_029748|||http://purl.uniprot.org/annotation/VSP_029749|||http://purl.uniprot.org/annotation/VSP_055624
http://togogenome.org/gene/9606:RECQL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQK2|||http://purl.uniprot.org/uniprot/O94762|||http://purl.uniprot.org/uniprot/Q8WYH5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA helicase Q5|||Abolishes helicase activity.|||Abolishes interaction with POLR2A.|||Abolishes interaction with RAD51.|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Impairs protein folding and abolishes interaction with POLR2A.|||In isoform 4.|||In isoform Alpha.|||In isoform Gamma.|||Interaction with POLR2A|||Interaction with RAD51|||Loss of phosphorylation in early mitosis.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Polar residues|||RecQ helicase-like 5|||Reduces interaction with POLR2A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205055|||http://purl.uniprot.org/annotation/VAR_024272|||http://purl.uniprot.org/annotation/VAR_051733|||http://purl.uniprot.org/annotation/VSP_005568|||http://purl.uniprot.org/annotation/VSP_005569|||http://purl.uniprot.org/annotation/VSP_005570|||http://purl.uniprot.org/annotation/VSP_057431
http://togogenome.org/gene/9606:ZFHX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; degenerate|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||In isoform 2 and isoform 5.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger homeobox protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278465|||http://purl.uniprot.org/annotation/VAR_057375|||http://purl.uniprot.org/annotation/VAR_057376|||http://purl.uniprot.org/annotation/VSP_023298|||http://purl.uniprot.org/annotation/VSP_023299|||http://purl.uniprot.org/annotation/VSP_023300|||http://purl.uniprot.org/annotation/VSP_023301|||http://purl.uniprot.org/annotation/VSP_023302|||http://purl.uniprot.org/annotation/VSP_023303|||http://purl.uniprot.org/annotation/VSP_023304
http://togogenome.org/gene/9606:CPNE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QZ18|||http://purl.uniprot.org/uniprot/Q99829                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Copine-1|||Inhibits translocation to the cell membrane in a calcium-dependent manner and does not inhibit neuronal progenitor cell differentiation; when associated with A-21.|||Inhibits translocation to the cell membrane in a calcium-dependent manner and does not inhibit neuronal progenitor cell differentiation; when associated with A-216.|||Inhibits translocation to the cell membrane in a calcium-dependent manner and does not inhibit neuronal progenitor cell differentiation; when associated with A-222.|||Inhibits translocation to the cell membrane in a calcium-dependent manner and does not inhibit neuronal progenitor cell differentiation; when associated with A-90.|||N6-acetyllysine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144834|||http://purl.uniprot.org/annotation/VAR_024423|||http://purl.uniprot.org/annotation/VAR_048846|||http://purl.uniprot.org/annotation/VAR_048847
http://togogenome.org/gene/9606:NOL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60936|||http://purl.uniprot.org/uniprot/Q5TZN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-17 and R-163.|||Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-17 and R-68.|||Abolished ubiquitination in response to an apoptotic stimulus; when associated with R-68 and R-163.|||Acidic residues|||CARD|||Did not reduce creatine kinase release or infarct size after myocardial ischemia/reperfusion. Causes loss of mitochondrial membrane potential and nuclear condensation. Failes to prevent the increase in Bax. Interacts with BAX.|||Disordered|||In MYOCL1.|||In MYOCL1; the mutation may alter post-translational modification of the protein.|||In isoform 1.|||In isoform 3.|||N-myristoyl glycine|||Nucleolar protein 3|||Phosphothreonine; by CK2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144099|||http://purl.uniprot.org/annotation/VAR_069731|||http://purl.uniprot.org/annotation/VAR_072644|||http://purl.uniprot.org/annotation/VSP_054607|||http://purl.uniprot.org/annotation/VSP_057515
http://togogenome.org/gene/9606:C1QA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02745                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q subcomponent subunit A|||Disordered|||Interchain (with C-29 in B chain)|||N-linked (GlcNAc...) asparagine|||O-linked (Gal...) hydroxylysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003517|||http://purl.uniprot.org/annotation/VAR_021090
http://togogenome.org/gene/9606:TMEM187                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14656                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 187                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084262|||http://purl.uniprot.org/annotation/VAR_051431|||http://purl.uniprot.org/annotation/VAR_051432|||http://purl.uniprot.org/annotation/VAR_051433
http://togogenome.org/gene/9606:SAMD4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2R1|||http://purl.uniprot.org/uniprot/Q8WW19|||http://purl.uniprot.org/uniprot/Q9UPU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Smaug homolog 1|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097570|||http://purl.uniprot.org/annotation/VSP_037778|||http://purl.uniprot.org/annotation/VSP_037779
http://togogenome.org/gene/9606:HOXB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17509                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Homeobox|||Homeobox protein Hox-B6|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200135|||http://purl.uniprot.org/annotation/VSP_002388|||http://purl.uniprot.org/annotation/VSP_002389
http://togogenome.org/gene/9606:OR9K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW01|||http://purl.uniprot.org/uniprot/Q8NGE7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150682|||http://purl.uniprot.org/annotation/VAR_048057|||http://purl.uniprot.org/annotation/VAR_048058|||http://purl.uniprot.org/annotation/VAR_048059
http://togogenome.org/gene/9606:SELENOK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6D0                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Non standard residue|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by CAPN2|||Disordered|||Helical|||Removed|||Selenocysteine|||Selenoprotein K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097669|||http://purl.uniprot.org/annotation/VAR_053921
http://togogenome.org/gene/9606:RHPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RhoA.|||BRO1|||Does not induce actin disassembly but still interacts with RhoA; when associated with A-518.|||Does not induce actin disassembly but still interacts with RhoA; when associated with A-526 and A-527.|||In isoform 2.|||Interaction with Rho|||PDZ|||Phosphothreonine|||REM-1|||Rhophilin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218898|||http://purl.uniprot.org/annotation/VAR_061996|||http://purl.uniprot.org/annotation/VAR_061997|||http://purl.uniprot.org/annotation/VSP_055548
http://togogenome.org/gene/9606:CDH23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYR8|||http://purl.uniprot.org/uniprot/A5D6V9|||http://purl.uniprot.org/uniprot/Q6P152|||http://purl.uniprot.org/uniprot/Q8N5B3|||http://purl.uniprot.org/uniprot/Q9H251                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cadherin-23|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNB12.|||In PITA5.|||In PITA5; unknown pathological significance.|||In USH1D and USH1DF.|||In USH1D.|||In USH1D; atypical.|||In USH1D; benign variant.|||In USH1D; mild retinal affection.|||In USH1D; most likely affects splicing.|||In isoform 10 and isoform 11.|||In isoform 2 and isoform 8.|||In isoform 3.|||In isoform 4, isoform 9 and isoform 11.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 9.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003824|||http://purl.uniprot.org/annotation/PRO_5002679718|||http://purl.uniprot.org/annotation/PRO_5004278210|||http://purl.uniprot.org/annotation/PRO_5006541695|||http://purl.uniprot.org/annotation/PRO_5014312271|||http://purl.uniprot.org/annotation/VAR_012166|||http://purl.uniprot.org/annotation/VAR_012167|||http://purl.uniprot.org/annotation/VAR_012168|||http://purl.uniprot.org/annotation/VAR_012169|||http://purl.uniprot.org/annotation/VAR_012170|||http://purl.uniprot.org/annotation/VAR_012171|||http://purl.uniprot.org/annotation/VAR_012172|||http://purl.uniprot.org/annotation/VAR_012173|||http://purl.uniprot.org/annotation/VAR_012174|||http://purl.uniprot.org/annotation/VAR_012175|||http://purl.uniprot.org/annotation/VAR_012176|||http://purl.uniprot.org/annotation/VAR_012177|||http://purl.uniprot.org/annotation/VAR_012178|||http://purl.uniprot.org/annotation/VAR_012179|||http://purl.uniprot.org/annotation/VAR_012180|||http://purl.uniprot.org/annotation/VAR_012181|||http://purl.uniprot.org/annotation/VAR_012182|||http://purl.uniprot.org/annotation/VAR_012183|||http://purl.uniprot.org/annotation/VAR_012184|||http://purl.uniprot.org/annotation/VAR_012185|||http://purl.uniprot.org/annotation/VAR_012186|||http://purl.uniprot.org/annotation/VAR_012187|||http://purl.uniprot.org/annotation/VAR_012188|||http://purl.uniprot.org/annotation/VAR_012189|||http://purl.uniprot.org/annotation/VAR_012190|||http://purl.uniprot.org/annotation/VAR_024030|||http://purl.uniprot.org/annotation/VAR_024031|||http://purl.uniprot.org/annotation/VAR_024032|||http://purl.uniprot.org/annotation/VAR_024033|||http://purl.uniprot.org/annotation/VAR_024034|||http://purl.uniprot.org/annotation/VAR_027317|||http://purl.uniprot.org/annotation/VAR_027318|||http://purl.uniprot.org/annotation/VAR_027319|||http://purl.uniprot.org/annotation/VAR_027320|||http://purl.uniprot.org/annotation/VAR_027321|||http://purl.uniprot.org/annotation/VAR_027322|||http://purl.uniprot.org/annotation/VAR_027323|||http://purl.uniprot.org/annotation/VAR_027324|||http://purl.uniprot.org/annotation/VAR_027325|||http://purl.uniprot.org/annotation/VAR_027326|||http://purl.uniprot.org/annotation/VAR_027327|||http://purl.uniprot.org/annotation/VAR_027328|||http://purl.uniprot.org/annotation/VAR_027329|||http://purl.uniprot.org/annotation/VAR_027330|||http://purl.uniprot.org/annotation/VAR_027331|||http://purl.uniprot.org/annotation/VAR_027332|||http://purl.uniprot.org/annotation/VAR_027333|||http://purl.uniprot.org/annotation/VAR_027334|||http://purl.uniprot.org/annotation/VAR_027335|||http://purl.uniprot.org/annotation/VAR_027336|||http://purl.uniprot.org/annotation/VAR_027337|||http://purl.uniprot.org/annotation/VAR_027338|||http://purl.uniprot.org/annotation/VAR_027339|||http://purl.uniprot.org/annotation/VAR_027340|||http://purl.uniprot.org/annotation/VAR_027341|||http://purl.uniprot.org/annotation/VAR_027342|||http://purl.uniprot.org/annotation/VAR_027343|||http://purl.uniprot.org/annotation/VAR_027344|||http://purl.uniprot.org/annotation/VAR_027345|||http://purl.uniprot.org/annotation/VAR_027346|||http://purl.uniprot.org/annotation/VAR_027347|||http://purl.uniprot.org/annotation/VAR_046404|||http://purl.uniprot.org/annotation/VAR_046405|||http://purl.uniprot.org/annotation/VAR_046406|||http://purl.uniprot.org/annotation/VAR_046407|||http://purl.uniprot.org/annotation/VAR_046408|||http://purl.uniprot.org/annotation/VAR_046409|||http://purl.uniprot.org/annotation/VAR_046410|||http://purl.uniprot.org/annotation/VAR_046411|||http://purl.uniprot.org/annotation/VAR_046412|||http://purl.uniprot.org/annotation/VAR_046413|||http://purl.uniprot.org/annotation/VAR_046414|||http://purl.uniprot.org/annotation/VAR_046415|||http://purl.uniprot.org/annotation/VAR_046416|||http://purl.uniprot.org/annotation/VAR_046417|||http://purl.uniprot.org/annotation/VAR_046418|||http://purl.uniprot.org/annotation/VAR_046419|||http://purl.uniprot.org/annotation/VAR_046420|||http://purl.uniprot.org/annotation/VAR_046421|||http://purl.uniprot.org/annotation/VAR_046422|||http://purl.uniprot.org/annotation/VAR_046423|||http://purl.uniprot.org/annotation/VAR_046424|||http://purl.uniprot.org/annotation/VAR_046425|||http://purl.uniprot.org/annotation/VAR_046426|||http://purl.uniprot.org/annotation/VAR_046427|||http://purl.uniprot.org/annotation/VAR_046428|||http://purl.uniprot.org/annotation/VAR_046429|||http://purl.uniprot.org/annotation/VAR_046430|||http://purl.uniprot.org/annotation/VAR_046431|||http://purl.uniprot.org/annotation/VAR_046432|||http://purl.uniprot.org/annotation/VAR_046433|||http://purl.uniprot.org/annotation/VAR_046434|||http://purl.uniprot.org/annotation/VAR_046435|||http://purl.uniprot.org/annotation/VAR_046436|||http://purl.uniprot.org/annotation/VAR_046437|||http://purl.uniprot.org/annotation/VAR_046438|||http://purl.uniprot.org/annotation/VAR_071407|||http://purl.uniprot.org/annotation/VAR_071408|||http://purl.uniprot.org/annotation/VAR_071409|||http://purl.uniprot.org/annotation/VAR_071410|||http://purl.uniprot.org/annotation/VAR_071411|||http://purl.uniprot.org/annotation/VAR_071412|||http://purl.uniprot.org/annotation/VAR_071413|||http://purl.uniprot.org/annotation/VAR_071414|||http://purl.uniprot.org/annotation/VAR_071415|||http://purl.uniprot.org/annotation/VAR_071416|||http://purl.uniprot.org/annotation/VAR_071417|||http://purl.uniprot.org/annotation/VAR_071418|||http://purl.uniprot.org/annotation/VAR_071419|||http://purl.uniprot.org/annotation/VAR_071420|||http://purl.uniprot.org/annotation/VAR_071421|||http://purl.uniprot.org/annotation/VAR_071422|||http://purl.uniprot.org/annotation/VAR_071423|||http://purl.uniprot.org/annotation/VAR_071424|||http://purl.uniprot.org/annotation/VAR_071425|||http://purl.uniprot.org/annotation/VAR_071426|||http://purl.uniprot.org/annotation/VAR_071427|||http://purl.uniprot.org/annotation/VAR_071428|||http://purl.uniprot.org/annotation/VAR_071429|||http://purl.uniprot.org/annotation/VAR_072661|||http://purl.uniprot.org/annotation/VAR_072662|||http://purl.uniprot.org/annotation/VAR_079747|||http://purl.uniprot.org/annotation/VAR_080381|||http://purl.uniprot.org/annotation/VAR_080382|||http://purl.uniprot.org/annotation/VAR_080383|||http://purl.uniprot.org/annotation/VAR_080384|||http://purl.uniprot.org/annotation/VSP_000645|||http://purl.uniprot.org/annotation/VSP_000646|||http://purl.uniprot.org/annotation/VSP_000647|||http://purl.uniprot.org/annotation/VSP_013268|||http://purl.uniprot.org/annotation/VSP_013269|||http://purl.uniprot.org/annotation/VSP_035289|||http://purl.uniprot.org/annotation/VSP_035290|||http://purl.uniprot.org/annotation/VSP_044260|||http://purl.uniprot.org/annotation/VSP_044261|||http://purl.uniprot.org/annotation/VSP_047923|||http://purl.uniprot.org/annotation/VSP_047924
http://togogenome.org/gene/9606:TIMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK57|||http://purl.uniprot.org/uniprot/P16035                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Involved in metalloproteinase-binding|||Metalloproteinase inhibitor 2|||NTR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034335|||http://purl.uniprot.org/annotation/PRO_5007491749
http://togogenome.org/gene/9606:BSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPA5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||3 X 7 AA tandem repeats of K-A-S-P-[LQ]-[APS]-[KST]|||5 X 2 AA tandem repeats of P-G|||7 X 2 AA tandem repeats of P-G|||Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||C4-type|||Disordered|||N-myristoyl glycine|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein bassoon|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065002|||http://purl.uniprot.org/annotation/VAR_055105|||http://purl.uniprot.org/annotation/VAR_055106|||http://purl.uniprot.org/annotation/VAR_055107
http://togogenome.org/gene/9606:LOC102724652                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8C8KJZ9|||http://purl.uniprot.org/uniprot/P02489                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Alpha-crystallin A chain|||Alpha-crystallin A(1-162)|||Alpha-crystallin A(1-168)|||Alpha-crystallin A(1-172)|||Deamidated asparagine; partial|||Deamidated glutamine; partial|||Impairs chaperone activity.|||In CTRCT9.|||In CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus.|||In CTRCT9; decreases oligomer formation.|||In CTRCT9; delays HSP70 expression increase in response to heat shock.|||In CTRCT9; forms inclusion bodies, decreases chaperone activity, decreases protein stability at 45 degrees Celsius and increases protein aggregate formation in response to DTT in vitro.|||In CTRCT9; reduces protein solubility.|||In CTRCT9; results in protein aggregation in the cytoplasm.|||In CTRCT9; reverse phase-high-performance liquid chromatography suggests an increased hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme.|||In CTRCT9; unknown pathological significance.|||In CTRCT9; unknown pathological significance; reduced chaperone-like activity in vitro.|||In CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity.|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Required for complex formation with BFSP1 and BFSP2; during homooligomerization, mediates the association of 2 dimers to form a tetramer|||SHSP|||Susceptible to oxidation|||With 1 phosphate group.|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125865|||http://purl.uniprot.org/annotation/PRO_0000226639|||http://purl.uniprot.org/annotation/PRO_0000423503|||http://purl.uniprot.org/annotation/PRO_0000423504|||http://purl.uniprot.org/annotation/VAR_003819|||http://purl.uniprot.org/annotation/VAR_036564|||http://purl.uniprot.org/annotation/VAR_038375|||http://purl.uniprot.org/annotation/VAR_046892|||http://purl.uniprot.org/annotation/VAR_046893|||http://purl.uniprot.org/annotation/VAR_070032|||http://purl.uniprot.org/annotation/VAR_084768|||http://purl.uniprot.org/annotation/VAR_084769|||http://purl.uniprot.org/annotation/VAR_084770|||http://purl.uniprot.org/annotation/VAR_084771|||http://purl.uniprot.org/annotation/VAR_084772|||http://purl.uniprot.org/annotation/VAR_084773|||http://purl.uniprot.org/annotation/VAR_084774|||http://purl.uniprot.org/annotation/VAR_084775|||http://purl.uniprot.org/annotation/VAR_084776|||http://purl.uniprot.org/annotation/VAR_084777|||http://purl.uniprot.org/annotation/VAR_084778|||http://purl.uniprot.org/annotation/VAR_084779|||http://purl.uniprot.org/annotation/VAR_084780|||http://purl.uniprot.org/annotation/VAR_084781
http://togogenome.org/gene/9606:PLEKHM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters interaction with sifA.|||Disordered|||In isoform 2.|||Interaction with KIF5B|||Interaction with sifA|||Loss of interaction with sifA.|||N-acetylmethionine|||No effect on lysosomal location; loss of interaction with kinesin-1 and movement of lysosomes to the periphery; when associated with A-207-208-A.|||No effect on lysosomal location; loss of interaction with kinesin-1 and movement of lysosomes to the periphery; when associated with A-236-237-A.|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family M member 2|||Polar residues|||RUN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309455|||http://purl.uniprot.org/annotation/VAR_036950|||http://purl.uniprot.org/annotation/VSP_061018
http://togogenome.org/gene/9606:MEPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC19|||http://purl.uniprot.org/uniprot/Q9NQ76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  ASARM motif; interaction with PHEX|||Basic and acidic residues|||Cell attachment site|||Dentonin|||Disordered|||In isoform 2.|||In isoform 3.|||Matrix extracellular phosphoglycoprotein|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021668|||http://purl.uniprot.org/annotation/PRO_5004314250|||http://purl.uniprot.org/annotation/VAR_034094|||http://purl.uniprot.org/annotation/VSP_043986|||http://purl.uniprot.org/annotation/VSP_046892
http://togogenome.org/gene/9606:GRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLS6|||http://purl.uniprot.org/uniprot/Q9Y3R0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glutamate receptor-interacting protein 1|||In isoform 2.|||In isoform 3.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ 7|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083849|||http://purl.uniprot.org/annotation/VAR_056904|||http://purl.uniprot.org/annotation/VSP_009743|||http://purl.uniprot.org/annotation/VSP_040281
http://togogenome.org/gene/9606:SNX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAR|||Disordered|||In isoform 2.|||In isoform 3.|||PX|||Pro residues|||SH3|||Sorting nexin-18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213866|||http://purl.uniprot.org/annotation/VAR_052480|||http://purl.uniprot.org/annotation/VAR_052481|||http://purl.uniprot.org/annotation/VSP_035839|||http://purl.uniprot.org/annotation/VSP_045476
http://togogenome.org/gene/9606:PNPLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8XXQ3|||http://purl.uniprot.org/uniprot/Q8N8W4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||DGA/G|||Disordered|||GXSXG|||In ARCI10; decreased omega-hydroxyceramide transacylase activity.|||In ARCI10; loss of omega-hydroxyceramide transacylase activity.|||In isoform 2 and isoform 3.|||In isoform 3.|||Nucleophile|||Omega-hydroxyceramide transacylase|||PNPLA|||Polar residues|||Pro residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292019|||http://purl.uniprot.org/annotation/VAR_032929|||http://purl.uniprot.org/annotation/VAR_032930|||http://purl.uniprot.org/annotation/VAR_032931|||http://purl.uniprot.org/annotation/VAR_069566|||http://purl.uniprot.org/annotation/VAR_084012|||http://purl.uniprot.org/annotation/VAR_084013|||http://purl.uniprot.org/annotation/VSP_026371|||http://purl.uniprot.org/annotation/VSP_026372
http://togogenome.org/gene/9606:MMP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99542                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine switch|||Disordered|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Matrix metalloproteinase-19|||N-linked (GlcNAc...) asparagine|||Reduced autolysis rate.|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028826|||http://purl.uniprot.org/annotation/PRO_0000028827|||http://purl.uniprot.org/annotation/VAR_021036|||http://purl.uniprot.org/annotation/VAR_021037|||http://purl.uniprot.org/annotation/VAR_021038|||http://purl.uniprot.org/annotation/VAR_054006|||http://purl.uniprot.org/annotation/VSP_005457|||http://purl.uniprot.org/annotation/VSP_005458|||http://purl.uniprot.org/annotation/VSP_041893|||http://purl.uniprot.org/annotation/VSP_041894|||http://purl.uniprot.org/annotation/VSP_054573|||http://purl.uniprot.org/annotation/VSP_054574|||http://purl.uniprot.org/annotation/VSP_054575
http://togogenome.org/gene/9606:TMEM163                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HLD25; does not rescue developmental defects and myelin deficit in zebrafish morphants but results in a more severe phenotype; affects cell development and survival when expressed in oligodendroglial cells.|||In HLD25; results in decreased function in zinc transport; affects cell development and survival when expressed in oligodendroglial cells.|||In HLD25; severely decreased function in zinc transport; does not rescue developmental defects and myelin deficit in zebrafish morphants but results in a more severe phenotype.|||In HLD25; unknown pathological significance; results in decreased function in zinc transport; affects cell development and survival when expressed in oligodendroglial cells.|||In isoform 2.|||In isoform 3.|||Loss of interaction with MCOLN1.|||Phosphoserine|||Pro residues|||Reduced interaction with MCOLN1.|||Required for interaction with MCOLN1|||Results in decreased zinc efflux.|||Severely reduced zinc efflux; when associated with A-124.|||Severely reduced zinc efflux; when associated with A-128.|||Transmembrane protein 163                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278539|||http://purl.uniprot.org/annotation/VAR_088115|||http://purl.uniprot.org/annotation/VAR_088116|||http://purl.uniprot.org/annotation/VAR_088117|||http://purl.uniprot.org/annotation/VAR_088118|||http://purl.uniprot.org/annotation/VAR_088119|||http://purl.uniprot.org/annotation/VAR_088120|||http://purl.uniprot.org/annotation/VAR_088121|||http://purl.uniprot.org/annotation/VAR_088122|||http://purl.uniprot.org/annotation/VSP_023328|||http://purl.uniprot.org/annotation/VSP_023329|||http://purl.uniprot.org/annotation/VSP_023330|||http://purl.uniprot.org/annotation/VSP_023331|||http://purl.uniprot.org/annotation/VSP_023332
http://togogenome.org/gene/9606:DECR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUI1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Microbody targeting signal|||N-acetylalanine|||N6-acetyllysine|||Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]|||Phosphoserine|||Reduces enzyme activity by 97%.|||Reduces enzyme activity by 98%.|||Reduces enzyme activity by about 95%.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054559|||http://purl.uniprot.org/annotation/VSP_013629|||http://purl.uniprot.org/annotation/VSP_013630|||http://purl.uniprot.org/annotation/VSP_013631|||http://purl.uniprot.org/annotation/VSP_013632
http://togogenome.org/gene/9606:SYT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7P8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cysteine motif|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Necessary for cell membrane association (isoform 2)|||Phosphoserine|||Synaptotagmin-6|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183954|||http://purl.uniprot.org/annotation/VSP_036619
http://togogenome.org/gene/9606:SLC12A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPF4|||http://purl.uniprot.org/uniprot/Q13621|||http://purl.uniprot.org/uniprot/Q8IUN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished interaction with OXSR1/OSR1 and STK39/SPAK and subsequent phosphorylation and activation.|||Abolished phosphoryation by OXSR1/OSR1 and STK39/SPAK in vitro.|||Amino acid permease N-terminal|||Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect interaction with OXSR1/OSR1 and STK39/SPAK.|||Helical|||In BARTS1.|||In isoform F.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by OXSR1 and STK39|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||Polar residues|||RFXV motif|||SLC12A transporter C-terminal|||Solute carrier family 12 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178018|||http://purl.uniprot.org/annotation/VAR_010223|||http://purl.uniprot.org/annotation/VAR_010224|||http://purl.uniprot.org/annotation/VAR_047257|||http://purl.uniprot.org/annotation/VSP_035701
http://togogenome.org/gene/9606:TBX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75333                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||T-box|||T-box transcription factor TBX10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184441|||http://purl.uniprot.org/annotation/VAR_021984|||http://purl.uniprot.org/annotation/VAR_052262
http://togogenome.org/gene/9606:DBI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZWD1|||http://purl.uniprot.org/uniprot/B8ZWD8|||http://purl.uniprot.org/uniprot/P07108                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ACB|||Acyl-CoA-binding protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214004|||http://purl.uniprot.org/annotation/VAR_048160|||http://purl.uniprot.org/annotation/VAR_048161|||http://purl.uniprot.org/annotation/VAR_048162|||http://purl.uniprot.org/annotation/VSP_000068|||http://purl.uniprot.org/annotation/VSP_038680|||http://purl.uniprot.org/annotation/VSP_043437|||http://purl.uniprot.org/annotation/VSP_043438|||http://purl.uniprot.org/annotation/VSP_044114
http://togogenome.org/gene/9606:IL18BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1C5|||http://purl.uniprot.org/uniprot/O95998                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Ig-like|||Ig-like C2-type|||In isoform B.|||In isoform D.|||Interleukin-18-binding protein|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014778|||http://purl.uniprot.org/annotation/PRO_5015091646|||http://purl.uniprot.org/annotation/VAR_024497|||http://purl.uniprot.org/annotation/VAR_059393|||http://purl.uniprot.org/annotation/VSP_002515|||http://purl.uniprot.org/annotation/VSP_002516|||http://purl.uniprot.org/annotation/VSP_037605|||http://purl.uniprot.org/annotation/VSP_037606
http://togogenome.org/gene/9606:EFNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15768                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of Nipah protein G binding.|||Cytoplasmic|||Disordered|||Ephrin RBD|||Ephrin-B3|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008395|||http://purl.uniprot.org/annotation/VAR_002356
http://togogenome.org/gene/9606:SPRYD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDT6|||http://purl.uniprot.org/uniprot/Q5W111                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||In isoform 2.|||N-acetylalanine|||Removed|||SPRY domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243925|||http://purl.uniprot.org/annotation/VSP_019498
http://togogenome.org/gene/9606:RFC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35249                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Polar residues|||Replication factor C subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121757|||http://purl.uniprot.org/annotation/VAR_014307|||http://purl.uniprot.org/annotation/VAR_036121|||http://purl.uniprot.org/annotation/VSP_055862|||http://purl.uniprot.org/annotation/VSP_055863
http://togogenome.org/gene/9606:NUP214                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAV2|||http://purl.uniprot.org/uniprot/P35658                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Binds human adenovirus 5 (HAdV-5) protein L3 (hexon)|||1|||10|||11|||11 X 3 AA approximate repeats|||11 X 5 AA approximate repeats|||12|||13|||14|||15|||16|||17|||18|||18 X 4 AA approximate repeats|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34|||35|||36|||37|||38|||39|||4|||40|||41|||42|||43|||44|||44 X 2 AA repeats of F-G|||5|||6|||7|||8|||9|||Blade 1|||Blade 2|||Blade 3|||Blade 4|||Blade 5|||Blade 6|||Blade 7|||Breakpoint|||Breakpoint for translocation to form the NUP214-ABL1 fusion protein|||Breakpoint for translocation to form the NUP214-SQSTM1 fusion protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with DDX19B.|||In IIAE9.|||In IIAE9; decreased nuclear transport in patient cells; decreased protein levels in patient cells.|||In IIAE9; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Leucine-zipper 1|||Leucine-zipper 2|||N-acetylglycine|||Nuclear pore complex protein Nup214|||Nuclear pore complex protein Nup214 phenylalanine-glycine (FG)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced binding to DDX19B.|||Removed|||Seven-bladed beta propeller                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204861|||http://purl.uniprot.org/annotation/VAR_035856|||http://purl.uniprot.org/annotation/VAR_035857|||http://purl.uniprot.org/annotation/VAR_035858|||http://purl.uniprot.org/annotation/VAR_045691|||http://purl.uniprot.org/annotation/VAR_061533|||http://purl.uniprot.org/annotation/VAR_082629|||http://purl.uniprot.org/annotation/VAR_082630|||http://purl.uniprot.org/annotation/VAR_082631|||http://purl.uniprot.org/annotation/VSP_034896|||http://purl.uniprot.org/annotation/VSP_034897|||http://purl.uniprot.org/annotation/VSP_034898|||http://purl.uniprot.org/annotation/VSP_034899
http://togogenome.org/gene/9606:KRTAP3-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185166|||http://purl.uniprot.org/annotation/VAR_053454|||http://purl.uniprot.org/annotation/VAR_053455|||http://purl.uniprot.org/annotation/VAR_053456
http://togogenome.org/gene/9606:KANSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2N6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8.|||In isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||KAT8 regulatory NSL complex subunit 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416242|||http://purl.uniprot.org/annotation/VAR_032268|||http://purl.uniprot.org/annotation/VSP_025324|||http://purl.uniprot.org/annotation/VSP_025325|||http://purl.uniprot.org/annotation/VSP_025326|||http://purl.uniprot.org/annotation/VSP_025327|||http://purl.uniprot.org/annotation/VSP_025328|||http://purl.uniprot.org/annotation/VSP_025329|||http://purl.uniprot.org/annotation/VSP_025330|||http://purl.uniprot.org/annotation/VSP_025331|||http://purl.uniprot.org/annotation/VSP_025332|||http://purl.uniprot.org/annotation/VSP_025333
http://togogenome.org/gene/9606:KCNH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCM2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CAD (involved in subunit assembly)|||Calmodulin-binding|||Cytoplasmic|||Disordered|||Extracellular|||Found in a child with sporadic epilepsy; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 5|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054010|||http://purl.uniprot.org/annotation/VAR_065162|||http://purl.uniprot.org/annotation/VAR_077834|||http://purl.uniprot.org/annotation/VSP_000972|||http://purl.uniprot.org/annotation/VSP_000973|||http://purl.uniprot.org/annotation/VSP_000974|||http://purl.uniprot.org/annotation/VSP_000975|||http://purl.uniprot.org/annotation/VSP_000976
http://togogenome.org/gene/9606:LATS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95835                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes phosphorylation by NUAK1 and NUAK2.|||Basic and acidic residues|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with YAP1|||Loss of interaction with YAP1.|||Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression.|||PPxY motif 1|||PPxY motif 2|||Phosphoserine|||Phosphoserine; by NUAK1 and NUAK2|||Phosphoserine; by STK3/MST2|||Phosphothreonine|||Phosphothreonine; by STK3/MST2|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LATS1|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086232|||http://purl.uniprot.org/annotation/VAR_040660|||http://purl.uniprot.org/annotation/VAR_040661|||http://purl.uniprot.org/annotation/VAR_040662|||http://purl.uniprot.org/annotation/VAR_040663|||http://purl.uniprot.org/annotation/VAR_040664|||http://purl.uniprot.org/annotation/VAR_040665|||http://purl.uniprot.org/annotation/VAR_040666|||http://purl.uniprot.org/annotation/VAR_040667|||http://purl.uniprot.org/annotation/VAR_040668|||http://purl.uniprot.org/annotation/VSP_051604|||http://purl.uniprot.org/annotation/VSP_051605
http://togogenome.org/gene/9606:FICD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVA6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes adenylyltransferase activity.|||Abolishes homodimerization.|||Cytoplasmic|||Decreased AMPylation.|||Does not affect auto-AMPylation.|||Does not affect level of auto-AMPylation.|||Fido|||Helical; Signal-anchor for type II membrane protein|||Important for autoinhibition of adenylyltransferase activity|||Inhibitory (S/T)XXXE(G/N) motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-AMP-serine; by autocatalysis|||O-AMP-threonine; by autocatalysis|||Promotes adenylyltransferase activity.|||Protein adenylyltransferase FICD|||Slightly decreased N-glycosylation. Abolished N-glycosylation; when associated with Q-275.|||Strongly decreased N-glycosylation. Abolished N-glycosylation; when associated with Q-446.|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317301
http://togogenome.org/gene/9606:PRDM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2; atypical|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In BCS2.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||PR domain zinc finger protein 5|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047761|||http://purl.uniprot.org/annotation/VAR_066393|||http://purl.uniprot.org/annotation/VSP_035652|||http://purl.uniprot.org/annotation/VSP_035653|||http://purl.uniprot.org/annotation/VSP_035654|||http://purl.uniprot.org/annotation/VSP_054395|||http://purl.uniprot.org/annotation/VSP_054396
http://togogenome.org/gene/9606:CREBBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92793                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with ASF1A.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form KAT6A-CREBBP|||Breakpoint for translocation to form KAT6B-CREBBP|||Bromo|||CBP/p300-type HAT|||CREB-binding protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Impairs binding to acetylated histones.|||Impairs interaction with ASF1A.|||In MKHK1.|||In RSTS1.|||In RSTS1; abolishes acetyltransferase activity and the ability of transactivate CREB.|||In RSTS1; abolishes acetyltransferase activity.|||In RSTS1; incomplete.|||In RSTS1; mild form; impairs binding to ASF1A and acetylated histone H3.|||In isoform 2.|||Interaction with ASF1A|||Interaction with SRCAP|||Interaction with TRERF1|||Interaction with histone|||KIX|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by IKKA|||Polar residues|||Pro residues|||Removed|||TAZ-type 1|||TAZ-type 2|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211190|||http://purl.uniprot.org/annotation/VAR_015578|||http://purl.uniprot.org/annotation/VAR_027953|||http://purl.uniprot.org/annotation/VAR_035080|||http://purl.uniprot.org/annotation/VAR_035081|||http://purl.uniprot.org/annotation/VAR_035082|||http://purl.uniprot.org/annotation/VAR_035083|||http://purl.uniprot.org/annotation/VAR_035084|||http://purl.uniprot.org/annotation/VAR_037305|||http://purl.uniprot.org/annotation/VAR_072912|||http://purl.uniprot.org/annotation/VAR_072913|||http://purl.uniprot.org/annotation/VAR_072914|||http://purl.uniprot.org/annotation/VAR_072915|||http://purl.uniprot.org/annotation/VAR_072916|||http://purl.uniprot.org/annotation/VAR_072917|||http://purl.uniprot.org/annotation/VAR_072918|||http://purl.uniprot.org/annotation/VAR_072919|||http://purl.uniprot.org/annotation/VAR_072920|||http://purl.uniprot.org/annotation/VAR_072921|||http://purl.uniprot.org/annotation/VAR_072922|||http://purl.uniprot.org/annotation/VAR_072923|||http://purl.uniprot.org/annotation/VAR_072924|||http://purl.uniprot.org/annotation/VAR_078557|||http://purl.uniprot.org/annotation/VAR_078558|||http://purl.uniprot.org/annotation/VAR_078559|||http://purl.uniprot.org/annotation/VAR_078560|||http://purl.uniprot.org/annotation/VAR_078561|||http://purl.uniprot.org/annotation/VAR_078562|||http://purl.uniprot.org/annotation/VAR_078563|||http://purl.uniprot.org/annotation/VAR_078564|||http://purl.uniprot.org/annotation/VAR_078565|||http://purl.uniprot.org/annotation/VAR_078566|||http://purl.uniprot.org/annotation/VAR_081979|||http://purl.uniprot.org/annotation/VAR_081980|||http://purl.uniprot.org/annotation/VAR_081981|||http://purl.uniprot.org/annotation/VAR_081982|||http://purl.uniprot.org/annotation/VAR_081983|||http://purl.uniprot.org/annotation/VAR_081984|||http://purl.uniprot.org/annotation/VAR_081985|||http://purl.uniprot.org/annotation/VSP_045700
http://togogenome.org/gene/9606:AKR1B15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JRZ8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Site|||Splice Variant                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member B15|||In isoform 2.|||Lowers pKa of active site Tyr|||N6-acetyllysine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395341|||http://purl.uniprot.org/annotation/VSP_041606
http://togogenome.org/gene/9606:SERPINA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL23|||http://purl.uniprot.org/uniprot/P01009                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by Staphylococcus aureus aureolysin/Aur|||(Microbial infection) Cleavage; by Staphylococcus aureus serine and cysteine proteinases|||Alpha-1-antitrypsin|||In Aberrant form.|||In Basque.|||In Christchurch.|||In F.|||In I.|||In L-Frankfurt.|||In L-Offenbach.|||In M-Heerlen.|||In M-Malton, M-Nichinan and M-Palermo; associated with very low serum levels of AAT; homozygosity for allele M-Malton may be associated with a risk for chronic emphysema or infantile liver cirrhosis.|||In M-Mineral springs; causes reduced AAT secretion.|||In M-Procida.|||In M1A and Z; associated with K-366 in Z.|||In M2 and M3; associated with H-125 in M2.|||In M2-Obernburg.|||In M2; associated with D-400.|||In M5-Berlin.|||In M5-Karlsruhe.|||In M6-Bonn.|||In M6-Passau.|||In P-Duarte/P-Cardiff/P-Lowell; associated with H-415 in Y-Barcelona.|||In P-St.Albans/P-Donauwoerth.|||In Pittsburgh; has antithrombin activity; inhibits factor VIIa activity; causes fatal bleeding diathesis.|||In QO-Lisbon; deficient AAT with very low serum levels.|||In QO-Ludwigshafen.|||In QO-Newport.|||In S and T.|||In S-Iiyama.|||In S-Munich.|||In Sao Tome.|||In V and M-Nichinan.|||In V-Munich.|||In W-Bethesda.|||In X.|||In Y-Barcelona; associated with V-280.|||In Z-Bristol; deficient AA; disrupts the N-glycosylation site N-107.|||In Z-Wrexham.|||In Z/Z-Augsburg/Z-Tun; associated with A-237 in Z.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||Oxidation-resistant inhibitor of therapeutic importance.|||Phosphoserine|||Phosphoserine; by FAM20C|||RCL|||Reactive bond|||S-cysteinyl cysteine|||Serpin|||Short peptide from AAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032377|||http://purl.uniprot.org/annotation/PRO_0000364030|||http://purl.uniprot.org/annotation/PRO_5014303308|||http://purl.uniprot.org/annotation/VAR_006978|||http://purl.uniprot.org/annotation/VAR_006979|||http://purl.uniprot.org/annotation/VAR_006980|||http://purl.uniprot.org/annotation/VAR_006981|||http://purl.uniprot.org/annotation/VAR_006982|||http://purl.uniprot.org/annotation/VAR_006983|||http://purl.uniprot.org/annotation/VAR_006984|||http://purl.uniprot.org/annotation/VAR_006985|||http://purl.uniprot.org/annotation/VAR_006986|||http://purl.uniprot.org/annotation/VAR_006987|||http://purl.uniprot.org/annotation/VAR_006988|||http://purl.uniprot.org/annotation/VAR_006989|||http://purl.uniprot.org/annotation/VAR_006990|||http://purl.uniprot.org/annotation/VAR_006991|||http://purl.uniprot.org/annotation/VAR_006992|||http://purl.uniprot.org/annotation/VAR_006993|||http://purl.uniprot.org/annotation/VAR_006994|||http://purl.uniprot.org/annotation/VAR_006995|||http://purl.uniprot.org/annotation/VAR_006996|||http://purl.uniprot.org/annotation/VAR_006997|||http://purl.uniprot.org/annotation/VAR_006998|||http://purl.uniprot.org/annotation/VAR_006999|||http://purl.uniprot.org/annotation/VAR_007000|||http://purl.uniprot.org/annotation/VAR_007001|||http://purl.uniprot.org/annotation/VAR_007002|||http://purl.uniprot.org/annotation/VAR_007003|||http://purl.uniprot.org/annotation/VAR_007004|||http://purl.uniprot.org/annotation/VAR_007005|||http://purl.uniprot.org/annotation/VAR_007006|||http://purl.uniprot.org/annotation/VAR_007007|||http://purl.uniprot.org/annotation/VAR_007008|||http://purl.uniprot.org/annotation/VAR_007009|||http://purl.uniprot.org/annotation/VAR_007010|||http://purl.uniprot.org/annotation/VAR_007011|||http://purl.uniprot.org/annotation/VAR_009216|||http://purl.uniprot.org/annotation/VAR_011620|||http://purl.uniprot.org/annotation/VAR_036746|||http://purl.uniprot.org/annotation/VAR_051938|||http://purl.uniprot.org/annotation/VSP_028889|||http://purl.uniprot.org/annotation/VSP_028890
http://togogenome.org/gene/9606:PCNX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6ZDM2|||http://purl.uniprot.org/uniprot/Q63HM2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Pecanex C-terminal|||Pecanex-like protein|||Pecanex-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253892|||http://purl.uniprot.org/annotation/PRO_5002850649|||http://purl.uniprot.org/annotation/VAR_028745|||http://purl.uniprot.org/annotation/VAR_028746|||http://purl.uniprot.org/annotation/VAR_028747
http://togogenome.org/gene/9606:ZNF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRP4|||http://purl.uniprot.org/uniprot/P17036|||http://purl.uniprot.org/uniprot/Q86U76                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Phosphothreonine|||Zinc finger protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047368|||http://purl.uniprot.org/annotation/VAR_052743|||http://purl.uniprot.org/annotation/VSP_041156
http://togogenome.org/gene/9606:CHAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUX1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glutathione-specific gamma-glutamylcyclotransferase 1|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239010|||http://purl.uniprot.org/annotation/VSP_038960
http://togogenome.org/gene/9606:DNTT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04053                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT|||DNA nucleotidylexotransferase|||Disordered|||In isoform 2.|||Involved in DNA binding|||Mediates interaction with DNTTIP2|||Nearly abolishes enzyme activity.|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218791|||http://purl.uniprot.org/annotation/VAR_058200|||http://purl.uniprot.org/annotation/VSP_038397
http://togogenome.org/gene/9606:USP33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEY7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with Q-673.|||Abolishes deubiquitinating activity. Does not inhibit lysosomal trafficking of ADRB2; when associated with S-194.|||DUSP 1|||DUSP 2|||Disordered|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080664|||http://purl.uniprot.org/annotation/VSP_008591|||http://purl.uniprot.org/annotation/VSP_008592|||http://purl.uniprot.org/annotation/VSP_008593|||http://purl.uniprot.org/annotation/VSP_008594
http://togogenome.org/gene/9606:RNFT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5M7Z0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased ubiquitin ligase activity; when associated with S-375.|||Decreased ubiquitin ligase activity; when associated with S-378.|||Disordered|||E3 ubiquitin-protein ligase RNFT1|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||RING-type|||Required for ubiquitin ligase activity and for protection against ER stress-induced cell death                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320635|||http://purl.uniprot.org/annotation/VSP_031698|||http://purl.uniprot.org/annotation/VSP_031699|||http://purl.uniprot.org/annotation/VSP_031700|||http://purl.uniprot.org/annotation/VSP_031701
http://togogenome.org/gene/9606:CYSRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MQ03                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine-rich tail protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332287
http://togogenome.org/gene/9606:REEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H902                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In SPG31 and DSMA6; impairs normal ER-targeting.|||In SPG31.|||In SPG31; impairs normal ER-targeting.|||In SPG31; loss of function mutation; shows severely altered localization to numerous punctate small structures throughout the cytoplasm; does not localize to the endoplasmic reticulum; impairs normal ER targeting.|||In SPG31; unknown pathological significance; does not impair normal ER-targeting.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Receptor expression-enhancing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101821|||http://purl.uniprot.org/annotation/VAR_027351|||http://purl.uniprot.org/annotation/VAR_067265|||http://purl.uniprot.org/annotation/VAR_067266|||http://purl.uniprot.org/annotation/VAR_067267|||http://purl.uniprot.org/annotation/VAR_067268|||http://purl.uniprot.org/annotation/VAR_072609|||http://purl.uniprot.org/annotation/VAR_072610|||http://purl.uniprot.org/annotation/VAR_072611|||http://purl.uniprot.org/annotation/VSP_042573|||http://purl.uniprot.org/annotation/VSP_043251|||http://purl.uniprot.org/annotation/VSP_043252
http://togogenome.org/gene/9606:TLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4G6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  FERM|||Found in patients with fifth finger camptodactyly syndrome; unknown pathological significance.|||I/LWEQ|||Interaction with PIP5K1C|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Talin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219431|||http://purl.uniprot.org/annotation/VAR_014432|||http://purl.uniprot.org/annotation/VAR_014433|||http://purl.uniprot.org/annotation/VAR_055313|||http://purl.uniprot.org/annotation/VAR_055314|||http://purl.uniprot.org/annotation/VAR_055315|||http://purl.uniprot.org/annotation/VAR_059136|||http://purl.uniprot.org/annotation/VAR_076545
http://togogenome.org/gene/9606:MRE11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W7U8|||http://purl.uniprot.org/uniprot/P49959|||http://purl.uniprot.org/uniprot/Q05D78                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Double-strand break repair protein MRE11|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ATLD1.|||In a breast cancer sample; somatic mutation.|||In cancer.|||In isoform 2.|||In isoform 3.|||In ovarian cancer.|||Mre11 DNA-binding|||N-acetylserine|||Phosphoserine|||Polar residues|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138672|||http://purl.uniprot.org/annotation/VAR_008513|||http://purl.uniprot.org/annotation/VAR_011625|||http://purl.uniprot.org/annotation/VAR_011626|||http://purl.uniprot.org/annotation/VAR_011627|||http://purl.uniprot.org/annotation/VAR_011628|||http://purl.uniprot.org/annotation/VAR_019288|||http://purl.uniprot.org/annotation/VAR_019289|||http://purl.uniprot.org/annotation/VAR_025528|||http://purl.uniprot.org/annotation/VAR_036416|||http://purl.uniprot.org/annotation/VAR_036417|||http://purl.uniprot.org/annotation/VSP_003262|||http://purl.uniprot.org/annotation/VSP_057350
http://togogenome.org/gene/9606:ANKRD55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KP44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 55|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274410|||http://purl.uniprot.org/annotation/VAR_030283|||http://purl.uniprot.org/annotation/VAR_055516|||http://purl.uniprot.org/annotation/VSP_022740|||http://purl.uniprot.org/annotation/VSP_022741
http://togogenome.org/gene/9606:CXCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19876                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-X-C motif chemokine 3|||GRO-gamma(5-73)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005065|||http://purl.uniprot.org/annotation/PRO_0000005066|||http://purl.uniprot.org/annotation/VAR_059210
http://togogenome.org/gene/9606:NUP98                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52948                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form NUP98-CCDC28A|||Breakpoint for translocation to form NUP98-PHF23 oncogene|||Breakpoint for translocation to form the NUP98-HOXA9 fusion protein. Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein|||Breakpoint for translocation to form the NUP98-KDM5A fusion protein|||Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein. Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein|||Cleavage; by autolysis|||Disordered|||FG repeats 1|||FG repeats 2|||GLEBS; interaction with RAE1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 6.|||Loss of autoprocessing. Loss of nuclear membrane localization.|||Loss of processing. Loss of nuclear membrane localization.|||Moderate reduction in autoprocessing.|||N6-acetyllysine; alternate|||No effect in autoprocessing.|||No effect on autoprocessing. Severe loss of autoprocessing; when associated with A-879.|||Nuclear pore complex protein Nup96|||Nuclear pore complex protein Nup98|||Nucleophile|||Peptidase S59|||Phosphoserine|||Phosphothreonine|||Polar residues|||Slight reduction in autoprocessing.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019929|||http://purl.uniprot.org/annotation/PRO_0000019930|||http://purl.uniprot.org/annotation/VAR_035859|||http://purl.uniprot.org/annotation/VSP_003619|||http://purl.uniprot.org/annotation/VSP_007942|||http://purl.uniprot.org/annotation/VSP_007943|||http://purl.uniprot.org/annotation/VSP_007944|||http://purl.uniprot.org/annotation/VSP_038328
http://togogenome.org/gene/9606:BTNL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX41                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin-like protein 8|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014541|||http://purl.uniprot.org/annotation/VAR_049839|||http://purl.uniprot.org/annotation/VAR_049840|||http://purl.uniprot.org/annotation/VAR_069135|||http://purl.uniprot.org/annotation/VAR_069136|||http://purl.uniprot.org/annotation/VAR_069137|||http://purl.uniprot.org/annotation/VSP_012718|||http://purl.uniprot.org/annotation/VSP_012719|||http://purl.uniprot.org/annotation/VSP_045471|||http://purl.uniprot.org/annotation/VSP_045472|||http://purl.uniprot.org/annotation/VSP_045781|||http://purl.uniprot.org/annotation/VSP_046067|||http://purl.uniprot.org/annotation/VSP_046068|||http://purl.uniprot.org/annotation/VSP_046069
http://togogenome.org/gene/9606:PRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JNB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5002546234
http://togogenome.org/gene/9606:MTNR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49286                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melatonin receptor type 1B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069870|||http://purl.uniprot.org/annotation/VAR_009262|||http://purl.uniprot.org/annotation/VAR_009263|||http://purl.uniprot.org/annotation/VAR_049421
http://togogenome.org/gene/9606:TMEM225B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP42                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Transmembrane protein 225B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440046
http://togogenome.org/gene/9606:VCX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H322                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 10 AA tandem repeats of L-S-Q-E-S-[EQ]-V-E-E-P|||Basic residues|||Disordered|||Polar residues|||Variable charge X-linked protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184660|||http://purl.uniprot.org/annotation/VAR_047772|||http://purl.uniprot.org/annotation/VAR_047773|||http://purl.uniprot.org/annotation/VAR_047774|||http://purl.uniprot.org/annotation/VAR_047775
http://togogenome.org/gene/9606:FGF21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3L5M7|||http://purl.uniprot.org/uniprot/Q9NSA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor|||Fibroblast growth factor 21|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008994|||http://purl.uniprot.org/annotation/PRO_5031600779|||http://purl.uniprot.org/annotation/VAR_049064|||http://purl.uniprot.org/annotation/VAR_055375
http://togogenome.org/gene/9606:TULP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||SOCS box|||TUB|||Tubby-related protein 4|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186472|||http://purl.uniprot.org/annotation/VAR_052417|||http://purl.uniprot.org/annotation/VAR_052418|||http://purl.uniprot.org/annotation/VAR_052419|||http://purl.uniprot.org/annotation/VAR_052420|||http://purl.uniprot.org/annotation/VAR_052421|||http://purl.uniprot.org/annotation/VAR_059841|||http://purl.uniprot.org/annotation/VSP_006676|||http://purl.uniprot.org/annotation/VSP_006677
http://togogenome.org/gene/9606:APC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95996                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 20 AA approximate repeat of F-X-V-E-X-T-P-X-C-F-S-R-X-S-S-L-S-S-L-S|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||Adenomatous polyposis coli protein 2|||Basic and acidic residues|||Disordered|||In CDCBM10.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with CTNNB1|||Interaction with MAPRE1 and MAPRE3|||Phosphoserine|||Polar residues|||Pro residues|||Required for localization to microtubules and function in microtubule stabilization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313686|||http://purl.uniprot.org/annotation/VAR_037703|||http://purl.uniprot.org/annotation/VAR_037704|||http://purl.uniprot.org/annotation/VAR_037705|||http://purl.uniprot.org/annotation/VAR_081224|||http://purl.uniprot.org/annotation/VAR_083414|||http://purl.uniprot.org/annotation/VAR_083415|||http://purl.uniprot.org/annotation/VAR_083416|||http://purl.uniprot.org/annotation/VSP_030106|||http://purl.uniprot.org/annotation/VSP_030107
http://togogenome.org/gene/9606:CDH11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BUU9|||http://purl.uniprot.org/uniprot/P55287                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-11|||Cytoplasmic|||Extracellular|||Helical|||In ESWS.|||In TBHS2.|||In TBHS2; results in decreased cell adhesion as shown by a cell-substrate adhesion assay.|||In TBHS2; results in increased cell migration as shown by an in vitro wound closure assay using patient cells.|||In TBHS2; results in loss of cell adhesion as shown by a cell-substrate adhesion assay.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003785|||http://purl.uniprot.org/annotation/PRO_0000003786|||http://purl.uniprot.org/annotation/VAR_031945|||http://purl.uniprot.org/annotation/VAR_031946|||http://purl.uniprot.org/annotation/VAR_031947|||http://purl.uniprot.org/annotation/VAR_080481|||http://purl.uniprot.org/annotation/VAR_086894|||http://purl.uniprot.org/annotation/VAR_086895|||http://purl.uniprot.org/annotation/VAR_086896|||http://purl.uniprot.org/annotation/VAR_086897|||http://purl.uniprot.org/annotation/VAR_086898|||http://purl.uniprot.org/annotation/VAR_086899|||http://purl.uniprot.org/annotation/VAR_086900|||http://purl.uniprot.org/annotation/VAR_086901|||http://purl.uniprot.org/annotation/VAR_086902|||http://purl.uniprot.org/annotation/VSP_000640|||http://purl.uniprot.org/annotation/VSP_000641
http://togogenome.org/gene/9606:MIER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N108                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 10.|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4, isoform 8 and isoform 10.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with HDAC1|||Loss of transcriptional repression and HDAC1 recruitment activity.|||Mesoderm induction early response protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197141|||http://purl.uniprot.org/annotation/VSP_042449|||http://purl.uniprot.org/annotation/VSP_042450|||http://purl.uniprot.org/annotation/VSP_042451|||http://purl.uniprot.org/annotation/VSP_042452|||http://purl.uniprot.org/annotation/VSP_042453|||http://purl.uniprot.org/annotation/VSP_043218|||http://purl.uniprot.org/annotation/VSP_044343|||http://purl.uniprot.org/annotation/VSP_044344|||http://purl.uniprot.org/annotation/VSP_055710|||http://purl.uniprot.org/annotation/VSP_055711
http://togogenome.org/gene/9606:SIGLEC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PQ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014953|||http://purl.uniprot.org/annotation/VAR_014259|||http://purl.uniprot.org/annotation/VAR_020088|||http://purl.uniprot.org/annotation/VAR_020089|||http://purl.uniprot.org/annotation/VAR_024501|||http://purl.uniprot.org/annotation/VAR_049931|||http://purl.uniprot.org/annotation/VAR_049932|||http://purl.uniprot.org/annotation/VAR_049933|||http://purl.uniprot.org/annotation/VAR_049934|||http://purl.uniprot.org/annotation/VAR_049935|||http://purl.uniprot.org/annotation/VAR_061327|||http://purl.uniprot.org/annotation/VSP_002566
http://togogenome.org/gene/9606:H4C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:FRRS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0K9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  DOMON|||DOMON domain-containing protein FRRS1L|||Disordered|||Helical|||In DEE37.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228720|||http://purl.uniprot.org/annotation/VAR_077052
http://togogenome.org/gene/9606:TCHHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QJ38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||Polar residues|||Trichohyalin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341543|||http://purl.uniprot.org/annotation/VAR_044083
http://togogenome.org/gene/9606:FABP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDY5|||http://purl.uniprot.org/uniprot/P05413                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, heart|||N-acetylvaline|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by Tyr-kinases|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067321|||http://purl.uniprot.org/annotation/VAR_061165
http://togogenome.org/gene/9606:SLC17A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDX2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In DFNA25.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Vesicular|||Vesicular glutamate transporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331614|||http://purl.uniprot.org/annotation/VAR_042905|||http://purl.uniprot.org/annotation/VAR_054130|||http://purl.uniprot.org/annotation/VAR_054131|||http://purl.uniprot.org/annotation/VAR_054132|||http://purl.uniprot.org/annotation/VSP_033265
http://togogenome.org/gene/9606:JAK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52333                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  About 40% loss of STAT5a activation.|||About 80% loss of STAT5a activation.|||FERM|||In T(-)B(+)NK(-) SCID.|||In T(-)B(+)NK(-) SCID; constitutive phosphorylation.|||In T(-)B(+)NK(-) SCID; lack of phosphorylation in response to cytokine stimulation.|||In T(-)B(+)NK(-) SCID; likely benign variant.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 1.|||In isoform 3.|||Interaction with cytokine/interferon/growth hormone receptors|||More than 90% loss of STAT5a activation.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||SH2; atypical|||Strong decrease of JAK3 phosphorylation.|||Tyrosine-protein kinase JAK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088115|||http://purl.uniprot.org/annotation/VAR_006284|||http://purl.uniprot.org/annotation/VAR_010492|||http://purl.uniprot.org/annotation/VAR_010493|||http://purl.uniprot.org/annotation/VAR_010494|||http://purl.uniprot.org/annotation/VAR_010495|||http://purl.uniprot.org/annotation/VAR_010496|||http://purl.uniprot.org/annotation/VAR_010497|||http://purl.uniprot.org/annotation/VAR_010498|||http://purl.uniprot.org/annotation/VAR_019336|||http://purl.uniprot.org/annotation/VAR_019337|||http://purl.uniprot.org/annotation/VAR_019338|||http://purl.uniprot.org/annotation/VAR_019339|||http://purl.uniprot.org/annotation/VAR_041722|||http://purl.uniprot.org/annotation/VAR_041723|||http://purl.uniprot.org/annotation/VAR_041724|||http://purl.uniprot.org/annotation/VAR_041725|||http://purl.uniprot.org/annotation/VAR_041726|||http://purl.uniprot.org/annotation/VSP_004989|||http://purl.uniprot.org/annotation/VSP_054165|||http://purl.uniprot.org/annotation/VSP_054166
http://togogenome.org/gene/9606:PINLYP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC86                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||UPAR/Ly6|||phospholipase A2 inhibitor and Ly6/PLAUR domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332737|||http://purl.uniprot.org/annotation/VSP_044188|||http://purl.uniprot.org/annotation/VSP_044189|||http://purl.uniprot.org/annotation/VSP_044190
http://togogenome.org/gene/9606:RERE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2R6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Arginine-glutamic acid dipeptide repeats protein|||BAH|||Basic and acidic residues|||Disordered|||ELM2|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDBEH; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083504|||http://purl.uniprot.org/annotation/VAR_077007|||http://purl.uniprot.org/annotation/VAR_077008|||http://purl.uniprot.org/annotation/VAR_077009|||http://purl.uniprot.org/annotation/VAR_077010|||http://purl.uniprot.org/annotation/VSP_016878
http://togogenome.org/gene/9606:APLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ1                                                                                  ^@                                                                                  Molecule Processing|||Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Apelin-13|||Apelin-28|||Apelin-31|||Apelin-36|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001759|||http://purl.uniprot.org/annotation/PRO_0000001760|||http://purl.uniprot.org/annotation/PRO_0000001761|||http://purl.uniprot.org/annotation/PRO_0000001762|||http://purl.uniprot.org/annotation/PRO_0000001763
http://togogenome.org/gene/9606:MRGBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MRG/MORF4L-binding protein|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215876
http://togogenome.org/gene/9606:SRP72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76094|||http://purl.uniprot.org/uniprot/V9HWK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Diminished RNA binding.|||Disordered|||Does not affect RNA binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In BMFS1; affects protein localization to ER.|||In isoform 2.|||Loss of RNA binding.|||Loss of interaction with SRP68.|||Loss of interaction with SRP68. Diminished localization to endoplasmic reticulum.|||Loss of interaction with SRP72; when associated with A-598 in SRP68.|||N-acetylalanine|||No impact on RNA binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding|||Reduced interaction with SRP68.|||Reduced interaction with SRP68. Diminished localization to endoplasmic reticulum.|||Removed|||Required for interaction with SRP68|||Required for the interaction with the SRP68/7SL RNA complex|||Signal recognition particle SRP72 subunit RNA-binding|||Signal recognition particle subunit SRP72|||Stronger interaction with SRP68.|||Strongly reduced RNA binding.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135234|||http://purl.uniprot.org/annotation/VAR_068522|||http://purl.uniprot.org/annotation/VSP_045576
http://togogenome.org/gene/9606:PSMD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48556|||http://purl.uniprot.org/uniprot/V9HW09                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||PCI|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173846
http://togogenome.org/gene/9606:AP5Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43299                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-5 complex subunit zeta-1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261357|||http://purl.uniprot.org/annotation/VAR_049511|||http://purl.uniprot.org/annotation/VSP_021672|||http://purl.uniprot.org/annotation/VSP_021673|||http://purl.uniprot.org/annotation/VSP_021674|||http://purl.uniprot.org/annotation/VSP_021675|||http://purl.uniprot.org/annotation/VSP_021676
http://togogenome.org/gene/9606:EPG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTI0|||http://purl.uniprot.org/uniprot/Q9HCE0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ectopic P granules protein 5 homolog|||In VICIS.|||In VICIS; relatively mild phenotype characterized by absence or later onset of cardiac or immunologic features; a normally spliced transcript with the missense variant and multiple misspliced transcripts are detected in patient cells; results in 50% decrease of mRNA levels in patient cells most probably due to nonsense-mediated decay of misspliced transcripts.|||In VICIS; unknown pathological significance.|||In VICIS; unknown pathological significance; associated in cis with P-457.|||In VICIS; unknown pathological significance; associated in cis with P-784.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306255|||http://purl.uniprot.org/annotation/VAR_035278|||http://purl.uniprot.org/annotation/VAR_035279|||http://purl.uniprot.org/annotation/VAR_035280|||http://purl.uniprot.org/annotation/VAR_035281|||http://purl.uniprot.org/annotation/VAR_035282|||http://purl.uniprot.org/annotation/VAR_035283|||http://purl.uniprot.org/annotation/VAR_036525|||http://purl.uniprot.org/annotation/VAR_036526|||http://purl.uniprot.org/annotation/VAR_036527|||http://purl.uniprot.org/annotation/VAR_062210|||http://purl.uniprot.org/annotation/VAR_069224|||http://purl.uniprot.org/annotation/VAR_081369|||http://purl.uniprot.org/annotation/VAR_081370|||http://purl.uniprot.org/annotation/VAR_081371|||http://purl.uniprot.org/annotation/VAR_081372|||http://purl.uniprot.org/annotation/VAR_081373|||http://purl.uniprot.org/annotation/VAR_081374|||http://purl.uniprot.org/annotation/VAR_081375|||http://purl.uniprot.org/annotation/VAR_081376|||http://purl.uniprot.org/annotation/VAR_081377|||http://purl.uniprot.org/annotation/VAR_081378|||http://purl.uniprot.org/annotation/VAR_081379|||http://purl.uniprot.org/annotation/VAR_081380|||http://purl.uniprot.org/annotation/VAR_081381|||http://purl.uniprot.org/annotation/VAR_081382|||http://purl.uniprot.org/annotation/VAR_081383|||http://purl.uniprot.org/annotation/VAR_081384|||http://purl.uniprot.org/annotation/VAR_081385|||http://purl.uniprot.org/annotation/VAR_081386|||http://purl.uniprot.org/annotation/VAR_081387|||http://purl.uniprot.org/annotation/VAR_081388|||http://purl.uniprot.org/annotation/VAR_081389|||http://purl.uniprot.org/annotation/VAR_081390|||http://purl.uniprot.org/annotation/VSP_028435
http://togogenome.org/gene/9606:KIAA2012                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C5G6                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:FLT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35916                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Cytoplasmic|||Decreases autophosphorylation on tyrosine residues upon ligand binding. Abolishes autophosphorylation on tyrosine residues upon ligand binding; when associated with E-446 and A-516.|||Decreases autophosphorylation on tyrosine residues upon ligand binding; when associated with A-516. Abolishes autophosphorylation on tyrosine residues upon ligand binding; when associated with A-516 and A-737.|||Decreases autophosphorylation on tyrosine residues upon ligand binding; when associated with E-446. Abolishes autophosphorylation on tyrosine residues upon ligand binding; when associated with E-446 and A-737.|||Disordered|||Extracellular|||Global loss of autophosphorylation. Abolishes stimulation of cell proliferation and cell migration.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In CHTD7.|||In CHTD7; unknown pathological significance.|||In HCI.|||In LMPHM1.|||In LMPHM1; loss of kinase activity.|||In LMPHM1; recessive form.|||In LMPHM1; recessive form; results in reduced autophosphorylation; results in impaired ligand-induced receptor internalization and downstream signaling.|||In a metastatic melanoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration.|||Loss of phosphorylation site. Reduced autophosphorylation.|||Loss of phosphorylation site. Slightly reduced autophosphorylation.|||Loss of phosphorylation site. Strongly reduces stimulation of cell proliferation and cell migration.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis and SRC|||Probable disease-associated variant found in sporadic congenital lymphedema; de novo mutation.|||Protein kinase|||Proton acceptor|||Reduced autophosphorylation. Strongly reduces stimulation of cell proliferation and cell migration.|||Vascular endothelial growth factor receptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016776|||http://purl.uniprot.org/annotation/VAR_018407|||http://purl.uniprot.org/annotation/VAR_018408|||http://purl.uniprot.org/annotation/VAR_018409|||http://purl.uniprot.org/annotation/VAR_018410|||http://purl.uniprot.org/annotation/VAR_018411|||http://purl.uniprot.org/annotation/VAR_018412|||http://purl.uniprot.org/annotation/VAR_018413|||http://purl.uniprot.org/annotation/VAR_018414|||http://purl.uniprot.org/annotation/VAR_018415|||http://purl.uniprot.org/annotation/VAR_018416|||http://purl.uniprot.org/annotation/VAR_018417|||http://purl.uniprot.org/annotation/VAR_034379|||http://purl.uniprot.org/annotation/VAR_042062|||http://purl.uniprot.org/annotation/VAR_042063|||http://purl.uniprot.org/annotation/VAR_042064|||http://purl.uniprot.org/annotation/VAR_042065|||http://purl.uniprot.org/annotation/VAR_042066|||http://purl.uniprot.org/annotation/VAR_042067|||http://purl.uniprot.org/annotation/VAR_042068|||http://purl.uniprot.org/annotation/VAR_074044|||http://purl.uniprot.org/annotation/VAR_074045|||http://purl.uniprot.org/annotation/VAR_074046|||http://purl.uniprot.org/annotation/VAR_074047|||http://purl.uniprot.org/annotation/VAR_074048|||http://purl.uniprot.org/annotation/VAR_074049|||http://purl.uniprot.org/annotation/VAR_074050|||http://purl.uniprot.org/annotation/VAR_074051|||http://purl.uniprot.org/annotation/VAR_083806|||http://purl.uniprot.org/annotation/VAR_083807|||http://purl.uniprot.org/annotation/VAR_083808|||http://purl.uniprot.org/annotation/VAR_083809|||http://purl.uniprot.org/annotation/VAR_083810|||http://purl.uniprot.org/annotation/VAR_083811|||http://purl.uniprot.org/annotation/VAR_083812|||http://purl.uniprot.org/annotation/VAR_083813|||http://purl.uniprot.org/annotation/VSP_041993|||http://purl.uniprot.org/annotation/VSP_041994|||http://purl.uniprot.org/annotation/VSP_041995
http://togogenome.org/gene/9606:PTGER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43116                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Prostaglandin E2 receptor EP2 subtype                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070054
http://togogenome.org/gene/9606:FAM89A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM89A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271761
http://togogenome.org/gene/9606:HSD17B11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBQ5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Estradiol 17-beta-dehydrogenase 11|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031970
http://togogenome.org/gene/9606:KMT2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEZ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||Abolishes interaction with S-adenosyl-L-methionine.|||Asymmetric dimethylarginine|||Basic and acidic residues|||C2HC pre-PHD-type 1; degenerate|||C2HC pre-PHD-type 2|||Confers a WRAD-dependent gain-of-function histone H3 dimethylation activity. Converts H3K4me1 into H3K4me2.|||DHHC|||Disordered|||FYR C-terminal|||FYR N-terminal|||Histone-lysine N-methyltransferase 2C|||In KLEFS2.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4|||PHD-type 5|||PHD-type 6|||PHD-type 7|||PHD-type 8|||Phosphoserine|||Polar residues|||Post-SET|||Pro residues|||RING-type|||SET|||WDR5 interaction motif (WIN)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124879|||http://purl.uniprot.org/annotation/VAR_017117|||http://purl.uniprot.org/annotation/VAR_017118|||http://purl.uniprot.org/annotation/VAR_036311|||http://purl.uniprot.org/annotation/VAR_036312|||http://purl.uniprot.org/annotation/VAR_036313|||http://purl.uniprot.org/annotation/VAR_036314|||http://purl.uniprot.org/annotation/VAR_057360|||http://purl.uniprot.org/annotation/VAR_057361|||http://purl.uniprot.org/annotation/VAR_057362|||http://purl.uniprot.org/annotation/VAR_057363|||http://purl.uniprot.org/annotation/VAR_057364|||http://purl.uniprot.org/annotation/VAR_061911|||http://purl.uniprot.org/annotation/VAR_061912|||http://purl.uniprot.org/annotation/VAR_080246|||http://purl.uniprot.org/annotation/VAR_080247|||http://purl.uniprot.org/annotation/VAR_080248|||http://purl.uniprot.org/annotation/VSP_008562|||http://purl.uniprot.org/annotation/VSP_036223
http://togogenome.org/gene/9606:CHMP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW88|||http://purl.uniprot.org/uniprot/B2RE76|||http://purl.uniprot.org/uniprot/Q9UQN3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Charged multivesicular body protein 2b|||Disordered|||In FTDALS7.|||In FTDALS7; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A overall indicating a defect in the autophagic pathway.|||In FTDALS7; cells expressing the mutant protein have large cytoplasmic vacuoles with an accumulation of the mutant protein on the outer membrane termed halos; cells with the mutant protein also have aberrant localization of CD63 and an increase in MAP1LC3A1 overall indicating a defect in the autophagic pathway.|||In isoform 2.|||MIT-interacting motif|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211469|||http://purl.uniprot.org/annotation/VAR_023383|||http://purl.uniprot.org/annotation/VAR_038373|||http://purl.uniprot.org/annotation/VAR_038374|||http://purl.uniprot.org/annotation/VAR_068689|||http://purl.uniprot.org/annotation/VSP_045142
http://togogenome.org/gene/9606:ADAM18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAI3|||http://purl.uniprot.org/uniprot/Q9Y3Q7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 18|||EGF-like|||Extracellular|||Helical|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029096|||http://purl.uniprot.org/annotation/PRO_0000029097|||http://purl.uniprot.org/annotation/VAR_051588|||http://purl.uniprot.org/annotation/VAR_066312|||http://purl.uniprot.org/annotation/VAR_066313|||http://purl.uniprot.org/annotation/VAR_066314|||http://purl.uniprot.org/annotation/VAR_066315|||http://purl.uniprot.org/annotation/VAR_066316|||http://purl.uniprot.org/annotation/VSP_012033|||http://purl.uniprot.org/annotation/VSP_043285|||http://purl.uniprot.org/annotation/VSP_043286
http://togogenome.org/gene/9606:RPL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30050                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Large ribosomal subunit protein uL11|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000104456|||http://purl.uniprot.org/annotation/VSP_034695
http://togogenome.org/gene/9606:IL2RG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31785                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytokine receptor common subunit gamma|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||In XCID.|||In XSCID.|||In XSCID; atypical.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010866|||http://purl.uniprot.org/annotation/VAR_002668|||http://purl.uniprot.org/annotation/VAR_002669|||http://purl.uniprot.org/annotation/VAR_002670|||http://purl.uniprot.org/annotation/VAR_002671|||http://purl.uniprot.org/annotation/VAR_002672|||http://purl.uniprot.org/annotation/VAR_002673|||http://purl.uniprot.org/annotation/VAR_002674|||http://purl.uniprot.org/annotation/VAR_002675|||http://purl.uniprot.org/annotation/VAR_002676|||http://purl.uniprot.org/annotation/VAR_002677|||http://purl.uniprot.org/annotation/VAR_002678|||http://purl.uniprot.org/annotation/VAR_002679|||http://purl.uniprot.org/annotation/VAR_002680|||http://purl.uniprot.org/annotation/VAR_002681|||http://purl.uniprot.org/annotation/VAR_002682|||http://purl.uniprot.org/annotation/VAR_002683|||http://purl.uniprot.org/annotation/VAR_002684|||http://purl.uniprot.org/annotation/VAR_002685|||http://purl.uniprot.org/annotation/VAR_002686|||http://purl.uniprot.org/annotation/VAR_002687|||http://purl.uniprot.org/annotation/VAR_002688|||http://purl.uniprot.org/annotation/VAR_002689|||http://purl.uniprot.org/annotation/VAR_002690|||http://purl.uniprot.org/annotation/VAR_002691|||http://purl.uniprot.org/annotation/VAR_002692|||http://purl.uniprot.org/annotation/VAR_002693|||http://purl.uniprot.org/annotation/VAR_002694|||http://purl.uniprot.org/annotation/VAR_002695|||http://purl.uniprot.org/annotation/VAR_002696|||http://purl.uniprot.org/annotation/VAR_002697|||http://purl.uniprot.org/annotation/VAR_002698|||http://purl.uniprot.org/annotation/VAR_002699|||http://purl.uniprot.org/annotation/VAR_002701|||http://purl.uniprot.org/annotation/VAR_002702|||http://purl.uniprot.org/annotation/VAR_020611|||http://purl.uniprot.org/annotation/VAR_059301|||http://purl.uniprot.org/annotation/VSP_047581|||http://purl.uniprot.org/annotation/VSP_047582
http://togogenome.org/gene/9606:OR4F15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW41|||http://purl.uniprot.org/uniprot/Q8NGB8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150549
http://togogenome.org/gene/9606:OR10H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVU5|||http://purl.uniprot.org/uniprot/Q9Y4A9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150702|||http://purl.uniprot.org/annotation/VAR_024127|||http://purl.uniprot.org/annotation/VAR_054124|||http://purl.uniprot.org/annotation/VAR_054125
http://togogenome.org/gene/9606:ACTR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61158                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Actin-related protein 3|||N-acetylalanine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089079
http://togogenome.org/gene/9606:CYP17A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05093|||http://purl.uniprot.org/uniprot/Q1HB44                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In AH5.|||In AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity.|||In AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities.|||In AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities.|||In AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity.|||In AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity.|||In AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation.|||In AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities.|||In AH5; partial loss of activity.|||In AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity.|||Increases the affinity for progesterone, resulting in preferential hydroxylation of progesterone at C17 over C16; increases the catalytic efficiency in the 17,20 lyase reaction.|||Steroid 17-alpha-hydroxylase/17,20 lyase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051931|||http://purl.uniprot.org/annotation/PRO_5014308298|||http://purl.uniprot.org/annotation/VAR_001270|||http://purl.uniprot.org/annotation/VAR_001271|||http://purl.uniprot.org/annotation/VAR_001272|||http://purl.uniprot.org/annotation/VAR_001273|||http://purl.uniprot.org/annotation/VAR_001274|||http://purl.uniprot.org/annotation/VAR_001275|||http://purl.uniprot.org/annotation/VAR_001276|||http://purl.uniprot.org/annotation/VAR_001277|||http://purl.uniprot.org/annotation/VAR_001278|||http://purl.uniprot.org/annotation/VAR_001279|||http://purl.uniprot.org/annotation/VAR_001280|||http://purl.uniprot.org/annotation/VAR_011755|||http://purl.uniprot.org/annotation/VAR_013147|||http://purl.uniprot.org/annotation/VAR_022745|||http://purl.uniprot.org/annotation/VAR_022746|||http://purl.uniprot.org/annotation/VAR_022747|||http://purl.uniprot.org/annotation/VAR_022748|||http://purl.uniprot.org/annotation/VAR_022749|||http://purl.uniprot.org/annotation/VAR_022750|||http://purl.uniprot.org/annotation/VAR_022751|||http://purl.uniprot.org/annotation/VAR_022752|||http://purl.uniprot.org/annotation/VAR_022753|||http://purl.uniprot.org/annotation/VAR_022754|||http://purl.uniprot.org/annotation/VAR_022755|||http://purl.uniprot.org/annotation/VAR_022756|||http://purl.uniprot.org/annotation/VAR_022757|||http://purl.uniprot.org/annotation/VAR_073043|||http://purl.uniprot.org/annotation/VAR_073044|||http://purl.uniprot.org/annotation/VAR_073045|||http://purl.uniprot.org/annotation/VAR_073046|||http://purl.uniprot.org/annotation/VAR_073047
http://togogenome.org/gene/9606:USP17L13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JLJ4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421089
http://togogenome.org/gene/9606:ASB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8I2|||http://purl.uniprot.org/uniprot/Q8WXI3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 10|||In GLC1F; uncertain pathological significance.|||In isoform 2.|||In isoform 3.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066942|||http://purl.uniprot.org/annotation/VAR_022090|||http://purl.uniprot.org/annotation/VAR_069867|||http://purl.uniprot.org/annotation/VAR_069868|||http://purl.uniprot.org/annotation/VAR_069869|||http://purl.uniprot.org/annotation/VAR_069870|||http://purl.uniprot.org/annotation/VAR_069871|||http://purl.uniprot.org/annotation/VAR_069872|||http://purl.uniprot.org/annotation/VAR_069873|||http://purl.uniprot.org/annotation/VAR_069874|||http://purl.uniprot.org/annotation/VAR_069875|||http://purl.uniprot.org/annotation/VAR_069876|||http://purl.uniprot.org/annotation/VAR_069877|||http://purl.uniprot.org/annotation/VAR_069878|||http://purl.uniprot.org/annotation/VAR_069879|||http://purl.uniprot.org/annotation/VAR_069880|||http://purl.uniprot.org/annotation/VAR_069881|||http://purl.uniprot.org/annotation/VAR_069882|||http://purl.uniprot.org/annotation/VAR_069883|||http://purl.uniprot.org/annotation/VAR_069884|||http://purl.uniprot.org/annotation/VAR_069885|||http://purl.uniprot.org/annotation/VAR_069886|||http://purl.uniprot.org/annotation/VAR_069887|||http://purl.uniprot.org/annotation/VAR_069888|||http://purl.uniprot.org/annotation/VAR_069889|||http://purl.uniprot.org/annotation/VAR_069890|||http://purl.uniprot.org/annotation/VAR_069891|||http://purl.uniprot.org/annotation/VAR_082796|||http://purl.uniprot.org/annotation/VAR_082797|||http://purl.uniprot.org/annotation/VAR_082798|||http://purl.uniprot.org/annotation/VSP_023357|||http://purl.uniprot.org/annotation/VSP_038997
http://togogenome.org/gene/9606:ORMDL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FV1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||ORM1-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215636
http://togogenome.org/gene/9606:NYAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Involved in CYFIP1- and NCKAP1-binding|||Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325830|||http://purl.uniprot.org/annotation/VAR_039933|||http://purl.uniprot.org/annotation/VAR_039934|||http://purl.uniprot.org/annotation/VSP_032431|||http://purl.uniprot.org/annotation/VSP_032432|||http://purl.uniprot.org/annotation/VSP_032433|||http://purl.uniprot.org/annotation/VSP_032434|||http://purl.uniprot.org/annotation/VSP_032435
http://togogenome.org/gene/9606:UPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z634|||http://purl.uniprot.org/uniprot/O95045                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Nucleoside phosphorylase|||Redox-active|||Uridine phosphorylase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063193|||http://purl.uniprot.org/annotation/VAR_024431|||http://purl.uniprot.org/annotation/VAR_034580|||http://purl.uniprot.org/annotation/VSP_043756
http://togogenome.org/gene/9606:TSPO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGU0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Translocator protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292005|||http://purl.uniprot.org/annotation/VSP_026363|||http://purl.uniprot.org/annotation/VSP_026364
http://togogenome.org/gene/9606:NLRP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMW2                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  NLR family pyrin domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433153
http://togogenome.org/gene/9606:SHMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJQ3|||http://purl.uniprot.org/uniprot/B4DLV4|||http://purl.uniprot.org/uniprot/P34897|||http://purl.uniprot.org/uniprot/Q5BJF5|||http://purl.uniprot.org/uniprot/Q5HYG8|||http://purl.uniprot.org/uniprot/V9HW06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes pyridoxal phosphate-binding, leading to oxidative phosphorylation deficiency.|||Abolishes serine hydroxymethyltransferase activity, leading to oxidative phosphorylation deficiency; when associated with F-106.|||Abolishes serine hydroxymethyltransferase activity, leading to oxidative phosphorylation deficiency; when associated with L-98.|||Decreased succinylation level and hydroxymethyltransferase activity.|||Disordered|||Does not affect succinylation level or hydroxymethyltransferase activity.|||In NEDCASB; no effect on protein abundance; decreased glycine hydroxymethyltransferase activity; associated with altered mitochondrial redox metabolism.|||In NEDCASB; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Polar residues|||Serine hydroxymethyltransferase, mitochondrial|||Serine hydroxymethyltransferase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032562|||http://purl.uniprot.org/annotation/VAR_085466|||http://purl.uniprot.org/annotation/VAR_085467|||http://purl.uniprot.org/annotation/VAR_085468|||http://purl.uniprot.org/annotation/VAR_085469|||http://purl.uniprot.org/annotation/VAR_085470|||http://purl.uniprot.org/annotation/VAR_085471|||http://purl.uniprot.org/annotation/VSP_043088|||http://purl.uniprot.org/annotation/VSP_043844
http://togogenome.org/gene/9606:SOCS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75159                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abrogates the ability to induce EGFR degradation.|||Abrogates the interaction with ELOB and ELOC and the ability to suppress EGFR signaling; when associated with F-488.|||Abrogates the interaction with ELOB and ELOC and the ability to suppress EGFR signaling; when associated with P-484.|||Basic and acidic residues|||Disordered|||Required for interaction with IL4R|||SH2|||SOCS box|||Suppressor of cytokine signaling 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181249
http://togogenome.org/gene/9606:SLC25A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75746                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal domain|||Carrier domain|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Electrogenic aspartate/glutamate antiporter SLC25A12, mitochondrial|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In DEE39; decreased antiporter activity; significant loss in ability to transport aspartate or glutamate; no effect on localization to mitochondrial inner membrane; no effect on protein abundance.|||In DEE39; loss of antiporter activity; unable to transport aspartate or glutamate; no effect on localization to mitochondrial inner membrane; no effect on protein abundance.|||In isoform 2.|||Linker loop domain|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Regulatory N-terminal domain|||Removed|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090598|||http://purl.uniprot.org/annotation/VAR_047917|||http://purl.uniprot.org/annotation/VAR_063253|||http://purl.uniprot.org/annotation/VAR_071976|||http://purl.uniprot.org/annotation/VSP_054469
http://togogenome.org/gene/9606:CD177                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVM2|||http://purl.uniprot.org/uniprot/Q8N6Q3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mass|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CD177 antigen|||GPI-anchor amidated glycine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6|||UPAR/Ly6 1|||UPAR/Ly6 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231643|||http://purl.uniprot.org/annotation/PRO_0000231644|||http://purl.uniprot.org/annotation/PRO_5001831972|||http://purl.uniprot.org/annotation/VAR_025858|||http://purl.uniprot.org/annotation/VAR_025859|||http://purl.uniprot.org/annotation/VAR_025860|||http://purl.uniprot.org/annotation/VAR_026156|||http://purl.uniprot.org/annotation/VAR_026157|||http://purl.uniprot.org/annotation/VAR_026158|||http://purl.uniprot.org/annotation/VAR_079754|||http://purl.uniprot.org/annotation/VAR_079755|||http://purl.uniprot.org/annotation/VAR_079756|||http://purl.uniprot.org/annotation/VSP_017858|||http://purl.uniprot.org/annotation/VSP_017859|||http://purl.uniprot.org/annotation/VSP_017860|||http://purl.uniprot.org/annotation/VSP_017861
http://togogenome.org/gene/9606:IFRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12894                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Interferon-related developmental regulator 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153289|||http://purl.uniprot.org/annotation/VAR_029302
http://togogenome.org/gene/9606:CACNA1I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium ion selectivity and permeability|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; lower channel deactivation kinetics compared to wild type.|||In NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; lower channel deactivation kinetics compared to wild type; when expressed in chromaffin cells it affects the mode of action potential firing.|||In NEDSIS; gain-of-function variant; affects voltage-gated calcium channel activity by altering channel gating properties; changes current kinetics and left-shifts the voltage dependence of activation; when expressed in chromaffin cells it affects the mode of action potential firing.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Voltage-dependent T-type calcium channel subunit alpha-1I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053957|||http://purl.uniprot.org/annotation/VAR_013883|||http://purl.uniprot.org/annotation/VAR_013884|||http://purl.uniprot.org/annotation/VAR_020050|||http://purl.uniprot.org/annotation/VAR_048745|||http://purl.uniprot.org/annotation/VAR_087825|||http://purl.uniprot.org/annotation/VAR_087826|||http://purl.uniprot.org/annotation/VAR_087827|||http://purl.uniprot.org/annotation/VAR_087828|||http://purl.uniprot.org/annotation/VSP_000950|||http://purl.uniprot.org/annotation/VSP_000951
http://togogenome.org/gene/9606:SUV39H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5I1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chromo|||Histone-lysine N-methyltransferase SUV39H2|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||In isoform 2.|||Phosphoserine|||Post-SET|||Pre-SET|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186059|||http://purl.uniprot.org/annotation/VAR_036344|||http://purl.uniprot.org/annotation/VSP_002209|||http://purl.uniprot.org/annotation/VSP_002210
http://togogenome.org/gene/9606:PPP3R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LZ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Calcineurin A binding|||Calcineurin subunit B type 2|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Interaction with PxVP motif in substrates of the catalytic subunit|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073499
http://togogenome.org/gene/9606:BOLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9W6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DAZ|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Protein boule-like|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081494|||http://purl.uniprot.org/annotation/VSP_009444|||http://purl.uniprot.org/annotation/VSP_009445|||http://purl.uniprot.org/annotation/VSP_009446|||http://purl.uniprot.org/annotation/VSP_036805|||http://purl.uniprot.org/annotation/VSP_055382|||http://purl.uniprot.org/annotation/VSP_055383
http://togogenome.org/gene/9606:SPRYD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW59                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  B30.2/SPRY|||N6-acetyllysine|||N6-succinyllysine|||SPRY domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240856|||http://purl.uniprot.org/annotation/VAR_051381
http://togogenome.org/gene/9606:SPIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JUX0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Histone H3K4me3 and H3R8me2a binding|||In isoform 2.|||Spindlin-3|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259591|||http://purl.uniprot.org/annotation/VSP_021482|||http://purl.uniprot.org/annotation/VSP_021483
http://togogenome.org/gene/9606:GANC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWC5|||http://purl.uniprot.org/uniprot/E7EWB6|||http://purl.uniprot.org/uniprot/H3BN99|||http://purl.uniprot.org/uniprot/Q8TET4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycoside hydrolase family 31 N-terminal|||Neutral alpha-glucosidase C|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185364|||http://purl.uniprot.org/annotation/VAR_018984|||http://purl.uniprot.org/annotation/VAR_018985|||http://purl.uniprot.org/annotation/VAR_018986|||http://purl.uniprot.org/annotation/VAR_018987|||http://purl.uniprot.org/annotation/VAR_018988|||http://purl.uniprot.org/annotation/VAR_018989|||http://purl.uniprot.org/annotation/VAR_056237
http://togogenome.org/gene/9606:PRSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07477                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Alpha-trypsin chain 1|||Alpha-trypsin chain 2|||Charge relay system|||In PCTT.|||In PCTT; Lys-79 trypsin activates anionic trypsinogen PRSS2 2-fold while the common pancreatitis-associated mutants His-122 or Ile-29 have no such effect.|||In PCTT; associated with Ile-29; the double mutant shows increased autocatalytic activation which is solely due to the Ile-29 mutation.|||In PCTT; disrupts signal sequence cleavage site.|||In PCTT; increased rate of activation.|||In PCTT; suppresses an autocleavage site which is probably part of a fail-safe mechanism by which trypsin, which is activated within the pancreas, may be inactivated; loss of this cleavage site would permit autodigestion resulting in pancreatitis.|||In PCTT; suppresses an autocleavage site.|||In a colorectal cancer sample; somatic mutation.|||Lack of sulfation.|||Peptidase S1|||Required for specificity|||Serine protease 1|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028197|||http://purl.uniprot.org/annotation/PRO_0000028198|||http://purl.uniprot.org/annotation/PRO_0000313570|||http://purl.uniprot.org/annotation/PRO_0000313571|||http://purl.uniprot.org/annotation/VAR_006720|||http://purl.uniprot.org/annotation/VAR_006721|||http://purl.uniprot.org/annotation/VAR_011652|||http://purl.uniprot.org/annotation/VAR_011653|||http://purl.uniprot.org/annotation/VAR_011654|||http://purl.uniprot.org/annotation/VAR_011655|||http://purl.uniprot.org/annotation/VAR_011656|||http://purl.uniprot.org/annotation/VAR_011693|||http://purl.uniprot.org/annotation/VAR_012712|||http://purl.uniprot.org/annotation/VAR_012713|||http://purl.uniprot.org/annotation/VAR_036299|||http://purl.uniprot.org/annotation/VAR_037908|||http://purl.uniprot.org/annotation/VAR_037909
http://togogenome.org/gene/9606:ZNF703                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7S9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Removed|||Zinc finger protein 703                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047702
http://togogenome.org/gene/9606:FGD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9G1|||http://purl.uniprot.org/uniprot/Q5JSP0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 3|||FYVE-type|||In isoform 2.|||In isoform 3.|||PH|||PH 1|||PH 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080944|||http://purl.uniprot.org/annotation/VAR_021492|||http://purl.uniprot.org/annotation/VSP_013074|||http://purl.uniprot.org/annotation/VSP_013075|||http://purl.uniprot.org/annotation/VSP_055703
http://togogenome.org/gene/9606:CEP70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG2|||http://purl.uniprot.org/uniprot/B7Z2D2|||http://purl.uniprot.org/uniprot/Q8NHQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 70 kDa|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089497|||http://purl.uniprot.org/annotation/VAR_021177|||http://purl.uniprot.org/annotation/VAR_061590|||http://purl.uniprot.org/annotation/VSP_012745|||http://purl.uniprot.org/annotation/VSP_012746|||http://purl.uniprot.org/annotation/VSP_012747|||http://purl.uniprot.org/annotation/VSP_042140|||http://purl.uniprot.org/annotation/VSP_042141
http://togogenome.org/gene/9606:TFF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03403                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  P-type 1|||P-type 2|||Trefoil factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023460|||http://purl.uniprot.org/annotation/VAR_053564
http://togogenome.org/gene/9606:RMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZD4|||http://purl.uniprot.org/uniprot/B7Z201|||http://purl.uniprot.org/uniprot/B7Z2Y1|||http://purl.uniprot.org/uniprot/B7Z3Q1|||http://purl.uniprot.org/uniprot/K7ENL9|||http://purl.uniprot.org/uniprot/Q96DM3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Mic1|||Regulator of MON1-CCZ1 complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096481
http://togogenome.org/gene/9606:KRTAP13-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI77                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 10 AA approximate repeats|||Keratin-associated protein 13-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185204|||http://purl.uniprot.org/annotation/VAR_047849|||http://purl.uniprot.org/annotation/VAR_053472
http://togogenome.org/gene/9606:ZNF664-RFLNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||Pro residues|||Refilin-A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274331|||http://purl.uniprot.org/annotation/VSP_022713
http://togogenome.org/gene/9606:IL22RA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969J5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Critical for IL22-binding|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2 and isoform 3.|||In isoform 3.|||Interleukin-22 receptor subunit alpha-2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011016|||http://purl.uniprot.org/annotation/VAR_021493|||http://purl.uniprot.org/annotation/VAR_021494|||http://purl.uniprot.org/annotation/VSP_013105|||http://purl.uniprot.org/annotation/VSP_013106|||http://purl.uniprot.org/annotation/VSP_013107
http://togogenome.org/gene/9606:NLGN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSB7|||http://purl.uniprot.org/uniprot/A0A8I5QJH8|||http://purl.uniprot.org/uniprot/B7Z3P8|||http://purl.uniprot.org/uniprot/Q4G160|||http://purl.uniprot.org/uniprot/Q6MZK0|||http://purl.uniprot.org/uniprot/Q9NZ94|||http://purl.uniprot.org/uniprot/X5D2P6|||http://purl.uniprot.org/uniprot/X5D7L6|||http://purl.uniprot.org/uniprot/X5DNV3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carboxylesterase type B|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AUTSX1.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuroligin-3|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008645|||http://purl.uniprot.org/annotation/PRO_5004238719|||http://purl.uniprot.org/annotation/PRO_5004953874|||http://purl.uniprot.org/annotation/PRO_5004955886|||http://purl.uniprot.org/annotation/PRO_5014316170|||http://purl.uniprot.org/annotation/VAR_015668|||http://purl.uniprot.org/annotation/VAR_068887|||http://purl.uniprot.org/annotation/VAR_068888|||http://purl.uniprot.org/annotation/VAR_068889|||http://purl.uniprot.org/annotation/VAR_068890|||http://purl.uniprot.org/annotation/VSP_007534|||http://purl.uniprot.org/annotation/VSP_053827
http://togogenome.org/gene/9606:PCSK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16549                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||P/Homo B|||Peptidase S8|||Proprotein convertase subtilisin/kexin type 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027114|||http://purl.uniprot.org/annotation/PRO_0000027115|||http://purl.uniprot.org/annotation/VAR_044419|||http://purl.uniprot.org/annotation/VAR_044420|||http://purl.uniprot.org/annotation/VAR_044421|||http://purl.uniprot.org/annotation/VAR_044422|||http://purl.uniprot.org/annotation/VAR_044423
http://togogenome.org/gene/9606:LUZP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P127                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arg-rich; required for RNA-binding|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Interaction with DDX39B/UAP56|||Interaction with NXF1|||Leucine zipper protein 4|||Leucine-zipper; required for RNA-binding and for its relocalization to the cytoplasm during cell division|||Phosphoserine|||Polar residues|||RS-containing His-rich (RS-H); necessary for nuclear localization|||UAP56-binding motif (UBM); required for proper nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288649|||http://purl.uniprot.org/annotation/VAR_051146|||http://purl.uniprot.org/annotation/VAR_051147|||http://purl.uniprot.org/annotation/VSP_053926|||http://purl.uniprot.org/annotation/VSP_053927
http://togogenome.org/gene/9606:STRN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GV6|||http://purl.uniprot.org/uniprot/Q9NRL3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Calmodulin-binding|||Caveolin-binding|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Striatin N-terminal|||Striatin-4|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051239|||http://purl.uniprot.org/annotation/VAR_053419|||http://purl.uniprot.org/annotation/VSP_056170|||http://purl.uniprot.org/annotation/VSP_056171|||http://purl.uniprot.org/annotation/VSP_056172|||http://purl.uniprot.org/annotation/VSP_056738
http://togogenome.org/gene/9606:CTSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07339|||http://purl.uniprot.org/uniprot/V9HWI3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Associated with increased risk for AD; possibly influences secretion and intracellular maturation.|||Cathepsin D|||Cathepsin D heavy chain|||Cathepsin D light chain|||In CLN10.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025949|||http://purl.uniprot.org/annotation/PRO_0000025950|||http://purl.uniprot.org/annotation/PRO_0000025951|||http://purl.uniprot.org/annotation/PRO_0000025952|||http://purl.uniprot.org/annotation/PRO_5014314732|||http://purl.uniprot.org/annotation/VAR_011621|||http://purl.uniprot.org/annotation/VAR_029362|||http://purl.uniprot.org/annotation/VAR_029363|||http://purl.uniprot.org/annotation/VAR_058490
http://togogenome.org/gene/9606:UGT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16880                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  2-hydroxyacylsphingosine 1-beta-galactosyltransferase|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036064|||http://purl.uniprot.org/annotation/VAR_052466|||http://purl.uniprot.org/annotation/VAR_052467
http://togogenome.org/gene/9606:ARIH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95376|||http://purl.uniprot.org/uniprot/Q53ET9|||http://purl.uniprot.org/uniprot/Q6IBL8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity.|||Acidic residues|||Ariadne domain|||Disordered|||Does not affect interaction with UBE2L3.|||E3 ubiquitin-protein ligase ARIH2|||IBR-type|||Loss of effect in myelopoiesis.|||Loss of effect in myelopoiesis. Abolishes interaction with UBE2L3.|||Phosphoserine|||RING-type|||RING-type 1|||RING-type 2; atypical|||Reduced interaction with neddylated CUL5; when associated with 84-A--A-86.|||Reduced interaction with neddylated CUL5; when associated with A-100.|||TRIAD supradomain|||UBA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055755|||http://purl.uniprot.org/annotation/VAR_054105|||http://purl.uniprot.org/annotation/VAR_054106
http://togogenome.org/gene/9606:SLC2A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11169                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Confers moderate fructose transport activity.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Important for selectivity against fructose|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Solute carrier family 2, facilitated glucose transporter member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050353|||http://purl.uniprot.org/annotation/VAR_052502
http://togogenome.org/gene/9606:TMEM38B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRS4|||http://purl.uniprot.org/uniprot/Q9NVV0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical;Name=1|||Helical;Name=2|||Helical;Name=3|||Helical;Name=4|||Helical;Name=5|||Helical;Name=6|||Helical;Name=7|||Lumenal|||Phosphoserine|||Trimeric intracellular cation channel type B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291524|||http://purl.uniprot.org/annotation/VAR_032811
http://togogenome.org/gene/9606:IRGQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZA9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IRG-type G|||Immunity-related GTPase family Q protein|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264463
http://togogenome.org/gene/9606:DYRK1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6I6|||http://purl.uniprot.org/uniprot/Q13627                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protein kinase activity.|||Basic residues|||Bipartite nuclear localization signal|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 1A|||Histidine-rich domain (HRD)|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mildly reduces kinase activity. Does not abolish autophosphorylation on tyrosine residues.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085931|||http://purl.uniprot.org/annotation/VAR_009395|||http://purl.uniprot.org/annotation/VAR_009396|||http://purl.uniprot.org/annotation/VAR_040453|||http://purl.uniprot.org/annotation/VSP_004917|||http://purl.uniprot.org/annotation/VSP_004918|||http://purl.uniprot.org/annotation/VSP_004919|||http://purl.uniprot.org/annotation/VSP_004920|||http://purl.uniprot.org/annotation/VSP_004921|||http://purl.uniprot.org/annotation/VSP_004922|||http://purl.uniprot.org/annotation/VSP_004923
http://togogenome.org/gene/9606:ZNF235                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14590                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 235                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047474|||http://purl.uniprot.org/annotation/VAR_029806|||http://purl.uniprot.org/annotation/VSP_022166
http://togogenome.org/gene/9606:C20orf204                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTL2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Uncharacterized protein C20orf204                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5008408615
http://togogenome.org/gene/9606:CEP135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66GS9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 135 kDa|||Disordered|||In isoform 2.|||Interchain|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089491|||http://purl.uniprot.org/annotation/VAR_057785|||http://purl.uniprot.org/annotation/VSP_012743|||http://purl.uniprot.org/annotation/VSP_012744
http://togogenome.org/gene/9606:SLC6A17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1V8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MRT48.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Sodium-dependent neutral amino acid transporter SLC6A17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214803|||http://purl.uniprot.org/annotation/VAR_061814|||http://purl.uniprot.org/annotation/VAR_073371|||http://purl.uniprot.org/annotation/VAR_073372
http://togogenome.org/gene/9606:C1QTNF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003531|||http://purl.uniprot.org/annotation/VSP_011624|||http://purl.uniprot.org/annotation/VSP_011625|||http://purl.uniprot.org/annotation/VSP_043157
http://togogenome.org/gene/9606:CFAP144                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NL82                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 144|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340271
http://togogenome.org/gene/9606:HMX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0J4|||http://purl.uniprot.org/uniprot/Q9NP08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||HMX family specific domain 1|||HMX family specific domain 2|||Homeobox|||Homeobox protein HMX1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278453
http://togogenome.org/gene/9606:LMAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPY7|||http://purl.uniprot.org/uniprot/Q12907                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||L-type lectin-like|||Lumenal|||N-linked (GlcNAc...) asparagine|||Vesicular integral-membrane protein VIP36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017666|||http://purl.uniprot.org/annotation/PRO_5033362500
http://togogenome.org/gene/9606:STPG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM74|||http://purl.uniprot.org/uniprot/Q8N7X2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Protein STPG3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325615|||http://purl.uniprot.org/annotation/VAR_039898|||http://purl.uniprot.org/annotation/VSP_059447|||http://purl.uniprot.org/annotation/VSP_059448|||http://purl.uniprot.org/annotation/VSP_059449
http://togogenome.org/gene/9606:PYCR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQS1|||http://purl.uniprot.org/uniprot/B4DGI7|||http://purl.uniprot.org/uniprot/Q53H96                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Pyrroline-5-carboxylate reductase 3|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Pyrroline-5-carboxylate reductase dimerisation|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324561|||http://purl.uniprot.org/annotation/VAR_039828|||http://purl.uniprot.org/annotation/VAR_039829|||http://purl.uniprot.org/annotation/VAR_039830|||http://purl.uniprot.org/annotation/VSP_057219
http://togogenome.org/gene/9606:DDIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35638|||http://purl.uniprot.org/uniprot/Q53YD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BZIP|||Basic and acidic residues|||Basic motif|||DNA damage-inducible transcript 3 protein|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with TRIB3|||Leucine-zipper|||N-terminal|||Phosphoserine; by CK2|||Phosphoserine; by MAPK14|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076642|||http://purl.uniprot.org/annotation/VAR_036000|||http://purl.uniprot.org/annotation/VSP_047277
http://togogenome.org/gene/9606:GRIPAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4V328                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Disordered|||GRASP-1 C-terminal chain|||GRIP1-associated protein 1|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087581|||http://purl.uniprot.org/annotation/PRO_0000441811|||http://purl.uniprot.org/annotation/VAR_080637|||http://purl.uniprot.org/annotation/VSP_015700|||http://purl.uniprot.org/annotation/VSP_015702|||http://purl.uniprot.org/annotation/VSP_015703|||http://purl.uniprot.org/annotation/VSP_015704|||http://purl.uniprot.org/annotation/VSP_015705
http://togogenome.org/gene/9606:FXYD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H4X8|||http://purl.uniprot.org/uniprot/Q96DB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FXYD domain-containing ion transport regulator|||FXYD domain-containing ion transport regulator 5|||Helical|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010369|||http://purl.uniprot.org/annotation/PRO_5013982299|||http://purl.uniprot.org/annotation/VAR_012349|||http://purl.uniprot.org/annotation/VAR_027959|||http://purl.uniprot.org/annotation/VSP_001584
http://togogenome.org/gene/9606:CLDN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75508                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-11|||Cytoplasmic|||Extracellular|||Helical|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144760
http://togogenome.org/gene/9606:COLCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS62|||http://purl.uniprot.org/uniprot/W0FBW3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Colorectal cancer-associated protein 1|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340692
http://togogenome.org/gene/9606:TMEM175                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6UWG6|||http://purl.uniprot.org/uniprot/Q9BSA9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished interaction with LAMP1 and subsequent inhibition.|||Abolished potassium channel activity and decreased proton channel activity.|||Abolished potassium channel activity without affecting proton channel activity.|||Abolished proton and potassium channel activity.|||Abolished proton and potassium channel activity; when associated with M-271.|||Abolished proton permeability without altering potassium permeability.|||Associated with decreased risk for Parkinson disease; gain-of-function variant; does not affect lysosomal localization.|||Associated with increased risk for Parkinson disease; reduced potassium channel activity; does not affect lysosomal localization.|||Cytoplasmic|||Decreased channel activity.|||Decreased selectivity for potassium ion.|||Decreased selectivity for potassium ion. Abolished proton and potassium channel activity. Decreased selectivity for potassium ion; when associated with 45-A--A-49.|||Decreased selectivity for potassium ion; when associated with A-274.|||Disordered|||Does not affect potassium channel activity.|||Does not affect proton and potassium channel activity.|||Does not affect selectivity; when associated with A-275.|||Does not affect selectivity; when associated with A-278.|||Does not affect selectivity; when associated with A-50.|||Does not affect selectivity; when associated with A-53.|||Endosomal/lysosomal proton channel TMEM175|||Helical|||Helical; Name=TM1-1|||Helical; Name=TM1-2|||Helical; Name=TM2-1|||Helical; Name=TM2-2|||Helical; Name=TM3-1|||Helical; Name=TM3-2|||Helical; Name=TM4-1|||Helical; Name=TM4-2|||Helical; Name=TM5-1|||Helical; Name=TM5-2|||Helical; Name=TM6-1|||Helical; Name=TM6-2|||Hydrophobic filter residue 1-1|||Hydrophobic filter residue 1-2|||Hydrophobic filter residue 2-1|||Hydrophobic filter residue 2-2|||Hydrophobic filter residue 3-1|||Hydrophobic filter residue 3-2|||Impaired potassium channel activity.|||Impaired selectivity; can conduct both K(+) and Na(+); when associated with N-271.|||Impaired selectivity; can conduct both K(+) and Na(+); when associated with N-46.|||In isoform 2.|||Increased potassium and proton channel activity.|||Lumenal|||Phosphothreonine|||Reduced channel activation, probably caused by decreased interaction with AKT1; when associated with A-241.|||Reduced channel activation, probably caused by decreased interaction with AKT1; when associated with A-338.|||Reduced potassium and proton channel activity.|||Reduced potassium channel activity without affecting proton channel activity.|||Reduced potassium channel activity without altering proton channel activity.|||Reduced potassium channel activity.|||RxxxFSD motif 1|||RxxxFSD motif 2|||Short helix H1-1|||Short helix H1-2|||Short helix H2-1|||Short helix H2-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282588|||http://purl.uniprot.org/annotation/VAR_053873|||http://purl.uniprot.org/annotation/VAR_053874|||http://purl.uniprot.org/annotation/VSP_024213
http://togogenome.org/gene/9606:NAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4Z6T7|||http://purl.uniprot.org/uniprot/P11245                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Arylamine N-acetyltransferase 2|||Helical|||In allele NAT2*14A, allele NAT2*14B, allele NAT2*14C, allele NAT2*14D, allele NAT2*14E, allele NAT2*14F and allele NAT2*14G; a slow acetylator.|||In allele NAT2*17.|||In allele NAT2*18.|||In allele NAT2*19.|||In allele NAT2*5A, allele NAT2*5B, allele NAT2*5C, allele NAT2*5D, allele NAT2*5E, allele NAT2*5F, allele NAT2*14B and allele NAT2*14E; a slow acetylator.|||In allele NAT2*5A, allele NAT2*5D, allele NAT2*5E, allele NAT2*6A, allele NAT2*6B, allele NAT2*6D, allele NAT2*7A, allele NAT2*7B, NAT2*14A, allele NAT2*14B, allele NAT2*14D, allele NAT2*17, allele NAT2*18, allele NAT2*19.|||In allele NAT2*5E, allele NAT2*6A, allele NAT2*6B, allele NAT2*6C, allele NAT2*6D and allele NAT2*14D; a slow acetylator.|||In allele NAT2*7A and allele NAT2*7B; a slow acetylator.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107905|||http://purl.uniprot.org/annotation/VAR_004608|||http://purl.uniprot.org/annotation/VAR_004609|||http://purl.uniprot.org/annotation/VAR_004610|||http://purl.uniprot.org/annotation/VAR_004611|||http://purl.uniprot.org/annotation/VAR_004612|||http://purl.uniprot.org/annotation/VAR_009075|||http://purl.uniprot.org/annotation/VAR_009076|||http://purl.uniprot.org/annotation/VAR_009077|||http://purl.uniprot.org/annotation/VAR_018853|||http://purl.uniprot.org/annotation/VAR_018854|||http://purl.uniprot.org/annotation/VAR_020385|||http://purl.uniprot.org/annotation/VAR_020386|||http://purl.uniprot.org/annotation/VAR_028781|||http://purl.uniprot.org/annotation/VAR_028782|||http://purl.uniprot.org/annotation/VAR_046905|||http://purl.uniprot.org/annotation/VAR_061368
http://togogenome.org/gene/9606:ABHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RC89|||http://purl.uniprot.org/uniprot/P08910                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Monoacylglycerol lipase ABHD2|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212457|||http://purl.uniprot.org/annotation/VAR_031203
http://togogenome.org/gene/9606:ELMOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ELMO|||ELMO domain-containing protein 3|||In DFNA81; perturbed subcellular location with loss of colocalization with F-actin in the cytoplasm and concentration in the nucleus; may also have a shorter half-life than the wild-type protein.|||In DFNB88; perturbed subcellular location with loss of targeting to stereocilia and concentration in the nucleus; loss of ARL2 GAP activity.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274903|||http://purl.uniprot.org/annotation/VAR_030362|||http://purl.uniprot.org/annotation/VAR_030363|||http://purl.uniprot.org/annotation/VAR_070125|||http://purl.uniprot.org/annotation/VAR_086112|||http://purl.uniprot.org/annotation/VSP_022918|||http://purl.uniprot.org/annotation/VSP_022919|||http://purl.uniprot.org/annotation/VSP_022920|||http://purl.uniprot.org/annotation/VSP_022922|||http://purl.uniprot.org/annotation/VSP_022923|||http://purl.uniprot.org/annotation/VSP_022924
http://togogenome.org/gene/9606:TFB2M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5Q4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||DNA-binding|||Dimethyladenosine transferase 2, mitochondrial|||Disordered|||Impairs transcription initiation; when associated with A-330.|||Impairs transcription initiation; when associated with A-331.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273179|||http://purl.uniprot.org/annotation/VAR_030097|||http://purl.uniprot.org/annotation/VAR_030098|||http://purl.uniprot.org/annotation/VAR_071249|||http://purl.uniprot.org/annotation/VAR_071250
http://togogenome.org/gene/9606:RNF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z229|||http://purl.uniprot.org/uniprot/Q9UBS8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||D-box|||E3 ubiquitin-protein ligase RNF14|||IBR-type|||In isoform 2.|||Interaction with androgen receptor|||Loss of interaction with UBE2E2 and of autoubiquitination.|||Phosphoserine|||RING-type|||RING-type 1|||RING-type 2; atypical|||RWD|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056057|||http://purl.uniprot.org/annotation/VSP_045780
http://togogenome.org/gene/9606:H2BC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99877                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-N|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071830
http://togogenome.org/gene/9606:OR13J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGT2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150741|||http://purl.uniprot.org/annotation/VAR_053304
http://togogenome.org/gene/9606:PCDHGA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003958|||http://purl.uniprot.org/annotation/VAR_048560|||http://purl.uniprot.org/annotation/VSP_008669|||http://purl.uniprot.org/annotation/VSP_008670
http://togogenome.org/gene/9606:ZNF726                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5GK09|||http://purl.uniprot.org/uniprot/A6NNF4|||http://purl.uniprot.org/uniprot/E9PLI7|||http://purl.uniprot.org/uniprot/F1T0F3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 726                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340682|||http://purl.uniprot.org/annotation/VSP_061120
http://togogenome.org/gene/9606:DIPK1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUD6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Divergent protein kinase domain 1B|||Helical|||In isoform 2.|||Lumenal|||May mediate ER retention                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287231|||http://purl.uniprot.org/annotation/VAR_032295|||http://purl.uniprot.org/annotation/VSP_025405
http://togogenome.org/gene/9606:CCAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX12                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cell division cycle and apoptosis regulator protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with AR|||Interaction with GATA1|||Interaction with GATA2|||Phosphoserine|||Phosphothreonine|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233148|||http://purl.uniprot.org/annotation/VAR_035497|||http://purl.uniprot.org/annotation/VAR_058330|||http://purl.uniprot.org/annotation/VAR_058331|||http://purl.uniprot.org/annotation/VAR_058332|||http://purl.uniprot.org/annotation/VSP_037736
http://togogenome.org/gene/9606:TBC1D16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208044|||http://purl.uniprot.org/annotation/VAR_052542|||http://purl.uniprot.org/annotation/VSP_053995|||http://purl.uniprot.org/annotation/VSP_053996|||http://purl.uniprot.org/annotation/VSP_055665|||http://purl.uniprot.org/annotation/VSP_055666|||http://purl.uniprot.org/annotation/VSP_055667|||http://purl.uniprot.org/annotation/VSP_055668
http://togogenome.org/gene/9606:SRXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYN0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Interchain|||No effect on association with PRDX1, PRDX2, PRDX3 or PRDX4.|||Omega-N-methylarginine|||Phosphoserine|||Sulfiredoxin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211431
http://togogenome.org/gene/9606:DCXR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4W1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  L-xylulose reductase|||Loss of function. Probably due to defects in formation of the active site and binding of coenzyme.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054554
http://togogenome.org/gene/9606:ATP9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR18|||http://purl.uniprot.org/uniprot/O75110|||http://purl.uniprot.org/uniprot/Q2NLD0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Extracellular|||Helical|||In NEDGBA.|||In NEDGBA; results in the formation of aggregated puncta distributed in the cytoplasm.|||In NEDGBA; severely reduced mRNA expression in homozygous patient cells.|||In isoform Short.|||N-acetylthreonine|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Probable phospholipid-transporting ATPase IIA|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046375|||http://purl.uniprot.org/annotation/VAR_088107|||http://purl.uniprot.org/annotation/VAR_088108|||http://purl.uniprot.org/annotation/VAR_088109|||http://purl.uniprot.org/annotation/VAR_088110|||http://purl.uniprot.org/annotation/VSP_000432
http://togogenome.org/gene/9606:ZYX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15942|||http://purl.uniprot.org/uniprot/Q96AF9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93.|||In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||N-acetylalanine|||N6-acetyllysine|||No targeting to focal adhesions and reduced actin-rich structures; when associated with A-71; A-93 and A-104.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced interaction with ENAH and VASP.|||Removed|||Zyxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075913|||http://purl.uniprot.org/annotation/VAR_034081|||http://purl.uniprot.org/annotation/VSP_057288
http://togogenome.org/gene/9606:NEU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3R4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Motif|||Mutagenesis Site|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BNR 1|||BNR 2|||FRIP motif|||Loss of enzyme activity.|||No effect on enzyme activity.|||Nucleophile|||Proton acceptor|||Reduced activity; increased sensitivity to inhibition by oseltamivir carboxylate.|||Sialidase-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208899|||http://purl.uniprot.org/annotation/VAR_024461|||http://purl.uniprot.org/annotation/VAR_024462|||http://purl.uniprot.org/annotation/VAR_049204|||http://purl.uniprot.org/annotation/VAR_055311|||http://purl.uniprot.org/annotation/VAR_055312
http://togogenome.org/gene/9606:LZTS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y250                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Leucine zipper putative tumor suppressor 1|||N-myristoyl glycine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182971|||http://purl.uniprot.org/annotation/VAR_018274|||http://purl.uniprot.org/annotation/VAR_018275|||http://purl.uniprot.org/annotation/VAR_018276|||http://purl.uniprot.org/annotation/VAR_053490|||http://purl.uniprot.org/annotation/VSP_009940|||http://purl.uniprot.org/annotation/VSP_009941|||http://purl.uniprot.org/annotation/VSP_009942|||http://purl.uniprot.org/annotation/VSP_009943|||http://purl.uniprot.org/annotation/VSP_009944|||http://purl.uniprot.org/annotation/VSP_009945|||http://purl.uniprot.org/annotation/VSP_009946
http://togogenome.org/gene/9606:FZD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14332|||http://purl.uniprot.org/uniprot/Q86UZ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Found in a patient with features of Robinow syndrome; unknown pathological significance.|||Frizzled-2|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In OMOD2.|||In OMOD2; also found in a patient with features of Robinow syndrome.|||In OMOD2; decreased Wnt signaling.|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Probable disease-associated variant found in a patient with features of Robinow syndrome.|||Strongly reduced interaction with C.difficile toxin TcdB.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012978|||http://purl.uniprot.org/annotation/VAR_081993|||http://purl.uniprot.org/annotation/VAR_081994|||http://purl.uniprot.org/annotation/VAR_081995|||http://purl.uniprot.org/annotation/VAR_083242|||http://purl.uniprot.org/annotation/VAR_083243|||http://purl.uniprot.org/annotation/VAR_083244
http://togogenome.org/gene/9606:CLDN24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NM45                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Putative claudin-24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320201|||http://purl.uniprot.org/annotation/VAR_055660
http://togogenome.org/gene/9606:TP53INP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXH6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||LIR|||Phosphoserine|||Polar residues|||Pro residues|||Tumor protein p53-inducible nuclear protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072409
http://togogenome.org/gene/9606:ENO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNW6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Enolase 4|||In isoform 2.|||In isoform 4.|||Pro residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348454|||http://purl.uniprot.org/annotation/VSP_059947|||http://purl.uniprot.org/annotation/VSP_059948|||http://purl.uniprot.org/annotation/VSP_059949|||http://purl.uniprot.org/annotation/VSP_059950|||http://purl.uniprot.org/annotation/VSP_059951
http://togogenome.org/gene/9606:PHF21A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BD5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IDDBCS.|||In IDDBCS; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||PHD finger protein 21A|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for transcriptional repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226767|||http://purl.uniprot.org/annotation/VAR_025515|||http://purl.uniprot.org/annotation/VAR_083199|||http://purl.uniprot.org/annotation/VAR_083200|||http://purl.uniprot.org/annotation/VSP_017448|||http://purl.uniprot.org/annotation/VSP_017449
http://togogenome.org/gene/9606:KIF26B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2KJY2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with spinocerebellar ataxia; unknown pathological significance.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF26B|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307301|||http://purl.uniprot.org/annotation/VAR_080730|||http://purl.uniprot.org/annotation/VSP_028687|||http://purl.uniprot.org/annotation/VSP_028693
http://togogenome.org/gene/9606:MAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04201|||http://purl.uniprot.org/uniprot/W8W3P4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fails to activate GNA11.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Proto-oncogene Mas                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069714
http://togogenome.org/gene/9606:SLC22A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75751                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreased TEA uptake.|||Helical|||N-linked (GlcNAc...) asparagine|||Proline-rich sequence|||Solute carrier family 22 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220503|||http://purl.uniprot.org/annotation/VAR_020351|||http://purl.uniprot.org/annotation/VAR_020352
http://togogenome.org/gene/9606:CRAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MD53|||http://purl.uniprot.org/uniprot/B2RNX8|||http://purl.uniprot.org/uniprot/Q96RY5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Protein cramped-like|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264471
http://togogenome.org/gene/9606:TPST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60507                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Interaction with peptide substrate|||Loss of one glycosylation site. Loss of N-glycosylation; when associated with A-262.|||Loss of one glycosylation site. Loss of N-glycosylation; when associated with A-60.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein-tyrosine sulfotransferase 1|||Proton donor/acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189826
http://togogenome.org/gene/9606:MTUS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In HCC.|||In HNSCC cell lines.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Microtubule-associated tumor suppressor 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305197|||http://purl.uniprot.org/annotation/VAR_035173|||http://purl.uniprot.org/annotation/VAR_035174|||http://purl.uniprot.org/annotation/VAR_035175|||http://purl.uniprot.org/annotation/VAR_035176|||http://purl.uniprot.org/annotation/VAR_035177|||http://purl.uniprot.org/annotation/VAR_035178|||http://purl.uniprot.org/annotation/VAR_035179|||http://purl.uniprot.org/annotation/VAR_035180|||http://purl.uniprot.org/annotation/VAR_035181|||http://purl.uniprot.org/annotation/VAR_035182|||http://purl.uniprot.org/annotation/VAR_035183|||http://purl.uniprot.org/annotation/VAR_035184|||http://purl.uniprot.org/annotation/VSP_028270|||http://purl.uniprot.org/annotation/VSP_028271|||http://purl.uniprot.org/annotation/VSP_028272|||http://purl.uniprot.org/annotation/VSP_028273|||http://purl.uniprot.org/annotation/VSP_028274|||http://purl.uniprot.org/annotation/VSP_028275|||http://purl.uniprot.org/annotation/VSP_028276|||http://purl.uniprot.org/annotation/VSP_028277|||http://purl.uniprot.org/annotation/VSP_028278|||http://purl.uniprot.org/annotation/VSP_044849
http://togogenome.org/gene/9606:AHCYL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HN2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenosylhomocysteinase 3|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LISN domain, inhibits interaction with ITPR1|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116909|||http://purl.uniprot.org/annotation/VSP_040095|||http://purl.uniprot.org/annotation/VSP_043185|||http://purl.uniprot.org/annotation/VSP_043186|||http://purl.uniprot.org/annotation/VSP_046278|||http://purl.uniprot.org/annotation/VSP_046279
http://togogenome.org/gene/9606:SEL1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protein sel-1 homolog 3|||Sel1-like 1|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5|||Sel1-like 6|||Sel1-like 7|||Sel1-like 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321894|||http://purl.uniprot.org/annotation/VAR_039369|||http://purl.uniprot.org/annotation/VAR_053965|||http://purl.uniprot.org/annotation/VAR_053966|||http://purl.uniprot.org/annotation/VAR_053967|||http://purl.uniprot.org/annotation/VAR_053968|||http://purl.uniprot.org/annotation/VSP_031811|||http://purl.uniprot.org/annotation/VSP_031812
http://togogenome.org/gene/9606:PCDHGC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-C5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003989|||http://purl.uniprot.org/annotation/VAR_024394|||http://purl.uniprot.org/annotation/VAR_048574|||http://purl.uniprot.org/annotation/VSP_008702|||http://purl.uniprot.org/annotation/VSP_008703
http://togogenome.org/gene/9606:SF3B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGZ4|||http://purl.uniprot.org/uniprot/O75533                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-310.|||Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-338.|||Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-310 and A-338.|||Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-293; A-310 and A-338.|||Abolishes interaction with RBM39; when associated with A-200; A-218; A-254; A-293; A-310 and A-338.|||Abolishes interaction with RBM39; when associated with A-200; A-232; A-254; A-293; A-310 and A-338.|||Abolishes interaction with RBM39; when associated with A-218; A-232; A-254; A-293; A-310 and A-338.|||Basic and acidic residues|||Citrulline|||Disordered|||Does not affect the stability of the SF3B complex interaction with U2AF65. Does not decrease the affinity to RNA.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||Interaction with PHF5A|||Interaction with PPP1R8|||Interaction with RNA|||Interaction with SF3B14|||Interaction with SF3B3|||Interaction with SF3B3 and SF3B5|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on interaction with PPP1R8.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by DYRK1A|||Polar residues|||Slight inhibition of interaction with PPP1R8.|||Splicing factor 3B subunit 1|||U2AF homology region; mediates interaction with RBM39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174323|||http://purl.uniprot.org/annotation/VSP_046182|||http://purl.uniprot.org/annotation/VSP_046183
http://togogenome.org/gene/9606:CCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00622|||http://purl.uniprot.org/uniprot/Q6FI18                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CCN family member 1|||CTCK|||Heparin-binding|||IGFBP N-terminal|||Phosphoserine; by FAM20C|||TSP type-1|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014398|||http://purl.uniprot.org/annotation/PRO_5014310457|||http://purl.uniprot.org/annotation/VAR_018934
http://togogenome.org/gene/9606:HOPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPY8                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Homeobox; atypical|||Homeodomain-only protein|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049129|||http://purl.uniprot.org/annotation/VSP_012659|||http://purl.uniprot.org/annotation/VSP_047290
http://togogenome.org/gene/9606:DNAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P225                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Basic and acidic residues|||Disordered|||Dynein axonemal heavy chain 2|||In RNA edited version.|||In SPGF45; decreased protein abundance; loss of inner dynein arm assembly; in spermatozoa from patients.|||In SPGF45; unknown pathological significance; decreased protein abundance.|||In isoform 2.|||In isoform 3.|||Polar residues|||Stalk|||Stem|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322542|||http://purl.uniprot.org/annotation/VAR_039407|||http://purl.uniprot.org/annotation/VAR_039408|||http://purl.uniprot.org/annotation/VAR_039409|||http://purl.uniprot.org/annotation/VAR_039410|||http://purl.uniprot.org/annotation/VAR_039411|||http://purl.uniprot.org/annotation/VAR_060134|||http://purl.uniprot.org/annotation/VAR_082806|||http://purl.uniprot.org/annotation/VAR_082807|||http://purl.uniprot.org/annotation/VAR_082808|||http://purl.uniprot.org/annotation/VAR_082809|||http://purl.uniprot.org/annotation/VAR_082810|||http://purl.uniprot.org/annotation/VAR_082811|||http://purl.uniprot.org/annotation/VAR_082812|||http://purl.uniprot.org/annotation/VAR_082813|||http://purl.uniprot.org/annotation/VAR_082814|||http://purl.uniprot.org/annotation/VAR_082815|||http://purl.uniprot.org/annotation/VAR_082816|||http://purl.uniprot.org/annotation/VAR_082817|||http://purl.uniprot.org/annotation/VAR_085171|||http://purl.uniprot.org/annotation/VAR_085172|||http://purl.uniprot.org/annotation/VAR_085173|||http://purl.uniprot.org/annotation/VAR_085174|||http://purl.uniprot.org/annotation/VAR_085175|||http://purl.uniprot.org/annotation/VSP_031913|||http://purl.uniprot.org/annotation/VSP_031914|||http://purl.uniprot.org/annotation/VSP_031915|||http://purl.uniprot.org/annotation/VSP_031916|||http://purl.uniprot.org/annotation/VSP_031917|||http://purl.uniprot.org/annotation/VSP_031918
http://togogenome.org/gene/9606:ATXN1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7T5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  AXH|||Ataxin-1-like|||Basic and acidic residues|||Disordered|||Interaction with NCOR2 and ATXN1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343709|||http://purl.uniprot.org/annotation/VAR_044496
http://togogenome.org/gene/9606:FAM177B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6PVY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Protein FAM177B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325915|||http://purl.uniprot.org/annotation/VAR_039953|||http://purl.uniprot.org/annotation/VAR_054090|||http://purl.uniprot.org/annotation/VSP_032476|||http://purl.uniprot.org/annotation/VSP_032477
http://togogenome.org/gene/9606:IBSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21815                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Bone sialoprotein 2|||Cell attachment site|||Disordered|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020330|||http://purl.uniprot.org/annotation/VAR_056579|||http://purl.uniprot.org/annotation/VAR_056580|||http://purl.uniprot.org/annotation/VAR_058014|||http://purl.uniprot.org/annotation/VAR_058015|||http://purl.uniprot.org/annotation/VAR_058016|||http://purl.uniprot.org/annotation/VAR_058017
http://togogenome.org/gene/9606:ZNF670                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BS34                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||KRAB|||Phosphotyrosine|||Zinc finger protein 670                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233989
http://togogenome.org/gene/9606:HAPLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZV7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  Hyaluronan and proteoglycan link protein 2|||Ig-like V-type|||Link 1|||Link 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013187
http://togogenome.org/gene/9606:GCSAML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PLW0|||http://purl.uniprot.org/uniprot/Q5JQS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Germinal center-associated signaling and motility-like protein|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294242|||http://purl.uniprot.org/annotation/VSP_026612
http://togogenome.org/gene/9606:KHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VXA5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||KH homology domain-containing protein 1|||KH; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311358|||http://purl.uniprot.org/annotation/VSP_029543
http://togogenome.org/gene/9606:FAM114A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWE2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein NOXP20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274561|||http://purl.uniprot.org/annotation/VAR_030320|||http://purl.uniprot.org/annotation/VAR_030321|||http://purl.uniprot.org/annotation/VAR_030322|||http://purl.uniprot.org/annotation/VAR_030323|||http://purl.uniprot.org/annotation/VAR_030324|||http://purl.uniprot.org/annotation/VAR_053823|||http://purl.uniprot.org/annotation/VAR_053824|||http://purl.uniprot.org/annotation/VSP_056466
http://togogenome.org/gene/9606:PLSCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRY7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 1.|||In isoform 3.|||Phospholipid scramblase 2|||Phosphothreonine; by PKC|||Proline-rich domain (PRD)|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100787|||http://purl.uniprot.org/annotation/VSP_055239|||http://purl.uniprot.org/annotation/VSP_055240
http://togogenome.org/gene/9606:EIF1AX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47813                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Eukaryotic translation initiation factor 1A, X-chromosomal|||S1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145101
http://togogenome.org/gene/9606:RTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95197                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with BACE1|||Interaction with FADD|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Reticulon|||Reticulon-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168163|||http://purl.uniprot.org/annotation/VAR_031164|||http://purl.uniprot.org/annotation/VAR_057713|||http://purl.uniprot.org/annotation/VSP_023759|||http://purl.uniprot.org/annotation/VSP_023760|||http://purl.uniprot.org/annotation/VSP_023761|||http://purl.uniprot.org/annotation/VSP_045319|||http://purl.uniprot.org/annotation/VSP_045320|||http://purl.uniprot.org/annotation/VSP_047008
http://togogenome.org/gene/9606:ACD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adrenocortical dysplasia protein homolog|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DKCA6 and DKCB7; localizes properly on telomeres; unable to recruit telomerase to the telomeres.|||In DKCB7; localizes properly on telomeres; decreased interaction with TINF2.|||In isoform 2.|||Interaction with POT1|||PWI|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239019|||http://purl.uniprot.org/annotation/VAR_060224|||http://purl.uniprot.org/annotation/VAR_060225|||http://purl.uniprot.org/annotation/VAR_075693|||http://purl.uniprot.org/annotation/VAR_075694|||http://purl.uniprot.org/annotation/VSP_060243
http://togogenome.org/gene/9606:UCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RP3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Urocortin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006239|||http://purl.uniprot.org/annotation/PRO_0000006240
http://togogenome.org/gene/9606:OR6B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95007                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150620|||http://purl.uniprot.org/annotation/VAR_034238
http://togogenome.org/gene/9606:FAM181A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Protein FAM181A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089951|||http://purl.uniprot.org/annotation/VAR_022834|||http://purl.uniprot.org/annotation/VAR_057822|||http://purl.uniprot.org/annotation/VSP_014549
http://togogenome.org/gene/9606:CD47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A1TSG4|||http://purl.uniprot.org/uniprot/Q08722                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform OA3-293.|||In isoform OA3-305.|||In isoform OA3-312.|||Leukocyte surface antigen CD47|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014880|||http://purl.uniprot.org/annotation/PRO_5001990366|||http://purl.uniprot.org/annotation/VSP_002535|||http://purl.uniprot.org/annotation/VSP_002536|||http://purl.uniprot.org/annotation/VSP_002537|||http://purl.uniprot.org/annotation/VSP_002538
http://togogenome.org/gene/9606:SULT1C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75897|||http://purl.uniprot.org/uniprot/Q6PD90                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Proton acceptor|||Sulfotransferase|||Sulfotransferase 1C4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085137|||http://purl.uniprot.org/annotation/VAR_025404|||http://purl.uniprot.org/annotation/VAR_061889|||http://purl.uniprot.org/annotation/VSP_056255
http://togogenome.org/gene/9606:MDK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21741                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  In 35% of the chains.|||In isoform 2.|||Midkine|||Required for high affinity binding to PTRZ1 by interacting with the chondroitin sulfate chains of PTRZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024662|||http://purl.uniprot.org/annotation/VAR_006353|||http://purl.uniprot.org/annotation/VSP_047452
http://togogenome.org/gene/9606:GJC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IDC0|||http://purl.uniprot.org/uniprot/P36383                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction gamma-1 protein|||Gap junction protein cysteine-rich|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057826
http://togogenome.org/gene/9606:ADAMTS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXS8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 14|||Disintegrin|||Disordered|||In isoform B and isoform C.|||In isoform C and isoform D.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Polar residues|||Pro residues|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029190|||http://purl.uniprot.org/annotation/PRO_0000029191|||http://purl.uniprot.org/annotation/VAR_047837|||http://purl.uniprot.org/annotation/VAR_047838|||http://purl.uniprot.org/annotation/VAR_047839|||http://purl.uniprot.org/annotation/VAR_047840|||http://purl.uniprot.org/annotation/VAR_047841|||http://purl.uniprot.org/annotation/VSP_005501|||http://purl.uniprot.org/annotation/VSP_006958
http://togogenome.org/gene/9606:PDZD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15018                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cleavage; by caspases|||Disordered|||In isoform 2.|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ domain-containing protein 2|||Phosphoserine|||Polar residues|||Processed PDZ domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058294|||http://purl.uniprot.org/annotation/PRO_0000302756|||http://purl.uniprot.org/annotation/VAR_031654|||http://purl.uniprot.org/annotation/VAR_031655|||http://purl.uniprot.org/annotation/VAR_031656|||http://purl.uniprot.org/annotation/VAR_031657|||http://purl.uniprot.org/annotation/VAR_031658|||http://purl.uniprot.org/annotation/VAR_031659|||http://purl.uniprot.org/annotation/VAR_061691|||http://purl.uniprot.org/annotation/VSP_012369|||http://purl.uniprot.org/annotation/VSP_012370|||http://purl.uniprot.org/annotation/VSP_012371|||http://purl.uniprot.org/annotation/VSP_012372|||http://purl.uniprot.org/annotation/VSP_012373
http://togogenome.org/gene/9606:CORO7-PAM16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYL4                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  DUF1899|||Disordered|||Polar residues|||WD                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:NKX3-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99801                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-3.1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048945|||http://purl.uniprot.org/annotation/VAR_011612|||http://purl.uniprot.org/annotation/VSP_002230|||http://purl.uniprot.org/annotation/VSP_002231|||http://purl.uniprot.org/annotation/VSP_002232|||http://purl.uniprot.org/annotation/VSP_002233
http://togogenome.org/gene/9606:AURKAIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWT8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Small ribosomal subunit protein mS38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064536|||http://purl.uniprot.org/annotation/VAR_020132
http://togogenome.org/gene/9606:METTL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W50                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished methyltransferase activity in vitro.|||Abolished methyltransferase activity.|||Abolishes methyltransferase activity.|||Disordered|||Does not affect methyltransferase activity.|||Does not affect methyltransferase activity; when associated with A-26.|||Does not affect methyltransferase activity; when associated with A-31.|||Found in patients with large intestine cancer; abolished methyltransferase activity.|||In isoform 2.|||Increased methyltransferase activity in vitro.|||K-loop|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA N6-adenosine-methyltransferase METTL16|||RNA-binding|||Reduced methyltransferase activity.|||VCR 1|||VCR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310767|||http://purl.uniprot.org/annotation/VAR_037086|||http://purl.uniprot.org/annotation/VAR_081134|||http://purl.uniprot.org/annotation/VSP_029340|||http://purl.uniprot.org/annotation/VSP_029341
http://togogenome.org/gene/9606:TEFM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QE5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrion|||Transcription elongation factor, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000406329|||http://purl.uniprot.org/annotation/VAR_045689|||http://purl.uniprot.org/annotation/VSP_040808|||http://purl.uniprot.org/annotation/VSP_040809
http://togogenome.org/gene/9606:TNFRSF10D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBN6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Death; truncated|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 10D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034584|||http://purl.uniprot.org/annotation/VAR_011417|||http://purl.uniprot.org/annotation/VAR_011418|||http://purl.uniprot.org/annotation/VAR_057288|||http://purl.uniprot.org/annotation/VAR_061854
http://togogenome.org/gene/9606:ANP32B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92688                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic leucine-rich nuclear phosphoprotein 32 family member B|||Acidic residues|||Basic and acidic residues|||Complete loss of cleavage by CASP3.|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137595|||http://purl.uniprot.org/annotation/VSP_019304
http://togogenome.org/gene/9606:SLC35A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFI1|||http://purl.uniprot.org/uniprot/A6NKM8|||http://purl.uniprot.org/uniprot/B4DE15|||http://purl.uniprot.org/uniprot/P78381                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport.|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport. No effect on localization to Golgi apparatus.|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport; when associated with A-125, A-126 and A-129. No effect on localization to Golgi apparatus.|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport; when associated with A-125, A-126 and A-278. No effect on localization to Golgi apparatus.|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport; when associated with A-125, A-129 and A-278. No effect on localization to Golgi apparatus.|||Does not rescue defective Gb3Cer expression in SLC35A2-deficient cells suggesting loss of UDP-galactose transport; when associated with A-126, A-129 and A-278. No effect on localization to Golgi apparatus.|||ER retention motif|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||Found in a patient with West syndrome; unknown pathological significance; does not rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||Found in a patient with cerebral visual impairment; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||Found in a patient with infantile spasms and cortical abnormalities; somatic mutation; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||Found in a patient with non-lesional focal epilepsy; somatic mutation; unknown pathological significance; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||Helical|||In CDG2M.|||In CDG2M; fails to rescue defective galactosylation in SLC35A2-deficient cells; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||In CDG2M; has no effect on localization to Golgi; partially rescues defective Gb3Cer expression in SLC35A2-deficient cells.|||In CDG2M; in patient fibroblasts, results in reduced UDP-galactose transport into the Golgi; able to rescue defective Gb3Cer expression in SLC35A2-deficient cells.|||In CDG2M; loss of UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus.|||In CDG2M; no effect on localization to Golgi apparatus.|||In CDG2M; reduced UDP-galactose transport in patient fibroblasts.|||In CDG2M; reduced UDP-galactose transport in patient fibroblasts; no effect on localization to Golgi apparatus.|||In CDG2M; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||No effect on localization to Golgi apparatus.|||Partially rescues defective Gb3Cer expression in SLC35A2-deficient cells suggesting reduced UDP-galactose transport.|||Partially rescues defective Gb3Cer expression in SLC35A2-deficient cells suggesting reduced UDP-galactose transport. No effect on localization to Golgi apparatus.|||UDP-galactose translocator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213353|||http://purl.uniprot.org/annotation/VAR_036579|||http://purl.uniprot.org/annotation/VAR_069773|||http://purl.uniprot.org/annotation/VAR_071699|||http://purl.uniprot.org/annotation/VAR_079035|||http://purl.uniprot.org/annotation/VAR_086839|||http://purl.uniprot.org/annotation/VAR_086840|||http://purl.uniprot.org/annotation/VAR_086841|||http://purl.uniprot.org/annotation/VAR_086842|||http://purl.uniprot.org/annotation/VAR_086843|||http://purl.uniprot.org/annotation/VAR_087467|||http://purl.uniprot.org/annotation/VAR_087468|||http://purl.uniprot.org/annotation/VAR_087469|||http://purl.uniprot.org/annotation/VAR_087470|||http://purl.uniprot.org/annotation/VAR_087471|||http://purl.uniprot.org/annotation/VAR_087472|||http://purl.uniprot.org/annotation/VAR_087473|||http://purl.uniprot.org/annotation/VAR_087474|||http://purl.uniprot.org/annotation/VAR_087475|||http://purl.uniprot.org/annotation/VAR_087476|||http://purl.uniprot.org/annotation/VAR_087477|||http://purl.uniprot.org/annotation/VAR_087478|||http://purl.uniprot.org/annotation/VAR_087479|||http://purl.uniprot.org/annotation/VAR_087480|||http://purl.uniprot.org/annotation/VAR_087481|||http://purl.uniprot.org/annotation/VAR_087482|||http://purl.uniprot.org/annotation/VAR_087483|||http://purl.uniprot.org/annotation/VAR_087484|||http://purl.uniprot.org/annotation/VAR_087485|||http://purl.uniprot.org/annotation/VAR_087486|||http://purl.uniprot.org/annotation/VSP_003728|||http://purl.uniprot.org/annotation/VSP_042029|||http://purl.uniprot.org/annotation/VSP_054335|||http://purl.uniprot.org/annotation/VSP_055197
http://togogenome.org/gene/9606:CBX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45973                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand                                                                                  ^@                                                                                  Abolishes interaction with TRIM28, CHAF1A, NIPBL and HP1BP3, fails to localize to centromeres in mitosis.|||Chromo 1|||Chromo 2; shadow subtype|||Chromobox protein homolog 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||No effect on interaction with POGZ. Abolishes interaction with TRIM28, CHAF1A and NIPBL.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080208
http://togogenome.org/gene/9606:ITM2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZM6|||http://purl.uniprot.org/uniprot/Q9NQX7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Peptide|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BRICHOS|||CT-BRI3|||Cleavage; by furin|||Completely abrogates proteolytic processing.|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Integral membrane protein 2C|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154826|||http://purl.uniprot.org/annotation/PRO_0000232645|||http://purl.uniprot.org/annotation/VAR_022111|||http://purl.uniprot.org/annotation/VSP_013471|||http://purl.uniprot.org/annotation/VSP_013472
http://togogenome.org/gene/9606:RABEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5N1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by GSK3-alpha|||Polar residues|||Rab GTPase-binding effector protein 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187559|||http://purl.uniprot.org/annotation/VSP_010458|||http://purl.uniprot.org/annotation/VSP_010459
http://togogenome.org/gene/9606:BNIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12982                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BCL2/adenovirus E1B 19 kDa protein-interacting protein 2|||CRAL-TRIO|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064961|||http://purl.uniprot.org/annotation/VAR_018837|||http://purl.uniprot.org/annotation/VSP_038964
http://togogenome.org/gene/9606:LIPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTR8|||http://purl.uniprot.org/uniprot/Q9Y5X9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Endothelial lipase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PLAT|||phospholipase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017797|||http://purl.uniprot.org/annotation/PRO_5014085114|||http://purl.uniprot.org/annotation/VAR_017027|||http://purl.uniprot.org/annotation/VAR_017028|||http://purl.uniprot.org/annotation/VAR_017029|||http://purl.uniprot.org/annotation/VAR_034082|||http://purl.uniprot.org/annotation/VSP_013302|||http://purl.uniprot.org/annotation/VSP_013303
http://togogenome.org/gene/9606:PEX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z497|||http://purl.uniprot.org/uniprot/P40855                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to PEX10, PEX11B, PEX12 and PEX13. Does not affect binding to PEX3 and PEX16.|||Abolishes binding to PEX3.|||Abolishes farnesylation. Abolishes PEX19 function on peroxisome biogenesis. Does not affect binding to ABCD1, ABCD2 and ABCD3.|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Docking to the peroxisome membrane and binding to PEX3|||Found in patients with progressive myoclonus epilepsy and dementia; unknown pathological significance.|||In isoform 6.|||N-acetylalanine|||Necessary for PEX19 function on peroxisome biogenesis|||Peroxisomal biogenesis factor 19|||Phosphoserine|||Phosphothreonine|||Removed|||Removed in mature form|||S-farnesyl cysteine|||Slightly inhibits PEX19 function on peroxisome biogenesis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218759|||http://purl.uniprot.org/annotation/PRO_0000393944|||http://purl.uniprot.org/annotation/VAR_085044|||http://purl.uniprot.org/annotation/VSP_061572|||http://purl.uniprot.org/annotation/VSP_061573
http://togogenome.org/gene/9606:KHDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7F0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KH 1|||KH 2|||KH homology domain-containing protein 4|||Phosphoserine|||Polar residues|||Pro residues|||Required for nuclear retention                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296669|||http://purl.uniprot.org/annotation/VSP_027238|||http://purl.uniprot.org/annotation/VSP_027239|||http://purl.uniprot.org/annotation/VSP_027240|||http://purl.uniprot.org/annotation/VSP_027241|||http://purl.uniprot.org/annotation/VSP_027242|||http://purl.uniprot.org/annotation/VSP_027243
http://togogenome.org/gene/9606:SMTNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAL5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Smoothelin-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317278|||http://purl.uniprot.org/annotation/VAR_038498|||http://purl.uniprot.org/annotation/VAR_060164|||http://purl.uniprot.org/annotation/VSP_030931
http://togogenome.org/gene/9606:CRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUF7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation. No effect on localization to the apical cell membrane.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with EPB41L5|||Loss of interaction with PARD6A and PALS1. No effect on interaction with EPB41L5.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Protein crumbs homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021005|||http://purl.uniprot.org/annotation/VSP_013989
http://togogenome.org/gene/9606:PPP1R27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WC6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Protein phosphatase 1 regulatory subunit 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264469
http://togogenome.org/gene/9606:GNLY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3H9|||http://purl.uniprot.org/uniprot/P22749                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Granulysin|||In isoform Short.|||Saposin B-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031659|||http://purl.uniprot.org/annotation/PRO_5014085120|||http://purl.uniprot.org/annotation/VAR_027868|||http://purl.uniprot.org/annotation/VSP_006016
http://togogenome.org/gene/9606:KCNC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14003                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases protein abundance.|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Important for normal N-type inactivation|||In SCA13; alters gating; slows channel closing; decreases protein abundance; no effect on localization to the plasma membrane; no effect on N-glycosylation; no effect on tetramerization.|||In SCA13; changes channel activity; shifts the voltage dependence of activation.|||In SCA13; dominant negative that induces loss of channel activity; decreases protein abundance; decreases protein stability; decreases localization to the plasma membrane and alters the localization of the wild-type protein; impairs N-glycosylation; no effect on tetramerization.|||In SCA13; dominant negative that reduces channel activity; alters gating; decreases protein abundance; decreases localization to the plasma membrane; no effect on tetramerization.|||In SCA13; unknown pathological significance; changes channel activity; shifts the voltage dependence of activation.|||In SCA13; unknown pathological significance; dominant negative that decreases channel activity; decreases protein abundance; decreases protein stability; decreases localization to the plasma membrane; no effect on tetramerization.|||In SCA13; unknown pathological significance; no effect on channel activity.|||In SCA13; unknown pathological significance; reduces channel activity; shifts the voltage dependence of activation.|||Loss of N-type inactivation.|||Loss of interaction with ACTR3. No effect on voltage-dependent channel opening or current amplitude, but decreased rate of inactivation during prolonged depolarization.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Potassium voltage-gated channel subfamily C member 3|||Pro residues|||Selectivity filter|||Variant of uncertain significance; changes channel activity; activates more quickly and deactivates more slowly.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054055|||http://purl.uniprot.org/annotation/VAR_029530|||http://purl.uniprot.org/annotation/VAR_029531|||http://purl.uniprot.org/annotation/VAR_074192|||http://purl.uniprot.org/annotation/VAR_074193|||http://purl.uniprot.org/annotation/VAR_074194|||http://purl.uniprot.org/annotation/VAR_074195|||http://purl.uniprot.org/annotation/VAR_074196|||http://purl.uniprot.org/annotation/VAR_074197|||http://purl.uniprot.org/annotation/VAR_074198|||http://purl.uniprot.org/annotation/VAR_074199|||http://purl.uniprot.org/annotation/VAR_074200|||http://purl.uniprot.org/annotation/VAR_074201|||http://purl.uniprot.org/annotation/VAR_074202|||http://purl.uniprot.org/annotation/VAR_074203
http://togogenome.org/gene/9606:EVA1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWG0|||http://purl.uniprot.org/uniprot/P58658                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Protein eva-1 homolog C|||SUEL-type lectin|||SUEL-type lectin 1|||SUEL-type lectin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017671|||http://purl.uniprot.org/annotation/VSP_003103|||http://purl.uniprot.org/annotation/VSP_003104|||http://purl.uniprot.org/annotation/VSP_055198
http://togogenome.org/gene/9606:USP37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T82                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes deubiquitinase activity.|||Abolishes phosphorylation by CDK2, leading to lower deubiquitinase activity.|||Basic and acidic residues|||D-box 1|||D-box 2|||D-box 3|||Disordered|||Impaired interaction with FZR1/CDH1 and subsequent ubiquitination.|||In isoform 2.|||KEN box 1|||KEN box 2|||KEN box 3|||Loss of phosphorylation following cisplatin treatment.|||No effect.|||Nucleophile|||Phosphoserine|||Phosphoserine; by CDK2|||Polar residues|||Proton acceptor|||UIM 1|||UIM 2|||UIM 3|||USP|||Ubiquitin carboxyl-terminal hydrolase 37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080667|||http://purl.uniprot.org/annotation/VAR_059752|||http://purl.uniprot.org/annotation/VSP_041740|||http://purl.uniprot.org/annotation/VSP_041741
http://togogenome.org/gene/9606:TTC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRC7|||http://purl.uniprot.org/uniprot/Q6P3X3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||Tetratricopeptide repeat protein 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295096|||http://purl.uniprot.org/annotation/VAR_033207|||http://purl.uniprot.org/annotation/VAR_033208|||http://purl.uniprot.org/annotation/VAR_052628|||http://purl.uniprot.org/annotation/VAR_061905
http://togogenome.org/gene/9606:CENPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2Z9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centromere protein S|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||No effect on CENPX- and FANCM-binding; loss of double-stranded DNA-binding of the MHF heterodimer and of FANCM recruitment to fork DNA; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 87-A-A-88.|||Partial loss of CENPX- and FANCM-binding; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 73-A-A-74.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249477|||http://purl.uniprot.org/annotation/VSP_020432|||http://purl.uniprot.org/annotation/VSP_020433|||http://purl.uniprot.org/annotation/VSP_020434
http://togogenome.org/gene/9606:PGAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRR3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Almost abolishes GPI-GalNAc transferase activity. No effect on Golgi apparatus membrane location.|||Cytoplasmic|||DXD motif|||Glycosylated; when associated with A-87.|||Helical|||Loss of GPI-GalNAc transferase activity.|||Loss of glycosylation. Not glycosylated; when associated with N-283. Glycosylated; when associated with N-347.|||Lumenal|||N-linked (GalNAc...) asparagine|||No effect on GPI-GalNAc transferase activity. No effect on Golgi apparatus membrane location.|||Not glycosylated; when associated with A-87.|||Post-GPI attachment to proteins factor 4|||Reduces GPI-GalNAc transferase activity. No effect on Golgi apparatus membrane location.|||Slightly reduces GPI-GalNAc transferase activity. No effect on Golgi apparatus membrane location.|||Strongly reduces GPI-GalNAc transferase activity. Accumulates in the endoplasmic reticulum.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089731
http://togogenome.org/gene/9606:RCOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ40                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Pro residues|||REST corepressor 2|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226776|||http://purl.uniprot.org/annotation/VAR_025516
http://togogenome.org/gene/9606:DNAAF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal assembly factor 8|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294345|||http://purl.uniprot.org/annotation/VAR_033157|||http://purl.uniprot.org/annotation/VAR_033158|||http://purl.uniprot.org/annotation/VAR_033159|||http://purl.uniprot.org/annotation/VAR_033160|||http://purl.uniprot.org/annotation/VAR_033161|||http://purl.uniprot.org/annotation/VAR_033162|||http://purl.uniprot.org/annotation/VAR_033163|||http://purl.uniprot.org/annotation/VAR_061618
http://togogenome.org/gene/9606:CPEB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWY2|||http://purl.uniprot.org/uniprot/Q9BZB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes stress granule assembly and correct localization in dcp1 bodies.|||Cytoplasmic polyadenylation element-binding protein 1|||Disordered|||Does not affect its localization.|||Important for the positionning of RRM1 relative to RRM2|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 3.|||Necessary for stress granule assembly and correct localization in dcp1 bodies|||Phosphoserine|||Phosphothreonine; by AURKA and CAMK2A|||Polar residues|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269251|||http://purl.uniprot.org/annotation/VAR_076387|||http://purl.uniprot.org/annotation/VAR_076388|||http://purl.uniprot.org/annotation/VSP_022027|||http://purl.uniprot.org/annotation/VSP_022028|||http://purl.uniprot.org/annotation/VSP_022029
http://togogenome.org/gene/9606:COBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75128                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||KKRRAP 1|||KKRRAP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein cordon-bleu|||WH2 1|||WH2 2|||WH2 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260491|||http://purl.uniprot.org/annotation/VAR_029043|||http://purl.uniprot.org/annotation/VAR_029044|||http://purl.uniprot.org/annotation/VAR_029045|||http://purl.uniprot.org/annotation/VAR_029046|||http://purl.uniprot.org/annotation/VAR_050894|||http://purl.uniprot.org/annotation/VAR_050895|||http://purl.uniprot.org/annotation/VSP_021607|||http://purl.uniprot.org/annotation/VSP_021608|||http://purl.uniprot.org/annotation/VSP_021609|||http://purl.uniprot.org/annotation/VSP_021610|||http://purl.uniprot.org/annotation/VSP_021611|||http://purl.uniprot.org/annotation/VSP_021612|||http://purl.uniprot.org/annotation/VSP_021613|||http://purl.uniprot.org/annotation/VSP_040711|||http://purl.uniprot.org/annotation/VSP_040712
http://togogenome.org/gene/9606:SPIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5J4                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding                                                                                  ^@                                                                                  ETS|||Transcription factor Spi-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204140
http://togogenome.org/gene/9606:NACA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13765                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine; alternate|||NAC-A/B|||Nascent polypeptide-associated complex subunit alpha|||Phosphoserine|||Phosphoserine; by ILK1|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Polar residues|||RNA/DNA-binding|||Required for DNA-binding|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135576
http://togogenome.org/gene/9606:TNPO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14787|||http://purl.uniprot.org/uniprot/Q05D48|||http://purl.uniprot.org/uniprot/Q4LE60                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Importin N-terminal|||In IDDHISD.|||In isoform 2.|||N6-acetyllysine|||Pro residues|||Transportin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120767|||http://purl.uniprot.org/annotation/VAR_069373|||http://purl.uniprot.org/annotation/VAR_086356|||http://purl.uniprot.org/annotation/VAR_086357|||http://purl.uniprot.org/annotation/VAR_086358|||http://purl.uniprot.org/annotation/VAR_086359|||http://purl.uniprot.org/annotation/VAR_086360|||http://purl.uniprot.org/annotation/VAR_086361|||http://purl.uniprot.org/annotation/VAR_086362|||http://purl.uniprot.org/annotation/VAR_086363|||http://purl.uniprot.org/annotation/VAR_086364|||http://purl.uniprot.org/annotation/VAR_086365|||http://purl.uniprot.org/annotation/VAR_086366|||http://purl.uniprot.org/annotation/VAR_086367|||http://purl.uniprot.org/annotation/VSP_009657
http://togogenome.org/gene/9606:SCML4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S9|||http://purl.uniprot.org/uniprot/B4E0X3|||http://purl.uniprot.org/uniprot/Q8N228                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Polycomb group protein RNA binding region|||SAM|||SLED|||Sex comb on midleg-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337171|||http://purl.uniprot.org/annotation/VAR_043669|||http://purl.uniprot.org/annotation/VSP_033943|||http://purl.uniprot.org/annotation/VSP_033944|||http://purl.uniprot.org/annotation/VSP_033945|||http://purl.uniprot.org/annotation/VSP_033946
http://togogenome.org/gene/9606:OR52K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVF2|||http://purl.uniprot.org/uniprot/Q8NGK4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150781|||http://purl.uniprot.org/annotation/VAR_060038|||http://purl.uniprot.org/annotation/VAR_060039
http://togogenome.org/gene/9606:RETSAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUM9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  All-trans-retinol 13,14-reductase|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225665|||http://purl.uniprot.org/annotation/VAR_025473|||http://purl.uniprot.org/annotation/VAR_059243|||http://purl.uniprot.org/annotation/VAR_059244|||http://purl.uniprot.org/annotation/VSP_017410|||http://purl.uniprot.org/annotation/VSP_017411
http://togogenome.org/gene/9606:RAB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWB9|||http://purl.uniprot.org/uniprot/P51153|||http://purl.uniprot.org/uniprot/Q504R6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region                                                                                  ^@                                                                                  (Microbial infection) N6-stearoyl lysine|||Constitutively active mutant locked in the active GTP-bound form. Impairs transports of cargo from the trans-Golgi network to the recycling endosomes and alters the assembly of functional tight junctions.|||Cysteine methyl ester|||Disordered|||Dominant negative.|||Effector region|||In 3KR mutant; abolished stearoylation in response to S.flexneri infection.|||Phosphoserine|||Ras-related protein Rab-13|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121182|||http://purl.uniprot.org/annotation/PRO_0000370756
http://togogenome.org/gene/9606:AGGF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N302                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Angiogenic factor with G patch and FHA domains 1|||Basic and acidic residues|||Disordered|||FHA|||G-patch|||In KTS; in 5 patients; displays a stronger angiogenic activity.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064495|||http://purl.uniprot.org/annotation/VAR_017901|||http://purl.uniprot.org/annotation/VAR_017902|||http://purl.uniprot.org/annotation/VAR_037446|||http://purl.uniprot.org/annotation/VAR_037447|||http://purl.uniprot.org/annotation/VSP_009631|||http://purl.uniprot.org/annotation/VSP_009632|||http://purl.uniprot.org/annotation/VSP_009633|||http://purl.uniprot.org/annotation/VSP_009634
http://togogenome.org/gene/9606:CT47A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:VAMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WCA0|||http://purl.uniprot.org/uniprot/P63027                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)|||(Microbial infection) Cleavage; by C.tetani toxin (tetX)|||65% reduction in cleavage by BoNT/F.|||70% reduction in cleavage by C.botulinum neurotoxin type F (BoNT/F, botF).|||90% reduction in cleavage by BoNT/F.|||98% reduction in cleavage by BoNT/F.|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In NEDHAHM.|||In NEDHAHM; impaired vesicle fusion.|||In NEDHAHM; no effect on vesicle fusion.|||N-acetylserine|||Removed|||Required for interaction with SEPT8|||Significant loss of phosphorylation; when associated with A-28, A-61 and A-75.|||Significant loss of phosphorylation; when associated with A-28, A-61 and A-80.|||Significant loss of phosphorylation; when associated with A-28, A-75 and A-80.|||Significant loss of phosphorylation; when associated with A-61, A-75 and A-80.|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 2|||Vesicular|||Wild-type cleavage by BoNT/F.|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206723|||http://purl.uniprot.org/annotation/VAR_083584|||http://purl.uniprot.org/annotation/VAR_083585|||http://purl.uniprot.org/annotation/VAR_083586|||http://purl.uniprot.org/annotation/VAR_083587|||http://purl.uniprot.org/annotation/VAR_083588
http://togogenome.org/gene/9606:ATL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXC4|||http://purl.uniprot.org/uniprot/F5H6I7|||http://purl.uniprot.org/uniprot/Q6DD88                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alters endoplasmic reticulum morphogenesis.|||Atlastin-3|||Cytoplasmic|||GB1/RHD3-type G|||Helical|||In HSN1F; causes mislocalization of the protein; the mutant protein accumulates in condensed structures near the nucleus and localizes to unbranched tubules; has a dominant-negative disruptive effect on the regular structure of the endoplasmic reticulum.|||Lumenal|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287109|||http://purl.uniprot.org/annotation/VAR_070973
http://togogenome.org/gene/9606:SLFN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYM2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased ribonuclease activity; when associated with E-368.|||Decreased ribonuclease activity; when associated with E-573.|||Decreased ribosomal RNA ribonuclease activity.|||Increased ribonuclease activity; when associated with A-368.|||Increased ribonuclease activity; when associated with A-573.|||Loss of function in the E2-induced apoptotic signaling pathway.|||Loss of interaction with SERPINB2.|||Mediates interaction with PDE3A|||Phosphoserine|||Ribonuclease SLFN12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282984|||http://purl.uniprot.org/annotation/VAR_031447|||http://purl.uniprot.org/annotation/VAR_031448|||http://purl.uniprot.org/annotation/VAR_053877
http://togogenome.org/gene/9606:KIF24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7B8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Impairs ability to suppress cilia formation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with MPHOSPH9|||Kinesin motor|||Kinesin-like protein KIF24|||Phosphoserine|||Phosphoserine; by NEK2|||Phosphothreonine; by NEK2|||Polar residues|||Reduces phosphorylation by NEK2 and abolishes ability to suppress cilia formation.|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278248|||http://purl.uniprot.org/annotation/VAR_030720|||http://purl.uniprot.org/annotation/VAR_030721|||http://purl.uniprot.org/annotation/VAR_049706|||http://purl.uniprot.org/annotation/VAR_049707|||http://purl.uniprot.org/annotation/VAR_061284|||http://purl.uniprot.org/annotation/VAR_061285|||http://purl.uniprot.org/annotation/VSP_023210|||http://purl.uniprot.org/annotation/VSP_023211|||http://purl.uniprot.org/annotation/VSP_023212|||http://purl.uniprot.org/annotation/VSP_023213
http://togogenome.org/gene/9606:MATN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH7|||http://purl.uniprot.org/uniprot/O00339|||http://purl.uniprot.org/uniprot/Q8N2G3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like|||EGF-like 1|||EGF-like 10|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Matrilin-2|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007655|||http://purl.uniprot.org/annotation/PRO_5004312864|||http://purl.uniprot.org/annotation/PRO_5007491759|||http://purl.uniprot.org/annotation/VAR_021568|||http://purl.uniprot.org/annotation/VAR_055753|||http://purl.uniprot.org/annotation/VAR_055754|||http://purl.uniprot.org/annotation/VAR_055755|||http://purl.uniprot.org/annotation/VAR_055756|||http://purl.uniprot.org/annotation/VAR_055757|||http://purl.uniprot.org/annotation/VSP_001399|||http://purl.uniprot.org/annotation/VSP_013284|||http://purl.uniprot.org/annotation/VSP_014540
http://togogenome.org/gene/9606:GOT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00505                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine; alternate|||Aspartate aminotransferase, mitochondrial|||Asymmetric dimethylarginine|||In DEE82; decreased glutamate oxaloacetate transferase activity.|||In DEE82; unknown pathological significance.|||In DEE82; unknown pathological significance; decreased glutamate oxaloacetate transferase activity.|||In isoform 2.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001215|||http://purl.uniprot.org/annotation/VAR_031710|||http://purl.uniprot.org/annotation/VAR_031711|||http://purl.uniprot.org/annotation/VAR_031712|||http://purl.uniprot.org/annotation/VAR_055494|||http://purl.uniprot.org/annotation/VAR_083488|||http://purl.uniprot.org/annotation/VAR_083489|||http://purl.uniprot.org/annotation/VAR_083490|||http://purl.uniprot.org/annotation/VAR_083491|||http://purl.uniprot.org/annotation/VSP_054848
http://togogenome.org/gene/9606:KPNA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52292                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Complete loss of binding to KPNB1.|||Disordered|||IBB|||Importin subunit alpha-1|||N-acetylserine|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120722|||http://purl.uniprot.org/annotation/VAR_013137|||http://purl.uniprot.org/annotation/VAR_067625|||http://purl.uniprot.org/annotation/VAR_067626|||http://purl.uniprot.org/annotation/VAR_067627
http://togogenome.org/gene/9606:SMAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1X9|||http://purl.uniprot.org/uniprot/Q8IYB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with clathrin heavy chains|||Stromal membrane-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235838|||http://purl.uniprot.org/annotation/VAR_048326|||http://purl.uniprot.org/annotation/VSP_018502|||http://purl.uniprot.org/annotation/VSP_018503
http://togogenome.org/gene/9606:POTEB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYL3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066917|||http://purl.uniprot.org/annotation/VAR_080177|||http://purl.uniprot.org/annotation/VAR_080178|||http://purl.uniprot.org/annotation/VAR_080179|||http://purl.uniprot.org/annotation/VAR_080180
http://togogenome.org/gene/9606:EXTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPY9|||http://purl.uniprot.org/uniprot/O43909                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Exostosin GT47|||Exostosin-like 3|||Found in a small consanguineous family with intellectual disability; unknown pathological significance.|||Glycosyl transferase 64|||Helical|||Helical; Signal-anchor for type II membrane protein|||In ISDNA; changed glycosaminoglycan synthesis.|||In ISDNA; changed glycosaminoglycan synthesis; no localization to Golgi apparatus in patient fibroblasts.|||Interchain (with C-793)|||Interchain (with C-915)|||Lumenal|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Phosphoserine|||Required for interaction with REG3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149657|||http://purl.uniprot.org/annotation/VAR_049229|||http://purl.uniprot.org/annotation/VAR_061194|||http://purl.uniprot.org/annotation/VAR_079089|||http://purl.uniprot.org/annotation/VAR_079090|||http://purl.uniprot.org/annotation/VAR_079091|||http://purl.uniprot.org/annotation/VAR_079092|||http://purl.uniprot.org/annotation/VAR_079093|||http://purl.uniprot.org/annotation/VAR_079094|||http://purl.uniprot.org/annotation/VAR_080762
http://togogenome.org/gene/9606:TAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20366|||http://purl.uniprot.org/uniprot/Q9Y494                                                                                  ^@                                                                                  Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  C-terminal-flanking peptide|||Cleavage; by ACE|||Cleavage; by ACE and MME|||Cleavage; by FAP|||Cleavage; by MME|||In isoform Alpha and isoform Delta.|||In isoform Gamma and isoform Delta.|||Methionine amide|||Neurokinin A|||Neuropeptide K|||Neuropeptide gamma, 1st part|||Neuropeptide gamma, 2nd part|||Substance P|||Tachykinin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033529|||http://purl.uniprot.org/annotation/PRO_0000033530|||http://purl.uniprot.org/annotation/PRO_0000033531|||http://purl.uniprot.org/annotation/PRO_0000033532|||http://purl.uniprot.org/annotation/PRO_0000033533|||http://purl.uniprot.org/annotation/PRO_0000033534|||http://purl.uniprot.org/annotation/PRO_0000033535|||http://purl.uniprot.org/annotation/VSP_006375|||http://purl.uniprot.org/annotation/VSP_006376|||http://purl.uniprot.org/annotation/VSP_006377
http://togogenome.org/gene/9606:RAPGEF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95398|||http://purl.uniprot.org/uniprot/Q99777                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activation of RAP1A.|||Abolishes interaction with PDE3B.|||Basic and acidic residues|||DEP|||Diminishes GEF activity dependence on cAMP concentration.|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PDE3B|||N-terminal Ras-GEF|||Phosphoserine|||Rap guanine nucleotide exchange factor 3|||Ras-GEF|||Reduces activation of RAP1A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068867|||http://purl.uniprot.org/annotation/VAR_047924|||http://purl.uniprot.org/annotation/VAR_047925|||http://purl.uniprot.org/annotation/VAR_047926|||http://purl.uniprot.org/annotation/VAR_061784|||http://purl.uniprot.org/annotation/VSP_007608|||http://purl.uniprot.org/annotation/VSP_007609|||http://purl.uniprot.org/annotation/VSP_047007
http://togogenome.org/gene/9606:DTX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2E6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase DTX4|||In isoform 2.|||Polar residues|||RING-type; atypical|||WWE 1|||WWE 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280555|||http://purl.uniprot.org/annotation/VSP_023784
http://togogenome.org/gene/9606:ZNF146                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15072                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Induces a decrease in sumoylation. Induces a strong decrease but does not abolish sumoylation; when associated with R-157.|||Induces a decrease in sumoylation. Induces a strong decrease but does not abolish sumoylation; when associated with R-169.|||Interaction with TERF2IP|||Zinc finger protein OZF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047276|||http://purl.uniprot.org/annotation/VAR_023746
http://togogenome.org/gene/9606:MYOM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTT5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||In isoform 3.|||Myomesin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315394|||http://purl.uniprot.org/annotation/VAR_038179|||http://purl.uniprot.org/annotation/VAR_038180|||http://purl.uniprot.org/annotation/VAR_038181|||http://purl.uniprot.org/annotation/VAR_038182|||http://purl.uniprot.org/annotation/VAR_038183|||http://purl.uniprot.org/annotation/VAR_038184|||http://purl.uniprot.org/annotation/VAR_038185|||http://purl.uniprot.org/annotation/VAR_038186|||http://purl.uniprot.org/annotation/VAR_038187|||http://purl.uniprot.org/annotation/VAR_038188|||http://purl.uniprot.org/annotation/VAR_038189|||http://purl.uniprot.org/annotation/VAR_049910|||http://purl.uniprot.org/annotation/VSP_030542|||http://purl.uniprot.org/annotation/VSP_030543|||http://purl.uniprot.org/annotation/VSP_030544|||http://purl.uniprot.org/annotation/VSP_030545
http://togogenome.org/gene/9606:GDF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27539                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Embryonic growth/differentiation factor 1|||Found in a patient with atrioventricular canal-cleft mitral valve; unknown pathological significance.|||In CHTD6 and RAI.|||In CHTD6.|||In CTHM; double-outlet right ventricle.|||In RAI.|||In TOF.|||In a patient with Rastelli type atrioventricular canal.|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033898|||http://purl.uniprot.org/annotation/PRO_0000033899|||http://purl.uniprot.org/annotation/VAR_028274|||http://purl.uniprot.org/annotation/VAR_065332|||http://purl.uniprot.org/annotation/VAR_065333|||http://purl.uniprot.org/annotation/VAR_065334|||http://purl.uniprot.org/annotation/VAR_065335|||http://purl.uniprot.org/annotation/VAR_065336|||http://purl.uniprot.org/annotation/VAR_065337|||http://purl.uniprot.org/annotation/VAR_065338|||http://purl.uniprot.org/annotation/VAR_080779|||http://purl.uniprot.org/annotation/VAR_080780|||http://purl.uniprot.org/annotation/VAR_080781
http://togogenome.org/gene/9606:NPY1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25929                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 1|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069920|||http://purl.uniprot.org/annotation/VAR_014681
http://togogenome.org/gene/9606:LRRTM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43300                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Repeat|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Involved in DLG4-binding|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane neuronal protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018353
http://togogenome.org/gene/9606:OR6C75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW92|||http://purl.uniprot.org/uniprot/A6NL08                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C75                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309494|||http://purl.uniprot.org/annotation/VAR_036972|||http://purl.uniprot.org/annotation/VAR_036973
http://togogenome.org/gene/9606:LIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPH8|||http://purl.uniprot.org/uniprot/A0A8V8TQC4|||http://purl.uniprot.org/uniprot/B4DM52|||http://purl.uniprot.org/uniprot/F5GZ28|||http://purl.uniprot.org/uniprot/P18858                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA ligase family profile|||Basic and acidic residues|||DNA ligase 1|||Disordered|||In IMD96; loss of DNA ligase activity.|||In IMD96; results in decreased repair response to DNA damage as shown by rescue assays in LIG1-deficient cells; severely reduced DNA ligase activity; 2-fold decrease of affinity for DNA; 5-fold increase of affiniy for Mg2+.|||In IMD96; results in decreased repair response to DNA damage as shown by rescue assays in LIG1-deficient cells; severely reduced DNA ligase activity; 3-fold decrease of affinity for DNA; 4-fold increase of affiniy for Mg2+.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with target DNA|||Loss of DNA ligase activity.|||N6-AMP-lysine intermediate|||N6-acetyllysine|||No effect on DNA ligase activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Severely reduced DNA ligase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059570|||http://purl.uniprot.org/annotation/VAR_002262|||http://purl.uniprot.org/annotation/VAR_002263|||http://purl.uniprot.org/annotation/VAR_016766|||http://purl.uniprot.org/annotation/VAR_016767|||http://purl.uniprot.org/annotation/VAR_016768|||http://purl.uniprot.org/annotation/VAR_016769|||http://purl.uniprot.org/annotation/VAR_016770|||http://purl.uniprot.org/annotation/VAR_018802|||http://purl.uniprot.org/annotation/VAR_018803|||http://purl.uniprot.org/annotation/VAR_018804|||http://purl.uniprot.org/annotation/VAR_018805|||http://purl.uniprot.org/annotation/VAR_018806|||http://purl.uniprot.org/annotation/VAR_020194|||http://purl.uniprot.org/annotation/VAR_020195|||http://purl.uniprot.org/annotation/VAR_036511|||http://purl.uniprot.org/annotation/VAR_036512|||http://purl.uniprot.org/annotation/VAR_087009|||http://purl.uniprot.org/annotation/VAR_087010|||http://purl.uniprot.org/annotation/VAR_087011|||http://purl.uniprot.org/annotation/VSP_056139|||http://purl.uniprot.org/annotation/VSP_056140|||http://purl.uniprot.org/annotation/VSP_057320|||http://purl.uniprot.org/annotation/VSP_057321
http://togogenome.org/gene/9606:SPATA33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KRC8|||http://purl.uniprot.org/uniprot/Q96N06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with ATG16L1|||Interaction with VDAC2|||PQIIIT|||Phosphoserine|||Polar residues|||Spermatogenesis-associated protein 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282409|||http://purl.uniprot.org/annotation/VAR_050897|||http://purl.uniprot.org/annotation/VSP_053288
http://togogenome.org/gene/9606:COL8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27658                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen alpha-1(VIII) chain|||Disordered|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Pro residues|||Triple-helical region (COL1)|||Vastatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005762|||http://purl.uniprot.org/annotation/PRO_0000390484
http://togogenome.org/gene/9606:TRPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48995                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Short.|||Polar residues|||Short transient receptor potential channel 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215303|||http://purl.uniprot.org/annotation/VSP_006560
http://togogenome.org/gene/9606:AMTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0L8|||http://purl.uniprot.org/uniprot/Q6UX39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Amelotin|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022613|||http://purl.uniprot.org/annotation/PRO_5003272569|||http://purl.uniprot.org/annotation/VAR_035791|||http://purl.uniprot.org/annotation/VAR_050661|||http://purl.uniprot.org/annotation/VAR_050662|||http://purl.uniprot.org/annotation/VSP_023919
http://togogenome.org/gene/9606:SGK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EW6|||http://purl.uniprot.org/uniprot/Q5H9Q5|||http://purl.uniprot.org/uniprot/Q96BR1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes activity.|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased activation.|||Nuclear localization signal|||PX|||Partially localized to the membrane.|||Phosphoserine|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086649|||http://purl.uniprot.org/annotation/VAR_035636|||http://purl.uniprot.org/annotation/VAR_041076|||http://purl.uniprot.org/annotation/VSP_041903
http://togogenome.org/gene/9606:PACRGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K679|||http://purl.uniprot.org/uniprot/D6RGK2|||http://purl.uniprot.org/uniprot/Q8N7B6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||PACRG-like protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278243|||http://purl.uniprot.org/annotation/VSP_023206|||http://purl.uniprot.org/annotation/VSP_043351|||http://purl.uniprot.org/annotation/VSP_045095|||http://purl.uniprot.org/annotation/VSP_045096
http://togogenome.org/gene/9606:PRADC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSG0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Signal Peptide|||Site                                                                                  ^@                                                                                  Abolishes N-glycosylation. Abolishes N-glycosylation; when associated with Q-121.|||Does not affect glycosylation state. Abolishes N-glycosylation; when associated with Q-171.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||PA|||Protease-associated domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022001
http://togogenome.org/gene/9606:PLEKHJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EIZ3|||http://purl.uniprot.org/uniprot/Q9NW61                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||PH|||Pleckstrin homology domain-containing family J member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309230
http://togogenome.org/gene/9606:TENT5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEK8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decrease about 50% the poly(A) elongation activity; when associated with E-312 and E-313.|||Does not affect poly (A) elongation activity; when associated with E-312. Decrease about 50% the poly(A) elongation activity; when associated with P-136 and E-312.|||Does not affect poly (A) elongation activity; when associated with E-313. Decrease about 50% the poly(A) elongation activity; when associated with P-136 and E-313.|||Loss of poly(A) elongation activity.|||Terminal nucleotidyltransferase 5D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259939|||http://purl.uniprot.org/annotation/VAR_028980
http://togogenome.org/gene/9606:DHX30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BXY3|||http://purl.uniprot.org/uniprot/Q7L2E3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX30|||DEAH box|||DRBM|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In NEDMIAL; changed localization to stress granules; decreased RNA-binding; no effect on RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis.|||In NEDMIAL; changed localization to stress granules; decreased RNA-dependent ATPase activity; by inducing the formation of stress granules probably indirectly decreases global protein synthesis.|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245538|||http://purl.uniprot.org/annotation/VAR_080611|||http://purl.uniprot.org/annotation/VAR_080612|||http://purl.uniprot.org/annotation/VAR_080613|||http://purl.uniprot.org/annotation/VAR_080614|||http://purl.uniprot.org/annotation/VAR_080615|||http://purl.uniprot.org/annotation/VAR_080616|||http://purl.uniprot.org/annotation/VSP_022118|||http://purl.uniprot.org/annotation/VSP_036891|||http://purl.uniprot.org/annotation/VSP_036892
http://togogenome.org/gene/9606:XPO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0E2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Exportin-4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204711|||http://purl.uniprot.org/annotation/VAR_048958|||http://purl.uniprot.org/annotation/VAR_048959
http://togogenome.org/gene/9606:BEND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5X7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  BEN 1|||BEN 2|||BEN 3|||BEN 4|||BEN domain-containing protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Loss of nuclear localization.|||Nuclear localization signal|||Partial loss of sumoylation. Almost complete loss of sumoylation, partial loss of transcription repression, no effect on subcellular location, loss of rDNA silencing; when associated with R-20.|||Partial loss of sumoylation. Almost complete loss of sumoylation, partial loss of transcription repression, no effect on subcellular location, loss of rDNA silencing; when associated with R-512.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290200
http://togogenome.org/gene/9606:PSAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y617                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NLS2.|||In PSATD; reduced Vmax.|||In isoform 2.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine aminotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150135|||http://purl.uniprot.org/annotation/VAR_037252|||http://purl.uniprot.org/annotation/VAR_048235|||http://purl.uniprot.org/annotation/VAR_072571|||http://purl.uniprot.org/annotation/VAR_072572|||http://purl.uniprot.org/annotation/VSP_000237
http://togogenome.org/gene/9606:OR4F16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV92|||http://purl.uniprot.org/uniprot/Q6IEY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F3/4F16/4F29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150551
http://togogenome.org/gene/9606:MINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4C8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 1, isoform 2 and isoform 5.|||In isoform 2.|||In isoform 4 and isoform 5.|||Mediates interaction with RAP2A|||Misshapen-like kinase 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086329|||http://purl.uniprot.org/annotation/VAR_040799|||http://purl.uniprot.org/annotation/VAR_040800|||http://purl.uniprot.org/annotation/VAR_046058|||http://purl.uniprot.org/annotation/VAR_046059|||http://purl.uniprot.org/annotation/VAR_046060|||http://purl.uniprot.org/annotation/VAR_046061|||http://purl.uniprot.org/annotation/VSP_007059|||http://purl.uniprot.org/annotation/VSP_007060|||http://purl.uniprot.org/annotation/VSP_041871
http://togogenome.org/gene/9606:GUCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVD9|||http://purl.uniprot.org/uniprot/Q7Z629|||http://purl.uniprot.org/uniprot/Q96NT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Protein GUCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079574|||http://purl.uniprot.org/annotation/VSP_044730|||http://purl.uniprot.org/annotation/VSP_055753
http://togogenome.org/gene/9606:GPR15LG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWK7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Protein GPR15LG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260084
http://togogenome.org/gene/9606:RIPOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS17                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho family-interacting cell polarization regulator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289110|||http://purl.uniprot.org/annotation/VSP_025903|||http://purl.uniprot.org/annotation/VSP_043315|||http://purl.uniprot.org/annotation/VSP_045002
http://togogenome.org/gene/9606:CRYGC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0X8GLL6|||http://purl.uniprot.org/uniprot/P07315                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Gamma-crystallin C|||In CTRCT2.|||In CTRCT2; congenital lamellar cataract; unknown pathological significance.|||In CTRCT2; reduces protein-protein interactions in vivo.|||In CTRCT2; unknown pathological significance.|||Removed|||S-methylcysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057587|||http://purl.uniprot.org/annotation/VAR_021142|||http://purl.uniprot.org/annotation/VAR_021143|||http://purl.uniprot.org/annotation/VAR_021144|||http://purl.uniprot.org/annotation/VAR_038432|||http://purl.uniprot.org/annotation/VAR_067212|||http://purl.uniprot.org/annotation/VAR_084798|||http://purl.uniprot.org/annotation/VAR_084799
http://togogenome.org/gene/9606:STAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LE48|||http://purl.uniprot.org/uniprot/Q8WVM7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cohesin subunit SA-1|||Disordered|||Found in a patient with cohesinopathy.|||Found in a patient with cohesinopathy; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRD47.|||In isoform 2.|||Phosphoserine|||Polar residues|||SCD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120182|||http://purl.uniprot.org/annotation/VAR_046968|||http://purl.uniprot.org/annotation/VAR_079487|||http://purl.uniprot.org/annotation/VAR_079488|||http://purl.uniprot.org/annotation/VAR_079489|||http://purl.uniprot.org/annotation/VAR_079490|||http://purl.uniprot.org/annotation/VAR_079491|||http://purl.uniprot.org/annotation/VAR_079492|||http://purl.uniprot.org/annotation/VAR_079493|||http://purl.uniprot.org/annotation/VAR_079494|||http://purl.uniprot.org/annotation/VAR_082291|||http://purl.uniprot.org/annotation/VAR_082292|||http://purl.uniprot.org/annotation/VSP_054496
http://togogenome.org/gene/9606:BIRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13490                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BIR 1|||BIR 2|||BIR 3|||Baculoviral IAP repeat-containing protein 2|||CARD|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122347|||http://purl.uniprot.org/annotation/VAR_025016|||http://purl.uniprot.org/annotation/VAR_025017|||http://purl.uniprot.org/annotation/VAR_025018|||http://purl.uniprot.org/annotation/VAR_049535|||http://purl.uniprot.org/annotation/VSP_045314
http://togogenome.org/gene/9606:TRIM15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SRL0|||http://purl.uniprot.org/uniprot/Q9C019                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM15|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056218|||http://purl.uniprot.org/annotation/VAR_014228|||http://purl.uniprot.org/annotation/VAR_052129|||http://purl.uniprot.org/annotation/VAR_052130|||http://purl.uniprot.org/annotation/VAR_052131|||http://purl.uniprot.org/annotation/VAR_052132|||http://purl.uniprot.org/annotation/VSP_005760|||http://purl.uniprot.org/annotation/VSP_005761
http://togogenome.org/gene/9606:EDEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92611                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||ER degradation-enhancing alpha-mannosidase-like protein 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Normal affinity for misfolded glycoproteins, but impaired SEL1L binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210321|||http://purl.uniprot.org/annotation/VSP_056703|||http://purl.uniprot.org/annotation/VSP_056704
http://togogenome.org/gene/9606:TRPM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIX5|||http://purl.uniprot.org/uniprot/Q8TD43                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ability to restore sensitivity to Ca(2+) after desensitization.|||Alters the monovalent cation permeability sequence and results in a pore with moderate Ca(2+) permeability.|||Calmodulin-binding|||Cytoplasmic|||Decreases the sensitivity to Ca(2+).|||Does not affect PIP2-binding.|||Extracellular|||Helical|||In EKVP6; increased calcium activated cation channel activity; increased keratinocytes proliferation and differentiation; no effect on localization at cell membrane.|||In PFHB1B.|||In PFHB1B; atrioventricular block.|||In PFHB1B; attenuated desumoylation of TRPM4 resulting in constitutive sumoylation of the channel leading to impaired endocytosis and elevated channel density at the cell surface.|||In PFHB1B; incomplete right bundle-branch block.|||In PFHB1B; right bundle-branch block.|||In isoform 2.|||In isoform 3.|||Induces a functional channel that combines the gating hallmarks of TRPM4 (activation by Ca(2+)) with TRPV6-like sensitivity to block by extracellular Ca(2+) and Mg(2+) as well as Ca(2+) permeation.|||Ion transport|||Mediates modulation by decavanadate and PIP2-binding|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine; by PKC|||Pore-forming|||Results in a channel with normal permeability properties but with a reduced sensitivity to block by intracellular spermine.|||Results in a channel with very rapid desensitization and highly reduced sensitivity to PIP2.|||Results in a functional channel that exhibits extremely fast desensitization, possibly indicating destabilization of the pore.|||Results in a non-functional channel with a dominant negative phenotype.|||Selectivity filter|||Transient receptor potential cation channel subfamily M member 4|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259529|||http://purl.uniprot.org/annotation/VAR_064042|||http://purl.uniprot.org/annotation/VAR_066761|||http://purl.uniprot.org/annotation/VAR_066762|||http://purl.uniprot.org/annotation/VAR_066763|||http://purl.uniprot.org/annotation/VAR_066764|||http://purl.uniprot.org/annotation/VAR_066765|||http://purl.uniprot.org/annotation/VAR_066766|||http://purl.uniprot.org/annotation/VAR_066767|||http://purl.uniprot.org/annotation/VAR_066768|||http://purl.uniprot.org/annotation/VAR_066769|||http://purl.uniprot.org/annotation/VAR_066770|||http://purl.uniprot.org/annotation/VAR_066771|||http://purl.uniprot.org/annotation/VAR_066772|||http://purl.uniprot.org/annotation/VAR_066773|||http://purl.uniprot.org/annotation/VAR_066774|||http://purl.uniprot.org/annotation/VAR_066775|||http://purl.uniprot.org/annotation/VAR_066776|||http://purl.uniprot.org/annotation/VAR_083166|||http://purl.uniprot.org/annotation/VAR_083167|||http://purl.uniprot.org/annotation/VSP_021442|||http://purl.uniprot.org/annotation/VSP_021443
http://togogenome.org/gene/9606:NHSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SYE7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NHS-like protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341353|||http://purl.uniprot.org/annotation/VAR_044055|||http://purl.uniprot.org/annotation/VAR_044056|||http://purl.uniprot.org/annotation/VSP_040818|||http://purl.uniprot.org/annotation/VSP_040819
http://togogenome.org/gene/9606:CD101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93033                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EWI motif|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Immunoglobulin superfamily member 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253539|||http://purl.uniprot.org/annotation/VAR_028371|||http://purl.uniprot.org/annotation/VAR_028372|||http://purl.uniprot.org/annotation/VAR_028373|||http://purl.uniprot.org/annotation/VAR_028374|||http://purl.uniprot.org/annotation/VAR_028375|||http://purl.uniprot.org/annotation/VAR_028376|||http://purl.uniprot.org/annotation/VAR_054434|||http://purl.uniprot.org/annotation/VAR_054435|||http://purl.uniprot.org/annotation/VAR_054436|||http://purl.uniprot.org/annotation/VAR_054437|||http://purl.uniprot.org/annotation/VAR_054438
http://togogenome.org/gene/9606:SH2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNV5|||http://purl.uniprot.org/uniprot/B4DLN5|||http://purl.uniprot.org/uniprot/Q9NRF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes self-association and interaction with INSR and IGF1R.|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with JAK2 (low-affinity binding; independent of JAK2 phosphorylation)|||Interaction with RAC1|||Omega-N-methylarginine|||PH|||Phosphoserine|||Phosphotyrosine; by JAK1, JAK2|||Phosphotyrosine; by JAK1, JAK2 and PDGFR|||Polar residues|||Pro residues|||Required for NGF signaling|||Required for nuclear localization|||Required for self-association|||SH2|||SH2B adapter protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323593|||http://purl.uniprot.org/annotation/VAR_039550|||http://purl.uniprot.org/annotation/VAR_039551|||http://purl.uniprot.org/annotation/VSP_032027|||http://purl.uniprot.org/annotation/VSP_032028
http://togogenome.org/gene/9606:FBXL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKA2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||F-box|||F-box/LRR-repeat protein 4|||In MTDPS13.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119844|||http://purl.uniprot.org/annotation/VAR_070858|||http://purl.uniprot.org/annotation/VAR_070859|||http://purl.uniprot.org/annotation/VAR_070860|||http://purl.uniprot.org/annotation/VAR_070861|||http://purl.uniprot.org/annotation/VAR_070862|||http://purl.uniprot.org/annotation/VAR_070863|||http://purl.uniprot.org/annotation/VAR_076547
http://togogenome.org/gene/9606:CCND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclin N-terminal|||Disordered|||G1/S-specific cyclin-D2|||In MPPH3.|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080437|||http://purl.uniprot.org/annotation/VAR_018820|||http://purl.uniprot.org/annotation/VAR_072370|||http://purl.uniprot.org/annotation/VAR_072371|||http://purl.uniprot.org/annotation/VAR_072372|||http://purl.uniprot.org/annotation/VAR_072373|||http://purl.uniprot.org/annotation/VAR_072374|||http://purl.uniprot.org/annotation/VSP_057295|||http://purl.uniprot.org/annotation/VSP_057296
http://togogenome.org/gene/9606:TELO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4R8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2 in response to growth factor deprivation and subsequent ubiquitination and degradation.|||Disordered|||Hydroxyproline|||In YHFS.|||Interaction with PIH1D1|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by CK2|||Telomere length regulation protein TEL2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318515|||http://purl.uniprot.org/annotation/VAR_038752|||http://purl.uniprot.org/annotation/VAR_038753|||http://purl.uniprot.org/annotation/VAR_038754|||http://purl.uniprot.org/annotation/VAR_061839|||http://purl.uniprot.org/annotation/VAR_061840|||http://purl.uniprot.org/annotation/VAR_077025|||http://purl.uniprot.org/annotation/VAR_077026|||http://purl.uniprot.org/annotation/VAR_077027|||http://purl.uniprot.org/annotation/VAR_077028|||http://purl.uniprot.org/annotation/VAR_077029
http://togogenome.org/gene/9606:VCY1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14598                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Testis-specific basic protein Y 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184663
http://togogenome.org/gene/9606:AFF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJU9|||http://purl.uniprot.org/uniprot/P51825|||http://purl.uniprot.org/uniprot/Q14C88                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  AF4/FMR2 C-terminal homology|||AF4/FMR2 family member 1|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215910|||http://purl.uniprot.org/annotation/VAR_020370|||http://purl.uniprot.org/annotation/VAR_036130|||http://purl.uniprot.org/annotation/VSP_046095|||http://purl.uniprot.org/annotation/VSP_046096
http://togogenome.org/gene/9606:ICOSLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y5W7|||http://purl.uniprot.org/uniprot/A0N0L8|||http://purl.uniprot.org/uniprot/B7Z1W8|||http://purl.uniprot.org/uniprot/O75144                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||ICOS ligand|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014803|||http://purl.uniprot.org/annotation/PRO_5014296527|||http://purl.uniprot.org/annotation/PRO_5036456740|||http://purl.uniprot.org/annotation/VAR_049880|||http://purl.uniprot.org/annotation/VSP_002520|||http://purl.uniprot.org/annotation/VSP_054718
http://togogenome.org/gene/9606:CLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7I0|||http://purl.uniprot.org/uniprot/B7Z8N6|||http://purl.uniprot.org/uniprot/P49760                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK2|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphoserine; by autocatalysis|||Phosphothreonine; by PKB/AKT1|||Phosphothreonine; by PKB/AKT2|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085868|||http://purl.uniprot.org/annotation/VSP_004856|||http://purl.uniprot.org/annotation/VSP_004857|||http://purl.uniprot.org/annotation/VSP_038744
http://togogenome.org/gene/9606:RBM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98179                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; in A2780 ovarian carcinoma cell line|||Disordered|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||RNA-binding protein 3|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081752
http://togogenome.org/gene/9606:ELMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JJ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ELMO|||Engulfment and cell motility protein 2|||In isoform 2.|||PH|||Phosphoserine|||Phosphotyrosine|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153714|||http://purl.uniprot.org/annotation/VAR_048928|||http://purl.uniprot.org/annotation/VSP_055477
http://togogenome.org/gene/9606:PFKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17858|||http://purl.uniprot.org/uniprot/Q7L2M7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent 6-phosphofructokinase, liver type|||C-terminal regulatory PFK domain 2|||Does not affect GlcNAcylation.|||In isoform 2.|||Interdomain linker|||N-acetylalanine|||N-terminal catalytic PFK domain 1|||O-linked (GlcNAc) serine|||Phosphofructokinase|||Phosphoserine|||Phosphotyrosine|||Prevents GlcNAcylation and enhance enzyme activity.|||Proton acceptor|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112021|||http://purl.uniprot.org/annotation/VAR_006070|||http://purl.uniprot.org/annotation/VAR_006071|||http://purl.uniprot.org/annotation/VAR_030872|||http://purl.uniprot.org/annotation/VSP_011854
http://togogenome.org/gene/9606:SERGEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8C1|||http://purl.uniprot.org/uniprot/Q9UGK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||Secretion-regulating guanine nucleotide exchange factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206649|||http://purl.uniprot.org/annotation/VAR_017156|||http://purl.uniprot.org/annotation/VAR_017157|||http://purl.uniprot.org/annotation/VSP_050614|||http://purl.uniprot.org/annotation/VSP_050615
http://togogenome.org/gene/9606:RASSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS23                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform A and isoform E.|||In isoform B.|||In isoform C and isoform H.|||In isoform E.|||In isoform F.|||In isoform G and isoform H.|||In isoform G.|||MOAP1-binding|||Mediates interaction with E4F1|||N-acetylserine|||Omega-N-methylarginine|||Phorbol-ester/DAG-type|||Phosphoserine|||Prevents G1 cell cycle arrest; reduced protein phosphorylation.|||Ras association domain-containing protein 1|||Ras-associating|||Removed|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068891|||http://purl.uniprot.org/annotation/VAR_019542|||http://purl.uniprot.org/annotation/VAR_019543|||http://purl.uniprot.org/annotation/VAR_019544|||http://purl.uniprot.org/annotation/VAR_019545|||http://purl.uniprot.org/annotation/VAR_019546|||http://purl.uniprot.org/annotation/VAR_019547|||http://purl.uniprot.org/annotation/VAR_059794|||http://purl.uniprot.org/annotation/VSP_050770|||http://purl.uniprot.org/annotation/VSP_050771|||http://purl.uniprot.org/annotation/VSP_050772|||http://purl.uniprot.org/annotation/VSP_050773|||http://purl.uniprot.org/annotation/VSP_050774|||http://purl.uniprot.org/annotation/VSP_050775|||http://purl.uniprot.org/annotation/VSP_050776|||http://purl.uniprot.org/annotation/VSP_050777|||http://purl.uniprot.org/annotation/VSP_050778
http://togogenome.org/gene/9606:LRRC75B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VPJ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 75B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254046|||http://purl.uniprot.org/annotation/VAR_051125|||http://purl.uniprot.org/annotation/VSP_021172|||http://purl.uniprot.org/annotation/VSP_021173
http://togogenome.org/gene/9606:MYOZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In CMH16.|||Myozenin-2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111099|||http://purl.uniprot.org/annotation/VAR_065469|||http://purl.uniprot.org/annotation/VAR_065470
http://togogenome.org/gene/9606:ZNF219                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger protein 219                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047461|||http://purl.uniprot.org/annotation/VAR_067624
http://togogenome.org/gene/9606:C1QL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0INP7|||http://purl.uniprot.org/uniprot/Q86Z23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen-like|||Complement C1q-like protein 4|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274338|||http://purl.uniprot.org/annotation/PRO_5035366276
http://togogenome.org/gene/9606:S100Z                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXG8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Protein S100-Z|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144033|||http://purl.uniprot.org/annotation/VAR_060484
http://togogenome.org/gene/9606:STARD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0AZS2|||http://purl.uniprot.org/uniprot/Q96DR4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||START|||StAR-related lipid transfer protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220667|||http://purl.uniprot.org/annotation/VSP_057170
http://togogenome.org/gene/9606:PRPF40B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VU11|||http://purl.uniprot.org/uniprot/Q6NWY9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FF|||FF 1|||FF 2|||FF 3|||FF 4|||FF 5|||FF 6|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pre-mRNA-processing factor 40 homolog B|||Pro residues|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309282|||http://purl.uniprot.org/annotation/VSP_029116|||http://purl.uniprot.org/annotation/VSP_029117|||http://purl.uniprot.org/annotation/VSP_029118|||http://purl.uniprot.org/annotation/VSP_029119|||http://purl.uniprot.org/annotation/VSP_029120|||http://purl.uniprot.org/annotation/VSP_029121
http://togogenome.org/gene/9606:ZFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D65|||http://purl.uniprot.org/uniprot/Q96KR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DZF|||Disordered|||Found in a patient with spastic paraplegia; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Zinc finger RNA-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312719|||http://purl.uniprot.org/annotation/VAR_037554|||http://purl.uniprot.org/annotation/VAR_037555|||http://purl.uniprot.org/annotation/VAR_077851
http://togogenome.org/gene/9606:LNPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z829|||http://purl.uniprot.org/uniprot/Q9C0E8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes myristoylation. Inhibits three-way ER tubular junction formation. Does not inhibit transmembrane domain 1-induced membrane translocation.|||C4-type; plays a role in ER morphology|||Cytoplasmic|||Disordered|||Endoplasmic reticulum junction formation protein lunapark|||Helical|||In NEDEHCC.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis and prevents homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-177; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Inhibits phosphorylation and degradation in mitosis but does not prevent homodimerization and three-way ER tubular junction formations; when associated with A-179; A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231.|||Lumenal|||Lunapark|||N-myristoyl glycine|||No change in N-myristoylation. Inhibits three-way ER tubular junction formation.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248310|||http://purl.uniprot.org/annotation/VAR_081176|||http://purl.uniprot.org/annotation/VSP_020238|||http://purl.uniprot.org/annotation/VSP_020239|||http://purl.uniprot.org/annotation/VSP_054427
http://togogenome.org/gene/9606:FBXO38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AZE0|||http://purl.uniprot.org/uniprot/Q6PIJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 38|||In HMN2D; unable to promote activation of KLF7 target genes including CDKN1A and L1CAM in both cultured cells and patient-derived cells.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with KLF7|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear export signal 3|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119933|||http://purl.uniprot.org/annotation/VAR_028099|||http://purl.uniprot.org/annotation/VAR_049049|||http://purl.uniprot.org/annotation/VAR_070923|||http://purl.uniprot.org/annotation/VSP_011448|||http://purl.uniprot.org/annotation/VSP_011449
http://togogenome.org/gene/9606:CHSY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70JA7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate synthase 3|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189562|||http://purl.uniprot.org/annotation/VAR_021174|||http://purl.uniprot.org/annotation/VAR_027540
http://togogenome.org/gene/9606:CEBPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49716                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||CCAAT/enhancer-binding protein delta|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Leucine-zipper|||Loss of sumoylation.|||N-acetylserine|||Pro residues|||Removed|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076621|||http://purl.uniprot.org/annotation/VAR_037087
http://togogenome.org/gene/9606:TMEM101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFS4|||http://purl.uniprot.org/uniprot/Q96IK0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 101                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240864
http://togogenome.org/gene/9606:DTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6X2|||http://purl.uniprot.org/uniprot/Q8TEA8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||D-aminoacyl-tRNA deacylase 1|||Disordered|||Gly-cisPro motif, important for rejection of L-amino acids|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164626
http://togogenome.org/gene/9606:PANK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1K9|||http://purl.uniprot.org/uniprot/Q9BZ23                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cleavage; by MPP|||Disordered|||In NBIA1.|||In NBIA1; atypical.|||In NBIA1; atypical; loss of enzyme activity; no effect on its mitochondrial localization.|||In NBIA1; atypical; no effect on enzyme activity or its inhibition by acetyl CoA.|||In NBIA1; atypical; no effect on enzyme activity or its mitochondrial localization.|||In NBIA1; atypical; no effect on enzyme activity.|||In NBIA1; atypical; unknown pathological significance.|||In NBIA1; classic and atypical forms; loss of enzyme activity; no effect on its mitochondrial localization; loss of proteolytic cleavage to yield the mature form.|||In NBIA1; classic and atypical forms; unknown pathological significance; no effect on enzyme activity, mitochondrial localization or its inhibition by acetyl CoA.|||In NBIA1; no effect on enzyme activity or its mitochondrial localization.|||In NBIA1; no effect on enzyme activity.|||In NBIA1; significant loss of enzyme activity.|||In NBIA1; significant loss of enzyme activity; no effect on its mitochondrial localization or its inhibition by acetyl CoA.|||In NBIA1; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of export from nucleus.|||Loss of nuclear localization.|||Mitochondrion|||Nuclear export signal|||Nucleolar localization signal|||Pantothenate kinase 2, mitochondrial intermediate form|||Pantothenate kinase 2, mitochondrial mature form|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023201|||http://purl.uniprot.org/annotation/PRO_0000452676|||http://purl.uniprot.org/annotation/VAR_015152|||http://purl.uniprot.org/annotation/VAR_015153|||http://purl.uniprot.org/annotation/VAR_015154|||http://purl.uniprot.org/annotation/VAR_015155|||http://purl.uniprot.org/annotation/VAR_015156|||http://purl.uniprot.org/annotation/VAR_015157|||http://purl.uniprot.org/annotation/VAR_015158|||http://purl.uniprot.org/annotation/VAR_015159|||http://purl.uniprot.org/annotation/VAR_015160|||http://purl.uniprot.org/annotation/VAR_015161|||http://purl.uniprot.org/annotation/VAR_015162|||http://purl.uniprot.org/annotation/VAR_015163|||http://purl.uniprot.org/annotation/VAR_015164|||http://purl.uniprot.org/annotation/VAR_015165|||http://purl.uniprot.org/annotation/VAR_015166|||http://purl.uniprot.org/annotation/VAR_015167|||http://purl.uniprot.org/annotation/VAR_015168|||http://purl.uniprot.org/annotation/VAR_015169|||http://purl.uniprot.org/annotation/VAR_054484|||http://purl.uniprot.org/annotation/VAR_060934|||http://purl.uniprot.org/annotation/VAR_060935|||http://purl.uniprot.org/annotation/VAR_060936|||http://purl.uniprot.org/annotation/VAR_060937|||http://purl.uniprot.org/annotation/VAR_060938|||http://purl.uniprot.org/annotation/VAR_060939|||http://purl.uniprot.org/annotation/VAR_060940|||http://purl.uniprot.org/annotation/VAR_060941|||http://purl.uniprot.org/annotation/VAR_060942|||http://purl.uniprot.org/annotation/VAR_060943|||http://purl.uniprot.org/annotation/VAR_060944|||http://purl.uniprot.org/annotation/VAR_060945|||http://purl.uniprot.org/annotation/VAR_060946|||http://purl.uniprot.org/annotation/VAR_060947|||http://purl.uniprot.org/annotation/VAR_060948|||http://purl.uniprot.org/annotation/VAR_060949|||http://purl.uniprot.org/annotation/VAR_076594|||http://purl.uniprot.org/annotation/VAR_076595|||http://purl.uniprot.org/annotation/VAR_076596|||http://purl.uniprot.org/annotation/VAR_076597|||http://purl.uniprot.org/annotation/VSP_007424|||http://purl.uniprot.org/annotation/VSP_018825|||http://purl.uniprot.org/annotation/VSP_038494|||http://purl.uniprot.org/annotation/VSP_038495
http://togogenome.org/gene/9606:GPR162                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0I9QPQ8|||http://purl.uniprot.org/uniprot/Q16538                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Probable G-protein coupled receptor 162                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069647|||http://purl.uniprot.org/annotation/VAR_049407|||http://purl.uniprot.org/annotation/VSP_016302|||http://purl.uniprot.org/annotation/VSP_016303
http://togogenome.org/gene/9606:LRIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III|||Helical|||Ig-like|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||LRRNT|||Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309344|||http://purl.uniprot.org/annotation/VAR_036935|||http://purl.uniprot.org/annotation/VAR_036936|||http://purl.uniprot.org/annotation/VAR_036937|||http://purl.uniprot.org/annotation/VAR_036938|||http://purl.uniprot.org/annotation/VAR_036939|||http://purl.uniprot.org/annotation/VSP_054539
http://togogenome.org/gene/9606:FBXO33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6M2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  F-box|||F-box only protein 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119925
http://togogenome.org/gene/9606:PRAMEF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXH4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156980
http://togogenome.org/gene/9606:TMEM145                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBT3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 145                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280355|||http://purl.uniprot.org/annotation/VAR_060400
http://togogenome.org/gene/9606:ABCF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5L1|||http://purl.uniprot.org/uniprot/Q9NUQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 3|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248042|||http://purl.uniprot.org/annotation/VAR_027247|||http://purl.uniprot.org/annotation/VAR_027248|||http://purl.uniprot.org/annotation/VSP_020142
http://togogenome.org/gene/9606:NAGPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK23                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  10% of wild-type of activity; when associated with M-51.|||11% of wild-type of activity.|||15% of wild-type of activity, and almost no traffic to Golgi.|||16% of wild-type of activity.|||22% of wild-type of activity.|||43% of wild-type of activity.|||6% of wild-type of activity.|||65% of wild-type of activity.|||67% of wild-type of activity.|||87% of wild-type of activity.|||Complete loss of activity.|||Cytoplasmic|||EGF-like|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with AP4M1 is abolished.|||Lumenal|||Mediates the interaction with AP4M1|||N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase|||N-linked (GlcNAc...) asparagine|||NPF internalization motif|||No traffic to Golgi.|||Rare variant; found in individuals suffering from stuttering; unknown pathological significance.|||Removed in mature form|||Tyrosine-based internalization motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021788|||http://purl.uniprot.org/annotation/PRO_0000424659|||http://purl.uniprot.org/annotation/VAR_020609|||http://purl.uniprot.org/annotation/VAR_073225|||http://purl.uniprot.org/annotation/VAR_073226|||http://purl.uniprot.org/annotation/VSP_012267|||http://purl.uniprot.org/annotation/VSP_012268|||http://purl.uniprot.org/annotation/VSP_012269
http://togogenome.org/gene/9606:ZC3H8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5P1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Zinc finger CCCH domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213903|||http://purl.uniprot.org/annotation/VAR_057489
http://togogenome.org/gene/9606:H1-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZA3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||H15|||Histone H1.8|||In isoform 2.|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343412|||http://purl.uniprot.org/annotation/VAR_061208|||http://purl.uniprot.org/annotation/VSP_034592
http://togogenome.org/gene/9606:CST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09228                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mass|||Motif|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cystatin-SA|||Reactive site|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006652
http://togogenome.org/gene/9606:UBE2V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2F7|||http://purl.uniprot.org/uniprot/Q13404                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 variant 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082600|||http://purl.uniprot.org/annotation/VSP_038032|||http://purl.uniprot.org/annotation/VSP_038033|||http://purl.uniprot.org/annotation/VSP_038034|||http://purl.uniprot.org/annotation/VSP_038035|||http://purl.uniprot.org/annotation/VSP_038036|||http://purl.uniprot.org/annotation/VSP_044818
http://togogenome.org/gene/9606:CSMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z408                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 10|||CUB 11|||CUB 12|||CUB 13|||CUB 14|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||CUB 6|||CUB 7|||CUB 8|||CUB 9|||CUB and sushi domain-containing protein 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 21|||Sushi 22|||Sushi 23|||Sushi 24|||Sushi 25|||Sushi 26|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079405|||http://purl.uniprot.org/annotation/VAR_024330|||http://purl.uniprot.org/annotation/VAR_028081|||http://purl.uniprot.org/annotation/VAR_028082|||http://purl.uniprot.org/annotation/VAR_028083|||http://purl.uniprot.org/annotation/VAR_028084|||http://purl.uniprot.org/annotation/VAR_028085|||http://purl.uniprot.org/annotation/VAR_028086|||http://purl.uniprot.org/annotation/VAR_050917|||http://purl.uniprot.org/annotation/VSP_009038|||http://purl.uniprot.org/annotation/VSP_009039|||http://purl.uniprot.org/annotation/VSP_009040|||http://purl.uniprot.org/annotation/VSP_009041|||http://purl.uniprot.org/annotation/VSP_009042|||http://purl.uniprot.org/annotation/VSP_009043|||http://purl.uniprot.org/annotation/VSP_009044|||http://purl.uniprot.org/annotation/VSP_009045|||http://purl.uniprot.org/annotation/VSP_009046|||http://purl.uniprot.org/annotation/VSP_055687|||http://purl.uniprot.org/annotation/VSP_055688|||http://purl.uniprot.org/annotation/VSP_055689
http://togogenome.org/gene/9606:SLC25A21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQT8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In MTDPS18; loss of 2-oxoglutarate transporter activity.|||In isoform 2.|||Mitochondrial 2-oxodicarboxylate carrier|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090644|||http://purl.uniprot.org/annotation/VAR_050131|||http://purl.uniprot.org/annotation/VAR_083870|||http://purl.uniprot.org/annotation/VSP_046690
http://togogenome.org/gene/9606:ARHGAP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CB8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Rho GTPase-activating protein 19|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280465|||http://purl.uniprot.org/annotation/VAR_031152|||http://purl.uniprot.org/annotation/VSP_023695|||http://purl.uniprot.org/annotation/VSP_023696|||http://purl.uniprot.org/annotation/VSP_023697|||http://purl.uniprot.org/annotation/VSP_023698|||http://purl.uniprot.org/annotation/VSP_023699|||http://purl.uniprot.org/annotation/VSP_023700|||http://purl.uniprot.org/annotation/VSP_023701
http://togogenome.org/gene/9606:CEACAM21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1W4|||http://purl.uniprot.org/uniprot/A0A0G2JSC8|||http://purl.uniprot.org/uniprot/Q3KPI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 21|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297615|||http://purl.uniprot.org/annotation/VAR_034651|||http://purl.uniprot.org/annotation/VAR_034652|||http://purl.uniprot.org/annotation/VSP_027303|||http://purl.uniprot.org/annotation/VSP_027304
http://togogenome.org/gene/9606:TMEM82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 82                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309236|||http://purl.uniprot.org/annotation/VAR_036917
http://togogenome.org/gene/9606:EMC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||ER membrane protein complex subunit 7|||Helical|||Lumenal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240860
http://togogenome.org/gene/9606:DTNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z202|||http://purl.uniprot.org/uniprot/B7Z6A9|||http://purl.uniprot.org/uniprot/E7EVB6|||http://purl.uniprot.org/uniprot/E9PEY4|||http://purl.uniprot.org/uniprot/O60941|||http://purl.uniprot.org/uniprot/Q1I0L3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dystrobrevin beta|||In isoform 2 and isoform 5.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5 and isoform 6.|||In isoform 6 and isoform 7.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Syntrophin-binding region|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086878|||http://purl.uniprot.org/annotation/VAR_069146|||http://purl.uniprot.org/annotation/VAR_069147|||http://purl.uniprot.org/annotation/VSP_004223|||http://purl.uniprot.org/annotation/VSP_004224|||http://purl.uniprot.org/annotation/VSP_004225|||http://purl.uniprot.org/annotation/VSP_004226|||http://purl.uniprot.org/annotation/VSP_043445|||http://purl.uniprot.org/annotation/VSP_045534|||http://purl.uniprot.org/annotation/VSP_045535
http://togogenome.org/gene/9606:SERPINB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05120                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Not cleaved|||Plasminogen activator inhibitor 2|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223296|||http://purl.uniprot.org/annotation/VAR_011743|||http://purl.uniprot.org/annotation/VAR_011744|||http://purl.uniprot.org/annotation/VAR_011745|||http://purl.uniprot.org/annotation/VAR_014173|||http://purl.uniprot.org/annotation/VAR_051946
http://togogenome.org/gene/9606:INTS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV88                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Integrator complex subunit 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259557|||http://purl.uniprot.org/annotation/VSP_043011|||http://purl.uniprot.org/annotation/VSP_044306
http://togogenome.org/gene/9606:IMMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16891                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MICOS complex subunit MIC60|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084184|||http://purl.uniprot.org/annotation/VAR_021530|||http://purl.uniprot.org/annotation/VAR_051068|||http://purl.uniprot.org/annotation/VSP_013220|||http://purl.uniprot.org/annotation/VSP_013221|||http://purl.uniprot.org/annotation/VSP_047362
http://togogenome.org/gene/9606:SYNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZP0|||http://purl.uniprot.org/uniprot/Q8WXH0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cytoplasmic|||Disordered|||Disrupts interaction with SUN2.|||Helical; Anchor for type IV membrane protein|||In EDMD5.|||In a breast cancer sample; somatic mutation.|||In isoform 10.|||In isoform 11.|||In isoform 13.|||In isoform 2, isoform 5 and isoform 12.|||In isoform 2, isoform 6 and isoform 10.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 12.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interchain (with C-563 in SUN2)|||KASH|||N6-acetyllysine|||Nesprin-2|||Perinuclear space|||Phosphoserine|||Polar residues|||Pro residues|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 23|||Spectrin 24|||Spectrin 25|||Spectrin 26|||Spectrin 27|||Spectrin 28|||Spectrin 29|||Spectrin 3|||Spectrin 30|||Spectrin 31|||Spectrin 32|||Spectrin 33|||Spectrin 34|||Spectrin 35|||Spectrin 36|||Spectrin 37|||Spectrin 38|||Spectrin 39|||Spectrin 4|||Spectrin 40|||Spectrin 41|||Spectrin 42|||Spectrin 43|||Spectrin 44|||Spectrin 45|||Spectrin 46|||Spectrin 47|||Spectrin 48|||Spectrin 49|||Spectrin 5|||Spectrin 50|||Spectrin 51|||Spectrin 52|||Spectrin 53|||Spectrin 54|||Spectrin 55|||Spectrin 56|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Sufficient for interaction with SUN2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163592|||http://purl.uniprot.org/annotation/VAR_027947|||http://purl.uniprot.org/annotation/VAR_027948|||http://purl.uniprot.org/annotation/VAR_027949|||http://purl.uniprot.org/annotation/VAR_027950|||http://purl.uniprot.org/annotation/VAR_027951|||http://purl.uniprot.org/annotation/VAR_036255|||http://purl.uniprot.org/annotation/VAR_036256|||http://purl.uniprot.org/annotation/VAR_050238|||http://purl.uniprot.org/annotation/VAR_050239|||http://purl.uniprot.org/annotation/VAR_050240|||http://purl.uniprot.org/annotation/VAR_050241|||http://purl.uniprot.org/annotation/VAR_050242|||http://purl.uniprot.org/annotation/VAR_050243|||http://purl.uniprot.org/annotation/VAR_050244|||http://purl.uniprot.org/annotation/VAR_050245|||http://purl.uniprot.org/annotation/VAR_050246|||http://purl.uniprot.org/annotation/VAR_050247|||http://purl.uniprot.org/annotation/VAR_050248|||http://purl.uniprot.org/annotation/VAR_050249|||http://purl.uniprot.org/annotation/VAR_050250|||http://purl.uniprot.org/annotation/VAR_050251|||http://purl.uniprot.org/annotation/VAR_050252|||http://purl.uniprot.org/annotation/VAR_050253|||http://purl.uniprot.org/annotation/VAR_050254|||http://purl.uniprot.org/annotation/VAR_050255|||http://purl.uniprot.org/annotation/VAR_050256|||http://purl.uniprot.org/annotation/VAR_050257|||http://purl.uniprot.org/annotation/VAR_050258|||http://purl.uniprot.org/annotation/VAR_050259|||http://purl.uniprot.org/annotation/VAR_050260|||http://purl.uniprot.org/annotation/VAR_050261|||http://purl.uniprot.org/annotation/VAR_050262|||http://purl.uniprot.org/annotation/VAR_050263|||http://purl.uniprot.org/annotation/VAR_050264|||http://purl.uniprot.org/annotation/VAR_062977|||http://purl.uniprot.org/annotation/VSP_007154|||http://purl.uniprot.org/annotation/VSP_007155|||http://purl.uniprot.org/annotation/VSP_007156|||http://purl.uniprot.org/annotation/VSP_007157|||http://purl.uniprot.org/annotation/VSP_007158|||http://purl.uniprot.org/annotation/VSP_007159|||http://purl.uniprot.org/annotation/VSP_007160|||http://purl.uniprot.org/annotation/VSP_007161|||http://purl.uniprot.org/annotation/VSP_007162|||http://purl.uniprot.org/annotation/VSP_007163|||http://purl.uniprot.org/annotation/VSP_007164|||http://purl.uniprot.org/annotation/VSP_007165|||http://purl.uniprot.org/annotation/VSP_007166|||http://purl.uniprot.org/annotation/VSP_057483|||http://purl.uniprot.org/annotation/VSP_057484|||http://purl.uniprot.org/annotation/VSP_057485|||http://purl.uniprot.org/annotation/VSP_057486|||http://purl.uniprot.org/annotation/VSP_057487
http://togogenome.org/gene/9606:DOK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BQ19|||http://purl.uniprot.org/uniprot/Q8TEW6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  DKFBH motif|||Docking protein 4|||IRS-type PTB|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187274
http://togogenome.org/gene/9606:ZFP36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QY76|||http://purl.uniprot.org/uniprot/P26651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with CNOT1 and impairs TNF mRNA deadenylation.|||Abolishes interaction with CNOT1.|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Inhibits ARE-containing RNA-binding, deadenylation and RNA decapping activities.|||Inhibits PKM-induced ZFP36 degradation through a p38 MAPK signaling pathway.|||Inhibits binding to ARE-containing transcripts. Inhibits binding to and deadenylation activities of ARE-containing mRNAs. Inhibits localization of ARE-containing mRNAs to processing bodies (PBs).|||Inhibits both ARE-binding and mRNA deadenylation activities.|||Inhibits interaction with SH3KBP1.|||Interaction with CNOT1|||Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activation|||Necessary for RNA-binding|||Necessary for interaction with PABPN1|||Necessary for localization of ARE-containing mRNAs to processing bodies (PBs)|||Necessary for mRNA decay activation|||Necessary for nuclear export|||Necessary for nuclear localization|||P-P-P-P-G|||Phosphoserine|||Phosphoserine; by MAPK1; in vitro|||Phosphoserine; by MAPKAPK2|||Phosphothreonine|||Polar residues|||mRNA decay activator protein ZFP36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089163|||http://purl.uniprot.org/annotation/VAR_021064|||http://purl.uniprot.org/annotation/VAR_021065|||http://purl.uniprot.org/annotation/VAR_021066|||http://purl.uniprot.org/annotation/VAR_052324
http://togogenome.org/gene/9606:PTPRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23470|||http://purl.uniprot.org/uniprot/Q49A02                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Ancestral active site|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||Loss of dimerization; when associated with E-958.|||Loss of dimerization; when associated with E-960.|||Loss of dimerization; when associated with K-1305.|||Loss of dimerization; when associated with K-1306.|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Receptor-type tyrosine-protein phosphatase gamma|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025441|||http://purl.uniprot.org/annotation/VAR_020301|||http://purl.uniprot.org/annotation/VAR_031562|||http://purl.uniprot.org/annotation/VAR_070892|||http://purl.uniprot.org/annotation/VSP_024353
http://togogenome.org/gene/9606:SCMH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMZ7|||http://purl.uniprot.org/uniprot/Q96GD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 6.|||In isoform 6.|||MBT|||MBT 1|||MBT 2|||Polar residues|||Polycomb protein SCMH1|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114334|||http://purl.uniprot.org/annotation/VSP_043395|||http://purl.uniprot.org/annotation/VSP_051676|||http://purl.uniprot.org/annotation/VSP_051677|||http://purl.uniprot.org/annotation/VSP_051678|||http://purl.uniprot.org/annotation/VSP_051679
http://togogenome.org/gene/9606:IFI27L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BM0                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||Interferon alpha-inducible protein 27-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147371|||http://purl.uniprot.org/annotation/VAR_062245
http://togogenome.org/gene/9606:FRMD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6L3|||http://purl.uniprot.org/uniprot/Q9BZ67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FERM|||FERM domain-containing protein 8|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295778|||http://purl.uniprot.org/annotation/VSP_027085|||http://purl.uniprot.org/annotation/VSP_056059
http://togogenome.org/gene/9606:CIBAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTR7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-105; E-108; E-1112; E-130 and E-132.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-105; E-108; E-112; E-130 and E-134.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-105; E-108; E-112; E-132 and E-134.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-105; E-108; E-130; E-132 and E-134.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-105; E-112; E-130; E-132 and E-134.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-108; E-112; E-130; E-132 and E-134.|||BAR-like|||CBY1-interacting BAR domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333004|||http://purl.uniprot.org/annotation/VAR_043035
http://togogenome.org/gene/9606:N4BP2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPY1|||http://purl.uniprot.org/uniprot/Q92802|||http://purl.uniprot.org/uniprot/Q9Y3H6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||NEDD4-binding protein 2-like 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299026|||http://purl.uniprot.org/annotation/PRO_5014567684|||http://purl.uniprot.org/annotation/VAR_034765|||http://purl.uniprot.org/annotation/VSP_027518|||http://purl.uniprot.org/annotation/VSP_041337|||http://purl.uniprot.org/annotation/VSP_041338|||http://purl.uniprot.org/annotation/VSP_041339
http://togogenome.org/gene/9606:ZBTB8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAP8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Zinc finger and BTB domain-containing protein 8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047721|||http://purl.uniprot.org/annotation/VAR_035602|||http://purl.uniprot.org/annotation/VSP_039858
http://togogenome.org/gene/9606:LNX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N448                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Ligand of Numb protein X 2|||NPXY motif|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055915|||http://purl.uniprot.org/annotation/VAR_024612
http://togogenome.org/gene/9606:CDH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55285                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003761|||http://purl.uniprot.org/annotation/PRO_0000003762|||http://purl.uniprot.org/annotation/VSP_000636|||http://purl.uniprot.org/annotation/VSP_000637
http://togogenome.org/gene/9606:TIPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRF3|||http://purl.uniprot.org/uniprot/Q9BVW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chromosome segregation in meiosis protein 3|||Disordered|||Interaction with TIMELESS|||Phosphoserine|||Phosphothreonine|||TIMELESS-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305253|||http://purl.uniprot.org/annotation/VAR_035194|||http://purl.uniprot.org/annotation/VAR_035195|||http://purl.uniprot.org/annotation/VAR_035196|||http://purl.uniprot.org/annotation/VAR_053952|||http://purl.uniprot.org/annotation/VAR_054483|||http://purl.uniprot.org/annotation/VAR_062207
http://togogenome.org/gene/9606:PAXIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW49                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with TP53BP1; impairs intact cellular response to DNA damage.|||Abolishes interaction with TP53BP1; prevents recruitment to DNA damage foci.|||Acidic residues|||BRCT 1|||BRCT 2|||BRCT 3|||BRCT 4|||BRCT 5|||BRCT 6|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PAGR1|||Interaction with TP53BP1|||Nuclear localization signal|||PAX-interacting protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296262|||http://purl.uniprot.org/annotation/VAR_034627|||http://purl.uniprot.org/annotation/VSP_040300|||http://purl.uniprot.org/annotation/VSP_040303
http://togogenome.org/gene/9606:METRNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q641Q3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Meteorin-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289104|||http://purl.uniprot.org/annotation/VSP_056101
http://togogenome.org/gene/9606:DBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNG2                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein DBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302849|||http://purl.uniprot.org/annotation/VAR_034969
http://togogenome.org/gene/9606:TUBA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71U36                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||5-glutamyl polyglutamate|||Detyrosinated tubulin alpha-1A chain|||Disordered|||In LIS3.|||In isoform 2.|||Involved in polymerization|||N6-acetyllysine|||Phosphoserine|||Tubulin alpha-1A chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048111|||http://purl.uniprot.org/annotation/PRO_0000437378|||http://purl.uniprot.org/annotation/VAR_034540|||http://purl.uniprot.org/annotation/VAR_039332|||http://purl.uniprot.org/annotation/VAR_039333|||http://purl.uniprot.org/annotation/VAR_039334|||http://purl.uniprot.org/annotation/VAR_039335|||http://purl.uniprot.org/annotation/VAR_039336|||http://purl.uniprot.org/annotation/VAR_039337|||http://purl.uniprot.org/annotation/VAR_039338|||http://purl.uniprot.org/annotation/VAR_078711|||http://purl.uniprot.org/annotation/VSP_046782
http://togogenome.org/gene/9606:ATP2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3L2|||http://purl.uniprot.org/uniprot/P16615                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In AKV; no effect on protein abundance; loss of calcium ion transmembrane transport.|||In DD.|||In DD; comedonal type.|||In DD; depression.|||In DD; haemorrhagic lesions and neuropsychiatric phenotype.|||In DD; haemorrhagic lesions.|||In DD; learning difficulties.|||In DD; mild/moderate form.|||In DD; mild/moderate/severe form; one patient with epilepsy.|||In DD; moderate form.|||In DD; multiple neuropsychiatric features.|||In DD; neuropsychiatric phenotype.|||In DD; retinitis pigmentosa.|||In DD; severe form.|||In DD; severe form; petit mal epilepsy.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with HAX1|||Interaction with PLN|||Interaction with TMEM64 and PDIA3|||Lumenal|||No effect on interaction with VMP1.|||Phosphoserine|||Phosphothreonine|||Sarcoplasmic/endoplasmic reticulum calcium ATPase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046196|||http://purl.uniprot.org/annotation/VAR_008608|||http://purl.uniprot.org/annotation/VAR_008609|||http://purl.uniprot.org/annotation/VAR_008610|||http://purl.uniprot.org/annotation/VAR_008611|||http://purl.uniprot.org/annotation/VAR_008612|||http://purl.uniprot.org/annotation/VAR_008613|||http://purl.uniprot.org/annotation/VAR_008614|||http://purl.uniprot.org/annotation/VAR_008615|||http://purl.uniprot.org/annotation/VAR_008616|||http://purl.uniprot.org/annotation/VAR_008617|||http://purl.uniprot.org/annotation/VAR_008618|||http://purl.uniprot.org/annotation/VAR_008619|||http://purl.uniprot.org/annotation/VAR_008620|||http://purl.uniprot.org/annotation/VAR_008621|||http://purl.uniprot.org/annotation/VAR_008622|||http://purl.uniprot.org/annotation/VAR_008623|||http://purl.uniprot.org/annotation/VAR_008624|||http://purl.uniprot.org/annotation/VAR_008625|||http://purl.uniprot.org/annotation/VAR_008626|||http://purl.uniprot.org/annotation/VAR_008627|||http://purl.uniprot.org/annotation/VAR_008628|||http://purl.uniprot.org/annotation/VAR_008629|||http://purl.uniprot.org/annotation/VAR_008630|||http://purl.uniprot.org/annotation/VAR_008631|||http://purl.uniprot.org/annotation/VAR_008632|||http://purl.uniprot.org/annotation/VAR_008633|||http://purl.uniprot.org/annotation/VAR_008634|||http://purl.uniprot.org/annotation/VAR_008635|||http://purl.uniprot.org/annotation/VAR_008636|||http://purl.uniprot.org/annotation/VAR_008637|||http://purl.uniprot.org/annotation/VAR_008638|||http://purl.uniprot.org/annotation/VAR_009508|||http://purl.uniprot.org/annotation/VAR_009509|||http://purl.uniprot.org/annotation/VAR_017532|||http://purl.uniprot.org/annotation/VAR_063398|||http://purl.uniprot.org/annotation/VAR_079685|||http://purl.uniprot.org/annotation/VAR_079686|||http://purl.uniprot.org/annotation/VAR_079687|||http://purl.uniprot.org/annotation/VAR_079688|||http://purl.uniprot.org/annotation/VAR_079689|||http://purl.uniprot.org/annotation/VAR_079690|||http://purl.uniprot.org/annotation/VAR_079691|||http://purl.uniprot.org/annotation/VAR_079692|||http://purl.uniprot.org/annotation/VAR_079693|||http://purl.uniprot.org/annotation/VAR_079694|||http://purl.uniprot.org/annotation/VAR_079695|||http://purl.uniprot.org/annotation/VAR_079696|||http://purl.uniprot.org/annotation/VAR_079697|||http://purl.uniprot.org/annotation/VSP_000358|||http://purl.uniprot.org/annotation/VSP_039392|||http://purl.uniprot.org/annotation/VSP_039393|||http://purl.uniprot.org/annotation/VSP_039394
http://togogenome.org/gene/9606:MZT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P582                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Mitotic-spindle organizing protein 2A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338987
http://togogenome.org/gene/9606:LHX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5S4|||http://purl.uniprot.org/uniprot/Q969G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In CPHD4.|||In CPHD4; has impaired activity on CGA, POU1F1 and TSHB promoters but exhibits normal DNA binding to the CGA pituitary glycoprotein basal element (PGBE) and interaction with the POU1F1 protein.|||In CPHD4; the mutant protein is inactive in DNA binding and pituitary gene activation assays.|||Interaction with 5-mCpG DNA|||Interaction with DNA|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075787|||http://purl.uniprot.org/annotation/VAR_046661|||http://purl.uniprot.org/annotation/VAR_058715|||http://purl.uniprot.org/annotation/VAR_058716|||http://purl.uniprot.org/annotation/VAR_058717|||http://purl.uniprot.org/annotation/VAR_063241
http://togogenome.org/gene/9606:SLC12A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSI7|||http://purl.uniprot.org/uniprot/Q9UHW9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amino acid permease/ SLC12A|||Basic and acidic residues|||Cytoplasmic|||Decreased phosphorylation by WNK kinases, leading to increased potassium-chloride cotransport activity. Increases Rb(+) uptake; when associated with D-96 and D-1048.|||Decreased phosphorylation by WNK kinases, leading to increased potassium-chloride cotransport activity. Increases Rb(+) uptake; when associated with D-96 and D-991.|||Decreases Rb(+) uptake; when associated with D-96 and D-1048.|||Decreases Rb(+) uptake; when associated with D-96 and D-991.|||Decreases Rb(+) uptake; when associated with D-991 and D-1048.|||Discontinuously helical|||Disordered|||Does not affect potassium-chloride cotransport activity.|||Extracellular|||Helical|||In ACCPN.|||In ACCPN; loss of potassium-chloride cotransport activity in Xenopus laevis oocytes likely due to impaired transit to cell membrane; loss of cell membrane localization.|||In ACCPN; loss of potassium-chloride cotransport activity; abnormal localization within the cytoplasm instead of cell membrane.|||In ACCPN; loss of potassium-chloride cotransport activity; abnormal perinuclear localization; stabilization of homodimeric state.|||In CMT2II.|||In CMT2II; abolished WNK kinase-dependent inhibitory phosphorylation; constitutively enhanced potassium-chloride cotransport activity; reduced acute swelling response to hypotonic stress.|||In CMT2II; unknown pathological significance.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||Increases Rb(+) uptake; when associated with D-991 and D-991.|||Increases trasnsporter activity.|||Interaction with CKB|||N-linked (GlcNAc...) asparagine|||No effect on transporter activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||Phosphotyrosine|||Polar residues|||SLC12A transporter C-terminal|||Slightly reduces transporter activity.|||Solute carrier family 12 member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178037|||http://purl.uniprot.org/annotation/VAR_014960|||http://purl.uniprot.org/annotation/VAR_087853|||http://purl.uniprot.org/annotation/VAR_087854|||http://purl.uniprot.org/annotation/VAR_087855|||http://purl.uniprot.org/annotation/VAR_087856|||http://purl.uniprot.org/annotation/VAR_087857|||http://purl.uniprot.org/annotation/VAR_087858|||http://purl.uniprot.org/annotation/VAR_087859|||http://purl.uniprot.org/annotation/VAR_087860|||http://purl.uniprot.org/annotation/VAR_087861|||http://purl.uniprot.org/annotation/VAR_087862|||http://purl.uniprot.org/annotation/VAR_087863|||http://purl.uniprot.org/annotation/VSP_006115|||http://purl.uniprot.org/annotation/VSP_006116|||http://purl.uniprot.org/annotation/VSP_041387|||http://purl.uniprot.org/annotation/VSP_041388|||http://purl.uniprot.org/annotation/VSP_041389
http://togogenome.org/gene/9606:SPACDR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ16                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Sperm acrosome developmental regulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325782
http://togogenome.org/gene/9606:IL27RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWB1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Interleukin-27 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010876
http://togogenome.org/gene/9606:EGFL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUX8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||Epidermal growth factor-like protein 6|||In isoform 2.|||MAM|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295811|||http://purl.uniprot.org/annotation/VAR_033366|||http://purl.uniprot.org/annotation/VAR_033367|||http://purl.uniprot.org/annotation/VAR_033368|||http://purl.uniprot.org/annotation/VAR_033369|||http://purl.uniprot.org/annotation/VSP_027089
http://togogenome.org/gene/9606:HNRNPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMB1|||http://purl.uniprot.org/uniprot/B4DMD1|||http://purl.uniprot.org/uniprot/B4DT28|||http://purl.uniprot.org/uniprot/O43390|||http://purl.uniprot.org/uniprot/Q0VGD6|||http://purl.uniprot.org/uniprot/Q6MZS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1; approximate|||2|||3 X 11 AA approximate repeats of D-D-Y-Y-G-Y-D-Y-H-D-Y|||3; approximate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein R|||In NEDDFSB.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Polar residues|||RNA-binding RGG-box|||RRM|||RRM 1|||RRM 2|||RRM 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081870|||http://purl.uniprot.org/annotation/VAR_087802|||http://purl.uniprot.org/annotation/VAR_087803|||http://purl.uniprot.org/annotation/VSP_038360|||http://purl.uniprot.org/annotation/VSP_047647|||http://purl.uniprot.org/annotation/VSP_054703
http://togogenome.org/gene/9606:SPTBN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15020                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In SCA5.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-acetylserine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin beta chain, non-erythrocytic 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073463|||http://purl.uniprot.org/annotation/VAR_026767|||http://purl.uniprot.org/annotation/VAR_026768|||http://purl.uniprot.org/annotation/VAR_026769|||http://purl.uniprot.org/annotation/VAR_026770|||http://purl.uniprot.org/annotation/VAR_026771|||http://purl.uniprot.org/annotation/VAR_035458|||http://purl.uniprot.org/annotation/VAR_048631|||http://purl.uniprot.org/annotation/VAR_070232|||http://purl.uniprot.org/annotation/VSP_000722
http://togogenome.org/gene/9606:SFT2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV19                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||Phosphoserine|||Vesicle transport protein SFT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238607|||http://purl.uniprot.org/annotation/VAR_034492
http://togogenome.org/gene/9606:CAND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75155                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Cullin-associated NEDD8-dissociated protein 2|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 21|||HEAT 22|||HEAT 23|||HEAT 24|||HEAT 25|||HEAT 26|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089297|||http://purl.uniprot.org/annotation/VAR_055023|||http://purl.uniprot.org/annotation/VAR_055024|||http://purl.uniprot.org/annotation/VAR_055025|||http://purl.uniprot.org/annotation/VAR_055026|||http://purl.uniprot.org/annotation/VAR_055027|||http://purl.uniprot.org/annotation/VAR_055028|||http://purl.uniprot.org/annotation/VAR_055029|||http://purl.uniprot.org/annotation/VAR_055030|||http://purl.uniprot.org/annotation/VSP_037240|||http://purl.uniprot.org/annotation/VSP_037241|||http://purl.uniprot.org/annotation/VSP_037242
http://togogenome.org/gene/9606:LBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52954                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||Transcription factor LBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049166
http://togogenome.org/gene/9606:FIP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UN15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Arg/Asp/Glu-rich domain|||Basic and acidic residues|||Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein|||Disordered|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Necessary for stimulating PAPOLA activity|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pre-mRNA 3'-end-processing factor FIP1|||Pro residues|||Sufficient for interaction with CPSF1 and CSTF3|||Sufficient for interaction with CPSF4|||Sufficient for interaction with PAPOLA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215037|||http://purl.uniprot.org/annotation/VSP_016728|||http://purl.uniprot.org/annotation/VSP_016729|||http://purl.uniprot.org/annotation/VSP_016730|||http://purl.uniprot.org/annotation/VSP_016731|||http://purl.uniprot.org/annotation/VSP_016732|||http://purl.uniprot.org/annotation/VSP_046213
http://togogenome.org/gene/9606:PRDX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32119|||http://purl.uniprot.org/uniprot/V9HW12                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH) intermediate|||Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity|||In isoform 2.|||Interchain (with C-172); in linked form|||Interchain (with C-51); in linked form|||N-acetylalanine|||Peroxiredoxin-2|||Phosphoserine|||Phosphothreonine|||Removed|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135080|||http://purl.uniprot.org/annotation/VAR_025051|||http://purl.uniprot.org/annotation/VSP_042924
http://togogenome.org/gene/9606:RHOH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15669|||http://purl.uniprot.org/uniprot/Q6ICP4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In EV4; loss-of-function variant resulting in impaired T-cell differentiation; unable to rescue T-cell lymphopenia in RHOH knockout mice; no protein detected in patient cells; results in defective TCR signaling in patient cells.|||Interaction with ZAP70|||Removed in mature form|||Rho-related GTP-binding protein RhoH|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198867|||http://purl.uniprot.org/annotation/PRO_0000281218|||http://purl.uniprot.org/annotation/VAR_081933
http://togogenome.org/gene/9606:USP17L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCW0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331645
http://togogenome.org/gene/9606:FMN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHS8|||http://purl.uniprot.org/uniprot/Q68DA7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FH1|||FH2|||Formin-1|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||Mediates interaction with alpha-catenin|||Microtubule-binding|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296361|||http://purl.uniprot.org/annotation/VAR_034630|||http://purl.uniprot.org/annotation/VSP_027208|||http://purl.uniprot.org/annotation/VSP_027209|||http://purl.uniprot.org/annotation/VSP_027210|||http://purl.uniprot.org/annotation/VSP_027211|||http://purl.uniprot.org/annotation/VSP_027212|||http://purl.uniprot.org/annotation/VSP_027213
http://togogenome.org/gene/9606:CHAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28329|||http://purl.uniprot.org/uniprot/Q6LEN5|||http://purl.uniprot.org/uniprot/Q6LEN6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Choline O-acetyltransferase|||Choline/carnitine acyltransferase|||Disordered|||In CMS6.|||In CMS6; completely lack activity.|||In CMS6; impaired activity.|||In isoform R.|||In isoform S.|||Phosphoserine|||Pro residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210154|||http://purl.uniprot.org/annotation/VAR_011666|||http://purl.uniprot.org/annotation/VAR_011667|||http://purl.uniprot.org/annotation/VAR_011668|||http://purl.uniprot.org/annotation/VAR_011669|||http://purl.uniprot.org/annotation/VAR_011670|||http://purl.uniprot.org/annotation/VAR_011671|||http://purl.uniprot.org/annotation/VAR_011672|||http://purl.uniprot.org/annotation/VAR_011673|||http://purl.uniprot.org/annotation/VAR_011674|||http://purl.uniprot.org/annotation/VAR_011675|||http://purl.uniprot.org/annotation/VAR_011676|||http://purl.uniprot.org/annotation/VAR_038605|||http://purl.uniprot.org/annotation/VAR_046683|||http://purl.uniprot.org/annotation/VAR_046684|||http://purl.uniprot.org/annotation/VAR_046685|||http://purl.uniprot.org/annotation/VAR_046686|||http://purl.uniprot.org/annotation/VAR_046687|||http://purl.uniprot.org/annotation/VAR_046688|||http://purl.uniprot.org/annotation/VSP_000790|||http://purl.uniprot.org/annotation/VSP_000791
http://togogenome.org/gene/9606:UXS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBZ7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished UDP-glucuronic acid decarboxylase activity.|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Proton acceptor|||Reduced UDP-glucuronic acid decarboxylase activity.|||Strongly reduced UDP-glucuronic acid decarboxylase activity, caused by a local unfolding of the active site that allows for a rotation of the dimer interface, leading to the formation of a homohexamer.|||Strongly reduced UDP-glucuronic acid decarboxylase activity.|||UDP-glucuronic acid decarboxylase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183269|||http://purl.uniprot.org/annotation/VSP_016756|||http://purl.uniprot.org/annotation/VSP_016757
http://togogenome.org/gene/9606:NR1H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8P7|||http://purl.uniprot.org/uniprot/P55055                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired ability to act as an anti-inflammatory role during the hepatic acute phase response; when associated with R-409.|||Impaired ability to act as an anti-inflammatory role during the hepatic acute phase response; when associated with R-447.|||In isoform 2.|||NR C4-type|||NR LBD|||Nuclear receptor|||Oxysterols receptor LXR-beta|||Polar residues|||Transactivation AF-1; required for ligand-independent transactivation function|||Transactivation AF-2; required for ligand-dependent transactivation function; mediates interaction with CCAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053532|||http://purl.uniprot.org/annotation/VAR_050579|||http://purl.uniprot.org/annotation/VSP_053789
http://togogenome.org/gene/9606:CSF2RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15509                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Granulocyte-macrophage colony-stimulating factor receptor subunit alpha|||Helical|||In SMDP4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010872|||http://purl.uniprot.org/annotation/VAR_058507|||http://purl.uniprot.org/annotation/VSP_001663|||http://purl.uniprot.org/annotation/VSP_001664|||http://purl.uniprot.org/annotation/VSP_001665|||http://purl.uniprot.org/annotation/VSP_001666|||http://purl.uniprot.org/annotation/VSP_001667|||http://purl.uniprot.org/annotation/VSP_001668|||http://purl.uniprot.org/annotation/VSP_001669|||http://purl.uniprot.org/annotation/VSP_001670|||http://purl.uniprot.org/annotation/VSP_043715|||http://purl.uniprot.org/annotation/VSP_044272
http://togogenome.org/gene/9606:ZNF432                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94892                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  3'-nitrotyrosine|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a breast cancer sample; somatic mutation.|||KRAB|||Zinc finger protein 432                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047580|||http://purl.uniprot.org/annotation/VAR_035577|||http://purl.uniprot.org/annotation/VAR_035578
http://togogenome.org/gene/9606:MRGPRX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB2|||http://purl.uniprot.org/uniprot/W8W3P5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decrease in ligand-mediated and ligand-independent receptor activity.|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increase in ligand-mediated receptor activity.|||Mas-related G-protein coupled receptor member X1|||N-linked (GlcNAc...) asparagine|||No alteration in ligand-mediated receptor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069772|||http://purl.uniprot.org/annotation/VAR_019432|||http://purl.uniprot.org/annotation/VAR_075462|||http://purl.uniprot.org/annotation/VAR_075463|||http://purl.uniprot.org/annotation/VAR_075464|||http://purl.uniprot.org/annotation/VAR_075465|||http://purl.uniprot.org/annotation/VAR_075466|||http://purl.uniprot.org/annotation/VAR_075467
http://togogenome.org/gene/9606:TLR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00206                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes LPS-response and prevents the cell surface expression.|||Abolishes LPS-response.|||Abolishes MYD88-binding and LPS-response.|||Cytoplasmic|||Extracellular|||Helical|||In allele TLR4*B; reduced LPS-response.|||In allele TLR4*B; reduced LPS-response; associated with an increased risk for age-related macular degeneration in Caucasian carriers.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||N-linked (GlcNAc...) asparagine|||Partially diminishes NF-kappa-B activation induced by Ni(2+). Strongly reduces NF-kappa-B activation induced by Ni(2+); when associated with A-431. Suppresses NF-kappa-B activation induced by Ni(2+); when associated with A-456.|||Partially diminishes NF-kappa-B activation induced by Ni(2+). Strongly reduces NF-kappa-B activation induced by Ni(2+); when associated with A-431. Suppresses NF-kappa-B activation induced by Ni(2+); when associated with A-458.|||Partially diminishes NF-kappa-B activation induced by Ni(2+). Strongly reduces NF-kappa-B activation induced by Ni(2+); when associated with A-456 or A-458.|||TIR|||Toll-like receptor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034722|||http://purl.uniprot.org/annotation/VAR_012739|||http://purl.uniprot.org/annotation/VAR_012740|||http://purl.uniprot.org/annotation/VAR_018729|||http://purl.uniprot.org/annotation/VAR_018730|||http://purl.uniprot.org/annotation/VAR_018731|||http://purl.uniprot.org/annotation/VAR_018732|||http://purl.uniprot.org/annotation/VAR_018733|||http://purl.uniprot.org/annotation/VAR_018734|||http://purl.uniprot.org/annotation/VAR_018735|||http://purl.uniprot.org/annotation/VAR_018736|||http://purl.uniprot.org/annotation/VAR_018737|||http://purl.uniprot.org/annotation/VAR_020334|||http://purl.uniprot.org/annotation/VAR_020335|||http://purl.uniprot.org/annotation/VAR_021977|||http://purl.uniprot.org/annotation/VAR_037668|||http://purl.uniprot.org/annotation/VAR_047563|||http://purl.uniprot.org/annotation/VAR_047564|||http://purl.uniprot.org/annotation/VAR_074187|||http://purl.uniprot.org/annotation/VSP_035793|||http://purl.uniprot.org/annotation/VSP_035794
http://togogenome.org/gene/9606:GRK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34947                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  15-20 fold defects in kinase activity; when associated with A-484.|||15-20 fold defects in kinase activity; when associated with A-485.|||AGC-kinase C-terminal|||Disordered|||Exerts a protective effect in heart failure and ischemia.|||Failed to phosphorylate p53/TP53.|||G protein-coupled receptor kinase 5|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||Interaction with calmodulin|||N-terminal|||No detectable plasma membrane localization; when associated with A-550; A-551; and A-554.|||No detectable plasma membrane localization; when associated with A-550; A-551; and A-555.|||No detectable plasma membrane localization; when associated with A-550; A-554; and A-555.|||No detectable plasma membrane localization; when associated with A-551; A-554; and A-555.|||Nuclear exclusion; when associated with A-388; A-389; A-391 and A-393.|||Nuclear exclusion; when associated with A-388; A-389; A-391 and A-394.|||Nuclear exclusion; when associated with A-388; A-389; A-393 and A-394.|||Nuclear exclusion; when associated with A-388; A-391; A-393 and A-394.|||Nuclear exclusion; when associated with A-389; A-391; A-393 and A-394.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RGS|||Sufficient for membrane localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085971|||http://purl.uniprot.org/annotation/VAR_040517|||http://purl.uniprot.org/annotation/VAR_040518|||http://purl.uniprot.org/annotation/VAR_040519|||http://purl.uniprot.org/annotation/VAR_040520|||http://purl.uniprot.org/annotation/VAR_040521|||http://purl.uniprot.org/annotation/VAR_040522|||http://purl.uniprot.org/annotation/VAR_040523
http://togogenome.org/gene/9606:TPRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Tumor protein p63-regulated gene 1 protein|||hSac2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268825
http://togogenome.org/gene/9606:CXCR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0R2|||http://purl.uniprot.org/uniprot/A8K647|||http://purl.uniprot.org/uniprot/P32302|||http://purl.uniprot.org/uniprot/Q2YD84                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-X-C chemokine receptor type 5|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||In isoform Short.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069360|||http://purl.uniprot.org/annotation/VAR_011838|||http://purl.uniprot.org/annotation/VAR_035757|||http://purl.uniprot.org/annotation/VSP_001892
http://togogenome.org/gene/9606:NUTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Basic and acidic residues|||Breakpoint for translocation to form BRD4-NUTM1 and BRD3-NUTM1 fusion proteins|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N5-methylglutamine|||NUT family member 1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311394|||http://purl.uniprot.org/annotation/VAR_037239|||http://purl.uniprot.org/annotation/VAR_037240|||http://purl.uniprot.org/annotation/VAR_037241|||http://purl.uniprot.org/annotation/VAR_037242|||http://purl.uniprot.org/annotation/VAR_037243|||http://purl.uniprot.org/annotation/VAR_037244|||http://purl.uniprot.org/annotation/VSP_029559|||http://purl.uniprot.org/annotation/VSP_029560|||http://purl.uniprot.org/annotation/VSP_029561|||http://purl.uniprot.org/annotation/VSP_055644|||http://purl.uniprot.org/annotation/VSP_055645
http://togogenome.org/gene/9606:MRPL38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein mL38|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261652|||http://purl.uniprot.org/annotation/VAR_029472|||http://purl.uniprot.org/annotation/VAR_059808|||http://purl.uniprot.org/annotation/VSP_056090
http://togogenome.org/gene/9606:SYCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAF6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Syncollin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295276|||http://purl.uniprot.org/annotation/VAR_033284
http://togogenome.org/gene/9606:SCARA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AZY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Collagen-like 1|||Collagen-like 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||Scavenger receptor class A member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181633|||http://purl.uniprot.org/annotation/VAR_025228|||http://purl.uniprot.org/annotation/VAR_025229|||http://purl.uniprot.org/annotation/VAR_025230|||http://purl.uniprot.org/annotation/VAR_025231|||http://purl.uniprot.org/annotation/VAR_025232|||http://purl.uniprot.org/annotation/VAR_025233|||http://purl.uniprot.org/annotation/VSP_017135|||http://purl.uniprot.org/annotation/VSP_017136
http://togogenome.org/gene/9606:TUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K9B1|||http://purl.uniprot.org/uniprot/F5H0R1|||http://purl.uniprot.org/uniprot/Q9H6E5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes adenylyltransferase activity; when associated with A-216.|||Abolishes adenylyltransferase activity; when associated with A-218.|||Basic and acidic residues|||Disordered|||KA1; binds the bulging loops of U6 snRNA but is dispensable for terminal uridylyltransferase activity|||Matrin-type|||PAP-associated|||Phosphoserine|||Polar residues|||RRM|||Reduced terminal uridylyltransferase activity; when associated with A-779.|||Reduced terminal uridylyltransferase activity; when associated with A-783.|||Speckle targeted PIP5K1A-regulated poly(A) polymerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254186|||http://purl.uniprot.org/annotation/VAR_028833
http://togogenome.org/gene/9606:APEX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWI9|||http://purl.uniprot.org/uniprot/B7ZA71|||http://purl.uniprot.org/uniprot/E5KN95|||http://purl.uniprot.org/uniprot/Q9UBZ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Abolished 3'-5' exonuclease activity; when associated with Asn-197. Synthetic lethality in a BRCA1 or BRCA2 mutant cell line background; when associated with Asn-197.|||Abolished 3'-5' exonuclease activity; when associated with Gln-48. Synthetic lethality in a BRCA1 or BRCA2 mutant cell line background; when associated with Gln-48.|||Abolishes AP endodeoxyribonuclease, 3'-5' exonuclease activity and 3'-phosphodiesterase activities.|||DNA-(apurinic or apyrimidinic site) endonuclease 2|||Disordered|||GRF-type|||Identified in a patient with mtDNA maintenance disorders.|||Important for catalytic activity|||Interaction with DNA substrate|||Loss of interaction with PCNA.|||Proton acceptor|||Proton donor/acceptor|||Reduces 3'-5' exonuclease activity in presence of PCNA. Does not abolish the 3'-5' exonuclease activity. Does only partially redistributes together with PCNA in nuclear foci in presence of oxidative-induced DNA damaging agents.|||Required for the interaction and colocalization with PCNA in nuclear foci in presence of oxidative-induced DNA damaging agents|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200014|||http://purl.uniprot.org/annotation/VAR_023390|||http://purl.uniprot.org/annotation/VAR_048261|||http://purl.uniprot.org/annotation/VAR_064033|||http://purl.uniprot.org/annotation/VAR_064034
http://togogenome.org/gene/9606:C16orf89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX73                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||UPF0764 protein C16orf89                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326202|||http://purl.uniprot.org/annotation/VAR_040004|||http://purl.uniprot.org/annotation/VAR_040005|||http://purl.uniprot.org/annotation/VAR_057992|||http://purl.uniprot.org/annotation/VSP_032600
http://togogenome.org/gene/9606:LRP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75197                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-propeller 1|||Beta-propeller 2|||Beta-propeller 3|||Beta-propeller 4|||Could be associated with idiopathic osteoporosis; does not result in a significant alteration of Wnt signal transduction.|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Found in a family affected by polycystic kidney and liver disease; unknown pathological significance; the patients carried additional PKD1 variants; the mutation results in significantly reduced WNT3A-induced signaling pathway.|||Found in a family with osteoporosis pseudoglioma syndrome; impairs protein trafficking to the endoplasmic reticulum and cell membrane.|||Found in a patient affected by polycystic kidney disease; unknown pathological significance; the patient also carried a PKD1 variant; results in significantly reduced WNT3A-induced signaling pathway.|||Helical|||In EVR1; decreases protein abundance.|||In EVR1; reduces Norrin signal transduction.|||In EVR4 and OPPG; unknown pathological significance; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In EVR4.|||In EVR4; an individual with abnormal retinal vasculature and retinal folds.|||In EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction.|||In EVR4; associated in a EVR1 patient with mutation Gln-417 in FZD4.|||In EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction.|||In EVR4; autosomal recessive.|||In EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction.|||In EVR4; de novo mutation found in a patient also carrying mutation P-540; unknown pathological significance; the mutation results in significantly reduced Norrin signal transduction.|||In EVR4; the mutation results in significantly reduced Norrin signal transduction.|||In EVR4; unknown pathological significance.|||In HBM.|||In HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1.|||In HBM; unknown pathological significance; lowered LRP5-mediated Wnt signaling; no effect on DKK1 binding.|||In OPPG and EVR1; reduces Norrin signal transduction.|||In OPPG.|||In OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In OPPG; is unable to traffic normally; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In OPPG; unknown pathological significance.|||In OPPG; unknown pathological significance; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In OPTA1, VBCH2 and WENHY.|||In OPTA1.|||In PCLD4; found in a family affected by polycystic liver disease; unknown pathological significance.|||In PCLD4; the mutation results in significantly reduced WNT3A-induced signaling pathway.|||In PCLD4; unknown pathological significance.|||In PCLD4; unknown pathological significance; the mutation results in significantly reduced WNT3A-induced signaling pathway.|||In PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant.|||In WENHY.|||In idiopathic osteoporosis and OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal.|||In idiopathic osteoporosis; shows an inhibitory effect on Wnt signal transduction.|||In primary osteoporosis.|||In primary osteoporosis; unknown pathological significance; found in a patient affected by polycystic kidney disease; unknown pathological significance.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 18|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Likely benign variant; no effect on Norrin signal transduction.|||Low-density lipoprotein receptor-related protein 5|||N-linked (GlcNAc...) asparagine|||PPPSP motif A|||PPPSP motif B|||PPPSP motif C|||PPPSP motif D|||PPPSP motif E|||Polar residues|||Pro residues|||YWTD 1|||YWTD 10|||YWTD 11|||YWTD 2|||YWTD 3|||YWTD 4|||YWTD 5|||YWTD 6|||YWTD 7|||YWTD 8|||YWTD 9 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017328|||http://purl.uniprot.org/annotation/VAR_018465|||http://purl.uniprot.org/annotation/VAR_018466|||http://purl.uniprot.org/annotation/VAR_018467|||http://purl.uniprot.org/annotation/VAR_021222|||http://purl.uniprot.org/annotation/VAR_021223|||http://purl.uniprot.org/annotation/VAR_021224|||http://purl.uniprot.org/annotation/VAR_021225|||http://purl.uniprot.org/annotation/VAR_021804|||http://purl.uniprot.org/annotation/VAR_021805|||http://purl.uniprot.org/annotation/VAR_021806|||http://purl.uniprot.org/annotation/VAR_021807|||http://purl.uniprot.org/annotation/VAR_021808|||http://purl.uniprot.org/annotation/VAR_021809|||http://purl.uniprot.org/annotation/VAR_021810|||http://purl.uniprot.org/annotation/VAR_021811|||http://purl.uniprot.org/annotation/VAR_021812|||http://purl.uniprot.org/annotation/VAR_021813|||http://purl.uniprot.org/annotation/VAR_021814|||http://purl.uniprot.org/annotation/VAR_021815|||http://purl.uniprot.org/annotation/VAR_021816|||http://purl.uniprot.org/annotation/VAR_021817|||http://purl.uniprot.org/annotation/VAR_035208|||http://purl.uniprot.org/annotation/VAR_058582|||http://purl.uniprot.org/annotation/VAR_063412|||http://purl.uniprot.org/annotation/VAR_063941|||http://purl.uniprot.org/annotation/VAR_063942|||http://purl.uniprot.org/annotation/VAR_063943|||http://purl.uniprot.org/annotation/VAR_063944|||http://purl.uniprot.org/annotation/VAR_063945|||http://purl.uniprot.org/annotation/VAR_063946|||http://purl.uniprot.org/annotation/VAR_063947|||http://purl.uniprot.org/annotation/VAR_063948|||http://purl.uniprot.org/annotation/VAR_063949|||http://purl.uniprot.org/annotation/VAR_063950|||http://purl.uniprot.org/annotation/VAR_063951|||http://purl.uniprot.org/annotation/VAR_063952|||http://purl.uniprot.org/annotation/VAR_063953|||http://purl.uniprot.org/annotation/VAR_063954|||http://purl.uniprot.org/annotation/VAR_063955|||http://purl.uniprot.org/annotation/VAR_063956|||http://purl.uniprot.org/annotation/VAR_063957|||http://purl.uniprot.org/annotation/VAR_063958|||http://purl.uniprot.org/annotation/VAR_063959|||http://purl.uniprot.org/annotation/VAR_063960|||http://purl.uniprot.org/annotation/VAR_063961|||http://purl.uniprot.org/annotation/VAR_063962|||http://purl.uniprot.org/annotation/VAR_063963|||http://purl.uniprot.org/annotation/VAR_063964|||http://purl.uniprot.org/annotation/VAR_063965|||http://purl.uniprot.org/annotation/VAR_063966|||http://purl.uniprot.org/annotation/VAR_063967|||http://purl.uniprot.org/annotation/VAR_063968|||http://purl.uniprot.org/annotation/VAR_063969|||http://purl.uniprot.org/annotation/VAR_063970|||http://purl.uniprot.org/annotation/VAR_063971|||http://purl.uniprot.org/annotation/VAR_063972|||http://purl.uniprot.org/annotation/VAR_063973|||http://purl.uniprot.org/annotation/VAR_063974|||http://purl.uniprot.org/annotation/VAR_063975|||http://purl.uniprot.org/annotation/VAR_063976|||http://purl.uniprot.org/annotation/VAR_063977|||http://purl.uniprot.org/annotation/VAR_063978|||http://purl.uniprot.org/annotation/VAR_063979|||http://purl.uniprot.org/annotation/VAR_063980|||http://purl.uniprot.org/annotation/VAR_063981|||http://purl.uniprot.org/annotation/VAR_071012|||http://purl.uniprot.org/annotation/VAR_071013|||http://purl.uniprot.org/annotation/VAR_071014|||http://purl.uniprot.org/annotation/VAR_071015|||http://purl.uniprot.org/annotation/VAR_076548|||http://purl.uniprot.org/annotation/VAR_076549|||http://purl.uniprot.org/annotation/VAR_076550|||http://purl.uniprot.org/annotation/VAR_080857|||http://purl.uniprot.org/annotation/VAR_080858|||http://purl.uniprot.org/annotation/VAR_080859|||http://purl.uniprot.org/annotation/VAR_080860|||http://purl.uniprot.org/annotation/VAR_080861|||http://purl.uniprot.org/annotation/VAR_080862|||http://purl.uniprot.org/annotation/VAR_080863|||http://purl.uniprot.org/annotation/VAR_080935|||http://purl.uniprot.org/annotation/VAR_080936|||http://purl.uniprot.org/annotation/VAR_080937|||http://purl.uniprot.org/annotation/VAR_080938|||http://purl.uniprot.org/annotation/VAR_085732|||http://purl.uniprot.org/annotation/VAR_085733|||http://purl.uniprot.org/annotation/VAR_085734
http://togogenome.org/gene/9606:MKNK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K341|||http://purl.uniprot.org/uniprot/Q9BUB5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active.|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of kinase activity; when associated with D-232.|||Loss of kinase activity; when associated with K-78.|||Loss of kinase activity; when associated with T-250.|||Loss of kinase activity; when associated with T-255.|||MAP kinase-interacting serine/threonine-protein kinase 1|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086334|||http://purl.uniprot.org/annotation/VAR_040801|||http://purl.uniprot.org/annotation/VAR_040802|||http://purl.uniprot.org/annotation/VAR_040803|||http://purl.uniprot.org/annotation/VAR_040804|||http://purl.uniprot.org/annotation/VSP_007352|||http://purl.uniprot.org/annotation/VSP_017515
http://togogenome.org/gene/9606:SLC38A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUX1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Involved in pH-sensing to the transport activity regulation|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Sodium-coupled neutral amino acid transporter 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312115|||http://purl.uniprot.org/annotation/VAR_037396|||http://purl.uniprot.org/annotation/VSP_029702
http://togogenome.org/gene/9606:GAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54826                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated serine|||Growth arrest-specific protein 1|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021318|||http://purl.uniprot.org/annotation/PRO_0000021319
http://togogenome.org/gene/9606:PRELP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51888                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||Pro residues|||Prolargin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032744|||http://purl.uniprot.org/annotation/VAR_011976|||http://purl.uniprot.org/annotation/VAR_052012|||http://purl.uniprot.org/annotation/VAR_052013|||http://purl.uniprot.org/annotation/VAR_061804
http://togogenome.org/gene/9606:TMEM8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDV4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333039|||http://purl.uniprot.org/annotation/VSP_033450|||http://purl.uniprot.org/annotation/VSP_033451|||http://purl.uniprot.org/annotation/VSP_033452|||http://purl.uniprot.org/annotation/VSP_033453
http://togogenome.org/gene/9606:ALK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6D4Y2|||http://purl.uniprot.org/uniprot/Q9UM73                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ALK tyrosine kinase receptor|||Abolished heparin-binding, leading to decreased ALK activation.|||Basic and acidic residues|||Breakpoint for translocation to form the EML4-ALK fusion protein (variant 1)|||Breakpoint for translocation to form the EML4-ALK fusion protein (variant 2)|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Heparin-binding region|||Impairs interaction with SHC1.|||In NBLST3.|||In NBLST3; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments.|||In NBLST3; somatic mutation.|||In NBLST3; somatic mutation; constitutively activated; retained in the endoplasmic reticulum and Golgi compartments.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||LDL-receptor class A|||MAM|||MAM 1|||MAM 2|||N-linked (GlcNAc...) asparagine|||Observed in neuroblastoma.|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||SlStrongly reduced autophosphorylation and subsequent activation; when associated with A-966.|||Slightly decreased autophosphorylation. Decreased autophosphorylation and subsequent activation; when associated with A-859.|||Slightly decreased autophosphorylation. Decreased autophosphorylation and subsequent activation; when associated with A-974.|||Slightly decreased autophosphorylation. Strongly reduced autophosphorylation and subsequent activation; when associated with A-994.|||Tyrosine-protein kinase receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016740|||http://purl.uniprot.org/annotation/PRO_5002841536|||http://purl.uniprot.org/annotation/VAR_031042|||http://purl.uniprot.org/annotation/VAR_031043|||http://purl.uniprot.org/annotation/VAR_031044|||http://purl.uniprot.org/annotation/VAR_041477|||http://purl.uniprot.org/annotation/VAR_041478|||http://purl.uniprot.org/annotation/VAR_041479|||http://purl.uniprot.org/annotation/VAR_041480|||http://purl.uniprot.org/annotation/VAR_041481|||http://purl.uniprot.org/annotation/VAR_041482|||http://purl.uniprot.org/annotation/VAR_041483|||http://purl.uniprot.org/annotation/VAR_041484|||http://purl.uniprot.org/annotation/VAR_041485|||http://purl.uniprot.org/annotation/VAR_041486|||http://purl.uniprot.org/annotation/VAR_041487|||http://purl.uniprot.org/annotation/VAR_041488|||http://purl.uniprot.org/annotation/VAR_041489|||http://purl.uniprot.org/annotation/VAR_041490|||http://purl.uniprot.org/annotation/VAR_041491|||http://purl.uniprot.org/annotation/VAR_055987|||http://purl.uniprot.org/annotation/VAR_055988|||http://purl.uniprot.org/annotation/VAR_061288|||http://purl.uniprot.org/annotation/VAR_063850|||http://purl.uniprot.org/annotation/VAR_063851|||http://purl.uniprot.org/annotation/VAR_063852|||http://purl.uniprot.org/annotation/VAR_063853|||http://purl.uniprot.org/annotation/VAR_063854|||http://purl.uniprot.org/annotation/VAR_063855|||http://purl.uniprot.org/annotation/VAR_063856|||http://purl.uniprot.org/annotation/VAR_063857|||http://purl.uniprot.org/annotation/VAR_063858|||http://purl.uniprot.org/annotation/VAR_063859|||http://purl.uniprot.org/annotation/VAR_063860|||http://purl.uniprot.org/annotation/VAR_063861|||http://purl.uniprot.org/annotation/VAR_063862|||http://purl.uniprot.org/annotation/VAR_063863|||http://purl.uniprot.org/annotation/VAR_063864|||http://purl.uniprot.org/annotation/VAR_063865|||http://purl.uniprot.org/annotation/VAR_063866
http://togogenome.org/gene/9606:SLC19A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41440                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Completely abolishes N-glycosylation without affecting subcellular location or folate:anion antiporter activity.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MEGAF; loss of cellular uptake of folates, including methotrexate.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduced folate transporter|||Required for substrate-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178660|||http://purl.uniprot.org/annotation/VAR_020210|||http://purl.uniprot.org/annotation/VAR_052404|||http://purl.uniprot.org/annotation/VAR_085516|||http://purl.uniprot.org/annotation/VSP_042891|||http://purl.uniprot.org/annotation/VSP_044497
http://togogenome.org/gene/9606:JAM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX67                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased palmitoylation. Abolishes palmitoylation; when associated with S-264.|||Decreased palmitoylation. Abolishes palmitoylation; when associated with S-265.|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In HDBSCC; normal location at the cell membrane.|||In HDBSCC; the mutant is retained in the endoplasmic reticulum.|||In isoform 2.|||Junctional adhesion molecule C|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine|||Soluble form of JAM-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015071|||http://purl.uniprot.org/annotation/PRO_0000445336|||http://purl.uniprot.org/annotation/VAR_069529|||http://purl.uniprot.org/annotation/VAR_069530|||http://purl.uniprot.org/annotation/VSP_042561
http://togogenome.org/gene/9606:PIP4K2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQV3|||http://purl.uniprot.org/uniprot/Q8TBX8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Loss of interaction with PIP5K1A. Loss of inhibition of PIP5K1A activity.|||N-acetylalanine|||PIPK|||Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma|||Phosphoserine|||Removed|||Required for interaction with PIP5K1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285750|||http://purl.uniprot.org/annotation/VAR_032049|||http://purl.uniprot.org/annotation/VAR_032050|||http://purl.uniprot.org/annotation/VAR_032051|||http://purl.uniprot.org/annotation/VSP_042929|||http://purl.uniprot.org/annotation/VSP_043369
http://togogenome.org/gene/9606:MAB21L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y586                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In MCSKS; Decreased stability; does not affect subcellular localization.|||In MCSKS; complete loss of ssRNA-binding activity with the variant protein.|||In MCSKS; complete loss of ssRNA-binding activity with the variant protein; shows a higher stability than wild-type in tetracycline-inducible cells.|||Protein mab-21-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312787|||http://purl.uniprot.org/annotation/VAR_071831|||http://purl.uniprot.org/annotation/VAR_071832|||http://purl.uniprot.org/annotation/VAR_071833|||http://purl.uniprot.org/annotation/VAR_071834|||http://purl.uniprot.org/annotation/VAR_079053
http://togogenome.org/gene/9606:APOL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Apolipoprotein L5|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137603|||http://purl.uniprot.org/annotation/VAR_020355|||http://purl.uniprot.org/annotation/VAR_020356|||http://purl.uniprot.org/annotation/VAR_020357|||http://purl.uniprot.org/annotation/VAR_053012
http://togogenome.org/gene/9606:MROH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGR9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||Maestro heat-like repeat-containing protein family member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320922|||http://purl.uniprot.org/annotation/VAR_039305|||http://purl.uniprot.org/annotation/VAR_039306|||http://purl.uniprot.org/annotation/VAR_039307|||http://purl.uniprot.org/annotation/VAR_061595
http://togogenome.org/gene/9606:RFX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YED2|||http://purl.uniprot.org/uniprot/Q6ZV50                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DNA-binding protein RFX8|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||RFX-type winged-helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325808|||http://purl.uniprot.org/annotation/VSP_039427|||http://purl.uniprot.org/annotation/VSP_039428|||http://purl.uniprot.org/annotation/VSP_039429|||http://purl.uniprot.org/annotation/VSP_039430|||http://purl.uniprot.org/annotation/VSP_039431
http://togogenome.org/gene/9606:HDAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92769                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Histone deacetylase|||Histone deacetylase 2|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114693|||http://purl.uniprot.org/annotation/VAR_025311|||http://purl.uniprot.org/annotation/VAR_025312|||http://purl.uniprot.org/annotation/VSP_056175
http://togogenome.org/gene/9606:SRPRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q549N5|||http://purl.uniprot.org/uniprot/Q9Y5M8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Phosphothreonine|||Signal recognition particle receptor subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101227|||http://purl.uniprot.org/annotation/VAR_057335
http://togogenome.org/gene/9606:PSME3IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2, strongly reduces interaction with PSME3 and abolishes effect on proteasome activity.|||Basic and acidic residues|||Disordered|||Interaction with PSME3|||N-acetylmethionine|||N6-acetyllysine|||PSME3-interacting protein|||Phosphoserine|||Phosphoserine; by CK2|||Reduces phosphorylation by CK2 and interaction with PSME3; when associated with A-222.|||Reduces phosphorylation by CK2 and interaction with PSME3; when associated with A-228.|||Strongly reduces phosphorylation by CK2 and interaction with PSME3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096847
http://togogenome.org/gene/9606:HERC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAQ8|||http://purl.uniprot.org/uniprot/O95714                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to SUMO; when associated with S-2708.|||Abolishes binding to SUMO; when associated with S-2711.|||Acidic residues|||Basic and acidic residues|||Cytochrome b5 heme-binding|||DOC|||Disordered|||E3 ubiquitin-protein ligase HERC2|||Glycyl thioester intermediate|||HECT|||In MRT38; decreased protein abundance in transfected cells.|||MIB/HERC2|||Phosphoserine|||Phosphothreonine|||Prevents HERC2 C-terminal fragment binding to endogenous RNF8.|||RCC1|||RCC1 1-1|||RCC1 1-2|||RCC1 1-3|||RCC1 1-4|||RCC1 1-5|||RCC1 1-6|||RCC1 1-7|||RCC1 2-1|||RCC1 2-2|||RCC1 2-3|||RCC1 2-4|||RCC1 2-5|||RCC1 2-6|||RCC1 2-7|||RCC1 3-1|||RCC1 3-2|||RCC1 3-3|||RCC1 3-4|||RCC1 3-5|||RCC1 3-6|||RCC1 3-7|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229739|||http://purl.uniprot.org/annotation/VAR_069282
http://togogenome.org/gene/9606:DENND5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0Z4N9|||http://purl.uniprot.org/uniprot/Q6IQ26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DENN domain-containing protein 5A|||Disordered|||In DEE49; unknown pathological significance.|||In isoform 2.|||PLAT|||Phosphoserine|||Phosphothreonine|||RUN|||RUN 1|||RUN 2|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097142|||http://purl.uniprot.org/annotation/VAR_028409|||http://purl.uniprot.org/annotation/VAR_078555|||http://purl.uniprot.org/annotation/VSP_044688
http://togogenome.org/gene/9606:WIPI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX63|||http://purl.uniprot.org/uniprot/G5EA37|||http://purl.uniprot.org/uniprot/Q5MNZ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||L/FRRG motif|||Loss of binding to phosphoinositides and abolishes puncta formation.|||Loss of binding to phosphoinositides, does not disrupt the MPR pathway.|||Nuclear receptor interaction|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat domain phosphoinositide-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051437|||http://purl.uniprot.org/annotation/VAR_024848|||http://purl.uniprot.org/annotation/VAR_053439|||http://purl.uniprot.org/annotation/VSP_016966
http://togogenome.org/gene/9606:DVL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14640                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DEP|||DIX|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||Polar residues|||Segment polarity protein dishevelled homolog DVL-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145742|||http://purl.uniprot.org/annotation/VSP_024460
http://togogenome.org/gene/9606:GAREM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H706                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  CABIT|||Disordered|||Does not abolish phosphorylation upon EGF stimulation. Abolishes interaction with PTPN11. Abolishes phosphorylation upon EGF stimulation; when associated with F-105.|||Does not abolish phosphorylation upon EGF stimulation. Reduces interaction with GRB2. Abolishes phosphorylation, interaction with GRB2 and ERK activation upon EGF stimulation; when associated with F-453.|||GRB2-associated and regulator of MAPK protein 1|||In isoform 2.|||In isoform 3.|||Necessary for interaction with GRB2|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277647|||http://purl.uniprot.org/annotation/VAR_030580|||http://purl.uniprot.org/annotation/VAR_030581|||http://purl.uniprot.org/annotation/VAR_030582|||http://purl.uniprot.org/annotation/VAR_030583|||http://purl.uniprot.org/annotation/VAR_030584|||http://purl.uniprot.org/annotation/VSP_023047|||http://purl.uniprot.org/annotation/VSP_023048
http://togogenome.org/gene/9606:HSFY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Heat shock transcription factor, Y-linked|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124573|||http://purl.uniprot.org/annotation/VSP_009179|||http://purl.uniprot.org/annotation/VSP_009180|||http://purl.uniprot.org/annotation/VSP_009181|||http://purl.uniprot.org/annotation/VSP_009182
http://togogenome.org/gene/9606:OPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6K4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a family with foveal hypoplasia; unknown pathological significance.|||In OPA3.|||In isoform 2.|||Optic atrophy 3 protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220763|||http://purl.uniprot.org/annotation/VAR_033103|||http://purl.uniprot.org/annotation/VAR_033104|||http://purl.uniprot.org/annotation/VAR_085736|||http://purl.uniprot.org/annotation/VSP_032681
http://togogenome.org/gene/9606:JMJD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C870                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7|||Impairs homodimer formation.|||Interchain|||JmjC|||Loss of peptidase activity toward methylated histones and reduced anchorage-independent growth of transformed cells; when associated with A-180 and A-277.|||Loss of peptidase activity toward methylated histones and reduced anchorage-independent growth of transformed cells; when associated with A-180 and A-277. Impairs L-lysine (3S)-hydroxylase activity. Impairs the interaction with DRG1 and DRG2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349374|||http://purl.uniprot.org/annotation/VAR_027046|||http://purl.uniprot.org/annotation/VAR_069392
http://togogenome.org/gene/9606:ERLIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384ME54|||http://purl.uniprot.org/uniprot/O94905                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Band 7|||Cytoplasmic|||Erlin|||Erlin-2|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with ERLIN1|||Loss of glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002787|||http://purl.uniprot.org/annotation/PRO_5017404720|||http://purl.uniprot.org/annotation/VAR_059140|||http://purl.uniprot.org/annotation/VSP_008713|||http://purl.uniprot.org/annotation/VSP_008714|||http://purl.uniprot.org/annotation/VSP_013940|||http://purl.uniprot.org/annotation/VSP_013941
http://togogenome.org/gene/9606:JADE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92613                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Protein Jade-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059309
http://togogenome.org/gene/9606:RPL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18621                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein uL22|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125331|||http://purl.uniprot.org/annotation/VSP_045445|||http://purl.uniprot.org/annotation/VSP_046965
http://togogenome.org/gene/9606:OR4K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGD4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150552|||http://purl.uniprot.org/annotation/VAR_054121|||http://purl.uniprot.org/annotation/VAR_054122|||http://purl.uniprot.org/annotation/VAR_054123
http://togogenome.org/gene/9606:OR14J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW10|||http://purl.uniprot.org/uniprot/Q9UGF5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 14J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150616|||http://purl.uniprot.org/annotation/VAR_034234|||http://purl.uniprot.org/annotation/VAR_034235
http://togogenome.org/gene/9606:ZNF497                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNH5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Zinc finger protein 497                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047618|||http://purl.uniprot.org/annotation/VAR_055270
http://togogenome.org/gene/9606:PELI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase pellino homolog 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194176|||http://purl.uniprot.org/annotation/VAR_061502|||http://purl.uniprot.org/annotation/VSP_008639|||http://purl.uniprot.org/annotation/VSP_008640|||http://purl.uniprot.org/annotation/VSP_008641|||http://purl.uniprot.org/annotation/VSP_008642
http://togogenome.org/gene/9606:TCF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGU0|||http://purl.uniprot.org/uniprot/W5ZR30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||Basic and acidic residues|||Basic residues|||C2HC pre-PHD-type; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In DDVIBA.|||In DDVIBA; unknown pathological significance.|||In isoform 2.|||Leucine-zipper|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Transcription factor 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072448|||http://purl.uniprot.org/annotation/VAR_025427|||http://purl.uniprot.org/annotation/VAR_025428|||http://purl.uniprot.org/annotation/VAR_025429|||http://purl.uniprot.org/annotation/VAR_025430|||http://purl.uniprot.org/annotation/VAR_051419|||http://purl.uniprot.org/annotation/VAR_051420|||http://purl.uniprot.org/annotation/VAR_082677|||http://purl.uniprot.org/annotation/VAR_082678|||http://purl.uniprot.org/annotation/VAR_082679|||http://purl.uniprot.org/annotation/VAR_082680|||http://purl.uniprot.org/annotation/VAR_082681|||http://purl.uniprot.org/annotation/VAR_082682|||http://purl.uniprot.org/annotation/VAR_082683|||http://purl.uniprot.org/annotation/VAR_082684|||http://purl.uniprot.org/annotation/VAR_082685|||http://purl.uniprot.org/annotation/VAR_082686|||http://purl.uniprot.org/annotation/VAR_082687|||http://purl.uniprot.org/annotation/VAR_082688|||http://purl.uniprot.org/annotation/VAR_082689|||http://purl.uniprot.org/annotation/VAR_082690|||http://purl.uniprot.org/annotation/VAR_082691|||http://purl.uniprot.org/annotation/VAR_082692|||http://purl.uniprot.org/annotation/VAR_082693|||http://purl.uniprot.org/annotation/VAR_082694|||http://purl.uniprot.org/annotation/VAR_082695|||http://purl.uniprot.org/annotation/VAR_082696|||http://purl.uniprot.org/annotation/VAR_082697|||http://purl.uniprot.org/annotation/VAR_082698|||http://purl.uniprot.org/annotation/VSP_003984|||http://purl.uniprot.org/annotation/VSP_003985
http://togogenome.org/gene/9606:CYP24A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07973                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial|||In HCINF1; complete loss of function.|||In HCINF1; retains small but measurable levels of activity.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003615|||http://purl.uniprot.org/annotation/VAR_048464|||http://purl.uniprot.org/annotation/VAR_048465|||http://purl.uniprot.org/annotation/VAR_048466|||http://purl.uniprot.org/annotation/VAR_066408|||http://purl.uniprot.org/annotation/VAR_066409|||http://purl.uniprot.org/annotation/VAR_066410|||http://purl.uniprot.org/annotation/VAR_066411|||http://purl.uniprot.org/annotation/VSP_043101|||http://purl.uniprot.org/annotation/VSP_053367|||http://purl.uniprot.org/annotation/VSP_053368
http://togogenome.org/gene/9606:USP17L20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RJB6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421094
http://togogenome.org/gene/9606:ASB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6TX30|||http://purl.uniprot.org/uniprot/Q9NWX5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 6|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066933|||http://purl.uniprot.org/annotation/VSP_042006
http://togogenome.org/gene/9606:OSTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92882                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||N-acetylserine|||Osteoclast-stimulating factor 1|||Phosphoserine|||Phosphothreonine|||Removed|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067035|||http://purl.uniprot.org/annotation/VAR_026573|||http://purl.uniprot.org/annotation/VAR_048309
http://togogenome.org/gene/9606:ODF2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULJ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 6.|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 5.|||Protein BCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308909|||http://purl.uniprot.org/annotation/VAR_036882|||http://purl.uniprot.org/annotation/VAR_036883|||http://purl.uniprot.org/annotation/VSP_029057|||http://purl.uniprot.org/annotation/VSP_029058|||http://purl.uniprot.org/annotation/VSP_029059|||http://purl.uniprot.org/annotation/VSP_029060|||http://purl.uniprot.org/annotation/VSP_040930
http://togogenome.org/gene/9606:MAP3K7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43318                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate|||Abolishes ubiquitination.|||Disordered|||Enhances autophosphorylation; Alters MAPK signaling.|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CSCF.|||In FMD2.|||In FMD2; does not affect interaction with TAB2; does not affect homodimerization; increases autophosphorylation; increases MAPK signaling; increases NF-kappa-B signaling.|||In FMD2; increases autophosphorylation; no effect on MAPK signaling; no effect on NF-kappa-B signaling.|||In isoform 1A and isoform 1D.|||In isoform 1C and isoform 1D.|||Interaction with MAPK8IP1|||Loss of kinase activity. Loss of autophosphorylation.|||Mitogen-activated protein kinase kinase kinase 7|||No effect on ubiquitination.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis; alternate|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly decreases ubiquitination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086252|||http://purl.uniprot.org/annotation/VAR_077341|||http://purl.uniprot.org/annotation/VAR_077342|||http://purl.uniprot.org/annotation/VAR_077343|||http://purl.uniprot.org/annotation/VAR_077344|||http://purl.uniprot.org/annotation/VAR_077345|||http://purl.uniprot.org/annotation/VAR_077346|||http://purl.uniprot.org/annotation/VAR_077347|||http://purl.uniprot.org/annotation/VAR_080761|||http://purl.uniprot.org/annotation/VSP_004886|||http://purl.uniprot.org/annotation/VSP_004887|||http://purl.uniprot.org/annotation/VSP_004888
http://togogenome.org/gene/9606:GNG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59768                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2|||N-acetylalanine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012611|||http://purl.uniprot.org/annotation/PRO_0000012612
http://togogenome.org/gene/9606:RANBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK94|||http://purl.uniprot.org/uniprot/B3KUP2|||http://purl.uniprot.org/uniprot/B4DE76|||http://purl.uniprot.org/uniprot/F6WQW2|||http://purl.uniprot.org/uniprot/P43487                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Ran-specific GTPase-activating protein|||RanBD1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213667|||http://purl.uniprot.org/annotation/VAR_036567|||http://purl.uniprot.org/annotation/VAR_053629|||http://purl.uniprot.org/annotation/VSP_055104
http://togogenome.org/gene/9606:RTN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQC3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 6.|||In isoform B.|||In isoform B2.|||In isoform C.|||In isoform D.|||Lumenal|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reticulon|||Reticulon-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168165|||http://purl.uniprot.org/annotation/VAR_035904|||http://purl.uniprot.org/annotation/VAR_053633|||http://purl.uniprot.org/annotation/VAR_053634|||http://purl.uniprot.org/annotation/VAR_053635|||http://purl.uniprot.org/annotation/VSP_005652|||http://purl.uniprot.org/annotation/VSP_005653|||http://purl.uniprot.org/annotation/VSP_005654|||http://purl.uniprot.org/annotation/VSP_005655|||http://purl.uniprot.org/annotation/VSP_037112|||http://purl.uniprot.org/annotation/VSP_037113
http://togogenome.org/gene/9606:BBOF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND07                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basal body-orientation factor 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252293|||http://purl.uniprot.org/annotation/VAR_027815|||http://purl.uniprot.org/annotation/VAR_059618|||http://purl.uniprot.org/annotation/VAR_059619|||http://purl.uniprot.org/annotation/VAR_059620
http://togogenome.org/gene/9606:ME2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23368                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes activation by fumarate.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||NAD-dependent malic enzyme, mitochondrial|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018537|||http://purl.uniprot.org/annotation/VAR_034104|||http://purl.uniprot.org/annotation/VAR_050017|||http://purl.uniprot.org/annotation/VSP_042717
http://togogenome.org/gene/9606:SOSTDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D125|||http://purl.uniprot.org/uniprot/Q6X4U4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||CTCK|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sclerostin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033180|||http://purl.uniprot.org/annotation/PRO_5014296869|||http://purl.uniprot.org/annotation/VAR_053682|||http://purl.uniprot.org/annotation/VSP_054240
http://togogenome.org/gene/9606:SLC2A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK5|||http://purl.uniprot.org/uniprot/B4DG19|||http://purl.uniprot.org/uniprot/P22732                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect D-fructose or D-glucose transport.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Major facilitator superfamily (MFS) profile|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050369|||http://purl.uniprot.org/annotation/VAR_081827|||http://purl.uniprot.org/annotation/VSP_042031
http://togogenome.org/gene/9606:TMUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Q3|||http://purl.uniprot.org/uniprot/Q9BVT8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Required to release iHOPS from membranes|||Transmembrane and ubiquitin-like domain-containing protein 1|||Ubiquitin-like|||iHOPS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114922|||http://purl.uniprot.org/annotation/PRO_0000435488
http://togogenome.org/gene/9606:MYO18B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUG5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GPA|||IQ|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Myosin motor|||Phosphoserine|||Polar residues|||Tail|||Unconventional myosin-XVIIIb                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123478|||http://purl.uniprot.org/annotation/VAR_015862|||http://purl.uniprot.org/annotation/VAR_015863|||http://purl.uniprot.org/annotation/VAR_015864|||http://purl.uniprot.org/annotation/VAR_015865|||http://purl.uniprot.org/annotation/VAR_015866|||http://purl.uniprot.org/annotation/VAR_015867|||http://purl.uniprot.org/annotation/VAR_015868|||http://purl.uniprot.org/annotation/VAR_015869|||http://purl.uniprot.org/annotation/VAR_015870|||http://purl.uniprot.org/annotation/VAR_015871|||http://purl.uniprot.org/annotation/VAR_015872|||http://purl.uniprot.org/annotation/VAR_015873|||http://purl.uniprot.org/annotation/VAR_015874|||http://purl.uniprot.org/annotation/VAR_015875|||http://purl.uniprot.org/annotation/VAR_015876|||http://purl.uniprot.org/annotation/VAR_015877|||http://purl.uniprot.org/annotation/VAR_015878|||http://purl.uniprot.org/annotation/VAR_015879|||http://purl.uniprot.org/annotation/VAR_056190|||http://purl.uniprot.org/annotation/VAR_056191|||http://purl.uniprot.org/annotation/VAR_056192|||http://purl.uniprot.org/annotation/VAR_056193|||http://purl.uniprot.org/annotation/VAR_056194|||http://purl.uniprot.org/annotation/VAR_056195|||http://purl.uniprot.org/annotation/VAR_056196|||http://purl.uniprot.org/annotation/VAR_056197|||http://purl.uniprot.org/annotation/VAR_056198|||http://purl.uniprot.org/annotation/VAR_056199|||http://purl.uniprot.org/annotation/VAR_056200|||http://purl.uniprot.org/annotation/VAR_056201|||http://purl.uniprot.org/annotation/VAR_056202|||http://purl.uniprot.org/annotation/VSP_007764|||http://purl.uniprot.org/annotation/VSP_007765|||http://purl.uniprot.org/annotation/VSP_059434
http://togogenome.org/gene/9606:CDC37L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L3B6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Hsp90 co-chaperone Cdc37-like 1|||Interaction with Hsp70|||Phosphoserine|||Required for interaction with STIP1|||Self-association|||Self-association and interaction with Hsp90                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318521|||http://purl.uniprot.org/annotation/VAR_038755
http://togogenome.org/gene/9606:SAYSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPB0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||SAYSvFN domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089517|||http://purl.uniprot.org/annotation/VSP_014597|||http://purl.uniprot.org/annotation/VSP_014598
http://togogenome.org/gene/9606:GLTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZD2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  1|||18% decrease in activity.|||2|||2 X 12 AA approximate tandem repeats|||46% decrease in activity.|||About 25% decrease in activity.|||About 50% decrease in activity.|||Almost complete inactivation; 1-3% residual activity.|||Almost complete inactivation; 1-3% residual activity. No effect on autophagy.|||Glycolipid transfer protein|||N-acetylalanine|||No loss of activity; 90% residual activity.|||No loss of activity; 90-97% residual activity.|||Partial inactivation; 63% residual activity.|||Removed|||Significant inactivation; 15% residual activity.|||Significant inactivation; 5% residual acti vity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148915
http://togogenome.org/gene/9606:CACNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54284                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mediates interaction with the alpha subunit|||Phosphoserine|||Polar residues|||SH3|||Voltage-dependent L-type calcium channel subunit beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144056|||http://purl.uniprot.org/annotation/VAR_024384|||http://purl.uniprot.org/annotation/VSP_000634|||http://purl.uniprot.org/annotation/VSP_046708|||http://purl.uniprot.org/annotation/VSP_046709|||http://purl.uniprot.org/annotation/VSP_046710
http://togogenome.org/gene/9606:PRR18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4B5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Proline-rich protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307747|||http://purl.uniprot.org/annotation/VAR_036642
http://togogenome.org/gene/9606:BPY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14599                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Testis-specific basic protein Y 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184664
http://togogenome.org/gene/9606:HSPA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5I0|||http://purl.uniprot.org/uniprot/P0DMV8|||http://purl.uniprot.org/uniprot/P0DMV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of in vitro methylation by METTL21A.|||Disordered|||Heat shock 70 kDa protein 1A|||Heat shock 70 kDa protein 1B|||In isoform 2.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by METTL21A; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||No loss of acetylation and ATPase activity. Exhibits normal protein refolding activity during the early phase but exhibits defects in ubiquitin-mediated protein degradation during the later phase.|||Nucleotide-binding domain (NBD)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Reduces affinity for ADP.|||Removed|||Significant loss of acetylation and ATPase activity. Decreased binding to HOPX and HSP90 and increased binding to STUB1 and NAA10. Impaired capacity for protein refolding during the early phase after stress but shows normal protein degradation activity in the late phase.|||Substrate-binding domain (SBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078249|||http://purl.uniprot.org/annotation/PRO_0000433115|||http://purl.uniprot.org/annotation/VAR_029053|||http://purl.uniprot.org/annotation/VAR_029054|||http://purl.uniprot.org/annotation/VAR_032152|||http://purl.uniprot.org/annotation/VAR_032153|||http://purl.uniprot.org/annotation/VSP_044427
http://togogenome.org/gene/9606:AATF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylalanine|||POLR2J binding|||Phosphoserine|||Polar residues|||Protein AATF|||RB1 and SP1 binding|||RB1 binding|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056616
http://togogenome.org/gene/9606:BSDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BSD|||BSD domain-containing protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 7.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282639|||http://purl.uniprot.org/annotation/VSP_024216|||http://purl.uniprot.org/annotation/VSP_024217|||http://purl.uniprot.org/annotation/VSP_024218|||http://purl.uniprot.org/annotation/VSP_024219|||http://purl.uniprot.org/annotation/VSP_024220|||http://purl.uniprot.org/annotation/VSP_024221|||http://purl.uniprot.org/annotation/VSP_024222|||http://purl.uniprot.org/annotation/VSP_024223|||http://purl.uniprot.org/annotation/VSP_024224|||http://purl.uniprot.org/annotation/VSP_041672|||http://purl.uniprot.org/annotation/VSP_041673
http://togogenome.org/gene/9606:DPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DPH-type MB|||Diphthamide biosynthesis protein 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082620|||http://purl.uniprot.org/annotation/VSP_012411
http://togogenome.org/gene/9606:FNDC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type III domain-containing protein 5|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Irisin|||Microbody targeting signal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328971|||http://purl.uniprot.org/annotation/PRO_0000415857|||http://purl.uniprot.org/annotation/VSP_032860|||http://purl.uniprot.org/annotation/VSP_032861|||http://purl.uniprot.org/annotation/VSP_032862|||http://purl.uniprot.org/annotation/VSP_032863
http://togogenome.org/gene/9606:PPM1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY54                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||11 X 2 AA tandem repeats of P-E|||2|||3|||4|||5|||6|||7|||8; approximate|||9|||Acidic residues|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||PPM-type phosphatase|||Phosphoserine|||Pro residues|||Protein phosphatase 1E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286820|||http://purl.uniprot.org/annotation/VAR_036518|||http://purl.uniprot.org/annotation/VAR_036519|||http://purl.uniprot.org/annotation/VAR_063769|||http://purl.uniprot.org/annotation/VSP_025198
http://togogenome.org/gene/9606:BCL7C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUZ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  B-cell CLL/lymphoma 7 protein family member C|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239833|||http://purl.uniprot.org/annotation/VSP_019282
http://togogenome.org/gene/9606:SLC9B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z488|||http://purl.uniprot.org/uniprot/B7Z676|||http://purl.uniprot.org/uniprot/E9PE63|||http://purl.uniprot.org/uniprot/Q86UD5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes Na(+) Li(+)/H(+) antiporter activity. Changes subcellular localization. Retained in the ER.|||Abolishes Na(+) Li(+)/H(+) antiporter activity. Does not affect plasma membrane localization.|||Abolishes Na(+) Li(+)/H(+) antiporter activity. Shifts the specificity from Na(+) to Li(+); when associated with R-215. Decreases plasma membrane localization; when associated with R-215. Partially retained in the ER; when associated with R-215.|||Abolishes Na(+) Li(+)/H(+) antiporter activity. Shifts the specificity of the transporter from Na(+) to Li(+); when associated with E-432. Decreases plasma membrane localization. Partially retained in the ER; when associated with E-432.|||Cation/H+ exchanger|||Cytoplasmic|||Decreases Na(+) Li(+)/H(+) antiporter activity.|||Decreases Na(+) Li(+)/H(+) antiporter activity; when associated with K-57.|||Decreases Na(+) Li(+)/H(+) antiporter activity; when associated with K-58.|||Disordered|||Does not affect Na(+) Li(+)/H(+) antiporter activity; when associated with A-58.|||Does not affect plasma membrane localization. Abolishes antiporter activity. Less sensitive to phloretin inhibition.|||Does not affect plasma membrane localization. Change in the substrate specificity with a preference for Li(+) over Na(+).|||Does not affect plasma membrane localization. Decreases Na(+) Li(+)/H(+) antiporter activity.|||Does not affect plasma membrane localization. Decreases the substrate specificity for Li(+).|||Does not affect plasma membrane localization. Less sensitive to phloretin inhibition.|||Does not affect tNa(+) Li(+)/H(+) antiporter activity; when associated with A-57.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Loss of ion transport activity.|||Loss of ion transport activity; Does not rescue insulin secretion defect induced by knockdown of SLC9B2 in Min6 cells.|||Phosphoserine|||Polar residues|||Sodium/hydrogen exchanger 9B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331270|||http://purl.uniprot.org/annotation/VAR_042751|||http://purl.uniprot.org/annotation/VAR_042752|||http://purl.uniprot.org/annotation/VAR_042753|||http://purl.uniprot.org/annotation/VSP_033152|||http://purl.uniprot.org/annotation/VSP_033153
http://togogenome.org/gene/9606:KLHL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH77                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by PKC, promoting ubiquitination and degradation of WNK4.|||BACK|||BTB|||Found in a patient with hypertension; unknown pathological significance.|||In PHA2D.|||In PHA2D; abolished interaction with WNK1.|||In PHA2D; decreased interaction with WNK4.|||In PHA2D; does not affect interaction with WNK1 or CUL3.|||In PHA2D; dominant negative effect due to homodimer formation; impaired interaction with WNK1 and WNK4 and impaired ubiquitination of WNK4.|||In PHA2D; impaired interaction with CUL3.|||In PHA2D; impaired interaction with CUL3; de novo mutation.|||In PHA2D; impaired interaction with WNK1.|||In PHA2D; increased level of WNK4, leading to increased NaCl reabsorption.|||In isoform B.|||In isoform C.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 3|||Mimics phosphorylation, preventing binding and degradation of WNK4.|||Phosphoserine|||Phosphoserine; by PKA and PKC|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119103|||http://purl.uniprot.org/annotation/VAR_067501|||http://purl.uniprot.org/annotation/VAR_067502|||http://purl.uniprot.org/annotation/VAR_067503|||http://purl.uniprot.org/annotation/VAR_067504|||http://purl.uniprot.org/annotation/VAR_067505|||http://purl.uniprot.org/annotation/VAR_067506|||http://purl.uniprot.org/annotation/VAR_067507|||http://purl.uniprot.org/annotation/VAR_067508|||http://purl.uniprot.org/annotation/VAR_067509|||http://purl.uniprot.org/annotation/VAR_067510|||http://purl.uniprot.org/annotation/VAR_067511|||http://purl.uniprot.org/annotation/VAR_067512|||http://purl.uniprot.org/annotation/VAR_067513|||http://purl.uniprot.org/annotation/VAR_067514|||http://purl.uniprot.org/annotation/VAR_067515|||http://purl.uniprot.org/annotation/VAR_067516|||http://purl.uniprot.org/annotation/VAR_067517|||http://purl.uniprot.org/annotation/VAR_067518|||http://purl.uniprot.org/annotation/VAR_067519|||http://purl.uniprot.org/annotation/VAR_067520|||http://purl.uniprot.org/annotation/VAR_067521|||http://purl.uniprot.org/annotation/VAR_067522|||http://purl.uniprot.org/annotation/VAR_067523|||http://purl.uniprot.org/annotation/VAR_067524|||http://purl.uniprot.org/annotation/VAR_067525|||http://purl.uniprot.org/annotation/VAR_067526|||http://purl.uniprot.org/annotation/VAR_067527|||http://purl.uniprot.org/annotation/VAR_067528|||http://purl.uniprot.org/annotation/VAR_067529|||http://purl.uniprot.org/annotation/VAR_067530|||http://purl.uniprot.org/annotation/VAR_067531|||http://purl.uniprot.org/annotation/VAR_079630|||http://purl.uniprot.org/annotation/VAR_079631|||http://purl.uniprot.org/annotation/VAR_088176|||http://purl.uniprot.org/annotation/VAR_088177|||http://purl.uniprot.org/annotation/VAR_088178|||http://purl.uniprot.org/annotation/VSP_002816|||http://purl.uniprot.org/annotation/VSP_002817
http://togogenome.org/gene/9606:POLH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KN75|||http://purl.uniprot.org/uniprot/Q9Y253                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity.|||DNA polymerase eta|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In XPV.|||In XPV; impairs translesion synthesis.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased DNA polymerase activity and translesion bypass compared to wild-type.|||PIP-box|||Polar residues|||Reduces DNA polymerase activity.|||Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass.|||Reduces binding to chromatin and to monoubiquitinated PCNA. Abolishes binding to monoubiquitinated PCNA; when associated with 705-E--H-713 Del.|||Reduces cell resistance to UV-induced DNA damage.|||Reduces cell resistance to UV-induced DNA damage. Reduces binding to chromatin and to monoubiquitinated PCNA. Abolishes binding to monoubiquitinated PCNA; when associated with 324-A--A-326.|||Reduces enzymatic activity by two-thirds.|||Severe reduction in thymine dimer translesion bypass.|||UBZ3-type|||UmuC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173986|||http://purl.uniprot.org/annotation/VAR_021226|||http://purl.uniprot.org/annotation/VAR_021227|||http://purl.uniprot.org/annotation/VAR_021228|||http://purl.uniprot.org/annotation/VAR_021229|||http://purl.uniprot.org/annotation/VAR_021230|||http://purl.uniprot.org/annotation/VAR_021231|||http://purl.uniprot.org/annotation/VAR_021232|||http://purl.uniprot.org/annotation/VAR_021233|||http://purl.uniprot.org/annotation/VAR_021234|||http://purl.uniprot.org/annotation/VAR_021235|||http://purl.uniprot.org/annotation/VAR_021236|||http://purl.uniprot.org/annotation/VAR_021237|||http://purl.uniprot.org/annotation/VAR_021238|||http://purl.uniprot.org/annotation/VAR_036220|||http://purl.uniprot.org/annotation/VAR_070835|||http://purl.uniprot.org/annotation/VAR_070836|||http://purl.uniprot.org/annotation/VAR_070837|||http://purl.uniprot.org/annotation/VAR_070838|||http://purl.uniprot.org/annotation/VAR_070839|||http://purl.uniprot.org/annotation/VSP_012799
http://togogenome.org/gene/9606:TMSB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63313                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Thymosin beta-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045931|||http://purl.uniprot.org/annotation/VAR_052304
http://togogenome.org/gene/9606:ETFBKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXQ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Transit Peptide                                                                                  ^@                                                                                  Electron transfer flavoprotein beta subunit lysine methyltransferase|||Loss of lysine methyltransferase activity.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318709
http://togogenome.org/gene/9606:ZNF676                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7Q3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 676                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233996|||http://purl.uniprot.org/annotation/VAR_047437|||http://purl.uniprot.org/annotation/VAR_047438|||http://purl.uniprot.org/annotation/VAR_047439
http://togogenome.org/gene/9606:ZNF98                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 98                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316948
http://togogenome.org/gene/9606:CCDC90B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 90B, mitochondrial|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295695|||http://purl.uniprot.org/annotation/VAR_033322|||http://purl.uniprot.org/annotation/VSP_027003|||http://purl.uniprot.org/annotation/VSP_055663
http://togogenome.org/gene/9606:TIA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31483                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytotoxic granule associated RNA binding protein TIA1|||Disordered|||In ALS26; accelerated formation of TIA1 amyloid-like fibrils; impaired stress granule disassembly; accumulation of insoluble TARDBP/TDP43-positive stress granules.|||In ALS26; unknown pathological significance.|||In WDM; results in a mild increase of stress granule numbers compared to controls; impaired stress granule disassembly.|||In isoform 3.|||In isoform Short.|||N-acetylmethionine|||Polar residues|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031031|||http://purl.uniprot.org/annotation/VAR_069897|||http://purl.uniprot.org/annotation/VAR_085357|||http://purl.uniprot.org/annotation/VAR_085358|||http://purl.uniprot.org/annotation/VAR_085359|||http://purl.uniprot.org/annotation/VAR_085360|||http://purl.uniprot.org/annotation/VAR_085361|||http://purl.uniprot.org/annotation/VAR_085362|||http://purl.uniprot.org/annotation/VSP_005892|||http://purl.uniprot.org/annotation/VSP_057403|||http://purl.uniprot.org/annotation/VSP_057404
http://togogenome.org/gene/9606:DUOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRD9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dual oxidase 1|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||In isoform 2.|||Interaction with TXNDC11|||N-linked (GlcNAc...) asparagine|||Peroxidase-like; mediates peroxidase activity|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223344|||http://purl.uniprot.org/annotation/VAR_025321|||http://purl.uniprot.org/annotation/VAR_025322|||http://purl.uniprot.org/annotation/VAR_049104|||http://purl.uniprot.org/annotation/VSP_017262|||http://purl.uniprot.org/annotation/VSP_017263
http://togogenome.org/gene/9606:PCYT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSC8|||http://purl.uniprot.org/uniprot/B7Z4W6|||http://purl.uniprot.org/uniprot/I3L1R7|||http://purl.uniprot.org/uniprot/Q99447                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cytidyltransferase-like|||Disordered|||Ethanolamine-phosphate cytidylyltransferase|||In SPG82; decreased protein abundance; loss of ethanolamine-phosphate cytidylyltransferase activity.|||In SPG82; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208461|||http://purl.uniprot.org/annotation/VAR_083888|||http://purl.uniprot.org/annotation/VAR_083889|||http://purl.uniprot.org/annotation/VAR_083890|||http://purl.uniprot.org/annotation/VSP_045131|||http://purl.uniprot.org/annotation/VSP_046844|||http://purl.uniprot.org/annotation/VSP_054615
http://togogenome.org/gene/9606:LY6H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94772                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||In isoform 2.|||Lymphocyte antigen 6H|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036148|||http://purl.uniprot.org/annotation/PRO_0000036149|||http://purl.uniprot.org/annotation/VSP_053497
http://togogenome.org/gene/9606:STX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75558                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Syntaxin-11|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210221|||http://purl.uniprot.org/annotation/VAR_011995|||http://purl.uniprot.org/annotation/VAR_011996|||http://purl.uniprot.org/annotation/VAR_029769|||http://purl.uniprot.org/annotation/VAR_029770
http://togogenome.org/gene/9606:LRRC70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2Q7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 70|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317750
http://togogenome.org/gene/9606:NPAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14207                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP.|||Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18.|||Impairs activation of histone gene transcription; when associated with A-27.|||Impairs activation of histone gene transcription; when associated with A-30.|||Impairs activation of histone gene transcription; when associated with A-775; A-1100; A-1270 and A-1350.|||Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1270.|||Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1350.|||Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1270 and A-1350.|||Impairs activation of histone gene transcription; when associated with A-779; A-1100; A-1270 and A-1350.|||Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15.|||Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18.|||Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18.|||Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18.|||Interaction with MIZF|||LisH|||Mediates transcriptional activation|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine; by CDK2|||Polar residues|||Protein NPAT|||Required for acceleration of G1 phase|||Required for activation of histone gene transcription and interaction with MIZF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318163|||http://purl.uniprot.org/annotation/VAR_038696|||http://purl.uniprot.org/annotation/VAR_038697|||http://purl.uniprot.org/annotation/VAR_038698|||http://purl.uniprot.org/annotation/VAR_038699|||http://purl.uniprot.org/annotation/VAR_038700|||http://purl.uniprot.org/annotation/VAR_038701|||http://purl.uniprot.org/annotation/VAR_038702|||http://purl.uniprot.org/annotation/VAR_038703|||http://purl.uniprot.org/annotation/VAR_038704|||http://purl.uniprot.org/annotation/VAR_038705|||http://purl.uniprot.org/annotation/VAR_038706|||http://purl.uniprot.org/annotation/VAR_038707|||http://purl.uniprot.org/annotation/VAR_038708
http://togogenome.org/gene/9606:LCE3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 3D|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235336|||http://purl.uniprot.org/annotation/VAR_053485|||http://purl.uniprot.org/annotation/VAR_062120
http://togogenome.org/gene/9606:BTBD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P203                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB 1|||BTB 2|||BTB/POZ domain-containing protein 7|||Basic and acidic residues|||Disordered|||In isoform 3.|||In isoform 5.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186215|||http://purl.uniprot.org/annotation/VSP_041481|||http://purl.uniprot.org/annotation/VSP_041482|||http://purl.uniprot.org/annotation/VSP_041483|||http://purl.uniprot.org/annotation/VSP_041487
http://togogenome.org/gene/9606:CNTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P232                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Contactin-3|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated serine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014705|||http://purl.uniprot.org/annotation/PRO_0000014706|||http://purl.uniprot.org/annotation/VAR_019906|||http://purl.uniprot.org/annotation/VAR_056042
http://togogenome.org/gene/9606:ALDH7A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49419                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Alpha-aminoadipic semialdehyde dehydrogenase|||In PDE.|||In PDE; loss of alpha-AASA dehydrogenase activity.|||In isoform 2.|||In isoform 4.|||Mitochondrion|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleophile|||Proton acceptor|||Removed|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056490|||http://purl.uniprot.org/annotation/VAR_028202|||http://purl.uniprot.org/annotation/VAR_028203|||http://purl.uniprot.org/annotation/VAR_031718|||http://purl.uniprot.org/annotation/VAR_031719|||http://purl.uniprot.org/annotation/VAR_069184|||http://purl.uniprot.org/annotation/VAR_069185|||http://purl.uniprot.org/annotation/VAR_069186|||http://purl.uniprot.org/annotation/VAR_069187|||http://purl.uniprot.org/annotation/VAR_069188|||http://purl.uniprot.org/annotation/VAR_069189|||http://purl.uniprot.org/annotation/VAR_085776|||http://purl.uniprot.org/annotation/VSP_038987|||http://purl.uniprot.org/annotation/VSP_045905
http://togogenome.org/gene/9606:ZCCHC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PEW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150971|||http://purl.uniprot.org/annotation/VAR_045908|||http://purl.uniprot.org/annotation/VAR_045909|||http://purl.uniprot.org/annotation/VAR_045910|||http://purl.uniprot.org/annotation/VAR_075208
http://togogenome.org/gene/9606:MUC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KY81|||http://purl.uniprot.org/uniprot/Q8WXI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||12 X approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mucin-16|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEA|||SEA 1|||SEA 10|||SEA 11|||SEA 12|||SEA 13|||SEA 14|||SEA 15|||SEA 16|||SEA 2|||SEA 3|||SEA 4|||SEA 5|||SEA 6|||SEA 7|||SEA 8|||SEA 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000436078|||http://purl.uniprot.org/annotation/VAR_056592|||http://purl.uniprot.org/annotation/VAR_056593|||http://purl.uniprot.org/annotation/VAR_056594|||http://purl.uniprot.org/annotation/VAR_056595|||http://purl.uniprot.org/annotation/VAR_056596|||http://purl.uniprot.org/annotation/VAR_056597|||http://purl.uniprot.org/annotation/VAR_056598|||http://purl.uniprot.org/annotation/VAR_056599|||http://purl.uniprot.org/annotation/VAR_056600|||http://purl.uniprot.org/annotation/VAR_056601|||http://purl.uniprot.org/annotation/VAR_056602|||http://purl.uniprot.org/annotation/VAR_056603|||http://purl.uniprot.org/annotation/VAR_056604|||http://purl.uniprot.org/annotation/VAR_056605|||http://purl.uniprot.org/annotation/VAR_056606|||http://purl.uniprot.org/annotation/VAR_056607|||http://purl.uniprot.org/annotation/VAR_056608|||http://purl.uniprot.org/annotation/VAR_056609|||http://purl.uniprot.org/annotation/VAR_056610|||http://purl.uniprot.org/annotation/VAR_056611|||http://purl.uniprot.org/annotation/VAR_056612|||http://purl.uniprot.org/annotation/VAR_056613|||http://purl.uniprot.org/annotation/VAR_056614|||http://purl.uniprot.org/annotation/VAR_056615|||http://purl.uniprot.org/annotation/VAR_056616
http://togogenome.org/gene/9606:HNF4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9VVT8|||http://purl.uniprot.org/uniprot/F1D8S2|||http://purl.uniprot.org/uniprot/F1D8T0|||http://purl.uniprot.org/uniprot/F1D8T1|||http://purl.uniprot.org/uniprot/P41235                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Abolishes AMPK-mediated phosphorylation.|||Disordered|||Found in a patient with non-insulin-dependent diabetes mellitus; does not affect activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hepatocyte nuclear factor 4-alpha|||In FRTS4.|||In MODY1.|||In MODY1; results in loss of function.|||In T2D; reduced transactivation activity.|||In isoform HNF4-Alpha-2 and isoform HNF4-Alpha-8.|||In isoform HNF4-Alpha-3 and isoform HNF4-Alpha-9.|||In isoform HNF4-Alpha-4.|||In isoform HNF4-Alpha-7, isoform HNF4-Alpha-8 and isoform HNF4-Alpha-9.|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphomimetic mutant that leads to reduced ability to bind DNA.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053558|||http://purl.uniprot.org/annotation/VAR_004668|||http://purl.uniprot.org/annotation/VAR_004669|||http://purl.uniprot.org/annotation/VAR_004670|||http://purl.uniprot.org/annotation/VAR_010600|||http://purl.uniprot.org/annotation/VAR_010601|||http://purl.uniprot.org/annotation/VAR_011785|||http://purl.uniprot.org/annotation/VAR_062267|||http://purl.uniprot.org/annotation/VAR_071951|||http://purl.uniprot.org/annotation/VAR_071952|||http://purl.uniprot.org/annotation/VSP_003673|||http://purl.uniprot.org/annotation/VSP_003674|||http://purl.uniprot.org/annotation/VSP_003675|||http://purl.uniprot.org/annotation/VSP_026030
http://togogenome.org/gene/9606:RUNX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEN7|||http://purl.uniprot.org/uniprot/Q13950|||http://purl.uniprot.org/uniprot/Q32MY8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CLCD1.|||In CLCD1; abolishes DNA binding.|||In CLCD1; decreased protein stability; decreased transactivation activity; decreased osteoblast differentiation.|||In CLCD1; decreased subcellular localization in the nucleus; decreased transactivation activity.|||In CLCD1; has severely impaired DNA binding and transactivation.|||In CLCD1; interferes with nuclear localization; abolishes DNA binding.|||In CLCD1; interferes with nuclear localization; has severely impaired DNA binding and transactivation.|||In CLCD1; mild; associated also with isolated dental anomalies; normal DNA binding.|||In CLCD1; retains heterodimerization activity together with a trace potential for DNA binding; retains a low but still substantial transactivation activity.|||In CLCD1; the patient also shows brachydactyly of hands and feet.|||In CLCD1; unchanged subcellular localization; decreased transactivation activity.|||In isoform 2.|||In isoform 3.|||Interaction with KAT6A|||Interaction with KAT6B|||Phosphoserine|||Phosphoserine; by CDK1|||Polar residues|||Pro residues|||Reduced DNA-binding and impaired phosphorylation.|||Required for interaction with FOXO1|||Runt|||Runt-related transcription factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174659|||http://purl.uniprot.org/annotation/VAR_012130|||http://purl.uniprot.org/annotation/VAR_012131|||http://purl.uniprot.org/annotation/VAR_012132|||http://purl.uniprot.org/annotation/VAR_012133|||http://purl.uniprot.org/annotation/VAR_012134|||http://purl.uniprot.org/annotation/VAR_012135|||http://purl.uniprot.org/annotation/VAR_012136|||http://purl.uniprot.org/annotation/VAR_012137|||http://purl.uniprot.org/annotation/VAR_012138|||http://purl.uniprot.org/annotation/VAR_012139|||http://purl.uniprot.org/annotation/VAR_012140|||http://purl.uniprot.org/annotation/VAR_012141|||http://purl.uniprot.org/annotation/VAR_012142|||http://purl.uniprot.org/annotation/VAR_012143|||http://purl.uniprot.org/annotation/VAR_012144|||http://purl.uniprot.org/annotation/VAR_012145|||http://purl.uniprot.org/annotation/VAR_012146|||http://purl.uniprot.org/annotation/VAR_012147|||http://purl.uniprot.org/annotation/VAR_012148|||http://purl.uniprot.org/annotation/VAR_012149|||http://purl.uniprot.org/annotation/VAR_012150|||http://purl.uniprot.org/annotation/VAR_064081|||http://purl.uniprot.org/annotation/VAR_064082|||http://purl.uniprot.org/annotation/VAR_064083|||http://purl.uniprot.org/annotation/VAR_064084|||http://purl.uniprot.org/annotation/VAR_064085|||http://purl.uniprot.org/annotation/VAR_064086|||http://purl.uniprot.org/annotation/VAR_064087|||http://purl.uniprot.org/annotation/VAR_064088|||http://purl.uniprot.org/annotation/VAR_064089|||http://purl.uniprot.org/annotation/VAR_064090|||http://purl.uniprot.org/annotation/VAR_064091|||http://purl.uniprot.org/annotation/VAR_064092|||http://purl.uniprot.org/annotation/VAR_064093|||http://purl.uniprot.org/annotation/VAR_064094|||http://purl.uniprot.org/annotation/VAR_064095|||http://purl.uniprot.org/annotation/VAR_064096|||http://purl.uniprot.org/annotation/VAR_064097|||http://purl.uniprot.org/annotation/VAR_064098|||http://purl.uniprot.org/annotation/VAR_064099|||http://purl.uniprot.org/annotation/VAR_064100|||http://purl.uniprot.org/annotation/VAR_064101|||http://purl.uniprot.org/annotation/VAR_064102|||http://purl.uniprot.org/annotation/VAR_064103|||http://purl.uniprot.org/annotation/VAR_064104|||http://purl.uniprot.org/annotation/VAR_064105|||http://purl.uniprot.org/annotation/VAR_064106|||http://purl.uniprot.org/annotation/VAR_064107|||http://purl.uniprot.org/annotation/VAR_064108|||http://purl.uniprot.org/annotation/VAR_079576|||http://purl.uniprot.org/annotation/VAR_079577|||http://purl.uniprot.org/annotation/VAR_079578|||http://purl.uniprot.org/annotation/VAR_079579|||http://purl.uniprot.org/annotation/VAR_079580|||http://purl.uniprot.org/annotation/VSP_005937|||http://purl.uniprot.org/annotation/VSP_005938
http://togogenome.org/gene/9606:DDX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13206                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable ATP-dependent RNA helicase DDX10|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055083|||http://purl.uniprot.org/annotation/VAR_035840
http://togogenome.org/gene/9606:UNC13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14795|||http://purl.uniprot.org/uniprot/Q4LE73                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 2|||C2 3|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||MHD1|||MHD2|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188575|||http://purl.uniprot.org/annotation/VAR_036615|||http://purl.uniprot.org/annotation/VAR_037273|||http://purl.uniprot.org/annotation/VAR_037274|||http://purl.uniprot.org/annotation/VSP_057319
http://togogenome.org/gene/9606:SLC34A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N130                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Name=M3|||Helical; Name=M4|||Helical; Name=M5|||Helical; Name=M6|||Helical; Name=M7|||Helical; Name=M8|||In HHRH.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent phosphate transport protein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068617|||http://purl.uniprot.org/annotation/VAR_025706|||http://purl.uniprot.org/annotation/VAR_025707|||http://purl.uniprot.org/annotation/VAR_025708|||http://purl.uniprot.org/annotation/VAR_025709|||http://purl.uniprot.org/annotation/VAR_025710|||http://purl.uniprot.org/annotation/VAR_025711|||http://purl.uniprot.org/annotation/VAR_025712|||http://purl.uniprot.org/annotation/VAR_025713|||http://purl.uniprot.org/annotation/VAR_025714|||http://purl.uniprot.org/annotation/VAR_025715|||http://purl.uniprot.org/annotation/VAR_025716
http://togogenome.org/gene/9606:WDR37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2I8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In NOCGUS.|||In NOCGUS; loss of interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm.|||In NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization.|||In NOCGUS; no effect on interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm.|||In NOCGUS; unknown pathological significance; no effect on interaction with PACS1 and PACS2; does not affect homodimerization; does not affect subcellular location to cytoplasm.|||In isoform 2.|||In isoform 3.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051387|||http://purl.uniprot.org/annotation/VAR_025432|||http://purl.uniprot.org/annotation/VAR_070805|||http://purl.uniprot.org/annotation/VAR_070806|||http://purl.uniprot.org/annotation/VAR_083347|||http://purl.uniprot.org/annotation/VAR_083348|||http://purl.uniprot.org/annotation/VAR_083349|||http://purl.uniprot.org/annotation/VAR_083350|||http://purl.uniprot.org/annotation/VAR_087686|||http://purl.uniprot.org/annotation/VAR_087687|||http://purl.uniprot.org/annotation/VAR_087688|||http://purl.uniprot.org/annotation/VAR_087689|||http://purl.uniprot.org/annotation/VAR_087690|||http://purl.uniprot.org/annotation/VSP_054011|||http://purl.uniprot.org/annotation/VSP_054012|||http://purl.uniprot.org/annotation/VSP_054013
http://togogenome.org/gene/9606:C1QL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0IND4|||http://purl.uniprot.org/uniprot/Q7Z5L3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Collagen-like|||Complement C1q-like protein 2|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274335|||http://purl.uniprot.org/annotation/PRO_5035403041
http://togogenome.org/gene/9606:PLXDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Plexin domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234574|||http://purl.uniprot.org/annotation/VAR_026292|||http://purl.uniprot.org/annotation/VAR_026293|||http://purl.uniprot.org/annotation/VSP_018377|||http://purl.uniprot.org/annotation/VSP_018378
http://togogenome.org/gene/9606:ENTPD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V4I0|||http://purl.uniprot.org/uniprot/O75356                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||No effect on protein stability. No effect on nucleoside-diphosphatase activity.|||Nucleoside diphosphate phosphatase ENTPD5|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019908|||http://purl.uniprot.org/annotation/PRO_5015091598|||http://purl.uniprot.org/annotation/VAR_050308
http://togogenome.org/gene/9606:THAP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EK4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Motif|||Region|||Sequence Conflict|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||HCFC1-binding motif (HBM)|||THAP domain-containing protein 11|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068653
http://togogenome.org/gene/9606:PSTPIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5P3|||http://purl.uniprot.org/uniprot/O43586                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to MEFV. Cytoplasmic filaments are finer with fewer branches.|||Decreases binding to MEFV.|||F-BAR|||In PAPAS.|||In PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; increased induction of MEFV in response to retroviral infection.|||In PAPAS; severely reduced binding with PTPN12; markedly increased binding to MEFV; accentuates IL1B secretion; no effect on filament formation; increased induction of MEFV in response to retroviral infection.|||In isoform 2.|||No effect on filament formation.|||Phosphoserine|||Phosphotyrosine|||Proline-serine-threonine phosphatase-interacting protein 1|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058539|||http://purl.uniprot.org/annotation/VAR_023515|||http://purl.uniprot.org/annotation/VAR_023516|||http://purl.uniprot.org/annotation/VAR_023517|||http://purl.uniprot.org/annotation/VAR_023518|||http://purl.uniprot.org/annotation/VAR_023519|||http://purl.uniprot.org/annotation/VAR_023520|||http://purl.uniprot.org/annotation/VAR_023521|||http://purl.uniprot.org/annotation/VAR_023522|||http://purl.uniprot.org/annotation/VAR_023523|||http://purl.uniprot.org/annotation/VAR_070635|||http://purl.uniprot.org/annotation/VSP_015627
http://togogenome.org/gene/9606:TMEM31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK58|||http://purl.uniprot.org/uniprot/Q5JXX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Transmembrane protein 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284800
http://togogenome.org/gene/9606:NDUFA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y39                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylalanine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118841|||http://purl.uniprot.org/annotation/VSP_033813
http://togogenome.org/gene/9606:ZNF732                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXR9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; degenerate|||C2H2-type 16; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 732                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000382922
http://togogenome.org/gene/9606:CCDC107                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV48                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 107|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282407|||http://purl.uniprot.org/annotation/VAR_031406|||http://purl.uniprot.org/annotation/VAR_031407|||http://purl.uniprot.org/annotation/VAR_031408|||http://purl.uniprot.org/annotation/VSP_024128|||http://purl.uniprot.org/annotation/VSP_024129|||http://purl.uniprot.org/annotation/VSP_024130|||http://purl.uniprot.org/annotation/VSP_024131|||http://purl.uniprot.org/annotation/VSP_024132|||http://purl.uniprot.org/annotation/VSP_024133|||http://purl.uniprot.org/annotation/VSP_042165
http://togogenome.org/gene/9606:TBC1D22A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRY0|||http://purl.uniprot.org/uniprot/Q8WUA7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Complete loss of 14-3-3 protein-binding.|||Decreased 14-3-3 protein-binding.|||Decreased ACBD3-binding.|||Disordered|||Drastically decreased ACBD3-binding. No effect on binding to 14-3-3 protein.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||N-acetylalanine|||No effect on 14-3-3 protein-binding.|||No effect on ACBD3-binding.|||No effect on interaction with ACBD3, nor with 14-3-3 proteins.|||No effect on interaction with ACBD3. Decreased 14-3-3 protein-binding.|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||Removed|||TBC1 domain family member 22A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208051|||http://purl.uniprot.org/annotation/VSP_010382|||http://purl.uniprot.org/annotation/VSP_010383|||http://purl.uniprot.org/annotation/VSP_015142|||http://purl.uniprot.org/annotation/VSP_015143|||http://purl.uniprot.org/annotation/VSP_015144
http://togogenome.org/gene/9606:TECTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PL2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Beta-tectorin|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041741|||http://purl.uniprot.org/annotation/PRO_0000041742
http://togogenome.org/gene/9606:QPCTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXS2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Glutaminyl-peptide cyclotransferase-like protein|||Helical|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302002|||http://purl.uniprot.org/annotation/VAR_034937|||http://purl.uniprot.org/annotation/VSP_054066
http://togogenome.org/gene/9606:G2E3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL73|||http://purl.uniprot.org/uniprot/F5GX24|||http://purl.uniprot.org/uniprot/Q49AD9|||http://purl.uniprot.org/uniprot/Q7L622                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC pre-PHD-type|||G2/M phase-specific E3 ubiquitin-protein ligase|||Glycyl thioester intermediate|||HECT|||Loss of nucleolar localization. No effect on nuclear localization.|||No effect on subcellular location. Strong activity; when associated with A-84; A-258 and A261. Strong activity; when associated with A-84 and A-147. No activity; when associated with A-147; A-258 and A-261.|||PHD-type|||PHD-type 1|||PHD-type 2; degenerate|||PHD-type 3|||Strong activity; when associated with A-258; A-261 and A-666. Strong activity; when associated with A-147 and A-666. No activity; when associated with A-147; A-258 and A-261.|||Strong activity; when associated with A-84 and A-666. No activity; when associated with A-258; A-261 and A-666. No activity; when associated with A-84; A-258 and A-261.|||Strong activity; when associated with A-84; A-258 and A-666. No activity; when associated with A-84; A-147 and A-258. No activity; when associated with A-147; A-258 and A-666.|||Strong activity; when associated with A-84; A-261 and A-666. No activity; when associated with A-147; A-261 and A-666. No activity; when associated with A-84; A-147 and A-261.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248343|||http://purl.uniprot.org/annotation/VAR_027273
http://togogenome.org/gene/9606:CLDN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DX19|||http://purl.uniprot.org/uniprot/O00501                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144745
http://togogenome.org/gene/9606:TP53TG3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:KIR2DL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43626|||http://purl.uniprot.org/uniprot/Q6H2H2|||http://purl.uniprot.org/uniprot/Q6H2H3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with ARRB2; when associated with A-302.|||Abolishes interaction with ARRB2; when associated with A-332. Diminishes interaction with ARRB2.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Immunoglobulin subtype|||In isoform 2.|||Killer cell immunoglobulin-like receptor 2DL1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015078|||http://purl.uniprot.org/annotation/PRO_5014310459|||http://purl.uniprot.org/annotation/PRO_5015098284|||http://purl.uniprot.org/annotation/VAR_003949|||http://purl.uniprot.org/annotation/VAR_003950|||http://purl.uniprot.org/annotation/VAR_003951|||http://purl.uniprot.org/annotation/VAR_010331|||http://purl.uniprot.org/annotation/VAR_010332|||http://purl.uniprot.org/annotation/VAR_010333|||http://purl.uniprot.org/annotation/VAR_010334|||http://purl.uniprot.org/annotation/VAR_010335|||http://purl.uniprot.org/annotation/VAR_056091|||http://purl.uniprot.org/annotation/VAR_061332|||http://purl.uniprot.org/annotation/VAR_061333|||http://purl.uniprot.org/annotation/VSP_056314
http://togogenome.org/gene/9606:OR4M2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGB6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4M2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150562|||http://purl.uniprot.org/annotation/VAR_047831|||http://purl.uniprot.org/annotation/VAR_047832|||http://purl.uniprot.org/annotation/VAR_047833|||http://purl.uniprot.org/annotation/VAR_047834|||http://purl.uniprot.org/annotation/VAR_047835
http://togogenome.org/gene/9606:KY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBH2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 3.|||Kyphoscoliosis peptidase|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288604|||http://purl.uniprot.org/annotation/VSP_060754
http://togogenome.org/gene/9606:TPTEP2-CSNK1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRV2|||http://purl.uniprot.org/uniprot/P49674|||http://purl.uniprot.org/uniprot/Q5U045                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Casein kinase I isoform epsilon|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||Loss of kinase activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192837|||http://purl.uniprot.org/annotation/VAR_042082|||http://purl.uniprot.org/annotation/VAR_042083
http://togogenome.org/gene/9606:AHRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A9YTQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Aryl hydrocarbon receptor repressor|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Needed for transcriptional repression|||PAS|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333857|||http://purl.uniprot.org/annotation/VAR_043308|||http://purl.uniprot.org/annotation/VAR_043309|||http://purl.uniprot.org/annotation/VAR_043310|||http://purl.uniprot.org/annotation/VAR_043311|||http://purl.uniprot.org/annotation/VSP_033563|||http://purl.uniprot.org/annotation/VSP_033564
http://togogenome.org/gene/9606:SELPLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||12 X 10 AA tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-46. Binding L-lectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-51. Binding of L-selectin reduced by 91%; when associated with F-46; F-51 and A-57.|||Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-48. Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75%, and lymphocyte rolling reduced by 69%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-48 and F-51. Binding of L-selectin reduced by 91%; when associated with F-48; F-51 and A-57.|||Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75% and, lymphocyte rolling reduced by 69%; when associated with F-46. Binding L-selectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-48; Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-48. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and A-57.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In short form; not an alternative splicing.|||Interchain|||N-linked (GlcNAc...) asparagine|||No E- nor P-selectin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51.|||No dimer formation. No effect on P-selectin binding.|||No effect on L-selectin binding nor neutrophil rolling.|||No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding.|||O-linked (GalNAc...) threonine|||P-selectin glycoprotein ligand 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pyrrolidone carboxylic acid|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022302|||http://purl.uniprot.org/annotation/PRO_0000022303|||http://purl.uniprot.org/annotation/VAR_005611|||http://purl.uniprot.org/annotation/VAR_019156|||http://purl.uniprot.org/annotation/VAR_019157|||http://purl.uniprot.org/annotation/VAR_076761|||http://purl.uniprot.org/annotation/VSP_044827
http://togogenome.org/gene/9606:ASGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07307|||http://purl.uniprot.org/uniprot/Q7Z4G9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Asialoglycoprotein receptor 2|||C-type lectin|||Cytoplasmic|||Disordered|||Endocytosis signal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046654|||http://purl.uniprot.org/annotation/VAR_068747|||http://purl.uniprot.org/annotation/VSP_003060|||http://purl.uniprot.org/annotation/VSP_003061
http://togogenome.org/gene/9606:SLC5A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8N3|||http://purl.uniprot.org/uniprot/Q8WWX8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Reduces serum myo-inositol concentration.|||Sodium/myo-inositol cotransporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331568|||http://purl.uniprot.org/annotation/VAR_042896|||http://purl.uniprot.org/annotation/VAR_042897|||http://purl.uniprot.org/annotation/VAR_042898|||http://purl.uniprot.org/annotation/VAR_042899|||http://purl.uniprot.org/annotation/VAR_052494|||http://purl.uniprot.org/annotation/VAR_061877|||http://purl.uniprot.org/annotation/VSP_033259|||http://purl.uniprot.org/annotation/VSP_045034|||http://purl.uniprot.org/annotation/VSP_045035|||http://purl.uniprot.org/annotation/VSP_045036|||http://purl.uniprot.org/annotation/VSP_052789|||http://purl.uniprot.org/annotation/VSP_052790
http://togogenome.org/gene/9606:PCOLCE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKZ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CUB 1|||CUB 2|||N-linked (GlcNAc...) asparagine|||NTR|||Procollagen C-endopeptidase enhancer 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022020|||http://purl.uniprot.org/annotation/VAR_022448|||http://purl.uniprot.org/annotation/VAR_051264
http://togogenome.org/gene/9606:TBC1D32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NH3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Protein broad-minded|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089557|||http://purl.uniprot.org/annotation/VAR_046958|||http://purl.uniprot.org/annotation/VAR_046959|||http://purl.uniprot.org/annotation/VAR_046960|||http://purl.uniprot.org/annotation/VAR_046961|||http://purl.uniprot.org/annotation/VSP_014546|||http://purl.uniprot.org/annotation/VSP_035579|||http://purl.uniprot.org/annotation/VSP_035580
http://togogenome.org/gene/9606:HOXA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43364                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-A2|||In MHICP.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200036|||http://purl.uniprot.org/annotation/VAR_048023
http://togogenome.org/gene/9606:DNAI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWV9|||http://purl.uniprot.org/uniprot/A0A140VJI0|||http://purl.uniprot.org/uniprot/Q9UI46                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal intermediate chain 1|||In KTGS.|||In isoform 2.|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114658|||http://purl.uniprot.org/annotation/VAR_016774|||http://purl.uniprot.org/annotation/VAR_016775|||http://purl.uniprot.org/annotation/VAR_033876|||http://purl.uniprot.org/annotation/VAR_033877|||http://purl.uniprot.org/annotation/VAR_033878|||http://purl.uniprot.org/annotation/VAR_033879|||http://purl.uniprot.org/annotation/VSP_056963|||http://purl.uniprot.org/annotation/VSP_056964
http://togogenome.org/gene/9606:VSTM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW00                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptide Lv|||V-set and transmembrane domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274483|||http://purl.uniprot.org/annotation/PRO_0000431303|||http://purl.uniprot.org/annotation/VAR_030291|||http://purl.uniprot.org/annotation/VAR_035539|||http://purl.uniprot.org/annotation/VAR_065188|||http://purl.uniprot.org/annotation/VSP_022766|||http://purl.uniprot.org/annotation/VSP_022767
http://togogenome.org/gene/9606:ATXN7L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTQ8|||http://purl.uniprot.org/uniprot/Q9ULK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Ataxin-7-like protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||SCA7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064718|||http://purl.uniprot.org/annotation/VSP_032351|||http://purl.uniprot.org/annotation/VSP_032352|||http://purl.uniprot.org/annotation/VSP_041344|||http://purl.uniprot.org/annotation/VSP_041345
http://togogenome.org/gene/9606:FAM229A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BQW9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Protein FAM229A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421723
http://togogenome.org/gene/9606:CDH22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0L9|||http://purl.uniprot.org/uniprot/Q9UJ99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-22|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003821|||http://purl.uniprot.org/annotation/PRO_5002725395
http://togogenome.org/gene/9606:CELF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59G45|||http://purl.uniprot.org/uniprot/Q5SZQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  CUGBP Elav-like family member 3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295198|||http://purl.uniprot.org/annotation/VSP_026824|||http://purl.uniprot.org/annotation/VSP_026825|||http://purl.uniprot.org/annotation/VSP_046642
http://togogenome.org/gene/9606:KHNYN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6L5|||http://purl.uniprot.org/uniprot/O15037                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||Protein KHNYN|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084290|||http://purl.uniprot.org/annotation/VAR_030843|||http://purl.uniprot.org/annotation/VAR_030844
http://togogenome.org/gene/9606:FAM120A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TNY3|||http://purl.uniprot.org/uniprot/Q9NZB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Constitutive coactivator of PPAR-gamma-like protein 1|||Disordered|||In isoform B.|||In isoform D.|||In isoform E.|||In isoform F.|||Interaction with YES1, SRC and FYN|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221627|||http://purl.uniprot.org/annotation/VAR_054400|||http://purl.uniprot.org/annotation/VSP_004147|||http://purl.uniprot.org/annotation/VSP_004148|||http://purl.uniprot.org/annotation/VSP_017278|||http://purl.uniprot.org/annotation/VSP_017279|||http://purl.uniprot.org/annotation/VSP_017280|||http://purl.uniprot.org/annotation/VSP_036324
http://togogenome.org/gene/9606:PPP1R3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95685|||http://purl.uniprot.org/uniprot/Q86X09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  CBM21|||Disordered|||PP1-binding motif|||Phosphoserine|||Pro residues|||Protein phosphatase 1 regulatory subunit 3D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071503
http://togogenome.org/gene/9606:MEGF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75095                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 20|||EGF-like 21|||EGF-like 22|||EGF-like 23|||EGF-like 24|||EGF-like 25|||EGF-like 26|||EGF-like 27|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7|||EGF-like 8; calcium-binding|||EGF-like 9|||EMI|||In isoform 2.|||Multiple epidermal growth factor-like domains protein 6|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007524|||http://purl.uniprot.org/annotation/VAR_058361|||http://purl.uniprot.org/annotation/VAR_058362|||http://purl.uniprot.org/annotation/VAR_058363|||http://purl.uniprot.org/annotation/VAR_059258|||http://purl.uniprot.org/annotation/VAR_059259|||http://purl.uniprot.org/annotation/VAR_059260|||http://purl.uniprot.org/annotation/VAR_061155|||http://purl.uniprot.org/annotation/VAR_061156|||http://purl.uniprot.org/annotation/VAR_061157|||http://purl.uniprot.org/annotation/VSP_037740|||http://purl.uniprot.org/annotation/VSP_037741|||http://purl.uniprot.org/annotation/VSP_037742|||http://purl.uniprot.org/annotation/VSP_037743|||http://purl.uniprot.org/annotation/VSP_037744
http://togogenome.org/gene/9606:UGGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYU2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  2% active.|||4% active.|||41% active.|||7% active.|||Disordered|||Glucosyltransferase|||In isoform 2.|||Inactive.|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Prevents secretion from ER|||UDP-glucose:glycoprotein glucosyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012271|||http://purl.uniprot.org/annotation/VSP_036508
http://togogenome.org/gene/9606:RAD23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1J3|||http://purl.uniprot.org/uniprot/P54725                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with HIV-1 vpr.|||Abolishes interaction with PSMD4; when associated with A-9.|||Abolishes interaction with PSMD4; when associated with T-49.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HIV-1 vpr binding|||Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-10.|||Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-47.|||Impairs UBL-UBA domain interaction and enhances ubiquitin-binding; when associated with Glu-77.|||Impairs interaction with PSMD4.|||In isoform 2.|||In isoform 3.|||Increases interaction with PSMD1 and PSMC1.|||No effect on UBL-UBA domain interaction.|||No effect on interaction with EEF1A1.|||No effect on interaction with PSMD4.|||Phosphoserine|||Polar residues|||UBA|||UBA 1|||UBA 2|||UV excision repair protein RAD23 homolog A|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114904|||http://purl.uniprot.org/annotation/VAR_016251|||http://purl.uniprot.org/annotation/VAR_016252|||http://purl.uniprot.org/annotation/VAR_020377|||http://purl.uniprot.org/annotation/VSP_047565|||http://purl.uniprot.org/annotation/VSP_054694
http://togogenome.org/gene/9606:TTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33981                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dual specificity protein kinase TTK|||In isoform 2.|||Loss of kinase activity.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086774|||http://purl.uniprot.org/annotation/VAR_037141|||http://purl.uniprot.org/annotation/VAR_037142|||http://purl.uniprot.org/annotation/VSP_043072
http://togogenome.org/gene/9606:SEMA4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92854                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes PLXNB1 binding.|||Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with N-244.|||Abolishes homodimerization, abolishes collapse of growth cones and reduces PLXNB1 binding; when associated with S-246.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Sema|||Semaphorin-4D|||Strongly reduces PLXNB1 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032327|||http://purl.uniprot.org/annotation/VAR_030293|||http://purl.uniprot.org/annotation/VAR_057175|||http://purl.uniprot.org/annotation/VSP_039483|||http://purl.uniprot.org/annotation/VSP_039484
http://togogenome.org/gene/9606:FAM193A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78312                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||Protein FAM193A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089430|||http://purl.uniprot.org/annotation/VAR_022863|||http://purl.uniprot.org/annotation/VAR_056783|||http://purl.uniprot.org/annotation/VSP_014614|||http://purl.uniprot.org/annotation/VSP_014615|||http://purl.uniprot.org/annotation/VSP_014616|||http://purl.uniprot.org/annotation/VSP_014617|||http://purl.uniprot.org/annotation/VSP_045574|||http://purl.uniprot.org/annotation/VSP_045575|||http://purl.uniprot.org/annotation/VSP_047163
http://togogenome.org/gene/9606:CD68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34810                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||2 X 30 AA tandem repeats|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform Short and isoform 3.|||In isoform Short.|||Macrosialin|||Mucin-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017102|||http://purl.uniprot.org/annotation/VAR_016144|||http://purl.uniprot.org/annotation/VAR_016145|||http://purl.uniprot.org/annotation/VAR_049725|||http://purl.uniprot.org/annotation/VAR_049726|||http://purl.uniprot.org/annotation/VSP_003041|||http://purl.uniprot.org/annotation/VSP_003042
http://togogenome.org/gene/9606:GADD45GIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAE8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Motif|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein mL64|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228620
http://togogenome.org/gene/9606:RBM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52756                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type; atypical|||Disordered|||G-patch|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||RNA-binding protein 5|||RRM 1|||RRM 2|||RanBP2-type|||Required for interaction with U2AF2|||Sufficient for interaction with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and SNRNP200                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081759|||http://purl.uniprot.org/annotation/VAR_061831|||http://purl.uniprot.org/annotation/VSP_037429|||http://purl.uniprot.org/annotation/VSP_037430|||http://purl.uniprot.org/annotation/VSP_037431|||http://purl.uniprot.org/annotation/VSP_037432|||http://purl.uniprot.org/annotation/VSP_037433|||http://purl.uniprot.org/annotation/VSP_037434|||http://purl.uniprot.org/annotation/VSP_037435
http://togogenome.org/gene/9606:SV2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E000|||http://purl.uniprot.org/uniprot/Q7L0J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with SYT1|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239764|||http://purl.uniprot.org/annotation/VSP_019265
http://togogenome.org/gene/9606:CNBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4K2|||http://purl.uniprot.org/uniprot/A0A0S2Z4Q3|||http://purl.uniprot.org/uniprot/P62633                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||CCHC-type 4|||CCHC-type 5|||CCHC-type 6|||CCHC-type 7|||CCHC-type zinc finger nucleic acid binding protein|||In isoform 2, isoform 5 and isoform 8.|||In isoform 3.|||In isoform 4 and isoform 8.|||In isoform 5 and isoform 6.|||In isoform 7.|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||RNA-binding Arg/Gly-rich region (RGG-box)|||Removed|||Significantly reduces methylation; when associated with K-25.|||Significantly reduces methylation; when associated with K-27.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089965|||http://purl.uniprot.org/annotation/VSP_010981|||http://purl.uniprot.org/annotation/VSP_010982|||http://purl.uniprot.org/annotation/VSP_043304|||http://purl.uniprot.org/annotation/VSP_043424|||http://purl.uniprot.org/annotation/VSP_055084
http://togogenome.org/gene/9606:DNAJB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KPS0|||http://purl.uniprot.org/uniprot/Q9NXW2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished histidine methylation by METTL9.|||Abolishes interaction with HSPA8/Hsc70.|||Cytoplasmic|||Disordered|||DnaJ homolog subfamily B member 12|||Helical|||In delta(G/F); impaired ability to form tetramers and impaired ability to promote potassium channel assembly into tetramers.|||In isoform 2.|||J|||Lumenal|||N-acetylmethionine|||Polar residues|||Pros-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071037|||http://purl.uniprot.org/annotation/VAR_017864|||http://purl.uniprot.org/annotation/VSP_039040
http://togogenome.org/gene/9606:ZC3H18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTK7|||http://purl.uniprot.org/uniprot/E7ERS3|||http://purl.uniprot.org/uniprot/Q86VM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger CCCH domain-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311242|||http://purl.uniprot.org/annotation/VAR_037188|||http://purl.uniprot.org/annotation/VAR_037189
http://togogenome.org/gene/9606:PGBD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N328                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||PiggyBac transposable element-derived protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288054|||http://purl.uniprot.org/annotation/VAR_032391|||http://purl.uniprot.org/annotation/VAR_035621|||http://purl.uniprot.org/annotation/VAR_051274
http://togogenome.org/gene/9606:GKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VSY0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||G kinase-anchoring protein 1|||In isoform 2.|||Interaction with IRS1|||Phosphoserine|||Phosphoserine; by PKG|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315654|||http://purl.uniprot.org/annotation/VSP_030596
http://togogenome.org/gene/9606:COX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0S2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial|||Disordered|||Helical|||In MC4DN22; isolated complex IV deficiency in homozygous patient cells.|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019556|||http://purl.uniprot.org/annotation/VAR_085648
http://togogenome.org/gene/9606:NLGN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2Q7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not affect subcellular location.|||In AUTS20; risk factor for disease development; decreased function in dendritic spine formation; decreased protein abundance; does not localize to the plasma membrane but is retained in the endoplasmic reticulum.|||In AUTS20; unknown pathological significance.|||In AUTS20; unknown pathological significance; does not affect dendritic spine formation; no effect on protein abundance; no effect on subcellular localization.|||In isoform 2.|||Likely benign variant; does not affect dendritic spine formation; does not affect localization to plasma membrane.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Neuroligin-1|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008640|||http://purl.uniprot.org/annotation/VAR_084195|||http://purl.uniprot.org/annotation/VAR_084196|||http://purl.uniprot.org/annotation/VAR_084197|||http://purl.uniprot.org/annotation/VAR_084198|||http://purl.uniprot.org/annotation/VAR_084199|||http://purl.uniprot.org/annotation/VAR_084200|||http://purl.uniprot.org/annotation/VAR_084201|||http://purl.uniprot.org/annotation/VSP_060231
http://togogenome.org/gene/9606:B3GALT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43825                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyltransferase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219150
http://togogenome.org/gene/9606:MEX3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U5Q3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||KH 1|||KH 2|||Phosphoserine|||Polar residues|||Prevents RNA binding.|||Pro residues|||RING-type|||RNA-binding E3 ubiquitin-protein ligase MEX3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278782|||http://purl.uniprot.org/annotation/VAR_030832
http://togogenome.org/gene/9606:ZER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7L7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Abolishes interaction with ELOC.|||Complete loss of N-degron binding.|||LRR 1|||LRR 2|||LRR 3|||N-acetylalanine|||Protein zer-1 homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066598|||http://purl.uniprot.org/annotation/VAR_060159
http://togogenome.org/gene/9606:OTUD7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE49                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||Basic and acidic residues|||Catalytic|||Disordered|||In isoform 2.|||Nuclear localization signal|||Nucleophile|||OTU|||OTU domain-containing protein 7A|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Proton acceptor|||TRAF-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188789|||http://purl.uniprot.org/annotation/VSP_011430
http://togogenome.org/gene/9606:SPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z351|||http://purl.uniprot.org/uniprot/P10451|||http://purl.uniprot.org/uniprot/Q3LGB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cell attachment site|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Osteopontin|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphothreonine; by FAM20C|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020321|||http://purl.uniprot.org/annotation/PRO_5040057958|||http://purl.uniprot.org/annotation/VAR_014717|||http://purl.uniprot.org/annotation/VAR_050432|||http://purl.uniprot.org/annotation/VSP_003777|||http://purl.uniprot.org/annotation/VSP_011639|||http://purl.uniprot.org/annotation/VSP_043695
http://togogenome.org/gene/9606:PLXDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUK5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Plexin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232751|||http://purl.uniprot.org/annotation/VAR_064050|||http://purl.uniprot.org/annotation/VSP_017970|||http://purl.uniprot.org/annotation/VSP_017971|||http://purl.uniprot.org/annotation/VSP_017972|||http://purl.uniprot.org/annotation/VSP_017973|||http://purl.uniprot.org/annotation/VSP_017974
http://togogenome.org/gene/9606:ULBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZM5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||MHC class I alpha-1 like|||MHC class I alpha-2 like|||N-linked (GlcNAc...) asparagine|||Not secreted.|||Removed in mature form|||Secreted.|||UL16-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019017|||http://purl.uniprot.org/annotation/PRO_0000019018
http://togogenome.org/gene/9606:SLITRK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW52                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with schizophrenia; found as somatic mutation in a colorectal cancer sample; unknown pathological significance; decreased localization to cell membrane; decreased function in synaptogenesis.|||Found in a patient with schizophrenia; unknown pathological significance; decreased localization to cell membrane; decreased function in synaptogenesis.|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||SLIT and NTRK-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032679|||http://purl.uniprot.org/annotation/VAR_036602|||http://purl.uniprot.org/annotation/VAR_077632
http://togogenome.org/gene/9606:IVL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07476                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Lipid Binding|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24; approximate|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||34|||35|||36; approximate|||37|||38|||39 X 10 AA approximate tandem repeats of [LP]-[EKG]-[LHVYQEK]-[PLSQE]-[EQDV]-[QHEKRGA]-Q-[EMVQLP]-[GKLE]-[QHVNLD]|||39; approximate|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Involucrin|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)|||Omega-hydroxyceramide glutamate ester|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159736|||http://purl.uniprot.org/annotation/VAR_029019|||http://purl.uniprot.org/annotation/VAR_029020|||http://purl.uniprot.org/annotation/VAR_029021|||http://purl.uniprot.org/annotation/VAR_029022|||http://purl.uniprot.org/annotation/VAR_029023|||http://purl.uniprot.org/annotation/VAR_029024|||http://purl.uniprot.org/annotation/VAR_058411|||http://purl.uniprot.org/annotation/VAR_058412
http://togogenome.org/gene/9606:LARP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4E2|||http://purl.uniprot.org/uniprot/Q71RC2|||http://purl.uniprot.org/uniprot/Q96J85                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with PABPC1|||Interaction with the poly-A tract of mRNA|||La-related protein 4|||N-acetylmethionine|||Nearly abolishes interaction with PABPC1; when associated with A-15.|||Nearly abolishes interaction with PABPC1; when associated with A-22.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207611|||http://purl.uniprot.org/annotation/VAR_055936|||http://purl.uniprot.org/annotation/VAR_055937|||http://purl.uniprot.org/annotation/VSP_014611|||http://purl.uniprot.org/annotation/VSP_014612|||http://purl.uniprot.org/annotation/VSP_033811|||http://purl.uniprot.org/annotation/VSP_033812|||http://purl.uniprot.org/annotation/VSP_045677|||http://purl.uniprot.org/annotation/VSP_046780|||http://purl.uniprot.org/annotation/VSP_046781
http://togogenome.org/gene/9606:BBS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXC9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Bardet-Biedl syndrome 2 protein|||In BBS2 and RP74.|||In BBS2.|||In BBS2; has a modifier effect on BBS.|||In BBS2; in linkage disequilibrium with V-123 in a Bedouin kindred.|||In RP74.|||In a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10; uncertain pathological role.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064843|||http://purl.uniprot.org/annotation/VAR_013162|||http://purl.uniprot.org/annotation/VAR_013163|||http://purl.uniprot.org/annotation/VAR_013164|||http://purl.uniprot.org/annotation/VAR_013165|||http://purl.uniprot.org/annotation/VAR_013166|||http://purl.uniprot.org/annotation/VAR_013167|||http://purl.uniprot.org/annotation/VAR_013168|||http://purl.uniprot.org/annotation/VAR_013169|||http://purl.uniprot.org/annotation/VAR_029747|||http://purl.uniprot.org/annotation/VAR_029748|||http://purl.uniprot.org/annotation/VAR_038889|||http://purl.uniprot.org/annotation/VAR_038890|||http://purl.uniprot.org/annotation/VAR_038891|||http://purl.uniprot.org/annotation/VAR_038892|||http://purl.uniprot.org/annotation/VAR_066280|||http://purl.uniprot.org/annotation/VAR_066281|||http://purl.uniprot.org/annotation/VAR_066282|||http://purl.uniprot.org/annotation/VAR_066283|||http://purl.uniprot.org/annotation/VAR_066284|||http://purl.uniprot.org/annotation/VAR_066285|||http://purl.uniprot.org/annotation/VAR_075726|||http://purl.uniprot.org/annotation/VAR_075727|||http://purl.uniprot.org/annotation/VAR_075728
http://togogenome.org/gene/9606:FHIP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N612                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHF complex subunit HOOK-interacting protein 1B|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253859|||http://purl.uniprot.org/annotation/VAR_028739|||http://purl.uniprot.org/annotation/VAR_028740|||http://purl.uniprot.org/annotation/VAR_028741|||http://purl.uniprot.org/annotation/VAR_057805|||http://purl.uniprot.org/annotation/VSP_021128|||http://purl.uniprot.org/annotation/VSP_021129|||http://purl.uniprot.org/annotation/VSP_021130|||http://purl.uniprot.org/annotation/VSP_021131
http://togogenome.org/gene/9606:RALGAPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2PPJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PKB|||Phosphothreonine; by PKB|||Polar residues|||Ral GTPase-activating protein subunit alpha-2|||Rap-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286972|||http://purl.uniprot.org/annotation/VAR_049157|||http://purl.uniprot.org/annotation/VSP_025247|||http://purl.uniprot.org/annotation/VSP_025248
http://togogenome.org/gene/9606:OR10J5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV70|||http://purl.uniprot.org/uniprot/Q8NHC4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10J5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150709|||http://purl.uniprot.org/annotation/VAR_062064
http://togogenome.org/gene/9606:THAP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5L6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  DNA transposase THAP9|||HCFC1-binding motif (HBM)|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317246|||http://purl.uniprot.org/annotation/VAR_038486|||http://purl.uniprot.org/annotation/VAR_038487|||http://purl.uniprot.org/annotation/VAR_038488|||http://purl.uniprot.org/annotation/VAR_061842
http://togogenome.org/gene/9606:CD81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJK1|||http://purl.uniprot.org/uniprot/P60033                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CD81 antigen|||Cytoplasmic|||Extracellular|||Helical|||Important for interaction with integrin|||Mildly reduced affinity for HCV protein E2.|||No effect on integrin binding.|||Reduced affinity for cholesterol binding.|||Reduces binding to integrin.|||Reduces binding to integrin; when associated with E-144.|||Reduces binding to integrin; when associated with E-148.|||Strongly reduced affinity for HCV protein E2.|||Strongly reduced affinity for HCV protein E2; when associated with E-196.|||Strongly reduced affinity for HCV protein E2; when associated with K-188 or Q-188.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219221
http://togogenome.org/gene/9606:BOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IK1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Biorientation of chromosomes in cell division protein 1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187028|||http://purl.uniprot.org/annotation/VSP_016161|||http://purl.uniprot.org/annotation/VSP_016162
http://togogenome.org/gene/9606:LIPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXI9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Lipase member N|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286831|||http://purl.uniprot.org/annotation/VAR_032192
http://togogenome.org/gene/9606:PGD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2U0|||http://purl.uniprot.org/uniprot/P52209                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  6-phosphogluconate dehydrogenase C-terminal|||6-phosphogluconate dehydrogenase, decarboxylating|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Proton acceptor|||Proton donor|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090063|||http://purl.uniprot.org/annotation/VAR_048104|||http://purl.uniprot.org/annotation/VSP_055767
http://togogenome.org/gene/9606:MED15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2H7|||http://purl.uniprot.org/uniprot/G3V1P5|||http://purl.uniprot.org/uniprot/Q6PKB8|||http://purl.uniprot.org/uniprot/Q96RN5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates interaction with SREBF1.|||Asymmetric dimethylarginine|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with SREBF1|||Mediator of RNA polymerase II transcription subunit 15|||Nuclear localization signal|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058264|||http://purl.uniprot.org/annotation/VAR_013136|||http://purl.uniprot.org/annotation/VSP_003922|||http://purl.uniprot.org/annotation/VSP_013024
http://togogenome.org/gene/9606:GPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24298                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Alanine aminotransferase 1|||Found in patient with Joubert syndrome; unknown pathological significance.|||In allele GPT*2.|||N-acetylalanine|||N6-(pyridoxal phosphate)lysine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123933|||http://purl.uniprot.org/annotation/VAR_000561|||http://purl.uniprot.org/annotation/VAR_075711|||http://purl.uniprot.org/annotation/VAR_075712
http://togogenome.org/gene/9606:RNF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78317                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||Disordered|||Dominant-negative E2-binding mutant, leads to increased trapping of PARP1 to chromatin; when associated with A-177.|||Dominant-negative E2-binding mutant, leads to increased trapping of PARP1 to chromatin; when associated with S-136.|||E3 ubiquitin-protein ligase RNF4|||In isoform 2.|||Mediates interaction with TRPS1|||Phosphoserine|||Polar residues|||RING-type|||Required for ubiquitination activity|||SUMO interaction motif 1|||SUMO interaction motif 2|||SUMO interaction motif 3|||SUMO interaction motif 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056043|||http://purl.uniprot.org/annotation/VSP_045789|||http://purl.uniprot.org/annotation/VSP_045790
http://togogenome.org/gene/9606:TCERG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FF 1|||FF 2|||In a colorectal cancer sample; somatic mutation.|||Transcription elongation regulator 1-like protein|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312872|||http://purl.uniprot.org/annotation/VAR_037601|||http://purl.uniprot.org/annotation/VAR_037602|||http://purl.uniprot.org/annotation/VAR_037603|||http://purl.uniprot.org/annotation/VAR_037604
http://togogenome.org/gene/9606:DMRTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor A1|||In a colorectal cancer sample; somatic mutation.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242700|||http://purl.uniprot.org/annotation/VAR_036331
http://togogenome.org/gene/9606:SLC35F5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZV6|||http://purl.uniprot.org/uniprot/B8ZZY4|||http://purl.uniprot.org/uniprot/Q8WV83                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  EamA|||Helical|||In isoform 2.|||Phosphoserine|||Solute carrier family 35 member F5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311956|||http://purl.uniprot.org/annotation/VSP_029665|||http://purl.uniprot.org/annotation/VSP_029666|||http://purl.uniprot.org/annotation/VSP_029667|||http://purl.uniprot.org/annotation/VSP_029668
http://togogenome.org/gene/9606:SNAP23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K287|||http://purl.uniprot.org/uniprot/O00161                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform SNAP-23b.|||N-acetylmethionine|||Phosphoserine|||S-palmitoyl cysteine|||Synaptosomal-associated protein 23|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology 1|||t-SNARE coiled-coil homology 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213598|||http://purl.uniprot.org/annotation/VSP_006187|||http://purl.uniprot.org/annotation/VSP_006188
http://togogenome.org/gene/9606:GRIK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8D9PH75|||http://purl.uniprot.org/uniprot/A8K0H7|||http://purl.uniprot.org/uniprot/Q13002|||http://purl.uniprot.org/uniprot/Q8IY40                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutamate receptor ionotropic, kainate 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||In NEDLAS; causes markedly reduced peak current amplitudes and very fast gating kinetics; no effect on homomeric receptor localization to the plasma membrane when expressed in heterologous cells.|||In NEDLAS; causes profound slowing of channel deactivation and constitutive tonic current activation compared to wild-type, indicating altered channel gating kinetics; may decrease cell surface expression.|||In NEDLAS; gain of function; when incorporated into kainate receptor, produces constitutively active channels with significantly altered gating kinetics; may decrease cell surface expression.|||In RNA edited version.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 7.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC|||Receptor ligand binding region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011544|||http://purl.uniprot.org/annotation/VAR_000305|||http://purl.uniprot.org/annotation/VAR_000306|||http://purl.uniprot.org/annotation/VAR_000307|||http://purl.uniprot.org/annotation/VAR_035694|||http://purl.uniprot.org/annotation/VAR_037633|||http://purl.uniprot.org/annotation/VAR_049186|||http://purl.uniprot.org/annotation/VAR_078426|||http://purl.uniprot.org/annotation/VAR_086335|||http://purl.uniprot.org/annotation/VAR_086336|||http://purl.uniprot.org/annotation/VAR_086337|||http://purl.uniprot.org/annotation/VSP_022334|||http://purl.uniprot.org/annotation/VSP_022335|||http://purl.uniprot.org/annotation/VSP_022336|||http://purl.uniprot.org/annotation/VSP_022337|||http://purl.uniprot.org/annotation/VSP_044388|||http://purl.uniprot.org/annotation/VSP_044389
http://togogenome.org/gene/9606:CXADR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78310                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to adenovirus type 5.|||Affects basolateral localization in airway epithelial cells.|||Basic and acidic residues|||Coxsackievirus and adenovirus receptor|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of palmitoylation and altered localization.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014739|||http://purl.uniprot.org/annotation/VAR_049871|||http://purl.uniprot.org/annotation/VSP_014819|||http://purl.uniprot.org/annotation/VSP_014820|||http://purl.uniprot.org/annotation/VSP_014821|||http://purl.uniprot.org/annotation/VSP_014822|||http://purl.uniprot.org/annotation/VSP_014823|||http://purl.uniprot.org/annotation/VSP_014824|||http://purl.uniprot.org/annotation/VSP_014825|||http://purl.uniprot.org/annotation/VSP_014826|||http://purl.uniprot.org/annotation/VSP_047357|||http://purl.uniprot.org/annotation/VSP_047729
http://togogenome.org/gene/9606:CFHR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92496                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Complement factor H-related protein 4|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000072607|||http://purl.uniprot.org/annotation/VAR_047151|||http://purl.uniprot.org/annotation/VAR_070195|||http://purl.uniprot.org/annotation/VAR_070196|||http://purl.uniprot.org/annotation/VSP_046418|||http://purl.uniprot.org/annotation/VSP_053528
http://togogenome.org/gene/9606:SIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14190                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform SIM2S.|||No effect on nuclear translocation.|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Reduced nuclear translocation.|||Single-minded C-terminal|||Single-minded homolog 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127441|||http://purl.uniprot.org/annotation/VAR_024281|||http://purl.uniprot.org/annotation/VSP_002148|||http://purl.uniprot.org/annotation/VSP_012767
http://togogenome.org/gene/9606:CTH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32929                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cystathionine gamma-lyase|||In CSTNU; reduces catalytic activity and affinity for pyridoxal phosphate.|||In CSTNU; strongly reduces catalytic activity and affinity for pyridoxal phosphate.|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114749|||http://purl.uniprot.org/annotation/VAR_015450|||http://purl.uniprot.org/annotation/VAR_015451|||http://purl.uniprot.org/annotation/VAR_015452|||http://purl.uniprot.org/annotation/VSP_006306|||http://purl.uniprot.org/annotation/VSP_047274
http://togogenome.org/gene/9606:IGFL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6B9Z1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Insulin growth factor-like family member 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045062|||http://purl.uniprot.org/annotation/VAR_049571|||http://purl.uniprot.org/annotation/VAR_049572
http://togogenome.org/gene/9606:ECSIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ95                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Complete loss of interaction with RELA and NFKB1 together with loss of NF-kappa-B-dependent gene expression.|||Disordered|||Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291985|||http://purl.uniprot.org/annotation/VAR_032907|||http://purl.uniprot.org/annotation/VAR_032908|||http://purl.uniprot.org/annotation/VSP_026345|||http://purl.uniprot.org/annotation/VSP_026346|||http://purl.uniprot.org/annotation/VSP_046689|||http://purl.uniprot.org/annotation/VSP_055626
http://togogenome.org/gene/9606:H3-3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4P9|||http://purl.uniprot.org/uniprot/P84243                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolished serotonylation by TGM2.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H2A/H2B/H3|||Histone H3.3|||In BRYLIB1 and BRYLIB2.|||In BRYLIB1 and BRYLIB2; unknown pathological significance.|||In BRYLIB1.|||In BRYLIB1; decreased protein abundance.|||In BRYLIB1; unknown pathological significance.|||In BRYLIB1; unknown pathological significance; decreased protein abundance; increased interaction with DAXX; not changed subcellular location.|||In BRYLIB1; unknown pathological significance; increased protein abundance.|||In BRYLIB1; unknown pathological significance; no effect on protein abundance.|||In BRYLIB2.|||In BRYLIB2; unknown pathological significance.|||In BRYLIB2; unknown pathological significance; decreased protein abundance.|||In BRYLIB2; unknown pathological significance; no effect on protein abundance.|||In GLM and BRYLIB2; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels.|||In GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels.|||In GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels.|||Interaction with ZMYND11|||Loss of interaction with DNAJC9, but not with other histone chaperones, such as ASF1A, MCCM2, NASP or SPT2.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||Probable disease-associated variant found in chondroblastoma and clear cell chondrosarcoma; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in giant cell tumors of bone; somatic mutation.|||Reduced binding of histone H1 to histone H3.3-containing nucleosomes.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221247|||http://purl.uniprot.org/annotation/VAR_079021|||http://purl.uniprot.org/annotation/VAR_079022|||http://purl.uniprot.org/annotation/VAR_079023|||http://purl.uniprot.org/annotation/VAR_079024|||http://purl.uniprot.org/annotation/VAR_079025|||http://purl.uniprot.org/annotation/VAR_087155|||http://purl.uniprot.org/annotation/VAR_087156|||http://purl.uniprot.org/annotation/VAR_087157|||http://purl.uniprot.org/annotation/VAR_087158|||http://purl.uniprot.org/annotation/VAR_087159|||http://purl.uniprot.org/annotation/VAR_087160|||http://purl.uniprot.org/annotation/VAR_087161|||http://purl.uniprot.org/annotation/VAR_087162|||http://purl.uniprot.org/annotation/VAR_087163|||http://purl.uniprot.org/annotation/VAR_087164|||http://purl.uniprot.org/annotation/VAR_087165|||http://purl.uniprot.org/annotation/VAR_087166|||http://purl.uniprot.org/annotation/VAR_087167|||http://purl.uniprot.org/annotation/VAR_087168|||http://purl.uniprot.org/annotation/VAR_087169|||http://purl.uniprot.org/annotation/VAR_087170|||http://purl.uniprot.org/annotation/VAR_087171|||http://purl.uniprot.org/annotation/VAR_087172|||http://purl.uniprot.org/annotation/VAR_087173|||http://purl.uniprot.org/annotation/VAR_087174|||http://purl.uniprot.org/annotation/VAR_087175|||http://purl.uniprot.org/annotation/VAR_087176|||http://purl.uniprot.org/annotation/VAR_087177|||http://purl.uniprot.org/annotation/VAR_087178|||http://purl.uniprot.org/annotation/VAR_087179|||http://purl.uniprot.org/annotation/VAR_087180|||http://purl.uniprot.org/annotation/VAR_087181|||http://purl.uniprot.org/annotation/VAR_087182|||http://purl.uniprot.org/annotation/VAR_087183|||http://purl.uniprot.org/annotation/VAR_087184|||http://purl.uniprot.org/annotation/VAR_087185|||http://purl.uniprot.org/annotation/VAR_087186|||http://purl.uniprot.org/annotation/VAR_087187|||http://purl.uniprot.org/annotation/VAR_087188|||http://purl.uniprot.org/annotation/VAR_087189|||http://purl.uniprot.org/annotation/VAR_087190|||http://purl.uniprot.org/annotation/VAR_087191|||http://purl.uniprot.org/annotation/VAR_087192|||http://purl.uniprot.org/annotation/VAR_087193
http://togogenome.org/gene/9606:SLC7A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPY5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cystine/glutamate transporter|||Cytoplasmic|||Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.|||Does not affect L-cystine transport activity.|||Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.|||Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.|||Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.|||Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.|||Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.|||Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.|||Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.|||Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.|||Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.|||Extracellular|||Helical|||Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.|||Increases sensitivity to erastin-induced ferroptosis.|||Interchain (with C-210 in SLC3A2)|||Loss of L-cystine transport activity.|||Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.|||Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.|||N-linked (GlcNAc...) asparagine|||Phosphoserine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054279
http://togogenome.org/gene/9606:YAE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRH1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein YAE1 homolog|||deca-GX3 motif; required for interaction with LTO1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089591|||http://purl.uniprot.org/annotation/VAR_024306|||http://purl.uniprot.org/annotation/VSP_055295|||http://purl.uniprot.org/annotation/VSP_055296
http://togogenome.org/gene/9606:C8orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P047                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C8orf74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270931|||http://purl.uniprot.org/annotation/VAR_033684|||http://purl.uniprot.org/annotation/VAR_061596
http://togogenome.org/gene/9606:DQX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE96                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DQX1|||DEAQ box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284377|||http://purl.uniprot.org/annotation/VSP_024470|||http://purl.uniprot.org/annotation/VSP_024471|||http://purl.uniprot.org/annotation/VSP_024472
http://togogenome.org/gene/9606:KRR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13601                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KH|||KRR1 small subunit processome component homolog|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050114|||http://purl.uniprot.org/annotation/VAR_049680|||http://purl.uniprot.org/annotation/VSP_042223
http://togogenome.org/gene/9606:ADCK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIX3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein kinase|||Uncharacterized aarF domain-containing protein kinase 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271800|||http://purl.uniprot.org/annotation/VAR_029996
http://togogenome.org/gene/9606:CFAP410                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43822                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 410|||Disordered|||In RDMS.|||In SMDAX.|||In SMDAX; abolishes interaction with NEK1.|||In SMDAX; increases protein degradation; changes protein localization.|||In SMDAX; patients may exhibit clinical features overlapping with Jeune syndrome; decreased function in ciliogenesis; abolishes interaction with NEK1.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform Short.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079503|||http://purl.uniprot.org/annotation/VAR_016155|||http://purl.uniprot.org/annotation/VAR_050927|||http://purl.uniprot.org/annotation/VAR_075924|||http://purl.uniprot.org/annotation/VAR_075925|||http://purl.uniprot.org/annotation/VAR_075926|||http://purl.uniprot.org/annotation/VAR_075927|||http://purl.uniprot.org/annotation/VAR_079180|||http://purl.uniprot.org/annotation/VAR_079181|||http://purl.uniprot.org/annotation/VAR_079182|||http://purl.uniprot.org/annotation/VSP_004138|||http://purl.uniprot.org/annotation/VSP_004139|||http://purl.uniprot.org/annotation/VSP_047417|||http://purl.uniprot.org/annotation/VSP_047418
http://togogenome.org/gene/9606:POU3F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03052                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||Disordered|||Homeobox|||POU domain, class 3, transcription factor 1|||POU-specific                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100720
http://togogenome.org/gene/9606:WFDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUB2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||WAP 1|||WAP 2|||WAP 3|||WAP 4|||WAP four-disulfide core domain protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041381|||http://purl.uniprot.org/annotation/VAR_052951|||http://purl.uniprot.org/annotation/VAR_059962
http://togogenome.org/gene/9606:TUFT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4Y1|||http://purl.uniprot.org/uniprot/Q9NNX1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Tuftelin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183186|||http://purl.uniprot.org/annotation/VAR_034574|||http://purl.uniprot.org/annotation/VAR_052424|||http://purl.uniprot.org/annotation/VSP_006685|||http://purl.uniprot.org/annotation/VSP_006686
http://togogenome.org/gene/9606:RGCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4X1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Loss of phosphorylation. Reduced stimulation of CDK1 activity.|||Phosphoserine|||Phosphothreonine; by CDK1|||Polar residues|||Regulator of cell cycle RGCC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274701|||http://purl.uniprot.org/annotation/VSP_022873
http://togogenome.org/gene/9606:AGPAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R640|||http://purl.uniprot.org/uniprot/Q9NUQ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon|||HXXXXD motif|||Helical|||Phospholipid/glycerol acyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208200|||http://purl.uniprot.org/annotation/VAR_022696
http://togogenome.org/gene/9606:TERF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15554                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type|||In isoform 2.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine; by ATM|||Polar residues|||TRFH dimerization|||Telomeric repeat-binding factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197131|||http://purl.uniprot.org/annotation/VAR_050196|||http://purl.uniprot.org/annotation/VSP_003304|||http://purl.uniprot.org/annotation/VSP_003305
http://togogenome.org/gene/9606:TIGD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RP2                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DDE-1|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Tigger transposable element-derived protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272619|||http://purl.uniprot.org/annotation/VAR_030044|||http://purl.uniprot.org/annotation/VAR_030045
http://togogenome.org/gene/9606:MORC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ATPase MORC2|||Abolishes homodimerization. No effect on ATPase activity. Loss of HUSH-dependent gene silencing.|||Abolishes phosphorylation by PAK1. Not recruited on damaged chromatin. Loss of ATPase activity. Prevents chromatin remodeling. Upon irradiation, increases levels of damaged DNA.|||Basic and acidic residues|||CW-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CMT2Z and DIGFAN; decreased ATPase activity; ATP-independent homodimerization; increases HUSH-dependent gene silencing.|||In CMT2Z.|||In CMT2Z; increases HUSH-dependent gene silencing.|||In CMT2Z; slightly decreased ATPase activity; increases HUSH-dependent gene silencing.|||In CMT2Z; unknown pathological significance.|||In DIGFAN and CMT2Z.|||In DIGFAN.|||In DIGFAN; increases HUSH-dependent gene silencing.|||In isoform 2.|||Increases HUSH-dependent gene silencing.|||Loss of ATP-binding and ATPase activity. Does not homodimerizes. Seems to abolish chromatin compaction.|||Loss of ATP-binding and ATPase activity. Loss of binding to ATP and ATPase activity; when associated with A-69. Prevents chromatin remodeling.|||Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-329.|||Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-326 and E-333.|||Loss of HUSH-dependent gene silencing. Decreases dsDNA-binding affinity; when associated with E-329 and E-333.|||N-acetylalanine|||No effect on HUSH-dependent gene silencing.|||No effect on binding to ATP and ATPase activity; when associated with A-68.|||No effect on phosphorylation by PAK1.|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphothreonine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a child with spinal atrophy-phenotype, cerebellar atrophy and diaphragmatic paralysis; also found in a second child with early onset cerebellar ataxia, axonal polyneuropathy and nocturanl hypoventilation; increased ATPase activity; increased rate of dimer assembly and disassembly; decreased HUSH-dependent gene silencing.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096537|||http://purl.uniprot.org/annotation/VAR_076454|||http://purl.uniprot.org/annotation/VAR_076455|||http://purl.uniprot.org/annotation/VAR_076456|||http://purl.uniprot.org/annotation/VAR_076457|||http://purl.uniprot.org/annotation/VAR_076458|||http://purl.uniprot.org/annotation/VAR_076459|||http://purl.uniprot.org/annotation/VAR_076460|||http://purl.uniprot.org/annotation/VAR_076461|||http://purl.uniprot.org/annotation/VAR_076462|||http://purl.uniprot.org/annotation/VAR_076463|||http://purl.uniprot.org/annotation/VAR_081260|||http://purl.uniprot.org/annotation/VAR_085367|||http://purl.uniprot.org/annotation/VAR_085368|||http://purl.uniprot.org/annotation/VAR_085369|||http://purl.uniprot.org/annotation/VAR_085370|||http://purl.uniprot.org/annotation/VAR_085371|||http://purl.uniprot.org/annotation/VAR_085372|||http://purl.uniprot.org/annotation/VAR_085373|||http://purl.uniprot.org/annotation/VAR_085374|||http://purl.uniprot.org/annotation/VAR_085375|||http://purl.uniprot.org/annotation/VAR_085376|||http://purl.uniprot.org/annotation/VAR_085377|||http://purl.uniprot.org/annotation/VAR_085378|||http://purl.uniprot.org/annotation/VAR_085379|||http://purl.uniprot.org/annotation/VAR_085380|||http://purl.uniprot.org/annotation/VAR_085381|||http://purl.uniprot.org/annotation/VAR_085382|||http://purl.uniprot.org/annotation/VAR_085383|||http://purl.uniprot.org/annotation/VSP_041759
http://togogenome.org/gene/9606:RAB42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4Z0                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Ras-related protein Rab-42|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269848|||http://purl.uniprot.org/annotation/VSP_059258
http://togogenome.org/gene/9606:CBARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N350                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Voltage-dependent calcium channel beta subunit-associated regulatory protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079983|||http://purl.uniprot.org/annotation/VSP_058134|||http://purl.uniprot.org/annotation/VSP_058135
http://togogenome.org/gene/9606:MAZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56270|||http://purl.uniprot.org/uniprot/Q59GP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; atypical|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Myc-associated zinc finger protein|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047215|||http://purl.uniprot.org/annotation/VSP_044561|||http://purl.uniprot.org/annotation/VSP_047560|||http://purl.uniprot.org/annotation/VSP_055108
http://togogenome.org/gene/9606:GP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCN6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Dramatically reduces collagen binding.|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In BDPLT11; results in abnormal protein migration and a loss of collagen binding.|||In BDPLT11; shows strongly reduced membrane expression and decreased interaction with the snake toxin convulxin.|||In isoform 2.|||In isoform 3.|||Increases collagen binding.|||N-linked (GlcNAc...) asparagine|||No effect on collagen binding.|||Platelet glycoprotein VI|||Reduces collagen binding (65 to 70%).|||Reduces collagen binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232383|||http://purl.uniprot.org/annotation/VAR_059389|||http://purl.uniprot.org/annotation/VAR_059390|||http://purl.uniprot.org/annotation/VAR_060352|||http://purl.uniprot.org/annotation/VAR_060353|||http://purl.uniprot.org/annotation/VAR_060354|||http://purl.uniprot.org/annotation/VAR_060355|||http://purl.uniprot.org/annotation/VAR_066590|||http://purl.uniprot.org/annotation/VAR_066591|||http://purl.uniprot.org/annotation/VSP_017879|||http://purl.uniprot.org/annotation/VSP_017880
http://togogenome.org/gene/9606:DHRS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPW9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Decreases androsterone dehydrogenase activity; when associated with F-176.|||Decreases androsterone dehydrogenase activity; when associated with R-180.|||Dehydrogenase/reductase SDR family member 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042617|||http://purl.uniprot.org/annotation/VAR_052320|||http://purl.uniprot.org/annotation/VSP_015875|||http://purl.uniprot.org/annotation/VSP_015876|||http://purl.uniprot.org/annotation/VSP_054357
http://togogenome.org/gene/9606:MBOAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0AZU0|||http://purl.uniprot.org/uniprot/B7Z3I3|||http://purl.uniprot.org/uniprot/Q6ZWT7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Lysophospholipid acyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273020|||http://purl.uniprot.org/annotation/VAR_030068
http://togogenome.org/gene/9606:ITGAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BN02|||http://purl.uniprot.org/uniprot/P20702                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Integrin alpha-X|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016294|||http://purl.uniprot.org/annotation/PRO_5001424941|||http://purl.uniprot.org/annotation/VAR_018672|||http://purl.uniprot.org/annotation/VAR_031925|||http://purl.uniprot.org/annotation/VAR_031926|||http://purl.uniprot.org/annotation/VAR_031927|||http://purl.uniprot.org/annotation/VAR_031928|||http://purl.uniprot.org/annotation/VAR_049632|||http://purl.uniprot.org/annotation/VAR_059363|||http://purl.uniprot.org/annotation/VAR_066662
http://togogenome.org/gene/9606:DUS4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0R5|||http://purl.uniprot.org/uniprot/O95620                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DUS-like FMN-binding|||In isoform 2.|||Proton donor|||tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247347|||http://purl.uniprot.org/annotation/VAR_027094|||http://purl.uniprot.org/annotation/VAR_048938|||http://purl.uniprot.org/annotation/VSP_019975
http://togogenome.org/gene/9606:ZNF160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QZI7|||http://purl.uniprot.org/uniprot/Q9HCG1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 160                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047433|||http://purl.uniprot.org/annotation/VAR_057400|||http://purl.uniprot.org/annotation/VAR_060274|||http://purl.uniprot.org/annotation/VSP_055940|||http://purl.uniprot.org/annotation/VSP_055941
http://togogenome.org/gene/9606:OR6S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH40                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150637|||http://purl.uniprot.org/annotation/VAR_057562|||http://purl.uniprot.org/annotation/VAR_057563|||http://purl.uniprot.org/annotation/VAR_057564|||http://purl.uniprot.org/annotation/VAR_057565
http://togogenome.org/gene/9606:LILRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSV6|||http://purl.uniprot.org/uniprot/A0A087WSX8|||http://purl.uniprot.org/uniprot/A0A0B4J1W1|||http://purl.uniprot.org/uniprot/A8MVE2|||http://purl.uniprot.org/uniprot/D9IDM5|||http://purl.uniprot.org/uniprot/Q8NHL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Leukocyte immunoglobulin-like receptor subfamily B member 1|||N-linked (GlcNAc...) asparagine|||No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644.|||No effect on PTPN6 binding; when associated with F-533.|||Phosphotyrosine|||Polar residues|||Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014820|||http://purl.uniprot.org/annotation/PRO_5001831881|||http://purl.uniprot.org/annotation/PRO_5002105561|||http://purl.uniprot.org/annotation/PRO_5002726826|||http://purl.uniprot.org/annotation/PRO_5014013280|||http://purl.uniprot.org/annotation/PRO_5014088082|||http://purl.uniprot.org/annotation/VAR_016993|||http://purl.uniprot.org/annotation/VAR_016994|||http://purl.uniprot.org/annotation/VAR_016995|||http://purl.uniprot.org/annotation/VAR_016996|||http://purl.uniprot.org/annotation/VAR_049888|||http://purl.uniprot.org/annotation/VAR_059398|||http://purl.uniprot.org/annotation/VAR_067316|||http://purl.uniprot.org/annotation/VAR_067317|||http://purl.uniprot.org/annotation/VSP_008456|||http://purl.uniprot.org/annotation/VSP_008457|||http://purl.uniprot.org/annotation/VSP_057087|||http://purl.uniprot.org/annotation/VSP_057088
http://togogenome.org/gene/9606:FBLN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6G3|||http://purl.uniprot.org/uniprot/Q9UBX5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||Fibulin-5|||Found in a patient with autosomal recessive cutis laxa also carrying a mutation in ELN; unknown pathological significance.|||In ARCL1A; decreases expression; produces protein misfolding; abolishes secretion; reduces interaction with ELN; increases homodimerization; impairs elastic fiber development.|||In ARCL1A; formation of extracellular globular aggregates; decreases cell growth; reduces interaction with ELN; abolishes secretion; increases homodimerization.|||In ARMD3, ARCL1A and CMT1H; produces protein misolding; decreases secretion; no effect on homodimerization.|||In ARMD3; almost abolishes secretion; no effect on homodimerization.|||In ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+).|||In ARMD3; decreases secretion; slightly increases homodimerization in absence of Ca(2+); no effect on protein folding.|||In ARMD3; no effect on secretion.|||In ARMD3; no effect on secretion; no effect on homodimerization.|||In ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+).|||In CMT1H.|||N-linked (GlcNAc...) asparagine|||No effect on secretion; slightly increases homodimerization in absence of Ca(2+).|||Slightly increases homodimerization in absence of Ca(2+); no effect on protein folding; no effect on secretion.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007577|||http://purl.uniprot.org/annotation/VAR_017153|||http://purl.uniprot.org/annotation/VAR_019814|||http://purl.uniprot.org/annotation/VAR_019815|||http://purl.uniprot.org/annotation/VAR_019816|||http://purl.uniprot.org/annotation/VAR_019817|||http://purl.uniprot.org/annotation/VAR_019818|||http://purl.uniprot.org/annotation/VAR_019819|||http://purl.uniprot.org/annotation/VAR_019820|||http://purl.uniprot.org/annotation/VAR_026986|||http://purl.uniprot.org/annotation/VAR_072389|||http://purl.uniprot.org/annotation/VAR_072390|||http://purl.uniprot.org/annotation/VAR_072391|||http://purl.uniprot.org/annotation/VAR_072392|||http://purl.uniprot.org/annotation/VAR_072393|||http://purl.uniprot.org/annotation/VAR_072394|||http://purl.uniprot.org/annotation/VAR_076289|||http://purl.uniprot.org/annotation/VAR_076290|||http://purl.uniprot.org/annotation/VAR_076291
http://togogenome.org/gene/9606:DYNLT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7M0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Dynein light chain Tctex-type 5|||May act as disease modifier for Duchenne muscular dystrophy being associated with earlier loss of ambulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284885|||http://purl.uniprot.org/annotation/VAR_031852|||http://purl.uniprot.org/annotation/VAR_055700
http://togogenome.org/gene/9606:HHIPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic residues|||Disordered|||HHIP-like protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314964|||http://purl.uniprot.org/annotation/VAR_053986|||http://purl.uniprot.org/annotation/VAR_062220|||http://purl.uniprot.org/annotation/VAR_062221|||http://purl.uniprot.org/annotation/VAR_062222
http://togogenome.org/gene/9606:UBR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95071                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase UBR5|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Loss of ubiquitin binding.|||N-acetylthreonine|||PABC|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086931|||http://purl.uniprot.org/annotation/VAR_051466|||http://purl.uniprot.org/annotation/VSP_054399
http://togogenome.org/gene/9606:PLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00747|||http://purl.uniprot.org/uniprot/Q5TEH5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Angiostatin|||Apple|||Charge relay system|||Cleavage; by plasminogen activator|||Cleavage; by stromelysin-1|||Cleavage; by stromelysin-19|||Disordered|||In HAE4.|||In HAE4; unknown pathological significance.|||In PLGD.|||In PLGD; Kanagawa-1; 50% activity.|||In PLGD; Nagoya-1.|||In PLGD; common mutation.|||In PLGD; may be associated with susceptibility to thrombosis.|||In PLGD; severe type 1 deficiency.|||In PLGD; type 2 plasminogen deficiency; decreased activity; Nagoya-2/Tochigi/Kagoshima; may be associated with susceptibility to thrombosis.|||Interacts with fibrin|||Interchain (between A and B chains)|||Kringle|||Kringle 1|||Kringle 2|||Kringle 3|||Kringle 4|||Kringle 5|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||PAN|||Peptidase S1|||Phosphoserine|||Plasmin heavy chain A|||Plasmin heavy chain A, short form|||Plasmin light chain B|||Plasminogen|||Proteolytically cleaved, but abolishes plasmin activity and cell detachment. Prevents invasion of the mosquito vector midgut by parasite P.falciparum ookinetes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000016|||http://purl.uniprot.org/annotation/CAR_000017|||http://purl.uniprot.org/annotation/CAR_000018|||http://purl.uniprot.org/annotation/PRO_0000028053|||http://purl.uniprot.org/annotation/PRO_0000028054|||http://purl.uniprot.org/annotation/PRO_0000028055|||http://purl.uniprot.org/annotation/PRO_0000028056|||http://purl.uniprot.org/annotation/PRO_0000028057|||http://purl.uniprot.org/annotation/PRO_0000028058|||http://purl.uniprot.org/annotation/PRO_5014586896|||http://purl.uniprot.org/annotation/VAR_006627|||http://purl.uniprot.org/annotation/VAR_006628|||http://purl.uniprot.org/annotation/VAR_006629|||http://purl.uniprot.org/annotation/VAR_006630|||http://purl.uniprot.org/annotation/VAR_011779|||http://purl.uniprot.org/annotation/VAR_011780|||http://purl.uniprot.org/annotation/VAR_016287|||http://purl.uniprot.org/annotation/VAR_016288|||http://purl.uniprot.org/annotation/VAR_016289|||http://purl.uniprot.org/annotation/VAR_016290|||http://purl.uniprot.org/annotation/VAR_016291|||http://purl.uniprot.org/annotation/VAR_016292|||http://purl.uniprot.org/annotation/VAR_016293|||http://purl.uniprot.org/annotation/VAR_018657|||http://purl.uniprot.org/annotation/VAR_018658|||http://purl.uniprot.org/annotation/VAR_018659|||http://purl.uniprot.org/annotation/VAR_018660|||http://purl.uniprot.org/annotation/VAR_031213|||http://purl.uniprot.org/annotation/VAR_085811|||http://purl.uniprot.org/annotation/VAR_085812|||http://purl.uniprot.org/annotation/VAR_085813
http://togogenome.org/gene/9606:TMEM106C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVX2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Removed|||Transmembrane protein 106C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243900|||http://purl.uniprot.org/annotation/VAR_026868|||http://purl.uniprot.org/annotation/VAR_052338|||http://purl.uniprot.org/annotation/VSP_019483
http://togogenome.org/gene/9606:ANKRD62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC57                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 62|||Basic and acidic residues|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328818|||http://purl.uniprot.org/annotation/VAR_042527|||http://purl.uniprot.org/annotation/VAR_042528|||http://purl.uniprot.org/annotation/VAR_042529|||http://purl.uniprot.org/annotation/VAR_042530|||http://purl.uniprot.org/annotation/VSP_032799
http://togogenome.org/gene/9606:IQCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX19|||http://purl.uniprot.org/uniprot/A0A087WX45|||http://purl.uniprot.org/uniprot/B3KRY4|||http://purl.uniprot.org/uniprot/B4DDX4|||http://purl.uniprot.org/uniprot/B4DXN1|||http://purl.uniprot.org/uniprot/Q6IPM2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||IQ domain-containing protein E|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284110|||http://purl.uniprot.org/annotation/VAR_031697|||http://purl.uniprot.org/annotation/VAR_031698|||http://purl.uniprot.org/annotation/VAR_031699|||http://purl.uniprot.org/annotation/VAR_031700|||http://purl.uniprot.org/annotation/VAR_031701|||http://purl.uniprot.org/annotation/VAR_031702|||http://purl.uniprot.org/annotation/VSP_024433|||http://purl.uniprot.org/annotation/VSP_024434|||http://purl.uniprot.org/annotation/VSP_024435
http://togogenome.org/gene/9606:MIS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1M4|||http://purl.uniprot.org/uniprot/Q9H081                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Protein MIS12 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248234|||http://purl.uniprot.org/annotation/VAR_034106
http://togogenome.org/gene/9606:GUCY2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02846                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  At homozygosity may be associated with Leber congenital amaurosis in some populations.|||Basic and acidic residues|||Changes the substrate specificity from GTP to ATP.|||Cytoplasmic|||Disordered|||Extracellular|||Fails to become activated by GUCA1A and by GUCA1B. Does not affect the binding to RP3.|||Found in a patient with LCA1.|||Guanylate cyclase|||Helical|||In CACD1; unknown pathological significance.|||In CORD6.|||In CORD6; decreases basal and GUCA1A-induced guanylate cyclase activity; inhibition by RD3 is less effective; does not affect endoplasmic reticulum membrane localization.|||In CORD6; loss basal and GUCA1A-induced guanylate cyclase activity; does not affect endoplasmic reticulum membrane localization.|||In LCA1 and CSNB1I.|||In LCA1.|||In LCA1; does not affect basal guanylate cyclase activity; reduces GUCA1A-induced guanylate cyclase activity.|||In LCA1; increases basal and GUCA1A-induced guanylate cyclase activity; inhibition by RD3 is less effective; does not affect endoplasmic reticulum membrane localization.|||In LCA1; loss of activity.|||In LCA1; loss of basal and GUCA1A-induced guanylate cyclase activity; does not affect endoplasmic reticulum membrane localization.|||In LCA1; requires 2 nucleotide substitutions.|||In LCA1; severely impairs basal and GUCA1A induced guanylate cyclase.|||In LCA1; severely impairs basal and GUCA1A-induced guanylate cyclase activity.|||In LCA1; unknown pathological significance.|||In a metastatic melanoma sample; somatic mutation.|||Interchain|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Retinal guanylyl cyclase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012381|||http://purl.uniprot.org/annotation/VAR_003435|||http://purl.uniprot.org/annotation/VAR_003436|||http://purl.uniprot.org/annotation/VAR_003437|||http://purl.uniprot.org/annotation/VAR_003438|||http://purl.uniprot.org/annotation/VAR_009129|||http://purl.uniprot.org/annotation/VAR_009130|||http://purl.uniprot.org/annotation/VAR_009131|||http://purl.uniprot.org/annotation/VAR_009132|||http://purl.uniprot.org/annotation/VAR_009133|||http://purl.uniprot.org/annotation/VAR_009134|||http://purl.uniprot.org/annotation/VAR_009135|||http://purl.uniprot.org/annotation/VAR_015373|||http://purl.uniprot.org/annotation/VAR_023770|||http://purl.uniprot.org/annotation/VAR_023771|||http://purl.uniprot.org/annotation/VAR_042229|||http://purl.uniprot.org/annotation/VAR_042230|||http://purl.uniprot.org/annotation/VAR_042231|||http://purl.uniprot.org/annotation/VAR_042232|||http://purl.uniprot.org/annotation/VAR_049254|||http://purl.uniprot.org/annotation/VAR_049255|||http://purl.uniprot.org/annotation/VAR_049256|||http://purl.uniprot.org/annotation/VAR_067168|||http://purl.uniprot.org/annotation/VAR_067169|||http://purl.uniprot.org/annotation/VAR_067170|||http://purl.uniprot.org/annotation/VAR_067171|||http://purl.uniprot.org/annotation/VAR_067172|||http://purl.uniprot.org/annotation/VAR_067173|||http://purl.uniprot.org/annotation/VAR_067174|||http://purl.uniprot.org/annotation/VAR_067175|||http://purl.uniprot.org/annotation/VAR_067176|||http://purl.uniprot.org/annotation/VAR_067177|||http://purl.uniprot.org/annotation/VAR_067178|||http://purl.uniprot.org/annotation/VAR_067179|||http://purl.uniprot.org/annotation/VAR_067180|||http://purl.uniprot.org/annotation/VAR_067181|||http://purl.uniprot.org/annotation/VAR_067182|||http://purl.uniprot.org/annotation/VAR_067183|||http://purl.uniprot.org/annotation/VAR_071605|||http://purl.uniprot.org/annotation/VAR_071606|||http://purl.uniprot.org/annotation/VAR_071607|||http://purl.uniprot.org/annotation/VAR_071608|||http://purl.uniprot.org/annotation/VAR_080484|||http://purl.uniprot.org/annotation/VAR_082624|||http://purl.uniprot.org/annotation/VAR_082625|||http://purl.uniprot.org/annotation/VAR_082626|||http://purl.uniprot.org/annotation/VAR_082627|||http://purl.uniprot.org/annotation/VAR_082628
http://togogenome.org/gene/9606:STAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14765                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  About 50% loss of transcriptional activity.|||Abrogates phosphorylation and transcriptional activity.|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine; by MAP2K6|||Phosphotyrosine; by JAK|||SH2|||Signal transducer and activator of transcription 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182420|||http://purl.uniprot.org/annotation/VAR_020190|||http://purl.uniprot.org/annotation/VAR_036002|||http://purl.uniprot.org/annotation/VAR_047939
http://togogenome.org/gene/9606:CSRNP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H175                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteine/serine-rich nuclear protein 2|||Disordered|||N-acetylmethionine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114790|||http://purl.uniprot.org/annotation/VAR_053016
http://togogenome.org/gene/9606:NINJ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJR9|||http://purl.uniprot.org/uniprot/B4DJC1|||http://purl.uniprot.org/uniprot/F5H3L1|||http://purl.uniprot.org/uniprot/F8WBZ3|||http://purl.uniprot.org/uniprot/Q9NZG7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Helix alpha3|||Helical;Name=Helix alpha4|||Helix alpha1|||Helix alpha2|||Ninjurin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159646
http://togogenome.org/gene/9606:TRPV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2KYM6|||http://purl.uniprot.org/uniprot/Q8NET8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In FNEPPK2; gain of function mutation.|||In OLMS1; gain of function mutation; results in constitutive channel activation.|||In isoform 2.|||In isoform 3.|||Ion transport|||Polar residues|||Pore-forming|||Transient receptor potential cation channel subfamily V member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215345|||http://purl.uniprot.org/annotation/VAR_052388|||http://purl.uniprot.org/annotation/VAR_052389|||http://purl.uniprot.org/annotation/VAR_052390|||http://purl.uniprot.org/annotation/VAR_067920|||http://purl.uniprot.org/annotation/VAR_067921|||http://purl.uniprot.org/annotation/VAR_067922|||http://purl.uniprot.org/annotation/VAR_073832|||http://purl.uniprot.org/annotation/VSP_013433|||http://purl.uniprot.org/annotation/VSP_013434|||http://purl.uniprot.org/annotation/VSP_013435
http://togogenome.org/gene/9606:SH2D3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG32|||http://purl.uniprot.org/uniprot/Q8N5H7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Ras-GEF|||SH2|||SH2 domain-containing protein 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228833|||http://purl.uniprot.org/annotation/VAR_051352|||http://purl.uniprot.org/annotation/VSP_017706|||http://purl.uniprot.org/annotation/VSP_017707|||http://purl.uniprot.org/annotation/VSP_017708|||http://purl.uniprot.org/annotation/VSP_044581|||http://purl.uniprot.org/annotation/VSP_044582
http://togogenome.org/gene/9606:FSHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQE8|||http://purl.uniprot.org/uniprot/P01225                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Follitropin subunit beta|||Glycoprotein hormone subunit beta|||In HH24.|||Increased activation of the follicle-stimulating hormone signaling pathway.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011711|||http://purl.uniprot.org/annotation/PRO_5002521295|||http://purl.uniprot.org/annotation/VAR_012047|||http://purl.uniprot.org/annotation/VAR_033015
http://togogenome.org/gene/9606:RBMY1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEQ0|||http://purl.uniprot.org/uniprot/J3KPK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member E|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341539
http://togogenome.org/gene/9606:IDH3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50213                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Complete loss of activity of the heterotetramer, heterodimer composed of IDH3A and IDH3B subunits and the heterodimer composed of IDH3A and IDH3G subunits with no effect on their oligomeric states.|||Complete loss of the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||Critical for catalysis|||In RP90.|||In RP90; unknown pathological significance.|||In isoform 2.|||Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No significant effect on the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||Phosphothreonine|||Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate and ADP.|||Significantly impairs the activation of the heterodimer composed of IDH3A and IDH3G subunits by citrate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014436|||http://purl.uniprot.org/annotation/VAR_084723|||http://purl.uniprot.org/annotation/VAR_084724|||http://purl.uniprot.org/annotation/VAR_084725|||http://purl.uniprot.org/annotation/VAR_084726|||http://purl.uniprot.org/annotation/VAR_084727|||http://purl.uniprot.org/annotation/VAR_084728|||http://purl.uniprot.org/annotation/VAR_084729|||http://purl.uniprot.org/annotation/VAR_084730|||http://purl.uniprot.org/annotation/VSP_014516
http://togogenome.org/gene/9606:AFM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43652                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Afamin|||Albumin 1|||Albumin 2|||Albumin 3|||Binding pocket for hydrophobic ligands|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (complex) asparagine; atypical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001106|||http://purl.uniprot.org/annotation/VAR_048218|||http://purl.uniprot.org/annotation/VAR_061003
http://togogenome.org/gene/9606:ELOF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60002                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  Transcription elongation factor 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120941
http://togogenome.org/gene/9606:PFN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60673                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Profilin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199579
http://togogenome.org/gene/9606:INHBB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09529                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Inhibin beta B chain|||Interchain|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033722|||http://purl.uniprot.org/annotation/PRO_0000033723
http://togogenome.org/gene/9606:P4HTM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXG6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EF-hand 1|||EF-hand 2|||Fe2OG dioxygenase|||Helical; Signal-anchor for type II membrane protein|||In HIDEA.|||In HIDEA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Transmembrane prolyl 4-hydroxylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206668|||http://purl.uniprot.org/annotation/VAR_082950|||http://purl.uniprot.org/annotation/VAR_082951|||http://purl.uniprot.org/annotation/VSP_007573|||http://purl.uniprot.org/annotation/VSP_007574
http://togogenome.org/gene/9606:PPP2R2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63151                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Removed|||Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071415|||http://purl.uniprot.org/annotation/VSP_043100
http://togogenome.org/gene/9606:SERTAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14140                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes the interaction with XPO1 as well as the nuclear export and the subsequent proteasomal degradation.|||Disordered|||Nuclear export signal (NES)|||Polar residues|||Required for transactivation activity|||SERTA|||SERTA domain-containing protein 2|||Slight decrease of interaction with XPO1 and resistance to proteasomal degradation, no effect on nuclear export.|||Slight resistance to proteasomal degradation, no effect on the interaction with XPO1 neither on nuclear export.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191613
http://togogenome.org/gene/9606:MT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02795                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-2|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197245|||http://purl.uniprot.org/annotation/VAR_025840
http://togogenome.org/gene/9606:MBLAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2B0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Loss of endoribonuclease activity; when associated with A-169 and A-192.|||Loss of endoribonuclease activity; when associated with A-169 and A-231.|||Loss of endoribonuclease activity; when associated with A-192 and A-231.|||Metallo-beta-lactamase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337027|||http://purl.uniprot.org/annotation/VAR_043567|||http://purl.uniprot.org/annotation/VAR_043568
http://togogenome.org/gene/9606:ZNF225                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK10                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 225                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047466|||http://purl.uniprot.org/annotation/VAR_033560|||http://purl.uniprot.org/annotation/VAR_033561
http://togogenome.org/gene/9606:C1QTNF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0J259|||http://purl.uniprot.org/uniprot/P0C862                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||Basic and acidic residues|||C1q|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Complement C1q and tumor necrosis factor-related protein 9A|||Disordered|||O-linked (Gal...) hydroxylysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291751|||http://purl.uniprot.org/annotation/PRO_5017335448|||http://purl.uniprot.org/annotation/VAR_032840|||http://purl.uniprot.org/annotation/VAR_032841|||http://purl.uniprot.org/annotation/VAR_059148
http://togogenome.org/gene/9606:SPATC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0A9                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Speriolin-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079519|||http://purl.uniprot.org/annotation/VAR_059639|||http://purl.uniprot.org/annotation/VAR_059640|||http://purl.uniprot.org/annotation/VSP_039151
http://togogenome.org/gene/9606:PRPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60891                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding of phosphoribosylpyrophosphate|||In ARTS.|||In CMTX5.|||In DFNX1.|||In PRPS1 superactivity; no effect on Km; resistant to inhibition by ADP and GDP.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||No effect on catalytic activity.|||Probable disease-associated variant found in a patient with an intermediate phenotype between ARTS and PRPS1 superactivity; normal PRPP synthetase activity in fibroblasts; loss of activity in erythrocytes.|||Probable disease-associated variant found in patients with phosphoribosyl pyrophosphate synthetase I deficiency.|||Reduces catalytic activity.|||Removed|||Ribose-phosphate pyrophosphokinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141071|||http://purl.uniprot.org/annotation/VAR_004163|||http://purl.uniprot.org/annotation/VAR_004164|||http://purl.uniprot.org/annotation/VAR_016044|||http://purl.uniprot.org/annotation/VAR_016045|||http://purl.uniprot.org/annotation/VAR_016046|||http://purl.uniprot.org/annotation/VAR_016047|||http://purl.uniprot.org/annotation/VAR_036593|||http://purl.uniprot.org/annotation/VAR_036594|||http://purl.uniprot.org/annotation/VAR_036595|||http://purl.uniprot.org/annotation/VAR_036941|||http://purl.uniprot.org/annotation/VAR_036942|||http://purl.uniprot.org/annotation/VAR_036943|||http://purl.uniprot.org/annotation/VAR_036944|||http://purl.uniprot.org/annotation/VAR_063522|||http://purl.uniprot.org/annotation/VAR_063523|||http://purl.uniprot.org/annotation/VAR_063524|||http://purl.uniprot.org/annotation/VAR_063525|||http://purl.uniprot.org/annotation/VAR_072719|||http://purl.uniprot.org/annotation/VAR_078489|||http://purl.uniprot.org/annotation/VSP_056028
http://togogenome.org/gene/9606:ZNF117                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03924                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 117                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047407|||http://purl.uniprot.org/annotation/VAR_057396|||http://purl.uniprot.org/annotation/VAR_057397
http://togogenome.org/gene/9606:RBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82980                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Retinol-binding protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067400|||http://purl.uniprot.org/annotation/VAR_034445|||http://purl.uniprot.org/annotation/VAR_034446|||http://purl.uniprot.org/annotation/VAR_049013
http://togogenome.org/gene/9606:NSMCE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MF7                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  E3 SUMO-protein ligase NSE2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||Induces a strong decrease in SUMO ligase activity.|||N-acetylmethionine|||Phosphoserine|||SP-RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270939|||http://purl.uniprot.org/annotation/VAR_036327|||http://purl.uniprot.org/annotation/VAR_050537
http://togogenome.org/gene/9606:VGLL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MV65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Transcription cofactor vestigial-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324661|||http://purl.uniprot.org/annotation/VSP_052713
http://togogenome.org/gene/9606:CLDN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1I9|||http://purl.uniprot.org/uniprot/P56748                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-8|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interactions with TJP1, TJP2 and TJP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144753|||http://purl.uniprot.org/annotation/VAR_020387|||http://purl.uniprot.org/annotation/VAR_024417|||http://purl.uniprot.org/annotation/VAR_048739
http://togogenome.org/gene/9606:FBXO47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MNV8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 47|||Found in a consanguineous family with intellectual disability; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119952|||http://purl.uniprot.org/annotation/VAR_049052|||http://purl.uniprot.org/annotation/VAR_080770
http://togogenome.org/gene/9606:CELA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNI1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 1|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027677|||http://purl.uniprot.org/annotation/PRO_0000027678|||http://purl.uniprot.org/annotation/VAR_033645|||http://purl.uniprot.org/annotation/VAR_033646|||http://purl.uniprot.org/annotation/VAR_033647|||http://purl.uniprot.org/annotation/VAR_033648|||http://purl.uniprot.org/annotation/VAR_036295
http://togogenome.org/gene/9606:ZCCHC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXF8|||http://purl.uniprot.org/uniprot/A0A087WXU5|||http://purl.uniprot.org/uniprot/A0A087WYF0|||http://purl.uniprot.org/uniprot/A0A087WYV3|||http://purl.uniprot.org/uniprot/A0A0D9SEW3|||http://purl.uniprot.org/uniprot/B4DYA9|||http://purl.uniprot.org/uniprot/Q9NP64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CCHC-type|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||S1 motif|||Zinc finger CCHC domain-containing protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096902|||http://purl.uniprot.org/annotation/VSP_015308|||http://purl.uniprot.org/annotation/VSP_054531
http://togogenome.org/gene/9606:NUBPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB37|||http://purl.uniprot.org/uniprot/X5D2R5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Defect in complex I assembly; when associated with A-244.|||Defect in complex I assembly; when associated with A-247.|||In MC1DN21.|||In isoform 2.|||Iron-sulfur protein NUBPL|||Mitochondrion|||Rare variant found in a patient with mitochondrial complex I deficiency; unknown pathological significance; found in association with a nucleotide transition causing exon skipping; does not affect protein stability, processing and import in the mitochondrion; can restore complex I activity when overexpressed in patient fibroblasts.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184950|||http://purl.uniprot.org/annotation/PRO_5004954348|||http://purl.uniprot.org/annotation/VAR_027895|||http://purl.uniprot.org/annotation/VAR_064570|||http://purl.uniprot.org/annotation/VAR_069767|||http://purl.uniprot.org/annotation/VAR_069768|||http://purl.uniprot.org/annotation/VSP_008797|||http://purl.uniprot.org/annotation/VSP_020985
http://togogenome.org/gene/9606:GPR84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 84|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069589|||http://purl.uniprot.org/annotation/VAR_049397|||http://purl.uniprot.org/annotation/VAR_069393
http://togogenome.org/gene/9606:KCNN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3F2YNY5|||http://purl.uniprot.org/uniprot/Q9H2S1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Basic residues|||Calmodulin-binding|||Disordered|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In DYT34; unknown pathological significance.|||In NEDMAB.|||In NEDMAB; loss of function of homomeric channels.|||In NEDMAB; requires 2 nucleotide substitutions.|||In NEDMAB; unknown pathological significance; no effect on channel function.|||In isoform 2.|||Phosphotyrosine|||Polar residues|||Pore-forming; Name=Segment H5|||Small conductance calcium-activated potassium channel protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155010|||http://purl.uniprot.org/annotation/VAR_086742|||http://purl.uniprot.org/annotation/VAR_086743|||http://purl.uniprot.org/annotation/VAR_086744|||http://purl.uniprot.org/annotation/VAR_086745|||http://purl.uniprot.org/annotation/VAR_086746|||http://purl.uniprot.org/annotation/VAR_086747|||http://purl.uniprot.org/annotation/VAR_086748|||http://purl.uniprot.org/annotation/VAR_086749|||http://purl.uniprot.org/annotation/VAR_086750|||http://purl.uniprot.org/annotation/VAR_086751|||http://purl.uniprot.org/annotation/VSP_044584
http://togogenome.org/gene/9606:MIIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JXC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with IGFBP2|||Migration and invasion-inhibitory protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324322|||http://purl.uniprot.org/annotation/VAR_039729|||http://purl.uniprot.org/annotation/VAR_039730|||http://purl.uniprot.org/annotation/VAR_039731|||http://purl.uniprot.org/annotation/VAR_059688|||http://purl.uniprot.org/annotation/VAR_059689|||http://purl.uniprot.org/annotation/VAR_059690|||http://purl.uniprot.org/annotation/VSP_032214
http://togogenome.org/gene/9606:ZNF574                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFM2|||http://purl.uniprot.org/uniprot/Q6ZN55|||http://purl.uniprot.org/uniprot/Q71MF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15; degenerate|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 574                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274861|||http://purl.uniprot.org/annotation/VAR_030351|||http://purl.uniprot.org/annotation/VAR_030352|||http://purl.uniprot.org/annotation/VAR_052870|||http://purl.uniprot.org/annotation/VSP_022878
http://togogenome.org/gene/9606:MACO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Macoilin|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070266|||http://purl.uniprot.org/annotation/VSP_017203|||http://purl.uniprot.org/annotation/VSP_017204|||http://purl.uniprot.org/annotation/VSP_017205
http://togogenome.org/gene/9606:ABHD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFV4                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||N6-succinyllysine|||Protein ABHD11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281003|||http://purl.uniprot.org/annotation/VSP_023924|||http://purl.uniprot.org/annotation/VSP_023925|||http://purl.uniprot.org/annotation/VSP_023926|||http://purl.uniprot.org/annotation/VSP_023927|||http://purl.uniprot.org/annotation/VSP_023928|||http://purl.uniprot.org/annotation/VSP_023929|||http://purl.uniprot.org/annotation/VSP_023930|||http://purl.uniprot.org/annotation/VSP_046994
http://togogenome.org/gene/9606:CT45A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMU7|||http://purl.uniprot.org/uniprot/P0DMU8|||http://purl.uniprot.org/uniprot/P0DMV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A5|||Cancer/testis antigen family 45 member A6|||Cancer/testis antigen family 45 member A7|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308950|||http://purl.uniprot.org/annotation/PRO_0000433029|||http://purl.uniprot.org/annotation/PRO_0000433117
http://togogenome.org/gene/9606:ANXA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R657|||http://purl.uniprot.org/uniprot/P20073                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3 X 5 AA tandem repeats of G-Y-P-P-X|||Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A7|||Disordered|||In isoform 2.|||N6-acetyllysine|||Pro residues|||Repeat-rich region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067499|||http://purl.uniprot.org/annotation/VAR_048253|||http://purl.uniprot.org/annotation/VSP_011843
http://togogenome.org/gene/9606:NBAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRP1|||http://purl.uniprot.org/uniprot/G1UI26                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in a patient with a multisystem disease involving liver, eye, immune system, connective tissue and bone; unknown pathological significance.|||Found in a patient with a multisystem disease involving liver, eye, immune system, connective tissue and bone; unknown pathological significance; reduced collagen secretion, diffuse collagen bundles and reduced protein expression in fibroblasts.|||Found in a patient with a multisystem disease involving liver, eye, immune system, connective tissue and bone; unknown pathological significance; reduced protein expression levels in fibroblasts.|||In ILFS2.|||In ILFS2; unknown pathological significance.|||In SOPH; also found in patients with a multisystem disease involving liver, eye, immune system, connective tissue and bone; unknown pathological significance; reduced collagen secretion, diffuse collagen bundles and reduced protein expression in fibroblasts..|||In isoform 2.|||Interaction with USE1|||Interaction with ZW10 and RINT1|||N6-acetyllysine|||NBAS subunit of NRZ tethering complex|||Neuroblastoma-amplified sequence N-terminal|||Phosphoserine|||Probable disease-associated variant found in patients with a multisystem disease involving liver, eye, immune system, connective tissue and bone.|||Sec39|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292806|||http://purl.uniprot.org/annotation/VAR_057611|||http://purl.uniprot.org/annotation/VAR_057612|||http://purl.uniprot.org/annotation/VAR_057613|||http://purl.uniprot.org/annotation/VAR_057614|||http://purl.uniprot.org/annotation/VAR_057615|||http://purl.uniprot.org/annotation/VAR_068954|||http://purl.uniprot.org/annotation/VAR_068955|||http://purl.uniprot.org/annotation/VAR_068956|||http://purl.uniprot.org/annotation/VAR_068957|||http://purl.uniprot.org/annotation/VAR_074643|||http://purl.uniprot.org/annotation/VAR_074644|||http://purl.uniprot.org/annotation/VAR_074645|||http://purl.uniprot.org/annotation/VAR_074646|||http://purl.uniprot.org/annotation/VAR_074647|||http://purl.uniprot.org/annotation/VAR_074648|||http://purl.uniprot.org/annotation/VAR_074649|||http://purl.uniprot.org/annotation/VAR_074650|||http://purl.uniprot.org/annotation/VAR_074651|||http://purl.uniprot.org/annotation/VAR_074652|||http://purl.uniprot.org/annotation/VAR_074653|||http://purl.uniprot.org/annotation/VAR_085212|||http://purl.uniprot.org/annotation/VAR_085213|||http://purl.uniprot.org/annotation/VAR_085214|||http://purl.uniprot.org/annotation/VAR_085215|||http://purl.uniprot.org/annotation/VAR_085216|||http://purl.uniprot.org/annotation/VAR_085217|||http://purl.uniprot.org/annotation/VAR_085218|||http://purl.uniprot.org/annotation/VAR_085219|||http://purl.uniprot.org/annotation/VAR_085220|||http://purl.uniprot.org/annotation/VSP_026445
http://togogenome.org/gene/9606:PCDH15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTR6|||http://purl.uniprot.org/uniprot/A0A087WZN9|||http://purl.uniprot.org/uniprot/A0A087X1T6|||http://purl.uniprot.org/uniprot/A2A3D8|||http://purl.uniprot.org/uniprot/A2A3E6|||http://purl.uniprot.org/uniprot/A2A3E7|||http://purl.uniprot.org/uniprot/A2A3E8|||http://purl.uniprot.org/uniprot/A9Z1W1|||http://purl.uniprot.org/uniprot/E7EM53|||http://purl.uniprot.org/uniprot/Q96QU1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNB23.|||In USH1DF.|||In USH1F.|||In USH1F; benign variant.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Protocadherin-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003998|||http://purl.uniprot.org/annotation/PRO_5001831906|||http://purl.uniprot.org/annotation/PRO_5001832093|||http://purl.uniprot.org/annotation/PRO_5001832195|||http://purl.uniprot.org/annotation/PRO_5002642149|||http://purl.uniprot.org/annotation/PRO_5002642399|||http://purl.uniprot.org/annotation/PRO_5002642602|||http://purl.uniprot.org/annotation/PRO_5002642615|||http://purl.uniprot.org/annotation/PRO_5002745787|||http://purl.uniprot.org/annotation/PRO_5003219409|||http://purl.uniprot.org/annotation/VAR_024035|||http://purl.uniprot.org/annotation/VAR_024036|||http://purl.uniprot.org/annotation/VAR_024037|||http://purl.uniprot.org/annotation/VAR_024038|||http://purl.uniprot.org/annotation/VAR_028289|||http://purl.uniprot.org/annotation/VAR_028290|||http://purl.uniprot.org/annotation/VAR_028291|||http://purl.uniprot.org/annotation/VAR_028292|||http://purl.uniprot.org/annotation/VAR_069297|||http://purl.uniprot.org/annotation/VAR_071696|||http://purl.uniprot.org/annotation/VAR_071697|||http://purl.uniprot.org/annotation/VAR_071698|||http://purl.uniprot.org/annotation/VAR_079507|||http://purl.uniprot.org/annotation/VAR_082801|||http://purl.uniprot.org/annotation/VSP_028257|||http://purl.uniprot.org/annotation/VSP_028258|||http://purl.uniprot.org/annotation/VSP_028259|||http://purl.uniprot.org/annotation/VSP_028260|||http://purl.uniprot.org/annotation/VSP_046616|||http://purl.uniprot.org/annotation/VSP_046617|||http://purl.uniprot.org/annotation/VSP_046618|||http://purl.uniprot.org/annotation/VSP_046621|||http://purl.uniprot.org/annotation/VSP_046622
http://togogenome.org/gene/9606:LRRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1F6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Death|||Disordered|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 25|||LRR 26|||LRR 27|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat and death domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325804|||http://purl.uniprot.org/annotation/VSP_032412|||http://purl.uniprot.org/annotation/VSP_032413
http://togogenome.org/gene/9606:STEAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q687X5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ferric oxidoreductase|||Helical|||In isoform 2.|||Metalloreductase STEAP4|||N-linked (GlcNAc...) asparagine|||Strongly reduced enzyme activity. No effect on trimerization and on heme binding.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285174|||http://purl.uniprot.org/annotation/VAR_031976|||http://purl.uniprot.org/annotation/VAR_031977|||http://purl.uniprot.org/annotation/VSP_024833
http://togogenome.org/gene/9606:CST7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76096                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cystatin-F|||Interchain (with C-26)|||Interchain (with C-63)|||N-linked (GlcNAc...) asparagine|||Reactive site|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006646
http://togogenome.org/gene/9606:UBE3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6J8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase E3D|||HECT-like|||Interaction with UBE2C|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311190|||http://purl.uniprot.org/annotation/VAR_037152|||http://purl.uniprot.org/annotation/VAR_037153
http://togogenome.org/gene/9606:ARHGAP24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N264                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not abolish the effect on actin stress fibers but moderates its capability to induce membrane protrusions.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of function.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 24|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280473|||http://purl.uniprot.org/annotation/VSP_023711|||http://purl.uniprot.org/annotation/VSP_023712|||http://purl.uniprot.org/annotation/VSP_023713|||http://purl.uniprot.org/annotation/VSP_023714|||http://purl.uniprot.org/annotation/VSP_023715|||http://purl.uniprot.org/annotation/VSP_023716|||http://purl.uniprot.org/annotation/VSP_023717|||http://purl.uniprot.org/annotation/VSP_023718
http://togogenome.org/gene/9606:SLC25A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RBE8|||http://purl.uniprot.org/uniprot/A0A024RBH9|||http://purl.uniprot.org/uniprot/Q00325|||http://purl.uniprot.org/uniprot/Q6MZF9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In MPCD.|||In isoform B.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-methyllysine|||Phosphotyrosine|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019256|||http://purl.uniprot.org/annotation/VAR_032850|||http://purl.uniprot.org/annotation/VSP_003269
http://togogenome.org/gene/9606:BORCS8-MEF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02080                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199431|||http://purl.uniprot.org/annotation/VSP_042322
http://togogenome.org/gene/9606:CCDC126                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EE4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 126|||Disordered|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288816
http://togogenome.org/gene/9606:GFUS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC8|||http://purl.uniprot.org/uniprot/Q13630                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  GDP-L-fucose synthase|||Important for catalytic activity|||Lowers pKa of active site Tyr|||NAD-dependent epimerase/dehydratase|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174350
http://togogenome.org/gene/9606:RAD54L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K996|||http://purl.uniprot.org/uniprot/Q92698                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEGH box|||DNA repair and recombination protein RAD54-like|||Defect in homologous recombination (HR).|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In a breast cancer sample; invasive ductal.|||In a colon adenocarcinoma sample.|||In a non-Hodgkin lymphoma sample.|||Loss of acetylation.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by NEK1|||Promotes homologous recombination (HR), but causes RAD51 removal from chromatin.|||Required for chromatin remodeling, strand pairing activities and coupling of ATPase activity|||Unable to rescue the MMS-sensitive phenotype of S cerevisiae rad54delta cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074337|||http://purl.uniprot.org/annotation/VAR_019559|||http://purl.uniprot.org/annotation/VAR_019560|||http://purl.uniprot.org/annotation/VAR_019561|||http://purl.uniprot.org/annotation/VAR_019562|||http://purl.uniprot.org/annotation/VAR_055363|||http://purl.uniprot.org/annotation/VAR_055364|||http://purl.uniprot.org/annotation/VAR_055365|||http://purl.uniprot.org/annotation/VAR_055366|||http://purl.uniprot.org/annotation/VAR_055367|||http://purl.uniprot.org/annotation/VAR_055368
http://togogenome.org/gene/9606:ALG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H553                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3/1,6-mannosyltransferase ALG2|||Helical|||In CMS14; shows severely reduced expression of the mutant protein.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080260|||http://purl.uniprot.org/annotation/VAR_049351|||http://purl.uniprot.org/annotation/VAR_049352|||http://purl.uniprot.org/annotation/VAR_073332|||http://purl.uniprot.org/annotation/VSP_013188|||http://purl.uniprot.org/annotation/VSP_013189
http://togogenome.org/gene/9606:ASB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK59                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 14|||In isoform 2.|||In isoform 3.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066951|||http://purl.uniprot.org/annotation/VSP_036925|||http://purl.uniprot.org/annotation/VSP_036926|||http://purl.uniprot.org/annotation/VSP_046197|||http://purl.uniprot.org/annotation/VSP_046198
http://togogenome.org/gene/9606:IPCEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  CRAC domain|||Disordered|||In isoform IPCEF1-2.|||Interactor protein for cytohesin exchange factors 1|||PH|||Phosphoserine|||Polar residues|||Required for interaction with CYTH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326630|||http://purl.uniprot.org/annotation/VAR_042410|||http://purl.uniprot.org/annotation/VSP_032682
http://togogenome.org/gene/9606:SYT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2B2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Phosphoserine; by MAPK8|||Synaptotagmin-4|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183948|||http://purl.uniprot.org/annotation/VAR_052239|||http://purl.uniprot.org/annotation/VSP_056643
http://togogenome.org/gene/9606:PSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9F7|||http://purl.uniprot.org/uniprot/O75238|||http://purl.uniprot.org/uniprot/P11464                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014908|||http://purl.uniprot.org/annotation/PRO_5010133019|||http://purl.uniprot.org/annotation/PRO_5014091989|||http://purl.uniprot.org/annotation/VAR_056063|||http://purl.uniprot.org/annotation/VAR_056064|||http://purl.uniprot.org/annotation/VAR_056065|||http://purl.uniprot.org/annotation/VAR_056066|||http://purl.uniprot.org/annotation/VAR_056067|||http://purl.uniprot.org/annotation/VAR_056068|||http://purl.uniprot.org/annotation/VAR_056069|||http://purl.uniprot.org/annotation/VAR_056070|||http://purl.uniprot.org/annotation/VAR_056071|||http://purl.uniprot.org/annotation/VAR_056072|||http://purl.uniprot.org/annotation/VAR_059408|||http://purl.uniprot.org/annotation/VSP_002548|||http://purl.uniprot.org/annotation/VSP_002549|||http://purl.uniprot.org/annotation/VSP_002550
http://togogenome.org/gene/9606:BCCIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P287                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BRCA2 and CDKN1A-interacting protein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with BRCA2|||Interaction with CDKN1A|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249687|||http://purl.uniprot.org/annotation/VAR_046642|||http://purl.uniprot.org/annotation/VSP_020540|||http://purl.uniprot.org/annotation/VSP_020541|||http://purl.uniprot.org/annotation/VSP_042023
http://togogenome.org/gene/9606:HLA-DMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q31604|||http://purl.uniprot.org/uniprot/Q6ICR9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Ig-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5004274595|||http://purl.uniprot.org/annotation/PRO_5015097382
http://togogenome.org/gene/9606:RRAGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZM2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased RPTOR-binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Maintains GTP-bound state. Increased RPTOR-binding.|||N-acetylmethionine|||Ras-related GTP-binding protein B|||Reduced affinity for all nucleotides, but with preferential binding of GDP over GTP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239948|||http://purl.uniprot.org/annotation/VSP_052073
http://togogenome.org/gene/9606:TRMT1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXX1|||http://purl.uniprot.org/uniprot/Q7Z2T5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||TRMT1-like protein|||Trm1 methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317568|||http://purl.uniprot.org/annotation/VSP_031042|||http://purl.uniprot.org/annotation/VSP_031043
http://togogenome.org/gene/9606:FATE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969F0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  16% of the population; infertile and fertile individuals.|||Disordered|||Fetal and adult testis-expressed transcript protein|||Helical|||Impairs association with mitochondria.|||In fertile and infertile individuals.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087200|||http://purl.uniprot.org/annotation/VAR_016917|||http://purl.uniprot.org/annotation/VAR_016918|||http://purl.uniprot.org/annotation/VAR_016919
http://togogenome.org/gene/9606:STAT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4S9|||http://purl.uniprot.org/uniprot/B4DQB3|||http://purl.uniprot.org/uniprot/P42226                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the interaction with NCOA1; when associated with A-802.|||Abolishes the interaction with NCOA1; when associated with A-805.|||Disordered|||In isoform 2.|||In isoform 3.|||LXXLL motif|||N-acetylserine|||Phosphotyrosine; by JAK|||Polar residues|||Removed|||SH2|||Signal transducer and activator of transcription 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182433|||http://purl.uniprot.org/annotation/VAR_013094|||http://purl.uniprot.org/annotation/VAR_059812|||http://purl.uniprot.org/annotation/VSP_031871|||http://purl.uniprot.org/annotation/VSP_031872|||http://purl.uniprot.org/annotation/VSP_045282
http://togogenome.org/gene/9606:PTPRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EM83|||http://purl.uniprot.org/uniprot/I6L9F8|||http://purl.uniprot.org/uniprot/Q92932                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||IA-2beta60|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Involved in localization to secretory granules; interaction with CPE|||Leucine-based sorting signal|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||No effect to increase invasion, migration, and metastatic lung colonization in mice breast cancer model.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Protein-tyrosine phosphatase receptor IA-2 ectodomain|||Receptor-type tyrosine-protein phosphatase N2|||Tyrosine specific protein phosphatases|||Tyrosine-based internalization motif|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025454|||http://purl.uniprot.org/annotation/PRO_0000438088|||http://purl.uniprot.org/annotation/PRO_5003217458|||http://purl.uniprot.org/annotation/PRO_5003704249|||http://purl.uniprot.org/annotation/VAR_020302|||http://purl.uniprot.org/annotation/VAR_022015|||http://purl.uniprot.org/annotation/VAR_027955|||http://purl.uniprot.org/annotation/VAR_027956|||http://purl.uniprot.org/annotation/VAR_035648|||http://purl.uniprot.org/annotation/VAR_046301|||http://purl.uniprot.org/annotation/VAR_046302|||http://purl.uniprot.org/annotation/VSP_007779|||http://purl.uniprot.org/annotation/VSP_035264|||http://purl.uniprot.org/annotation/VSP_045032
http://togogenome.org/gene/9606:DCAKD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DPCK|||Dephospho-CoA kinase domain-containing protein|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316849|||http://purl.uniprot.org/annotation/VAR_038406|||http://purl.uniprot.org/annotation/VSP_030810|||http://purl.uniprot.org/annotation/VSP_030811
http://togogenome.org/gene/9606:CTSS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25774                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes glycosylation.|||Activation peptide|||Cathepsin S|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026313|||http://purl.uniprot.org/annotation/PRO_0000026314|||http://purl.uniprot.org/annotation/VAR_025385|||http://purl.uniprot.org/annotation/VAR_025386|||http://purl.uniprot.org/annotation/VSP_042712
http://togogenome.org/gene/9606:FRS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU20                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor receptor substrate 2|||IRS-type PTB|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine; by FGFR1|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087344|||http://purl.uniprot.org/annotation/VAR_046966|||http://purl.uniprot.org/annotation/VAR_046967
http://togogenome.org/gene/9606:IFT70A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WT1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Intraflagellar transport protein 70A|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333200|||http://purl.uniprot.org/annotation/VAR_043123|||http://purl.uniprot.org/annotation/VAR_054660
http://togogenome.org/gene/9606:CIITA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2I7|||http://purl.uniprot.org/uniprot/A0A0B4J1S1|||http://purl.uniprot.org/uniprot/P33076|||http://purl.uniprot.org/uniprot/Q66X48                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In BLS2.|||In BLS2; mild immunodeficiency; has residual MHC class II trans activation activity.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||MHC class II transactivator|||NACHT|||Polar residues|||Required for acetyltransferase activity|||Strongly reduces GTP-binding and abolishes transactivation at MHC promoters.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089241|||http://purl.uniprot.org/annotation/VAR_005127|||http://purl.uniprot.org/annotation/VAR_005128|||http://purl.uniprot.org/annotation/VAR_005129|||http://purl.uniprot.org/annotation/VAR_015551|||http://purl.uniprot.org/annotation/VAR_015552|||http://purl.uniprot.org/annotation/VAR_015553|||http://purl.uniprot.org/annotation/VAR_015554|||http://purl.uniprot.org/annotation/VAR_015555|||http://purl.uniprot.org/annotation/VAR_029270|||http://purl.uniprot.org/annotation/VAR_047907|||http://purl.uniprot.org/annotation/VAR_047908|||http://purl.uniprot.org/annotation/VAR_057711|||http://purl.uniprot.org/annotation/VAR_060104|||http://purl.uniprot.org/annotation/VSP_055099|||http://purl.uniprot.org/annotation/VSP_055100|||http://purl.uniprot.org/annotation/VSP_055101|||http://purl.uniprot.org/annotation/VSP_055102|||http://purl.uniprot.org/annotation/VSP_055103
http://togogenome.org/gene/9606:NAA38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L3Z2|||http://purl.uniprot.org/uniprot/I3L4V0|||http://purl.uniprot.org/uniprot/Q9BRA0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||N-alpha-acetyltransferase 38, NatC auxiliary subunit|||Phosphoserine|||Removed|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299155|||http://purl.uniprot.org/annotation/VAR_082914|||http://purl.uniprot.org/annotation/VSP_027566
http://togogenome.org/gene/9606:OR2AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVS5|||http://purl.uniprot.org/uniprot/Q8NGE2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150475
http://togogenome.org/gene/9606:NR2E3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8Q9|||http://purl.uniprot.org/uniprot/Q9Y5X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Associated with ESCS.|||Associated with ESCS; impairs protein folding and stability.|||Associated with autosomal recessive retinitis pigmentosa.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In ESCS.|||In ESCS; impairs protein folding and stability and hinders the ability to form stable dimers.|||In ESCS; impairs protein folding and stability.|||In ESCS; impairs protein folding.|||In RP37.|||In isoform Short.|||NR C4-type|||NR LBD|||Nuclear receptor|||Photoreceptor-specific nuclear receptor|||Polar residues|||Reduces transcription repressor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053599|||http://purl.uniprot.org/annotation/VAR_009265|||http://purl.uniprot.org/annotation/VAR_009266|||http://purl.uniprot.org/annotation/VAR_009267|||http://purl.uniprot.org/annotation/VAR_010025|||http://purl.uniprot.org/annotation/VAR_010026|||http://purl.uniprot.org/annotation/VAR_010027|||http://purl.uniprot.org/annotation/VAR_010028|||http://purl.uniprot.org/annotation/VAR_010029|||http://purl.uniprot.org/annotation/VAR_010030|||http://purl.uniprot.org/annotation/VAR_010031|||http://purl.uniprot.org/annotation/VAR_010032|||http://purl.uniprot.org/annotation/VAR_010033|||http://purl.uniprot.org/annotation/VAR_010034|||http://purl.uniprot.org/annotation/VAR_010035|||http://purl.uniprot.org/annotation/VAR_010036|||http://purl.uniprot.org/annotation/VAR_020839|||http://purl.uniprot.org/annotation/VAR_020840|||http://purl.uniprot.org/annotation/VAR_020841|||http://purl.uniprot.org/annotation/VAR_020842|||http://purl.uniprot.org/annotation/VAR_020843|||http://purl.uniprot.org/annotation/VAR_037026|||http://purl.uniprot.org/annotation/VAR_062768|||http://purl.uniprot.org/annotation/VAR_062769|||http://purl.uniprot.org/annotation/VAR_062770|||http://purl.uniprot.org/annotation/VAR_062771|||http://purl.uniprot.org/annotation/VAR_062772|||http://purl.uniprot.org/annotation/VSP_003679
http://togogenome.org/gene/9606:TAS2R10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082238|||http://purl.uniprot.org/annotation/VAR_030009
http://togogenome.org/gene/9606:ARMCX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1M9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||Armadillo repeat-containing X-linked protein 5|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191371
http://togogenome.org/gene/9606:KDM4E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||JmjC|||JmjN|||Lysine-specific demethylase 4E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395404|||http://purl.uniprot.org/annotation/VAR_063402|||http://purl.uniprot.org/annotation/VAR_063403|||http://purl.uniprot.org/annotation/VAR_063404|||http://purl.uniprot.org/annotation/VAR_063405
http://togogenome.org/gene/9606:PCDH11Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70LR4|||http://purl.uniprot.org/uniprot/Q9BZA8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Protocadherin-11 Y-linked                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232764|||http://purl.uniprot.org/annotation/VAR_026020|||http://purl.uniprot.org/annotation/VAR_026021|||http://purl.uniprot.org/annotation/VAR_048576|||http://purl.uniprot.org/annotation/VSP_017996|||http://purl.uniprot.org/annotation/VSP_017997|||http://purl.uniprot.org/annotation/VSP_017998|||http://purl.uniprot.org/annotation/VSP_017999|||http://purl.uniprot.org/annotation/VSP_018000
http://togogenome.org/gene/9606:ZNF629                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UEG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger protein 629                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280426|||http://purl.uniprot.org/annotation/VAR_052883
http://togogenome.org/gene/9606:CASP8AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||CASP8-associated protein 2|||Disordered|||N-acetylalanine|||N6-acetyllysine|||NCOA2-binding|||Phosphoserine|||Polar residues|||Removed|||SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates|||SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates|||SUMO interaction motif 3 (SIM); mediates the binding to polysumoylated substrates                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076188|||http://purl.uniprot.org/annotation/VAR_050700
http://togogenome.org/gene/9606:TAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D299|||http://purl.uniprot.org/uniprot/P49848                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ALYUS; decreased interaction with TAF1 and TBP shown by functional expression studies in a Drosophila cell line.|||In ALYUS; decreased interaction with TAF1, TAF9 and TBP shown by functional expression studies in a Drosophila cell line.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||TATA box binding protein associated factor (TAF) histone-like fold|||Transcription initiation factor TFIID subunit 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118873|||http://purl.uniprot.org/annotation/VAR_014349|||http://purl.uniprot.org/annotation/VAR_077840|||http://purl.uniprot.org/annotation/VAR_077841|||http://purl.uniprot.org/annotation/VSP_037476|||http://purl.uniprot.org/annotation/VSP_043709|||http://purl.uniprot.org/annotation/VSP_059851
http://togogenome.org/gene/9606:NAGK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6G7|||http://purl.uniprot.org/uniprot/C9JEV6|||http://purl.uniprot.org/uniprot/Q9UJ70                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase BadF/BadG/BcrA/BcrD type|||Abolished ability to phosphorylate muramyl dipeptide.|||In isoform 2.|||N-acetyl-D-glucosamine kinase|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096696|||http://purl.uniprot.org/annotation/VAR_029763|||http://purl.uniprot.org/annotation/VAR_029764|||http://purl.uniprot.org/annotation/VSP_044586
http://togogenome.org/gene/9606:LTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSL2|||http://purl.uniprot.org/uniprot/E7ER44|||http://purl.uniprot.org/uniprot/P02788|||http://purl.uniprot.org/uniprot/Q2TUW9|||http://purl.uniprot.org/uniprot/V9HWI4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to heparin, lipid A, lysozyme and DNA.|||Almost no protease activity.|||Associated with lower plasma lactoferrin concentrations.|||Bactericidal and antifungal activity|||Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding|||Decreased antibacterial activity against Gram-positive bacteria; seems to reduce susceptibility to localized juvenile periodontitis; associated with increased plasma lactoferrin concentrations and possibly with susceptibility to coronary artery stenosis.|||Destabilizes iron binding significantly.|||Destabilizes iron binding slightly.|||Destabilizes iron binding.|||Disrupts anion binding site and destabilizes iron binding.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly impairs binding to heparin, lipid A, lysozyme and DNA. Impairs antibacterial activity.|||Impairs binding to heparin, lipid A, lysozyme and DNA.|||Impairs iron binding and changes domain closure.|||Important for full bactericidal and antifungal activities|||Important for iron binding|||In isoform DeltaLf.|||Interaction with PspA|||Interaction with lipopolysaccharide|||Involved in glycosaminoglycan binding|||Kaliocin-1|||Lactoferricin-H|||Lactoferroxin-A|||Lactoferroxin-B|||Lactoferroxin-C|||Lactotransferrin|||N-linked (GlcNAc...) asparagine|||No effect.|||No protease activity.|||Nucleophile|||O-linked (GlcNAc) serine; alternate|||Phosphoserine; alternate|||Transferrin-like|||Transferrin-like 1|||Transferrin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035732|||http://purl.uniprot.org/annotation/PRO_0000035733|||http://purl.uniprot.org/annotation/PRO_0000035734|||http://purl.uniprot.org/annotation/PRO_0000035735|||http://purl.uniprot.org/annotation/PRO_0000035736|||http://purl.uniprot.org/annotation/PRO_0000422770|||http://purl.uniprot.org/annotation/PRO_5003217500|||http://purl.uniprot.org/annotation/PRO_5004216633|||http://purl.uniprot.org/annotation/PRO_5004777100|||http://purl.uniprot.org/annotation/VAR_013504|||http://purl.uniprot.org/annotation/VAR_013505|||http://purl.uniprot.org/annotation/VAR_013506|||http://purl.uniprot.org/annotation/VAR_013507|||http://purl.uniprot.org/annotation/VAR_013508|||http://purl.uniprot.org/annotation/VAR_069298|||http://purl.uniprot.org/annotation/VSP_044308
http://togogenome.org/gene/9606:LPIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92539                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  C-LIP|||DXDXT motif|||Disordered|||In MJDS.|||LXXIL motif|||N-LIP|||Nuclear localization signal|||Phosphatidate phosphatase LPIN2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209881|||http://purl.uniprot.org/annotation/VAR_023817
http://togogenome.org/gene/9606:IQGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VI3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calponin-homology (CH)|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||Phosphoserine|||Phosphotyrosine|||Ras GTPase-activating-like protein IQGAP3|||Ras-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056651|||http://purl.uniprot.org/annotation/VAR_055278|||http://purl.uniprot.org/annotation/VAR_055279|||http://purl.uniprot.org/annotation/VAR_055280|||http://purl.uniprot.org/annotation/VAR_055281|||http://purl.uniprot.org/annotation/VAR_055282|||http://purl.uniprot.org/annotation/VAR_055283|||http://purl.uniprot.org/annotation/VAR_055284
http://togogenome.org/gene/9606:CAMKMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z624                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-lysine N-methyltransferase|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300115|||http://purl.uniprot.org/annotation/VSP_027784|||http://purl.uniprot.org/annotation/VSP_027785
http://togogenome.org/gene/9606:KBTBD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94819                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch repeat and BTB domain-containing protein 11|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119090
http://togogenome.org/gene/9606:SPAG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R06                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-111, A974 and A-978.|||Decreased phosphorylation by GSK3-beta. Partial loss of spindle association; when associated with A-937, A974 and A-978.|||Decreased phosphorylation by GSK3-beta; when associated with A-978. Partial loss of spindle association; when associated with A-111, A937 and A-978.|||Decreased phosphorylation by GSK3-beta; when associated with A-97A. Partial loss of spindle association; when associated with A-111, A-937 and A-974.|||Disordered|||Interaction with KNSTRN|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Polar residues|||Sperm-associated antigen 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072093
http://togogenome.org/gene/9606:CLSTN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4D0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cadherin 1|||Cadherin 2|||Calsyntenin-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004023|||http://purl.uniprot.org/annotation/VAR_036112|||http://purl.uniprot.org/annotation/VAR_036113|||http://purl.uniprot.org/annotation/VAR_039557|||http://purl.uniprot.org/annotation/VAR_055615
http://togogenome.org/gene/9606:TOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NM4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HMG box|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Nuclear localization signal|||Polar residues|||Required for transcriptional activation|||TOX high mobility group box family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048571|||http://purl.uniprot.org/annotation/VAR_049560|||http://purl.uniprot.org/annotation/VSP_002187|||http://purl.uniprot.org/annotation/VSP_045645|||http://purl.uniprot.org/annotation/VSP_047108
http://togogenome.org/gene/9606:ADSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30566|||http://purl.uniprot.org/uniprot/X5D8S6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylosuccinate lyase|||Adenylosuccinate lyase C-terminal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In ADSLD; mild.|||In ADSLD; mild; strongly reduced activity with SAMP, but only slightly reduced activity with SAICAR; abolishes cooperativity.|||In ADSLD; moderate.|||In ADSLD; moderate; strongly reduced catalytic activity.|||In ADSLD; severe.|||In ADSLD; severe; abolishes cooperativity and reduces enzyme activity.|||In ADSLD; severe; most frequent mutation.|||In ADSLD; severe; reduces protein stability.|||In ADSLD; severe; slightly reduced enzyme activity.|||In ADSLD; severe; total loss of activity.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Proton donor/acceptor|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137892|||http://purl.uniprot.org/annotation/VAR_000680|||http://purl.uniprot.org/annotation/VAR_007972|||http://purl.uniprot.org/annotation/VAR_007973|||http://purl.uniprot.org/annotation/VAR_007974|||http://purl.uniprot.org/annotation/VAR_007975|||http://purl.uniprot.org/annotation/VAR_007976|||http://purl.uniprot.org/annotation/VAR_007977|||http://purl.uniprot.org/annotation/VAR_007978|||http://purl.uniprot.org/annotation/VAR_016930|||http://purl.uniprot.org/annotation/VAR_016931|||http://purl.uniprot.org/annotation/VAR_016932|||http://purl.uniprot.org/annotation/VAR_017078|||http://purl.uniprot.org/annotation/VAR_017079|||http://purl.uniprot.org/annotation/VAR_017080|||http://purl.uniprot.org/annotation/VAR_017081|||http://purl.uniprot.org/annotation/VAR_017082|||http://purl.uniprot.org/annotation/VAR_017083|||http://purl.uniprot.org/annotation/VAR_017084|||http://purl.uniprot.org/annotation/VAR_017085|||http://purl.uniprot.org/annotation/VAR_017086|||http://purl.uniprot.org/annotation/VAR_017087|||http://purl.uniprot.org/annotation/VAR_017088|||http://purl.uniprot.org/annotation/VAR_017089|||http://purl.uniprot.org/annotation/VAR_017090|||http://purl.uniprot.org/annotation/VAR_017091|||http://purl.uniprot.org/annotation/VAR_017092|||http://purl.uniprot.org/annotation/VAR_017093|||http://purl.uniprot.org/annotation/VAR_037883|||http://purl.uniprot.org/annotation/VAR_037884|||http://purl.uniprot.org/annotation/VSP_000318
http://togogenome.org/gene/9606:SDHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RFM5|||http://purl.uniprot.org/uniprot/P31040                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  FAD-dependent oxidoreductase 2 FAD binding|||Fumarate reductase/succinate dehydrogenase flavoprotein-like C-terminal|||In LS.|||In LS; decrease in succinate dehydrogenase activity.|||In MC2DN1 and CMD1GG.|||In MC2DN1; unknown pathological significance.|||In NDAXOA.|||In PGL5; loss of activity.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphotyrosine; by SRC|||Proton acceptor|||Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial|||Tele-8alpha-FAD histidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010335|||http://purl.uniprot.org/annotation/VAR_002449|||http://purl.uniprot.org/annotation/VAR_016878|||http://purl.uniprot.org/annotation/VAR_016879|||http://purl.uniprot.org/annotation/VAR_049214|||http://purl.uniprot.org/annotation/VAR_049215|||http://purl.uniprot.org/annotation/VAR_049216|||http://purl.uniprot.org/annotation/VAR_049217|||http://purl.uniprot.org/annotation/VAR_059307|||http://purl.uniprot.org/annotation/VAR_065975|||http://purl.uniprot.org/annotation/VAR_071037|||http://purl.uniprot.org/annotation/VAR_074022|||http://purl.uniprot.org/annotation/VAR_085396|||http://purl.uniprot.org/annotation/VAR_085397|||http://purl.uniprot.org/annotation/VAR_085584|||http://purl.uniprot.org/annotation/VSP_055077|||http://purl.uniprot.org/annotation/VSP_055078
http://togogenome.org/gene/9606:ATP6V1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEY4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||V-type proton ATPase subunit C 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285669|||http://purl.uniprot.org/annotation/VAR_032041|||http://purl.uniprot.org/annotation/VSP_024883
http://togogenome.org/gene/9606:SCN9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15858                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  13-fold less blocked by the spider huwentoxin-IV, 3-fold less inhibited by the spider protoxin-II, and has a significant impact on channel activation by shifiting the V(50) towart 0 mV when targeted by protoxin-II.|||18-fold less blocked by the spider huwentoxin-IV.|||19-fold less blocked by the spider huwentoxin-IV.|||4-fold less inhibited by the spider protoxin-II.|||400-fold less blocked by the spider huwentoxin-IV.|||5-fold less blocked by the spider huwentoxin-IV.|||5-fold less inhibited by the spider protoxin-II.|||8-fold less inhibited by the spider protoxin-II.|||9-fold less inhibited by the spider protoxin-II.|||Abolishes stimulation by agents that stimulate PKC activity.|||Basic and acidic residues|||Cytoplasmic|||Decrease of the inhibition of fast inactivation produced by the scorpion alpha-toxin CvIV4 on this channel.|||Depolarizes the voltage-dependence of steady-state fast inactivation; enhances persistent current.|||Disordered|||Extracellular|||Found in a patient with febrile seizures; unknown pathological significance.|||Found in a patient with severe myoclonic epilepsy in infancy; unknown pathological significance.|||Found in patients with febrile seizures plus; unknown pathological significance.|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||Hyperpolarizes the voltage dependence of activation by 10.6 mV and prolonges fast-inactivation duration when coexpressed with SCN1B and SCN2B.|||I|||II|||III|||IQ|||IV|||Important increase in inhibition by saxitoxin and little increase in inhibition by tetrodotoxin.|||In CIP; significant reduction in membrane localization of the mutant protein compared to the wild-type; complete loss of function of the sodium channel.|||In PERYTHM and PEXPD; hyperpolarizes voltage-dependence of channel activation; depolarizes the voltage-dependence of steady-state fast inactivation; slows channel deactivation; enhances persistent and resurgent current; enhances neuronal hyperexcitability in dorsal root ganglion neurons.|||In PERYTHM.|||In PERYTHM; activated at more negative potentials; slower inactivation kinetics than wild-type channels.|||In PERYTHM; causes a hyperpolarizing shift in channel activation, a depolarizing shift of inactivation and an 18-fold increase in deactivation time compared to wild-type; the mean ramp current amplitude in response to slow depolarization is higher in the mutant channels.|||In PERYTHM; causes a hyperpolarizing shift of -5.3 mV for the midpoint of activation which is smaller than that seen in other mutations causing early-onset erythromelalgia mutations; also causes a faster rate of activation and slower deactivation compared to wild-type; expression of the mutant protein induced hyperexcitability in dorsal root ganglion neurons but the increase is smaller than that produced by Thr-859.|||In PERYTHM; hyperpolarizes the voltage dependence of activation by 11 mV, accelerates activation, slows deactivation and enhances the response to slow, small depolarizations.|||In PERYTHM; no effect on voltage-dependence of channel activation; depolarizes the voltage dependence of steady-state fast inactivation; accelerates channel deactivation; no increase in persistent and resurgent currents; enhances neuronal hyperexcitability in dorsal root ganglion neurons.|||In PERYTHM; produces a hyperpolarizing shift in channel activation and a depolarizing shift in steady-state activation.|||In PERYTHM; sporadic; activated at more negative potentials; slower inactivation kinetics than wild-type channels.|||In PEXPD.|||In PEXPD; depolarizes the voltage-dependence of channel activation and steady-state fast inactivation; increases ramp current.|||In PEXPD; reduction in fast inactivation leading to persistent sodium current.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Increases current amplitude.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||Is directly targeted by the spider protoxin-II|||Less inhibited by the spider protoxin-II.|||N-linked (GlcNAc...) asparagine|||No change in inhibition (IC(50)) by the spider protoxin-II, but has a significant impact on channel activation by shifiting the V(50) towart 0 mV when targeted by protoxin-II.|||No change in inhibition by the spider protoxin-II.|||No effect on voltage-dependence of steady-state fast inactivation.|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Sodium channel protein type 9 subunit alpha ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048502|||http://purl.uniprot.org/annotation/VAR_019947|||http://purl.uniprot.org/annotation/VAR_019948|||http://purl.uniprot.org/annotation/VAR_019949|||http://purl.uniprot.org/annotation/VAR_019950|||http://purl.uniprot.org/annotation/VAR_030444|||http://purl.uniprot.org/annotation/VAR_032014|||http://purl.uniprot.org/annotation/VAR_032015|||http://purl.uniprot.org/annotation/VAR_032016|||http://purl.uniprot.org/annotation/VAR_032017|||http://purl.uniprot.org/annotation/VAR_032018|||http://purl.uniprot.org/annotation/VAR_032019|||http://purl.uniprot.org/annotation/VAR_032020|||http://purl.uniprot.org/annotation/VAR_032021|||http://purl.uniprot.org/annotation/VAR_032022|||http://purl.uniprot.org/annotation/VAR_032023|||http://purl.uniprot.org/annotation/VAR_055646|||http://purl.uniprot.org/annotation/VAR_064595|||http://purl.uniprot.org/annotation/VAR_064596|||http://purl.uniprot.org/annotation/VAR_064597|||http://purl.uniprot.org/annotation/VAR_064598|||http://purl.uniprot.org/annotation/VAR_064599|||http://purl.uniprot.org/annotation/VAR_064600|||http://purl.uniprot.org/annotation/VAR_064602|||http://purl.uniprot.org/annotation/VAR_064603|||http://purl.uniprot.org/annotation/VAR_064604|||http://purl.uniprot.org/annotation/VAR_064605|||http://purl.uniprot.org/annotation/VAR_064606|||http://purl.uniprot.org/annotation/VAR_064607|||http://purl.uniprot.org/annotation/VAR_064608|||http://purl.uniprot.org/annotation/VAR_064609|||http://purl.uniprot.org/annotation/VAR_064610|||http://purl.uniprot.org/annotation/VAR_064611|||http://purl.uniprot.org/annotation/VAR_064612|||http://purl.uniprot.org/annotation/VAR_064613|||http://purl.uniprot.org/annotation/VAR_064614|||http://purl.uniprot.org/annotation/VAR_072279|||http://purl.uniprot.org/annotation/VAR_072280|||http://purl.uniprot.org/annotation/VAR_072281|||http://purl.uniprot.org/annotation/VSP_012028|||http://purl.uniprot.org/annotation/VSP_012029
http://togogenome.org/gene/9606:CAPN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHC0|||http://purl.uniprot.org/uniprot/B1B154                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-8|||Domain III|||EF-hand 1|||EF-hand 2|||EF-hand 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349280
http://togogenome.org/gene/9606:HMGN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05114|||http://purl.uniprot.org/uniprot/Q6NSG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mass|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylserine|||ADP-ribosylserine; alternate|||Basic and acidic residues|||Disordered|||In RNA edited version.|||N6-acetyllysine|||Non-histone chromosomal protein HMG-14|||Phosphoserine|||Phosphoserine; alternate; by RPS6KA5|||Phosphoserine; by RPS6KA5|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206691|||http://purl.uniprot.org/annotation/VAR_054790
http://togogenome.org/gene/9606:DLG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDM6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disks large homolog 5|||Disordered|||Guanylate kinase-like|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094564|||http://purl.uniprot.org/annotation/VAR_027897|||http://purl.uniprot.org/annotation/VAR_027898|||http://purl.uniprot.org/annotation/VAR_027899|||http://purl.uniprot.org/annotation/VSP_016349|||http://purl.uniprot.org/annotation/VSP_027197|||http://purl.uniprot.org/annotation/VSP_027198|||http://purl.uniprot.org/annotation/VSP_027199|||http://purl.uniprot.org/annotation/VSP_027200|||http://purl.uniprot.org/annotation/VSP_027201
http://togogenome.org/gene/9606:ERFE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0M1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  C1q|||Disordered|||Erythroferrone|||Hydroxyproline|||N-linked (GlcNAc...) asparagine|||Required for correct protein folding in the endoplasmic reticulum                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340250
http://togogenome.org/gene/9606:RIC8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPQ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Synembryn-A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235890|||http://purl.uniprot.org/annotation/VSP_018507|||http://purl.uniprot.org/annotation/VSP_018508|||http://purl.uniprot.org/annotation/VSP_039849
http://togogenome.org/gene/9606:USP17L8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Inactive ubiquitin carboxyl-terminal hydrolase 17-like protein 8|||Polar residues|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331650
http://togogenome.org/gene/9606:TSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NL82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bms1-type G|||Disordered|||Pre-rRNA-processing protein TSR1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311274|||http://purl.uniprot.org/annotation/VAR_037211|||http://purl.uniprot.org/annotation/VAR_037212|||http://purl.uniprot.org/annotation/VAR_037213|||http://purl.uniprot.org/annotation/VAR_037214
http://togogenome.org/gene/9606:CSH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6C2|||http://purl.uniprot.org/uniprot/P0DML2|||http://purl.uniprot.org/uniprot/P0DML3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chorionic somatomammotropin hormone 1|||Chorionic somatomammotropin hormone 2|||In isoform 2.|||In isoform 3.|||In monomeric form|||Interchain (with C-208); in dimeric form|||Interchain (with C-215); in dimeric form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032958|||http://purl.uniprot.org/annotation/PRO_0000429797|||http://purl.uniprot.org/annotation/PRO_5014297542|||http://purl.uniprot.org/annotation/VAR_007167|||http://purl.uniprot.org/annotation/VSP_055244|||http://purl.uniprot.org/annotation/VSP_055245
http://togogenome.org/gene/9606:NR2C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2YGU2|||http://purl.uniprot.org/uniprot/P49116                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 2 group C member 2|||Phosphoserine|||Phosphoserine; by MAPK|||Reduces interaction with JAZF1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053588|||http://purl.uniprot.org/annotation/VSP_039522
http://togogenome.org/gene/9606:FAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5L6|||http://purl.uniprot.org/uniprot/P16930                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Does not cause a clinically relevant phenotype; results in lower enzyme activity.|||Fumarylacetoacetase|||Fumarylacetoacetase N-terminal|||Fumarylacetoacetase-like C-terminal|||In TYRSN1.|||In TYRSN1; atypical mild phenotype.|||In TYRSN1; loss of activity.|||In TYRSN1; may affect splicing resulting in skipping of exon 8 alone or together with exon 9; lower activity as compared to wild type.|||In TYRSN1; requires 2 nucleotide substitutions.|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156825|||http://purl.uniprot.org/annotation/VAR_005205|||http://purl.uniprot.org/annotation/VAR_005206|||http://purl.uniprot.org/annotation/VAR_005207|||http://purl.uniprot.org/annotation/VAR_005208|||http://purl.uniprot.org/annotation/VAR_005209|||http://purl.uniprot.org/annotation/VAR_005210|||http://purl.uniprot.org/annotation/VAR_005211|||http://purl.uniprot.org/annotation/VAR_005212|||http://purl.uniprot.org/annotation/VAR_005213|||http://purl.uniprot.org/annotation/VAR_005214|||http://purl.uniprot.org/annotation/VAR_005215|||http://purl.uniprot.org/annotation/VAR_005216|||http://purl.uniprot.org/annotation/VAR_005217|||http://purl.uniprot.org/annotation/VAR_005218|||http://purl.uniprot.org/annotation/VAR_005219|||http://purl.uniprot.org/annotation/VAR_005220|||http://purl.uniprot.org/annotation/VAR_005221|||http://purl.uniprot.org/annotation/VAR_005222|||http://purl.uniprot.org/annotation/VAR_005223|||http://purl.uniprot.org/annotation/VAR_005224|||http://purl.uniprot.org/annotation/VAR_065454|||http://purl.uniprot.org/annotation/VAR_065455|||http://purl.uniprot.org/annotation/VSP_055491
http://togogenome.org/gene/9606:ZNF442                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7R0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Found in a renal cell carcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 442                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047591|||http://purl.uniprot.org/annotation/VAR_024217|||http://purl.uniprot.org/annotation/VAR_024218|||http://purl.uniprot.org/annotation/VAR_035581|||http://purl.uniprot.org/annotation/VAR_035582|||http://purl.uniprot.org/annotation/VAR_052830|||http://purl.uniprot.org/annotation/VAR_052831|||http://purl.uniprot.org/annotation/VAR_064763|||http://purl.uniprot.org/annotation/VSP_055953
http://togogenome.org/gene/9606:CCT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78371                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||T-complex protein 1 subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128316|||http://purl.uniprot.org/annotation/VSP_042648
http://togogenome.org/gene/9606:SSBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWW4|||http://purl.uniprot.org/uniprot/Q9NW25                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||LisH|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Single-stranded DNA-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123828|||http://purl.uniprot.org/annotation/VSP_006260|||http://purl.uniprot.org/annotation/VSP_006261
http://togogenome.org/gene/9606:SYMPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92797                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes stimulation of SSU72 phosphatase activity.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In isoform 2.|||Interaction with HSF1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Symplekin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072385|||http://purl.uniprot.org/annotation/VSP_014842|||http://purl.uniprot.org/annotation/VSP_014843
http://togogenome.org/gene/9606:NRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2Y5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CNH|||Disordered|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Nik-related protein kinase|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250511|||http://purl.uniprot.org/annotation/VAR_033908|||http://purl.uniprot.org/annotation/VAR_033909|||http://purl.uniprot.org/annotation/VAR_040951|||http://purl.uniprot.org/annotation/VAR_040952|||http://purl.uniprot.org/annotation/VAR_040953|||http://purl.uniprot.org/annotation/VAR_040954|||http://purl.uniprot.org/annotation/VAR_040955|||http://purl.uniprot.org/annotation/VAR_040956|||http://purl.uniprot.org/annotation/VAR_040957|||http://purl.uniprot.org/annotation/VAR_040958|||http://purl.uniprot.org/annotation/VAR_040959|||http://purl.uniprot.org/annotation/VAR_040960|||http://purl.uniprot.org/annotation/VAR_040961|||http://purl.uniprot.org/annotation/VAR_040962|||http://purl.uniprot.org/annotation/VAR_051653|||http://purl.uniprot.org/annotation/VSP_020654|||http://purl.uniprot.org/annotation/VSP_020655|||http://purl.uniprot.org/annotation/VSP_020656|||http://purl.uniprot.org/annotation/VSP_020657
http://togogenome.org/gene/9606:SCRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWW7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; atypical|||Disordered|||SNAG domain|||Transcriptional repressor scratch 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047036|||http://purl.uniprot.org/annotation/VAR_045990
http://togogenome.org/gene/9606:TMEM120B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PK00                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 120B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309529
http://togogenome.org/gene/9606:RPS19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39019                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DBA1.|||In DBA1; affects assembly into a functional ribosomal subunit.|||In DBA1; affects protein stability; does not localize to the nucleolus.|||In DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit.|||In DBA1; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit.|||In DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit.|||N6-acetyllysine|||N6-succinyllysine|||Omega-N-methylarginine|||Removed|||Small ribosomal subunit protein eS19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153810|||http://purl.uniprot.org/annotation/VAR_006924|||http://purl.uniprot.org/annotation/VAR_018437|||http://purl.uniprot.org/annotation/VAR_018438|||http://purl.uniprot.org/annotation/VAR_018439|||http://purl.uniprot.org/annotation/VAR_018440|||http://purl.uniprot.org/annotation/VAR_018441|||http://purl.uniprot.org/annotation/VAR_018442|||http://purl.uniprot.org/annotation/VAR_018443|||http://purl.uniprot.org/annotation/VAR_018444|||http://purl.uniprot.org/annotation/VAR_018445|||http://purl.uniprot.org/annotation/VAR_018446|||http://purl.uniprot.org/annotation/VAR_018447|||http://purl.uniprot.org/annotation/VAR_046145|||http://purl.uniprot.org/annotation/VAR_046146|||http://purl.uniprot.org/annotation/VAR_046147|||http://purl.uniprot.org/annotation/VAR_046148|||http://purl.uniprot.org/annotation/VAR_046149|||http://purl.uniprot.org/annotation/VAR_055436|||http://purl.uniprot.org/annotation/VAR_055437|||http://purl.uniprot.org/annotation/VAR_055438|||http://purl.uniprot.org/annotation/VAR_055439|||http://purl.uniprot.org/annotation/VAR_055440|||http://purl.uniprot.org/annotation/VAR_055441|||http://purl.uniprot.org/annotation/VAR_055442|||http://purl.uniprot.org/annotation/VAR_055443|||http://purl.uniprot.org/annotation/VAR_055444|||http://purl.uniprot.org/annotation/VAR_055445
http://togogenome.org/gene/9606:FAM151B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXP7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM151B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317105|||http://purl.uniprot.org/annotation/VAR_053992
http://togogenome.org/gene/9606:MAP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Microtubule-associated protein 10|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050794
http://togogenome.org/gene/9606:C17orf100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MU93                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein C17orf100                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340708
http://togogenome.org/gene/9606:LRRC14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHZ5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 14B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344240
http://togogenome.org/gene/9606:GAS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60861                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||F-BAR|||Growth arrest-specific protein 7|||In isoform 1.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Polar residues|||SH3|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076057|||http://purl.uniprot.org/annotation/VSP_006802|||http://purl.uniprot.org/annotation/VSP_006803|||http://purl.uniprot.org/annotation/VSP_035988|||http://purl.uniprot.org/annotation/VSP_044294|||http://purl.uniprot.org/annotation/VSP_044295
http://togogenome.org/gene/9606:CHEK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT73|||http://purl.uniprot.org/uniprot/E7EPP6|||http://purl.uniprot.org/uniprot/O14757                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes kinase activity.|||Abrogates interaction with RAD51; when associated with A-317. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Impairs interaction with YWHAZ which is required for nuclear retention after checkpoint activation.|||Abrogates interaction with RAD51; when associated with A-345. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Abrogates nuclear retention upon checkpoint activation. Impairs interaction with FBXO6.|||Autoinhibitory region|||Disordered|||Enhances interaction with RAD51; when associated with E-317.|||Enhances interaction with RAD51; when associated with E-345.|||Enhances stability of the protein, probably by preventing ubiquitination at this site.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs nuclear export.|||In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-376.|||In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-379.|||In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-376 and E-379.|||In isoform 2.|||In isoform 3.|||Interaction with CLSPN|||No effect on phosphorylation induced by hydroxyurea.|||Phosphoserine|||Phosphoserine; by ATM and ATR|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Chk1|||Strong reduction of chromatin-associated CHK1 ubiquitination.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085848|||http://purl.uniprot.org/annotation/VAR_021123|||http://purl.uniprot.org/annotation/VAR_024571|||http://purl.uniprot.org/annotation/VAR_040407|||http://purl.uniprot.org/annotation/VAR_040408|||http://purl.uniprot.org/annotation/VSP_044008|||http://purl.uniprot.org/annotation/VSP_044009|||http://purl.uniprot.org/annotation/VSP_045075
http://togogenome.org/gene/9606:TMEM98                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In NNO4.|||Required for interaction with MYRF|||Transmembrane protein 98                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251711|||http://purl.uniprot.org/annotation/VAR_051451|||http://purl.uniprot.org/annotation/VAR_071807|||http://purl.uniprot.org/annotation/VAR_081643
http://togogenome.org/gene/9606:PRKAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43741                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'-AMP-activated protein kinase subunit beta-2|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphoserine; by ULK1|||Phosphothreonine|||Results in an AMPK enzyme that is activable by phosphorylation but has significantly increased rate of dephosphorylation in phosphatase assays.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204368|||http://purl.uniprot.org/annotation/VSP_055820|||http://purl.uniprot.org/annotation/VSP_055821
http://togogenome.org/gene/9606:ALPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7C7|||http://purl.uniprot.org/uniprot/P05187                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alkaline phosphatase|||Alkaline phosphatase, placental type|||Disordered|||GPI-anchor amidated aspartate|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine intermediate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024031|||http://purl.uniprot.org/annotation/PRO_0000024032|||http://purl.uniprot.org/annotation/PRO_5002781810|||http://purl.uniprot.org/annotation/VAR_017419|||http://purl.uniprot.org/annotation/VAR_050520|||http://purl.uniprot.org/annotation/VAR_050521|||http://purl.uniprot.org/annotation/VAR_050522|||http://purl.uniprot.org/annotation/VAR_050523
http://togogenome.org/gene/9606:IL1RL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01638                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Flexible linker|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 4.|||In isoform B and isoform 4.|||In isoform C.|||Interleukin-1 receptor-like 1|||N-linked (GlcNAc...) asparagine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015442|||http://purl.uniprot.org/annotation/VAR_023749|||http://purl.uniprot.org/annotation/VAR_053373|||http://purl.uniprot.org/annotation/VAR_053374|||http://purl.uniprot.org/annotation/VAR_053375|||http://purl.uniprot.org/annotation/VAR_053376|||http://purl.uniprot.org/annotation/VAR_053377|||http://purl.uniprot.org/annotation/VSP_002664|||http://purl.uniprot.org/annotation/VSP_002665|||http://purl.uniprot.org/annotation/VSP_002666|||http://purl.uniprot.org/annotation/VSP_002667|||http://purl.uniprot.org/annotation/VSP_054933
http://togogenome.org/gene/9606:MRPL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWU5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein uL22m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261644|||http://purl.uniprot.org/annotation/VAR_029471|||http://purl.uniprot.org/annotation/VSP_021745|||http://purl.uniprot.org/annotation/VSP_044501
http://togogenome.org/gene/9606:HDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19113                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Histidine decarboxylase|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Loss of enzyme activity.|||N6-(pyridoxal phosphate)lysine|||Strongly decreases affinity for histidine. Strongly increases affinity for L-DOPA and confers enzyme activity toward L-DOPA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146950|||http://purl.uniprot.org/annotation/VAR_033846|||http://purl.uniprot.org/annotation/VAR_036470|||http://purl.uniprot.org/annotation/VAR_036471|||http://purl.uniprot.org/annotation/VAR_048873|||http://purl.uniprot.org/annotation/VAR_048874|||http://purl.uniprot.org/annotation/VSP_056296
http://togogenome.org/gene/9606:GNB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAV0                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Guanine nucleotide-binding protein subunit beta-4|||In CMTDIF; the mutant protein has impaired bradykinin-induced G-protein-coupled receptor intracellular signaling compared to the wild-type protein.|||N-acetylserine|||Phosphohistidine|||Phosphoserine|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127702|||http://purl.uniprot.org/annotation/VAR_069908|||http://purl.uniprot.org/annotation/VAR_069909
http://togogenome.org/gene/9606:ARHGAP42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI28                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BAR|||Disordered|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Rho GTPase-activating protein 42|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342407
http://togogenome.org/gene/9606:SLC25A41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5S1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Mitochondrial carrier protein SCaMC-3L|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319990|||http://purl.uniprot.org/annotation/VAR_050132|||http://purl.uniprot.org/annotation/VAR_050133|||http://purl.uniprot.org/annotation/VSP_035524|||http://purl.uniprot.org/annotation/VSP_052690
http://togogenome.org/gene/9606:PLAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DJT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes single and double sumoylation; nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-263 and R-353.|||Activates transcription; Inhibition of nuclear import due to lack of NLS and KPNA2 interaction|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Decreased nuclear import with localization in the nucleus but also in the cytoplasm|||Decreases sumoylation; Abolishes double sumoylation only; Nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-353.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||Inhibition of KPNA2 interaction when mutation occurs in the NLS; decreased nuclear import with localization in the nucleus but also in the cytoplasm; Complete inhibition of nuclear import when associated with a lack of zinc-finger domains.|||Interaction with KPNA2|||Massively activates transcription|||No effect on sumoylation. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-263.|||No effect on transcription activation capacity.|||No inhibition of KPNA2 interaction and no change in nuclear import.|||Nuclear localization signal|||Polar residues|||Prevents formation of functional zinc-finger 3; induces drastic decrease of DNA affinity and complete modification of DNA binding specificity.|||Prevents formation of functional zinc-finger 7 and inhibits DNA binding; No proliferation and transformation of cultured cells.|||Repression domain; contains 3 sumoylation motifs and massively decrease transcription activity|||Zinc finger protein PLAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295107|||http://purl.uniprot.org/annotation/VAR_033212|||http://purl.uniprot.org/annotation/VSP_045183
http://togogenome.org/gene/9606:ZPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75312                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C4-type 1|||C4-type 2|||Disordered|||In GKAF; unknown pathological significance; homozygous patient fibroblasts have impaired ability to progress through the cell cycle; decreased protein abundance in patient fibroblasts.|||Pro residues|||Zinc finger protein ZPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119036|||http://purl.uniprot.org/annotation/VAR_052999|||http://purl.uniprot.org/annotation/VAR_085794
http://togogenome.org/gene/9606:ABCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZC7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 2|||Abolishes methylation by N6AMT1.|||Basic and acidic residues|||Disordered|||Helical|||In IDPOGSA.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||N5-methylglutamine|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093290|||http://purl.uniprot.org/annotation/VAR_044526|||http://purl.uniprot.org/annotation/VAR_044527|||http://purl.uniprot.org/annotation/VAR_082138|||http://purl.uniprot.org/annotation/VSP_035283|||http://purl.uniprot.org/annotation/VSP_035284|||http://purl.uniprot.org/annotation/VSP_040937|||http://purl.uniprot.org/annotation/VSP_060910
http://togogenome.org/gene/9606:HES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14469                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Orange|||Polar residues|||Pro residues|||Transcription factor HES-1|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127202
http://togogenome.org/gene/9606:DEPDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2C3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEP|||DEP domain-containing protein 4|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284783|||http://purl.uniprot.org/annotation/VAR_031815|||http://purl.uniprot.org/annotation/VSP_024646|||http://purl.uniprot.org/annotation/VSP_024647
http://togogenome.org/gene/9606:WNK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished serine/threonine-protein kinase activity without affecting ability to regulate localization of SLC12A9.|||Basic and acidic residues|||Catalytically inactive form. Inhibits sodium-coupled chloride cotransporters and activates potassium-coupled chloride cotransporters.|||Disordered|||Impaired interaction with KLHL3.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 3 and isoform 2.|||In isoform 3 and isoform 4.|||Interaction with KLHL3|||Mimics phosphorylation, leading to decreased interaction with KLHL3 and subsequent ubiquitination.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase WNK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086823|||http://purl.uniprot.org/annotation/VAR_041323|||http://purl.uniprot.org/annotation/VAR_041324|||http://purl.uniprot.org/annotation/VAR_041325|||http://purl.uniprot.org/annotation/VAR_041326|||http://purl.uniprot.org/annotation/VAR_041327|||http://purl.uniprot.org/annotation/VAR_041328|||http://purl.uniprot.org/annotation/VAR_041329|||http://purl.uniprot.org/annotation/VSP_041932|||http://purl.uniprot.org/annotation/VSP_041933
http://togogenome.org/gene/9606:DYRK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43781                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to the nucleus, leading to impaired dissolution of nuclear speckles during mitosis.|||Decreased stability of the protein.|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 3|||In isoform 2.|||Kinase dead; Induces formation of stress granules-like in absence of stress. Impaired dissolution of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material.|||Nuclear localization signal|||Phosphomimetic mutant; increased stability of the protein.|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085938|||http://purl.uniprot.org/annotation/VAR_040464|||http://purl.uniprot.org/annotation/VSP_026178|||http://purl.uniprot.org/annotation/VSP_026179
http://togogenome.org/gene/9606:EMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15006                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Decreased interaction with EMC3.|||Decreased interaction with EMC5 and EMC8.|||Decreased transmembrane domain binding of tail-anchored proteins.|||ER membrane protein complex subunit 2|||Loss of interaction with EMC5 and EMC8.|||Loss of interaction with EMC5.|||N-acetylalanine|||N6-acetyllysine|||No effect on transmembrane domain binding of tail-anchored proteins.|||No effect on transmembrane domain binding of tail-anchored proteins; when associated with K-61 and E-122.|||No effect on transmembrane domain binding of tail-anchored proteins; when associated with K-61 and K-95.|||No effect on transmembrane domain binding of tail-anchored proteins; when associated with K-95 and E-122.|||Removed|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106353
http://togogenome.org/gene/9606:OPRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZI09|||http://purl.uniprot.org/uniprot/P41145                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Kappa-type opioid receptor|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069967|||http://purl.uniprot.org/annotation/VAR_028067|||http://purl.uniprot.org/annotation/VSP_055313
http://togogenome.org/gene/9606:JPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z682|||http://purl.uniprot.org/uniprot/Q86VR1|||http://purl.uniprot.org/uniprot/Q9HDC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||Junctophilin-1|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159844|||http://purl.uniprot.org/annotation/VAR_053445|||http://purl.uniprot.org/annotation/VAR_053446
http://togogenome.org/gene/9606:ERO1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Abolishes phosphorylation. Does not affect interaction with ERP44.|||Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB.|||Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94.|||Alternate|||Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131.|||Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB.|||ERO1-like protein alpha|||Increased catalytical activity.|||Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99.|||Induces a decrease in activity.|||Loss of regulatory disulfide bond formation and increased activity towards P4HB. Loss of regulatory disulfide bond formation and strongly increased activity towards P4HB; when associated with A-85. Loss of regulatory disulfide bond formation, strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-104.|||N-linked (GlcNAc...) asparagine|||No effect on activity.|||No effect.|||No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131.|||Phosphomimetic mutant. Does not affect interaction with ERP44. Shows two-fold increase in enzyme activity. Accelerates immunoglobulin folding.|||Phosphoserine|||Phosphoserine; by FAM20C|||Redox-active|||Redox-active; alternate|||Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008415
http://togogenome.org/gene/9606:SPTSSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969W0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Serine palmitoyltransferase small subunit A|||Within the serine palmitoyltransferase (SPT) complex, defines the length of the acyl chain-binding pocket, determining the acyl-CoA substrate preference|||Within the serine palmitoyltransferase (SPT) complex, leads to a strong decrease in SPT catalytic activity with L-serine and palmitoyl-CoA as substrates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089949
http://togogenome.org/gene/9606:TMX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1E5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Redox-active|||Thioredoxin|||Thioredoxin-related transmembrane protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034191|||http://purl.uniprot.org/annotation/VAR_052578|||http://purl.uniprot.org/annotation/VAR_052579
http://togogenome.org/gene/9606:NF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21359                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||CRAL-TRIO|||Disordered|||Found in mismatch repair deficient cancer cells; also found in a cutaneous neurofibroma from a patient with neurofibromatosis; somatic mutation.|||In FSNF; no cafe-au-lait macules; null mutation; 50% reduction of protein level.|||In NF1 and NFNS; significant reduction of intrinsic GAP activity.|||In NF1 and mismatch repair deficient cancer cells.|||In NF1.|||In NF1; affects splicing by creating a novel splice acceptor site.|||In NF1; complete loss of GAP activity.|||In NF1; most patients carrying the mutation do not manifest cutaneous neurofibromas.|||In NF1; patient with cafe-au-lait spots; may be a distinct form of NF1.|||In NF1; reduced splicing enhancement.|||In NF1; reduces protein stability.|||In NF1; significant reduction of GAP activity.|||In NF1; sporadic.|||In NF1; unknown pathological significance.|||In NF1; with neurofibromatous neuropathy.|||In NFNS.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a cutaneous neurofibroma from a patient with neurofibromatosis; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform I and isoform 6.|||In mismatch repair deficient cancer cells.|||Lipid binding|||N-acetylalanine|||Neurofibromin|||Neurofibromin truncated|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras-GAP|||Reduces phospholipid binding; when associated with A-1691; A-169 and A-1769.|||Reduces phospholipid binding; when associated with A-1691; A-1695 and A-1771.|||Reduces phospholipid binding; when associated with A-1691; A-1769 and A-1771.|||Reduces phospholipid binding; when associated with A-1695; A-1769 and A-1771.|||Reduces protein stability.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010773|||http://purl.uniprot.org/annotation/PRO_0000010774|||http://purl.uniprot.org/annotation/VAR_002653|||http://purl.uniprot.org/annotation/VAR_002654|||http://purl.uniprot.org/annotation/VAR_002655|||http://purl.uniprot.org/annotation/VAR_002656|||http://purl.uniprot.org/annotation/VAR_002657|||http://purl.uniprot.org/annotation/VAR_002658|||http://purl.uniprot.org/annotation/VAR_002659|||http://purl.uniprot.org/annotation/VAR_002660|||http://purl.uniprot.org/annotation/VAR_002661|||http://purl.uniprot.org/annotation/VAR_002662|||http://purl.uniprot.org/annotation/VAR_002663|||http://purl.uniprot.org/annotation/VAR_002664|||http://purl.uniprot.org/annotation/VAR_002665|||http://purl.uniprot.org/annotation/VAR_002666|||http://purl.uniprot.org/annotation/VAR_002667|||http://purl.uniprot.org/annotation/VAR_008129|||http://purl.uniprot.org/annotation/VAR_010989|||http://purl.uniprot.org/annotation/VAR_010990|||http://purl.uniprot.org/annotation/VAR_010991|||http://purl.uniprot.org/annotation/VAR_010992|||http://purl.uniprot.org/annotation/VAR_010993|||http://purl.uniprot.org/annotation/VAR_010994|||http://purl.uniprot.org/annotation/VAR_010995|||http://purl.uniprot.org/annotation/VAR_010996|||http://purl.uniprot.org/annotation/VAR_010997|||http://purl.uniprot.org/annotation/VAR_010998|||http://purl.uniprot.org/annotation/VAR_017550|||http://purl.uniprot.org/annotation/VAR_017551|||http://purl.uniprot.org/annotation/VAR_017552|||http://purl.uniprot.org/annotation/VAR_017553|||http://purl.uniprot.org/annotation/VAR_017554|||http://purl.uniprot.org/annotation/VAR_017555|||http://purl.uniprot.org/annotation/VAR_017669|||http://purl.uniprot.org/annotation/VAR_021730|||http://purl.uniprot.org/annotation/VAR_021731|||http://purl.uniprot.org/annotation/VAR_021732|||http://purl.uniprot.org/annotation/VAR_021733|||http://purl.uniprot.org/annotation/VAR_021734|||http://purl.uniprot.org/annotation/VAR_021735|||http://purl.uniprot.org/annotation/VAR_021736|||http://purl.uniprot.org/annotation/VAR_021737|||http://purl.uniprot.org/annotation/VAR_021738|||http://purl.uniprot.org/annotation/VAR_021739|||http://purl.uniprot.org/annotation/VAR_021740|||http://purl.uniprot.org/annotation/VAR_021741|||http://purl.uniprot.org/annotation/VAR_021742|||http://purl.uniprot.org/annotation/VAR_021743|||http://purl.uniprot.org/annotation/VAR_021744|||http://purl.uniprot.org/annotation/VAR_021745|||http://purl.uniprot.org/annotation/VAR_021746|||http://purl.uniprot.org/annotation/VAR_021747|||http://purl.uniprot.org/annotation/VAR_021748|||http://purl.uniprot.org/annotation/VAR_021749|||http://purl.uniprot.org/annotation/VAR_021750|||http://purl.uniprot.org/annotation/VAR_021751|||http://purl.uniprot.org/annotation/VAR_021752|||http://purl.uniprot.org/annotation/VAR_021753|||http://purl.uniprot.org/annotation/VAR_021754|||http://purl.uniprot.org/annotation/VAR_021755|||http://purl.uniprot.org/annotation/VAR_021756|||http://purl.uniprot.org/annotation/VAR_021757|||http://purl.uniprot.org/annotation/VAR_021758|||http://purl.uniprot.org/annotation/VAR_021759|||http://purl.uniprot.org/annotation/VAR_021760|||http://purl.uniprot.org/annotation/VAR_021761|||http://purl.uniprot.org/annotation/VAR_021762|||http://purl.uniprot.org/annotation/VAR_021763|||http://purl.uniprot.org/annotation/VAR_021764|||http://purl.uniprot.org/annotation/VAR_021765|||http://purl.uniprot.org/annotation/VAR_021766|||http://purl.uniprot.org/annotation/VAR_022254|||http://purl.uniprot.org/annotation/VAR_022255|||http://purl.uniprot.org/annotation/VAR_022256|||http://purl.uniprot.org/annotation/VAR_022257|||http://purl.uniprot.org/annotation/VAR_032459|||http://purl.uniprot.org/annotation/VAR_032460|||http://purl.uniprot.org/annotation/VAR_032461|||http://purl.uniprot.org/annotation/VAR_032462|||http://purl.uniprot.org/annotation/VAR_032463|||http://purl.uniprot.org/annotation/VAR_032464|||http://purl.uniprot.org/annotation/VAR_032465|||http://purl.uniprot.org/annotation/VAR_032466|||http://purl.uniprot.org/annotation/VAR_032467|||http://purl.uniprot.org/annotation/VAR_032468|||http://purl.uniprot.org/annotation/VAR_032469|||http://purl.uniprot.org/annotation/VAR_032470|||http://purl.uniprot.org/annotation/VAR_032471|||http://purl.uniprot.org/annotation/VAR_032472|||http://purl.uniprot.org/annotation/VAR_032473|||http://purl.uniprot.org/annotation/VAR_032474|||http://purl.uniprot.org/annotation/VAR_032475|||http://purl.uniprot.org/annotation/VAR_032476|||http://purl.uniprot.org/annotation/VAR_032477|||http://purl.uniprot.org/annotation/VAR_035543|||http://purl.uniprot.org/annotation/VAR_035544|||http://purl.uniprot.org/annotation/VAR_035545|||http://purl.uniprot.org/annotation/VAR_049135|||http://purl.uniprot.org/annotation/VAR_065236|||http://purl.uniprot.org/annotation/VAR_065888|||http://purl.uniprot.org/annotation/VAR_067201|||http://purl.uniprot.org/annotation/VAR_067202|||http://purl.uniprot.org/annotation/VAR_067203|||http://purl.uniprot.org/annotation/VAR_067204|||http://purl.uniprot.org/annotation/VAR_067205|||http://purl.uniprot.org/annotation/VAR_067206|||http://purl.uniprot.org/annotation/VAR_071668|||http://purl.uniprot.org/annotation/VAR_071669|||http://purl.uniprot.org/annotation/VAR_071670|||http://purl.uniprot.org/annotation/VAR_071671|||http://purl.uniprot.org/annotation/VAR_082822|||http://purl.uniprot.org/annotation/VAR_082823|||http://purl.uniprot.org/annotation/VSP_001628|||http://purl.uniprot.org/annotation/VSP_001629|||http://purl.uniprot.org/annotation/VSP_001630|||http://purl.uniprot.org/annotation/VSP_001631|||http://purl.uniprot.org/annotation/VSP_001632|||http://purl.uniprot.org/annotation/VSP_043467|||http://purl.uniprot.org/annotation/VSP_043468|||http://purl.uniprot.org/annotation/VSP_053587
http://togogenome.org/gene/9606:TRIM74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UV6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||In isoform 2.|||RING-type|||Tripartite motif-containing protein 74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056279|||http://purl.uniprot.org/annotation/VAR_039576|||http://purl.uniprot.org/annotation/VSP_032087
http://togogenome.org/gene/9606:INKA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Inka box|||PAK4-inhibitor INKA2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304994
http://togogenome.org/gene/9606:ZNG1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y5V3|||http://purl.uniprot.org/uniprot/Q4V339                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region                                                                                  ^@                                                                                  CXCC motif|||CobW C-terminal|||Disordered|||Zinc-regulated GTPase metalloprotein activator 1F|||psi-PxLVp motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316774
http://togogenome.org/gene/9606:PER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15534                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||CRY binding domain|||Disordered|||Found in a patient with Moyamoya disease; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with BTRC|||LXXLL|||No effect on interaction with BTRC and FBXW11.|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear export signal 3|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Period circadian protein homolog 1|||Phosphoserine|||Phosphoserine; by CSNK1E|||Phosphothreonine; by CSNK1E|||Polar residues|||Pro residues|||Required for phosphorylation by CSNK1E|||Strongly decreases interaction with BTRC and FBXW11 and inhibits degradation promoted by CSNK1E.|||Strongly decreases interaction with BTRC and FBXW11.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162627|||http://purl.uniprot.org/annotation/VAR_036038|||http://purl.uniprot.org/annotation/VAR_036039|||http://purl.uniprot.org/annotation/VAR_036040|||http://purl.uniprot.org/annotation/VAR_047899|||http://purl.uniprot.org/annotation/VAR_047900|||http://purl.uniprot.org/annotation/VAR_079176|||http://purl.uniprot.org/annotation/VSP_056205|||http://purl.uniprot.org/annotation/VSP_056206|||http://purl.uniprot.org/annotation/VSP_056207
http://togogenome.org/gene/9606:CCER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L3R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing glutamate-rich protein 2|||Disordered|||Found in patients with Moyamoya disease; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425553|||http://purl.uniprot.org/annotation/VAR_079159|||http://purl.uniprot.org/annotation/VAR_079160|||http://purl.uniprot.org/annotation/VAR_079161|||http://purl.uniprot.org/annotation/VAR_079162|||http://purl.uniprot.org/annotation/VAR_079163|||http://purl.uniprot.org/annotation/VAR_079164|||http://purl.uniprot.org/annotation/VAR_079165|||http://purl.uniprot.org/annotation/VAR_079166|||http://purl.uniprot.org/annotation/VAR_079167|||http://purl.uniprot.org/annotation/VAR_079168|||http://purl.uniprot.org/annotation/VAR_079169|||http://purl.uniprot.org/annotation/VAR_079170|||http://purl.uniprot.org/annotation/VAR_079171|||http://purl.uniprot.org/annotation/VAR_079172
http://togogenome.org/gene/9606:TCF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ75|||http://purl.uniprot.org/uniprot/P36402                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CTNNB1-binding|||Disordered|||HMG box|||In isoform 1L and isoform 1S.|||In isoform 1S, isoform 2S, isoform 3S, isoform 4S, isoform 5S, isoform 6S, isoform 7S and isoform 8S.|||In isoform 2L and isoform 2S.|||In isoform 3L and isoform 3S.|||In isoform 5L and isoform 5S.|||In isoform 6L and isoform 6S.|||In isoform 7L and isoform 7S.|||In isoform 8L and isoform 8S.|||Nuclear localization signal|||Polar residues|||Pro residues|||Transcription factor 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048612|||http://purl.uniprot.org/annotation/VSP_002191|||http://purl.uniprot.org/annotation/VSP_002192|||http://purl.uniprot.org/annotation/VSP_006960|||http://purl.uniprot.org/annotation/VSP_006961|||http://purl.uniprot.org/annotation/VSP_012160|||http://purl.uniprot.org/annotation/VSP_012161|||http://purl.uniprot.org/annotation/VSP_012162|||http://purl.uniprot.org/annotation/VSP_012163
http://togogenome.org/gene/9606:CIMIP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43247                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule inner protein 4|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086902|||http://purl.uniprot.org/annotation/VSP_028351
http://togogenome.org/gene/9606:OPHN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0Z4E9|||http://purl.uniprot.org/uniprot/O60890                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MRXSBL.|||In isoform 2.|||Oligophrenin-1|||PH|||Pro residues|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056760|||http://purl.uniprot.org/annotation/VAR_013638|||http://purl.uniprot.org/annotation/VAR_013639|||http://purl.uniprot.org/annotation/VAR_033452|||http://purl.uniprot.org/annotation/VAR_061184|||http://purl.uniprot.org/annotation/VAR_066746|||http://purl.uniprot.org/annotation/VSP_055336|||http://purl.uniprot.org/annotation/VSP_055337
http://togogenome.org/gene/9606:HTATIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUP3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Highly associated with hepatocellular carcinoma (HCC) progression.|||In a hepatocellular carcinoma sample.|||In a hepatocellular carcinoma sample; reduces protein stability.|||In isoform 2.|||In isoform 3.|||Loss of association with nucleus.|||Loss of proapoptotic and metastatis-inhibiting effect.|||N-acetylalanine|||Oxidoreductase HTATIP2|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072544|||http://purl.uniprot.org/annotation/VAR_023713|||http://purl.uniprot.org/annotation/VAR_023714|||http://purl.uniprot.org/annotation/VAR_023715|||http://purl.uniprot.org/annotation/VAR_023716|||http://purl.uniprot.org/annotation/VAR_023717|||http://purl.uniprot.org/annotation/VAR_023718|||http://purl.uniprot.org/annotation/VSP_038339|||http://purl.uniprot.org/annotation/VSP_051864|||http://purl.uniprot.org/annotation/VSP_051865
http://togogenome.org/gene/9606:ADH1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07327                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Alcohol dehydrogenase 1A|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160658
http://togogenome.org/gene/9606:ZKSCAN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MAY2|||http://purl.uniprot.org/uniprot/C9J6L6|||http://purl.uniprot.org/uniprot/Q0VAP0|||http://purl.uniprot.org/uniprot/Q9P0L1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Polar residues|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047437|||http://purl.uniprot.org/annotation/VAR_052782|||http://purl.uniprot.org/annotation/VAR_052783|||http://purl.uniprot.org/annotation/VAR_052784|||http://purl.uniprot.org/annotation/VAR_052785|||http://purl.uniprot.org/annotation/VAR_052786|||http://purl.uniprot.org/annotation/VAR_052787|||http://purl.uniprot.org/annotation/VAR_052788|||http://purl.uniprot.org/annotation/VSP_011955|||http://purl.uniprot.org/annotation/VSP_011956
http://togogenome.org/gene/9606:WNT9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EPC3|||http://purl.uniprot.org/uniprot/O14905                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt|||Protein Wnt-9b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041458|||http://purl.uniprot.org/annotation/PRO_5014088878|||http://purl.uniprot.org/annotation/VAR_030839
http://togogenome.org/gene/9606:FUBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDX9|||http://purl.uniprot.org/uniprot/B4DT31|||http://purl.uniprot.org/uniprot/Q96AE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Far upstream element-binding protein 1|||In isoform 2.|||K Homology|||KH 1|||KH 2|||KH 3|||KH 4|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050135|||http://purl.uniprot.org/annotation/VAR_049679|||http://purl.uniprot.org/annotation/VSP_008321|||http://purl.uniprot.org/annotation/VSP_021107
http://togogenome.org/gene/9606:MAP4K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92918                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CNH|||Disordered|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Mitogen-activated protein kinase kinase kinase kinase 1|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor|||Retains kinase activity. Not degraded by the Cul7-RING ubiquitin-protein ligase complex containing FBXW8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086273|||http://purl.uniprot.org/annotation/VAR_040739|||http://purl.uniprot.org/annotation/VAR_040740|||http://purl.uniprot.org/annotation/VAR_040741|||http://purl.uniprot.org/annotation/VAR_040742|||http://purl.uniprot.org/annotation/VAR_051643|||http://purl.uniprot.org/annotation/VSP_040340
http://togogenome.org/gene/9606:GNMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5F2|||http://purl.uniprot.org/uniprot/Q14749|||http://purl.uniprot.org/uniprot/V9HW60                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycine N-methyltransferase|||In GNMT deficiency; 0.5% wild-type glycine N-methyltransferase activity.|||In GNMT deficiency; 10% wild-type glycine N-methyltransferase activity.|||In GNMT deficiency; 75% wild-type glycine N-methyltransferase activity, decreases stability of the tetramer.|||Methyltransferase|||N-acetylvaline|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087524|||http://purl.uniprot.org/annotation/VAR_012766|||http://purl.uniprot.org/annotation/VAR_012767|||http://purl.uniprot.org/annotation/VAR_019840
http://togogenome.org/gene/9606:RANBP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||CTLH|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with CALB1|||Interaction with FMR1|||LisH|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues|||Ran-binding protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097169|||http://purl.uniprot.org/annotation/VSP_013175|||http://purl.uniprot.org/annotation/VSP_056049
http://togogenome.org/gene/9606:CNGA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV77                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cyclic nucleotide-gated cation channel alpha-4|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||IQ-type|||In isoform 2.|||Loss of inhibition produced by calcium/calmodulin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317107|||http://purl.uniprot.org/annotation/VAR_038480|||http://purl.uniprot.org/annotation/VSP_039919|||http://purl.uniprot.org/annotation/VSP_039920|||http://purl.uniprot.org/annotation/VSP_039921
http://togogenome.org/gene/9606:RYR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92736                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X approximate repeats|||Abolishes phosphorylation by PKA.|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Basic and acidic residues|||Changed ryanodine-sensitive calcium-release channel activity characterized by increased sensitivity to cytosolic calcium activation.|||Cytoplasmic|||Decreased function in release of sequestered calcium ion into cytosol by sarcoplasmic reticulum. Changed ryanodine-sensitive calcium-release channel activity. Mutant channels are less resposive to activation by caffeine and store calcium overload. Affects channel sensitivity to cytosolic and luminal calcium activation.|||Disordered|||Found in a patient with short-coupled polymorphic ventricular tachycardia at rest; unknown pathological significance; no effect on cytosolic Ca(2+) activation.|||Helical|||In CPVT1.|||In CPVT1; changed ryanodine-sensitive calcium-release channel activity; increased sensitivity to cytosolic calcium activation.|||In CPVT1; decreases protein stability.|||In CPVT1; unknown pathological significance.|||In VACRDS; decreased function in release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; changed ryanodine-sensitive calcium-release channel activity; diminishes the response to activation by luminal Ca(2+) but has little effect on the sensitivity of the channel to activation by cytosolic Ca(2+); shows caffeine-induced Ca(2+) release but exhibits no store-overload-induced Ca(2+) release (SOICR); HL1 cardiac cells transfected with the G-4860 mutant displayed attenuated SOICR activity compared to cells transfected with wild-type RYR2.|||In VACRDS; decreased function in release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; changed ryanodine-sensitive calcium-release channel activity; mutant channels are less responsive to activation by caffeine and store calcium overload; affects channel sensitivity to cytosolic and luminal calcium activation.|||In VACRDS; decreased function in release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; changed ryanodine-sensitive calcium-release channel activity; mutant channels are less resposive to activation by caffeine and store calcium overload; affects channel sensitivity to cytosolic and luminal calcium activation.|||In isoform 2.|||Interaction with CALM|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Phosphoserine|||Phosphoserine; by CaMK2D|||Phosphoserine; by CaMK2D and PKA|||Phosphoserine; by PKA|||Pore-forming|||Probable disease-associated variant found in a patient with intellectual disability, seizures, short stature and severe atrial arrhythmias.|||Ryanodine receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219361|||http://purl.uniprot.org/annotation/VAR_011395|||http://purl.uniprot.org/annotation/VAR_011396|||http://purl.uniprot.org/annotation/VAR_011397|||http://purl.uniprot.org/annotation/VAR_011398|||http://purl.uniprot.org/annotation/VAR_011399|||http://purl.uniprot.org/annotation/VAR_011400|||http://purl.uniprot.org/annotation/VAR_011401|||http://purl.uniprot.org/annotation/VAR_011402|||http://purl.uniprot.org/annotation/VAR_011403|||http://purl.uniprot.org/annotation/VAR_011590|||http://purl.uniprot.org/annotation/VAR_022078|||http://purl.uniprot.org/annotation/VAR_023694|||http://purl.uniprot.org/annotation/VAR_023695|||http://purl.uniprot.org/annotation/VAR_023696|||http://purl.uniprot.org/annotation/VAR_044086|||http://purl.uniprot.org/annotation/VAR_044087|||http://purl.uniprot.org/annotation/VAR_044088|||http://purl.uniprot.org/annotation/VAR_044089|||http://purl.uniprot.org/annotation/VAR_044090|||http://purl.uniprot.org/annotation/VAR_044091|||http://purl.uniprot.org/annotation/VAR_044092|||http://purl.uniprot.org/annotation/VAR_044093|||http://purl.uniprot.org/annotation/VAR_044094|||http://purl.uniprot.org/annotation/VAR_044095|||http://purl.uniprot.org/annotation/VAR_044096|||http://purl.uniprot.org/annotation/VAR_044097|||http://purl.uniprot.org/annotation/VAR_044098|||http://purl.uniprot.org/annotation/VAR_044099|||http://purl.uniprot.org/annotation/VAR_044100|||http://purl.uniprot.org/annotation/VAR_044101|||http://purl.uniprot.org/annotation/VAR_044102|||http://purl.uniprot.org/annotation/VAR_044103|||http://purl.uniprot.org/annotation/VAR_044104|||http://purl.uniprot.org/annotation/VAR_044105|||http://purl.uniprot.org/annotation/VAR_044106|||http://purl.uniprot.org/annotation/VAR_044107|||http://purl.uniprot.org/annotation/VAR_044108|||http://purl.uniprot.org/annotation/VAR_044109|||http://purl.uniprot.org/annotation/VAR_044110|||http://purl.uniprot.org/annotation/VAR_044111|||http://purl.uniprot.org/annotation/VAR_044112|||http://purl.uniprot.org/annotation/VAR_044113|||http://purl.uniprot.org/annotation/VAR_075283|||http://purl.uniprot.org/annotation/VAR_078648|||http://purl.uniprot.org/annotation/VAR_079513|||http://purl.uniprot.org/annotation/VAR_079514|||http://purl.uniprot.org/annotation/VAR_079515|||http://purl.uniprot.org/annotation/VAR_079516|||http://purl.uniprot.org/annotation/VAR_079517|||http://purl.uniprot.org/annotation/VAR_085649|||http://purl.uniprot.org/annotation/VAR_085650|||http://purl.uniprot.org/annotation/VAR_085651|||http://purl.uniprot.org/annotation/VAR_085652|||http://purl.uniprot.org/annotation/VSP_005953
http://togogenome.org/gene/9606:OR10AD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGE0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10AD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150691|||http://purl.uniprot.org/annotation/VAR_024125|||http://purl.uniprot.org/annotation/VAR_053267|||http://purl.uniprot.org/annotation/VAR_053268|||http://purl.uniprot.org/annotation/VAR_053269
http://togogenome.org/gene/9606:KLK13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1R3UCE9|||http://purl.uniprot.org/uniprot/Q5BQ99|||http://purl.uniprot.org/uniprot/Q86VI7|||http://purl.uniprot.org/uniprot/Q9UKR3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Kallikrein-13|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027957|||http://purl.uniprot.org/annotation/PRO_5010221827|||http://purl.uniprot.org/annotation/PRO_5014105553|||http://purl.uniprot.org/annotation/PRO_5014107235|||http://purl.uniprot.org/annotation/VAR_051857|||http://purl.uniprot.org/annotation/VSP_056631
http://togogenome.org/gene/9606:PCDHA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Polar residues|||Protocadherin alpha-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003888|||http://purl.uniprot.org/annotation/VAR_021874|||http://purl.uniprot.org/annotation/VAR_021875|||http://purl.uniprot.org/annotation/VAR_048524|||http://purl.uniprot.org/annotation/VAR_048525|||http://purl.uniprot.org/annotation/VAR_061060|||http://purl.uniprot.org/annotation/VSP_000675|||http://purl.uniprot.org/annotation/VSP_000676
http://togogenome.org/gene/9606:MYO1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12965|||http://purl.uniprot.org/uniprot/Q4KMR3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In FSGS6.|||In FSGS6; loss of microfilament motor activity; results in altered clathrin-coated vesicle dynamics when expressed in a heterolgous system; no effect on localization to cell-cell junctions and clathrin-coated vesicles.|||In FSGS6; results in altered clathrin-coated vesicle dynamics when expressed in a heterolgous system; severely decreased localization to cell-cell junctions and clathrin-coated vesicles.|||In FSGS6; the mutant shows diffuse cytosolic localization with a punctate pattern.|||Myosin motor|||Phosphoserine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a patient with steroid-resistant nephrotic syndrome.|||Probable disease-associated variant found in a patient with steroid-resistant, minimal change nephrotic syndrome.|||SH3|||TH1|||Unconventional myosin-Ie                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123450|||http://purl.uniprot.org/annotation/VAR_065958|||http://purl.uniprot.org/annotation/VAR_065959|||http://purl.uniprot.org/annotation/VAR_065960|||http://purl.uniprot.org/annotation/VAR_065961|||http://purl.uniprot.org/annotation/VAR_065962|||http://purl.uniprot.org/annotation/VAR_081166|||http://purl.uniprot.org/annotation/VAR_087568|||http://purl.uniprot.org/annotation/VAR_087569|||http://purl.uniprot.org/annotation/VAR_087570|||http://purl.uniprot.org/annotation/VAR_087571|||http://purl.uniprot.org/annotation/VAR_087572
http://togogenome.org/gene/9606:TNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01375|||http://purl.uniprot.org/uniprot/Q5STB3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished myristoylation.|||Biologically inactive.|||C-domain 1|||C-domain 2|||Cleavage; by ADAM17|||Cleavage; by SPPL2A or SPPL2B|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||Intracellular domain 1|||Intracellular domain 2|||Low activity.|||N6-myristoyl lysine|||O-linked (GalNAc...) serine; in soluble form|||Phosphoserine; by CK1|||TNF family profile|||Tumor necrosis factor, membrane form|||Tumor necrosis factor, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034423|||http://purl.uniprot.org/annotation/PRO_0000034424|||http://purl.uniprot.org/annotation/PRO_0000417231|||http://purl.uniprot.org/annotation/PRO_0000417232|||http://purl.uniprot.org/annotation/PRO_0000417233|||http://purl.uniprot.org/annotation/PRO_0000417234|||http://purl.uniprot.org/annotation/VAR_011927|||http://purl.uniprot.org/annotation/VAR_019378
http://togogenome.org/gene/9606:SBK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C264                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Protein kinase|||Proton acceptor|||Uncharacterized serine/threonine-protein kinase SBK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262995
http://togogenome.org/gene/9606:ATP5MC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05496|||http://purl.uniprot.org/uniprot/Q6FIH7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Site|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  ATP synthase F(0) complex subunit C1, mitochondrial|||Helical|||Mitochondrion|||N6,N6,N6-trimethyllysine|||Reversibly protonated during proton transport|||V-ATPase proteolipid subunit C-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002557
http://togogenome.org/gene/9606:FAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K9J972|||http://purl.uniprot.org/uniprot/P25445|||http://purl.uniprot.org/uniprot/Q59FU8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolished GlcNAcylation by E.coli NleB1.|||Constitutive activation. Promotes apoptosis, both in the presence and in the absence of stimulation by a ligand.|||Cytoplasmic|||Death|||Decreased interaction with FADD.|||Extracellular|||Helical|||In ALPS1A.|||In ALPS1A; also found in non-Hodgkin lymphoma; somatic mutation; loss of interaction with FADD.|||In ALPS1A; associated with autoimmune hepatitis type 2.|||In ALPS1A; loss of interaction with FADD.|||In ALPS1A; no effect on interaction with FADD.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In non-Hodgkin lymphoma; somatic mutation.|||In squamous cell carcinoma; burn-scar related; somatic mutation.|||Interaction with CALM|||Interaction with HIPK3|||Loss of interaction with FADD.|||Loss of palmitoylation.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine|||Strongly decreased interaction with FADD.|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034563|||http://purl.uniprot.org/annotation/PRO_5040056762|||http://purl.uniprot.org/annotation/VAR_013416|||http://purl.uniprot.org/annotation/VAR_013417|||http://purl.uniprot.org/annotation/VAR_013418|||http://purl.uniprot.org/annotation/VAR_013419|||http://purl.uniprot.org/annotation/VAR_013420|||http://purl.uniprot.org/annotation/VAR_013421|||http://purl.uniprot.org/annotation/VAR_013422|||http://purl.uniprot.org/annotation/VAR_013423|||http://purl.uniprot.org/annotation/VAR_013424|||http://purl.uniprot.org/annotation/VAR_013425|||http://purl.uniprot.org/annotation/VAR_013426|||http://purl.uniprot.org/annotation/VAR_013427|||http://purl.uniprot.org/annotation/VAR_013428|||http://purl.uniprot.org/annotation/VAR_013429|||http://purl.uniprot.org/annotation/VAR_013430|||http://purl.uniprot.org/annotation/VAR_013431|||http://purl.uniprot.org/annotation/VAR_013432|||http://purl.uniprot.org/annotation/VAR_013433|||http://purl.uniprot.org/annotation/VAR_013434|||http://purl.uniprot.org/annotation/VAR_013435|||http://purl.uniprot.org/annotation/VAR_013436|||http://purl.uniprot.org/annotation/VAR_013437|||http://purl.uniprot.org/annotation/VAR_013438|||http://purl.uniprot.org/annotation/VAR_018321|||http://purl.uniprot.org/annotation/VAR_018322|||http://purl.uniprot.org/annotation/VAR_018323|||http://purl.uniprot.org/annotation/VAR_020008|||http://purl.uniprot.org/annotation/VAR_020009|||http://purl.uniprot.org/annotation/VAR_020942|||http://purl.uniprot.org/annotation/VAR_052347|||http://purl.uniprot.org/annotation/VAR_058910|||http://purl.uniprot.org/annotation/VAR_065128|||http://purl.uniprot.org/annotation/VAR_065129|||http://purl.uniprot.org/annotation/VAR_065130|||http://purl.uniprot.org/annotation/VAR_065131|||http://purl.uniprot.org/annotation/VAR_065132|||http://purl.uniprot.org/annotation/VSP_006481|||http://purl.uniprot.org/annotation/VSP_006482|||http://purl.uniprot.org/annotation/VSP_006483|||http://purl.uniprot.org/annotation/VSP_006484|||http://purl.uniprot.org/annotation/VSP_006485|||http://purl.uniprot.org/annotation/VSP_006486|||http://purl.uniprot.org/annotation/VSP_006487|||http://purl.uniprot.org/annotation/VSP_006488|||http://purl.uniprot.org/annotation/VSP_006489|||http://purl.uniprot.org/annotation/VSP_045235|||http://purl.uniprot.org/annotation/VSP_045236
http://togogenome.org/gene/9606:NBPF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TAG4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Neuroblastoma breakpoint family member 12|||Olduvai 1|||Olduvai 10|||Olduvai 11|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5|||Olduvai 6|||Olduvai 7|||Olduvai 8|||Olduvai 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288047
http://togogenome.org/gene/9606:C1GALT1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EU7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C1GALT1-specific chaperone 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In TNPS.|||In TNPS; loss capacity to promote Tn synthase activity.|||Lumenal|||Retains capacity to promote Tn synthase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285074|||http://purl.uniprot.org/annotation/VAR_031910|||http://purl.uniprot.org/annotation/VAR_031911|||http://purl.uniprot.org/annotation/VAR_069274|||http://purl.uniprot.org/annotation/VAR_069275|||http://purl.uniprot.org/annotation/VAR_069276
http://togogenome.org/gene/9606:FOXJ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein J3|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091855|||http://purl.uniprot.org/annotation/VAR_039104|||http://purl.uniprot.org/annotation/VAR_039105|||http://purl.uniprot.org/annotation/VSP_010367
http://togogenome.org/gene/9606:PLEKHB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UF11                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||PH|||Pleckstrin homology domain-containing family B member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053886|||http://purl.uniprot.org/annotation/VSP_009779|||http://purl.uniprot.org/annotation/VSP_009780
http://togogenome.org/gene/9606:CAPN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z479|||http://purl.uniprot.org/uniprot/Q9Y6W3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-7|||Domain III|||Domain N|||N-acetylmethionine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207720
http://togogenome.org/gene/9606:MAPK13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RD04|||http://purl.uniprot.org/uniprot/O15264                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Loss of kinase activity.|||Mitogen-activated protein kinase 13|||Phosphoserine|||Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7|||Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7|||Protein kinase|||Proton acceptor|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186286|||http://purl.uniprot.org/annotation/VAR_042267|||http://purl.uniprot.org/annotation/VAR_042268|||http://purl.uniprot.org/annotation/VAR_042269|||http://purl.uniprot.org/annotation/VSP_056558|||http://purl.uniprot.org/annotation/VSP_056559
http://togogenome.org/gene/9606:RUFY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNE9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||In isoform 2.|||RUN|||RUN and FYVE domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284671|||http://purl.uniprot.org/annotation/VSP_035815|||http://purl.uniprot.org/annotation/VSP_035816
http://togogenome.org/gene/9606:GOLGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08378                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage by caspase-2.|||Abolishes cleavage by caspase-3.|||Abolishes cleavage by caspase-7.|||Basic and acidic residues|||Cleavage; by caspase-2|||Cleavage; by caspase-3|||Cleavage; by caspase-7|||Disordered|||Golgi-targeting domain|||Golgin subfamily A member 3|||In isoform 2.|||In isoform 3.|||Interaction with GOPC|||Loss of interaction with GOPC; when associated with A-121 and A-128.|||Loss of interaction with GOPC; when associated with A-121 and A-135.|||Loss of interaction with GOPC; when associated with A-128 and A-135.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190057|||http://purl.uniprot.org/annotation/VAR_020153|||http://purl.uniprot.org/annotation/VAR_020154|||http://purl.uniprot.org/annotation/VAR_021901|||http://purl.uniprot.org/annotation/VSP_007728|||http://purl.uniprot.org/annotation/VSP_007729|||http://purl.uniprot.org/annotation/VSP_038000|||http://purl.uniprot.org/annotation/VSP_038001
http://togogenome.org/gene/9606:KLHL36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4N3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274691|||http://purl.uniprot.org/annotation/VSP_022867
http://togogenome.org/gene/9606:POLR1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15160                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerases I and III subunit RPAC1|||In HLD11.|||In HLD11; decreased localization to the nucleus and retained in the cytoplasm; loss of association with RNA polymerase III-transcribed genes; decreased association with RNA polymerase III complex; probably prevents RNA polymerase III complex assembly and activity.|||In TCS3.|||In TCS3; no effect on localization to the nucleus; no effect on association with RNA polymerase I and RNA polymerase III complexes.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132739|||http://purl.uniprot.org/annotation/VAR_064899|||http://purl.uniprot.org/annotation/VAR_064900|||http://purl.uniprot.org/annotation/VAR_074655|||http://purl.uniprot.org/annotation/VAR_074656|||http://purl.uniprot.org/annotation/VAR_074657|||http://purl.uniprot.org/annotation/VAR_074658|||http://purl.uniprot.org/annotation/VAR_074659|||http://purl.uniprot.org/annotation/VAR_074660|||http://purl.uniprot.org/annotation/VAR_074661|||http://purl.uniprot.org/annotation/VAR_074662|||http://purl.uniprot.org/annotation/VAR_074663|||http://purl.uniprot.org/annotation/VAR_074664|||http://purl.uniprot.org/annotation/VAR_074665|||http://purl.uniprot.org/annotation/VAR_074666|||http://purl.uniprot.org/annotation/VSP_005913
http://togogenome.org/gene/9606:WDR5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  DDB1-binding motif|||Disordered|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 5B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278461
http://togogenome.org/gene/9606:PTS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03393                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  6-pyruvoyl tetrahydrobiopterin synthase|||Charge relay system|||Decrease in activity; abolishes phosphorylation by PKG.|||In HPABH4A.|||In HPABH4A; abolishes activity; no effect on phosphorylation by PKG.|||In HPABH4A; mild form.|||In HPABH4A; severe decrease in activity; diminishes phosphorylation by PKG.|||In HPABH4A; severe form.|||In HPABH4A; transient phenotype due to partial PTS deficiency; mild decrease of activity.|||In HPABH4A; transient phenotype due to partial PTS deficiency; total loss of activity.|||Phosphoserine|||Phosphoserine; by PKG|||Phosphotyrosine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057914|||http://purl.uniprot.org/annotation/VAR_006816|||http://purl.uniprot.org/annotation/VAR_006817|||http://purl.uniprot.org/annotation/VAR_006818|||http://purl.uniprot.org/annotation/VAR_006819|||http://purl.uniprot.org/annotation/VAR_006820|||http://purl.uniprot.org/annotation/VAR_006821|||http://purl.uniprot.org/annotation/VAR_006822|||http://purl.uniprot.org/annotation/VAR_006823|||http://purl.uniprot.org/annotation/VAR_006824|||http://purl.uniprot.org/annotation/VAR_006825|||http://purl.uniprot.org/annotation/VAR_006826|||http://purl.uniprot.org/annotation/VAR_006827|||http://purl.uniprot.org/annotation/VAR_006828|||http://purl.uniprot.org/annotation/VAR_006829|||http://purl.uniprot.org/annotation/VAR_006830|||http://purl.uniprot.org/annotation/VAR_006831|||http://purl.uniprot.org/annotation/VAR_006832|||http://purl.uniprot.org/annotation/VAR_006833|||http://purl.uniprot.org/annotation/VAR_008040|||http://purl.uniprot.org/annotation/VAR_008041|||http://purl.uniprot.org/annotation/VAR_058265|||http://purl.uniprot.org/annotation/VAR_058266|||http://purl.uniprot.org/annotation/VAR_058267|||http://purl.uniprot.org/annotation/VAR_058268|||http://purl.uniprot.org/annotation/VAR_058269
http://togogenome.org/gene/9606:CRYM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14894                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DFNA40.|||Ketimine reductase mu-crystallin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200678|||http://purl.uniprot.org/annotation/VAR_073780|||http://purl.uniprot.org/annotation/VAR_073781
http://togogenome.org/gene/9606:TYRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17643                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5,6-dihydroxyindole-2-carboxylic acid oxidase|||Associated with blond hair in individuals from the Solomon Islands; rare or absent outside of Oceania.|||Cytoplasmic|||Helical|||In OCA3.|||Lumenal, melanosome|||N-linked (GlcNAc...) asparagine|||No effect; when associated with F-362 and S-374.|||No effect; when associated with F-362 and V-391.|||No effect; when associated with S-374 and V-391.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035889|||http://purl.uniprot.org/annotation/VAR_026827|||http://purl.uniprot.org/annotation/VAR_026828|||http://purl.uniprot.org/annotation/VAR_068176|||http://purl.uniprot.org/annotation/VAR_072599
http://togogenome.org/gene/9606:ETNPPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z224|||http://purl.uniprot.org/uniprot/E7ENR6|||http://purl.uniprot.org/uniprot/Q8TBG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ethanolamine-phosphate phospho-lyase|||In isoform 2.|||In isoform 3.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287663|||http://purl.uniprot.org/annotation/VAR_032342|||http://purl.uniprot.org/annotation/VSP_025583|||http://purl.uniprot.org/annotation/VSP_046097
http://togogenome.org/gene/9606:TIPRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75663                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PPP2CA, PPP2CB and PPP4C.|||Diminishes interaction with PPP2CA.|||In isoform 2.|||Interaction with PPP2CA|||N6-acetyllysine|||Phosphoserine|||TIP41-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301853|||http://purl.uniprot.org/annotation/VSP_027883|||http://purl.uniprot.org/annotation/VSP_027884
http://togogenome.org/gene/9606:NGLY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IV0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Nucleophile|||PAW|||PUB|||Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248971|||http://purl.uniprot.org/annotation/VAR_027385|||http://purl.uniprot.org/annotation/VAR_027386|||http://purl.uniprot.org/annotation/VSP_020343|||http://purl.uniprot.org/annotation/VSP_020344|||http://purl.uniprot.org/annotation/VSP_020345|||http://purl.uniprot.org/annotation/VSP_020346|||http://purl.uniprot.org/annotation/VSP_043501
http://togogenome.org/gene/9606:DZIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y13                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitin ligase activity.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase DZIP3|||In isoform 2.|||Polar residues|||RING-type; atypical|||Strongly decreases RNA-binding activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055898|||http://purl.uniprot.org/annotation/VSP_010971|||http://purl.uniprot.org/annotation/VSP_010972
http://togogenome.org/gene/9606:INAFM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Putative transmembrane protein INAFM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000430932
http://togogenome.org/gene/9606:DPYS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14117                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dihydropyrimidinase|||In DPYSD.|||N6-carboxylysine|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||via carbamate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165906|||http://purl.uniprot.org/annotation/VAR_002267|||http://purl.uniprot.org/annotation/VAR_002268|||http://purl.uniprot.org/annotation/VAR_002269|||http://purl.uniprot.org/annotation/VAR_002270|||http://purl.uniprot.org/annotation/VAR_002271
http://togogenome.org/gene/9606:ZIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15915                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In BAIDCS.|||In CRS6.|||Polar residues|||Zinc finger protein ZIC 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047244|||http://purl.uniprot.org/annotation/VAR_075867|||http://purl.uniprot.org/annotation/VAR_075868|||http://purl.uniprot.org/annotation/VAR_083723|||http://purl.uniprot.org/annotation/VAR_083724|||http://purl.uniprot.org/annotation/VAR_083725
http://togogenome.org/gene/9606:IBA57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T440                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MMDS3; loss of stability and consequently decrease in various mitochondrial 4Fe-4S proteins and in proteins covalently linked to lipoic acid.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Putative transferase CAF17, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278633|||http://purl.uniprot.org/annotation/VAR_030794|||http://purl.uniprot.org/annotation/VAR_069821
http://togogenome.org/gene/9606:LSM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83369                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In AGS8; impaired histone 3'-end pre-mRNA processing, leading to defects in chromatin structure; promoting CGAS-dependent activation of the type I interferon pathway.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SM 1|||SM 2|||Sm|||U7 snRNA-associated Sm-like protein LSm11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125587|||http://purl.uniprot.org/annotation/VAR_085527
http://togogenome.org/gene/9606:PRAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60831                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||PRA1 family protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220881|||http://purl.uniprot.org/annotation/VAR_050628
http://togogenome.org/gene/9606:LEFTY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75610                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Left-right determination factor 1|||N-linked (GlcNAc...) asparagine|||Or 135                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033810|||http://purl.uniprot.org/annotation/PRO_0000033811|||http://purl.uniprot.org/annotation/VAR_024231|||http://purl.uniprot.org/annotation/VAR_052567|||http://purl.uniprot.org/annotation/VAR_070888|||http://purl.uniprot.org/annotation/VAR_070889
http://togogenome.org/gene/9606:OR5C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW42|||http://purl.uniprot.org/uniprot/Q8NGR4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150590
http://togogenome.org/gene/9606:LENG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JMY0|||http://purl.uniprot.org/uniprot/Q96PV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with developmental delay, hypotonia since birth and dysmorphic features such as triangular face, brachycephaly epicanthal fold, hypertelorism, broad nasal bridge and strabismus; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Leukocyte receptor cluster member 8|||N-acetylalanine|||PCI|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306391|||http://purl.uniprot.org/annotation/VAR_035294|||http://purl.uniprot.org/annotation/VAR_035295|||http://purl.uniprot.org/annotation/VAR_082146|||http://purl.uniprot.org/annotation/VSP_059455|||http://purl.uniprot.org/annotation/VSP_059456|||http://purl.uniprot.org/annotation/VSP_059457
http://togogenome.org/gene/9606:SP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08047                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Abolishes MAPK-mediated phosphorylation, 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-739.|||Abolishes MAPK-mediated phosphorylation. 50% reduction in MAPK1/MAPK3-mediated activity on VEGF promoter, 40% reduction in protein levels during mitosis and no effect on dephosphorylation by PP2A. Greatly reduced MAPK1-mediated activity on VEGF promoter; when associated with A-453. Protein levels during mitosis reduced by 70%; when associated with A-278.|||Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-668 and A-681.|||Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. No effect on DNA binding; when associated with A-670 and A-681.|||Abolishes PRKCzeta-mediated but not PKCdelta-mediated phosphorylation. Some effect on dephosphorylation by PP2A. No effect on DNA binding; when associated with A-668 and A-681.|||Abolishes PRKCzeta-mediated phosphorylation. Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702.|||Abolishes acetylation. Increases recruitment of p300 to the promoter and enhances gene transcription.|||Almost complete abolition of activated MAPK8-mediated phosphorylation and 40% reduction in protein levels during mitosis. Protein levels reduced by 70% during mitosis; when associated with A-739.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Cleavage|||Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-698.|||Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-640; A-641 and A-702.|||Diminished glycosylation. Inhibits transcriptional activity; when associated with A-612; A-641; A-698 and A-702.|||Diminished glycosylation. Inhibits transcriptional activity; when associated with A-640; A-641; A-698 and A-702.|||Disordered|||Domain D|||Enhanced transcriptional activity.|||Exhibits attenuated endoproteolytic cleavage; when associated with A-728.|||Exhibits attenuated endoproteolytic cleavage; when associated with A-732.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Increase in phosphorylation on DNA damage.|||Increase in protein stability. No change in sumoylation.|||Increased protein stability during mitosis; when associated with D-278.|||Increased protein stability during mitosis; when associated with D-739.|||Little effect on activated MAPK8-mediated phosphorylation.|||Loss of O-glycosylation. Increase in transcriptional activity.|||Loss of phosphorylation. No effect on activated MAPK8-mediated phosphorylation. Similar loss of phosphorylation as by dephosphorylation by PP2AC. Reduced proteolytic processing.|||Loss of sumoylation. Increased cleavage and enhanced transcriptional activity.|||Loss of sumoylation. No cleavage and reduced transcriptional activity.|||N-acetylserine|||N6-acetyllysine|||No effect on activated MAPK8-mediated phosphorylation.|||No effect on dephosphorylation by PP2A.|||No effect on phosphorylation on DNA damage.|||No effect on sumoylation nor on proteolytic cleavage.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine; alternate|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by ATM|||Phosphoserine; by PKC/PRKCZ|||Phosphoserine; by PKC/PRKCZ; alternate|||Phosphothreonine|||Phosphothreonine; alternate|||Phosphothreonine; by MAPK1 and MAPK3|||Phosphothreonine; by MAPK1, MAPK3 and MAPK8|||Phosphothreonine; by MAPK8|||Phosphothreonine; by PKC/PRKCZ|||Polar residues|||Removed|||Repressor domain|||Significant reduction of phosphorylation on DNA damage.|||Some association with chromatin, increased phosphorylation levels and decreased glycosylation.|||Transactivation domain A (Gln-rich)|||Transactivation domain B (Gln-rich)|||Transactivation domain C (highly charged)|||Transcription factor Sp1|||VZV IE62-binding ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047137|||http://purl.uniprot.org/annotation/VAR_019971|||http://purl.uniprot.org/annotation/VSP_053934|||http://purl.uniprot.org/annotation/VSP_053935
http://togogenome.org/gene/9606:CNTNAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZ76                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein-like 3|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||In isoform 2.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019509|||http://purl.uniprot.org/annotation/VAR_046710|||http://purl.uniprot.org/annotation/VAR_046711|||http://purl.uniprot.org/annotation/VSP_003535|||http://purl.uniprot.org/annotation/VSP_003536
http://togogenome.org/gene/9606:ALG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJL6|||http://purl.uniprot.org/uniprot/Q9BT22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Chitobiosyldiphosphodolichol beta-mannosyltransferase|||Cytoplasmic|||Disordered|||Glycosyl transferase family 1|||Helical; Signal-anchor for type II membrane protein|||In CDG1K; decreased function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain.|||In isoform 2.|||Lumenal|||No effect on function in protein glycosylation as shown by rescue assays in an ALG1-deficient yeast strain.|||No effect on function in protein glycosylation.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080249|||http://purl.uniprot.org/annotation/PRO_5032518128|||http://purl.uniprot.org/annotation/VAR_023364|||http://purl.uniprot.org/annotation/VAR_023365|||http://purl.uniprot.org/annotation/VAR_023366|||http://purl.uniprot.org/annotation/VAR_023367|||http://purl.uniprot.org/annotation/VAR_038425|||http://purl.uniprot.org/annotation/VAR_038426|||http://purl.uniprot.org/annotation/VAR_038427|||http://purl.uniprot.org/annotation/VAR_049350|||http://purl.uniprot.org/annotation/VAR_077187|||http://purl.uniprot.org/annotation/VAR_077188|||http://purl.uniprot.org/annotation/VAR_077189|||http://purl.uniprot.org/annotation/VAR_077190|||http://purl.uniprot.org/annotation/VAR_077191|||http://purl.uniprot.org/annotation/VAR_077192|||http://purl.uniprot.org/annotation/VAR_077193|||http://purl.uniprot.org/annotation/VAR_077194|||http://purl.uniprot.org/annotation/VAR_077195|||http://purl.uniprot.org/annotation/VAR_077196|||http://purl.uniprot.org/annotation/VAR_077197|||http://purl.uniprot.org/annotation/VAR_077198|||http://purl.uniprot.org/annotation/VAR_077199|||http://purl.uniprot.org/annotation/VAR_077200|||http://purl.uniprot.org/annotation/VAR_077201|||http://purl.uniprot.org/annotation/VAR_077202|||http://purl.uniprot.org/annotation/VAR_077203|||http://purl.uniprot.org/annotation/VAR_077204|||http://purl.uniprot.org/annotation/VAR_077205|||http://purl.uniprot.org/annotation/VAR_077206|||http://purl.uniprot.org/annotation/VAR_077207|||http://purl.uniprot.org/annotation/VSP_056931
http://togogenome.org/gene/9606:ZNF157                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51786                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 157                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047432
http://togogenome.org/gene/9606:LHPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H008                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phospholysine phosphohistidine inorganic pyrophosphate phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305074|||http://purl.uniprot.org/annotation/VAR_035163|||http://purl.uniprot.org/annotation/VSP_041685|||http://purl.uniprot.org/annotation/VSP_041686
http://togogenome.org/gene/9606:FOXF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12947                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein F2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091834
http://togogenome.org/gene/9606:PAQR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ42|||http://purl.uniprot.org/uniprot/K9J969|||http://purl.uniprot.org/uniprot/Q5TCK7|||http://purl.uniprot.org/uniprot/Q6TCH4|||http://purl.uniprot.org/uniprot/Q7Z4Q8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Membrane progestin receptor delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218850|||http://purl.uniprot.org/annotation/VAR_082793|||http://purl.uniprot.org/annotation/VSP_011483|||http://purl.uniprot.org/annotation/VSP_011484|||http://purl.uniprot.org/annotation/VSP_011485|||http://purl.uniprot.org/annotation/VSP_054538
http://togogenome.org/gene/9606:PPP1R15A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 34 AA approximate repeats|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Impairs PP1 activation.|||In isoform 2.|||Interaction with KMT2A/MLL1|||Interaction with SMAD7|||Interaction with SMARCB1|||Localizes to cytoplasm, degraded more slowly.|||Localizes to cytoplasm.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Protein phosphatase 1 regulatory subunit 15A|||Reduces PP1-binding.|||Reduces PP1-binding; when associated with K-612.|||Reduces PP1-binding; when associated with K-614.|||Reduces interaction with SMARCB1.|||Required for localization in the endoplasmic reticulum|||Significantly reduced turnover.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320518|||http://purl.uniprot.org/annotation/VAR_039186|||http://purl.uniprot.org/annotation/VAR_039187|||http://purl.uniprot.org/annotation/VAR_039188|||http://purl.uniprot.org/annotation/VAR_039189|||http://purl.uniprot.org/annotation/VAR_039190|||http://purl.uniprot.org/annotation/VAR_039191|||http://purl.uniprot.org/annotation/VAR_039192|||http://purl.uniprot.org/annotation/VAR_039193|||http://purl.uniprot.org/annotation/VAR_039194|||http://purl.uniprot.org/annotation/VAR_039195|||http://purl.uniprot.org/annotation/VAR_062226|||http://purl.uniprot.org/annotation/VSP_057083|||http://purl.uniprot.org/annotation/VSP_057084
http://togogenome.org/gene/9606:MGAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10469                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In CDG2A.|||In CDG2A; strongly reduced protein levels; loss of enzyme activity.|||Loss of catalytic activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nearly abolishes catalytic activity and strongly decreases affinity for UDP-GlcNAc.|||Nearly abolishes catalytic activity.|||Strongly decreased catalytic activity and affinity for UDP-GlcNAc.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080517|||http://purl.uniprot.org/annotation/VAR_003415|||http://purl.uniprot.org/annotation/VAR_003416|||http://purl.uniprot.org/annotation/VAR_012343
http://togogenome.org/gene/9606:GSS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48637|||http://purl.uniprot.org/uniprot/V9HWJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutathione synthase substrate-binding|||Glutathione synthetase|||In GSS deficiency.|||In GSS deficiency; 10-fold decreased glutathione synthase activity.|||In GSS deficiency; 100-fold decreased glutathione synthase activity.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211260|||http://purl.uniprot.org/annotation/VAR_003602|||http://purl.uniprot.org/annotation/VAR_003603|||http://purl.uniprot.org/annotation/VAR_003604|||http://purl.uniprot.org/annotation/VAR_003605|||http://purl.uniprot.org/annotation/VAR_003606|||http://purl.uniprot.org/annotation/VAR_003607|||http://purl.uniprot.org/annotation/VAR_003608|||http://purl.uniprot.org/annotation/VAR_003609|||http://purl.uniprot.org/annotation/VAR_003610|||http://purl.uniprot.org/annotation/VAR_003611|||http://purl.uniprot.org/annotation/VAR_003612|||http://purl.uniprot.org/annotation/VAR_003613|||http://purl.uniprot.org/annotation/VAR_003614|||http://purl.uniprot.org/annotation/VAR_025047|||http://purl.uniprot.org/annotation/VAR_025048|||http://purl.uniprot.org/annotation/VAR_078567|||http://purl.uniprot.org/annotation/VSP_047617
http://togogenome.org/gene/9606:RHEB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15382                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Causes slight reduction in RPS6KB1 activation.|||Causes slightly reduced phosphorylation of EIF4EBP1.|||Cysteine methyl ester|||Decreased ubiquitination by RNF152. Does not affect polyubiquitination in response to amino acids.|||Decreased ubiquitination in response to amino acids; when associated with R-109, R-135 and R-151.|||Decreased ubiquitination in response to amino acids; when associated with R-109, R-135 and R-178.|||Decreased ubiquitination in response to amino acids; when associated with R-109, R-151 and R-178.|||Decreased ubiquitination in response to amino acids; when associated with R-135, R-151 and R-178.|||Deficient in guanine nucleotide binding. Unable to rescue RPS6KB1 from inactivation by amino-acid withdrawal.|||Dominant mutant, which can activate mTORC1 in both GDP- and GTP-bound forms.|||Effector region|||GTP-binding protein Rheb|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Has a higher basal GTPase level, however, is still sensitive to TSC2 GAP activity.|||Impairs RPS6KB1 activation, but still binds guanine nucleotides normally.|||Impairs interaction with MTOR. Impairs signaling through mTORC1, but still binds guanine nucleotides normally.|||Important for autoinhibition of GTPase activity|||In a colorectal cancer sample; somatic mutation.|||Increased GTPase ativity; insensitive to TSC2 regulation, leading to impaired regulation of mTORC1 signaling.|||No effect.|||Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and RPS6KB1 activation.|||Partially resistant to inactivation by TSC1-TSC2.|||Phosphoserine; by MAPKAPK5|||Reduces the ability to rescue RPS6KB1 from inactivation by amino-acid withdrawal.|||Removed in mature form|||Renders RHEB insensitive to TSC2 regulation, leading to impaired regulation of mTORC1 signaling.|||S-farnesyl cysteine|||Slightly impairs signaling through mTORC1, but still binds guanine nucleotides normally.|||Unable to bind Mg(2+), preventing nucleotide-binding.|||Unstable protein, which cannot load GTP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082708|||http://purl.uniprot.org/annotation/PRO_0000281365|||http://purl.uniprot.org/annotation/VAR_036310
http://togogenome.org/gene/9606:SPOCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||SPOC|||SPOC domain-containing protein 1|||TFIIS central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287472|||http://purl.uniprot.org/annotation/VAR_035660|||http://purl.uniprot.org/annotation/VAR_051379|||http://purl.uniprot.org/annotation/VAR_051380|||http://purl.uniprot.org/annotation/VSP_025489|||http://purl.uniprot.org/annotation/VSP_025490|||http://purl.uniprot.org/annotation/VSP_025491|||http://purl.uniprot.org/annotation/VSP_025492|||http://purl.uniprot.org/annotation/VSP_025493|||http://purl.uniprot.org/annotation/VSP_025494|||http://purl.uniprot.org/annotation/VSP_025495|||http://purl.uniprot.org/annotation/VSP_025496|||http://purl.uniprot.org/annotation/VSP_025497
http://togogenome.org/gene/9606:CNGB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQW8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclic nucleotide-gated cation channel beta-3|||Cytoplasmic|||Disordered|||Extracellular|||Found in macular degeneration; unknown pathological significance.|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||In ACHM3.|||In ACHM3; requires 2 nucleotide substitutions.|||In ACHM3; unknown pathological significance.|||In STGD1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219320|||http://purl.uniprot.org/annotation/VAR_018109|||http://purl.uniprot.org/annotation/VAR_018110|||http://purl.uniprot.org/annotation/VAR_018111|||http://purl.uniprot.org/annotation/VAR_018112|||http://purl.uniprot.org/annotation/VAR_024418|||http://purl.uniprot.org/annotation/VAR_025524|||http://purl.uniprot.org/annotation/VAR_025525|||http://purl.uniprot.org/annotation/VAR_047606|||http://purl.uniprot.org/annotation/VAR_047607|||http://purl.uniprot.org/annotation/VAR_047608|||http://purl.uniprot.org/annotation/VAR_047609|||http://purl.uniprot.org/annotation/VAR_047610|||http://purl.uniprot.org/annotation/VAR_047611|||http://purl.uniprot.org/annotation/VAR_047612|||http://purl.uniprot.org/annotation/VAR_047613|||http://purl.uniprot.org/annotation/VAR_047614|||http://purl.uniprot.org/annotation/VAR_047615|||http://purl.uniprot.org/annotation/VAR_047616|||http://purl.uniprot.org/annotation/VAR_047617|||http://purl.uniprot.org/annotation/VAR_047618|||http://purl.uniprot.org/annotation/VAR_047619|||http://purl.uniprot.org/annotation/VAR_047620|||http://purl.uniprot.org/annotation/VAR_047621|||http://purl.uniprot.org/annotation/VAR_047622|||http://purl.uniprot.org/annotation/VSP_009742
http://togogenome.org/gene/9606:GLIPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUM5|||http://purl.uniprot.org/uniprot/A0A088AWP7|||http://purl.uniprot.org/uniprot/Q5VZR0|||http://purl.uniprot.org/uniprot/Q9H4G4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi-associated plant pathogenesis-related protein 1|||Interaction with CAV1|||N-myristoyl glycine|||Removed|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211524
http://togogenome.org/gene/9606:SLC25A43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUT9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291823|||http://purl.uniprot.org/annotation/VAR_032865|||http://purl.uniprot.org/annotation/VSP_026245
http://togogenome.org/gene/9606:CASQ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14958                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Calsequestrin-2|||Disordered|||In CPVT2.|||In CPVT2; alters protein folding; reduces calcium-binding; reduces calcium-dependent oligomerization; decreases sarcoplasmic reticulum Ca(2+) storing capacity; reduces the amplitude of I(Ca)-induced Ca(2+) transients; reduces spontaneous Ca(2+) sparks in permeabilized myocytes.|||In CPVT2; reduces calcium-binding; impairs calcium-dependent oligomerization; causes 50% decrease in calcium-dependent binding to TRDN; causes 50% decrease in calcium-dependent binding to ASPH.|||In CPVT2; reduces calcium-dependent dimerization.|||In isoform 2.|||Increases dimerization in the absence of calcium.|||N-linked (GlcNAc...) asparagine|||No effect on calcium-binding and calcium-dependent dimerization.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004218|||http://purl.uniprot.org/annotation/VAR_016075|||http://purl.uniprot.org/annotation/VAR_023692|||http://purl.uniprot.org/annotation/VAR_023693|||http://purl.uniprot.org/annotation/VAR_044118|||http://purl.uniprot.org/annotation/VAR_055234|||http://purl.uniprot.org/annotation/VAR_067036|||http://purl.uniprot.org/annotation/VAR_067037|||http://purl.uniprot.org/annotation/VAR_076546|||http://purl.uniprot.org/annotation/VSP_056477
http://togogenome.org/gene/9606:C2orf69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8R5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Transit Peptide                                                                                  ^@                                                                                  Abolishes mitochondrial localization.|||Mitochondrial protein C2orf69|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329088
http://togogenome.org/gene/9606:TMEM74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Transmembrane protein 74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259600
http://togogenome.org/gene/9606:PTCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13635                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In BCNS1 and BCC.|||In BCNS1.|||In BCNS1; unknown pathological significance.|||In HPE7.|||In isoform L'.|||In isoform M.|||In isoform S.|||In squamous cell carcinoma.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein patched homolog 1|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205964|||http://purl.uniprot.org/annotation/VAR_007843|||http://purl.uniprot.org/annotation/VAR_007844|||http://purl.uniprot.org/annotation/VAR_007845|||http://purl.uniprot.org/annotation/VAR_007846|||http://purl.uniprot.org/annotation/VAR_007847|||http://purl.uniprot.org/annotation/VAR_010974|||http://purl.uniprot.org/annotation/VAR_010975|||http://purl.uniprot.org/annotation/VAR_010976|||http://purl.uniprot.org/annotation/VAR_010977|||http://purl.uniprot.org/annotation/VAR_010978|||http://purl.uniprot.org/annotation/VAR_010979|||http://purl.uniprot.org/annotation/VAR_010980|||http://purl.uniprot.org/annotation/VAR_010981|||http://purl.uniprot.org/annotation/VAR_010982|||http://purl.uniprot.org/annotation/VAR_010983|||http://purl.uniprot.org/annotation/VAR_010984|||http://purl.uniprot.org/annotation/VAR_020440|||http://purl.uniprot.org/annotation/VAR_020845|||http://purl.uniprot.org/annotation/VAR_020846|||http://purl.uniprot.org/annotation/VAR_020847|||http://purl.uniprot.org/annotation/VAR_032952|||http://purl.uniprot.org/annotation/VAR_032953|||http://purl.uniprot.org/annotation/VAR_032954|||http://purl.uniprot.org/annotation/VAR_032955|||http://purl.uniprot.org/annotation/VAR_032956|||http://purl.uniprot.org/annotation/VAR_032957|||http://purl.uniprot.org/annotation/VAR_032958|||http://purl.uniprot.org/annotation/VSP_041369|||http://purl.uniprot.org/annotation/VSP_041370|||http://purl.uniprot.org/annotation/VSP_041371
http://togogenome.org/gene/9606:NDUFA4L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRX3                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118825
http://togogenome.org/gene/9606:EIF3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15371                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit D|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||RNA gate|||Reduced binding to JUN mRNA.|||Reduced binding to JUN mRNA; when associated with 262-I-A-263.|||Reduced binding to JUN mRNA; when associated with Q-249.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123520|||http://purl.uniprot.org/annotation/VAR_074184|||http://purl.uniprot.org/annotation/VSP_055473|||http://purl.uniprot.org/annotation/VSP_055474
http://togogenome.org/gene/9606:PDZRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2I8|||http://purl.uniprot.org/uniprot/B7Z5Q3|||http://purl.uniprot.org/uniprot/B7Z5X9|||http://purl.uniprot.org/uniprot/B7ZAG0|||http://purl.uniprot.org/uniprot/E7ENB6|||http://purl.uniprot.org/uniprot/Q9UPQ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase PDZRN3|||In isoform 2.|||In isoform 3.|||PDZ|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues|||RING-type; degenerate|||TRAF-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055917|||http://purl.uniprot.org/annotation/VAR_020965|||http://purl.uniprot.org/annotation/VSP_012606|||http://purl.uniprot.org/annotation/VSP_012607|||http://purl.uniprot.org/annotation/VSP_012608|||http://purl.uniprot.org/annotation/VSP_012609
http://togogenome.org/gene/9606:AP5B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VPB7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  AP-5 complex subunit beta-1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000405404
http://togogenome.org/gene/9606:SAFB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14151                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Interaction with SAFB1|||N-acetylalanine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||SAP|||Scaffold attachment factor B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081907|||http://purl.uniprot.org/annotation/VSP_056404|||http://purl.uniprot.org/annotation/VSP_056405
http://togogenome.org/gene/9606:C14orf28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4W4Y0                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C14orf28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274307
http://togogenome.org/gene/9606:MYL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXJ4|||http://purl.uniprot.org/uniprot/Q9BUA6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin regulatory light chain 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322130|||http://purl.uniprot.org/annotation/VAR_039401
http://togogenome.org/gene/9606:OR4N5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN4|||http://purl.uniprot.org/uniprot/Q8IXE1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4N5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150565|||http://purl.uniprot.org/annotation/VAR_024095|||http://purl.uniprot.org/annotation/VAR_034208|||http://purl.uniprot.org/annotation/VAR_034209|||http://purl.uniprot.org/annotation/VAR_053175
http://togogenome.org/gene/9606:L3MBTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHHC-type; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with DCAF5|||Interaction with RBPJ. Required for transcription repressor activity on Notch target genes|||Lethal(3)malignant brain tumor-like protein 3|||Loss of interaction with DNMT1.|||MBT 1|||MBT 2|||MBT 3|||Phosphoserine|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084450|||http://purl.uniprot.org/annotation/VAR_022368|||http://purl.uniprot.org/annotation/VSP_013508
http://togogenome.org/gene/9606:CACNA2D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3S7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cache|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||In isoform 7.|||Interchain (between alpha-2-4 and delta-4 chains)|||MIDAS-like motif|||N-linked (GlcNAc...) asparagine|||VWFA|||Voltage-dependent calcium channel subunit alpha-2-4|||Voltage-dependent calcium channel subunit alpha-2/delta-4|||Voltage-dependent calcium channel subunit delta-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304655|||http://purl.uniprot.org/annotation/PRO_0000304656|||http://purl.uniprot.org/annotation/PRO_0000304657|||http://purl.uniprot.org/annotation/VAR_035049|||http://purl.uniprot.org/annotation/VAR_035050|||http://purl.uniprot.org/annotation/VAR_035051|||http://purl.uniprot.org/annotation/VSP_028069|||http://purl.uniprot.org/annotation/VSP_028070|||http://purl.uniprot.org/annotation/VSP_028071|||http://purl.uniprot.org/annotation/VSP_044107|||http://purl.uniprot.org/annotation/VSP_044108|||http://purl.uniprot.org/annotation/VSP_044109|||http://purl.uniprot.org/annotation/VSP_044110
http://togogenome.org/gene/9606:GINS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRT9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  DNA replication complex GINS protein SLD5|||DNA replication complex GINS protein SLD5, N-terminally processed|||Important for GINS complex assembly|||In isoform 2.|||N-acetylmethionine|||N-acetylthreonine; in DNA replication complex GINS protein SLD5, N-terminally processed|||Phosphoserine|||Removed; alternate|||This is the measured mass for the GINS complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327620|||http://purl.uniprot.org/annotation/PRO_0000421794|||http://purl.uniprot.org/annotation/VSP_032738|||http://purl.uniprot.org/annotation/VSP_032739
http://togogenome.org/gene/9606:ASIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42127                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Agouti|||Agouti-signaling protein|||Disordered|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001028|||http://purl.uniprot.org/annotation/VAR_005003|||http://purl.uniprot.org/annotation/VAR_022125
http://togogenome.org/gene/9606:SLC6A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y4I3|||http://purl.uniprot.org/uniprot/B7Z3C5|||http://purl.uniprot.org/uniprot/P30531                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of GABA transporter activity.|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with generalized epilepsy; unknown pathological significance; complete loss of GABA transporter activity.|||Found in a patient with generalized epilepsy; unknown pathological significance; retains about 6% of wild-type GABA transporter activity.|||Found in a patient with intractable absence epilepsy; unknown pathological significance; retains about 27% of wild-type GABA transporter activity.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In MAE.|||In MAE; unknown pathological significance; retains about 13% of wild-type GABA transporter activity.|||In MAE; unknown pathological significance; retains about 2% of wild-type GABA transporter activity.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||Sodium- and chloride-dependent GABA transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214743|||http://purl.uniprot.org/annotation/VAR_055088|||http://purl.uniprot.org/annotation/VAR_073852|||http://purl.uniprot.org/annotation/VAR_073853|||http://purl.uniprot.org/annotation/VAR_073854|||http://purl.uniprot.org/annotation/VAR_073855|||http://purl.uniprot.org/annotation/VAR_086249|||http://purl.uniprot.org/annotation/VAR_086250|||http://purl.uniprot.org/annotation/VAR_086251|||http://purl.uniprot.org/annotation/VAR_086252|||http://purl.uniprot.org/annotation/VAR_086253|||http://purl.uniprot.org/annotation/VAR_086254|||http://purl.uniprot.org/annotation/VAR_086255
http://togogenome.org/gene/9606:PIK3CB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DER4|||http://purl.uniprot.org/uniprot/P42338                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Activation loop|||C2 PI3K-type|||Catalytic loop|||Enhanced inhibition by PIK3R1 leading to reduced lipid kinase activity and reduced oncogenicity. Does not modify regulation by GPCRs.|||G-loop|||Loss of autophosphorylation. Decreased basal and stimulated phosphatidylinositol-4,5-bisphosphate 3-kinase activity.|||Loss of autophosphorylation. No effect on phosphatidylinositol-4,5-bisphosphate 3-kinase activity.|||Loss of lipid kinase activity. May not affect insulin signaling and cell proliferation. Partially affects oncogene-induced transformation.|||Nuclear localization signal|||PI3K-ABD|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform|||Phosphoserine|||Phosphoserine; by autocatalysis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088787|||http://purl.uniprot.org/annotation/VAR_050530
http://togogenome.org/gene/9606:MCRIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MAPK regulated corepressor interacting protein 2|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274328|||http://purl.uniprot.org/annotation/VSP_022712
http://togogenome.org/gene/9606:TBC1D3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DHY5|||http://purl.uniprot.org/uniprot/Q6IPX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3C|||TBC1 domain family member 3G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300265|||http://purl.uniprot.org/annotation/PRO_0000300266
http://togogenome.org/gene/9606:ZNF367                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTV3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||In isoform 2.|||Phosphoserine|||Zinc finger protein 367                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285297|||http://purl.uniprot.org/annotation/VSP_024865
http://togogenome.org/gene/9606:GPX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36969|||http://purl.uniprot.org/uniprot/Q6PI42                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non standard residue|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Non standard residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Almost complete loss of enzyme activity.|||Glutathione peroxidase|||In SMDS.|||In a patient affected by cryptorchidism.|||In isoform Cytoplasmic.|||Loss of enzyme activity.|||Mitochondrion|||Phospholipid hydroperoxide glutathione peroxidase|||Phosphoserine|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013067|||http://purl.uniprot.org/annotation/PRO_5004278983|||http://purl.uniprot.org/annotation/VAR_017063|||http://purl.uniprot.org/annotation/VAR_017064|||http://purl.uniprot.org/annotation/VAR_080140|||http://purl.uniprot.org/annotation/VSP_018740
http://togogenome.org/gene/9606:CDR2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X02                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cerebellar degeneration-related protein 2-like|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307234|||http://purl.uniprot.org/annotation/VAR_035384
http://togogenome.org/gene/9606:COL5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05997                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  3-hydroxyproline; partial|||Basic and acidic residues|||C-terminal propeptide|||Cell attachment site|||Collagen alpha-2(V) chain|||Disordered|||Fibrillar collagen NC1|||Hydroxyproline|||In EDSCL2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005830|||http://purl.uniprot.org/annotation/PRO_0000005831|||http://purl.uniprot.org/annotation/VAR_013588|||http://purl.uniprot.org/annotation/VAR_048799|||http://purl.uniprot.org/annotation/VAR_048800|||http://purl.uniprot.org/annotation/VAR_057910|||http://purl.uniprot.org/annotation/VAR_057911|||http://purl.uniprot.org/annotation/VAR_057912|||http://purl.uniprot.org/annotation/VAR_057913|||http://purl.uniprot.org/annotation/VAR_078424
http://togogenome.org/gene/9606:SCAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXB0|||http://purl.uniprot.org/uniprot/B4E2V7|||http://purl.uniprot.org/uniprot/O15126                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Pro residues|||Removed|||Secretory carrier-associated membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191250|||http://purl.uniprot.org/annotation/VSP_004380
http://togogenome.org/gene/9606:CENPS-CORT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT10|||http://purl.uniprot.org/uniprot/Q8N2Z9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Centromere protein S|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||No effect on CENPX- and FANCM-binding; loss of double-stranded DNA-binding of the MHF heterodimer and of FANCM recruitment to fork DNA; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 87-A-A-88.|||Partial loss of CENPX- and FANCM-binding; partial decrease in FA core complex activity, as shown by lower levels of FANCD2 monoubiquitination and higher frequency of sister chromatin exchanges. Complete loss of CENPX- and FANCM-binding; when associated with 73-A-A-74.|||Somatostatin/Cortistatin C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249477|||http://purl.uniprot.org/annotation/VSP_020432|||http://purl.uniprot.org/annotation/VSP_020433|||http://purl.uniprot.org/annotation/VSP_020434
http://togogenome.org/gene/9606:OXSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95747                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with SLC12A2/NKCC1 and WNK4.|||Abolished interaction with WNK4.|||Basic and acidic residues|||Decreased interaction with WNK4.|||Disordered|||Does not affect activation by WNK kinases.|||In a metastatic melanoma sample; somatic mutation.|||Loss of RELT, RELL1 and RELL2 phosphorylation. Retention of some autophosphorylation activity may be due to complex formation with other endogenous kinases in the assay.|||Loss of autophosphorylation and kinase activity.|||Mimics phosphorylation; promoting kinase activity independently of WNK kinases.|||Mimics phosphorylation; slighlty promoting kinase activity independently of WNK kinases.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by WNK1|||Prevents phosphorylation and activation by WNK kinases.|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase OSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086456|||http://purl.uniprot.org/annotation/VAR_023232|||http://purl.uniprot.org/annotation/VAR_025181|||http://purl.uniprot.org/annotation/VAR_040969
http://togogenome.org/gene/9606:RAD51B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JYJ0|||http://purl.uniprot.org/uniprot/O15315                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with BCR-ABLSH3 domain.|||Breakpoint for translocation to form HMGA2-RAD51B|||DNA repair protein RAD51 homolog 2|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Interaction with RAD51C|||RecA family profile 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122939|||http://purl.uniprot.org/annotation/VAR_025243|||http://purl.uniprot.org/annotation/VAR_025244|||http://purl.uniprot.org/annotation/VAR_025245|||http://purl.uniprot.org/annotation/VAR_025246|||http://purl.uniprot.org/annotation/VAR_025247|||http://purl.uniprot.org/annotation/VAR_025248|||http://purl.uniprot.org/annotation/VAR_035437|||http://purl.uniprot.org/annotation/VAR_051730|||http://purl.uniprot.org/annotation/VSP_008817|||http://purl.uniprot.org/annotation/VSP_008818|||http://purl.uniprot.org/annotation/VSP_008819|||http://purl.uniprot.org/annotation/VSP_008820
http://togogenome.org/gene/9606:TTLL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N841                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased binding to microtubules and polyglutamylase activity; when associated with 396-E--E-398 and E-416.|||Decreased binding to microtubules and polyglutamylase activity; when associated with 396-E--E-398 and E-419.|||Decreased binding to microtubules and polyglutamylase activity; when associated with E-416 and E-419.|||Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||Important for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 2.|||Polar residues|||TTL|||Tubulin polyglutamylase TTLL6|||c-MTBD region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326160|||http://purl.uniprot.org/annotation/VAR_039993|||http://purl.uniprot.org/annotation/VAR_082930|||http://purl.uniprot.org/annotation/VSP_052727|||http://purl.uniprot.org/annotation/VSP_052728
http://togogenome.org/gene/9606:IFT43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||In RP81; results in cilia shortening.|||In SRTD18; patient cells show reduced amount of IFT43 protein and do not have cilia.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Intraflagellar transport protein 43 homolog|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254041|||http://purl.uniprot.org/annotation/VAR_056839|||http://purl.uniprot.org/annotation/VAR_080629|||http://purl.uniprot.org/annotation/VAR_080630|||http://purl.uniprot.org/annotation/VAR_082868|||http://purl.uniprot.org/annotation/VSP_021169|||http://purl.uniprot.org/annotation/VSP_041319|||http://purl.uniprot.org/annotation/VSP_047398
http://togogenome.org/gene/9606:SEMA6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1 and isoform 2.|||In isoform 1 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sema|||Semaphorin-6D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000044615|||http://purl.uniprot.org/annotation/VAR_051931|||http://purl.uniprot.org/annotation/VAR_051932|||http://purl.uniprot.org/annotation/VAR_051933|||http://purl.uniprot.org/annotation/VSP_016564|||http://purl.uniprot.org/annotation/VSP_016565|||http://purl.uniprot.org/annotation/VSP_016566|||http://purl.uniprot.org/annotation/VSP_016567|||http://purl.uniprot.org/annotation/VSP_016572|||http://purl.uniprot.org/annotation/VSP_054084
http://togogenome.org/gene/9606:GPRIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2K8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G protein-regulated inducer of neurite outgrowth 1|||In isoform 2.|||Interaction with GNAO1|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235977|||http://purl.uniprot.org/annotation/VAR_056902|||http://purl.uniprot.org/annotation/VAR_056903|||http://purl.uniprot.org/annotation/VAR_063136|||http://purl.uniprot.org/annotation/VAR_063137|||http://purl.uniprot.org/annotation/VSP_018546|||http://purl.uniprot.org/annotation/VSP_018547
http://togogenome.org/gene/9606:TRUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWH5                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished RNA-binding and ability to promote processing of let-7 miRNAs.|||Abolished pseudouridine synthase activity without affecting ability to promote processing of let-7 miRNAs; when associated with A-121.|||Abolished pseudouridine synthase activity without affecting ability to promote processing of let-7 miRNAs; when associated with A-163.|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Pseudouridylate synthase TRUB1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252087|||http://purl.uniprot.org/annotation/VAR_027748|||http://purl.uniprot.org/annotation/VAR_051607
http://togogenome.org/gene/9606:ACVR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13705                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activin receptor type-2B|||Cytoplasmic|||Extracellular|||Helical|||In HTX4.|||Interaction with DYNLT1|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024404|||http://purl.uniprot.org/annotation/VAR_013281|||http://purl.uniprot.org/annotation/VAR_013282|||http://purl.uniprot.org/annotation/VAR_041396|||http://purl.uniprot.org/annotation/VAR_050594
http://togogenome.org/gene/9606:DNAJC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Y2X3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||DnaJ homolog subfamily C member 14|||Helical|||J|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247493
http://togogenome.org/gene/9606:ZCCHC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5U6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished rRNA methyltransferase activity.|||CCHC-type|||DHHC|||Decreased S-adenosyl-L-methionine-binding.|||Disordered|||GRF-type|||In isoform 2.|||In isoform 3.|||Increased rRNA methylation.|||Loss of methyltransferase activity.|||Regulatory loop|||Strongly impaired rRNA methyltransferase activity.|||rRNA N6-adenosine-methyltransferase ZCCHC4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150952|||http://purl.uniprot.org/annotation/VAR_024925|||http://purl.uniprot.org/annotation/VAR_053751|||http://purl.uniprot.org/annotation/VSP_043359|||http://purl.uniprot.org/annotation/VSP_043360
http://togogenome.org/gene/9606:POLR2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QYL9|||http://purl.uniprot.org/uniprot/P61218                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||DNA-directed RNA polymerases I, II, and III subunit RPABC2|||Disordered|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||Phosphoserine; by CK2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000133799|||http://purl.uniprot.org/annotation/VAR_036571
http://togogenome.org/gene/9606:MPC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DKB6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Mitochondrial matrix|||Mitochondrial pyruvate carrier 1-like protein|||Mother cell cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419605
http://togogenome.org/gene/9606:OVOL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Transcription factor Ovo-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047013|||http://purl.uniprot.org/annotation/VSP_038260
http://togogenome.org/gene/9606:ZFAND5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76080                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||AN1-type|||AN1-type zinc finger protein 5|||Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066557
http://togogenome.org/gene/9606:SPRY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43609                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Polar residues|||Protein sprouty homolog 1|||SPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076898
http://togogenome.org/gene/9606:PNMA6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CW24                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Paraneoplastic antigen-like protein 6A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311219
http://togogenome.org/gene/9606:GJB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PEY0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gap junction beta-7 protein|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271343|||http://purl.uniprot.org/annotation/VAR_047627|||http://purl.uniprot.org/annotation/VAR_047628|||http://purl.uniprot.org/annotation/VAR_061125
http://togogenome.org/gene/9606:CCL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92583                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005211|||http://purl.uniprot.org/annotation/VAR_048708|||http://purl.uniprot.org/annotation/VAR_048709
http://togogenome.org/gene/9606:TCOF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRA2|||http://purl.uniprot.org/uniprot/E7ETY2|||http://purl.uniprot.org/uniprot/Q13428                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In TCS1.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 8.|||In isoform 3, isoform 7 and isoform 8.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||LisH|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Treacle protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072459|||http://purl.uniprot.org/annotation/VAR_005630|||http://purl.uniprot.org/annotation/VAR_005631|||http://purl.uniprot.org/annotation/VAR_005632|||http://purl.uniprot.org/annotation/VAR_005633|||http://purl.uniprot.org/annotation/VAR_005634|||http://purl.uniprot.org/annotation/VAR_029869|||http://purl.uniprot.org/annotation/VAR_035666|||http://purl.uniprot.org/annotation/VAR_057002|||http://purl.uniprot.org/annotation/VAR_059729|||http://purl.uniprot.org/annotation/VAR_059730|||http://purl.uniprot.org/annotation/VAR_061709|||http://purl.uniprot.org/annotation/VSP_022295|||http://purl.uniprot.org/annotation/VSP_022296|||http://purl.uniprot.org/annotation/VSP_022297|||http://purl.uniprot.org/annotation/VSP_023133|||http://purl.uniprot.org/annotation/VSP_023134|||http://purl.uniprot.org/annotation/VSP_040382
http://togogenome.org/gene/9606:UPF3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes NMD.|||Abolishes NMD; when associated with E-447 and E-449.|||Abolishes NMD; when associated with E-447 and E-451.|||Abolishes NMD; when associated with E-449 and E-451.|||Abolishes interaction with UPF2.|||Basic and acidic residues|||Binds to UPF2|||Disordered|||Does not abolish interaction with UPF2.|||Impairs association with EJC.|||In MRXS14.|||In isoform 2.|||Necessary for interaction with RBM8A and for activating NMD|||Necessary for interaction with UPF2|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Reduces NMD.|||Regulator of nonsense transcripts 3B|||Sufficient for association with EJC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215297|||http://purl.uniprot.org/annotation/VAR_037666|||http://purl.uniprot.org/annotation/VSP_012963
http://togogenome.org/gene/9606:BCAP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PAJ1|||http://purl.uniprot.org/uniprot/Q9UHQ4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B-cell receptor-associated protein 29|||BAP29/BAP31 transmembrane|||Bap31/Bap29 cytoplasmic coiled-coil|||Cytoplasmic|||Di-lysine motif|||Disordered|||Helical|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142888|||http://purl.uniprot.org/annotation/VSP_047096
http://togogenome.org/gene/9606:LARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15031                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||In HLASA; decreased leucine-tRNA ligase activity.|||In PRLTS4 and HLASA; reduced activity; decreased leucine-tRNA ligase activity.|||In PRLTS4; unknown pathological significance; the mutant is functional in a yeast complementation assay.|||Leucine--tRNA ligase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035806|||http://purl.uniprot.org/annotation/VAR_052638|||http://purl.uniprot.org/annotation/VAR_052639|||http://purl.uniprot.org/annotation/VAR_070094|||http://purl.uniprot.org/annotation/VAR_070095|||http://purl.uniprot.org/annotation/VAR_076997
http://togogenome.org/gene/9606:AMDHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVC5|||http://purl.uniprot.org/uniprot/Q96NU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Amidohydrolase-related|||Probable imidazolonepropionase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282582|||http://purl.uniprot.org/annotation/VAR_031419|||http://purl.uniprot.org/annotation/VAR_031420
http://togogenome.org/gene/9606:OR10X1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWA4|||http://purl.uniprot.org/uniprot/Q8NGY0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10X1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150720|||http://purl.uniprot.org/annotation/VAR_053290|||http://purl.uniprot.org/annotation/VAR_053291|||http://purl.uniprot.org/annotation/VAR_053292|||http://purl.uniprot.org/annotation/VAR_053293
http://togogenome.org/gene/9606:THEM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUY1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Phosphoserine|||Protein THEM6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285636|||http://purl.uniprot.org/annotation/VAR_032034
http://togogenome.org/gene/9606:CD96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40200|||http://purl.uniprot.org/uniprot/Q8WUE2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type 1|||Ig-like V-type 2|||In CSYN.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||T-cell surface protein tactile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014970|||http://purl.uniprot.org/annotation/VAR_021928|||http://purl.uniprot.org/annotation/VAR_037578|||http://purl.uniprot.org/annotation/VSP_029908
http://togogenome.org/gene/9606:TRIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5Y8|||http://purl.uniprot.org/uniprot/O75382                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||Disordered|||Filamin|||In isoform 4.|||In isoform Beta.|||In isoform Gamma.|||Interaction with KIF21B|||N-acetylalanine|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Phosphoserine|||Polar residues|||RING-type|||Removed|||Strong loss of ubiquitin ligase activity; when associated with S-22.|||Strong loss of ubiquitin ligase activity; when associated with S-25.|||Tripartite motif-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056197|||http://purl.uniprot.org/annotation/VAR_052124|||http://purl.uniprot.org/annotation/VSP_005758|||http://purl.uniprot.org/annotation/VSP_005759|||http://purl.uniprot.org/annotation/VSP_044780|||http://purl.uniprot.org/annotation/VSP_044781
http://togogenome.org/gene/9606:ITK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08881                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||Complete loss of interaction with PPIA/CYPA.|||In LPFS1; shows nearly undetectable mutant ITK protein consistent with severe protein instability.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||PH|||Phosphoserine|||Phosphotyrosine; by LCK|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Tyrosine-protein kinase ITK/TSK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088106|||http://purl.uniprot.org/annotation/VAR_041710|||http://purl.uniprot.org/annotation/VAR_041711|||http://purl.uniprot.org/annotation/VAR_041712|||http://purl.uniprot.org/annotation/VAR_041713|||http://purl.uniprot.org/annotation/VAR_041714|||http://purl.uniprot.org/annotation/VAR_051696|||http://purl.uniprot.org/annotation/VAR_063424
http://togogenome.org/gene/9606:LILRA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI73                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Leukocyte immunoglobulin-like receptor subfamily A member 5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318708|||http://purl.uniprot.org/annotation/VSP_031276|||http://purl.uniprot.org/annotation/VSP_031277
http://togogenome.org/gene/9606:MED21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAW0|||http://purl.uniprot.org/uniprot/Q13503                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Sequence Conflict                                                                                  ^@                                                                                  Mediator of RNA polymerase II transcription subunit 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096375
http://togogenome.org/gene/9606:RNF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDP2|||http://purl.uniprot.org/uniprot/A0A0S2Z4G9|||http://purl.uniprot.org/uniprot/Q9Y252                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF6|||Found in an esophageal cancer sample; esophageal squamous cell carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056047|||http://purl.uniprot.org/annotation/VAR_034465|||http://purl.uniprot.org/annotation/VAR_052094|||http://purl.uniprot.org/annotation/VAR_052095|||http://purl.uniprot.org/annotation/VAR_063490|||http://purl.uniprot.org/annotation/VAR_063491|||http://purl.uniprot.org/annotation/VAR_063492|||http://purl.uniprot.org/annotation/VAR_063493|||http://purl.uniprot.org/annotation/VAR_063494|||http://purl.uniprot.org/annotation/VSP_055424|||http://purl.uniprot.org/annotation/VSP_055425|||http://purl.uniprot.org/annotation/VSP_055426|||http://purl.uniprot.org/annotation/VSP_055427
http://togogenome.org/gene/9606:SLC44A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTF4|||http://purl.uniprot.org/uniprot/E9PIC5|||http://purl.uniprot.org/uniprot/Q8N4M1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Choline transporter-like protein 3|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5 and isoform 6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191720|||http://purl.uniprot.org/annotation/VAR_023405|||http://purl.uniprot.org/annotation/VAR_064752|||http://purl.uniprot.org/annotation/VSP_036151|||http://purl.uniprot.org/annotation/VSP_036152|||http://purl.uniprot.org/annotation/VSP_044713|||http://purl.uniprot.org/annotation/VSP_045974
http://togogenome.org/gene/9606:DNAH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI6|||http://purl.uniprot.org/uniprot/Q9P2D7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||CFDEFNR motif|||Disordered|||Dynein axonemal heavy chain 1|||Dynein heavy chain 3 AAA+ lid|||Dynein heavy chain AAA 5 extension|||Dynein heavy chain AAA lid|||Dynein heavy chain AAA module D4|||Dynein heavy chain ATP-binding dynein motor region|||Dynein heavy chain C-terminal|||Dynein heavy chain coiled coil stalk|||Dynein heavy chain hydrolytic ATP-binding dynein motor region|||Dynein heavy chain linker|||Dynein heavy chain region D6 P-loop|||GPAGTGKT motif|||In CILD37.|||In SPGF18.|||In SPGF18; unknown pathological significance.|||In isoform 3.|||In isoform 6.|||In isoform 7.|||Polar residues|||Pro residues|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318936|||http://purl.uniprot.org/annotation/VAR_038912|||http://purl.uniprot.org/annotation/VAR_038913|||http://purl.uniprot.org/annotation/VAR_038914|||http://purl.uniprot.org/annotation/VAR_038915|||http://purl.uniprot.org/annotation/VAR_062176|||http://purl.uniprot.org/annotation/VAR_064924|||http://purl.uniprot.org/annotation/VAR_079510|||http://purl.uniprot.org/annotation/VAR_079511|||http://purl.uniprot.org/annotation/VAR_079512|||http://purl.uniprot.org/annotation/VAR_080888|||http://purl.uniprot.org/annotation/VAR_080889|||http://purl.uniprot.org/annotation/VAR_080890|||http://purl.uniprot.org/annotation/VAR_080891|||http://purl.uniprot.org/annotation/VAR_080892|||http://purl.uniprot.org/annotation/VAR_080893|||http://purl.uniprot.org/annotation/VAR_080894|||http://purl.uniprot.org/annotation/VAR_080895|||http://purl.uniprot.org/annotation/VAR_080896|||http://purl.uniprot.org/annotation/VAR_080897|||http://purl.uniprot.org/annotation/VAR_080898|||http://purl.uniprot.org/annotation/VAR_080899|||http://purl.uniprot.org/annotation/VAR_080900|||http://purl.uniprot.org/annotation/VAR_080901|||http://purl.uniprot.org/annotation/VAR_080902|||http://purl.uniprot.org/annotation/VSP_031305|||http://purl.uniprot.org/annotation/VSP_031306|||http://purl.uniprot.org/annotation/VSP_059797|||http://purl.uniprot.org/annotation/VSP_059798|||http://purl.uniprot.org/annotation/VSP_059799|||http://purl.uniprot.org/annotation/VSP_059800
http://togogenome.org/gene/9606:ALKBH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NS38                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of PCNA-binding.|||DNA oxidative demethylase ALKBH2|||Decreases activity toward N1-methyladenine adduct in either ssDNA or dsDNA.|||Decreases activity toward N1-methyladenine adduct in ssDNA. Has no effect on lesion repair in dsDNA.|||Decreases activity.|||Disordered|||Fe2OG dioxygenase|||Found in a patient with endometrial cancer; slightly decreased PCNA-binding.|||Impairs PCNA-binding. No effect on PCNA-binding; when associated with R-7.|||In isoform 2.|||Increased PCNA-binding.|||Leads to cytoplasmic relocalization.|||Loss of activity associated with decreased rDNA transcription.|||Loss of activity toward N1-methyladenine adduct in either ssDNA or dsDNA.|||Loss of activity toward N1-methyladenine adduct in either ssDNA or dsDNA; when associated with A-102.|||Loss of activity.|||No effect on PCNA-binding.|||No effect on PCNA-binding; when associated with K-3.|||PCNA-binding|||Strong decrease in PCNA-binding.|||Strong decrease of activity toward N1-methyladenine adduct in both ssDNA and dsDNA substrates.|||Strong decrease of activity toward N1-methyladenine adduct in ssDNA. Has no effect on lesion repair in dsDNA.|||Strong decrease of activity toward N1-methyladenine adduct. Loss of activity toward N1-methyladenine adduct in either ssDNA or dsDNA; when associated with G-101.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239275|||http://purl.uniprot.org/annotation/VAR_048223|||http://purl.uniprot.org/annotation/VAR_086049|||http://purl.uniprot.org/annotation/VAR_086050|||http://purl.uniprot.org/annotation/VSP_042923
http://togogenome.org/gene/9606:SETX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z333                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with EXOSC9 and UBE2I and decreases sumoylation.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ALS4.|||In ALS4; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation and ubiquitination; does not inhibit homodimerization; unlike the wild-type protein the mutant induces interaction with C14orf178.|||In ALS4; heterozygous; does not affect the interaction with EXOSC9 and UBE2I; does not decrease sumoylation.|||In ALS4; likely benign variant.|||In SCAN2.|||In SCAN2; abolishes interaction with EXOSC9; does not abolish interaction with UBE2I; decreases sumoylation.|||In SCAN2; atypical; associated with D-603.|||In SCAN2; atypical; associated with K-653.|||In SCAN2; heterozygous in a British family.|||In isoform 3.|||In isoform 4.|||Necessary for nuclear localization|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable helicase senataxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080724|||http://purl.uniprot.org/annotation/VAR_018776|||http://purl.uniprot.org/annotation/VAR_018777|||http://purl.uniprot.org/annotation/VAR_018778|||http://purl.uniprot.org/annotation/VAR_018779|||http://purl.uniprot.org/annotation/VAR_018780|||http://purl.uniprot.org/annotation/VAR_018781|||http://purl.uniprot.org/annotation/VAR_018782|||http://purl.uniprot.org/annotation/VAR_018783|||http://purl.uniprot.org/annotation/VAR_018784|||http://purl.uniprot.org/annotation/VAR_018785|||http://purl.uniprot.org/annotation/VAR_018786|||http://purl.uniprot.org/annotation/VAR_018787|||http://purl.uniprot.org/annotation/VAR_018788|||http://purl.uniprot.org/annotation/VAR_018789|||http://purl.uniprot.org/annotation/VAR_018790|||http://purl.uniprot.org/annotation/VAR_018791|||http://purl.uniprot.org/annotation/VAR_018792|||http://purl.uniprot.org/annotation/VAR_018793|||http://purl.uniprot.org/annotation/VAR_036646|||http://purl.uniprot.org/annotation/VAR_036647|||http://purl.uniprot.org/annotation/VAR_036648|||http://purl.uniprot.org/annotation/VAR_036649|||http://purl.uniprot.org/annotation/VAR_036650|||http://purl.uniprot.org/annotation/VAR_056208|||http://purl.uniprot.org/annotation/VAR_059458|||http://purl.uniprot.org/annotation/VAR_071682|||http://purl.uniprot.org/annotation/VAR_071683|||http://purl.uniprot.org/annotation/VAR_071684|||http://purl.uniprot.org/annotation/VAR_071685|||http://purl.uniprot.org/annotation/VAR_071686|||http://purl.uniprot.org/annotation/VAR_071687|||http://purl.uniprot.org/annotation/VAR_071688|||http://purl.uniprot.org/annotation/VAR_072587|||http://purl.uniprot.org/annotation/VAR_072588|||http://purl.uniprot.org/annotation/VSP_017124|||http://purl.uniprot.org/annotation/VSP_028826
http://togogenome.org/gene/9606:PDGFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYY3|||http://purl.uniprot.org/uniprot/P01127                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic residues|||Disordered|||In IBGC5; loss of protein expression.|||In isoform 2.|||Interchain|||Involved in receptor binding|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor (PDGF) family profile|||Platelet-derived growth factor subunit B|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023371|||http://purl.uniprot.org/annotation/PRO_0000023372|||http://purl.uniprot.org/annotation/PRO_0000023373|||http://purl.uniprot.org/annotation/PRO_5017417476|||http://purl.uniprot.org/annotation/VAR_014578|||http://purl.uniprot.org/annotation/VAR_070870|||http://purl.uniprot.org/annotation/VAR_070871|||http://purl.uniprot.org/annotation/VSP_044913
http://togogenome.org/gene/9606:ZNF419                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HQ0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 5.|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||KRAB|||Zinc finger protein 419                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047574|||http://purl.uniprot.org/annotation/VAR_046651|||http://purl.uniprot.org/annotation/VAR_046652|||http://purl.uniprot.org/annotation/VSP_016033|||http://purl.uniprot.org/annotation/VSP_016034|||http://purl.uniprot.org/annotation/VSP_046149|||http://purl.uniprot.org/annotation/VSP_047106
http://togogenome.org/gene/9606:GRIN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8D9PHB2|||http://purl.uniprot.org/uniprot/Q13224                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and slowed response rise time and deactivation time course.|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Found in a patient with Landau-Kleffner syndrome; unknown pathological significance.|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||Functional determinant of NMDA receptors|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 2B|||Helical|||In DEE27; decreased protein abundance; decreased localization to the cell membrane; increased glutamate-gated calcium ion channel activity via an allosteric effect which is characterized by increased glutamate and glycine potency and increased open probability; the mutant channel is less sensitive to magnesium inhibition and has increased calcium permeability compared to wild-type.|||In DEE27; severe phenotype with early onset seizures; gain of function mutation; results in neuronal hyperexcitability; the mutant channel is not inhibited by magnesium and has increased calcium permeability compared to wild-type.|||In DEE27; unknown pathological significance.|||In MRD6.|||In MRD6; decreased protein abundance; decreased localization to the cell membrane.|||In MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by decreased glutamate potency.|||In MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency and increased open probability.|||In MRD6; decreased protein abundance; decreased localization to the cell membrane; changed glutamate-gated calcium ion channel activity characterized by increased glutamate and glycine potency.|||In MRD6; decreased protein abundance; decreased localization to the cell membrane; decreased glutamate-gated calcium ion channel activity characterized by decreased glutamate potency and increased glycine potency.|||In MRD6; decreased protein abundance; no effect on localization to the cell membrane; no significant effect on calcium ion transmembrane import into cytosol; analysis of agonist dose-response curves for glutamate and glycine are not consistent.|||In MRD6; no effect on localization to the cell membrane; loss of glutamate-gated calcium ion channel activity.|||Increased glutamate and glycine agonist potency.|||Interaction with DAPK1|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphoserine; by DAPK1|||Phosphotyrosine|||Polar residues|||Pore-forming|||Probable disease-associated variant found in a patient with autism spectrum disorder.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011577|||http://purl.uniprot.org/annotation/PRO_5033969783|||http://purl.uniprot.org/annotation/VAR_011317|||http://purl.uniprot.org/annotation/VAR_065900|||http://purl.uniprot.org/annotation/VAR_069384|||http://purl.uniprot.org/annotation/VAR_072663|||http://purl.uniprot.org/annotation/VAR_072664|||http://purl.uniprot.org/annotation/VAR_072665|||http://purl.uniprot.org/annotation/VAR_076764|||http://purl.uniprot.org/annotation/VAR_078235|||http://purl.uniprot.org/annotation/VAR_078236|||http://purl.uniprot.org/annotation/VAR_078647|||http://purl.uniprot.org/annotation/VAR_079943|||http://purl.uniprot.org/annotation/VAR_079944|||http://purl.uniprot.org/annotation/VAR_079945|||http://purl.uniprot.org/annotation/VAR_079946|||http://purl.uniprot.org/annotation/VAR_079947|||http://purl.uniprot.org/annotation/VAR_079948|||http://purl.uniprot.org/annotation/VAR_079949|||http://purl.uniprot.org/annotation/VAR_079950|||http://purl.uniprot.org/annotation/VAR_079951|||http://purl.uniprot.org/annotation/VAR_079952|||http://purl.uniprot.org/annotation/VAR_079953|||http://purl.uniprot.org/annotation/VAR_079954|||http://purl.uniprot.org/annotation/VAR_079955|||http://purl.uniprot.org/annotation/VAR_079956|||http://purl.uniprot.org/annotation/VAR_079957
http://togogenome.org/gene/9606:CXCL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43927|||http://purl.uniprot.org/uniprot/Q53X90                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Non-terminal Residue|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-X-C motif chemokine|||C-X-C motif chemokine 13|||Chemokine interleukin-8-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005113|||http://purl.uniprot.org/annotation/PRO_5014205859
http://togogenome.org/gene/9606:CHCHD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U9EWT9|||http://purl.uniprot.org/uniprot/Q9BSY4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Splice Variant|||Turn                                                                                  ^@                                                                                  CHCH|||CHCH 1|||CHCH 2|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 5|||Cx9C motif 1|||Cx9C motif 2|||Cx9C motif 3|||Cx9C motif 4|||IMS import disulfide relay-system CHCH-CHCH-like Cx9C|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129167|||http://purl.uniprot.org/annotation/VSP_056577
http://togogenome.org/gene/9606:SIPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FS4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056744|||http://purl.uniprot.org/annotation/VAR_049148|||http://purl.uniprot.org/annotation/VAR_049149|||http://purl.uniprot.org/annotation/VAR_049150|||http://purl.uniprot.org/annotation/VAR_049151
http://togogenome.org/gene/9606:BCKDHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12694|||http://purl.uniprot.org/uniprot/Q59EI3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial|||Dehydrogenase E1 component|||Disordered|||In MSUD1A.|||In MSUD1A; decreased 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; decreased solubility; loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; unknown pathological significance; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; unknown pathological significance; decreased solubility; changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; unknown pathological significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; unknown pathological significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; decreased affinity for the cofactor thiamine diphosphate; decreased 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1A; unknown pathological significance; no effect on solubility; no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020465|||http://purl.uniprot.org/annotation/VAR_004968|||http://purl.uniprot.org/annotation/VAR_004969|||http://purl.uniprot.org/annotation/VAR_004970|||http://purl.uniprot.org/annotation/VAR_004971|||http://purl.uniprot.org/annotation/VAR_004972|||http://purl.uniprot.org/annotation/VAR_004973|||http://purl.uniprot.org/annotation/VAR_015101|||http://purl.uniprot.org/annotation/VAR_015102|||http://purl.uniprot.org/annotation/VAR_034360|||http://purl.uniprot.org/annotation/VAR_034361|||http://purl.uniprot.org/annotation/VAR_069748|||http://purl.uniprot.org/annotation/VAR_069749|||http://purl.uniprot.org/annotation/VAR_069750|||http://purl.uniprot.org/annotation/VAR_069751|||http://purl.uniprot.org/annotation/VAR_069752|||http://purl.uniprot.org/annotation/VAR_088268|||http://purl.uniprot.org/annotation/VAR_088269|||http://purl.uniprot.org/annotation/VAR_088270|||http://purl.uniprot.org/annotation/VAR_088271|||http://purl.uniprot.org/annotation/VAR_088272|||http://purl.uniprot.org/annotation/VAR_088273|||http://purl.uniprot.org/annotation/VAR_088274|||http://purl.uniprot.org/annotation/VSP_056156|||http://purl.uniprot.org/annotation/VSP_056157
http://togogenome.org/gene/9606:SOAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75908                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished cholesterol O-acyltransferase activity.|||Abolished ubiquitination and sterol-regulated stabilization.|||Basic and acidic residues|||Cysteine sulfenic acid (-SOH); alternate|||Cytoplasmic|||Disordered|||Does not affect ubiquitination and sterol-regulated stabilization.|||Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-279.|||Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-54.|||FYXDWWN motif|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-100, R-102, R-108, R-242 and R-299.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-242.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-299.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-242 and R-299.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-108, R-242 and R-299.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-102, R-108, R-242 and R-299.|||In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-80, R-100, R-102, R-108, R-242 and R-299.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||Sterol O-acyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207645|||http://purl.uniprot.org/annotation/VAR_020373|||http://purl.uniprot.org/annotation/VAR_020374|||http://purl.uniprot.org/annotation/VSP_057158|||http://purl.uniprot.org/annotation/VSP_057159|||http://purl.uniprot.org/annotation/VSP_057160|||http://purl.uniprot.org/annotation/VSP_057161|||http://purl.uniprot.org/annotation/VSP_057162
http://togogenome.org/gene/9606:IGLL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A064                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C region|||Ig-like C1-type|||Immunoglobulin lambda-like polypeptide 5|||In isoform 2.|||J region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000405596|||http://purl.uniprot.org/annotation/VSP_040709|||http://purl.uniprot.org/annotation/VSP_040710
http://togogenome.org/gene/9606:C2orf66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXQ4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Uncharacterized protein C2orf66                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317179
http://togogenome.org/gene/9606:EDDM3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14507|||http://purl.uniprot.org/uniprot/W0UTC5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Epididymal secretory protein E3-alpha|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021188|||http://purl.uniprot.org/annotation/VAR_050968
http://togogenome.org/gene/9606:H4C14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:SLCO4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Solute carrier organic anion transporter family member 4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191067|||http://purl.uniprot.org/annotation/VAR_053678|||http://purl.uniprot.org/annotation/VAR_053679|||http://purl.uniprot.org/annotation/VSP_006152|||http://purl.uniprot.org/annotation/VSP_006153|||http://purl.uniprot.org/annotation/VSP_006154|||http://purl.uniprot.org/annotation/VSP_006155|||http://purl.uniprot.org/annotation/VSP_006156
http://togogenome.org/gene/9606:PRKCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIU5|||http://purl.uniprot.org/uniprot/B2R5T1|||http://purl.uniprot.org/uniprot/B7Z3W6|||http://purl.uniprot.org/uniprot/P05129                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||C2|||In SCA14.|||In isoform 2.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SYK|||Protein kinase|||Protein kinase C gamma type|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055689|||http://purl.uniprot.org/annotation/VAR_008755|||http://purl.uniprot.org/annotation/VAR_008756|||http://purl.uniprot.org/annotation/VAR_008757|||http://purl.uniprot.org/annotation/VAR_008758|||http://purl.uniprot.org/annotation/VAR_017060|||http://purl.uniprot.org/annotation/VAR_017061|||http://purl.uniprot.org/annotation/VAR_017062|||http://purl.uniprot.org/annotation/VAR_080740|||http://purl.uniprot.org/annotation/VAR_080741|||http://purl.uniprot.org/annotation/VSP_056467|||http://purl.uniprot.org/annotation/VSP_056468|||http://purl.uniprot.org/annotation/VSP_056469
http://togogenome.org/gene/9606:MYBPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAB1|||http://purl.uniprot.org/uniprot/B3KPP3|||http://purl.uniprot.org/uniprot/Q00872|||http://purl.uniprot.org/uniprot/Q86TA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In CMYP16; changes in electrostatic interactions resulting in increased myosin binding; no effect on actin binding.|||In CMYP16; decreased binding to myosin; no effect on actin binding.|||In CMYP16; no effects on myosin or actin binding; reduced helicity of certain domains.|||In DA1B.|||In DA1B; may affect splicing.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 7, isoform 8, isoform 9 and isoform 10.|||In isoform 4, isoform 5, isoform 8, isoform 9 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Myosin-binding protein C, slow-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072689|||http://purl.uniprot.org/annotation/VAR_021923|||http://purl.uniprot.org/annotation/VAR_067045|||http://purl.uniprot.org/annotation/VAR_067046|||http://purl.uniprot.org/annotation/VAR_075219|||http://purl.uniprot.org/annotation/VAR_083207|||http://purl.uniprot.org/annotation/VAR_083208|||http://purl.uniprot.org/annotation/VAR_083209|||http://purl.uniprot.org/annotation/VAR_083210|||http://purl.uniprot.org/annotation/VSP_039105|||http://purl.uniprot.org/annotation/VSP_039106|||http://purl.uniprot.org/annotation/VSP_045241|||http://purl.uniprot.org/annotation/VSP_046735|||http://purl.uniprot.org/annotation/VSP_046736|||http://purl.uniprot.org/annotation/VSP_046737|||http://purl.uniprot.org/annotation/VSP_046738|||http://purl.uniprot.org/annotation/VSP_046739|||http://purl.uniprot.org/annotation/VSP_046740
http://togogenome.org/gene/9606:TMEM70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUB7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC5DN2.|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Transmembrane protein 70, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251472|||http://purl.uniprot.org/annotation/VAR_027686|||http://purl.uniprot.org/annotation/VAR_027687|||http://purl.uniprot.org/annotation/VAR_027688|||http://purl.uniprot.org/annotation/VAR_034565|||http://purl.uniprot.org/annotation/VAR_068847|||http://purl.uniprot.org/annotation/VSP_020759|||http://purl.uniprot.org/annotation/VSP_054227|||http://purl.uniprot.org/annotation/VSP_054228
http://togogenome.org/gene/9606:WNT5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1J7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-5b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041434
http://togogenome.org/gene/9606:G0S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27469                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||G0/G1 switch protein 2|||No effect on BCL2-binding; when associated with A-35.|||No effect on BCL2-binding; when associated with A-36.|||No effect on BCL2-binding; when associated with A-38.|||No effect on BCL2-binding; when associated with A-39.|||No effect on BCL2-binding; when associated with A-43.|||No effect on BCL2-binding; when associated with A-44.|||No effect on BCL2-binding; when associated with A-45.|||No effect on BCL2-binding; when associated with A-46.|||Reduced BCL2-binding and reduced pro-apoptotic activity; when associated with A-57. No effect on mitochondrial localization; when associated with A-57.|||Reduced BCL2-binding and reduced pro-apoptotic activity; when associated with A-58. No effect on mitochondrial localization; when associated with A-58.|||Reduced BCL2-binding; when associated with A-50.|||Reduced BCL2-binding; when associated with A-51.|||Reduced BCL2-binding; when associated with A-54.|||Reduced BCL2-binding; when associated with A-55.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087405
http://togogenome.org/gene/9606:CDK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50750                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates autophosphorylation; no effect on kinase activity, but impaired CTD phosphorylation.|||Abrogates kinase activity.|||Constitutive kinase activity.|||Cyclin-dependent kinase 9|||Decreased acetylation; leading to enhanced protein kinase activity.|||Disordered|||Found in patients with global developmental delay and epilepsy with history of choanal atresia; unknown pathological significance.|||Impaired kinase and transcriptional elongation activities, but normal cyclin T1 and HEXIM1 binding.|||In isoform 2.|||Loss of autophosphorylation and impaired interaction with HIVTAT.|||Mimics acetylation; leading to impaired protein kinase activity.|||Mimics autophosphorylation and promotes interaction with HIVTAT.|||Mimics autophosphorylation; constitutive kinase activity, independently of calcium signaling.|||Mimics phosphorylation, constitutive loss of kinase activity.|||N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A|||N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A|||Phosphoserine|||Phosphoserine; by CDK9|||Phosphoserine; by CDK9 and PKA|||Phosphothreonine|||Phosphothreonine; by CDK9|||Phosphothreonine; by CaMK1D|||Polar residues|||Protein kinase|||Proton acceptor|||T-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085800|||http://purl.uniprot.org/annotation/VAR_013456|||http://purl.uniprot.org/annotation/VAR_041982|||http://purl.uniprot.org/annotation/VAR_082140|||http://purl.uniprot.org/annotation/VSP_016288
http://togogenome.org/gene/9606:RFX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48378                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-binding protein RFX2|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||RFX-type winged-helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215288|||http://purl.uniprot.org/annotation/VAR_036530|||http://purl.uniprot.org/annotation/VAR_036531|||http://purl.uniprot.org/annotation/VAR_057151|||http://purl.uniprot.org/annotation/VAR_058416|||http://purl.uniprot.org/annotation/VSP_037811
http://togogenome.org/gene/9606:TMCO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane and coiled-coil domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305149|||http://purl.uniprot.org/annotation/VAR_035169|||http://purl.uniprot.org/annotation/VAR_035170|||http://purl.uniprot.org/annotation/VSP_028242
http://togogenome.org/gene/9606:UQCRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31930                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 1, mitochondrial|||In PKNPY.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026786|||http://purl.uniprot.org/annotation/VAR_013629|||http://purl.uniprot.org/annotation/VAR_034581|||http://purl.uniprot.org/annotation/VAR_085428|||http://purl.uniprot.org/annotation/VAR_085429
http://togogenome.org/gene/9606:ELOVL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB03                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Elongation of very long chain fatty acids protein 3|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207540
http://togogenome.org/gene/9606:FHOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A068F7M9|||http://purl.uniprot.org/uniprot/Q9Y613                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DAD|||Disordered|||FH1|||FH1/FH2 domain-containing protein 1|||FH2|||GBD/FH3|||Interaction with ROCK1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194905
http://togogenome.org/gene/9606:CFAP52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1V2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 52|||In HTX10; loss of panaxonemal expression in respiratory cilia.|||In isoform 2.|||In isoform 3.|||WD 1|||WD 10|||WD 11|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233153|||http://purl.uniprot.org/annotation/VAR_026057|||http://purl.uniprot.org/annotation/VAR_085332|||http://purl.uniprot.org/annotation/VSP_018067|||http://purl.uniprot.org/annotation/VSP_018068
http://togogenome.org/gene/9606:PPIAL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y536                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324640
http://togogenome.org/gene/9606:ZNF354B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Polar residues|||Zinc finger protein 354B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280406
http://togogenome.org/gene/9606:CRIPTO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H1T8|||http://purl.uniprot.org/uniprot/P13385                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Alters the localization and decreases the biological activity.|||EGF-like|||GPI-anchor amidated aspartate|||N-linked (GlcNAc...) asparagine|||Protein Cripto|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007503|||http://purl.uniprot.org/annotation/PRO_0000395410|||http://purl.uniprot.org/annotation/VAR_021903|||http://purl.uniprot.org/annotation/VAR_024262|||http://purl.uniprot.org/annotation/VAR_048975
http://togogenome.org/gene/9606:NPIPA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PKD4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Nuclear pore complex-interacting protein family member A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423918|||http://purl.uniprot.org/annotation/VSP_056345|||http://purl.uniprot.org/annotation/VSP_056346
http://togogenome.org/gene/9606:TXNIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3M7                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interchain|||Phosphoserine|||Thioredoxin-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250489|||http://purl.uniprot.org/annotation/VAR_048334|||http://purl.uniprot.org/annotation/VSP_054401
http://togogenome.org/gene/9606:KIF27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kinesin motor|||Kinesin-like protein KIF27|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307143|||http://purl.uniprot.org/annotation/VAR_035361|||http://purl.uniprot.org/annotation/VAR_035362|||http://purl.uniprot.org/annotation/VAR_061286|||http://purl.uniprot.org/annotation/VSP_028602|||http://purl.uniprot.org/annotation/VSP_028603|||http://purl.uniprot.org/annotation/VSP_028604|||http://purl.uniprot.org/annotation/VSP_028605|||http://purl.uniprot.org/annotation/VSP_028606
http://togogenome.org/gene/9606:SLC4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04920|||http://purl.uniprot.org/uniprot/Q59GF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Anion exchange protein 2|||Band 3 cytoplasmic|||Basic and acidic residues|||Bicarbonate transporter-like transmembrane|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with autosomal recessive osteopetrosis; unknown pathological significance; reduced chloride:bicarbonate antiporter activity; impaired dynamic organization of podosome in osteoclasts; failure to rescue impaired osteoclast differentiation when expressed in a Slc4a2-knockdown mouse macrophage cell line RAW 264.7.|||Helical|||In isoform B1.|||In isoform B2.|||Membrane (anion exchange)|||N-linked (GlcNAc...) asparagine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079215|||http://purl.uniprot.org/annotation/VAR_025168|||http://purl.uniprot.org/annotation/VAR_025169|||http://purl.uniprot.org/annotation/VAR_025170|||http://purl.uniprot.org/annotation/VAR_025171|||http://purl.uniprot.org/annotation/VAR_087349|||http://purl.uniprot.org/annotation/VAR_087350|||http://purl.uniprot.org/annotation/VSP_000456|||http://purl.uniprot.org/annotation/VSP_045953
http://togogenome.org/gene/9606:MSRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Methionine-R-sulfoxide reductase B2, mitochondrial|||Mitochondrion|||MsrB|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140324|||http://purl.uniprot.org/annotation/VAR_050448
http://togogenome.org/gene/9606:MORN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PF18                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interaction with MDM2|||Interaction with SIRT1|||Interaction with TP53|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN repeat-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247459|||http://purl.uniprot.org/annotation/VSP_019996|||http://purl.uniprot.org/annotation/VSP_019997
http://togogenome.org/gene/9606:TIMM44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43615                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit TIM44|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034314
http://togogenome.org/gene/9606:TEKTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYK2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Phosphotyrosine|||Tektin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279391|||http://purl.uniprot.org/annotation/VAR_030875|||http://purl.uniprot.org/annotation/VAR_030876|||http://purl.uniprot.org/annotation/VAR_030877|||http://purl.uniprot.org/annotation/VAR_056774|||http://purl.uniprot.org/annotation/VAR_056775
http://togogenome.org/gene/9606:APPBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92624                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Amyloid protein-binding protein 2|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106259|||http://purl.uniprot.org/annotation/VAR_052606
http://togogenome.org/gene/9606:ERGIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969X5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endoplasmic reticulum-Golgi intermediate compartment protein 1|||Helical|||In AMC2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087023|||http://purl.uniprot.org/annotation/VAR_080480|||http://purl.uniprot.org/annotation/VSP_011560|||http://purl.uniprot.org/annotation/VSP_011561|||http://purl.uniprot.org/annotation/VSP_011562|||http://purl.uniprot.org/annotation/VSP_011563|||http://purl.uniprot.org/annotation/VSP_011564
http://togogenome.org/gene/9606:LCE6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A183                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 6A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313639
http://togogenome.org/gene/9606:SULT2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K015|||http://purl.uniprot.org/uniprot/Q06520                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Completely eliminates the substrate inhibition when ADT is used as substrate. Partially eliminates substrate inhibition when DHEA is used as substrate. Completely eliminates the substrate inhibition for DHEA, when associated with I-137.|||Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone.|||Decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone.|||Phosphoserine|||Proton acceptor|||Strongly reduces substrate inhibition when ADT or DHEA are used as substrates.|||Substrate inhibition is completely eliminated for DHEA; when associated with A-238.|||Sulfating activity toward both DHEA and pregnenolone is completely abolished.|||Sulfotransferase|||Sulfotransferase 2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085141|||http://purl.uniprot.org/annotation/VAR_052520|||http://purl.uniprot.org/annotation/VAR_052521|||http://purl.uniprot.org/annotation/VAR_083881|||http://purl.uniprot.org/annotation/VAR_083882|||http://purl.uniprot.org/annotation/VAR_083883|||http://purl.uniprot.org/annotation/VAR_083884|||http://purl.uniprot.org/annotation/VAR_083885|||http://purl.uniprot.org/annotation/VAR_083886|||http://purl.uniprot.org/annotation/VAR_083887
http://togogenome.org/gene/9606:RPS27L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71UM5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Disordered|||Ribosomal protein eS27-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149054
http://togogenome.org/gene/9606:DIRAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95661                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||GTP-binding protein Di-Ras3|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191654|||http://purl.uniprot.org/annotation/PRO_0000370781
http://togogenome.org/gene/9606:MCOLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDD5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-108 and N-111.|||Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-108 and N-112.|||Abolishes basal channel activity without affecting channel activation by a synthetic agonist; when associated with N-111 and N-112.|||Abolishes channel activity.|||Constitutive active channel; abolishes inhibition by lumenal H(+); increases the pore diameter.|||Constitutive active channel; abolishes inhibition by lumenal H(+); retains the Ca(2+)-dependent inactivation of the Ca(2+) current. Decreases inhibition by lumenal H(+); when associated with A-252. Decreases inhibition by lumenal H(+); when associated with A-273.|||Constitutive active channel; greatly impairs inhibition by lumenal Na(+).|||Cytoplasmic|||Decreases in Ca(2+) permeability and selectivity; decreases channel pore dynamic behavior.|||Enhances endocytosis.|||Extracellular|||Extracellular/lumenal pore loop|||Helical|||In isoform 2.|||Increases inhibition by lumenal H(+).|||Increases inhibition by lumenal H(+). Decreases inhibition by lumenal H(+); when associated with A-283.|||Interaction with phosphoinositides|||Mucolipin-3|||N-linked (GlcNAc...) asparagine|||Nearly abolishes channel activation by a synthetic agonist.|||Nearly abolishes channel activity; inhibits starvation-induced autophagy.|||Pore-forming|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215367|||http://purl.uniprot.org/annotation/VSP_010823
http://togogenome.org/gene/9606:LONP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36776                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes ATPase activity, and presumably ATP-driven protein unfolding, but does not block access to the proteolytic active site or prevent a substrate from binding to it.|||Basic and acidic residues|||Disordered|||Enhances the basal, but not the stimulated ATPase activity, and abolishes peptidase activity.|||Enhances the basal, but not the stimulated ATPase activity, and retains peptidase activity.|||Enhances the basal, but not the stimulated ATPase activity.|||Has low basal, but normal stimulated ATPase activity, and retains peptidase activity.|||Has normal basal, but low stimulated ATPase activity, and abolishes peptidase activity.|||In CODASS.|||In isoform 2.|||In isoform 3.|||Lacks both ATPase and protease activity, but retains DNA binding activity.|||Lon N-terminal|||Lon protease homolog, mitochondrial|||Lon proteolytic|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026734|||http://purl.uniprot.org/annotation/VAR_051564|||http://purl.uniprot.org/annotation/VAR_051565|||http://purl.uniprot.org/annotation/VAR_067708|||http://purl.uniprot.org/annotation/VAR_067709|||http://purl.uniprot.org/annotation/VAR_073338|||http://purl.uniprot.org/annotation/VAR_073339|||http://purl.uniprot.org/annotation/VAR_073340|||http://purl.uniprot.org/annotation/VAR_073341|||http://purl.uniprot.org/annotation/VAR_073342|||http://purl.uniprot.org/annotation/VAR_073343|||http://purl.uniprot.org/annotation/VAR_073344|||http://purl.uniprot.org/annotation/VAR_073345|||http://purl.uniprot.org/annotation/VAR_073346|||http://purl.uniprot.org/annotation/VAR_073347|||http://purl.uniprot.org/annotation/VAR_073348|||http://purl.uniprot.org/annotation/VSP_054617|||http://purl.uniprot.org/annotation/VSP_055310
http://togogenome.org/gene/9606:GAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05329|||http://purl.uniprot.org/uniprot/Q5VZ30                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glutamate decarboxylase 2|||N6-(pyridoxal phosphate)lysine|||No effect on glutamate decarboxylase activity.|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146968|||http://purl.uniprot.org/annotation/VAR_018821|||http://purl.uniprot.org/annotation/VAR_018822|||http://purl.uniprot.org/annotation/VAR_018823|||http://purl.uniprot.org/annotation/VAR_018824|||http://purl.uniprot.org/annotation/VAR_029176|||http://purl.uniprot.org/annotation/VAR_029177|||http://purl.uniprot.org/annotation/VAR_029178
http://togogenome.org/gene/9606:KRTAP23-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A580                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 23-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290066
http://togogenome.org/gene/9606:PPIH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43447|||http://purl.uniprot.org/uniprot/Q6FH36                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes inhibition by cyclosporin A.|||In isoform 2.|||N-acetylalanine|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase H|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064162|||http://purl.uniprot.org/annotation/VSP_056587
http://togogenome.org/gene/9606:ADCY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSC1|||http://purl.uniprot.org/uniprot/B7ZLX9|||http://purl.uniprot.org/uniprot/O60266                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 3|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Guanylate cyclase|||Helical|||In OBESITY; risk factor.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by CaMK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195687|||http://purl.uniprot.org/annotation/VAR_048248|||http://purl.uniprot.org/annotation/VAR_080791|||http://purl.uniprot.org/annotation/VAR_080792|||http://purl.uniprot.org/annotation/VSP_055813|||http://purl.uniprot.org/annotation/VSP_055814|||http://purl.uniprot.org/annotation/VSP_055815
http://togogenome.org/gene/9606:SMN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP61|||http://purl.uniprot.org/uniprot/E7EQZ4|||http://purl.uniprot.org/uniprot/Q16637                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs GEMIN2 binding.|||Impairs GEMIN8 binding.|||Impairs SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4. Abolishes interaction with SNRPD1 and SNRPD3. Impairs binding to substrate containing dimethylated arginine.|||Impairs binding to substrate containing dimethylated arginine.|||Impairs homooligomerization and GEMIN8 binding.|||Impairs homooligomerization.|||In SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization.|||In SMA1; abolishes the interaction with ELAVL4.|||In SMA1; slightly reduces SMN binding to RPP20/POP7. Impairs homooligomerization and axon localization.|||In SMA2 and SMA3.|||In SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization.|||In SMA2.|||In SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4.|||In SMA3.|||In SMA3; impairs GEMIN2 binding.|||In SMA3; impairs homooligomerization..|||In SMA3; reduces SMN binding to Sm proteins.|||In SMA3; slightly reduces SMN binding to RPP20/POP7.|||In isoform SMN-delta5 and isoform SMN-delta57.|||In isoform SMN-delta7 and isoform SMN-delta57.|||Interacts with GEMIN2|||Involved in homooligomerization|||N-acetylalanine|||P2 (binding site for SNRPB)|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues|||Pro residues|||Removed|||Required for interaction with RPP20/POP7|||Required for interaction with SYNCRIP|||Survival motor neuron Tudor|||Survival motor neuron protein|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218903|||http://purl.uniprot.org/annotation/VAR_005615|||http://purl.uniprot.org/annotation/VAR_005616|||http://purl.uniprot.org/annotation/VAR_005617|||http://purl.uniprot.org/annotation/VAR_005618|||http://purl.uniprot.org/annotation/VAR_005619|||http://purl.uniprot.org/annotation/VAR_005620|||http://purl.uniprot.org/annotation/VAR_007990|||http://purl.uniprot.org/annotation/VAR_010051|||http://purl.uniprot.org/annotation/VAR_034803|||http://purl.uniprot.org/annotation/VAR_034804|||http://purl.uniprot.org/annotation/VAR_034805|||http://purl.uniprot.org/annotation/VAR_034806|||http://purl.uniprot.org/annotation/VAR_034807|||http://purl.uniprot.org/annotation/VAR_034808|||http://purl.uniprot.org/annotation/VAR_034809|||http://purl.uniprot.org/annotation/VSP_006183|||http://purl.uniprot.org/annotation/VSP_006184|||http://purl.uniprot.org/annotation/VSP_006185
http://togogenome.org/gene/9606:PPP1R12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAH5|||http://purl.uniprot.org/uniprot/O14974                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Abolishes binding to the POLO box domains of PLK1.|||Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-472.|||Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-445 and A-910.|||Abolishes phosphorylation by NUAK1 and interaction with 14-3-3; when associated with A-472 and A-910.|||Basic and acidic residues|||Disordered|||In GUBS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with ROCK2|||KVKF motif|||Loss of binding to PRKG1; when associated with A-1007.|||Loss of binding to PRKG1; when associated with A-1014.|||Loss of binding to PRKG1; when associated with A-1021.|||Loss of binding to PRKG1; when associated with A-1028.|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by NUAK1|||Phosphoserine; by PKA and PKG; in vitro|||Phosphoserine; by ROCK2|||Phosphothreonine|||Phosphothreonine; by ROCK1, ROCK2, CDC42BP, ZIPK/DAPK3 and RAF1|||Phosphotyrosine|||Polar residues|||Protein phosphatase 1 regulatory subunit 12A|||cGMP-dependent protein kinase interacting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067025|||http://purl.uniprot.org/annotation/VAR_038949|||http://purl.uniprot.org/annotation/VAR_038950|||http://purl.uniprot.org/annotation/VAR_038951|||http://purl.uniprot.org/annotation/VAR_083871|||http://purl.uniprot.org/annotation/VAR_083872|||http://purl.uniprot.org/annotation/VAR_083873|||http://purl.uniprot.org/annotation/VAR_083874|||http://purl.uniprot.org/annotation/VAR_083875|||http://purl.uniprot.org/annotation/VSP_009251|||http://purl.uniprot.org/annotation/VSP_009252|||http://purl.uniprot.org/annotation/VSP_009253|||http://purl.uniprot.org/annotation/VSP_045079
http://togogenome.org/gene/9606:AK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VS11|||http://purl.uniprot.org/uniprot/P27144                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes mitochondrial import; when associated with G-4.|||Abolishes mitochondrial import; when associated with G-7.|||Adenylate kinase 4, mitochondrial|||Adenylate kinase active site lid|||LID|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NMP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158926
http://togogenome.org/gene/9606:HCFC1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWW0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Host cell factor C1 regulator 1|||In isoform 2.|||Interaction with HCFC1|||Loss of interaction with HCFC1.|||Nuclear export signal|||Reduces nuclear export.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338978|||http://purl.uniprot.org/annotation/VAR_043849|||http://purl.uniprot.org/annotation/VSP_034082
http://togogenome.org/gene/9606:WDR33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0J8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Collagen-like|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||pre-mRNA 3' end processing protein WDR33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051382|||http://purl.uniprot.org/annotation/VAR_046717|||http://purl.uniprot.org/annotation/VAR_053427|||http://purl.uniprot.org/annotation/VSP_041333|||http://purl.uniprot.org/annotation/VSP_041334|||http://purl.uniprot.org/annotation/VSP_042684|||http://purl.uniprot.org/annotation/VSP_042685
http://togogenome.org/gene/9606:WDR18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV38                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051365|||http://purl.uniprot.org/annotation/VAR_031577|||http://purl.uniprot.org/annotation/VAR_031578|||http://purl.uniprot.org/annotation/VAR_031579
http://togogenome.org/gene/9606:DEFA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01524                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Peptide|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Mass|||Mutagenesis Site|||Peptide|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Abrogates self-assembly to fibrils and attenuates agglutination of bacteria and prevention of L.monocytogenes invasion.|||Abrogates self-assembly to fibrils and attenuates agglutination of bacteria and prevention of L.monocytogenes invasion. Fails to block intestinal cell adhesion and biofilm formation of C.albicans.|||Defensin-6|||Does not impact fibril formation or agglutination of bacteria.|||Oxidized form.|||Perturbs self-assembly to fibrils and reduces agglutination of bacteria.|||Perturbs self-assembly to fibrils and reduces agglutination of bacteria. Does not abolish antimicrobial activity against B.adolescentis and formation of extracellular net-like structures (under reducing conditions).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006790|||http://purl.uniprot.org/annotation/PRO_0000006791
http://togogenome.org/gene/9606:DNAAF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK67|||http://purl.uniprot.org/uniprot/Q96MX6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dynein axonemal assembly factor 10|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301671|||http://purl.uniprot.org/annotation/VAR_053438|||http://purl.uniprot.org/annotation/VSP_045123
http://togogenome.org/gene/9606:ATP1B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform B.|||Nuclear|||Perinuclear space|||Protein ATP1B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219122|||http://purl.uniprot.org/annotation/VAR_055535|||http://purl.uniprot.org/annotation/VSP_000351
http://togogenome.org/gene/9606:OCM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CE72                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||N-acetylserine|||Oncomodulin-1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073582
http://togogenome.org/gene/9606:UBXN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mediates interaction with LMAN1|||PUB|||Phosphoserine|||Polar residues|||UBX|||UBX domain-containing protein 6|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211025|||http://purl.uniprot.org/annotation/VAR_047821|||http://purl.uniprot.org/annotation/VAR_061924|||http://purl.uniprot.org/annotation/VSP_007453
http://togogenome.org/gene/9606:NSUN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P11                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  28S rRNA (cytosine-C(5))-methyltransferase|||Abolished methyltransferase activity without affecting nucleolar localization; when associated with S-308.|||Abolished methyltransferase activity without affecting nucleolar localization; when associated with S-359.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylglycine|||Nucleophile|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261669|||http://purl.uniprot.org/annotation/VAR_051889|||http://purl.uniprot.org/annotation/VSP_021752|||http://purl.uniprot.org/annotation/VSP_021753|||http://purl.uniprot.org/annotation/VSP_021754|||http://purl.uniprot.org/annotation/VSP_021755|||http://purl.uniprot.org/annotation/VSP_021756|||http://purl.uniprot.org/annotation/VSP_043352|||http://purl.uniprot.org/annotation/VSP_045492
http://togogenome.org/gene/9606:NUS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E22                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  3.5-fold reduction in catalytic activity and no marked change in affinity for FPP and IPP.|||Almost complete loss of catalytic activity.|||Decreases binding to DHDDS.|||Dehydrodolichyl diphosphate synthase complex subunit NUS1|||Disrupts NUS1-DHDDS heterodimerization.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||In CDG1AA; loss of function in protein glycosylation; 5-fold reduction in catalytic activity and reduced affinity for FPP and IPP..|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with Parkinson's disease; 40 % reduction in prenyltransferase activity.|||Probable disease-associated variant found in a patient with progressive myoclonus epilepsy.|||RXG motif; crucial for prenyltransferase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273167|||http://purl.uniprot.org/annotation/VAR_030092|||http://purl.uniprot.org/annotation/VAR_030093|||http://purl.uniprot.org/annotation/VAR_030094|||http://purl.uniprot.org/annotation/VAR_030095|||http://purl.uniprot.org/annotation/VAR_030096|||http://purl.uniprot.org/annotation/VAR_071210|||http://purl.uniprot.org/annotation/VAR_083900|||http://purl.uniprot.org/annotation/VAR_085036
http://togogenome.org/gene/9606:COX7C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15954                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7C, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006164
http://togogenome.org/gene/9606:ANKS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DUE4|||http://purl.uniprot.org/uniprot/F6WF08|||http://purl.uniprot.org/uniprot/Q6ZW76|||http://purl.uniprot.org/uniprot/Q86W77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3-hydroxyasparagine|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SAM domain-containing protein 3|||Decreased homooligomerization. Decreased interaction with ANKS6.|||Decreased homooligomerization. No effect on interaction with ANKS6.|||Disordered|||In isoform 2.|||Interaction with NEK7|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230777|||http://purl.uniprot.org/annotation/VAR_048283|||http://purl.uniprot.org/annotation/VAR_048284|||http://purl.uniprot.org/annotation/VSP_038183
http://togogenome.org/gene/9606:IQCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||IQ|||IQ domain-containing protein H|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282565|||http://purl.uniprot.org/annotation/VAR_051077|||http://purl.uniprot.org/annotation/VSP_024188|||http://purl.uniprot.org/annotation/VSP_024189|||http://purl.uniprot.org/annotation/VSP_024190|||http://purl.uniprot.org/annotation/VSP_024191|||http://purl.uniprot.org/annotation/VSP_024192|||http://purl.uniprot.org/annotation/VSP_024193|||http://purl.uniprot.org/annotation/VSP_024194|||http://purl.uniprot.org/annotation/VSP_024195|||http://purl.uniprot.org/annotation/VSP_024196|||http://purl.uniprot.org/annotation/VSP_045251|||http://purl.uniprot.org/annotation/VSP_045252
http://togogenome.org/gene/9606:MRPL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZR1|||http://purl.uniprot.org/uniprot/Q9BYD2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein bL9m|||Mitochondrion|||Ribosomal protein L9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030550|||http://purl.uniprot.org/annotation/VAR_028136|||http://purl.uniprot.org/annotation/VAR_028137
http://togogenome.org/gene/9606:RND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61587                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Removed in mature form|||Rho-related GTP-binding protein RhoE|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198878|||http://purl.uniprot.org/annotation/PRO_0000281230
http://togogenome.org/gene/9606:ADGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7X0|||http://purl.uniprot.org/uniprot/Q9H5S1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Androglobin|||Basic and acidic residues|||Calpain catalytic|||Disordered|||IQ|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232525|||http://purl.uniprot.org/annotation/VAR_025948|||http://purl.uniprot.org/annotation/VAR_063158|||http://purl.uniprot.org/annotation/VSP_039243|||http://purl.uniprot.org/annotation/VSP_039244
http://togogenome.org/gene/9606:ASF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVP2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolishes CDAN1 interaction.|||Histone chaperone ASF1B|||Interaction with CHAF1B|||Interaction with histone H3|||No apparent effect on ASF1B phosphorylation by TLK2. Reduced phosphorylation of ASF1B by TLK2 when associated with A-198.|||Phosphoserine; by TLK2|||Reduced phosphorylation of ASF1B by TLK2 when associated with A-169.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284015
http://togogenome.org/gene/9606:FSTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N475                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Follistatin-related protein 5|||Ig-like 1|||Ig-like 2|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Kazal-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010118|||http://purl.uniprot.org/annotation/VAR_036135|||http://purl.uniprot.org/annotation/VAR_049092|||http://purl.uniprot.org/annotation/VAR_049093|||http://purl.uniprot.org/annotation/VSP_046215|||http://purl.uniprot.org/annotation/VSP_046216
http://togogenome.org/gene/9606:PIGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01833                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1; required for binding to polymeric IgA and IgM|||Ig-like V-type 2|||Ig-like V-type 3|||Ig-like V-type 4|||Ig-like V-type 5|||Interchain (with C-179 of IGHA2/constant region of IgA2 heavy chain)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Polymeric immunoglobulin receptor|||Secretory component                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014900|||http://purl.uniprot.org/annotation/PRO_0000014901|||http://purl.uniprot.org/annotation/VAR_003920|||http://purl.uniprot.org/annotation/VAR_025283|||http://purl.uniprot.org/annotation/VAR_032822
http://togogenome.org/gene/9606:PASD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV76                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Circadian clock protein PASD1|||Disordered|||In isoform 2.|||Necessary for transcriptional repression|||PAS|||Reduces inhibition of CLOCK-BMAL1 heterodimer activity; when associated with E-36.|||Reduces inhibition of CLOCK-BMAL1 heterodimer activity; when associated with R-45.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299445|||http://purl.uniprot.org/annotation/VAR_034819|||http://purl.uniprot.org/annotation/VSP_027663|||http://purl.uniprot.org/annotation/VSP_027664
http://togogenome.org/gene/9606:PPP2R3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Q6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||In MEGD.|||In isoform 2.|||Serine/threonine-protein phosphatase 2A regulatory subunit B" subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277833|||http://purl.uniprot.org/annotation/VAR_082202|||http://purl.uniprot.org/annotation/VAR_082203|||http://purl.uniprot.org/annotation/VAR_082204|||http://purl.uniprot.org/annotation/VSP_023113
http://togogenome.org/gene/9606:MLEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GX14|||http://purl.uniprot.org/uniprot/Q14165                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||Malectin|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013982|||http://purl.uniprot.org/annotation/PRO_5003324697
http://togogenome.org/gene/9606:GZMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQ52|||http://purl.uniprot.org/uniprot/P10144|||http://purl.uniprot.org/uniprot/Q67BC3|||http://purl.uniprot.org/uniprot/Q6XGZ4                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Granzyme B|||Mediates preference for Asp-containing substrates|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027399|||http://purl.uniprot.org/annotation/PRO_0000027400|||http://purl.uniprot.org/annotation/VAR_018371|||http://purl.uniprot.org/annotation/VAR_018381|||http://purl.uniprot.org/annotation/VAR_047409
http://togogenome.org/gene/9606:FCGR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31994                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with susceptibility to SLE; associated with resistance to malaria; found at an increased frequency in African and Asian populations from areas where malaria is endemic; enhances phagocytosis of Plasmodium falciparum-infected erythrocytes in vitro.|||Cytoplasmic|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 4 and isoform 5.|||In isoform IIB2 and isoform 5.|||In isoform IIB3.|||Low affinity immunoglobulin gamma Fc region receptor II-b|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015147|||http://purl.uniprot.org/annotation/VAR_008798|||http://purl.uniprot.org/annotation/VAR_015515|||http://purl.uniprot.org/annotation/VAR_027045|||http://purl.uniprot.org/annotation/VAR_059430|||http://purl.uniprot.org/annotation/VSP_002642|||http://purl.uniprot.org/annotation/VSP_002643|||http://purl.uniprot.org/annotation/VSP_058635
http://togogenome.org/gene/9606:PLEKHA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB20                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Interaction with SACM1L|||Interaction with VAPA and VAPB|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family A member 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053878
http://togogenome.org/gene/9606:PHLPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes activity.|||Decreases activity.|||Disordered|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PH|||PH domain leucine-rich repeat-containing protein phosphatase 2|||PPM-type phosphatase|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057784|||http://purl.uniprot.org/annotation/VSP_014056|||http://purl.uniprot.org/annotation/VSP_014057|||http://purl.uniprot.org/annotation/VSP_017265
http://togogenome.org/gene/9606:RC3H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to CDERNA but not dsRNA.|||C3H1-type|||Cleavage; by MALT1|||Decreases dsRNA-binding.|||Disordered|||HEPN-C|||HEPN-N|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||Loss of activity. Loss of MAP3K5 ubiquitination.|||Phosphoserine|||Polar residues|||RING-type; degenerate|||ROQ|||Roquin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055968|||http://purl.uniprot.org/annotation/VSP_015017|||http://purl.uniprot.org/annotation/VSP_015018|||http://purl.uniprot.org/annotation/VSP_015019|||http://purl.uniprot.org/annotation/VSP_015020|||http://purl.uniprot.org/annotation/VSP_015021|||http://purl.uniprot.org/annotation/VSP_015022|||http://purl.uniprot.org/annotation/VSP_015023|||http://purl.uniprot.org/annotation/VSP_015024
http://togogenome.org/gene/9606:VIPAS39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMB7|||http://purl.uniprot.org/uniprot/Q6IA61|||http://purl.uniprot.org/uniprot/Q9H9C1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Disrupts endodsomal colocalization with VPS33B.|||In ARCS2.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spermatogenesis-defective protein 39 homolog|||Vps16 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089935|||http://purl.uniprot.org/annotation/VAR_087661|||http://purl.uniprot.org/annotation/VSP_043055
http://togogenome.org/gene/9606:EEA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15075                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes endosomal location.|||Abolishes endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1373.|||Abolishes phosphatidylinositol 3-phosphate binding and endosomal location.|||Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1372.|||Basic and acidic residues|||C2H2-type|||Disordered|||Early endosome antigen 1|||FYVE-type|||Phosphoserine|||Polar residues|||Reduces phosphatidylinositol 3-phosphate binding and endosomal location.|||Strongly reduces interaction with RAB5C.|||Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location.|||Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098706|||http://purl.uniprot.org/annotation/VAR_052980
http://togogenome.org/gene/9606:ZNF333                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JL9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB 1|||KRAB 2|||Zinc finger protein 333                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047536|||http://purl.uniprot.org/annotation/VAR_024210|||http://purl.uniprot.org/annotation/VAR_052812|||http://purl.uniprot.org/annotation/VSP_055945|||http://purl.uniprot.org/annotation/VSP_055946|||http://purl.uniprot.org/annotation/VSP_055947|||http://purl.uniprot.org/annotation/VSP_055948
http://togogenome.org/gene/9606:C6orf136                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P5T2|||http://purl.uniprot.org/uniprot/Q5SQH8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Uncharacterized protein C6orf136                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089531|||http://purl.uniprot.org/annotation/VSP_014618|||http://purl.uniprot.org/annotation/VSP_014619|||http://purl.uniprot.org/annotation/VSP_046640
http://togogenome.org/gene/9606:NUDT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36639                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.|||Associated with type I diabetes in Japanese female population; may be associated with an increased risk for small cell lung carcinoma (SCLC); decreased localization to mitochondrion.|||Enhances 2-oxo-dATPase activity and greatly reduces 8-oxo-dGTPase activity.|||Enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.|||Greatly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.|||Greatly reduces or abolishes 2-oxo-dATPase and 8-oxo-dGTPase activities.|||In isoform p21.|||In isoform p22.|||In isoform p26.|||Loss of 2-oxo-dATPase activity, reduces 8-oxo-dGTPase activity.|||Loss of ability to prevent DNA damage. Expected to cause loss of enzyme activity.|||Loss of activity.|||Mildly decreased 2-oxo-dATPase activity, nearly abolishes 8-oxo-dGTPase activity.|||Nudix box|||Nudix hydrolase|||Oxidized purine nucleoside triphosphate hydrolase|||Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.|||Reduces 2-oxo-dATPase and 8-oxo-dGTPase activities.|||Reduces activity by 60%.|||Reduces activity by 97%.|||Slightly enhances 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.|||Slightly reduces 2-oxo-dATPase and 8-oxo-dGTPase activities and increases thermolability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019944|||http://purl.uniprot.org/annotation/VAR_013757|||http://purl.uniprot.org/annotation/VAR_068715|||http://purl.uniprot.org/annotation/VSP_061188|||http://purl.uniprot.org/annotation/VSP_061189|||http://purl.uniprot.org/annotation/VSP_061190
http://togogenome.org/gene/9606:KCNQ5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In MRD46; decreased protein abundance; decreased potassium ion transmembrane transport; changed voltage-gated potassium channel activity; changed gating properties.|||In MRD46; no effect on protein abundance; no effect on potassium ion transmembrane transport; changed voltage-gated potassium channel activity; changed gating properties.|||In MRD46; no effect on protein abundance; no effect on potassium ion transmembrane transport; increased voltage-gated potassium channel activity; changed gating properties resulting in a gain of function.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 5|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054040|||http://purl.uniprot.org/annotation/VAR_035772|||http://purl.uniprot.org/annotation/VAR_035773|||http://purl.uniprot.org/annotation/VAR_079219|||http://purl.uniprot.org/annotation/VAR_079220|||http://purl.uniprot.org/annotation/VAR_079221|||http://purl.uniprot.org/annotation/VAR_079222|||http://purl.uniprot.org/annotation/VSP_001014|||http://purl.uniprot.org/annotation/VSP_001015|||http://purl.uniprot.org/annotation/VSP_022318|||http://purl.uniprot.org/annotation/VSP_022319|||http://purl.uniprot.org/annotation/VSP_045487|||http://purl.uniprot.org/annotation/VSP_056730|||http://purl.uniprot.org/annotation/VSP_056731
http://togogenome.org/gene/9606:MIS18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYP9                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site                                                                                  ^@                                                                                  Abolishes interaction with OIP5; when associated with D-176.|||Abolishes interaction with OIP5; when associated with E-82.|||Abolishes location at the centromere.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mis18|||No effect.|||Phosphoserine|||Protein Mis18-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079515
http://togogenome.org/gene/9606:ZNF580                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK33                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Pro residues|||Zinc finger protein 580                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047671
http://togogenome.org/gene/9606:MAGOH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61326                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; K-73 and R-117.|||Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; R-72 and K-73.|||Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-68; R-72 and R-117.|||Abolishes interaction with PYM1 leading to increase EJC association with spliced mRNAs; when associated with R-72; K-73 and R-117.|||Complete loss of nonsense-mediated decay activity.|||Fully active.|||Impaired nonsense-mediated decay activity.|||In isoform 2.|||N-acetylmethionine|||Protein mago nashi homolog|||Slightly reduced nonsense-mediated decay activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174145|||http://purl.uniprot.org/annotation/VSP_056246
http://togogenome.org/gene/9606:AOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75106                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  2',4',5'-topaquinone|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Retina-specific copper amine oxidase|||Schiff-base intermediate with substrate; via topaquinone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035671|||http://purl.uniprot.org/annotation/VAR_025022|||http://purl.uniprot.org/annotation/VAR_025023|||http://purl.uniprot.org/annotation/VAR_025024|||http://purl.uniprot.org/annotation/VAR_025025|||http://purl.uniprot.org/annotation/VAR_025026|||http://purl.uniprot.org/annotation/VSP_006549
http://togogenome.org/gene/9606:PCDH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95206                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protocadherin-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003993|||http://purl.uniprot.org/annotation/VAR_017171|||http://purl.uniprot.org/annotation/VAR_017172|||http://purl.uniprot.org/annotation/VAR_017173|||http://purl.uniprot.org/annotation/VAR_036108|||http://purl.uniprot.org/annotation/VAR_059191|||http://purl.uniprot.org/annotation/VSP_008706
http://togogenome.org/gene/9606:LRRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0T1|||http://purl.uniprot.org/uniprot/Q9H3W5|||http://purl.uniprot.org/uniprot/Q9NUU4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat neuronal protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045823|||http://purl.uniprot.org/annotation/PRO_5004331999|||http://purl.uniprot.org/annotation/PRO_5014296873|||http://purl.uniprot.org/annotation/VAR_049901
http://togogenome.org/gene/9606:STING1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WV6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished ability to activate IRF3 and induce the production of type I interferon.|||Abolished ability to induce autophagy. Abolished interaction with SEC24C.|||Abolished ability to induce the production of type I interferon.|||Abolished cGAMP-binding.|||Abolished cGAMP-binding. Abolished ability to induce autophagy.|||Abolished inhibition by small-molecule H-151; abolished palmitoylation.|||Abolished translocation from the endoplasmic reticulum in response to cGAMP-binding. Reduced phosphorylation by TBK1.|||Abolishes the endoplasmic reticulum location.|||Abolishes ubiquitination, homodimerization and subsequent production of IFN-beta.|||Abrogates interaction with STEEP.|||Activated by both 2'-3' linked cGAMP and 3'-3' linked cGAMP.|||C-terminal tail (CTT)|||Constitutively active mutant that promotes the production of type I interferon in absence of cGAMP ligand.|||Cyclic dinucleotide-binding domain (CBD)|||Cytoplasmic|||Decreased phosphorylation by TBK1, leading to reduced ability to activate IRF3.|||Disordered|||Does not affect ability to activate IRF3.|||Does not affect ability to activate IRF3. Abolished ability to induce the production of type I interferon.|||Does not affect amount of ubiquitination.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In SAVI.|||In SAVI; constitutively active mutant that promotes the production of type I interferon in absence of cGAMP ligand.|||Induces a decrease in phosphorylation by TBK1.|||Induces a decrease in phosphorylation by TBK1. Abolished ability to activate IRF3.|||Loss of deubiquitination by USP44.|||Lumenal|||Mediates interaction with ZDHHC1 and ZDHHC11|||Partially constitutively active mutant that promotes the production of type I interferon in absence of cGAMP ligand.|||Phosphomimetic mutant; retains some ability to activate IRF3. It probably incompletely mimics phosphorylation.|||Phosphoserine; by TBK1|||Polar residues|||Probable disease-associated variant found in a 9-month-old patient who died following a fever and severe neck abscess without indication of any severe bacterial infection; may affect splicing; constitutively active mutant that promotes the production of type I interferon in absence of cyclic dinucleotide ligand; localizes to the perinuclear region in absence of cyclic dinucleotide ligand.|||Renders the enzyme sensitive to 5,6-dimethylxanthenone 4-acetic acid (DMXAA) drug, leading to activation of the STING1 pathway.|||Renders the enzyme sensitive to 5,6-dimethylxanthenone 4-acetic acid (DMXAA) drug, leading to activation of the STING1 pathway; when associated with A-162.|||S-palmitoyl cysteine|||Slight decrease in c-di-GMP-binding.|||Slight decrease in c-di-GMP-binding. Renders the enzyme sensitive to 5,6-dimethylxanthenone 4-acetic acid (DMXAA) drug, leading to activation of the STING1 pathway. Renders the enzyme sensitive to 5,6-dimethylxanthenone 4-acetic acid (DMXAA) drug; when associated with I-266.|||Slightly affects ability to induce the production of type I interferon.|||Stimulator of interferon genes protein|||Strong decrease in c-di-GMP and cGAMP-binding.|||Strong decrease in c-di-GMP-binding.|||Strong decrease in cGAMP-binding without affecting interaction with TBK1. Abolished ability to induce autophagy.|||pLxIS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271116|||http://purl.uniprot.org/annotation/VAR_029863|||http://purl.uniprot.org/annotation/VAR_029864|||http://purl.uniprot.org/annotation/VAR_029865|||http://purl.uniprot.org/annotation/VAR_071878|||http://purl.uniprot.org/annotation/VAR_071879|||http://purl.uniprot.org/annotation/VAR_071880|||http://purl.uniprot.org/annotation/VAR_081660
http://togogenome.org/gene/9606:RBM27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2N5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNA-binding protein 27|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273044
http://togogenome.org/gene/9606:TMEM244                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVB8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Putative transmembrane protein 244                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238467|||http://purl.uniprot.org/annotation/VAR_026549|||http://purl.uniprot.org/annotation/VAR_026550|||http://purl.uniprot.org/annotation/VAR_026551|||http://purl.uniprot.org/annotation/VAR_033681
http://togogenome.org/gene/9606:ACOT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3I5F7                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 6|||Charge relay system|||In isoform 2.|||Peroxisome targeting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305098|||http://purl.uniprot.org/annotation/VAR_052302|||http://purl.uniprot.org/annotation/VSP_061185
http://togogenome.org/gene/9606:BPIFA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K739|||http://purl.uniprot.org/uniprot/Q96DR5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPI fold-containing family A member 2|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017184|||http://purl.uniprot.org/annotation/PRO_5002722185|||http://purl.uniprot.org/annotation/VAR_049751|||http://purl.uniprot.org/annotation/VAR_049752|||http://purl.uniprot.org/annotation/VAR_049753
http://togogenome.org/gene/9606:LUC7L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y383                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5-hydroxylysine; by JMJD6|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Induces a decrease in lysyl-hydroxylation. Abolishes lysyl-hydroxylation; when associated with R-266.|||Induces a decrease in lysyl-hydroxylation. Abolishes lysyl-hydroxylation; when associated with R-269.|||Phosphoserine|||Putative RNA-binding protein Luc7-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187282|||http://purl.uniprot.org/annotation/VAR_034067|||http://purl.uniprot.org/annotation/VSP_010217|||http://purl.uniprot.org/annotation/VSP_044896
http://togogenome.org/gene/9606:GGCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7V5|||http://purl.uniprot.org/uniprot/O75223                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity without altering structure.|||Gamma-glutamylcyclotransferase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Little or no change in reaction kinetics.|||Marked decrease in catalytic efficiency and specific activity.|||Marked decrease in catalytic efficiency.|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089580|||http://purl.uniprot.org/annotation/VSP_035599|||http://purl.uniprot.org/annotation/VSP_035600|||http://purl.uniprot.org/annotation/VSP_046463|||http://purl.uniprot.org/annotation/VSP_046464
http://togogenome.org/gene/9606:RANBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49792                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||2 X 50 AA approximate repeats|||20|||21|||22|||22 X 2 AA repeats of F-G|||3|||4|||5|||6|||7|||8|||9|||Abolishes binding to UBE2I and SUMOE3 ligase activity.|||Abolishes interaction with sumoylated RANGAP1.|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Breakpoint for translocation to form RANBP2-FGFR1 protein|||Disordered|||E3 SUMO-protein ligase RanBP2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs SUMOE3 ligase activity.|||In IIAE3.|||In IIAE3; decreased interaction with COX11.|||Interaction with BICD2|||Interaction with SUMO1|||Interaction with UBE2I|||Interaction with sumoylated RANGAP1|||N6-acetyllysine|||No effect on SUMOE3 ligase activity.|||Omega-N-methylarginine; alternate|||PPIase cyclophilin-type|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RanBD1 1|||RanBD1 2|||RanBD1 3|||RanBD1 4|||RanBP2-type 1|||RanBP2-type 2|||RanBP2-type 3|||RanBP2-type 4|||RanBP2-type 5|||RanBP2-type 6|||RanBP2-type 7|||RanBP2-type 8|||Required for E3 SUMO-ligase activity|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204913|||http://purl.uniprot.org/annotation/VAR_014886|||http://purl.uniprot.org/annotation/VAR_023939|||http://purl.uniprot.org/annotation/VAR_029765|||http://purl.uniprot.org/annotation/VAR_029766|||http://purl.uniprot.org/annotation/VAR_029767|||http://purl.uniprot.org/annotation/VAR_029768|||http://purl.uniprot.org/annotation/VAR_050575|||http://purl.uniprot.org/annotation/VAR_050576|||http://purl.uniprot.org/annotation/VAR_054997|||http://purl.uniprot.org/annotation/VAR_054998|||http://purl.uniprot.org/annotation/VAR_054999
http://togogenome.org/gene/9606:ALLC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6M5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Probable inactive allantoicase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205905|||http://purl.uniprot.org/annotation/VAR_080299|||http://purl.uniprot.org/annotation/VSP_015618
http://togogenome.org/gene/9606:ASNSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWL6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Sequence Variant                                                                                  ^@                                                                                  Asparagine synthetase|||Asparagine synthetase domain-containing protein 1|||For GATase activity|||Glutamine amidotransferase type-2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324760|||http://purl.uniprot.org/annotation/VAR_039876|||http://purl.uniprot.org/annotation/VAR_039877
http://togogenome.org/gene/9606:ROBO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1RMC8|||http://purl.uniprot.org/uniprot/Q9Y6N7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Found in a patient with early-onset epileptic encephalopathy; unknown pathological significance.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In CPHD8.|||In CPHD8; unknown pathological significance.|||In NORS.|||In NORS; unknown pathological significance.|||In NYS8; unknown pathological significance.|||In a breast cancer sample.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 5 and isoform 6.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL; in vitro|||Polar residues|||Pro residues|||Roundabout homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031033|||http://purl.uniprot.org/annotation/VAR_019071|||http://purl.uniprot.org/annotation/VAR_019072|||http://purl.uniprot.org/annotation/VAR_053640|||http://purl.uniprot.org/annotation/VAR_053641|||http://purl.uniprot.org/annotation/VAR_088311|||http://purl.uniprot.org/annotation/VAR_088312|||http://purl.uniprot.org/annotation/VAR_088313|||http://purl.uniprot.org/annotation/VAR_088314|||http://purl.uniprot.org/annotation/VAR_088315|||http://purl.uniprot.org/annotation/VAR_088316|||http://purl.uniprot.org/annotation/VAR_088317|||http://purl.uniprot.org/annotation/VAR_088318|||http://purl.uniprot.org/annotation/VAR_088319|||http://purl.uniprot.org/annotation/VAR_088320|||http://purl.uniprot.org/annotation/VAR_088321|||http://purl.uniprot.org/annotation/VAR_088322|||http://purl.uniprot.org/annotation/VAR_088323|||http://purl.uniprot.org/annotation/VAR_088324|||http://purl.uniprot.org/annotation/VAR_088325|||http://purl.uniprot.org/annotation/VAR_088326|||http://purl.uniprot.org/annotation/VSP_010643|||http://purl.uniprot.org/annotation/VSP_010644|||http://purl.uniprot.org/annotation/VSP_010645|||http://purl.uniprot.org/annotation/VSP_010646|||http://purl.uniprot.org/annotation/VSP_043881|||http://purl.uniprot.org/annotation/VSP_043882|||http://purl.uniprot.org/annotation/VSP_046084
http://togogenome.org/gene/9606:HAND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96004                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heart- and neural crest derivatives-expressed protein 1|||Phosphoserine; by PLK4|||Phosphothreonine; by PLK4|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127184
http://togogenome.org/gene/9606:KCTD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ13                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD14|||Disordered|||In isoform 3b.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191299|||http://purl.uniprot.org/annotation/VSP_054562
http://togogenome.org/gene/9606:PSG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LNM5|||http://purl.uniprot.org/uniprot/Q13046                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014914|||http://purl.uniprot.org/annotation/VAR_056075
http://togogenome.org/gene/9606:MTCH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8YXX5|||http://purl.uniprot.org/uniprot/Q9NZJ7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 3.|||Mitochondrial carrier homolog 1|||Mitochondrial intermembrane|||Omega-N-methylarginine|||Solcar|||Solcar 1|||Solcar 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232385|||http://purl.uniprot.org/annotation/VSP_017881|||http://purl.uniprot.org/annotation/VSP_017882
http://togogenome.org/gene/9606:HLA-DPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I4EC15|||http://purl.uniprot.org/uniprot/P04440                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Allele DPB1*41:01 and allele DPB1*83:01.|||Beta-1|||Beta-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DP beta 1 chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DPB1*01:01, allele DPB1*01:02, allele DPB1*09:02, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*15:01, allele DPB1*20:02, allele DPB1*21:02, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*39:01, allele DPB1*40:01, allele DPB1*49:01, allele DPB1*53:01, allele DPB1*65:01, allele DPB1*74:01, allele DPB1*85:01, allele DPB1*89:01 and allele DPB1*96:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*03:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*31:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*63:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*97:01 and allele DPB1*98:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*13:01, allele DPB1*14:01, allele DPB1*15:01, allele DPB1*18:01, allele DPB1*19:01, allele DPB1*20:01, allele DPB1*26:01, allele DPB1*45:01 and allele DPB1*85:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01 and allele DPB1*98:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:02, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*21:02, allele DPB1*20:01, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*56:01, allele DPB1*69:01, allele DPB1*74:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*89:01, allele DPB1*90:01, allele DPB1*92:01 and allele DPB1*93:01.|||In allele DPB1*01:01, allele DPB1*03:01, allele DPB1*05:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*17:02, allele DPB1*21:02, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:01, allele DPB1*29:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*65:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*84:01, allele DPB1*88:01, allele DPB1*90:01 and allele DPB1*92:01.|||In allele DPB1*01:01.|||In allele DPB1*01:02, allele DPB1*02:01, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*04:03, allele DPB1*05:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:01, allele DPB1*19:02, allele DPB1*21:01, allele DPB1*20:01, allele DPB1*22:01, allele DPB1*22:02, allele DPB1*23:01, allele DPB1*25:01, allele DPB1*26:02, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*32:01, allele DPB1*34:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*38:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*47:01, allele DPB1*48:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*57:01, allele DPB1*58:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*62:01, allele DPB1*63:01, allele DPB1*67:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*71:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*84:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*93:01, allele DPB1*94:01, allele DPB1*95:01, allele DPB1*97:01 and allele DPB1*98:01.|||In allele DPB1*01:02, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*05:01, allele DPB1*08:02, allele DPB1*17:02, allele DPB1*19:01, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*24:01, allele DPB1*30:01, allele DPB1*36:01, allele DPB1*38:01, allele DPB1*47:01, allele DPB1*54:01, allele DPB1*84:01 and allele DPB1*97:01.|||In allele DPB1*02:01, allele DPB1*02:02, allele DPB1*02:03, allele DPB1*04:03, allele DPB1*06:01, allele DPB1*08:01, allele DPB1*08:02, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:02, allele DPB1*19:01, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*26:02, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*32:01, allele DPB1*33:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*46:01, allele DPB1*47:01, allele DPB1*48:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*58:01, allele DPB1*71:01, allele DPB1*81:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*93:01 and allele DPB1*95:01.|||In allele DPB1*02:01, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:01, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:02, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*32:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*48:01, allele DPB1*49:01, allele DPB1*50:01, allele DPB1*51:01, allele DPB1*53:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*81:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*94:01 and allele DPB1*98:01.|||In allele DPB1*02:01, allele DPB1*03:01, allele DPB1*04:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*06:02, allele DPB1*08:01, allele DPB1*09:01, allele DPB1*10:01, allele DPB1*10:02, allele DPB1*11:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*18:01, allele DPB1*18:02, allele DPB1*19:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*25:02, allele DPB1*26:02, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*32:01, allele DPB1*35:01, allele DPB1*37:01, allele DPB1*41:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*46:01, allele DPB1*48:01, allele DPB1*49:01, allele DPB1*50:01, allele DPB1*51:01, allele DPB1*53:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*60:01, allele DPB1*68:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*73:01, allele DPB1*75:01, allele DPB1*76:01, allele DPB1*77:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*80:01, allele DPB1*81:01, allele DPB1*82:01, allele DPB1*83:01, allele DPB1*84:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01, allele DPB1*94:01 and allele DPB1*98:01.|||In allele DPB1*02:02, allele DPB1*02:03, allele DPB1*05:01, allele DPB1*15:02, allele DPB1*17:02, allele DPB1*19:02, allele DPB1*21:01, allele DPB1*21:01, allele DPB1*22:01, allele DPB1*34:01, allele DPB1*36:01, allele DPB1*38:01, allele DPB1*44:01, allele DPB1*48:01, allele DPB1*58:01, allele DPB1*62:01, allele DPB1*63:01, allele DPB1*95:01 and allele DPB1*97:01.|||In allele DPB1*02:03.|||In allele DPB1*03:01, allele DPB1*03:02, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*10:02, allele DPB1*11:01, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*15:01, allele DPB1*17:02, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*28:01, allele DPB1*29:01, allele DPB1*31:01, allele DPB1*34:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*50:01, allele DPB1*52:01, allele DPB1*56:01, allele DPB1*57:01, allele DPB1*59:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*72:01, allele DPB1*73:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*87:01, allele DPB1*91:01, allele DPB1*92:01 and allele DPB1*95:01.|||In allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*09:02, allele DPB1*10:01, allele DPB1*11:01, allele DPB1*11:02, allele DPB1*13:01, allele DPB1*13:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*17:02, allele DPB1*20:02, allele DPB1*21:01, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*25:01, allele DPB1*26:01, allele DPB1*27:01, allele DPB1*29:01, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*36:01, allele DPB1*37:01, allele DPB1*44:01, allele DPB1*45:01, allele DPB1*52:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*56:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*74:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*79:01, allele DPB1*85:01, allele DPB1*86:01, allele DPB1*87:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01, allele DPB1*93:01 and allele DPB1*98:01; requires 2 nucleotide substitutions.|||In allele DPB1*03:01, allele DPB1*05:02, allele DPB1*06:01, allele DPB1*09:01, allele DPB1*10:02, allele DPB1*14:01, allele DPB1*14:02, allele DPB1*17:01, allele DPB1*20:01, allele DPB1*22:02, allele DPB1*29:01, allele DPB1*35:01, allele DPB1*44:01, allele DPB1*46:01, allele DPB1*50:01, allele DPB1*57:01, allele DPB1*69:01, allele DPB1*70:01, allele DPB1*76:01, allele DPB1*78:01, allele DPB1*80:01, allele DPB1*86:01, allele DPB1*88:01, allele DPB1*91:01, allele DPB1*92:01 and allele DPB1*98:01.|||In allele DPB1*04:02.|||In allele DPB1*05:01 and allele DPB1*19:01.|||In allele DPB1*08:02, allele DPB1*09:02, allele DPB1*13:01, allele DPB1*13:02 and allele DPB1*19:01.|||In allele DPB1*09:01, allele DPB1*10:01, allele DPB1*14:01, allele DPB1*16:02, allele DPB1*17:01, allele DPB1*22:02, allele DPB1*30:01, allele DPB1*35:01, allele DPB1*45:01, allele DPB1*54:01, allele DPB1*55:01, allele DPB1*58:01, allele DPB1*66:01, allele DPB1*67:01, allele DPB1*76:01, allele DPB1*86:01, allele DPB1*91:01 and allele DPB1*98:01; requires 2 nucleotide substitutions.|||In allele DPB1*09:02.|||In allele DPB1*11:01, allele DPB1*15:01, allele DPB1*69:01 and allele DPB1*74:01.|||In allele DPB1*14:02 and allele DPB1*21:02.|||In allele DPB1*15:01, allele DPB1*18:01, allele DPB1*28:01, allele DPB1*34:01, allele DPB1*40:01, allele DPB1*53:01, allele DPB1*62:01 and allele DPB1*74:01.|||In allele DPB1*15:01.|||In allele DPB1*18:02.|||In allele DPB1*22:02; requires 2 nucleotide substitutions.|||In allele DPB1*24:02.|||In allele DPB1*26:02.|||In allele DPB1*31:01 and allele DPB1*34:01.|||In allele DPB1*32:01.|||In allele DPB1*38:01.|||In allele DPB1*60:01.|||In allele DPB1*70:01; requires 2 nucleotide substitutions.|||In allele DPB1*75:01.|||In allele DPB1*75:01; requires 2 nucleotide substitutions.|||In allele DPB1*77:01.|||In allele DPB1*78:01.|||In allele DPB1*82:01 and allele DPB1*85:01.|||In allele DPB1*94:01.|||In allele DPB1*96:01.|||In allele DPB1*97:01.|||In allele DPB1*99:01.|||Ind allele DPB1*11:01, allele DPB1*15:01 and allele DPB1*74:01.|||N-linked (GlcNAc...) asparagine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018984|||http://purl.uniprot.org/annotation/PRO_5015093999|||http://purl.uniprot.org/annotation/VAR_033433|||http://purl.uniprot.org/annotation/VAR_033434|||http://purl.uniprot.org/annotation/VAR_033435|||http://purl.uniprot.org/annotation/VAR_033436|||http://purl.uniprot.org/annotation/VAR_033437|||http://purl.uniprot.org/annotation/VAR_033438|||http://purl.uniprot.org/annotation/VAR_033439|||http://purl.uniprot.org/annotation/VAR_033440|||http://purl.uniprot.org/annotation/VAR_033441|||http://purl.uniprot.org/annotation/VAR_033442|||http://purl.uniprot.org/annotation/VAR_033443|||http://purl.uniprot.org/annotation/VAR_033444|||http://purl.uniprot.org/annotation/VAR_033445|||http://purl.uniprot.org/annotation/VAR_033446|||http://purl.uniprot.org/annotation/VAR_033447|||http://purl.uniprot.org/annotation/VAR_033448|||http://purl.uniprot.org/annotation/VAR_050393|||http://purl.uniprot.org/annotation/VAR_050394|||http://purl.uniprot.org/annotation/VAR_054662|||http://purl.uniprot.org/annotation/VAR_059511|||http://purl.uniprot.org/annotation/VAR_059512|||http://purl.uniprot.org/annotation/VAR_059513|||http://purl.uniprot.org/annotation/VAR_060627|||http://purl.uniprot.org/annotation/VAR_060628|||http://purl.uniprot.org/annotation/VAR_060629|||http://purl.uniprot.org/annotation/VAR_060630|||http://purl.uniprot.org/annotation/VAR_060631|||http://purl.uniprot.org/annotation/VAR_060632|||http://purl.uniprot.org/annotation/VAR_060633|||http://purl.uniprot.org/annotation/VAR_060634|||http://purl.uniprot.org/annotation/VAR_060635|||http://purl.uniprot.org/annotation/VAR_060636|||http://purl.uniprot.org/annotation/VAR_060637|||http://purl.uniprot.org/annotation/VAR_060638|||http://purl.uniprot.org/annotation/VAR_060639|||http://purl.uniprot.org/annotation/VAR_060640|||http://purl.uniprot.org/annotation/VAR_060641|||http://purl.uniprot.org/annotation/VAR_060642|||http://purl.uniprot.org/annotation/VAR_060643|||http://purl.uniprot.org/annotation/VAR_060644|||http://purl.uniprot.org/annotation/VAR_060645|||http://purl.uniprot.org/annotation/VAR_060646|||http://purl.uniprot.org/annotation/VAR_060647|||http://purl.uniprot.org/annotation/VAR_060648|||http://purl.uniprot.org/annotation/VAR_060649|||http://purl.uniprot.org/annotation/VAR_060650|||http://purl.uniprot.org/annotation/VAR_060651|||http://purl.uniprot.org/annotation/VAR_060652|||http://purl.uniprot.org/annotation/VAR_060653|||http://purl.uniprot.org/annotation/VAR_060654|||http://purl.uniprot.org/annotation/VAR_060655|||http://purl.uniprot.org/annotation/VAR_060656|||http://purl.uniprot.org/annotation/VAR_060657|||http://purl.uniprot.org/annotation/VAR_060658|||http://purl.uniprot.org/annotation/VAR_060659|||http://purl.uniprot.org/annotation/VAR_060660
http://togogenome.org/gene/9606:RRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14718                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Visual pigment-like receptor peropsin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197819
http://togogenome.org/gene/9606:FBXO10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59F51|||http://purl.uniprot.org/uniprot/Q9UK96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carbohydrate-binding/sugar hydrolysis|||Disordered|||F-box|||F-box only protein 10|||Found in a patient with lymphoma.|||Found in a patient with lymphoma; inhibits interaction with SKP1.|||Found in a patient with lymphoma; partial loss of function in controlling the stability of BCL2.|||In isoform 2.|||PbH1 1|||PbH1 10|||PbH1 11|||PbH1 12|||PbH1 13|||PbH1 14|||PbH1 15|||PbH1 16|||PbH1 17|||PbH1 2|||PbH1 3|||PbH1 4|||PbH1 5|||PbH1 6|||PbH1 7|||PbH1 8|||PbH1 9|||Phosphoserine|||Polar residues|||Requires 2 nucleotide substitutions; found in a patient with lymphoma; partial loss of function in controlling the stability of BCL2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119889|||http://purl.uniprot.org/annotation/VAR_055801|||http://purl.uniprot.org/annotation/VAR_070692|||http://purl.uniprot.org/annotation/VAR_070693|||http://purl.uniprot.org/annotation/VAR_070694|||http://purl.uniprot.org/annotation/VSP_056318
http://togogenome.org/gene/9606:TSEN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T914|||http://purl.uniprot.org/uniprot/C9J7Z4|||http://purl.uniprot.org/uniprot/Q8NCE0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In PCH2B.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||tRNA intron endonuclease N-terminal|||tRNA intron endonuclease catalytic|||tRNA-splicing endonuclease subunit Sen2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109452|||http://purl.uniprot.org/annotation/VAR_048931|||http://purl.uniprot.org/annotation/VAR_048932|||http://purl.uniprot.org/annotation/VAR_054810|||http://purl.uniprot.org/annotation/VSP_010985|||http://purl.uniprot.org/annotation/VSP_010986|||http://purl.uniprot.org/annotation/VSP_046192|||http://purl.uniprot.org/annotation/VSP_046193|||http://purl.uniprot.org/annotation/VSP_046194
http://togogenome.org/gene/9606:SIRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTG7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes processing by MPP (in vitro).|||Deacetylase sirtuin-type|||Disordered|||In isoform 2.|||Loss of function.|||Mitochondrion|||N6-succinyllysine|||NAD-dependent protein deacetylase sirtuin-3, mitochondrial|||Proton acceptor|||Reduces targeting to mitochondrion; when associated with G-17 or Q-17.|||Reduces targeting to mitochondrion; when associated with G-21 or Q-21.|||Suppresses targeting to mitochondrion; when associated with G-13 or Q-13.|||Suppresses targeting to mitochondrion; when associated with G-7 or Q-7.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032612|||http://purl.uniprot.org/annotation/VAR_051977|||http://purl.uniprot.org/annotation/VAR_051978|||http://purl.uniprot.org/annotation/VAR_051979|||http://purl.uniprot.org/annotation/VSP_043792
http://togogenome.org/gene/9606:DCDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 2|||In DFNB66; results in ciliary abnormalities including increased ciliary length.|||In NSC.|||In NSC; loss of localization to the cilium axoneme.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079804|||http://purl.uniprot.org/annotation/VAR_022890|||http://purl.uniprot.org/annotation/VAR_050946|||http://purl.uniprot.org/annotation/VAR_050947|||http://purl.uniprot.org/annotation/VAR_074667|||http://purl.uniprot.org/annotation/VAR_077245|||http://purl.uniprot.org/annotation/VAR_078767|||http://purl.uniprot.org/annotation/VAR_078768|||http://purl.uniprot.org/annotation/VSP_014670|||http://purl.uniprot.org/annotation/VSP_014671
http://togogenome.org/gene/9606:CXCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25025|||http://purl.uniprot.org/uniprot/Q53PC4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by Staphylococcus aureus/SspP|||C-X-C chemokine receptor type 2|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069337|||http://purl.uniprot.org/annotation/VAR_014679
http://togogenome.org/gene/9606:EPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95208                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 3 AA repeats of N-P-F|||4|||5|||6|||6 X 3 AA repeats of [DE]-P-W|||Disordered|||ENTH|||Epsin-2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||UIM 1|||UIM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074516|||http://purl.uniprot.org/annotation/VAR_047923|||http://purl.uniprot.org/annotation/VAR_053080|||http://purl.uniprot.org/annotation/VAR_053081|||http://purl.uniprot.org/annotation/VSP_009154|||http://purl.uniprot.org/annotation/VSP_009155|||http://purl.uniprot.org/annotation/VSP_047003
http://togogenome.org/gene/9606:PIGH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14442                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In GPIBD17; decreased expression of GPI-anchored proteins, including FCGR3B/CD16B and CD55, in patient's granulocytes.|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058435|||http://purl.uniprot.org/annotation/VAR_080993
http://togogenome.org/gene/9606:MCHR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969V1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melanin-concentrating hormone receptor 2|||N-linked (GlcNAc...) asparagine|||No changes in receptor binding or functional signaling.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069740|||http://purl.uniprot.org/annotation/VAR_026661|||http://purl.uniprot.org/annotation/VAR_026662
http://togogenome.org/gene/9606:SMG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q15                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Basic and acidic residues|||Catalytic loop|||Disordered|||FAT|||FATC|||G-loop|||HEAT|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with SMG8 and SMG9|||Loss of function.|||N6-acetyllysine|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein kinase SMG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229791|||http://purl.uniprot.org/annotation/VAR_041623|||http://purl.uniprot.org/annotation/VAR_041624|||http://purl.uniprot.org/annotation/VAR_041625|||http://purl.uniprot.org/annotation/VAR_041626|||http://purl.uniprot.org/annotation/VAR_041627|||http://purl.uniprot.org/annotation/VAR_041628|||http://purl.uniprot.org/annotation/VAR_041629|||http://purl.uniprot.org/annotation/VAR_041630|||http://purl.uniprot.org/annotation/VAR_041631|||http://purl.uniprot.org/annotation/VAR_041632|||http://purl.uniprot.org/annotation/VAR_041633|||http://purl.uniprot.org/annotation/VAR_041634|||http://purl.uniprot.org/annotation/VAR_041635|||http://purl.uniprot.org/annotation/VAR_041636|||http://purl.uniprot.org/annotation/VAR_041637|||http://purl.uniprot.org/annotation/VAR_041638|||http://purl.uniprot.org/annotation/VAR_041639|||http://purl.uniprot.org/annotation/VAR_041640|||http://purl.uniprot.org/annotation/VAR_041641|||http://purl.uniprot.org/annotation/VAR_041642|||http://purl.uniprot.org/annotation/VAR_041643|||http://purl.uniprot.org/annotation/VAR_041644|||http://purl.uniprot.org/annotation/VAR_041645|||http://purl.uniprot.org/annotation/VAR_041646|||http://purl.uniprot.org/annotation/VAR_041647|||http://purl.uniprot.org/annotation/VAR_041648|||http://purl.uniprot.org/annotation/VAR_041649|||http://purl.uniprot.org/annotation/VAR_041650|||http://purl.uniprot.org/annotation/VAR_041651|||http://purl.uniprot.org/annotation/VAR_041652|||http://purl.uniprot.org/annotation/VAR_041653|||http://purl.uniprot.org/annotation/VAR_041654|||http://purl.uniprot.org/annotation/VAR_041655|||http://purl.uniprot.org/annotation/VAR_041656|||http://purl.uniprot.org/annotation/VAR_041657|||http://purl.uniprot.org/annotation/VSP_017746|||http://purl.uniprot.org/annotation/VSP_017747|||http://purl.uniprot.org/annotation/VSP_017748
http://togogenome.org/gene/9606:SH3D21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU49                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||Pro residues|||SH3|||SH3 domain-containing protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337129|||http://purl.uniprot.org/annotation/VAR_043619|||http://purl.uniprot.org/annotation/VAR_056763|||http://purl.uniprot.org/annotation/VSP_040923|||http://purl.uniprot.org/annotation/VSP_040924|||http://purl.uniprot.org/annotation/VSP_040925|||http://purl.uniprot.org/annotation/VSP_040926|||http://purl.uniprot.org/annotation/VSP_040927|||http://purl.uniprot.org/annotation/VSP_040928|||http://purl.uniprot.org/annotation/VSP_045936
http://togogenome.org/gene/9606:NSG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y328                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Neuronal vesicle trafficking-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164366
http://togogenome.org/gene/9606:PLEKHG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6X4|||http://purl.uniprot.org/uniprot/Q58EX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Polar residues|||Puratrophin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000224996|||http://purl.uniprot.org/annotation/VAR_050509|||http://purl.uniprot.org/annotation/VAR_050510|||http://purl.uniprot.org/annotation/VAR_050511|||http://purl.uniprot.org/annotation/VAR_050512|||http://purl.uniprot.org/annotation/VAR_061519|||http://purl.uniprot.org/annotation/VSP_017329|||http://purl.uniprot.org/annotation/VSP_017330|||http://purl.uniprot.org/annotation/VSP_017331
http://togogenome.org/gene/9606:CA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75493                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase-related protein 11|||Disordered|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004245
http://togogenome.org/gene/9606:TAS2R4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082205|||http://purl.uniprot.org/annotation/VAR_020200|||http://purl.uniprot.org/annotation/VAR_020201|||http://purl.uniprot.org/annotation/VAR_020202|||http://purl.uniprot.org/annotation/VAR_034535|||http://purl.uniprot.org/annotation/VAR_034536|||http://purl.uniprot.org/annotation/VAR_053341|||http://purl.uniprot.org/annotation/VAR_053342
http://togogenome.org/gene/9606:PSMA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK44|||http://purl.uniprot.org/uniprot/P60900                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N6-acetyllysine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphotyrosine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124130|||http://purl.uniprot.org/annotation/VSP_054586|||http://purl.uniprot.org/annotation/VSP_054587
http://togogenome.org/gene/9606:NCAPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42695                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Condensin-2 complex subunit D3|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||In MCPH22; impairs mitotic chromosome compaction.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050716|||http://purl.uniprot.org/annotation/VAR_053043|||http://purl.uniprot.org/annotation/VAR_053044|||http://purl.uniprot.org/annotation/VAR_053045|||http://purl.uniprot.org/annotation/VAR_080955
http://togogenome.org/gene/9606:ARMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7Q2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Age-related maculopathy susceptibility protein 2|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342668|||http://purl.uniprot.org/annotation/VAR_044330|||http://purl.uniprot.org/annotation/VAR_044331
http://togogenome.org/gene/9606:ZNF655                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DU4|||http://purl.uniprot.org/uniprot/Q8N720                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Zinc finger protein 655                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047700|||http://purl.uniprot.org/annotation/VAR_028165|||http://purl.uniprot.org/annotation/VSP_036030|||http://purl.uniprot.org/annotation/VSP_036031|||http://purl.uniprot.org/annotation/VSP_041157|||http://purl.uniprot.org/annotation/VSP_044809|||http://purl.uniprot.org/annotation/VSP_044810
http://togogenome.org/gene/9606:CASTOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHX0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  ACT 1|||ACT 2|||Cytosolic arginine sensor for mTORC1 subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341304
http://togogenome.org/gene/9606:TAF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16594                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Transcription initiation factor TFIID subunit 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118888|||http://purl.uniprot.org/annotation/VAR_016279|||http://purl.uniprot.org/annotation/VAR_052260
http://togogenome.org/gene/9606:CFAP90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4QMS7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 90|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336090|||http://purl.uniprot.org/annotation/VAR_043546|||http://purl.uniprot.org/annotation/VAR_043547|||http://purl.uniprot.org/annotation/VAR_043548
http://togogenome.org/gene/9606:NDFIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGY6|||http://purl.uniprot.org/uniprot/Q9NV92                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interaction with NEDD4|||Loss of E3 ubiquitin-protein ligase activation; when associated with 149-P--G-151 and 175-P--G-177. Greatly decreases NEDD4-binding; when associated with 149-P--G-151 and 175-P--G-177. No effect on PTEN-binding; when associated with 149-P--G-151 and 175-P--G-177.|||Loss of E3 ubiquitin-protein ligase activation; when associated with 149-P--G-151 and 184-P--G-186. Greatly decreases NEDD4-binding; when associated with 149-P-G-151 and 184-P--G-186. No effect on PTEN-binding; when associated with 149-P--G-151 and 184-P--G-186.|||Loss of E3 ubiquitin-protein ligase activation; when associated with 175-P--G-177 and 184-P--G-186. Greatly decreases NEDD4-binding; when associated with 175-P--G-177 and 184-P--G-186. No effect on PTEN-binding; when associated with 175-P--G-177 and 184-P--G-186.|||Loss of NDFIP2 phosphorylation by SRC.|||NEDD4 family-interacting protein 2|||Not phosphorylated by SRC|||PPxY motif 1|||PPxY motif 2|||PPxY motif 3|||Phosphotyrosine; by SRC|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096794|||http://purl.uniprot.org/annotation/VAR_023414|||http://purl.uniprot.org/annotation/VAR_061687
http://togogenome.org/gene/9606:FAM236B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUQ0|||http://purl.uniprot.org/uniprot/A0A1B0GV22                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM236A|||Protein FAM236B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440023|||http://purl.uniprot.org/annotation/PRO_0000440024
http://togogenome.org/gene/9606:IFNAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48551|||http://purl.uniprot.org/uniprot/Q9BUA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to HVB infection; lower cell surface levels; lower induction of MHC class 1 expression by INF-alpha.|||Cytoplasmic|||Disordered|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-411. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-411. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-411.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-337 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-318.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-316 and F-337.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-306; F-318 and F-337.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-269; F-316; F-318 and F-337.|||Does not inhibit STAT1, STAT2 and STAT3 activation by IFN. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-337; F-411 and F-512. Inhibits STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318; F-411 and F-512. Does not inhibit STAT1, STAT2 and STAT3 activation by IFN; when associated with F-306; F-316; F-318 and F-337.|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3.|||Interferon alpha/beta receptor 2|||Interferon/interleukin receptor|||Mediates interaction with STAT2 (and required for the recruitment of USP18)|||N-linked (GlcNAc...) asparagine|||No effect on activation of STAT1 upon IFNA2 or IFNG binding.|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011006|||http://purl.uniprot.org/annotation/VAR_020521|||http://purl.uniprot.org/annotation/VAR_020522|||http://purl.uniprot.org/annotation/VAR_020523|||http://purl.uniprot.org/annotation/VAR_084099|||http://purl.uniprot.org/annotation/VAR_084100|||http://purl.uniprot.org/annotation/VAR_084101|||http://purl.uniprot.org/annotation/VAR_084102|||http://purl.uniprot.org/annotation/VAR_084103|||http://purl.uniprot.org/annotation/VAR_084104|||http://purl.uniprot.org/annotation/VAR_084105|||http://purl.uniprot.org/annotation/VAR_084106|||http://purl.uniprot.org/annotation/VAR_084107|||http://purl.uniprot.org/annotation/VAR_084108|||http://purl.uniprot.org/annotation/VAR_084109|||http://purl.uniprot.org/annotation/VAR_084110|||http://purl.uniprot.org/annotation/VSP_001736|||http://purl.uniprot.org/annotation/VSP_001737|||http://purl.uniprot.org/annotation/VSP_001738|||http://purl.uniprot.org/annotation/VSP_001739
http://togogenome.org/gene/9606:HMHB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O97980                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Peptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  CTL recognition.|||Complete loss of CTL recognition.|||Decreased CTL recognition.|||In allele HB-1Y; loss of CTL recognition for epitope HB-1. No influence on HLA-B/HLA-B44 binding, nor on the processing by the proteasome.|||Loss of recognition by cytotoxic T lymphocyte (CTL)|||Minor histocompatibility antigen HB-1|||Minor histocompatibility protein HB-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330317|||http://purl.uniprot.org/annotation/PRO_0000330318|||http://purl.uniprot.org/annotation/VAR_042698
http://togogenome.org/gene/9606:GPR155                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXK4|||http://purl.uniprot.org/uniprot/Q49AJ5|||http://purl.uniprot.org/uniprot/Q7Z3F1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolished ability to regulate mTORC1.|||DEP|||Does not affect cholesterol-binding.|||Helical|||In 4CA, abolished ability to regulate mTORC1; when associated with A-595, A-604 and A-629.|||In 4CA, abolished ability to regulate mTORC1; when associated with A-595, A-604 and A-638.|||In 4CA, abolished ability to regulate mTORC1; when associated with A-595, A-629 and A-638.|||In 4CA, abolished ability to regulate mTORC1; when associated with A-604, A-629 and A-638.|||Lysosomal cholesterol signaling protein|||N-linked (GlcNAc...) asparagine|||Nearly abolished cholesterol-binding.|||Strongly reduced cholesterol-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087551|||http://purl.uniprot.org/annotation/PRO_5004235110
http://togogenome.org/gene/9606:JAZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with NR2C2.|||Acidic residues|||Breakpoint for translocation to form JAZF1-SUZ12 oncogene|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||Disordered|||In isoform 3.|||Juxtaposed with another zinc finger protein 1|||Little effect on interaction with NR2C2.|||Phosphothreonine|||Polar residues|||Reduces interaction with NR2C2.|||Required for interaction with NR2C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046985|||http://purl.uniprot.org/annotation/VSP_061580
http://togogenome.org/gene/9606:CARD18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57730                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix                                                                                  ^@                                                                                  CARD|||Caspase recruitment domain-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084145
http://togogenome.org/gene/9606:GLOD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK44                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Glyoxalase domain-containing protein 5|||VOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305326
http://togogenome.org/gene/9606:SAFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2F6|||http://purl.uniprot.org/uniprot/B7ZLP5|||http://purl.uniprot.org/uniprot/Q15424                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Interaction with POLR2A. Interaction with SFRS1; SFRS9 and SFRS10|||Interaction with SAFB2|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||SAP|||Scaffold attachment factor B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081905|||http://purl.uniprot.org/annotation/VSP_045838|||http://purl.uniprot.org/annotation/VSP_045839|||http://purl.uniprot.org/annotation/VSP_046902
http://togogenome.org/gene/9606:ACTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68032                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin, alpha cardiac muscle 1|||Actin, alpha cardiac muscle 1, intermediate form|||In ASD5; reduced affinity for myosin; normal actin filament polymerization ability; normal actomyosin motor function.|||In CMD1R.|||In CMH11.|||Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1|||Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1|||Methionine (R)-sulfoxide|||N-acetylcysteine; in intermediate form|||N6-methyllysine|||Removed|||Tele-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000813|||http://purl.uniprot.org/annotation/PRO_0000442998|||http://purl.uniprot.org/annotation/VAR_012857|||http://purl.uniprot.org/annotation/VAR_012858|||http://purl.uniprot.org/annotation/VAR_012859|||http://purl.uniprot.org/annotation/VAR_012860|||http://purl.uniprot.org/annotation/VAR_012861|||http://purl.uniprot.org/annotation/VAR_012862|||http://purl.uniprot.org/annotation/VAR_045924|||http://purl.uniprot.org/annotation/VAR_045925|||http://purl.uniprot.org/annotation/VAR_046502|||http://purl.uniprot.org/annotation/VAR_046503|||http://purl.uniprot.org/annotation/VAR_046504
http://togogenome.org/gene/9606:KCNA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RP8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Motif|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily A member 7|||S-palmitoyl cysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308273|||http://purl.uniprot.org/annotation/VAR_036776|||http://purl.uniprot.org/annotation/VAR_036777
http://togogenome.org/gene/9606:OR3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP1|||http://purl.uniprot.org/uniprot/P47881                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150515|||http://purl.uniprot.org/annotation/VAR_012059|||http://purl.uniprot.org/annotation/VAR_057542
http://togogenome.org/gene/9606:KRT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05787|||http://purl.uniprot.org/uniprot/Q7L4M3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Generates normal-appearing filaments, that are destabilized by okadaic acid.|||Generates normal-appearing filaments, that remain stable after okadaic acid treatment.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In CIRRH.|||In isoform 2.|||Increases phosphorylation.|||Keratin, type II cytoskeletal 8|||Linker 1|||Linker 12|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine|||Necessary for interaction with PNN|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by CaMK2 and MAPK|||Phosphoserine; by MAPK|||Phosphoserine; by PKC/PRKCE|||Phosphothreonine|||Phosphotyrosine|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063740|||http://purl.uniprot.org/annotation/VAR_023058|||http://purl.uniprot.org/annotation/VAR_023059|||http://purl.uniprot.org/annotation/VAR_023060|||http://purl.uniprot.org/annotation/VAR_023061|||http://purl.uniprot.org/annotation/VAR_049805|||http://purl.uniprot.org/annotation/VAR_069106|||http://purl.uniprot.org/annotation/VAR_069107|||http://purl.uniprot.org/annotation/VSP_046000
http://togogenome.org/gene/9606:NUDCD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CS|||Disordered|||NudC domain-containing protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057985|||http://purl.uniprot.org/annotation/VAR_031709|||http://purl.uniprot.org/annotation/VAR_054036
http://togogenome.org/gene/9606:NHLH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02575|||http://purl.uniprot.org/uniprot/Q5T203                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||Helix-loop-helix protein 1|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127197
http://togogenome.org/gene/9606:TP53BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12888                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR).|||Abolishes recruitment to double strand breaks.|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1609.|||Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1618.|||Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'.|||Disordered|||Does not affect recruitment to double strand breaks.|||GAR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-13; A-25; A-29; A-105; A-166; A-176 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-105; A-166; A-176 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1171.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-176.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-176 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-166; A-176 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-29; A-105; A-166; A-176 and A-178.|||In 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-25; A-29; A-105; A-166; A-176 and A-178.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks.|||Interaction with dimethylated histone H4|||Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1495.|||Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1521.|||Loss of phosphorylation site.|||No detectable effect on methylation by PRMT1 (in vitro).|||No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1401.|||No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1403.|||No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1401 and A-1403.|||No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1400; A-1401 and A-1403.|||No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1398; A-1400; A-1401 and A-1403.|||No effect on in class-switch recombination (CSR).|||No effect on recruitment to double strand breaks.|||Omega-N-methylarginine|||Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with D-1618.|||Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with E-1609.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400.|||Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401.|||Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401.|||Reduced recruitment to double strand breaks.|||Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'.|||Reduces recruitment to double strand breaks.|||Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR).|||Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). Does not affect interaction with histone H4 dimethylated at 'Lys-20' (H4K20me2). Impaired interaction with histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub).|||TP53-binding protein 1|||Tudor-like|||UDR ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072643|||http://purl.uniprot.org/annotation/VAR_022172|||http://purl.uniprot.org/annotation/VAR_022173|||http://purl.uniprot.org/annotation/VAR_022174|||http://purl.uniprot.org/annotation/VAR_022175|||http://purl.uniprot.org/annotation/VAR_022176|||http://purl.uniprot.org/annotation/VAR_022177|||http://purl.uniprot.org/annotation/VAR_022178|||http://purl.uniprot.org/annotation/VAR_022179|||http://purl.uniprot.org/annotation/VAR_022180|||http://purl.uniprot.org/annotation/VAR_034558|||http://purl.uniprot.org/annotation/VAR_034559|||http://purl.uniprot.org/annotation/VAR_034560|||http://purl.uniprot.org/annotation/VAR_038689|||http://purl.uniprot.org/annotation/VSP_018390|||http://purl.uniprot.org/annotation/VSP_055062
http://togogenome.org/gene/9606:ATRAID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UW56                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  All-trans retinoic acid-induced differentiation factor|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020752|||http://purl.uniprot.org/annotation/VAR_057991|||http://purl.uniprot.org/annotation/VSP_014108|||http://purl.uniprot.org/annotation/VSP_037521
http://togogenome.org/gene/9606:AFAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRV0|||http://purl.uniprot.org/uniprot/Q8N556                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin filament-associated protein 1|||Decreased tyrosine phosphorylation.|||Disordered|||In isoform 2.|||Interaction with F-actin|||N-acetylmethionine|||No effect on tyrosine phosphorylation.|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-125; F-451 and F-453.|||Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-451.|||Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-453.|||Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-451 and F-453.|||Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-94; F-125; F-451 and F-453.|||SH2-binding 1|||SH2-binding 2|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317658|||http://purl.uniprot.org/annotation/VAR_038578|||http://purl.uniprot.org/annotation/VAR_038579|||http://purl.uniprot.org/annotation/VSP_044838
http://togogenome.org/gene/9606:ARPP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BMD8|||http://purl.uniprot.org/uniprot/P56211                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform ARPP-16.|||N-acetylmethionine|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by GWL|||Polar residues|||Removed|||cAMP-regulated phosphoprotein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008041|||http://purl.uniprot.org/annotation/VSP_018555
http://togogenome.org/gene/9606:SLC38A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BMC5|||http://purl.uniprot.org/uniprot/Q9NVC3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Amino acid transporter transmembrane|||Helical|||In isoform 2.|||Phosphoserine|||Sodium-coupled neutral amino acid transporter 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319597|||http://purl.uniprot.org/annotation/VAR_039015|||http://purl.uniprot.org/annotation/VAR_039016|||http://purl.uniprot.org/annotation/VSP_031511
http://togogenome.org/gene/9606:HMMR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75330                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Hyaluronan mediated motility receptor|||Hyaluronic acid-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Required for interaction with FAM83D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084007|||http://purl.uniprot.org/annotation/VAR_020044|||http://purl.uniprot.org/annotation/VAR_024155|||http://purl.uniprot.org/annotation/VAR_024156|||http://purl.uniprot.org/annotation/VAR_024157|||http://purl.uniprot.org/annotation/VAR_031661|||http://purl.uniprot.org/annotation/VAR_056917|||http://purl.uniprot.org/annotation/VAR_056918|||http://purl.uniprot.org/annotation/VAR_056919|||http://purl.uniprot.org/annotation/VSP_004286|||http://purl.uniprot.org/annotation/VSP_038378|||http://purl.uniprot.org/annotation/VSP_041266
http://togogenome.org/gene/9606:DLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K019|||http://purl.uniprot.org/uniprot/P80370                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||Extracellular|||Fetal antigen 1|||Helical|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical; partial|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Protein delta homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007518|||http://purl.uniprot.org/annotation/PRO_0000007519|||http://purl.uniprot.org/annotation/PRO_5002722084|||http://purl.uniprot.org/annotation/VAR_002274|||http://purl.uniprot.org/annotation/VAR_055715|||http://purl.uniprot.org/annotation/VAR_055716|||http://purl.uniprot.org/annotation/VAR_055717|||http://purl.uniprot.org/annotation/VAR_060335|||http://purl.uniprot.org/annotation/VAR_060336|||http://purl.uniprot.org/annotation/VSP_001377
http://togogenome.org/gene/9606:ERMAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1C9HIH9|||http://purl.uniprot.org/uniprot/Q96PL5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Cytoplasmic|||Erythroid membrane-associated protein|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In Sc-3 allele.|||In Sc2 antigen.|||In Sc4 antigen.|||In Sc5 antigen.|||In Sc6 antigen.|||In Sc7 antigen.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226088|||http://purl.uniprot.org/annotation/PRO_5014266671|||http://purl.uniprot.org/annotation/VAR_025478|||http://purl.uniprot.org/annotation/VAR_025479|||http://purl.uniprot.org/annotation/VAR_025480|||http://purl.uniprot.org/annotation/VAR_025481|||http://purl.uniprot.org/annotation/VAR_025482|||http://purl.uniprot.org/annotation/VAR_025483|||http://purl.uniprot.org/annotation/VAR_025484|||http://purl.uniprot.org/annotation/VAR_025485|||http://purl.uniprot.org/annotation/VAR_025486|||http://purl.uniprot.org/annotation/VAR_025487|||http://purl.uniprot.org/annotation/VAR_025488
http://togogenome.org/gene/9606:PNMA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PV4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Paraneoplastic antigen-like protein 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311217|||http://purl.uniprot.org/annotation/VAR_037164|||http://purl.uniprot.org/annotation/VAR_037165
http://togogenome.org/gene/9606:MMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN15|||http://purl.uniprot.org/uniprot/P03956|||http://purl.uniprot.org/uniprot/Q53G95                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  22 kDa interstitial collagenase|||27 kDa interstitial collagenase|||Activation peptide|||Cleavage; by autolysis|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Interstitial collagenase|||Metalloprotease|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Partial reduction of tyrosine phosphorylation in the presence of PKDCC/VLK.|||Peptidase metallopeptidase|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by PKDCC|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000105|||http://purl.uniprot.org/annotation/PRO_0000028703|||http://purl.uniprot.org/annotation/PRO_0000028704|||http://purl.uniprot.org/annotation/PRO_0000028705|||http://purl.uniprot.org/annotation/PRO_0000028706|||http://purl.uniprot.org/annotation/VAR_011969|||http://purl.uniprot.org/annotation/VAR_011970|||http://purl.uniprot.org/annotation/VAR_021024|||http://purl.uniprot.org/annotation/VAR_021025|||http://purl.uniprot.org/annotation/VAR_021026|||http://purl.uniprot.org/annotation/VAR_054005
http://togogenome.org/gene/9606:TMEM109                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVC6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Voltage-gated monoatomic cation channel TMEM109                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000044618
http://togogenome.org/gene/9606:CCDC102A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A19                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 102A|||Disordered|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274400
http://togogenome.org/gene/9606:CD1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29017                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Internalization signal|||N-linked (GlcNAc...) asparagine|||T-cell surface glycoprotein CD1c                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014580|||http://purl.uniprot.org/annotation/VAR_031564|||http://purl.uniprot.org/annotation/VAR_031565
http://togogenome.org/gene/9606:CCDC182                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NF36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 182                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329034
http://togogenome.org/gene/9606:TTC33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PID6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287515|||http://purl.uniprot.org/annotation/VAR_032317
http://togogenome.org/gene/9606:RAB34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DI83|||http://purl.uniprot.org/uniprot/Q9BZG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||13 x 9 AA approximate tandem-repeats of P-R-V-I-V-G-(S/T)-P-R|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||Effector region|||In isoform 2.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Ras-related protein Rab-34|||Ras-related protein Rab-34, isoform NARR|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121243|||http://purl.uniprot.org/annotation/PRO_0000412533|||http://purl.uniprot.org/annotation/VAR_015097|||http://purl.uniprot.org/annotation/VSP_010142|||http://purl.uniprot.org/annotation/VSP_044734
http://togogenome.org/gene/9606:TSPAN31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFJ7|||http://purl.uniprot.org/uniprot/F8VWE0|||http://purl.uniprot.org/uniprot/Q12999                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219270|||http://purl.uniprot.org/annotation/PRO_5010105405
http://togogenome.org/gene/9606:PRR23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Proline-rich protein 23A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332252
http://togogenome.org/gene/9606:ST6GAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JF0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-galactoside alpha-2,6-sialyltransferase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314785|||http://purl.uniprot.org/annotation/VAR_038046|||http://purl.uniprot.org/annotation/VAR_038047|||http://purl.uniprot.org/annotation/VSP_030356
http://togogenome.org/gene/9606:MYOT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFM5|||http://purl.uniprot.org/uniprot/B4DT68|||http://purl.uniprot.org/uniprot/Q9UBF9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In MFM3 and MFM3.|||In MFM3.|||In MFM3; does not abolish interaction with ACTN1.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Myotilin|||Necessary for interaction with ACTA1|||Necessary for interaction with ACTN1|||Necessary for interaction with FLNC|||Omega-N-methylarginine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072687|||http://purl.uniprot.org/annotation/VAR_021569|||http://purl.uniprot.org/annotation/VAR_021570|||http://purl.uniprot.org/annotation/VAR_021571|||http://purl.uniprot.org/annotation/VAR_021572|||http://purl.uniprot.org/annotation/VAR_021573|||http://purl.uniprot.org/annotation/VAR_029532|||http://purl.uniprot.org/annotation/VAR_029533|||http://purl.uniprot.org/annotation/VAR_035520|||http://purl.uniprot.org/annotation/VAR_049914|||http://purl.uniprot.org/annotation/VSP_041450
http://togogenome.org/gene/9606:CLINT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Y4|||http://purl.uniprot.org/uniprot/A0A0S2Z5H3|||http://purl.uniprot.org/uniprot/Q14677                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to VTI1B.|||Abolished binding to VTI1B. Rescued binding to VTI1BR-23 mutant.|||Abolishes lipid binding; when associated with L-29.|||Basic and acidic residues|||Clathrin interactor 1|||Decreases AP-1 and AP-2 binding.|||Disordered|||ENTH|||In isoform 2.|||In isoform 3.|||Interaction with AP1G1 and AP1G2|||Interaction with AP1G1, AP1G2 and GGA2|||Interaction with VTI1B|||Normal binding to VTI1B.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces lipid binding. Abolishes lipid binding; when associated with G-34.|||Slightly decreases AP-1 binding.|||Strongly decreases clathrin binding.|||Strongly reduces clathrin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074521|||http://purl.uniprot.org/annotation/VSP_009160|||http://purl.uniprot.org/annotation/VSP_009161|||http://purl.uniprot.org/annotation/VSP_043302
http://togogenome.org/gene/9606:KRT82                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSB4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type II cuticular Hb2|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063697|||http://purl.uniprot.org/annotation/VAR_018118|||http://purl.uniprot.org/annotation/VAR_032786|||http://purl.uniprot.org/annotation/VAR_032787
http://togogenome.org/gene/9606:NXPE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DL1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||NXPE family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297592|||http://purl.uniprot.org/annotation/VAR_034647|||http://purl.uniprot.org/annotation/VSP_040454|||http://purl.uniprot.org/annotation/VSP_040455
http://togogenome.org/gene/9606:TMEM128                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3K1|||http://purl.uniprot.org/uniprot/Q5BJH2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 128                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254556|||http://purl.uniprot.org/annotation/VAR_080190|||http://purl.uniprot.org/annotation/VSP_021229
http://togogenome.org/gene/9606:TBC1D25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF03|||http://purl.uniprot.org/uniprot/Q3MII6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with GABARAP. Does not localize at autophagosomes.|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-GAP TBC|||Severely affects interaction with GABARAP. Does not localize at autophagosomes.|||TBC1 domain family member 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288508|||http://purl.uniprot.org/annotation/VAR_057345|||http://purl.uniprot.org/annotation/VSP_025703|||http://purl.uniprot.org/annotation/VSP_025704
http://togogenome.org/gene/9606:OR8K5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH50                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8K5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150673|||http://purl.uniprot.org/annotation/VAR_048056
http://togogenome.org/gene/9606:ZBTB7C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1YPR0|||http://purl.uniprot.org/uniprot/B2RG49                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||Disordered|||Zinc finger and BTB domain-containing protein 7C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337869
http://togogenome.org/gene/9606:GUCA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16661                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Guanylate cyclase C-activating peptide 2|||Uroguanylin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013147|||http://purl.uniprot.org/annotation/PRO_0000013148|||http://purl.uniprot.org/annotation/PRO_0000013149|||http://purl.uniprot.org/annotation/VAR_053362
http://togogenome.org/gene/9606:SPG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y632|||http://purl.uniprot.org/uniprot/Q9UQ90                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||Helical|||In SPG7.|||In SPG7; function impaired.|||In isoform 2.|||Interaction with PPIF|||Loss of proteolytic activity but no loss of interaction with PPIF; when associated with G-574 and S-577.|||Loss of proteolytic activity but no loss of interaction with PPIF; when associated with G-575 and S-577.|||Might be implicated in the hereditary spastic paraplegia phenotype.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||No loss of interaction with PPIF. Loss of proteolytic activity but no loss of interaction with PPIF; when associated with G-574 and G-575.|||Paraplegin|||Removed in mature form|||Requires 2 nucleotide substitutions; might be implicated in the hereditary spastic paraplegia phenotype.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084675|||http://purl.uniprot.org/annotation/PRO_0000442305|||http://purl.uniprot.org/annotation/VAR_017433|||http://purl.uniprot.org/annotation/VAR_017434|||http://purl.uniprot.org/annotation/VAR_045898|||http://purl.uniprot.org/annotation/VAR_048117|||http://purl.uniprot.org/annotation/VAR_048118|||http://purl.uniprot.org/annotation/VAR_059086|||http://purl.uniprot.org/annotation/VAR_063603|||http://purl.uniprot.org/annotation/VAR_063604|||http://purl.uniprot.org/annotation/VAR_063605|||http://purl.uniprot.org/annotation/VAR_063606|||http://purl.uniprot.org/annotation/VAR_063607|||http://purl.uniprot.org/annotation/VAR_063608|||http://purl.uniprot.org/annotation/VAR_063609|||http://purl.uniprot.org/annotation/VAR_063610|||http://purl.uniprot.org/annotation/VAR_063611|||http://purl.uniprot.org/annotation/VAR_063612|||http://purl.uniprot.org/annotation/VAR_063613|||http://purl.uniprot.org/annotation/VAR_063614|||http://purl.uniprot.org/annotation/VAR_063615|||http://purl.uniprot.org/annotation/VSP_009192|||http://purl.uniprot.org/annotation/VSP_009193
http://togogenome.org/gene/9606:PGS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32NB8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337105|||http://purl.uniprot.org/annotation/VSP_033897|||http://purl.uniprot.org/annotation/VSP_033898|||http://purl.uniprot.org/annotation/VSP_033899|||http://purl.uniprot.org/annotation/VSP_033900|||http://purl.uniprot.org/annotation/VSP_033901|||http://purl.uniprot.org/annotation/VSP_033902|||http://purl.uniprot.org/annotation/VSP_033903
http://togogenome.org/gene/9606:B4GALT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAZ5|||http://purl.uniprot.org/uniprot/B3KM35|||http://purl.uniprot.org/uniprot/O60513                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase|||Beta-1,4-galactosyltransferase 4|||Cytoplasmic|||Galactosyltransferase C-terminal|||Galactosyltransferase N-terminal|||Has no impact on N-glycosylation.|||Has no impact on localization to the Golgi apparatus. Decreases N-glycosylation. Impairs the catalytic activity. Impairs keratan sulfate biosynthesis; when associated with A-337.|||Helical; Signal-anchor for type II membrane protein|||Impairs localization to the Golgi apparatus. Abolishes N-glycosylation. Impairs the interaction with SLC35A/UGT1. Impairs the catalytic activity. Impairs keratan sulfate biosynthesis; when associated with A-222.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080542|||http://purl.uniprot.org/annotation/PRO_5002789993|||http://purl.uniprot.org/annotation/PRO_5014298332|||http://purl.uniprot.org/annotation/VAR_022697
http://togogenome.org/gene/9606:KRTAP5-7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8G8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184105
http://togogenome.org/gene/9606:CTAGE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX94                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||cTAGE family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189540
http://togogenome.org/gene/9606:FEZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99689                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fasciculation and elongation protein zeta-1|||In isoform Short.|||Interchain|||Loss of SCOC-binding. No effect on ULK1-binding.|||No effect on SCOC--binding.|||No effect on SCOC-binding.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189525|||http://purl.uniprot.org/annotation/VAR_020461|||http://purl.uniprot.org/annotation/VSP_006951
http://togogenome.org/gene/9606:NR1I3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1DAL4|||http://purl.uniprot.org/uniprot/Q14994                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Found in a patient with Kleefstra syndrome; unknown pathological significance.|||In isoform 13.|||In isoform 2, isoform 5, isoform 6, isoform 9 and isoform 10.|||In isoform 3.|||In isoform 4, isoform 5, isoform 6, isoform 9, isoform 10, isoform 11 and isoform 15.|||In isoform 4, isoform 7, isoform 14 and isoform 15.|||In isoform 6, isoform 8, isoform 10, isoform 11 and isoform 13.|||In isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 14 and isoform 15.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 1 group I member 3|||Phosphothreonine; by PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053552|||http://purl.uniprot.org/annotation/VAR_018344|||http://purl.uniprot.org/annotation/VAR_080264|||http://purl.uniprot.org/annotation/VSP_010634|||http://purl.uniprot.org/annotation/VSP_043144|||http://purl.uniprot.org/annotation/VSP_043730|||http://purl.uniprot.org/annotation/VSP_043731|||http://purl.uniprot.org/annotation/VSP_043732|||http://purl.uniprot.org/annotation/VSP_046144|||http://purl.uniprot.org/annotation/VSP_055180
http://togogenome.org/gene/9606:ARHGAP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P85298|||http://purl.uniprot.org/uniprot/Q6PJW1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CRAL-TRIO|||Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Rho GTPase-activating protein 8|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308161|||http://purl.uniprot.org/annotation/VAR_049138|||http://purl.uniprot.org/annotation/VAR_049139|||http://purl.uniprot.org/annotation/VAR_049140|||http://purl.uniprot.org/annotation/VAR_061182|||http://purl.uniprot.org/annotation/VSP_001652|||http://purl.uniprot.org/annotation/VSP_001656|||http://purl.uniprot.org/annotation/VSP_001657|||http://purl.uniprot.org/annotation/VSP_028883|||http://purl.uniprot.org/annotation/VSP_054100|||http://purl.uniprot.org/annotation/VSP_054101
http://togogenome.org/gene/9606:SLC25A48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZT89                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325768|||http://purl.uniprot.org/annotation/VSP_032397|||http://purl.uniprot.org/annotation/VSP_032398|||http://purl.uniprot.org/annotation/VSP_032399
http://togogenome.org/gene/9606:PLAUR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R1I2|||http://purl.uniprot.org/uniprot/Q03405                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by U-PA|||GPI-anchor amidated glycine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6|||UPAR/Ly6 1|||UPAR/Ly6 2|||UPAR/Ly6 3|||Urokinase plasminogen activator surface receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036090|||http://purl.uniprot.org/annotation/PRO_0000036091|||http://purl.uniprot.org/annotation/PRO_5004004107|||http://purl.uniprot.org/annotation/VAR_014922|||http://purl.uniprot.org/annotation/VAR_016322|||http://purl.uniprot.org/annotation/VAR_016323|||http://purl.uniprot.org/annotation/VAR_016324|||http://purl.uniprot.org/annotation/VAR_016325|||http://purl.uniprot.org/annotation/VAR_016326|||http://purl.uniprot.org/annotation/VAR_052698|||http://purl.uniprot.org/annotation/VSP_006715|||http://purl.uniprot.org/annotation/VSP_046345|||http://purl.uniprot.org/annotation/VSP_046346
http://togogenome.org/gene/9606:ZSCAN18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243921|||http://purl.uniprot.org/annotation/VAR_026871|||http://purl.uniprot.org/annotation/VSP_019497|||http://purl.uniprot.org/annotation/VSP_043272|||http://purl.uniprot.org/annotation/VSP_047060
http://togogenome.org/gene/9606:SSX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTT5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||KRAB-related|||Phosphoserine|||Polar residues|||Protein SSX7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227811|||http://purl.uniprot.org/annotation/VAR_053694
http://togogenome.org/gene/9606:DDRGK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HY6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDRGK domain-containing protein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)|||Impairs interaction with UFL1 and ufmylation. Impairs interaction with ERN1/IRE1-alpha and ability to regulate its stability. Does not affect ability to promote reticulophagy. Impairs some post-translational modification without affecting interaction with UFL1; when associated with 116-R--R-128, R-146, R-176, R-193, 224-R--R-227 and R-267.|||Impairs some post-translational modification without affecting interaction with UFL1; when associated with 116-R--R-128, R-146, R-176, R-193 and R-267.|||Impairs some post-translational modification without affecting interaction with UFL1; when associated with 116-R--R-128, R-146, R-193, 224-R--R-227 and R-267.|||Impairs some post-translational modification without affecting interaction with UFL1; when associated with 116-R--R-128, R-176, R-193, 224-R--R-227 and R-267.|||Impairs some post-translational modification without affecting interaction with UFL1; when associated with R-146, R-176, R-193, 224-R--R-227 and R-267.|||In isoform 2.|||Mediates interaction with CDK5RAP3|||Mediates interaction with TRIP4|||Mediates interaction with UFL1|||PCI|||Phosphoserine|||Weak or no effect on ufmylation.|||Weak or no effect on ufmylation. Impairs some post-translational modification without affecting interaction with UFL1; when associated with 116-R--R-128, R-146, R-176, 224-R--R-227 and R-267.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021033|||http://purl.uniprot.org/annotation/VAR_016923|||http://purl.uniprot.org/annotation/VSP_008391
http://togogenome.org/gene/9606:EMC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YNH6|||http://purl.uniprot.org/uniprot/Q9Y3B6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  ER membrane protein complex subunit 9|||MPN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221189|||http://purl.uniprot.org/annotation/PRO_5003546766|||http://purl.uniprot.org/annotation/VAR_052532
http://togogenome.org/gene/9606:STAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0IN09|||http://purl.uniprot.org/uniprot/Q6ZMT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of interaction with CACNA1S.|||Mildly decreased affinity for CACNA1S.|||No effect on the structure of the two SH3 domains.|||Phorbol-ester/DAG-type|||Phosphoserine|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 and cysteine-rich domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274413|||http://purl.uniprot.org/annotation/VSP_022742
http://togogenome.org/gene/9606:GPRC5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFJ5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Retinoic acid-induced protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206895|||http://purl.uniprot.org/annotation/VAR_018296|||http://purl.uniprot.org/annotation/VAR_049281|||http://purl.uniprot.org/annotation/VAR_049282
http://togogenome.org/gene/9606:TAS2R40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59535                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082288|||http://purl.uniprot.org/annotation/VAR_053350|||http://purl.uniprot.org/annotation/VAR_053351
http://togogenome.org/gene/9606:CDK11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DII1|||http://purl.uniprot.org/uniprot/P21127                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 11B|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform SV5 and isoform 8.|||In isoform 2.|||In isoform 3.|||In isoform 7.|||In isoform SV1, isoform 2, isoform SV5, isoform 8, isoform SV10 and isoform SV11.|||In isoform SV11.|||In isoform SV4.|||In isoform SV5 and isoform SV10.|||Phosphoserine|||Phosphoserine; by CDK7|||Phosphothreonine|||Phosphothreonine; by CDK7|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024311|||http://purl.uniprot.org/annotation/VAR_041958|||http://purl.uniprot.org/annotation/VAR_041959|||http://purl.uniprot.org/annotation/VAR_041960|||http://purl.uniprot.org/annotation/VAR_041961|||http://purl.uniprot.org/annotation/VAR_041962|||http://purl.uniprot.org/annotation/VAR_041963|||http://purl.uniprot.org/annotation/VAR_041964|||http://purl.uniprot.org/annotation/VAR_045577|||http://purl.uniprot.org/annotation/VAR_045578|||http://purl.uniprot.org/annotation/VAR_057775|||http://purl.uniprot.org/annotation/VAR_062199|||http://purl.uniprot.org/annotation/VSP_008273|||http://purl.uniprot.org/annotation/VSP_008274|||http://purl.uniprot.org/annotation/VSP_008275|||http://purl.uniprot.org/annotation/VSP_008276|||http://purl.uniprot.org/annotation/VSP_008277|||http://purl.uniprot.org/annotation/VSP_008278|||http://purl.uniprot.org/annotation/VSP_008279|||http://purl.uniprot.org/annotation/VSP_008280|||http://purl.uniprot.org/annotation/VSP_018834
http://togogenome.org/gene/9606:PTX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26022                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interchain|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Pentraxin-related protein PTX3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023545|||http://purl.uniprot.org/annotation/VAR_043140|||http://purl.uniprot.org/annotation/VAR_043141|||http://purl.uniprot.org/annotation/VAR_043142|||http://purl.uniprot.org/annotation/VAR_043143
http://togogenome.org/gene/9606:NFATC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5B2P4|||http://purl.uniprot.org/uniprot/Q13469                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3 X approximate SP repeats|||3; approximate|||9aaTAD|||Calcineurin-binding|||Disordered|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Nuclear export signal|||Nuclear factor of activated T-cells, cytoplasmic 2|||Nuclear localization signal|||Phosphoserine|||Polar residues|||RHD|||Required for cytoplasmic retention of the phosphorylated form|||Transactivation domain A (TAD-A)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205178|||http://purl.uniprot.org/annotation/VAR_051783|||http://purl.uniprot.org/annotation/VSP_005595|||http://purl.uniprot.org/annotation/VSP_042757|||http://purl.uniprot.org/annotation/VSP_055926
http://togogenome.org/gene/9606:TRIML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJA0|||http://purl.uniprot.org/uniprot/B7ZLC3|||http://purl.uniprot.org/uniprot/Q8N7C3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||In isoform 2.|||Probable E3 ubiquitin-protein ligase TRIML2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317435|||http://purl.uniprot.org/annotation/VSP_055447|||http://purl.uniprot.org/annotation/VSP_055448
http://togogenome.org/gene/9606:INSRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14616                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||Insulin receptor-related protein|||Insulin receptor-related protein alpha chain|||Insulin receptor-related protein beta chain|||Interchain (between alpha and beta chains)|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016701|||http://purl.uniprot.org/annotation/PRO_0000016702|||http://purl.uniprot.org/annotation/PRO_0000016703|||http://purl.uniprot.org/annotation/VAR_041434|||http://purl.uniprot.org/annotation/VAR_041435|||http://purl.uniprot.org/annotation/VAR_041436|||http://purl.uniprot.org/annotation/VAR_041437|||http://purl.uniprot.org/annotation/VAR_041438|||http://purl.uniprot.org/annotation/VAR_041439|||http://purl.uniprot.org/annotation/VAR_041440|||http://purl.uniprot.org/annotation/VAR_041441
http://togogenome.org/gene/9606:VNN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95497                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||CN hydrolase|||GPI-anchor amidated glycine|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Pantetheinase|||Proton acceptor|||Proton donor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019712|||http://purl.uniprot.org/annotation/PRO_0000019713|||http://purl.uniprot.org/annotation/VAR_023529|||http://purl.uniprot.org/annotation/VAR_023967|||http://purl.uniprot.org/annotation/VAR_023968|||http://purl.uniprot.org/annotation/VAR_023969|||http://purl.uniprot.org/annotation/VAR_023970|||http://purl.uniprot.org/annotation/VAR_023971|||http://purl.uniprot.org/annotation/VAR_023972|||http://purl.uniprot.org/annotation/VAR_023973|||http://purl.uniprot.org/annotation/VAR_023974
http://togogenome.org/gene/9606:HSPB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14558|||http://purl.uniprot.org/uniprot/V9HWB6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Deamidated glutamine|||Decreases heteromer formation with CRYAB.|||Decreases phosphorylation at Ser-16; abolishes cardioprotective effects.|||Heat shock protein beta-6|||Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-3.|||Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-5.|||Involved in stabilization of the HSPB1:HSBP6 heterodimer|||No effect on homodimer-based self-association properties; no effect on chaperone activity.|||Phosphoserine; by PKA|||SHSP|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125939|||http://purl.uniprot.org/annotation/VAR_077818
http://togogenome.org/gene/9606:SKIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PGP7                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Found in a THES1 patient.|||In THES1.|||N-acetylserine|||Removed|||Superkiller complex protein 3|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 17|||TPR 18|||TPR 19|||TPR 2|||TPR 20|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251722|||http://purl.uniprot.org/annotation/VAR_027705|||http://purl.uniprot.org/annotation/VAR_027706|||http://purl.uniprot.org/annotation/VAR_065297|||http://purl.uniprot.org/annotation/VAR_065298|||http://purl.uniprot.org/annotation/VAR_065299|||http://purl.uniprot.org/annotation/VAR_065300|||http://purl.uniprot.org/annotation/VAR_067957|||http://purl.uniprot.org/annotation/VAR_067958|||http://purl.uniprot.org/annotation/VAR_067959
http://togogenome.org/gene/9606:CISD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7P0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  CDGSH iron-sulfur domain-containing protein 3, mitochondrial|||Increases iron-sulfur cluster stability; when associated with C-113.|||Increases iron-sulfur cluster stability; when associated with C-75.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341405
http://togogenome.org/gene/9606:ADH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28332|||http://purl.uniprot.org/uniprot/Q8IUN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alcohol dehydrogenase 6|||Alcohol dehydrogenase-like C-terminal|||Alcohol dehydrogenase-like N-terminal|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160687|||http://purl.uniprot.org/annotation/VAR_022655|||http://purl.uniprot.org/annotation/VAR_022656|||http://purl.uniprot.org/annotation/VAR_048198|||http://purl.uniprot.org/annotation/VSP_037702
http://togogenome.org/gene/9606:RPS24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y849|||http://purl.uniprot.org/uniprot/P62847                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphothreonine|||Small ribosomal subunit protein eS24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137623|||http://purl.uniprot.org/annotation/VSP_005724|||http://purl.uniprot.org/annotation/VSP_039113|||http://purl.uniprot.org/annotation/VSP_045672
http://togogenome.org/gene/9606:HTR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K215|||http://purl.uniprot.org/uniprot/P28222|||http://purl.uniprot.org/uniprot/X5D7I5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 1B|||Abolishes agonist binding.|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes and signaling|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for species-specific agonist sensitivity|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||No effect on agonist binding.|||S-palmitoyl cysteine|||Slightly decreases agonist binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068916|||http://purl.uniprot.org/annotation/VAR_011715|||http://purl.uniprot.org/annotation/VAR_011831|||http://purl.uniprot.org/annotation/VAR_011832|||http://purl.uniprot.org/annotation/VAR_011833
http://togogenome.org/gene/9606:OTUD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G74                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cys-loop|||Disordered|||His-loop|||In MCAND; decreased mRNA and protein levels; no effect on cleavage activity towards 'K-48'-chains but not 'K-63'-chains; in mice embryo the mutation is lethal; no effect on phosphorylation.|||In MCAND; in mice embryo the mutation is lethal; reduced cleavage activity towards 'K-48'-chains but not 'K-63'-chains; no effect on nuclear location; no effect on phosphorylation.|||In MCAND; partial mislocation at the cytoplasm; reduced cleavage activity towards 'K-63'- and 'K-48'-chains; no effect on phosphorylation.|||In MCAND; reduced cleavage activity towards 'K-48'-chains but not 'K-63'-chains; no effect on phosphorylation.|||In MCAND; reduced cleavage activity towards 'K-63'- and 'K-48'-chains; no effect on phosphorylation.|||In MCAND; unknown pathological significance.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-542.|||Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-549.|||Loss of deubiquitinase activity. Abolishes activation by protein kinases.|||Loss of deubiquitinase activity. Loss of suppression of IFN production. No effect on nuclear location.|||Nucleophile|||OTU|||OTU domain-containing protein 5|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Reduced phosphorylation. Reduced ability to promote stabilization of BTRC; when associated with A-328 and A-337.|||Reduced phosphorylation. Reduced ability to promote stabilization of BTRC; when associated with A-328 and A-508.|||Reduced phosphorylation. Reduced ability to promote stabilization of BTRC; when associated with A-337 and A-508.|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278223|||http://purl.uniprot.org/annotation/VAR_085336|||http://purl.uniprot.org/annotation/VAR_085337|||http://purl.uniprot.org/annotation/VAR_085338|||http://purl.uniprot.org/annotation/VAR_085339|||http://purl.uniprot.org/annotation/VAR_085340|||http://purl.uniprot.org/annotation/VAR_085341|||http://purl.uniprot.org/annotation/VAR_085342|||http://purl.uniprot.org/annotation/VSP_023192|||http://purl.uniprot.org/annotation/VSP_023193|||http://purl.uniprot.org/annotation/VSP_023194|||http://purl.uniprot.org/annotation/VSP_023195|||http://purl.uniprot.org/annotation/VSP_045185
http://togogenome.org/gene/9606:ZMYND12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0C1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  MYND-type; atypical|||TPR 1|||TPR 2|||Zinc finger MYND domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218316|||http://purl.uniprot.org/annotation/VAR_018425
http://togogenome.org/gene/9606:WSCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658N2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Sialate:O-sulfotransferase 1|||WSC 1|||WSC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305061|||http://purl.uniprot.org/annotation/VAR_035160
http://togogenome.org/gene/9606:DAXX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCS3|||http://purl.uniprot.org/uniprot/B4E1C1|||http://purl.uniprot.org/uniprot/Q53F85|||http://purl.uniprot.org/uniprot/Q9UER7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Interaction with Puumala hantavirus nucleoprotein|||Abolishes interaction with histone H3.3.|||Abolishes interaction with histones H3 and H4.|||Abolishes sumoylation.|||Abolishes sumoylation; when associated with A-630.|||Abolishes sumoylation; when associated with A-631.|||Acidic residues|||Daxx N-terminal Rassf1C-interacting|||Death domain-associated protein 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with histones H3 and H4.|||In isoform 2.|||In isoform 3.|||In isoform beta.|||In isoform gamma.|||Interaction with MAP3K5|||Interaction with SPOP|||Interaction with histone H3.3|||N6-acetyllysine|||Necessary for interaction with USP7|||Necessary for interaction with USP7 and ATRX|||No effect on cytosol translocation. upon glucose deprivation.|||No translocation to the cytosol upon glucose deprivation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sumo interaction motif (SIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000151258|||http://purl.uniprot.org/annotation/VSP_001270|||http://purl.uniprot.org/annotation/VSP_045588|||http://purl.uniprot.org/annotation/VSP_057437|||http://purl.uniprot.org/annotation/VSP_057438|||http://purl.uniprot.org/annotation/VSP_057439|||http://purl.uniprot.org/annotation/VSP_057440
http://togogenome.org/gene/9606:OR10G4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWS5|||http://purl.uniprot.org/uniprot/Q8NGN3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10G4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150697|||http://purl.uniprot.org/annotation/VAR_034283|||http://purl.uniprot.org/annotation/VAR_034284|||http://purl.uniprot.org/annotation/VAR_053275|||http://purl.uniprot.org/annotation/VAR_053276|||http://purl.uniprot.org/annotation/VAR_053277|||http://purl.uniprot.org/annotation/VAR_053278|||http://purl.uniprot.org/annotation/VAR_053279|||http://purl.uniprot.org/annotation/VAR_060025|||http://purl.uniprot.org/annotation/VAR_060026|||http://purl.uniprot.org/annotation/VAR_060027|||http://purl.uniprot.org/annotation/VAR_060028
http://togogenome.org/gene/9606:KLK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFQ5|||http://purl.uniprot.org/uniprot/Q5BQA0|||http://purl.uniprot.org/uniprot/Q9Y5K2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Kallikrein-4|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027937|||http://purl.uniprot.org/annotation/PRO_0000027938|||http://purl.uniprot.org/annotation/PRO_5014105534|||http://purl.uniprot.org/annotation/PRO_5014222190|||http://purl.uniprot.org/annotation/VAR_028364|||http://purl.uniprot.org/annotation/VAR_028365|||http://purl.uniprot.org/annotation/VAR_033009|||http://purl.uniprot.org/annotation/VSP_056629|||http://purl.uniprot.org/annotation/VSP_056630
http://togogenome.org/gene/9606:SPAAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVQ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Small regulatory polypeptide of amino acid response                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000439038|||http://purl.uniprot.org/annotation/VSP_058780
http://togogenome.org/gene/9606:PCDHA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003898|||http://purl.uniprot.org/annotation/VAR_021876|||http://purl.uniprot.org/annotation/VAR_048529|||http://purl.uniprot.org/annotation/VAR_059181|||http://purl.uniprot.org/annotation/VSP_000686|||http://purl.uniprot.org/annotation/VSP_000687
http://togogenome.org/gene/9606:PLA2G5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39877                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Decreases arachidonate release from cell membranes; when associated with E-112.|||Decreases arachidonate release from cell membranes; when associated with E-113.|||Impairs arachidonate release from cell membranes.|||In FRFB.|||Phospholipase A2 group V                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022761|||http://purl.uniprot.org/annotation/VAR_067343|||http://purl.uniprot.org/annotation/VAR_067344
http://togogenome.org/gene/9606:TANGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4A5|||http://purl.uniprot.org/uniprot/Q6ICL3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes mitochondrial localization.|||Disordered|||In MECRCN.|||In MECRCN; delayed ER-to-Golgi transport; altered mitochondrial morphology.|||In MECRCN; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||Transport and Golgi organization protein 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253891|||http://purl.uniprot.org/annotation/VAR_028742|||http://purl.uniprot.org/annotation/VAR_028743|||http://purl.uniprot.org/annotation/VAR_028744|||http://purl.uniprot.org/annotation/VAR_076912|||http://purl.uniprot.org/annotation/VAR_085626|||http://purl.uniprot.org/annotation/VAR_085627|||http://purl.uniprot.org/annotation/VAR_085628|||http://purl.uniprot.org/annotation/VAR_085629|||http://purl.uniprot.org/annotation/VAR_085630|||http://purl.uniprot.org/annotation/VAR_085631|||http://purl.uniprot.org/annotation/VAR_085632|||http://purl.uniprot.org/annotation/VAR_085633|||http://purl.uniprot.org/annotation/VAR_085634|||http://purl.uniprot.org/annotation/VAR_085635|||http://purl.uniprot.org/annotation/VAR_085636|||http://purl.uniprot.org/annotation/VAR_085637|||http://purl.uniprot.org/annotation/VAR_085638|||http://purl.uniprot.org/annotation/VAR_085639|||http://purl.uniprot.org/annotation/VSP_021137|||http://purl.uniprot.org/annotation/VSP_021138|||http://purl.uniprot.org/annotation/VSP_021139|||http://purl.uniprot.org/annotation/VSP_055604|||http://purl.uniprot.org/annotation/VSP_055605|||http://purl.uniprot.org/annotation/VSP_055606|||http://purl.uniprot.org/annotation/VSP_055607
http://togogenome.org/gene/9606:MUCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PEI6|||http://purl.uniprot.org/uniprot/Q3MIW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Mucin-like protein 3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318686|||http://purl.uniprot.org/annotation/PRO_5014571001|||http://purl.uniprot.org/annotation/VAR_038857|||http://purl.uniprot.org/annotation/VAR_038858|||http://purl.uniprot.org/annotation/VAR_038859|||http://purl.uniprot.org/annotation/VSP_031268|||http://purl.uniprot.org/annotation/VSP_031269
http://togogenome.org/gene/9606:RBBP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99708                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes BRCA1 interaction and ubiquitination. No activation of CHEK1 after DNA damage.|||Abolishes damage recruitment capability.|||Abrogates dissociation of BRCA1.|||Basic and acidic residues|||Can form homodimers but not homotetramers. Abolishes ability to promote homologous recombination and DNA resection. Defective binding to DNA. Defective in localizing to sites of DNA damage. Does not affect interaction with MRN complex components MRE11, NBN or RAD50.|||DNA endonuclease RBBP8|||Damage-recruitment motif|||Decreased CUL3/KLHL15-mediated proteasomal degradation.|||Decreased PIN1-binding. Impaired PIN1-binding, partially decreased CUL3/KLHL15-mediated proteasomal degradation, no effect on BRCA1-, MRE11-, nor on KLHL15-binding; when associated with A-276.|||Decreased interaction with KLHL15, decreased polyubiquitination and CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-end resection activity.|||Defective binding to DNA. No effect on CUL3/KLHL15-mediated proteasomal degradation. Does not affect tetramerization.|||Disordered|||Essential for binding to the MRN complex and for RPA focus formation on DNA damage|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired FZR1-binding and APC/C-mediated polyubiquitination. Increased stability. No effect on MRE11-binding, nor on CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-en resection activity.|||Impairs DNA resection.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-115; R-132 and R-133.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759 and R-760.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-760 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-759; R-760 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-572; R-640; R-759; R-760 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-404; R-578; R-640; R-759; R-760 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-132; R-133; R-572; R-578; R-640; R-759; R-760 and R-782.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115 and R-132.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-115 and R-133.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-62; R-78; R-132 and R-133.|||In K12R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-78; R-115; R-132; R-133; R-404; R-572; R-578; R-640; R-759; R-760 and R-782. In K5R; defects in ability to promoting DNA resection and homologous recombination; when associated with R-78; R-115; R-132 and R-133.|||In SCKL2.|||In isoform 2.|||In isoform 3.|||KLHL15-binding|||Mimics constitutive phosphorylation.|||No effect on FZR1-binding.|||No effect on KLHL15-binding, nor on CUL3/KLHL15-mediated proteasomal degradation.|||No effect on PIN1-binding. Impaired PIN1-binding, partially decreased CUL3/KLHL15-mediated proteasomal degradation, no effect on BRCA1-, MRE11-, nor on KLHL15-binding; when associated with A-315.|||No effect on RPA focus formation on DNA damage.|||PXDLS motif|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine; by CDK1|||Phosphothreonine; by CDK2|||Polar residues|||Reduces Zn(2+) content; when associated with A-89.|||Reduces Zn(2+) content; when associated with A-92.|||Required for interaction with LMO4, probably by making physical contact with LMO4|||Required for interaction with LMO4, probably by stabilizing the interaction through RPPB8 dimerization ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097179|||http://purl.uniprot.org/annotation/VAR_028308|||http://purl.uniprot.org/annotation/VAR_051308|||http://purl.uniprot.org/annotation/VAR_075824|||http://purl.uniprot.org/annotation/VSP_043220|||http://purl.uniprot.org/annotation/VSP_045247|||http://purl.uniprot.org/annotation/VSP_045248
http://togogenome.org/gene/9606:ATP5MG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75964                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  ATP synthase subunit g, mitochondrial|||N-acetylalanine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071691
http://togogenome.org/gene/9606:FAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 28|||Cadherin 29|||Cadherin 3|||Cadherin 30|||Cadherin 31|||Cadherin 32|||Cadherin 33|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Polar residues|||Protocadherin Fat 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324634|||http://purl.uniprot.org/annotation/VAR_039851|||http://purl.uniprot.org/annotation/VAR_039852|||http://purl.uniprot.org/annotation/VAR_039853|||http://purl.uniprot.org/annotation/VAR_039854|||http://purl.uniprot.org/annotation/VAR_039855|||http://purl.uniprot.org/annotation/VAR_039856|||http://purl.uniprot.org/annotation/VAR_039857|||http://purl.uniprot.org/annotation/VAR_039858|||http://purl.uniprot.org/annotation/VAR_039859|||http://purl.uniprot.org/annotation/VSP_059739|||http://purl.uniprot.org/annotation/VSP_059761
http://togogenome.org/gene/9606:SUCNR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXA5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes activation by succinate.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||No effect on receptor function.|||Succinate receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070134
http://togogenome.org/gene/9606:GH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1A4G6|||http://purl.uniprot.org/uniprot/B1A4G7|||http://purl.uniprot.org/uniprot/P01241                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Deamidated asparagine; by deterioration|||Deamidated glutamine; by deterioration|||Found in patients with isolated growth hormone deficiency.|||In IGHD1B.|||In IGHD1B; reduced ability to activate the JAK/STAT pathway.|||In IGHD1B; reduced secretion.|||In IGHD1B; suppresses secretion.|||In IGHD2.|||In KWKS; loss of activity.|||In KWKS; no effect on GHR signaling pathway; does not affect interaction with GHR; results in a stronger interaction with GHBP; does not affect subcellular location.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In short stature; idiopathic autosomal.|||In short stature; idiopathic autosomal; affects binding affinity of GH for GHR and the potency of GH to activate the JAK2/STAT5 signaling pathway.|||Phosphoserine|||Somatotropin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032988|||http://purl.uniprot.org/annotation/PRO_5014298185|||http://purl.uniprot.org/annotation/PRO_5014298186|||http://purl.uniprot.org/annotation/VAR_011917|||http://purl.uniprot.org/annotation/VAR_011918|||http://purl.uniprot.org/annotation/VAR_011919|||http://purl.uniprot.org/annotation/VAR_015801|||http://purl.uniprot.org/annotation/VAR_015802|||http://purl.uniprot.org/annotation/VAR_015803|||http://purl.uniprot.org/annotation/VAR_015804|||http://purl.uniprot.org/annotation/VAR_015805|||http://purl.uniprot.org/annotation/VAR_015806|||http://purl.uniprot.org/annotation/VAR_015807|||http://purl.uniprot.org/annotation/VAR_015808|||http://purl.uniprot.org/annotation/VAR_015809|||http://purl.uniprot.org/annotation/VAR_015810|||http://purl.uniprot.org/annotation/VAR_015811|||http://purl.uniprot.org/annotation/VAR_015812|||http://purl.uniprot.org/annotation/VAR_015813|||http://purl.uniprot.org/annotation/VAR_015814|||http://purl.uniprot.org/annotation/VAR_015815|||http://purl.uniprot.org/annotation/VAR_032702|||http://purl.uniprot.org/annotation/VAR_032703|||http://purl.uniprot.org/annotation/VSP_006200|||http://purl.uniprot.org/annotation/VSP_006201|||http://purl.uniprot.org/annotation/VSP_006202|||http://purl.uniprot.org/annotation/VSP_045642
http://togogenome.org/gene/9606:CAPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXY5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcyphosin-2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073540|||http://purl.uniprot.org/annotation/VAR_061085|||http://purl.uniprot.org/annotation/VSP_014408|||http://purl.uniprot.org/annotation/VSP_014409|||http://purl.uniprot.org/annotation/VSP_014410
http://togogenome.org/gene/9606:MAPK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13164                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Loss activation by MAP2K5.|||May not be required for kinase activity; required to stimulate MEF2C activity|||Mitogen-activated protein kinase 7|||N-acetylalanine|||Necessary for oligomerization|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Removed|||Required for binding to MAP2K5|||Required for cytoplasmic targeting|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186260|||http://purl.uniprot.org/annotation/VAR_042257|||http://purl.uniprot.org/annotation/VAR_046225|||http://purl.uniprot.org/annotation/VSP_035198|||http://purl.uniprot.org/annotation/VSP_035199|||http://purl.uniprot.org/annotation/VSP_035200
http://togogenome.org/gene/9606:SAXO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA69                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Stabilizer of axonemal microtubules 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297660|||http://purl.uniprot.org/annotation/VAR_034664|||http://purl.uniprot.org/annotation/VAR_034665|||http://purl.uniprot.org/annotation/VAR_034666|||http://purl.uniprot.org/annotation/VAR_034667|||http://purl.uniprot.org/annotation/VAR_034668
http://togogenome.org/gene/9606:GOLGA6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 6D|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395400
http://togogenome.org/gene/9606:BORCS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BLOC-1-related complex subunit 6|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286827
http://togogenome.org/gene/9606:S100PBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5M0|||http://purl.uniprot.org/uniprot/Q96BU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||S100P-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317051|||http://purl.uniprot.org/annotation/VSP_052661
http://togogenome.org/gene/9606:CACNA1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15878|||http://purl.uniprot.org/uniprot/Q59FG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Binding to the beta subunit|||Calcium ion selectivity and permeability|||Cytoplasmic|||Disordered|||EF-hand|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In DEE69.|||In DEE69; gain-of-function variant affecting channel activity; results in hyperpolarizing shift in half activation voltage.|||In DEE69; gain-of-function variant affecting channel activity; shifts the voltage dependence of activation toward more negative potentials and slows the fast inactivation time course.|||In DEE69; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Voltage-dependent R-type calcium channel subunit alpha-1E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053938|||http://purl.uniprot.org/annotation/VAR_031912|||http://purl.uniprot.org/annotation/VAR_046996|||http://purl.uniprot.org/annotation/VAR_081838|||http://purl.uniprot.org/annotation/VAR_081839|||http://purl.uniprot.org/annotation/VAR_081840|||http://purl.uniprot.org/annotation/VAR_081841|||http://purl.uniprot.org/annotation/VAR_081842|||http://purl.uniprot.org/annotation/VAR_081843|||http://purl.uniprot.org/annotation/VAR_081844|||http://purl.uniprot.org/annotation/VAR_081845|||http://purl.uniprot.org/annotation/VAR_081846|||http://purl.uniprot.org/annotation/VAR_081847|||http://purl.uniprot.org/annotation/VAR_081848|||http://purl.uniprot.org/annotation/VAR_081849|||http://purl.uniprot.org/annotation/VAR_081850|||http://purl.uniprot.org/annotation/VAR_081851|||http://purl.uniprot.org/annotation/VAR_081852|||http://purl.uniprot.org/annotation/VAR_081853|||http://purl.uniprot.org/annotation/VSP_000937|||http://purl.uniprot.org/annotation/VSP_024817
http://togogenome.org/gene/9606:SEC14L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLM6|||http://purl.uniprot.org/uniprot/Q59HE8|||http://purl.uniprot.org/uniprot/Q7Z3R7|||http://purl.uniprot.org/uniprot/Q92503                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CRAL-TRIO|||GOLD|||In isoform 2.|||In isoform 3.|||PRELI/MSF1|||Phosphoserine|||Phosphothreonine|||Required for interaction and inhibitory function toward RIGI|||SEC14-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210753|||http://purl.uniprot.org/annotation/VAR_057173|||http://purl.uniprot.org/annotation/VAR_060480|||http://purl.uniprot.org/annotation/VAR_060481|||http://purl.uniprot.org/annotation/VAR_060482|||http://purl.uniprot.org/annotation/VSP_040117|||http://purl.uniprot.org/annotation/VSP_040118
http://togogenome.org/gene/9606:PARL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JNP8|||http://purl.uniprot.org/uniprot/Q9H300                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Peptide|||Sequence Variant|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Abolishes the beta cleavage.|||Helical|||In isoform 2.|||Loss of PGAM5 cleavage.|||Loss of cleavage of CLPB, DIABLO, STARD7 and TTC19.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Nucleophile|||P-beta|||Phosphoserine|||Phosphothreonine|||Presenilin-associated rhomboid-like protein, mitochondrial|||Strongly reduces the beta cleavage; when associated with D-65 and D-69.|||Strongly reduces the beta cleavage; when associated with D-65 and D-70.|||Strongly reduces the beta cleavage; when associated with D-69 and D-70.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027386|||http://purl.uniprot.org/annotation/PRO_0000027387|||http://purl.uniprot.org/annotation/VAR_021578|||http://purl.uniprot.org/annotation/VAR_029801|||http://purl.uniprot.org/annotation/VSP_013310
http://togogenome.org/gene/9606:PUM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15397                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HA-8|||In allele HA-8P and allele HA-8PL.|||In allele HA-8PL.|||N6-acetyllysine|||Nuclear localization signal|||PUM-HD|||Pumilio 1|||Pumilio 10|||Pumilio 11|||Pumilio 2|||Pumilio 3|||Pumilio 4|||Pumilio 5|||Pumilio 6|||Pumilio 7|||Pumilio 8|||Pumilio 9|||Pumilio homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075929|||http://purl.uniprot.org/annotation/VAR_023772|||http://purl.uniprot.org/annotation/VAR_023773|||http://purl.uniprot.org/annotation/VAR_051613|||http://purl.uniprot.org/annotation/VAR_051614|||http://purl.uniprot.org/annotation/VAR_051615|||http://purl.uniprot.org/annotation/VAR_051616
http://togogenome.org/gene/9606:CSAG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5P2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chondrosarcoma-associated gene 2/3 protein|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079390|||http://purl.uniprot.org/annotation/VSP_004469|||http://purl.uniprot.org/annotation/VSP_034912|||http://purl.uniprot.org/annotation/VSP_034913
http://togogenome.org/gene/9606:CBLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSS7|||http://purl.uniprot.org/uniprot/B4DYP3|||http://purl.uniprot.org/uniprot/B7ZAG1|||http://purl.uniprot.org/uniprot/Q13191                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  4H|||Abolishes E3 activity but does not affect binding to substrates.|||Abolishes interaction with ubiquitinated proteins.|||Basic and acidic residues|||Cbl-PTB|||Decreases affinity for E2 ubiquitin-conjugating enzymes.|||Disordered|||E3 ubiquitin-protein ligase CBL-B|||EF-hand-like|||In isoform Truncated 1.|||In isoform Truncated 2.|||Inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated with F-665.|||Inhibits interaction with SYK. No effect on E3 activity.|||Interaction with SH3KBP1|||Interaction with VAV1|||Interferes with dimerization. Reduced E3 ubiquitin-protein ligase activity. Reduced levels of tyrosine phosphorylation.|||Linker|||Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation.|||No effect on interaction with CD2AP. Reduced interaction with SH3KBP1. Strongly reduced interaction with SH3KBP1; when associated with A-911.|||No effect on interaction with SH3KBP1. Reduced interaction with CD2AP. Strongly reduced interaction with CD2AP; when associated with A-911.|||No effect on interaction with ubiquitinated proteins.|||Phosphoserine|||Phosphoserine; by PKC/PRKCQ|||Phosphotyrosine|||Polar residues|||Pro residues|||RING-type|||Reduced interaction with CD2AP and with SH3KBP1. Strongly reduced interaction with CD2AP; when associated with A-907. Strongly reduced interaction with SH3KBP1; when associated with A-904.|||SH2-like|||Slightly inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated with F-709.|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055860|||http://purl.uniprot.org/annotation/VAR_025303|||http://purl.uniprot.org/annotation/VAR_039241|||http://purl.uniprot.org/annotation/VSP_005729|||http://purl.uniprot.org/annotation/VSP_005730|||http://purl.uniprot.org/annotation/VSP_005731
http://togogenome.org/gene/9606:DMAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW81                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Distal membrane-arm assembly complex protein 2|||In isoform 2 and isoform 5.|||In isoform 2, isoform 3 and isoform 6.|||In isoform 3 and isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318695|||http://purl.uniprot.org/annotation/VAR_057798|||http://purl.uniprot.org/annotation/VAR_057799|||http://purl.uniprot.org/annotation/VAR_057800|||http://purl.uniprot.org/annotation/VAR_057801|||http://purl.uniprot.org/annotation/VAR_060165|||http://purl.uniprot.org/annotation/VSP_031270|||http://purl.uniprot.org/annotation/VSP_031271|||http://purl.uniprot.org/annotation/VSP_043807
http://togogenome.org/gene/9606:ZAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYT6|||http://purl.uniprot.org/uniprot/Q9Y493                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  66 X heptapeptide repeats (approximate) (mucin-like domain)|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||MAM 1|||MAM 2|||MAM 3|||N-linked (GlcNAc...) asparagine|||Polar residues|||Requires 2 nucleotide substitutions.|||TIL 1|||TIL 2|||TIL 3|||TIL 4|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFD|||VWFD 1|||VWFD 2|||VWFD 3|||VWFD 4|||Zonadhesin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007783|||http://purl.uniprot.org/annotation/VAR_055785|||http://purl.uniprot.org/annotation/VAR_055786|||http://purl.uniprot.org/annotation/VAR_055787|||http://purl.uniprot.org/annotation/VAR_055788|||http://purl.uniprot.org/annotation/VAR_055789|||http://purl.uniprot.org/annotation/VAR_055790|||http://purl.uniprot.org/annotation/VAR_055791|||http://purl.uniprot.org/annotation/VAR_055792|||http://purl.uniprot.org/annotation/VAR_055793|||http://purl.uniprot.org/annotation/VAR_055794|||http://purl.uniprot.org/annotation/VAR_059278|||http://purl.uniprot.org/annotation/VAR_059279|||http://purl.uniprot.org/annotation/VAR_059280|||http://purl.uniprot.org/annotation/VAR_059281|||http://purl.uniprot.org/annotation/VAR_061162|||http://purl.uniprot.org/annotation/VAR_061163|||http://purl.uniprot.org/annotation/VAR_061164|||http://purl.uniprot.org/annotation/VAR_064584|||http://purl.uniprot.org/annotation/VAR_064585|||http://purl.uniprot.org/annotation/VAR_064586|||http://purl.uniprot.org/annotation/VAR_064587|||http://purl.uniprot.org/annotation/VAR_064588|||http://purl.uniprot.org/annotation/VAR_064589|||http://purl.uniprot.org/annotation/VSP_001420|||http://purl.uniprot.org/annotation/VSP_001421|||http://purl.uniprot.org/annotation/VSP_001422|||http://purl.uniprot.org/annotation/VSP_001423|||http://purl.uniprot.org/annotation/VSP_001424|||http://purl.uniprot.org/annotation/VSP_001425|||http://purl.uniprot.org/annotation/VSP_001426|||http://purl.uniprot.org/annotation/VSP_001427|||http://purl.uniprot.org/annotation/VSP_001428|||http://purl.uniprot.org/annotation/VSP_001429|||http://purl.uniprot.org/annotation/VSP_001430|||http://purl.uniprot.org/annotation/VSP_001431
http://togogenome.org/gene/9606:BLOC1S6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BST1|||http://purl.uniprot.org/uniprot/Q9UL45                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Biogenesis of lysosome-related organelles complex 1 subunit 6|||Disordered|||In HPS9; reduces NK cell cytolytic activity; increases LAMP1/CD107A and CD63 levels at the cell membrane.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058458|||http://purl.uniprot.org/annotation/VAR_081117|||http://purl.uniprot.org/annotation/VSP_009293|||http://purl.uniprot.org/annotation/VSP_009294
http://togogenome.org/gene/9606:SMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K984|||http://purl.uniprot.org/uniprot/B3KMB1|||http://purl.uniprot.org/uniprot/B7ZLZ7|||http://purl.uniprot.org/uniprot/O95347|||http://purl.uniprot.org/uniprot/Q05BV1|||http://purl.uniprot.org/uniprot/Q05D74|||http://purl.uniprot.org/uniprot/Q6IPS5|||http://purl.uniprot.org/uniprot/Q7Z2X1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||RecF/RecN/SMC N-terminal|||SMC hinge|||Structural maintenance of chromosomes protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118995|||http://purl.uniprot.org/annotation/VAR_047489|||http://purl.uniprot.org/annotation/VSP_007243|||http://purl.uniprot.org/annotation/VSP_007244
http://togogenome.org/gene/9606:POU4F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12837                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Absent from nuclear speckle; no change in transcriptional activity.|||Basic residues|||Disordered|||Homeobox|||In isoform 2.|||Nuclear speckle targeting signal|||POU domain, class 4, transcription factor 2|||POU-IV box|||POU-specific|||Polar residues|||Required for DNA-binding and transcriptional repression|||Required for transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100740|||http://purl.uniprot.org/annotation/VAR_059321|||http://purl.uniprot.org/annotation/VSP_058837
http://togogenome.org/gene/9606:NHLRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JS37                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL repeat-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317194|||http://purl.uniprot.org/annotation/VAR_051233|||http://purl.uniprot.org/annotation/VSP_042858
http://togogenome.org/gene/9606:ING2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RA15|||http://purl.uniprot.org/uniprot/Q9H160                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Histone H3K4me3 binding|||In isoform ING2b.|||Inhibitor of growth protein 2|||PBR|||PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212663|||http://purl.uniprot.org/annotation/VSP_047821
http://togogenome.org/gene/9606:DRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSC6|||http://purl.uniprot.org/uniprot/Q9H069                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dynein regulatory complex subunit 3|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227774|||http://purl.uniprot.org/annotation/VAR_025625|||http://purl.uniprot.org/annotation/VAR_051120|||http://purl.uniprot.org/annotation/VAR_051121|||http://purl.uniprot.org/annotation/VSP_017578|||http://purl.uniprot.org/annotation/VSP_017579
http://togogenome.org/gene/9606:ZKSCAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNP9|||http://purl.uniprot.org/uniprot/B3KRF7|||http://purl.uniprot.org/uniprot/E9PC66|||http://purl.uniprot.org/uniprot/P17029                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047753|||http://purl.uniprot.org/annotation/VAR_024839
http://togogenome.org/gene/9606:G6PC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQR9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glucose-6-phosphatase 2|||Helical|||In isoform 2.|||In isoform 3.|||Loss of N-glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on N-glycosylation.|||Nucleophile|||Prevents secretion from ER|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334509|||http://purl.uniprot.org/annotation/VAR_043372|||http://purl.uniprot.org/annotation/VAR_043373|||http://purl.uniprot.org/annotation/VAR_043374|||http://purl.uniprot.org/annotation/VAR_043375|||http://purl.uniprot.org/annotation/VAR_043376|||http://purl.uniprot.org/annotation/VAR_043377|||http://purl.uniprot.org/annotation/VSP_033648|||http://purl.uniprot.org/annotation/VSP_033649|||http://purl.uniprot.org/annotation/VSP_046180|||http://purl.uniprot.org/annotation/VSP_046181
http://togogenome.org/gene/9606:F2RL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55085                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes signaling through accumulation of intracellular calcium and phosphoinositide; no effect in signaling through MAPK.|||Cleavage; by trypsin|||Cytoplasmic|||Decreases cell surface expression; when associate with A-222.|||Decreases cell surface expression; when associated with A-30. Loss of sensitivity towards all tested proteases.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increase of sensitivity towards tryptase.|||Loss of palmitoylation; increases surface expression and internalization following trypsin activation, decreases sensitivity and intracellular calcium signaling, increases ERK activation through G(i) subunit alpha.|||N-linked (GlcNAc...) asparagine|||No defect in ligand-mediated receptor activation.|||Proteinase-activated receptor 2|||Proteinase-activated receptor 2, alternate cleaved 1|||Proteinase-activated receptor 2, alternate cleaved 2|||Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-363.|||Reduces receptor desensitization and internalization, activates ERK1/2; when associated with A-366.|||Removed for receptor activation|||S-palmitoyl cysteine|||Severe reduction in ligand-mediated receptor activation.|||Slight reduction in ligand-mediated receptor activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012750|||http://purl.uniprot.org/annotation/PRO_0000012751|||http://purl.uniprot.org/annotation/PRO_0000412954|||http://purl.uniprot.org/annotation/PRO_0000412956|||http://purl.uniprot.org/annotation/VAR_012846|||http://purl.uniprot.org/annotation/VAR_012847|||http://purl.uniprot.org/annotation/VAR_012848|||http://purl.uniprot.org/annotation/VAR_049435
http://togogenome.org/gene/9606:CCNQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1B3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-Q|||Disordered|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297567|||http://purl.uniprot.org/annotation/VAR_034642|||http://purl.uniprot.org/annotation/VSP_034527
http://togogenome.org/gene/9606:MICA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCL3|||http://purl.uniprot.org/uniprot/A0A0G2JJ55|||http://purl.uniprot.org/uniprot/Q96QC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Ig-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5014589245
http://togogenome.org/gene/9606:RAB41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JT25                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Motif|||Splice Variant                                                                                  ^@                                                                                  Effector region|||In isoform 2.|||Ras-related protein Rab-41|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244618|||http://purl.uniprot.org/annotation/VSP_037051
http://togogenome.org/gene/9606:TUBE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJT0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict                                                                                  ^@                                                                                  Tubulin epsilon chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048486
http://togogenome.org/gene/9606:ERGIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TD3|||http://purl.uniprot.org/uniprot/Q96RQ1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endoplasmic reticulum vesicle transporter C-terminal|||Endoplasmic reticulum-Golgi intermediate compartment protein 2|||Helical|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239382
http://togogenome.org/gene/9606:TNFRSF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8T4|||http://purl.uniprot.org/uniprot/P28908                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||TNFR-Cys 5|||TNFR-Cys 6|||Tumor necrosis factor receptor superfamily member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034573|||http://purl.uniprot.org/annotation/VAR_018753|||http://purl.uniprot.org/annotation/VAR_018754|||http://purl.uniprot.org/annotation/VAR_054213|||http://purl.uniprot.org/annotation/VAR_055257|||http://purl.uniprot.org/annotation/VAR_055258|||http://purl.uniprot.org/annotation/VAR_055259|||http://purl.uniprot.org/annotation/VSP_018900|||http://purl.uniprot.org/annotation/VSP_055032|||http://purl.uniprot.org/annotation/VSP_055033
http://togogenome.org/gene/9606:LETM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1M9|||http://purl.uniprot.org/uniprot/E9PMA4|||http://purl.uniprot.org/uniprot/Q2VYF4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||LETM1 domain-containing protein LETM2, mitochondrial|||LETM2 N-terminal|||Letm1 RBD|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307137|||http://purl.uniprot.org/annotation/VSP_028588|||http://purl.uniprot.org/annotation/VSP_028589|||http://purl.uniprot.org/annotation/VSP_028590|||http://purl.uniprot.org/annotation/VSP_028591
http://togogenome.org/gene/9606:BPIFC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFQ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPI fold-containing family C protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017166|||http://purl.uniprot.org/annotation/VAR_024516|||http://purl.uniprot.org/annotation/VAR_024517|||http://purl.uniprot.org/annotation/VAR_033631|||http://purl.uniprot.org/annotation/VAR_049741|||http://purl.uniprot.org/annotation/VSP_056033|||http://purl.uniprot.org/annotation/VSP_056034
http://togogenome.org/gene/9606:CD200R1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Q8B3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell surface glycoprotein CD200 receptor 2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346451|||http://purl.uniprot.org/annotation/VAR_045897|||http://purl.uniprot.org/annotation/VSP_035002
http://togogenome.org/gene/9606:TFAP2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92754                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||H-S-H (helix-span-helix), dimerization|||In isoform 2.|||Loss of interaction with WWOX; when associated with A-59.|||Loss of interaction with WWOX; when associated with A-64.|||PPxY motif|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Transcription factor AP-2 gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184803|||http://purl.uniprot.org/annotation/VSP_056501
http://togogenome.org/gene/9606:UBAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6G6AA68|||http://purl.uniprot.org/uniprot/Q9NZ09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolished interaction with PTPN23.|||Abolishes association with the ESCRT-I complex.|||Disordered|||Does not affect interaction with PTPN23.|||In SPG80.|||In SPG80; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with ESCRT-I|||Interaction with PTPN23|||Phosphoserine|||Polar residues|||Strongly reduced interaction with ubiquitinated proteins.|||UBA|||UBA 1|||UBA 2|||UMA|||Ubiquitin-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211017|||http://purl.uniprot.org/annotation/VAR_034577|||http://purl.uniprot.org/annotation/VAR_082199|||http://purl.uniprot.org/annotation/VAR_082200|||http://purl.uniprot.org/annotation/VSP_013650|||http://purl.uniprot.org/annotation/VSP_046866|||http://purl.uniprot.org/annotation/VSP_046867
http://togogenome.org/gene/9606:COX20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5RI15                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX20, mitochondrial|||Helical|||In MC4DN11; reduced protein expression; defective mitochondrial respiratory chain complex IV assembly; decreased interaction with MT-CO2/COX2; increased interaction with TMEM177.|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186815|||http://purl.uniprot.org/annotation/VAR_080123|||http://purl.uniprot.org/annotation/VAR_080124|||http://purl.uniprot.org/annotation/VSP_014855
http://togogenome.org/gene/9606:TM4SF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30408                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with SDCBP2. Loss of colocalization with SDCBP2 at the apical region of the cell.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 4 L6 family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219295
http://togogenome.org/gene/9606:GPR142                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QSD0|||http://purl.uniprot.org/uniprot/Q7Z601                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues|||Probable G-protein coupled receptor 142                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069620|||http://purl.uniprot.org/annotation/VAR_061219
http://togogenome.org/gene/9606:COMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJG8|||http://purl.uniprot.org/uniprot/P21964                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catechol O-methyltransferase|||Correlated with reduced enzyme activity; associated with increased risk for schizophrenia.|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In allele COMT*2; associated with low enzyme activity and thermolability; may increase the tendency to develop high blood pressure and abdominal obesity.|||In isoform Soluble.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020971|||http://purl.uniprot.org/annotation/VAR_005139|||http://purl.uniprot.org/annotation/VAR_013925|||http://purl.uniprot.org/annotation/VAR_013926|||http://purl.uniprot.org/annotation/VAR_020274|||http://purl.uniprot.org/annotation/VAR_020275|||http://purl.uniprot.org/annotation/VSP_018778
http://togogenome.org/gene/9606:ANGPT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y264                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Angiopoietin-4|||Fibrinogen C-terminal|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009116|||http://purl.uniprot.org/annotation/VAR_049070|||http://purl.uniprot.org/annotation/VSP_055091
http://togogenome.org/gene/9606:INPP4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EQN9|||http://purl.uniprot.org/uniprot/O15327                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolished phosphotyrosine phosphatase activity.|||C2|||Disordered|||Does not alter phosphotyrosine phosphatase activity. Abolished lipid phosphatase activity.|||Helical|||In isoform 2.|||Increased phosphotyrosine phosphatase activity. Does not alter lipid phosphatase activity for the substrate phosphatidylinositol(3,4)P2, but reduced hydrolysis of inositol(1,3,4)P3 by about 70%.|||Inositol polyphosphate 4-phosphatase type II|||Polar residues|||Significantly reduces phosphotyrosine phosphatase activity. Not able to dephosphorylate phosphatidylinositol(3,4)P2 but retains approximately 35% of activity towards Inosotol(1,3,4)P3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190235|||http://purl.uniprot.org/annotation/VAR_023324|||http://purl.uniprot.org/annotation/VSP_047696|||http://purl.uniprot.org/annotation/VSP_047697
http://togogenome.org/gene/9606:MGLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFN3|||http://purl.uniprot.org/uniprot/B2ZGL7|||http://purl.uniprot.org/uniprot/Q99685                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Charge relay system|||Disordered|||Does not affect ability to hydrolyze 1- or 2-monoacylglycerol.|||In isoform 2.|||Monoglyceride lipase|||Nucleophile|||Phosphothreonine|||Reduced 1-monoacylglycerol lipase activity.|||Serine aminopeptidase S33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191265|||http://purl.uniprot.org/annotation/VSP_045138|||http://purl.uniprot.org/annotation/VSP_045139
http://togogenome.org/gene/9606:GSTCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8J7|||http://purl.uniprot.org/uniprot/Q8NEC7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GST C-terminal|||Glutathione S-transferase C-terminal domain-containing protein|||In isoform 2.|||Methyltransferase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316952|||http://purl.uniprot.org/annotation/VSP_045228
http://togogenome.org/gene/9606:RHOBTB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94844                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  BTB 1|||BTB 2|||Disordered|||Rho-like|||Rho-related BTB domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198960
http://togogenome.org/gene/9606:SPRR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35321                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 12 AA approximate repeats|||3|||4|||5|||6|||6 X 8 AA approximate tandem repeats|||Cornifin-A|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149995|||http://purl.uniprot.org/annotation/VAR_021097|||http://purl.uniprot.org/annotation/VAR_021098
http://togogenome.org/gene/9606:CNOT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75175                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 3|||Disordered|||In IDDSADF.|||In IDDSADF; unknown pathological significance.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Repressor domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198333|||http://purl.uniprot.org/annotation/VAR_083405|||http://purl.uniprot.org/annotation/VAR_083406|||http://purl.uniprot.org/annotation/VAR_083407|||http://purl.uniprot.org/annotation/VAR_083408|||http://purl.uniprot.org/annotation/VAR_083409|||http://purl.uniprot.org/annotation/VAR_083410|||http://purl.uniprot.org/annotation/VAR_083411|||http://purl.uniprot.org/annotation/VAR_083412|||http://purl.uniprot.org/annotation/VAR_083413
http://togogenome.org/gene/9606:SHISA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NL88                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Protein shisa-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344472
http://togogenome.org/gene/9606:ZNF565                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9K5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 565                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047655|||http://purl.uniprot.org/annotation/VAR_023938|||http://purl.uniprot.org/annotation/VSP_055965
http://togogenome.org/gene/9606:SLC41A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RMP2|||http://purl.uniprot.org/uniprot/Q8IVJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In NPHPL2; results in exon 6 skipping; results in loss of magnesium ion transmembrane transporter activity; does not affect localization to basolateral cell membrane.|||Increased magnesium ion transmembrane transporter activity; no effect on plasma membrane localization.|||Polar residues|||SLC41A/MgtE integral membrane|||Solute carrier family 41 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295111|||http://purl.uniprot.org/annotation/VAR_086146|||http://purl.uniprot.org/annotation/VAR_086248
http://togogenome.org/gene/9606:COLGALT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IT37|||http://purl.uniprot.org/uniprot/B3KT92|||http://purl.uniprot.org/uniprot/B4DF84|||http://purl.uniprot.org/uniprot/Q8IYK4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Procollagen galactosyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309541|||http://purl.uniprot.org/annotation/PRO_5002800811|||http://purl.uniprot.org/annotation/PRO_5017182994|||http://purl.uniprot.org/annotation/VAR_036978
http://togogenome.org/gene/9606:DYNC1LI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43237|||http://purl.uniprot.org/uniprot/Q63HJ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytoplasmic dynein 1 light intermediate chain 2|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114670|||http://purl.uniprot.org/annotation/VSP_054663
http://togogenome.org/gene/9606:PC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11498                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-grasp|||Biotin carboxylation|||Biotinyl-binding|||In PC deficiency.|||In PC deficiency; mild.|||In PC deficiency; mild; strongly reduced pyruvate carboxylase activity.|||In isoform 2.|||Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-biotinyllysine|||N6-carboxylysine|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphothreonine|||Pyruvate carboxylase, mitochondrial|||Pyruvate carboxyltransferase|||via carbamate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002840|||http://purl.uniprot.org/annotation/VAR_008095|||http://purl.uniprot.org/annotation/VAR_008096|||http://purl.uniprot.org/annotation/VAR_015199|||http://purl.uniprot.org/annotation/VAR_015200|||http://purl.uniprot.org/annotation/VAR_048416|||http://purl.uniprot.org/annotation/VAR_058957|||http://purl.uniprot.org/annotation/VAR_058958|||http://purl.uniprot.org/annotation/VAR_058959|||http://purl.uniprot.org/annotation/VAR_058960|||http://purl.uniprot.org/annotation/VAR_058961|||http://purl.uniprot.org/annotation/VAR_058962|||http://purl.uniprot.org/annotation/VSP_056358|||http://purl.uniprot.org/annotation/VSP_056359
http://togogenome.org/gene/9606:LRRC72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJI9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000346430
http://togogenome.org/gene/9606:GPR151                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 151|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069632|||http://purl.uniprot.org/annotation/VAR_049404|||http://purl.uniprot.org/annotation/VAR_049405|||http://purl.uniprot.org/annotation/VAR_049406
http://togogenome.org/gene/9606:PCNX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKB5|||http://purl.uniprot.org/uniprot/B3KNZ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Pecanex C-terminal|||Pecanex-like protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333965|||http://purl.uniprot.org/annotation/VAR_043341|||http://purl.uniprot.org/annotation/VAR_050479|||http://purl.uniprot.org/annotation/VAR_061498|||http://purl.uniprot.org/annotation/VAR_061499|||http://purl.uniprot.org/annotation/VSP_033605|||http://purl.uniprot.org/annotation/VSP_033606|||http://purl.uniprot.org/annotation/VSP_033607|||http://purl.uniprot.org/annotation/VSP_033608|||http://purl.uniprot.org/annotation/VSP_033609|||http://purl.uniprot.org/annotation/VSP_033610|||http://purl.uniprot.org/annotation/VSP_033611|||http://purl.uniprot.org/annotation/VSP_035048|||http://purl.uniprot.org/annotation/VSP_035049|||http://purl.uniprot.org/annotation/VSP_035050
http://togogenome.org/gene/9606:EIF3J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75822                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit J|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Promotes stable association with the 40S ribosome|||Removed|||Sufficient for interaction with EIF3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123506|||http://purl.uniprot.org/annotation/VAR_034007|||http://purl.uniprot.org/annotation/VSP_054593|||http://purl.uniprot.org/annotation/VSP_054776
http://togogenome.org/gene/9606:IFFO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TF58                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||IF rod|||Intermediate filament family orphan 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326185
http://togogenome.org/gene/9606:B3GNT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9Q8|||http://purl.uniprot.org/uniprot/Q6ZMB0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289218|||http://purl.uniprot.org/annotation/VSP_025963|||http://purl.uniprot.org/annotation/VSP_025964|||http://purl.uniprot.org/annotation/VSP_047091
http://togogenome.org/gene/9606:SASH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75995                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In IMD102; decreased protein abundance; patient T cells show decreased proliferation and cell cycle progression and increased apoptosis; functional signaling defects of the T cell receptor.|||In IMD102; loss of protein expression.|||In IMD102; loss of protein expression; patient T cells show decreased proliferation and cell cycle progression and increased apoptosis; functional signaling defects of the T cell receptor.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SAM|||SAM and SH3 domain-containing protein 3|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071962|||http://purl.uniprot.org/annotation/VAR_087463|||http://purl.uniprot.org/annotation/VAR_087464|||http://purl.uniprot.org/annotation/VAR_087465|||http://purl.uniprot.org/annotation/VAR_087466
http://togogenome.org/gene/9606:PPIL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0I0|||http://purl.uniprot.org/uniprot/Q13356                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Gain of a peptidyl-prolyl cis-trans isomerase activity; enables interaction with cyclosporin A.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||No peptidyl-prolyl cis-trans isomerase activity; enables interaction with cyclosporin A.|||PPIase cyclophilin-type|||Phosphoserine|||Polar residues|||RING-type E3 ubiquitin-protein ligase PPIL2|||U-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064171|||http://purl.uniprot.org/annotation/VSP_005182
http://togogenome.org/gene/9606:MS4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2E9|||http://purl.uniprot.org/uniprot/Q01362                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||High affinity immunoglobulin epsilon receptor subunit beta|||Phosphoserine|||Phosphotyrosine|||Risk factor for atopic dermatitis and asthma.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158629|||http://purl.uniprot.org/annotation/VAR_003965|||http://purl.uniprot.org/annotation/VAR_053515|||http://purl.uniprot.org/annotation/VAR_053516
http://togogenome.org/gene/9606:ZNF614                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N883                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; atypical|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 614                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234598|||http://purl.uniprot.org/annotation/VAR_052878|||http://purl.uniprot.org/annotation/VAR_052879|||http://purl.uniprot.org/annotation/VAR_052880|||http://purl.uniprot.org/annotation/VAR_061959|||http://purl.uniprot.org/annotation/VSP_056549|||http://purl.uniprot.org/annotation/VSP_056550
http://togogenome.org/gene/9606:CCNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96020                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||G1/S-specific cyclin-E2|||In isoform Short.|||Increase of steady state level.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080461|||http://purl.uniprot.org/annotation/VAR_021347|||http://purl.uniprot.org/annotation/VSP_001256
http://togogenome.org/gene/9606:C16orf46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P387                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Uncharacterized protein C16orf46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279429|||http://purl.uniprot.org/annotation/VAR_030893|||http://purl.uniprot.org/annotation/VAR_030894|||http://purl.uniprot.org/annotation/VAR_030895|||http://purl.uniprot.org/annotation/VAR_030896|||http://purl.uniprot.org/annotation/VAR_030897|||http://purl.uniprot.org/annotation/VSP_023435
http://togogenome.org/gene/9606:ZNF862                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60290                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  In isoform 2.|||KRAB 1|||KRAB 2|||TTF-type 1|||TTF-type 2|||Zinc finger protein 862                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320644|||http://purl.uniprot.org/annotation/VAR_039248|||http://purl.uniprot.org/annotation/VSP_031702|||http://purl.uniprot.org/annotation/VSP_031703
http://togogenome.org/gene/9606:CEP250                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXD2|||http://purl.uniprot.org/uniprot/Q9BV73                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosome-associated protein CEP250|||Disordered|||Found in autosomal recessive retinitis pigmentosa; unknown pathological significance; results in increased ciliary length.|||In CRDHL2.|||In CRDHL2; also found in a family with non-syndromic retinitis pigmentosa.|||In CRDHL2; the retinal involvement is more severe in double homozygotes also carrying a PCARE truncating variant.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by NEK2|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089487|||http://purl.uniprot.org/annotation/VAR_015649|||http://purl.uniprot.org/annotation/VAR_021858|||http://purl.uniprot.org/annotation/VAR_050898|||http://purl.uniprot.org/annotation/VAR_081745|||http://purl.uniprot.org/annotation/VAR_081746|||http://purl.uniprot.org/annotation/VAR_081747|||http://purl.uniprot.org/annotation/VAR_081748|||http://purl.uniprot.org/annotation/VAR_081749|||http://purl.uniprot.org/annotation/VAR_081750|||http://purl.uniprot.org/annotation/VSP_007372
http://togogenome.org/gene/9606:MSX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28360                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Homeobox|||Homeobox protein MSX-1|||In ECTD3.|||In OFC5; bilateral cleft palate.|||In OFC5; cleft palate only.|||In OFC5; unilateral cleft palate.|||In STHAG1.|||Required for interaction with EHMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049086|||http://purl.uniprot.org/annotation/VAR_003754|||http://purl.uniprot.org/annotation/VAR_015712|||http://purl.uniprot.org/annotation/VAR_018391|||http://purl.uniprot.org/annotation/VAR_018392|||http://purl.uniprot.org/annotation/VAR_018393|||http://purl.uniprot.org/annotation/VAR_018394|||http://purl.uniprot.org/annotation/VAR_018395|||http://purl.uniprot.org/annotation/VAR_088427
http://togogenome.org/gene/9606:TRIM43B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCK2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 43B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318857
http://togogenome.org/gene/9606:UTP14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVJ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||U3 small nucleolar RNA-associated protein 14 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065733|||http://purl.uniprot.org/annotation/VAR_022811|||http://purl.uniprot.org/annotation/VAR_069181|||http://purl.uniprot.org/annotation/VAR_078693|||http://purl.uniprot.org/annotation/VSP_014475|||http://purl.uniprot.org/annotation/VSP_014476|||http://purl.uniprot.org/annotation/VSP_046389
http://togogenome.org/gene/9606:FAM50B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y247                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Protein FAM50B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068286
http://togogenome.org/gene/9606:EIF2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41214                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 2D|||In isoform 2.|||N-acetylmethionine|||PUA|||Phosphoserine|||Polar residues|||SUI1|||SWIB/MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130611|||http://purl.uniprot.org/annotation/VAR_052507|||http://purl.uniprot.org/annotation/VSP_006300
http://togogenome.org/gene/9606:CATSPER4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTX7                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated protein 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Pore-forming|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295681|||http://purl.uniprot.org/annotation/VAR_033310|||http://purl.uniprot.org/annotation/VAR_033311|||http://purl.uniprot.org/annotation/VAR_033312|||http://purl.uniprot.org/annotation/VAR_033313|||http://purl.uniprot.org/annotation/VSP_026979|||http://purl.uniprot.org/annotation/VSP_026980
http://togogenome.org/gene/9606:GJD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IE23|||http://purl.uniprot.org/uniprot/Q9UKL4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction delta-2 protein|||Gap junction protein cysteine-rich|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057835
http://togogenome.org/gene/9606:NRXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR89|||http://purl.uniprot.org/uniprot/Q9HDB5|||http://purl.uniprot.org/uniprot/Q9Y4C0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Helical|||In isoform 2b.|||In isoform 3a.|||In isoform 3b and isoform 4b.|||In isoform 3b.|||In isoform 4a.|||In isoform 4b.|||Laminin G|||Laminin G-like|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin G-like 6|||N-linked (GlcNAc...) asparagine|||Neurexin-3|||Neurexin-3-beta|||Neurexin-3-beta, C-terminal fragment|||Neurexin-3-beta, soluble form|||O-linked (Xyl...) (heparan sulfate) serine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019499|||http://purl.uniprot.org/annotation/PRO_0000019502|||http://purl.uniprot.org/annotation/PRO_0000412543|||http://purl.uniprot.org/annotation/PRO_0000412544|||http://purl.uniprot.org/annotation/VSP_035644|||http://purl.uniprot.org/annotation/VSP_035646|||http://purl.uniprot.org/annotation/VSP_035647|||http://purl.uniprot.org/annotation/VSP_036463|||http://purl.uniprot.org/annotation/VSP_036464|||http://purl.uniprot.org/annotation/VSP_036465|||http://purl.uniprot.org/annotation/VSP_036466|||http://purl.uniprot.org/annotation/VSP_040988|||http://purl.uniprot.org/annotation/VSP_041699|||http://purl.uniprot.org/annotation/VSP_041700|||http://purl.uniprot.org/annotation/VSP_041701|||http://purl.uniprot.org/annotation/VSP_041702|||http://purl.uniprot.org/annotation/VSP_041703|||http://purl.uniprot.org/annotation/VSP_041704
http://togogenome.org/gene/9606:WDR75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 75                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051430
http://togogenome.org/gene/9606:KCNA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22459                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In MCIDDS; unknown pathological significance; mildly decreased function in potassium transmembrane transport.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 4|||S4-S5 linker|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053981|||http://purl.uniprot.org/annotation/VAR_081837
http://togogenome.org/gene/9606:MAST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2H9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||Disordered|||In MCCCHCM.|||In MCCCHCM; expression of this variant in transgenic mice results in thicker corpus callosum, hypoplastic cortex and hypoplastic cerebellum.|||In MCCCHCM; unknown pathological significance.|||In a metastatic melanoma sample; somatic mutation.|||In a patient with neurodevelopmental abnormalities; de novo variant; unknown pathological significance.|||In an ovarian serous carcinoma sample; somatic mutation.|||Microtubule-associated serine/threonine-protein kinase 1|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086309|||http://purl.uniprot.org/annotation/VAR_040768|||http://purl.uniprot.org/annotation/VAR_040769|||http://purl.uniprot.org/annotation/VAR_040770|||http://purl.uniprot.org/annotation/VAR_051644|||http://purl.uniprot.org/annotation/VAR_081872|||http://purl.uniprot.org/annotation/VAR_081873|||http://purl.uniprot.org/annotation/VAR_081874|||http://purl.uniprot.org/annotation/VAR_081875|||http://purl.uniprot.org/annotation/VAR_081876|||http://purl.uniprot.org/annotation/VAR_081877|||http://purl.uniprot.org/annotation/VAR_081878|||http://purl.uniprot.org/annotation/VAR_081879
http://togogenome.org/gene/9606:LRATD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KN4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation.|||In isoform 2.|||LRAT|||No effect on phosphorylation.|||Phosphoserine|||Protein LRATD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234425|||http://purl.uniprot.org/annotation/VSP_018314
http://togogenome.org/gene/9606:TRIM36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PBG3|||http://purl.uniprot.org/uniprot/Q4R1Q4|||http://purl.uniprot.org/uniprot/Q9NQ86                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B box-type 1|||B box-type 2|||B30.2/SPRY|||COS|||E3 ubiquitin-protein ligase TRIM36|||Fibronectin type-III|||In ANPH1; decreases protein stability; leads to microtubules disruption; exhibits multipolar spindles; exhibits abnormal cytokinesis.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056252|||http://purl.uniprot.org/annotation/VAR_020490|||http://purl.uniprot.org/annotation/VAR_023197|||http://purl.uniprot.org/annotation/VAR_023198|||http://purl.uniprot.org/annotation/VAR_057221|||http://purl.uniprot.org/annotation/VAR_079581|||http://purl.uniprot.org/annotation/VSP_043511|||http://purl.uniprot.org/annotation/VSP_043512|||http://purl.uniprot.org/annotation/VSP_045791|||http://purl.uniprot.org/annotation/VSP_045792|||http://purl.uniprot.org/annotation/VSP_053818
http://togogenome.org/gene/9606:ANKRD34C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C6C1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 34C|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319104|||http://purl.uniprot.org/annotation/VAR_038953|||http://purl.uniprot.org/annotation/VAR_038954|||http://purl.uniprot.org/annotation/VAR_038955
http://togogenome.org/gene/9606:LYPLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJC9|||http://purl.uniprot.org/uniprot/O95372                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to mediate depalmitoylation of ZDHHC6.|||Abolishes palmitoylation.|||Acyl-protein thioesterase 2|||Charge relay system|||Phospholipase/carboxylesterase/thioesterase|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102271
http://togogenome.org/gene/9606:HSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03933|||http://purl.uniprot.org/uniprot/Q9BS48                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fails to translocate to nucleus.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HSF-type DNA-binding|||Heat shock factor protein 2|||Hydrophobic repeat HR-A/B|||Hydrophobic repeat HR-C|||In isoform 2.|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124569|||http://purl.uniprot.org/annotation/VSP_041128
http://togogenome.org/gene/9606:SCAND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8W9|||http://purl.uniprot.org/uniprot/A0A2R8Y5N3|||http://purl.uniprot.org/uniprot/Q6R2W3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Integrase catalytic|||SCAN box|||SCAN domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245846|||http://purl.uniprot.org/annotation/VAR_027012|||http://purl.uniprot.org/annotation/VAR_061703
http://togogenome.org/gene/9606:P2RX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56373                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161551|||http://purl.uniprot.org/annotation/VAR_034674
http://togogenome.org/gene/9606:GCNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95395                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288545
http://togogenome.org/gene/9606:MRPL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7H8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with intellectual disability and ataxia; unknown pathological significance.|||In isoform 2.|||Large ribosomal subunit protein uL10m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273075|||http://purl.uniprot.org/annotation/VAR_030078|||http://purl.uniprot.org/annotation/VAR_083398|||http://purl.uniprot.org/annotation/VSP_044481
http://togogenome.org/gene/9606:PTGER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00325|||http://purl.uniprot.org/uniprot/P43115                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 12.|||In isoform EP3-III.|||In isoform EP3-IV.|||In isoform EP3-V.|||In isoform EP3B.|||In isoform EP3C.|||In isoform EP3D.|||In isoform EP3E.|||In isoform EP3E2.|||In isoform EP3F.|||In isoform EP3G.|||N-linked (GlcNAc...) asparagine|||Prostaglandin E2 receptor EP3 subtype                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070058|||http://purl.uniprot.org/annotation/VAR_014694|||http://purl.uniprot.org/annotation/VAR_014695|||http://purl.uniprot.org/annotation/VAR_029218|||http://purl.uniprot.org/annotation/VAR_049436|||http://purl.uniprot.org/annotation/VSP_001935|||http://purl.uniprot.org/annotation/VSP_001936|||http://purl.uniprot.org/annotation/VSP_001937|||http://purl.uniprot.org/annotation/VSP_001938|||http://purl.uniprot.org/annotation/VSP_001939|||http://purl.uniprot.org/annotation/VSP_013271|||http://purl.uniprot.org/annotation/VSP_053774|||http://purl.uniprot.org/annotation/VSP_053775|||http://purl.uniprot.org/annotation/VSP_053776|||http://purl.uniprot.org/annotation/VSP_053777|||http://purl.uniprot.org/annotation/VSP_058943
http://togogenome.org/gene/9606:ACTL6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94805                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Actin-like protein 6B|||Essential for mediating its function in dendritic development; may contribute to neuronal-specific targeting|||In DEE76.|||In DEE76; unknown pathological significance.|||In IDDSSAD; probable gain-of-function mutation.|||In IDDSSAD; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089135|||http://purl.uniprot.org/annotation/VAR_082123|||http://purl.uniprot.org/annotation/VAR_082124|||http://purl.uniprot.org/annotation/VAR_082125|||http://purl.uniprot.org/annotation/VAR_082126|||http://purl.uniprot.org/annotation/VAR_082127|||http://purl.uniprot.org/annotation/VAR_082128|||http://purl.uniprot.org/annotation/VAR_082129|||http://purl.uniprot.org/annotation/VAR_082130|||http://purl.uniprot.org/annotation/VAR_082131|||http://purl.uniprot.org/annotation/VAR_082132|||http://purl.uniprot.org/annotation/VAR_082133|||http://purl.uniprot.org/annotation/VAR_082134|||http://purl.uniprot.org/annotation/VAR_082135|||http://purl.uniprot.org/annotation/VAR_082136|||http://purl.uniprot.org/annotation/VAR_082137
http://togogenome.org/gene/9606:ANXA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09525                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A4|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067482|||http://purl.uniprot.org/annotation/VAR_055500|||http://purl.uniprot.org/annotation/VSP_056396|||http://purl.uniprot.org/annotation/VSP_061413
http://togogenome.org/gene/9606:SIGLEC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abrogates glycan-binding.|||Abrogates interaction with HCST and TYROBP.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sialic acid-binding Ig-like lectin 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294369|||http://purl.uniprot.org/annotation/VAR_033174|||http://purl.uniprot.org/annotation/VSP_056817|||http://purl.uniprot.org/annotation/VSP_056818
http://togogenome.org/gene/9606:PRRC2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSZ5|||http://purl.uniprot.org/uniprot/Q9BU62                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAT2 N-terminal|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein PRRC2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274481|||http://purl.uniprot.org/annotation/VAR_030289|||http://purl.uniprot.org/annotation/VAR_030290|||http://purl.uniprot.org/annotation/VAR_057735|||http://purl.uniprot.org/annotation/VSP_022760|||http://purl.uniprot.org/annotation/VSP_022761|||http://purl.uniprot.org/annotation/VSP_022762|||http://purl.uniprot.org/annotation/VSP_039905
http://togogenome.org/gene/9606:POLR2J3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2F8|||http://purl.uniprot.org/uniprot/Q9GZM3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB11-b1|||DNA-directed RNA polymerase RBP11-like dimerisation|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316946|||http://purl.uniprot.org/annotation/VAR_070807|||http://purl.uniprot.org/annotation/VSP_030820
http://togogenome.org/gene/9606:TNFRSF13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H8V1|||http://purl.uniprot.org/uniprot/Q96RJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes a disulfide bond and thereby changes the specificity, so that both TNFSF13B and TNFSF13 can be bound.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Essential for TNFSF13B/TALL1/BAFF/BLyS binding|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||In CVID4; fails to bind TNFSF13B and fails to induce downstream NF-kappa-B processing.|||In isoform 2.|||Polar residues|||Pro residues|||Strongly reduced affinity for TNFSF13B.|||TNFR-Cys; truncated|||Tumor necrosis factor receptor superfamily member 13C|||Tumour necrosis factor receptor 13C TALL-1 binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058933|||http://purl.uniprot.org/annotation/VAR_063888|||http://purl.uniprot.org/annotation/VAR_063889|||http://purl.uniprot.org/annotation/VAR_063890|||http://purl.uniprot.org/annotation/VSP_006505
http://togogenome.org/gene/9606:MPHOSPH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99547                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||M-phase phosphoprotein 6|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122437|||http://purl.uniprot.org/annotation/VAR_056150
http://togogenome.org/gene/9606:TOMM22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q549C5|||http://purl.uniprot.org/uniprot/Q9NS69                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||C-tail signal; necessary for mitochondrion outer membrane localization and integration in the TOM complex|||Cytoplasmic|||Disordered|||Helical|||Import sequence; necessary for mitochondrion outer membrane localization and integration in the TOM complex|||Mitochondrial import receptor subunit TOM22 homolog|||Mitochondrial intermembrane|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||TMD; necessary for mitochondrion outer membrane localization and integration in the TOM complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076106
http://togogenome.org/gene/9606:ZNF616                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AN1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 616                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280424|||http://purl.uniprot.org/annotation/VAR_031149|||http://purl.uniprot.org/annotation/VAR_061960
http://togogenome.org/gene/9606:TGM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J576|||http://purl.uniprot.org/uniprot/P49221                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein-glutamine gamma-glutamyltransferase 4|||Transglutaminase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213711|||http://purl.uniprot.org/annotation/VAR_052555|||http://purl.uniprot.org/annotation/VAR_052556|||http://purl.uniprot.org/annotation/VAR_052557|||http://purl.uniprot.org/annotation/VAR_052558|||http://purl.uniprot.org/annotation/VAR_052559|||http://purl.uniprot.org/annotation/VAR_052560|||http://purl.uniprot.org/annotation/VAR_052561|||http://purl.uniprot.org/annotation/VAR_052562|||http://purl.uniprot.org/annotation/VAR_052563
http://togogenome.org/gene/9606:GLT6D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4J2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Putative glycosyltransferase 6 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311971|||http://purl.uniprot.org/annotation/VAR_037382|||http://purl.uniprot.org/annotation/VAR_037383|||http://purl.uniprot.org/annotation/VAR_080956
http://togogenome.org/gene/9606:CCL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00626                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-C motif chemokine 22|||MDC(3-69)|||MDC(5-69)|||MDC(7-69)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005224|||http://purl.uniprot.org/annotation/PRO_0000005225|||http://purl.uniprot.org/annotation/PRO_0000005226|||http://purl.uniprot.org/annotation/PRO_0000005227|||http://purl.uniprot.org/annotation/VAR_055117
http://togogenome.org/gene/9606:RAI14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0K7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankycorbin|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239630|||http://purl.uniprot.org/annotation/VAR_026673|||http://purl.uniprot.org/annotation/VAR_055517|||http://purl.uniprot.org/annotation/VAR_055518|||http://purl.uniprot.org/annotation/VAR_055519|||http://purl.uniprot.org/annotation/VSP_019248|||http://purl.uniprot.org/annotation/VSP_019249|||http://purl.uniprot.org/annotation/VSP_045814
http://togogenome.org/gene/9606:NOTCH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X983|||http://purl.uniprot.org/uniprot/Q99466                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 10|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 2|||EGF-like 20|||EGF-like 21|||EGF-like 22|||EGF-like 23|||EGF-like 24|||EGF-like 25|||EGF-like 26|||EGF-like 27|||EGF-like 28|||EGF-like 29|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||LNR|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||Neurogenic locus notch homolog protein 4|||Notch 4 extracellular truncation|||Notch 4 intracellular domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007701|||http://purl.uniprot.org/annotation/PRO_0000007702|||http://purl.uniprot.org/annotation/PRO_0000007703|||http://purl.uniprot.org/annotation/PRO_5010954369|||http://purl.uniprot.org/annotation/VAR_012866|||http://purl.uniprot.org/annotation/VAR_012867|||http://purl.uniprot.org/annotation/VAR_012868|||http://purl.uniprot.org/annotation/VAR_012869|||http://purl.uniprot.org/annotation/VAR_012870|||http://purl.uniprot.org/annotation/VAR_033828|||http://purl.uniprot.org/annotation/VAR_033829|||http://purl.uniprot.org/annotation/VAR_033830|||http://purl.uniprot.org/annotation/VAR_033831|||http://purl.uniprot.org/annotation/VAR_048991|||http://purl.uniprot.org/annotation/VAR_048992|||http://purl.uniprot.org/annotation/VAR_048993|||http://purl.uniprot.org/annotation/VAR_059271|||http://purl.uniprot.org/annotation/VSP_001406|||http://purl.uniprot.org/annotation/VSP_001407
http://togogenome.org/gene/9606:NIPBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJS4|||http://purl.uniprot.org/uniprot/Q6KC79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CBX3; when associated with A-1003.|||Abolishes interaction with CBX3; when associated with A-1005.|||Abolishes interaction with CBX5; when associated with E-1003.|||Abolishes interaction with CBX5; when associated with E-1005.|||Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In CDLS1.|||In CDLS1; benign variant; no effect on interaction with SCC4.|||In CDLS1; no effect on interaction with SCC4.|||In CDLS1; strongly inhibits interaction with SCC4.|||In CDLS1; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nipped-B-like protein|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||PxVxL motif|||Sister chromatid cohesion C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218596|||http://purl.uniprot.org/annotation/VAR_019518|||http://purl.uniprot.org/annotation/VAR_019519|||http://purl.uniprot.org/annotation/VAR_019520|||http://purl.uniprot.org/annotation/VAR_019521|||http://purl.uniprot.org/annotation/VAR_021596|||http://purl.uniprot.org/annotation/VAR_021597|||http://purl.uniprot.org/annotation/VAR_021598|||http://purl.uniprot.org/annotation/VAR_021599|||http://purl.uniprot.org/annotation/VAR_021600|||http://purl.uniprot.org/annotation/VAR_021601|||http://purl.uniprot.org/annotation/VAR_021602|||http://purl.uniprot.org/annotation/VAR_021603|||http://purl.uniprot.org/annotation/VAR_021604|||http://purl.uniprot.org/annotation/VAR_021605|||http://purl.uniprot.org/annotation/VAR_021606|||http://purl.uniprot.org/annotation/VAR_021607|||http://purl.uniprot.org/annotation/VAR_021608|||http://purl.uniprot.org/annotation/VAR_036164|||http://purl.uniprot.org/annotation/VAR_038411|||http://purl.uniprot.org/annotation/VAR_038412|||http://purl.uniprot.org/annotation/VAR_038413|||http://purl.uniprot.org/annotation/VAR_064544|||http://purl.uniprot.org/annotation/VAR_064545|||http://purl.uniprot.org/annotation/VAR_064546|||http://purl.uniprot.org/annotation/VAR_064547|||http://purl.uniprot.org/annotation/VAR_072996|||http://purl.uniprot.org/annotation/VAR_072997|||http://purl.uniprot.org/annotation/VAR_072998|||http://purl.uniprot.org/annotation/VAR_072999|||http://purl.uniprot.org/annotation/VAR_073000|||http://purl.uniprot.org/annotation/VAR_073001|||http://purl.uniprot.org/annotation/VAR_073002|||http://purl.uniprot.org/annotation/VAR_073003|||http://purl.uniprot.org/annotation/VAR_073004|||http://purl.uniprot.org/annotation/VAR_073005|||http://purl.uniprot.org/annotation/VAR_073006|||http://purl.uniprot.org/annotation/VAR_073007|||http://purl.uniprot.org/annotation/VAR_073008|||http://purl.uniprot.org/annotation/VAR_073009|||http://purl.uniprot.org/annotation/VAR_073010|||http://purl.uniprot.org/annotation/VAR_073011|||http://purl.uniprot.org/annotation/VAR_073012|||http://purl.uniprot.org/annotation/VAR_073013|||http://purl.uniprot.org/annotation/VAR_073014|||http://purl.uniprot.org/annotation/VAR_073015|||http://purl.uniprot.org/annotation/VAR_073016|||http://purl.uniprot.org/annotation/VAR_073017|||http://purl.uniprot.org/annotation/VAR_073018|||http://purl.uniprot.org/annotation/VSP_011091|||http://purl.uniprot.org/annotation/VSP_011092|||http://purl.uniprot.org/annotation/VSP_011093
http://togogenome.org/gene/9606:ZMAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UDW3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||Disordered|||Zinc finger matrin-type protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254114
http://togogenome.org/gene/9606:SS18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLD3|||http://purl.uniprot.org/uniprot/Q15532|||http://purl.uniprot.org/uniprot/Q4VAX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Site|||Splice Variant                                                                                  ^@                                                                                  1|||2|||2 X 13 AA imperfect tandem repeats|||Breakpoint for translocation to form the SSXT-SSX1 fusion protein (rare)|||Breakpoint for translocation to form the SSXT-SSX1 or SSXT-SSX2 fusion proteins|||Disordered|||In isoform 2.|||N-acetylserine|||Polar residues|||Protein SSXT|||Removed|||SH2-binding|||SH3-binding|||SS18 N-terminal|||Transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181823|||http://purl.uniprot.org/annotation/VSP_006258
http://togogenome.org/gene/9606:ZFC3H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60293                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||In isoform 2.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||Zinc finger C3H1 domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286103|||http://purl.uniprot.org/annotation/VAR_032070|||http://purl.uniprot.org/annotation/VAR_032071|||http://purl.uniprot.org/annotation/VSP_024992|||http://purl.uniprot.org/annotation/VSP_024993|||http://purl.uniprot.org/annotation/VSP_024995
http://togogenome.org/gene/9606:ITPKC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calmodulin-binding|||Disordered|||Inositol-trisphosphate 3-kinase C|||Loss of kinase activity.|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234070
http://togogenome.org/gene/9606:LIN7C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUP9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif                                                                                  ^@                                                                                  Kinase interacting site|||L27|||N-acetylalanine|||PDZ|||Protein lin-7 homolog C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189629
http://togogenome.org/gene/9606:KLHL21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with CUL3.|||BACK|||BTB|||Basic and acidic residues|||Disordered|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119125|||http://purl.uniprot.org/annotation/VSP_032563|||http://purl.uniprot.org/annotation/VSP_032564
http://togogenome.org/gene/9606:LGALS3BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Y1|||http://purl.uniprot.org/uniprot/Q08380                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Galectin-3-binding protein|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033230|||http://purl.uniprot.org/annotation/PRO_5014239312
http://togogenome.org/gene/9606:FOLH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04609                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Can be associated with lower folate and higher homocysteine levels.|||Charge relay system|||Complete loss of activity.|||Cytoplasmic|||Extracellular|||Glutamate carboxypeptidase 2|||Helical; Signal-anchor for type II membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform PSMA'.|||In isoform PSMA-3.|||In isoform PSMA-4.|||In isoform PSMA-7 and isoform PSMA-9.|||In isoform PSMA-8 and isoform PSMA-9.|||Loss of glycosylation. Abolishes enzyme activity.|||Loss of glycosylation. Reduces enzyme activity.|||Loss of glycosylation. Severely reduced enzyme activity.|||N-linked (GlcNAc...) asparagine|||NAALADase|||No effect on enzyme activity.|||Nucleophile; for NAALADase activity|||Phosphoserine|||Reduces enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174117|||http://purl.uniprot.org/annotation/VAR_012736|||http://purl.uniprot.org/annotation/VAR_024592|||http://purl.uniprot.org/annotation/VAR_028882|||http://purl.uniprot.org/annotation/VAR_036398|||http://purl.uniprot.org/annotation/VSP_005336|||http://purl.uniprot.org/annotation/VSP_038058|||http://purl.uniprot.org/annotation/VSP_038059|||http://purl.uniprot.org/annotation/VSP_040243|||http://purl.uniprot.org/annotation/VSP_040244|||http://purl.uniprot.org/annotation/VSP_040245|||http://purl.uniprot.org/annotation/VSP_044287
http://togogenome.org/gene/9606:PRLR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16471                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In HPRL; loss of function.|||In MFAB; confers constitutive activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 8.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Prolactin receptor|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010977|||http://purl.uniprot.org/annotation/VAR_049172|||http://purl.uniprot.org/annotation/VAR_070894|||http://purl.uniprot.org/annotation/VAR_070895|||http://purl.uniprot.org/annotation/VSP_001720|||http://purl.uniprot.org/annotation/VSP_012620|||http://purl.uniprot.org/annotation/VSP_012621|||http://purl.uniprot.org/annotation/VSP_026531|||http://purl.uniprot.org/annotation/VSP_026532|||http://purl.uniprot.org/annotation/VSP_026533|||http://purl.uniprot.org/annotation/VSP_026534|||http://purl.uniprot.org/annotation/VSP_026535|||http://purl.uniprot.org/annotation/VSP_026536|||http://purl.uniprot.org/annotation/VSP_026537|||http://purl.uniprot.org/annotation/VSP_026538|||http://purl.uniprot.org/annotation/VSP_026539|||http://purl.uniprot.org/annotation/VSP_047882|||http://purl.uniprot.org/annotation/VSP_047883
http://togogenome.org/gene/9606:ALOX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16050                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  36% of arachidonate 15-lipoxygenase activity.|||46% of arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate.|||Catalyzes 15- and 12-lipoxygenation.|||Does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate.|||Does not affect arachidonate 15-lipoxygenase activity. Does not affect protein affinity for (9Z,12Z)-octadecadienoate..|||In isoform 2.|||Lipoxygenase|||Loss of arachidonate 15-lipoxygenase activity.|||Loss of catalytic activity; Loss of arachidonate 15-lipoxygenase activity..|||PLAT|||Polyunsaturated fatty acid lipoxygenase ALOX15|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220697|||http://purl.uniprot.org/annotation/VAR_018746|||http://purl.uniprot.org/annotation/VAR_018747|||http://purl.uniprot.org/annotation/VAR_018748|||http://purl.uniprot.org/annotation/VAR_035036|||http://purl.uniprot.org/annotation/VAR_035037|||http://purl.uniprot.org/annotation/VAR_035038|||http://purl.uniprot.org/annotation/VAR_035039|||http://purl.uniprot.org/annotation/VAR_083449|||http://purl.uniprot.org/annotation/VAR_083450|||http://purl.uniprot.org/annotation/VAR_083451|||http://purl.uniprot.org/annotation/VAR_083452|||http://purl.uniprot.org/annotation/VSP_056681
http://togogenome.org/gene/9606:SF3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15459                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to SF3A3.|||Acidic residues|||Basic and acidic residues|||Critical for binding to SF3A3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N6-acetyllysine|||No effect on binding to SF3A3.|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Removed|||Required and sufficient for nuclear import|||SLURP 1 motif acquires binding to SF3A3; when associated with Leu-55.|||SLURP 1 motif acquires binding to SF3A3; when associated with Phe-48.|||SURP motif 1|||SURP motif 2|||Splicing factor 3A subunit 1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114917|||http://purl.uniprot.org/annotation/VAR_036290|||http://purl.uniprot.org/annotation/VSP_054090
http://togogenome.org/gene/9606:PDHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDR8|||http://purl.uniprot.org/uniprot/P11177                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Does not affect interaction with DLAT.|||Important for interaction with DLAT|||In PDHBD.|||In isoform 2.|||In isoform 3.|||Inhibits interaction with DLAT. Does not affect pyruvate decarboxylase activity. Loss of multienzyme pyruvate dehydrogenase complex activity.|||Mitochondrion|||N6-acetyllysine|||Phosphotyrosine|||Pyruvate dehydrogenase E1 component subunit beta, mitochondrial|||Reduces interaction with DLAT. Reduces multienzyme pyruvate dehydrogenase complex activity. Does not affect pyruvate decarboxylase activity.|||Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT.|||Transketolase-like pyrimidine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020457|||http://purl.uniprot.org/annotation/VAR_004967|||http://purl.uniprot.org/annotation/VAR_021058|||http://purl.uniprot.org/annotation/VAR_030954|||http://purl.uniprot.org/annotation/VSP_012675|||http://purl.uniprot.org/annotation/VSP_043364
http://togogenome.org/gene/9606:C11orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00193                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Small acidic protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263656
http://togogenome.org/gene/9606:BCL2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16548                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BH1|||BH2|||Bcl-2-related protein A1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143094|||http://purl.uniprot.org/annotation/VAR_020342|||http://purl.uniprot.org/annotation/VAR_020343|||http://purl.uniprot.org/annotation/VAR_020344|||http://purl.uniprot.org/annotation/VAR_044059|||http://purl.uniprot.org/annotation/VSP_043106
http://togogenome.org/gene/9606:SOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00441|||http://purl.uniprot.org/uniprot/V9HWC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33)|||Abolishes dimerization; when associated with E-50 and E-51.|||Abolishes dimerization; when associated with Q-134.|||Decreased succinylation.|||Destabilization of dimer and loss of zinc binding; when associated with S-81.|||Destabilization of dimer and loss of zinc binding; when associated with S-84.|||Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147.|||Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147.|||Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112.|||Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147.|||Exhibits very slow copper acquisition.|||In ALS.|||In ALS1.|||In ALS1; 'benign' form; 80% of wild-type activity; ubiquitinated by RNF19A.|||In ALS1; 30% of wild-type activity.|||In ALS1; destabilizes dimeric protein structure and increases tendency to form fibrillar aggregates.|||In ALS1; does not seem to be linked with a decrease in activity.|||In ALS1; increases tendency to form fibrillar aggregates.|||In ALS1; increases tendency to form fibrillar aggregates; ubiquitinated by RNF19A.|||In ALS1; mild form; ubiquitinated by RNF19A. Ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.|||In ALS1; reduced metal binding; increases tendency to form fibrillar aggregates.|||In ALS1; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.|||In ALS1; reduces tendency to form fibrillar aggregates.|||In ALS1; severe form; reduces structural stability and enzyme activity; increases tendency to form fibrillar aggregates.|||In ALS1; slow progression.|||In ALS1; sporadic form; interferes with zinc binding; requires 2 nucleotide substitutions.|||In ALS1; sporadic young onset.|||In ALS1; ubiquitinated by RNF19A; interferes with zinc-binding; ubiquitinated by MARCH5; leading to the degradation of mitochondrial SOD1.|||Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81.|||Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84.|||Mimicks constitutive succinylation state; decreased activity.|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No palmitoylation, reduced nuclear targeting.|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Superoxide dismutase [Cu-Zn]|||Superoxide dismutase copper/zinc binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164057|||http://purl.uniprot.org/annotation/VAR_007130|||http://purl.uniprot.org/annotation/VAR_007131|||http://purl.uniprot.org/annotation/VAR_007132|||http://purl.uniprot.org/annotation/VAR_007133|||http://purl.uniprot.org/annotation/VAR_007134|||http://purl.uniprot.org/annotation/VAR_007135|||http://purl.uniprot.org/annotation/VAR_007136|||http://purl.uniprot.org/annotation/VAR_007137|||http://purl.uniprot.org/annotation/VAR_007138|||http://purl.uniprot.org/annotation/VAR_007139|||http://purl.uniprot.org/annotation/VAR_007140|||http://purl.uniprot.org/annotation/VAR_007141|||http://purl.uniprot.org/annotation/VAR_007142|||http://purl.uniprot.org/annotation/VAR_007143|||http://purl.uniprot.org/annotation/VAR_007144|||http://purl.uniprot.org/annotation/VAR_007145|||http://purl.uniprot.org/annotation/VAR_007146|||http://purl.uniprot.org/annotation/VAR_007147|||http://purl.uniprot.org/annotation/VAR_007148|||http://purl.uniprot.org/annotation/VAR_007149|||http://purl.uniprot.org/annotation/VAR_007150|||http://purl.uniprot.org/annotation/VAR_007151|||http://purl.uniprot.org/annotation/VAR_007152|||http://purl.uniprot.org/annotation/VAR_007153|||http://purl.uniprot.org/annotation/VAR_007154|||http://purl.uniprot.org/annotation/VAR_007155|||http://purl.uniprot.org/annotation/VAR_007156|||http://purl.uniprot.org/annotation/VAR_007157|||http://purl.uniprot.org/annotation/VAR_007158|||http://purl.uniprot.org/annotation/VAR_007159|||http://purl.uniprot.org/annotation/VAR_007160|||http://purl.uniprot.org/annotation/VAR_007161|||http://purl.uniprot.org/annotation/VAR_007162|||http://purl.uniprot.org/annotation/VAR_007163|||http://purl.uniprot.org/annotation/VAR_007164|||http://purl.uniprot.org/annotation/VAR_008717|||http://purl.uniprot.org/annotation/VAR_008718|||http://purl.uniprot.org/annotation/VAR_008719|||http://purl.uniprot.org/annotation/VAR_008720|||http://purl.uniprot.org/annotation/VAR_008721|||http://purl.uniprot.org/annotation/VAR_008722|||http://purl.uniprot.org/annotation/VAR_008723|||http://purl.uniprot.org/annotation/VAR_008724|||http://purl.uniprot.org/annotation/VAR_008725|||http://purl.uniprot.org/annotation/VAR_013518|||http://purl.uniprot.org/annotation/VAR_013519|||http://purl.uniprot.org/annotation/VAR_013520|||http://purl.uniprot.org/annotation/VAR_013521|||http://purl.uniprot.org/annotation/VAR_013522|||http://purl.uniprot.org/annotation/VAR_013523|||http://purl.uniprot.org/annotation/VAR_013524|||http://purl.uniprot.org/annotation/VAR_013525|||http://purl.uniprot.org/annotation/VAR_013526|||http://purl.uniprot.org/annotation/VAR_013527|||http://purl.uniprot.org/annotation/VAR_013528|||http://purl.uniprot.org/annotation/VAR_013529|||http://purl.uniprot.org/annotation/VAR_013530|||http://purl.uniprot.org/annotation/VAR_013531|||http://purl.uniprot.org/annotation/VAR_013532|||http://purl.uniprot.org/annotation/VAR_013533|||http://purl.uniprot.org/annotation/VAR_013534|||http://purl.uniprot.org/annotation/VAR_013535|||http://purl.uniprot.org/annotation/VAR_013536|||http://purl.uniprot.org/annotation/VAR_013537|||http://purl.uniprot.org/annotation/VAR_013538|||http://purl.uniprot.org/annotation/VAR_013539|||http://purl.uniprot.org/annotation/VAR_013540|||http://purl.uniprot.org/annotation/VAR_016874|||http://purl.uniprot.org/annotation/VAR_045876|||http://purl.uniprot.org/annotation/VAR_045877|||http://purl.uniprot.org/annotation/VAR_045878|||http://purl.uniprot.org/annotation/VAR_045879|||http://purl.uniprot.org/annotation/VAR_045880|||http://purl.uniprot.org/annotation/VAR_045881|||http://purl.uniprot.org/annotation/VAR_045882|||http://purl.uniprot.org/annotation/VAR_045883|||http://purl.uniprot.org/annotation/VAR_045884|||http://purl.uniprot.org/annotation/VAR_045885|||http://purl.uniprot.org/annotation/VAR_065194|||http://purl.uniprot.org/annotation/VAR_065560|||http://purl.uniprot.org/annotation/VAR_077327
http://togogenome.org/gene/9606:EXOSC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B26                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exosome complex component RRP43|||In PCH1C.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139967|||http://purl.uniprot.org/annotation/VAR_072558|||http://purl.uniprot.org/annotation/VAR_072559
http://togogenome.org/gene/9606:ARMH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIY5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  Armadillo-like helical domain containing protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320611|||http://purl.uniprot.org/annotation/VSP_031683
http://togogenome.org/gene/9606:CRACDL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NV74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CRACD-like protein|||Disordered|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289161|||http://purl.uniprot.org/annotation/VAR_047335
http://togogenome.org/gene/9606:GTF2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R506|||http://purl.uniprot.org/uniprot/P52657                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand                                                                                  ^@                                                                                  Transcription initiation factor IIA gamma subunit C-terminal|||Transcription initiation factor IIA gamma subunit N-terminal|||Transcription initiation factor IIA subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194042
http://togogenome.org/gene/9606:CYP2R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6VVX0                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In VDDR1B; complete loss of activity.|||Reduces 25-hydroxylase activity.|||Vitamin D 25-hydroxylase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051778|||http://purl.uniprot.org/annotation/VAR_021534|||http://purl.uniprot.org/annotation/VAR_075532
http://togogenome.org/gene/9606:OGDHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  2-oxoglutarate dehydrogenase-like, mitochondrial|||Disordered|||In YOBELN.|||In YOBELN; unknown pathological significance.|||In YOBELN; unknown pathological significance; fails to rescue knockdown-induced defects of neuronal function in a Drosophila model system.|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310983|||http://purl.uniprot.org/annotation/VAR_037125|||http://purl.uniprot.org/annotation/VAR_037126|||http://purl.uniprot.org/annotation/VAR_037127|||http://purl.uniprot.org/annotation/VAR_037128|||http://purl.uniprot.org/annotation/VAR_037129|||http://purl.uniprot.org/annotation/VAR_086797|||http://purl.uniprot.org/annotation/VAR_086798|||http://purl.uniprot.org/annotation/VAR_086799|||http://purl.uniprot.org/annotation/VAR_086800|||http://purl.uniprot.org/annotation/VAR_086801|||http://purl.uniprot.org/annotation/VAR_086802|||http://purl.uniprot.org/annotation/VAR_086803|||http://purl.uniprot.org/annotation/VAR_086804|||http://purl.uniprot.org/annotation/VAR_086805|||http://purl.uniprot.org/annotation/VAR_086806|||http://purl.uniprot.org/annotation/VSP_041350|||http://purl.uniprot.org/annotation/VSP_041351
http://togogenome.org/gene/9606:PRKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WBA3|||http://purl.uniprot.org/uniprot/Q15139                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Constitutive activation and constitutive phosphorylation of S-738 and S-742.|||Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL.|||Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502.|||Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502.|||Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity.|||Disordered|||In CHDED.|||In a colorectal cancer sample; somatic mutation.|||In a lung bronchoalveolar carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||Increase in ability to bind phorbol ester, loss of ability to bind DAG.|||Loss of activation.|||Loss of kinase activity.|||No effect on ability to bind phorbol ester, slight increase in ability to bind DAG.|||PH|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by MAPK13|||Phosphoserine; by PKC/PRKCD|||Phosphoserine; by autocatalysis|||Phosphoserine; by autocatalysis and PKC/PRKCD|||Phosphotyrosine|||Phosphotyrosine; by ABL|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055714|||http://purl.uniprot.org/annotation/VAR_035468|||http://purl.uniprot.org/annotation/VAR_035469|||http://purl.uniprot.org/annotation/VAR_042324|||http://purl.uniprot.org/annotation/VAR_042325|||http://purl.uniprot.org/annotation/VAR_042326|||http://purl.uniprot.org/annotation/VAR_042327|||http://purl.uniprot.org/annotation/VAR_042328|||http://purl.uniprot.org/annotation/VAR_042329|||http://purl.uniprot.org/annotation/VAR_046988|||http://purl.uniprot.org/annotation/VAR_078602|||http://purl.uniprot.org/annotation/VAR_078603
http://togogenome.org/gene/9606:MYCT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N699                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Myc target protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310959|||http://purl.uniprot.org/annotation/VAR_037115|||http://purl.uniprot.org/annotation/VAR_037116
http://togogenome.org/gene/9606:TMEM86B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N661                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Lysoplasmalogenase TMEM86B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000201841|||http://purl.uniprot.org/annotation/VAR_052343|||http://purl.uniprot.org/annotation/VAR_052344
http://togogenome.org/gene/9606:XK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51811                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum membrane adapter protein XK|||Extracellular|||Helical|||In MLS.|||In MLS; atypical without hematologic, neuromuscular, or cerebral involvement.|||Interchain (with C-72 in Kell)|||Loss of Kell-XK complex.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190767|||http://purl.uniprot.org/annotation/VAR_013817|||http://purl.uniprot.org/annotation/VAR_013818|||http://purl.uniprot.org/annotation/VAR_023581|||http://purl.uniprot.org/annotation/VAR_086162|||http://purl.uniprot.org/annotation/VAR_086163
http://togogenome.org/gene/9606:B3GNT9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX72                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000352762
http://togogenome.org/gene/9606:DNMT3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJW3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADD|||DNA (cytosine-5)-methyltransferase 3-like|||GATA-type; atypical|||In isoform 2.|||Loss of binding to DNMT3A.|||PHD-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088047|||http://purl.uniprot.org/annotation/VAR_051962|||http://purl.uniprot.org/annotation/VSP_041295
http://togogenome.org/gene/9606:PDLIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JY6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes ability to suppress anchorage independent growth but not cell adhesion to collagen; when associated with S-313.|||Abolishes ability to suppress anchorage independent growth but not cell adhesion to collagen; when associated with S-316.|||Abolishes cell adhesion to collagen and ability to suppress anchorage independent growth.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM zinc-binding|||PDZ|||PDZ and LIM domain protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075862|||http://purl.uniprot.org/annotation/VSP_014058|||http://purl.uniprot.org/annotation/VSP_014059|||http://purl.uniprot.org/annotation/VSP_014060|||http://purl.uniprot.org/annotation/VSP_014061|||http://purl.uniprot.org/annotation/VSP_047113
http://togogenome.org/gene/9606:CDKN1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46527|||http://purl.uniprot.org/uniprot/Q6I9V6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes LYN-mediated phosphorylation, reduces CDK2-mediated phosphorylation on T-187, has greater cell cycle arrest into S-phase, no effect on binding CDK2 complexes, reduced CDK4 binding and inhibits CDK4 enzyme activity. No nuclear translocation. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-89.|||Abolishes PKB/AKT1-mediated phosphorylation. 46% cytoplasmic location. Greatly reduced binding to YWHAQ. Equally reduced binding; when associated with A-10 and A-187. No nuclear import; when associated with A-157. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-157.|||Abolishes phosphorylation-dependent ubiquitination.|||Basic and acidic residues|||Cyclin-dependent kinase inhibitor|||Cyclin-dependent kinase inhibitor 1B|||Disordered|||Exported to the cytoplasm. Inhibits cell cycle arrest.|||Found in a patient with multiple endocrine tumors; germline mutation; reduced expression levels; shows impaired binding to CDK2.|||Greatly reduced PKB/AKT1-mediated phosphorylation. Nuclear location. Inhibits cyclin E/CDK2 cell cycle progression. No effect on binding AKT1. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-198.|||Increased stability in vivo and in vitro.|||Interaction with CDK2|||Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest.|||No change in PKB/AKT1- nor UHMK1-mediated phosphorylation.|||No change in PKB/AKT1-mediated phosphorylation.|||No change in binding CDK4 and no inhibition of CDK4 activity. Translocates to nucleus. No effect on in vitro phosphorylation of CDK4 by CCNH-CDK7.|||No effect on binding CDK2 complexes, reduced CDK4 binding and greatly inhibits CDK4 enzyme activity. No nuclear translocation. Inhibits in vitro phosphorylation of CDK4 by CCNH-CDK7. Completely abolishes CDK4 binding; when associated with F-88.|||Nuclear localization signal|||Phosphoserine; by UHMK1|||Phosphothreonine|||Phosphothreonine; by CaMK1, PKB/AKT1 and PIM1|||Phosphothreonine; by CaMK1, PKB/AKT1, RPS6KA1, RPS6KA3 and PIM1|||Phosphothreonine; by PKB/AKT1, CDK1 and CDK2|||Phosphotyrosine|||Phosphotyrosine; by ABL, LYN, SRC and JAK2|||Phosphotyrosine; by SRC|||Strongly reduced ubiquitination by a TRIM21-containing SCF(SKP2) complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190084|||http://purl.uniprot.org/annotation/VAR_011871|||http://purl.uniprot.org/annotation/VAR_011872|||http://purl.uniprot.org/annotation/VAR_064429
http://togogenome.org/gene/9606:SPATA31A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280245
http://togogenome.org/gene/9606:RFXAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00287                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||C-terminal domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Regulatory factor X-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097310
http://togogenome.org/gene/9606:URGCP-MRPS24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/S4R325                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:CALCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10092                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Calcitonin gene-related peptide 2|||Phenylalanine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004086|||http://purl.uniprot.org/annotation/PRO_0000004087|||http://purl.uniprot.org/annotation/PRO_0000004088
http://togogenome.org/gene/9606:MAN2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z754|||http://purl.uniprot.org/uniprot/E9PCD7|||http://purl.uniprot.org/uniprot/Q9Y2E5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alpha-mannosidase|||Disordered|||Epididymis-specific alpha-mannosidase|||Glycoside hydrolase family 38 central|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012077|||http://purl.uniprot.org/annotation/PRO_5017848718|||http://purl.uniprot.org/annotation/PRO_5017853172|||http://purl.uniprot.org/annotation/VAR_025328|||http://purl.uniprot.org/annotation/VAR_025329|||http://purl.uniprot.org/annotation/VAR_025330|||http://purl.uniprot.org/annotation/VAR_025331|||http://purl.uniprot.org/annotation/VAR_055840|||http://purl.uniprot.org/annotation/VSP_013816
http://togogenome.org/gene/9606:ATP10D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P241                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||Impairs ATPase flippase activity.|||In isoform 2.|||Increases ATPase flippase activity.|||Phospholipid-transporting ATPase VD|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046382|||http://purl.uniprot.org/annotation/VAR_020187|||http://purl.uniprot.org/annotation/VAR_024371|||http://purl.uniprot.org/annotation/VAR_048385|||http://purl.uniprot.org/annotation/VAR_048386|||http://purl.uniprot.org/annotation/VAR_048387|||http://purl.uniprot.org/annotation/VAR_048388|||http://purl.uniprot.org/annotation/VAR_048389|||http://purl.uniprot.org/annotation/VAR_048390|||http://purl.uniprot.org/annotation/VAR_048391|||http://purl.uniprot.org/annotation/VAR_048392|||http://purl.uniprot.org/annotation/VAR_048393|||http://purl.uniprot.org/annotation/VAR_048394|||http://purl.uniprot.org/annotation/VAR_048395|||http://purl.uniprot.org/annotation/VSP_006954
http://togogenome.org/gene/9606:RPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUL2|||http://purl.uniprot.org/uniprot/P15927                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RFWD3, leading to impair DNA interstrand cross-links (ICL) repair.|||Disordered|||Does not affect interaction with RFWD3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ubiquitination without affecting homologous recombination.|||In isoform 2.|||In isoform 3.|||Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-4.|||Increased RAD51 foci formation and homologous recombination efficiency at DNA double-strand breaks; when associated with A-8.|||Interaction with RAD52, TIPIN, UNG and XPA|||Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-33. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-23; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-23; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-23; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-23; D-29 and D-33.|||Lower homologous recombination efficiency following DNA double strand break. Impaired DNA synthesis following DNA damage; when associated with D-8. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-29. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-29. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-29. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-29.|||N-acetylmethionine|||No effect on DNA synthesis following DNA damage; when associated with D-23. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-23 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-23 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-23 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-23 and D-33.|||No effect on DNA synthesis following DNA damage; when associated with D-29. No effect on cell-cycle progression, nor DNA synthesis in undamaged cells; when associated with D-8; D-29 and D-33. Impaired DNA double strand breaks repair; when associated with D-8; D-29 and D-33. Extended DNA damage-induced G2-M checkpoint; when associated with D-8; D-29 and D-33. Preferentially interacts with RAD51; when associated with D-8; D-29 and D-33.|||OB|||Phosphoserine; by CDK1|||Phosphoserine; by CDK2|||Phosphoserine; by PRKDC|||Phosphothreonine; by PRKDC|||Reduces phosphorylation by CDK1.|||Replication protein A 32 kDa subunit|||Replication protein A C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097270|||http://purl.uniprot.org/annotation/VAR_023300|||http://purl.uniprot.org/annotation/VAR_023301|||http://purl.uniprot.org/annotation/VAR_023302|||http://purl.uniprot.org/annotation/VSP_017201|||http://purl.uniprot.org/annotation/VSP_017202
http://togogenome.org/gene/9606:CRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3K9|||http://purl.uniprot.org/uniprot/A0A0S2Z3Q4|||http://purl.uniprot.org/uniprot/L7RT18|||http://purl.uniprot.org/uniprot/P46108                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with DOCK1.|||Abolishes interaction with DOCK5. Abolishes RAP1 activation.|||Abolishes interaction with PEAK3.|||Adapter molecule crk|||Disordered|||In isoform Crk-I.|||N-acetylalanine|||No effect on interaction with PEAK3.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Pro residues|||Proline switch|||Removed|||SH2|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079351|||http://purl.uniprot.org/annotation/VSP_041153|||http://purl.uniprot.org/annotation/VSP_041154
http://togogenome.org/gene/9606:KIF5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12840                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Globular|||In ALS25.|||In ALS25; unknown pathological significance.|||In SPG10.|||In SPG10; complicated form.|||In SPG10; decreases microtubule affinity; reduces gliding velocity; reduces microtubule-dependent ATP turnover.|||In SPG10; does not affect microtubule affinity; does not affect gliding velocity; does not affect microtubule-dependent ATP turnover.|||In SPG10; pure form.|||In SPG10; slightly decreases microtubule affinity; reduces gliding velocity; reduces microtubule-dependent ATP turnover.|||Interaction with BICD2|||Kinesin heavy chain isoform 5A|||Kinesin motor|||Microtubule-binding|||N-acetylalanine|||Necessary for interaction with ZFYVE27|||Phosphothreonine|||Polar residues|||Removed|||Strongly reduces microtubule affinity; slightly reduces gliding velocity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125353|||http://purl.uniprot.org/annotation/VAR_032842|||http://purl.uniprot.org/annotation/VAR_032843|||http://purl.uniprot.org/annotation/VAR_032844|||http://purl.uniprot.org/annotation/VAR_033108|||http://purl.uniprot.org/annotation/VAR_046744|||http://purl.uniprot.org/annotation/VAR_058741|||http://purl.uniprot.org/annotation/VAR_058742|||http://purl.uniprot.org/annotation/VAR_058743|||http://purl.uniprot.org/annotation/VAR_058744|||http://purl.uniprot.org/annotation/VAR_058745|||http://purl.uniprot.org/annotation/VAR_058746|||http://purl.uniprot.org/annotation/VAR_058747|||http://purl.uniprot.org/annotation/VAR_058748|||http://purl.uniprot.org/annotation/VAR_066616|||http://purl.uniprot.org/annotation/VAR_080647|||http://purl.uniprot.org/annotation/VAR_080648|||http://purl.uniprot.org/annotation/VAR_080649|||http://purl.uniprot.org/annotation/VAR_080650|||http://purl.uniprot.org/annotation/VAR_080651|||http://purl.uniprot.org/annotation/VAR_080652
http://togogenome.org/gene/9606:MTMR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13615                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||In a breast cancer sample; somatic mutation.|||In isoform A and isoform C.|||In isoform A.|||Loss of lipid phosphatase activity.|||Myotubularin phosphatase|||Myotubularin-related protein 3|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094936|||http://purl.uniprot.org/annotation/VAR_035656|||http://purl.uniprot.org/annotation/VSP_007781|||http://purl.uniprot.org/annotation/VSP_007782
http://togogenome.org/gene/9606:ST3GAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXG9|||http://purl.uniprot.org/uniprot/Q16842                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2|||Cytoplasmic|||Has a moderate effect on N-glycosylation and sialyltransferase activity; when associated with Q-211.|||Helical|||Helical; Signal-anchor for type II membrane protein|||Impairs N-glycosylation. Impairs exit from the endoplasmic reticulum. Decreases sialyltransferase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149258
http://togogenome.org/gene/9606:PTK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13308                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by MMP14|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inactive tyrosine-protein kinase 7|||Interaction with CTNNB1|||N-linked (GlcNAc...) asparagine|||No impact on proteolysis by MMP14.|||Phosphoserine|||Prevents proteolysis by MMP14.|||Protein kinase; inactive                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016748|||http://purl.uniprot.org/annotation/VAR_041502|||http://purl.uniprot.org/annotation/VAR_041503|||http://purl.uniprot.org/annotation/VAR_041504|||http://purl.uniprot.org/annotation/VAR_041505|||http://purl.uniprot.org/annotation/VAR_041506|||http://purl.uniprot.org/annotation/VAR_041507|||http://purl.uniprot.org/annotation/VAR_041508|||http://purl.uniprot.org/annotation/VAR_041509|||http://purl.uniprot.org/annotation/VAR_041510|||http://purl.uniprot.org/annotation/VSP_037181|||http://purl.uniprot.org/annotation/VSP_037182|||http://purl.uniprot.org/annotation/VSP_037183|||http://purl.uniprot.org/annotation/VSP_037184|||http://purl.uniprot.org/annotation/VSP_037185|||http://purl.uniprot.org/annotation/VSP_044775
http://togogenome.org/gene/9606:MYH13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-13|||N6,N6,N6-trimethyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123430|||http://purl.uniprot.org/annotation/VAR_024543|||http://purl.uniprot.org/annotation/VAR_030231|||http://purl.uniprot.org/annotation/VAR_030232|||http://purl.uniprot.org/annotation/VAR_030233|||http://purl.uniprot.org/annotation/VAR_030234
http://togogenome.org/gene/9606:AQP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBQ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-11|||Cytoplasmic|||Does not affect endoplasmic reticulum localization. Does not affect trafficking to the plasma membrane. Increases osmotic water permeability. Decreases homomultimerization.|||Does not affect endoplasmic reticulum localization. Does not affect trafficking to the plasma membrane. Reduces protein expression. Increases osmotic water permeability.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||NPA|||NPC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063968|||http://purl.uniprot.org/annotation/VAR_020446
http://togogenome.org/gene/9606:ERICH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGS2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glutamate-rich protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340277
http://togogenome.org/gene/9606:ZNF429                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Phosphoserine|||Zinc finger protein 429                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047577|||http://purl.uniprot.org/annotation/VAR_047848
http://togogenome.org/gene/9606:LDAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6V9                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lipid droplet-associated hydrolase|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300124|||http://purl.uniprot.org/annotation/VSP_042202|||http://purl.uniprot.org/annotation/VSP_054624|||http://purl.uniprot.org/annotation/VSP_055283
http://togogenome.org/gene/9606:SUMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55854                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the formation of poly(SUMO) chains.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired interaction with USP25; when associated with A-33.|||Impaired interaction with USP25; when associated with A-34.|||In isoform 2.|||Small ubiquitin-related modifier 3|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035957|||http://purl.uniprot.org/annotation/PRO_0000035958|||http://purl.uniprot.org/annotation/VAR_052692|||http://purl.uniprot.org/annotation/VSP_054693
http://togogenome.org/gene/9606:RRP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43159                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Phosphoserine|||Polar residues|||Ribosomal RNA-processing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084090|||http://purl.uniprot.org/annotation/VAR_051034|||http://purl.uniprot.org/annotation/VAR_051035
http://togogenome.org/gene/9606:CDON                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule-related/down-regulated by oncogenes|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||In HPE11.|||In HPE11; benign variant.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234054|||http://purl.uniprot.org/annotation/VAR_056038|||http://purl.uniprot.org/annotation/VAR_056039|||http://purl.uniprot.org/annotation/VAR_056040|||http://purl.uniprot.org/annotation/VAR_056041|||http://purl.uniprot.org/annotation/VAR_066497|||http://purl.uniprot.org/annotation/VAR_066498|||http://purl.uniprot.org/annotation/VAR_066499|||http://purl.uniprot.org/annotation/VAR_066500|||http://purl.uniprot.org/annotation/VAR_066501|||http://purl.uniprot.org/annotation/VAR_066502|||http://purl.uniprot.org/annotation/VSP_018201
http://togogenome.org/gene/9606:TM9SF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QYR8|||http://purl.uniprot.org/uniprot/Q99805                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Transmembrane 9 superfamily member|||Transmembrane 9 superfamily member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034365|||http://purl.uniprot.org/annotation/PRO_5014202964
http://togogenome.org/gene/9606:RPL29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47914                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||Disordered|||Large ribosomal subunit protein eL29|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219134
http://togogenome.org/gene/9606:C10orf90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M02                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  (E2-independent) E3 ubiquitin-conjugating enzyme FATS|||ALMS motif|||Basic and acidic residues|||Disordered|||In isoform 2.|||Required for interaction with HDAC1|||Required for interaction with p53/TP53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279492|||http://purl.uniprot.org/annotation/VAR_030908|||http://purl.uniprot.org/annotation/VAR_030909|||http://purl.uniprot.org/annotation/VAR_050855|||http://purl.uniprot.org/annotation/VAR_050856|||http://purl.uniprot.org/annotation/VSP_023458
http://togogenome.org/gene/9606:LOXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08397                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  2',4',5'-topaquinone; alternate|||Associated with exfoliation syndrome in the presence of D-153.|||Associated with exfoliation syndrome in the presence of L-141.|||Disordered|||Lysine tyrosylquinone (Lys-Tyr); alternate|||Lysyl oxidase homolog 1|||Lysyl-oxidase like|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018528|||http://purl.uniprot.org/annotation/PRO_0000018529|||http://purl.uniprot.org/annotation/VAR_022135|||http://purl.uniprot.org/annotation/VAR_028436
http://togogenome.org/gene/9606:GALK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51570|||http://purl.uniprot.org/uniprot/V9HWE7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  GHMP kinase C-terminal|||GHMP kinase N-terminal|||Galactokinase|||Galactokinase N-terminal|||In GALAC2.|||In GALAC2; founder Romani mutation.|||In GALAC2; mild deficiency; Osaka.|||Phosphoserine|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184645|||http://purl.uniprot.org/annotation/VAR_002547|||http://purl.uniprot.org/annotation/VAR_008514|||http://purl.uniprot.org/annotation/VAR_015746|||http://purl.uniprot.org/annotation/VAR_023486|||http://purl.uniprot.org/annotation/VAR_023487|||http://purl.uniprot.org/annotation/VAR_023488|||http://purl.uniprot.org/annotation/VAR_023489|||http://purl.uniprot.org/annotation/VAR_023490|||http://purl.uniprot.org/annotation/VAR_023491|||http://purl.uniprot.org/annotation/VAR_023492|||http://purl.uniprot.org/annotation/VAR_023493|||http://purl.uniprot.org/annotation/VAR_023494|||http://purl.uniprot.org/annotation/VAR_023495|||http://purl.uniprot.org/annotation/VAR_023496
http://togogenome.org/gene/9606:KRTAP8-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  12 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 8-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185185
http://togogenome.org/gene/9606:PPP1R12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E1CKY7|||http://purl.uniprot.org/uniprot/O60237                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 12B|||cGMP-dependent protein kinase interacting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067028|||http://purl.uniprot.org/annotation/VAR_017480|||http://purl.uniprot.org/annotation/VAR_024177|||http://purl.uniprot.org/annotation/VSP_009256|||http://purl.uniprot.org/annotation/VSP_009257|||http://purl.uniprot.org/annotation/VSP_009258|||http://purl.uniprot.org/annotation/VSP_009259|||http://purl.uniprot.org/annotation/VSP_043159|||http://purl.uniprot.org/annotation/VSP_043160|||http://purl.uniprot.org/annotation/VSP_059344
http://togogenome.org/gene/9606:ATAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PL18                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 2|||Acidic residues|||Basic and acidic residues|||Bromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with Q-532.|||Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with T-473.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084796|||http://purl.uniprot.org/annotation/VAR_047625|||http://purl.uniprot.org/annotation/VSP_015633|||http://purl.uniprot.org/annotation/VSP_015634|||http://purl.uniprot.org/annotation/VSP_015635
http://togogenome.org/gene/9606:ADI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV57                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acireductone dioxygenase|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of aci-reductone dioxygenase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162942|||http://purl.uniprot.org/annotation/VSP_015822
http://togogenome.org/gene/9606:RPS10-NUDT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQS6                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nudix hydrolase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:OR52E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGJ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150772|||http://purl.uniprot.org/annotation/VAR_053332|||http://purl.uniprot.org/annotation/VAR_053333|||http://purl.uniprot.org/annotation/VAR_053334
http://togogenome.org/gene/9606:ALCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNN9|||http://purl.uniprot.org/uniprot/Q13740                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD166 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014659|||http://purl.uniprot.org/annotation/PRO_5002788623|||http://purl.uniprot.org/annotation/VAR_003907|||http://purl.uniprot.org/annotation/VAR_003908|||http://purl.uniprot.org/annotation/VAR_029514|||http://purl.uniprot.org/annotation/VAR_029515|||http://purl.uniprot.org/annotation/VAR_029516|||http://purl.uniprot.org/annotation/VAR_049856|||http://purl.uniprot.org/annotation/VSP_021797|||http://purl.uniprot.org/annotation/VSP_053529|||http://purl.uniprot.org/annotation/VSP_053530|||http://purl.uniprot.org/annotation/VSP_053531|||http://purl.uniprot.org/annotation/VSP_053532
http://togogenome.org/gene/9606:GAL3ST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3Q3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Galactose-3-O-sulfotransferase 2|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085203|||http://purl.uniprot.org/annotation/VAR_047060
http://togogenome.org/gene/9606:DACT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SW24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Dapper homolog 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ-binding|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326199|||http://purl.uniprot.org/annotation/VAR_059969|||http://purl.uniprot.org/annotation/VAR_059970|||http://purl.uniprot.org/annotation/VSP_032595|||http://purl.uniprot.org/annotation/VSP_032596|||http://purl.uniprot.org/annotation/VSP_032597|||http://purl.uniprot.org/annotation/VSP_032598
http://togogenome.org/gene/9606:ARAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96P48                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Arf-GAP|||Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1|||C4-type|||Disordered|||In isoform 1 and isoform 2.|||In isoform 2, isoform 3, isoform 5 and isoform 7.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 7.|||PH 1|||PH 2|||PH 3|||PH 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Ras-associating|||Rho-GAP|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074214|||http://purl.uniprot.org/annotation/VAR_055529|||http://purl.uniprot.org/annotation/VAR_061023|||http://purl.uniprot.org/annotation/VSP_000311|||http://purl.uniprot.org/annotation/VSP_014998|||http://purl.uniprot.org/annotation/VSP_015000|||http://purl.uniprot.org/annotation/VSP_015001|||http://purl.uniprot.org/annotation/VSP_036607|||http://purl.uniprot.org/annotation/VSP_036608|||http://purl.uniprot.org/annotation/VSP_043530
http://togogenome.org/gene/9606:SLC22A18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PRM7|||http://purl.uniprot.org/uniprot/Q96BI1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a rhabdomyosarcoma sample.|||In lung cancer; somatic mutation.|||Solute carrier family 22 member 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220509|||http://purl.uniprot.org/annotation/VAR_024061|||http://purl.uniprot.org/annotation/VAR_024062|||http://purl.uniprot.org/annotation/VAR_024063|||http://purl.uniprot.org/annotation/VAR_055406|||http://purl.uniprot.org/annotation/VAR_055407|||http://purl.uniprot.org/annotation/VAR_055408
http://togogenome.org/gene/9606:PITX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78337|||http://purl.uniprot.org/uniprot/X5D9A5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In CCF; reduces the ability to transactivate a luciferase reporter gene; suppresses wild-type activity in a dose-dependent manner.|||Interaction with PIT-1|||N-acetylmethionine|||Nuclear localization signal|||OAR|||Phosphoserine|||Pituitary homeobox 1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049218|||http://purl.uniprot.org/annotation/VAR_049586|||http://purl.uniprot.org/annotation/VAR_058113
http://togogenome.org/gene/9606:ZNF83                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQJ6|||http://purl.uniprot.org/uniprot/P51522                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||Zinc finger protein 83                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047396|||http://purl.uniprot.org/annotation/VAR_058206|||http://purl.uniprot.org/annotation/VAR_058207|||http://purl.uniprot.org/annotation/VAR_058208|||http://purl.uniprot.org/annotation/VAR_058209|||http://purl.uniprot.org/annotation/VSP_037663
http://togogenome.org/gene/9606:CMTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PAX0|||http://purl.uniprot.org/uniprot/Q8IZ96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  CKLF-like MARVEL transmembrane domain-containing protein 1|||Disordered|||Helical|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 14.|||In isoform 16.|||In isoform 1a, isoform 1b and isoform 19.|||In isoform 1b, isoform 2 and isoform 5.|||In isoform 2 and isoform 5.|||In isoform 24.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 6.|||In isoform 8 and isoform 19.|||MARVEL|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186097|||http://purl.uniprot.org/annotation/VAR_053039|||http://purl.uniprot.org/annotation/VSP_008229|||http://purl.uniprot.org/annotation/VSP_008230|||http://purl.uniprot.org/annotation/VSP_008231|||http://purl.uniprot.org/annotation/VSP_008232|||http://purl.uniprot.org/annotation/VSP_008233|||http://purl.uniprot.org/annotation/VSP_008234|||http://purl.uniprot.org/annotation/VSP_008235|||http://purl.uniprot.org/annotation/VSP_008236|||http://purl.uniprot.org/annotation/VSP_008237|||http://purl.uniprot.org/annotation/VSP_008238|||http://purl.uniprot.org/annotation/VSP_008239|||http://purl.uniprot.org/annotation/VSP_008240|||http://purl.uniprot.org/annotation/VSP_008241|||http://purl.uniprot.org/annotation/VSP_008242|||http://purl.uniprot.org/annotation/VSP_008243|||http://purl.uniprot.org/annotation/VSP_008244|||http://purl.uniprot.org/annotation/VSP_008245|||http://purl.uniprot.org/annotation/VSP_008246|||http://purl.uniprot.org/annotation/VSP_008247|||http://purl.uniprot.org/annotation/VSP_008248|||http://purl.uniprot.org/annotation/VSP_008249|||http://purl.uniprot.org/annotation/VSP_008250|||http://purl.uniprot.org/annotation/VSP_008251|||http://purl.uniprot.org/annotation/VSP_008252|||http://purl.uniprot.org/annotation/VSP_043579
http://togogenome.org/gene/9606:HCRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43612                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In NRCLP1; early-onset; impaired trafficking and processing.|||Leucine amide|||Methionine amide|||Orexin-A|||Orexin-B|||Pyrrolidone carboxylic acid|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020261|||http://purl.uniprot.org/annotation/PRO_0000020262|||http://purl.uniprot.org/annotation/PRO_0000020263|||http://purl.uniprot.org/annotation/VAR_011633
http://togogenome.org/gene/9606:DEFB106B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N104                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Peptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Peptide|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Beta-defensin 106                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006977
http://togogenome.org/gene/9606:DNAJB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25686                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CAAX motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily B member 2|||In DSMA5.|||In isoform 2.|||J|||Loss of interaction with HSP70 and loss of the ability to promote ATXN3 proteasomal degradation.|||Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-222 and A-262.|||Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-222 and A-265.|||Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-219; A-262 and A-265.|||Loss of interaction with polyubiquitin chains, loss of interaction with PSMA3, and loss of the ability to protect ATXN3 from proteasomal degradation; when associated with A-222; A-262 and A-265.|||Loss of localization to the endoplasmic reticulum and relocalization to cytoplasm and nucleus.|||N-acetylalanine|||No effect on localization to the endoplasmic reticulum membrane.|||Phosphoserine|||Polar residues|||Probable loss of interaction with HSP70 and loss of the ability to reduce PRKN aggregation.|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine|||UIM 1|||UIM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071018|||http://purl.uniprot.org/annotation/PRO_0000438687|||http://purl.uniprot.org/annotation/VAR_048910|||http://purl.uniprot.org/annotation/VAR_073286|||http://purl.uniprot.org/annotation/VSP_001286|||http://purl.uniprot.org/annotation/VSP_001287
http://togogenome.org/gene/9606:EIF4E1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EIF4EBP1/2/3 binding|||Eukaryotic translation initiation factor 4E type 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342513|||http://purl.uniprot.org/annotation/VAR_044209
http://togogenome.org/gene/9606:MEOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50222                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes DNA-binding. Does not affect ability to activate expression of CDKN2A.|||Basic and acidic residues|||Basic residues|||Disordered|||Homeobox|||Homeobox protein MOX-2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049197|||http://purl.uniprot.org/annotation/VAR_026040|||http://purl.uniprot.org/annotation/VAR_026041|||http://purl.uniprot.org/annotation/VAR_049585
http://togogenome.org/gene/9606:ND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03891|||http://purl.uniprot.org/uniprot/Q7GXY9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In AD-MT.|||In LHON; rare primary mutation.|||In LHON; secondary mutation; does not seem to directly cause the disease.|||In LS; unknown pathological significance; decrease in enzyme activity and impaired assembly of complex I.|||NADH dehydrogenase subunit 2 C-terminal|||NADH-ubiquinone oxidoreductase chain 2|||NADH:quinone oxidoreductase/Mrp antiporter membrane subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117595|||http://purl.uniprot.org/annotation/VAR_004755|||http://purl.uniprot.org/annotation/VAR_004756|||http://purl.uniprot.org/annotation/VAR_004757|||http://purl.uniprot.org/annotation/VAR_004758|||http://purl.uniprot.org/annotation/VAR_008590|||http://purl.uniprot.org/annotation/VAR_008591|||http://purl.uniprot.org/annotation/VAR_008592|||http://purl.uniprot.org/annotation/VAR_008593|||http://purl.uniprot.org/annotation/VAR_008594|||http://purl.uniprot.org/annotation/VAR_008595|||http://purl.uniprot.org/annotation/VAR_008596|||http://purl.uniprot.org/annotation/VAR_008597|||http://purl.uniprot.org/annotation/VAR_011348|||http://purl.uniprot.org/annotation/VAR_011349|||http://purl.uniprot.org/annotation/VAR_011350|||http://purl.uniprot.org/annotation/VAR_011351|||http://purl.uniprot.org/annotation/VAR_011352|||http://purl.uniprot.org/annotation/VAR_011353|||http://purl.uniprot.org/annotation/VAR_011354|||http://purl.uniprot.org/annotation/VAR_011355|||http://purl.uniprot.org/annotation/VAR_011356|||http://purl.uniprot.org/annotation/VAR_084383
http://togogenome.org/gene/9606:SSX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60225                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||KRAB-related|||Polar residues|||Protein SSX5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181832|||http://purl.uniprot.org/annotation/VAR_027805|||http://purl.uniprot.org/annotation/VSP_006274
http://togogenome.org/gene/9606:SMYD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PHG3|||http://purl.uniprot.org/uniprot/Q5HYE8|||http://purl.uniprot.org/uniprot/Q8NB12                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Histone-lysine N-methyltransferase SMYD1|||MYND-type|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218307|||http://purl.uniprot.org/annotation/VAR_052990
http://togogenome.org/gene/9606:ODAD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8V7|||http://purl.uniprot.org/uniprot/B3KPH7|||http://purl.uniprot.org/uniprot/K7EN59                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Outer dynein arm-docking complex subunit 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321526|||http://purl.uniprot.org/annotation/VAR_050743|||http://purl.uniprot.org/annotation/VSP_056903
http://togogenome.org/gene/9606:CHIC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKJ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Site                                                                                  ^@                                                                                  Breakpoint for translocation to form CHIC2-ETV6 in AML|||CHIC motif (Cys-rich)|||Cysteine-rich hydrophobic domain-containing protein 2|||Loss of palmitoylation. Abolishes membrane association.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189556
http://togogenome.org/gene/9606:CAND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Cullin-associated NEDD8-dissociated protein 1|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 21|||HEAT 22|||HEAT 23|||HEAT 24|||HEAT 25|||HEAT 26|||HEAT 27|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089293|||http://purl.uniprot.org/annotation/VAR_025327|||http://purl.uniprot.org/annotation/VAR_054041|||http://purl.uniprot.org/annotation/VSP_013947|||http://purl.uniprot.org/annotation/VSP_013948|||http://purl.uniprot.org/annotation/VSP_013949|||http://purl.uniprot.org/annotation/VSP_013950
http://togogenome.org/gene/9606:PANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE04                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Loss of nuclear localization.|||Nucleolar localization signal|||Pantothenate kinase 1|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161802|||http://purl.uniprot.org/annotation/VSP_004520|||http://purl.uniprot.org/annotation/VSP_004521|||http://purl.uniprot.org/annotation/VSP_012823|||http://purl.uniprot.org/annotation/VSP_012824
http://togogenome.org/gene/9606:SYTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with RAB27A.|||Basic and acidic residues|||C2 1|||C2 2|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4, isoform 8 and isoform 12.|||In isoform 4, isoform 6, isoform 8 and isoform 11.|||In isoform 5, isoform 6 and isoform 8.|||In isoform 7.|||In isoform 9.|||Polar residues|||RabBD|||Synaptotagmin-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190213|||http://purl.uniprot.org/annotation/VAR_082906|||http://purl.uniprot.org/annotation/VAR_082907|||http://purl.uniprot.org/annotation/VSP_007885|||http://purl.uniprot.org/annotation/VSP_019004|||http://purl.uniprot.org/annotation/VSP_037896|||http://purl.uniprot.org/annotation/VSP_037899|||http://purl.uniprot.org/annotation/VSP_037900|||http://purl.uniprot.org/annotation/VSP_037901|||http://purl.uniprot.org/annotation/VSP_037902|||http://purl.uniprot.org/annotation/VSP_037904|||http://purl.uniprot.org/annotation/VSP_037905|||http://purl.uniprot.org/annotation/VSP_037906
http://togogenome.org/gene/9606:TMEM144                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5S9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 144                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288971|||http://purl.uniprot.org/annotation/VAR_032544|||http://purl.uniprot.org/annotation/VSP_025850|||http://purl.uniprot.org/annotation/VSP_025851
http://togogenome.org/gene/9606:NECTIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15223                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||Impairs interaction with herpes simplex glycoprotein D. Decreases susceptibility to infection by herpes simplex virus.|||In isoform Alpha.|||In isoform Gamma.|||Interaction with FGFR|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Nectin-1|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015133|||http://purl.uniprot.org/annotation/VSP_002624|||http://purl.uniprot.org/annotation/VSP_002625|||http://purl.uniprot.org/annotation/VSP_002626|||http://purl.uniprot.org/annotation/VSP_002627
http://togogenome.org/gene/9606:TRIM21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19474                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM21|||In isoform 2.|||Loss of E3 ubiquitin-protein ligase activity. Does not inhibit NF-kappa-B-induced gene expression. Loss of E3 ubiquitin-protein ligase activity; when associated with 31-A--A-33.|||Loss of E3 ubiquitin-protein ligase activity; when associated with A-16.|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056115|||http://purl.uniprot.org/annotation/VAR_013749|||http://purl.uniprot.org/annotation/VAR_013750|||http://purl.uniprot.org/annotation/VAR_013751|||http://purl.uniprot.org/annotation/VAR_061821|||http://purl.uniprot.org/annotation/VSP_039627
http://togogenome.org/gene/9606:C2orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCI8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Uncharacterized protein C2orf78                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319422
http://togogenome.org/gene/9606:IER3IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5U9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Immediate early response 3-interacting protein 1|||In MEDS1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257961|||http://purl.uniprot.org/annotation/VAR_066569|||http://purl.uniprot.org/annotation/VAR_066570
http://togogenome.org/gene/9606:CHRNA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15825                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with receptor activation|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000360|||http://purl.uniprot.org/annotation/VAR_048171|||http://purl.uniprot.org/annotation/VSP_042713
http://togogenome.org/gene/9606:LONRF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2D3|||http://purl.uniprot.org/uniprot/B3KUN7|||http://purl.uniprot.org/uniprot/Q496Y0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||LON peptidase N-terminal domain and RING finger protein 3|||Lon N-terminal|||Polar residues|||RING-type|||RING-type 1|||RING-type 2|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277671|||http://purl.uniprot.org/annotation/VAR_035954|||http://purl.uniprot.org/annotation/VSP_023080|||http://purl.uniprot.org/annotation/VSP_023081|||http://purl.uniprot.org/annotation/VSP_023082
http://togogenome.org/gene/9606:HSBP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JCN9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict                                                                                  ^@                                                                                  Heat shock factor-binding protein 1-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394662
http://togogenome.org/gene/9606:ADAMTSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZQ3|||http://purl.uniprot.org/uniprot/Q8N6G6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mass|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  ADAMTS-like protein 1|||Abolishes N-glycosylation. Reduces secretion of ADAMTSL1.|||Abolishes secretion of ADAMTSL1.|||C-linked (Man) tryptophan|||Disordered|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Modest reduction in secretion of ADAMTSL1.|||N-linked (GlcNAc...) asparagine|||No effect on secretion of ADAMTSL1.|||Not glycosylated|||O-linked (Fuc...) serine|||O-linked (Fuc...) threonine|||PLAC|||Polar residues|||Significant reduction in secretion of ADAMTSL1.|||Small increase in secretion of ADAMTSL1. About 40% increase in secretion of ADAMTSL1; when associated with A-312. Dramatic increase in secretion of ADAMTSL1; when associated with A-312 and A-451.|||Small increase in secretion of ADAMTSL1. About 40% increase in secretion of ADAMTSL1; when associated with A-391. Dramatic increase in secretion of ADAMTSL1; when associated with A-391 and A-451.|||Small increase in secretion of ADAMTSL1. Dramatic increase in secretion of ADAMTSL1; when associated with A-312 and A-391.|||Small reduction in secretion of ADAMTSL1.|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9|||The measured range is 28-525.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035860|||http://purl.uniprot.org/annotation/VAR_017174|||http://purl.uniprot.org/annotation/VSP_039322|||http://purl.uniprot.org/annotation/VSP_039323|||http://purl.uniprot.org/annotation/VSP_039324|||http://purl.uniprot.org/annotation/VSP_039325|||http://purl.uniprot.org/annotation/VSP_039326|||http://purl.uniprot.org/annotation/VSP_039327|||http://purl.uniprot.org/annotation/VSP_039328|||http://purl.uniprot.org/annotation/VSP_039329|||http://purl.uniprot.org/annotation/VSP_039330|||http://purl.uniprot.org/annotation/VSP_039331
http://togogenome.org/gene/9606:WNT7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00755                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered linker|||Does not affect interaction with RECK.|||In 4A; abolished interaction with RECK; when associated with 251-A-A-252 and A-262.|||In 4A; abolished interaction with RECK; when associated with A-241 and 251-A-A-252.|||In 4A; abolished interaction with RECK; when associated with A-241 and A-262.|||In FUHRS; retains activity that is significant but not comparable to wild-type activity.|||In LPHAS.|||In LPHAS; results in a loss of function mutation with some residual activity.|||In LPHAS; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-7a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041442|||http://purl.uniprot.org/annotation/VAR_030673|||http://purl.uniprot.org/annotation/VAR_030674|||http://purl.uniprot.org/annotation/VAR_064480|||http://purl.uniprot.org/annotation/VAR_065765|||http://purl.uniprot.org/annotation/VAR_077340
http://togogenome.org/gene/9606:ILKAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0C8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Integrin-linked kinase-associated serine/threonine phosphatase 2C|||Loss of >90% of activity.|||N-acetylmethionine|||N6-acetyllysine|||PPM-type phosphatase|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272271|||http://purl.uniprot.org/annotation/VAR_061542
http://togogenome.org/gene/9606:FEZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHY8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fasciculation and elongation protein zeta-2|||In isoform 2.|||Interchain|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189528|||http://purl.uniprot.org/annotation/VAR_053771|||http://purl.uniprot.org/annotation/VAR_053772|||http://purl.uniprot.org/annotation/VSP_041368
http://togogenome.org/gene/9606:RNF19B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMZ0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF19B|||Helical|||IBR-type|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||Polar residues|||Pro residues|||RING-type 1|||RING-type 2; atypical|||Required for ubiquitin ligase activity and for protection against staurosporin-induced cell death|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084129|||http://purl.uniprot.org/annotation/VSP_028632|||http://purl.uniprot.org/annotation/VSP_028633|||http://purl.uniprot.org/annotation/VSP_028634|||http://purl.uniprot.org/annotation/VSP_028635
http://togogenome.org/gene/9606:THTPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V5Q5|||http://purl.uniprot.org/uniprot/Q9BU02                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CYTH|||Decreases enzyme activity.|||In isoform 2.|||Mildly decreases enzyme activity.|||N-acetylalanine|||Removed|||Strongly decreases affinity for thiamine triphosphate and enzyme activity.|||Strongly decreases enzyme activity. No effect on affinity for thiamine triphosphate.|||Thiamine-triphosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221490|||http://purl.uniprot.org/annotation/VAR_062152|||http://purl.uniprot.org/annotation/VSP_047213|||http://purl.uniprot.org/annotation/VSP_047214
http://togogenome.org/gene/9606:ADGRF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor F4|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070336|||http://purl.uniprot.org/annotation/VAR_024476|||http://purl.uniprot.org/annotation/VAR_036224|||http://purl.uniprot.org/annotation/VAR_055930
http://togogenome.org/gene/9606:RNF214                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING finger protein 214|||RING-type; atypical|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280546|||http://purl.uniprot.org/annotation/VSP_054566
http://togogenome.org/gene/9606:PADI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULC6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Nucleophile|||Protein-arginine deiminase type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220023|||http://purl.uniprot.org/annotation/VAR_053557
http://togogenome.org/gene/9606:ATG13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0S6|||http://purl.uniprot.org/uniprot/O75143                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ATG101; when associated with D-133.|||Abolishes interaction with ATG101; when associated with H-127.|||Autophagy-related protein 13|||Autophagy-related protein 13 N-terminal|||Decreases interaction with ATG101; when associated with D-131.|||Decreases interaction with ATG101; when associated with D-134.|||Decreases interaction with MAP1LC3A.|||Disordered|||Important for interaction with ATG101|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIR|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by ULK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050767|||http://purl.uniprot.org/annotation/VSP_002431|||http://purl.uniprot.org/annotation/VSP_002432|||http://purl.uniprot.org/annotation/VSP_002433|||http://purl.uniprot.org/annotation/VSP_044503|||http://purl.uniprot.org/annotation/VSP_044504|||http://purl.uniprot.org/annotation/VSP_044640
http://togogenome.org/gene/9606:B4GALNT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L9W6|||http://purl.uniprot.org/uniprot/Q8N9V0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4-N-acetylgalactosaminyltransferase 3|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||PA14|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252368|||http://purl.uniprot.org/annotation/VAR_027842|||http://purl.uniprot.org/annotation/VAR_027843|||http://purl.uniprot.org/annotation/VAR_027844|||http://purl.uniprot.org/annotation/VAR_048717|||http://purl.uniprot.org/annotation/VAR_048718
http://togogenome.org/gene/9606:FAM89B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5H3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||In isoform 4.|||LRR|||Leucine repeat adapter protein 25|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271763|||http://purl.uniprot.org/annotation/VSP_045015|||http://purl.uniprot.org/annotation/VSP_045016|||http://purl.uniprot.org/annotation/VSP_045631|||http://purl.uniprot.org/annotation/VSP_045632
http://togogenome.org/gene/9606:MTFR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5H6|||http://purl.uniprot.org/uniprot/Q9H019                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrial fission regulator 1-like|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341566|||http://purl.uniprot.org/annotation/VAR_044084|||http://purl.uniprot.org/annotation/VSP_034338|||http://purl.uniprot.org/annotation/VSP_034339
http://togogenome.org/gene/9606:FCRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LA6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fc receptor-like protein 1|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||ITIM motif 5|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331638|||http://purl.uniprot.org/annotation/VAR_042923|||http://purl.uniprot.org/annotation/VSP_033290|||http://purl.uniprot.org/annotation/VSP_033291|||http://purl.uniprot.org/annotation/VSP_033292|||http://purl.uniprot.org/annotation/VSP_033293|||http://purl.uniprot.org/annotation/VSP_033294|||http://purl.uniprot.org/annotation/VSP_033295
http://togogenome.org/gene/9606:PHRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM65|||http://purl.uniprot.org/uniprot/B7ZM66|||http://purl.uniprot.org/uniprot/E9PJ24|||http://purl.uniprot.org/uniprot/F8WEF5|||http://purl.uniprot.org/uniprot/Q9P1Y6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||PHD and RING finger domain-containing protein 1|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278266|||http://purl.uniprot.org/annotation/VAR_030727|||http://purl.uniprot.org/annotation/VAR_030728|||http://purl.uniprot.org/annotation/VAR_030729|||http://purl.uniprot.org/annotation/VSP_023247|||http://purl.uniprot.org/annotation/VSP_023248|||http://purl.uniprot.org/annotation/VSP_039187
http://togogenome.org/gene/9606:PLA2G7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13093                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activity is higher than wild-type.|||Almost no activity.|||Associated with asthma and atopy; retains the ability to associate with HDL particles.|||Charge relay system|||Diminishes activity.|||Impairs the association with HDL particles.|||Impairs the association with LDL particles.|||In PAFAD; loss of function.|||In PAFAD; loss of function; risk factor for coronary arthery disease and stroke.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||No change in activity.|||Nucleophile|||Platelet-activating factor acetylhydrolase|||Reduces the association with HDL particles.|||Reduces the association with LDL particles.|||Retains the ability to associate with HDL particles.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017833|||http://purl.uniprot.org/annotation/VAR_004268|||http://purl.uniprot.org/annotation/VAR_011583|||http://purl.uniprot.org/annotation/VAR_011584|||http://purl.uniprot.org/annotation/VAR_011585|||http://purl.uniprot.org/annotation/VAR_011586|||http://purl.uniprot.org/annotation/VAR_047970|||http://purl.uniprot.org/annotation/VAR_047971
http://togogenome.org/gene/9606:PYDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXC3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict                                                                                  ^@                                                                                  Pyrin|||Pyrin domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280593
http://togogenome.org/gene/9606:TRAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RD84|||http://purl.uniprot.org/uniprot/Q15035                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||TLC|||Translocating chain-associated membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185532
http://togogenome.org/gene/9606:EEF1AKMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPI9|||http://purl.uniprot.org/uniprot/Q8TC28|||http://purl.uniprot.org/uniprot/Q8WYV4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EEF1A lysine methyltransferase 2|||Highly reduces methylation activity toward EEF1A1.|||Methyltransferase|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325882|||http://purl.uniprot.org/annotation/VAR_050295
http://togogenome.org/gene/9606:ZNF34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG42|||http://purl.uniprot.org/uniprot/Q8IZ26                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Phosphoserine|||Polar residues|||Zinc finger protein 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047365
http://togogenome.org/gene/9606:C6orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5S2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Protein LEG1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252385|||http://purl.uniprot.org/annotation/VAR_033675
http://togogenome.org/gene/9606:CRELD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXH1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CXXC|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||FU 1|||FU 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Protein disulfide isomerase CRELD2|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256244|||http://purl.uniprot.org/annotation/VAR_028892|||http://purl.uniprot.org/annotation/VAR_028893|||http://purl.uniprot.org/annotation/VAR_028894|||http://purl.uniprot.org/annotation/VSP_021339|||http://purl.uniprot.org/annotation/VSP_021340|||http://purl.uniprot.org/annotation/VSP_021341|||http://purl.uniprot.org/annotation/VSP_021342|||http://purl.uniprot.org/annotation/VSP_021343|||http://purl.uniprot.org/annotation/VSP_021344
http://togogenome.org/gene/9606:SPATA21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z572                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330686|||http://purl.uniprot.org/annotation/VAR_042711|||http://purl.uniprot.org/annotation/VAR_042712|||http://purl.uniprot.org/annotation/VAR_042713|||http://purl.uniprot.org/annotation/VAR_042714|||http://purl.uniprot.org/annotation/VAR_042715|||http://purl.uniprot.org/annotation/VSP_053865
http://togogenome.org/gene/9606:CLCN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51797                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation; when associated with A-410 and A-422.|||Abolishes N-glycosylation; when associated with A-410 and A-432.|||Abolishes N-glycosylation; when associated with A-422 and A-432.|||Abolishes proton transport, but not chloride transport. Strongly increases anion current; when associated with S-576.|||CBS 1|||CBS 2|||Cytoplasmic|||H(+)/Cl(-) exchange transporter 6|||Helical|||In CONRIBA; strongly slowed gating and increased current amplitudes.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increases the nitrate/chloride conductance ratio.|||Loss of proton and chloride transport.|||Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport|||Mediates proton transfer from the protein to the inner aqueous phase|||N-linked (GlcNAc...) asparagine|||Note=Loop between two helices|||Phosphoserine|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3|||Strongly increases anion current; when associated with A-200.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094449|||http://purl.uniprot.org/annotation/VAR_023051|||http://purl.uniprot.org/annotation/VAR_085384|||http://purl.uniprot.org/annotation/VSP_001043|||http://purl.uniprot.org/annotation/VSP_001044|||http://purl.uniprot.org/annotation/VSP_001045|||http://purl.uniprot.org/annotation/VSP_001046|||http://purl.uniprot.org/annotation/VSP_001047|||http://purl.uniprot.org/annotation/VSP_001048|||http://purl.uniprot.org/annotation/VSP_017188|||http://purl.uniprot.org/annotation/VSP_047169
http://togogenome.org/gene/9606:HECTD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4G1|||http://purl.uniprot.org/uniprot/B3KU34|||http://purl.uniprot.org/uniprot/Q5T447                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  DOC|||E3 ubiquitin-protein ligase HECTD3|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Loss of ubiquitin-ligase activity.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000241445|||http://purl.uniprot.org/annotation/VSP_019439|||http://purl.uniprot.org/annotation/VSP_019440
http://togogenome.org/gene/9606:HMGCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL2|||http://purl.uniprot.org/uniprot/P54868                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Hydroxymethylglutaryl-CoA synthase, mitochondrial|||Hydroxymethylglutaryl-coenzyme A synthase C-terminal|||Hydroxymethylglutaryl-coenzyme A synthase N-terminal|||In HMGCS2D.|||In HMGCS2D; abolished enzymatic activity.|||In HMGCS2D; abolished protein expression.|||In HMGCS2D; decreased protein abundance; abolished enzymatic activity.|||In HMGCS2D; decreased protein abundance; abolished enzymatic activity; requires 2 nucleotide substitutions.|||In HMGCS2D; decreased protein abundance; stong reduction of enzymatic activity.|||In HMGCS2D; reduced peptide level; strong reduction of enzymatic activity.|||In HMGCS2D; strong decreased of protein expression; abolished enzymatic activity.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013483|||http://purl.uniprot.org/annotation/VAR_032711|||http://purl.uniprot.org/annotation/VAR_032757|||http://purl.uniprot.org/annotation/VAR_032758|||http://purl.uniprot.org/annotation/VAR_032759|||http://purl.uniprot.org/annotation/VAR_032760|||http://purl.uniprot.org/annotation/VAR_083500|||http://purl.uniprot.org/annotation/VAR_083501|||http://purl.uniprot.org/annotation/VAR_083502|||http://purl.uniprot.org/annotation/VAR_083503|||http://purl.uniprot.org/annotation/VAR_083504|||http://purl.uniprot.org/annotation/VAR_083505|||http://purl.uniprot.org/annotation/VAR_083506|||http://purl.uniprot.org/annotation/VAR_083507|||http://purl.uniprot.org/annotation/VAR_083508|||http://purl.uniprot.org/annotation/VAR_083509|||http://purl.uniprot.org/annotation/VAR_083510|||http://purl.uniprot.org/annotation/VAR_083511|||http://purl.uniprot.org/annotation/VAR_083512|||http://purl.uniprot.org/annotation/VAR_083513|||http://purl.uniprot.org/annotation/VAR_083514|||http://purl.uniprot.org/annotation/VSP_042892|||http://purl.uniprot.org/annotation/VSP_047445
http://togogenome.org/gene/9606:CFAP97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2B7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 97|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309224|||http://purl.uniprot.org/annotation/VAR_036915|||http://purl.uniprot.org/annotation/VAR_036916|||http://purl.uniprot.org/annotation/VSP_029098|||http://purl.uniprot.org/annotation/VSP_029099
http://togogenome.org/gene/9606:TMEM254                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZM8|||http://purl.uniprot.org/uniprot/B4DU43|||http://purl.uniprot.org/uniprot/Q8TBM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed|||Transmembrane protein 254                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089796|||http://purl.uniprot.org/annotation/VSP_047062|||http://purl.uniprot.org/annotation/VSP_047063
http://togogenome.org/gene/9606:ACOX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15254                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Microbody targeting signal|||N-acetylalanine|||Peroxisomal acyl-coenzyme A oxidase 3|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204685|||http://purl.uniprot.org/annotation/VAR_030802|||http://purl.uniprot.org/annotation/VAR_030803|||http://purl.uniprot.org/annotation/VSP_023355|||http://purl.uniprot.org/annotation/VSP_023356
http://togogenome.org/gene/9606:NDUFB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX14                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Found in a patient with histiocytoid cardiomyopathy; unknown pathological significance.|||Helical|||In MC1DN30.|||In isoform 2.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020057|||http://purl.uniprot.org/annotation/VAR_076277|||http://purl.uniprot.org/annotation/VAR_078941|||http://purl.uniprot.org/annotation/VAR_078942|||http://purl.uniprot.org/annotation/VSP_018251
http://togogenome.org/gene/9606:EXOC6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRB6|||http://purl.uniprot.org/uniprot/Q9Y2D4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Exocyst complex component 6B|||Exocyst complex subunit Sec15 C-terminal|||In SEMDJL3; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118954|||http://purl.uniprot.org/annotation/VAR_082175|||http://purl.uniprot.org/annotation/VSP_040838|||http://purl.uniprot.org/annotation/VSP_040839
http://togogenome.org/gene/9606:HARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDN8|||http://purl.uniprot.org/uniprot/P49590                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Anticodon-binding|||Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core|||Histidine--tRNA ligase, mitochondrial|||In PRLTS2; the mutant protein is expressed, can dimerize and localizes to the mitochondria; has significantly decreased enzymatic activity compared to wild-type.|||In PRLTS2; unknown pathological significance.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136336|||http://purl.uniprot.org/annotation/VAR_069532|||http://purl.uniprot.org/annotation/VAR_069533|||http://purl.uniprot.org/annotation/VAR_083046|||http://purl.uniprot.org/annotation/VAR_083047|||http://purl.uniprot.org/annotation/VAR_083048|||http://purl.uniprot.org/annotation/VAR_083049|||http://purl.uniprot.org/annotation/VAR_083050|||http://purl.uniprot.org/annotation/VSP_055133
http://togogenome.org/gene/9606:ROM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03395                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In patients with macular dysfunction; macular dysfunction severity is influenced by the presence of a W-172 mutation in PRPH2..|||Lumenal|||Rod outer segment membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168111|||http://purl.uniprot.org/annotation/VAR_006896|||http://purl.uniprot.org/annotation/VAR_006897|||http://purl.uniprot.org/annotation/VAR_006898|||http://purl.uniprot.org/annotation/VAR_006899|||http://purl.uniprot.org/annotation/VAR_006900|||http://purl.uniprot.org/annotation/VAR_008269|||http://purl.uniprot.org/annotation/VAR_008270|||http://purl.uniprot.org/annotation/VAR_008271|||http://purl.uniprot.org/annotation/VAR_008272
http://togogenome.org/gene/9606:ARL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6T311                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 9|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207475|||http://purl.uniprot.org/annotation/VSP_055413
http://togogenome.org/gene/9606:KCTD20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5Y7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD20|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255248|||http://purl.uniprot.org/annotation/VAR_028854|||http://purl.uniprot.org/annotation/VSP_021277|||http://purl.uniprot.org/annotation/VSP_021278|||http://purl.uniprot.org/annotation/VSP_055669
http://togogenome.org/gene/9606:FAM81A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBF8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict                                                                                  ^@                                                                                  Protein FAM81A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265119
http://togogenome.org/gene/9606:OR2T3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVW5|||http://purl.uniprot.org/uniprot/Q8NH03                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150498|||http://purl.uniprot.org/annotation/VAR_053151
http://togogenome.org/gene/9606:RAB5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20339                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Disordered|||Effector region|||In isoform 2.|||Increased interaction wih ATP9A.|||Loss of GTPase activity. Does not inhibit filopodia formation.|||Loss of phosphorylation. No effect on GDI1 and GDI2 binding.|||No effect on RABEP1 binding affinity.|||Phosphomimetic mutant. Loss of GDI1 and GDI2 binding.|||Phosphoserine; by LRRK2|||Ras-related protein Rab-5A|||S-geranylgeranyl cysteine|||Strongly decreases RABEP1 and ZFYVE20 binding affinity.|||Strongly decreases RABEP1 binding affinity.|||Strongly decreases RABEP1 binding affinity. Impairs endosome fusion.|||Strongly decreases ZFYVE20 binding affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121104|||http://purl.uniprot.org/annotation/VSP_055830
http://togogenome.org/gene/9606:SIX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15475                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX1|||In BOR; uncertain pathological significance.|||In BOS3.|||In BOS3; crucial for DNA binding and transcription factor activity.|||In BOS3; crucial for interaction with EYA1 and EYA2 and transcription factor activity.|||In BOS3; crucial for interaction with EYA1, DNA binding and transcription factor activity.|||In BOS3; crucial for protein stability, DNA binding and transcription factor activity.|||In DFNA23; in addition to deafness the patient had renal anomalies suggesting a branchiootorenal syndrome; crucial for interaction with EYA1, DNA binding and transcription factor activity.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049295|||http://purl.uniprot.org/annotation/VAR_031024|||http://purl.uniprot.org/annotation/VAR_031025|||http://purl.uniprot.org/annotation/VAR_031026|||http://purl.uniprot.org/annotation/VAR_064948|||http://purl.uniprot.org/annotation/VAR_064949|||http://purl.uniprot.org/annotation/VAR_064950|||http://purl.uniprot.org/annotation/VAR_064951|||http://purl.uniprot.org/annotation/VAR_064952|||http://purl.uniprot.org/annotation/VAR_064953|||http://purl.uniprot.org/annotation/VAR_064954|||http://purl.uniprot.org/annotation/VAR_067446
http://togogenome.org/gene/9606:GALNT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCL4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 6|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059114|||http://purl.uniprot.org/annotation/VAR_019580
http://togogenome.org/gene/9606:CLPSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUU4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Colipase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337013|||http://purl.uniprot.org/annotation/VAR_043560
http://togogenome.org/gene/9606:TRAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY2|||http://purl.uniprot.org/uniprot/Q12931|||http://purl.uniprot.org/uniprot/Q53FS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Heat shock protein 75 kDa, mitochondrial|||Histidine kinase/HSP90-like ATPase|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013604|||http://purl.uniprot.org/annotation/VAR_016108|||http://purl.uniprot.org/annotation/VAR_049625|||http://purl.uniprot.org/annotation/VAR_049626|||http://purl.uniprot.org/annotation/VAR_061272|||http://purl.uniprot.org/annotation/VSP_055061
http://togogenome.org/gene/9606:EPPIN-WFDC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95925                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-123.|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-127.|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-123 and A-127.|||Eppin|||In isoform 2.|||In isoform 3.|||Interaction with LTF|||Interaction with SEMG1|||Loss of effect on KLK3 activity.|||Reduces the binding to SEMG1 by 45%.|||Reduces the binding to SEMG1 by 68% and to LTF by 73%.|||Reduces the binding to SEMG1 by 68%.|||WAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041378|||http://purl.uniprot.org/annotation/VAR_024696|||http://purl.uniprot.org/annotation/VAR_052950|||http://purl.uniprot.org/annotation/VSP_006755|||http://purl.uniprot.org/annotation/VSP_043679
http://togogenome.org/gene/9606:PIGT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969N2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased function in GPI-anchor attachment to protein.|||GPI transamidase component PIG-T|||Helical|||In MCAHS3.|||In MCAHS3; decreased function in GPI-anchor attachment to protein.|||In MCAHS3; decreased function in GPI-anchor attachment to protein; does not rescue GPI-anchored CD59 surface expression as efficiently as the wild-type in PIGT-knockout cells.|||In MCAHS3; decreased function in GPI-anchor attachment to protein; does not rescue GPI-anchored proteins surface expression as efficiently as the wild-type in PIGT-knockout cells.|||In MCAHS3; decreased function in GPI-anchor attachment to protein; flow cytometric analysis of patient granulocytes and monocytes show decreased amounts of GPI-anchored proteins CD16B and CD59 compared to controls.|||In MCAHS3; decreased function in GPI-anchor attachment to protein; reduced amounts of GPI-anchored proteins in homozygous patient cells.|||In MCAHS3; loss of function in GPI-anchor attachment to protein.|||In MCAHS3; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interchain (with C-92 in PIGK/GPI8)|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on function in GPI-anchor attachment to protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024107|||http://purl.uniprot.org/annotation/VAR_053583|||http://purl.uniprot.org/annotation/VAR_070448|||http://purl.uniprot.org/annotation/VAR_088155|||http://purl.uniprot.org/annotation/VAR_088156|||http://purl.uniprot.org/annotation/VAR_088157|||http://purl.uniprot.org/annotation/VAR_088158|||http://purl.uniprot.org/annotation/VAR_088159|||http://purl.uniprot.org/annotation/VAR_088160|||http://purl.uniprot.org/annotation/VAR_088161|||http://purl.uniprot.org/annotation/VAR_088162|||http://purl.uniprot.org/annotation/VAR_088163|||http://purl.uniprot.org/annotation/VAR_088164|||http://purl.uniprot.org/annotation/VAR_088165|||http://purl.uniprot.org/annotation/VAR_088166|||http://purl.uniprot.org/annotation/VAR_088167|||http://purl.uniprot.org/annotation/VAR_088168|||http://purl.uniprot.org/annotation/VAR_088169|||http://purl.uniprot.org/annotation/VAR_088170|||http://purl.uniprot.org/annotation/VAR_088171|||http://purl.uniprot.org/annotation/VAR_088172|||http://purl.uniprot.org/annotation/VAR_088173|||http://purl.uniprot.org/annotation/VSP_009536|||http://purl.uniprot.org/annotation/VSP_009537|||http://purl.uniprot.org/annotation/VSP_009538|||http://purl.uniprot.org/annotation/VSP_009539|||http://purl.uniprot.org/annotation/VSP_009540|||http://purl.uniprot.org/annotation/VSP_043167
http://togogenome.org/gene/9606:MCM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMX0|||http://purl.uniprot.org/uniprot/B4DLA6|||http://purl.uniprot.org/uniprot/P33991                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Arginine finger|||DNA replication licensing factor MCM4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MCM|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDC7|||Phosphothreonine|||Polar residues|||Reduced MCM complex DNA helicase activity. No effect on MCM complex formation. No effect on MCM complex ssDNA binding and ATPase activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194101|||http://purl.uniprot.org/annotation/VAR_020500|||http://purl.uniprot.org/annotation/VAR_020501
http://togogenome.org/gene/9606:GHRHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y6|||http://purl.uniprot.org/uniprot/Q02643                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Growth hormone-releasing hormone receptor|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In IGHD4.|||In IGHD4; reduced cAMP response to GHRH.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012828|||http://purl.uniprot.org/annotation/PRO_5010017639|||http://purl.uniprot.org/annotation/VAR_015796|||http://purl.uniprot.org/annotation/VAR_015797|||http://purl.uniprot.org/annotation/VAR_015798|||http://purl.uniprot.org/annotation/VAR_015799|||http://purl.uniprot.org/annotation/VAR_015800|||http://purl.uniprot.org/annotation/VAR_033962|||http://purl.uniprot.org/annotation/VAR_033963|||http://purl.uniprot.org/annotation/VAR_033964|||http://purl.uniprot.org/annotation/VAR_033965|||http://purl.uniprot.org/annotation/VAR_036223|||http://purl.uniprot.org/annotation/VAR_081172
http://togogenome.org/gene/9606:OR5P3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVE6|||http://purl.uniprot.org/uniprot/Q8WZ94                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5P3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150611|||http://purl.uniprot.org/annotation/VAR_048048|||http://purl.uniprot.org/annotation/VAR_048094
http://togogenome.org/gene/9606:RPP25L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5L8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Ribonuclease P protein subunit p25-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271032
http://togogenome.org/gene/9606:SHCBP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZQ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 4.|||N6-acetyllysine|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4|||Phosphoserine|||Testicular spindle-associated protein SHCBP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284838|||http://purl.uniprot.org/annotation/VAR_031836|||http://purl.uniprot.org/annotation/VSP_024673|||http://purl.uniprot.org/annotation/VSP_024676|||http://purl.uniprot.org/annotation/VSP_024677|||http://purl.uniprot.org/annotation/VSP_024678
http://togogenome.org/gene/9606:PIH1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWS0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to ECD, EFTUD2, RPB1, TELO2 and UBR5.|||Abolishes binding to TELO2.|||Abolishes binding to histone H4.|||In isoform 2.|||In isoform 3.|||Interacts with TELO2|||No effect on binding to histone H4.|||PIH1 domain-containing protein 1|||Phosphoserine|||Reduces binding to TELO2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307328|||http://purl.uniprot.org/annotation/VAR_035410|||http://purl.uniprot.org/annotation/VAR_035411|||http://purl.uniprot.org/annotation/VAR_035412|||http://purl.uniprot.org/annotation/VAR_035413|||http://purl.uniprot.org/annotation/VAR_035414|||http://purl.uniprot.org/annotation/VSP_044424|||http://purl.uniprot.org/annotation/VSP_044425
http://togogenome.org/gene/9606:PSMB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5LHX3|||http://purl.uniprot.org/uniprot/B3KVC3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nucleophile|||Proteasome subunit beta type-11|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300011|||http://purl.uniprot.org/annotation/PRO_0000300012|||http://purl.uniprot.org/annotation/VAR_051550
http://togogenome.org/gene/9606:DEFB115                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KQ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 115                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045343
http://togogenome.org/gene/9606:WDR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X295|||http://purl.uniprot.org/uniprot/B4E256|||http://purl.uniprot.org/uniprot/E9PDU5|||http://purl.uniprot.org/uniprot/Q9NNW5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylmethionine|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 17|||WD 18|||WD 19|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||tRNA (34-2'-O)-methyltransferase regulator WDR6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051352
http://togogenome.org/gene/9606:BAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95816                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BAG|||BAG family molecular chaperone regulator 2|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088866|||http://purl.uniprot.org/annotation/VSP_056462
http://togogenome.org/gene/9606:SNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75324                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Mitochondrial intermembrane|||Phosphoserine|||Stannin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072014|||http://purl.uniprot.org/annotation/VAR_018842|||http://purl.uniprot.org/annotation/VAR_018843
http://togogenome.org/gene/9606:CLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFF3|||http://purl.uniprot.org/uniprot/B4DMY6|||http://purl.uniprot.org/uniprot/Q13286|||http://purl.uniprot.org/uniprot/Q2TA70                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Battenin|||Cysteine methyl ester|||Cytoplasmic|||Disordered|||Does not affect glycosylation.|||Does not affect lysosomal localization in AP3D1 or AP2A2 or AP1G1 deficient cells. Abolishes the interaction of AP3D1, AP2A2 and AP1G1. Loss of lysosomal localization.|||Does not affect lysosomal targeting; when associated with A-409. Loss of lysosomal targeting; when associated with A-253 and A-254. Loss of lysosomal targeting; when associated with 242-A--A-244 and A-409. Does not affect interaction with CLN5; when associated with A-409. Does not affect interaction with CLN5; when associated with A-253; A-254 and A-409. Loss of lysosomal targeting; when associated with A-253; A-254 and A-409. Loss of lysosomal localization in AP3D1 or AP1G1 deficient cells; when associated with A-409.|||Does not affect lysosomal targeting; when associated with A-419. Loss of lysosomal targeting; when associated with A-253 and A-254. Loss of lysosomal targeting; when associated with 242-A--A-244 and A-419. Does not affect interaction with CLN5; when associated with A-419. Does not affect interaction with CLN5; when associated with A-253; A-254 and A-419. Loss of lysosomal targeting; when associated with A-253; A-254 and A-419. Loss of lysosomal localization in AP3D1 or AP1G1 deficient cells; when associated with A-419.|||Helical|||In CLN3.|||In CLN3; Decreases synthesis of bis(monoacylglycerol)phosphate..|||In CLN3; Does not affect lysosomal localization. Does not affect lysosomal protein catabolic process. Does not affect lysosomal pH.|||In CLN3; Loss of lysosomal localization.|||In CLN3; the mutant is located to vesicles clustered in a perinuclear region. Does not affect protein synthesis and maturation. Does not affect lysosomal localization..|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of lysosomal localization; when associated with 242-A--A-244.|||Loss of lysosomal targeting. Does not affect interaction with CLN5; when associated with A-253. Does not affect interaction with CLN5; when associated with A-253; A-409 and A-419. Loss of lysosomal targeting; when associated with A-253; A-409 and A-409.|||Loss of lysosomal targeting; when associated with A-254. Does not affect interaction with CLN5; when associated with A-254. Does not affect interaction with CLN5; when associated with A-254; A-409 and A-419. Loss of lysosomal targeting; when associated with A-254; A-409 and A-409.|||Loss of lysosomal targeting; when associated with A-409 and A-419. Loss of lysosomal localization; when associated with A-246.|||Lumenal|||Lysosomal targeting motif|||Lysosomal targeting motif. Required for AP1G1, AP2A2 and AP3D1 interaction|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089857|||http://purl.uniprot.org/annotation/PRO_0000422290|||http://purl.uniprot.org/annotation/VAR_005131|||http://purl.uniprot.org/annotation/VAR_005132|||http://purl.uniprot.org/annotation/VAR_005133|||http://purl.uniprot.org/annotation/VAR_005134|||http://purl.uniprot.org/annotation/VAR_005135|||http://purl.uniprot.org/annotation/VAR_005136|||http://purl.uniprot.org/annotation/VAR_066892|||http://purl.uniprot.org/annotation/VAR_066893|||http://purl.uniprot.org/annotation/VAR_066894|||http://purl.uniprot.org/annotation/VAR_083168|||http://purl.uniprot.org/annotation/VSP_004166|||http://purl.uniprot.org/annotation/VSP_004167|||http://purl.uniprot.org/annotation/VSP_004168|||http://purl.uniprot.org/annotation/VSP_004169|||http://purl.uniprot.org/annotation/VSP_004170|||http://purl.uniprot.org/annotation/VSP_047631|||http://purl.uniprot.org/annotation/VSP_047632|||http://purl.uniprot.org/annotation/VSP_057347
http://togogenome.org/gene/9606:NDRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5L7|||http://purl.uniprot.org/uniprot/A0A0S2Z5R7|||http://purl.uniprot.org/uniprot/B7Z9X4|||http://purl.uniprot.org/uniprot/Q9ULP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Protein NDRG4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159579|||http://purl.uniprot.org/annotation/VSP_003421|||http://purl.uniprot.org/annotation/VSP_003422|||http://purl.uniprot.org/annotation/VSP_003423|||http://purl.uniprot.org/annotation/VSP_022956|||http://purl.uniprot.org/annotation/VSP_022957|||http://purl.uniprot.org/annotation/VSP_045830|||http://purl.uniprot.org/annotation/VSP_046326
http://togogenome.org/gene/9606:FGF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1P5|||http://purl.uniprot.org/uniprot/Q92913                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor 13|||In DEE90.|||In DEE90; loss of ability to induce SCN8A long-term inactivation; no effect on pro-excitatory properties; no effect on interaction with SCN8A.|||In DEE90; loss of ability to induce SCN8A long-term inactivation; no effect on pro-excitatory properties; no effect on interaction with SCN8A; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of interaction with SCN1A.|||Mediates interaction with sodium channels|||Mediates targeting to the nucleus|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147607|||http://purl.uniprot.org/annotation/VAR_020945|||http://purl.uniprot.org/annotation/VAR_085434|||http://purl.uniprot.org/annotation/VAR_085435|||http://purl.uniprot.org/annotation/VAR_085436|||http://purl.uniprot.org/annotation/VAR_087934|||http://purl.uniprot.org/annotation/VSP_001529|||http://purl.uniprot.org/annotation/VSP_043460|||http://purl.uniprot.org/annotation/VSP_043461|||http://purl.uniprot.org/annotation/VSP_044129
http://togogenome.org/gene/9606:IFNGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K881|||http://purl.uniprot.org/uniprot/E7EUY1|||http://purl.uniprot.org/uniprot/P38484                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Complete inhibition of transport to the cell membrane.|||Cytoplasmic|||Dileucine internalization motif|||Does not affect accumulation on the cell membrane.|||Does not affect function.|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In IMD28; affects receptor trafficking to the cell surface.|||In IMD28; does not affect receptor trafficking to the cell surface; loss of function due to gain of N-glycosylation.|||In IMD28; encodes misfolded protein with abnormal glycosylation; affects receptor trafficking to the cell surface; reduces response to IFNG.|||Interferon gamma receptor 2|||Leads to overaccumulation on the cell membrane.|||Leads to overaccumulation on the cell membrane. Enhances function.|||Leads to small increase in accumulation on the cell membrane.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011011|||http://purl.uniprot.org/annotation/PRO_5003219018|||http://purl.uniprot.org/annotation/PRO_5014297552|||http://purl.uniprot.org/annotation/VAR_002718|||http://purl.uniprot.org/annotation/VAR_020003|||http://purl.uniprot.org/annotation/VAR_021383|||http://purl.uniprot.org/annotation/VAR_021384|||http://purl.uniprot.org/annotation/VAR_023281|||http://purl.uniprot.org/annotation/VAR_023282|||http://purl.uniprot.org/annotation/VAR_075305|||http://purl.uniprot.org/annotation/VAR_075306|||http://purl.uniprot.org/annotation/VAR_075307|||http://purl.uniprot.org/annotation/VAR_075308
http://togogenome.org/gene/9606:HOXA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20719                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200057
http://togogenome.org/gene/9606:GPR35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2J1|||http://purl.uniprot.org/uniprot/B2RA17|||http://purl.uniprot.org/uniprot/Q9HC97                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 35|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069563|||http://purl.uniprot.org/annotation/VAR_013601|||http://purl.uniprot.org/annotation/VAR_013602|||http://purl.uniprot.org/annotation/VAR_013603|||http://purl.uniprot.org/annotation/VAR_013604|||http://purl.uniprot.org/annotation/VAR_013605|||http://purl.uniprot.org/annotation/VAR_013606|||http://purl.uniprot.org/annotation/VAR_033467|||http://purl.uniprot.org/annotation/VSP_045871
http://togogenome.org/gene/9606:KIR3DL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1WNF3|||http://purl.uniprot.org/uniprot/P43630|||http://purl.uniprot.org/uniprot/Q8NHI6|||http://purl.uniprot.org/uniprot/Q8NHK6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Immunoglobulin subtype|||In isoform 2.|||Killer cell immunoglobulin-like receptor 3DL2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015090|||http://purl.uniprot.org/annotation/PRO_5014107531|||http://purl.uniprot.org/annotation/PRO_5015048862|||http://purl.uniprot.org/annotation/VAR_010325|||http://purl.uniprot.org/annotation/VAR_010326|||http://purl.uniprot.org/annotation/VAR_010327|||http://purl.uniprot.org/annotation/VAR_010328|||http://purl.uniprot.org/annotation/VAR_010329|||http://purl.uniprot.org/annotation/VAR_010330|||http://purl.uniprot.org/annotation/VAR_049992|||http://purl.uniprot.org/annotation/VAR_049993|||http://purl.uniprot.org/annotation/VSP_047374
http://togogenome.org/gene/9606:ZNF764                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 764                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274398|||http://purl.uniprot.org/annotation/VAR_047845|||http://purl.uniprot.org/annotation/VSP_045352
http://togogenome.org/gene/9606:ACTL7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKC6|||http://purl.uniprot.org/uniprot/Q9Y614                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Actin-like protein 7B|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089139
http://togogenome.org/gene/9606:SAMD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YEJ0|||http://purl.uniprot.org/uniprot/Q8N8I0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  SAM|||Sterile alpha motif domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279502
http://togogenome.org/gene/9606:GRIA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42263|||http://purl.uniprot.org/uniprot/Q17R51|||http://purl.uniprot.org/uniprot/Q5XKG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in patients with familial episodic ataxia and impairment of speech development; unknown pathological significance.|||Glutamate receptor|||Glutamate receptor 3|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||In MRXSW.|||In MRXSW; homomers have minimal or no current; heteromers have altered desensitization kinetics.|||In MRXSW; reduced receptor expression possibly due to rapid degradation.|||In isoform Flip.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011536|||http://purl.uniprot.org/annotation/PRO_5014587137|||http://purl.uniprot.org/annotation/PRO_5027143338|||http://purl.uniprot.org/annotation/VAR_023579|||http://purl.uniprot.org/annotation/VAR_043484|||http://purl.uniprot.org/annotation/VAR_043485|||http://purl.uniprot.org/annotation/VAR_043486|||http://purl.uniprot.org/annotation/VAR_043487|||http://purl.uniprot.org/annotation/VAR_081437|||http://purl.uniprot.org/annotation/VSP_053351
http://togogenome.org/gene/9606:OR4A47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IF82                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4A47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150527|||http://purl.uniprot.org/annotation/VAR_047759|||http://purl.uniprot.org/annotation/VAR_047760|||http://purl.uniprot.org/annotation/VAR_047761|||http://purl.uniprot.org/annotation/VAR_047762
http://togogenome.org/gene/9606:KRT86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K872|||http://purl.uniprot.org/uniprot/O43790                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||In MNLIX.|||Keratin, type II cuticular Hb6|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063704|||http://purl.uniprot.org/annotation/VAR_018125|||http://purl.uniprot.org/annotation/VAR_018126|||http://purl.uniprot.org/annotation/VAR_018127|||http://purl.uniprot.org/annotation/VAR_018128|||http://purl.uniprot.org/annotation/VAR_018129|||http://purl.uniprot.org/annotation/VAR_023053|||http://purl.uniprot.org/annotation/VAR_073050|||http://purl.uniprot.org/annotation/VAR_073051
http://togogenome.org/gene/9606:NUFIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z417                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FMR1-interacting protein NUFIP2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245521|||http://purl.uniprot.org/annotation/VSP_056177
http://togogenome.org/gene/9606:NIPAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NN97|||http://purl.uniprot.org/uniprot/Q6P499                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||NIPA-like protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242150|||http://purl.uniprot.org/annotation/VSP_019445|||http://purl.uniprot.org/annotation/VSP_019446|||http://purl.uniprot.org/annotation/VSP_019447
http://togogenome.org/gene/9606:SUPT20HL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7V6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Putative transcription factor SPT20 homolog-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344460
http://togogenome.org/gene/9606:MAFK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60675                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic motif|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Leucine-zipper|||Phosphoserine|||Transcription factor MafK|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076503
http://togogenome.org/gene/9606:REEP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RGS2|||http://purl.uniprot.org/uniprot/Q9H6H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Receptor expression-enhancing protein|||Receptor expression-enhancing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101830|||http://purl.uniprot.org/annotation/PRO_5003198348|||http://purl.uniprot.org/annotation/VSP_016636|||http://purl.uniprot.org/annotation/VSP_016637
http://togogenome.org/gene/9606:ARRDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBH0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arrestin domain-containing protein 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244347|||http://purl.uniprot.org/annotation/VAR_026895|||http://purl.uniprot.org/annotation/VAR_026896|||http://purl.uniprot.org/annotation/VAR_026897|||http://purl.uniprot.org/annotation/VAR_026898|||http://purl.uniprot.org/annotation/VSP_019544
http://togogenome.org/gene/9606:SLC39A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H72                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In EDSSPD3.|||In EDSSPD3; unknown pathological significance.|||In isoform 2.|||Lumenal|||XEXPHE-motif|||Zinc transporter ZIP13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312309|||http://purl.uniprot.org/annotation/VAR_037484|||http://purl.uniprot.org/annotation/VAR_037485|||http://purl.uniprot.org/annotation/VAR_054127|||http://purl.uniprot.org/annotation/VAR_087851|||http://purl.uniprot.org/annotation/VSP_029819
http://togogenome.org/gene/9606:FFAR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWG6|||http://purl.uniprot.org/uniprot/Q5NUL3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with increased risk of obesity; significantly decreases LCFA-induced intracellular calcium release..|||Cytoplasmic|||Extracellular|||Free fatty acid receptor 4|||G-protein coupled receptors family 1 profile|||Has no effect on LCFA-induced intracellular calcium release.|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs LCFA-induced intracellular calcium release.|||Impairs LCFA-mediated phosphorylation and interaction with ARRB2.|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069610|||http://purl.uniprot.org/annotation/VAR_067799|||http://purl.uniprot.org/annotation/VAR_067800|||http://purl.uniprot.org/annotation/VSP_060543
http://togogenome.org/gene/9606:GML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99445                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Glycosyl-phosphatidylinositol-anchored molecule-like protein|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036166|||http://purl.uniprot.org/annotation/VAR_020174
http://togogenome.org/gene/9606:CPOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36551                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Important for dimerization|||In HARPO.|||In HCP.|||In HCP; <5% of activity.|||In HCP; a patient carrying also the L-12 mutation in ALAD.|||In isoform 2.|||Loss for dimerization.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006029|||http://purl.uniprot.org/annotation/VAR_002151|||http://purl.uniprot.org/annotation/VAR_002152|||http://purl.uniprot.org/annotation/VAR_002153|||http://purl.uniprot.org/annotation/VAR_002154|||http://purl.uniprot.org/annotation/VAR_002155|||http://purl.uniprot.org/annotation/VAR_002156|||http://purl.uniprot.org/annotation/VAR_002157|||http://purl.uniprot.org/annotation/VAR_002158|||http://purl.uniprot.org/annotation/VAR_002159|||http://purl.uniprot.org/annotation/VAR_002160|||http://purl.uniprot.org/annotation/VAR_002161|||http://purl.uniprot.org/annotation/VAR_002162|||http://purl.uniprot.org/annotation/VAR_002163|||http://purl.uniprot.org/annotation/VAR_019067|||http://purl.uniprot.org/annotation/VAR_019068|||http://purl.uniprot.org/annotation/VAR_019069|||http://purl.uniprot.org/annotation/VAR_023444|||http://purl.uniprot.org/annotation/VAR_023445|||http://purl.uniprot.org/annotation/VAR_023446|||http://purl.uniprot.org/annotation/VAR_048827|||http://purl.uniprot.org/annotation/VAR_058005|||http://purl.uniprot.org/annotation/VAR_084511|||http://purl.uniprot.org/annotation/VAR_084512|||http://purl.uniprot.org/annotation/VSP_057182|||http://purl.uniprot.org/annotation/VSP_057183
http://togogenome.org/gene/9606:NOLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAU8|||http://purl.uniprot.org/uniprot/Q14978|||http://purl.uniprot.org/uniprot/Q96J17                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  11 X 12 AA approximate repeats of an acidic serine cluster|||Acidic serine cluster 1|||Acidic serine cluster 10|||Acidic serine cluster 11|||Acidic serine cluster 2|||Acidic serine cluster 3|||Acidic serine cluster 4|||Acidic serine cluster 5|||Acidic serine cluster 6|||Acidic serine cluster 7|||Acidic serine cluster 8|||Acidic serine cluster 9|||Basic and acidic residues|||Diphosphoserine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 3.|||In isoform Beta.|||Interaction with RPA194|||LisH|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal|||Nucleolar and coiled-body phosphoprotein 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Srp40 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096942|||http://purl.uniprot.org/annotation/VAR_031677|||http://purl.uniprot.org/annotation/VAR_031678|||http://purl.uniprot.org/annotation/VSP_004338|||http://purl.uniprot.org/annotation/VSP_035415
http://togogenome.org/gene/9606:C1orf116                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW04                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Specifically androgen-regulated gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318575|||http://purl.uniprot.org/annotation/VAR_038775|||http://purl.uniprot.org/annotation/VAR_038776|||http://purl.uniprot.org/annotation/VAR_038777|||http://purl.uniprot.org/annotation/VAR_038778|||http://purl.uniprot.org/annotation/VAR_038779|||http://purl.uniprot.org/annotation/VAR_038780|||http://purl.uniprot.org/annotation/VAR_038781|||http://purl.uniprot.org/annotation/VSP_031228
http://togogenome.org/gene/9606:STPG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N412                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  STPGR 1|||STPGR 2|||STPGR 3|||STPGR 4|||STPGR 5|||STPGR 6|||STPGR 7|||STPGR 8|||STPGR 9|||Sperm-tail PG-rich repeat-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311960|||http://purl.uniprot.org/annotation/VAR_037359|||http://purl.uniprot.org/annotation/VAR_037360|||http://purl.uniprot.org/annotation/VAR_037361|||http://purl.uniprot.org/annotation/VAR_037362|||http://purl.uniprot.org/annotation/VAR_037363|||http://purl.uniprot.org/annotation/VAR_037364
http://togogenome.org/gene/9606:GPR156                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFN8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Probable G-protein coupled receptor 156                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206899|||http://purl.uniprot.org/annotation/VAR_049284|||http://purl.uniprot.org/annotation/VSP_044603
http://togogenome.org/gene/9606:CCDC34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HJ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Coiled-coil domain-containing protein 34|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339111|||http://purl.uniprot.org/annotation/VAR_043866|||http://purl.uniprot.org/annotation/VAR_043867|||http://purl.uniprot.org/annotation/VAR_043868|||http://purl.uniprot.org/annotation/VAR_050750|||http://purl.uniprot.org/annotation/VSP_034096|||http://purl.uniprot.org/annotation/VSP_034097
http://togogenome.org/gene/9606:CD247                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPP4|||http://purl.uniprot.org/uniprot/A0A8V8TQM0|||http://purl.uniprot.org/uniprot/P20963                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreases cell surface expression of IgGFc receptor complex.|||Disordered|||Extracellular|||Helical|||ITAM 1|||ITAM 2|||ITAM 3|||In isoform 3.|||Phosphoserine|||Phosphotyrosine|||T-cell surface glycoprotein CD3 zeta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016493|||http://purl.uniprot.org/annotation/VSP_036459
http://togogenome.org/gene/9606:SAMD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5K651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In M7MLS2.|||In MIRAGE; decreased cell proliferation; changed endosome organization.|||In NFTC; loss of cytoplasmic expression.|||No defect in double-stranded nucleic acid binding but defective at inhibiting viral replication.|||Polar residues|||SAM|||Sterile alpha motif domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097573|||http://purl.uniprot.org/annotation/VAR_031526|||http://purl.uniprot.org/annotation/VAR_031527|||http://purl.uniprot.org/annotation/VAR_031528|||http://purl.uniprot.org/annotation/VAR_031529|||http://purl.uniprot.org/annotation/VAR_077813|||http://purl.uniprot.org/annotation/VAR_077885|||http://purl.uniprot.org/annotation/VAR_077886|||http://purl.uniprot.org/annotation/VAR_077887|||http://purl.uniprot.org/annotation/VAR_077888|||http://purl.uniprot.org/annotation/VAR_077889|||http://purl.uniprot.org/annotation/VAR_077890|||http://purl.uniprot.org/annotation/VAR_077891|||http://purl.uniprot.org/annotation/VAR_085147
http://togogenome.org/gene/9606:HPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32754                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyphenylpyruvate dioxygenase|||In TYRSN3.|||In isoform 2.|||In two patients with hawkinsinuria.|||N-acetylthreonine|||N6-succinyllysine|||Phosphoserine|||Removed|||VOC 1|||VOC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088388|||http://purl.uniprot.org/annotation/VAR_015444|||http://purl.uniprot.org/annotation/VAR_015445|||http://purl.uniprot.org/annotation/VAR_015446|||http://purl.uniprot.org/annotation/VAR_015447|||http://purl.uniprot.org/annotation/VAR_015448|||http://purl.uniprot.org/annotation/VAR_015449|||http://purl.uniprot.org/annotation/VAR_048101|||http://purl.uniprot.org/annotation/VSP_044302
http://togogenome.org/gene/9606:TSPY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CV98|||http://purl.uniprot.org/uniprot/P0CW01|||http://purl.uniprot.org/uniprot/Q01534                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Testis-specific Y-encoded protein 1|||Testis-specific Y-encoded protein 10|||Testis-specific Y-encoded protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185668|||http://purl.uniprot.org/annotation/PRO_0000408001|||http://purl.uniprot.org/annotation/PRO_0000408004|||http://purl.uniprot.org/annotation/VAR_016226|||http://purl.uniprot.org/annotation/VAR_016227|||http://purl.uniprot.org/annotation/VAR_016228|||http://purl.uniprot.org/annotation/VSP_008012
http://togogenome.org/gene/9606:ORC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0P7|||http://purl.uniprot.org/uniprot/O43913|||http://purl.uniprot.org/uniprot/Q53FC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Orc1-like AAA ATPase|||Origin recognition complex subunit 5|||Origin recognition complex subunit 5 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127092|||http://purl.uniprot.org/annotation/VAR_011800|||http://purl.uniprot.org/annotation/VAR_014524|||http://purl.uniprot.org/annotation/VAR_014525|||http://purl.uniprot.org/annotation/VSP_042037
http://togogenome.org/gene/9606:RIOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6W3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||JmjC|||N-acetylmethionine|||Phosphoserine|||Ribosomal oxygenase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264613|||http://purl.uniprot.org/annotation/VAR_057819|||http://purl.uniprot.org/annotation/VAR_060191|||http://purl.uniprot.org/annotation/VAR_062422|||http://purl.uniprot.org/annotation/VAR_062423|||http://purl.uniprot.org/annotation/VSP_038663
http://togogenome.org/gene/9606:RAB3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E17                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Loss of phosphorylation. No effect on GDI2, CHM and CHML binding.|||Phosphomimetic mutant. Loss of GDI2, CHM and CHML binding.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3C|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121085
http://togogenome.org/gene/9606:TSPAN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19075                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219252|||http://purl.uniprot.org/annotation/VAR_012054|||http://purl.uniprot.org/annotation/VAR_020093|||http://purl.uniprot.org/annotation/VAR_061848
http://togogenome.org/gene/9606:DOCK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 3|||Disordered|||In NEDIDHA.|||In NEDIDHA; unknown pathological significance.|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189988|||http://purl.uniprot.org/annotation/VAR_081831|||http://purl.uniprot.org/annotation/VAR_081832|||http://purl.uniprot.org/annotation/VAR_081833|||http://purl.uniprot.org/annotation/VAR_081834
http://togogenome.org/gene/9606:BSX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3C1V8                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Brain-specific homeobox protein homolog|||Disordered|||Homeobox                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299170
http://togogenome.org/gene/9606:PLGLB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02325                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  PAN|||Plasminogen-like protein B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022105
http://togogenome.org/gene/9606:KRTAP17-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYP8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 17-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223903
http://togogenome.org/gene/9606:SNX25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3E2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||PX|||PXA|||Phosphoserine|||RGS|||Sorting nexin-25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213875|||http://purl.uniprot.org/annotation/VAR_047057|||http://purl.uniprot.org/annotation/VAR_047058|||http://purl.uniprot.org/annotation/VAR_047059|||http://purl.uniprot.org/annotation/VSP_057156|||http://purl.uniprot.org/annotation/VSP_057157
http://togogenome.org/gene/9606:FAM221A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D161|||http://purl.uniprot.org/uniprot/B8ZZQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||Protein FAM221A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295139|||http://purl.uniprot.org/annotation/VAR_033215|||http://purl.uniprot.org/annotation/VAR_033216|||http://purl.uniprot.org/annotation/VAR_033217|||http://purl.uniprot.org/annotation/VAR_033218|||http://purl.uniprot.org/annotation/VAR_033219|||http://purl.uniprot.org/annotation/VSP_026738|||http://purl.uniprot.org/annotation/VSP_026739
http://togogenome.org/gene/9606:PNPLA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP80                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium-independent phospholipase A2-gamma|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Nucleophile|||PNPLA|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303214|||http://purl.uniprot.org/annotation/VSP_028005|||http://purl.uniprot.org/annotation/VSP_045594
http://togogenome.org/gene/9606:TMEM185B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7F4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 185B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188009
http://togogenome.org/gene/9606:TACSTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09758                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Thyroglobulin type-1|||Tumor-associated calcium signal transducer 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022468|||http://purl.uniprot.org/annotation/VAR_012451|||http://purl.uniprot.org/annotation/VAR_016981|||http://purl.uniprot.org/annotation/VAR_051407
http://togogenome.org/gene/9606:OR9A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVB1|||http://purl.uniprot.org/uniprot/Q8NGU2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150677
http://togogenome.org/gene/9606:DESI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICB0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  Desumoylating isopeptidase 1|||Nuclear export signal 1|||Nuclear export signal 2|||PPPDE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318150
http://togogenome.org/gene/9606:H2AC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FI13                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A type 2-A|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055232
http://togogenome.org/gene/9606:PHIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPV5|||http://purl.uniprot.org/uniprot/Q8WWQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Bromo 1|||Bromo 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In CHUJANS.|||In CHUJANS; unknown pathological significance.|||In CHUJANS; unknown pathological significance; found in a patient who also carries a de novo missense variant in TBC1D8B.|||In a colorectal cancer sample; somatic mutation.|||Mediates interaction with IRS1|||N6-acetyllysine|||PH-interacting protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297757|||http://purl.uniprot.org/annotation/VAR_034683|||http://purl.uniprot.org/annotation/VAR_034684|||http://purl.uniprot.org/annotation/VAR_034685|||http://purl.uniprot.org/annotation/VAR_034686|||http://purl.uniprot.org/annotation/VAR_034687|||http://purl.uniprot.org/annotation/VAR_036238|||http://purl.uniprot.org/annotation/VAR_036239|||http://purl.uniprot.org/annotation/VAR_078691|||http://purl.uniprot.org/annotation/VAR_080981|||http://purl.uniprot.org/annotation/VAR_080982|||http://purl.uniprot.org/annotation/VAR_080983|||http://purl.uniprot.org/annotation/VAR_080984|||http://purl.uniprot.org/annotation/VAR_080985|||http://purl.uniprot.org/annotation/VAR_080986|||http://purl.uniprot.org/annotation/VAR_080987|||http://purl.uniprot.org/annotation/VAR_080988|||http://purl.uniprot.org/annotation/VAR_080989|||http://purl.uniprot.org/annotation/VAR_080990|||http://purl.uniprot.org/annotation/VAR_080991
http://togogenome.org/gene/9606:CCDC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V121|||http://purl.uniprot.org/uniprot/Q86WR0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished binding to neutrophil extracellular traps (NETs).|||Basic and acidic residues|||Coiled-coil domain-containing protein 25|||Cytoplasmic|||DNA-binding|||Disordered|||Does not affect binding to neutrophil extracellular traps (NETs).|||Extracellular|||Helical|||In isoform 2.|||N6-acetyllysine|||NFACT RNA-binding|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233404|||http://purl.uniprot.org/annotation/VSP_056046
http://togogenome.org/gene/9606:TBX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15119                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In UMS.|||In isoform I.|||In isoform III.|||Phosphoserine|||Polar residues|||Reduces binding to T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence.|||T-box transcription factor TBX3|||T-box; first part|||T-box; second part|||Transcription repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184428|||http://purl.uniprot.org/annotation/VAR_009601|||http://purl.uniprot.org/annotation/VAR_009602|||http://purl.uniprot.org/annotation/VSP_006384|||http://purl.uniprot.org/annotation/VSP_006385|||http://purl.uniprot.org/annotation/VSP_006386
http://togogenome.org/gene/9606:CST11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5Z6|||http://purl.uniprot.org/uniprot/Q9H112                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cystatin|||Cystatin-11|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006658|||http://purl.uniprot.org/annotation/PRO_5033788092|||http://purl.uniprot.org/annotation/VSP_001260
http://togogenome.org/gene/9606:HACD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Y1H2                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not restore any protein tyrosine phosphatase activity.|||Helical|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed|||Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349319
http://togogenome.org/gene/9606:B9D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J223|||http://purl.uniprot.org/uniprot/A0A2R8Y646|||http://purl.uniprot.org/uniprot/A0A6Q8PFJ7|||http://purl.uniprot.org/uniprot/A8MYG7|||http://purl.uniprot.org/uniprot/B4DEW0|||http://purl.uniprot.org/uniprot/Q9UPM9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  B9 domain-containing protein 1|||C2 B9-type|||Disordered|||In JBTS27.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307667|||http://purl.uniprot.org/annotation/PRO_5002107024|||http://purl.uniprot.org/annotation/PRO_5002726087|||http://purl.uniprot.org/annotation/PRO_5002800804|||http://purl.uniprot.org/annotation/PRO_5015317094|||http://purl.uniprot.org/annotation/PRO_5028145604|||http://purl.uniprot.org/annotation/VAR_066995|||http://purl.uniprot.org/annotation/VAR_075700|||http://purl.uniprot.org/annotation/VAR_076974|||http://purl.uniprot.org/annotation/VAR_076975|||http://purl.uniprot.org/annotation/VAR_076976|||http://purl.uniprot.org/annotation/VSP_028770
http://togogenome.org/gene/9606:KRTDAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60985                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Keratinocyte differentiation-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022609|||http://purl.uniprot.org/annotation/VSP_030856
http://togogenome.org/gene/9606:DCDC2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344449
http://togogenome.org/gene/9606:NRDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1R5|||http://purl.uniprot.org/uniprot/O43847|||http://purl.uniprot.org/uniprot/Q6UUU9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Nardilysin|||Peptidase M16 C-terminal|||Peptidase M16 N-terminal|||Peptidase M16 middle/third|||Phosphoserine|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026755|||http://purl.uniprot.org/annotation/VAR_057058|||http://purl.uniprot.org/annotation/VAR_080827|||http://purl.uniprot.org/annotation/VSP_007114
http://togogenome.org/gene/9606:RFNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9R1|||http://purl.uniprot.org/uniprot/Q9Y644                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-N-acetylglucosaminyltransferase radical fringe|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219185
http://togogenome.org/gene/9606:ISCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U28                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In MMDS4.|||In isoform 2.|||Iron-sulfur cluster assembly 2 homolog, mitochondrial|||Mitochondrion|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277588|||http://purl.uniprot.org/annotation/VAR_073794|||http://purl.uniprot.org/annotation/VSP_055691|||http://purl.uniprot.org/annotation/VSP_055692
http://togogenome.org/gene/9606:KRTAP4-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29 X 5 AA repeats of C-C-[GIKRQVH]-[SPT]-[STA]|||3|||4|||5|||6|||7|||8|||9|||In allele KAP3-v1.|||In allele KAP3-v2.|||Keratin-associated protein 4-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185171|||http://purl.uniprot.org/annotation/VAR_053457|||http://purl.uniprot.org/annotation/VAR_053458|||http://purl.uniprot.org/annotation/VAR_064557|||http://purl.uniprot.org/annotation/VAR_064558
http://togogenome.org/gene/9606:KCNAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R776|||http://purl.uniprot.org/uniprot/Q13303                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||NADP-dependent oxidoreductase|||No effect on its activity in promoting KCNA4 channel closure.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Proton donor/acceptor|||Voltage-gated potassium channel subunit beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148746|||http://purl.uniprot.org/annotation/VSP_001054|||http://purl.uniprot.org/annotation/VSP_041189|||http://purl.uniprot.org/annotation/VSP_041190|||http://purl.uniprot.org/annotation/VSP_044311|||http://purl.uniprot.org/annotation/VSP_057282
http://togogenome.org/gene/9606:KLF14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 14|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047186|||http://purl.uniprot.org/annotation/VAR_052718
http://togogenome.org/gene/9606:DDX47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0S4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||DEAD box|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Probable ATP-dependent RNA helicase DDX47|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055050|||http://purl.uniprot.org/annotation/VAR_083613|||http://purl.uniprot.org/annotation/VAR_083614|||http://purl.uniprot.org/annotation/VSP_045239
http://togogenome.org/gene/9606:SERPINA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6I9|||http://purl.uniprot.org/uniprot/P29622                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Kallistatin|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Serpin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032425|||http://purl.uniprot.org/annotation/PRO_5014214252
http://togogenome.org/gene/9606:PCSK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16519                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Decreased secretion; reduced proglucagon processing.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Neuroendocrine convertase 2|||No effect on secretion; no effect on proglucagon processing.|||P/Homo B|||Peptidase S8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027065|||http://purl.uniprot.org/annotation/PRO_0000027066|||http://purl.uniprot.org/annotation/VAR_036548|||http://purl.uniprot.org/annotation/VAR_069075|||http://purl.uniprot.org/annotation/VAR_069076|||http://purl.uniprot.org/annotation/VAR_079730|||http://purl.uniprot.org/annotation/VAR_079731|||http://purl.uniprot.org/annotation/VAR_079732|||http://purl.uniprot.org/annotation/VAR_079733|||http://purl.uniprot.org/annotation/VSP_043358|||http://purl.uniprot.org/annotation/VSP_045873
http://togogenome.org/gene/9606:ZNF311                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8W3|||http://purl.uniprot.org/uniprot/Q5JNZ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 311                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280404|||http://purl.uniprot.org/annotation/VAR_031136|||http://purl.uniprot.org/annotation/VAR_031137
http://togogenome.org/gene/9606:TAS2R50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59544                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082337|||http://purl.uniprot.org/annotation/VAR_024187
http://togogenome.org/gene/9606:CDKN2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42773|||http://purl.uniprot.org/uniprot/Q6ICV4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase 4 inhibitor C|||In breast cancer; loss of CDK6 interaction.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144186|||http://purl.uniprot.org/annotation/VAR_001490|||http://purl.uniprot.org/annotation/VAR_038604
http://togogenome.org/gene/9606:OR5L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150603|||http://purl.uniprot.org/annotation/VAR_034229|||http://purl.uniprot.org/annotation/VAR_062045
http://togogenome.org/gene/9606:DDIT4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D03                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  DNA damage-inducible transcript 4-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307204|||http://purl.uniprot.org/annotation/VAR_053971
http://togogenome.org/gene/9606:RPAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2F9|||http://purl.uniprot.org/uniprot/Q9BWH6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RNA polymerase II-associated protein 1|||RNA polymerase II-associated protein 1 C-terminal|||RNA polymerase II-associated protein 1 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284841|||http://purl.uniprot.org/annotation/VAR_036469|||http://purl.uniprot.org/annotation/VAR_057738|||http://purl.uniprot.org/annotation/VAR_057739|||http://purl.uniprot.org/annotation/VAR_057740|||http://purl.uniprot.org/annotation/VAR_060348|||http://purl.uniprot.org/annotation/VAR_060349|||http://purl.uniprot.org/annotation/VAR_060350|||http://purl.uniprot.org/annotation/VSP_024679|||http://purl.uniprot.org/annotation/VSP_024680|||http://purl.uniprot.org/annotation/VSP_024681
http://togogenome.org/gene/9606:AP2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95782                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-2 complex subunit alpha-1|||Basic and acidic residues|||Disordered|||In isoform B.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193730|||http://purl.uniprot.org/annotation/VAR_060544|||http://purl.uniprot.org/annotation/VSP_000161
http://togogenome.org/gene/9606:REG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYZ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  C-type lectin|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Regenerating islet-derived protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017437|||http://purl.uniprot.org/annotation/VAR_050122|||http://purl.uniprot.org/annotation/VSP_014305|||http://purl.uniprot.org/annotation/VSP_014308
http://togogenome.org/gene/9606:VPS13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RL7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abnormal localization to the cytosol.|||Chorein N-terminal|||FFAT|||In CHAC.|||In CHAC; abolishes association with lipid droplets and disrupts subcellular localization with protein XK on lipid droplets..|||In CHAC; disrupts subcellular localization with protein XK on lipid droplets..|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Intermembrane lipid transfer protein VPS13A|||Phosphoserine|||Reduced interaction with VAPA.|||Required for lipid droplet localization|||Required for mitochondrial localization|||SHR-BD|||TPR 1|||TPR 10|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106277|||http://purl.uniprot.org/annotation/VAR_012803|||http://purl.uniprot.org/annotation/VAR_036324|||http://purl.uniprot.org/annotation/VAR_038420|||http://purl.uniprot.org/annotation/VAR_038421|||http://purl.uniprot.org/annotation/VAR_058114|||http://purl.uniprot.org/annotation/VAR_058115|||http://purl.uniprot.org/annotation/VAR_058116|||http://purl.uniprot.org/annotation/VAR_058117|||http://purl.uniprot.org/annotation/VAR_058118|||http://purl.uniprot.org/annotation/VAR_058119|||http://purl.uniprot.org/annotation/VAR_058120|||http://purl.uniprot.org/annotation/VAR_058121|||http://purl.uniprot.org/annotation/VAR_058122|||http://purl.uniprot.org/annotation/VAR_086164|||http://purl.uniprot.org/annotation/VAR_086165|||http://purl.uniprot.org/annotation/VAR_086166|||http://purl.uniprot.org/annotation/VAR_086167|||http://purl.uniprot.org/annotation/VAR_086168|||http://purl.uniprot.org/annotation/VAR_086169|||http://purl.uniprot.org/annotation/VAR_086170|||http://purl.uniprot.org/annotation/VAR_086171|||http://purl.uniprot.org/annotation/VAR_086172|||http://purl.uniprot.org/annotation/VAR_086173|||http://purl.uniprot.org/annotation/VAR_086174|||http://purl.uniprot.org/annotation/VAR_086175|||http://purl.uniprot.org/annotation/VAR_086176|||http://purl.uniprot.org/annotation/VAR_086177|||http://purl.uniprot.org/annotation/VAR_086178|||http://purl.uniprot.org/annotation/VAR_086179|||http://purl.uniprot.org/annotation/VAR_086180|||http://purl.uniprot.org/annotation/VAR_086181|||http://purl.uniprot.org/annotation/VAR_086182|||http://purl.uniprot.org/annotation/VAR_086183|||http://purl.uniprot.org/annotation/VSP_006550|||http://purl.uniprot.org/annotation/VSP_014904|||http://purl.uniprot.org/annotation/VSP_014905|||http://purl.uniprot.org/annotation/VSP_014906
http://togogenome.org/gene/9606:ATP6V1B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK65|||http://purl.uniprot.org/uniprot/P21281                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase F1/V1/A1 complex alpha/beta subunit N-terminal|||ATPase F1/V1/A1 complex alpha/beta subunit nucleotide-binding|||In ZLS2.|||V-type proton ATPase subunit B, brain isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144626|||http://purl.uniprot.org/annotation/VAR_073962
http://togogenome.org/gene/9606:JPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H910                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Jupiter microtubule associated homolog 2|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054921|||http://purl.uniprot.org/annotation/VSP_014706|||http://purl.uniprot.org/annotation/VSP_057423
http://togogenome.org/gene/9606:PRDM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IU23|||http://purl.uniprot.org/uniprot/B4DW27|||http://purl.uniprot.org/uniprot/O75626|||http://purl.uniprot.org/uniprot/Q5T4E8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Found in an activated B cell-like diffuse large B-cell lymphoma (ABC-DLBCL) cell line; protein instability caused by increased susceptibility to proteasomal degradation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Interaction with PIAS1|||PR domain zinc finger protein 1|||Polar residues|||Protein instability caused by increased susceptibility to proteasomal degradation.|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047757|||http://purl.uniprot.org/annotation/VAR_019983|||http://purl.uniprot.org/annotation/VAR_024221|||http://purl.uniprot.org/annotation/VAR_083591|||http://purl.uniprot.org/annotation/VAR_083592|||http://purl.uniprot.org/annotation/VSP_039188|||http://purl.uniprot.org/annotation/VSP_043646|||http://purl.uniprot.org/annotation/VSP_043647
http://togogenome.org/gene/9606:MTRFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3J6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||GGQ|||GGQ domain|||In COXPD7; decreased cytochrome c oxidase activity in fibroblasts; severe assembly defects in mitochondrial complexes I, IV and V with a milder defect in the assembly of complex III; no effect on mitochondrial transcripts, rRNAs and tRNAs levels.|||In SPG55 and COXPD7; decreased activity of mitochondrial respiratory chain; no effect on mitochondrial morphology.|||In SPG55.|||In isoform 2.|||Mitochondrial translation release factor in rescue|||Mitochondrion|||N5-methylglutamine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311835|||http://purl.uniprot.org/annotation/VAR_037325|||http://purl.uniprot.org/annotation/VAR_084490|||http://purl.uniprot.org/annotation/VAR_084491|||http://purl.uniprot.org/annotation/VAR_084492|||http://purl.uniprot.org/annotation/VAR_084493|||http://purl.uniprot.org/annotation/VSP_029602|||http://purl.uniprot.org/annotation/VSP_029603
http://togogenome.org/gene/9606:TMEM232                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JQI7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 1.|||Transmembrane protein 232                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395035|||http://purl.uniprot.org/annotation/VSP_039352
http://togogenome.org/gene/9606:VN1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZP7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele VN1R1*2.|||In allele VN1R1*3.|||N-linked (GlcNAc...) asparagine|||Vomeronasal type-1 receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070213|||http://purl.uniprot.org/annotation/VAR_022795|||http://purl.uniprot.org/annotation/VAR_022796|||http://purl.uniprot.org/annotation/VAR_022797|||http://purl.uniprot.org/annotation/VAR_049452
http://togogenome.org/gene/9606:FIS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Approximately 40% of cells display fragmented mitochondria.|||Approximately 40% of cells display fragmented mitochondria. No change in binding to DNM1L.|||Cytoplasmic|||Helical|||Less than 15% of cells display fragmented mitochondria.|||Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L.|||Mitochondrial fission 1 protein|||Mitochondrial intermembrane|||N-acetylmethionine|||Phosphoserine|||Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-149.|||Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-151.|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106393
http://togogenome.org/gene/9606:CDH17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12864                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin-17|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003812|||http://purl.uniprot.org/annotation/VAR_031694|||http://purl.uniprot.org/annotation/VAR_031695|||http://purl.uniprot.org/annotation/VAR_031696|||http://purl.uniprot.org/annotation/VAR_055567
http://togogenome.org/gene/9606:MICB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JHB5|||http://purl.uniprot.org/uniprot/A0A7D9H7X8|||http://purl.uniprot.org/uniprot/B4DUT9|||http://purl.uniprot.org/uniprot/B7Z8M1|||http://purl.uniprot.org/uniprot/F5H7Q8|||http://purl.uniprot.org/uniprot/Q29980                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C1-type|||In allele MICB*001, allele MICB*002, allele MICB*003, allele MICB*005, allele MICB*006, allele MICB*007, allele MICB*008, allele MICB*010, allele MICB*011, allele MICB*012, allele MICB*013, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*018, allele MICB*019 and allele MICB*022.|||In allele MICB*001, allele MICB*002, allele MICB*005, allele MICB*006, allele MICB*007, allele MICB*008, allele MICB*012, allele MICB*013, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*018, allele MICB*019, allele MICB*020 and allele MICB*022.|||In allele MICB*001, allele MICB*016, allele MICB*018, allele MICB*019, allele MICB*020 and allele MICB*022.|||In allele MICB*001.|||In allele MICB*002, allele MICB*007, allele MICB*008, allele MICB*014, allele MICB*015, allele MICB*016, allele MICB*019 and allele MICB*022.|||In allele MICB*002, allele MICB*007, allele MICB*008, allele MICB*014, allele MICB*015, allele MICB*018, allele MICB*020 and allele MICB*022.|||In allele MICB*003.|||In allele MICB*006 and allele MICB*015.|||In allele MICB*007.|||In allele MICB*008.|||In allele MICB*011.|||In allele MICB*012.|||In allele MICB*013, allele MICB*014, allele MICB*015 and allele MICB*016.|||In allele MICB*022.|||In isoform 2.|||In isoform 3.|||MHC class I polypeptide-related sequence B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341418|||http://purl.uniprot.org/annotation/PRO_5002545976|||http://purl.uniprot.org/annotation/PRO_5033588527|||http://purl.uniprot.org/annotation/VAR_044068|||http://purl.uniprot.org/annotation/VAR_044069|||http://purl.uniprot.org/annotation/VAR_044070|||http://purl.uniprot.org/annotation/VAR_044071|||http://purl.uniprot.org/annotation/VAR_044072|||http://purl.uniprot.org/annotation/VAR_044073|||http://purl.uniprot.org/annotation/VAR_044074|||http://purl.uniprot.org/annotation/VAR_044075|||http://purl.uniprot.org/annotation/VAR_044076|||http://purl.uniprot.org/annotation/VAR_044077|||http://purl.uniprot.org/annotation/VAR_044078|||http://purl.uniprot.org/annotation/VAR_044079|||http://purl.uniprot.org/annotation/VAR_044080|||http://purl.uniprot.org/annotation/VAR_044081|||http://purl.uniprot.org/annotation/VAR_059527|||http://purl.uniprot.org/annotation/VSP_052801|||http://purl.uniprot.org/annotation/VSP_052802|||http://purl.uniprot.org/annotation/VSP_055246
http://togogenome.org/gene/9606:TEKT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEB7|||http://purl.uniprot.org/uniprot/Q8WW24                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Polar residues|||Tektin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261161|||http://purl.uniprot.org/annotation/VAR_029085|||http://purl.uniprot.org/annotation/VAR_029086|||http://purl.uniprot.org/annotation/VAR_029087|||http://purl.uniprot.org/annotation/VAR_035941|||http://purl.uniprot.org/annotation/VAR_062151
http://togogenome.org/gene/9606:FAM136A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EQY1|||http://purl.uniprot.org/uniprot/Q96C01                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphothreonine|||Protein FAM136A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296950
http://togogenome.org/gene/9606:CYP26C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6V0L0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 26C1|||Helical|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051987|||http://purl.uniprot.org/annotation/VAR_022886
http://togogenome.org/gene/9606:TAPBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCT1|||http://purl.uniprot.org/uniprot/A0A0A0MSV9|||http://purl.uniprot.org/uniprot/A0A0A0MT98|||http://purl.uniprot.org/uniprot/O15533                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes the recruitment of PDIA3, CALR and B2M to the peptide-loading complex.|||Cytoplasmic|||Helical|||Ig-like|||Ig-like C1-type|||In allele TAPBP*01.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inter-subunit salt bridge with TAP1-TAP2. Essential peptide loading complex assembly|||Interchain (with C-57 in PDIA3)|||Lumenal|||May be involved in interaction with TAP|||N-linked (GlcNAc...) asparagine|||Reduces the recruitment of PDIA3 to TAP1-TAP2 transporter.|||Restores interaction with TAP1-TAP2; when associated with TAP1 K-92 or TAP2 K-16.|||Tapasin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014990|||http://purl.uniprot.org/annotation/PRO_5010606084|||http://purl.uniprot.org/annotation/PRO_5014506439|||http://purl.uniprot.org/annotation/PRO_5014506440|||http://purl.uniprot.org/annotation/VAR_010253|||http://purl.uniprot.org/annotation/VSP_002577|||http://purl.uniprot.org/annotation/VSP_017055|||http://purl.uniprot.org/annotation/VSP_044455
http://togogenome.org/gene/9606:OR1K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVB9|||http://purl.uniprot.org/uniprot/Q8NGR3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150441|||http://purl.uniprot.org/annotation/VAR_034168
http://togogenome.org/gene/9606:RBFOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43251                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Disordered|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 9 and isoform 10.|||In isoform 2, isoform 8 and isoform 9.|||In isoform 3, isoform 5, isoform 7 and isoform 9.|||In isoform 3.|||In isoform 4 and isoform 9.|||In isoform 6 and isoform 8.|||In isoform 7.|||Interaction with RNA|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphothreonine|||Polar residues|||Pro residues|||RNA binding protein fox-1 homolog 2|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081766|||http://purl.uniprot.org/annotation/VSP_007180|||http://purl.uniprot.org/annotation/VSP_007181|||http://purl.uniprot.org/annotation/VSP_007182|||http://purl.uniprot.org/annotation/VSP_007183|||http://purl.uniprot.org/annotation/VSP_030889|||http://purl.uniprot.org/annotation/VSP_030890|||http://purl.uniprot.org/annotation/VSP_030891
http://togogenome.org/gene/9606:MRPL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYD1                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein uL13m|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000133793
http://togogenome.org/gene/9606:APBB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4M9|||http://purl.uniprot.org/uniprot/O00213                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-204.|||Abolished acetylation by KAT5, leading to decreased transcription activator activity; when associated with R-701.|||Abrogates phosphorylation and stimulation of transcription by ABL1, and increases the interaction with RASD1/DEXRAS1.|||Acidic residues|||Amyloid beta precursor protein binding family B member 1|||Basic and acidic residues|||Disordered|||Impairs transcriptional activation and inhibits binding to ABL1.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 6.|||Mimics acetylation; leading to increased transcription activator activity; when associated with Q-204.|||Mimics acetylation; leading to increased transcription activator activity; when associated with Q-701.|||N6-acetyllysine|||No effect on phosphorylation by ABL1.|||PID|||PID 1|||PID 2|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphotyrosine; by ABL1|||Polar residues|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076049|||http://purl.uniprot.org/annotation/VAR_014444|||http://purl.uniprot.org/annotation/VAR_014445|||http://purl.uniprot.org/annotation/VSP_011658|||http://purl.uniprot.org/annotation/VSP_045326|||http://purl.uniprot.org/annotation/VSP_045327|||http://purl.uniprot.org/annotation/VSP_047459|||http://purl.uniprot.org/annotation/VSP_054709
http://togogenome.org/gene/9606:SCRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FV2                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphothreonine|||Secernin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262552|||http://purl.uniprot.org/annotation/VAR_029509|||http://purl.uniprot.org/annotation/VAR_029510|||http://purl.uniprot.org/annotation/VAR_029511|||http://purl.uniprot.org/annotation/VAR_035263|||http://purl.uniprot.org/annotation/VAR_035264|||http://purl.uniprot.org/annotation/VSP_044566
http://togogenome.org/gene/9606:KIF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60333                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis.|||Confers susceptibility to pheochromocytoma; found as germline mutation in a pheochromocytoma family; loss of ability to induce apoptosis.|||Disordered|||FHA|||In CMT2A1.|||In a medulloblastoma sample; somatic mutation; loss of ability to induce apoptosis.|||In a pheochromocytoma sample; loss of ability to induce apoptosis.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with KBP|||Kinesin motor|||Kinesin-like protein KIF1B|||N-acetylserine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125407|||http://purl.uniprot.org/annotation/VAR_011515|||http://purl.uniprot.org/annotation/VAR_063531|||http://purl.uniprot.org/annotation/VAR_063532|||http://purl.uniprot.org/annotation/VAR_063533|||http://purl.uniprot.org/annotation/VAR_063534|||http://purl.uniprot.org/annotation/VAR_063535|||http://purl.uniprot.org/annotation/VAR_063536|||http://purl.uniprot.org/annotation/VAR_063537|||http://purl.uniprot.org/annotation/VAR_063538|||http://purl.uniprot.org/annotation/VSP_002858|||http://purl.uniprot.org/annotation/VSP_002859|||http://purl.uniprot.org/annotation/VSP_002860|||http://purl.uniprot.org/annotation/VSP_002861|||http://purl.uniprot.org/annotation/VSP_009381
http://togogenome.org/gene/9606:SEC16A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KPG1|||http://purl.uniprot.org/uniprot/F1T0I1|||http://purl.uniprot.org/uniprot/O15027                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ancestral coatomer element 1 Sec16/Sec31|||Basic and acidic residues|||Central conserved domain (CCD); mediates interaction with RNF183, LRRK2 and SEC13|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with MIA3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein transport protein Sec16A|||Required for endoplasmic reticulum localization|||Required for interaction with SEC23A|||Required for localization to endoplasmic reticulum exit sites|||Sec16 central conserved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050746|||http://purl.uniprot.org/annotation/VAR_023332|||http://purl.uniprot.org/annotation/VSP_015252|||http://purl.uniprot.org/annotation/VSP_015253|||http://purl.uniprot.org/annotation/VSP_034370|||http://purl.uniprot.org/annotation/VSP_036029
http://togogenome.org/gene/9606:PARP16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5Y8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP-ribosyl aspartic acid|||ADP-ribosyl glutamic acid|||ADP-ribosyltransferase activity is only 6% of wild-type; when associated with A-182.|||ADP-ribosyltransferase activity is only 6% of wild-type; when associated with Q-152.|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Loss of ADP-ribosyltransferase activity; when associated with A-254.|||Loss of ADP-ribosyltransferase activity; when associated with H-152.|||Lumenal|||N6-(ADP-ribosyl)lysine|||Nicotinamide-stacking aromate|||PARP alpha-helical|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252437|||http://purl.uniprot.org/annotation/VAR_027864|||http://purl.uniprot.org/annotation/VSP_020973|||http://purl.uniprot.org/annotation/VSP_020974
http://togogenome.org/gene/9606:PYROXD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2H3                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244071|||http://purl.uniprot.org/annotation/VAR_026877|||http://purl.uniprot.org/annotation/VAR_026878|||http://purl.uniprot.org/annotation/VAR_026879
http://togogenome.org/gene/9606:PMM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92871                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylalanine|||Nucleophile|||Phosphomannomutase 1|||Phosphoserine|||Proton donor/acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199692
http://togogenome.org/gene/9606:KRT28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3Y7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 28|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312705|||http://purl.uniprot.org/annotation/VAR_056009|||http://purl.uniprot.org/annotation/VAR_056010|||http://purl.uniprot.org/annotation/VAR_060236
http://togogenome.org/gene/9606:DMKN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IYI1|||http://purl.uniprot.org/uniprot/Q6E0U4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Dermokine|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform 11 and isoform 12.|||In isoform 13 and isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 2.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 4 and isoform 16.|||In isoform 4, isoform 12 and isoform 14.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330764|||http://purl.uniprot.org/annotation/VAR_042720|||http://purl.uniprot.org/annotation/VAR_042721|||http://purl.uniprot.org/annotation/VAR_047337|||http://purl.uniprot.org/annotation/VAR_056865|||http://purl.uniprot.org/annotation/VAR_056866|||http://purl.uniprot.org/annotation/VAR_059652|||http://purl.uniprot.org/annotation/VAR_059653|||http://purl.uniprot.org/annotation/VSP_033087|||http://purl.uniprot.org/annotation/VSP_033088|||http://purl.uniprot.org/annotation/VSP_033089|||http://purl.uniprot.org/annotation/VSP_033090|||http://purl.uniprot.org/annotation/VSP_033091|||http://purl.uniprot.org/annotation/VSP_033092|||http://purl.uniprot.org/annotation/VSP_033093|||http://purl.uniprot.org/annotation/VSP_033094|||http://purl.uniprot.org/annotation/VSP_033095|||http://purl.uniprot.org/annotation/VSP_033096|||http://purl.uniprot.org/annotation/VSP_033097|||http://purl.uniprot.org/annotation/VSP_033098|||http://purl.uniprot.org/annotation/VSP_033099|||http://purl.uniprot.org/annotation/VSP_033100|||http://purl.uniprot.org/annotation/VSP_033101|||http://purl.uniprot.org/annotation/VSP_033102|||http://purl.uniprot.org/annotation/VSP_033103|||http://purl.uniprot.org/annotation/VSP_033104|||http://purl.uniprot.org/annotation/VSP_033105|||http://purl.uniprot.org/annotation/VSP_033106|||http://purl.uniprot.org/annotation/VSP_047249
http://togogenome.org/gene/9606:ZBED5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AG3                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BED-type|||Zinc finger BED domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291958|||http://purl.uniprot.org/annotation/VAR_032895|||http://purl.uniprot.org/annotation/VAR_032896|||http://purl.uniprot.org/annotation/VAR_032897|||http://purl.uniprot.org/annotation/VAR_059741
http://togogenome.org/gene/9606:BLVRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30043|||http://purl.uniprot.org/uniprot/V9HWI1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Flavin reductase (NADPH)|||NAD(P)-binding|||Phosphoserine|||Reduced affinity for biliverdin.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064948|||http://purl.uniprot.org/annotation/VAR_019168
http://togogenome.org/gene/9606:SMCO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU48                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Single-pass membrane and coiled-coil domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336988|||http://purl.uniprot.org/annotation/VAR_043558|||http://purl.uniprot.org/annotation/VAR_043559
http://togogenome.org/gene/9606:KRTAP19-4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI73                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 19-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223906|||http://purl.uniprot.org/annotation/VAR_053475
http://togogenome.org/gene/9606:POU6F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78424                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In WT5.|||In isoform 2.|||POU domain, class 6, transcription factor 2|||POU-specific|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100762|||http://purl.uniprot.org/annotation/VAR_022419|||http://purl.uniprot.org/annotation/VAR_028410|||http://purl.uniprot.org/annotation/VAR_028411|||http://purl.uniprot.org/annotation/VAR_028412|||http://purl.uniprot.org/annotation/VSP_002336
http://togogenome.org/gene/9606:ACYP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD7|||http://purl.uniprot.org/uniprot/E9PF46|||http://purl.uniprot.org/uniprot/F8WA34|||http://purl.uniprot.org/uniprot/P14621|||http://purl.uniprot.org/uniprot/U3KQL2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Acylphosphatase-2|||Acylphosphatase-like|||Disordered|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158542
http://togogenome.org/gene/9606:F8A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  40-kDa huntingtin-associated protein|||Disordered|||N-acetylalanine|||Nuclear localization signal|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087159
http://togogenome.org/gene/9606:CCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32246|||http://purl.uniprot.org/uniprot/Q5U003                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-C chemokine receptor type 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069228
http://togogenome.org/gene/9606:MSANTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6R9L8|||http://purl.uniprot.org/uniprot/Q6ZTZ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Myb-like|||Myb/SANT-like DNA-binding|||Myb/SANT-like DNA-binding domain-containing protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321819
http://togogenome.org/gene/9606:TXNDC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY7|||http://purl.uniprot.org/uniprot/Q9BRA2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Contributes to redox potential value|||Loss of peroxidase activity.|||N-acetylalanine|||Nucleophile|||Redox-active|||Removed|||Thioredoxin|||Thioredoxin domain-containing protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120022
http://togogenome.org/gene/9606:USF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4U5|||http://purl.uniprot.org/uniprot/P22415                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Leucine-zipper|||Upstream stimulatory factor 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127496|||http://purl.uniprot.org/annotation/VSP_047740
http://togogenome.org/gene/9606:TSSC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5U2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hom2; mediates interaction with the U5 snRNP complexes and required for spliceosomal tri-snRNP complex assembly|||Hom3; mediates interaction with the U5 snRNP complexes|||Hom4; necessary for interaction with the PRPF19 complex and required for spliceosomal tri-snRNP complex assembly|||In isoform 2.|||Interaction with SNRNP200|||Loss of interaction with PRPF8 and SNRNP200; when associated with A-162, A-201, A-202, A-315 and A-316.|||Loss of interaction with PRPF8 and SNRNP200; when associated with A-165, A-201, A-202, A-315 and A-316.|||Loss of interaction with SNRNP200; when associated with A-201, A-202 and A-315. Loss of interaction with PRPF8 and SNRNP200; when associated with A-162, A-165, A-201, A-202 and A-315.|||Loss of interaction with SNRNP200; when associated with A-201, A-202 and A-316. Loss of interaction with PRPF8 and SNRNP200; when associated with A-162, A-165, A-201, A-202 and A-316.|||Loss of interaction with SNRNP200; when associated with A-201, A-315 and A-316. Loss of interaction with PRPF8 and SNRNP200; when associated with A-162, A-165, A-201, A-315 and A-316.|||Loss of interaction with SNRNP200; when associated with A-202, A-315 and A-316. Loss of interaction with PRPF8 and SNRNP200; when associated with A-162, A-165, A-202, A-315 and A-316.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||U5 small nuclear ribonucleoprotein TSSC4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076360|||http://purl.uniprot.org/annotation/VAR_057826|||http://purl.uniprot.org/annotation/VAR_057827|||http://purl.uniprot.org/annotation/VAR_057828|||http://purl.uniprot.org/annotation/VAR_060194|||http://purl.uniprot.org/annotation/VAR_063128|||http://purl.uniprot.org/annotation/VSP_016561
http://togogenome.org/gene/9606:NMBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28336                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuromedin-B receptor|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069903|||http://purl.uniprot.org/annotation/VAR_044513
http://togogenome.org/gene/9606:ESPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14674                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autocleavage; when associated with A-1161 and A-1210.|||Abolishes autocleavage; when associated with A-1161 and A-1281.|||Abolishes autocleavage; when associated with A-1181 and A-1210.|||Abolishes autocleavage; when associated with R-1178; E-1181; R-1207 and E-1210. Does not affect the protease function.|||Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation.|||Abolishes protease activity.|||Basic and acidic residues|||Cleavage; by autolysis|||Disordered|||Does not affect autocleavage. Does not affect the protease function.|||In isoform 2.|||Peptidase C50|||Phosphoserine|||Polar residues|||Separin|||Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205900|||http://purl.uniprot.org/annotation/VAR_057703|||http://purl.uniprot.org/annotation/VAR_057704|||http://purl.uniprot.org/annotation/VAR_057705|||http://purl.uniprot.org/annotation/VAR_057706|||http://purl.uniprot.org/annotation/VAR_057707|||http://purl.uniprot.org/annotation/VAR_057708|||http://purl.uniprot.org/annotation/VSP_009361
http://togogenome.org/gene/9606:TNNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRJ5|||http://purl.uniprot.org/uniprot/P45379|||http://purl.uniprot.org/uniprot/Q15607                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In CMD1D.|||In CMH2.|||In isoform 10, isoform 11 and isoform 12.|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 12.|||In isoform 5.|||In isoform 6 and isoform 11.|||In isoform 7.|||In isoform 8.|||In isoform 9 and isoform 12.|||N-acetylserine|||Phosphoserine; by CK2|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine; by PKC/PRKCA|||Phosphothreonine; by PKC/PRKCA and RAF1|||Removed|||Troponin T, cardiac muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186173|||http://purl.uniprot.org/annotation/VAR_007605|||http://purl.uniprot.org/annotation/VAR_007606|||http://purl.uniprot.org/annotation/VAR_007607|||http://purl.uniprot.org/annotation/VAR_007608|||http://purl.uniprot.org/annotation/VAR_007609|||http://purl.uniprot.org/annotation/VAR_007610|||http://purl.uniprot.org/annotation/VAR_007611|||http://purl.uniprot.org/annotation/VAR_007612|||http://purl.uniprot.org/annotation/VAR_007613|||http://purl.uniprot.org/annotation/VAR_009194|||http://purl.uniprot.org/annotation/VAR_013021|||http://purl.uniprot.org/annotation/VAR_013022|||http://purl.uniprot.org/annotation/VAR_016195|||http://purl.uniprot.org/annotation/VAR_016196|||http://purl.uniprot.org/annotation/VAR_016197|||http://purl.uniprot.org/annotation/VAR_016198|||http://purl.uniprot.org/annotation/VAR_016199|||http://purl.uniprot.org/annotation/VAR_019877|||http://purl.uniprot.org/annotation/VAR_019878|||http://purl.uniprot.org/annotation/VAR_019879|||http://purl.uniprot.org/annotation/VAR_019880|||http://purl.uniprot.org/annotation/VAR_022931|||http://purl.uniprot.org/annotation/VAR_029450|||http://purl.uniprot.org/annotation/VAR_029451|||http://purl.uniprot.org/annotation/VAR_042747|||http://purl.uniprot.org/annotation/VAR_042748|||http://purl.uniprot.org/annotation/VAR_043983|||http://purl.uniprot.org/annotation/VAR_043984|||http://purl.uniprot.org/annotation/VAR_043985|||http://purl.uniprot.org/annotation/VAR_057310|||http://purl.uniprot.org/annotation/VAR_067259|||http://purl.uniprot.org/annotation/VSP_006641|||http://purl.uniprot.org/annotation/VSP_006642|||http://purl.uniprot.org/annotation/VSP_006643|||http://purl.uniprot.org/annotation/VSP_006644|||http://purl.uniprot.org/annotation/VSP_006645|||http://purl.uniprot.org/annotation/VSP_006646|||http://purl.uniprot.org/annotation/VSP_006647|||http://purl.uniprot.org/annotation/VSP_006648
http://togogenome.org/gene/9606:SHPRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX98|||http://purl.uniprot.org/uniprot/Q149N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 activity.|||Basic and acidic residues|||Basic residues|||DEAQ box|||Disordered|||E3 ubiquitin-protein ligase SHPRH|||Found in a renal cell carcinoma sample; somatic mutation.|||H15|||Helicase ATP-binding; first part|||Helicase ATP-binding; second part|||Helicase C-terminal|||In a melanoma cell line.|||In an ovarian cancer cell line.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PHD-type|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284918|||http://purl.uniprot.org/annotation/VAR_031857|||http://purl.uniprot.org/annotation/VAR_031858|||http://purl.uniprot.org/annotation/VAR_031859|||http://purl.uniprot.org/annotation/VAR_064750|||http://purl.uniprot.org/annotation/VSP_024753|||http://purl.uniprot.org/annotation/VSP_024756|||http://purl.uniprot.org/annotation/VSP_024757|||http://purl.uniprot.org/annotation/VSP_024758|||http://purl.uniprot.org/annotation/VSP_024759|||http://purl.uniprot.org/annotation/VSP_024760|||http://purl.uniprot.org/annotation/VSP_024761|||http://purl.uniprot.org/annotation/VSP_024762|||http://purl.uniprot.org/annotation/VSP_024763
http://togogenome.org/gene/9606:CD27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26842                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CD27 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In LPFS2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Phosphoserine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034571|||http://purl.uniprot.org/annotation/VAR_016148|||http://purl.uniprot.org/annotation/VAR_052348|||http://purl.uniprot.org/annotation/VAR_069793
http://togogenome.org/gene/9606:TFDP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14188                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||DCB1|||DCB2|||DEF box|||Dimerization|||Disordered|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform Beta and isoform Gamma.|||In isoform Beta, isoform Gamma, isoform Delta and isoform Epsilon.|||In isoform Gamma and isoform Epsilon.|||Interaction with CEBPA|||N-acetylthreonine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Removed|||Transcription factor Dp-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219477|||http://purl.uniprot.org/annotation/VAR_002272|||http://purl.uniprot.org/annotation/VAR_020567|||http://purl.uniprot.org/annotation/VSP_001352|||http://purl.uniprot.org/annotation/VSP_001353|||http://purl.uniprot.org/annotation/VSP_001354|||http://purl.uniprot.org/annotation/VSP_043140|||http://purl.uniprot.org/annotation/VSP_043141|||http://purl.uniprot.org/annotation/VSP_045455|||http://purl.uniprot.org/annotation/VSP_047415
http://togogenome.org/gene/9606:NR2F6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8R3|||http://purl.uniprot.org/uniprot/P10588                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Important for dimerization|||Loss of DNA (TRE) binding. Reduces the corepressor activity towards THRB.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 2 group F member 6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053613
http://togogenome.org/gene/9606:UBB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG47|||http://purl.uniprot.org/uniprot/Q5U5U6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  (Microbial infection) ADP-ribosylthreonine|||ADP-ribosylglycine|||Abolishes HLTF-mediated polyubiquitination of PCNA.|||Essential for function|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In UBB(+1); loss of polyubiquitination; impairs the ubiquitin-proteasome pathway; refractory to disassembly by DUBs; slow degradation by UCHL3.|||Interacts with activating enzyme|||Loss of ADP-ribosylation.|||Loss of DTX3L-mediated polyubiquitination of histone H3 and H4.|||No effect on ADP-ribosylation, when associated with K-72.|||No effect on ADP-ribosylation, when associated with K-74.|||No effect on ADP-ribosylation.|||No effect on HLTF-mediated polyubiquitination of PCNA.|||Phosphomimetic mutant that binds and activates PRKN.|||Phosphoserine; by PINK1|||Prevents phosphorylation in case of mitophagy. Decreased localization of PRKN to mitochondria.|||Ubiquitin|||Ubiquitin-like|||Ubiquitin-like 1|||Ubiquitin-like 2|||Ubiquitin-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000396174|||http://purl.uniprot.org/annotation/PRO_0000396175|||http://purl.uniprot.org/annotation/PRO_0000396176|||http://purl.uniprot.org/annotation/PRO_0000396177|||http://purl.uniprot.org/annotation/VAR_066248
http://togogenome.org/gene/9606:SPANXN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MJ08|||http://purl.uniprot.org/uniprot/X6R7N2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Sperm protein associated with the nucleus on the X chromosome N4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285541|||http://purl.uniprot.org/annotation/VAR_032027
http://togogenome.org/gene/9606:AIPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0B5|||http://purl.uniprot.org/uniprot/F1T0B6|||http://purl.uniprot.org/uniprot/F1T0C0|||http://purl.uniprot.org/uniprot/F1T0C4|||http://purl.uniprot.org/uniprot/Q7Z3H1|||http://purl.uniprot.org/uniprot/Q9NZN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Aryl-hydrocarbon-interacting protein-like 1|||Disordered|||Found in a patient with LCA4.|||Found in a patient with LCA4; there is no interaction with NUB1.|||In LCA4.|||In LCA4; no significant effect on interaction with NUB1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||No interaction with NUB1.|||No significant effect on interaction with NUB1.|||PPIase FKBP-type|||Pro residues|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075342|||http://purl.uniprot.org/annotation/VAR_010139|||http://purl.uniprot.org/annotation/VAR_010140|||http://purl.uniprot.org/annotation/VAR_050626|||http://purl.uniprot.org/annotation/VAR_050627|||http://purl.uniprot.org/annotation/VAR_067165|||http://purl.uniprot.org/annotation/VAR_067166|||http://purl.uniprot.org/annotation/VAR_067167|||http://purl.uniprot.org/annotation/VSP_041507|||http://purl.uniprot.org/annotation/VSP_041508|||http://purl.uniprot.org/annotation/VSP_047708|||http://purl.uniprot.org/annotation/VSP_047709
http://togogenome.org/gene/9606:CPSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9W3|||http://purl.uniprot.org/uniprot/Q9UKF6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-Casp|||Cleavage and polyadenylation specificity factor subunit 3|||Does not inhibit histone 3'-end processing.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In NEDMHS.|||In NEDMHS; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||Inhibits histone 3'-end processing.|||Loss of histone 3'-end processing.|||Metallo-beta-lactamase|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Pre-mRNA 3'-end-processing endonuclease polyadenylation factor C-term|||Proton donor|||Reduced sumoylation; when associated with R-462 and R-465.|||Reduced sumoylation; when associated with R-462 and R-545.|||Reduced sumoylation; when associated with R-465 and R-545.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074400|||http://purl.uniprot.org/annotation/VAR_035873|||http://purl.uniprot.org/annotation/VAR_037646|||http://purl.uniprot.org/annotation/VAR_087333|||http://purl.uniprot.org/annotation/VAR_087334
http://togogenome.org/gene/9606:MAGEC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreases interaction with TRIM28, abolishes in vitro ubiquitination of TP53.|||Disordered|||In a breast cancer sample; somatic mutation.|||Interaction with TRIM28|||MAGE|||Melanoma-associated antigen C2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156721|||http://purl.uniprot.org/annotation/VAR_036583
http://togogenome.org/gene/9606:SPDYE16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNV3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Putative speedy protein E16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341229
http://togogenome.org/gene/9606:COPRS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9KV77|||http://purl.uniprot.org/uniprot/Q9NQ92                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coordinator of PRMT5 and differentiation stimulator|||Disordered|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336077|||http://purl.uniprot.org/annotation/VAR_043538
http://togogenome.org/gene/9606:ANK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01484                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Acidic residues|||Ankyrin-2|||Basic and acidic residues|||Death 1|||Death 2|||Disordered|||In LQT4; loss of function.|||In LQT4; unknown pathological significance; abnormal calcium ion homeostasis, when tested in a heterologous system.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Interaction with SPTBN1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Prevents binding to SPTBN1.|||Repeat A|||Repeat A; approximate|||Repeat-rich region|||UPA domain|||Weak binding to SPTBN1.|||ZU5 1|||ZU5 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066885|||http://purl.uniprot.org/annotation/VAR_022934|||http://purl.uniprot.org/annotation/VAR_022935|||http://purl.uniprot.org/annotation/VAR_022936|||http://purl.uniprot.org/annotation/VAR_022937|||http://purl.uniprot.org/annotation/VAR_022938|||http://purl.uniprot.org/annotation/VAR_035606|||http://purl.uniprot.org/annotation/VAR_035607|||http://purl.uniprot.org/annotation/VAR_035608|||http://purl.uniprot.org/annotation/VAR_055504|||http://purl.uniprot.org/annotation/VAR_055505|||http://purl.uniprot.org/annotation/VAR_081135|||http://purl.uniprot.org/annotation/VSP_000268|||http://purl.uniprot.org/annotation/VSP_037057|||http://purl.uniprot.org/annotation/VSP_037058|||http://purl.uniprot.org/annotation/VSP_037059|||http://purl.uniprot.org/annotation/VSP_037060
http://togogenome.org/gene/9606:TOMM20L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXN7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Mitochondrial intermembrane|||TOMM20-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317747
http://togogenome.org/gene/9606:INPP5K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT40                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Catalytic|||In MDCCAID; decreased phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In MDCCAID; decreased phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; shows normal localization indistinguishable from the wild-type.|||In MDCCAID; no phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||In MDCCAID; no phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; shows normal localization indistinguishable from the wild-type.|||In MDCCAID; shows a diffuse perinuclear mislocalization.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Inositol polyphosphate 5-phosphatase K|||No effect on EGF-induced ruffle localization.|||No phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity.|||Required for interaction with GPR78 and PAK1|||Required for ruffle localization|||Significant decrease in EGF-induced ruffle localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209727|||http://purl.uniprot.org/annotation/VAR_036497|||http://purl.uniprot.org/annotation/VAR_078998|||http://purl.uniprot.org/annotation/VAR_078999|||http://purl.uniprot.org/annotation/VAR_079000|||http://purl.uniprot.org/annotation/VAR_079001|||http://purl.uniprot.org/annotation/VAR_079002|||http://purl.uniprot.org/annotation/VAR_079003|||http://purl.uniprot.org/annotation/VAR_079004|||http://purl.uniprot.org/annotation/VAR_079005|||http://purl.uniprot.org/annotation/VSP_050612
http://togogenome.org/gene/9606:IKBKE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B7B4|||http://purl.uniprot.org/uniprot/Q14164                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decrease in kinase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Inhibitor of nuclear factor kappa-B kinase subunit epsilon|||Interaction with DDX3X|||Leucine-zipper|||Loss of autophosphorylation and of kinase activity.|||Loss of kinase activity and loss of nuclear import.|||Loss of sumoylation and loss of targeting to nuclear bodies.|||Loss of ubiquitination and decreased kinase activity. Decreases interaction with IKBKB, IKBKG and MYD88. No effect on homodimerization.|||Loss of ubiquitination and decreased kinase activity. No effect on homodimerization.|||No effect on ubiquitination.|||Phosphoserine|||Phosphoserine; by autocatalysis and IKKB|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Slight decrease of kinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086017|||http://purl.uniprot.org/annotation/VAR_019989|||http://purl.uniprot.org/annotation/VAR_038816|||http://purl.uniprot.org/annotation/VAR_038817|||http://purl.uniprot.org/annotation/VAR_038818|||http://purl.uniprot.org/annotation/VAR_038819|||http://purl.uniprot.org/annotation/VAR_038820|||http://purl.uniprot.org/annotation/VAR_040571|||http://purl.uniprot.org/annotation/VAR_040572|||http://purl.uniprot.org/annotation/VSP_044305
http://togogenome.org/gene/9606:SPINK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hemofiltrate peptide HF6478|||Hemofiltrate peptide HF7665|||In isoform long.|||In isoform short.|||Kazal-like 10|||Kazal-like 11|||Kazal-like 12|||Kazal-like 13|||Kazal-like 14|||Kazal-like 15|||Kazal-like 1; atypical|||Kazal-like 2|||Kazal-like 3|||Kazal-like 4|||Kazal-like 5|||Kazal-like 6|||Kazal-like 7|||Kazal-like 8|||Kazal-like 9|||Reactive bond|||Serine protease inhibitor Kazal-type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016572|||http://purl.uniprot.org/annotation/PRO_0000016573|||http://purl.uniprot.org/annotation/PRO_0000016574|||http://purl.uniprot.org/annotation/VAR_015537|||http://purl.uniprot.org/annotation/VAR_047115|||http://purl.uniprot.org/annotation/VAR_047116|||http://purl.uniprot.org/annotation/VAR_047117|||http://purl.uniprot.org/annotation/VAR_047118|||http://purl.uniprot.org/annotation/VAR_047119|||http://purl.uniprot.org/annotation/VAR_047120|||http://purl.uniprot.org/annotation/VAR_047121|||http://purl.uniprot.org/annotation/VAR_047122|||http://purl.uniprot.org/annotation/VAR_047123|||http://purl.uniprot.org/annotation/VAR_047124|||http://purl.uniprot.org/annotation/VAR_047125|||http://purl.uniprot.org/annotation/VAR_061337|||http://purl.uniprot.org/annotation/VSP_040019|||http://purl.uniprot.org/annotation/VSP_040020|||http://purl.uniprot.org/annotation/VSP_040021
http://togogenome.org/gene/9606:LMCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEY6|||http://purl.uniprot.org/uniprot/B7Z6R5|||http://purl.uniprot.org/uniprot/H7C3D2|||http://purl.uniprot.org/uniprot/Q9NZU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LIM and cysteine-rich domains protein 1|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||PET|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075815|||http://purl.uniprot.org/annotation/VSP_053895
http://togogenome.org/gene/9606:PRSS23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95084                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Serine protease 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027847|||http://purl.uniprot.org/annotation/VSP_056628
http://togogenome.org/gene/9606:ZNF777                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Polar residues|||Zinc finger protein 777                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293692|||http://purl.uniprot.org/annotation/VAR_057451|||http://purl.uniprot.org/annotation/VAR_057452|||http://purl.uniprot.org/annotation/VAR_061965
http://togogenome.org/gene/9606:SHLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYI0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Shieldin complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286612|||http://purl.uniprot.org/annotation/VAR_032144|||http://purl.uniprot.org/annotation/VSP_025125
http://togogenome.org/gene/9606:FGF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVZ5|||http://purl.uniprot.org/uniprot/Q92914                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147602|||http://purl.uniprot.org/annotation/VAR_018886
http://togogenome.org/gene/9606:ABCA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWZ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter 1|||ABC transporter 2|||Cholesterol transporter ABCA5|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250669|||http://purl.uniprot.org/annotation/VAR_027571|||http://purl.uniprot.org/annotation/VAR_027572|||http://purl.uniprot.org/annotation/VAR_027573|||http://purl.uniprot.org/annotation/VAR_027574|||http://purl.uniprot.org/annotation/VAR_027575|||http://purl.uniprot.org/annotation/VAR_048128|||http://purl.uniprot.org/annotation/VAR_048129|||http://purl.uniprot.org/annotation/VSP_020690|||http://purl.uniprot.org/annotation/VSP_020691|||http://purl.uniprot.org/annotation/VSP_020692
http://togogenome.org/gene/9606:TFPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C1Z6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues|||TCF3 fusion partner                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254581|||http://purl.uniprot.org/annotation/VSP_058937
http://togogenome.org/gene/9606:CEP95                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 95 kDa|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234505|||http://purl.uniprot.org/annotation/VAR_033666|||http://purl.uniprot.org/annotation/VAR_050751|||http://purl.uniprot.org/annotation/VSP_056356
http://togogenome.org/gene/9606:RMND5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSG5|||http://purl.uniprot.org/uniprot/F5H6G4|||http://purl.uniprot.org/uniprot/Q96G75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CTLH|||E3 ubiquitin-protein transferase RMND5B|||In isoform 2.|||LisH|||N-acetylmethionine|||RING-Gid-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065709|||http://purl.uniprot.org/annotation/VSP_013174
http://togogenome.org/gene/9606:DYNLRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJH9|||http://purl.uniprot.org/uniprot/H3BQI1|||http://purl.uniprot.org/uniprot/Q8TF09                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein light chain roadblock-type 2|||N-acetylalanine|||Removed|||Roadblock/LAMTOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220958|||http://purl.uniprot.org/annotation/VAR_049126
http://togogenome.org/gene/9606:PCCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05165                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-grasp|||Biotin carboxylation|||Biotinyl-binding|||In PA-1.|||In PA-1; loss of biotinylation.|||In PA-1; loss of function.|||In PA-1; unstable protein; loss of function.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-biotinyllysine; by HLCS|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Propionyl-CoA carboxylase alpha chain, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002837|||http://purl.uniprot.org/annotation/VAR_009087|||http://purl.uniprot.org/annotation/VAR_009088|||http://purl.uniprot.org/annotation/VAR_009089|||http://purl.uniprot.org/annotation/VAR_009090|||http://purl.uniprot.org/annotation/VAR_009091|||http://purl.uniprot.org/annotation/VAR_009092|||http://purl.uniprot.org/annotation/VAR_009093|||http://purl.uniprot.org/annotation/VAR_009094|||http://purl.uniprot.org/annotation/VAR_009095|||http://purl.uniprot.org/annotation/VAR_009096|||http://purl.uniprot.org/annotation/VAR_009097|||http://purl.uniprot.org/annotation/VAR_009098|||http://purl.uniprot.org/annotation/VAR_009099|||http://purl.uniprot.org/annotation/VAR_009100|||http://purl.uniprot.org/annotation/VAR_009101|||http://purl.uniprot.org/annotation/VAR_009102|||http://purl.uniprot.org/annotation/VAR_023843|||http://purl.uniprot.org/annotation/VAR_023844|||http://purl.uniprot.org/annotation/VAR_023845|||http://purl.uniprot.org/annotation/VAR_023846|||http://purl.uniprot.org/annotation/VSP_039857|||http://purl.uniprot.org/annotation/VSP_044458
http://togogenome.org/gene/9606:GRHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZI5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases affinity for target DNA.|||Disordered|||Grainyhead-like protein 1 homolog|||Grh/CP2 DB|||In isoform 2.|||In isoform 3.|||Increases activity as transcriptional activator.|||Interaction with DNA|||Loss of activity as transcriptional activator. Nearly abolishes affinity for target DNA. Causes steric hindrance that impedes DNA-binding by neighboring residues.|||Loss of activity as transcriptional activator. Strongly decreases affinity for target DNA.|||No effect on affinity for target DNA.|||Phosphothreonine|||Reduces activity as transcriptional activator.|||Transcription activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227990|||http://purl.uniprot.org/annotation/VAR_025663|||http://purl.uniprot.org/annotation/VAR_025664|||http://purl.uniprot.org/annotation/VSP_017636|||http://purl.uniprot.org/annotation/VSP_017637|||http://purl.uniprot.org/annotation/VSP_017638|||http://purl.uniprot.org/annotation/VSP_017639
http://togogenome.org/gene/9606:FOXS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43638                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091893|||http://purl.uniprot.org/annotation/VAR_021844
http://togogenome.org/gene/9606:PDE11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCR9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A|||GAF 1|||GAF 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity.|||PDEase|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247040|||http://purl.uniprot.org/annotation/VAR_027056|||http://purl.uniprot.org/annotation/VAR_027057|||http://purl.uniprot.org/annotation/VSP_019898|||http://purl.uniprot.org/annotation/VSP_019899|||http://purl.uniprot.org/annotation/VSP_019900|||http://purl.uniprot.org/annotation/VSP_019901
http://togogenome.org/gene/9606:GPR22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV13|||http://purl.uniprot.org/uniprot/Q3KNS9|||http://purl.uniprot.org/uniprot/Q99680                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 22|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069543
http://togogenome.org/gene/9606:CTBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56545                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||C-terminal-binding protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076044|||http://purl.uniprot.org/annotation/VSP_027615|||http://purl.uniprot.org/annotation/VSP_058946
http://togogenome.org/gene/9606:OR1E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW81|||http://purl.uniprot.org/uniprot/P47887                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150428|||http://purl.uniprot.org/annotation/VAR_029292|||http://purl.uniprot.org/annotation/VAR_036207
http://togogenome.org/gene/9606:NME8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N427                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||NDK 1|||NDK 2|||NDK 3|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120156|||http://purl.uniprot.org/annotation/VAR_022766|||http://purl.uniprot.org/annotation/VAR_032948|||http://purl.uniprot.org/annotation/VAR_036171|||http://purl.uniprot.org/annotation/VAR_061898
http://togogenome.org/gene/9606:PPM1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4M2|||http://purl.uniprot.org/uniprot/O15297                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates phosphatase activity.|||Basic residues|||Disordered|||In BC; may be associated with disease susceptibility.|||In BC; may be associated with disease susceptibility; gain-of-function mutation that results in increased negative regulation of p53 expression in response to ionizing radiation exposure.|||In JDVS.|||In OC; may be associated with disease susceptibility.|||In isoform 2.|||Interaction with CHEK1|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Protein phosphatase 1D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057752|||http://purl.uniprot.org/annotation/VAR_070430|||http://purl.uniprot.org/annotation/VAR_080081|||http://purl.uniprot.org/annotation/VAR_080082|||http://purl.uniprot.org/annotation/VAR_080083|||http://purl.uniprot.org/annotation/VAR_080084|||http://purl.uniprot.org/annotation/VAR_080085|||http://purl.uniprot.org/annotation/VAR_080086|||http://purl.uniprot.org/annotation/VAR_080087|||http://purl.uniprot.org/annotation/VAR_080088|||http://purl.uniprot.org/annotation/VAR_080089|||http://purl.uniprot.org/annotation/VAR_080090|||http://purl.uniprot.org/annotation/VSP_056377|||http://purl.uniprot.org/annotation/VSP_056378
http://togogenome.org/gene/9606:ZBTB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y330                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Phosphothreonine|||Pro residues|||Zinc finger and BTB domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047728
http://togogenome.org/gene/9606:ZNF649                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BS31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Polar residues|||Zinc finger protein 649                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251224|||http://purl.uniprot.org/annotation/VAR_027668|||http://purl.uniprot.org/annotation/VAR_027669
http://togogenome.org/gene/9606:CTSO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43234                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Cathepsin O|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026321|||http://purl.uniprot.org/annotation/PRO_0000026322
http://togogenome.org/gene/9606:ULK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYT8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CTD-like region|||Decreased kinase activity and decreased autophosphorylation.|||Disordered|||In a metastatic melanoma sample; somatic mutation.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086782|||http://purl.uniprot.org/annotation/VAR_041281|||http://purl.uniprot.org/annotation/VAR_041282|||http://purl.uniprot.org/annotation/VAR_041283|||http://purl.uniprot.org/annotation/VAR_041284|||http://purl.uniprot.org/annotation/VAR_041285|||http://purl.uniprot.org/annotation/VAR_055287|||http://purl.uniprot.org/annotation/VAR_055288
http://togogenome.org/gene/9606:ARL13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H913                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 13A|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284145|||http://purl.uniprot.org/annotation/VSP_042678
http://togogenome.org/gene/9606:SLC30A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14863                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased homodimerization.|||Helical|||Lumenal|||Probable proton-coupled zinc antiporter SLC30A4|||Zinc binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206099
http://togogenome.org/gene/9606:PGK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00558|||http://purl.uniprot.org/uniprot/V9HWF4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In Munchen; 21% of activity.|||In PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens.|||In PGK1D; with chronic hemolytic anemia; variant Alabama.|||In PGK1D; with chronic hemolytic anemia; variant Antwerp.|||In PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity.|||In PGK1D; with chronic hemolytic anemia; variant Michigan.|||In PGK1D; with chronic hemolytic anemia; variant Shizuoka.|||In PGK1D; with chronic hemolytic anemia; variant Uppsala.|||In PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo.|||In PGK1D; with congenital non-spherocytic anemia; variant Matsue.|||In PGK1D; with rhabdomyolysis; variant Creteil.|||In isoform 2.|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoglycerate kinase 1|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145831|||http://purl.uniprot.org/annotation/VAR_006076|||http://purl.uniprot.org/annotation/VAR_006077|||http://purl.uniprot.org/annotation/VAR_006078|||http://purl.uniprot.org/annotation/VAR_006079|||http://purl.uniprot.org/annotation/VAR_006080|||http://purl.uniprot.org/annotation/VAR_006081|||http://purl.uniprot.org/annotation/VAR_006082|||http://purl.uniprot.org/annotation/VAR_006083|||http://purl.uniprot.org/annotation/VAR_006084|||http://purl.uniprot.org/annotation/VAR_006085|||http://purl.uniprot.org/annotation/VAR_006086|||http://purl.uniprot.org/annotation/VAR_006087|||http://purl.uniprot.org/annotation/VSP_056159
http://togogenome.org/gene/9606:CEP55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EZ4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with PDCD6IP.|||Centrosomal protein of 55 kDa|||Diminishes interaction with PDCD6IP.|||Disordered|||In MARCH.|||In MARCH; loss of protein localization to midbody ring; loss of function; fails to rescue craniofacial development when expressed in a zebrafish heterologous system.|||In isoform 2.|||Interaction with PDCD6IP|||Interaction with TSG101|||No effect on phosphorylation in mitotic cells.|||No effect on phosphorylation in mitotic cells. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-428.|||No effect on protein localization to midbody ring.|||No effect on protein localization to midbody ring; rescues craniofacial development when expressed in a zebrafish heterologous system.|||Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-425. Remains associated with the centrosome throughout mitosis; when associated with A-425. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-436.|||Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-428. Remains associated with the centrosome throughout mitosis; when associated with A-428. Arrests mitotic cells at the midbody stage; when associated with A-428 and A-436.|||Phosphoserine|||Phosphoserine; by CDK1 and MAPK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Polar residues|||Required for localization to the interphase centrosome and to the midbody during cytokinesis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089777|||http://purl.uniprot.org/annotation/VAR_022996|||http://purl.uniprot.org/annotation/VAR_022997|||http://purl.uniprot.org/annotation/VAR_026559|||http://purl.uniprot.org/annotation/VAR_056791|||http://purl.uniprot.org/annotation/VAR_079363|||http://purl.uniprot.org/annotation/VAR_079364|||http://purl.uniprot.org/annotation/VSP_014750|||http://purl.uniprot.org/annotation/VSP_014751
http://togogenome.org/gene/9606:SH3KBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQF6|||http://purl.uniprot.org/uniprot/B7Z6E8|||http://purl.uniprot.org/uniprot/Q5JPT6|||http://purl.uniprot.org/uniprot/Q96B97                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 domain-containing kinase-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097728|||http://purl.uniprot.org/annotation/VAR_015667|||http://purl.uniprot.org/annotation/VSP_007504|||http://purl.uniprot.org/annotation/VSP_044655|||http://purl.uniprot.org/annotation/VSP_044656
http://togogenome.org/gene/9606:TRIM71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2Q1W2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes repression on mRNA. Abolishes interaction with AGO2, PABPC1 and PUM2. Increases interaction with HSP90AA1.|||B box-type 1; atypical|||B box-type 2|||Decreases repression on mRNA. Abolishes interaction with AGO2, HSP90AA1, PABPC1 and PUM2.|||Decreases repression on mRNA. Decreases interaction with HSP90AA1. Abolishes interaction with PABPC1 and PUM2. Increases interaction with AGO2.|||Disordered|||E3 ubiquitin-protein ligase TRIM71|||Filamin|||In HYC4.|||N-acetylalanine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Polar residues|||Pro residues|||RING-type|||Removed|||Strongly decreases repression on mRNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279511|||http://purl.uniprot.org/annotation/VAR_083426|||http://purl.uniprot.org/annotation/VAR_083427
http://togogenome.org/gene/9606:UVRAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2Y5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by MTOR, decreases interaction with RUBCN, increases interaction with VPS16 and VPS39, promotes autophagosome maturation and endosome-lysosomal degradation of EGFR.|||C2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Required for interaction with PRKDC, XRCC6 and XRCC5|||Sufficient for interaction with STX7; VTI1B AND STX8|||Sufficient for interaction with VPS16, required for interaction with CEP63|||UV radiation resistance-associated gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065750|||http://purl.uniprot.org/annotation/VAR_059737|||http://purl.uniprot.org/annotation/VSP_056176
http://togogenome.org/gene/9606:FANCF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPI8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fanconi anemia group F protein|||Reduced monoubiquitination of FANCD2.|||Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-341.|||Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-344.|||Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-341 and A-344.|||Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-339; A-341 and A-344.|||Strongly reduced monoubiquitination of FANCD2; when associated with A-289; A-339; A-341 and A-344.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087188|||http://purl.uniprot.org/annotation/VAR_022270|||http://purl.uniprot.org/annotation/VAR_050988
http://togogenome.org/gene/9606:ELAPOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLZ2|||http://purl.uniprot.org/uniprot/B4DWM4|||http://purl.uniprot.org/uniprot/Q6UXG2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endosome/lysosome-associated apoptosis and autophagy regulator 1|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MRH|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286600|||http://purl.uniprot.org/annotation/VAR_032138|||http://purl.uniprot.org/annotation/VAR_032139|||http://purl.uniprot.org/annotation/VAR_032140|||http://purl.uniprot.org/annotation/VAR_035751|||http://purl.uniprot.org/annotation/VSP_025115|||http://purl.uniprot.org/annotation/VSP_025116|||http://purl.uniprot.org/annotation/VSP_025117
http://togogenome.org/gene/9606:E2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01094|||http://purl.uniprot.org/uniprot/Q9BSD8                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes acetylation; when associated with R-117 and R-120.|||Abolishes acetylation; when associated with R-117 and R-125.|||Abolishes acetylation; when associated with R-120 and R-125.|||Abolishes interaction with and repression of CEBPA and inhibition of adipogenesis.|||Abrogates in vitro phosphorylation by CHEK2 and CHEK2-dependent stabilization of E2F1 upon DNA damage.|||Abrogates methylation by SETD7. Loss of interaction with L3MBTL3. Loss of ubiquitination by the CRL4-DCAF5 E3 ubiquitin ligase complex.|||Cyclin A:CDK2 binding|||DEF box|||Decreased phosphorylation by GSK3B, leading to abolished interaction with USP11 and subsequent deubiquitination.|||Decreased phosphorylation by GSK3B.|||Dimerization|||Disordered|||Interaction with BIRC2/c-IAP1|||Leucine-zipper|||N6-acetyllysine|||N6-methyllysine; by SETD7|||No retinoblastoma protein binding. No effect on interaction with and repression of CEBPA.|||Phosphoserine|||Phosphoserine; by CHEK2|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by GSK3-beta|||RB1 binding|||Required for interaction with TRIM28|||Transactivation|||Transcription factor E2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219461|||http://purl.uniprot.org/annotation/VAR_013607|||http://purl.uniprot.org/annotation/VAR_013608|||http://purl.uniprot.org/annotation/VAR_013609|||http://purl.uniprot.org/annotation/VAR_013610|||http://purl.uniprot.org/annotation/VAR_048907
http://togogenome.org/gene/9606:ZNF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17030                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||KRAB|||Zinc finger protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047354|||http://purl.uniprot.org/annotation/VAR_035567|||http://purl.uniprot.org/annotation/VAR_035568|||http://purl.uniprot.org/annotation/VAR_052748|||http://purl.uniprot.org/annotation/VSP_007846|||http://purl.uniprot.org/annotation/VSP_007847
http://togogenome.org/gene/9606:C22orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Uncharacterized protein C22orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079576|||http://purl.uniprot.org/annotation/VSP_014462|||http://purl.uniprot.org/annotation/VSP_014463
http://togogenome.org/gene/9606:TEKT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M29                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Tektin-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261171|||http://purl.uniprot.org/annotation/VAR_053722|||http://purl.uniprot.org/annotation/VAR_053723|||http://purl.uniprot.org/annotation/VAR_053724|||http://purl.uniprot.org/annotation/VAR_053725
http://togogenome.org/gene/9606:C1orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV19                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C1orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251189|||http://purl.uniprot.org/annotation/VAR_054409
http://togogenome.org/gene/9606:NSF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTI6|||http://purl.uniprot.org/uniprot/P46459                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||CDC48|||CDC48 N-terminal subdomain|||In DEE96.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CDK16|||Phosphotyrosine|||Vesicle-fusing ATPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084563|||http://purl.uniprot.org/annotation/VAR_029580|||http://purl.uniprot.org/annotation/VAR_085695|||http://purl.uniprot.org/annotation/VAR_085696|||http://purl.uniprot.org/annotation/VSP_056420|||http://purl.uniprot.org/annotation/VSP_056421
http://togogenome.org/gene/9606:PTPRU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92729                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like C2-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1380.|||MAM|||Mediates interaction with CTNNB1|||N-linked (GlcNAc...) asparagine|||No effect on phosphatase activity toward CTNNB1. Loss of the inhibitory effect on CTNNB1 transcriptional activity without effect on interaction with CTNNB1; when associated with S-1085.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Receptor-type tyrosine-protein phosphatase U|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000371658|||http://purl.uniprot.org/annotation/VAR_035650|||http://purl.uniprot.org/annotation/VAR_035651|||http://purl.uniprot.org/annotation/VAR_035652|||http://purl.uniprot.org/annotation/VAR_055075|||http://purl.uniprot.org/annotation/VAR_055076|||http://purl.uniprot.org/annotation/VAR_055077|||http://purl.uniprot.org/annotation/VSP_037082|||http://purl.uniprot.org/annotation/VSP_037083|||http://purl.uniprot.org/annotation/VSP_037084|||http://purl.uniprot.org/annotation/VSP_037085
http://togogenome.org/gene/9606:KCNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14721                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FFAT|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In DEE26; change in the ion selectivity from potassium-selective to nonselective cation channels and significant decrease in cell membrane localization.|||In DEE26; dominant-negative mutation resulting in loss of endogenous channel currents and greatly suppresses repetitive firing in cultured cortical neurons.|||In DEE26; inhibits ion selectivity and gain of a depolarizing inward cation conductance; trafficks normally to the cell surface.|||In DEE26; reduces sensitivity and cooperativity of the voltage sensor for channel opening and greatly suppresses repetitive firing in cultured cortical neurons.|||Increases channel activity.|||No effect on channel activity.|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CDK5, MAPK14; in vitro|||Phosphoserine; by CDK5; in vitro|||Phosphotyrosine; by Src|||Polar residues|||Potassium voltage-gated channel subfamily B member 1|||Reduces channel activity. Inhibits interaction with KCNG4. Impairs hetetrotetramerization with KCNG1, KCNG3 or KCNG4. Does not impair homotetramerization.|||Reduces interaction with KCNG1 and self-interaction and impairs plasma membrane subcellular localization, homotetramerization and hetetrotetramerization with KCNG4; when associated with R-74.|||Reduces interaction with KCNG1 and self-interaction and impairs plasma membrane subcellular localization, homotetramerization and hetetrotetramerization with KCNG4; when associated with R-75.|||Selectivity filter|||Self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054042|||http://purl.uniprot.org/annotation/VAR_034049|||http://purl.uniprot.org/annotation/VAR_062182|||http://purl.uniprot.org/annotation/VAR_062183|||http://purl.uniprot.org/annotation/VAR_062184|||http://purl.uniprot.org/annotation/VAR_071991|||http://purl.uniprot.org/annotation/VAR_071992|||http://purl.uniprot.org/annotation/VAR_071993|||http://purl.uniprot.org/annotation/VAR_075573|||http://purl.uniprot.org/annotation/VAR_075574|||http://purl.uniprot.org/annotation/VAR_075575
http://togogenome.org/gene/9606:MC3R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41968                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with susceptibility to obesity; completely lacks signaling in response to agonist stimulation; coexpression of the wild-type and the mutant receptor shows that it does not exert dominant-negative activity on wild-type.|||Associated with susceptibility to obesity; in vitro expression studies demonstrate that the mutation causes complete loss of function; transfected cells show diffuse cytoplasmic staining indicating intracellular retention of the receptor.|||Cytoplasmic|||Extracellular|||Have ligand binding and signaling properties similar to wild-type.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melanocortin receptor 3|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069718|||http://purl.uniprot.org/annotation/VAR_020070|||http://purl.uniprot.org/annotation/VAR_055000|||http://purl.uniprot.org/annotation/VAR_055001
http://togogenome.org/gene/9606:LRP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14114                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to myocardial infarction type 1; increases activation of MAPK14 by oxidized low density lipoprotein.|||Clustered O-linked oligosaccharides|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||Low-density lipoprotein receptor-related protein 8|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017332|||http://purl.uniprot.org/annotation/VAR_018468|||http://purl.uniprot.org/annotation/VAR_018469|||http://purl.uniprot.org/annotation/VAR_037624|||http://purl.uniprot.org/annotation/VAR_037625|||http://purl.uniprot.org/annotation/VAR_037626|||http://purl.uniprot.org/annotation/VAR_037627|||http://purl.uniprot.org/annotation/VAR_037628|||http://purl.uniprot.org/annotation/VAR_046974|||http://purl.uniprot.org/annotation/VAR_059079|||http://purl.uniprot.org/annotation/VSP_010305|||http://purl.uniprot.org/annotation/VSP_010306|||http://purl.uniprot.org/annotation/VSP_010307|||http://purl.uniprot.org/annotation/VSP_010308|||http://purl.uniprot.org/annotation/VSP_038181
http://togogenome.org/gene/9606:STRBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SI9|||http://purl.uniprot.org/uniprot/V9HWK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||DRBM|||DRBM 1|||DRBM 2|||DZF|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||Spermatid perinuclear RNA-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274917|||http://purl.uniprot.org/annotation/VAR_035662|||http://purl.uniprot.org/annotation/VSP_022937
http://togogenome.org/gene/9606:PYGO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Almost complete loss of interaction with H3K4me2.|||Disordered|||In isoform 2.|||Interaction with BCL9|||Interaction with H3K4me2|||Loss of interaction with H3K4me2.|||Nuclear localization signal|||PHD-type|||Polar residues|||Pygopus homolog 1|||Reduces interaction with H3K4me2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097121|||http://purl.uniprot.org/annotation/VAR_051292|||http://purl.uniprot.org/annotation/VSP_056648
http://togogenome.org/gene/9606:ANKRD54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NXT1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 54|||Disordered|||In isoform 2.|||LYN-binding|||N-acetylalanine|||Nuclear export signal (NES)|||Nuclear localization signal (NLS)|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274493|||http://purl.uniprot.org/annotation/VSP_022770|||http://purl.uniprot.org/annotation/VSP_022771
http://togogenome.org/gene/9606:GSPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic peptide chain release factor GTP-binding subunit ERF3B|||G1|||G2|||G3|||G4|||G5|||Impairs interaction with UPF1 and PABPC1; when associated with A-55, K-56 and A-59.|||Impairs interaction with UPF1 and PABPC1; when associated with K-52, A-55 and K-56.|||Impairs interaction with UPF1 and PABPC1; when associated with K-52, K-56 and A-59.|||Impairs interaction with UPF1 and PABPC1; when associated with K52, A-55, and A-59.|||Polar residues|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327256|||http://purl.uniprot.org/annotation/VAR_042431
http://togogenome.org/gene/9606:LZIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZA0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein LZIC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263691|||http://purl.uniprot.org/annotation/VAR_053371|||http://purl.uniprot.org/annotation/VSP_056083
http://togogenome.org/gene/9606:FYN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06241                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine; by PKC|||Phosphotyrosine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine|||SH2|||SH3|||Tyrosine-protein kinase Fyn                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088099|||http://purl.uniprot.org/annotation/VAR_014661|||http://purl.uniprot.org/annotation/VAR_041704|||http://purl.uniprot.org/annotation/VAR_041705|||http://purl.uniprot.org/annotation/VAR_041706|||http://purl.uniprot.org/annotation/VSP_024108|||http://purl.uniprot.org/annotation/VSP_024110
http://togogenome.org/gene/9606:CLDN18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56856                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-18|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform A2.|||Phosphoserine|||Required for role in regulation of RANKL-induced osteoclast differentiation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144779|||http://purl.uniprot.org/annotation/VAR_033775|||http://purl.uniprot.org/annotation/VSP_001102
http://togogenome.org/gene/9606:TMEM181                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2C4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Pro residues|||Transmembrane protein 181                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239661
http://togogenome.org/gene/9606:ABI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2A4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ABI gene family member 3|||Disordered|||In isoform 2.|||Phosphoserine|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191792|||http://purl.uniprot.org/annotation/VAR_022030|||http://purl.uniprot.org/annotation/VAR_060243|||http://purl.uniprot.org/annotation/VAR_060993|||http://purl.uniprot.org/annotation/VSP_041467
http://togogenome.org/gene/9606:AADACL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUY2                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Motif|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Arylacetamide deacetylase-like 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265937
http://togogenome.org/gene/9606:EML4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC35                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Breakpoint for translocation to form the EML4-ALK fusion protein (variant 1)|||Breakpoint for translocation to form the EML4-ALK fusion protein (variant 2)|||Disordered|||Echinoderm microtubule-associated protein-like 4|||In isoform 2.|||Microtubule-binding|||N-acetylmethionine|||Phosphomimetic mutant which shows reduced localization to microtubules during interphase; when associated with D-144.|||Phosphomimetic mutant which shows reduced localization to microtubules during interphase; when associated with D-146.|||Phosphorylation-deficient mutant which shows increased localization to microtubules during mitosis, increased microtubule stability and impaired chromosome congression; when associated with A-144.|||Phosphorylation-deficient mutant which shows increased localization to microtubules during mitosis, increased microtubule stability and impaired chromosome congression; when associated with A-146.|||Phosphoserine|||Phosphoserine; by NEK6|||Phosphoserine; by NEK6 and NEK7|||Phosphoserine; by NEK7|||Phosphothreonine|||Phosphothreonine; by NEK6|||Phosphothreonine; by NEK6 and NEK7|||Phosphotyrosine|||Polar residues|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050963|||http://purl.uniprot.org/annotation/VAR_031726|||http://purl.uniprot.org/annotation/VAR_031727|||http://purl.uniprot.org/annotation/VAR_031728|||http://purl.uniprot.org/annotation/VAR_031729|||http://purl.uniprot.org/annotation/VSP_047192
http://togogenome.org/gene/9606:LRRC8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1C7|||http://purl.uniprot.org/uniprot/Q8IWT6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished ability to transport 2'-3'-cGAMP.|||Abolished localization to lysosomes.|||Abolishes N-glycosylation; when associated with A-66.|||Abolishes N-glycosylation; when associated with A-83.|||Affects ion selectivity of the channel.|||Altered anion selectivity.|||Anion channel is more selective to iodite compared to chloride.|||Cytoplasmic|||Decreased amplitudes of swelling-activated currents.|||Di-leucine motif|||Extracellular|||Found in a patient with Sertoli cell-only syndrome; unknown pathological significance.|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRC8 pannexin-like TM region|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||No effect.|||Phosphoserine|||Phosphothreonine|||Required for anion selectivity|||Volume-regulated anion channel subunit LRRC8A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084499|||http://purl.uniprot.org/annotation/VAR_084194
http://togogenome.org/gene/9606:GDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2T3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Guanine deaminase|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122298|||http://purl.uniprot.org/annotation/VSP_042075|||http://purl.uniprot.org/annotation/VSP_042076
http://togogenome.org/gene/9606:MT1M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N339                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223180|||http://purl.uniprot.org/annotation/VAR_025310
http://togogenome.org/gene/9606:PTP4A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12974                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Locates in the nucleus and cytosol. No interaction with RABGGTB.|||No effect on interaction with RABGGTB.|||Phosphocysteine intermediate|||Protein tyrosine phosphatase type IVA 2|||Proton donor|||Removed in mature form|||S-farnesyl cysteine|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094785|||http://purl.uniprot.org/annotation/PRO_0000396731|||http://purl.uniprot.org/annotation/VSP_014404|||http://purl.uniprot.org/annotation/VSP_014405|||http://purl.uniprot.org/annotation/VSP_044813|||http://purl.uniprot.org/annotation/VSP_055056
http://togogenome.org/gene/9606:ACTRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYD9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-related protein T3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089142|||http://purl.uniprot.org/annotation/VAR_055483
http://togogenome.org/gene/9606:H2BC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4S9|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A/H2B/H3|||Histone H2B type 1-C/E/F/G/I|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:SLC2A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PXP3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished fructose transport.|||Cytoplasmic|||Disordered|||Does not affect glucose or fructose transport.|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317274|||http://purl.uniprot.org/annotation/VAR_052504|||http://purl.uniprot.org/annotation/VAR_061879
http://togogenome.org/gene/9606:RNF166                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A37                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC RNF-type|||Complete loss of SQSTM1 ubiquitination; in association with A-33.|||Complete loss of SQSTM1 ubiquitination; in association with A-36.|||E3 ubiquitin-protein ligase RNF166|||In isoform 2.|||In isoform 3.|||RING-type|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245588|||http://purl.uniprot.org/annotation/VSP_019750|||http://purl.uniprot.org/annotation/VSP_046147
http://togogenome.org/gene/9606:APCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02743|||http://purl.uniprot.org/uniprot/V9HWP0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Pentraxin (PTX)|||Pentraxin family member|||Serum amyloid P-component|||Serum amyloid P-component(1-203)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000169|||http://purl.uniprot.org/annotation/PRO_0000023540|||http://purl.uniprot.org/annotation/PRO_0000023541|||http://purl.uniprot.org/annotation/PRO_5014206133|||http://purl.uniprot.org/annotation/VAR_006054|||http://purl.uniprot.org/annotation/VAR_006055|||http://purl.uniprot.org/annotation/VAR_035814
http://togogenome.org/gene/9606:PCDHGB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003974|||http://purl.uniprot.org/annotation/VAR_048568|||http://purl.uniprot.org/annotation/VAR_061071|||http://purl.uniprot.org/annotation/VAR_061072|||http://purl.uniprot.org/annotation/VSP_008686|||http://purl.uniprot.org/annotation/VSP_008687
http://togogenome.org/gene/9606:DDHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEL9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DDHD|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Markedly decreased enzymatic activity.|||No effect on enzymatic activity.|||No effect on homooligomer formation; when associated with S-590.|||No effect on homooligomer formation; when associated with S-593.|||Phospholipase DDHD1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079845|||http://purl.uniprot.org/annotation/VSP_008628|||http://purl.uniprot.org/annotation/VSP_008629|||http://purl.uniprot.org/annotation/VSP_045340
http://togogenome.org/gene/9606:TXNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43396|||http://purl.uniprot.org/uniprot/V9HW51                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  PITH|||Phosphoserine|||Redox-active|||Removed|||Thioredoxin|||Thioredoxin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120016
http://togogenome.org/gene/9606:ATRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ36|||http://purl.uniprot.org/uniprot/O75882                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Attractin|||C-type lectin|||CUB|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 2|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||PSI 1|||PSI 2|||PSI 3|||PSI 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007483|||http://purl.uniprot.org/annotation/PRO_0000394771|||http://purl.uniprot.org/annotation/VAR_048967|||http://purl.uniprot.org/annotation/VAR_048968|||http://purl.uniprot.org/annotation/VAR_048969|||http://purl.uniprot.org/annotation/VAR_048970|||http://purl.uniprot.org/annotation/VSP_001372|||http://purl.uniprot.org/annotation/VSP_001375
http://togogenome.org/gene/9606:TRIM47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LD4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM47|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056270|||http://purl.uniprot.org/annotation/VAR_057223|||http://purl.uniprot.org/annotation/VSP_055440
http://togogenome.org/gene/9606:NFASC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRH7|||http://purl.uniprot.org/uniprot/O94856                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In NEDCPMD; decreased protein abundance in patient-derived cells; decreased cell surface localization; unknown pathological significance.|||In NEDCPMD; no protein expression; unknown pathological significance.|||In NEDCPMD; unknown pathological significance.|||In isoform 13.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 5, isoform 8 and isoform 10.|||In isoform 3, isoform 8 and isoform 11.|||In isoform 3, isoform 8, isoform 10 and isoform 11.|||In isoform 4, isoform 9 and isoform 12.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8, isoform 10, isoform 11 and isoform 12.|||N-linked (GlcNAc...) asparagine|||Neurofascin|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015049|||http://purl.uniprot.org/annotation/VAR_017251|||http://purl.uniprot.org/annotation/VAR_083116|||http://purl.uniprot.org/annotation/VAR_083117|||http://purl.uniprot.org/annotation/VAR_083118|||http://purl.uniprot.org/annotation/VSP_008937|||http://purl.uniprot.org/annotation/VSP_008938|||http://purl.uniprot.org/annotation/VSP_008940|||http://purl.uniprot.org/annotation/VSP_016424|||http://purl.uniprot.org/annotation/VSP_016425|||http://purl.uniprot.org/annotation/VSP_016426|||http://purl.uniprot.org/annotation/VSP_016427|||http://purl.uniprot.org/annotation/VSP_016428|||http://purl.uniprot.org/annotation/VSP_016429|||http://purl.uniprot.org/annotation/VSP_016430|||http://purl.uniprot.org/annotation/VSP_016431|||http://purl.uniprot.org/annotation/VSP_016432|||http://purl.uniprot.org/annotation/VSP_016433|||http://purl.uniprot.org/annotation/VSP_016434
http://togogenome.org/gene/9606:ZNF699                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32M78                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||KRAB|||Zinc finger protein 699                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233279
http://togogenome.org/gene/9606:ENPEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07075                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binds calcium which modulates its enzyme activity|||Cytoplasmic|||Disordered|||Extracellular|||Glutamyl aminopeptidase|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Polar residues|||Proton acceptor|||Reduced enzyme activity.|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095095|||http://purl.uniprot.org/annotation/VAR_030359|||http://purl.uniprot.org/annotation/VAR_030360|||http://purl.uniprot.org/annotation/VAR_036047|||http://purl.uniprot.org/annotation/VAR_057056|||http://purl.uniprot.org/annotation/VAR_057057
http://togogenome.org/gene/9606:PHF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R336|||http://purl.uniprot.org/uniprot/A8K856|||http://purl.uniprot.org/uniprot/Q9BWX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC pre-PHD-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||PHD finger protein 7|||PHD-type|||RING-type|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055996|||http://purl.uniprot.org/annotation/VAR_035957|||http://purl.uniprot.org/annotation/VSP_046255
http://togogenome.org/gene/9606:MAT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00266                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Flexible loop|||In MATD.|||In MATD; abolishes enzyme activity.|||In MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme.|||In MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme.|||In MATD; dominant mutation.|||In MATD; has virtually no enzymatic activity.|||In MATD; retains 11% of wild-type activity.|||In MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme.|||S-adenosylmethionine synthase isoform type-1|||S-nitrosocysteine|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174432|||http://purl.uniprot.org/annotation/VAR_006935|||http://purl.uniprot.org/annotation/VAR_006936|||http://purl.uniprot.org/annotation/VAR_006937|||http://purl.uniprot.org/annotation/VAR_006938|||http://purl.uniprot.org/annotation/VAR_006939|||http://purl.uniprot.org/annotation/VAR_006940|||http://purl.uniprot.org/annotation/VAR_006941|||http://purl.uniprot.org/annotation/VAR_006942|||http://purl.uniprot.org/annotation/VAR_028944|||http://purl.uniprot.org/annotation/VAR_031242|||http://purl.uniprot.org/annotation/VAR_031243|||http://purl.uniprot.org/annotation/VAR_031244|||http://purl.uniprot.org/annotation/VAR_031245
http://togogenome.org/gene/9606:SLC25A24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUK1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-terminal transmembrane transporter domain|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In FPS.|||In FPS; no effect on protein abundance; no effect on localization to the mitochondrion; altered mitochondrial ATP transport; increased sensitivity to oxidative stress that leads to mitochondrial swelling.|||In isoform 2.|||Linker region|||Mitochondrial adenyl nucleotide antiporter SLC25A24|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Regulatory N-terminal domain|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317594|||http://purl.uniprot.org/annotation/VAR_080617|||http://purl.uniprot.org/annotation/VAR_080618|||http://purl.uniprot.org/annotation/VSP_031066
http://togogenome.org/gene/9606:CRLF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUI8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytokine receptor-like factor 3|||Fibronectin type-III|||In isoform 2.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288936|||http://purl.uniprot.org/annotation/VAR_032539|||http://purl.uniprot.org/annotation/VAR_049180|||http://purl.uniprot.org/annotation/VSP_044648
http://togogenome.org/gene/9606:SDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18827                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (heparan sulfate) serine|||Phosphoserine|||Polar residues|||Syndecan-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033499|||http://purl.uniprot.org/annotation/VAR_052242|||http://purl.uniprot.org/annotation/VAR_052243
http://togogenome.org/gene/9606:NKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969G9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||EF-hand|||Interaction with DVL1, DVL2 and DVL3|||N-myristoyl glycine|||Polar residues|||Protein naked cuticle homolog 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301990
http://togogenome.org/gene/9606:ZMYND11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15326|||http://purl.uniprot.org/uniprot/Q5BJG6|||http://purl.uniprot.org/uniprot/Q5UGI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abolished interaction with PXLXP ligand proteins.|||Abolishes binding to DNA. No effect on nuclear location.|||Abolishes interaction with Histone 3. Diffused distribution in the nucleus.|||Abrogates binding to EZH2.|||Basic and acidic residues|||Bromo|||Decreases binding to DNA.|||Decreases interaction with Epstein-Barr virus EBNA2 protein.|||Diffused distribution in the nucleus.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly decreases interaction with Epstein-Barr virus EBNA2 protein.|||Highly decreases interaction with Epstein-Barr virus EBNA2 protein. Almost abolishes interaction with Epstein-Barr virus EBNA2 protein and inhibition of EBNA2-mediated transcriptional activation; when associated with A-590.|||Highly decreases interaction with Epstein-Barr virus EBNA2 protein. No effect on the inhibition of EBNA2-mediated transcriptional activation. Almost abolishes interaction with Epstein-Barr virus EBNA2 protein and inhibition of EBNA2-mediated transcriptional activation; when associated with A-590.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6.|||Interaction with human adenovirus E1A|||MYND-type|||No effect on interaction with Histone 3. Abolishes binding to DNA. Changes location from nuclear to cytoplasmic.|||No effect on nuclear location.|||Nuclear localization signal|||PHD-type|||PWWP|||Phosphoserine|||Polar residues|||Reduced interaction with PXLXP ligand MGA without affecting interaction with viral human adenovirus early E1A protein.|||Reduced interaction with PXLXP ligand proteins.|||SAMD1-like winged helix (WH)|||Zinc finger MYND domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211218|||http://purl.uniprot.org/annotation/VSP_044482|||http://purl.uniprot.org/annotation/VSP_044483|||http://purl.uniprot.org/annotation/VSP_046246|||http://purl.uniprot.org/annotation/VSP_047209
http://togogenome.org/gene/9606:C12orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VV63|||http://purl.uniprot.org/uniprot/Q96LP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Uncharacterized protein C12orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274274|||http://purl.uniprot.org/annotation/VAR_030229|||http://purl.uniprot.org/annotation/VAR_030230|||http://purl.uniprot.org/annotation/VSP_022691|||http://purl.uniprot.org/annotation/VSP_022692|||http://purl.uniprot.org/annotation/VSP_022693
http://togogenome.org/gene/9606:ZNF653                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Nuclear localization signal|||Polar residues|||Zinc finger protein 653                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253344|||http://purl.uniprot.org/annotation/VAR_028076|||http://purl.uniprot.org/annotation/VAR_057438
http://togogenome.org/gene/9606:SSC5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4H1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||SRCR 5|||Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332985|||http://purl.uniprot.org/annotation/VSP_040792|||http://purl.uniprot.org/annotation/VSP_040793
http://togogenome.org/gene/9606:C5AR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P296                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C5a anaphylatoxin chemotactic receptor 2|||Cytoplasmic|||Extracellular|||Found in a family with familial combined hyperlipemia; unknown pathological significance; associated with increased plasma triglyceride, plasma cholesterol, low-density lipoprotein cholesterol, apolipoprotein B and ASP.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069216|||http://purl.uniprot.org/annotation/VAR_068748|||http://purl.uniprot.org/annotation/VAR_068749
http://togogenome.org/gene/9606:SFXN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIJ8|||http://purl.uniprot.org/uniprot/B8ZZJ6|||http://purl.uniprot.org/uniprot/Q8TD22                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Sideroflexin-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000177043
http://togogenome.org/gene/9606:CCSAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centriole, cilia and spindle-associated protein|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Pro residues|||ST]-E-Y-X(3)-Y motif 1; required for efficient microtubule binding and stabilization|||ST]-E-Y-X(3)-Y motif 2; required for efficient microtubule binding and stabilization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284643|||http://purl.uniprot.org/annotation/VAR_059594|||http://purl.uniprot.org/annotation/VSP_024582|||http://purl.uniprot.org/annotation/VSP_024583|||http://purl.uniprot.org/annotation/VSP_024584|||http://purl.uniprot.org/annotation/VSP_024585|||http://purl.uniprot.org/annotation/VSP_024586|||http://purl.uniprot.org/annotation/VSP_024587
http://togogenome.org/gene/9606:LGALS9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B8N2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Galectin 1|||Galectin 2|||Galectin-9B|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321949|||http://purl.uniprot.org/annotation/VSP_035176
http://togogenome.org/gene/9606:FOSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53539                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||In isoform 10.|||In isoform 11.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 4, isoform 6, isoform 7 and isoform 9.|||In isoform 8 and isoform 9.|||Interchain (with C-285 in JUND)|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||Protein FosB|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076476|||http://purl.uniprot.org/annotation/VAR_022286|||http://purl.uniprot.org/annotation/VSP_046167|||http://purl.uniprot.org/annotation/VSP_055562|||http://purl.uniprot.org/annotation/VSP_055563|||http://purl.uniprot.org/annotation/VSP_055564|||http://purl.uniprot.org/annotation/VSP_055565|||http://purl.uniprot.org/annotation/VSP_061374
http://togogenome.org/gene/9606:NBDY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRE5|||http://purl.uniprot.org/uniprot/A0A4P8PLQ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Disordered|||Impaired interaction with EDC4.|||Negative regulator of P-body association|||No effect on interaction with EDC4.|||Required for interaction with EDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000439205
http://togogenome.org/gene/9606:ICAM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32942                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Intercellular adhesion molecule 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014794|||http://purl.uniprot.org/annotation/VAR_024498|||http://purl.uniprot.org/annotation/VAR_046547|||http://purl.uniprot.org/annotation/VAR_046548|||http://purl.uniprot.org/annotation/VAR_059394
http://togogenome.org/gene/9606:ZNF692                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU19                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Does not affect phosphorylation by AMPK.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues|||Reduces phosphorylation by AMPK. Does not affect DNA binding. Does not repress transcription of PCK1.|||Zinc finger protein 692                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234014|||http://purl.uniprot.org/annotation/VAR_033590|||http://purl.uniprot.org/annotation/VSP_018185|||http://purl.uniprot.org/annotation/VSP_018186|||http://purl.uniprot.org/annotation/VSP_018187|||http://purl.uniprot.org/annotation/VSP_018188|||http://purl.uniprot.org/annotation/VSP_043025
http://togogenome.org/gene/9606:HAVCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes TCR-induced NFAT activation; when associated with A-265.|||Abolishes TCR-induced NFAT activation; when associated with A-272.|||Cytoplasmic|||Extracellular|||Helical|||Hepatitis A virus cellular receptor 2|||Ig-like V-type|||In SPTCL; associated with disease susceptibility; affects protein folding; decreased localization at the cell membrane.|||In SPTCL; associated with disease susceptibility; results in dysregulated secretion of inflammatory cytokines by macrophages; affects protein folding; decreased localization at the cell membrane.|||In SPTCL; may be associated with disease susceptibility.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on TCR-induced NFAT activation (phosphomimetic mutation); when associated with E-265.|||No effect on TCR-induced NFAT activation (phosphomimetic mutation); when associated with E-272.|||O-linked (GalNAc...) threonine|||Phosphotyrosine; by ITK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042101|||http://purl.uniprot.org/annotation/VAR_025342|||http://purl.uniprot.org/annotation/VAR_082211|||http://purl.uniprot.org/annotation/VAR_082212|||http://purl.uniprot.org/annotation/VAR_082213|||http://purl.uniprot.org/annotation/VSP_017287|||http://purl.uniprot.org/annotation/VSP_017288
http://togogenome.org/gene/9606:GGCX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5QJA4|||http://purl.uniprot.org/uniprot/P38435                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In PXEL-MCFD.|||In VKCFD1.|||In VKCFD1; affects glutamate binding.|||In isoform 2.|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||No activity.|||No effect on activity.|||Polar residues|||Proton acceptor|||Removed|||Vitamin K-dependent gamma-carboxylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191823|||http://purl.uniprot.org/annotation/VAR_005780|||http://purl.uniprot.org/annotation/VAR_005781|||http://purl.uniprot.org/annotation/VAR_015218|||http://purl.uniprot.org/annotation/VAR_021826|||http://purl.uniprot.org/annotation/VAR_032979|||http://purl.uniprot.org/annotation/VAR_032980|||http://purl.uniprot.org/annotation/VAR_032981|||http://purl.uniprot.org/annotation/VAR_032982|||http://purl.uniprot.org/annotation/VAR_032983|||http://purl.uniprot.org/annotation/VSP_046179
http://togogenome.org/gene/9606:ACHE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22303                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acetylcholinesterase|||Acyl-ester intermediate|||Charge relay system|||GPI-anchor amidated glycine|||Impairment of interchain disulfide bridge formation.|||In Yt(b) antigen.|||In isoform 4.|||In isoform H.|||In isoform R.|||Interchain|||Loss of activity.|||Misfolding, absence of secretion.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008587|||http://purl.uniprot.org/annotation/VAR_002359|||http://purl.uniprot.org/annotation/VAR_011934|||http://purl.uniprot.org/annotation/VAR_021325|||http://purl.uniprot.org/annotation/VAR_021326|||http://purl.uniprot.org/annotation/VSP_001457|||http://purl.uniprot.org/annotation/VSP_035568|||http://purl.uniprot.org/annotation/VSP_035569|||http://purl.uniprot.org/annotation/VSP_035570
http://togogenome.org/gene/9606:RPL35A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18077                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In DBA5.|||In DBA5; may result in aberrant splicing.|||Large ribosomal subunit protein eL33|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192796|||http://purl.uniprot.org/annotation/VAR_055446|||http://purl.uniprot.org/annotation/VAR_055447
http://togogenome.org/gene/9606:EOLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HY62|||http://purl.uniprot.org/uniprot/Q96DE9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  ASCH|||Protein EOLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079741
http://togogenome.org/gene/9606:GTF2H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTQ8|||http://purl.uniprot.org/uniprot/P32780                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BSD|||BSD 1|||BSD 2|||Disordered|||General transcription factor IIH subunit 1|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119245|||http://purl.uniprot.org/annotation/VAR_014345|||http://purl.uniprot.org/annotation/VAR_014346|||http://purl.uniprot.org/annotation/VAR_014347|||http://purl.uniprot.org/annotation/VSP_056562
http://togogenome.org/gene/9606:CYP3A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24462                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 3A7|||Has no effect on catalytic activity.|||In isoform 2.|||Increases catalytic activity.|||Reduces affinity for substrate and catalytic efficiency.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051790|||http://purl.uniprot.org/annotation/VAR_020124|||http://purl.uniprot.org/annotation/VAR_055564|||http://purl.uniprot.org/annotation/VSP_055577
http://togogenome.org/gene/9606:OIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43482                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site                                                                                  ^@                                                                                  Abolishes interaction with MIS18A; when associated with D-172.|||Abolishes interaction with MIS18A; when associated with E-77.|||Mis18|||Phosphoserine|||Phosphothreonine|||Protein Mis18-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058038
http://togogenome.org/gene/9606:B3GALT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L58                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyltransferase 6|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In ALGAZ; normal Golgi apparatus subcellular localization; proteoglycans maturation altered.|||In ALGAZ; unknown pathological significance; normal Golgi apparatus subcellular localization.|||In EDSSPD2.|||In EDSSPD2; no effect on Golgi apparatus subcellular localization.|||In EDSSPD2; normal Golgi apparatus subcellular localization.|||In EDSSPD2; unknown pathological significance.|||In SEMDJL1; also found in patients with EDSSPD2; decreased localization to the Golgi apparatus.|||In SEMDJL1; decreased galactosylxylosylprotein 3-beta-galactosyltransferase activity; decreased localization to the Golgi apparatus.|||In SEMDJL1; decreased localization to the Golgi apparatus.|||In SEMDJL1; loss of galactosylxylosylprotein 3-beta-galactosyltransferase activity; decreased localization to the Golgi apparatus.|||In SEMDJL1; loss of galactosylxylosylprotein 3-beta-galactosyltransferase activity; normal Golgi apparatus subcellular localization.|||In SEMDJL1; normal Golgi apparatus subcellular localization.|||In SEMDJL1; the activity of the enzyme is significantly decreased; decreased localization to the Golgi apparatus.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219168|||http://purl.uniprot.org/annotation/VAR_059317|||http://purl.uniprot.org/annotation/VAR_070132|||http://purl.uniprot.org/annotation/VAR_070133|||http://purl.uniprot.org/annotation/VAR_070134|||http://purl.uniprot.org/annotation/VAR_070135|||http://purl.uniprot.org/annotation/VAR_070136|||http://purl.uniprot.org/annotation/VAR_070137|||http://purl.uniprot.org/annotation/VAR_070138|||http://purl.uniprot.org/annotation/VAR_070139|||http://purl.uniprot.org/annotation/VAR_070140|||http://purl.uniprot.org/annotation/VAR_070141|||http://purl.uniprot.org/annotation/VAR_084154|||http://purl.uniprot.org/annotation/VAR_084155|||http://purl.uniprot.org/annotation/VAR_084156|||http://purl.uniprot.org/annotation/VAR_084157|||http://purl.uniprot.org/annotation/VAR_084158|||http://purl.uniprot.org/annotation/VAR_084159|||http://purl.uniprot.org/annotation/VAR_084160
http://togogenome.org/gene/9606:SFTPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35247                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||Basic and acidic residues|||C-type lectin|||Collagen-like|||Disordered|||N-linked (GlcNAc...) asparagine|||Pro residues|||Pulmonary surfactant-associated protein D|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017465|||http://purl.uniprot.org/annotation/VAR_020937|||http://purl.uniprot.org/annotation/VAR_020938|||http://purl.uniprot.org/annotation/VAR_020939|||http://purl.uniprot.org/annotation/VAR_020940|||http://purl.uniprot.org/annotation/VAR_020941
http://togogenome.org/gene/9606:PDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1N1|||http://purl.uniprot.org/uniprot/Q9P0J1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In PDP deficiency; low activity.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||PPM-type phosphatase|||[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025419|||http://purl.uniprot.org/annotation/VAR_029882|||http://purl.uniprot.org/annotation/VSP_046869
http://togogenome.org/gene/9606:TERF2IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Myb-like|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Removed|||Telomeric repeat-binding factor 2-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197126|||http://purl.uniprot.org/annotation/VAR_050195
http://togogenome.org/gene/9606:SPCS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61009                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Signal peptidase complex subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218938
http://togogenome.org/gene/9606:TNFRSF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J9PH39|||http://purl.uniprot.org/uniprot/P19438                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolished GlcNAcylation by E.coli NleB1.|||Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||In FPF.|||In FPF; benign variant.|||In FPF; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-SMase activation domain (NSD)|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 1A, membrane form|||Tumor necrosis factor-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034543|||http://purl.uniprot.org/annotation/PRO_0000034544|||http://purl.uniprot.org/annotation/VAR_011813|||http://purl.uniprot.org/annotation/VAR_013410|||http://purl.uniprot.org/annotation/VAR_013411|||http://purl.uniprot.org/annotation/VAR_013412|||http://purl.uniprot.org/annotation/VAR_013413|||http://purl.uniprot.org/annotation/VAR_013414|||http://purl.uniprot.org/annotation/VAR_013415|||http://purl.uniprot.org/annotation/VAR_019302|||http://purl.uniprot.org/annotation/VAR_019303|||http://purl.uniprot.org/annotation/VAR_019304|||http://purl.uniprot.org/annotation/VAR_019305|||http://purl.uniprot.org/annotation/VAR_019329|||http://purl.uniprot.org/annotation/VAR_019330|||http://purl.uniprot.org/annotation/VAR_019331|||http://purl.uniprot.org/annotation/VAR_019332|||http://purl.uniprot.org/annotation/VSP_037153|||http://purl.uniprot.org/annotation/VSP_037154|||http://purl.uniprot.org/annotation/VSP_044949|||http://purl.uniprot.org/annotation/VSP_047613|||http://purl.uniprot.org/annotation/VSP_047614
http://togogenome.org/gene/9606:DSC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14574                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cytoplasmic|||Desmocollin-3|||Extracellular|||Helical|||In isoform 3B.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003875|||http://purl.uniprot.org/annotation/PRO_0000003876|||http://purl.uniprot.org/annotation/VAR_048515|||http://purl.uniprot.org/annotation/VAR_048516|||http://purl.uniprot.org/annotation/VAR_048517|||http://purl.uniprot.org/annotation/VAR_048518|||http://purl.uniprot.org/annotation/VAR_048519|||http://purl.uniprot.org/annotation/VAR_048520|||http://purl.uniprot.org/annotation/VSP_000663|||http://purl.uniprot.org/annotation/VSP_000664
http://togogenome.org/gene/9606:CALHM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU99                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Has no effect on glycosylation.|||Helical|||Impaired ion channel activity in response to change in extracellular Ca(2+) concentration.|||Impairs ability to activate the ERK1 and ERK2 cascade.|||N-linked (GlcNAc...) asparagine|||No effect.|||Not glycosylated|||Prevents glycosylation and impairs ability to activate the ERK1 and ERK2 cascade.|||Significant inhibition on the control of cytosolic Ca(2+) levels. Does not affect ion channel activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186723|||http://purl.uniprot.org/annotation/VAR_023095
http://togogenome.org/gene/9606:MANSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8J5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||MANSC|||MANSC domain-containing protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021636|||http://purl.uniprot.org/annotation/VAR_021840|||http://purl.uniprot.org/annotation/VAR_021841|||http://purl.uniprot.org/annotation/VAR_051151|||http://purl.uniprot.org/annotation/VAR_061682|||http://purl.uniprot.org/annotation/VSP_055927
http://togogenome.org/gene/9606:RPL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83731|||http://purl.uniprot.org/uniprot/V9HW01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||Abolished mono-ADP-ribosylation by PARP16, leading to increased protein synthesis.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein eL24|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||TRASH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136867
http://togogenome.org/gene/9606:MSH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCM1|||http://purl.uniprot.org/uniprot/O43196                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA mismatch repair proteins mutS family|||Disordered|||In POF13; decreased function in DNA repair as suggested by the persistence of gamma-H2AX foci following cell treatment with etoposide.|||In POF13; unknown pathological significance.|||In SPGF74; unknown pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||MutS protein homolog 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115202|||http://purl.uniprot.org/annotation/VAR_025082|||http://purl.uniprot.org/annotation/VAR_025083|||http://purl.uniprot.org/annotation/VAR_025084|||http://purl.uniprot.org/annotation/VAR_025085|||http://purl.uniprot.org/annotation/VAR_025086|||http://purl.uniprot.org/annotation/VAR_025087|||http://purl.uniprot.org/annotation/VAR_025088|||http://purl.uniprot.org/annotation/VAR_078116|||http://purl.uniprot.org/annotation/VAR_078117|||http://purl.uniprot.org/annotation/VAR_078118|||http://purl.uniprot.org/annotation/VAR_087415|||http://purl.uniprot.org/annotation/VSP_017113|||http://purl.uniprot.org/annotation/VSP_017114|||http://purl.uniprot.org/annotation/VSP_017115
http://togogenome.org/gene/9606:ATP6V0A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y487                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||V-type proton ATPase 116 kDa subunit a 2|||Vacuolar                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119216|||http://purl.uniprot.org/annotation/VAR_042730|||http://purl.uniprot.org/annotation/VAR_042731
http://togogenome.org/gene/9606:HHEX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03014                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes interaction with EIF4E and inhibitory effect on EIF4E-mediated mRNA nuclear export.|||Basic and acidic residues|||Disordered|||Hematopoietically-expressed homeobox protein HHEX|||Homeobox|||Interaction with SOX13|||Loss of nuclear localization; when associated with A-188.|||Loss of nuclear localization; when associated with A-189.|||Phosphoserine|||Polar residues|||Required for WNT signaling induction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049074
http://togogenome.org/gene/9606:ST6GALNAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ37                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149272
http://togogenome.org/gene/9606:PRMT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60678|||http://purl.uniprot.org/uniprot/Q8WUV3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||Disordered|||In isoform 2.|||Loss of interaction with ALDH1A1.|||Markedly reduced affinity for RPS2.|||Mediates interaction with ALDH1A1|||N-acetylcysteine|||No effect on ALDH1A1 activity regulation.|||No effect on interaction with RPS2.|||Not phosphorylated|||Phosphoserine|||Protein arginine N-methyltransferase 3|||Removed|||SAM-dependent MTase PRMT-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212326|||http://purl.uniprot.org/annotation/VAR_024584|||http://purl.uniprot.org/annotation/VAR_024585|||http://purl.uniprot.org/annotation/VAR_030943|||http://purl.uniprot.org/annotation/VSP_040330
http://togogenome.org/gene/9606:MYH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12883                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In CMD1S.|||In CMD1S; unknown pathological significance.|||In CMH1 and CMD1S.|||In CMH1 and LVNC5.|||In CMH1.|||In CMH1; associated with phenotype variability.|||In CMH1; in cis with M-606 gives a more severe phenotype.|||In CMH1; in cis with V-728 gives a more severe phenotype.|||In CMH1; infrequent.|||In CMH1; malignant phenotype.|||In CMH1; unknown pathological significance.|||In CMYP7A.|||In CMYP7B.|||In LVNC5.|||In LVNC5; unknown pathological significance.|||In MPD1.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-7|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123407|||http://purl.uniprot.org/annotation/VAR_004566|||http://purl.uniprot.org/annotation/VAR_004567|||http://purl.uniprot.org/annotation/VAR_004568|||http://purl.uniprot.org/annotation/VAR_004569|||http://purl.uniprot.org/annotation/VAR_004570|||http://purl.uniprot.org/annotation/VAR_004571|||http://purl.uniprot.org/annotation/VAR_004572|||http://purl.uniprot.org/annotation/VAR_004573|||http://purl.uniprot.org/annotation/VAR_004574|||http://purl.uniprot.org/annotation/VAR_004575|||http://purl.uniprot.org/annotation/VAR_004576|||http://purl.uniprot.org/annotation/VAR_004577|||http://purl.uniprot.org/annotation/VAR_004578|||http://purl.uniprot.org/annotation/VAR_004579|||http://purl.uniprot.org/annotation/VAR_004580|||http://purl.uniprot.org/annotation/VAR_004581|||http://purl.uniprot.org/annotation/VAR_004582|||http://purl.uniprot.org/annotation/VAR_004583|||http://purl.uniprot.org/annotation/VAR_004584|||http://purl.uniprot.org/annotation/VAR_004585|||http://purl.uniprot.org/annotation/VAR_004586|||http://purl.uniprot.org/annotation/VAR_004587|||http://purl.uniprot.org/annotation/VAR_004588|||http://purl.uniprot.org/annotation/VAR_004589|||http://purl.uniprot.org/annotation/VAR_004590|||http://purl.uniprot.org/annotation/VAR_004591|||http://purl.uniprot.org/annotation/VAR_004592|||http://purl.uniprot.org/annotation/VAR_004593|||http://purl.uniprot.org/annotation/VAR_004594|||http://purl.uniprot.org/annotation/VAR_004595|||http://purl.uniprot.org/annotation/VAR_004596|||http://purl.uniprot.org/annotation/VAR_004597|||http://purl.uniprot.org/annotation/VAR_004598|||http://purl.uniprot.org/annotation/VAR_014199|||http://purl.uniprot.org/annotation/VAR_017745|||http://purl.uniprot.org/annotation/VAR_017746|||http://purl.uniprot.org/annotation/VAR_017747|||http://purl.uniprot.org/annotation/VAR_017748|||http://purl.uniprot.org/annotation/VAR_017749|||http://purl.uniprot.org/annotation/VAR_017750|||http://purl.uniprot.org/annotation/VAR_017751|||http://purl.uniprot.org/annotation/VAR_017753|||http://purl.uniprot.org/annotation/VAR_017754|||http://purl.uniprot.org/annotation/VAR_019845|||http://purl.uniprot.org/annotation/VAR_019846|||http://purl.uniprot.org/annotation/VAR_019847|||http://purl.uniprot.org/annotation/VAR_019848|||http://purl.uniprot.org/annotation/VAR_019849|||http://purl.uniprot.org/annotation/VAR_019850|||http://purl.uniprot.org/annotation/VAR_019851|||http://purl.uniprot.org/annotation/VAR_019852|||http://purl.uniprot.org/annotation/VAR_019853|||http://purl.uniprot.org/annotation/VAR_019854|||http://purl.uniprot.org/annotation/VAR_019855|||http://purl.uniprot.org/annotation/VAR_019856|||http://purl.uniprot.org/annotation/VAR_019857|||http://purl.uniprot.org/annotation/VAR_019858|||http://purl.uniprot.org/annotation/VAR_019859|||http://purl.uniprot.org/annotation/VAR_019860|||http://purl.uniprot.org/annotation/VAR_019861|||http://purl.uniprot.org/annotation/VAR_019862|||http://purl.uniprot.org/annotation/VAR_019863|||http://purl.uniprot.org/annotation/VAR_019864|||http://purl.uniprot.org/annotation/VAR_019865|||http://purl.uniprot.org/annotation/VAR_019866|||http://purl.uniprot.org/annotation/VAR_019867|||http://purl.uniprot.org/annotation/VAR_019868|||http://purl.uniprot.org/annotation/VAR_019869|||http://purl.uniprot.org/annotation/VAR_019870|||http://purl.uniprot.org/annotation/VAR_019871|||http://purl.uniprot.org/annotation/VAR_020797|||http://purl.uniprot.org/annotation/VAR_020798|||http://purl.uniprot.org/annotation/VAR_020799|||http://purl.uniprot.org/annotation/VAR_020800|||http://purl.uniprot.org/annotation/VAR_020801|||http://purl.uniprot.org/annotation/VAR_020802|||http://purl.uniprot.org/annotation/VAR_020803|||http://purl.uniprot.org/annotation/VAR_020804|||http://purl.uniprot.org/annotation/VAR_020805|||http://purl.uniprot.org/annotation/VAR_020806|||http://purl.uniprot.org/annotation/VAR_020807|||http://purl.uniprot.org/annotation/VAR_020808|||http://purl.uniprot.org/annotation/VAR_020809|||http://purl.uniprot.org/annotation/VAR_020810|||http://purl.uniprot.org/annotation/VAR_020811|||http://purl.uniprot.org/annotation/VAR_020812|||http://purl.uniprot.org/annotation/VAR_020813|||http://purl.uniprot.org/annotation/VAR_020814|||http://purl.uniprot.org/annotation/VAR_020815|||http://purl.uniprot.org/annotation/VAR_020816|||http://purl.uniprot.org/annotation/VAR_020817|||http://purl.uniprot.org/annotation/VAR_020818|||http://purl.uniprot.org/annotation/VAR_020819|||http://purl.uniprot.org/annotation/VAR_020820|||http://purl.uniprot.org/annotation/VAR_020821|||http://purl.uniprot.org/annotation/VAR_022369|||http://purl.uniprot.org/annotation/VAR_022370|||http://purl.uniprot.org/annotation/VAR_022371|||http://purl.uniprot.org/annotation/VAR_029430|||http://purl.uniprot.org/annotation/VAR_029431|||http://purl.uniprot.org/annotation/VAR_029432|||http://purl.uniprot.org/annotation/VAR_029433|||http://purl.uniprot.org/annotation/VAR_029434|||http://purl.uniprot.org/annotation/VAR_029435|||http://purl.uniprot.org/annotation/VAR_029436|||http://purl.uniprot.org/annotation/VAR_029437|||http://purl.uniprot.org/annotation/VAR_029438|||http://purl.uniprot.org/annotation/VAR_029439|||http://purl.uniprot.org/annotation/VAR_029440|||http://purl.uniprot.org/annotation/VAR_029441|||http://purl.uniprot.org/annotation/VAR_029442|||http://purl.uniprot.org/annotation/VAR_029443|||http://purl.uniprot.org/annotation/VAR_029444|||http://purl.uniprot.org/annotation/VAR_039562|||http://purl.uniprot.org/annotation/VAR_039563|||http://purl.uniprot.org/annotation/VAR_042762|||http://purl.uniprot.org/annotation/VAR_042763|||http://purl.uniprot.org/annotation/VAR_042764|||http://purl.uniprot.org/annotation/VAR_042765|||http://purl.uniprot.org/annotation/VAR_042766|||http://purl.uniprot.org/annotation/VAR_042767|||http://purl.uniprot.org/annotation/VAR_042768|||http://purl.uniprot.org/annotation/VAR_042769|||http://purl.uniprot.org/annotation/VAR_042770|||http://purl.uniprot.org/annotation/VAR_042771|||http://purl.uniprot.org/annotation/VAR_042772|||http://purl.uniprot.org/annotation/VAR_042773|||http://purl.uniprot.org/annotation/VAR_042774|||http://purl.uniprot.org/annotation/VAR_042775|||http://purl.uniprot.org/annotation/VAR_042776|||http://purl.uniprot.org/annotation/VAR_042777|||http://purl.uniprot.org/annotation/VAR_042778|||http://purl.uniprot.org/annotation/VAR_042779|||http://purl.uniprot.org/annotation/VAR_042780|||http://purl.uniprot.org/annotation/VAR_042781|||http://purl.uniprot.org/annotation/VAR_042782|||http://purl.uniprot.org/annotation/VAR_042783|||http://purl.uniprot.org/annotation/VAR_042784|||http://purl.uniprot.org/annotation/VAR_042785|||http://purl.uniprot.org/annotation/VAR_042786|||http://purl.uniprot.org/annotation/VAR_042787|||http://purl.uniprot.org/annotation/VAR_042788|||http://purl.uniprot.org/annotation/VAR_042789|||http://purl.uniprot.org/annotation/VAR_042790|||http://purl.uniprot.org/annotation/VAR_042791|||http://purl.uniprot.org/annotation/VAR_042792|||http://purl.uniprot.org/annotation/VAR_042793|||http://purl.uniprot.org/annotation/VAR_042794|||http://purl.uniprot.org/annotation/VAR_042795|||http://purl.uniprot.org/annotation/VAR_042796|||http://purl.uniprot.org/annotation/VAR_042797|||http://purl.uniprot.org/annotation/VAR_042798|||http://purl.uniprot.org/annotation/VAR_042799|||http://purl.uniprot.org/annotation/VAR_042800|||http://purl.uniprot.org/annotation/VAR_042801|||http://purl.uniprot.org/annotation/VAR_042802|||http://purl.uniprot.org/annotation/VAR_042803|||http://purl.uniprot.org/annotation/VAR_042804|||http://purl.uniprot.org/annotation/VAR_042805|||http://purl.uniprot.org/annotation/VAR_042806|||http://purl.uniprot.org/annotation/VAR_042807|||http://purl.uniprot.org/annotation/VAR_042808|||http://purl.uniprot.org/annotation/VAR_042809|||http://purl.uniprot.org/annotation/VAR_042810|||http://purl.uniprot.org/annotation/VAR_042811|||http://purl.uniprot.org/annotation/VAR_042812|||http://purl.uniprot.org/annotation/VAR_042813|||http://purl.uniprot.org/annotation/VAR_042814|||http://purl.uniprot.org/annotation/VAR_042815|||http://purl.uniprot.org/annotation/VAR_042816|||http://purl.uniprot.org/annotation/VAR_042817|||http://purl.uniprot.org/annotation/VAR_042818|||http://purl.uniprot.org/annotation/VAR_042819|||http://purl.uniprot.org/annotation/VAR_042820|||http://purl.uniprot.org/annotation/VAR_042821|||http://purl.uniprot.org/annotation/VAR_042822|||http://purl.uniprot.org/annotation/VAR_042823|||http://purl.uniprot.org/annotation/VAR_042824|||http://purl.uniprot.org/annotation/VAR_042825|||http://purl.uniprot.org/annotation/VAR_042826|||http://purl.uniprot.org/annotation/VAR_042827|||http://purl.uniprot.org/annotation/VAR_042828|||http://purl.uniprot.org/annotation/VAR_042829|||http://purl.uniprot.org/annotation/VAR_042830|||http://purl.uniprot.org/annotation/VAR_042831|||http://purl.uniprot.org/annotation/VAR_042832|||http://purl.uniprot.org/annotation/VAR_042833|||http://purl.uniprot.org/annotation/VAR_042834|||http://purl.uniprot.org/annotation/VAR_042835|||http://purl.uniprot.org/annotation/VAR_042836|||http://purl.uniprot.org/annotation/VAR_042837|||http://purl.uniprot.org/annotation/VAR_042838|||http://purl.uniprot.org/annotation/VAR_042839|||http://purl.uniprot.org/annotation/VAR_042840|||http://purl.uniprot.org/annotation/VAR_042841|||http://purl.uniprot.org/annotation/VAR_042842|||http://purl.uniprot.org/annotation/VAR_045926|||http://purl.uniprot.org/annotation/VAR_045927|||http://purl.uniprot.org/annotation/VAR_045928|||http://purl.uniprot.org/annotation/VAR_067260|||http://purl.uniprot.org/annotation/VAR_067261|||http://purl.uniprot.org/annotation/VAR_067262|||http://purl.uniprot.org/annotation/VAR_067263|||http://purl.uniprot.org/annotation/VAR_072816|||http://purl.uniprot.org/annotation/VAR_073875|||http://purl.uniprot.org/annotation/VAR_073876|||http://purl.uniprot.org/annotation/VAR_073877|||http://purl.uniprot.org/annotation/VAR_073878|||http://purl.uniprot.org/annotation/VAR_073879|||http://purl.uniprot.org/annotation/VAR_073880|||http://purl.uniprot.org/annotation/VAR_073881|||http://purl.uniprot.org/annotation/VAR_073882|||http://purl.uniprot.org/annotation/VAR_073883|||http://purl.uniprot.org/annotation/VAR_073884|||http://purl.uniprot.org/annotation/VAR_073885|||http://purl.uniprot.org/annotation/VAR_073886|||http://purl.uniprot.org/annotation/VAR_073887|||http://purl.uniprot.org/annotation/VAR_073888|||http://purl.uniprot.org/annotation/VAR_080399
http://togogenome.org/gene/9606:SLIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8V1|||http://purl.uniprot.org/uniprot/O75093                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CTCK|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRCT 3|||LRRCT 4|||LRRNT|||LRRNT 2|||LRRNT 3|||LRRNT 4|||Laminin G|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Slit homolog 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007722|||http://purl.uniprot.org/annotation/PRO_5002698532|||http://purl.uniprot.org/annotation/VAR_049003|||http://purl.uniprot.org/annotation/VSP_009706|||http://purl.uniprot.org/annotation/VSP_009707|||http://purl.uniprot.org/annotation/VSP_009708
http://togogenome.org/gene/9606:CDS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92903                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||Omega-N-methylarginine|||Phosphatidate cytidylyltransferase 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090713|||http://purl.uniprot.org/annotation/VAR_036129|||http://purl.uniprot.org/annotation/VAR_048736
http://togogenome.org/gene/9606:TMBIM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55061                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||INTRAMEM|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes calcium flux properties.|||Bax inhibitor 1|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179078|||http://purl.uniprot.org/annotation/VSP_055119
http://togogenome.org/gene/9606:AKAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MQY7|||http://purl.uniprot.org/uniprot/Q5JQC9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor 110kDa C-terminal|||A-kinase anchor protein 4|||Disordered|||In isoform 2.|||PKA-RI and PKA-RII subunit binding domain|||PKA-RI-alpha subunit binding domain|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RII binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248230|||http://purl.uniprot.org/annotation/PRO_0000248231|||http://purl.uniprot.org/annotation/VAR_027266|||http://purl.uniprot.org/annotation/VAR_048206|||http://purl.uniprot.org/annotation/VSP_052142
http://togogenome.org/gene/9606:FHL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14192|||http://purl.uniprot.org/uniprot/Q2XQU9|||http://purl.uniprot.org/uniprot/Q6I9R8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Disordered|||Four and a half LIM domains protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075737|||http://purl.uniprot.org/annotation/VAR_067455|||http://purl.uniprot.org/annotation/VSP_056999|||http://purl.uniprot.org/annotation/VSP_057000
http://togogenome.org/gene/9606:KCNH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 3|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054005
http://togogenome.org/gene/9606:EVI5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR55|||http://purl.uniprot.org/uniprot/Q96CN4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Disordered|||EVI5-like protein|||Glutamine finger|||In isoform 2.|||Phosphoserine|||Polar residues|||Rab-GAP TBC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263097|||http://purl.uniprot.org/annotation/VSP_043456
http://togogenome.org/gene/9606:SYNJ2BP-COX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYV9                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||PDZ                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RPS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62841                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Removed|||Small ribosomal subunit protein uS19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130027
http://togogenome.org/gene/9606:OR52H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWQ6|||http://purl.uniprot.org/uniprot/Q8NGJ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150777|||http://purl.uniprot.org/annotation/VAR_054361|||http://purl.uniprot.org/annotation/VAR_054362|||http://purl.uniprot.org/annotation/VAR_054363|||http://purl.uniprot.org/annotation/VAR_054364|||http://purl.uniprot.org/annotation/VAR_054365|||http://purl.uniprot.org/annotation/VAR_054366|||http://purl.uniprot.org/annotation/VAR_062083
http://togogenome.org/gene/9606:CHCT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||CHD1 helical C-terminal domain (CHCT)|||CHD1 helical C-terminal domain containing protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287174
http://togogenome.org/gene/9606:MYH7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2Y1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In isoform 2.|||In isoform 3.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349312|||http://purl.uniprot.org/annotation/VAR_046359|||http://purl.uniprot.org/annotation/VAR_046360|||http://purl.uniprot.org/annotation/VAR_046361|||http://purl.uniprot.org/annotation/VAR_046362|||http://purl.uniprot.org/annotation/VAR_046363|||http://purl.uniprot.org/annotation/VAR_046364|||http://purl.uniprot.org/annotation/VAR_046365|||http://purl.uniprot.org/annotation/VAR_054814|||http://purl.uniprot.org/annotation/VSP_035359|||http://purl.uniprot.org/annotation/VSP_035361|||http://purl.uniprot.org/annotation/VSP_059497|||http://purl.uniprot.org/annotation/VSP_059498
http://togogenome.org/gene/9606:MPZL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5D4|||http://purl.uniprot.org/uniprot/O95297                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Myelin protein zero-like protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-241.|||Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-263.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240335|||http://purl.uniprot.org/annotation/PRO_5014297540|||http://purl.uniprot.org/annotation/VSP_019342|||http://purl.uniprot.org/annotation/VSP_019343|||http://purl.uniprot.org/annotation/VSP_019344|||http://purl.uniprot.org/annotation/VSP_043341
http://togogenome.org/gene/9606:PTPN20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4JDK3|||http://purl.uniprot.org/uniprot/Q4JDL3|||http://purl.uniprot.org/uniprot/Q5H9Q9|||http://purl.uniprot.org/uniprot/Q9Y406                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 13 and isoform 15.|||In isoform 2, isoform 8, isoform 11 and isoform 15.|||In isoform 3 and isoform 12.|||In isoform 4, isoform 5, isoform 9 and isoform 14.|||In isoform 5 and isoform 11.|||In isoform 6.|||In isoform 7, isoform 8, isoform 12 and isoform 14.|||In isoform 9.|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295755|||http://purl.uniprot.org/annotation/VSP_027063|||http://purl.uniprot.org/annotation/VSP_027064|||http://purl.uniprot.org/annotation/VSP_027065|||http://purl.uniprot.org/annotation/VSP_027066|||http://purl.uniprot.org/annotation/VSP_027067|||http://purl.uniprot.org/annotation/VSP_027068|||http://purl.uniprot.org/annotation/VSP_027069|||http://purl.uniprot.org/annotation/VSP_027070|||http://purl.uniprot.org/annotation/VSP_027071|||http://purl.uniprot.org/annotation/VSP_027072|||http://purl.uniprot.org/annotation/VSP_027073|||http://purl.uniprot.org/annotation/VSP_038003|||http://purl.uniprot.org/annotation/VSP_038004
http://togogenome.org/gene/9606:DAGLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCG7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Diacylglycerol lipase-beta|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248350|||http://purl.uniprot.org/annotation/VAR_027275|||http://purl.uniprot.org/annotation/VSP_020245|||http://purl.uniprot.org/annotation/VSP_020246|||http://purl.uniprot.org/annotation/VSP_020247|||http://purl.uniprot.org/annotation/VSP_043309
http://togogenome.org/gene/9606:AREL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T811|||http://purl.uniprot.org/uniprot/O15033                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Apoptosis-resistant E3 ubiquitin protein ligase 1|||Disordered|||Failure to form ubiquitin thioester complex.|||Filamin|||Glycyl thioester intermediate|||HECT|||In isoform 2.|||Interaction with SOCS2|||Loss of interaction with SOCS2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120349|||http://purl.uniprot.org/annotation/VAR_083342|||http://purl.uniprot.org/annotation/VSP_013259
http://togogenome.org/gene/9606:PIWIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8J9G8U8|||http://purl.uniprot.org/uniprot/B4DYF7|||http://purl.uniprot.org/uniprot/Q7Z3Z3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||PAZ|||Piwi|||Piwi-like protein 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234571|||http://purl.uniprot.org/annotation/VAR_034383|||http://purl.uniprot.org/annotation/VAR_034384|||http://purl.uniprot.org/annotation/VAR_034385|||http://purl.uniprot.org/annotation/VAR_054774|||http://purl.uniprot.org/annotation/VAR_059130|||http://purl.uniprot.org/annotation/VAR_061024
http://togogenome.org/gene/9606:ZNF84                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51523                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Zinc finger protein 84                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047397
http://togogenome.org/gene/9606:COG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 8|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213521|||http://purl.uniprot.org/annotation/VAR_047655
http://togogenome.org/gene/9606:ARHGAP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LW3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with PTPN13/PTPL1|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 29|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317582|||http://purl.uniprot.org/annotation/VAR_038552|||http://purl.uniprot.org/annotation/VAR_038553|||http://purl.uniprot.org/annotation/VAR_049145|||http://purl.uniprot.org/annotation/VSP_031058|||http://purl.uniprot.org/annotation/VSP_031059
http://togogenome.org/gene/9606:EIF4ENIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished interaction with EIF4E2.|||Abolished interaction with LSM14A.|||Abolishes interaction with EIF4E and EIF4E2. Impaired ability to repress mRNA translation.|||Abolishes the nuclear localization.|||Basic and acidic residues|||Disordered|||Does not affect interaction with LSM14A.|||Eukaryotic translation initiation factor 4E transporter|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-693.|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-587 and A-752.|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-513, A-693 and A-752.|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-374, A-587, A-693 and A-752.|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-301, A-513, A-587, A-693 and A-752.|||In S6A mutant; abolished phosphorylation by MAPK8/JNK1; impaired P-body assembly in response to oxidative stress when associated with A-374, A-513, A-587, A-693 and A-752.|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with CSDE1|||Interaction with DDX6|||Interaction with LSM14A|||Interaction with PATL1|||N6-acetyllysine|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Strongly reduced interaction with EIF4E and EIF4E2.|||YXXXXLphi motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064381|||http://purl.uniprot.org/annotation/VSP_003783|||http://purl.uniprot.org/annotation/VSP_003784|||http://purl.uniprot.org/annotation/VSP_047042
http://togogenome.org/gene/9606:PLAAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY88|||http://purl.uniprot.org/uniprot/Q8NE88|||http://purl.uniprot.org/uniprot/Q96KN8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Disordered|||In isoform 2.|||In isoform 3.|||LRAT|||Phospholipase A and acyltransferase 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152488|||http://purl.uniprot.org/annotation/VAR_024486|||http://purl.uniprot.org/annotation/VAR_049477|||http://purl.uniprot.org/annotation/VAR_049478|||http://purl.uniprot.org/annotation/VAR_049479|||http://purl.uniprot.org/annotation/VSP_045825|||http://purl.uniprot.org/annotation/VSP_045826
http://togogenome.org/gene/9606:MESP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VG99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||13 X 2 AA tandem repeats of G-Q|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||In a patient with spondylocostal dysostosis; inactive.|||Mesoderm posterior protein 2|||Polar residues|||Pro residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296301|||http://purl.uniprot.org/annotation/VAR_046779|||http://purl.uniprot.org/annotation/VAR_046780|||http://purl.uniprot.org/annotation/VAR_046781|||http://purl.uniprot.org/annotation/VAR_061257
http://togogenome.org/gene/9606:ND6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03923|||http://purl.uniprot.org/uniprot/U5Z977                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In LDYT; decrease in enzyme activity.|||In LDYT; most severe mutation with no vision recovery.|||In LHON.|||In LHON; low severity; up to 50% of vision recovery; results in decreased complex I activity.|||In LS; decrease in enzyme activity and impaired assembly of complex I.|||In MELAS.|||NADH-ubiquinone oxidoreductase chain 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118291|||http://purl.uniprot.org/annotation/PRO_5015101637|||http://purl.uniprot.org/annotation/VAR_004763|||http://purl.uniprot.org/annotation/VAR_004764|||http://purl.uniprot.org/annotation/VAR_008394|||http://purl.uniprot.org/annotation/VAR_008395|||http://purl.uniprot.org/annotation/VAR_008396|||http://purl.uniprot.org/annotation/VAR_008512|||http://purl.uniprot.org/annotation/VAR_008604|||http://purl.uniprot.org/annotation/VAR_014393|||http://purl.uniprot.org/annotation/VAR_014394|||http://purl.uniprot.org/annotation/VAR_014395|||http://purl.uniprot.org/annotation/VAR_014396|||http://purl.uniprot.org/annotation/VAR_014397|||http://purl.uniprot.org/annotation/VAR_064568
http://togogenome.org/gene/9606:SPPL2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUH8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Loss of aspartyl protease activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||PA|||PAL|||Signal peptide peptidase-like 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314797|||http://purl.uniprot.org/annotation/VAR_038048|||http://purl.uniprot.org/annotation/VAR_038049|||http://purl.uniprot.org/annotation/VAR_038050|||http://purl.uniprot.org/annotation/VAR_038051|||http://purl.uniprot.org/annotation/VAR_038052|||http://purl.uniprot.org/annotation/VAR_038053|||http://purl.uniprot.org/annotation/VAR_038054|||http://purl.uniprot.org/annotation/VAR_057147|||http://purl.uniprot.org/annotation/VAR_060590
http://togogenome.org/gene/9606:STAMBPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FJ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10-fold decrease in activity, no change in substrate affinity.|||12-fold decrease in substrate affinity, little effect on catalytic activity.|||161-fold decrease in activity, no change in substrate affinity.|||18-fold decrease in substrate affinity, little effect on catalytic activity.|||19-fold decrease in activity, no change in substrate affinity.|||3-fold decrease in substrate affinity.|||34-fold decrease in activity.|||35-fold decrease in activity, slight increase in substrate affinity.|||402-fold decrease in activity, slight increase in substrate affinity.|||AMSH-like protease|||Complete loss of catalytic activity.|||In isoform 2.|||Indirect zinc-binding|||JAMM motif|||MPN|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194874|||http://purl.uniprot.org/annotation/VAR_051817|||http://purl.uniprot.org/annotation/VAR_051818|||http://purl.uniprot.org/annotation/VAR_051819|||http://purl.uniprot.org/annotation/VSP_014648
http://togogenome.org/gene/9606:CHP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43745                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcineurin B homologous protein 2|||Does not reduce calcium-binding.|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Localizes in the nucleus and increases cell proliferation.|||N-myristoyl glycine|||Nuclear export signal|||Phosphoserine|||Reduces calcium-binding. Inhibits calcium-binding and cell membrane localization; when associated with A-135.|||Reduces calcium-binding. Inhibits calcium-binding and cell membrane localization; when associated with A-176.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073848|||http://purl.uniprot.org/annotation/VAR_048664
http://togogenome.org/gene/9606:TNRC6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCJ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes association with CCR4-NOT complex.|||Abolishes interaction with PABPC1, impairs interaction with PAN2, no effect on interaction with CCR4-NOT complex, reduces RNA deadenylation rate; when associated with 1388-A-A-1389.|||Abolishes interaction with PABPC1, impairs interaction with PAN2, no effect on interaction with CCR4-NOT complex, reduces RNA deadenylation rate; when associated with 1395-A-A-1396.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1487, A-1494, A-1504, A-1515 and A-1605.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1487, A-1494, A-1504, A-1515 and A-1648.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1487, A-1494, A-1504, A-1605 and A-1648.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1487, A-1494, A-1515, A-1605 and A-1648.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1487, A-1504, A-1515, A-1605 and A-1648.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1445, A-1494, A-1504, A-1515, A-1605 and A-1648.|||Abolishes translational repression when tethered to a target mRNA, abolishes association with the CCR4-NOT complex; when associated with A-1487, A-1494, A-1504, A-1515, A-1605 and A-1648.|||Basic and acidic residues|||Disordered|||Impairs interaction with the CCR4-NOT complex, no effect on interaction with PABPC1; when associated with 1647-A-A-1649.|||Impairs interaction with the CCR4-NOT complex, no effect on interaction with PABPC1; when associated with 1658-A-A-1660.|||In isoform 2.|||Interaction with the CCR4-NOT complex|||Omega-N-methylarginine|||PABPC1-interacting motif-2 (PAM2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||Required for interaction with PABPC1|||Silencing domain; interaction with CNOT1 and PAN3|||Strongly reduced ability to repress translation of target mRNAs.|||Sufficient for interaction with argonaute family proteins|||Sufficient for translational repression when tethered to a target mRNA|||Trinucleotide repeat-containing gene 6C protein|||UBA|||Weakly reduced ability to repress translation of target mRNAs.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278526|||http://purl.uniprot.org/annotation/VAR_052237|||http://purl.uniprot.org/annotation/VSP_023322|||http://purl.uniprot.org/annotation/VSP_054230
http://togogenome.org/gene/9606:NAGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17050                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminidase|||In KANZD.|||In KANZD; loss of activity.|||In SCHIND; type I and type III.|||In SCHIND; type III.|||Loss of glycosylation site; no effect on enzyme activity and stability.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001018|||http://purl.uniprot.org/annotation/VAR_000496|||http://purl.uniprot.org/annotation/VAR_000497|||http://purl.uniprot.org/annotation/VAR_000498|||http://purl.uniprot.org/annotation/VAR_022525
http://togogenome.org/gene/9606:SNORC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6M4NK13|||http://purl.uniprot.org/uniprot/Q6UX34                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Protein SNORC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317641|||http://purl.uniprot.org/annotation/PRO_5026745110
http://togogenome.org/gene/9606:DGCR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYQ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DRBM 1|||DRBM 2|||Disordered|||Does not inhibit heme-binding and dimerization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Inhibits heme-binding and dimerization.|||Interaction with DROSHA|||Microprocessor complex subunit DGCR8|||Necessary for heme-binding and pri-miRNA processing|||Necessary for interaction with NCL|||Necessary for nuclear localization and retention|||Phosphoserine|||Phosphothreonine|||Reduces pri-miRNA binding affinity and pri-miRNA processing activity. Does not inhibit interaction with DROSHA. When associated with A-676 and S-677, strongly reduces binding affinity and pri-miRNA processing activity.|||Reduces pri-miRNA binding affinity and pri-miRNA processing activity. Slightly inhibits interaction with DROSHA. When associated with A-568 and A-568, strongly reduces binding affinity and pri-miRNA processing activity.|||Strongly reduces pri-miRNA binding affinity.|||WW|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079878|||http://purl.uniprot.org/annotation/VAR_050952|||http://purl.uniprot.org/annotation/VAR_050953|||http://purl.uniprot.org/annotation/VSP_003847|||http://purl.uniprot.org/annotation/VSP_003848|||http://purl.uniprot.org/annotation/VSP_012707
http://togogenome.org/gene/9606:OR52N2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGI0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150787|||http://purl.uniprot.org/annotation/VAR_024150|||http://purl.uniprot.org/annotation/VAR_024151
http://togogenome.org/gene/9606:CAPN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-11|||Disordered|||Domain III|||Domain IV|||EF-hand 1|||EF-hand 2|||Linker                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207729|||http://purl.uniprot.org/annotation/VAR_024587|||http://purl.uniprot.org/annotation/VAR_033713|||http://purl.uniprot.org/annotation/VAR_033714|||http://purl.uniprot.org/annotation/VAR_033715|||http://purl.uniprot.org/annotation/VAR_033716
http://togogenome.org/gene/9606:PTP4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75365                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  95% loss of enzymatic activity.|||Abolishes enzymatic activity.|||Cysteine methyl ester|||Enhances catalytic activity.|||In isoform 2.|||In isoform 3.|||No effect on enzymatic activity.|||Phosphocysteine intermediate|||Protein tyrosine phosphatase type IVA 3|||Proton donor|||Reduces migration-promoting activity.|||Removed in mature form|||S-farnesyl cysteine|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094788|||http://purl.uniprot.org/annotation/PRO_0000396735|||http://purl.uniprot.org/annotation/VSP_014406|||http://purl.uniprot.org/annotation/VSP_014407
http://togogenome.org/gene/9606:NEDD4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2P9|||http://purl.uniprot.org/uniprot/B7Z6K0|||http://purl.uniprot.org/uniprot/Q96PU5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity. No effect on USP36 protein levels.|||Abolishes interaction with 1433F.|||Basic and acidic residues|||C2|||Disordered|||E3 ubiquitin-protein ligase NEDD4-like|||Glycyl thioester intermediate|||HECT|||Impaired ability to inhibit SCNN.|||In PVNH7.|||In PVNH7; increased degradation; changed function in regulation of TOR signaling.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 8.|||In isoform 5, isoform 6 and isoform 8.|||In isoform 6 and isoform 7.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by PKA and SGK1|||Phosphoserine; by WNK1 and WNK4|||Phosphothreonine|||Phosphothreonine; by SGK1|||Polar residues|||Removed|||WW|||WW 1|||WW 2|||WW 3|||WW 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120323|||http://purl.uniprot.org/annotation/VAR_023415|||http://purl.uniprot.org/annotation/VAR_023416|||http://purl.uniprot.org/annotation/VAR_077880|||http://purl.uniprot.org/annotation/VAR_077881|||http://purl.uniprot.org/annotation/VAR_077882|||http://purl.uniprot.org/annotation/VAR_077883|||http://purl.uniprot.org/annotation/VSP_015444|||http://purl.uniprot.org/annotation/VSP_015446|||http://purl.uniprot.org/annotation/VSP_015447|||http://purl.uniprot.org/annotation/VSP_015448|||http://purl.uniprot.org/annotation/VSP_043848
http://togogenome.org/gene/9606:TRIM26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCP3|||http://purl.uniprot.org/uniprot/Q12899                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||B box-type|||B30.2/SPRY|||Disordered|||RING-type|||Strong loss of ubiquitination activity.|||Tripartite motif-containing protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056235|||http://purl.uniprot.org/annotation/VAR_052138
http://togogenome.org/gene/9606:CT47B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C2W7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen family 47 member B1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286433|||http://purl.uniprot.org/annotation/VAR_076267
http://togogenome.org/gene/9606:IFITM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01628                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Accumulates at the plasma membrane. Loss of anti-SARS-CoV-2 activity by enhancing Spike-mediated cell-to-cell fusion.|||Cytoplasmic|||Decreases anti-SARS-CoV-2 activity.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with SPP1|||Interaction with VAPA|||Interferon-induced transmembrane protein 3|||Loss of anti-HCV activity. Only localizes at the lysosome. No effect on SARS-CoV-2 infection; when associated with 71-A-A-72. Loss of anti-influenza A virus activity; when associated with 71-A-A-72.|||Loss of anti-HCV activity. Only localizes at the lysosome. No effect on SARS-CoV-2 infection; when associated with A-105. Loss of anti-influenza A virus activity; when associated with A-105.|||Loss of phosphorylation. Accumulates at the plasma membrane. Increases anti-HCV properties. Loss of anti-SARS-CoV-2 activity by enhancing Spike-mediated cell-to-cell fusion.|||Phosphotyrosine|||S-palmitoyl cysteine|||Slightly enhances infection by SARS-CoV-2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153729|||http://purl.uniprot.org/annotation/VAR_053810
http://togogenome.org/gene/9606:VARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X9B3|||http://purl.uniprot.org/uniprot/B4DG77|||http://purl.uniprot.org/uniprot/B4E0K6|||http://purl.uniprot.org/uniprot/Q5ST30                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Aminoacyl-tRNA synthetase class Ia|||Basic and acidic residues|||Disordered|||In COXPD20.|||In COXPD20; decreased levels of the protein.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding|||Mitochondrion|||Valine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338000|||http://purl.uniprot.org/annotation/VAR_043730|||http://purl.uniprot.org/annotation/VAR_043731|||http://purl.uniprot.org/annotation/VAR_043732|||http://purl.uniprot.org/annotation/VAR_043733|||http://purl.uniprot.org/annotation/VAR_043734|||http://purl.uniprot.org/annotation/VAR_043735|||http://purl.uniprot.org/annotation/VAR_052651|||http://purl.uniprot.org/annotation/VAR_061910|||http://purl.uniprot.org/annotation/VAR_071850|||http://purl.uniprot.org/annotation/VAR_071851|||http://purl.uniprot.org/annotation/VAR_071852|||http://purl.uniprot.org/annotation/VSP_034032|||http://purl.uniprot.org/annotation/VSP_045483|||http://purl.uniprot.org/annotation/VSP_046102
http://togogenome.org/gene/9606:ATOSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32MH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Atos homolog protein A|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Required for macropage invasion|||Transactivation domain 1 (TAD1)|||Transactivation domain 2 (TAD2)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315613|||http://purl.uniprot.org/annotation/VAR_038258|||http://purl.uniprot.org/annotation/VAR_038259|||http://purl.uniprot.org/annotation/VSP_030580|||http://purl.uniprot.org/annotation/VSP_030581|||http://purl.uniprot.org/annotation/VSP_042435
http://togogenome.org/gene/9606:OR6K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV58|||http://purl.uniprot.org/uniprot/Q8NGY2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150629|||http://purl.uniprot.org/annotation/VAR_034248|||http://purl.uniprot.org/annotation/VAR_034249|||http://purl.uniprot.org/annotation/VAR_034250
http://togogenome.org/gene/9606:CHRNE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04844                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetylcholine receptor subunit epsilon|||Cytoplasmic|||Extracellular|||Helical|||In CMS4A; markedly prolonged channel openings in presence of agonist; as well as opening in the absence of agonist.|||In CMS4A; mild form with variable penetrance.|||In CMS4A; rare example of recessive inheritance.|||In CMS4A; slow-channel mutation; increases gating equilibrium constant by 25-fold, owing to increased opening rate and decreased closing rate; no effect on the choline dissociation rate constant.|||In CMS4A; slows rate of AChR channel closure and increases apparent affinity for ACh; causes pathologic channel openings even in the absence of ACh resulting in a leaky channel.|||In CMS4B; causes an increase in distributions of rates for channel opening and closing increasing the range of activation kinetics.|||In CMS4B; fails to assemble with alpha CHRNA1 subunit of AChR.|||In CMS4B; impaired association with alpha CHRNA1 subunit of AChR.|||In CMS4B; marked decrease in rate of AChR channel opening; reduction in frequency of open channel state and resistance to desensitization by ACh.|||In CMS4B; strongly reduces agonist affinity and gating efficiency.|||In CMS4C; prolongs burst open duration 2-fold by slowing the rate of channel closing.|||In CMS4C; shortens burst duration 2-fold by slowing the rate of channel opening and speeding the rate of ACh dissociation; has a mild fast-channel kinetic effect on the AChR by shortening the long burst and increasing the decay of the endplate current.|||In CMS4C; significantly reduced AChR expression.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000329|||http://purl.uniprot.org/annotation/VAR_000289|||http://purl.uniprot.org/annotation/VAR_000290|||http://purl.uniprot.org/annotation/VAR_000291|||http://purl.uniprot.org/annotation/VAR_000292|||http://purl.uniprot.org/annotation/VAR_000293|||http://purl.uniprot.org/annotation/VAR_000294|||http://purl.uniprot.org/annotation/VAR_019567|||http://purl.uniprot.org/annotation/VAR_019568|||http://purl.uniprot.org/annotation/VAR_021213|||http://purl.uniprot.org/annotation/VAR_021214|||http://purl.uniprot.org/annotation/VAR_021215|||http://purl.uniprot.org/annotation/VAR_048170|||http://purl.uniprot.org/annotation/VAR_071629|||http://purl.uniprot.org/annotation/VAR_077364
http://togogenome.org/gene/9606:ADAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2V6Q1|||http://purl.uniprot.org/uniprot/Q9NPF8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Arf-GAP with dual PH domain-containing protein 2|||C4-type|||In isoform 2.|||PH|||PH 1|||PH 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074206|||http://purl.uniprot.org/annotation/VSP_011180
http://togogenome.org/gene/9606:HSD17B13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5P4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase 13|||Decreased retinol/retinal dehydrogenase activity.|||Decreased retinol/retinal dehydrogenase activity; when associated with A-101.|||Decreased retinol/retinal dehydrogenase activity; when associated with A-97.|||Does not localize to lipid droplets.|||In isoform 1.|||Loss of retinol/retinal dehydrogenase activity.|||Loss of retinol/retinal dehydrogenase activity; does not affect localization to lipid droplets.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-153.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-156.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-185.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-189.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-199.|||Loss of retinol/retinal dehydrogenase activity; when associated with A-202.|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042583|||http://purl.uniprot.org/annotation/VAR_087865|||http://purl.uniprot.org/annotation/VSP_015860
http://togogenome.org/gene/9606:MAGEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60732                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MAGE|||Melanoma-associated antigen C1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156720|||http://purl.uniprot.org/annotation/VAR_053501|||http://purl.uniprot.org/annotation/VAR_053502|||http://purl.uniprot.org/annotation/VAR_053503|||http://purl.uniprot.org/annotation/VAR_053504|||http://purl.uniprot.org/annotation/VAR_060068|||http://purl.uniprot.org/annotation/VAR_062121|||http://purl.uniprot.org/annotation/VSP_056382
http://togogenome.org/gene/9606:IMPG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0J3|||http://purl.uniprot.org/uniprot/Q9BZV3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Extracellular|||Found in a patient with VMD5; unknown pathological significance.|||Found in a patient with retinitis pigmentosa; unknown pathological significance.|||Found in a patient with vitelliform macular dystophy; unknown pathological significance.|||Found in a patient with vitelliform macular dystrophy; unknown pathological significance.|||Helical|||Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding|||Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motif|||Hyaluronan-binding motif involved in chondroitin sulfate A-binding|||Hyaluronan-binding motif involved in chondroitin sulfate C-binding|||In RP56.|||In VMD5.|||Interphotoreceptor matrix proteoglycan 2|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Polar residues|||SEA|||SEA 1|||SEA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320149|||http://purl.uniprot.org/annotation/PRO_5003275715|||http://purl.uniprot.org/annotation/VAR_039144|||http://purl.uniprot.org/annotation/VAR_039145|||http://purl.uniprot.org/annotation/VAR_039146|||http://purl.uniprot.org/annotation/VAR_064336|||http://purl.uniprot.org/annotation/VAR_072671|||http://purl.uniprot.org/annotation/VAR_082176|||http://purl.uniprot.org/annotation/VAR_082177|||http://purl.uniprot.org/annotation/VAR_082178|||http://purl.uniprot.org/annotation/VAR_082179|||http://purl.uniprot.org/annotation/VAR_082180|||http://purl.uniprot.org/annotation/VAR_082181|||http://purl.uniprot.org/annotation/VAR_082182|||http://purl.uniprot.org/annotation/VAR_082183|||http://purl.uniprot.org/annotation/VAR_082184|||http://purl.uniprot.org/annotation/VAR_082185|||http://purl.uniprot.org/annotation/VAR_082186|||http://purl.uniprot.org/annotation/VAR_082187|||http://purl.uniprot.org/annotation/VAR_082188|||http://purl.uniprot.org/annotation/VAR_082189|||http://purl.uniprot.org/annotation/VAR_082190|||http://purl.uniprot.org/annotation/VAR_082191
http://togogenome.org/gene/9606:XIRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4UGR9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 4, isoform 6 and isoform 8.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Xin 1|||Xin 10|||Xin 11|||Xin 12|||Xin 13|||Xin 14|||Xin 15|||Xin 16|||Xin 17|||Xin 18|||Xin 19|||Xin 2|||Xin 20|||Xin 21|||Xin 22|||Xin 23|||Xin 24|||Xin 25|||Xin 26|||Xin 27|||Xin 28|||Xin 3|||Xin 4|||Xin 5|||Xin 6|||Xin 7|||Xin 8|||Xin 9|||Xin actin-binding repeat-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316987|||http://purl.uniprot.org/annotation/VAR_038449|||http://purl.uniprot.org/annotation/VAR_038450|||http://purl.uniprot.org/annotation/VAR_038451|||http://purl.uniprot.org/annotation/VAR_038452|||http://purl.uniprot.org/annotation/VAR_038453|||http://purl.uniprot.org/annotation/VAR_038454|||http://purl.uniprot.org/annotation/VAR_038455|||http://purl.uniprot.org/annotation/VAR_038456|||http://purl.uniprot.org/annotation/VAR_038457|||http://purl.uniprot.org/annotation/VAR_038458|||http://purl.uniprot.org/annotation/VAR_038459|||http://purl.uniprot.org/annotation/VAR_038460|||http://purl.uniprot.org/annotation/VAR_038461|||http://purl.uniprot.org/annotation/VAR_038462|||http://purl.uniprot.org/annotation/VAR_038463|||http://purl.uniprot.org/annotation/VAR_076434|||http://purl.uniprot.org/annotation/VAR_082888|||http://purl.uniprot.org/annotation/VAR_082889|||http://purl.uniprot.org/annotation/VAR_082890|||http://purl.uniprot.org/annotation/VSP_030846|||http://purl.uniprot.org/annotation/VSP_030847|||http://purl.uniprot.org/annotation/VSP_030848|||http://purl.uniprot.org/annotation/VSP_035717|||http://purl.uniprot.org/annotation/VSP_035718|||http://purl.uniprot.org/annotation/VSP_035719|||http://purl.uniprot.org/annotation/VSP_035720
http://togogenome.org/gene/9606:HNRNPCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXH8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Heterogeneous nuclear ribonucleoprotein C-like 2|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000430276
http://togogenome.org/gene/9606:SMARCAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4L7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CUE 1|||CUE 2|||DEGD box|||DEGH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||No effect on subcellular localization and on histone deacetylation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074356|||http://purl.uniprot.org/annotation/VAR_028037|||http://purl.uniprot.org/annotation/VAR_028038|||http://purl.uniprot.org/annotation/VAR_028039|||http://purl.uniprot.org/annotation/VAR_028040|||http://purl.uniprot.org/annotation/VAR_028041|||http://purl.uniprot.org/annotation/VAR_028042|||http://purl.uniprot.org/annotation/VAR_028043|||http://purl.uniprot.org/annotation/VAR_028044|||http://purl.uniprot.org/annotation/VSP_007104|||http://purl.uniprot.org/annotation/VSP_043110
http://togogenome.org/gene/9606:KPNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z752|||http://purl.uniprot.org/uniprot/Q14974                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Essential for high affinity interaction with RPL23A|||HEAT|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||IAB-binding|||Importin N-terminal|||Importin subunit beta-1|||In isoform 2.|||Largely reduced binding to FxFG repeats and reduced nuclear import.|||Loss of binding to FxFG repeats and reduced nuclear import.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Ran-GTP binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120745|||http://purl.uniprot.org/annotation/VSP_054612
http://togogenome.org/gene/9606:POTEM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI47                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||Putative POTE ankyrin domain family member M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332150
http://togogenome.org/gene/9606:SNX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP69|||http://purl.uniprot.org/uniprot/E9PNL2|||http://purl.uniprot.org/uniprot/Q9UNH6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BAR|||Disordered|||In isoform 2.|||In isoform 3.|||PX|||Sorting nexin-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213848|||http://purl.uniprot.org/annotation/VAR_057331|||http://purl.uniprot.org/annotation/VAR_057332|||http://purl.uniprot.org/annotation/VSP_006191|||http://purl.uniprot.org/annotation/VSP_039044
http://togogenome.org/gene/9606:CIAO2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D0                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine                                                                                  ^@                                                                                  Cytosolic iron-sulfur assembly component 2B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212691
http://togogenome.org/gene/9606:SNX33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV41                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  BAR|||Disordered|||PX|||Phosphoserine|||Polar residues|||SH3|||Sorting nexin-33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311948
http://togogenome.org/gene/9606:EZH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSY9|||http://purl.uniprot.org/uniprot/Q92800                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CXC|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase EZH1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of methyltransferase activity.|||Nuclear localization signal|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213990|||http://purl.uniprot.org/annotation/VSP_036384|||http://purl.uniprot.org/annotation/VSP_036385|||http://purl.uniprot.org/annotation/VSP_036386|||http://purl.uniprot.org/annotation/VSP_036387
http://togogenome.org/gene/9606:PAGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||PAXIP1-associated glutamate-rich protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sufficient for interaction with ESR1|||Sufficient for interaction with NCOA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248334
http://togogenome.org/gene/9606:TACC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6A5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Disrupts localization to mitotic spindle and impairs recruitment of clathrin to mitotic spindle.|||Impairs localization to mitotic spindle.|||N-acetylserine|||Necessary but not sufficient for spindle localization|||Phosphoserine|||Phosphoserine; by AURKA|||Polar residues|||Removed|||Transforming acidic coiled-coil-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179990|||http://purl.uniprot.org/annotation/VAR_053714|||http://purl.uniprot.org/annotation/VAR_053715|||http://purl.uniprot.org/annotation/VAR_053716|||http://purl.uniprot.org/annotation/VAR_053717
http://togogenome.org/gene/9606:RARA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K840|||http://purl.uniprot.org/uniprot/A8MUP8|||http://purl.uniprot.org/uniprot/F1D8N9|||http://purl.uniprot.org/uniprot/P10276|||http://purl.uniprot.org/uniprot/Q6I9R7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||Abolishes PKB/AKT1-mediated phosphorylation. Repressed transactivation.|||Abolishes interaction with ASXL1 and NCOA1.|||Abrogates interaction with NCOR1 or NCOR2. Increased affinity for NCOR1 and NCOR2 in the presence of BMS493. Increased transcriptional activity in the presence of agonist and decreased activity in the presence of neutral antagonist.|||Abrogates sumoylation in the presence or absence of ATRA and primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-166; R-171 and R-399.|||Breakpoint for translocation to form PLZF-RAR-alpha, RAR-alpha1-PLZF and PML-RAR-alpha oncogenes|||Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-166 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-399.|||Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-171 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-171 and R-399.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Hinge|||Impairs interaction with ASXL1 and NCOA1; when associated with Q-412.|||Impairs interaction with ASXL1 and NCOA1; when associated with Q-415.|||In isoform Alpha-1-deltaBC.|||In isoform Alpha-2.|||In the absence of ATRA, abolishes sumoylation and is mainly nuclear. In the presence of ATRA, some sumoylation, cytoplasmic location, reduced transcriptional activity and no SENP6 binding. Low sumoylation levels in the presence of ATRA and nuclear location in the absence of ATRA; when associated with R-166 or with R-171. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-171.|||Modulating|||NR C4-type|||NR LBD|||No effect on PKB/AKT1-mediated phosphorylation. No repression of transactivation.|||No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation.|||No effect on heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, no increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-369.|||No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-219.|||No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-369.|||Nuclear receptor|||Phosphoserine; by CDK7|||Phosphoserine; by PKA|||Phosphoserine; by PKB/AKT1|||Polar residues|||Required for binding corepressor NCOR1|||Retinoic acid receptor alpha|||Some inhibition of heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-219.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053461|||http://purl.uniprot.org/annotation/VSP_003629|||http://purl.uniprot.org/annotation/VSP_043143
http://togogenome.org/gene/9606:ATG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1Y0                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autophagy protein 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)|||In SCAR25; reduced conjugation to ATG12; decrease in autophagy activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform Short.|||Loss of conjugaction with ATG12. Does affect interaction with DHX58, nor with MAVS.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218994|||http://purl.uniprot.org/annotation/VAR_036243|||http://purl.uniprot.org/annotation/VAR_079274|||http://purl.uniprot.org/annotation/VSP_003791
http://togogenome.org/gene/9606:BEST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Bestrophin-4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143120|||http://purl.uniprot.org/annotation/VAR_048411|||http://purl.uniprot.org/annotation/VAR_048412|||http://purl.uniprot.org/annotation/VAR_048413|||http://purl.uniprot.org/annotation/VAR_048414
http://togogenome.org/gene/9606:MTMR11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FU01                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Myotubularin phosphatase|||Myotubularin-related protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337098|||http://purl.uniprot.org/annotation/VAR_043598|||http://purl.uniprot.org/annotation/VAR_043599|||http://purl.uniprot.org/annotation/VSP_033883|||http://purl.uniprot.org/annotation/VSP_033884|||http://purl.uniprot.org/annotation/VSP_033885|||http://purl.uniprot.org/annotation/VSP_033886|||http://purl.uniprot.org/annotation/VSP_033887|||http://purl.uniprot.org/annotation/VSP_033888|||http://purl.uniprot.org/annotation/VSP_033889|||http://purl.uniprot.org/annotation/VSP_033890|||http://purl.uniprot.org/annotation/VSP_035725|||http://purl.uniprot.org/annotation/VSP_035726
http://togogenome.org/gene/9606:GDF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2A5D6|||http://purl.uniprot.org/uniprot/Q6KF10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Growth/differentiation factor 6|||In KFS1, MCOP4 and LCA17; reduced protein expression associated with decrease in growth factor activity.|||In KFS1.|||In LCA17; found also in a patient with microphthalmia isolated with coloboma type 6 carrying a mutation in GDF3; reduced protein expression associated with decrease in growth factor activity.|||In LCA17; increased protein expression associated with decrease in growth factor activity.|||In LCA17; reduced protein expression associated with decrease in growth factor activity.|||In MCOP4.|||In SYNS4; increases chondrogenic activity; increases SMAD1/5/8 signaling pathway activation; not inhibited by NOG.|||In SYNS4; unknown pathological significance.|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042253|||http://purl.uniprot.org/annotation/PRO_0000342206|||http://purl.uniprot.org/annotation/PRO_5014239205|||http://purl.uniprot.org/annotation/VAR_023599|||http://purl.uniprot.org/annotation/VAR_046903|||http://purl.uniprot.org/annotation/VAR_046904|||http://purl.uniprot.org/annotation/VAR_063024|||http://purl.uniprot.org/annotation/VAR_063025|||http://purl.uniprot.org/annotation/VAR_063026|||http://purl.uniprot.org/annotation/VAR_063027|||http://purl.uniprot.org/annotation/VAR_063028|||http://purl.uniprot.org/annotation/VAR_063029|||http://purl.uniprot.org/annotation/VAR_065151|||http://purl.uniprot.org/annotation/VAR_070254|||http://purl.uniprot.org/annotation/VAR_070255|||http://purl.uniprot.org/annotation/VAR_075366|||http://purl.uniprot.org/annotation/VAR_080489
http://togogenome.org/gene/9606:RASSF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75901                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Ras association domain-containing protein 9|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299452|||http://purl.uniprot.org/annotation/VAR_034820
http://togogenome.org/gene/9606:NAIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YI7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Nuclear apoptosis-inducing factor 1|||Required for nuclear localization and apoptosis-inducing activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089724|||http://purl.uniprot.org/annotation/VSP_014447|||http://purl.uniprot.org/annotation/VSP_014448
http://togogenome.org/gene/9606:NQO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLR8|||http://purl.uniprot.org/uniprot/P15559                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the interaction with TP73.|||Decreases the catalytic efficiency toward menadione. Increases the affinity toward NADH. Increases the catalytic afficiency toward nitrobenzene substrate. Has no effect on the affinity toward NADH; when associated with V-204.|||Flavodoxin-like fold|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Has no effect on the affinity toward NADH; when associated with Y-105.|||Important for apoenzyme conformational stability|||In isoform 2.|||In isoform 3.|||Loss of function associated with defective cofactor binding and accelerated proteasomal degradation.|||NAD(P)H dehydrogenase [quinone] 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071622|||http://purl.uniprot.org/annotation/VAR_008384|||http://purl.uniprot.org/annotation/VAR_016170|||http://purl.uniprot.org/annotation/VAR_050220|||http://purl.uniprot.org/annotation/VSP_042716|||http://purl.uniprot.org/annotation/VSP_044446
http://togogenome.org/gene/9606:LSM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62310                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylalanine|||Removed|||Sm|||U6 snRNA-associated Sm-like protein LSm3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125560
http://togogenome.org/gene/9606:RAB39B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DA2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active mutant locked in the active GTP-bound form.|||Cysteine methyl ester|||Dominant negative mutant.|||Effector region|||In WSMN.|||In WSMN; impaired localization to cytoplasmic vesicles.|||In WSMN; loss of function mutation; expression of the mutation in neuroblastoma cells results in low levels of the mutant protein.|||Phosphoserine|||Ras-related protein Rab-39B|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121255|||http://purl.uniprot.org/annotation/VAR_073264|||http://purl.uniprot.org/annotation/VAR_078514|||http://purl.uniprot.org/annotation/VAR_078515
http://togogenome.org/gene/9606:COMMD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RJ90|||http://purl.uniprot.org/uniprot/Q9Y6G5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 10|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077405|||http://purl.uniprot.org/annotation/VAR_061122
http://togogenome.org/gene/9606:TRPC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCX4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKG/PRKG1|||Short transient receptor potential channel 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215324|||http://purl.uniprot.org/annotation/VSP_043035|||http://purl.uniprot.org/annotation/VSP_044897
http://togogenome.org/gene/9606:ANAPC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5EA39|||http://purl.uniprot.org/uniprot/P60006                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Anaphase-promoting complex subunit 15|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084072|||http://purl.uniprot.org/annotation/VSP_055048
http://togogenome.org/gene/9606:SCN3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY72                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a case of idiopathic ventricular fibrillation; unknown pathological significance.|||Helical|||Ig-like C2-type|||In ATFB16; affects steady-state channel inactivation.|||In ATFB16; results in a decrease in peak sodium current density.|||In ATFB16; results in decreased sodium current density.|||In BRGDA7 and ATFB16; unknown pathological significance; results in a decrease in peak sodium current density.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Sodium channel subunit beta-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014933|||http://purl.uniprot.org/annotation/VAR_035521|||http://purl.uniprot.org/annotation/VAR_035522|||http://purl.uniprot.org/annotation/VAR_049928|||http://purl.uniprot.org/annotation/VAR_062529|||http://purl.uniprot.org/annotation/VAR_065232|||http://purl.uniprot.org/annotation/VAR_071314|||http://purl.uniprot.org/annotation/VAR_071315|||http://purl.uniprot.org/annotation/VAR_071316
http://togogenome.org/gene/9606:PAEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XNE0|||http://purl.uniprot.org/uniprot/B2R4F9|||http://purl.uniprot.org/uniprot/B4E3C0|||http://purl.uniprot.org/uniprot/P09466                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycodelin|||In isoform 2.|||In isoform 3.|||Lipocalin/cytosolic fatty-acid binding|||N-linked (GlcNAc...) (complex) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000123|||http://purl.uniprot.org/annotation/CAR_000124|||http://purl.uniprot.org/annotation/PRO_0000017953|||http://purl.uniprot.org/annotation/PRO_5002801146|||http://purl.uniprot.org/annotation/PRO_5014565766|||http://purl.uniprot.org/annotation/VAR_034355|||http://purl.uniprot.org/annotation/VAR_050178|||http://purl.uniprot.org/annotation/VSP_003140|||http://purl.uniprot.org/annotation/VSP_003141
http://togogenome.org/gene/9606:PRDM14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Interaction with CBFA2T2|||PR domain zinc finger protein 14|||Phosphoserine|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047771|||http://purl.uniprot.org/annotation/VAR_021895
http://togogenome.org/gene/9606:C3orf20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Uncharacterized protein C3orf20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228843|||http://purl.uniprot.org/annotation/VAR_025722|||http://purl.uniprot.org/annotation/VAR_027886|||http://purl.uniprot.org/annotation/VAR_027887|||http://purl.uniprot.org/annotation/VAR_027888|||http://purl.uniprot.org/annotation/VAR_027889|||http://purl.uniprot.org/annotation/VAR_027890|||http://purl.uniprot.org/annotation/VAR_027891|||http://purl.uniprot.org/annotation/VAR_056770|||http://purl.uniprot.org/annotation/VAR_056771|||http://purl.uniprot.org/annotation/VSP_017722
http://togogenome.org/gene/9606:DHX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8F4|||http://purl.uniprot.org/uniprot/F5H658|||http://purl.uniprot.org/uniprot/K7END7|||http://purl.uniprot.org/uniprot/Q05CV4|||http://purl.uniprot.org/uniprot/Q14562|||http://purl.uniprot.org/uniprot/Q86YB2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX8|||Basic and acidic residues|||Basic residues|||DEAH box|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In GET; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.|||In LAT; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA.|||Phosphoserine|||S1 motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055131|||http://purl.uniprot.org/annotation/VAR_052174|||http://purl.uniprot.org/annotation/VAR_083620
http://togogenome.org/gene/9606:XRCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEK2|||http://purl.uniprot.org/uniprot/O43543                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  DNA repair protein XRCC2|||Does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells.|||Found in a patient with borderline microcephaly, bilateral hypoplastic thumb, multiple cafe late spots, strabismus and dysmorphic facial features; unknown pathological significance.|||In SPGF50 and POF17; due to a nucleotide substitution that causes partial exon 2 skipping; patient cells contain both normally spliced transcripts and transcripts lacking exon 2.|||Likely benign variant; does not affect function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells.|||Phosphoserine|||Rare variant; found in breast cancer; unknown pathological significance; moderately decreased function in double-strand break repair via homologous recombination as shown in rescue assays of XRCC2-deficient cells.|||RecA family profile 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122948|||http://purl.uniprot.org/annotation/VAR_020403|||http://purl.uniprot.org/annotation/VAR_020404|||http://purl.uniprot.org/annotation/VAR_029294|||http://purl.uniprot.org/annotation/VAR_077167|||http://purl.uniprot.org/annotation/VAR_077168|||http://purl.uniprot.org/annotation/VAR_077169|||http://purl.uniprot.org/annotation/VAR_077170|||http://purl.uniprot.org/annotation/VAR_077171|||http://purl.uniprot.org/annotation/VAR_077172|||http://purl.uniprot.org/annotation/VAR_077173|||http://purl.uniprot.org/annotation/VAR_077174|||http://purl.uniprot.org/annotation/VAR_077175|||http://purl.uniprot.org/annotation/VAR_077176|||http://purl.uniprot.org/annotation/VAR_077177|||http://purl.uniprot.org/annotation/VAR_077178|||http://purl.uniprot.org/annotation/VAR_077179|||http://purl.uniprot.org/annotation/VAR_077180|||http://purl.uniprot.org/annotation/VAR_077181|||http://purl.uniprot.org/annotation/VAR_077182|||http://purl.uniprot.org/annotation/VAR_077183|||http://purl.uniprot.org/annotation/VAR_077184|||http://purl.uniprot.org/annotation/VAR_077185|||http://purl.uniprot.org/annotation/VAR_077186|||http://purl.uniprot.org/annotation/VAR_082157|||http://purl.uniprot.org/annotation/VAR_085247
http://togogenome.org/gene/9606:BEST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1M1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Bestrophin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143121|||http://purl.uniprot.org/annotation/VAR_048409|||http://purl.uniprot.org/annotation/VAR_048410|||http://purl.uniprot.org/annotation/VSP_008977|||http://purl.uniprot.org/annotation/VSP_008978|||http://purl.uniprot.org/annotation/VSP_008981|||http://purl.uniprot.org/annotation/VSP_008982|||http://purl.uniprot.org/annotation/VSP_008983|||http://purl.uniprot.org/annotation/VSP_046979|||http://purl.uniprot.org/annotation/VSP_046980
http://togogenome.org/gene/9606:PSKH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||Polar residues|||Protein kinase|||Serine/threonine-protein kinase H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086171|||http://purl.uniprot.org/annotation/VAR_040615|||http://purl.uniprot.org/annotation/VAR_040616|||http://purl.uniprot.org/annotation/VAR_040617|||http://purl.uniprot.org/annotation/VAR_040618|||http://purl.uniprot.org/annotation/VAR_040619|||http://purl.uniprot.org/annotation/VAR_040620|||http://purl.uniprot.org/annotation/VAR_040621|||http://purl.uniprot.org/annotation/VAR_040622|||http://purl.uniprot.org/annotation/VAR_040623|||http://purl.uniprot.org/annotation/VAR_040624|||http://purl.uniprot.org/annotation/VAR_040625|||http://purl.uniprot.org/annotation/VAR_040626
http://togogenome.org/gene/9606:PRDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13029                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; atypical|||C2H2-type 8; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||Loss of histone methyltransferase activity.|||PR domain zinc finger protein 2|||Phosphoserine|||Polar residues|||Pro residues|||Reduced histone methyltransferase activity.|||Retinoblastoma protein binding|||SET|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041634|||http://purl.uniprot.org/annotation/VAR_052929|||http://purl.uniprot.org/annotation/VAR_052930|||http://purl.uniprot.org/annotation/VSP_006927|||http://purl.uniprot.org/annotation/VSP_006928|||http://purl.uniprot.org/annotation/VSP_018974|||http://purl.uniprot.org/annotation/VSP_046421|||http://purl.uniprot.org/annotation/VSP_046422
http://togogenome.org/gene/9606:USP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54578                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 14|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080636|||http://purl.uniprot.org/annotation/VSP_047343|||http://purl.uniprot.org/annotation/VSP_057292
http://togogenome.org/gene/9606:BLCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62952                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Bladder cancer-associated protein|||Helical|||In RNA edited version.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064850|||http://purl.uniprot.org/annotation/VAR_068908|||http://purl.uniprot.org/annotation/VAR_068909|||http://purl.uniprot.org/annotation/VAR_068910
http://togogenome.org/gene/9606:SLC43A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0AZP8|||http://purl.uniprot.org/uniprot/Q8NBI5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Equilibrative nucleobase transporter 1|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305036|||http://purl.uniprot.org/annotation/VAR_035156|||http://purl.uniprot.org/annotation/VSP_055620
http://togogenome.org/gene/9606:TRIM49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PK69|||http://purl.uniprot.org/uniprot/P0CI25                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 49                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056273|||http://purl.uniprot.org/annotation/VAR_061824
http://togogenome.org/gene/9606:NONO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Z9|||http://purl.uniprot.org/uniprot/Q15233                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-267.|||Abolishes interaction with PSPC1 and localization in nuclear paraspeckles; when associated with A-271.|||Breakpoint for translocation to form NONO-TFE3|||DBHS|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Non-POU domain-containing octamer-binding protein|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081683|||http://purl.uniprot.org/annotation/VSP_045470
http://togogenome.org/gene/9606:TMEM150A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TG1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 150A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274775|||http://purl.uniprot.org/annotation/VSP_022874|||http://purl.uniprot.org/annotation/VSP_022875
http://togogenome.org/gene/9606:EEFSEC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57772                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1|||G2|||G3|||G4|||G5|||In isoform 2.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Selenocysteine-specific elongation factor|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091478|||http://purl.uniprot.org/annotation/VAR_055712|||http://purl.uniprot.org/annotation/VSP_057185
http://togogenome.org/gene/9606:CCNG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16589                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-G2|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080469|||http://purl.uniprot.org/annotation/VAR_014333|||http://purl.uniprot.org/annotation/VAR_014334|||http://purl.uniprot.org/annotation/VSP_053893
http://togogenome.org/gene/9606:TENM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6N022                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||Extracellular|||Found in a patiend with developmental delay, cleft palate and proliferative retinopathy; unknown pathological significance.|||Helical|||In ETM5; dominant negative effect on central nervous myelination and axon guidance; changed localization to the plasma membrane; clustered plasma membrane localization.|||In ETM5; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Phosphoserine|||Phosphothreonine|||Polar residues|||Teneurin N-terminal|||Teneurin-4|||YD 1|||YD 10|||YD 11|||YD 12|||YD 13|||YD 14|||YD 15|||YD 16|||YD 17|||YD 18|||YD 19|||YD 2|||YD 20|||YD 21|||YD 22|||YD 23|||YD 3|||YD 4|||YD 5|||YD 6|||YD 7|||YD 8|||YD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259508|||http://purl.uniprot.org/annotation/VAR_060130|||http://purl.uniprot.org/annotation/VAR_060131|||http://purl.uniprot.org/annotation/VAR_062167|||http://purl.uniprot.org/annotation/VAR_076521|||http://purl.uniprot.org/annotation/VAR_076522|||http://purl.uniprot.org/annotation/VAR_076523|||http://purl.uniprot.org/annotation/VAR_076654|||http://purl.uniprot.org/annotation/VAR_076655|||http://purl.uniprot.org/annotation/VAR_076656|||http://purl.uniprot.org/annotation/VAR_076657|||http://purl.uniprot.org/annotation/VAR_076658|||http://purl.uniprot.org/annotation/VAR_076659|||http://purl.uniprot.org/annotation/VAR_076660|||http://purl.uniprot.org/annotation/VAR_076661|||http://purl.uniprot.org/annotation/VAR_085138
http://togogenome.org/gene/9606:VWA3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCI4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||VWFA 1|||VWFA 2|||von Willebrand factor A domain-containing protein 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324623|||http://purl.uniprot.org/annotation/VAR_057020|||http://purl.uniprot.org/annotation/VAR_057021|||http://purl.uniprot.org/annotation/VAR_059738|||http://purl.uniprot.org/annotation/VSP_032318|||http://purl.uniprot.org/annotation/VSP_032319|||http://purl.uniprot.org/annotation/VSP_032320|||http://purl.uniprot.org/annotation/VSP_032321
http://togogenome.org/gene/9606:CMPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494BXC7|||http://purl.uniprot.org/uniprot/P30085                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||LID|||N6-acetyllysine|||N6-succinyllysine|||NMP|||Phosphoserine|||UMP-CMP kinase|||nucleoside-diphosphate kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158949|||http://purl.uniprot.org/annotation/PRO_5019733336|||http://purl.uniprot.org/annotation/VSP_046683|||http://purl.uniprot.org/annotation/VSP_060085
http://togogenome.org/gene/9606:OR2T5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IEZ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150500|||http://purl.uniprot.org/annotation/VAR_080453
http://togogenome.org/gene/9606:SUPV3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z611|||http://purl.uniprot.org/uniprot/Q8IYB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase SUPV3L1, mitochondrial|||Abolishes ATPase activity. Abolishes helicase activity and reduces double-stranded RNA degradation. Does not abolish formation of the mitochondrial RNA-degrading complex.|||Abolishes ATPase and dsDNA and dsRNA helicase activities.|||Basic and acidic residues|||Disordered|||Does not abolish ATPase activity. Shows a loss of double-stranded RNA-binding, helicase and degrading activities.|||Helicase ATP-binding|||Helicase C-terminal|||Interaction with LAMTOR5, important for protein stability|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310545|||http://purl.uniprot.org/annotation/VAR_037076|||http://purl.uniprot.org/annotation/VAR_061214
http://togogenome.org/gene/9606:GORASP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPY8|||http://purl.uniprot.org/uniprot/B4E1H8|||http://purl.uniprot.org/uniprot/Q9BQQ3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Essential for interaction with GOLGA2/GM130|||GRASP|||Golgi reassembly-stacking protein 1|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||PDZ GRASP-type|||PDZ GRASP-type 1|||PDZ GRASP-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087570|||http://purl.uniprot.org/annotation/VAR_051016|||http://purl.uniprot.org/annotation/VSP_011306|||http://purl.uniprot.org/annotation/VSP_011307|||http://purl.uniprot.org/annotation/VSP_011308|||http://purl.uniprot.org/annotation/VSP_011309
http://togogenome.org/gene/9606:RAB6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||Interacts with APBA1. Abolishes localization of VPS13B to the Golgi.|||Loss of APBA1-binding. Abolishes localization of VPS13B to the Golgi.|||O-AMP-tyrosine; by Legionella DrrA|||Ras-related protein Rab-6B|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121115|||http://purl.uniprot.org/annotation/VSP_055831
http://togogenome.org/gene/9606:SLC39A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRY0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Phosphoserine|||Zinc transporter ZIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312868|||http://purl.uniprot.org/annotation/VAR_037599|||http://purl.uniprot.org/annotation/VAR_037600|||http://purl.uniprot.org/annotation/VSP_029920|||http://purl.uniprot.org/annotation/VSP_029921
http://togogenome.org/gene/9606:GALR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47211                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Galanin receptor type 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069463|||http://purl.uniprot.org/annotation/VAR_003514|||http://purl.uniprot.org/annotation/VAR_014682|||http://purl.uniprot.org/annotation/VAR_014683
http://togogenome.org/gene/9606:CLRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PK11                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Clarin-2|||Helical|||In DFNB117; due to a nucleotide substitution that can result in aberrant splicing; patient cells contain both normally spliced transcripts and transcripts that retained intron 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274697|||http://purl.uniprot.org/annotation/VAR_053826|||http://purl.uniprot.org/annotation/VAR_053827|||http://purl.uniprot.org/annotation/VAR_085237
http://togogenome.org/gene/9606:RTN4RL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Basic residues|||Disordered|||GPI-anchor amidated serine|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||LRRNT|||Removed in mature form|||Reticulon-4 receptor-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046042|||http://purl.uniprot.org/annotation/PRO_0000046043
http://togogenome.org/gene/9606:DTWD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBA8                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  DXTW|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||tRNA-uridine aminocarboxypropyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271128|||http://purl.uniprot.org/annotation/VSP_060608
http://togogenome.org/gene/9606:FGD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6J4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 2|||FYVE-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH 1|||PH 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080942|||http://purl.uniprot.org/annotation/VAR_021491|||http://purl.uniprot.org/annotation/VSP_013065|||http://purl.uniprot.org/annotation/VSP_013066|||http://purl.uniprot.org/annotation/VSP_013067|||http://purl.uniprot.org/annotation/VSP_013068|||http://purl.uniprot.org/annotation/VSP_013070|||http://purl.uniprot.org/annotation/VSP_013071|||http://purl.uniprot.org/annotation/VSP_013072|||http://purl.uniprot.org/annotation/VSP_038219
http://togogenome.org/gene/9606:PIPOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0Z9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Microbody targeting signal|||N6-acetyllysine|||Peroxisomal sarcosine oxidase|||S-8alpha-FAD cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213773
http://togogenome.org/gene/9606:TCEAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969E4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Phosphoserine|||Transcription elongation factor A protein-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239207|||http://purl.uniprot.org/annotation/VAR_059829
http://togogenome.org/gene/9606:DEFB128                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7B8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 128                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007004|||http://purl.uniprot.org/annotation/VAR_048866
http://togogenome.org/gene/9606:WDR74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6RFH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N6-methyllysine|||Phosphoserine|||Reduces interaction with NVL.|||Required for nucleolar and nuclear location|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051428|||http://purl.uniprot.org/annotation/VSP_011957
http://togogenome.org/gene/9606:BAHCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P281                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||BAH|||BAH and coiled-coil domain-containing protein 1|||Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312118|||http://purl.uniprot.org/annotation/VAR_050685|||http://purl.uniprot.org/annotation/VAR_059589|||http://purl.uniprot.org/annotation/VAR_061559|||http://purl.uniprot.org/annotation/VAR_061560|||http://purl.uniprot.org/annotation/VAR_061561|||http://purl.uniprot.org/annotation/VAR_061562
http://togogenome.org/gene/9606:SNRPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14678|||http://purl.uniprot.org/uniprot/Q66K91                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Dimethylated arginine; in A2780 ovarian carcinoma cell line|||Disordered|||In CCMS.|||In CCMS; expression of the protein is reduced.|||In isoform SM-B.|||In isoform SM-B1.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Pro residues|||Repeat-rich region|||Sm|||Small nuclear ribonucleoprotein-associated proteins B and B'                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125517|||http://purl.uniprot.org/annotation/VAR_052274|||http://purl.uniprot.org/annotation/VAR_073380|||http://purl.uniprot.org/annotation/VAR_073381|||http://purl.uniprot.org/annotation/VAR_073382|||http://purl.uniprot.org/annotation/VAR_073383|||http://purl.uniprot.org/annotation/VSP_005914|||http://purl.uniprot.org/annotation/VSP_012221
http://togogenome.org/gene/9606:ZDHHC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZN3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||In isoform 2.|||Lumenal|||Palmitoyltransferase ZDHHC14|||Phosphoserine|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212891|||http://purl.uniprot.org/annotation/VAR_034586|||http://purl.uniprot.org/annotation/VSP_008651
http://togogenome.org/gene/9606:KIZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X251|||http://purl.uniprot.org/uniprot/Q2M2Z5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by PLK1.|||Basic and acidic residues|||Centrosomal protein kizuna|||Disordered|||Does not affect phosphorylation status.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphomimetic mutant able to partially restore focused bipolar spindles to PLK1-depleted cells that otherwise possess aberrant spindles with diffuse or multiple gamma-tubulin signals.|||Phosphoserine|||Phosphothreonine; by PLK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301851|||http://purl.uniprot.org/annotation/VAR_034909|||http://purl.uniprot.org/annotation/VAR_034910|||http://purl.uniprot.org/annotation/VSP_027879|||http://purl.uniprot.org/annotation/VSP_027880|||http://purl.uniprot.org/annotation/VSP_027881|||http://purl.uniprot.org/annotation/VSP_027882|||http://purl.uniprot.org/annotation/VSP_037837|||http://purl.uniprot.org/annotation/VSP_037838
http://togogenome.org/gene/9606:ERCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07992                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  DNA excision repair protein ERCC-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HhH2, dimerization with ERCC4/XPF|||Impaired interaction with ERCC4.|||In COFS4; does not alter interaction with ERCC4/XPF.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087006|||http://purl.uniprot.org/annotation/VAR_019167|||http://purl.uniprot.org/annotation/VAR_032776|||http://purl.uniprot.org/annotation/VSP_042727|||http://purl.uniprot.org/annotation/VSP_043455|||http://purl.uniprot.org/annotation/VSP_053474
http://togogenome.org/gene/9606:ZNF772                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DY9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 772                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263689|||http://purl.uniprot.org/annotation/VAR_029604|||http://purl.uniprot.org/annotation/VAR_029605|||http://purl.uniprot.org/annotation/VSP_021882|||http://purl.uniprot.org/annotation/VSP_043423
http://togogenome.org/gene/9606:CCDC158                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIY6|||http://purl.uniprot.org/uniprot/Q5M9N0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 158|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325760|||http://purl.uniprot.org/annotation/VAR_039909|||http://purl.uniprot.org/annotation/VAR_039910|||http://purl.uniprot.org/annotation/VSP_032390|||http://purl.uniprot.org/annotation/VSP_032391|||http://purl.uniprot.org/annotation/VSP_032392
http://togogenome.org/gene/9606:DHDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ10                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Site                                                                                  ^@                                                                                  May play an important role for the adaptation of the alcohol substrate into the binding site|||May play an important role in catalytic activity|||May play an important role in coenzyme binding|||Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315361|||http://purl.uniprot.org/annotation/VAR_038174|||http://purl.uniprot.org/annotation/VAR_038175|||http://purl.uniprot.org/annotation/VAR_038176|||http://purl.uniprot.org/annotation/VAR_038177|||http://purl.uniprot.org/annotation/VAR_038178
http://togogenome.org/gene/9606:EP400                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L91                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DEAH box-like|||Disordered|||E1A-binding protein p400|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Interaction with ZNF42|||Interactions with RUVBL1 and RUVBL2|||Myb-like|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074312|||http://purl.uniprot.org/annotation/VAR_046957|||http://purl.uniprot.org/annotation/VSP_011992|||http://purl.uniprot.org/annotation/VSP_011993|||http://purl.uniprot.org/annotation/VSP_011994|||http://purl.uniprot.org/annotation/VSP_011995
http://togogenome.org/gene/9606:TMIGD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMS9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||Transmembrane domain-containing protein TMIGD3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416044|||http://purl.uniprot.org/annotation/VSP_057521
http://togogenome.org/gene/9606:DUSP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTR2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 19|||In isoform 2.|||N-acetylmethionine|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094832|||http://purl.uniprot.org/annotation/VAR_051755|||http://purl.uniprot.org/annotation/VSP_005138
http://togogenome.org/gene/9606:SERPINB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3Q8|||http://purl.uniprot.org/uniprot/O75635                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Reactive bond|||Serpin|||Serpin B7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094108|||http://purl.uniprot.org/annotation/VAR_034512|||http://purl.uniprot.org/annotation/VSP_044711
http://togogenome.org/gene/9606:IKZF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5V7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Decreased protein abundance. Decreased chromatin binding. Decreased localization to the nucleus. Tends to remain in the cytosol.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In THC7; unknown pathological significance.|||No effect on protein abundance. No effect on chromatin binding. No effect on localization to the nucleus.|||Polar residues|||Zinc finger protein Pegasus                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299471|||http://purl.uniprot.org/annotation/VAR_085558|||http://purl.uniprot.org/annotation/VAR_085559
http://togogenome.org/gene/9606:MAGEA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43356|||http://purl.uniprot.org/uniprot/Q6P448                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Improves ability to bind to HLA-A1.|||MAGE|||Melanoma-associated antigen 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156702
http://togogenome.org/gene/9606:TBXAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24557|||http://purl.uniprot.org/uniprot/Q53F23                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect thromboxane-A synthase activity. Does not affect heme-binding.|||Helical|||In GHDD.|||In a breast cancer sample; somatic mutation.|||In allele CYP5A1*2.|||In allele CYP5A1*3.|||In allele CYP5A1*4.|||In allele CYP5A1*5; KM value about 1.5 higher for PEG2; Vmax/KM approximately 27% of that of the wild-type.|||In allele CYP5A1*6; does not affect KM value for PEG2; does not affect Vmax/KM value.|||In allele CYP5A1*7; does not affect KM value for PEG2; does not affect Vmax/KM value.|||In allele CYP5A1*8; KM value about 1.5 higher for PEG2; Vmax/KM approximately 56 % of that of the wild-type.|||In allele CYP5A1*9.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of thromboxane-A synthase activity. Decreased heme-binding.|||Lumenal|||The KM value is about 1.5 higher for PEG2; in allele CYP5A1*5; KM value about 1.5 higher for PEG2; Vmax/KM approximately 50% of that of the wild-type.|||Thromboxane-A synthase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052256|||http://purl.uniprot.org/annotation/VAR_010919|||http://purl.uniprot.org/annotation/VAR_010920|||http://purl.uniprot.org/annotation/VAR_010921|||http://purl.uniprot.org/annotation/VAR_010922|||http://purl.uniprot.org/annotation/VAR_010923|||http://purl.uniprot.org/annotation/VAR_010924|||http://purl.uniprot.org/annotation/VAR_010925|||http://purl.uniprot.org/annotation/VAR_014157|||http://purl.uniprot.org/annotation/VAR_014158|||http://purl.uniprot.org/annotation/VAR_014159|||http://purl.uniprot.org/annotation/VAR_014160|||http://purl.uniprot.org/annotation/VAR_014161|||http://purl.uniprot.org/annotation/VAR_014647|||http://purl.uniprot.org/annotation/VAR_014648|||http://purl.uniprot.org/annotation/VAR_014649|||http://purl.uniprot.org/annotation/VAR_016158|||http://purl.uniprot.org/annotation/VAR_018378|||http://purl.uniprot.org/annotation/VAR_018379|||http://purl.uniprot.org/annotation/VAR_018380|||http://purl.uniprot.org/annotation/VAR_036294|||http://purl.uniprot.org/annotation/VAR_044386|||http://purl.uniprot.org/annotation/VAR_044387|||http://purl.uniprot.org/annotation/VAR_044388|||http://purl.uniprot.org/annotation/VAR_044389|||http://purl.uniprot.org/annotation/VAR_044390|||http://purl.uniprot.org/annotation/VAR_044391|||http://purl.uniprot.org/annotation/VAR_055565|||http://purl.uniprot.org/annotation/VAR_055566|||http://purl.uniprot.org/annotation/VAR_058465|||http://purl.uniprot.org/annotation/VAR_058466|||http://purl.uniprot.org/annotation/VSP_047217|||http://purl.uniprot.org/annotation/VSP_054121|||http://purl.uniprot.org/annotation/VSP_054122|||http://purl.uniprot.org/annotation/VSP_054123
http://togogenome.org/gene/9606:RELCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y566|||http://purl.uniprot.org/uniprot/Q96ES0|||http://purl.uniprot.org/uniprot/Q9P260                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT|||HEAT 1|||HEAT 2|||HEAT 3|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with RAB11A and RAB11B|||LisH|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RAB11-binding protein RELCH|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313093|||http://purl.uniprot.org/annotation/VAR_037660|||http://purl.uniprot.org/annotation/VSP_030016|||http://purl.uniprot.org/annotation/VSP_030017
http://togogenome.org/gene/9606:DOP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein dopey-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190974|||http://purl.uniprot.org/annotation/VAR_027939|||http://purl.uniprot.org/annotation/VAR_027940|||http://purl.uniprot.org/annotation/VAR_027941|||http://purl.uniprot.org/annotation/VAR_027942|||http://purl.uniprot.org/annotation/VAR_034688|||http://purl.uniprot.org/annotation/VSP_027387
http://togogenome.org/gene/9606:GMPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK6|||http://purl.uniprot.org/uniprot/P49915                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  For GATase activity|||GMP synthase [glutamine-hydrolyzing]|||GMPS ATP-PPase|||Glutamine amidotransferase type-1|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000140257|||http://purl.uniprot.org/annotation/VSP_053933
http://togogenome.org/gene/9606:CPSF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16630                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Binds to HIV-1 capsid protein p24 (CA)|||Abolishes interaction with NUDT21/CPSF5; when associated with V-86.|||Abolishes interaction with NUDT21/CPSF5; when associated with V-87.|||Arg/Ser-rich domain|||Basic and acidic residues|||Cleavage and polyadenylation specificity factor subunit 6|||Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-202 and A-206.|||Decreased methylation in presence of PRMT5/WDR77. Loss of methylation in presence of PRMT5/WDR77 or PRMT1; when associated with A-204 and A-206.|||Disordered|||GAR|||In isoform 2.|||In isoform 3.|||Increases affinity for UGUARNA by 40%.|||Loss of methylation in presence of PRMT5/WDR77 or PRMT1.|||Necessary for RNA-binding|||Necessary for interaction with NUDT21/CPSF5|||Necessary for interaction with NXF1|||Necessary for interaction with SRSF3, SRSF7 and TRA2B/SFRS10|||Necessary for nuclear paraspeckles localization|||Phosphoserine|||Phosphothreonine|||Pro residues|||RRM|||Reduces affinity for UGUARNA by 40%; when associated with A-128.|||Reduces affinity for UGUARNA by 40%; when associated with A-84.|||Reduces affinity for UGUARNA by 70%. Strongly reduced affinity for UGUARNA; when associated with A-94.|||Reduces affinity for UGUARNA by 85%.|||Strongly reduced affinity for UGUARNA; when associated with 90-A-A-91.|||Sufficient for nuclear speckle localization|||Sufficient for nuclear targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081521|||http://purl.uniprot.org/annotation/VSP_017191|||http://purl.uniprot.org/annotation/VSP_017192
http://togogenome.org/gene/9606:TRAPPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DI81|||http://purl.uniprot.org/uniprot/P0DI82                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SEDT; loss of interaction with ENO1, PITX1 and SF1.|||In SEDT; loss-of-function mutation.|||In SEDT; mild form; loss of interaction with ENO1, PITX1 and SF1.|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||Trafficking protein particle complex subunit 2|||Trafficking protein particle complex subunit 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211566|||http://purl.uniprot.org/annotation/PRO_0000412454|||http://purl.uniprot.org/annotation/VAR_012358|||http://purl.uniprot.org/annotation/VAR_012359|||http://purl.uniprot.org/annotation/VAR_012360|||http://purl.uniprot.org/annotation/VAR_012361|||http://purl.uniprot.org/annotation/VSP_006040|||http://purl.uniprot.org/annotation/VSP_041681|||http://purl.uniprot.org/annotation/VSP_041682
http://togogenome.org/gene/9606:NOP16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nucleolar protein 16|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050817|||http://purl.uniprot.org/annotation/VSP_045583|||http://purl.uniprot.org/annotation/VSP_057393
http://togogenome.org/gene/9606:AK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4Y4|||http://purl.uniprot.org/uniprot/Q9UIJ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylate kinase active site lid|||GTP:AMP phosphotransferase AK3, mitochondrial|||In isoform 2.|||In isoform 3.|||LID|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||NMP|||NMPbind|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158922|||http://purl.uniprot.org/annotation/VSP_043090|||http://purl.uniprot.org/annotation/VSP_044876
http://togogenome.org/gene/9606:C1orf146                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVC0                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein SPO16 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299020
http://togogenome.org/gene/9606:VRTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8Y1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||Vertnin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089926|||http://purl.uniprot.org/annotation/VAR_035677|||http://purl.uniprot.org/annotation/VAR_050876
http://togogenome.org/gene/9606:SAP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYF9|||http://purl.uniprot.org/uniprot/Q8TEE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Histone deacetylase complex subunit SAP25|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000350873
http://togogenome.org/gene/9606:HPS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9V4|||http://purl.uniprot.org/uniprot/Q969F9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BLOC-2 complex member HPS3|||BLOC-2 complex member HPS3 C-terminal|||BLOC-2 complex member HPS3 N-terminal|||BLOC-2 complex member HPS3 central region|||Clathrin-binding|||In HPS3; mild.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084050|||http://purl.uniprot.org/annotation/VAR_013251|||http://purl.uniprot.org/annotation/VAR_035928|||http://purl.uniprot.org/annotation/VAR_038379|||http://purl.uniprot.org/annotation/VSP_003878|||http://purl.uniprot.org/annotation/VSP_003879
http://togogenome.org/gene/9606:OSBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22059                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FFAT|||Impaired lipid exchange activity. Abolishes interaction with VAPA.|||Impaired lipid exchange activity. Induces a shift in subcellular location to the endoplasmic reticulum.|||In a colorectal cancer sample; somatic mutation.|||N-acetylalanine|||Oxysterol-binding protein 1|||PH|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100364|||http://purl.uniprot.org/annotation/VAR_036099
http://togogenome.org/gene/9606:ZNF320                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRD8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 320                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300263
http://togogenome.org/gene/9606:RNASE7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1E1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mass|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Critical for catalytic activity|||Important for antibacterial activity|||Loss of catalytic activity. No effect on bactericidal activity.|||Moderate loss of bactericidal activity. No effect on catalytic activity.|||N-linked (GlcNAc...) asparagine|||No significant effect on bactericidal activity or catalytic activity.|||Proton acceptor|||Proton donor|||Ribonuclease 7|||Significant loss of bactericidal activity. No effect on catalytic activity.|||Slight loss of bactericidal activity. No effect on catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030901|||http://purl.uniprot.org/annotation/VAR_024619|||http://purl.uniprot.org/annotation/VAR_024620
http://togogenome.org/gene/9606:LRRC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BKY1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||Leucine-rich repeat-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084470
http://togogenome.org/gene/9606:CDHR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8X2|||http://purl.uniprot.org/uniprot/E7EQG5|||http://purl.uniprot.org/uniprot/Q6ZTQ4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-related family member 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Increases cell surface expression.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305903|||http://purl.uniprot.org/annotation/VAR_035228|||http://purl.uniprot.org/annotation/VAR_035229|||http://purl.uniprot.org/annotation/VAR_035230|||http://purl.uniprot.org/annotation/VSP_028352|||http://purl.uniprot.org/annotation/VSP_028353|||http://purl.uniprot.org/annotation/VSP_028354
http://togogenome.org/gene/9606:TJP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95049                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 3.|||In isoform 4.|||In isoform 6.|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||Tight junction protein ZO-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094546|||http://purl.uniprot.org/annotation/VAR_056114|||http://purl.uniprot.org/annotation/VSP_040238|||http://purl.uniprot.org/annotation/VSP_047022|||http://purl.uniprot.org/annotation/VSP_053844
http://togogenome.org/gene/9606:DOCK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT38|||http://purl.uniprot.org/uniprot/A6H8Z6|||http://purl.uniprot.org/uniprot/B3KXE2|||http://purl.uniprot.org/uniprot/B7Z2G6|||http://purl.uniprot.org/uniprot/B9EG73|||http://purl.uniprot.org/uniprot/Q9BZ29                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 9|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with CDC42|||PH|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189999|||http://purl.uniprot.org/annotation/VAR_053067|||http://purl.uniprot.org/annotation/VAR_062000|||http://purl.uniprot.org/annotation/VSP_004024|||http://purl.uniprot.org/annotation/VSP_007709|||http://purl.uniprot.org/annotation/VSP_007710|||http://purl.uniprot.org/annotation/VSP_017128|||http://purl.uniprot.org/annotation/VSP_045683|||http://purl.uniprot.org/annotation/VSP_045684
http://togogenome.org/gene/9606:BTBD17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NE02                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  BACK|||BTB|||BTB/POZ domain-containing protein 17|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340704
http://togogenome.org/gene/9606:PLPPR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32ZL2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Phospholipid phosphatase-related protein type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321933|||http://purl.uniprot.org/annotation/VSP_031828
http://togogenome.org/gene/9606:METTL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XA0|||http://purl.uniprot.org/uniprot/Q8N712                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Histone-arginine methyltransferase METTL23|||In MRT44.|||In MRT44; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321520|||http://purl.uniprot.org/annotation/VAR_039343|||http://purl.uniprot.org/annotation/VAR_085971|||http://purl.uniprot.org/annotation/VAR_085972|||http://purl.uniprot.org/annotation/VSP_055637
http://togogenome.org/gene/9606:TUBAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHL2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||MREC motif|||Tubulin alpha chain-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313709|||http://purl.uniprot.org/annotation/VAR_037706|||http://purl.uniprot.org/annotation/VAR_037707|||http://purl.uniprot.org/annotation/VSP_030108
http://togogenome.org/gene/9606:MRPL46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2W6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL46|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030576|||http://purl.uniprot.org/annotation/VAR_052046
http://togogenome.org/gene/9606:POC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA72                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrin-binding (CBR) 1|||Centrin-binding (CBR) 2|||Centrin-binding (CBR) 3|||Centrosomal protein POC5|||Disordered|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281908|||http://purl.uniprot.org/annotation/VAR_031324|||http://purl.uniprot.org/annotation/VAR_031325|||http://purl.uniprot.org/annotation/VAR_050778|||http://purl.uniprot.org/annotation/VSP_024098|||http://purl.uniprot.org/annotation/VSP_024099|||http://purl.uniprot.org/annotation/VSP_024100
http://togogenome.org/gene/9606:FAM229B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0N7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM229B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335816
http://togogenome.org/gene/9606:MBD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P0P0|||http://purl.uniprot.org/uniprot/Q96DN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||MBD|||Methyl-CpG-binding domain protein 6|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096267
http://togogenome.org/gene/9606:MMP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0I2|||http://purl.uniprot.org/uniprot/P22894                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||N-linked (GlcNAc...) asparagine|||Neutrophil collagenase|||Peptidase metallopeptidase|||Phosphotyrosine; by PKDCC|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028744|||http://purl.uniprot.org/annotation/PRO_0000028745|||http://purl.uniprot.org/annotation/VAR_006730|||http://purl.uniprot.org/annotation/VAR_025036|||http://purl.uniprot.org/annotation/VAR_025037|||http://purl.uniprot.org/annotation/VAR_025038|||http://purl.uniprot.org/annotation/VAR_025039|||http://purl.uniprot.org/annotation/VAR_025040|||http://purl.uniprot.org/annotation/VAR_025041|||http://purl.uniprot.org/annotation/VAR_025042
http://togogenome.org/gene/9606:TMEM245                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H330                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Removed|||Transmembrane protein 245                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089670|||http://purl.uniprot.org/annotation/VAR_056815|||http://purl.uniprot.org/annotation/VAR_056816|||http://purl.uniprot.org/annotation/VAR_059604|||http://purl.uniprot.org/annotation/VSP_014680|||http://purl.uniprot.org/annotation/VSP_059402|||http://purl.uniprot.org/annotation/VSP_059403|||http://purl.uniprot.org/annotation/VSP_059404
http://togogenome.org/gene/9606:TAF5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75529                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051261|||http://purl.uniprot.org/annotation/VSP_010156|||http://purl.uniprot.org/annotation/VSP_010157
http://togogenome.org/gene/9606:TVP23C-CDRT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYB9|||http://purl.uniprot.org/uniprot/Q96ET8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Golgi apparatus membrane protein TVP23 homolog C|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212831|||http://purl.uniprot.org/annotation/VAR_024929|||http://purl.uniprot.org/annotation/VAR_055797|||http://purl.uniprot.org/annotation/VSP_017019|||http://purl.uniprot.org/annotation/VSP_017020|||http://purl.uniprot.org/annotation/VSP_040556|||http://purl.uniprot.org/annotation/VSP_040557
http://togogenome.org/gene/9606:NEK10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KTB8|||http://purl.uniprot.org/uniprot/Q6ZWH5|||http://purl.uniprot.org/uniprot/Q8N774                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM|||Catalytically inactive. Impaired mucociliary transport.|||Disordered|||In CILD44; unknown pathological significance.|||In a metastatic melanoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Increased mucociliary transport.|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259767|||http://purl.uniprot.org/annotation/VAR_040928|||http://purl.uniprot.org/annotation/VAR_040929|||http://purl.uniprot.org/annotation/VAR_040930|||http://purl.uniprot.org/annotation/VAR_040931|||http://purl.uniprot.org/annotation/VAR_040932|||http://purl.uniprot.org/annotation/VAR_040933|||http://purl.uniprot.org/annotation/VAR_040934|||http://purl.uniprot.org/annotation/VAR_083827|||http://purl.uniprot.org/annotation/VAR_083828|||http://purl.uniprot.org/annotation/VSP_021534|||http://purl.uniprot.org/annotation/VSP_021535|||http://purl.uniprot.org/annotation/VSP_021536|||http://purl.uniprot.org/annotation/VSP_035688|||http://purl.uniprot.org/annotation/VSP_035689|||http://purl.uniprot.org/annotation/VSP_035690|||http://purl.uniprot.org/annotation/VSP_035691|||http://purl.uniprot.org/annotation/VSP_035692|||http://purl.uniprot.org/annotation/VSP_035693|||http://purl.uniprot.org/annotation/VSP_035694
http://togogenome.org/gene/9606:FKBP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1M5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FK506-binding protein 15|||Important for function in growth cone organization|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||PPIase FKBP-type|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299556|||http://purl.uniprot.org/annotation/VAR_034851|||http://purl.uniprot.org/annotation/VAR_034852|||http://purl.uniprot.org/annotation/VAR_034853|||http://purl.uniprot.org/annotation/VAR_061543|||http://purl.uniprot.org/annotation/VAR_061544|||http://purl.uniprot.org/annotation/VSP_027756|||http://purl.uniprot.org/annotation/VSP_027757|||http://purl.uniprot.org/annotation/VSP_027758
http://togogenome.org/gene/9606:APLP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE9|||http://purl.uniprot.org/uniprot/B4E3I5|||http://purl.uniprot.org/uniprot/Q06481                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Amyloid beta precursor like protein 2|||BPTI/Kunitz inhibitor|||Basic and acidic residues|||CuBD subdomain|||Cytoplasmic|||Disordered|||E1|||E2|||Extracellular|||GFLD subdomain|||Helical|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with DAB2|||NPXY motif|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine; by FAM20C|||Reactive bond|||Required for Cu(2+) reduction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000207|||http://purl.uniprot.org/annotation/PRO_5002801149|||http://purl.uniprot.org/annotation/PRO_5007491780|||http://purl.uniprot.org/annotation/VAR_022039|||http://purl.uniprot.org/annotation/VSP_000018|||http://purl.uniprot.org/annotation/VSP_000019|||http://purl.uniprot.org/annotation/VSP_030921|||http://purl.uniprot.org/annotation/VSP_046881|||http://purl.uniprot.org/annotation/VSP_046882
http://togogenome.org/gene/9606:SLC13A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QL78|||http://purl.uniprot.org/uniprot/Q13183                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||Solute carrier family 13 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000172488|||http://purl.uniprot.org/annotation/VAR_020399|||http://purl.uniprot.org/annotation/VAR_020400|||http://purl.uniprot.org/annotation/VAR_029254|||http://purl.uniprot.org/annotation/VAR_029255|||http://purl.uniprot.org/annotation/VAR_029256|||http://purl.uniprot.org/annotation/VAR_029257|||http://purl.uniprot.org/annotation/VAR_052000|||http://purl.uniprot.org/annotation/VSP_046426|||http://purl.uniprot.org/annotation/VSP_046427
http://togogenome.org/gene/9606:CCDC40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0X9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 40|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305250|||http://purl.uniprot.org/annotation/VAR_035193|||http://purl.uniprot.org/annotation/VSP_028302|||http://purl.uniprot.org/annotation/VSP_028303|||http://purl.uniprot.org/annotation/VSP_028304|||http://purl.uniprot.org/annotation/VSP_028305|||http://purl.uniprot.org/annotation/VSP_028306|||http://purl.uniprot.org/annotation/VSP_028307|||http://purl.uniprot.org/annotation/VSP_028308|||http://purl.uniprot.org/annotation/VSP_028309
http://togogenome.org/gene/9606:TEX46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BTG2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Testis-expressed protein 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423414|||http://purl.uniprot.org/annotation/VSP_047833|||http://purl.uniprot.org/annotation/VSP_047834
http://togogenome.org/gene/9606:DDOST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39656                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit|||Helical|||In CDG1R.|||In isoform 2.|||In isoform 3.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021957|||http://purl.uniprot.org/annotation/VAR_047911|||http://purl.uniprot.org/annotation/VAR_067544|||http://purl.uniprot.org/annotation/VSP_055498|||http://purl.uniprot.org/annotation/VSP_055499
http://togogenome.org/gene/9606:IL31RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNJ2|||http://purl.uniprot.org/uniprot/Q8NI17                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abrogates STAT3 activation. Loss of interaction with STAT3. Mild effect on STAT1 activation. No effect on STAT5 activation.|||Abrogates STAT5 activation. Mild effect on STAT1 activation. No effect on STAT3 activation.|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||In PLCA2.|||In isoform 10.|||In isoform 11.|||In isoform 2, isoform 4, isoform 5 and isoform 8.|||In isoform 3 and isoform 5.|||In isoform 3, isoform 7, isoform 9, isoform 10, isoform 11 and isoform 12.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interleukin-31 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-670.|||No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-708.|||No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-670 and A-708.|||No effect on STAT3 and STAT5 activation. Mild effect on STAT1 activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274572|||http://purl.uniprot.org/annotation/VAR_030328|||http://purl.uniprot.org/annotation/VAR_030329|||http://purl.uniprot.org/annotation/VAR_065809|||http://purl.uniprot.org/annotation/VSP_022798|||http://purl.uniprot.org/annotation/VSP_022799|||http://purl.uniprot.org/annotation/VSP_022800|||http://purl.uniprot.org/annotation/VSP_022801|||http://purl.uniprot.org/annotation/VSP_022802|||http://purl.uniprot.org/annotation/VSP_022803|||http://purl.uniprot.org/annotation/VSP_022804|||http://purl.uniprot.org/annotation/VSP_022805|||http://purl.uniprot.org/annotation/VSP_022806|||http://purl.uniprot.org/annotation/VSP_022807|||http://purl.uniprot.org/annotation/VSP_022808|||http://purl.uniprot.org/annotation/VSP_022809|||http://purl.uniprot.org/annotation/VSP_022810|||http://purl.uniprot.org/annotation/VSP_022811|||http://purl.uniprot.org/annotation/VSP_022812|||http://purl.uniprot.org/annotation/VSP_022813
http://togogenome.org/gene/9606:EGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11161                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||E3 SUMO-protein ligase EGR2|||HCFC1-binding-motif (HBM)|||In CHN1.|||In CHN1; loss of large and small myelinated nerve fibers.|||In CMT1D.|||In CMT1D; loss of myelinated and unmyelinated nerve fibers.|||In CMT1D; unknown pathological significance.|||In DSS and CMT1D; associated with A-136 in the GJB1 gene in a DSSKorean girl; loss of DNA binding and loss of transactivation activity; loss of small and large myelinated nerve fibers; residual fibers with thin myelin sheaths.|||In DSS.|||In DSS; loss of DNA binding and loss of transactivation activity.|||In isoform Short.|||Inhibits association with HCFC1.|||N6-acetyllysine; by EP300|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047119|||http://purl.uniprot.org/annotation/VAR_007735|||http://purl.uniprot.org/annotation/VAR_007736|||http://purl.uniprot.org/annotation/VAR_007737|||http://purl.uniprot.org/annotation/VAR_007738|||http://purl.uniprot.org/annotation/VAR_009874|||http://purl.uniprot.org/annotation/VAR_009875|||http://purl.uniprot.org/annotation/VAR_029958|||http://purl.uniprot.org/annotation/VAR_029959|||http://purl.uniprot.org/annotation/VAR_083343|||http://purl.uniprot.org/annotation/VAR_083344|||http://purl.uniprot.org/annotation/VAR_083345|||http://purl.uniprot.org/annotation/VAR_083346|||http://purl.uniprot.org/annotation/VSP_006863
http://togogenome.org/gene/9606:ZFP57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8V5|||http://purl.uniprot.org/uniprot/B7ZW61|||http://purl.uniprot.org/uniprot/Q9NU63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||Crucial for 5-methylcytosine recognition|||Disordered|||In TNDM1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 57 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291964|||http://purl.uniprot.org/annotation/VAR_032902|||http://purl.uniprot.org/annotation/VAR_032903|||http://purl.uniprot.org/annotation/VAR_054771|||http://purl.uniprot.org/annotation/VAR_054772|||http://purl.uniprot.org/annotation/VAR_054773|||http://purl.uniprot.org/annotation/VSP_026329|||http://purl.uniprot.org/annotation/VSP_026330|||http://purl.uniprot.org/annotation/VSP_036659
http://togogenome.org/gene/9606:BTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62324|||http://purl.uniprot.org/uniprot/Q6IBC8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Anti-proliferative protein|||Phosphoserine|||Protein BTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143800|||http://purl.uniprot.org/annotation/VAR_021345|||http://purl.uniprot.org/annotation/VAR_021346
http://togogenome.org/gene/9606:SQLE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14534|||http://purl.uniprot.org/uniprot/Q5HYI4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes degradation in response to high membrane cholesterol levels.|||Cytoplasmic|||Helical|||Hydrophobic; mediates interaction with membranes|||Important for enzyme activity|||Increased expression levels and decreased degradation in response to high membrane cholesterol levels; when associated with A-35; A-37 and A-65.|||Increased expression levels and decreased degradation in response to high membrane cholesterol levels; when associated with A-35; A-37 and A-69.|||Increased expression levels and decreased degradation in response to high membrane cholesterol levels; when associated with A-35; A-65 and A-69.|||Increased expression levels and decreased degradation in response to high membrane cholesterol levels; when associated with A-37; A-65 and A-69.|||Interaction with MARCHF6|||Loss of enzyme activity.|||Required for degradation in response to high membrane cholesterol levels|||Squalene epoxidase|||Squalene monooxygenase|||Sufficient for enzyme activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209838
http://togogenome.org/gene/9606:HOXD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31249                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-D3|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200204|||http://purl.uniprot.org/annotation/VAR_011881
http://togogenome.org/gene/9606:ISLR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Immunoglobulin superfamily containing leucine-rich repeat protein 2|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317498|||http://purl.uniprot.org/annotation/VAR_049881
http://togogenome.org/gene/9606:KRTAP4-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||25 X 5 AA repeats of C-C-[IKRQVHEC]-[SPRT]-[STCVQPR]|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 4-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185175
http://togogenome.org/gene/9606:KCNIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2W7                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes cleavage by caspase-3.|||Calsenilin|||Disordered|||EF-hand 1; degenerate|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with KCND2|||Phosphoserine|||Phosphoserine; by CK1|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073814|||http://purl.uniprot.org/annotation/VAR_035463|||http://purl.uniprot.org/annotation/VAR_035464|||http://purl.uniprot.org/annotation/VAR_048663|||http://purl.uniprot.org/annotation/VSP_015040|||http://purl.uniprot.org/annotation/VSP_040982|||http://purl.uniprot.org/annotation/VSP_040983
http://togogenome.org/gene/9606:KTI12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EK9                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Protein KTI12 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285686|||http://purl.uniprot.org/annotation/VAR_032046
http://togogenome.org/gene/9606:LCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31025                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Lipocalin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017974
http://togogenome.org/gene/9606:FKBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26885|||http://purl.uniprot.org/uniprot/Q53XJ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP2|||Prevents secretion from ER|||peptidylprolyl isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025506|||http://purl.uniprot.org/annotation/PRO_5014309559|||http://purl.uniprot.org/annotation/VAR_006410|||http://purl.uniprot.org/annotation/VAR_006411|||http://purl.uniprot.org/annotation/VAR_006412|||http://purl.uniprot.org/annotation/VAR_050623
http://togogenome.org/gene/9606:PRELID3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N28                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Site|||Splice Variant                                                                                  ^@                                                                                  Impairs interaction with TRIAP1.|||Important for interaction with TRIAP1|||In isoform 2.|||PRELI domain containing protein 3A|||PRELI/MSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295215|||http://purl.uniprot.org/annotation/VSP_056666
http://togogenome.org/gene/9606:AKT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG79|||http://purl.uniprot.org/uniprot/P31751                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Constitutively active; when associated with D-474.|||Constitutively active; when associated with E-309.|||Impairs interaction with TTC3; when associated with A-309.|||Impairs interaction with TTC3; when associated with A-474.|||In HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes.|||In T2D; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject.|||In isoform 2.|||N-acetylmethionine|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||RAC-beta serine/threonine-protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085608|||http://purl.uniprot.org/annotation/VAR_040356|||http://purl.uniprot.org/annotation/VAR_040357|||http://purl.uniprot.org/annotation/VAR_067309|||http://purl.uniprot.org/annotation/VAR_067310|||http://purl.uniprot.org/annotation/VSP_056930
http://togogenome.org/gene/9606:SERPINB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RC45|||http://purl.uniprot.org/uniprot/P48595                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes nuclear localization.|||No effect on cell proliferation.|||Nuclear localization signal|||Reactive bond|||Redox-active|||Serpin|||Serpin B10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094114|||http://purl.uniprot.org/annotation/VAR_022116|||http://purl.uniprot.org/annotation/VAR_024353|||http://purl.uniprot.org/annotation/VAR_024354|||http://purl.uniprot.org/annotation/VAR_024355|||http://purl.uniprot.org/annotation/VAR_051949|||http://purl.uniprot.org/annotation/VAR_051950|||http://purl.uniprot.org/annotation/VAR_051951
http://togogenome.org/gene/9606:UBE2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SG71|||http://purl.uniprot.org/uniprot/P49459                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||In MRXSN.|||In isoform 2.|||In isoform 3.|||Phosphoserine; by CDK9|||UBC core|||Ubiquitin-conjugating enzyme E2 A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082445|||http://purl.uniprot.org/annotation/VAR_066627|||http://purl.uniprot.org/annotation/VAR_066628|||http://purl.uniprot.org/annotation/VSP_043851|||http://purl.uniprot.org/annotation/VSP_043852
http://togogenome.org/gene/9606:PCTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L2M9|||http://purl.uniprot.org/uniprot/I3L3H0|||http://purl.uniprot.org/uniprot/Q549N3|||http://purl.uniprot.org/uniprot/Q9UKL6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||Phosphatidylcholine transfer protein|||Phosphoserine|||Reduces activity by 20%.|||START                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220658|||http://purl.uniprot.org/annotation/VAR_052070|||http://purl.uniprot.org/annotation/VSP_041363
http://togogenome.org/gene/9606:FNDC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVV2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  Fibronectin type III domain-containing protein 11|||Fibronectin type-III                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232867
http://togogenome.org/gene/9606:CHCHD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUK0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Splice Variant|||Turn                                                                                  ^@                                                                                  CHCH|||Coiled-coil-helix-coiled-coil-helix domain-containing protein 7|||Cx9C motif 1|||Cx9C motif 2|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129171|||http://purl.uniprot.org/annotation/VSP_038076|||http://purl.uniprot.org/annotation/VSP_038077|||http://purl.uniprot.org/annotation/VSP_046698
http://togogenome.org/gene/9606:VANGL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In NTD; does not abolish ability to interact with DVL1, DVL2 and DVL3.|||In NTD; unknown pathological significance.|||In SDAM; abolishes ability to interact with DVL1, DVL2 and DVL3.|||In isoform 2.|||Phosphoserine|||Polar residues|||Vang-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186193|||http://purl.uniprot.org/annotation/VAR_027143|||http://purl.uniprot.org/annotation/VAR_035209|||http://purl.uniprot.org/annotation/VAR_035210|||http://purl.uniprot.org/annotation/VAR_035211|||http://purl.uniprot.org/annotation/VAR_035435|||http://purl.uniprot.org/annotation/VAR_062321|||http://purl.uniprot.org/annotation/VAR_062322|||http://purl.uniprot.org/annotation/VAR_062323|||http://purl.uniprot.org/annotation/VAR_062324|||http://purl.uniprot.org/annotation/VAR_062325|||http://purl.uniprot.org/annotation/VAR_062326|||http://purl.uniprot.org/annotation/VAR_062327|||http://purl.uniprot.org/annotation/VAR_062328|||http://purl.uniprot.org/annotation/VAR_062329|||http://purl.uniprot.org/annotation/VAR_062330|||http://purl.uniprot.org/annotation/VSP_008742
http://togogenome.org/gene/9606:RPP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Pro residues|||Ribonuclease P protein subunit p25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237582
http://togogenome.org/gene/9606:DEFB123                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N688                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Beta-defensin 123|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006994|||http://purl.uniprot.org/annotation/VSP_057460|||http://purl.uniprot.org/annotation/VSP_057461
http://togogenome.org/gene/9606:RESP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W5W9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 1.|||In isoform 3.|||Regulated endocrine-specific protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336992|||http://purl.uniprot.org/annotation/VSP_059544|||http://purl.uniprot.org/annotation/VSP_059545|||http://purl.uniprot.org/annotation/VSP_059546|||http://purl.uniprot.org/annotation/VSP_059547|||http://purl.uniprot.org/annotation/VSP_059548|||http://purl.uniprot.org/annotation/VSP_059549
http://togogenome.org/gene/9606:MRM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC36                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||rRNA methyltransferase 3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311301|||http://purl.uniprot.org/annotation/VAR_037217|||http://purl.uniprot.org/annotation/VAR_037218|||http://purl.uniprot.org/annotation/VAR_037219|||http://purl.uniprot.org/annotation/VAR_037220
http://togogenome.org/gene/9606:TRIM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F44                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity.|||B box-type|||B30.2/SPRY|||Does not affect autoubiquitination.|||E3 ubiquitin-protein ligase TRIM11|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||RING-type|||Reduced autoubiquitination, leading to abolish interaction with SQSTM1/p62.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056215|||http://purl.uniprot.org/annotation/VSP_012057|||http://purl.uniprot.org/annotation/VSP_012058|||http://purl.uniprot.org/annotation/VSP_039628
http://togogenome.org/gene/9606:GRM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4F9|||http://purl.uniprot.org/uniprot/A8K0J8|||http://purl.uniprot.org/uniprot/B7ZLU9|||http://purl.uniprot.org/uniprot/Q14833                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Metabotropic glutamate receptor 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012930|||http://purl.uniprot.org/annotation/PRO_5014296769|||http://purl.uniprot.org/annotation/PRO_5014568448|||http://purl.uniprot.org/annotation/VAR_012992|||http://purl.uniprot.org/annotation/VAR_049275|||http://purl.uniprot.org/annotation/VSP_044740|||http://purl.uniprot.org/annotation/VSP_044741|||http://purl.uniprot.org/annotation/VSP_045218|||http://purl.uniprot.org/annotation/VSP_046761|||http://purl.uniprot.org/annotation/VSP_046762|||http://purl.uniprot.org/annotation/VSP_046763
http://togogenome.org/gene/9606:CXorf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLS7|||http://purl.uniprot.org/uniprot/Q96LI9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein CXorf58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271066|||http://purl.uniprot.org/annotation/VAR_029857|||http://purl.uniprot.org/annotation/VAR_029858
http://togogenome.org/gene/9606:NUTM2G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NUT family member 2G|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266034|||http://purl.uniprot.org/annotation/VSP_034023|||http://purl.uniprot.org/annotation/VSP_034024
http://togogenome.org/gene/9606:CHRNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6F7YAP6|||http://purl.uniprot.org/uniprot/P07510                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetylcholine receptor subunit gamma|||Cytoplasmic|||Extracellular|||Helical|||In EVMPS and LMPS.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000334|||http://purl.uniprot.org/annotation/PRO_5026378716|||http://purl.uniprot.org/annotation/VAR_030753|||http://purl.uniprot.org/annotation/VAR_030754|||http://purl.uniprot.org/annotation/VAR_030755|||http://purl.uniprot.org/annotation/VSP_055775
http://togogenome.org/gene/9606:OR1Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15612                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150450|||http://purl.uniprot.org/annotation/VAR_024768|||http://purl.uniprot.org/annotation/VAR_053126|||http://purl.uniprot.org/annotation/VAR_053127
http://togogenome.org/gene/9606:PRDM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||Disordered|||In PDA3.|||In PDA3; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||Polar residues|||Pro residues|||Putative histone-lysine N-methyltransferase PRDM6|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047762|||http://purl.uniprot.org/annotation/VAR_077014|||http://purl.uniprot.org/annotation/VAR_077015|||http://purl.uniprot.org/annotation/VAR_077016|||http://purl.uniprot.org/annotation/VSP_006929|||http://purl.uniprot.org/annotation/VSP_036348
http://togogenome.org/gene/9606:MTUS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JR59                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Localization to the growing distal tip of microtubules|||Mediates interaction with MAPRE1|||Microtubule-associated tumor suppressor candidate 2|||Polar residues|||Sufficient for interaction with KIF2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280111|||http://purl.uniprot.org/annotation/VAR_055941|||http://purl.uniprot.org/annotation/VAR_058831|||http://purl.uniprot.org/annotation/VSP_023540|||http://purl.uniprot.org/annotation/VSP_023541|||http://purl.uniprot.org/annotation/VSP_023543
http://togogenome.org/gene/9606:VPS18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P253                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CHCR|||Disordered|||In a colorectal cancer sample; somatic mutation.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||RING-type|||Removed|||Vacuolar protein sorting-associated protein 18 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055906|||http://purl.uniprot.org/annotation/VAR_035950
http://togogenome.org/gene/9606:ASCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR60|||http://purl.uniprot.org/uniprot/Q8N3C0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes 3'-5' DNA helicase activity and ability to promote DNA repair.|||Activating signal cointegrator 1 complex subunit 3|||DEIH box|||DEVH box|||Defective activation of the ribosome quality control (RQC) pathway. Impairs its association with ribosomes.|||Helicase ATP-binding|||Helicase ATP-binding 1|||Helicase ATP-binding 2|||Helicase C-terminal|||Helicase C-terminal 1|||Helicase C-terminal 2|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Required for interaction with ASCC2|||SEC63 1|||SEC63 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102093|||http://purl.uniprot.org/annotation/VAR_034859|||http://purl.uniprot.org/annotation/VAR_034860|||http://purl.uniprot.org/annotation/VAR_034861|||http://purl.uniprot.org/annotation/VAR_034862|||http://purl.uniprot.org/annotation/VAR_034863|||http://purl.uniprot.org/annotation/VAR_034864|||http://purl.uniprot.org/annotation/VAR_049339|||http://purl.uniprot.org/annotation/VAR_049340|||http://purl.uniprot.org/annotation/VAR_049341|||http://purl.uniprot.org/annotation/VAR_049342|||http://purl.uniprot.org/annotation/VAR_061212|||http://purl.uniprot.org/annotation/VSP_042955|||http://purl.uniprot.org/annotation/VSP_042956|||http://purl.uniprot.org/annotation/VSP_042957|||http://purl.uniprot.org/annotation/VSP_042958
http://togogenome.org/gene/9606:CDH26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXH8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin-like protein 26|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 1.|||In isoform 2 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003829|||http://purl.uniprot.org/annotation/VAR_055568|||http://purl.uniprot.org/annotation/VAR_055569|||http://purl.uniprot.org/annotation/VAR_055570|||http://purl.uniprot.org/annotation/VAR_055571|||http://purl.uniprot.org/annotation/VAR_055572|||http://purl.uniprot.org/annotation/VSP_008333|||http://purl.uniprot.org/annotation/VSP_008334|||http://purl.uniprot.org/annotation/VSP_059693|||http://purl.uniprot.org/annotation/VSP_059694
http://togogenome.org/gene/9606:MMACHC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGU2|||http://purl.uniprot.org/uniprot/Q9Y4U1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyanocobalamin reductase / alkylcobalamin dealkylase|||Disordered|||Impairs protein folding.|||In MAHCC.|||In MAHCC; loss of cyanocobalamin binding.|||In MAHCC; results in decreased stability and decreased methylcobalamin dealkylation activity.|||In MAHCC; results in decreased stability and reduced stabilization induced by cobalamin binding; has reduced affinity for cyanocobalamin and reduced activity in dealkylation of methylcobalamin.|||Phosphoserine|||Pro residues|||Reduced activity in dealkylation of methylcobalamin.|||Reduced affinity for cyanocobalamin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076258|||http://purl.uniprot.org/annotation/VAR_024770|||http://purl.uniprot.org/annotation/VAR_024771|||http://purl.uniprot.org/annotation/VAR_024772|||http://purl.uniprot.org/annotation/VAR_024773|||http://purl.uniprot.org/annotation/VAR_024774|||http://purl.uniprot.org/annotation/VAR_024775|||http://purl.uniprot.org/annotation/VAR_024776|||http://purl.uniprot.org/annotation/VAR_024777|||http://purl.uniprot.org/annotation/VAR_024778|||http://purl.uniprot.org/annotation/VAR_024779|||http://purl.uniprot.org/annotation/VAR_024780|||http://purl.uniprot.org/annotation/VAR_024781|||http://purl.uniprot.org/annotation/VAR_024782|||http://purl.uniprot.org/annotation/VAR_024783|||http://purl.uniprot.org/annotation/VAR_038805
http://togogenome.org/gene/9606:TAAR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969N4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070174|||http://purl.uniprot.org/annotation/VAR_049447|||http://purl.uniprot.org/annotation/VAR_049448|||http://purl.uniprot.org/annotation/VAR_066638
http://togogenome.org/gene/9606:SMN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP61|||http://purl.uniprot.org/uniprot/E7EQZ4|||http://purl.uniprot.org/uniprot/Q16637                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs GEMIN2 binding.|||Impairs GEMIN8 binding.|||Impairs SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4. Abolishes interaction with SNRPD1 and SNRPD3. Impairs binding to substrate containing dimethylated arginine.|||Impairs binding to substrate containing dimethylated arginine.|||Impairs homooligomerization and GEMIN8 binding.|||Impairs homooligomerization.|||In SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization.|||In SMA1; abolishes the interaction with ELAVL4.|||In SMA1; slightly reduces SMN binding to RPP20/POP7. Impairs homooligomerization and axon localization.|||In SMA2 and SMA3.|||In SMA2 and SMA3; Impairs SMN1 binding to RPP20/POP7, GEMIN8 and homooligomerization.|||In SMA2.|||In SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4.|||In SMA3.|||In SMA3; impairs GEMIN2 binding.|||In SMA3; impairs homooligomerization..|||In SMA3; reduces SMN binding to Sm proteins.|||In SMA3; slightly reduces SMN binding to RPP20/POP7.|||In isoform SMN-delta5 and isoform SMN-delta57.|||In isoform SMN-delta7 and isoform SMN-delta57.|||Interacts with GEMIN2|||Involved in homooligomerization|||N-acetylalanine|||P2 (binding site for SNRPB)|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Polar residues|||Pro residues|||Removed|||Required for interaction with RPP20/POP7|||Required for interaction with SYNCRIP|||Survival motor neuron Tudor|||Survival motor neuron protein|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218903|||http://purl.uniprot.org/annotation/VAR_005615|||http://purl.uniprot.org/annotation/VAR_005616|||http://purl.uniprot.org/annotation/VAR_005617|||http://purl.uniprot.org/annotation/VAR_005618|||http://purl.uniprot.org/annotation/VAR_005619|||http://purl.uniprot.org/annotation/VAR_005620|||http://purl.uniprot.org/annotation/VAR_007990|||http://purl.uniprot.org/annotation/VAR_010051|||http://purl.uniprot.org/annotation/VAR_034803|||http://purl.uniprot.org/annotation/VAR_034804|||http://purl.uniprot.org/annotation/VAR_034805|||http://purl.uniprot.org/annotation/VAR_034806|||http://purl.uniprot.org/annotation/VAR_034807|||http://purl.uniprot.org/annotation/VAR_034808|||http://purl.uniprot.org/annotation/VAR_034809|||http://purl.uniprot.org/annotation/VSP_006183|||http://purl.uniprot.org/annotation/VSP_006184|||http://purl.uniprot.org/annotation/VSP_006185
http://togogenome.org/gene/9606:JHY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUM2|||http://purl.uniprot.org/uniprot/Q6NUN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Jhy protein homolog|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280764|||http://purl.uniprot.org/annotation/VAR_050863|||http://purl.uniprot.org/annotation/VSP_023915|||http://purl.uniprot.org/annotation/VSP_023916
http://togogenome.org/gene/9606:CA5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35218                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 5A, mitochondrial|||In CA5AD; decreased carbonate dehydratase activity; decreased protein thermal stability.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004234|||http://purl.uniprot.org/annotation/VAR_071188
http://togogenome.org/gene/9606:MAD1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6D9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to closed and open conformations of MAD2L1 and impairs mitotic checkpint signaling abolishing mitotic arrest, and shortens the duration of mitosis; in association with A-543.|||Abolishes binding to closed and open conformations of MAD2L1 and impairs mitotic checkpoint signaling abolishing mitotic arrest, and shortens the duration of mitosis; in association with A-541.|||Defective dimerization. Abolishes binding to the closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest, and shortens the duration of mitosis.|||Defective dimerization. Reduces binding to the closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest, and shortens the duration of mitosis.|||Does not impact the duration of mitosis.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs mitotic checkpoint signaling and shortens the duration of mitosis.|||Important for interaction with IK|||In MVA7; decreased protein abundance in cells from the patient and from his heterozygous parents.|||In a breast cancer cell line; somatic mutation.|||In a cancer cell line.|||In a lymphoid cancer cell line; somatic mutation.|||In a prostate cancer cell line; somatic mutation.|||In isoform 2.|||In isoform 3.|||In lung cancer cell line; somatic mutation.|||In one individual with lung cancer.|||Loss of interaction with MAD2L1.|||Loss of nuclear localization.|||Mitotic spindle assembly checkpoint protein MAD1|||N-acetylmethionine|||N6-acetyllysine; alternate|||Necessary for interaction with MAD2L1|||Necessary for interaction with NEK2|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Reduces binding to closed and open conformations of MAD2L1. Does not impact the duration of mitosis.|||Reduces binding to closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest, and shortens the duration of mitosis.|||Reduces binding to closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling and shortens the duration of mitosis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213800|||http://purl.uniprot.org/annotation/VAR_019707|||http://purl.uniprot.org/annotation/VAR_019708|||http://purl.uniprot.org/annotation/VAR_019709|||http://purl.uniprot.org/annotation/VAR_019710|||http://purl.uniprot.org/annotation/VAR_019711|||http://purl.uniprot.org/annotation/VAR_019712|||http://purl.uniprot.org/annotation/VAR_019713|||http://purl.uniprot.org/annotation/VAR_019714|||http://purl.uniprot.org/annotation/VAR_019715|||http://purl.uniprot.org/annotation/VAR_019716|||http://purl.uniprot.org/annotation/VAR_019717|||http://purl.uniprot.org/annotation/VAR_019718|||http://purl.uniprot.org/annotation/VAR_019719|||http://purl.uniprot.org/annotation/VAR_087991|||http://purl.uniprot.org/annotation/VAR_087992|||http://purl.uniprot.org/annotation/VSP_056160|||http://purl.uniprot.org/annotation/VSP_056161|||http://purl.uniprot.org/annotation/VSP_061075
http://togogenome.org/gene/9606:RGPD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99666|||http://purl.uniprot.org/uniprot/V9HWE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RANBP2-like and GRIP domain-containing protein 5/6|||RanBD1|||RanBD1 1|||RanBD1 2|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204915|||http://purl.uniprot.org/annotation/VSP_038968|||http://purl.uniprot.org/annotation/VSP_038969
http://togogenome.org/gene/9606:ARAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2A5|||http://purl.uniprot.org/uniprot/Q8WZ64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2|||Basic and acidic residues|||C4-type|||Disordered|||PH|||PH 1|||PH 2|||PH 3|||PH 4|||PH 5|||Phosphoserine|||Phosphotyrosine|||Ras-associating|||Rho-GAP|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074212|||http://purl.uniprot.org/annotation/VAR_027952|||http://purl.uniprot.org/annotation/VAR_055530|||http://purl.uniprot.org/annotation/VAR_055531
http://togogenome.org/gene/9606:MRPL24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A35                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  KOW|||Large ribosomal subunit protein uL24m|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270488
http://togogenome.org/gene/9606:SRRM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS81|||http://purl.uniprot.org/uniprot/Q4G0Z0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Serine/arginine repetitive matrix protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395306
http://togogenome.org/gene/9606:PSPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXF1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-198.|||Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-200.|||Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-198 and A-200.|||Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-121; A-198 and A-200.|||Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-275.|||Abolishes interaction with NONO and localization in nuclear paraspeckles; when associated with A-279.|||Disordered|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Paraspeckle component 1|||Phosphoserine|||Polar residues|||RRM 1|||RRM 2|||Sufficient for paraspeckles localization|||Sufficient for perinucleolar caps localization and interaction with NONO                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297540|||http://purl.uniprot.org/annotation/VSP_027274|||http://purl.uniprot.org/annotation/VSP_027275
http://togogenome.org/gene/9606:KIFAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92845                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kinesin-associated protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084302|||http://purl.uniprot.org/annotation/VAR_051081|||http://purl.uniprot.org/annotation/VSP_044505|||http://purl.uniprot.org/annotation/VSP_047132|||http://purl.uniprot.org/annotation/VSP_047133
http://togogenome.org/gene/9606:KRTAP29-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MX34                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 29-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348961
http://togogenome.org/gene/9606:FDFT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQ47|||http://purl.uniprot.org/uniprot/P37268                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Influences plasma cholesterol levels; associated with increased total cholesterol and non-high-density lipoprotein cholesterol.|||Squalene synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067443|||http://purl.uniprot.org/annotation/VAR_011786|||http://purl.uniprot.org/annotation/VAR_011787|||http://purl.uniprot.org/annotation/VSP_056282|||http://purl.uniprot.org/annotation/VSP_056283|||http://purl.uniprot.org/annotation/VSP_056517|||http://purl.uniprot.org/annotation/VSP_056518
http://togogenome.org/gene/9606:KRT79                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XKE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 79|||Linker 1|||Linker 12|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314893|||http://purl.uniprot.org/annotation/VAR_038113|||http://purl.uniprot.org/annotation/VAR_038114|||http://purl.uniprot.org/annotation/VAR_038115|||http://purl.uniprot.org/annotation/VAR_038116
http://togogenome.org/gene/9606:PMPCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXH0|||http://purl.uniprot.org/uniprot/A0A9L9PXI7|||http://purl.uniprot.org/uniprot/B3KM34|||http://purl.uniprot.org/uniprot/O75439|||http://purl.uniprot.org/uniprot/Q96CP5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  In MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast.|||In MMDS6; small decrease in protein level; impaired frataxin/FXN processing, leading to the accumulation of an intermediate form, called iFXN.|||Mitochondrial-processing peptidase subunit beta|||Mitochondrion|||Peptidase M16 C-terminal|||Peptidase M16 N-terminal|||Proton acceptor|||Required for the specific determination of the substrate cleavage site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026777|||http://purl.uniprot.org/annotation/VAR_051572|||http://purl.uniprot.org/annotation/VAR_080804|||http://purl.uniprot.org/annotation/VAR_080805|||http://purl.uniprot.org/annotation/VAR_080806|||http://purl.uniprot.org/annotation/VAR_080807|||http://purl.uniprot.org/annotation/VAR_080808
http://togogenome.org/gene/9606:APMAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HDC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adipocyte plasma membrane-associated protein|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-acetylserine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205945|||http://purl.uniprot.org/annotation/VAR_014128|||http://purl.uniprot.org/annotation/VAR_055039|||http://purl.uniprot.org/annotation/VAR_055040|||http://purl.uniprot.org/annotation/VSP_036992|||http://purl.uniprot.org/annotation/VSP_036993
http://togogenome.org/gene/9606:RPL21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46778|||http://purl.uniprot.org/uniprot/Q6IAX2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In HYPT12; autosomal dominant.|||Large ribosomal subunit protein eL21|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149669|||http://purl.uniprot.org/annotation/VAR_034459|||http://purl.uniprot.org/annotation/VAR_066030
http://togogenome.org/gene/9606:OR4K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP5|||http://purl.uniprot.org/uniprot/Q8NGD2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150553|||http://purl.uniprot.org/annotation/VAR_053171
http://togogenome.org/gene/9606:ADAMTS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2N4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 9|||Cleavage|||Cysteine switch|||Disintegrin|||Disordered|||GON|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No effect on mature form production.|||No mature form produced.|||Peptidase M12B|||Polar residues|||Spacer|||TSP type-1 1|||TSP type-1 10|||TSP type-1 11|||TSP type-1 12|||TSP type-1 13|||TSP type-1 14|||TSP type-1 15|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029182|||http://purl.uniprot.org/annotation/PRO_0000029183|||http://purl.uniprot.org/annotation/VAR_047081|||http://purl.uniprot.org/annotation/VAR_047082|||http://purl.uniprot.org/annotation/VAR_047083|||http://purl.uniprot.org/annotation/VAR_047084|||http://purl.uniprot.org/annotation/VAR_047085|||http://purl.uniprot.org/annotation/VAR_047086|||http://purl.uniprot.org/annotation/VAR_051592|||http://purl.uniprot.org/annotation/VAR_051593|||http://purl.uniprot.org/annotation/VSP_005499|||http://purl.uniprot.org/annotation/VSP_005500|||http://purl.uniprot.org/annotation/VSP_007548|||http://purl.uniprot.org/annotation/VSP_007549|||http://purl.uniprot.org/annotation/VSP_053399
http://togogenome.org/gene/9606:CYP2A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W816|||http://purl.uniprot.org/uniprot/P20853                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cytochrome P450 2A7|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051669|||http://purl.uniprot.org/annotation/PRO_5003385517|||http://purl.uniprot.org/annotation/VAR_047815|||http://purl.uniprot.org/annotation/VAR_047816|||http://purl.uniprot.org/annotation/VAR_047817|||http://purl.uniprot.org/annotation/VAR_047818|||http://purl.uniprot.org/annotation/VAR_047819|||http://purl.uniprot.org/annotation/VAR_047820|||http://purl.uniprot.org/annotation/VAR_061043|||http://purl.uniprot.org/annotation/VAR_061044
http://togogenome.org/gene/9606:CTDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5B0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||BRCT|||Basic and acidic residues|||Disordered|||FCP1 homology|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RNA polymerase II subunit A C-terminal domain phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212564|||http://purl.uniprot.org/annotation/VAR_018264|||http://purl.uniprot.org/annotation/VAR_032763|||http://purl.uniprot.org/annotation/VAR_060440|||http://purl.uniprot.org/annotation/VAR_060441|||http://purl.uniprot.org/annotation/VSP_009865
http://togogenome.org/gene/9606:NME3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13232                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Nucleoside diphosphate kinase 3|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137123
http://togogenome.org/gene/9606:TTC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8G6|||http://purl.uniprot.org/uniprot/J3KR69|||http://purl.uniprot.org/uniprot/Q53G14|||http://purl.uniprot.org/uniprot/Q9H892                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In CILD45; reduced protein abundance; changed axonemal dynein complex assembly.|||In CILD45; reduced protein abundance; changed axonemal dynein complex assembly; loss of sperm axoneme assembly.|||In isoform 2.|||Phosphothreonine|||TPR|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106395|||http://purl.uniprot.org/annotation/VAR_031431|||http://purl.uniprot.org/annotation/VAR_031432|||http://purl.uniprot.org/annotation/VAR_061903|||http://purl.uniprot.org/annotation/VAR_083923|||http://purl.uniprot.org/annotation/VAR_083924|||http://purl.uniprot.org/annotation/VAR_083925|||http://purl.uniprot.org/annotation/VSP_009119
http://togogenome.org/gene/9606:SIAE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAT2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  At homozygosity may predispose to autoimmunity; normal enzyme activity.|||Defective enzyme secretion and activity.|||In AIS6; defective enzyme secretion and activity.|||In isoform 2.|||May predispose to autoimmunity; defective enzyme secretion and activity.|||N-linked (GlcNAc...) asparagine|||Rare variant found in a patient with Crohn disease; probably not involved in disease susceptibility; the mutant enzyme has normal activity and is normally secreted.|||Rare variant found in a patient with Crohn disease; probably not involved in disease susceptibility; the mutant protein has normal activity.|||Rare variant found in a patient with rheumatoid arthritis; probably not involved in disease susceptibility; the mutant enzyme has normal activity and is normally secreted.|||Sialate O-acetylesterase|||The mutant enzyme has normal activity and is normally secreted.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042241|||http://purl.uniprot.org/annotation/VAR_051356|||http://purl.uniprot.org/annotation/VAR_051357|||http://purl.uniprot.org/annotation/VAR_064438|||http://purl.uniprot.org/annotation/VAR_064439|||http://purl.uniprot.org/annotation/VAR_064440|||http://purl.uniprot.org/annotation/VAR_064441|||http://purl.uniprot.org/annotation/VAR_064442|||http://purl.uniprot.org/annotation/VAR_064443|||http://purl.uniprot.org/annotation/VAR_064444|||http://purl.uniprot.org/annotation/VAR_064445|||http://purl.uniprot.org/annotation/VAR_064446|||http://purl.uniprot.org/annotation/VAR_064447|||http://purl.uniprot.org/annotation/VAR_064448|||http://purl.uniprot.org/annotation/VAR_064449|||http://purl.uniprot.org/annotation/VAR_064450|||http://purl.uniprot.org/annotation/VAR_064451|||http://purl.uniprot.org/annotation/VAR_064452|||http://purl.uniprot.org/annotation/VAR_064453|||http://purl.uniprot.org/annotation/VAR_064454|||http://purl.uniprot.org/annotation/VAR_064455|||http://purl.uniprot.org/annotation/VAR_064456|||http://purl.uniprot.org/annotation/VAR_064457|||http://purl.uniprot.org/annotation/VAR_064458|||http://purl.uniprot.org/annotation/VSP_018993
http://togogenome.org/gene/9606:SOX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57073                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  9aaTAD|||Basic and acidic residues|||Dimerization (DIM)|||Disordered|||HMG box|||Polar residues|||Transactivation domain (TAC)|||Transactivation domain (TAM)|||Transcription factor SOX-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048733
http://togogenome.org/gene/9606:SLC30A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEW0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||His-rich loop|||Lumenal|||Zinc transporter 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314299
http://togogenome.org/gene/9606:CDCA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXL8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Cell division cycle-associated protein 4|||SERTA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191617
http://togogenome.org/gene/9606:SSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16385|||http://purl.uniprot.org/uniprot/R9QTR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form the SSXT-SSX2 fusion protein|||Breakpoint for translocation to form the SSXT-SSX2 fusion protein (rare)|||Disordered|||In isoform 2.|||Interaction with RAB3IP|||Interaction with SSX2IP|||KRAB-related|||Phosphoserine|||Polar residues|||Protein SSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181829|||http://purl.uniprot.org/annotation/VSP_017595
http://togogenome.org/gene/9606:ZBTB33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates both sequence-specific and methylation-dependent DNA-binding.|||Acidic residues|||BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with CBFA2T3|||Interaction with CTNND1|||Interaction with NCOR1|||Nuclear localization signal|||Phosphothreonine|||Required for DNA-binding|||Self-association|||Transcriptional regulator Kaiso                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046988
http://togogenome.org/gene/9606:CACNG7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62955                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Voltage-dependent calcium channel gamma-7 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164687
http://togogenome.org/gene/9606:SPDYE2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Speedy protein E2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000399479|||http://purl.uniprot.org/annotation/VSP_039852
http://togogenome.org/gene/9606:PRR5-ARHGAP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AHC3                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  CRAL-TRIO|||Disordered|||Rho-GAP                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:BUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYG2|||http://purl.uniprot.org/uniprot/O43683                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BUB1 N-terminal|||Diminished interaction with PLK1.|||Disordered|||Essential for loading of BUBR1, MAD1L1 and MAD2L1 to kinetochores|||In colorectal cancer.|||In isoform 2.|||In isoform 3.|||In pancreatic cancer; associated with C-259; complete rescue of the spindle-assembly checkpoint activity; increased rate of chromosome congression errors.|||In pancreatic cancer; associated with N-265; failure to rescue the spindle-assembly checkpoint activity as a result of a deficient recruitment of MAD2L1 and BUBR1 to kinetochores; efficient restoration of chromosome congression; reduced binding to BUB3; rescue of the ability of kinetochores to bind SGO1 and CENPF but not MCAK.|||KEN box 1|||KEN box 2|||Loss of activity.|||Loss of interaction with KNL1.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-536.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-535 and A-537.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-536 and A-537.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-626.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-625 and A-627.|||Loss of ubiquitination and CDH1-dependent degradation; when associated with A-626 and A-627.|||Mitotic checkpoint serine/threonine-protein kinase BUB1|||Necessary for interaction with BUB3|||Necessary for interaction with KNL1|||Necessary for kinetochore localization|||Nuclear localization signal|||Partial rescue of the spindle-assembly checkpoint activity. Increased rate of chromosome congression errors. Impaired localization to kinetochores and loss of kinetochore binding of CENPF, SGO1 and BUBR1 but not of MCAK, MAD1L1 or MAD2L1.|||Phosphoserine|||Phosphothreonine; by CDK1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085671|||http://purl.uniprot.org/annotation/VAR_008849|||http://purl.uniprot.org/annotation/VAR_008850|||http://purl.uniprot.org/annotation/VAR_008851|||http://purl.uniprot.org/annotation/VAR_015687|||http://purl.uniprot.org/annotation/VAR_015688|||http://purl.uniprot.org/annotation/VAR_040400|||http://purl.uniprot.org/annotation/VAR_040401|||http://purl.uniprot.org/annotation/VSP_054760|||http://purl.uniprot.org/annotation/VSP_054761
http://togogenome.org/gene/9606:USP50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70EL3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Inactive ubiquitin carboxyl-terminal hydrolase 50|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249527|||http://purl.uniprot.org/annotation/VSP_054248
http://togogenome.org/gene/9606:LMNTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9Z9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||LTD|||Lamin tail domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317247|||http://purl.uniprot.org/annotation/VAR_049809|||http://purl.uniprot.org/annotation/VAR_049810|||http://purl.uniprot.org/annotation/VAR_049811|||http://purl.uniprot.org/annotation/VAR_049812|||http://purl.uniprot.org/annotation/VAR_049813|||http://purl.uniprot.org/annotation/VSP_030922|||http://purl.uniprot.org/annotation/VSP_040489|||http://purl.uniprot.org/annotation/VSP_040490|||http://purl.uniprot.org/annotation/VSP_040491|||http://purl.uniprot.org/annotation/VSP_040492
http://togogenome.org/gene/9606:SPINT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV6|||http://purl.uniprot.org/uniprot/O43291                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DIAR3; has a significantly reduced ability to inhibit trypsin compared to wild-type.|||In isoform 2.|||Kunitz-type protease inhibitor 2|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016885|||http://purl.uniprot.org/annotation/PRO_5007491743|||http://purl.uniprot.org/annotation/VAR_012482|||http://purl.uniprot.org/annotation/VAR_058718|||http://purl.uniprot.org/annotation/VSP_043680
http://togogenome.org/gene/9606:PRSS36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNP1|||http://purl.uniprot.org/uniprot/Q5K4E3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Peptidase S1 1|||Peptidase S1 2|||Peptidase S1 3|||Polyserase-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027879|||http://purl.uniprot.org/annotation/PRO_0000027880|||http://purl.uniprot.org/annotation/VSP_044718|||http://purl.uniprot.org/annotation/VSP_046639
http://togogenome.org/gene/9606:RERGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H628                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Ras-related and estrogen-regulated growth inhibitor-like protein|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320563|||http://purl.uniprot.org/annotation/VAR_039208
http://togogenome.org/gene/9606:HUNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57058                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hormonally up-regulated neu tumor-associated kinase|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086004|||http://purl.uniprot.org/annotation/VAR_040561|||http://purl.uniprot.org/annotation/VAR_040562|||http://purl.uniprot.org/annotation/VAR_040563|||http://purl.uniprot.org/annotation/VAR_040564
http://togogenome.org/gene/9606:FGF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3L4E7|||http://purl.uniprot.org/uniprot/O95750                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Fibroblast growth factor|||Fibroblast growth factor 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008993|||http://purl.uniprot.org/annotation/PRO_5035486505
http://togogenome.org/gene/9606:TGFB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A499FJK2|||http://purl.uniprot.org/uniprot/P01137                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interchain disulfide bond with LTBP1 and/or LRRC32, and subsequent regulation of activation of TGF-beta-1.|||Arm domain|||Associated with lower bone mineral density and higher frequency of vertebral fractures in Japanese post-menopausal women.|||Bowtie tail|||Cell attachment site|||Cleavage; by FURIN|||Does not affect integrin-binding or activation of TGF-beta-1.|||In CAEND.|||In CAEND; higher levels of active TGF-beta-1 in the culture medium.|||In CAEND; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro.|||In CAEND; leads to TGF-beta-1 intracellular accumulation.|||In CAEND; sporadic case; higher levels of active TGF-beta-1 in the culture medium.|||In IBDIMDE; decreased TGFB1-mediated activation of SMAD signaling; reduced levels of secreted TGFB1.|||In IBDIMDE; loss of TGFB1-mediated activation of SMAD signaling; mutant TGFB1 is not secreted.|||Interchain|||Interchain (with C-1359 or C-1384 in LTBP1); in inactive form|||Interchain (with C-223)|||Interchain (with C-225)|||Latency-associated peptide|||N-linked (GlcNAc...) asparagine|||Prevents cleavage and subsequent maturation of the protein. Generated in order to mimic the structure of the Transforming growth factor beta-1 proprotein.|||Straightjacket domain|||Strongly inhibits integrin-binding and activation of TGF-beta-1.|||TGF-beta family profile|||Transforming growth factor beta|||Transforming growth factor beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033762|||http://purl.uniprot.org/annotation/PRO_0000033763|||http://purl.uniprot.org/annotation/PRO_5019883448|||http://purl.uniprot.org/annotation/VAR_016171|||http://purl.uniprot.org/annotation/VAR_016172|||http://purl.uniprot.org/annotation/VAR_016173|||http://purl.uniprot.org/annotation/VAR_017607|||http://purl.uniprot.org/annotation/VAR_017608|||http://purl.uniprot.org/annotation/VAR_017609|||http://purl.uniprot.org/annotation/VAR_017610|||http://purl.uniprot.org/annotation/VAR_017611|||http://purl.uniprot.org/annotation/VAR_067303|||http://purl.uniprot.org/annotation/VAR_067304|||http://purl.uniprot.org/annotation/VAR_081584|||http://purl.uniprot.org/annotation/VAR_081585|||http://purl.uniprot.org/annotation/VAR_081586
http://togogenome.org/gene/9606:RNASE13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GAN3|||http://purl.uniprot.org/uniprot/V9HW52                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Probable inactive ribonuclease-like protein 13|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308705|||http://purl.uniprot.org/annotation/PRO_5014314733|||http://purl.uniprot.org/annotation/VAR_036874
http://togogenome.org/gene/9606:ENTREP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15884|||http://purl.uniprot.org/uniprot/Q8WU02                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased interaction with ITCH and no effect on interaction with EPN1; when associated with A-151.|||Decreased interaction with ITCH and no effect on interaction with EPN1; when associated with A-197.|||Disordered|||Endosomal transmembrane epsin interactor 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 1.|||In isoform 4.|||Lumenal|||Mediates interaction with EPN1|||PPxY; mediates interaction with ITCH|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089698|||http://purl.uniprot.org/annotation/VAR_047364|||http://purl.uniprot.org/annotation/VAR_050823|||http://purl.uniprot.org/annotation/VSP_035737|||http://purl.uniprot.org/annotation/VSP_061674
http://togogenome.org/gene/9606:ZNF69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UC07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 69                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295545|||http://purl.uniprot.org/annotation/VSP_026927|||http://purl.uniprot.org/annotation/VSP_026928
http://togogenome.org/gene/9606:GPR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46093                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Displays smaller cAMP, rho, PLC responses to mildly alkaline to acidic pH of 7.1 but almost the same or higher responses to severely acidic pH values of 6.5-6.2.|||Extracellular|||G-protein coupled receptor 4|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||No effect on pH-sensing activity.|||Polar residues|||Signaling-defective mutant. Endothelial permeability is decreased under acid conditions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069512|||http://purl.uniprot.org/annotation/VAR_049390
http://togogenome.org/gene/9606:OR1J4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW06|||http://purl.uniprot.org/uniprot/Q8NGS1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1J4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150440
http://togogenome.org/gene/9606:NOB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||NOB1|||PINc|||Phosphoserine|||RNA-binding protein NOB1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233265|||http://purl.uniprot.org/annotation/VAR_050287|||http://purl.uniprot.org/annotation/VAR_050288
http://togogenome.org/gene/9606:PDCD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKX4|||http://purl.uniprot.org/uniprot/Q53EL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of phosphorylation site, and loss of nuclear accumulation. Abolishes phosphorylation by PKB; when associated with A-67.|||Loss of phosphorylation site. Reduces interaction with BTRC. Abolishes phosphorylation by PKB; when associated with A-457.|||MI|||MI 1|||MI 2|||N-acetylmethionine|||No effect on inhibition of EIF4A1 and on inhibition of translation.|||No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-333.|||No effect on inhibition of EIF4A1 and on inhibition of translation; when associated with A-340.|||Nuclear localization signal|||Phosphodegron|||Phosphoserine|||Phosphoserine; by PKB|||Phosphoserine; by PKB and RPS6KB1|||Phosphotyrosine|||Polar residues|||Programmed cell death protein 4|||Reduced inhibition of EIF4A1 helicase activity.|||Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation.|||Reduced interaction with EIF4A1.|||Reduced interaction with EIF4A1. Strongly reduced inhibition of translation.|||Strongly reduced inhibition of EIF4A1. Strongly reduced inhibition of translation.|||Strongly reduced interaction with BTRC. Strongly reduced ubiquitination.|||Strongly reduced interaction with EIF4A1.|||Strongly reduced interaction with EIF4A1. Reduced inhibition of EIF4A1 helicase activity. Strongly reduced inhibition of translation.|||Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation.|||Strongly reduced interaction with EIF4A1. Strongly reduced inhibition of translation. Reduced inhibition of EIF4A1 helicase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256519|||http://purl.uniprot.org/annotation/VAR_028901|||http://purl.uniprot.org/annotation/VAR_028902|||http://purl.uniprot.org/annotation/VAR_036375|||http://purl.uniprot.org/annotation/VSP_045622
http://togogenome.org/gene/9606:ACACA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13085|||http://purl.uniprot.org/uniprot/Q7Z5W8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-grasp|||Abolishes interaction with BRCA1.|||Acetyl-CoA carboxylase 1|||Biotin carboxylation|||Biotinyl-binding|||Carboxyltransferase|||CoA carboxyltransferase C-terminal|||CoA carboxyltransferase N-terminal|||Frequency <0.004; may play a role in breast cancer susceptibility.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||N6-acetyllysine|||N6-biotinyllysine|||No effect on interaction with BRCA1.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146764|||http://purl.uniprot.org/annotation/VAR_028929|||http://purl.uniprot.org/annotation/VAR_036514|||http://purl.uniprot.org/annotation/VAR_042941|||http://purl.uniprot.org/annotation/VSP_026098|||http://purl.uniprot.org/annotation/VSP_026099|||http://purl.uniprot.org/annotation/VSP_026100
http://togogenome.org/gene/9606:LY96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Y9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes LPS-response.|||In isoform 2.|||Interaction with lipopolysaccharide|||Lymphocyte antigen 96|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018619|||http://purl.uniprot.org/annotation/VAR_024532|||http://purl.uniprot.org/annotation/VAR_050030|||http://purl.uniprot.org/annotation/VSP_055045
http://togogenome.org/gene/9606:STX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32856                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 1.|||In isoform 2.|||Syntaxin-2|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210196|||http://purl.uniprot.org/annotation/VAR_014850|||http://purl.uniprot.org/annotation/VAR_057259|||http://purl.uniprot.org/annotation/VSP_006334|||http://purl.uniprot.org/annotation/VSP_006335
http://togogenome.org/gene/9606:CTTNBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q20BG9|||http://purl.uniprot.org/uniprot/Q8WZ74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Asymmetric dimethylarginine|||Cortactin-binding protein 2|||Cortactin-binding protein-2 N-terminal|||Disordered|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227002|||http://purl.uniprot.org/annotation/VAR_025535|||http://purl.uniprot.org/annotation/VAR_048294
http://togogenome.org/gene/9606:UMPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5J1|||http://purl.uniprot.org/uniprot/P11172                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Domain linker|||For OMPdecase activity|||In ORAC1; increased OPRT activity; reduced ODC activity; reduced OPRT and ODC activities when associated with G-96.|||In ORAC1; reduced OPRT activity; no effect on ODC activity; reduced OPRT and ODC activities when associated with R-429.|||In ORAC1; reduced OPRT activity; reduced ODC activity.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of OMPdecase activity.|||N-acetylalanine|||OMPdecase|||OPRTase|||Orotidine 5'-phosphate decarboxylase|||Phosphoserine|||Phosphotyrosine|||Removed|||Uridine 5'-monophosphate synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139649|||http://purl.uniprot.org/annotation/VAR_006807|||http://purl.uniprot.org/annotation/VAR_006808|||http://purl.uniprot.org/annotation/VAR_006809|||http://purl.uniprot.org/annotation/VAR_006810|||http://purl.uniprot.org/annotation/VAR_020614|||http://purl.uniprot.org/annotation/VAR_020615|||http://purl.uniprot.org/annotation/VSP_009273|||http://purl.uniprot.org/annotation/VSP_047611|||http://purl.uniprot.org/annotation/VSP_047612
http://togogenome.org/gene/9606:ARL17B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0M5|||http://purl.uniprot.org/uniprot/Q8IVW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 17|||ADP-ribosylation factor-like protein 17 C-terminal|||In isoform 2.|||In isoform 4.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207482|||http://purl.uniprot.org/annotation/VAR_017170|||http://purl.uniprot.org/annotation/VSP_008753|||http://purl.uniprot.org/annotation/VSP_008756
http://togogenome.org/gene/9606:SLC31A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15432|||http://purl.uniprot.org/uniprot/Q53X94                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases almost 7 times the Cu(2+) affinity at pH 7.4 compared to wild-type. Decreases almost 10 times the Cu(2+) affinity at pH 7.4 compared to wild-type.|||Extracellular|||Helical|||Phosphoserine|||Protein SLC31A2|||Slightly decreases Cu(2+) affinity at pH 7.4. Decreases about 3 times the Cu(2+) affinity at pH 7.4 compared to wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195043
http://togogenome.org/gene/9606:PGPEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXJ5|||http://purl.uniprot.org/uniprot/S4R2Y9|||http://purl.uniprot.org/uniprot/U3KQ24                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pyroglutamyl-peptidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184761|||http://purl.uniprot.org/annotation/VSP_056472
http://togogenome.org/gene/9606:GPHA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R579|||http://purl.uniprot.org/uniprot/Q96T91                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  CTCK|||Glycoprotein hormone alpha-2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011672|||http://purl.uniprot.org/annotation/PRO_5014214215
http://togogenome.org/gene/9606:SHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92529                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CH1|||Disordered|||In isoform p52.|||PID|||Phosphoserine|||SH2|||SHC-transforming protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097734|||http://purl.uniprot.org/annotation/VSP_009805
http://togogenome.org/gene/9606:TMEM210                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLX4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 210                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329080
http://togogenome.org/gene/9606:E4F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66K89                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Alters DNA-binding.|||Alters DNA-binding; when associated with L-237.|||Alters DNA-binding; when associated with M-249.|||Alters DNA-binding; when associated with N-238.|||Alters DNA-binding; when associated with S-250.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Increases DNA-binding; when associated with S-194.|||Increases DNA-binding; when associated with S-197.|||Interaction with BMI1|||Mediates dimerization, DNA-binding, transcription repression of CCNA2 and interaction with HMGA2|||Mediates interaction with CDKN2A|||Mediates interaction with RASSF1|||Mediates interaction with TP53|||Phosphoserine|||Required for ubiquitin ligase activity|||Transcription factor E4F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324307|||http://purl.uniprot.org/annotation/VAR_060270|||http://purl.uniprot.org/annotation/VAR_060271
http://togogenome.org/gene/9606:ZNF257                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Q1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||Zinc finger protein 257                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047490|||http://purl.uniprot.org/annotation/VSP_040858|||http://purl.uniprot.org/annotation/VSP_040859|||http://purl.uniprot.org/annotation/VSP_040860
http://togogenome.org/gene/9606:C2CD2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14523                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Association with the cell membrane|||Basic and acidic residues|||C2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||Phospholipid transfer protein C2CD2L|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMP-LBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072596|||http://purl.uniprot.org/annotation/VAR_028797|||http://purl.uniprot.org/annotation/VSP_021158
http://togogenome.org/gene/9606:SLC26A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2B4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In CAON.|||In CAON; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||STAS|||Sulfate anion transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080155|||http://purl.uniprot.org/annotation/VAR_046727|||http://purl.uniprot.org/annotation/VAR_077134|||http://purl.uniprot.org/annotation/VAR_077135|||http://purl.uniprot.org/annotation/VAR_077136|||http://purl.uniprot.org/annotation/VSP_043671|||http://purl.uniprot.org/annotation/VSP_043672
http://togogenome.org/gene/9606:PUSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Z8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nucleophile|||Phosphoserine|||tRNA pseudouridine synthase-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057522|||http://purl.uniprot.org/annotation/VAR_034424|||http://purl.uniprot.org/annotation/VAR_051869|||http://purl.uniprot.org/annotation/VSP_036048
http://togogenome.org/gene/9606:MUC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E2RYF6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  124 X 10 AA approximate repeats|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Mucin-22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410470|||http://purl.uniprot.org/annotation/VAR_065357
http://togogenome.org/gene/9606:C5orf22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||UPF0489 protein C5orf22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305002|||http://purl.uniprot.org/annotation/VAR_035149|||http://purl.uniprot.org/annotation/VAR_035150|||http://purl.uniprot.org/annotation/VSP_028182|||http://purl.uniprot.org/annotation/VSP_028183|||http://purl.uniprot.org/annotation/VSP_028184
http://togogenome.org/gene/9606:RWDD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R7R2|||http://purl.uniprot.org/uniprot/B4DZK9|||http://purl.uniprot.org/uniprot/Q9UIY3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||RWD|||RWD domain-containing protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097543|||http://purl.uniprot.org/annotation/VSP_055504
http://togogenome.org/gene/9606:FOXA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0ZTD4|||http://purl.uniprot.org/uniprot/Q9Y261                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fork-head|||Hepatocyte nuclear factor 3-beta|||In Japanese subjects with maturity-onset diabetes of the young; unknown pathological significance.|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Transactivation domain 1|||Transactivation domain 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091795|||http://purl.uniprot.org/annotation/VAR_008858|||http://purl.uniprot.org/annotation/VSP_041212
http://togogenome.org/gene/9606:UBXN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T124                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 8 AA tandem repeats of P-G-P-G-P-G-P-S|||Disordered|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||Pro residues|||SEP|||UBX|||UBX domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284921|||http://purl.uniprot.org/annotation/VAR_031860|||http://purl.uniprot.org/annotation/VAR_031861|||http://purl.uniprot.org/annotation/VAR_031862|||http://purl.uniprot.org/annotation/VAR_031863|||http://purl.uniprot.org/annotation/VAR_031864|||http://purl.uniprot.org/annotation/VAR_031865|||http://purl.uniprot.org/annotation/VAR_052690|||http://purl.uniprot.org/annotation/VSP_024771|||http://purl.uniprot.org/annotation/VSP_024772|||http://purl.uniprot.org/annotation/VSP_024773|||http://purl.uniprot.org/annotation/VSP_024774|||http://purl.uniprot.org/annotation/VSP_024775|||http://purl.uniprot.org/annotation/VSP_024776|||http://purl.uniprot.org/annotation/VSP_024777
http://togogenome.org/gene/9606:C5orf63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NC05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glutaredoxin-like protein C5orf63|||In isoform 2.|||Polar residues|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328756|||http://purl.uniprot.org/annotation/VSP_044904
http://togogenome.org/gene/9606:STS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJL0|||http://purl.uniprot.org/uniprot/A6PYA4|||http://purl.uniprot.org/uniprot/P08842|||http://purl.uniprot.org/uniprot/Q0W975                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Cytoplasmic|||Does not affect steryl-sulfatase activity.|||Helical|||In IXL.|||In IXL; loss of steryl-sulfatase activity.|||In IXL; strong decreases of steryl-sulfatase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Nucleophile|||Steryl-sulfatase|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033414|||http://purl.uniprot.org/annotation/PRO_5040077377|||http://purl.uniprot.org/annotation/VAR_007240|||http://purl.uniprot.org/annotation/VAR_007241|||http://purl.uniprot.org/annotation/VAR_007242|||http://purl.uniprot.org/annotation/VAR_014020|||http://purl.uniprot.org/annotation/VAR_014021|||http://purl.uniprot.org/annotation/VAR_014022|||http://purl.uniprot.org/annotation/VAR_014023|||http://purl.uniprot.org/annotation/VAR_081729
http://togogenome.org/gene/9606:QARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z840|||http://purl.uniprot.org/uniprot/P47897                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Decreases catalytic efficiency about 60-fold.|||Glutamine--tRNA ligase|||Glutaminyl-tRNA synthetase class Ib non-specific RNA-binding|||In MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; does not interact with RARS1; results in reduced protein solubility.|||In MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; results in reduced protein solubility.|||In MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195860|||http://purl.uniprot.org/annotation/PRO_5002866797|||http://purl.uniprot.org/annotation/VAR_071189|||http://purl.uniprot.org/annotation/VAR_071190|||http://purl.uniprot.org/annotation/VAR_071191|||http://purl.uniprot.org/annotation/VAR_071192|||http://purl.uniprot.org/annotation/VSP_055107
http://togogenome.org/gene/9606:ZNRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND25                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  About 10-fold decreased binding to UBE2N.|||Complete loss of binding to ATP1A1; when associated with A-145.|||Complete loss of binding to ATP1A1; when associated with A-148.|||Disordered|||E3 ubiquitin-protein ligase ZNRF1|||Greatly reduced binding to ATP1A1.|||In isoform 2.|||Loss of E3 activity.|||N-myristoyl glycine|||Partial loss of binding to 14-3-3.|||Phosphoserine|||Phosphotyrosine; by SRC|||RING-type; atypical|||Removed|||Required for endosomal and lysosomal localization and myristoylation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277799|||http://purl.uniprot.org/annotation/VSP_023088
http://togogenome.org/gene/9606:GTSE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G2 and S phase-expressed protein 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083875|||http://purl.uniprot.org/annotation/VAR_021973|||http://purl.uniprot.org/annotation/VAR_024154|||http://purl.uniprot.org/annotation/VAR_032816|||http://purl.uniprot.org/annotation/VAR_032817|||http://purl.uniprot.org/annotation/VAR_032818|||http://purl.uniprot.org/annotation/VAR_032819|||http://purl.uniprot.org/annotation/VAR_032820|||http://purl.uniprot.org/annotation/VAR_032821|||http://purl.uniprot.org/annotation/VAR_056905
http://togogenome.org/gene/9606:UNC5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K385|||http://purl.uniprot.org/uniprot/O95185                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Cytoplasmic|||Death|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||In AD; associated with susceptibility to late-onset disease; increased susceptibility to neuronal cell death.|||In isoform 2.|||Interaction with DCC|||N-linked (GlcNAc...) asparagine|||Netrin receptor UNC5|||Netrin receptor UNC5C|||Phosphoserine|||Phosphotyrosine|||Required for netrin-mediated axon repulsion of neuronal growth cones|||TSP type-1 1|||TSP type-1 2|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036075|||http://purl.uniprot.org/annotation/PRO_5002724629|||http://purl.uniprot.org/annotation/VAR_019731|||http://purl.uniprot.org/annotation/VAR_019732|||http://purl.uniprot.org/annotation/VAR_055327|||http://purl.uniprot.org/annotation/VAR_081368|||http://purl.uniprot.org/annotation/VSP_011700|||http://purl.uniprot.org/annotation/VSP_011701
http://togogenome.org/gene/9606:NUDT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C024                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for coenzyme A binding|||In isoform 2.|||In isoform 3.|||Microbody targeting signal|||N6-succinyllysine|||Nudix box|||Nudix hydrolase|||Peroxisomal coenzyme A diphosphatase NUDT7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057140|||http://purl.uniprot.org/annotation/VAR_050415|||http://purl.uniprot.org/annotation/VAR_050416|||http://purl.uniprot.org/annotation/VSP_047605|||http://purl.uniprot.org/annotation/VSP_053820|||http://purl.uniprot.org/annotation/VSP_053821
http://togogenome.org/gene/9606:DENND2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DENN domain-containing protein 2C|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242684|||http://purl.uniprot.org/annotation/VAR_026859|||http://purl.uniprot.org/annotation/VAR_026860|||http://purl.uniprot.org/annotation/VSP_019468|||http://purl.uniprot.org/annotation/VSP_036782
http://togogenome.org/gene/9606:SLC35B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZW4|||http://purl.uniprot.org/uniprot/B2R8V5|||http://purl.uniprot.org/uniprot/B4E1Q6|||http://purl.uniprot.org/uniprot/Q9H1N7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Adenosine 3'-phospho 5'-phosphosulfate transporter 2|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213379|||http://purl.uniprot.org/annotation/VSP_016193|||http://purl.uniprot.org/annotation/VSP_016194|||http://purl.uniprot.org/annotation/VSP_016195|||http://purl.uniprot.org/annotation/VSP_016196
http://togogenome.org/gene/9606:FZD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-3|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012982|||http://purl.uniprot.org/annotation/VAR_066960|||http://purl.uniprot.org/annotation/VAR_066961|||http://purl.uniprot.org/annotation/VAR_066962
http://togogenome.org/gene/9606:CERS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5B7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Altered specificity toward acyl donor; generates C22-C24 ceramides instead of C16-ceramide.|||Ceramide synthase 5|||Cytoplasmic|||Decreased phosphorylation.|||Disordered|||Does not affect ceramide synthase activity.|||Does not affect specificity toward acyl donor.|||Helical|||Homeobox-like|||In isoform 2.|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reduced N-glycosylation.|||Strongly decreased ceramide synthase activity.|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185514|||http://purl.uniprot.org/annotation/VAR_019558|||http://purl.uniprot.org/annotation/VSP_054572
http://togogenome.org/gene/9606:TMEM192                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY95                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Transmembrane protein 192                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311267|||http://purl.uniprot.org/annotation/VSP_029502
http://togogenome.org/gene/9606:ABCB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP58                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family B member 6|||Abolishes ATP hydrolysis. Abolishes coproporphyrin III transport.|||Cytoplasmic|||Decrease expression; does not affect substrate binding; does not affect ATP-binding; loss of plasma membrane expression.|||Decreases protein expression. Affects protein stability. Loss of ability to stimulate porphyrin synthesis.|||Decreases protein expression. Impairs endoplasmic reticulum exit; when associated with C-8. Affects protein stability.|||Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-498 and Q-677. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-498 and Q-677.|||Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-498; and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-498; and Q-775.|||Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-447; Q-677 and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-447; Q-677 and Q-775.|||Does not affect N-glycosylation. Does not affect N-glycosylation; when associated with Q-498; Q-677 and Q-775. Does not affect trafficking from endoplasmic reticulum; when associated with Q-498; Q-677 and Q-775.|||Does not affect subcellular location in early melanosome and lysosome. Does not rescue the normal amyloid fibril formation and normal maturation of pigmented melanosomes. Does not influence trafficking of melanosomal proteins. Fails to rescue vacuolar sequestration of cadmium in Schizosaccharomyces pombe and Caenorhabditis elegans strains defective for HMT-1. Fails to rescue the cadmium tolerance in Schizosaccharomyces pombe and Caenorhabditis elegans strains defective for HMT-1. Does not rescue vacuolar cadmium levels in hmt-1 mutant S.pombe.|||Does not affect substrate binding. Does not affect N-glycosylation. Impairs endoplasmic reticulum exit. Impairs endoplasmic reticulum exit; when associated with C-8. Increases ABCB6 proteasomal degradation. Affects protein stability. Does not affect migration in the presence of DTT; when associated with A-50 and A-120.|||Does not affect substrate-stimulate ATPase activity.|||Helical|||In DUH3.|||In DUH3; the protein is retained in the Golgi apparatus.|||In DUH3; the protein is retained in the Golgi apparatus. Does not affect subcellular location in early melanosome and lysosome. Does not rescue the normal amyloid fibril formation and normal maturation of pigmented melanosomes. Does not influence trafficking of melanosomal proteins..|||In MCOPCB7; hypomorphic mutation.|||In MCOPCB7; unknown pathological significance; hypomorphic mutation.|||In PSHK2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increases migration in the absence of DTT; when associated with A-120. Reduces migration in with the presence of DTT; when associated with A-120.|||Increases migration in the absence of DTT; when associated with A-50. Reduces migration in with the presence of DTT; when associated with A-50.|||Loss of N-glycosylation.|||Loss of N-glycosylation. Loss of N-glycosylation; when associated with Q-447; Q-498; Q-677 and Q-775. Does not affect substrate binding.|||Loss of substrate-stimulate ATPase activity.|||Loss of substrate-stimulate ATPase activity. Impairs protein expression.|||Lumenal|||May be a modifier of disease severity in porphyria patients; increases expression; does not affect substrate binding; impairs ATP-binding; Loss of ATP-dependent coproporphyrin III transport; Highly decrease plasma membrane expression.|||May be a modifier of disease severity in porphyria patients; loss of expression.|||N-linked (GlcNAc...) asparagine|||Required for ATPase activity|||Required for the lysosomal targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000248|||http://purl.uniprot.org/annotation/VAR_029749|||http://purl.uniprot.org/annotation/VAR_035732|||http://purl.uniprot.org/annotation/VAR_047552|||http://purl.uniprot.org/annotation/VAR_060986|||http://purl.uniprot.org/annotation/VAR_067394|||http://purl.uniprot.org/annotation/VAR_067395|||http://purl.uniprot.org/annotation/VAR_070602|||http://purl.uniprot.org/annotation/VAR_070603|||http://purl.uniprot.org/annotation/VAR_070604|||http://purl.uniprot.org/annotation/VAR_071133|||http://purl.uniprot.org/annotation/VAR_071134|||http://purl.uniprot.org/annotation/VAR_071135|||http://purl.uniprot.org/annotation/VAR_071136|||http://purl.uniprot.org/annotation/VAR_073973|||http://purl.uniprot.org/annotation/VAR_073974|||http://purl.uniprot.org/annotation/VAR_076206|||http://purl.uniprot.org/annotation/VAR_084494|||http://purl.uniprot.org/annotation/VAR_084495|||http://purl.uniprot.org/annotation/VAR_084496|||http://purl.uniprot.org/annotation/VAR_084497|||http://purl.uniprot.org/annotation/VAR_084498|||http://purl.uniprot.org/annotation/VAR_084499|||http://purl.uniprot.org/annotation/VSP_021973
http://togogenome.org/gene/9606:ABLIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK02|||http://purl.uniprot.org/uniprot/F5GYR0|||http://purl.uniprot.org/uniprot/Q6H8Q1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding LIM protein 2|||Basic and acidic residues|||Disordered|||HP|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2, isoform 3, isoform 5 and isoform 8.|||In isoform 3, isoform 4 and isoform 6.|||In isoform 3, isoform 6, isoform 7 and isoform 8.|||In isoform 4, isoform 5, isoform 6, isoform 8 and isoform 9.|||In isoform 4.|||In isoform 6.|||In isoform 9.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075699|||http://purl.uniprot.org/annotation/VAR_062665|||http://purl.uniprot.org/annotation/VAR_062666|||http://purl.uniprot.org/annotation/VSP_012112|||http://purl.uniprot.org/annotation/VSP_012113|||http://purl.uniprot.org/annotation/VSP_012114|||http://purl.uniprot.org/annotation/VSP_012115|||http://purl.uniprot.org/annotation/VSP_012116|||http://purl.uniprot.org/annotation/VSP_012117|||http://purl.uniprot.org/annotation/VSP_012118|||http://purl.uniprot.org/annotation/VSP_012119|||http://purl.uniprot.org/annotation/VSP_046646
http://togogenome.org/gene/9606:ENO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06733                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-enolase|||Decreased 2-hydroxyisobutyrylation leading to decreased phosphopyruvate hydratase activity.|||Epitope recognized by CAR and healthy patient antibodies|||Epitope recognized by CAR antibodies|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform MBP-1.|||Loss of transcriptional repression and cell growth inhibition; when associated with A-384.|||Loss of transcriptional repression and cell growth inhibition; when associated with A-388.|||MBP1 protein production. No MBP1 protein production; when associated with I-94.|||MBP1 protein production. No MBP1 protein production; when associated with I-97.|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed|||Required for interaction with PLG|||Required for repression of c-myc promoter activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134097|||http://purl.uniprot.org/annotation/VAR_025172|||http://purl.uniprot.org/annotation/VAR_048936|||http://purl.uniprot.org/annotation/VSP_018725
http://togogenome.org/gene/9606:ITGA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTN6|||http://purl.uniprot.org/uniprot/Q9UKX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||Helical|||In isoform 2.|||Integrin alpha-11|||N-linked (GlcNAc...) asparagine|||No effect on RAB21-binding.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016318|||http://purl.uniprot.org/annotation/PRO_5002788440|||http://purl.uniprot.org/annotation/VAR_009889|||http://purl.uniprot.org/annotation/VAR_009890|||http://purl.uniprot.org/annotation/VAR_009891|||http://purl.uniprot.org/annotation/VAR_009892|||http://purl.uniprot.org/annotation/VAR_009894|||http://purl.uniprot.org/annotation/VAR_020038|||http://purl.uniprot.org/annotation/VAR_020039|||http://purl.uniprot.org/annotation/VSP_053416
http://togogenome.org/gene/9606:FAM131A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXB0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||In isoform 2.|||Protein FAM131A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243932|||http://purl.uniprot.org/annotation/VAR_036118|||http://purl.uniprot.org/annotation/VSP_059988|||http://purl.uniprot.org/annotation/VSP_059989
http://togogenome.org/gene/9606:PLXNC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60486                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-C1|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232749|||http://purl.uniprot.org/annotation/VAR_050602
http://togogenome.org/gene/9606:TICAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Complete loss of phosphorylation in response to LPS.|||Disordered|||In isoform 2.|||Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4.|||Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation.|||Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal.|||Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B.|||N-myristoyl glycine|||No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B.|||No effect on phosphorylation.|||Phosphoserine; by PKC/PRKCE|||Phosphotyrosine|||Removed|||Results in relocalization from membrane to cytosol; Loss of ability to transduce TLR4-signal. Loss of TLR2-mediated activation of IRF7.|||Significant decrease of localization in the membrane.|||TIR|||TIR domain-containing adapter molecule 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317689|||http://purl.uniprot.org/annotation/VSP_047437
http://togogenome.org/gene/9606:RNF180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T96                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||E3 ubiquitin-protein ligase RNF180|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with ZIC2|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261617|||http://purl.uniprot.org/annotation/VSP_021738|||http://purl.uniprot.org/annotation/VSP_021739|||http://purl.uniprot.org/annotation/VSP_021740
http://togogenome.org/gene/9606:H2BW2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C1H6|||http://purl.uniprot.org/uniprot/W0TYI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Histone H2A/H2B/H3|||Histone H2B type F-M|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244827
http://togogenome.org/gene/9606:PCGF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSM1                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with BCOR and BCORL1.|||Abolishes repressor activity. May be a PKC phosphorylation site.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Marked decrease of repressor activity. May be a kinase phosphorylation site.|||N-acetylalanine|||Phosphoserine|||Polycomb group RING finger protein 1|||RING-finger and WD40-associated ubiquitin-like domain (RAWUL); sufficient for interaction with BCOR and BCORL1|||RING-type|||Removed|||Required for repressor activity|||Required for the interaction with the KDM2B-SKP1 heterodimeric complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277855|||http://purl.uniprot.org/annotation/VSP_036393
http://togogenome.org/gene/9606:ZNF74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5P3|||http://purl.uniprot.org/uniprot/Q05BG0|||http://purl.uniprot.org/uniprot/Q16587                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||KRAB|||Zinc finger protein 74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047383|||http://purl.uniprot.org/annotation/VAR_012993|||http://purl.uniprot.org/annotation/VAR_012994|||http://purl.uniprot.org/annotation/VSP_006891|||http://purl.uniprot.org/annotation/VSP_006892|||http://purl.uniprot.org/annotation/VSP_006893|||http://purl.uniprot.org/annotation/VSP_045530|||http://purl.uniprot.org/annotation/VSP_045531
http://togogenome.org/gene/9606:CCDC117                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z820|||http://purl.uniprot.org/uniprot/Q8IWD4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 117|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254138|||http://purl.uniprot.org/annotation/VAR_028823|||http://purl.uniprot.org/annotation/VAR_028824|||http://purl.uniprot.org/annotation/VSP_021185|||http://purl.uniprot.org/annotation/VSP_054912|||http://purl.uniprot.org/annotation/VSP_054913
http://togogenome.org/gene/9606:TBC1D2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RTQ2|||http://purl.uniprot.org/uniprot/Q9UPU7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In NEDSGO.|||In NEDSGO; severely reduced protein abundance due to nonsense-mediated decay of mutant transcripts in homozygous patient cells.|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315713|||http://purl.uniprot.org/annotation/VAR_085821|||http://purl.uniprot.org/annotation/VAR_085822|||http://purl.uniprot.org/annotation/VAR_085823|||http://purl.uniprot.org/annotation/VSP_030666|||http://purl.uniprot.org/annotation/VSP_030667|||http://purl.uniprot.org/annotation/VSP_030668|||http://purl.uniprot.org/annotation/VSP_030669
http://togogenome.org/gene/9606:QTRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H974                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Queuine tRNA-ribosyltransferase accessory subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295633|||http://purl.uniprot.org/annotation/VSP_045140|||http://purl.uniprot.org/annotation/VSP_045141|||http://purl.uniprot.org/annotation/VSP_046859
http://togogenome.org/gene/9606:NFYC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13952                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 1, isoform 2, isoform 4, isoform 6 and isoform 7.|||In isoform 1, isoform 4, isoform 5, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Nuclear transcription factor Y subunit gamma|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218246|||http://purl.uniprot.org/annotation/VAR_035702|||http://purl.uniprot.org/annotation/VSP_000851|||http://purl.uniprot.org/annotation/VSP_000852|||http://purl.uniprot.org/annotation/VSP_043348|||http://purl.uniprot.org/annotation/VSP_043349|||http://purl.uniprot.org/annotation/VSP_046350
http://togogenome.org/gene/9606:KRTAP10-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60371                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||29 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185214|||http://purl.uniprot.org/annotation/VAR_017699|||http://purl.uniprot.org/annotation/VAR_057649|||http://purl.uniprot.org/annotation/VAR_060049|||http://purl.uniprot.org/annotation/VAR_060050|||http://purl.uniprot.org/annotation/VAR_062533
http://togogenome.org/gene/9606:GAA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10253                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  70 kDa lysosomal alpha-glucosidase|||76 kDa lysosomal alpha-glucosidase|||Disordered|||Found in a patient with GSD2; unknown pathological significance.|||In GSD2.|||In GSD2; adult form.|||In GSD2; almost complete loss of activity.|||In GSD2; extremely low residual enzymatic activity.|||In GSD2; infantile form.|||In GSD2; infantile form; most common mutation; deficient in phosphorylation and in proteolytic processing.|||In GSD2; infantile form; severe.|||In GSD2; infantile form; severe; almost complete loss of activity.|||In GSD2; infantile form; severe; complete loss of activity.|||In GSD2; infantile form; severe; loss of activity.|||In GSD2; infantile form; severe; loss of activity; shows enzyme localization primarily in the ER-Golgi compartment suggesting that mutation could affect the normal processing and stability of the enzyme.|||In GSD2; infantile/adult form.|||In GSD2; infantile/juvenile form; severe; loss of activity.|||In GSD2; infantile; mild partial loss of activity.|||In GSD2; infantile; severe.|||In GSD2; juvenile form.|||In GSD2; juvenile form; almost complete loss of activity.|||In GSD2; juvenile form; loss of activity.|||In GSD2; juvenile form; mild; partial loss of activity.|||In GSD2; juvenile form; severe.|||In GSD2; loss of function of the mutant enzyme.|||In GSD2; mild; partial loss of activity.|||In GSD2; mild; requires 2 nucleotide substitutions.|||In GSD2; no enzymatic activity; shows enzyme localization primarily in the ER-Golgi compartment suggesting that mutation could affect the normal processing and stability of the enzyme.|||In GSD2; no residual enzymatic activity.|||In GSD2; severe.|||In GSD2; severe; loss of activity.|||In GSD2; unknown pathological significance.|||In allele GAA*2; lower affinity for glycogen and starch but not for lower-molecular weight substrates.|||In allele GAA*4.|||Loss of activity.|||Loss of glycosylation site.|||Lysosomal alpha-glucosidase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||P-type|||Retains about half of the activity compared with the wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018565|||http://purl.uniprot.org/annotation/PRO_0000018566|||http://purl.uniprot.org/annotation/PRO_0000018567|||http://purl.uniprot.org/annotation/PRO_0000018568|||http://purl.uniprot.org/annotation/VAR_004285|||http://purl.uniprot.org/annotation/VAR_004286|||http://purl.uniprot.org/annotation/VAR_004287|||http://purl.uniprot.org/annotation/VAR_004288|||http://purl.uniprot.org/annotation/VAR_004289|||http://purl.uniprot.org/annotation/VAR_004290|||http://purl.uniprot.org/annotation/VAR_004291|||http://purl.uniprot.org/annotation/VAR_004292|||http://purl.uniprot.org/annotation/VAR_004293|||http://purl.uniprot.org/annotation/VAR_004294|||http://purl.uniprot.org/annotation/VAR_004295|||http://purl.uniprot.org/annotation/VAR_004296|||http://purl.uniprot.org/annotation/VAR_004297|||http://purl.uniprot.org/annotation/VAR_004298|||http://purl.uniprot.org/annotation/VAR_004299|||http://purl.uniprot.org/annotation/VAR_004300|||http://purl.uniprot.org/annotation/VAR_004301|||http://purl.uniprot.org/annotation/VAR_004302|||http://purl.uniprot.org/annotation/VAR_004303|||http://purl.uniprot.org/annotation/VAR_004304|||http://purl.uniprot.org/annotation/VAR_004305|||http://purl.uniprot.org/annotation/VAR_004306|||http://purl.uniprot.org/annotation/VAR_004307|||http://purl.uniprot.org/annotation/VAR_004308|||http://purl.uniprot.org/annotation/VAR_004309|||http://purl.uniprot.org/annotation/VAR_004310|||http://purl.uniprot.org/annotation/VAR_004311|||http://purl.uniprot.org/annotation/VAR_004312|||http://purl.uniprot.org/annotation/VAR_004313|||http://purl.uniprot.org/annotation/VAR_004314|||http://purl.uniprot.org/annotation/VAR_004315|||http://purl.uniprot.org/annotation/VAR_004316|||http://purl.uniprot.org/annotation/VAR_004317|||http://purl.uniprot.org/annotation/VAR_004318|||http://purl.uniprot.org/annotation/VAR_008689|||http://purl.uniprot.org/annotation/VAR_008690|||http://purl.uniprot.org/annotation/VAR_008692|||http://purl.uniprot.org/annotation/VAR_018078|||http://purl.uniprot.org/annotation/VAR_018079|||http://purl.uniprot.org/annotation/VAR_018080|||http://purl.uniprot.org/annotation/VAR_018081|||http://purl.uniprot.org/annotation/VAR_018082|||http://purl.uniprot.org/annotation/VAR_018083|||http://purl.uniprot.org/annotation/VAR_018084|||http://purl.uniprot.org/annotation/VAR_018085|||http://purl.uniprot.org/annotation/VAR_018086|||http://purl.uniprot.org/annotation/VAR_018087|||http://purl.uniprot.org/annotation/VAR_018088|||http://purl.uniprot.org/annotation/VAR_018089|||http://purl.uniprot.org/annotation/VAR_018090|||http://purl.uniprot.org/annotation/VAR_018091|||http://purl.uniprot.org/annotation/VAR_018092|||http://purl.uniprot.org/annotation/VAR_018093|||http://purl.uniprot.org/annotation/VAR_018094|||http://purl.uniprot.org/annotation/VAR_018095|||http://purl.uniprot.org/annotation/VAR_018096|||http://purl.uniprot.org/annotation/VAR_018097|||http://purl.uniprot.org/annotation/VAR_029025|||http://purl.uniprot.org/annotation/VAR_029026|||http://purl.uniprot.org/annotation/VAR_029027|||http://purl.uniprot.org/annotation/VAR_029028|||http://purl.uniprot.org/annotation/VAR_029029|||http://purl.uniprot.org/annotation/VAR_029030|||http://purl.uniprot.org/annotation/VAR_029031|||http://purl.uniprot.org/annotation/VAR_029032|||http://purl.uniprot.org/annotation/VAR_029033|||http://purl.uniprot.org/annotation/VAR_029034|||http://purl.uniprot.org/annotation/VAR_029035|||http://purl.uniprot.org/annotation/VAR_029036|||http://purl.uniprot.org/annotation/VAR_029037|||http://purl.uniprot.org/annotation/VAR_029038|||http://purl.uniprot.org/annotation/VAR_029039|||http://purl.uniprot.org/annotation/VAR_029040|||http://purl.uniprot.org/annotation/VAR_046467|||http://purl.uniprot.org/annotation/VAR_046468|||http://purl.uniprot.org/annotation/VAR_046469|||http://purl.uniprot.org/annotation/VAR_046470|||http://purl.uniprot.org/annotation/VAR_046471|||http://purl.uniprot.org/annotation/VAR_046472|||http://purl.uniprot.org/annotation/VAR_046473|||http://purl.uniprot.org/annotation/VAR_046474|||http://purl.uniprot.org/annotation/VAR_046475|||http://purl.uniprot.org/annotation/VAR_046476|||http://purl.uniprot.org/annotation/VAR_046477|||http://purl.uniprot.org/annotation/VAR_046478|||http://purl.uniprot.org/annotation/VAR_046479|||http://purl.uniprot.org/annotation/VAR_068564|||http://purl.uniprot.org/annotation/VAR_068565|||http://purl.uniprot.org/annotation/VAR_068566|||http://purl.uniprot.org/annotation/VAR_068567|||http://purl.uniprot.org/annotation/VAR_068568|||http://purl.uniprot.org/annotation/VAR_068569|||http://purl.uniprot.org/annotation/VAR_068570|||http://purl.uniprot.org/annotation/VAR_068571|||http://purl.uniprot.org/annotation/VAR_068572|||http://purl.uniprot.org/annotation/VAR_068573|||http://purl.uniprot.org/annotation/VAR_068574|||http://purl.uniprot.org/annotation/VAR_068575|||http://purl.uniprot.org/annotation/VAR_068576|||http://purl.uniprot.org/annotation/VAR_068577|||http://purl.uniprot.org/annotation/VAR_068578|||http://purl.uniprot.org/annotation/VAR_068579|||http://purl.uniprot.org/annotation/VAR_068580|||http://purl.uniprot.org/annotation/VAR_068581|||http://purl.uniprot.org/annotation/VAR_068582|||http://purl.uniprot.org/annotation/VAR_068583|||http://purl.uniprot.org/annotation/VAR_068584|||http://purl.uniprot.org/annotation/VAR_068585|||http://purl.uniprot.org/annotation/VAR_068586|||http://purl.uniprot.org/annotation/VAR_068587|||http://purl.uniprot.org/annotation/VAR_068588|||http://purl.uniprot.org/annotation/VAR_068589|||http://purl.uniprot.org/annotation/VAR_068590|||http://purl.uniprot.org/annotation/VAR_068591|||http://purl.uniprot.org/annotation/VAR_068592|||http://purl.uniprot.org/annotation/VAR_068593|||http://purl.uniprot.org/annotation/VAR_068594|||http://purl.uniprot.org/annotation/VAR_068595|||http://purl.uniprot.org/annotation/VAR_068596|||http://purl.uniprot.org/annotation/VAR_068597|||http://purl.uniprot.org/annotation/VAR_068598|||http://purl.uniprot.org/annotation/VAR_068599|||http://purl.uniprot.org/annotation/VAR_068600|||http://purl.uniprot.org/annotation/VAR_068601|||http://purl.uniprot.org/annotation/VAR_068602|||http://purl.uniprot.org/annotation/VAR_068603|||http://purl.uniprot.org/annotation/VAR_068604|||http://purl.uniprot.org/annotation/VAR_068605|||http://purl.uniprot.org/annotation/VAR_068606|||http://purl.uniprot.org/annotation/VAR_068607|||http://purl.uniprot.org/annotation/VAR_068608|||http://purl.uniprot.org/annotation/VAR_068609|||http://purl.uniprot.org/annotation/VAR_068610|||http://purl.uniprot.org/annotation/VAR_068611|||http://purl.uniprot.org/annotation/VAR_068612|||http://purl.uniprot.org/annotation/VAR_068613|||http://purl.uniprot.org/annotation/VAR_068614|||http://purl.uniprot.org/annotation/VAR_068615|||http://purl.uniprot.org/annotation/VAR_068616|||http://purl.uniprot.org/annotation/VAR_068617|||http://purl.uniprot.org/annotation/VAR_068618|||http://purl.uniprot.org/annotation/VAR_068619|||http://purl.uniprot.org/annotation/VAR_068620|||http://purl.uniprot.org/annotation/VAR_068621|||http://purl.uniprot.org/annotation/VAR_068622|||http://purl.uniprot.org/annotation/VAR_068623|||http://purl.uniprot.org/annotation/VAR_068624|||http://purl.uniprot.org/annotation/VAR_068625|||http://purl.uniprot.org/annotation/VAR_068626|||http://purl.uniprot.org/annotation/VAR_068627|||http://purl.uniprot.org/annotation/VAR_068628|||http://purl.uniprot.org/annotation/VAR_068629|||http://purl.uniprot.org/annotation/VAR_068630|||http://purl.uniprot.org/annotation/VAR_068631|||http://purl.uniprot.org/annotation/VAR_068632|||http://purl.uniprot.org/annotation/VAR_068633|||http://purl.uniprot.org/annotation/VAR_068634|||http://purl.uniprot.org/annotation/VAR_068635|||http://purl.uniprot.org/annotation/VAR_070017|||http://purl.uniprot.org/annotation/VAR_070018|||http://purl.uniprot.org/annotation/VAR_070019|||http://purl.uniprot.org/annotation/VAR_070020|||http://purl.uniprot.org/annotation/VAR_074277|||http://purl.uniprot.org/annotation/VAR_074278|||http://purl.uniprot.org/annotation/VAR_074279
http://togogenome.org/gene/9606:CLEC12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QGZ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 12 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313578|||http://purl.uniprot.org/annotation/VAR_037669|||http://purl.uniprot.org/annotation/VSP_030030|||http://purl.uniprot.org/annotation/VSP_030031|||http://purl.uniprot.org/annotation/VSP_030032|||http://purl.uniprot.org/annotation/VSP_030033|||http://purl.uniprot.org/annotation/VSP_039854
http://togogenome.org/gene/9606:TPD52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55327                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Polar residues|||Tumor protein D52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185738|||http://purl.uniprot.org/annotation/VAR_061860|||http://purl.uniprot.org/annotation/VSP_035751|||http://purl.uniprot.org/annotation/VSP_037378|||http://purl.uniprot.org/annotation/VSP_043510|||http://purl.uniprot.org/annotation/VSP_047718|||http://purl.uniprot.org/annotation/VSP_047719|||http://purl.uniprot.org/annotation/VSP_047720
http://togogenome.org/gene/9606:ENTPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49961                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 1|||Extracellular|||Helical|||In SPG64.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209902|||http://purl.uniprot.org/annotation/VAR_022099|||http://purl.uniprot.org/annotation/VAR_071082|||http://purl.uniprot.org/annotation/VSP_003607|||http://purl.uniprot.org/annotation/VSP_003608|||http://purl.uniprot.org/annotation/VSP_003609|||http://purl.uniprot.org/annotation/VSP_044283|||http://purl.uniprot.org/annotation/VSP_044284|||http://purl.uniprot.org/annotation/VSP_046050
http://togogenome.org/gene/9606:PHKG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15735                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding (domain-C)|||Calmodulin-binding (domain-N)|||In GSD9C.|||In isoform 2.|||Phosphorylase b kinase gamma catalytic chain, liver/testis isoform|||Phosphoserine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086512|||http://purl.uniprot.org/annotation/VAR_009517|||http://purl.uniprot.org/annotation/VAR_009518|||http://purl.uniprot.org/annotation/VAR_020854|||http://purl.uniprot.org/annotation/VAR_020855|||http://purl.uniprot.org/annotation/VAR_040996|||http://purl.uniprot.org/annotation/VAR_051658|||http://purl.uniprot.org/annotation/VSP_041858|||http://purl.uniprot.org/annotation/VSP_041859
http://togogenome.org/gene/9606:KLF16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXK1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 16|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047158
http://togogenome.org/gene/9606:MATN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RRP8|||http://purl.uniprot.org/uniprot/A5D8U1|||http://purl.uniprot.org/uniprot/A6NNA4|||http://purl.uniprot.org/uniprot/B3KQB2|||http://purl.uniprot.org/uniprot/O95460                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1; incomplete|||EGF-like 2|||EGF-like 3|||EGF-like 4|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Matrilin-4|||N-linked (GlcNAc...) asparagine|||VWFA|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007660|||http://purl.uniprot.org/annotation/PRO_5002680927|||http://purl.uniprot.org/annotation/PRO_5005660229|||http://purl.uniprot.org/annotation/PRO_5005662607|||http://purl.uniprot.org/annotation/PRO_5014296828|||http://purl.uniprot.org/annotation/VAR_055758|||http://purl.uniprot.org/annotation/VAR_055759|||http://purl.uniprot.org/annotation/VSP_001400|||http://purl.uniprot.org/annotation/VSP_015255|||http://purl.uniprot.org/annotation/VSP_015256
http://togogenome.org/gene/9606:NATD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6N6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N-acetyltransferase|||Protein NATD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320656|||http://purl.uniprot.org/annotation/VAR_062227
http://togogenome.org/gene/9606:TFCP2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Grh/CP2 DB|||Impairs the formation of oligomeric homo-complexes in solution.|||Polar residues|||SAM2-like domain|||Transcription factor CP2-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228006
http://togogenome.org/gene/9606:CRYGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140CTX8|||http://purl.uniprot.org/uniprot/P22914                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Gamma-crystallin S|||In CTRCT20.|||In CTRCT20; unknown pathological significance.|||N-acetylserine|||N-terminal arm|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057565|||http://purl.uniprot.org/annotation/VAR_069797|||http://purl.uniprot.org/annotation/VAR_084793|||http://purl.uniprot.org/annotation/VAR_084794|||http://purl.uniprot.org/annotation/VAR_084795
http://togogenome.org/gene/9606:TRAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13077                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes CASP8-mediated cleavage.|||Cleavage; by CASP8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||MATH|||Nearly abolished ubiquitination; when associated with R-185.|||Nearly abolished ubiquitination; when associated with R-193.|||Phosphoserine|||TNF receptor-associated factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056397|||http://purl.uniprot.org/annotation/VAR_054161|||http://purl.uniprot.org/annotation/VSP_043092
http://togogenome.org/gene/9606:SEC22B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75396                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Longin|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Vesicle-trafficking protein SEC22b|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206770
http://togogenome.org/gene/9606:AIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55008|||http://purl.uniprot.org/uniprot/Q4V347                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Allograft inflammatory factor 1|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2; degenerate|||In isoform 2.|||In isoform 3.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073865|||http://purl.uniprot.org/annotation/VAR_048665|||http://purl.uniprot.org/annotation/VSP_043837|||http://purl.uniprot.org/annotation/VSP_043838|||http://purl.uniprot.org/annotation/VSP_043839
http://togogenome.org/gene/9606:SEMA3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95025                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic residues|||Disordered|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||PSI|||Sema|||Semaphorin-3D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032314|||http://purl.uniprot.org/annotation/VAR_021513
http://togogenome.org/gene/9606:PDCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2J4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Interaction with XIAP|||Loss of acetylation. Increases protein stability.|||N-acetylmethionine|||Phosducin-like protein 3|||Phosphoserine|||Thioredoxin fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163758
http://togogenome.org/gene/9606:SH2D5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV89                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||PID|||SH2|||SH2 domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231581|||http://purl.uniprot.org/annotation/VSP_045938
http://togogenome.org/gene/9606:CD160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95971|||http://purl.uniprot.org/uniprot/Q6FH89                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CD160 antigen|||CD160 antigen, soluble form|||GPI-anchor amidated serine|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014543|||http://purl.uniprot.org/annotation/PRO_0000014544|||http://purl.uniprot.org/annotation/PRO_0000446049|||http://purl.uniprot.org/annotation/PRO_5014310432|||http://purl.uniprot.org/annotation/VAR_027747|||http://purl.uniprot.org/annotation/VSP_060017|||http://purl.uniprot.org/annotation/VSP_060018|||http://purl.uniprot.org/annotation/VSP_060019
http://togogenome.org/gene/9606:HOXB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KR72|||http://purl.uniprot.org/uniprot/Q92826                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Found in prostate cancer samples; unknown pathological significance.|||Homeobox|||Homeobox protein Hox-B13|||In PC; rare variant associated with disease susceptibility.|||Interaction with 5-mCpG DNA|||Interaction with DNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200160|||http://purl.uniprot.org/annotation/VAR_031849|||http://purl.uniprot.org/annotation/VAR_071866|||http://purl.uniprot.org/annotation/VAR_071867|||http://purl.uniprot.org/annotation/VAR_071868|||http://purl.uniprot.org/annotation/VAR_071869|||http://purl.uniprot.org/annotation/VAR_071870|||http://purl.uniprot.org/annotation/VAR_077246
http://togogenome.org/gene/9606:DDX21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR30                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 5 AA repeats|||Basic and acidic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In mutant DEV; loss of helicase activity. Defects in release of P-TEFb from inhibitory 7SK snRNP.|||In mutant SAT; ATPase defective. Defects in release of P-TEFb from inhibitory 7SK snRNP.|||Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-137 and Q-600.|||Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-18 and Q-137.|||Mimics acetylation; impaired ability to resolve R-loops; when associated with Q-18 and Q-600.|||N-acetylmethionine|||N6-acetyllysine|||Nucleolar RNA helicase 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055027|||http://purl.uniprot.org/annotation/VAR_052161|||http://purl.uniprot.org/annotation/VSP_015716
http://togogenome.org/gene/9606:VTI1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UEU0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished binding to CLINT1.|||Abolished binding to CLINT1. Abnormal subcellular localization restricted to late endosomes and lysosomes.|||Abolished binding to CLINT1. Rescued binding to CLINT1 E-146 mutant.|||Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform Short.|||Interaction with CLINT1|||N-acetylalanine|||Normal binding to CLINT1.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Reduced binding to CLINT1.|||Removed|||Vesicle transport through interaction with t-SNAREs homolog 1B|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218228|||http://purl.uniprot.org/annotation/VSP_006753
http://togogenome.org/gene/9606:FAM72C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y354                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM72C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000424443
http://togogenome.org/gene/9606:AURKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GD4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished acetylation by KAT5, leading to impaired chromosome segregation.|||Aurora kinase B|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Leads to loss of kinase activity and severely impairs mitotic progression.|||Mimics acetylation, promoting accurate chromosome segregation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085656|||http://purl.uniprot.org/annotation/VAR_027970|||http://purl.uniprot.org/annotation/VAR_027971|||http://purl.uniprot.org/annotation/VAR_040383|||http://purl.uniprot.org/annotation/VAR_040384|||http://purl.uniprot.org/annotation/VSP_044384|||http://purl.uniprot.org/annotation/VSP_044385|||http://purl.uniprot.org/annotation/VSP_044386|||http://purl.uniprot.org/annotation/VSP_044387|||http://purl.uniprot.org/annotation/VSP_047103
http://togogenome.org/gene/9606:CLDN25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JDP6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Putative claudin-25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395403|||http://purl.uniprot.org/annotation/VAR_063401
http://togogenome.org/gene/9606:NCALD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB70|||http://purl.uniprot.org/uniprot/P61601                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||N-myristoyl glycine|||Neurocalcin-delta|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073782
http://togogenome.org/gene/9606:HDDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK7|||http://purl.uniprot.org/uniprot/Q7Z4H3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  5'-deoxynucleotidase HDDC2|||HD|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311389|||http://purl.uniprot.org/annotation/VAR_037238|||http://purl.uniprot.org/annotation/VSP_029556|||http://purl.uniprot.org/annotation/VSP_029557|||http://purl.uniprot.org/annotation/VSP_029558
http://togogenome.org/gene/9606:GJA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36382|||http://purl.uniprot.org/uniprot/X5D2H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-5 protein|||Gap junction protein cysteine-rich|||Helical|||In ATFB11.|||In ATRST1.|||In ATRST1; somatic.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057819|||http://purl.uniprot.org/annotation/VAR_035013|||http://purl.uniprot.org/annotation/VAR_035014|||http://purl.uniprot.org/annotation/VAR_066249|||http://purl.uniprot.org/annotation/VAR_066250|||http://purl.uniprot.org/annotation/VAR_066251
http://togogenome.org/gene/9606:KIAA0586                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYM5|||http://purl.uniprot.org/uniprot/A0A494C171|||http://purl.uniprot.org/uniprot/B4DYW5|||http://purl.uniprot.org/uniprot/B7Z7W7|||http://purl.uniprot.org/uniprot/Q9BVV6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS23.|||In JBTS23; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein TALPID3|||Required for centrosomal localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050766|||http://purl.uniprot.org/annotation/VAR_069108|||http://purl.uniprot.org/annotation/VAR_074596|||http://purl.uniprot.org/annotation/VAR_076328|||http://purl.uniprot.org/annotation/VSP_040642|||http://purl.uniprot.org/annotation/VSP_040643|||http://purl.uniprot.org/annotation/VSP_046005|||http://purl.uniprot.org/annotation/VSP_046006|||http://purl.uniprot.org/annotation/VSP_046007|||http://purl.uniprot.org/annotation/VSP_046387
http://togogenome.org/gene/9606:METTL13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C4B4C6|||http://purl.uniprot.org/uniprot/Q8N6R0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acts as suppressor of deafness and is associated with normal hearing in individuals homozygous for a deafness-associated mutation in the GAB1 gene.|||Decreased activity.|||Decreased eEF1A lysine methyltransferase activity.|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Loss of activity.|||Loss of eEF1A lysine methyltransferase activity.|||Methyltransferase type 11|||N-acetylmethionine|||No effect on activity.|||Phosphoserine|||eEF1A lysine and N-terminal methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050779|||http://purl.uniprot.org/annotation/VAR_034040|||http://purl.uniprot.org/annotation/VAR_034041|||http://purl.uniprot.org/annotation/VAR_064730|||http://purl.uniprot.org/annotation/VAR_080810|||http://purl.uniprot.org/annotation/VSP_013919|||http://purl.uniprot.org/annotation/VSP_013920|||http://purl.uniprot.org/annotation/VSP_013921|||http://purl.uniprot.org/annotation/VSP_013922
http://togogenome.org/gene/9606:ACOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NK06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished cis-aconitate decarboxylase activity.|||Cis-aconitate decarboxylase|||Disordered|||Does not affect cis-aconitate decarboxylase activity.|||Increased cis-aconitate decarboxylase activity.|||Polar residues|||Strongly reduced cis-aconitate decarboxylase activity.|||Strongly reduced cis-aconitate decarboxylase activity; reduced protein stability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318692|||http://purl.uniprot.org/annotation/VAR_086754|||http://purl.uniprot.org/annotation/VAR_086755|||http://purl.uniprot.org/annotation/VAR_086756|||http://purl.uniprot.org/annotation/VAR_086757|||http://purl.uniprot.org/annotation/VAR_086758|||http://purl.uniprot.org/annotation/VAR_086759|||http://purl.uniprot.org/annotation/VAR_086760|||http://purl.uniprot.org/annotation/VAR_086761
http://togogenome.org/gene/9606:UGT1A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5DSZ7|||http://purl.uniprot.org/uniprot/Q9HAW7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In allele UGT1A7*2 and allele UGT1A7*3.|||In allele UGT1A7*3 and allele UGT1A7*4.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036006|||http://purl.uniprot.org/annotation/PRO_5005143630|||http://purl.uniprot.org/annotation/VAR_015556|||http://purl.uniprot.org/annotation/VAR_015557|||http://purl.uniprot.org/annotation/VAR_015558|||http://purl.uniprot.org/annotation/VAR_052462|||http://purl.uniprot.org/annotation/VSP_053963
http://togogenome.org/gene/9606:F9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00740                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Activation peptide|||Charge relay system|||Cleavage; by factor XIa|||Coagulation factor IX|||Coagulation factor IXa heavy chain|||Coagulation factor IXa light chain|||EGF-like 1; calcium-binding|||EGF-like 2|||Gla|||In HEMB.|||In HEMB; Bergamo; increased protein abundance; loss of function in blood coagulation.|||In HEMB; Iran.|||In HEMB; Italy.|||In HEMB; Mechtal.|||In HEMB; Milano.|||In HEMB; Monschau.|||In HEMB; Schmallenberg.|||In HEMB; Varel.|||In HEMB; decreased protein abundance; decreased function in blood coagulation.|||In HEMB; decreased protein abundance; loss of function in blood coagulation.|||In HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4.|||In HEMB; mild.|||In HEMB; mild; Cardiff-2.|||In HEMB; mild; Durham.|||In HEMB; mild; Hong Kong-11.|||In HEMB; moderate to severe.|||In HEMB; moderate.|||In HEMB; moderate; Alabama.|||In HEMB; moderate; Albuquerque, Cardiff-1.|||In HEMB; moderate; Chapel-Hill, Chicago-2.|||In HEMB; moderate; HB130.|||In HEMB; moderate; decreased protein abundance; decreased function in blood coagulation.|||In HEMB; moderately severe.|||In HEMB; moderately severe; Long Beach, Los Angeles and Vancouver.|||In HEMB; moderately severe; Niigata.|||In HEMB; reduced protein abundance; loss of function in blood coagulation.|||In HEMB; severe.|||In HEMB; severe; Amagasaki.|||In HEMB; severe; Angers.|||In HEMB; severe; Barcelos.|||In HEMB; severe; Basel.|||In HEMB; severe; Bendorf, Beuten, Gleiwitz; impairs removal of propeptide.|||In HEMB; severe; Boxtel, Heiden, Lienen; impairs removal of propeptide.|||In HEMB; severe; Calgary-16.|||In HEMB; severe; Cambridge; impaired processing of the propeptide; impaired gamma-carboxylation; decreased protein abundance; loss of function in blood coagulation.|||In HEMB; severe; Chongqing; Gla mutant.|||In HEMB; severe; Gla mutant.|||In HEMB; severe; HB151; Gla mutant.|||In HEMB; severe; Hilo and Novara; no effect on protein abundance; loss of function in blood coagulation.|||In HEMB; severe; Hong Kong-1.|||In HEMB; severe; Iceland-1, London and Sesimbra.|||In HEMB; severe; Kashihara.|||In HEMB; severe; Los Angeles-4.|||In HEMB; severe; Lousada.|||In HEMB; severe; Luanda.|||In HEMB; severe; Madrid.|||In HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho.|||In HEMB; severe; Nagoya-4; Gla mutant.|||In HEMB; severe; New London.|||In HEMB; severe; Oxford-B2; Gla mutant.|||In HEMB; severe; Oxford-D1.|||In HEMB; severe; San Dimas, Oxford-3, Strasbourg-2; impairs removal of propeptide.|||In HEMB; severe; Seattle E.|||In HEMB; severe; Seattle-3; Gla mutant.|||In HEMB; severe; UK 22.|||In HEMB; severe; decreased protein abundance; loss of function in blood coagulation.|||In HEMB; unknown pathological significance; decreased protein abundance; decreased function in blood coagulation.|||In HEMB; unknown pathological significance; no effect on protein abundance; loss of function in blood coagulation.|||In THPH8; factor IXPadua; higher specific activity than wild-type.|||In WARFS; 2.5-fold decreased in the EC(50) for warfarin.|||In WARFS; reduced affinity of the glutamate carboxylase for the factor IX precursor; 4.4-fold decreased in the EC(50) for warfarin.|||In isoform 2.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) serine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; alternate|||O-linked (Glc...) serine|||Peptidase S1|||Phosphoserine|||Phosphothreonine; alternate|||Strongly decreases enzyme activity with a synthetic peptide substrate.|||Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; A-365 and T-391.|||Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; T-311 and A-365.|||Strongly increases enzyme activity with a synthetic peptide substrate; when associated with T-311; A-365 and T-391.|||Sulfotyrosine|||via 4-carboxyglutamate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000009|||http://purl.uniprot.org/annotation/CAR_000010|||http://purl.uniprot.org/annotation/PRO_0000027755|||http://purl.uniprot.org/annotation/PRO_0000027756|||http://purl.uniprot.org/annotation/PRO_0000027757|||http://purl.uniprot.org/annotation/PRO_0000027758|||http://purl.uniprot.org/annotation/PRO_0000027759|||http://purl.uniprot.org/annotation/VAR_006520|||http://purl.uniprot.org/annotation/VAR_006521|||http://purl.uniprot.org/annotation/VAR_006522|||http://purl.uniprot.org/annotation/VAR_006523|||http://purl.uniprot.org/annotation/VAR_006524|||http://purl.uniprot.org/annotation/VAR_006525|||http://purl.uniprot.org/annotation/VAR_006526|||http://purl.uniprot.org/annotation/VAR_006527|||http://purl.uniprot.org/annotation/VAR_006528|||http://purl.uniprot.org/annotation/VAR_006529|||http://purl.uniprot.org/annotation/VAR_006530|||http://purl.uniprot.org/annotation/VAR_006531|||http://purl.uniprot.org/annotation/VAR_006532|||http://purl.uniprot.org/annotation/VAR_006533|||http://purl.uniprot.org/annotation/VAR_006534|||http://purl.uniprot.org/annotation/VAR_006535|||http://purl.uniprot.org/annotation/VAR_006536|||http://purl.uniprot.org/annotation/VAR_006537|||http://purl.uniprot.org/annotation/VAR_006538|||http://purl.uniprot.org/annotation/VAR_006539|||http://purl.uniprot.org/annotation/VAR_006540|||http://purl.uniprot.org/annotation/VAR_006541|||http://purl.uniprot.org/annotation/VAR_006542|||http://purl.uniprot.org/annotation/VAR_006543|||http://purl.uniprot.org/annotation/VAR_006544|||http://purl.uniprot.org/annotation/VAR_006545|||http://purl.uniprot.org/annotation/VAR_006546|||http://purl.uniprot.org/annotation/VAR_006547|||http://purl.uniprot.org/annotation/VAR_006548|||http://purl.uniprot.org/annotation/VAR_006549|||http://purl.uniprot.org/annotation/VAR_006550|||http://purl.uniprot.org/annotation/VAR_006551|||http://purl.uniprot.org/annotation/VAR_006552|||http://purl.uniprot.org/annotation/VAR_006553|||http://purl.uniprot.org/annotation/VAR_006554|||http://purl.uniprot.org/annotation/VAR_006555|||http://purl.uniprot.org/annotation/VAR_006556|||http://purl.uniprot.org/annotation/VAR_006557|||http://purl.uniprot.org/annotation/VAR_006558|||http://purl.uniprot.org/annotation/VAR_006559|||http://purl.uniprot.org/annotation/VAR_006560|||http://purl.uniprot.org/annotation/VAR_006561|||http://purl.uniprot.org/annotation/VAR_006562|||http://purl.uniprot.org/annotation/VAR_006563|||http://purl.uniprot.org/annotation/VAR_006564|||http://purl.uniprot.org/annotation/VAR_006565|||http://purl.uniprot.org/annotation/VAR_006566|||http://purl.uniprot.org/annotation/VAR_006567|||http://purl.uniprot.org/annotation/VAR_006568|||http://purl.uniprot.org/annotation/VAR_006569|||http://purl.uniprot.org/annotation/VAR_006570|||http://purl.uniprot.org/annotation/VAR_006571|||http://purl.uniprot.org/annotation/VAR_006572|||http://purl.uniprot.org/annotation/VAR_006573|||http://purl.uniprot.org/annotation/VAR_006574|||http://purl.uniprot.org/annotation/VAR_006575|||http://purl.uniprot.org/annotation/VAR_006576|||http://purl.uniprot.org/annotation/VAR_006577|||http://purl.uniprot.org/annotation/VAR_006578|||http://purl.uniprot.org/annotation/VAR_006579|||http://purl.uniprot.org/annotation/VAR_006580|||http://purl.uniprot.org/annotation/VAR_006581|||http://purl.uniprot.org/annotation/VAR_006582|||http://purl.uniprot.org/annotation/VAR_006583|||http://purl.uniprot.org/annotation/VAR_006584|||http://purl.uniprot.org/annotation/VAR_006585|||http://purl.uniprot.org/annotation/VAR_006586|||http://purl.uniprot.org/annotation/VAR_006587|||http://purl.uniprot.org/annotation/VAR_006588|||http://purl.uniprot.org/annotation/VAR_006589|||http://purl.uniprot.org/annotation/VAR_006590|||http://purl.uniprot.org/annotation/VAR_006591|||http://purl.uniprot.org/annotation/VAR_006592|||http://purl.uniprot.org/annotation/VAR_006593|||http://purl.uniprot.org/annotation/VAR_006594|||http://purl.uniprot.org/annotation/VAR_006595|||http://purl.uniprot.org/annotation/VAR_006596|||http://purl.uniprot.org/annotation/VAR_006597|||http://purl.uniprot.org/annotation/VAR_006598|||http://purl.uniprot.org/annotation/VAR_006599|||http://purl.uniprot.org/annotation/VAR_006600|||http://purl.uniprot.org/annotation/VAR_006601|||http://purl.uniprot.org/annotation/VAR_006602|||http://purl.uniprot.org/annotation/VAR_006603|||http://purl.uniprot.org/annotation/VAR_006604|||http://purl.uniprot.org/annotation/VAR_006605|||http://purl.uniprot.org/annotation/VAR_006606|||http://purl.uniprot.org/annotation/VAR_006607|||http://purl.uniprot.org/annotation/VAR_006608|||http://purl.uniprot.org/annotation/VAR_006609|||http://purl.uniprot.org/annotation/VAR_006610|||http://purl.uniprot.org/annotation/VAR_006611|||http://purl.uniprot.org/annotation/VAR_006612|||http://purl.uniprot.org/annotation/VAR_006613|||http://purl.uniprot.org/annotation/VAR_006614|||http://purl.uniprot.org/annotation/VAR_006615|||http://purl.uniprot.org/annotation/VAR_006616|||http://purl.uniprot.org/annotation/VAR_006617|||http://purl.uniprot.org/annotation/VAR_006618|||http://purl.uniprot.org/annotation/VAR_006619|||http://purl.uniprot.org/annotation/VAR_006620|||http://purl.uniprot.org/annotation/VAR_006621|||http://purl.uniprot.org/annotation/VAR_011773|||http://purl.uniprot.org/annotation/VAR_014308|||http://purl.uniprot.org/annotation/VAR_017307|||http://purl.uniprot.org/annotation/VAR_017308|||http://purl.uniprot.org/annotation/VAR_017309|||http://purl.uniprot.org/annotation/VAR_017310|||http://purl.uniprot.org/annotation/VAR_017311|||http://purl.uniprot.org/annotation/VAR_017312|||http://purl.uniprot.org/annotation/VAR_017313|||http://purl.uniprot.org/annotation/VAR_017314|||http://purl.uniprot.org/annotation/VAR_017315|||http://purl.uniprot.org/annotation/VAR_017316|||http://purl.uniprot.org/annotation/VAR_017317|||http://purl.uniprot.org/annotation/VAR_017318|||http://purl.uniprot.org/annotation/VAR_017319|||http://purl.uniprot.org/annotation/VAR_017320|||http://purl.uniprot.org/annotation/VAR_017321|||http://purl.uniprot.org/annotation/VAR_017322|||http://purl.uniprot.org/annotation/VAR_017323|||http://purl.uniprot.org/annotation/VAR_017324|||http://purl.uniprot.org/annotation/VAR_017343|||http://purl.uniprot.org/annotation/VAR_017344|||http://purl.uniprot.org/annotation/VAR_017345|||http://purl.uniprot.org/annotation/VAR_017346|||http://purl.uniprot.org/annotation/VAR_017347|||http://purl.uniprot.org/annotation/VAR_017348|||http://purl.uniprot.org/annotation/VAR_017349|||http://purl.uniprot.org/annotation/VAR_017350|||http://purl.uniprot.org/annotation/VAR_017351|||http://purl.uniprot.org/annotation/VAR_017352|||http://purl.uniprot.org/annotation/VAR_017353|||http://purl.uniprot.org/annotation/VAR_017354|||http://purl.uniprot.org/annotation/VAR_017355|||http://purl.uniprot.org/annotation/VAR_017356|||http://purl.uniprot.org/annotation/VAR_017357|||http://purl.uniprot.org/annotation/VAR_017358|||http://purl.uniprot.org/annotation/VAR_017359|||http://purl.uniprot.org/annotation/VAR_017360|||http://purl.uniprot.org/annotation/VAR_017361|||http://purl.uniprot.org/annotation/VAR_017362|||http://purl.uniprot.org/annotation/VAR_017363|||http://purl.uniprot.org/annotation/VAR_017364|||http://purl.uniprot.org/annotation/VAR_017365|||http://purl.uniprot.org/annotation/VAR_062999|||http://purl.uniprot.org/annotation/VAR_073975|||http://purl.uniprot.org/annotation/VAR_073976|||http://purl.uniprot.org/annotation/VAR_073977|||http://purl.uniprot.org/annotation/VAR_073978|||http://purl.uniprot.org/annotation/VAR_073979|||http://purl.uniprot.org/annotation/VAR_073980|||http://purl.uniprot.org/annotation/VAR_073981|||http://purl.uniprot.org/annotation/VAR_073982|||http://purl.uniprot.org/annotation/VAR_073983|||http://purl.uniprot.org/annotation/VAR_083981|||http://purl.uniprot.org/annotation/VSP_047689
http://togogenome.org/gene/9606:FAM209A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JX71                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Protein FAM209A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264155|||http://purl.uniprot.org/annotation/VAR_029621|||http://purl.uniprot.org/annotation/VAR_029622|||http://purl.uniprot.org/annotation/VAR_029623|||http://purl.uniprot.org/annotation/VAR_029624|||http://purl.uniprot.org/annotation/VAR_033761
http://togogenome.org/gene/9606:ZNF551                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z340                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Phosphoserine|||Zinc finger protein 551                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047646|||http://purl.uniprot.org/annotation/VAR_028077|||http://purl.uniprot.org/annotation/VAR_028078|||http://purl.uniprot.org/annotation/VSP_014799|||http://purl.uniprot.org/annotation/VSP_014800
http://togogenome.org/gene/9606:CD74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04233                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form a CD74-ROS1 fusion protein|||Class-II-associated invariant chain peptide|||Cytoplasmic|||Decreases inhibition of Ebola virus infection.|||Disordered|||Extracellular|||HLA class II histocompatibility antigen gamma chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 3.|||In isoform p35 and isoform p33.|||In isoform p41 and isoform p33.|||N-linked (GlcNAc...) asparagine|||No effect on inhibition of Ebola virus infection.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Required for interaction with CTSL|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067954|||http://purl.uniprot.org/annotation/PRO_0000448886|||http://purl.uniprot.org/annotation/VSP_005331|||http://purl.uniprot.org/annotation/VSP_037869|||http://purl.uniprot.org/annotation/VSP_037870|||http://purl.uniprot.org/annotation/VSP_060904
http://togogenome.org/gene/9606:RBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQT0|||http://purl.uniprot.org/uniprot/P09455                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Decreases cellular retinol uptake and impairs retinol storage.|||Disordered|||Important for interaction with STRA6|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake.|||Omega-N-methylarginine|||Retinol-binding protein 1|||Strongly decreased affinity for retinol. Further decrease in affinity for retinol; when associated with L-109.|||Strongly decreased affinity for retinol. Further decrease in for retinol; when associated with L-41.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067392|||http://purl.uniprot.org/annotation/VSP_046201|||http://purl.uniprot.org/annotation/VSP_046202|||http://purl.uniprot.org/annotation/VSP_046203
http://togogenome.org/gene/9606:SYNPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBG9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X approximate repeats|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Synaptoporin|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179157|||http://purl.uniprot.org/annotation/VSP_046199
http://togogenome.org/gene/9606:CILP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUL8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Cartilage intermediate layer protein 2|||Cartilage intermediate layer protein 2 C1|||Cartilage intermediate layer protein 2 C2|||Disordered|||Ig-like C2-type|||N-linked (GlcNAc...) asparagine|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014678|||http://purl.uniprot.org/annotation/PRO_0000014679|||http://purl.uniprot.org/annotation/PRO_0000014680
http://togogenome.org/gene/9606:C11orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A22                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein C11orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263609|||http://purl.uniprot.org/annotation/VAR_029587
http://togogenome.org/gene/9606:PHLPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60346                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with NHERF1|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of function in vivo, but does not abolishes intrinsic phosphatase activity.|||N-acetylmethionine|||PDZ-binding; required for interaction with NHERF1|||PH|||PH domain leucine-rich repeat-containing protein phosphatase 1|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057781|||http://purl.uniprot.org/annotation/VAR_056725|||http://purl.uniprot.org/annotation/VSP_057809
http://togogenome.org/gene/9606:GLDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23378                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Glycine dehydrogenase (decarboxylating), mitochondrial|||In NKH.|||In NKH; common mutation in Finland.|||In NKH; decreased GCSP-protein glycine exchange activity; no effect on abundance.|||In NKH; decreased glycine catabolic process; changed localization to the mitochondria; also expressed diffusely throughout the cytosol; decreased abundance.|||In NKH; decreased glycine catabolic process; decreased abundance.|||In NKH; loss of GCSP-protein glycine exchange activity; no effect on abundance.|||In NKH; loss of glycine catabolic process; decreased abundance.|||In NKH; loss of glycine catabolic process; loss of expression.|||In one non-ketotic hyperglycinemia patient.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010740|||http://purl.uniprot.org/annotation/VAR_004979|||http://purl.uniprot.org/annotation/VAR_009939|||http://purl.uniprot.org/annotation/VAR_016849|||http://purl.uniprot.org/annotation/VAR_016850|||http://purl.uniprot.org/annotation/VAR_016851|||http://purl.uniprot.org/annotation/VAR_078776|||http://purl.uniprot.org/annotation/VAR_078777|||http://purl.uniprot.org/annotation/VAR_078778|||http://purl.uniprot.org/annotation/VAR_078779|||http://purl.uniprot.org/annotation/VAR_078780|||http://purl.uniprot.org/annotation/VAR_078781|||http://purl.uniprot.org/annotation/VAR_078782|||http://purl.uniprot.org/annotation/VAR_078783|||http://purl.uniprot.org/annotation/VAR_078784|||http://purl.uniprot.org/annotation/VAR_078785|||http://purl.uniprot.org/annotation/VAR_078786|||http://purl.uniprot.org/annotation/VAR_078787|||http://purl.uniprot.org/annotation/VAR_078788|||http://purl.uniprot.org/annotation/VAR_078789|||http://purl.uniprot.org/annotation/VAR_078790|||http://purl.uniprot.org/annotation/VAR_078791|||http://purl.uniprot.org/annotation/VAR_078792|||http://purl.uniprot.org/annotation/VAR_078793|||http://purl.uniprot.org/annotation/VAR_079313
http://togogenome.org/gene/9606:COX5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20674                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 5A, mitochondrial|||In MC4DN20; decreased protein abundance in patient fibroblasts; decreased proteins abundance of mitochondrial respiratory chain complex IV in patient fibroblasts; no effect on respiratory chain complex IV assembly in patient fibroblasts; increased protein abundance of S1 complex IV intermediate in patient fibroblasts.|||Mitochondrion|||N6-acetyllysine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006100|||http://purl.uniprot.org/annotation/VAR_078264
http://togogenome.org/gene/9606:NLRP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59045                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||NACHT|||NACHT, LRR and PYD domains-containing protein 11|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080898|||http://purl.uniprot.org/annotation/VAR_057710|||http://purl.uniprot.org/annotation/VAR_060212|||http://purl.uniprot.org/annotation/VAR_062141|||http://purl.uniprot.org/annotation/VSP_007068|||http://purl.uniprot.org/annotation/VSP_038210
http://togogenome.org/gene/9606:BARD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ19|||http://purl.uniprot.org/uniprot/A0AVN2|||http://purl.uniprot.org/uniprot/C9IYG1|||http://purl.uniprot.org/uniprot/F6MDI0|||http://purl.uniprot.org/uniprot/F6MDI1|||http://purl.uniprot.org/uniprot/F6MDI2|||http://purl.uniprot.org/uniprot/Q99728                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4; degenerate|||BRCA1-associated RING domain protein 1|||BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||Disordered|||Flexible linker|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In an ovarian clear cell adenocarcinoma.|||In an uterine cancer sample; somatic mutation.|||In isoform alpha.|||In isoform beta.|||In isoform gamma.|||Interaction with BRCA1|||Phosphoserine|||Phosphothreonine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055819|||http://purl.uniprot.org/annotation/VAR_010354|||http://purl.uniprot.org/annotation/VAR_010355|||http://purl.uniprot.org/annotation/VAR_010356|||http://purl.uniprot.org/annotation/VAR_010357|||http://purl.uniprot.org/annotation/VAR_010358|||http://purl.uniprot.org/annotation/VAR_010359|||http://purl.uniprot.org/annotation/VAR_010360|||http://purl.uniprot.org/annotation/VAR_010361|||http://purl.uniprot.org/annotation/VAR_020109|||http://purl.uniprot.org/annotation/VAR_024611|||http://purl.uniprot.org/annotation/VAR_028309|||http://purl.uniprot.org/annotation/VAR_038371|||http://purl.uniprot.org/annotation/VAR_038372|||http://purl.uniprot.org/annotation/VSP_055874|||http://purl.uniprot.org/annotation/VSP_055875|||http://purl.uniprot.org/annotation/VSP_055876|||http://purl.uniprot.org/annotation/VSP_055877|||http://purl.uniprot.org/annotation/VSP_055878
http://togogenome.org/gene/9606:POTEB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JP26                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||POTE ankyrin domain family member B3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432398|||http://purl.uniprot.org/annotation/VAR_019915|||http://purl.uniprot.org/annotation/VAR_019919|||http://purl.uniprot.org/annotation/VAR_019921|||http://purl.uniprot.org/annotation/VAR_019922|||http://purl.uniprot.org/annotation/VAR_059119|||http://purl.uniprot.org/annotation/VAR_080181|||http://purl.uniprot.org/annotation/VAR_080182|||http://purl.uniprot.org/annotation/VAR_080183|||http://purl.uniprot.org/annotation/VSP_059380|||http://purl.uniprot.org/annotation/VSP_059381|||http://purl.uniprot.org/annotation/VSP_059382
http://togogenome.org/gene/9606:MGARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||Mitochondrial intermembrane|||Polar residues|||Protein MGARP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318764|||http://purl.uniprot.org/annotation/VAR_051256
http://togogenome.org/gene/9606:SLC6A18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N87                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Inactive sodium-dependent neutral amino acid transporter B(0)AT3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214806|||http://purl.uniprot.org/annotation/VAR_027975|||http://purl.uniprot.org/annotation/VAR_027976|||http://purl.uniprot.org/annotation/VAR_027977|||http://purl.uniprot.org/annotation/VAR_057210|||http://purl.uniprot.org/annotation/VAR_064796|||http://purl.uniprot.org/annotation/VAR_064797
http://togogenome.org/gene/9606:CIAO2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5X1                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosolic iron-sulfur assembly component 2A|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212689|||http://purl.uniprot.org/annotation/VSP_042683
http://togogenome.org/gene/9606:TNFSF13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR02|||http://purl.uniprot.org/uniprot/O75888|||http://purl.uniprot.org/uniprot/Q2QBA2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes proteolytic processing.|||Cleavage; by furin|||Disordered|||Helical|||In isoform 4.|||In isoform 5.|||In isoform Beta.|||In isoform Gamma.|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034524|||http://purl.uniprot.org/annotation/PRO_0000034525|||http://purl.uniprot.org/annotation/VAR_052586|||http://purl.uniprot.org/annotation/VAR_052587|||http://purl.uniprot.org/annotation/VSP_006450|||http://purl.uniprot.org/annotation/VSP_006451|||http://purl.uniprot.org/annotation/VSP_043154|||http://purl.uniprot.org/annotation/VSP_046725|||http://purl.uniprot.org/annotation/VSP_046726
http://togogenome.org/gene/9606:SMS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52788                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  100,000-fold decrease in catalytic efficiency.|||200,000-fold decrease in catalytic efficiency.|||800-fold decrease in catalytic efficiency.|||In MRXSSR.|||In MRXSSR; a reduced spermine/spermidine ratio is observed in patient lymphoblastoid cells consistent with impaired spermine biosynthesis.|||In MRXSSR; mild disease phenotype; a reduced spermine/spermidine ratio is observed in patient lymphoblastoid cells consistent with impaired spermine biosynthesis.|||In isoform 2.|||N-acetylalanine|||PABS|||Phosphoserine|||Proton acceptor|||Removed|||Spermine synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156538|||http://purl.uniprot.org/annotation/VAR_071048|||http://purl.uniprot.org/annotation/VAR_072748|||http://purl.uniprot.org/annotation/VAR_076449|||http://purl.uniprot.org/annotation/VAR_076450|||http://purl.uniprot.org/annotation/VAR_076451|||http://purl.uniprot.org/annotation/VAR_076452|||http://purl.uniprot.org/annotation/VSP_034406
http://togogenome.org/gene/9606:JTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76095                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Protein JTB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021535|||http://purl.uniprot.org/annotation/VAR_033994|||http://purl.uniprot.org/annotation/VSP_041400
http://togogenome.org/gene/9606:RASIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U651|||http://purl.uniprot.org/uniprot/Q7L251|||http://purl.uniprot.org/uniprot/Q8IUR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dilute|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Ras-associating|||Ras-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097163|||http://purl.uniprot.org/annotation/VAR_051302
http://togogenome.org/gene/9606:MSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5Y2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).|||Acidic residues|||Basic and acidic residues|||Diminishes DNA-binding.|||Diminishes DNA-binding; when associated with A-55.|||Diminishes DNA-binding; when associated with A-65.|||Diminishes interaction with histone H4 monomethylated at 'Lys-20'(H4K20Me1).|||Disordered|||In MRXSBA.|||In MRXSBA; loss of interaction with MOF and MSL1.|||In MRXSBA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MRG|||Male-specific lethal 3 homolog|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for the histone acetyltransferase activity of the MSL complex|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080247|||http://purl.uniprot.org/annotation/VAR_048732|||http://purl.uniprot.org/annotation/VAR_069061|||http://purl.uniprot.org/annotation/VAR_082955|||http://purl.uniprot.org/annotation/VAR_082956|||http://purl.uniprot.org/annotation/VAR_082957|||http://purl.uniprot.org/annotation/VAR_082958|||http://purl.uniprot.org/annotation/VSP_007636|||http://purl.uniprot.org/annotation/VSP_007637|||http://purl.uniprot.org/annotation/VSP_043342|||http://purl.uniprot.org/annotation/VSP_045652|||http://purl.uniprot.org/annotation/VSP_045653|||http://purl.uniprot.org/annotation/VSP_045654|||http://purl.uniprot.org/annotation/VSP_055376|||http://purl.uniprot.org/annotation/VSP_055377
http://togogenome.org/gene/9606:DNAJA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM81|||http://purl.uniprot.org/uniprot/Q53G26|||http://purl.uniprot.org/uniprot/Q59E88|||http://purl.uniprot.org/uniprot/Q96EY1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn|||Zinc Finger                                                                                  ^@                                                                                  CR-type|||CXXCXGXG motif|||Disordered|||DnaJ homolog subfamily A member 3, mitochondrial|||In isoform 2 and isoform 3.|||In isoform 3.|||J|||Loss of modulation of apoptosis.|||Mitochondrion|||N6-acetyllysine|||Omega-N-methylarginine; by CARM1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007256|||http://purl.uniprot.org/annotation/VAR_027965|||http://purl.uniprot.org/annotation/VSP_007425|||http://purl.uniprot.org/annotation/VSP_007426|||http://purl.uniprot.org/annotation/VSP_055728
http://togogenome.org/gene/9606:BORA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV86|||http://purl.uniprot.org/uniprot/Q6PGQ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein aurora borealis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273205|||http://purl.uniprot.org/annotation/VAR_030110|||http://purl.uniprot.org/annotation/VAR_030111|||http://purl.uniprot.org/annotation/VSP_055543
http://togogenome.org/gene/9606:PHOSPHO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCD6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  Nucleophile|||Proton donor|||Pyridoxal phosphate phosphatase PHOSPHO2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068833|||http://purl.uniprot.org/annotation/VAR_062092
http://togogenome.org/gene/9606:SLITRK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94991                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||SLIT and NTRK-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032681|||http://purl.uniprot.org/annotation/VSP_056676|||http://purl.uniprot.org/annotation/VSP_056677
http://togogenome.org/gene/9606:KCNJ11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HHV7|||http://purl.uniprot.org/uniprot/B2RC52|||http://purl.uniprot.org/uniprot/Q14654                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 11|||Cytoplasmic|||Displays gain of function; increased open state stability, reduced ATP sensitivity and increased channel activity; almost completely abolishes high affinity sensitivity to glibenclamide, an inhibitor of ATP-sensitive potassium channels.|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In HHF2.|||In HHF2; does neither affect channel expression nor channel response to MgADP.|||In HHF2; impairs trafficking and abolishes channel function.|||In HHF2; impairs trafficking of the mutant channel.|||In HHF2; prevents the ER export and surface expression of the channel.|||In MODY13.|||In NIDDM.|||In NIDDM; Afro-Caribbean.|||In PNDM2.|||In PNDM2; ability of ATP to block mutant channels greatly reduced.|||In PNDM2; alters gating characteristics; decreases sensitivity to inhibition by ATP and increases intrinsic open probability.|||In PNDM2; decreased inhibition by ATP; enhanced activation by Mg(2+); increased current.|||In PNDM2; has severely impaired sensitivity to ATP and markedly increases open channel probability.|||In PNDM2; individual also diagnosed with West syndrome.|||In PNDM2; the patient also carries L-64 in cis; displays gain of function; increases the intrinsic channel open probability and decreases sensitivity toward ATP inhibition; variant L-64 associated in cis is thought to ameliorate the effect of the Y-60 mutation on the channel ATP sensitivity.|||In PNDM2; unknown pathological significance; the patient also carries Y-60 in cis; only subtle effects, if any, on channel ATP sensitivity; thought to attenuate the deleterious effect of the Y-60 mutation associated in cis on the channel ATP sensitivity.|||In PNDM2; with neurologic features.|||In PNDM2; with neurologic features; produces larger current and more change in ATP sensitivity than mutation associated with mild disease C-201.|||In PNDM2; with neurologic features; produces larger current and more change in ATP sensitivity than mutation associated with mild disease C-201; decreases ATP sensitivity indirectly by favoring the open conformation of the channel.|||In PNDM2; with neurologic features; produces smaller current and less change in ATP sensitivity than mutations associated with severe disease R-52 and G-59.|||In TNDM3; increased spontaneous open probability; reduced ATP sensitivity; reduced expression at the cell surface of the functional ATP-sensitive form.|||In TNDM3; reduction in the sensitivity to ATP when compared with wild-type.|||In isoform 2.|||Inward rectifier potassium channel C-terminal|||Phosphoserine; by MAPK1|||Phosphothreonine; by MAPK1|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154957|||http://purl.uniprot.org/annotation/VAR_001557|||http://purl.uniprot.org/annotation/VAR_008659|||http://purl.uniprot.org/annotation/VAR_008660|||http://purl.uniprot.org/annotation/VAR_008661|||http://purl.uniprot.org/annotation/VAR_008662|||http://purl.uniprot.org/annotation/VAR_008663|||http://purl.uniprot.org/annotation/VAR_008664|||http://purl.uniprot.org/annotation/VAR_008665|||http://purl.uniprot.org/annotation/VAR_014929|||http://purl.uniprot.org/annotation/VAR_026498|||http://purl.uniprot.org/annotation/VAR_026499|||http://purl.uniprot.org/annotation/VAR_026500|||http://purl.uniprot.org/annotation/VAR_026501|||http://purl.uniprot.org/annotation/VAR_026502|||http://purl.uniprot.org/annotation/VAR_026503|||http://purl.uniprot.org/annotation/VAR_026504|||http://purl.uniprot.org/annotation/VAR_026505|||http://purl.uniprot.org/annotation/VAR_026506|||http://purl.uniprot.org/annotation/VAR_026507|||http://purl.uniprot.org/annotation/VAR_026508|||http://purl.uniprot.org/annotation/VAR_026509|||http://purl.uniprot.org/annotation/VAR_026510|||http://purl.uniprot.org/annotation/VAR_026511|||http://purl.uniprot.org/annotation/VAR_026512|||http://purl.uniprot.org/annotation/VAR_026513|||http://purl.uniprot.org/annotation/VAR_026514|||http://purl.uniprot.org/annotation/VAR_026515|||http://purl.uniprot.org/annotation/VAR_026516|||http://purl.uniprot.org/annotation/VAR_026517|||http://purl.uniprot.org/annotation/VAR_031329|||http://purl.uniprot.org/annotation/VAR_031330|||http://purl.uniprot.org/annotation/VAR_031331|||http://purl.uniprot.org/annotation/VAR_031332|||http://purl.uniprot.org/annotation/VAR_031333|||http://purl.uniprot.org/annotation/VAR_031334|||http://purl.uniprot.org/annotation/VAR_031335|||http://purl.uniprot.org/annotation/VAR_031336|||http://purl.uniprot.org/annotation/VAR_031337|||http://purl.uniprot.org/annotation/VAR_031338|||http://purl.uniprot.org/annotation/VAR_031339|||http://purl.uniprot.org/annotation/VAR_031340|||http://purl.uniprot.org/annotation/VAR_031341|||http://purl.uniprot.org/annotation/VAR_031342|||http://purl.uniprot.org/annotation/VAR_031343|||http://purl.uniprot.org/annotation/VAR_031344|||http://purl.uniprot.org/annotation/VAR_031345|||http://purl.uniprot.org/annotation/VAR_031346|||http://purl.uniprot.org/annotation/VAR_031347|||http://purl.uniprot.org/annotation/VAR_031348|||http://purl.uniprot.org/annotation/VAR_055978|||http://purl.uniprot.org/annotation/VAR_073681|||http://purl.uniprot.org/annotation/VAR_073682|||http://purl.uniprot.org/annotation/VAR_073683|||http://purl.uniprot.org/annotation/VAR_073684|||http://purl.uniprot.org/annotation/VAR_073685|||http://purl.uniprot.org/annotation/VAR_073686|||http://purl.uniprot.org/annotation/VAR_073687|||http://purl.uniprot.org/annotation/VSP_045270
http://togogenome.org/gene/9606:EWSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01844                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||31 X approximate tandem repeats|||4|||5|||6|||7|||8|||9|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Asymmetric dimethylarginine; alternate; by PRMT8|||Asymmetric dimethylarginine; by PRMT8|||Basic and acidic residues|||Breakpoint for insertion to form EWSR1-FEV fusion protein|||Breakpoint for translocation to form chimeric EWSR1/ATF1 protein|||Cytoplasmic localization.|||Disordered|||EAD (Gln/Pro/Thr-rich)|||IQ|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform EWS-B.|||N6-acetyllysine|||No effect on nuclear targeting.|||Nuclear localization signal|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; alternate; by PRMT8|||Phosphoserine; by PKC|||Polar residues|||Pro residues|||RNA-binding protein EWS|||RRM|||RanBP2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081586|||http://purl.uniprot.org/annotation/VSP_005793|||http://purl.uniprot.org/annotation/VSP_043451|||http://purl.uniprot.org/annotation/VSP_043452|||http://purl.uniprot.org/annotation/VSP_043453|||http://purl.uniprot.org/annotation/VSP_043454|||http://purl.uniprot.org/annotation/VSP_045412
http://togogenome.org/gene/9606:SYPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0R1|||http://purl.uniprot.org/uniprot/Q16563                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||MARVEL|||N-linked (GlcNAc...) asparagine|||Removed|||Synaptophysin-like protein 1|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179164|||http://purl.uniprot.org/annotation/VSP_008557
http://togogenome.org/gene/9606:CTPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1E0|||http://purl.uniprot.org/uniprot/P17812                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CTP synthase 1|||CTP synthase N-terminal|||Disordered|||For GATase activity|||Glutamine amidotransferase|||Glutamine amidotransferase type-1|||In isoform 2.|||Localizes to cystolic filament structures.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138275|||http://purl.uniprot.org/annotation/VAR_027055|||http://purl.uniprot.org/annotation/VSP_055827
http://togogenome.org/gene/9606:LRRC3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJW4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 3C|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345962
http://togogenome.org/gene/9606:GCAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K228|||http://purl.uniprot.org/uniprot/O75600                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial|||Aminotransferase class I/classII|||In isoform 2.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001246|||http://purl.uniprot.org/annotation/VAR_015094|||http://purl.uniprot.org/annotation/VAR_048229|||http://purl.uniprot.org/annotation/VSP_044607
http://togogenome.org/gene/9606:PTPN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29350|||http://purl.uniprot.org/uniprot/Q53XS4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LYN|||SH2|||SH2 1|||SH2 2|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094758|||http://purl.uniprot.org/annotation/VSP_005129|||http://purl.uniprot.org/annotation/VSP_005130|||http://purl.uniprot.org/annotation/VSP_007775|||http://purl.uniprot.org/annotation/VSP_044447
http://togogenome.org/gene/9606:RSPO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVP3|||http://purl.uniprot.org/uniprot/Q6UXX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||FU|||In HHRRD; loss of LGR5-, RNF43- and ZNRF3-binding; decreased ability to amplify WNT3A signaling.|||In TETAMS2.|||In TETAMS2; loss of LGR5-, RNF43- and ZNRF3-binding; complete loss of amplification of WNT3A signaling.|||In isoform 2.|||In isoform 3.|||Loss of LGR5-binding, no effect on interaction with RNF43 and ZNRF3, no effect on WNT3A signaling; when associated with A-105.|||Loss of LGR5-binding, no effect on interaction with RNF43 and ZNRF3, no effect on WNT3A signaling; when associated with A-109.|||N-linked (GlcNAc...) asparagine|||R-spondin Fu-CRD|||R-spondin-2|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234439|||http://purl.uniprot.org/annotation/VAR_026247|||http://purl.uniprot.org/annotation/VAR_081036|||http://purl.uniprot.org/annotation/VAR_081037|||http://purl.uniprot.org/annotation/VAR_081038|||http://purl.uniprot.org/annotation/VSP_018321|||http://purl.uniprot.org/annotation/VSP_018322|||http://purl.uniprot.org/annotation/VSP_018323
http://togogenome.org/gene/9606:YBX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16989                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CSD|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Removed|||Y-box-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100214|||http://purl.uniprot.org/annotation/VAR_013114|||http://purl.uniprot.org/annotation/VSP_001135|||http://purl.uniprot.org/annotation/VSP_001136
http://togogenome.org/gene/9606:FAM200A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Protein FAM200A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279405
http://togogenome.org/gene/9606:GDPD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTR4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||GP-PDE|||Glycerophosphodiester phosphodiesterase domain-containing protein 5|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251941|||http://purl.uniprot.org/annotation/VAR_027733|||http://purl.uniprot.org/annotation/VSP_020813|||http://purl.uniprot.org/annotation/VSP_020814|||http://purl.uniprot.org/annotation/VSP_020815|||http://purl.uniprot.org/annotation/VSP_020816
http://togogenome.org/gene/9606:COL13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TAT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen alpha-1(XIII) chain|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 10.|||In isoform 11.|||In isoform 2, isoform 3, isoform 4, isoform 9 and isoform 11.|||In isoform 3, isoform 4, isoform 7, isoform 8, isoform 9 and isoform 11.|||In isoform 4, isoform 5, isoform 9, isoform 10 and isoform 11.|||In isoform 6 and isoform 7.|||In isoform 8 and isoform 10.|||In isoform 9.|||Nonhelical region 1 (NC1)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Nonhelical region 4 (NC4)|||Pro residues|||Triple-helical region 1 (COL1)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284679|||http://purl.uniprot.org/annotation/VAR_055670|||http://purl.uniprot.org/annotation/VSP_043361|||http://purl.uniprot.org/annotation/VSP_047230|||http://purl.uniprot.org/annotation/VSP_047231|||http://purl.uniprot.org/annotation/VSP_052382|||http://purl.uniprot.org/annotation/VSP_052383|||http://purl.uniprot.org/annotation/VSP_052384|||http://purl.uniprot.org/annotation/VSP_052385|||http://purl.uniprot.org/annotation/VSP_052386|||http://purl.uniprot.org/annotation/VSP_052387
http://togogenome.org/gene/9606:ARHGEF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6B2|||http://purl.uniprot.org/uniprot/E9PG37|||http://purl.uniprot.org/uniprot/Q9NR81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Polar residues|||Rho guanine nucleotide exchange factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080911|||http://purl.uniprot.org/annotation/VAR_021935|||http://purl.uniprot.org/annotation/VAR_021936|||http://purl.uniprot.org/annotation/VSP_011612|||http://purl.uniprot.org/annotation/VSP_027204|||http://purl.uniprot.org/annotation/VSP_027205|||http://purl.uniprot.org/annotation/VSP_027206
http://togogenome.org/gene/9606:OR1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH92                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150451|||http://purl.uniprot.org/annotation/VAR_048039|||http://purl.uniprot.org/annotation/VAR_048040|||http://purl.uniprot.org/annotation/VAR_048041|||http://purl.uniprot.org/annotation/VAR_048042|||http://purl.uniprot.org/annotation/VAR_048043|||http://purl.uniprot.org/annotation/VAR_048044
http://togogenome.org/gene/9606:NAMPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43490                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||N-acetylmethionine|||Nicotinamide phosphoribosyltransferase|||No effect on activity towards nicotinamide. Alters specificity, so that the enzyme acquires activity towards nicotinic acid.|||Phosphoserine|||Phosphotyrosine|||Reduces activity towards nicotinamide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205863|||http://purl.uniprot.org/annotation/VAR_036614
http://togogenome.org/gene/9606:TOGARAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHM7|||http://purl.uniprot.org/uniprot/G3XAE9|||http://purl.uniprot.org/uniprot/Q6P183|||http://purl.uniprot.org/uniprot/Q9Y4F4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In JBTS37.|||In JBTS37; affects ciliogenesis resulting in shorter cilia; does not affect the interaction with ARMC9.|||In JBTS37; loss of interaction with ARMC9.|||In JBTS37; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Polar residues|||TOG|||TOG 1|||TOG 2|||TOG 3|||TOG 4|||TOG array regulator of axonemal microtubules protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251952|||http://purl.uniprot.org/annotation/VAR_027739|||http://purl.uniprot.org/annotation/VAR_027740|||http://purl.uniprot.org/annotation/VAR_085345|||http://purl.uniprot.org/annotation/VAR_085346|||http://purl.uniprot.org/annotation/VAR_085347|||http://purl.uniprot.org/annotation/VAR_085348|||http://purl.uniprot.org/annotation/VAR_085349|||http://purl.uniprot.org/annotation/VAR_085350|||http://purl.uniprot.org/annotation/VAR_085351|||http://purl.uniprot.org/annotation/VAR_085352|||http://purl.uniprot.org/annotation/VSP_020821|||http://purl.uniprot.org/annotation/VSP_020822|||http://purl.uniprot.org/annotation/VSP_020823|||http://purl.uniprot.org/annotation/VSP_020824
http://togogenome.org/gene/9606:HIF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0VY79|||http://purl.uniprot.org/uniprot/Q16665                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine|||(Microbial infection) N-beta-linked (GlcNAc) arginine|||4-hydroxyproline|||Abolishes 1 sumoylation. Abolishes 1 sumoylation; when associated with R-532. Abolishes 2 sumoylations; when associated with R-477. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-477 and R-532.|||Abolishes 1 sumoylation. Abolishes 2 sumoylations; when associated with R-391. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-532.|||Abolishes SIRT2-mediated deacetylation, increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation. Increases interaction with EGLN1.|||Abolishes VHLE3-dependent ubiquitination; when associated with A-397.|||Abolishes VHLE3-dependent ubiquitination; when associated with A-400.|||Abolishes hypoxia-inducible transcriptional activation of ctaD.|||Abolishes in VHLE3-dependent ubiquitination, abolishes oxygen-dependent regulation of VP16, partially reduced VHLE target site ubiquitination and no interaction with VHL. No VHLE target site ubiquitination; when associated with G-564. Increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation; when associated with A-564.|||BHLH|||Blocks increase in transcriptional activation caused by nitrosylation.|||C-terminal VHL recognition site|||CTAD|||Constitutive expression under nonhypoxic conditions by decreasing ubiquitination.|||Constitutive kinase activity.|||DNA-binding|||Disordered|||Dramatic reduction of accumulation in the nucleus in response to hypoxia.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hypoxia-inducible factor 1-alpha|||ID|||Impaired kinase activity.|||In isoform 2.|||In isoform 3.|||Increases HIF1A instability and reduces HIF1A-induced target gene transcriptional activation; when associated with A-402.|||Induces stabilization of the protein.|||Inhibits interaction with EP300 and transactivation activity.|||Interaction with TSGA10|||N-terminal VHL recognition site|||N6-acetyllysine|||NTAD|||No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-391; R-477 and R-532.|||No change in VHL-dependent ubiquitination. Partially reduced VHLE target site ubiquitination. No VHLE target site ubiquitination; when associated with A-402.|||No change in VHLE3-dependent ubiquitination.|||No change in sumoylation nor in ARD1-mediated acetylation.|||No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-538.|||No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-547.|||No change in sumoylation.|||Nuclear localization signal|||ODD|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphoserine; by CK1|||Phosphoserine; by GSK3-beta|||Phosphoserine; by PLK3|||Phosphothreonine; by GSK3-beta|||Polar residues|||Recruits CREBBP. No enhancement of CREBBP by Clioquinol in the presence of FIH1. No change in nuclear location nor on repression of transcriptional activity in the presence of histone deacetylase inhibitor.|||Reduced ubiquitination. No change in sumoylation nor on interaction with NAA10. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-477. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-538 and K-547.|||Required for heterodimer formation with ARNT|||S-nitrosocysteine|||Strongly reduced GlcNAcylation by E.coli NleB1.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127220|||http://purl.uniprot.org/annotation/VAR_015854|||http://purl.uniprot.org/annotation/VAR_049541|||http://purl.uniprot.org/annotation/VAR_049542|||http://purl.uniprot.org/annotation/VSP_007738|||http://purl.uniprot.org/annotation/VSP_044942|||http://purl.uniprot.org/annotation/VSP_047335
http://togogenome.org/gene/9606:DGKH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0I1|||http://purl.uniprot.org/uniprot/B4DYW1|||http://purl.uniprot.org/uniprot/Q86XP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DAGKc|||Diacylglycerol kinase eta|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Loss of homoligomerization and heterooligomerization but not diacylglycerol kinase activity.|||PDZ-binding|||PH|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Polar residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239367|||http://purl.uniprot.org/annotation/VAR_033867|||http://purl.uniprot.org/annotation/VSP_019183|||http://purl.uniprot.org/annotation/VSP_019185|||http://purl.uniprot.org/annotation/VSP_019186
http://togogenome.org/gene/9606:OR56A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVB5|||http://purl.uniprot.org/uniprot/Q8NGH5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 56A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150793
http://togogenome.org/gene/9606:TESPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of ITPR1-binding.|||Phosphoserine|||Polar residues|||Protein TESPA1|||Strong decrease in ITPR1-binding. Complete loss of ITPR1-binding; when associated with A-185.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315219|||http://purl.uniprot.org/annotation/VAR_049513|||http://purl.uniprot.org/annotation/VSP_030488|||http://purl.uniprot.org/annotation/VSP_030489
http://togogenome.org/gene/9606:CUL4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K4DI93|||http://purl.uniprot.org/uniprot/Q13620                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cullin family profile|||Cullin-4B|||Disordered|||Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-56. Disrupts nuclear localization.|||Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-57. Disrupts nuclear localization.|||Distributed in cytoplasm. Fails to promote cell proliferation. No binding to KPNA2, KPNA4 and KPNA1.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In MRXSC.|||In MRXSC; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||No impairment in nuclear localization.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393946|||http://purl.uniprot.org/annotation/VAR_032272|||http://purl.uniprot.org/annotation/VAR_032273|||http://purl.uniprot.org/annotation/VAR_032274|||http://purl.uniprot.org/annotation/VAR_032275|||http://purl.uniprot.org/annotation/VSP_039084|||http://purl.uniprot.org/annotation/VSP_039085|||http://purl.uniprot.org/annotation/VSP_039086
http://togogenome.org/gene/9606:VAX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SQQ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In MCOPS11; loss of function mutation.|||In isoform 2.|||Pro residues|||Ventral anterior homeobox 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240522|||http://purl.uniprot.org/annotation/VAR_067307|||http://purl.uniprot.org/annotation/VSP_019396
http://togogenome.org/gene/9606:ATP12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0R9|||http://purl.uniprot.org/uniprot/P54707                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Abolishes targeting to the apical plasma membrane.|||Cation-transporting P-type ATPase C-terminal|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Phosphoserine; by PKA|||Potassium-transporting ATPase alpha chain 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046260|||http://purl.uniprot.org/annotation/VAR_020186|||http://purl.uniprot.org/annotation/VSP_034640
http://togogenome.org/gene/9606:OR6P1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV72|||http://purl.uniprot.org/uniprot/Q8NGX9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6P1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150635
http://togogenome.org/gene/9606:MBD3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWY6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Methyl-CpG-binding domain protein 3-like 1|||Transcription repressor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096251|||http://purl.uniprot.org/annotation/VAR_051155
http://togogenome.org/gene/9606:CBLC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULV8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  4H|||Abolishes E3 activity.|||Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity.|||Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination.|||Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC.|||Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351.|||Cbl-PTB|||Decreases interactions with EGFR and SRC as well as SRC ubiquitination.|||Disordered|||E3 ubiquitin-protein ligase CBL-C|||EF-hand-like|||Enhances interaction with EGFR and SRC as well as SRC ubiquitination.|||In isoform 2.|||Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster.|||Interaction with RET|||Linker|||No effect on TGFB1I1 and SRC interactions. Abolishes SRC ubiquitination. Abolishes interaction with TGFB1I1; when associated with A-366. Abolishes interaction with RET and inhibition of RET degradation.|||No effect on interaction with EGFR and SRC as well as on SRC ubiquitination.|||No effect on interaction with RET. Binds slightly to SRC, this interaction is independent of SRC phosphorylation. Strongly decreases SRC ubiquitination. Abolishes interaction with EGFR.|||Phosphotyrosine; by SRC|||Pro residues|||RING-type|||SH2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055866|||http://purl.uniprot.org/annotation/VAR_018298|||http://purl.uniprot.org/annotation/VSP_005732
http://togogenome.org/gene/9606:GPANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCU2|||http://purl.uniprot.org/uniprot/B2RA66|||http://purl.uniprot.org/uniprot/O95872                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Disordered|||Found in a clear cell renal carcinoma case; somatic mutation.|||G patch domain and ankyrin repeat-containing protein 1|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066972|||http://purl.uniprot.org/annotation/VAR_020096|||http://purl.uniprot.org/annotation/VAR_048291|||http://purl.uniprot.org/annotation/VAR_048292|||http://purl.uniprot.org/annotation/VAR_048293|||http://purl.uniprot.org/annotation/VAR_064698
http://togogenome.org/gene/9606:TRMT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4G4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed|||tRNA (guanine(10)-N2)-methyltransferase homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230288|||http://purl.uniprot.org/annotation/VAR_025786|||http://purl.uniprot.org/annotation/VSP_017816|||http://purl.uniprot.org/annotation/VSP_017817|||http://purl.uniprot.org/annotation/VSP_017818
http://togogenome.org/gene/9606:KRBOX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2F6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||KRAB|||KRAB domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330293|||http://purl.uniprot.org/annotation/VSP_033024|||http://purl.uniprot.org/annotation/VSP_033025|||http://purl.uniprot.org/annotation/VSP_033026
http://togogenome.org/gene/9606:SMARCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KMX2|||http://purl.uniprot.org/uniprot/Q92925                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||DM2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2|||SWIB/MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071985|||http://purl.uniprot.org/annotation/VSP_040530|||http://purl.uniprot.org/annotation/VSP_040531|||http://purl.uniprot.org/annotation/VSP_040532
http://togogenome.org/gene/9606:POU2F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2.|||In isoform 3.|||POU domain, class 2, transcription factor 3|||POU-specific|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100717|||http://purl.uniprot.org/annotation/VAR_031618|||http://purl.uniprot.org/annotation/VAR_055906|||http://purl.uniprot.org/annotation/VSP_043900|||http://purl.uniprot.org/annotation/VSP_043901
http://togogenome.org/gene/9606:METTL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased affinity for S-adenosyl-L-methionine.|||Does not affect affinity for S-adenosyl-L-methionine.|||In isoform 2.|||Nearly abolished affinity for S-adenosyl-L-methionine.|||Strongly decreased affinity for S-adenosyl-L-methionine.|||Strongly reduced RNA (cytosine-3-)-methyltransferase activity.|||tRNA N(3)-methylcytidine methyltransferase METTL6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204454|||http://purl.uniprot.org/annotation/VSP_008480
http://togogenome.org/gene/9606:CLDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5JSJ9|||http://purl.uniprot.org/uniprot/O95832                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Interactions with TJP1, TJP2, TJP3 and PATJ|||Loss of HCV receptor activity. Significant loss of interaction with CD81. Reduced interaction with OCLN.|||Loss of HCV receptor activity. Significant loss of interaction with CD81. Reduced interaction with OCLN. According to PubMed:17325668 no effect observed on HCV infection susceptibility in cell culture.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144729
http://togogenome.org/gene/9606:SOX13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HMG box|||Phosphoserine|||Polar residues|||Required for homodimerization|||Transcription factor SOX-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048756|||http://purl.uniprot.org/annotation/VAR_062671
http://togogenome.org/gene/9606:TAF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12962                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes methylation. Does not affect interaction with LOXL2 but greatly reduces deamination by LOXL2.|||Allysine; alternate|||Disordered|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||Transcription initiation factor TFIID subunit 10|||[KR]-[STA]-K motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118897|||http://purl.uniprot.org/annotation/VAR_013706
http://togogenome.org/gene/9606:RARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54136                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||Arginine--tRNA ligase, cytoplasmic|||Could be involved in the assembly of the multisynthetase complex|||In HLD9.|||In isoform Monomeric.|||Interaction with tRNA|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035797|||http://purl.uniprot.org/annotation/VAR_020106|||http://purl.uniprot.org/annotation/VAR_020107|||http://purl.uniprot.org/annotation/VAR_052635|||http://purl.uniprot.org/annotation/VAR_072666|||http://purl.uniprot.org/annotation/VAR_072667|||http://purl.uniprot.org/annotation/VSP_018905
http://togogenome.org/gene/9606:IDO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A348GSI3|||http://purl.uniprot.org/uniprot/P14902                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Indoleamine 2,3-dioxygenase 1|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215204|||http://purl.uniprot.org/annotation/VAR_053368
http://togogenome.org/gene/9606:DUSP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95147|||http://purl.uniprot.org/uniprot/Q6FI36                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Strand                                                                                  ^@                                                                                  Dual specificity protein phosphatase 14|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094822
http://togogenome.org/gene/9606:ZNF175                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y473                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Nuclear localization signal|||Zinc finger protein 175                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047440|||http://purl.uniprot.org/annotation/VAR_052789|||http://purl.uniprot.org/annotation/VAR_061938|||http://purl.uniprot.org/annotation/VAR_083478
http://togogenome.org/gene/9606:GLMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV34|||http://purl.uniprot.org/uniprot/A0A087X0W3|||http://purl.uniprot.org/uniprot/Q8WWB7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glycosylated lysosomal membrane protein|||Helical|||In isoform 2.|||Lumenal|||Lysosomal targeting motif|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284484|||http://purl.uniprot.org/annotation/VAR_031742|||http://purl.uniprot.org/annotation/VAR_031743|||http://purl.uniprot.org/annotation/VAR_031744|||http://purl.uniprot.org/annotation/VSP_037842
http://togogenome.org/gene/9606:GP1BA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7UYB8|||http://purl.uniprot.org/uniprot/P07359                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by ADAM17|||Cytoplasmic|||Decreased binding to vWF.|||Disordered|||Extracellular|||Glycocalicin|||Helical|||In BSS and BSSA2.|||In BSS.|||In Siba(+).|||In VWDP.|||In VWDP; increased binding to vWF.|||Increased binding to vWF.|||Interchain (with C-147 in GP1BB)|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||No change.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Platelet glycoprotein Ib alpha chain|||Polar residues|||Pro residues|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021343|||http://purl.uniprot.org/annotation/PRO_0000021344|||http://purl.uniprot.org/annotation/PRO_5003984641|||http://purl.uniprot.org/annotation/VAR_005256|||http://purl.uniprot.org/annotation/VAR_005257|||http://purl.uniprot.org/annotation/VAR_005258|||http://purl.uniprot.org/annotation/VAR_005259|||http://purl.uniprot.org/annotation/VAR_005260|||http://purl.uniprot.org/annotation/VAR_005261|||http://purl.uniprot.org/annotation/VAR_005262|||http://purl.uniprot.org/annotation/VAR_011909|||http://purl.uniprot.org/annotation/VAR_011910|||http://purl.uniprot.org/annotation/VAR_013511|||http://purl.uniprot.org/annotation/VAR_014206|||http://purl.uniprot.org/annotation/VAR_014207|||http://purl.uniprot.org/annotation/VAR_019657
http://togogenome.org/gene/9606:RBAK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with AR|||KRAB|||RB-associated KRAB zinc finger protein|||Required for interaction with RB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316976|||http://purl.uniprot.org/annotation/VAR_038438|||http://purl.uniprot.org/annotation/VSP_044805|||http://purl.uniprot.org/annotation/VSP_044806
http://togogenome.org/gene/9606:LY6G5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7Y6|||http://purl.uniprot.org/uniprot/Q5SRR4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Lymphocyte antigen 6 complex locus protein G5c|||N-linked (GlcNAc...) asparagine|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323016|||http://purl.uniprot.org/annotation/VSP_032004|||http://purl.uniprot.org/annotation/VSP_042107
http://togogenome.org/gene/9606:OR7A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW60|||http://purl.uniprot.org/uniprot/Q15622                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150643
http://togogenome.org/gene/9606:KRT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02533                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In EBS1A and EBS1B.|||In EBS1A.|||In EBS1A; unknown pathological significance.|||In EBS1B and EBS1A.|||In EBS1B and EBS1C.|||In EBS1B and EBS1C; unknown pathological significance.|||In EBS1B.|||In EBS1C and EBS1B.|||In EBS1C.|||In EBS1C; also found in a patient with epidermolysis bullosa simplex with unspecified subtype.|||In EBS1C; unknown pathological significance.|||In EBS1D.|||Increase in keratin-positive aggregates and keratin intermediate filament networks that are very thin and sparse with short filaments.|||Interaction with Type I keratins and keratin filaments|||Interchain|||Keratin, type I cytoskeletal 14|||Linker 1|||Linker 12|||No effect on interaction with KRT5 or keratin intermediate filament networks.|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with epidermolysis bullosa simplex with unspecified subtype.|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063653|||http://purl.uniprot.org/annotation/VAR_003837|||http://purl.uniprot.org/annotation/VAR_003838|||http://purl.uniprot.org/annotation/VAR_003839|||http://purl.uniprot.org/annotation/VAR_003841|||http://purl.uniprot.org/annotation/VAR_003842|||http://purl.uniprot.org/annotation/VAR_003843|||http://purl.uniprot.org/annotation/VAR_003844|||http://purl.uniprot.org/annotation/VAR_003845|||http://purl.uniprot.org/annotation/VAR_010437|||http://purl.uniprot.org/annotation/VAR_010438|||http://purl.uniprot.org/annotation/VAR_010439|||http://purl.uniprot.org/annotation/VAR_010440|||http://purl.uniprot.org/annotation/VAR_010441|||http://purl.uniprot.org/annotation/VAR_010442|||http://purl.uniprot.org/annotation/VAR_010443|||http://purl.uniprot.org/annotation/VAR_010444|||http://purl.uniprot.org/annotation/VAR_010445|||http://purl.uniprot.org/annotation/VAR_010446|||http://purl.uniprot.org/annotation/VAR_010447|||http://purl.uniprot.org/annotation/VAR_010448|||http://purl.uniprot.org/annotation/VAR_010449|||http://purl.uniprot.org/annotation/VAR_010450|||http://purl.uniprot.org/annotation/VAR_010451|||http://purl.uniprot.org/annotation/VAR_010452|||http://purl.uniprot.org/annotation/VAR_023719|||http://purl.uniprot.org/annotation/VAR_023720|||http://purl.uniprot.org/annotation/VAR_023721|||http://purl.uniprot.org/annotation/VAR_023722|||http://purl.uniprot.org/annotation/VAR_023723|||http://purl.uniprot.org/annotation/VAR_023724|||http://purl.uniprot.org/annotation/VAR_023725|||http://purl.uniprot.org/annotation/VAR_027718|||http://purl.uniprot.org/annotation/VAR_027719|||http://purl.uniprot.org/annotation/VAR_027720|||http://purl.uniprot.org/annotation/VAR_027721|||http://purl.uniprot.org/annotation/VAR_031634|||http://purl.uniprot.org/annotation/VAR_031635|||http://purl.uniprot.org/annotation/VAR_031636|||http://purl.uniprot.org/annotation/VAR_031637|||http://purl.uniprot.org/annotation/VAR_031638|||http://purl.uniprot.org/annotation/VAR_031639|||http://purl.uniprot.org/annotation/VAR_033496|||http://purl.uniprot.org/annotation/VAR_049784|||http://purl.uniprot.org/annotation/VAR_055347|||http://purl.uniprot.org/annotation/VAR_071705|||http://purl.uniprot.org/annotation/VAR_086617|||http://purl.uniprot.org/annotation/VAR_086618|||http://purl.uniprot.org/annotation/VAR_086619|||http://purl.uniprot.org/annotation/VAR_086620|||http://purl.uniprot.org/annotation/VAR_086621|||http://purl.uniprot.org/annotation/VAR_086622
http://togogenome.org/gene/9606:FBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00757                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Almost completely abolishes nuclear localization.|||Causes conformational change of N-terminal residues and decreased sensitivity towards AMP with lack of conversion to the inactive T-state in the presence of AMP.|||Fructose-1,6-bisphosphatase isozyme 2|||Greatly reduces affinity towards Ca(2+) and slightly reduces affinity towards Mg(2+).|||Greatly reduces nuclear lozalization.|||Greatly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA.|||Important for interaction with ALDOA|||Important for the conversion from active R-state to inactive T-state in the presence of AMP|||In CORLK; decreased activity; decreased sensitivity to allosteric inhibition by AMP; decreased thermal stability.|||Minor reduction in nuclear localization.|||No effect on kinetic properties and interaction with ALDOA.|||No effect on kinetic properties but decreases binding to ALDOA.|||Nuclear localization signal|||Phosphotyrosine|||Reduces sensitivity to AMP; when associated with E-21 and C-180.|||Reduces sensitivity to AMP; when associated with E-21 and M-178.|||Reduces sensitivity to AMP; when associated with M-178 and C-180.|||Reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA.|||Significantly reduces nuclear localization.|||Slightly reduces sensitivity to inhibition by AMP and Ca(2+) and activation by Mg(2+). Decreases binding to ALDOA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200504|||http://purl.uniprot.org/annotation/VAR_024448|||http://purl.uniprot.org/annotation/VAR_087242
http://togogenome.org/gene/9606:COMMD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VX2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077399|||http://purl.uniprot.org/annotation/VSP_038372
http://togogenome.org/gene/9606:ANG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03950|||http://purl.uniprot.org/uniprot/W0UV28                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  15- to 18-fold increase in RNase activity.|||3- to 5-fold increase in RNase activity.|||Angiogenin|||Homodimerization is similar to wild-type; causes mislocalization in the cytoplasm; strongly reduces ribonucleolytic activity.|||In ALS9.|||In ALS9; homodimerization is similar to wild-type; localization in the nucleus is similar to the wild-type; strongly reduces ribonucleolytic activity.|||In ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; retains nuclear translocation.|||In ALS9; loss of angiogenic activity; reduced ribonucleolytic activity; unable to translocate to the nucleus.|||In ALS9; marginally reduced ribonucleolytic activity; wild type far-UVCD spectra.|||In ALS9; reduced ribonucleolytic activity.|||In ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; moderate reduction of thermal stability.|||In ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; reduced thermal stability.|||In ALS9; reduced ribonucleolytic activity; low angiogenic activity; reduced mitogenic activity; wild type far-UVCD spectra.|||In some ALS9 patients; pathogenicity uncertain; reduced ribonucleolytic activity; moderate reduction of thermal stability.|||Nucleolar localization signal|||Over 18-fold increase in RNase activity.|||Proton acceptor|||Proton donor|||Pyrrolidone carboxylic acid|||Ribonuclease A-domain|||Significantly decreases binding affinity for RNH1.|||Slightly decreases binding affinity for RNH1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030843|||http://purl.uniprot.org/annotation/PRO_5007751491|||http://purl.uniprot.org/annotation/VAR_013148|||http://purl.uniprot.org/annotation/VAR_044145|||http://purl.uniprot.org/annotation/VAR_044146|||http://purl.uniprot.org/annotation/VAR_044147|||http://purl.uniprot.org/annotation/VAR_044148|||http://purl.uniprot.org/annotation/VAR_044149|||http://purl.uniprot.org/annotation/VAR_044150|||http://purl.uniprot.org/annotation/VAR_044151|||http://purl.uniprot.org/annotation/VAR_044152|||http://purl.uniprot.org/annotation/VAR_044153|||http://purl.uniprot.org/annotation/VAR_044154|||http://purl.uniprot.org/annotation/VAR_044155|||http://purl.uniprot.org/annotation/VAR_044156|||http://purl.uniprot.org/annotation/VAR_044157|||http://purl.uniprot.org/annotation/VAR_073021|||http://purl.uniprot.org/annotation/VAR_073022
http://togogenome.org/gene/9606:SCNN1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P37088                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amiloride-sensitive sodium channel subunit alpha|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In BESC2; hyperactive mutation resulting in a significant increase of amiloride-sensitive sodium currents.|||In BESC2; hypoactive mutation resulting in reduction of protein expression and a significant decrease of amiloride-sensitive sodium currents.|||In LIDLS3; increased channel activity.|||In PHA1B1.|||In PHA1B1; results in a significant reduction of channel function as compared to wild-type; significantly lowers both Li+ and Na+ ion currents.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increased channel activity.|||Pro residues|||Results in a 4-fold increase of amiloride-sensitive sodium currents; found in BESC2 patients at higher frequency than in controls; associated with an increased risk for ischemic cerebrovascular events.|||Significant decrease of amiloride-sensitive sodium currents.|||Significant increase of amiloride-sensitive sodium currents.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181261|||http://purl.uniprot.org/annotation/VAR_015833|||http://purl.uniprot.org/annotation/VAR_015834|||http://purl.uniprot.org/annotation/VAR_015835|||http://purl.uniprot.org/annotation/VAR_022142|||http://purl.uniprot.org/annotation/VAR_026518|||http://purl.uniprot.org/annotation/VAR_052035|||http://purl.uniprot.org/annotation/VAR_060793|||http://purl.uniprot.org/annotation/VAR_060794|||http://purl.uniprot.org/annotation/VAR_060795|||http://purl.uniprot.org/annotation/VAR_060796|||http://purl.uniprot.org/annotation/VAR_060797|||http://purl.uniprot.org/annotation/VAR_081179|||http://purl.uniprot.org/annotation/VSP_007719|||http://purl.uniprot.org/annotation/VSP_007720|||http://purl.uniprot.org/annotation/VSP_007721|||http://purl.uniprot.org/annotation/VSP_007722|||http://purl.uniprot.org/annotation/VSP_007723|||http://purl.uniprot.org/annotation/VSP_043667
http://togogenome.org/gene/9606:PAGE2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JRK9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Phosphothreonine|||Polar residues|||Putative G antigen family E member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247363
http://togogenome.org/gene/9606:PRICKLE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TBC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LIM zinc-binding 1|||LIM zinc-binding 2|||PET|||Polar residues|||Prickle-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231619|||http://purl.uniprot.org/annotation/VAR_056165|||http://purl.uniprot.org/annotation/VSP_017857|||http://purl.uniprot.org/annotation/VSP_039377
http://togogenome.org/gene/9606:PLIN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00G26                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Essential for lipid droplet targeting|||Interaction with LIPE|||Interaction with PNPLA2 and ABHD5|||Perilipin-5|||Phosphoserine|||Recruits mitochondria at the lipid droplet surface                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338982|||http://purl.uniprot.org/annotation/VAR_043850|||http://purl.uniprot.org/annotation/VAR_043851|||http://purl.uniprot.org/annotation/VAR_043852
http://togogenome.org/gene/9606:TMEM115                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12893                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||Mediates homooligomerization|||Mediates localization to the Golgi|||Phosphothreonine|||Transmembrane protein 115                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058451
http://togogenome.org/gene/9606:DICER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPY3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10-fold decrease in activity; when associated with Y-971.|||10-fold decrease in activity; when associated with Y-972.|||2-fold decrease in activity.|||5-fold decrease in activity.|||Acidic residues|||DECH box|||DRBM|||Decreased activity. Loss of activity; when associated with D-1320.|||Decreased activity. Loss of activity; when associated with D-1709.|||Decreased activity. Loss of activity; when associated with E-1444.|||Decreased activity. Loss of activity; when associated with E-1813.|||Dicer dsRNA-binding fold|||Disordered|||Endoribonuclease Dicer|||Found in Wilms tumor from a patient with GLOW syndrome; somatic mutation; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||Important for activity|||In GLOW; somatic mutation.|||In MNG1.|||In PPB.|||In isoform 2.|||In isoform 3.|||In non-epithelial ovarian tumor; somatic mutation.|||In non-epithelial ovarian tumor; somatic mutation; results in reduced RNase IIIb activity but retention of RNase IIIa activity.|||No effect on activity.|||PAZ|||Phosphoserine|||RNase III 1|||RNase III 2|||Required for interaction with PRKRA and TARBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180470|||http://purl.uniprot.org/annotation/VAR_063150|||http://purl.uniprot.org/annotation/VAR_065301|||http://purl.uniprot.org/annotation/VAR_067091|||http://purl.uniprot.org/annotation/VAR_067092|||http://purl.uniprot.org/annotation/VAR_067093|||http://purl.uniprot.org/annotation/VAR_067094|||http://purl.uniprot.org/annotation/VAR_067095|||http://purl.uniprot.org/annotation/VAR_067096|||http://purl.uniprot.org/annotation/VAR_067097|||http://purl.uniprot.org/annotation/VAR_067098|||http://purl.uniprot.org/annotation/VAR_067099|||http://purl.uniprot.org/annotation/VAR_067100|||http://purl.uniprot.org/annotation/VAR_081917|||http://purl.uniprot.org/annotation/VAR_081918|||http://purl.uniprot.org/annotation/VAR_081919|||http://purl.uniprot.org/annotation/VAR_081920|||http://purl.uniprot.org/annotation/VSP_042832|||http://purl.uniprot.org/annotation/VSP_055341|||http://purl.uniprot.org/annotation/VSP_055342
http://togogenome.org/gene/9606:XRN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZC3|||http://purl.uniprot.org/uniprot/Q9H0D6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  5'-3' exoribonuclease 2|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||CCHC-type|||Disordered|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Xrn1 N-terminal|||Xrn1 helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071396|||http://purl.uniprot.org/annotation/VAR_027516|||http://purl.uniprot.org/annotation/VAR_053002|||http://purl.uniprot.org/annotation/VSP_020596
http://togogenome.org/gene/9606:BEX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWD9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Interaction with SIRT2|||Interaction with alpha-tubulin|||Polar residues|||Protein BEX4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229783
http://togogenome.org/gene/9606:PSTPIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4R2|||http://purl.uniprot.org/uniprot/Q9H939                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-BAR|||In isoform 2.|||Phosphotyrosine|||Proline-serine-threonine phosphatase-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058541|||http://purl.uniprot.org/annotation/VAR_059708|||http://purl.uniprot.org/annotation/VAR_059709|||http://purl.uniprot.org/annotation/VSP_004070
http://togogenome.org/gene/9606:PREPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4J6C6                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Found in a patient with intellectual disability, short stature, chronic lung disease and failure to thrive; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity.|||N-acetylmethionine|||No effect on catalytic activity.|||Prolyl endopeptidase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314860|||http://purl.uniprot.org/annotation/VAR_082151|||http://purl.uniprot.org/annotation/VSP_030401|||http://purl.uniprot.org/annotation/VSP_030402|||http://purl.uniprot.org/annotation/VSP_030403
http://togogenome.org/gene/9606:MIX23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VC31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylalanine|||N6-acetyllysine|||Protein MIX23|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239441
http://togogenome.org/gene/9606:GXYLT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glucoside xylosyltransferase 2|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288539
http://togogenome.org/gene/9606:RLIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N999                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes RNA ligation activity, in vitro.|||Deficient in auto-AMPylation activity, in vitro. Abolishes RNA ligation activity, in vitro.|||Has no effect on RNA ligation activity, in vitro.|||In isoform 2.|||In isoform 3.|||RNA ligase 1|||Reduces RNA ligation activity to about 12%, in vitro.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305272|||http://purl.uniprot.org/annotation/VAR_035197|||http://purl.uniprot.org/annotation/VAR_035198|||http://purl.uniprot.org/annotation/VSP_028316|||http://purl.uniprot.org/annotation/VSP_028317|||http://purl.uniprot.org/annotation/VSP_028318|||http://purl.uniprot.org/annotation/VSP_028319
http://togogenome.org/gene/9606:STK25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4B2|||http://purl.uniprot.org/uniprot/A0A0S2Z4Y2|||http://purl.uniprot.org/uniprot/B3KRS6|||http://purl.uniprot.org/uniprot/B4DMA5|||http://purl.uniprot.org/uniprot/B4DVS7|||http://purl.uniprot.org/uniprot/B4E185|||http://purl.uniprot.org/uniprot/O00506|||http://purl.uniprot.org/uniprot/Q96BA2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Loss of kinase activity and autophosphorylation.|||Loss of kinase activity.|||Phosphoserine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086713|||http://purl.uniprot.org/annotation/VAR_051674|||http://purl.uniprot.org/annotation/VSP_054397|||http://purl.uniprot.org/annotation/VSP_054683
http://togogenome.org/gene/9606:CUEDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H467                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  CUE|||CUE domain-containing protein 2|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282992
http://togogenome.org/gene/9606:MRPL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52815                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  In COXPD45; MRPL12 steady state level are reduced in patient fibroblasts; results in defective mt-LSU assembly; reduced mitochondrial translation with a significant decrease of synthesis of COXI, COXII and COXIII subunits.|||Large ribosomal subunit protein bL12m|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030458|||http://purl.uniprot.org/annotation/VAR_052001|||http://purl.uniprot.org/annotation/VAR_084463
http://togogenome.org/gene/9606:TRIM58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG06                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM58|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272301|||http://purl.uniprot.org/annotation/VAR_030036|||http://purl.uniprot.org/annotation/VAR_030037|||http://purl.uniprot.org/annotation/VAR_030038
http://togogenome.org/gene/9606:TMEM18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B42                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  DNA-binding|||Helical|||In isoform 2.|||Nuclear|||Nuclear localization signal|||Perinuclear space|||Transmembrane protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284369|||http://purl.uniprot.org/annotation/VSP_024469
http://togogenome.org/gene/9606:TSC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y5S3|||http://purl.uniprot.org/uniprot/Q32NF0|||http://purl.uniprot.org/uniprot/Q92574|||http://purl.uniprot.org/uniprot/X5D9D2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with TBC1D7.|||Abolished interaction with TBC1D7; when associated with 965-A--A-969.|||Basic and acidic residues|||Disordered|||Found in a patient suspected of having tuberous sclerosis; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling.|||Found in a patient suspected of having tuberous sclerosis; unknown pathological significance; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling.|||Hamartin|||In FCORD2; somatic mutation; decreased interaction with TSC2; decreased function in negative regulation of TOR signaling.|||In TSC1.|||In TSC1; reduced expression; altered subcellular localization; reduced interaction with TSC2; reduced inhibition of TORC1 signaling.|||In TSC1; reduced expression; reduced inhibition of TORC1 signaling.|||In TSC1; unknown pathological significance.|||In TSC1; unknown pathological significance; does not affect interaction with TSC2.|||In TSC1; unknown pathological significance; no effect on expression; no effect on inhibition of TORC1 signaling.|||In TSC1; unknown pathological significance; no effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling.|||In TSC1; unknown pathological significance; reduced expression; altered subcellular localization; reduced inhibition of TORC1 signaling.|||In a bladder tumor; diffuse punctate cytoplasmic distribution in aminoacid-starved conditions; does not affect interaction with TSC2.|||In a bladder tumor; somatic mutation; reduced stability; does not affect interaction with TSC2.|||In isoform 2.|||Mediates interaction with WDR45B|||Might be associated with susceptibility to focal cortical dysplasia of the Taylor balloon cell type.|||No effect on expression; no effect on inhibition of TORC1 signaling.|||No effect on expression; no effect on subcellular localization; no effect on inhibition of TORC1 signaling.|||Phosphoserine|||Polar residues|||Reduced interaction with TBC1D7 without affecting interaction with TSC2.|||Slightly reduced interaction with TBC1D7 without affecting interaction with TSC2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065651|||http://purl.uniprot.org/annotation/VAR_009397|||http://purl.uniprot.org/annotation/VAR_009398|||http://purl.uniprot.org/annotation/VAR_009399|||http://purl.uniprot.org/annotation/VAR_009400|||http://purl.uniprot.org/annotation/VAR_009401|||http://purl.uniprot.org/annotation/VAR_009402|||http://purl.uniprot.org/annotation/VAR_009403|||http://purl.uniprot.org/annotation/VAR_009404|||http://purl.uniprot.org/annotation/VAR_009405|||http://purl.uniprot.org/annotation/VAR_009406|||http://purl.uniprot.org/annotation/VAR_009407|||http://purl.uniprot.org/annotation/VAR_009408|||http://purl.uniprot.org/annotation/VAR_009409|||http://purl.uniprot.org/annotation/VAR_009410|||http://purl.uniprot.org/annotation/VAR_009411|||http://purl.uniprot.org/annotation/VAR_009412|||http://purl.uniprot.org/annotation/VAR_009413|||http://purl.uniprot.org/annotation/VAR_009414|||http://purl.uniprot.org/annotation/VAR_054386|||http://purl.uniprot.org/annotation/VAR_054387|||http://purl.uniprot.org/annotation/VAR_054388|||http://purl.uniprot.org/annotation/VAR_054389|||http://purl.uniprot.org/annotation/VAR_054390|||http://purl.uniprot.org/annotation/VAR_054391|||http://purl.uniprot.org/annotation/VAR_070636|||http://purl.uniprot.org/annotation/VAR_070637|||http://purl.uniprot.org/annotation/VAR_070638|||http://purl.uniprot.org/annotation/VAR_070639|||http://purl.uniprot.org/annotation/VAR_070640|||http://purl.uniprot.org/annotation/VAR_070641|||http://purl.uniprot.org/annotation/VAR_070642|||http://purl.uniprot.org/annotation/VAR_070643|||http://purl.uniprot.org/annotation/VAR_070644|||http://purl.uniprot.org/annotation/VAR_070645|||http://purl.uniprot.org/annotation/VAR_070646|||http://purl.uniprot.org/annotation/VAR_070647|||http://purl.uniprot.org/annotation/VAR_070648|||http://purl.uniprot.org/annotation/VAR_070649|||http://purl.uniprot.org/annotation/VAR_070650|||http://purl.uniprot.org/annotation/VAR_070651|||http://purl.uniprot.org/annotation/VAR_070652|||http://purl.uniprot.org/annotation/VAR_070653|||http://purl.uniprot.org/annotation/VAR_070654|||http://purl.uniprot.org/annotation/VAR_070655|||http://purl.uniprot.org/annotation/VAR_070656|||http://purl.uniprot.org/annotation/VAR_070657|||http://purl.uniprot.org/annotation/VAR_070658|||http://purl.uniprot.org/annotation/VAR_070659|||http://purl.uniprot.org/annotation/VAR_070660|||http://purl.uniprot.org/annotation/VAR_070661|||http://purl.uniprot.org/annotation/VAR_070662|||http://purl.uniprot.org/annotation/VAR_070663|||http://purl.uniprot.org/annotation/VAR_070664|||http://purl.uniprot.org/annotation/VAR_078844|||http://purl.uniprot.org/annotation/VAR_078845|||http://purl.uniprot.org/annotation/VAR_078846|||http://purl.uniprot.org/annotation/VSP_042890
http://togogenome.org/gene/9606:NIPAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H841                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NIPA-like protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242148|||http://purl.uniprot.org/annotation/VSP_060660|||http://purl.uniprot.org/annotation/VSP_060661
http://togogenome.org/gene/9606:EFEMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95967|||http://purl.uniprot.org/uniprot/Q9H3D5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Cleavage|||Cleavage; by ELANE|||Cleavage; by MMP2, MMP3, MMP7, MMP9, MMP12|||EGF-containing fibulin-like extracellular matrix protein 2|||EGF-like|||EGF-like 1; atypical|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||In ARCL1B.|||In ARCL1B; does not affect secretion; decreased elastic fiber assembly; loss of interaction with collagen type IV trimer, FBN1, highly glycosylated form of LOX and LTBP1; Does not affect interaction with LOX when LOX is non-glycosylated; proteolyzed by PLG.|||In ARCL1B; increased N-glycosylation; introduced an extra O-glycosylation site; does not affect secretion; decreased elastic fiber assembly; decreased interaction with collagen type IV trimer, FBN1, ELN, LTBP1, LOXL1 and LOXL2; new fragments proteolyzed by ELANE.|||In ARCL1B; loss of protein expression in patient dermal fibroblasts; increased transforming growth factor beta receptor signaling pathway in patient fibroblasts; loss of protein expression; strongly decreased secretion.|||In ARCL1B; loss of secretion.|||In ARCL1B; slightly decreased protein abundance in patient dermal fibroblasts; increased transforming growth factor beta receptor signaling pathway in patient fibroblasts; strongly decreased secretion; decreased elastic fiber assembly; loss of interaction with collagen type IV trimer, FBN1 and LTBP1; decreased interaction with LOXL2; new fragments proteolyzed by ELANE; new one fragment proteolyzed by MMP2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007575|||http://purl.uniprot.org/annotation/PRO_5004327935|||http://purl.uniprot.org/annotation/VAR_027019|||http://purl.uniprot.org/annotation/VAR_027020|||http://purl.uniprot.org/annotation/VAR_067069|||http://purl.uniprot.org/annotation/VAR_067070|||http://purl.uniprot.org/annotation/VAR_084029|||http://purl.uniprot.org/annotation/VAR_084030|||http://purl.uniprot.org/annotation/VAR_084031|||http://purl.uniprot.org/annotation/VAR_084032|||http://purl.uniprot.org/annotation/VAR_084033
http://togogenome.org/gene/9606:SH3BGRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75368                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Adapter SH3BGRL|||Required for interaction with HER2|||Required for interaction with PFN1, HER2, and ATG12|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220745
http://togogenome.org/gene/9606:KCNS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULS6                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Potassium voltage-gated channel subfamily S member 2|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054084
http://togogenome.org/gene/9606:CCNJL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZA8|||http://purl.uniprot.org/uniprot/Q8IV13                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin C-terminal|||Cyclin N-terminal|||Cyclin-J-like protein|||Cyclin-like|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309319|||http://purl.uniprot.org/annotation/VAR_053053|||http://purl.uniprot.org/annotation/VSP_029130|||http://purl.uniprot.org/annotation/VSP_029131|||http://purl.uniprot.org/annotation/VSP_029132
http://togogenome.org/gene/9606:TEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V5X7|||http://purl.uniprot.org/uniprot/Q99973                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||NACHT|||Polar residues|||TEP1 N-terminal 1|||TEP1 N-terminal 2|||TEP1 N-terminal 3|||TEP1 N-terminal 4|||TROVE|||Telomerase protein component 1|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 17|||WD 18|||WD 19|||WD 2|||WD 20|||WD 21|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050982|||http://purl.uniprot.org/annotation/VAR_018490|||http://purl.uniprot.org/annotation/VAR_018491|||http://purl.uniprot.org/annotation/VAR_018492|||http://purl.uniprot.org/annotation/VAR_018493|||http://purl.uniprot.org/annotation/VAR_018494|||http://purl.uniprot.org/annotation/VAR_018495|||http://purl.uniprot.org/annotation/VAR_018496|||http://purl.uniprot.org/annotation/VAR_018497|||http://purl.uniprot.org/annotation/VAR_018498|||http://purl.uniprot.org/annotation/VAR_047631|||http://purl.uniprot.org/annotation/VAR_047632|||http://purl.uniprot.org/annotation/VAR_047633|||http://purl.uniprot.org/annotation/VAR_047634|||http://purl.uniprot.org/annotation/VAR_047635|||http://purl.uniprot.org/annotation/VAR_047636|||http://purl.uniprot.org/annotation/VAR_047637|||http://purl.uniprot.org/annotation/VAR_047638|||http://purl.uniprot.org/annotation/VAR_047639|||http://purl.uniprot.org/annotation/VAR_047640|||http://purl.uniprot.org/annotation/VAR_047641|||http://purl.uniprot.org/annotation/VAR_047642|||http://purl.uniprot.org/annotation/VSP_010359
http://togogenome.org/gene/9606:WDR88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMY6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 88                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285630|||http://purl.uniprot.org/annotation/VAR_032030|||http://purl.uniprot.org/annotation/VAR_035892|||http://purl.uniprot.org/annotation/VSP_024873
http://togogenome.org/gene/9606:CNIH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLH6|||http://purl.uniprot.org/uniprot/Q9P003                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Protein cornichon homolog 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122230|||http://purl.uniprot.org/annotation/VAR_048830|||http://purl.uniprot.org/annotation/VSP_013466
http://togogenome.org/gene/9606:RHOXF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7M4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in infertile men; unknown pathological significance.|||Found in infertile men; unknown pathological significance; decreased induction of target genes expression.|||Homeobox|||Nuclear localization signal|||Rhox homeobox family member 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339371|||http://purl.uniprot.org/annotation/VAR_078301|||http://purl.uniprot.org/annotation/VAR_078302|||http://purl.uniprot.org/annotation/VAR_078303|||http://purl.uniprot.org/annotation/VAR_078304
http://togogenome.org/gene/9606:AGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J975|||http://purl.uniprot.org/uniprot/E7ESL9|||http://purl.uniprot.org/uniprot/Q86ST5|||http://purl.uniprot.org/uniprot/Q86XV5|||http://purl.uniprot.org/uniprot/Q96P47                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3|||C4-type|||Disordered|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4 and isoform 6.|||In isoform 5.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074220|||http://purl.uniprot.org/annotation/VSP_018534|||http://purl.uniprot.org/annotation/VSP_018535|||http://purl.uniprot.org/annotation/VSP_018536|||http://purl.uniprot.org/annotation/VSP_018537|||http://purl.uniprot.org/annotation/VSP_040373|||http://purl.uniprot.org/annotation/VSP_054890|||http://purl.uniprot.org/annotation/VSP_054891
http://togogenome.org/gene/9606:ELP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IA86                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with ELP1 and ELP3.|||Elongator complex protein 2|||In MRT58; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||No effect on interaction with ELP1 or ELP3; when associated with A-634, A-636 and A-670.|||No effect on interaction with ELP1 or ELP3; when associated with A-634, A-636 and A-689.|||No effect on interaction with ELP1 or ELP3; when associated with A-634, A-670 and A-689.|||No effect on interaction with ELP1 or ELP3; when associated with A-636, A-670 and A-689.|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051241|||http://purl.uniprot.org/annotation/VAR_024072|||http://purl.uniprot.org/annotation/VAR_024073|||http://purl.uniprot.org/annotation/VAR_024074|||http://purl.uniprot.org/annotation/VAR_024075|||http://purl.uniprot.org/annotation/VAR_024076|||http://purl.uniprot.org/annotation/VAR_033804|||http://purl.uniprot.org/annotation/VAR_033805|||http://purl.uniprot.org/annotation/VAR_033806|||http://purl.uniprot.org/annotation/VAR_077989|||http://purl.uniprot.org/annotation/VAR_077990|||http://purl.uniprot.org/annotation/VSP_016531|||http://purl.uniprot.org/annotation/VSP_016532|||http://purl.uniprot.org/annotation/VSP_016533|||http://purl.uniprot.org/annotation/VSP_043410|||http://purl.uniprot.org/annotation/VSP_044978|||http://purl.uniprot.org/annotation/VSP_044979
http://togogenome.org/gene/9606:PGAM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Y7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Site                                                                                  ^@                                                                                  N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Probable phosphoglycerate mutase 4|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179832|||http://purl.uniprot.org/annotation/VAR_014355|||http://purl.uniprot.org/annotation/VAR_014356|||http://purl.uniprot.org/annotation/VAR_014357
http://togogenome.org/gene/9606:INSIG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQ23|||http://purl.uniprot.org/uniprot/Q9Y5U4                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished interaction with SCAP even in the presence of 25-hydroxycholesterol.|||Abolished interaction with SCAP without affecting binding to 25-hydroxycholesterol.|||Abolished phosphorylation by PCK1, does not affect oxysterol-binding, does not affect the interaction with SCAP.|||Cysteine sulfenic acid (-SOH); alternate|||Cytoplasmic|||Decreased binding to 25-hydroxycholesterol and subsequent interaction with SCAP.|||Decreased binding to 25-hydroxycholesterol, leading to decreased interaction with SCAP.|||Does not affect degradation of the protein.|||Does not affect interaction with SCAP.|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Insulin-induced gene 2 protein|||KxHxx|||Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR. Abolished interaction with SCAP without affecting binding to 25-hydroxycholesterol.|||Lumenal|||Phosphomimetic mutant, reduced binding to oxysterol.|||Phosphoserine; by PCK1|||Prevents degradation because of impaired ubiquitination.|||Promotes ubiquitination by AMFR/gp78, which does not take place normally.|||Required for the recognition of 25-hydroxycholesterol                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286797
http://togogenome.org/gene/9606:SF3B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6V3|||http://purl.uniprot.org/uniprot/Q15393                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage/polyadenylation specificity factor A subunit C-terminal|||Cleavage/polyadenylation specificity factor A subunit N-terminal|||In isoform 2.|||In isoform 3.|||Interaction with PHF5A, SF3B1 and SF3B5|||Interaction with SF3B1|||Interaction with SF3B1 and SF3B5|||Interaction with SF3B5|||Phosphoserine|||Phosphothreonine|||Splicing factor 3B subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218639|||http://purl.uniprot.org/annotation/VAR_053647|||http://purl.uniprot.org/annotation/VSP_022977|||http://purl.uniprot.org/annotation/VSP_022978|||http://purl.uniprot.org/annotation/VSP_022979
http://togogenome.org/gene/9606:NAALADL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q58DX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Inactive N-acetylated-alpha-linked acidic dipeptidase-like protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315721|||http://purl.uniprot.org/annotation/VAR_038288|||http://purl.uniprot.org/annotation/VAR_038289|||http://purl.uniprot.org/annotation/VAR_038290|||http://purl.uniprot.org/annotation/VAR_038291|||http://purl.uniprot.org/annotation/VAR_038292|||http://purl.uniprot.org/annotation/VAR_038293|||http://purl.uniprot.org/annotation/VSP_030676|||http://purl.uniprot.org/annotation/VSP_030677|||http://purl.uniprot.org/annotation/VSP_030678
http://togogenome.org/gene/9606:C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JL69|||http://purl.uniprot.org/uniprot/B4DQI1|||http://purl.uniprot.org/uniprot/B4DV48|||http://purl.uniprot.org/uniprot/P06681|||http://purl.uniprot.org/uniprot/Q53HP3|||http://purl.uniprot.org/uniprot/Q5JP69|||http://purl.uniprot.org/uniprot/Q8N6L6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C3/C5 convertase|||Charge relay system|||Complement C2|||Complement C2a fragment|||Complement C2b fragment|||EMO_00033 electrostatic stabiliser,EMO_00033 electrostatic stabiliser,EMO_00033 electrostatic stabiliser,EMO_00033 electrostatic stabiliser|||EMO_00066 proton acceptor,EMO_00066 proton acceptor,EMO_00068 proton donor,EMO_00068 proton donor|||EMO_00068 proton donor,EMO_00066 proton acceptor,EMO_00054 nucleophile,EMO_00058 nucleofuge|||In C2D.|||In isoform 2.|||In isoform 3.|||MIDAS-like motif|||May be associated with a reduced risk for age-related macular degeneration.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027610|||http://purl.uniprot.org/annotation/PRO_0000027611|||http://purl.uniprot.org/annotation/PRO_0000027612|||http://purl.uniprot.org/annotation/PRO_5004248832|||http://purl.uniprot.org/annotation/PRO_5014589044|||http://purl.uniprot.org/annotation/PRO_5015097921|||http://purl.uniprot.org/annotation/VAR_008544|||http://purl.uniprot.org/annotation/VAR_008545|||http://purl.uniprot.org/annotation/VAR_008546|||http://purl.uniprot.org/annotation/VAR_011772|||http://purl.uniprot.org/annotation/VAR_019158|||http://purl.uniprot.org/annotation/VAR_019159|||http://purl.uniprot.org/annotation/VSP_043038|||http://purl.uniprot.org/annotation/VSP_043039|||http://purl.uniprot.org/annotation/VSP_046103
http://togogenome.org/gene/9606:SPATA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072174|||http://purl.uniprot.org/annotation/VAR_070808
http://togogenome.org/gene/9606:SPDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EA4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein Spindly                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274516|||http://purl.uniprot.org/annotation/VAR_030307|||http://purl.uniprot.org/annotation/VAR_030308|||http://purl.uniprot.org/annotation/VSP_022777|||http://purl.uniprot.org/annotation/VSP_054244
http://togogenome.org/gene/9606:LIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55344                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Cytoplasmic|||Extracellular|||Helical|||In CTRCT19.|||In isoform 2.|||Lens fiber membrane intrinsic protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164664|||http://purl.uniprot.org/annotation/VAR_069796|||http://purl.uniprot.org/annotation/VSP_005073
http://togogenome.org/gene/9606:PRR14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Increased binding to GRB2 and enhanced cell proliferation.|||Loss of heterochromatin association during interphase and loss of chromatin association during anaphase.|||Loss of heterochromatin association. Loss of interaction with CBX5.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||Proline-rich protein 14|||Required for nuclear lamina association|||Required for nuclear localization|||Required for the interaction with GRB2 and sufficient to promote the phosphorylation of AKT and cell proliferation|||Sufficient for heterochromatin association in interphase and chromatin association in anaphase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307269|||http://purl.uniprot.org/annotation/VAR_035389
http://togogenome.org/gene/9606:ZNF280C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 280C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227975
http://togogenome.org/gene/9606:FBXW11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKB1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  F-box|||F-box/WD repeat-containing protein 11|||Homodimerization domain D|||In NEDJED.|||In isoform A.|||In isoform B.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050981|||http://purl.uniprot.org/annotation/VAR_084385|||http://purl.uniprot.org/annotation/VAR_084386|||http://purl.uniprot.org/annotation/VAR_084387|||http://purl.uniprot.org/annotation/VAR_084388|||http://purl.uniprot.org/annotation/VAR_084389|||http://purl.uniprot.org/annotation/VAR_084390|||http://purl.uniprot.org/annotation/VAR_084391|||http://purl.uniprot.org/annotation/VSP_006765|||http://purl.uniprot.org/annotation/VSP_006766
http://togogenome.org/gene/9606:CLVS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUQ0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to PtdIns(3,5)P2. No effect on subcellular location.|||CRAL-TRIO|||Clavesin-1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297655|||http://purl.uniprot.org/annotation/VSP_027328|||http://purl.uniprot.org/annotation/VSP_027329
http://togogenome.org/gene/9606:CELF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J87                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUGBP Elav-like family member 6|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295229|||http://purl.uniprot.org/annotation/VAR_033265|||http://purl.uniprot.org/annotation/VSP_026847|||http://purl.uniprot.org/annotation/VSP_026848|||http://purl.uniprot.org/annotation/VSP_043242|||http://purl.uniprot.org/annotation/VSP_043243|||http://purl.uniprot.org/annotation/VSP_043244|||http://purl.uniprot.org/annotation/VSP_043245
http://togogenome.org/gene/9606:GREB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4ZG55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein GREB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320944|||http://purl.uniprot.org/annotation/VAR_039313|||http://purl.uniprot.org/annotation/VAR_039314|||http://purl.uniprot.org/annotation/VAR_039315|||http://purl.uniprot.org/annotation/VAR_039316|||http://purl.uniprot.org/annotation/VAR_039317|||http://purl.uniprot.org/annotation/VAR_039318|||http://purl.uniprot.org/annotation/VAR_039319|||http://purl.uniprot.org/annotation/VAR_061654|||http://purl.uniprot.org/annotation/VAR_061655|||http://purl.uniprot.org/annotation/VSP_031757|||http://purl.uniprot.org/annotation/VSP_031758|||http://purl.uniprot.org/annotation/VSP_031759|||http://purl.uniprot.org/annotation/VSP_031760|||http://purl.uniprot.org/annotation/VSP_031761
http://togogenome.org/gene/9606:ZFP36L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47974                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||Disordered|||Impaired mRNA-binding; when associated with K-195.|||Impaired mRNA-binding; when associated with R-157.|||In OZEMA13; results in decreased mRNA catabolic process.|||In OZEMA13; unknown pathological significance.|||Phosphoserine|||Phosphoserine; by RPS6KA1|||Phosphothreonine|||Polar residues|||Pro residues|||RNA-binding|||mRNA decay activator protein ZFP36L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089170|||http://purl.uniprot.org/annotation/VAR_087928|||http://purl.uniprot.org/annotation/VAR_087929
http://togogenome.org/gene/9606:FOXD4L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6VB84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein D4-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301980
http://togogenome.org/gene/9606:MEI4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MW99                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Meiosis-specific protein MEI4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343703
http://togogenome.org/gene/9606:TCEAL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYN2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239216
http://togogenome.org/gene/9606:SP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K350|||http://purl.uniprot.org/uniprot/Q8IXZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 1.|||In isoform 2.|||In isoform 4.|||Polar residues|||Transcription factor Sp8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047152|||http://purl.uniprot.org/annotation/VSP_007441|||http://purl.uniprot.org/annotation/VSP_011036|||http://purl.uniprot.org/annotation/VSP_044094
http://togogenome.org/gene/9606:CT47A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:OR10A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H208                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 10A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261139|||http://purl.uniprot.org/annotation/VAR_034277|||http://purl.uniprot.org/annotation/VAR_034278|||http://purl.uniprot.org/annotation/VAR_034279|||http://purl.uniprot.org/annotation/VAR_053261|||http://purl.uniprot.org/annotation/VAR_060022
http://togogenome.org/gene/9606:NDFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT67                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with ITCH|||Interaction with UBE2L3|||Loss of phosphorylation; when associated with 41-P-Y-42 and 66-S-Y-67. Greatly decreases NEDD4-binding; when associated with 41-P-Y-42 and 66-S-Y-67. No effect on PTEN-binding; when associated with 41-P-Y-42 and 66-S-Y-67.|||Loss of phosphorylation; when associated with 41-P-Y-42 and 75-S-Y-76. Greatly decreases NEDD4-binding; when associated with 41-P-Y-42 and 75-S-Y-76. No effect on PTEN-binding; when associated with 41-P-Y-42 and 75-S-Y-76.|||Loss of phosphorylation; when associated with 66-S-Y-67 and 75-S-Y-76. Greatly decreases NEDD4-binding; when associated with 66-S-Y-67 and 75-S-Y-76. No effect on PTEN-binding; when associated with 66-S-Y-67 and 75-S-Y-76.|||N-acetylalanine|||NEDD4 family-interacting protein 1|||PPxY motif 1|||PPxY motif 2|||PPxY motif 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076269|||http://purl.uniprot.org/annotation/VSP_016474|||http://purl.uniprot.org/annotation/VSP_016475
http://togogenome.org/gene/9606:ZFYVE26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DK2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphatidylinositol 3-phosphate-binding and localization to the midbody.|||Basic and acidic residues|||Disordered|||FYVE-type|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Zinc finger FYVE domain-containing protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314612|||http://purl.uniprot.org/annotation/VAR_037987|||http://purl.uniprot.org/annotation/VAR_037988|||http://purl.uniprot.org/annotation/VAR_037989|||http://purl.uniprot.org/annotation/VAR_037990|||http://purl.uniprot.org/annotation/VAR_037991|||http://purl.uniprot.org/annotation/VAR_037992|||http://purl.uniprot.org/annotation/VAR_037993|||http://purl.uniprot.org/annotation/VAR_037994|||http://purl.uniprot.org/annotation/VAR_037995|||http://purl.uniprot.org/annotation/VAR_037996|||http://purl.uniprot.org/annotation/VAR_037997|||http://purl.uniprot.org/annotation/VSP_030338|||http://purl.uniprot.org/annotation/VSP_030339|||http://purl.uniprot.org/annotation/VSP_030340|||http://purl.uniprot.org/annotation/VSP_030341|||http://purl.uniprot.org/annotation/VSP_041049|||http://purl.uniprot.org/annotation/VSP_041050|||http://purl.uniprot.org/annotation/VSP_058963|||http://purl.uniprot.org/annotation/VSP_058964
http://togogenome.org/gene/9606:CSTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05048                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage stimulation factor subunit 1|||Hydrophobic|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050944
http://togogenome.org/gene/9606:UBN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPG3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly diminishes interaction with HIRA.|||Strongly diminishes interaction with HIRA; when associated with E-138 and L-139.|||Strongly diminishes interaction with HIRA; when associated with E-138 and L-140.|||Strongly diminishes interaction with HIRA; when associated with E-139 and L-140.|||Sufficient for interaction with HIRA|||Ubinuclein-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065712|||http://purl.uniprot.org/annotation/VAR_051465|||http://purl.uniprot.org/annotation/VSP_036971
http://togogenome.org/gene/9606:ARHGAP33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5D2|||http://purl.uniprot.org/uniprot/O14559                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||PX; atypical|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 33|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056721|||http://purl.uniprot.org/annotation/VSP_014287|||http://purl.uniprot.org/annotation/VSP_014288|||http://purl.uniprot.org/annotation/VSP_014289|||http://purl.uniprot.org/annotation/VSP_014290|||http://purl.uniprot.org/annotation/VSP_014291|||http://purl.uniprot.org/annotation/VSP_014292
http://togogenome.org/gene/9606:SLC25A37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 4.|||Mitoferrin-1|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235251|||http://purl.uniprot.org/annotation/VAR_043144|||http://purl.uniprot.org/annotation/VAR_043145|||http://purl.uniprot.org/annotation/VSP_018400|||http://purl.uniprot.org/annotation/VSP_018402|||http://purl.uniprot.org/annotation/VSP_018403
http://togogenome.org/gene/9606:CDC26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHZ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region                                                                                  ^@                                                                                  Anaphase-promoting complex subunit CDC26|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271194
http://togogenome.org/gene/9606:TNFRSF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0R7FDM1|||http://purl.uniprot.org/uniprot/Q9Y5U5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034595|||http://purl.uniprot.org/annotation/PRO_5006587680|||http://purl.uniprot.org/annotation/VAR_052354|||http://purl.uniprot.org/annotation/VAR_052355|||http://purl.uniprot.org/annotation/VAR_052356|||http://purl.uniprot.org/annotation/VAR_052357|||http://purl.uniprot.org/annotation/VSP_006508|||http://purl.uniprot.org/annotation/VSP_041021
http://togogenome.org/gene/9606:NEK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC98                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Autoinhibitory|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increase in catalytic activity.|||Interaction with APBB1|||Interaction with ARHGAP33, ANKRA2, CDC42, PRDX3, RAD26L, RBBP6, RPS7 and TRIP4|||Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-74.|||Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-75.|||Phosphoserine|||Phosphoserine; by NEK9|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086427|||http://purl.uniprot.org/annotation/VSP_041798|||http://purl.uniprot.org/annotation/VSP_041799|||http://purl.uniprot.org/annotation/VSP_041800
http://togogenome.org/gene/9606:EPS8L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE68                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Epidermal growth factor receptor kinase substrate 8-like protein 1|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||PTB|||Phosphoserine|||Phosphothreonine|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239082|||http://purl.uniprot.org/annotation/VAR_056870|||http://purl.uniprot.org/annotation/VAR_060375|||http://purl.uniprot.org/annotation/VAR_060376|||http://purl.uniprot.org/annotation/VAR_060377|||http://purl.uniprot.org/annotation/VAR_061647|||http://purl.uniprot.org/annotation/VSP_019082|||http://purl.uniprot.org/annotation/VSP_019083|||http://purl.uniprot.org/annotation/VSP_019084|||http://purl.uniprot.org/annotation/VSP_019085|||http://purl.uniprot.org/annotation/VSP_019086|||http://purl.uniprot.org/annotation/VSP_019087|||http://purl.uniprot.org/annotation/VSP_019088|||http://purl.uniprot.org/annotation/VSP_019089
http://togogenome.org/gene/9606:DYNC1I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE9|||http://purl.uniprot.org/uniprot/B4DPZ3|||http://purl.uniprot.org/uniprot/Q13409                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic dynein 1 intermediate chain 2|||Diphosphoserine|||Disordered|||In NEDMIBA; loss-of-function variant; does not rescue neurodevelopmental defects in zebrafish morphants.|||In isoform 2B, isoform 2C and isoform 2F.|||In isoform 2C, isoform 2F and isoform 3.|||In isoform 2E and isoform 2F.|||In isoform 3.|||Likely benign variant; can rescue neurodevelopmental defects in zebrafish morphants.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114655|||http://purl.uniprot.org/annotation/VAR_082947|||http://purl.uniprot.org/annotation/VAR_082948|||http://purl.uniprot.org/annotation/VAR_082949|||http://purl.uniprot.org/annotation/VSP_001336|||http://purl.uniprot.org/annotation/VSP_001337|||http://purl.uniprot.org/annotation/VSP_023011|||http://purl.uniprot.org/annotation/VSP_054377
http://togogenome.org/gene/9606:SERPINE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MV23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reactive bond|||Serpin E3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340684|||http://purl.uniprot.org/annotation/VAR_044021|||http://purl.uniprot.org/annotation/VSP_037586
http://togogenome.org/gene/9606:IL12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60595|||http://purl.uniprot.org/uniprot/P29459                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Interchain (with C-199 in IL12B)|||Interleukin-12 subunit alpha|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015604
http://togogenome.org/gene/9606:BEX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBH7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||His cluster|||Phosphoserine|||Protein BEX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229772|||http://purl.uniprot.org/annotation/VAR_025756|||http://purl.uniprot.org/annotation/VAR_025757|||http://purl.uniprot.org/annotation/VAR_042667|||http://purl.uniprot.org/annotation/VAR_042668|||http://purl.uniprot.org/annotation/VAR_042669|||http://purl.uniprot.org/annotation/VAR_042670|||http://purl.uniprot.org/annotation/VAR_042671
http://togogenome.org/gene/9606:ADCYAP1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8F8|||http://purl.uniprot.org/uniprot/A0A994J7E9|||http://purl.uniprot.org/uniprot/P41586                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for ligand binding and specificity|||In isoform N-HOP1 and isoform S-HOP1.|||In isoform S, isoform S-HOP1 and isoform VS.|||In isoform VS.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pituitary adenylate cyclase-activating polypeptide type I receptor|||Reduced affinity for ADCYAP1.|||Strongly reduced affinity for ADCYAP1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012841|||http://purl.uniprot.org/annotation/PRO_5001860384|||http://purl.uniprot.org/annotation/PRO_5038627612|||http://purl.uniprot.org/annotation/VSP_042669|||http://purl.uniprot.org/annotation/VSP_042670|||http://purl.uniprot.org/annotation/VSP_042671
http://togogenome.org/gene/9606:DPEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4A9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dipeptidase 2|||GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231603|||http://purl.uniprot.org/annotation/PRO_0000231604|||http://purl.uniprot.org/annotation/VAR_033894|||http://purl.uniprot.org/annotation/VAR_060230|||http://purl.uniprot.org/annotation/VSP_017851|||http://purl.uniprot.org/annotation/VSP_059428|||http://purl.uniprot.org/annotation/VSP_059429
http://togogenome.org/gene/9606:IL27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEV9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interleukin-27 subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320139|||http://purl.uniprot.org/annotation/VAR_039140|||http://purl.uniprot.org/annotation/VAR_039141
http://togogenome.org/gene/9606:PRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  C-type lectin|||Proteoglycan 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250421|||http://purl.uniprot.org/annotation/VAR_050117|||http://purl.uniprot.org/annotation/VAR_050118
http://togogenome.org/gene/9606:FSCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14926                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  Fascin-2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219382|||http://purl.uniprot.org/annotation/VSP_047285
http://togogenome.org/gene/9606:CIMAP1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SX64                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Protein CIMAP1D|||STPGR 1|||STPGR 2|||STPGR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274520|||http://purl.uniprot.org/annotation/VAR_053951|||http://purl.uniprot.org/annotation/VSP_022778
http://togogenome.org/gene/9606:WAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTA9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient severe intellectual disability.|||WW|||WW domain-containing adapter protein with coiled-coil                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254558|||http://purl.uniprot.org/annotation/VAR_028838|||http://purl.uniprot.org/annotation/VAR_028839|||http://purl.uniprot.org/annotation/VAR_036351|||http://purl.uniprot.org/annotation/VAR_053448|||http://purl.uniprot.org/annotation/VAR_078694|||http://purl.uniprot.org/annotation/VSP_021230|||http://purl.uniprot.org/annotation/VSP_021231|||http://purl.uniprot.org/annotation/VSP_021233|||http://purl.uniprot.org/annotation/VSP_021236
http://togogenome.org/gene/9606:LRRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RV3|||http://purl.uniprot.org/uniprot/Q5S007                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased kinase activity and loss of RAB29-mediated activation.|||Decreased kinase activity. Loss of RAB29-mediated activation and autophosphorylation of S-910, S-935, S-955, S-973 and S-1292. Decreased membrane association; when associated with G-1441, C-1699 and S-2019.|||Decreased kinase activity; when associated with G-1343.|||Decreased kinase activity; when associated with Q-1398.|||Decreased membrane association when associated with D-727, D-728, or D-729. Inhibits autophosphorylation and RAB10 phosphorylation when associated with N-1348 or A-2017.|||Decreases WD domain homodimerization.|||Decreases WD domain homodimerization. Increases kinase activity and autophosphorylation at Ser-1292.|||Decreases WD domain homodimerization. No effect on kinase activity.|||Does not inhibit interaction with RAB29; shows a progressive increase in neurite length and branching.|||Found in a renal cell carcinoma sample; somatic mutation.|||GTPase-dead mutant. Loss of interaction with SEC16A and impaired ability to recruit SEC16A to endoplasmic reticulum exit sites.|||In PARK8.|||In PARK8; no effect on WD domain homodimerization; no effect on kinase activity.|||In PARK8; shows a progressive reduction in neurite length and branching; shows an increase in activity in phosphorylation of RAB8A and RAB10; decreases phosphorylation-dependent binding to YWHAG.|||In PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB10; decreases phosphorylation-dependent binding to YWHAG.|||In PARK8; shows an increase in activity in both autophosphorylation and phosphorylation of a generic substrate; results in increased PRDX3 phosphorylation promoting dysregulation of mitochondrial function and oxidative damage; results in increased APP phosphorylation on 'T-743' promoting neurotoxicity in dopaminergic neurons; shows increased kinase activity in the phosphorylation of RAB10; does not inhibit interaction with RAB29; shows a progressive reduction in neurite length and branching; shows distinctive spheroid-like inclusions within both neuronal processes and at intracellular membranous structures; shows lysosomal swelling and reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows apoptotic mechanism of cell death; no loss of interaction with SEC16A.|||In PARK8; shows an increase in activity in phosphorylation of RAB8A and RAB10.|||In PARK8; shows an increase in activity in phosphorylation of RAB8A and RAB10; decreases phosphorylation-dependent binding to YWHAG.|||In PARK8; shows decreased WD domain homodimerization; no effect on kinase activity.|||In PARK8; shows no progressive reduction in neurite length and branching; no loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB8A and RAB10.|||In PARK8; significant increase in autophosphorylation of about 40% in comparison to wild-type protein in vitro; shows a progressive reduction in neurite length and branching; shows an increase in activity in phosphorylation of RAB8A and RAB10.|||In PARK8; under conditions of oxidative stress the variant protein is more toxic and is associated with a higher rate of apoptosis; reduced binding to synaptic vesicles; no loss of interaction with SEC16A; shows an increase in activity in phosphorylation of RAB8A and RAB10; shows decreased WD domain homodimerization; reduced autophosphorylation at Ser-935.|||In PARK8; unknown pathological significance.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||Increases kinase activity.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat serine/threonine-protein kinase 2|||Loss of GTP binding. Inhibits autophosphorylation and RAB10 phosphorylation; when associated with G-1441, C-1699, or S-2019.|||Loss of kinase activity and ability to enhance NOD2 signaling.|||Loss of kinase activity.|||Loss of kinase activity. Decreases proteasomal degradation of MAPT; when associated with A-1906 and N-1994. Loss of phosphorylation of RAB10; when associated with G-1441, C-1699, or S-2019.|||Loss of kinase activity. Decreases proteasomal degradation of MAPT; when associated with N-1994 and A-2017.|||Loss of kinase activity. No loss of interaction with SEC16A and no loss of ability to recruit SEC16A to endoplasmic reticulum exit sites. Decreases proteasomal degradation of MAPT; when associated with A-1906 and A-2017.|||May be associated with Parkinson disease in some populations.|||No effect on WD domain homodimerization. No effect on kinase activity.|||No effect on kinase activity and RAB29-mediated activation.|||Phosphoserine|||Protein kinase|||Proton acceptor|||Required for RAB29-mediated activation|||Roc|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086238|||http://purl.uniprot.org/annotation/VAR_024931|||http://purl.uniprot.org/annotation/VAR_024932|||http://purl.uniprot.org/annotation/VAR_024933|||http://purl.uniprot.org/annotation/VAR_024934|||http://purl.uniprot.org/annotation/VAR_024935|||http://purl.uniprot.org/annotation/VAR_024936|||http://purl.uniprot.org/annotation/VAR_024937|||http://purl.uniprot.org/annotation/VAR_024938|||http://purl.uniprot.org/annotation/VAR_024939|||http://purl.uniprot.org/annotation/VAR_024940|||http://purl.uniprot.org/annotation/VAR_024941|||http://purl.uniprot.org/annotation/VAR_024942|||http://purl.uniprot.org/annotation/VAR_024943|||http://purl.uniprot.org/annotation/VAR_024944|||http://purl.uniprot.org/annotation/VAR_024945|||http://purl.uniprot.org/annotation/VAR_024946|||http://purl.uniprot.org/annotation/VAR_024947|||http://purl.uniprot.org/annotation/VAR_024948|||http://purl.uniprot.org/annotation/VAR_024949|||http://purl.uniprot.org/annotation/VAR_024950|||http://purl.uniprot.org/annotation/VAR_024951|||http://purl.uniprot.org/annotation/VAR_024952|||http://purl.uniprot.org/annotation/VAR_024953|||http://purl.uniprot.org/annotation/VAR_024954|||http://purl.uniprot.org/annotation/VAR_024955|||http://purl.uniprot.org/annotation/VAR_024956|||http://purl.uniprot.org/annotation/VAR_024957|||http://purl.uniprot.org/annotation/VAR_024958|||http://purl.uniprot.org/annotation/VAR_024959|||http://purl.uniprot.org/annotation/VAR_024960|||http://purl.uniprot.org/annotation/VAR_024961|||http://purl.uniprot.org/annotation/VAR_024962|||http://purl.uniprot.org/annotation/VAR_024963|||http://purl.uniprot.org/annotation/VAR_024964|||http://purl.uniprot.org/annotation/VAR_024965|||http://purl.uniprot.org/annotation/VAR_033903|||http://purl.uniprot.org/annotation/VAR_033904|||http://purl.uniprot.org/annotation/VAR_040678|||http://purl.uniprot.org/annotation/VAR_040679|||http://purl.uniprot.org/annotation/VAR_047022|||http://purl.uniprot.org/annotation/VAR_054740|||http://purl.uniprot.org/annotation/VAR_054741|||http://purl.uniprot.org/annotation/VAR_054742|||http://purl.uniprot.org/annotation/VAR_054743|||http://purl.uniprot.org/annotation/VAR_054744|||http://purl.uniprot.org/annotation/VAR_054745|||http://purl.uniprot.org/annotation/VAR_054746|||http://purl.uniprot.org/annotation/VAR_054747|||http://purl.uniprot.org/annotation/VAR_054748|||http://purl.uniprot.org/annotation/VAR_054749|||http://purl.uniprot.org/annotation/VAR_054750|||http://purl.uniprot.org/annotation/VAR_064728|||http://purl.uniprot.org/annotation/VAR_071101|||http://purl.uniprot.org/annotation/VAR_082047|||http://purl.uniprot.org/annotation/VAR_082048|||http://purl.uniprot.org/annotation/VAR_082049|||http://purl.uniprot.org/annotation/VAR_082050|||http://purl.uniprot.org/annotation/VAR_082051
http://togogenome.org/gene/9606:CDIPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3L7|||http://purl.uniprot.org/uniprot/O14735                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CDP-diacylglycerol--inositol 3-phosphatidyltransferase|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056802|||http://purl.uniprot.org/annotation/VAR_048734|||http://purl.uniprot.org/annotation/VSP_013618|||http://purl.uniprot.org/annotation/VSP_013619|||http://purl.uniprot.org/annotation/VSP_013620|||http://purl.uniprot.org/annotation/VSP_054767
http://togogenome.org/gene/9606:TLCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||TLC|||TLC domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285677|||http://purl.uniprot.org/annotation/VSP_055726
http://togogenome.org/gene/9606:REV3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60673|||http://purl.uniprot.org/uniprot/Q9UG47                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CysA-type|||CysB motif|||DNA polymerase zeta catalytic subunit|||DNA-directed DNA polymerase family B multifunctional|||DUF1725|||Disordered|||In isoform 2.|||Loss of DNA polymerase catalytic activity; when associated with N-2614.|||Loss of DNA polymerase catalytic activity; when associated with N-2783.|||Mediates interaction with MAD2L2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046468|||http://purl.uniprot.org/annotation/VAR_008516|||http://purl.uniprot.org/annotation/VAR_008517|||http://purl.uniprot.org/annotation/VAR_008518|||http://purl.uniprot.org/annotation/VAR_008519|||http://purl.uniprot.org/annotation/VAR_016147|||http://purl.uniprot.org/annotation/VAR_022226|||http://purl.uniprot.org/annotation/VAR_022227|||http://purl.uniprot.org/annotation/VAR_022228|||http://purl.uniprot.org/annotation/VAR_022229|||http://purl.uniprot.org/annotation/VAR_022230|||http://purl.uniprot.org/annotation/VAR_022231|||http://purl.uniprot.org/annotation/VAR_022232|||http://purl.uniprot.org/annotation/VAR_022233|||http://purl.uniprot.org/annotation/VAR_022234|||http://purl.uniprot.org/annotation/VAR_022235|||http://purl.uniprot.org/annotation/VAR_022236|||http://purl.uniprot.org/annotation/VAR_022237|||http://purl.uniprot.org/annotation/VAR_022238|||http://purl.uniprot.org/annotation/VAR_022239|||http://purl.uniprot.org/annotation/VAR_022240|||http://purl.uniprot.org/annotation/VAR_022241|||http://purl.uniprot.org/annotation/VAR_022242|||http://purl.uniprot.org/annotation/VAR_022243|||http://purl.uniprot.org/annotation/VAR_022244|||http://purl.uniprot.org/annotation/VAR_048883|||http://purl.uniprot.org/annotation/VAR_048884|||http://purl.uniprot.org/annotation/VAR_048885|||http://purl.uniprot.org/annotation/VSP_024121
http://togogenome.org/gene/9606:PCDHA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  6 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||PXXP 6|||Polar residues|||Protocadherin alpha-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003904|||http://purl.uniprot.org/annotation/VAR_048538|||http://purl.uniprot.org/annotation/VAR_048539|||http://purl.uniprot.org/annotation/VSP_000693|||http://purl.uniprot.org/annotation/VSP_000694
http://togogenome.org/gene/9606:GNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62879|||http://purl.uniprot.org/uniprot/Q6FHM2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2|||In NEDHYDF.|||In SSS4; leads to a sustained activation of cardiac G protein-coupled inwardly-rectifying potassium (GIRK) channels, which is likely to hyperpolarize the myocellular membrane potential and reduce their spontaneous activity; does not affect protein levels, subcellular location, nor interaction with GNAI2 and GNG2.|||In isoform 2.|||N-acetylserine|||Phosphotyrosine|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127695|||http://purl.uniprot.org/annotation/VAR_086042|||http://purl.uniprot.org/annotation/VAR_086043|||http://purl.uniprot.org/annotation/VAR_086044|||http://purl.uniprot.org/annotation/VAR_086045|||http://purl.uniprot.org/annotation/VAR_086046|||http://purl.uniprot.org/annotation/VAR_086047|||http://purl.uniprot.org/annotation/VAR_086048|||http://purl.uniprot.org/annotation/VSP_056515
http://togogenome.org/gene/9606:CRAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43155                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carnitine O-acetyltransferase|||In NBIA8; unknown pathological significance; loss of expression at the protein level and drastic decrease in beta-oxidation of palmitate in homozygous patient's primary fibroblasts as compared to wild-type cells; primary fibroblasts from a homozygous patient show much higher intracellular iron content than fibroblasts from control individuals and abnormally elevated levels of transferrin receptor 1/TFRC at the cell surface.|||In isoform 2.|||In isoform 3.|||Increases the KM for carnitine 100-fold.|||Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold.|||Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold.|||Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold.|||Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210172|||http://purl.uniprot.org/annotation/VAR_047780|||http://purl.uniprot.org/annotation/VAR_047781|||http://purl.uniprot.org/annotation/VAR_080636|||http://purl.uniprot.org/annotation/VSP_000792|||http://purl.uniprot.org/annotation/VSP_012798
http://togogenome.org/gene/9606:TUBB4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68371                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Acidic residues|||Disordered|||In LCAEOD; affects microtubules polymerization.|||MREI motif|||N6-acetyllysine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta-4B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048248|||http://purl.uniprot.org/annotation/VAR_080782|||http://purl.uniprot.org/annotation/VAR_080783
http://togogenome.org/gene/9606:MRPS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DP77|||http://purl.uniprot.org/uniprot/P82664                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Small ribosomal subunit protein uS10|||Small ribosomal subunit protein uS10m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146675
http://togogenome.org/gene/9606:PAK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96013                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Approximately 3-fold increased autophosphorylation.|||Approximately 30-fold increased autophosphorylation (constitutively active mutant).|||Basic and acidic residues|||CRIB|||Disordered|||GEF-interaction domain (GID)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Linker|||N6-methyllysine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086474|||http://purl.uniprot.org/annotation/VAR_040970|||http://purl.uniprot.org/annotation/VAR_040971|||http://purl.uniprot.org/annotation/VSP_004892|||http://purl.uniprot.org/annotation/VSP_004893|||http://purl.uniprot.org/annotation/VSP_017572|||http://purl.uniprot.org/annotation/VSP_017573
http://togogenome.org/gene/9606:NBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTY6|||http://purl.uniprot.org/uniprot/P41271                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  CTCK|||Disordered|||In isoform 2.|||Neuroblastoma suppressor of tumorigenicity 1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006722|||http://purl.uniprot.org/annotation/VSP_036438
http://togogenome.org/gene/9606:LPXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5P7|||http://purl.uniprot.org/uniprot/O60711                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LD motif 1|||LD motif 2|||LD motif 3|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Leupaxin|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by LYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075836|||http://purl.uniprot.org/annotation/VAR_050152|||http://purl.uniprot.org/annotation/VSP_042655
http://togogenome.org/gene/9606:NACC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RE7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BEN|||BTB|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NECFM.|||Nucleus accumbens-associated protein 1|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274041|||http://purl.uniprot.org/annotation/VAR_078808
http://togogenome.org/gene/9606:TXK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42681                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Impairs kinase activity.|||Nuclear localization signal|||Phosphotyrosine; by FYN and autocatalysis|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces expression levels if IFN-gamma.|||SH2|||SH3|||Tyrosine-protein kinase TXK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088175|||http://purl.uniprot.org/annotation/VAR_028368|||http://purl.uniprot.org/annotation/VAR_028369|||http://purl.uniprot.org/annotation/VAR_041869
http://togogenome.org/gene/9606:APOBEC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y235                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  C->U-editing enzyme APOBEC-2|||CMP/dCMP-type deaminase|||Disordered|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171749|||http://purl.uniprot.org/annotation/VAR_024406
http://togogenome.org/gene/9606:SLC14A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15849                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Urea transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065739|||http://purl.uniprot.org/annotation/VAR_038690|||http://purl.uniprot.org/annotation/VAR_057016|||http://purl.uniprot.org/annotation/VAR_057017|||http://purl.uniprot.org/annotation/VAR_057018|||http://purl.uniprot.org/annotation/VAR_060255|||http://purl.uniprot.org/annotation/VAR_060256|||http://purl.uniprot.org/annotation/VSP_031171
http://togogenome.org/gene/9606:BHMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2M3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Hcy-binding|||In isoform 2.|||Phosphoserine|||S-methylmethionine--homocysteine S-methyltransferase BHMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273224|||http://purl.uniprot.org/annotation/VSP_042938
http://togogenome.org/gene/9606:SPAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38567|||http://purl.uniprot.org/uniprot/Q5D1J4                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a renal cell carcinoma sample; somatic mutation.|||GPI-anchor amidated serine|||Helical|||Hyaluronidase PH-20|||In isoform 2.|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||Proton donor|||Reduces activity by 80%.|||Reduces activity by over 90%.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012089|||http://purl.uniprot.org/annotation/PRO_0000012090|||http://purl.uniprot.org/annotation/VAR_049213|||http://purl.uniprot.org/annotation/VAR_064756|||http://purl.uniprot.org/annotation/VSP_042714
http://togogenome.org/gene/9606:RNF186                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXI6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RNF186|||Exhibits a reduced ability to ubiquitinate EPHB2 but retained ability to ubiquitinate EPHB3.|||Helical|||Loss of ability to decrease SESN2 protein.|||Loss of autoubiquitination; loss of BNIP1 polyubiquitination; no effect on interaction with BNIP1; decreased effect on calcium release from the endoplasmic reticulum.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261624|||http://purl.uniprot.org/annotation/VAR_029460|||http://purl.uniprot.org/annotation/VAR_052111
http://togogenome.org/gene/9606:IL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D4HNR6|||http://purl.uniprot.org/uniprot/P05112|||http://purl.uniprot.org/uniprot/Q5FC01                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  About 500-fold lower interaction with IL4R than WT.|||In isoform 2.|||Interleukin-4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015532|||http://purl.uniprot.org/annotation/PRO_5014302578|||http://purl.uniprot.org/annotation/PRO_5014309781|||http://purl.uniprot.org/annotation/VAR_020392|||http://purl.uniprot.org/annotation/VSP_002672
http://togogenome.org/gene/9606:EHHADH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08426                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  3-hydroxyacyl-CoA dehydrogenase|||Enoyl-CoA hydratase / isomerase|||Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.|||Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.|||Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.|||Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.|||Important for catalytic activity|||In FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells.|||In isoform 2.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Peroxisomal bifunctional enzyme|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109247|||http://purl.uniprot.org/annotation/VAR_047132|||http://purl.uniprot.org/annotation/VAR_047133|||http://purl.uniprot.org/annotation/VAR_047134|||http://purl.uniprot.org/annotation/VAR_047135|||http://purl.uniprot.org/annotation/VAR_047136|||http://purl.uniprot.org/annotation/VAR_054329|||http://purl.uniprot.org/annotation/VAR_054330|||http://purl.uniprot.org/annotation/VAR_054331|||http://purl.uniprot.org/annotation/VAR_054332|||http://purl.uniprot.org/annotation/VAR_070949|||http://purl.uniprot.org/annotation/VSP_042811
http://togogenome.org/gene/9606:ZFP91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitination of MAP3K14/NIK; when associated with A-344.|||Abolishes ubiquitination of MAP3K14/NIK; when associated with A-349.|||Acidic residues|||Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||E3 ubiquitin-protein ligase ZFP91|||In isoform 2.|||Interaction with MAP3K14/NIK|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047312|||http://purl.uniprot.org/annotation/VAR_021889|||http://purl.uniprot.org/annotation/VAR_032454|||http://purl.uniprot.org/annotation/VSP_012686|||http://purl.uniprot.org/annotation/VSP_012687
http://togogenome.org/gene/9606:HPCAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGW9|||http://purl.uniprot.org/uniprot/Q9UM19                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Hippocalcin-like protein 4|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073777
http://togogenome.org/gene/9606:SRCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRS2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||Acidic residues|||Basic and acidic residues|||Disordered|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||Helicase SRCAP|||In DEHMBA.|||In FLHS.|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311236|||http://purl.uniprot.org/annotation/VAR_086403|||http://purl.uniprot.org/annotation/VAR_086404|||http://purl.uniprot.org/annotation/VAR_086405|||http://purl.uniprot.org/annotation/VAR_086406|||http://purl.uniprot.org/annotation/VAR_086407|||http://purl.uniprot.org/annotation/VAR_086408|||http://purl.uniprot.org/annotation/VAR_086409|||http://purl.uniprot.org/annotation/VSP_029441|||http://purl.uniprot.org/annotation/VSP_029442
http://togogenome.org/gene/9606:BTN1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13410|||http://purl.uniprot.org/uniprot/Q4VAN2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin subfamily 1 member A1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014527|||http://purl.uniprot.org/annotation/PRO_5004245482|||http://purl.uniprot.org/annotation/VAR_021169|||http://purl.uniprot.org/annotation/VAR_026546|||http://purl.uniprot.org/annotation/VAR_030770|||http://purl.uniprot.org/annotation/VAR_061302
http://togogenome.org/gene/9606:LCOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JN0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH psq-type|||In isoform 2.|||In isoform 3.|||Interaction with nuclear receptors|||Ligand-dependent corepressor|||Loss of estradiol-dependent interaction with ESR1 and ESR2.|||N6,N6-dimethyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236807|||http://purl.uniprot.org/annotation/VSP_018585|||http://purl.uniprot.org/annotation/VSP_018586|||http://purl.uniprot.org/annotation/VSP_058760
http://togogenome.org/gene/9606:FKBP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8G6|||http://purl.uniprot.org/uniprot/Q14318                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-149.|||Abolishes calcium-binding and reduces affinity for BCL2; when associated with Asn-151.|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform 2.|||In isoform 3.|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP8|||Phosphoserine|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075331|||http://purl.uniprot.org/annotation/VAR_044225|||http://purl.uniprot.org/annotation/VSP_034486|||http://purl.uniprot.org/annotation/VSP_047717
http://togogenome.org/gene/9606:PTAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6K3                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||PFTA 1|||PFTA 2|||PFTA 3|||PFTA 4|||PFTA 5|||Protein prenyltransferase alpha subunit repeat-containing protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316843
http://togogenome.org/gene/9606:RILPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVV3|||http://purl.uniprot.org/uniprot/Q5EBL4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Loss of interaction with RAB8A and RAB10.|||Loss of interaction with RAB8A.|||No loss of interaction with RAB8A.|||Phosphoserine|||RH1|||RH2|||RILP-like protein 1|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299310|||http://purl.uniprot.org/annotation/VSP_027605|||http://purl.uniprot.org/annotation/VSP_027606|||http://purl.uniprot.org/annotation/VSP_027607|||http://purl.uniprot.org/annotation/VSP_027608
http://togogenome.org/gene/9606:USP28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLZ9|||http://purl.uniprot.org/uniprot/B4E3L3|||http://purl.uniprot.org/uniprot/Q96RU2                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes deubiquitinase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Prevents ZNF304 ubiquitination reduction.|||Proton acceptor|||UIM|||USP|||Ubiquitin carboxyl-terminal hydrolase 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080657|||http://purl.uniprot.org/annotation/VSP_015580|||http://purl.uniprot.org/annotation/VSP_057359|||http://purl.uniprot.org/annotation/VSP_057360
http://togogenome.org/gene/9606:SLC16A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95907                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes basolateral membrane localization; when associated with A-471.|||Abolishes basolateral membrane localization; when associated with A-472.|||Affects subcellular localization leading to apical localization.|||Affects subcellular localization leading to apical localization; when associated with A-481.|||Affects subcellular localization leading to apical localization; when associated with A-482.|||Basic and acidic residues|||Basolateral sorting signal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Monocarboxylate transporter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211390|||http://purl.uniprot.org/annotation/VAR_053654|||http://purl.uniprot.org/annotation/VAR_060107
http://togogenome.org/gene/9606:FNIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P278                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished GTPase activation (GAP) activity of FLCN.|||Basic and acidic residues|||Disordered|||Folliculin-interacting protein 2|||In isoform 2.|||Interaction with PRKAA1|||Phosphoserine|||Polar residues|||cDENN FNIP1/2-type|||dDENN FNIP1/2-type|||uDENN FNIP1/2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320553|||http://purl.uniprot.org/annotation/VAR_045612|||http://purl.uniprot.org/annotation/VSP_031656
http://togogenome.org/gene/9606:CHD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWF9|||http://purl.uniprot.org/uniprot/Q9P2D1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 7|||DEAH box|||Disordered|||Found in a patient with cleft lip and palate; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||In CHARGES and HH5.|||In CHARGES and HH5; has no effect on interaction with CHD8.|||In CHARGES and HH5; unknown pathological significance.|||In CHARGES.|||In CHARGES; no effect on interaction with CHD8.|||In CHARGES; unknown pathological significance.|||In CHARGES; unknown pathological significance; has no effect on interaction with CHD8.|||In HH5.|||In HH5; phenotype consistent with Kallmann syndrome.|||In HH5; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080232|||http://purl.uniprot.org/annotation/VAR_021059|||http://purl.uniprot.org/annotation/VAR_021060|||http://purl.uniprot.org/annotation/VAR_033245|||http://purl.uniprot.org/annotation/VAR_033246|||http://purl.uniprot.org/annotation/VAR_033247|||http://purl.uniprot.org/annotation/VAR_033248|||http://purl.uniprot.org/annotation/VAR_033249|||http://purl.uniprot.org/annotation/VAR_033250|||http://purl.uniprot.org/annotation/VAR_033251|||http://purl.uniprot.org/annotation/VAR_048731|||http://purl.uniprot.org/annotation/VAR_054623|||http://purl.uniprot.org/annotation/VAR_054624|||http://purl.uniprot.org/annotation/VAR_054625|||http://purl.uniprot.org/annotation/VAR_054626|||http://purl.uniprot.org/annotation/VAR_054627|||http://purl.uniprot.org/annotation/VAR_068104|||http://purl.uniprot.org/annotation/VAR_068105|||http://purl.uniprot.org/annotation/VAR_068106|||http://purl.uniprot.org/annotation/VAR_068107|||http://purl.uniprot.org/annotation/VAR_068108|||http://purl.uniprot.org/annotation/VAR_068109|||http://purl.uniprot.org/annotation/VAR_068110|||http://purl.uniprot.org/annotation/VAR_068111|||http://purl.uniprot.org/annotation/VAR_068112|||http://purl.uniprot.org/annotation/VAR_068113|||http://purl.uniprot.org/annotation/VAR_068114|||http://purl.uniprot.org/annotation/VAR_068115|||http://purl.uniprot.org/annotation/VAR_068116|||http://purl.uniprot.org/annotation/VAR_068117|||http://purl.uniprot.org/annotation/VAR_068118|||http://purl.uniprot.org/annotation/VAR_068119|||http://purl.uniprot.org/annotation/VAR_068120|||http://purl.uniprot.org/annotation/VAR_068121|||http://purl.uniprot.org/annotation/VAR_068122|||http://purl.uniprot.org/annotation/VAR_068123|||http://purl.uniprot.org/annotation/VAR_068124|||http://purl.uniprot.org/annotation/VAR_068125|||http://purl.uniprot.org/annotation/VAR_068126|||http://purl.uniprot.org/annotation/VAR_068127|||http://purl.uniprot.org/annotation/VAR_068128|||http://purl.uniprot.org/annotation/VAR_068129|||http://purl.uniprot.org/annotation/VAR_068130|||http://purl.uniprot.org/annotation/VAR_068131|||http://purl.uniprot.org/annotation/VAR_068132|||http://purl.uniprot.org/annotation/VAR_068133|||http://purl.uniprot.org/annotation/VAR_068134|||http://purl.uniprot.org/annotation/VAR_068135|||http://purl.uniprot.org/annotation/VAR_068136|||http://purl.uniprot.org/annotation/VAR_068137|||http://purl.uniprot.org/annotation/VAR_068138|||http://purl.uniprot.org/annotation/VAR_068139|||http://purl.uniprot.org/annotation/VAR_068140|||http://purl.uniprot.org/annotation/VAR_068141|||http://purl.uniprot.org/annotation/VAR_068142|||http://purl.uniprot.org/annotation/VAR_068143|||http://purl.uniprot.org/annotation/VAR_068144|||http://purl.uniprot.org/annotation/VAR_068145|||http://purl.uniprot.org/annotation/VAR_068146|||http://purl.uniprot.org/annotation/VAR_068147|||http://purl.uniprot.org/annotation/VAR_068148|||http://purl.uniprot.org/annotation/VAR_068149|||http://purl.uniprot.org/annotation/VAR_068150|||http://purl.uniprot.org/annotation/VAR_068151|||http://purl.uniprot.org/annotation/VAR_068152|||http://purl.uniprot.org/annotation/VAR_068153|||http://purl.uniprot.org/annotation/VAR_068154|||http://purl.uniprot.org/annotation/VAR_068155|||http://purl.uniprot.org/annotation/VAR_068156|||http://purl.uniprot.org/annotation/VAR_068157|||http://purl.uniprot.org/annotation/VAR_068158|||http://purl.uniprot.org/annotation/VAR_068159|||http://purl.uniprot.org/annotation/VAR_068160|||http://purl.uniprot.org/annotation/VAR_068374|||http://purl.uniprot.org/annotation/VAR_068375|||http://purl.uniprot.org/annotation/VAR_068376|||http://purl.uniprot.org/annotation/VAR_068377|||http://purl.uniprot.org/annotation/VAR_068378|||http://purl.uniprot.org/annotation/VAR_068379|||http://purl.uniprot.org/annotation/VAR_068380|||http://purl.uniprot.org/annotation/VAR_068381|||http://purl.uniprot.org/annotation/VAR_068382|||http://purl.uniprot.org/annotation/VAR_068383|||http://purl.uniprot.org/annotation/VAR_068384|||http://purl.uniprot.org/annotation/VAR_068385|||http://purl.uniprot.org/annotation/VAR_068386|||http://purl.uniprot.org/annotation/VAR_068387|||http://purl.uniprot.org/annotation/VAR_068388|||http://purl.uniprot.org/annotation/VAR_068389|||http://purl.uniprot.org/annotation/VAR_068390|||http://purl.uniprot.org/annotation/VAR_068391|||http://purl.uniprot.org/annotation/VAR_068392|||http://purl.uniprot.org/annotation/VAR_068393|||http://purl.uniprot.org/annotation/VAR_068394|||http://purl.uniprot.org/annotation/VAR_068395|||http://purl.uniprot.org/annotation/VAR_068396|||http://purl.uniprot.org/annotation/VAR_068397|||http://purl.uniprot.org/annotation/VAR_068398|||http://purl.uniprot.org/annotation/VAR_068399|||http://purl.uniprot.org/annotation/VAR_068400|||http://purl.uniprot.org/annotation/VAR_068401|||http://purl.uniprot.org/annotation/VAR_068402|||http://purl.uniprot.org/annotation/VAR_068403|||http://purl.uniprot.org/annotation/VAR_068404|||http://purl.uniprot.org/annotation/VAR_068405|||http://purl.uniprot.org/annotation/VAR_068406|||http://purl.uniprot.org/annotation/VAR_068407|||http://purl.uniprot.org/annotation/VAR_068408|||http://purl.uniprot.org/annotation/VAR_068409|||http://purl.uniprot.org/annotation/VAR_068410|||http://purl.uniprot.org/annotation/VAR_068411|||http://purl.uniprot.org/annotation/VAR_068412|||http://purl.uniprot.org/annotation/VAR_068413|||http://purl.uniprot.org/annotation/VAR_068414|||http://purl.uniprot.org/annotation/VAR_068415|||http://purl.uniprot.org/annotation/VAR_068416|||http://purl.uniprot.org/annotation/VAR_068417|||http://purl.uniprot.org/annotation/VAR_068418|||http://purl.uniprot.org/annotation/VAR_068419|||http://purl.uniprot.org/annotation/VAR_068420|||http://purl.uniprot.org/annotation/VAR_068421|||http://purl.uniprot.org/annotation/VAR_068422|||http://purl.uniprot.org/annotation/VAR_068423|||http://purl.uniprot.org/annotation/VAR_069032|||http://purl.uniprot.org/annotation/VAR_069033|||http://purl.uniprot.org/annotation/VAR_069034|||http://purl.uniprot.org/annotation/VAR_069035|||http://purl.uniprot.org/annotation/VAR_072954|||http://purl.uniprot.org/annotation/VAR_072955|||http://purl.uniprot.org/annotation/VAR_072956|||http://purl.uniprot.org/annotation/VAR_072957|||http://purl.uniprot.org/annotation/VAR_072958|||http://purl.uniprot.org/annotation/VAR_072959|||http://purl.uniprot.org/annotation/VAR_072960|||http://purl.uniprot.org/annotation/VAR_072961|||http://purl.uniprot.org/annotation/VAR_072962|||http://purl.uniprot.org/annotation/VAR_072963|||http://purl.uniprot.org/annotation/VAR_072964|||http://purl.uniprot.org/annotation/VAR_072965|||http://purl.uniprot.org/annotation/VAR_072966|||http://purl.uniprot.org/annotation/VAR_072967|||http://purl.uniprot.org/annotation/VAR_072968|||http://purl.uniprot.org/annotation/VAR_072969|||http://purl.uniprot.org/annotation/VAR_078703|||http://purl.uniprot.org/annotation/VSP_026038|||http://purl.uniprot.org/annotation/VSP_026039|||http://purl.uniprot.org/annotation/VSP_046563|||http://purl.uniprot.org/annotation/VSP_046564|||http://purl.uniprot.org/annotation/VSP_046565
http://togogenome.org/gene/9606:RORA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFP5|||http://purl.uniprot.org/uniprot/A0A0C4DG53|||http://purl.uniprot.org/uniprot/P35398                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AF-2|||Abolishes transcriptional activity. Protects from protein degradation.|||About 40% loss of transcriptional activity.|||About 60% loss of transcriptional activity.|||About 80% loss of transcriptional activity.|||Almost total loss of transcriptional activity.|||Attenuates transcriptional activity.|||Basic and acidic residues|||Complete loss of transcriptional activity; when associated with A-339.|||Complete loss of transcriptional activity; when associated with A-507.|||Decreases interaction with NCOA2. Loss of interaction with FOXP3.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Greatly increased transcriptional activity. Decrease in repression by NR1D1.|||Greatly reduced transcriptional activity. Protects from protein degradation.|||In IDDECA.|||In IDDECA; deleterious effect on embryonic development, when assayed in a heterologous system.|||In IDDECA; loss of function in cerebellar development, when assayed in a heterologous system.|||In IDDECA; unknown pathological significance.|||In a colorectal cancer sample, somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased transcriptional activity. No effect on protein degradation.|||Less effect on transcriptional activity with cholesterol sulfate as substrate as compared to cholesterol as substrate.|||Loss of sumoylation.|||N6-methyllysine|||NR C4-type|||NR LBD|||No effect on cerebellar development, when assayed in a heterologous system.|||No effect on sumoylation.|||Nuclear receptor|||Nuclear receptor ROR-alpha|||Phosphothreonine; by MAPK1|||Polar residues|||Slight loss of transcriptional activity.|||Small reduction in transcriptional activity. No protein degradation.|||Some increase in transcriptional activity.|||Some increase in transcriptional activity. No change in repression by NR1D1.|||Strongly decreases interaction with NCOA2 and MED1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053512|||http://purl.uniprot.org/annotation/VAR_081089|||http://purl.uniprot.org/annotation/VAR_081090|||http://purl.uniprot.org/annotation/VAR_081091|||http://purl.uniprot.org/annotation/VAR_081092|||http://purl.uniprot.org/annotation/VAR_081093|||http://purl.uniprot.org/annotation/VAR_081094|||http://purl.uniprot.org/annotation/VAR_081095|||http://purl.uniprot.org/annotation/VAR_082877|||http://purl.uniprot.org/annotation/VSP_053973|||http://purl.uniprot.org/annotation/VSP_053974|||http://purl.uniprot.org/annotation/VSP_053975
http://togogenome.org/gene/9606:VHLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6RSH7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Beta-domain|||Disordered|||Preferentially binds to a hydroxylated ODD peptide.|||von Hippel-Lindau-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265087
http://togogenome.org/gene/9606:CSN1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47710                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alpha-S1-casein|||Casoxin-D|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004450|||http://purl.uniprot.org/annotation/PRO_0000004451|||http://purl.uniprot.org/annotation/VAR_048614|||http://purl.uniprot.org/annotation/VSP_000795|||http://purl.uniprot.org/annotation/VSP_000796|||http://purl.uniprot.org/annotation/VSP_046130
http://togogenome.org/gene/9606:EIF2AK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQI3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 2-alpha kinase 1|||HRM 1|||HRM 2|||Heme-binding|||In LEMSPAD; unknown pathological significance; mildly reduced phosphorylation of eukaryotic translation initiation factor 2-alpha.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085941|||http://purl.uniprot.org/annotation/VAR_015732|||http://purl.uniprot.org/annotation/VAR_040466|||http://purl.uniprot.org/annotation/VAR_040467|||http://purl.uniprot.org/annotation/VAR_040468|||http://purl.uniprot.org/annotation/VAR_040469|||http://purl.uniprot.org/annotation/VAR_040470|||http://purl.uniprot.org/annotation/VAR_040471|||http://purl.uniprot.org/annotation/VAR_040472|||http://purl.uniprot.org/annotation/VAR_040473|||http://purl.uniprot.org/annotation/VAR_084259|||http://purl.uniprot.org/annotation/VSP_007589
http://togogenome.org/gene/9606:ZNF451                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYS2|||http://purl.uniprot.org/uniprot/Q96JY2|||http://purl.uniprot.org/uniprot/Q9Y4E5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; atypical|||C2H2-type 8|||C2H2-type 9|||Disordered|||E3 SUMO-protein ligase ZNF451|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs interaction with SUMO1. No effect on negative regulation of SMAD4-mediated transcription activation.|||Important for interaction with SMAD4|||Important for interaction with SUMO1 and SUMO2|||Important for ubiquitin binding|||In isoform 2.|||In isoform 3.|||Interaction with SUMO2 1|||Interaction with SUMO2 2|||Mildly reduces E3 SUMO-protein ligase activity.|||Nearly abolishes E3 SUMO-protein ligase activity (in vitro).|||No effect on negative regulation of SMAD4-mediated transcription activation.|||Omega-N-methylarginine|||PLRP|||Phosphoserine|||Polar residues|||Reduces E3 SUMO-protein ligase activity by 96% (in vitro).|||Reduces E3 SUMO-protein ligase activity by 97% (in vitro).|||Sufficient for E3 SUMO-protein ligase activity|||ZNF451 PIN-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047598|||http://purl.uniprot.org/annotation/VSP_008624|||http://purl.uniprot.org/annotation/VSP_035312
http://togogenome.org/gene/9606:TRMT61A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FX7                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylserine|||Phosphoserine|||Removed|||tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233094|||http://purl.uniprot.org/annotation/VAR_026053
http://togogenome.org/gene/9606:GRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28799                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Granulin-1|||Granulin-2|||Granulin-3|||Granulin-4|||Granulin-5|||Granulin-6|||Granulin-7|||In UP-FTD; no significant difference in the total mRNA between cases and controls; although the mutant protein is expressed it is not secreted and appears to be trapped within an intracellular compartment.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Paragranulin|||Progranulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012693|||http://purl.uniprot.org/annotation/PRO_0000012694|||http://purl.uniprot.org/annotation/PRO_0000012695|||http://purl.uniprot.org/annotation/PRO_0000012696|||http://purl.uniprot.org/annotation/PRO_0000012697|||http://purl.uniprot.org/annotation/PRO_0000012698|||http://purl.uniprot.org/annotation/PRO_0000012699|||http://purl.uniprot.org/annotation/PRO_0000012700|||http://purl.uniprot.org/annotation/PRO_0000012701|||http://purl.uniprot.org/annotation/VAR_014830|||http://purl.uniprot.org/annotation/VAR_044451|||http://purl.uniprot.org/annotation/VAR_064625|||http://purl.uniprot.org/annotation/VAR_064626|||http://purl.uniprot.org/annotation/VAR_064627|||http://purl.uniprot.org/annotation/VAR_064628|||http://purl.uniprot.org/annotation/VAR_064629|||http://purl.uniprot.org/annotation/VAR_064630|||http://purl.uniprot.org/annotation/VAR_064631|||http://purl.uniprot.org/annotation/VAR_064632|||http://purl.uniprot.org/annotation/VAR_064633|||http://purl.uniprot.org/annotation/VAR_064634|||http://purl.uniprot.org/annotation/VAR_064635|||http://purl.uniprot.org/annotation/VAR_064636|||http://purl.uniprot.org/annotation/VSP_001837|||http://purl.uniprot.org/annotation/VSP_053472|||http://purl.uniprot.org/annotation/VSP_053473
http://togogenome.org/gene/9606:CYB5D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9G0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytochrome b5 domain-containing protein 1|||Cytochrome b5 heme-binding|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312315|||http://purl.uniprot.org/annotation/VAR_037486|||http://purl.uniprot.org/annotation/VSP_029823|||http://purl.uniprot.org/annotation/VSP_029824
http://togogenome.org/gene/9606:NXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DKJ4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In RRS2.|||In RRS2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Nucleoredoxin|||Removed|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332933|||http://purl.uniprot.org/annotation/VAR_083246|||http://purl.uniprot.org/annotation/VAR_083247|||http://purl.uniprot.org/annotation/VSP_033392|||http://purl.uniprot.org/annotation/VSP_033393|||http://purl.uniprot.org/annotation/VSP_033394|||http://purl.uniprot.org/annotation/VSP_033395|||http://purl.uniprot.org/annotation/VSP_042792|||http://purl.uniprot.org/annotation/VSP_042793
http://togogenome.org/gene/9606:CIB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJX0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Calcium and integrin-binding family member 4|||EF-hand 1|||EF-hand 2|||EF-hand 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289290|||http://purl.uniprot.org/annotation/VAR_048637
http://togogenome.org/gene/9606:OR2C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95371                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150465|||http://purl.uniprot.org/annotation/VAR_047490|||http://purl.uniprot.org/annotation/VAR_047491|||http://purl.uniprot.org/annotation/VAR_047492
http://togogenome.org/gene/9606:ZNF525                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KR62|||http://purl.uniprot.org/uniprot/Q8N782                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 525                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047638
http://togogenome.org/gene/9606:PEX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG33|||http://purl.uniprot.org/uniprot/B4DER6|||http://purl.uniprot.org/uniprot/O43933                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||Basic and acidic residues|||Disordered|||In A1 mutant; abolished ATP-binding; decreased interaction with PEX6; decreased localization to peroxisomal membranes.|||In A2 mutant; abolished ATP-binding; decreased interaction with PEX6; decreased localization to peroxisomal membranes.|||In B1 mutant; abolished ATP hydrolysis; decreased interaction with PEX6; decreased localization to peroxisomal membranes.|||In B2 mutant; abolished ATP hydrolysis; does not affect interaction with PEX6; does not affect localization to peroxisomal membranes.|||In HMLR1; results in mild functional decrease in peroxisome biogenesis.|||In PBD-CG1.|||In PBD1A and PBD1B.|||In PBD1A and PBD1B; decreased binding to PEX6; impaired protein import into peroxisomes.|||In PBD1A, PBD1B and PBD-CG1.|||In PBD1A.|||In PBD1A; impaired protein import into peroxisomes.|||In PBD1B and HMLR1.|||In PBD1B.|||In isoform 2.|||Peroxisomal ATPase PEX1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084604|||http://purl.uniprot.org/annotation/VAR_008876|||http://purl.uniprot.org/annotation/VAR_008877|||http://purl.uniprot.org/annotation/VAR_014358|||http://purl.uniprot.org/annotation/VAR_034376|||http://purl.uniprot.org/annotation/VAR_048113|||http://purl.uniprot.org/annotation/VAR_058376|||http://purl.uniprot.org/annotation/VAR_058377|||http://purl.uniprot.org/annotation/VAR_058378|||http://purl.uniprot.org/annotation/VAR_058379|||http://purl.uniprot.org/annotation/VAR_058380|||http://purl.uniprot.org/annotation/VAR_074108|||http://purl.uniprot.org/annotation/VAR_074109|||http://purl.uniprot.org/annotation/VAR_075871|||http://purl.uniprot.org/annotation/VAR_077503|||http://purl.uniprot.org/annotation/VAR_077504|||http://purl.uniprot.org/annotation/VAR_087133|||http://purl.uniprot.org/annotation/VAR_087134|||http://purl.uniprot.org/annotation/VAR_087135|||http://purl.uniprot.org/annotation/VAR_087136|||http://purl.uniprot.org/annotation/VSP_057136
http://togogenome.org/gene/9606:SYNE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG40|||http://purl.uniprot.org/uniprot/B4E3R1|||http://purl.uniprot.org/uniprot/B7Z9Y6|||http://purl.uniprot.org/uniprot/F8WAI0|||http://purl.uniprot.org/uniprot/Q8NF91                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the nuclear envelope targeting, induces a cytoplasmic localization.|||Actin-binding|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Cytoplasmic|||Disordered|||Found in a patient with mild intellectual disability, spastic paraplegia, axon neuropathy and leukoencephalopathy; unknown pathological significance.|||Helical; Anchor for type IV membrane protein|||In AMC3.|||In EDMD4.|||In EDMD4; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 9.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||In isoform GSRP-56.|||Interchain (C-563 in SUN2); alternate|||Interchain (with C-657 in SUN1); alternate|||KASH|||Nesprin-1|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 23|||Spectrin 24|||Spectrin 25|||Spectrin 26|||Spectrin 27|||Spectrin 28|||Spectrin 29|||Spectrin 3|||Spectrin 30|||Spectrin 31|||Spectrin 32|||Spectrin 33|||Spectrin 34|||Spectrin 35|||Spectrin 36|||Spectrin 37|||Spectrin 38|||Spectrin 39|||Spectrin 4|||Spectrin 40|||Spectrin 41|||Spectrin 42|||Spectrin 43|||Spectrin 44|||Spectrin 45|||Spectrin 46|||Spectrin 47|||Spectrin 48|||Spectrin 49|||Spectrin 5|||Spectrin 50|||Spectrin 51|||Spectrin 52|||Spectrin 53|||Spectrin 54|||Spectrin 55|||Spectrin 56|||Spectrin 57|||Spectrin 58|||Spectrin 59|||Spectrin 6|||Spectrin 60|||Spectrin 61|||Spectrin 62|||Spectrin 63|||Spectrin 64|||Spectrin 65|||Spectrin 66|||Spectrin 67|||Spectrin 68|||Spectrin 69|||Spectrin 7|||Spectrin 70|||Spectrin 71|||Spectrin 72|||Spectrin 73|||Spectrin 74|||Spectrin 8|||Spectrin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163591|||http://purl.uniprot.org/annotation/VAR_015548|||http://purl.uniprot.org/annotation/VAR_036250|||http://purl.uniprot.org/annotation/VAR_036251|||http://purl.uniprot.org/annotation/VAR_036252|||http://purl.uniprot.org/annotation/VAR_036253|||http://purl.uniprot.org/annotation/VAR_036254|||http://purl.uniprot.org/annotation/VAR_056211|||http://purl.uniprot.org/annotation/VAR_056212|||http://purl.uniprot.org/annotation/VAR_056213|||http://purl.uniprot.org/annotation/VAR_056214|||http://purl.uniprot.org/annotation/VAR_056215|||http://purl.uniprot.org/annotation/VAR_056216|||http://purl.uniprot.org/annotation/VAR_056217|||http://purl.uniprot.org/annotation/VAR_056218|||http://purl.uniprot.org/annotation/VAR_056219|||http://purl.uniprot.org/annotation/VAR_056220|||http://purl.uniprot.org/annotation/VAR_056221|||http://purl.uniprot.org/annotation/VAR_056222|||http://purl.uniprot.org/annotation/VAR_056223|||http://purl.uniprot.org/annotation/VAR_056224|||http://purl.uniprot.org/annotation/VAR_056225|||http://purl.uniprot.org/annotation/VAR_056226|||http://purl.uniprot.org/annotation/VAR_056227|||http://purl.uniprot.org/annotation/VAR_056228|||http://purl.uniprot.org/annotation/VAR_056229|||http://purl.uniprot.org/annotation/VAR_056230|||http://purl.uniprot.org/annotation/VAR_056231|||http://purl.uniprot.org/annotation/VAR_056232|||http://purl.uniprot.org/annotation/VAR_056233|||http://purl.uniprot.org/annotation/VAR_056234|||http://purl.uniprot.org/annotation/VAR_056235|||http://purl.uniprot.org/annotation/VAR_056236|||http://purl.uniprot.org/annotation/VAR_062974|||http://purl.uniprot.org/annotation/VAR_062975|||http://purl.uniprot.org/annotation/VAR_062976|||http://purl.uniprot.org/annotation/VAR_070561|||http://purl.uniprot.org/annotation/VAR_070562|||http://purl.uniprot.org/annotation/VAR_074190|||http://purl.uniprot.org/annotation/VAR_082986|||http://purl.uniprot.org/annotation/VAR_082987|||http://purl.uniprot.org/annotation/VSP_007130|||http://purl.uniprot.org/annotation/VSP_007131|||http://purl.uniprot.org/annotation/VSP_007132|||http://purl.uniprot.org/annotation/VSP_007133|||http://purl.uniprot.org/annotation/VSP_007134|||http://purl.uniprot.org/annotation/VSP_007135|||http://purl.uniprot.org/annotation/VSP_007136|||http://purl.uniprot.org/annotation/VSP_007137|||http://purl.uniprot.org/annotation/VSP_007138|||http://purl.uniprot.org/annotation/VSP_007139|||http://purl.uniprot.org/annotation/VSP_007140|||http://purl.uniprot.org/annotation/VSP_007141|||http://purl.uniprot.org/annotation/VSP_007142|||http://purl.uniprot.org/annotation/VSP_007143|||http://purl.uniprot.org/annotation/VSP_007144|||http://purl.uniprot.org/annotation/VSP_057476|||http://purl.uniprot.org/annotation/VSP_057477|||http://purl.uniprot.org/annotation/VSP_057478|||http://purl.uniprot.org/annotation/VSP_057479|||http://purl.uniprot.org/annotation/VSP_057480|||http://purl.uniprot.org/annotation/VSP_057481|||http://purl.uniprot.org/annotation/VSP_057482
http://togogenome.org/gene/9606:SDF2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCN8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  MIR 1|||MIR 2|||MIR 3|||Phosphoserine|||Prevents secretion from ER|||Stromal cell-derived factor 2-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031957
http://togogenome.org/gene/9606:ASH2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPT1|||http://purl.uniprot.org/uniprot/F5H8F7|||http://purl.uniprot.org/uniprot/Q9UBL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes methylation.|||Asymmetric dimethylarginine; by PRMT1 and PRMT5|||B30.2/SPRY|||Basic and acidic residues|||C4-type|||DNA-binding|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with RBBP5|||N-acetylmethionine|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Set1/Ash2 histone methyltransferase complex subunit ASH2|||Slightly decreased methylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064697|||http://purl.uniprot.org/annotation/VAR_050679|||http://purl.uniprot.org/annotation/VSP_007577|||http://purl.uniprot.org/annotation/VSP_007578
http://togogenome.org/gene/9606:FAM9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Protein FAM9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119033|||http://purl.uniprot.org/annotation/VSP_055087|||http://purl.uniprot.org/annotation/VSP_055088
http://togogenome.org/gene/9606:THEM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1C6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes cleavage of mitochondrial transit peptide.|||Abolishes import into the mitochondria.|||Acyl-coenzyme A thioesterase THEM4|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Nearly abolishes enzyme activity. Strongly reduced affinity for myristoyl-CoA.|||No effect on enzyme activity.|||Phosphoserine|||Proton donor/acceptor|||Reduces enzyme activity.|||Slightly reduced enzyme activity.|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314179|||http://purl.uniprot.org/annotation/VAR_037865|||http://purl.uniprot.org/annotation/VAR_037866
http://togogenome.org/gene/9606:LRRC23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8K2|||http://purl.uniprot.org/uniprot/Q53EV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||Leucine-rich repeat-containing protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264236|||http://purl.uniprot.org/annotation/VAR_051106|||http://purl.uniprot.org/annotation/VAR_051107|||http://purl.uniprot.org/annotation/VAR_051108|||http://purl.uniprot.org/annotation/VSP_021889
http://togogenome.org/gene/9606:C17orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2W7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NTR|||Pro residues|||UPF0450 protein C17orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279445|||http://purl.uniprot.org/annotation/VAR_030902|||http://purl.uniprot.org/annotation/VSP_036597
http://togogenome.org/gene/9606:MOGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDR6|||http://purl.uniprot.org/uniprot/Q13724|||http://purl.uniprot.org/uniprot/Q58F09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum targeting|||Glycosyl hydrolase family 63 C-terminal|||Glycosyl hydrolase family 63 N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In CDGIIb; loss of activity.|||In isoform 2.|||Lumenal|||Mannosyl-oligosaccharide glucosidase|||N-linked (GlcNAc...) asparagine|||Required for endoplasmic reticulum targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057710|||http://purl.uniprot.org/annotation/VAR_018966|||http://purl.uniprot.org/annotation/VAR_018967|||http://purl.uniprot.org/annotation/VAR_019361|||http://purl.uniprot.org/annotation/VAR_019362|||http://purl.uniprot.org/annotation/VAR_049233|||http://purl.uniprot.org/annotation/VAR_049234|||http://purl.uniprot.org/annotation/VAR_049235|||http://purl.uniprot.org/annotation/VAR_049236|||http://purl.uniprot.org/annotation/VSP_046921
http://togogenome.org/gene/9606:GATA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23771                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Flexible linker|||GATA-type 1|||GATA-type 2|||In HDR.|||In HDR; loss of enhancer activity on PTH gene promoter and on GATA responsive element.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with TBX21|||Phosphoserine|||Polar residues|||Trans-acting T-cell-specific transcription factor GATA-3|||YxKxHxxxRP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083408|||http://purl.uniprot.org/annotation/VAR_017818|||http://purl.uniprot.org/annotation/VAR_019202|||http://purl.uniprot.org/annotation/VAR_033025|||http://purl.uniprot.org/annotation/VAR_075427|||http://purl.uniprot.org/annotation/VSP_001598
http://togogenome.org/gene/9606:SMURF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DE7|||http://purl.uniprot.org/uniprot/Q9HAU4                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SMAD2 and SMAD7.|||Abolishes interaction with SMAD7.|||Activates autocatalytic activity.|||C2|||E3 ubiquitin-protein ligase SMURF2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||Increases auto-ubiquitination.|||Increases auto-ubiquitination; when associated with A-56.|||Increases auto-ubiquitination; when associated with A-57.|||Loss of activity. Loss of ability to ubiquitinate SMAD1 and SMAD2 and no down-regulation of SMAD1 and SMAD2 protein levels.|||Loss of catalytic activity.|||Loss of catalytic activity. Increases SMAD7-bound TGF-beta receptors in membrane rafts. Decreases interaction with TTC3. Decreased VP40 virus-like particle budding.|||Partial loss of catalytic activity.|||WW 1|||WW 2|||WW 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120329
http://togogenome.org/gene/9606:PRKRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V2I8|||http://purl.uniprot.org/uniprot/B4DJC7|||http://purl.uniprot.org/uniprot/O75569                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abrogates apoptosis induction under conditions of stress and binding to EIF2AK2. Prevents activation of EIF2AK2 in stressed cells; when associated with A-287.|||Abrogates apoptosis induction under conditions of stress.|||Abrogates apoptosis induction under conditions of stress. Prevents activation of EIF2AK2 in stressed cells; when associated with A-246.|||Abrogates interaction with DICER1 but does not affect interaction with AGO2.|||DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||Disordered|||Does not induce apoptosis.|||In DYT16.|||In isoform 2.|||In isoform 3.|||Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-246.|||Induces activation of EIF2AK2 and apoptosis in unstressed cells; when associated with D-287.|||Interferon-inducible double-stranded RNA-dependent protein kinase activator A|||No effect on apoptosis induction under conditions of stress.|||Phosphoserine|||Sufficient for self-association and interaction with TARBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223609|||http://purl.uniprot.org/annotation/VAR_046213|||http://purl.uniprot.org/annotation/VSP_017282|||http://purl.uniprot.org/annotation/VSP_017283
http://togogenome.org/gene/9606:TMLHE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVH6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In AUTSX6; loss of function.|||In AUTSX6; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Mitochondrion|||N6-acetyllysine|||No catalytic activity.|||Trimethyllysine dioxygenase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002795|||http://purl.uniprot.org/annotation/VAR_076251|||http://purl.uniprot.org/annotation/VAR_076252|||http://purl.uniprot.org/annotation/VSP_021579|||http://purl.uniprot.org/annotation/VSP_042275|||http://purl.uniprot.org/annotation/VSP_042276|||http://purl.uniprot.org/annotation/VSP_042277|||http://purl.uniprot.org/annotation/VSP_042278|||http://purl.uniprot.org/annotation/VSP_042279|||http://purl.uniprot.org/annotation/VSP_042280|||http://purl.uniprot.org/annotation/VSP_042281
http://togogenome.org/gene/9606:CHGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05060                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||CCB peptide|||Disordered|||GAWK peptide|||O-glycosylated at one site|||O-linked (Xyl...) (chondroitin sulfate) serine|||PE-11|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphotyrosine|||Secretogranin-1|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005438|||http://purl.uniprot.org/annotation/PRO_0000005439|||http://purl.uniprot.org/annotation/PRO_0000005440|||http://purl.uniprot.org/annotation/PRO_0000432730|||http://purl.uniprot.org/annotation/VAR_020287|||http://purl.uniprot.org/annotation/VAR_022012|||http://purl.uniprot.org/annotation/VAR_024414|||http://purl.uniprot.org/annotation/VAR_024415|||http://purl.uniprot.org/annotation/VAR_024416|||http://purl.uniprot.org/annotation/VAR_028235|||http://purl.uniprot.org/annotation/VAR_028236|||http://purl.uniprot.org/annotation/VAR_028237|||http://purl.uniprot.org/annotation/VAR_028238|||http://purl.uniprot.org/annotation/VAR_043578
http://togogenome.org/gene/9606:CAAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8G2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Caspase activity and apoptosis inhibitor 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089717|||http://purl.uniprot.org/annotation/VAR_056818|||http://purl.uniprot.org/annotation/VSP_044253
http://togogenome.org/gene/9606:MAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BP11|||http://purl.uniprot.org/uniprot/O75444                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BZIP|||Basic motif|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In AYGRP.|||In CTRCT21.|||In CTRCT21; unknown pathological significance.|||In isoform 1.|||Leucine-zipper|||Polar residues|||Represses ARE-mediated transcription|||Transcription factor Maf|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076491|||http://purl.uniprot.org/annotation/VAR_029369|||http://purl.uniprot.org/annotation/VAR_029370|||http://purl.uniprot.org/annotation/VAR_073891|||http://purl.uniprot.org/annotation/VAR_073892|||http://purl.uniprot.org/annotation/VAR_073893|||http://purl.uniprot.org/annotation/VAR_073894|||http://purl.uniprot.org/annotation/VAR_073895|||http://purl.uniprot.org/annotation/VAR_073896|||http://purl.uniprot.org/annotation/VAR_073897|||http://purl.uniprot.org/annotation/VAR_073898|||http://purl.uniprot.org/annotation/VAR_084822|||http://purl.uniprot.org/annotation/VAR_084823|||http://purl.uniprot.org/annotation/VSP_000583
http://togogenome.org/gene/9606:RGS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15492                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  30% decrease in GAP activity.|||No effect on GAP activity.|||Phosphotyrosine|||Phosphotyrosine; by EGFR|||RGS|||Regulator of G-protein signaling 16|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204221|||http://purl.uniprot.org/annotation/VAR_046528
http://togogenome.org/gene/9606:MRPL40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ50                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein mL40|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030558|||http://purl.uniprot.org/annotation/VAR_016088|||http://purl.uniprot.org/annotation/VAR_061809
http://togogenome.org/gene/9606:ARHGAP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53QZ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||PH|||Phosphoserine|||Rho GTPase-activating protein 15|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317574
http://togogenome.org/gene/9606:HDX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z353                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly divergent homeobox|||Homeobox 1|||Homeobox 2|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299487|||http://purl.uniprot.org/annotation/VAR_034827|||http://purl.uniprot.org/annotation/VAR_034828|||http://purl.uniprot.org/annotation/VSP_027708
http://togogenome.org/gene/9606:SCAF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99590                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein SCAF11|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076314|||http://purl.uniprot.org/annotation/VAR_059722|||http://purl.uniprot.org/annotation/VAR_059723|||http://purl.uniprot.org/annotation/VSP_037665
http://togogenome.org/gene/9606:GNL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVP2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic|||Acidic residues|||Basic|||Basic and acidic residues|||Basic residues|||CP-type G|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Guanine nucleotide-binding protein-like 3|||In isoform 2.|||Intermediate|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122444|||http://purl.uniprot.org/annotation/VAR_022160|||http://purl.uniprot.org/annotation/VAR_022161|||http://purl.uniprot.org/annotation/VSP_013411
http://togogenome.org/gene/9606:SRSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R6F3|||http://purl.uniprot.org/uniprot/P84103                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2 X approximate repeats, basic|||Abolishes interaction with NXF1.|||B-1|||B-2|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||RRM|||Serine/arginine-rich splicing factor 3|||Sufficient for interaction with NXF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081923|||http://purl.uniprot.org/annotation/VSP_056243
http://togogenome.org/gene/9606:C1QB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAB9|||http://purl.uniprot.org/uniprot/P02746                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||C1q|||Collagen-like 1|||Collagen-like 2|||Complement C1q subcomponent subunit B|||Disordered|||In C1QD2.|||In a breast cancer sample; somatic mutation.|||Interchain (with C-26 in chain A)|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003521|||http://purl.uniprot.org/annotation/PRO_5014214287|||http://purl.uniprot.org/annotation/VAR_008541|||http://purl.uniprot.org/annotation/VAR_035551
http://togogenome.org/gene/9606:HEXIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94992                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes interaction with 7SK snRNA.|||Abolishes interaction with P-TEFb. Same effect; when associated with D-203.|||Abolishes interaction with P-TEFb; when associated with D-205.|||Acidic residues|||Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localization|||Basic and acidic residues|||Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1|||Basic residues|||Disordered|||Interaction with P-TEFb|||Loss of function.|||Loss of oligomerization; when associated with A-287; A-294 and A-332.|||Loss of oligomerization; when associated with A-287; A-294 and A-339.|||Loss of oligomerization; when associated with A-287; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-287.|||Loss of oligomerization; when associated with A-294; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-294.|||Mediates interaction with CCNT1|||Partial loss of function.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein HEXIM1|||Required for inhibition of ESR1-dependent transcription                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305263
http://togogenome.org/gene/9606:ABCB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3G0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family B member 5|||Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 1, isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253575|||http://purl.uniprot.org/annotation/VAR_028387|||http://purl.uniprot.org/annotation/VAR_028388|||http://purl.uniprot.org/annotation/VAR_028389|||http://purl.uniprot.org/annotation/VAR_028390|||http://purl.uniprot.org/annotation/VAR_033456|||http://purl.uniprot.org/annotation/VAR_035731|||http://purl.uniprot.org/annotation/VAR_062662|||http://purl.uniprot.org/annotation/VSP_056752|||http://purl.uniprot.org/annotation/VSP_056753|||http://purl.uniprot.org/annotation/VSP_056754|||http://purl.uniprot.org/annotation/VSP_056755|||http://purl.uniprot.org/annotation/VSP_056756
http://togogenome.org/gene/9606:DERA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PPM8|||http://purl.uniprot.org/uniprot/Q9Y315                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes deoxyribose-phosphate aldolase activity.|||Deoxyribose-phosphate aldolase|||Proton donor/acceptor|||Schiff-base intermediate with acetaldehyde                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057310
http://togogenome.org/gene/9606:WNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDX3|||http://purl.uniprot.org/uniprot/P09544                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt|||Protein Wnt-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041410|||http://purl.uniprot.org/annotation/PRO_5017212149|||http://purl.uniprot.org/annotation/VAR_013865|||http://purl.uniprot.org/annotation/VAR_013866|||http://purl.uniprot.org/annotation/VAR_052954
http://togogenome.org/gene/9606:E2F6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3K8|||http://purl.uniprot.org/uniprot/O75461|||http://purl.uniprot.org/uniprot/Q53YM3|||http://purl.uniprot.org/uniprot/Q6Q9Z5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DEF box|||Dimerization|||Disordered|||E2F transcription factor CC-MB|||E2F/DP family winged-helix DNA-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Polar residues|||Reduction in repressor activity, little effect on S-phase entry.|||Transcription factor E2F6|||Transcription repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219472|||http://purl.uniprot.org/annotation/VSP_008771|||http://purl.uniprot.org/annotation/VSP_054754
http://togogenome.org/gene/9606:SLC6A19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q695T7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect cell membrane localization; does not affect amino acid transport activity.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In HND; abolishes amino acid transport activity.|||In HND; does not affect amino acid transport activity when expressed alone; decreases amino acid transport activity in presence of ACE2 or CLTRN; decreased surface cell expression when expressed with CLTRN or ACE2.|||In HND; does not affect interaction with ACE2; coexpression with ACE2 increased the transport rate whereas coexpression with CLTRN has the opposite effect.|||In HND; increases cell membrane localization in presence of ACE2 or CLTRN; does not affect interaction with ACE2; amino acid transport activity is not activated in presence of ACE2 or CLTRN.|||In HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; increases surface cell expression when expressed alone or coexpressed with CLTRN or ACE2.|||In HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed alone or coexpressed with CLTRN or ACE2.|||In HND; no amino acid transport activity when expressed alone or coexpressed with CLTRN or ACE2; loss of surface expression when expressed coexpressed with CLTRN or ACE2.|||In HND; population allele frequency among Europeans is 0.007; reduced transport activity by 50% but does not completely inactivates the transporter; coexpression with ACE2 increased the transport rate whereas coexpression with CLTRN has the opposite effect; does not affect interaction with ACE2; decreased cell membrane localization in presence of CLTRN.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent neutral amino acid transporter B(0)AT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214809|||http://purl.uniprot.org/annotation/VAR_023314|||http://purl.uniprot.org/annotation/VAR_023315|||http://purl.uniprot.org/annotation/VAR_023316|||http://purl.uniprot.org/annotation/VAR_023317|||http://purl.uniprot.org/annotation/VAR_023318|||http://purl.uniprot.org/annotation/VAR_023319|||http://purl.uniprot.org/annotation/VAR_081070|||http://purl.uniprot.org/annotation/VAR_081071|||http://purl.uniprot.org/annotation/VAR_081072|||http://purl.uniprot.org/annotation/VAR_081073|||http://purl.uniprot.org/annotation/VAR_081074|||http://purl.uniprot.org/annotation/VAR_081075|||http://purl.uniprot.org/annotation/VAR_081076|||http://purl.uniprot.org/annotation/VAR_081077|||http://purl.uniprot.org/annotation/VAR_081078|||http://purl.uniprot.org/annotation/VAR_081079
http://togogenome.org/gene/9606:FANCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW38                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes UBE2T charging.|||Abolishes interaction with UBE2T and ubiquitin ligase activity.|||Abolishes ubiquitin ligase activity.|||Does not affect interaction with FANCI and FANCD2; when associated with A-149.|||E3 ubiquitin-protein ligase FANCL|||Impairs interaction with FANCI and FANCD2.|||Impairs interaction with FANCI and FANCD2; when associated with A-248, A-252 and A-254.|||Impairs interaction with FANCI and FANCD2; when associated with A-248, A-252 and A-265.|||Impairs interaction with FANCI and FANCD2; when associated with A-248, A-254 and A-265.|||Impairs interaction with FANCI and FANCD2; when associated with A-252, A-254 and A-265.|||In isoform 2.|||Loss of interaction with UBE2T.|||N-acetylalanine|||No effect on interaction with FANCI and FANCD2.|||No effect on interaction with FANCI and FANCD2; when associated with A-166.|||RING-type; degenerate|||Removed|||UBC-RWD region (URD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055908|||http://purl.uniprot.org/annotation/VAR_052082|||http://purl.uniprot.org/annotation/VSP_041727
http://togogenome.org/gene/9606:JRKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4A0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  DDE-1|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Jerky protein homolog-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126130
http://togogenome.org/gene/9606:ERVH48-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M5A8F1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Suppressyn                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000430056
http://togogenome.org/gene/9606:LIMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48059                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters interaction with ILK.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM and senescent cell antigen-like-containing domain protein 1|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||LIM zinc-binding 5|||Loss of interaction with ILK and loss of localization to focal adhesion.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075888|||http://purl.uniprot.org/annotation/VSP_042672|||http://purl.uniprot.org/annotation/VSP_043210|||http://purl.uniprot.org/annotation/VSP_043211|||http://purl.uniprot.org/annotation/VSP_043212
http://togogenome.org/gene/9606:TNFRSF21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75509                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Repeat|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes one glycosylation site and reduces total N-glycosylation. Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-141; Q-252; Q-257 and Q-289.|||Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-252; Q-278 and Q-289.|||Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278 and Q-289.|||Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-278.|||Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-141; Q-252; Q-278 and Q-289.|||Abolishes one glycosylation site and reduces total N-glycosylation; when associated with Q-82; Q-252; Q-278 and Q-289.|||Abolishes palmitoylation.|||Cytoplasmic|||Death|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034602
http://togogenome.org/gene/9606:RPL26L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNX3                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Crosslink|||Region                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Ribosomal protein uL24-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130791
http://togogenome.org/gene/9606:CCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22362                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005141
http://togogenome.org/gene/9606:CYP2C9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11712|||http://purl.uniprot.org/uniprot/S5RV20                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2C9|||In allele CYP2C9*10.|||In allele CYP2C9*11.|||In allele CYP2C9*12.|||In allele CYP2C9*14.|||In allele CYP2C9*2.|||In allele CYP2C9*35.|||In allele CYP2C9*3; responsible for the tolbutamide poor metabolizer phenotype.|||In allele CYP2C9*4.|||In allele CYP2C9*57.|||In allele CYP2C9*59; produces warfarin hypersensitivity; increases affinity but highly decreases enzymatic activity for tolbutamide; no effect on affinity but decreases enzymatic activity for diclofenac; decreases affinity and highly decreases enzymatic activity for losartan.|||In allele CYP2C9*5; increases the K(m) value for substrates tested.|||In allele CYP2C9*7.|||In allele CYP2C9*8.|||In allele CYP2C9*9.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051700|||http://purl.uniprot.org/annotation/PRO_5014313513|||http://purl.uniprot.org/annotation/VAR_008343|||http://purl.uniprot.org/annotation/VAR_008344|||http://purl.uniprot.org/annotation/VAR_008345|||http://purl.uniprot.org/annotation/VAR_008346|||http://purl.uniprot.org/annotation/VAR_013515|||http://purl.uniprot.org/annotation/VAR_013516|||http://purl.uniprot.org/annotation/VAR_018862|||http://purl.uniprot.org/annotation/VAR_018863|||http://purl.uniprot.org/annotation/VAR_018864|||http://purl.uniprot.org/annotation/VAR_018865|||http://purl.uniprot.org/annotation/VAR_018866|||http://purl.uniprot.org/annotation/VAR_018867|||http://purl.uniprot.org/annotation/VAR_024717|||http://purl.uniprot.org/annotation/VAR_075286|||http://purl.uniprot.org/annotation/VAR_075287|||http://purl.uniprot.org/annotation/VAR_075288|||http://purl.uniprot.org/annotation/VAR_075289|||http://purl.uniprot.org/annotation/VSP_055573|||http://purl.uniprot.org/annotation/VSP_055574
http://togogenome.org/gene/9606:MAPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28482|||http://purl.uniprot.org/uniprot/Q1HBJ4|||http://purl.uniprot.org/uniprot/Q499G7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytoplasmic retention motif|||Does not inhibit interaction with MAP2K1.|||In NS13.|||In NS13; results in increased MAPK signaling; increased translocation to the nucleus; reduced interaction with DUSP6; no effect on interaction with MAP2K1.|||In NS13; results in increased MAPK signaling; reduced interaction with DUSP6; no effect on interaction with MAP2K1.|||In isoform 2.|||Inhibits homodimerization and interaction with TPR.|||Inhibits interaction with MAP2K1 but not with TPR; when associated with N-318.|||Inhibits interaction with MAP2K1 but not with TPR; when associated with N-321.|||Inhibits interaction with TPR.|||Inhibits interaction with TPR; when associated with A-185.|||Inhibits interaction with TPR; when associated with A-187.|||Loss of dephosphorylation by PTPRJ.|||Mitogen-activated protein kinase 1|||N-acetylalanine|||Nuclear translocation motif|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine; by MAP2K1 and MAP2K2|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by MAP2K1 and MAP2K2|||Protein kinase|||Proton acceptor|||Removed|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186247|||http://purl.uniprot.org/annotation/VAR_085093|||http://purl.uniprot.org/annotation/VAR_085094|||http://purl.uniprot.org/annotation/VAR_085095|||http://purl.uniprot.org/annotation/VAR_085096|||http://purl.uniprot.org/annotation/VAR_085097|||http://purl.uniprot.org/annotation/VAR_085098|||http://purl.uniprot.org/annotation/VAR_085099|||http://purl.uniprot.org/annotation/VSP_047815
http://togogenome.org/gene/9606:GNRHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30968                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gonadotropin-releasing hormone receptor|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In HH7.|||In HH7; altered hormone binding.|||In HH7; complete loss of function.|||In HH7; complete loss of ligand binding and receptor activation; specific receptor binding of radioisotope-labeled GnRH ligand is undetectable in transfected cells.|||In HH7; complete loss of the receptor-mediated signaling response.|||In HH7; completely eliminates detectable GnRH-binding activity and prevents GnRH-induced stimulation of inositol phosphate accumulation in vitro.|||In HH7; is able to bind GnRH but with a reduced affinity in vitro.|||In HH7; minimal effects upon receptor affinity but receptor expression decreased.|||In HH7; some patients also carry mutations in FGFR1; decreases but does not eliminate GnRH binding.|||In HH7; the patient also carries a mutation in FGFR1.|||In HH7; unknown pathological significance.|||In HH7; unknown pathological significance; some patients also carry mutations in FGFR1; minimal effects upon receptor affinity but expression decreased; altered activation of phospholipase C.|||In HH7; virtual abolition of GnRH agonist binding and agonist-stimulated phosphoinositide turnover; impairs GnRHR-effector coupling.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069487|||http://purl.uniprot.org/annotation/VAR_019311|||http://purl.uniprot.org/annotation/VAR_019312|||http://purl.uniprot.org/annotation/VAR_019313|||http://purl.uniprot.org/annotation/VAR_019314|||http://purl.uniprot.org/annotation/VAR_019315|||http://purl.uniprot.org/annotation/VAR_019316|||http://purl.uniprot.org/annotation/VAR_019317|||http://purl.uniprot.org/annotation/VAR_019318|||http://purl.uniprot.org/annotation/VAR_019319|||http://purl.uniprot.org/annotation/VAR_019320|||http://purl.uniprot.org/annotation/VAR_069960|||http://purl.uniprot.org/annotation/VAR_072970|||http://purl.uniprot.org/annotation/VAR_072971|||http://purl.uniprot.org/annotation/VAR_072972|||http://purl.uniprot.org/annotation/VAR_072973|||http://purl.uniprot.org/annotation/VAR_072974|||http://purl.uniprot.org/annotation/VSP_001914
http://togogenome.org/gene/9606:CNN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7E1|||http://purl.uniprot.org/uniprot/P51911|||http://purl.uniprot.org/uniprot/Q53FP8|||http://purl.uniprot.org/uniprot/V9HWA5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Calponin-1|||Calponin-homology (CH)|||Calponin-like 1|||Calponin-like 2|||Calponin-like 3|||In isoform 2.|||Phosphoserine; by ROCK2|||Phosphothreonine; by ROCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204767|||http://purl.uniprot.org/annotation/VSP_056948
http://togogenome.org/gene/9606:S100A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99584                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||Phosphoserine|||Protein S100-A13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144019
http://togogenome.org/gene/9606:AMPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23109                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP deaminase 1|||Activity comparable to wild-type.|||In MMDD; loss of AMP deaminase activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194403|||http://purl.uniprot.org/annotation/VAR_013270|||http://purl.uniprot.org/annotation/VAR_013271|||http://purl.uniprot.org/annotation/VAR_013272|||http://purl.uniprot.org/annotation/VAR_035801|||http://purl.uniprot.org/annotation/VAR_048860|||http://purl.uniprot.org/annotation/VSP_042638
http://togogenome.org/gene/9606:SPANXB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS25                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nuclear localization signal|||Polar residues|||Sperm protein associated with the nucleus on the X chromosome B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189550|||http://purl.uniprot.org/annotation/VAR_021163
http://togogenome.org/gene/9606:SLC38A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AI6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Putative sodium-coupled neutral amino acid transporter 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326059|||http://purl.uniprot.org/annotation/VAR_039981|||http://purl.uniprot.org/annotation/VSP_032529
http://togogenome.org/gene/9606:TNFAIP8L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GJ75                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Binding to phosphoinositides|||Disordered|||Tumor necrosis factor alpha-induced protein 8-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331424|||http://purl.uniprot.org/annotation/VAR_042860
http://togogenome.org/gene/9606:MYO5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7A5|||http://purl.uniprot.org/uniprot/Q9ULV0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RAB11A; has no effect on RAB8A interaction.|||Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with C-1307.|||Abolishes interaction with RAB8A and has no effect on RAB11A interaction; when associated with L-1300.|||Actin-binding|||Basic and acidic residues|||Dilute|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||In DIAR2 and PFIC10.|||In DIAR2.|||In DIAR2; found in a compound heterozygote also carrying F-550; enterocytes carrying S-538 and F-550 display disruption of cell polarity, mislocalized apical and basolateral transporter proteins and altered distribution of endosomal/lysosomal constituents including Rab GTPases.|||In DIAR2; found in a compound heterozygote also carrying S-538; enterocytes carrying S-538 and F-550 display disruption of cell polarity, mislocalized apical and basolateral transporter proteins and altered distribution of endosomal/lysosomal constituents including Rab GTPases.|||In DIAR2; patient enterocytes show alterations in junctional composition, loss of polarity in basolateral and apical compartments, loss of apical brush border and formation of microvillus inclusions in cells at the villus tips; the mutation causes the motor to move slowly along F-actin.|||In DIAR2; unknown pathological significance.|||In PFIC10 and DIAR2.|||In PFIC10.|||In PFIC10; decreased ABCB11 targeting to the apical/canalicular plasma membrane in hepatocytes from a homozygous patient.|||In PFIC10; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Myosin N-terminal SH3-like|||Myosin motor|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Requires for interaction with LIMA1|||Unconventional myosin-Vb                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123460|||http://purl.uniprot.org/annotation/VAR_054993|||http://purl.uniprot.org/annotation/VAR_054994|||http://purl.uniprot.org/annotation/VAR_054995|||http://purl.uniprot.org/annotation/VAR_056182|||http://purl.uniprot.org/annotation/VAR_056183|||http://purl.uniprot.org/annotation/VAR_056184|||http://purl.uniprot.org/annotation/VAR_056185|||http://purl.uniprot.org/annotation/VAR_063141|||http://purl.uniprot.org/annotation/VAR_063142|||http://purl.uniprot.org/annotation/VAR_071649|||http://purl.uniprot.org/annotation/VAR_071650|||http://purl.uniprot.org/annotation/VAR_071651|||http://purl.uniprot.org/annotation/VAR_071652|||http://purl.uniprot.org/annotation/VAR_071653|||http://purl.uniprot.org/annotation/VAR_071654|||http://purl.uniprot.org/annotation/VAR_071655|||http://purl.uniprot.org/annotation/VAR_071656|||http://purl.uniprot.org/annotation/VAR_071657|||http://purl.uniprot.org/annotation/VAR_071658|||http://purl.uniprot.org/annotation/VAR_072814|||http://purl.uniprot.org/annotation/VAR_072815|||http://purl.uniprot.org/annotation/VAR_087245|||http://purl.uniprot.org/annotation/VAR_087246|||http://purl.uniprot.org/annotation/VAR_087247|||http://purl.uniprot.org/annotation/VAR_087248|||http://purl.uniprot.org/annotation/VAR_087249|||http://purl.uniprot.org/annotation/VAR_087250|||http://purl.uniprot.org/annotation/VAR_087251|||http://purl.uniprot.org/annotation/VAR_087252|||http://purl.uniprot.org/annotation/VAR_087253|||http://purl.uniprot.org/annotation/VAR_087254|||http://purl.uniprot.org/annotation/VAR_087255|||http://purl.uniprot.org/annotation/VAR_087256|||http://purl.uniprot.org/annotation/VAR_087257|||http://purl.uniprot.org/annotation/VAR_087258|||http://purl.uniprot.org/annotation/VAR_087259|||http://purl.uniprot.org/annotation/VAR_087260|||http://purl.uniprot.org/annotation/VAR_087261|||http://purl.uniprot.org/annotation/VAR_087262|||http://purl.uniprot.org/annotation/VAR_087263|||http://purl.uniprot.org/annotation/VAR_087264|||http://purl.uniprot.org/annotation/VAR_087265|||http://purl.uniprot.org/annotation/VAR_087266|||http://purl.uniprot.org/annotation/VAR_087267|||http://purl.uniprot.org/annotation/VAR_087268|||http://purl.uniprot.org/annotation/VAR_087269|||http://purl.uniprot.org/annotation/VAR_087270|||http://purl.uniprot.org/annotation/VAR_087271|||http://purl.uniprot.org/annotation/VAR_087272|||http://purl.uniprot.org/annotation/VAR_087273|||http://purl.uniprot.org/annotation/VAR_087274|||http://purl.uniprot.org/annotation/VAR_087275|||http://purl.uniprot.org/annotation/VAR_087276|||http://purl.uniprot.org/annotation/VAR_087277|||http://purl.uniprot.org/annotation/VAR_087278|||http://purl.uniprot.org/annotation/VAR_087279|||http://purl.uniprot.org/annotation/VAR_087280|||http://purl.uniprot.org/annotation/VAR_087281|||http://purl.uniprot.org/annotation/VAR_087282|||http://purl.uniprot.org/annotation/VAR_087283|||http://purl.uniprot.org/annotation/VAR_087284|||http://purl.uniprot.org/annotation/VAR_087285|||http://purl.uniprot.org/annotation/VAR_087286|||http://purl.uniprot.org/annotation/VAR_087287|||http://purl.uniprot.org/annotation/VAR_087288|||http://purl.uniprot.org/annotation/VAR_087289|||http://purl.uniprot.org/annotation/VSP_056198|||http://purl.uniprot.org/annotation/VSP_056199|||http://purl.uniprot.org/annotation/VSP_056200
http://togogenome.org/gene/9606:CDH24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UP0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-24|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003827|||http://purl.uniprot.org/annotation/PRO_0000003828|||http://purl.uniprot.org/annotation/VSP_008717|||http://purl.uniprot.org/annotation/VSP_008718|||http://purl.uniprot.org/annotation/VSP_008719
http://togogenome.org/gene/9606:PTF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTS3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pancreas transcription factor 1 subunit alpha|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233143|||http://purl.uniprot.org/annotation/VAR_049548
http://togogenome.org/gene/9606:MOCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96007|||http://purl.uniprot.org/uniprot/O96033                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand                                                                                  ^@                                                                                  1-thioglycine; alternate|||Glycyl adenylate; alternate|||In MOCODB.|||In MOCODB; in a patient with mild form of the disease; impairs interaction with MOCS2B.|||Molybdopterin synthase catalytic subunit|||Molybdopterin synthase sulfur carrier subunit|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163111|||http://purl.uniprot.org/annotation/PRO_0000209134|||http://purl.uniprot.org/annotation/VAR_012765|||http://purl.uniprot.org/annotation/VAR_050090|||http://purl.uniprot.org/annotation/VAR_050091|||http://purl.uniprot.org/annotation/VAR_050092|||http://purl.uniprot.org/annotation/VAR_050093|||http://purl.uniprot.org/annotation/VAR_050094|||http://purl.uniprot.org/annotation/VAR_054854
http://togogenome.org/gene/9606:CD40LG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29965                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD40 ligand, membrane form|||CD40 ligand, soluble form|||Cleavage|||Cytoplasmic|||Decreases ITGA5:ITGB1 binding, B-cell activation, activation of NF-kappa-B signaling, and anti-apoptotic signaling; in soluble form. No effect on CD40 binding; in soluble form.|||Decreases ITGA5:ITGB1 binding, B-cell activation, activation of NF-kappa-B signaling, and anti-apoptotic signaling; in soluble form. Slightly decreases CD40 binding; in soluble form.|||Decreases ITGA5:ITGB1 binding, B-cell activation, activation of NF-kappa-B signaling, and anti-apoptotic signaling; when associated with E-224 in soluble form. No effect on CD40 binding; when associated with E-224 in soluble form.|||Decreases ITGA5:ITGB1 binding, B-cell activation, activation of NF-kappa-B signaling, and anti-apoptotic signaling; when associated with E-226 in soluble form. No effect on CD40 binding; when associated with E-226 in soluble form.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In HIGM1.|||In HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling.|||In HIGM1; decreases ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; decreases activation of NF-kappa-B signaling; slightly decreases CD40 binding of the soluble form.|||In HIGM1; no effect on ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; increases NF-kappa-B signaling.|||In HIGM1; no effect on ITGA5:ITGB1 and ITGAV:ITGB3 binding of the soluble form; slightly increases NF-kappa-B signaling.|||N-linked (GlcNAc...) (complex) asparagine; alternate|||N-linked (GlcNAc...) (high mannose) asparagine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034484|||http://purl.uniprot.org/annotation/PRO_0000034485|||http://purl.uniprot.org/annotation/VAR_007513|||http://purl.uniprot.org/annotation/VAR_007514|||http://purl.uniprot.org/annotation/VAR_007515|||http://purl.uniprot.org/annotation/VAR_007516|||http://purl.uniprot.org/annotation/VAR_007517|||http://purl.uniprot.org/annotation/VAR_007518|||http://purl.uniprot.org/annotation/VAR_007519|||http://purl.uniprot.org/annotation/VAR_007520|||http://purl.uniprot.org/annotation/VAR_007521|||http://purl.uniprot.org/annotation/VAR_007522|||http://purl.uniprot.org/annotation/VAR_007523|||http://purl.uniprot.org/annotation/VAR_007524|||http://purl.uniprot.org/annotation/VAR_007525|||http://purl.uniprot.org/annotation/VAR_007526|||http://purl.uniprot.org/annotation/VAR_007527|||http://purl.uniprot.org/annotation/VAR_007528|||http://purl.uniprot.org/annotation/VAR_017922|||http://purl.uniprot.org/annotation/VAR_017923|||http://purl.uniprot.org/annotation/VAR_017924|||http://purl.uniprot.org/annotation/VAR_017925|||http://purl.uniprot.org/annotation/VAR_017926|||http://purl.uniprot.org/annotation/VAR_017927|||http://purl.uniprot.org/annotation/VAR_017928|||http://purl.uniprot.org/annotation/VAR_017929|||http://purl.uniprot.org/annotation/VAR_017930|||http://purl.uniprot.org/annotation/VAR_017931|||http://purl.uniprot.org/annotation/VAR_017932|||http://purl.uniprot.org/annotation/VAR_017933|||http://purl.uniprot.org/annotation/VAR_017934|||http://purl.uniprot.org/annotation/VAR_017935|||http://purl.uniprot.org/annotation/VAR_017936|||http://purl.uniprot.org/annotation/VAR_017937|||http://purl.uniprot.org/annotation/VAR_017938|||http://purl.uniprot.org/annotation/VAR_017939|||http://purl.uniprot.org/annotation/VAR_017940
http://togogenome.org/gene/9606:H4C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:FRRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome b561|||DOMON|||Ferric-chelate reductase 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reelin|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314843|||http://purl.uniprot.org/annotation/VSP_030400
http://togogenome.org/gene/9606:KLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1R3UCD2|||http://purl.uniprot.org/uniprot/P06870                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Associated with a significant decrease in urinary kallikrein activity.|||Charge relay system|||In isoform 2.|||Kallikrein-1|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Not associated with changes in urinary kallikrein activity.|||O-linked (GalNAc...) serine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027923|||http://purl.uniprot.org/annotation/PRO_0000027924|||http://purl.uniprot.org/annotation/PRO_5014274114|||http://purl.uniprot.org/annotation/VAR_006625|||http://purl.uniprot.org/annotation/VAR_006626|||http://purl.uniprot.org/annotation/VAR_014567|||http://purl.uniprot.org/annotation/VAR_014568|||http://purl.uniprot.org/annotation/VSP_037483
http://togogenome.org/gene/9606:SLCO5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUC7|||http://purl.uniprot.org/uniprot/Q9H2Y9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier organic anion transporter family member 5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191070|||http://purl.uniprot.org/annotation/VAR_022041|||http://purl.uniprot.org/annotation/VSP_045498|||http://purl.uniprot.org/annotation/VSP_045499|||http://purl.uniprot.org/annotation/VSP_045500
http://togogenome.org/gene/9606:POLR1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L6J2|||http://purl.uniprot.org/uniprot/Q9P1U0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase I subunit RPA12|||TFIIS-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121460|||http://purl.uniprot.org/annotation/VAR_052287
http://togogenome.org/gene/9606:EPB41L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ76|||http://purl.uniprot.org/uniprot/I6L9B1|||http://purl.uniprot.org/uniprot/O43491|||http://purl.uniprot.org/uniprot/Q59FD8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Band 4.1 C-terminal|||Band 4.1-like protein 2|||Basic and acidic residues|||C-terminal (CTD)|||Disordered|||FERM|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hydrophilic|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Spectrin--actin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219397|||http://purl.uniprot.org/annotation/VAR_020145|||http://purl.uniprot.org/annotation/VSP_042910|||http://purl.uniprot.org/annotation/VSP_045090|||http://purl.uniprot.org/annotation/VSP_047181|||http://purl.uniprot.org/annotation/VSP_047182
http://togogenome.org/gene/9606:ZNF705A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN79                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||KRAB|||Zinc finger protein 705A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233283|||http://purl.uniprot.org/annotation/VAR_033595|||http://purl.uniprot.org/annotation/VAR_059929|||http://purl.uniprot.org/annotation/VAR_059930|||http://purl.uniprot.org/annotation/VAR_059931
http://togogenome.org/gene/9606:ETV4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43268                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-226 and R-260.|||Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-226.|||Altered sumoylation pattern. Loss of sumoylation, ubiquitination and transcriptional activator function; when associated with R-96 and R-260.|||Disordered|||ETS|||ETS translocation variant 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Loss of polysumoylation and ubiquitination; when associated with A-228; A-262; A-324 and A-443.|||Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-324.|||Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-262 and A-443.|||Loss of polysumoylation and ubiquitination; when associated with A-98; A-228; A-324 and A-443.|||Loss of polysumoylation and ubiquitination; when associated with A-98; A-262; A-324 and A-443.|||Loss of sumoylation at K-96.|||Normal sumoylation at K-96.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204116|||http://purl.uniprot.org/annotation/VAR_048950|||http://purl.uniprot.org/annotation/VAR_069110|||http://purl.uniprot.org/annotation/VSP_046036|||http://purl.uniprot.org/annotation/VSP_055314
http://togogenome.org/gene/9606:ADGRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor A3|||Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Ig-like|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012900|||http://purl.uniprot.org/annotation/VAR_033971|||http://purl.uniprot.org/annotation/VAR_033972|||http://purl.uniprot.org/annotation/VSP_010738|||http://purl.uniprot.org/annotation/VSP_010740|||http://purl.uniprot.org/annotation/VSP_010741|||http://purl.uniprot.org/annotation/VSP_010742|||http://purl.uniprot.org/annotation/VSP_010743|||http://purl.uniprot.org/annotation/VSP_010744|||http://purl.uniprot.org/annotation/VSP_010745|||http://purl.uniprot.org/annotation/VSP_010746
http://togogenome.org/gene/9606:PDCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13371                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylthreonine|||Phosducin-like protein|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000163755|||http://purl.uniprot.org/annotation/VAR_050525|||http://purl.uniprot.org/annotation/VSP_053571
http://togogenome.org/gene/9606:LYPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8E0|||http://purl.uniprot.org/uniprot/Q6UWN0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GPI-anchor amidated alanine|||In isoform 2.|||Ly6/PLAUR domain-containing protein 4|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226759|||http://purl.uniprot.org/annotation/PRO_0000226760|||http://purl.uniprot.org/annotation/PRO_5014297541|||http://purl.uniprot.org/annotation/VAR_052703|||http://purl.uniprot.org/annotation/VSP_017506
http://togogenome.org/gene/9606:LYZL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A080YUZ9|||http://purl.uniprot.org/uniprot/Q7Z4W2                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lysozyme|||Glycosyl hydrolases family 22 (GH22)|||In isoform 2.|||Lysozyme-like protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240637|||http://purl.uniprot.org/annotation/VAR_026818|||http://purl.uniprot.org/annotation/VSP_019717
http://togogenome.org/gene/9606:LGALSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCW2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin-related protein|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315766
http://togogenome.org/gene/9606:WASHC2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5W5|||http://purl.uniprot.org/uniprot/B3KMC4|||http://purl.uniprot.org/uniprot/Q9Y4E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Disrupts interaction with F-actin-capping protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3).|||Disrupts interaction with VPS35.|||FAM21/CAPZIP|||Impairs interaction with VPS35.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Interaction with VPS35|||Interaction with phospholipids|||LFa 1|||LFa 10|||LFa 11|||LFa 12|||LFa 13|||LFa 14|||LFa 15|||LFa 16|||LFa 17|||LFa 18|||LFa 19|||LFa 2|||LFa 20|||LFa 21|||LFa 3|||LFa 4|||LFa 5|||LFa 6|||LFa 7|||LFa 8|||LFa 9|||Phosphoserine|||Polar residues|||Required for interaction with F-actin-capping protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)|||Sufficient for interaction with CCDC93|||Sufficient for interaction with WASHC3, WASHC4 and WASHC5; required for interaction with WASHC1|||WASH complex subunit 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186714|||http://purl.uniprot.org/annotation/VSP_061811|||http://purl.uniprot.org/annotation/VSP_061812|||http://purl.uniprot.org/annotation/VSP_061813|||http://purl.uniprot.org/annotation/VSP_061814|||http://purl.uniprot.org/annotation/VSP_061815|||http://purl.uniprot.org/annotation/VSP_061816|||http://purl.uniprot.org/annotation/VSP_061817
http://togogenome.org/gene/9606:PPWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTS1|||http://purl.uniprot.org/uniprot/B4DP34|||http://purl.uniprot.org/uniprot/B4DT22|||http://purl.uniprot.org/uniprot/F5H7P7|||http://purl.uniprot.org/uniprot/Q96BP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||PPIase cyclophilin-type|||Peptidylprolyl isomerase domain and WD repeat-containing protein 1|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240306|||http://purl.uniprot.org/annotation/VSP_055266
http://togogenome.org/gene/9606:TPGS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUC8|||http://purl.uniprot.org/uniprot/K7EKC0|||http://purl.uniprot.org/uniprot/Q68CL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Knr4/Smi1-like|||Polar residues|||Tubulin polyglutamylase complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079304|||http://purl.uniprot.org/annotation/VAR_027410|||http://purl.uniprot.org/annotation/VSP_014884|||http://purl.uniprot.org/annotation/VSP_014885|||http://purl.uniprot.org/annotation/VSP_020113|||http://purl.uniprot.org/annotation/VSP_054525|||http://purl.uniprot.org/annotation/VSP_055634
http://togogenome.org/gene/9606:ZNF75D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51815|||http://purl.uniprot.org/uniprot/Q86TD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||SCAN box|||Zinc finger protein 75D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047384|||http://purl.uniprot.org/annotation/VSP_044460
http://togogenome.org/gene/9606:MUC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6W4X9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1; truncated|||2|||Approximate repeats|||CTCK|||Disordered|||Mucin-6|||N-linked (GlcNAc...) asparagine|||Polar residues|||TIL|||VWFD 1|||VWFD 2|||VWFD 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259496|||http://purl.uniprot.org/annotation/VAR_059542|||http://purl.uniprot.org/annotation/VAR_061488
http://togogenome.org/gene/9606:HNRNPDL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUK2|||http://purl.uniprot.org/uniprot/O14979                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein D-like|||In LGMDD3.|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-acetyllysine|||N6-methyllysine|||Necessary for interaction with TNPO1|||Necessary for its nuclear import and export|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2|||Reduces significantly its nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287239|||http://purl.uniprot.org/annotation/VAR_072567|||http://purl.uniprot.org/annotation/VAR_072568|||http://purl.uniprot.org/annotation/VSP_025410|||http://purl.uniprot.org/annotation/VSP_025411
http://togogenome.org/gene/9606:RXRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHH6|||http://purl.uniprot.org/uniprot/P19793|||http://purl.uniprot.org/uniprot/Q6P3U7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes acetylation by EP300, DNA binding and transcriptional activity. Impairs interaction with EP300.|||Abolishes acetylation by EP300.|||Abolishes nuclear export.|||Abolishes nuclear localization and transcriptional activity.|||Abolishes nuclear localization.|||Abolishes phosphorylation. No change in increase of RARA-mediated transcriptional activity.|||As a heterodimer with NR1H4, impairs interaction with coactivator NCOA1. Impairs transcriptional activity.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Hinge|||In isoform 2.|||Increase in RARA-mediated transcriptional activity.|||Modulating|||N6-acetyllysine; by EP300|||NR C4-type|||NR LBD|||No impact on acetylation by EP300.|||Nuclear localization signal|||Nuclear receptor|||Phosphoserine|||Phosphoserine; by MAPK8 and MAPK9|||Phosphothreonine; by MAPK8 and MAPK9|||Polar residues|||Required for nuclear export|||Retinoic acid receptor RXR-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053566|||http://purl.uniprot.org/annotation/VAR_014620|||http://purl.uniprot.org/annotation/VAR_014621|||http://purl.uniprot.org/annotation/VAR_050582|||http://purl.uniprot.org/annotation/VAR_050583|||http://purl.uniprot.org/annotation/VSP_056565
http://togogenome.org/gene/9606:UGT1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22309|||http://purl.uniprot.org/uniprot/Q5DT03                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Decreased SN-38 glucuronosyltransferase activity.|||Helical|||In CN1 and CN2.|||In CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4.|||In CN1.|||In CN1; has no residual bilirubin glucuronidation activity.|||In CN1; has no residual bilirubin glucuronidation activity; N-glycosylation does take place at this new additional site.|||In CN1; no bilirubin glucuronidation activity.|||In CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity.|||In CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity.|||In CN2, GILBS and HBLRTFN; has significant residual bilirubin glucuronidation activity of about 25% to 50% of that of the wild-type protein; displays no change in biluribin affinity.|||In CN2.|||In CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein.|||In CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein.|||In CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein.|||In CN2; has no residual bilirubin glucuronidation activity.|||In CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein.|||In CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell.|||In GILBS and CN2; 40-55% normal bilirubin glucuronidation activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype.|||In GILBS.|||In GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036000|||http://purl.uniprot.org/annotation/PRO_5014205883|||http://purl.uniprot.org/annotation/VAR_007695|||http://purl.uniprot.org/annotation/VAR_007697|||http://purl.uniprot.org/annotation/VAR_007698|||http://purl.uniprot.org/annotation/VAR_007699|||http://purl.uniprot.org/annotation/VAR_007700|||http://purl.uniprot.org/annotation/VAR_007701|||http://purl.uniprot.org/annotation/VAR_007702|||http://purl.uniprot.org/annotation/VAR_007703|||http://purl.uniprot.org/annotation/VAR_007704|||http://purl.uniprot.org/annotation/VAR_007705|||http://purl.uniprot.org/annotation/VAR_007706|||http://purl.uniprot.org/annotation/VAR_007707|||http://purl.uniprot.org/annotation/VAR_007708|||http://purl.uniprot.org/annotation/VAR_007709|||http://purl.uniprot.org/annotation/VAR_009504|||http://purl.uniprot.org/annotation/VAR_009505|||http://purl.uniprot.org/annotation/VAR_012283|||http://purl.uniprot.org/annotation/VAR_019410|||http://purl.uniprot.org/annotation/VAR_019411|||http://purl.uniprot.org/annotation/VAR_019412|||http://purl.uniprot.org/annotation/VAR_025355|||http://purl.uniprot.org/annotation/VAR_026134|||http://purl.uniprot.org/annotation/VAR_026135|||http://purl.uniprot.org/annotation/VAR_026136|||http://purl.uniprot.org/annotation/VAR_026137|||http://purl.uniprot.org/annotation/VAR_026138|||http://purl.uniprot.org/annotation/VAR_026139|||http://purl.uniprot.org/annotation/VAR_026140|||http://purl.uniprot.org/annotation/VAR_026141|||http://purl.uniprot.org/annotation/VAR_026142|||http://purl.uniprot.org/annotation/VAR_026143|||http://purl.uniprot.org/annotation/VAR_026144|||http://purl.uniprot.org/annotation/VAR_026145|||http://purl.uniprot.org/annotation/VAR_026146|||http://purl.uniprot.org/annotation/VAR_026147|||http://purl.uniprot.org/annotation/VAR_026148|||http://purl.uniprot.org/annotation/VAR_026149|||http://purl.uniprot.org/annotation/VAR_026150|||http://purl.uniprot.org/annotation/VAR_064955|||http://purl.uniprot.org/annotation/VAR_064956|||http://purl.uniprot.org/annotation/VAR_064957|||http://purl.uniprot.org/annotation/VAR_064958|||http://purl.uniprot.org/annotation/VAR_064959|||http://purl.uniprot.org/annotation/VAR_064960|||http://purl.uniprot.org/annotation/VAR_064961|||http://purl.uniprot.org/annotation/VAR_071402|||http://purl.uniprot.org/annotation/VAR_071403|||http://purl.uniprot.org/annotation/VAR_071404|||http://purl.uniprot.org/annotation/VSP_053958
http://togogenome.org/gene/9606:FOXI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E0XEN6|||http://purl.uniprot.org/uniprot/Q12951                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein I1|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091846|||http://purl.uniprot.org/annotation/VAR_049160|||http://purl.uniprot.org/annotation/VAR_049161|||http://purl.uniprot.org/annotation/VSP_001543
http://togogenome.org/gene/9606:PPP1R9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SB3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Actin-binding|||Basic and acidic residues|||Disordered|||Interaction with ADRA2A, ADRA2B and ADRA2C|||Interaction with D(2) dopamine receptor|||Interaction with RGS2|||Interaction with TGN38|||Interaction with protein phosphatase 1|||Neurabin-2|||PDZ|||PP1-binding motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228614|||http://purl.uniprot.org/annotation/VAR_059776
http://togogenome.org/gene/9606:PPIAL4G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DN37                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324639
http://togogenome.org/gene/9606:NUMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49757                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9.|||In isoform 3, isoform 4, isoform 6 and isoform 8.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 7 and isoform 8.|||In isoform 9.|||Loss of AAK1-mediated phosphorylation.|||PID|||Phosphoserine|||Phosphoserine; by CaMK1|||Phosphothreonine|||Phosphothreonine; by AAK1|||Polar residues|||Pro residues|||Protein numb homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058001|||http://purl.uniprot.org/annotation/VAR_051249|||http://purl.uniprot.org/annotation/VAR_051250|||http://purl.uniprot.org/annotation/VSP_004348|||http://purl.uniprot.org/annotation/VSP_004349|||http://purl.uniprot.org/annotation/VSP_047756|||http://purl.uniprot.org/annotation/VSP_053745|||http://purl.uniprot.org/annotation/VSP_053763
http://togogenome.org/gene/9606:UNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KTA5|||http://purl.uniprot.org/uniprot/E5KTA6|||http://purl.uniprot.org/uniprot/P13051                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosine-DNA glycosylase activity.|||Disordered|||FAM72A-binding|||In HIGM5; fully active and stable when expressed in E.coli; mistargeted to mitochondria rather than the nucleus.|||In isoform 1.|||Loss of activity.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Thymine-DNA glycosylase activity.|||Uracil-DNA glycosylase|||Uracil-DNA glycosylase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000176173|||http://purl.uniprot.org/annotation/VAR_017094|||http://purl.uniprot.org/annotation/VAR_052697|||http://purl.uniprot.org/annotation/VSP_008513
http://togogenome.org/gene/9606:SLC35E3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z769                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Solute carrier family 35 member E3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297899
http://togogenome.org/gene/9606:GLP1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A142FHB8|||http://purl.uniprot.org/uniprot/P43220                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine|||ADP-ribosylcysteine|||Abolishes inhibition by negative allosteric modulators.|||Abolishes inhibition by the negative allosteric modulators NNC0640 and PF-06372222, but does not abolish inhibition by MK-0893.|||Abolishes stimulation of cAMP accumulation in response to GLP-1.|||Causes the formation of an artifactual disulfide bond that abolishes signaling in response to GLP-1 binding; when associated with C-317.|||Causes the formation of an artifactual disulfide bond that abolishes signaling in response to GLP-1 binding; when associated with C-361.|||Cytoplasmic|||Decreases sensitivity to GLP-1.|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Glucagon-like peptide 1 receptor|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for allosteric inhibitor binding|||Interaction with the endogenous ligand GLP-1|||N-linked (GlcNAc...) asparagine|||No effect on stimulation of cAMP accumulation and on GLP-1 binding.|||No effect on stimulation of cAMP accumulation in response to GLP-1.|||Slightly decreases stimulation of cAMP accumulation in response to GLP-1.|||Strongly decreased stimulation of cAMP accumulation in response to GLP-1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012835|||http://purl.uniprot.org/annotation/PRO_5007494908|||http://purl.uniprot.org/annotation/VAR_015098|||http://purl.uniprot.org/annotation/VAR_018924|||http://purl.uniprot.org/annotation/VAR_018925|||http://purl.uniprot.org/annotation/VAR_018926|||http://purl.uniprot.org/annotation/VAR_018927|||http://purl.uniprot.org/annotation/VAR_018928|||http://purl.uniprot.org/annotation/VAR_018929|||http://purl.uniprot.org/annotation/VAR_018930|||http://purl.uniprot.org/annotation/VAR_018931
http://togogenome.org/gene/9606:AP3M2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYL6|||http://purl.uniprot.org/uniprot/P53677                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  AP-3 complex subunit mu-2|||In isoform 2.|||MHD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193784|||http://purl.uniprot.org/annotation/VSP_055790|||http://purl.uniprot.org/annotation/VSP_055791
http://togogenome.org/gene/9606:ITGA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13683|||http://purl.uniprot.org/uniprot/Q4LE35                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||3 X 4 AA repeats of D-X-H-P|||Basic and acidic residues|||Cleavage; by urokinase|||Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 2.|||In isoform Alpha-7X1B and isoform 2.|||In isoform Alpha-7X1X2A.|||In isoform Alpha-7X2B.|||In isoform Alpha-7X2DB.|||Integrin alpha-2|||Integrin alpha-7|||Integrin alpha-7 70 kDa form|||Integrin alpha-7 heavy chain|||Integrin alpha-7 light chain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016267|||http://purl.uniprot.org/annotation/PRO_0000016268|||http://purl.uniprot.org/annotation/PRO_0000016269|||http://purl.uniprot.org/annotation/PRO_0000398833|||http://purl.uniprot.org/annotation/VAR_014759|||http://purl.uniprot.org/annotation/VAR_067015|||http://purl.uniprot.org/annotation/VAR_067016|||http://purl.uniprot.org/annotation/VAR_067017|||http://purl.uniprot.org/annotation/VAR_067018|||http://purl.uniprot.org/annotation/VSP_002727|||http://purl.uniprot.org/annotation/VSP_002728|||http://purl.uniprot.org/annotation/VSP_002730|||http://purl.uniprot.org/annotation/VSP_040487|||http://purl.uniprot.org/annotation/VSP_040488|||http://purl.uniprot.org/annotation/VSP_042364
http://togogenome.org/gene/9606:FAM135B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49AJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Protein FAM135B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314171|||http://purl.uniprot.org/annotation/VAR_053980|||http://purl.uniprot.org/annotation/VAR_053981|||http://purl.uniprot.org/annotation/VAR_062218|||http://purl.uniprot.org/annotation/VAR_062219|||http://purl.uniprot.org/annotation/VSP_030232|||http://purl.uniprot.org/annotation/VSP_030233|||http://purl.uniprot.org/annotation/VSP_030234|||http://purl.uniprot.org/annotation/VSP_030235|||http://purl.uniprot.org/annotation/VSP_030236
http://togogenome.org/gene/9606:PMEPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JY37|||http://purl.uniprot.org/uniprot/Q969W9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Impairs interaction with NEDD4. Impairs polyubiquitination of AR; when associated with A-232.|||In isoform 2.|||In isoform 3.|||Lumenal|||PPxY motif 1|||PPxY motif 2|||Polar residues|||Protein TMEPAI|||SMAD interaction motif (SIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185442|||http://purl.uniprot.org/annotation/VAR_062154|||http://purl.uniprot.org/annotation/VSP_006438|||http://purl.uniprot.org/annotation/VSP_044588
http://togogenome.org/gene/9606:METTL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7U3|||http://purl.uniprot.org/uniprot/B3KW44|||http://purl.uniprot.org/uniprot/B4DLT0|||http://purl.uniprot.org/uniprot/Q9H825                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Abolished N(3)-methylcytidine methyltransferase activity.|||Abolished SUMOylation.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||Methyltransferase|||Mitochondrion|||Partial relocalization to the cytoplasm; when associated with Q-4.|||Partial relocalization to the cytoplasm; when associated with Q-9.|||tRNA N(3)-methylcytidine methyltransferase METTL8, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311291|||http://purl.uniprot.org/annotation/VSP_029514
http://togogenome.org/gene/9606:TMT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX53                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Signal Peptide                                                                                  ^@                                                                                  Loss of catalytic activity.|||Thiol S-methyltransferase TMT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251922
http://togogenome.org/gene/9606:PTDSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVG9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphatidylserine synthase 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056832
http://togogenome.org/gene/9606:TIMM10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4A9|||http://purl.uniprot.org/uniprot/Q9Y5J6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Sequence Variant                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit Tim10 B|||Tim10-like|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193598|||http://purl.uniprot.org/annotation/VAR_025665|||http://purl.uniprot.org/annotation/VAR_061843
http://togogenome.org/gene/9606:NDUFA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16795                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In MC1DN26; loss of function in complex I assembly; accumulation of several low and high molecular weight assembly intermediates is observed in patient fibroblasts.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019992|||http://purl.uniprot.org/annotation/VAR_078936|||http://purl.uniprot.org/annotation/VAR_081457
http://togogenome.org/gene/9606:ZNF75A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJE0|||http://purl.uniprot.org/uniprot/Q68CU0|||http://purl.uniprot.org/uniprot/Q96N20                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||In a breast cancer sample; somatic mutation.|||KRAB|||SCAN box|||Zinc finger protein 75A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047385|||http://purl.uniprot.org/annotation/VAR_033545|||http://purl.uniprot.org/annotation/VAR_035570
http://togogenome.org/gene/9606:CCDC134                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0QY51|||http://purl.uniprot.org/uniprot/B4DRL0|||http://purl.uniprot.org/uniprot/Q9H6E4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Motif|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 134|||Disordered|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254109|||http://purl.uniprot.org/annotation/PRO_5002753633|||http://purl.uniprot.org/annotation/PRO_5002800985
http://togogenome.org/gene/9606:STX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNK0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Phosphoserine|||Syntaxin-8|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210217
http://togogenome.org/gene/9606:RAB11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15907                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Citrulline|||Constitutively active mutant locked in the active GTP-bound form; alters apical recycling.|||Cysteine methyl ester|||Disordered|||Dominant negative mutant locked in the inactive GDP-bound form; alters apical recycling. Does not interact with ZFYV2E and KIF5A.|||Effector region|||In NDAGSCW.|||In isoform 2.|||N-acetylglycine|||Polar residues|||Ras-related protein Rab-11B|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121158|||http://purl.uniprot.org/annotation/PRO_0000370815|||http://purl.uniprot.org/annotation/VAR_080598|||http://purl.uniprot.org/annotation/VAR_080599|||http://purl.uniprot.org/annotation/VSP_055832
http://togogenome.org/gene/9606:ANKRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYH5|||http://purl.uniprot.org/uniprot/Q15327                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 1|||Found in a sporadic case of total anomalous pulmonary venous return; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240479|||http://purl.uniprot.org/annotation/VAR_047112
http://togogenome.org/gene/9606:ZDHHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L202|||http://purl.uniprot.org/uniprot/Q8WTX9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||Lumenal|||Mediates interaction with STING1|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC1|||Polar residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212857|||http://purl.uniprot.org/annotation/VAR_052972
http://togogenome.org/gene/9606:KRTAP12-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59990                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 5 AA approximate repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 12-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185196
http://togogenome.org/gene/9606:GABARAPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60520                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Cleavage; by ATG4|||Gamma-aminobutyric acid receptor-associated protein-like 2|||Impaired phosphorylation by TBK1.|||Impairs localization at the autophagosomal membrane.|||N6-acetyllysine|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Phospho-mimetic mutant; abolished localization to autophagosomes.|||Phospho-mimetic mutant; impaired interaction with ATG4 proteins, preventing cleavage at the C-terminus, conjugation to phosphatidylethanolamine.|||Phosphoserine|||Phosphoserine; by TBK1|||Removed in mature form|||Strongly reduced interaction with UBA5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212373|||http://purl.uniprot.org/annotation/PRO_0000423070|||http://purl.uniprot.org/annotation/VAR_049756
http://togogenome.org/gene/9606:CLEC18B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXF7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 18 member B|||EGF-like|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324315|||http://purl.uniprot.org/annotation/VSP_037307|||http://purl.uniprot.org/annotation/VSP_037308|||http://purl.uniprot.org/annotation/VSP_037309
http://togogenome.org/gene/9606:ACP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPH0                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity by interfering with water access to the active site cavity.|||Abolishes enzyme activity.|||Decreases activity toward substrates with medium and long aliphatic chains, but not toward substrates with short aliphatic chains.|||Decreases enzyme activity by interfering with water access to the active site cavity.|||Decreases enzyme activity.|||In isoform 2.|||Lysophosphatidic acid phosphatase type 6|||Mitochondrion|||Nucleophile|||Proton donor|||Substrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023965|||http://purl.uniprot.org/annotation/VAR_022678|||http://purl.uniprot.org/annotation/VSP_014121|||http://purl.uniprot.org/annotation/VSP_014122
http://togogenome.org/gene/9606:KLHL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVR0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch-like protein 11|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243918
http://togogenome.org/gene/9606:OR4X1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH49                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4X1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150570|||http://purl.uniprot.org/annotation/VAR_034210|||http://purl.uniprot.org/annotation/VAR_034211|||http://purl.uniprot.org/annotation/VAR_034212|||http://purl.uniprot.org/annotation/VAR_053178|||http://purl.uniprot.org/annotation/VAR_053179
http://togogenome.org/gene/9606:LAIR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZ84|||http://purl.uniprot.org/uniprot/D3YTC8|||http://purl.uniprot.org/uniprot/Q6GTX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like C2-type|||Immunoglobulin subtype|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Leukocyte-associated immunoglobulin-like receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Reduced tyrosine phosphorylation and loss of binding to PTPN6 and CSK as well as complete loss of inhibitory activity. Loss of phosphorylation and of inhibition of calcium mobilization; when associated with F-281.|||Reduced tyrosine phosphorylation and loss of binding to PTPN6. Partial inhibition of cytotoxic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250682|||http://purl.uniprot.org/annotation/PRO_5003052449|||http://purl.uniprot.org/annotation/VAR_027598|||http://purl.uniprot.org/annotation/VAR_085777|||http://purl.uniprot.org/annotation/VAR_085778|||http://purl.uniprot.org/annotation/VAR_085779|||http://purl.uniprot.org/annotation/VSP_020710|||http://purl.uniprot.org/annotation/VSP_020711|||http://purl.uniprot.org/annotation/VSP_020712
http://togogenome.org/gene/9606:OR51E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK0|||http://purl.uniprot.org/uniprot/Q9H255                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150751
http://togogenome.org/gene/9606:NUDT17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C025                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Nucleoside diphosphate-linked moiety X motif 17|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019953
http://togogenome.org/gene/9606:TRAFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14545                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||TRAF-type|||TRAF-type zinc finger domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278457|||http://purl.uniprot.org/annotation/VSP_056085|||http://purl.uniprot.org/annotation/VSP_056086
http://togogenome.org/gene/9606:AIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVV5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Androgen-induced gene 1 protein|||Cytoplasmic|||Extracellular|||Helical|||Important for catalytic activity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of hydrolase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190098|||http://purl.uniprot.org/annotation/VAR_057502|||http://purl.uniprot.org/annotation/VSP_060689|||http://purl.uniprot.org/annotation/VSP_060690|||http://purl.uniprot.org/annotation/VSP_060691|||http://purl.uniprot.org/annotation/VSP_060692|||http://purl.uniprot.org/annotation/VSP_060693|||http://purl.uniprot.org/annotation/VSP_060694|||http://purl.uniprot.org/annotation/VSP_060695
http://togogenome.org/gene/9606:SPACA5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN7|||http://purl.uniprot.org/uniprot/Q96QH8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  C-type lysozyme|||Sperm acrosome-associated protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284470|||http://purl.uniprot.org/annotation/PRO_5010061088
http://togogenome.org/gene/9606:ASPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45381|||http://purl.uniprot.org/uniprot/Q6FH48                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-fold decrease in activity.|||Abolishes enzymatic activity.|||Aspartoacylase|||In CAND.|||In CAND; 12% residual enzyme activity.|||In CAND; 3% residual enzyme activity.|||In CAND; 5.5% residual enzyme activity.|||In CAND; <0.5% residual enzyme activity.|||In CAND; <1% residual enzyme activity.|||In CAND; Loss of catalytic activity.|||In CAND; about 25% residual enzyme activity.|||In CAND; loss of activity.|||In CAND; pan-European origin; most prevalent among non-Jewish CAND patients; probably the most ancient mutation; loss of activity.|||In CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity.|||In CAND; undetectable enzyme activity.|||Reduces activity by 99%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216871|||http://purl.uniprot.org/annotation/VAR_004995|||http://purl.uniprot.org/annotation/VAR_004996|||http://purl.uniprot.org/annotation/VAR_004997|||http://purl.uniprot.org/annotation/VAR_004998|||http://purl.uniprot.org/annotation/VAR_004999|||http://purl.uniprot.org/annotation/VAR_005000|||http://purl.uniprot.org/annotation/VAR_005001|||http://purl.uniprot.org/annotation/VAR_016778|||http://purl.uniprot.org/annotation/VAR_016779|||http://purl.uniprot.org/annotation/VAR_016780|||http://purl.uniprot.org/annotation/VAR_016781|||http://purl.uniprot.org/annotation/VAR_016782|||http://purl.uniprot.org/annotation/VAR_016783|||http://purl.uniprot.org/annotation/VAR_016784|||http://purl.uniprot.org/annotation/VAR_016785|||http://purl.uniprot.org/annotation/VAR_016786|||http://purl.uniprot.org/annotation/VAR_016787|||http://purl.uniprot.org/annotation/VAR_016788|||http://purl.uniprot.org/annotation/VAR_039079|||http://purl.uniprot.org/annotation/VAR_039080|||http://purl.uniprot.org/annotation/VAR_039081|||http://purl.uniprot.org/annotation/VAR_039082|||http://purl.uniprot.org/annotation/VAR_039083|||http://purl.uniprot.org/annotation/VAR_039084|||http://purl.uniprot.org/annotation/VAR_039085|||http://purl.uniprot.org/annotation/VAR_039086|||http://purl.uniprot.org/annotation/VAR_039087|||http://purl.uniprot.org/annotation/VAR_039088|||http://purl.uniprot.org/annotation/VAR_039089|||http://purl.uniprot.org/annotation/VAR_039090|||http://purl.uniprot.org/annotation/VAR_039091|||http://purl.uniprot.org/annotation/VAR_078086|||http://purl.uniprot.org/annotation/VAR_078087|||http://purl.uniprot.org/annotation/VAR_078088|||http://purl.uniprot.org/annotation/VAR_078089|||http://purl.uniprot.org/annotation/VAR_078090|||http://purl.uniprot.org/annotation/VAR_078091|||http://purl.uniprot.org/annotation/VAR_078092|||http://purl.uniprot.org/annotation/VAR_078093|||http://purl.uniprot.org/annotation/VAR_078094|||http://purl.uniprot.org/annotation/VAR_078095|||http://purl.uniprot.org/annotation/VAR_078096|||http://purl.uniprot.org/annotation/VAR_078097|||http://purl.uniprot.org/annotation/VAR_078098
http://togogenome.org/gene/9606:PDLIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00151|||http://purl.uniprot.org/uniprot/V9HW92                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  LIM zinc-binding|||N-acetylthreonine|||PDZ|||PDZ and LIM domain protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075859|||http://purl.uniprot.org/annotation/VAR_022271
http://togogenome.org/gene/9606:PIK3R5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L7RT34|||http://purl.uniprot.org/uniprot/Q8WYR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Heterodimerization|||In AOA3.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with beta-gamma G protein dimers|||N-acetylmethionine|||Phosphoinositide 3-kinase regulatory subunit 5|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058421|||http://purl.uniprot.org/annotation/VAR_036227|||http://purl.uniprot.org/annotation/VAR_067052|||http://purl.uniprot.org/annotation/VSP_016388
http://togogenome.org/gene/9606:MCU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE86                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes calcium channel activity.|||According to a report, inhibits calcium uptake. According to a subsequent report, does not affect greatly calcium uptake.|||Calcium uniporter protein, mitochondrial|||DXXE|||Decreased MCU current; when associated with A-57.|||Decreased MCU current; when associated with A-92.|||Does not affect greatly calcium uptake.|||Does not inhibit calcium uptake. Strongly reduced sensitivity to ruthenium red inhibition.|||Dominant negative (DN) mutant; inhibits calcium uptake. Inhibits calcium channel activity. Expression of the dominant negative protein in mice, leads to mice that are incapable of physiological fight or flight heart rate acceleration.|||Helical|||Impairs Ca(2+) uptake, but has no effect on oligomerization and interaction with MCU1 and MCU2.|||In isoform 2.|||In isoform 3.|||Inner juxtamembrane helix (IJMH)|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N-terminal MCU domain|||N6-acetyllysine|||No effect on Ca(2+) uptake, oligomerization and interaction with MCU1 and MCU2.|||Outer juxtamembrane helix (OJMH)|||Partially functional; does not completely abolish calcium channel activity.|||Phosphoserine; by CaMK2|||Prevents entrance of calcium into the pore.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282976|||http://purl.uniprot.org/annotation/VSP_024263|||http://purl.uniprot.org/annotation/VSP_041687
http://togogenome.org/gene/9606:TBC1D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60343                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-642.|||80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-751.|||80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-642 and A-751.|||80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-588; A-642 and A-751.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Loss of Rab GTPase activation. Only 20% reduction of GLUT4 translocation; even when associated with A-318; A-588; A-642 and A-751.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||PID 1|||PID 2|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Pro residues|||Rab-GAP TBC|||TBC1 domain family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208026|||http://purl.uniprot.org/annotation/VAR_052534|||http://purl.uniprot.org/annotation/VAR_052535|||http://purl.uniprot.org/annotation/VAR_054862|||http://purl.uniprot.org/annotation/VAR_059855|||http://purl.uniprot.org/annotation/VAR_061891|||http://purl.uniprot.org/annotation/VAR_061892|||http://purl.uniprot.org/annotation/VSP_036868|||http://purl.uniprot.org/annotation/VSP_036869|||http://purl.uniprot.org/annotation/VSP_036870|||http://purl.uniprot.org/annotation/VSP_036871
http://togogenome.org/gene/9606:HOXB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09629                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200142|||http://purl.uniprot.org/annotation/VAR_058204
http://togogenome.org/gene/9606:DDX39A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00148                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX39A|||Acidic residues|||DECD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055067|||http://purl.uniprot.org/annotation/VAR_052166|||http://purl.uniprot.org/annotation/VSP_046559|||http://purl.uniprot.org/annotation/VSP_046560|||http://purl.uniprot.org/annotation/VSP_057426|||http://purl.uniprot.org/annotation/VSP_057427
http://togogenome.org/gene/9606:VWA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KMH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PEX7|||Mitochondrion|||N-linked (GlcNAc...) asparagine|||VWFA|||von Willebrand factor A domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342685|||http://purl.uniprot.org/annotation/VAR_044337|||http://purl.uniprot.org/annotation/VAR_044338|||http://purl.uniprot.org/annotation/VAR_044339|||http://purl.uniprot.org/annotation/VAR_044340|||http://purl.uniprot.org/annotation/VAR_049512|||http://purl.uniprot.org/annotation/VAR_061239|||http://purl.uniprot.org/annotation/VSP_034533|||http://purl.uniprot.org/annotation/VSP_061575
http://togogenome.org/gene/9606:AVP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01185|||http://purl.uniprot.org/uniprot/X5DQP6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Arg-vasopressin|||Copeptin|||Gain of antagonist activity on V1aR/AVPR1A (and loss of agonist activity on this receptor). 42-fold decrease in affinity for V1aR/AVPR1A, 2000-fold decrease in affinity for V1bR/AVPR1B, 5-fold decrease in affinity for V2R/AVPR2 and no change in affinity for oxytocin receptor (OXTR).|||Glycine amide|||Important for agonist activity on V1aR/AVPR1A|||In NDI.|||In NDI; probably causes insufficient processing of precursor.|||In NDI; strong accumulation in the endoplasmic reticulum and an altered morphology of this organelle.|||In NDI; weakly active.|||N-linked (GlcNAc...) asparagine|||Neurophysin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020515|||http://purl.uniprot.org/annotation/PRO_0000020516|||http://purl.uniprot.org/annotation/PRO_0000020517|||http://purl.uniprot.org/annotation/PRO_5014316171|||http://purl.uniprot.org/annotation/VAR_004980|||http://purl.uniprot.org/annotation/VAR_004981|||http://purl.uniprot.org/annotation/VAR_004982|||http://purl.uniprot.org/annotation/VAR_004983|||http://purl.uniprot.org/annotation/VAR_004984|||http://purl.uniprot.org/annotation/VAR_004985|||http://purl.uniprot.org/annotation/VAR_004986|||http://purl.uniprot.org/annotation/VAR_004987|||http://purl.uniprot.org/annotation/VAR_004988|||http://purl.uniprot.org/annotation/VAR_004989|||http://purl.uniprot.org/annotation/VAR_004990|||http://purl.uniprot.org/annotation/VAR_004991|||http://purl.uniprot.org/annotation/VAR_004992|||http://purl.uniprot.org/annotation/VAR_004993|||http://purl.uniprot.org/annotation/VAR_004994|||http://purl.uniprot.org/annotation/VAR_011894|||http://purl.uniprot.org/annotation/VAR_011895|||http://purl.uniprot.org/annotation/VAR_015262|||http://purl.uniprot.org/annotation/VAR_015263|||http://purl.uniprot.org/annotation/VAR_015264|||http://purl.uniprot.org/annotation/VAR_015265|||http://purl.uniprot.org/annotation/VAR_015266|||http://purl.uniprot.org/annotation/VAR_015267|||http://purl.uniprot.org/annotation/VAR_015268|||http://purl.uniprot.org/annotation/VAR_015269|||http://purl.uniprot.org/annotation/VAR_015270|||http://purl.uniprot.org/annotation/VAR_015271|||http://purl.uniprot.org/annotation/VAR_015272|||http://purl.uniprot.org/annotation/VAR_015273|||http://purl.uniprot.org/annotation/VAR_015274|||http://purl.uniprot.org/annotation/VAR_015275|||http://purl.uniprot.org/annotation/VAR_015276|||http://purl.uniprot.org/annotation/VAR_015277|||http://purl.uniprot.org/annotation/VAR_015278|||http://purl.uniprot.org/annotation/VAR_015279|||http://purl.uniprot.org/annotation/VAR_019273|||http://purl.uniprot.org/annotation/VAR_019274|||http://purl.uniprot.org/annotation/VAR_019275|||http://purl.uniprot.org/annotation/VAR_019276|||http://purl.uniprot.org/annotation/VAR_029997|||http://purl.uniprot.org/annotation/VAR_029998|||http://purl.uniprot.org/annotation/VAR_029999
http://togogenome.org/gene/9606:SMIM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7WNH4|||http://purl.uniprot.org/uniprot/Q9BQ49                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Small integral membrane protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284047
http://togogenome.org/gene/9606:CACFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGQ2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium channel flower homolog|||Helical|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089671|||http://purl.uniprot.org/annotation/VAR_069103|||http://purl.uniprot.org/annotation/VSP_012997|||http://purl.uniprot.org/annotation/VSP_042522
http://togogenome.org/gene/9606:GRAMD1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUR5|||http://purl.uniprot.org/uniprot/Q8IYS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRAM|||Helical|||In isoform 2.|||Polar residues|||Protein Aster-C|||VASt                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287451|||http://purl.uniprot.org/annotation/PRO_5010105250|||http://purl.uniprot.org/annotation/VAR_032302|||http://purl.uniprot.org/annotation/VSP_025477
http://togogenome.org/gene/9606:CENPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXU7|||http://purl.uniprot.org/uniprot/P49454                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||2 X 177 AA tandem repeats|||Basic and acidic residues|||Centromere protein Cenp-F N-terminal|||Centromere protein Cenp-F leucine-rich repeat-containing|||Centromere protein F|||Cysteine methyl ester|||Disordered|||Interaction with NDE1 and NDEL1|||Interaction with SNAP25 and required for localization to the cytoplasm|||Kinetochore protein Cenp-F/LEK1 Rb protein-binding|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine|||Sufficient for centromere localization|||Sufficient for nuclear localization|||Sufficient for self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089477|||http://purl.uniprot.org/annotation/PRO_0000396744|||http://purl.uniprot.org/annotation/VAR_014839|||http://purl.uniprot.org/annotation/VAR_034712|||http://purl.uniprot.org/annotation/VAR_034713|||http://purl.uniprot.org/annotation/VAR_034714|||http://purl.uniprot.org/annotation/VAR_034715|||http://purl.uniprot.org/annotation/VAR_034716|||http://purl.uniprot.org/annotation/VAR_034717|||http://purl.uniprot.org/annotation/VAR_034718|||http://purl.uniprot.org/annotation/VAR_034719|||http://purl.uniprot.org/annotation/VAR_034720|||http://purl.uniprot.org/annotation/VAR_034723|||http://purl.uniprot.org/annotation/VAR_055049|||http://purl.uniprot.org/annotation/VAR_055050|||http://purl.uniprot.org/annotation/VAR_055638
http://togogenome.org/gene/9606:SLC4A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY07                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Electrogenic sodium bicarbonate cotransporter 4|||Extracellular|||Helical|||In isoform 2 and isoform 6.|||In isoform 3, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328920|||http://purl.uniprot.org/annotation/VAR_048350|||http://purl.uniprot.org/annotation/VAR_061032|||http://purl.uniprot.org/annotation/VSP_052770|||http://purl.uniprot.org/annotation/VSP_052771|||http://purl.uniprot.org/annotation/VSP_052772|||http://purl.uniprot.org/annotation/VSP_052773|||http://purl.uniprot.org/annotation/VSP_052774|||http://purl.uniprot.org/annotation/VSP_052775|||http://purl.uniprot.org/annotation/VSP_052776|||http://purl.uniprot.org/annotation/VSP_052777|||http://purl.uniprot.org/annotation/VSP_052778|||http://purl.uniprot.org/annotation/VSP_052779|||http://purl.uniprot.org/annotation/VSP_052780|||http://purl.uniprot.org/annotation/VSP_052781
http://togogenome.org/gene/9606:CEP97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGU8|||http://purl.uniprot.org/uniprot/E9PG22|||http://purl.uniprot.org/uniprot/Q8IW35                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CCP110-binding|||Centrosomal protein of 97 kDa|||Disordered|||IQ|||In isoform 2.|||Interaction with MPHOSPH9|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263705|||http://purl.uniprot.org/annotation/VSP_031155
http://togogenome.org/gene/9606:KIAA1217                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZM29|||http://purl.uniprot.org/uniprot/Q5T5P2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin interacting protein 3-like C-terminal|||Basic and acidic residues|||Disordered|||Found in a patient with Klippel-Feil syndrome; unknown pathological significance.|||In isoform 10.|||In isoform 2, isoform 4 and isoform 9.|||In isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 10.|||In isoform 3, isoform 4, isoform 6 and isoform 7.|||In isoform 5 and isoform 7.|||In isoform 6 and isoform 10.|||In isoform 9.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Sickle tail protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287897|||http://purl.uniprot.org/annotation/VAR_051358|||http://purl.uniprot.org/annotation/VAR_051359|||http://purl.uniprot.org/annotation/VAR_051360|||http://purl.uniprot.org/annotation/VAR_085329|||http://purl.uniprot.org/annotation/VSP_030353|||http://purl.uniprot.org/annotation/VSP_052427|||http://purl.uniprot.org/annotation/VSP_052428|||http://purl.uniprot.org/annotation/VSP_052429|||http://purl.uniprot.org/annotation/VSP_052430|||http://purl.uniprot.org/annotation/VSP_052431|||http://purl.uniprot.org/annotation/VSP_052432|||http://purl.uniprot.org/annotation/VSP_054107|||http://purl.uniprot.org/annotation/VSP_054874
http://togogenome.org/gene/9606:ULBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZM4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||MHC class I alpha-1 like|||MHC class I alpha-2 like|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UL16-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019019|||http://purl.uniprot.org/annotation/PRO_0000019020
http://togogenome.org/gene/9606:RAD54L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV54|||http://purl.uniprot.org/uniprot/Q9Y4B4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ARIP4|||Helicase ATP-binding|||Helicase C-terminal|||LXXLL motif 1|||LXXLL motif 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315781|||http://purl.uniprot.org/annotation/VAR_038302
http://togogenome.org/gene/9606:CXXC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J9JIF5                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  CXXC-type|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:IFT80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2H3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In SRTD2.|||In isoform 2.|||In isoform IFT80-L.|||Intraflagellar transport protein 80 homolog|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051042|||http://purl.uniprot.org/annotation/VAR_035006|||http://purl.uniprot.org/annotation/VAR_035007|||http://purl.uniprot.org/annotation/VAR_035008|||http://purl.uniprot.org/annotation/VAR_035009|||http://purl.uniprot.org/annotation/VSP_045456|||http://purl.uniprot.org/annotation/VSP_057524
http://togogenome.org/gene/9606:SENP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9F5|||http://purl.uniprot.org/uniprot/Q96HI0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Disordered|||In isoform 2.|||Protease|||Sentrin-specific protease 5|||Ubiquitin-like protease family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101723|||http://purl.uniprot.org/annotation/VAR_057045|||http://purl.uniprot.org/annotation/VAR_061732|||http://purl.uniprot.org/annotation/VSP_056415
http://togogenome.org/gene/9606:TBC1D3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300264
http://togogenome.org/gene/9606:RBPJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06330                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-binding|||Disordered|||IPT/TIG|||In AOS3; shows decreased binding to the HES1 promoter compared to wild-type.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform APCR-1.|||In isoform APCR-3.|||N6-acetyllysine|||Recombining binding protein suppressor of hairless                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208567|||http://purl.uniprot.org/annotation/VAR_028994|||http://purl.uniprot.org/annotation/VAR_028995|||http://purl.uniprot.org/annotation/VAR_028996|||http://purl.uniprot.org/annotation/VAR_028997|||http://purl.uniprot.org/annotation/VAR_028998|||http://purl.uniprot.org/annotation/VAR_057244|||http://purl.uniprot.org/annotation/VAR_068929|||http://purl.uniprot.org/annotation/VAR_068930|||http://purl.uniprot.org/annotation/VSP_002717|||http://purl.uniprot.org/annotation/VSP_002718|||http://purl.uniprot.org/annotation/VSP_002719|||http://purl.uniprot.org/annotation/VSP_021572|||http://purl.uniprot.org/annotation/VSP_021573|||http://purl.uniprot.org/annotation/VSP_021574|||http://purl.uniprot.org/annotation/VSP_042637
http://togogenome.org/gene/9606:ADA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0I3|||http://purl.uniprot.org/uniprot/B4E3Q4|||http://purl.uniprot.org/uniprot/Q9NZK5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes secretion.|||Adenosine deaminase|||Adenosine deaminase 2|||Adenosine/AMP deaminase N-terminal|||Dimerization|||In SNDNS.|||In VAIHS.|||In VAIHS; there is a decreased expression of the mutant protein compared to wild-type.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PRB domain|||Proton acceptor|||Proton donor|||Reduces dimerization and enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006725|||http://purl.uniprot.org/annotation/VAR_029802|||http://purl.uniprot.org/annotation/VAR_071137|||http://purl.uniprot.org/annotation/VAR_071138|||http://purl.uniprot.org/annotation/VAR_071139|||http://purl.uniprot.org/annotation/VAR_071140|||http://purl.uniprot.org/annotation/VAR_071141|||http://purl.uniprot.org/annotation/VAR_071142|||http://purl.uniprot.org/annotation/VAR_071143|||http://purl.uniprot.org/annotation/VAR_071144|||http://purl.uniprot.org/annotation/VAR_072562|||http://purl.uniprot.org/annotation/VAR_072563|||http://purl.uniprot.org/annotation/VSP_041509|||http://purl.uniprot.org/annotation/VSP_041510
http://togogenome.org/gene/9606:HSFY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Heat shock transcription factor, Y-linked|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124573|||http://purl.uniprot.org/annotation/VSP_009179|||http://purl.uniprot.org/annotation/VSP_009180|||http://purl.uniprot.org/annotation/VSP_009181|||http://purl.uniprot.org/annotation/VSP_009182
http://togogenome.org/gene/9606:DNAJC25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1X3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 25|||Helical|||In isoform 2.|||In isoform 3.|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348569|||http://purl.uniprot.org/annotation/VSP_035180|||http://purl.uniprot.org/annotation/VSP_035181|||http://purl.uniprot.org/annotation/VSP_035182
http://togogenome.org/gene/9606:PKD1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z443                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Channel pore-region|||Cytoplasmic|||Extracellular|||GPS|||Helical|||N-linked (GlcNAc...) asparagine|||PLAT|||Polycystin-1-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322578|||http://purl.uniprot.org/annotation/VAR_039453|||http://purl.uniprot.org/annotation/VAR_039454|||http://purl.uniprot.org/annotation/VAR_039455|||http://purl.uniprot.org/annotation/VAR_039456|||http://purl.uniprot.org/annotation/VAR_039457|||http://purl.uniprot.org/annotation/VAR_039458|||http://purl.uniprot.org/annotation/VAR_039459|||http://purl.uniprot.org/annotation/VAR_039460|||http://purl.uniprot.org/annotation/VAR_039461|||http://purl.uniprot.org/annotation/VAR_039462
http://togogenome.org/gene/9606:GLI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YGX0|||http://purl.uniprot.org/uniprot/P10071                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In GCPS.|||In GCPS; the patient was originally classifed as being affected by acrocallosal syndrome due to the absence of corpus callosum.|||In PAPA1 and PAPB.|||In a colorectal cancer sample; somatic mutation.|||Loss of phosphorylation and proteolytic processing.|||Loss of proteolytic processing.|||Mediates interaction with DZIP1|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Transcriptional activator GLI3|||Transcriptional repressor GLI3R                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047202|||http://purl.uniprot.org/annotation/PRO_0000406137|||http://purl.uniprot.org/annotation/VAR_009876|||http://purl.uniprot.org/annotation/VAR_010052|||http://purl.uniprot.org/annotation/VAR_010053|||http://purl.uniprot.org/annotation/VAR_010054|||http://purl.uniprot.org/annotation/VAR_010055|||http://purl.uniprot.org/annotation/VAR_010056|||http://purl.uniprot.org/annotation/VAR_010057|||http://purl.uniprot.org/annotation/VAR_021481|||http://purl.uniprot.org/annotation/VAR_021482|||http://purl.uniprot.org/annotation/VAR_028276|||http://purl.uniprot.org/annotation/VAR_028278|||http://purl.uniprot.org/annotation/VAR_034865|||http://purl.uniprot.org/annotation/VAR_035560|||http://purl.uniprot.org/annotation/VAR_035561
http://togogenome.org/gene/9606:COX6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R9B7|||http://purl.uniprot.org/uniprot/P09669                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 6C|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006131
http://togogenome.org/gene/9606:NLRP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59044                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished formation of an inflammasome filament.|||Basic and acidic residues|||Decreased formation of an inflammasome filament.|||Decreased formation of an inflammasome filament. Abolished ability to promote PYCARD/ASC polymerization.|||Decreased formation of an inflammasome filament. Decreased ability to promote PYCARD/ASC polymerization.|||Disordered|||Does not affect formation of an inflammasome filament.|||Does not prevent formation of an inflammasome filament.|||Impaired formation of liquid-liquid phase separation (LLPS).|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||NACHT|||NACHT, LRR and PYD domains-containing protein 6|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080892|||http://purl.uniprot.org/annotation/VAR_058968|||http://purl.uniprot.org/annotation/VAR_058969|||http://purl.uniprot.org/annotation/VAR_079497|||http://purl.uniprot.org/annotation/VSP_054400
http://togogenome.org/gene/9606:BCL11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZV9|||http://purl.uniprot.org/uniprot/D9YZW0|||http://purl.uniprot.org/uniprot/Q9H165                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||B-cell lymphoma/leukemia 11A|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3, does not affect the interaction of isoform 2 with TBR1.|||In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.|||In IDPFH, de novo mutation, loss of function transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3, does not affect the interaction of isoform 2 with TBR1.|||In IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3; does not affect the interaction of isoform 2 with TBR1.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for nuclear body formation and for SUMO1 recruitment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047102|||http://purl.uniprot.org/annotation/VAR_035553|||http://purl.uniprot.org/annotation/VAR_076921|||http://purl.uniprot.org/annotation/VAR_076922|||http://purl.uniprot.org/annotation/VAR_076923|||http://purl.uniprot.org/annotation/VAR_082936|||http://purl.uniprot.org/annotation/VAR_082937|||http://purl.uniprot.org/annotation/VAR_082938|||http://purl.uniprot.org/annotation/VAR_082939|||http://purl.uniprot.org/annotation/VAR_082940|||http://purl.uniprot.org/annotation/VAR_082941|||http://purl.uniprot.org/annotation/VSP_009548|||http://purl.uniprot.org/annotation/VSP_009550|||http://purl.uniprot.org/annotation/VSP_009552|||http://purl.uniprot.org/annotation/VSP_009554|||http://purl.uniprot.org/annotation/VSP_009555|||http://purl.uniprot.org/annotation/VSP_058656|||http://purl.uniprot.org/annotation/VSP_058657
http://togogenome.org/gene/9606:OXLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L208|||http://purl.uniprot.org/uniprot/Q5BKU9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Oxidoreductase-like|||Oxidoreductase-like domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314123
http://togogenome.org/gene/9606:ZFP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BV40|||http://purl.uniprot.org/uniprot/J3KNQ1|||http://purl.uniprot.org/uniprot/Q6P2D0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Does not affect nuclear localization pattern|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Required for correct nuclear localization and exclusion from the nucleoli|||Zinc finger protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047279|||http://purl.uniprot.org/annotation/VSP_012682
http://togogenome.org/gene/9606:SPSB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99619                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||Disordered|||Enhances interaction with PAWR.|||In isoform 2.|||Polar residues|||SOCS box|||SPRY domain-containing SOCS box protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238474|||http://purl.uniprot.org/annotation/VSP_057167
http://togogenome.org/gene/9606:PNPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCS8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In COXPD13; the mutation alters multimerization of the protein.|||In DFNB70; results in a hypofunctional protein leading to disturbed enzyme trimerization and impaired mitochondrial RNA import.|||Inhibits poly(A) polymerase and RNA degradation activities. Does not inhibit the import or stabilization of RNase PRNA into the mitochondrial matrix. Does not inhibit homotrimerization activity.|||Inhibits poly(A) polymerase and RNA degradation activities. Inhibits the import or stabilization of RNase PRNA into the mitochondrial matrix. Does not inhibit homotrimerization activity.|||KH|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Polyribonucleotide nucleotidyltransferase 1, mitochondrial|||S1 motif|||Stimulates in vitro poly(A) polymerase activity. Inhibits RNA degradation activity. Does not inhibit the import or stabilization of RNase PRNA into the mitochondrial matrix. Does not inhibit homotrimerization activity.|||Stimulates in vitro poly(A) polymerase activity. Inhibits RNA degradation activity. Inhibits the import or stabilization of RNase PRNA into the mitochondrial matrix. Does not inhibit homotrimerization activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024751|||http://purl.uniprot.org/annotation/VAR_027787|||http://purl.uniprot.org/annotation/VAR_027788|||http://purl.uniprot.org/annotation/VAR_050610|||http://purl.uniprot.org/annotation/VAR_069248|||http://purl.uniprot.org/annotation/VAR_069249
http://togogenome.org/gene/9606:SLC32A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H598                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3'-nitrotyrosine|||Cytoplasmic|||Disordered|||Helical|||Lumenal, vesicle|||Vesicular inhibitory amino acid transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093820|||http://purl.uniprot.org/annotation/VAR_048121
http://togogenome.org/gene/9606:USP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMW8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes deubiquitinating activity.|||Basic and acidic residues|||Disordered|||In PTORCH2.|||In isoform 2.|||Mediates interaction with IFNAR2|||Mediates interaction with STAT2|||Mediates interaction with STAT2 and necessary for the negative regulation of the type I IFN signaling pathway|||Nucleophile|||Proton acceptor|||USP|||Ubl carboxyl-terminal hydrolase 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080644|||http://purl.uniprot.org/annotation/VAR_024589|||http://purl.uniprot.org/annotation/VAR_078772|||http://purl.uniprot.org/annotation/VSP_055236
http://togogenome.org/gene/9606:BCAS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDM0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form BCAS4-BCAS3|||Breast carcinoma-amplified sequence 4|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064865|||http://purl.uniprot.org/annotation/VAR_016031|||http://purl.uniprot.org/annotation/VAR_059590|||http://purl.uniprot.org/annotation/VSP_007854|||http://purl.uniprot.org/annotation/VSP_007855|||http://purl.uniprot.org/annotation/VSP_015289|||http://purl.uniprot.org/annotation/VSP_015290
http://togogenome.org/gene/9606:LAYN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDS5|||http://purl.uniprot.org/uniprot/Q6UX15                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||2 X 4 AA repeats of N-X-I-Y|||2-1|||2-2|||3 X 5 AA repeats of E-S-G-X-V|||C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Interaction with NF2|||Interaction with TLN1|||Layilin|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262508|||http://purl.uniprot.org/annotation/VAR_029496|||http://purl.uniprot.org/annotation/VSP_021781|||http://purl.uniprot.org/annotation/VSP_054660|||http://purl.uniprot.org/annotation/VSP_054661
http://togogenome.org/gene/9606:ANKDD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495B1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and death domain-containing protein 1A|||Death|||In isoform 1.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287882|||http://purl.uniprot.org/annotation/VAR_032358|||http://purl.uniprot.org/annotation/VSP_038675|||http://purl.uniprot.org/annotation/VSP_038676|||http://purl.uniprot.org/annotation/VSP_038677|||http://purl.uniprot.org/annotation/VSP_038678
http://togogenome.org/gene/9606:RBM15B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with Epstein-Barr virus BMLF1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||Putative RNA-binding protein 15B|||RRM 1|||RRM 2|||RRM 3|||SPOC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081778|||http://purl.uniprot.org/annotation/VSP_053878
http://togogenome.org/gene/9606:CDC14B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60729                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A|||B|||Disordered|||Dual specificity protein phosphatase CDC14B|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Linker|||Nucleolar localization signal|||Phosphocysteine intermediate|||Polar residues|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094878|||http://purl.uniprot.org/annotation/VAR_019959|||http://purl.uniprot.org/annotation/VAR_019960|||http://purl.uniprot.org/annotation/VSP_012038|||http://purl.uniprot.org/annotation/VSP_012039|||http://purl.uniprot.org/annotation/VSP_030720|||http://purl.uniprot.org/annotation/VSP_043576
http://togogenome.org/gene/9606:THOC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13769                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs mRNA binding, enhances CXCL12-dependent cell migration.|||In a breast cancer sample; somatic mutation.|||Interaction with CSF1R|||Interaction with THOC7|||N-acetylserine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by SRC|||Removed|||THO complex subunit 5 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079577|||http://purl.uniprot.org/annotation/VAR_021410|||http://purl.uniprot.org/annotation/VAR_035692|||http://purl.uniprot.org/annotation/VAR_035693|||http://purl.uniprot.org/annotation/VAR_037134|||http://purl.uniprot.org/annotation/VAR_037135
http://togogenome.org/gene/9606:DNAJB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59910                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DnaJ homolog subfamily B member 13|||In CILD34; loss of expression in patient cells; increased proteasome-mediated degradation; no effect on homodimerization.|||In isoform 2.|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071039|||http://purl.uniprot.org/annotation/VAR_077053|||http://purl.uniprot.org/annotation/VSP_008519|||http://purl.uniprot.org/annotation/VSP_008520
http://togogenome.org/gene/9606:BPGM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R782|||http://purl.uniprot.org/uniprot/P07738                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Bisphosphoglycerate mutase|||In ECYT8.|||In ECYT8; mutation identified at protein level; marked decrease in synthase and mutase activities; no effect on phosphatase activity.|||N-acetylserine|||N-linked (Glc) (glycation) lysine|||N-linked (Glc) (glycation) lysine; in vitro|||Not glycated|||Phosphothreonine|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179834|||http://purl.uniprot.org/annotation/VAR_065367|||http://purl.uniprot.org/annotation/VAR_065368
http://togogenome.org/gene/9606:PID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2X4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In variant with duplicated exon 2.|||PID|||PTB-containing, cubilin and LRP1-interacting protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274900|||http://purl.uniprot.org/annotation/VAR_030361|||http://purl.uniprot.org/annotation/VSP_022909|||http://purl.uniprot.org/annotation/VSP_022910|||http://purl.uniprot.org/annotation/VSP_022911|||http://purl.uniprot.org/annotation/VSP_022912
http://togogenome.org/gene/9606:MED27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2C8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NEDSCAC; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Mediator of RNA polymerase II transcription subunit 27|||N6-methyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079361|||http://purl.uniprot.org/annotation/VAR_085606|||http://purl.uniprot.org/annotation/VAR_085607|||http://purl.uniprot.org/annotation/VAR_085608|||http://purl.uniprot.org/annotation/VAR_085609|||http://purl.uniprot.org/annotation/VAR_085610|||http://purl.uniprot.org/annotation/VAR_085611|||http://purl.uniprot.org/annotation/VAR_085612|||http://purl.uniprot.org/annotation/VSP_051869|||http://purl.uniprot.org/annotation/VSP_055411|||http://purl.uniprot.org/annotation/VSP_055412
http://togogenome.org/gene/9606:DNAJC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVH1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 11|||In isoform 2.|||In isoform 3.|||J|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247157|||http://purl.uniprot.org/annotation/VAR_027078|||http://purl.uniprot.org/annotation/VAR_027079|||http://purl.uniprot.org/annotation/VAR_055703|||http://purl.uniprot.org/annotation/VSP_019932|||http://purl.uniprot.org/annotation/VSP_019933
http://togogenome.org/gene/9606:MLXIPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carbohydrate-responsive element-binding protein|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||Leucine-zipper|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Polar residues|||Pro residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127504|||http://purl.uniprot.org/annotation/VAR_049556|||http://purl.uniprot.org/annotation/VAR_049557|||http://purl.uniprot.org/annotation/VSP_002167|||http://purl.uniprot.org/annotation/VSP_002168|||http://purl.uniprot.org/annotation/VSP_002169|||http://purl.uniprot.org/annotation/VSP_002170|||http://purl.uniprot.org/annotation/VSP_002171|||http://purl.uniprot.org/annotation/VSP_002172|||http://purl.uniprot.org/annotation/VSP_002173
http://togogenome.org/gene/9606:STMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E0CX11                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Short transmembrane mitochondrial protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413534
http://togogenome.org/gene/9606:GRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15835                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||C-terminal|||Cysteine methyl ester|||Disordered|||In CSNBO2.|||Interaction with RCVRN|||Loss of autophosphorylation and RHO phosphorylation.|||N-terminal|||Not phosphorylated by PKA.|||Phosphoserine|||Phosphoserine; by PKA and autocatalysis|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RGS|||Removed in mature form|||Rhodopsin kinase GRK1|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024375|||http://purl.uniprot.org/annotation/PRO_0000024376|||http://purl.uniprot.org/annotation/VAR_006215|||http://purl.uniprot.org/annotation/VAR_008283|||http://purl.uniprot.org/annotation/VAR_008284|||http://purl.uniprot.org/annotation/VAR_008285|||http://purl.uniprot.org/annotation/VAR_008286|||http://purl.uniprot.org/annotation/VAR_008287|||http://purl.uniprot.org/annotation/VAR_008288|||http://purl.uniprot.org/annotation/VAR_008289|||http://purl.uniprot.org/annotation/VAR_037904
http://togogenome.org/gene/9606:FAXDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IV6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Fatty acid hydroxylase|||Fatty acid hydroxylase domain-containing protein 2|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249848|||http://purl.uniprot.org/annotation/VAR_048900|||http://purl.uniprot.org/annotation/VSP_056995
http://togogenome.org/gene/9606:TTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9KL36|||http://purl.uniprot.org/uniprot/P02766                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  4-carboxyglutamate; in a patient with Moyamoya disease|||In AMYL-TTR.|||In AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy.|||In AMYL-TTR; amyloid cardiomyopathy.|||In AMYL-TTR; amyloid polyneuropathy and cardiomyopathy.|||In AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome.|||In AMYL-TTR; amyloid polyneuropathy.|||In AMYL-TTR; amyloid polyneuropathy; almost no RBP binding.|||In AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation.|||In AMYL-TTR; early-onset amyloid polyneuropathy.|||In AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome.|||In AMYL-TTR; leptomeningeal amyloidosis; leads to unfolding and exposure of N-118 to glycosylation by STT3B and subsequent degradation by the ERAD pathway.|||In AMYL-TTR; leptomeningeal amyloidosis; vitreous amyloid in some patients.|||In AMYL-TTR; vitrous amyloid.|||In CTS1; amyloid deposit on carpal tunnel; patients show no other abnormalities.|||In Chicago variant.|||In DTTRH; increased affinity for thyroxine.|||In a patient with amyloidosis.|||Loss of tetramerization; when associated with M-107.|||Loss of tetramerization; when associated with M-130.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Requires 2 nucleotide substitutions.|||Sulfocysteine|||Transthyretin|||Transthyretin/hydroxyisourate hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035755|||http://purl.uniprot.org/annotation/PRO_5014205518|||http://purl.uniprot.org/annotation/VAR_007546|||http://purl.uniprot.org/annotation/VAR_007547|||http://purl.uniprot.org/annotation/VAR_007548|||http://purl.uniprot.org/annotation/VAR_007549|||http://purl.uniprot.org/annotation/VAR_007550|||http://purl.uniprot.org/annotation/VAR_007551|||http://purl.uniprot.org/annotation/VAR_007552|||http://purl.uniprot.org/annotation/VAR_007553|||http://purl.uniprot.org/annotation/VAR_007554|||http://purl.uniprot.org/annotation/VAR_007555|||http://purl.uniprot.org/annotation/VAR_007556|||http://purl.uniprot.org/annotation/VAR_007557|||http://purl.uniprot.org/annotation/VAR_007558|||http://purl.uniprot.org/annotation/VAR_007559|||http://purl.uniprot.org/annotation/VAR_007560|||http://purl.uniprot.org/annotation/VAR_007561|||http://purl.uniprot.org/annotation/VAR_007562|||http://purl.uniprot.org/annotation/VAR_007563|||http://purl.uniprot.org/annotation/VAR_007564|||http://purl.uniprot.org/annotation/VAR_007565|||http://purl.uniprot.org/annotation/VAR_007566|||http://purl.uniprot.org/annotation/VAR_007567|||http://purl.uniprot.org/annotation/VAR_007568|||http://purl.uniprot.org/annotation/VAR_007569|||http://purl.uniprot.org/annotation/VAR_007570|||http://purl.uniprot.org/annotation/VAR_007571|||http://purl.uniprot.org/annotation/VAR_007572|||http://purl.uniprot.org/annotation/VAR_007573|||http://purl.uniprot.org/annotation/VAR_007574|||http://purl.uniprot.org/annotation/VAR_007575|||http://purl.uniprot.org/annotation/VAR_007576|||http://purl.uniprot.org/annotation/VAR_007577|||http://purl.uniprot.org/annotation/VAR_007578|||http://purl.uniprot.org/annotation/VAR_007579|||http://purl.uniprot.org/annotation/VAR_007580|||http://purl.uniprot.org/annotation/VAR_007581|||http://purl.uniprot.org/annotation/VAR_007582|||http://purl.uniprot.org/annotation/VAR_007583|||http://purl.uniprot.org/annotation/VAR_007584|||http://purl.uniprot.org/annotation/VAR_007585|||http://purl.uniprot.org/annotation/VAR_007586|||http://purl.uniprot.org/annotation/VAR_007587|||http://purl.uniprot.org/annotation/VAR_007588|||http://purl.uniprot.org/annotation/VAR_007589|||http://purl.uniprot.org/annotation/VAR_007590|||http://purl.uniprot.org/annotation/VAR_007591|||http://purl.uniprot.org/annotation/VAR_007592|||http://purl.uniprot.org/annotation/VAR_007593|||http://purl.uniprot.org/annotation/VAR_007594|||http://purl.uniprot.org/annotation/VAR_007595|||http://purl.uniprot.org/annotation/VAR_007596|||http://purl.uniprot.org/annotation/VAR_007597|||http://purl.uniprot.org/annotation/VAR_007598|||http://purl.uniprot.org/annotation/VAR_007599|||http://purl.uniprot.org/annotation/VAR_007600|||http://purl.uniprot.org/annotation/VAR_010658|||http://purl.uniprot.org/annotation/VAR_010659|||http://purl.uniprot.org/annotation/VAR_038959|||http://purl.uniprot.org/annotation/VAR_038960|||http://purl.uniprot.org/annotation/VAR_038961|||http://purl.uniprot.org/annotation/VAR_038962|||http://purl.uniprot.org/annotation/VAR_038963|||http://purl.uniprot.org/annotation/VAR_038964|||http://purl.uniprot.org/annotation/VAR_038965|||http://purl.uniprot.org/annotation/VAR_038966|||http://purl.uniprot.org/annotation/VAR_038967|||http://purl.uniprot.org/annotation/VAR_038968|||http://purl.uniprot.org/annotation/VAR_038969|||http://purl.uniprot.org/annotation/VAR_038970|||http://purl.uniprot.org/annotation/VAR_038971|||http://purl.uniprot.org/annotation/VAR_038972|||http://purl.uniprot.org/annotation/VAR_038973|||http://purl.uniprot.org/annotation/VAR_038974|||http://purl.uniprot.org/annotation/VAR_038975|||http://purl.uniprot.org/annotation/VAR_038976|||http://purl.uniprot.org/annotation/VAR_038977|||http://purl.uniprot.org/annotation/VAR_038978|||http://purl.uniprot.org/annotation/VAR_038979|||http://purl.uniprot.org/annotation/VAR_038980|||http://purl.uniprot.org/annotation/VAR_038981|||http://purl.uniprot.org/annotation/VAR_038982|||http://purl.uniprot.org/annotation/VAR_038983|||http://purl.uniprot.org/annotation/VAR_038984|||http://purl.uniprot.org/annotation/VAR_038985|||http://purl.uniprot.org/annotation/VAR_038986|||http://purl.uniprot.org/annotation/VAR_038987|||http://purl.uniprot.org/annotation/VAR_038988
http://togogenome.org/gene/9606:CHIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13231                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chitin-binding type-2|||Chitotriosidase-1|||Common variant detected in patients with Gaucher disease type 1 as well as healthy individuals; slightly reduced activity towards 4-methylumbelliferyl-chitotrioside but no effect on activity towards 4-methylumbelliferyl-deoxychitobioside.|||Disordered|||GH18|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine; in variant S-102|||Proton donor|||Rare variant detected in patients with Gaucher disease type 1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011941|||http://purl.uniprot.org/annotation/VAR_022138|||http://purl.uniprot.org/annotation/VAR_024458|||http://purl.uniprot.org/annotation/VAR_049190|||http://purl.uniprot.org/annotation/VAR_049191|||http://purl.uniprot.org/annotation/VAR_065914|||http://purl.uniprot.org/annotation/VSP_008631|||http://purl.uniprot.org/annotation/VSP_008632|||http://purl.uniprot.org/annotation/VSP_008633|||http://purl.uniprot.org/annotation/VSP_044816
http://togogenome.org/gene/9606:SIRPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H106                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Signal-regulatory protein delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014919|||http://purl.uniprot.org/annotation/VAR_056078
http://togogenome.org/gene/9606:AP1G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE7|||http://purl.uniprot.org/uniprot/O43747|||http://purl.uniprot.org/uniprot/Q8IY97                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP-1 complex subunit gamma-1|||Disordered|||GAE|||In USRISD; does not fully rescue morphological defects in a zebrafish animal model.|||In USRISD; does not rescue morphological defects in a zebrafish animal model.|||In USRISR; does not fully rescue morphological defects in a zebrafish animal model; affects trafficking of transferrin from early to recycling endosomes; no effect on subcellular location in the perinuclear region; does not affect interaction with AP-1 complex subunits AP1B1, AP1M1 and AP1S1.|||In USRISR; does not fully rescue morphological defects in a zebrafish animal model; affects trafficking of transferrin from recycling endosomes to plasma membrane; no effect on subcellular location in the perinuclear region; does not affect interaction with AP-1 complex subunits AP1B1, AP1M1 and AP1S1.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193758|||http://purl.uniprot.org/annotation/VAR_013572|||http://purl.uniprot.org/annotation/VAR_048194|||http://purl.uniprot.org/annotation/VAR_086350|||http://purl.uniprot.org/annotation/VAR_086351|||http://purl.uniprot.org/annotation/VAR_086352|||http://purl.uniprot.org/annotation/VAR_086353|||http://purl.uniprot.org/annotation/VAR_086354|||http://purl.uniprot.org/annotation/VAR_086355|||http://purl.uniprot.org/annotation/VSP_040133
http://togogenome.org/gene/9606:SYTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||RabBD|||Synaptotagmin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190211|||http://purl.uniprot.org/annotation/VSP_007883
http://togogenome.org/gene/9606:IGSF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSI5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||Immunoglobulin superfamily member 5|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316295|||http://purl.uniprot.org/annotation/VAR_038381|||http://purl.uniprot.org/annotation/VAR_038382|||http://purl.uniprot.org/annotation/VAR_038383|||http://purl.uniprot.org/annotation/VAR_038384
http://togogenome.org/gene/9606:EDN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14138|||http://purl.uniprot.org/uniprot/Q4FAT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by KEL|||Disordered|||Endothelin-3|||Endothelin-like|||Endothelin-like toxin|||In HSCR4; risk factor associated with disease susceptibility.|||In WS4B.|||In isoform 3.|||In isoform Short.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008111|||http://purl.uniprot.org/annotation/PRO_0000008112|||http://purl.uniprot.org/annotation/PRO_0000008113|||http://purl.uniprot.org/annotation/PRO_5014104936|||http://purl.uniprot.org/annotation/VAR_002353|||http://purl.uniprot.org/annotation/VAR_009078|||http://purl.uniprot.org/annotation/VAR_009079|||http://purl.uniprot.org/annotation/VAR_015238|||http://purl.uniprot.org/annotation/VSP_001445|||http://purl.uniprot.org/annotation/VSP_043139
http://togogenome.org/gene/9606:HAO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYQ3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  2-Hydroxyacid oxidase 2|||FMN hydroxy acid dehydrogenase|||In isoform 2.|||Microbody targeting signal|||Phosphothreonine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206320|||http://purl.uniprot.org/annotation/VAR_049087|||http://purl.uniprot.org/annotation/VAR_049088|||http://purl.uniprot.org/annotation/VSP_055095
http://togogenome.org/gene/9606:SMC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY18                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Flexible hinge|||In ATELS2; loss-of-function variant; unable to rescue microcephaly and aberrant craniofacial patterning in zebrafish lacking SMC5; does not relocalize efficiently to sites of laser irradiation-induced DNA damage; loss of interaction with SLF2 and NSMCE2; severely decreased interaction with SMC6.|||In ATELS2; loss-of-function variant; unable to rescue microcephaly and aberrant craniofacial patterning in zebrafish lacking SMC5; does not relocalize efficiently to sites of laser irradiation-induced DNA damage; no effect on interaction with SLF2, SMC6 and NSMCE2.|||In ATELS2; loss-of-function variant; unable to rescue microcephaly and aberrant craniofacial patterning in zebrafish lacking SMC5; loss of interaction with SLF2, SMC6 and NSMCE2.|||Phosphoserine|||Polar residues|||Structural maintenance of chromosomes protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270951|||http://purl.uniprot.org/annotation/VAR_029824|||http://purl.uniprot.org/annotation/VAR_029825|||http://purl.uniprot.org/annotation/VAR_061869|||http://purl.uniprot.org/annotation/VAR_087971|||http://purl.uniprot.org/annotation/VAR_087972|||http://purl.uniprot.org/annotation/VAR_087973
http://togogenome.org/gene/9606:RTEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ71|||http://purl.uniprot.org/uniprot/R4IXY3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes ATPase activity.|||DEAH box|||Disordered|||Helicase ATP-binding|||In DKCA4.|||In DKCB5, abolishes activity.|||In DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome.|||In DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome.|||In PFBMFT3.|||In isoform 1.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Nuclear localization signal|||PIP-box|||Polar residues|||Regulator of telomere elongation helicase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101985|||http://purl.uniprot.org/annotation/VAR_054970|||http://purl.uniprot.org/annotation/VAR_054971|||http://purl.uniprot.org/annotation/VAR_069714|||http://purl.uniprot.org/annotation/VAR_069715|||http://purl.uniprot.org/annotation/VAR_069716|||http://purl.uniprot.org/annotation/VAR_069717|||http://purl.uniprot.org/annotation/VAR_069718|||http://purl.uniprot.org/annotation/VAR_069719|||http://purl.uniprot.org/annotation/VAR_069720|||http://purl.uniprot.org/annotation/VAR_069721|||http://purl.uniprot.org/annotation/VAR_069722|||http://purl.uniprot.org/annotation/VAR_069723|||http://purl.uniprot.org/annotation/VAR_069724|||http://purl.uniprot.org/annotation/VAR_069725|||http://purl.uniprot.org/annotation/VAR_069726|||http://purl.uniprot.org/annotation/VAR_069727|||http://purl.uniprot.org/annotation/VAR_069728|||http://purl.uniprot.org/annotation/VAR_069729|||http://purl.uniprot.org/annotation/VAR_069730|||http://purl.uniprot.org/annotation/VAR_073795|||http://purl.uniprot.org/annotation/VAR_073796|||http://purl.uniprot.org/annotation/VAR_073797|||http://purl.uniprot.org/annotation/VAR_082827|||http://purl.uniprot.org/annotation/VAR_082828|||http://purl.uniprot.org/annotation/VAR_082829|||http://purl.uniprot.org/annotation/VAR_082830|||http://purl.uniprot.org/annotation/VAR_082831|||http://purl.uniprot.org/annotation/VSP_007076|||http://purl.uniprot.org/annotation/VSP_007077|||http://purl.uniprot.org/annotation/VSP_017093|||http://purl.uniprot.org/annotation/VSP_017094|||http://purl.uniprot.org/annotation/VSP_036937|||http://purl.uniprot.org/annotation/VSP_036938|||http://purl.uniprot.org/annotation/VSP_036939|||http://purl.uniprot.org/annotation/VSP_036940
http://togogenome.org/gene/9606:YIF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGW1|||http://purl.uniprot.org/uniprot/A8K509|||http://purl.uniprot.org/uniprot/O95070                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||Phosphoserine|||Protein YIF1A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233275
http://togogenome.org/gene/9606:GALM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDW6|||http://purl.uniprot.org/uniprot/Q96C23                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased activity by 300-fold.|||Decreased activity by 5-fold.|||Galactose mutarotase|||In GALAC4; decreased protein stability.|||In GALAC4; loss of protein accumulation.|||In GALAC4; unknown pathological significance; decreased protein stability.|||Loss of activity.|||N-acetylalanine|||Phosphoserine|||Proton acceptor|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197433|||http://purl.uniprot.org/annotation/VAR_024451|||http://purl.uniprot.org/annotation/VAR_083547|||http://purl.uniprot.org/annotation/VAR_083548|||http://purl.uniprot.org/annotation/VAR_083549|||http://purl.uniprot.org/annotation/VAR_083550
http://togogenome.org/gene/9606:DCTN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5D4|||http://purl.uniprot.org/uniprot/Q9NSJ5|||http://purl.uniprot.org/uniprot/Q9UJW0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dynactin subunit 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114 and S-277.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-114 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-111; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-76; S-79; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-73; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-70; S-76; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-54, S-73; S-76; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-51; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-33; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-30; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280.|||Loss of ATP7B-binding; when associated with S-33; S-51; S-54; S-70, S-73; S-76; S-79; S-111; S-114; S-277 and S-280.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079823|||http://purl.uniprot.org/annotation/VAR_024336|||http://purl.uniprot.org/annotation/VAR_024337|||http://purl.uniprot.org/annotation/VAR_033847|||http://purl.uniprot.org/annotation/VAR_054037|||http://purl.uniprot.org/annotation/VSP_041306|||http://purl.uniprot.org/annotation/VSP_041307
http://togogenome.org/gene/9606:OR2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW45|||http://purl.uniprot.org/uniprot/Q6IF42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150453|||http://purl.uniprot.org/annotation/VAR_053128|||http://purl.uniprot.org/annotation/VAR_059982|||http://purl.uniprot.org/annotation/VAR_059983
http://togogenome.org/gene/9606:FIGNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNH6|||http://purl.uniprot.org/uniprot/Q6PIW4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Basic and acidic residues|||Disordered|||Fidgetin-like protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Inhibits HR-mediated DNA repair.|||N6-acetyllysine|||Necessary and sufficient for interaction with RAD51|||Phosphoserine|||Reduces interaction with RAD51 and inhibits HR-mediated DNA repair. Strongly reduce, but does abolish, interaction with RAD51; when associated with E-340.|||Reduces weakly interaction with RAD51. Strongly reduce, but does abolish, interaction with RAD51; when associated with E-295.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302723|||http://purl.uniprot.org/annotation/VAR_034941|||http://purl.uniprot.org/annotation/VAR_034942|||http://purl.uniprot.org/annotation/VSP_027937
http://togogenome.org/gene/9606:ZUP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z644|||http://purl.uniprot.org/uniprot/Q96AP4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||In isoform 2.|||Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole|||Loss of catalytic activity.|||MIU|||N6-acetyllysine|||No effect.|||Nucleophile|||Proton acceptor|||Zinc finger-containing ubiquitin peptidase 1|||zUBD/ZHA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244336|||http://purl.uniprot.org/annotation/VAR_026889|||http://purl.uniprot.org/annotation/VSP_019533
http://togogenome.org/gene/9606:ENPP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWV6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased enzyme activity with sphingomyelin and para-nitrophenylphosphorylcholine.|||Decreased enzyme activity; when associated with E-271.|||Decreased enzyme activity; when associated with E-343.|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 7|||Extracellular|||Helical|||Loss of activity.|||Loss of enzyme activity with sphingomyelin.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Required for enzyme activity|||Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-146 and Q-168.|||Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267.|||Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267.|||Strongly reduces N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267.|||Strongly reduces activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036403|||http://purl.uniprot.org/annotation/VAR_021506
http://togogenome.org/gene/9606:CFAP69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8W1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 69|||Disordered|||In SPGF24.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320596|||http://purl.uniprot.org/annotation/VAR_039219|||http://purl.uniprot.org/annotation/VAR_039220|||http://purl.uniprot.org/annotation/VAR_039221|||http://purl.uniprot.org/annotation/VAR_039222|||http://purl.uniprot.org/annotation/VAR_039223|||http://purl.uniprot.org/annotation/VAR_081046|||http://purl.uniprot.org/annotation/VSP_031673|||http://purl.uniprot.org/annotation/VSP_031674|||http://purl.uniprot.org/annotation/VSP_031675|||http://purl.uniprot.org/annotation/VSP_031676|||http://purl.uniprot.org/annotation/VSP_036548
http://togogenome.org/gene/9606:UBAP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYY5|||http://purl.uniprot.org/uniprot/F8W726|||http://purl.uniprot.org/uniprot/Q14157                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBA|||Ubiquitin-associated protein 2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211020|||http://purl.uniprot.org/annotation/VAR_026829|||http://purl.uniprot.org/annotation/VSP_019417|||http://purl.uniprot.org/annotation/VSP_021728|||http://purl.uniprot.org/annotation/VSP_038235|||http://purl.uniprot.org/annotation/VSP_042167
http://togogenome.org/gene/9606:MOSPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHP6|||http://purl.uniprot.org/uniprot/R4GMN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CRAL-TRIO|||Cytoplasmic|||Disordered|||Does not affect endoplasmic reticulum distribution. Does not impair the folding of the CRAL-TRIO domain. Decreases lipid droplets (LDs) binding.|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||Loss of localization to endoplasmic reticulum membrane.|||MSP|||Motile sperm domain-containing protein 2|||Partially affects the binding of the FFAT motif of OSBPL1A. Partially affects the binding of the phosphorylated FFAT motif of STARD3.|||Polar residues|||Prevents binding to the FFAT motif of target proteins STARD3, STARD3NL, RMDN3, OSBPL1A and CERT1 and impairs recruitment to interorganelle membrane contacts; when associated with D-404. Significantly increases the recruitment at the periphery of lipid droplets, both in the presence and in the absence of oleic acid (OA); when associated with D-404. Does not affect endoplasmic reticulum membrane location; when associated with D-404.|||Prevents binding to the FFAT motif of target proteins STARD3, STARD3NL, RMDN3, OSBPL1A and CERT1 and impairs recruitment to interorganelle membrane contacts; when associated with D-406. Significantly increases the recruitment at the periphery of lipid droplets, both in the presence and in the absence of oleic acid (OA); when associated with D-406. Does not affect endoplasmic reticulum membrane location; when associated with D-406.|||Required for FFAT motif binding|||Required for FFAT motif binding and phosphorylated FFAT motif binding|||Required for phosphorylated FFAT motif binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213463|||http://purl.uniprot.org/annotation/VAR_034109|||http://purl.uniprot.org/annotation/VSP_014046
http://togogenome.org/gene/9606:TEX13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXU3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||RanBP2-type|||Testis-expressed protein 13A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065700
http://togogenome.org/gene/9606:TFAP2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6R9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||H-S-H (helix-span-helix), dimerization|||In a breast cancer sample; somatic mutation.|||Phosphoserine; by PKA|||Transcription factor AP-2-delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309513|||http://purl.uniprot.org/annotation/VAR_036975
http://togogenome.org/gene/9606:TCF7L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CTNNB1-binding|||Disordered|||HMG box|||In a breast cancer sample; somatic mutation.|||Nuclear localization signal|||Pro residues|||Transcription factor 7-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048614|||http://purl.uniprot.org/annotation/VAR_035938|||http://purl.uniprot.org/annotation/VAR_049561
http://togogenome.org/gene/9606:NTSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95665                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Neurotensin receptor type 2|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069949|||http://purl.uniprot.org/annotation/VAR_049425|||http://purl.uniprot.org/annotation/VAR_061225
http://togogenome.org/gene/9606:CBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16152                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Carbonyl reductase [NADPH] 1|||In isoform 2.|||N-acetylserine|||N6-1-carboxyethyl lysine|||Phosphoserine|||Proton acceptor|||Reduced affinity for NADPH and reduced activity towards daunorubicin and prostaglandin E2.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054602|||http://purl.uniprot.org/annotation/VAR_031706|||http://purl.uniprot.org/annotation/VAR_059053|||http://purl.uniprot.org/annotation/VSP_054796|||http://purl.uniprot.org/annotation/VSP_054797
http://togogenome.org/gene/9606:MBD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95243                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In TPDS2 and UVM1.|||In TPDS2.|||In TPDS2; loss of DNAN-glycosylase activity.|||In TPDS2; no MBD4 protein detected by immunohistochemical analysis in patient tumor tissue.|||In UVM1.|||In UVM1; loss of DNAN-glycosylase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of DNAN-glycosylase activity.|||MBD|||Methyl-CpG-binding domain protein 4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096264|||http://purl.uniprot.org/annotation/VAR_019357|||http://purl.uniprot.org/annotation/VAR_019358|||http://purl.uniprot.org/annotation/VAR_019359|||http://purl.uniprot.org/annotation/VAR_019360|||http://purl.uniprot.org/annotation/VAR_019514|||http://purl.uniprot.org/annotation/VAR_019515|||http://purl.uniprot.org/annotation/VAR_029306|||http://purl.uniprot.org/annotation/VAR_087522|||http://purl.uniprot.org/annotation/VAR_087523|||http://purl.uniprot.org/annotation/VAR_087524|||http://purl.uniprot.org/annotation/VAR_087525|||http://purl.uniprot.org/annotation/VAR_087526|||http://purl.uniprot.org/annotation/VAR_087527|||http://purl.uniprot.org/annotation/VAR_087528|||http://purl.uniprot.org/annotation/VAR_087529|||http://purl.uniprot.org/annotation/VAR_087530|||http://purl.uniprot.org/annotation/VSP_010816|||http://purl.uniprot.org/annotation/VSP_010817|||http://purl.uniprot.org/annotation/VSP_010818|||http://purl.uniprot.org/annotation/VSP_054845|||http://purl.uniprot.org/annotation/VSP_054846
http://togogenome.org/gene/9606:GPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D4PHA4|||http://purl.uniprot.org/uniprot/Q86WP2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Vasculin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324110|||http://purl.uniprot.org/annotation/VAR_039654|||http://purl.uniprot.org/annotation/VSP_032135|||http://purl.uniprot.org/annotation/VSP_032136|||http://purl.uniprot.org/annotation/VSP_032137
http://togogenome.org/gene/9606:SERINC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IM8|||http://purl.uniprot.org/uniprot/Q96SA4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Serine incorporator 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218968|||http://purl.uniprot.org/annotation/PRO_5004322513|||http://purl.uniprot.org/annotation/VAR_061838|||http://purl.uniprot.org/annotation/VSP_042463|||http://purl.uniprot.org/annotation/VSP_042464|||http://purl.uniprot.org/annotation/VSP_046840
http://togogenome.org/gene/9606:TRMT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32P41                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In PNSED; decreased mitochondrial tRNA methylation.|||tRNA (guanine(37)-N1)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256513|||http://purl.uniprot.org/annotation/VAR_028898|||http://purl.uniprot.org/annotation/VAR_028899|||http://purl.uniprot.org/annotation/VAR_028900|||http://purl.uniprot.org/annotation/VAR_075655|||http://purl.uniprot.org/annotation/VAR_075656
http://togogenome.org/gene/9606:CCDC66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUB6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 66|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Loss of association with microtubules and localization to centrosomes.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320037|||http://purl.uniprot.org/annotation/VAR_039111|||http://purl.uniprot.org/annotation/VAR_039112|||http://purl.uniprot.org/annotation/VAR_039113|||http://purl.uniprot.org/annotation/VAR_080466|||http://purl.uniprot.org/annotation/VAR_080467|||http://purl.uniprot.org/annotation/VSP_031586|||http://purl.uniprot.org/annotation/VSP_031587|||http://purl.uniprot.org/annotation/VSP_036545|||http://purl.uniprot.org/annotation/VSP_036546
http://togogenome.org/gene/9606:MECR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV79                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Enoyl-[acyl-carrier-protein] reductase, mitochondrial|||In DYTOABG.|||In DYTOABG; probably decreased protein abundance.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton donor|||Reduces catalytic activity by 68%.|||Reduces catalytic activity by 69%.|||Reduces catalytic activity by 87%. Strongly reduces affinity for trans-oct-2-enoyl-CoA.|||Reduces catalytic activity by 95%. Strongly reduces affinity for trans-oct-2-enoyl-CoA.|||Reduces catalytic activity by 98%. Strongly reduces affinity for trans-oct-2-enoyl-CoA.|||Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 25%. Decreases activity with trans-hexadec-2-enoyl-CoA by 68%.|||Strongly increases activity with trans-oct-2-enoyl-CoA. Decreases activity with trans-tetradec-2-enoyl-CoA by 73%. Decreases activity with trans-hexadec-2-enoyl-CoA by 80%.|||Strongly increases activity with trans-oct-2-enoyl-CoA. No effect on activity with trans-tetradec-2-enoyl-CoA. Decreases activity with trans-hexadec-2-enoyl-CoA by 20%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000888|||http://purl.uniprot.org/annotation/VAR_027935|||http://purl.uniprot.org/annotation/VAR_055486|||http://purl.uniprot.org/annotation/VAR_055487|||http://purl.uniprot.org/annotation/VAR_077997|||http://purl.uniprot.org/annotation/VAR_077998|||http://purl.uniprot.org/annotation/VAR_077999|||http://purl.uniprot.org/annotation/VAR_078000|||http://purl.uniprot.org/annotation/VSP_041131
http://togogenome.org/gene/9606:NAPSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QXC5|||http://purl.uniprot.org/uniprot/O96009                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||N-linked (GlcNAc...) asparagine|||Napsin-A|||Peptidase A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025996|||http://purl.uniprot.org/annotation/PRO_0000025997|||http://purl.uniprot.org/annotation/PRO_5040109165|||http://purl.uniprot.org/annotation/VAR_024586|||http://purl.uniprot.org/annotation/VAR_051510
http://togogenome.org/gene/9606:HYDIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0P3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hydrocephalus-inducing protein homolog|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Interaction with KIF9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284844|||http://purl.uniprot.org/annotation/VAR_031837|||http://purl.uniprot.org/annotation/VAR_031838|||http://purl.uniprot.org/annotation/VAR_031839|||http://purl.uniprot.org/annotation/VAR_031840|||http://purl.uniprot.org/annotation/VAR_051036|||http://purl.uniprot.org/annotation/VAR_051037|||http://purl.uniprot.org/annotation/VAR_051038|||http://purl.uniprot.org/annotation/VAR_051039|||http://purl.uniprot.org/annotation/VAR_051040|||http://purl.uniprot.org/annotation/VAR_051041|||http://purl.uniprot.org/annotation/VAR_051042|||http://purl.uniprot.org/annotation/VAR_051043|||http://purl.uniprot.org/annotation/VAR_051044|||http://purl.uniprot.org/annotation/VAR_051045|||http://purl.uniprot.org/annotation/VAR_051046|||http://purl.uniprot.org/annotation/VAR_051047|||http://purl.uniprot.org/annotation/VAR_051048|||http://purl.uniprot.org/annotation/VAR_051049|||http://purl.uniprot.org/annotation/VAR_051050|||http://purl.uniprot.org/annotation/VAR_051051|||http://purl.uniprot.org/annotation/VAR_051052|||http://purl.uniprot.org/annotation/VAR_051053|||http://purl.uniprot.org/annotation/VAR_051054|||http://purl.uniprot.org/annotation/VAR_051055|||http://purl.uniprot.org/annotation/VAR_051056|||http://purl.uniprot.org/annotation/VAR_051058|||http://purl.uniprot.org/annotation/VAR_059667|||http://purl.uniprot.org/annotation/VAR_059668|||http://purl.uniprot.org/annotation/VAR_059669|||http://purl.uniprot.org/annotation/VAR_059670|||http://purl.uniprot.org/annotation/VAR_059671|||http://purl.uniprot.org/annotation/VAR_059672|||http://purl.uniprot.org/annotation/VAR_059673|||http://purl.uniprot.org/annotation/VAR_059674|||http://purl.uniprot.org/annotation/VAR_059675|||http://purl.uniprot.org/annotation/VAR_059676|||http://purl.uniprot.org/annotation/VAR_059677|||http://purl.uniprot.org/annotation/VAR_059678|||http://purl.uniprot.org/annotation/VAR_059679|||http://purl.uniprot.org/annotation/VAR_059680|||http://purl.uniprot.org/annotation/VAR_059681|||http://purl.uniprot.org/annotation/VAR_059682|||http://purl.uniprot.org/annotation/VAR_059683|||http://purl.uniprot.org/annotation/VAR_059684|||http://purl.uniprot.org/annotation/VAR_059685|||http://purl.uniprot.org/annotation/VAR_059686|||http://purl.uniprot.org/annotation/VAR_059687|||http://purl.uniprot.org/annotation/VAR_061666|||http://purl.uniprot.org/annotation/VSP_024684|||http://purl.uniprot.org/annotation/VSP_024687|||http://purl.uniprot.org/annotation/VSP_024688|||http://purl.uniprot.org/annotation/VSP_024691|||http://purl.uniprot.org/annotation/VSP_024692|||http://purl.uniprot.org/annotation/VSP_024697|||http://purl.uniprot.org/annotation/VSP_024698|||http://purl.uniprot.org/annotation/VSP_042692|||http://purl.uniprot.org/annotation/VSP_042693|||http://purl.uniprot.org/annotation/VSP_042694|||http://purl.uniprot.org/annotation/VSP_046818
http://togogenome.org/gene/9606:KDM3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7LBC6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C6-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DIJOS.|||In DIJOS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||JmjC|||LXXLL motif|||Lysine-specific demethylase 3B|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234373|||http://purl.uniprot.org/annotation/VAR_026221|||http://purl.uniprot.org/annotation/VAR_026222|||http://purl.uniprot.org/annotation/VAR_083997|||http://purl.uniprot.org/annotation/VAR_083998|||http://purl.uniprot.org/annotation/VAR_083999|||http://purl.uniprot.org/annotation/VAR_084000|||http://purl.uniprot.org/annotation/VAR_084001|||http://purl.uniprot.org/annotation/VAR_084002|||http://purl.uniprot.org/annotation/VAR_084003|||http://purl.uniprot.org/annotation/VAR_084004|||http://purl.uniprot.org/annotation/VAR_084005|||http://purl.uniprot.org/annotation/VAR_084006|||http://purl.uniprot.org/annotation/VAR_084007|||http://purl.uniprot.org/annotation/VAR_084008|||http://purl.uniprot.org/annotation/VAR_084009|||http://purl.uniprot.org/annotation/VAR_084010|||http://purl.uniprot.org/annotation/VSP_018298|||http://purl.uniprot.org/annotation/VSP_018299|||http://purl.uniprot.org/annotation/VSP_018300
http://togogenome.org/gene/9606:SMOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWM0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||No change in enzymatic activity.|||Spermine oxidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099877|||http://purl.uniprot.org/annotation/VAR_019531|||http://purl.uniprot.org/annotation/VAR_036546|||http://purl.uniprot.org/annotation/VAR_059114|||http://purl.uniprot.org/annotation/VSP_011123|||http://purl.uniprot.org/annotation/VSP_011124|||http://purl.uniprot.org/annotation/VSP_011125|||http://purl.uniprot.org/annotation/VSP_011126
http://togogenome.org/gene/9606:PPP1R16A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I34                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 16A|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067040|||http://purl.uniprot.org/annotation/PRO_0000396707
http://togogenome.org/gene/9606:AGBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MI9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytosolic carboxypeptidase 4|||Disordered|||In FECD8; decreased TCF4-binding.|||In FECD8; enriched in the nucleus, decreased TCF4-binding.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304999|||http://purl.uniprot.org/annotation/VAR_048604|||http://purl.uniprot.org/annotation/VAR_048605|||http://purl.uniprot.org/annotation/VAR_059195|||http://purl.uniprot.org/annotation/VAR_070225|||http://purl.uniprot.org/annotation/VAR_070226
http://togogenome.org/gene/9606:IFFO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ16|||http://purl.uniprot.org/uniprot/B4DQQ1|||http://purl.uniprot.org/uniprot/Q0D2I5|||http://purl.uniprot.org/uniprot/Q6P593|||http://purl.uniprot.org/uniprot/Q9Y4M3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased interaction with LMNA.|||Decreased interaction with LMNA. Loss of ability to immobilize broken ends; when associated with H-85.|||Decreased interaction with XRCC4; when associated with A-490. Loss of interaction with XRCC4; when associated with A-490 and A-509.|||Decreased interaction with XRCC4; when associated with A-516. Loss of interaction with XRCC4; when associated with A-509 and A-516.|||Disordered|||Does not affect the interaction with LMNA.|||IF rod|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 7.|||LMNA binding|||Loss of interaction with XRCC4, loss of localization at the sites of DNA damages and loss of ability to immobilize broken ends.|||Loss of interaction with XRCC4.|||Loss of interaction with XRCC4; when associated with A-490 and A-516.|||Loss of interaction with XRCC4; when associated with R-480.|||Loss of interaction with XRCC4; when associated with R-487.|||Non-homologous end joining factor IFFO1|||Polar residues|||Pro residues|||XCCR4 binding. Required for localization to the double-strand breaks (DSBs)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316794|||http://purl.uniprot.org/annotation/VSP_030781|||http://purl.uniprot.org/annotation/VSP_030782|||http://purl.uniprot.org/annotation/VSP_030783|||http://purl.uniprot.org/annotation/VSP_030784|||http://purl.uniprot.org/annotation/VSP_038240|||http://purl.uniprot.org/annotation/VSP_039709
http://togogenome.org/gene/9606:DUSP29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68J44                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Dual specificity phosphatase 29|||Phosphocysteine intermediate|||Polar residues|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295877|||http://purl.uniprot.org/annotation/VAR_033376|||http://purl.uniprot.org/annotation/VAR_051757
http://togogenome.org/gene/9606:ZNF184                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99676                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Polar residues|||Zinc finger protein 184                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047443|||http://purl.uniprot.org/annotation/VAR_045989
http://togogenome.org/gene/9606:GMPPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IJ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In AAMR.|||In AAMR; drastically reduced protein expression.|||In isoform 2.|||Mannose-1-phosphate guanyltransferase alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327872|||http://purl.uniprot.org/annotation/VAR_042434|||http://purl.uniprot.org/annotation/VAR_042435|||http://purl.uniprot.org/annotation/VAR_070203|||http://purl.uniprot.org/annotation/VAR_070204|||http://purl.uniprot.org/annotation/VAR_070205|||http://purl.uniprot.org/annotation/VAR_070206|||http://purl.uniprot.org/annotation/VAR_070207|||http://purl.uniprot.org/annotation/VSP_032741
http://togogenome.org/gene/9606:FAM169A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Soluble lamin-associated protein of 75 kDa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320587|||http://purl.uniprot.org/annotation/VSP_031670|||http://purl.uniprot.org/annotation/VSP_031671
http://togogenome.org/gene/9606:OR7G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVS6|||http://purl.uniprot.org/uniprot/Q8NGA0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7G1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150650|||http://purl.uniprot.org/annotation/VAR_034255|||http://purl.uniprot.org/annotation/VAR_034256|||http://purl.uniprot.org/annotation/VAR_048074|||http://purl.uniprot.org/annotation/VAR_048075|||http://purl.uniprot.org/annotation/VAR_048076
http://togogenome.org/gene/9606:KRT19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08727                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments.|||Asymmetric dimethylarginine; alternate|||Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cytoskeletal 19|||Linker 1|||Linker 12|||Necessary for interaction with PNN|||No effect on phosphorylation; no functional effect.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Rod-like helical tail|||Stutter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063671|||http://purl.uniprot.org/annotation/VAR_014629
http://togogenome.org/gene/9606:CCZ1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86790|||http://purl.uniprot.org/uniprot/P86791                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar fusion protein CCZ1 homolog|||Vacuolar fusion protein CCZ1 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089584|||http://purl.uniprot.org/annotation/PRO_0000401065
http://togogenome.org/gene/9606:FBXL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1E6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 14|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Required for down-regulation of SNAI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119861|||http://purl.uniprot.org/annotation/VAR_049033
http://togogenome.org/gene/9606:ZNF350                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 350                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047546|||http://purl.uniprot.org/annotation/VAR_019902|||http://purl.uniprot.org/annotation/VAR_019903|||http://purl.uniprot.org/annotation/VAR_019904|||http://purl.uniprot.org/annotation/VAR_019905|||http://purl.uniprot.org/annotation/VAR_046718|||http://purl.uniprot.org/annotation/VAR_046719|||http://purl.uniprot.org/annotation/VAR_046720|||http://purl.uniprot.org/annotation/VAR_046721
http://togogenome.org/gene/9606:NT5C3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0P0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of nucleotidase and phosphotransferase activity.|||Cytosolic 5'-nucleotidase 3A|||In P5ND.|||In P5ND; almost complete loss of catalytic activity.|||In P5ND; greatly reduced catalytic activity.|||In P5ND; reduced catalytic activity especially towards UMP.|||In P5ND; reduced catalytic activity in vitro; reduced protein stability in vivo, probably through increased proteasomal degradation.|||In P5ND; reduced catalytic activity.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Loss of nucleotidase and phosphotransferase activity.|||No effect on nucleotidase activity. Almost complete loss of phosphotransferase activity.|||No effect on nucleotidase and phosphotransferase activity.|||Nucleophile|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064387|||http://purl.uniprot.org/annotation/VAR_023511|||http://purl.uniprot.org/annotation/VAR_023512|||http://purl.uniprot.org/annotation/VAR_023513|||http://purl.uniprot.org/annotation/VAR_023514|||http://purl.uniprot.org/annotation/VAR_073160|||http://purl.uniprot.org/annotation/VAR_073161|||http://purl.uniprot.org/annotation/VAR_073162|||http://purl.uniprot.org/annotation/VAR_073163|||http://purl.uniprot.org/annotation/VSP_015623|||http://purl.uniprot.org/annotation/VSP_015624|||http://purl.uniprot.org/annotation/VSP_021565
http://togogenome.org/gene/9606:UCKL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53HM1|||http://purl.uniprot.org/uniprot/Q9NWZ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoribulokinase/uridine kinase|||Phosphoserine|||Polar residues|||Uridine-cytidine kinase-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164460|||http://purl.uniprot.org/annotation/VSP_021802|||http://purl.uniprot.org/annotation/VSP_025641|||http://purl.uniprot.org/annotation/VSP_025642|||http://purl.uniprot.org/annotation/VSP_043171
http://togogenome.org/gene/9606:PLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26678|||http://purl.uniprot.org/uniprot/Q5R352                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes phosphorylation by PKA.|||Cardiac phospholamban|||Cytoplasmic|||Helical|||In CMD1P; impairs phosphorylation by PKA and inhibition of ATP2A1-mediated calcium uptake.|||In CMD1P; impairs phosphorylation by PKA, destabilizes the homopentamer and mildly reduces inhibition of ATP2A1-mediated calcium uptake.|||Involved in HAX1 binding|||N-acetylmethionine|||No effect on phosphorylation by PKA.|||Phosphoserine; by PKA and DMPK|||Phosphothreonine; by CaMK2|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191244|||http://purl.uniprot.org/annotation/VAR_025989|||http://purl.uniprot.org/annotation/VAR_025990|||http://purl.uniprot.org/annotation/VAR_072925|||http://purl.uniprot.org/annotation/VAR_072926
http://togogenome.org/gene/9606:CEMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PRD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cementoblastoma-derived protein 1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264475|||http://purl.uniprot.org/annotation/VAR_050792
http://togogenome.org/gene/9606:TMEM121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Pro residues|||Transmembrane protein 121                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251245
http://togogenome.org/gene/9606:CPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15088                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Mast cell carboxypeptidase A|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004395|||http://purl.uniprot.org/annotation/PRO_0000004396|||http://purl.uniprot.org/annotation/VAR_033725|||http://purl.uniprot.org/annotation/VAR_048602
http://togogenome.org/gene/9606:ANO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHL6|||http://purl.uniprot.org/uniprot/B7Z9B9|||http://purl.uniprot.org/uniprot/Q9BYT9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin dimerisation|||Anoctamin-3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DYT24.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072565|||http://purl.uniprot.org/annotation/VAR_057287|||http://purl.uniprot.org/annotation/VAR_069732|||http://purl.uniprot.org/annotation/VAR_069733|||http://purl.uniprot.org/annotation/VAR_069734|||http://purl.uniprot.org/annotation/VAR_069735|||http://purl.uniprot.org/annotation/VSP_056893
http://togogenome.org/gene/9606:IQCN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0JP07|||http://purl.uniprot.org/uniprot/Q9H0B3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||IQ domain-containing protein N|||In SPGF78.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050801|||http://purl.uniprot.org/annotation/VAR_023418|||http://purl.uniprot.org/annotation/VAR_023419|||http://purl.uniprot.org/annotation/VAR_023420|||http://purl.uniprot.org/annotation/VAR_023421|||http://purl.uniprot.org/annotation/VAR_023422|||http://purl.uniprot.org/annotation/VAR_034042|||http://purl.uniprot.org/annotation/VAR_034043|||http://purl.uniprot.org/annotation/VAR_049520|||http://purl.uniprot.org/annotation/VAR_049521|||http://purl.uniprot.org/annotation/VAR_049522|||http://purl.uniprot.org/annotation/VAR_049523|||http://purl.uniprot.org/annotation/VAR_049524|||http://purl.uniprot.org/annotation/VAR_049525|||http://purl.uniprot.org/annotation/VAR_087804|||http://purl.uniprot.org/annotation/VSP_015473|||http://purl.uniprot.org/annotation/VSP_015474|||http://purl.uniprot.org/annotation/VSP_015475|||http://purl.uniprot.org/annotation/VSP_015476|||http://purl.uniprot.org/annotation/VSP_045713|||http://purl.uniprot.org/annotation/VSP_045714
http://togogenome.org/gene/9606:ZNF207                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43670                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BUB3-interacting and GLEBS motif-containing protein ZNF207|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||GLEBS|||In BuGZAA: Abolishes interaction with BUB3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Microtubule-binding region|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047453|||http://purl.uniprot.org/annotation/VAR_019974|||http://purl.uniprot.org/annotation/VSP_006903|||http://purl.uniprot.org/annotation/VSP_006904|||http://purl.uniprot.org/annotation/VSP_006905
http://togogenome.org/gene/9606:ARHGAP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N392                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes GTPase activation activity.|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 18|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245789|||http://purl.uniprot.org/annotation/VAR_060460|||http://purl.uniprot.org/annotation/VAR_060461|||http://purl.uniprot.org/annotation/VAR_060462|||http://purl.uniprot.org/annotation/VSP_052092
http://togogenome.org/gene/9606:MKS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V2M0|||http://purl.uniprot.org/uniprot/Q9NXB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2 B9-type|||Disordered|||Found in a patient with Joubert syndrome also carrying a deletion in MKS1 intron 15 and a missense mutation in TCTN3 gene 'P-95'; unknown pathological significance.|||In BBS13.|||In JBTS28.|||In MKS1; no rescue of ciliation defects in an MKS1-knockdown cell line.|||In MKS1; unknown pathological significance.|||In MKS1; unknown pathological significance; decreased primary cilia formation in starved fibroblasts from a patient also carrying a mutation potentially affecting splicing; complete rescue of ciliation defects in an MKS1-knockdown cell line; no effect on the localization to the transition zone.|||In MKS1; unknown pathological significance; no defect of primary cilia formation in starved fibroblasts from a patient also carrying E-317; no effect on the localization to the transition zone.|||In MKS1; unknown pathological significance; no defect of primary cilia formation in starved fibroblasts from a patient also carrying a deletion of S-372; no effect on the localization to the transition zone.|||In MKS1; unknown pathological significance; no effect on primary cilia formation in starved fibroblasts from a patient also carrying a mutation creating a frameshift and a premature stop codon; partial rescue of ciliation defects in an MKS1-knockdown cell line; no effect on the localization to the transition zone.|||In isoform 2.|||In isoform 3.|||Pro residues|||Tectonic-like complex member MKS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225686|||http://purl.uniprot.org/annotation/VAR_060161|||http://purl.uniprot.org/annotation/VAR_062287|||http://purl.uniprot.org/annotation/VAR_062288|||http://purl.uniprot.org/annotation/VAR_062289|||http://purl.uniprot.org/annotation/VAR_062290|||http://purl.uniprot.org/annotation/VAR_062291|||http://purl.uniprot.org/annotation/VAR_062292|||http://purl.uniprot.org/annotation/VAR_076978|||http://purl.uniprot.org/annotation/VAR_077515|||http://purl.uniprot.org/annotation/VAR_077516|||http://purl.uniprot.org/annotation/VAR_077517|||http://purl.uniprot.org/annotation/VAR_077518|||http://purl.uniprot.org/annotation/VAR_077519|||http://purl.uniprot.org/annotation/VAR_077520|||http://purl.uniprot.org/annotation/VSP_017414|||http://purl.uniprot.org/annotation/VSP_046063
http://togogenome.org/gene/9606:GYPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15421                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycophorin-E|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012138|||http://purl.uniprot.org/annotation/VAR_053111|||http://purl.uniprot.org/annotation/VAR_062006
http://togogenome.org/gene/9606:RMDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DB5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||N6-succinyllysine|||Regulator of microtubule dynamics protein 1|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187181|||http://purl.uniprot.org/annotation/VAR_049028|||http://purl.uniprot.org/annotation/VSP_054647|||http://purl.uniprot.org/annotation/VSP_055727
http://togogenome.org/gene/9606:CSNK1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49674|||http://purl.uniprot.org/uniprot/Q5U045                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Casein kinase I isoform epsilon|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||Loss of kinase activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192837|||http://purl.uniprot.org/annotation/VAR_042082|||http://purl.uniprot.org/annotation/VAR_042083
http://togogenome.org/gene/9606:STON1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB25|||http://purl.uniprot.org/uniprot/Q9Y6Q2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||MHD|||Polar residues|||SHD|||Stonin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185736|||http://purl.uniprot.org/annotation/VAR_020183|||http://purl.uniprot.org/annotation/VAR_020184|||http://purl.uniprot.org/annotation/VAR_020185|||http://purl.uniprot.org/annotation/VAR_052156|||http://purl.uniprot.org/annotation/VSP_045845|||http://purl.uniprot.org/annotation/VSP_045846
http://togogenome.org/gene/9606:LINGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L985                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324389|||http://purl.uniprot.org/annotation/VAR_039798
http://togogenome.org/gene/9606:RCOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKL0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ELM2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with HDAC1|||Interaction with KDM1A|||Phosphoserine|||Polar residues|||REST corepressor 1|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226773
http://togogenome.org/gene/9606:ADNP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ32                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Activity-dependent neuroprotector homeobox protein 2|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280416
http://togogenome.org/gene/9606:TSC22D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKI8|||http://purl.uniprot.org/uniprot/Q9Y3Q8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||TSC22 domain family protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219374|||http://purl.uniprot.org/annotation/VAR_036284|||http://purl.uniprot.org/annotation/VSP_056245
http://togogenome.org/gene/9606:NISCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2I1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits targeting to endosomes.|||Interaction with ITGA5|||Interaction with LIMK|||Interaction with PAK1|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||N-acetylalanine|||Necessary for binding to phosphoinositide-3-P; not sufficient for targeting to endosomes|||Necessary for homooligomerization and targeting to endosomes|||Nischarin|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348265|||http://purl.uniprot.org/annotation/VAR_046130|||http://purl.uniprot.org/annotation/VAR_046131|||http://purl.uniprot.org/annotation/VSP_035131|||http://purl.uniprot.org/annotation/VSP_035132|||http://purl.uniprot.org/annotation/VSP_035133|||http://purl.uniprot.org/annotation/VSP_035134|||http://purl.uniprot.org/annotation/VSP_035135
http://togogenome.org/gene/9606:SH3GL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FGM0|||http://purl.uniprot.org/uniprot/Q99961                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  BAR|||Basic and acidic residues|||Breakpoint for translocation to form KMT2A/MLL1-EEN oncogene|||Disordered|||Endophilin-A2|||In isoform 2.|||In isoform 3.|||Interaction with ARC|||Membrane-binding amphipathic helix|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Required for dimerization upon membrane association|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146744|||http://purl.uniprot.org/annotation/VSP_045837|||http://purl.uniprot.org/annotation/VSP_047037
http://togogenome.org/gene/9606:BRAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H81|||http://purl.uniprot.org/uniprot/Q7Z569                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BRCA1-associated protein|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of E3 ubiquitin-protein ligase activity.|||Phosphoserine|||RING-type|||UBP-type|||UBP-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055825|||http://purl.uniprot.org/annotation/VSP_055881|||http://purl.uniprot.org/annotation/VSP_055882
http://togogenome.org/gene/9606:FUBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Far upstream element-binding protein 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KH 1|||KH 2|||KH 3|||KH 4|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050140|||http://purl.uniprot.org/annotation/VSP_008323|||http://purl.uniprot.org/annotation/VSP_008324
http://togogenome.org/gene/9606:PIKFYVE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2I7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  1-phosphatidylinositol 3-phosphate 5-kinase|||Basic and acidic residues|||Catalytic|||Chaperonin-like domain|||DEP|||Disordered|||FYVE-type|||In CFD.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||Loss of autophosphorylation. Loss of phosphatidylinositol 3-phosphate 5-kinase activity.|||N-acetylalanine|||No effect on phosphatidylinositol 3-phosphate 5-kinase activity.|||PIPK|||Phosphoserine|||Phosphoserine; by PKB/AKT1 or PKB/AKT2|||Phosphoserine; by autocatalysis|||Polar residues|||Reduces 2-folds phosphatidylinositol 3-phosphate 5-kinase activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185452|||http://purl.uniprot.org/annotation/VAR_025309|||http://purl.uniprot.org/annotation/VAR_057097|||http://purl.uniprot.org/annotation/VAR_057098|||http://purl.uniprot.org/annotation/VAR_057099|||http://purl.uniprot.org/annotation/VAR_063406|||http://purl.uniprot.org/annotation/VAR_063407|||http://purl.uniprot.org/annotation/VAR_063408|||http://purl.uniprot.org/annotation/VAR_063409|||http://purl.uniprot.org/annotation/VAR_063410|||http://purl.uniprot.org/annotation/VAR_083736|||http://purl.uniprot.org/annotation/VSP_040108|||http://purl.uniprot.org/annotation/VSP_040109|||http://purl.uniprot.org/annotation/VSP_040110|||http://purl.uniprot.org/annotation/VSP_040111
http://togogenome.org/gene/9606:RPL39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62891                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Large ribosomal subunit protein eL39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127024
http://togogenome.org/gene/9606:IQCF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7M6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  IQ|||IQ domain-containing protein F3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339381
http://togogenome.org/gene/9606:EMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0I2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||ER membrane protein complex subunit 3|||Helical|||In isoform 2.|||Lumenal|||No effect on EMC assembly and no effect on membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC.|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC.|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC; when associated S-101, S-106 and S-110.|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC; when associated S-101, S-106 and S-111.|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC; when associated S-101, S-110 and S-111.|||No effect on EMC assembly but decreased membrane insertion of hydrophobic transmembrane helices-containing proteins by the EMC; when associated S-106, S-110 and S-111.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211406|||http://purl.uniprot.org/annotation/VSP_014886
http://togogenome.org/gene/9606:IPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y573                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding protein IPP|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119075|||http://purl.uniprot.org/annotation/VAR_050045|||http://purl.uniprot.org/annotation/VSP_040993
http://togogenome.org/gene/9606:PPP3CA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4B5|||http://purl.uniprot.org/uniprot/A0A0S2Z4C6|||http://purl.uniprot.org/uniprot/Q08209                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Autoinhibitory domain|||Autoinhibitory segment|||Calcineurin B binding|||Calmodulin-binding|||Catalytic|||Disordered|||In ACCIID.|||In IECEE1.|||In IECEE1; results in constitutive phosphatase activity in the absence of calmodulin.|||In IECEE1; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PxIxIF motif in substrate|||Interaction with PxVP motif in substrate|||Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341.|||N-acetylserine|||Partial loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with F-341.|||Phosphoserine|||Polar residues|||Protein phosphatase 3 catalytic subunit alpha|||Proton donor|||Removed|||Resistant to cyclosporin A-mediated inhibition. Loss of Ca(2+)-mediated transcription factor NFAT activation; when associated with N-288, A-228 or 328-V--R-332 DEL. Partial loss in Ca(2+)-mediated transcription factor NFAT activation; when associated with F-288.|||SAPNY motif|||Serine/threonine specific protein phosphatases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058822|||http://purl.uniprot.org/annotation/VAR_080348|||http://purl.uniprot.org/annotation/VAR_080349|||http://purl.uniprot.org/annotation/VAR_080350|||http://purl.uniprot.org/annotation/VAR_080351|||http://purl.uniprot.org/annotation/VAR_080352|||http://purl.uniprot.org/annotation/VAR_081900|||http://purl.uniprot.org/annotation/VAR_081901|||http://purl.uniprot.org/annotation/VAR_081902|||http://purl.uniprot.org/annotation/VAR_081903|||http://purl.uniprot.org/annotation/VAR_085829|||http://purl.uniprot.org/annotation/VSP_018562|||http://purl.uniprot.org/annotation/VSP_043378|||http://purl.uniprot.org/annotation/VSP_047755|||http://purl.uniprot.org/annotation/VSP_054467
http://togogenome.org/gene/9606:CD38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E006|||http://purl.uniprot.org/uniprot/P28907                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of cADPR hydrolase activity.|||Loss of cADPR hydrolase and ADP-ribosyl cyclase activity.|||N-linked (GlcNAc...) asparagine|||Seems to contribute to the development of type II diabetes; 50% reduction in activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144066|||http://purl.uniprot.org/annotation/VAR_001323|||http://purl.uniprot.org/annotation/VSP_000707|||http://purl.uniprot.org/annotation/VSP_000708
http://togogenome.org/gene/9606:MLIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MMCKR.|||In MMCKR; decreased transcript level in muscle from homozygous patient, no effect on subcellular location.|||In MMCKR; may decrease the expression level in muscle from homozygous patient.|||In isoform 1 and isoform 4.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||Interaction with LMNA|||Muscular LMNA-interacting protein|||Phosphoserine|||Polar residues|||Required for interaction with ISL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089538|||http://purl.uniprot.org/annotation/VAR_023381|||http://purl.uniprot.org/annotation/VAR_023382|||http://purl.uniprot.org/annotation/VAR_056800|||http://purl.uniprot.org/annotation/VAR_087829|||http://purl.uniprot.org/annotation/VAR_087830|||http://purl.uniprot.org/annotation/VAR_087831|||http://purl.uniprot.org/annotation/VAR_087832|||http://purl.uniprot.org/annotation/VAR_087833|||http://purl.uniprot.org/annotation/VSP_061852|||http://purl.uniprot.org/annotation/VSP_061853|||http://purl.uniprot.org/annotation/VSP_061854|||http://purl.uniprot.org/annotation/VSP_061855|||http://purl.uniprot.org/annotation/VSP_061856|||http://purl.uniprot.org/annotation/VSP_061857
http://togogenome.org/gene/9606:H1-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02539                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.1|||N-acetylserine|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Significant destabilization of binding to chromatin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195905|||http://purl.uniprot.org/annotation/VAR_049301|||http://purl.uniprot.org/annotation/VAR_049302|||http://purl.uniprot.org/annotation/VAR_049303
http://togogenome.org/gene/9606:OR10W1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGF6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 10W1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150719|||http://purl.uniprot.org/annotation/VAR_057568
http://togogenome.org/gene/9606:LIMK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53671                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cofilin phosphorylation and enhancement of stress fiber formation.|||Abrogates kinase activity.|||Disordered|||In isoform 3.|||In isoform LIMK2b and isoform 3.|||LIM domain kinase 2|||LIM zinc-binding 1|||LIM zinc-binding 2|||PDZ|||Phosphomimetic mutant; enhances kinase activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by ROCK1 and CDC42BP|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075809|||http://purl.uniprot.org/annotation/VAR_034069|||http://purl.uniprot.org/annotation/VAR_042249|||http://purl.uniprot.org/annotation/VAR_042250|||http://purl.uniprot.org/annotation/VAR_042251|||http://purl.uniprot.org/annotation/VAR_042252|||http://purl.uniprot.org/annotation/VAR_050149|||http://purl.uniprot.org/annotation/VSP_012287|||http://purl.uniprot.org/annotation/VSP_043332
http://togogenome.org/gene/9606:PRR20D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86478|||http://purl.uniprot.org/uniprot/P86479|||http://purl.uniprot.org/uniprot/P86480|||http://purl.uniprot.org/uniprot/P86481|||http://purl.uniprot.org/uniprot/P86496                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 20A|||Proline-rich protein 20B|||Proline-rich protein 20C|||Proline-rich protein 20D|||Proline-rich protein 20E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336092|||http://purl.uniprot.org/annotation/PRO_0000393890|||http://purl.uniprot.org/annotation/PRO_0000393891|||http://purl.uniprot.org/annotation/PRO_0000393892|||http://purl.uniprot.org/annotation/PRO_0000393893
http://togogenome.org/gene/9606:RCC1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I51                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrion|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||RCC1-like G exchanging factor-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206656|||http://purl.uniprot.org/annotation/VAR_027972|||http://purl.uniprot.org/annotation/VSP_055617|||http://purl.uniprot.org/annotation/VSP_055618|||http://purl.uniprot.org/annotation/VSP_055619
http://togogenome.org/gene/9606:DCLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N568                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Doublecortin 1|||Doublecortin 2|||Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085922|||http://purl.uniprot.org/annotation/VAR_040441|||http://purl.uniprot.org/annotation/VAR_040442|||http://purl.uniprot.org/annotation/VAR_040443|||http://purl.uniprot.org/annotation/VAR_073158|||http://purl.uniprot.org/annotation/VSP_012793|||http://purl.uniprot.org/annotation/VSP_012794
http://togogenome.org/gene/9606:VMA21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZAQ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Vacuolar ATPase assembly integral membrane protein VMA21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331499|||http://purl.uniprot.org/annotation/VSP_041257
http://togogenome.org/gene/9606:FCAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24071                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Immunoglobulin alpha Fc receptor|||In isoform A.2, isoform U02 and isoform U13.|||In isoform A.3.|||In isoform B and isoform B-delta-S2.|||In isoform B-delta-S2, isoform L10, isoform U09, isoform U10, isoform U11 and isoform U13.|||In isoform L10.|||In isoform U02.|||In isoform U09.|||In isoform U10.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015138|||http://purl.uniprot.org/annotation/VAR_049996|||http://purl.uniprot.org/annotation/VAR_049997|||http://purl.uniprot.org/annotation/VSP_002632|||http://purl.uniprot.org/annotation/VSP_002633|||http://purl.uniprot.org/annotation/VSP_002634|||http://purl.uniprot.org/annotation/VSP_002635|||http://purl.uniprot.org/annotation/VSP_002636|||http://purl.uniprot.org/annotation/VSP_043565|||http://purl.uniprot.org/annotation/VSP_043566|||http://purl.uniprot.org/annotation/VSP_043567
http://togogenome.org/gene/9606:CNPY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N129                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Protein canopy homolog 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314018|||http://purl.uniprot.org/annotation/VAR_062216
http://togogenome.org/gene/9606:ZMPSTE24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75844                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CAAX prenyl protease 1 homolog|||Helical|||In MADB.|||In MADB; does not affect enzyme activity.|||Loss of catalytic activity but not viral restriction.|||Lumenal|||Nuclear                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000138844|||http://purl.uniprot.org/annotation/VAR_019308|||http://purl.uniprot.org/annotation/VAR_034711|||http://purl.uniprot.org/annotation/VAR_064501|||http://purl.uniprot.org/annotation/VAR_064502
http://togogenome.org/gene/9606:NUDT16L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRJ7|||http://purl.uniprot.org/uniprot/W4VSQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with TP53BP1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with PXN|||Pro residues|||Required for interaction with TP53BP1|||Still able to interact with TP53BP1.|||Tudor-interacting repair regulator protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097648|||http://purl.uniprot.org/annotation/VSP_014276
http://togogenome.org/gene/9606:GRPEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||GrpE protein homolog 1, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013049
http://togogenome.org/gene/9606:KCTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3U043|||http://purl.uniprot.org/uniprot/Q719H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||BTB|||BTB/POZ domain-containing protein KCTD1|||Disordered|||In SENS.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247144|||http://purl.uniprot.org/annotation/VAR_049722|||http://purl.uniprot.org/annotation/VAR_069971|||http://purl.uniprot.org/annotation/VAR_069972|||http://purl.uniprot.org/annotation/VAR_069973|||http://purl.uniprot.org/annotation/VAR_069974|||http://purl.uniprot.org/annotation/VAR_069975|||http://purl.uniprot.org/annotation/VAR_069976|||http://purl.uniprot.org/annotation/VAR_069977|||http://purl.uniprot.org/annotation/VAR_069978
http://togogenome.org/gene/9606:EMID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A84                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Collagen-like|||Disordered|||EMI|||EMI domain-containing protein 1|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007823|||http://purl.uniprot.org/annotation/VAR_019803|||http://purl.uniprot.org/annotation/VSP_008445|||http://purl.uniprot.org/annotation/VSP_011824
http://togogenome.org/gene/9606:ZNF586                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXT0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 586                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000241449|||http://purl.uniprot.org/annotation/VSP_043420|||http://purl.uniprot.org/annotation/VSP_043421|||http://purl.uniprot.org/annotation/VSP_044808
http://togogenome.org/gene/9606:MAN1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59G34|||http://purl.uniprot.org/uniprot/Q9NR34                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210315
http://togogenome.org/gene/9606:SPATA2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUW3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Spermatogenesis-associated protein 2-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297670|||http://purl.uniprot.org/annotation/VSP_027332|||http://purl.uniprot.org/annotation/VSP_027333
http://togogenome.org/gene/9606:OR10AG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVM8|||http://purl.uniprot.org/uniprot/Q8NH19                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10AG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150692
http://togogenome.org/gene/9606:NDUFAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y375                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Complex I intermediate-associated protein 30, mitochondrial|||Disordered|||In MC1DN11.|||In MC1DN11; due to a nucleotide substitution located in the splice site consensus sequence at the end of exon 3; patient cells contain normally spliced transcripts corresponding to protein variant R-253 but also transcripts lacking the final 6 base pairs of exon 3 and corresponding to protein variant 252-VK-253 del.|||In MC1DN11; due to a nucleotide substitution located in the splice site consensus sequence at the end of exon 3; patient cells contain transcripts lacking the final 6 base pairs of exon 3 but also contain normally spliced transcripts corresponding to protein variant R-253.|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005464|||http://purl.uniprot.org/annotation/VAR_013559|||http://purl.uniprot.org/annotation/VAR_013560|||http://purl.uniprot.org/annotation/VAR_013561|||http://purl.uniprot.org/annotation/VAR_013562|||http://purl.uniprot.org/annotation/VAR_081445|||http://purl.uniprot.org/annotation/VAR_081446|||http://purl.uniprot.org/annotation/VAR_081447|||http://purl.uniprot.org/annotation/VAR_081448|||http://purl.uniprot.org/annotation/VAR_081449
http://togogenome.org/gene/9606:PCDHGB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-B6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003981|||http://purl.uniprot.org/annotation/VAR_021883|||http://purl.uniprot.org/annotation/VAR_021884|||http://purl.uniprot.org/annotation/VAR_048572|||http://purl.uniprot.org/annotation/VSP_008694|||http://purl.uniprot.org/annotation/VSP_008695
http://togogenome.org/gene/9606:LSAMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z661|||http://purl.uniprot.org/uniprot/Q13449                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  GPI-anchor amidated asparagine; alternate|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Limbic system-associated membrane protein|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; alternate|||Phosphotyrosine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015102|||http://purl.uniprot.org/annotation/PRO_0000015103|||http://purl.uniprot.org/annotation/PRO_5002866756|||http://purl.uniprot.org/annotation/VAR_083713
http://togogenome.org/gene/9606:STK19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8L3|||http://purl.uniprot.org/uniprot/P49842                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 1.|||In isoform 3 and isoform 1.|||Inactive serine/threonine-protein kinase 19|||Recurrent gain-of-function variant found in metastatic melanoma; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072275|||http://purl.uniprot.org/annotation/VAR_042361|||http://purl.uniprot.org/annotation/VAR_042362|||http://purl.uniprot.org/annotation/VAR_042363|||http://purl.uniprot.org/annotation/VAR_051387|||http://purl.uniprot.org/annotation/VSP_061960|||http://purl.uniprot.org/annotation/VSP_061961
http://togogenome.org/gene/9606:CTAGE15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2H0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||cTAGE family member 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422399
http://togogenome.org/gene/9606:ERVFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60507                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CKS-17|||CX6CC|||CXXC|||Cleavage|||Cytoplasmic|||Endogenous retrovirus group FC1 Env polyprotein|||Extracellular|||Fusion peptide|||Helical|||N-linked (GlcNAc...) asparagine|||Surface protein|||Transmembrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008430|||http://purl.uniprot.org/annotation/PRO_0000008431|||http://purl.uniprot.org/annotation/PRO_0000008432
http://togogenome.org/gene/9606:UBTF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17480                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HMG box 1|||HMG box 2|||HMG box 3|||HMG box 4|||HMG box 5|||HMG box 6|||In CONDBA; increased RNA polymerase I core element sequence-specific DNA binding; increased transcription from RNA polymerase I promoter.|||In isoform UBF2.|||N-acetylmethionine|||Nucleolar transcription factor 1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048625|||http://purl.uniprot.org/annotation/VAR_080139|||http://purl.uniprot.org/annotation/VSP_002193
http://togogenome.org/gene/9606:ARHGAP44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ERK8|||http://purl.uniprot.org/uniprot/Q17R89|||http://purl.uniprot.org/uniprot/Q69Z00                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAR|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Interaction with BST2|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 44|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280480|||http://purl.uniprot.org/annotation/VAR_031159|||http://purl.uniprot.org/annotation/VSP_053616|||http://purl.uniprot.org/annotation/VSP_053617|||http://purl.uniprot.org/annotation/VSP_053618
http://togogenome.org/gene/9606:LY6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14210                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||Lymphocyte antigen 6D|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036134|||http://purl.uniprot.org/annotation/PRO_0000036135|||http://purl.uniprot.org/annotation/VAR_038712
http://togogenome.org/gene/9606:CHST14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCH0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 14|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In EDSMC1; associated in a complex allele with G-135; results in altered intracellular processing.|||In EDSMC1; associated in a complex allele with Q-137; results in altered intracellular processing.|||In EDSMC1; loss of activity.|||In EDSMC1; results in altered intracellular processing.|||In EDSMC1; results in altered intracellular processing; loss of activity.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189672|||http://purl.uniprot.org/annotation/VAR_063754|||http://purl.uniprot.org/annotation/VAR_063755|||http://purl.uniprot.org/annotation/VAR_063756|||http://purl.uniprot.org/annotation/VAR_063757|||http://purl.uniprot.org/annotation/VAR_064555|||http://purl.uniprot.org/annotation/VAR_064556
http://togogenome.org/gene/9606:GGT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJJ9|||http://purl.uniprot.org/uniprot/Q9UJ14                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Glutathione hydrolase 7 heavy chain|||Glutathione hydrolase 7 light chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011066|||http://purl.uniprot.org/annotation/PRO_0000011067|||http://purl.uniprot.org/annotation/VSP_008133|||http://purl.uniprot.org/annotation/VSP_008134|||http://purl.uniprot.org/annotation/VSP_008136|||http://purl.uniprot.org/annotation/VSP_008137|||http://purl.uniprot.org/annotation/VSP_008138|||http://purl.uniprot.org/annotation/VSP_008139|||http://purl.uniprot.org/annotation/VSP_008140|||http://purl.uniprot.org/annotation/VSP_008141
http://togogenome.org/gene/9606:RASAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIU1|||http://purl.uniprot.org/uniprot/A0A8Q3SJF6|||http://purl.uniprot.org/uniprot/A8K2P3|||http://purl.uniprot.org/uniprot/Q9UJF2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras GTPase-activating protein nGAP|||Ras-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056653|||http://purl.uniprot.org/annotation/VAR_035541|||http://purl.uniprot.org/annotation/VAR_035542|||http://purl.uniprot.org/annotation/VSP_045777|||http://purl.uniprot.org/annotation/VSP_045778
http://togogenome.org/gene/9606:AMIGO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amphoterin-induced protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014506
http://togogenome.org/gene/9606:ATAD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWS5|||http://purl.uniprot.org/uniprot/Q9ULI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 2B|||Acidic residues|||Basic and acidic residues|||Bromo|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050789|||http://purl.uniprot.org/annotation/VAR_055467|||http://purl.uniprot.org/annotation/VSP_023276
http://togogenome.org/gene/9606:SGPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX95                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Abolishes phosphatase activity.|||Basic and acidic residues|||Disordered|||Helical|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphoserine|||Phosphothreonine|||Proton donor|||Sphingosine-1-phosphate phosphatase 1|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114477
http://togogenome.org/gene/9606:PSMA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0X6|||http://purl.uniprot.org/uniprot/P25786                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform Long.|||N-acetylmethionine|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; alternate|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124060|||http://purl.uniprot.org/annotation/VAR_067454|||http://purl.uniprot.org/annotation/VSP_005279
http://togogenome.org/gene/9606:BMP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95393                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein 10|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033888|||http://purl.uniprot.org/annotation/PRO_0000033889|||http://purl.uniprot.org/annotation/VAR_052572|||http://purl.uniprot.org/annotation/VAR_052573
http://togogenome.org/gene/9606:MTERF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99551                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Interaction with DNA|||Mitochondrion|||Reduces affinity for cognate DNA; when associated with A-162 and A-243.|||Reduces affinity for cognate DNA; when associated with A-162 and A-288.|||Reduces affinity for cognate DNA; when associated with A-243 and A-288.|||Reduces transcription termination.|||Strongly reduces affinity for DNA. Strongly reduces transcription termination.|||Strongly reduces affinity for cognate DNA. Strongly reduces transcription termination.|||Strongly reduces transcription termination.|||Transcription termination factor 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021779|||http://purl.uniprot.org/annotation/VAR_024237|||http://purl.uniprot.org/annotation/VAR_053785
http://togogenome.org/gene/9606:HLA-DRB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2Z4LKS3|||http://purl.uniprot.org/uniprot/Q30154                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1|||Beta-2|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DR beta 5 chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DRB5*01:02, allele DRB5*01:03, allele DRB5*01:05, allele DRB5*01:14, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05.|||In allele DRB5*01:02, allele DRB5*01:03, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05.|||In allele DRB5*01:03.|||In allele DRB5*01:04; requires 2 nucleotide substitutions.|||In allele DRB5*01:06, allele DRB5*01:07, allele DRB5*01:11, allele DRB5*02:02 and allele DRB5*02:03.|||In allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03 and allele DRB5*02:04; requires 2 nucleotide substitutions.|||In allele DRB5*01:06, allele DRB5*01:11, allele DRB5*02:02, allele DRB5*02:03, allele DRB5*02:04 and allele DRB5*02:05; requires 2 nucleotide substitutions.|||In allele DRB5*01:06, allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05.|||In allele DRB5*01:09.|||In allele DRB5*01:12.|||In allele DRB5*01:12; requires 2 nucleotide substitutions.|||In allele DRB5*01:13.|||In allele DRB5*01:14.|||In allele DRB5*02:02, allele DRB5*02:04 and allele DRB5*02:05.|||In allele DRB5*02:02.|||In allele DRB5*02:02; requires 2 nucleotide substitutions.|||In allele DRB5*02:05.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000143106|||http://purl.uniprot.org/annotation/PRO_5033339605|||http://purl.uniprot.org/annotation/VAR_039871|||http://purl.uniprot.org/annotation/VAR_039872|||http://purl.uniprot.org/annotation/VAR_050355|||http://purl.uniprot.org/annotation/VAR_050356|||http://purl.uniprot.org/annotation/VAR_050357|||http://purl.uniprot.org/annotation/VAR_050358|||http://purl.uniprot.org/annotation/VAR_050359|||http://purl.uniprot.org/annotation/VAR_060951|||http://purl.uniprot.org/annotation/VAR_060952|||http://purl.uniprot.org/annotation/VAR_060953|||http://purl.uniprot.org/annotation/VAR_060954|||http://purl.uniprot.org/annotation/VAR_060955|||http://purl.uniprot.org/annotation/VAR_060956|||http://purl.uniprot.org/annotation/VAR_060958|||http://purl.uniprot.org/annotation/VAR_060959|||http://purl.uniprot.org/annotation/VAR_060960|||http://purl.uniprot.org/annotation/VAR_060961|||http://purl.uniprot.org/annotation/VAR_060962|||http://purl.uniprot.org/annotation/VAR_060963|||http://purl.uniprot.org/annotation/VAR_060964|||http://purl.uniprot.org/annotation/VAR_060965|||http://purl.uniprot.org/annotation/VAR_060966|||http://purl.uniprot.org/annotation/VAR_060967|||http://purl.uniprot.org/annotation/VAR_060968|||http://purl.uniprot.org/annotation/VAR_060969|||http://purl.uniprot.org/annotation/VAR_060970|||http://purl.uniprot.org/annotation/VAR_060971|||http://purl.uniprot.org/annotation/VAR_060972|||http://purl.uniprot.org/annotation/VAR_060973|||http://purl.uniprot.org/annotation/VAR_060974|||http://purl.uniprot.org/annotation/VAR_060975|||http://purl.uniprot.org/annotation/VAR_060976|||http://purl.uniprot.org/annotation/VAR_060977|||http://purl.uniprot.org/annotation/VAR_060978|||http://purl.uniprot.org/annotation/VAR_060979|||http://purl.uniprot.org/annotation/VAR_060980|||http://purl.uniprot.org/annotation/VAR_060981
http://togogenome.org/gene/9606:RRP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMR5|||http://purl.uniprot.org/uniprot/Q5JTH9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||RRP12-like protein|||Ribosomal RNA-processing protein 12-like conserved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050768|||http://purl.uniprot.org/annotation/VAR_057756|||http://purl.uniprot.org/annotation/VAR_057757|||http://purl.uniprot.org/annotation/VSP_014798|||http://purl.uniprot.org/annotation/VSP_045674
http://togogenome.org/gene/9606:TSPAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60635                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Loss of glycosylation.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219234|||http://purl.uniprot.org/annotation/VAR_034573|||http://purl.uniprot.org/annotation/VAR_052327
http://togogenome.org/gene/9606:FBXO25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCJ0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 25|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with beta-actin|||Loss of SKP1-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119911|||http://purl.uniprot.org/annotation/VAR_049043|||http://purl.uniprot.org/annotation/VAR_061167|||http://purl.uniprot.org/annotation/VSP_007374|||http://purl.uniprot.org/annotation/VSP_013060|||http://purl.uniprot.org/annotation/VSP_013061
http://togogenome.org/gene/9606:C21orf140                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A014                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Uncharacterized protein C21orf140                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415166
http://togogenome.org/gene/9606:CYP1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16678                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Associated with ocular hypertension susceptibility.|||Cytochrome P450 1B1|||In GLC3A and GLC1A; acts as GLC1A disease modifier in patients also carrying Val-399 mutation in MYOC.|||In GLC3A.|||In GLC3A; adult-onset.|||In GLC3A; adult-onset; hypomorphic allele; reduces the abundance of the enzyme.|||In GLC3A; allele CYP1B1*12; reduces enzymatic activity.|||In GLC3A; allele CYP1B1*18.|||In GLC3A; allele CYP1B1*20.|||In GLC3A; allele CYP1B1*21.|||In GLC3A; allele CYP1B1*23.|||In GLC3A; allele CYP1B1*25.|||In GLC3A; allele CYP1B1*7; unknown pathological significance.|||In GLC3A; juvenile onset; allele CYP1B1*11.|||In GLC3A; juvenile-onset.|||In GLC3A; juvenile-onset; hypomorphic allele; reduces the abundance of the enzyme.|||In GLC3A; reduces enzymatic activity and also the abundance of the enzyme.|||In GLC3A; reduces enzymatic activity.|||In GLC3A; requires 2 nucleotide substitutions; unknown pathological significance.|||In GLC3A; unknown pathological significance.|||In allele CYP1B1*19.|||In allele CYP1B1*2, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7.|||In allele CYP1B1*2, allele CYP1B1*6 and allele CYP1B1*7; significantly associated with breast or lung cancer; no significant change in 17beta-estradiol 2- and 4-hydroxylation activities and 17beta-estradiol affinity; 1.5-fold reduction in testosterone affinity but nearly no change in testosterone 6beta-hydroxylation activity; 2-fold increase in progesterone 6beta- and 16alpha-hydroxylation activities and 5-fold reduction in progesterone affinity.|||In allele CYP1B1*3, allele CYP1B1*5, allele CYP1B1*6 and allele CYP1B1*7; 1.6-fold increase in 17beta-estradiol 4-hydroxylation activity but no change in 17beta-estradiol 2-hydroxylation activity; 2-fold reduction in testosterone 6beta-hydroxylation activity and 3-fold reduction in testosterone affinity; 6-fold and 4-fold increase in progesterone 6beta- and 16alpha-hydroxylation activity, respectively and 7-fold reduction in progesterone affinity.|||In allele CYP1B1*4.|||Invertes the 4OHE2:2OHE2 hydroxylation preference from 5.1 to 0.45.|||Major determinant of CYP1B1 17beta-estradiol hydroxylation regiospecificity|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051660|||http://purl.uniprot.org/annotation/VAR_001244|||http://purl.uniprot.org/annotation/VAR_001245|||http://purl.uniprot.org/annotation/VAR_001246|||http://purl.uniprot.org/annotation/VAR_001247|||http://purl.uniprot.org/annotation/VAR_001248|||http://purl.uniprot.org/annotation/VAR_008350|||http://purl.uniprot.org/annotation/VAR_008351|||http://purl.uniprot.org/annotation/VAR_008352|||http://purl.uniprot.org/annotation/VAR_008353|||http://purl.uniprot.org/annotation/VAR_008354|||http://purl.uniprot.org/annotation/VAR_008355|||http://purl.uniprot.org/annotation/VAR_011752|||http://purl.uniprot.org/annotation/VAR_011753|||http://purl.uniprot.org/annotation/VAR_016034|||http://purl.uniprot.org/annotation/VAR_018774|||http://purl.uniprot.org/annotation/VAR_018869|||http://purl.uniprot.org/annotation/VAR_018870|||http://purl.uniprot.org/annotation/VAR_028735|||http://purl.uniprot.org/annotation/VAR_028736|||http://purl.uniprot.org/annotation/VAR_028737|||http://purl.uniprot.org/annotation/VAR_028738|||http://purl.uniprot.org/annotation/VAR_054227|||http://purl.uniprot.org/annotation/VAR_054228|||http://purl.uniprot.org/annotation/VAR_054229|||http://purl.uniprot.org/annotation/VAR_054230|||http://purl.uniprot.org/annotation/VAR_054231|||http://purl.uniprot.org/annotation/VAR_054232|||http://purl.uniprot.org/annotation/VAR_054233|||http://purl.uniprot.org/annotation/VAR_054234|||http://purl.uniprot.org/annotation/VAR_054235|||http://purl.uniprot.org/annotation/VAR_054236|||http://purl.uniprot.org/annotation/VAR_054237|||http://purl.uniprot.org/annotation/VAR_054238|||http://purl.uniprot.org/annotation/VAR_054239|||http://purl.uniprot.org/annotation/VAR_054240|||http://purl.uniprot.org/annotation/VAR_054241|||http://purl.uniprot.org/annotation/VAR_054242|||http://purl.uniprot.org/annotation/VAR_054243|||http://purl.uniprot.org/annotation/VAR_054244|||http://purl.uniprot.org/annotation/VAR_054245|||http://purl.uniprot.org/annotation/VAR_054246|||http://purl.uniprot.org/annotation/VAR_054247|||http://purl.uniprot.org/annotation/VAR_054248|||http://purl.uniprot.org/annotation/VAR_054249|||http://purl.uniprot.org/annotation/VAR_054250|||http://purl.uniprot.org/annotation/VAR_054251|||http://purl.uniprot.org/annotation/VAR_054252|||http://purl.uniprot.org/annotation/VAR_054253|||http://purl.uniprot.org/annotation/VAR_054254|||http://purl.uniprot.org/annotation/VAR_054255|||http://purl.uniprot.org/annotation/VAR_054256|||http://purl.uniprot.org/annotation/VAR_054257|||http://purl.uniprot.org/annotation/VAR_054258|||http://purl.uniprot.org/annotation/VAR_054259|||http://purl.uniprot.org/annotation/VAR_054260|||http://purl.uniprot.org/annotation/VAR_054261|||http://purl.uniprot.org/annotation/VAR_054262|||http://purl.uniprot.org/annotation/VAR_054263|||http://purl.uniprot.org/annotation/VAR_054264|||http://purl.uniprot.org/annotation/VAR_054265|||http://purl.uniprot.org/annotation/VAR_054266|||http://purl.uniprot.org/annotation/VAR_054267|||http://purl.uniprot.org/annotation/VAR_054268
http://togogenome.org/gene/9606:ISL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A47                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Insulin gene enhancer protein ISL-2|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM-binding domain (LID)|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075752
http://togogenome.org/gene/9606:RASGRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFL3|||http://purl.uniprot.org/uniprot/O14827|||http://purl.uniprot.org/uniprot/Q68DX5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DH|||Disordered|||IQ|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||Loss of phosphorylation by CDK5.|||N-terminal Ras-GEF|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphoserine; by CDK5|||Polar residues|||Ras-GEF|||Ras-specific guanine nucleotide-releasing factor 2|||Regulates proteasomal degradation|||Responsible of the affinity for farnesylated versus geranylgeranylated Ras                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312863|||http://purl.uniprot.org/annotation/VAR_037595|||http://purl.uniprot.org/annotation/VAR_037596|||http://purl.uniprot.org/annotation/VAR_037597|||http://purl.uniprot.org/annotation/VAR_037598
http://togogenome.org/gene/9606:NPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C0P6                                                                                  ^@                                                                                  Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Neuropeptide S                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042888|||http://purl.uniprot.org/annotation/PRO_0000042889|||http://purl.uniprot.org/annotation/VAR_051239|||http://purl.uniprot.org/annotation/VAR_051240
http://togogenome.org/gene/9606:F12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00748|||http://purl.uniprot.org/uniprot/Q8IZZ5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-factor XIIa part 1|||Charge relay system|||Coagulation factor XIIa heavy chain|||Coagulation factor XIIa light chain|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||Fibronectin type-I|||Fibronectin type-II|||In FA12D; CRM-negative phenotype.|||In FA12D; CRM-negative phenotype; accumulation in the cell; low secretion.|||In FA12D; CRM-negative phenotype; low levels of accumulation in the cell; not secreted.|||In FA12D; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted.|||In FA12D; CRM-positive phenotype.|||In FA12D; Locarno; inactive.|||In FA12D; Shizuoka; CRM-negative phenotype; transcribed and synthesized at wild-type levels; not secreted.|||In FA12D; Tenri; inactive.|||In FA12D; Washington D.C.; inactive.|||In HAE3.|||Kringle|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc) threonine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Peptidase S1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027833|||http://purl.uniprot.org/annotation/PRO_0000027834|||http://purl.uniprot.org/annotation/PRO_0000027835|||http://purl.uniprot.org/annotation/PRO_5004311537|||http://purl.uniprot.org/annotation/VAR_006623|||http://purl.uniprot.org/annotation/VAR_006624|||http://purl.uniprot.org/annotation/VAR_014336|||http://purl.uniprot.org/annotation/VAR_014337|||http://purl.uniprot.org/annotation/VAR_014338|||http://purl.uniprot.org/annotation/VAR_014426|||http://purl.uniprot.org/annotation/VAR_029191|||http://purl.uniprot.org/annotation/VAR_031500|||http://purl.uniprot.org/annotation/VAR_031501|||http://purl.uniprot.org/annotation/VAR_031502|||http://purl.uniprot.org/annotation/VAR_031503|||http://purl.uniprot.org/annotation/VAR_031504|||http://purl.uniprot.org/annotation/VAR_031505|||http://purl.uniprot.org/annotation/VAR_031506|||http://purl.uniprot.org/annotation/VAR_031507|||http://purl.uniprot.org/annotation/VAR_031508|||http://purl.uniprot.org/annotation/VAR_031509
http://togogenome.org/gene/9606:PLEKHM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4G2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Disrupts interaction with RAB7A.|||Disrupts interaction with Rab7 and no localization to endososmal membranes; when associated with G-1021, G-1024 and G-1032.|||Disrupts interaction with Rab7 and no localization to endososmal membranes; when associated with G-1021, L-1029 and G-1032.|||Disrupts interaction with Rab7 and no localization to endososmal membranes; when associated with G-1024, L-1029 and G-1032.|||Disrupts interaction with Rab7and no localization to endososmal membranes; when associated with G-1021, G-1024 and L-1029.|||In OPTA3; unknown pathological significance.|||Interaction with RAB7A|||LIR|||No effect on interaction with ARL8B. No effect on interaction with RAB7A.|||PH 1|||PH 2|||Phorbol-ester/DAG-type|||Phosphoserine|||Pleckstrin homology domain-containing family M member 1|||Polar residues|||RUN|||Reduces interaction with ARL8B. No effect on interaction with RAB7A. Loss of interaction with ARL8B as well as late endosome and lysosome clustering; when associated with A-60.|||Strongly reduces interaction with ARL8B. No effect on interaction with RAB7A. No effect on late endosome and lysosome clustering. Loss of interaction with ARL8B as well as late endosome and lysosome clustering; when associated with 119-A--A-123.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309335|||http://purl.uniprot.org/annotation/VAR_036932|||http://purl.uniprot.org/annotation/VAR_081102
http://togogenome.org/gene/9606:TASL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAI6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site                                                                                  ^@                                                                                  Abolished ability to activate IRF5.|||Phosphomimetic mutant; retains ability to activate IRF5.|||Phosphoserine|||TLR adapter interacting with SLC15A4 on the lysosome|||pLxIS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251252
http://togogenome.org/gene/9606:ZNF665                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7R5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 665                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325613|||http://purl.uniprot.org/annotation/VAR_039895|||http://purl.uniprot.org/annotation/VAR_039896|||http://purl.uniprot.org/annotation/VAR_039897
http://togogenome.org/gene/9606:CAV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A9XTE5|||http://purl.uniprot.org/uniprot/Q03135|||http://purl.uniprot.org/uniprot/Q2TNI1|||http://purl.uniprot.org/uniprot/Q59E85|||http://purl.uniprot.org/uniprot/Q7Z4F3                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||INTRAMEM|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Caveolin-1|||Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical|||In breast cancer; seems to form misfolded oligomers that are retained within the Golgi complex and are not targeted to caveolae or the plasma membrane; loss of interaction with VCP.|||In isoform 2.|||Interaction with CAVIN3|||Interacts with SPRY1, SPRY2, SPRY3 and SPRY4|||Interacts with SPRY1, SPRY2, and SPRY4|||N-acetylalanine|||N-acetylserine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Removed|||Required for homooligomerization|||Resistance to ZNRF1-mediated degradation.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004764|||http://purl.uniprot.org/annotation/VAR_015103|||http://purl.uniprot.org/annotation/VSP_018692
http://togogenome.org/gene/9606:TAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16559                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||T-cell acute lymphocytic leukemia protein 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127456
http://togogenome.org/gene/9606:PALM2AKAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2D5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 1.|||In isoform 2 and isoform 5.|||In isoform 2, isoform 1 and isoform 4.|||In isoform 6.|||In isoform 7.|||PALM2-AKAP2 fusion protein|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064524|||http://purl.uniprot.org/annotation/VAR_024248|||http://purl.uniprot.org/annotation/VSP_062014|||http://purl.uniprot.org/annotation/VSP_062015|||http://purl.uniprot.org/annotation/VSP_062016|||http://purl.uniprot.org/annotation/VSP_062017|||http://purl.uniprot.org/annotation/VSP_062018|||http://purl.uniprot.org/annotation/VSP_062019|||http://purl.uniprot.org/annotation/VSP_062020|||http://purl.uniprot.org/annotation/VSP_062021|||http://purl.uniprot.org/annotation/VSP_062022
http://togogenome.org/gene/9606:LRCH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DU23|||http://purl.uniprot.org/uniprot/Q96II8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||DISP complex protein LRCH3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Mediates direct interaction with MYO6|||Mediates interaction with DOCK7|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253484|||http://purl.uniprot.org/annotation/VAR_056931|||http://purl.uniprot.org/annotation/VSP_021043|||http://purl.uniprot.org/annotation/VSP_021044|||http://purl.uniprot.org/annotation/VSP_057212|||http://purl.uniprot.org/annotation/VSP_057213
http://togogenome.org/gene/9606:KCNG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32MC1|||http://purl.uniprot.org/uniprot/Q547S7|||http://purl.uniprot.org/uniprot/Q8TDN1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||Ion transport|||Potassium channel tetramerisation-type BTB|||Potassium voltage-gated channel subfamily G member 4|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054080|||http://purl.uniprot.org/annotation/VAR_053861|||http://purl.uniprot.org/annotation/VAR_053862|||http://purl.uniprot.org/annotation/VAR_053863|||http://purl.uniprot.org/annotation/VAR_053864|||http://purl.uniprot.org/annotation/VAR_053865|||http://purl.uniprot.org/annotation/VAR_053866|||http://purl.uniprot.org/annotation/VSP_001029|||http://purl.uniprot.org/annotation/VSP_001030
http://togogenome.org/gene/9606:CATSPERB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWW9|||http://purl.uniprot.org/uniprot/Q9H7T0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit beta|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089953|||http://purl.uniprot.org/annotation/VAR_061634|||http://purl.uniprot.org/annotation/VSP_027008
http://togogenome.org/gene/9606:KCNH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS40                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Phosphoserine|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 7|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054015|||http://purl.uniprot.org/annotation/VAR_057767|||http://purl.uniprot.org/annotation/VSP_037116|||http://purl.uniprot.org/annotation/VSP_037117|||http://purl.uniprot.org/annotation/VSP_037118
http://togogenome.org/gene/9606:BICDL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A5D9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BICD family-like cargo adapter 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302861|||http://purl.uniprot.org/annotation/VAR_034978|||http://purl.uniprot.org/annotation/VAR_060543|||http://purl.uniprot.org/annotation/VSP_027976
http://togogenome.org/gene/9606:SPATA18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKF4|||http://purl.uniprot.org/uniprot/Q8TC71                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mitochondria-eating protein|||Mitochondria-eating protein C-terminal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254165|||http://purl.uniprot.org/annotation/VAR_028828|||http://purl.uniprot.org/annotation/VAR_028829|||http://purl.uniprot.org/annotation/VSP_041048
http://togogenome.org/gene/9606:TLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLW3|||http://purl.uniprot.org/uniprot/O43897                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||In ASD6.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M12A|||Tolloid-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046023|||http://purl.uniprot.org/annotation/PRO_0000046024|||http://purl.uniprot.org/annotation/VAR_036142|||http://purl.uniprot.org/annotation/VAR_051585|||http://purl.uniprot.org/annotation/VAR_062519|||http://purl.uniprot.org/annotation/VAR_062520|||http://purl.uniprot.org/annotation/VAR_062521|||http://purl.uniprot.org/annotation/VSP_017197|||http://purl.uniprot.org/annotation/VSP_017198
http://togogenome.org/gene/9606:AFG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV93                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site                                                                                  ^@                                                                                  AFG1-like ATPase|||Does not affect mitochondrial targeting. Increased amount of unprocessed protein form. Fails to rescue the increased accumulation of complex IV subunits in AFG1L-deficient cell line. Reduces mitochondrial targeting; when associated with V-143.|||Does not affect subcellular location. Fails to rescue the increased accumulation of complex IV subunits in AFG1L-deficient cell line.|||Reduces mitochondrial targeting. Increased amount of unprocessed protein form. Reduces mitochondrial targeting; when associated with A-142.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279521
http://togogenome.org/gene/9606:AVPR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47901                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Vasopressin V1b receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070203|||http://purl.uniprot.org/annotation/VAR_025159|||http://purl.uniprot.org/annotation/VAR_025160|||http://purl.uniprot.org/annotation/VAR_025161|||http://purl.uniprot.org/annotation/VAR_025162|||http://purl.uniprot.org/annotation/VAR_061228
http://togogenome.org/gene/9606:HECTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2H1|||http://purl.uniprot.org/uniprot/A0A8I5QJU2|||http://purl.uniprot.org/uniprot/H0YJD4|||http://purl.uniprot.org/uniprot/Q9ULT8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Abolished E3 ubiquitin-protein ligase activity.|||Acidic residues|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase HECTD1|||Glycyl thioester intermediate|||HECT|||K-box|||MIB/HERC2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083945|||http://purl.uniprot.org/annotation/VAR_059666|||http://purl.uniprot.org/annotation/VAR_067707
http://togogenome.org/gene/9606:ELL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||OCEL|||Polar residues|||RNA polymerase II elongation factor ELL3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146736|||http://purl.uniprot.org/annotation/VAR_018992|||http://purl.uniprot.org/annotation/VAR_053074|||http://purl.uniprot.org/annotation/VSP_045937
http://togogenome.org/gene/9606:DPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07507                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1-1|||1-2|||2 X 53-55 AA tandem repeats|||2-1|||2-2|||3 X 6 AA repeats of D-R-[EQ]-W-[NQK]-[FY]|||3-3|||Dermatopontin|||Or C-106 with C-132|||Or C-90 with C-133|||Pyrrolidone carboxylic acid|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007368|||http://purl.uniprot.org/annotation/VAR_048888
http://togogenome.org/gene/9606:ETNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVF9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ethanolamine kinase 2|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206229|||http://purl.uniprot.org/annotation/VAR_022145|||http://purl.uniprot.org/annotation/VSP_039098|||http://purl.uniprot.org/annotation/VSP_039558
http://togogenome.org/gene/9606:PFDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60925                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylalanine|||Prefoldin subunit 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124830
http://togogenome.org/gene/9606:RIMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7W2|||http://purl.uniprot.org/uniprot/B7Z9Z3|||http://purl.uniprot.org/uniprot/Q3ZCW0|||http://purl.uniprot.org/uniprot/Q86UR5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with SYT1 and CACNA1B.|||Basic and acidic residues|||C2|||C2 1|||C2 2|||Disordered|||FYVE-type|||In CORD7.|||In isoform 10.|||In isoform 11.|||In isoform 12 and isoform 13.|||In isoform 2.|||In isoform 3, isoform 4, isoform 7 and isoform 13.|||In isoform 3, isoform 6, isoform 7, isoform 9, isoform 10, isoform 12 and isoform 13.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 7, isoform 8 and isoform 12.|||In isoform 5.|||In isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 13.|||In isoform 6.|||In isoform 8.|||In isoform 9, isoform 10 and isoform 12.|||In isoform 9.|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||RabBD|||Regulating synaptic membrane exocytosis protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190198|||http://purl.uniprot.org/annotation/PRO_5002863941|||http://purl.uniprot.org/annotation/VAR_016804|||http://purl.uniprot.org/annotation/VSP_008161|||http://purl.uniprot.org/annotation/VSP_008162|||http://purl.uniprot.org/annotation/VSP_008163|||http://purl.uniprot.org/annotation/VSP_008164|||http://purl.uniprot.org/annotation/VSP_008165|||http://purl.uniprot.org/annotation/VSP_008166|||http://purl.uniprot.org/annotation/VSP_008167|||http://purl.uniprot.org/annotation/VSP_008168|||http://purl.uniprot.org/annotation/VSP_008169|||http://purl.uniprot.org/annotation/VSP_008170|||http://purl.uniprot.org/annotation/VSP_008171|||http://purl.uniprot.org/annotation/VSP_043177|||http://purl.uniprot.org/annotation/VSP_043178|||http://purl.uniprot.org/annotation/VSP_043179|||http://purl.uniprot.org/annotation/VSP_043180|||http://purl.uniprot.org/annotation/VSP_045485|||http://purl.uniprot.org/annotation/VSP_045486|||http://purl.uniprot.org/annotation/VSP_046796
http://togogenome.org/gene/9606:USP36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P275                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes deubiquitinase activity. No effect on NTRK1 ubiquitination levels.|||Basic and acidic residues|||Disordered|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080666|||http://purl.uniprot.org/annotation/VAR_037277|||http://purl.uniprot.org/annotation/VAR_037278|||http://purl.uniprot.org/annotation/VAR_037279|||http://purl.uniprot.org/annotation/VAR_037280|||http://purl.uniprot.org/annotation/VAR_037281|||http://purl.uniprot.org/annotation/VAR_037282|||http://purl.uniprot.org/annotation/VAR_058034|||http://purl.uniprot.org/annotation/VAR_080193
http://togogenome.org/gene/9606:JAGN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5M9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In SCN6.|||Lumenal|||Phosphoserine|||Protein jagunal homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313608|||http://purl.uniprot.org/annotation/VAR_071795|||http://purl.uniprot.org/annotation/VAR_071796|||http://purl.uniprot.org/annotation/VAR_071797|||http://purl.uniprot.org/annotation/VAR_071798|||http://purl.uniprot.org/annotation/VAR_071799
http://togogenome.org/gene/9606:SLC17A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2C5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of glycosylation and significant reduction in the tranport of thyroid hormones T3 and T4; when associated with A-66 and A-90.|||Loss of glycosylation and significant reduction in the tranport of thyroid hormones T3 and T4; when associated with A-75 and A-90.|||N-linked (GlcNAc...) asparagine|||Probable small intestine urate exporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318166|||http://purl.uniprot.org/annotation/VAR_038709|||http://purl.uniprot.org/annotation/VSP_031178|||http://purl.uniprot.org/annotation/VSP_054938|||http://purl.uniprot.org/annotation/VSP_054939|||http://purl.uniprot.org/annotation/VSP_054940|||http://purl.uniprot.org/annotation/VSP_054941
http://togogenome.org/gene/9606:TTLL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14679                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased binding to microtubules and polyglutamylase activity.|||Disordered|||Essential for specifying initiation versus elongation step of the polyglutamylase activity|||Phosphoserine|||Polar residues|||TTL|||Tubulin monoglutamylase TTLL4|||c-MTBD region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212442|||http://purl.uniprot.org/annotation/VAR_013140|||http://purl.uniprot.org/annotation/VAR_031464|||http://purl.uniprot.org/annotation/VAR_031465|||http://purl.uniprot.org/annotation/VAR_031466|||http://purl.uniprot.org/annotation/VAR_031467|||http://purl.uniprot.org/annotation/VAR_031468|||http://purl.uniprot.org/annotation/VAR_031469|||http://purl.uniprot.org/annotation/VAR_057315
http://togogenome.org/gene/9606:EIF2S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20042|||http://purl.uniprot.org/uniprot/Q6IBR8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C4-type|||Disordered|||Eukaryotic translation initiation factor 2 subunit 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Translation initiation factor IF2/IF5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137406|||http://purl.uniprot.org/annotation/VAR_048909
http://togogenome.org/gene/9606:ZNF467                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JAX3|||http://purl.uniprot.org/uniprot/Q7Z7K2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Zinc finger protein 467                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247517|||http://purl.uniprot.org/annotation/VAR_052835
http://togogenome.org/gene/9606:FRG2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FRG2-like-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300692|||http://purl.uniprot.org/annotation/VAR_060156|||http://purl.uniprot.org/annotation/VAR_060157
http://togogenome.org/gene/9606:PRR23E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N813                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 23E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242665
http://togogenome.org/gene/9606:STAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75886                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ITAM|||In isoform 2.|||Interaction with HGS|||Interaction with USP8|||Polar residues|||PxVxL motif|||SH3|||Signal transducing adapter molecule 2|||UIM|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190147|||http://purl.uniprot.org/annotation/VSP_014848
http://togogenome.org/gene/9606:MYRIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Myosin-binding|||Negative regulation of PKA-binding|||PKA-binding|||Phosphoserine|||Polar residues|||Rab effector MyRIP|||RabBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190224|||http://purl.uniprot.org/annotation/VAR_051717|||http://purl.uniprot.org/annotation/VAR_061755|||http://purl.uniprot.org/annotation/VAR_061756|||http://purl.uniprot.org/annotation/VSP_043539|||http://purl.uniprot.org/annotation/VSP_043540|||http://purl.uniprot.org/annotation/VSP_043541|||http://purl.uniprot.org/annotation/VSP_043542|||http://purl.uniprot.org/annotation/VSP_043543|||http://purl.uniprot.org/annotation/VSP_054896|||http://purl.uniprot.org/annotation/VSP_054897
http://togogenome.org/gene/9606:PEX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28328                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=TM1|||Helical; Name=TM2|||Helical; Name=TM3|||Helical; Name=TM4|||Helical; Name=TM5|||In PBD5A.|||In PBD5B and PBD5A.|||In PBD5B.|||In PBD5B; infantile Refsum disease.|||N6-acetyllysine|||Peroxisomal matrix|||Peroxisome biogenesis factor 2|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056369|||http://purl.uniprot.org/annotation/VAR_011389|||http://purl.uniprot.org/annotation/VAR_060784|||http://purl.uniprot.org/annotation/VAR_087141|||http://purl.uniprot.org/annotation/VAR_087142|||http://purl.uniprot.org/annotation/VAR_087143|||http://purl.uniprot.org/annotation/VAR_087144
http://togogenome.org/gene/9606:ZNF534                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1T7F5|||http://purl.uniprot.org/uniprot/Q1T7F6|||http://purl.uniprot.org/uniprot/Q76KX8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 534                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394145|||http://purl.uniprot.org/annotation/VSP_039177
http://togogenome.org/gene/9606:SYNGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43760                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||MARVEL|||N-acetylmethionine|||Phosphoserine|||Synaptogyrin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183993|||http://purl.uniprot.org/annotation/VSP_056179
http://togogenome.org/gene/9606:SEC22A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IW7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Longin|||Lumenal|||N-acetylserine|||Phosphoserine|||Removed|||Vesicle-trafficking protein SEC22a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253043
http://togogenome.org/gene/9606:OIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWZ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like; calcium-binding|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Oncoprotein-induced transcript 3 protein|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298931|||http://purl.uniprot.org/annotation/VAR_034742|||http://purl.uniprot.org/annotation/VSP_027482|||http://purl.uniprot.org/annotation/VSP_027483
http://togogenome.org/gene/9606:CENPW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EE01                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand                                                                                  ^@                                                                                  Centromere protein W|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311183|||http://purl.uniprot.org/annotation/VSP_055708
http://togogenome.org/gene/9606:TMEM132C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3T6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324577|||http://purl.uniprot.org/annotation/VAR_039832|||http://purl.uniprot.org/annotation/VAR_039833|||http://purl.uniprot.org/annotation/VAR_039834|||http://purl.uniprot.org/annotation/VAR_039835|||http://purl.uniprot.org/annotation/VAR_039836|||http://purl.uniprot.org/annotation/VAR_039837|||http://purl.uniprot.org/annotation/VAR_039838
http://togogenome.org/gene/9606:ABCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33897                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 1|||Does not affect ACOT activity. Transport activity of VLCFA is strongly reduced.|||Does not affect PEX19 interaction.|||Does not affect fatty acid beta-oxidation.|||Helical|||Impairs PEX19 interaction.|||In ALD.|||In ALD; ACALD and CALD-types.|||In ALD; ACALD type.|||In ALD; AD-type.|||In ALD; ADO and AMN-types with cerebral involvement.|||In ALD; ADO-type.|||In ALD; ALD and AMN-types; does not affect protein stability, homo- and heterodimerization with ABCD2 and ABCD3.|||In ALD; ALD-type and asymptomatic.|||In ALD; ALD-type.|||In ALD; ALD/AMN/ADO-types and asymptomatic.|||In ALD; AMN and ALMD-types.|||In ALD; AMN-type.|||In ALD; AMN-type; significantly decreases homodimerization and abolishes heterodimerization with ABCD2 and ABCD3.|||In ALD; CALD and AMN-types.|||In ALD; CALD and AS-types; reduced ATPase activity.|||In ALD; CALD type.|||In ALD; CALD, ALMD and AS-types.|||In ALD; CALD, AMN and AD-types.|||In ALD; CALD, AMN and ADO-types; significantly decreases homodimerization and abolishes heterodimerization with ABCD2 and ABCD3.|||In ALD; CALD, AMN and ALMD-types.|||In ALD; CALD-type and AMN-type.|||In ALD; CALD-type.|||In ALD; CALD-types.|||In ALD; asymptomatic.|||In ALD; decreased ATP-binding affinity.|||In ALD; does not affect protein stability, homo- and heterodimerization with ABCD2 and ABCD3.|||In ALD; not able to restore defective beta-oxidation in fibroblast from patients with ALD.|||In ALD; unknown pathological significance.|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine|||PEX19 binding site and required for peroxisomal targeting|||Phosphoserine|||Required for homodimerization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093304|||http://purl.uniprot.org/annotation/VAR_000024|||http://purl.uniprot.org/annotation/VAR_000025|||http://purl.uniprot.org/annotation/VAR_000026|||http://purl.uniprot.org/annotation/VAR_000027|||http://purl.uniprot.org/annotation/VAR_000028|||http://purl.uniprot.org/annotation/VAR_000029|||http://purl.uniprot.org/annotation/VAR_000030|||http://purl.uniprot.org/annotation/VAR_000032|||http://purl.uniprot.org/annotation/VAR_000033|||http://purl.uniprot.org/annotation/VAR_000034|||http://purl.uniprot.org/annotation/VAR_000035|||http://purl.uniprot.org/annotation/VAR_000037|||http://purl.uniprot.org/annotation/VAR_000038|||http://purl.uniprot.org/annotation/VAR_000039|||http://purl.uniprot.org/annotation/VAR_000040|||http://purl.uniprot.org/annotation/VAR_000041|||http://purl.uniprot.org/annotation/VAR_000043|||http://purl.uniprot.org/annotation/VAR_000044|||http://purl.uniprot.org/annotation/VAR_000045|||http://purl.uniprot.org/annotation/VAR_000046|||http://purl.uniprot.org/annotation/VAR_000047|||http://purl.uniprot.org/annotation/VAR_000048|||http://purl.uniprot.org/annotation/VAR_000049|||http://purl.uniprot.org/annotation/VAR_000050|||http://purl.uniprot.org/annotation/VAR_000051|||http://purl.uniprot.org/annotation/VAR_000052|||http://purl.uniprot.org/annotation/VAR_000053|||http://purl.uniprot.org/annotation/VAR_000054|||http://purl.uniprot.org/annotation/VAR_000055|||http://purl.uniprot.org/annotation/VAR_000056|||http://purl.uniprot.org/annotation/VAR_000057|||http://purl.uniprot.org/annotation/VAR_000058|||http://purl.uniprot.org/annotation/VAR_000059|||http://purl.uniprot.org/annotation/VAR_000060|||http://purl.uniprot.org/annotation/VAR_000061|||http://purl.uniprot.org/annotation/VAR_000062|||http://purl.uniprot.org/annotation/VAR_000063|||http://purl.uniprot.org/annotation/VAR_000064|||http://purl.uniprot.org/annotation/VAR_000065|||http://purl.uniprot.org/annotation/VAR_000066|||http://purl.uniprot.org/annotation/VAR_000067|||http://purl.uniprot.org/annotation/VAR_000068|||http://purl.uniprot.org/annotation/VAR_000069|||http://purl.uniprot.org/annotation/VAR_000070|||http://purl.uniprot.org/annotation/VAR_000071|||http://purl.uniprot.org/annotation/VAR_000072|||http://purl.uniprot.org/annotation/VAR_000073|||http://purl.uniprot.org/annotation/VAR_000074|||http://purl.uniprot.org/annotation/VAR_000075|||http://purl.uniprot.org/annotation/VAR_000076|||http://purl.uniprot.org/annotation/VAR_000077|||http://purl.uniprot.org/annotation/VAR_000078|||http://purl.uniprot.org/annotation/VAR_000079|||http://purl.uniprot.org/annotation/VAR_000080|||http://purl.uniprot.org/annotation/VAR_000081|||http://purl.uniprot.org/annotation/VAR_000082|||http://purl.uniprot.org/annotation/VAR_000083|||http://purl.uniprot.org/annotation/VAR_000084|||http://purl.uniprot.org/annotation/VAR_000085|||http://purl.uniprot.org/annotation/VAR_000086|||http://purl.uniprot.org/annotation/VAR_000087|||http://purl.uniprot.org/annotation/VAR_000088|||http://purl.uniprot.org/annotation/VAR_000089|||http://purl.uniprot.org/annotation/VAR_000090|||http://purl.uniprot.org/annotation/VAR_009349|||http://purl.uniprot.org/annotation/VAR_009350|||http://purl.uniprot.org/annotation/VAR_009351|||http://purl.uniprot.org/annotation/VAR_009352|||http://purl.uniprot.org/annotation/VAR_009353|||http://purl.uniprot.org/annotation/VAR_009354|||http://purl.uniprot.org/annotation/VAR_009355|||http://purl.uniprot.org/annotation/VAR_009356|||http://purl.uniprot.org/annotation/VAR_009357|||http://purl.uniprot.org/annotation/VAR_009358|||http://purl.uniprot.org/annotation/VAR_009359|||http://purl.uniprot.org/annotation/VAR_009360|||http://purl.uniprot.org/annotation/VAR_009361|||http://purl.uniprot.org/annotation/VAR_009362|||http://purl.uniprot.org/annotation/VAR_009363|||http://purl.uniprot.org/annotation/VAR_009364|||http://purl.uniprot.org/annotation/VAR_009365|||http://purl.uniprot.org/annotation/VAR_009366|||http://purl.uniprot.org/annotation/VAR_009367|||http://purl.uniprot.org/annotation/VAR_009368|||http://purl.uniprot.org/annotation/VAR_009369|||http://purl.uniprot.org/annotation/VAR_009370|||http://purl.uniprot.org/annotation/VAR_009371|||http://purl.uniprot.org/annotation/VAR_009372|||http://purl.uniprot.org/annotation/VAR_009373|||http://purl.uniprot.org/annotation/VAR_009374|||http://purl.uniprot.org/annotation/VAR_009375|||http://purl.uniprot.org/annotation/VAR_009376|||http://purl.uniprot.org/annotation/VAR_009377|||http://purl.uniprot.org/annotation/VAR_009378|||http://purl.uniprot.org/annotation/VAR_009379|||http://purl.uniprot.org/annotation/VAR_009380|||http://purl.uniprot.org/annotation/VAR_009381|||http://purl.uniprot.org/annotation/VAR_009382|||http://purl.uniprot.org/annotation/VAR_009383|||http://purl.uniprot.org/annotation/VAR_009384|||http://purl.uniprot.org/annotation/VAR_009385|||http://purl.uniprot.org/annotation/VAR_009386|||http://purl.uniprot.org/annotation/VAR_009387|||http://purl.uniprot.org/annotation/VAR_009388|||http://purl.uniprot.org/annotation/VAR_009389|||http://purl.uniprot.org/annotation/VAR_009390|||http://purl.uniprot.org/annotation/VAR_009391|||http://purl.uniprot.org/annotation/VAR_009392|||http://purl.uniprot.org/annotation/VAR_009393|||http://purl.uniprot.org/annotation/VAR_013340|||http://purl.uniprot.org/annotation/VAR_013341|||http://purl.uniprot.org/annotation/VAR_013342|||http://purl.uniprot.org/annotation/VAR_013343|||http://purl.uniprot.org/annotation/VAR_013344|||http://purl.uniprot.org/annotation/VAR_013345|||http://purl.uniprot.org/annotation/VAR_013346|||http://purl.uniprot.org/annotation/VAR_013347|||http://purl.uniprot.org/annotation/VAR_013348|||http://purl.uniprot.org/annotation/VAR_013349|||http://purl.uniprot.org/annotation/VAR_013350|||http://purl.uniprot.org/annotation/VAR_013351|||http://purl.uniprot.org/annotation/VAR_013352|||http://purl.uniprot.org/annotation/VAR_013353|||http://purl.uniprot.org/annotation/VAR_013354|||http://purl.uniprot.org/annotation/VAR_013355|||http://purl.uniprot.org/annotation/VAR_013356|||http://purl.uniprot.org/annotation/VAR_013357|||http://purl.uniprot.org/annotation/VAR_013358|||http://purl.uniprot.org/annotation/VAR_013359|||http://purl.uniprot.org/annotation/VAR_013360|||http://purl.uniprot.org/annotation/VAR_067239|||http://purl.uniprot.org/annotation/VAR_067240|||http://purl.uniprot.org/annotation/VAR_067241|||http://purl.uniprot.org/annotation/VAR_067242|||http://purl.uniprot.org/annotation/VAR_067243|||http://purl.uniprot.org/annotation/VAR_067244|||http://purl.uniprot.org/annotation/VAR_067245|||http://purl.uniprot.org/annotation/VAR_067246|||http://purl.uniprot.org/annotation/VAR_067328|||http://purl.uniprot.org/annotation/VAR_067329|||http://purl.uniprot.org/annotation/VAR_075284|||http://purl.uniprot.org/annotation/VAR_075285
http://togogenome.org/gene/9606:FREM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CSPG 1|||CSPG 10|||CSPG 11|||CSPG 12|||CSPG 2|||CSPG 3|||CSPG 4|||CSPG 5|||CSPG 6|||CSPG 7|||CSPG 8|||CSPG 9|||Calx-beta 1|||Calx-beta 2|||Calx-beta 3|||Calx-beta 4|||Calx-beta 5|||Cytoplasmic|||Disordered|||Extracellular|||FRAS1-related extracellular matrix protein 2|||Helical|||In CRYPTOP and FRASRS2; decreases cell adhesion; decreases interaction with FREM1.|||In CRYPTOP.|||In FRASRS2; may impair calcium-binding in the 2nd Calx-beta domain; decreases cell adhesion; decreases interaction with FREM1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010124|||http://purl.uniprot.org/annotation/VAR_023201|||http://purl.uniprot.org/annotation/VAR_023202|||http://purl.uniprot.org/annotation/VAR_023203|||http://purl.uniprot.org/annotation/VAR_023204|||http://purl.uniprot.org/annotation/VAR_033933|||http://purl.uniprot.org/annotation/VAR_033934|||http://purl.uniprot.org/annotation/VAR_033935|||http://purl.uniprot.org/annotation/VAR_033936|||http://purl.uniprot.org/annotation/VAR_033937|||http://purl.uniprot.org/annotation/VAR_037569|||http://purl.uniprot.org/annotation/VAR_037570|||http://purl.uniprot.org/annotation/VAR_037571|||http://purl.uniprot.org/annotation/VAR_061174|||http://purl.uniprot.org/annotation/VAR_061175|||http://purl.uniprot.org/annotation/VAR_082581|||http://purl.uniprot.org/annotation/VAR_082582|||http://purl.uniprot.org/annotation/VAR_082583|||http://purl.uniprot.org/annotation/VAR_082584|||http://purl.uniprot.org/annotation/VSP_015035|||http://purl.uniprot.org/annotation/VSP_015036
http://togogenome.org/gene/9606:C18orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32NC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||UPF0711 protein C18orf21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279448|||http://purl.uniprot.org/annotation/VAR_030903|||http://purl.uniprot.org/annotation/VSP_055184
http://togogenome.org/gene/9606:LRRC30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NM36                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 30|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310986
http://togogenome.org/gene/9606:GDF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75RY1|||http://purl.uniprot.org/uniprot/Q7Z4P5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Growth/differentiation factor 7|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033922|||http://purl.uniprot.org/annotation/PRO_0000033923|||http://purl.uniprot.org/annotation/PRO_5004285948
http://togogenome.org/gene/9606:CHM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K545|||http://purl.uniprot.org/uniprot/B4DRL9|||http://purl.uniprot.org/uniprot/P24386                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes prenylation of RAB1A and association with RGGT.|||Disordered|||Impairs prenylation of RAB1A and abolishes association with RGGT.|||In CHM.|||In CHM; impairs the interaction with RABGGTA.|||In CHM; may affect splicing.|||In isoform 2.|||Polar residues|||Rab proteins geranylgeranyltransferase component A 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056686|||http://purl.uniprot.org/annotation/VAR_008273|||http://purl.uniprot.org/annotation/VAR_066847|||http://purl.uniprot.org/annotation/VAR_066848|||http://purl.uniprot.org/annotation/VSP_042817|||http://purl.uniprot.org/annotation/VSP_042818
http://togogenome.org/gene/9606:TMPRSS11D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60235                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (between non-catalytic and catalytic chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 11D catalytic chain|||Transmembrane protease serine 11D non-catalytic chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027885|||http://purl.uniprot.org/annotation/PRO_0000027886
http://togogenome.org/gene/9606:PRPF38B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTL8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Pre-mRNA-splicing factor 38B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287235|||http://purl.uniprot.org/annotation/VSP_025408|||http://purl.uniprot.org/annotation/VSP_025409
http://togogenome.org/gene/9606:KLKB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9A9|||http://purl.uniprot.org/uniprot/B4DMX2|||http://purl.uniprot.org/uniprot/E9PBC5|||http://purl.uniprot.org/uniprot/P03952                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Apple|||Apple 1|||Apple 2|||Apple 3|||Apple 4|||Charge relay system|||In PKKD.|||In PKKD; reduces the binding activity of Apple domain 2 to HMW kininogen.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Plasma kallikrein heavy chain|||Plasma kallikrein light chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028021|||http://purl.uniprot.org/annotation/PRO_0000028022|||http://purl.uniprot.org/annotation/PRO_5002725522|||http://purl.uniprot.org/annotation/VAR_013598|||http://purl.uniprot.org/annotation/VAR_013599|||http://purl.uniprot.org/annotation/VAR_013600|||http://purl.uniprot.org/annotation/VAR_016280|||http://purl.uniprot.org/annotation/VAR_016281|||http://purl.uniprot.org/annotation/VAR_016282|||http://purl.uniprot.org/annotation/VAR_016283|||http://purl.uniprot.org/annotation/VAR_016284|||http://purl.uniprot.org/annotation/VAR_016285|||http://purl.uniprot.org/annotation/VAR_016286|||http://purl.uniprot.org/annotation/VAR_020180|||http://purl.uniprot.org/annotation/VAR_054907|||http://purl.uniprot.org/annotation/VAR_054908
http://togogenome.org/gene/9606:MRPL52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9P5|||http://purl.uniprot.org/uniprot/Q86TS9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Large ribosomal subunit protein mL52|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273093|||http://purl.uniprot.org/annotation/PRO_5003475785|||http://purl.uniprot.org/annotation/VAR_030080|||http://purl.uniprot.org/annotation/VAR_030081|||http://purl.uniprot.org/annotation/VAR_052044|||http://purl.uniprot.org/annotation/VSP_044560|||http://purl.uniprot.org/annotation/VSP_045242|||http://purl.uniprot.org/annotation/VSP_054094|||http://purl.uniprot.org/annotation/VSP_054095
http://togogenome.org/gene/9606:SCAMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK92|||http://purl.uniprot.org/uniprot/A8K769|||http://purl.uniprot.org/uniprot/O15127                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Interaction with SLC9A7|||Lumenal|||Phosphoserine|||Polar residues|||Secretory carrier-associated membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191254
http://togogenome.org/gene/9606:TMEM39B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRL9|||http://purl.uniprot.org/uniprot/Q9BT39|||http://purl.uniprot.org/uniprot/Q9GZU3|||http://purl.uniprot.org/uniprot/Q9NW51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 39B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279232|||http://purl.uniprot.org/annotation/VSP_056123|||http://purl.uniprot.org/annotation/VSP_056124|||http://purl.uniprot.org/annotation/VSP_056125|||http://purl.uniprot.org/annotation/VSP_056126|||http://purl.uniprot.org/annotation/VSP_056127|||http://purl.uniprot.org/annotation/VSP_056128
http://togogenome.org/gene/9606:GOLPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4A6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-171 or L-171.|||Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-174.|||Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-81.|||Abolishes phosphoinositide binding and localization to the Golgi apparatus; when associated with A-90.|||Altered binding to coatomer.|||Basic and acidic residues|||Beta-hairpin required for oligomerization|||Disordered|||Golgi phosphoprotein 3|||Loss of binding to coatomer.|||Loss of function in vesicle budding, abolishes phosphoinositide binding and localization to the Golgi apparatus.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123819
http://togogenome.org/gene/9606:ARHGEF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92888                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In IMD62; impairs RhoAGTPase activation and GNA12- and GNA13-mediated signaling; reduces actin polymerization.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||Lowers the exchange activity.|||No effect.|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by JAK2|||Polar residues|||RGSL|||Rho guanine nucleotide exchange factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080906|||http://purl.uniprot.org/annotation/VAR_033521|||http://purl.uniprot.org/annotation/VAR_035969|||http://purl.uniprot.org/annotation/VAR_082652|||http://purl.uniprot.org/annotation/VSP_008125|||http://purl.uniprot.org/annotation/VSP_037766|||http://purl.uniprot.org/annotation/VSP_057289
http://togogenome.org/gene/9606:SLC26A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50443                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In ACG1B; reduced sulfate transport; loss of cell membrane localization.|||In ACG1B; significant loss of sulfate transport.|||In AO2 and EDM4; no effect on sulfate transport and cell membrane localization.|||In AO2 and EDM4; reduced sulfate transport; significant reduction in sulfate-oxalate exchange activity; no effect on cell membrane localization.|||In AO2; significant loss of sulfate transport.|||In EDM4.|||In EDM4; no effect on sulfate transport and cell membrane localization.|||In diatrophic dysplasia; broad bone-platyspondylic variant; no effect on sulfate transport and cell membrane localization.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||STAS|||Sulfate transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080158|||http://purl.uniprot.org/annotation/VAR_007434|||http://purl.uniprot.org/annotation/VAR_007435|||http://purl.uniprot.org/annotation/VAR_007436|||http://purl.uniprot.org/annotation/VAR_007437|||http://purl.uniprot.org/annotation/VAR_007438|||http://purl.uniprot.org/annotation/VAR_007439|||http://purl.uniprot.org/annotation/VAR_018654|||http://purl.uniprot.org/annotation/VAR_018655|||http://purl.uniprot.org/annotation/VAR_020402|||http://purl.uniprot.org/annotation/VAR_058415|||http://purl.uniprot.org/annotation/VAR_066835
http://togogenome.org/gene/9606:PLCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR47|||http://purl.uniprot.org/uniprot/A8K8F9|||http://purl.uniprot.org/uniprot/P51178                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1|||Abolishes hydrolysis inositol phospholipids. No effect on binding to phosphatidylinositol 4,5-bisphosphate.|||C2|||Decreases hydrolysis inositol phospholipids.|||Decreases on hydrolysis inositol phospholipids.|||EF-hand|||EF-hand 1|||EF-hand 2|||In NDNC3.|||In isoform 2.|||No effect on hydrolysis inositol phospholipids.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Phosphothreonine|||Substrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088504|||http://purl.uniprot.org/annotation/VAR_046560|||http://purl.uniprot.org/annotation/VAR_066399|||http://purl.uniprot.org/annotation/VAR_066400|||http://purl.uniprot.org/annotation/VSP_042919
http://togogenome.org/gene/9606:ZSCAN25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSZ9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||SCAN box|||Zinc finger and SCAN domain-containing protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309332|||http://purl.uniprot.org/annotation/VAR_036931|||http://purl.uniprot.org/annotation/VSP_029145|||http://purl.uniprot.org/annotation/VSP_029146|||http://purl.uniprot.org/annotation/VSP_029147
http://togogenome.org/gene/9606:MAP3K11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16584                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Greatly reduced autophosphorylation activity.|||In isoform 2.|||Leucine-zipper 1|||Leucine-zipper 2|||Loss of kinase activity. Prevents activation of SAPK and MAPK14.|||Mitogen-activated protein kinase kinase kinase 11|||No effect on SAPK activation.|||No effect on autophosphorylation activity or activation of SAPK and MAPK14.|||Phosphoserine|||Phosphoserine; by autocatalysis and MAP4K1|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Pro residues|||Protein kinase|||Proton acceptor|||Reduced autophosphorylation activity. Reduced activation of SAPK and MAPK14.|||SH3|||Severely reduced autophosphorylation activity. Prevents phosphorylation of SAPK and MAPK14.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086260|||http://purl.uniprot.org/annotation/VAR_030604|||http://purl.uniprot.org/annotation/VAR_040703|||http://purl.uniprot.org/annotation/VAR_040704|||http://purl.uniprot.org/annotation/VSP_056183
http://togogenome.org/gene/9606:ABCC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J66                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 11|||Cytoplasmic|||Disordered|||Does not affect N-glycosylation.|||Helical|||In dry earwax and lack of axillary odor phenotype; loss of N-glycosylation; strongly reduced plasma membrane localization; no DHEAS transport and largely reduced estrone 3-sulfate transport; decreased protein concentration in axillary sweat.|||In isoform 2.|||Loss of N-glycosylation.|||N-linked (GlcNAc...) asparagine|||No effect on glycosylation.|||No effect on glycosylation; no effect on transport activity; no effect on plasma membrane localization.|||Significantly decreased transport activity of DHEAS and estrone 3-sulfate; no effect on glycosylation; reduced ATP-dependent 5-FdUMP transport; no effect on plasma membrane localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225594|||http://purl.uniprot.org/annotation/VAR_025437|||http://purl.uniprot.org/annotation/VAR_025438|||http://purl.uniprot.org/annotation/VAR_048144|||http://purl.uniprot.org/annotation/VAR_048145|||http://purl.uniprot.org/annotation/VAR_048146|||http://purl.uniprot.org/annotation/VAR_048147|||http://purl.uniprot.org/annotation/VAR_048148|||http://purl.uniprot.org/annotation/VAR_048149|||http://purl.uniprot.org/annotation/VAR_077575|||http://purl.uniprot.org/annotation/VAR_077576|||http://purl.uniprot.org/annotation/VSP_017351
http://togogenome.org/gene/9606:HGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14210                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Hepatocyte growth factor alpha chain|||Hepatocyte growth factor beta chain|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 6.|||Interchain (between alpha and beta chains)|||Kringle 1|||Kringle 2|||Kringle 3|||Kringle 4|||Loss of activity due to absence of proteolytic cleavage.|||N-linked (GlcNAc...) (complex) asparagine|||O-linked (GalNAc...) threonine|||PAN|||Peptidase S1|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000021|||http://purl.uniprot.org/annotation/CAR_000022|||http://purl.uniprot.org/annotation/CAR_000023|||http://purl.uniprot.org/annotation/CAR_000024|||http://purl.uniprot.org/annotation/CAR_000025|||http://purl.uniprot.org/annotation/PRO_0000028091|||http://purl.uniprot.org/annotation/PRO_0000028092|||http://purl.uniprot.org/annotation/VAR_019199|||http://purl.uniprot.org/annotation/VAR_019200|||http://purl.uniprot.org/annotation/VSP_009617|||http://purl.uniprot.org/annotation/VSP_009618|||http://purl.uniprot.org/annotation/VSP_009619|||http://purl.uniprot.org/annotation/VSP_009620|||http://purl.uniprot.org/annotation/VSP_009621|||http://purl.uniprot.org/annotation/VSP_009622|||http://purl.uniprot.org/annotation/VSP_009623
http://togogenome.org/gene/9606:DET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5Y6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  DET1 homolog|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129026|||http://purl.uniprot.org/annotation/VSP_043012
http://togogenome.org/gene/9606:ECM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI7|||http://purl.uniprot.org/uniprot/Q16610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||2|||2 X approximate repeats|||Disordered|||Extracellular matrix protein 1|||In LiP.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021146|||http://purl.uniprot.org/annotation/PRO_5007491836|||http://purl.uniprot.org/annotation/VAR_014761|||http://purl.uniprot.org/annotation/VAR_014762|||http://purl.uniprot.org/annotation/VAR_014763|||http://purl.uniprot.org/annotation/VAR_018690|||http://purl.uniprot.org/annotation/VAR_018691|||http://purl.uniprot.org/annotation/VSP_036411|||http://purl.uniprot.org/annotation/VSP_036412|||http://purl.uniprot.org/annotation/VSP_036413|||http://purl.uniprot.org/annotation/VSP_036414|||http://purl.uniprot.org/annotation/VSP_036415|||http://purl.uniprot.org/annotation/VSP_036416
http://togogenome.org/gene/9606:SLC6A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VAM4|||http://purl.uniprot.org/uniprot/Q4VAM6|||http://purl.uniprot.org/uniprot/Q9Y345                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased glycine transport.|||Decreased surface expression. Decreased glycine transport.|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In HKPX3; compound heterozygote with S-509; impairment of glycine transport when coexpressed with S-509 in vitro.|||In HKPX3; compound heterozygote with V-306; no effect on subcellular location; impairs glycine transport.|||In HKPX3; impairs glycine transport; no effect on subcellular location.|||In HKPX3; no effect on subcellular location; impairs glycine transport.|||In HKPX3; results in the formation of large aggregates in the cytoplasm; loss of glycine transport.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Mild decrease of glycine transport; Vmax of the mutant is reduced to 60% compared to wild-type; decreased expression at the cell surface.|||N-linked (GlcNAc...) asparagine|||No effect on glycine transport.|||No effect on subcellular location; no effect on glycine transport.|||Phosphoserine|||Phosphothreonine|||Sodium- and chloride-dependent glycine transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214762|||http://purl.uniprot.org/annotation/PRO_5004245393|||http://purl.uniprot.org/annotation/VAR_011591|||http://purl.uniprot.org/annotation/VAR_011592|||http://purl.uniprot.org/annotation/VAR_011593|||http://purl.uniprot.org/annotation/VAR_036160|||http://purl.uniprot.org/annotation/VAR_044163|||http://purl.uniprot.org/annotation/VAR_044164|||http://purl.uniprot.org/annotation/VAR_044165|||http://purl.uniprot.org/annotation/VAR_044166|||http://purl.uniprot.org/annotation/VAR_044167|||http://purl.uniprot.org/annotation/VAR_044168|||http://purl.uniprot.org/annotation/VAR_044169|||http://purl.uniprot.org/annotation/VAR_044170|||http://purl.uniprot.org/annotation/VAR_044171|||http://purl.uniprot.org/annotation/VAR_044172|||http://purl.uniprot.org/annotation/VAR_044173|||http://purl.uniprot.org/annotation/VAR_044174|||http://purl.uniprot.org/annotation/VAR_044175|||http://purl.uniprot.org/annotation/VAR_044176|||http://purl.uniprot.org/annotation/VAR_082588|||http://purl.uniprot.org/annotation/VAR_087307|||http://purl.uniprot.org/annotation/VSP_061562|||http://purl.uniprot.org/annotation/VSP_061563
http://togogenome.org/gene/9606:STAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PH|||Phosphotyrosine|||SH2|||Signal-transducing adaptor protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072237
http://togogenome.org/gene/9606:KANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14678                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  10-fold decrease in binding to KIF21A.|||15-fold decrease in binding to KIF21A.|||4.5-fold decrease in binding to KIF21A.|||ANK 0; degenerate|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Abolishes binding to KIF21A.|||Abolishes phosphorylation by PKB. Abolishes interaction with YWHAB; YWHAG; YWHAE; YWHAH; YWHAQ; YWHAZ and SFN.|||Disordered|||Enhanced cytoplasmic localization; when associated with 65-A--68 and 979-A--A-981.|||Enhanced cytoplasmic localization; when associated with 65-A--A-68 and 991-A-A-992.|||Enhanced cytoplasmic localization; when associated with 979-A--A-981 and 991-A-A-992.|||Found in a patient with nephrotic syndrome; unknown pathological significance; no effect on protein localization.|||In isoform 2.|||Interaction with KIF21A|||KN motif and ankyrin repeat domain-containing protein 1|||Nuclear export signal 1 (NES 1)|||Nuclear export signal 2 (NES 2)|||Nuclear export signal 3 (NES 3)|||Nuclear localization signal 1 (NLS 1)|||Nuclear localization signal 2 (NLS 2)|||Nuclear localization; when associated A-43; A-125; A-129; A-134; A-613; A-616; A-620 and A-622.|||Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-620.|||Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-616 and A-622.|||Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-613; A-620 and A-622.|||Nuclear localization; when associated A-43; A-52; A-125; A-129; A-134; A-616; A-620 and A-622.|||Nuclear localization; when associated A-43; A-52; A-125; A-129; A-613; A-616; A-620 and A-622.|||Nuclear localization; when associated A-43; A-52; A-125; A-134; A-613; A-616; A-620 and A-622.|||Nuclear localization; when associated A-43; A-52; A-129; A-134; A-613; A-616; A-620 and A-622.|||Nuclear localization; when associated A-52; A-125; A-129; A-134; A-613; A-616; A-620 and A-622.|||Phosphoserine|||Phosphoserine; by PKB|||Polar residues|||Very weak binding affinity for KIF21A.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066911|||http://purl.uniprot.org/annotation/VAR_016697|||http://purl.uniprot.org/annotation/VAR_026212|||http://purl.uniprot.org/annotation/VAR_026213|||http://purl.uniprot.org/annotation/VAR_048298|||http://purl.uniprot.org/annotation/VAR_048299|||http://purl.uniprot.org/annotation/VAR_048300|||http://purl.uniprot.org/annotation/VAR_048301|||http://purl.uniprot.org/annotation/VAR_048302|||http://purl.uniprot.org/annotation/VAR_048303|||http://purl.uniprot.org/annotation/VAR_080958|||http://purl.uniprot.org/annotation/VSP_043958
http://togogenome.org/gene/9606:ESCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56NI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHH-type|||Disordered|||In JHS; strongly decreased protein levels.|||In RBS.|||In isoform 2.|||N-acetyltransferase ESCO2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074542|||http://purl.uniprot.org/annotation/VAR_022649|||http://purl.uniprot.org/annotation/VAR_033840|||http://purl.uniprot.org/annotation/VAR_060994|||http://purl.uniprot.org/annotation/VAR_085392|||http://purl.uniprot.org/annotation/VSP_055773|||http://purl.uniprot.org/annotation/VSP_055774
http://togogenome.org/gene/9606:LINGO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UY18                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324184
http://togogenome.org/gene/9606:TNS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJP3|||http://purl.uniprot.org/uniprot/Q8IZW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Abolishes cleavage by caspase-3.|||Abolishes focal adhesion localization; when associated with A-474.|||Abolishes interaction with DLC1. Abolishes interaction with CBL following EGF stimulation. Loss of ability to reduce ubiquitination of activated EGFR. Significant decrease in interaction with MET, faster MET trafficking to the lysosome and significant increase in MET turnover. Significant inhibition of basal and HGF-stimulated cell migration. No effect on focal adhesion localization. Abolishes focal adhesion localization; when associated with 100-F--L-118 DEL.|||Abolishes interaction with ITGB1. Does not affect interaction with CBL following EGF stimulation.|||Cleavage; by caspase-3|||Disordered|||In a colorectal cancer sample; somatic mutation.|||No effect on cleavage by caspase-3.|||PTB|||Phosphoserine|||Polar residues|||SH2|||Tensin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248213|||http://purl.uniprot.org/annotation/VAR_027264|||http://purl.uniprot.org/annotation/VAR_027265|||http://purl.uniprot.org/annotation/VAR_036515|||http://purl.uniprot.org/annotation/VAR_055292
http://togogenome.org/gene/9606:PURG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Purine-rich element-binding protein gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255952|||http://purl.uniprot.org/annotation/VAR_036317|||http://purl.uniprot.org/annotation/VAR_053613|||http://purl.uniprot.org/annotation/VAR_053614|||http://purl.uniprot.org/annotation/VAR_053615|||http://purl.uniprot.org/annotation/VSP_021319
http://togogenome.org/gene/9606:NFE2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J9JIE5|||http://purl.uniprot.org/uniprot/Q14494|||http://purl.uniprot.org/uniprot/Q8NF22                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BZIP|||Basic and acidic residues|||Basic motif|||CPD|||Cholesterol recognition/amino acid consensus (CRAC) region|||Cleavage; by DDI2|||Destruction motif|||Disordered|||Endoplasmic reticulum membrane sensor NFE2L1|||Helical; Signal-anchor for type II membrane protein|||Impaired interaction with CEBPB.|||In isoform 2.|||In m1; impaired protein cleavage.|||In m2; impaired protein cleavage.|||In m3; impaired protein cleavage.|||In m4; Slightly impaired protein cleavage.|||In m5; impaired protein cleavage.|||In m6; Slightly impaired protein cleavage.|||Leucine-zipper|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by CK2|||Phosphoserine; by PKA|||Polar residues|||Transcription factor NRF1|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076447|||http://purl.uniprot.org/annotation/PRO_0000443103|||http://purl.uniprot.org/annotation/VAR_048440|||http://purl.uniprot.org/annotation/VSP_000579
http://togogenome.org/gene/9606:TRIP13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15645                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MVA3; loss of protein expression; impairment of spindle assembly checkpoint.|||In OZEMA9; decreased protein level in patient cells.|||In OZEMA9; unknown pathological significance.|||In isoform 2.|||N-acetylmethionine|||Pachytene checkpoint protein 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084782|||http://purl.uniprot.org/annotation/VAR_079275|||http://purl.uniprot.org/annotation/VAR_084761|||http://purl.uniprot.org/annotation/VAR_084762|||http://purl.uniprot.org/annotation/VAR_084763|||http://purl.uniprot.org/annotation/VAR_084764|||http://purl.uniprot.org/annotation/VAR_084765|||http://purl.uniprot.org/annotation/VSP_016957
http://togogenome.org/gene/9606:IPO13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94829                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Importin N-terminal|||Importin-13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120758
http://togogenome.org/gene/9606:EVC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PCN4|||http://purl.uniprot.org/uniprot/P57679|||http://purl.uniprot.org/uniprot/Q5U3C2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EvC complex member EVC|||Extracellular|||Helical|||In EVC.|||In EVC; atypical phenotype with septal cardiac defects, rhizomelic limb shortening and polydactyly without the typical lip, dental and nail abnormalities of EVC.|||In WAD.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087102|||http://purl.uniprot.org/annotation/VAR_009942|||http://purl.uniprot.org/annotation/VAR_009943|||http://purl.uniprot.org/annotation/VAR_009944|||http://purl.uniprot.org/annotation/VAR_009945|||http://purl.uniprot.org/annotation/VAR_009946|||http://purl.uniprot.org/annotation/VAR_009947|||http://purl.uniprot.org/annotation/VAR_009948|||http://purl.uniprot.org/annotation/VAR_009949|||http://purl.uniprot.org/annotation/VAR_009950|||http://purl.uniprot.org/annotation/VAR_009951|||http://purl.uniprot.org/annotation/VAR_033852|||http://purl.uniprot.org/annotation/VAR_033853|||http://purl.uniprot.org/annotation/VAR_066447|||http://purl.uniprot.org/annotation/VAR_066448
http://togogenome.org/gene/9606:CCL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55774                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 18|||CCL18(1-68)|||CCL18(3-69)|||CCL18(4-69)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005212|||http://purl.uniprot.org/annotation/PRO_0000041851|||http://purl.uniprot.org/annotation/PRO_0000041852|||http://purl.uniprot.org/annotation/PRO_0000041853
http://togogenome.org/gene/9606:CKAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWK9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoskeleton-associated protein 2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245774|||http://purl.uniprot.org/annotation/VAR_054018|||http://purl.uniprot.org/annotation/VAR_069359|||http://purl.uniprot.org/annotation/VSP_047100|||http://purl.uniprot.org/annotation/VSP_047101|||http://purl.uniprot.org/annotation/VSP_047102|||http://purl.uniprot.org/annotation/VSP_055686
http://togogenome.org/gene/9606:ADIRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15847                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Adipogenesis regulatory factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064637
http://togogenome.org/gene/9606:RPS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23396                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by MAPK and translocation to the nucleus following exposure of cells to hydrogen peroxide. No effect on phosphorylation by CDK1 or PRKCD.|||Abolishes phosphorylation by PKB.|||Asymmetric dimethylarginine; by PRMT1|||Disordered|||Does not affect ability to cleave DNA but abolishes binding to 8-oxoG.|||Does not affect ubiquitination in response to ribosome stalling.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||KH type-2|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221.|||No effect on phosphorylation by MAPK. Significantly reduces phosphorylation by CDK1 and nuclear accumulation. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-6.|||No effect on phosphorylation by PRKCD.|||No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB.|||No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. Does not affect ubiquitination in response to ribosome stalling.|||No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. Abolished ubiquitination by RNF10 in response to ribosome stalling and deubiquitination by USP10.|||No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230.|||Phosphomimetic mutant which is detected exclusively in the nucleus.|||Phosphoserine|||Phosphoserine; by IKKB|||Phosphoserine; by PKC/PRKCD|||Phosphothreonine|||Phosphothreonine; by CDK1 and PKC/PRKCD|||Phosphothreonine; by MAPK|||Phosphothreonine; by PKB|||Reduced phosphorylation by IKKB.|||Removed|||Small ribosomal subunit protein uS3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130320|||http://purl.uniprot.org/annotation/VSP_046667
http://togogenome.org/gene/9606:PABPC1L2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQF8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polyadenylate-binding protein 1-like 2|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304509
http://togogenome.org/gene/9606:ZNF281                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMX4|||http://purl.uniprot.org/uniprot/Q9Y2X9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 281                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047505|||http://purl.uniprot.org/annotation/VAR_035576|||http://purl.uniprot.org/annotation/VSP_054815
http://togogenome.org/gene/9606:WWC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IX03                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADDV motif|||Acidic residues|||Associated with Ala-735; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P.|||Associated with Ile-734; affects KIBRA lipid-binding specificity showing stronger interactions with PI(4)P and PI(5)P.|||Basic and acidic residues|||C2|||Disordered|||In isoform 2.|||Interaction with PRKCZ|||Interaction with histone H3|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by PKC/PRKCZ|||Phosphothreonine|||Polar residues|||Protein KIBRA|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242153|||http://purl.uniprot.org/annotation/VAR_026844|||http://purl.uniprot.org/annotation/VAR_053449|||http://purl.uniprot.org/annotation/VAR_053450|||http://purl.uniprot.org/annotation/VSP_019448
http://togogenome.org/gene/9606:MAGEB18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Interaction with LNX1|||MAGE|||Melanoma-associated antigen B18|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156719|||http://purl.uniprot.org/annotation/VAR_053500
http://togogenome.org/gene/9606:GATD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB37                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glutamine amidotransferase-like class 1 domain-containing protein 1|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305094|||http://purl.uniprot.org/annotation/VSP_028231|||http://purl.uniprot.org/annotation/VSP_028232|||http://purl.uniprot.org/annotation/VSP_028233
http://togogenome.org/gene/9606:S100A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33763                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||In isoform 2.|||Protein S100-A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143980|||http://purl.uniprot.org/annotation/VAR_001305|||http://purl.uniprot.org/annotation/VSP_055506
http://togogenome.org/gene/9606:CNOT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95628                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with E2 ubiquitin ligases.|||Asymmetric dimethylarginine|||C3H1-type|||CCR4-NOT transcription complex subunit 4|||Disordered|||In isoform 2, isoform 8 and isoform 9.|||In isoform 3.|||In isoform 4 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 9 and isoform 10.|||Phosphoserine|||Polar residues|||RING-type; degenerate|||RRM|||Strongly reduced interaction with UBE2D2.|||Strongly reduces interaction with E2 ubiquitin ligases.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081679|||http://purl.uniprot.org/annotation/VAR_027833|||http://purl.uniprot.org/annotation/VSP_009923|||http://purl.uniprot.org/annotation/VSP_009924|||http://purl.uniprot.org/annotation/VSP_009925|||http://purl.uniprot.org/annotation/VSP_009926|||http://purl.uniprot.org/annotation/VSP_009927|||http://purl.uniprot.org/annotation/VSP_009928|||http://purl.uniprot.org/annotation/VSP_009929|||http://purl.uniprot.org/annotation/VSP_045469
http://togogenome.org/gene/9606:AMY2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04746|||http://purl.uniprot.org/uniprot/Q53F26                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity.|||Abolishes chloride binding; has only slight effect on activity.|||Abolishes chloride binding; strongly reduces activity.|||Alpha-amylase|||Alpha-amylase C-terminal|||Glycosyl hydrolase family 13 catalytic|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Pancreatic alpha-amylase|||Proton donor|||Pyrrolidone carboxylic acid|||Reduces activity.|||Reduces affinity for chloride; reduces activity.|||Strongly reduces activity.|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001397|||http://purl.uniprot.org/annotation/PRO_5012249232|||http://purl.uniprot.org/annotation/VSP_055822|||http://purl.uniprot.org/annotation/VSP_055823
http://togogenome.org/gene/9606:DBH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09172                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||DOMON|||Disordered|||Dopamine beta-hydroxylase|||Helical; Signal-anchor for type II membrane protein|||In ORTHYP1.|||In allele DBH-B.|||Interchain (with C-528)|||Interchain (with C-530)|||Intragranular|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Soluble dopamine beta-hydroxylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006356|||http://purl.uniprot.org/annotation/PRO_0000308209|||http://purl.uniprot.org/annotation/VAR_002196|||http://purl.uniprot.org/annotation/VAR_013947|||http://purl.uniprot.org/annotation/VAR_013948|||http://purl.uniprot.org/annotation/VAR_014706|||http://purl.uniprot.org/annotation/VAR_014707|||http://purl.uniprot.org/annotation/VAR_014708|||http://purl.uniprot.org/annotation/VAR_014709|||http://purl.uniprot.org/annotation/VAR_014710|||http://purl.uniprot.org/annotation/VAR_022758|||http://purl.uniprot.org/annotation/VAR_022759|||http://purl.uniprot.org/annotation/VAR_022760|||http://purl.uniprot.org/annotation/VAR_048838
http://togogenome.org/gene/9606:OR10H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVV2|||http://purl.uniprot.org/uniprot/Q8NGA5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10H4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150705|||http://purl.uniprot.org/annotation/VAR_034290|||http://purl.uniprot.org/annotation/VAR_034291|||http://purl.uniprot.org/annotation/VAR_062063
http://togogenome.org/gene/9606:LGALS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK26|||http://purl.uniprot.org/uniprot/Q96DT0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  Galectin|||Galectin 1|||Galectin 2|||Galectin-12|||In isoform B and isoform D.|||In isoform C and isoform D.|||In isoform E and isoform F.|||In isoform F and isoform G.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076949|||http://purl.uniprot.org/annotation/VSP_003099|||http://purl.uniprot.org/annotation/VSP_003100|||http://purl.uniprot.org/annotation/VSP_003101|||http://purl.uniprot.org/annotation/VSP_003102
http://togogenome.org/gene/9606:PCDHB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN67                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003932
http://togogenome.org/gene/9606:MYOCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZQ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HDAC5-binding|||In MGBL; loss of function in transcriptional activation.|||In MGBL; unknown pathological significance; decreased function in transcriptional activation.|||In isoform 2 and isoform 3.|||In isoform 2.|||MEF2C-binding|||Myocardin|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK1 and MAPK3|||Phosphothreonine; by MAPK1 and MAPK3|||Polar residues|||RPEL 1|||RPEL 2|||RPEL 3|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126631|||http://purl.uniprot.org/annotation/VAR_083482|||http://purl.uniprot.org/annotation/VAR_083483|||http://purl.uniprot.org/annotation/VSP_007658|||http://purl.uniprot.org/annotation/VSP_007659|||http://purl.uniprot.org/annotation/VSP_007660|||http://purl.uniprot.org/annotation/VSP_007661
http://togogenome.org/gene/9606:TNFRSF11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Q6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In FEO.|||In OPTB7; a patient with osteoclast-poor osteopetrosis.|||In OPTB7; one patient with osteoclast-poor osteopetrosis.|||In OPTB7; two patients with osteoclast-poor osteopetrosis.|||In OPTB7; two siblings with osteoclast-poor osteopetrosis.|||In PDB2.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform RANK-e5a.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Required for interaction with EEIG1 and osteoclast differentiation|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 11A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034585|||http://purl.uniprot.org/annotation/VAR_011516|||http://purl.uniprot.org/annotation/VAR_011517|||http://purl.uniprot.org/annotation/VAR_011518|||http://purl.uniprot.org/annotation/VAR_046788|||http://purl.uniprot.org/annotation/VAR_046789|||http://purl.uniprot.org/annotation/VAR_046790|||http://purl.uniprot.org/annotation/VAR_046791|||http://purl.uniprot.org/annotation/VAR_046792|||http://purl.uniprot.org/annotation/VAR_046793|||http://purl.uniprot.org/annotation/VSP_046901|||http://purl.uniprot.org/annotation/VSP_054179|||http://purl.uniprot.org/annotation/VSP_054180|||http://purl.uniprot.org/annotation/VSP_054181|||http://purl.uniprot.org/annotation/VSP_054182|||http://purl.uniprot.org/annotation/VSP_054183
http://togogenome.org/gene/9606:ATP5PF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18859                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATP synthase-coupling factor 6, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002527|||http://purl.uniprot.org/annotation/VAR_083477|||http://purl.uniprot.org/annotation/VSP_046187
http://togogenome.org/gene/9606:FBH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV95|||http://purl.uniprot.org/uniprot/F6UZG9|||http://purl.uniprot.org/uniprot/Q2TAK1|||http://purl.uniprot.org/uniprot/Q8NFZ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  APIM motif|||Abolishes helicase activity and prevents accumulation on single-stranded DNA.|||Basic and acidic residues|||Disordered|||F-box|||F-box DNA helicase 1|||Impaired localization to DNA damage sites in response to UV irradiation.|||Impairs formation of the SCF(FBH1) complex and impairs accumulation on single-stranded DNA.|||In PIPdeg3A; reduced ubiquitination.|||In isoform 2.|||No effect; when associated with A-56.|||No effect; when associated with A-583.|||PIP-box|||Phosphoserine|||UvrD-like helicase ATP-binding|||UvrD-like helicase C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119901|||http://purl.uniprot.org/annotation/VSP_037942
http://togogenome.org/gene/9606:NBPF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG53|||http://purl.uniprot.org/uniprot/P0DPF3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Neuroblastoma breakpoint family member 9|||Olduvai|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5|||Olduvai 6|||Olduvai 7|||Olduvai 8|||Olduvai 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288044|||http://purl.uniprot.org/annotation/VSP_059364
http://togogenome.org/gene/9606:TDG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E127|||http://purl.uniprot.org/uniprot/Q13569                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G/T mismatch-specific thymine DNA glycosylase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Increased DNA glycosylase activity on G/T mispairs.|||Loss of DNA glycosylase activity but still able to bind DNA.|||Reduced DNA glycosylase activity on G/T and G/U mispairs.|||Reduced DNA glycosylase activity on G/T mispairs.|||Restores the DNA-binding ability of the sumoylated form.|||Uracil-DNA glycosylase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185777|||http://purl.uniprot.org/annotation/VAR_018892|||http://purl.uniprot.org/annotation/VAR_018893|||http://purl.uniprot.org/annotation/VAR_050140|||http://purl.uniprot.org/annotation/VAR_059450
http://togogenome.org/gene/9606:SELENOI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D9                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Non standard residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Ethanolaminephosphotransferase 1|||Helical|||In SPG81; loss of ethanolaminephosphotransferase activity.|||N-acetylalanine|||Removed|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056813|||http://purl.uniprot.org/annotation/VAR_083878
http://togogenome.org/gene/9606:CDY1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chromo|||Disordered|||In isoform 2.|||Polar residues|||Testis-specific chromodomain protein Y 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080219|||http://purl.uniprot.org/annotation/VSP_001079
http://togogenome.org/gene/9606:SUSD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60279                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Link|||Sushi|||Sushi domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274247|||http://purl.uniprot.org/annotation/VAR_030217|||http://purl.uniprot.org/annotation/VAR_030218|||http://purl.uniprot.org/annotation/VAR_051391|||http://purl.uniprot.org/annotation/VAR_051392|||http://purl.uniprot.org/annotation/VAR_051393
http://togogenome.org/gene/9606:FUCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04066                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  In FUCA1D.|||In FUCA1D; less than 1% of residual activity.|||In FUCA1D; loss of activity.|||In allele FUCA1*2.|||May be important for catalysis|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Tissue alpha-L-fucosidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010308|||http://purl.uniprot.org/annotation/VAR_002442|||http://purl.uniprot.org/annotation/VAR_002443|||http://purl.uniprot.org/annotation/VAR_002444|||http://purl.uniprot.org/annotation/VAR_016233|||http://purl.uniprot.org/annotation/VAR_016234|||http://purl.uniprot.org/annotation/VAR_016235|||http://purl.uniprot.org/annotation/VAR_049106|||http://purl.uniprot.org/annotation/VAR_049107|||http://purl.uniprot.org/annotation/VAR_049108
http://togogenome.org/gene/9606:CARD16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EG05                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CARD|||Caspase recruitment domain-containing protein 16|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349180|||http://purl.uniprot.org/annotation/VAR_046279|||http://purl.uniprot.org/annotation/VAR_046280|||http://purl.uniprot.org/annotation/VAR_046281|||http://purl.uniprot.org/annotation/VAR_046282|||http://purl.uniprot.org/annotation/VSP_035216
http://togogenome.org/gene/9606:MAPKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPZ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with ATF2|||Interaction with MAP3K2|||Interaction with NBN|||N-acetylalanine|||Phosphoserine|||Removed|||Target of rapamycin complex 2 subunit MAPKAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218768|||http://purl.uniprot.org/annotation/VSP_006098|||http://purl.uniprot.org/annotation/VSP_033202|||http://purl.uniprot.org/annotation/VSP_033203|||http://purl.uniprot.org/annotation/VSP_033204|||http://purl.uniprot.org/annotation/VSP_033205|||http://purl.uniprot.org/annotation/VSP_033206|||http://purl.uniprot.org/annotation/VSP_033207
http://togogenome.org/gene/9606:SCP2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJQ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  SCP2|||SCP2 sterol-binding domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079444|||http://purl.uniprot.org/annotation/VAR_024332
http://togogenome.org/gene/9606:SANBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSI8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||SANT|||SANT and BTB domain regulator of class switch recombination                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324598|||http://purl.uniprot.org/annotation/VAR_082836|||http://purl.uniprot.org/annotation/VSP_032299|||http://purl.uniprot.org/annotation/VSP_032300|||http://purl.uniprot.org/annotation/VSP_032301|||http://purl.uniprot.org/annotation/VSP_032302
http://togogenome.org/gene/9606:BRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAW0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||Abolishes response to oxidative stress. Abolishes the decrease in the formation of a ternary complex with DNA and TBP in response to oxidative stress.|||Cysteine sulfenic acid (-SOH)|||Decreases affinity for DNA.|||Disordered|||Impairs formation of a ternary complex with DNA and TBP.|||In isoform 2.|||Interaction with target DNA|||Phosphoserine|||Required for interaction with TBP and formation of a ternary complex with DNA and TBP|||Required for the formation of a ternary complex with DNA and TBP; not required for interaction with TBP in the absence of DNA|||TFIIB-type|||Transcription factor IIIB 50 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337187|||http://purl.uniprot.org/annotation/VSP_056834
http://togogenome.org/gene/9606:CADM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N126                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In CMT2FF; results in misfolding due to the creation of a non-native disulfide bond with C-152.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046067|||http://purl.uniprot.org/annotation/VAR_059383|||http://purl.uniprot.org/annotation/VAR_086232|||http://purl.uniprot.org/annotation/VSP_017221|||http://purl.uniprot.org/annotation/VSP_022008
http://togogenome.org/gene/9606:KLK14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1R3UHJ7|||http://purl.uniprot.org/uniprot/Q9P0G3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Kallikrein-14|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027958|||http://purl.uniprot.org/annotation/PRO_0000027959|||http://purl.uniprot.org/annotation/PRO_5040062220|||http://purl.uniprot.org/annotation/VAR_058018|||http://purl.uniprot.org/annotation/VAR_058019|||http://purl.uniprot.org/annotation/VAR_058020
http://togogenome.org/gene/9606:CSF2RB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32927|||http://purl.uniprot.org/uniprot/Q6NSJ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytokine receptor common subunit beta|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Pro residues|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010862|||http://purl.uniprot.org/annotation/VAR_014801|||http://purl.uniprot.org/annotation/VAR_014802|||http://purl.uniprot.org/annotation/VAR_014803|||http://purl.uniprot.org/annotation/VAR_042521|||http://purl.uniprot.org/annotation/VAR_042522|||http://purl.uniprot.org/annotation/VSP_032798
http://togogenome.org/gene/9606:CCDC141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZB3|||http://purl.uniprot.org/uniprot/Q6ZP82                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 141|||Disordered|||Ig-like|||In isoform 1.|||Phosphothreonine|||Reduced affinity for MRLC and impairs cortical migration.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317296|||http://purl.uniprot.org/annotation/VAR_047904|||http://purl.uniprot.org/annotation/VAR_047905|||http://purl.uniprot.org/annotation/VAR_047906|||http://purl.uniprot.org/annotation/VSP_062007|||http://purl.uniprot.org/annotation/VSP_062008
http://togogenome.org/gene/9606:NIBAN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96TA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Loss of melanoma cell invasion; when associated with A-641; A-646; A-665; A-668 and A-679.|||Loss of melanoma cell invasion; when associated with A-641; A-646; A-665; A-668 and A-683.|||Loss of melanoma cell invasion; when associated with A-641; A-646; A-665; A-679 and A-683.|||Loss of melanoma cell invasion; when associated with A-641; A-646; A-681; A-679 and A-683.|||Loss of melanoma cell invasion; when associated with A-641; A-665; A-681; A-679 and A-683.|||Loss of melanoma cell invasion; when associated with A-646; A-665; A-681; A-679 and A-683.|||N-myristoyl glycine|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Promotes melanoma cell invasion; when associated with D/E-628; D/E-633; D/E-652; D/E-668 and D/E-679.|||Promotes melanoma cell invasion; when associated with D/E-628; D/E-633; D/E-652; D/E-668 and D/E-683.|||Promotes melanoma cell invasion; when associated with D/E-628; D/E-633; D/E-652; D/E-679 and D/E-683.|||Promotes melanoma cell invasion; when associated with D/E-628; D/E-633; D/E-668; D/E-679 and D/E-683.|||Promotes melanoma cell invasion; when associated with D/E-628; D/E-652; D/E-668; D/E-679 and D/E-683.|||Promotes melanoma cell invasion; when associated with D/E-633; D/E-652; D/E-668; D/E-679 and D/E-683.|||Protein Niban 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213121|||http://purl.uniprot.org/annotation/VSP_041810
http://togogenome.org/gene/9606:HTR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E398|||http://purl.uniprot.org/uniprot/P46098                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 3A|||Abolished 5-hydroxytryptamine (serotonin) binding to the heteromeric receptor.|||Cytoplasmic|||Disordered|||Extracellular|||HA-stretch; determines single-channel conductance in 5-HT3 receptors|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Increased conductance. Massive increase of conductance; when associated with Q-432 and A-440.|||Increased conductance. Massive increase of conductance; when associated with Q-432 and D-436.|||Little effect on conductance. Massive increase of conductance; when associated with D-436 and A-440.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000408|||http://purl.uniprot.org/annotation/PRO_5022250066|||http://purl.uniprot.org/annotation/VAR_037398|||http://purl.uniprot.org/annotation/VAR_037399|||http://purl.uniprot.org/annotation/VAR_037400|||http://purl.uniprot.org/annotation/VAR_037401|||http://purl.uniprot.org/annotation/VAR_037402|||http://purl.uniprot.org/annotation/VSP_000078|||http://purl.uniprot.org/annotation/VSP_042214|||http://purl.uniprot.org/annotation/VSP_043484
http://togogenome.org/gene/9606:DRD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21917                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1; approximate|||2|||3|||4 X 16 AA approximate tandem repeats of [PA]-A-P-G-L-P-[PQR]-[DG]-P-C-G-P-D-C-A-P|||4; approximate|||Cytoplasmic|||D(4) dopamine receptor|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele D4.2.|||In allele D4.7.|||Increased basal level of G protein-mediated signaling.|||Loss of palmitoylation.|||N-linked (GlcNAc...) asparagine|||No effect on palmitoylation.|||Pro residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069401|||http://purl.uniprot.org/annotation/VAR_003464|||http://purl.uniprot.org/annotation/VAR_003465|||http://purl.uniprot.org/annotation/VAR_081438
http://togogenome.org/gene/9606:ZKSCAN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15776|||http://purl.uniprot.org/uniprot/Q59HG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Phosphoserine|||Polar residues|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047445|||http://purl.uniprot.org/annotation/VAR_009877|||http://purl.uniprot.org/annotation/VSP_056437|||http://purl.uniprot.org/annotation/VSP_056438
http://togogenome.org/gene/9606:GALE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL38|||http://purl.uniprot.org/uniprot/Q14376                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In GALAC3.|||In GALAC3; 2-fold decrease in UDP-galactose epimerization activity.|||In GALAC3; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine.|||In GALAC3; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose.|||In GALAC3; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine.|||In GALAC3; 800-fold decrease in UDP-galactose epimerization activity.|||In GALAC3; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine.|||In GALAC3; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation.|||In GALAC3; peripheral; 3-fold decrease in UDP-galactose epimerization activity.|||In GALAC3; peripheral; nearly normal activity towards UDP-galactose.|||In isoform 2.|||Loss of activity.|||NAD(P)-binding|||No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine.|||Proton acceptor|||UDP-glucose 4-epimerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183189|||http://purl.uniprot.org/annotation/VAR_002539|||http://purl.uniprot.org/annotation/VAR_002540|||http://purl.uniprot.org/annotation/VAR_002541|||http://purl.uniprot.org/annotation/VAR_002542|||http://purl.uniprot.org/annotation/VAR_002543|||http://purl.uniprot.org/annotation/VAR_002544|||http://purl.uniprot.org/annotation/VAR_002545|||http://purl.uniprot.org/annotation/VAR_002546|||http://purl.uniprot.org/annotation/VAR_010058|||http://purl.uniprot.org/annotation/VAR_037733|||http://purl.uniprot.org/annotation/VAR_037734|||http://purl.uniprot.org/annotation/VAR_037735|||http://purl.uniprot.org/annotation/VAR_037736|||http://purl.uniprot.org/annotation/VAR_037737|||http://purl.uniprot.org/annotation/VAR_037738|||http://purl.uniprot.org/annotation/VAR_037739|||http://purl.uniprot.org/annotation/VAR_037740|||http://purl.uniprot.org/annotation/VSP_056822
http://togogenome.org/gene/9606:RBMX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38159                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine; in Heterogeneous nuclear ribonucleoprotein G; alternate|||N-acetylvaline; in Heterogeneous nuclear ribonucleoprotein G, N-terminally processed|||N6-acetyllysine|||Necessary for RNA-binding|||Necessary for the association to nascent RNAPII transcripts and nuclear localization|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Promotes cell proliferation. Inhibits transcriptional up-regulation of the TXNIP promoter.|||RNA-binding motif protein, X chromosome|||RNA-binding motif protein, X chromosome, N-terminally processed|||RRM|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081854|||http://purl.uniprot.org/annotation/PRO_0000304582|||http://purl.uniprot.org/annotation/VSP_042203|||http://purl.uniprot.org/annotation/VSP_043650|||http://purl.uniprot.org/annotation/VSP_043651
http://togogenome.org/gene/9606:LILRA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/U5XH19                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Ig-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5004666658
http://togogenome.org/gene/9606:WBP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX94                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||WW domain binding protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000241450|||http://purl.uniprot.org/annotation/VAR_026839|||http://purl.uniprot.org/annotation/VAR_026840|||http://purl.uniprot.org/annotation/VSP_041670
http://togogenome.org/gene/9606:OR5H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGV7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150596|||http://purl.uniprot.org/annotation/VAR_053195|||http://purl.uniprot.org/annotation/VAR_053196|||http://purl.uniprot.org/annotation/VAR_053197
http://togogenome.org/gene/9606:OR4E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C645                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315824|||http://purl.uniprot.org/annotation/VAR_080171|||http://purl.uniprot.org/annotation/VAR_080172|||http://purl.uniprot.org/annotation/VAR_080173
http://togogenome.org/gene/9606:C12orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6X4T0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein C12orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274305|||http://purl.uniprot.org/annotation/VAR_030252|||http://purl.uniprot.org/annotation/VSP_022708|||http://purl.uniprot.org/annotation/VSP_022709
http://togogenome.org/gene/9606:ASAH2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7U1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Putative inactive neutral ceramidase B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343741|||http://purl.uniprot.org/annotation/VSP_056938
http://togogenome.org/gene/9606:KIF1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43896                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FHA|||In SPAX2.|||Kinesin motor|||Kinesin-like protein KIF1C|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125410|||http://purl.uniprot.org/annotation/VAR_070937
http://togogenome.org/gene/9606:PBXIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0K4|||http://purl.uniprot.org/uniprot/Q96AQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pre-B-cell leukemia transcription factor-interacting protein 1|||Reduces interaction with ESR1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306115|||http://purl.uniprot.org/annotation/VAR_035265|||http://purl.uniprot.org/annotation/VAR_051263|||http://purl.uniprot.org/annotation/VSP_028418|||http://purl.uniprot.org/annotation/VSP_028419
http://togogenome.org/gene/9606:TM6SF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4D7|||http://purl.uniprot.org/uniprot/Q9BZW5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  EXPERA|||EXPERA 1|||EXPERA 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Transmembrane 6 superfamily member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181833|||http://purl.uniprot.org/annotation/VAR_012844|||http://purl.uniprot.org/annotation/VAR_024661|||http://purl.uniprot.org/annotation/VSP_045697
http://togogenome.org/gene/9606:MGST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10620                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Microsomal glutathione S-transferase 1|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000217736|||http://purl.uniprot.org/annotation/VSP_046160
http://togogenome.org/gene/9606:GSTT2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G9J6Q5|||http://purl.uniprot.org/uniprot/P0CG30                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase theta-2B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395344|||http://purl.uniprot.org/annotation/VAR_033982
http://togogenome.org/gene/9606:RHOT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BXZ6|||http://purl.uniprot.org/uniprot/Q8IXI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes the formation of thread-like mitochondria.|||Causes constitutive activation inducing an aggregation of the mitochondrial network.|||Causes constitutive inactivation.|||Cytoplasmic|||EF-hand|||EF-hand 1|||EF-hand 2|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Miro|||Miro 1|||Miro 2|||Mitochondrial Rho GTPase 1|||Mitochondrial intermembrane|||No effect on PINK1-PRKN-mediated degradation.|||No effect.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239313|||http://purl.uniprot.org/annotation/VSP_019153|||http://purl.uniprot.org/annotation/VSP_019154|||http://purl.uniprot.org/annotation/VSP_019155|||http://purl.uniprot.org/annotation/VSP_019156|||http://purl.uniprot.org/annotation/VSP_019157|||http://purl.uniprot.org/annotation/VSP_019158|||http://purl.uniprot.org/annotation/VSP_047651
http://togogenome.org/gene/9606:COG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Conserved oligomeric Golgi complex subunit 3|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213500|||http://purl.uniprot.org/annotation/VAR_036454|||http://purl.uniprot.org/annotation/VAR_055663|||http://purl.uniprot.org/annotation/VSP_013652|||http://purl.uniprot.org/annotation/VSP_013653
http://togogenome.org/gene/9606:SPRR2E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22531                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA tandem repeats of P-K-C-P-[EQ]-P-C-P-P|||Disordered|||Small proline-rich protein 2E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150011
http://togogenome.org/gene/9606:GLRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48167                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycine receptor subunit beta|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||In HKPX2; heteropentameric channel complexes with GLRA1 have reduced expression at the cell membrane and display spontaneous channel opening in the absence of extracellular glycine.|||In HKPX2; heteropentameric channel complexes with GLRA1 have reduced expression at the cell membrane and reduced channel activity.|||In HKPX2; heteropentameric channel complexes with GLRA1 require much higher glycine levels for channel activation.|||In HKPX2; heteropentameric channel complexes with GLRA1 require much higher glycine levels for channel activation; no effect on expression at the cell membrane.|||In HKPX2; reduced GLRB protein levels; reduced glycine sensitivity; reduced channel activity; does not affect chloride selectivity of the receptor ionophore.|||In isoform 2.|||Loss of glycosylation. Prevents proper assembly of the GLRA2/GLRB heteropentamer receptor.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Prevents proper assembly of the GLRA2/GLRB heteropentamer receptor.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000423|||http://purl.uniprot.org/annotation/VAR_035070|||http://purl.uniprot.org/annotation/VAR_068246|||http://purl.uniprot.org/annotation/VAR_075502|||http://purl.uniprot.org/annotation/VAR_075503|||http://purl.uniprot.org/annotation/VAR_088405|||http://purl.uniprot.org/annotation/VSP_045466|||http://purl.uniprot.org/annotation/VSP_045467
http://togogenome.org/gene/9606:COPS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99627                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  COP9 signalosome complex subunit 8|||In isoform 2.|||PCI|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121007|||http://purl.uniprot.org/annotation/VSP_042715
http://togogenome.org/gene/9606:TPRG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0D9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Important for homomultimer formation|||Important for homomultimer formation and localization to presynaptic regions|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Tumor protein p63-regulated gene 1-like protein|||hSac2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269186|||http://purl.uniprot.org/annotation/VSP_022019
http://togogenome.org/gene/9606:PTGDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41222                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Increases enzyme activity about two-fold.|||Loss of enzyme activity.|||N-linked (GlcNAc...) (complex) asparagine|||Nucleophile|||O-linked (GalNAc...) serine|||Prostaglandin-H2 D-isomerase|||Reduces enzyme activity about five-fold.|||Reduces enzyme activity almost ten-fold.|||Reduces enzyme activity over ten-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017945|||http://purl.uniprot.org/annotation/VAR_004273
http://togogenome.org/gene/9606:IFT172                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UG01                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In BBS20; hypomorphic mutation.|||In BBS20; unknown pathological significance.|||In RP71; hypomorphic mutation.|||In RP71; represents a null allele.|||In SRTD10.|||In isoform 2.|||In isoform 3.|||Intraflagellar transport protein 172 homolog|||N-acetylmethionine|||Omega-N-methylarginine|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328941|||http://purl.uniprot.org/annotation/VAR_042581|||http://purl.uniprot.org/annotation/VAR_070956|||http://purl.uniprot.org/annotation/VAR_070957|||http://purl.uniprot.org/annotation/VAR_070958|||http://purl.uniprot.org/annotation/VAR_070959|||http://purl.uniprot.org/annotation/VAR_070960|||http://purl.uniprot.org/annotation/VAR_070961|||http://purl.uniprot.org/annotation/VAR_073800|||http://purl.uniprot.org/annotation/VAR_073801|||http://purl.uniprot.org/annotation/VAR_073802|||http://purl.uniprot.org/annotation/VAR_086152|||http://purl.uniprot.org/annotation/VAR_086153|||http://purl.uniprot.org/annotation/VSP_032848|||http://purl.uniprot.org/annotation/VSP_032849|||http://purl.uniprot.org/annotation/VSP_054428|||http://purl.uniprot.org/annotation/VSP_054429
http://togogenome.org/gene/9606:CAPN13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZZ7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-13|||EF-hand 1|||EF-hand 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259582|||http://purl.uniprot.org/annotation/VAR_028964|||http://purl.uniprot.org/annotation/VAR_028965|||http://purl.uniprot.org/annotation/VAR_028966|||http://purl.uniprot.org/annotation/VSP_021476|||http://purl.uniprot.org/annotation/VSP_021477
http://togogenome.org/gene/9606:SCCPDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPM7|||http://purl.uniprot.org/uniprot/Q8NBX0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylalanine|||Phosphoserine|||Removed|||Saccharopine dehydrogenase NADP binding|||Saccharopine dehydrogenase-like C-terminal|||Saccharopine dehydrogenase-like oxidoreductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212840|||http://purl.uniprot.org/annotation/VAR_034486
http://togogenome.org/gene/9606:POLDIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0L0|||http://purl.uniprot.org/uniprot/F6VRR5|||http://purl.uniprot.org/uniprot/Q659C6|||http://purl.uniprot.org/uniprot/Q9BY77                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by RPS6KB1|||Phosphothreonine|||Polymerase delta-interacting protein 3|||RRM|||Reduces in vitro phosphorylation by RPS6KB1. Abolishes in vitro phosphorylation by RPS6KB1; when associated with A-385.|||Reduces in vitro phosphorylation by RPS6KB1. Reduces in vitro phosphorylation by RPS6KB1; when associated with A-383.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081722|||http://purl.uniprot.org/annotation/VSP_011056
http://togogenome.org/gene/9606:RPH3AL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K7D5|||http://purl.uniprot.org/uniprot/Q9UNE2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FYVE-type|||In isoform 2.|||Polar residues|||Rab effector Noc2|||RabBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278263|||http://purl.uniprot.org/annotation/VSP_023244
http://togogenome.org/gene/9606:ZDHHC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AMU0|||http://purl.uniprot.org/uniprot/B4DNL2|||http://purl.uniprot.org/uniprot/Q969W1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Lumenal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC16|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212897|||http://purl.uniprot.org/annotation/VSP_008716|||http://purl.uniprot.org/annotation/VSP_016274|||http://purl.uniprot.org/annotation/VSP_016275
http://togogenome.org/gene/9606:NXNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CM4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In a patient with retinal dytrophy; unknown pathological significance; loss of interaction with BSG; loss of ability to sustain retinal cone survival.|||Nucleoredoxin-like protein 1|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319543|||http://purl.uniprot.org/annotation/VAR_083662|||http://purl.uniprot.org/annotation/VAR_083663|||http://purl.uniprot.org/annotation/VAR_083664|||http://purl.uniprot.org/annotation/VAR_083665|||http://purl.uniprot.org/annotation/VAR_083666|||http://purl.uniprot.org/annotation/VAR_083667|||http://purl.uniprot.org/annotation/VAR_083668
http://togogenome.org/gene/9606:ZNF880                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PDB4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 880                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326033|||http://purl.uniprot.org/annotation/VSP_032509|||http://purl.uniprot.org/annotation/VSP_032510
http://togogenome.org/gene/9606:OR51B5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CQ2|||http://purl.uniprot.org/uniprot/Q9H339                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 51B5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150747|||http://purl.uniprot.org/annotation/VAR_053307|||http://purl.uniprot.org/annotation/VAR_053308|||http://purl.uniprot.org/annotation/VAR_053309|||http://purl.uniprot.org/annotation/VAR_053310|||http://purl.uniprot.org/annotation/VAR_053311|||http://purl.uniprot.org/annotation/VAR_062078|||http://purl.uniprot.org/annotation/VAR_062079
http://togogenome.org/gene/9606:LAMA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSA0|||http://purl.uniprot.org/uniprot/A0A0A0MTS5|||http://purl.uniprot.org/uniprot/A0A0A6YYF2|||http://purl.uniprot.org/uniprot/Q16787                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Domain II and I|||Domain III A|||Domain III B|||Domain IV 1 (domain IV B)|||Domain V|||In JEB2B.|||In isoform 1.|||In isoform 3 and isoform 4.|||In isoform 4.|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 14|||Laminin EGF-like 15; truncated|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin IV type A|||Laminin N-terminal|||Laminin subunit alpha-3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017058|||http://purl.uniprot.org/annotation/PRO_5001967258|||http://purl.uniprot.org/annotation/PRO_5014015977|||http://purl.uniprot.org/annotation/PRO_5014017126|||http://purl.uniprot.org/annotation/VAR_047374|||http://purl.uniprot.org/annotation/VAR_047375|||http://purl.uniprot.org/annotation/VAR_050078|||http://purl.uniprot.org/annotation/VAR_050079|||http://purl.uniprot.org/annotation/VAR_050080|||http://purl.uniprot.org/annotation/VAR_059444|||http://purl.uniprot.org/annotation/VAR_059445|||http://purl.uniprot.org/annotation/VAR_086401|||http://purl.uniprot.org/annotation/VSP_035738|||http://purl.uniprot.org/annotation/VSP_035739|||http://purl.uniprot.org/annotation/VSP_043487|||http://purl.uniprot.org/annotation/VSP_047079|||http://purl.uniprot.org/annotation/VSP_047080
http://togogenome.org/gene/9606:OR8B8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW73|||http://purl.uniprot.org/uniprot/Q15620                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8B8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150657
http://togogenome.org/gene/9606:CCDC137                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PK04                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 137|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288452|||http://purl.uniprot.org/annotation/VAR_050739|||http://purl.uniprot.org/annotation/VAR_050740|||http://purl.uniprot.org/annotation/VAR_050741|||http://purl.uniprot.org/annotation/VAR_061582
http://togogenome.org/gene/9606:NXPE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Y0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||NXPE family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297594|||http://purl.uniprot.org/annotation/VAR_049024
http://togogenome.org/gene/9606:WLS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9L3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In ZKS; results in decreased secretion of WNT3A and WNT5A; decreased activation of WNT signaling.|||In isoform 2.|||In isoform 3.|||Interaction with Wnt proteins|||Lumenal|||Protein wntless homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271777|||http://purl.uniprot.org/annotation/VAR_029991|||http://purl.uniprot.org/annotation/VAR_086565|||http://purl.uniprot.org/annotation/VAR_086566|||http://purl.uniprot.org/annotation/VAR_086567|||http://purl.uniprot.org/annotation/VAR_086568|||http://purl.uniprot.org/annotation/VSP_022346|||http://purl.uniprot.org/annotation/VSP_022347|||http://purl.uniprot.org/annotation/VSP_046143
http://togogenome.org/gene/9606:GLUD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK14|||http://purl.uniprot.org/uniprot/P49448                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ADP-ribosylcysteine|||Glutamate dehydrogenase 2, mitochondrial|||Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase C-terminal|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007208|||http://purl.uniprot.org/annotation/VAR_048867
http://togogenome.org/gene/9606:ASPSCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form ASPSCR1-TFE3|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with GLUT4|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Tether containing UBX domain for GLUT4|||UBX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249885|||http://purl.uniprot.org/annotation/VAR_027503|||http://purl.uniprot.org/annotation/VAR_027504|||http://purl.uniprot.org/annotation/VAR_034745|||http://purl.uniprot.org/annotation/VSP_020574|||http://purl.uniprot.org/annotation/VSP_020575|||http://purl.uniprot.org/annotation/VSP_020576|||http://purl.uniprot.org/annotation/VSP_020577|||http://purl.uniprot.org/annotation/VSP_020578
http://togogenome.org/gene/9606:PIMREG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5C7|||http://purl.uniprot.org/uniprot/A0A0S2Z5F0|||http://purl.uniprot.org/uniprot/Q9BSJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||D-box 1|||D-box 2|||Disordered|||Great reduction in ubiquitination. Complete loss of ubiquitination; when associated with 14-A--A-17.|||In isoform 2.|||No effect on phosphorylation.|||Phosphoserine|||Phosphoserine; by UHMK1; in vitro|||Polar residues|||Protein PIMREG|||Reduced phosphorylation.|||Weak reduction in ubiquitination. Complete loss of ubiquitination; when associated with 53-A--A-56.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281159|||http://purl.uniprot.org/annotation/VAR_056873|||http://purl.uniprot.org/annotation/VSP_023997
http://togogenome.org/gene/9606:MDGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z553                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fibronectin type-III|||GPI-anchor amidated aspartate|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||In isoform 2.|||In isoform 3.|||MAM|||MAM domain-containing glycosylphosphatidylinositol anchor protein 2|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014859|||http://purl.uniprot.org/annotation/PRO_0000292043|||http://purl.uniprot.org/annotation/VAR_059400|||http://purl.uniprot.org/annotation/VSP_042468|||http://purl.uniprot.org/annotation/VSP_045240
http://togogenome.org/gene/9606:TBCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99426                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CAP-Gly|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PAK1|||Phosphotyrosine|||Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-128.|||Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-65.|||Tubulin-folding cofactor B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083534|||http://purl.uniprot.org/annotation/VSP_055521
http://togogenome.org/gene/9606:TRIM40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8U1|||http://purl.uniprot.org/uniprot/Q6P9F5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||E3 ubiquitin ligase TRIM40|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056260|||http://purl.uniprot.org/annotation/VAR_055309|||http://purl.uniprot.org/annotation/VAR_055310|||http://purl.uniprot.org/annotation/VAR_057222|||http://purl.uniprot.org/annotation/VSP_012131
http://togogenome.org/gene/9606:ALDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPN7|||http://purl.uniprot.org/uniprot/P05091                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase|||Aldehyde dehydrogenase, mitochondrial|||In AMEDS; allele ALDH2*2; drastic reduction of enzyme activity.|||In allele ALDH2*3.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Nucleophile|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007168|||http://purl.uniprot.org/annotation/VAR_002248|||http://purl.uniprot.org/annotation/VAR_011302|||http://purl.uniprot.org/annotation/VAR_011869|||http://purl.uniprot.org/annotation/VSP_046715
http://togogenome.org/gene/9606:CACNA1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43497                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium ion selectivity and permeability|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In SCA42; changed voltage-gated calcium channel activity; membrane potential dependency is shifted toward more positive potentials.|||In SCA42ND; gain-of-function mutation; results in slower channel inactivation and negatively shifted potential for half-inactivation.|||In isoform 1, isoform 2, isoform 3, isoform 4, isoform 8, isoform 9, isoform 10, isoform 21, isoform 26, isoform 27, isoform 28 and isoform 32.|||In isoform 1, isoform 2, isoform 4, isoform 6, isoform 9, isoform 11, isoform 13, isoform 14, isoform 16, isoform 17, isoform 18, isoform 20, isoform 21, isoform 22, isoform 23, isoform 25, isoform 33, isoform 34 and isoform 35.|||In isoform 1, isoform 4, isoform 6, isoform 7, isoform 8, isoform 18, isoform 19, isoform 24, isoform 25, isoform 31, isoform 32, isoform 34 and isoform 35.|||In isoform 10.|||In isoform 14 and isoform 16.|||In isoform 2, isoform 13, isoform 14, isoform 15, isoform 22, isoform 26 and isoform 29.|||In isoform 20.|||In isoform 21, isoform 22, isoform 23, isoform 24 and isoform 25.|||In isoform 26, isoform 28, isoform 29, isoform 30 and isoform 31.|||In isoform 27.|||In isoform 33 and isoform 35.|||In isoform 34.|||In isoform 4, isoform 17 and isoform 18.|||In isoform 7, isoform 8, isoform 12, isoform 15 and isoform 24.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Voltage-dependent T-type calcium channel subunit alpha-1G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053952|||http://purl.uniprot.org/annotation/VAR_076292|||http://purl.uniprot.org/annotation/VAR_081177|||http://purl.uniprot.org/annotation/VAR_081178|||http://purl.uniprot.org/annotation/VSP_000940|||http://purl.uniprot.org/annotation/VSP_000943|||http://purl.uniprot.org/annotation/VSP_000944|||http://purl.uniprot.org/annotation/VSP_000945|||http://purl.uniprot.org/annotation/VSP_000946|||http://purl.uniprot.org/annotation/VSP_000947|||http://purl.uniprot.org/annotation/VSP_000948|||http://purl.uniprot.org/annotation/VSP_047545|||http://purl.uniprot.org/annotation/VSP_047546|||http://purl.uniprot.org/annotation/VSP_047547|||http://purl.uniprot.org/annotation/VSP_047548|||http://purl.uniprot.org/annotation/VSP_047549|||http://purl.uniprot.org/annotation/VSP_047550|||http://purl.uniprot.org/annotation/VSP_047551|||http://purl.uniprot.org/annotation/VSP_047552|||http://purl.uniprot.org/annotation/VSP_047553
http://togogenome.org/gene/9606:MED7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43513|||http://purl.uniprot.org/uniprot/Q6IAZ5                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Mediator of RNA polymerase II transcription subunit 7|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079408
http://togogenome.org/gene/9606:GRAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8E3|||http://purl.uniprot.org/uniprot/O75791|||http://purl.uniprot.org/uniprot/Q6FI14                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRB2-related adapter protein 2|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SH2|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088208|||http://purl.uniprot.org/annotation/VAR_012079|||http://purl.uniprot.org/annotation/VSP_055234|||http://purl.uniprot.org/annotation/VSP_055235
http://togogenome.org/gene/9606:SLC66A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAA1|||http://purl.uniprot.org/uniprot/Q6ZP29                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes lysosomal localization.|||Abolishes uptake of arginine and lysine.|||Cytoplasmic|||Di-leucine motif|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Lysosomal amino acid transporter 1 homolog|||N-linked (GlcNAc...) asparagine|||PQ-loop 1|||PQ-loop 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282434|||http://purl.uniprot.org/annotation/VAR_031409|||http://purl.uniprot.org/annotation/VSP_024151|||http://purl.uniprot.org/annotation/VSP_024152
http://togogenome.org/gene/9606:CENPU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71F23                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Centromere protein U|||Disordered|||Failed to enhance the PLK1-dependent degradation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Insensitive to PLK1-induced degradation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PLK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247672|||http://purl.uniprot.org/annotation/VAR_027144|||http://purl.uniprot.org/annotation/VAR_027145|||http://purl.uniprot.org/annotation/VAR_027146|||http://purl.uniprot.org/annotation/VAR_048692|||http://purl.uniprot.org/annotation/VAR_048693|||http://purl.uniprot.org/annotation/VSP_020030|||http://purl.uniprot.org/annotation/VSP_053526|||http://purl.uniprot.org/annotation/VSP_053527
http://togogenome.org/gene/9606:HSP90AA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K9JA46|||http://purl.uniprot.org/uniprot/P07900|||http://purl.uniprot.org/uniprot/Q86SX1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATPase activity.|||Basic and acidic residues|||Disordered|||Essential for interaction with SGTA and TTC1|||Essential for interaction with SMYD3, TSC1 and STIP1/HOP|||Heat shock protein HSP 90-alpha|||Histidine kinase/HSP90-like ATPase|||Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2. Los of interaction with TSC1.|||In isoform 2.|||Interaction with FLCN and FNIP1|||Interaction with FNIP2 and TSC1|||Interaction with NR1D1|||Interaction with NR3C1|||Loss of S-nitrosylation.|||Loss of interaction with TOMM70.|||Loss of interaction with TOMM70. No effect on interaction with IRF3.|||Loss of interaction with TSC1 and increases interaction with AHSA1.|||Loss of interaction with TSC1.|||N6-acetyllysine|||No deffect on the interaction with TSC1.|||Phosphoserine|||Phosphothreonine; by PRKDC|||Phosphotyrosine|||Reduces ATPase activity and client protein activation.|||Removed|||Required for homodimerization|||S-nitrosocysteine|||Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2. No effect on interaction with TSC1.|||TPR repeat-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000062911|||http://purl.uniprot.org/annotation/VAR_082835|||http://purl.uniprot.org/annotation/VSP_026604
http://togogenome.org/gene/9606:SCARB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14108                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mass|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Does not prevent the targeting of the protein to lysosomes completely.|||Helical|||Important for interaction with GBA1|||In EPM4; no renal failure.|||In isoform 2.|||Lumenal|||Lysosome membrane protein 2|||May act as a modifier of Gaucher disease.|||N-linked (GlcNAc...) asparagine|||Normal targeting of the protein to lysosomes.|||Prevents the targeting of the protein to lysosomes.|||Some loss in the efficiency of targeting of the protein to lysosomes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144155|||http://purl.uniprot.org/annotation/VAR_066744|||http://purl.uniprot.org/annotation/VAR_066745|||http://purl.uniprot.org/annotation/VSP_044826
http://togogenome.org/gene/9606:CFAP126                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein Flattop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316972
http://togogenome.org/gene/9606:RAET1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD07                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MHC class I alpha-1 like; down-regulates the cell surface expression of KLRK1|||MHC class I alpha-2 like; down-regulates the cell surface expression of KLRK1|||N-linked (GlcNAc...) asparagine|||Retinoic acid early transcript 1E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019021|||http://purl.uniprot.org/annotation/VAR_020271|||http://purl.uniprot.org/annotation/VAR_024534|||http://purl.uniprot.org/annotation/VAR_024535|||http://purl.uniprot.org/annotation/VAR_024536|||http://purl.uniprot.org/annotation/VAR_050408|||http://purl.uniprot.org/annotation/VAR_050409|||http://purl.uniprot.org/annotation/VAR_061483|||http://purl.uniprot.org/annotation/VSP_010441|||http://purl.uniprot.org/annotation/VSP_010442|||http://purl.uniprot.org/annotation/VSP_010443|||http://purl.uniprot.org/annotation/VSP_045012|||http://purl.uniprot.org/annotation/VSP_059262|||http://purl.uniprot.org/annotation/VSP_059263
http://togogenome.org/gene/9606:NDUFB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75438                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118827|||http://purl.uniprot.org/annotation/VSP_037859
http://togogenome.org/gene/9606:IGDCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVU1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Immunoglobulin superfamily DCC subclass member 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014920|||http://purl.uniprot.org/annotation/VAR_060356
http://togogenome.org/gene/9606:SEPTIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNL2|||http://purl.uniprot.org/uniprot/Q8WYJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||G1 motif|||G3 motif|||G4 motif|||Great reduction in phosphorylation.|||Important for dimerization|||In isoform 2.|||No effect on phosphorylation.|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphothreonine|||Polar residues|||Septin-1|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173513|||http://purl.uniprot.org/annotation/VAR_051934|||http://purl.uniprot.org/annotation/VSP_038269|||http://purl.uniprot.org/annotation/VSP_038270
http://togogenome.org/gene/9606:HPS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YV9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  BLOC-2 complex member HPS6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084056
http://togogenome.org/gene/9606:IKBKG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1B1|||http://purl.uniprot.org/uniprot/Q9Y6K9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished ubiquitin-binding.|||Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level; when associated with R-285. No change in the ubiquitination level; when associated with R-115 or R-224.|||Abolishes MARCH2F-mediated K48-linked ubiquitination and subsequent suppression of antiviral and antibacterial innate immune response.|||Abolishes binding to polyubiquitin.|||Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B activity.|||CCHC NOA-type|||Complete loss of cleavage by HAV protease 3c.|||Decreased ability to activate NF-kappa-B. Important decrease in the ubiquitination level; when associated with R-399.|||Decreases ubiquitination and abolishes nuclear export.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin and interchain with MARCHF2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Greatly impairs tandem ubiquitin binding,impairs oligomerization, impairs TNF-induced NF-kappa-B activation.|||Greatly impairs tandem ubiquitin binding.|||Impairs binding to polyubiquitin.|||Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-329.|||Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin, impairs TNF-induced NF-kappa-B activation; when associated with A-336.|||Impairs tandem ubiquitin binding.|||In EDAID1.|||In EDAID1; abolishes binding to polyubiquitin ('K63'-linked and linear) and greatly impairs tandem ubiquitin binding.|||In EDAID1; loss of sumoylation.|||In IMD33.|||In IMD33; greatly impairs tandem ubiquitin binding. Impairs oligomerization, impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation.|||In IMD33; impairs tandem ubiquitin binding.|||In IP.|||In IP; diminishes interaction with TRAF6 and polyubiquitination, greatly impairs tandem ubiquitin binding. Impairs oligomerization, greatly impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation.|||In IP; impairs binding to ubiquitin.|||In IP; only 46.3% of the activation obtained with the wild-type protein.|||In IP; shows the same luciferase activity as the control.|||In isoform 2.|||In isoform 3.|||Increases formation of homodimers.|||Interaction with CHUK/IKBKB|||Interaction with CYLD|||Interaction with TANK|||Interchain|||Leucine-zipper|||MNo effet on oligomerization, preferentially binds tri-ubiquitin chains ('Lys-48' or 'Lys-63'-linked).|||NF-kappa-B essential modulator|||No change in the ubiquitination level; when associated with R-399.|||No effect on MARCH2F-mediated K48-linked ubiquitination.|||No effet on oligomerization,impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin, impairs TNF-induced NF-kappa-B activation.|||Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-277. No effect on MARCH2F-mediated K48-linked ubiquitination.|||Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphoserine; by IKKB|||Required for interaction with TNFAIP3|||Required for interaction with and ubiquitination by MARCHF2|||Self-association|||Ubiquitin-binding (UBAN)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096782|||http://purl.uniprot.org/annotation/VAR_009182|||http://purl.uniprot.org/annotation/VAR_011320|||http://purl.uniprot.org/annotation/VAR_011321|||http://purl.uniprot.org/annotation/VAR_011322|||http://purl.uniprot.org/annotation/VAR_011323|||http://purl.uniprot.org/annotation/VAR_011324|||http://purl.uniprot.org/annotation/VAR_011325|||http://purl.uniprot.org/annotation/VAR_011326|||http://purl.uniprot.org/annotation/VAR_026491|||http://purl.uniprot.org/annotation/VAR_026492|||http://purl.uniprot.org/annotation/VAR_026493|||http://purl.uniprot.org/annotation/VAR_026494|||http://purl.uniprot.org/annotation/VAR_026495|||http://purl.uniprot.org/annotation/VAR_026496|||http://purl.uniprot.org/annotation/VAR_031958|||http://purl.uniprot.org/annotation/VAR_031959|||http://purl.uniprot.org/annotation/VAR_031960|||http://purl.uniprot.org/annotation/VAR_042666|||http://purl.uniprot.org/annotation/VAR_072603|||http://purl.uniprot.org/annotation/VAR_072604|||http://purl.uniprot.org/annotation/VAR_072605|||http://purl.uniprot.org/annotation/VAR_072606|||http://purl.uniprot.org/annotation/VAR_072607|||http://purl.uniprot.org/annotation/VAR_072608|||http://purl.uniprot.org/annotation/VSP_041000|||http://purl.uniprot.org/annotation/VSP_041001|||http://purl.uniprot.org/annotation/VSP_041002
http://togogenome.org/gene/9606:ADAM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKD2|||http://purl.uniprot.org/uniprot/O75078                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 11|||Disordered|||EGF-like|||Extracellular|||Helical|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Required for localization to cerebellar cortex basket cell terminals. Also required for localization of KCNA1, KCNA2, DLG4 and ADAM22 to cerebellar cortex basket cell terminal perisomatic axons and pinceaux                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029074|||http://purl.uniprot.org/annotation/PRO_0000029075|||http://purl.uniprot.org/annotation/VAR_062669|||http://purl.uniprot.org/annotation/VSP_005472|||http://purl.uniprot.org/annotation/VSP_005473|||http://purl.uniprot.org/annotation/VSP_005474|||http://purl.uniprot.org/annotation/VSP_005475
http://togogenome.org/gene/9606:DNAJC5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7Z1|||http://purl.uniprot.org/uniprot/Q9UF47                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 5B|||J|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071055
http://togogenome.org/gene/9606:FBXO44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1P2|||http://purl.uniprot.org/uniprot/Q9H4M3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 44|||FBA|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119945|||http://purl.uniprot.org/annotation/VSP_011346|||http://purl.uniprot.org/annotation/VSP_011347
http://togogenome.org/gene/9606:POLR3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05423                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerase III subunit RPC4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073967
http://togogenome.org/gene/9606:MPP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3DX46|||http://purl.uniprot.org/uniprot/Q13368                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Guanylate kinase-like|||In isoform 2.|||L27|||L27 1|||L27 2|||MAGUK p55 subfamily member 3|||PDZ|||Phosphoserine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094575|||http://purl.uniprot.org/annotation/VAR_050014|||http://purl.uniprot.org/annotation/VSP_061794
http://togogenome.org/gene/9606:TOR4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXH8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Torsin-4A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287489
http://togogenome.org/gene/9606:THBS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H4Z8|||http://purl.uniprot.org/uniprot/P49746                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP C-terminal|||TSP type-3|||TSP type-3 1|||TSP type-3 2|||TSP type-3 3|||TSP type-3 4|||TSP type-3 5|||TSP type-3 6|||TSP type-3 7|||TSP type-3 8|||Thrombospondin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035849|||http://purl.uniprot.org/annotation/PRO_5003327266|||http://purl.uniprot.org/annotation/VAR_035808|||http://purl.uniprot.org/annotation/VAR_052658|||http://purl.uniprot.org/annotation/VSP_045328
http://togogenome.org/gene/9606:OXT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01178|||http://purl.uniprot.org/uniprot/X5D7M6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Gain of antagonist activity on V1aR/AVPR1A (and loss of agonist activity on this receptor). 310-fold decrease in affinity for oxytocin receptor (OXTR), 13-fold decrease in affinity for V1aR/AVPR1A, and complete loss of affinity for V1bR/AVPR1B and V2R/AVPR2.|||Glycine amide|||Neurophysin 1|||Oxytocin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020495|||http://purl.uniprot.org/annotation/PRO_0000020496|||http://purl.uniprot.org/annotation/PRO_5014316169
http://togogenome.org/gene/9606:GPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N158                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated glycine|||Glypican-2|||In a breast cancer sample; somatic mutation.|||O-linked (Xyl...) (heparan sulfate) serine|||Removed in mature form|||Secreted glypican-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012303|||http://purl.uniprot.org/annotation/PRO_0000012304|||http://purl.uniprot.org/annotation/PRO_0000333841|||http://purl.uniprot.org/annotation/VAR_036045
http://togogenome.org/gene/9606:PPP4R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||No effect on RPA2-binding, nor on PPP4C-binding.|||No effect on RPA2-binding; decrease in PPP4C-binding.|||No effect on RPA2-binding; loss of PPP4C-binding.|||Phosphoserine|||Polar residues|||Serine/threonine-protein phosphatase 4 regulatory subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299365|||http://purl.uniprot.org/annotation/VAR_034811|||http://purl.uniprot.org/annotation/VAR_051749|||http://purl.uniprot.org/annotation/VSP_027612|||http://purl.uniprot.org/annotation/VSP_027613
http://togogenome.org/gene/9606:POLE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR33                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  DNA polymerase epsilon subunit 4|||Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191746|||http://purl.uniprot.org/annotation/VAR_028050
http://togogenome.org/gene/9606:CCL27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ77|||http://purl.uniprot.org/uniprot/Q9Y4X3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  9-fold reduction in binding affinity for Link domain of TNFAIP6.|||C-C motif chemokine 27|||Chemokine interleukin-8-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005239|||http://purl.uniprot.org/annotation/PRO_5014310170|||http://purl.uniprot.org/annotation/VAR_022103|||http://purl.uniprot.org/annotation/VAR_022104
http://togogenome.org/gene/9606:USP34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70CQ2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of function.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249519|||http://purl.uniprot.org/annotation/VAR_047106|||http://purl.uniprot.org/annotation/VAR_047107|||http://purl.uniprot.org/annotation/VAR_047108|||http://purl.uniprot.org/annotation/VSP_020463|||http://purl.uniprot.org/annotation/VSP_035639|||http://purl.uniprot.org/annotation/VSP_035640
http://togogenome.org/gene/9606:RALGDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12967|||http://purl.uniprot.org/uniprot/Q8N4Y1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||N-terminal Ras-GEF|||Phosphotyrosine; by MET|||Polar residues|||Pro residues|||Ral guanine nucleotide dissociation stimulator|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068877|||http://purl.uniprot.org/annotation/VAR_035822|||http://purl.uniprot.org/annotation/VSP_035301|||http://purl.uniprot.org/annotation/VSP_043659|||http://purl.uniprot.org/annotation/VSP_055215|||http://purl.uniprot.org/annotation/VSP_055216|||http://purl.uniprot.org/annotation/VSP_055217
http://togogenome.org/gene/9606:SPSB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||Basic and acidic residues|||Disordered|||SOCS box|||SPRY domain-containing SOCS box protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238477
http://togogenome.org/gene/9606:NOX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3QRJ0|||http://purl.uniprot.org/uniprot/Q96PH1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-terminal catalytic dehydrogenase domain|||C-terminal lobe of N-terminal regulatory EF domain|||Cytoplasmic|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3; atypical; contains an insert of 28 residues|||EF-hand 4|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||In isoform v1, isoform v2 and isoform v6.|||In isoform v2 and isoform v4.|||In isoform v5.|||In isoform v6.|||Loss of CaMK2-mediated activation of its activity.|||Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-494 and A-498.|||Loss of activity but no effect on protein levels.|||Loss of binding of 1 calcium molecule. No effect on catalytic activity.|||N-terminal lobe of N-terminal regulatory EF domain|||N-terminal regulatory EF domain|||NADPH oxidase 5|||No effect on CaMK2-mediated activation of its activity.|||No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-490 and A-494.|||No effect on CaMK2-mediated activation of its activity. Loss of PKC/PRKCA-mediated activation of its activity; when associated with A-490 and A-498.|||No effect on cell membrane localization and catalytic activity.|||No effect on cell membrane localization but loss of catalytic activity.|||Phosphoserine; by CaMK2|||Phosphoserine; by CaMK2 and PKC/PRKCA|||Phosphothreonine; by CaMK2 and PKC/PRKCA|||Phosphothreonine; by PKC/PRKCA|||Reduced nitrosylation. Very significant loss of catalytic activity.|||S-nitrosocysteine|||Significant reduction in cell membrane localization and catalytic activity. No effect on calcium-dependent interaction between the N-terminal regulatory region and the C-terminal catalytic region.|||Significant reduction in cell membrane localization and catalytic activity. Reduced calcium-dependent interaction between the N-terminal regulatory region and the C-terminal catalytic region.|||Substantial loss of catalytic activity.|||Very significant loss of catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000224995|||http://purl.uniprot.org/annotation/VAR_055820|||http://purl.uniprot.org/annotation/VAR_055821|||http://purl.uniprot.org/annotation/VSP_017326|||http://purl.uniprot.org/annotation/VSP_017327|||http://purl.uniprot.org/annotation/VSP_017328|||http://purl.uniprot.org/annotation/VSP_041619
http://togogenome.org/gene/9606:BCKDHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKB3|||http://purl.uniprot.org/uniprot/B4E2N3|||http://purl.uniprot.org/uniprot/B7ZB80|||http://purl.uniprot.org/uniprot/P21953                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-oxoisovalerate dehydrogenase subunit beta, mitochondrial|||In MSUD1B.|||In MSUD1B; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In MSUD1B; unknown pathological significance; loss of 3-methyl-2-oxobutanoate dehydrogenase activity.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Transketolase-like pyrimidine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020470|||http://purl.uniprot.org/annotation/PRO_5007491843|||http://purl.uniprot.org/annotation/VAR_004974|||http://purl.uniprot.org/annotation/VAR_024851|||http://purl.uniprot.org/annotation/VAR_024852|||http://purl.uniprot.org/annotation/VAR_050437|||http://purl.uniprot.org/annotation/VAR_068348|||http://purl.uniprot.org/annotation/VAR_068349|||http://purl.uniprot.org/annotation/VAR_088297|||http://purl.uniprot.org/annotation/VSP_056370|||http://purl.uniprot.org/annotation/VSP_056371
http://togogenome.org/gene/9606:ANKRD52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWN0|||http://purl.uniprot.org/uniprot/Q8NB46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 24|||ANK 25|||ANK 26|||ANK 27|||ANK 28|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Basic and acidic residues|||Disordered|||Phosphoserine|||Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244587
http://togogenome.org/gene/9606:CDC25B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS38|||http://purl.uniprot.org/uniprot/B4DIG0|||http://purl.uniprot.org/uniprot/B4DQZ3|||http://purl.uniprot.org/uniprot/B4DRC3|||http://purl.uniprot.org/uniprot/E1YMX4|||http://purl.uniprot.org/uniprot/G8JLH2|||http://purl.uniprot.org/uniprot/P30305|||http://purl.uniprot.org/uniprot/Q6MZW8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 1 and isoform 4.|||In isoform 2.|||In isoform 4.|||M-phase inducer phosphatase 2|||Phosphoserine|||Phosphoserine; by AURKA|||Phosphoserine; by BRSK1 and MAPK14|||Phosphoserine; by MELK|||Phosphoserine; by MELK and MAPK14|||Polar residues|||Rhodanese                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198644|||http://purl.uniprot.org/annotation/VAR_020933|||http://purl.uniprot.org/annotation/VSP_000861|||http://purl.uniprot.org/annotation/VSP_000862|||http://purl.uniprot.org/annotation/VSP_012587
http://togogenome.org/gene/9606:THRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10828                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Impairs hormone binding and ligand-dependent conformational changes.|||In GRTHD.|||In GRTHD; impairs hormone binding and ligand-dependent conformational changes.|||In GRTHD; impairs hormone binding.|||In GRTHR.|||In PRTH.|||In PRTH; impairs hormone binding.|||In isoform Beta-2.|||Inhibits homodimer formation on a minimal response element (in vitro).|||Interaction with NR2F6|||Modestly inhibits homodimer formation on a minimal response element (in vitro).|||Modulating|||NR C4-type|||NR LBD|||No effect on thyroid hormone binding.|||Nuclear receptor|||Stabilizes homodimer.|||Thyroid hormone receptor beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053446|||http://purl.uniprot.org/annotation/VAR_004632|||http://purl.uniprot.org/annotation/VAR_004633|||http://purl.uniprot.org/annotation/VAR_004634|||http://purl.uniprot.org/annotation/VAR_004635|||http://purl.uniprot.org/annotation/VAR_004636|||http://purl.uniprot.org/annotation/VAR_004637|||http://purl.uniprot.org/annotation/VAR_004638|||http://purl.uniprot.org/annotation/VAR_004639|||http://purl.uniprot.org/annotation/VAR_004640|||http://purl.uniprot.org/annotation/VAR_004641|||http://purl.uniprot.org/annotation/VAR_004642|||http://purl.uniprot.org/annotation/VAR_004643|||http://purl.uniprot.org/annotation/VAR_004644|||http://purl.uniprot.org/annotation/VAR_004645|||http://purl.uniprot.org/annotation/VAR_004646|||http://purl.uniprot.org/annotation/VAR_004647|||http://purl.uniprot.org/annotation/VAR_004648|||http://purl.uniprot.org/annotation/VAR_004649|||http://purl.uniprot.org/annotation/VAR_004650|||http://purl.uniprot.org/annotation/VAR_004651|||http://purl.uniprot.org/annotation/VAR_004652|||http://purl.uniprot.org/annotation/VAR_004653|||http://purl.uniprot.org/annotation/VAR_004654|||http://purl.uniprot.org/annotation/VAR_004655|||http://purl.uniprot.org/annotation/VAR_011784|||http://purl.uniprot.org/annotation/VAR_050577|||http://purl.uniprot.org/annotation/VAR_058508|||http://purl.uniprot.org/annotation/VAR_059041|||http://purl.uniprot.org/annotation/VAR_059042|||http://purl.uniprot.org/annotation/VAR_059043|||http://purl.uniprot.org/annotation/VAR_059044|||http://purl.uniprot.org/annotation/VAR_059045|||http://purl.uniprot.org/annotation/VAR_059046|||http://purl.uniprot.org/annotation/VAR_059047|||http://purl.uniprot.org/annotation/VAR_059048|||http://purl.uniprot.org/annotation/VAR_059049|||http://purl.uniprot.org/annotation/VSP_031077
http://togogenome.org/gene/9606:NPIPB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MRT5|||http://purl.uniprot.org/uniprot/B4E0Y1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Nuclear pore complex-interacting protein family member B5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348052
http://togogenome.org/gene/9606:ITPRIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWB1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Inositol 1,4,5-trisphosphate receptor-interacting protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293728
http://togogenome.org/gene/9606:LMTK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWU2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In a lung large cell carcinoma sample; somatic mutation.|||Lumenal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase LMTK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259458|||http://purl.uniprot.org/annotation/VAR_028940|||http://purl.uniprot.org/annotation/VAR_028941|||http://purl.uniprot.org/annotation/VAR_028942|||http://purl.uniprot.org/annotation/VAR_041727|||http://purl.uniprot.org/annotation/VAR_041728|||http://purl.uniprot.org/annotation/VAR_041729|||http://purl.uniprot.org/annotation/VAR_041730|||http://purl.uniprot.org/annotation/VAR_041731|||http://purl.uniprot.org/annotation/VAR_041732|||http://purl.uniprot.org/annotation/VAR_041733|||http://purl.uniprot.org/annotation/VAR_041734|||http://purl.uniprot.org/annotation/VAR_041735|||http://purl.uniprot.org/annotation/VAR_041736
http://togogenome.org/gene/9606:KPRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T749                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Keratinocyte proline-rich protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271008|||http://purl.uniprot.org/annotation/VAR_029840|||http://purl.uniprot.org/annotation/VAR_029841|||http://purl.uniprot.org/annotation/VAR_029842|||http://purl.uniprot.org/annotation/VAR_029843|||http://purl.uniprot.org/annotation/VAR_029844|||http://purl.uniprot.org/annotation/VAR_029845
http://togogenome.org/gene/9606:PPM1K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3J5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Loss of activity.|||Mitochondrion|||PPM-type phosphatase|||Phosphoserine|||Polar residues|||Protein phosphatase 1K, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278208|||http://purl.uniprot.org/annotation/VAR_030691|||http://purl.uniprot.org/annotation/VAR_050621|||http://purl.uniprot.org/annotation/VAR_069736|||http://purl.uniprot.org/annotation/VSP_023156|||http://purl.uniprot.org/annotation/VSP_023157|||http://purl.uniprot.org/annotation/VSP_023158|||http://purl.uniprot.org/annotation/VSP_023159
http://togogenome.org/gene/9606:DNAJC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6AHX3|||http://purl.uniprot.org/uniprot/Q9H3Z4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 5|||Helical|||In CLN4B; results in near absence of palmitoylated monomeric forms of the protein and formation of high molecular mass aggregates with diffuse intracellular localization.|||In isoform 2.|||Increased syntaxin binding.|||J|||N6-acetyllysine|||No effect on oligomerization.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071052|||http://purl.uniprot.org/annotation/VAR_066555|||http://purl.uniprot.org/annotation/VAR_066556|||http://purl.uniprot.org/annotation/VSP_001292
http://togogenome.org/gene/9606:ALPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QP1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the serine/threonine-protein kinase and ability to initiate the innate immune response.|||Alpha-protein kinase 1|||Alpha-type protein kinase|||Disordered|||Impaired ADP-D-glycero-beta-D-manno-heptose-binding and ability to activate the serine/threonine-protein kinase activity.|||Impaired ADP-D-glycero-beta-D-manno-heptose-binding and ability to activate the serine/threonine-protein kinase activity; when associated with A-231.|||Impaired ADP-D-glycero-beta-D-manno-heptose-binding and ability to activate the serine/threonine-protein kinase activity; when associated with A-67.|||Impaired ADP-D-glycero-beta-D-manno-heptose-binding and ability to activate the serine/threonine-protein kinase activity; when associated with E-237.|||Impaired ADP-D-glycero-beta-D-manno-heptose-binding and ability to activate the serine/threonine-protein kinase activity; when associated with K-295.|||In ROSAH.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260028|||http://purl.uniprot.org/annotation/VAR_028982|||http://purl.uniprot.org/annotation/VAR_028983|||http://purl.uniprot.org/annotation/VAR_028984|||http://purl.uniprot.org/annotation/VAR_028985|||http://purl.uniprot.org/annotation/VAR_028986|||http://purl.uniprot.org/annotation/VAR_028987|||http://purl.uniprot.org/annotation/VAR_028988|||http://purl.uniprot.org/annotation/VAR_041511|||http://purl.uniprot.org/annotation/VAR_041512|||http://purl.uniprot.org/annotation/VAR_041513|||http://purl.uniprot.org/annotation/VAR_041514|||http://purl.uniprot.org/annotation/VAR_041515|||http://purl.uniprot.org/annotation/VAR_041516|||http://purl.uniprot.org/annotation/VAR_041517|||http://purl.uniprot.org/annotation/VAR_041518|||http://purl.uniprot.org/annotation/VAR_041519|||http://purl.uniprot.org/annotation/VAR_041520|||http://purl.uniprot.org/annotation/VAR_041521|||http://purl.uniprot.org/annotation/VAR_041522|||http://purl.uniprot.org/annotation/VAR_041523|||http://purl.uniprot.org/annotation/VAR_057741|||http://purl.uniprot.org/annotation/VAR_084993|||http://purl.uniprot.org/annotation/VSP_044735
http://togogenome.org/gene/9606:SFR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XK3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Swi5-dependent recombination DNA repair protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089805|||http://purl.uniprot.org/annotation/VAR_023098|||http://purl.uniprot.org/annotation/VSP_040037|||http://purl.uniprot.org/annotation/VSP_040038
http://togogenome.org/gene/9606:MMP27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H306                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Loss of N-glycosylation; when associated with Q-110 and Q-452.|||Loss of N-glycosylation; when associated with Q-55 and Q-110.|||Loss of N-glycosylation; when associated with Q-55 and Q-452.|||Matrix metalloproteinase-27|||N-linked (GlcNAc...) asparagine|||Required for retention in the endoplasmic reticulum|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287561|||http://purl.uniprot.org/annotation/PRO_0000287562|||http://purl.uniprot.org/annotation/VAR_032326|||http://purl.uniprot.org/annotation/VAR_032327|||http://purl.uniprot.org/annotation/VAR_032328|||http://purl.uniprot.org/annotation/VAR_032329|||http://purl.uniprot.org/annotation/VAR_032330|||http://purl.uniprot.org/annotation/VAR_032331|||http://purl.uniprot.org/annotation/VAR_032332
http://togogenome.org/gene/9606:P2RY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47900                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of ADP analog binding.|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 1|||Strongly decreased affinity for ADP analog.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070006
http://togogenome.org/gene/9606:TUBA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68363                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||5-glutamyl polyglutamate|||Abolished GTPase activity; microtubules have an expanded lattice with a negative twist and display high binding to microtubule-end binding proteins such as MAPRE3.|||Abolished GTPase activity; microtubules have an expanded lattice with a positive twist and display low binding to microtubule-end binding proteins such as MAPRE3.|||Detyrosinated tubulin alpha-1B chain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Involved in polymerization|||MREC motif|||N6,N6,N6-trimethyllysine; alternate|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Tubulin alpha-1B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048108|||http://purl.uniprot.org/annotation/PRO_0000437384|||http://purl.uniprot.org/annotation/VSP_055764
http://togogenome.org/gene/9606:AP1S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHW1|||http://purl.uniprot.org/uniprot/P56377|||http://purl.uniprot.org/uniprot/Q549M9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP complex mu/sigma subunit|||AP-1 complex subunit sigma-2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193799|||http://purl.uniprot.org/annotation/VSP_053671|||http://purl.uniprot.org/annotation/VSP_053672
http://togogenome.org/gene/9606:SIRT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6E7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Transit Peptide                                                                                  ^@                                                                                  Abolishes inhibition of PDH complex activity.|||Deacetylase sirtuin-type|||Mitochondrion|||NAD-dependent protein lipoamidase sirtuin-4, mitochondrial|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110264
http://togogenome.org/gene/9606:CHRM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20309                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basolateral sorting signal|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of basolateral sorting.|||Loss of basolateral sorting. No effect on basolateral sorting; when associated with L-280 and L-281.|||Muscarinic acetylcholine receptor M3|||N-linked (GlcNAc...) asparagine|||No effect on basolateral sorting.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069029|||http://purl.uniprot.org/annotation/VAR_033461|||http://purl.uniprot.org/annotation/VAR_049368
http://togogenome.org/gene/9606:BCL2L14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZR8                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Splice Variant                                                                                  ^@                                                                                  Apoptosis facilitator Bcl-2-like protein 14|||BH2|||BH3|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143075|||http://purl.uniprot.org/annotation/VSP_012239|||http://purl.uniprot.org/annotation/VSP_012240|||http://purl.uniprot.org/annotation/VSP_012241|||http://purl.uniprot.org/annotation/VSP_012242
http://togogenome.org/gene/9606:SON                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QSZ5|||http://purl.uniprot.org/uniprot/P18583|||http://purl.uniprot.org/uniprot/Q6ZRV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-10|||1-11|||1-12|||1-13|||1-14|||1-2|||1-3|||1-4|||1-5|||1-6|||1-7|||1-8|||1-9|||11 X 7 AA tandem repeats of [DR]-P-Y-R-[LI][AG][QHP]|||14 X 6 AA repeats of [ED]-R-S-M-M-S|||17 X 10 AA tandem repeats of L-A-[ST]-[NSG]-[TS]-MDSQM|||2 X 19 AA repeats of P-S-R-R-R-R-S-R-S-V-V-R-R-R-S-F-S-I-S|||2-1|||2-2|||2-3|||2-4|||2-5|||2-6|||2-7|||3 X 11 AA tandem repats of P-P-L-P-P-E-E-P-P-[TME]-[MTG]|||3 X tandem repeats of [ST]-P-[VLI]-R-[RL]-[RK]-[RF]-S-R|||3-1|||3-2|||4 X 8 AA tandem repeats of V-L-E-SS-[AVT]-VT|||7 X 7 AA repeats of P-S-R-R-S-R-[TS]|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||DRBM|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In ZTTKS; unknown pathological significance; de novo mutation associated in cis with S-1637.|||In ZTTKS; unknown pathological significance; de novo mutation associated in cis with Y-1843.|||In isoform A and isoform D.|||In isoform A.|||In isoform B.|||In isoform C.|||In isoform E.|||In isoform G.|||In isoform H.|||In isoform I.|||In isoform J.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein SON|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072037|||http://purl.uniprot.org/annotation/VAR_056990|||http://purl.uniprot.org/annotation/VAR_056991|||http://purl.uniprot.org/annotation/VAR_065456|||http://purl.uniprot.org/annotation/VAR_065457|||http://purl.uniprot.org/annotation/VAR_065458|||http://purl.uniprot.org/annotation/VAR_077864|||http://purl.uniprot.org/annotation/VAR_077865|||http://purl.uniprot.org/annotation/VSP_004401|||http://purl.uniprot.org/annotation/VSP_004402|||http://purl.uniprot.org/annotation/VSP_004403|||http://purl.uniprot.org/annotation/VSP_004404|||http://purl.uniprot.org/annotation/VSP_004405|||http://purl.uniprot.org/annotation/VSP_004406|||http://purl.uniprot.org/annotation/VSP_004407|||http://purl.uniprot.org/annotation/VSP_004408|||http://purl.uniprot.org/annotation/VSP_004409|||http://purl.uniprot.org/annotation/VSP_004410|||http://purl.uniprot.org/annotation/VSP_004411|||http://purl.uniprot.org/annotation/VSP_004412|||http://purl.uniprot.org/annotation/VSP_004413|||http://purl.uniprot.org/annotation/VSP_004414|||http://purl.uniprot.org/annotation/VSP_004415
http://togogenome.org/gene/9606:FAM151A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW52                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Protein FAM151A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310955|||http://purl.uniprot.org/annotation/VAR_037109|||http://purl.uniprot.org/annotation/VAR_037110|||http://purl.uniprot.org/annotation/VAR_037111|||http://purl.uniprot.org/annotation/VAR_037112|||http://purl.uniprot.org/annotation/VAR_037113|||http://purl.uniprot.org/annotation/VAR_037114|||http://purl.uniprot.org/annotation/VSP_029357
http://togogenome.org/gene/9606:ADSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R5Q7|||http://purl.uniprot.org/uniprot/P30520                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylosuccinate synthetase isozyme 2|||Disordered|||Proton acceptor|||Proton donor|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095130|||http://purl.uniprot.org/annotation/VAR_051881
http://togogenome.org/gene/9606:DUOXA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1HG44                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dual oxidase maturation factor 2|||Extracellular|||Helical|||In TDH5; unknown pathological significance; impairs hydrogen peroxide metabolic process.|||In isoform 2.|||Interchain (with C-568 in DUXA2)|||Interchain (with C-582 in DUXA2)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264245|||http://purl.uniprot.org/annotation/VAR_047367|||http://purl.uniprot.org/annotation/VAR_074025|||http://purl.uniprot.org/annotation/VSP_046554|||http://purl.uniprot.org/annotation/VSP_046555
http://togogenome.org/gene/9606:IKBKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14920                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-acetylthreonine; by Yersinia YopJ|||COmplete loss of TBK1-mediated phosphorylation.|||Decrease of activity.|||Disordered|||Full activation. Interaction with TRIM21 is enhanced; when associated with E-177. Monoubiquitinated; when associated with R-163 and E-177. Strongly promoted NF-kappa-B gene expression; when associated with E-177.|||Full activation. Interaction with TRIM21 is enhanced; when associated with E-181. Monoubiquitinated; when associated with R-163 and E-181. Strongly promoted NF-kappa-B gene expression; when associated with E-181.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Hydroxyproline|||In IMD15A; gain-of-function mutation resulting in increased activation of NF-kappa-B signaling pathway.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased activation of NF-kappa-B signaling.|||Inhibitor of nuclear factor kappa-B kinase subunit beta|||Leucine-zipper|||Loss of activation of NF-kappa-B signaling.|||Loss of hypoxic inducibility.|||Loss of kinase activity and no effect on binding to NIK.|||Loss of protein kinase activity.|||Monoubiquitinated; when associated with E-177 and E-181.|||NEMO-binding|||Phosphoserine|||Phosphoserine; by TBK1 and PKC/PRKCZ|||Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086013|||http://purl.uniprot.org/annotation/VAR_021124|||http://purl.uniprot.org/annotation/VAR_035626|||http://purl.uniprot.org/annotation/VAR_040567|||http://purl.uniprot.org/annotation/VAR_040568|||http://purl.uniprot.org/annotation/VAR_040569|||http://purl.uniprot.org/annotation/VAR_040570|||http://purl.uniprot.org/annotation/VAR_051628|||http://purl.uniprot.org/annotation/VAR_081275|||http://purl.uniprot.org/annotation/VSP_041825|||http://purl.uniprot.org/annotation/VSP_041826|||http://purl.uniprot.org/annotation/VSP_041827|||http://purl.uniprot.org/annotation/VSP_043408
http://togogenome.org/gene/9606:EED                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJK2|||http://purl.uniprot.org/uniprot/O75530                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to H3K27me3.|||Disordered|||Impairs interaction with EZH2.|||Impairs interaction with the matrix protein MA of HIV-1.|||In COGIS.|||In COGIS; decreased trimethylation of 'Lys-27' of histone H3.|||In COGIS; decreased trimethylation of 'Lys-27' of histone H3; no effect on interaction with EZH2.|||In isoform 2.|||In isoform 3.|||Interaction with EZH2|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-methyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polycomb protein EED|||Removed|||Required for interaction with the matrix protein MA of HIV-1|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343725|||http://purl.uniprot.org/annotation/VAR_078316|||http://purl.uniprot.org/annotation/VAR_078317|||http://purl.uniprot.org/annotation/VAR_079255|||http://purl.uniprot.org/annotation/VAR_079256|||http://purl.uniprot.org/annotation/VAR_079257|||http://purl.uniprot.org/annotation/VAR_079258|||http://purl.uniprot.org/annotation/VSP_034691|||http://purl.uniprot.org/annotation/VSP_034692
http://togogenome.org/gene/9606:HDAC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCQ6|||http://purl.uniprot.org/uniprot/Q96DB2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Histone deacetylase|||Histone deacetylase 11|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114715|||http://purl.uniprot.org/annotation/VSP_043082|||http://purl.uniprot.org/annotation/VSP_043083
http://togogenome.org/gene/9606:PRKN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60260|||http://purl.uniprot.org/uniprot/X5DR79                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Decreased autoinhibition and increased E3 activity.|||Disordered|||E3 ubiquitin-protein ligase parkin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||IBR-type|||Impaired activity.|||Impairs folding of IBR domain.|||Impairs protein folding.|||Impairs the ability of self-ubiquitination and to ubiquitinate SNCAIP.|||Impairs the ability to ubiquitinate SNCAIP.|||Impairs the ability to ubiquitinate target proteins. No effect on translocation to mitochondria.|||In PARK2 and PARK; at heterozygosity it is associated with late onset Parkinson disease; impairs the ability to ubiquitinate SNCAIP and ZNF746; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression.|||In PARK2 and PARK; at heterozygosity it is associated with late onset Parkinson disease; impairs the ability to ubiquitinate SNCAIP; abolishes p53/TP53 transcriptional repression; impairs the ability to ubiquitinate and degrade SYT11.|||In PARK2 and PARK; induces a conformational change in the PSMD4-binding site of Ubl resulting in impaired proteasomal binding; decreases ubiquitination and degradation; increased aggregation; impairs the ability to ubiquitinate and degrade SYT11.|||In PARK2.|||In PARK2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression.|||In PARK2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression; fails to ubiquitinate SYT11 but does not loose ability to bind SYT11.|||In PARK2; does not affect PINK-1 dependent localization to depolarized mitochondria.|||In PARK2; impaired E3 ubiquitin-protein ligase toward BCL2.|||In PARK2; impaired E3 ubiquitin-protein ligase toward ZNF746 and BCL2.|||In PARK2; impairs PINK1-dependent localization to dysfunctional depolarized mitochondria; impaired E3 ubiquitin-protein ligase toward ZNF746.|||In PARK2; impairs folding of IBR domain.|||In PARK2; impairs the ability to ubiquitinate SNCAIP and BCL2; loss of UBE2L3 binding; severely compromises the mitochondrial localization.|||In PARK2; impairs the ability to ubiquitinate SNCAIP; does not affect turnover of CDCRE1; impairs PINK1-dependent localization to dysfunctional depolarized mitochondria.|||In PARK2; increased aggregation; fails to ubiquitinate SYT11; loses ability to bind SYT11; impaired relocalization to damaged mitochondria; loss of function in mitophagy.|||In PARK2; severely compromises the mitochondrial localization; fails to stabilize BCL2.|||In PARK2; severely compromises the mitochondrial localization; fails to stabilize BCL2; decreased binding to the TP53 promoter; abolishes TP53 transcriptional repression.|||In PARK2; unknown pathological significance.|||In PARK; does not affect PINK-1 dependent localization to depolarized mitochondria.|||In PARK; late onset.|||In a patient with Parkinson disease; unknown pathological significance.|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||Loss of activity and self-ubiquitination. Loss of monoubiquitination resulting in an increase in apoptosis. No effect on polyubiquitination or mitophagy.|||Loss of activity towards MIRO1.|||Loss of activity.|||Loss of mitochondrial localization.|||Loss of phosphorylation. Reduced mitochondrial localization; when associated with A-175.|||Loss of phosphorylation. Reduced mitochondrial localization; when associated with A-217.|||Loss of phosphorylation. Undergoes autoubiquitination in the presence of phosphorylated ubiquitin.|||Loss of self-ubiquitination.|||Necessary for PINK1-dependent localization to mitochondria|||Phosphomimetic mutant. Mostly localizes to the mitochondria; when associated with E-175.|||Phosphomimetic mutant. Mostly localizes to the mitochondria; when associated with E-217.|||Phosphomimetic mutant; still requires PINK1 for activation. PRKN is activated in presence of phosphorylated ubiquitin.|||Phosphoserine; by PINK1|||Phosphothreonine|||Phosphothreonine; by PINK1|||REP|||RING-type|||RING-type 0; atypical|||RING-type 1|||RING-type 2; atypical|||Reduced self-ubiquitination.|||SYT11 binding 1|||SYT11 binding 2|||TRIAD supradomain|||Ubiquitin-like ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058576|||http://purl.uniprot.org/annotation/VAR_019733|||http://purl.uniprot.org/annotation/VAR_019734|||http://purl.uniprot.org/annotation/VAR_019735|||http://purl.uniprot.org/annotation/VAR_019736|||http://purl.uniprot.org/annotation/VAR_019737|||http://purl.uniprot.org/annotation/VAR_019738|||http://purl.uniprot.org/annotation/VAR_019739|||http://purl.uniprot.org/annotation/VAR_019740|||http://purl.uniprot.org/annotation/VAR_019741|||http://purl.uniprot.org/annotation/VAR_019742|||http://purl.uniprot.org/annotation/VAR_019743|||http://purl.uniprot.org/annotation/VAR_019744|||http://purl.uniprot.org/annotation/VAR_019746|||http://purl.uniprot.org/annotation/VAR_019747|||http://purl.uniprot.org/annotation/VAR_019748|||http://purl.uniprot.org/annotation/VAR_019749|||http://purl.uniprot.org/annotation/VAR_019750|||http://purl.uniprot.org/annotation/VAR_019751|||http://purl.uniprot.org/annotation/VAR_019752|||http://purl.uniprot.org/annotation/VAR_019753|||http://purl.uniprot.org/annotation/VAR_019754|||http://purl.uniprot.org/annotation/VAR_019755|||http://purl.uniprot.org/annotation/VAR_019756|||http://purl.uniprot.org/annotation/VAR_019757|||http://purl.uniprot.org/annotation/VAR_019758|||http://purl.uniprot.org/annotation/VAR_019759|||http://purl.uniprot.org/annotation/VAR_019760|||http://purl.uniprot.org/annotation/VAR_019761|||http://purl.uniprot.org/annotation/VAR_019762|||http://purl.uniprot.org/annotation/VAR_019763|||http://purl.uniprot.org/annotation/VAR_019764|||http://purl.uniprot.org/annotation/VAR_019765|||http://purl.uniprot.org/annotation/VAR_019766|||http://purl.uniprot.org/annotation/VAR_019767|||http://purl.uniprot.org/annotation/VAR_054107|||http://purl.uniprot.org/annotation/VAR_062672|||http://purl.uniprot.org/annotation/VAR_062673|||http://purl.uniprot.org/annotation/VAR_070078|||http://purl.uniprot.org/annotation/VAR_070079|||http://purl.uniprot.org/annotation/VAR_070080|||http://purl.uniprot.org/annotation/VSP_011705|||http://purl.uniprot.org/annotation/VSP_011706|||http://purl.uniprot.org/annotation/VSP_011707|||http://purl.uniprot.org/annotation/VSP_011708|||http://purl.uniprot.org/annotation/VSP_011709|||http://purl.uniprot.org/annotation/VSP_011710|||http://purl.uniprot.org/annotation/VSP_011711|||http://purl.uniprot.org/annotation/VSP_011712|||http://purl.uniprot.org/annotation/VSP_041563|||http://purl.uniprot.org/annotation/VSP_053651
http://togogenome.org/gene/9606:MYF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23409                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with centronuclear myopathy; also identified in a Becker muscular dystrophy patient; unknown pathological significance.|||Myogenic factor 6|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127351|||http://purl.uniprot.org/annotation/VAR_004493|||http://purl.uniprot.org/annotation/VAR_004494
http://togogenome.org/gene/9606:TMEM91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNR0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Transmembrane protein 91                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135699|||http://purl.uniprot.org/annotation/VSP_042819|||http://purl.uniprot.org/annotation/VSP_045717|||http://purl.uniprot.org/annotation/VSP_047211|||http://purl.uniprot.org/annotation/VSP_047212
http://togogenome.org/gene/9606:XYLT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT06|||http://purl.uniprot.org/uniprot/Q9H1B5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In PXE; acts as a modifier of disease severity; more frequent in patients with a severe disease course.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Xylosyltransferase 2|||Xylosyltransferase C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191406|||http://purl.uniprot.org/annotation/VAR_022453|||http://purl.uniprot.org/annotation/VAR_022454|||http://purl.uniprot.org/annotation/VAR_049328|||http://purl.uniprot.org/annotation/VAR_071276|||http://purl.uniprot.org/annotation/VAR_071277|||http://purl.uniprot.org/annotation/VAR_071278|||http://purl.uniprot.org/annotation/VSP_013758|||http://purl.uniprot.org/annotation/VSP_013759
http://togogenome.org/gene/9606:DPP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHL4                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Dipeptidyl peptidase 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027314|||http://purl.uniprot.org/annotation/PRO_0000027315|||http://purl.uniprot.org/annotation/VAR_047087
http://togogenome.org/gene/9606:DESI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSY9                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Deubiquitinase DESI2|||Disordered|||In isoform 2.|||Loss of deubiquitination activity.|||PPPDE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221630|||http://purl.uniprot.org/annotation/VSP_011422
http://togogenome.org/gene/9606:CDKN2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55273                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase 4 inhibitor D|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144188
http://togogenome.org/gene/9606:RGMB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNF6|||http://purl.uniprot.org/uniprot/Q6NW40                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Disordered|||GPI-anchor amidated asparagine|||Introduces a N-linked glycan; changes interaction with NEO1 from a 2:2 to a 1:1 stoichiometry.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Removed in mature form|||Repulsive guidance molecule B|||Repulsive guidance molecule C-terminal|||Repulsive guidance molecule N-terminal|||Severely impairs interaction with NEO1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030394|||http://purl.uniprot.org/annotation/PRO_0000030395
http://togogenome.org/gene/9606:USB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BN52|||http://purl.uniprot.org/uniprot/H3BNM8|||http://purl.uniprot.org/uniprot/Q9BQ65                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes exoribonuclease activity. Does not rescue the molecular phenotype caused by USB1 depletion. Does not restore U6 snRNA processing when expressed in deleted mpn1 yeast cells; when associated with A-120. Increases the accumulation of unspliced pre-mRNAs when expressed in deleted mpn1 yeast cells; when associated with A-120. Slows growth in the cold when expressed in deleted mpn1 yeast cells; when associated with A-120. Abolishes exoribonuclease activity; when associated with A-120. Decreases U6 and U6atac motility.|||Abolishes exoribonuclease activity. Does not restore U6 snRNA processing when expressed in deleted mpn1 yeast cells; when associated with A-208. Increases the accumulation of unspliced pre-mRNAs when expressed in deleted mpn1 yeast cells; when associated with A-208. Slows growth in the cold when expressed in deleted mpn1 yeast cells; when associated with A-208. Abolishes exoribonuclease activity; when associated with A-208. Decreases U6 and U6atac motility.|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of exonuclease activity.|||Polar residues|||Proton acceptor|||Proton donor|||Proton donor/acceptor|||Significantly decreases exonuclease activity.|||U6 snRNA phosphodiesterase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274391|||http://purl.uniprot.org/annotation/VAR_030277|||http://purl.uniprot.org/annotation/VAR_053822|||http://purl.uniprot.org/annotation/VSP_042878|||http://purl.uniprot.org/annotation/VSP_042936
http://togogenome.org/gene/9606:FITM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6M3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-coenzyme A diphosphatase FITM2|||Cytoplasmic|||Helical|||In SIDDIS.|||Loss of oleoyl-CoA diphosphatase activity; when associated with A-155. Impaired ER morphology, ER homeostasis and lipid droplet biogenesis. No difference in the appearance of the Golgi apparatus, lysosomes or peroxisomes.|||Loss of oleoyl-CoA diphosphatase activity; when associated with A-214. Impaired ER morphology. No difference in the appearance of the Golgi apparatus, lysosomes or peroxisomes.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021035|||http://purl.uniprot.org/annotation/VAR_081219|||http://purl.uniprot.org/annotation/VAR_083498|||http://purl.uniprot.org/annotation/VAR_083499
http://togogenome.org/gene/9606:ERVV-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6SEH8|||http://purl.uniprot.org/uniprot/M9QQA5                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Endogenous retrovirus group V member 1 Env polyprotein|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411000|||http://purl.uniprot.org/annotation/PRO_5004101998
http://togogenome.org/gene/9606:CFAP91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4T9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 91|||Disordered|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064417|||http://purl.uniprot.org/annotation/VAR_030243|||http://purl.uniprot.org/annotation/VAR_030244|||http://purl.uniprot.org/annotation/VAR_030245|||http://purl.uniprot.org/annotation/VSP_014907|||http://purl.uniprot.org/annotation/VSP_014910|||http://purl.uniprot.org/annotation/VSP_014911|||http://purl.uniprot.org/annotation/VSP_039503|||http://purl.uniprot.org/annotation/VSP_039504|||http://purl.uniprot.org/annotation/VSP_059499|||http://purl.uniprot.org/annotation/VSP_059500
http://togogenome.org/gene/9606:UBE4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95155                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by caspase-3 and caspase-7.|||Abolishes cleavage by caspase-6 and granzyme B.|||Abolishes cleavage by caspase-6. No effect on cleavage by granzyme B.|||Basic and acidic residues|||Cleavage; by caspase-3 and caspase-7|||Cleavage; by caspase-6 and granzyme B|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues|||U-box|||Ubiquitin conjugation factor E4 B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194993|||http://purl.uniprot.org/annotation/VAR_052437|||http://purl.uniprot.org/annotation/VSP_007101|||http://purl.uniprot.org/annotation/VSP_007102|||http://purl.uniprot.org/annotation/VSP_007103|||http://purl.uniprot.org/annotation/VSP_053372
http://togogenome.org/gene/9606:CRMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT07|||http://purl.uniprot.org/uniprot/B3KV96|||http://purl.uniprot.org/uniprot/E9PD68|||http://purl.uniprot.org/uniprot/Q14194|||http://purl.uniprot.org/uniprot/Q96I11|||http://purl.uniprot.org/uniprot/X5DNI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2.5-fold increase in cells with a defect of cytokinesis.|||3'-nitrotyrosine|||Amidohydrolase-related|||Basic and acidic residues|||Dihydropyrimidinase-related protein 1|||Disordered|||In isoform LCRMP-1.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by AURKA|||Phosphotyrosine|||Polar residues|||Required for interaction with FLNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165909|||http://purl.uniprot.org/annotation/VAR_037745|||http://purl.uniprot.org/annotation/VSP_042545
http://togogenome.org/gene/9606:MUC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3R2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Helical|||Mucin-13|||N-linked (GlcNAc...) asparagine|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019284|||http://purl.uniprot.org/annotation/VAR_056589|||http://purl.uniprot.org/annotation/VAR_056590|||http://purl.uniprot.org/annotation/VAR_056591|||http://purl.uniprot.org/annotation/VAR_063124
http://togogenome.org/gene/9606:PKDCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504Y2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Extracellular tyrosine-protein kinase PKDCC|||In RLSDF.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263010|||http://purl.uniprot.org/annotation/VAR_083938
http://togogenome.org/gene/9606:TIGD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY51                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||Tigger transposable element-derived protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272616|||http://purl.uniprot.org/annotation/VAR_030042|||http://purl.uniprot.org/annotation/VAR_057509|||http://purl.uniprot.org/annotation/VAR_057510
http://togogenome.org/gene/9606:AQP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13520                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||NPA 1|||NPA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063955|||http://purl.uniprot.org/annotation/VAR_047233
http://togogenome.org/gene/9606:NUDT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G61                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Diphosphoinositol polyphosphate phosphohydrolase 3-beta|||Disordered|||Nudix box|||Nudix hydrolase|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057065|||http://purl.uniprot.org/annotation/VAR_022738
http://togogenome.org/gene/9606:ZNF433                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JQA6|||http://purl.uniprot.org/uniprot/F8VTV7|||http://purl.uniprot.org/uniprot/F8W0C9|||http://purl.uniprot.org/uniprot/Q8N7K0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 433                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047581|||http://purl.uniprot.org/annotation/PRO_5040053924|||http://purl.uniprot.org/annotation/VSP_035523
http://togogenome.org/gene/9606:PDIA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14554                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Prevents secretion from ER|||Protein disulfide-isomerase A5|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034233|||http://purl.uniprot.org/annotation/VAR_052581|||http://purl.uniprot.org/annotation/VSP_056536|||http://purl.uniprot.org/annotation/VSP_056537
http://togogenome.org/gene/9606:LEMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68G75                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||LEM|||LEM domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285247|||http://purl.uniprot.org/annotation/VAR_031999|||http://purl.uniprot.org/annotation/VSP_024846|||http://purl.uniprot.org/annotation/VSP_024847|||http://purl.uniprot.org/annotation/VSP_024848|||http://purl.uniprot.org/annotation/VSP_024849|||http://purl.uniprot.org/annotation/VSP_024850|||http://purl.uniprot.org/annotation/VSP_024851|||http://purl.uniprot.org/annotation/VSP_024852|||http://purl.uniprot.org/annotation/VSP_024853|||http://purl.uniprot.org/annotation/VSP_024854
http://togogenome.org/gene/9606:SUOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51687                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cytochrome b5 heme-binding|||Hinge|||Homodimerization|||In ISOD.|||In ISOD; 2% of activity.|||Mitochondrion|||Moco domain|||Phosphoserine|||Sulfite oxidase, mitochondrial|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006481|||http://purl.uniprot.org/annotation/VAR_002200|||http://purl.uniprot.org/annotation/VAR_002201|||http://purl.uniprot.org/annotation/VAR_002202|||http://purl.uniprot.org/annotation/VAR_002203|||http://purl.uniprot.org/annotation/VAR_015724|||http://purl.uniprot.org/annotation/VAR_015725|||http://purl.uniprot.org/annotation/VAR_015726|||http://purl.uniprot.org/annotation/VAR_015727|||http://purl.uniprot.org/annotation/VAR_015728|||http://purl.uniprot.org/annotation/VAR_015729|||http://purl.uniprot.org/annotation/VAR_015730
http://togogenome.org/gene/9606:RSL1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76021                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ribosomal L1 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125844|||http://purl.uniprot.org/annotation/VSP_056143
http://togogenome.org/gene/9606:C11orf65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCR3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein MFI                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263665|||http://purl.uniprot.org/annotation/VSP_056888|||http://purl.uniprot.org/annotation/VSP_056889
http://togogenome.org/gene/9606:LPAR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99677                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lysophosphatidic acid receptor 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070033
http://togogenome.org/gene/9606:MEIS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00470                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with susceptibility to restless legs syndrome.|||Homeobox protein Meis1|||Homeobox; TALE-type|||In isoform 2.|||Interaction with DNA|||MEIS N-terminal|||Polar residues|||Required for transcriptional activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049105|||http://purl.uniprot.org/annotation/VAR_063166|||http://purl.uniprot.org/annotation/VSP_034957|||http://purl.uniprot.org/annotation/VSP_034958
http://togogenome.org/gene/9606:LCE1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T752                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1D|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235327|||http://purl.uniprot.org/annotation/VAR_060065|||http://purl.uniprot.org/annotation/VAR_062116
http://togogenome.org/gene/9606:GALNT15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JGI4|||http://purl.uniprot.org/uniprot/Q4G146|||http://purl.uniprot.org/uniprot/Q8N3T1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Glycosyltransferase 2-like|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase|||Polypeptide N-acetylgalactosaminyltransferase 15|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059137|||http://purl.uniprot.org/annotation/PRO_5002996435|||http://purl.uniprot.org/annotation/VAR_019593|||http://purl.uniprot.org/annotation/VAR_049243|||http://purl.uniprot.org/annotation/VAR_049244|||http://purl.uniprot.org/annotation/VAR_049245|||http://purl.uniprot.org/annotation/VAR_049246
http://togogenome.org/gene/9606:ATG4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVU2|||http://purl.uniprot.org/uniprot/Q9Y4P1                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by ULK1; promotes hydrolase activity, leading to increased proteolytic activation and delipidation of ATG8 family proteins.|||Complete loss of protease activity.|||Cysteine protease ATG4B|||Decreased phosphorylation by AKT2, leading to reduced proteolytic activation of ATG8 family proteins.|||Decreased phosphorylation by AKT2; when associated with A-121.|||Decreased phosphorylation by AKT2; when associated with A-262.|||Decreased phosphorylation, leading to decreased hydrolase activity and autophagic flux. Does not affect interaction with ATG8 family proteins.|||Does not affect S-nitrosylation. Does not affect formation of disulfide bonds.|||Does not affect S-nitrosylation. Strongly decreased S-nitrosylation, leading to increased hydrolase activity and autophagic flux; when associated with S-189. Reduced formation of intrachain and interchain disulfide bonds in response to oxidation. Abolished formation of disulfide bonds, leading to increased autophagy; when associated with S-361.|||Does not affect S-nitrosylation. Strongly decreased S-nitrosylation, leading to increased hydrolase activity and autophagic flux; when associated with S-292. Does not affect formation of disulfide bonds.|||Does not affect formation of disulfide bonds.|||In 2mLIR; decreased interaction with ATG8 family proteins MAP1LC3A, MAP1LC3B and MAP1LC3C. Decreased ability to mediate delipidation of ATG8 proteins conjugated to phosphatidylethanolamine (PE).|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interchain (with C-292)|||Interchain (with C-361)|||LIR|||N-acetylmethionine|||Nucleophile|||Peptidase C54 catalytic|||Phospho-mimetic mutant; does not affect interaction with ATG8 family proteins.|||Phospho-mimetic mutant; increased proteolytic activation of ATG8 family proteins.|||Phospho-mimetic mutant; reduced hydrolase activity, leading to decreased proteolytic activation and delipidation of ATG8 family proteins.|||Phospho-mimetic mutant; slightly increased interaction with ATG8 family proteins.|||Phosphoserine|||Phosphoserine; by PKB/AKT1 and PKB/AKT2|||Phosphoserine; by STK26|||Phosphoserine; by ULK1|||Reduced formation of intrachain and interchain disulfide bonds in response to oxidation. Abolished formation of disulfide bonds, leading to increased autophagy; when associated with S-292.|||Reduces the redox sensitivity and retains activity in presence of H(2)O(2).|||S-nitrosocysteine|||Strongly reduced protease activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215844|||http://purl.uniprot.org/annotation/VAR_021486|||http://purl.uniprot.org/annotation/VSP_013028|||http://purl.uniprot.org/annotation/VSP_013029|||http://purl.uniprot.org/annotation/VSP_013031|||http://purl.uniprot.org/annotation/VSP_013032|||http://purl.uniprot.org/annotation/VSP_013033|||http://purl.uniprot.org/annotation/VSP_013034
http://togogenome.org/gene/9606:PPP2R5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15172                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071448|||http://purl.uniprot.org/annotation/VSP_042889
http://togogenome.org/gene/9606:B3GAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V150|||http://purl.uniprot.org/uniprot/O94766|||http://purl.uniprot.org/uniprot/Q5U676                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Absence of enzymatic activity in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA). Does not increase PXYLP1-induced 2-phosphoxylose phosphatase activity in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA).|||Cytoplasmic|||Disordered|||Enzyme inactivation and loss of glycosylation.|||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3|||Helical; Signal-anchor for type II membrane protein|||In JDSCD; reduced glucuronyltransferase activity; patient fibroblasts have decreased levels of dermatan sulfate, chondroitin sulfate and heparan sulfate proteoglycans.|||In JDSCD; unknown pathological significance.|||In isoform 2.|||Interaction with galactose moiety of substrate glycoprotein|||Interchain|||Loss of dimer formation and reduced activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195176|||http://purl.uniprot.org/annotation/VAR_066624|||http://purl.uniprot.org/annotation/VAR_075370|||http://purl.uniprot.org/annotation/VAR_075371|||http://purl.uniprot.org/annotation/VSP_056347
http://togogenome.org/gene/9606:SMTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVP4|||http://purl.uniprot.org/uniprot/A0A087X1R1|||http://purl.uniprot.org/uniprot/B4DI56|||http://purl.uniprot.org/uniprot/B4E229|||http://purl.uniprot.org/uniprot/P53814                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform A.|||In isoform B2.|||In isoform B3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Smoothelin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071976|||http://purl.uniprot.org/annotation/VAR_035657|||http://purl.uniprot.org/annotation/VAR_035658|||http://purl.uniprot.org/annotation/VAR_038785|||http://purl.uniprot.org/annotation/VAR_038786|||http://purl.uniprot.org/annotation/VAR_038787|||http://purl.uniprot.org/annotation/VAR_038788|||http://purl.uniprot.org/annotation/VAR_062223|||http://purl.uniprot.org/annotation/VSP_004398|||http://purl.uniprot.org/annotation/VSP_007020|||http://purl.uniprot.org/annotation/VSP_031242
http://togogenome.org/gene/9606:PPP1R1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVQ9|||http://purl.uniprot.org/uniprot/Q9UD71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine; by CDK5|||Phosphothreonine; by PKA|||Polar residues|||Protein phosphatase 1 regulatory subunit 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071473|||http://purl.uniprot.org/annotation/VSP_005117
http://togogenome.org/gene/9606:ALKAL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX46                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  ALK and LTK ligand 2|||Abolished association with the cell membrane, leading to impaired activation of receptor tyrosine kinase ALK.|||Abolished interchain disulfide bond without affecting homodimerization.|||In isoform 2.|||Interchain|||Reduced affinity for receptor tyrosine kinases ALK and LTK.|||Slightly reduced affinity for receptor tyrosine kinase LTK.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317193|||http://purl.uniprot.org/annotation/VSP_037017|||http://purl.uniprot.org/annotation/VSP_037018
http://togogenome.org/gene/9606:GALNT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY28                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Probable polypeptide N-acetylgalactosaminyltransferase 8|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059119|||http://purl.uniprot.org/annotation/VAR_019581|||http://purl.uniprot.org/annotation/VAR_019582|||http://purl.uniprot.org/annotation/VAR_019583|||http://purl.uniprot.org/annotation/VAR_019584|||http://purl.uniprot.org/annotation/VAR_019585|||http://purl.uniprot.org/annotation/VAR_019586|||http://purl.uniprot.org/annotation/VAR_019587|||http://purl.uniprot.org/annotation/VAR_019588|||http://purl.uniprot.org/annotation/VAR_033947|||http://purl.uniprot.org/annotation/VAR_049241
http://togogenome.org/gene/9606:FAM180A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWF9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Protein FAM180A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317516|||http://purl.uniprot.org/annotation/VAR_054081
http://togogenome.org/gene/9606:EGLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KS0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta(2)beta(3) 'finger-like' loop|||Bipartite nuclear localization signal|||Cytoplasmic and nuclear localization. Reduced transcriptional activity of HIF1A as for wild type.|||Disordered|||Eliminates hydroxylase activity on a HIF1A peptide.|||Eliminates hydroxylase activity.|||Fe2OG dioxygenase|||In isoform p40.|||Leads to expression of isoform p40 only.|||Leads to expression of isoform p43 only.|||Phosphoserine|||Polar residues|||Prolyl hydroxylase EGLN2|||Retained in the nucleus.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206664|||http://purl.uniprot.org/annotation/VSP_038836
http://togogenome.org/gene/9606:HDAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15379                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Histone deacetylase|||Histone deacetylase 3|||Impaired protein deacetylase activity without affecting the protein decrotonylase activity.|||In isoform 2.|||Phosphoserine|||Strongly decreased protein deacetylase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114696|||http://purl.uniprot.org/annotation/VAR_033988|||http://purl.uniprot.org/annotation/VSP_002079
http://togogenome.org/gene/9606:DEFB110                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KQ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Beta-defensin 110|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045336|||http://purl.uniprot.org/annotation/VSP_038146
http://togogenome.org/gene/9606:DNAJC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 27|||In isoform 2.|||In isoform 3.|||J|||Required for interaction with MAPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332975|||http://purl.uniprot.org/annotation/VSP_033409|||http://purl.uniprot.org/annotation/VSP_033410|||http://purl.uniprot.org/annotation/VSP_033411|||http://purl.uniprot.org/annotation/VSP_033412
http://togogenome.org/gene/9606:RCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15293|||http://purl.uniprot.org/uniprot/V9HW95                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Prevents secretion from ER|||Reticulocalbin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004145|||http://purl.uniprot.org/annotation/PRO_5004777705|||http://purl.uniprot.org/annotation/VAR_011965|||http://purl.uniprot.org/annotation/VAR_035460|||http://purl.uniprot.org/annotation/VSP_055511
http://togogenome.org/gene/9606:NTAQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RHC2|||http://purl.uniprot.org/uniprot/Q96HA8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Protein N-terminal glutamine amidohydrolase|||Protein N-terminal glutamine amidohydrolase alpha beta roll                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279409|||http://purl.uniprot.org/annotation/VAR_030882|||http://purl.uniprot.org/annotation/VAR_030883|||http://purl.uniprot.org/annotation/VAR_030884|||http://purl.uniprot.org/annotation/VAR_030885|||http://purl.uniprot.org/annotation/VSP_055268
http://togogenome.org/gene/9606:UFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q541A5|||http://purl.uniprot.org/uniprot/Q92890                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 3.|||In isoform Long.|||N-acetylmethionine|||Phosphoserine|||Ubiquitin recognition factor in ER-associated degradation protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194984|||http://purl.uniprot.org/annotation/VAR_052436|||http://purl.uniprot.org/annotation/VSP_006707|||http://purl.uniprot.org/annotation/VSP_045044
http://togogenome.org/gene/9606:METRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJH8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Meteorin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021680
http://togogenome.org/gene/9606:TMEM164                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U3C3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Transmembrane protein 164                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259640|||http://purl.uniprot.org/annotation/VAR_035671|||http://purl.uniprot.org/annotation/VAR_054035|||http://purl.uniprot.org/annotation/VSP_044964
http://togogenome.org/gene/9606:CPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75976                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Carboxypeptidase D|||Carboxypeptidase-like 1|||Carboxypeptidase-like 2|||Carboxypeptidase-like 3|||Cell attachment site|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor/acceptor|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004401|||http://purl.uniprot.org/annotation/VAR_027771|||http://purl.uniprot.org/annotation/VAR_027772|||http://purl.uniprot.org/annotation/VAR_027773|||http://purl.uniprot.org/annotation/VAR_027774|||http://purl.uniprot.org/annotation/VSP_045833|||http://purl.uniprot.org/annotation/VSP_045834
http://togogenome.org/gene/9606:ANOS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23352                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Anosmin-1|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||In HH1.|||In HH1; phenotype consistent with Kallmann syndrome.|||In HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; Reduced FGFR1-binding.|||In HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; complete loss of FGFR1-binding.|||In HH1; phenotype consistent with Kallmann syndrome; loss of effect on the migratory activity of GnRH neurons; reduced FGFR1-binding.|||In HH1; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism; the patient also carries a mutation in FGFR1.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with Kallmann syndrome; the patient also carries mutation Ala-688 in SEMA3A.|||WAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041395|||http://purl.uniprot.org/annotation/VAR_007720|||http://purl.uniprot.org/annotation/VAR_007721|||http://purl.uniprot.org/annotation/VAR_012742|||http://purl.uniprot.org/annotation/VAR_031011|||http://purl.uniprot.org/annotation/VAR_031012|||http://purl.uniprot.org/annotation/VAR_031013|||http://purl.uniprot.org/annotation/VAR_031014|||http://purl.uniprot.org/annotation/VAR_031015|||http://purl.uniprot.org/annotation/VAR_031016|||http://purl.uniprot.org/annotation/VAR_031017|||http://purl.uniprot.org/annotation/VAR_031018|||http://purl.uniprot.org/annotation/VAR_031019|||http://purl.uniprot.org/annotation/VAR_031020|||http://purl.uniprot.org/annotation/VAR_065362|||http://purl.uniprot.org/annotation/VAR_065363|||http://purl.uniprot.org/annotation/VAR_065364|||http://purl.uniprot.org/annotation/VAR_069207|||http://purl.uniprot.org/annotation/VAR_069968|||http://purl.uniprot.org/annotation/VAR_072992
http://togogenome.org/gene/9606:SEL1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCU6|||http://purl.uniprot.org/uniprot/Q9UBV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Fibronectin type-II|||Helical|||Important for homodimerization and oligomerization|||In isoform 2.|||Interaction with ERLEC1, OS9 and SYVN1|||Interaction with SYVN1|||Lumenal|||Mediates retention in the endoplasmic reticulum|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Protein sel-1 homolog 1|||Sel1-like 1|||Sel1-like 10|||Sel1-like 11|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5|||Sel1-like 6|||Sel1-like 7|||Sel1-like 8|||Sel1-like 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022294|||http://purl.uniprot.org/annotation/VAR_029303|||http://purl.uniprot.org/annotation/VAR_053963|||http://purl.uniprot.org/annotation/VSP_013322|||http://purl.uniprot.org/annotation/VSP_013323
http://togogenome.org/gene/9606:IRAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6F6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Helical|||In isoform 1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||Inositol 1,4,5-triphosphate receptor associated 1|||Interaction with ITPR1|||Interaction with PRKG1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305292|||http://purl.uniprot.org/annotation/VAR_056942|||http://purl.uniprot.org/annotation/VAR_056943|||http://purl.uniprot.org/annotation/VAR_056944|||http://purl.uniprot.org/annotation/VAR_056945|||http://purl.uniprot.org/annotation/VAR_056946|||http://purl.uniprot.org/annotation/VSP_028341|||http://purl.uniprot.org/annotation/VSP_028342|||http://purl.uniprot.org/annotation/VSP_040452|||http://purl.uniprot.org/annotation/VSP_046361|||http://purl.uniprot.org/annotation/VSP_046362|||http://purl.uniprot.org/annotation/VSP_046363|||http://purl.uniprot.org/annotation/VSP_059440|||http://purl.uniprot.org/annotation/VSP_059441|||http://purl.uniprot.org/annotation/VSP_059442
http://togogenome.org/gene/9606:ZNF215                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL58                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||In isoform 2.|||KRAB|||SCAN box|||Zinc finger protein 215                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047459|||http://purl.uniprot.org/annotation/VAR_021890|||http://purl.uniprot.org/annotation/VAR_024200|||http://purl.uniprot.org/annotation/VAR_057405|||http://purl.uniprot.org/annotation/VAR_057406|||http://purl.uniprot.org/annotation/VAR_057407|||http://purl.uniprot.org/annotation/VAR_060423|||http://purl.uniprot.org/annotation/VSP_054156|||http://purl.uniprot.org/annotation/VSP_054157
http://togogenome.org/gene/9606:CELA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08217                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 2A|||In AOMS4; strongly decreased elastase activity; abolishes interaction with SERPINA1; impaired insulin degradation; increased platelet aggregation.|||In AOMS4; strongly decreased elastase activity; abolishes interaction with SERPINA1; increased levels in plasma; impaired insulin degradation; increased platelet aggregation.|||In AOMS4; unknown pathological significance; strongly decreased elastase activity; no effect on interaction with SERPINA1; no effect on insulin degradation; increased platelet aggregation.|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027693|||http://purl.uniprot.org/annotation/PRO_0000027694|||http://purl.uniprot.org/annotation/VAR_051837|||http://purl.uniprot.org/annotation/VAR_083326|||http://purl.uniprot.org/annotation/VAR_083327|||http://purl.uniprot.org/annotation/VAR_083328
http://togogenome.org/gene/9606:OR8H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N162                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8H2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150666|||http://purl.uniprot.org/annotation/VAR_034262|||http://purl.uniprot.org/annotation/VAR_034263|||http://purl.uniprot.org/annotation/VAR_062060
http://togogenome.org/gene/9606:LIPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8W7|||http://purl.uniprot.org/uniprot/Q05469                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha/beta hydrolase fold-3|||Disordered|||Hormone-sensitive lipase|||Hormone-sensitive lipase N-terminal|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||Phosphoserine|||Phosphoserine; by AMPK|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071547|||http://purl.uniprot.org/annotation/VAR_025108|||http://purl.uniprot.org/annotation/VAR_025109|||http://purl.uniprot.org/annotation/VAR_025110|||http://purl.uniprot.org/annotation/VAR_025111|||http://purl.uniprot.org/annotation/VAR_025112|||http://purl.uniprot.org/annotation/VAR_025113|||http://purl.uniprot.org/annotation/VAR_025114|||http://purl.uniprot.org/annotation/VAR_025115|||http://purl.uniprot.org/annotation/VAR_025116|||http://purl.uniprot.org/annotation/VAR_036539|||http://purl.uniprot.org/annotation/VSP_017116
http://togogenome.org/gene/9606:STK32B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9M8|||http://purl.uniprot.org/uniprot/Q9NY57                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 32B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232413|||http://purl.uniprot.org/annotation/VAR_025899|||http://purl.uniprot.org/annotation/VAR_041166|||http://purl.uniprot.org/annotation/VAR_041167|||http://purl.uniprot.org/annotation/VAR_041168|||http://purl.uniprot.org/annotation/VAR_041169|||http://purl.uniprot.org/annotation/VSP_051997
http://togogenome.org/gene/9606:RESF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Retroelement silencing factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295242|||http://purl.uniprot.org/annotation/VAR_033268|||http://purl.uniprot.org/annotation/VAR_033269|||http://purl.uniprot.org/annotation/VAR_033270|||http://purl.uniprot.org/annotation/VAR_033271|||http://purl.uniprot.org/annotation/VAR_033272|||http://purl.uniprot.org/annotation/VAR_033273|||http://purl.uniprot.org/annotation/VAR_033274|||http://purl.uniprot.org/annotation/VAR_033275|||http://purl.uniprot.org/annotation/VAR_033276|||http://purl.uniprot.org/annotation/VAR_033277|||http://purl.uniprot.org/annotation/VAR_033278|||http://purl.uniprot.org/annotation/VAR_033279|||http://purl.uniprot.org/annotation/VAR_033280|||http://purl.uniprot.org/annotation/VAR_033281|||http://purl.uniprot.org/annotation/VAR_061608|||http://purl.uniprot.org/annotation/VAR_061609
http://togogenome.org/gene/9606:AFF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHB7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  AF4/FMR2 family member 4|||Basic and acidic residues|||Breakpoint for insertion to form KMT2A/MLL1-AFF4 fusion protein|||Disordered|||Found in a clear cell renal carcinoma case; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CHOPS.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239393|||http://purl.uniprot.org/annotation/VAR_053003|||http://purl.uniprot.org/annotation/VAR_064693|||http://purl.uniprot.org/annotation/VAR_073790|||http://purl.uniprot.org/annotation/VAR_073791|||http://purl.uniprot.org/annotation/VAR_073792|||http://purl.uniprot.org/annotation/VSP_019218|||http://purl.uniprot.org/annotation/VSP_019219|||http://purl.uniprot.org/annotation/VSP_019220|||http://purl.uniprot.org/annotation/VSP_019221
http://togogenome.org/gene/9606:TIAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01085|||http://purl.uniprot.org/uniprot/Q49AS9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||Nucleolysin TIAR|||Phosphoserine|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081978|||http://purl.uniprot.org/annotation/VSP_043700
http://togogenome.org/gene/9606:RO60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9R9|||http://purl.uniprot.org/uniprot/P10155                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform Short.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||RNA-binding|||RNA-binding protein RO60|||TROVE|||VWFA-like domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174169|||http://purl.uniprot.org/annotation/VSP_005911|||http://purl.uniprot.org/annotation/VSP_005912|||http://purl.uniprot.org/annotation/VSP_045262|||http://purl.uniprot.org/annotation/VSP_045797|||http://purl.uniprot.org/annotation/VSP_054041
http://togogenome.org/gene/9606:RNF224                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DH78                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  RING finger protein 224|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000412182
http://togogenome.org/gene/9606:BRD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYC2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Uncharacterized protein KIAA2026                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288922|||http://purl.uniprot.org/annotation/VSP_039334
http://togogenome.org/gene/9606:FUT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495W5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-(1,3)-fucosyltransferase 11|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299009|||http://purl.uniprot.org/annotation/VAR_034763|||http://purl.uniprot.org/annotation/VSP_027511
http://togogenome.org/gene/9606:PKP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13835                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Disordered|||In isoform 1.|||Phosphoserine|||Plakophilin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064284|||http://purl.uniprot.org/annotation/VAR_033526|||http://purl.uniprot.org/annotation/VAR_033527|||http://purl.uniprot.org/annotation/VAR_033528|||http://purl.uniprot.org/annotation/VAR_053811|||http://purl.uniprot.org/annotation/VAR_062171|||http://purl.uniprot.org/annotation/VSP_006735
http://togogenome.org/gene/9606:TMEM139                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Phosphoserine|||Transmembrane protein 139                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285948
http://togogenome.org/gene/9606:GRIA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42261|||http://purl.uniprot.org/uniprot/Q59GL5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Glutamate receptor 1|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||In MRD67; decreased AMPA glutamate receptor activity; no effect on localization to the cell membrane.|||In MRD67; increased AMPA glutamate receptor activity; increased sensitivity towards glutamate; no effect on localization to the cell membrane.|||In MRD67; unknown pathological significance; no effect on localization to the cell membrane; does not affect AMPA glutamate receptor activity.|||In MRT76; loss of expression; loss of AMPA glutamate receptor activity.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform Flip and isoform 6.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011529|||http://purl.uniprot.org/annotation/VAR_028071|||http://purl.uniprot.org/annotation/VAR_028072|||http://purl.uniprot.org/annotation/VAR_028073|||http://purl.uniprot.org/annotation/VAR_028074|||http://purl.uniprot.org/annotation/VAR_028075|||http://purl.uniprot.org/annotation/VAR_078689|||http://purl.uniprot.org/annotation/VAR_087404|||http://purl.uniprot.org/annotation/VAR_087405|||http://purl.uniprot.org/annotation/VAR_087406|||http://purl.uniprot.org/annotation/VAR_087407|||http://purl.uniprot.org/annotation/VSP_045119|||http://purl.uniprot.org/annotation/VSP_045120|||http://purl.uniprot.org/annotation/VSP_047024|||http://purl.uniprot.org/annotation/VSP_053349
http://togogenome.org/gene/9606:CD40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z349|||http://purl.uniprot.org/uniprot/A0A0S2Z3C7|||http://purl.uniprot.org/uniprot/A0A8Q3SI60|||http://purl.uniprot.org/uniprot/P25942|||http://purl.uniprot.org/uniprot/Q6P2H9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HIGM3.|||In bladder carcinoma cell line Hu549.|||In bladder carcinoma cell line Hu549; requires 2 nucleotide substitutions.|||In isoform II.|||N-linked (GlcNAc...) asparagine|||TNFR-Cys|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034559|||http://purl.uniprot.org/annotation/PRO_5004278823|||http://purl.uniprot.org/annotation/PRO_5006608188|||http://purl.uniprot.org/annotation/PRO_5006608204|||http://purl.uniprot.org/annotation/PRO_5035769455|||http://purl.uniprot.org/annotation/VAR_013628|||http://purl.uniprot.org/annotation/VAR_018751|||http://purl.uniprot.org/annotation/VAR_018752|||http://purl.uniprot.org/annotation/VAR_039301|||http://purl.uniprot.org/annotation/VAR_039302|||http://purl.uniprot.org/annotation/VAR_039303|||http://purl.uniprot.org/annotation/VAR_077569|||http://purl.uniprot.org/annotation/VSP_006472|||http://purl.uniprot.org/annotation/VSP_006473
http://togogenome.org/gene/9606:MLLT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55198                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient)|||Leucine-zipper|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein AF-17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215937|||http://purl.uniprot.org/annotation/VAR_022076|||http://purl.uniprot.org/annotation/VAR_080170
http://togogenome.org/gene/9606:H1-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16401                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.5|||In a colorectal cancer sample; somatic mutation.|||N-acetylserine; partial|||N6-(beta-hydroxybutyryl)lysine|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine|||N6-methyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by GSK3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195909|||http://purl.uniprot.org/annotation/VAR_036204|||http://purl.uniprot.org/annotation/VAR_049308|||http://purl.uniprot.org/annotation/VAR_049309
http://togogenome.org/gene/9606:FCRLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZF2|||http://purl.uniprot.org/uniprot/Q7L513                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Fc receptor-like A|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2 and isoform 10.|||In isoform 3 and isoform 12.|||In isoform 4 and isoform 11.|||In isoform 5 and isoform 14.|||In isoform 6 and isoform 13.|||In isoform 7 and isoform 15.|||In isoform 8.|||In isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 14 and isoform 15.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227935|||http://purl.uniprot.org/annotation/VAR_025646|||http://purl.uniprot.org/annotation/VSP_017603|||http://purl.uniprot.org/annotation/VSP_017604|||http://purl.uniprot.org/annotation/VSP_017605|||http://purl.uniprot.org/annotation/VSP_017606|||http://purl.uniprot.org/annotation/VSP_017607|||http://purl.uniprot.org/annotation/VSP_017608|||http://purl.uniprot.org/annotation/VSP_017609|||http://purl.uniprot.org/annotation/VSP_038297
http://togogenome.org/gene/9606:SKAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5R3|||http://purl.uniprot.org/uniprot/O75563                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homodimerization|||PH|||Phosphoserine|||Phosphotyrosine|||SH3|||Src kinase-associated phosphoprotein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270179|||http://purl.uniprot.org/annotation/VAR_029812|||http://purl.uniprot.org/annotation/VAR_029813
http://togogenome.org/gene/9606:PHYHIPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FC7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Fibronectin type-III|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phytanoyl-CoA hydroxylase-interacting protein-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338641|||http://purl.uniprot.org/annotation/VAR_043817|||http://purl.uniprot.org/annotation/VSP_034067|||http://purl.uniprot.org/annotation/VSP_034068|||http://purl.uniprot.org/annotation/VSP_034069
http://togogenome.org/gene/9606:SLC49A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SL1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes lysosomal localization.|||Cytoplasmic|||Di-leucine motif; mediates lysosomal localization|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Solute carrier family 49 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271338|||http://purl.uniprot.org/annotation/VSP_022302|||http://purl.uniprot.org/annotation/VSP_022303
http://togogenome.org/gene/9606:DCP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPI6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||Lowers decapping activity.|||Phosphoserine|||Phosphothreonine|||Polar residues|||mRNA-decapping enzyme 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189632|||http://purl.uniprot.org/annotation/VSP_057206
http://togogenome.org/gene/9606:VNN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95498                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CN hydrolase|||GPI-anchor amidated cysteine|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Pantetheine hydrolase VNN2|||Proton acceptor|||Proton donor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019718|||http://purl.uniprot.org/annotation/PRO_0000019719|||http://purl.uniprot.org/annotation/VAR_023530|||http://purl.uniprot.org/annotation/VAR_025177|||http://purl.uniprot.org/annotation/VAR_025178|||http://purl.uniprot.org/annotation/VAR_025179|||http://purl.uniprot.org/annotation/VAR_025180|||http://purl.uniprot.org/annotation/VAR_031261|||http://purl.uniprot.org/annotation/VSP_038554|||http://purl.uniprot.org/annotation/VSP_038555|||http://purl.uniprot.org/annotation/VSP_038556|||http://purl.uniprot.org/annotation/VSP_038557|||http://purl.uniprot.org/annotation/VSP_038558|||http://purl.uniprot.org/annotation/VSP_038559|||http://purl.uniprot.org/annotation/VSP_038560|||http://purl.uniprot.org/annotation/VSP_044912
http://togogenome.org/gene/9606:CYP2J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51589                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cytochrome P450 2J2|||In allele CYP2J2*2; significantly reduced metabolism of both arachidonic acid and linoleic acid.|||In allele CYP2J2*3; significantly reduced metabolism of both arachidonic acid and linoleic acid.|||In allele CYP2J2*4; significantly reduced metabolism of arachidonic acid only.|||In allele CYP2J2*5; no change in activity.|||In allele CYP2J2*6; significantly reduced metabolism of both arachidonic acid and linoleic acid.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051769|||http://purl.uniprot.org/annotation/VAR_014317|||http://purl.uniprot.org/annotation/VAR_014318|||http://purl.uniprot.org/annotation/VAR_014319|||http://purl.uniprot.org/annotation/VAR_014320|||http://purl.uniprot.org/annotation/VAR_014321|||http://purl.uniprot.org/annotation/VAR_022084|||http://purl.uniprot.org/annotation/VAR_029159|||http://purl.uniprot.org/annotation/VAR_029160
http://togogenome.org/gene/9606:EEF2KMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7ES84|||http://purl.uniprot.org/uniprot/Q96G04                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FAM86 N-terminal|||In isoform 2.|||N-acetylmethionine|||Protein-lysine N-methyltransferase EEF2KMT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076218|||http://purl.uniprot.org/annotation/VAR_033854|||http://purl.uniprot.org/annotation/VAR_060160|||http://purl.uniprot.org/annotation/VAR_067704|||http://purl.uniprot.org/annotation/VAR_067705|||http://purl.uniprot.org/annotation/VAR_067706|||http://purl.uniprot.org/annotation/VSP_017097
http://togogenome.org/gene/9606:ZNF347                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1S9|||http://purl.uniprot.org/uniprot/Q96SE7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 347                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047545|||http://purl.uniprot.org/annotation/VAR_052815|||http://purl.uniprot.org/annotation/VAR_059913|||http://purl.uniprot.org/annotation/VSP_046841
http://togogenome.org/gene/9606:C7orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Uncharacterized protein C7orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309510
http://togogenome.org/gene/9606:SPNS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMD2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Protein spinster homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305046|||http://purl.uniprot.org/annotation/VAR_035158|||http://purl.uniprot.org/annotation/VAR_035159|||http://purl.uniprot.org/annotation/VAR_035968|||http://purl.uniprot.org/annotation/VSP_028197|||http://purl.uniprot.org/annotation/VSP_028198
http://togogenome.org/gene/9606:PSAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07602                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In GDSAPC.|||In KRBSAPA.|||In MLDSAPB.|||In MLDSAPB; juvenile; affects glycosylation at N-215.|||In MLDSAPB; reduces the intracellular activity of the protein significantly.|||In MLDSAPB; severe.|||In PARK24; associated with disease susceptibility; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; cells carrying this variant show accumulation of autophagic vacuoles, impaired autophagic flux and alpha-synuclein/SNCA aggregation.|||In PARK24; associated with disease susceptibility; affects the intracellular trafficking, resulting in endoplasmic reticulum retention; cells carrying this variant show accumulation of autophagic vacuoles, impaired autophagic flux and alpha-synuclein/SNCA aggregation.|||In isoform Sap-mu-6.|||In isoform Sap-mu-9.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Not glycosylated; in variant MLDSAPB Ile-217|||Prosaposin|||Saposin A-type 1|||Saposin A-type 2|||Saposin B-type 1|||Saposin B-type 2|||Saposin B-type 3|||Saposin B-type 4|||Saposin-A|||Saposin-B|||Saposin-B-Val|||Saposin-C|||Saposin-D|||Strongly decreases stimulation of cerebroside sulfate hydrolysis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000176|||http://purl.uniprot.org/annotation/PRO_0000031616|||http://purl.uniprot.org/annotation/PRO_0000031617|||http://purl.uniprot.org/annotation/PRO_0000031618|||http://purl.uniprot.org/annotation/PRO_0000031619|||http://purl.uniprot.org/annotation/PRO_0000031620|||http://purl.uniprot.org/annotation/PRO_0000031621|||http://purl.uniprot.org/annotation/PRO_0000031622|||http://purl.uniprot.org/annotation/PRO_0000031623|||http://purl.uniprot.org/annotation/PRO_0000031624|||http://purl.uniprot.org/annotation/PRO_0000031625|||http://purl.uniprot.org/annotation/PRO_0000424774|||http://purl.uniprot.org/annotation/VAR_006943|||http://purl.uniprot.org/annotation/VAR_006944|||http://purl.uniprot.org/annotation/VAR_006945|||http://purl.uniprot.org/annotation/VAR_031823|||http://purl.uniprot.org/annotation/VAR_031899|||http://purl.uniprot.org/annotation/VAR_042440|||http://purl.uniprot.org/annotation/VAR_042441|||http://purl.uniprot.org/annotation/VAR_086130|||http://purl.uniprot.org/annotation/VAR_086131|||http://purl.uniprot.org/annotation/VSP_006014|||http://purl.uniprot.org/annotation/VSP_006015
http://togogenome.org/gene/9606:NUDT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95989                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Diphosphoinositol polyphosphate phosphohydrolase 1|||Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis.|||Loss of diphosphoinositol polyphosphate phosphohydrolase activity.|||Loss of endopolyphosphatase activity.|||Loss of mRNA-decapping activity.|||N-acetylmethionine|||No effect on diphosphoinositol polyphosphate phosphohydrolase activity.|||Nudix box|||Nudix hydrolase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057055
http://togogenome.org/gene/9606:KCTD15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD15|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247251|||http://purl.uniprot.org/annotation/VAR_027090|||http://purl.uniprot.org/annotation/VSP_019958|||http://purl.uniprot.org/annotation/VSP_019959
http://togogenome.org/gene/9606:EMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54849                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Epithelial membrane protein 1|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164653|||http://purl.uniprot.org/annotation/VAR_050608|||http://purl.uniprot.org/annotation/VSP_056984
http://togogenome.org/gene/9606:ZNF598                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UK7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity, leading to enhanced readthrough on the poly(A)-stall sequences.|||Basic and acidic residues|||C2H2-type|||Disordered|||E3 ubiquitin-protein ligase ZNF598|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 4.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250568|||http://purl.uniprot.org/annotation/VAR_034470|||http://purl.uniprot.org/annotation/VAR_034471|||http://purl.uniprot.org/annotation/VAR_052147|||http://purl.uniprot.org/annotation/VAR_059818|||http://purl.uniprot.org/annotation/VSP_020660|||http://purl.uniprot.org/annotation/VSP_020661|||http://purl.uniprot.org/annotation/VSP_020662|||http://purl.uniprot.org/annotation/VSP_020663|||http://purl.uniprot.org/annotation/VSP_020664|||http://purl.uniprot.org/annotation/VSP_020665
http://togogenome.org/gene/9606:ITGB3BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13352                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-89.|||Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-96.|||Abolishes interaction with nuclear receptors.|||Abolishes localization to nucleus.|||Basic and acidic residues|||Centromere protein R|||DD1|||Decreased interaction with nuclear receptors.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LXXIL motif|||LXXLL motif|||Loss of repressor function.|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057949|||http://purl.uniprot.org/annotation/VAR_048691|||http://purl.uniprot.org/annotation/VSP_010831|||http://purl.uniprot.org/annotation/VSP_010832|||http://purl.uniprot.org/annotation/VSP_010833|||http://purl.uniprot.org/annotation/VSP_010834
http://togogenome.org/gene/9606:MTMR12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0I1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Interaction with MTM1|||Myotubularin phosphatase|||Myotubularin-related protein 12|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315825|||http://purl.uniprot.org/annotation/VSP_030721|||http://purl.uniprot.org/annotation/VSP_030722
http://togogenome.org/gene/9606:HERPUD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 2 protein|||Polar residues|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280627|||http://purl.uniprot.org/annotation/VAR_031182|||http://purl.uniprot.org/annotation/VAR_031183
http://togogenome.org/gene/9606:PCF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KX04|||http://purl.uniprot.org/uniprot/O94913                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by WNK1, leading to mRNA retention in the nucleus and in prolonged association with polyadenylated mRNAs at transcription loci.|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||CID|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylserine|||Phosphoserine|||Phosphoserine; by WNK1|||Phosphothreonine|||Phosphothreonine; by WNK1|||Polar residues|||Pre-mRNA cleavage complex 2 protein Pcf11|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058246|||http://purl.uniprot.org/annotation/VAR_036878|||http://purl.uniprot.org/annotation/VAR_036879|||http://purl.uniprot.org/annotation/VAR_036880
http://togogenome.org/gene/9606:LSM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62312                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  N6-acetyllysine|||Sm|||U6 snRNA-associated Sm-like protein LSm6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125575
http://togogenome.org/gene/9606:CFD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XNE2|||http://purl.uniprot.org/uniprot/K7ERG9|||http://purl.uniprot.org/uniprot/P00746                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Complement factor D|||In CFDD.|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027560|||http://purl.uniprot.org/annotation/PRO_0000027561|||http://purl.uniprot.org/annotation/PRO_5002702870|||http://purl.uniprot.org/annotation/PRO_5014099472|||http://purl.uniprot.org/annotation/VAR_034866|||http://purl.uniprot.org/annotation/VAR_034867|||http://purl.uniprot.org/annotation/VAR_034868
http://togogenome.org/gene/9606:TMEM265                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTH1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Transmembrane protein 265                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432548
http://togogenome.org/gene/9606:FOXO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98177                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation. No effect on cellular location or transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-197.|||Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-197 and A-262.|||Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-262.|||Disordered|||Fork-head|||Forkhead box protein O4|||In isoform Zeta.|||Phosphoserine; by PKB/AKT1|||Phosphothreonine; by PKB/AKT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091875|||http://purl.uniprot.org/annotation/VSP_001552
http://togogenome.org/gene/9606:ACR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10323                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acrosin|||Acrosin heavy chain|||Acrosin light chain|||Charge relay system|||Disordered|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Pro residues|||Pro-rich                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027518|||http://purl.uniprot.org/annotation/PRO_0000027519|||http://purl.uniprot.org/annotation/PRO_0000027520|||http://purl.uniprot.org/annotation/PRO_0000027521|||http://purl.uniprot.org/annotation/VAR_011650|||http://purl.uniprot.org/annotation/VAR_011651
http://togogenome.org/gene/9606:VPS33A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AX1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-438.|||Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-429. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441.|||Disrupts interaction with VPS16. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-438. Disrupts interaction with VPS18 and impairs endosome-lysosome fusion; when associated with K-441.|||In MPSPS; may induce lysosome hyperacidification; does not affect the interaction with VPS16 and STX17; does not affect intracellular trafficking, lipid trafficking, nor cathepsin D processing.|||Vacuolar protein sorting-associated protein 33A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206302|||http://purl.uniprot.org/annotation/VAR_052471|||http://purl.uniprot.org/annotation/VAR_078032
http://togogenome.org/gene/9606:F11R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FIB4|||http://purl.uniprot.org/uniprot/Q9Y624                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by H.pylori PqqE|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||Junctional adhesion molecule A|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015066|||http://purl.uniprot.org/annotation/PRO_5015098273|||http://purl.uniprot.org/annotation/VSP_056218
http://togogenome.org/gene/9606:LY6K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RY6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||In isoform 2.|||Lymphocyte antigen 6K|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337084|||http://purl.uniprot.org/annotation/PRO_0000337085|||http://purl.uniprot.org/annotation/VSP_045602|||http://purl.uniprot.org/annotation/VSP_045603
http://togogenome.org/gene/9606:GH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0M6L0J9|||http://purl.uniprot.org/uniprot/P01242                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Growth hormone variant|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033061|||http://purl.uniprot.org/annotation/PRO_5005806235|||http://purl.uniprot.org/annotation/VAR_014591|||http://purl.uniprot.org/annotation/VSP_006203|||http://purl.uniprot.org/annotation/VSP_043206|||http://purl.uniprot.org/annotation/VSP_043480
http://togogenome.org/gene/9606:ANGPTL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKU9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Angiopoietin-related protein 2|||Fibrinogen C-terminal|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009120|||http://purl.uniprot.org/annotation/VSP_056934
http://togogenome.org/gene/9606:TOMM34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15785                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mitochondrial import receptor subunit TOM34|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106334|||http://purl.uniprot.org/annotation/VAR_059860
http://togogenome.org/gene/9606:RBKS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H477                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Proton acceptor|||Ribokinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080092|||http://purl.uniprot.org/annotation/VSP_054380
http://togogenome.org/gene/9606:ATF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18847                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||Cyclic AMP-dependent transcription factor ATF-3|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||Phosphothreonine|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076581|||http://purl.uniprot.org/annotation/VAR_048442|||http://purl.uniprot.org/annotation/VAR_081532|||http://purl.uniprot.org/annotation/VSP_000592|||http://purl.uniprot.org/annotation/VSP_043150|||http://purl.uniprot.org/annotation/VSP_043182|||http://purl.uniprot.org/annotation/VSP_046966
http://togogenome.org/gene/9606:HAUS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CZ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HAUS augmin-like complex subunit 3|||In isoform 2.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301951|||http://purl.uniprot.org/annotation/VAR_034912|||http://purl.uniprot.org/annotation/VSP_057022|||http://purl.uniprot.org/annotation/VSP_057023
http://togogenome.org/gene/9606:CUX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14529                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CUT 1|||CUT 2|||CUT 3|||Disordered|||Homeobox|||Homeobox protein cut-like 2|||In DEE67.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202396|||http://purl.uniprot.org/annotation/VAR_065096|||http://purl.uniprot.org/annotation/VAR_081600
http://togogenome.org/gene/9606:ARMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXS3|||http://purl.uniprot.org/uniprot/Q5W041                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Armadillo repeat-containing protein 3|||Basic and acidic residues|||Disordered|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284403|||http://purl.uniprot.org/annotation/VAR_050669|||http://purl.uniprot.org/annotation/VAR_050670|||http://purl.uniprot.org/annotation/VAR_050671|||http://purl.uniprot.org/annotation/VSP_024498|||http://purl.uniprot.org/annotation/VSP_024500|||http://purl.uniprot.org/annotation/VSP_024501|||http://purl.uniprot.org/annotation/VSP_028551|||http://purl.uniprot.org/annotation/VSP_028552
http://togogenome.org/gene/9606:KDELR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33947                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||ER lumen protein-retaining receptor 2|||Helical|||Important for recycling of cargo proteins with the sequence motif K-D-E-L from the Golgi to the endoplasmic reticulum|||In OI21; changed maintenance of protein localization in endoplasmic reticulum; SERPINH1 is not retained in the endoplasmic reticulum and secreted; leads to a loss of fiber formation of the bones connective tissue; no effect on protein abundance.|||In OI21; loss of protein expression; changed maintenance of protein localization in endoplasmic reticulum; SERPINH1 is not retained in the endoplasmic reticulum and secreted; leads to a loss of fiber formation of the bones connective tissue.|||In OI21; unknown pathological significance.|||In isoform 2.|||Interaction with the K-D-E-L motif on target proteins|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194155|||http://purl.uniprot.org/annotation/VAR_085601|||http://purl.uniprot.org/annotation/VAR_085602|||http://purl.uniprot.org/annotation/VAR_085603|||http://purl.uniprot.org/annotation/VAR_085604|||http://purl.uniprot.org/annotation/VAR_085605|||http://purl.uniprot.org/annotation/VSP_036712
http://togogenome.org/gene/9606:MTFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P444                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Mitochondrial fission regulator 2|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087164|||http://purl.uniprot.org/annotation/VSP_039795|||http://purl.uniprot.org/annotation/VSP_039796
http://togogenome.org/gene/9606:HLF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16534                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Disordered|||Hepatic leukemia factor|||In fusion protein; decreases DNA-binding activity.|||In isoform 2.|||Leucine-zipper|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076510|||http://purl.uniprot.org/annotation/VAR_008515|||http://purl.uniprot.org/annotation/VSP_053852
http://togogenome.org/gene/9606:RSPH10B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RC85                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MORN 1|||MORN 10|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||MORN 9|||Polar residues|||Radial spoke head 10 homolog B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349254|||http://purl.uniprot.org/annotation/VAR_037357|||http://purl.uniprot.org/annotation/VSP_035277|||http://purl.uniprot.org/annotation/VSP_035278|||http://purl.uniprot.org/annotation/VSP_035279
http://togogenome.org/gene/9606:TTC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TAA0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||Tetratricopeptide repeat protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263098|||http://purl.uniprot.org/annotation/VAR_029585|||http://purl.uniprot.org/annotation/VSP_021859|||http://purl.uniprot.org/annotation/VSP_021860
http://togogenome.org/gene/9606:FBXO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with glycosylated concanavalin-A in vitro.|||Disordered|||F-box|||F-box only protein 6|||FBA|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119882|||http://purl.uniprot.org/annotation/VAR_022158|||http://purl.uniprot.org/annotation/VAR_049039
http://togogenome.org/gene/9606:SLC39A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13433                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Zinc transporter ZIP6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041650|||http://purl.uniprot.org/annotation/VAR_059964|||http://purl.uniprot.org/annotation/VSP_014309|||http://purl.uniprot.org/annotation/VSP_014310|||http://purl.uniprot.org/annotation/VSP_014311
http://togogenome.org/gene/9606:CACNG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXS5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Polar residues|||Pro residues|||Voltage-dependent calcium channel gamma-8 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164690
http://togogenome.org/gene/9606:EVI5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60447|||http://purl.uniprot.org/uniprot/Q59FE7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form EVI5-TRNG10 fusion protein|||Dimerization|||Disordered|||Ecotropic viral integration site 5 protein homolog|||In isoform 2.|||Interaction with AURKB and INCENP|||Interaction with alpha-tubulin, gamma-tubulin, BIRC5 and FBXO5|||Phosphoserine|||Polar residues|||Rab-GAP TBC|||Targeting to the centrosomes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256241|||http://purl.uniprot.org/annotation/VAR_028890|||http://purl.uniprot.org/annotation/VAR_028891|||http://purl.uniprot.org/annotation/VAR_047753|||http://purl.uniprot.org/annotation/VSP_056828
http://togogenome.org/gene/9606:EPYC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99645                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Epiphycan|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRRNT|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (dermatan sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032768|||http://purl.uniprot.org/annotation/VAR_031595
http://togogenome.org/gene/9606:PIK3C2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG55|||http://purl.uniprot.org/uniprot/L7RRS0|||http://purl.uniprot.org/uniprot/O00443                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PtdIns(4,5)P2-containing membranes.|||Abolishes lipid kinase activity. Affects clathrin distribution when combined with a truncation encompassing the region of clathrin interaction.|||Abolishes phosphorylation, no change in activity.|||Activation loop|||Basic and acidic residues|||C2|||C2 PI3K-type|||Catalytic loop|||Disordered|||G-loop|||In OCSKD; no protein detected by Wester blot in patient cells.|||In isoform 2.|||Interaction with PtdIns(4,5)P2-containing membranes|||Interaction with clathrin; sufficient to induce clathrin assembly|||N-acetylalanine|||No effect on phosphorylation in vitro.|||Not phosphorylated|||Nuclear localization signal|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||PX|||Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha|||Phosphoserine|||Protects from proteolysis.|||Reduces affinity for PtdIns(4,5)P2-containing membranes 23-fold.|||Reduces affinity for PtdIns(4,5)P2-containing membranes 5-fold.|||Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold.|||Reduces clathrin binding.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088795|||http://purl.uniprot.org/annotation/VAR_023333|||http://purl.uniprot.org/annotation/VAR_082616|||http://purl.uniprot.org/annotation/VSP_056158
http://togogenome.org/gene/9606:MCMBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5P5|||http://purl.uniprot.org/uniprot/Q9BTE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Mini-chromosome maintenance complex-binding protein|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089827|||http://purl.uniprot.org/annotation/VSP_014707|||http://purl.uniprot.org/annotation/VSP_040721
http://togogenome.org/gene/9606:OSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAX0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Protein odd-skipped-related 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047004
http://togogenome.org/gene/9606:GIMAP1-GIMAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTJ2                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  AIG1-type G|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RC3H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZMB3|||http://purl.uniprot.org/uniprot/B9EGU6|||http://purl.uniprot.org/uniprot/Q5TC82                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes CDERNA-binding but no effect on dsRNA binding.|||C3H1-type|||Cleavage; by MALT1|||Disordered|||HEPN-C|||HEPN-N|||In IMDYSHI; decreased protein abundance; loss of localization to P-bodies; decreased interaction with CCR4-NOT deadenylase complex; loss of function in regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA; failed to regulate the production of inflammatory cytokines.|||In isoform 2.|||No effect on CDERNA-binding but abolishes dsRNA binding; when associated with 135-E-E-136.|||No effect on CDERNA-binding but abolishes dsRNA binding; when associated with E-164 or A-322-323-A.|||Phosphoserine|||Polar residues|||RING-type|||RING-type; degenerate|||ROQ|||Roquin-1|||Slightly reduces stem-loop RNA and dsRNA binding.|||Strongly decreases binding to RNA containing CDE stem-loop motifs. Abolishes binding to RNA containing CDE stem-loop motifs and dsRNA; when associated with 219-A-A-220.|||Strongly decreases binding to RNA containing CDE stem-loop motifs. Abolishes binding to RNA containing CDE stem-loop motifs and dsRNA; when associated with 259-A-A-260.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055965|||http://purl.uniprot.org/annotation/VAR_084832|||http://purl.uniprot.org/annotation/VSP_015015|||http://purl.uniprot.org/annotation/VSP_015016
http://togogenome.org/gene/9606:ATP1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13733                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with phosphoinositide-3 kinase|||Phosphoserine; by PKA|||Polar residues|||Sodium/potassium-transporting ATPase subunit alpha-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046303|||http://purl.uniprot.org/annotation/VAR_048375|||http://purl.uniprot.org/annotation/VAR_048376|||http://purl.uniprot.org/annotation/VAR_048377|||http://purl.uniprot.org/annotation/VAR_048378|||http://purl.uniprot.org/annotation/VSP_007364
http://togogenome.org/gene/9606:F2RL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00254                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Altered signal upon thrombin cleavage.|||Cleavage; by thrombin|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No proteolytic cleavage by thrombin.|||Proteinase-activated receptor 3|||Removed for receptor activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012756|||http://purl.uniprot.org/annotation/PRO_0000012757|||http://purl.uniprot.org/annotation/VAR_012849|||http://purl.uniprot.org/annotation/VAR_012850|||http://purl.uniprot.org/annotation/VAR_012851|||http://purl.uniprot.org/annotation/VSP_045116
http://togogenome.org/gene/9606:PLIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60240                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Perilipin-1|||Phosphoserine|||Phosphothreonine|||Required for interaction with CIDEC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099884|||http://purl.uniprot.org/annotation/VAR_055046|||http://purl.uniprot.org/annotation/VAR_055047|||http://purl.uniprot.org/annotation/VAR_055048|||http://purl.uniprot.org/annotation/VAR_061505
http://togogenome.org/gene/9606:MAP3K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2U5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In a lung large cell carcinoma sample; somatic mutation.|||Mitogen-activated protein kinase kinase kinase 2|||PB1|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086243|||http://purl.uniprot.org/annotation/VAR_040682|||http://purl.uniprot.org/annotation/VAR_040683|||http://purl.uniprot.org/annotation/VAR_040684
http://togogenome.org/gene/9606:TBC1D3F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NER0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344451
http://togogenome.org/gene/9606:PSMB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28062|||http://purl.uniprot.org/uniprot/X5CMJ9                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Disordered|||In PRAAS1; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity.|||In PRAAS1; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function; some patients are heterozygotes for this mutation and also carry a mutation in PSMA3; patients' cells show reduction of proteasome content and endopeptidase activity of the proteasome.|||In PRAAS1; some patients are heterozygotes for this mutation and also carry a mutation in PSMB4.|||In PRAAS1; unknown pathological significance.|||In allele LMP7C.|||In allele LPM7C.|||In isoform 2.|||Nucleophile|||Phosphothreonine|||Proteasome subunit beta type-8|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026597|||http://purl.uniprot.org/annotation/PRO_0000026598|||http://purl.uniprot.org/annotation/VAR_006488|||http://purl.uniprot.org/annotation/VAR_006489|||http://purl.uniprot.org/annotation/VAR_057046|||http://purl.uniprot.org/annotation/VAR_065204|||http://purl.uniprot.org/annotation/VAR_065291|||http://purl.uniprot.org/annotation/VAR_066449|||http://purl.uniprot.org/annotation/VAR_075256|||http://purl.uniprot.org/annotation/VAR_075257|||http://purl.uniprot.org/annotation/VSP_005287
http://togogenome.org/gene/9606:NCF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15080                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with membranes enriched in phosphatidylinositol 3-phosphate.|||In CGD3; the protein remains cytosolic, does not localize to phagosomes or endosomes and is unable to bind phosphatidylinositol 3-phosphate (PtdIns(3)P) in a lipid-binding assay; unable to rescue the NADPH-oxidase defect of NCF4 functionally null cells.|||In isoform 3.|||Neutrophil cytosol factor 4|||No effect on phosphorylation.|||PB1|||PX|||Phosphoserine|||Phosphothreonine|||Reduces phosphorylation.|||SH3|||Slightly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate.|||Strongly reduces interaction with membranes enriched in phosphatidylinositol 3-phosphate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096764|||http://purl.uniprot.org/annotation/VAR_009314|||http://purl.uniprot.org/annotation/VAR_034136|||http://purl.uniprot.org/annotation/VAR_065949|||http://purl.uniprot.org/annotation/VAR_082885|||http://purl.uniprot.org/annotation/VSP_042681
http://togogenome.org/gene/9606:TSPOAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2C5|||http://purl.uniprot.org/uniprot/B2RUT8|||http://purl.uniprot.org/uniprot/B7ZVZ7|||http://purl.uniprot.org/uniprot/O95153|||http://purl.uniprot.org/uniprot/X5DQQ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||In isoform 2.|||In isoform 3.|||Peripheral-type benzodiazepine receptor-associated protein 1|||Polar residues|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221380|||http://purl.uniprot.org/annotation/VAR_017446|||http://purl.uniprot.org/annotation/VAR_017447|||http://purl.uniprot.org/annotation/VAR_017448|||http://purl.uniprot.org/annotation/VAR_017449|||http://purl.uniprot.org/annotation/VAR_017450|||http://purl.uniprot.org/annotation/VAR_017451|||http://purl.uniprot.org/annotation/VAR_031662|||http://purl.uniprot.org/annotation/VAR_031663|||http://purl.uniprot.org/annotation/VAR_031664|||http://purl.uniprot.org/annotation/VAR_070193|||http://purl.uniprot.org/annotation/VSP_009204|||http://purl.uniprot.org/annotation/VSP_009205
http://togogenome.org/gene/9606:CBFA2T2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43439                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form RUNX1-CBFA2T2 in acute myeloid leukemia|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PRDM14|||MYND-type|||Nervy homology region 2 (NHR2)|||Nervy homology region 3 (NHR3)|||Phosphoserine|||Polar residues|||Pro residues|||Protein CBFA2T2|||TAFH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218301|||http://purl.uniprot.org/annotation/VSP_008121|||http://purl.uniprot.org/annotation/VSP_008122|||http://purl.uniprot.org/annotation/VSP_008123|||http://purl.uniprot.org/annotation/VSP_008124|||http://purl.uniprot.org/annotation/VSP_047410
http://togogenome.org/gene/9606:CLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92989                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates RNA kinase activity and tRNA splicing activity.|||Abrogates RNA kinase activity. Abrogates complementation of tRNA splicing activity in yeast; when associated with A-128.|||Abrogates complementation of tRNA splicing activity in yeast.|||In PCH10; decreases kinase activity, impairs formation of the tRNA splicing endonuclease complex and impairs ability to mediate tRNA splicing and maturation.|||In isoform 2.|||Polyribonucleotide 5'-hydroxyl-kinase Clp1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089863|||http://purl.uniprot.org/annotation/VAR_070952|||http://purl.uniprot.org/annotation/VSP_041164
http://togogenome.org/gene/9606:NDUFA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI09                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MC1DN23.|||In isoform 2.|||N-acetylmethionine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118845|||http://purl.uniprot.org/annotation/VAR_060682|||http://purl.uniprot.org/annotation/VAR_081459|||http://purl.uniprot.org/annotation/VSP_046948
http://togogenome.org/gene/9606:IFT122                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXT5|||http://purl.uniprot.org/uniprot/Q9HBG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In CED1; decreased ciliogenesis; perturbed ciliary protein trafficking; strongly decreases interaction with ITF43:WDR35; fail to assemble IFT-A complex at the cilia base.|||In CED1; no effect on interaction with ITF43:WDR35.|||In CED1; perturbed ciliary protein trafficking; no effect on interaction with ITF43:WDR35; fail to assemble IFT-A complex at the cilia base; no effect on ciliogenesis.|||In CED1; strongly decreases interaction with ITF43:WDR35.|||In CED1; unknown pathological significance.|||In isoform 10.|||In isoform 11.|||In isoform 3, isoform 4, isoform 6, isoform 7, isoform 9 and isoform 11.|||In isoform 4, isoform 6, isoform 9 and isoform 10.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7 and isoform 8.|||In isoform 9.|||Intraflagellar transport protein 122 homolog|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051045|||http://purl.uniprot.org/annotation/VAR_063584|||http://purl.uniprot.org/annotation/VAR_063585|||http://purl.uniprot.org/annotation/VAR_063586|||http://purl.uniprot.org/annotation/VAR_081601|||http://purl.uniprot.org/annotation/VAR_081602|||http://purl.uniprot.org/annotation/VAR_081603|||http://purl.uniprot.org/annotation/VAR_081604|||http://purl.uniprot.org/annotation/VAR_081605|||http://purl.uniprot.org/annotation/VSP_041161|||http://purl.uniprot.org/annotation/VSP_043310|||http://purl.uniprot.org/annotation/VSP_043311|||http://purl.uniprot.org/annotation/VSP_045224|||http://purl.uniprot.org/annotation/VSP_056773|||http://purl.uniprot.org/annotation/VSP_056774|||http://purl.uniprot.org/annotation/VSP_056775|||http://purl.uniprot.org/annotation/VSP_056776|||http://purl.uniprot.org/annotation/VSP_056777|||http://purl.uniprot.org/annotation/VSP_056778
http://togogenome.org/gene/9606:HOXC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53XI4|||http://purl.uniprot.org/uniprot/Q9NYD6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein Hox-C10|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200190
http://togogenome.org/gene/9606:ZBTB16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3C6|||http://purl.uniprot.org/uniprot/Q05516                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Breakpoint for translocation to form PLZF-RAR-alpha oncogene|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In SGYMR.|||In isoform PLZFA.|||Interaction with RUNX1T1|||Phosphoserine; by PDPK1|||Phosphothreonine; by PDPK1|||Zinc finger and BTB domain-containing protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047729|||http://purl.uniprot.org/annotation/VAR_054912|||http://purl.uniprot.org/annotation/VSP_006896
http://togogenome.org/gene/9606:GPR55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K858|||http://purl.uniprot.org/uniprot/Q9Y2T6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 55|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069577|||http://purl.uniprot.org/annotation/VAR_024257|||http://purl.uniprot.org/annotation/VAR_049395
http://togogenome.org/gene/9606:KDF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NAX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ECTD12; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||Keratinocyte differentiation factor 1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289048|||http://purl.uniprot.org/annotation/VAR_032561|||http://purl.uniprot.org/annotation/VAR_032562|||http://purl.uniprot.org/annotation/VAR_032563|||http://purl.uniprot.org/annotation/VAR_035616|||http://purl.uniprot.org/annotation/VAR_078070
http://togogenome.org/gene/9606:ACTR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61163                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  Alpha-centractin|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089058
http://togogenome.org/gene/9606:HCFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cleavage; by autolysis|||Disordered|||Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Eliminates VIC formation and association with VP16. Weak association with POU2F1. Unable to associate with CREBZF and BAP1. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Eliminates VIC formation, but only minor reduction in association with VP16. Unable to associate with POU2F1, but only minor reduction in association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells.|||Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HCF C-terminal chain 1|||HCF C-terminal chain 2|||HCF C-terminal chain 3|||HCF C-terminal chain 4|||HCF C-terminal chain 5|||HCF C-terminal chain 6|||HCF N-terminal chain 1|||HCF N-terminal chain 2|||HCF N-terminal chain 3|||HCF N-terminal chain 4|||HCF N-terminal chain 5|||HCF N-terminal chain 6|||HCF repeat 1|||HCF repeat 2|||HCF repeat 3|||HCF repeat 4; degenerate|||HCF repeat 5|||HCF repeat 6|||HCF repeat 7; degenerate|||HCF repeat 8|||In MAHCX; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactivates cleavage at HCF repeat.|||Interaction with GABP2|||Interaction with SIN3A|||Interaction with ZBTB17|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells.|||Minor reduction in VIC formation and association with VP16. Weak association with POU2F1. Severely reduces association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells.|||Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells.|||N-acetylalanine|||N6-acetyllysine|||No effect on cleavage at HCF repeat.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces and disrupts cleavage at HCF repeat.|||Reduces cleavage at HCF repeat.|||Removed|||Required for interaction with OGT|||Severely reduces VIC formation, but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells.|||Severely reduces VP16-induced complex (VIC) formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Abolishes interaction with CREB3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016611|||http://purl.uniprot.org/annotation/PRO_0000016612|||http://purl.uniprot.org/annotation/PRO_0000016613|||http://purl.uniprot.org/annotation/PRO_0000016614|||http://purl.uniprot.org/annotation/PRO_0000016615|||http://purl.uniprot.org/annotation/PRO_0000016616|||http://purl.uniprot.org/annotation/PRO_0000016617|||http://purl.uniprot.org/annotation/PRO_0000016618|||http://purl.uniprot.org/annotation/PRO_0000016619|||http://purl.uniprot.org/annotation/PRO_0000016620|||http://purl.uniprot.org/annotation/PRO_0000016621|||http://purl.uniprot.org/annotation/PRO_0000016622|||http://purl.uniprot.org/annotation/VAR_019813|||http://purl.uniprot.org/annotation/VAR_050043|||http://purl.uniprot.org/annotation/VAR_069098|||http://purl.uniprot.org/annotation/VSP_002815|||http://purl.uniprot.org/annotation/VSP_012984|||http://purl.uniprot.org/annotation/VSP_012985|||http://purl.uniprot.org/annotation/VSP_047138
http://togogenome.org/gene/9606:KCNK12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HB15                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101760
http://togogenome.org/gene/9606:OR4C13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGP0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150534|||http://purl.uniprot.org/annotation/VAR_067440|||http://purl.uniprot.org/annotation/VAR_067441
http://togogenome.org/gene/9606:KRTAP2-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYU5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  10 X 5 AA repeats of C-C-[CDPQRWG]-[APRS]-[CIPSTVD]|||Keratin-associated protein 2-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331450
http://togogenome.org/gene/9606:NUP62CL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5E8|||http://purl.uniprot.org/uniprot/Q9H1M0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Nucleoporin NSP1-like C-terminal|||Nucleoporin-62 C-terminal-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257834|||http://purl.uniprot.org/annotation/VAR_028920|||http://purl.uniprot.org/annotation/VAR_050569|||http://purl.uniprot.org/annotation/VSP_021367|||http://purl.uniprot.org/annotation/VSP_021368
http://togogenome.org/gene/9606:NMI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13287                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of TRIM21-mediated ubiquitination and loss of Sendai virus-triggered type IIFN-beta production. Loss of TRIM21-mediated ubiquitination and decreased Sendai virus-triggered type IIFN-beta production; when associated with R-27.|||N-myc-interactor|||NID 1|||NID 2|||No change in TRIM21-mediated ubiquitination and no change in Sendai virus-triggered type IIFN-beta production. Loss of TRIM21-mediated ubiquitination and decreased Sendai virus-triggered type IIFN-beta production; when associated with R-22.|||No change in TRIM21-mediated ubiquitination; when associated with R-176.|||No change in TRIM21-mediated ubiquitination; when associated with R-183.|||No change in TRIM21-mediated ubiquitination; when associated with R-56.|||No change in TRIM21-mediated ubiquitination; when associated with R-61.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159702|||http://purl.uniprot.org/annotation/VAR_028190
http://togogenome.org/gene/9606:RBMY1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15415                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member F/J|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314164|||http://purl.uniprot.org/annotation/VSP_030217|||http://purl.uniprot.org/annotation/VSP_030218
http://togogenome.org/gene/9606:UBE2Q2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVN8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||UBC core|||Ubiquitin-conjugating enzyme E2 Q2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223879|||http://purl.uniprot.org/annotation/VSP_017298|||http://purl.uniprot.org/annotation/VSP_017299|||http://purl.uniprot.org/annotation/VSP_044817|||http://purl.uniprot.org/annotation/VSP_055681
http://togogenome.org/gene/9606:ARSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK06|||http://purl.uniprot.org/uniprot/P51689                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase D|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Sulfatase N-terminal|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033424|||http://purl.uniprot.org/annotation/PRO_5007491840|||http://purl.uniprot.org/annotation/VAR_052508|||http://purl.uniprot.org/annotation/VAR_052509|||http://purl.uniprot.org/annotation/VAR_052510|||http://purl.uniprot.org/annotation/VSP_015798|||http://purl.uniprot.org/annotation/VSP_015799|||http://purl.uniprot.org/annotation/VSP_035667
http://togogenome.org/gene/9606:NT5C1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJC7|||http://purl.uniprot.org/uniprot/B3KUK6|||http://purl.uniprot.org/uniprot/B4DXZ9|||http://purl.uniprot.org/uniprot/B4DZ86|||http://purl.uniprot.org/uniprot/Q96P26                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytosolic 5'-nucleotidase 1B|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144796|||http://purl.uniprot.org/annotation/VSP_010201|||http://purl.uniprot.org/annotation/VSP_010202|||http://purl.uniprot.org/annotation/VSP_010203
http://togogenome.org/gene/9606:SHF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTY1|||http://purl.uniprot.org/uniprot/B4DWP8|||http://purl.uniprot.org/uniprot/B4E1A9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||SH2                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PFKFB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8A0|||http://purl.uniprot.org/uniprot/Q16875                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  20-fold decrease in Km for ATP and 3-fold decrease in Km for fructose-6 phsphate.|||6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3|||Disordered|||Fructose-2,6-bisphosphatase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of activity.|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphothreonine|||Phosphothreonine; by PKC|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179968|||http://purl.uniprot.org/annotation/VSP_004680|||http://purl.uniprot.org/annotation/VSP_047165|||http://purl.uniprot.org/annotation/VSP_054549
http://togogenome.org/gene/9606:GPR183                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32249                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold reduction in receptor activation.|||10-fold reduction in receptor activation. Strongly reduced localization to the cell membrane.|||500-fold decrease of IC(50) for GSK682753A. No effect on oxysterol agonist-binding and receptor activation.|||Abolishes localization to the cell membrane without affecting protein expression levels.|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 183|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In an acute myeloid leukemia sample; somatic mutation.|||Increased receptor activation.|||Increased receptor activation. Strongly reduced localization to the cell membrane.|||Interaction with G proteins|||Loss of receptor activation without affecting oxysterol agonist-binding.|||No effect.|||Phosphoserine|||Reduced localization to the cell membrane and reduced receptor function, without affecting oxysterol agonist-binding.|||Reduced localization to the cell membrane and reduced receptor function.|||Reduced localization to the cell membrane and reduced receptor function. Reduced oxysterol agonist-binding.|||Slight decrease in oxysterol agonist-binding and receptor activation.|||Strong decrease in oxysterol agonist-binding and receptor activation.|||Strong reduction in ligand potency.|||Strongly reduced localization to the cell membrane and reduced protein expression levels.|||Strongly reduced localization to the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069411|||http://purl.uniprot.org/annotation/VAR_054147
http://togogenome.org/gene/9606:SULT1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMM9|||http://purl.uniprot.org/uniprot/P0DMN0|||http://purl.uniprot.org/uniprot/Q1ET61                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases levels of sulfotransferase activity.|||Decreases levels of sulfotransferase activity; accelerates proteasome-dependent degradation.|||In isoform 2.|||In isoform 3.|||No effect on sulfotransferase activity.|||Proton acceptor|||Sulfotransferase|||Sulfotransferase 1A3|||Sulfotransferase 1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085159|||http://purl.uniprot.org/annotation/PRO_0000430204|||http://purl.uniprot.org/annotation/VAR_071108|||http://purl.uniprot.org/annotation/VAR_071109|||http://purl.uniprot.org/annotation/VAR_071110|||http://purl.uniprot.org/annotation/VAR_071111|||http://purl.uniprot.org/annotation/VAR_071112|||http://purl.uniprot.org/annotation/VAR_071113|||http://purl.uniprot.org/annotation/VAR_071114|||http://purl.uniprot.org/annotation/VAR_071115|||http://purl.uniprot.org/annotation/VSP_012326|||http://purl.uniprot.org/annotation/VSP_047771
http://togogenome.org/gene/9606:SIX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95343                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Bind to RHO promoter|||Decreased interaction with TLE5 and loss ineteraction with TLE1.|||Disordered|||Homeobox|||Homeobox protein SIX3|||In HPE2.|||In HPE2; Significantly decreased interaction with NR4A3; Significantly decreased its ability to activate NR4A3.|||In HPE2; Significantly decreased its ability to activate NR4A3.|||In SCHZC and HPE2.|||In SCHZC.|||Interaction with TLE5|||Loss of interaction with TLE1 and TLE5; when associated with P-95.|||Loss of interaction with TLE1 and TLE5; when associated with P-99.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049299|||http://purl.uniprot.org/annotation/VAR_003771|||http://purl.uniprot.org/annotation/VAR_003772|||http://purl.uniprot.org/annotation/VAR_003773|||http://purl.uniprot.org/annotation/VAR_023797|||http://purl.uniprot.org/annotation/VAR_023798|||http://purl.uniprot.org/annotation/VAR_023799|||http://purl.uniprot.org/annotation/VAR_023800|||http://purl.uniprot.org/annotation/VAR_023801|||http://purl.uniprot.org/annotation/VAR_023802|||http://purl.uniprot.org/annotation/VAR_038418|||http://purl.uniprot.org/annotation/VAR_071335|||http://purl.uniprot.org/annotation/VAR_071336|||http://purl.uniprot.org/annotation/VAR_071337|||http://purl.uniprot.org/annotation/VAR_071338|||http://purl.uniprot.org/annotation/VAR_071339|||http://purl.uniprot.org/annotation/VAR_071340|||http://purl.uniprot.org/annotation/VAR_071341|||http://purl.uniprot.org/annotation/VAR_071342|||http://purl.uniprot.org/annotation/VAR_071343|||http://purl.uniprot.org/annotation/VAR_071344|||http://purl.uniprot.org/annotation/VAR_071345|||http://purl.uniprot.org/annotation/VAR_071346|||http://purl.uniprot.org/annotation/VAR_071347|||http://purl.uniprot.org/annotation/VAR_071348|||http://purl.uniprot.org/annotation/VAR_071349|||http://purl.uniprot.org/annotation/VAR_071350|||http://purl.uniprot.org/annotation/VAR_071351|||http://purl.uniprot.org/annotation/VAR_071352|||http://purl.uniprot.org/annotation/VAR_071353|||http://purl.uniprot.org/annotation/VAR_071354|||http://purl.uniprot.org/annotation/VAR_071355|||http://purl.uniprot.org/annotation/VAR_071356|||http://purl.uniprot.org/annotation/VAR_071357|||http://purl.uniprot.org/annotation/VAR_071358
http://togogenome.org/gene/9606:CCDC71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV32                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Coiled-coil domain-containing protein 71|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234421|||http://purl.uniprot.org/annotation/VAR_026236|||http://purl.uniprot.org/annotation/VAR_026237
http://togogenome.org/gene/9606:CD48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1S7|||http://purl.uniprot.org/uniprot/P09326                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CD48 antigen|||GPI-anchor amidated serine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014881|||http://purl.uniprot.org/annotation/PRO_0000014882|||http://purl.uniprot.org/annotation/PRO_5001832191|||http://purl.uniprot.org/annotation/VAR_020082|||http://purl.uniprot.org/annotation/VAR_049909|||http://purl.uniprot.org/annotation/VSP_055598|||http://purl.uniprot.org/annotation/VSP_055599
http://togogenome.org/gene/9606:RAB40B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12829                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Lipid Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Ras-related protein Rab-40B|||S-geranylgeranyl cysteine|||S-palmitoyl cysteine|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121259
http://togogenome.org/gene/9606:FRMD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVP2|||http://purl.uniprot.org/uniprot/B3KVN9|||http://purl.uniprot.org/uniprot/H0YKW6|||http://purl.uniprot.org/uniprot/Q7Z6J6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FERM|||FERM C-terminal PH-like|||FERM adjacent|||FERM domain-containing protein 5|||Helical|||In NEDEMA.|||In NEDEMA; unknown pathological significance.|||In isoform 2.|||Interaction with ROCK1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247446|||http://purl.uniprot.org/annotation/VAR_087746|||http://purl.uniprot.org/annotation/VAR_087747|||http://purl.uniprot.org/annotation/VAR_087748|||http://purl.uniprot.org/annotation/VAR_087749|||http://purl.uniprot.org/annotation/VAR_087750|||http://purl.uniprot.org/annotation/VAR_087751|||http://purl.uniprot.org/annotation/VAR_087752|||http://purl.uniprot.org/annotation/VSP_019982
http://togogenome.org/gene/9606:PRR36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6K5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Proline-rich protein 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329437|||http://purl.uniprot.org/annotation/VSP_057467
http://togogenome.org/gene/9606:N4BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2ZZ87|||http://purl.uniprot.org/uniprot/Q86UW6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||CUE|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||NEDD4-binding protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Smr                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096681|||http://purl.uniprot.org/annotation/VAR_035474|||http://purl.uniprot.org/annotation/VAR_051215|||http://purl.uniprot.org/annotation/VAR_051216|||http://purl.uniprot.org/annotation/VAR_051217|||http://purl.uniprot.org/annotation/VAR_051218|||http://purl.uniprot.org/annotation/VSP_009721
http://togogenome.org/gene/9606:OR10A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWR0|||http://purl.uniprot.org/uniprot/Q9H207                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150687|||http://purl.uniprot.org/annotation/VAR_034282
http://togogenome.org/gene/9606:CEP131                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L2J8|||http://purl.uniprot.org/uniprot/Q9UPN4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 131 kDa|||Disordered|||IQ|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with PLK4|||No effect on interaction with 14-3-3.|||Partially reduces in vitro phosphorylation by MAPKAPK2 and decreases binding to 14-3-3. Abolishes in vitro phosphorylation by MAPKAPK2, interaction with 14-3-3 and stress-induced centriolar satellite remodeling; when associated with A-47. Loss of PLK4-mediated phosphorylation. No effect on its localization to centriole and centriolar satellite or on its function in ciliogenesis. Cannot rescue centriolar satellite dispersion defect mediated by deletion of CEP131.|||Partially reduces in vitro phosphorylation by MAPKAPK2 and decreases binding to 14-3-3. Abolishes in vitro phosphorylation by MAPKAPK2, interaction with 14-3-3 and stress-induced centriolar satellite remodeling; when associated with A-78.|||Phosphomimetic mutant. No effect on its localization to centriole and centriolar satellite or on its function in ciliogenesis. Can rescue centriolar satellite dispersion defect mediated by deletion of CEP131.|||Phosphoserine|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by MAPKAPK2 and PLK4|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064781|||http://purl.uniprot.org/annotation/VAR_056740|||http://purl.uniprot.org/annotation/VAR_060226|||http://purl.uniprot.org/annotation/VAR_060227|||http://purl.uniprot.org/annotation/VAR_060228|||http://purl.uniprot.org/annotation/VAR_060229|||http://purl.uniprot.org/annotation/VSP_015823|||http://purl.uniprot.org/annotation/VSP_040204
http://togogenome.org/gene/9606:COL4A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7MBN3|||http://purl.uniprot.org/uniprot/P29400|||http://purl.uniprot.org/uniprot/Q49AM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen IV NC1|||Collagen alpha-5(IV) chain|||Disordered|||In ATS1.|||In ATS1; adult and juvenile types.|||In ATS1; adult type.|||In ATS1; found on the same allele as variant Glu-1211.|||In ATS1; found on the same allele as variant Val-953.|||In ATS1; juvenile and adult types.|||In ATS1; juvenile type.|||In ATS1; juvenile type; unknown pathological significance.|||In ATS1; mild phenotype.|||In ATS1; presenting with dot-and-fleck retinopathy.|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC2)|||Or C-1476 with C-1564|||Or C-1509 with C-1567|||Or C-1586 with C-1678|||Or C-1620 with C-1681|||Pro residues|||S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1549)|||S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1667)|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005852|||http://purl.uniprot.org/annotation/PRO_5005660708|||http://purl.uniprot.org/annotation/VAR_001914|||http://purl.uniprot.org/annotation/VAR_001915|||http://purl.uniprot.org/annotation/VAR_001916|||http://purl.uniprot.org/annotation/VAR_001917|||http://purl.uniprot.org/annotation/VAR_001918|||http://purl.uniprot.org/annotation/VAR_001919|||http://purl.uniprot.org/annotation/VAR_001920|||http://purl.uniprot.org/annotation/VAR_001921|||http://purl.uniprot.org/annotation/VAR_001922|||http://purl.uniprot.org/annotation/VAR_001923|||http://purl.uniprot.org/annotation/VAR_001924|||http://purl.uniprot.org/annotation/VAR_001925|||http://purl.uniprot.org/annotation/VAR_001926|||http://purl.uniprot.org/annotation/VAR_001927|||http://purl.uniprot.org/annotation/VAR_001928|||http://purl.uniprot.org/annotation/VAR_001929|||http://purl.uniprot.org/annotation/VAR_001930|||http://purl.uniprot.org/annotation/VAR_001931|||http://purl.uniprot.org/annotation/VAR_001932|||http://purl.uniprot.org/annotation/VAR_001933|||http://purl.uniprot.org/annotation/VAR_001934|||http://purl.uniprot.org/annotation/VAR_001935|||http://purl.uniprot.org/annotation/VAR_001936|||http://purl.uniprot.org/annotation/VAR_001937|||http://purl.uniprot.org/annotation/VAR_001938|||http://purl.uniprot.org/annotation/VAR_001939|||http://purl.uniprot.org/annotation/VAR_001940|||http://purl.uniprot.org/annotation/VAR_001941|||http://purl.uniprot.org/annotation/VAR_001942|||http://purl.uniprot.org/annotation/VAR_001943|||http://purl.uniprot.org/annotation/VAR_001944|||http://purl.uniprot.org/annotation/VAR_001945|||http://purl.uniprot.org/annotation/VAR_001946|||http://purl.uniprot.org/annotation/VAR_001947|||http://purl.uniprot.org/annotation/VAR_001948|||http://purl.uniprot.org/annotation/VAR_001949|||http://purl.uniprot.org/annotation/VAR_001950|||http://purl.uniprot.org/annotation/VAR_001951|||http://purl.uniprot.org/annotation/VAR_001952|||http://purl.uniprot.org/annotation/VAR_001953|||http://purl.uniprot.org/annotation/VAR_001954|||http://purl.uniprot.org/annotation/VAR_001955|||http://purl.uniprot.org/annotation/VAR_001956|||http://purl.uniprot.org/annotation/VAR_001957|||http://purl.uniprot.org/annotation/VAR_001958|||http://purl.uniprot.org/annotation/VAR_001959|||http://purl.uniprot.org/annotation/VAR_001960|||http://purl.uniprot.org/annotation/VAR_001961|||http://purl.uniprot.org/annotation/VAR_001962|||http://purl.uniprot.org/annotation/VAR_001963|||http://purl.uniprot.org/annotation/VAR_001964|||http://purl.uniprot.org/annotation/VAR_001965|||http://purl.uniprot.org/annotation/VAR_001966|||http://purl.uniprot.org/annotation/VAR_001967|||http://purl.uniprot.org/annotation/VAR_001968|||http://purl.uniprot.org/annotation/VAR_001969|||http://purl.uniprot.org/annotation/VAR_001970|||http://purl.uniprot.org/annotation/VAR_001971|||http://purl.uniprot.org/annotation/VAR_001972|||http://purl.uniprot.org/annotation/VAR_001973|||http://purl.uniprot.org/annotation/VAR_001974|||http://purl.uniprot.org/annotation/VAR_007991|||http://purl.uniprot.org/annotation/VAR_007992|||http://purl.uniprot.org/annotation/VAR_007993|||http://purl.uniprot.org/annotation/VAR_007994|||http://purl.uniprot.org/annotation/VAR_007995|||http://purl.uniprot.org/annotation/VAR_007996|||http://purl.uniprot.org/annotation/VAR_007997|||http://purl.uniprot.org/annotation/VAR_007998|||http://purl.uniprot.org/annotation/VAR_007999|||http://purl.uniprot.org/annotation/VAR_008000|||http://purl.uniprot.org/annotation/VAR_008001|||http://purl.uniprot.org/annotation/VAR_008002|||http://purl.uniprot.org/annotation/VAR_008003|||http://purl.uniprot.org/annotation/VAR_008004|||http://purl.uniprot.org/annotation/VAR_008005|||http://purl.uniprot.org/annotation/VAR_008006|||http://purl.uniprot.org/annotation/VAR_008007|||http://purl.uniprot.org/annotation/VAR_008008|||http://purl.uniprot.org/annotation/VAR_008009|||http://purl.uniprot.org/annotation/VAR_008010|||http://purl.uniprot.org/annotation/VAR_008011|||http://purl.uniprot.org/annotation/VAR_008012|||http://purl.uniprot.org/annotation/VAR_008013|||http://purl.uniprot.org/annotation/VAR_008014|||http://purl.uniprot.org/annotation/VAR_008015|||http://purl.uniprot.org/annotation/VAR_008016|||http://purl.uniprot.org/annotation/VAR_011220|||http://purl.uniprot.org/annotation/VAR_011221|||http://purl.uniprot.org/annotation/VAR_011222|||http://purl.uniprot.org/annotation/VAR_011223|||http://purl.uniprot.org/annotation/VAR_011224|||http://purl.uniprot.org/annotation/VAR_011225|||http://purl.uniprot.org/annotation/VAR_011226|||http://purl.uniprot.org/annotation/VAR_011227|||http://purl.uniprot.org/annotation/VAR_011228|||http://purl.uniprot.org/annotation/VAR_011229|||http://purl.uniprot.org/annotation/VAR_011230|||http://purl.uniprot.org/annotation/VAR_011231|||http://purl.uniprot.org/annotation/VAR_011232|||http://purl.uniprot.org/annotation/VAR_011233|||http://purl.uniprot.org/annotation/VAR_011234|||http://purl.uniprot.org/annotation/VAR_011235|||http://purl.uniprot.org/annotation/VAR_011236|||http://purl.uniprot.org/annotation/VAR_011237|||http://purl.uniprot.org/annotation/VAR_011238|||http://purl.uniprot.org/annotation/VAR_011239|||http://purl.uniprot.org/annotation/VAR_011240|||http://purl.uniprot.org/annotation/VAR_011241|||http://purl.uniprot.org/annotation/VAR_011242|||http://purl.uniprot.org/annotation/VAR_011243|||http://purl.uniprot.org/annotation/VAR_011244|||http://purl.uniprot.org/annotation/VAR_011245|||http://purl.uniprot.org/annotation/VAR_011246|||http://purl.uniprot.org/annotation/VAR_011247|||http://purl.uniprot.org/annotation/VAR_011248|||http://purl.uniprot.org/annotation/VAR_011249|||http://purl.uniprot.org/annotation/VAR_011250|||http://purl.uniprot.org/annotation/VAR_011251|||http://purl.uniprot.org/annotation/VAR_011252|||http://purl.uniprot.org/annotation/VAR_011253|||http://purl.uniprot.org/annotation/VAR_011254|||http://purl.uniprot.org/annotation/VAR_011255|||http://purl.uniprot.org/annotation/VAR_011256|||http://purl.uniprot.org/annotation/VAR_011257|||http://purl.uniprot.org/annotation/VAR_011258|||http://purl.uniprot.org/annotation/VAR_011259|||http://purl.uniprot.org/annotation/VAR_011260|||http://purl.uniprot.org/annotation/VAR_011261|||http://purl.uniprot.org/annotation/VAR_011262|||http://purl.uniprot.org/annotation/VAR_011263|||http://purl.uniprot.org/annotation/VAR_011264|||http://purl.uniprot.org/annotation/VAR_011265|||http://purl.uniprot.org/annotation/VAR_011266|||http://purl.uniprot.org/annotation/VAR_011267|||http://purl.uniprot.org/annotation/VAR_011268|||http://purl.uniprot.org/annotation/VAR_011269|||http://purl.uniprot.org/annotation/VAR_011270|||http://purl.uniprot.org/annotation/VAR_011271|||http://purl.uniprot.org/annotation/VAR_011272|||http://purl.uniprot.org/annotation/VAR_011273|||http://purl.uniprot.org/annotation/VAR_011274|||http://purl.uniprot.org/annotation/VAR_011275|||http://purl.uniprot.org/annotation/VAR_011276|||http://purl.uniprot.org/annotation/VAR_011277|||http://purl.uniprot.org/annotation/VAR_011278|||http://purl.uniprot.org/annotation/VAR_011279|||http://purl.uniprot.org/annotation/VAR_011280|||http://purl.uniprot.org/annotation/VAR_011281|||http://purl.uniprot.org/annotation/VAR_011282|||http://purl.uniprot.org/annotation/VAR_011283|||http://purl.uniprot.org/annotation/VAR_011284|||http://purl.uniprot.org/annotation/VAR_011285|||http://purl.uniprot.org/annotation/VAR_011286|||http://purl.uniprot.org/annotation/VAR_011287|||http://purl.uniprot.org/annotation/VAR_011288|||http://purl.uniprot.org/annotation/VAR_011289|||http://purl.uniprot.org/annotation/VAR_011290|||http://purl.uniprot.org/annotation/VAR_011291|||http://purl.uniprot.org/annotation/VAR_019594|||http://purl.uniprot.org/annotation/VAR_019595|||http://purl.uniprot.org/annotation/VAR_071932|||http://purl.uniprot.org/annotation/VSP_001173
http://togogenome.org/gene/9606:PIAS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMR4|||http://purl.uniprot.org/uniprot/Q8N2W9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Abolished SUMO ligase activity. Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347.|||Acidic residues|||Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules.|||Disordered|||E3 SUMO-protein ligase PIAS4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding.|||LXXLL motif|||Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding.|||N-acetylalanine|||N6-acetyllysine|||PINIT|||Removed|||SAP|||SP-RING-type|||Some loss of sumoylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218982
http://togogenome.org/gene/9606:DTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FN9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Variant                                                                                  ^@                                                                                  D-aminoacyl-tRNA deacylase 2|||Gly-transPro motif, allows the protein to recognize chirality of D-amino acids                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254049|||http://purl.uniprot.org/annotation/VAR_028802
http://togogenome.org/gene/9606:BACH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14867                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||Basic motif|||Disordered|||Leucine-zipper|||Phosphoserine|||Polar residues|||Transcription regulator protein BACH1|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076454|||http://purl.uniprot.org/annotation/VAR_048441
http://togogenome.org/gene/9606:KLRC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07444                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In allele NKG2-E*01 and allele NKG2-E*03; requires 2 nucleotide substitutions.|||In allele NKG2-E*02.|||In isoform NKG2-H.|||N-linked (GlcNAc...) asparagine|||NKG2-E type II integral membrane protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046671|||http://purl.uniprot.org/annotation/VAR_013296|||http://purl.uniprot.org/annotation/VAR_014660|||http://purl.uniprot.org/annotation/VAR_062954|||http://purl.uniprot.org/annotation/VAR_062955|||http://purl.uniprot.org/annotation/VAR_062956|||http://purl.uniprot.org/annotation/VAR_063132|||http://purl.uniprot.org/annotation/VAR_063133|||http://purl.uniprot.org/annotation/VSP_003067
http://togogenome.org/gene/9606:NEUROG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4Z2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In DIAR4; attenuated NEUROG3 function in vivo.|||Neurogenin-3|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127402|||http://purl.uniprot.org/annotation/VAR_029003|||http://purl.uniprot.org/annotation/VAR_029004|||http://purl.uniprot.org/annotation/VAR_055316
http://togogenome.org/gene/9606:MYSM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVJ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes H2A deubiquitination.|||Deubiquitinase MYSM1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BMFS4.|||In isoform 2.|||In isoform 3.|||JAMM motif|||LXXLL motif|||MPN|||Phosphoserine|||Phosphothreonine|||SANT|||SWIRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234073|||http://purl.uniprot.org/annotation/VAR_051814|||http://purl.uniprot.org/annotation/VAR_051815|||http://purl.uniprot.org/annotation/VAR_051816|||http://purl.uniprot.org/annotation/VAR_081184|||http://purl.uniprot.org/annotation/VAR_081185|||http://purl.uniprot.org/annotation/VSP_018210|||http://purl.uniprot.org/annotation/VSP_018211
http://togogenome.org/gene/9606:PWWP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9M0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||PWWP|||PWWP domain-containing DNA repair factor 3B|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257832|||http://purl.uniprot.org/annotation/VAR_057776
http://togogenome.org/gene/9606:ARHGEF26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU4|||http://purl.uniprot.org/uniprot/B3KXG0|||http://purl.uniprot.org/uniprot/Q96DR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  DH|||Disordered|||Fails to localize at sites of membrane ruffling.|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 26|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322568|||http://purl.uniprot.org/annotation/VAR_039425|||http://purl.uniprot.org/annotation/VAR_039426|||http://purl.uniprot.org/annotation/VAR_058205|||http://purl.uniprot.org/annotation/VSP_031934|||http://purl.uniprot.org/annotation/VSP_031935|||http://purl.uniprot.org/annotation/VSP_045570
http://togogenome.org/gene/9606:SLC26A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZI7|||http://purl.uniprot.org/uniprot/Q8TE54                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anion exchange transporter|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Membrane targeting|||Probable disease-associated variant found in patients with thyroid dyshormonogenesis and congenital goitrous hypothyroidism.|||Probable disease-associated variant found in patients with thyroid dyshormonogenesis and congenital goitrous hypothyroidism; loss of membrane localization and iodide transporter activity.|||STAS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320681|||http://purl.uniprot.org/annotation/VAR_053666|||http://purl.uniprot.org/annotation/VAR_053667|||http://purl.uniprot.org/annotation/VAR_088113|||http://purl.uniprot.org/annotation/VAR_088114|||http://purl.uniprot.org/annotation/VSP_052689
http://togogenome.org/gene/9606:PLCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Inactive phospholipase C-like protein 2|||N-acetylalanine|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288851|||http://purl.uniprot.org/annotation/VAR_032507|||http://purl.uniprot.org/annotation/VAR_032508|||http://purl.uniprot.org/annotation/VAR_032509|||http://purl.uniprot.org/annotation/VAR_032510|||http://purl.uniprot.org/annotation/VAR_032511|||http://purl.uniprot.org/annotation/VSP_025790|||http://purl.uniprot.org/annotation/VSP_025791|||http://purl.uniprot.org/annotation/VSP_025792
http://togogenome.org/gene/9606:MAP3K4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1M2|||http://purl.uniprot.org/uniprot/Q9Y6R4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of activity.|||Mitogen-activated protein kinase kinase kinase 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086247|||http://purl.uniprot.org/annotation/VAR_040686|||http://purl.uniprot.org/annotation/VAR_040687|||http://purl.uniprot.org/annotation/VAR_040688|||http://purl.uniprot.org/annotation/VAR_040689|||http://purl.uniprot.org/annotation/VAR_040690|||http://purl.uniprot.org/annotation/VAR_040691|||http://purl.uniprot.org/annotation/VAR_040692|||http://purl.uniprot.org/annotation/VAR_059767|||http://purl.uniprot.org/annotation/VSP_004884
http://togogenome.org/gene/9606:DEF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4E7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes PtdInsP3 binding.|||Abolishes interaction with RAC1.|||Basic and acidic residues|||Differentially expressed in FDCP 6 homolog|||Disordered|||In IMD87; affects function in vesicle-mediated protein transport as shown by impaired CTLA4 trafficking to cell surface in homozygous patient T cells; decreased interaction with RAB11A.|||In IMD87; affects function in vesicle-mediated protein transport as shown by impaired CTLA4 trafficking to cell surface in homozygous patient T cells; severely decreased protein levels in patient T cells; increased protein degradation.|||In IMD87; protein not detected in homozygous patient T cells or when the mutant is expressed in a heterologous system.|||Loss of phosphorylation by LCK and abolition of PtdInsP3 binding.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294522|||http://purl.uniprot.org/annotation/VAR_033193|||http://purl.uniprot.org/annotation/VAR_033194|||http://purl.uniprot.org/annotation/VAR_086410|||http://purl.uniprot.org/annotation/VAR_086411|||http://purl.uniprot.org/annotation/VAR_086412
http://togogenome.org/gene/9606:C1QL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75973                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  C1q|||C1q-related factor|||Collagen-like|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003527
http://togogenome.org/gene/9606:STARD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14849                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes ability to transfer cholesterol between membranes.|||Abolishes interaction with VAPA and VAPB, thereby preventing contact with the endoplasmic reticulum membrane.|||Abolishes interaction with VAPA, VAPB and MOSPD2, thereby preventing contact with the endoplasmic reticulum membrane. Abolishes cholesterol accumulation in endosomes.|||Abolishes localization to late endosomes and leads to mislocalization to the endoplasmic reticulum.|||Cytoplasmic|||Does not affect VAPA and VAPB interactions; when associated with A-210. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome; when associated with A-210. Restores cholesterol accumulation in late endosomes; when associated with A-210. Moderately interacts with MOSPD2. Almost impairs interaction with MOSPD2; when associated with A-210.|||Does not affect VAPA and VAPB interactions; when associated with D-209. Improve VAPA interaction. Does not interact with VAPA and VAPB. Recruits VAPA and VAPB around the endosome; when associated with D-209.Restores cholesterol accumulation in late endosomes; when associated with A-209. Almost impairs interaction with MOSPD2; when associated with A-209.|||Does not affect localization to late endosomes.|||Extracellular|||FFAT|||Helical|||Impairs VAPA and VAPB interaction. Does not affect endoplasmic reticulum membrane location of VAPA, VAPB and MOSPD2. Is unable to make ER-endosome contacts. Does not accumulate cholesterol in late endosomes (LEs). Does not interact with MOSPD2.|||In isoform 2.|||In isoform 3.|||MENTAL|||Phosphoserine|||START|||StAR-related lipid transfer protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220653|||http://purl.uniprot.org/annotation/VAR_027877|||http://purl.uniprot.org/annotation/VAR_027878|||http://purl.uniprot.org/annotation/VSP_042710|||http://purl.uniprot.org/annotation/VSP_045361
http://togogenome.org/gene/9606:TCF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Transcription factor 23|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315820|||http://purl.uniprot.org/annotation/VAR_038325|||http://purl.uniprot.org/annotation/VAR_038326
http://togogenome.org/gene/9606:BRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUW1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Protein BRICK1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283646|||http://purl.uniprot.org/annotation/VSP_024350
http://togogenome.org/gene/9606:CELSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||Acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cadherin EGF LAG seven-pass G-type receptor 2|||Cytoplasmic|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||Extracellular|||Found in a patient with congenital hydrocephalus; unknown pathological significance.|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Laminin EGF-like|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012916|||http://purl.uniprot.org/annotation/VAR_024481|||http://purl.uniprot.org/annotation/VAR_049474|||http://purl.uniprot.org/annotation/VAR_049475|||http://purl.uniprot.org/annotation/VAR_049476|||http://purl.uniprot.org/annotation/VAR_083430
http://togogenome.org/gene/9606:HMGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H2A4|||http://purl.uniprot.org/uniprot/F5H6H0|||http://purl.uniprot.org/uniprot/P52926|||http://purl.uniprot.org/uniprot/Q1M183                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||Disordered|||High mobility group protein HMGI-C|||In SRS5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with E4F1|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206711|||http://purl.uniprot.org/annotation/VAR_084335|||http://purl.uniprot.org/annotation/VSP_042564|||http://purl.uniprot.org/annotation/VSP_047772|||http://purl.uniprot.org/annotation/VSP_047773|||http://purl.uniprot.org/annotation/VSP_047774|||http://purl.uniprot.org/annotation/VSP_047775
http://togogenome.org/gene/9606:DLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K119|||http://purl.uniprot.org/uniprot/Q96QB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with EF1A1.|||Abolishes interaction with TNS4 and results in diffuse cytoplasmic localization.|||Basic and acidic residues|||Disordered|||Focal adhesion-targeting (FAT)|||In isoform 1 and isoform 4.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||No catalytic activity.|||Phosphoserine|||Polar residues|||Polybasic cluster (PBR)|||Rho GTPase-activating protein 7|||Rho-GAP|||SAM|||START|||Unable to displace endogenous DLC1 from focal adhesions. Abolishes interaction with TNS4 and results in diffuse cytoplasmic localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056707|||http://purl.uniprot.org/annotation/VAR_014229|||http://purl.uniprot.org/annotation/VAR_014230|||http://purl.uniprot.org/annotation/VAR_014231|||http://purl.uniprot.org/annotation/VAR_014232|||http://purl.uniprot.org/annotation/VAR_014233|||http://purl.uniprot.org/annotation/VAR_014234|||http://purl.uniprot.org/annotation/VAR_014235|||http://purl.uniprot.org/annotation/VAR_059293|||http://purl.uniprot.org/annotation/VAR_059294|||http://purl.uniprot.org/annotation/VAR_059295|||http://purl.uniprot.org/annotation/VAR_059296|||http://purl.uniprot.org/annotation/VAR_059297|||http://purl.uniprot.org/annotation/VAR_059298|||http://purl.uniprot.org/annotation/VSP_037871|||http://purl.uniprot.org/annotation/VSP_037872|||http://purl.uniprot.org/annotation/VSP_037873|||http://purl.uniprot.org/annotation/VSP_037874|||http://purl.uniprot.org/annotation/VSP_044651|||http://purl.uniprot.org/annotation/VSP_046331|||http://purl.uniprot.org/annotation/VSP_046332|||http://purl.uniprot.org/annotation/VSP_053836|||http://purl.uniprot.org/annotation/VSP_053837
http://togogenome.org/gene/9606:OR5M8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWD6|||http://purl.uniprot.org/uniprot/Q8NGP6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150606
http://togogenome.org/gene/9606:PVALB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20472                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Inactivation.|||N-acetylserine|||Parvalbumin alpha|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073588
http://togogenome.org/gene/9606:TRMO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T114|||http://purl.uniprot.org/uniprot/Q9BU70                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||TsaA-like|||tRNA (adenine(37)-N6)-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288886|||http://purl.uniprot.org/annotation/VAR_032527|||http://purl.uniprot.org/annotation/VAR_032528|||http://purl.uniprot.org/annotation/VAR_032529
http://togogenome.org/gene/9606:CKLF-CMTM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVB3|||http://purl.uniprot.org/uniprot/A0A087X286|||http://purl.uniprot.org/uniprot/E9PSG2                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Helical|||MARVEL                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TSKS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by TSSK1 and TSSK2|||Polar residues|||Testis-specific serine kinase substrate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065665|||http://purl.uniprot.org/annotation/VAR_036272|||http://purl.uniprot.org/annotation/VAR_051459|||http://purl.uniprot.org/annotation/VAR_051460|||http://purl.uniprot.org/annotation/VSP_009591|||http://purl.uniprot.org/annotation/VSP_009592|||http://purl.uniprot.org/annotation/VSP_009593
http://togogenome.org/gene/9606:RPS6KA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJF8|||http://purl.uniprot.org/uniprot/B4DPV1|||http://purl.uniprot.org/uniprot/E9PJN1|||http://purl.uniprot.org/uniprot/O75676                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by MAPK1, MAPK3 and MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by MAPK1, MAPK3 and MAPK14|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Required for nuclear targeting and association with MAPK14|||Ribosomal protein S6 kinase alpha-4|||Strongly elevates basal activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086205|||http://purl.uniprot.org/annotation/VAR_040632|||http://purl.uniprot.org/annotation/VAR_040633|||http://purl.uniprot.org/annotation/VSP_017733
http://togogenome.org/gene/9606:ABCF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7X1|||http://purl.uniprot.org/uniprot/Q9UG63                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093323|||http://purl.uniprot.org/annotation/VSP_054715
http://togogenome.org/gene/9606:PDHA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08559                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes inactivation by phosphorylation; when associated with A-232 and A-293.|||Abolishes inactivation by phosphorylation; when associated with A-293 and A-300.|||In PDHAD.|||In PDHAD; affects mitochondrial import of precursor protein.|||In PDHAD; loss of activity; common mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interferes with substrate binding.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by PDK1|||Phosphoserine; by PDK1, PDK2, PDK3 and PDK4|||Phosphotyrosine|||Probable disease-associated variant found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate.|||Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial|||Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020440|||http://purl.uniprot.org/annotation/VAR_004949|||http://purl.uniprot.org/annotation/VAR_004950|||http://purl.uniprot.org/annotation/VAR_004951|||http://purl.uniprot.org/annotation/VAR_004952|||http://purl.uniprot.org/annotation/VAR_004953|||http://purl.uniprot.org/annotation/VAR_004954|||http://purl.uniprot.org/annotation/VAR_004955|||http://purl.uniprot.org/annotation/VAR_004956|||http://purl.uniprot.org/annotation/VAR_004957|||http://purl.uniprot.org/annotation/VAR_004958|||http://purl.uniprot.org/annotation/VAR_004959|||http://purl.uniprot.org/annotation/VAR_004960|||http://purl.uniprot.org/annotation/VAR_004961|||http://purl.uniprot.org/annotation/VAR_004962|||http://purl.uniprot.org/annotation/VAR_004963|||http://purl.uniprot.org/annotation/VAR_004964|||http://purl.uniprot.org/annotation/VAR_004965|||http://purl.uniprot.org/annotation/VAR_004966|||http://purl.uniprot.org/annotation/VAR_010238|||http://purl.uniprot.org/annotation/VAR_020908|||http://purl.uniprot.org/annotation/VAR_020909|||http://purl.uniprot.org/annotation/VAR_021053|||http://purl.uniprot.org/annotation/VAR_021054|||http://purl.uniprot.org/annotation/VAR_021055|||http://purl.uniprot.org/annotation/VAR_021056|||http://purl.uniprot.org/annotation/VAR_050436|||http://purl.uniprot.org/annotation/VAR_069381|||http://purl.uniprot.org/annotation/VSP_042569|||http://purl.uniprot.org/annotation/VSP_042570|||http://purl.uniprot.org/annotation/VSP_043363
http://togogenome.org/gene/9606:WWTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZV5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of interaction with TEAD4.|||No effect on binding to PRRG4.|||PDZ-binding|||Partial resistance to inhibition by MST2 and LATS2.|||Phosphoserine|||Phosphoserine; by LATS2|||Polar residues|||Reduced binding to PRRG4.|||Required for interaction with PALS1|||Significant resistance to inhibition by STK3/MST2 and LATS2. No effect on binding to PRRG4.|||WW|||WW domain-containing transcription regulator protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076069
http://togogenome.org/gene/9606:CCR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0Q0|||http://purl.uniprot.org/uniprot/J3KSS9|||http://purl.uniprot.org/uniprot/P32248                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 7|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012735|||http://purl.uniprot.org/annotation/PRO_5003772096|||http://purl.uniprot.org/annotation/PRO_5014296520|||http://purl.uniprot.org/annotation/VAR_049383
http://togogenome.org/gene/9606:MID1IP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPA3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  Mid1-interacting protein 1|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123777
http://togogenome.org/gene/9606:COX4I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H6SG14|||http://purl.uniprot.org/uniprot/Q96KJ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 4 isoform 2, mitochondrial|||Disordered|||Helical|||In EPIDACH; expression in patient fibroblasts is reduced to 25% of control values in normoxic conditions; the mutant protein shows an impaired response to hypoxia.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006089|||http://purl.uniprot.org/annotation/VAR_033815|||http://purl.uniprot.org/annotation/VAR_058101
http://togogenome.org/gene/9606:OR11A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCH9|||http://purl.uniprot.org/uniprot/Q9GZK7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-18*02.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150722|||http://purl.uniprot.org/annotation/VAR_010955|||http://purl.uniprot.org/annotation/VAR_053294
http://togogenome.org/gene/9606:SRRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4W1|||http://purl.uniprot.org/uniprot/B7Z7U0|||http://purl.uniprot.org/uniprot/Q8IYB3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Necessary for DNA and RNA-binding|||Necessary for mRNA 3'-end cleavage and cytoplasmic accumulation|||Necessary for speckles and matrix localization|||PWI|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Serine/arginine repetitive matrix protein 1|||Strongly reduces DNA and RNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076326|||http://purl.uniprot.org/annotation/VAR_024065|||http://purl.uniprot.org/annotation/VSP_016522|||http://purl.uniprot.org/annotation/VSP_016523
http://togogenome.org/gene/9606:DBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10586                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic motif|||D site-binding protein|||Disordered|||Leucine-zipper|||Phosphoserine|||Pro residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076507
http://togogenome.org/gene/9606:LGALS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56470|||http://purl.uniprot.org/uniprot/Q6FHZ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Galectin|||Galectin 1|||Galectin 2|||Galectin-4|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076934|||http://purl.uniprot.org/annotation/VAR_049769
http://togogenome.org/gene/9606:SPAG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75602                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Sperm-associated antigen 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072095|||http://purl.uniprot.org/annotation/VAR_024282|||http://purl.uniprot.org/annotation/VAR_035659|||http://purl.uniprot.org/annotation/VSP_013442|||http://purl.uniprot.org/annotation/VSP_013443|||http://purl.uniprot.org/annotation/VSP_013444|||http://purl.uniprot.org/annotation/VSP_013445|||http://purl.uniprot.org/annotation/VSP_045337
http://togogenome.org/gene/9606:PCDHB15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R708|||http://purl.uniprot.org/uniprot/Q9Y5E8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003942|||http://purl.uniprot.org/annotation/PRO_5002780114|||http://purl.uniprot.org/annotation/VAR_019633|||http://purl.uniprot.org/annotation/VAR_019634|||http://purl.uniprot.org/annotation/VAR_036106|||http://purl.uniprot.org/annotation/VAR_036107
http://togogenome.org/gene/9606:DAND5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N907                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  CTCK|||DAN domain family member 5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311804
http://togogenome.org/gene/9606:TARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26639                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not restore in vitro translation, does not replace endogenous yeast enzyme.|||Does not restore in vitro translation, probably does not bind BN.|||In TTD7.|||In TTD7; loss of protein stability; loss of threonine-tRNA ligase activity.|||In isoform 2.|||N6-acetyllysine|||Partially restores in vitro translation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Replaces endogenous yeast enzyme.|||TGS|||Threonine--tRNA ligase 1, cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101119|||http://purl.uniprot.org/annotation/VAR_034533|||http://purl.uniprot.org/annotation/VAR_083226|||http://purl.uniprot.org/annotation/VAR_083227|||http://purl.uniprot.org/annotation/VAR_083228|||http://purl.uniprot.org/annotation/VSP_045114
http://togogenome.org/gene/9606:PIGU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H490                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreased function in GPI-anchor attachment to protein.|||Helical|||In NEDBSS.|||In isoform 2.|||May be involved in recognition of long-chain fatty acids in GPI|||No effect on function in GPI-anchor attachment to protein.|||Phosphatidylinositol glycan anchor biosynthesis class U protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121394|||http://purl.uniprot.org/annotation/VAR_083263|||http://purl.uniprot.org/annotation/VAR_083264|||http://purl.uniprot.org/annotation/VSP_009543
http://togogenome.org/gene/9606:RBM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57052                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Disordered|||In isoform 3.|||Polar residues|||RRM|||Splicing regulator RBM11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081769|||http://purl.uniprot.org/annotation/VAR_024621|||http://purl.uniprot.org/annotation/VSP_061576|||http://purl.uniprot.org/annotation/VSP_061577
http://togogenome.org/gene/9606:NFS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FP3|||http://purl.uniprot.org/uniprot/Q9Y697                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aminotransferase class V|||Cysteine desulfurase|||Cysteine persulfide|||Cysteine persulfide intermediate|||In COXPD52; decreased protein expression in homozygous patient cells.|||In isoform 3.|||In isoform Cytoplasmic.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||via persulfide group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001292|||http://purl.uniprot.org/annotation/VAR_085966|||http://purl.uniprot.org/annotation/VSP_018646|||http://purl.uniprot.org/annotation/VSP_045860
http://togogenome.org/gene/9606:ATP6V0D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61421                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Phosphoserine|||Phosphotyrosine|||V-type proton ATPase subunit d 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119350
http://togogenome.org/gene/9606:FBN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35555                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus.|||Asprosin|||C-terminal domain|||Cell attachment site|||Cleavage; by furin|||Defects in protein processing at the C-terminus.|||Disordered|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18; calcium-binding|||EGF-like 19; calcium-binding|||EGF-like 2|||EGF-like 20; calcium-binding|||EGF-like 21; calcium-binding|||EGF-like 22; calcium-binding|||EGF-like 23; calcium-binding|||EGF-like 24; calcium-binding|||EGF-like 25; calcium-binding|||EGF-like 26; calcium-binding|||EGF-like 27; calcium-binding|||EGF-like 28; calcium-binding|||EGF-like 29; calcium-binding|||EGF-like 3|||EGF-like 30; calcium-binding|||EGF-like 31; calcium-binding|||EGF-like 32; calcium-binding|||EGF-like 33; calcium-binding|||EGF-like 34; calcium-binding|||EGF-like 35; calcium-binding|||EGF-like 36; calcium-binding|||EGF-like 37; calcium-binding|||EGF-like 38; calcium-binding|||EGF-like 39; calcium-binding|||EGF-like 40; calcium-binding|||EGF-like 41; calcium-binding|||EGF-like 42; calcium-binding|||EGF-like 43; calcium-binding|||EGF-like 44; calcium-binding|||EGF-like 45; calcium-binding|||EGF-like 46; calcium-binding|||EGF-like 47; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibrillin unique N-terminal (FUN) domain|||Fibrillin-1|||Hybrid domain 1|||Hybrid domain 2|||In ACMICD.|||In ECTOL1 and MFS.|||In ECTOL1.|||In ECTOL1; patient presenting also flat corneas.|||In ECTOL1; patient presenting also mitral valve prolapse.|||In GPHYSD2 and ACMICD.|||In GPHYSD2.|||In MFLS.|||In MFS and ECTOL1.|||In MFS.|||In MFS; also found in a patient with Shprintzen-Goldberg craniosynostosis syndrome.|||In MFS; also in a patient with ectopia lentis and retinal detachment.|||In MFS; atypical.|||In MFS; enhances proteolytic degradation.|||In MFS; mild form.|||In MFS; neonatal form.|||In MFS; neonatal.|||In MFS; severe neonatal.|||In MFS; severe.|||In MFS; unknown pathological significance.|||In SSKS.|||In WMS2.|||In a patient with mitral valve prolapse.|||Interaction with MFAP4|||Loss of integrin-mediated cell adhesion.|||N-linked (GlcNAc...) asparagine|||N-terminal domain|||O-linked (Glc) serine|||Phosphoserine|||Phosphoserine; by FAM20C|||Probable disease-associated variant found in a patient with Marfan-like syndrome.|||Probable disease-associated variant found in a patient with Marfan-like syndrome; defects in protein processing.|||Probable disease-associated variant found in a patient with Marfan-like syndrome; prevents secretion into the extracellular matrix.|||TB 1|||TB 2|||TB 3|||TB 4|||TB 5|||TB 6|||TB 7|||TB 8|||TB 9                                                                                  ^@                                                                                  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://purl.uniprot.org/annotation/VAR_023906|||http://purl.uniprot.org/annotation/VAR_023907|||http://purl.uniprot.org/annotation/VAR_023908|||http://purl.uniprot.org/annotation/VAR_023909|||http://purl.uniprot.org/annotation/VAR_023910|||http://purl.uniprot.org/annotation/VAR_023912|||http://purl.uniprot.org/annotation/VAR_023913|||http://purl.uniprot.org/annotation/VAR_023914|||http://purl.uniprot.org/annotation/VAR_023915|||http://purl.uniprot.org/annotation/VAR_055723|||http://purl.uniprot.org/annotation/VAR_055724|||http://purl.uniprot.org/annotation/VAR_055725|||http://purl.uniprot.org/annotation/VAR_055726|||http://purl.uniprot.org/annotation/VAR_055727|||http://purl.uniprot.org/annotation/VAR_055728|||http://purl.uniprot.org/annotation/VAR_055729|||http://purl.uniprot.org/annotation/VAR_055730|||http://purl.uniprot.org/annotation/VAR_055731|||http://purl.uniprot.org/annotation/VAR_055732|||http://purl.uniprot.org/annotation/VAR_055733|||http://purl.uniprot.org/annotation/VAR_055734|||http://purl.uniprot.org/annotation/VAR_055735|||http://purl.uniprot.org/annotation/VAR_058090|||http://purl.uniprot.org/annotation/VAR_064046|||http://purl.uniprot.org/annotation/VAR_064047|||http://purl.uniprot.org/annotation/VAR_064048|||http://purl.uniprot.org/annotation/VAR_064049|||http://purl.uniprot.org/annotation/VAR_064503|||http://purl.uniprot.org/annotation/VAR_065981|||http://purl.uniprot.org/annotation/VAR_065982|||http://purl.uniprot.org/annotation/VAR_065983|||http://purl.uniprot.org/annotation/VAR_065984|||http://purl.uniprot.org/annotation/VAR_065985|||http://purl.uniprot.org/annotation/VAR_065986|||http://purl.uniprot.org/annotation/VAR_065987|||http://purl.uniprot.org/annotation/VAR_065988|||http://purl.uniprot.org/annotation/VAR_065989|||http://purl.uniprot.org/annotation/VAR_065990|||http://purl.uniprot.org/annotation/VAR_065991|||http://purl.uniprot.org/annotation/VAR_065992|||http://purl.uniprot.org/annotation/VAR_065993|||http://purl.uniprot.org/annotation/VAR_065994|||http://purl.uniprot.org/annotation/VAR_065995|||http://purl.uniprot.org/annotation/VAR_065996|||http://purl.uniprot.org/annotation/VAR_065997|||http://purl.uniprot.org/annotation/VAR_065998|||http://purl.uniprot.org/annotation/VAR_065999|||http://purl.uniprot.org/annotation/VAR_066000|||http://purl.uniprot.org/annotation/VAR_066001|||http://purl.uniprot.org/annotation/VAR_066002|||http://purl.uniprot.org/annotation/VAR_066003|||http://purl.uniprot.org/annotation/VAR_066004|||http://purl.uniprot.org/annotation/VAR_066005|||http://purl.uniprot.org/annotation/VAR_066006|||http://purl.uniprot.org/annotation/VAR_066007|||http://purl.uniprot.org/annotation/VAR_066008|||http://purl.uniprot.org/annotation/VAR_066009|||http://purl.uniprot.org/annotation/VAR_066010|||http://purl.uniprot.org/annotation/VAR_066011|||http://purl.uniprot.org/annotation/VAR_066527|||http://purl.uniprot.org/annotation/VAR_066528|||http://purl.uniprot.org/annotation/VAR_066529|||http://purl.uniprot.org/annotation/VAR_066530|||http://purl.uniprot.org/annotation/VAR_066531|||http://purl.uniprot.org/annotation/VAR_066532|||http://purl.uniprot.org/annotation/VAR_066533|||http://purl.uniprot.org/annotation/VAR_066534|||http://purl.uniprot.org/annotation/VAR_066535|||http://purl.uniprot.org/annotation/VAR_066536|||http://purl.uniprot.org/annotation/VAR_066537|||http://purl.uniprot.org/annotation/VAR_066538|||http://purl.uniprot.org/annotation/VAR_066539|||http://purl.uniprot.org/annotation/VAR_066540|||http://purl.uniprot.org/annotation/VAR_066541|||http://purl.uniprot.org/annotation/VAR_066542|||http://purl.uniprot.org/annotation/VAR_075984|||http://purl.uniprot.org/annotation/VAR_075985|||http://purl.uniprot.org/annotation/VAR_075986|||http://purl.uniprot.org/annotation/VAR_075987|||http://purl.uniprot.org/annotation/VAR_075988|||http://purl.uniprot.org/annotation/VAR_075989|||http://purl.uniprot.org/annotation/VAR_075990|||http://purl.uniprot.org/annotation/VAR_075991|||http://purl.uniprot.org/annotation/VAR_075992|||http://purl.uniprot.org/annotation/VAR_075993|||http://purl.uniprot.org/annotation/VAR_075994|||http://purl.uniprot.org/annotation/VAR_075995|||http://purl.uniprot.org/annotation/VAR_075996|||http://purl.uniprot.org/annotation/VAR_075997|||http://purl.uniprot.org/annotation/VAR_075998|||http://purl.uniprot.org/annotation/VAR_075999|||http://purl.uniprot.org/annotation/VAR_076000|||http://purl.uniprot.org/annotation/VAR_076001|||http://purl.uniprot.org/annotation/VAR_076002|||http://purl.uniprot.org/annotation/VAR_076003|||http://purl.uniprot.org/annotation/VAR_076004|||http://purl.uniprot.org/annotation/VAR_076005|||http://purl.uniprot.org/annotation/VAR_076006|||http://purl.uniprot.org/annotation/VAR_076007|||http://purl.uniprot.org/annotation/VAR_076008|||http://purl.uniprot.org/annotation/VAR_076009|||http://purl.uniprot.org/annotation/VAR_076010|||http://purl.uniprot.org/annotation/VAR_076011|||http://purl.uniprot.org/annotation/VAR_076012|||http://purl.uniprot.org/annotation/VAR_076013|||http://purl.uniprot.org/annotation/VAR_076014|||http://purl.uniprot.org/annotation/VAR_076015|||http://purl.uniprot.org/annotation/VAR_076016|||http://purl.uniprot.org/annotation/VAR_076017|||http://purl.uniprot.org/annotation/VAR_076018|||http://purl.uniprot.org/annotation/VAR_076019|||http://purl.uniprot.org/annotation/VAR_076020|||http://purl.uniprot.org/annotation/VAR_076021|||http://purl.uniprot.org/annotation/VAR_076022|||http://purl.uniprot.org/annotation/VAR_076023|||http://purl.uniprot.org/annotation/VAR_076024|||http://purl.uniprot.org/annotation/VAR_076025|||http://purl.uniprot.org/annotation/VAR_076026|||http://purl.uniprot.org/annotation/VAR_076027|||http://purl.uniprot.org/annotation/VAR_076028|||http://purl.uniprot.org/annotation/VAR_076029|||http://purl.uniprot.org/annotation/VAR_076030|||http://purl.uniprot.org/annotation/VAR_076031|||http://purl.uniprot.org/annotation/VAR_076032|||http://purl.uniprot.org/annotation/VAR_076033|||http://purl.uniprot.org/annotation/VAR_076034|||http://purl.uniprot.org/annotation/VAR_076035|||http://purl.uniprot.org/annotation/VAR_076036|||http://purl.uniprot.org/annotation/VAR_076037|||http://purl.uniprot.org/annotation/VAR_076038|||http://purl.uniprot.org/annotation/VAR_076039|||http://purl.uniprot.org/annotation/VAR_076040|||http://purl.uniprot.org/annotation/VAR_076041|||http://purl.uniprot.org/annotation/VAR_076042|||http://purl.uniprot.org/annotation/VAR_076043|||http://purl.uniprot.org/annotation/VAR_076044|||http://purl.uniprot.org/annotation/VAR_076045|||http://purl.uniprot.org/annotation/VAR_076046|||http://purl.uniprot.org/annotation/VAR_076047|||http://purl.uniprot.org/annotation/VAR_076048|||http://purl.uniprot.org/annotation/VAR_076049|||http://purl.uniprot.org/annotation/VAR_076050|||http://purl.uniprot.org/annotation/VAR_076051|||http://purl.uniprot.org/annotation/VAR_076052|||http://purl.uniprot.org/annotation/VAR_076053|||http://purl.uniprot.org/annotation/VAR_076054|||http://purl.uniprot.org/annotation/VAR_076055|||http://purl.uniprot.org/annotation/VAR_076056|||http://purl.uniprot.org/annotation/VAR_076057|||http://purl.uniprot.org/annotation/VAR_076058|||http://purl.uniprot.org/annotation/VAR_076059|||http://purl.uniprot.org/annotation/VAR_076060|||http://purl.uniprot.org/annotation/VAR_076061|||http://purl.uniprot.org/annotation/VAR_076062|||http://purl.uniprot.org/annotation/VAR_076063|||http://purl.uniprot.org/annotation/VAR_076064|||http://purl.uniprot.org/annotation/VAR_076065|||http://purl.uniprot.org/annotation/VAR_076066|||http://purl.uniprot.org/annotation/VAR_076067|||http://purl.uniprot.org/annotation/VAR_076068|||http://purl.uniprot.org/annotation/VAR_076069|||http://purl.uniprot.org/annotation/VAR_076070|||http://purl.uniprot.org/annotation/VAR_076071|||http://purl.uniprot.org/annotation/VAR_076072|||http://purl.uniprot.org/annotation/VAR_076073|||http://purl.uniprot.org/annotation/VAR_076074|||http://purl.uniprot.org/annotation/VAR_076075|||http://purl.uniprot.org/annotation/VAR_076076|||http://purl.uniprot.org/annotation/VAR_076077|||http://purl.uniprot.org/annotation/VAR_076078|||http://purl.uniprot.org/annotation/VAR_076079|||http://purl.uniprot.org/annotation/VAR_076080|||http://purl.uniprot.org/annotation/VAR_076081|||http://purl.uniprot.org/annotation/VAR_076082|||http://purl.uniprot.org/annotation/VAR_076083|||http://purl.uniprot.org/annotation/VAR_076084|||http://purl.uniprot.org/annotation/VAR_076085|||http://purl.uniprot.org/annotation/VAR_076086|||http://purl.uniprot.org/annotation/VAR_076087|||http://purl.uniprot.org/annotation/VAR_076088|||http://purl.uniprot.org/annotation/VAR_076089|||http://purl.uniprot.org/annotation/VAR_076090|||http://purl.uniprot.org/annotation/VAR_076091|||http://purl.uniprot.org/annotation/VAR_076092|||http://purl.uniprot.org/annotation/VAR_076093|||http://purl.uniprot.org/annotation/VAR_076094|||http://purl.uniprot.org/annotation/VAR_076095|||http://purl.uniprot.org/annotation/VAR_076096|||http://purl.uniprot.org/annotation/VAR_076097|||http://purl.uniprot.org/annotation/VAR_076098|||http://purl.uniprot.org/annotation/VAR_076099|||http://purl.uniprot.org/annotation/VAR_076100|||http://purl.uniprot.org/annotation/VAR_076101|||http://purl.uniprot.org/annotation/VAR_076102|||http://purl.uniprot.org/annotation/VAR_076103|||http://purl.uniprot.org/annotation/VAR_076104|||http://purl.uniprot.org/annotation/VAR_076105|||http://purl.uniprot.org/annotation/VAR_076106|||http://purl.uniprot.org/annotation/VAR_076107|||http://purl.uniprot.org/annotation/VAR_076108|||http://purl.uniprot.org/annotation/VAR_076109|||http://purl.uniprot.org/annotation/VAR_076110|||http://purl.uniprot.org/annotation/VAR_076111|||http://purl.uniprot.org/annotation/VAR_076112|||http://purl.uniprot.org/annotation/VAR_076113|||http://purl.uniprot.org/annotation/VAR_076114|||http://purl.uniprot.org/annotation/VAR_076115|||http://purl.uniprot.org/annotation/VAR_076116|||http://purl.uniprot.org/annotation/VAR_076117|||http://purl.uniprot.org/annotation/VAR_076118|||http://purl.uniprot.org/annotation/VAR_076119|||http://purl.uniprot.org/annotation/VAR_076120|||http://purl.uniprot.org/annotation/VAR_076121|||http://purl.uniprot.org/annotation/VAR_076122|||http://purl.uniprot.org/annotation/VAR_076123|||http://purl.uniprot.org/annotation/VAR_076124|||http://purl.uniprot.org/annotation/VAR_076125|||http://purl.uniprot.org/annotation/VAR_076126|||http://purl.uniprot.org/annotation/VAR_076127|||http://purl.uniprot.org/annotation/VAR_076128|||http://purl.uniprot.org/annotation/VAR_076129|||http://purl.uniprot.org/annotation/VAR_076130|||http://purl.uniprot.org/annotation/VAR_076131|||http://purl.uniprot.org/annotation/VAR_076132|||http://purl.uniprot.org/annotation/VAR_076133|||http://purl.uniprot.org/annotation/VAR_076134|||http://purl.uniprot.org/annotation/VAR_076135|||http://purl.uniprot.org/annotation/VAR_076136|||http://purl.uniprot.org/annotation/VAR_076137|||http://purl.uniprot.org/annotation/VAR_076138|||http://purl.uniprot.org/annotation/VAR_076139|||http://purl.uniprot.org/annotation/VAR_076140|||http://purl.uniprot.org/annotation/VAR_076141|||http://purl.uniprot.org/annotation/VAR_076142|||http://purl.uniprot.org/annotation/VAR_076143|||http://purl.uniprot.org/annotation/VAR_076144|||http://purl.uniprot.org/annotation/VAR_076145|||http://purl.uniprot.org/annotation/VAR_076146|||http://purl.uniprot.org/annotation/VAR_076147|||http://purl.uniprot.org/annotation/VAR_076148|||http://purl.uniprot.org/annotation/VAR_076149|||http://purl.uniprot.org/annotation/VAR_076150|||http://purl.uniprot.org/annotation/VAR_076151|||http://purl.uniprot.org/annotation/VAR_076152|||http://purl.uniprot.org/annotation/VAR_076153|||http://purl.uniprot.org/annotation/VAR_076154|||http://purl.uniprot.org/annotation/VAR_076155|||http://purl.uniprot.org/annotation/VAR_076156|||http://purl.uniprot.org/annotation/VAR_076157|||http://purl.uniprot.org/annotation/VAR_076158|||http://purl.uniprot.org/annotation/VAR_076159|||http://purl.uniprot.org/annotation/VAR_076160|||http://purl.uniprot.org/annotation/VAR_076161|||http://purl.uniprot.org/annotation/VAR_076162|||http://purl.uniprot.org/annotation/VAR_076163|||http://purl.uniprot.org/annotation/VAR_076164|||http://purl.uniprot.org/annotation/VAR_076165|||http://purl.uniprot.org/annotation/VAR_076166|||http://purl.uniprot.org/annotation/VAR_080327
http://togogenome.org/gene/9606:ZSCAN32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX65                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047582|||http://purl.uniprot.org/annotation/VAR_024215|||http://purl.uniprot.org/annotation/VAR_052826|||http://purl.uniprot.org/annotation/VSP_046571|||http://purl.uniprot.org/annotation/VSP_055988
http://togogenome.org/gene/9606:NCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM80|||http://purl.uniprot.org/uniprot/P19338                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5; truncated|||6|||7|||8|||8 X 8 AA tandem repeats of X-T-P-X-K-K-X-X|||Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nucleolin|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||RRM 3|||RRM 4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081691|||http://purl.uniprot.org/annotation/VAR_046353|||http://purl.uniprot.org/annotation/VAR_046354|||http://purl.uniprot.org/annotation/VAR_046355
http://togogenome.org/gene/9606:TDRD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7E2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with dimethylarginine-containing protein motifs and reduces association with mRNA stress granules.|||Basic and acidic residues|||Disordered|||EBM motif; may mediate interaction with the EJC|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Loss of interaction with the EJC.|||Phosphoserine|||Polar residues|||Tudor|||Tudor domain-containing protein 3|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183163|||http://purl.uniprot.org/annotation/VSP_037052|||http://purl.uniprot.org/annotation/VSP_037053
http://togogenome.org/gene/9606:SYDE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein SYDE2|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312160|||http://purl.uniprot.org/annotation/VAR_037419|||http://purl.uniprot.org/annotation/VAR_037420|||http://purl.uniprot.org/annotation/VAR_037421|||http://purl.uniprot.org/annotation/VSP_029718|||http://purl.uniprot.org/annotation/VSP_029719
http://togogenome.org/gene/9606:TOP3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13472                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA topoisomerase 3-alpha|||Decreased DNA decatenation.|||Disordered|||GRF-type 1|||GRF-type 2|||In MGRISCE2.|||In PEOB5.|||In PEOB5; results in decreased DNA decatenation.|||In isoform 3.|||In isoform Short.|||O-(5'-phospho-DNA)-tyrosine intermediate|||Polar residues|||Toprim                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145190|||http://purl.uniprot.org/annotation/VAR_007529|||http://purl.uniprot.org/annotation/VAR_052588|||http://purl.uniprot.org/annotation/VAR_052589|||http://purl.uniprot.org/annotation/VAR_052590|||http://purl.uniprot.org/annotation/VAR_081105|||http://purl.uniprot.org/annotation/VAR_081106|||http://purl.uniprot.org/annotation/VAR_081107|||http://purl.uniprot.org/annotation/VSP_006524|||http://purl.uniprot.org/annotation/VSP_054189
http://togogenome.org/gene/9606:SCYL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RQQ9|||http://purl.uniprot.org/uniprot/Q6P3W7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HEAT|||In AMC4.|||In a lung adenocarcinoma sample; somatic mutation.|||Necessary for interaction with AP2 complex and clathrin, interaction with clathrin is necessary for its targeting to the TGN and endosomal membranes|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||SCY1-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252446|||http://purl.uniprot.org/annotation/VAR_041368|||http://purl.uniprot.org/annotation/VAR_041369|||http://purl.uniprot.org/annotation/VAR_041370|||http://purl.uniprot.org/annotation/VAR_083876
http://togogenome.org/gene/9606:CARMIL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TRE2|||http://purl.uniprot.org/uniprot/Q5VZK9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||CARMIL C-terminal|||CARMIL pleckstrin homology|||Disordered|||F-actin-uncapping protein LRRC16A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits capping activity of CAPZA2|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-acetylmethionine|||Necessary for localization at the cell membrane|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325815|||http://purl.uniprot.org/annotation/VAR_039923|||http://purl.uniprot.org/annotation/VAR_039924|||http://purl.uniprot.org/annotation/VAR_039925|||http://purl.uniprot.org/annotation/VAR_039926|||http://purl.uniprot.org/annotation/VSP_032415|||http://purl.uniprot.org/annotation/VSP_032416|||http://purl.uniprot.org/annotation/VSP_032417|||http://purl.uniprot.org/annotation/VSP_032418|||http://purl.uniprot.org/annotation/VSP_032419|||http://purl.uniprot.org/annotation/VSP_032420
http://togogenome.org/gene/9606:MAPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTM0|||http://purl.uniprot.org/uniprot/P10636                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein.|||70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.|||8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein.|||Basic and acidic residues|||Deamidated asparagine; in tau and PHF-tau; partial|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); in PHF-tau|||In FTD and CBD; reduction in the ability to promote microtubule assembly.|||In FTD.|||In FTD/Alzheimer disease; accelerates aggregation of tau into filaments; reduces tau phosphorylation in cells compared to both the wild-type and other mutant forms.|||In FTD; increased aggregation propensity and altered binding affinity towards microtubules and F-actin.|||In FTD; less able to promote microtubule assembly than wild-type tau.|||In FTD; minimal parkinsonism; very early age of onset.|||In FTD; most common mutation; reduction in the ability to promote microtubule assembly; accelerates aggregation of tau into filaments.|||In FTD; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level.|||In FTD; reduces the ability of tau to promote microtubule assembly and promotes fibril formation in vitro.|||In FTD; ultrastructural and biochemical characteristics indistinguishable from Alzheimer disease; accelerates aggregation of tau into filaments.|||In FTD; with parkinsonism.|||In PIDB; 90% reduction in the rate of microtubule assembly.|||In PIDB; in vitro the mutation reduces the ability of tau to promote microtubule assembly by 25 to 30%.|||In PIDB; markedly reduced ability of tau to promote microtubule assembly.|||In PIDB; reduces the ability to promote microtubule assembly by 70%.|||In PSNP1.|||In PSNP1/atypical PSNP1; heterozygosity may be a risk factor for both a PSNP1-like syndrome and Parkinson disease; reduced the ability of tau to promote microtubule assembly without having a significant effect on tau filament formation; effects at both the RNA and the protein level.|||In PSNP1; delays assembly initiation and lowers the mass of microtubules formed; but the assembly rate is increased compared to normal tau.|||In fatal respiratory hypoventilation; unusual apparent autosomal recessive inheritance; reduced binding to microtubules as well as increased fibrillization and aggregation.|||In isoform Tau-A, isoform Tau-B, isoform Tau-C and isoform Fetal-tau.|||In isoform Tau-A, isoform Tau-B, isoform Tau-C, isoform Tau-D, isoform Tau-E, isoform Tau-F and isoform Fetal-tau.|||In isoform Tau-A, isoform Tau-B, isoform Tau-D, isoform Tau-E and isoform Fetal-tau.|||In isoform Tau-A, isoform Tau-D and isoform Fetal-tau.|||In isoform Tau-A.|||In isoform Tau-G.|||Microtubule-associated protein tau|||Microtubule-binding domain|||N-acetylalanine|||N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||No association with plasma membrane.|||No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein.|||Not glycated|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CK1 and PDPK1|||Phosphoserine; by CK1, PDPK1 and TTBK1|||Phosphoserine; by CaMK2 and TTBK1|||Phosphoserine; by MARK1, MARK2, MARK3, MARK4, BRSK1, BRSK2 and PHK|||Phosphoserine; by PDPK1|||Phosphoserine; by PDPK1 and TTBK1|||Phosphoserine; by PHK|||Phosphoserine; by PKA|||Phosphoserine; by SGK1|||Phosphoserine; in PHF-tau|||Phosphothreonine|||Phosphothreonine; by BRSK1, BRSK2, DYRK2 and PDPK1|||Phosphothreonine; by CK1 and PDPK1|||Phosphothreonine; by GSK3-beta and PDPK1|||Phosphothreonine; by PDPK1|||Phosphothreonine; by TTBK1|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Phosphotyrosine; by TTBK1|||Polar residues|||Removed|||Risk factor for PSNP1.|||Tau/MAP 1|||Tau/MAP 2|||Tau/MAP 3|||Tau/MAP 4 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072739|||http://purl.uniprot.org/annotation/VAR_010340|||http://purl.uniprot.org/annotation/VAR_010341|||http://purl.uniprot.org/annotation/VAR_010342|||http://purl.uniprot.org/annotation/VAR_010343|||http://purl.uniprot.org/annotation/VAR_010344|||http://purl.uniprot.org/annotation/VAR_010345|||http://purl.uniprot.org/annotation/VAR_010346|||http://purl.uniprot.org/annotation/VAR_010347|||http://purl.uniprot.org/annotation/VAR_010348|||http://purl.uniprot.org/annotation/VAR_010349|||http://purl.uniprot.org/annotation/VAR_010350|||http://purl.uniprot.org/annotation/VAR_010351|||http://purl.uniprot.org/annotation/VAR_010352|||http://purl.uniprot.org/annotation/VAR_010353|||http://purl.uniprot.org/annotation/VAR_019660|||http://purl.uniprot.org/annotation/VAR_019661|||http://purl.uniprot.org/annotation/VAR_019662|||http://purl.uniprot.org/annotation/VAR_019663|||http://purl.uniprot.org/annotation/VAR_019664|||http://purl.uniprot.org/annotation/VAR_019665|||http://purl.uniprot.org/annotation/VAR_019666|||http://purl.uniprot.org/annotation/VAR_019667|||http://purl.uniprot.org/annotation/VAR_019668|||http://purl.uniprot.org/annotation/VAR_037439|||http://purl.uniprot.org/annotation/VAR_037440|||http://purl.uniprot.org/annotation/VAR_056121|||http://purl.uniprot.org/annotation/VAR_064622|||http://purl.uniprot.org/annotation/VAR_064623|||http://purl.uniprot.org/annotation/VAR_064624|||http://purl.uniprot.org/annotation/VAR_084361|||http://purl.uniprot.org/annotation/VSP_003175|||http://purl.uniprot.org/annotation/VSP_003176|||http://purl.uniprot.org/annotation/VSP_003177|||http://purl.uniprot.org/annotation/VSP_003178|||http://purl.uniprot.org/annotation/VSP_003179|||http://purl.uniprot.org/annotation/VSP_003180|||http://purl.uniprot.org/annotation/VSP_003181|||http://purl.uniprot.org/annotation/VSP_026780
http://togogenome.org/gene/9606:SDR9C7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEX9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In ARCI13; decreased protein abundance.|||Phosphoserine|||Proton acceptor|||Short-chain dehydrogenase/reductase family 9C member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316885|||http://purl.uniprot.org/annotation/VAR_079292|||http://purl.uniprot.org/annotation/VAR_079293
http://togogenome.org/gene/9606:SCAMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14828                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with TSG101.|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Secretory carrier-associated membrane protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191257|||http://purl.uniprot.org/annotation/VAR_011885|||http://purl.uniprot.org/annotation/VAR_011886|||http://purl.uniprot.org/annotation/VAR_011887|||http://purl.uniprot.org/annotation/VAR_011888|||http://purl.uniprot.org/annotation/VSP_004381
http://togogenome.org/gene/9606:COMMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X83                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077386|||http://purl.uniprot.org/annotation/VAR_028010|||http://purl.uniprot.org/annotation/VAR_028011|||http://purl.uniprot.org/annotation/VSP_055533
http://togogenome.org/gene/9606:CAMSAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTI4|||http://purl.uniprot.org/uniprot/Q08AD1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CKK|||Calmodulin-regulated spectrin-associated protein 2|||Calponin-homology (CH)|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||MBD region|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316832|||http://purl.uniprot.org/annotation/VAR_038399|||http://purl.uniprot.org/annotation/VAR_038400|||http://purl.uniprot.org/annotation/VAR_038401|||http://purl.uniprot.org/annotation/VAR_057796|||http://purl.uniprot.org/annotation/VAR_057797|||http://purl.uniprot.org/annotation/VSP_030805|||http://purl.uniprot.org/annotation/VSP_030806
http://togogenome.org/gene/9606:SEC24B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTM6|||http://purl.uniprot.org/uniprot/O95487                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Decreased ability to package the SNARESEC22B cargo into COPII vesicles. Has no effect on other cargos packaging.|||Disordered|||Gelsolin-like|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein transport protein Sec24B|||Removed|||Sec23/Sec24 beta-sandwich|||Sec23/Sec24 helical|||Sec23/Sec24 trunk|||Zinc finger Sec23/Sec24-type|||Zinc finger-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205155|||http://purl.uniprot.org/annotation/VAR_047934|||http://purl.uniprot.org/annotation/VSP_035987|||http://purl.uniprot.org/annotation/VSP_054432|||http://purl.uniprot.org/annotation/VSP_054433
http://togogenome.org/gene/9606:PARP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB27|||http://purl.uniprot.org/uniprot/E9PFI7|||http://purl.uniprot.org/uniprot/Q8N3A8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylcysteine|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||PARP catalytic|||Polar residues|||Protein mono-ADP-ribosyltransferase PARP8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252433|||http://purl.uniprot.org/annotation/VAR_035853|||http://purl.uniprot.org/annotation/VSP_020970
http://togogenome.org/gene/9606:CCDC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LX7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 17|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302852|||http://purl.uniprot.org/annotation/VAR_034976|||http://purl.uniprot.org/annotation/VAR_034977|||http://purl.uniprot.org/annotation/VAR_059599|||http://purl.uniprot.org/annotation/VAR_063516|||http://purl.uniprot.org/annotation/VSP_039651|||http://purl.uniprot.org/annotation/VSP_039652|||http://purl.uniprot.org/annotation/VSP_039653
http://togogenome.org/gene/9606:DMRTC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX56|||http://purl.uniprot.org/uniprot/Q8IXT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DM|||Disordered|||Doublesex- and mab-3-related transcription factor C2|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244106|||http://purl.uniprot.org/annotation/VSP_019525|||http://purl.uniprot.org/annotation/VSP_019526
http://togogenome.org/gene/9606:IRF2BPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1B7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDAMSS.|||In NEDAMSS; loss of function.|||In NEDAMSS; unknown pathological significance.|||In NEDAMSS; unknown pathological significance; no effect on function.|||Loss of transcription activity.|||Phosphoserine|||Polar residues|||Pro residues|||Probable E3 ubiquitin-protein ligase IRF2BPL|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056411|||http://purl.uniprot.org/annotation/VAR_081415|||http://purl.uniprot.org/annotation/VAR_081416|||http://purl.uniprot.org/annotation/VAR_081417|||http://purl.uniprot.org/annotation/VAR_081418|||http://purl.uniprot.org/annotation/VAR_081419|||http://purl.uniprot.org/annotation/VAR_081420|||http://purl.uniprot.org/annotation/VAR_081421
http://togogenome.org/gene/9606:ATP6V1G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95670|||http://purl.uniprot.org/uniprot/Q6NVJ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||V-type proton ATPase subunit G 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192900|||http://purl.uniprot.org/annotation/VSP_045909|||http://purl.uniprot.org/annotation/VSP_047411
http://togogenome.org/gene/9606:SMIM14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QK8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In N-gly,C; does not create a N-glycosylation site.|||In N-gly,N; creates a N-glycosylation site.|||Lumenal|||Small integral membrane protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268816
http://togogenome.org/gene/9606:PPARA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07869                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes heterodimerization with RXRA, DNA binding and transactivation activity.|||Abolishes heterodimerization with RXRA. No DNA binding.|||Essential for heterodimerization with RXRA|||In isoform 2.|||NR C4-type|||NR LBD|||No effect on heterodimerization with RXRA nor on DNA binding and transactivation activity.|||No effect on heterodimerization with RXRA nor on DNA binding.|||Nuclear receptor|||Peroxisome proliferator-activated receptor alpha|||Prevents DNA binding but no effect on heterodimerization with RXRA.|||Reduced heterodimerization with RXRA. Reduced DNA binding.|||Required for heterodimerization with RXRA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053481|||http://purl.uniprot.org/annotation/VAR_016110|||http://purl.uniprot.org/annotation/VAR_016111|||http://purl.uniprot.org/annotation/VAR_016112|||http://purl.uniprot.org/annotation/VAR_016113|||http://purl.uniprot.org/annotation/VAR_016114|||http://purl.uniprot.org/annotation/VAR_016115|||http://purl.uniprot.org/annotation/VAR_050578|||http://purl.uniprot.org/annotation/VSP_047571|||http://purl.uniprot.org/annotation/VSP_047572
http://togogenome.org/gene/9606:ADM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JUS6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Putative adrenomedullin-5-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392551
http://togogenome.org/gene/9606:HTR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34969                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 7|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform A.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068979|||http://purl.uniprot.org/annotation/VAR_012995|||http://purl.uniprot.org/annotation/VAR_012996|||http://purl.uniprot.org/annotation/VAR_049365|||http://purl.uniprot.org/annotation/VSP_001856|||http://purl.uniprot.org/annotation/VSP_001857
http://togogenome.org/gene/9606:DROSHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNase activity.|||Abolishes RNase activity; when associated with A-923.|||Abolishes RNase activity; when associated with A-927.|||Abolishes interaction with DGCR8.|||Acidic residues|||Basic and acidic residues|||DRBM|||Disordered|||Impairs RNase activity.|||Impairs pri-miRNA processing activity. Abolishes cleavage of the 3' strand. Abolishes enzyme activity; when associated with Q-1222.|||Impairs pri-miRNA processing activity. Abolishes cleavage of the 5' strand. Abolishes enzyme activity; when associated with Q-1045.|||Impairs protein folding and stability.|||Impairs protein folding and stability; when associated with A-536.|||Impairs protein folding and stability; when associated with A-538.|||Important for activity|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Loss of one DGCR8 interaction site; no effect on the second DGCR8 interaction site.|||Necessary for interaction with DGCR8 and pri-miRNA processing activity|||No effect on pri-miRNA processing activity.|||Phosphoserine|||Polar residues|||Pro residues|||RNase III 1|||RNase III 2|||Ribonuclease 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000180468|||http://purl.uniprot.org/annotation/VAR_051866|||http://purl.uniprot.org/annotation/VAR_061778|||http://purl.uniprot.org/annotation/VSP_005777|||http://purl.uniprot.org/annotation/VSP_012450|||http://purl.uniprot.org/annotation/VSP_012451|||http://purl.uniprot.org/annotation/VSP_012452|||http://purl.uniprot.org/annotation/VSP_012453
http://togogenome.org/gene/9606:ZMIZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EWM3|||http://purl.uniprot.org/uniprot/Q8NF64                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with AR|||Omega-N-methylarginine|||Polar residues|||Pro residues|||SP-RING-type|||Zinc finger MIZ domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218989|||http://purl.uniprot.org/annotation/VAR_050536|||http://purl.uniprot.org/annotation/VSP_012190|||http://purl.uniprot.org/annotation/VSP_024918
http://togogenome.org/gene/9606:GALNT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7M9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Polypeptide N-acetylgalactosaminyltransferase 5|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059110|||http://purl.uniprot.org/annotation/VAR_019578|||http://purl.uniprot.org/annotation/VAR_019579|||http://purl.uniprot.org/annotation/VAR_035991|||http://purl.uniprot.org/annotation/VAR_035992
http://togogenome.org/gene/9606:FABP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7DVW4|||http://purl.uniprot.org/uniprot/P15090                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Cytosolic fatty-acid binding proteins|||Fatty acid-binding protein, adipocyte|||In a breast cancer sample; somatic mutation.|||N-acetylcysteine|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine; by Tyr-kinases|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067366|||http://purl.uniprot.org/annotation/VAR_036320
http://togogenome.org/gene/9606:SCRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ03                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; atypical|||Disordered|||SNAG domain|||Transcriptional repressor scratch 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047038
http://togogenome.org/gene/9606:MSANTD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IT52                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative uncharacterized protein MSANTD5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000451609
http://togogenome.org/gene/9606:UBE2D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2X8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2 D4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270202
http://togogenome.org/gene/9606:TOMM40L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969M1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Mitochondrial import receptor subunit TOM40B|||Required for mitochondrial targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051536|||http://purl.uniprot.org/annotation/VAR_035815|||http://purl.uniprot.org/annotation/VSP_054885
http://togogenome.org/gene/9606:OR5K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVB4|||http://purl.uniprot.org/uniprot/Q8NHB8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150601
http://togogenome.org/gene/9606:EXOSC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQT4                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Exosome complex component RRP46|||In CABAC.|||In CABAC; decreased interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system.|||In CABAC; strongly decreased interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system.|||In CABAC; unknown pathological significance; no detectable effect on interaction with EXOSC3, EXOSC9 and EXOSC10, when assayed in a heterologous system.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139975|||http://purl.uniprot.org/annotation/VAR_030788|||http://purl.uniprot.org/annotation/VAR_051868|||http://purl.uniprot.org/annotation/VAR_086374|||http://purl.uniprot.org/annotation/VAR_086375|||http://purl.uniprot.org/annotation/VAR_086376|||http://purl.uniprot.org/annotation/VAR_086377
http://togogenome.org/gene/9606:C19orf18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEA5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Uncharacterized protein C19orf18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019567|||http://purl.uniprot.org/annotation/VAR_050909
http://togogenome.org/gene/9606:CD300C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08708                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMRF35-like molecule 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014681|||http://purl.uniprot.org/annotation/VAR_039133
http://togogenome.org/gene/9606:TFF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07654                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interchain|||P-type|||Trefoil factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023465
http://togogenome.org/gene/9606:YJU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW85                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Polar residues|||Splicing factor YJU2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234018
http://togogenome.org/gene/9606:NR5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8R8|||http://purl.uniprot.org/uniprot/Q13285                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Important for dimerization|||In AINR.|||In POF7.|||In POF7; without adrenal failure; partial loss of activity.|||In SPGF8 and POF7; activity levels similar to wild-type.|||In SPGF8 and POF7; loss of activity.|||In SPGF8; impairs transactivational activity.|||In SRXY3 and SRXX4; decreased transactivator activity; loss of DNA binding, at least to some known consensus target sequences; no effect on nuclear location.|||In SRXY3, SRXX4 and AINR; decreased transactivator activity; no effect on nuclear location.|||In SRXY3; loss of DNA-binding; significantly decreased transactivator activity.|||In SRXY3; with adrenal failure.|||In SRXY3; without adrenal failure.|||In SRXY3; without adrenal failure; markedly impaired transcriptional activity.|||Loss of sumoylation.|||Loss of sumoylation; when associated with R-194.|||Loss of transactivation; when associated with A-440.|||Loss of transactivation; when associated with F-436.|||N6-acetyllysine|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine; by CDK7|||Pro residues|||Reduced transactivation. Strongly reduced transactivation; when associated with E-341.|||Reduced transactivation. Strongly reduced transactivation; when associated with F-344.|||Steroidogenic factor 1|||Strongly reduced transactivation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053729|||http://purl.uniprot.org/annotation/VAR_004737|||http://purl.uniprot.org/annotation/VAR_016982|||http://purl.uniprot.org/annotation/VAR_016983|||http://purl.uniprot.org/annotation/VAR_039106|||http://purl.uniprot.org/annotation/VAR_039107|||http://purl.uniprot.org/annotation/VAR_039108|||http://purl.uniprot.org/annotation/VAR_062967|||http://purl.uniprot.org/annotation/VAR_062968|||http://purl.uniprot.org/annotation/VAR_062969|||http://purl.uniprot.org/annotation/VAR_062970|||http://purl.uniprot.org/annotation/VAR_063255|||http://purl.uniprot.org/annotation/VAR_063256|||http://purl.uniprot.org/annotation/VAR_063257|||http://purl.uniprot.org/annotation/VAR_063258|||http://purl.uniprot.org/annotation/VAR_065866|||http://purl.uniprot.org/annotation/VAR_065867|||http://purl.uniprot.org/annotation/VAR_065868|||http://purl.uniprot.org/annotation/VAR_065869|||http://purl.uniprot.org/annotation/VAR_078136|||http://purl.uniprot.org/annotation/VAR_078137|||http://purl.uniprot.org/annotation/VAR_079571|||http://purl.uniprot.org/annotation/VAR_079572
http://togogenome.org/gene/9606:UBE2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62837                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Catalytically inactive. Loss of ability to promote FBXW2-mediated GCM1 ubiquitination. Inhibition of TNF-alpha-induced degradation of NFKBIA.|||Glycyl thioester intermediate|||In isoform 2.|||Strongly reduced interaction with CNTO4.|||UBC core|||Ubiquitin-conjugating enzyme E2 D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082462|||http://purl.uniprot.org/annotation/VSP_045180
http://togogenome.org/gene/9606:CRABP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29373                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Motif|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Cellular retinoic acid-binding protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Loss of ligand-induced nuclear import; when associated with A-21 and A-30.|||Loss of ligand-induced nuclear import; when associated with A-21 and A-31.|||Loss of ligand-induced nuclear import; when associated with A-30 and A-31.|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067415
http://togogenome.org/gene/9606:MAGEL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||MAGE|||MAGE-like protein 2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156738
http://togogenome.org/gene/9606:CDR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01850                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cerebellar degeneration-related protein 2|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089456
http://togogenome.org/gene/9606:PCP4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||IQ|||Phosphothreonine|||Polar residues|||Purkinje cell protein 4-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331432
http://togogenome.org/gene/9606:COPS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5N1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  COP9 signalosome complex subunit 6|||Interaction with Vpr|||MPN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194860
http://togogenome.org/gene/9606:ANKFY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPZ0|||http://purl.uniprot.org/uniprot/Q9P2R3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||BTB|||Decreases interaction with EHD1.|||Disrupts interaction with EHD1.|||FYVE-type|||In isoform 2.|||In isoform 4.|||Interaction with RHOD and RAB5A|||N-acetylalanine|||NPF|||Phosphoserine|||Rabankyrin-5|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066890|||http://purl.uniprot.org/annotation/VSP_035607|||http://purl.uniprot.org/annotation/VSP_041447
http://togogenome.org/gene/9606:INSIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2M9|||http://purl.uniprot.org/uniprot/F5H6P3|||http://purl.uniprot.org/uniprot/O15503                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished phosphorylation by PCK1, does not affect oxysterol-binding, does not affect the interaction with SCAP.|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Insulin-induced gene 1 protein|||KxHxx|||Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR.|||Loss of ubiquitination and degradation.|||Lumenal|||Phosphomimetic mutant, reduced binding to oxysterol.|||Phosphoserine; by PCK1|||Required for the recognition of 25-hydroxycholesterol                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191675|||http://purl.uniprot.org/annotation/VAR_027683|||http://purl.uniprot.org/annotation/VSP_045084|||http://purl.uniprot.org/annotation/VSP_045085
http://togogenome.org/gene/9606:MCOLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZU1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes association with membranes.|||Abolishes formation and extrusion of tubulo-vesicular structures and decreases lysosomal exocytosis when overexpressed.|||Abolishes interaction with PDCD6 and decreases formation of aberrant endosomes upon overexpression.|||Abolishes interaction with PDCD6.|||Abolishes localization to lysosomes and leads to expression at the cell membrane; when associated with A-15.|||Abolishes localization to lysosomes and leads to expression at the cell membrane; when associated with A-577.|||Cytoplasmic|||Dileucine internalization motif; mediates AP2 complex-dependent internalization|||Dileucine motif; mediates targeting to lysosomes|||Disordered|||Disrupts tetrameric assembly and abolishes lysosomal localization; when associated with K-144.|||Disrupts tetrameric assembly and abolishes lysosomal localization; when associated with S-146.|||Does not prevent proteolytic cleavage but changes cleavage pattern.|||Extracellular|||Extracellular/lumenal pore loop|||Fails to rescue defect of lactosylceramide traffic through the late endocytic pathway in ML4 patient cells.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In ML4.|||In ML4; affects channel activity; abolishes Fe(2+) permeability.|||In ML4; decreases formation and extrusion of tubulo-vesicular structures when overexpressed; disrupts tetrameric assembly; abolishes lysosomal localization.|||In ML4; does not affect channel activity; affects channel inhibition by low pH; impairs Fe(2+) permeability.|||In ML4; fails to localize to late endosomes; abolishes Fe(2+) permeability; disrupts tetrameric assembly; abolishes lysosomal localization.|||In ML4; impairs Fe(2+) permeability.|||In ML4; mild psychomotor involvement; does not affect channel activity; affects channel inhibition by low pH; still localizes to late endosomes.|||In ML4; still localizes to late endosomes; fails to rescue defect of lactosylceramide traffic through the late endocytic pathway in ML4 patient cells; minor effect on formation and extrusion of tubulo-vesicular structures when overexpressed.|||In a breast cancer sample; somatic mutation.|||Interaction with phosphoinositides|||Mediates localization to the plasma membrane and strong inwardly rectifying current.|||Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-111 and Q-114.|||Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-111 and Q-115.|||Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-114 and Q-115.|||Modulates ion conduction; when associoated with C-110 and C-112.|||Modulates ion conduction; when associoated with C-110 and C-113.|||Modulates ion conduction; when associoated with C-112 and C-113.|||Mucolipin-1|||N-linked (GlcNAc...) asparagine|||No effect on localization to lysosomes.|||Phosphoserine|||Phosphoserine; by PAK|||Pore-forming|||Reduces PtdIns(3,5)P2 sensitivity.|||Reduces PtdIns(4,5)P2 sensitivity.|||Required for palmitoylation and association with membranes|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215362|||http://purl.uniprot.org/annotation/VAR_019369|||http://purl.uniprot.org/annotation/VAR_019370|||http://purl.uniprot.org/annotation/VAR_019371|||http://purl.uniprot.org/annotation/VAR_019372|||http://purl.uniprot.org/annotation/VAR_019373|||http://purl.uniprot.org/annotation/VAR_019374|||http://purl.uniprot.org/annotation/VAR_019375|||http://purl.uniprot.org/annotation/VAR_036453|||http://purl.uniprot.org/annotation/VAR_038380
http://togogenome.org/gene/9606:IL18R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13478                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreases the affinity for IL18 suggesting that the N-linked glycosylation contributes to ligand recognition.|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Interleukin-18 receptor 1|||N-linked (GlcNAc...) asparagine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015448|||http://purl.uniprot.org/annotation/VAR_014955|||http://purl.uniprot.org/annotation/VAR_053379|||http://purl.uniprot.org/annotation/VAR_053380|||http://purl.uniprot.org/annotation/VAR_053381|||http://purl.uniprot.org/annotation/VAR_053382
http://togogenome.org/gene/9606:MICAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDZ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ARHGAP26 ANDARHGAP10.|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Important for interaction with ARHGAP26 AND ARHGAP10|||Important for interaction with RAB8A|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased association with Rab8- Rab10- and GRAPHs-positive endosomal tubules. Decreased WDR44-positive endosomal tubules formation. Loss of E-cadherin and MMP14 export and decreased CFTR export.|||LIM zinc-binding|||Monooxygenase domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Requires 2 nucleotide substitutions.|||[F-actin]-monooxygenase MICAL1|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075842|||http://purl.uniprot.org/annotation/VAR_017903|||http://purl.uniprot.org/annotation/VAR_036191|||http://purl.uniprot.org/annotation/VAR_050153|||http://purl.uniprot.org/annotation/VAR_050154|||http://purl.uniprot.org/annotation/VAR_061355|||http://purl.uniprot.org/annotation/VAR_067063|||http://purl.uniprot.org/annotation/VAR_067064|||http://purl.uniprot.org/annotation/VAR_067065|||http://purl.uniprot.org/annotation/VAR_067066|||http://purl.uniprot.org/annotation/VAR_067067|||http://purl.uniprot.org/annotation/VAR_067068|||http://purl.uniprot.org/annotation/VSP_009637|||http://purl.uniprot.org/annotation/VSP_009638|||http://purl.uniprot.org/annotation/VSP_009639|||http://purl.uniprot.org/annotation/VSP_042590
http://togogenome.org/gene/9606:GTF2E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29083                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C4-type|||Disordered|||General transcription factor IIE subunit 1|||HTH TFE/IIEalpha-type|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211222|||http://purl.uniprot.org/annotation/VAR_020321
http://togogenome.org/gene/9606:SPRTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H040                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished ability to mediate autocleavage in presence of ssDNA.|||Abolished ability to mediate autocleavage. Does not affect DNA-binding.|||Abolished ability to mediate autocleavage. Strongly reduced DNA-binding.|||Abolished acetylation, leading to impaired localization to chromatin.|||Abolished interaction with PCNA.|||Abolished metalloprotease activity and ability to cleave covalent DNA-protein cross-links (DPCs).|||Abolished metalloprotease activity and ability to cleave covalent DNA-protein cross-links (DPCs). Abolished ability to cleave CHEK1 during physiological DNA replication.|||Abolished metalloprotease activity and ability to mediate autocleavage. Slightly impaired ability to cleave covalent DNA-protein cross-links (DPCs).|||Abolished metalloprotease activity, ability to cleave covalent DNA-protein cross-links (DPCs) and to mediate autocleavage.|||Abolished phosphorylation by CHEK1; when associated with A-373 and A-374.|||Abolished phosphorylation by CHEK1; when associated with A-373 and A-383.|||Abolished phosphorylation by CHEK1; when associated with A-374 and A-383.|||Abolishes binding to VCP/p97; when associated with A-253.|||Abolishes binding to VCP/p97; when associated with A-260.|||Abolishes binding to ubiquitin.|||Cleavage; by autolysis|||DNA-dependent metalloprotease SPRTN|||Decreased interaction with PCNA.|||Disordered|||Does not abolish monoubiquitination; when associated with R-341, R-376 and R-414.|||Does not abolish monoubiquitination; when associated with R-341, R-376 and R-435.|||Does not abolish monoubiquitination; when associated with R-341, R-414 and R-435.|||Does not abolish monoubiquitination; when associated with R-376, R-414 and R-435.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In RJALS; impaired metalloprotease activity and ability to cleave covalent DNA-protein cross-links (DPCs); cells are completely unable to restore DNA replication fork progression.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increased ability to mediate autocleavage.|||Mimics acetylation, promoting cleavage of covalent DNA-protein cross-links (DPCs).|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||PIP-box|||Phosphoserine|||Phosphoserine; by CHEK1|||Polar residues|||Promotes relocalization to the cytoplasm.|||SHP-box|||SprT-like|||Strongly reduced ability to mediate autocleavage. Strongly reduced DNA-binding.|||UBZ4-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312748|||http://purl.uniprot.org/annotation/VAR_037556|||http://purl.uniprot.org/annotation/VAR_072708|||http://purl.uniprot.org/annotation/VSP_029891|||http://purl.uniprot.org/annotation/VSP_029892|||http://purl.uniprot.org/annotation/VSP_046925
http://togogenome.org/gene/9606:ANKRD63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JTQ0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat domain-containing protein 63|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000411002
http://togogenome.org/gene/9606:RAB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61026                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of phosphorylation. No effect on GDI1 and GDI2 binding. Increases localization to the cytosol.|||N6-acetyllysine|||Phosphomimetic mutant. Loss of GDI1 and GDI2 binding. Increases localization to the Golgi complex.|||Phosphothreonine; by LRRK2|||Probable constitutively active mutant unable to hydrolyze GTP; accumulates at the base of the primary cilium and alters the basolateral recycling pathway in epithelial cells. No effect on endoplasmic reticulum recruitment to the Legionella-containing vacuole.|||Probable dominant negative mutant locked in the inactive GDP-bound form; alters the basolateral recycling pathway in epithelial cells and endoplasmic reticulum membrane morphology. Reduces endoplasmic reticulum recruitment to the Legionella-containing vacuole.|||Ras-related protein Rab-10|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121146
http://togogenome.org/gene/9606:ABHD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L211                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Protein ABHD13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281076
http://togogenome.org/gene/9606:DYRK1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y463                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes kinase activity.|||Abolishes kinase activity; when associated with F-271.|||Abolishes kinase activity; when associated with F-273.|||Bipartite nuclear localization signal|||Disordered|||Dual specificity tyrosine-phosphorylation-regulated kinase 1B|||In AOMS3; accumulation of intracellular lipid is significantly greater than with wild-type protein; cells expressing the variant are able to transform into mature adipocytes without requiring adipogenic medium; expression levels of CEBPA, PPARG forms 1 and 2 and PPARGC1A are higher and those of GLI1 and CDKN1B are lower in cells transfected with the mutant protein compared to wild-type; WNT1 signaling activity is lower in mutant cells compared to wild-type.|||In AOMS3; expression of glucose-6-phosphatase is significantly higher than wild-type.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with RANBP9|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085934|||http://purl.uniprot.org/annotation/VAR_040454|||http://purl.uniprot.org/annotation/VAR_040455|||http://purl.uniprot.org/annotation/VAR_040456|||http://purl.uniprot.org/annotation/VAR_040457|||http://purl.uniprot.org/annotation/VAR_071773|||http://purl.uniprot.org/annotation/VAR_071774|||http://purl.uniprot.org/annotation/VSP_004925|||http://purl.uniprot.org/annotation/VSP_004926
http://togogenome.org/gene/9606:BMI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35226                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-174.|||Disordered|||Increases stimulation of RNF2 ubiquitin ligase activity; when associated with E-77.|||Increases stimulation of RNF2 ubiquitin ligase activity; when associated with N-73.|||Interaction with E4F1|||Interaction with PHC2|||Mildly decreases histone H2A ubiquitination. Strongly decreases histone H2A ubiquitination; when associated with A-62.|||Nuclear localization signal|||Polar residues|||Polycomb complex protein BMI-1|||RING-type|||Strongly decreases affinity for PHC2.|||Strongly decreases affinity for PHC2. Abolishes interaction with PHC2; when associated with E-165.|||Strongly decreases histone H2A ubiquitination; when associated with A-64.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055987|||http://purl.uniprot.org/annotation/VAR_052087
http://togogenome.org/gene/9606:FRA10AC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70Z53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In NEDGFC.|||In NEDGFC; unknown pathological significance; decreased protein abundance; no effect on protein localization.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Protein FRA10AC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087148|||http://purl.uniprot.org/annotation/VAR_023237|||http://purl.uniprot.org/annotation/VAR_023238|||http://purl.uniprot.org/annotation/VAR_056872|||http://purl.uniprot.org/annotation/VAR_087878|||http://purl.uniprot.org/annotation/VAR_087879|||http://purl.uniprot.org/annotation/VAR_087880|||http://purl.uniprot.org/annotation/VSP_015123|||http://purl.uniprot.org/annotation/VSP_015124|||http://purl.uniprot.org/annotation/VSP_015125|||http://purl.uniprot.org/annotation/VSP_015126|||http://purl.uniprot.org/annotation/VSP_015127|||http://purl.uniprot.org/annotation/VSP_015128
http://togogenome.org/gene/9606:GSX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4S2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GS homeobox 1|||Homeobox|||SNAG domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048894
http://togogenome.org/gene/9606:PDE6D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZK5|||http://purl.uniprot.org/uniprot/O43924|||http://purl.uniprot.org/uniprot/Q6IB24                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  GMP phosphodiesterase delta subunit|||Required for association with membranes|||Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221208
http://togogenome.org/gene/9606:IGSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75054                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||EWI motif|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Immunoglobulin superfamily member 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320134|||http://purl.uniprot.org/annotation/VAR_039134|||http://purl.uniprot.org/annotation/VAR_039135|||http://purl.uniprot.org/annotation/VAR_039136|||http://purl.uniprot.org/annotation/VSP_031609
http://togogenome.org/gene/9606:CCDC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYE1|||http://purl.uniprot.org/uniprot/Q96LI1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 13|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089409|||http://purl.uniprot.org/annotation/VAR_033664|||http://purl.uniprot.org/annotation/VAR_055093|||http://purl.uniprot.org/annotation/VAR_055094
http://togogenome.org/gene/9606:PPME1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK39|||http://purl.uniprot.org/uniprot/Q9Y570                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  AB hydrolase-1|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Protein phosphatase methylesterase 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090390|||http://purl.uniprot.org/annotation/VSP_010335|||http://purl.uniprot.org/annotation/VSP_010336|||http://purl.uniprot.org/annotation/VSP_010337|||http://purl.uniprot.org/annotation/VSP_054818
http://togogenome.org/gene/9606:POLG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KS15|||http://purl.uniprot.org/uniprot/Q9UHN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Anticodon-binding|||Basic and acidic residues|||DNA polymerase subunit gamma-2, mitochondrial|||Disordered|||In MTDPS16; decreased function in mitochondrial DNA replication; decreased protein stability; no effect on DNA binding.|||In MTDPS16B; decreased DNA polymerase processivity factor activity; results in decreased stability; affects the secondary structure as shown by circular dichroism spectroscopy.|||In PEOA4; affects stimulation of the catalytic subunit.|||Mitochondrion|||No functional deficit.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007314|||http://purl.uniprot.org/annotation/VAR_029364|||http://purl.uniprot.org/annotation/VAR_032028|||http://purl.uniprot.org/annotation/VAR_032029|||http://purl.uniprot.org/annotation/VAR_078773|||http://purl.uniprot.org/annotation/VAR_086017
http://togogenome.org/gene/9606:ZCCHC24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2G6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Phosphoserine|||Zinc finger CCHC domain-containing protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274289|||http://purl.uniprot.org/annotation/VAR_030249
http://togogenome.org/gene/9606:ZNF750                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32MQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes the ability to induce epidermal terminal differentiation; when associated with A-27.|||Abolishes the ability to induce epidermal terminal differentiation; when associated with A-30.|||Abolishes the ability to induce epidermal terminal differentiation; when associated with A-39.|||Abolishes the ability to induce epidermal terminal differentiation; when associated with A-43.|||Basic and acidic residues|||C2H2-type; degenerate|||Disordered|||Polar residues|||Zinc finger protein 750                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247070|||http://purl.uniprot.org/annotation/VAR_027062|||http://purl.uniprot.org/annotation/VAR_051502|||http://purl.uniprot.org/annotation/VAR_051503
http://togogenome.org/gene/9606:ETFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3L0|||http://purl.uniprot.org/uniprot/P13804                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decreased protein stability.|||Domain I|||Domain II|||Electron transfer flavoprotein alpha/beta-subunit N-terminal|||Electron transfer flavoprotein subunit alpha, mitochondrial|||In GA2A.|||In GA2A; decreased electron transfer activity.|||In GA2A; impaired protein stability and loss of electron transfer activity.|||In isoform 2.|||Loss of electron transfer activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008650|||http://purl.uniprot.org/annotation/VAR_002366|||http://purl.uniprot.org/annotation/VAR_002367|||http://purl.uniprot.org/annotation/VAR_002368|||http://purl.uniprot.org/annotation/VAR_008547|||http://purl.uniprot.org/annotation/VSP_043246
http://togogenome.org/gene/9606:ZNF91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05481                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27; degenerate|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 31|||C2H2-type 32|||C2H2-type 33|||C2H2-type 34|||C2H2-type 35|||C2H2-type 36|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 91                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047400|||http://purl.uniprot.org/annotation/VAR_057393|||http://purl.uniprot.org/annotation/VAR_057394|||http://purl.uniprot.org/annotation/VAR_059897|||http://purl.uniprot.org/annotation/VAR_059898|||http://purl.uniprot.org/annotation/VAR_059899|||http://purl.uniprot.org/annotation/VAR_060417|||http://purl.uniprot.org/annotation/VAR_060418|||http://purl.uniprot.org/annotation/VAR_060419|||http://purl.uniprot.org/annotation/VAR_060420|||http://purl.uniprot.org/annotation/VAR_060421|||http://purl.uniprot.org/annotation/VSP_040288
http://togogenome.org/gene/9606:CCDC85C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKD9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 85C|||Disordered|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345410
http://togogenome.org/gene/9606:TRNP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8E5N8C3|||http://purl.uniprot.org/uniprot/Q6NT89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pro residues|||TMF-regulated nuclear protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336088|||http://purl.uniprot.org/annotation/VAR_043545
http://togogenome.org/gene/9606:DAPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHI4|||http://purl.uniprot.org/uniprot/P53355|||http://purl.uniprot.org/uniprot/Q59H88                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Autoinhibitory domain|||Calmodulin-binding|||Death|||Death-associated protein kinase 1|||Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of activity, apoptotic function and of autophosphorylation.|||Loss of phosphorylation and significant increase in proapoptotic activity.|||Minimal effect on activity.|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphoserine; by RPS6KA1 and RPS6KA3|||Phosphoserine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity.|||Reduction in proapoptotic activity.|||Roc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085910|||http://purl.uniprot.org/annotation/VAR_033235|||http://purl.uniprot.org/annotation/VAR_040420|||http://purl.uniprot.org/annotation/VAR_040421|||http://purl.uniprot.org/annotation/VAR_040422|||http://purl.uniprot.org/annotation/VAR_040423|||http://purl.uniprot.org/annotation/VAR_040424|||http://purl.uniprot.org/annotation/VAR_040425|||http://purl.uniprot.org/annotation/VAR_040426|||http://purl.uniprot.org/annotation/VAR_040427|||http://purl.uniprot.org/annotation/VAR_040428|||http://purl.uniprot.org/annotation/VAR_040429|||http://purl.uniprot.org/annotation/VAR_040430|||http://purl.uniprot.org/annotation/VAR_040431|||http://purl.uniprot.org/annotation/VAR_040432|||http://purl.uniprot.org/annotation/VAR_040433|||http://purl.uniprot.org/annotation/VAR_040434|||http://purl.uniprot.org/annotation/VAR_040435|||http://purl.uniprot.org/annotation/VAR_060693|||http://purl.uniprot.org/annotation/VAR_060694|||http://purl.uniprot.org/annotation/VSP_042053|||http://purl.uniprot.org/annotation/VSP_042054|||http://purl.uniprot.org/annotation/VSP_042055|||http://purl.uniprot.org/annotation/VSP_042056|||http://purl.uniprot.org/annotation/VSP_054478
http://togogenome.org/gene/9606:ELOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14241                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation domain|||BC-box|||Basic and acidic residues|||Disordered|||Elongin-A|||F-box|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||TFIIS N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086960|||http://purl.uniprot.org/annotation/VAR_020104|||http://purl.uniprot.org/annotation/VAR_033850|||http://purl.uniprot.org/annotation/VAR_033851
http://togogenome.org/gene/9606:CCDC39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UFE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 39|||Disordered|||In CILD14; unknown pathological significance.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234493|||http://purl.uniprot.org/annotation/VAR_072468|||http://purl.uniprot.org/annotation/VSP_037014|||http://purl.uniprot.org/annotation/VSP_037015|||http://purl.uniprot.org/annotation/VSP_037016
http://togogenome.org/gene/9606:TMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDI8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNA36.|||In DFNB7.|||Transmembrane channel-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185380|||http://purl.uniprot.org/annotation/VAR_014125|||http://purl.uniprot.org/annotation/VAR_014126|||http://purl.uniprot.org/annotation/VAR_052333|||http://purl.uniprot.org/annotation/VAR_052334|||http://purl.uniprot.org/annotation/VAR_052335
http://togogenome.org/gene/9606:NSMCE4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXX6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Non-structural maintenance of chromosomes element 4 homolog A|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214101|||http://purl.uniprot.org/annotation/VAR_057657|||http://purl.uniprot.org/annotation/VSP_014601|||http://purl.uniprot.org/annotation/VSP_014602
http://togogenome.org/gene/9606:KCNE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7LFK2|||http://purl.uniprot.org/uniprot/A7LFK4|||http://purl.uniprot.org/uniprot/C7S316|||http://purl.uniprot.org/uniprot/P15382|||http://purl.uniprot.org/uniprot/Q6FHJ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  50% reduction of cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5 and T-7; when associated with T-28.|||Cytoplasmic|||Helical|||In JLNS2.|||In JLNS2; impairs glycosylation at N-5.|||In LQT5 and JLNS2; suppresses KCNQ1 currents markedly.|||In LQT5.|||In LQT5; mild phenotype; unknown pathological significance; no effect on KCNQ1 C-terminus interaction; increases cAMP-mediated up-regulation of the I(KS) current; no effect on phosphorylation at S27.|||In LQT5; moderately reduces I(KS) current density; no change of the voltage dependence of channel activation; markedly reduces interaction with KCNQ1 C-terminus; no effect on plasma membrane localization; loss of cAMP-mediated up-regulation of the I(KS) current; no effect on interaction with AKAP9; impairs phosphorylation at S-27 during cAMP-dependent stimulation.|||In LQT5; unknown pathological significance.|||Increase in inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.|||Interacts with the scolopendra toxin SSD609|||Loss inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.|||Lowers current 2-fold and leads to faster deactivation of KCNQ1/KCNE1 channel.|||N-linked (GlcNAc...) asparagine|||No change in inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.|||No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5; when associated with Q-5. 50% reduction of cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5 and T-7; when associated with A-7.|||No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5; when associated with T-28.|||No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex. Loss of glycosylation at T-7.|||O-linked (GalNAc...) threonine|||Phosphoserine; by PKC|||Potassium voltage-gated channel subfamily E member 1|||Predisposes to acquired LQT5 susceptibility; shows a significant difference in current density and midpoint potential compared to the wild-type channel.|||Totally suppressed interaction with KCNQ1 C-terminus.|||interaction with KCNQ1 C-terminus                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144278|||http://purl.uniprot.org/annotation/VAR_001558|||http://purl.uniprot.org/annotation/VAR_001559|||http://purl.uniprot.org/annotation/VAR_008897|||http://purl.uniprot.org/annotation/VAR_008898|||http://purl.uniprot.org/annotation/VAR_008899|||http://purl.uniprot.org/annotation/VAR_008900|||http://purl.uniprot.org/annotation/VAR_008901|||http://purl.uniprot.org/annotation/VAR_008902|||http://purl.uniprot.org/annotation/VAR_008903|||http://purl.uniprot.org/annotation/VAR_009906|||http://purl.uniprot.org/annotation/VAR_009907|||http://purl.uniprot.org/annotation/VAR_009908|||http://purl.uniprot.org/annotation/VAR_012802|||http://purl.uniprot.org/annotation/VAR_048024|||http://purl.uniprot.org/annotation/VAR_074908|||http://purl.uniprot.org/annotation/VAR_074909|||http://purl.uniprot.org/annotation/VAR_074910|||http://purl.uniprot.org/annotation/VAR_074911|||http://purl.uniprot.org/annotation/VAR_074912|||http://purl.uniprot.org/annotation/VAR_074913|||http://purl.uniprot.org/annotation/VAR_074914|||http://purl.uniprot.org/annotation/VAR_074915|||http://purl.uniprot.org/annotation/VAR_074916|||http://purl.uniprot.org/annotation/VAR_074917|||http://purl.uniprot.org/annotation/VAR_074918|||http://purl.uniprot.org/annotation/VAR_074919|||http://purl.uniprot.org/annotation/VAR_074920
http://togogenome.org/gene/9606:LRRC52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7C0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 52|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226826|||http://purl.uniprot.org/annotation/VAR_051122
http://togogenome.org/gene/9606:CNTLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AMC8|||http://purl.uniprot.org/uniprot/Q9NXG0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centlein|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227567|||http://purl.uniprot.org/annotation/VAR_025608|||http://purl.uniprot.org/annotation/VAR_025609|||http://purl.uniprot.org/annotation/VAR_025610|||http://purl.uniprot.org/annotation/VAR_056840|||http://purl.uniprot.org/annotation/VAR_056841|||http://purl.uniprot.org/annotation/VSP_017558|||http://purl.uniprot.org/annotation/VSP_032864|||http://purl.uniprot.org/annotation/VSP_032865
http://togogenome.org/gene/9606:TRIM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HHS7|||http://purl.uniprot.org/uniprot/Q9C035                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ligase activity.|||B box-type|||B30.2/SPRY|||In isoform Beta.|||In isoform Delta.|||In isoform Epsilon.|||In isoform Gamma.|||In isoform Iota.|||Increases strongly cell restriction against HIV-1 and SIVmac infection.|||Increases strongly cell restriction against HIV-1 infection.|||N-acetylalanine|||No effect on HIV-1 and SIVmac infection.|||Phosphoserine|||RING-type|||Removed|||Required for interaction with GABARAP and for autophagy|||Tripartite motif-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056201|||http://purl.uniprot.org/annotation/VAR_017397|||http://purl.uniprot.org/annotation/VAR_017398|||http://purl.uniprot.org/annotation/VAR_030154|||http://purl.uniprot.org/annotation/VAR_030155|||http://purl.uniprot.org/annotation/VAR_030156|||http://purl.uniprot.org/annotation/VAR_030157|||http://purl.uniprot.org/annotation/VAR_060707|||http://purl.uniprot.org/annotation/VAR_060708|||http://purl.uniprot.org/annotation/VAR_060709|||http://purl.uniprot.org/annotation/VAR_060710|||http://purl.uniprot.org/annotation/VSP_009010|||http://purl.uniprot.org/annotation/VSP_009011|||http://purl.uniprot.org/annotation/VSP_009012|||http://purl.uniprot.org/annotation/VSP_009013|||http://purl.uniprot.org/annotation/VSP_009014|||http://purl.uniprot.org/annotation/VSP_009015|||http://purl.uniprot.org/annotation/VSP_009016|||http://purl.uniprot.org/annotation/VSP_009017|||http://purl.uniprot.org/annotation/VSP_044095|||http://purl.uniprot.org/annotation/VSP_044096
http://togogenome.org/gene/9606:ALDH5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51649|||http://purl.uniprot.org/uniprot/X5D299|||http://purl.uniprot.org/uniprot/X5DQN2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  48% of activity.|||65% of activity.|||83% of activity.|||Aldehyde dehydrogenase|||In SSADHD.|||In SSADHD; 1% of activity.|||In SSADHD; 17% of activity.|||In SSADHD; 2% of activity.|||In SSADHD; 3% of activity.|||In SSADHD; 4% of activity.|||In SSADHD; 5% of activity.|||In SSADHD; <1% of activity.|||In inhibited form|||In isoform 2.|||Loss of regulation by redox state.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on succinate-semialdehyde dehydrogenase activity.|||Nucleophile|||Phosphoserine|||Proton acceptor|||Reduces catalytic activity to less than 15% of wild-type.|||Succinate-semialdehyde dehydrogenase, mitochondrial|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007184|||http://purl.uniprot.org/annotation/VAR_016758|||http://purl.uniprot.org/annotation/VAR_016759|||http://purl.uniprot.org/annotation/VAR_026199|||http://purl.uniprot.org/annotation/VAR_026200|||http://purl.uniprot.org/annotation/VAR_026201|||http://purl.uniprot.org/annotation/VAR_026202|||http://purl.uniprot.org/annotation/VAR_026203|||http://purl.uniprot.org/annotation/VAR_026204|||http://purl.uniprot.org/annotation/VAR_026205|||http://purl.uniprot.org/annotation/VAR_026206|||http://purl.uniprot.org/annotation/VAR_026207|||http://purl.uniprot.org/annotation/VAR_026208|||http://purl.uniprot.org/annotation/VAR_026209|||http://purl.uniprot.org/annotation/VAR_026210|||http://purl.uniprot.org/annotation/VAR_026227|||http://purl.uniprot.org/annotation/VAR_026228|||http://purl.uniprot.org/annotation/VAR_026229|||http://purl.uniprot.org/annotation/VAR_069047|||http://purl.uniprot.org/annotation/VSP_045231
http://togogenome.org/gene/9606:HSPA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK72|||http://purl.uniprot.org/uniprot/P48723                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heat shock 70 kDa protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013558|||http://purl.uniprot.org/annotation/PRO_5007491841
http://togogenome.org/gene/9606:SCEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95171                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||16 X approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||LIM zinc-binding|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Sciellin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075903|||http://purl.uniprot.org/annotation/VAR_047920|||http://purl.uniprot.org/annotation/VAR_047921|||http://purl.uniprot.org/annotation/VAR_047922|||http://purl.uniprot.org/annotation/VSP_035980|||http://purl.uniprot.org/annotation/VSP_045288|||http://purl.uniprot.org/annotation/VSP_045289
http://togogenome.org/gene/9606:LARP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KWU3|||http://purl.uniprot.org/uniprot/Q6PKG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes RNA binding. Abolishes inhibition of EIF4G1 binding to mRNA molecules with a 5'TOP motif; when associated with A-960.|||Abolishes RNA binding. Abolishes translational repression of mRNAs with a 5'TOP motif. Abolishes inhibition of EIF4G1 binding to mRNA molecules with a 5'TOP motif; when associated with E-917.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH La-type RNA-binding|||In isoform 2.|||Interaction with 7-methylguanosine mRNA cap structure|||Interaction with mRNA|||La-related protein 1|||Loss of interaction with RPTOR.|||Loss of phosphorylation by MTOR; when associated with A-766. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-847 and A-1058.|||Loss of phosphorylation by MTOR; when associated with A-769. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-769; A-847 and A-1058.|||N-acetylalanine|||N6-acetyllysine|||No effect on interaction with RPTOR.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Required for interaction with PABPC1|||Required for interaction with RPTOR and for repression of mRNAs with a 5'TOP motif|||Strongly decreased RNA binding.|||Strongly reduced interaction with PABPC1.|||Strongly reduced phosphorylation mediated by AKT and RPS6KB1. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-769 and A-847.|||Strongly reduced phosphorylation mediated by Akt and RPS6KB1. Decreased interaction with RPTOR and impaired dissociation from the 5'UTR of mRNA molecules; when associated with A-766; A-769 and A-1058.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207609|||http://purl.uniprot.org/annotation/VSP_015114|||http://purl.uniprot.org/annotation/VSP_015115
http://togogenome.org/gene/9606:MYRFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LU7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Myelin regulatory factor-like protein|||NDT80|||Peptidase S74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252150|||http://purl.uniprot.org/annotation/VAR_027780|||http://purl.uniprot.org/annotation/VAR_033742|||http://purl.uniprot.org/annotation/VAR_069018
http://togogenome.org/gene/9606:PTPN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZD9|||http://purl.uniprot.org/uniprot/P35236                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cysteine sulfenic acid (-SOH)|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with MAP kinases|||Loss of catalytic activity.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphothreonine|||Prevents dissociation of bound MAP kinase and enhances their dephosphorylation.|||Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66.|||Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93.|||Reduced catalytic activity.|||Reduces binding of MAP kinase.|||Strongly reduced catalytic activity.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094761|||http://purl.uniprot.org/annotation/VSP_026925|||http://purl.uniprot.org/annotation/VSP_047275
http://togogenome.org/gene/9606:ADAMTS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2U9|||http://purl.uniprot.org/uniprot/O15072|||http://purl.uniprot.org/uniprot/Q96AY5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 3|||Basic and acidic residues|||Disintegrin|||Disordered|||In HKLLS3; affects proteolytic maturation and impairs secretion.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Peptidase M12B propeptide|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029162|||http://purl.uniprot.org/annotation/PRO_0000029163|||http://purl.uniprot.org/annotation/VAR_055012|||http://purl.uniprot.org/annotation/VAR_055013|||http://purl.uniprot.org/annotation/VAR_081558|||http://purl.uniprot.org/annotation/VAR_081559
http://togogenome.org/gene/9606:AQP7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SI91|||http://purl.uniprot.org/uniprot/A0A8Q3SJ69|||http://purl.uniprot.org/uniprot/A0A8Q3WL09                                                                                  ^@                                                                                  Region|||Transmembrane                                                                                  ^@                                                                                  Transmembrane                                                                                  ^@                                                                                  Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:RHAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02094|||http://purl.uniprot.org/uniprot/Q96E98                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ammonium transporter AmtB-like|||Ammonium transporter Rh type A|||Cytoplasmic|||Extracellular|||Helical|||In DSLK or RHAG3 antigen (030003).|||In Duclos or RHAG1 antigen (030001).|||In OHST; enhances monovalent cation leak; decreases ammonium fluxes; highly decreases STOM expression; decreases membrane expression; no effect on water permeability.|||In OHST; strongly enhances monovalent cation leak.|||In Ol(a) or RHAG2 antigen (030002).|||In RHN.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168199|||http://purl.uniprot.org/annotation/VAR_006921|||http://purl.uniprot.org/annotation/VAR_015855|||http://purl.uniprot.org/annotation/VAR_015856|||http://purl.uniprot.org/annotation/VAR_015857|||http://purl.uniprot.org/annotation/VAR_015858|||http://purl.uniprot.org/annotation/VAR_047999|||http://purl.uniprot.org/annotation/VAR_076283|||http://purl.uniprot.org/annotation/VAR_076284|||http://purl.uniprot.org/annotation/VAR_076285|||http://purl.uniprot.org/annotation/VAR_076286|||http://purl.uniprot.org/annotation/VAR_076287|||http://purl.uniprot.org/annotation/VSP_047629|||http://purl.uniprot.org/annotation/VSP_047630
http://togogenome.org/gene/9606:SLC9A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIX7|||http://purl.uniprot.org/uniprot/Q9Y2E8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cation/H+ exchanger|||Helical|||In isoform 2.|||Induces endosomal clustering.|||Phosphoserine|||Phosphothreonine|||Sodium/hydrogen exchanger 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052365|||http://purl.uniprot.org/annotation/VSP_037686
http://togogenome.org/gene/9606:TXNRD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRZ5|||http://purl.uniprot.org/uniprot/Q86VQ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Non standard residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Cysteinyl-selenocysteine (Cys-Sec)|||Disordered|||FAD/NAD(P)-binding|||Glutaredoxin|||N6-succinyllysine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Proton acceptor|||Pyridine nucleotide-disulphide oxidoreductase dimerisation|||Redox-active|||Selenocysteine|||Thioredoxin reductase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320695
http://togogenome.org/gene/9606:FAM9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM9A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119032
http://togogenome.org/gene/9606:POLRMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00411|||http://purl.uniprot.org/uniprot/Q4G0F4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerase N-terminal|||DNA-directed RNA polymerase, mitochondrial|||Disordered|||In COXPD55.|||In COXPD55; results in decreased transcription of mitochondrial DNA in vitro.|||In COXPD55; results in decreased transcription of mitochondrial DNA in vitro; reduced DNA primase activity.|||In COXPD55; results in mild reduction of transcription of mitochondrial DNA in an in vitro assay.|||In COXPD55; results in mild reduction of transcription of mitochondrial DNA in vitro; reduced DNA primase activity.|||In COXPD55; unknown pathological significance; results in decreased transcription of mitochondrial DNA in vitro.|||In COXPD55; when associated in cis with F-1193.|||In COXPD55; when associated in cis with S-566.|||Mediates interaction with TEFM|||Mitochondrion|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031068|||http://purl.uniprot.org/annotation/VAR_019427|||http://purl.uniprot.org/annotation/VAR_086918|||http://purl.uniprot.org/annotation/VAR_086919|||http://purl.uniprot.org/annotation/VAR_086920|||http://purl.uniprot.org/annotation/VAR_086921|||http://purl.uniprot.org/annotation/VAR_086922|||http://purl.uniprot.org/annotation/VAR_086923|||http://purl.uniprot.org/annotation/VAR_086924|||http://purl.uniprot.org/annotation/VAR_086925|||http://purl.uniprot.org/annotation/VAR_086926|||http://purl.uniprot.org/annotation/VAR_086927|||http://purl.uniprot.org/annotation/VAR_086928
http://togogenome.org/gene/9606:UCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969E3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Isoleucine amide|||Urocortin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006245|||http://purl.uniprot.org/annotation/PRO_0000006246|||http://purl.uniprot.org/annotation/VAR_060410|||http://purl.uniprot.org/annotation/VAR_060411
http://togogenome.org/gene/9606:MPRIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6WCQ1|||http://purl.uniprot.org/uniprot/Q8N236                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with F-actin|||Interaction with PPP1R12A|||Interaction with RHOA|||Myosin phosphatase Rho-interacting protein|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223930|||http://purl.uniprot.org/annotation/VAR_051203|||http://purl.uniprot.org/annotation/VSP_051947|||http://purl.uniprot.org/annotation/VSP_051948
http://togogenome.org/gene/9606:ZNF784                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Zinc finger protein 784                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270996
http://togogenome.org/gene/9606:THSD7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0I4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||TSP type-1 1|||TSP type-1 10|||TSP type-1 11|||TSP type-1 12|||TSP type-1 13|||TSP type-1 14|||TSP type-1 15|||TSP type-1 16|||TSP type-1 17|||TSP type-1 18|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9|||Thrombospondin type-1 domain-containing protein 7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260251
http://togogenome.org/gene/9606:RAMP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2L1|||http://purl.uniprot.org/uniprot/O60896                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Receptor activity-modifying protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030176|||http://purl.uniprot.org/annotation/PRO_5014296878|||http://purl.uniprot.org/annotation/VAR_024602|||http://purl.uniprot.org/annotation/VAR_034437|||http://purl.uniprot.org/annotation/VAR_053628
http://togogenome.org/gene/9606:NPAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXF0|||http://purl.uniprot.org/uniprot/X5D2Q4|||http://purl.uniprot.org/uniprot/X5D988                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Basic residues|||DNA-binding|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5 and isoform 6.|||In isoform 5.|||Neuronal PAS domain-containing protein 3|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127408|||http://purl.uniprot.org/annotation/VSP_009084|||http://purl.uniprot.org/annotation/VSP_009085|||http://purl.uniprot.org/annotation/VSP_009086|||http://purl.uniprot.org/annotation/VSP_009087|||http://purl.uniprot.org/annotation/VSP_009088|||http://purl.uniprot.org/annotation/VSP_009089
http://togogenome.org/gene/9606:DSG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14126                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with CMD1BB and ARVD10 although it may not be sufficient by itself to result in cardiomyopathy.|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein repeat 3|||Desmoglein repeat 4|||Desmoglein repeat 5|||Desmoglein repeat 6|||Desmoglein-2|||Disordered|||Extracellular|||Helical|||In ARVD10.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003845|||http://purl.uniprot.org/annotation/PRO_0000003846|||http://purl.uniprot.org/annotation/VAR_029365|||http://purl.uniprot.org/annotation/VAR_029366|||http://purl.uniprot.org/annotation/VAR_029367|||http://purl.uniprot.org/annotation/VAR_029368|||http://purl.uniprot.org/annotation/VAR_048508|||http://purl.uniprot.org/annotation/VAR_048509|||http://purl.uniprot.org/annotation/VAR_048510|||http://purl.uniprot.org/annotation/VAR_048511|||http://purl.uniprot.org/annotation/VAR_048512|||http://purl.uniprot.org/annotation/VAR_048513|||http://purl.uniprot.org/annotation/VAR_062387|||http://purl.uniprot.org/annotation/VAR_062388|||http://purl.uniprot.org/annotation/VAR_062389|||http://purl.uniprot.org/annotation/VAR_062390|||http://purl.uniprot.org/annotation/VAR_065686
http://togogenome.org/gene/9606:ZNF106                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGM5|||http://purl.uniprot.org/uniprot/Q9H2Y7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||Zinc finger protein 106                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051467|||http://purl.uniprot.org/annotation/VAR_053440|||http://purl.uniprot.org/annotation/VAR_053441|||http://purl.uniprot.org/annotation/VAR_053442|||http://purl.uniprot.org/annotation/VAR_053443|||http://purl.uniprot.org/annotation/VSP_057120|||http://purl.uniprot.org/annotation/VSP_057121
http://togogenome.org/gene/9606:C12orf71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTZ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C12orf71                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343577|||http://purl.uniprot.org/annotation/VAR_056837
http://togogenome.org/gene/9606:ZNF837                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Zinc finger protein 837                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321906|||http://purl.uniprot.org/annotation/VAR_039373|||http://purl.uniprot.org/annotation/VAR_061979
http://togogenome.org/gene/9606:SSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JBX5|||http://purl.uniprot.org/uniprot/P43307                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Translocon-associated protein subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033281|||http://purl.uniprot.org/annotation/PRO_5002996419|||http://purl.uniprot.org/annotation/VAR_022427|||http://purl.uniprot.org/annotation/VSP_013621
http://togogenome.org/gene/9606:CRTAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95727                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Cytotoxic and regulatory T-cell molecule|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Reduced binding to CADM1. Severely impairs interaction with CADM1; when associated with A-56, A-57 and A-101.|||Reduced binding to CADM1. Severely impairs interaction with CADM1; when associated with A-56, A-57 and A-67.|||Reduced binding to CADM1. Severely impairs interaction with CADM1; when associated with A-56, A-67 and A-101.|||Reduced binding to CADM1. Severely impairs interaction with CADM1; when associated with A-57, A-67 and A-101.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292602|||http://purl.uniprot.org/annotation/VAR_032999|||http://purl.uniprot.org/annotation/VAR_033000|||http://purl.uniprot.org/annotation/VAR_049868|||http://purl.uniprot.org/annotation/VAR_049869|||http://purl.uniprot.org/annotation/VAR_049870|||http://purl.uniprot.org/annotation/VSP_052471|||http://purl.uniprot.org/annotation/VSP_052472
http://togogenome.org/gene/9606:NPLOC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAT6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished interaction with VCP; when associated with 6-A--A-8 and A-17.|||Abolished interaction with VCP; when associated with 6-A--A-8 and A-50.|||Abolished interaction with VCP; when associated with A-17 and A-50.|||In isoform 2.|||MPN|||N-acetylalanine|||N6-acetyllysine|||Nuclear protein localization protein 4 homolog|||RanBP2-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057941|||http://purl.uniprot.org/annotation/VSP_009789
http://togogenome.org/gene/9606:ZC3H12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYM0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||In isoform 2.|||Polar residues|||Probable ribonuclease ZC3H12B|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254045|||http://purl.uniprot.org/annotation/VSP_039896
http://togogenome.org/gene/9606:IZUMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYV9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with IZUMO1R.|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Important for interaction with IZUMO1R|||In isoform 2.|||In isoform 3.|||Izumo sperm-egg fusion protein 1|||Mildly decreases interaction with IZUMO1R.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes interaction with IZUMO1R.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045482|||http://purl.uniprot.org/annotation/VAR_055399|||http://purl.uniprot.org/annotation/VSP_016960|||http://purl.uniprot.org/annotation/VSP_016961|||http://purl.uniprot.org/annotation/VSP_016962|||http://purl.uniprot.org/annotation/VSP_016963
http://togogenome.org/gene/9606:LRFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P244                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||LRRNT|||Leucine-rich repeat and fibronectin type III domain-containing protein 1|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334145
http://togogenome.org/gene/9606:KYNU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16719                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mass|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In HYXKY; reduced 3-hydroxykynureninase activity.|||In VCRL2; strongly reduced 3-hydroxykynureninase activity.|||In isoform 2.|||Kynureninase|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||The reported mass is given to only three significant figures.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218657|||http://purl.uniprot.org/annotation/VAR_022092|||http://purl.uniprot.org/annotation/VAR_049724|||http://purl.uniprot.org/annotation/VAR_054401|||http://purl.uniprot.org/annotation/VAR_080254|||http://purl.uniprot.org/annotation/VSP_042739|||http://purl.uniprot.org/annotation/VSP_042740
http://togogenome.org/gene/9606:LGR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K8C7|||http://purl.uniprot.org/uniprot/O75473                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes activation of Wnt signaling.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impaired internalization to the trans-Golgi network; when associated with A-861.|||Impaired internalization to the trans-Golgi network; when associated with A-864.|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||Leucine-rich repeat-containing G-protein coupled receptor 5|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012794|||http://purl.uniprot.org/annotation/PRO_5014220899|||http://purl.uniprot.org/annotation/VAR_049411|||http://purl.uniprot.org/annotation/VAR_049412|||http://purl.uniprot.org/annotation/VSP_037746|||http://purl.uniprot.org/annotation/VSP_054782
http://togogenome.org/gene/9606:AMBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02760                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-1-microglobulin|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Cleavage; in the presence of oxyhemoglobin or MPO|||Glycopeptide (secretory piece)|||Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-137. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-137.|||Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-149.|||Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-137 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-137 and T-149.|||Impairs the reductase activity toward cytochrome c independently of the electron donnor. Decreases the reductase activity toward methemoglobin. Decreases the reductase activity toward oxidized collagen.|||Inhibitory (P1) (chymotrypsin, elastase)|||Inhibitory (P1) (trypsin)|||Inter-alpha-trypsin inhibitor light chain|||N-linked (GlcNAc...) (complex) asparagine|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Trypstatin|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000172|||http://purl.uniprot.org/annotation/PRO_0000017886|||http://purl.uniprot.org/annotation/PRO_0000017887|||http://purl.uniprot.org/annotation/PRO_0000318926
http://togogenome.org/gene/9606:SFSWAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12872|||http://purl.uniprot.org/uniprot/Q8IV81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SURP motif|||SURP motif 1|||SURP motif 2|||Splicing factor, suppressor of white-apricot homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081934|||http://purl.uniprot.org/annotation/VAR_021789|||http://purl.uniprot.org/annotation/VAR_046442|||http://purl.uniprot.org/annotation/VAR_046443|||http://purl.uniprot.org/annotation/VAR_046444|||http://purl.uniprot.org/annotation/VAR_057248|||http://purl.uniprot.org/annotation/VAR_057249|||http://purl.uniprot.org/annotation/VAR_057250|||http://purl.uniprot.org/annotation/VSP_044786
http://togogenome.org/gene/9606:P2RY6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15077                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||P2Y purinoceptor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070028
http://togogenome.org/gene/9606:PPIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3V4|||http://purl.uniprot.org/uniprot/A0A0S2Z5A8|||http://purl.uniprot.org/uniprot/Q9H2H8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylserine|||Omega-N-methylarginine|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase-like 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064166|||http://purl.uniprot.org/annotation/VAR_023417|||http://purl.uniprot.org/annotation/VSP_015468
http://togogenome.org/gene/9606:POTEJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG39                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Actin-like|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395414
http://togogenome.org/gene/9606:TECR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSQ1|||http://purl.uniprot.org/uniprot/Q9NZ01                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In MRT14; reduced enzyme activity; reduced protein stability; no effect on subcellular localization.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Steroid 5-alpha reductase C-terminal|||Very-long-chain enoyl-CoA reductase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213683|||http://purl.uniprot.org/annotation/VAR_065918|||http://purl.uniprot.org/annotation/VSP_005957
http://togogenome.org/gene/9606:RPL3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92901                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In CMD2D; unknown pathological significance.|||Ribosomal protein uL3-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077233|||http://purl.uniprot.org/annotation/VAR_034461|||http://purl.uniprot.org/annotation/VAR_085880|||http://purl.uniprot.org/annotation/VAR_085881|||http://purl.uniprot.org/annotation/VAR_085882|||http://purl.uniprot.org/annotation/VAR_085883|||http://purl.uniprot.org/annotation/VAR_085884|||http://purl.uniprot.org/annotation/VAR_085885|||http://purl.uniprot.org/annotation/VAR_085886|||http://purl.uniprot.org/annotation/VAR_087799|||http://purl.uniprot.org/annotation/VAR_087800
http://togogenome.org/gene/9606:BCL7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VC05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  B-cell CLL/lymphoma 7 protein family member A|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239823|||http://purl.uniprot.org/annotation/VAR_033539|||http://purl.uniprot.org/annotation/VSP_019271
http://togogenome.org/gene/9606:SORD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00796                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In SORDD.|||In SORDD; results in protein aggregation.|||In SORDD; unknown pathological significance.|||In SORDD; unknown pathological significance; results in protein aggregation.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Sorbitol dehydrogenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160817|||http://purl.uniprot.org/annotation/VAR_000430|||http://purl.uniprot.org/annotation/VAR_060351|||http://purl.uniprot.org/annotation/VAR_084362|||http://purl.uniprot.org/annotation/VAR_084363|||http://purl.uniprot.org/annotation/VAR_084364|||http://purl.uniprot.org/annotation/VAR_084365|||http://purl.uniprot.org/annotation/VAR_084366|||http://purl.uniprot.org/annotation/VAR_084367|||http://purl.uniprot.org/annotation/VAR_084368|||http://purl.uniprot.org/annotation/VAR_084369|||http://purl.uniprot.org/annotation/VSP_056353|||http://purl.uniprot.org/annotation/VSP_056354
http://togogenome.org/gene/9606:GALNT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SF2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-acetylgalactosaminyltransferase 7|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059116
http://togogenome.org/gene/9606:AGBL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDL9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytosolic carboxypeptidase-like protein 5|||Disordered|||In RP75.|||In RP75; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305921|||http://purl.uniprot.org/annotation/VAR_035231|||http://purl.uniprot.org/annotation/VAR_077018|||http://purl.uniprot.org/annotation/VAR_077019|||http://purl.uniprot.org/annotation/VAR_079522|||http://purl.uniprot.org/annotation/VAR_079523|||http://purl.uniprot.org/annotation/VAR_079524|||http://purl.uniprot.org/annotation/VAR_079525|||http://purl.uniprot.org/annotation/VAR_079526|||http://purl.uniprot.org/annotation/VSP_028359|||http://purl.uniprot.org/annotation/VSP_028360|||http://purl.uniprot.org/annotation/VSP_028361|||http://purl.uniprot.org/annotation/VSP_028362
http://togogenome.org/gene/9606:FAM174B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Membrane protein FAM174B|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326114|||http://purl.uniprot.org/annotation/VAR_039989
http://togogenome.org/gene/9606:GTF2I                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9W7|||http://purl.uniprot.org/uniprot/P78347|||http://purl.uniprot.org/uniprot/Q499G6|||http://purl.uniprot.org/uniprot/X5D2J9|||http://purl.uniprot.org/uniprot/X5D939|||http://purl.uniprot.org/uniprot/X5DNP5|||http://purl.uniprot.org/uniprot/X5DR09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-503.|||Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-398 and F-503.|||Disordered|||GTF2I-like 1|||GTF2I-like 2|||GTF2I-like 3|||GTF2I-like 4|||GTF2I-like 5|||GTF2I-like 6|||General transcription factor II-I|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-398.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 5.|||N-acetylalanine|||N6-acetyllysine; alternate|||No change on BTK-mediated transcriptional activation.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PKG/PRKG1|||Phosphothreonine|||Phosphotyrosine; by BTK|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083872|||http://purl.uniprot.org/annotation/VAR_051026|||http://purl.uniprot.org/annotation/VSP_003867|||http://purl.uniprot.org/annotation/VSP_003868|||http://purl.uniprot.org/annotation/VSP_055195|||http://purl.uniprot.org/annotation/VSP_055196
http://togogenome.org/gene/9606:CYP4F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08477                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4F3|||Helical|||In isoform CYP4F3B.|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051851|||http://purl.uniprot.org/annotation/VAR_001258|||http://purl.uniprot.org/annotation/VAR_020664|||http://purl.uniprot.org/annotation/VAR_020665|||http://purl.uniprot.org/annotation/VAR_048457|||http://purl.uniprot.org/annotation/VAR_048458|||http://purl.uniprot.org/annotation/VSP_047193
http://togogenome.org/gene/9606:OLFML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYE3|||http://purl.uniprot.org/uniprot/Q6UWY5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Olfactomedin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020090|||http://purl.uniprot.org/annotation/PRO_5004257316|||http://purl.uniprot.org/annotation/VAR_034362|||http://purl.uniprot.org/annotation/VAR_034363
http://togogenome.org/gene/9606:COG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALW7|||http://purl.uniprot.org/uniprot/Q14746                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  COG complex component COG2 C-terminal|||Conserved oligomeric Golgi complex subunit 2|||Conserved oligomeric Golgi complex subunit 2 N-terminal|||Disordered|||In CDG2Q.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213495|||http://purl.uniprot.org/annotation/VAR_029274|||http://purl.uniprot.org/annotation/VAR_048757|||http://purl.uniprot.org/annotation/VAR_048758|||http://purl.uniprot.org/annotation/VAR_078769|||http://purl.uniprot.org/annotation/VSP_042942
http://togogenome.org/gene/9606:PRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04553|||http://purl.uniprot.org/uniprot/Q3MN80                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Initiator Methionine|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Initiator Methionine|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Interchain|||Interchain (with C-39)|||Removed|||Sperm protamine P1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191482
http://togogenome.org/gene/9606:MYH14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L2Z2|||http://purl.uniprot.org/uniprot/B3KWH4|||http://purl.uniprot.org/uniprot/Q7Z406                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||IQ|||In DFNA4A.|||In PNMHH.|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin tail|||Myosin-14|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123431|||http://purl.uniprot.org/annotation/VAR_022866|||http://purl.uniprot.org/annotation/VAR_022867|||http://purl.uniprot.org/annotation/VAR_022868|||http://purl.uniprot.org/annotation/VAR_022869|||http://purl.uniprot.org/annotation/VAR_022870|||http://purl.uniprot.org/annotation/VAR_037302|||http://purl.uniprot.org/annotation/VAR_056176|||http://purl.uniprot.org/annotation/VAR_056177|||http://purl.uniprot.org/annotation/VAR_056178|||http://purl.uniprot.org/annotation/VAR_066338|||http://purl.uniprot.org/annotation/VAR_066339|||http://purl.uniprot.org/annotation/VSP_014628|||http://purl.uniprot.org/annotation/VSP_014629|||http://purl.uniprot.org/annotation/VSP_014630|||http://purl.uniprot.org/annotation/VSP_040881|||http://purl.uniprot.org/annotation/VSP_040882
http://togogenome.org/gene/9606:HAVCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPB1|||http://purl.uniprot.org/uniprot/Q96D42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||10|||11|||12|||12 X 6 AA approximate tandem repeats of V-P-T-T-T-T]|||2|||3|||4|||5|||6|||7|||8|||9|||About 25% loss of Chikungunya virus entry.|||About 50% loss of ubiquitination.|||About 60% loss of Chikungunya virus entry.|||Complete loss of ubiquitination; when associated with R-338.|||Complete loss of ubiquitination; when associated with R-346.|||Cytoplasmic|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Hepatitis A virus cellular receptor 1|||Ig-like|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014981|||http://purl.uniprot.org/annotation/PRO_5002803475|||http://purl.uniprot.org/annotation/VAR_023323|||http://purl.uniprot.org/annotation/VAR_056080|||http://purl.uniprot.org/annotation/VAR_081334
http://togogenome.org/gene/9606:DSPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZW4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cell attachment site|||Dentin phosphoprotein|||Dentin sialophosphoprotein|||Dentin sialoprotein|||Disordered|||In DFNA39/DGI1 and DGI3.|||In DFNA39/DGI1; dominant negative mutation; the mutant protein is retained intracellularly.|||In DGI2 and DGI3; dominant negative mutation; the mutant protein is retained intracellularly.|||In DGI2.|||In DGI2; dominant negative mutation; results in signal peptide retention; the mutant protein is retained within the rough ER membrane.|||In DGI2; dominant negative mutation; the mutant protein is retained intracellularly.|||In DGI3; the mutant protein is largely retained in the ER.|||In DTDP2; the mutant protein does not translocate into the endoplasmic reticulum.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by CK1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021120|||http://purl.uniprot.org/annotation/PRO_0000021121|||http://purl.uniprot.org/annotation/PRO_0000021122|||http://purl.uniprot.org/annotation/VAR_012280|||http://purl.uniprot.org/annotation/VAR_012281|||http://purl.uniprot.org/annotation/VAR_030661|||http://purl.uniprot.org/annotation/VAR_036861|||http://purl.uniprot.org/annotation/VAR_036862|||http://purl.uniprot.org/annotation/VAR_047551|||http://purl.uniprot.org/annotation/VAR_054443|||http://purl.uniprot.org/annotation/VAR_070252|||http://purl.uniprot.org/annotation/VAR_070253
http://togogenome.org/gene/9606:DHDDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects chain elongation resulting in shorter products.|||Dehydrodolichyl diphosphate synthase complex subunit DHDDS|||Delays cell growth; when associated with A-306 and A-313.|||Delays cell growth; when associated with A-306 and A-317.|||Delays cell growth; when associated with A-313 and A-317.|||Found in a patient with progressive myoclonus epilepsy; unknown pathological significance.|||In DEDSM; also found in a patient with progressive myoclonus epilepsy and developmental delay; unknown pathological significance.|||In DEDSM; unknown pathological significance.|||In RP59; 5-fold reduction in catalytic activity and reduced affinity for FPP but not for IPP..|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-12 and A-15.|||Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-12 and A-19.|||Markedly decreases phosphatidylinositol-mediated activation of cis-prenyltransferase activity resulting in products with longer chain length; when associated with A-15 and A-19.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123749|||http://purl.uniprot.org/annotation/VAR_028088|||http://purl.uniprot.org/annotation/VAR_065356|||http://purl.uniprot.org/annotation/VAR_080708|||http://purl.uniprot.org/annotation/VAR_080709|||http://purl.uniprot.org/annotation/VAR_085034|||http://purl.uniprot.org/annotation/VAR_085035|||http://purl.uniprot.org/annotation/VSP_010030|||http://purl.uniprot.org/annotation/VSP_010031|||http://purl.uniprot.org/annotation/VSP_045007
http://togogenome.org/gene/9606:SGCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16585|||http://purl.uniprot.org/uniprot/Q5U0N0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-sarcoglycan|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In LGMDR4.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with a myopathy resembling Becker muscular dystrophy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000175242|||http://purl.uniprot.org/annotation/VAR_010391|||http://purl.uniprot.org/annotation/VAR_010392|||http://purl.uniprot.org/annotation/VAR_010393|||http://purl.uniprot.org/annotation/VAR_010394|||http://purl.uniprot.org/annotation/VAR_010395|||http://purl.uniprot.org/annotation/VAR_010421|||http://purl.uniprot.org/annotation/VAR_010422|||http://purl.uniprot.org/annotation/VAR_010423|||http://purl.uniprot.org/annotation/VAR_010424|||http://purl.uniprot.org/annotation/VAR_010425|||http://purl.uniprot.org/annotation/VAR_010426|||http://purl.uniprot.org/annotation/VAR_010427|||http://purl.uniprot.org/annotation/VAR_010428|||http://purl.uniprot.org/annotation/VAR_081100|||http://purl.uniprot.org/annotation/VSP_056894
http://togogenome.org/gene/9606:ILVBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L0T0|||http://purl.uniprot.org/uniprot/M0R026                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  2-hydroxyacyl-CoA lyase 2|||Helical|||Thiamine pyrophosphate binding|||Thiamine pyrophosphate enzyme N-terminal TPP-binding|||Thiamine pyrophosphate enzyme TPP-binding|||Thiamine pyrophosphate enzyme central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314825|||http://purl.uniprot.org/annotation/VAR_038064|||http://purl.uniprot.org/annotation/VAR_061901
http://togogenome.org/gene/9606:PDSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2R2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  All trans-polyprenyl-diphosphate synthase PDSS1|||Disordered|||In COQ10D2.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123975|||http://purl.uniprot.org/annotation/VAR_034879|||http://purl.uniprot.org/annotation/VSP_017100|||http://purl.uniprot.org/annotation/VSP_017101
http://togogenome.org/gene/9606:SPINK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60575|||http://purl.uniprot.org/uniprot/V9HWG8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Kazal-like|||Reactive bond|||Serine protease inhibitor Kazal-type 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016569|||http://purl.uniprot.org/annotation/PRO_5014314730|||http://purl.uniprot.org/annotation/VAR_011898
http://togogenome.org/gene/9606:RGS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14924                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||GoLoco|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6.|||Omega-N-methylarginine|||PDZ|||PID|||Phosphoserine|||Polar residues|||Pro residues|||RBD 1|||RBD 2|||RGS|||Regulator of G-protein signaling 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204213|||http://purl.uniprot.org/annotation/VAR_020208|||http://purl.uniprot.org/annotation/VAR_034451|||http://purl.uniprot.org/annotation/VAR_034452|||http://purl.uniprot.org/annotation/VSP_005682|||http://purl.uniprot.org/annotation/VSP_005683|||http://purl.uniprot.org/annotation/VSP_005684|||http://purl.uniprot.org/annotation/VSP_005685|||http://purl.uniprot.org/annotation/VSP_005686|||http://purl.uniprot.org/annotation/VSP_005687|||http://purl.uniprot.org/annotation/VSP_047741|||http://purl.uniprot.org/annotation/VSP_047742|||http://purl.uniprot.org/annotation/VSP_047743|||http://purl.uniprot.org/annotation/VSP_047744
http://togogenome.org/gene/9606:ADGRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4P7|||http://purl.uniprot.org/uniprot/Q499H0|||http://purl.uniprot.org/uniprot/Q8IZP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G-protein coupled receptor G2|||Cytoplasmic|||Disordered|||Extracellular|||Found in a family with intellectual disability; unknown pathological significance.|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 10.|||In isoform 2.|||In isoform 3 and isoform 10.|||In isoform 4 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012886|||http://purl.uniprot.org/annotation/VAR_055289|||http://purl.uniprot.org/annotation/VAR_055290|||http://purl.uniprot.org/annotation/VAR_076259|||http://purl.uniprot.org/annotation/VAR_080773|||http://purl.uniprot.org/annotation/VSP_009791|||http://purl.uniprot.org/annotation/VSP_009792|||http://purl.uniprot.org/annotation/VSP_009793|||http://purl.uniprot.org/annotation/VSP_009794|||http://purl.uniprot.org/annotation/VSP_009795|||http://purl.uniprot.org/annotation/VSP_009796|||http://purl.uniprot.org/annotation/VSP_009797|||http://purl.uniprot.org/annotation/VSP_009798|||http://purl.uniprot.org/annotation/VSP_054522
http://togogenome.org/gene/9606:USHBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUE8|||http://purl.uniprot.org/uniprot/G8JLM4|||http://purl.uniprot.org/uniprot/Q8N6Y0|||http://purl.uniprot.org/uniprot/Q8N8Y1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Harmonin-binding protein USHBP1|||Harmonin-binding protein USHBP1 PDZ-binding|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252109|||http://purl.uniprot.org/annotation/VAR_027753|||http://purl.uniprot.org/annotation/VAR_027754|||http://purl.uniprot.org/annotation/VAR_051481|||http://purl.uniprot.org/annotation/VSP_052080
http://togogenome.org/gene/9606:EIF5AL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IS14                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 5A-1-like|||Hypusine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340263
http://togogenome.org/gene/9606:CALM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ51|||http://purl.uniprot.org/uniprot/P0DP23|||http://purl.uniprot.org/uniprot/P0DP24|||http://purl.uniprot.org/uniprot/P0DP25|||http://purl.uniprot.org/uniprot/Q96HY3|||http://purl.uniprot.org/uniprot/Q9BRL5                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT6; decreased calcium-binding affinity; not changed binding to RYR2; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed action potential duration.|||In LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release.|||In LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2.|||In LQT15.|||In LQT15; reduction in calcium affinity.|||In LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT16.|||In LQT16; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Necessary and sufficient for interaction with PCP4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CaMK4|||Phosphotyrosine|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000439932|||http://purl.uniprot.org/annotation/PRO_0000439933|||http://purl.uniprot.org/annotation/PRO_0000439934|||http://purl.uniprot.org/annotation/VAR_069222|||http://purl.uniprot.org/annotation/VAR_073275|||http://purl.uniprot.org/annotation/VAR_073276|||http://purl.uniprot.org/annotation/VAR_073277|||http://purl.uniprot.org/annotation/VAR_073279|||http://purl.uniprot.org/annotation/VAR_073280|||http://purl.uniprot.org/annotation/VAR_073281|||http://purl.uniprot.org/annotation/VAR_073282|||http://purl.uniprot.org/annotation/VAR_078261|||http://purl.uniprot.org/annotation/VAR_078262|||http://purl.uniprot.org/annotation/VAR_078263|||http://purl.uniprot.org/annotation/VAR_078541|||http://purl.uniprot.org/annotation/VAR_078542|||http://purl.uniprot.org/annotation/VAR_078543|||http://purl.uniprot.org/annotation/VAR_078544|||http://purl.uniprot.org/annotation/VAR_083814|||http://purl.uniprot.org/annotation/VAR_083815|||http://purl.uniprot.org/annotation/VAR_083816
http://togogenome.org/gene/9606:MOB3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BX8                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  MOB kinase activator 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193570
http://togogenome.org/gene/9606:MAP1S                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66K74                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MAP1S heavy chain|||MAP1S light chain|||Microtubule-associated protein 1S|||Necessary for association with actin|||Necessary for association with microtubules|||Necessary for interaction with RASSF1 isoform A and isoform C|||Necessary for the microtubule-organizing center localization|||Necessary for the mitochondrial aggregation and genome destruction|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311379|||http://purl.uniprot.org/annotation/PRO_0000311380|||http://purl.uniprot.org/annotation/PRO_0000311381|||http://purl.uniprot.org/annotation/VAR_037236|||http://purl.uniprot.org/annotation/VAR_037237|||http://purl.uniprot.org/annotation/VAR_050023|||http://purl.uniprot.org/annotation/VSP_056043
http://togogenome.org/gene/9606:RPRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||CID|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Regulation of nuclear pre-mRNA domain-containing protein 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244355|||http://purl.uniprot.org/annotation/VAR_061700|||http://purl.uniprot.org/annotation/VSP_019546|||http://purl.uniprot.org/annotation/VSP_019547|||http://purl.uniprot.org/annotation/VSP_035574|||http://purl.uniprot.org/annotation/VSP_035575|||http://purl.uniprot.org/annotation/VSP_053733|||http://purl.uniprot.org/annotation/VSP_053734
http://togogenome.org/gene/9606:AVEN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cell death regulator Aven|||Disordered|||N6-methyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064768|||http://purl.uniprot.org/annotation/VAR_020144
http://togogenome.org/gene/9606:MYDGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969H8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Increased secretion.|||Myeloid-derived growth factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021008|||http://purl.uniprot.org/annotation/VAR_060183
http://togogenome.org/gene/9606:ST8SIA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92187                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149293|||http://purl.uniprot.org/annotation/VAR_036169|||http://purl.uniprot.org/annotation/VAR_068976|||http://purl.uniprot.org/annotation/VSP_044867
http://togogenome.org/gene/9606:PPTC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI37                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||PPM-type phosphatase|||Protein phosphatase PTC7 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328745
http://togogenome.org/gene/9606:FOXC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12948|||http://purl.uniprot.org/uniprot/W6CJ52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity.|||Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity.|||Decreased protein stability. Decreased transcriptional activity.|||Decreased protein stability. No effect on transcriptional activity.|||Disordered|||Fork-head|||Forkhead box protein C1|||In ASGD3 and RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In ASGD3 and RIEG3; with glaucoma; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In ASGD3.|||In ASGD3; no change in protein abundance; changed post-translational phosphorylation; changed protein structure; decreased location at the nucleus; novel location at the cytoplasm; increased protein aggregation, aggregation do not correspond to microtubule-dependent inclusion bodies; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity.|||In ASGD3; no effect on protein abundance; increased protein stability; no effect on nuclear location; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3 and ASGD3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3 and ASGD3; with glaucoma; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3.|||In RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity; no change on DNA bending activity.|||In RIEG3; decreased protein abundance; decreased protein stability; decreased location at nucleus; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity.|||In RIEG3; hypomorphic mutation; decreased protein abundance; decreased protein stability; changed post-translational phosphorylation; decreased location at the nucleus; novel location at the cytoplasm; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; loss of protein stability.|||In RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; no change in location at the nucleus; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; no effect on protein abundance; changed post-translational phosphorylation; novel location at aggresome, aggregation correspond to microtubule-dependent inclusion bodies; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; no effect on protein abundance; increased protein stability; decreased location at nucleus; loss of transcription regulatory region DNA binding; loss of sequence-specific DNA binding transcription factor activity.|||In RIEG3; no effect on protein abundance; no effect on protein stability; no effect on location at nucleus; no effect on transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity.|||In RIEG3; unknown pathological significance.|||Loss of protein stability.|||No effect on protein abundance; no effect on protein stability; no effect on nuclear location; no effect on transcription regulatory region DNA binding; no effect on sequence-specific DNA binding transcription factor activity.|||No effect on protein stability. No effect on transcriptional activity.|||Nuclear localization signal 1 (NLS 1)|||Nuclear localization signal 2 (NLS 2)|||Phosphoserine|||Polar residues|||Pro residues|||Required for transcriptional activation|||Required for transcriptional inhibition|||Severely disrupts the protein function. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091806|||http://purl.uniprot.org/annotation/VAR_007815|||http://purl.uniprot.org/annotation/VAR_007816|||http://purl.uniprot.org/annotation/VAR_007817|||http://purl.uniprot.org/annotation/VAR_007944|||http://purl.uniprot.org/annotation/VAR_007945|||http://purl.uniprot.org/annotation/VAR_018150|||http://purl.uniprot.org/annotation/VAR_058722|||http://purl.uniprot.org/annotation/VAR_058723|||http://purl.uniprot.org/annotation/VAR_058724|||http://purl.uniprot.org/annotation/VAR_058725|||http://purl.uniprot.org/annotation/VAR_058726|||http://purl.uniprot.org/annotation/VAR_058727|||http://purl.uniprot.org/annotation/VAR_058728|||http://purl.uniprot.org/annotation/VAR_058729|||http://purl.uniprot.org/annotation/VAR_058730|||http://purl.uniprot.org/annotation/VAR_058731|||http://purl.uniprot.org/annotation/VAR_058732|||http://purl.uniprot.org/annotation/VAR_058733|||http://purl.uniprot.org/annotation/VAR_058734|||http://purl.uniprot.org/annotation/VAR_078501|||http://purl.uniprot.org/annotation/VAR_078502|||http://purl.uniprot.org/annotation/VAR_078503|||http://purl.uniprot.org/annotation/VAR_078504|||http://purl.uniprot.org/annotation/VAR_078505|||http://purl.uniprot.org/annotation/VAR_078506|||http://purl.uniprot.org/annotation/VAR_078507|||http://purl.uniprot.org/annotation/VAR_078508|||http://purl.uniprot.org/annotation/VAR_078509|||http://purl.uniprot.org/annotation/VAR_078510|||http://purl.uniprot.org/annotation/VAR_078511|||http://purl.uniprot.org/annotation/VAR_078512
http://togogenome.org/gene/9606:PRNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F7VJQ1|||http://purl.uniprot.org/uniprot/P04156|||http://purl.uniprot.org/uniprot/Q53YK7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 8 AA tandem repeats of P-H-G-G-G-W-G-Q|||Alternative prion protein|||Confers relative protection against acquired, sporadic and some inherited prion diseases in the heterozygous state, possibly by preventing homodimerization; determines the disease phenotype in patients who have a PrP mutation at position 178; patients with M-129 develop FFI, those with V-129 develop CJD.|||Confers relative protection against sporadic Creutzfeldt-Jakob disease (CJD) in the heterozygous state.|||Disordered|||GPI-anchor amidated serine|||Helical|||In CJD.|||In CJD; unknown pathological significance.|||In FFI and CJD.|||In GSD and early-onset dementia.|||In GSD.|||In GSD; atypical form with neurofibrillary tangles.|||In GSD; with neurofibrillary tangles.|||In SENF and early-onset dementia; induces loss of glycosylation at N-181.|||In early-onset dementia; dementia associated to prion diseases.|||In schizoaffective disorder.|||Interaction with ADGRG6|||Interaction with GRB2, ERI3 and SYN1|||Linked to development of dementing Gerstmann-Straussler disease.|||Major prion protein|||N-linked (GlcNAc...) asparagine|||Prion/Doppel protein beta-ribbon|||Removed in mature form|||Variant that has been selected for in response to the Kuru epidemic and confers resistance to prion disease by acting as a 'dominant negative' inhibitor of prion conversion; is not only itself resistant to conformational conversion, but also inhibits conversion of wild-type proteins; confers protection against classical Creutzfeldt-Jakob disease (CJD) and Kuru in the heterozygous state, but can be infected with variant CJD prions, resulting from exposure to bovine spongiform encephalopathy prions; confers complete resistance to all prion strains when homozygous. Always associated with M-129 variant.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025675|||http://purl.uniprot.org/annotation/PRO_0000025676|||http://purl.uniprot.org/annotation/PRO_0000420424|||http://purl.uniprot.org/annotation/PRO_5014309518|||http://purl.uniprot.org/annotation/VAR_006464|||http://purl.uniprot.org/annotation/VAR_006465|||http://purl.uniprot.org/annotation/VAR_006466|||http://purl.uniprot.org/annotation/VAR_006467|||http://purl.uniprot.org/annotation/VAR_006468|||http://purl.uniprot.org/annotation/VAR_006469|||http://purl.uniprot.org/annotation/VAR_006470|||http://purl.uniprot.org/annotation/VAR_006471|||http://purl.uniprot.org/annotation/VAR_006472|||http://purl.uniprot.org/annotation/VAR_006473|||http://purl.uniprot.org/annotation/VAR_006474|||http://purl.uniprot.org/annotation/VAR_006475|||http://purl.uniprot.org/annotation/VAR_006476|||http://purl.uniprot.org/annotation/VAR_006477|||http://purl.uniprot.org/annotation/VAR_006478|||http://purl.uniprot.org/annotation/VAR_008746|||http://purl.uniprot.org/annotation/VAR_008747|||http://purl.uniprot.org/annotation/VAR_008748|||http://purl.uniprot.org/annotation/VAR_008749|||http://purl.uniprot.org/annotation/VAR_008750|||http://purl.uniprot.org/annotation/VAR_008751|||http://purl.uniprot.org/annotation/VAR_008752|||http://purl.uniprot.org/annotation/VAR_008753|||http://purl.uniprot.org/annotation/VAR_008754|||http://purl.uniprot.org/annotation/VAR_013763|||http://purl.uniprot.org/annotation/VAR_014264|||http://purl.uniprot.org/annotation/VAR_073722
http://togogenome.org/gene/9606:MYL12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14950                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin regulatory light chain 12B|||Phosphoserine; by MLCK and ZIPK/DAPK3|||Phosphothreonine; by MLCK and ZIPK/DAPK3|||Shows a decrease in the number of actin filament bundles.|||Shows a larger number of actin filament bundles.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349364|||http://purl.uniprot.org/annotation/VAR_046371
http://togogenome.org/gene/9606:ZBTB39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15060                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Pro residues|||Zinc finger and BTB domain-containing protein 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047744|||http://purl.uniprot.org/annotation/VAR_019985
http://togogenome.org/gene/9606:WARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGM6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In NEMMLAS and PKDYS3.|||In NEMMLAS and PKDYS3; hypomorphic variant, clinically relevant when present in trans with an amorphic variant; impaired mitochondrial localization.|||In NEMMLAS.|||In NEMMLAS; unknown pathological significance.|||In PKDYS3.|||In isoform 2.|||Mitochondrion|||Tryptophan--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035828|||http://purl.uniprot.org/annotation/VAR_020217|||http://purl.uniprot.org/annotation/VAR_028848|||http://purl.uniprot.org/annotation/VAR_052407|||http://purl.uniprot.org/annotation/VAR_078435|||http://purl.uniprot.org/annotation/VAR_079734|||http://purl.uniprot.org/annotation/VAR_079735|||http://purl.uniprot.org/annotation/VAR_079736|||http://purl.uniprot.org/annotation/VAR_079737|||http://purl.uniprot.org/annotation/VAR_079738|||http://purl.uniprot.org/annotation/VAR_079739|||http://purl.uniprot.org/annotation/VAR_079740|||http://purl.uniprot.org/annotation/VAR_086908|||http://purl.uniprot.org/annotation/VAR_086909|||http://purl.uniprot.org/annotation/VAR_086910|||http://purl.uniprot.org/annotation/VAR_086911|||http://purl.uniprot.org/annotation/VSP_041414|||http://purl.uniprot.org/annotation/VSP_041415
http://togogenome.org/gene/9606:ZNF443                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2A4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 443                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047592|||http://purl.uniprot.org/annotation/VAR_057420|||http://purl.uniprot.org/annotation/VAR_059917|||http://purl.uniprot.org/annotation/VAR_059918|||http://purl.uniprot.org/annotation/VAR_061947|||http://purl.uniprot.org/annotation/VAR_061948
http://togogenome.org/gene/9606:PDLIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYF8|||http://purl.uniprot.org/uniprot/A0A2U3TZH4|||http://purl.uniprot.org/uniprot/Q53GG5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||LIM zinc-binding|||PDZ|||PDZ and LIM domain protein 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075867|||http://purl.uniprot.org/annotation/VAR_050166|||http://purl.uniprot.org/annotation/VSP_016500|||http://purl.uniprot.org/annotation/VSP_016501|||http://purl.uniprot.org/annotation/VSP_016502
http://togogenome.org/gene/9606:GGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-binding protein GGA2|||Disordered|||GAE|||GAT|||Partial loss of clathrin-binding.|||Phosphoserine|||Polar residues|||Unstructured hinge|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212682|||http://purl.uniprot.org/annotation/VAR_028275
http://togogenome.org/gene/9606:LGR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBX8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a colorectal cancer sample; somatic mutation; no effect Wnt signlaing upon RSPO1-binding.|||In isoform 1.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||Leucine-rich repeat-containing G-protein coupled receptor 6|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069699|||http://purl.uniprot.org/annotation/VAR_033479|||http://purl.uniprot.org/annotation/VAR_035762|||http://purl.uniprot.org/annotation/VAR_035763|||http://purl.uniprot.org/annotation/VAR_049413|||http://purl.uniprot.org/annotation/VAR_059324|||http://purl.uniprot.org/annotation/VSP_013596|||http://purl.uniprot.org/annotation/VSP_028006|||http://purl.uniprot.org/annotation/VSP_028007
http://togogenome.org/gene/9606:SUPT3H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75486                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Transcription initiation protein SPT3 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072313|||http://purl.uniprot.org/annotation/VAR_057000|||http://purl.uniprot.org/annotation/VSP_059496
http://togogenome.org/gene/9606:RSRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L4I2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arginine/serine-rich coiled-coil protein 2|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314937|||http://purl.uniprot.org/annotation/VAR_038133|||http://purl.uniprot.org/annotation/VSP_030440
http://togogenome.org/gene/9606:CDX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99626                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  4S motif; modulates transactivation activity and protein stability|||Disordered|||Homeobox|||Homeobox protein CDX-2|||Interaction with 5-mCpG DNA|||Interaction with DNA|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048849|||http://purl.uniprot.org/annotation/VAR_014530
http://togogenome.org/gene/9606:TMC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BNW8|||http://purl.uniprot.org/uniprot/Q7Z402                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TMC|||Transmembrane channel-like protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287165|||http://purl.uniprot.org/annotation/VAR_032278|||http://purl.uniprot.org/annotation/VAR_032279|||http://purl.uniprot.org/annotation/VAR_032280|||http://purl.uniprot.org/annotation/VAR_061852|||http://purl.uniprot.org/annotation/VSP_054226
http://togogenome.org/gene/9606:A2M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01023                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-2-macroglobulin|||Bait region|||Inhibitory|||Interchain (with C-278)|||Interchain (with C-431)|||Isoglutamyl cysteine thioester (Cys-Gln)|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-? in other proteins)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Probably interferes with the activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000055|||http://purl.uniprot.org/annotation/VAR_000012|||http://purl.uniprot.org/annotation/VAR_000013|||http://purl.uniprot.org/annotation/VAR_000014|||http://purl.uniprot.org/annotation/VAR_026820|||http://purl.uniprot.org/annotation/VAR_026821
http://togogenome.org/gene/9606:HSD3B7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2F3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  3 beta-hydroxysteroid dehydrogenase type 7|||Helical|||In CBAS1.|||In CBAS1; loss of activity.|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087791|||http://purl.uniprot.org/annotation/VAR_031040|||http://purl.uniprot.org/annotation/VAR_048100|||http://purl.uniprot.org/annotation/VAR_054775|||http://purl.uniprot.org/annotation/VAR_054776|||http://purl.uniprot.org/annotation/VSP_042658
http://togogenome.org/gene/9606:ARHGAP36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRI8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Rho GTPase-activating protein 36|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256699|||http://purl.uniprot.org/annotation/VSP_021357|||http://purl.uniprot.org/annotation/VSP_021358|||http://purl.uniprot.org/annotation/VSP_039235|||http://purl.uniprot.org/annotation/VSP_039236
http://togogenome.org/gene/9606:C11orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7L8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||Uncharacterized protein C11orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320641|||http://purl.uniprot.org/annotation/VAR_039242|||http://purl.uniprot.org/annotation/VAR_039243|||http://purl.uniprot.org/annotation/VAR_039244|||http://purl.uniprot.org/annotation/VAR_039245|||http://purl.uniprot.org/annotation/VAR_039246|||http://purl.uniprot.org/annotation/VAR_039247
http://togogenome.org/gene/9606:LPIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQK8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-LIP|||DXDXT motif|||Disordered|||In isoform 2.|||LXXIL motif|||N-LIP|||Nuclear localization signal|||Phosphatidate phosphatase LPIN3|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209883|||http://purl.uniprot.org/annotation/VAR_053489|||http://purl.uniprot.org/annotation/VSP_036885
http://togogenome.org/gene/9606:FKBP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W6G9|||http://purl.uniprot.org/uniprot/P68106                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075295|||http://purl.uniprot.org/annotation/VSP_005184
http://togogenome.org/gene/9606:FAM181B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEQ2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein FAM181B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324302|||http://purl.uniprot.org/annotation/VAR_039694|||http://purl.uniprot.org/annotation/VAR_039695
http://togogenome.org/gene/9606:ATP11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKX1|||http://purl.uniprot.org/uniprot/B4E3T1|||http://purl.uniprot.org/uniprot/Q9Y2G3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Extracellular|||Helical|||Impairs ATPase activity.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase IF|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046371
http://togogenome.org/gene/9606:PRAMEF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60809                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156984|||http://purl.uniprot.org/annotation/VAR_029104|||http://purl.uniprot.org/annotation/VAR_029105|||http://purl.uniprot.org/annotation/VAR_029106|||http://purl.uniprot.org/annotation/VAR_029107
http://togogenome.org/gene/9606:RPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15880                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ubiquitination and degradation by RNF10.|||Disordered|||Does not affect readthrough on the poly(A)-stall sequences; when associated with R-275.|||Does not affect readthrough on the poly(A)-stall sequences; when associated with R-58.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||S5 DRBM|||Small ribosomal subunit protein uS5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131673
http://togogenome.org/gene/9606:OR52K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK8|||http://purl.uniprot.org/uniprot/Q8NGK3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52K2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150782|||http://purl.uniprot.org/annotation/VAR_034347|||http://purl.uniprot.org/annotation/VAR_034348|||http://purl.uniprot.org/annotation/VAR_047827
http://togogenome.org/gene/9606:KLF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13351                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Found in a patient with autosomal recessive microcytic hypochromic anemia and increased fetal hemoglobin; unknown pathological significance; no effect on protein abundance; no effect on protein localization; decreased transcriptional activity.|||Found in a patient with autosomal recessive microcytic hypochromic anemia and increased fetal hemoglobin; with microcytic hypochromic anemia; no effect on protein abundance; no effect on protein localization; decreased transcriptional activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In CDAN4; has a dominant-negative effect on the transcriptional activation of CD44 and AQP1 promoters.|||In blood group-In(Lu).|||Krueppel-like factor 1|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphothreonine; by CK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047160|||http://purl.uniprot.org/annotation/VAR_043981|||http://purl.uniprot.org/annotation/VAR_043982|||http://purl.uniprot.org/annotation/VAR_058108|||http://purl.uniprot.org/annotation/VAR_058109|||http://purl.uniprot.org/annotation/VAR_058110|||http://purl.uniprot.org/annotation/VAR_058111|||http://purl.uniprot.org/annotation/VAR_064901|||http://purl.uniprot.org/annotation/VAR_072737|||http://purl.uniprot.org/annotation/VAR_072738|||http://purl.uniprot.org/annotation/VAR_074272|||http://purl.uniprot.org/annotation/VAR_074273|||http://purl.uniprot.org/annotation/VAR_074274|||http://purl.uniprot.org/annotation/VAR_074275|||http://purl.uniprot.org/annotation/VAR_074276
http://togogenome.org/gene/9606:MYO10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD67                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Abolishes interaction with CALM3.|||Abolishes interaction with DCC.|||Abolishes interaction with tubulin; when associated with D-1647.|||Abolishes interaction with tubulin; when associated with D-1650.|||Actin-binding|||Almost abolishes interaction with DCC.|||Basic and acidic residues|||Disordered|||FERM|||IQ 1|||IQ 2|||IQ 3|||In isoform 2.|||In isoform Headless.|||MyTH4|||Myosin motor|||N-acetylmethionine|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAH|||Unconventional myosin-X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123473|||http://purl.uniprot.org/annotation/VAR_046328|||http://purl.uniprot.org/annotation/VAR_046329|||http://purl.uniprot.org/annotation/VAR_046330|||http://purl.uniprot.org/annotation/VAR_046331|||http://purl.uniprot.org/annotation/VAR_046332|||http://purl.uniprot.org/annotation/VAR_061366|||http://purl.uniprot.org/annotation/VSP_054975|||http://purl.uniprot.org/annotation/VSP_054976|||http://purl.uniprot.org/annotation/VSP_054977
http://togogenome.org/gene/9606:MROH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGP6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In isoform 2.|||Maestro heat-like repeat-containing protein family member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285028|||http://purl.uniprot.org/annotation/VAR_031903|||http://purl.uniprot.org/annotation/VAR_031904|||http://purl.uniprot.org/annotation/VAR_031905|||http://purl.uniprot.org/annotation/VSP_047654
http://togogenome.org/gene/9606:ALS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4R4|||http://purl.uniprot.org/uniprot/Q96Q42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alsin|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||MORN 1|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphothreonine|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080903|||http://purl.uniprot.org/annotation/VAR_015655|||http://purl.uniprot.org/annotation/VAR_015656|||http://purl.uniprot.org/annotation/VAR_015657|||http://purl.uniprot.org/annotation/VAR_036747|||http://purl.uniprot.org/annotation/VAR_036748|||http://purl.uniprot.org/annotation/VAR_036749|||http://purl.uniprot.org/annotation/VSP_050521|||http://purl.uniprot.org/annotation/VSP_050522|||http://purl.uniprot.org/annotation/VSP_050523|||http://purl.uniprot.org/annotation/VSP_050524
http://togogenome.org/gene/9606:GATAD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXI9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CR1; interaction with MBD2 and MBD3|||CR2; histone tail-binding|||Disordered|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Transcriptional repressor p66-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083502|||http://purl.uniprot.org/annotation/VAR_069363|||http://purl.uniprot.org/annotation/VAR_069364
http://togogenome.org/gene/9606:ARFGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9L0|||http://purl.uniprot.org/uniprot/Q8N6H7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosylation factor GTPase-activating protein 2|||Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Required for interaction with coatomer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278468|||http://purl.uniprot.org/annotation/VAR_030780|||http://purl.uniprot.org/annotation/VAR_048321|||http://purl.uniprot.org/annotation/VAR_048322|||http://purl.uniprot.org/annotation/VAR_048323|||http://purl.uniprot.org/annotation/VSP_056054|||http://purl.uniprot.org/annotation/VSP_056055|||http://purl.uniprot.org/annotation/VSP_056056
http://togogenome.org/gene/9606:SLC22A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R807|||http://purl.uniprot.org/uniprot/Q8TCC7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of function.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In 3.5% of Asian-American; reduced function.|||In 6% of African-Americans.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Organic anion transporter 3|||Phosphoserine|||Reduced function.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273439|||http://purl.uniprot.org/annotation/VAR_030146|||http://purl.uniprot.org/annotation/VAR_030147|||http://purl.uniprot.org/annotation/VAR_030148|||http://purl.uniprot.org/annotation/VAR_030149|||http://purl.uniprot.org/annotation/VAR_030150|||http://purl.uniprot.org/annotation/VAR_030151|||http://purl.uniprot.org/annotation/VAR_030152|||http://purl.uniprot.org/annotation/VAR_030153|||http://purl.uniprot.org/annotation/VSP_022562|||http://purl.uniprot.org/annotation/VSP_022563|||http://purl.uniprot.org/annotation/VSP_022564|||http://purl.uniprot.org/annotation/VSP_022565|||http://purl.uniprot.org/annotation/VSP_045272|||http://purl.uniprot.org/annotation/VSP_045824
http://togogenome.org/gene/9606:PKDREJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||PLAT|||Polar residues|||Polycystin family receptor for egg jelly|||REJ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024299|||http://purl.uniprot.org/annotation/VAR_034386|||http://purl.uniprot.org/annotation/VAR_036573|||http://purl.uniprot.org/annotation/VAR_036574|||http://purl.uniprot.org/annotation/VAR_050544|||http://purl.uniprot.org/annotation/VAR_050545|||http://purl.uniprot.org/annotation/VAR_050546|||http://purl.uniprot.org/annotation/VAR_050547|||http://purl.uniprot.org/annotation/VAR_050548|||http://purl.uniprot.org/annotation/VAR_050549|||http://purl.uniprot.org/annotation/VAR_050550|||http://purl.uniprot.org/annotation/VAR_050551|||http://purl.uniprot.org/annotation/VAR_059550
http://togogenome.org/gene/9606:ZNF846                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q147U1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 846                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332245|||http://purl.uniprot.org/annotation/VAR_052911|||http://purl.uniprot.org/annotation/VAR_052912|||http://purl.uniprot.org/annotation/VSP_033362|||http://purl.uniprot.org/annotation/VSP_033363
http://togogenome.org/gene/9606:HDDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4P3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abrogates ppGpp hydrolase activity.|||Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1|||HD|||In isoform 2.|||N-acetylglycine|||N6-acetyllysine|||Nucleophile|||Reduces ppGpp hydrolase activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263110|||http://purl.uniprot.org/annotation/VSP_021866|||http://purl.uniprot.org/annotation/VSP_021867
http://togogenome.org/gene/9606:DNMT3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG02|||http://purl.uniprot.org/uniprot/F8WE91|||http://purl.uniprot.org/uniprot/Q59HC6|||http://purl.uniprot.org/uniprot/Q9Y6K1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ADD|||Basic and acidic residues|||DNA (cytosine-5)-methyltransferase 3A|||Disordered|||GATA-type; atypical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HESJAS; changed DNA methylation; results in aberrant expression of genes involved in developmental processes.|||In HESJAS; no effect on protein expression; changed DNA methylation; results in aberrant expression of genes involved in developmental processes.|||In TBRS and AML; somatic variant in AML.|||In TBRS; somatic mutation.|||In TBRS; unknown pathological significance.|||In a patient with chronic myelomonocytic leukemia.|||In a patient with chronic myelomonocytic leukemia; somatic mutation.|||In isoform 2.|||In isoform 3.|||Interaction with DNMT1 and DNMT3B|||Interaction with the PRC2/EED-EZH2 complex|||Loss of activity due to the incapacity to bind the regulatory subunit DNMT3L.|||Omega-N-methylarginine|||PHD-type|||PHD-type; atypical|||PWWP|||Phosphoserine|||Phosphothreonine|||Pro residues|||S-methylcysteine; by autocatalysis|||SAM-dependent MTase C5-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088043|||http://purl.uniprot.org/annotation/VAR_067234|||http://purl.uniprot.org/annotation/VAR_067235|||http://purl.uniprot.org/annotation/VAR_067236|||http://purl.uniprot.org/annotation/VAR_067237|||http://purl.uniprot.org/annotation/VAR_067238|||http://purl.uniprot.org/annotation/VAR_071463|||http://purl.uniprot.org/annotation/VAR_071464|||http://purl.uniprot.org/annotation/VAR_071465|||http://purl.uniprot.org/annotation/VAR_071466|||http://purl.uniprot.org/annotation/VAR_071467|||http://purl.uniprot.org/annotation/VAR_071468|||http://purl.uniprot.org/annotation/VAR_071469|||http://purl.uniprot.org/annotation/VAR_071470|||http://purl.uniprot.org/annotation/VAR_071471|||http://purl.uniprot.org/annotation/VAR_071472|||http://purl.uniprot.org/annotation/VAR_077522|||http://purl.uniprot.org/annotation/VAR_077523|||http://purl.uniprot.org/annotation/VAR_077524|||http://purl.uniprot.org/annotation/VAR_077525|||http://purl.uniprot.org/annotation/VAR_083539|||http://purl.uniprot.org/annotation/VAR_083540|||http://purl.uniprot.org/annotation/VSP_040998|||http://purl.uniprot.org/annotation/VSP_040999|||http://purl.uniprot.org/annotation/VSP_046254
http://togogenome.org/gene/9606:LDHD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WU2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAD-binding PCMH-type|||In DLACD; probable enzymatic loss-of-function; contrary to the wild-type protein, unable to restore basal D-lactate levels when tested in knockout zebrafish model.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Probable D-lactate dehydrogenase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262952|||http://purl.uniprot.org/annotation/VAR_029561|||http://purl.uniprot.org/annotation/VAR_082214|||http://purl.uniprot.org/annotation/VAR_082215|||http://purl.uniprot.org/annotation/VSP_052253
http://togogenome.org/gene/9606:STN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H668                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CST complex subunit STN1|||Defective of TEN1 binding; when associated with Ala-164 or Ala-167.|||Defective of TEN1 binding; when associated with Ala-78.|||In CRMCC2.|||Interaction with CTC1|||OB|||Winged helix-turn-helix (wHTH) 1|||Winged helix-turn-helix (wHTH) 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058020|||http://purl.uniprot.org/annotation/VAR_022364|||http://purl.uniprot.org/annotation/VAR_022365|||http://purl.uniprot.org/annotation/VAR_078499|||http://purl.uniprot.org/annotation/VAR_078500
http://togogenome.org/gene/9606:SNRPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JVQ0|||http://purl.uniprot.org/uniprot/F5H013|||http://purl.uniprot.org/uniprot/P62308|||http://purl.uniprot.org/uniprot/Q49AN9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Sm|||Small nuclear ribonucleoprotein G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125545
http://togogenome.org/gene/9606:CHST6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 6|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In MCD.|||In MCD; abolishes ability to sulfate keratan.|||In MCD; abolishes the ability to sulfate keratan.|||In MCD; unknown pathological significance.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085197|||http://purl.uniprot.org/annotation/VAR_021417|||http://purl.uniprot.org/annotation/VAR_021418|||http://purl.uniprot.org/annotation/VAR_021419|||http://purl.uniprot.org/annotation/VAR_021420|||http://purl.uniprot.org/annotation/VAR_021421|||http://purl.uniprot.org/annotation/VAR_021422|||http://purl.uniprot.org/annotation/VAR_021423|||http://purl.uniprot.org/annotation/VAR_021424|||http://purl.uniprot.org/annotation/VAR_021425|||http://purl.uniprot.org/annotation/VAR_021426|||http://purl.uniprot.org/annotation/VAR_021427|||http://purl.uniprot.org/annotation/VAR_021428|||http://purl.uniprot.org/annotation/VAR_021429|||http://purl.uniprot.org/annotation/VAR_021430|||http://purl.uniprot.org/annotation/VAR_021431|||http://purl.uniprot.org/annotation/VAR_021432|||http://purl.uniprot.org/annotation/VAR_021433|||http://purl.uniprot.org/annotation/VAR_021434|||http://purl.uniprot.org/annotation/VAR_021435|||http://purl.uniprot.org/annotation/VAR_021436|||http://purl.uniprot.org/annotation/VAR_021437|||http://purl.uniprot.org/annotation/VAR_021438|||http://purl.uniprot.org/annotation/VAR_021439|||http://purl.uniprot.org/annotation/VAR_021440|||http://purl.uniprot.org/annotation/VAR_021441|||http://purl.uniprot.org/annotation/VAR_021442|||http://purl.uniprot.org/annotation/VAR_021443|||http://purl.uniprot.org/annotation/VAR_021444|||http://purl.uniprot.org/annotation/VAR_021445|||http://purl.uniprot.org/annotation/VAR_021446|||http://purl.uniprot.org/annotation/VAR_021447|||http://purl.uniprot.org/annotation/VAR_021448|||http://purl.uniprot.org/annotation/VAR_021449|||http://purl.uniprot.org/annotation/VAR_021450|||http://purl.uniprot.org/annotation/VAR_021451|||http://purl.uniprot.org/annotation/VAR_021452|||http://purl.uniprot.org/annotation/VAR_021453|||http://purl.uniprot.org/annotation/VAR_021454|||http://purl.uniprot.org/annotation/VAR_021455|||http://purl.uniprot.org/annotation/VAR_021456|||http://purl.uniprot.org/annotation/VAR_021457|||http://purl.uniprot.org/annotation/VAR_021458|||http://purl.uniprot.org/annotation/VAR_021459|||http://purl.uniprot.org/annotation/VAR_021460|||http://purl.uniprot.org/annotation/VAR_021461|||http://purl.uniprot.org/annotation/VAR_021462|||http://purl.uniprot.org/annotation/VAR_021463|||http://purl.uniprot.org/annotation/VAR_021464|||http://purl.uniprot.org/annotation/VAR_021465|||http://purl.uniprot.org/annotation/VAR_021466|||http://purl.uniprot.org/annotation/VAR_021467|||http://purl.uniprot.org/annotation/VAR_021468|||http://purl.uniprot.org/annotation/VAR_021469|||http://purl.uniprot.org/annotation/VAR_033735|||http://purl.uniprot.org/annotation/VAR_075522|||http://purl.uniprot.org/annotation/VAR_075523|||http://purl.uniprot.org/annotation/VAR_075524|||http://purl.uniprot.org/annotation/VAR_075525|||http://purl.uniprot.org/annotation/VAR_075526|||http://purl.uniprot.org/annotation/VAR_075527
http://togogenome.org/gene/9606:ZDHHC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y397                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes palmitoyltransferase activity.|||Cytoplasmic|||DHHC|||Disordered|||Helical|||In MRXSR.|||Lumenal|||Palmitoyltransferase ZDHHC9|||Polar residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212880|||http://purl.uniprot.org/annotation/VAR_062674|||http://purl.uniprot.org/annotation/VAR_062675
http://togogenome.org/gene/9606:CAPNS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ5|||http://purl.uniprot.org/uniprot/P04632                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calpain small subunit 1|||EF-hand|||EF-hand 1; atypical|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073713|||http://purl.uniprot.org/annotation/VAR_021089
http://togogenome.org/gene/9606:TMEM186                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B77                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 186                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279439
http://togogenome.org/gene/9606:PTPN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06124                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphatase activity. Enhances interaction with NEDD9.|||Disordered|||In JMML.|||In JMML; also in myelodysplastic syndrome.|||In JMML; increases protein tyrosine phosphatase activity against CDC73.|||In LPRD1.|||In LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73.|||In LPRD1; reduced phosphatase activity.|||In NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis.|||In NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73.|||In NS1.|||In NS1; also found in myelodysplastic syndrome.|||In NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia.|||In NS1; common mutation.|||In NS1; increased phosphatase activity.|||In NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity.|||In NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1.|||In NS1; some patients also manifest giant cell lesions of bone and soft tissue.|||In NS1; unknown pathological significance.|||In acute myeloid leukemia; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3.|||In myelodysplastic syndrome.|||N-acetylthreonine|||Phosphocysteine intermediate|||Phosphotyrosine|||Phosphotyrosine; by PDGFR|||Removed|||SH2 1|||SH2 2|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094767|||http://purl.uniprot.org/annotation/VAR_015601|||http://purl.uniprot.org/annotation/VAR_015602|||http://purl.uniprot.org/annotation/VAR_015603|||http://purl.uniprot.org/annotation/VAR_015604|||http://purl.uniprot.org/annotation/VAR_015605|||http://purl.uniprot.org/annotation/VAR_015606|||http://purl.uniprot.org/annotation/VAR_015607|||http://purl.uniprot.org/annotation/VAR_015608|||http://purl.uniprot.org/annotation/VAR_015609|||http://purl.uniprot.org/annotation/VAR_015610|||http://purl.uniprot.org/annotation/VAR_015611|||http://purl.uniprot.org/annotation/VAR_015612|||http://purl.uniprot.org/annotation/VAR_015613|||http://purl.uniprot.org/annotation/VAR_015614|||http://purl.uniprot.org/annotation/VAR_015615|||http://purl.uniprot.org/annotation/VAR_015616|||http://purl.uniprot.org/annotation/VAR_015617|||http://purl.uniprot.org/annotation/VAR_015618|||http://purl.uniprot.org/annotation/VAR_015619|||http://purl.uniprot.org/annotation/VAR_015620|||http://purl.uniprot.org/annotation/VAR_015621|||http://purl.uniprot.org/annotation/VAR_015622|||http://purl.uniprot.org/annotation/VAR_015623|||http://purl.uniprot.org/annotation/VAR_015624|||http://purl.uniprot.org/annotation/VAR_015990|||http://purl.uniprot.org/annotation/VAR_015991|||http://purl.uniprot.org/annotation/VAR_015992|||http://purl.uniprot.org/annotation/VAR_015993|||http://purl.uniprot.org/annotation/VAR_015994|||http://purl.uniprot.org/annotation/VAR_015995|||http://purl.uniprot.org/annotation/VAR_015996|||http://purl.uniprot.org/annotation/VAR_015997|||http://purl.uniprot.org/annotation/VAR_015998|||http://purl.uniprot.org/annotation/VAR_015999|||http://purl.uniprot.org/annotation/VAR_016000|||http://purl.uniprot.org/annotation/VAR_016001|||http://purl.uniprot.org/annotation/VAR_016002|||http://purl.uniprot.org/annotation/VAR_016003|||http://purl.uniprot.org/annotation/VAR_027183|||http://purl.uniprot.org/annotation/VAR_027184|||http://purl.uniprot.org/annotation/VAR_027185|||http://purl.uniprot.org/annotation/VAR_027186|||http://purl.uniprot.org/annotation/VAR_027187|||http://purl.uniprot.org/annotation/VAR_027188|||http://purl.uniprot.org/annotation/VAR_027189|||http://purl.uniprot.org/annotation/VAR_027190|||http://purl.uniprot.org/annotation/VAR_027191|||http://purl.uniprot.org/annotation/VAR_027192|||http://purl.uniprot.org/annotation/VAR_027193|||http://purl.uniprot.org/annotation/VAR_027194|||http://purl.uniprot.org/annotation/VAR_027195|||http://purl.uniprot.org/annotation/VAR_027196|||http://purl.uniprot.org/annotation/VAR_027197|||http://purl.uniprot.org/annotation/VAR_066060|||http://purl.uniprot.org/annotation/VAR_071706|||http://purl.uniprot.org/annotation/VAR_076499|||http://purl.uniprot.org/annotation/VAR_078101|||http://purl.uniprot.org/annotation/VAR_078102|||http://purl.uniprot.org/annotation/VAR_078103|||http://purl.uniprot.org/annotation/VAR_078104|||http://purl.uniprot.org/annotation/VAR_078105|||http://purl.uniprot.org/annotation/VSP_060437|||http://purl.uniprot.org/annotation/VSP_060438|||http://purl.uniprot.org/annotation/VSP_060439
http://togogenome.org/gene/9606:NEFM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07197|||http://purl.uniprot.org/uniprot/Q9UK51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 13 AA approximate tandem repeats of K-S-P-V-[PS]-K-S-P-V-E-E-[KA]-[GAK]|||Acidic residues|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Head|||IF rod|||In isoform 2.|||Linker 1|||Linker 12|||Linker 2|||N-acetylserine|||Neurofilament medium polypeptide|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063794|||http://purl.uniprot.org/annotation/VAR_056024|||http://purl.uniprot.org/annotation/VAR_060732|||http://purl.uniprot.org/annotation/VSP_046306
http://togogenome.org/gene/9606:TRIM31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L6J1|||http://purl.uniprot.org/uniprot/Q9BZY9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity and ability to ubiquitinate MAVS.|||Abolished E3 ubiquitin-protein ligase activity and ability to ubiquitinate NLRP3; when associated with A-16.|||Abolished E3 ubiquitin-protein ligase activity and ability to ubiquitinate NLRP3; when associated with A-31.|||B box-type|||Disordered|||E3 ubiquitin-protein ligase TRIM31|||In isoform Beta.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056245|||http://purl.uniprot.org/annotation/VAR_019962|||http://purl.uniprot.org/annotation/VAR_022728|||http://purl.uniprot.org/annotation/VAR_022729|||http://purl.uniprot.org/annotation/VAR_052139|||http://purl.uniprot.org/annotation/VAR_052140|||http://purl.uniprot.org/annotation/VSP_005764|||http://purl.uniprot.org/annotation/VSP_005765
http://togogenome.org/gene/9606:IFNA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C383|||http://purl.uniprot.org/uniprot/P01567                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016364|||http://purl.uniprot.org/annotation/PRO_5030724927
http://togogenome.org/gene/9606:CHST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4C5|||http://purl.uniprot.org/uniprot/V9HVX9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 2|||Cytoplasmic|||Disordered|||Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39.|||Has weak or no effect.|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Induces a strong decrease in enzyme activity.|||Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12.|||Loss of function.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect.|||Not glycosylated|||Reduced localization in the Golgi.|||Sulfotransferase|||Unable to sulfate the sialyl Lewis X tetrasaccharide.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085186|||http://purl.uniprot.org/annotation/VSP_018887
http://togogenome.org/gene/9606:MTMR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9Q7|||http://purl.uniprot.org/uniprot/B7ZAG8|||http://purl.uniprot.org/uniprot/Q9Y216                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Myotubularin phosphatase|||Myotubularin-related protein 7|||Phosphocysteine intermediate|||Phosphothreonine|||Polar residues|||Tyrosine specific protein phosphatases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094940|||http://purl.uniprot.org/annotation/VAR_057144|||http://purl.uniprot.org/annotation/VAR_059779|||http://purl.uniprot.org/annotation/VSP_017000|||http://purl.uniprot.org/annotation/VSP_017001
http://togogenome.org/gene/9606:MAMLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKM8|||http://purl.uniprot.org/uniprot/Q13495                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Mastermind-like domain-containing protein 1|||Phosphoserine|||Polar residues|||Pro residues|||Reduces transcriptional activation of the HES3 promoter.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089592|||http://purl.uniprot.org/annotation/VAR_020273|||http://purl.uniprot.org/annotation/VAR_030024|||http://purl.uniprot.org/annotation/VAR_030025|||http://purl.uniprot.org/annotation/VSP_037654|||http://purl.uniprot.org/annotation/VSP_037655
http://togogenome.org/gene/9606:ADCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TW2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  AarF domain-containing protein kinase 1|||In isoform 2.|||In isoform 3.|||No effect on role in maintaining mitochondrial structure and function.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252249|||http://purl.uniprot.org/annotation/VSP_020885|||http://purl.uniprot.org/annotation/VSP_046794
http://togogenome.org/gene/9606:INO80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes DNA-dependent ATPase and nucleosome remodeling activities.|||Assembles INO80 complex module consisting of conserved components ACTR8, ACTL6A and YY1|||Assembles INO80 complex module consisting of conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2|||Assembles INO80 complex module with putative regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1 and IN80D|||Basic and acidic residues|||Chromatin-remodeling ATPase INO80|||DBINO|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248829|||http://purl.uniprot.org/annotation/VAR_049500|||http://purl.uniprot.org/annotation/VAR_061233
http://togogenome.org/gene/9606:YBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P67809                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to C5-methylcytosine (m5C)-containing mRNAs.|||Abrogates unconventional secretion.|||Basic and acidic residues|||C5-methylcytosine binding|||CSD|||Cleavage; by 20S proteasomal protease|||Decreased binding to C5-methylcytosine (m5C)-containing mRNAs. Decreased ability to discriminate between m5C-containing and unmethylated mRNAs.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Important for C5-methylcytosine-recognition|||Interaction with ss-DNA|||Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Removed|||Y-box-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100219
http://togogenome.org/gene/9606:HNRNPU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00839|||http://purl.uniprot.org/uniprot/Q96BA7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylserine|||ATPase domain|||Acidic residues|||Actin-binding|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||B30.2/SPRY|||Basic and acidic residues|||Citrulline|||Cleavage; by CASP3|||Dimethylated arginine; in A2780 ovarian carcinoma cell line|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein U|||In DEE54.|||In DEE54; unknown pathological significance.|||In isoform 2.|||Increases mitotic chromosome misalignment and chromosome segregation defects and decreases time required to progress through mitosis.|||Loss of actin-binding.|||N-acetylserine; partial|||N6-acetyllysine|||N6-acetyllysine; alternate|||No change in interaction with AURKA, PLK1 and TPX2. Increases mitotic chromosome misalignment and chromosome segregation defects and time required to progress through mitosis.|||No cleavage by caspases during apoptosis. Inhibits CASP3-induced cleavage in vitro.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RNA-binding RGG-box|||Removed|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081872|||http://purl.uniprot.org/annotation/VAR_014712|||http://purl.uniprot.org/annotation/VAR_078622|||http://purl.uniprot.org/annotation/VAR_078623|||http://purl.uniprot.org/annotation/VSP_005846
http://togogenome.org/gene/9606:LCE2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA82                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Late cornified envelope protein 2D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235332|||http://purl.uniprot.org/annotation/VAR_053483
http://togogenome.org/gene/9606:RPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IZU8|||http://purl.uniprot.org/uniprot/C9J9T0|||http://purl.uniprot.org/uniprot/Q96AT9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters protein structure.|||Alters protein structure. Nearly abolishes enzyme activity.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||Lowers enzyme activity by 10%.|||N-acetylalanine|||Nearly abolishes enzyme activity.|||No effect on enzyme activity.|||Proton acceptor|||Proton donor|||Reduces enzyme activity by half.|||Removed|||Ribulose-phosphate 3-epimerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171587|||http://purl.uniprot.org/annotation/VSP_008317|||http://purl.uniprot.org/annotation/VSP_008318|||http://purl.uniprot.org/annotation/VSP_047117|||http://purl.uniprot.org/annotation/VSP_055265
http://togogenome.org/gene/9606:TIFAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNK6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  FHA|||TRAF-interacting protein with FHA domain-containing protein B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320692
http://togogenome.org/gene/9606:RNF32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E940|||http://purl.uniprot.org/uniprot/Q9H0A6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  IQ|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||RING finger protein 32|||RING-type|||RING-type 1; atypical|||RING-type 2; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245532|||http://purl.uniprot.org/annotation/VAR_026982|||http://purl.uniprot.org/annotation/VAR_026983|||http://purl.uniprot.org/annotation/VAR_026984|||http://purl.uniprot.org/annotation/VSP_019738|||http://purl.uniprot.org/annotation/VSP_019739|||http://purl.uniprot.org/annotation/VSP_019740|||http://purl.uniprot.org/annotation/VSP_019741|||http://purl.uniprot.org/annotation/VSP_019743|||http://purl.uniprot.org/annotation/VSP_019744
http://togogenome.org/gene/9606:LCA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDJ7|||http://purl.uniprot.org/uniprot/Q86VQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In LCA5; unknown pathological significance.|||Lebercilin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089546|||http://purl.uniprot.org/annotation/VAR_023094|||http://purl.uniprot.org/annotation/VAR_038989|||http://purl.uniprot.org/annotation/VAR_038990|||http://purl.uniprot.org/annotation/VAR_038991|||http://purl.uniprot.org/annotation/VAR_038992|||http://purl.uniprot.org/annotation/VAR_081583
http://togogenome.org/gene/9606:PALMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5E7|||http://purl.uniprot.org/uniprot/Q9NP74                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Palmdelphin|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262528|||http://purl.uniprot.org/annotation/VAR_053805|||http://purl.uniprot.org/annotation/VAR_053806|||http://purl.uniprot.org/annotation/VAR_053807|||http://purl.uniprot.org/annotation/VSP_021786|||http://purl.uniprot.org/annotation/VSP_021787
http://togogenome.org/gene/9606:ATM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13315                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with PEX5 and translocation to peroxisomes in response to reactive oxygen species (ROS).|||Activation loop|||Catalytic loop|||Decreased phosphorylation of target proteins.|||Disrupts the dimer.|||FAT|||FATC|||Found in B-cell non-Hodgkin lymphoma; unknown pathological significance.|||Found in T-prolymphocytic leukemia; unknown pathological significance.|||Found in a patient with breast cancer; unknown pathological significance.|||Found in a patient with early-onset breast cancer; unknown pathological significance.|||Found in a patient with familial breast cancer; unknown pathological significance.|||Found in a patient with familial pancreatic cancer; also found in a lung adenocarcinoma sample; unknown pathological significance; decreased phosphorylation of target proteins.|||Found in a patient with familial pancreatic cancer; unknown pathological significance.|||Found in patients with familial pancreatic cancer; also found in a lung adenocarcinoma sample; unknown pathological significance.|||Found in patients with familial pancreatic cancer; also found in a small cell lung cancer sample; unknown pathological significance.|||Found in patients with familial pancreatic cancer; unknown pathological significance.|||G-loop|||In AT, B-cell chronic lymphocytic leukemia and familial cancer patients; no effect on phosphorylation of target proteins.|||In AT, B-cell chronic lymphocytic leukemia, breast cancer patients and familial cancer patients; no effect on phosphorylation of target proteins.|||In AT.|||In AT; also found in B-cell chronic lymphocytic leukemia and T-prolymphocytic leukemia; may be associated with increased risk for breast cancer; decreased phosphorylation of target proteins.|||In AT; also found in B-cell non-Hodgkin lymphoma; increases protein abundance.|||In AT; also found in T-prolymphocytic leukemia and T-cell acute lymphoblastic leukemia; lack of phosphorylation of target proteins.|||In AT; also found in T-prolymphocytic leukemia and mantle cell lymphoma; lack of phosphorylation of target proteins.|||In AT; also found in T-prolymphocytic leukemia; lack of phosphorylation of target proteins.|||In AT; associated with T-cell acute lymphoblastic leukemia.|||In AT; associated with lymphoma; decrease phosphorylation of target proteins; increases protein abundance.|||In AT; associated with preleukemic T-cell proliferation; decreased phosphorylation of target proteins.|||In AT; decreased phosphorylation of target proteins.|||In AT; decreased protein abundance.|||In AT; decreased protein abundance; loss of DNA damage induced protein autophosphorylation.|||In AT; increases protein abundance.|||In AT; lack of phosphorylation of target proteins.|||In AT; loss of DNA damage induced protein autophosphorylation.|||In AT; loss of protein expression.|||In AT; might be associated with susceptibility to cancer.|||In AT; mild; decreased phosphorylation of target proteins.|||In AT; requires 2 nucleotide substitutions.|||In AT; unknown pathological significance.|||In AT; unknown pathological significance; increases protein abundance.|||In AT; unknown pathological significance; no effect on phosphorylation of target proteins.|||In AT; unknown pathological significance; reduces protein abundance.|||In B-cell chronic lymphocytic leukemia.|||In B-cell chronic lymphocytic leukemia; unknown pathological significance; no effect on phosphorylation of target proteins.|||In T-prolymphocytic leukemia and B-cell chronic lymphocytic leukemia.|||In T-prolymphocytic leukemia.|||In T-prolymphocytic leukemia; also found in a patient with early-onset breast cancer; unknown pathological significance.|||In T-prolymphocytic leukemia; also in a lung adenocarcinoma sample; somatic mutation.|||In T-prolymphocytic leukemia; somatic mutation.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In a renal papillary cancer sample; somatic mutation.|||In mantle cell lymphoma.|||Interaction with ABL1|||Loss of DNA damage-inducible acetylation. Retains constitutive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes S-1981 autophosphorylation.|||Loss of IR-induced S-1893 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1981 autophosphorylation.|||Loss of IR-induced S-1981 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-367 nor S-1893 autophosphorylation. No dimer disruption.|||Loss of IR-induced S-367 autophosphorylation. Reduced correction of cell cycle checkpoint defects and DNA-repair activity. No effect on S-1893 nor S-1981 autophosphorylation.|||Loss of kinase activity.|||Loss of phosphorylation of target proteins.|||May contribute to breast cancer; lack of phosphorylation of target proteins.|||Microbody targeting signal; atypical|||Might contribute to B-cell chronic lymphocytic leukemia.|||Mimics acetylation, preventing dephosphorylation and subsequent ATM deactivation during the late stage of DNA damage response.|||N-acetylserine|||N6-acetyllysine|||No effect on phosphorylation of target proteins.|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphoserine; by autocatalysis|||Removed|||Retains DNA damage-inducible acetylation and S-1981 autophosphorylation.|||Serine-protein kinase ATM ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088840|||http://purl.uniprot.org/annotation/VAR_010798|||http://purl.uniprot.org/annotation/VAR_010799|||http://purl.uniprot.org/annotation/VAR_010800|||http://purl.uniprot.org/annotation/VAR_010801|||http://purl.uniprot.org/annotation/VAR_010802|||http://purl.uniprot.org/annotation/VAR_010803|||http://purl.uniprot.org/annotation/VAR_010804|||http://purl.uniprot.org/annotation/VAR_010805|||http://purl.uniprot.org/annotation/VAR_010806|||http://purl.uniprot.org/annotation/VAR_010807|||http://purl.uniprot.org/annotation/VAR_010808|||http://purl.uniprot.org/annotation/VAR_010809|||http://purl.uniprot.org/annotation/VAR_010810|||http://purl.uniprot.org/annotation/VAR_010812|||http://purl.uniprot.org/annotation/VAR_010813|||http://purl.uniprot.org/annotation/VAR_010814|||http://purl.uniprot.org/annotation/VAR_010815|||http://purl.uniprot.org/annotation/VAR_010816|||http://purl.uniprot.org/annotation/VAR_010817|||http://purl.uniprot.org/annotation/VAR_010818|||http://purl.uniprot.org/annotation/VAR_010819|||http://purl.uniprot.org/annotation/VAR_010820|||http://purl.uniprot.org/annotation/VAR_010821|||http://purl.uniprot.org/annotation/VAR_010822|||http://purl.uniprot.org/annotation/VAR_010823|||http://purl.uniprot.org/annotation/VAR_010825|||http://purl.uniprot.org/annotation/VAR_010826|||http://purl.uniprot.org/annotation/VAR_010827|||http://purl.uniprot.org/annotation/VAR_010828|||http://purl.uniprot.org/annotation/VAR_010829|||http://purl.uniprot.org/annotation/VAR_010830|||http://purl.uniprot.org/annotation/VAR_010831|||http://purl.uniprot.org/annotation/VAR_010832|||http://purl.uniprot.org/annotation/VAR_010833|||http://purl.uniprot.org/annotation/VAR_010834|||http://purl.uniprot.org/annotation/VAR_010835|||http://purl.uniprot.org/annotation/VAR_010836|||http://purl.uniprot.org/annotation/VAR_010837|||http://purl.uniprot.org/annotation/VAR_010838|||http://purl.uniprot.org/annotation/VAR_010839|||http://purl.uniprot.org/annotation/VAR_010840|||http://purl.uniprot.org/annotation/VAR_010841|||http://purl.uniprot.org/annotation/VAR_010842|||http://purl.uniprot.org/annotation/VAR_010843|||http://purl.uniprot.org/annotation/VAR_010844|||http://purl.uniprot.org/annotation/VAR_010845|||http://purl.uniprot.org/annotation/VAR_010846|||http://purl.uniprot.org/annotation/VAR_010847|||http://purl.uniprot.org/annotation/VAR_010848|||http://purl.uniprot.org/annotation/VAR_010849|||http://purl.uniprot.org/annotation/VAR_010850|||http://purl.uniprot.org/annotation/VAR_010851|||http://purl.uniprot.org/annotation/VAR_010852|||http://purl.uniprot.org/annotation/VAR_010853|||http://purl.uniprot.org/annotation/VAR_010854|||http://purl.uniprot.org/annotation/VAR_010855|||http://purl.uniprot.org/annotation/VAR_010856|||http://purl.uniprot.org/annotation/VAR_010857|||http://purl.uniprot.org/annotation/VAR_010858|||http://purl.uniprot.org/annotation/VAR_010859|||http://purl.uniprot.org/annotation/VAR_010860|||http://purl.uniprot.org/annotation/VAR_010861|||http://purl.uniprot.org/annotation/VAR_010862|||http://purl.uniprot.org/annotation/VAR_010863|||http://purl.uniprot.org/annotation/VAR_010864|||http://purl.uniprot.org/annotation/VAR_010865|||http://purl.uniprot.org/annotation/VAR_010866|||http://purl.uniprot.org/annotation/VAR_010868|||http://purl.uniprot.org/annotation/VAR_010869|||http://purl.uniprot.org/annotation/VAR_010870|||http://purl.uniprot.org/annotation/VAR_010871|||http://purl.uniprot.org/annotation/VAR_010872|||http://purl.uniprot.org/annotation/VAR_010873|||http://purl.uniprot.org/annotation/VAR_010874|||http://purl.uniprot.org/annotation/VAR_010875|||http://purl.uniprot.org/annotation/VAR_010876|||http://purl.uniprot.org/annotation/VAR_010877|||http://purl.uniprot.org/annotation/VAR_010878|||http://purl.uniprot.org/annotation/VAR_010879|||http://purl.uniprot.org/annotation/VAR_010880|||http://purl.uniprot.org/annotation/VAR_010881|||http://purl.uniprot.org/annotation/VAR_010882|||http://purl.uniprot.org/annotation/VAR_010883|||http://purl.uniprot.org/annotation/VAR_010884|||http://purl.uniprot.org/annotation/VAR_010885|||http://purl.uniprot.org/annotation/VAR_010886|||http://purl.uniprot.org/annotation/VAR_010887|||http://purl.uniprot.org/annotation/VAR_010888|||http://purl.uniprot.org/annotation/VAR_010889|||http://purl.uniprot.org/annotation/VAR_010890|||http://purl.uniprot.org/annotation/VAR_010892|||http://purl.uniprot.org/annotation/VAR_010893|||http://purl.uniprot.org/annotation/VAR_010894|||http://purl.uniprot.org/annotation/VAR_010895|||http://purl.uniprot.org/annotation/VAR_041545|||http://purl.uniprot.org/annotation/VAR_041546|||http://purl.uniprot.org/annotation/VAR_041547|||http://purl.uniprot.org/annotation/VAR_041548|||http://purl.uniprot.org/annotation/VAR_041549|||http://purl.uniprot.org/annotation/VAR_041550|||http://purl.uniprot.org/annotation/VAR_041551|||http://purl.uniprot.org/annotation/VAR_041552|||http://purl.uniprot.org/annotation/VAR_041553|||http://purl.uniprot.org/annotation/VAR_041554|||http://purl.uniprot.org/annotation/VAR_041555|||http://purl.uniprot.org/annotation/VAR_041556|||http://purl.uniprot.org/annotation/VAR_041557|||http://purl.uniprot.org/annotation/VAR_041558|||http://purl.uniprot.org/annotation/VAR_041559|||http://purl.uniprot.org/annotation/VAR_041560|||http://purl.uniprot.org/annotation/VAR_041561|||http://purl.uniprot.org/annotation/VAR_041562|||http://purl.uniprot.org/annotation/VAR_041563|||http://purl.uniprot.org/annotation/VAR_041564|||http://purl.uniprot.org/annotation/VAR_041565|||http://purl.uniprot.org/annotation/VAR_041566|||http://purl.uniprot.org/annotation/VAR_041567|||http://purl.uniprot.org/annotation/VAR_041568|||http://purl.uniprot.org/annotation/VAR_041569|||http://purl.uniprot.org/annotation/VAR_041570|||http://purl.uniprot.org/annotation/VAR_041571|||http://purl.uniprot.org/annotation/VAR_041572|||http://purl.uniprot.org/annotation/VAR_041573|||http://purl.uniprot.org/annotation/VAR_041574|||http://purl.uniprot.org/annotation/VAR_041575|||http://purl.uniprot.org/annotation/VAR_041576|||http://purl.uniprot.org/annotation/VAR_041577|||http://purl.uniprot.org/annotation/VAR_041578|||http://purl.uniprot.org/annotation/VAR_041579|||http://purl.uniprot.org/annotation/VAR_041580|||http://purl.uniprot.org/annotation/VAR_041581|||http://purl.uniprot.org/annotation/VAR_041582|||http://purl.uniprot.org/annotation/VAR_041583|||http://purl.uniprot.org/annotation/VAR_056678|||http://purl.uniprot.org/annotation/VAR_056679|||http://purl.uniprot.org/annotation/VAR_056680|||http://purl.uniprot.org/annotation/VAR_056681|||http://purl.uniprot.org/annotation/VAR_056682|||http://purl.uniprot.org/annotation/VAR_056683|||http://purl.uniprot.org/annotation/VAR_056684|||http://purl.uniprot.org/annotation/VAR_056685|||http://purl.uniprot.org/annotation/VAR_056686|||http://purl.uniprot.org/annotation/VAR_056687|||http://purl.uniprot.org/annotation/VAR_056688|||http://purl.uniprot.org/annotation/VAR_056689|||http://purl.uniprot.org/annotation/VAR_056690|||http://purl.uniprot.org/annotation/VAR_056691|||http://purl.uniprot.org/annotation/VAR_056692|||http://purl.uniprot.org/annotation/VAR_077237|||http://purl.uniprot.org/annotation/VAR_077238|||http://purl.uniprot.org/annotation/VAR_077239|||http://purl.uniprot.org/annotation/VAR_077240|||http://purl.uniprot.org/annotation/VAR_077241|||http://purl.uniprot.org/annotation/VAR_077242|||http://purl.uniprot.org/annotation/VAR_077243|||http://purl.uniprot.org/annotation/VAR_080300|||http://purl.uniprot.org/annotation/VAR_083373|||http://purl.uniprot.org/annotation/VAR_083374|||http://purl.uniprot.org/annotation/VAR_083375|||http://purl.uniprot.org/annotation/VAR_083376|||http://purl.uniprot.org/annotation/VAR_083377|||http://purl.uniprot.org/annotation/VAR_083378|||http://purl.uniprot.org/annotation/VAR_083379|||http://purl.uniprot.org/annotation/VAR_083380|||http://purl.uniprot.org/annotation/VAR_083381|||http://purl.uniprot.org/annotation/VAR_083382|||http://purl.uniprot.org/annotation/VAR_083383|||http://purl.uniprot.org/annotation/VAR_083384|||http://purl.uniprot.org/annotation/VAR_083385|||http://purl.uniprot.org/annotation/VAR_083386|||http://purl.uniprot.org/annotation/VAR_083387|||http://purl.uniprot.org/annotation/VAR_083388|||http://purl.uniprot.org/annotation/VAR_083389|||http://purl.uniprot.org/annotation/VAR_083390|||http://purl.uniprot.org/annotation/VAR_083391|||http://purl.uniprot.org/annotation/VAR_083392|||http://purl.uniprot.org/annotation/VAR_085060|||http://purl.uniprot.org/annotation/VAR_085061|||http://purl.uniprot.org/annotation/VAR_085062|||http://purl.uniprot.org/annotation/VAR_085063|||http://purl.uniprot.org/annotation/VAR_085064|||http://purl.uniprot.org/annotation/VAR_085065|||http://purl.uniprot.org/annotation/VAR_085066|||http://purl.uniprot.org/annotation/VAR_085067|||http://purl.uniprot.org/annotation/VAR_085068|||http://purl.uniprot.org/annotation/VAR_085069|||http://purl.uniprot.org/annotation/VAR_085070|||http://purl.uniprot.org/annotation/VAR_085071
http://togogenome.org/gene/9606:BMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1RMZ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolished binding to S-adenosyl-L-methionine without affecting ability to associate with GATOR1 and KICSTOR complexes.|||Disordered|||S-adenosylmethionine sensor upstream of mTORC1|||Strongly decreased ability to associate with GATOR1 and KICSTOR complexes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321539
http://togogenome.org/gene/9606:MUC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0L2|||http://purl.uniprot.org/uniprot/A0A0A0MRB3|||http://purl.uniprot.org/uniprot/A0A0C4DGW3|||http://purl.uniprot.org/uniprot/A0A384NPK6|||http://purl.uniprot.org/uniprot/A5YRU5|||http://purl.uniprot.org/uniprot/A5YRU7|||http://purl.uniprot.org/uniprot/A5YRV0|||http://purl.uniprot.org/uniprot/A5YRV2|||http://purl.uniprot.org/uniprot/A6ZID6|||http://purl.uniprot.org/uniprot/A6ZID7|||http://purl.uniprot.org/uniprot/A6ZIE4|||http://purl.uniprot.org/uniprot/A6ZIE6|||http://purl.uniprot.org/uniprot/B6ECB3|||http://purl.uniprot.org/uniprot/P15941|||http://purl.uniprot.org/uniprot/Q7Z538|||http://purl.uniprot.org/uniprot/Q7Z551                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||1; approximate|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||2; approximate|||3|||30|||31|||32|||33|||34|||35|||36|||37|||38|||39|||4|||40|||41|||42|||42 X 20 AA approximate tandem repeats of P-A-P-G-S-T-A-P-P-A-H-G-V-T-S-A-P-D-T-R|||43|||44|||45|||46; approximate|||47; approximate|||48; approximate|||5|||6|||7|||8|||9|||Almost complete cleavage.|||Cleavage; by autolysis|||Completely abrogates cleavage.|||Cytoplasmic|||Disordered|||Extracellular|||Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding.|||Greatly reduced formation of isoform 5/isoform Y complex.|||Helical|||In isoform 2, isoform Y-LSP, isoform E2, isoform J13, isoform S2 and isoform T10.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8, isoform 9 and isoform M6.|||In isoform 9 and isoform S2.|||In isoform E2.|||In isoform F.|||In isoform J13, isoform Y, isoform Y-LSP and isoform S2.|||In isoform J13.|||In isoform M6.|||In isoform T10.|||In isoform ZD.|||Interaction with GRB2|||Interaction with P53|||Interaction with SRC and ESR1|||Loss of PRKCD-mediated phosphorylation. Decreased PRKCD binding. No increased binding to CTNNB1 in the presence of autophosphorylated PRKCD. Increases formation of E-cadherin/beta-catenin complex.|||Mucin-1|||Mucin-1 subunit alpha|||Mucin-1 subunit beta|||N-linked (GlcNAc...) asparagine|||No change in PRKCD- nor GSK3B-mediated phosphorylation.|||No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1.|||No effect on EGFR-mediated phosphorylation.|||No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1.|||No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness.|||No effect on endocytosis.|||No effect on formation of isoform 5/isoform Y complex.|||No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness.|||No effect on palmitoylation.|||No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by PKC/PRKCD|||Phosphotyrosine|||Phosphotyrosine; by CSK, EGFR and SRC|||Phosphotyrosine; by PDGFR|||Polar residues|||Reduced endocytosis by 30%. Greatly reduced binding to AP1S2 and GRB2. Binding AP1S1 reduced by 25%. Reduced endocytosis by 77%; when associated with N-1243. Accumulates in intracellular compartments; when associated with C-1184 and C-1186.|||Reduces binding to AP1S2 by 33%. Greatly reduced binding to GRB2. Reduced endocytosis by 50%. Reduced endocytosis by 77%; when associated with N-1203.|||Required for interaction with AP1S2|||Required for interaction with GSK3B|||Required for interaction with beta- and gamma-catenins|||S-palmitoyl cysteine|||S-palmitoylation reduced by 50%. Complete loss of palmitoylation, no effect on endocytosis, recycling inhibited and AP1S1 binding reduced by 30%; when associated with C-1186. Accumulates in intracellular compartments; when associated with C-1186 and N-1203.|||S-palmitoylation reduced by 50%. Complete loss of palmitoylation, no effect on endocytosis, recycling inhibited, and AP1S1 binding reduced by 30%; when associated with C-1184. Accumulates in intracellular compartments; when associated with C-1184 and N-1203.|||SEA|||Some reduction in EGFR-mediated phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019277|||http://purl.uniprot.org/annotation/PRO_0000317446|||http://purl.uniprot.org/annotation/PRO_0000317447|||http://purl.uniprot.org/annotation/PRO_5001832146|||http://purl.uniprot.org/annotation/PRO_5001967087|||http://purl.uniprot.org/annotation/PRO_5002181428|||http://purl.uniprot.org/annotation/PRO_5002690021|||http://purl.uniprot.org/annotation/PRO_5002690093|||http://purl.uniprot.org/annotation/PRO_5002690095|||http://purl.uniprot.org/annotation/PRO_5002690152|||http://purl.uniprot.org/annotation/PRO_5002703655|||http://purl.uniprot.org/annotation/PRO_5002705839|||http://purl.uniprot.org/annotation/PRO_5002705887|||http://purl.uniprot.org/annotation/PRO_5002844348|||http://purl.uniprot.org/annotation/PRO_5004296928|||http://purl.uniprot.org/annotation/PRO_5004296931|||http://purl.uniprot.org/annotation/PRO_5014565778|||http://purl.uniprot.org/annotation/PRO_5017387969|||http://purl.uniprot.org/annotation/VAR_019390|||http://purl.uniprot.org/annotation/VAR_019391|||http://purl.uniprot.org/annotation/VSP_003280|||http://purl.uniprot.org/annotation/VSP_003281|||http://purl.uniprot.org/annotation/VSP_003282|||http://purl.uniprot.org/annotation/VSP_003283|||http://purl.uniprot.org/annotation/VSP_003284|||http://purl.uniprot.org/annotation/VSP_003285|||http://purl.uniprot.org/annotation/VSP_003286|||http://purl.uniprot.org/annotation/VSP_003287|||http://purl.uniprot.org/annotation/VSP_003288|||http://purl.uniprot.org/annotation/VSP_003289|||http://purl.uniprot.org/annotation/VSP_035046|||http://purl.uniprot.org/annotation/VSP_035047|||http://purl.uniprot.org/annotation/VSP_046962|||http://purl.uniprot.org/annotation/VSP_046963|||http://purl.uniprot.org/annotation/VSP_047575|||http://purl.uniprot.org/annotation/VSP_047576|||http://purl.uniprot.org/annotation/VSP_047872|||http://purl.uniprot.org/annotation/VSP_047873|||http://purl.uniprot.org/annotation/VSP_047874
http://togogenome.org/gene/9606:FCHSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WN1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||F-BAR and double SH3 domains protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278212|||http://purl.uniprot.org/annotation/VAR_030692|||http://purl.uniprot.org/annotation/VAR_030693|||http://purl.uniprot.org/annotation/VSP_023160|||http://purl.uniprot.org/annotation/VSP_023161|||http://purl.uniprot.org/annotation/VSP_023162|||http://purl.uniprot.org/annotation/VSP_023163|||http://purl.uniprot.org/annotation/VSP_023164|||http://purl.uniprot.org/annotation/VSP_023165
http://togogenome.org/gene/9606:SKOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2VWA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Polar residues|||Pro residues|||SKI family transcriptional corepressor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334611|||http://purl.uniprot.org/annotation/VAR_043438|||http://purl.uniprot.org/annotation/VSP_033691|||http://purl.uniprot.org/annotation/VSP_033692
http://togogenome.org/gene/9606:PI4KA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYG5|||http://purl.uniprot.org/uniprot/P42356|||http://purl.uniprot.org/uniprot/Q4LE69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Activation loop|||Catalytic loop|||Disordered|||G-loop|||In GIDID2; decreased interaction with TTC7A resulting in reduced PI4K complex stability; no effect on kinase activity.|||In NEDSPLB.|||In NEDSPLB; loss of kinase activity; no effect on protein abundance.|||In NEDSPLB; unknown pathological significance.|||In SPG84; unknown pathological significance.|||In isoform 2.|||Loss of kinase activity.|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4-kinase alpha|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088827|||http://purl.uniprot.org/annotation/VAR_050531|||http://purl.uniprot.org/annotation/VAR_059549|||http://purl.uniprot.org/annotation/VAR_074640|||http://purl.uniprot.org/annotation/VAR_086468|||http://purl.uniprot.org/annotation/VAR_086469|||http://purl.uniprot.org/annotation/VAR_086470|||http://purl.uniprot.org/annotation/VAR_086471|||http://purl.uniprot.org/annotation/VAR_086472|||http://purl.uniprot.org/annotation/VAR_086473|||http://purl.uniprot.org/annotation/VAR_086474|||http://purl.uniprot.org/annotation/VAR_086475|||http://purl.uniprot.org/annotation/VAR_086476|||http://purl.uniprot.org/annotation/VAR_086477|||http://purl.uniprot.org/annotation/VAR_086478|||http://purl.uniprot.org/annotation/VAR_086479|||http://purl.uniprot.org/annotation/VAR_086480|||http://purl.uniprot.org/annotation/VAR_086481|||http://purl.uniprot.org/annotation/VAR_086482|||http://purl.uniprot.org/annotation/VAR_086483|||http://purl.uniprot.org/annotation/VAR_086484|||http://purl.uniprot.org/annotation/VAR_086485|||http://purl.uniprot.org/annotation/VAR_086486|||http://purl.uniprot.org/annotation/VAR_086487|||http://purl.uniprot.org/annotation/VAR_086488|||http://purl.uniprot.org/annotation/VAR_086489|||http://purl.uniprot.org/annotation/VSP_008805
http://togogenome.org/gene/9606:SLC6A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99884                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Sodium-dependent proline transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214770|||http://purl.uniprot.org/annotation/VAR_011390
http://togogenome.org/gene/9606:RBM43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSC3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  RNA-binding protein 43|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264247|||http://purl.uniprot.org/annotation/VAR_033722
http://togogenome.org/gene/9606:EFCAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7B9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand calcium-binding domain-containing protein 3|||In isoform 2.|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253547|||http://purl.uniprot.org/annotation/VAR_028377|||http://purl.uniprot.org/annotation/VAR_028378|||http://purl.uniprot.org/annotation/VAR_028379|||http://purl.uniprot.org/annotation/VSP_047183
http://togogenome.org/gene/9606:ZNF384                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJE2|||http://purl.uniprot.org/uniprot/Q8TF68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Zinc finger protein 384                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047552|||http://purl.uniprot.org/annotation/VSP_006920|||http://purl.uniprot.org/annotation/VSP_040314|||http://purl.uniprot.org/annotation/VSP_040315
http://togogenome.org/gene/9606:C8orf48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LL4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C8orf48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285631|||http://purl.uniprot.org/annotation/VAR_063134|||http://purl.uniprot.org/annotation/VAR_063135
http://togogenome.org/gene/9606:SPON2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUD6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Important for metal ion-dependent interaction with integrin|||Spondin|||Spondin-2|||Strongly reduced metal-dependent interaction with integrin; when associated with A-141.|||Strongly reduced metal-dependent interaction with integrin; when associated with A-42.|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035870|||http://purl.uniprot.org/annotation/VAR_019701|||http://purl.uniprot.org/annotation/VAR_019702|||http://purl.uniprot.org/annotation/VAR_019703|||http://purl.uniprot.org/annotation/VAR_055149
http://togogenome.org/gene/9606:RXFP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDU9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Relaxin-3 receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070106|||http://purl.uniprot.org/annotation/VAR_021516
http://togogenome.org/gene/9606:PSEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R6A3|||http://purl.uniprot.org/uniprot/A0A0S2Z4D2|||http://purl.uniprot.org/uniprot/P49768                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes PKA-mediated phosphorylation; no effect on caspase-mediated cleavage.|||Abolishes PKC-mediated phosphorylation; no effect on PKA-mediated phosphorylation.|||Abolishes caspase cleavage.|||Abolishes gamma-secretase activity. Reduces production of amyloid-beta in APP processing. Accumulation of full-length PS1. Loss of binding of transition state analog gamma-secretase inhibitor.|||Abolishes protease activity with APP.|||Alters gamma-secretase cleavage specificity. Increased production of amyloid-beta protein 42. No effect on enzymatic activity.|||Basic and acidic residues|||Cleavage|||Cleavage; alternate|||Cleavage; by caspase|||Cytoplasmic|||Decreased protease activity with APP.|||Decreased protease activity with APP. Increased amyloid-beta 42/amyloid-beta 40 ratio in vitro.|||Disordered|||Formation of an artifactual disulfide bond with a substrate protein.|||Found in a renal cell carcinoma sample; somatic mutation.|||Greatly reduced endoproteolytic cleavage. Very little APP and NOTCH1 processing. Very low levels of amyloid-beta protein 40 and no detectable amyloid-beta protein 42.|||Helical|||Impaired ability to cleave Ephb2/CTF1.|||Important for cleavage of target proteins|||In AD3.|||In AD3; abolishes protease activity with APP resulting in decreased amyloid-beta 42 and amyloid-beta 40 production.|||In AD3; abolishes protease activity with APP.|||In AD3; abolishes protease activity with APP; decreased activity for Notch cleavage.|||In AD3; affects APP processing resulting in increased amyloid-beta 42/amyloid-beta 40 ratio; does not affect NOTCH processing; does not affect endoproteolysis; reduced interaction with PEN2; results in decreased protein levels in the endoplasmic reticulum but increased levels in early endosome; reduced ability to maintain ER calcium homeostasis.|||In AD3; also found in late-onset Alzheimer disease; impaired protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; no effect on interaction with GFAP.|||In AD3; atypical phenotype presenting as language impairment, impaired frontal executive function and relative preservation of memory; severe decrease of APP and Notch proteolysis.|||In AD3; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1.|||In AD3; decreased protease activity with APP; no effect on interaction with GFAP.|||In AD3; decreased protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; disease phenotype includes spastic paraparesis; abolishes protease activity with APP resulting in decreased amyloid-beta 42 and amyloid-beta 40 production.|||In AD3; disease phenotype includes spastic paraparesis; unknown pathological significance; severe decrease of protease activity with APP; results in decreased amyloid-beta 42 and amyloid-beta 40 production.|||In AD3; disease phenotype shows high clinical variability; founder mutation originating from Southern Italy and distributed worldwide; alters the conformation of the active site; slightly increased protease activity with APP; decreased activity for Notch1 cleavage; no loss of its ability to cleave Ephb2/CTF1.|||In AD3; impaired ability to cleave Ephb2/CTF1; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; impaired regulation of neurite outgrowth.|||In AD3; impaired protease activity with APP and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; impaired protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; increases protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; loss of function as calcium-leak channel; results in calcium overload in the endoplasmic reticulum.|||In AD3; loss of protease activity with APP.|||In AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1.|||In AD3; nearly abolishes protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; no loss of its ability to cleave Ephb2/CTF1.|||In AD3; onset in adolescence; severe decrease of protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; results in reduced Notch proteolysis.|||In AD3; partially abolishes gamma-secretase activity; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; reduced APP cleavage resulting in decreased amyloid-beta 42 and amyloid-beta 40 production; no relevant change in amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; impaired regulation of neurite outgrowth.|||In AD3; results in reduced APP and Notch proteolysis.|||In AD3; results in reduced APP and Notch proteolysis; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; severe decrease of protease activity with APP.|||In AD3; slightly decreased protease activity with APP and slightly decreased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; slightly decreased protease activity with APP resulting in altered amyloid-beta production and mildly increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; slightly increased protease activity with APP and slightly increased amyloid-beta 42 production.|||In AD3; some AD3 patients manifest spastic paraparesis and unusual amyloid plaques with prominent amyloid angiopathy on brain biopsy; decreased protease activity with APP; increased amyloid-beta 42/amyloid-beta 40 ratio; impaired ability to cleave Ephb2/CTF1.|||In AD3; strong deposition of amyloid-beta 42 is observed in brain regions of AD3 patients; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio; decreased activity for Notch1 cleavage.|||In AD3; the patient also manifest spastic paraparesis and apraxia; loss of protease activity with APP in vitro; altered amyloid-beta production in cells transfected with the mutant and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; uncertain pathological significance; loss of protease activity with APP.|||In AD3; unknown pathological significance.|||In AD3; unknown pathological significance; abolishes protease activity with APP resulting in decreased amyloid-beta 42 and amyloid-beta 40 production.|||In AD3; unknown pathological significance; abolishes protease activity with APP.|||In AD3; unknown pathological significance; decreased protease activity with APP.|||In AD3; unknown pathological significance; decreased protease activity with APP; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; nearly abolishes protease activity with APP.|||In AD3; unknown pathological significance; no significant change of protease activity with APP.|||In AD3; unknown pathological significance; reduced protease activity with APP resulting in reduced amyloid-beta 40 levels but no relevant changes in amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; reduced protease activity with APP; no relevant change in amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; results in decreased protease activity with APP and decreased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; slightly decreased protease activity with APP.|||In AD3; unknown pathological significance; slightly increased protease activity with APP and slightly increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; unknown pathological significance; slightly reduced protease activity with APP.|||In AD3; unusual amyloid cotton wool plaques detected in one patient's brain; severe decrease of protease activity with APP; results in increased amyloid-beta 42/amyloid-beta 40 ratio.|||In AD3; with unusual amyloid cotton wool plaques; almost abolishes gamma-secretase activity; no endoproteolytic cleavage; no APP nor NOTCH1 processing; no detectable amyloid-beta.|||In AD3; with unusual amyloid cotton wool plaques; decreased protease activity with APP resulting in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||In CMD1U; results in slightly decreased protease activity with APP and slightly decreased amyloid-beta 42/amyloid-beta 40 ratio.|||In PIDB and AD3; neuropathologic examination of brain sections from the patient shows the presence of Pick bodies and absence of beta-amyloid plaques; unknown pathological significance; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio in vitro.|||In frontotemporal dementia.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||Increased amyloid-beta 42/amyloid-beta 40 ratio in vitro.|||Increases production of amyloid-beta in APP processing.|||Increases protease activity with APP.|||Inhibits caspase-mediated cleavage. Modulates progression of apoptosis.|||Interaction with MTCH1|||Loss of NOTCH1 and APPC83 cleavage.|||Loss of endoproteolytic cleavage.|||Loss of endoproteolytic cleavage. Severe decrease of protease activity with APP. Reduces production of amyloid-beta. Loss of NOTCH1 cleavage. Disassembly of the N-cadherin/PS1 complex at the cell surface. Impairs CDH2 processing.|||Loss of endoproteolytic cleavage. Severe decrease of protease activity with APP. Reduces production of amyloid-beta. Reduces production of NICD in NOTCH1 processing.|||Loss of interaction with GFAP.|||Lumenal|||Nearly abolishes protease activity with APP.|||Nearly abolishes protease activity with APP. Increased amyloid-beta 42/amyloid-beta 40 ratio in vitro.|||No effect on caspase cleavage.|||No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing.|||No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Reduced amyloid-beta protein 42/40 ratio.|||No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Slightly increased amyloid-beta protein 42/40 ratio.|||No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Greatly reduced amyloid-beta protein 42/40 ratio.|||No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Some increase in amyloid-beta protein 42/40 ratio.|||No effect on interaction with GFAP.|||No endoproteolytic cleavage. No APP nor NOTCH1 processing. No detectable amyloid-beta.|||No endoproteolytic cleavage; no APP, nor NOTCH1 processing. No detectable amyloid-beta.|||No significant change of protease activity with APP.|||PAL|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKC|||Polar residues|||Presenilin-1 CTF subunit|||Presenilin-1 CTF12|||Presenilin-1 NTF subunit|||Probable disease-associated variant found in a patient with dementia.|||Probable disease-associated variant found in patients with late-onset Alzheimer disease; results in altered amyloid-beta production and increased amyloid-beta 42/amyloid-beta 40 ratio.|||Reduces production of NICD in NOTCH1 processing.|||Required for interaction with CTNNB1|||Required for interaction with CTNND2|||Severe decrease of protease activity with APP.|||Severe decrease of protease activity with APP. Increased amyloid-beta 42/amyloid-beta 40 ratio in vitro.|||Slightly increased protease activity with APP.|||Some loss of endoproteolytic cleavage. Some loss of APP and NOTCH1 processing. 6 to 13-fold increase in amyloid-beta protein 42/40 ratio.|||Very little endoproteolysis. Little APP processing. No NOTCH1 processing. Very low levels amyloid-beta protein 40 and no detectable amyloid-beta protein 42. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025591|||http://purl.uniprot.org/annotation/PRO_0000025592|||http://purl.uniprot.org/annotation/PRO_0000236055|||http://purl.uniprot.org/annotation/VAR_006413|||http://purl.uniprot.org/annotation/VAR_006414|||http://purl.uniprot.org/annotation/VAR_006415|||http://purl.uniprot.org/annotation/VAR_006416|||http://purl.uniprot.org/annotation/VAR_006417|||http://purl.uniprot.org/annotation/VAR_006418|||http://purl.uniprot.org/annotation/VAR_006419|||http://purl.uniprot.org/annotation/VAR_006420|||http://purl.uniprot.org/annotation/VAR_006421|||http://purl.uniprot.org/annotation/VAR_006422|||http://purl.uniprot.org/annotation/VAR_006423|||http://purl.uniprot.org/annotation/VAR_006424|||http://purl.uniprot.org/annotation/VAR_006425|||http://purl.uniprot.org/annotation/VAR_006426|||http://purl.uniprot.org/annotation/VAR_006427|||http://purl.uniprot.org/annotation/VAR_006428|||http://purl.uniprot.org/annotation/VAR_006429|||http://purl.uniprot.org/annotation/VAR_006430|||http://purl.uniprot.org/annotation/VAR_006431|||http://purl.uniprot.org/annotation/VAR_006432|||http://purl.uniprot.org/annotation/VAR_006433|||http://purl.uniprot.org/annotation/VAR_006434|||http://purl.uniprot.org/annotation/VAR_006435|||http://purl.uniprot.org/annotation/VAR_006436|||http://purl.uniprot.org/annotation/VAR_006437|||http://purl.uniprot.org/annotation/VAR_006438|||http://purl.uniprot.org/annotation/VAR_006439|||http://purl.uniprot.org/annotation/VAR_006440|||http://purl.uniprot.org/annotation/VAR_006441|||http://purl.uniprot.org/annotation/VAR_006442|||http://purl.uniprot.org/annotation/VAR_006443|||http://purl.uniprot.org/annotation/VAR_006444|||http://purl.uniprot.org/annotation/VAR_006445|||http://purl.uniprot.org/annotation/VAR_006447|||http://purl.uniprot.org/annotation/VAR_006448|||http://purl.uniprot.org/annotation/VAR_006449|||http://purl.uniprot.org/annotation/VAR_006450|||http://purl.uniprot.org/annotation/VAR_006451|||http://purl.uniprot.org/annotation/VAR_006452|||http://purl.uniprot.org/annotation/VAR_006453|||http://purl.uniprot.org/annotation/VAR_006454|||http://purl.uniprot.org/annotation/VAR_006455|||http://purl.uniprot.org/annotation/VAR_006456|||http://purl.uniprot.org/annotation/VAR_006457|||http://purl.uniprot.org/annotation/VAR_006458|||http://purl.uniprot.org/annotation/VAR_006459|||http://purl.uniprot.org/annotation/VAR_006460|||http://purl.uniprot.org/annotation/VAR_008141|||http://purl.uniprot.org/annotation/VAR_009208|||http://purl.uniprot.org/annotation/VAR_009209|||http://purl.uniprot.org/annotation/VAR_009210|||http://purl.uniprot.org/annotation/VAR_009211|||http://purl.uniprot.org/annotation/VAR_009212|||http://purl.uniprot.org/annotation/VAR_009213|||http://purl.uniprot.org/annotation/VAR_010120|||http://purl.uniprot.org/annotation/VAR_010121|||http://purl.uniprot.org/annotation/VAR_010122|||http://purl.uniprot.org/annotation/VAR_010123|||http://purl.uniprot.org/annotation/VAR_010124|||http://purl.uniprot.org/annotation/VAR_010125|||http://purl.uniprot.org/annotation/VAR_010126|||http://purl.uniprot.org/annotation/VAR_010127|||http://purl.uniprot.org/annotation/VAR_010128|||http://purl.uniprot.org/annotation/VAR_010129|||http://purl.uniprot.org/annotation/VAR_011876|||http://purl.uniprot.org/annotation/VAR_016214|||http://purl.uniprot.org/annotation/VAR_016215|||http://purl.uniprot.org/annotation/VAR_016216|||http://purl.uniprot.org/annotation/VAR_016217|||http://purl.uniprot.org/annotation/VAR_016218|||http://purl.uniprot.org/annotation/VAR_016219|||http://purl.uniprot.org/annotation/VAR_016220|||http://purl.uniprot.org/annotation/VAR_025605|||http://purl.uniprot.org/annotation/VAR_064747|||http://purl.uniprot.org/annotation/VAR_064902|||http://purl.uniprot.org/annotation/VAR_070023|||http://purl.uniprot.org/annotation/VAR_070024|||http://purl.uniprot.org/annotation/VAR_070025|||http://purl.uniprot.org/annotation/VAR_070026|||http://purl.uniprot.org/annotation/VAR_075260|||http://purl.uniprot.org/annotation/VAR_075261|||http://purl.uniprot.org/annotation/VAR_075262|||http://purl.uniprot.org/annotation/VAR_075263|||http://purl.uniprot.org/annotation/VAR_075264|||http://purl.uniprot.org/annotation/VAR_075265|||http://purl.uniprot.org/annotation/VAR_075266|||http://purl.uniprot.org/annotation/VAR_075267|||http://purl.uniprot.org/annotation/VAR_075268|||http://purl.uniprot.org/annotation/VAR_075269|||http://purl.uniprot.org/annotation/VAR_075270|||http://purl.uniprot.org/annotation/VAR_075271|||http://purl.uniprot.org/annotation/VAR_075272|||http://purl.uniprot.org/annotation/VAR_075273|||http://purl.uniprot.org/annotation/VAR_075274|||http://purl.uniprot.org/annotation/VAR_075275|||http://purl.uniprot.org/annotation/VAR_075276|||http://purl.uniprot.org/annotation/VAR_075277|||http://purl.uniprot.org/annotation/VAR_075278|||http://purl.uniprot.org/annotation/VAR_075280|||http://purl.uniprot.org/annotation/VAR_075282|||http://purl.uniprot.org/annotation/VAR_081228|||http://purl.uniprot.org/annotation/VAR_081229|||http://purl.uniprot.org/annotation/VAR_081230|||http://purl.uniprot.org/annotation/VAR_081231|||http://purl.uniprot.org/annotation/VAR_081232|||http://purl.uniprot.org/annotation/VAR_081233|||http://purl.uniprot.org/annotation/VAR_081234|||http://purl.uniprot.org/annotation/VAR_081235|||http://purl.uniprot.org/annotation/VAR_081236|||http://purl.uniprot.org/annotation/VAR_081237|||http://purl.uniprot.org/annotation/VAR_081238|||http://purl.uniprot.org/annotation/VAR_081239|||http://purl.uniprot.org/annotation/VAR_081240|||http://purl.uniprot.org/annotation/VAR_081241|||http://purl.uniprot.org/annotation/VAR_081242|||http://purl.uniprot.org/annotation/VAR_081243|||http://purl.uniprot.org/annotation/VAR_081244|||http://purl.uniprot.org/annotation/VAR_081245|||http://purl.uniprot.org/annotation/VAR_081246|||http://purl.uniprot.org/annotation/VAR_081247|||http://purl.uniprot.org/annotation/VAR_081248|||http://purl.uniprot.org/annotation/VAR_081249|||http://purl.uniprot.org/annotation/VAR_081250|||http://purl.uniprot.org/annotation/VAR_081251|||http://purl.uniprot.org/annotation/VAR_081252|||http://purl.uniprot.org/annotation/VAR_081253|||http://purl.uniprot.org/annotation/VAR_081254|||http://purl.uniprot.org/annotation/VAR_081255|||http://purl.uniprot.org/annotation/VAR_081256|||http://purl.uniprot.org/annotation/VAR_081257|||http://purl.uniprot.org/annotation/VAR_081258|||http://purl.uniprot.org/annotation/VAR_081259|||http://purl.uniprot.org/annotation/VSP_005191|||http://purl.uniprot.org/annotation/VSP_005192|||http://purl.uniprot.org/annotation/VSP_007986|||http://purl.uniprot.org/annotation/VSP_007987|||http://purl.uniprot.org/annotation/VSP_012288|||http://purl.uniprot.org/annotation/VSP_041440
http://togogenome.org/gene/9606:C8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z550|||http://purl.uniprot.org/uniprot/B7Z555|||http://purl.uniprot.org/uniprot/P07358                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-linked (Man) tryptophan|||Complement component C8 beta chain|||Disordered|||EGF-like|||In allotype C8BB.|||LDL-receptor class A|||MACPF|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||TSP type-1 1|||TSP type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023591|||http://purl.uniprot.org/annotation/PRO_0000023592|||http://purl.uniprot.org/annotation/VAR_012642|||http://purl.uniprot.org/annotation/VAR_027649|||http://purl.uniprot.org/annotation/VAR_027650
http://togogenome.org/gene/9606:FHDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FH2|||FH2 domain-containing protein 1|||Loss of actin-binding and ability to induce Golgi ribbon formation. Induces a significant increase in average cilia length.|||MTBD; microtubule-binding domain|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317280|||http://purl.uniprot.org/annotation/VAR_050990|||http://purl.uniprot.org/annotation/VAR_069394
http://togogenome.org/gene/9606:CFAP299                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6V702                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 299|||In isoform 1.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301955|||http://purl.uniprot.org/annotation/VAR_034913|||http://purl.uniprot.org/annotation/VAR_034914|||http://purl.uniprot.org/annotation/VSP_037233|||http://purl.uniprot.org/annotation/VSP_037234|||http://purl.uniprot.org/annotation/VSP_037235
http://togogenome.org/gene/9606:NCOA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPW8|||http://purl.uniprot.org/uniprot/Q15596                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Breakpoint for translocation to form KAT6A-NCOA2|||By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 693-A-A-694.|||By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 748-A-A-749.|||By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 693-A-A-694 and 748-A-A-749.|||CASP8AP2-binding|||DUF1518|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Has little effect on transcriptional coactivation.|||Interaction with BMAL1|||LLXXLXXXL motif|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||N-acetylserine|||N6-acetyllysine|||Nuclear receptor coactivator 2|||Omega-N-methylarginine|||PAS|||Phosphoserine|||Polar residues|||Reduces transcriptional coactivation and disrupts interaction with CREBBP/CBP.|||Removed|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094402|||http://purl.uniprot.org/annotation/VAR_024546
http://togogenome.org/gene/9606:HHATL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QTR4|||http://purl.uniprot.org/uniprot/Q9HCP6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein-cysteine N-palmitoyltransferase HHAT-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213130|||http://purl.uniprot.org/annotation/VAR_014947
http://togogenome.org/gene/9606:USP17L11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JVI0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421087
http://togogenome.org/gene/9606:OBP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLH4|||http://purl.uniprot.org/uniprot/Q5T8A4|||http://purl.uniprot.org/uniprot/Q5T8A5|||http://purl.uniprot.org/uniprot/Q9NY56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases binding affinity for undecanal, efficient aldehydes and aliphatic acids from 9- to 12-carbons long. No effect on binding affinity of benzenic or heterocyclic aldehydes.|||Disordered|||In isoform Ab.|||In isoform Ad.|||In isoform Ag.|||Lipocalin/cytosolic fatty-acid binding|||Lipocalin/cytosolic fatty-acid binding domain-containing protein|||No effect on binding affinity for undecanal, palmitic acid, efficient aldehydes, benzenic aldehydes, heterocyclic aldehydes or aliphatic acids.|||Odorant-binding protein 2a|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017937|||http://purl.uniprot.org/annotation/PRO_5012790894|||http://purl.uniprot.org/annotation/PRO_5012791111|||http://purl.uniprot.org/annotation/PRO_5012949217|||http://purl.uniprot.org/annotation/VAR_034354|||http://purl.uniprot.org/annotation/VAR_050176|||http://purl.uniprot.org/annotation/VAR_061359|||http://purl.uniprot.org/annotation/VAR_061360|||http://purl.uniprot.org/annotation/VSP_003135|||http://purl.uniprot.org/annotation/VSP_003136|||http://purl.uniprot.org/annotation/VSP_003137
http://togogenome.org/gene/9606:SLC45A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RXG1|||http://purl.uniprot.org/uniprot/E7EV90|||http://purl.uniprot.org/uniprot/Q5BKX6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Solute carrier family 45 member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333803|||http://purl.uniprot.org/annotation/VAR_043164|||http://purl.uniprot.org/annotation/VAR_043165|||http://purl.uniprot.org/annotation/VSP_033540|||http://purl.uniprot.org/annotation/VSP_033541|||http://purl.uniprot.org/annotation/VSP_033542
http://togogenome.org/gene/9606:CFTR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13569                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Abolishes MARCHF2-mediated degradation.|||Abolishes N-glycosylation, enhances endocytosis and impairs subsequent recycling to the cell surface; when associated with D-894.|||Abolishes N-glycosylation, enhances endocytosis and impairs subsequent recycling to the cell surface; when associated with D-900.|||Abolishes channel activity. Impairs protein maturation, suggesting the protein is retained in the endoplasmic reticulum.|||Basic and acidic residues|||Cystic fibrosis transmembrane conductance regulator|||Cytoplasmic|||Decreases channel activity, no visible effect on protein maturation.|||Discontinuously helical; Name=8|||Disordered|||Disordered R region|||Enhances trafficking from the endoplasmic reticulum to the cell membrane.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=9|||Impaired maturation of glycan chains indicating impaired trafficking from the endoplasmic reticulum to the cell membrane.|||In CBAVD and CF.|||In CBAVD and CF; decrease in bicarbonate transport; no effect on chloride channel activity.|||In CBAVD and CF; unknown pathological significance; found in cis of the IVS8 TG11-T5 allele, which affects exon 9 splicing; no effect on protein maturation, trafficking to the cell membrane, nor on channel activity.|||In CBAVD.|||In CBAVD; decreased channel activity; has no effect on glycan maturation.|||In CBAVD; no effect on glycan maturation but decreased channel activity.|||In CBAVD; small decrease in bicarbonate transport; increase in chloride channel activity in vitro; no effect on glycan maturation.|||In CBAVD; unknown pathological significance.|||In CBAVD; unknown pathological significance; no effect on glycan maturation; no effect on channel activity.|||In CF and CBAVD.|||In CF and CBAVD; decreases channel activity; no visible effect on protein maturation.|||In CF and CBAVD; mild; does not prevent maturation of glycans.|||In CF and CBAVD; most common mutation in Caucasian CF chromosomes; impairs protein folding and stability; causes local changes to the surface that mediates interactions between domains; decreases frequency of channel opening in vitro; binds to the cytokeratin-8 and through this binding is primed for the degradation pathway that ends in the proteasome, thus impairing trafficking; impairs maturation and trafficking to the cell membrane; impairs recycling to the cell membrane after endocytosis.|||In CF and CBAVD; strong decrease in single channel conductance; promotes rapid return to the closed state of the channel; decrease in bicarbonate transport.|||In CF and CBAVD; unknown pathological significance.|||In CF.|||In CF; abolishes channel activity; no visible effect on protein maturation.|||In CF; decrease in bicarbonate transport; no effect chloride channel activity.|||In CF; decrease in bicarbonate transport; no effect on chloride channel activity.|||In CF; decrease in the frequency of channel opening in vitro; decrease in channel activity and ATPase activity; complete loss of bicarbonate transport; no effect on trafficking to the cell membrane, protein stability, nor on the maturation of glycans.|||In CF; decreased presence at the cell membrane due to increased internalization from the apical cell membrane; no effect on single channel gating and conductance.|||In CF; decreases channel activity; no visible effect on protein maturation.|||In CF; dominant mutation but mild phenotype.|||In CF; impaired maturation of glycan chains.|||In CF; impaired maturation of glycan chains; has low in vitro channel activity at low temperature.|||In CF; impairs maturation and trafficking to the cell membrane; decrease in channel activity.|||In CF; loss of bicarbonate transport; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity.|||In CF; mild.|||In CF; mild; isolated hypotonic dehydration.|||In CF; no effect on glycan maturation but decreased channel activity.|||In CF; strong decrease in bicarbonate transport; increase in chloride channel activity in vitro; no effect on glycan maturation.|||In CF; unknown pathological significance.|||In CF; unknown pathological significance; loss of bicarbonate transport; decreased inhibition of epithelial sodium channel (ENaC), when tested in a heterologous system; no effect on protein maturation, subcellular location at the plasma membrane, nor on chloride channel activity.|||In CF; unknown pathological significance; no effect on glycan maturation and channel activity.|||In CF; unknown pathological significance; no effect on glycan maturation; no effect on channel activity.|||In isoform 2.|||In isoform 3.|||In thoracic sarcoidosis; unknown pathological significance; no effect on glycan maturation and channel activity.|||Interaction with GORASP2|||N-linked (GlcNAc...) asparagine|||No effect on maturation of glycans, suggesting that trafficking to the plasma membrane is not altered.|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKC|||Phosphothreonine|||Reduces interaction with MARCHF2 and abolishes subsequent MARCHF2-mediated degradation. No effect on localization to the Golgi.|||S-palmitoyl cysteine ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093419|||http://purl.uniprot.org/annotation/VAR_000101|||http://purl.uniprot.org/annotation/VAR_000102|||http://purl.uniprot.org/annotation/VAR_000103|||http://purl.uniprot.org/annotation/VAR_000104|||http://purl.uniprot.org/annotation/VAR_000105|||http://purl.uniprot.org/annotation/VAR_000106|||http://purl.uniprot.org/annotation/VAR_000107|||http://purl.uniprot.org/annotation/VAR_000108|||http://purl.uniprot.org/annotation/VAR_000109|||http://purl.uniprot.org/annotation/VAR_000110|||http://purl.uniprot.org/annotation/VAR_000111|||http://purl.uniprot.org/annotation/VAR_000112|||http://purl.uniprot.org/annotation/VAR_000113|||http://purl.uniprot.org/annotation/VAR_000114|||http://purl.uniprot.org/annotation/VAR_000115|||http://purl.uniprot.org/annotation/VAR_000116|||http://purl.uniprot.org/annotation/VAR_000118|||http://purl.uniprot.org/annotation/VAR_000119|||http://purl.uniprot.org/annotation/VAR_000120|||http://purl.uniprot.org/annotation/VAR_000121|||http://purl.uniprot.org/annotation/VAR_000122|||http://purl.uniprot.org/annotation/VAR_000123|||http://purl.uniprot.org/annotation/VAR_000124|||http://purl.uniprot.org/annotation/VAR_000125|||http://purl.uniprot.org/annotation/VAR_000126|||http://purl.uniprot.org/annotation/VAR_000127|||http://purl.uniprot.org/annotation/VAR_000128|||http://purl.uniprot.org/annotation/VAR_000129|||http://purl.uniprot.org/annotation/VAR_000130|||http://purl.uniprot.org/annotation/VAR_000131|||http://purl.uniprot.org/annotation/VAR_000132|||http://purl.uniprot.org/annotation/VAR_000133|||http://purl.uniprot.org/annotation/VAR_000134|||http://purl.uniprot.org/annotation/VAR_000135|||http://purl.uniprot.org/annotation/VAR_000136|||http://purl.uniprot.org/annotation/VAR_000137|||http://purl.uniprot.org/annotation/VAR_000138|||http://purl.uniprot.org/annotation/VAR_000139|||http://purl.uniprot.org/annotation/VAR_000140|||http://purl.uniprot.org/annotation/VAR_000141|||http://purl.uniprot.org/annotation/VAR_000142|||http://purl.uniprot.org/annotation/VAR_000143|||http://purl.uniprot.org/annotation/VAR_000144|||http://purl.uniprot.org/annotation/VAR_000145|||http://purl.uniprot.org/annotation/VAR_000146|||http://purl.uniprot.org/annotation/VAR_000147|||http://purl.uniprot.org/annotation/VAR_000148|||http://purl.uniprot.org/annotation/VAR_000150|||http://purl.uniprot.org/annotation/VAR_000151|||http://purl.uniprot.org/annotation/VAR_000152|||http://purl.uniprot.org/annotation/VAR_000153|||http://purl.uniprot.org/annotation/VAR_000154|||http://purl.uniprot.org/annotation/VAR_000155|||http://purl.uniprot.org/annotation/VAR_000156|||http://purl.uniprot.org/annotation/VAR_000157|||http://purl.uniprot.org/annotation/VAR_000158|||http://purl.uniprot.org/annotation/VAR_000159|||http://purl.uniprot.org/annotation/VAR_000160|||http://purl.uniprot.org/annotation/VAR_000161|||http://purl.uniprot.org/annotation/VAR_000162|||http://purl.uniprot.org/annotation/VAR_000163|||http://purl.uniprot.org/annotation/VAR_000164|||http://purl.uniprot.org/annotation/VAR_000165|||http://purl.uniprot.org/annotation/VAR_000166|||http://purl.uniprot.org/annotation/VAR_000167|||http://purl.uniprot.org/annotation/VAR_000168|||http://purl.uniprot.org/annotation/VAR_000169|||http://purl.uniprot.org/annotation/VAR_000170|||http://purl.uniprot.org/annotation/VAR_000171|||http://purl.uniprot.org/annotation/VAR_000172|||http://purl.uniprot.org/annotation/VAR_000173|||http://purl.uniprot.org/annotation/VAR_000174|||http://purl.uniprot.org/annotation/VAR_000175|||http://purl.uniprot.org/annotation/VAR_000176|||http://purl.uniprot.org/annotation/VAR_000177|||http://purl.uniprot.org/annotation/VAR_000178|||http://purl.uniprot.org/annotation/VAR_000179|||http://purl.uniprot.org/annotation/VAR_000180|||http://purl.uniprot.org/annotation/VAR_000181|||http://purl.uniprot.org/annotation/VAR_000182|||http://purl.uniprot.org/annotation/VAR_000183|||http://purl.uniprot.org/annotation/VAR_000184|||http://purl.uniprot.org/annotation/VAR_000185|||http://purl.uniprot.org/annotation/VAR_000186|||http://purl.uniprot.org/annotation/VAR_000187|||http://purl.uniprot.org/annotation/VAR_000188|||http://purl.uniprot.org/annotation/VAR_000189|||http://purl.uniprot.org/annotation/VAR_000190|||http://purl.uniprot.org/annotation/VAR_000191|||http://purl.uniprot.org/annotation/VAR_000192|||http://purl.uniprot.org/annotation/VAR_000193|||http://purl.uniprot.org/annotation/VAR_000194|||http://purl.uniprot.org/annotation/VAR_000195|||http://purl.uniprot.org/annotation/VAR_000196|||http://purl.uniprot.org/annotation/VAR_000197|||http://purl.uniprot.org/annotation/VAR_000198|||http://purl.uniprot.org/annotation/VAR_000199|||http://purl.uniprot.org/annotation/VAR_000200|||http://purl.uniprot.org/annotation/VAR_000201|||http://purl.uniprot.org/annotation/VAR_000202|||http://purl.uniprot.org/annotation/VAR_000203|||http://purl.uniprot.org/annotation/VAR_000204|||http://purl.uniprot.org/annotation/VAR_000205|||http://purl.uniprot.org/annotation/VAR_000206|||http://purl.uniprot.org/annotation/VAR_000207|||http://purl.uniprot.org/annotation/VAR_000208|||http://purl.uniprot.org/annotation/VAR_000209|||http://purl.uniprot.org/annotation/VAR_000210|||http://purl.uniprot.org/annotation/VAR_000211|||http://purl.uniprot.org/annotation/VAR_000212|||http://purl.uniprot.org/annotation/VAR_000213|||http://purl.uniprot.org/annotation/VAR_000214|||http://purl.uniprot.org/annotation/VAR_000215|||http://purl.uniprot.org/annotation/VAR_000216|||http://purl.uniprot.org/annotation/VAR_000217|||http://purl.uniprot.org/annotation/VAR_000218|||http://purl.uniprot.org/annotation/VAR_000219|||http://purl.uniprot.org/annotation/VAR_000220|||http://purl.uniprot.org/annotation/VAR_000221|||http://purl.uniprot.org/annotation/VAR_000222|||http://purl.uniprot.org/annotation/VAR_000223|||http://purl.uniprot.org/annotation/VAR_000224|||http://purl.uniprot.org/annotation/VAR_000225|||http://purl.uniprot.org/annotation/VAR_000226|||http://purl.uniprot.org/annotation/VAR_000227|||http://purl.uniprot.org/annotation/VAR_000228|||http://purl.uniprot.org/annotation/VAR_000229|||http://purl.uniprot.org/annotation/VAR_000230|||http://purl.uniprot.org/annotation/VAR_000231|||http://purl.uniprot.org/annotation/VAR_000232|||http://purl.uniprot.org/annotation/VAR_000233|||http://purl.uniprot.org/annotation/VAR_000234|||http://purl.uniprot.org/annotation/VAR_000235|||http://purl.uniprot.org/annotation/VAR_000236|||http://purl.uniprot.org/annotation/VAR_000237|||http://purl.uniprot.org/annotation/VAR_000238|||http://purl.uniprot.org/annotation/VAR_000239|||http://purl.uniprot.org/annotation/VAR_000240|||http://purl.uniprot.org/annotation/VAR_000241|||http://purl.uniprot.org/annotation/VAR_000242|||http://purl.uniprot.org/annotation/VAR_000243|||http://purl.uniprot.org/annotation/VAR_000244|||http://purl.uniprot.org/annotation/VAR_000245|||http://purl.uniprot.org/annotation/VAR_000246|||http://purl.uniprot.org/annotation/VAR_000247|||http://purl.uniprot.org/annotation/VAR_000248|||http://purl.uniprot.org/annotation/VAR_000249|||http://purl.uniprot.org/annotation/VAR_000250|||http://purl.uniprot.org/annotation/VAR_000251|||http://purl.uniprot.org/annotation/VAR_000252|||http://purl.uniprot.org/annotation/VAR_000253|||http://purl.uniprot.org/annotation/VAR_000254|||http://purl.uniprot.org/annotation/VAR_000255|||http://purl.uniprot.org/annotation/VAR_000256|||http://purl.uniprot.org/annotation/VAR_000257|||http://purl.uniprot.org/annotation/VAR_000258|||http://purl.uniprot.org/annotation/VAR_000259|||http://purl.uniprot.org/annotation/VAR_000260|||http://purl.uniprot.org/annotation/VAR_000261|||http://purl.uniprot.org/annotation/VAR_000262|||http://purl.uniprot.org/annotation/VAR_000263|||http://purl.uniprot.org/annotation/VAR_000264|||http://purl.uniprot.org/annotation/VAR_000265|||http://purl.uniprot.org/annotation/VAR_000266|||http://purl.uniprot.org/annotation/VAR_000267|||http://purl.uniprot.org/annotation/VAR_000268|||http://purl.uniprot.org/annotation/VAR_000269|||http://purl.uniprot.org/annotation/VAR_000270|||http://purl.uniprot.org/annotation/VAR_009895|||http://purl.uniprot.org/annotation/VAR_009896|||http://purl.uniprot.org/annotation/VAR_009897|||http://purl.uniprot.org/annotation/VAR_009898|||http://purl.uniprot.org/annotation/VAR_009899|||http://purl.uniprot.org/annotation/VAR_009900|||http://purl.uniprot.org/annotation/VAR_009901|||http://purl.uniprot.org/annotation/VAR_009902|||http://purl.uniprot.org/annotation/VAR_009903|||http://purl.uniprot.org/annotation/VAR_009904|||http://purl.uniprot.org/annotation/VAR_009905|||http://purl.uniprot.org/annotation/VAR_011564|||http://purl.uniprot.org/annotation/VAR_011565|||http://purl.uniprot.org/annotation/VAR_048150|||http://purl.uniprot.org/annotation/VAR_048151|||http://purl.uniprot.org/annotation/VAR_048152|||http://purl.uniprot.org/annotation/VAR_080302|||http://purl.uniprot.org/annotation/VAR_080303|||http://purl.uniprot.org/annotation/VAR_080304|||http://purl.uniprot.org/annotation/VAR_080305|||http://purl.uniprot.org/annotation/VAR_080306|||http://purl.uniprot.org/annotation/VAR_080307|||http://purl.uniprot.org/annotation/VAR_080308|||http://purl.uniprot.org/annotation/VAR_080309|||http://purl.uniprot.org/annotation/VAR_080310|||http://purl.uniprot.org/annotation/VAR_080311|||http://purl.uniprot.org/annotation/VAR_080312|||http://purl.uniprot.org/annotation/VAR_080313|||http://purl.uniprot.org/annotation/VAR_080314|||http://purl.uniprot.org/annotation/VAR_080315|||http://purl.uniprot.org/annotation/VAR_080316|||http://purl.uniprot.org/annotation/VAR_080317|||http://purl.uniprot.org/annotation/VAR_080318|||http://purl.uniprot.org/annotation/VAR_080319|||http://purl.uniprot.org/annotation/VAR_080320|||http://purl.uniprot.org/annotation/VAR_080321|||http://purl.uniprot.org/annotation/VAR_080322|||http://purl.uniprot.org/annotation/VAR_080323|||http://purl.uniprot.org/annotation/VAR_080324|||http://purl.uniprot.org/annotation/VAR_080325|||http://purl.uniprot.org/annotation/VAR_080326|||http://purl.uniprot.org/annotation/VSP_022123|||http://purl.uniprot.org/annotation/VSP_022124|||http://purl.uniprot.org/annotation/VSP_022125
http://togogenome.org/gene/9606:TMEM273                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T292                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Transmembrane protein 273                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307322|||http://purl.uniprot.org/annotation/VAR_035409|||http://purl.uniprot.org/annotation/VSP_028715|||http://purl.uniprot.org/annotation/VSP_028716|||http://purl.uniprot.org/annotation/VSP_028717
http://togogenome.org/gene/9606:ACSF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H5A1|||http://purl.uniprot.org/uniprot/Q4G176                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Impairs malonyl-CoA synthase activity.|||In CMAMMA.|||Malonate--CoA ligase ACSF3, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315800|||http://purl.uniprot.org/annotation/VAR_038306|||http://purl.uniprot.org/annotation/VAR_038307|||http://purl.uniprot.org/annotation/VAR_038308|||http://purl.uniprot.org/annotation/VAR_066504|||http://purl.uniprot.org/annotation/VAR_066505|||http://purl.uniprot.org/annotation/VAR_066506|||http://purl.uniprot.org/annotation/VAR_066507|||http://purl.uniprot.org/annotation/VAR_066508|||http://purl.uniprot.org/annotation/VAR_066509|||http://purl.uniprot.org/annotation/VAR_066510|||http://purl.uniprot.org/annotation/VAR_066511|||http://purl.uniprot.org/annotation/VAR_066512|||http://purl.uniprot.org/annotation/VAR_066513
http://togogenome.org/gene/9606:GAGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFV5|||http://purl.uniprot.org/uniprot/P0DTW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 1|||GAGE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148339
http://togogenome.org/gene/9606:OR2AG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVD0|||http://purl.uniprot.org/uniprot/Q9H205                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2AG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150472|||http://purl.uniprot.org/annotation/VAR_053140|||http://purl.uniprot.org/annotation/VAR_059985|||http://purl.uniprot.org/annotation/VAR_059986
http://togogenome.org/gene/9606:VPS37D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328927
http://togogenome.org/gene/9606:FAAP20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NZ36|||http://purl.uniprot.org/uniprot/Q6ZRT9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to ubiquitin.|||Abolishes binding to ubiquitin. Abolishes binding to ubiquitin; when associated with A-150.|||Abolishes binding to ubiquitin; when associated with A-147.|||Disordered|||Fanconi anemia core complex-associated protein 20|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||UBZ2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316882|||http://purl.uniprot.org/annotation/VAR_038434|||http://purl.uniprot.org/annotation/VSP_030812|||http://purl.uniprot.org/annotation/VSP_030813|||http://purl.uniprot.org/annotation/VSP_030814|||http://purl.uniprot.org/annotation/VSP_030815|||http://purl.uniprot.org/annotation/VSP_030816|||http://purl.uniprot.org/annotation/VSP_047264
http://togogenome.org/gene/9606:CX3CL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0N7|||http://purl.uniprot.org/uniprot/P78423                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chemokine and involved in interaction with ITGAV:ITGB3 and ITGA4:ITGB1|||Chemokine interleukin-8-like|||Cleavage; to produce soluble form|||Cytoplasmic|||Disordered|||Dominant-negative mutant, reduced binding to integrins ITGAV:ITGB3 and ITGA4:ITGB1, no effect on binding to CX3CR1, defective in ternary complex formation, integrin activation and fractalkine signaling and suppression of leukocyte recruitment in the peritonitis model in vivo; when associated with E-60.|||Dominant-negative mutant, reduced binding to integrins ITGAV:ITGB3 and ITGA4:ITGB1, no effect on binding to CX3CR1, defective in ternary complex formation, integrin activation and fractalkine signaling and suppression of leukocyte recruitment in the peritonitis model in vivo; when associated with E-61.|||Extracellular|||Fractalkine|||Helical|||Little or no effect on binding to integrin ITGAV:ITGB3.|||Little or no effect on binding to integrin ITGAV:ITGB3; when associated with A-78.|||Little or no effect on binding to integrin ITGAV:ITGB3; when associated with A-83.|||Loss of binding to CX3CR1 and ability to induce chemotaxis but no effect on binding to integrins.|||Mucin-like stalk|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues|||Processed fractalkine|||Reduced binding to integrin ITGAV:ITGB3, but no effect on binding to CX3CR1; when associated with A-60.|||Reduced binding to integrin ITGAV:ITGB3, but no effect on binding to CX3CR1; when associated with A-61.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005252|||http://purl.uniprot.org/annotation/PRO_0000296224|||http://purl.uniprot.org/annotation/PRO_5014296589|||http://purl.uniprot.org/annotation/VAR_048714
http://togogenome.org/gene/9606:ARMCX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5M7|||http://purl.uniprot.org/uniprot/Q7L311                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||Armadillo repeat-containing|||Armadillo repeat-containing X-linked protein 2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191364
http://togogenome.org/gene/9606:KDM4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFL8|||http://purl.uniprot.org/uniprot/F5GX28|||http://purl.uniprot.org/uniprot/O94953                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes lysine-specific histone demethylase activity.|||Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||In MRD65.|||In MRD65; unknown pathological significance.|||In isoform 2.|||JmjC|||JmjN|||Lysine-specific demethylase 4B|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183175|||http://purl.uniprot.org/annotation/VAR_026223|||http://purl.uniprot.org/annotation/VAR_026224|||http://purl.uniprot.org/annotation/VAR_085967|||http://purl.uniprot.org/annotation/VAR_085968|||http://purl.uniprot.org/annotation/VAR_085969|||http://purl.uniprot.org/annotation/VAR_085970|||http://purl.uniprot.org/annotation/VSP_018307|||http://purl.uniprot.org/annotation/VSP_018308
http://togogenome.org/gene/9606:MAGEB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43366                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen B1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156712|||http://purl.uniprot.org/annotation/VAR_053499
http://togogenome.org/gene/9606:SUSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WAQ1|||http://purl.uniprot.org/uniprot/Q6UWL2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 2|||Sushi domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251972|||http://purl.uniprot.org/annotation/PRO_5003385534|||http://purl.uniprot.org/annotation/VAR_027743|||http://purl.uniprot.org/annotation/VAR_051390|||http://purl.uniprot.org/annotation/VSP_020832|||http://purl.uniprot.org/annotation/VSP_026677
http://togogenome.org/gene/9606:RABEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMM4|||http://purl.uniprot.org/uniprot/Q15276                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the interaction with AP1G1, AP1G2, GGA1, GGA2 and GGA3.|||Abolishes the interaction with AP1G2, GGA1 and GGA2.|||Disordered|||In isoform 2.|||Interaction with AP1G1, AP1G2, GGA1, GGA2 and GGA3|||N-acetylalanine|||N6-acetyllysine|||No effect on RAB5A binding affinity.|||Phosphoserine|||Phosphothreonine|||Rab GTPase-binding effector protein 1|||Rabaptin GTPase-Rab5 binding|||Rabaptin coiled-coil|||Reduces the interaction with AP1G1 and GGA3.|||Reduces the interaction with AP1G2, GGA1, GGA2.|||Removed|||Strongly decreases RAB5A binding affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187556|||http://purl.uniprot.org/annotation/VAR_028106|||http://purl.uniprot.org/annotation/VSP_010451
http://togogenome.org/gene/9606:SLC41A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JW4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Solute carrier family 41 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295040
http://togogenome.org/gene/9606:GAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4W2|||http://purl.uniprot.org/uniprot/B3KTC3|||http://purl.uniprot.org/uniprot/Q9H2C0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||Gigaxonin|||In GAN1.|||In GAN1; complete loss of binding to TBCB.|||In GAN1; no effect on binding to TBCB.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Probable disease-associated variant found in hereditary motor and sensory neuropathy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119070|||http://purl.uniprot.org/annotation/VAR_010757|||http://purl.uniprot.org/annotation/VAR_010759|||http://purl.uniprot.org/annotation/VAR_010760|||http://purl.uniprot.org/annotation/VAR_010761|||http://purl.uniprot.org/annotation/VAR_010762|||http://purl.uniprot.org/annotation/VAR_010763|||http://purl.uniprot.org/annotation/VAR_010764|||http://purl.uniprot.org/annotation/VAR_010765|||http://purl.uniprot.org/annotation/VAR_010766|||http://purl.uniprot.org/annotation/VAR_010767|||http://purl.uniprot.org/annotation/VAR_015560|||http://purl.uniprot.org/annotation/VAR_015680|||http://purl.uniprot.org/annotation/VAR_015681|||http://purl.uniprot.org/annotation/VAR_054113|||http://purl.uniprot.org/annotation/VAR_054114|||http://purl.uniprot.org/annotation/VAR_054115|||http://purl.uniprot.org/annotation/VAR_054116|||http://purl.uniprot.org/annotation/VAR_054117|||http://purl.uniprot.org/annotation/VAR_054118|||http://purl.uniprot.org/annotation/VAR_073289|||http://purl.uniprot.org/annotation/VAR_073290
http://togogenome.org/gene/9606:CAMK2N2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S95                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Calcium/calmodulin-dependent protein kinase II inhibitor 2|||Disordered|||Inhibitory domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327266
http://togogenome.org/gene/9606:TMEM50B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56557                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylalanine|||Removed|||Transmembrane protein 50B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174183
http://togogenome.org/gene/9606:CLU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10909                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Affects proteolytic cleavage.|||Cleavage|||Clusterin|||Clusterin alpha chain|||Clusterin beta chain|||Decreases molecular mass of alpha chain; when associated with Q-291 and Q-354. Decreases secretion; when associated with Q-291 and Q-354.|||Decreases molecular mass of alpha chain; when associated with Q-291 and Q-374. Decreases secretion; when associated with Q-291 and Q-374.|||Decreases molecular mass of alpha chain; when associated with Q-354 and Q-374. Decreases secretion; when associated with Q-354 and Q-374.|||Decreases molecular mass of beta chain; when associated with Q-103 and Q-145.|||Decreases molecular mass of beta chain; when associated with Q-86 and Q-103.|||Decreases molecular mass of beta chain; when associated with Q-86 and Q-145.|||Does not affect proteolytic cleavage.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interchain (between beta and alpha chains)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005529|||http://purl.uniprot.org/annotation/PRO_0000005530|||http://purl.uniprot.org/annotation/PRO_0000005531|||http://purl.uniprot.org/annotation/VAR_019366|||http://purl.uniprot.org/annotation/VAR_019367|||http://purl.uniprot.org/annotation/VAR_019368|||http://purl.uniprot.org/annotation/VSP_037661|||http://purl.uniprot.org/annotation/VSP_041475|||http://purl.uniprot.org/annotation/VSP_041476|||http://purl.uniprot.org/annotation/VSP_041477|||http://purl.uniprot.org/annotation/VSP_060188|||http://purl.uniprot.org/annotation/VSP_060192
http://togogenome.org/gene/9606:SAA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJI9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Amyloid A2 protein|||Disordered|||In allele SAA2.1.|||In isoform 2.|||Serum amyloid A-2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000418061|||http://purl.uniprot.org/annotation/PRO_0000450359|||http://purl.uniprot.org/annotation/VAR_006930|||http://purl.uniprot.org/annotation/VSP_045626
http://togogenome.org/gene/9606:ERBB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H1T4|||http://purl.uniprot.org/uniprot/J3QLU9|||http://purl.uniprot.org/uniprot/P04626|||http://purl.uniprot.org/uniprot/X5DNK3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Furin-like cysteine-rich|||Growth factor receptor|||Helical|||In GASC; somatic mutation; unknown pathological significance.|||In GLM; somatic mutation; unknown pathological significance.|||In LNCR; somatic mutation; unknown pathological significance.|||In OC; somatic mutation; unknown pathological significance.|||In VSCN2; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane.|||In allele B2 and allele B3.|||In allele B3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with PIK3C2B|||N-linked (GlcNAc...) asparagine|||No effect on isoform production.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Prevents synthesis of isoform 2.|||Prevents synthesis of isoform 3.|||Pro residues|||Protein kinase|||Proton acceptor|||Receptor L-domain|||Receptor protein-tyrosine kinase|||Receptor tyrosine-protein kinase erbB-2|||Reduces dimerization with ERBB3.|||Required for interaction with KPNB1 and EEA1|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016669|||http://purl.uniprot.org/annotation/PRO_5003776645|||http://purl.uniprot.org/annotation/PRO_5004954909|||http://purl.uniprot.org/annotation/VAR_004077|||http://purl.uniprot.org/annotation/VAR_004078|||http://purl.uniprot.org/annotation/VAR_016317|||http://purl.uniprot.org/annotation/VAR_016318|||http://purl.uniprot.org/annotation/VAR_042097|||http://purl.uniprot.org/annotation/VAR_042098|||http://purl.uniprot.org/annotation/VAR_042099|||http://purl.uniprot.org/annotation/VAR_042100|||http://purl.uniprot.org/annotation/VAR_055432|||http://purl.uniprot.org/annotation/VAR_055433|||http://purl.uniprot.org/annotation/VAR_055434|||http://purl.uniprot.org/annotation/VAR_055435|||http://purl.uniprot.org/annotation/VAR_086107|||http://purl.uniprot.org/annotation/VSP_039248|||http://purl.uniprot.org/annotation/VSP_039249|||http://purl.uniprot.org/annotation/VSP_039250|||http://purl.uniprot.org/annotation/VSP_054787|||http://purl.uniprot.org/annotation/VSP_055902|||http://purl.uniprot.org/annotation/VSP_055903|||http://purl.uniprot.org/annotation/VSP_055904
http://togogenome.org/gene/9606:PIK3CG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9G9|||http://purl.uniprot.org/uniprot/P48736                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes protein and lipid kinase activity. Does not abolish interaction with GRK2.|||Activation loop|||C2 PI3K-type|||Catalytic loop|||G-loop|||In IMD97; loss of phosphatidylinositol-3,4-bisphosphate 5-kinase activity.|||In IMD97; loss-of-function variant unable to rescue reduced T-cell activation when expressed in Jurkat PIK3CG-deficient cells.|||Loss of autophosphorylation. No effect on phosphatidylinositol-4,5-bisphosphate 3-kinase activity.|||Loss of kinase activity. Loss of autophosphorylation. Reduced inflammatory reactions but no alterations in cardiac contractility.|||PI3K-ABD|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform|||Phosphoserine; by autocatalysis|||Phosphothreonine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088792|||http://purl.uniprot.org/annotation/VAR_087092|||http://purl.uniprot.org/annotation/VAR_087093|||http://purl.uniprot.org/annotation/VAR_087094
http://togogenome.org/gene/9606:OXER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDS5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Oxoeicosanoid receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069993|||http://purl.uniprot.org/annotation/VAR_023940|||http://purl.uniprot.org/annotation/VAR_049428
http://togogenome.org/gene/9606:GINS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14691                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Mass|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mass|||Sequence Variant|||Strand                                                                                  ^@                                                                                  DNA replication complex GINS protein PSF1|||In IMD55; lower GINS1 protein levels and defective DNA replication are observed in patient cells.|||In IMD55; lower GINS1 protein levels and defective DNA replication are observed in patient cells; the mutant does not interact with GINS3 and GINS4.|||This is the measured mass for the GINS complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219035|||http://purl.uniprot.org/annotation/VAR_051606|||http://purl.uniprot.org/annotation/VAR_080619|||http://purl.uniprot.org/annotation/VAR_080620
http://togogenome.org/gene/9606:RCSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKW8|||http://purl.uniprot.org/uniprot/Q6JBY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CapZ-interacting protein|||Disordered|||FAM21/CAPZIP|||In isoform 2.|||Phosphoserine|||Phosphoserine; by MAPK12 and MAPK13|||Phosphoserine; by MAPK8; in vitro|||Phosphoserine; by MAPKAPK2 and MAPKAPK3|||Phosphoserine; by MAPKAPK2 or MAPKAPK3; in vitro|||Phosphothreonine|||Polar residues|||RCSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320262|||http://purl.uniprot.org/annotation/VAR_039181|||http://purl.uniprot.org/annotation/VSP_031648
http://togogenome.org/gene/9606:ATP6V0B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PNL3|||http://purl.uniprot.org/uniprot/Q99437                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Essential for proton translocation|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Lumenal|||V-ATPase proteolipid subunit C-like|||V-type proton ATPase 21 kDa proteolipid subunit c""" /id="PRO_0000071777                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/VAR_035703|||http://purl.uniprot.org/annotation/VSP_046288
http://togogenome.org/gene/9606:OSBPL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYM3|||http://purl.uniprot.org/uniprot/Q9BZF1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Impaired lipid countertransport between the endoplasmic reticulum and the plasma membrane.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Oxysterol-binding protein-related protein 8|||PH|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100378|||http://purl.uniprot.org/annotation/VSP_009120|||http://purl.uniprot.org/annotation/VSP_045801
http://togogenome.org/gene/9606:PLA2G2E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZK7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Group IIE secretory phospholipase A2|||Loss of catalytic activity.|||Significantly decreases the catalytic efficiency.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022757
http://togogenome.org/gene/9606:PSMC3IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RUX1|||http://purl.uniprot.org/uniprot/K7ERB6|||http://purl.uniprot.org/uniprot/Q9P2W1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-binding|||Homologous-pairing protein 2 homolog|||Homologous-pairing protein 2 winged helix|||In ODG3; impairs function as estrogen receptor coactivator.|||In isoform 2.|||In isoform 3.|||Leucine zipper with capping helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314135|||http://purl.uniprot.org/annotation/VAR_037841|||http://purl.uniprot.org/annotation/VAR_066636|||http://purl.uniprot.org/annotation/VSP_030213|||http://purl.uniprot.org/annotation/VSP_047716
http://togogenome.org/gene/9606:DEFB134                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4QY38                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 134                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045360
http://togogenome.org/gene/9606:WDR87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZG8|||http://purl.uniprot.org/uniprot/E7ESW6|||http://purl.uniprot.org/uniprot/Q6ZQQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 87                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314821|||http://purl.uniprot.org/annotation/VAR_057638|||http://purl.uniprot.org/annotation/VAR_057639|||http://purl.uniprot.org/annotation/VAR_057640|||http://purl.uniprot.org/annotation/VAR_057641|||http://purl.uniprot.org/annotation/VSP_030380
http://togogenome.org/gene/9606:BANF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75531                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Turn                                                                                  ^@                                                                                  (Microbial infection) Phosphothreonine; by viral VacV B1 kinase|||75% cytoplasmic localization.|||85% cytoplasmic localization.|||95% nuclear localization. Loss of BAF phosphorylation and ability to suppress vaccinia virus DNA replication.|||Abolishes homodimerization, preventing ability to cross-bridge DNA. Abolished ability to mediate nuclear membrane reformation at the end of mitosis. Abolished ability to outcompete CGAS for DNA-binding, leading to innate immune activation. Complete loss of EMD, histone H1/H3 and LEMD3/MAN1 binding.|||Abolishes interaction with LEM domain-containing proteins without affecting homodimerization and DNA-binding. Does not affect its involvement in nuclear membrane reformation at the end of mitosis. Does not affect ability to outcompete CGAS for DNA-binding.|||Barrier-to-autointegration factor|||Barrier-to-autointegration factor, N-terminally processed|||Complete loss of EMD binding and reduces dsDNA binding.|||Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding.|||Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding.|||Complete loss of LEMD3/MAN1 and histone H1/H3 binding.|||Complete loss of LEMD3/MAN1 binding.|||Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding.|||Complete loss of dsDNA and LEMD3/MAN1 binding.|||Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding.|||Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding.|||Complete loss of phosphorylation and mislocalization of EMD in nucleus.|||Delayed phosphorylation with a 10-fold decrease in the initial phosphorylation rate. 71% loss of binding to lamin A.|||Enhances histone H1/H3 binding.|||Fails to bind dsDNA.|||Fails to promote HIV-1 genome integration.|||HhH|||In NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability.|||N-acetylmethionine|||N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processed|||No effect on LEMD3/MAN1 and enhances histone H1/H3 binding.|||No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding.|||No effect on histone H1/H3 and LEMD3/MAN1 binding.|||No effect on histone H1/H3 binding.|||No effect on the initial rate of phosphorylation but a second slow phase of phosphorylation is absent.|||Phosphoserine; by viral VacV B1 kinase, VRK1 and VRK2|||Phosphothreonine; by VRK1 and VRK2|||Reduces LEMD3/MAN1 binding.|||Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding.|||Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding.|||Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. Reduced interaction with PARP1.|||Reduces binding to dsDNA.|||Reduces binding to dsDNA. No effect on histone H1/H3 binding.|||Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration.|||Reduces histone H1/H3 binding.|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221026|||http://purl.uniprot.org/annotation/PRO_0000423190|||http://purl.uniprot.org/annotation/VAR_065954
http://togogenome.org/gene/9606:SNRPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62318                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 2 AA tandem repeats of [RM]-G; required for interaction with SMN1|||In isoform 2.|||N-acetylserine|||Removed|||Sm|||Small nuclear ribonucleoprotein Sm D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122214|||http://purl.uniprot.org/annotation/VSP_056478
http://togogenome.org/gene/9606:PNLDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NA58                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In SPGF57.|||In SPGF57; unknown pathological significance.|||In isoform 2.|||Interaction with poly(A)|||Poly(A)-specific ribonuclease PNLDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311365|||http://purl.uniprot.org/annotation/VAR_085807|||http://purl.uniprot.org/annotation/VAR_085808|||http://purl.uniprot.org/annotation/VAR_085809|||http://purl.uniprot.org/annotation/VSP_029552
http://togogenome.org/gene/9606:CLPSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWE3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Colipase-like protein 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022608|||http://purl.uniprot.org/annotation/VSP_035621
http://togogenome.org/gene/9606:NDUFA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16718                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118632|||http://purl.uniprot.org/annotation/VSP_055164
http://togogenome.org/gene/9606:HOXC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31273                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Antp-type hexapeptide|||Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-C8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200180
http://togogenome.org/gene/9606:ZBTB25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V2K3|||http://purl.uniprot.org/uniprot/P24278                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type 1|||C2H2-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger and BTB domain-containing protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047738
http://togogenome.org/gene/9606:GPR89B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAQ6|||http://purl.uniprot.org/uniprot/P0CG08|||http://purl.uniprot.org/uniprot/X5D7G6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abscisic acid G-protein coupled receptor-like|||Golgi pH regulator A|||Golgi pH regulator B|||Golgi pH regulator conserved|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223260|||http://purl.uniprot.org/annotation/PRO_0000395006|||http://purl.uniprot.org/annotation/VSP_017247|||http://purl.uniprot.org/annotation/VSP_039346|||http://purl.uniprot.org/annotation/VSP_055892|||http://purl.uniprot.org/annotation/VSP_055893
http://togogenome.org/gene/9606:ERCC6L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T890                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||DNA excision repair protein ERCC-6-like 2|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326086|||http://purl.uniprot.org/annotation/VAR_039987|||http://purl.uniprot.org/annotation/VSP_054666|||http://purl.uniprot.org/annotation/VSP_054667|||http://purl.uniprot.org/annotation/VSP_054668|||http://purl.uniprot.org/annotation/VSP_054669
http://togogenome.org/gene/9606:ZNF780A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75290|||http://purl.uniprot.org/uniprot/Q05CQ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 780A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263690|||http://purl.uniprot.org/annotation/VSP_037718|||http://purl.uniprot.org/annotation/VSP_037719|||http://purl.uniprot.org/annotation/VSP_037720|||http://purl.uniprot.org/annotation/VSP_046465
http://togogenome.org/gene/9606:CCDC169-SOHLH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315700|||http://purl.uniprot.org/annotation/VAR_038283|||http://purl.uniprot.org/annotation/VAR_038284|||http://purl.uniprot.org/annotation/VSP_030652|||http://purl.uniprot.org/annotation/VSP_030653|||http://purl.uniprot.org/annotation/VSP_042423
http://togogenome.org/gene/9606:HSD17B10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z410|||http://purl.uniprot.org/uniprot/Q99714                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyacyl-CoA dehydrogenase type-2|||Abolishes dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation. Does not affect homotetramerization.|||Decreased dehydrogenase activity. Does not affect mitochondrial tRNA 5'-end processing. Does not affect tRNA methylation.|||In HSD10MD.|||In HSD10MD; 4-fold decrease of 3-hydroxyacyl-CoA dehydrogenase activity; decreased interaction with TRMT10C; decreased function in mitochondrial tRNA methylation; decreased function in mitochondrial tRNA processing.|||In HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity.|||In HSD10MD; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; no effect on NAD(+) binding; complete loss of phospholipase C-like activity toward cardiolipin.|||In HSD10MD; decreased 3-hydroxyacyl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization.|||In HSD10MD; decreased dehydrogenase activity; decreased tRNA methylation; decreased mitochondrial tRNA 5'-end processing.|||In HSD10MD; decreased dehydrogenase activity; strongly decreased tRNA methylation; strongly decreased mitochondrial tRNA 5'-end processing.|||In HSD10MD; decreased stability; decreased 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; decreased mitochondrial tRNA 5'-end processing; decreased tRNA methylation; does not affect homotetramerization; complete loss of phospholipase C-like activity toward cardiolipin.|||In HSD10MD; loss of 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; does not bind NAD(+); complete loss of phospholipase C-like activity toward cardiolipin.|||In HSD10MD; strongly decreased 3-hydroxyacyl-CoA dehydrogenase activity; abolished mitochondrial tRNA 5'-end processing; abolished tRNA methylation; impaired homotetramerization.|||In HSD10MD; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054810|||http://purl.uniprot.org/annotation/VAR_015987|||http://purl.uniprot.org/annotation/VAR_015988|||http://purl.uniprot.org/annotation/VAR_032093|||http://purl.uniprot.org/annotation/VAR_078863|||http://purl.uniprot.org/annotation/VAR_078864|||http://purl.uniprot.org/annotation/VAR_078865|||http://purl.uniprot.org/annotation/VAR_078866|||http://purl.uniprot.org/annotation/VAR_078867|||http://purl.uniprot.org/annotation/VAR_080049|||http://purl.uniprot.org/annotation/VAR_080050|||http://purl.uniprot.org/annotation/VAR_080051|||http://purl.uniprot.org/annotation/VAR_080052|||http://purl.uniprot.org/annotation/VSP_007830
http://togogenome.org/gene/9606:ACVRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z310|||http://purl.uniprot.org/uniprot/P37023                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affinity for BMP9 decreased by 200-fold.|||Cytoplasmic|||Extracellular|||Found in a patient with hereditary hemorrhagic talagiectasia; unknown pathological significance.|||Found in a patient with pulmonary arterial hypertension; unknown pathological significance.|||Found in patients with pulmonary arterial hypertension; unknown pathological significance.|||GS|||Helical|||In HHT2.|||In HHT2; loss of receptor activity in response to BMP9; predominantly retained in the endoplasmic reticulum.|||In HHT2; loss of receptor activity in response to BMP9; retained in the endoplasmic reticulum.|||In HHT2; mutant protein is capable of targeting the cell surface appropriately.|||In HHT2; no loss of receptor activity in response to BMP9; mutant protein is capable of targeting the cell surface appropriately; affects splicing by inducing the creation of a new donor splice site and the loss of the 3' end of exon 6.|||In HHT2; retained in the endoplasmic reticulum.|||Mediates specificity for BMP ligand|||N-linked (GlcNAc...) asparagine|||No loss of receptor activity in response to BMP9; mutant protein is capable of targeting the cell surface appropriately.|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase receptor|||Serine/threonine-protein kinase receptor R3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024420|||http://purl.uniprot.org/annotation/PRO_5006608194|||http://purl.uniprot.org/annotation/VAR_006204|||http://purl.uniprot.org/annotation/VAR_006205|||http://purl.uniprot.org/annotation/VAR_006206|||http://purl.uniprot.org/annotation/VAR_006207|||http://purl.uniprot.org/annotation/VAR_006208|||http://purl.uniprot.org/annotation/VAR_006209|||http://purl.uniprot.org/annotation/VAR_006210|||http://purl.uniprot.org/annotation/VAR_006211|||http://purl.uniprot.org/annotation/VAR_006212|||http://purl.uniprot.org/annotation/VAR_006213|||http://purl.uniprot.org/annotation/VAR_006214|||http://purl.uniprot.org/annotation/VAR_011717|||http://purl.uniprot.org/annotation/VAR_026784|||http://purl.uniprot.org/annotation/VAR_026785|||http://purl.uniprot.org/annotation/VAR_026786|||http://purl.uniprot.org/annotation/VAR_026787|||http://purl.uniprot.org/annotation/VAR_026788|||http://purl.uniprot.org/annotation/VAR_026789|||http://purl.uniprot.org/annotation/VAR_026790|||http://purl.uniprot.org/annotation/VAR_026791|||http://purl.uniprot.org/annotation/VAR_026792|||http://purl.uniprot.org/annotation/VAR_026793|||http://purl.uniprot.org/annotation/VAR_026794|||http://purl.uniprot.org/annotation/VAR_026795|||http://purl.uniprot.org/annotation/VAR_026796|||http://purl.uniprot.org/annotation/VAR_026797|||http://purl.uniprot.org/annotation/VAR_026798|||http://purl.uniprot.org/annotation/VAR_026799|||http://purl.uniprot.org/annotation/VAR_026800|||http://purl.uniprot.org/annotation/VAR_026801|||http://purl.uniprot.org/annotation/VAR_026802|||http://purl.uniprot.org/annotation/VAR_026803|||http://purl.uniprot.org/annotation/VAR_026804|||http://purl.uniprot.org/annotation/VAR_026805|||http://purl.uniprot.org/annotation/VAR_026806|||http://purl.uniprot.org/annotation/VAR_026807|||http://purl.uniprot.org/annotation/VAR_026808|||http://purl.uniprot.org/annotation/VAR_026809|||http://purl.uniprot.org/annotation/VAR_026810|||http://purl.uniprot.org/annotation/VAR_026811|||http://purl.uniprot.org/annotation/VAR_026812|||http://purl.uniprot.org/annotation/VAR_026813|||http://purl.uniprot.org/annotation/VAR_026814|||http://purl.uniprot.org/annotation/VAR_026815|||http://purl.uniprot.org/annotation/VAR_026816|||http://purl.uniprot.org/annotation/VAR_070308|||http://purl.uniprot.org/annotation/VAR_070309|||http://purl.uniprot.org/annotation/VAR_070310|||http://purl.uniprot.org/annotation/VAR_070311|||http://purl.uniprot.org/annotation/VAR_070312|||http://purl.uniprot.org/annotation/VAR_070313|||http://purl.uniprot.org/annotation/VAR_070314|||http://purl.uniprot.org/annotation/VAR_070315|||http://purl.uniprot.org/annotation/VAR_070316|||http://purl.uniprot.org/annotation/VAR_070317|||http://purl.uniprot.org/annotation/VAR_070318|||http://purl.uniprot.org/annotation/VAR_070319|||http://purl.uniprot.org/annotation/VAR_070320|||http://purl.uniprot.org/annotation/VAR_070321|||http://purl.uniprot.org/annotation/VAR_070322|||http://purl.uniprot.org/annotation/VAR_070323|||http://purl.uniprot.org/annotation/VAR_070324|||http://purl.uniprot.org/annotation/VAR_070325|||http://purl.uniprot.org/annotation/VAR_070326|||http://purl.uniprot.org/annotation/VAR_070327|||http://purl.uniprot.org/annotation/VAR_070328|||http://purl.uniprot.org/annotation/VAR_070329|||http://purl.uniprot.org/annotation/VAR_070330|||http://purl.uniprot.org/annotation/VAR_070331|||http://purl.uniprot.org/annotation/VAR_070332|||http://purl.uniprot.org/annotation/VAR_070333|||http://purl.uniprot.org/annotation/VAR_070334|||http://purl.uniprot.org/annotation/VAR_070335|||http://purl.uniprot.org/annotation/VAR_070336|||http://purl.uniprot.org/annotation/VAR_070337|||http://purl.uniprot.org/annotation/VAR_070338|||http://purl.uniprot.org/annotation/VAR_070339|||http://purl.uniprot.org/annotation/VAR_070340|||http://purl.uniprot.org/annotation/VAR_070341|||http://purl.uniprot.org/annotation/VAR_070342|||http://purl.uniprot.org/annotation/VAR_070343|||http://purl.uniprot.org/annotation/VAR_070344|||http://purl.uniprot.org/annotation/VAR_075231|||http://purl.uniprot.org/annotation/VAR_075232|||http://purl.uniprot.org/annotation/VAR_075233|||http://purl.uniprot.org/annotation/VAR_075234|||http://purl.uniprot.org/annotation/VAR_075235|||http://purl.uniprot.org/annotation/VAR_075236|||http://purl.uniprot.org/annotation/VAR_075237|||http://purl.uniprot.org/annotation/VAR_075238|||http://purl.uniprot.org/annotation/VAR_075239|||http://purl.uniprot.org/annotation/VAR_075240|||http://purl.uniprot.org/annotation/VAR_075241|||http://purl.uniprot.org/annotation/VAR_075242|||http://purl.uniprot.org/annotation/VAR_075243|||http://purl.uniprot.org/annotation/VAR_075244|||http://purl.uniprot.org/annotation/VAR_075245|||http://purl.uniprot.org/annotation/VAR_079583|||http://purl.uniprot.org/annotation/VAR_079584|||http://purl.uniprot.org/annotation/VAR_079585|||http://purl.uniprot.org/annotation/VAR_079586|||http://purl.uniprot.org/annotation/VAR_079587
http://togogenome.org/gene/9606:DHX34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14147                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||Negatively regulates interaction with UPF1|||Phosphoserine|||Probable ATP-dependent RNA helicase DHX34|||Required for phosphorylation of UPF1. Not required for interaction with UPF1|||Required for the interaction with SMG1 and subsequent phosphorylation of UPF1|||Results in interaction with ETF1/eRF1, GSPT1/eRF3a and GSPT2/eRF3b. Increases mRNA binding. Reduces UPF1 phosphorylation. Reduces ATPase activity. No effect on interaction with SMG1.|||Results in interaction with ETF1/eRF1, GSPT1/eRF3a and GSPT2/eRF3b. Reduces UPF1 phosphorylation. No effect on mRNA binding or interaction with SMG1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055166|||http://purl.uniprot.org/annotation/VAR_057241|||http://purl.uniprot.org/annotation/VAR_057242|||http://purl.uniprot.org/annotation/VAR_083625|||http://purl.uniprot.org/annotation/VAR_083626|||http://purl.uniprot.org/annotation/VAR_083627
http://togogenome.org/gene/9606:OR4C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGB2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4C5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150530
http://togogenome.org/gene/9606:KRTAP22-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI68                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 22-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336084
http://togogenome.org/gene/9606:NYNRIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2P1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Integrase catalytic|||Polar residues|||Protein NYNRIN|||RNase H type-1|||RNase NYN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314174|||http://purl.uniprot.org/annotation/VAR_037857|||http://purl.uniprot.org/annotation/VAR_037858|||http://purl.uniprot.org/annotation/VAR_037859|||http://purl.uniprot.org/annotation/VAR_037860|||http://purl.uniprot.org/annotation/VAR_037861|||http://purl.uniprot.org/annotation/VSP_030237|||http://purl.uniprot.org/annotation/VSP_030238|||http://purl.uniprot.org/annotation/VSP_030239
http://togogenome.org/gene/9606:NOS1AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75052                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein|||Disordered|||In NPHS22; loss of promotion of filipodia and podosome formation and migration.|||In isoform 2.|||In isoform 3.|||Interaction with NOS1|||PDZ-binding|||PID|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089316|||http://purl.uniprot.org/annotation/VAR_085238|||http://purl.uniprot.org/annotation/VSP_042751|||http://purl.uniprot.org/annotation/VSP_042752|||http://purl.uniprot.org/annotation/VSP_043350
http://togogenome.org/gene/9606:TCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2TDC0|||http://purl.uniprot.org/uniprot/O15273                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with dilated cardiomyopathy; unknown pathological significance.|||In CMH25.|||In CMH25; increased interaction with TTN and MYOZ2.|||In CMH25; unknown pathological significance.|||Phosphoserine|||Probable disease-associated variant found in a patient with dilated cardiomyopathy; impairs the interaction with CSRP3, TTN and MYOZ2.|||Telethonin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072483|||http://purl.uniprot.org/annotation/VAR_015397|||http://purl.uniprot.org/annotation/VAR_026649|||http://purl.uniprot.org/annotation/VAR_026650|||http://purl.uniprot.org/annotation/VAR_026651|||http://purl.uniprot.org/annotation/VAR_029445|||http://purl.uniprot.org/annotation/VAR_029446|||http://purl.uniprot.org/annotation/VAR_029447|||http://purl.uniprot.org/annotation/VAR_029448|||http://purl.uniprot.org/annotation/VAR_051421
http://togogenome.org/gene/9606:REPIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8H1|||http://purl.uniprot.org/uniprot/Q9BWE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Replication initiator 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274912|||http://purl.uniprot.org/annotation/VAR_030364|||http://purl.uniprot.org/annotation/VAR_030365|||http://purl.uniprot.org/annotation/VAR_030366|||http://purl.uniprot.org/annotation/VAR_030367|||http://purl.uniprot.org/annotation/VAR_052730|||http://purl.uniprot.org/annotation/VSP_054069
http://togogenome.org/gene/9606:ARSJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FYB0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Arylsulfatase J|||Basic residues|||Disordered|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042217|||http://purl.uniprot.org/annotation/VAR_052515
http://togogenome.org/gene/9606:KMT5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SF94|||http://purl.uniprot.org/uniprot/Q86Y97                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Histone-lysine N-methyltransferase KMT5C|||In isoform 2.|||Phosphothreonine|||Required for heterochromatin localization|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281793|||http://purl.uniprot.org/annotation/VSP_043947|||http://purl.uniprot.org/annotation/VSP_043948
http://togogenome.org/gene/9606:NTPCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TDE9|||http://purl.uniprot.org/uniprot/Q9BSD7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||Cancer-related nucleoside-triphosphatase|||N-acetylalanine|||N6-acetyllysine|||Reduced activity, especially towards ATP, GTP and TTP.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146711|||http://purl.uniprot.org/annotation/VAR_053071
http://togogenome.org/gene/9606:GNA15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30679                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203755|||http://purl.uniprot.org/annotation/VAR_028000
http://togogenome.org/gene/9606:CPVL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3G5                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Probable serine carboxypeptidase CPVL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004280|||http://purl.uniprot.org/annotation/PRO_0000004281|||http://purl.uniprot.org/annotation/VAR_022612|||http://purl.uniprot.org/annotation/VAR_048681|||http://purl.uniprot.org/annotation/VAR_048682|||http://purl.uniprot.org/annotation/VAR_048683
http://togogenome.org/gene/9606:TRAPPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUR0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Trafficking protein particle complex subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211579|||http://purl.uniprot.org/annotation/VAR_052398
http://togogenome.org/gene/9606:AKAIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KS16|||http://purl.uniprot.org/uniprot/P0CW23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  A-kinase anchor protein 7 RI-RII subunit-binding|||A-kinase anchor protein inhibitor 1|||Basic and acidic residues|||Disordered|||PKA-RII subunit binding domain|||Reduces binding to RII subunits of PKA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410771
http://togogenome.org/gene/9606:C1orf198                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H425                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Uncharacterized protein C1orf198                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280342|||http://purl.uniprot.org/annotation/VAR_050707|||http://purl.uniprot.org/annotation/VAR_050708|||http://purl.uniprot.org/annotation/VSP_044252|||http://purl.uniprot.org/annotation/VSP_046926
http://togogenome.org/gene/9606:GSTM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKE3|||http://purl.uniprot.org/uniprot/Q03013                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 4|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185824|||http://purl.uniprot.org/annotation/VAR_033979|||http://purl.uniprot.org/annotation/VAR_033980|||http://purl.uniprot.org/annotation/VAR_049487|||http://purl.uniprot.org/annotation/VAR_049488|||http://purl.uniprot.org/annotation/VAR_049489|||http://purl.uniprot.org/annotation/VAR_049490|||http://purl.uniprot.org/annotation/VSP_011773|||http://purl.uniprot.org/annotation/VSP_011774|||http://purl.uniprot.org/annotation/VSP_047688
http://togogenome.org/gene/9606:MCRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EZ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FHA|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Microspherule protein 1|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096305|||http://purl.uniprot.org/annotation/VAR_035473|||http://purl.uniprot.org/annotation/VSP_016259|||http://purl.uniprot.org/annotation/VSP_016260|||http://purl.uniprot.org/annotation/VSP_054571
http://togogenome.org/gene/9606:SYT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT88                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||Phosphoserine|||Polar residues|||Synaptotagmin-11|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183969|||http://purl.uniprot.org/annotation/VAR_047656|||http://purl.uniprot.org/annotation/VAR_047657
http://togogenome.org/gene/9606:GPR31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00270                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069551|||http://purl.uniprot.org/annotation/VAR_049392
http://togogenome.org/gene/9606:SLAMF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0V8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||SLAM family member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014965|||http://purl.uniprot.org/annotation/VAR_049940|||http://purl.uniprot.org/annotation/VAR_049941|||http://purl.uniprot.org/annotation/VAR_049942|||http://purl.uniprot.org/annotation/VSP_013896
http://togogenome.org/gene/9606:CCDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXW2|||http://purl.uniprot.org/uniprot/Q9Y3X0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Coiled-coil domain-containing protein 9|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089403|||http://purl.uniprot.org/annotation/VAR_033670|||http://purl.uniprot.org/annotation/VAR_033671|||http://purl.uniprot.org/annotation/VAR_050767
http://togogenome.org/gene/9606:CD5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43866                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CD5 antigen-like|||No effect; when associated with 129-A--A-132.|||No effect; when associated with A-123.|||SRCR 1|||SRCR 2|||SRCR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033225|||http://purl.uniprot.org/annotation/VAR_033728
http://togogenome.org/gene/9606:SAR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR31                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases transport of STING1 from the endoplasmic reticulum to the Golgi.|||GTP-binding protein SAR1a|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206258|||http://purl.uniprot.org/annotation/VSP_056220
http://togogenome.org/gene/9606:HPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02790|||http://purl.uniprot.org/uniprot/Q9BS19                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Hemopexin|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Hemopexin 5|||Hemopexin 6|||Hemopexin 7|||Hemopexin 8|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) threonine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021406|||http://purl.uniprot.org/annotation/PRO_5014312668|||http://purl.uniprot.org/annotation/VAR_033990|||http://purl.uniprot.org/annotation/VAR_047137
http://togogenome.org/gene/9606:PDCD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUL8                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-172.|||Loss of interaction with CCM2 and PXN; when associated with D-132; D-139 and D-179.|||Loss of interaction with CCM2 and PXN; when associated with D-132; D-172 and D-179.|||Loss of interaction with CCM2 and PXN; when associated with D-139; D-172 and D-179.|||Loss of interaction with CCM2.|||N6-acetyllysine|||Programmed cell death protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187562|||http://purl.uniprot.org/annotation/VAR_023578
http://togogenome.org/gene/9606:RNF114                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y508                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC RNF-type|||E3 ubiquitin-protein ligase RNF114|||In isoform 2.|||N6-acetyllysine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056307|||http://purl.uniprot.org/annotation/VSP_036843|||http://purl.uniprot.org/annotation/VSP_036844
http://togogenome.org/gene/9606:RAB5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61020                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active.|||Constitutively inactivated. Strongly reduces interaction with RIN2.|||Disordered|||Effector region|||In isoform 2.|||Loss of phosphorylation. No effect on GDI1, GDI2, CHML and CHM binding.|||N-acetylthreonine|||Phosphomimetic mutant. Loss of GDI1, GDI2, CHML and CHM binding.|||Phosphoserine; by LRRK2|||Polar residues|||Ras-related protein Rab-5B|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121107|||http://purl.uniprot.org/annotation/VSP_045301
http://togogenome.org/gene/9606:DOK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P104                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  DKFBH motif|||Docking protein 5|||IRS-type PTB|||In isoform 2.|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187277|||http://purl.uniprot.org/annotation/VSP_003854
http://togogenome.org/gene/9606:BTBD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q07                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||BTB/POZ domain-containing protein 9|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186217|||http://purl.uniprot.org/annotation/VSP_042543|||http://purl.uniprot.org/annotation/VSP_042544|||http://purl.uniprot.org/annotation/VSP_044247
http://togogenome.org/gene/9606:PNKD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N490                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In DYT8.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Probable hydrolase PNKD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299549|||http://purl.uniprot.org/annotation/VAR_034844|||http://purl.uniprot.org/annotation/VAR_034845|||http://purl.uniprot.org/annotation/VSP_027736|||http://purl.uniprot.org/annotation/VSP_027737|||http://purl.uniprot.org/annotation/VSP_027738|||http://purl.uniprot.org/annotation/VSP_027739|||http://purl.uniprot.org/annotation/VSP_027740
http://togogenome.org/gene/9606:POGLUT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4H8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Filamin|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein O-glucosyltransferase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247196|||http://purl.uniprot.org/annotation/VAR_027086|||http://purl.uniprot.org/annotation/VSP_019944|||http://purl.uniprot.org/annotation/VSP_019945|||http://purl.uniprot.org/annotation/VSP_019946|||http://purl.uniprot.org/annotation/VSP_019947
http://togogenome.org/gene/9606:MMUT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RD82|||http://purl.uniprot.org/uniprot/B2R6K1|||http://purl.uniprot.org/uniprot/P22033                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  B12-binding|||In MMAM.|||In MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity.|||In MMAM; decreased protein expression.|||In MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity.|||In MMAM; likely benign variant.|||In MMAM; mut- and mut0.|||In MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity.|||In MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability.|||In MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut-.|||In MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin.|||In MMAM; mut-; affects proper folding; no effect on protein abundance; no effect on methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability.|||In MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity.|||In MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability.|||In MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin.|||In MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut-; no effect on protein abundance; interfers with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability.|||In MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut-; unknown pathological significance.|||In MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability.|||In MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability.|||In MMAM; mut0.|||In MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity.|||In MMAM; mut0; affects proper folding; reduced strongly protein level.|||In MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity.|||In MMAM; mut0; decreased methylmalonyl-CoA mutase activity.|||In MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity.|||In MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity.|||In MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity.|||In MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity.|||In MMAM; no effect on protein abundance.|||In MMAM; unknown pathological significance.|||Methylmalonyl-CoA mutase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019293|||http://purl.uniprot.org/annotation/VAR_004409|||http://purl.uniprot.org/annotation/VAR_004410|||http://purl.uniprot.org/annotation/VAR_004411|||http://purl.uniprot.org/annotation/VAR_004412|||http://purl.uniprot.org/annotation/VAR_004413|||http://purl.uniprot.org/annotation/VAR_004414|||http://purl.uniprot.org/annotation/VAR_004415|||http://purl.uniprot.org/annotation/VAR_004416|||http://purl.uniprot.org/annotation/VAR_004417|||http://purl.uniprot.org/annotation/VAR_004418|||http://purl.uniprot.org/annotation/VAR_004419|||http://purl.uniprot.org/annotation/VAR_004420|||http://purl.uniprot.org/annotation/VAR_004421|||http://purl.uniprot.org/annotation/VAR_004422|||http://purl.uniprot.org/annotation/VAR_004423|||http://purl.uniprot.org/annotation/VAR_004424|||http://purl.uniprot.org/annotation/VAR_004425|||http://purl.uniprot.org/annotation/VAR_004426|||http://purl.uniprot.org/annotation/VAR_004427|||http://purl.uniprot.org/annotation/VAR_004428|||http://purl.uniprot.org/annotation/VAR_004429|||http://purl.uniprot.org/annotation/VAR_004430|||http://purl.uniprot.org/annotation/VAR_004431|||http://purl.uniprot.org/annotation/VAR_004432|||http://purl.uniprot.org/annotation/VAR_022393|||http://purl.uniprot.org/annotation/VAR_022394|||http://purl.uniprot.org/annotation/VAR_022395|||http://purl.uniprot.org/annotation/VAR_022396|||http://purl.uniprot.org/annotation/VAR_022397|||http://purl.uniprot.org/annotation/VAR_022398|||http://purl.uniprot.org/annotation/VAR_022399|||http://purl.uniprot.org/annotation/VAR_022400|||http://purl.uniprot.org/annotation/VAR_022401|||http://purl.uniprot.org/annotation/VAR_022402|||http://purl.uniprot.org/annotation/VAR_022403|||http://purl.uniprot.org/annotation/VAR_022404|||http://purl.uniprot.org/annotation/VAR_022405|||http://purl.uniprot.org/annotation/VAR_022406|||http://purl.uniprot.org/annotation/VAR_022407|||http://purl.uniprot.org/annotation/VAR_022408|||http://purl.uniprot.org/annotation/VAR_022409|||http://purl.uniprot.org/annotation/VAR_022410|||http://purl.uniprot.org/annotation/VAR_022411|||http://purl.uniprot.org/annotation/VAR_022412|||http://purl.uniprot.org/annotation/VAR_022413|||http://purl.uniprot.org/annotation/VAR_022414|||http://purl.uniprot.org/annotation/VAR_022415|||http://purl.uniprot.org/annotation/VAR_022416|||http://purl.uniprot.org/annotation/VAR_022417|||http://purl.uniprot.org/annotation/VAR_022418|||http://purl.uniprot.org/annotation/VAR_023472|||http://purl.uniprot.org/annotation/VAR_023473|||http://purl.uniprot.org/annotation/VAR_023474|||http://purl.uniprot.org/annotation/VAR_023475|||http://purl.uniprot.org/annotation/VAR_023476|||http://purl.uniprot.org/annotation/VAR_023477|||http://purl.uniprot.org/annotation/VAR_026592|||http://purl.uniprot.org/annotation/VAR_026593|||http://purl.uniprot.org/annotation/VAR_026594|||http://purl.uniprot.org/annotation/VAR_026595|||http://purl.uniprot.org/annotation/VAR_026596|||http://purl.uniprot.org/annotation/VAR_026597|||http://purl.uniprot.org/annotation/VAR_026598|||http://purl.uniprot.org/annotation/VAR_026599|||http://purl.uniprot.org/annotation/VAR_026600|||http://purl.uniprot.org/annotation/VAR_026601|||http://purl.uniprot.org/annotation/VAR_026602|||http://purl.uniprot.org/annotation/VAR_026603|||http://purl.uniprot.org/annotation/VAR_026604|||http://purl.uniprot.org/annotation/VAR_026605|||http://purl.uniprot.org/annotation/VAR_026606|||http://purl.uniprot.org/annotation/VAR_026607|||http://purl.uniprot.org/annotation/VAR_026608|||http://purl.uniprot.org/annotation/VAR_026609|||http://purl.uniprot.org/annotation/VAR_026610|||http://purl.uniprot.org/annotation/VAR_026611|||http://purl.uniprot.org/annotation/VAR_026612|||http://purl.uniprot.org/annotation/VAR_026613|||http://purl.uniprot.org/annotation/VAR_026614|||http://purl.uniprot.org/annotation/VAR_026615|||http://purl.uniprot.org/annotation/VAR_026616|||http://purl.uniprot.org/annotation/VAR_026617|||http://purl.uniprot.org/annotation/VAR_026618|||http://purl.uniprot.org/annotation/VAR_026619|||http://purl.uniprot.org/annotation/VAR_026620|||http://purl.uniprot.org/annotation/VAR_026621|||http://purl.uniprot.org/annotation/VAR_026622|||http://purl.uniprot.org/annotation/VAR_026623|||http://purl.uniprot.org/annotation/VAR_026624|||http://purl.uniprot.org/annotation/VAR_026625|||http://purl.uniprot.org/annotation/VAR_026626|||http://purl.uniprot.org/annotation/VAR_026627|||http://purl.uniprot.org/annotation/VAR_030495|||http://purl.uniprot.org/annotation/VAR_075379|||http://purl.uniprot.org/annotation/VAR_075380|||http://purl.uniprot.org/annotation/VAR_075381|||http://purl.uniprot.org/annotation/VAR_075382|||http://purl.uniprot.org/annotation/VAR_075383|||http://purl.uniprot.org/annotation/VAR_075384|||http://purl.uniprot.org/annotation/VAR_075385|||http://purl.uniprot.org/annotation/VAR_075386|||http://purl.uniprot.org/annotation/VAR_075387|||http://purl.uniprot.org/annotation/VAR_075388|||http://purl.uniprot.org/annotation/VAR_075389|||http://purl.uniprot.org/annotation/VAR_075390|||http://purl.uniprot.org/annotation/VAR_075391|||http://purl.uniprot.org/annotation/VAR_075392|||http://purl.uniprot.org/annotation/VAR_075393|||http://purl.uniprot.org/annotation/VAR_075394|||http://purl.uniprot.org/annotation/VAR_077210|||http://purl.uniprot.org/annotation/VAR_077211|||http://purl.uniprot.org/annotation/VAR_077212|||http://purl.uniprot.org/annotation/VAR_077213|||http://purl.uniprot.org/annotation/VAR_077214|||http://purl.uniprot.org/annotation/VAR_077215|||http://purl.uniprot.org/annotation/VAR_077216|||http://purl.uniprot.org/annotation/VAR_077217|||http://purl.uniprot.org/annotation/VAR_077218|||http://purl.uniprot.org/annotation/VAR_077219|||http://purl.uniprot.org/annotation/VAR_077220|||http://purl.uniprot.org/annotation/VAR_077221|||http://purl.uniprot.org/annotation/VAR_077222|||http://purl.uniprot.org/annotation/VAR_077223|||http://purl.uniprot.org/annotation/VAR_077224|||http://purl.uniprot.org/annotation/VAR_077225|||http://purl.uniprot.org/annotation/VAR_077226|||http://purl.uniprot.org/annotation/VAR_077227|||http://purl.uniprot.org/annotation/VAR_077228|||http://purl.uniprot.org/annotation/VAR_077229|||http://purl.uniprot.org/annotation/VAR_077230|||http://purl.uniprot.org/annotation/VAR_077231|||http://purl.uniprot.org/annotation/VAR_077232|||http://purl.uniprot.org/annotation/VAR_078342|||http://purl.uniprot.org/annotation/VAR_078343|||http://purl.uniprot.org/annotation/VAR_078344|||http://purl.uniprot.org/annotation/VAR_078345|||http://purl.uniprot.org/annotation/VAR_078346|||http://purl.uniprot.org/annotation/VAR_078347|||http://purl.uniprot.org/annotation/VAR_078348|||http://purl.uniprot.org/annotation/VAR_078349|||http://purl.uniprot.org/annotation/VAR_080031|||http://purl.uniprot.org/annotation/VAR_080032|||http://purl.uniprot.org/annotation/VAR_080033
http://togogenome.org/gene/9606:TMEM35A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FP2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Interaction with NGFR|||Lumenal|||Novel acetylcholine receptor chaperone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271607
http://togogenome.org/gene/9606:FN3KRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA64                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Ketosamine-3-kinase|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216339|||http://purl.uniprot.org/annotation/VAR_034057
http://togogenome.org/gene/9606:TAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17542|||http://purl.uniprot.org/uniprot/Q16509                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  BHLH|||Disordered|||In isoform PP22-TAL1.|||In isoform PP39-TAL1.|||Phosphoserine|||Polar residues|||T-cell acute lymphocytic leukemia protein 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127454|||http://purl.uniprot.org/annotation/VSP_002153|||http://purl.uniprot.org/annotation/VSP_002154
http://togogenome.org/gene/9606:PIK3R4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99570                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||In a breast cancer sample; somatic mutation.|||N-myristoyl glycine|||Phosphoinositide 3-kinase regulatory subunit 4|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086524|||http://purl.uniprot.org/annotation/VAR_035632|||http://purl.uniprot.org/annotation/VAR_040997|||http://purl.uniprot.org/annotation/VAR_040998|||http://purl.uniprot.org/annotation/VAR_040999|||http://purl.uniprot.org/annotation/VAR_041000|||http://purl.uniprot.org/annotation/VAR_041001|||http://purl.uniprot.org/annotation/VAR_041002|||http://purl.uniprot.org/annotation/VAR_041003
http://togogenome.org/gene/9606:ZNF626                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DY1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 626                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270994|||http://purl.uniprot.org/annotation/VAR_029837|||http://purl.uniprot.org/annotation/VAR_047338|||http://purl.uniprot.org/annotation/VAR_047339|||http://purl.uniprot.org/annotation/VAR_047340|||http://purl.uniprot.org/annotation/VAR_047341|||http://purl.uniprot.org/annotation/VAR_047342|||http://purl.uniprot.org/annotation/VSP_022263|||http://purl.uniprot.org/annotation/VSP_043270|||http://purl.uniprot.org/annotation/VSP_043271
http://togogenome.org/gene/9606:CCDC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CP8|||http://purl.uniprot.org/uniprot/Q16204                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  1|||2|||3|||4; approximate|||5|||5 X 29 AA tandem repeats|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form RET-CCDC6 oncogene|||Coiled-coil domain-containing protein 6|||Disordered|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089398|||http://purl.uniprot.org/annotation/VAR_062971
http://togogenome.org/gene/9606:TAF4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTH2|||http://purl.uniprot.org/uniprot/Q92750                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Histone-fold|||In isoform 2.|||Nuclear export signal|||Phosphoserine|||Required for interaction with P65/RELA|||Required for interaction with TAF12|||Sufficient for interaction with ZNF628|||TAFH|||Transcription initiation factor TFIID subunit 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118872|||http://purl.uniprot.org/annotation/VAR_052259|||http://purl.uniprot.org/annotation/VAR_061836|||http://purl.uniprot.org/annotation/VSP_022025|||http://purl.uniprot.org/annotation/VSP_022026
http://togogenome.org/gene/9606:GATA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||GATA-type 1|||GATA-type 2|||In CHTD5; decreased transcriptional activity.|||In CHTD5; loss of transcriptional activity.|||In CHTD5; unknown pathological significance.|||In CHTD5; unknown pathological significance; decreased transcriptional activity.|||Polar residues|||Transcription factor GATA-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083418|||http://purl.uniprot.org/annotation/VAR_067699|||http://purl.uniprot.org/annotation/VAR_067700|||http://purl.uniprot.org/annotation/VAR_067701|||http://purl.uniprot.org/annotation/VAR_073070|||http://purl.uniprot.org/annotation/VAR_073071|||http://purl.uniprot.org/annotation/VAR_073072|||http://purl.uniprot.org/annotation/VAR_073073|||http://purl.uniprot.org/annotation/VAR_073309|||http://purl.uniprot.org/annotation/VAR_073310|||http://purl.uniprot.org/annotation/VAR_073311|||http://purl.uniprot.org/annotation/VAR_073312|||http://purl.uniprot.org/annotation/VAR_073313|||http://purl.uniprot.org/annotation/VAR_073314|||http://purl.uniprot.org/annotation/VAR_073315|||http://purl.uniprot.org/annotation/VAR_073316|||http://purl.uniprot.org/annotation/VAR_073317|||http://purl.uniprot.org/annotation/VAR_073318|||http://purl.uniprot.org/annotation/VAR_080604|||http://purl.uniprot.org/annotation/VAR_080605|||http://purl.uniprot.org/annotation/VAR_080606|||http://purl.uniprot.org/annotation/VAR_080607|||http://purl.uniprot.org/annotation/VAR_080608|||http://purl.uniprot.org/annotation/VAR_080609
http://togogenome.org/gene/9606:TGFB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61812|||http://purl.uniprot.org/uniprot/Q59EG9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In LDS4.|||In isoform B.|||Interchain|||Latency-associated peptide|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a family with non-syndromic aortic disease.|||TGF-beta propeptide|||Transforming growth factor beta-2|||Transforming growth factor beta-2 proprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033784|||http://purl.uniprot.org/annotation/PRO_0000033785|||http://purl.uniprot.org/annotation/PRO_0000456180|||http://purl.uniprot.org/annotation/PRO_5004252718|||http://purl.uniprot.org/annotation/VAR_012708|||http://purl.uniprot.org/annotation/VAR_018923|||http://purl.uniprot.org/annotation/VAR_068931|||http://purl.uniprot.org/annotation/VAR_068932|||http://purl.uniprot.org/annotation/VAR_068933|||http://purl.uniprot.org/annotation/VAR_068934|||http://purl.uniprot.org/annotation/VAR_072740|||http://purl.uniprot.org/annotation/VAR_080342|||http://purl.uniprot.org/annotation/VAR_080343|||http://purl.uniprot.org/annotation/VSP_006417
http://togogenome.org/gene/9606:DDX59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5N6|||http://purl.uniprot.org/uniprot/Q5T1V6                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIT-type|||Helical|||Helicase ATP-binding|||Helicase C-terminal|||In OFD5.|||In OFD5; markedly reduced expression in fibroblasts compared to wild-type protein; impaired SHH signaling in SAG-treated fibroblasts.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Probable ATP-dependent RNA helicase DDX59|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282713|||http://purl.uniprot.org/annotation/VAR_031424|||http://purl.uniprot.org/annotation/VAR_033001|||http://purl.uniprot.org/annotation/VAR_035842|||http://purl.uniprot.org/annotation/VAR_070198|||http://purl.uniprot.org/annotation/VAR_070199|||http://purl.uniprot.org/annotation/VSP_024227
http://togogenome.org/gene/9606:LTBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DH07|||http://purl.uniprot.org/uniprot/B3KXY6|||http://purl.uniprot.org/uniprot/Q8N2S1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15|||EGF-like 16|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In URDS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 4|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||TB|||TB 1|||TB 2|||TB 3|||TB 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310964|||http://purl.uniprot.org/annotation/VAR_037119|||http://purl.uniprot.org/annotation/VAR_037120|||http://purl.uniprot.org/annotation/VAR_037121|||http://purl.uniprot.org/annotation/VAR_037122|||http://purl.uniprot.org/annotation/VAR_037123|||http://purl.uniprot.org/annotation/VAR_037124|||http://purl.uniprot.org/annotation/VAR_064153|||http://purl.uniprot.org/annotation/VSP_029362|||http://purl.uniprot.org/annotation/VSP_029363|||http://purl.uniprot.org/annotation/VSP_029364|||http://purl.uniprot.org/annotation/VSP_029365|||http://purl.uniprot.org/annotation/VSP_029366|||http://purl.uniprot.org/annotation/VSP_029367
http://togogenome.org/gene/9606:GFRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00451                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GDNF family receptor alpha-2|||GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010785|||http://purl.uniprot.org/annotation/PRO_0000010786|||http://purl.uniprot.org/annotation/VAR_059976|||http://purl.uniprot.org/annotation/VSP_001661|||http://purl.uniprot.org/annotation/VSP_046112
http://togogenome.org/gene/9606:NOS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35228                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||DINNN-motif; mediates interaction with SPSB1, SPSB2 and SPSB4|||FAD-binding FR-type|||Flavodoxin-like|||Found in patients with very early onset inflammatory bowel disease; increases NOS2 activity.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of interaction with SPSB1 and SPSB4.|||Nitric oxide synthase, inducible|||Phosphoserine; by PKA|||Phosphotyrosine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170930|||http://purl.uniprot.org/annotation/VAR_022127|||http://purl.uniprot.org/annotation/VAR_024548|||http://purl.uniprot.org/annotation/VAR_025020|||http://purl.uniprot.org/annotation/VAR_025021|||http://purl.uniprot.org/annotation/VAR_036302|||http://purl.uniprot.org/annotation/VSP_003582|||http://purl.uniprot.org/annotation/VSP_003583
http://togogenome.org/gene/9606:ISY1-RAB43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULR0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 1.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor ISY1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235813|||http://purl.uniprot.org/annotation/VSP_039410|||http://purl.uniprot.org/annotation/VSP_039411
http://togogenome.org/gene/9606:KRTAP9-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 5 AA repeats of C-C-[RQVSGE]-[SPSNQ]-[TASPI]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185192
http://togogenome.org/gene/9606:KCNK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00180                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes N-glycosylation.|||Abolishes change in ion selectivity in the presence of subphysiological K(+) levels.|||Abolishes channel activity and formation of disulfide-linked homodimers.|||Converts the electrically silent channel that is present at the cell membrane to an active channel.|||Converts the electrically silent channel that is present at the cell membrane to an active channel. No effect on retention in recycling endosomes.|||Cytoplasmic|||Decreases channel activity and abolishes inhibition by acidification of the extracellular medium.|||Does not increase the low intrinsic channel activity.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Helical; Name=Pore helix 1|||Helical; Name=Pore helix 2|||Impairs selectivity for K(+) ions and increases permeability to Na(+) ions, both at pH 7.4 and at pH 6.|||Important for increased permeability to Na(+) when K(+) levels are subphysiological|||Important for intracellular retention in recycling endosomes|||Increases channel activity, and has only a minor effect on the inhibition by acidification of the extracellular medium.|||Increases channel activity.|||Increases channel activity. Strongly increases channel activity; when associated with S-146.|||Increases channel activity. Strongly increases channel activity; when associated with S-261.|||Interchain|||N-linked (GlcNAc...) asparagine|||No effect on channel activity.|||No effect on intracellular retention in recycling endosomes.|||No effect on selectivity for K(+) ions.|||Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability|||Phosphoserine|||Potassium channel subfamily K member 1|||Selectivity filter 1|||Selectivity filter 2|||Slightly decreases the increased permeability to Na(+) ions at pH 6.|||Strongly decreases activity of homodimeric channels and of heterodimeric channels formed with KCNK3 and with KCNK9. No effect on location at the cell membrane.|||Strongly increases location at the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101740
http://togogenome.org/gene/9606:DEXI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95424                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Dexamethasone-induced protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096669
http://togogenome.org/gene/9606:ALB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02768                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Albumin|||Albumin 1|||Albumin 2|||Albumin 3|||Aspirin-acetylated lysine|||Impairs metal binding.|||In Bergamo.|||In Bleinheim/Iowa city-2.|||In Brest.|||In Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown.|||In Casebrook.|||In Caserta.|||In Castel di Sangro.|||In Christchurch/Honolulu-2.|||In Church bay.|||In Coari I/Porto Alegre.|||In Dublin.|||In FDAH.|||In Fukuoka-1/Paris-2.|||In Fukuoka-2/Lille/Taipei/Varese/Komagome-3.|||In Gent/Milano Fast.|||In Hawkes bay.|||In Herborn.|||In Hiroshima-1.|||In Hiroshima-2.|||In Iowa city-1.|||In Jaffna.|||In Kenitra.|||In Komagome-2.|||In Larino.|||In Liprizzi.|||In Maddaloni.|||In Maku.|||In Malmo-10.|||In Malmo-47.|||In Malmo-5.|||In Malmo-61.|||In Malmo-95/Dalakarlia.|||In Manaus-1/Adana/Lambadi/Vancouver.|||In Mexico.|||In Nagasaki-1.|||In Nagasaki-2.|||In Nagasaki-3.|||In Nagoya.|||In Naskapi/Mersin/Komagome-1.|||In Ortonovo.|||In Osaka-1.|||In Osaka-2/Phnom Phen/albumin B/Verona.|||In Parklands.|||In Redhill/Malmo-I/Tradate; associated with T-344 in Redhill.|||In Redhill; associated with C-23.|||In Roma.|||In Sondrio.|||In Takefu/Honolulu-1.|||In Tochigi.|||In Torino.|||In Tradate-2.|||In Tregasio.|||In Trieste.|||In Vanves.|||In Venezia.|||In Vibo Valentia.|||In Yanomama-2.|||In isoform 2.|||In isoform 3.|||N-linked (Glc) (glycation) lysine|||N-linked (Glc) (glycation) lysine; alternate|||N-linked (Glc) (glycation) lysine; in vitro|||N-linked (GlcNAc...) asparagine; in variant Casebrook|||N-linked (GlcNAc...) asparagine; in variant Redhill|||N6-methyllysine; alternate|||N6-succinyllysine|||Not glycated|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphothreonine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000069|||http://purl.uniprot.org/annotation/CAR_000226|||http://purl.uniprot.org/annotation/PRO_0000001067|||http://purl.uniprot.org/annotation/PRO_0000001068|||http://purl.uniprot.org/annotation/VAR_000499|||http://purl.uniprot.org/annotation/VAR_000500|||http://purl.uniprot.org/annotation/VAR_000501|||http://purl.uniprot.org/annotation/VAR_000502|||http://purl.uniprot.org/annotation/VAR_000503|||http://purl.uniprot.org/annotation/VAR_000504|||http://purl.uniprot.org/annotation/VAR_000505|||http://purl.uniprot.org/annotation/VAR_000506|||http://purl.uniprot.org/annotation/VAR_000507|||http://purl.uniprot.org/annotation/VAR_000508|||http://purl.uniprot.org/annotation/VAR_000509|||http://purl.uniprot.org/annotation/VAR_000510|||http://purl.uniprot.org/annotation/VAR_000511|||http://purl.uniprot.org/annotation/VAR_000512|||http://purl.uniprot.org/annotation/VAR_000513|||http://purl.uniprot.org/annotation/VAR_000514|||http://purl.uniprot.org/annotation/VAR_000515|||http://purl.uniprot.org/annotation/VAR_000516|||http://purl.uniprot.org/annotation/VAR_000517|||http://purl.uniprot.org/annotation/VAR_000518|||http://purl.uniprot.org/annotation/VAR_000519|||http://purl.uniprot.org/annotation/VAR_000520|||http://purl.uniprot.org/annotation/VAR_000521|||http://purl.uniprot.org/annotation/VAR_000522|||http://purl.uniprot.org/annotation/VAR_000523|||http://purl.uniprot.org/annotation/VAR_000524|||http://purl.uniprot.org/annotation/VAR_000525|||http://purl.uniprot.org/annotation/VAR_000526|||http://purl.uniprot.org/annotation/VAR_000527|||http://purl.uniprot.org/annotation/VAR_000528|||http://purl.uniprot.org/annotation/VAR_000529|||http://purl.uniprot.org/annotation/VAR_000530|||http://purl.uniprot.org/annotation/VAR_000531|||http://purl.uniprot.org/annotation/VAR_000532|||http://purl.uniprot.org/annotation/VAR_000533|||http://purl.uniprot.org/annotation/VAR_000534|||http://purl.uniprot.org/annotation/VAR_000535|||http://purl.uniprot.org/annotation/VAR_000536|||http://purl.uniprot.org/annotation/VAR_000537|||http://purl.uniprot.org/annotation/VAR_000538|||http://purl.uniprot.org/annotation/VAR_000539|||http://purl.uniprot.org/annotation/VAR_000540|||http://purl.uniprot.org/annotation/VAR_000541|||http://purl.uniprot.org/annotation/VAR_000542|||http://purl.uniprot.org/annotation/VAR_000543|||http://purl.uniprot.org/annotation/VAR_000544|||http://purl.uniprot.org/annotation/VAR_000545|||http://purl.uniprot.org/annotation/VAR_000546|||http://purl.uniprot.org/annotation/VAR_000547|||http://purl.uniprot.org/annotation/VAR_010657|||http://purl.uniprot.org/annotation/VAR_012981|||http://purl.uniprot.org/annotation/VAR_013011|||http://purl.uniprot.org/annotation/VAR_013012|||http://purl.uniprot.org/annotation/VAR_013013|||http://purl.uniprot.org/annotation/VAR_013014|||http://purl.uniprot.org/annotation/VAR_013015|||http://purl.uniprot.org/annotation/VAR_013016|||http://purl.uniprot.org/annotation/VAR_013017|||http://purl.uniprot.org/annotation/VAR_013018|||http://purl.uniprot.org/annotation/VAR_013019|||http://purl.uniprot.org/annotation/VAR_014290|||http://purl.uniprot.org/annotation/VAR_014291|||http://purl.uniprot.org/annotation/VAR_014292|||http://purl.uniprot.org/annotation/VAR_014293|||http://purl.uniprot.org/annotation/VAR_014294|||http://purl.uniprot.org/annotation/VAR_014295|||http://purl.uniprot.org/annotation/VSP_021275|||http://purl.uniprot.org/annotation/VSP_057389
http://togogenome.org/gene/9606:SDCBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H190                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-197. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-197.|||Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-244.|||Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-113.|||Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-167; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-167.|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||PDZ 1|||PDZ 2|||Syntenin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184004|||http://purl.uniprot.org/annotation/VAR_036544|||http://purl.uniprot.org/annotation/VAR_053700|||http://purl.uniprot.org/annotation/VAR_053701|||http://purl.uniprot.org/annotation/VAR_053702|||http://purl.uniprot.org/annotation/VSP_006352
http://togogenome.org/gene/9606:SERPINB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29508                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Increased antiprotease activity and increased MAPK8 inhibition activity.|||Loss of inhibitory activity to papain but does not decrease the suppression activity to MAPK8.|||Loss of inhibitory activity.|||N-acetylmethionine|||Reactive bond|||Serpin B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094103|||http://purl.uniprot.org/annotation/VAR_024351|||http://purl.uniprot.org/annotation/VAR_024352|||http://purl.uniprot.org/annotation/VSP_032657
http://togogenome.org/gene/9606:UTY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0Y2|||http://purl.uniprot.org/uniprot/A0A087X248|||http://purl.uniprot.org/uniprot/A0A087X2I9|||http://purl.uniprot.org/uniprot/A0A096LPD8|||http://purl.uniprot.org/uniprot/E1NZ93|||http://purl.uniprot.org/uniprot/E1U198|||http://purl.uniprot.org/uniprot/E1U1M3|||http://purl.uniprot.org/uniprot/E1U1M9|||http://purl.uniprot.org/uniprot/F4MH27|||http://purl.uniprot.org/uniprot/F4MH29|||http://purl.uniprot.org/uniprot/F4MH30|||http://purl.uniprot.org/uniprot/F4MH31|||http://purl.uniprot.org/uniprot/F4MH32|||http://purl.uniprot.org/uniprot/F4MH35|||http://purl.uniprot.org/uniprot/F4MH36|||http://purl.uniprot.org/uniprot/F4MH40|||http://purl.uniprot.org/uniprot/F4MH46|||http://purl.uniprot.org/uniprot/F4MH47|||http://purl.uniprot.org/uniprot/F4MH50|||http://purl.uniprot.org/uniprot/F4MH51|||http://purl.uniprot.org/uniprot/F4MH60|||http://purl.uniprot.org/uniprot/F4MH62|||http://purl.uniprot.org/uniprot/F4MH91|||http://purl.uniprot.org/uniprot/F4MH92|||http://purl.uniprot.org/uniprot/F5GWV3|||http://purl.uniprot.org/uniprot/F5H3N7|||http://purl.uniprot.org/uniprot/F5H8B4|||http://purl.uniprot.org/uniprot/O14607                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Unsure Residue                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Unsure Residue                                                                                  ^@                                                                                  Abolishes lysine demethylase activity.|||Basic and acidic residues|||D or N|||Disordered|||Histone demethylase UTY|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||JmjC|||No effect on lysine demethylase activity.|||Phosphothreonine|||Polar residues|||Pro residues|||Significantly higher lysine demethylase activity.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106411|||http://purl.uniprot.org/annotation/VSP_006556|||http://purl.uniprot.org/annotation/VSP_036783|||http://purl.uniprot.org/annotation/VSP_036784|||http://purl.uniprot.org/annotation/VSP_045611|||http://purl.uniprot.org/annotation/VSP_045612|||http://purl.uniprot.org/annotation/VSP_045613
http://togogenome.org/gene/9606:CEP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBI5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Centrosomal protein 15 kDa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089388
http://togogenome.org/gene/9606:HMGCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04035                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3-hydroxy-3-methylglutaryl-coenzyme A reductase|||Abolishes sterol-mediated ubiquitination and degradation; when associated with R-248.|||Abolishes sterol-mediated ubiquitination and degradation; when associated with R-89.|||Charge relay system|||Cytoplasmic|||Does not affect hydroxymethylglutaryl-CoA reductase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||INSIG-binding motif|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton donor|||Reduced sterol-mediated release from the ER. Not deglycosylated in response to sterols.|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114419|||http://purl.uniprot.org/annotation/VAR_011954|||http://purl.uniprot.org/annotation/VSP_002207|||http://purl.uniprot.org/annotation/VSP_046492
http://togogenome.org/gene/9606:DLG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J587|||http://purl.uniprot.org/uniprot/A0A994J7Q5|||http://purl.uniprot.org/uniprot/B7Z2T4|||http://purl.uniprot.org/uniprot/E9PIJ9|||http://purl.uniprot.org/uniprot/Q15700                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disks large homolog 2|||Guanylate kinase-like|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphotyrosine|||S-palmitoyl cysteine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094553|||http://purl.uniprot.org/annotation/VSP_015511|||http://purl.uniprot.org/annotation/VSP_015512|||http://purl.uniprot.org/annotation/VSP_015513|||http://purl.uniprot.org/annotation/VSP_015514|||http://purl.uniprot.org/annotation/VSP_015515|||http://purl.uniprot.org/annotation/VSP_015516|||http://purl.uniprot.org/annotation/VSP_045634
http://togogenome.org/gene/9606:OR5W2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH69                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5W2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150618|||http://purl.uniprot.org/annotation/VAR_034236|||http://purl.uniprot.org/annotation/VAR_034237|||http://purl.uniprot.org/annotation/VAR_053213|||http://purl.uniprot.org/annotation/VAR_053214|||http://purl.uniprot.org/annotation/VAR_053215|||http://purl.uniprot.org/annotation/VAR_053216|||http://purl.uniprot.org/annotation/VAR_062046
http://togogenome.org/gene/9606:DHRSX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5I4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Initiator Methionine|||Sequence Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member on chromosome X|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031974|||http://purl.uniprot.org/annotation/VAR_016100|||http://purl.uniprot.org/annotation/VAR_055354|||http://purl.uniprot.org/annotation/VAR_055355
http://togogenome.org/gene/9606:ABL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42684                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CAP|||Disordered|||F-actin-binding|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 10.|||In isoform 4, isoform 5, isoform 7 and isoform 10.|||In isoform 6, isoform 7 and isoform 8.|||In isoform 8.|||Kinase activation loop|||N-myristoyl glycine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1 and autocatalysis|||Phosphotyrosine; by autocatalysis|||Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||SH2|||SH3|||Somatic mutation in a breast cancer sample.|||Somatic mutation in a lung squamous cell carcinoma.|||Tyrosine-protein kinase ABL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088052|||http://purl.uniprot.org/annotation/VAR_029232|||http://purl.uniprot.org/annotation/VAR_029233|||http://purl.uniprot.org/annotation/VAR_029234|||http://purl.uniprot.org/annotation/VAR_029235|||http://purl.uniprot.org/annotation/VAR_029236|||http://purl.uniprot.org/annotation/VAR_055411|||http://purl.uniprot.org/annotation/VAR_055412|||http://purl.uniprot.org/annotation/VAR_055413|||http://purl.uniprot.org/annotation/VAR_055414|||http://purl.uniprot.org/annotation/VAR_082895|||http://purl.uniprot.org/annotation/VSP_004961|||http://purl.uniprot.org/annotation/VSP_017112|||http://purl.uniprot.org/annotation/VSP_021308|||http://purl.uniprot.org/annotation/VSP_041772|||http://purl.uniprot.org/annotation/VSP_041773|||http://purl.uniprot.org/annotation/VSP_041774
http://togogenome.org/gene/9606:PLEKHA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PKC0|||http://purl.uniprot.org/uniprot/Q6IQ23                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with CTNND1|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family A member 7|||Polar residues|||Pro residues|||WW|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287692|||http://purl.uniprot.org/annotation/VAR_032346|||http://purl.uniprot.org/annotation/VAR_032347|||http://purl.uniprot.org/annotation/VAR_032348|||http://purl.uniprot.org/annotation/VAR_032349|||http://purl.uniprot.org/annotation/VAR_061517|||http://purl.uniprot.org/annotation/VSP_025592|||http://purl.uniprot.org/annotation/VSP_039543
http://togogenome.org/gene/9606:VPS37C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8V6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312198|||http://purl.uniprot.org/annotation/VAR_037451|||http://purl.uniprot.org/annotation/VAR_037452
http://togogenome.org/gene/9606:TSPYL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Found in patients with mild intellectual disability; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs effect on cell proliferation; when associated with A-20.|||Impairs effect on cell proliferation; when associated with A-340.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Testis-specific Y-encoded-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289100|||http://purl.uniprot.org/annotation/VAR_075536
http://togogenome.org/gene/9606:TSPAN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L157                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311905|||http://purl.uniprot.org/annotation/VAR_037337
http://togogenome.org/gene/9606:CDH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H5X9|||http://purl.uniprot.org/uniprot/Q8IY78|||http://purl.uniprot.org/uniprot/Q9ULB5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-7|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003769|||http://purl.uniprot.org/annotation/PRO_0000003770|||http://purl.uniprot.org/annotation/PRO_5003324764|||http://purl.uniprot.org/annotation/PRO_5004308674|||http://purl.uniprot.org/annotation/VAR_060247|||http://purl.uniprot.org/annotation/VAR_061057
http://togogenome.org/gene/9606:MIEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTI2|||http://purl.uniprot.org/uniprot/Q9BRT3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes prenylation. Predominantly cysolic with little plasma membrane-associated expression. Reduces cell migration by affecting filopodia formation.|||Disordered|||Migration and invasion enhancer 1|||N-acetylserine|||No effect on subcellular location. Low protein abundance, suggesting that stability is affected.|||Redox-active|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265099|||http://purl.uniprot.org/annotation/PRO_0000396008
http://togogenome.org/gene/9606:CCSER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0I3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Serine-rich coiled-coil domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349292|||http://purl.uniprot.org/annotation/VAR_059336|||http://purl.uniprot.org/annotation/VSP_035318|||http://purl.uniprot.org/annotation/VSP_035319
http://togogenome.org/gene/9606:SS18L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHA2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Motif                                                                                  ^@                                                                                  SH2-binding|||SS18-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181826
http://togogenome.org/gene/9606:CPQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y646                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Carboxypeptidase Q|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000055941|||http://purl.uniprot.org/annotation/PRO_5000055942|||http://purl.uniprot.org/annotation/VAR_037466
http://togogenome.org/gene/9606:DDX51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8A6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX51|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||N-acetylalanine|||Phosphoserine|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228096|||http://purl.uniprot.org/annotation/VAR_055299|||http://purl.uniprot.org/annotation/VAR_055300|||http://purl.uniprot.org/annotation/VAR_055301|||http://purl.uniprot.org/annotation/VAR_055302|||http://purl.uniprot.org/annotation/VAR_055303|||http://purl.uniprot.org/annotation/VAR_055304|||http://purl.uniprot.org/annotation/VAR_055305|||http://purl.uniprot.org/annotation/VAR_061825
http://togogenome.org/gene/9606:TAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKB7|||http://purl.uniprot.org/uniprot/P17735                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminotransferase class I/classII|||In TYRSN2.|||N-acetylmethionine|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Reduced catalytic activity.|||Tyrosine aminotransferase|||Tyrosine aminotransferase ubiquitination region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123887|||http://purl.uniprot.org/annotation/VAR_000560|||http://purl.uniprot.org/annotation/VAR_048226
http://togogenome.org/gene/9606:SAMD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYL1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  SAM|||Sterile alpha motif domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097568
http://togogenome.org/gene/9606:PXYLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3R9|||http://purl.uniprot.org/uniprot/Q8TE99|||http://purl.uniprot.org/uniprot/Q9NT50                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Non-terminal Residue|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  2-phosphoxylose phosphatase 1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314924|||http://purl.uniprot.org/annotation/PRO_5014568441|||http://purl.uniprot.org/annotation/VSP_030432
http://togogenome.org/gene/9606:NGDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEJ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||Necessary for interaction with EIF4E|||Neuroguidin|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114331|||http://purl.uniprot.org/annotation/VAR_051898|||http://purl.uniprot.org/annotation/VAR_051899|||http://purl.uniprot.org/annotation/VSP_009935|||http://purl.uniprot.org/annotation/VSP_009936
http://togogenome.org/gene/9606:MRPL39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYK5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Large ribosomal subunit protein mL39|||N6-acetyllysine|||TGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087684|||http://purl.uniprot.org/annotation/VAR_052041|||http://purl.uniprot.org/annotation/VSP_005718
http://togogenome.org/gene/9606:LRRC45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CN5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Repeat                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Leucine-rich repeat-containing protein 45|||Phosphoserine; by NEK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223923
http://togogenome.org/gene/9606:CLCN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51798                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CBS 1|||CBS 2|||Cytoplasmic|||Disordered|||H(+)/Cl(-) exchange transporter 7|||Helical|||In HOD; increased voltage-gated chloride channel activity; increased lysosomal lumen acidification; increased cytoplasmic vacuole size.|||In OPTA2 and OPTB4.|||In OPTA2 and OPTB4; not detected in the fibroblasts from the patient.|||In OPTA2.|||In OPTA2; unknown pathological significance.|||In OPTB4.|||In OPTB4; unknown pathological significance.|||In isoform 2.|||Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport|||Mediates proton transfer from the protein to the inner aqueous phase|||Note=Loop between two helices|||Phosphoserine|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094452|||http://purl.uniprot.org/annotation/VAR_017838|||http://purl.uniprot.org/annotation/VAR_017839|||http://purl.uniprot.org/annotation/VAR_017840|||http://purl.uniprot.org/annotation/VAR_020997|||http://purl.uniprot.org/annotation/VAR_020998|||http://purl.uniprot.org/annotation/VAR_020999|||http://purl.uniprot.org/annotation/VAR_021000|||http://purl.uniprot.org/annotation/VAR_021001|||http://purl.uniprot.org/annotation/VAR_021002|||http://purl.uniprot.org/annotation/VAR_021003|||http://purl.uniprot.org/annotation/VAR_021004|||http://purl.uniprot.org/annotation/VAR_021005|||http://purl.uniprot.org/annotation/VAR_021006|||http://purl.uniprot.org/annotation/VAR_021007|||http://purl.uniprot.org/annotation/VAR_021008|||http://purl.uniprot.org/annotation/VAR_037427|||http://purl.uniprot.org/annotation/VAR_064637|||http://purl.uniprot.org/annotation/VAR_064638|||http://purl.uniprot.org/annotation/VAR_064639|||http://purl.uniprot.org/annotation/VAR_064640|||http://purl.uniprot.org/annotation/VAR_064641|||http://purl.uniprot.org/annotation/VAR_064642|||http://purl.uniprot.org/annotation/VAR_064643|||http://purl.uniprot.org/annotation/VAR_064644|||http://purl.uniprot.org/annotation/VAR_064645|||http://purl.uniprot.org/annotation/VAR_064646|||http://purl.uniprot.org/annotation/VAR_064647|||http://purl.uniprot.org/annotation/VAR_064648|||http://purl.uniprot.org/annotation/VAR_075576|||http://purl.uniprot.org/annotation/VAR_075577|||http://purl.uniprot.org/annotation/VAR_075578|||http://purl.uniprot.org/annotation/VAR_075579|||http://purl.uniprot.org/annotation/VAR_075580|||http://purl.uniprot.org/annotation/VAR_075581|||http://purl.uniprot.org/annotation/VAR_075582|||http://purl.uniprot.org/annotation/VAR_075583|||http://purl.uniprot.org/annotation/VAR_075584|||http://purl.uniprot.org/annotation/VAR_083175|||http://purl.uniprot.org/annotation/VSP_045698
http://togogenome.org/gene/9606:TOR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14657                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Decreases interaction with TOR1AIP2.|||Highly reduces ATPase activity induced by TOR1AIP2.|||Loss of ATPase activity. Produces sinusoidal endoplasmic reticulum structures where it accumulates. Highly enhances interaction with TOR1AIP2. Localizes in the nuclear envelope.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with TOR1AIP2.|||Torsin-1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005509|||http://purl.uniprot.org/annotation/VAR_059220
http://togogenome.org/gene/9606:ADRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAG8|||http://purl.uniprot.org/uniprot/P13945                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-3 adrenergic receptor|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069143|||http://purl.uniprot.org/annotation/VAR_003456|||http://purl.uniprot.org/annotation/VAR_014166|||http://purl.uniprot.org/annotation/VAR_025102|||http://purl.uniprot.org/annotation/VAR_029205
http://togogenome.org/gene/9606:KLF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75840                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD; inactive|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Found in a patient with developmental delay/intellectual disability, neuromuscular and psychiatric symptoms; unknown pathological significance.|||Found in two patients with developmental delay/intellectual disability, neuromuscular and psychiatric symptoms; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Krueppel-like factor 7|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047174|||http://purl.uniprot.org/annotation/VAR_081574|||http://purl.uniprot.org/annotation/VAR_081575|||http://purl.uniprot.org/annotation/VAR_081576|||http://purl.uniprot.org/annotation/VSP_047030|||http://purl.uniprot.org/annotation/VSP_047031|||http://purl.uniprot.org/annotation/VSP_047032|||http://purl.uniprot.org/annotation/VSP_047477|||http://purl.uniprot.org/annotation/VSP_047478|||http://purl.uniprot.org/annotation/VSP_047479
http://togogenome.org/gene/9606:KRTAP5-10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8G5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184108
http://togogenome.org/gene/9606:IL1R1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZW4|||http://purl.uniprot.org/uniprot/P14778                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Interleukin-1 receptor type 1, membrane form|||Interleukin-1 receptor type 1, soluble form|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Reduces NF-kappa-B activation and receptor-associated kinase activation.|||Reduces NF-kappa-B activation.|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015435|||http://purl.uniprot.org/annotation/PRO_0000415344|||http://purl.uniprot.org/annotation/PRO_5002879410|||http://purl.uniprot.org/annotation/VAR_019131|||http://purl.uniprot.org/annotation/VAR_029189
http://togogenome.org/gene/9606:FEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39748|||http://purl.uniprot.org/uniprot/Q6FHX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Diminishes nucleolar localization.|||Disordered|||Fails to translocate from nucleoli to the nuclear plasma.|||Flap endonuclease 1|||I-domain|||Impairs ability to localize to sites of DNA replication or repair.|||In isoform FENMIT.|||Interaction with PCNA|||Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding.|||Loss of flap endonuclease activity and substrate binding.|||Loss of flap endonuclease activity but substrate binding activity is retained.|||N-domain|||N6-acetyllysine|||No effect on flap endonuclease activity or substrate binding.|||No significant effect on exonuclease activity or flap endonuclease activity.|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Polar residues|||Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted.|||Symmetric dimethylarginine; by PRMT5|||XPG N-terminal|||XPG-I                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154069|||http://purl.uniprot.org/annotation/VSP_047520
http://togogenome.org/gene/9606:SEC61A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ68|||http://purl.uniprot.org/uniprot/Q8TC24|||http://purl.uniprot.org/uniprot/Q9H9S3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||Lumenal|||Protein transport protein Sec61 subunit alpha isoform 2|||Translocon Sec61/SecY plug                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131795|||http://purl.uniprot.org/annotation/VSP_010472|||http://purl.uniprot.org/annotation/VSP_046380
http://togogenome.org/gene/9606:PATE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3GLJ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Prostate and testis expressed protein 3|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000354972|||http://purl.uniprot.org/annotation/VAR_059884
http://togogenome.org/gene/9606:KRTAP10-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60368                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||22 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185210|||http://purl.uniprot.org/annotation/VAR_017690|||http://purl.uniprot.org/annotation/VAR_017691|||http://purl.uniprot.org/annotation/VAR_017692|||http://purl.uniprot.org/annotation/VAR_017693|||http://purl.uniprot.org/annotation/VAR_053462
http://togogenome.org/gene/9606:DMXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDJ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||DmX-like protein 2|||In DEE81.|||In DFNA71.|||In PEPNS.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223324|||http://purl.uniprot.org/annotation/VAR_057593|||http://purl.uniprot.org/annotation/VAR_057594|||http://purl.uniprot.org/annotation/VAR_057595|||http://purl.uniprot.org/annotation/VAR_057596|||http://purl.uniprot.org/annotation/VAR_062094|||http://purl.uniprot.org/annotation/VAR_069028|||http://purl.uniprot.org/annotation/VAR_072642|||http://purl.uniprot.org/annotation/VAR_079484|||http://purl.uniprot.org/annotation/VAR_083446|||http://purl.uniprot.org/annotation/VAR_083447|||http://purl.uniprot.org/annotation/VSP_043015|||http://purl.uniprot.org/annotation/VSP_044977
http://togogenome.org/gene/9606:ATP8B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43520                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Acidic residues|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A.|||Helical|||Impaired PC flippase activity.|||In BRIC1 and PFIC1; common mutation; reduces interaction with TMEM30A.|||In BRIC1.|||In BRIC1; compound heterozygote with N-70.|||In BRIC1; compound heterozygote with Q-600; uncertain pathological significance; may be associated with ICP; reduces interaction with TMEM30A; has no effect on PC flippase activity.|||In BRIC1; loss of PC flippase activity.|||In ICP1.|||In ICP1; reduces interaction with TMEM30A.|||In ICP1; unknown pathological significance.|||In PFIC1 and BRIC1.|||In PFIC1.|||In PFIC1; greatly reduced expression due to proteosomal degradation; abolishes interaction with TMEM30A.|||In PFIC1; greatly reduces interaction with TMEM30A.|||In PFIC1; loss of PC flippase activity.|||In a breast cancer sample; somatic mutation.|||Phospholipid-transporting ATPase IC|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046364|||http://purl.uniprot.org/annotation/VAR_008809|||http://purl.uniprot.org/annotation/VAR_008810|||http://purl.uniprot.org/annotation/VAR_008811|||http://purl.uniprot.org/annotation/VAR_008812|||http://purl.uniprot.org/annotation/VAR_008813|||http://purl.uniprot.org/annotation/VAR_008814|||http://purl.uniprot.org/annotation/VAR_015423|||http://purl.uniprot.org/annotation/VAR_029271|||http://purl.uniprot.org/annotation/VAR_029272|||http://purl.uniprot.org/annotation/VAR_029273|||http://purl.uniprot.org/annotation/VAR_036499|||http://purl.uniprot.org/annotation/VAR_036500|||http://purl.uniprot.org/annotation/VAR_043044|||http://purl.uniprot.org/annotation/VAR_043045|||http://purl.uniprot.org/annotation/VAR_043046|||http://purl.uniprot.org/annotation/VAR_043047|||http://purl.uniprot.org/annotation/VAR_043048|||http://purl.uniprot.org/annotation/VAR_043049|||http://purl.uniprot.org/annotation/VAR_043050|||http://purl.uniprot.org/annotation/VAR_043051|||http://purl.uniprot.org/annotation/VAR_043052|||http://purl.uniprot.org/annotation/VAR_043053|||http://purl.uniprot.org/annotation/VAR_043054|||http://purl.uniprot.org/annotation/VAR_043055|||http://purl.uniprot.org/annotation/VAR_043056|||http://purl.uniprot.org/annotation/VAR_043057|||http://purl.uniprot.org/annotation/VAR_043058|||http://purl.uniprot.org/annotation/VAR_043059|||http://purl.uniprot.org/annotation/VAR_043060|||http://purl.uniprot.org/annotation/VAR_043061|||http://purl.uniprot.org/annotation/VAR_043062|||http://purl.uniprot.org/annotation/VAR_043063|||http://purl.uniprot.org/annotation/VAR_043064|||http://purl.uniprot.org/annotation/VAR_043065|||http://purl.uniprot.org/annotation/VAR_043066|||http://purl.uniprot.org/annotation/VAR_043067|||http://purl.uniprot.org/annotation/VAR_043068|||http://purl.uniprot.org/annotation/VAR_043069|||http://purl.uniprot.org/annotation/VAR_043070|||http://purl.uniprot.org/annotation/VAR_043071|||http://purl.uniprot.org/annotation/VAR_043072|||http://purl.uniprot.org/annotation/VAR_043073|||http://purl.uniprot.org/annotation/VAR_055045|||http://purl.uniprot.org/annotation/VAR_071045|||http://purl.uniprot.org/annotation/VAR_071046
http://togogenome.org/gene/9606:SMIM20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5G0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Phenylalanine amide|||Phoenixin-14|||Phoenixin-20|||Small integral membrane protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326049|||http://purl.uniprot.org/annotation/PRO_0000449025|||http://purl.uniprot.org/annotation/PRO_0000449026|||http://purl.uniprot.org/annotation/VAR_039968|||http://purl.uniprot.org/annotation/VAR_082869|||http://purl.uniprot.org/annotation/VAR_082870|||http://purl.uniprot.org/annotation/VAR_082871|||http://purl.uniprot.org/annotation/VSP_038831
http://togogenome.org/gene/9606:PPBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02775                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Beta-thromboglobulin|||Connective tissue-activating peptide III|||Connective tissue-activating peptide III(1-81)|||Neutrophil-activating peptide 2|||Neutrophil-activating peptide 2(1-63)|||Neutrophil-activating peptide 2(1-66)|||Neutrophil-activating peptide 2(73)|||Neutrophil-activating peptide 2(74)|||Platelet basic protein|||TC-1|||TC-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005088|||http://purl.uniprot.org/annotation/PRO_0000005089|||http://purl.uniprot.org/annotation/PRO_0000005090|||http://purl.uniprot.org/annotation/PRO_0000005091|||http://purl.uniprot.org/annotation/PRO_0000005092|||http://purl.uniprot.org/annotation/PRO_0000005093|||http://purl.uniprot.org/annotation/PRO_0000005094|||http://purl.uniprot.org/annotation/PRO_0000005095|||http://purl.uniprot.org/annotation/PRO_0000005096|||http://purl.uniprot.org/annotation/PRO_0000041949|||http://purl.uniprot.org/annotation/PRO_0000041950
http://togogenome.org/gene/9606:CTIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43310                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CBP80/20-dependent translation initiation factor|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with NCBP1/CBP80|||MIF4G|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050754|||http://purl.uniprot.org/annotation/VAR_020041|||http://purl.uniprot.org/annotation/VAR_035749|||http://purl.uniprot.org/annotation/VAR_035750|||http://purl.uniprot.org/annotation/VSP_013774
http://togogenome.org/gene/9606:FADD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13158                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) N-beta-linked (GlcNAc) arginine|||Abolished GlcNAcylation by E.coli NleB1.|||DED|||Death|||Decreased interaction with FAS.|||Disordered|||FAS-associated death domain protein|||In IEHDCM; reduced folding stability as measured by differential scanning calorimetry of the mutant protein; impairs interaction with FAS.|||Loss of interaction with CASP8.|||Loss of interaction with CASP8. Abolishes induction of apoptosis. Decreased interaction with FAS.|||Loss of interaction with FAS.|||Loss of interaction with FAS. Loss of self-association. Abolishes induction of apoptosis.|||Loss of self-association.|||Phosphoserine|||Strongly decreased interaction with FAS.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191279|||http://purl.uniprot.org/annotation/VAR_065124
http://togogenome.org/gene/9606:PPP1R12C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZL4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||N-acetylserine|||Phosphoserine|||Phosphothreonine; by CDC42BP and ROCK2|||Polar residues|||Pro residues|||Protein phosphatase 1 regulatory subunit 12C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315863|||http://purl.uniprot.org/annotation/VAR_048310|||http://purl.uniprot.org/annotation/VSP_030750|||http://purl.uniprot.org/annotation/VSP_030751|||http://purl.uniprot.org/annotation/VSP_052643|||http://purl.uniprot.org/annotation/VSP_057216|||http://purl.uniprot.org/annotation/VSP_057217
http://togogenome.org/gene/9606:MSI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43347                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Phosphoserine|||RNA-binding protein Musashi homolog 1|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081649|||http://purl.uniprot.org/annotation/VAR_035485
http://togogenome.org/gene/9606:UBE2S                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16763                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl thioester intermediate|||Impairs polyubiquitination in the presence of APC/C complex, decreasing affinity for substrate.|||Loss of function.|||N-acetylmethionine|||Phosphoserine|||Reduced ubiquitination activity.|||UBC core|||Ubiquitin-conjugating enzyme E2 S                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082507
http://togogenome.org/gene/9606:FADS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR51|||http://purl.uniprot.org/uniprot/O60427                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-CoA (8-3)-desaturase|||Cytochrome b5 heme-binding|||Cytoplasmic|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||Lumenal|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307096|||http://purl.uniprot.org/annotation/VAR_035340|||http://purl.uniprot.org/annotation/VSP_047521
http://togogenome.org/gene/9606:TTC21A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDW8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SPGF37.|||In isoform 3.|||In isoform 5 and isoform 6.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 6.|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 14|||TPR 15|||TPR 16|||TPR 17|||TPR 18|||TPR 19|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 21A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291915|||http://purl.uniprot.org/annotation/VAR_032879|||http://purl.uniprot.org/annotation/VAR_032880|||http://purl.uniprot.org/annotation/VAR_032881|||http://purl.uniprot.org/annotation/VAR_032882|||http://purl.uniprot.org/annotation/VAR_032883|||http://purl.uniprot.org/annotation/VAR_032884|||http://purl.uniprot.org/annotation/VAR_032885|||http://purl.uniprot.org/annotation/VAR_032886|||http://purl.uniprot.org/annotation/VAR_032887|||http://purl.uniprot.org/annotation/VAR_059861|||http://purl.uniprot.org/annotation/VAR_082207|||http://purl.uniprot.org/annotation/VAR_082208|||http://purl.uniprot.org/annotation/VSP_026297|||http://purl.uniprot.org/annotation/VSP_038428|||http://purl.uniprot.org/annotation/VSP_038429|||http://purl.uniprot.org/annotation/VSP_038430|||http://purl.uniprot.org/annotation/VSP_038431
http://togogenome.org/gene/9606:NMNAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFG2|||http://purl.uniprot.org/uniprot/Q49AL4|||http://purl.uniprot.org/uniprot/Q96T66                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytidyltransferase-like|||DTW|||In isoform 2.|||In isoform 3.|||Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135016|||http://purl.uniprot.org/annotation/VSP_010267|||http://purl.uniprot.org/annotation/VSP_043203
http://togogenome.org/gene/9606:TP53BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13625                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Apoptosis-stimulating of p53 protein 2|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with APPBP1|||Loss of interaction with APC2.|||Mediates interaction with APC2|||Phosphoserine|||Polar residues|||Pro residues|||SH3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066964|||http://purl.uniprot.org/annotation/VSP_008010|||http://purl.uniprot.org/annotation/VSP_043509
http://togogenome.org/gene/9606:PAX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55771|||http://purl.uniprot.org/uniprot/Q2L4T1                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with KDM5B.|||In STHAG3.|||Interaction with KDM5B|||PAI subdomain|||Paired|||Paired box protein Pax-9|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050203|||http://purl.uniprot.org/annotation/VAR_015698|||http://purl.uniprot.org/annotation/VAR_034371
http://togogenome.org/gene/9606:CD320                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD320 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MMATC; unknown pathological significance; decreased function in cobalamin transport; does not affect stability; does not affect interaction with TCN2.|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045798|||http://purl.uniprot.org/annotation/VAR_047315|||http://purl.uniprot.org/annotation/VAR_047316|||http://purl.uniprot.org/annotation/VAR_064080|||http://purl.uniprot.org/annotation/VAR_077921|||http://purl.uniprot.org/annotation/VSP_045368
http://togogenome.org/gene/9606:TFR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UP52                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Endocytosis signal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Hereditary hemochromatosis modifier.|||In HFE3.|||In isoform Beta.|||In isoform Gamma.|||Interchain|||N-linked (GlcNAc...) asparagine|||Transferrin receptor protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174136|||http://purl.uniprot.org/annotation/VAR_012738|||http://purl.uniprot.org/annotation/VAR_034122|||http://purl.uniprot.org/annotation/VAR_034123|||http://purl.uniprot.org/annotation/VAR_034124|||http://purl.uniprot.org/annotation/VAR_042515|||http://purl.uniprot.org/annotation/VAR_042516|||http://purl.uniprot.org/annotation/VAR_042517|||http://purl.uniprot.org/annotation/VSP_005354|||http://purl.uniprot.org/annotation/VSP_005355
http://togogenome.org/gene/9606:RBM17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W009|||http://purl.uniprot.org/uniprot/Q96I25                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing.|||Basic and acidic residues|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs interaction with SF1 and U2AF2 and abolishes interaction with SF3B1. Abolishes regulation of alternative splicing.|||Impairs interaction with SF1; has minor effect on interaction with SF3B1 and U2AF2.|||Impairs interaction with SF3B1, SF1 and U2AF2. Abolishes regulation of alternative splicing.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||RRM|||Removed|||Splicing factor 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081903
http://togogenome.org/gene/9606:NRCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z670|||http://purl.uniprot.org/uniprot/C9JYY6|||http://purl.uniprot.org/uniprot/Q14CA1|||http://purl.uniprot.org/uniprot/Q92823                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Helical|||Ig-like|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||In NEDNMS.|||In NEDNMS; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Neuronal cell adhesion molecule|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015057|||http://purl.uniprot.org/annotation/PRO_5002866218|||http://purl.uniprot.org/annotation/PRO_5002997336|||http://purl.uniprot.org/annotation/PRO_5004183070|||http://purl.uniprot.org/annotation/VAR_035528|||http://purl.uniprot.org/annotation/VAR_035529|||http://purl.uniprot.org/annotation/VAR_047550|||http://purl.uniprot.org/annotation/VAR_087388|||http://purl.uniprot.org/annotation/VAR_087389|||http://purl.uniprot.org/annotation/VAR_087390|||http://purl.uniprot.org/annotation/VAR_087391|||http://purl.uniprot.org/annotation/VAR_087392|||http://purl.uniprot.org/annotation/VAR_087393|||http://purl.uniprot.org/annotation/VAR_087394|||http://purl.uniprot.org/annotation/VAR_087395|||http://purl.uniprot.org/annotation/VAR_087396|||http://purl.uniprot.org/annotation/VSP_007837|||http://purl.uniprot.org/annotation/VSP_007838|||http://purl.uniprot.org/annotation/VSP_007839|||http://purl.uniprot.org/annotation/VSP_007840|||http://purl.uniprot.org/annotation/VSP_007841|||http://purl.uniprot.org/annotation/VSP_007842|||http://purl.uniprot.org/annotation/VSP_007843|||http://purl.uniprot.org/annotation/VSP_045040
http://togogenome.org/gene/9606:UBE2G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60604                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl thioester intermediate|||In isoform 2.|||N-acetylalanine|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082483|||http://purl.uniprot.org/annotation/VSP_046260
http://togogenome.org/gene/9606:STEEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5V9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abrogates interaction with STING1 and impairs STING1-mediated signaling.|||In isoform 2.|||In isoform 3.|||STING ER exit protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287609|||http://purl.uniprot.org/annotation/VSP_044273|||http://purl.uniprot.org/annotation/VSP_044274
http://togogenome.org/gene/9606:MAN1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YG20|||http://purl.uniprot.org/uniprot/Q9UKM7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  About 4-fold reduction in K(cat).|||About 44-fold reduction in K(cat), slight reduction in K(m), about 100-fold increase in binding affinity for Man(9)GlcnAc(2) but no change in binding affinity for the inhibitor, dMNJ. Even further greater reduction in K(cat) and increase in K(m); when associated with Q-599.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase|||Helical|||Helical; Signal-anchor for type II membrane protein|||In RAFQS; disrupts stable protein expression.|||In RAFQS; results in about 1300-fold decrease in activity.|||Lumenal|||Polar residues|||Proton donor|||Some reduction in K(cat) but no change in K(m), abolishes almost all binding to Man(9)GlcnAc(2) but reduced binding to the inhibitor dMNJ by about 73-fold. Further reduction in K(m) but slight increase in K(m); when associated with Q-599.|||Very significant reduction in K(cat), 4-fold weaker binding affinity for Man(9)GlcnAc(2) but about 1000-fold reduction in binding affinity for the inhibitor, dMNJ. Significant reductions in K(cat) and slight increase in K(m); when associated with E-330 or N-463.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210314|||http://purl.uniprot.org/annotation/VAR_055841|||http://purl.uniprot.org/annotation/VAR_066592|||http://purl.uniprot.org/annotation/VAR_066593
http://togogenome.org/gene/9606:ZBTB43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43298                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphothreonine|||Polar residues|||Zinc finger and BTB domain-containing protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047519
http://togogenome.org/gene/9606:BNC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR27|||http://purl.uniprot.org/uniprot/Q5H9S4|||http://purl.uniprot.org/uniprot/Q6ZN30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In LUTO.|||In LUTO; unknown pathological significance.|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger protein basonuclin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046934|||http://purl.uniprot.org/annotation/VAR_033543|||http://purl.uniprot.org/annotation/VAR_052707|||http://purl.uniprot.org/annotation/VAR_083492|||http://purl.uniprot.org/annotation/VAR_083493|||http://purl.uniprot.org/annotation/VAR_083494|||http://purl.uniprot.org/annotation/VAR_083495|||http://purl.uniprot.org/annotation/VSP_051873|||http://purl.uniprot.org/annotation/VSP_051874
http://togogenome.org/gene/9606:COQ4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3A0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In COQ10D7.|||In isoform 2.|||Mitochondrion|||Phosphoserine|||Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115240|||http://purl.uniprot.org/annotation/VAR_048829|||http://purl.uniprot.org/annotation/VAR_054861|||http://purl.uniprot.org/annotation/VAR_073356|||http://purl.uniprot.org/annotation/VAR_073357|||http://purl.uniprot.org/annotation/VAR_073358|||http://purl.uniprot.org/annotation/VAR_073359|||http://purl.uniprot.org/annotation/VAR_073360|||http://purl.uniprot.org/annotation/VSP_036866
http://togogenome.org/gene/9606:R3HDM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15032                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Pro residues|||R3H|||R3H domain-containing protein 1|||SUZ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097139|||http://purl.uniprot.org/annotation/VAR_025423|||http://purl.uniprot.org/annotation/VAR_025424|||http://purl.uniprot.org/annotation/VSP_017344|||http://purl.uniprot.org/annotation/VSP_017345|||http://purl.uniprot.org/annotation/VSP_054308|||http://purl.uniprot.org/annotation/VSP_054309|||http://purl.uniprot.org/annotation/VSP_054310
http://togogenome.org/gene/9606:ANKRD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UB98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Ankyrin repeat domain-containing protein 12|||Basic and acidic residues|||Basic residues|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066908|||http://purl.uniprot.org/annotation/VAR_019425|||http://purl.uniprot.org/annotation/VAR_022088|||http://purl.uniprot.org/annotation/VAR_024173|||http://purl.uniprot.org/annotation/VAR_026042|||http://purl.uniprot.org/annotation/VAR_048271|||http://purl.uniprot.org/annotation/VAR_048272|||http://purl.uniprot.org/annotation/VAR_048273|||http://purl.uniprot.org/annotation/VAR_048274|||http://purl.uniprot.org/annotation/VAR_048275|||http://purl.uniprot.org/annotation/VAR_081528|||http://purl.uniprot.org/annotation/VSP_010901
http://togogenome.org/gene/9606:ZNF474                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S9Z5                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC/C3H-type 1|||C2HC/C3H-type 2|||C2HC/C3H-type 3|||C2HC/C3H-type 4|||Disordered|||Zinc finger protein 474                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280414|||http://purl.uniprot.org/annotation/VAR_031146
http://togogenome.org/gene/9606:INSR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06213                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with IRS1 and SHC1.|||Abolishes interaction with IRS1 and significantly reduces interaction with SHC1. Has no effect on interaction with PIK3R1.|||Abolishes interaction with IRS1. Severely disrupts, but does not abolish interaction with SHC1.|||Abolishes the kinase activity and abolishes interaction with IRS1, SHC1, GRB7 and PIK3R1.|||Abolishes the kinase activity.|||Cytoplasmic|||Disordered|||Does not affect interaction with IRS1, SHC1 or PIK3R1.|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Has no effect on insulin-stimulated autophosphorylation, but inhibits the biological activity of the receptor. Abolishes interaction with IRS1 and almost completely prevents interaction with SHC1. Has no effect on interaction with PIK3R1. Abolishes interaction with STAT5B.|||Helical|||Important for interaction with IRS1, SHC1 and STAT5B|||In HHF5 and IRAN type A; interferes with kinase activation by insulin.|||In IRAN type A.|||In IRAN type A; accelerates degradation of the protein and impairs kinase activity.|||In IRAN type A; impairs proteolytic processing.|||In IRAN type A; inhibits receptor internalization.|||In IRAN type A; interferes with receptor processing.|||In IRAN type A; moderate.|||In IRAN type A; unknown pathological significance.|||In Ins resistance; severe.|||In LEPRCH and RMS; reduces insulin binding possibly due to reduced receptor levels on the cell surface.|||In LEPRCH.|||In LEPRCH; ARK-1.|||In LEPRCH; Atlanta-1; abolishes insulin binding.|||In LEPRCH; Geldeimalsen.|||In LEPRCH; Helmond; inhibits processing and transport.|||In LEPRCH; Verona-1.|||In LEPRCH; abolishes insulin binding.|||In LEPRCH; abolishes post-translational processing.|||In LEPRCH; abolishes post-translational processing; abolishes insulin binding.|||In LEPRCH; impaired receptor processing; impairs post-translational processing.|||In LEPRCH; impairs post-translational processing.|||In LEPRCH; impairs transport of the receptor to the cell surface.|||In LEPRCH; inhibits receptor processing.|||In LEPRCH; markedly impairs insulin binding.|||In LEPRCH; markedly impairs insulin binding;impairs post-translational processing.|||In LEPRCH; mild.|||In LEPRCH; partially inhibits receptor processing and autophosphorylation; strongly impairs ERK phosphorylation; induces wild-type levels of IRS-1 phosphorylation.|||In RMS and LEPRCH.|||In RMS and LEPRCH; Winnipeg; may impair receptor processing.|||In RMS.|||In RMS; abolishes insulin binding.|||In RMS; decreases post-translational processing.|||In RMS; impairs post-translational processing.|||In RMS; impairs transport to the plasma membrane and reduces the affinity to bind insulin.|||In RMS; may impair receptor processing.|||In RMS; reduces insulin binding.|||In T2D.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a patient with insulin resistance.|||In a subject with non-insulin dependent diabetes mellitus.|||In isoform Short.|||Increases kinase activity.|||Insulin receptor subunit alpha|||Insulin receptor subunit beta|||Insulin-binding|||Interchain|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||PIK3R1-binding|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton donor/acceptor|||Reduced interaction with GRB7.|||Reduces interaction with IRS1 but has no effect on interaction with SHC1.|||Severely reduces interaction with SHC1. Has no effect on interaction with IRS1.|||Strongly reduced interaction with GRB7.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016687|||http://purl.uniprot.org/annotation/PRO_0000016689|||http://purl.uniprot.org/annotation/VAR_004079|||http://purl.uniprot.org/annotation/VAR_004080|||http://purl.uniprot.org/annotation/VAR_004081|||http://purl.uniprot.org/annotation/VAR_004082|||http://purl.uniprot.org/annotation/VAR_004083|||http://purl.uniprot.org/annotation/VAR_004084|||http://purl.uniprot.org/annotation/VAR_004085|||http://purl.uniprot.org/annotation/VAR_004086|||http://purl.uniprot.org/annotation/VAR_004087|||http://purl.uniprot.org/annotation/VAR_004088|||http://purl.uniprot.org/annotation/VAR_004089|||http://purl.uniprot.org/annotation/VAR_004090|||http://purl.uniprot.org/annotation/VAR_004091|||http://purl.uniprot.org/annotation/VAR_004092|||http://purl.uniprot.org/annotation/VAR_004093|||http://purl.uniprot.org/annotation/VAR_004094|||http://purl.uniprot.org/annotation/VAR_004095|||http://purl.uniprot.org/annotation/VAR_004096|||http://purl.uniprot.org/annotation/VAR_004097|||http://purl.uniprot.org/annotation/VAR_004098|||http://purl.uniprot.org/annotation/VAR_004099|||http://purl.uniprot.org/annotation/VAR_004100|||http://purl.uniprot.org/annotation/VAR_004101|||http://purl.uniprot.org/annotation/VAR_015539|||http://purl.uniprot.org/annotation/VAR_015540|||http://purl.uniprot.org/annotation/VAR_015541|||http://purl.uniprot.org/annotation/VAR_015542|||http://purl.uniprot.org/annotation/VAR_015907|||http://purl.uniprot.org/annotation/VAR_015908|||http://purl.uniprot.org/annotation/VAR_015909|||http://purl.uniprot.org/annotation/VAR_015910|||http://purl.uniprot.org/annotation/VAR_015911|||http://purl.uniprot.org/annotation/VAR_015912|||http://purl.uniprot.org/annotation/VAR_015913|||http://purl.uniprot.org/annotation/VAR_015914|||http://purl.uniprot.org/annotation/VAR_015915|||http://purl.uniprot.org/annotation/VAR_015916|||http://purl.uniprot.org/annotation/VAR_015917|||http://purl.uniprot.org/annotation/VAR_015918|||http://purl.uniprot.org/annotation/VAR_015919|||http://purl.uniprot.org/annotation/VAR_015920|||http://purl.uniprot.org/annotation/VAR_015921|||http://purl.uniprot.org/annotation/VAR_015922|||http://purl.uniprot.org/annotation/VAR_015923|||http://purl.uniprot.org/annotation/VAR_015924|||http://purl.uniprot.org/annotation/VAR_015925|||http://purl.uniprot.org/annotation/VAR_015926|||http://purl.uniprot.org/annotation/VAR_015927|||http://purl.uniprot.org/annotation/VAR_015928|||http://purl.uniprot.org/annotation/VAR_015929|||http://purl.uniprot.org/annotation/VAR_015930|||http://purl.uniprot.org/annotation/VAR_015931|||http://purl.uniprot.org/annotation/VAR_015932|||http://purl.uniprot.org/annotation/VAR_015933|||http://purl.uniprot.org/annotation/VAR_015934|||http://purl.uniprot.org/annotation/VAR_031518|||http://purl.uniprot.org/annotation/VAR_031519|||http://purl.uniprot.org/annotation/VAR_031520|||http://purl.uniprot.org/annotation/VAR_031521|||http://purl.uniprot.org/annotation/VAR_041429|||http://purl.uniprot.org/annotation/VAR_041430|||http://purl.uniprot.org/annotation/VAR_041431|||http://purl.uniprot.org/annotation/VAR_041432|||http://purl.uniprot.org/annotation/VAR_041433|||http://purl.uniprot.org/annotation/VAR_055986|||http://purl.uniprot.org/annotation/VAR_058395|||http://purl.uniprot.org/annotation/VAR_058396|||http://purl.uniprot.org/annotation/VAR_079535|||http://purl.uniprot.org/annotation/VAR_079536|||http://purl.uniprot.org/annotation/VAR_079537|||http://purl.uniprot.org/annotation/VAR_079538|||http://purl.uniprot.org/annotation/VAR_079539|||http://purl.uniprot.org/annotation/VAR_079540|||http://purl.uniprot.org/annotation/VAR_079541|||http://purl.uniprot.org/annotation/VAR_079542|||http://purl.uniprot.org/annotation/VAR_079543|||http://purl.uniprot.org/annotation/VAR_079544|||http://purl.uniprot.org/annotation/VAR_079545|||http://purl.uniprot.org/annotation/VAR_079546|||http://purl.uniprot.org/annotation/VAR_079547|||http://purl.uniprot.org/annotation/VAR_079548|||http://purl.uniprot.org/annotation/VAR_079549|||http://purl.uniprot.org/annotation/VSP_002898
http://togogenome.org/gene/9606:MED10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTT4                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix                                                                                  ^@                                                                                  Mediator of RNA polymerase II transcription subunit 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303151
http://togogenome.org/gene/9606:LRRFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7NGI8|||http://purl.uniprot.org/uniprot/B4DPC0|||http://purl.uniprot.org/uniprot/Q32MZ4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Leucine-rich repeat flightless-interacting protein 1|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248392|||http://purl.uniprot.org/annotation/VAR_027291|||http://purl.uniprot.org/annotation/VAR_027292|||http://purl.uniprot.org/annotation/VAR_027293|||http://purl.uniprot.org/annotation/VAR_027294|||http://purl.uniprot.org/annotation/VAR_027295|||http://purl.uniprot.org/annotation/VAR_027296|||http://purl.uniprot.org/annotation/VAR_036037|||http://purl.uniprot.org/annotation/VAR_056111|||http://purl.uniprot.org/annotation/VSP_020264|||http://purl.uniprot.org/annotation/VSP_020265|||http://purl.uniprot.org/annotation/VSP_046809|||http://purl.uniprot.org/annotation/VSP_046810|||http://purl.uniprot.org/annotation/VSP_046811|||http://purl.uniprot.org/annotation/VSP_046812|||http://purl.uniprot.org/annotation/VSP_046813|||http://purl.uniprot.org/annotation/VSP_046814
http://togogenome.org/gene/9606:SPMIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Protein SPMIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444981
http://togogenome.org/gene/9606:LMTK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISL5                                                                                  ^@                                                                                  Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Protein kinase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PRSS55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWB4                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||Disordered|||GPI-anchor amidated serine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Serine protease 55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328815|||http://purl.uniprot.org/annotation/PRO_0000449398|||http://purl.uniprot.org/annotation/VAR_042525|||http://purl.uniprot.org/annotation/VAR_042526|||http://purl.uniprot.org/annotation/VSP_044557
http://togogenome.org/gene/9606:ANKUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFN9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 1.|||In isoform 3.|||Protein ANKUB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344463|||http://purl.uniprot.org/annotation/VAR_045621|||http://purl.uniprot.org/annotation/VAR_045622|||http://purl.uniprot.org/annotation/VAR_045623|||http://purl.uniprot.org/annotation/VSP_059614|||http://purl.uniprot.org/annotation/VSP_059615|||http://purl.uniprot.org/annotation/VSP_059616
http://togogenome.org/gene/9606:STAC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In CMYP13; loss of interaction with CACNA1S.|||In isoform 2.|||In isoform 3.|||Phorbol-ester/DAG-type|||Polar residues|||SH3 1|||SH3 2|||SH3 and cysteine-rich domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232582|||http://purl.uniprot.org/annotation/VAR_071313|||http://purl.uniprot.org/annotation/VSP_017914|||http://purl.uniprot.org/annotation/VSP_055272
http://togogenome.org/gene/9606:FGF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3L5M4|||http://purl.uniprot.org/uniprot/P12034|||http://purl.uniprot.org/uniprot/Q8NBG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor|||Fibroblast growth factor 5|||In TCMGLY.|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008958|||http://purl.uniprot.org/annotation/PRO_5031604619|||http://purl.uniprot.org/annotation/VAR_025174|||http://purl.uniprot.org/annotation/VAR_072566|||http://purl.uniprot.org/annotation/VSP_001518|||http://purl.uniprot.org/annotation/VSP_001519
http://togogenome.org/gene/9606:RAB21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL25                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Defects in GTP hydrolysis. Does not affect the interaction with VAMP8 in response to starvation. Does not affect the interaction with TMED10.|||Defects in GTP-binding. Abolishes the interaction with VAMP8 in response to starvation. Abolishes the interaction with TMED10.|||Disordered|||Effector region|||N-acetylalanine|||Polar residues|||Ras-related protein Rab-21|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121205|||http://purl.uniprot.org/annotation/PRO_0000370768
http://togogenome.org/gene/9606:ABRACL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1F3                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand                                                                                  ^@                                                                                  Costars family protein ABRACL|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089521
http://togogenome.org/gene/9606:TGFBR3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BV60                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Pro residues|||Transforming growth factor-beta receptor type 3-like protein|||ZP; truncated                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000419495|||http://purl.uniprot.org/annotation/VSP_061943
http://togogenome.org/gene/9606:RNASE9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60153|||http://purl.uniprot.org/uniprot/W0UV99                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Inactive ribonuclease-like protein 9|||N-linked (GlcNAc...) asparagine|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030951|||http://purl.uniprot.org/annotation/PRO_5004797956|||http://purl.uniprot.org/annotation/VAR_034473|||http://purl.uniprot.org/annotation/VAR_052197|||http://purl.uniprot.org/annotation/VSP_041856
http://togogenome.org/gene/9606:BMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12644|||http://purl.uniprot.org/uniprot/Q53XC5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Bone morphogenetic protein 4|||Disordered|||In MCOPS6.|||In OFC11.|||In OFC11; also found in renal hypodysplasia patients.|||In a renal hypodysplasia patient.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033856|||http://purl.uniprot.org/annotation/PRO_0000033857|||http://purl.uniprot.org/annotation/PRO_5014309520|||http://purl.uniprot.org/annotation/VAR_016174|||http://purl.uniprot.org/annotation/VAR_043531|||http://purl.uniprot.org/annotation/VAR_043532|||http://purl.uniprot.org/annotation/VAR_043533|||http://purl.uniprot.org/annotation/VAR_043534|||http://purl.uniprot.org/annotation/VAR_043535|||http://purl.uniprot.org/annotation/VAR_043536|||http://purl.uniprot.org/annotation/VAR_043537|||http://purl.uniprot.org/annotation/VAR_058314|||http://purl.uniprot.org/annotation/VAR_058315|||http://purl.uniprot.org/annotation/VAR_058316|||http://purl.uniprot.org/annotation/VAR_058317|||http://purl.uniprot.org/annotation/VAR_058318
http://togogenome.org/gene/9606:H2BC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-A|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-lactoyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071842
http://togogenome.org/gene/9606:FREY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JXX5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Protein Frey 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394235|||http://purl.uniprot.org/annotation/VAR_063154
http://togogenome.org/gene/9606:PDZK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2W1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF3|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058287|||http://purl.uniprot.org/annotation/VSP_044637
http://togogenome.org/gene/9606:GPR65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5B0C2|||http://purl.uniprot.org/uniprot/Q8IYL9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increased lysosomal pH; increased lipid droplets accumulation.|||N-linked (GlcNAc...) asparagine|||Psychosine receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070087|||http://purl.uniprot.org/annotation/VAR_022064
http://togogenome.org/gene/9606:RNF208                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0X6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||RING finger protein 208|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274613
http://togogenome.org/gene/9606:TAS1R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE23                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 1 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012957|||http://purl.uniprot.org/annotation/VAR_020787|||http://purl.uniprot.org/annotation/VAR_027901|||http://purl.uniprot.org/annotation/VAR_027902|||http://purl.uniprot.org/annotation/VAR_061199|||http://purl.uniprot.org/annotation/VAR_061200|||http://purl.uniprot.org/annotation/VAR_061201|||http://purl.uniprot.org/annotation/VAR_061202
http://togogenome.org/gene/9606:OR1L8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVC5|||http://purl.uniprot.org/uniprot/Q8NGR8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1L8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150446|||http://purl.uniprot.org/annotation/VAR_024087|||http://purl.uniprot.org/annotation/VAR_024088
http://togogenome.org/gene/9606:NOL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6R4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleolar protein 6|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215647|||http://purl.uniprot.org/annotation/VAR_053541|||http://purl.uniprot.org/annotation/VAR_053542|||http://purl.uniprot.org/annotation/VSP_013530|||http://purl.uniprot.org/annotation/VSP_013531|||http://purl.uniprot.org/annotation/VSP_013532
http://togogenome.org/gene/9606:ZNF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS94|||http://purl.uniprot.org/uniprot/P17098                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Polar residues|||Zinc finger protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047331
http://togogenome.org/gene/9606:ZNF296                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Zinc finger protein 296                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047542
http://togogenome.org/gene/9606:CUBN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60494                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  CUB 1|||CUB 10|||CUB 11|||CUB 12|||CUB 13|||CUB 14|||CUB 15|||CUB 16|||CUB 17|||CUB 18|||CUB 19|||CUB 2|||CUB 20|||CUB 21|||CUB 22|||CUB 23|||CUB 24|||CUB 25|||CUB 26|||CUB 27|||CUB 3|||CUB 4|||CUB 5|||CUB 6|||CUB 7|||CUB 8|||CUB 9|||Cleavage; by furin|||Cubilin|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||Found in a renal cell carcinoma case; somatic mutation.|||Higher frequency in West Africans than in individuals of European ancestry; occurs with variants F-2153 and V-2984 only in individuals of European ancestry.|||Higher frequency in West Africans than in individuals of European ancestry; occurs with variants V-2984 and G-3002 only in individuals of European ancestry.|||In IGS1.|||In IGS1; decreases strongly the CBLIF binding affinity.|||In IGS1; unknown pathological significance; results in intracellular retention of the mutant protein.|||In PROCHOB.|||In PROCHOB; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In a breast cancer sample; somatic mutation; may be associated with albuminuria and slightly increased glomerular filtration rate.|||In a colorectal cancer sample; somatic mutation.|||Interaction with AMN|||May be associated with albuminuria and slightly increased glomerular filtration rate.|||N-linked (GlcNAc...) asparagine|||Not found in West Africans; occurs with variants F-2153 and G-3002 only in individuals of European ancestry; associated with albuminuria in individuals of European ancestry and African Americans, both with and without diabetes; may be associated with increased risk of developing persistent microalbuminuria in individuals with type I diabetes.|||Phosphothreonine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046072|||http://purl.uniprot.org/annotation/PRO_0000046073|||http://purl.uniprot.org/annotation/VAR_025284|||http://purl.uniprot.org/annotation/VAR_025285|||http://purl.uniprot.org/annotation/VAR_025286|||http://purl.uniprot.org/annotation/VAR_025287|||http://purl.uniprot.org/annotation/VAR_025288|||http://purl.uniprot.org/annotation/VAR_025289|||http://purl.uniprot.org/annotation/VAR_025290|||http://purl.uniprot.org/annotation/VAR_025291|||http://purl.uniprot.org/annotation/VAR_025292|||http://purl.uniprot.org/annotation/VAR_025293|||http://purl.uniprot.org/annotation/VAR_025294|||http://purl.uniprot.org/annotation/VAR_025295|||http://purl.uniprot.org/annotation/VAR_025296|||http://purl.uniprot.org/annotation/VAR_025297|||http://purl.uniprot.org/annotation/VAR_025298|||http://purl.uniprot.org/annotation/VAR_025299|||http://purl.uniprot.org/annotation/VAR_025300|||http://purl.uniprot.org/annotation/VAR_025301|||http://purl.uniprot.org/annotation/VAR_035829|||http://purl.uniprot.org/annotation/VAR_035830|||http://purl.uniprot.org/annotation/VAR_035831|||http://purl.uniprot.org/annotation/VAR_035832|||http://purl.uniprot.org/annotation/VAR_047443|||http://purl.uniprot.org/annotation/VAR_047444|||http://purl.uniprot.org/annotation/VAR_047445|||http://purl.uniprot.org/annotation/VAR_047446|||http://purl.uniprot.org/annotation/VAR_047447|||http://purl.uniprot.org/annotation/VAR_047448|||http://purl.uniprot.org/annotation/VAR_047449|||http://purl.uniprot.org/annotation/VAR_047450|||http://purl.uniprot.org/annotation/VAR_047451|||http://purl.uniprot.org/annotation/VAR_047452|||http://purl.uniprot.org/annotation/VAR_047453|||http://purl.uniprot.org/annotation/VAR_055714|||http://purl.uniprot.org/annotation/VAR_061154|||http://purl.uniprot.org/annotation/VAR_064704|||http://purl.uniprot.org/annotation/VAR_084400|||http://purl.uniprot.org/annotation/VAR_084401|||http://purl.uniprot.org/annotation/VAR_084402|||http://purl.uniprot.org/annotation/VAR_084403|||http://purl.uniprot.org/annotation/VAR_084404|||http://purl.uniprot.org/annotation/VAR_084405|||http://purl.uniprot.org/annotation/VAR_084406|||http://purl.uniprot.org/annotation/VAR_084407|||http://purl.uniprot.org/annotation/VAR_084408|||http://purl.uniprot.org/annotation/VAR_084409|||http://purl.uniprot.org/annotation/VAR_084410|||http://purl.uniprot.org/annotation/VAR_084411|||http://purl.uniprot.org/annotation/VAR_084412|||http://purl.uniprot.org/annotation/VAR_084413|||http://purl.uniprot.org/annotation/VAR_084414|||http://purl.uniprot.org/annotation/VAR_084415|||http://purl.uniprot.org/annotation/VAR_084416|||http://purl.uniprot.org/annotation/VAR_084417|||http://purl.uniprot.org/annotation/VAR_084418|||http://purl.uniprot.org/annotation/VAR_084419|||http://purl.uniprot.org/annotation/VAR_084420|||http://purl.uniprot.org/annotation/VAR_084421|||http://purl.uniprot.org/annotation/VAR_084422|||http://purl.uniprot.org/annotation/VAR_084423|||http://purl.uniprot.org/annotation/VAR_084424|||http://purl.uniprot.org/annotation/VAR_084425|||http://purl.uniprot.org/annotation/VAR_084426|||http://purl.uniprot.org/annotation/VAR_084427
http://togogenome.org/gene/9606:UNC13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISZ1|||http://purl.uniprot.org/uniprot/Q8NB66                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||Disordered|||MHD1|||MHD2|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog C|||Rare variant; may act as a phenotype modifier in EIEE13 patients carrying SCN8A mutations.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188578|||http://purl.uniprot.org/annotation/VAR_052468|||http://purl.uniprot.org/annotation/VAR_061873|||http://purl.uniprot.org/annotation/VAR_067540|||http://purl.uniprot.org/annotation/VAR_067541
http://togogenome.org/gene/9606:ARL5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NH57                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding                                                                                  ^@                                                                                  N-myristoyl glycine|||Putative ADP-ribosylation factor-like protein 5C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332303
http://togogenome.org/gene/9606:SIGIRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JFX4|||http://purl.uniprot.org/uniprot/Q6IA17                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type III membrane protein|||Ig-like|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Single Ig IL-1-related receptor|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000099065|||http://purl.uniprot.org/annotation/VAR_058702|||http://purl.uniprot.org/annotation/VAR_074164|||http://purl.uniprot.org/annotation/VAR_074165|||http://purl.uniprot.org/annotation/VSP_015717
http://togogenome.org/gene/9606:PHACTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75167                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2 and isoform 5.|||N-myristoyl glycine|||Phosphatase and actin regulator 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RPEL 1|||RPEL 2|||RPEL 3|||RPEL 4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126636|||http://purl.uniprot.org/annotation/VAR_045628|||http://purl.uniprot.org/annotation/VAR_053646|||http://purl.uniprot.org/annotation/VSP_012272|||http://purl.uniprot.org/annotation/VSP_012273
http://togogenome.org/gene/9606:GTF3C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969F1                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||General transcription factor 3C polypeptide 6|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089507
http://togogenome.org/gene/9606:SIK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0K1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Constitutively active.|||Disordered|||N6-acetyllysine; by EP300|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SIK2|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086662|||http://purl.uniprot.org/annotation/VAR_041093|||http://purl.uniprot.org/annotation/VAR_041094|||http://purl.uniprot.org/annotation/VAR_041095|||http://purl.uniprot.org/annotation/VAR_051667|||http://purl.uniprot.org/annotation/VAR_051668
http://togogenome.org/gene/9606:DAZAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z569|||http://purl.uniprot.org/uniprot/Q96EP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DAZ-associated protein 1|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Polar residues|||Pro residues|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081565|||http://purl.uniprot.org/annotation/VAR_035480|||http://purl.uniprot.org/annotation/VSP_009441
http://togogenome.org/gene/9606:TSGA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A218MIY9|||http://purl.uniprot.org/uniprot/Q9BZW7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with HIF1A|||Phosphoserine|||Testis-specific gene 10 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307125|||http://purl.uniprot.org/annotation/VSP_054409|||http://purl.uniprot.org/annotation/VSP_054410
http://togogenome.org/gene/9606:EBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2U8|||http://purl.uniprot.org/uniprot/Q9UH73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C5-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||IPT/TIG|||Impaired EBF1-mediated cell differentiation and gene expression mostly without changing EBF1 occupancy.|||In isoform 2.|||Interaction with DNA|||N-acetylmethionine|||Polar residues|||Transcription factor COE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000107825|||http://purl.uniprot.org/annotation/VSP_012304|||http://purl.uniprot.org/annotation/VSP_012305
http://togogenome.org/gene/9606:ZNF266                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3F2YPB8|||http://purl.uniprot.org/uniprot/Q14584                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Zinc finger protein 266                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047493|||http://purl.uniprot.org/annotation/VAR_014828
http://togogenome.org/gene/9606:C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR57|||http://purl.uniprot.org/uniprot/P01024|||http://purl.uniprot.org/uniprot/V9HWA9                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Acylation stimulating protein|||Anaphylatoxin-like|||C3-beta-c|||C3a anaphylatoxin|||Cleavage; by C3 convertase|||Cleavage; by S.pyogenes SpeB|||Cleavage; by carboxypeptidases|||Cleavage; by factor I|||Complement C3|||Complement C3 alpha chain|||Complement C3 beta chain|||Complement C3/4/5 macroglobulin|||Complement C3b alpha' chain|||Complement C3c alpha' chain fragment 1|||Complement C3c alpha' chain fragment 2|||Complement C3d fragment|||Complement C3dg fragment|||Complement C3f fragment|||Complement C3g fragment|||Coordinates Mg2+ for interaction with Complement factor B Bb fragment|||Disordered|||Impaired binding of C3d to CR2.|||Impaired binding of C3d to CR2; when associated with A-1163.|||In AHUS5.|||In AHUS5; leads to impaired binding to the regulator CD46/MCP and resistance to cleavage by factor I.|||In ARMD9; results in resistance to proteolytic inactivation by CFH and CFI.|||In C3D; impairs secretion; variant confirmed at protein level.|||In allele C3F; associated with susceptibility to ARMD9; results in decreased binding affinity for regulator factor H; results in reduced sensitivity to cleavage by factor I.|||Interaction with CFP/properdin|||Interchain (between beta and alpha chains)|||Isoglutamyl cysteine thioester (Cys-Gln)|||Macroglobulin|||Minor effect on binding of C3d to CR2.|||N-linked (GlcNAc...) asparagine|||NTR|||No effect on binding of C3d to CR2.|||No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109.|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005907|||http://purl.uniprot.org/annotation/PRO_0000005908|||http://purl.uniprot.org/annotation/PRO_0000005909|||http://purl.uniprot.org/annotation/PRO_0000005910|||http://purl.uniprot.org/annotation/PRO_0000005911|||http://purl.uniprot.org/annotation/PRO_0000005912|||http://purl.uniprot.org/annotation/PRO_0000005913|||http://purl.uniprot.org/annotation/PRO_0000005914|||http://purl.uniprot.org/annotation/PRO_0000005915|||http://purl.uniprot.org/annotation/PRO_0000005916|||http://purl.uniprot.org/annotation/PRO_0000273948|||http://purl.uniprot.org/annotation/PRO_0000419935|||http://purl.uniprot.org/annotation/PRO_0000430430|||http://purl.uniprot.org/annotation/PRO_5002803789|||http://purl.uniprot.org/annotation/PRO_5004777240|||http://purl.uniprot.org/annotation/VAR_001983|||http://purl.uniprot.org/annotation/VAR_001984|||http://purl.uniprot.org/annotation/VAR_001985|||http://purl.uniprot.org/annotation/VAR_019206|||http://purl.uniprot.org/annotation/VAR_019207|||http://purl.uniprot.org/annotation/VAR_019208|||http://purl.uniprot.org/annotation/VAR_020262|||http://purl.uniprot.org/annotation/VAR_029326|||http://purl.uniprot.org/annotation/VAR_029792|||http://purl.uniprot.org/annotation/VAR_029793|||http://purl.uniprot.org/annotation/VAR_063213|||http://purl.uniprot.org/annotation/VAR_063214|||http://purl.uniprot.org/annotation/VAR_063215|||http://purl.uniprot.org/annotation/VAR_063216|||http://purl.uniprot.org/annotation/VAR_063217|||http://purl.uniprot.org/annotation/VAR_063218|||http://purl.uniprot.org/annotation/VAR_063219|||http://purl.uniprot.org/annotation/VAR_063220|||http://purl.uniprot.org/annotation/VAR_063654|||http://purl.uniprot.org/annotation/VAR_063655|||http://purl.uniprot.org/annotation/VAR_070941
http://togogenome.org/gene/9606:TPCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59G56|||http://purl.uniprot.org/uniprot/Q8NHX9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with SHEP10.|||Cytoplasmic|||Extracellular|||Gain of function. Increased sodium currents.|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Pore-forming|||Interaction with phosphatidylinositol 3,5-bisphosphate|||Ion transport|||Localizes at the plasma membrane.|||N-linked (GlcNAc...) asparagine|||No effect on lysosomal location. Loss of NAADP-sensitive calcium-release channel activity. Inhibits Ebola virus infection.|||Not activated by phosphatidylinositol 3,5-bisphosphate.|||Reduces binding with phosphatidylinositol 3,5-bisphosphate.|||Requires both phosphatidylinositol 3,5-bisphosphate and a positive membrane potential for activation.|||Strongly reduces binding with phosphatidylinositol 3,5-bisphosphate.|||Strongly reduces binding with phosphatidylinositol 3,5-bisphosphate. Decreases sodium transport. No effect on calcium release.|||Two pore channel protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000276856|||http://purl.uniprot.org/annotation/PRO_5004252476|||http://purl.uniprot.org/annotation/VAR_030492|||http://purl.uniprot.org/annotation/VAR_030493|||http://purl.uniprot.org/annotation/VAR_030494|||http://purl.uniprot.org/annotation/VAR_047956
http://togogenome.org/gene/9606:SLC35D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTN3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Found in a patient with type II collagenopathy; markedly decreases transporter activity.|||Helical|||In SHNKND; loss of transporter activity.|||In isoform 2.|||Nucleotide sugar transporter SLC35D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213394|||http://purl.uniprot.org/annotation/VAR_042729|||http://purl.uniprot.org/annotation/VAR_087509|||http://purl.uniprot.org/annotation/VAR_087510|||http://purl.uniprot.org/annotation/VAR_087511|||http://purl.uniprot.org/annotation/VSP_056860|||http://purl.uniprot.org/annotation/VSP_056861
http://togogenome.org/gene/9606:SELL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14151                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||EGF-like|||Extracellular|||Helical|||Impairs interaction with cognate oligosaccharide. Abolishes cell rolling on glycan ligands.|||In isoform 2.|||L-selectin|||Loss of one glycosylation site.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017475|||http://purl.uniprot.org/annotation/PRO_0000017476|||http://purl.uniprot.org/annotation/VAR_019134|||http://purl.uniprot.org/annotation/VAR_019135|||http://purl.uniprot.org/annotation/VAR_019136|||http://purl.uniprot.org/annotation/VAR_019137|||http://purl.uniprot.org/annotation/VSP_042650
http://togogenome.org/gene/9606:C9orf40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Pro residues|||Uncharacterized protein C9orf40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089682
http://togogenome.org/gene/9606:C6orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C6orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089537|||http://purl.uniprot.org/annotation/VAR_022939|||http://purl.uniprot.org/annotation/VAR_030643
http://togogenome.org/gene/9606:ZYG11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0D3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ELOC.|||Complete loss of N-degron binding.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||Protein zyg-11 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305087|||http://purl.uniprot.org/annotation/VSP_028224
http://togogenome.org/gene/9606:ZNF436                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0F3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||KRAB|||Polar residues|||Zinc finger protein 436                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047584|||http://purl.uniprot.org/annotation/VAR_035579
http://togogenome.org/gene/9606:H2AC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04908|||http://purl.uniprot.org/uniprot/Q08AJ9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1-B/E|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055237
http://togogenome.org/gene/9606:G3BP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13283|||http://purl.uniprot.org/uniprot/Q5U0Q1|||http://purl.uniprot.org/uniprot/Q6ZP53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with CAPRIN1 and ability to undergo liquid-liquid phase separation. Abolished interaction with USP10.|||Abolished mRNA-binding and ability to undergo liquid-liquid phase separation.|||Acidic disordered region|||Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Cleavage; by human enterovirus 71 protease 3C|||Cytoplasmic. Partially nuclear; when associated with E-149.|||Decreased interaction with USP10.|||Dimethylated arginine; alternate|||Disordered|||Does not affect interaction with USP10.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-64 and R-123.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-357 and R-376.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-357 and R-393.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-376 and R-393.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123,R-357, R-376 and R-393.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-64 and R-76.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-50 and R-59.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-50 and R-64.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-59, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-59, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-59 and R-64.|||In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-50, R-59, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-50, R-59, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-50, R-59 and R-64.|||In isoform 2.|||Loss of cleavage by human enterovirus 71 protease 3C.|||Mimics phosphorylation; decreased ability to undergo liquid-liquid phase separation. Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization.|||N6-acetyllysine; alternate|||NTF2|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||RG-rich region|||RRM|||Ras GTPase-activating protein-binding protein 1|||Removed|||Slightly increased ability to undergo liquid-liquid phase separation. Increased ability to undergo liquid-liquid phase separation; when associated with A-232. Cytoplasmic.|||Slightly increased ability to undergo liquid-liquid phase separation; when associated with A-149. Cytoplasmic. Partially nuclear; when associated with E-149. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194798|||http://purl.uniprot.org/annotation/VSP_056280|||http://purl.uniprot.org/annotation/VSP_056281
http://togogenome.org/gene/9606:CES4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XG92|||http://purl.uniprot.org/uniprot/Q6P2E5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acyl-ester intermediate|||Carboxylesterase 4A|||Carboxylesterase type B|||Charge relay system|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 6 and isoform 7.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325923|||http://purl.uniprot.org/annotation/VSP_032480|||http://purl.uniprot.org/annotation/VSP_032483|||http://purl.uniprot.org/annotation/VSP_032485|||http://purl.uniprot.org/annotation/VSP_040063|||http://purl.uniprot.org/annotation/VSP_040064|||http://purl.uniprot.org/annotation/VSP_040065|||http://purl.uniprot.org/annotation/VSP_040066|||http://purl.uniprot.org/annotation/VSP_040067
http://togogenome.org/gene/9606:TMEM204                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSN7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 204                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089865|||http://purl.uniprot.org/annotation/VAR_051435
http://togogenome.org/gene/9606:CXorf51B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTR3|||http://purl.uniprot.org/uniprot/P0DPH9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Uncharacterized protein CXorf51A|||Uncharacterized protein CXorf51B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000444693|||http://purl.uniprot.org/annotation/PRO_0000444694
http://togogenome.org/gene/9606:ACAA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R2M6|||http://purl.uniprot.org/uniprot/A0A140VJX0|||http://purl.uniprot.org/uniprot/P09110                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-ketoacyl-CoA thiolase, peroxisomal|||Abolished localization to peroxisomes.|||Acyl-thioester intermediate|||Does not affect localization to peroxisomes.|||In S3E mutant; Abolished localization to peroxisomes.|||In isoform 2.|||PTS2-type peroxisomal targeting signal|||Peroxisome|||Phosphothreonine|||Proton acceptor|||Thiolase C-terminal|||Thiolase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034067|||http://purl.uniprot.org/annotation/VAR_011904|||http://purl.uniprot.org/annotation/VAR_069148|||http://purl.uniprot.org/annotation/VSP_046195|||http://purl.uniprot.org/annotation/VSP_046196
http://togogenome.org/gene/9606:EPAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW07|||http://purl.uniprot.org/uniprot/Q99814                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine|||4-hydroxyproline|||Abolishes hypoxia-inducible transcriptional activation of ctaD.|||CTAD|||DNA-binding|||Disordered|||Endothelial PAS domain-containing protein 1|||HIF-1 alpha C-terminal transactivation|||In ECYT4.|||In ECYT4; affects the interaction with EGLN1 and VHL.|||In ECYT4; gain of function; affects hydroxylation.|||In ECYT4; impairs interaction with EGLN1 and VHL.|||In ECYT4; impairs interaction with EGLN1.|||NTAD|||PAC|||PAS 1|||PAS 2|||Phosphothreonine|||Polar residues|||Required for heterodimer formation with ARNT|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127419|||http://purl.uniprot.org/annotation/VAR_042443|||http://purl.uniprot.org/annotation/VAR_061261|||http://purl.uniprot.org/annotation/VAR_061262|||http://purl.uniprot.org/annotation/VAR_067358|||http://purl.uniprot.org/annotation/VAR_067359|||http://purl.uniprot.org/annotation/VAR_067360|||http://purl.uniprot.org/annotation/VAR_067361|||http://purl.uniprot.org/annotation/VAR_067362
http://togogenome.org/gene/9606:NANOS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY41                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Motif|||Region|||Sequence Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2HC 1|||C2HC 2|||Disordered|||Essential for its translational repressor activity|||Found in a patient affected by oligo-astheno-teratozoospermia also carrying H-246 on the same allele; requires 2 nucleotide substitutions; unknown pathological significance.|||Found in a patient affected by oligo-astheno-teratozoospermia also carrying Y-276 on the same allele; unknown pathological significance.|||In SPGF12.|||Nanos homolog 1|||Nanos-type|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207685|||http://purl.uniprot.org/annotation/VAR_070569|||http://purl.uniprot.org/annotation/VAR_070570|||http://purl.uniprot.org/annotation/VAR_070571|||http://purl.uniprot.org/annotation/VAR_070572|||http://purl.uniprot.org/annotation/VAR_070573
http://togogenome.org/gene/9606:PTRHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GMV3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Found in a family with early-onset autosomal recessive parkinsonism and intellectual disability; unknown pathological significance.|||Putative peptidyl-tRNA hydrolase PTRHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321818|||http://purl.uniprot.org/annotation/VAR_078547|||http://purl.uniprot.org/annotation/VAR_078548
http://togogenome.org/gene/9606:TEK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02763|||http://purl.uniprot.org/uniprot/Q59HG2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with SHC1.|||Angiopoietin-1 receptor|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the autophosphorylation increases when associated with Phe-897.|||Found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the hyperphosphorylation increases when associated with Leu-915.|||Found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation.|||Found in patients with solitary and multiple sporadic venous malformations; increased ligand-independent autophosphorylation; novel location at endoplasmic reticulum and Golgi apparatus; partially retained at endoplasmic reticulum and Golgi apparatus.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In GLC3E; enhanced proteasomal degradation.|||In GLC3E; formation of protein aggregates.|||In GLC3E; reduced response to ligand; loss of ligand-induced phosphorylation; no effect on basal membrane location.|||In GLC3E; unknown pathological significance; 10-fold decrease of Tyr-1102 phosphorylation; no effect on membrane location.|||In VMCM; also found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation and kinase activation.|||In VMCM; increased ligand-independent autophosphorylation and kinase activation.|||In VMCM; increased ligand-independent autophosphorylation and kinase activation; no effect on location at membrane.|||In VMCM; strongly increased ligand-independent autophosphorylation and kinase activation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of kinase activity.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduces protein abundance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024474|||http://purl.uniprot.org/annotation/VAR_006352|||http://purl.uniprot.org/annotation/VAR_008716|||http://purl.uniprot.org/annotation/VAR_024578|||http://purl.uniprot.org/annotation/VAR_035714|||http://purl.uniprot.org/annotation/VAR_041855|||http://purl.uniprot.org/annotation/VAR_041856|||http://purl.uniprot.org/annotation/VAR_041857|||http://purl.uniprot.org/annotation/VAR_041858|||http://purl.uniprot.org/annotation/VAR_041859|||http://purl.uniprot.org/annotation/VAR_041860|||http://purl.uniprot.org/annotation/VAR_041861|||http://purl.uniprot.org/annotation/VAR_041862|||http://purl.uniprot.org/annotation/VAR_048002|||http://purl.uniprot.org/annotation/VAR_048003|||http://purl.uniprot.org/annotation/VAR_066606|||http://purl.uniprot.org/annotation/VAR_066607|||http://purl.uniprot.org/annotation/VAR_066608|||http://purl.uniprot.org/annotation/VAR_066609|||http://purl.uniprot.org/annotation/VAR_066610|||http://purl.uniprot.org/annotation/VAR_066611|||http://purl.uniprot.org/annotation/VAR_078045|||http://purl.uniprot.org/annotation/VAR_078046|||http://purl.uniprot.org/annotation/VAR_078047|||http://purl.uniprot.org/annotation/VAR_078048|||http://purl.uniprot.org/annotation/VAR_078049|||http://purl.uniprot.org/annotation/VAR_078050|||http://purl.uniprot.org/annotation/VAR_078051|||http://purl.uniprot.org/annotation/VAR_078052|||http://purl.uniprot.org/annotation/VAR_078053|||http://purl.uniprot.org/annotation/VAR_078054|||http://purl.uniprot.org/annotation/VSP_042137|||http://purl.uniprot.org/annotation/VSP_042138|||http://purl.uniprot.org/annotation/VSP_042139
http://togogenome.org/gene/9606:ADGRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YN44|||http://purl.uniprot.org/uniprot/Q96PE1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor A2|||Basic residues|||Cleavage; by thrombin|||Cytoplasmic|||Disordered|||Extracellular|||Fails to interact with DLG1.|||Found in a family with atypical autism and severe epilepsy; unknown pathological significance.|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Ig-like|||In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Minimal effect on thrombin cleavage. Abolishes thrombin cleavage; when associated with A-369.|||Minimal effect on thrombin cleavage. Abolishes thrombin cleavage; when associated with G-398.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Polar residues|||Pro residues|||RGD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012898|||http://purl.uniprot.org/annotation/PRO_5004282475|||http://purl.uniprot.org/annotation/VAR_072079|||http://purl.uniprot.org/annotation/VAR_072561|||http://purl.uniprot.org/annotation/VSP_010076|||http://purl.uniprot.org/annotation/VSP_036215
http://togogenome.org/gene/9606:ARHGAP30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRJ8|||http://purl.uniprot.org/uniprot/A0A0A0MRJ9|||http://purl.uniprot.org/uniprot/Q7Z6I6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 30|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280478|||http://purl.uniprot.org/annotation/VAR_031157|||http://purl.uniprot.org/annotation/VAR_031158|||http://purl.uniprot.org/annotation/VSP_023732|||http://purl.uniprot.org/annotation/VSP_023733|||http://purl.uniprot.org/annotation/VSP_023734|||http://purl.uniprot.org/annotation/VSP_023735
http://togogenome.org/gene/9606:RHBDL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58872                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||Helical|||In isoform 2.|||In isoform 3.|||Nucleophile|||Rhomboid-related protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206177|||http://purl.uniprot.org/annotation/VAR_024593|||http://purl.uniprot.org/annotation/VSP_056259|||http://purl.uniprot.org/annotation/VSP_056260
http://togogenome.org/gene/9606:H3C11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:PCSK1N                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHG2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Abolishes inhibition of PCSK1.|||Big LEN|||Big PEN-LEN|||Big SAAS|||C-terminal inhibitory domain; interacts with PCSK1|||Disordered|||Greatly reduces inhibition of PCSK1.|||KEP|||Little LEN|||Little SAAS|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||PEN|||ProSAAS|||ProSAAS(1-180)|||Reduces inhibition of PCSK1.|||Sufficient for inhibition of PCSK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259673|||http://purl.uniprot.org/annotation/PRO_0000259674|||http://purl.uniprot.org/annotation/PRO_0000259675|||http://purl.uniprot.org/annotation/PRO_0000259676|||http://purl.uniprot.org/annotation/PRO_0000259677|||http://purl.uniprot.org/annotation/PRO_0000259678|||http://purl.uniprot.org/annotation/PRO_0000259679|||http://purl.uniprot.org/annotation/PRO_0000259680|||http://purl.uniprot.org/annotation/VAR_028971
http://togogenome.org/gene/9606:CRYGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8I5|||http://purl.uniprot.org/uniprot/Q8WXF5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Disordered|||Gamma-crystallin N|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311281|||http://purl.uniprot.org/annotation/VSP_029507|||http://purl.uniprot.org/annotation/VSP_029508
http://togogenome.org/gene/9606:SLC35A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78382                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-sialic acid transporter|||Cytoplasmic|||Disordered|||Helical|||In CDG2F.|||In CDG2F; results in decreased CMP-sialic acid transmembrane transporter activity when expressed in a heterologous system; does not affect localization to Golgi apparatus.|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213351|||http://purl.uniprot.org/annotation/VAR_086836|||http://purl.uniprot.org/annotation/VAR_086837|||http://purl.uniprot.org/annotation/VAR_086838|||http://purl.uniprot.org/annotation/VSP_042916
http://togogenome.org/gene/9606:ZFHX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2P1H683|||http://purl.uniprot.org/uniprot/B7ZM83|||http://purl.uniprot.org/uniprot/B9EK48|||http://purl.uniprot.org/uniprot/Q9C0A1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||Homeobox|||Homeobox 1|||Homeobox 2|||Homeobox 3|||In MARSIS.|||In isoform 2.|||Polar residues|||Pro residues|||Zinc finger homeobox protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047243|||http://purl.uniprot.org/annotation/VAR_081116|||http://purl.uniprot.org/annotation/VSP_039496|||http://purl.uniprot.org/annotation/VSP_039497
http://togogenome.org/gene/9606:ZNF800                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TB10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 800                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304410|||http://purl.uniprot.org/annotation/VAR_052904
http://togogenome.org/gene/9606:EML6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMW3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Echinoderm microtubule-associated protein-like 6|||In isoform 2.|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 15|||WD 16|||WD 17|||WD 18|||WD 19|||WD 2|||WD 20|||WD 21|||WD 22|||WD 23|||WD 24|||WD 25|||WD 26|||WD 27|||WD 28|||WD 29|||WD 3|||WD 30|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325976|||http://purl.uniprot.org/annotation/VSP_034221
http://togogenome.org/gene/9606:ENTPD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDM7|||http://purl.uniprot.org/uniprot/B4DHS2|||http://purl.uniprot.org/uniprot/B4DU64|||http://purl.uniprot.org/uniprot/B4E1D1|||http://purl.uniprot.org/uniprot/O75354                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect nucleoside-triphosphatase activity. Does not affeet KM for GDP.|||Ectonucleoside triphosphate diphosphohydrolase 6|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209913|||http://purl.uniprot.org/annotation/VAR_017863|||http://purl.uniprot.org/annotation/VAR_027812|||http://purl.uniprot.org/annotation/VAR_027813|||http://purl.uniprot.org/annotation/VAR_027814|||http://purl.uniprot.org/annotation/VAR_050309|||http://purl.uniprot.org/annotation/VSP_039122|||http://purl.uniprot.org/annotation/VSP_054314
http://togogenome.org/gene/9606:PHOSPHO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCT1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphatase activity.|||In isoform 2.|||In isoform 3.|||Nucleophile|||Phosphoethanolamine/phosphocholine phosphatase|||Proton donor|||Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-123.|||Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-43.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068829|||http://purl.uniprot.org/annotation/VSP_040624|||http://purl.uniprot.org/annotation/VSP_045709
http://togogenome.org/gene/9606:MB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1K0FU49|||http://purl.uniprot.org/uniprot/P02144                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Globin family profile|||Myoglobin|||Phosphoserine|||Phosphothreonine|||Removed|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053303|||http://purl.uniprot.org/annotation/VAR_003180|||http://purl.uniprot.org/annotation/VAR_003181|||http://purl.uniprot.org/annotation/VAR_003182|||http://purl.uniprot.org/annotation/VAR_003183
http://togogenome.org/gene/9606:NELFCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0UI80|||http://purl.uniprot.org/uniprot/Q8IXH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 3.|||In isoform NELF-D.|||Negative elongation factor C/D|||Reduces RNA binding; when associated with M-315, M-371, M-372, M-374, M-384, M-388, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-372, M-374, M-384, M-388 and Q-419.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-372, M-374, M-384, M-388 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-372, M-374, M-384, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-372, M-374, M-388, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-372, M-384, M-388, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-371, M-374, M-384, M-388, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-315, M-372, M-374, M-384, M-388, Q-419 and Q-506.|||Reduces RNA binding; when associated with Q-291, M-371, M-372, M-374, M-384, M-388, Q-419 and Q-506.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019456|||http://purl.uniprot.org/annotation/VSP_008950|||http://purl.uniprot.org/annotation/VSP_008951|||http://purl.uniprot.org/annotation/VSP_018769
http://togogenome.org/gene/9606:S100A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||Protein S100-A14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144021
http://togogenome.org/gene/9606:DST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGY0|||http://purl.uniprot.org/uniprot/B4DSS9|||http://purl.uniprot.org/uniprot/E9PHM6|||http://purl.uniprot.org/uniprot/F6QMI7|||http://purl.uniprot.org/uniprot/Q03001|||http://purl.uniprot.org/uniprot/Q6P0N6                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Actin-binding|||Basic and acidic residues|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Dystonin|||EF-hand|||EF-hand 1|||EF-hand 2|||GAR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Loss of association with microtubule growing ends.|||Loss of interaction with MAPRE1 and association with microtubule growing ends.|||Loss of interaction with MAPRE1 and association with the growing microtubule plus ends.|||Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7552.|||Loss of interaction with MAPRE1 and association with the growing microtubule plus ends; when associated with N-7553.|||Microtubule tip localization signal|||Nuclear localization signal; in isoform 6|||Phosphoserine|||Plectin 1|||Plectin 2|||Plectin 3|||Plectin 4|||Plectin 5|||Polar residues|||SH3|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 23|||Spectrin 24|||Spectrin 25|||Spectrin 26|||Spectrin 27|||Spectrin 28|||Spectrin 29|||Spectrin 3|||Spectrin 30|||Spectrin 31|||Spectrin 32|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078138|||http://purl.uniprot.org/annotation/VAR_063045|||http://purl.uniprot.org/annotation/VAR_063046|||http://purl.uniprot.org/annotation/VAR_063047|||http://purl.uniprot.org/annotation/VAR_063048|||http://purl.uniprot.org/annotation/VSP_041524|||http://purl.uniprot.org/annotation/VSP_041525|||http://purl.uniprot.org/annotation/VSP_041526|||http://purl.uniprot.org/annotation/VSP_041527|||http://purl.uniprot.org/annotation/VSP_041528|||http://purl.uniprot.org/annotation/VSP_041529|||http://purl.uniprot.org/annotation/VSP_041530|||http://purl.uniprot.org/annotation/VSP_041531|||http://purl.uniprot.org/annotation/VSP_041532|||http://purl.uniprot.org/annotation/VSP_041533|||http://purl.uniprot.org/annotation/VSP_041534|||http://purl.uniprot.org/annotation/VSP_041535|||http://purl.uniprot.org/annotation/VSP_041536|||http://purl.uniprot.org/annotation/VSP_041537|||http://purl.uniprot.org/annotation/VSP_041538|||http://purl.uniprot.org/annotation/VSP_041539|||http://purl.uniprot.org/annotation/VSP_041540|||http://purl.uniprot.org/annotation/VSP_058835|||http://purl.uniprot.org/annotation/VSP_058836
http://togogenome.org/gene/9606:ZNF121                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58317                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 121                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047408
http://togogenome.org/gene/9606:C14orf132                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GU51|||http://purl.uniprot.org/uniprot/A0A1B0GWH2|||http://purl.uniprot.org/uniprot/Q9NPU4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Uncharacterized protein C14orf132                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089934
http://togogenome.org/gene/9606:SSTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30872|||http://purl.uniprot.org/uniprot/Q86SW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine|||Somatostatin receptor type 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070116
http://togogenome.org/gene/9606:LHFPL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y693                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LHFPL tetraspan subfamily member 6 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244756
http://togogenome.org/gene/9606:CLDN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384ME58|||http://purl.uniprot.org/uniprot/F5H496|||http://purl.uniprot.org/uniprot/O95471                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin|||Claudin-7|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interactions with TJP1, TJP2 and TJP3|||Interacts with CD81, and exhibits HCV infection susceptibility in cell culture.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144750|||http://purl.uniprot.org/annotation/PRO_5003327256|||http://purl.uniprot.org/annotation/PRO_5017347812|||http://purl.uniprot.org/annotation/VAR_014538|||http://purl.uniprot.org/annotation/VAR_030736|||http://purl.uniprot.org/annotation/VSP_013230
http://togogenome.org/gene/9606:GIMAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8P9|||http://purl.uniprot.org/uniprot/Q96F15                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AIG1-type G|||Cytoplasmic|||Disordered|||GTPase IMAP family member 5|||Helical|||Helical; Anchor for type IV membrane protein|||In NCPH2; unknown pathological significance.|||In NCPH2; unknown pathological significance; strong decrease in protein level.|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190990|||http://purl.uniprot.org/annotation/VAR_081683|||http://purl.uniprot.org/annotation/VAR_086141|||http://purl.uniprot.org/annotation/VAR_086142|||http://purl.uniprot.org/annotation/VAR_086143|||http://purl.uniprot.org/annotation/VSP_008961
http://togogenome.org/gene/9606:HEATR5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2D3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||HEAT repeat-containing protein 5B|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311994|||http://purl.uniprot.org/annotation/VAR_037392|||http://purl.uniprot.org/annotation/VSP_029690|||http://purl.uniprot.org/annotation/VSP_029691|||http://purl.uniprot.org/annotation/VSP_029692
http://togogenome.org/gene/9606:ZRANB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GYN7|||http://purl.uniprot.org/uniprot/Q5FWF4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) S-methylcysteine|||APIM motif|||Abolishes ATPase activity. Abolishes endonuclease activity; when associated with A-1021.|||Abolishes fork regression activity.|||Abolishes interaction with 'Lys-63'-linked polyubiquitin.|||Abolishes interaction with PCNA; when associated with A-519.|||Abolishes interaction with PCNA; when associated with A-519; 525-A-A-526 and A-1075.|||Abolishes interaction with PCNA; when associated with A-519; A-522 and 525-A-A-526.|||Abolishes interaction with PCNA; when associated with A-519; A-522 and A-1075.|||Abolishes interaction with PCNA; when associated with A-522; 525-A-A-526 and A-1075. Abolishes interaction with PCNA; when associated with A-525.|||DEAH box|||DNA annealing helicase activity|||DNA annealing helicase and endonuclease ZRANB3|||Disordered|||Does not affect endonuclease. Abolishes endonuclease activity; when associated with R-65.|||Endonuclease activity|||HNH|||Helicase ATP-binding|||Helicase C-terminal|||Impaired interaction with 'Lys-63'-linked polyubiquitin.|||Impaired interaction with polyubiquitin.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Loss of DNA-binding, DNA-dependent ATPase and nuclease activities.|||Loss of DNA-dependent ATPase activity.|||PIP-box|||Phosphoserine|||RanBP2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278182|||http://purl.uniprot.org/annotation/VAR_030671|||http://purl.uniprot.org/annotation/VAR_030672|||http://purl.uniprot.org/annotation/VAR_061237|||http://purl.uniprot.org/annotation/VSP_023138|||http://purl.uniprot.org/annotation/VSP_023139|||http://purl.uniprot.org/annotation/VSP_023140|||http://purl.uniprot.org/annotation/VSP_044175|||http://purl.uniprot.org/annotation/VSP_044176|||http://purl.uniprot.org/annotation/VSP_044177|||http://purl.uniprot.org/annotation/VSP_044178
http://togogenome.org/gene/9606:GLB1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJK0|||http://purl.uniprot.org/uniprot/B4DTH1|||http://purl.uniprot.org/uniprot/Q6UWU2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Beta-galactosidase-1-like protein|||Glycoside hydrolase 35 catalytic|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313604|||http://purl.uniprot.org/annotation/PRO_5002803849|||http://purl.uniprot.org/annotation/PRO_5007491837|||http://purl.uniprot.org/annotation/VSP_030059
http://togogenome.org/gene/9606:SLC25A19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JPC1|||http://purl.uniprot.org/uniprot/Q9HC21                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Decreases thiamine pyrophosphate transmembrane transporter activity.|||Decreases thiamine pyrophosphate transmembrane transporter activity. Does not affect protein expression.|||Does not affect thiamine pyrophosphate transmembrane transporter activity.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In MCPHA; diminishes thiamine pyrophosphate transmembrane transporter activity by 70%.|||In THMD4; affects function as shown by complementation studies in yeast.|||In THMD4; reduced protein expression.|||In isoform 2.|||Mitochondrial thiamine pyrophosphate carrier|||Phosphoserine|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3|||Substrate recognition                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090611|||http://purl.uniprot.org/annotation/VAR_014103|||http://purl.uniprot.org/annotation/VAR_065125|||http://purl.uniprot.org/annotation/VAR_087311|||http://purl.uniprot.org/annotation/VSP_053908
http://togogenome.org/gene/9606:MGAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2H8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Glucoamylase|||Helical|||In isoform 2.|||Lumenal|||Maltase|||N-linked (GlcNAc...) asparagine|||Nucleophile|||P-type 1|||P-type 2|||Probable maltase-glucoamylase 2|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341380|||http://purl.uniprot.org/annotation/VSP_055415|||http://purl.uniprot.org/annotation/VSP_055416
http://togogenome.org/gene/9606:TMCO6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DC7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane and coiled-coil domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305157|||http://purl.uniprot.org/annotation/VAR_035171|||http://purl.uniprot.org/annotation/VSP_028249
http://togogenome.org/gene/9606:AADAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22760                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glycosylation at this site and causes moderate decrease in activity.|||Abolishes glycosylation at this site and causes substantial decrease in activity and reduced substrate affinity.|||Arylacetamide deacetylase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In allele AADAC*3; decreased enzyme activity.|||In alleles AADAC*2 and AADAC*3; mildly decreased enzyme activity.|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071542|||http://purl.uniprot.org/annotation/VAR_014798|||http://purl.uniprot.org/annotation/VAR_070543
http://togogenome.org/gene/9606:RPL7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62424                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein eL8|||N6-acetyllysine|||N6-acetyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136747
http://togogenome.org/gene/9606:ELL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55199|||http://purl.uniprot.org/uniprot/U3KQ90                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Disordered|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient)|||N-acetylalanine|||Nuclear localization signal|||OCEL|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA polymerase II elongation factor ELL|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146733|||http://purl.uniprot.org/annotation/VAR_053072|||http://purl.uniprot.org/annotation/VAR_053073
http://togogenome.org/gene/9606:GTF3C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12789                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||General transcription factor 3C polypeptide 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209710|||http://purl.uniprot.org/annotation/VAR_047534|||http://purl.uniprot.org/annotation/VAR_047535|||http://purl.uniprot.org/annotation/VAR_047536|||http://purl.uniprot.org/annotation/VSP_021819
http://togogenome.org/gene/9606:CYREN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWK5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with XRCC5/Ku80 and XRCC6/Ku70 and ability to inhibit classical non-homologous end joining (NHEJ).|||Cell cycle regulator of non-homologous end joining|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KBM|||N-acetylmethionine|||Polar residues|||XLM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320948|||http://purl.uniprot.org/annotation/VAR_039320|||http://purl.uniprot.org/annotation/VSP_031767|||http://purl.uniprot.org/annotation/VSP_031768|||http://purl.uniprot.org/annotation/VSP_058524|||http://purl.uniprot.org/annotation/VSP_058525
http://togogenome.org/gene/9606:TYRO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YNK6|||http://purl.uniprot.org/uniprot/Q06418                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes dimerization.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor TYRO3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024478|||http://purl.uniprot.org/annotation/VAR_041876|||http://purl.uniprot.org/annotation/VAR_045886|||http://purl.uniprot.org/annotation/VAR_045887|||http://purl.uniprot.org/annotation/VAR_045888|||http://purl.uniprot.org/annotation/VAR_045889|||http://purl.uniprot.org/annotation/VAR_045890|||http://purl.uniprot.org/annotation/VAR_045891
http://togogenome.org/gene/9606:OMG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23515                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRNT|||N-linked (GlcNAc...) asparagine|||Oligodendrocyte-myelin glycoprotein|||Removed in mature form|||Ser/Thr-rich                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021888|||http://purl.uniprot.org/annotation/PRO_0000021889|||http://purl.uniprot.org/annotation/VAR_051252|||http://purl.uniprot.org/annotation/VAR_051253
http://togogenome.org/gene/9606:APOM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95445                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Apolipoprotein M|||In isoform 2.|||Introduces a signal cleavage site. Abolishes interaction with lipoprotein particles. Leads to rapid elimination from plasma.|||Loss of glycosylation.|||N-linked (GlcNAc...) asparagine|||No loss of glycosylation.|||Not cleaved                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223278|||http://purl.uniprot.org/annotation/VSP_045586
http://togogenome.org/gene/9606:COL4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01955                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  7S domain|||Cell attachment site|||Cleavage; by collagenase|||Collagen IV NC1|||Collagen alpha-3(IV) chain|||Disordered|||Epitope recognized by Goodpasture antibodies|||In ATS2.|||In ATS2; in isolated microhematuria at heterozygosity.|||In ATS2; unknown pathological significance.|||In ATS3; in isolated microhematuria at heterozygosity.|||In BFH2.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Or C-1460 with C-1548|||Or C-1493 with C-1551|||Or C-1570 with C-1662|||Or C-1604 with C-1665|||Pro residues|||Required for the anti-angiogenic activity of tumstatin|||Required for the anti-tumor cell activity of tumstatin|||S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)|||S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)|||Triple-helical region|||Tumstatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005844|||http://purl.uniprot.org/annotation/PRO_0000279684|||http://purl.uniprot.org/annotation/VAR_001908|||http://purl.uniprot.org/annotation/VAR_001909|||http://purl.uniprot.org/annotation/VAR_011202|||http://purl.uniprot.org/annotation/VAR_011203|||http://purl.uniprot.org/annotation/VAR_011204|||http://purl.uniprot.org/annotation/VAR_011205|||http://purl.uniprot.org/annotation/VAR_011206|||http://purl.uniprot.org/annotation/VAR_011207|||http://purl.uniprot.org/annotation/VAR_011208|||http://purl.uniprot.org/annotation/VAR_011209|||http://purl.uniprot.org/annotation/VAR_011210|||http://purl.uniprot.org/annotation/VAR_011211|||http://purl.uniprot.org/annotation/VAR_011212|||http://purl.uniprot.org/annotation/VAR_011213|||http://purl.uniprot.org/annotation/VAR_011214|||http://purl.uniprot.org/annotation/VAR_011215|||http://purl.uniprot.org/annotation/VAR_011216|||http://purl.uniprot.org/annotation/VAR_011217|||http://purl.uniprot.org/annotation/VAR_011218|||http://purl.uniprot.org/annotation/VAR_011219|||http://purl.uniprot.org/annotation/VAR_030944|||http://purl.uniprot.org/annotation/VAR_030945|||http://purl.uniprot.org/annotation/VAR_030946|||http://purl.uniprot.org/annotation/VAR_030947|||http://purl.uniprot.org/annotation/VAR_030948|||http://purl.uniprot.org/annotation/VAR_030949|||http://purl.uniprot.org/annotation/VAR_030950|||http://purl.uniprot.org/annotation/VAR_061118|||http://purl.uniprot.org/annotation/VAR_080826|||http://purl.uniprot.org/annotation/VSP_001170|||http://purl.uniprot.org/annotation/VSP_001171|||http://purl.uniprot.org/annotation/VSP_023498|||http://purl.uniprot.org/annotation/VSP_023499|||http://purl.uniprot.org/annotation/VSP_023500
http://togogenome.org/gene/9606:NHLH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02577                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with features of hypogonadotropic hypogonadism and Kabuki syndrome also carrying a KMT2D variant; unknown pathological significance; reduced transactivation activity on KISS1 promoter; requires 2 nucleotide substitutions.|||Helix-loop-helix protein 2|||In HH27; the patient also carries KISS1 and PROKR2 variants; unknown pathological significance.|||In HH27; unknown pathological significance; severely reduced binding to MC4R promoter; reduced transactivation activity on KISS1 promoter.|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127199|||http://purl.uniprot.org/annotation/VAR_086934|||http://purl.uniprot.org/annotation/VAR_086935|||http://purl.uniprot.org/annotation/VAR_086936
http://togogenome.org/gene/9606:CDCA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FF9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Alters interaction with PDS5A and PDS5B and the cohesin complex.|||Basic and acidic residues|||Disordered|||FGF motif|||KEN box|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sororin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089449|||http://purl.uniprot.org/annotation/VAR_050777
http://togogenome.org/gene/9606:IMPDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N6C2|||http://purl.uniprot.org/uniprot/P12268                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CBS|||CBS 1|||CBS 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Inosine-5'-monophosphate dehydrogenase 2|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Removed|||Results in 10-fold decrease of enzymatic activity.|||Thioimidate intermediate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093673|||http://purl.uniprot.org/annotation/VAR_070542
http://togogenome.org/gene/9606:RNF207                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRF8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Associated with prolonged QT interval in heart's electrical cycle; behaves like wild-type in terms of protein expression, subcellular location and shortening of heart's action potential duration, when expressed in neonatal rabbit cardiomyocytes.|||B box-type; atypical|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of KCNH2 up-regulation.|||Polar residues|||RING finger protein 207|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300809|||http://purl.uniprot.org/annotation/VAR_052112|||http://purl.uniprot.org/annotation/VAR_052113|||http://purl.uniprot.org/annotation/VAR_052114|||http://purl.uniprot.org/annotation/VAR_061818|||http://purl.uniprot.org/annotation/VSP_027863|||http://purl.uniprot.org/annotation/VSP_027864|||http://purl.uniprot.org/annotation/VSP_028439|||http://purl.uniprot.org/annotation/VSP_028440|||http://purl.uniprot.org/annotation/VSP_028441|||http://purl.uniprot.org/annotation/VSP_028442|||http://purl.uniprot.org/annotation/VSP_028443
http://togogenome.org/gene/9606:SGK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z325|||http://purl.uniprot.org/uniprot/E9PR89|||http://purl.uniprot.org/uniprot/O00141                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  10-fold activation.|||AGC-kinase C-terminal|||Abolishes enzymatic activity.|||Abolishes interaction with NEDD4 and NEDD4L.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interchain (with C-193)|||Interchain (with C-258)|||Low activity.|||Necessary for localization to the mitochondria|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAPK7|||Phosphothreonine; by PDPK1|||Phosphothreonine; by PKA|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Sgk1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086642|||http://purl.uniprot.org/annotation/VAR_041071|||http://purl.uniprot.org/annotation/VAR_041072|||http://purl.uniprot.org/annotation/VSP_037784|||http://purl.uniprot.org/annotation/VSP_037785|||http://purl.uniprot.org/annotation/VSP_037786|||http://purl.uniprot.org/annotation/VSP_037787
http://togogenome.org/gene/9606:PDZD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y892|||http://purl.uniprot.org/uniprot/A0A2R8YFN1|||http://purl.uniprot.org/uniprot/Q9H5P4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In DFNB57.|||In DFNB57; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ domain-containing protein 7|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058297|||http://purl.uniprot.org/annotation/VAR_080820|||http://purl.uniprot.org/annotation/VAR_080821|||http://purl.uniprot.org/annotation/VAR_080822|||http://purl.uniprot.org/annotation/VAR_080823|||http://purl.uniprot.org/annotation/VAR_080824|||http://purl.uniprot.org/annotation/VAR_081066|||http://purl.uniprot.org/annotation/VAR_081067|||http://purl.uniprot.org/annotation/VSP_059941|||http://purl.uniprot.org/annotation/VSP_059942|||http://purl.uniprot.org/annotation/VSP_059943
http://togogenome.org/gene/9606:ZNF865                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CJ78                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Pro residues|||Zinc finger protein 865                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000404594
http://togogenome.org/gene/9606:SPOUT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T280                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Putative methyltransferase C9orf114                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238468|||http://purl.uniprot.org/annotation/VAR_026552|||http://purl.uniprot.org/annotation/VAR_026553|||http://purl.uniprot.org/annotation/VAR_050844
http://togogenome.org/gene/9606:SNAI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KNW1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||SNAG domain|||Zinc finger protein SNAI3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330037
http://togogenome.org/gene/9606:CIB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q77                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcium and integrin-binding family member 3|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073536|||http://purl.uniprot.org/annotation/VAR_060268|||http://purl.uniprot.org/annotation/VSP_055509
http://togogenome.org/gene/9606:TNFSF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5J8I0|||http://purl.uniprot.org/uniprot/P41273                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||TNF family profile|||Tumor necrosis factor ligand superfamily member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185501|||http://purl.uniprot.org/annotation/VAR_011928
http://togogenome.org/gene/9606:ELAVL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15717                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by CARM1; alternate|||Decreases phosphorylation by PRKCD.|||Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-221.|||Decreases phosphorylation by PRKCD. Nearly abolishes phosphorylation by PRKCD and translocation from the nucleus into the cytoplasm; when associated with A-318.|||ELAV-like protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylserine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||RRM 1|||RRM 2|||RRM 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081577|||http://purl.uniprot.org/annotation/VSP_056148
http://togogenome.org/gene/9606:CALU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQF5|||http://purl.uniprot.org/uniprot/O43852|||http://purl.uniprot.org/uniprot/Q6IAW5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Calumenin|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13 and isoform 14.|||In isoform 15.|||In isoform 2, isoform 4, isoform 7 and isoform 8.|||In isoform 3, isoform 4 and isoform 14.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) (complex) asparagine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphotyrosine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004153|||http://purl.uniprot.org/annotation/PRO_5002788425|||http://purl.uniprot.org/annotation/PRO_5014310476|||http://purl.uniprot.org/annotation/VAR_022051|||http://purl.uniprot.org/annotation/VSP_007317|||http://purl.uniprot.org/annotation/VSP_043570|||http://purl.uniprot.org/annotation/VSP_045939|||http://purl.uniprot.org/annotation/VSP_045940|||http://purl.uniprot.org/annotation/VSP_045941|||http://purl.uniprot.org/annotation/VSP_045942|||http://purl.uniprot.org/annotation/VSP_045943|||http://purl.uniprot.org/annotation/VSP_045944|||http://purl.uniprot.org/annotation/VSP_045945|||http://purl.uniprot.org/annotation/VSP_045946|||http://purl.uniprot.org/annotation/VSP_045947|||http://purl.uniprot.org/annotation/VSP_045948|||http://purl.uniprot.org/annotation/VSP_045949|||http://purl.uniprot.org/annotation/VSP_045950|||http://purl.uniprot.org/annotation/VSP_045951
http://togogenome.org/gene/9606:MAP2K6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3Y2|||http://purl.uniprot.org/uniprot/P52564                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-acetylserine; by Yersinia YopJ; alternate|||(Microbial infection) O-acetylthreonine; by Yersinia YopJ; alternate|||Cleavage; by anthrax lethal factor|||Constitutive activation according to PubMed:8622669, but not to PubMed:8621675.|||D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 6|||In isoform 2.|||Inactivation.|||Phosphoserine; by MAP3K; alternate|||Phosphothreonine; by MAP3K; alternate|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086386|||http://purl.uniprot.org/annotation/VSP_004882
http://togogenome.org/gene/9606:RPS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62081                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylmethionine|||N6-acetyllysine; alternate|||Small ribosomal subunit protein eS7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174190
http://togogenome.org/gene/9606:MSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21757                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Collagen-like|||Cytoplasmic|||Disordered|||Extracellular|||Found in a family with prostate cancer.|||Found in patients with Barrett esophagus.|||Found in patients with prostate cancer.|||Helical; Signal-anchor for type II membrane protein|||In isoform II.|||In isoform III.|||Macrophage scavenger receptor types I and II|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||SRCR|||Spacer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181627|||http://purl.uniprot.org/annotation/VAR_025190|||http://purl.uniprot.org/annotation/VAR_025191|||http://purl.uniprot.org/annotation/VAR_052061|||http://purl.uniprot.org/annotation/VAR_066581|||http://purl.uniprot.org/annotation/VAR_066582|||http://purl.uniprot.org/annotation/VAR_066583|||http://purl.uniprot.org/annotation/VAR_066584|||http://purl.uniprot.org/annotation/VAR_066585|||http://purl.uniprot.org/annotation/VAR_066586|||http://purl.uniprot.org/annotation/VAR_066587|||http://purl.uniprot.org/annotation/VSP_006229|||http://purl.uniprot.org/annotation/VSP_006230|||http://purl.uniprot.org/annotation/VSP_036842
http://togogenome.org/gene/9606:USP6NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92738                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of GAP activity on RAB5A.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Rab-GAP TBC|||USP6 N-terminal-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208056|||http://purl.uniprot.org/annotation/VSP_040850
http://togogenome.org/gene/9606:PATZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBE1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||BTB|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||POZ-, AT hook-, and zinc finger-containing protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047504|||http://purl.uniprot.org/annotation/VAR_052724|||http://purl.uniprot.org/annotation/VSP_008799|||http://purl.uniprot.org/annotation/VSP_008800|||http://purl.uniprot.org/annotation/VSP_008801|||http://purl.uniprot.org/annotation/VSP_008802
http://togogenome.org/gene/9606:PRODH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UF12                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Hydroxyproline dehydrogenase|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308623|||http://purl.uniprot.org/annotation/VAR_036852|||http://purl.uniprot.org/annotation/VAR_036853
http://togogenome.org/gene/9606:FOXE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00358                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein E1|||In BAMLAZ; loss of sequence-specific DNA binding; loss of transcriptional activity.|||In BAMLAZ; no effect on protein abundance; no effect on sequence-specific DNA binding; enhances transcriptional activity toward TG and TPO genes.|||In BAMLAZ; without choanal atresia; no effect on protein abundance; no effect on localization to the nucleus; decreased sequence-specific DNA binding; decreased transcriptional activity.|||In NMTC4; increased cell growth; increased cell migration; associated with increased expression of the WNT5A gene.|||In congenital hypothyroidism; loss of sequence-specific DNA binding; loss of transcriptional activity.|||In congenital hypothyroidism; slightly decreased sequence-specific DNA binding to the TPO promoter; 0.5 fold decreased transcriptional activity.|||In congenital hypothyroidism; with absence of thyroid agenesis; loss of sequence-specific DNA binding; loss of transcriptional activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091826|||http://purl.uniprot.org/annotation/VAR_008857|||http://purl.uniprot.org/annotation/VAR_016882|||http://purl.uniprot.org/annotation/VAR_027508|||http://purl.uniprot.org/annotation/VAR_037643|||http://purl.uniprot.org/annotation/VAR_075978|||http://purl.uniprot.org/annotation/VAR_075979|||http://purl.uniprot.org/annotation/VAR_075980|||http://purl.uniprot.org/annotation/VAR_075981
http://togogenome.org/gene/9606:MYL6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14649                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin light chain 6B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198695
http://togogenome.org/gene/9606:ZC3H7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWR0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||In isoform 2.|||Phosphothreonine|||TPR 1|||TPR 2|||TPR 3|||Zinc finger CCCH domain-containing protein 7A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106321|||http://purl.uniprot.org/annotation/VAR_052632|||http://purl.uniprot.org/annotation/VAR_052633|||http://purl.uniprot.org/annotation/VSP_014383
http://togogenome.org/gene/9606:IGSF21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ID5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Ig-like 1|||Ig-like 2|||Immunoglobulin superfamily member 21|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223338|||http://purl.uniprot.org/annotation/VAR_035518|||http://purl.uniprot.org/annotation/VAR_056049|||http://purl.uniprot.org/annotation/VAR_056050
http://togogenome.org/gene/9606:VCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55072                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NPLOC4; when associated with 52-A--A-55.|||Abolishes interaction with NPLOC4; when associated with A-110.|||Abolishes methylation by VCPKMT.|||Defect in ubiquitin-dependent protein degradation by the proteasome; when associated with Q-578.|||Disordered|||Does not affect methylation by VCPKMT.|||Does not inhibit interaction with RHBDD1. Increased interaction with CAV1 and UBXN6. Impaired autophagic function. Defect in ubiquitin-dependent protein degradation by the proteasome; when associated with Q-305. Increases interaction with ZFAND1 in an arsenite-dependent manner.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs ERAD degradation of HMGCR and does not inhibit interaction with RHBDD1; when associated with Q-524.|||Impairs ERAD degradation of HMGCR; when associated with Q-251.|||Impairs catalytic activity of RNF19A toward SOD1 mutant. Does not inhibit interaction with RHBDD1; when associated with A-251.|||In CMT2Y; increased ATPase activity.|||In CMT2Y; normal ATPase activity; impaired autophagic function.|||In FTDALS6 and IBMPFD1; abolishes enhancement of K-315 methylation by ASPSCR1.|||In FTDALS6 and IBMPFD1; properly assembles into a hexameric structure; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP; shows normal ATPase activity according to PubMed:16321991 while according to PubMed:25878907 and PubMed:25125609 shows increased ATPase activity; no defect in ubiquitin-dependent protein degradation by the proteasome; impaired autophagic function; defective maturation of ubiquitin-containing autophagosomes; decreased interaction with CAV1 and UBXN6; decreased endosome to lysosome transport via multivesicular body sorting pathway of CAV1; decreases the arsenite-induced stress granules (SGs) clearance process.|||In FTDALS6.|||In IBMPFD1.|||In IBMPFD1; also in one patient without evidence of Paget disease of the bone.|||In IBMPFD1; cultured cells expressing the mutant protein show a marked general increase in the level of ubiquitin-conjugated proteins and impaired protein degradation through the endoplasmic reticulum-associated degradation (ERAD) pathway; shows strongly reduced affinity for ADP and increased affinity for ATP; abolishes enhancement of K-315 methylation by ASPSCR1; decreased interaction with CAV1 and UBXN6.|||In IBMPFD1; impaired autophagic function.|||In IBMPFD1; increased ATPase activity; impaired autophagic function.|||In IBMPFD1; increased ATPase activity; no defect in ubiquitin-dependent protein degradation by the proteasome; impaired autophagic function; defect in maturation of ubiquitin-containing autophagosomes; decreased interaction with CAV1 and UBXN6.|||In IBMPFD1; unknown pathological significance.|||In IBMPFD1; without frontotemporal dementia; abolishes enhancement of K-315 methylation by ASPSCR1.|||Interaction with UBXN6|||Minor effect on affinity for ATP and ADP.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by VCPKMT|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No effect on binding to DERL1.|||PIM motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Severely reduced binding to DERL1.|||Strongly impairs methylation by VCPKMT.|||Strongly increased affinity for ATP. Strongly reduced affinity for ADP.|||Transitional endoplasmic reticulum ATPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084572|||http://purl.uniprot.org/annotation/VAR_033016|||http://purl.uniprot.org/annotation/VAR_033017|||http://purl.uniprot.org/annotation/VAR_033018|||http://purl.uniprot.org/annotation/VAR_033019|||http://purl.uniprot.org/annotation/VAR_033020|||http://purl.uniprot.org/annotation/VAR_033021|||http://purl.uniprot.org/annotation/VAR_033022|||http://purl.uniprot.org/annotation/VAR_065910|||http://purl.uniprot.org/annotation/VAR_065911|||http://purl.uniprot.org/annotation/VAR_076464|||http://purl.uniprot.org/annotation/VAR_076465|||http://purl.uniprot.org/annotation/VAR_076466|||http://purl.uniprot.org/annotation/VAR_076467|||http://purl.uniprot.org/annotation/VAR_076468|||http://purl.uniprot.org/annotation/VAR_078910|||http://purl.uniprot.org/annotation/VAR_078911|||http://purl.uniprot.org/annotation/VAR_088265|||http://purl.uniprot.org/annotation/VAR_088266|||http://purl.uniprot.org/annotation/VAR_088267
http://togogenome.org/gene/9606:WDR26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7D7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CTLH|||Disordered|||In SKDEAS.|||In SKDEAS; unknown pathological significance.|||In SKDEAS; unknown pathological significance; slightly decreased protein expression;.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LisH|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051373|||http://purl.uniprot.org/annotation/VAR_079297|||http://purl.uniprot.org/annotation/VAR_079298|||http://purl.uniprot.org/annotation/VAR_079299|||http://purl.uniprot.org/annotation/VAR_079300|||http://purl.uniprot.org/annotation/VAR_079301|||http://purl.uniprot.org/annotation/VAR_079302|||http://purl.uniprot.org/annotation/VAR_079303|||http://purl.uniprot.org/annotation/VAR_079304|||http://purl.uniprot.org/annotation/VAR_079305|||http://purl.uniprot.org/annotation/VSP_023895|||http://purl.uniprot.org/annotation/VSP_023896|||http://purl.uniprot.org/annotation/VSP_023897|||http://purl.uniprot.org/annotation/VSP_023898|||http://purl.uniprot.org/annotation/VSP_023899
http://togogenome.org/gene/9606:ATP23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6H3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  Mitochondrial inner membrane protease ATP23 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330344|||http://purl.uniprot.org/annotation/VAR_054489
http://togogenome.org/gene/9606:SLTM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWH9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RRM|||Removed|||SAFB-like transcription modulator|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307798|||http://purl.uniprot.org/annotation/VAR_037088|||http://purl.uniprot.org/annotation/VSP_056051
http://togogenome.org/gene/9606:CEACAM19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z692                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carcinoembryonic antigen-related cell adhesion molecule 19|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014576|||http://purl.uniprot.org/annotation/VSP_010708|||http://purl.uniprot.org/annotation/VSP_010709|||http://purl.uniprot.org/annotation/VSP_043228
http://togogenome.org/gene/9606:ADCY7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSJ0|||http://purl.uniprot.org/uniprot/F5H4D1|||http://purl.uniprot.org/uniprot/P51828|||http://purl.uniprot.org/uniprot/Q86YI0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 7|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect cAMP biosynthetic process in response to C5 alpha chain stimulation. Reduces by 40?60% cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation.|||Does not affect cAMP biosynthetic process in response to sphingosine 1-phosphate stimulation. Reduces by 40% cAMP biosynthetic process in response to C5 alpha chain stimulation.|||Guanylate cyclase|||Guanylate cyclase 1|||Guanylate cyclase 2|||Helical|||Mediates regulation of adenylate cyclase activity by C5 alpha-induced G- beta and gamma pathway|||Mediates regulation of adenylate cyclase activity by sphingosine 1-phosphate-induced G alpha 13 pathway|||Modulates adenylate cyclase activity by modulating the binding of G(s)alpha to the high-affinity G(s)alpha binding site in 7C1a/7C2|||N-linked (GlcNAc...) asparagine|||Reduces cAMP biosynthetic process in response to C5 alpha chain stimulation and more severely in response to sphingosine 1-phosphate stimulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195703
http://togogenome.org/gene/9606:HSF2BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75031|||http://purl.uniprot.org/uniprot/Q6IAT7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with BRCA2.|||Heat shock factor 2-binding protein|||In POF19; in mice this mutation leads to a decreased protein stability with reduced fertility due to a lower frequency of crossovers in meiocytes.|||In isoform 2.|||Interaction with BRCA2|||Interaction with BRME1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084077|||http://purl.uniprot.org/annotation/VAR_084602|||http://purl.uniprot.org/annotation/VSP_054158
http://togogenome.org/gene/9606:ATG4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEA4|||http://purl.uniprot.org/uniprot/Q8WYN0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine protease ATG4A|||Decreased ability to mediate proteolytic activation and delipidation of ATG8 proteins.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LIR|||Nucleophile|||Peptidase C54 catalytic|||Phospho-mimetic mutant; slightly increased delipidation of ATG8 proteins.|||Reduces the redox sensitivity and retains activity in presence of H(2)O(2).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215838|||http://purl.uniprot.org/annotation/VSP_013025|||http://purl.uniprot.org/annotation/VSP_025902|||http://purl.uniprot.org/annotation/VSP_030499
http://togogenome.org/gene/9606:YY1AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQQ0|||http://purl.uniprot.org/uniprot/I6L9C2|||http://purl.uniprot.org/uniprot/Q9H869                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In GRNG.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3, isoform 5 and isoform 9.|||In isoform 3 and isoform 6.|||In isoform 5.|||In isoform 7.|||In isoform 8 and isoform 9.|||Phosphoserine|||YY1-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076369|||http://purl.uniprot.org/annotation/VAR_051497|||http://purl.uniprot.org/annotation/VAR_051498|||http://purl.uniprot.org/annotation/VAR_078760|||http://purl.uniprot.org/annotation/VAR_078761|||http://purl.uniprot.org/annotation/VAR_078762|||http://purl.uniprot.org/annotation/VAR_078763|||http://purl.uniprot.org/annotation/VSP_016585|||http://purl.uniprot.org/annotation/VSP_016586|||http://purl.uniprot.org/annotation/VSP_016587|||http://purl.uniprot.org/annotation/VSP_016588|||http://purl.uniprot.org/annotation/VSP_016589|||http://purl.uniprot.org/annotation/VSP_046858
http://togogenome.org/gene/9606:FLG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5D862                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Filaggrin 1|||Filaggrin 10|||Filaggrin 2|||Filaggrin 3|||Filaggrin 4|||Filaggrin 5|||Filaggrin 6|||Filaggrin 7|||Filaggrin 8|||Filaggrin 9|||Filaggrin-2|||In PSS6; reduced protein abundance in patient's skin.|||Phosphoserine|||Polar residues|||S-100-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331454|||http://purl.uniprot.org/annotation/VAR_042868|||http://purl.uniprot.org/annotation/VAR_042869|||http://purl.uniprot.org/annotation/VAR_042870|||http://purl.uniprot.org/annotation/VAR_042871|||http://purl.uniprot.org/annotation/VAR_042872|||http://purl.uniprot.org/annotation/VAR_042873|||http://purl.uniprot.org/annotation/VAR_042874|||http://purl.uniprot.org/annotation/VAR_042875|||http://purl.uniprot.org/annotation/VAR_042876|||http://purl.uniprot.org/annotation/VAR_042877|||http://purl.uniprot.org/annotation/VAR_059173|||http://purl.uniprot.org/annotation/VAR_081283|||http://purl.uniprot.org/annotation/VAR_081284|||http://purl.uniprot.org/annotation/VAR_085409|||http://purl.uniprot.org/annotation/VAR_085410
http://togogenome.org/gene/9606:KCNJ4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48050|||http://purl.uniprot.org/uniprot/Q58F07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||INTRAMEM|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Inward rectifier potassium channel 4|||Inward rectifier potassium channel C-terminal|||Loss of pH-sensitivity.|||PDZ-binding|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter|||Val/Gly/Ala/Pro stretch                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154930
http://togogenome.org/gene/9606:ZNF558                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NG5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 558                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047648|||http://purl.uniprot.org/annotation/VSP_055963
http://togogenome.org/gene/9606:CAMKK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RR4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Basic and acidic residues|||Calcium/calmodulin-dependent protein kinase kinase 2|||Calmodulin-binding|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2 and isoform 6.|||In isoform 2, isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 7.|||N-acetylserine|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||RP domain|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086144|||http://purl.uniprot.org/annotation/VAR_020532|||http://purl.uniprot.org/annotation/VAR_020533|||http://purl.uniprot.org/annotation/VAR_032788|||http://purl.uniprot.org/annotation/VAR_040610|||http://purl.uniprot.org/annotation/VAR_040611|||http://purl.uniprot.org/annotation/VAR_040612|||http://purl.uniprot.org/annotation/VAR_040613|||http://purl.uniprot.org/annotation/VSP_012142|||http://purl.uniprot.org/annotation/VSP_012143|||http://purl.uniprot.org/annotation/VSP_012144|||http://purl.uniprot.org/annotation/VSP_012145|||http://purl.uniprot.org/annotation/VSP_012146|||http://purl.uniprot.org/annotation/VSP_012147|||http://purl.uniprot.org/annotation/VSP_012148|||http://purl.uniprot.org/annotation/VSP_012149
http://togogenome.org/gene/9606:LY75-CD302                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60449                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin 1|||C-type lectin 10|||C-type lectin 2|||C-type lectin 3|||C-type lectin 4|||C-type lectin 5|||C-type lectin 6|||C-type lectin 7|||C-type lectin 8|||C-type lectin 9|||Cytoplasmic|||Extracellular|||Fibronectin type-II|||Helical|||In isoform 2.|||In isoform 3.|||Lymphocyte antigen 75|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017552|||http://purl.uniprot.org/annotation/VAR_024522|||http://purl.uniprot.org/annotation/VAR_027824|||http://purl.uniprot.org/annotation/VAR_027825|||http://purl.uniprot.org/annotation/VAR_027826|||http://purl.uniprot.org/annotation/VAR_027827|||http://purl.uniprot.org/annotation/VAR_027828|||http://purl.uniprot.org/annotation/VAR_027829|||http://purl.uniprot.org/annotation/VAR_027830|||http://purl.uniprot.org/annotation/VAR_027831|||http://purl.uniprot.org/annotation/VAR_056156|||http://purl.uniprot.org/annotation/VAR_056157|||http://purl.uniprot.org/annotation/VAR_056158|||http://purl.uniprot.org/annotation/VSP_020908|||http://purl.uniprot.org/annotation/VSP_020909
http://togogenome.org/gene/9606:RPS25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62851                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Small ribosomal subunit protein eS25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192869
http://togogenome.org/gene/9606:KLF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13887|||http://purl.uniprot.org/uniprot/Q5T6X2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs ubiquitination and degradation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with WWP1|||Krueppel-like factor 5|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047169|||http://purl.uniprot.org/annotation/VAR_035555|||http://purl.uniprot.org/annotation/VSP_047474|||http://purl.uniprot.org/annotation/VSP_047475|||http://purl.uniprot.org/annotation/VSP_047476|||http://purl.uniprot.org/annotation/VSP_057567
http://togogenome.org/gene/9606:MYORG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSJ0                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Does not change nuclear membrane localization. Does not rescue the myogenetic defect induced by depletion of endogenous MYORG.|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In IBGC7.|||In IBGC7; unknown pathological significance.|||Myogenesis-regulating glycosidase|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295752|||http://purl.uniprot.org/annotation/VAR_033359|||http://purl.uniprot.org/annotation/VAR_033360|||http://purl.uniprot.org/annotation/VAR_033361|||http://purl.uniprot.org/annotation/VAR_033362|||http://purl.uniprot.org/annotation/VAR_081940|||http://purl.uniprot.org/annotation/VAR_081941|||http://purl.uniprot.org/annotation/VAR_081942|||http://purl.uniprot.org/annotation/VAR_081943|||http://purl.uniprot.org/annotation/VAR_081944|||http://purl.uniprot.org/annotation/VAR_081945|||http://purl.uniprot.org/annotation/VAR_081946|||http://purl.uniprot.org/annotation/VAR_081947|||http://purl.uniprot.org/annotation/VAR_081948|||http://purl.uniprot.org/annotation/VAR_081949|||http://purl.uniprot.org/annotation/VAR_081950|||http://purl.uniprot.org/annotation/VAR_081951|||http://purl.uniprot.org/annotation/VAR_081952|||http://purl.uniprot.org/annotation/VAR_081953|||http://purl.uniprot.org/annotation/VAR_081954|||http://purl.uniprot.org/annotation/VAR_081955|||http://purl.uniprot.org/annotation/VAR_081956|||http://purl.uniprot.org/annotation/VAR_081957|||http://purl.uniprot.org/annotation/VAR_081958|||http://purl.uniprot.org/annotation/VAR_081959|||http://purl.uniprot.org/annotation/VAR_081960|||http://purl.uniprot.org/annotation/VAR_081961|||http://purl.uniprot.org/annotation/VAR_081962|||http://purl.uniprot.org/annotation/VAR_081963|||http://purl.uniprot.org/annotation/VAR_081964|||http://purl.uniprot.org/annotation/VAR_081965
http://togogenome.org/gene/9606:MRPL37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZE1|||http://purl.uniprot.org/uniprot/S4R369                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein mL37|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045905|||http://purl.uniprot.org/annotation/VAR_025269|||http://purl.uniprot.org/annotation/VAR_025270
http://togogenome.org/gene/9606:LRRC51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E66                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||Leucine-rich repeat-containing protein 51                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225500|||http://purl.uniprot.org/annotation/VSP_036893|||http://purl.uniprot.org/annotation/VSP_036894|||http://purl.uniprot.org/annotation/VSP_036895|||http://purl.uniprot.org/annotation/VSP_036896|||http://purl.uniprot.org/annotation/VSP_041852
http://togogenome.org/gene/9606:GCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35557|||http://purl.uniprot.org/uniprot/Q53Y25                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Hexokinase|||Hexokinase C-terminal|||Hexokinase N-terminal|||Hexokinase large subdomain|||Hexokinase small subdomain|||Hexokinase-4|||In HHF3; increased affinity for glucose.|||In HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GCKR.|||In HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; decreased inhibition by GCKR; no effect on affinity for ATP.|||In HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GCKR; no effect on affinity for ATP.|||In HHF3; increased glucokinase activity based on measure of catalytic efficiency; increased affinity for glucose; loss of inhibition by GCKR; unchanged affinity for ATP.|||In HHF3; increased glucokinase activity; increased affinity for glucose.|||In HHF3; increased glucokinase activity; increased affinity for glucose; increased affinity for ATP.|||In MODY2 and PNDM1.|||In MODY2 and PNDM1; associated in cis with N-217 in some patients; highly decreased glucokinase activity; loss of glucokinase activity when associated with N-217; decreased affinity for glucose.|||In MODY2 and PNDM1; decreased stability; no effect on glucokinase activity; no effect on affinity for glucose.|||In MODY2 and T2D.|||In MODY2.|||In MODY2; almost complete loss of glucokinase activity.|||In MODY2; associated in cis with K-248; highly decreased glucokinase activity; loss of glucokinase activity when associated with K-248.|||In MODY2; associated in cis with M-225; highly decreased glucokinase activity; loss of glucokinase activity when associated with M-225.|||In MODY2; associated in cis with R-261 in some patients; mildly increased glucokinase activity; loss of glucokinase activity when associated with R-261.|||In MODY2; decreased affinity for glucose.|||In MODY2; decreased glucokinase activity; decreased affinity for glucose.|||In MODY2; decreased glucokinase activity; decreased affinity for glucose; decreased affinity for ATP.|||In MODY2; decreased glucokinase activity; decreased affinity for glucose; increased affinity for ATP.|||In MODY2; decreased glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP.|||In MODY2; loss of glucokinase activity; loss of affinity for glucose; loss of affinity for ATP.|||In MODY2; no effect on glucokinase activity; decreased affinity for glucose; no effect on affinity for ATP.|||In MODY2; no effect on stability; decreased glucokinase activity; decreased affinity for glucose.|||In MODY2; unknown pathological significance.|||In MODY2; unknown pathological significance; mildly increases glucokinase activity.|||In MODY2; unknown pathological significance; no change in glucokinase activity.|||In PNDM1.|||In PNDM1; decreased glucokinase activity; decreased affinity for glucose.|||In PNDM1; decreased stability; decreased glucokinase activity; decreased affinity for glucose.|||In PNDM1; decreased stability; decreased glucokinase activity; no effect on affinity for glucose.|||In PNDM1; decreased stability; increased glucokinase activity; increased affinity for glucose.|||In PNDM1; decreased stability; increased glucokinase activity; no effect on affinity for glucose.|||In PNDM1; loss of stability; loss of glucokinase activity; decreased affinity for glucose.|||In isoform 2.|||In isoform 3.|||Inactive enzyme with no glucokinase activity.|||Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose.|||Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. Loss of inhibition by GCKR. No effect on affinity for ATP.|||Increased glucokinase activity based on measure of catalytic efficiency. Increased affinity for glucose. No effect on affinity for ATP.|||Small change in glucokinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197593|||http://purl.uniprot.org/annotation/VAR_003692|||http://purl.uniprot.org/annotation/VAR_003693|||http://purl.uniprot.org/annotation/VAR_003694|||http://purl.uniprot.org/annotation/VAR_003695|||http://purl.uniprot.org/annotation/VAR_003696|||http://purl.uniprot.org/annotation/VAR_003697|||http://purl.uniprot.org/annotation/VAR_003698|||http://purl.uniprot.org/annotation/VAR_003699|||http://purl.uniprot.org/annotation/VAR_003700|||http://purl.uniprot.org/annotation/VAR_003701|||http://purl.uniprot.org/annotation/VAR_003702|||http://purl.uniprot.org/annotation/VAR_003703|||http://purl.uniprot.org/annotation/VAR_003704|||http://purl.uniprot.org/annotation/VAR_003705|||http://purl.uniprot.org/annotation/VAR_003706|||http://purl.uniprot.org/annotation/VAR_003707|||http://purl.uniprot.org/annotation/VAR_003708|||http://purl.uniprot.org/annotation/VAR_003709|||http://purl.uniprot.org/annotation/VAR_003710|||http://purl.uniprot.org/annotation/VAR_003711|||http://purl.uniprot.org/annotation/VAR_003712|||http://purl.uniprot.org/annotation/VAR_003713|||http://purl.uniprot.org/annotation/VAR_003714|||http://purl.uniprot.org/annotation/VAR_003715|||http://purl.uniprot.org/annotation/VAR_010583|||http://purl.uniprot.org/annotation/VAR_010584|||http://purl.uniprot.org/annotation/VAR_010585|||http://purl.uniprot.org/annotation/VAR_010586|||http://purl.uniprot.org/annotation/VAR_010587|||http://purl.uniprot.org/annotation/VAR_010588|||http://purl.uniprot.org/annotation/VAR_010589|||http://purl.uniprot.org/annotation/VAR_010590|||http://purl.uniprot.org/annotation/VAR_010591|||http://purl.uniprot.org/annotation/VAR_010592|||http://purl.uniprot.org/annotation/VAR_010593|||http://purl.uniprot.org/annotation/VAR_010594|||http://purl.uniprot.org/annotation/VAR_010595|||http://purl.uniprot.org/annotation/VAR_010596|||http://purl.uniprot.org/annotation/VAR_010597|||http://purl.uniprot.org/annotation/VAR_010598|||http://purl.uniprot.org/annotation/VAR_010599|||http://purl.uniprot.org/annotation/VAR_012350|||http://purl.uniprot.org/annotation/VAR_012351|||http://purl.uniprot.org/annotation/VAR_012352|||http://purl.uniprot.org/annotation/VAR_012353|||http://purl.uniprot.org/annotation/VAR_012354|||http://purl.uniprot.org/annotation/VAR_066615|||http://purl.uniprot.org/annotation/VAR_075220|||http://purl.uniprot.org/annotation/VAR_075221|||http://purl.uniprot.org/annotation/VAR_075222|||http://purl.uniprot.org/annotation/VAR_075223|||http://purl.uniprot.org/annotation/VAR_075224|||http://purl.uniprot.org/annotation/VAR_078243|||http://purl.uniprot.org/annotation/VAR_078244|||http://purl.uniprot.org/annotation/VAR_078245|||http://purl.uniprot.org/annotation/VAR_078246|||http://purl.uniprot.org/annotation/VAR_078247|||http://purl.uniprot.org/annotation/VAR_078248|||http://purl.uniprot.org/annotation/VAR_078249|||http://purl.uniprot.org/annotation/VAR_078250|||http://purl.uniprot.org/annotation/VAR_078251|||http://purl.uniprot.org/annotation/VAR_078252|||http://purl.uniprot.org/annotation/VAR_078253|||http://purl.uniprot.org/annotation/VAR_078254|||http://purl.uniprot.org/annotation/VAR_078255|||http://purl.uniprot.org/annotation/VAR_078256|||http://purl.uniprot.org/annotation/VAR_078257|||http://purl.uniprot.org/annotation/VAR_078258|||http://purl.uniprot.org/annotation/VAR_079430|||http://purl.uniprot.org/annotation/VAR_079431|||http://purl.uniprot.org/annotation/VAR_079432|||http://purl.uniprot.org/annotation/VAR_079433|||http://purl.uniprot.org/annotation/VAR_079434|||http://purl.uniprot.org/annotation/VAR_079435|||http://purl.uniprot.org/annotation/VAR_079436|||http://purl.uniprot.org/annotation/VAR_079437|||http://purl.uniprot.org/annotation/VAR_079438|||http://purl.uniprot.org/annotation/VAR_079439|||http://purl.uniprot.org/annotation/VAR_079440|||http://purl.uniprot.org/annotation/VAR_079441|||http://purl.uniprot.org/annotation/VAR_079442|||http://purl.uniprot.org/annotation/VAR_079443|||http://purl.uniprot.org/annotation/VAR_079444|||http://purl.uniprot.org/annotation/VAR_079445|||http://purl.uniprot.org/annotation/VAR_079446|||http://purl.uniprot.org/annotation/VAR_079447|||http://purl.uniprot.org/annotation/VAR_079448|||http://purl.uniprot.org/annotation/VAR_079449|||http://purl.uniprot.org/annotation/VAR_079450|||http://purl.uniprot.org/annotation/VAR_079451|||http://purl.uniprot.org/annotation/VAR_079452|||http://purl.uniprot.org/annotation/VAR_079453|||http://purl.uniprot.org/annotation/VAR_079454|||http://purl.uniprot.org/annotation/VAR_079455|||http://purl.uniprot.org/annotation/VAR_079456|||http://purl.uniprot.org/annotation/VAR_079457|||http://purl.uniprot.org/annotation/VAR_079458|||http://purl.uniprot.org/annotation/VAR_079459|||http://purl.uniprot.org/annotation/VAR_079460|||http://purl.uniprot.org/annotation/VAR_079461|||http://purl.uniprot.org/annotation/VAR_079462|||http://purl.uniprot.org/annotation/VAR_079463|||http://purl.uniprot.org/annotation/VAR_079464|||http://purl.uniprot.org/annotation/VAR_079465|||http://purl.uniprot.org/annotation/VAR_079466|||http://purl.uniprot.org/annotation/VAR_079467|||http://purl.uniprot.org/annotation/VAR_079468|||http://purl.uniprot.org/annotation/VAR_079469|||http://purl.uniprot.org/annotation/VAR_079470|||http://purl.uniprot.org/annotation/VAR_079471|||http://purl.uniprot.org/annotation/VAR_079472|||http://purl.uniprot.org/annotation/VAR_079473|||http://purl.uniprot.org/annotation/VAR_079474|||http://purl.uniprot.org/annotation/VAR_079475|||http://purl.uniprot.org/annotation/VAR_079476|||http://purl.uniprot.org/annotation/VAR_079477|||http://purl.uniprot.org/annotation/VAR_081975|||http://purl.uniprot.org/annotation/VAR_081976|||http://purl.uniprot.org/annotation/VSP_002074|||http://purl.uniprot.org/annotation/VSP_002075
http://togogenome.org/gene/9606:PTPRD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23468|||http://purl.uniprot.org/uniprot/Q2HXI4|||http://purl.uniprot.org/uniprot/Q3KPI9|||http://purl.uniprot.org/uniprot/Q59H90                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  2.5-fold reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1181.|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 7.|||In isoform 6.|||In isoform 7.|||Interaction with IL1RAPL1|||Mini-exon peptide A9; sufficient for interaction with IL1RAPL1|||Mini-exon peptide B; required for interaction with SLITRK2 and in the function in pre-synaptic differentiation; Acts as an adjustable linker to control relative positions and orientations of the PTPRD second and third immunoglobilin domains for their simultaneous interactions with the first immunoglobilin domain of IL1RAPL1 and IL1RAP; Modulates affinity for IL1RAPL1 and IL1RAP|||N-linked (GlcNAc...) asparagine|||No reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1178.|||Phosphocysteine intermediate|||Receptor-type tyrosine-protein phosphatase delta|||Required for interaction with IL1RAP|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025437|||http://purl.uniprot.org/annotation/PRO_5004209372|||http://purl.uniprot.org/annotation/PRO_5014586318|||http://purl.uniprot.org/annotation/VAR_024581|||http://purl.uniprot.org/annotation/VAR_035645|||http://purl.uniprot.org/annotation/VAR_035646|||http://purl.uniprot.org/annotation/VAR_035647|||http://purl.uniprot.org/annotation/VAR_051761|||http://purl.uniprot.org/annotation/VAR_061761|||http://purl.uniprot.org/annotation/VSP_005147|||http://purl.uniprot.org/annotation/VSP_005148|||http://purl.uniprot.org/annotation/VSP_005149|||http://purl.uniprot.org/annotation/VSP_005150|||http://purl.uniprot.org/annotation/VSP_043384|||http://purl.uniprot.org/annotation/VSP_043385|||http://purl.uniprot.org/annotation/VSP_043386|||http://purl.uniprot.org/annotation/VSP_043387|||http://purl.uniprot.org/annotation/VSP_043388|||http://purl.uniprot.org/annotation/VSP_043389|||http://purl.uniprot.org/annotation/VSP_043390|||http://purl.uniprot.org/annotation/VSP_054220|||http://purl.uniprot.org/annotation/VSP_054221
http://togogenome.org/gene/9606:ARFIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1E4|||http://purl.uniprot.org/uniprot/B4DUZ3|||http://purl.uniprot.org/uniprot/B4DXH2|||http://purl.uniprot.org/uniprot/P53365                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  AH|||Abolished ability to regulate ATG9A trafficking.|||Arfaptin-2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064667|||http://purl.uniprot.org/annotation/VSP_042524|||http://purl.uniprot.org/annotation/VSP_046913
http://togogenome.org/gene/9606:SLC24A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AI2A5; autosomal recessive.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Sodium/potassium/calcium exchanger 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019373|||http://purl.uniprot.org/annotation/VAR_042664|||http://purl.uniprot.org/annotation/VAR_070183|||http://purl.uniprot.org/annotation/VAR_071475|||http://purl.uniprot.org/annotation/VSP_008369|||http://purl.uniprot.org/annotation/VSP_008370|||http://purl.uniprot.org/annotation/VSP_008371|||http://purl.uniprot.org/annotation/VSP_008372
http://togogenome.org/gene/9606:PKMYT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0IJ49|||http://purl.uniprot.org/uniprot/Q99640                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with CDC2-CCNB1|||Interaction with PIN1|||Loss of CDC2-CCNB1 interaction.|||Loss of kinase activity.|||Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase|||Membrane-association motif|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by PLK1|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086573|||http://purl.uniprot.org/annotation/VAR_019928|||http://purl.uniprot.org/annotation/VAR_019929|||http://purl.uniprot.org/annotation/VAR_019930|||http://purl.uniprot.org/annotation/VAR_041034|||http://purl.uniprot.org/annotation/VAR_041035|||http://purl.uniprot.org/annotation/VAR_041036|||http://purl.uniprot.org/annotation/VSP_045699|||http://purl.uniprot.org/annotation/VSP_046846|||http://purl.uniprot.org/annotation/VSP_046847
http://togogenome.org/gene/9606:GEMIN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H840                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Gem-associated protein 7|||N-acetylmethionine|||Phosphothreonine|||SUZ-C|||Sm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087462
http://togogenome.org/gene/9606:COL19A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14993                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Cell attachment site|||Collagen alpha-1(XIX) chain|||Collagen-like 1|||Collagen-like 10|||Collagen-like 11|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Collagen-like 9|||Disordered|||In a breast cancer sample; somatic mutation.|||Laminin G-like|||Pro residues|||Triple-helical region 1 (COL1)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)|||Triple-helical region 4 (COL4)|||Triple-helical region 5 (COL5)|||Triple-helical region 6 (COL6)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005797|||http://purl.uniprot.org/annotation/VAR_024419|||http://purl.uniprot.org/annotation/VAR_035746|||http://purl.uniprot.org/annotation/VAR_035747|||http://purl.uniprot.org/annotation/VAR_048782|||http://purl.uniprot.org/annotation/VAR_048783
http://togogenome.org/gene/9606:ARID5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03989                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 5A|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Interaction with SOX9|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288930|||http://purl.uniprot.org/annotation/VSP_058969
http://togogenome.org/gene/9606:SUDS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7L9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Mediates interaction with USP17L2|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Sin3 histone deacetylase corepressor complex component SDS3|||Sin3 interaction domain (SID)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097652
http://togogenome.org/gene/9606:LIX1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||LIX1-like protein|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232872
http://togogenome.org/gene/9606:B9D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPU9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  B9 domain-containing protein 2|||C2 B9-type|||In JBTS34; unknown pathological significance.|||In MKS10; loss-of-function; could not rescue in vitro dosage-dependent ciliary defects; fails to interact with MKS1 although it retains its ability to interact with B9D1.|||In MKS10; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307674|||http://purl.uniprot.org/annotation/VAR_036626|||http://purl.uniprot.org/annotation/VAR_066996|||http://purl.uniprot.org/annotation/VAR_080463|||http://purl.uniprot.org/annotation/VAR_080464|||http://purl.uniprot.org/annotation/VAR_080465|||http://purl.uniprot.org/annotation/VAR_087299
http://togogenome.org/gene/9606:NANOS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60323                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC 1|||C2HC 2|||Disordered|||In isoform 2.|||Involved in RNA binding|||Nanos homolog 3|||Nanos-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207689|||http://purl.uniprot.org/annotation/VSP_038695
http://togogenome.org/gene/9606:SOAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35610                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished cholesterol O-acyltransferase activity.|||Abolished homodimerization; when associated with 504-A--A-508.|||Abolished homodimerization; when associated with A-367.|||Almost abolished cholesterol O-acyltransferase activity.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||FYXDWWN motif|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In QQ mutant; almost abolished cholesterol O-acyltransferase activity.|||In isoform 2.|||In isoform 3.|||Loss of enzymatic activity.|||Low expression, loss of enzymatic activity.|||Lumenal|||N-acetylmethionine|||Nearly normal expression and enzyme activity.|||No expression nor activity.|||Phosphoserine|||Reduced cholesterol O-acyltransferase activity.|||Sterol O-acyltransferase 1|||Strongly reduced cholesterol O-acyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207640|||http://purl.uniprot.org/annotation/VAR_052031|||http://purl.uniprot.org/annotation/VSP_045330|||http://purl.uniprot.org/annotation/VSP_045331
http://togogenome.org/gene/9606:HILPDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5L2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Hypoxia-inducible lipid droplet-associated protein|||Loss of targeting to lipid droplets and elimination of protein.|||No effect on lipid droplet targeting or protein expression; when associated with K-41.|||No effect on lipid droplet targeting or protein expression; when associated with K-44.|||Phosphoserine|||Polar residues|||Required for targeting to lipid droplets                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083976
http://togogenome.org/gene/9606:DHCR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R5F7|||http://purl.uniprot.org/uniprot/Q9UBM7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  7-dehydrocholesterol reductase|||Disordered|||Helical|||In SLOS.|||In SLOS; mild.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207502|||http://purl.uniprot.org/annotation/VAR_012717|||http://purl.uniprot.org/annotation/VAR_012718|||http://purl.uniprot.org/annotation/VAR_012719|||http://purl.uniprot.org/annotation/VAR_012720|||http://purl.uniprot.org/annotation/VAR_012721|||http://purl.uniprot.org/annotation/VAR_012722|||http://purl.uniprot.org/annotation/VAR_012723|||http://purl.uniprot.org/annotation/VAR_012724|||http://purl.uniprot.org/annotation/VAR_012725|||http://purl.uniprot.org/annotation/VAR_012726|||http://purl.uniprot.org/annotation/VAR_012727|||http://purl.uniprot.org/annotation/VAR_012728|||http://purl.uniprot.org/annotation/VAR_012729|||http://purl.uniprot.org/annotation/VAR_012730|||http://purl.uniprot.org/annotation/VAR_016975|||http://purl.uniprot.org/annotation/VAR_023148|||http://purl.uniprot.org/annotation/VAR_023149|||http://purl.uniprot.org/annotation/VAR_023150|||http://purl.uniprot.org/annotation/VAR_023151|||http://purl.uniprot.org/annotation/VAR_023152|||http://purl.uniprot.org/annotation/VAR_023153|||http://purl.uniprot.org/annotation/VAR_023154|||http://purl.uniprot.org/annotation/VAR_023155|||http://purl.uniprot.org/annotation/VAR_023156|||http://purl.uniprot.org/annotation/VAR_023157|||http://purl.uniprot.org/annotation/VAR_023158|||http://purl.uniprot.org/annotation/VAR_023159|||http://purl.uniprot.org/annotation/VAR_023160|||http://purl.uniprot.org/annotation/VAR_023161|||http://purl.uniprot.org/annotation/VAR_023162|||http://purl.uniprot.org/annotation/VAR_023163|||http://purl.uniprot.org/annotation/VAR_023164|||http://purl.uniprot.org/annotation/VAR_023165|||http://purl.uniprot.org/annotation/VAR_023166|||http://purl.uniprot.org/annotation/VAR_023167|||http://purl.uniprot.org/annotation/VAR_023168|||http://purl.uniprot.org/annotation/VAR_023169|||http://purl.uniprot.org/annotation/VAR_023170|||http://purl.uniprot.org/annotation/VAR_023171|||http://purl.uniprot.org/annotation/VAR_023172|||http://purl.uniprot.org/annotation/VAR_023173|||http://purl.uniprot.org/annotation/VAR_023174|||http://purl.uniprot.org/annotation/VAR_023175|||http://purl.uniprot.org/annotation/VAR_023176|||http://purl.uniprot.org/annotation/VAR_023177|||http://purl.uniprot.org/annotation/VAR_023178|||http://purl.uniprot.org/annotation/VAR_023179|||http://purl.uniprot.org/annotation/VAR_023180|||http://purl.uniprot.org/annotation/VAR_023181|||http://purl.uniprot.org/annotation/VAR_023182|||http://purl.uniprot.org/annotation/VAR_023183|||http://purl.uniprot.org/annotation/VAR_023184|||http://purl.uniprot.org/annotation/VAR_023185|||http://purl.uniprot.org/annotation/VAR_052154|||http://purl.uniprot.org/annotation/VAR_067456|||http://purl.uniprot.org/annotation/VAR_074180
http://togogenome.org/gene/9606:PRMT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LA8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by autocatalysis|||Disordered|||In PRMT6dn; abolishes histone methyltransferase H3R2me2a and transcriptional coactivator activities and reduces protein stability. This mutation abolishes automethylation.|||In isoform 2.|||Inhibits automethylation but does not affect methylation of other proteins. Reduces protein stability.|||Phosphothreonine|||Protein arginine N-methyltransferase 6|||SAM-dependent MTase PRMT-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212332|||http://purl.uniprot.org/annotation/VAR_057150|||http://purl.uniprot.org/annotation/VSP_037465
http://togogenome.org/gene/9606:PTPN21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16825                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||FERM|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219439|||http://purl.uniprot.org/annotation/VAR_055539|||http://purl.uniprot.org/annotation/VAR_060341|||http://purl.uniprot.org/annotation/VAR_060342
http://togogenome.org/gene/9606:NEK11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDN2|||http://purl.uniprot.org/uniprot/B4DM56|||http://purl.uniprot.org/uniprot/E9PHI8|||http://purl.uniprot.org/uniprot/Q8NG66                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of kinase activity.|||Phosphoserine; by CHEK1|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086438|||http://purl.uniprot.org/annotation/VAR_033907|||http://purl.uniprot.org/annotation/VAR_040935|||http://purl.uniprot.org/annotation/VAR_040936|||http://purl.uniprot.org/annotation/VAR_040937|||http://purl.uniprot.org/annotation/VAR_040938|||http://purl.uniprot.org/annotation/VAR_040939|||http://purl.uniprot.org/annotation/VAR_040940|||http://purl.uniprot.org/annotation/VAR_040941|||http://purl.uniprot.org/annotation/VAR_040942|||http://purl.uniprot.org/annotation/VAR_040943|||http://purl.uniprot.org/annotation/VAR_040944|||http://purl.uniprot.org/annotation/VSP_040080|||http://purl.uniprot.org/annotation/VSP_040081|||http://purl.uniprot.org/annotation/VSP_051820|||http://purl.uniprot.org/annotation/VSP_051821|||http://purl.uniprot.org/annotation/VSP_051822|||http://purl.uniprot.org/annotation/VSP_051823
http://togogenome.org/gene/9606:TRIM37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94972                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to monoubiquitinate 'Lys-119' of histone H2A (H2AK119Ub).|||B box-type|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TRIM37|||In MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates.|||In MUL; no effect on E3 ubiquitin-protein ligase activity.|||In MUL; no effect on ubiquitination but affects subcellular localization.|||In isoform 2.|||In isoform 3.|||MATH|||N-acetylmethionine|||Phosphoserine|||Polar residues|||RING-type; degenerate|||Reduces ubiquitination and abolishes the formation of perinuclear aggregates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056254|||http://purl.uniprot.org/annotation/VAR_052142|||http://purl.uniprot.org/annotation/VAR_060217|||http://purl.uniprot.org/annotation/VAR_060218|||http://purl.uniprot.org/annotation/VAR_060219|||http://purl.uniprot.org/annotation/VAR_060220|||http://purl.uniprot.org/annotation/VAR_075470|||http://purl.uniprot.org/annotation/VSP_011919|||http://purl.uniprot.org/annotation/VSP_011920|||http://purl.uniprot.org/annotation/VSP_057468
http://togogenome.org/gene/9606:YAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJQ9|||http://purl.uniprot.org/uniprot/G3V212|||http://purl.uniprot.org/uniprot/Q8IY57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||RanBP2-type|||YY1-associated factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066113|||http://purl.uniprot.org/annotation/VSP_043415|||http://purl.uniprot.org/annotation/VSP_044598|||http://purl.uniprot.org/annotation/VSP_044599|||http://purl.uniprot.org/annotation/VSP_055659
http://togogenome.org/gene/9606:BGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNL4|||http://purl.uniprot.org/uniprot/P21810                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Biglycan|||In MRLS; unknown pathological significance.|||In SEMDX.|||In SEMDX; reduced protein stability.|||In a breast cancer sample; somatic mutation.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (glycosaminoglycan) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032691|||http://purl.uniprot.org/annotation/PRO_0000032692|||http://purl.uniprot.org/annotation/PRO_5011019687|||http://purl.uniprot.org/annotation/VAR_036605|||http://purl.uniprot.org/annotation/VAR_036606|||http://purl.uniprot.org/annotation/VAR_076590|||http://purl.uniprot.org/annotation/VAR_076591|||http://purl.uniprot.org/annotation/VAR_078028|||http://purl.uniprot.org/annotation/VAR_078029
http://togogenome.org/gene/9606:CHTF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG13                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Chromosome transmission fidelity protein 8 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327253
http://togogenome.org/gene/9606:ORMDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0S3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||ORM1-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215630
http://togogenome.org/gene/9606:MAP7D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWC1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MAP7 domain-containing protein 3|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306812|||http://purl.uniprot.org/annotation/VAR_035314|||http://purl.uniprot.org/annotation/VAR_035315|||http://purl.uniprot.org/annotation/VAR_077003|||http://purl.uniprot.org/annotation/VSP_028498|||http://purl.uniprot.org/annotation/VSP_028499|||http://purl.uniprot.org/annotation/VSP_045008
http://togogenome.org/gene/9606:TPSB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJT7|||http://purl.uniprot.org/uniprot/P20231                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In allele beta-II.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Phosphotyrosine|||Tryptase beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027481|||http://purl.uniprot.org/annotation/PRO_0000027482|||http://purl.uniprot.org/annotation/PRO_5007491786|||http://purl.uniprot.org/annotation/VAR_088016|||http://purl.uniprot.org/annotation/VAR_088017|||http://purl.uniprot.org/annotation/VAR_088018
http://togogenome.org/gene/9606:INTS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVM9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Integrator complex subunit 13|||Loss of nuclear location. Location is mainly cytoplasmic or diffuse. Loss of Dynein recruitment to nuclear envelope.|||Nuclear localization signal (NLS)|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089845|||http://purl.uniprot.org/annotation/VAR_035673|||http://purl.uniprot.org/annotation/VAR_050864|||http://purl.uniprot.org/annotation/VSP_056514
http://togogenome.org/gene/9606:HOXD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSX5|||http://purl.uniprot.org/uniprot/P13378                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D8|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200216|||http://purl.uniprot.org/annotation/VSP_042856|||http://purl.uniprot.org/annotation/VSP_045862|||http://purl.uniprot.org/annotation/VSP_045863
http://togogenome.org/gene/9606:SMC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  20% loss of sister chromatid cohesion, no effect on cohesin complex assembly; when associated with A-105.|||20% loss of sister chromatid cohesion, no effect on cohesin complex assembly; when associated with A-106.|||Disordered|||In CDLS3.|||In CDLS3; affects the affinity of SMC hinge dimers for DNA; mutated hinge dimers bind DNA with higher affinity than wild-type proteins.|||N6-acetyllysine|||No effect on sister chromatid cohesion, nor on cohesin complex assembly; when associated with Q-105.|||No effect on sister chromatid cohesion, nor on cohesin complex assembly; when associated with Q-106.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMC hinge|||Stabilizes interaction with PDS5A and WAPL; when associated with R-105.|||Stabilizes interaction with PDS5A and WAPL; when associated with R-106.|||Structural maintenance of chromosomes protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119001|||http://purl.uniprot.org/annotation/VAR_032845|||http://purl.uniprot.org/annotation/VAR_083979
http://togogenome.org/gene/9606:KRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04264                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In AEI2 and EHK.|||In AEI2.|||In EHK.|||In EHK; severe.|||In NEPPK.|||In allele 1B.|||In palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas.|||Keratin, type II cytoskeletal 1|||Linker 1|||Linker 12|||N6,N6-dimethyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063709|||http://purl.uniprot.org/annotation/VAR_003853|||http://purl.uniprot.org/annotation/VAR_003854|||http://purl.uniprot.org/annotation/VAR_003855|||http://purl.uniprot.org/annotation/VAR_003856|||http://purl.uniprot.org/annotation/VAR_003857|||http://purl.uniprot.org/annotation/VAR_003858|||http://purl.uniprot.org/annotation/VAR_003859|||http://purl.uniprot.org/annotation/VAR_003860|||http://purl.uniprot.org/annotation/VAR_003861|||http://purl.uniprot.org/annotation/VAR_003862|||http://purl.uniprot.org/annotation/VAR_003863|||http://purl.uniprot.org/annotation/VAR_003864|||http://purl.uniprot.org/annotation/VAR_017819|||http://purl.uniprot.org/annotation/VAR_017820|||http://purl.uniprot.org/annotation/VAR_017821|||http://purl.uniprot.org/annotation/VAR_017822|||http://purl.uniprot.org/annotation/VAR_017823|||http://purl.uniprot.org/annotation/VAR_017824|||http://purl.uniprot.org/annotation/VAR_017825|||http://purl.uniprot.org/annotation/VAR_017826|||http://purl.uniprot.org/annotation/VAR_017827|||http://purl.uniprot.org/annotation/VAR_017828|||http://purl.uniprot.org/annotation/VAR_038627|||http://purl.uniprot.org/annotation/VAR_038628|||http://purl.uniprot.org/annotation/VAR_038629|||http://purl.uniprot.org/annotation/VAR_071986|||http://purl.uniprot.org/annotation/VAR_071987|||http://purl.uniprot.org/annotation/VAR_071988
http://togogenome.org/gene/9606:POU4F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15319                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Homeobox|||In DFNA15.|||In DFNA15; decreases subcellular localization in the nucleus.|||In DFNA15; decreases subcellular localization in the nucleus; decreases DNA-binding activity; decreases transcriptional activity.|||In DFNA15; unknown pathological significance.|||POU domain, class 4, transcription factor 3|||POU-IV box|||POU-specific                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100742|||http://purl.uniprot.org/annotation/VAR_045682|||http://purl.uniprot.org/annotation/VAR_045683|||http://purl.uniprot.org/annotation/VAR_079859|||http://purl.uniprot.org/annotation/VAR_079860|||http://purl.uniprot.org/annotation/VAR_079861|||http://purl.uniprot.org/annotation/VAR_079862|||http://purl.uniprot.org/annotation/VAR_079863|||http://purl.uniprot.org/annotation/VAR_079864|||http://purl.uniprot.org/annotation/VAR_079865|||http://purl.uniprot.org/annotation/VAR_079866|||http://purl.uniprot.org/annotation/VAR_079867|||http://purl.uniprot.org/annotation/VAR_079868|||http://purl.uniprot.org/annotation/VAR_079869|||http://purl.uniprot.org/annotation/VAR_079870|||http://purl.uniprot.org/annotation/VAR_079871
http://togogenome.org/gene/9606:CCL4L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHW4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-C motif chemokine 4-like|||In isoform 10.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326234|||http://purl.uniprot.org/annotation/VSP_032625|||http://purl.uniprot.org/annotation/VSP_032626|||http://purl.uniprot.org/annotation/VSP_032627|||http://purl.uniprot.org/annotation/VSP_032628|||http://purl.uniprot.org/annotation/VSP_032629|||http://purl.uniprot.org/annotation/VSP_032630|||http://purl.uniprot.org/annotation/VSP_032631|||http://purl.uniprot.org/annotation/VSP_032632|||http://purl.uniprot.org/annotation/VSP_032633
http://togogenome.org/gene/9606:MFAP3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75121                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||In isoform 3.|||Microfibrillar-associated protein 3-like|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by EGFR|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014869|||http://purl.uniprot.org/annotation/VSP_011100|||http://purl.uniprot.org/annotation/VSP_014094|||http://purl.uniprot.org/annotation/VSP_014095
http://togogenome.org/gene/9606:SP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLN9|||http://purl.uniprot.org/uniprot/Q02447|||http://purl.uniprot.org/uniprot/Q59FX5|||http://purl.uniprot.org/uniprot/Q86TP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  200-fold increase in transcriptional activation.|||9aaTAD|||A decreased interaction with HDAC1 and deacetylation of SP3. Increase of about 4.5% of activity of the TERT promoter. Decreased recruitment of HDAC1 and increased binding of RNA polymerase II with promoter DNA.|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Great loss of sumoylation, 20-fold increase in transcriptional activity and diffuse nuclear localization. Further small increase in transcriptional activity; when associated with R-120. Increased interaction with HDAC1 and deacetylation of SP3. About 50% decrease in activity of the TERT promoter. Enhances recruitment of HDAC1 and inhibits binding of RNA polymerase II with promoter DNA.|||In isoform 2 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Increases transcriptional activity.|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Repressor domain|||Some loss of sumoylation. Slight increase in transcriptional activity. Large increase in transcriptional activity; when associated with R-551.|||Transactivation domain (Gln-rich)|||Transcription factor Sp3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047141|||http://purl.uniprot.org/annotation/VAR_016123|||http://purl.uniprot.org/annotation/VSP_026698|||http://purl.uniprot.org/annotation/VSP_026699|||http://purl.uniprot.org/annotation/VSP_026700|||http://purl.uniprot.org/annotation/VSP_026701|||http://purl.uniprot.org/annotation/VSP_026702
http://togogenome.org/gene/9606:CLEC7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5Q1|||http://purl.uniprot.org/uniprot/Q68D78|||http://purl.uniprot.org/uniprot/Q9BXN2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 7 member A|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||ITAM-like|||In isoform 10.|||In isoform 2, isoform 6 and isoform 7.|||In isoform 3 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||May be associated with invasive aspergillosis.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269491|||http://purl.uniprot.org/annotation/VAR_050111|||http://purl.uniprot.org/annotation/VAR_084643|||http://purl.uniprot.org/annotation/VSP_022048|||http://purl.uniprot.org/annotation/VSP_022049|||http://purl.uniprot.org/annotation/VSP_022050|||http://purl.uniprot.org/annotation/VSP_022051|||http://purl.uniprot.org/annotation/VSP_022052|||http://purl.uniprot.org/annotation/VSP_022053|||http://purl.uniprot.org/annotation/VSP_022054|||http://purl.uniprot.org/annotation/VSP_022055|||http://purl.uniprot.org/annotation/VSP_022056|||http://purl.uniprot.org/annotation/VSP_022057|||http://purl.uniprot.org/annotation/VSP_043298|||http://purl.uniprot.org/annotation/VSP_043299|||http://purl.uniprot.org/annotation/VSP_047589|||http://purl.uniprot.org/annotation/VSP_047590
http://togogenome.org/gene/9606:PAPOLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1Z6|||http://purl.uniprot.org/uniprot/Q9NRJ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Disordered|||Interaction with RNA|||Poly(A) polymerase RNA-binding|||Poly(A) polymerase beta|||Poly(A) polymerase central|||Polymerase nucleotidyl transferase|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051622
http://togogenome.org/gene/9606:RASA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43374                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||C2 1|||C2 2|||Disordered|||In isoform 2.|||PH|||Polar residues|||Ras GTPase-activating protein 4|||Ras-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056647|||http://purl.uniprot.org/annotation/VAR_027680|||http://purl.uniprot.org/annotation/VAR_027681|||http://purl.uniprot.org/annotation/VSP_039965
http://togogenome.org/gene/9606:ATOSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L5A3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Atos homolog protein B|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Pro residues|||Required for macropage invasion|||Transactivation domain 1 (TAD1)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313620|||http://purl.uniprot.org/annotation/VSP_030063|||http://purl.uniprot.org/annotation/VSP_042437
http://togogenome.org/gene/9606:BRICD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PL45                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BRICHOS|||BRICHOS domain-containing protein 5|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284046|||http://purl.uniprot.org/annotation/VAR_031629|||http://purl.uniprot.org/annotation/VAR_061620|||http://purl.uniprot.org/annotation/VAR_061621|||http://purl.uniprot.org/annotation/VSP_024411
http://togogenome.org/gene/9606:MYBPHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUH7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||Myosin-binding protein H-like|||Omega-N-methylarginine|||Phosphoserine|||Probable disease-associated variant found in a family with dilated cardiomyopathy and atrial and ventricular arrhythmias; subject to nonsense-mediated decay; disrupted myosin-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330019|||http://purl.uniprot.org/annotation/VAR_042686|||http://purl.uniprot.org/annotation/VAR_083211|||http://purl.uniprot.org/annotation/VSP_055601
http://togogenome.org/gene/9606:GP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14770                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In BSS.|||LRR|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein IX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021360|||http://purl.uniprot.org/annotation/VAR_005263|||http://purl.uniprot.org/annotation/VAR_005264|||http://purl.uniprot.org/annotation/VAR_024996|||http://purl.uniprot.org/annotation/VAR_024997|||http://purl.uniprot.org/annotation/VAR_024998|||http://purl.uniprot.org/annotation/VAR_024999|||http://purl.uniprot.org/annotation/VAR_025008|||http://purl.uniprot.org/annotation/VAR_025009
http://togogenome.org/gene/9606:RETREG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with ATG8 family proteins, induction of ER fragmentation and ER degradation.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||LIR motif|||Lumenal|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced formation of autophagosomes.|||Removed|||Reticulophagy regulator 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288469|||http://purl.uniprot.org/annotation/VSP_056991
http://togogenome.org/gene/9606:PRKCB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05771                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||C2|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform Beta-II.|||N-acetylalanine|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by SYK|||Polar residues|||Protein kinase|||Protein kinase C beta type|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055684|||http://purl.uniprot.org/annotation/VAR_042304|||http://purl.uniprot.org/annotation/VAR_042305|||http://purl.uniprot.org/annotation/VAR_042306|||http://purl.uniprot.org/annotation/VSP_004738
http://togogenome.org/gene/9606:CIP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCG1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreases homodimerization. Reduces binding to PPP2R5C. Decreases protein level.|||Helical|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Protein CIP2A|||Reduces binding to PPP2R5C.|||Required for homodimerization|||Required for interaction with PPP2R5C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287141|||http://purl.uniprot.org/annotation/VAR_046939|||http://purl.uniprot.org/annotation/VAR_046940|||http://purl.uniprot.org/annotation/VAR_046941|||http://purl.uniprot.org/annotation/VAR_046942|||http://purl.uniprot.org/annotation/VAR_046943|||http://purl.uniprot.org/annotation/VAR_046944|||http://purl.uniprot.org/annotation/VAR_046945|||http://purl.uniprot.org/annotation/VAR_046946|||http://purl.uniprot.org/annotation/VSP_025336
http://togogenome.org/gene/9606:SCOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIL1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Causes tetramerization and loss of interaction with FEZ1; when associated with L-125.|||Causes tetramerization and loss of interaction with FEZ1; when associated with V-132.|||Causes trimerization and impairs interaction with FEZ1 coiled coil but does not impair interaction with full-length FEZ1; when associated with L-97.|||Causes trimerization and impairs interaction with FEZ1 coiled coil but does not impair interaction with full-length FEZ1; when associated with V-93.|||Impairs interaction with FEZ1 coiled coil but does not impair interaction with full-length FEZ1.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Short coiled-coil protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334164|||http://purl.uniprot.org/annotation/VSP_033642|||http://purl.uniprot.org/annotation/VSP_033643|||http://purl.uniprot.org/annotation/VSP_033644|||http://purl.uniprot.org/annotation/VSP_033645
http://togogenome.org/gene/9606:PAIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H074                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||MIF4G|||N-acetylalanine|||Omega-N-methylarginine|||PABPC1-interacting motif-1 (PAM1)|||PABPC1-interacting motif-2 (PAM2)|||PAIP1 middle domain (PAIP1M)|||Polar residues|||Polyadenylate-binding protein-interacting protein 1|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058177|||http://purl.uniprot.org/annotation/VSP_010005|||http://purl.uniprot.org/annotation/VSP_047503
http://togogenome.org/gene/9606:SBSPON                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Alternate|||N-linked (GlcNAc...) asparagine|||SMB|||Somatomedin-B and thrombospondin type-1 domain-containing protein|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332158|||http://purl.uniprot.org/annotation/VAR_042961|||http://purl.uniprot.org/annotation/VAR_061914
http://togogenome.org/gene/9606:CACNA1S                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALM3|||http://purl.uniprot.org/uniprot/Q13698                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Binding to the beta subunit|||Cytoplasmic|||Dihydropyridine binding|||Disordered|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In CMYP18.|||In CMYP18; decreased protein abundance.|||In CMYP18; unknown pathological significance.|||In CMYP18; unknown pathological significance; patient myotubes show decreased depolarization-induced release of sequestered calcium ion into cytosol compared to control.|||In HOKPP1.|||In MHS5.|||Interaction with STAC, STAC2 and STAC3 (via SH3 domains)|||Interaction with calmodulin|||N-linked (GlcNAc...) asparagine|||Phenylalkylamine binding|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKA and CAMK2|||Pore-forming|||Selectivity filter of repeat I|||Selectivity filter of repeat II|||Selectivity filter of repeat III|||Selectivity filter of repeat IV|||Voltage-dependent L-type calcium channel subunit alpha-1S|||Voltage-dependent calcium channel alpha-1 subunit IQ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053943|||http://purl.uniprot.org/annotation/VAR_001498|||http://purl.uniprot.org/annotation/VAR_001499|||http://purl.uniprot.org/annotation/VAR_001500|||http://purl.uniprot.org/annotation/VAR_001501|||http://purl.uniprot.org/annotation/VAR_001502|||http://purl.uniprot.org/annotation/VAR_001503|||http://purl.uniprot.org/annotation/VAR_046970|||http://purl.uniprot.org/annotation/VAR_046971|||http://purl.uniprot.org/annotation/VAR_046972|||http://purl.uniprot.org/annotation/VAR_046973|||http://purl.uniprot.org/annotation/VAR_054953|||http://purl.uniprot.org/annotation/VAR_054954|||http://purl.uniprot.org/annotation/VAR_088226|||http://purl.uniprot.org/annotation/VAR_088227|||http://purl.uniprot.org/annotation/VAR_088228|||http://purl.uniprot.org/annotation/VAR_088229|||http://purl.uniprot.org/annotation/VAR_088230|||http://purl.uniprot.org/annotation/VAR_088231|||http://purl.uniprot.org/annotation/VAR_088232|||http://purl.uniprot.org/annotation/VAR_088233|||http://purl.uniprot.org/annotation/VAR_088234
http://togogenome.org/gene/9606:DIP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14689|||http://purl.uniprot.org/uniprot/Q96NX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Basic and acidic residues|||DMAP1-binding|||Disco-interacting protein 2 homolog A|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PXXP motif; required for interaction with CTTN|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079906|||http://purl.uniprot.org/annotation/VAR_047372|||http://purl.uniprot.org/annotation/VAR_047373|||http://purl.uniprot.org/annotation/VSP_007748|||http://purl.uniprot.org/annotation/VSP_007749|||http://purl.uniprot.org/annotation/VSP_007750|||http://purl.uniprot.org/annotation/VSP_007751|||http://purl.uniprot.org/annotation/VSP_045408|||http://purl.uniprot.org/annotation/VSP_045409|||http://purl.uniprot.org/annotation/VSP_045410|||http://purl.uniprot.org/annotation/VSP_047246
http://togogenome.org/gene/9606:DEFA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59666|||http://purl.uniprot.org/uniprot/Q6EZE9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Peptide|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  HP 3-56|||Mammalian defensins|||Neutrophil defensin 2|||Neutrophil defensin 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006777|||http://purl.uniprot.org/annotation/PRO_0000006778|||http://purl.uniprot.org/annotation/PRO_0000006779|||http://purl.uniprot.org/annotation/PRO_0000006780|||http://purl.uniprot.org/annotation/PRO_5014310427
http://togogenome.org/gene/9606:PURB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QR8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Removed|||Transcriptional activator protein Pur-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225615
http://togogenome.org/gene/9606:A4GNT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNA3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,4-N-acetylglucosaminyltransferase|||Cytoplasmic|||DXD motif|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080583|||http://purl.uniprot.org/annotation/VAR_022096
http://togogenome.org/gene/9606:PRKACB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVC4|||http://purl.uniprot.org/uniprot/B1APF9|||http://purl.uniprot.org/uniprot/B1APG3|||http://purl.uniprot.org/uniprot/B2RB89|||http://purl.uniprot.org/uniprot/B7ZA00|||http://purl.uniprot.org/uniprot/P22694                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Deamidated asparagine|||In CAFD2.|||In CAFD2; increased sensitivity to cAMP activation.|||In CAFD2; increased sensitivity to cAMP activation; decreased interaction with regulatory subunits PRKAR1A and PRKAR2B.|||In isoform 10.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 10.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Removed|||cAMP-dependent protein kinase catalytic subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086060|||http://purl.uniprot.org/annotation/VAR_040594|||http://purl.uniprot.org/annotation/VAR_085199|||http://purl.uniprot.org/annotation/VAR_085200|||http://purl.uniprot.org/annotation/VAR_085201|||http://purl.uniprot.org/annotation/VAR_085202|||http://purl.uniprot.org/annotation/VSP_017364|||http://purl.uniprot.org/annotation/VSP_017365|||http://purl.uniprot.org/annotation/VSP_017366|||http://purl.uniprot.org/annotation/VSP_017367|||http://purl.uniprot.org/annotation/VSP_017368|||http://purl.uniprot.org/annotation/VSP_017369|||http://purl.uniprot.org/annotation/VSP_017370|||http://purl.uniprot.org/annotation/VSP_017371|||http://purl.uniprot.org/annotation/VSP_036556|||http://purl.uniprot.org/annotation/VSP_036557|||http://purl.uniprot.org/annotation/VSP_043372|||http://purl.uniprot.org/annotation/VSP_046238
http://togogenome.org/gene/9606:OCIAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q56VL3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||OCIA|||OCIA domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299392|||http://purl.uniprot.org/annotation/VAR_053950|||http://purl.uniprot.org/annotation/VSP_027626
http://togogenome.org/gene/9606:USP17L18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6R9N7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421092
http://togogenome.org/gene/9606:SLC4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02730                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  (Microbial infection) 5ABC region; interaction with P.falciparum (isolate 3D7) MSP9|||(Microbial infection) Interaction with P.falciparum (isolate K1) FBPA|||Acidic residues|||Band 3 anion transport protein|||Cytoplasmic|||Dimerization arm|||Discontinuously helical|||Discontinuously helical; Name=10|||Discontinuously helical; Name=3|||Disordered|||Extracellular|||Found in patients with hemolytic anemia; unknown pathological significance; Montefiore.|||Globular|||Helical; Name=1|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Impairs expression at the cell membrane.|||Important for anion transport|||Important for anion-proton cotransport|||In BOW antigen.|||In BP(a) antigen.|||In CHC; Blackburn; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.|||In CHC; Hemel; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.|||In CHC; Hurstpierpont; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.|||In DRTA1.|||In DRTA1; detected subapically and at the apical membrane as well as at the basolateral membrane in contrast to the normal basolateral appearance of wild-type protein.|||In DRTA1; impairs expression at the cell membrane.|||In DRTA1; markedly increased red cell sulfate transport but almost normal red cell iodide transport.|||In DRTA1; reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain.|||In DRTA4 and dRTA-NRC; impairs expression at the cell membrane.|||In DRTA4.|||In DRTA4; decreased expression; decreased stability; no effect on dimerization.|||In Di(a)/Memphis-II antigen.|||In ELO antigen.|||In FR(a+) antigen.|||In HG(a) antigen.|||In KREP antigen.|||In MO(a) antigen.|||In NFLD+ antigen.|||In PN(a) antigen.|||In RB(A) antigen.|||In SAO and DRTA4; increased rigidity of the erythrocyte membrane leading to increased resistance to shear stress and increased resistance to P.falciparum.|||In SPH4; Benesov.|||In SPH4; Bicetre I.|||In SPH4; Birmingham.|||In SPH4; Boston.|||In SPH4; Cape Town.|||In SPH4; Chur.|||In SPH4; Coimbra; also in AR-dRTA.|||In SPH4; Dresden.|||In SPH4; Fukoka.|||In SPH4; Horam; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.|||In SPH4; Hradec Kralove.|||In SPH4; Jablonec.|||In SPH4; Mondego.|||In SPH4; Most.|||In SPH4; Nagoya.|||In SPH4; Napoli II.|||In SPH4; Nara.|||In SPH4; Okinawa.|||In SPH4; Osnabruck II.|||In SPH4; Philadelphia.|||In SPH4; Pinhal.|||In SPH4; Prague II; induces abnormal cations sodium and potassium fluxes; decreases anion chloride transport.|||In SPH4; Prague III.|||In SPH4; Tambau.|||In SPH4; Tokyo.|||In SPH4; Tuscaloosa.|||In SPH4; Yamagata.|||In SW(a+) antigen.|||In TR(A) antigen.|||In VG(a) antigen.|||In WARR antigen.|||In WD(a) antigen.|||In WR(a) antigen.|||In WU antigen.|||In acanthocytosis; slightly increases transporter activity; impairs expression at the cell membrane.|||In dRTA-NRC.|||In isoform 2.|||Interaction with ANK1|||Involved in anion transport|||Loss of N-glycosylation site.|||N-acetylmethionine|||N-linked (GlcNAc...) (complex) asparagine|||Phosphoserine|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079209|||http://purl.uniprot.org/annotation/VAR_000798|||http://purl.uniprot.org/annotation/VAR_000799|||http://purl.uniprot.org/annotation/VAR_000800|||http://purl.uniprot.org/annotation/VAR_000801|||http://purl.uniprot.org/annotation/VAR_000802|||http://purl.uniprot.org/annotation/VAR_000803|||http://purl.uniprot.org/annotation/VAR_000804|||http://purl.uniprot.org/annotation/VAR_000805|||http://purl.uniprot.org/annotation/VAR_000806|||http://purl.uniprot.org/annotation/VAR_000807|||http://purl.uniprot.org/annotation/VAR_000808|||http://purl.uniprot.org/annotation/VAR_013784|||http://purl.uniprot.org/annotation/VAR_013785|||http://purl.uniprot.org/annotation/VAR_013786|||http://purl.uniprot.org/annotation/VAR_013787|||http://purl.uniprot.org/annotation/VAR_013788|||http://purl.uniprot.org/annotation/VAR_013789|||http://purl.uniprot.org/annotation/VAR_013790|||http://purl.uniprot.org/annotation/VAR_013791|||http://purl.uniprot.org/annotation/VAR_013792|||http://purl.uniprot.org/annotation/VAR_013793|||http://purl.uniprot.org/annotation/VAR_013794|||http://purl.uniprot.org/annotation/VAR_013795|||http://purl.uniprot.org/annotation/VAR_013796|||http://purl.uniprot.org/annotation/VAR_013797|||http://purl.uniprot.org/annotation/VAR_013798|||http://purl.uniprot.org/annotation/VAR_013799|||http://purl.uniprot.org/annotation/VAR_013800|||http://purl.uniprot.org/annotation/VAR_013801|||http://purl.uniprot.org/annotation/VAR_013802|||http://purl.uniprot.org/annotation/VAR_013803|||http://purl.uniprot.org/annotation/VAR_013804|||http://purl.uniprot.org/annotation/VAR_013805|||http://purl.uniprot.org/annotation/VAR_013806|||http://purl.uniprot.org/annotation/VAR_013807|||http://purl.uniprot.org/annotation/VAR_013808|||http://purl.uniprot.org/annotation/VAR_013809|||http://purl.uniprot.org/annotation/VAR_013810|||http://purl.uniprot.org/annotation/VAR_013811|||http://purl.uniprot.org/annotation/VAR_013812|||http://purl.uniprot.org/annotation/VAR_013813|||http://purl.uniprot.org/annotation/VAR_013814|||http://purl.uniprot.org/annotation/VAR_013815|||http://purl.uniprot.org/annotation/VAR_013816|||http://purl.uniprot.org/annotation/VAR_014612|||http://purl.uniprot.org/annotation/VAR_014613|||http://purl.uniprot.org/annotation/VAR_014614|||http://purl.uniprot.org/annotation/VAR_014615|||http://purl.uniprot.org/annotation/VAR_014616|||http://purl.uniprot.org/annotation/VAR_014617|||http://purl.uniprot.org/annotation/VAR_014618|||http://purl.uniprot.org/annotation/VAR_014619|||http://purl.uniprot.org/annotation/VAR_015104|||http://purl.uniprot.org/annotation/VAR_015105|||http://purl.uniprot.org/annotation/VAR_015106|||http://purl.uniprot.org/annotation/VAR_015107|||http://purl.uniprot.org/annotation/VAR_015108|||http://purl.uniprot.org/annotation/VAR_015109|||http://purl.uniprot.org/annotation/VAR_015171|||http://purl.uniprot.org/annotation/VAR_025090|||http://purl.uniprot.org/annotation/VAR_036693|||http://purl.uniprot.org/annotation/VAR_039290|||http://purl.uniprot.org/annotation/VAR_039291|||http://purl.uniprot.org/annotation/VAR_039292|||http://purl.uniprot.org/annotation/VAR_039293|||http://purl.uniprot.org/annotation/VAR_039294|||http://purl.uniprot.org/annotation/VAR_039295|||http://purl.uniprot.org/annotation/VAR_039296|||http://purl.uniprot.org/annotation/VAR_039297|||http://purl.uniprot.org/annotation/VAR_058035|||http://purl.uniprot.org/annotation/VAR_058036|||http://purl.uniprot.org/annotation/VAR_058037|||http://purl.uniprot.org/annotation/VAR_058038|||http://purl.uniprot.org/annotation/VAR_058039|||http://purl.uniprot.org/annotation/VAR_058040|||http://purl.uniprot.org/annotation/VAR_058041|||http://purl.uniprot.org/annotation/VAR_058042|||http://purl.uniprot.org/annotation/VAR_058043|||http://purl.uniprot.org/annotation/VAR_087559|||http://purl.uniprot.org/annotation/VSP_057833
http://togogenome.org/gene/9606:MRPL23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16540                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Large ribosomal subunit protein uL23m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129484|||http://purl.uniprot.org/annotation/VAR_057197|||http://purl.uniprot.org/annotation/VAR_057198|||http://purl.uniprot.org/annotation/VAR_057199|||http://purl.uniprot.org/annotation/VAR_057200|||http://purl.uniprot.org/annotation/VAR_057201
http://togogenome.org/gene/9606:TRNAU1AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||RRM 1|||RRM 2|||tRNA selenocysteine 1-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304917|||http://purl.uniprot.org/annotation/VSP_028130
http://togogenome.org/gene/9606:EHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZN4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Complete loss of localization to CAV1 positive caveolae.|||Disordered|||Distorded caveolae.|||Dynamin-type G|||EF-hand|||EH|||EH domain-containing protein 2|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||In isoform 2.|||Incapable of binding membranes and localizing to caveolae.|||KPF loop; caveolar targeting|||Lowers the level of CAV1; distorded caveolae.|||Mediates membrane-binding|||No effect on caveolae targeting.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146111|||http://purl.uniprot.org/annotation/VAR_033917|||http://purl.uniprot.org/annotation/VSP_056212
http://togogenome.org/gene/9606:TMEM201                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SNT2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes localization to the nuclear envelopee; abolishes its localization to the nuclear envelope; impairs localization of SUN1 and EMD to the nuclear envelope.|||Disordered|||Helical|||Impairs organization of the nuclear envelope; abolishes its localization to the nuclear envelope; impairs localization of SUN1 and EMD to the nuclear envelope.|||In isoform 2.|||N-acetylmethionine|||Nuclear|||Perinuclear space|||Phosphoserine|||Transmembrane protein 201                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317198|||http://purl.uniprot.org/annotation/VSP_030915|||http://purl.uniprot.org/annotation/VSP_030916
http://togogenome.org/gene/9606:CCNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4M5|||http://purl.uniprot.org/uniprot/O60563                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylhistidine|||ADP-ribosylserine|||Basic and acidic residues|||Basic residues|||Cyclin-T1|||Cyclin-like|||Disordered|||Essential for interacting with HIV-1 Tat|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histidine-rich domain (HRD)|||In isoform 2.|||In mutant 9A; impaired formation of phase-separated liquid droplets, leading to decreased ability to activate CDK9.|||Loss of HIV-1 Tat transactivation.|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||Nuclear localization signal, and interaction with Tat-TAR RNA|||Phosphoserine|||Polar residues|||Pro residues|||Required for interaction with ZMYND8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080491|||http://purl.uniprot.org/annotation/VAR_053054|||http://purl.uniprot.org/annotation/VAR_069400|||http://purl.uniprot.org/annotation/VSP_054569|||http://purl.uniprot.org/annotation/VSP_054570
http://togogenome.org/gene/9606:SULT1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMM9|||http://purl.uniprot.org/uniprot/P0DMN0|||http://purl.uniprot.org/uniprot/Q1ET61                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases levels of sulfotransferase activity.|||Decreases levels of sulfotransferase activity; accelerates proteasome-dependent degradation.|||In isoform 2.|||In isoform 3.|||No effect on sulfotransferase activity.|||Proton acceptor|||Sulfotransferase|||Sulfotransferase 1A3|||Sulfotransferase 1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085159|||http://purl.uniprot.org/annotation/PRO_0000430204|||http://purl.uniprot.org/annotation/VAR_071108|||http://purl.uniprot.org/annotation/VAR_071109|||http://purl.uniprot.org/annotation/VAR_071110|||http://purl.uniprot.org/annotation/VAR_071111|||http://purl.uniprot.org/annotation/VAR_071112|||http://purl.uniprot.org/annotation/VAR_071113|||http://purl.uniprot.org/annotation/VAR_071114|||http://purl.uniprot.org/annotation/VAR_071115|||http://purl.uniprot.org/annotation/VSP_012326|||http://purl.uniprot.org/annotation/VSP_047771
http://togogenome.org/gene/9606:WFDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEX5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Protein WFDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041385|||http://purl.uniprot.org/annotation/VAR_021911
http://togogenome.org/gene/9606:CNPPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV87                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein CNPPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089352|||http://purl.uniprot.org/annotation/VAR_022825|||http://purl.uniprot.org/annotation/VAR_024298|||http://purl.uniprot.org/annotation/VAR_024299|||http://purl.uniprot.org/annotation/VAR_024300|||http://purl.uniprot.org/annotation/VAR_056769
http://togogenome.org/gene/9606:MAGEB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15481                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||Disordered|||MAGE|||Melanoma-associated antigen B4|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156715
http://togogenome.org/gene/9606:SV2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT41|||http://purl.uniprot.org/uniprot/Q496J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) C.botulinum neurotoxin type A-binding|||Basic and acidic residues|||Cytoplasmic|||Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/AHC.|||Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/AHC. Greater reduction in weight; when associated with Q-565.|||Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.|||Disordered|||Extracellular|||Helical|||Interaction with SYT1|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/AHC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/AHC.|||No longer interacts with BoNT/AHC.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Synaptic vesicle glycoprotein 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239771|||http://purl.uniprot.org/annotation/VAR_050303|||http://purl.uniprot.org/annotation/VAR_050304
http://togogenome.org/gene/9606:RABL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYI8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In PNCA5; associated with disease susceptibility.|||In PNCA5; associated with disease susceptibility; increased KRAS signaling and cell proliferation; increased interaction with RAP1GDS1; increased KRAS prenylation.|||Rab-like protein 3|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312166|||http://purl.uniprot.org/annotation/VAR_083453|||http://purl.uniprot.org/annotation/VAR_083454
http://togogenome.org/gene/9606:ASCL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ33                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Achaete-scute homolog 3|||Basic motif|||Helix-loop-helix motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127133|||http://purl.uniprot.org/annotation/VAR_055948
http://togogenome.org/gene/9606:LYRM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NU23                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  LYR motif-containing protein 2|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251175|||http://purl.uniprot.org/annotation/VAR_034099|||http://purl.uniprot.org/annotation/VAR_050417|||http://purl.uniprot.org/annotation/VAR_050418
http://togogenome.org/gene/9606:TAAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RJ0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070141|||http://purl.uniprot.org/annotation/VAR_049445|||http://purl.uniprot.org/annotation/VAR_049446
http://togogenome.org/gene/9606:GAPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N292                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with GRB2.|||Disordered|||Helical|||Protein GAPT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271123|||http://purl.uniprot.org/annotation/VAR_033673
http://togogenome.org/gene/9606:TMEM67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JHI2|||http://purl.uniprot.org/uniprot/Q5HYA8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cysteine-rich|||Cytoplasmic|||Decreased function in non-canonical Wnt signaling activation. When expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A.|||Discontinuously helical; Name=4|||Discontinuously helical; Name=5|||Discontinuously helical; Name=6|||Does not affect Wnt signaling regulation; when expressed in TMEM67-null cells it induces ROR2 phosphorylation upon stimulation by WNT5A.|||Does not affect function in non-canonical Wnt signaling activation. When expressed in TMEM67-null cells it induces ROR2 phosphorylation upon stimulation by WNT5A.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4A|||Helical; Name=4B|||Helical; Name=5A|||Helical; Name=5B|||Helical; Name=6A|||Helical; Name=6B|||Helical; Name=7|||In COACH1 and JBTS6.|||In COACH1 and JBTS6; found in a patient with Joubert syndrome that also carries mutation 1329-R--S-1332 Del in KIF7.|||In COACH1 and MKS3; loss of interaction with WNT5A.|||In COACH1.|||In COACH1; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A.|||In COACH1; does not affect protein abundance; fails to rescue the hydrocephalus phenotype in a zebrafish model.|||In COACH1; unknown pathological significance.|||In JBTS6, MKS3 and COACH1.|||In JBTS6, MKS3 and RHYNS.|||In JBTS6.|||In JBTS6; unknown pathological significance.|||In MKS3 and COACH1; loss of interaction with WNT5A; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling.|||In MKS3, COACH1 and NPHP11; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling.|||In MKS3, JBTS6 and COACH1; loss of interaction with WNT5A.|||In MKS3.|||In MKS3; affects Wnt signaling regulation; when expressed in TMEM67-null cells does not rescue increased canonical Wnt signaling.|||In MKS3; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A.|||In MKS3; leads to endoplasmic reticulum retention and prevents localization at the cell membrane; decreased function in non-canonical Wnt signaling activation; when expressed in TMEM67-null cells does not induce ROR2 phosphorylation upon stimulation by WNT5A; loss of interaction with WNT5A.|||In MKS3; unknown pathological significance.|||In NPHP11.|||In RHYNS; may result in exon 13 skipping.|||Is a modifier of Bardet-Biedl syndrome; found in a BBS14 patient also carrying a homozygous truncating mutation of the CEP290 gene.|||Meckelin|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in Joubert syndrome-related disorder.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225689|||http://purl.uniprot.org/annotation/PRO_5032361047|||http://purl.uniprot.org/annotation/VAR_025474|||http://purl.uniprot.org/annotation/VAR_025475|||http://purl.uniprot.org/annotation/VAR_031987|||http://purl.uniprot.org/annotation/VAR_031988|||http://purl.uniprot.org/annotation/VAR_062310|||http://purl.uniprot.org/annotation/VAR_062311|||http://purl.uniprot.org/annotation/VAR_062312|||http://purl.uniprot.org/annotation/VAR_062313|||http://purl.uniprot.org/annotation/VAR_062314|||http://purl.uniprot.org/annotation/VAR_062315|||http://purl.uniprot.org/annotation/VAR_062316|||http://purl.uniprot.org/annotation/VAR_062317|||http://purl.uniprot.org/annotation/VAR_062318|||http://purl.uniprot.org/annotation/VAR_062319|||http://purl.uniprot.org/annotation/VAR_062320|||http://purl.uniprot.org/annotation/VAR_063783|||http://purl.uniprot.org/annotation/VAR_063784|||http://purl.uniprot.org/annotation/VAR_063785|||http://purl.uniprot.org/annotation/VAR_063786|||http://purl.uniprot.org/annotation/VAR_063787|||http://purl.uniprot.org/annotation/VAR_063788|||http://purl.uniprot.org/annotation/VAR_063789|||http://purl.uniprot.org/annotation/VAR_063790|||http://purl.uniprot.org/annotation/VAR_063791|||http://purl.uniprot.org/annotation/VAR_063792|||http://purl.uniprot.org/annotation/VAR_063793|||http://purl.uniprot.org/annotation/VAR_063794|||http://purl.uniprot.org/annotation/VAR_063795|||http://purl.uniprot.org/annotation/VAR_063796|||http://purl.uniprot.org/annotation/VAR_063797|||http://purl.uniprot.org/annotation/VAR_063798|||http://purl.uniprot.org/annotation/VAR_063799|||http://purl.uniprot.org/annotation/VAR_063800|||http://purl.uniprot.org/annotation/VAR_063801|||http://purl.uniprot.org/annotation/VAR_063802|||http://purl.uniprot.org/annotation/VAR_063803|||http://purl.uniprot.org/annotation/VAR_064185|||http://purl.uniprot.org/annotation/VAR_064186|||http://purl.uniprot.org/annotation/VAR_064187|||http://purl.uniprot.org/annotation/VAR_075699|||http://purl.uniprot.org/annotation/VAR_076871|||http://purl.uniprot.org/annotation/VAR_076872|||http://purl.uniprot.org/annotation/VAR_076873|||http://purl.uniprot.org/annotation/VAR_076874|||http://purl.uniprot.org/annotation/VAR_076875|||http://purl.uniprot.org/annotation/VAR_076876|||http://purl.uniprot.org/annotation/VAR_076877|||http://purl.uniprot.org/annotation/VAR_076878|||http://purl.uniprot.org/annotation/VAR_076879|||http://purl.uniprot.org/annotation/VAR_076880|||http://purl.uniprot.org/annotation/VAR_079632|||http://purl.uniprot.org/annotation/VAR_081741|||http://purl.uniprot.org/annotation/VAR_081742|||http://purl.uniprot.org/annotation/VAR_081743|||http://purl.uniprot.org/annotation/VAR_081744|||http://purl.uniprot.org/annotation/VAR_087308|||http://purl.uniprot.org/annotation/VAR_087309|||http://purl.uniprot.org/annotation/VAR_087310
http://togogenome.org/gene/9606:AJAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKB5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adherens junction-associated protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||No effect on membrane localization.|||Polar residues|||Predominantly localized to the apical membrane.|||Targeting signals                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284801|||http://purl.uniprot.org/annotation/VAR_031821
http://togogenome.org/gene/9606:SACS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIQ1|||http://purl.uniprot.org/uniprot/Q9NZJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with spastic paraplegia; unknown pathological significance.|||HEPN|||In SACS.|||In SACS; associated with P-556.|||In SACS; associated with Q-2798.|||In SACS; associated with Q-3636.|||In SACS; associated with T-3652.|||In SACS; atypical phenotype without spasticity or hyperreflexia.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||J|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in non-ataxic spastic paraplegia with peripheral neuropathy.|||Sacsin|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097563|||http://purl.uniprot.org/annotation/VAR_010296|||http://purl.uniprot.org/annotation/VAR_035986|||http://purl.uniprot.org/annotation/VAR_059716|||http://purl.uniprot.org/annotation/VAR_059717|||http://purl.uniprot.org/annotation/VAR_059718|||http://purl.uniprot.org/annotation/VAR_059719|||http://purl.uniprot.org/annotation/VAR_059720|||http://purl.uniprot.org/annotation/VAR_059721|||http://purl.uniprot.org/annotation/VAR_064801|||http://purl.uniprot.org/annotation/VAR_064802|||http://purl.uniprot.org/annotation/VAR_064803|||http://purl.uniprot.org/annotation/VAR_064804|||http://purl.uniprot.org/annotation/VAR_064805|||http://purl.uniprot.org/annotation/VAR_064806|||http://purl.uniprot.org/annotation/VAR_064807|||http://purl.uniprot.org/annotation/VAR_064808|||http://purl.uniprot.org/annotation/VAR_064809|||http://purl.uniprot.org/annotation/VAR_064810|||http://purl.uniprot.org/annotation/VAR_064811|||http://purl.uniprot.org/annotation/VAR_064812|||http://purl.uniprot.org/annotation/VAR_064813|||http://purl.uniprot.org/annotation/VAR_064814|||http://purl.uniprot.org/annotation/VAR_064815|||http://purl.uniprot.org/annotation/VAR_064816|||http://purl.uniprot.org/annotation/VAR_064817|||http://purl.uniprot.org/annotation/VAR_064818|||http://purl.uniprot.org/annotation/VAR_064819|||http://purl.uniprot.org/annotation/VAR_064820|||http://purl.uniprot.org/annotation/VAR_064821|||http://purl.uniprot.org/annotation/VAR_064822|||http://purl.uniprot.org/annotation/VAR_064823|||http://purl.uniprot.org/annotation/VAR_064824|||http://purl.uniprot.org/annotation/VAR_064825|||http://purl.uniprot.org/annotation/VAR_064826|||http://purl.uniprot.org/annotation/VAR_069775|||http://purl.uniprot.org/annotation/VAR_076760|||http://purl.uniprot.org/annotation/VAR_083891|||http://purl.uniprot.org/annotation/VSP_022325
http://togogenome.org/gene/9606:FAM76B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GX09|||http://purl.uniprot.org/uniprot/Q5HYJ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM76B|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245763|||http://purl.uniprot.org/annotation/VSP_022679|||http://purl.uniprot.org/annotation/VSP_022680|||http://purl.uniprot.org/annotation/VSP_057354
http://togogenome.org/gene/9606:HCAR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49019                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abrogates completely the activation by OH-octanoid acid.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hydroxycarboxylic acid receptor 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069604|||http://purl.uniprot.org/annotation/VAR_038715|||http://purl.uniprot.org/annotation/VAR_038716|||http://purl.uniprot.org/annotation/VAR_038717|||http://purl.uniprot.org/annotation/VAR_038718|||http://purl.uniprot.org/annotation/VAR_038719|||http://purl.uniprot.org/annotation/VAR_038720
http://togogenome.org/gene/9606:OSR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2R0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||Disordered|||In isoform 2.|||In isoform 3.|||Protein odd-skipped-related 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047007|||http://purl.uniprot.org/annotation/VSP_017121|||http://purl.uniprot.org/annotation/VSP_054849
http://togogenome.org/gene/9606:PLCD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRC7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4|||Abolishes binding to GNAI3.|||Abolishes binding to and activation of GNAI3.|||Acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||GBA|||In isoform 2.|||Marked but incomplete decrease in GNAI3 binding and reduced activation of G-protein signaling.|||PDZ-binding|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Substrate binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306824|||http://purl.uniprot.org/annotation/VSP_028501|||http://purl.uniprot.org/annotation/VSP_028502
http://togogenome.org/gene/9606:PLA2G12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX93                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Group XIIB secretory phospholipase A2-like protein|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022772|||http://purl.uniprot.org/annotation/VSP_054398
http://togogenome.org/gene/9606:FTMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4E7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Ferritin, mitochondrial|||Ferritin-like diiron|||Increases ferroxidase activity and iron binding.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008850
http://togogenome.org/gene/9606:MEIOSIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JSJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif; degenerate|||Disordered|||HMG box|||Helix-loop-helix motif|||Meiosis initiator protein|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000430831
http://togogenome.org/gene/9606:TCF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4LBB6|||http://purl.uniprot.org/uniprot/Q12870|||http://purl.uniprot.org/uniprot/Q6NVX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||Transcription factor 15|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127460
http://togogenome.org/gene/9606:DEK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35659                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylserine|||Acidic residues|||Basic and acidic residues|||DEK-C|||Disordered|||In isoform 2.|||N-acetylserine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Phosphothreonine; by CK2|||Protein DEK|||Removed|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079858|||http://purl.uniprot.org/annotation/VAR_050949|||http://purl.uniprot.org/annotation/VSP_042951
http://togogenome.org/gene/9606:WEE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30291|||http://purl.uniprot.org/uniprot/Q86V29                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity.|||Abolishes phosphorylation by BRSK1 and BRSK2.|||Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-123.|||Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-53.|||Acidic residues|||Basic and acidic residues|||Disordered|||Impairs binding of the SCF(BTRC) complex.|||In isoform 2.|||Phosphoserine|||Phosphoserine; by BRSK1 and BRSK2|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor|||Wee1-like protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086810|||http://purl.uniprot.org/annotation/VAR_041302|||http://purl.uniprot.org/annotation/VAR_041303|||http://purl.uniprot.org/annotation/VSP_044959
http://togogenome.org/gene/9606:BARX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein BarH-like 2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048838
http://togogenome.org/gene/9606:SNTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y5T2|||http://purl.uniprot.org/uniprot/B2RA84|||http://purl.uniprot.org/uniprot/Q9NSN8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Gamma-1-syntrophin|||In isoform 2.|||PDZ|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184013|||http://purl.uniprot.org/annotation/VSP_006360
http://togogenome.org/gene/9606:PNMA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U5Z3|||http://purl.uniprot.org/uniprot/Q9UL42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylalanine|||Paraneoplastic antigen Ma2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155202|||http://purl.uniprot.org/annotation/VAR_053597
http://togogenome.org/gene/9606:TMA16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EY4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylserine|||Disordered|||Translation machinery-associated protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321559|||http://purl.uniprot.org/annotation/VAR_039349|||http://purl.uniprot.org/annotation/VAR_039350|||http://purl.uniprot.org/annotation/VAR_054013
http://togogenome.org/gene/9606:ERG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG41|||http://purl.uniprot.org/uniprot/B4DN83|||http://purl.uniprot.org/uniprot/B4DVX5|||http://purl.uniprot.org/uniprot/B5MDW0|||http://purl.uniprot.org/uniprot/P11308                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form ELF4-ERG oncogene|||Disordered|||ETS|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||PNT|||Phosphoserine|||Polar residues|||Transcriptional regulator ERG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204103|||http://purl.uniprot.org/annotation/VSP_060677|||http://purl.uniprot.org/annotation/VSP_060678|||http://purl.uniprot.org/annotation/VSP_060679|||http://purl.uniprot.org/annotation/VSP_060680|||http://purl.uniprot.org/annotation/VSP_060681|||http://purl.uniprot.org/annotation/VSP_060682|||http://purl.uniprot.org/annotation/VSP_060683
http://togogenome.org/gene/9606:ZNF789                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FWF6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 789                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293697|||http://purl.uniprot.org/annotation/VAR_052903|||http://purl.uniprot.org/annotation/VSP_026561|||http://purl.uniprot.org/annotation/VSP_046816|||http://purl.uniprot.org/annotation/VSP_046817
http://togogenome.org/gene/9606:CCDC179                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BU77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 179|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421698
http://togogenome.org/gene/9606:TMEM50A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5M7|||http://purl.uniprot.org/uniprot/O95807|||http://purl.uniprot.org/uniprot/Q7RU07                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylserine|||Phosphoserine|||Removed|||Transmembrane protein 50A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174181|||http://purl.uniprot.org/annotation/VAR_007851|||http://purl.uniprot.org/annotation/VAR_013121
http://togogenome.org/gene/9606:SLC27A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5K4L6|||http://purl.uniprot.org/uniprot/X6R3N0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Long-chain fatty acid transport protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193207|||http://purl.uniprot.org/annotation/VAR_048241|||http://purl.uniprot.org/annotation/VAR_048242|||http://purl.uniprot.org/annotation/VSP_016218|||http://purl.uniprot.org/annotation/VSP_036534|||http://purl.uniprot.org/annotation/VSP_036535
http://togogenome.org/gene/9606:NELL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z625|||http://purl.uniprot.org/uniprot/Q99435                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protein kinase C-binding protein NELL2|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007666|||http://purl.uniprot.org/annotation/VAR_048987|||http://purl.uniprot.org/annotation/VAR_048988|||http://purl.uniprot.org/annotation/VAR_048989|||http://purl.uniprot.org/annotation/VSP_043801|||http://purl.uniprot.org/annotation/VSP_043802|||http://purl.uniprot.org/annotation/VSP_043869
http://togogenome.org/gene/9606:DIPK2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7Y0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Divergent protein kinase domain 2B|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019568|||http://purl.uniprot.org/annotation/VAR_047103|||http://purl.uniprot.org/annotation/VAR_047104|||http://purl.uniprot.org/annotation/VSP_035633|||http://purl.uniprot.org/annotation/VSP_035634
http://togogenome.org/gene/9606:IL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40933                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform IL15-S21AA.|||Interleukin-15|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015393|||http://purl.uniprot.org/annotation/PRO_0000015394|||http://purl.uniprot.org/annotation/VSP_002660
http://togogenome.org/gene/9606:SERPINI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z455|||http://purl.uniprot.org/uniprot/Q99574                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  In FENIB; Portland.|||In FENIB; Syracuse; decreased protein stability; decreased proteinase inhibitor activity; increased tendency to form polymers.|||Increases protein stability and abolishes tendency to form polymers. No effect on inhibitory activity.|||Increases protein stability and decreases tendency to form polymers. No effect on inhibitory activity.|||N-linked (GlcNAc...) asparagine|||Neuroserpin|||O-linked (Xyl...) (chondroitin sulfate) serine|||Reactive bond|||Serpin|||Slightly decreases inhibitory activity. No effect on thermal stability.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032521|||http://purl.uniprot.org/annotation/PRO_5006608245|||http://purl.uniprot.org/annotation/VAR_008520|||http://purl.uniprot.org/annotation/VAR_008521
http://togogenome.org/gene/9606:CCDC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKY2|||http://purl.uniprot.org/uniprot/Q96M83                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 7|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089399|||http://purl.uniprot.org/annotation/VAR_024308|||http://purl.uniprot.org/annotation/VAR_033692|||http://purl.uniprot.org/annotation/VAR_033693|||http://purl.uniprot.org/annotation/VAR_050766|||http://purl.uniprot.org/annotation/VAR_061586|||http://purl.uniprot.org/annotation/VSP_010525|||http://purl.uniprot.org/annotation/VSP_010526|||http://purl.uniprot.org/annotation/VSP_058366|||http://purl.uniprot.org/annotation/VSP_058367|||http://purl.uniprot.org/annotation/VSP_058368|||http://purl.uniprot.org/annotation/VSP_058369|||http://purl.uniprot.org/annotation/VSP_058370|||http://purl.uniprot.org/annotation/VSP_058371
http://togogenome.org/gene/9606:TCEAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKK0|||http://purl.uniprot.org/uniprot/Q96EI5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Transcription elongation factor A protein-like 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239209|||http://purl.uniprot.org/annotation/VSP_019109
http://togogenome.org/gene/9606:REST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQA1|||http://purl.uniprot.org/uniprot/Q13127                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Does not change transcriptional repression activity.|||In GINGF5.|||In WT6.|||In WT6; inhibits transcriptional repression activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibits transcriptional repression activity.|||Interaction with RCOR1|||Interaction with SIN3A|||Interaction with SIN3B|||Interaction with ZFP90|||Lack of deubiquitination by USP7.|||Loss of interaction with BTRC.|||Loss of interaction with BTRC. Reduced ubiquitination. Decreased proteasomal degradation in G2. Decreased average time from nuclear envelope breakdown to anaphase onset. Increased number of lagging chromosomes and chromosome bridges in anaphase and prematurely separated sister chromatids. Reduced MAD2 levels.|||No effect on nuclear localization.|||No impact on deubiquitination by USP7.|||Phosphoserine|||Polar residues|||RE1-silencing transcription factor|||Reduced nuclear localization.|||Required for binding to the neuron-restrictive silencer element                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269547|||http://purl.uniprot.org/annotation/VAR_029795|||http://purl.uniprot.org/annotation/VAR_029796|||http://purl.uniprot.org/annotation/VAR_029797|||http://purl.uniprot.org/annotation/VAR_029798|||http://purl.uniprot.org/annotation/VAR_076333|||http://purl.uniprot.org/annotation/VAR_076334|||http://purl.uniprot.org/annotation/VAR_076335|||http://purl.uniprot.org/annotation/VAR_076336|||http://purl.uniprot.org/annotation/VAR_079529|||http://purl.uniprot.org/annotation/VSP_022064|||http://purl.uniprot.org/annotation/VSP_022065|||http://purl.uniprot.org/annotation/VSP_022066|||http://purl.uniprot.org/annotation/VSP_022067|||http://purl.uniprot.org/annotation/VSP_022068
http://togogenome.org/gene/9606:MSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26038|||http://purl.uniprot.org/uniprot/V9HWC0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by STK10.|||Basic and acidic residues|||Completely abolishes the interaction between N- and C-terminal domains.|||Disordered|||FERM|||Impairs phosphorylation by STK10.|||In IMD50; decreased protein abundance in T cell; loss of T cell proliferation after T cell activation; does not affect immunologic synapses formation; decreased T cell migration in response to activation by chemokines; increased T cell adhesion in response to activation by integrins.|||Inhibits S-nitrosylation of Cys-117; when associated with M-115.|||Inhibits S-nitrosylation of Cys-117; when associated with M-120.|||Moesin|||N6-acetyllysine|||N6-succinyllysine|||Phosphomimetic mutant.|||Phosphoserine|||Phosphothreonine; by ROCK2 and STK10|||Phosphotyrosine|||Removed|||S-nitrosocysteine|||[IL]-x-C-x-x-[DE] motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219416|||http://purl.uniprot.org/annotation/VAR_078026
http://togogenome.org/gene/9606:ADGRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60242                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor B3|||CUB|||Cytoplasmic|||Extracellular|||GPS|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012865|||http://purl.uniprot.org/annotation/VAR_046525|||http://purl.uniprot.org/annotation/VSP_056939
http://togogenome.org/gene/9606:KRT24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2I5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 24|||Linker 1|||Linker 12|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314850|||http://purl.uniprot.org/annotation/VAR_038068|||http://purl.uniprot.org/annotation/VAR_038069|||http://purl.uniprot.org/annotation/VAR_038070|||http://purl.uniprot.org/annotation/VAR_038071|||http://purl.uniprot.org/annotation/VAR_038072|||http://purl.uniprot.org/annotation/VAR_038073|||http://purl.uniprot.org/annotation/VAR_038074
http://togogenome.org/gene/9606:WIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5W5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||N-linked (GlcNAc...) asparagine|||WIF|||Wnt inhibitory factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007775
http://togogenome.org/gene/9606:SNX14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJ91|||http://purl.uniprot.org/uniprot/Q9Y5W7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||In SCAR20.|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||PX|||PXA|||Phosphoserine|||RGS|||Sorting nexin-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213861|||http://purl.uniprot.org/annotation/VAR_083399|||http://purl.uniprot.org/annotation/VSP_037775|||http://purl.uniprot.org/annotation/VSP_037776|||http://purl.uniprot.org/annotation/VSP_037777
http://togogenome.org/gene/9606:GNAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3H8|||http://purl.uniprot.org/uniprot/A0A0S2Z3S5|||http://purl.uniprot.org/uniprot/A0A7I2V5R6|||http://purl.uniprot.org/uniprot/B0AZR9|||http://purl.uniprot.org/uniprot/O95467|||http://purl.uniprot.org/uniprot/P63092|||http://purl.uniprot.org/uniprot/P84996|||http://purl.uniprot.org/uniprot/Q14455|||http://purl.uniprot.org/uniprot/Q5FWY2|||http://purl.uniprot.org/uniprot/Q5JWD1|||http://purl.uniprot.org/uniprot/Q5JWF2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||Acidic residues|||Basic and acidic residues|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GPIPIRRH peptide|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas|||Guanine nucleotide-binding protein G(s) subunit alpha isoforms short|||In AHO.|||In AHO/PHP1A.|||In AHO; defective GDP binding resulting in increased thermolability and decreased activation.|||In AHO; impairs the ability to mediate hormonal stimulation.|||In AHO; may alter guanine nucleotide binding which could lead to thermolability and impaired function.|||In AHO; uncouples receptors from adenylyl cyclases.|||In AIMAH1; also found in pituitary tumor and polyostotic fibrous dysplasia.|||In GNAS hyperfunction.|||In GNASHYP.|||In MAS and AIMAH1; also found in somatotrophinoma.|||In MAS.|||In MAS; also found in somatotrophinoma.|||In PHP1A.|||In PHP1A; the patient also shows testotoxicosis; constitutively activates adenylyl cyclase in vitro; rapidly degraded at 37 degrees resulting in loss of Gs activity.|||In PHP1C; significantly reduces receptor-mediated activation; displays normal receptor-independent activation.|||In POH.|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform Gnas-2.|||In isoform XLas-2.|||In isoform XLas-3.|||In non-MAS endocrine tumors.|||In pituitary adenomas; also found in a patient with severe Cushing syndrome.|||In somatotrophinoma.|||Increases GDP release and impairs receptor-mediated activation; markedly elevated intrinsic GTPase rate which will lead to more rapid inactivation.|||Increases GDP release but does not affect receptor-mediated activation.|||Increases binding to GAS2L2; when associated with L-227.|||Increases binding to GAS2L2; when associated with N-295.|||LHAL tetrapeptide|||N-palmitoyl glycine|||Neuroendocrine secretory protein 55|||Phosphoserine|||Polar residues|||Pro residues|||Protein ALEX|||Removed|||S-palmitoyl cysteine|||Unable to interact with the receptor for PTH.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203721|||http://purl.uniprot.org/annotation/PRO_0000253964|||http://purl.uniprot.org/annotation/PRO_0000253967|||http://purl.uniprot.org/annotation/PRO_0000253968|||http://purl.uniprot.org/annotation/PRO_0000253969|||http://purl.uniprot.org/annotation/PRO_0000253984|||http://purl.uniprot.org/annotation/VAR_003439|||http://purl.uniprot.org/annotation/VAR_003440|||http://purl.uniprot.org/annotation/VAR_003441|||http://purl.uniprot.org/annotation/VAR_003442|||http://purl.uniprot.org/annotation/VAR_003443|||http://purl.uniprot.org/annotation/VAR_003444|||http://purl.uniprot.org/annotation/VAR_015388|||http://purl.uniprot.org/annotation/VAR_017843|||http://purl.uniprot.org/annotation/VAR_017844|||http://purl.uniprot.org/annotation/VAR_017845|||http://purl.uniprot.org/annotation/VAR_017846|||http://purl.uniprot.org/annotation/VAR_017847|||http://purl.uniprot.org/annotation/VAR_017848|||http://purl.uniprot.org/annotation/VAR_017849|||http://purl.uniprot.org/annotation/VAR_017850|||http://purl.uniprot.org/annotation/VAR_028774|||http://purl.uniprot.org/annotation/VAR_028775|||http://purl.uniprot.org/annotation/VAR_028776|||http://purl.uniprot.org/annotation/VAR_028777|||http://purl.uniprot.org/annotation/VAR_028778|||http://purl.uniprot.org/annotation/VAR_028779|||http://purl.uniprot.org/annotation/VAR_031872|||http://purl.uniprot.org/annotation/VAR_031873|||http://purl.uniprot.org/annotation/VAR_031874|||http://purl.uniprot.org/annotation/VAR_031875|||http://purl.uniprot.org/annotation/VAR_031876|||http://purl.uniprot.org/annotation/VAR_031877|||http://purl.uniprot.org/annotation/VAR_031878|||http://purl.uniprot.org/annotation/VAR_031879|||http://purl.uniprot.org/annotation/VAR_031880|||http://purl.uniprot.org/annotation/VAR_031881|||http://purl.uniprot.org/annotation/VAR_034744|||http://purl.uniprot.org/annotation/VAR_035788|||http://purl.uniprot.org/annotation/VAR_035789|||http://purl.uniprot.org/annotation/VAR_049358|||http://purl.uniprot.org/annotation/VAR_059656|||http://purl.uniprot.org/annotation/VAR_066387|||http://purl.uniprot.org/annotation/VAR_066388|||http://purl.uniprot.org/annotation/VSP_001833|||http://purl.uniprot.org/annotation/VSP_001834|||http://purl.uniprot.org/annotation/VSP_026616|||http://purl.uniprot.org/annotation/VSP_026617|||http://purl.uniprot.org/annotation/VSP_047325|||http://purl.uniprot.org/annotation/VSP_052173|||http://purl.uniprot.org/annotation/VSP_052174|||http://purl.uniprot.org/annotation/VSP_052175
http://togogenome.org/gene/9606:CLXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAE3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Calaxin|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251969|||http://purl.uniprot.org/annotation/VSP_041330|||http://purl.uniprot.org/annotation/VSP_041331
http://togogenome.org/gene/9606:TRDMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14717|||http://purl.uniprot.org/uniprot/Q6ICS7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||SAM-dependent MTase C5-type|||tRNA (cytosine(38)-C(5))-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088040|||http://purl.uniprot.org/annotation/VAR_051961|||http://purl.uniprot.org/annotation/VSP_005628|||http://purl.uniprot.org/annotation/VSP_005629|||http://purl.uniprot.org/annotation/VSP_005630|||http://purl.uniprot.org/annotation/VSP_005631|||http://purl.uniprot.org/annotation/VSP_005632|||http://purl.uniprot.org/annotation/VSP_005633|||http://purl.uniprot.org/annotation/VSP_005634|||http://purl.uniprot.org/annotation/VSP_005635
http://togogenome.org/gene/9606:AKAP17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02040|||http://purl.uniprot.org/uniprot/Q05DA9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein 17A|||Abolishes binding to PKA-RI; when associated with 438-P-P-439.|||Abolishes binding to PKA-RI; when associated with 445-P-P-446.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||PKA-RI and PKA-RII subunit binding domain|||PKA-RI-alpha subunit binding domain|||Phosphoserine|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022692|||http://purl.uniprot.org/annotation/VAR_055353|||http://purl.uniprot.org/annotation/VSP_004490|||http://purl.uniprot.org/annotation/VSP_004491|||http://purl.uniprot.org/annotation/VSP_024947|||http://purl.uniprot.org/annotation/VSP_024948
http://togogenome.org/gene/9606:GTF3C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||General transcription factor 3C polypeptide 2|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050985|||http://purl.uniprot.org/annotation/VSP_010566|||http://purl.uniprot.org/annotation/VSP_010567
http://togogenome.org/gene/9606:FLI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01543                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ETS|||Friend leukemia integration 1 transcription factor|||In BDPLT21; decreased function in positive regulation of DNA-templated transcription.|||In BDPLT21; loss of function in positive regulation of DNA-templated transcription.|||In BDPLT21; loss of function in positive regulation of DNA-templated transcription; decreased localization to nucleus; no effect on protein abundance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PNT|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204124|||http://purl.uniprot.org/annotation/VAR_078929|||http://purl.uniprot.org/annotation/VAR_078930|||http://purl.uniprot.org/annotation/VAR_078931|||http://purl.uniprot.org/annotation/VAR_078932|||http://purl.uniprot.org/annotation/VAR_078933|||http://purl.uniprot.org/annotation/VSP_001478|||http://purl.uniprot.org/annotation/VSP_045276|||http://purl.uniprot.org/annotation/VSP_046943
http://togogenome.org/gene/9606:PRIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49642                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes NTP binding.|||Abolishes NTP binding. Loss of primase activity.|||DNA primase small subunit|||Decreases primase activity.|||Decreases the binding affinity for NTPs.|||Decreases the binding affinity for NTPs. Loss of primase activity.|||Disordered|||In PDIL; loss of function in DNA replication initiation; contrary to the wild type, the mutant does not rescue reduced cell proliferation, prolonged S-phase and impaired DNA replication when transfected in patient cells.|||Loss of primase activity.|||N-acetylmethionine|||Slightly decreases primase activity.|||Strongly decreases primase activity, which can be partially rescued by increasing primase concentration.|||Zinc knuckle motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046730|||http://purl.uniprot.org/annotation/VAR_021898|||http://purl.uniprot.org/annotation/VAR_087657
http://togogenome.org/gene/9606:WDR11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZH6                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  In HH14; abolishes the interaction with EMX1; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; decreases GLI3 protein levels.|||In HH14; abolishes the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; decreases GLI3 protein levels.|||In HH14; does not affect the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels.|||In HH14; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels.|||In HH14; mild phenotype; decreases capacity to shuttle from cilium to nucleus; decreases interaction with EMX1; no effect on GLI3 protein levels.|||In HH14; reduces the interaction with EMX1; does not affect the subcellular location of the protein; decreases capacity to shuttle from cilium to nucleus; decreases GLI3 protein levels.|||In MRT78; no protein detected in homozygous patient cells.|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050889|||http://purl.uniprot.org/annotation/VAR_069194|||http://purl.uniprot.org/annotation/VAR_069195|||http://purl.uniprot.org/annotation/VAR_069196|||http://purl.uniprot.org/annotation/VAR_069197|||http://purl.uniprot.org/annotation/VAR_069198|||http://purl.uniprot.org/annotation/VAR_069199|||http://purl.uniprot.org/annotation/VAR_080856|||http://purl.uniprot.org/annotation/VAR_088097
http://togogenome.org/gene/9606:SART1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43290                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||U4/U6.U5 tri-snRNP-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223308|||http://purl.uniprot.org/annotation/VAR_025319|||http://purl.uniprot.org/annotation/VAR_034504|||http://purl.uniprot.org/annotation/VAR_051367
http://togogenome.org/gene/9606:HRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04196                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cleavage; by plasmin|||Cystatin 1|||Cystatin 2|||Disordered|||Histidine-rich glycoprotein|||In THPH11; HRGTokushima 1; results in increased intracellular degradation and reduced protein secretion.|||In THPH11; HRGTokushima 2; results in increased intracellular degradation and reduced protein secretion.|||Interaction with ATP5F1A|||N-linked (GlcNAc...) asparagine|||Necessary for endothelial cell focal adhesions and anti-angiogenic activities|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006709|||http://purl.uniprot.org/annotation/VAR_014528|||http://purl.uniprot.org/annotation/VAR_020488|||http://purl.uniprot.org/annotation/VAR_020489|||http://purl.uniprot.org/annotation/VAR_022080|||http://purl.uniprot.org/annotation/VAR_024427|||http://purl.uniprot.org/annotation/VAR_024428|||http://purl.uniprot.org/annotation/VAR_024429|||http://purl.uniprot.org/annotation/VAR_048856|||http://purl.uniprot.org/annotation/VAR_063000|||http://purl.uniprot.org/annotation/VAR_063001
http://togogenome.org/gene/9606:RNF128                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEB7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase RNF128|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PA|||Polar residues|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261412|||http://purl.uniprot.org/annotation/VSP_021685
http://togogenome.org/gene/9606:CDK17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00537                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase 17|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086487|||http://purl.uniprot.org/annotation/VAR_064743|||http://purl.uniprot.org/annotation/VSP_043295
http://togogenome.org/gene/9606:TLDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||TLD domain-containing protein 2|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318690|||http://purl.uniprot.org/annotation/VAR_050439
http://togogenome.org/gene/9606:RFC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVY3|||http://purl.uniprot.org/uniprot/P35250|||http://purl.uniprot.org/uniprot/Q75MT5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Magnesium chelatase ChlI-like catalytic|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Replication factor C C-terminal|||Replication factor C subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121766|||http://purl.uniprot.org/annotation/VAR_023126|||http://purl.uniprot.org/annotation/VSP_005660
http://togogenome.org/gene/9606:DOT1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEK3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Basic and acidic residues|||Basic residues|||DOT1|||Disordered|||Histone-lysine N-methyltransferase, H3 lysine-79 specific|||In isoform 2.|||Loss of activity.|||No effect.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with nucleosomes and DNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186089|||http://purl.uniprot.org/annotation/VAR_014287|||http://purl.uniprot.org/annotation/VAR_014288|||http://purl.uniprot.org/annotation/VAR_014289|||http://purl.uniprot.org/annotation/VSP_059795
http://togogenome.org/gene/9606:BTG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14201|||http://purl.uniprot.org/uniprot/Q6IAU3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Anti-proliferative protein|||Disordered|||In isoform 2.|||Protein BTG3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143807|||http://purl.uniprot.org/annotation/VSP_000578
http://togogenome.org/gene/9606:DNAJB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6W7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||DnaJ homolog subfamily B member 7|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071027|||http://purl.uniprot.org/annotation/VAR_017779
http://togogenome.org/gene/9606:POLR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1W6|||http://purl.uniprot.org/uniprot/Q9H9Y6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase I subunit RPA2|||DNA-directed RNA polymerase subunit 2 hybrid-binding|||Disordered|||In TCS4.|||In TCS4; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||RNA polymerase Rpb2|||RNA polymerase beta subunit protrusion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048072|||http://purl.uniprot.org/annotation/VAR_034476|||http://purl.uniprot.org/annotation/VAR_071195|||http://purl.uniprot.org/annotation/VAR_084557|||http://purl.uniprot.org/annotation/VAR_084558|||http://purl.uniprot.org/annotation/VAR_084559|||http://purl.uniprot.org/annotation/VSP_017823|||http://purl.uniprot.org/annotation/VSP_056749|||http://purl.uniprot.org/annotation/VSP_056750|||http://purl.uniprot.org/annotation/VSP_056751
http://togogenome.org/gene/9606:GNG11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61952|||http://purl.uniprot.org/uniprot/Q53Y01                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Propeptide|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine methyl ester|||Disordered|||G protein gamma|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012659|||http://purl.uniprot.org/annotation/PRO_0000012660
http://togogenome.org/gene/9606:CREB3L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic motif|||Cleavage; by PS1|||Cyclic AMP-responsive element-binding protein 3-like protein 3|||Cytoplasmic|||Decreases proteolytic cleavage upon ER stress.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Signal-anchor for type II membrane protein|||In HYTG2; risk factor; loss of transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays.|||In HYTG2; risk factor; severely reduced transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays.|||In HYTG2; unknown pathological significance; no effect on transactivation activity in APOA4, APOC2 or FGF21 promoter-driven luciferase assays.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leucine-zipper|||Loss of ubiquitination by SYNV1/HRD1.|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Phosphoserine|||Polar residues|||Processed cyclic AMP-responsive element-binding protein 3-like protein 3|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288074|||http://purl.uniprot.org/annotation/PRO_0000296216|||http://purl.uniprot.org/annotation/VAR_085795|||http://purl.uniprot.org/annotation/VAR_085796|||http://purl.uniprot.org/annotation/VAR_085797|||http://purl.uniprot.org/annotation/VAR_085798|||http://purl.uniprot.org/annotation/VAR_085799|||http://purl.uniprot.org/annotation/VAR_085800|||http://purl.uniprot.org/annotation/VSP_025637|||http://purl.uniprot.org/annotation/VSP_054876|||http://purl.uniprot.org/annotation/VSP_055635|||http://purl.uniprot.org/annotation/VSP_055636
http://togogenome.org/gene/9606:TUBG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23258                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CDCBM4.|||In CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised.|||Phosphoserine; by BRSK1|||Tubulin gamma-1 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048465|||http://purl.uniprot.org/annotation/VAR_052674|||http://purl.uniprot.org/annotation/VAR_070577|||http://purl.uniprot.org/annotation/VAR_070578|||http://purl.uniprot.org/annotation/VAR_070579
http://togogenome.org/gene/9606:FAM25A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3EWG3|||http://purl.uniprot.org/uniprot/B3EWG5|||http://purl.uniprot.org/uniprot/B3EWG6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM25A|||Protein FAM25C|||Protein FAM25G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270919|||http://purl.uniprot.org/annotation/PRO_0000416047|||http://purl.uniprot.org/annotation/PRO_0000416048|||http://purl.uniprot.org/annotation/VAR_054062
http://togogenome.org/gene/9606:POLD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWF6|||http://purl.uniprot.org/uniprot/P49005                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA polymerase alpha/delta/epsilon subunit B|||DNA polymerase delta subunit 2|||DNA polymerase delta subunit OB-fold|||Loss of POLD3-binding in a yeast two-hybrid assay.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096166|||http://purl.uniprot.org/annotation/VAR_014885
http://togogenome.org/gene/9606:MRPS18B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0S7P4|||http://purl.uniprot.org/uniprot/Q9Y676                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Mitochondrion|||Phosphoserine|||Polar residues|||Small ribosomal subunit protein mS40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030627|||http://purl.uniprot.org/annotation/VAR_052056
http://togogenome.org/gene/9606:PLEKHG4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  DH|||Disordered|||PH|||Pleckstrin homology domain-containing family G member 4B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317286|||http://purl.uniprot.org/annotation/VAR_056672|||http://purl.uniprot.org/annotation/VAR_056673|||http://purl.uniprot.org/annotation/VAR_056674|||http://purl.uniprot.org/annotation/VAR_056675|||http://purl.uniprot.org/annotation/VAR_059547|||http://purl.uniprot.org/annotation/VAR_060453|||http://purl.uniprot.org/annotation/VAR_060454|||http://purl.uniprot.org/annotation/VAR_060455
http://togogenome.org/gene/9606:MOB1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L9L4                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||MOB kinase activator 1B|||N-acetylserine|||Phosphothreonine; by STK4/MST1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193564|||http://purl.uniprot.org/annotation/VSP_045097
http://togogenome.org/gene/9606:TAS2R38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59533                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082273|||http://purl.uniprot.org/annotation/VAR_017860|||http://purl.uniprot.org/annotation/VAR_017861|||http://purl.uniprot.org/annotation/VAR_017862
http://togogenome.org/gene/9606:VSIG10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0Z9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||V-set and immunoglobulin domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345115|||http://purl.uniprot.org/annotation/VAR_045692|||http://purl.uniprot.org/annotation/VAR_045693|||http://purl.uniprot.org/annotation/VSP_034915
http://togogenome.org/gene/9606:FOXB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99853                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein B1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091803
http://togogenome.org/gene/9606:TXNDC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZME4|||http://purl.uniprot.org/uniprot/Q9P2K2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Mediates endoplasmic reticulum retention|||N-linked (GlcNAc...) asparagine|||Thioredoxin|||Thioredoxin domain-containing protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257789|||http://purl.uniprot.org/annotation/VAR_028919|||http://purl.uniprot.org/annotation/VAR_061899|||http://purl.uniprot.org/annotation/VAR_061900
http://togogenome.org/gene/9606:TARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW92|||http://purl.uniprot.org/uniprot/U3KQG0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Aminoacyl-transfer RNA synthetases class-II family profile|||In COXPD21; decreased expression at mRNA and protein levels; decreased threonine-tRNA ligase activity; affects both Thr activation and transfer; decreased aminoacyl-tRNA editing activity; decreased protein stability; loss of homodimerization.|||In isoform 2.|||Mitochondrion|||Phosphoserine|||TGS|||Threonine--tRNA ligase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254586|||http://purl.uniprot.org/annotation/VAR_071853|||http://purl.uniprot.org/annotation/VSP_054537
http://togogenome.org/gene/9606:APOBEC3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC16                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||CMP/dCMP-type deaminase 1|||CMP/dCMP-type deaminase 2|||DNA dC->dU-editing enzyme APOBEC-3G|||Decreases cytidine deaminase activity and antiviral activity.|||Decreases cytidine deaminase activity.|||Does not decrease cytidine deaminase activity.|||Essential for cytoplasmic localization|||In isoform 3.|||Interaction with DNA|||Loss of cytidine deaminase activity and significant decrease in antiviral activity.|||Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259.|||Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67.|||Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity.|||Modifies the spectrum of action against mobile genetic elements; when associated with K-217.|||Modifies the spectrum of action against mobile genetic elements; when associated with K-247.|||Necessary for homooligomerization|||No effect on cytidine deaminase and antiviral activity.|||Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity.|||Phosphothreonine; by PKA|||Phosphothreonine; by PKA and CAMK2|||Proton donor|||Reduces enzyme activity.|||Remains sensitive to HIV-1 Vif and able to bind Vif.|||Resistant to HIV-1 Vif with complete loss of Vif-induced degradation and Vif binding.|||Slightly reduces enzyme activity.|||Strongly reduces enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171761|||http://purl.uniprot.org/annotation/VAR_017837|||http://purl.uniprot.org/annotation/VAR_025060|||http://purl.uniprot.org/annotation/VAR_048723|||http://purl.uniprot.org/annotation/VSP_009588|||http://purl.uniprot.org/annotation/VSP_009589
http://togogenome.org/gene/9606:SLC16A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15427                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes lactate transmembrane transporter activity. Does not affect cell membrane localization.|||Affects subcellular localization leading to apical localization. Affects subcellular localization leading to apical localization; when associated with A-425 and A-426.|||Affects subcellular localization leading to apical localization. Affects subcellular localization leading to apical localization; when associated with A-426 and A-427.|||Basolateral sorting signal|||Cytoplasmic|||Disordered|||Does not affect basolateral plasma membrane localization. Intracellular accumulation. Affects subcellular localization leading to apical localization; when associated with A-432.|||Does not affect basolateral plasma membrane localization. Intracellular accumulation. Affects subcellular localization leading to apical localization; when associated with A-433.|||Does not affect lactate transmembrane transporter activity.|||Extracellular|||Helical|||Leads to a nonpolar expression pattern. Affects subcellular localization leading to apical localization; when associated with A-425 and A-427.|||Monocarboxylate transporter 4|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211394
http://togogenome.org/gene/9606:RNF39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8G2|||http://purl.uniprot.org/uniprot/Q96QB5|||http://purl.uniprot.org/uniprot/Q9H2S5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||In isoform 2.|||In isoform 3.|||RING finger protein 39|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056080|||http://purl.uniprot.org/annotation/VAR_022723|||http://purl.uniprot.org/annotation/VAR_022724|||http://purl.uniprot.org/annotation/VAR_022725|||http://purl.uniprot.org/annotation/VAR_022726|||http://purl.uniprot.org/annotation/VSP_014240|||http://purl.uniprot.org/annotation/VSP_014241|||http://purl.uniprot.org/annotation/VSP_014242
http://togogenome.org/gene/9606:TGOLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43493                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 14 AA tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Endocytosis signal; in isoform TGN46 and isoform TGN48|||Endocytosis signal; in isoform TGN51|||Extracellular|||Helical|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform TGN48.|||Loss of relocalization to the trans-Golgi.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Polar residues|||Trans-Golgi network integral membrane protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022486|||http://purl.uniprot.org/annotation/VAR_034724|||http://purl.uniprot.org/annotation/VAR_034725|||http://purl.uniprot.org/annotation/VAR_034726|||http://purl.uniprot.org/annotation/VAR_034727|||http://purl.uniprot.org/annotation/VAR_034728|||http://purl.uniprot.org/annotation/VAR_034729|||http://purl.uniprot.org/annotation/VAR_034730|||http://purl.uniprot.org/annotation/VAR_082887|||http://purl.uniprot.org/annotation/VSP_060318|||http://purl.uniprot.org/annotation/VSP_060319|||http://purl.uniprot.org/annotation/VSP_060320|||http://purl.uniprot.org/annotation/VSP_060321|||http://purl.uniprot.org/annotation/VSP_060322|||http://purl.uniprot.org/annotation/VSP_060323
http://togogenome.org/gene/9606:DENND2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6A0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DENN domain-containing protein 2D|||In isoform 2.|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242686|||http://purl.uniprot.org/annotation/VAR_050950|||http://purl.uniprot.org/annotation/VSP_019471
http://togogenome.org/gene/9606:IL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNQ5|||http://purl.uniprot.org/uniprot/B4DVM1|||http://purl.uniprot.org/uniprot/P05231|||http://purl.uniprot.org/uniprot/Q75MH2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  87% loss of activity.|||Almost no loss of activity.|||Interleukin-6|||Loss of activity.|||N-linked (GlcNAc...) asparagine|||No loss of activity.|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015582|||http://purl.uniprot.org/annotation/PRO_5002803597|||http://purl.uniprot.org/annotation/PRO_5014310765|||http://purl.uniprot.org/annotation/VAR_013075|||http://purl.uniprot.org/annotation/VAR_013076|||http://purl.uniprot.org/annotation/VAR_029266
http://togogenome.org/gene/9606:DPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92784                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to acetylated histones H3 and H4.|||Abolishes binding to acetylated histones H3 and H4; when associated with R-360.|||Abolishes binding to acetylated histones H3 and H4; when associated with R-363.|||Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with HDGFL2|||Loss of interaction with HDGFL2. No effect on interaction with SMARCA4, SMARCC1 and SMARCD1.|||PHD-type 1|||PHD-type 2|||Phosphomimetic mutant. Increased interaction with HDGFL2.|||Phosphorylation-null mutant. Loss of interaction with HDGFL2.|||Phosphoserine|||Zinc finger protein DPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168154|||http://purl.uniprot.org/annotation/VAR_047771|||http://purl.uniprot.org/annotation/VAR_082912|||http://purl.uniprot.org/annotation/VSP_035882|||http://purl.uniprot.org/annotation/VSP_035883|||http://purl.uniprot.org/annotation/VSP_035884|||http://purl.uniprot.org/annotation/VSP_055748
http://togogenome.org/gene/9606:ZFTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JLR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Site                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form ZFTA-MLK2 fusion protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Pro residues|||Zinc finger translocation-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393909
http://togogenome.org/gene/9606:HSD17B7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56937                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054586|||http://purl.uniprot.org/annotation/VSP_006029|||http://purl.uniprot.org/annotation/VSP_012766
http://togogenome.org/gene/9606:SREK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXA9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Splicing regulatory glutamine/lysine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081940|||http://purl.uniprot.org/annotation/VSP_008399
http://togogenome.org/gene/9606:BTN3A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00478                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||Butyrophilin subfamily 3 member A3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014534|||http://purl.uniprot.org/annotation/VSP_045063|||http://purl.uniprot.org/annotation/VSP_045064
http://togogenome.org/gene/9606:CRACD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZU35                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Capping protein-inhibiting regulator of actin dynamics|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with actin-capping proteins                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342475|||http://purl.uniprot.org/annotation/VAR_044205|||http://purl.uniprot.org/annotation/VAR_044206|||http://purl.uniprot.org/annotation/VAR_044207|||http://purl.uniprot.org/annotation/VAR_044208|||http://purl.uniprot.org/annotation/VAR_079174
http://togogenome.org/gene/9606:NOVA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z770|||http://purl.uniprot.org/uniprot/P51513                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||In isoform 2.|||In isoform 3.|||K Homology|||KH 1|||KH 2|||KH 3|||Phosphoserine|||RNA-binding protein Nova-1|||Required for RNA binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050116|||http://purl.uniprot.org/annotation/VSP_060046|||http://purl.uniprot.org/annotation/VSP_060047|||http://purl.uniprot.org/annotation/VSP_060048
http://togogenome.org/gene/9606:ITGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17301                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In alloantigen HPA-5B.|||Integrin alpha-2|||Interaction with HPS5|||Markedly weakens RAB21-binding. Shows defective cytokinesis on collagen, but not on fibronectin.|||N-linked (GlcNAc...) asparagine|||No effect on RAB21-binding. Significant reduction of RAB21-binding; when associated with A-1161. Shows defective cytokinesis on collagen, but not on fibronectin; when associated with A-1161.|||No significant reduction of RAB21-binding by co-immunoprecipitation assay; when associated with A-1159 and A-1160.|||No significant reduction of RAB21-binding by co-immunoprecipitation assay; when associated with A-1160 and A-1162.|||Significant reduction of RAB21-binding; when associated with A-1160. Shows defective cytokinesis on collagen, but not on fibronectin; when associated with A-1160.|||Significant reduction of RAB21-binding; when associated with A-1160; A-1161 and A-1164.|||Significant reduction of RAB21-binding; when associated with A-1160; A-1161 and A-1165.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016233|||http://purl.uniprot.org/annotation/VAR_003977|||http://purl.uniprot.org/annotation/VAR_020036|||http://purl.uniprot.org/annotation/VAR_021855|||http://purl.uniprot.org/annotation/VAR_029146|||http://purl.uniprot.org/annotation/VAR_076939
http://togogenome.org/gene/9606:LACTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53H82                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Endoribonuclease LACTB2|||Loss of endoribonuclease activity.|||Loss of endoribonuclease activity. No effect on RNA-binding.|||Loss of endoribonuclease activity. Strongly decreases RNA-binding.|||Mildly decreases endoribonuclease activity. No effect on RNA-binding.|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315743
http://togogenome.org/gene/9606:KCNS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ31                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Potassium voltage-gated channel subfamily S member 3|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054087|||http://purl.uniprot.org/annotation/VAR_014200|||http://purl.uniprot.org/annotation/VAR_036986
http://togogenome.org/gene/9606:LDAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L288|||http://purl.uniprot.org/uniprot/I3NI23|||http://purl.uniprot.org/uniprot/Q96B96                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lipid droplet assembly factor 1|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279535|||http://purl.uniprot.org/annotation/VAR_030923|||http://purl.uniprot.org/annotation/VAR_030924|||http://purl.uniprot.org/annotation/VAR_057765|||http://purl.uniprot.org/annotation/VSP_056078
http://togogenome.org/gene/9606:PTCHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3VUI5|||http://purl.uniprot.org/uniprot/Q3KNS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Patched domain-containing protein 3|||Polar residues|||Pro residues|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309262|||http://purl.uniprot.org/annotation/VAR_036918|||http://purl.uniprot.org/annotation/VAR_036919|||http://purl.uniprot.org/annotation/VAR_036920|||http://purl.uniprot.org/annotation/VAR_036921|||http://purl.uniprot.org/annotation/VAR_036922|||http://purl.uniprot.org/annotation/VAR_036923|||http://purl.uniprot.org/annotation/VAR_036924|||http://purl.uniprot.org/annotation/VAR_036925|||http://purl.uniprot.org/annotation/VSP_061519|||http://purl.uniprot.org/annotation/VSP_061520
http://togogenome.org/gene/9606:OR2M7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVZ1|||http://purl.uniprot.org/uniprot/Q8NG81                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2M7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150494|||http://purl.uniprot.org/annotation/VAR_053149|||http://purl.uniprot.org/annotation/VAR_053150|||http://purl.uniprot.org/annotation/VAR_059992|||http://purl.uniprot.org/annotation/VAR_059993
http://togogenome.org/gene/9606:VSIG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y279                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like 1|||Ig-like 2|||In isoform 2.|||In isoform 3.|||V-set and immunoglobulin domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015006|||http://purl.uniprot.org/annotation/VAR_049956|||http://purl.uniprot.org/annotation/VAR_049957|||http://purl.uniprot.org/annotation/VAR_049958|||http://purl.uniprot.org/annotation/VAR_049959|||http://purl.uniprot.org/annotation/VSP_012813|||http://purl.uniprot.org/annotation/VSP_041213
http://togogenome.org/gene/9606:ALDH1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0Y2X5|||http://purl.uniprot.org/uniprot/P47895|||http://purl.uniprot.org/uniprot/Q7Z3A2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase|||Disordered|||In MCOP8.|||In MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels.|||N-acetylalanine|||Nucleophile|||Proton acceptor|||Removed|||Retinaldehyde dehydrogenase 3|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056478|||http://purl.uniprot.org/annotation/VAR_019706|||http://purl.uniprot.org/annotation/VAR_069322|||http://purl.uniprot.org/annotation/VAR_069323|||http://purl.uniprot.org/annotation/VAR_069324|||http://purl.uniprot.org/annotation/VAR_069325|||http://purl.uniprot.org/annotation/VAR_072332|||http://purl.uniprot.org/annotation/VAR_072333|||http://purl.uniprot.org/annotation/VAR_072334|||http://purl.uniprot.org/annotation/VAR_072335|||http://purl.uniprot.org/annotation/VAR_072336|||http://purl.uniprot.org/annotation/VAR_072337
http://togogenome.org/gene/9606:FOLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15328                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Folate receptor alpha|||GPI-anchor amidated serine|||Moderately reduced affinity for folate.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Slightly reduced affinity for folate.|||Strongly reduced affinity for folate.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008802|||http://purl.uniprot.org/annotation/PRO_0000008803|||http://purl.uniprot.org/annotation/VAR_011963|||http://purl.uniprot.org/annotation/VAR_059284
http://togogenome.org/gene/9606:CHEK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96017                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates autophosphorylation at Ser-379 and prevents ubiquitination.|||Confers a moderate risk of breast cancer; partially reduces kinase activity.|||Disordered|||FHA|||Impaired activation, phosphorylation by ATM and G2/M transition checkpoint.|||In BC.|||In BC; does not phosphorylate p53/TP53.|||In an osteogenic sarcoma sample; neutral allele among Ashkenazi Jewish women.|||In an osteogenic sarcoma sample; somatic mutation; might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer.|||In colon cancer and LFS2; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||In multiple cancers.|||In prostate cancer; germline mutation.|||In prostate cancer; somatic mutation.|||In prostate cancer; unknown pathological significance.|||In prostate cancer; unknown pathological significance; somatic mutation.|||Increased ubiquitination and degradation by the proteasome.|||Loss of activation and phosphorylation.|||Loss of autophosphorylation activity.|||Loss of kinase activity and of the ability to phosphorylate CDC25A.|||Loss of phosphorylation in response to ionizing radiation.|||May increase breast cancer risk.|||Might influence susceptibility to breast cancer; does not cause protein abrogation in familial colorectal cancer.|||Might influence susceptibility to different types of cancer; does not cause protein abrogation in familial colorectal cancer; loss of the ability to interact with and phosphorylate CDC25A and to promote CDC25A degradation in response to ionizing radiation.|||Phosphoserine|||Phosphoserine; by PLK3|||Phosphoserine; by autocatalysis|||Phosphothreonine; by ATM and MAP3K20|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Chk2|||T-loop/activation segment                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085858|||http://purl.uniprot.org/annotation/VAR_008554|||http://purl.uniprot.org/annotation/VAR_008555|||http://purl.uniprot.org/annotation/VAR_019101|||http://purl.uniprot.org/annotation/VAR_019102|||http://purl.uniprot.org/annotation/VAR_019103|||http://purl.uniprot.org/annotation/VAR_019104|||http://purl.uniprot.org/annotation/VAR_019105|||http://purl.uniprot.org/annotation/VAR_019106|||http://purl.uniprot.org/annotation/VAR_019107|||http://purl.uniprot.org/annotation/VAR_019108|||http://purl.uniprot.org/annotation/VAR_019109|||http://purl.uniprot.org/annotation/VAR_019110|||http://purl.uniprot.org/annotation/VAR_019111|||http://purl.uniprot.org/annotation/VAR_019112|||http://purl.uniprot.org/annotation/VAR_019113|||http://purl.uniprot.org/annotation/VAR_019114|||http://purl.uniprot.org/annotation/VAR_019115|||http://purl.uniprot.org/annotation/VAR_021117|||http://purl.uniprot.org/annotation/VAR_021118|||http://purl.uniprot.org/annotation/VAR_021119|||http://purl.uniprot.org/annotation/VAR_021120|||http://purl.uniprot.org/annotation/VAR_021121|||http://purl.uniprot.org/annotation/VAR_021122|||http://purl.uniprot.org/annotation/VAR_022461|||http://purl.uniprot.org/annotation/VAR_022462|||http://purl.uniprot.org/annotation/VAR_022463|||http://purl.uniprot.org/annotation/VAR_024572|||http://purl.uniprot.org/annotation/VAR_026630|||http://purl.uniprot.org/annotation/VAR_029154|||http://purl.uniprot.org/annotation/VAR_029155|||http://purl.uniprot.org/annotation/VAR_066012|||http://purl.uniprot.org/annotation/VAR_073020|||http://purl.uniprot.org/annotation/VSP_014556|||http://purl.uniprot.org/annotation/VSP_014557|||http://purl.uniprot.org/annotation/VSP_014558|||http://purl.uniprot.org/annotation/VSP_014559|||http://purl.uniprot.org/annotation/VSP_014560|||http://purl.uniprot.org/annotation/VSP_014561|||http://purl.uniprot.org/annotation/VSP_014562|||http://purl.uniprot.org/annotation/VSP_014563|||http://purl.uniprot.org/annotation/VSP_014564|||http://purl.uniprot.org/annotation/VSP_014565|||http://purl.uniprot.org/annotation/VSP_014566|||http://purl.uniprot.org/annotation/VSP_014567|||http://purl.uniprot.org/annotation/VSP_014568|||http://purl.uniprot.org/annotation/VSP_014569|||http://purl.uniprot.org/annotation/VSP_014570|||http://purl.uniprot.org/annotation/VSP_014571|||http://purl.uniprot.org/annotation/VSP_014572|||http://purl.uniprot.org/annotation/VSP_014573|||http://purl.uniprot.org/annotation/VSP_045148
http://togogenome.org/gene/9606:RPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35244                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylvaline|||Removed|||Replication protein A 14 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097276
http://togogenome.org/gene/9606:VPS54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1Q0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Vacuolar protein sorting-associated protein 54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148731|||http://purl.uniprot.org/annotation/VAR_052944|||http://purl.uniprot.org/annotation/VAR_061983|||http://purl.uniprot.org/annotation/VSP_013751|||http://purl.uniprot.org/annotation/VSP_013752|||http://purl.uniprot.org/annotation/VSP_013753|||http://purl.uniprot.org/annotation/VSP_013754|||http://purl.uniprot.org/annotation/VSP_013755|||http://purl.uniprot.org/annotation/VSP_013756
http://togogenome.org/gene/9606:KRTAP10-7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60409                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||30 X 5 AA repeats of C-C-X(3)|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185215|||http://purl.uniprot.org/annotation/VAR_047852|||http://purl.uniprot.org/annotation/VAR_047853|||http://purl.uniprot.org/annotation/VAR_047854|||http://purl.uniprot.org/annotation/VAR_047855|||http://purl.uniprot.org/annotation/VAR_060051
http://togogenome.org/gene/9606:GRXCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MXD5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Glutaredoxin|||Glutaredoxin domain-containing cysteine-rich protein 1|||In DFNB25.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349189|||http://purl.uniprot.org/annotation/VAR_063159|||http://purl.uniprot.org/annotation/VAR_063160|||http://purl.uniprot.org/annotation/VAR_063161|||http://purl.uniprot.org/annotation/VAR_063162|||http://purl.uniprot.org/annotation/VAR_063163|||http://purl.uniprot.org/annotation/VAR_063164|||http://purl.uniprot.org/annotation/VAR_063165
http://togogenome.org/gene/9606:TXLNB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3L3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Beta-taxilin|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189423|||http://purl.uniprot.org/annotation/VAR_019807|||http://purl.uniprot.org/annotation/VAR_057729|||http://purl.uniprot.org/annotation/VAR_057730|||http://purl.uniprot.org/annotation/VAR_057731
http://togogenome.org/gene/9606:ACMSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z681|||http://purl.uniprot.org/uniprot/Q6ZV40|||http://purl.uniprot.org/uniprot/Q8TDX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  2-amino-3-carboxymuconate-6-semialdehyde decarboxylase|||Amidohydrolase-related|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190979|||http://purl.uniprot.org/annotation/VSP_050622|||http://purl.uniprot.org/annotation/VSP_050623
http://togogenome.org/gene/9606:CYBB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3S6|||http://purl.uniprot.org/uniprot/P04839                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b-245 heavy chain|||Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In CGDX.|||In CGDX; completely inhibits NADPH oxidase activity; NADPH oxidase assembly is abolished.|||In CGDX; reduces NADPH oxidase activity to 4% of wild-type; translocation to the membrane of the phagosome is only attenuated.|||In CGDX; requires 2 nucleotide substitutions.|||In IMD34.|||N-linked (GlcNAc...) asparagine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210145|||http://purl.uniprot.org/annotation/VAR_002432|||http://purl.uniprot.org/annotation/VAR_002433|||http://purl.uniprot.org/annotation/VAR_002434|||http://purl.uniprot.org/annotation/VAR_002435|||http://purl.uniprot.org/annotation/VAR_002436|||http://purl.uniprot.org/annotation/VAR_002437|||http://purl.uniprot.org/annotation/VAR_002438|||http://purl.uniprot.org/annotation/VAR_002439|||http://purl.uniprot.org/annotation/VAR_002440|||http://purl.uniprot.org/annotation/VAR_002441|||http://purl.uniprot.org/annotation/VAR_007873|||http://purl.uniprot.org/annotation/VAR_007874|||http://purl.uniprot.org/annotation/VAR_007875|||http://purl.uniprot.org/annotation/VAR_007876|||http://purl.uniprot.org/annotation/VAR_007877|||http://purl.uniprot.org/annotation/VAR_007878|||http://purl.uniprot.org/annotation/VAR_007879|||http://purl.uniprot.org/annotation/VAR_007880|||http://purl.uniprot.org/annotation/VAR_007881|||http://purl.uniprot.org/annotation/VAR_007882|||http://purl.uniprot.org/annotation/VAR_007883|||http://purl.uniprot.org/annotation/VAR_007884|||http://purl.uniprot.org/annotation/VAR_007885|||http://purl.uniprot.org/annotation/VAR_007886|||http://purl.uniprot.org/annotation/VAR_007887|||http://purl.uniprot.org/annotation/VAR_007888|||http://purl.uniprot.org/annotation/VAR_007889|||http://purl.uniprot.org/annotation/VAR_007890|||http://purl.uniprot.org/annotation/VAR_007891|||http://purl.uniprot.org/annotation/VAR_007892|||http://purl.uniprot.org/annotation/VAR_007893|||http://purl.uniprot.org/annotation/VAR_007894|||http://purl.uniprot.org/annotation/VAR_007895|||http://purl.uniprot.org/annotation/VAR_007896|||http://purl.uniprot.org/annotation/VAR_007897|||http://purl.uniprot.org/annotation/VAR_007898|||http://purl.uniprot.org/annotation/VAR_008845|||http://purl.uniprot.org/annotation/VAR_016880|||http://purl.uniprot.org/annotation/VAR_016881|||http://purl.uniprot.org/annotation/VAR_025613|||http://purl.uniprot.org/annotation/VAR_025614|||http://purl.uniprot.org/annotation/VAR_025615|||http://purl.uniprot.org/annotation/VAR_025616|||http://purl.uniprot.org/annotation/VAR_025617|||http://purl.uniprot.org/annotation/VAR_025618|||http://purl.uniprot.org/annotation/VAR_025619|||http://purl.uniprot.org/annotation/VAR_025620|||http://purl.uniprot.org/annotation/VAR_025621|||http://purl.uniprot.org/annotation/VAR_025622|||http://purl.uniprot.org/annotation/VAR_025623|||http://purl.uniprot.org/annotation/VAR_025624|||http://purl.uniprot.org/annotation/VAR_047264|||http://purl.uniprot.org/annotation/VAR_047265|||http://purl.uniprot.org/annotation/VAR_047266|||http://purl.uniprot.org/annotation/VAR_047267|||http://purl.uniprot.org/annotation/VAR_047268|||http://purl.uniprot.org/annotation/VAR_047269|||http://purl.uniprot.org/annotation/VAR_047270|||http://purl.uniprot.org/annotation/VAR_047271|||http://purl.uniprot.org/annotation/VAR_047272|||http://purl.uniprot.org/annotation/VAR_047273|||http://purl.uniprot.org/annotation/VAR_047274|||http://purl.uniprot.org/annotation/VAR_047275|||http://purl.uniprot.org/annotation/VAR_047276|||http://purl.uniprot.org/annotation/VAR_065365|||http://purl.uniprot.org/annotation/VAR_065366|||http://purl.uniprot.org/annotation/VAR_068012|||http://purl.uniprot.org/annotation/VAR_068013|||http://purl.uniprot.org/annotation/VAR_071861|||http://purl.uniprot.org/annotation/VAR_071862|||http://purl.uniprot.org/annotation/VAR_071863|||http://purl.uniprot.org/annotation/VAR_078386
http://togogenome.org/gene/9606:NXPH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95158                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||II|||III|||IV (linker domain)|||N-linked (GlcNAc...) asparagine|||Neurexophilin-4|||V (Cys-rich)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020068
http://togogenome.org/gene/9606:CKAP2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYA6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates sumoylation.|||Basic and acidic residues|||Cytoskeleton-associated protein 2-like|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||KEN box|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324335|||http://purl.uniprot.org/annotation/VAR_039735|||http://purl.uniprot.org/annotation/VAR_039736|||http://purl.uniprot.org/annotation/VAR_039737|||http://purl.uniprot.org/annotation/VAR_039738|||http://purl.uniprot.org/annotation/VAR_039739|||http://purl.uniprot.org/annotation/VAR_039740|||http://purl.uniprot.org/annotation/VAR_039741|||http://purl.uniprot.org/annotation/VAR_039742|||http://purl.uniprot.org/annotation/VAR_039743|||http://purl.uniprot.org/annotation/VAR_039744|||http://purl.uniprot.org/annotation/VSP_032219|||http://purl.uniprot.org/annotation/VSP_032220|||http://purl.uniprot.org/annotation/VSP_053717
http://togogenome.org/gene/9606:OR2T1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVY3|||http://purl.uniprot.org/uniprot/A0A126GWK9|||http://purl.uniprot.org/uniprot/O43869                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150496|||http://purl.uniprot.org/annotation/VAR_057541
http://togogenome.org/gene/9606:TSPAN19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C672                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317254
http://togogenome.org/gene/9606:MPHOSPH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00566                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||U3 small nucleolar ribonucleoprotein protein MPP10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121535|||http://purl.uniprot.org/annotation/VAR_014470|||http://purl.uniprot.org/annotation/VAR_022000|||http://purl.uniprot.org/annotation/VAR_024539|||http://purl.uniprot.org/annotation/VAR_053511|||http://purl.uniprot.org/annotation/VAR_053512|||http://purl.uniprot.org/annotation/VAR_053513|||http://purl.uniprot.org/annotation/VAR_053514
http://togogenome.org/gene/9606:SNRNP200                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75643                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEIH box|||DEVH box|||Decreases ATP-dependent RNA helicase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding 1|||Helicase ATP-binding 2|||Helicase C-terminal 1|||Helicase C-terminal 2|||In RP33.|||In RP33; strongly reduced RNA helicase activity.|||In RP33; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with C9orf78 and WBP4|||Interaction with TSSC4|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||SEC63 1|||SEC63 2|||Strongly decreases ATP-dependent RNA helicase activity.|||U5 small nuclear ribonucleoprotein 200 kDa helicase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102087|||http://purl.uniprot.org/annotation/VAR_035943|||http://purl.uniprot.org/annotation/VAR_063539|||http://purl.uniprot.org/annotation/VAR_063540|||http://purl.uniprot.org/annotation/VAR_065587|||http://purl.uniprot.org/annotation/VAR_065588|||http://purl.uniprot.org/annotation/VAR_065589|||http://purl.uniprot.org/annotation/VAR_065590|||http://purl.uniprot.org/annotation/VAR_071689|||http://purl.uniprot.org/annotation/VAR_071690|||http://purl.uniprot.org/annotation/VAR_071691|||http://purl.uniprot.org/annotation/VAR_071692|||http://purl.uniprot.org/annotation/VAR_071693|||http://purl.uniprot.org/annotation/VAR_071694|||http://purl.uniprot.org/annotation/VAR_071695|||http://purl.uniprot.org/annotation/VSP_026622
http://togogenome.org/gene/9606:NDE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXR1|||http://purl.uniprot.org/uniprot/X5DP35|||http://purl.uniprot.org/uniprot/X5DR54                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with CENPF|||Interaction with PAFAH1B1|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-246.|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-243 and E-282.|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-228; E-246 and E-282.|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-215; E-243; E-246 and E-282.|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-191; E-228; E-243; E-246 and E-282.|||Loss of centrosomal localization and reduced ZNF365-binding; when associated with E-215; E-228; E-243; E-246 and E-282.|||NUDE|||Nuclear distribution protein nudE homolog 1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and A-282.|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-243 and V-246.|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-228; V-246 and A-282.|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-215; V-243; V-246 and A-282.|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-191; V-228; V-243; V-246 and A-282.|||Retained on spindle poles during mitosis, no loss of phosphorylation in vivo and increased ZNF365-binding; when associated with V-215; V-228; V-243; V-246 and A-282.|||S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7|||Self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240202|||http://purl.uniprot.org/annotation/VSP_059512
http://togogenome.org/gene/9606:EIF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41567|||http://purl.uniprot.org/uniprot/Q6IAV3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binds 40S ribosomal subunit|||Decrease in interaction with EIF4G1.|||Eukaryotic translation initiation factor 1|||N-acetylserine|||Phosphoserine|||Removed|||SUI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130554|||http://purl.uniprot.org/annotation/VAR_052505|||http://purl.uniprot.org/annotation/VAR_052506
http://togogenome.org/gene/9606:CABP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Calcium-binding protein 1|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform Calbrain.|||In isoform L-CaBP1.|||In isoform S-CaBP1.|||Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-352.|||Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-317 and A-354.|||Loss of binding to ITPRs; when associated with A-238; A-240; A-315; A-352 and A-354.|||Loss of binding to ITPRs; when associated with A-238; A-240; A-317; A-352 and A-354.|||Loss of magnesium-binding.|||Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-238; A-315; A-317; A-352 and A-354.|||Loss of magnesium-binding. Loss of binding to ITPRs; when associated with A-240; A-315; A-317; A-352 and A-354.|||Loss of phosphorylation and loss of calcium release by InsP(3).|||N-myristoyl glycine|||No effect on magnesium-binding.|||Phosphoserine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073513|||http://purl.uniprot.org/annotation/VSP_037936|||http://purl.uniprot.org/annotation/VSP_037937|||http://purl.uniprot.org/annotation/VSP_037938|||http://purl.uniprot.org/annotation/VSP_037939|||http://purl.uniprot.org/annotation/VSP_037940
http://togogenome.org/gene/9606:MAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20916|||http://purl.uniprot.org/uniprot/Q53ES7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like V-type|||In SPG75; alters proper folding; impairs N-glycosylation; retained in the endoplasmic reticulum; increased proteasome-dependent degradation.|||In SPG75; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with RTN4R and RTN4RL2|||Myelin-associated glycoprotein|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Not glycosylated|||Phosphoserine|||Required for normal axon myelination in the central nervous system|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014856|||http://purl.uniprot.org/annotation/PRO_5004249152|||http://purl.uniprot.org/annotation/VAR_059399|||http://purl.uniprot.org/annotation/VAR_076224|||http://purl.uniprot.org/annotation/VAR_076225|||http://purl.uniprot.org/annotation/VAR_077495|||http://purl.uniprot.org/annotation/VSP_042688|||http://purl.uniprot.org/annotation/VSP_045843
http://togogenome.org/gene/9606:ARHGEF39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4T4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Rho guanine nucleotide exchange factor 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291864|||http://purl.uniprot.org/annotation/VAR_032876|||http://purl.uniprot.org/annotation/VAR_061801|||http://purl.uniprot.org/annotation/VSP_026281|||http://purl.uniprot.org/annotation/VSP_026282|||http://purl.uniprot.org/annotation/VSP_026283|||http://purl.uniprot.org/annotation/VSP_026284|||http://purl.uniprot.org/annotation/VSP_026285|||http://purl.uniprot.org/annotation/VSP_026286
http://togogenome.org/gene/9606:RGS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXW5|||http://purl.uniprot.org/uniprot/P49802                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEP|||Diminishes interaction with GNB5.|||Disordered|||G protein gamma|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||RGS|||Regulator of G-protein signaling 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204196|||http://purl.uniprot.org/annotation/VAR_057153|||http://purl.uniprot.org/annotation/VAR_060604|||http://purl.uniprot.org/annotation/VSP_005671|||http://purl.uniprot.org/annotation/VSP_005672|||http://purl.uniprot.org/annotation/VSP_005673|||http://purl.uniprot.org/annotation/VSP_038388
http://togogenome.org/gene/9606:SS18L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSR7|||http://purl.uniprot.org/uniprot/O75177                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calcium-responsive transactivator|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||MFD domain|||Methionine-rich intra-molecular domain|||N-terminal auto-inhibitory domain; necessary for interaction with SMARCA4/BRG1|||Necessary for interaction with CREBBP and for the recruitment of CREBBP to the nuclear bodies|||Necessary for nuclear localization|||Polar residues|||SH2-binding|||SH3-binding|||SS18 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181825|||http://purl.uniprot.org/annotation/VAR_053691|||http://purl.uniprot.org/annotation/VAR_062534|||http://purl.uniprot.org/annotation/VSP_038697|||http://purl.uniprot.org/annotation/VSP_038698|||http://purl.uniprot.org/annotation/VSP_038699|||http://purl.uniprot.org/annotation/VSP_038700
http://togogenome.org/gene/9606:MAGEE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD90                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  MAGE 1|||MAGE 2|||Melanoma-associated antigen E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156731|||http://purl.uniprot.org/annotation/VAR_053509
http://togogenome.org/gene/9606:SPG11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JI7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In SPG11.|||In SPG11; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Spatacsin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287467|||http://purl.uniprot.org/annotation/VAR_032307|||http://purl.uniprot.org/annotation/VAR_032308|||http://purl.uniprot.org/annotation/VAR_058417|||http://purl.uniprot.org/annotation/VAR_078057|||http://purl.uniprot.org/annotation/VAR_078058|||http://purl.uniprot.org/annotation/VAR_078059|||http://purl.uniprot.org/annotation/VAR_078060|||http://purl.uniprot.org/annotation/VAR_078061|||http://purl.uniprot.org/annotation/VAR_078062|||http://purl.uniprot.org/annotation/VSP_025483|||http://purl.uniprot.org/annotation/VSP_025484|||http://purl.uniprot.org/annotation/VSP_045347
http://togogenome.org/gene/9606:C1orf122                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSJ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Uncharacterized protein C1orf122                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254193|||http://purl.uniprot.org/annotation/VSP_046648
http://togogenome.org/gene/9606:KRTAP5-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q701N2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184103
http://togogenome.org/gene/9606:FES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07332                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation.|||Abolishes kinase activity.|||Abolishes kinase activity. Fails to inhibit proliferation of melanoma cells.|||Abolishes pTyr binding. Abolishes association with microtubules. Abolishes autophosphorylation. Reduced kinase activity.|||Constitutively activated kinase that can act as oncogene. Promotes myeloid cell survival and proliferation.|||Disordered|||F-BAR|||Important for interaction with membranes containing phosphoinositides|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||Negligible effect on autophosphorylation and kinase activity.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduced autophosphorylation and strongly reduced kinase activity.|||Reduced binding to membranes containing phosphoinositides.|||Reduces kinase activity by over 90%.|||SH2|||Strongly reduced autophosphorylation and kinase activity.|||Tyrosine-protein kinase Fes/Fps                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088088|||http://purl.uniprot.org/annotation/VAR_041697|||http://purl.uniprot.org/annotation/VAR_041698|||http://purl.uniprot.org/annotation/VAR_041699|||http://purl.uniprot.org/annotation/VSP_041748|||http://purl.uniprot.org/annotation/VSP_041749
http://togogenome.org/gene/9606:TFAP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05549                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||H-S-H (helix-span-helix), dimerization|||In BOFS.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||No phosphorylation.|||PPxY motif|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Transcription factor AP-2-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184796|||http://purl.uniprot.org/annotation/VAR_045838|||http://purl.uniprot.org/annotation/VAR_045839|||http://purl.uniprot.org/annotation/VAR_045840|||http://purl.uniprot.org/annotation/VAR_045841|||http://purl.uniprot.org/annotation/VSP_006401|||http://purl.uniprot.org/annotation/VSP_043268|||http://purl.uniprot.org/annotation/VSP_047050
http://togogenome.org/gene/9606:FASTKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D57|||http://purl.uniprot.org/uniprot/Q53R41                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  FAST kinase domain-containing protein 1, mitochondrial|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284710|||http://purl.uniprot.org/annotation/VAR_031806|||http://purl.uniprot.org/annotation/VAR_031807|||http://purl.uniprot.org/annotation/VAR_031808|||http://purl.uniprot.org/annotation/VSP_024617
http://togogenome.org/gene/9606:RBM48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5RL73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||RNA-binding protein 48|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321514|||http://purl.uniprot.org/annotation/VSP_056683
http://togogenome.org/gene/9606:ZNF287                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PEZ3|||http://purl.uniprot.org/uniprot/Q9HBT7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||SCAN box|||Zinc finger protein 287                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047511|||http://purl.uniprot.org/annotation/VAR_024207
http://togogenome.org/gene/9606:GPRASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW05|||http://purl.uniprot.org/uniprot/Q96D09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Armadillo repeat-containing|||Basic and acidic residues|||Disordered|||G-protein coupled receptor-associated sorting protein 2|||In DFNX7; requires 2 nucleotide substitutions.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239053|||http://purl.uniprot.org/annotation/VAR_049265|||http://purl.uniprot.org/annotation/VAR_081645
http://togogenome.org/gene/9606:CTNND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60716                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 10|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Catenin delta-1|||Complete loss of cadherin interaction.|||Disordered|||Essential for interaction with cadherins|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BCDS2.|||In isoform 1AB, isoform 1A, isoform 1B, isoform 1, isoform 2AB, isoform 2A, isoform 2B, isoform 2, isoform 3AB, isoform 3A, isoform 3B, isoform 3, isoform 4AB, isoform 4A, isoform 4B and isoform 4.|||In isoform 1AC, isoform 1A, isoform 1C, isoform 1, isoform 2AC, isoform 2A, isoform 2C, isoform 2, isoform 3AC, isoform 3A, isoform 3C, isoform 3, isoform 4AC, isoform 4A, isoform 4C and isoform 4.|||In isoform 1BC, isoform 1B, isoform 1C, isoform 1, isoform 2BC, isoform 2B, isoform 2C, isoform 2, isoform 3BC, isoform 3B, isoform 3C, isoform 3, isoform 4BC, isoform 4B, isoform 4C and isoform 4.|||In isoform 2ABC, isoform 2AB, isoform 2AC, isoform 2BC, isoform 2A, isoform 2B, isoform 2C and isoform 2.|||In isoform 3ABC, isoform 3AB, isoform 3AC, isoform 3BC, isoform 3A, isoform 3B, isoform 3C and isoform 3.|||In isoform 4ABC, isoform 4AB, isoform 4AC, isoform 4BC, isoform 4A, isoform 4B, isoform 4C and isoform 4.|||N-acetylmethionine|||Necessary and sufficient for interaction with CCDC85B|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphoserine; by PAK5|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues|||Severely disrupts cadherin interaction.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064296|||http://purl.uniprot.org/annotation/VAR_020929|||http://purl.uniprot.org/annotation/VAR_020930|||http://purl.uniprot.org/annotation/VAR_020931|||http://purl.uniprot.org/annotation/VAR_038255|||http://purl.uniprot.org/annotation/VAR_079395|||http://purl.uniprot.org/annotation/VAR_079396|||http://purl.uniprot.org/annotation/VSP_006740|||http://purl.uniprot.org/annotation/VSP_006741|||http://purl.uniprot.org/annotation/VSP_006742|||http://purl.uniprot.org/annotation/VSP_006743|||http://purl.uniprot.org/annotation/VSP_006744|||http://purl.uniprot.org/annotation/VSP_006745
http://togogenome.org/gene/9606:CDCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXM1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CUB 1|||CUB 2|||CUB 3|||CUB domain-containing protein 2|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305071|||http://purl.uniprot.org/annotation/VAR_035162|||http://purl.uniprot.org/annotation/VSP_028212|||http://purl.uniprot.org/annotation/VSP_028213
http://togogenome.org/gene/9606:NMU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J202|||http://purl.uniprot.org/uniprot/A0A250SH36|||http://purl.uniprot.org/uniprot/E9PDJ7|||http://purl.uniprot.org/uniprot/P48645|||http://purl.uniprot.org/uniprot/Q86WB6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Asparagine amide|||Methionine sulfoxide; partial|||Neuromedin U C-terminal|||Neuromedin precursor-related peptide 33|||Neuromedin precursor-related peptide 36|||Neuromedin-U-25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019772|||http://purl.uniprot.org/annotation/PRO_0000019773|||http://purl.uniprot.org/annotation/PRO_0000019774|||http://purl.uniprot.org/annotation/PRO_0000445765|||http://purl.uniprot.org/annotation/PRO_0000445766|||http://purl.uniprot.org/annotation/PRO_5002105570|||http://purl.uniprot.org/annotation/PRO_5003244990|||http://purl.uniprot.org/annotation/PRO_5014281889|||http://purl.uniprot.org/annotation/VAR_053538|||http://purl.uniprot.org/annotation/VAR_053539
http://togogenome.org/gene/9606:TTC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BZ57|||http://purl.uniprot.org/uniprot/P53804                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes phosphorylation by Akt and impairs ubiquitin ligase activity on Akt.|||Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase TTC3|||In a breast cancer sample; somatic mutation.|||In an extended family with high risk of late-onset Alzheimer Disease.|||In isoform TPRDII.|||In isoform TPRDIII.|||Interaction with POLG|||Phosphoserine|||Phosphoserine; by PKB/AKT2|||Polar residues|||RING-type|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106378|||http://purl.uniprot.org/annotation/VAR_020312|||http://purl.uniprot.org/annotation/VAR_024676|||http://purl.uniprot.org/annotation/VAR_035868|||http://purl.uniprot.org/annotation/VAR_044428|||http://purl.uniprot.org/annotation/VAR_082645|||http://purl.uniprot.org/annotation/VSP_006554|||http://purl.uniprot.org/annotation/VSP_006555
http://togogenome.org/gene/9606:IFNA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C381|||http://purl.uniprot.org/uniprot/P32881                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Interferon alpha-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016365|||http://purl.uniprot.org/annotation/PRO_5030706726|||http://purl.uniprot.org/annotation/VAR_021975
http://togogenome.org/gene/9606:DYNC1H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14204                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Basic and acidic residues|||Cytoplasmic dynein 1 heavy chain 1|||Disordered|||Found in a patient with spinal muscular atrophy; unknown pathological significance.|||In CDCBM13.|||In CDCBM13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein.|||In CMT2O and SMALED1.|||In CMT2O and SMALED1; slight increased BICD2-binding.|||In CMT2O; impairs function.|||In SMALED1.|||In SMALED1; disrupts dynein complex stability and function.|||In SMALED1; slight increased BICD2-binding.|||Interaction with DYNC1I2|||Interaction with DYNC1LI2|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114627|||http://purl.uniprot.org/annotation/VAR_020889|||http://purl.uniprot.org/annotation/VAR_020890|||http://purl.uniprot.org/annotation/VAR_065085|||http://purl.uniprot.org/annotation/VAR_066651|||http://purl.uniprot.org/annotation/VAR_067820|||http://purl.uniprot.org/annotation/VAR_067821|||http://purl.uniprot.org/annotation/VAR_067822|||http://purl.uniprot.org/annotation/VAR_067823|||http://purl.uniprot.org/annotation/VAR_069437|||http://purl.uniprot.org/annotation/VAR_069438|||http://purl.uniprot.org/annotation/VAR_069439|||http://purl.uniprot.org/annotation/VAR_069440|||http://purl.uniprot.org/annotation/VAR_069441|||http://purl.uniprot.org/annotation/VAR_069442|||http://purl.uniprot.org/annotation/VAR_069443|||http://purl.uniprot.org/annotation/VAR_069444|||http://purl.uniprot.org/annotation/VAR_070580|||http://purl.uniprot.org/annotation/VAR_070581|||http://purl.uniprot.org/annotation/VAR_070582|||http://purl.uniprot.org/annotation/VAR_070583|||http://purl.uniprot.org/annotation/VAR_070584|||http://purl.uniprot.org/annotation/VAR_070585|||http://purl.uniprot.org/annotation/VAR_070586|||http://purl.uniprot.org/annotation/VAR_070587|||http://purl.uniprot.org/annotation/VAR_072092|||http://purl.uniprot.org/annotation/VAR_072093|||http://purl.uniprot.org/annotation/VAR_073155|||http://purl.uniprot.org/annotation/VAR_073156|||http://purl.uniprot.org/annotation/VAR_073157|||http://purl.uniprot.org/annotation/VAR_078241|||http://purl.uniprot.org/annotation/VAR_078242
http://togogenome.org/gene/9606:PBX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCR3|||http://purl.uniprot.org/uniprot/P40425                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox; TALE-type|||PBC|||PBC-A|||PBC-B|||Phosphoserine|||Polar residues|||Pre-B-cell leukemia transcription factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049237
http://togogenome.org/gene/9606:SPATA31H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||27 X 8 AA approximate tandem repeat of P-S-E-R-S-H-H-S|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||Uncharacterized protein C2orf16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281907|||http://purl.uniprot.org/annotation/VAR_031313|||http://purl.uniprot.org/annotation/VAR_031314|||http://purl.uniprot.org/annotation/VAR_031315|||http://purl.uniprot.org/annotation/VAR_031316|||http://purl.uniprot.org/annotation/VAR_031317|||http://purl.uniprot.org/annotation/VAR_031318|||http://purl.uniprot.org/annotation/VAR_031319|||http://purl.uniprot.org/annotation/VAR_031320|||http://purl.uniprot.org/annotation/VAR_031321|||http://purl.uniprot.org/annotation/VAR_031322|||http://purl.uniprot.org/annotation/VAR_031323
http://togogenome.org/gene/9606:SLC44A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5Y4|||http://purl.uniprot.org/uniprot/Q8NCS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Choline transporter-like protein 5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191726|||http://purl.uniprot.org/annotation/VSP_059802|||http://purl.uniprot.org/annotation/VSP_059803
http://togogenome.org/gene/9606:TMEM223                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJW6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Transmembrane protein 223                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321833|||http://purl.uniprot.org/annotation/VAR_039357|||http://purl.uniprot.org/annotation/VAR_039358
http://togogenome.org/gene/9606:CDT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H211                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding of cyclin A-dependent protein kinases.|||Alters interaction with GMNN.|||Cyclin-binding motif|||DNA replication factor Cdt1|||Disordered|||In MGORS4.|||Interaction with GMNN|||Interaction with LRWD1|||PIP-box K+4 motif|||Phosphoserine|||Phosphoserine; by MAPK8|||Phosphothreonine; by MAPK8|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191619|||http://purl.uniprot.org/annotation/VAR_024408|||http://purl.uniprot.org/annotation/VAR_029163|||http://purl.uniprot.org/annotation/VAR_029164|||http://purl.uniprot.org/annotation/VAR_029165|||http://purl.uniprot.org/annotation/VAR_054504|||http://purl.uniprot.org/annotation/VAR_054505|||http://purl.uniprot.org/annotation/VAR_065488|||http://purl.uniprot.org/annotation/VAR_065489|||http://purl.uniprot.org/annotation/VAR_065490|||http://purl.uniprot.org/annotation/VAR_065491|||http://purl.uniprot.org/annotation/VAR_065492
http://togogenome.org/gene/9606:TAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21675                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  25% decrease in histone acetylation.|||Acidic residues|||Basic and acidic residues|||Bromo 1|||Bromo 2|||Disordered|||Dramatic decrease in histone acetylation.|||Found in a patient with X-linked intellectual disability; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box; involved in promoter binding|||Histone acetyltransferase (HAT)|||In MRXS33.|||In MRXS33; unknown pathological significance.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung bronchoalveolar carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 1 and isoform 13.|||In isoform 13 and isoform 14.|||In isoform 15.|||In isoform 16.|||In isoform 2a, isoform 16, isoform 2c, isoform 2d and isoform 2g.|||In isoform 2e.|||In isoform 2h.|||In isoform 2i.|||In isoform 4, isoform 2a and isoform 2g.|||In isoform N-TAF1, isoform 2d and isoform 2g.|||Interaction with ASF1A and ASF1B|||N6-acetyllysine|||No decrease in kinase activity.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Protein kinase 1|||Protein kinase 2|||Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152.|||Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154.|||Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154.|||Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154.|||Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154.|||Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154.|||Reduces kinase activity; when associated with A-326; A-328; A-329 and A-330.|||Reduces kinase activity; when associated with A-326; A-328; A-329 and A-331.|||Reduces kinase activity; when associated with A-326; A-328; A-330 and A-331.|||Reduces kinase activity; when associated with A-326; A-329; A-330 and A-331.|||Reduces kinase activity; when associated with A-328; A-329; A-330 and A-331.|||Transcription initiation factor TFIID subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211215|||http://purl.uniprot.org/annotation/VAR_020678|||http://purl.uniprot.org/annotation/VAR_041930|||http://purl.uniprot.org/annotation/VAR_041931|||http://purl.uniprot.org/annotation/VAR_041932|||http://purl.uniprot.org/annotation/VAR_041933|||http://purl.uniprot.org/annotation/VAR_048433|||http://purl.uniprot.org/annotation/VAR_076394|||http://purl.uniprot.org/annotation/VAR_076395|||http://purl.uniprot.org/annotation/VAR_076396|||http://purl.uniprot.org/annotation/VAR_076397|||http://purl.uniprot.org/annotation/VAR_076398|||http://purl.uniprot.org/annotation/VAR_076399|||http://purl.uniprot.org/annotation/VAR_076400|||http://purl.uniprot.org/annotation/VAR_077838|||http://purl.uniprot.org/annotation/VAR_077839|||http://purl.uniprot.org/annotation/VSP_061987|||http://purl.uniprot.org/annotation/VSP_061988|||http://purl.uniprot.org/annotation/VSP_061989|||http://purl.uniprot.org/annotation/VSP_061990|||http://purl.uniprot.org/annotation/VSP_061991|||http://purl.uniprot.org/annotation/VSP_061992|||http://purl.uniprot.org/annotation/VSP_061993|||http://purl.uniprot.org/annotation/VSP_061994|||http://purl.uniprot.org/annotation/VSP_061995|||http://purl.uniprot.org/annotation/VSP_061996|||http://purl.uniprot.org/annotation/VSP_061997|||http://purl.uniprot.org/annotation/VSP_061998|||http://purl.uniprot.org/annotation/VSP_061999|||http://purl.uniprot.org/annotation/VSP_062000
http://togogenome.org/gene/9606:ZBTB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15916                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Phosphoserine|||Zinc finger and BTB domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047608
http://togogenome.org/gene/9606:BNIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C671                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Polar residues|||Protein BNIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317187|||http://purl.uniprot.org/annotation/VAR_056808
http://togogenome.org/gene/9606:RAB3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20337                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||Loss of phosphorylation. No effect on GDI2, CHM and CHML binding.|||N-acetylalanine|||Phosphomimetic mutant. Loss of GDI2, CHM and CHML binding.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3B|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121081
http://togogenome.org/gene/9606:MON1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKA0|||http://purl.uniprot.org/uniprot/E7EW32|||http://purl.uniprot.org/uniprot/Q6ZR87|||http://purl.uniprot.org/uniprot/Q7L1V2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FUZ/MON1/HPS1 first Longin|||FUZ/MON1/HPS1 second Longin|||FUZ/MON1/HPS1 third Longin|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Vacuolar fusion protein MON1 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285765|||http://purl.uniprot.org/annotation/VSP_054664|||http://purl.uniprot.org/annotation/VSP_054665
http://togogenome.org/gene/9606:CDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U2ZQU7|||http://purl.uniprot.org/uniprot/B3GN61|||http://purl.uniprot.org/uniprot/P12830|||http://purl.uniprot.org/uniprot/Q9UII7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to CBLL1.|||Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage.|||CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm.|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-1|||Cleavage; by S.pyogenes SpeB|||Cleavage; by a metalloproteinase|||Cleavage; by caspase-3|||Cleavage; by gamma-secretase/PS1|||Cytoplasmic|||Detected in an endometrial cancer sample.|||Detected in an endometrial cancer sample; loss of heterozygosity; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence.|||Disordered|||E-Cad/CTF1|||E-Cad/CTF2|||E-Cad/CTF3|||Extracellular|||Found in a gastric cancer sample; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence.|||Found in gastric and colorectal cancer samples; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence.|||Found in gastric carcinoma cell lines.|||Helical|||In BCDS1; abolishes protein abundance; loss of cell membrane localization.|||In BCDS1; decreases protein abundance; loss of cell membrane localization.|||In BCDS1; slightly decreases protein abundance; loss of cell membrane localization.|||In DGLBC.|||In a breast cancer sample; somatic mutation.|||In a diffuse gastric cancer sample.|||In a gastric cancer sample.|||In a gastric carcinoma sample.|||In a gastric carcinoma sample; loss of heterozygosity.|||In a thyroid cancer sample; may play a role in colorectal carcinogenesis.|||In an ovarian carcinoma sample; somatic mutation; loss of heterozygosity.|||In isoform 2.|||In lobular breast carcinoma.|||Interchain|||May contribute to prostate cancer.|||N-linked (GlcNAc...) asparagine|||No longer adheres to L.monocytogenes InlA coated beads, nor do cells take up InlA coated beads.|||No longer binds L.monocytogenes InlA.|||O-linked (Man...) serine|||O-linked (Man...) threonine|||Phosphoserine|||Phosphotyrosine; by SRC|||Protein is partially unfolded, no longer binds L.monocytogenes InlA.|||Required for binding CTNND1 and PSEN1|||Required for binding alpha, beta and gamma catenins                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003715|||http://purl.uniprot.org/annotation/PRO_0000003716|||http://purl.uniprot.org/annotation/PRO_0000236067|||http://purl.uniprot.org/annotation/PRO_0000236068|||http://purl.uniprot.org/annotation/PRO_0000236069|||http://purl.uniprot.org/annotation/PRO_5002788831|||http://purl.uniprot.org/annotation/PRO_5004334111|||http://purl.uniprot.org/annotation/PRO_5035398701|||http://purl.uniprot.org/annotation/VAR_001306|||http://purl.uniprot.org/annotation/VAR_001307|||http://purl.uniprot.org/annotation/VAR_001308|||http://purl.uniprot.org/annotation/VAR_001309|||http://purl.uniprot.org/annotation/VAR_001310|||http://purl.uniprot.org/annotation/VAR_001311|||http://purl.uniprot.org/annotation/VAR_001312|||http://purl.uniprot.org/annotation/VAR_001313|||http://purl.uniprot.org/annotation/VAR_001314|||http://purl.uniprot.org/annotation/VAR_001315|||http://purl.uniprot.org/annotation/VAR_001317|||http://purl.uniprot.org/annotation/VAR_001318|||http://purl.uniprot.org/annotation/VAR_001319|||http://purl.uniprot.org/annotation/VAR_001320|||http://purl.uniprot.org/annotation/VAR_001321|||http://purl.uniprot.org/annotation/VAR_001322|||http://purl.uniprot.org/annotation/VAR_008712|||http://purl.uniprot.org/annotation/VAR_008713|||http://purl.uniprot.org/annotation/VAR_013970|||http://purl.uniprot.org/annotation/VAR_013971|||http://purl.uniprot.org/annotation/VAR_021868|||http://purl.uniprot.org/annotation/VAR_021869|||http://purl.uniprot.org/annotation/VAR_023357|||http://purl.uniprot.org/annotation/VAR_023358|||http://purl.uniprot.org/annotation/VAR_023359|||http://purl.uniprot.org/annotation/VAR_033026|||http://purl.uniprot.org/annotation/VAR_033027|||http://purl.uniprot.org/annotation/VAR_048500|||http://purl.uniprot.org/annotation/VAR_048501|||http://purl.uniprot.org/annotation/VAR_048502|||http://purl.uniprot.org/annotation/VAR_055431|||http://purl.uniprot.org/annotation/VAR_079392|||http://purl.uniprot.org/annotation/VAR_079393|||http://purl.uniprot.org/annotation/VAR_079394|||http://purl.uniprot.org/annotation/VSP_055586
http://togogenome.org/gene/9606:H4C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:LOC100533997                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43359                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Polar residues|||Putative melanoma-associated antigen 5P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156705|||http://purl.uniprot.org/annotation/VAR_053492
http://togogenome.org/gene/9606:PRTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24158                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||Myeloblastin|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027707|||http://purl.uniprot.org/annotation/PRO_0000027708|||http://purl.uniprot.org/annotation/PRO_0000027709|||http://purl.uniprot.org/annotation/VAR_011691|||http://purl.uniprot.org/annotation/VAR_011713|||http://purl.uniprot.org/annotation/VAR_011714
http://togogenome.org/gene/9606:MST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XAK1|||http://purl.uniprot.org/uniprot/P26927|||http://purl.uniprot.org/uniprot/Q53GN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Apple|||Hepatocyte growth factor-like protein|||Hepatocyte growth factor-like protein alpha chain|||Hepatocyte growth factor-like protein beta chain|||Interchain (between alpha and beta chains)|||Kringle|||Kringle 1|||Kringle 2|||Kringle 3|||Kringle 4|||May be associated with inflammatory bowel disease; results in reduced binding affinity to MST1R.|||N-linked (GlcNAc...) asparagine|||PAN|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028085|||http://purl.uniprot.org/annotation/PRO_0000028086|||http://purl.uniprot.org/annotation/PRO_0000028087|||http://purl.uniprot.org/annotation/PRO_5012204042|||http://purl.uniprot.org/annotation/PRO_5015091868|||http://purl.uniprot.org/annotation/VAR_006631|||http://purl.uniprot.org/annotation/VAR_006632|||http://purl.uniprot.org/annotation/VAR_059787|||http://purl.uniprot.org/annotation/VAR_070224
http://togogenome.org/gene/9606:TRAPPC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43617                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Impairs interaction with TRAPPC1.|||In isoform 2.|||Loss of palmitoylation.|||S-palmitoyl cysteine|||Trafficking protein particle complex subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211572|||http://purl.uniprot.org/annotation/VSP_047015
http://togogenome.org/gene/9606:FAM234B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU67                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Protein FAM234B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288913
http://togogenome.org/gene/9606:TGM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIT7|||http://purl.uniprot.org/uniprot/B4DTN7|||http://purl.uniprot.org/uniprot/P21980|||http://purl.uniprot.org/uniprot/V9HWG3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished isopeptidase activity and reduced transamidase activity.|||Abolished isopeptidase and transamidase activities.|||Abolished protein-glutamine gamma-glutamyltransferase activity without affecting alpha-1 adrenergic receptor signaling. Abolished isopeptidase activity.|||Abolished protein-glutamine gamma-glutamyltransferase activity without affecting cytotoxic activity.|||Abolishes GTP-binding and transglutaminase activities. Does not have cytotoxic activity when overexpressed.|||Alternate|||Displays lower Ca(2+)-binding affinity and reduced transglutaminase activity.|||Does not affect the protein-glutamine deamidase activity.|||Dominant negative mutant. Abolishes WDR54 cross-linking.|||Impaired Ca(2+)-binding leading to reduced transglutaminase activity.|||Impaired substrate recognition for the protein-glutamine deamidase activity.|||Important for catalytic activity|||In TG2-I; strongly reduced transamidase activity without affecting the isopeptidase activity.|||In TG2-T; strongly reduced isopeptidase activity without affecting the transamidase activity.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In patients with early-onset diabetes type 2; unknown pathological significance.|||Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)|||N-acetylalanine|||N6-acetyllysine|||No effect on isopeptidase and transamidase activities.|||Phosphoserine|||Protein-glutamine gamma-glutamyltransferase 2|||Reduced isopeptidase and transamidase activities.|||Removed|||Substitution with F13A1 sequence. Abolished interaction with phospholipase C and ability to promote alpha-1 adrenergic receptor signaling.|||Transglutaminase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213707|||http://purl.uniprot.org/annotation/VAR_036554|||http://purl.uniprot.org/annotation/VAR_037998|||http://purl.uniprot.org/annotation/VAR_037999|||http://purl.uniprot.org/annotation/VAR_052553|||http://purl.uniprot.org/annotation/VAR_052554|||http://purl.uniprot.org/annotation/VAR_055357|||http://purl.uniprot.org/annotation/VAR_055358|||http://purl.uniprot.org/annotation/VAR_055359|||http://purl.uniprot.org/annotation/VSP_006411|||http://purl.uniprot.org/annotation/VSP_006412|||http://purl.uniprot.org/annotation/VSP_006413|||http://purl.uniprot.org/annotation/VSP_006414
http://togogenome.org/gene/9606:RND2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52198                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Effector region|||Removed in mature form|||Rho-related GTP-binding protein RhoN|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198876|||http://purl.uniprot.org/annotation/PRO_0000281228
http://togogenome.org/gene/9606:ITGAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAL6|||http://purl.uniprot.org/uniprot/P20701                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation and MEM-83-activated T-cell adhesion to ICAM1. Abolishes integrin alpha-L/beta-2 activation by CXCL12 and TERF2IP/RAP1. Does not affect heterodimerization of cell surface expression. Does not affect TCR- or phorbol ester-activated T-cell adhesion to ICAM1.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 2.|||In isoform 3.|||Integrin alpha-L|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016292|||http://purl.uniprot.org/annotation/PRO_5001423852|||http://purl.uniprot.org/annotation/VAR_025235|||http://purl.uniprot.org/annotation/VAR_025236|||http://purl.uniprot.org/annotation/VAR_025237|||http://purl.uniprot.org/annotation/VAR_025238|||http://purl.uniprot.org/annotation/VSP_002738|||http://purl.uniprot.org/annotation/VSP_042842|||http://purl.uniprot.org/annotation/VSP_042843
http://togogenome.org/gene/9606:EPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2F5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with MBTD1; when associated with D-651.|||Abolished interaction with MBTD1; when associated with D-660--663-D.|||Disordered|||Enhancer of polycomb homolog 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214153|||http://purl.uniprot.org/annotation/VAR_074181|||http://purl.uniprot.org/annotation/VSP_012875|||http://purl.uniprot.org/annotation/VSP_012877
http://togogenome.org/gene/9606:ZNF707                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C28                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 707                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233284|||http://purl.uniprot.org/annotation/VAR_033596
http://togogenome.org/gene/9606:H3C6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:RNF215                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6U7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||RING finger protein 215|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287534|||http://purl.uniprot.org/annotation/VAR_032319
http://togogenome.org/gene/9606:OR1S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGQ3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1S2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150452|||http://purl.uniprot.org/annotation/VAR_059980|||http://purl.uniprot.org/annotation/VAR_059981|||http://purl.uniprot.org/annotation/VAR_062013
http://togogenome.org/gene/9606:AMER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  APC membrane recruitment protein 1|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-166; A-181 and A-183.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-166 and A-181.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-166 and A-183.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-181 and A-183.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-83; A-166; A-181 and A-183.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-79; A-83; A-166; A-181 and A-183.|||Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-58; A-79; A-83; A-166; A-181 and A-183.|||Acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281887|||http://purl.uniprot.org/annotation/VAR_031304|||http://purl.uniprot.org/annotation/VAR_053870|||http://purl.uniprot.org/annotation/VAR_053871|||http://purl.uniprot.org/annotation/VAR_076268|||http://purl.uniprot.org/annotation/VSP_024091|||http://purl.uniprot.org/annotation/VSP_024092
http://togogenome.org/gene/9606:PDE3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14432                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||In HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; changed function in cAMP-mediated signaling.|||In HTNB; increased 3',5'-cyclic-AMP phosphodiesterase activity; increased function in cAMP-mediated signaling.|||In HTNB; increased phosphorylation at S-428 and S-438; increased affinity for 3',5'-cyclic-AMP; no effect on protein reaction kinetics for 3',5'-cyclic-AMP phosphodiesterase activity; increased 3',5'-cyclic-AMP phosphodiesterase activity; no effect on inhibition by 3',5'-cyclic-GMP; changed function in cAMP-mediated signaling.|||Interaction with SLFN12|||Loss of interaction with SLFN12.|||PDEase|||Phosphoserine|||Phosphoserine; by PKA and PKC|||Phosphothreonine|||Polar residues|||Proton donor|||cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198799|||http://purl.uniprot.org/annotation/VAR_059543|||http://purl.uniprot.org/annotation/VAR_073869|||http://purl.uniprot.org/annotation/VAR_073870|||http://purl.uniprot.org/annotation/VAR_073871|||http://purl.uniprot.org/annotation/VAR_073872|||http://purl.uniprot.org/annotation/VAR_073873|||http://purl.uniprot.org/annotation/VAR_073874
http://togogenome.org/gene/9606:NOP58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2X3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Nop|||Nucleolar protein 58|||Phosphoserine|||Phosphothreonine|||Restricted to nucleoplasm. Abolishes interaction with NOPCHAP1.|||Restricted to nucleoplasm. Decreases interaction with NOPCHAP1.|||Sufficient for interaction with NOPCHAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219023|||http://purl.uniprot.org/annotation/VAR_059461|||http://purl.uniprot.org/annotation/VAR_059462|||http://purl.uniprot.org/annotation/VAR_059463|||http://purl.uniprot.org/annotation/VAR_059464
http://togogenome.org/gene/9606:LOC102724560                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35520                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Associated with 1/3 to 2/3 the enzyme activity of the wild-type.|||Basic and acidic residues|||CBS|||Cystathionine beta-synthase|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In CBSD.|||In CBSD; 4% of activity; stable.|||In CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation.|||In CBSD; common mutation in Irish population; loss of activity.|||In CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates.|||In CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation.|||In CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation.|||In CBSD; decreased cystathionine beta-synthase activity; increased aggregation.|||In CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation.|||In CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation.|||In CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; has 36% of wild-type enzyme activity.|||In CBSD; has significantly decreased levels of enzyme activity.|||In CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; linked with C-369.|||In CBSD; linked with Q-125; loss of activity.|||In CBSD; linked with S-307.|||In CBSD; linked with V-114; 18% of activity.|||In CBSD; loss of activity.|||In CBSD; loss of cystathionine beta-synthase activity.|||In CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation.|||In CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation.|||In CBSD; loss of expression.|||In CBSD; mild form.|||In CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability.|||In CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure.|||In CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates.|||In CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates.|||In CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure.|||In CBSD; moderate form.|||In CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation.|||In CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity.|||In CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet.|||In CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation.|||In CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation.|||In CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation.|||In CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure.|||In CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure.|||In CBSD; protein expression is comparable to wild-type; loss of activity.|||In CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure.|||In CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity.|||In CBSD; severe form.|||In CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates.|||In CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation.|||In CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation.|||In CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation.|||In CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure.|||In CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation.|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure.|||Reduced heme content and cystathionine beta-synthase activity.|||axial binding residue ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167133|||http://purl.uniprot.org/annotation/VAR_002171|||http://purl.uniprot.org/annotation/VAR_002172|||http://purl.uniprot.org/annotation/VAR_002173|||http://purl.uniprot.org/annotation/VAR_002174|||http://purl.uniprot.org/annotation/VAR_002175|||http://purl.uniprot.org/annotation/VAR_002176|||http://purl.uniprot.org/annotation/VAR_002177|||http://purl.uniprot.org/annotation/VAR_002178|||http://purl.uniprot.org/annotation/VAR_002179|||http://purl.uniprot.org/annotation/VAR_002180|||http://purl.uniprot.org/annotation/VAR_002181|||http://purl.uniprot.org/annotation/VAR_002182|||http://purl.uniprot.org/annotation/VAR_002183|||http://purl.uniprot.org/annotation/VAR_002184|||http://purl.uniprot.org/annotation/VAR_002185|||http://purl.uniprot.org/annotation/VAR_002186|||http://purl.uniprot.org/annotation/VAR_002187|||http://purl.uniprot.org/annotation/VAR_002188|||http://purl.uniprot.org/annotation/VAR_002189|||http://purl.uniprot.org/annotation/VAR_002190|||http://purl.uniprot.org/annotation/VAR_002191|||http://purl.uniprot.org/annotation/VAR_002192|||http://purl.uniprot.org/annotation/VAR_002193|||http://purl.uniprot.org/annotation/VAR_002194|||http://purl.uniprot.org/annotation/VAR_008049|||http://purl.uniprot.org/annotation/VAR_008050|||http://purl.uniprot.org/annotation/VAR_008051|||http://purl.uniprot.org/annotation/VAR_008052|||http://purl.uniprot.org/annotation/VAR_008053|||http://purl.uniprot.org/annotation/VAR_008054|||http://purl.uniprot.org/annotation/VAR_008055|||http://purl.uniprot.org/annotation/VAR_008056|||http://purl.uniprot.org/annotation/VAR_008057|||http://purl.uniprot.org/annotation/VAR_008058|||http://purl.uniprot.org/annotation/VAR_008059|||http://purl.uniprot.org/annotation/VAR_008060|||http://purl.uniprot.org/annotation/VAR_008061|||http://purl.uniprot.org/annotation/VAR_008062|||http://purl.uniprot.org/annotation/VAR_008063|||http://purl.uniprot.org/annotation/VAR_008064|||http://purl.uniprot.org/annotation/VAR_008065|||http://purl.uniprot.org/annotation/VAR_008066|||http://purl.uniprot.org/annotation/VAR_008067|||http://purl.uniprot.org/annotation/VAR_008068|||http://purl.uniprot.org/annotation/VAR_008069|||http://purl.uniprot.org/annotation/VAR_008070|||http://purl.uniprot.org/annotation/VAR_008071|||http://purl.uniprot.org/annotation/VAR_008072|||http://purl.uniprot.org/annotation/VAR_008073|||http://purl.uniprot.org/annotation/VAR_008074|||http://purl.uniprot.org/annotation/VAR_008075|||http://purl.uniprot.org/annotation/VAR_008076|||http://purl.uniprot.org/annotation/VAR_008077|||http://purl.uniprot.org/annotation/VAR_008078|||http://purl.uniprot.org/annotation/VAR_008079|||http://purl.uniprot.org/annotation/VAR_008080|||http://purl.uniprot.org/annotation/VAR_008081|||http://purl.uniprot.org/annotation/VAR_008082|||http://purl.uniprot.org/annotation/VAR_008083|||http://purl.uniprot.org/annotation/VAR_008084|||http://purl.uniprot.org/annotation/VAR_008085|||http://purl.uniprot.org/annotation/VAR_008086|||http://purl.uniprot.org/annotation/VAR_008087|||http://purl.uniprot.org/annotation/VAR_008088|||http://purl.uniprot.org/annotation/VAR_008089|||http://purl.uniprot.org/annotation/VAR_008090|||http://purl.uniprot.org/annotation/VAR_008091|||http://purl.uniprot.org/annotation/VAR_008092|||http://purl.uniprot.org/annotation/VAR_008093|||http://purl.uniprot.org/annotation/VAR_021790|||http://purl.uniprot.org/annotation/VAR_021791|||http://purl.uniprot.org/annotation/VAR_021792|||http://purl.uniprot.org/annotation/VAR_021793|||http://purl.uniprot.org/annotation/VAR_021794|||http://purl.uniprot.org/annotation/VAR_021795|||http://purl.uniprot.org/annotation/VAR_021796|||http://purl.uniprot.org/annotation/VAR_021797|||http://purl.uniprot.org/annotation/VAR_021798|||http://purl.uniprot.org/annotation/VAR_021799|||http://purl.uniprot.org/annotation/VAR_021800|||http://purl.uniprot.org/annotation/VAR_021801|||http://purl.uniprot.org/annotation/VAR_021802|||http://purl.uniprot.org/annotation/VAR_021803|||http://purl.uniprot.org/annotation/VAR_046921|||http://purl.uniprot.org/annotation/VAR_046922|||http://purl.uniprot.org/annotation/VAR_046923|||http://purl.uniprot.org/annotation/VAR_046924|||http://purl.uniprot.org/annotation/VAR_046925|||http://purl.uniprot.org/annotation/VAR_046926|||http://purl.uniprot.org/annotation/VAR_046927|||http://purl.uniprot.org/annotation/VAR_046928|||http://purl.uniprot.org/annotation/VAR_046929|||http://purl.uniprot.org/annotation/VAR_046930|||http://purl.uniprot.org/annotation/VAR_046931|||http://purl.uniprot.org/annotation/VAR_046932|||http://purl.uniprot.org/annotation/VAR_046933|||http://purl.uniprot.org/annotation/VAR_046934|||http://purl.uniprot.org/annotation/VAR_046935|||http://purl.uniprot.org/annotation/VAR_046936|||http://purl.uniprot.org/annotation/VAR_046937|||http://purl.uniprot.org/annotation/VAR_046938|||http://purl.uniprot.org/annotation/VAR_066098|||http://purl.uniprot.org/annotation/VAR_066099|||http://purl.uniprot.org/annotation/VAR_066100|||http://purl.uniprot.org/annotation/VAR_066101|||http://purl.uniprot.org/annotation/VAR_066102|||http://purl.uniprot.org/annotation/VAR_066103|||http://purl.uniprot.org/annotation/VAR_074590|||http://purl.uniprot.org/annotation/VAR_074591|||http://purl.uniprot.org/annotation/VAR_074592|||http://purl.uniprot.org/annotation/VAR_074593|||http://purl.uniprot.org/annotation/VAR_074594|||http://purl.uniprot.org/annotation/VAR_074595|||http://purl.uniprot.org/annotation/VSP_001217
http://togogenome.org/gene/9606:FXYD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54710                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||In HOMG2; fails to localize to plasma membrane.|||In isoform 2.|||Sodium/potassium-transporting ATPase subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148185|||http://purl.uniprot.org/annotation/VAR_013280|||http://purl.uniprot.org/annotation/VSP_001580
http://togogenome.org/gene/9606:CUL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93034                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Cullin-5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119797
http://togogenome.org/gene/9606:UNC5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BXJ2|||http://purl.uniprot.org/uniprot/Q6UXZ4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase-3|||Cytoplasmic|||Death|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Important for interaction with FLRT2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Netrin receptor UNC5|||Netrin receptor UNC5D|||TSP type-1 1|||TSP type-1 2|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036079|||http://purl.uniprot.org/annotation/PRO_5025092123|||http://purl.uniprot.org/annotation/VAR_059848|||http://purl.uniprot.org/annotation/VSP_011703
http://togogenome.org/gene/9606:ARMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVT9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ARM|||Armadillo repeat-containing protein 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240882|||http://purl.uniprot.org/annotation/VSP_054645|||http://purl.uniprot.org/annotation/VSP_054646
http://togogenome.org/gene/9606:PHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78364|||http://purl.uniprot.org/uniprot/Q6GMQ3|||http://purl.uniprot.org/uniprot/Q6N083                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FCS-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MCPH11; significant reduction in mutant protein levels which is shown to result from proteasome-mediated degradation; patient cells show increased expression of GMNN and decreased interaction between the protein and ubiquitinated H2AC17 compared to control cells.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Polyhomeotic-like protein 1|||Pro residues|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058375|||http://purl.uniprot.org/annotation/VAR_054503|||http://purl.uniprot.org/annotation/VAR_070566
http://togogenome.org/gene/9606:HINT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQE9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  2.5-fold increase in affinity for indolepropinoic acyl-adenylate and cytosine; 2-fold decrease in hypoxanthine affinity; nearly no change in affinity for adenine, guanine and uracil.|||Abolishes adenosine 5'-monophosphoramidase activity.|||Adenosine 5'-monophosphoramidase HINT3|||Disordered|||HIT|||Histidine triad motif|||N-acetylalanine|||Removed|||Tele-AMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324327|||http://purl.uniprot.org/annotation/VAR_039734
http://togogenome.org/gene/9606:SIX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIU6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX4|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049303|||http://purl.uniprot.org/annotation/VAR_036441|||http://purl.uniprot.org/annotation/VAR_036442|||http://purl.uniprot.org/annotation/VAR_036443|||http://purl.uniprot.org/annotation/VAR_058281
http://togogenome.org/gene/9606:PRAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XND8|||http://purl.uniprot.org/uniprot/Q96NZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Proline-rich acidic protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299416|||http://purl.uniprot.org/annotation/PRO_5002704951|||http://purl.uniprot.org/annotation/VAR_034815|||http://purl.uniprot.org/annotation/VAR_034816|||http://purl.uniprot.org/annotation/VAR_034817|||http://purl.uniprot.org/annotation/VAR_034818|||http://purl.uniprot.org/annotation/VSP_027660|||http://purl.uniprot.org/annotation/VSP_027661|||http://purl.uniprot.org/annotation/VSP_027662
http://togogenome.org/gene/9606:TPM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7XZE4|||http://purl.uniprot.org/uniprot/P07951|||http://purl.uniprot.org/uniprot/Q5TCU3|||http://purl.uniprot.org/uniprot/V9HW25                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In CAPM2.|||In CAPM2; also found in a patient with congenital myopathy with fiber-type disproportion.|||In DA1A.|||In DA1A; also found in a patient with congenital myopathy with fiber-type disproportion.|||In DA1A; also found in patients with undefined congenital myopathy.|||In DA2B4, NEM4 and DA1A; also found in a patient with congenital myopathy with fiber-type disproportion.|||In DA2B4; unknown pathological significance.|||In NEM4.|||In NEM4; also found in a patient with congenital myopathy with fiber-type disproportion and patients with undefined congenital myopathy.|||In NEM4; also found in a patient with congenital myopathy with fiber-type disproportion.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PIK3CG|||Phosphothreonine|||Phosphotyrosine|||Probable disease-associated variant found in a patient with congenital myopathy with fiber-type disproportion and patients with undefined congenital myopathy.|||Probable disease-associated variant found in patients with undefined congenital myopathy.|||The measured range is 1-284.|||Tropomyosin beta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205627|||http://purl.uniprot.org/annotation/VAR_013468|||http://purl.uniprot.org/annotation/VAR_013469|||http://purl.uniprot.org/annotation/VAR_016086|||http://purl.uniprot.org/annotation/VAR_052402|||http://purl.uniprot.org/annotation/VAR_070978|||http://purl.uniprot.org/annotation/VAR_070979|||http://purl.uniprot.org/annotation/VAR_070980|||http://purl.uniprot.org/annotation/VAR_070981|||http://purl.uniprot.org/annotation/VAR_070982|||http://purl.uniprot.org/annotation/VAR_070983|||http://purl.uniprot.org/annotation/VAR_071485|||http://purl.uniprot.org/annotation/VAR_071486|||http://purl.uniprot.org/annotation/VAR_071487|||http://purl.uniprot.org/annotation/VAR_071488|||http://purl.uniprot.org/annotation/VAR_071489|||http://purl.uniprot.org/annotation/VAR_071490|||http://purl.uniprot.org/annotation/VAR_071491|||http://purl.uniprot.org/annotation/VAR_071492|||http://purl.uniprot.org/annotation/VAR_071493|||http://purl.uniprot.org/annotation/VAR_071494|||http://purl.uniprot.org/annotation/VAR_071495|||http://purl.uniprot.org/annotation/VAR_071496|||http://purl.uniprot.org/annotation/VAR_071497|||http://purl.uniprot.org/annotation/VAR_071498|||http://purl.uniprot.org/annotation/VAR_082273|||http://purl.uniprot.org/annotation/VSP_006594|||http://purl.uniprot.org/annotation/VSP_006595|||http://purl.uniprot.org/annotation/VSP_006596
http://togogenome.org/gene/9606:EBPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRV2|||http://purl.uniprot.org/uniprot/Q9BY08                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  EXPERA|||Emopamil-binding protein-like|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174347|||http://purl.uniprot.org/annotation/VSP_035417|||http://purl.uniprot.org/annotation/VSP_035418|||http://purl.uniprot.org/annotation/VSP_035419|||http://purl.uniprot.org/annotation/VSP_035420|||http://purl.uniprot.org/annotation/VSP_035421|||http://purl.uniprot.org/annotation/VSP_035422|||http://purl.uniprot.org/annotation/VSP_035423|||http://purl.uniprot.org/annotation/VSP_035424|||http://purl.uniprot.org/annotation/VSP_035425
http://togogenome.org/gene/9606:PANO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I0J062                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Necessary for nucleolar localization|||Proapoptotic nucleolar protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431904
http://togogenome.org/gene/9606:ZNF275                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFS0                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:C3orf70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Polar residues|||UPF0524 protein C3orf70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319976
http://togogenome.org/gene/9606:SLC45A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JT2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Solute carrier family 45 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122519
http://togogenome.org/gene/9606:CABS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Calcium-binding and spermatid-specific protein 1|||Disordered|||Phosphoserine|||Phosphothreonine; by CK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339178|||http://purl.uniprot.org/annotation/VAR_043924|||http://purl.uniprot.org/annotation/VAR_043925|||http://purl.uniprot.org/annotation/VAR_043926
http://togogenome.org/gene/9606:MVB12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7P6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MABP|||Multivesicular body subunit 12B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||UMA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249074|||http://purl.uniprot.org/annotation/VSP_020364
http://togogenome.org/gene/9606:SENP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QT09|||http://purl.uniprot.org/uniprot/Q9BQF6                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Nucleophile|||Phosphoserine|||Polar residues|||Protease|||Reduces deconjugation activity.|||Sentrin-specific protease 7|||Slightly increased deconjugation activity.|||Ubiquitin-like protease family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101726|||http://purl.uniprot.org/annotation/VAR_029651|||http://purl.uniprot.org/annotation/VAR_029652|||http://purl.uniprot.org/annotation/VSP_039498|||http://purl.uniprot.org/annotation/VSP_039499|||http://purl.uniprot.org/annotation/VSP_039500|||http://purl.uniprot.org/annotation/VSP_039501|||http://purl.uniprot.org/annotation/VSP_039502
http://togogenome.org/gene/9606:HNRNPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUQ1|||http://purl.uniprot.org/uniprot/P61978                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||2 X 22 AA approximate repeats|||2 X 6 AA approximate repeats|||2-1|||2-2|||3-1|||3-2|||3-3|||3-4|||3-5|||5 X 4 AA repeats of G-X-G-G|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein K|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with ASFV p30|||Interaction with ZIK1|||K Homology|||KH 1|||KH 2|||KH 3|||Loss of sumoylation.|||Loss of sumoylation. Loss of TP53 transcriptional stimulation.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Necessary for interaction with DDX1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RNA-binding RGG-box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050096|||http://purl.uniprot.org/annotation/VSP_002822|||http://purl.uniprot.org/annotation/VSP_021669
http://togogenome.org/gene/9606:RYR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RRH1|||http://purl.uniprot.org/uniprot/Q15413                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X approximate repeats|||B30.2/SPRY|||B30.2/SPRY 1|||B30.2/SPRY 2|||B30.2/SPRY 3|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EF-hand|||Helical|||Important for activation by Ca(2+)|||In CMYP20; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with CALM|||Interaction with FKBP1A|||MIR|||MIR 1|||MIR 2|||MIR 3|||MIR 4|||MIR 5|||Pore-forming|||Ryanodine receptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219363|||http://purl.uniprot.org/annotation/VAR_011404|||http://purl.uniprot.org/annotation/VAR_011405|||http://purl.uniprot.org/annotation/VAR_011406|||http://purl.uniprot.org/annotation/VAR_011407|||http://purl.uniprot.org/annotation/VAR_024077|||http://purl.uniprot.org/annotation/VAR_024078|||http://purl.uniprot.org/annotation/VAR_057166|||http://purl.uniprot.org/annotation/VAR_088349|||http://purl.uniprot.org/annotation/VAR_088350|||http://purl.uniprot.org/annotation/VAR_088351|||http://purl.uniprot.org/annotation/VAR_088352|||http://purl.uniprot.org/annotation/VSP_005954|||http://purl.uniprot.org/annotation/VSP_005955|||http://purl.uniprot.org/annotation/VSP_005956
http://togogenome.org/gene/9606:UNC50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z612|||http://purl.uniprot.org/uniprot/J3KQ47|||http://purl.uniprot.org/uniprot/Q53HI1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Protein unc-50 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308961
http://togogenome.org/gene/9606:FRAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75474                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||GSK-3-binding protein FRAT2|||Involved in GSK-3 binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087334
http://togogenome.org/gene/9606:C6orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZU0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Uncharacterized protein C6orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089514|||http://purl.uniprot.org/annotation/VAR_050803|||http://purl.uniprot.org/annotation/VAR_050804|||http://purl.uniprot.org/annotation/VSP_015616|||http://purl.uniprot.org/annotation/VSP_015617
http://togogenome.org/gene/9606:CT47A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:NAPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZQ7|||http://purl.uniprot.org/uniprot/Q9H115                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Beta-soluble NSF attachment protein|||In DEE107.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219060|||http://purl.uniprot.org/annotation/VAR_052026|||http://purl.uniprot.org/annotation/VAR_087810|||http://purl.uniprot.org/annotation/VAR_087811|||http://purl.uniprot.org/annotation/VSP_055276|||http://purl.uniprot.org/annotation/VSP_055277|||http://purl.uniprot.org/annotation/VSP_055278
http://togogenome.org/gene/9606:ZNF512                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DES6|||http://purl.uniprot.org/uniprot/B7Z9P6|||http://purl.uniprot.org/uniprot/Q96ME7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Zinc finger protein 512                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047630|||http://purl.uniprot.org/annotation/VSP_046933|||http://purl.uniprot.org/annotation/VSP_046934|||http://purl.uniprot.org/annotation/VSP_046935
http://togogenome.org/gene/9606:UPK1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00322                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Uroplakin-1a                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219286|||http://purl.uniprot.org/annotation/VAR_020094|||http://purl.uniprot.org/annotation/VAR_052332|||http://purl.uniprot.org/annotation/VSP_030005
http://togogenome.org/gene/9606:NUP160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12769                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In NPHS19; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Nuclear pore complex protein Nup160|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204851|||http://purl.uniprot.org/annotation/VAR_055409|||http://purl.uniprot.org/annotation/VAR_055410|||http://purl.uniprot.org/annotation/VAR_081362|||http://purl.uniprot.org/annotation/VAR_081363|||http://purl.uniprot.org/annotation/VAR_083006|||http://purl.uniprot.org/annotation/VSP_007093|||http://purl.uniprot.org/annotation/VSP_007094|||http://purl.uniprot.org/annotation/VSP_037350|||http://purl.uniprot.org/annotation/VSP_037351|||http://purl.uniprot.org/annotation/VSP_037352|||http://purl.uniprot.org/annotation/VSP_037353
http://togogenome.org/gene/9606:H2BC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33778                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-B|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071832
http://togogenome.org/gene/9606:SLC35G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBE7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EamA 1|||EamA 2|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Phosphoserine|||Solute carrier family 35 member G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244465|||http://purl.uniprot.org/annotation/VAR_026907
http://togogenome.org/gene/9606:CETP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3F6|||http://purl.uniprot.org/uniprot/A0A0S2Z3I8|||http://purl.uniprot.org/uniprot/B4DMZ5|||http://purl.uniprot.org/uniprot/P11597                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cholesteryl ester transfer protein|||In HALP1.|||In HALP1; reduced secretion into plasma.|||In isoform 2.|||Lipid-binding serum glycoprotein C-terminal|||Lipid-binding serum glycoprotein N-terminal|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Not secreted.|||Reduces activity by 60%.|||Reduces cholesteryl ester transfer by 60%.|||Reduces triglyceride transfer 10-fold. No effect on cholesteryl ester transfer.|||Reduces triglyceride transfer 10-fold. Slight reduction of cholesteryl ester transfer.|||Reduces triglyceride transfer 5-fold. Slight reduction of cholesteryl ester transfer.|||Reduces triglyceride transfer and cholesteryl ester transfer 5-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017155|||http://purl.uniprot.org/annotation/PRO_5014239307|||http://purl.uniprot.org/annotation/PRO_5014239323|||http://purl.uniprot.org/annotation/PRO_5015219175|||http://purl.uniprot.org/annotation/VAR_004172|||http://purl.uniprot.org/annotation/VAR_013919|||http://purl.uniprot.org/annotation/VAR_013920|||http://purl.uniprot.org/annotation/VAR_013921|||http://purl.uniprot.org/annotation/VAR_013922|||http://purl.uniprot.org/annotation/VAR_013923|||http://purl.uniprot.org/annotation/VAR_017018|||http://purl.uniprot.org/annotation/VAR_017019|||http://purl.uniprot.org/annotation/VAR_031127|||http://purl.uniprot.org/annotation/VAR_033098|||http://purl.uniprot.org/annotation/VAR_033099|||http://purl.uniprot.org/annotation/VAR_033100|||http://purl.uniprot.org/annotation/VSP_023645
http://togogenome.org/gene/9606:TMEM212                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NML5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 212                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341207
http://togogenome.org/gene/9606:ACADS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUH1|||http://purl.uniprot.org/uniprot/E5KSD5|||http://purl.uniprot.org/uniprot/E9PE82|||http://purl.uniprot.org/uniprot/P16219                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria.|||86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria.|||Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||In ACADSD.|||In ACADSD; loss of acyl-CoA dehydrogenase activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphothreonine|||Proton acceptor|||Short-chain specific acyl-CoA dehydrogenase, mitochondrial|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000498|||http://purl.uniprot.org/annotation/VAR_000310|||http://purl.uniprot.org/annotation/VAR_000311|||http://purl.uniprot.org/annotation/VAR_000312|||http://purl.uniprot.org/annotation/VAR_000314|||http://purl.uniprot.org/annotation/VAR_000315|||http://purl.uniprot.org/annotation/VAR_000316|||http://purl.uniprot.org/annotation/VAR_013565|||http://purl.uniprot.org/annotation/VAR_013566|||http://purl.uniprot.org/annotation/VAR_013567|||http://purl.uniprot.org/annotation/VAR_013568|||http://purl.uniprot.org/annotation/VAR_013569|||http://purl.uniprot.org/annotation/VAR_013570|||http://purl.uniprot.org/annotation/VAR_013571|||http://purl.uniprot.org/annotation/VAR_033458
http://togogenome.org/gene/9606:DAZ4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658T2|||http://purl.uniprot.org/uniprot/Q86SG3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  DAZ|||DAZ 1|||DAZ 2|||DAZ 3|||DAZ 4|||DAZ 5|||DAZ 6|||DAZ 7|||DAZ 8|||DAZ 9|||Deleted in azoospermia protein 4|||Disordered|||In isoform 2.|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081557|||http://purl.uniprot.org/annotation/PRO_5004268262|||http://purl.uniprot.org/annotation/VSP_009454|||http://purl.uniprot.org/annotation/VSP_009455|||http://purl.uniprot.org/annotation/VSP_009456
http://togogenome.org/gene/9606:EPHA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29317                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 2|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In CTRCT6; reduced protein stability and reduced ability to stimulate cell migration in absence of its ephrin ligand.|||In CTRCT6; retained in the cytoplasm and constitutively active it alters EPHA2 signaling.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Increases serum-induced chemotaxis. Loss of EFNA1-dependent regulation of cell migration.|||Loss of kinase activity.|||Loss of serum-induced phosphorylation by PKB. Loss of serum-induced chemotaxis.|||Mediates interaction with ARHGEF16 and ELMO2|||Mediates interaction with CLDN4|||N-linked (GlcNAc...) asparagine|||Negatively regulates interaction with ARHGEF16|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKB/AKT1, RPS6KA1, RPS6KA3 AND PKA|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM|||Significantly reduced response to EFNA1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016800|||http://purl.uniprot.org/annotation/VAR_042121|||http://purl.uniprot.org/annotation/VAR_042122|||http://purl.uniprot.org/annotation/VAR_042123|||http://purl.uniprot.org/annotation/VAR_042124|||http://purl.uniprot.org/annotation/VAR_042125|||http://purl.uniprot.org/annotation/VAR_055989|||http://purl.uniprot.org/annotation/VAR_055990|||http://purl.uniprot.org/annotation/VAR_058907|||http://purl.uniprot.org/annotation/VAR_058908|||http://purl.uniprot.org/annotation/VAR_062532|||http://purl.uniprot.org/annotation/VSP_056014|||http://purl.uniprot.org/annotation/VSP_056015
http://togogenome.org/gene/9606:KIAA1671                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Uncharacterized protein KIAA1671                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287145|||http://purl.uniprot.org/annotation/VSP_025337|||http://purl.uniprot.org/annotation/VSP_025338
http://togogenome.org/gene/9606:AP4S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y587                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  AP-4 complex subunit sigma-1|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193820|||http://purl.uniprot.org/annotation/VSP_040023|||http://purl.uniprot.org/annotation/VSP_046364|||http://purl.uniprot.org/annotation/VSP_046941
http://togogenome.org/gene/9606:FAM153A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYN1|||http://purl.uniprot.org/uniprot/A0A8V8TKN8|||http://purl.uniprot.org/uniprot/A0A8V8TM68|||http://purl.uniprot.org/uniprot/Q9UHL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM153A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318156
http://togogenome.org/gene/9606:PMM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4J6|||http://purl.uniprot.org/uniprot/O15305|||http://purl.uniprot.org/uniprot/Q59F02                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CDG1A.|||In CDG1A; frequent mutation; loss of activity; observed in heterozygous patients; homozygosis of this mutation is incompatible with life.|||In CDG1A; loss of activity.|||In CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate.|||In CDG1A; partial loss of activity.|||In CDG1A; reduction of activity.|||In CDG1A; severe.|||In CDG1A; slightly reduced activity.|||In CDG1A; this mutation seems to disrupt a splicing enhancer sequence and thus results in most cases in a protein with exon 5 skipped; slightly reduced activity.|||In CDG1A; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Nucleophile|||Phosphomannomutase 2|||Proton donor/acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199694|||http://purl.uniprot.org/annotation/VAR_006093|||http://purl.uniprot.org/annotation/VAR_006094|||http://purl.uniprot.org/annotation/VAR_006095|||http://purl.uniprot.org/annotation/VAR_006096|||http://purl.uniprot.org/annotation/VAR_006097|||http://purl.uniprot.org/annotation/VAR_006098|||http://purl.uniprot.org/annotation/VAR_006099|||http://purl.uniprot.org/annotation/VAR_006100|||http://purl.uniprot.org/annotation/VAR_006101|||http://purl.uniprot.org/annotation/VAR_006102|||http://purl.uniprot.org/annotation/VAR_006103|||http://purl.uniprot.org/annotation/VAR_006104|||http://purl.uniprot.org/annotation/VAR_006105|||http://purl.uniprot.org/annotation/VAR_006106|||http://purl.uniprot.org/annotation/VAR_006107|||http://purl.uniprot.org/annotation/VAR_006108|||http://purl.uniprot.org/annotation/VAR_006109|||http://purl.uniprot.org/annotation/VAR_006110|||http://purl.uniprot.org/annotation/VAR_006111|||http://purl.uniprot.org/annotation/VAR_006112|||http://purl.uniprot.org/annotation/VAR_006113|||http://purl.uniprot.org/annotation/VAR_006114|||http://purl.uniprot.org/annotation/VAR_006115|||http://purl.uniprot.org/annotation/VAR_006116|||http://purl.uniprot.org/annotation/VAR_009232|||http://purl.uniprot.org/annotation/VAR_012344|||http://purl.uniprot.org/annotation/VAR_022133|||http://purl.uniprot.org/annotation/VAR_022134|||http://purl.uniprot.org/annotation/VAR_022469|||http://purl.uniprot.org/annotation/VAR_022470|||http://purl.uniprot.org/annotation/VAR_022471|||http://purl.uniprot.org/annotation/VAR_022472|||http://purl.uniprot.org/annotation/VAR_022473|||http://purl.uniprot.org/annotation/VAR_022474|||http://purl.uniprot.org/annotation/VAR_022475|||http://purl.uniprot.org/annotation/VAR_022476|||http://purl.uniprot.org/annotation/VAR_022477|||http://purl.uniprot.org/annotation/VAR_022478|||http://purl.uniprot.org/annotation/VAR_022479|||http://purl.uniprot.org/annotation/VAR_022480|||http://purl.uniprot.org/annotation/VAR_022481|||http://purl.uniprot.org/annotation/VAR_022482|||http://purl.uniprot.org/annotation/VAR_022483|||http://purl.uniprot.org/annotation/VAR_022484|||http://purl.uniprot.org/annotation/VAR_022485|||http://purl.uniprot.org/annotation/VAR_022486|||http://purl.uniprot.org/annotation/VAR_022487|||http://purl.uniprot.org/annotation/VAR_022488|||http://purl.uniprot.org/annotation/VAR_022489|||http://purl.uniprot.org/annotation/VAR_022490|||http://purl.uniprot.org/annotation/VAR_022491|||http://purl.uniprot.org/annotation/VAR_022492|||http://purl.uniprot.org/annotation/VAR_022493|||http://purl.uniprot.org/annotation/VAR_022494|||http://purl.uniprot.org/annotation/VAR_022495|||http://purl.uniprot.org/annotation/VAR_022496|||http://purl.uniprot.org/annotation/VAR_022497|||http://purl.uniprot.org/annotation/VAR_022498|||http://purl.uniprot.org/annotation/VAR_022499|||http://purl.uniprot.org/annotation/VAR_022500|||http://purl.uniprot.org/annotation/VAR_022501|||http://purl.uniprot.org/annotation/VAR_022502|||http://purl.uniprot.org/annotation/VAR_022503|||http://purl.uniprot.org/annotation/VAR_022504|||http://purl.uniprot.org/annotation/VAR_022505|||http://purl.uniprot.org/annotation/VAR_022506|||http://purl.uniprot.org/annotation/VAR_022507|||http://purl.uniprot.org/annotation/VAR_022508|||http://purl.uniprot.org/annotation/VAR_022509|||http://purl.uniprot.org/annotation/VAR_022510|||http://purl.uniprot.org/annotation/VAR_022563|||http://purl.uniprot.org/annotation/VSP_056228|||http://purl.uniprot.org/annotation/VSP_056229
http://togogenome.org/gene/9606:MFSD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNN7|||http://purl.uniprot.org/uniprot/E7EPI8|||http://purl.uniprot.org/uniprot/Q71RE4|||http://purl.uniprot.org/uniprot/Q8NA29                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished lysophosphatidylcholine (LPC) transport.|||Cytoplasmic|||Disordered|||Does not affect lysophosphatidylcholine (LPC) transport.|||Drastic loss of cell sensitivity toward tunicamycin. Abolished lysophosphatidylcholine (LPC) transport.|||Extracellular|||Helical|||In NEDMISBA; no effect on cell membrane localization; decreased LPC transport activity.|||In NEDMISBA; no effect on cell membrane localization; loss of LPC transport activity.|||In NEDMISBA; reduced expression; no effect on cell membrane localization; decreased LPC transport activity.|||In NEDMISBA; reduced expression; no effect on cell membrane localization; loss of LPC transport activity.|||In NEDMISBA; reduced expression; no effect on cell membrane localization; no effect on LPC transport activity.|||In NEDMISBA; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Loss of glycosylation; when associated with Q-230.|||Loss of glycosylation; when associated with Q-240.|||Loss of plasma membrane localization. Loss of cell sensitivity toward tunicamycin.|||N-linked (GlcNAc...) asparagine|||No effect on cell sensitivity toward tunicamycin.|||Reduced expression; no effect on cell membrane localization; decreased LPC transport activity.|||Reduced lysophosphatidylcholine (LPC) transport.|||Sodium-dependent lysophosphatidylcholine symporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273387|||http://purl.uniprot.org/annotation/VAR_074624|||http://purl.uniprot.org/annotation/VAR_074625|||http://purl.uniprot.org/annotation/VAR_074626|||http://purl.uniprot.org/annotation/VAR_085538|||http://purl.uniprot.org/annotation/VAR_085539|||http://purl.uniprot.org/annotation/VAR_085540|||http://purl.uniprot.org/annotation/VAR_085541|||http://purl.uniprot.org/annotation/VAR_085542|||http://purl.uniprot.org/annotation/VSP_022539|||http://purl.uniprot.org/annotation/VSP_022540
http://togogenome.org/gene/9606:TIMMDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JU35|||http://purl.uniprot.org/uniprot/Q9NPL8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Complex I assembly factor TIMMDC1, mitochondrial|||Helical|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252478|||http://purl.uniprot.org/annotation/PRO_5002997858|||http://purl.uniprot.org/annotation/VAR_027885|||http://purl.uniprot.org/annotation/VAR_061572
http://togogenome.org/gene/9606:ZNF765                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L2R6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; atypical|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 765                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344217|||http://purl.uniprot.org/annotation/VAR_045598|||http://purl.uniprot.org/annotation/VSP_034746|||http://purl.uniprot.org/annotation/VSP_034747|||http://purl.uniprot.org/annotation/VSP_055629|||http://purl.uniprot.org/annotation/VSP_055630
http://togogenome.org/gene/9606:CCDC152                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0S7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 152|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320586|||http://purl.uniprot.org/annotation/VAR_059596|||http://purl.uniprot.org/annotation/VSP_056904
http://togogenome.org/gene/9606:STXBP5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKF6|||http://purl.uniprot.org/uniprot/E9PFI2|||http://purl.uniprot.org/uniprot/Q9Y2K9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a family with autosomal recessive infantile-onset neurodegenerative disease; unknown pathological significance; loss of axonal outgrowth.|||In isoform 2.|||N-acetylmethionine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Syntaxin-binding protein 5-like|||V-SNARE coiled-coil homology|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051247|||http://purl.uniprot.org/annotation/VAR_050076|||http://purl.uniprot.org/annotation/VAR_050077|||http://purl.uniprot.org/annotation/VAR_081642|||http://purl.uniprot.org/annotation/VSP_016293|||http://purl.uniprot.org/annotation/VSP_016294
http://togogenome.org/gene/9606:LYRM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RBV5|||http://purl.uniprot.org/uniprot/Q5U5X0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Complex 1 LYR protein|||Complex III assembly factor LYRM7|||In MC3DN8; results in impaired incorporation of the Rieske Fe-S protein into the CIII complex.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251179|||http://purl.uniprot.org/annotation/VAR_071187
http://togogenome.org/gene/9606:RAB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ22                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Effector region|||Loss of phosphorylation. No effect on GDI1 and GDI2 binding.|||N-acetylmethionine|||Phosphomimetic mutant. Loss of GDI1, GDI2, CHM and CHML binding.|||Phosphoserine|||Phosphoserine; by LRRK2|||Ras-related protein Rab-12|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271377
http://togogenome.org/gene/9606:ANKRD39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53RE8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 39|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244366|||http://purl.uniprot.org/annotation/VAR_026905
http://togogenome.org/gene/9606:GABRA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K177|||http://purl.uniprot.org/uniprot/P14867                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Completely abolishes potentiation and activation by the agonist alphaxalone.|||Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-1|||Helical|||In DEE19.|||In EIG13; the mutant protein is partially retained in the endoplasmic reticulum and has decreased expression at the plasma membrane; causes decreased current amplitude in response to GABA compared to wild-type and alters receptor gating kinetics including faster desensitization.|||In EJM5.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane|||Reduced potentiation and activation by the agonist alphaxalone.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000428|||http://purl.uniprot.org/annotation/PRO_5022260971|||http://purl.uniprot.org/annotation/VAR_013642|||http://purl.uniprot.org/annotation/VAR_071809|||http://purl.uniprot.org/annotation/VAR_071810|||http://purl.uniprot.org/annotation/VAR_071811|||http://purl.uniprot.org/annotation/VAR_071812|||http://purl.uniprot.org/annotation/VAR_078222
http://togogenome.org/gene/9606:KRTAP13-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LG2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 10 AA approximate repeats|||Keratin-associated protein 13-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185201|||http://purl.uniprot.org/annotation/VAR_053470|||http://purl.uniprot.org/annotation/VAR_053471
http://togogenome.org/gene/9606:CLEC2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92478                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 2 member B|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046611
http://togogenome.org/gene/9606:NMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JA08|||http://purl.uniprot.org/uniprot/Q96D46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  60S ribosomal export protein NMD3|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Necessary for the nuclear export of the 60S ribosomal subunit|||Nmd3 N-terminal|||Nuclear and nucleolar localization signal|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Reduces accumulation in the nucleus. Loss of nucleolar localization; when associated with A-405.|||Reduces accumulation in the nucleus. Loss of nucleolar localization; when associated with A-406.|||Reduces nuclear export.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323561|||http://purl.uniprot.org/annotation/VAR_039546
http://togogenome.org/gene/9606:ACTR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42025                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||Beta-centractin|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089060|||http://purl.uniprot.org/annotation/VAR_025315|||http://purl.uniprot.org/annotation/VAR_048187
http://togogenome.org/gene/9606:KLHL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GT1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||Disordered|||Found in a patient with isolated coloboma; unknown pathological significance.|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 22|||Loss of interaction with YWHAE. Loss of nuclear localization upon amino acid starvation.|||N-acetylalanine|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242155|||http://purl.uniprot.org/annotation/VAR_079854|||http://purl.uniprot.org/annotation/VSP_057028
http://togogenome.org/gene/9606:ENTREP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60320                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Pro residues|||Protein ENTREP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314455|||http://purl.uniprot.org/annotation/VAR_039544|||http://purl.uniprot.org/annotation/VAR_039545|||http://purl.uniprot.org/annotation/VAR_059333|||http://purl.uniprot.org/annotation/VAR_059334|||http://purl.uniprot.org/annotation/VAR_059335|||http://purl.uniprot.org/annotation/VSP_030273
http://togogenome.org/gene/9606:NKX2-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-2.3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048933
http://togogenome.org/gene/9606:TMEM106A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z779|||http://purl.uniprot.org/uniprot/Q96A25                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Transmembrane protein 106A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242137|||http://purl.uniprot.org/annotation/VSP_056642
http://togogenome.org/gene/9606:SPANXN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MJ07                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Sperm protein associated with the nucleus on the X chromosome N5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285542
http://togogenome.org/gene/9606:AIRE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43918                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with histone H3.|||Alters protein folding and abolishes interaction with histone H3. No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.|||Autoimmune regulator|||Disordered|||Dominant-negative effect on regulation of target gene transcription.|||Found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||Found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; unknown pathological significance.|||Found in a patient with pernicious anemia and neuropathy; unknown pathological significance; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||Found in patients with hypothyroidism and organ- and cytokine-specific autoantibodies; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||HSR|||In APS1.|||In APS1; abolishes association with cytoplasmic tubular structures and homodimerization; loss of doted nuclear localization; nuclear smear; severe decrease of transcriptional transactivation activity.|||In APS1; alters folding of the PHD-type 1 zinc finger.|||In APS1; benign variant; does not affect transcriptional transactivation activity.|||In APS1; changes the subcellular localization and in addition disrupts the transactivating capacity of the wild-type AIRE; acts with a dominant negative effect by binding to the wild-type AIRE thus preventing the protein from forming the complexes needed for transactivation.|||In APS1; decreases doted nuclear localization.|||In APS1; impairs zinc binding and folding of the PHD-type 1 zinc finger; dominant-negative effect on the regulation of target gene transcription; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||In APS1; loss of homooligomerization.|||In APS1; no effect on homooligomerization; no effect on subcellular localization; no effect on the transcriptional transactivation activity.|||In APS1; no effect on protein structure or on interaction with histone H3; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||In APS1; no significant effect on structure, but may alter protein interactions; no effect on doted nuclear localization; dominant-negative effect on regulation of target gene transcription.|||In APS1; no significant effect on transcriptional transactivation activity.|||In APS1; prevents homodimerization.|||In APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with histone H3 not methylated at 'Lys-4'|||LXXLL motif 1|||LXXLL motif 2|||LXXLL motif 3|||LXXLL motif 4|||Loss of doted nuclear location, forms nuclear smears. Loss of transactivation activity on target genes transcription.|||Loss of transactivation activity on target gene transcription; no dominant-negative effect on target gene transcription. Loss of doted nuclear localization.|||No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.|||No effect on regulation of target gene transcription.|||PHD-type 1|||PHD-type 2|||Reduces interaction with histone H3.|||Reduces transcription activation.|||Reduces transcriptional activation.|||SAND|||Strongly reduces interaction with histone H3.|||Strongly reduces interaction with unmethylated histone H3 and abolishes interaction with histone H3 trimethylated at 'Lys-4'. No effect on doted nuclear localization. Dominant-negative effect on target gene transcription.|||Unknown pathological significance; found in a patient with pernicious anemia.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064513|||http://purl.uniprot.org/annotation/VAR_005004|||http://purl.uniprot.org/annotation/VAR_005005|||http://purl.uniprot.org/annotation/VAR_005006|||http://purl.uniprot.org/annotation/VAR_013713|||http://purl.uniprot.org/annotation/VAR_013714|||http://purl.uniprot.org/annotation/VAR_013715|||http://purl.uniprot.org/annotation/VAR_013716|||http://purl.uniprot.org/annotation/VAR_013717|||http://purl.uniprot.org/annotation/VAR_013718|||http://purl.uniprot.org/annotation/VAR_013719|||http://purl.uniprot.org/annotation/VAR_013720|||http://purl.uniprot.org/annotation/VAR_013721|||http://purl.uniprot.org/annotation/VAR_013722|||http://purl.uniprot.org/annotation/VAR_013723|||http://purl.uniprot.org/annotation/VAR_013724|||http://purl.uniprot.org/annotation/VAR_014422|||http://purl.uniprot.org/annotation/VAR_026480|||http://purl.uniprot.org/annotation/VAR_026481|||http://purl.uniprot.org/annotation/VAR_026482|||http://purl.uniprot.org/annotation/VAR_026483|||http://purl.uniprot.org/annotation/VAR_026484|||http://purl.uniprot.org/annotation/VAR_026485|||http://purl.uniprot.org/annotation/VAR_026486|||http://purl.uniprot.org/annotation/VAR_076940|||http://purl.uniprot.org/annotation/VAR_076941|||http://purl.uniprot.org/annotation/VAR_076942|||http://purl.uniprot.org/annotation/VAR_076943|||http://purl.uniprot.org/annotation/VAR_076944|||http://purl.uniprot.org/annotation/VAR_076945|||http://purl.uniprot.org/annotation/VAR_076946|||http://purl.uniprot.org/annotation/VAR_076947|||http://purl.uniprot.org/annotation/VAR_076948|||http://purl.uniprot.org/annotation/VAR_076949|||http://purl.uniprot.org/annotation/VAR_076950|||http://purl.uniprot.org/annotation/VAR_076951|||http://purl.uniprot.org/annotation/VAR_076952|||http://purl.uniprot.org/annotation/VAR_076953|||http://purl.uniprot.org/annotation/VSP_004089|||http://purl.uniprot.org/annotation/VSP_004090|||http://purl.uniprot.org/annotation/VSP_043529
http://togogenome.org/gene/9606:OR8B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVQ4|||http://purl.uniprot.org/uniprot/Q96RD0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150654|||http://purl.uniprot.org/annotation/VAR_055147|||http://purl.uniprot.org/annotation/VAR_060011|||http://purl.uniprot.org/annotation/VAR_062058|||http://purl.uniprot.org/annotation/VAR_062059
http://togogenome.org/gene/9606:PDZD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5EBL8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PDZ|||PDZ domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058273|||http://purl.uniprot.org/annotation/VAR_069422|||http://purl.uniprot.org/annotation/VSP_015077
http://togogenome.org/gene/9606:DDX46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG89|||http://purl.uniprot.org/uniprot/Q7L014                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Probable ATP-dependent RNA helicase DDX46|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055121|||http://purl.uniprot.org/annotation/VAR_028079
http://togogenome.org/gene/9606:WASF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92558                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding protein WASF1|||Asymmetric dimethylarginine; alternate|||Disordered|||In NEDALVS.|||In NEDALVS; expression of a truncated and unstable protein; altered actin organization and longer mitochondria.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188992|||http://purl.uniprot.org/annotation/VAR_083471|||http://purl.uniprot.org/annotation/VAR_083472
http://togogenome.org/gene/9606:AZGP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK00|||http://purl.uniprot.org/uniprot/P25311                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Ig-like|||Ig-like C1-type|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Pyrrolidone carboxylic acid|||Zinc-alpha-2-glycoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019012|||http://purl.uniprot.org/annotation/PRO_5007491790
http://togogenome.org/gene/9606:SMNDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75940                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Increases binding to substrate containing dimethylated arginine.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Survival of motor neuron-related-splicing factor 30|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218908
http://togogenome.org/gene/9606:HEG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULI3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Protein HEG homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286981|||http://purl.uniprot.org/annotation/VAR_032253|||http://purl.uniprot.org/annotation/VAR_032254|||http://purl.uniprot.org/annotation/VAR_032255|||http://purl.uniprot.org/annotation/VAR_048984|||http://purl.uniprot.org/annotation/VAR_059269|||http://purl.uniprot.org/annotation/VSP_025275|||http://purl.uniprot.org/annotation/VSP_025276
http://togogenome.org/gene/9606:NRTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99748                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disordered|||Interchain|||May contribute to Hirschsprung disease in patients carrying a RET mutation.|||Neurturin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034010|||http://purl.uniprot.org/annotation/PRO_0000034011|||http://purl.uniprot.org/annotation/VAR_009498
http://togogenome.org/gene/9606:GLRX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS18                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Abolishes absorption at 320 nm and 420 nm suggesting the loss of 2Fe-2S-binding.|||Glutaredoxin|||Glutaredoxin-2, mitochondrial|||In isoform 2.|||Mitochondrion|||Phosphoserine|||Redox-active; alternate|||S-glutathionyl cysteine; alternate|||Specifically increases the specific activity but decreases affinity for glutathionylated substrates.|||Strongly impairs enzymatic activity.|||in inactive form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011628|||http://purl.uniprot.org/annotation/VAR_025234|||http://purl.uniprot.org/annotation/VAR_082825|||http://purl.uniprot.org/annotation/VSP_015221
http://togogenome.org/gene/9606:SLC25A27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHR4|||http://purl.uniprot.org/uniprot/O95847                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Mitochondrial uncoupling protein 4|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090676|||http://purl.uniprot.org/annotation/VAR_050137|||http://purl.uniprot.org/annotation/VAR_069101|||http://purl.uniprot.org/annotation/VSP_045916
http://togogenome.org/gene/9606:KBTBD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6T4|||http://purl.uniprot.org/uniprot/Q9NVX7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch repeat and BTB domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119080|||http://purl.uniprot.org/annotation/VAR_028046|||http://purl.uniprot.org/annotation/VSP_042068
http://togogenome.org/gene/9606:UQCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRT2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||Ubiquinol-cytochrome c reductase complex assembly factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089526
http://togogenome.org/gene/9606:CYP2S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 2S1|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051780|||http://purl.uniprot.org/annotation/VAR_033820|||http://purl.uniprot.org/annotation/VSP_010531
http://togogenome.org/gene/9606:ELOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDL3|||http://purl.uniprot.org/uniprot/Q15370                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Elongin-B|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114914|||http://purl.uniprot.org/annotation/VSP_045784
http://togogenome.org/gene/9606:TBC1D3H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7X1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344624
http://togogenome.org/gene/9606:RCAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PDJ2|||http://purl.uniprot.org/uniprot/P53805|||http://purl.uniprot.org/uniprot/Q6FGP2|||http://purl.uniprot.org/uniprot/Q6ZMM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Calcipressin-1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphorylation, no loss of interaction with PPP3CA and PPP3R1, reduced ability to inhibit calcineurin and increased protein half-life; alone or when associated with A-163.|||Loss of phosphorylation, no loss of interaction with PPP3CA and PPP3R1, reduced ability to inhibit calcineurin and increased protein half-life; alone or when associated with A-167.|||No loss of phosphorylation and no effect on protein half-life; alone or when associated with E-163.|||No loss of phosphorylation and no effect on protein half-life; alone or when associated with E-167.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211414|||http://purl.uniprot.org/annotation/VSP_001314|||http://purl.uniprot.org/annotation/VSP_001315|||http://purl.uniprot.org/annotation/VSP_001316
http://togogenome.org/gene/9606:PM20D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GTS8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-fatty-acyl-amino acid synthase/hydrolase PM20D1|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321928|||http://purl.uniprot.org/annotation/VAR_039380|||http://purl.uniprot.org/annotation/VAR_039381|||http://purl.uniprot.org/annotation/VAR_039382|||http://purl.uniprot.org/annotation/VAR_039383|||http://purl.uniprot.org/annotation/VAR_039384|||http://purl.uniprot.org/annotation/VAR_039385|||http://purl.uniprot.org/annotation/VAR_039386|||http://purl.uniprot.org/annotation/VSP_031826|||http://purl.uniprot.org/annotation/VSP_031827
http://togogenome.org/gene/9606:PTPRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHC3|||http://purl.uniprot.org/uniprot/Q15262|||http://purl.uniprot.org/uniprot/Q59EZ1|||http://purl.uniprot.org/uniprot/Q86WJ2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like|||Ig-like C2-type|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||MAM|||N-linked (GlcNAc...) asparagine|||Phosphocysteine intermediate|||Phosphoserine|||Receptor-type tyrosine-protein phosphatase kappa|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase 1|||Tyrosine-protein phosphatase 2|||protein-tyrosine-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025446|||http://purl.uniprot.org/annotation/PRO_5002803003|||http://purl.uniprot.org/annotation/PRO_5004304137|||http://purl.uniprot.org/annotation/VSP_024819|||http://purl.uniprot.org/annotation/VSP_042049|||http://purl.uniprot.org/annotation/VSP_054480
http://togogenome.org/gene/9606:GLIS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTH4|||http://purl.uniprot.org/uniprot/Q9BZE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Cleavage|||Disordered|||Interaction with CTNND1|||Polar residues|||Transcription activation|||Transcription repression|||Zinc finger protein GLIS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286983|||http://purl.uniprot.org/annotation/VAR_032256
http://togogenome.org/gene/9606:COX8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10176|||http://purl.uniprot.org/uniprot/Q53XN1                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 8A, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006186
http://togogenome.org/gene/9606:BECN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MW95                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes interaction with GPRASP1/GASP1 and ability to degrade G-protein coupled receptor. Does not affect function in autophagy.|||Basic and acidic residues|||Beclin-2|||Decreases homodimerization. Decreases interaction with ATG14.|||Decreases interaction with ATG14. Increases slightly homodimerization; when associated with L-190.|||Decreases interaction with ATG14. Increases slightly homodimerization; when associated with L-215.|||Decreases interaction with ATG14. Probably strongly increases homodimerization; when associated with L-197.|||Decreases interaction with ATG14. Probably strongly increases homodimerization; when associated with L-208.|||Disordered|||Increases homodimerization. Decreases interaction with ATG14.|||Increases strongly homodimerization. Decreases interaction with ATG14.|||Required for homodimer formation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332244
http://togogenome.org/gene/9606:SFTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8K0|||http://purl.uniprot.org/uniprot/Q6UW10                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Surfactant-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022610|||http://purl.uniprot.org/annotation/PRO_5014275542|||http://purl.uniprot.org/annotation/VAR_034423
http://togogenome.org/gene/9606:GLCCI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glucocorticoid-induced transcript 1 protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256128
http://togogenome.org/gene/9606:SPACA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sperm acrosome-associated protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274330|||http://purl.uniprot.org/annotation/VAR_030260|||http://purl.uniprot.org/annotation/VAR_035675
http://togogenome.org/gene/9606:CIDEB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHD4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  CIDE-N|||Lipid transferase CIDEB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144720
http://togogenome.org/gene/9606:TNK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13470                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Non-receptor tyrosine-protein kinase TNK1|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein kinase|||Proton acceptor|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088173|||http://purl.uniprot.org/annotation/VAR_041863|||http://purl.uniprot.org/annotation/VAR_041864|||http://purl.uniprot.org/annotation/VAR_041865|||http://purl.uniprot.org/annotation/VAR_041866|||http://purl.uniprot.org/annotation/VAR_041867|||http://purl.uniprot.org/annotation/VAR_041868|||http://purl.uniprot.org/annotation/VSP_051663
http://togogenome.org/gene/9606:RPRD1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGQ6|||http://purl.uniprot.org/uniprot/Q96P16                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  CID|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylserine|||Partial loss of binding to POLR2ACTD in vitro.|||Partial loss of binding to POLR2ACTD phosphorylated at 'Ser-2' in the heptad repeats in vitro.|||Phosphoserine|||Regulation of nuclear pre-mRNA domain-containing protein 1A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311344|||http://purl.uniprot.org/annotation/VAR_037229|||http://purl.uniprot.org/annotation/VSP_029531
http://togogenome.org/gene/9606:RBMX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y388                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||RNA-binding motif protein, X-linked 2|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081897|||http://purl.uniprot.org/annotation/VAR_033724
http://togogenome.org/gene/9606:UST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2C2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Uronyl 2-sulfotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207681|||http://purl.uniprot.org/annotation/VAR_059819
http://togogenome.org/gene/9606:PCBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0N5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Pterin-4-alpha-carbinolamine dehydratase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063057
http://togogenome.org/gene/9606:PIGV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUD9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GPI mannosyltransferase 2|||Helical|||In HPMRS1.|||Induces a reduces enzyme activity.|||Loss of function.|||Lumenal|||N-glycosylated due to the creation of an acceptor site for N-glycosylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246234|||http://purl.uniprot.org/annotation/VAR_064190|||http://purl.uniprot.org/annotation/VAR_064191|||http://purl.uniprot.org/annotation/VAR_064192|||http://purl.uniprot.org/annotation/VAR_064193
http://togogenome.org/gene/9606:MARVELD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4S9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||MARVEL|||MARVEL domain-containing protein 2|||OCEL|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271526|||http://purl.uniprot.org/annotation/VAR_047436|||http://purl.uniprot.org/annotation/VSP_022320|||http://purl.uniprot.org/annotation/VSP_022321|||http://purl.uniprot.org/annotation/VSP_035760
http://togogenome.org/gene/9606:VDAC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKM5|||http://purl.uniprot.org/uniprot/P45880                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes ceramide and phosphatidylcholine binding. Decreases apoptosis frequency following mitochondrial targeting of ceramide.|||Beta stranded|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 1.|||In isoform 2.|||Involved in ceramide and phosphatidylcholine binding|||N-acetylalanine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||Voltage-dependent anion-selective channel protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050505|||http://purl.uniprot.org/annotation/VAR_006380|||http://purl.uniprot.org/annotation/VSP_005076|||http://purl.uniprot.org/annotation/VSP_005077
http://togogenome.org/gene/9606:ATP2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01814|||http://purl.uniprot.org/uniprot/Q4LE63                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Calmodulin-binding subdomain A|||Calmodulin-binding subdomain B|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In DFNA82.|||In isoform WA, isoform XA, isoform YA and isoform ZA.|||In isoform XA and isoform XB.|||In isoform YA and isoform YB.|||In isoform ZA and isoform ZB.|||May exacerbate the severity of non-syndromic sensorineural hearing loss in patients with clinically relevant CDH23 variants; delayed calcium export.|||May exacerbate the severity of non-syndromic sensorineural hearing loss in patients with clinically relevant CDH23 variants; resulted in 50% decrease of the calcium ATPase activity.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKC|||Plasma membrane calcium-transporting ATPase 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046214|||http://purl.uniprot.org/annotation/VAR_084464|||http://purl.uniprot.org/annotation/VAR_084465|||http://purl.uniprot.org/annotation/VAR_086987|||http://purl.uniprot.org/annotation/VAR_086988|||http://purl.uniprot.org/annotation/VAR_086989|||http://purl.uniprot.org/annotation/VSP_000384|||http://purl.uniprot.org/annotation/VSP_000385|||http://purl.uniprot.org/annotation/VSP_000386|||http://purl.uniprot.org/annotation/VSP_040837
http://togogenome.org/gene/9606:SLX4IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein SLX4IP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306119|||http://purl.uniprot.org/annotation/VAR_035277
http://togogenome.org/gene/9606:STON2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IU55|||http://purl.uniprot.org/uniprot/H0YJ05|||http://purl.uniprot.org/uniprot/Q8WXE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MHD|||NPF 1|||NPF 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces interaction with SYT1.|||SHD|||Stonin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185732|||http://purl.uniprot.org/annotation/VAR_020182|||http://purl.uniprot.org/annotation/VAR_021912|||http://purl.uniprot.org/annotation/VAR_046643|||http://purl.uniprot.org/annotation/VAR_046644|||http://purl.uniprot.org/annotation/VSP_044863
http://togogenome.org/gene/9606:FBXO17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EF6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site                                                                                  ^@                                                                                  F-box|||F-box only protein 17|||FBA|||Reduces interaction with glycosylated concanavalin-A in vitro.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119898
http://togogenome.org/gene/9606:KCNK17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T54                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101768|||http://purl.uniprot.org/annotation/VAR_024683|||http://purl.uniprot.org/annotation/VAR_032362|||http://purl.uniprot.org/annotation/VAR_032363|||http://purl.uniprot.org/annotation/VSP_047354
http://togogenome.org/gene/9606:EXOC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00471                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Exocyst complex component 5|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118943|||http://purl.uniprot.org/annotation/VAR_048957
http://togogenome.org/gene/9606:ZNF562                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMG0|||http://purl.uniprot.org/uniprot/B4E2P7|||http://purl.uniprot.org/uniprot/K7EIE6|||http://purl.uniprot.org/uniprot/Q6V9R5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||KRAB|||Zinc finger protein 562                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047652|||http://purl.uniprot.org/annotation/VAR_023936|||http://purl.uniprot.org/annotation/VAR_023937|||http://purl.uniprot.org/annotation/VAR_059922|||http://purl.uniprot.org/annotation/VSP_016379|||http://purl.uniprot.org/annotation/VSP_016380
http://togogenome.org/gene/9606:LYPD6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI32                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated serine|||In isoform 2.|||Ly6/PLAUR domain-containing protein 6B|||Removed in mature form|||Sufficient for inhibiting alpha-7 nAChR currents|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321950|||http://purl.uniprot.org/annotation/PRO_0000321951|||http://purl.uniprot.org/annotation/VSP_031842
http://togogenome.org/gene/9606:SYT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43581                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Synaptotagmin-7|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183957|||http://purl.uniprot.org/annotation/VAR_052241|||http://purl.uniprot.org/annotation/VSP_045991|||http://purl.uniprot.org/annotation/VSP_058231|||http://purl.uniprot.org/annotation/VSP_058232|||http://purl.uniprot.org/annotation/VSP_058233|||http://purl.uniprot.org/annotation/VSP_058234
http://togogenome.org/gene/9606:CAMSAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1Y5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CKK|||Calmodulin-regulated spectrin-associated protein 3|||Calponin-homology (CH)|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050799|||http://purl.uniprot.org/annotation/VAR_053991|||http://purl.uniprot.org/annotation/VSP_041473
http://togogenome.org/gene/9606:TAF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16514                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Drastically reduces binding to TAF4.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-fold|||In isoform TAFII15.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription initiation factor TFIID subunit 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033580|||http://purl.uniprot.org/annotation/VSP_018888
http://togogenome.org/gene/9606:CXCR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U3FJG0|||http://purl.uniprot.org/uniprot/A0A0U3GXA9|||http://purl.uniprot.org/uniprot/A0A8Q3WLL1|||http://purl.uniprot.org/uniprot/P61073                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates.|||Basic and acidic residues|||C-X-C chemokine receptor type 4|||Chemokine binding|||Chemokine binding, important for signaling and HIV-1 coreceptor activity|||Constitutive G-protein activation, with further activation induced by agonist.|||Cytoplasmic|||Disordered|||Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-324.|||Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-325.|||Enhanced coreceptor activity on R5 HIV-1 isolate Envs. No effect on sulfate incorporation; when associated with A-8 and A-9.|||Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11.|||Extracellular|||Found in patients with Waldenstroem macroglobulinemia; somatic mutation.|||G-protein coupled receptors family 1 profile|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates.|||Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-7.|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Important for chemokine binding, signaling and HIV-1 coreceptor activity|||Important for signaling|||In WHIMS1.|||In WHIMS1; also found in patients with Waldenstroem macroglobulinemia; somatic mutation.|||In WHIMS1; common somatic mutation in patients with Waldenstroem macroglobulinemia; results in decreased CXCL12-triggered receptor internalization; enhanced AKT and MAPK signaling activation; confers resistance to ibrutinib-triggered apoptosis.|||In isoform 2.|||Increased thermostability.|||Involved in dimerization|||Involved in dimerization; when bound to chemokine|||Loss of agonist-induced G-protein activation.|||Loss of ubiquitination by RNF113A.|||Markedly reduced coreceptor activity for HIV-1 isolate LAI.|||Markedly reduced coreceptor activity for HIV-1 isolate NDK. Less effect for HIV-1 isolate LAI.|||Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-324.|||Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-325.|||N-linked (GlcNAc...) asparagine|||No effect on binding to ITCH.|||No effect on sulfate incorporation; when associated with A-8 and A-13.|||No effect on sulfate incorporation; when associated with A-9 and A-13.|||No effect on ubiquitination by RNF113A.|||No reduction of agonist-induced G-protein activation.|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by GRK6|||Phosphoserine; by PKC and GRK6|||Polar residues|||Reduced CXCL12 binding. Abolishes signaling.|||Reduced CXCL12 binding. Abolishes signaling. Markedly reduced coreceptor activity for HIV-1 isolate LAI.|||Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolate LAI. Enhanced coreceptor activity for HIV-1 isolate NDK.|||Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolates LAI and NDK.|||Reduced CXCL12 binding. No effect on signaling.|||Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolate NDK.|||Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolates LAI and NDk.|||Reduced coreceptor activity for HIV-1 isolate NDK.|||Reduced coreceptor activity for HIV-1 isolates LAI and NDK. Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-12.|||Reduced coreceptor activity for several HIV-1 isolates.|||Reduced molecular weight. Enhanced coreceptor activity on R5 HIV-1 isolate Envs. Slight further enhancement of coreceptor activity; when associated with A-13.|||Retains ligand-binding affinity but abolishes signaling.|||Sulfate incorporation greatly reduced; when associated with F-12 and F-21. Moderate reduction in sulfate incorporation; when associated with F-12 and A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-12; A-18 and F-21.|||Sulfate incorporation greatly reduced; when associated with F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and F-12. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; F-12; and F-21.|||Sulfate incorporation greatly reduced; when associated with F-7 and F-12. Sulfate incorporation greatly reduced; when associated with A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; F-12 and A-18.|||Sulfate incorporation greatly reduced; when associated with F-7 and F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; A-18 and F-21.|||Sulfotyrosine|||Sulfotyrosine; partial ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069352|||http://purl.uniprot.org/annotation/VAR_081112|||http://purl.uniprot.org/annotation/VAR_081113|||http://purl.uniprot.org/annotation/VAR_081114|||http://purl.uniprot.org/annotation/VAR_081115|||http://purl.uniprot.org/annotation/VSP_001890
http://togogenome.org/gene/9606:LRRC66                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Leucine-rich repeat-containing protein 66|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329433|||http://purl.uniprot.org/annotation/VAR_051124
http://togogenome.org/gene/9606:GCNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02742                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase|||Catalytic|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Loss of interaction with GOLPH3 and loss of localization to the Golgi.|||Lumenal|||Mediates interaction with GOLPH3 and is necessary and sufficient for localization to the Golgi|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Stem region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191395|||http://purl.uniprot.org/annotation/VAR_048000|||http://purl.uniprot.org/annotation/VAR_048001
http://togogenome.org/gene/9606:RASD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D21                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||GTP-binding protein Rhes|||Interaction with GNB1, GNB2 and GNB3|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082720|||http://purl.uniprot.org/annotation/PRO_0000281375
http://togogenome.org/gene/9606:ACCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z622|||http://purl.uniprot.org/uniprot/Q96QU6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-aminocyclopropane-1-carboxylate synthase-like protein 1|||Aminotransferase class I/classII|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N6-(pyridoxal phosphate)lysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318071|||http://purl.uniprot.org/annotation/VAR_038685|||http://purl.uniprot.org/annotation/VAR_038686|||http://purl.uniprot.org/annotation/VAR_038687|||http://purl.uniprot.org/annotation/VAR_048227|||http://purl.uniprot.org/annotation/VAR_048228|||http://purl.uniprot.org/annotation/VSP_055800|||http://purl.uniprot.org/annotation/VSP_055801
http://togogenome.org/gene/9606:RTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3B9|||http://purl.uniprot.org/uniprot/Q16799                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform RTN1-B.|||In isoform RTN1-C.|||Phosphoserine|||Polar residues|||Reticulon|||Reticulon-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168158|||http://purl.uniprot.org/annotation/VAR_053630|||http://purl.uniprot.org/annotation/VAR_053631|||http://purl.uniprot.org/annotation/VSP_005644|||http://purl.uniprot.org/annotation/VSP_005645|||http://purl.uniprot.org/annotation/VSP_005646
http://togogenome.org/gene/9606:YJEFN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6XGL0|||http://purl.uniprot.org/uniprot/Q6ZT45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pro residues|||YjeF N-terminal|||YjeF N-terminal domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348461|||http://purl.uniprot.org/annotation/VAR_061989|||http://purl.uniprot.org/annotation/VSP_035170
http://togogenome.org/gene/9606:GFAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14136                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Citrulline|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Does not affect intermediate filaments formation.|||Glial fibrillary acidic protein|||Head|||IF rod|||In ALXDRD.|||In ALXDRD; adult form.|||In ALXDRD; affects intermediate filaments formation yielding protein aggregates.|||In ALXDRD; affects intermediate filaments formation.|||In ALXDRD; associated with Gly-330.|||In ALXDRD; associated with Lys-332.|||In ALXDRD; impairs filaments formation.|||In ALXDRD; unknown pathological significance; does not affect intermediate filaments formation.|||In isoform 2.|||In isoform 3.|||Linker 1|||Linker 12|||Linker 2|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by AURKB and ROCK1|||Phosphothreonine|||Phosphothreonine; by AURKB and ROCK1|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063805|||http://purl.uniprot.org/annotation/VAR_017464|||http://purl.uniprot.org/annotation/VAR_017465|||http://purl.uniprot.org/annotation/VAR_017466|||http://purl.uniprot.org/annotation/VAR_017467|||http://purl.uniprot.org/annotation/VAR_017468|||http://purl.uniprot.org/annotation/VAR_017469|||http://purl.uniprot.org/annotation/VAR_017470|||http://purl.uniprot.org/annotation/VAR_017471|||http://purl.uniprot.org/annotation/VAR_017472|||http://purl.uniprot.org/annotation/VAR_017473|||http://purl.uniprot.org/annotation/VAR_017474|||http://purl.uniprot.org/annotation/VAR_017475|||http://purl.uniprot.org/annotation/VAR_017476|||http://purl.uniprot.org/annotation/VAR_017477|||http://purl.uniprot.org/annotation/VAR_017478|||http://purl.uniprot.org/annotation/VAR_017479|||http://purl.uniprot.org/annotation/VAR_071517|||http://purl.uniprot.org/annotation/VAR_071518|||http://purl.uniprot.org/annotation/VAR_071519|||http://purl.uniprot.org/annotation/VAR_071520|||http://purl.uniprot.org/annotation/VAR_071521|||http://purl.uniprot.org/annotation/VAR_071522|||http://purl.uniprot.org/annotation/VAR_071523|||http://purl.uniprot.org/annotation/VAR_071524|||http://purl.uniprot.org/annotation/VAR_071525|||http://purl.uniprot.org/annotation/VAR_071526|||http://purl.uniprot.org/annotation/VAR_071527|||http://purl.uniprot.org/annotation/VAR_071528|||http://purl.uniprot.org/annotation/VAR_071529|||http://purl.uniprot.org/annotation/VAR_071530|||http://purl.uniprot.org/annotation/VAR_071531|||http://purl.uniprot.org/annotation/VAR_071532|||http://purl.uniprot.org/annotation/VAR_071533|||http://purl.uniprot.org/annotation/VAR_071534|||http://purl.uniprot.org/annotation/VAR_071535|||http://purl.uniprot.org/annotation/VAR_071536|||http://purl.uniprot.org/annotation/VAR_071537|||http://purl.uniprot.org/annotation/VAR_071538|||http://purl.uniprot.org/annotation/VAR_071539|||http://purl.uniprot.org/annotation/VAR_071540|||http://purl.uniprot.org/annotation/VAR_071541|||http://purl.uniprot.org/annotation/VAR_071542|||http://purl.uniprot.org/annotation/VAR_071543|||http://purl.uniprot.org/annotation/VAR_071544|||http://purl.uniprot.org/annotation/VAR_071545|||http://purl.uniprot.org/annotation/VAR_071546|||http://purl.uniprot.org/annotation/VAR_071547|||http://purl.uniprot.org/annotation/VAR_071548|||http://purl.uniprot.org/annotation/VAR_071549|||http://purl.uniprot.org/annotation/VAR_071550|||http://purl.uniprot.org/annotation/VAR_071551|||http://purl.uniprot.org/annotation/VAR_071552|||http://purl.uniprot.org/annotation/VAR_071553|||http://purl.uniprot.org/annotation/VAR_071554|||http://purl.uniprot.org/annotation/VAR_071555|||http://purl.uniprot.org/annotation/VAR_071556|||http://purl.uniprot.org/annotation/VAR_071557|||http://purl.uniprot.org/annotation/VAR_071558|||http://purl.uniprot.org/annotation/VAR_071559|||http://purl.uniprot.org/annotation/VAR_071560|||http://purl.uniprot.org/annotation/VAR_071561|||http://purl.uniprot.org/annotation/VAR_071562|||http://purl.uniprot.org/annotation/VAR_071563|||http://purl.uniprot.org/annotation/VAR_071564|||http://purl.uniprot.org/annotation/VAR_071565|||http://purl.uniprot.org/annotation/VAR_071566|||http://purl.uniprot.org/annotation/VAR_071567|||http://purl.uniprot.org/annotation/VAR_071568|||http://purl.uniprot.org/annotation/VAR_082837|||http://purl.uniprot.org/annotation/VAR_082838|||http://purl.uniprot.org/annotation/VSP_017051|||http://purl.uniprot.org/annotation/VSP_017052
http://togogenome.org/gene/9606:COL26A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Collagen alpha-1(XXVI) chain|||Collagen-like 1|||Collagen-like 2|||Disordered|||EMI|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007825|||http://purl.uniprot.org/annotation/VAR_057530|||http://purl.uniprot.org/annotation/VSP_008447
http://togogenome.org/gene/9606:ARL8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||INTRAMEM|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||INTRAMEM|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 8A|||Note=Mediates targeting to membranes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232916
http://togogenome.org/gene/9606:SCGB1C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMR2|||http://purl.uniprot.org/uniprot/Q8TD33                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 1C member 1|||Secretoglobin family 1C member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223332|||http://purl.uniprot.org/annotation/PRO_0000431381|||http://purl.uniprot.org/annotation/VAR_063102
http://togogenome.org/gene/9606:DCUN1D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH26|||http://purl.uniprot.org/uniprot/Q92564                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DCN1-like protein 4|||DCUN1|||Disordered|||Does not affect localization at nucleus; when associated with A-250 and A-280.|||Does not affect localization at nucleus; when associated with A-250 and R-274.|||Does not affect localization at nucleus; when associated with R-274 and A-280.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129503|||http://purl.uniprot.org/annotation/VSP_016016|||http://purl.uniprot.org/annotation/VSP_054381
http://togogenome.org/gene/9606:ZXDB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98169                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Pro residues|||Required for interaction with ZXDC|||Required for transcriptional activation|||Zinc finger X-linked protein ZXDB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047777|||http://purl.uniprot.org/annotation/VAR_033003|||http://purl.uniprot.org/annotation/VAR_033004|||http://purl.uniprot.org/annotation/VAR_033005|||http://purl.uniprot.org/annotation/VAR_033006
http://togogenome.org/gene/9606:HIPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2X6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity, no effect on interaction with TP53 and TP73 or on BMP-induced transcriptional activation. Enhances BMP-induced transcriptional activation; when associated with 359-AAF-361.|||Autoinhibitory domain (AID)|||Cleavage; by CASP6|||Disordered|||Enhances BMP-induced transcriptional activation; when associated with R-228.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeodomain-interacting protein kinase 2|||Impaired nuclear localization.|||Impaired nuclear localization; when associated with A-803.|||Impaired nuclear localization; when associated with A-805.|||In isoform 2.|||In isoform 3.|||Interaction with AXIN1|||Interaction with CTBP1|||Interaction with DAXX|||Interaction with DAZAP2|||Interaction with HMGA1|||Interaction with POU4F1|||Interaction with SKI and SMAD1|||Interaction with TP53 and TP73|||Interaction with UBE2I|||Locates in the nucleoplasm, no effect on interaction with RANBP9, but loss of kinase activity toward PML, RUNX1, EP300 and DAZAP2.|||Loss of SUMO and CBX4 interaction, and impaired nuclear and PML-nuclear bodies localization.|||Loss of SUMO interaction, and impaired nuclear and PML-nuclear bodies localization.|||Nuclear localization signal 1 (NLS1)|||Nuclear localization signal 2 (NLS2)|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Required for localization to nuclear speckles|||SUMO interaction motifs (SIM); required for nuclear localization and kinase activity|||Transcriptional corepression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085995|||http://purl.uniprot.org/annotation/VAR_040547|||http://purl.uniprot.org/annotation/VAR_040548|||http://purl.uniprot.org/annotation/VSP_004804|||http://purl.uniprot.org/annotation/VSP_004805|||http://purl.uniprot.org/annotation/VSP_004806|||http://purl.uniprot.org/annotation/VSP_004807
http://togogenome.org/gene/9606:DHRS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LJ7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 1|||N-acetylalanine|||Omega-N-methylarginine|||Proton acceptor|||Removed|||Required for ER localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054640|||http://purl.uniprot.org/annotation/VAR_052318
http://togogenome.org/gene/9606:OR5AN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP9|||http://purl.uniprot.org/uniprot/Q8NGI8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5AN1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150577|||http://purl.uniprot.org/annotation/VAR_024098
http://togogenome.org/gene/9606:EIF2B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR50                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In VWM3.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Translation initiation factor eIF-2B subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156079|||http://purl.uniprot.org/annotation/VAR_015409|||http://purl.uniprot.org/annotation/VAR_015410|||http://purl.uniprot.org/annotation/VAR_048920|||http://purl.uniprot.org/annotation/VAR_068470|||http://purl.uniprot.org/annotation/VAR_068471|||http://purl.uniprot.org/annotation/VAR_068472|||http://purl.uniprot.org/annotation/VSP_001435|||http://purl.uniprot.org/annotation/VSP_001436
http://togogenome.org/gene/9606:PRPF31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWY3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes nuclear localization.|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In RP11; high penetrance.|||In RP11; mislocation of the protein in the cytoplasm and reduced interaction with PRPF6; the result may be a deficiency in splicing function in the retina.|||In RP11; mislocation of the protein in the cytoplasm, but no effect on interaction with PRPF6; the result may be a deficiency in splicing function in the retina.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with U4 snRNA|||Interaction with U4 snRNA and U4atac snRNA|||Interaction with U4atac snRNA|||N6-acetyllysine|||Nop|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Reduces binding to the complex formed by U4 snRNA and SNU13.|||U4/U6 small nuclear ribonucleoprotein Prp31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227799|||http://purl.uniprot.org/annotation/VAR_025629|||http://purl.uniprot.org/annotation/VAR_025630|||http://purl.uniprot.org/annotation/VAR_025631|||http://purl.uniprot.org/annotation/VSP_017581|||http://purl.uniprot.org/annotation/VSP_017582|||http://purl.uniprot.org/annotation/VSP_017583|||http://purl.uniprot.org/annotation/VSP_017584|||http://purl.uniprot.org/annotation/VSP_057390
http://togogenome.org/gene/9606:PLPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14494                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased lipid phosphatase activity.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||PDZ-binding; involved in localization to the apical cell membrane|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phospholipid phosphatase 1|||Polar residues|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220905|||http://purl.uniprot.org/annotation/VSP_009651
http://togogenome.org/gene/9606:TEX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMP-LTD|||Testis-expressed protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244479|||http://purl.uniprot.org/annotation/VAR_061712|||http://purl.uniprot.org/annotation/VSP_019569
http://togogenome.org/gene/9606:TECPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6L1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Polar residues|||TECPR 1|||TECPR 2|||TECPR 3|||TECPR 4|||TECPR 5|||TECPR 6|||TECPR 7|||TECPR 8|||TECPR 9|||Tectonin beta-propeller repeat-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337060|||http://purl.uniprot.org/annotation/VAR_060190|||http://purl.uniprot.org/annotation/VAR_062238|||http://purl.uniprot.org/annotation/VSP_033861|||http://purl.uniprot.org/annotation/VSP_042969|||http://purl.uniprot.org/annotation/VSP_042970|||http://purl.uniprot.org/annotation/VSP_042971|||http://purl.uniprot.org/annotation/VSP_042972|||http://purl.uniprot.org/annotation/VSP_042973
http://togogenome.org/gene/9606:BICC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H694                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Found in a family with atypical autism and severe epilepsy; unknown pathological significance.|||In CYSRD; may impair splicing; hypomorphic mutation.|||In isoform 2.|||KH 1|||KH 2|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein bicaudal C homolog 1|||SAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000267714|||http://purl.uniprot.org/annotation/VAR_029658|||http://purl.uniprot.org/annotation/VAR_033542|||http://purl.uniprot.org/annotation/VAR_060133|||http://purl.uniprot.org/annotation/VAR_066759|||http://purl.uniprot.org/annotation/VAR_066760|||http://purl.uniprot.org/annotation/VAR_072077|||http://purl.uniprot.org/annotation/VSP_021949
http://togogenome.org/gene/9606:CBX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D177|||http://purl.uniprot.org/uniprot/Q13185                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Chromo|||Chromo 1|||Chromo 2; shadow subtype|||Chromobox protein homolog 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080203
http://togogenome.org/gene/9606:MBOAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNC8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Lysophospholipid acyltransferase 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273018|||http://purl.uniprot.org/annotation/VAR_050025|||http://purl.uniprot.org/annotation/VSP_036729|||http://purl.uniprot.org/annotation/VSP_036730|||http://purl.uniprot.org/annotation/VSP_036731
http://togogenome.org/gene/9606:OSGEPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4B0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mimics acetylation; decreased formation of tRNA threonylcarbamoyladenosine modification.|||Mimics acetylation; increased formation of tRNA threonylcarbamoyladenosine modification.|||Mitochondrion|||N6-acetyllysine|||tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307778|||http://purl.uniprot.org/annotation/VAR_036651|||http://purl.uniprot.org/annotation/VSP_028828|||http://purl.uniprot.org/annotation/VSP_028829|||http://purl.uniprot.org/annotation/VSP_028830
http://togogenome.org/gene/9606:TRAF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQY7|||http://purl.uniprot.org/uniprot/Q6Q0C0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Complete loss of IFN-beta promoter inhibition after viral infection.|||Disordered|||E3 ubiquitin-protein ligase TRAF7|||In CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3.|||In CAFDADD; no significant effect on phosphorylation of MAPK1 and/or MAPK3.|||In isoform 2.|||Phosphoserine|||Polar residues|||RING-type|||TRAF-type|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051296|||http://purl.uniprot.org/annotation/VAR_081685|||http://purl.uniprot.org/annotation/VAR_081686|||http://purl.uniprot.org/annotation/VAR_081687|||http://purl.uniprot.org/annotation/VAR_081688|||http://purl.uniprot.org/annotation/VSP_051607
http://togogenome.org/gene/9606:GPHN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased palmitoylation. Decreased clustering at synaptic membranes. Decreased function in gamma-aminobutyric acid receptor clustering. Loss of palmitoylation, decreased clustering at synaptic membranes and loss of function in gamma-aminobutyric acid receptor clustering; when associated with S-212.|||Decreased palmitoylation. Decreased clustering at synaptic membranes. Decreased function in gamma-aminobutyric acid receptor clustering. Loss of palmitoylation, decreased clustering at synaptic membranes and loss of function in gamma-aminobutyric acid receptor clustering; when associated with S-284.|||Disordered|||Found in a patient with hyperekplexia; unknown pathological significance; does not disrupt GLRB-GPHN interactions; does not affect the structural lattices formed by GPHN.|||Gephyrin|||In MOCODC; lacks molybdenum cofactor synthesis activity.|||In MOCODC; patient phenotype resembling Dravet syndrome; abolishes postsynaptic clustering of GPHN; decreases cell-surface expression of GABA receptors; impairs postsynaptic currents; catalytically inactive; decreases binding affinity toward GABRA3; decreases binding affinity toward GLRB.|||In isoform 2.|||Interaction with GABARAP|||MPT Mo-transferase|||MPT adenylyltransferase|||Phosphoserine|||Phosphothreonine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170964|||http://purl.uniprot.org/annotation/VAR_044162|||http://purl.uniprot.org/annotation/VAR_070275|||http://purl.uniprot.org/annotation/VAR_075626|||http://purl.uniprot.org/annotation/VSP_021769
http://togogenome.org/gene/9606:SETSIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DME0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Protein SETSIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000426097
http://togogenome.org/gene/9606:TRO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK08|||http://purl.uniprot.org/uniprot/Q12816|||http://purl.uniprot.org/uniprot/Q9BX88|||http://purl.uniprot.org/uniprot/Q9BX90|||http://purl.uniprot.org/uniprot/Q9BX91                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15; approximate|||16|||17|||18|||19|||2|||20|||21|||22; approximate|||23|||24|||25|||26|||27; approximate|||28; approximate|||29|||30|||31|||32|||33|||34|||35|||36|||37; approximate|||38; approximate|||39|||3; approximate|||4|||40|||41|||42; approximate|||43; approximate|||44|||45|||46; approximate|||47|||48|||49|||5|||50; approximate|||51|||52; approximate|||53; approximate|||54; approximate|||55; approximate|||56; approximate|||57; approximate|||58; approximate|||59; approximate|||60; approximate|||61; approximate|||62 X 10 AA approximate tandem repeats|||62; approximate|||6; approximate|||7|||8; approximate|||9; approximate|||Disordered|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||MAGE|||Polar residues|||Trophinin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156742|||http://purl.uniprot.org/annotation/VAR_053510|||http://purl.uniprot.org/annotation/VAR_062122|||http://purl.uniprot.org/annotation/VAR_076264|||http://purl.uniprot.org/annotation/VSP_043513|||http://purl.uniprot.org/annotation/VSP_043514|||http://purl.uniprot.org/annotation/VSP_053937|||http://purl.uniprot.org/annotation/VSP_053938
http://togogenome.org/gene/9606:COL6A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMZ7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Collagen alpha-6(VI) chain|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||Triple-helical region|||VWFA 1|||VWFA 2|||VWFA 3|||VWFA 4|||VWFA 5|||VWFA 6|||VWFA 7|||VWFA 8|||VWFA 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000266306|||http://purl.uniprot.org/annotation/VAR_043609|||http://purl.uniprot.org/annotation/VAR_043610|||http://purl.uniprot.org/annotation/VAR_043611|||http://purl.uniprot.org/annotation/VAR_043612|||http://purl.uniprot.org/annotation/VAR_043613|||http://purl.uniprot.org/annotation/VAR_061120|||http://purl.uniprot.org/annotation/VSP_033914|||http://purl.uniprot.org/annotation/VSP_033915
http://togogenome.org/gene/9606:KRT15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVF5|||http://purl.uniprot.org/uniprot/P19012                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Head|||IF rod|||In isoform 2.|||Keratin, type I cytoskeletal 15|||Linker 1|||Linker 12|||Phosphoserine|||Phosphothreonine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063657|||http://purl.uniprot.org/annotation/VAR_047429|||http://purl.uniprot.org/annotation/VAR_047430|||http://purl.uniprot.org/annotation/VAR_047431|||http://purl.uniprot.org/annotation/VSP_056507|||http://purl.uniprot.org/annotation/VSP_056508|||http://purl.uniprot.org/annotation/VSP_056509
http://togogenome.org/gene/9606:CCM2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUG4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Cerebral cavernous malformations 2 protein-like|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079476|||http://purl.uniprot.org/annotation/VSP_007633|||http://purl.uniprot.org/annotation/VSP_007634|||http://purl.uniprot.org/annotation/VSP_007635
http://togogenome.org/gene/9606:MFNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00587                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-N-acetylglucosaminyltransferase manic fringe|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219182|||http://purl.uniprot.org/annotation/VAR_024467|||http://purl.uniprot.org/annotation/VSP_042857
http://togogenome.org/gene/9606:SPATA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VX52                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Spermatogenesis-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349215|||http://purl.uniprot.org/annotation/VAR_046284|||http://purl.uniprot.org/annotation/VSP_035223|||http://purl.uniprot.org/annotation/VSP_035224|||http://purl.uniprot.org/annotation/VSP_039875
http://togogenome.org/gene/9606:NAT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0A0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished acetylation.|||Abolished acetyltransferase activity, probably caused by impaired acetyl-CoA binding.|||Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RNA cytidine acetyltransferase|||Required for localization to the nucleolus and midbody                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215883|||http://purl.uniprot.org/annotation/VAR_059858|||http://purl.uniprot.org/annotation/VAR_061894|||http://purl.uniprot.org/annotation/VSP_054018
http://togogenome.org/gene/9606:CLN8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ER-retrieval signal|||Helical|||In CLN8.|||In CLN8; associated with M-16 on the same allele.|||In CLN8; associated with M-170 on the same allele.|||In CLN8; unknown pathological significance.|||In CLN8NE.|||Localizes to the Golgi complex.|||Protein CLN8|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185537|||http://purl.uniprot.org/annotation/VAR_013174|||http://purl.uniprot.org/annotation/VAR_013175|||http://purl.uniprot.org/annotation/VAR_026554|||http://purl.uniprot.org/annotation/VAR_026555|||http://purl.uniprot.org/annotation/VAR_026556|||http://purl.uniprot.org/annotation/VAR_026557|||http://purl.uniprot.org/annotation/VAR_031704|||http://purl.uniprot.org/annotation/VAR_058438|||http://purl.uniprot.org/annotation/VAR_058439|||http://purl.uniprot.org/annotation/VAR_060573|||http://purl.uniprot.org/annotation/VAR_060574|||http://purl.uniprot.org/annotation/VAR_060575|||http://purl.uniprot.org/annotation/VAR_066920|||http://purl.uniprot.org/annotation/VAR_066921|||http://purl.uniprot.org/annotation/VAR_066922|||http://purl.uniprot.org/annotation/VAR_066923|||http://purl.uniprot.org/annotation/VAR_066924|||http://purl.uniprot.org/annotation/VAR_066925|||http://purl.uniprot.org/annotation/VAR_066926|||http://purl.uniprot.org/annotation/VAR_066927|||http://purl.uniprot.org/annotation/VAR_066928|||http://purl.uniprot.org/annotation/VAR_075367|||http://purl.uniprot.org/annotation/VAR_075368
http://togogenome.org/gene/9606:IAPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10997                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Islet amyloid polypeptide|||Promotes formation of fibrillar aggregates.|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004105|||http://purl.uniprot.org/annotation/PRO_0000004106|||http://purl.uniprot.org/annotation/PRO_0000004107|||http://purl.uniprot.org/annotation/VAR_012080
http://togogenome.org/gene/9606:SH3PXD2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1X283|||http://purl.uniprot.org/uniprot/G3V144                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In FTHS.|||PX|||Phosphoserine|||Phosphotyrosine|||Pro residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 and PX domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312201|||http://purl.uniprot.org/annotation/VAR_046226|||http://purl.uniprot.org/annotation/VAR_063764
http://togogenome.org/gene/9606:KEAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14145                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with NFE2L2/NRF2; when associated with 123-A--A-127.|||Abolished interaction with NFE2L2/NRF2; when associated with 161-A-A-162.|||Abolishes repression of NFE2L2/NRF2-dependent gene expression.|||Abolishes repression of NFE2L2/NRF2-dependent gene expression. Slows down degradation of NFE2L2/NRF2.|||BACK|||BTB|||In a NSCLC cell line.|||In a NSCLC cell line; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression.|||In a breast cancer sample; somatic mutation.|||In a lung adenocarcinoma cell line; also in NSCLC cell lines; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression.|||In a lung adenocarcinoma patient.|||In a lung adenocarcinoma patient; somatic mutation; strongly reduces interaction with NFE2L2/NRF2 and reduces repression of NFE2L2/NRF2-dependent gene expression.|||Increases ubiquitination and proteolytic degradation.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like ECH-associated protein 1|||Loss of export from nucleus; when associated with A-308.|||Loss of export from nucleus; when associated with A-310.|||Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Does not affect interaction with SQSTM1/p62.|||Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Impaired interaction with SQSTM1/p62.|||Loss of interaction with NFE2L2/NRF2. Abolishes repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. Does not affect interaction with SQSTM1/p62.|||Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Abolishes interaction with SQSTM1/p62.|||Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Impaired interaction with SQSTM1/p62.|||Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5.|||Loss of interaction with NFE2L2/NRF2. Strongly reduces repression of NFE2L2/NRF2-dependent gene expression. Loss of interaction with PGAM5. Abolishes interaction with SQSTM1/p62.|||N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Arg-Cys) (interchain with C-151 in KEAP1)|||N5-[4-(S-L-cysteinyl)-5-methyl-1H-imidazol-2-yl]-L-ornithine (Cys-Arg) (interchain with R-135 in KEAP1)|||Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates.|||S-(2,3-dicarboxypropyl)cysteine|||S-(2,3-dicarboxypropyl)cysteine; alternate|||S-(2-succinyl)cysteine|||S-(2-succinyl)cysteine; alternate|||S-cGMP-cysteine|||S-nitrosocysteine; alternate|||Sensor for electrophilic agents|||Substitution with a bulky side chain that mimicks covalent modification by an electrophile; prevents ubiquitination and degradation of NFE2L2/NRF2, leading to constitutive activation of NFE2L2/NRF2 and subsequent expression of phase 2 detoxifying enzymes.|||Substitution with a small side chain that prevents covalent modification by an electrophile; promotes constitutive ubiquitination of NFE2L2/NRF2 and subsequent repression of phase 2 detoxifying enzymes. Resistance of ubiquitination of PGAM5 to inhibition by oxidative stress and sulforaphane. Impaired interaction with CUL3. Reduced formation of a high-molecular mass KEAP1 molecule when methylglyoxal accumulates.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119093|||http://purl.uniprot.org/annotation/VAR_032102|||http://purl.uniprot.org/annotation/VAR_032103|||http://purl.uniprot.org/annotation/VAR_032104|||http://purl.uniprot.org/annotation/VAR_032105|||http://purl.uniprot.org/annotation/VAR_032106|||http://purl.uniprot.org/annotation/VAR_032107|||http://purl.uniprot.org/annotation/VAR_032108|||http://purl.uniprot.org/annotation/VAR_032109|||http://purl.uniprot.org/annotation/VAR_036084|||http://purl.uniprot.org/annotation/VAR_036085
http://togogenome.org/gene/9606:CNTNAP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYK1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Contactin-associated protein-like 5|||Cytoplasmic|||EGF-like 1|||EGF-like 2|||Extracellular|||F5/8 type C|||Fibrinogen C-terminal|||Helical|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317377|||http://purl.uniprot.org/annotation/VAR_038518|||http://purl.uniprot.org/annotation/VAR_038519
http://togogenome.org/gene/9606:IFIT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T764                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Interferon-induced protein with tetratricopeptide repeats 1B|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285728|||http://purl.uniprot.org/annotation/VAR_052617
http://togogenome.org/gene/9606:AGMO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNB7|||http://purl.uniprot.org/uniprot/X5D773                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Alkylglycerol monooxygenase|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-224.|||Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-221 and A-225.|||Loss of function; when associated with A-132; A-136; A-145; A-148; A-149; A-224 and A-225.|||Loss of function; when associated with A-132; A-136; A-145; A-148; A-221; A-224 and A-225.|||Loss of function; when associated with A-132; A-136; A-145; A-149; A-221; A-224 and A-225.|||Loss of function; when associated with A-132; A-136; A-148; A-149; A-221; A-224 and A-225.|||Loss of function; when associated with A-132; A-145; A-148; A-149; A-221; A-224 and A-225.|||Loss of function; when associated with A-136; A-145; A-148; A-149; A-221; A-224 and A-225.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299300|||http://purl.uniprot.org/annotation/VAR_062201|||http://purl.uniprot.org/annotation/VAR_062202
http://togogenome.org/gene/9606:DUSP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16829                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Dual specificity protein phosphatase 7|||In isoform 2.|||Phosphocysteine intermediate|||Rhodanese|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094807|||http://purl.uniprot.org/annotation/VAR_051752|||http://purl.uniprot.org/annotation/VSP_012822
http://togogenome.org/gene/9606:ZNF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17024                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 1; atypical|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047344
http://togogenome.org/gene/9606:GNG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63218                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5|||N-acetylserine|||Phosphoserine|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012627|||http://purl.uniprot.org/annotation/PRO_0000012628
http://togogenome.org/gene/9606:SPATA31A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYR9                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||SPATA31|||SPATA31F3-like                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:HSPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3X4|||http://purl.uniprot.org/uniprot/P10809                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  60 kDa heat shock protein, mitochondrial|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HLD4; transfection with the mutant protein impairs cell growth that worsens with increasing temperature.|||In SPG13.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005026|||http://purl.uniprot.org/annotation/VAR_026748|||http://purl.uniprot.org/annotation/VAR_054785|||http://purl.uniprot.org/annotation/VSP_056144|||http://purl.uniprot.org/annotation/VSP_056145
http://togogenome.org/gene/9606:KRT33A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76009                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha3-I|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063688|||http://purl.uniprot.org/annotation/VAR_054432
http://togogenome.org/gene/9606:CDYL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8U2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Chromo|||Chromodomain Y-like protein 2|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080223
http://togogenome.org/gene/9606:FBXL20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IG2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 20|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119870|||http://purl.uniprot.org/annotation/VSP_030769
http://togogenome.org/gene/9606:ZNF395                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8N7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||No change in subcellular location; when associated with A-109.|||No change in subcellular location; when associated with A-113.|||No shuttle from the nucleus to the cytoplasm; when associated with A-169.|||No shuttle from the nucleus to the cytoplasm; when associated with A-172.|||Nuclear export signal|||Phosphoserine|||Polar residues|||Zinc finger protein 395                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047561
http://togogenome.org/gene/9606:SCUBE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS09|||http://purl.uniprot.org/uniprot/Q9NQ36                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CUB|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In isoform 2.|||In isoform 3.|||Interaction with the cholesterol-anchor of SHH|||N-linked (GlcNAc...) asparagine|||Signal peptide, CUB and EGF-like domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255580|||http://purl.uniprot.org/annotation/VAR_028870|||http://purl.uniprot.org/annotation/VAR_028871|||http://purl.uniprot.org/annotation/VAR_028872|||http://purl.uniprot.org/annotation/VAR_028873|||http://purl.uniprot.org/annotation/VAR_028874|||http://purl.uniprot.org/annotation/VSP_021293|||http://purl.uniprot.org/annotation/VSP_021294|||http://purl.uniprot.org/annotation/VSP_021295|||http://purl.uniprot.org/annotation/VSP_039955
http://togogenome.org/gene/9606:PAK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQU5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with F-566.|||CRIB|||Complete loss of PAK6 activation by MAP2K6/MAPKK6; when associated with A-165.|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||In isoform 2.|||Linker|||Phosphoserine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase PAK 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086476|||http://purl.uniprot.org/annotation/VAR_019993|||http://purl.uniprot.org/annotation/VAR_019994|||http://purl.uniprot.org/annotation/VAR_019995|||http://purl.uniprot.org/annotation/VAR_035631|||http://purl.uniprot.org/annotation/VAR_040972|||http://purl.uniprot.org/annotation/VAR_040973|||http://purl.uniprot.org/annotation/VAR_040974|||http://purl.uniprot.org/annotation/VAR_040975|||http://purl.uniprot.org/annotation/VAR_040976|||http://purl.uniprot.org/annotation/VAR_040977|||http://purl.uniprot.org/annotation/VAR_051655|||http://purl.uniprot.org/annotation/VAR_051656|||http://purl.uniprot.org/annotation/VAR_051657|||http://purl.uniprot.org/annotation/VSP_056733
http://togogenome.org/gene/9606:CENPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RHD3|||http://purl.uniprot.org/uniprot/Q9BS16                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Breakpoint for translocation to form KMT2A/MLL1-CENPK oncogene|||Centromere protein K|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249482
http://togogenome.org/gene/9606:TMEM129                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVI4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||E3 ubiquitin-protein ligase TM129|||Helical|||In isoform 2.|||Lumenal|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291041|||http://purl.uniprot.org/annotation/VAR_032803|||http://purl.uniprot.org/annotation/VSP_036641|||http://purl.uniprot.org/annotation/VSP_036642
http://togogenome.org/gene/9606:DIXDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q155Q3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Calponin-homology (CH)|||DIX|||Disordered|||Dixin|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Loss of interaction with DVL2. Abolishes activation of Wnt signaling.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287223|||http://purl.uniprot.org/annotation/VAR_032294|||http://purl.uniprot.org/annotation/VSP_025378|||http://purl.uniprot.org/annotation/VSP_025379|||http://purl.uniprot.org/annotation/VSP_025380|||http://purl.uniprot.org/annotation/VSP_025381|||http://purl.uniprot.org/annotation/VSP_054565
http://togogenome.org/gene/9606:MLF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4U8|||http://purl.uniprot.org/uniprot/A0A140VKD2|||http://purl.uniprot.org/uniprot/B2RD48|||http://purl.uniprot.org/uniprot/P58340|||http://purl.uniprot.org/uniprot/Q2TLE4|||http://purl.uniprot.org/uniprot/Q5HYH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form NPM-MLF1|||Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Interaction with COPS3|||Myeloid leukemia factor 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220752|||http://purl.uniprot.org/annotation/VAR_022070|||http://purl.uniprot.org/annotation/VSP_043130|||http://purl.uniprot.org/annotation/VSP_043131|||http://purl.uniprot.org/annotation/VSP_043725|||http://purl.uniprot.org/annotation/VSP_043726
http://togogenome.org/gene/9606:GZMH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20718                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Granzyme H|||In isoform 2.|||In isoform 3.|||Mediates the preference for acidic residues at the P3' and P4' sites|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027413|||http://purl.uniprot.org/annotation/PRO_0000027414|||http://purl.uniprot.org/annotation/VAR_014556|||http://purl.uniprot.org/annotation/VSP_047073|||http://purl.uniprot.org/annotation/VSP_047573
http://togogenome.org/gene/9606:CSNK2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19784                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Casein kinase II subunit alpha'|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085891|||http://purl.uniprot.org/annotation/VAR_040416
http://togogenome.org/gene/9606:STRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VSL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Pro residues|||Striatin-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187017|||http://purl.uniprot.org/annotation/VAR_076430|||http://purl.uniprot.org/annotation/VSP_014856|||http://purl.uniprot.org/annotation/VSP_014857|||http://purl.uniprot.org/annotation/VSP_014858|||http://purl.uniprot.org/annotation/VSP_014859|||http://purl.uniprot.org/annotation/VSP_014860|||http://purl.uniprot.org/annotation/VSP_014861|||http://purl.uniprot.org/annotation/VSP_014862
http://togogenome.org/gene/9606:CCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06307|||http://purl.uniprot.org/uniprot/Q6FG82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Cholecystokinin|||Cholecystokinin-12|||Cholecystokinin-18|||Cholecystokinin-25|||Cholecystokinin-33|||Cholecystokinin-39|||Cholecystokinin-5|||Cholecystokinin-58|||Cholecystokinin-58 desnonopeptide|||Cholecystokinin-7|||Cholecystokinin-8|||Disordered|||Gastrin/cholecystokinin peptide hormone|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phenylalanine amide|||Reduces the quantity of secreted CCK8 by 50%.|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010536|||http://purl.uniprot.org/annotation/PRO_0000010537|||http://purl.uniprot.org/annotation/PRO_0000010538|||http://purl.uniprot.org/annotation/PRO_0000010539|||http://purl.uniprot.org/annotation/PRO_0000010540|||http://purl.uniprot.org/annotation/PRO_0000010541|||http://purl.uniprot.org/annotation/PRO_0000010542|||http://purl.uniprot.org/annotation/PRO_0000010543|||http://purl.uniprot.org/annotation/PRO_0000306304|||http://purl.uniprot.org/annotation/PRO_0000306305|||http://purl.uniprot.org/annotation/PRO_0000306306|||http://purl.uniprot.org/annotation/PRO_0000306307|||http://purl.uniprot.org/annotation/PRO_0000306308|||http://purl.uniprot.org/annotation/PRO_5014310428|||http://purl.uniprot.org/annotation/VAR_018818|||http://purl.uniprot.org/annotation/VAR_024452
http://togogenome.org/gene/9606:TRPV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5S1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pore-forming|||Required for interaction with SLC50A1|||Transient receptor potential cation channel subfamily V member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215342|||http://purl.uniprot.org/annotation/VAR_024678|||http://purl.uniprot.org/annotation/VAR_059838
http://togogenome.org/gene/9606:TMEM247                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NEH6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Transmembrane protein 247                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328813
http://togogenome.org/gene/9606:TSGA10IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SY00                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Testis-specific protein 10-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331421|||http://purl.uniprot.org/annotation/VAR_042855|||http://purl.uniprot.org/annotation/VAR_042856|||http://purl.uniprot.org/annotation/VAR_042857|||http://purl.uniprot.org/annotation/VAR_042858|||http://purl.uniprot.org/annotation/VAR_042859|||http://purl.uniprot.org/annotation/VSP_033196|||http://purl.uniprot.org/annotation/VSP_033197
http://togogenome.org/gene/9606:TRIM16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP96|||http://purl.uniprot.org/uniprot/O95361                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of protection from cell death during oxidative stress; when associated with A-116.|||Loss of protection from cell death during oxidative stress; when associated with A-203.|||Phosphoserine|||Pro residues|||Tripartite motif-containing protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056222|||http://purl.uniprot.org/annotation/VAR_017412|||http://purl.uniprot.org/annotation/VAR_031668|||http://purl.uniprot.org/annotation/VAR_052133|||http://purl.uniprot.org/annotation/VSP_009098
http://togogenome.org/gene/9606:NKAPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5M9Q1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||NKAP-like protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260078|||http://purl.uniprot.org/annotation/VAR_028999|||http://purl.uniprot.org/annotation/VAR_029000|||http://purl.uniprot.org/annotation/VAR_029001|||http://purl.uniprot.org/annotation/VAR_029002
http://togogenome.org/gene/9606:EIF5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZV4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 5A-2|||Hypusine|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229764|||http://purl.uniprot.org/annotation/VAR_027943
http://togogenome.org/gene/9606:CCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41597                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-C chemokine receptor type 2|||Confers relative resistance to infection by HIV-1; delay in disease progression in African Americans but not in Caucasians.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by JAK2|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069232|||http://purl.uniprot.org/annotation/VAR_014339|||http://purl.uniprot.org/annotation/VAR_014340|||http://purl.uniprot.org/annotation/VAR_020066|||http://purl.uniprot.org/annotation/VSP_001893
http://togogenome.org/gene/9606:ZBTB41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SVQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||Zinc finger and BTB domain-containing protein 41                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277814|||http://purl.uniprot.org/annotation/VAR_030601|||http://purl.uniprot.org/annotation/VSP_023092|||http://purl.uniprot.org/annotation/VSP_023093
http://togogenome.org/gene/9606:RS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15537                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  F5/8 type C|||In XLRS1.|||In XLRS1; decreases protein stability; does not abrogate oligomerization or secretion.|||In XLRS1; loss of octamerization; no effect on secretion.|||In XLRS1; loss of secretion into the extracellular space; may impair protein folding.|||In XLRS1; no effect on oligomerization; no effect on protein stability.|||Interchain|||Interchain (with C-223)|||Interchain (with C-59)|||Retinoschisin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022695|||http://purl.uniprot.org/annotation/VAR_008180|||http://purl.uniprot.org/annotation/VAR_008181|||http://purl.uniprot.org/annotation/VAR_008182|||http://purl.uniprot.org/annotation/VAR_008183|||http://purl.uniprot.org/annotation/VAR_008184|||http://purl.uniprot.org/annotation/VAR_008185|||http://purl.uniprot.org/annotation/VAR_008209|||http://purl.uniprot.org/annotation/VAR_008210|||http://purl.uniprot.org/annotation/VAR_008211|||http://purl.uniprot.org/annotation/VAR_008212|||http://purl.uniprot.org/annotation/VAR_008213|||http://purl.uniprot.org/annotation/VAR_008214|||http://purl.uniprot.org/annotation/VAR_008215|||http://purl.uniprot.org/annotation/VAR_008216|||http://purl.uniprot.org/annotation/VAR_008217|||http://purl.uniprot.org/annotation/VAR_008218|||http://purl.uniprot.org/annotation/VAR_008219|||http://purl.uniprot.org/annotation/VAR_008220|||http://purl.uniprot.org/annotation/VAR_008221|||http://purl.uniprot.org/annotation/VAR_008222|||http://purl.uniprot.org/annotation/VAR_008223|||http://purl.uniprot.org/annotation/VAR_008224|||http://purl.uniprot.org/annotation/VAR_008225|||http://purl.uniprot.org/annotation/VAR_008226|||http://purl.uniprot.org/annotation/VAR_008227|||http://purl.uniprot.org/annotation/VAR_008228|||http://purl.uniprot.org/annotation/VAR_008229|||http://purl.uniprot.org/annotation/VAR_008230|||http://purl.uniprot.org/annotation/VAR_008231|||http://purl.uniprot.org/annotation/VAR_008232|||http://purl.uniprot.org/annotation/VAR_008233|||http://purl.uniprot.org/annotation/VAR_008234|||http://purl.uniprot.org/annotation/VAR_008235|||http://purl.uniprot.org/annotation/VAR_008236|||http://purl.uniprot.org/annotation/VAR_008237|||http://purl.uniprot.org/annotation/VAR_008238|||http://purl.uniprot.org/annotation/VAR_008239|||http://purl.uniprot.org/annotation/VAR_008240|||http://purl.uniprot.org/annotation/VAR_008241|||http://purl.uniprot.org/annotation/VAR_008242|||http://purl.uniprot.org/annotation/VAR_008243|||http://purl.uniprot.org/annotation/VAR_008244|||http://purl.uniprot.org/annotation/VAR_008245|||http://purl.uniprot.org/annotation/VAR_008246|||http://purl.uniprot.org/annotation/VAR_008247|||http://purl.uniprot.org/annotation/VAR_008248|||http://purl.uniprot.org/annotation/VAR_008249|||http://purl.uniprot.org/annotation/VAR_008251|||http://purl.uniprot.org/annotation/VAR_008252|||http://purl.uniprot.org/annotation/VAR_008253|||http://purl.uniprot.org/annotation/VAR_008254|||http://purl.uniprot.org/annotation/VAR_008255|||http://purl.uniprot.org/annotation/VAR_008256|||http://purl.uniprot.org/annotation/VAR_008257|||http://purl.uniprot.org/annotation/VAR_008258|||http://purl.uniprot.org/annotation/VAR_008259|||http://purl.uniprot.org/annotation/VAR_008260|||http://purl.uniprot.org/annotation/VAR_008261|||http://purl.uniprot.org/annotation/VAR_008262|||http://purl.uniprot.org/annotation/VAR_012078|||http://purl.uniprot.org/annotation/VAR_023959|||http://purl.uniprot.org/annotation/VAR_065326|||http://purl.uniprot.org/annotation/VAR_065327|||http://purl.uniprot.org/annotation/VAR_065328|||http://purl.uniprot.org/annotation/VAR_065329|||http://purl.uniprot.org/annotation/VAR_065330|||http://purl.uniprot.org/annotation/VAR_065331|||http://purl.uniprot.org/annotation/VAR_080439|||http://purl.uniprot.org/annotation/VAR_080440
http://togogenome.org/gene/9606:IRF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G0Z349|||http://purl.uniprot.org/uniprot/O14896                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3% in European-descended and 22% in Asian populations; responsible for 12% of the genetic contribution to cleft lip or palate; tripled the risk of recurrence in families that already had 1 affected child.|||Disordered|||IRF tryptophan pentad repeat|||In PPS.|||In PPS; abrogates DNA binding.|||In PPS; significant decrease of transcriptional activity.|||In PPS; unknown pathological significance.|||In VWS1 and OFC6.|||In VWS1 and PPS; abrogates DNA binding.|||In VWS1.|||In VWS1; abrogates DNA binding.|||In VWS1; does not affect DNA binding.|||In isoform 2.|||Interferon regulatory factor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154560|||http://purl.uniprot.org/annotation/VAR_014961|||http://purl.uniprot.org/annotation/VAR_014962|||http://purl.uniprot.org/annotation/VAR_014963|||http://purl.uniprot.org/annotation/VAR_014964|||http://purl.uniprot.org/annotation/VAR_014965|||http://purl.uniprot.org/annotation/VAR_014966|||http://purl.uniprot.org/annotation/VAR_014967|||http://purl.uniprot.org/annotation/VAR_014968|||http://purl.uniprot.org/annotation/VAR_014969|||http://purl.uniprot.org/annotation/VAR_014970|||http://purl.uniprot.org/annotation/VAR_014971|||http://purl.uniprot.org/annotation/VAR_014972|||http://purl.uniprot.org/annotation/VAR_014973|||http://purl.uniprot.org/annotation/VAR_014974|||http://purl.uniprot.org/annotation/VAR_014975|||http://purl.uniprot.org/annotation/VAR_014976|||http://purl.uniprot.org/annotation/VAR_014977|||http://purl.uniprot.org/annotation/VAR_014978|||http://purl.uniprot.org/annotation/VAR_014979|||http://purl.uniprot.org/annotation/VAR_014980|||http://purl.uniprot.org/annotation/VAR_014981|||http://purl.uniprot.org/annotation/VAR_014982|||http://purl.uniprot.org/annotation/VAR_014983|||http://purl.uniprot.org/annotation/VAR_014984|||http://purl.uniprot.org/annotation/VAR_014985|||http://purl.uniprot.org/annotation/VAR_014986|||http://purl.uniprot.org/annotation/VAR_014987|||http://purl.uniprot.org/annotation/VAR_014988|||http://purl.uniprot.org/annotation/VAR_014989|||http://purl.uniprot.org/annotation/VAR_014990|||http://purl.uniprot.org/annotation/VAR_014991|||http://purl.uniprot.org/annotation/VAR_030046|||http://purl.uniprot.org/annotation/VAR_030047|||http://purl.uniprot.org/annotation/VAR_030048|||http://purl.uniprot.org/annotation/VAR_030049|||http://purl.uniprot.org/annotation/VAR_030050|||http://purl.uniprot.org/annotation/VAR_030051|||http://purl.uniprot.org/annotation/VAR_030052|||http://purl.uniprot.org/annotation/VAR_030053|||http://purl.uniprot.org/annotation/VAR_030054|||http://purl.uniprot.org/annotation/VAR_030055|||http://purl.uniprot.org/annotation/VAR_030056|||http://purl.uniprot.org/annotation/VAR_059080|||http://purl.uniprot.org/annotation/VAR_064475|||http://purl.uniprot.org/annotation/VAR_064476|||http://purl.uniprot.org/annotation/VAR_085700|||http://purl.uniprot.org/annotation/VSP_046435
http://togogenome.org/gene/9606:PRSS38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L453                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Serine protease 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328820|||http://purl.uniprot.org/annotation/PRO_0000328821|||http://purl.uniprot.org/annotation/VAR_042531
http://togogenome.org/gene/9606:PAGE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2X7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||P antigen family member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247362|||http://purl.uniprot.org/annotation/VAR_053099
http://togogenome.org/gene/9606:MAGED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNF1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In BARTS5.|||In BARTS5; loss of interaction with GNAS.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||MAGE|||Melanoma-associated antigen D2|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156727|||http://purl.uniprot.org/annotation/VAR_011639|||http://purl.uniprot.org/annotation/VAR_036584|||http://purl.uniprot.org/annotation/VAR_053508|||http://purl.uniprot.org/annotation/VAR_076836|||http://purl.uniprot.org/annotation/VAR_076837|||http://purl.uniprot.org/annotation/VSP_008030
http://togogenome.org/gene/9606:LIMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNZ3|||http://purl.uniprot.org/uniprot/Q7Z4I7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In MDRCMTT; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM and senescent cell antigen-like-containing domain protein 2|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||LIM zinc-binding 5|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000266011|||http://purl.uniprot.org/annotation/VAR_076527|||http://purl.uniprot.org/annotation/VAR_076528|||http://purl.uniprot.org/annotation/VAR_076529|||http://purl.uniprot.org/annotation/VSP_021916|||http://purl.uniprot.org/annotation/VSP_021917|||http://purl.uniprot.org/annotation/VSP_045539|||http://purl.uniprot.org/annotation/VSP_046078
http://togogenome.org/gene/9606:TEX261                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWH6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Protein TEX261                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247433
http://togogenome.org/gene/9606:LIN7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14910                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Kinase interacting site|||L27|||PDZ|||Protein lin-7 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189623
http://togogenome.org/gene/9606:PRR23B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Proline-rich protein 23B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332251
http://togogenome.org/gene/9606:FAM86B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PN63|||http://purl.uniprot.org/uniprot/Q8N7N1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  FAM86 N-terminal|||In isoform 2.|||Putative protein N-methyltransferase FAM86B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307251|||http://purl.uniprot.org/annotation/VSP_028646|||http://purl.uniprot.org/annotation/VSP_028647
http://togogenome.org/gene/9606:FCHO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C3SFZ9|||http://purl.uniprot.org/uniprot/B7ZAZ3|||http://purl.uniprot.org/uniprot/O14526                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-BAR|||F-BAR domain only protein 1|||In IMD76.|||In IMD76; no effect on protein levels; formation of large cell membrane-dissociated agglomerations; failed to facilitate the formation of clathrin-coated vesicles; impaired TCR internalization.|||In IMD76; no effect on protein levels; loss of clathrin-coated vesicles location and association with cell membrane; failed to facilitate the formation of clathrin-coated vesicles; impaired TCR internalization.|||In isoform 2.|||In isoform 3.|||MHD|||Mediates interaction with AGFG1, CALM, DAB2, EPS15, EPS15R, ITSN1 and clathrin|||Mediates interaction with the adaptor protein complex AP-2|||Mediates membrane-binding|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271759|||http://purl.uniprot.org/annotation/VAR_085363|||http://purl.uniprot.org/annotation/VAR_085364|||http://purl.uniprot.org/annotation/VAR_085365|||http://purl.uniprot.org/annotation/VSP_022338|||http://purl.uniprot.org/annotation/VSP_046906
http://togogenome.org/gene/9606:COX8C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4L0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 8C, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006201
http://togogenome.org/gene/9606:ZNF124                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QKQ6|||http://purl.uniprot.org/uniprot/Q15973                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||KRAB|||Zinc finger protein 124                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047410|||http://purl.uniprot.org/annotation/VSP_006895|||http://purl.uniprot.org/annotation/VSP_015691|||http://purl.uniprot.org/annotation/VSP_015692|||http://purl.uniprot.org/annotation/VSP_046852
http://togogenome.org/gene/9606:GTF3C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNH2|||http://purl.uniprot.org/uniprot/Q9UKN8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||General transcription factor 3C polypeptide 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Transcription factor IIIC putative zinc-finger                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209713
http://togogenome.org/gene/9606:GALNTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4T8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059143|||http://purl.uniprot.org/annotation/VAR_019592|||http://purl.uniprot.org/annotation/VAR_080036|||http://purl.uniprot.org/annotation/VSP_011227|||http://purl.uniprot.org/annotation/VSP_011228
http://togogenome.org/gene/9606:PLA2G4E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MJ16                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Cytosolic phospholipase A2 epsilon|||Disordered|||Impairs localization at membrane structures and N-acyl transferase activity.|||In isoform 2.|||Nucleophile|||PLA2c|||Phosphoserine|||Proton acceptor|||Required for localization at membrane structures                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247025|||http://purl.uniprot.org/annotation/VAR_027052|||http://purl.uniprot.org/annotation/VAR_027053|||http://purl.uniprot.org/annotation/VSP_019883
http://togogenome.org/gene/9606:MEN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00255|||http://purl.uniprot.org/uniprot/Q9GZQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a parathyroid carcinoma sample; somatic mutation.|||In MEN1 and parathyroid tumor.|||In MEN1.|||In MEN1; almost complete loss of histone methylation; almost no effect on JUND-binding; yields insoluble protein.|||In MEN1; almost complete loss of histone methylation; loss of JUND-binding; no repression of JUND transactivation; reduced interaction with KMT2A.|||In MEN1; almost complete loss of histone methylation; strong decrease in JUND-binding; no repression of JUND transactivation; reduced interaction with KMT2A.|||In MEN1; almost no effect on JUND-binding.|||In MEN1; also found in isolated hyperparathyroidism.|||In MEN1; familial and sporadic cases; almost no effect on JUND-binding; no repression of JUND transactivation.|||In MEN1; loss of JUND-binding.|||In MEN1; loss of interaction with KMT2A and JUND.|||In MEN1; no effect on histone methylation; almost no effect on JUND-binding.|||In MEN1; no effect on histone methylation; almost no effect on JUND-binding; modest repression of JUND transactivation.|||In MEN1; no effect on histone methylation; almost no effect on JUND-binding; no repression of JUND transactivation.|||In MEN1; sporadic; with Zollinger-Ellison syndrome.|||In MEN1; strong decrease in JUND-binding.|||In adrenal adenoma; somatic.|||In isoform 2.|||In isoform 3.|||In parathyroid adenoma and MEN1.|||In parathyroid tumor.|||In parathyroid tumors; somatic.|||Interaction with FANCD2|||Loss of interaction with KMT2A and JUND.|||Menin|||Phosphoserine|||Phosphothreonine|||Probable disease-associated variant found in isolated hyperparathyroidism.|||Reduced interaction with KMT2A.|||Reduced interaction with KMT2A; when associated with A-366.|||Reduced interaction with KMT2A; when associated with A-370.|||Reduced interaction with KMT2A; when associated with R-285 and R-288.|||Reduced interaction with KMT2A; when associated with R-285 and R-290.|||Reduced interaction with KMT2A; when associated with R-288 and R-290.|||Requires 2 nucleotide substitutions; yields insoluble protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096411|||http://purl.uniprot.org/annotation/VAR_005425|||http://purl.uniprot.org/annotation/VAR_005426|||http://purl.uniprot.org/annotation/VAR_005427|||http://purl.uniprot.org/annotation/VAR_005428|||http://purl.uniprot.org/annotation/VAR_005429|||http://purl.uniprot.org/annotation/VAR_005430|||http://purl.uniprot.org/annotation/VAR_005431|||http://purl.uniprot.org/annotation/VAR_005432|||http://purl.uniprot.org/annotation/VAR_005433|||http://purl.uniprot.org/annotation/VAR_005434|||http://purl.uniprot.org/annotation/VAR_005436|||http://purl.uniprot.org/annotation/VAR_005437|||http://purl.uniprot.org/annotation/VAR_005438|||http://purl.uniprot.org/annotation/VAR_005439|||http://purl.uniprot.org/annotation/VAR_005440|||http://purl.uniprot.org/annotation/VAR_005441|||http://purl.uniprot.org/annotation/VAR_005442|||http://purl.uniprot.org/annotation/VAR_005443|||http://purl.uniprot.org/annotation/VAR_005444|||http://purl.uniprot.org/annotation/VAR_005445|||http://purl.uniprot.org/annotation/VAR_005446|||http://purl.uniprot.org/annotation/VAR_005447|||http://purl.uniprot.org/annotation/VAR_005448|||http://purl.uniprot.org/annotation/VAR_005449|||http://purl.uniprot.org/annotation/VAR_005450|||http://purl.uniprot.org/annotation/VAR_005451|||http://purl.uniprot.org/annotation/VAR_005452|||http://purl.uniprot.org/annotation/VAR_005453|||http://purl.uniprot.org/annotation/VAR_005454|||http://purl.uniprot.org/annotation/VAR_005455|||http://purl.uniprot.org/annotation/VAR_005456|||http://purl.uniprot.org/annotation/VAR_005457|||http://purl.uniprot.org/annotation/VAR_005458|||http://purl.uniprot.org/annotation/VAR_005459|||http://purl.uniprot.org/annotation/VAR_005460|||http://purl.uniprot.org/annotation/VAR_005461|||http://purl.uniprot.org/annotation/VAR_005462|||http://purl.uniprot.org/annotation/VAR_005463|||http://purl.uniprot.org/annotation/VAR_005464|||http://purl.uniprot.org/annotation/VAR_005465|||http://purl.uniprot.org/annotation/VAR_005466|||http://purl.uniprot.org/annotation/VAR_005467|||http://purl.uniprot.org/annotation/VAR_008017|||http://purl.uniprot.org/annotation/VAR_008018|||http://purl.uniprot.org/annotation/VAR_039587|||http://purl.uniprot.org/annotation/VAR_039588|||http://purl.uniprot.org/annotation/VAR_039589|||http://purl.uniprot.org/annotation/VAR_039590|||http://purl.uniprot.org/annotation/VAR_039591|||http://purl.uniprot.org/annotation/VAR_039592|||http://purl.uniprot.org/annotation/VAR_039593|||http://purl.uniprot.org/annotation/VAR_039594|||http://purl.uniprot.org/annotation/VAR_039595|||http://purl.uniprot.org/annotation/VAR_039596|||http://purl.uniprot.org/annotation/VAR_039597|||http://purl.uniprot.org/annotation/VAR_039598|||http://purl.uniprot.org/annotation/VAR_039599|||http://purl.uniprot.org/annotation/VAR_039600|||http://purl.uniprot.org/annotation/VAR_039601|||http://purl.uniprot.org/annotation/VAR_039602|||http://purl.uniprot.org/annotation/VAR_039603|||http://purl.uniprot.org/annotation/VAR_039604|||http://purl.uniprot.org/annotation/VAR_039605|||http://purl.uniprot.org/annotation/VAR_039606|||http://purl.uniprot.org/annotation/VAR_039607|||http://purl.uniprot.org/annotation/VAR_039608|||http://purl.uniprot.org/annotation/VAR_039609|||http://purl.uniprot.org/annotation/VAR_039610|||http://purl.uniprot.org/annotation/VAR_039611|||http://purl.uniprot.org/annotation/VAR_039612|||http://purl.uniprot.org/annotation/VAR_039613|||http://purl.uniprot.org/annotation/VAR_039614|||http://purl.uniprot.org/annotation/VAR_039615|||http://purl.uniprot.org/annotation/VAR_039616|||http://purl.uniprot.org/annotation/VAR_039617|||http://purl.uniprot.org/annotation/VAR_039618|||http://purl.uniprot.org/annotation/VAR_039619|||http://purl.uniprot.org/annotation/VAR_039620|||http://purl.uniprot.org/annotation/VAR_039621|||http://purl.uniprot.org/annotation/VAR_039622|||http://purl.uniprot.org/annotation/VAR_039623|||http://purl.uniprot.org/annotation/VAR_039624|||http://purl.uniprot.org/annotation/VAR_039625|||http://purl.uniprot.org/annotation/VAR_039626|||http://purl.uniprot.org/annotation/VAR_039627|||http://purl.uniprot.org/annotation/VAR_039628|||http://purl.uniprot.org/annotation/VAR_039629|||http://purl.uniprot.org/annotation/VAR_039630|||http://purl.uniprot.org/annotation/VAR_039631|||http://purl.uniprot.org/annotation/VAR_039632|||http://purl.uniprot.org/annotation/VAR_039633|||http://purl.uniprot.org/annotation/VAR_039634|||http://purl.uniprot.org/annotation/VAR_039635|||http://purl.uniprot.org/annotation/VAR_039636|||http://purl.uniprot.org/annotation/VAR_039637|||http://purl.uniprot.org/annotation/VAR_039638|||http://purl.uniprot.org/annotation/VAR_039639|||http://purl.uniprot.org/annotation/VAR_039640|||http://purl.uniprot.org/annotation/VAR_039641|||http://purl.uniprot.org/annotation/VAR_039642|||http://purl.uniprot.org/annotation/VAR_039643|||http://purl.uniprot.org/annotation/VAR_039644|||http://purl.uniprot.org/annotation/VAR_039645|||http://purl.uniprot.org/annotation/VAR_039646|||http://purl.uniprot.org/annotation/VAR_039647|||http://purl.uniprot.org/annotation/VAR_064937|||http://purl.uniprot.org/annotation/VAR_065152|||http://purl.uniprot.org/annotation/VAR_065153|||http://purl.uniprot.org/annotation/VAR_065154|||http://purl.uniprot.org/annotation/VAR_065155|||http://purl.uniprot.org/annotation/VAR_065156|||http://purl.uniprot.org/annotation/VAR_082607|||http://purl.uniprot.org/annotation/VSP_004323|||http://purl.uniprot.org/annotation/VSP_015854|||http://purl.uniprot.org/annotation/VSP_062035
http://togogenome.org/gene/9606:SPEM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P670                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Uncharacterized protein SPEM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286623|||http://purl.uniprot.org/annotation/VAR_032145|||http://purl.uniprot.org/annotation/VAR_032146
http://togogenome.org/gene/9606:RNASE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07998|||http://purl.uniprot.org/uniprot/W0UV93                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||No effect on inhibition by RNH1.|||Proton acceptor|||Proton donor|||Ribonuclease A-domain|||Ribonuclease pancreatic|||Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, A-116, D-117 and D-119.|||Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-117.|||Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, A-116 and D-119.|||Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-67, D-95, D-117 and D-119.|||Substantially decreases binding affinity for RNH1 but maintains high conformational stability; when associated with D-95, A-116, D-117 and D-119.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030921|||http://purl.uniprot.org/annotation/PRO_5007751500
http://togogenome.org/gene/9606:NECAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC96                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adaptin ear-binding coat-associated protein 1|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphothreonine|||WXXF motif 1|||WXXF motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213067|||http://purl.uniprot.org/annotation/VAR_034153|||http://purl.uniprot.org/annotation/VSP_013232|||http://purl.uniprot.org/annotation/VSP_013233
http://togogenome.org/gene/9606:CTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NKJ3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CST complex subunit CTC1|||Disordered|||In CRMCC1.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287181|||http://purl.uniprot.org/annotation/VAR_032282|||http://purl.uniprot.org/annotation/VAR_032283|||http://purl.uniprot.org/annotation/VAR_067369|||http://purl.uniprot.org/annotation/VAR_067370|||http://purl.uniprot.org/annotation/VAR_067371|||http://purl.uniprot.org/annotation/VAR_067372|||http://purl.uniprot.org/annotation/VAR_067373|||http://purl.uniprot.org/annotation/VAR_067374|||http://purl.uniprot.org/annotation/VAR_067375|||http://purl.uniprot.org/annotation/VAR_067376|||http://purl.uniprot.org/annotation/VAR_067377|||http://purl.uniprot.org/annotation/VAR_067378|||http://purl.uniprot.org/annotation/VAR_067379|||http://purl.uniprot.org/annotation/VSP_025351|||http://purl.uniprot.org/annotation/VSP_025352|||http://purl.uniprot.org/annotation/VSP_025353
http://togogenome.org/gene/9606:TUBGCP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RT8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gamma-tubulin complex component 5|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078129|||http://purl.uniprot.org/annotation/VAR_049252|||http://purl.uniprot.org/annotation/VSP_047496
http://togogenome.org/gene/9606:ARHGAP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ74|||http://purl.uniprot.org/uniprot/Q9BRR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||Lipid binding|||PH|||Phosphoserine|||Polar residues|||Reduced affinity for phosphoinositides.|||Rho GTPase-activating protein 9|||Rho-GAP|||SH3|||Strongly reduced affinity for phosphoinositides.|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056712|||http://purl.uniprot.org/annotation/VAR_055830|||http://purl.uniprot.org/annotation/VAR_055831|||http://purl.uniprot.org/annotation/VAR_055832|||http://purl.uniprot.org/annotation/VSP_010325|||http://purl.uniprot.org/annotation/VSP_010340|||http://purl.uniprot.org/annotation/VSP_046391
http://togogenome.org/gene/9606:COMTD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Catechol O-methyltransferase domain-containing protein 1|||Helical; Signal-anchor for type II membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233289
http://togogenome.org/gene/9606:NET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SQI5|||http://purl.uniprot.org/uniprot/Q5SQI7|||http://purl.uniprot.org/uniprot/Q7Z628                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylmethionine|||Necessary for nuclear localization|||Neuroepithelial cell-transforming gene 1 protein|||Nuclear localization signal|||PH|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080924|||http://purl.uniprot.org/annotation/VAR_035972|||http://purl.uniprot.org/annotation/VAR_051982|||http://purl.uniprot.org/annotation/VSP_011619|||http://purl.uniprot.org/annotation/VSP_011620
http://togogenome.org/gene/9606:IL17D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAD2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Interleukin-17D|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015430
http://togogenome.org/gene/9606:SETBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6X0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 8 AA tandem repeats of P-P-L-P-P-P-P-P|||A.T hook 1|||A.T hook 2|||A.T hook 3|||Basic and acidic residues|||Basic residues|||Disordered|||In ACML; somatic mutation in ACML and other myeloid malignancies.|||In AML.|||In MDS and myeloid malignancies.|||In SGMFS and ACML; somatic mutation in ACML and other myeloid malignancies.|||In SGMFS, ACML, JMML and MDS; also found in other myeloid malignancies; somatic mutation.|||In SGMFS, ACML, MDS and AML; somatic mutation in ACML and other myeloid malignancies; results in higher protein levels; cells expressing this mutant exhibit higher proliferation rates than those expressing the wild-type protein.|||In SGMFS.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In myeloid malignancies.|||N6-acetyllysine|||Polar residues|||Pro residues|||SET-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097698|||http://purl.uniprot.org/annotation/VAR_020317|||http://purl.uniprot.org/annotation/VAR_024347|||http://purl.uniprot.org/annotation/VAR_035987|||http://purl.uniprot.org/annotation/VAR_054646|||http://purl.uniprot.org/annotation/VAR_063806|||http://purl.uniprot.org/annotation/VAR_063807|||http://purl.uniprot.org/annotation/VAR_063808|||http://purl.uniprot.org/annotation/VAR_063809|||http://purl.uniprot.org/annotation/VAR_063810|||http://purl.uniprot.org/annotation/VAR_069848|||http://purl.uniprot.org/annotation/VAR_069849|||http://purl.uniprot.org/annotation/VAR_069850|||http://purl.uniprot.org/annotation/VAR_069851|||http://purl.uniprot.org/annotation/VAR_069852|||http://purl.uniprot.org/annotation/VAR_069853|||http://purl.uniprot.org/annotation/VAR_069854|||http://purl.uniprot.org/annotation/VAR_069855|||http://purl.uniprot.org/annotation/VAR_069856|||http://purl.uniprot.org/annotation/VAR_069857|||http://purl.uniprot.org/annotation/VAR_069858|||http://purl.uniprot.org/annotation/VAR_069859|||http://purl.uniprot.org/annotation/VAR_069860|||http://purl.uniprot.org/annotation/VAR_069861|||http://purl.uniprot.org/annotation/VAR_069862|||http://purl.uniprot.org/annotation/VAR_069863|||http://purl.uniprot.org/annotation/VAR_069864|||http://purl.uniprot.org/annotation/VSP_039060|||http://purl.uniprot.org/annotation/VSP_039061
http://togogenome.org/gene/9606:IL36RN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBH0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  In PSORS14.|||In PSORS14; expression of the protein is severely impaired compared to wild-type; the mutant protein is substantially less able to inhibit IL1RL2 signaling than wild-type.|||In PSORS14; shows impaired expression of the mutant protein which fails to antagonize the IL-36 signaling pathway.|||Interleukin-36 receptor antagonist protein|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153642|||http://purl.uniprot.org/annotation/VAR_023239|||http://purl.uniprot.org/annotation/VAR_066646|||http://purl.uniprot.org/annotation/VAR_066647|||http://purl.uniprot.org/annotation/VAR_066648|||http://purl.uniprot.org/annotation/VAR_068972
http://togogenome.org/gene/9606:SH3RF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6J0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Decreased Rac-binding ability.|||Decreased level of phosphorylation and Rac-binding ability and important loss of the ability to induce apoptosis.|||Decreased level of phosphorylation and no change in the ability to induce apoptosis.|||Disordered|||E3 ubiquitin-protein ligase SH3RF1|||In isoform 2.|||Interaction with AKT2|||Interaction with RAC1|||Loss of Ubl activity.|||Phosphoserine|||Polar residues|||RING-type|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||Significant reduction in autoubiquitination; when associated with A-28.|||Significant reduction in autoubiquitination; when associated with A-30.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334151|||http://purl.uniprot.org/annotation/VAR_043342|||http://purl.uniprot.org/annotation/VSP_033622|||http://purl.uniprot.org/annotation/VSP_033623
http://togogenome.org/gene/9606:S1PR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21453                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acts as a dominant negative GPCR and inhibits S1P-induced Rac activation, chemotaxis, and angiogenesis.|||Cytoplasmic|||Disordered|||Drastically reduced affinity for sphingosine 1-phosphate.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs sphingosine 1-phosphate binding and signaling.|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine; by PKB/AKT1|||Polar residues|||S-palmitoyl cysteine|||Slight activation of the receptor at maximal ligand concentration.|||Sphingosine 1-phosphate receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069412|||http://purl.uniprot.org/annotation/VAR_046158|||http://purl.uniprot.org/annotation/VAR_046159|||http://purl.uniprot.org/annotation/VAR_046160
http://togogenome.org/gene/9606:BPIFB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDL5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPI fold-containing family B member 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017180|||http://purl.uniprot.org/annotation/VAR_016756|||http://purl.uniprot.org/annotation/VAR_016757|||http://purl.uniprot.org/annotation/VAR_023361|||http://purl.uniprot.org/annotation/VAR_023362|||http://purl.uniprot.org/annotation/VAR_049747|||http://purl.uniprot.org/annotation/VAR_049748|||http://purl.uniprot.org/annotation/VAR_049749|||http://purl.uniprot.org/annotation/VAR_049750|||http://purl.uniprot.org/annotation/VSP_015285|||http://purl.uniprot.org/annotation/VSP_015286|||http://purl.uniprot.org/annotation/VSP_015287|||http://purl.uniprot.org/annotation/VSP_015288
http://togogenome.org/gene/9606:ADGRE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L1B9|||http://purl.uniprot.org/uniprot/B7Z5A1|||http://purl.uniprot.org/uniprot/E7EW83|||http://purl.uniprot.org/uniprot/Q0IJ53|||http://purl.uniprot.org/uniprot/Q9BY15                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor E3|||Cleavage|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012876|||http://purl.uniprot.org/annotation/PRO_5002635832|||http://purl.uniprot.org/annotation/PRO_5002866463|||http://purl.uniprot.org/annotation/PRO_5003217361|||http://purl.uniprot.org/annotation/PRO_5004173996|||http://purl.uniprot.org/annotation/VAR_024472|||http://purl.uniprot.org/annotation/VAR_055926|||http://purl.uniprot.org/annotation/VAR_060442|||http://purl.uniprot.org/annotation/VSP_009417|||http://purl.uniprot.org/annotation/VSP_009418
http://togogenome.org/gene/9606:NDP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00604                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  CTCK|||Impairs oligomerization.|||In EVR2 and ND; reduced amount of protein in the extracellular matrix.|||In EVR2.|||In EVR2; the patient presented significant phenotypic heterogeneity between the two eyes.|||In ND and EVR2.|||In ND.|||In ND; reduction of protein amount in the extracellular matrix.|||In ND; unknown pathological significance.|||In persistent fetal vasculature syndrome.|||In retinopathy of prematurity.|||Interchain|||Interchain (with C-93)|||Interchain (with C-95)|||Norrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021794|||http://purl.uniprot.org/annotation/VAR_005478|||http://purl.uniprot.org/annotation/VAR_005479|||http://purl.uniprot.org/annotation/VAR_005480|||http://purl.uniprot.org/annotation/VAR_005481|||http://purl.uniprot.org/annotation/VAR_005482|||http://purl.uniprot.org/annotation/VAR_005483|||http://purl.uniprot.org/annotation/VAR_005484|||http://purl.uniprot.org/annotation/VAR_005485|||http://purl.uniprot.org/annotation/VAR_005486|||http://purl.uniprot.org/annotation/VAR_005487|||http://purl.uniprot.org/annotation/VAR_005488|||http://purl.uniprot.org/annotation/VAR_005489|||http://purl.uniprot.org/annotation/VAR_005490|||http://purl.uniprot.org/annotation/VAR_005491|||http://purl.uniprot.org/annotation/VAR_005492|||http://purl.uniprot.org/annotation/VAR_005494|||http://purl.uniprot.org/annotation/VAR_005495|||http://purl.uniprot.org/annotation/VAR_005496|||http://purl.uniprot.org/annotation/VAR_005497|||http://purl.uniprot.org/annotation/VAR_005498|||http://purl.uniprot.org/annotation/VAR_005499|||http://purl.uniprot.org/annotation/VAR_005500|||http://purl.uniprot.org/annotation/VAR_005501|||http://purl.uniprot.org/annotation/VAR_005502|||http://purl.uniprot.org/annotation/VAR_005503|||http://purl.uniprot.org/annotation/VAR_005504|||http://purl.uniprot.org/annotation/VAR_005505|||http://purl.uniprot.org/annotation/VAR_009275|||http://purl.uniprot.org/annotation/VAR_016048|||http://purl.uniprot.org/annotation/VAR_016049|||http://purl.uniprot.org/annotation/VAR_016050|||http://purl.uniprot.org/annotation/VAR_016051|||http://purl.uniprot.org/annotation/VAR_034137|||http://purl.uniprot.org/annotation/VAR_063998|||http://purl.uniprot.org/annotation/VAR_063999|||http://purl.uniprot.org/annotation/VAR_064000|||http://purl.uniprot.org/annotation/VAR_064001|||http://purl.uniprot.org/annotation/VAR_064002|||http://purl.uniprot.org/annotation/VAR_064003|||http://purl.uniprot.org/annotation/VAR_064004|||http://purl.uniprot.org/annotation/VAR_064005|||http://purl.uniprot.org/annotation/VAR_064006|||http://purl.uniprot.org/annotation/VAR_064007|||http://purl.uniprot.org/annotation/VAR_064008|||http://purl.uniprot.org/annotation/VAR_064009|||http://purl.uniprot.org/annotation/VAR_064010|||http://purl.uniprot.org/annotation/VAR_064011|||http://purl.uniprot.org/annotation/VAR_064012|||http://purl.uniprot.org/annotation/VAR_064013|||http://purl.uniprot.org/annotation/VAR_064014|||http://purl.uniprot.org/annotation/VAR_064015|||http://purl.uniprot.org/annotation/VAR_064016|||http://purl.uniprot.org/annotation/VAR_064017|||http://purl.uniprot.org/annotation/VAR_064018|||http://purl.uniprot.org/annotation/VAR_064019|||http://purl.uniprot.org/annotation/VAR_064020|||http://purl.uniprot.org/annotation/VAR_064021|||http://purl.uniprot.org/annotation/VAR_064022|||http://purl.uniprot.org/annotation/VAR_064023|||http://purl.uniprot.org/annotation/VAR_064024|||http://purl.uniprot.org/annotation/VAR_064025|||http://purl.uniprot.org/annotation/VAR_064026|||http://purl.uniprot.org/annotation/VAR_085735
http://togogenome.org/gene/9606:OR52B6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGF0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52B6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150769|||http://purl.uniprot.org/annotation/VAR_048077|||http://purl.uniprot.org/annotation/VAR_048078|||http://purl.uniprot.org/annotation/VAR_048079|||http://purl.uniprot.org/annotation/VAR_048080|||http://purl.uniprot.org/annotation/VAR_048081
http://togogenome.org/gene/9606:WNK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D8Z4|||http://purl.uniprot.org/uniprot/F5GWT4|||http://purl.uniprot.org/uniprot/Q9H4A3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with EMC2.|||Abolished serine/threonine-protein kinase activity.|||Abolished serine/threonine-protein kinase activity. Does not affect ability to activate SGK1.|||Amphipathic alpha-helix|||Autoinhibitory domain|||Basic and acidic residues|||Basic residues|||Decreased autophosphorylation, preventing activation of the serine/threonine-protein kinase activity.|||Disordered|||Does not affect ability to phosphorylate OXSR1/OSR1.|||Does not affect binding to OXSR1/OSR1.|||Does not affect interaction with EMC2.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Interaction with KLHL3|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||RFXV motif 1|||RFXV motif 2|||RFXV motif 3|||RFXV motif 4|||Serine/threonine-protein kinase WNK1|||Slightly decreased binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1258. Abolished binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1258, A-1946 and A-1958.|||Slightly decreased binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1860. Abolished binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1860, A-1946 and A-1958.|||Slightly decreased binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1946. Abolished binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1258, A-1860 and A-1946.|||Slightly decreased binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1958. Abolished binding to OXSR1/OSR1 and STK39/SPAK; when associated with A-1257, A-1860 and A-1958.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086819|||http://purl.uniprot.org/annotation/VAR_019992|||http://purl.uniprot.org/annotation/VAR_035640|||http://purl.uniprot.org/annotation/VAR_035641|||http://purl.uniprot.org/annotation/VAR_041309|||http://purl.uniprot.org/annotation/VAR_041310|||http://purl.uniprot.org/annotation/VAR_041311|||http://purl.uniprot.org/annotation/VAR_041312|||http://purl.uniprot.org/annotation/VAR_041313|||http://purl.uniprot.org/annotation/VAR_041314|||http://purl.uniprot.org/annotation/VAR_041315|||http://purl.uniprot.org/annotation/VAR_041316|||http://purl.uniprot.org/annotation/VAR_041317|||http://purl.uniprot.org/annotation/VAR_041318|||http://purl.uniprot.org/annotation/VAR_041319|||http://purl.uniprot.org/annotation/VAR_041320|||http://purl.uniprot.org/annotation/VAR_041321|||http://purl.uniprot.org/annotation/VAR_041322|||http://purl.uniprot.org/annotation/VAR_059033|||http://purl.uniprot.org/annotation/VAR_059034|||http://purl.uniprot.org/annotation/VSP_040267|||http://purl.uniprot.org/annotation/VSP_040268|||http://purl.uniprot.org/annotation/VSP_040269|||http://purl.uniprot.org/annotation/VSP_040270|||http://purl.uniprot.org/annotation/VSP_050634|||http://purl.uniprot.org/annotation/VSP_050637|||http://purl.uniprot.org/annotation/VSP_050638|||http://purl.uniprot.org/annotation/VSP_053767
http://togogenome.org/gene/9606:SNX20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z614                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased binding activity to all phospholipids.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PX|||Phosphoserine|||Sorting nexin-20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325820|||http://purl.uniprot.org/annotation/VAR_039927|||http://purl.uniprot.org/annotation/VSP_032425|||http://purl.uniprot.org/annotation/VSP_032426|||http://purl.uniprot.org/annotation/VSP_032427|||http://purl.uniprot.org/annotation/VSP_032428|||http://purl.uniprot.org/annotation/VSP_032429
http://togogenome.org/gene/9606:GSPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCT6|||http://purl.uniprot.org/uniprot/P15170|||http://purl.uniprot.org/uniprot/Q7KZX8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Eukaryotic peptide chain release factor GTP-binding subunit ERF3A|||G1|||G2|||G3|||G4|||G5|||In isoform 2 and isoform 3.|||In isoform 2.|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091480|||http://purl.uniprot.org/annotation/VSP_042198|||http://purl.uniprot.org/annotation/VSP_042199
http://togogenome.org/gene/9606:KLHL33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUB7|||http://purl.uniprot.org/uniprot/A6NCF5|||http://purl.uniprot.org/uniprot/B2RUZ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||BACK|||BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324769|||http://purl.uniprot.org/annotation/VAR_039878|||http://purl.uniprot.org/annotation/VAR_039879|||http://purl.uniprot.org/annotation/VAR_039880|||http://purl.uniprot.org/annotation/VAR_039881
http://togogenome.org/gene/9606:FLOT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QLD9|||http://purl.uniprot.org/uniprot/Q14254|||http://purl.uniprot.org/uniprot/Q6FG43|||http://purl.uniprot.org/uniprot/Q9BTI6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Band 7|||Flotillin-2|||Loss of ZDHHC5-catalyzed palmitoylation; when associated with S-20. Partial loss of ZDHHC5-catalyzed palmitoylation; when associated with S-19. Complete loss of palmitoylation; when associated with S-19 and S-20.|||Loss of ZDHHC5-catalyzed palmitoylation; when associated with S-4. Partial loss of ZDHHC5-catalyzed palmitoylation; when associated with S-19. Complete loss of palmitoylation; when associated with S-4 and S-19.|||N-myristoyl glycine|||Partial loss of ZDHHC5-catalyzed palmitoylation; when associated with S-4 or S-20. Complete loss of palmitoylation; when associated with S-4 and S-20.|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||S-palmitoyl cysteine; by ZDHHC5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094049|||http://purl.uniprot.org/annotation/VAR_024375
http://togogenome.org/gene/9606:PRKACA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TL59|||http://purl.uniprot.org/uniprot/A8K8B9|||http://purl.uniprot.org/uniprot/P17612                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Deamidated asparagine|||Disordered|||Enhanced basal kinase activity; when associated with Q-96, L-121, A-124, K-182 and A-184.|||Enhanced basal kinase activity; when associated with R-48, L-121, A-124, K-182 and A-184.|||Enhanced basal kinase activity; when associated with R-48, Q-96, A-124, K-182 and A-184.|||Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and A-184.|||Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, A-124 and K-182.|||Enhanced basal kinase activity; when associated with R-48, Q-96, L-121, K-182 and A-184.|||In CAFD1; decreased interaction with regulatory subunit PRKAR2B.|||In PPNAD4; somatic mutation; the mutation results in cAMP-independent basal protein kinase activity and constitutive activation of protein kinase A.|||In isoform 2.|||Loss of allosteric regulation.|||N-myristoyl glycine|||No phosphorylation.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Removed|||cAMP-dependent protein kinase catalytic subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086052|||http://purl.uniprot.org/annotation/VAR_040591|||http://purl.uniprot.org/annotation/VAR_040592|||http://purl.uniprot.org/annotation/VAR_040593|||http://purl.uniprot.org/annotation/VAR_071707|||http://purl.uniprot.org/annotation/VAR_085198|||http://purl.uniprot.org/annotation/VSP_004759
http://togogenome.org/gene/9606:JMY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9B5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with p300/EP300|||Junction-mediating and -regulatory protein|||Phosphoserine|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324611|||http://purl.uniprot.org/annotation/VAR_039846|||http://purl.uniprot.org/annotation/VAR_039847|||http://purl.uniprot.org/annotation/VAR_039848|||http://purl.uniprot.org/annotation/VSP_032310
http://togogenome.org/gene/9606:OR2T27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH04                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150505|||http://purl.uniprot.org/annotation/VAR_053158|||http://purl.uniprot.org/annotation/VAR_062030
http://togogenome.org/gene/9606:WDR45B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MNZ6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to phosphoinositides.|||Abolished interaction with ATG2A.|||Does not affect binding to phosphoinositides.|||In NEDSBAS; unknown pathological significance.|||L/FRRG motif|||Loss of PtdIns3P binding.|||Strongly decreased interaction with ATG2A.|||Strongly decreased interaction with ATG2A; when associated with 59-Q--A-62.|||Strongly decreased interaction with ATG2A; when associated with A-125.|||Strongly decreased interaction with ATG2A; when associated with A-65.|||Strongly decreased interaction with ATG2A; when associated with Q-35.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat domain phosphoinositide-interacting protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051445|||http://purl.uniprot.org/annotation/VAR_081110|||http://purl.uniprot.org/annotation/VAR_081111
http://togogenome.org/gene/9606:RASL11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6T310                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region                                                                                  ^@                                                                                  Ras-like protein family member 11A|||Small GTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308360
http://togogenome.org/gene/9606:NPW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N729                                                                                  ^@                                                                                  Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Glycosylation Site|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Neuropeptide W-23|||Neuropeptide W-30|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019843|||http://purl.uniprot.org/annotation/PRO_0000019844|||http://purl.uniprot.org/annotation/PRO_0000019845|||http://purl.uniprot.org/annotation/VAR_050292
http://togogenome.org/gene/9606:CDK2AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75956|||http://purl.uniprot.org/uniprot/Q6IAV4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Cyclin-dependent kinase 2-associated protein 2|||Disordered|||Interaction with CDK2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079963
http://togogenome.org/gene/9606:CYTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00156|||http://purl.uniprot.org/uniprot/Q0ZFD6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to obesity.|||Cytochrome b|||Cytochrome b/b6 C-terminal region profile|||Cytochrome b/b6 N-terminal region profile|||Found in a patient with fatal post-partum cardiomyopathy; unknown pathological significance.|||Helical|||In CMIH.|||In LHON; secondary mutation; does not seem to directly cause the disease.|||In colorectal cancer.|||In exercice intolerance; with cardiomyopathy and septo-optic dysplasia.|||In exercise intolerance.|||In hyperthrophic cardiomyopathy.|||In mitochondrial myopathy.|||In mitochondrial myopathy; sporadic.|||In multisystem disorder.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000061045|||http://purl.uniprot.org/annotation/VAR_002197|||http://purl.uniprot.org/annotation/VAR_002198|||http://purl.uniprot.org/annotation/VAR_002199|||http://purl.uniprot.org/annotation/VAR_008388|||http://purl.uniprot.org/annotation/VAR_008389|||http://purl.uniprot.org/annotation/VAR_008585|||http://purl.uniprot.org/annotation/VAR_008586|||http://purl.uniprot.org/annotation/VAR_011339|||http://purl.uniprot.org/annotation/VAR_011340|||http://purl.uniprot.org/annotation/VAR_011341|||http://purl.uniprot.org/annotation/VAR_013643|||http://purl.uniprot.org/annotation/VAR_013644|||http://purl.uniprot.org/annotation/VAR_013645|||http://purl.uniprot.org/annotation/VAR_013646|||http://purl.uniprot.org/annotation/VAR_013647|||http://purl.uniprot.org/annotation/VAR_013648|||http://purl.uniprot.org/annotation/VAR_013649|||http://purl.uniprot.org/annotation/VAR_013650|||http://purl.uniprot.org/annotation/VAR_013651|||http://purl.uniprot.org/annotation/VAR_013652|||http://purl.uniprot.org/annotation/VAR_013653|||http://purl.uniprot.org/annotation/VAR_013654|||http://purl.uniprot.org/annotation/VAR_013655|||http://purl.uniprot.org/annotation/VAR_013656|||http://purl.uniprot.org/annotation/VAR_013657|||http://purl.uniprot.org/annotation/VAR_013658|||http://purl.uniprot.org/annotation/VAR_013659|||http://purl.uniprot.org/annotation/VAR_013660|||http://purl.uniprot.org/annotation/VAR_013661|||http://purl.uniprot.org/annotation/VAR_013662|||http://purl.uniprot.org/annotation/VAR_013663|||http://purl.uniprot.org/annotation/VAR_013664|||http://purl.uniprot.org/annotation/VAR_013665|||http://purl.uniprot.org/annotation/VAR_013666|||http://purl.uniprot.org/annotation/VAR_013667|||http://purl.uniprot.org/annotation/VAR_013668|||http://purl.uniprot.org/annotation/VAR_015571|||http://purl.uniprot.org/annotation/VAR_015572|||http://purl.uniprot.org/annotation/VAR_015573|||http://purl.uniprot.org/annotation/VAR_033058|||http://purl.uniprot.org/annotation/VAR_033059
http://togogenome.org/gene/9606:TCF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15923                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Basic and acidic residues|||Breakpoint for translocation to form TCF3-PBX1 oncogene|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In AGM8A; localizes normally to the nucleus; does not perform proper DNA binding; acts in a dominant-negative manner when coexpressed with wild-type.|||In AGM8B; decreased protein abundance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform E47.|||Leucine-zipper|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription factor E2-alpha|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127466|||http://purl.uniprot.org/annotation/VAR_036396|||http://purl.uniprot.org/annotation/VAR_049552|||http://purl.uniprot.org/annotation/VAR_049553|||http://purl.uniprot.org/annotation/VAR_049554|||http://purl.uniprot.org/annotation/VAR_082832|||http://purl.uniprot.org/annotation/VAR_087244|||http://purl.uniprot.org/annotation/VSP_002155|||http://purl.uniprot.org/annotation/VSP_057277|||http://purl.uniprot.org/annotation/VSP_057278
http://togogenome.org/gene/9606:RFFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase rififylin|||FYVE-type|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of E3 ubiquitin protein ligase activity.|||Phosphoserine|||Polar residues|||RING-type|||SAP 1|||SAP 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056025|||http://purl.uniprot.org/annotation/VSP_015751|||http://purl.uniprot.org/annotation/VSP_015752
http://togogenome.org/gene/9606:ZNF473                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY71|||http://purl.uniprot.org/uniprot/F8WEC7|||http://purl.uniprot.org/uniprot/Q8WTR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with SLBP/pre-mRNA complex|||KRAB|||Zinc finger protein 473                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047604|||http://purl.uniprot.org/annotation/VAR_052839|||http://purl.uniprot.org/annotation/VAR_052840|||http://purl.uniprot.org/annotation/VAR_052841|||http://purl.uniprot.org/annotation/VAR_052842|||http://purl.uniprot.org/annotation/VAR_052843|||http://purl.uniprot.org/annotation/VAR_052844
http://togogenome.org/gene/9606:GNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCR2|||http://purl.uniprot.org/uniprot/B4DYK6|||http://purl.uniprot.org/uniprot/P36915                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CP-type G|||Disordered|||Guanine nucleotide-binding protein-like 1|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122441|||http://purl.uniprot.org/annotation/VSP_026992|||http://purl.uniprot.org/annotation/VSP_026993
http://togogenome.org/gene/9606:RP1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWN7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-1; approximate|||1-2; approximate|||1-3|||2-1|||2-10|||2-11|||2-12; approximate|||2-13d|||2-14|||2-15; approximate|||2-16|||2-17|||2-18|||2-19|||2-2|||2-20|||2-21|||2-22|||2-23|||2-24|||2-25|||2-3|||2-4; approximate|||2-5|||2-6; approximate|||2-7|||2-8; approximate|||2-9; approximate|||25 X 16 AA approximate tandem repeats of [ED]-[AT]-[PQ]-[ED]-[AVT]-E-[GKE]-[ED]-[AMT]-Q-[EPK]-[EAT]-[TSELP]-[EG]-[EGSQDI]-[AVIE]|||3 X 16 AA approximate tandem repeats of T-E-E-G-L-Q-E-E-G-V-Q-L-E-E-T-K|||Acidic residues|||Basic and acidic residues|||Disordered|||Doublecortin 1|||Doublecortin 2|||In OCMD.|||In OCMD; unknown pathological significance.|||In RP88; unknown pathological significance.|||In allele RP1L1-2 and allele RP1L1-3.|||In allele RP1L1-2.|||In allele RP1L1-3.|||In allele RP1L1-4.|||In allele RP1L1-5.|||In allele RP1L1-6.|||In isoform 2.|||Polar residues|||Pro residues|||Retinitis pigmentosa 1-like 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097406|||http://purl.uniprot.org/annotation/VAR_017700|||http://purl.uniprot.org/annotation/VAR_017701|||http://purl.uniprot.org/annotation/VAR_017702|||http://purl.uniprot.org/annotation/VAR_017703|||http://purl.uniprot.org/annotation/VAR_017704|||http://purl.uniprot.org/annotation/VAR_017705|||http://purl.uniprot.org/annotation/VAR_017706|||http://purl.uniprot.org/annotation/VAR_017707|||http://purl.uniprot.org/annotation/VAR_017708|||http://purl.uniprot.org/annotation/VAR_017709|||http://purl.uniprot.org/annotation/VAR_017710|||http://purl.uniprot.org/annotation/VAR_017712|||http://purl.uniprot.org/annotation/VAR_017713|||http://purl.uniprot.org/annotation/VAR_017715|||http://purl.uniprot.org/annotation/VAR_017721|||http://purl.uniprot.org/annotation/VAR_017722|||http://purl.uniprot.org/annotation/VAR_017723|||http://purl.uniprot.org/annotation/VAR_017724|||http://purl.uniprot.org/annotation/VAR_017725|||http://purl.uniprot.org/annotation/VAR_017726|||http://purl.uniprot.org/annotation/VAR_017727|||http://purl.uniprot.org/annotation/VAR_017728|||http://purl.uniprot.org/annotation/VAR_017729|||http://purl.uniprot.org/annotation/VAR_017730|||http://purl.uniprot.org/annotation/VAR_017731|||http://purl.uniprot.org/annotation/VAR_017732|||http://purl.uniprot.org/annotation/VAR_017733|||http://purl.uniprot.org/annotation/VAR_017734|||http://purl.uniprot.org/annotation/VAR_017735|||http://purl.uniprot.org/annotation/VAR_017736|||http://purl.uniprot.org/annotation/VAR_017737|||http://purl.uniprot.org/annotation/VAR_017738|||http://purl.uniprot.org/annotation/VAR_047388|||http://purl.uniprot.org/annotation/VAR_056979|||http://purl.uniprot.org/annotation/VAR_056981|||http://purl.uniprot.org/annotation/VAR_065126|||http://purl.uniprot.org/annotation/VAR_065127|||http://purl.uniprot.org/annotation/VAR_068350|||http://purl.uniprot.org/annotation/VAR_080211|||http://purl.uniprot.org/annotation/VAR_080212|||http://purl.uniprot.org/annotation/VAR_080213|||http://purl.uniprot.org/annotation/VAR_080214|||http://purl.uniprot.org/annotation/VAR_080215|||http://purl.uniprot.org/annotation/VAR_080216|||http://purl.uniprot.org/annotation/VAR_080217|||http://purl.uniprot.org/annotation/VAR_083926|||http://purl.uniprot.org/annotation/VAR_083927|||http://purl.uniprot.org/annotation/VAR_083928|||http://purl.uniprot.org/annotation/VAR_083929|||http://purl.uniprot.org/annotation/VAR_083930|||http://purl.uniprot.org/annotation/VAR_083931|||http://purl.uniprot.org/annotation/VAR_083932|||http://purl.uniprot.org/annotation/VAR_083933|||http://purl.uniprot.org/annotation/VSP_009382|||http://purl.uniprot.org/annotation/VSP_009383
http://togogenome.org/gene/9606:CREBZF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PIM0|||http://purl.uniprot.org/uniprot/Q9NS37                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BZIP|||Basic motif|||CREB/ATF bZIP transcription factor|||Disordered|||Does not interact with HCFC1 and is inefficient at inhibiting CREB3 transcriptional activity. Does not colocalize with CREB3 in promyelocytic leukemia protein nuclear bodies (PML-NB).|||HCFC1-binding motif (HBM)|||Leucine-zipper|||Phosphoserine|||Polar residues|||Significantly reduced binding to HCFC1.|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076645
http://togogenome.org/gene/9606:MRPS26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYN8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||Small ribosomal subunit protein mS26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030591
http://togogenome.org/gene/9606:PAMR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXE9|||http://purl.uniprot.org/uniprot/B7Z4A8|||http://purl.uniprot.org/uniprot/B7Z6E5|||http://purl.uniprot.org/uniprot/Q6UXH9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CUB|||EGF-like|||In isoform 2.|||In isoform 3.|||Inactive serine protease PAMR1|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287602|||http://purl.uniprot.org/annotation/PRO_5002863973|||http://purl.uniprot.org/annotation/VAR_032335|||http://purl.uniprot.org/annotation/VSP_025568|||http://purl.uniprot.org/annotation/VSP_055371
http://togogenome.org/gene/9606:RFT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AA3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In CDG1N.|||Protein RFT1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311286|||http://purl.uniprot.org/annotation/VAR_037215|||http://purl.uniprot.org/annotation/VAR_044334|||http://purl.uniprot.org/annotation/VAR_062572|||http://purl.uniprot.org/annotation/VAR_062573
http://togogenome.org/gene/9606:LRGUK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M69                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Guanylate kinase-like|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||Leucine-rich repeat and guanylate kinase domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326408|||http://purl.uniprot.org/annotation/VAR_040063|||http://purl.uniprot.org/annotation/VAR_040064
http://togogenome.org/gene/9606:TXNL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P83876                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Phosphoserine|||Thioredoxin-like protein 4A|||Viable when expressed in S.pombe.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218287
http://togogenome.org/gene/9606:APOC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55056                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Apolipoprotein C-IV|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002036|||http://purl.uniprot.org/annotation/VAR_012068|||http://purl.uniprot.org/annotation/VAR_012069|||http://purl.uniprot.org/annotation/VAR_012081|||http://purl.uniprot.org/annotation/VAR_012082|||http://purl.uniprot.org/annotation/VAR_036540
http://togogenome.org/gene/9606:SLC16A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTY1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Monocarboxylate transporter 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289332|||http://purl.uniprot.org/annotation/VAR_032619|||http://purl.uniprot.org/annotation/VAR_032620|||http://purl.uniprot.org/annotation/VAR_062149
http://togogenome.org/gene/9606:BIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBW5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes dimerization and membrane binding; when associated with E-214.|||Abolishes dimerization and membrane binding; when associated with R-81.|||Acidic residues|||BAR|||Basic and acidic residues|||Bridging integrator 2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly reduces binding to membranes.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256140|||http://purl.uniprot.org/annotation/VAR_028883|||http://purl.uniprot.org/annotation/VAR_028884|||http://purl.uniprot.org/annotation/VSP_021328|||http://purl.uniprot.org/annotation/VSP_059731
http://togogenome.org/gene/9606:ROGDI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased protein stability.|||In KTZS.|||In KTZS; unknown pathological significance.|||N-acetylalanine|||Protein rogdi homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315664|||http://purl.uniprot.org/annotation/VAR_038273|||http://purl.uniprot.org/annotation/VAR_084016|||http://purl.uniprot.org/annotation/VAR_084017|||http://purl.uniprot.org/annotation/VAR_084018
http://togogenome.org/gene/9606:POT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTK3|||http://purl.uniprot.org/uniprot/Q9NUX5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-binding|||In CMM10.|||In CMM10; complete abolition of POT1-DNA complex formation, thus disrupting the interaction with telomeres and leading to elongated telomeres.|||In CMM10; increased telomere intensity signals and telomere fragility.|||In CMM10; significantly increased telomere length and numbers of fragile telomeres.|||In GLM9.|||In isoform 2.|||Protection of telomeres protein 1|||Protection of telomeres protein 1 ssDNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121728|||http://purl.uniprot.org/annotation/VAR_034393|||http://purl.uniprot.org/annotation/VAR_071390|||http://purl.uniprot.org/annotation/VAR_071391|||http://purl.uniprot.org/annotation/VAR_071392|||http://purl.uniprot.org/annotation/VAR_071393|||http://purl.uniprot.org/annotation/VAR_071394|||http://purl.uniprot.org/annotation/VAR_071395|||http://purl.uniprot.org/annotation/VAR_071396|||http://purl.uniprot.org/annotation/VAR_071397|||http://purl.uniprot.org/annotation/VAR_075717|||http://purl.uniprot.org/annotation/VSP_010846|||http://purl.uniprot.org/annotation/VSP_010847
http://togogenome.org/gene/9606:MRGPRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member F|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069764|||http://purl.uniprot.org/annotation/VAR_061220
http://togogenome.org/gene/9606:TLR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4S4|||http://purl.uniprot.org/uniprot/B3KWR9|||http://purl.uniprot.org/uniprot/O60603                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ATG16L1-binding motif|||Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain.|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interaction with bacterial lipopeptide|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||Loss of PPP1R11-mediated ubiquitination and degradation.|||N-linked (GlcNAc...) asparagine|||Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain.|||Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain.|||Reduced protein stability.|||Reduces TLR2-mediated NF-kappa-B activation.|||TIR|||Toll-like receptor|||Toll-like receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034710|||http://purl.uniprot.org/annotation/PRO_5011019880|||http://purl.uniprot.org/annotation/PRO_5011021330|||http://purl.uniprot.org/annotation/VAR_024663|||http://purl.uniprot.org/annotation/VAR_026765|||http://purl.uniprot.org/annotation/VAR_026766|||http://purl.uniprot.org/annotation/VAR_031236|||http://purl.uniprot.org/annotation/VAR_031237|||http://purl.uniprot.org/annotation/VAR_052360|||http://purl.uniprot.org/annotation/VAR_066349|||http://purl.uniprot.org/annotation/VAR_066350|||http://purl.uniprot.org/annotation/VAR_066351
http://togogenome.org/gene/9606:IL9R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01113                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3.|||Interleukin-9 receptor|||N-linked (GlcNAc...) asparagine|||Polar residues|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010911|||http://purl.uniprot.org/annotation/VAR_014804|||http://purl.uniprot.org/annotation/VAR_033920|||http://purl.uniprot.org/annotation/VAR_038784|||http://purl.uniprot.org/annotation/VAR_055348|||http://purl.uniprot.org/annotation/VAR_055349|||http://purl.uniprot.org/annotation/VSP_039025|||http://purl.uniprot.org/annotation/VSP_046207|||http://purl.uniprot.org/annotation/VSP_046208|||http://purl.uniprot.org/annotation/VSP_046209|||http://purl.uniprot.org/annotation/VSP_046210
http://togogenome.org/gene/9606:DPM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4Y5|||http://purl.uniprot.org/uniprot/H0Y368|||http://purl.uniprot.org/uniprot/O60762|||http://purl.uniprot.org/uniprot/Q5QPK2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Dolichol-phosphate mannosyltransferase subunit 1|||Glycosyltransferase 2-like|||In CDG1E.|||In CDG1E; abolishes interaction with DPM3.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059170|||http://purl.uniprot.org/annotation/VAR_012341|||http://purl.uniprot.org/annotation/VAR_019841|||http://purl.uniprot.org/annotation/VAR_070592
http://togogenome.org/gene/9606:ZFYVE19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K21                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to phosphatidylinositol-3-phosphate (PtdIns(3)P) without affecting localization to the midbody.|||Abscission/NoCut checkpoint regulator|||Breakpoint for translocation to form KMT2A/MLL1-ZFYVE19|||Disordered|||FYVE-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In PFIC9.|||In PFIC9; several lines of evidence suggest that M-76 may be the main initiator, a variant at this location would therefore disrupt translation initiation.|||In PFIC9; undetectable protein levels in the liver of a homozygous patient.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MIM1-A|||MIM1-B|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098718|||http://purl.uniprot.org/annotation/VAR_057494|||http://purl.uniprot.org/annotation/VAR_060474|||http://purl.uniprot.org/annotation/VAR_060475|||http://purl.uniprot.org/annotation/VAR_087108|||http://purl.uniprot.org/annotation/VAR_087109|||http://purl.uniprot.org/annotation/VAR_087110|||http://purl.uniprot.org/annotation/VAR_087111|||http://purl.uniprot.org/annotation/VAR_087112|||http://purl.uniprot.org/annotation/VAR_087113|||http://purl.uniprot.org/annotation/VSP_013791|||http://purl.uniprot.org/annotation/VSP_013792|||http://purl.uniprot.org/annotation/VSP_046008
http://togogenome.org/gene/9606:BUB1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60566                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes the cleavage by caspase-3.|||BUB1 N-terminal|||Cleavage; by caspase-3|||D-box|||Disordered|||Does not abolish the capacity to inhibit APC/CDC20.|||In MVA1; associated with F-844; heterozygous compound with nonsense mutation.|||In MVA1; associated with H-921; heterozygous compound with nonsense mutation.|||In MVA1; heterozygous compound with nonsense mutation.|||In PCS.|||In a colorectal cancer cell line.|||In isoform 2.|||In isoform 3.|||Induces chromosome congression defects and mitotic delay.|||Inhibits kinase activity.|||Loss of interaction with KNL1.|||Mitotic checkpoint serine/threonine-protein kinase BUB1 beta|||N6-acetyllysine; by PCAF|||Necessary for interaction with KNL1|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by PLK1|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085673|||http://purl.uniprot.org/annotation/VAR_008852|||http://purl.uniprot.org/annotation/VAR_008853|||http://purl.uniprot.org/annotation/VAR_008854|||http://purl.uniprot.org/annotation/VAR_028921|||http://purl.uniprot.org/annotation/VAR_028922|||http://purl.uniprot.org/annotation/VAR_028923|||http://purl.uniprot.org/annotation/VAR_028924|||http://purl.uniprot.org/annotation/VAR_028925|||http://purl.uniprot.org/annotation/VAR_028926|||http://purl.uniprot.org/annotation/VAR_028927|||http://purl.uniprot.org/annotation/VAR_028928|||http://purl.uniprot.org/annotation/VAR_040402|||http://purl.uniprot.org/annotation/VAR_054549|||http://purl.uniprot.org/annotation/VSP_036473|||http://purl.uniprot.org/annotation/VSP_036474|||http://purl.uniprot.org/annotation/VSP_036475|||http://purl.uniprot.org/annotation/VSP_036476
http://togogenome.org/gene/9606:SRI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHQ6|||http://purl.uniprot.org/uniprot/P30626                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||In isoform 2 and isoform 3.|||In isoform 3.|||Reduces affinity for calcium 5-fold.|||Sorcin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073725|||http://purl.uniprot.org/annotation/VSP_046277|||http://purl.uniprot.org/annotation/VSP_054463
http://togogenome.org/gene/9606:ARMCX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P291                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||Armadillo repeat-containing X-linked protein 1|||Cytoplasmic|||Disordered|||Helical; Signal-anchor|||Mitochondrial intermembrane|||Mitochondrion outer membrane (MOM)-targeting sequence                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191360
http://togogenome.org/gene/9606:HELLS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSW7|||http://purl.uniprot.org/uniprot/A0A0B4J1V9|||http://purl.uniprot.org/uniprot/Q0VGL2|||http://purl.uniprot.org/uniprot/Q76H82|||http://purl.uniprot.org/uniprot/Q9NRZ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAH box|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Helicase ATP-binding|||Helicase C-terminal|||In ICF4; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Lymphoid-specific helicase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260051|||http://purl.uniprot.org/annotation/VAR_064720|||http://purl.uniprot.org/annotation/VAR_076582|||http://purl.uniprot.org/annotation/VAR_076583|||http://purl.uniprot.org/annotation/VSP_052224|||http://purl.uniprot.org/annotation/VSP_052225|||http://purl.uniprot.org/annotation/VSP_052226|||http://purl.uniprot.org/annotation/VSP_052227|||http://purl.uniprot.org/annotation/VSP_052228|||http://purl.uniprot.org/annotation/VSP_052229|||http://purl.uniprot.org/annotation/VSP_052230|||http://purl.uniprot.org/annotation/VSP_052231|||http://purl.uniprot.org/annotation/VSP_052232|||http://purl.uniprot.org/annotation/VSP_052233|||http://purl.uniprot.org/annotation/VSP_052234
http://togogenome.org/gene/9606:TMEM54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969K7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Transmembrane protein 54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226989|||http://purl.uniprot.org/annotation/VAR_052342|||http://purl.uniprot.org/annotation/VSP_017532|||http://purl.uniprot.org/annotation/VSP_017533
http://togogenome.org/gene/9606:ELP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE02                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Elongator complex protein 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280817|||http://purl.uniprot.org/annotation/VAR_031205|||http://purl.uniprot.org/annotation/VAR_053882|||http://purl.uniprot.org/annotation/VSP_023920|||http://purl.uniprot.org/annotation/VSP_023921|||http://purl.uniprot.org/annotation/VSP_023922|||http://purl.uniprot.org/annotation/VSP_023923
http://togogenome.org/gene/9606:DRAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX65                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  DNA damage-regulated autophagy modulator protein 2|||Helical|||In CORD21.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254102|||http://purl.uniprot.org/annotation/VAR_075073|||http://purl.uniprot.org/annotation/VAR_075074|||http://purl.uniprot.org/annotation/VAR_075075|||http://purl.uniprot.org/annotation/VAR_075076|||http://purl.uniprot.org/annotation/VAR_075077
http://togogenome.org/gene/9606:LDHAL6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMR3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||L-lactate dehydrogenase A-like 6A|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168457
http://togogenome.org/gene/9606:RIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSK7|||http://purl.uniprot.org/uniprot/Q6ZRC2|||http://purl.uniprot.org/uniprot/Q86U22|||http://purl.uniprot.org/uniprot/Q8TB24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 4.|||Interaction with RAB5B|||Polar residues|||Pro residues|||Ras and Rab interactor 3|||Ras-associating|||SH2|||Strongly reduced guanine nucleotide exchange factor activity toward RAB31; when associated with A-825.|||Strongly reduced guanine nucleotide exchange factor activity toward RAB31; when associated with A-828.|||VPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191322|||http://purl.uniprot.org/annotation/VAR_046645|||http://purl.uniprot.org/annotation/VAR_046646|||http://purl.uniprot.org/annotation/VAR_046647|||http://purl.uniprot.org/annotation/VAR_046648|||http://purl.uniprot.org/annotation/VAR_052946|||http://purl.uniprot.org/annotation/VAR_059960|||http://purl.uniprot.org/annotation/VAR_059961|||http://purl.uniprot.org/annotation/VSP_007587|||http://purl.uniprot.org/annotation/VSP_007588
http://togogenome.org/gene/9606:FSCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK18|||http://purl.uniprot.org/uniprot/Q9NQT6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Fascin|||Fascin-3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219383|||http://purl.uniprot.org/annotation/VAR_022021|||http://purl.uniprot.org/annotation/VAR_033939|||http://purl.uniprot.org/annotation/VSP_057001|||http://purl.uniprot.org/annotation/VSP_057002|||http://purl.uniprot.org/annotation/VSP_057003
http://togogenome.org/gene/9606:JAKMIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UIU4|||http://purl.uniprot.org/uniprot/A0A590UJH1|||http://purl.uniprot.org/uniprot/A0A590UJT1|||http://purl.uniprot.org/uniprot/Q5VZ66                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||Janus kinase and microtubule-interacting protein 3|||Janus kinase and microtubule-interacting protein C-terminal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323011|||http://purl.uniprot.org/annotation/VAR_039473|||http://purl.uniprot.org/annotation/VAR_054016
http://togogenome.org/gene/9606:SLC18A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05940                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In PKDYS2; strong decrease in serotonin transport.|||In isoform 2.|||Lumenal, vesicle|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Synaptic vesicular amine transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127514|||http://purl.uniprot.org/annotation/VAR_081069|||http://purl.uniprot.org/annotation/VSP_057151|||http://purl.uniprot.org/annotation/VSP_057152
http://togogenome.org/gene/9606:FOSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z595|||http://purl.uniprot.org/uniprot/E9PKL5|||http://purl.uniprot.org/uniprot/E9PPX2|||http://purl.uniprot.org/uniprot/P15407                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  BZIP|||Basic and acidic residues|||Basic motif|||Disordered|||Fos-related antigen 1|||In isoform 2.|||Leucine-zipper|||Phosphoserine|||Polar residues|||Pro residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076479|||http://purl.uniprot.org/annotation/VSP_055566
http://togogenome.org/gene/9606:CHID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWS9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chitinase domain-containing protein 1|||GH18|||In isoform 2.|||In isoform 3.|||No noticeable effect.|||Significantly decreased carbohydrate binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280608|||http://purl.uniprot.org/annotation/VAR_031173|||http://purl.uniprot.org/annotation/VAR_031174|||http://purl.uniprot.org/annotation/VSP_023825|||http://purl.uniprot.org/annotation/VSP_023826
http://togogenome.org/gene/9606:TLE5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08117|||http://purl.uniprot.org/uniprot/Q8WY48                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CCN domain|||Disordered|||In isoform 2.|||Phosphoserine|||TLE family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050834|||http://purl.uniprot.org/annotation/VAR_011958|||http://purl.uniprot.org/annotation/VSP_043527
http://togogenome.org/gene/9606:RPGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92834                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with RPGRIP1.|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Does not reduce interaction with PDE6D.|||In RP3 and RPSRDF.|||In RP3.|||In RP3; benign variant.|||In RP3; impairs protein folding.|||In RP3; reduces interaction with PDE6D.|||In RP3; unknown pathological significance.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||Removed in mature form|||S-geranylgeranyl cysteine|||X-linked retinitis pigmentosa GTPase regulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206638|||http://purl.uniprot.org/annotation/PRO_0000370844|||http://purl.uniprot.org/annotation/VAR_006850|||http://purl.uniprot.org/annotation/VAR_006851|||http://purl.uniprot.org/annotation/VAR_006852|||http://purl.uniprot.org/annotation/VAR_008501|||http://purl.uniprot.org/annotation/VAR_008503|||http://purl.uniprot.org/annotation/VAR_008504|||http://purl.uniprot.org/annotation/VAR_008505|||http://purl.uniprot.org/annotation/VAR_008506|||http://purl.uniprot.org/annotation/VAR_008507|||http://purl.uniprot.org/annotation/VAR_008508|||http://purl.uniprot.org/annotation/VAR_008509|||http://purl.uniprot.org/annotation/VAR_008510|||http://purl.uniprot.org/annotation/VAR_008511|||http://purl.uniprot.org/annotation/VAR_011561|||http://purl.uniprot.org/annotation/VAR_011562|||http://purl.uniprot.org/annotation/VAR_011563|||http://purl.uniprot.org/annotation/VAR_013624|||http://purl.uniprot.org/annotation/VAR_013625|||http://purl.uniprot.org/annotation/VAR_013626|||http://purl.uniprot.org/annotation/VAR_013627|||http://purl.uniprot.org/annotation/VAR_018057|||http://purl.uniprot.org/annotation/VAR_018058|||http://purl.uniprot.org/annotation/VAR_018059|||http://purl.uniprot.org/annotation/VAR_018060|||http://purl.uniprot.org/annotation/VAR_018061|||http://purl.uniprot.org/annotation/VAR_018062|||http://purl.uniprot.org/annotation/VAR_018063|||http://purl.uniprot.org/annotation/VAR_018064|||http://purl.uniprot.org/annotation/VAR_018065|||http://purl.uniprot.org/annotation/VAR_018066|||http://purl.uniprot.org/annotation/VAR_018067|||http://purl.uniprot.org/annotation/VAR_018068|||http://purl.uniprot.org/annotation/VAR_025949|||http://purl.uniprot.org/annotation/VAR_026127|||http://purl.uniprot.org/annotation/VAR_026128|||http://purl.uniprot.org/annotation/VAR_033259|||http://purl.uniprot.org/annotation/VSP_005547|||http://purl.uniprot.org/annotation/VSP_005548|||http://purl.uniprot.org/annotation/VSP_005549|||http://purl.uniprot.org/annotation/VSP_005550|||http://purl.uniprot.org/annotation/VSP_009183|||http://purl.uniprot.org/annotation/VSP_009184|||http://purl.uniprot.org/annotation/VSP_044559
http://togogenome.org/gene/9606:AMPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49418                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Amphiphysin|||BAR|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192947|||http://purl.uniprot.org/annotation/VAR_053004|||http://purl.uniprot.org/annotation/VAR_053005|||http://purl.uniprot.org/annotation/VAR_053006|||http://purl.uniprot.org/annotation/VSP_000245
http://togogenome.org/gene/9606:EIF3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99613                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Eukaryotic translation initiation factor 3 subunit C|||In isoform 2.|||N6-acetyllysine|||PCI|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123525|||http://purl.uniprot.org/annotation/VSP_055472
http://togogenome.org/gene/9606:UBR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N806                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In LICAS; no UBR7 protein detected in patient cells.|||In LICAS; unknown pathological significance.|||PHD-type; atypical|||Phosphoserine|||Putative E3 ubiquitin-protein ligase UBR7|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089932|||http://purl.uniprot.org/annotation/VAR_085255|||http://purl.uniprot.org/annotation/VAR_085256
http://togogenome.org/gene/9606:GSDMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57764                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished ability to form a pore.|||Abolished ability to induce pyroptosis.|||Abolished cleavage by enterovirus 71 (EV71) Protease 3C and human coronavirus SARS-CoV-2 3C-like proteinase nsp5.|||Abolished generation of the Gasdermin-D, p40 chain and ability to promote secretion of IL33.|||Abolished ubiquitination by S.flexneri IpaH7.8.|||Beta stranded|||Cleavage; by CASP3 or CASP7|||Cleavage; by caspases CASP1, CASP4, CASP5 and CASP8|||Cleavage; by enterovirus 71 (EV71) Protease 3C and coronavirus SARS-CoV-2 proteinase nsp5|||Cleavage; by papain|||Constitutively active mutant; promotes activation of pyroptosis.|||Decreased effectiveness in pore formation and pyroptosis induction. No effect on cleavage by CASP1.|||Decreased induction of pyroptosis and defects in liposome-binding. No spontaneous pyroptosis-inducing activity; when associated with K-15.|||Does not affect ability to induce pyroptosis.|||Does not affect cleavage by enterovirus 71 (EV71) Protease 3C.|||Does not affect interaction with CASP4.|||Gasdermin-D|||Gasdermin-D, C-terminal|||Gasdermin-D, N-terminal|||Gasdermin-D, p13|||Gasdermin-D, p40|||Impaired pore-formation.|||Impairs interaction with CASP1 and CASP4 and subsequent cleavage.|||In AP1; promotes ability to release of interleukin-1 (IL1B and IL18) precursors.|||In AP2; promotes ability to release of interleukin-1 (IL1B and IL18) precursors.|||Linker helix loop|||Loss of cleavage by CASP1 and CASP4 and of LPS-induced pyroptosis. Does not affect interaction with CASP1 and CASP4.|||No effect.|||No spontaneous pyroptosis-inducing activity; when associated with D-192.|||Phosphoserine|||Phosphotyrosine|||Reduced ability to form a pore.|||S-(2-succinyl)cysteine|||Spontaneous pyroptosis-inducing activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148175|||http://purl.uniprot.org/annotation/PRO_0000437526|||http://purl.uniprot.org/annotation/PRO_0000437527|||http://purl.uniprot.org/annotation/PRO_0000459017|||http://purl.uniprot.org/annotation/PRO_0000459018
http://togogenome.org/gene/9606:CYLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXC8|||http://purl.uniprot.org/uniprot/P35663|||http://purl.uniprot.org/uniprot/Q6PEK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||8 X approximate tandem repeats|||Basic and acidic residues|||Cylicin N-terminal|||Cylicin-1|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079753|||http://purl.uniprot.org/annotation/VAR_050937
http://togogenome.org/gene/9606:OASL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15646                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2'-5'-oligoadenylate synthase-like protein|||In isoform 3.|||In isoform p30.|||N-acetylalanine|||Removed|||Ubiquitin-like 1|||Ubiquitin-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160266|||http://purl.uniprot.org/annotation/VAR_053544|||http://purl.uniprot.org/annotation/VSP_003743|||http://purl.uniprot.org/annotation/VSP_003744|||http://purl.uniprot.org/annotation/VSP_046572
http://togogenome.org/gene/9606:CLCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQC9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated chloride channel regulator 2|||Calcium-activated chloride channel regulator 2, 109 kDa form|||Calcium-activated chloride channel regulator 2, 35 kDa form|||Cleavage; by autolysis|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||No change in size.|||Reduction in size by around 2 kDa.|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333694|||http://purl.uniprot.org/annotation/PRO_0000333695|||http://purl.uniprot.org/annotation/PRO_0000344502|||http://purl.uniprot.org/annotation/VAR_043148|||http://purl.uniprot.org/annotation/VAR_043149|||http://purl.uniprot.org/annotation/VAR_054057|||http://purl.uniprot.org/annotation/VAR_054058
http://togogenome.org/gene/9606:OR52A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKL2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150765
http://togogenome.org/gene/9606:ZNF546                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVL3|||http://purl.uniprot.org/uniprot/M0QY24|||http://purl.uniprot.org/uniprot/Q86UE3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||KRAB|||Zinc finger protein 546                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234582|||http://purl.uniprot.org/annotation/VAR_035587|||http://purl.uniprot.org/annotation/VAR_055271|||http://purl.uniprot.org/annotation/VAR_055272|||http://purl.uniprot.org/annotation/VAR_055273|||http://purl.uniprot.org/annotation/VAR_055274|||http://purl.uniprot.org/annotation/VAR_055275|||http://purl.uniprot.org/annotation/VAR_055276|||http://purl.uniprot.org/annotation/VAR_055277
http://togogenome.org/gene/9606:PEX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13608                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In A1 mutant; abolished ATP-binding; decreased interaction with PEX1 or PEX26.|||In A2 mutant; abolished ATP-binding; decreased interaction with PEX1 or PEX26.|||In B1 mutant; abolished ATP hydrolysis; does not affect interaction with PEX6 or PEX26.|||In B2 mutant; does not affect interaction with PEX6 or PEX26.|||In HMLR2.|||In HMLR2; results in mild functional decrease in peroxisome biogenesis.|||In HMLR2; results in severe functional decrease in peroxisome biogenesis.|||In HMLR2; unknown pathological significance.|||In HMLR2; unknown pathological significance; results in mild functional decrease in peroxisome biogenesis.|||In PBD-CG4.|||In PBD-CG4; disease phenotype includes hearing loss, visual impairment, enamel dysplasia microcephaly with deep white matter changes and developmental delay.|||In PBD4A.|||In PBD4A; atypical.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Peroxisomal ATPase PEX6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084607|||http://purl.uniprot.org/annotation/VAR_007918|||http://purl.uniprot.org/annotation/VAR_007919|||http://purl.uniprot.org/annotation/VAR_048114|||http://purl.uniprot.org/annotation/VAR_048115|||http://purl.uniprot.org/annotation/VAR_048116|||http://purl.uniprot.org/annotation/VAR_058381|||http://purl.uniprot.org/annotation/VAR_058382|||http://purl.uniprot.org/annotation/VAR_058383|||http://purl.uniprot.org/annotation/VAR_058384|||http://purl.uniprot.org/annotation/VAR_058385|||http://purl.uniprot.org/annotation/VAR_058386|||http://purl.uniprot.org/annotation/VAR_058387|||http://purl.uniprot.org/annotation/VAR_074110|||http://purl.uniprot.org/annotation/VAR_075872|||http://purl.uniprot.org/annotation/VAR_077505|||http://purl.uniprot.org/annotation/VAR_077506|||http://purl.uniprot.org/annotation/VAR_077507|||http://purl.uniprot.org/annotation/VAR_077508|||http://purl.uniprot.org/annotation/VAR_077509|||http://purl.uniprot.org/annotation/VAR_077510|||http://purl.uniprot.org/annotation/VSP_057137|||http://purl.uniprot.org/annotation/VSP_057138|||http://purl.uniprot.org/annotation/VSP_057139
http://togogenome.org/gene/9606:SYNPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3V7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||PPxY motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Synaptopodin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187670|||http://purl.uniprot.org/annotation/VSP_010476|||http://purl.uniprot.org/annotation/VSP_010477
http://togogenome.org/gene/9606:SELENOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GYA4|||http://purl.uniprot.org/uniprot/Q9BQE4                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue|||Region|||Secondary Structure|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non standard residue|||Region|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Selenocysteine|||Selenoprotein S|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097672
http://togogenome.org/gene/9606:GPR152                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0I9RJ67|||http://purl.uniprot.org/uniprot/Q8TDT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Polar residues|||Probable G-protein coupled receptor 152                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069635|||http://purl.uniprot.org/annotation/VAR_059323
http://togogenome.org/gene/9606:MR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q95460                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Able to activate mouse MAIT cells (xeno-reactivity).|||Alpha-1|||Alpha-2|||Alpha-3|||Antigen-binding cleft|||Associates with B2M and translocates to plasma membrane in the absence of 6-FP. Impairs recognition by pan-cancer TCR, MC.7.G5.|||Connecting peptide|||Cytoplasmic|||Extracellular|||Fails to refold in the presence of 6-FP. Impairs the association with B2M and translocation to the plasma membrane.|||Helical|||Ig-like C1-type|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Major histocompatibility complex class I-related gene protein|||N-linked (GlcNAc...) asparagine|||No effect on cell surface expression.|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344441|||http://purl.uniprot.org/annotation/VAR_045608|||http://purl.uniprot.org/annotation/VAR_045609|||http://purl.uniprot.org/annotation/VAR_045610|||http://purl.uniprot.org/annotation/VSP_034755|||http://purl.uniprot.org/annotation/VSP_034756|||http://purl.uniprot.org/annotation/VSP_034757|||http://purl.uniprot.org/annotation/VSP_034758|||http://purl.uniprot.org/annotation/VSP_043479
http://togogenome.org/gene/9606:LRRC37A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NM11|||http://purl.uniprot.org/uniprot/Q5YKG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRC37A/B like protein 1 C-terminal|||Leucine-rich repeat-containing protein 37A2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337080|||http://purl.uniprot.org/annotation/VAR_070799|||http://purl.uniprot.org/annotation/VAR_070800|||http://purl.uniprot.org/annotation/VAR_070801|||http://purl.uniprot.org/annotation/VAR_070802
http://togogenome.org/gene/9606:C19orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZP8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Immortalization up-regulated protein|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084191|||http://purl.uniprot.org/annotation/VSP_007919
http://togogenome.org/gene/9606:GIMAP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8ND71                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  AIG1-type G 1|||AIG1-type G 2|||AIG1-type G 3|||Disordered|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341970|||http://purl.uniprot.org/annotation/VAR_044129
http://togogenome.org/gene/9606:SNX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KQS5|||http://purl.uniprot.org/uniprot/Q9NRS6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MIT|||Omega-N-methylarginine|||PX|||Phosphoserine|||Sorting nexin-15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213862|||http://purl.uniprot.org/annotation/VAR_052478|||http://purl.uniprot.org/annotation/VSP_006193
http://togogenome.org/gene/9606:CHN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0TVW3|||http://purl.uniprot.org/uniprot/A0A994J7L4|||http://purl.uniprot.org/uniprot/B3VCF4|||http://purl.uniprot.org/uniprot/B3VCF5|||http://purl.uniprot.org/uniprot/B3VCF6|||http://purl.uniprot.org/uniprot/B3VCF9|||http://purl.uniprot.org/uniprot/B7Z1V0|||http://purl.uniprot.org/uniprot/B7Z1W9|||http://purl.uniprot.org/uniprot/B7Z215|||http://purl.uniprot.org/uniprot/P52757                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Beta-chimaerin|||Disordered|||In isoform 3, isoform 5 and isoform 7.|||In isoform 4 and isoform 6.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||In isoform Beta-3.|||Phorbol-ester/DAG-type|||Polar residues|||Rho-GAP|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056697|||http://purl.uniprot.org/annotation/VAR_022118|||http://purl.uniprot.org/annotation/VAR_049136|||http://purl.uniprot.org/annotation/VSP_046271|||http://purl.uniprot.org/annotation/VSP_046272|||http://purl.uniprot.org/annotation/VSP_047600|||http://purl.uniprot.org/annotation/VSP_047601|||http://purl.uniprot.org/annotation/VSP_047602|||http://purl.uniprot.org/annotation/VSP_047603|||http://purl.uniprot.org/annotation/VSP_053323|||http://purl.uniprot.org/annotation/VSP_053679
http://togogenome.org/gene/9606:TMPRSS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z458|||http://purl.uniprot.org/uniprot/B7Z8X1|||http://purl.uniprot.org/uniprot/B7Z900|||http://purl.uniprot.org/uniprot/Q9NRS4                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes protease activity.|||Charge relay system|||Cleavage|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||LDL-receptor class A|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SRCR|||Transmembrane protease serine 4|||Transmembrane protease serine 4 catalytic chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088692|||http://purl.uniprot.org/annotation/PRO_0000451627|||http://purl.uniprot.org/annotation/VAR_024293|||http://purl.uniprot.org/annotation/VAR_046505|||http://purl.uniprot.org/annotation/VAR_046506|||http://purl.uniprot.org/annotation/VSP_013116|||http://purl.uniprot.org/annotation/VSP_013117|||http://purl.uniprot.org/annotation/VSP_054229
http://togogenome.org/gene/9606:EIF2AK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2K8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Histidyl-tRNA synthetase-like|||In PVOD2.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||RWD|||eIF-2-alpha kinase GCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085947|||http://purl.uniprot.org/annotation/VAR_040479|||http://purl.uniprot.org/annotation/VAR_040480|||http://purl.uniprot.org/annotation/VAR_040481|||http://purl.uniprot.org/annotation/VAR_040482|||http://purl.uniprot.org/annotation/VAR_040483|||http://purl.uniprot.org/annotation/VAR_040484|||http://purl.uniprot.org/annotation/VAR_040485|||http://purl.uniprot.org/annotation/VAR_040486|||http://purl.uniprot.org/annotation/VAR_040487|||http://purl.uniprot.org/annotation/VAR_070990|||http://purl.uniprot.org/annotation/VAR_070991|||http://purl.uniprot.org/annotation/VSP_013038|||http://purl.uniprot.org/annotation/VSP_039185|||http://purl.uniprot.org/annotation/VSP_039186
http://togogenome.org/gene/9606:CACNA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW63|||http://purl.uniprot.org/uniprot/B5TYJ1|||http://purl.uniprot.org/uniprot/O00555|||http://purl.uniprot.org/uniprot/Q9NS89                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Also found in patients with global developmental delay and congenital ataxia; gain of function observed in the Drosophila homolog.|||Basic and acidic residues|||Basic residues|||Binding to the beta subunit|||Binds to omega-Aga-IVA|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with late onset progressive myoclonus epilepsy; unknown pathological significance.|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In DEE42.|||In EA2 and SCA6.|||In EA2.|||In EA2; changed high voltage-gated calcium channel activity.|||In EA2; decreased voltage-gated calcium channel activity; reduces P/Q current densities.|||In EA2; loss of voltage-gated calcium channel activity.|||In FHM1 and EA2.|||In FHM1 and SCA6.|||In FHM1.|||In FHM1; increased high voltage-gated calcium channel activity.|||In FHM1; with progressive cerebellar ataxia.|||In SCA6.|||In SCA6; also found in patients with global developmental delay and congenital ataxia; loss of function observed in the Drosophila homolog.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Voltage-dependent P/Q-type calcium channel subunit alpha-1A|||Voltage-dependent calcium channel alpha-1 subunit IQ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053916|||http://purl.uniprot.org/annotation/VAR_001491|||http://purl.uniprot.org/annotation/VAR_001492|||http://purl.uniprot.org/annotation/VAR_001493|||http://purl.uniprot.org/annotation/VAR_001494|||http://purl.uniprot.org/annotation/VAR_014456|||http://purl.uniprot.org/annotation/VAR_014458|||http://purl.uniprot.org/annotation/VAR_014459|||http://purl.uniprot.org/annotation/VAR_014461|||http://purl.uniprot.org/annotation/VAR_014462|||http://purl.uniprot.org/annotation/VAR_014463|||http://purl.uniprot.org/annotation/VAR_043820|||http://purl.uniprot.org/annotation/VAR_043821|||http://purl.uniprot.org/annotation/VAR_043822|||http://purl.uniprot.org/annotation/VAR_043823|||http://purl.uniprot.org/annotation/VAR_043824|||http://purl.uniprot.org/annotation/VAR_043825|||http://purl.uniprot.org/annotation/VAR_043826|||http://purl.uniprot.org/annotation/VAR_043827|||http://purl.uniprot.org/annotation/VAR_043828|||http://purl.uniprot.org/annotation/VAR_043829|||http://purl.uniprot.org/annotation/VAR_043830|||http://purl.uniprot.org/annotation/VAR_043831|||http://purl.uniprot.org/annotation/VAR_043832|||http://purl.uniprot.org/annotation/VAR_043833|||http://purl.uniprot.org/annotation/VAR_043834|||http://purl.uniprot.org/annotation/VAR_043835|||http://purl.uniprot.org/annotation/VAR_043836|||http://purl.uniprot.org/annotation/VAR_043837|||http://purl.uniprot.org/annotation/VAR_043838|||http://purl.uniprot.org/annotation/VAR_043839|||http://purl.uniprot.org/annotation/VAR_043840|||http://purl.uniprot.org/annotation/VAR_043841|||http://purl.uniprot.org/annotation/VAR_043842|||http://purl.uniprot.org/annotation/VAR_059221|||http://purl.uniprot.org/annotation/VAR_059222|||http://purl.uniprot.org/annotation/VAR_063683|||http://purl.uniprot.org/annotation/VAR_063684|||http://purl.uniprot.org/annotation/VAR_063685|||http://purl.uniprot.org/annotation/VAR_063686|||http://purl.uniprot.org/annotation/VAR_063687|||http://purl.uniprot.org/annotation/VAR_063688|||http://purl.uniprot.org/annotation/VAR_063689|||http://purl.uniprot.org/annotation/VAR_063690|||http://purl.uniprot.org/annotation/VAR_063691|||http://purl.uniprot.org/annotation/VAR_063692|||http://purl.uniprot.org/annotation/VAR_063693|||http://purl.uniprot.org/annotation/VAR_063706|||http://purl.uniprot.org/annotation/VAR_067342|||http://purl.uniprot.org/annotation/VAR_077071|||http://purl.uniprot.org/annotation/VAR_077072|||http://purl.uniprot.org/annotation/VAR_077073|||http://purl.uniprot.org/annotation/VAR_077074|||http://purl.uniprot.org/annotation/VAR_077075|||http://purl.uniprot.org/annotation/VAR_079826|||http://purl.uniprot.org/annotation/VAR_080738|||http://purl.uniprot.org/annotation/VAR_080739|||http://purl.uniprot.org/annotation/VAR_085042|||http://purl.uniprot.org/annotation/VSP_059675|||http://purl.uniprot.org/annotation/VSP_059676|||http://purl.uniprot.org/annotation/VSP_059677|||http://purl.uniprot.org/annotation/VSP_059678|||http://purl.uniprot.org/annotation/VSP_059679|||http://purl.uniprot.org/annotation/VSP_059680|||http://purl.uniprot.org/annotation/VSP_059681|||http://purl.uniprot.org/annotation/VSP_059682
http://togogenome.org/gene/9606:MAGEA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43356                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Improves ability to bind to HLA-A1.|||MAGE|||Melanoma-associated antigen 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156702
http://togogenome.org/gene/9606:RHBG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H310                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Ammonium transporter Rh type B|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs protein stability resulting in loss of transporter activity.|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||Interaction with ANK3|||Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421.|||N-linked (GlcNAc...) asparagine|||Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-420.|||Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-421.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283597|||http://purl.uniprot.org/annotation/VAR_031497|||http://purl.uniprot.org/annotation/VAR_031498|||http://purl.uniprot.org/annotation/VAR_031499|||http://purl.uniprot.org/annotation/VAR_053637|||http://purl.uniprot.org/annotation/VSP_024340|||http://purl.uniprot.org/annotation/VSP_024341|||http://purl.uniprot.org/annotation/VSP_024342|||http://purl.uniprot.org/annotation/VSP_024343|||http://purl.uniprot.org/annotation/VSP_037136
http://togogenome.org/gene/9606:TNFRSF6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95407                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Repeat|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 6B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034570
http://togogenome.org/gene/9606:MRPS18C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3D5                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Mitochondrion|||Small ribosomal subunit protein bS18m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030629
http://togogenome.org/gene/9606:SCAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6H0|||http://purl.uniprot.org/uniprot/Q12770                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||ER export signal|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with SREBF2|||Loop-1|||Loop-7|||Lumenal|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||SSD|||Sterol regulatory element-binding protein cleavage-activating protein|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051208|||http://purl.uniprot.org/annotation/VAR_012203|||http://purl.uniprot.org/annotation/VSP_007451|||http://purl.uniprot.org/annotation/VSP_007452|||http://purl.uniprot.org/annotation/VSP_021105|||http://purl.uniprot.org/annotation/VSP_021106
http://togogenome.org/gene/9606:GPATCH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Found in a patient with primary congenital glaucoma; unknown pathological significance.|||Found in a patient with primary congenital glaucoma; unknown pathological significance; slightly increased transactivation activity on CXCR4 promoter; no effect on nuclear localization.|||Found in a patient with secondary congenital glaucoma associated with anterior segment dysgenesis and microphthalmia; unknown pathological significance.|||Found in patients with primary congenital glaucoma; unknown pathological significance; slightly increased transactivation activity on CXCR4 promoter; no effect on nuclear localization.|||G patch domain-containing protein 3|||G-patch                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087568|||http://purl.uniprot.org/annotation/VAR_051015|||http://purl.uniprot.org/annotation/VAR_079015|||http://purl.uniprot.org/annotation/VAR_079016|||http://purl.uniprot.org/annotation/VAR_079017
http://togogenome.org/gene/9606:OSER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX31                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Oxidative stress-responsive serine-rich protein 1|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079453|||http://purl.uniprot.org/annotation/VAR_024333
http://togogenome.org/gene/9606:ABCC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15440                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 5|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093363|||http://purl.uniprot.org/annotation/VSP_043397|||http://purl.uniprot.org/annotation/VSP_043398|||http://purl.uniprot.org/annotation/VSP_043399|||http://purl.uniprot.org/annotation/VSP_043400|||http://purl.uniprot.org/annotation/VSP_043401|||http://purl.uniprot.org/annotation/VSP_043402|||http://purl.uniprot.org/annotation/VSP_055354
http://togogenome.org/gene/9606:HHIPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0G3|||http://purl.uniprot.org/uniprot/Q96JK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HHIP-like protein 1|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314962|||http://purl.uniprot.org/annotation/PRO_5003270892|||http://purl.uniprot.org/annotation/VAR_060163|||http://purl.uniprot.org/annotation/VSP_030455|||http://purl.uniprot.org/annotation/VSP_030456
http://togogenome.org/gene/9606:HOXD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28356                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D9|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200220|||http://purl.uniprot.org/annotation/VAR_031851
http://togogenome.org/gene/9606:USP44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0E7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes deubiquitinase activity.|||Disordered|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||UBP-type|||USP|||Ubiquitin carboxyl-terminal hydrolase 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080673|||http://purl.uniprot.org/annotation/VAR_017125|||http://purl.uniprot.org/annotation/VAR_057043|||http://purl.uniprot.org/annotation/VAR_057044
http://togogenome.org/gene/9606:DGKA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23743                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binds calcium but with decreased affinity.|||DAGKc|||Diacylglycerol kinase alpha|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||Loss of calcium-binding.|||N6-acetyllysine|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218453|||http://purl.uniprot.org/annotation/VAR_031563|||http://purl.uniprot.org/annotation/VSP_032212|||http://purl.uniprot.org/annotation/VSP_032213|||http://purl.uniprot.org/annotation/VSP_047702|||http://purl.uniprot.org/annotation/VSP_047703
http://togogenome.org/gene/9606:EEIG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T8I3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  C2 NT-type|||EEIG family member 2|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236180|||http://purl.uniprot.org/annotation/VSP_034833
http://togogenome.org/gene/9606:SLC7A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01650                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased leucine transport activity.|||Disordered|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Interchain (with C-210 in SLC3A2)|||Large neutral amino acids transporter small subunit 1|||Nearly abolishes leucine transport activity.|||Phosphoserine|||Phosphothreonine|||Strongly decreased leucine transport activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054270|||http://purl.uniprot.org/annotation/VAR_048157|||http://purl.uniprot.org/annotation/VAR_070119
http://togogenome.org/gene/9606:ASXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q498B9|||http://purl.uniprot.org/uniprot/Q8IXJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with RARA.|||Basic and acidic residues|||DEUBAD|||Disordered|||HTH HARE-type|||In isoform 2.|||Interaction with NCOA1|||LXXLL motif|||Nuclear localization signal 1|||Nuclear localization signal 2|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Polycomb group protein ASXL1|||Required for interaction with RARA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059321|||http://purl.uniprot.org/annotation/VAR_028157|||http://purl.uniprot.org/annotation/VAR_028158|||http://purl.uniprot.org/annotation/VAR_051602|||http://purl.uniprot.org/annotation/VAR_051603|||http://purl.uniprot.org/annotation/VSP_007219|||http://purl.uniprot.org/annotation/VSP_007220
http://togogenome.org/gene/9606:VTCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7D3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||V-set domain-containing T-cell activation inhibitor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339237|||http://purl.uniprot.org/annotation/VSP_045423|||http://purl.uniprot.org/annotation/VSP_052841|||http://purl.uniprot.org/annotation/VSP_052842|||http://purl.uniprot.org/annotation/VSP_052843
http://togogenome.org/gene/9606:FBXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKC9                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CAAX motif|||F-box|||F-box/LRR-repeat protein 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interaction with Calmodulin|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of geranylgeranylation and association to membranes. Loss of interaction with NS5A, PIK3R1 and PIK3R2. No effect on interaction with PTPN13.|||Phosphothreonine|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119840|||http://purl.uniprot.org/annotation/VAR_036071|||http://purl.uniprot.org/annotation/VSP_044600
http://togogenome.org/gene/9606:KAT2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92830                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolised protein acetyltransferase activity.|||Bromo|||Catalytically dead mutant; abolished acyltransferase activity; when associated with A-575.|||Catalytically dead mutant; abolished acyltransferase activity; when associated with A-615.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone acetyltransferase KAT2A|||In isoform 2.|||Loop 3|||Mimics acetylation; reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with A-307 and A-735.|||N-acetylalanine|||N-acetyltransferase|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proton donor/acceptor|||Reduced ability to acetylate and inhibit PPARGC1A.|||Reduced histone succinylation without affecting histone acetylation. Reduced gene expression.|||Removed|||Slightly reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with A-307 and Q-549.|||Slightly reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with Q-549 and A-735.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211202|||http://purl.uniprot.org/annotation/VSP_000556
http://togogenome.org/gene/9606:ESR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A348FV93|||http://purl.uniprot.org/uniprot/Q0PTK2|||http://purl.uniprot.org/uniprot/Q7LCB3|||http://purl.uniprot.org/uniprot/Q92731                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes repression by activated ErbB2/ErbB3; when associated with D-105.|||Abolishes repression by activated ErbB2/ErbB3; when associated with D-87.|||Disordered|||Enhances repression by activated ErbB2/ErbB3; when associated with A-105.|||Enhances repression by activated ErbB2/ErbB3; when associated with A-87.|||Estrogen receptor beta|||Found in a patient with a 46,XY disorder of sex development; unknown pathological significance; no change in positive regulation of DNA-binding transcription factor activity.|||Found in a patient with a 46,XY disorder of sex development; unknown pathological significance; shows a higher positive regulation of DNA-binding transcription factor activity.|||Found in a patient with a 46,XY disorder of sex development; unknown pathological significance; shows increased positive regulation of DNA-binding transcription factor activity.|||In ODG8; completely inactive in positive regulation of DNA-binding transcription factor activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053642|||http://purl.uniprot.org/annotation/VAR_081786|||http://purl.uniprot.org/annotation/VAR_081787|||http://purl.uniprot.org/annotation/VAR_081788|||http://purl.uniprot.org/annotation/VAR_081789|||http://purl.uniprot.org/annotation/VSP_003684|||http://purl.uniprot.org/annotation/VSP_003685|||http://purl.uniprot.org/annotation/VSP_003686|||http://purl.uniprot.org/annotation/VSP_003687|||http://purl.uniprot.org/annotation/VSP_003688|||http://purl.uniprot.org/annotation/VSP_003689|||http://purl.uniprot.org/annotation/VSP_003690|||http://purl.uniprot.org/annotation/VSP_003691|||http://purl.uniprot.org/annotation/VSP_003692|||http://purl.uniprot.org/annotation/VSP_055746|||http://purl.uniprot.org/annotation/VSP_055747
http://togogenome.org/gene/9606:LMOD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAK6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In NEM10.|||In isoform 2.|||Interaction with tropomyosin alpha|||Leiomodin-3|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261175|||http://purl.uniprot.org/annotation/VAR_029088|||http://purl.uniprot.org/annotation/VAR_034083|||http://purl.uniprot.org/annotation/VAR_052401|||http://purl.uniprot.org/annotation/VAR_061863|||http://purl.uniprot.org/annotation/VAR_072643|||http://purl.uniprot.org/annotation/VSP_021664|||http://purl.uniprot.org/annotation/VSP_021665|||http://purl.uniprot.org/annotation/VSP_021666|||http://purl.uniprot.org/annotation/VSP_021667
http://togogenome.org/gene/9606:TOMM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q75MR5|||http://purl.uniprot.org/uniprot/Q9P0U1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Mitochondrial import receptor subunit TOM7 homolog|||Mitochondrial intermembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046759
http://togogenome.org/gene/9606:SERPINA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IW75                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage|||Fails to inhibit KLK7 activity. Increased protein stability in cleaved form and conformational changes which may allow escape of the substrate.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine|||Reactive center loop|||Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-221 and A-233.|||Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-221 and A-267.|||Reduced N-glycosylation. Loss of N-glycosylation; when associated with A-233 and A-267.|||Results in formation of an artificial disulfide bond which stabilizes the reactive center loop and enhances KLK7 inhibition activity; when associated with C-305.|||Results in formation of an artificial disulfide bond which stabilizes the reactive center loop and enhances KLK7 inhibition activity; when associated with C-383.|||Serpin A12|||Significantly enhances KLK7 inhibition activity. Slightly enhances KLK7 inhibition activity; when associated with E-302.|||Significantly impairs KLK7 inhibition activity. Slightly enhances KLK7 inhibition activity; when associated with S-379.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041976|||http://purl.uniprot.org/annotation/VAR_051943|||http://purl.uniprot.org/annotation/VAR_051944|||http://purl.uniprot.org/annotation/VAR_077875
http://togogenome.org/gene/9606:ZNF302                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYF4|||http://purl.uniprot.org/uniprot/B3KY96|||http://purl.uniprot.org/uniprot/B4DMN2|||http://purl.uniprot.org/uniprot/D6R9Q0|||http://purl.uniprot.org/uniprot/E7EVR1|||http://purl.uniprot.org/uniprot/Q8NC84|||http://purl.uniprot.org/uniprot/Q9NR11                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 302                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047522|||http://purl.uniprot.org/annotation/VSP_006914
http://togogenome.org/gene/9606:OVCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1V8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  CUB|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5014013299
http://togogenome.org/gene/9606:GBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92538                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arrests retrograde ERGIC/cis-Golgi-to-ER transport at an early step and causes disassembly of the Golgi and disassociation of COP1 from membranes.|||Basic and acidic residues|||Confers BFA tolerance.|||DCB; DCB:DCB domain and DCB:HUS domain interaction|||Disordered|||Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1|||HUS; DCB:HUS domain interaction|||In isoform 2 and isoform 3.|||In isoform 2.|||Increases interaction with COPG1 and PNPLA2.|||Inhibits Golgi membrane recruitment of GGA1, GGA2 and GGA3; generates misprocessing of PSAP.|||Interaction with RAB1B|||Phosphatidylinositol-phosphate binding; required for translocation to the leading edge and for ARF1 activation upon GPCR signaling|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by AMPK|||Phosphotyrosine|||Polar residues|||Prevents 2-DG-induced Golgi disassembly.|||Pro residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120210|||http://purl.uniprot.org/annotation/VAR_051926|||http://purl.uniprot.org/annotation/VSP_057522|||http://purl.uniprot.org/annotation/VSP_057523
http://togogenome.org/gene/9606:MDGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III|||GPI-anchor amidated serine|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||In isoform 2.|||MAM|||MAM domain-containing glycosylphosphatidylinositol anchor protein 1|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014864|||http://purl.uniprot.org/annotation/PRO_0000292042|||http://purl.uniprot.org/annotation/VAR_047660|||http://purl.uniprot.org/annotation/VAR_077845|||http://purl.uniprot.org/annotation/VSP_009835
http://togogenome.org/gene/9606:CNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09543                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2',3'-cyclic-nucleotide 3'-phosphodiesterase|||Cysteine methyl ester|||In HLD20; unknown pathological significance; decreased protein levels in patient cells.|||In isoform CNPI.|||Phosphoserine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089961|||http://purl.uniprot.org/annotation/PRO_0000422296|||http://purl.uniprot.org/annotation/VAR_033746|||http://purl.uniprot.org/annotation/VAR_085056|||http://purl.uniprot.org/annotation/VSP_004171
http://togogenome.org/gene/9606:ANKAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70AK8|||http://purl.uniprot.org/uniprot/Q7Z5J8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||Ankyrin and armadillo repeat-containing protein|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286806|||http://purl.uniprot.org/annotation/VAR_032164|||http://purl.uniprot.org/annotation/VAR_032165|||http://purl.uniprot.org/annotation/VSP_025166|||http://purl.uniprot.org/annotation/VSP_025167|||http://purl.uniprot.org/annotation/VSP_025168|||http://purl.uniprot.org/annotation/VSP_025169|||http://purl.uniprot.org/annotation/VSP_025170|||http://purl.uniprot.org/annotation/VSP_025171|||http://purl.uniprot.org/annotation/VSP_025172|||http://purl.uniprot.org/annotation/VSP_025173|||http://purl.uniprot.org/annotation/VSP_025174
http://togogenome.org/gene/9606:MYOZ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Binding to ACTN2|||Binding to ACTN2, PPP3CA and TCAP|||Binding to FLNC|||Disordered|||In isoform 2.|||In isoform 3.|||Myozenin-3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111102|||http://purl.uniprot.org/annotation/VAR_056203|||http://purl.uniprot.org/annotation/VAR_067718|||http://purl.uniprot.org/annotation/VSP_051876|||http://purl.uniprot.org/annotation/VSP_051877|||http://purl.uniprot.org/annotation/VSP_051878|||http://purl.uniprot.org/annotation/VSP_051879
http://togogenome.org/gene/9606:TMEM230                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTT2|||http://purl.uniprot.org/uniprot/Q96A57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In PARK; sporadic case; unknown pathological significance; results in decreased synaptic vesicle trafficking.|||In PARK; unknown pathological significance; results in decreased synaptic vesicle trafficking.|||In isoform 1.|||Phosphoserine|||Transmembrane protein 230                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233892|||http://purl.uniprot.org/annotation/VAR_076713|||http://purl.uniprot.org/annotation/VAR_076714|||http://purl.uniprot.org/annotation/VAR_076715|||http://purl.uniprot.org/annotation/VAR_082923|||http://purl.uniprot.org/annotation/VSP_018155
http://togogenome.org/gene/9606:POLR3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y1                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase III subunit RPC10|||In HLD21; decrease in expression levels of RNA polymerase III-transcribed genes such as 5S and 7S ribosomal RNAs.|||TFIIS-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121475|||http://purl.uniprot.org/annotation/VAR_027918|||http://purl.uniprot.org/annotation/VAR_085543
http://togogenome.org/gene/9606:CDH15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55291                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-15|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MRD3; affects cell-cell adhesion but not surface expression of the protein.|||In MRD3; uncertain pathological significance.|||N-linked (GlcNAc...) asparagine|||No effect on cell-cell adhesion.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003805|||http://purl.uniprot.org/annotation/PRO_0000003806|||http://purl.uniprot.org/annotation/VAR_054966|||http://purl.uniprot.org/annotation/VAR_054967|||http://purl.uniprot.org/annotation/VAR_054968|||http://purl.uniprot.org/annotation/VAR_054969
http://togogenome.org/gene/9606:MORF4L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to MRFAP1.|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with KAT8|||Interaction with RB1-1|||Interaction with RB1-2|||MRG|||Mortality factor 4-like protein 1|||N6-acetyllysine|||No effect on MRFAP1 binding.|||Nuclear localization signal|||Polar residues|||Reduces binding to MRFAP1.|||Sufficient for interaction with PHF12|||Sufficient for interaction with SIN3A|||Tudor-knot                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088764|||http://purl.uniprot.org/annotation/VSP_012889|||http://purl.uniprot.org/annotation/VSP_046016
http://togogenome.org/gene/9606:SLC26A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXK1|||http://purl.uniprot.org/uniprot/Q7LBE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased plasma membrane expression which partially accounts for decreased whole cell currents.|||Decreased plasma membrane expression which partially accounts for decreased whole cell currents; transport is reduced to about 50%.|||Disordered|||Displays higher channel activity and enhanced chloride-bicarbonate ion exchange.|||Extracellular|||Helical|||In isoform 2.|||Increased current.|||Increased current; when associated with A-781.|||Increased current; when associated with K-201.|||Polar residues|||Reduced chloride ion flux.|||Results in smaller halide currents but not for thiocyanate ion.|||STAS|||Solute carrier family 26 member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324492|||http://purl.uniprot.org/annotation/VAR_039801|||http://purl.uniprot.org/annotation/VAR_039802|||http://purl.uniprot.org/annotation/VAR_068683|||http://purl.uniprot.org/annotation/VAR_068684|||http://purl.uniprot.org/annotation/VAR_068685|||http://purl.uniprot.org/annotation/VAR_068686|||http://purl.uniprot.org/annotation/VAR_068687|||http://purl.uniprot.org/annotation/VAR_068688|||http://purl.uniprot.org/annotation/VSP_054056
http://togogenome.org/gene/9606:H4C9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:ULBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZM6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated glycine|||MHC class I alpha-1 like|||MHC class I alpha-2 like|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UL16-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019015|||http://purl.uniprot.org/annotation/PRO_0000019016|||http://purl.uniprot.org/annotation/VAR_050407
http://togogenome.org/gene/9606:BCL2L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3C5|||http://purl.uniprot.org/uniprot/Q07817|||http://purl.uniprot.org/uniprot/Q5TE63                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with DNM1L and endocytosis enhancement.|||Apoptosis regulator Bcl-2 family BH4|||BH1|||BH2|||BH3|||BH4|||Bcl-2-like protein 1|||Cleavage; by caspase-1|||Decreases interaction with DNM1L, no effect on endocytosis enhancement.|||Disordered|||Helical|||In isoform Bcl-X(S).|||In isoform Bcl-X(beta).|||Less stable at G2 checkpoint after DNA damage.|||Loss of anti-apoptotic activity.|||No cleavage by caspase-1 nor by caspase-3.|||No effect on caspase-1 cleavage.|||No heterodimerization with BAX.|||Phosphoserine; by CDK1|||Phosphoserine; by PLK3|||Reduces anti-apoptotic activity by about half.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143062|||http://purl.uniprot.org/annotation/VSP_000515|||http://purl.uniprot.org/annotation/VSP_000516
http://togogenome.org/gene/9606:GABPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SZG2|||http://purl.uniprot.org/uniprot/Q8TAK5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Disordered|||GA-binding protein subunit beta-2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325908|||http://purl.uniprot.org/annotation/VAR_039950
http://togogenome.org/gene/9606:OR2G6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW53|||http://purl.uniprot.org/uniprot/Q5TZ20                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2G6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150478|||http://purl.uniprot.org/annotation/VAR_053142|||http://purl.uniprot.org/annotation/VAR_062020
http://togogenome.org/gene/9606:MRPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYD6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein uL1m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252440|||http://purl.uniprot.org/annotation/VAR_027865|||http://purl.uniprot.org/annotation/VAR_027866
http://togogenome.org/gene/9606:SRPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPE1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||SRSF protein kinase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086709|||http://purl.uniprot.org/annotation/VAR_041119|||http://purl.uniprot.org/annotation/VAR_041120|||http://purl.uniprot.org/annotation/VAR_041121|||http://purl.uniprot.org/annotation/VSP_040939|||http://purl.uniprot.org/annotation/VSP_040940|||http://purl.uniprot.org/annotation/VSP_040941
http://togogenome.org/gene/9606:PSME2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SZ7|||http://purl.uniprot.org/uniprot/Q9UL46                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Proteasome activator PA28 C-terminal|||Proteasome activator PA28 N-terminal|||Proteasome activator complex subunit 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161785|||http://purl.uniprot.org/annotation/VAR_063111
http://togogenome.org/gene/9606:APBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59G28|||http://purl.uniprot.org/uniprot/Q99767                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Amyloid-beta A4 precursor protein-binding family A member 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ|||PDZ 1|||PDZ 2|||PID|||Phosphoserine|||Polar residues|||STXBP1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064616|||http://purl.uniprot.org/annotation/VAR_050665|||http://purl.uniprot.org/annotation/VSP_045692
http://togogenome.org/gene/9606:ITGB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05106                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function.|||CX3CL1-binding|||Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In BDPLT24; the mutant protein is constitutively active; decreased platelet surface expression; spontaneous FAK phosphosphorylation; abnormal cell shape.|||In BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape.|||In GT2.|||In GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1.|||In GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor.|||In GT2; not expressed on the surface and absent inside the transfected cells.|||In GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface.|||In GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation interupts the interaction of the ITGA2B/ITGB3 complex.|||In GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein.|||In GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression.|||In GT2; type B.|||In GT2; type I.|||In GT2; type II.|||In GT2; variant Strasbourg-1.|||In GT2; variant form.|||In alloantigen CA(+)/TU(+).|||In alloantigen HPA-1B.|||In alloantigen HPA-4B.|||In alloantigen MO(+); in a case of neonatal alloimmune thrombocytopenia.|||In alloantigen SR(A).|||In isoform Beta-3B.|||In isoform Beta-3C.|||Increases ligand-binding activity.|||Integrin beta-3|||Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding|||LIR|||N-linked (GlcNAc...) asparagine|||No effect on cell surface location but impairs interaction with TNS3 and PEAK1.|||PSI|||Phosphothreonine|||Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro|||Phosphotyrosine|||Slight increase in ligand-binding activity; when associated with 698-D--K-702 del.|||Slight increase in ligand-binding activity; when associated with A-659.|||VWFA|||in ADMIDAS binding site|||in ADMIDAS binding site and liganded-open conformation|||in ADMIDAS binding site and unliganded-closed conformation|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016344|||http://purl.uniprot.org/annotation/VAR_003993|||http://purl.uniprot.org/annotation/VAR_003994|||http://purl.uniprot.org/annotation/VAR_003995|||http://purl.uniprot.org/annotation/VAR_003996|||http://purl.uniprot.org/annotation/VAR_003997|||http://purl.uniprot.org/annotation/VAR_003998|||http://purl.uniprot.org/annotation/VAR_003999|||http://purl.uniprot.org/annotation/VAR_004000|||http://purl.uniprot.org/annotation/VAR_004001|||http://purl.uniprot.org/annotation/VAR_004002|||http://purl.uniprot.org/annotation/VAR_004003|||http://purl.uniprot.org/annotation/VAR_004004|||http://purl.uniprot.org/annotation/VAR_004005|||http://purl.uniprot.org/annotation/VAR_010649|||http://purl.uniprot.org/annotation/VAR_010651|||http://purl.uniprot.org/annotation/VAR_010671|||http://purl.uniprot.org/annotation/VAR_010672|||http://purl.uniprot.org/annotation/VAR_014178|||http://purl.uniprot.org/annotation/VAR_030473|||http://purl.uniprot.org/annotation/VAR_030474|||http://purl.uniprot.org/annotation/VAR_030475|||http://purl.uniprot.org/annotation/VAR_030476|||http://purl.uniprot.org/annotation/VAR_030477|||http://purl.uniprot.org/annotation/VAR_030478|||http://purl.uniprot.org/annotation/VAR_030479|||http://purl.uniprot.org/annotation/VAR_030480|||http://purl.uniprot.org/annotation/VAR_030481|||http://purl.uniprot.org/annotation/VAR_030482|||http://purl.uniprot.org/annotation/VAR_030483|||http://purl.uniprot.org/annotation/VAR_030484|||http://purl.uniprot.org/annotation/VAR_030485|||http://purl.uniprot.org/annotation/VAR_030486|||http://purl.uniprot.org/annotation/VAR_049633|||http://purl.uniprot.org/annotation/VAR_069920|||http://purl.uniprot.org/annotation/VAR_069921|||http://purl.uniprot.org/annotation/VAR_069922|||http://purl.uniprot.org/annotation/VAR_069923|||http://purl.uniprot.org/annotation/VAR_069924|||http://purl.uniprot.org/annotation/VAR_081732|||http://purl.uniprot.org/annotation/VSP_002745|||http://purl.uniprot.org/annotation/VSP_002746
http://togogenome.org/gene/9606:EPHA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJJ0|||http://purl.uniprot.org/uniprot/P29320|||http://purl.uniprot.org/uniprot/Q6P4R6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  10-fold suppression of kinase activity; when associated with F-596. Full kinase activity; when associated with F-596 and F-742. Full kinase activity; when associated with F-596 and A-768.|||10-fold suppression of kinase activity; when associated with F-602. Full kinase activity; when associated with F-602 and F-742. Full kinase activity; when associated with F-602 and A-768.|||Cytoplasmic|||Eph LBD|||Ephrin type-A receptor 3|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Full kinase activity; when associated with F-596 and F-602.|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung carcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Loss of EFNA5-binding ability and function.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SAM|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016802|||http://purl.uniprot.org/annotation/PRO_5004278260|||http://purl.uniprot.org/annotation/PRO_5010061075|||http://purl.uniprot.org/annotation/VAR_027919|||http://purl.uniprot.org/annotation/VAR_036086|||http://purl.uniprot.org/annotation/VAR_036087|||http://purl.uniprot.org/annotation/VAR_036088|||http://purl.uniprot.org/annotation/VAR_036089|||http://purl.uniprot.org/annotation/VAR_042126|||http://purl.uniprot.org/annotation/VAR_042127|||http://purl.uniprot.org/annotation/VAR_042128|||http://purl.uniprot.org/annotation/VAR_042129|||http://purl.uniprot.org/annotation/VAR_042130|||http://purl.uniprot.org/annotation/VAR_042131|||http://purl.uniprot.org/annotation/VAR_042132|||http://purl.uniprot.org/annotation/VAR_042133|||http://purl.uniprot.org/annotation/VAR_042134|||http://purl.uniprot.org/annotation/VAR_065831|||http://purl.uniprot.org/annotation/VAR_065832|||http://purl.uniprot.org/annotation/VAR_068853|||http://purl.uniprot.org/annotation/VSP_002995|||http://purl.uniprot.org/annotation/VSP_002996
http://togogenome.org/gene/9606:ZNF716                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NP11                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 716                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318855
http://togogenome.org/gene/9606:KIF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRS8|||http://purl.uniprot.org/uniprot/Q9P2E2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF17|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125450|||http://purl.uniprot.org/annotation/VAR_023527|||http://purl.uniprot.org/annotation/VAR_023528|||http://purl.uniprot.org/annotation/VAR_055983|||http://purl.uniprot.org/annotation/VAR_055984|||http://purl.uniprot.org/annotation/VAR_055985|||http://purl.uniprot.org/annotation/VAR_061282|||http://purl.uniprot.org/annotation/VSP_040346
http://togogenome.org/gene/9606:PDE5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9C5|||http://purl.uniprot.org/uniprot/O76074                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Changes substrate selectivity from cGMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with N-767 and Y-775.|||Changes substrate selectivity from cGMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with N-767 and Y-853.|||Changes substrate selectivity from cGMP-specific to dual cAMP and cGMP binding and hydrolysis; when associated with Y-775 and Y-853.|||Disordered|||GAF 1|||GAF 2|||In isoform PDE5A2.|||PDEase|||Phosphoserine|||Polar residues|||Proton donor|||cGMP-specific 3',5'-cyclic phosphodiesterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198823|||http://purl.uniprot.org/annotation/VAR_027775|||http://purl.uniprot.org/annotation/VAR_027776|||http://purl.uniprot.org/annotation/VSP_004591
http://togogenome.org/gene/9606:FYB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15117                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FYN-binding protein 1|||In THC3.|||In isoform 3.|||In isoform FYB-130 and isoform 3.|||Interaction with SKAP1|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2-binding|||SH2-binding; to FYN|||SH2-binding; to LCP2|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087396|||http://purl.uniprot.org/annotation/VAR_056880|||http://purl.uniprot.org/annotation/VAR_056881|||http://purl.uniprot.org/annotation/VAR_060592|||http://purl.uniprot.org/annotation/VAR_078810|||http://purl.uniprot.org/annotation/VSP_042309|||http://purl.uniprot.org/annotation/VSP_047288
http://togogenome.org/gene/9606:OR4F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV92|||http://purl.uniprot.org/uniprot/Q6IEY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4F3/4F16/4F29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150551
http://togogenome.org/gene/9606:WDR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TP22|||http://purl.uniprot.org/uniprot/O75083|||http://purl.uniprot.org/uniprot/V9HWG7                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In PFITS; almost complete loss of protein expression in peripheral blood mononuclear cells.|||In PFITS; contrary to wild-type, which shows a uniform distribution throughout the cytoplasm, forms cytoplasmic aggregates, which contain pyrin/MEFV, hence might trigger spontaneous inflammasome activation.|||In PFITS; unknown pathological significance.|||In PFITS; unknown pathological significance; almost complete loss of protein expression in peripheral blood mononuclear cells.|||In isoform 2.|||N6-acetyllysine|||Phosphotyrosine|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051341|||http://purl.uniprot.org/annotation/VAR_013445|||http://purl.uniprot.org/annotation/VAR_084593|||http://purl.uniprot.org/annotation/VAR_084594|||http://purl.uniprot.org/annotation/VAR_084595|||http://purl.uniprot.org/annotation/VAR_084596|||http://purl.uniprot.org/annotation/VAR_084597|||http://purl.uniprot.org/annotation/VAR_084598|||http://purl.uniprot.org/annotation/VAR_084599|||http://purl.uniprot.org/annotation/VAR_084600|||http://purl.uniprot.org/annotation/VAR_084601|||http://purl.uniprot.org/annotation/VSP_012926
http://togogenome.org/gene/9606:PRCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00LT1                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In RP36; loss of palmitoylation; reduced protein stability; fails to localize to the photoreceptor outer segment.|||In RP36; no effect on protein level.|||In RP36; unknown pathological significance; no effect on protein stability.|||Photoreceptor disk component PRCD|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280353|||http://purl.uniprot.org/annotation/VAR_031122|||http://purl.uniprot.org/annotation/VAR_031123|||http://purl.uniprot.org/annotation/VAR_031124|||http://purl.uniprot.org/annotation/VAR_078540
http://togogenome.org/gene/9606:CLEC4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTT0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man.|||C-type lectin|||C-type lectin domain family 4 member C|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Significantly impairs carbohydrate binding for the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046615|||http://purl.uniprot.org/annotation/VSP_012845
http://togogenome.org/gene/9606:TPPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94811|||http://purl.uniprot.org/uniprot/Q4L233                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-107 and A-159.|||In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-107.|||In 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-159.|||In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-07 and E-159.|||In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-107.|||In 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-159.|||In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-160.|||In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-45.|||In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-45 and A-160.|||In 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-18, A-45 and A-160.|||In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-160.|||In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-45.|||In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-45 and E-160.|||In 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-18, E-45 and E-160.|||Mediates interaction with LIMK1|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CDK1, CDK5 and MAPK1|||Phosphoserine; by ROCK1|||Phosphothreonine; by CDK1 and CDK5|||Phosphothreonine; by PKA; in vitro|||Tubulin polymerization-promoting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221135
http://togogenome.org/gene/9606:CYP1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05177                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 1A2|||In allele CYP1A2*10.|||In allele CYP1A2*11; drastic reduction in O-deethylation of phenacetin and 7-ethoxyresorufin; has a Vmax of approximately 5% of that of the wild-type and 5-fold lower Km value.|||In allele CYP1A2*12.|||In allele CYP1A2*13.|||In allele CYP1A2*14.|||In allele CYP1A2*15.|||In allele CYP1A2*16.|||In allele CYP1A2*2.|||In allele CYP1A2*3; increases N-hydroxylation activity of heterocyclic amines; reduces phenacetin O-deethylation activity.|||In allele CYP1A2*4; increases catalytic efficiency of N-hydroxylation towards some heterocyclic amines and reduces towards others; reduces catalytic efficiency of phenacetin O-deethylation due to a high decrease in the affinity for phenacetin.|||In allele CYP1A2*5; increases N-hydroxylation activity of heterocyclic amines; reduces catalytic efficiency of phenacetin O-deethylation.|||In allele CYP1A2*6; not detected when expressed in heterologous system as it may be critical for maintenance of protein tertiary structure.|||In allele CYP1A2*8.|||In allele CYP1A2*9.|||O-linked (GlcNAc) serine|||Removed|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051651|||http://purl.uniprot.org/annotation/VAR_008349|||http://purl.uniprot.org/annotation/VAR_020793|||http://purl.uniprot.org/annotation/VAR_020794|||http://purl.uniprot.org/annotation/VAR_020795|||http://purl.uniprot.org/annotation/VAR_020796|||http://purl.uniprot.org/annotation/VAR_020848|||http://purl.uniprot.org/annotation/VAR_020849|||http://purl.uniprot.org/annotation/VAR_020850|||http://purl.uniprot.org/annotation/VAR_020851|||http://purl.uniprot.org/annotation/VAR_020852|||http://purl.uniprot.org/annotation/VAR_020853|||http://purl.uniprot.org/annotation/VAR_023196|||http://purl.uniprot.org/annotation/VAR_024709|||http://purl.uniprot.org/annotation/VAR_024710|||http://purl.uniprot.org/annotation/VAR_025182|||http://purl.uniprot.org/annotation/VAR_025183|||http://purl.uniprot.org/annotation/VAR_025184|||http://purl.uniprot.org/annotation/VAR_025185|||http://purl.uniprot.org/annotation/VAR_025186|||http://purl.uniprot.org/annotation/VAR_025187|||http://purl.uniprot.org/annotation/VAR_025188|||http://purl.uniprot.org/annotation/VAR_025189|||http://purl.uniprot.org/annotation/VAR_055563
http://togogenome.org/gene/9606:ASB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q27                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Abolishes monoubiquitination.|||Abolishes phosphorylation. Abolishes degradation of FLNA. No effect on assembly into ubiquitin-protein ligase complex.|||Ankyrin repeat and SOCS box protein 2|||In isoform 2.|||No interaction with CUL5 or RNF7.|||No interaction with Elongin BC complex.|||Phosphomimetic mutant. No effect on isoform 2 FLNA degradation. No effect on assembly into ubiquitin-protein ligase complex.|||Phosphoserine; by MAPK|||Required for FLNA degradation|||SOCS box|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066925|||http://purl.uniprot.org/annotation/VAR_022089|||http://purl.uniprot.org/annotation/VSP_061164
http://togogenome.org/gene/9606:KIF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02241                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CDAN3A; results in loss of function; does not rescue defective cytokinesis when expressed in KIF3-deficient cells.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with ARF6|||Kinesin motor|||Kinesin-like protein KIF23|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125434|||http://purl.uniprot.org/annotation/VAR_049686|||http://purl.uniprot.org/annotation/VAR_086957|||http://purl.uniprot.org/annotation/VSP_021801|||http://purl.uniprot.org/annotation/VSP_057348|||http://purl.uniprot.org/annotation/VSP_057349
http://togogenome.org/gene/9606:MX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20592                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Defective GTP-hydrolysis. Disruption of nuclear import and cell-cycle progression.|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||In isoform 2.|||Interferon-induced GTP-binding protein Mx2|||Loss of GTP-binding and localization to nuclear pore. Disruption of nuclear import.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206598|||http://purl.uniprot.org/annotation/VSP_056443|||http://purl.uniprot.org/annotation/VSP_056444|||http://purl.uniprot.org/annotation/VSP_056445
http://togogenome.org/gene/9606:HOATZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI97                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein HOATZ|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328995|||http://purl.uniprot.org/annotation/VSP_032883|||http://purl.uniprot.org/annotation/VSP_032884
http://togogenome.org/gene/9606:S1PR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99500                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sphingosine 1-phosphate receptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069421|||http://purl.uniprot.org/annotation/VAR_033465
http://togogenome.org/gene/9606:DDB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92466                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA damage-binding protein 2|||DWD box|||Decreased acetylation levels.|||Disordered|||Does not affect acetylation levels.|||Impairs interaction with DDB1.|||In XP-E; impairs DNA-binding of the UV-DDB complex.|||In XP-E; impairs interaction with DDB1 and CUL4A.|||In isoform D1.|||In isoform D2.|||In isoform D3.|||In isoform D4.|||N6-acetyllysine|||Phosphoserine|||Photolesion recognition|||Required for interaction with DDB1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050953|||http://purl.uniprot.org/annotation/VAR_010141|||http://purl.uniprot.org/annotation/VAR_010142|||http://purl.uniprot.org/annotation/VAR_016337|||http://purl.uniprot.org/annotation/VAR_016338|||http://purl.uniprot.org/annotation/VSP_014674|||http://purl.uniprot.org/annotation/VSP_014675|||http://purl.uniprot.org/annotation/VSP_014676|||http://purl.uniprot.org/annotation/VSP_014677|||http://purl.uniprot.org/annotation/VSP_014678|||http://purl.uniprot.org/annotation/VSP_014679
http://togogenome.org/gene/9606:URB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14146                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Unhealthy ribosome biogenesis protein 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050720|||http://purl.uniprot.org/annotation/VAR_034031|||http://purl.uniprot.org/annotation/VAR_046975
http://togogenome.org/gene/9606:SORCS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XB2|||http://purl.uniprot.org/uniprot/Q9UPU3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Repeat|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BNR 1|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine|||PKD|||VPS10 domain-containing receptor SorCS3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033174
http://togogenome.org/gene/9606:CD2AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5K6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||CD2-associated protein|||Disordered|||Found in patients with steroid-resistant nephrotic syndrome; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with ANLN and localization to the midbody|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3 1; truncated|||SH3 2|||SH3 3|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089435|||http://purl.uniprot.org/annotation/VAR_033672|||http://purl.uniprot.org/annotation/VAR_087609|||http://purl.uniprot.org/annotation/VAR_087610
http://togogenome.org/gene/9606:UPK3BL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0FP48|||http://purl.uniprot.org/uniprot/E5RIL1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Uroplakin-3b-like protein 1|||Uroplakin-3b-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000375087|||http://purl.uniprot.org/annotation/PRO_5003196876
http://togogenome.org/gene/9606:NUP54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3B4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 2 AA repeats of F-G|||In isoform 2.|||In isoform 3.|||Nucleoporin p54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204874|||http://purl.uniprot.org/annotation/VSP_008740|||http://purl.uniprot.org/annotation/VSP_008741|||http://purl.uniprot.org/annotation/VSP_054355
http://togogenome.org/gene/9606:SLC36A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6YBV0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Neutral amino acid uniporter 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308318|||http://purl.uniprot.org/annotation/VAR_036791|||http://purl.uniprot.org/annotation/VAR_036792|||http://purl.uniprot.org/annotation/VAR_036793|||http://purl.uniprot.org/annotation/VSP_028959
http://togogenome.org/gene/9606:CACNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02641                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||SH3|||Voltage-dependent L-type calcium channel subunit beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144046|||http://purl.uniprot.org/annotation/VAR_036349|||http://purl.uniprot.org/annotation/VSP_000623|||http://purl.uniprot.org/annotation/VSP_000624|||http://purl.uniprot.org/annotation/VSP_000625
http://togogenome.org/gene/9606:GLT8D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CQ7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glycosyltransferase 8 domain-containing protein 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288528|||http://purl.uniprot.org/annotation/VAR_032443|||http://purl.uniprot.org/annotation/VSP_025705|||http://purl.uniprot.org/annotation/VSP_025706
http://togogenome.org/gene/9606:RMDN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFM4|||http://purl.uniprot.org/uniprot/Q96LZ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Regulator of microtubule dynamics protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287504|||http://purl.uniprot.org/annotation/VAR_032316|||http://purl.uniprot.org/annotation/VSP_025524|||http://purl.uniprot.org/annotation/VSP_025525|||http://purl.uniprot.org/annotation/VSP_025526|||http://purl.uniprot.org/annotation/VSP_025527
http://togogenome.org/gene/9606:BRINP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76B58                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BMP/retinoic acid-inducible neural-specific protein 3|||In isoform 2.|||MACPF|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045774|||http://purl.uniprot.org/annotation/VSP_055545|||http://purl.uniprot.org/annotation/VSP_055546
http://togogenome.org/gene/9606:KIF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FN5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In PFIC8.|||In PFIC8; unknown pathological significance.|||Kinesin motor|||Kinesin-like protein KIF12|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125444|||http://purl.uniprot.org/annotation/VAR_086702|||http://purl.uniprot.org/annotation/VAR_086703|||http://purl.uniprot.org/annotation/VAR_086704|||http://purl.uniprot.org/annotation/VAR_086705
http://togogenome.org/gene/9606:FAM170A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A519                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type; degenerate|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein FAM170A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326110|||http://purl.uniprot.org/annotation/VAR_047312|||http://purl.uniprot.org/annotation/VSP_032556|||http://purl.uniprot.org/annotation/VSP_032557|||http://purl.uniprot.org/annotation/VSP_035475|||http://purl.uniprot.org/annotation/VSP_035476|||http://purl.uniprot.org/annotation/VSP_035477
http://togogenome.org/gene/9606:PMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y6S3|||http://purl.uniprot.org/uniprot/A0A8V8TP61|||http://purl.uniprot.org/uniprot/A0A8V8TP84|||http://purl.uniprot.org/uniprot/A0A8V8TQ50|||http://purl.uniprot.org/uniprot/A0A8V8TQ92|||http://purl.uniprot.org/uniprot/A0A8V8TQG9|||http://purl.uniprot.org/uniprot/B4DGM0|||http://purl.uniprot.org/uniprot/C9J167|||http://purl.uniprot.org/uniprot/P54278|||http://purl.uniprot.org/uniprot/Q7Z3Q2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects binding to importins alpha, including KPNA2, hence may affect import to the nucleus.|||Basic and acidic residues|||DNA mismatch repair protein S5|||Decreased DNA mismatch repair activity; loss of ATPase activity.|||Disordered|||In LYNCH4; decreased DNA mismatch repair activity.|||In LYNCH4; strongly decreased DNA mismatch repair activity in an in vitro assay; loss of ATPase activity; reduced protein stability compared to wild-type; loss of structural identity.|||In LYNCH4; strongly decreased DNA mismatch repair activity.|||In LYNCH4; unknown pathological significance.|||In LYNCH4; unknown pathological significance; decreased DNA mismatch repair activity.|||In LYNCH4; unknown pathological significance; normal DNA mismatch repair activity.|||In LYNCH4; unknown pathological significance; normal DNA mismatch repair activity; no effect on protein stability compared to wild-type; no effect on ATPase activity; does not appear to induce a significant structural rearrangement.|||In LYNCH4; unknown pathological significance; significantly reduced interaction with MLH1; normal DNA mismatch repair activity.|||In MMRCS4 and LYNCH4; decreased DNA mismatch repair activity; decreased protein stability.|||In MMRCS4 and LYNCH4; strongly decreased DNA mismatch repair activity; no effect on protein abundance; no effect on subcellular localization.|||In MMRCS4 and LYNCH4; unknown pathological significance; normal DNA mismatch repair activity.|||In MMRCS4; decreased DNA mismatch repair activity.|||In MMRCS4; unknown pathological significance; decreased DNA mismatch repair activity.|||In MMRCS4; unknown pathological significance; normal DNA mismatch repair activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased DNA mismatch repair activity in an in vitro assay; no effect on protein stability.|||May affect protein stability, no effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type.|||Mismatch repair endonuclease PMS2|||MutL C-terminal dimerisation|||No effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type; loss of ATPase activity; retained ability to bind ATP; no effect on protein stability.|||No effect on DNA mismatch repair activity in an in vitro assay, compared to wild-type; no effect on ATPase activity; no effect on protein stability.|||No effect on DNA mismatch repair activity.|||No effect on protein abundance, no effect on subcellular localization and loss of DNA mismatch repair activity.|||No effect on protein abundance; no effect on subcellular localization; normal DNA mismatch repair activity.|||No effect on protein levels.|||No effect on protein levels; decreased DNA mismatch repair activity in an in vitro assay.|||Normal DNA mismatch repair activity.|||Normal DNA mismatch repair activity; significantly reduced interaction with MLH1.|||Nuclear localization signal|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178005|||http://purl.uniprot.org/annotation/VAR_004469|||http://purl.uniprot.org/annotation/VAR_012969|||http://purl.uniprot.org/annotation/VAR_012970|||http://purl.uniprot.org/annotation/VAR_012971|||http://purl.uniprot.org/annotation/VAR_012972|||http://purl.uniprot.org/annotation/VAR_012973|||http://purl.uniprot.org/annotation/VAR_012974|||http://purl.uniprot.org/annotation/VAR_016133|||http://purl.uniprot.org/annotation/VAR_016134|||http://purl.uniprot.org/annotation/VAR_016135|||http://purl.uniprot.org/annotation/VAR_024541|||http://purl.uniprot.org/annotation/VAR_066838|||http://purl.uniprot.org/annotation/VAR_078517|||http://purl.uniprot.org/annotation/VAR_078518|||http://purl.uniprot.org/annotation/VAR_078519|||http://purl.uniprot.org/annotation/VAR_078520|||http://purl.uniprot.org/annotation/VAR_078521|||http://purl.uniprot.org/annotation/VAR_078522|||http://purl.uniprot.org/annotation/VAR_078523|||http://purl.uniprot.org/annotation/VAR_078524|||http://purl.uniprot.org/annotation/VAR_078525|||http://purl.uniprot.org/annotation/VAR_078526|||http://purl.uniprot.org/annotation/VAR_078527|||http://purl.uniprot.org/annotation/VAR_078528|||http://purl.uniprot.org/annotation/VAR_078529|||http://purl.uniprot.org/annotation/VAR_078530|||http://purl.uniprot.org/annotation/VAR_078531|||http://purl.uniprot.org/annotation/VAR_078532|||http://purl.uniprot.org/annotation/VAR_078533|||http://purl.uniprot.org/annotation/VAR_078534|||http://purl.uniprot.org/annotation/VAR_078535|||http://purl.uniprot.org/annotation/VAR_078536|||http://purl.uniprot.org/annotation/VAR_078537|||http://purl.uniprot.org/annotation/VAR_078538|||http://purl.uniprot.org/annotation/VAR_078539|||http://purl.uniprot.org/annotation/VAR_079012|||http://purl.uniprot.org/annotation/VAR_079013|||http://purl.uniprot.org/annotation/VAR_079014|||http://purl.uniprot.org/annotation/VAR_079817|||http://purl.uniprot.org/annotation/VAR_079818|||http://purl.uniprot.org/annotation/VAR_079819|||http://purl.uniprot.org/annotation/VAR_079820|||http://purl.uniprot.org/annotation/VAR_079821|||http://purl.uniprot.org/annotation/VAR_087079|||http://purl.uniprot.org/annotation/VAR_087080|||http://purl.uniprot.org/annotation/VAR_087081|||http://purl.uniprot.org/annotation/VAR_087082|||http://purl.uniprot.org/annotation/VAR_087083|||http://purl.uniprot.org/annotation/VAR_087084|||http://purl.uniprot.org/annotation/VAR_087085|||http://purl.uniprot.org/annotation/VSP_029384|||http://purl.uniprot.org/annotation/VSP_029385|||http://purl.uniprot.org/annotation/VSP_029386|||http://purl.uniprot.org/annotation/VSP_029387|||http://purl.uniprot.org/annotation/VSP_029388
http://togogenome.org/gene/9606:MGAT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09328                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A|||Cytoplasmic|||Decreased catalytic activity.|||Helical; Signal-anchor for type II membrane protein|||Important for activity in FGF2 release|||Loss of catalytic activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on the biosynthesis of the secreted form.|||Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A|||Sufficient for catalytic activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080522|||http://purl.uniprot.org/annotation/PRO_0000445692
http://togogenome.org/gene/9606:TRIM42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||COS|||Fibronectin type-III|||In isoform 2.|||RING-type|||Tripartite motif-containing protein 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056263|||http://purl.uniprot.org/annotation/VAR_034468|||http://purl.uniprot.org/annotation/VAR_034469|||http://purl.uniprot.org/annotation/VAR_052143|||http://purl.uniprot.org/annotation/VSP_012066|||http://purl.uniprot.org/annotation/VSP_012067
http://togogenome.org/gene/9606:PTGES2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHH0|||http://purl.uniprot.org/uniprot/B3KPZ2|||http://purl.uniprot.org/uniprot/B4DWP1|||http://purl.uniprot.org/uniprot/Q9H7Z7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||GST C-terminal|||Glutaredoxin|||Helical|||Loss of prostaglandin-E synthase activity. Can bind glutathione-heme and exhibits PGH2 degradation activity.|||Lumenal|||Phosphoserine|||Prostaglandin E synthase 2|||Prostaglandin E synthase 2 truncated form|||Slightly decreased prostaglandin-E synthase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013127|||http://purl.uniprot.org/annotation/PRO_0000013128|||http://purl.uniprot.org/annotation/VAR_049494
http://togogenome.org/gene/9606:MYBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10243|||http://purl.uniprot.org/uniprot/Q495G0                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type|||HTH myb-type 1|||HTH myb-type 2|||HTH myb-type 3|||In isoform 2.|||Myb-like|||Myb-related protein A|||N6-acetyllysine|||Negative regulatory domain|||Transcriptional activation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197054|||http://purl.uniprot.org/annotation/VSP_042912
http://togogenome.org/gene/9606:HOXA11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31270                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Hox-A11|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200095
http://togogenome.org/gene/9606:LYSMD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWE4|||http://purl.uniprot.org/uniprot/F6SJM1|||http://purl.uniprot.org/uniprot/Q5XG99                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LysM|||LysM and putative peptidoglycan-binding domain-containing protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248013|||http://purl.uniprot.org/annotation/VAR_027200|||http://purl.uniprot.org/annotation/VAR_027201|||http://purl.uniprot.org/annotation/VAR_027202|||http://purl.uniprot.org/annotation/VSP_039883
http://togogenome.org/gene/9606:SUCLA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KS60|||http://purl.uniprot.org/uniprot/Q9P2R7|||http://purl.uniprot.org/uniprot/Q9Y4T0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-citrate lyase/succinyl-CoA ligase|||ATP-grasp|||Important for substrate specificity|||In MTDPS5.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033352|||http://purl.uniprot.org/annotation/VAR_013459|||http://purl.uniprot.org/annotation/VAR_046214|||http://purl.uniprot.org/annotation/VAR_046215|||http://purl.uniprot.org/annotation/VAR_046216|||http://purl.uniprot.org/annotation/VAR_070123|||http://purl.uniprot.org/annotation/VSP_006292
http://togogenome.org/gene/9606:RAB24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969Q5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Effector region|||Ras-related protein Rab-24|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121213
http://togogenome.org/gene/9606:ANO8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Anoctamin-8|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by FAM20C|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249003|||http://purl.uniprot.org/annotation/VSP_020351|||http://purl.uniprot.org/annotation/VSP_020352
http://togogenome.org/gene/9606:RPL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50914                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2 X 3 AA tandem repeats of K-[GA]-Q|||2-1|||2-2|||4 X 5 AA tandem repeats of Q-K-A-[PAS]-X|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL14|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132031|||http://purl.uniprot.org/annotation/VAR_006923|||http://purl.uniprot.org/annotation/VAR_013633|||http://purl.uniprot.org/annotation/VAR_013634|||http://purl.uniprot.org/annotation/VAR_013635|||http://purl.uniprot.org/annotation/VAR_013636|||http://purl.uniprot.org/annotation/VAR_013637|||http://purl.uniprot.org/annotation/VAR_014070|||http://purl.uniprot.org/annotation/VAR_047109
http://togogenome.org/gene/9606:DNASE1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92874                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Deoxyribonuclease-1-like 2|||Essential for enzymatic activity|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007286|||http://purl.uniprot.org/annotation/VSP_053879
http://togogenome.org/gene/9606:ZDHHC21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVQ6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Extracellular|||Helical|||Palmitoyltransferase ZDHHC21|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212908
http://togogenome.org/gene/9606:KRTAP19-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LHN2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 19-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223904|||http://purl.uniprot.org/annotation/VAR_053473|||http://purl.uniprot.org/annotation/VAR_053474
http://togogenome.org/gene/9606:GABRA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16445                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit alpha-6|||Helical|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000447|||http://purl.uniprot.org/annotation/VAR_036033|||http://purl.uniprot.org/annotation/VAR_036782|||http://purl.uniprot.org/annotation/VAR_036783
http://togogenome.org/gene/9606:CPA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1M3|||http://purl.uniprot.org/uniprot/Q9UI42                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase A4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase M14 carboxypeptidase A|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004357|||http://purl.uniprot.org/annotation/PRO_0000004358|||http://purl.uniprot.org/annotation/PRO_5014296863|||http://purl.uniprot.org/annotation/VAR_020393|||http://purl.uniprot.org/annotation/VAR_020394|||http://purl.uniprot.org/annotation/VAR_048594|||http://purl.uniprot.org/annotation/VAR_048595|||http://purl.uniprot.org/annotation/VSP_042894
http://togogenome.org/gene/9606:ACVR1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NER5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Activin receptor type-1C|||Cytoplasmic|||Extracellular|||GS|||Helical|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of response to NODAL and SMAD2 phosphorylation.|||Pro-apoptotic.|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042628|||http://purl.uniprot.org/annotation/VAR_041407|||http://purl.uniprot.org/annotation/VAR_041408|||http://purl.uniprot.org/annotation/VAR_041409|||http://purl.uniprot.org/annotation/VAR_041410|||http://purl.uniprot.org/annotation/VAR_041411|||http://purl.uniprot.org/annotation/VSP_051840|||http://purl.uniprot.org/annotation/VSP_051841|||http://purl.uniprot.org/annotation/VSP_051842
http://togogenome.org/gene/9606:KLK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2XQG6|||http://purl.uniprot.org/uniprot/Q9UKQ9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||Kallikrein-9|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027952|||http://purl.uniprot.org/annotation/PRO_5010137457|||http://purl.uniprot.org/annotation/VSP_057044|||http://purl.uniprot.org/annotation/VSP_057045
http://togogenome.org/gene/9606:OR51F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH61                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51F2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150753
http://togogenome.org/gene/9606:LAMB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0S4|||http://purl.uniprot.org/uniprot/B4DTV7|||http://purl.uniprot.org/uniprot/B7ZMJ6|||http://purl.uniprot.org/uniprot/C9JMJ0|||http://purl.uniprot.org/uniprot/O95127                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Domain I|||Domain II|||Domain alpha|||In isoform 2.|||In isoform 3.|||Interchain|||Laminin EGF-like|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 12|||Laminin EGF-like 13|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; truncated|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin IV type B|||Laminin N-terminal|||Laminin subunit beta-4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312857|||http://purl.uniprot.org/annotation/PRO_5002803305|||http://purl.uniprot.org/annotation/PRO_5002866694|||http://purl.uniprot.org/annotation/PRO_5002996572|||http://purl.uniprot.org/annotation/VAR_037588|||http://purl.uniprot.org/annotation/VAR_037589|||http://purl.uniprot.org/annotation/VAR_037590|||http://purl.uniprot.org/annotation/VAR_037591|||http://purl.uniprot.org/annotation/VAR_037592|||http://purl.uniprot.org/annotation/VAR_037593|||http://purl.uniprot.org/annotation/VAR_037594|||http://purl.uniprot.org/annotation/VAR_074174|||http://purl.uniprot.org/annotation/VSP_029913|||http://purl.uniprot.org/annotation/VSP_029914|||http://purl.uniprot.org/annotation/VSP_029915|||http://purl.uniprot.org/annotation/VSP_029916
http://togogenome.org/gene/9606:FAM186A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NE01                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Protein FAM186A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332201|||http://purl.uniprot.org/annotation/VAR_054419|||http://purl.uniprot.org/annotation/VAR_054420|||http://purl.uniprot.org/annotation/VAR_054421|||http://purl.uniprot.org/annotation/VAR_054422|||http://purl.uniprot.org/annotation/VAR_054423|||http://purl.uniprot.org/annotation/VAR_054424|||http://purl.uniprot.org/annotation/VAR_054425
http://togogenome.org/gene/9606:OBSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75147|||http://purl.uniprot.org/uniprot/Q9H8B3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Diminishes binding affinity for TTN.|||Disordered|||Fibronectin type-III|||Ig-like|||Ig-like 1|||Ig-like 10|||Ig-like 11|||Ig-like 12|||Ig-like 13|||Ig-like 14|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Ig-like 5|||Ig-like 6|||Ig-like 7|||Ig-like 8|||Ig-like 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with TTN|||Obscurin-like protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247959|||http://purl.uniprot.org/annotation/VSP_040784|||http://purl.uniprot.org/annotation/VSP_040785|||http://purl.uniprot.org/annotation/VSP_040786|||http://purl.uniprot.org/annotation/VSP_040787|||http://purl.uniprot.org/annotation/VSP_040788|||http://purl.uniprot.org/annotation/VSP_054755|||http://purl.uniprot.org/annotation/VSP_054756
http://togogenome.org/gene/9606:SSX2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16385|||http://purl.uniprot.org/uniprot/R9QTR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form the SSXT-SSX2 fusion protein|||Breakpoint for translocation to form the SSXT-SSX2 fusion protein (rare)|||Disordered|||In isoform 2.|||Interaction with RAB3IP|||Interaction with SSX2IP|||KRAB-related|||Phosphoserine|||Polar residues|||Protein SSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181829|||http://purl.uniprot.org/annotation/VSP_017595
http://togogenome.org/gene/9606:OR8D4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGM9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8D4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150661|||http://purl.uniprot.org/annotation/VAR_024118|||http://purl.uniprot.org/annotation/VAR_024119|||http://purl.uniprot.org/annotation/VAR_024120|||http://purl.uniprot.org/annotation/VAR_024121|||http://purl.uniprot.org/annotation/VAR_034257|||http://purl.uniprot.org/annotation/VAR_034258|||http://purl.uniprot.org/annotation/VAR_034259|||http://purl.uniprot.org/annotation/VAR_053245
http://togogenome.org/gene/9606:PER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15055                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CRY binding domain|||CSNK1E binding domain|||Disordered|||Important for protein stability|||In FASPS1; reduced in vitro phosphorylation by CSNK1E.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with PPARG|||LXXLL|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear export signal 3|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Period circadian protein homolog 2|||Phosphoserine|||Polar residues|||Restores CSNK1E-dependent phosphorylation of variant G-662.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162630|||http://purl.uniprot.org/annotation/VAR_024558|||http://purl.uniprot.org/annotation/VAR_029080|||http://purl.uniprot.org/annotation/VAR_036041|||http://purl.uniprot.org/annotation/VAR_051575|||http://purl.uniprot.org/annotation/VAR_051576|||http://purl.uniprot.org/annotation/VAR_051577|||http://purl.uniprot.org/annotation/VAR_051578|||http://purl.uniprot.org/annotation/VSP_021653|||http://purl.uniprot.org/annotation/VSP_021654
http://togogenome.org/gene/9606:PIP4K2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48426                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity; when associated with F-138.|||Abolishes catalytic activity; when associated with L-131.|||Acidic residues|||Disordered|||In isoform 2.|||Loss of kinase activity. Increases accumulation of lysosomal cholesterol.|||N-acetylalanine|||N6-acetyllysine|||No effect on kinase activity; increased accumulation of lysosomal cholesterol.|||PIPK|||Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha|||Phosphoserine|||Phosphothreonine|||Removed|||Required for interaction with PIP5K1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185465|||http://purl.uniprot.org/annotation/VAR_024565|||http://purl.uniprot.org/annotation/VAR_059764|||http://purl.uniprot.org/annotation/VSP_056458
http://togogenome.org/gene/9606:MDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V88                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Magnesium-dependent phosphatase 1|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068827|||http://purl.uniprot.org/annotation/VSP_015985|||http://purl.uniprot.org/annotation/VSP_015986|||http://purl.uniprot.org/annotation/VSP_015987|||http://purl.uniprot.org/annotation/VSP_015988
http://togogenome.org/gene/9606:DDX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R858|||http://purl.uniprot.org/uniprot/P26196                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to regulate RNA metabolism.|||Abolished helicase activity and ability to regulate RNA metabolism.|||Abolishes interaction with EDC3; when associated with A-320; A-323 and A-327.|||Abolishes interaction with EDC3; when associated with A-320; A-323 and A-331.|||Abolishes interaction with EDC3; when associated with A-320; A-327 and A-331.|||Abolishes interaction with EDC3; when associated with A-323; A-327 and A-331.|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Gyf binding|||Helicase ATP-binding|||Helicase C-terminal|||In CL-AA; abolishes interaction with PATL1 and reduces interaction with GIGYF1 and GIGYF2, but has no affect on interaction with EDC3, EIF4ENIF1 and LSM14A; when associated with A-324. In 4xmut; abolishes interaction with EDC3; when associated with A-324, A-349 and A-353.|||In CL-AA; abolishes interaction with PATL1 and reduces interaction with GIGYF1 and GIGYF2, but has no affect on interaction with EDC3, EIF4ENIF1 and LSM14A; when associated with A-328. In 4xmut; abolishes interaction with EDC3; when associated with A-328, A-349 and A-353.|||In IDDILF.|||In IDDILF; decreased P-body assembly.|||In IDDILF; decreased P-body assembly; decreased interaction with LSM14A; decreased interaction with LSM14B; decreased interaction with EIF4ENIF1/4E-T.|||In IDDILF; decreased P-body assembly; decreased interaction with LSM14A; decreased interaction with LSM14B; decreased interaction with EIF4ENIF1/4E-T; decreased interaction with PATL1.|||In LK-AA; abolishes interaction with PATL1 and reduces interaction with GIGYF1, GIGYF2, EDC3, EIF4ENIF1 and LSM14A; when associated with A-349. In 4xmut; abolishes interaction with EDC3; when associated with A-324; A-328 and A-349.|||In LK-AA; abolishes interaction with PATL1 and reduces interaction with GIGYF1, GIGYF2, EDC3, EIF4ENIF1 and LSM14A; when associated with A-353. In 4xmut; abolishes interaction with EDC3; when associated with A-324, A-328 and A-353.|||Phosphothreonine|||Polar residues|||Probable ATP-dependent RNA helicase DDX6|||Q motif|||RecA-like domain 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054983|||http://purl.uniprot.org/annotation/VAR_083368|||http://purl.uniprot.org/annotation/VAR_083369|||http://purl.uniprot.org/annotation/VAR_083370|||http://purl.uniprot.org/annotation/VAR_083371|||http://purl.uniprot.org/annotation/VAR_083372
http://togogenome.org/gene/9606:WASHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GWI9|||http://purl.uniprot.org/uniprot/F5GZ97|||http://purl.uniprot.org/uniprot/Q9Y3C0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-acetylmethionine|||WASH complex subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076201
http://togogenome.org/gene/9606:B3GALT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96024                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-galactosyltransferase 4|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219160
http://togogenome.org/gene/9606:SMPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9LUE8|||http://purl.uniprot.org/uniprot/E9LUE9|||http://purl.uniprot.org/uniprot/P17405|||http://purl.uniprot.org/uniprot/Q59EN6|||http://purl.uniprot.org/uniprot/Q8IUN0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished cleavage by CASP7.|||Abolishes constitutive secretion and decreases secretion in response to IL1B. No effect on lysosomal targeting. No effect on sphingomyelin phosphodiesterase activity. No effect on endolysosome location. Abolishes phosphorylation by PRKCD.|||Cleavage; by CASP7|||Disordered|||Does not affect cleavage by CASP7.|||Does not affect enzymatic activity.|||Helical|||In NPDA and NPDB.|||In NPDA and NPDB; also found in patients with an intermediate form.|||In NPDA and NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains very low enzyme activity.|||In NPDA.|||In NPDA; impairs enzyme activity; also in patients with an intermediate form.|||In NPDA; in 23% of NPDAAshkenazi Jewish patients; abolishes enzyme activity.|||In NPDA; in 32% of NPDAAshkenazi Jewish patients; nearly abolishes enzyme activity.|||In NPDA; intermediate form with clinical features of both Niemann-Pick disease types A and B.|||In NPDA; intermediate form.|||In NPDA; reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B.|||In NPDA; results in decreased activity; decreased stability.|||In NPDA; results in less than 0.5% of wild-type activity.|||In NPDA; results in loss of activity.|||In NPDA; severe decrease in activity; the mutant is highly unstable.|||In NPDA; strongly reduces enzyme activity; intermediate form with clinical features of both Niemann-Pick disease types A and B.|||In NPDA; unknown pathological significance.|||In NPDB and NPDA; also in patients with an intermediate form.|||In NPDB and NPDA; expresses protein level comparable to wild-type SMPD1 expressing cells; retains about 10% residual enzyme activity; loss of location to lysosome.|||In NPDB and NPDA; some patients have a NPDA/NPDB intermediate phenotype.|||In NPDB.|||In NPDB; 30% residual activity.|||In NPDB; abolishes enzyme activity.|||In NPDB; also in patients with an intermediate form.|||In NPDB; also in patients with an intermediate form; unknown pathological significance.|||In NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains 13% residual enzyme activity.|||In NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains 6.8% residual enzyme activity.|||In NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains no enzyme activity.|||In NPDB; expresses protein level comparable to wild-type SMPD1 expressing cells; retains very low enzyme activity; loss of location to lysosome.|||In NPDB; low sphingomyelin degradation rates.|||In NPDB; nearly abolishes enzyme activity; some patients have a NPDA/NPDB intermediate phenotype; loss of location to lysosome.|||In NPDB; reduces enzyme activity; some patients have a NPDA/NPDB intermediate phenotype.|||In NPDB; requires 2 nucleotide substitutions.|||In NPDB; results in 1-4% of wild type activity.|||In NPDB; results in 20% of wild-type activity.|||In NPDB; results in 64% of wild-type activity.|||In NPDB; results in loss of activity; the patient also carries mutation H-228 that has sufficient activity to account for the Niemann-Pick disease type B phenotype.|||In NPDB; some patients have a NPDA/NPDB intermediate phenotype.|||In NPDB; sphingomyelinase activity is decreased to 4% of wild-type activity; no effect on protein abundance; no effect on protein localization to lysosome; no effect on protein localization to extracellular space.|||In NPDB; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of sphingomyelin phosphodiesterase activity. Loss of secretion.|||N-linked (GlcNAc...) asparagine|||No effect on sphingomyelin phosphodiesterase activity. No effect on endolysosome location. No effect on phosphorylation by PRKCD.|||No effect on sphingomyelin phosphodiesterase activity. No effect on secretion.|||No effect on sphingomyelin phosphodiesterase activity. No effect on subcellular location. No effect on phosphorylation by PRKCD.|||Phosphoserine; by PKC/PRKCD|||Reduces protein levels. Reduces sphingomyelin phosphodiesterase activity. No effect on secretion.|||Reduces sphingomyelin phosphodiesterase activity. No effect on secretion.|||Saposin B-type|||Sphingomyelin phosphodiesterase|||Sphingomyelin phosphodiesterase, processed form ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002323|||http://purl.uniprot.org/annotation/PRO_0000456684|||http://purl.uniprot.org/annotation/VAR_005058|||http://purl.uniprot.org/annotation/VAR_005059|||http://purl.uniprot.org/annotation/VAR_005060|||http://purl.uniprot.org/annotation/VAR_005061|||http://purl.uniprot.org/annotation/VAR_005062|||http://purl.uniprot.org/annotation/VAR_005063|||http://purl.uniprot.org/annotation/VAR_005064|||http://purl.uniprot.org/annotation/VAR_005065|||http://purl.uniprot.org/annotation/VAR_005066|||http://purl.uniprot.org/annotation/VAR_005067|||http://purl.uniprot.org/annotation/VAR_005068|||http://purl.uniprot.org/annotation/VAR_011387|||http://purl.uniprot.org/annotation/VAR_011388|||http://purl.uniprot.org/annotation/VAR_015287|||http://purl.uniprot.org/annotation/VAR_015288|||http://purl.uniprot.org/annotation/VAR_015289|||http://purl.uniprot.org/annotation/VAR_015290|||http://purl.uniprot.org/annotation/VAR_015291|||http://purl.uniprot.org/annotation/VAR_015292|||http://purl.uniprot.org/annotation/VAR_015293|||http://purl.uniprot.org/annotation/VAR_038191|||http://purl.uniprot.org/annotation/VAR_054642|||http://purl.uniprot.org/annotation/VAR_054643|||http://purl.uniprot.org/annotation/VAR_054644|||http://purl.uniprot.org/annotation/VAR_060870|||http://purl.uniprot.org/annotation/VAR_060871|||http://purl.uniprot.org/annotation/VAR_060872|||http://purl.uniprot.org/annotation/VAR_060873|||http://purl.uniprot.org/annotation/VAR_060874|||http://purl.uniprot.org/annotation/VAR_060875|||http://purl.uniprot.org/annotation/VAR_060876|||http://purl.uniprot.org/annotation/VAR_060877|||http://purl.uniprot.org/annotation/VAR_060878|||http://purl.uniprot.org/annotation/VAR_060879|||http://purl.uniprot.org/annotation/VAR_060880|||http://purl.uniprot.org/annotation/VAR_060881|||http://purl.uniprot.org/annotation/VAR_060882|||http://purl.uniprot.org/annotation/VAR_060883|||http://purl.uniprot.org/annotation/VAR_060884|||http://purl.uniprot.org/annotation/VAR_060885|||http://purl.uniprot.org/annotation/VAR_060886|||http://purl.uniprot.org/annotation/VAR_060887|||http://purl.uniprot.org/annotation/VAR_060888|||http://purl.uniprot.org/annotation/VAR_060889|||http://purl.uniprot.org/annotation/VAR_060890|||http://purl.uniprot.org/annotation/VAR_060891|||http://purl.uniprot.org/annotation/VAR_060892|||http://purl.uniprot.org/annotation/VAR_060893|||http://purl.uniprot.org/annotation/VAR_060894|||http://purl.uniprot.org/annotation/VAR_060895|||http://purl.uniprot.org/annotation/VAR_060896|||http://purl.uniprot.org/annotation/VAR_060897|||http://purl.uniprot.org/annotation/VAR_060898|||http://purl.uniprot.org/annotation/VAR_060899|||http://purl.uniprot.org/annotation/VAR_060900|||http://purl.uniprot.org/annotation/VAR_060901|||http://purl.uniprot.org/annotation/VAR_060902|||http://purl.uniprot.org/annotation/VAR_060903|||http://purl.uniprot.org/annotation/VAR_060904|||http://purl.uniprot.org/annotation/VAR_060905|||http://purl.uniprot.org/annotation/VAR_060906|||http://purl.uniprot.org/annotation/VAR_060907|||http://purl.uniprot.org/annotation/VAR_060908|||http://purl.uniprot.org/annotation/VAR_060909|||http://purl.uniprot.org/annotation/VAR_060910|||http://purl.uniprot.org/annotation/VAR_060911|||http://purl.uniprot.org/annotation/VAR_060912|||http://purl.uniprot.org/annotation/VAR_060913|||http://purl.uniprot.org/annotation/VAR_060914|||http://purl.uniprot.org/annotation/VAR_060915|||http://purl.uniprot.org/annotation/VAR_060916|||http://purl.uniprot.org/annotation/VAR_060917|||http://purl.uniprot.org/annotation/VAR_060918|||http://purl.uniprot.org/annotation/VAR_060919|||http://purl.uniprot.org/annotation/VAR_060920|||http://purl.uniprot.org/annotation/VAR_060921|||http://purl.uniprot.org/annotation/VAR_060922|||http://purl.uniprot.org/annotation/VAR_060923|||http://purl.uniprot.org/annotation/VAR_060924|||http://purl.uniprot.org/annotation/VAR_060925|||http://purl.uniprot.org/annotation/VAR_060926|||http://purl.uniprot.org/annotation/VAR_060927|||http://purl.uniprot.org/annotation/VAR_060928|||http://purl.uniprot.org/annotation/VAR_060929|||http://purl.uniprot.org/annotation/VAR_060930|||http://purl.uniprot.org/annotation/VAR_060931|||http://purl.uniprot.org/annotation/VAR_060932|||http://purl.uniprot.org/annotation/VAR_060933|||http://purl.uniprot.org/annotation/VAR_068435|||http://purl.uniprot.org/annotation/VAR_068436|||http://purl.uniprot.org/annotation/VAR_068437|||http://purl.uniprot.org/annotation/VAR_068438|||http://purl.uniprot.org/annotation/VAR_068439|||http://purl.uniprot.org/annotation/VAR_068440|||http://purl.uniprot.org/annotation/VAR_068441|||http://purl.uniprot.org/annotation/VAR_075322|||http://purl.uniprot.org/annotation/VAR_075323|||http://purl.uniprot.org/annotation/VAR_075324|||http://purl.uniprot.org/annotation/VAR_075325|||http://purl.uniprot.org/annotation/VAR_075326|||http://purl.uniprot.org/annotation/VAR_075327|||http://purl.uniprot.org/annotation/VAR_075328|||http://purl.uniprot.org/annotation/VAR_075329|||http://purl.uniprot.org/annotation/VAR_075330|||http://purl.uniprot.org/annotation/VAR_075331|||http://purl.uniprot.org/annotation/VAR_075332|||http://purl.uniprot.org/annotation/VAR_075333|||http://purl.uniprot.org/annotation/VAR_075334|||http://purl.uniprot.org/annotation/VAR_075335|||http://purl.uniprot.org/annotation/VAR_077311|||http://purl.uniprot.org/annotation/VAR_077312|||http://purl.uniprot.org/annotation/VAR_077313|||http://purl.uniprot.org/annotation/VAR_077314|||http://purl.uniprot.org/annotation/VAR_077315|||http://purl.uniprot.org/annotation/VAR_077316|||http://purl.uniprot.org/annotation/VAR_077317|||http://purl.uniprot.org/annotation/VAR_077318|||http://purl.uniprot.org/annotation/VAR_077319|||http://purl.uniprot.org/annotation/VAR_077320|||http://purl.uniprot.org/annotation/VAR_077321|||http://purl.uniprot.org/annotation/VAR_077322|||http://purl.uniprot.org/annotation/VAR_077323|||http://purl.uniprot.org/annotation/VAR_077324|||http://purl.uniprot.org/annotation/VAR_077325|||http://purl.uniprot.org/annotation/VAR_077326|||http://purl.uniprot.org/annotation/VAR_080641|||http://purl.uniprot.org/annotation/VAR_080642|||http://purl.uniprot.org/annotation/VSP_000331|||http://purl.uniprot.org/annotation/VSP_000332|||http://purl.uniprot.org/annotation/VSP_000333|||http://purl.uniprot.org/annotation/VSP_046964
http://togogenome.org/gene/9606:MEGF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes tyrosine phosphorylation. Unable to enhance cell proliferation.|||Cytoplasmic|||Disordered|||Does not interact with GULP1; when associated with A-927.|||Does not interact with GULP1; when associated with A-930.|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||EMI|||Enhances cell proliferation.|||Extracellular|||Found in a patient with a late-onset mild myopathy and still ambulatory in late adulthood; unknown pathological significance.|||Helical|||In CMYP10B and CMYP10A; impaired tyrosine phosphorylation; no effect on cell membrane location; impairs binding to C1q; reduced apoptotic cell engulfement by astrocytes by 50%; reduced myoblast migration and proliferation; decreased interaction with NOTCH1; no effect on NOTCH1 nuclear location.|||In CMYP10B; slightly decreased tyrosine phosphorylation; slightly reduced apoptotic cell engulfement by astrocytes; no effect on cell membrane location; no effect on binding to C1q; no effect on myoblasts migration and proliferation; no effect on interaction with NOTCH1.|||In CMYP10B; unknown pathological significance.|||In CMYP10B; unknown pathological significance; impaired tyrosine phosphorylation.|||In isoform 2.|||Multiple epidermal growth factor-like domains protein 10|||N-linked (GlcNAc...) asparagine|||Necessary for formation of large intracellular vacuoles|||Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion pattern|||Phosphotyrosine; by SRC|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309732|||http://purl.uniprot.org/annotation/VAR_036988|||http://purl.uniprot.org/annotation/VAR_036989|||http://purl.uniprot.org/annotation/VAR_046377|||http://purl.uniprot.org/annotation/VAR_067469|||http://purl.uniprot.org/annotation/VAR_067470|||http://purl.uniprot.org/annotation/VAR_067471|||http://purl.uniprot.org/annotation/VAR_081905|||http://purl.uniprot.org/annotation/VAR_088236|||http://purl.uniprot.org/annotation/VAR_088237|||http://purl.uniprot.org/annotation/VAR_088238|||http://purl.uniprot.org/annotation/VSP_029244|||http://purl.uniprot.org/annotation/VSP_029245
http://togogenome.org/gene/9606:GREB1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C091                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Able to rescue renal hypoplasia in zebrafish morphants.|||Basic and acidic residues|||Disordered|||GREB1-like protein|||Helical|||In DFNA80.|||In DFNA80; unknown pathological significance.|||In RHDA3.|||In RHDA3; probable loss of function; does not rescue renal hypoplasia in zebrafish morphants.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320946|||http://purl.uniprot.org/annotation/VAR_080091|||http://purl.uniprot.org/annotation/VAR_080092|||http://purl.uniprot.org/annotation/VAR_080093|||http://purl.uniprot.org/annotation/VAR_080094|||http://purl.uniprot.org/annotation/VAR_080095|||http://purl.uniprot.org/annotation/VAR_080096|||http://purl.uniprot.org/annotation/VAR_080097|||http://purl.uniprot.org/annotation/VAR_080098|||http://purl.uniprot.org/annotation/VAR_080099|||http://purl.uniprot.org/annotation/VAR_080100|||http://purl.uniprot.org/annotation/VAR_080101|||http://purl.uniprot.org/annotation/VAR_080102|||http://purl.uniprot.org/annotation/VAR_080103|||http://purl.uniprot.org/annotation/VAR_080104|||http://purl.uniprot.org/annotation/VAR_080105|||http://purl.uniprot.org/annotation/VAR_080106|||http://purl.uniprot.org/annotation/VAR_080107|||http://purl.uniprot.org/annotation/VAR_080108|||http://purl.uniprot.org/annotation/VAR_080109|||http://purl.uniprot.org/annotation/VAR_080110|||http://purl.uniprot.org/annotation/VAR_080111|||http://purl.uniprot.org/annotation/VAR_080112|||http://purl.uniprot.org/annotation/VAR_080113|||http://purl.uniprot.org/annotation/VAR_080114|||http://purl.uniprot.org/annotation/VAR_080115|||http://purl.uniprot.org/annotation/VAR_080116|||http://purl.uniprot.org/annotation/VAR_080117|||http://purl.uniprot.org/annotation/VAR_080118|||http://purl.uniprot.org/annotation/VAR_080119|||http://purl.uniprot.org/annotation/VAR_080120|||http://purl.uniprot.org/annotation/VAR_080121|||http://purl.uniprot.org/annotation/VAR_080122|||http://purl.uniprot.org/annotation/VAR_085591|||http://purl.uniprot.org/annotation/VAR_085592|||http://purl.uniprot.org/annotation/VAR_085593|||http://purl.uniprot.org/annotation/VSP_031762|||http://purl.uniprot.org/annotation/VSP_031764|||http://purl.uniprot.org/annotation/VSP_031765
http://togogenome.org/gene/9606:SLC8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32418|||http://purl.uniprot.org/uniprot/Q4QQH3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Calx-beta|||Calx-beta 1|||Calx-beta 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 3, isoform 7 and isoform 10.|||In isoform 3.|||In isoform 7 and isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 1|||Sodium/calcium exchanger membrane region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019379|||http://purl.uniprot.org/annotation/VAR_014847|||http://purl.uniprot.org/annotation/VSP_003397|||http://purl.uniprot.org/annotation/VSP_003398|||http://purl.uniprot.org/annotation/VSP_003399|||http://purl.uniprot.org/annotation/VSP_003400
http://togogenome.org/gene/9606:CEP350                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT06                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes recruitment of PPARA to specific nuclear foci. No effect on interaction with PPARA (in vitro).|||Basic and acidic residues|||CAP-Gly|||Centrosome-associated protein 350|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233291|||http://purl.uniprot.org/annotation/VAR_026126|||http://purl.uniprot.org/annotation/VAR_048671|||http://purl.uniprot.org/annotation/VAR_059202|||http://purl.uniprot.org/annotation/VAR_059203|||http://purl.uniprot.org/annotation/VAR_059204|||http://purl.uniprot.org/annotation/VAR_059205|||http://purl.uniprot.org/annotation/VAR_061092
http://togogenome.org/gene/9606:CFAP276                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5A4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 276|||Disordered|||Found in patients with an intermediate form of Charcot-Marie-Tooth disease; does not affect subcellular location; reduced protein expression; increased intracellular Ca(2+).|||In isoform 2.|||Probable disease-associated variant found in patients with a form of Charcot-Marie-Tooth disease leading to demyelinating form; does not affect subcellular location; increased protein expression; increased aggregation in vesicles; increased intracellular Ca(2+); decreased mitochondrial Ca(2+).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000303065|||http://purl.uniprot.org/annotation/VAR_082033|||http://purl.uniprot.org/annotation/VAR_082034|||http://purl.uniprot.org/annotation/VSP_027993
http://togogenome.org/gene/9606:TLR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9N9|||http://purl.uniprot.org/uniprot/Q9NYK1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In IMD74; no enhanced expression after stimulation by imiquimod; defective up-regulation of type IIFN-related genes; decreased expression of IFNG.|||In SLEB17; increased NFKB1 activation after stimulation with cGMP.|||In SLEB17; increased NFKB1 activation after stimulation with guanosine and ssRNA.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 25|||LRR 26|||LRR 27|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||N-linked (GlcNAc...) asparagine|||TIR|||Toll-like receptor 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034733|||http://purl.uniprot.org/annotation/VAR_024665|||http://purl.uniprot.org/annotation/VAR_034554|||http://purl.uniprot.org/annotation/VAR_084629|||http://purl.uniprot.org/annotation/VAR_087534|||http://purl.uniprot.org/annotation/VAR_087535|||http://purl.uniprot.org/annotation/VAR_087536
http://togogenome.org/gene/9606:RALA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11233                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL|||Abolished monoglucosylation by P.sordellii toxin TcsL.|||Converts geranyl-geranylation to farnesylation. No effect on membrane localization. Fails to deflect GGTI-induced apoptosis of adherent cell cultures, but rescues anchorage-independent cell proliferation.|||Cysteine methyl ester|||Decreased localization to mitochondrion. Loss of function in mitochondrial fission.|||Effector region|||Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with L-72.|||Impaired cytokinesis, as shown by increased number of binucleate cells. Impaired cytokinesis; when associated with N-49 or 1-M--S-11. No effect on cytokinesis; when associated with E-49.|||Impaired cytokinesis, as shown by increased number of binucleate cells. No effect on cytokinesis; when associated with V-23. Decreased interaction with EXOC2 and EXOC8; when associated with V-23.|||Impaired cytokinesis, as shown by increased number of binucleate cells. No effect on interaction with EXOC2 and EXOC8. No effect on cytokinesis; when associated with R-38 or W-48. Decreased interaction with EXOC2 and EXOC8; when associated with R-38 or W-48.|||In HINCONS.|||In HINCONS; decreased GTPase activity; decreased RALA effector binding.|||In HINCONS; decreased GTPase activity; increased RALA effector binding.|||In HINCONS; unknown pathological significance.|||Increased localization to mitochondrion.|||Loss of geranylgeranylation and membrane localization.|||No effect on cytokinesis. Impaired cytokinesis, as shown by increased number of binucleate cells; when associated with L-72.|||No effect on cytokinesis; when associated with L-72.|||No effect on interaction with EXOC8.|||Phosphoserine; by AURKA|||Ras-related protein Ral-A|||Removed in mature form|||S-geranylgeranyl cysteine|||Strongly reduces interaction with EXOC8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082693|||http://purl.uniprot.org/annotation/PRO_0000281344|||http://purl.uniprot.org/annotation/VAR_085759|||http://purl.uniprot.org/annotation/VAR_085760|||http://purl.uniprot.org/annotation/VAR_085761|||http://purl.uniprot.org/annotation/VAR_085762|||http://purl.uniprot.org/annotation/VAR_085763|||http://purl.uniprot.org/annotation/VAR_085764|||http://purl.uniprot.org/annotation/VAR_085765
http://togogenome.org/gene/9606:CYTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRR1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cytokine-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020838|||http://purl.uniprot.org/annotation/VAR_050940|||http://purl.uniprot.org/annotation/VAR_050941
http://togogenome.org/gene/9606:NDUFB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95139                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylthreonine|||N6-acetyllysine|||NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118807|||http://purl.uniprot.org/annotation/VSP_045233
http://togogenome.org/gene/9606:IGF2BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKT5|||http://purl.uniprot.org/uniprot/F8W930|||http://purl.uniprot.org/uniprot/Q9Y6M1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 6.|||Insulin-like growth factor 2 mRNA-binding protein 2|||K Homology|||KH 1|||KH 2|||KH 3|||KH 4|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA; when associated with 445-E-E-446. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 445-E-E-446.|||Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA; when associated with 527-E-E-528. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 527-E-E-528.|||Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding, accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA; when associated with E-211. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; 445-E-E-445 and 526-E-E-527.|||Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding, accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA; when associated with E-292. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-292; 445-E-E-446 and 526-E-E-527.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244496|||http://purl.uniprot.org/annotation/VSP_036550|||http://purl.uniprot.org/annotation/VSP_036552|||http://purl.uniprot.org/annotation/VSP_036553|||http://purl.uniprot.org/annotation/VSP_043699
http://togogenome.org/gene/9606:SEPTIN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99719|||http://purl.uniprot.org/uniprot/X5DNA9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  G1 motif|||G3 motif|||G4 motif|||Important for dimerization|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Septin-5|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173521|||http://purl.uniprot.org/annotation/VSP_042689|||http://purl.uniprot.org/annotation/VSP_042690
http://togogenome.org/gene/9606:HSD17B8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92506                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyacyl-CoA dehydrogenase|||Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.|||In a breast cancer sample; somatic mutation.|||N6-succinyllysine|||No effect on the ability to restore growth of an OAR1-deficient yeast mutant.|||Phosphoserine|||Proton acceptor|||Reduced NADH-dependent reductase activity with acetoacetyl-CoA. Reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Increases NADPH-dependent reductase activities. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.|||Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054598|||http://purl.uniprot.org/annotation/VAR_035844|||http://purl.uniprot.org/annotation/VAR_052316
http://togogenome.org/gene/9606:CCDC159                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7I6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 159|||Disordered|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332996|||http://purl.uniprot.org/annotation/VAR_043032|||http://purl.uniprot.org/annotation/VSP_059513|||http://purl.uniprot.org/annotation/VSP_059514|||http://purl.uniprot.org/annotation/VSP_059515
http://togogenome.org/gene/9606:ADAM21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKJ8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 21|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029108|||http://purl.uniprot.org/annotation/PRO_0000029109
http://togogenome.org/gene/9606:IRAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51617                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Completely abolishes auto-phosphorylation in the kinase domain.|||Death|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interleukin-1 receptor-associated kinase 1|||Loss of kinase activity.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by IRAK4|||Phosphothreonine; by PKC/PRKCI|||Polar residues|||Pro residues|||ProST region|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086030|||http://purl.uniprot.org/annotation/VAR_040573|||http://purl.uniprot.org/annotation/VAR_040574|||http://purl.uniprot.org/annotation/VAR_040575|||http://purl.uniprot.org/annotation/VAR_040576|||http://purl.uniprot.org/annotation/VAR_040577|||http://purl.uniprot.org/annotation/VAR_040578|||http://purl.uniprot.org/annotation/VAR_040579|||http://purl.uniprot.org/annotation/VAR_040580|||http://purl.uniprot.org/annotation/VAR_051629|||http://purl.uniprot.org/annotation/VAR_051630|||http://purl.uniprot.org/annotation/VAR_051631|||http://purl.uniprot.org/annotation/VSP_011849|||http://purl.uniprot.org/annotation/VSP_011850|||http://purl.uniprot.org/annotation/VSP_011851|||http://purl.uniprot.org/annotation/VSP_041950
http://togogenome.org/gene/9606:EEF1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAR6|||http://purl.uniprot.org/uniprot/P29692                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Catalytic (GEF)|||Disordered|||Elongation factor 1 beta central acidic region eukaryote|||Elongation factor 1-delta|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leucine-zipper|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Removed|||Translation elongation factor EF1B beta/delta subunit guanine nucleotide exchange                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155046|||http://purl.uniprot.org/annotation/VSP_037884|||http://purl.uniprot.org/annotation/VSP_043812|||http://purl.uniprot.org/annotation/VSP_045960
http://togogenome.org/gene/9606:FCGR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12314                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreases cell membrane expression by 50% in absence of FCER1G.|||Disordered|||Extracellular|||Helical|||High affinity immunoglobulin gamma Fc receptor I|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In isoform 2.|||Increases cell membrane expression in absence of FCER1G.|||Interaction with EPB41L2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015139|||http://purl.uniprot.org/annotation/VAR_019522|||http://purl.uniprot.org/annotation/VSP_002637
http://togogenome.org/gene/9606:GLP2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTS7|||http://purl.uniprot.org/uniprot/B2RAN4|||http://purl.uniprot.org/uniprot/O95838                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||Glucagon-like peptide 2 receptor|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012838|||http://purl.uniprot.org/annotation/VAR_033967|||http://purl.uniprot.org/annotation/VAR_033968|||http://purl.uniprot.org/annotation/VAR_033969
http://togogenome.org/gene/9606:POTED                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YR6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Disordered|||POTE ankyrin domain family member D|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066913|||http://purl.uniprot.org/annotation/VAR_016242|||http://purl.uniprot.org/annotation/VAR_016243|||http://purl.uniprot.org/annotation/VAR_064765
http://togogenome.org/gene/9606:BLZF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2G9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Essential for interaction with GORASP2|||Golgin-45|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tankyrase-binding motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087539|||http://purl.uniprot.org/annotation/VAR_028142|||http://purl.uniprot.org/annotation/VAR_028143|||http://purl.uniprot.org/annotation/VSP_011186|||http://purl.uniprot.org/annotation/VSP_011187
http://togogenome.org/gene/9606:GRIN3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCU5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with schizophrenia; unknown pathological significance.|||GIT1-binding|||Glutamate receptor ionotropic, NMDA 3A|||Helical|||N-linked (GlcNAc...) asparagine|||PPP2CB binding site|||Probable disease-associated variant found in a patient with schizophrenia.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011568|||http://purl.uniprot.org/annotation/VAR_019672|||http://purl.uniprot.org/annotation/VAR_019673|||http://purl.uniprot.org/annotation/VAR_019674|||http://purl.uniprot.org/annotation/VAR_019675|||http://purl.uniprot.org/annotation/VAR_047150|||http://purl.uniprot.org/annotation/VAR_079892|||http://purl.uniprot.org/annotation/VAR_079893|||http://purl.uniprot.org/annotation/VAR_079894|||http://purl.uniprot.org/annotation/VAR_079895|||http://purl.uniprot.org/annotation/VAR_079896|||http://purl.uniprot.org/annotation/VAR_079897|||http://purl.uniprot.org/annotation/VAR_079898|||http://purl.uniprot.org/annotation/VAR_079899|||http://purl.uniprot.org/annotation/VAR_079900|||http://purl.uniprot.org/annotation/VAR_079901|||http://purl.uniprot.org/annotation/VAR_079902|||http://purl.uniprot.org/annotation/VAR_079903|||http://purl.uniprot.org/annotation/VAR_079904|||http://purl.uniprot.org/annotation/VAR_079905|||http://purl.uniprot.org/annotation/VAR_079906|||http://purl.uniprot.org/annotation/VAR_079907|||http://purl.uniprot.org/annotation/VAR_079908
http://togogenome.org/gene/9606:FGFR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Q6|||http://purl.uniprot.org/uniprot/A0A3B3ISD1|||http://purl.uniprot.org/uniprot/P11362                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with PLCG1 and SHB. Decreases phosphorylation of FRS2, activation of RAS and MAP kinase signaling and stimulation of cell proliferation.|||Abolishes interaction with PLCG1.|||Acidic residues|||Breakpoint for translocation to form CEP43-FGFR1 or FGFR1-CEP43 fusion proteins|||Breakpoint for translocation to form CNTRL-FGFR1 OR FGFR1-CNTRL fusion proteins|||Breakpoint for translocation to form FGFR1OP2-FGFR1|||Cytoplasmic|||Disordered|||Extracellular|||Fibroblast growth factor receptor|||Fibroblast growth factor receptor 1|||Helical|||Heparin-binding|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In ECCL; somatic mutation.|||In ECCL; somatic mutation; activating mutation; strongly increased speed of the first autophosphorylation and loss of the normal sequential order of autophosphorylation.|||In HH2.|||In HH2; also found in a family member with isolated anosmia.|||In HH2; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity.|||In HH2; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity.|||In HH2; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression.|||In HH2; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD.|||In HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in DUSP6.|||In HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in FLRT3.|||In HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in SPRY4.|||In HH2; phenotype consistent with Kallmann syndrome; the patient also carries a splice site mutation in NSMF.|||In HH2; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism.|||In HH2; some patients also carry GNRHR mutations.|||In HH2; some patients also carry GNRHR mutations; impairs tyrosine kinase activity.|||In HH2; some patients also carry KISS1R mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression.|||In HH2; some patients also carry PROKR2 and GNRH1 mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression.|||In HH2; the patient also carries a rare variant in FGF8.|||In HH2; unknown pathological significance.|||In HH2; with bimanual synkinesis.|||In HH2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones.|||In HH2; with cleft palate.|||In HH2; with or without anosmia.|||In HH2; with or without anosmia; also found in a family member with isolated anosmia; may impair proper folding.|||In HH2; with or without anosmia; results in Kallmann syndrome in the presence of HS6ST1 mutation TRP-306; reduces receptor affinity for fibroblast growth factor.|||In HH2; with severe ear anomalies.|||In HRTFDS.|||In OGD.|||In OGD; elevated basal activity and increased FGF2-mediated activity.|||In PS and JWS.|||In TRIGNO1.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a lung bronchoalveolar carcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 10, isoform 11, isoform 12 and isoform 13.|||In isoform 14, isoform 15, isoform 18, isoform 19 and isoform 21.|||In isoform 16.|||In isoform 17 and isoform 18.|||In isoform 19.|||In isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13.|||In isoform 20.|||In isoform 21.|||In isoform 3.|||In isoform 4, isoform 5, isoform 8, isoform 9, isoform 12 and isoform 13.|||In isoform 6, isoform 7, isoform 8, isoform 9, isoform 15, isoform 17 and isoform 18.|||Loss of kinase activity.|||Mediates interaction with PLCG1 and SHB|||N-linked (GlcNAc...) asparagine|||No effect on kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-654.|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-653.|||Strongly reduced autophosphorylation in response to FGF signaling. No effect on in vitro kinase activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016780|||http://purl.uniprot.org/annotation/PRO_5014239310|||http://purl.uniprot.org/annotation/PRO_5039987948|||http://purl.uniprot.org/annotation/VAR_004111|||http://purl.uniprot.org/annotation/VAR_017885|||http://purl.uniprot.org/annotation/VAR_017886|||http://purl.uniprot.org/annotation/VAR_017887|||http://purl.uniprot.org/annotation/VAR_017888|||http://purl.uniprot.org/annotation/VAR_017889|||http://purl.uniprot.org/annotation/VAR_017890|||http://purl.uniprot.org/annotation/VAR_017891|||http://purl.uniprot.org/annotation/VAR_017892|||http://purl.uniprot.org/annotation/VAR_019290|||http://purl.uniprot.org/annotation/VAR_019291|||http://purl.uniprot.org/annotation/VAR_019292|||http://purl.uniprot.org/annotation/VAR_030968|||http://purl.uniprot.org/annotation/VAR_030969|||http://purl.uniprot.org/annotation/VAR_030970|||http://purl.uniprot.org/annotation/VAR_030971|||http://purl.uniprot.org/annotation/VAR_030972|||http://purl.uniprot.org/annotation/VAR_030973|||http://purl.uniprot.org/annotation/VAR_030974|||http://purl.uniprot.org/annotation/VAR_030975|||http://purl.uniprot.org/annotation/VAR_030976|||http://purl.uniprot.org/annotation/VAR_030977|||http://purl.uniprot.org/annotation/VAR_030978|||http://purl.uniprot.org/annotation/VAR_030979|||http://purl.uniprot.org/annotation/VAR_030980|||http://purl.uniprot.org/annotation/VAR_030981|||http://purl.uniprot.org/annotation/VAR_030982|||http://purl.uniprot.org/annotation/VAR_030983|||http://purl.uniprot.org/annotation/VAR_030984|||http://purl.uniprot.org/annotation/VAR_030985|||http://purl.uniprot.org/annotation/VAR_030986|||http://purl.uniprot.org/annotation/VAR_030987|||http://purl.uniprot.org/annotation/VAR_030988|||http://purl.uniprot.org/annotation/VAR_030989|||http://purl.uniprot.org/annotation/VAR_030990|||http://purl.uniprot.org/annotation/VAR_030991|||http://purl.uniprot.org/annotation/VAR_030992|||http://purl.uniprot.org/annotation/VAR_030993|||http://purl.uniprot.org/annotation/VAR_030994|||http://purl.uniprot.org/annotation/VAR_030995|||http://purl.uniprot.org/annotation/VAR_030996|||http://purl.uniprot.org/annotation/VAR_030997|||http://purl.uniprot.org/annotation/VAR_030998|||http://purl.uniprot.org/annotation/VAR_030999|||http://purl.uniprot.org/annotation/VAR_031000|||http://purl.uniprot.org/annotation/VAR_031001|||http://purl.uniprot.org/annotation/VAR_031002|||http://purl.uniprot.org/annotation/VAR_031003|||http://purl.uniprot.org/annotation/VAR_031004|||http://purl.uniprot.org/annotation/VAR_031005|||http://purl.uniprot.org/annotation/VAR_031006|||http://purl.uniprot.org/annotation/VAR_031007|||http://purl.uniprot.org/annotation/VAR_031008|||http://purl.uniprot.org/annotation/VAR_031009|||http://purl.uniprot.org/annotation/VAR_031010|||http://purl.uniprot.org/annotation/VAR_042201|||http://purl.uniprot.org/annotation/VAR_042202|||http://purl.uniprot.org/annotation/VAR_042203|||http://purl.uniprot.org/annotation/VAR_069288|||http://purl.uniprot.org/annotation/VAR_069289|||http://purl.uniprot.org/annotation/VAR_069290|||http://purl.uniprot.org/annotation/VAR_069291|||http://purl.uniprot.org/annotation/VAR_069292|||http://purl.uniprot.org/annotation/VAR_069293|||http://purl.uniprot.org/annotation/VAR_069294|||http://purl.uniprot.org/annotation/VAR_069954|||http://purl.uniprot.org/annotation/VAR_069955|||http://purl.uniprot.org/annotation/VAR_069956|||http://purl.uniprot.org/annotation/VAR_069957|||http://purl.uniprot.org/annotation/VAR_069958|||http://purl.uniprot.org/annotation/VAR_069959|||http://purl.uniprot.org/annotation/VAR_070851|||http://purl.uniprot.org/annotation/VAR_070852|||http://purl.uniprot.org/annotation/VAR_070853|||http://purl.uniprot.org/annotation/VAR_070854|||http://purl.uniprot.org/annotation/VAR_070855|||http://purl.uniprot.org/annotation/VAR_070856|||http://purl.uniprot.org/annotation/VAR_071460|||http://purl.uniprot.org/annotation/VAR_072993|||http://purl.uniprot.org/annotation/VAR_072994|||http://purl.uniprot.org/annotation/VAR_072995|||http://purl.uniprot.org/annotation/VAR_074012|||http://purl.uniprot.org/annotation/VAR_074013|||http://purl.uniprot.org/annotation/VAR_074014|||http://purl.uniprot.org/annotation/VAR_075853|||http://purl.uniprot.org/annotation/VAR_075854|||http://purl.uniprot.org/annotation/VAR_075855|||http://purl.uniprot.org/annotation/VAR_080328|||http://purl.uniprot.org/annotation/VAR_080329|||http://purl.uniprot.org/annotation/VAR_080330|||http://purl.uniprot.org/annotation/VAR_082843|||http://purl.uniprot.org/annotation/VSP_002957|||http://purl.uniprot.org/annotation/VSP_002958|||http://purl.uniprot.org/annotation/VSP_002959|||http://purl.uniprot.org/annotation/VSP_002960|||http://purl.uniprot.org/annotation/VSP_009836|||http://purl.uniprot.org/annotation/VSP_009837|||http://purl.uniprot.org/annotation/VSP_009838|||http://purl.uniprot.org/annotation/VSP_009839|||http://purl.uniprot.org/annotation/VSP_009840|||http://purl.uniprot.org/annotation/VSP_009841|||http://purl.uniprot.org/annotation/VSP_009842|||http://purl.uniprot.org/annotation/VSP_009843|||http://purl.uniprot.org/annotation/VSP_038470|||http://purl.uniprot.org/annotation/VSP_038471|||http://purl.uniprot.org/annotation/VSP_041916|||http://purl.uniprot.org/annotation/VSP_041917|||http://purl.uniprot.org/annotation/VSP_041918
http://togogenome.org/gene/9606:PPP6R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75170                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 6.|||Phosphoserine|||Serine/threonine-protein phosphatase 6 regulatory subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046098|||http://purl.uniprot.org/annotation/VAR_058402|||http://purl.uniprot.org/annotation/VAR_058403|||http://purl.uniprot.org/annotation/VSP_030758|||http://purl.uniprot.org/annotation/VSP_030759|||http://purl.uniprot.org/annotation/VSP_030760|||http://purl.uniprot.org/annotation/VSP_030761|||http://purl.uniprot.org/annotation/VSP_037767|||http://purl.uniprot.org/annotation/VSP_037768
http://togogenome.org/gene/9606:SUN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDU5|||http://purl.uniprot.org/uniprot/A9Z1W8|||http://purl.uniprot.org/uniprot/Q8TC36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In SPGF16; in mouse model abolishes interaction with DNAJB13.|||In SPGF16; loss of protein expression; impaired localization to nuclear inner membrane.|||In SPGF16; loss of protein expression; in mouse model impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||In SPGF16; significant reduction in protein expression; impaired localization to nuclear inner membrane; in mouse model decreases interaction with DNAJB13.|||In SPGF16; unknown pathological significance; in mouse model decreases protein solubility as well as impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||In SPGF16; unknown pathological significance; in mouse model impairs nuclear inner membrane location and decreases interaction with DNAJB13.|||In SPGF16; unknown pathological significance; in mouse model increases interaction with DNAJB13; impaired localization to nuclear inner membrane.|||Nuclear|||Perinuclear space|||SUN|||SUN domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218919|||http://purl.uniprot.org/annotation/VAR_015147|||http://purl.uniprot.org/annotation/VAR_026677|||http://purl.uniprot.org/annotation/VAR_026678|||http://purl.uniprot.org/annotation/VAR_052285|||http://purl.uniprot.org/annotation/VAR_077983|||http://purl.uniprot.org/annotation/VAR_077984|||http://purl.uniprot.org/annotation/VAR_077985|||http://purl.uniprot.org/annotation/VAR_077986|||http://purl.uniprot.org/annotation/VAR_077987|||http://purl.uniprot.org/annotation/VAR_077988|||http://purl.uniprot.org/annotation/VAR_080157|||http://purl.uniprot.org/annotation/VAR_080158
http://togogenome.org/gene/9606:UTP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5J1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||U3 small nucleolar RNA-associated protein 18 homolog|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051405
http://togogenome.org/gene/9606:RDH14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBH5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue                                                                                  ^@                                                                                  Phosphothreonine|||Proton acceptor|||Retinol dehydrogenase 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054770
http://togogenome.org/gene/9606:APOOL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXV4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||MICOS complex subunit MIC27|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042052
http://togogenome.org/gene/9606:CDC42BPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XZ8|||http://purl.uniprot.org/uniprot/Q9Y5S2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||CNH|||CRIB|||Disordered|||In CHOCNS.|||In CHOCNS; unknown pathological significance.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a colorectal adenocarcinoma sample and CHOCNS; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||Omega-N-methylarginine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MRCK beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086394|||http://purl.uniprot.org/annotation/VAR_025847|||http://purl.uniprot.org/annotation/VAR_040834|||http://purl.uniprot.org/annotation/VAR_040835|||http://purl.uniprot.org/annotation/VAR_040836|||http://purl.uniprot.org/annotation/VAR_040837|||http://purl.uniprot.org/annotation/VAR_040838|||http://purl.uniprot.org/annotation/VAR_040839|||http://purl.uniprot.org/annotation/VAR_070886|||http://purl.uniprot.org/annotation/VAR_087124|||http://purl.uniprot.org/annotation/VAR_087125|||http://purl.uniprot.org/annotation/VAR_087126|||http://purl.uniprot.org/annotation/VAR_087127|||http://purl.uniprot.org/annotation/VAR_087128|||http://purl.uniprot.org/annotation/VAR_087129|||http://purl.uniprot.org/annotation/VAR_087130|||http://purl.uniprot.org/annotation/VAR_087131|||http://purl.uniprot.org/annotation/VAR_087132
http://togogenome.org/gene/9606:THUMPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6MZT3|||http://purl.uniprot.org/uniprot/Q9NXG2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In NEDSOA.|||In NEDSOA; loss of function in tRNA acetylation; N4-acetylcytidine is not detected in small and tRNA samples from a homozygous patient.|||In NEDSOA; severely decreased tRNA binding; decreased thermal stability.|||In NEDSOA; unknown pathological significance.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||THUMP|||THUMP domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072530|||http://purl.uniprot.org/annotation/VAR_037645|||http://purl.uniprot.org/annotation/VAR_082156|||http://purl.uniprot.org/annotation/VAR_087582|||http://purl.uniprot.org/annotation/VAR_087583|||http://purl.uniprot.org/annotation/VAR_087584|||http://purl.uniprot.org/annotation/VAR_087585|||http://purl.uniprot.org/annotation/VAR_087586
http://togogenome.org/gene/9606:CPXM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N436                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F5/8 type C|||Inactive carboxypeptidase-like protein X2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004409|||http://purl.uniprot.org/annotation/VAR_048603
http://togogenome.org/gene/9606:PHF24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N-myristoyl glycine|||Omega-N-methylarginine|||PHD finger protein 24|||PHD-type|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059331
http://togogenome.org/gene/9606:PIP5K1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6PW57|||http://purl.uniprot.org/uniprot/Q99755                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreased 1-phosphatidylinositol-4-phosphate 5-kinase activity with 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate (arachidonate-PtdIns4P) as substrate. Increased enzyme activation by diarachidonoyl phosphatidic acid (DAPA). No change in enzyme activation by 1-stearoyl-2-oleoyl phosphatidic acid (SOPA) or 1-stearoyl-2-arachidonoyl phosphatidic acid (SAPA).|||Disordered|||Does not affect targeting of RAC1 to the plasma membrane; when associated with N-322.|||Does not affect targeting of RAC1 to the plasma membrane; when associated with Q-440.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Increased enzyme activation by diarachidonoyl phosphatidic acid (DAPA).|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185456|||http://purl.uniprot.org/annotation/VSP_016007|||http://purl.uniprot.org/annotation/VSP_016008|||http://purl.uniprot.org/annotation/VSP_041912|||http://purl.uniprot.org/annotation/VSP_041913
http://togogenome.org/gene/9606:MAST4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKT8|||http://purl.uniprot.org/uniprot/B4DS23|||http://purl.uniprot.org/uniprot/B4DSE5|||http://purl.uniprot.org/uniprot/E7EX28|||http://purl.uniprot.org/uniprot/O15021|||http://purl.uniprot.org/uniprot/Q6T2V4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Basic and acidic residues|||Basic residues|||Disordered|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Microtubule-associated serine/threonine-protein kinase 4|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252256|||http://purl.uniprot.org/annotation/VAR_040787|||http://purl.uniprot.org/annotation/VAR_040788|||http://purl.uniprot.org/annotation/VAR_040789|||http://purl.uniprot.org/annotation/VAR_040790|||http://purl.uniprot.org/annotation/VAR_040791|||http://purl.uniprot.org/annotation/VAR_059768|||http://purl.uniprot.org/annotation/VSP_020888|||http://purl.uniprot.org/annotation/VSP_023109|||http://purl.uniprot.org/annotation/VSP_035852|||http://purl.uniprot.org/annotation/VSP_035853|||http://purl.uniprot.org/annotation/VSP_059373|||http://purl.uniprot.org/annotation/VSP_059374
http://togogenome.org/gene/9606:PRPS1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21108                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Region|||Sequence Variant                                                                                  ^@                                                                                  Binding of phosphoribosylpyrophosphate|||Removed|||Ribose-phosphate pyrophosphokinase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141078|||http://purl.uniprot.org/annotation/VAR_050062
http://togogenome.org/gene/9606:DNTTIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5QJE6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Deoxynucleotidyltransferase terminal-interacting protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||TdBR region; mediates interaction with DNTT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318505|||http://purl.uniprot.org/annotation/VAR_038748|||http://purl.uniprot.org/annotation/VAR_038749|||http://purl.uniprot.org/annotation/VAR_038750|||http://purl.uniprot.org/annotation/VAR_038751|||http://purl.uniprot.org/annotation/VAR_061710
http://togogenome.org/gene/9606:MOB3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TA1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict                                                                                  ^@                                                                                  MOB kinase activator 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193572
http://togogenome.org/gene/9606:C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01031|||http://purl.uniprot.org/uniprot/Q59GS8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Anaphylatoxin-like|||Associated with poor response to eculizumab in PNH patients.|||C5a anaphylatoxin|||Complement C5 alpha chain|||Complement C5 alpha' chain|||Complement C5 beta chain|||Confirmed at protein level.|||Involved in C5AR1 binding|||Involved in the tick complement inhibitor CirpT1|||N-linked (GlcNAc...) asparagine|||NTR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005985|||http://purl.uniprot.org/annotation/PRO_0000005986|||http://purl.uniprot.org/annotation/PRO_0000005987|||http://purl.uniprot.org/annotation/PRO_0000005988|||http://purl.uniprot.org/annotation/PRO_0000005989|||http://purl.uniprot.org/annotation/VAR_001996|||http://purl.uniprot.org/annotation/VAR_014574|||http://purl.uniprot.org/annotation/VAR_014575|||http://purl.uniprot.org/annotation/VAR_014576|||http://purl.uniprot.org/annotation/VAR_014577|||http://purl.uniprot.org/annotation/VAR_023946|||http://purl.uniprot.org/annotation/VAR_038735|||http://purl.uniprot.org/annotation/VAR_038736|||http://purl.uniprot.org/annotation/VAR_038737|||http://purl.uniprot.org/annotation/VAR_038738|||http://purl.uniprot.org/annotation/VAR_038739|||http://purl.uniprot.org/annotation/VAR_038740|||http://purl.uniprot.org/annotation/VAR_038741|||http://purl.uniprot.org/annotation/VAR_048822|||http://purl.uniprot.org/annotation/VAR_048823|||http://purl.uniprot.org/annotation/VAR_048824|||http://purl.uniprot.org/annotation/VAR_071067|||http://purl.uniprot.org/annotation/VAR_071068
http://togogenome.org/gene/9606:STRADA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTN6|||http://purl.uniprot.org/uniprot/Q86YC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inhibits interaction with STK11/LKB1.|||Inhibits interaction with STK11/LKB1; when associated with A-.|||Loss of STK11/LKB1-mediated phosphorylation.|||Phosphoserine|||Phosphothreonine; by LKB1|||Polar residues|||Protein kinase|||STE20-related kinase adapter protein alpha|||Suppresses STK11/LKB1 activation without affecting complex assembly.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260035|||http://purl.uniprot.org/annotation/VAR_041377|||http://purl.uniprot.org/annotation/VAR_041378|||http://purl.uniprot.org/annotation/VAR_041379|||http://purl.uniprot.org/annotation/VSP_043707|||http://purl.uniprot.org/annotation/VSP_043708|||http://purl.uniprot.org/annotation/VSP_044278|||http://purl.uniprot.org/annotation/VSP_044717|||http://purl.uniprot.org/annotation/VSP_052219|||http://purl.uniprot.org/annotation/VSP_052220|||http://purl.uniprot.org/annotation/VSP_052221
http://togogenome.org/gene/9606:TUBB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMJ5|||http://purl.uniprot.org/uniprot/B4DQN9|||http://purl.uniprot.org/uniprot/B4DY90|||http://purl.uniprot.org/uniprot/P07437|||http://purl.uniprot.org/uniprot/Q5ST81|||http://purl.uniprot.org/uniprot/Q5SU16                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl glycine|||5-glutamyl polyglutamate|||Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CDCBM6; arrests the assembly pathway of alpha/beta-tubulin; the mutant protein is unable to coassemble into a tubulin heterodimer but is instead distributed throughout the cytoplasm.|||In CDCBM6; decreases the ability of the protein to assemble into tubulin heterodimers.|||In CDCBM6; does not affect the ability of the mutant polypeptides to assemble into heterodimers and incorporate into microtubules.|||In CSCSC1; disrupts heterodimer assembly and microtubule dynamics.|||MREI motif|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Tubulin beta chain|||Tubulin/FtsZ 2-layer sandwich|||Tubulin/FtsZ GTPase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048243|||http://purl.uniprot.org/annotation/VAR_071763|||http://purl.uniprot.org/annotation/VAR_071764|||http://purl.uniprot.org/annotation/VAR_071765|||http://purl.uniprot.org/annotation/VAR_076543|||http://purl.uniprot.org/annotation/VAR_076544
http://togogenome.org/gene/9606:AP3B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5J4|||http://purl.uniprot.org/uniprot/O00203                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AP-3 complex subunit beta C-terminal|||AP-3 complex subunit beta-1|||Acidic residues|||Basic and acidic residues|||Beta-adaptin appendage C-terminal subdomain|||Disordered|||In HPS2.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193746|||http://purl.uniprot.org/annotation/VAR_011595|||http://purl.uniprot.org/annotation/VAR_011596|||http://purl.uniprot.org/annotation/VAR_058404|||http://purl.uniprot.org/annotation/VSP_054708
http://togogenome.org/gene/9606:CHST10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43529                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 10|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Induces a mild reduction in enzyme activity.|||Induces a reduction in enzyme activity.|||Loss of function.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189657|||http://purl.uniprot.org/annotation/VAR_021470|||http://purl.uniprot.org/annotation/VAR_033737
http://togogenome.org/gene/9606:ICAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEK5|||http://purl.uniprot.org/uniprot/P05362                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cell attachment site; atypical|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Immunoglobulin subtype|||In Kilifi; at homozygosity it is associated with increased susceptibility to cerebral malaria.|||Intercellular adhesion molecule 1|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014783|||http://purl.uniprot.org/annotation/PRO_5017224567|||http://purl.uniprot.org/annotation/VAR_010204|||http://purl.uniprot.org/annotation/VAR_014186|||http://purl.uniprot.org/annotation/VAR_014187|||http://purl.uniprot.org/annotation/VAR_014651|||http://purl.uniprot.org/annotation/VAR_014652|||http://purl.uniprot.org/annotation/VAR_014653|||http://purl.uniprot.org/annotation/VAR_014654|||http://purl.uniprot.org/annotation/VAR_016267
http://togogenome.org/gene/9606:IL10RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BTRC recognition motif|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In IBD28.|||Interleukin-10 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011012|||http://purl.uniprot.org/annotation/VAR_016294|||http://purl.uniprot.org/annotation/VAR_016295|||http://purl.uniprot.org/annotation/VAR_016296|||http://purl.uniprot.org/annotation/VAR_016297|||http://purl.uniprot.org/annotation/VAR_016298|||http://purl.uniprot.org/annotation/VAR_016299|||http://purl.uniprot.org/annotation/VAR_020004|||http://purl.uniprot.org/annotation/VAR_049175|||http://purl.uniprot.org/annotation/VAR_063542|||http://purl.uniprot.org/annotation/VAR_063543|||http://purl.uniprot.org/annotation/VAR_071663|||http://purl.uniprot.org/annotation/VAR_071664|||http://purl.uniprot.org/annotation/VAR_071665|||http://purl.uniprot.org/annotation/VAR_071666|||http://purl.uniprot.org/annotation/VAR_071667
http://togogenome.org/gene/9606:HENMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T8I9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Small RNA 2'-O-methyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304139|||http://purl.uniprot.org/annotation/VAR_035017|||http://purl.uniprot.org/annotation/VAR_035018|||http://purl.uniprot.org/annotation/VAR_035019
http://togogenome.org/gene/9606:ACER2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVV5|||http://purl.uniprot.org/uniprot/Q5QJU3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alkaline ceramidase 2|||Cytoplasmic|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of localization to the Golgi. No effect on the ceramidase activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Required for proper localization to the Golgi apparatus                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247748|||http://purl.uniprot.org/annotation/VAR_027150|||http://purl.uniprot.org/annotation/VSP_020033|||http://purl.uniprot.org/annotation/VSP_020034|||http://purl.uniprot.org/annotation/VSP_020035
http://togogenome.org/gene/9606:RTTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MSSP.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Rotatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308612|||http://purl.uniprot.org/annotation/VAR_036848|||http://purl.uniprot.org/annotation/VAR_036849|||http://purl.uniprot.org/annotation/VAR_036850|||http://purl.uniprot.org/annotation/VAR_036851|||http://purl.uniprot.org/annotation/VAR_069094|||http://purl.uniprot.org/annotation/VAR_069095|||http://purl.uniprot.org/annotation/VSP_029024|||http://purl.uniprot.org/annotation/VSP_029025|||http://purl.uniprot.org/annotation/VSP_029026|||http://purl.uniprot.org/annotation/VSP_029027|||http://purl.uniprot.org/annotation/VSP_029030|||http://purl.uniprot.org/annotation/VSP_029031
http://togogenome.org/gene/9606:YPEL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QA6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  Protein yippee-like 2|||Yippee                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212385
http://togogenome.org/gene/9606:SMARCA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2E1|||http://purl.uniprot.org/uniprot/B3KNW7|||http://purl.uniprot.org/uniprot/P51532|||http://purl.uniprot.org/uniprot/Q9HBD4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to 'Lys-15'-acetylated histone H3.|||Acidic residues|||Basic and acidic residues|||Bromo|||DEGH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HSA|||Helicase ATP-binding|||Helicase C-terminal|||In CSS4.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||N6-acetyllysine|||Necessary for interaction with SS18L1/CREST|||No effect on binding to 'Lys-15'-acetylated histone H3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||QLQ|||RNA-binding region which is sufficient for binding to lncRNA Evf2|||Required for binding to 'Lys-15'-acetylated histone 3|||Sufficient for interaction with DLX1|||Transcription activator BRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074353|||http://purl.uniprot.org/annotation/VAR_028215|||http://purl.uniprot.org/annotation/VAR_028216|||http://purl.uniprot.org/annotation/VAR_068209|||http://purl.uniprot.org/annotation/VAR_068210|||http://purl.uniprot.org/annotation/VAR_068211|||http://purl.uniprot.org/annotation/VAR_068212|||http://purl.uniprot.org/annotation/VAR_068213|||http://purl.uniprot.org/annotation/VAR_068214|||http://purl.uniprot.org/annotation/VSP_043137|||http://purl.uniprot.org/annotation/VSP_043677|||http://purl.uniprot.org/annotation/VSP_043678
http://togogenome.org/gene/9606:FADS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYB9|||http://purl.uniprot.org/uniprot/Q8N9I5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||3 X 6 AA tandem repeat of M-E-P-T-E-P|||Disordered|||Fatty acid desaturase|||Fatty acid desaturase 6|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341546|||http://purl.uniprot.org/annotation/VSP_034320
http://togogenome.org/gene/9606:EYA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Q2|||http://purl.uniprot.org/uniprot/A0A0S2Z3V9|||http://purl.uniprot.org/uniprot/B4DIV6|||http://purl.uniprot.org/uniprot/B4DRQ6|||http://purl.uniprot.org/uniprot/F2Z2Y1|||http://purl.uniprot.org/uniprot/O95677|||http://purl.uniprot.org/uniprot/Q96CJ7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Eyes absent homolog 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DFNA10.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||N-acetylmethionine|||Nucleophile|||Phosphoserine|||Polar residues|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218651|||http://purl.uniprot.org/annotation/VAR_022932|||http://purl.uniprot.org/annotation/VAR_036248|||http://purl.uniprot.org/annotation/VAR_036249|||http://purl.uniprot.org/annotation/VAR_074570|||http://purl.uniprot.org/annotation/VAR_074571|||http://purl.uniprot.org/annotation/VAR_079872|||http://purl.uniprot.org/annotation/VSP_001495|||http://purl.uniprot.org/annotation/VSP_001496|||http://purl.uniprot.org/annotation/VSP_001497|||http://purl.uniprot.org/annotation/VSP_001498|||http://purl.uniprot.org/annotation/VSP_001499|||http://purl.uniprot.org/annotation/VSP_042160
http://togogenome.org/gene/9606:RAB32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13637                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to protein kinase A type II regulatory subunit.|||Decreased GTP-binding activity.|||Effector region|||Impairs interaction with ANKRD27; when associated with M-91.|||Impairs interaction with ANKRD27; when associated with S-90 and L-94.|||Impairs interaction with ANKRD27; when associated with S-93.|||Impairs interaction with ANKRD27; when associated with T-89 and L-94.|||Impairs interaction with ANKRD27; when associated with T-89 and S-90.|||N-acetylalanine|||No change in GTPase activity.|||PKA-RII subunit binding domain|||Phosphoserine|||Ras-related protein Rab-32|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121235
http://togogenome.org/gene/9606:UCHL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5K5                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||Important for enzyme activity|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Interaction with ADRM1|||N6-acetyllysine|||N6-succinyllysine|||Nucleophile|||Proton donor|||Ubiquitin carboxyl-terminal hydrolase isozyme L5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211066|||http://purl.uniprot.org/annotation/VAR_011613|||http://purl.uniprot.org/annotation/VSP_005253|||http://purl.uniprot.org/annotation/VSP_005254|||http://purl.uniprot.org/annotation/VSP_017062
http://togogenome.org/gene/9606:NKX6-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJ46                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein Nkx-6.3|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311330|||http://purl.uniprot.org/annotation/VSP_029523
http://togogenome.org/gene/9606:PLPPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GM1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317538|||http://purl.uniprot.org/annotation/VAR_038546|||http://purl.uniprot.org/annotation/VSP_031010|||http://purl.uniprot.org/annotation/VSP_031011
http://togogenome.org/gene/9606:TEX30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFW4|||http://purl.uniprot.org/uniprot/Q5JUR7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||KANL3/Tex30 alpha/beta hydrolase-like|||Testis-expressed protein 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274312|||http://purl.uniprot.org/annotation/VSP_055706|||http://purl.uniprot.org/annotation/VSP_055707
http://togogenome.org/gene/9606:TENT5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IP4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||2|||3|||4|||Does not elongate poly(A) tail; when associated with N-139.|||Does not elongate poly(A) tail; when associated with N-141.|||In OI18; unknown pathological significance.|||In isoform 2.|||Terminal nucleotidyltransferase 5A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259929|||http://purl.uniprot.org/annotation/VAR_028978|||http://purl.uniprot.org/annotation/VAR_028979|||http://purl.uniprot.org/annotation/VAR_046649|||http://purl.uniprot.org/annotation/VAR_080798|||http://purl.uniprot.org/annotation/VAR_080799|||http://purl.uniprot.org/annotation/VSP_035502
http://togogenome.org/gene/9606:TMEM151A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4L1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In EKD3.|||In EKD3; unknown pathological significance.|||Transmembrane protein 151A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282986|||http://purl.uniprot.org/annotation/VAR_088181|||http://purl.uniprot.org/annotation/VAR_088182|||http://purl.uniprot.org/annotation/VAR_088183|||http://purl.uniprot.org/annotation/VAR_088184|||http://purl.uniprot.org/annotation/VAR_088185|||http://purl.uniprot.org/annotation/VAR_088186|||http://purl.uniprot.org/annotation/VAR_088187|||http://purl.uniprot.org/annotation/VAR_088188|||http://purl.uniprot.org/annotation/VAR_088189|||http://purl.uniprot.org/annotation/VAR_088190|||http://purl.uniprot.org/annotation/VAR_088191|||http://purl.uniprot.org/annotation/VAR_088192|||http://purl.uniprot.org/annotation/VAR_088193|||http://purl.uniprot.org/annotation/VAR_088194|||http://purl.uniprot.org/annotation/VAR_088195|||http://purl.uniprot.org/annotation/VAR_088196|||http://purl.uniprot.org/annotation/VAR_088197|||http://purl.uniprot.org/annotation/VAR_088198|||http://purl.uniprot.org/annotation/VAR_088199|||http://purl.uniprot.org/annotation/VAR_088200|||http://purl.uniprot.org/annotation/VAR_088201|||http://purl.uniprot.org/annotation/VAR_088202|||http://purl.uniprot.org/annotation/VAR_088203|||http://purl.uniprot.org/annotation/VAR_088204|||http://purl.uniprot.org/annotation/VAR_088205|||http://purl.uniprot.org/annotation/VAR_088206|||http://purl.uniprot.org/annotation/VAR_088207|||http://purl.uniprot.org/annotation/VAR_088208|||http://purl.uniprot.org/annotation/VAR_088209|||http://purl.uniprot.org/annotation/VAR_088210|||http://purl.uniprot.org/annotation/VAR_088211|||http://purl.uniprot.org/annotation/VAR_088212|||http://purl.uniprot.org/annotation/VAR_088213|||http://purl.uniprot.org/annotation/VAR_088214|||http://purl.uniprot.org/annotation/VAR_088215|||http://purl.uniprot.org/annotation/VAR_088216|||http://purl.uniprot.org/annotation/VAR_088217
http://togogenome.org/gene/9606:TPTE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56180                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C2 tensin-type|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphatase tensin-type|||Putative tyrosine-protein phosphatase TPTE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215907|||http://purl.uniprot.org/annotation/VAR_025400|||http://purl.uniprot.org/annotation/VAR_036516|||http://purl.uniprot.org/annotation/VAR_057347|||http://purl.uniprot.org/annotation/VAR_057348|||http://purl.uniprot.org/annotation/VAR_061895|||http://purl.uniprot.org/annotation/VAR_065097|||http://purl.uniprot.org/annotation/VSP_017319|||http://purl.uniprot.org/annotation/VSP_017320|||http://purl.uniprot.org/annotation/VSP_017321
http://togogenome.org/gene/9606:CBY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3M2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Minimal region for the interaction with PKD2|||Phosphoserine|||Polar residues|||Protein chibby homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058354
http://togogenome.org/gene/9606:MC1R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01726|||http://purl.uniprot.org/uniprot/Q1JUL4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with UV induced susceptibility to skin damage; shows a dramatically decreased cAMP production to NDP-MSH stimulation.|||Associated with UV induced susceptibility to skin damage; shows a strong decreased cAMP production to NDP-MSH stimulation.|||Associated with UV induced susceptibility to skin damage; unresponsive to NDP-MSH stimulation.|||Associated with a risk for developing melanoma; predominantly found in type I skin; shows a moderate and not significant decreased of cAMP production to NDP-MSH stimulation.|||Associated with a risk for developing melanoma; reduced expression at the cell surface.|||Associated with a risk for developing melanoma; shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a not significant decrease in cAMP production at any concentrations of NDP-MSH stimulation.|||Associated with a risk for developing melanoma; unable to stimulate cAMP production as strongly as the wild type receptor in response to alpha-melanocyte-stimulating hormone stimulation.|||Associated with a risk for developing melanoma; unable to stimulate cAMP production as strongly as the wild type receptor in response to alpha-melanocyte-stimulating hormone stimulation; reduced expression at the cell surface..|||Associated with fair hair and light skin; partial loss-of-function.|||Associated with red hair and light skin of type I; binds to alpha-MSH but cannot be stimulated to produce cAMP; reduced expression at the cell surface.|||Cytoplasmic|||Does not affect receptor surface expression, agonist binding and agonist-induced signaling.|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CMM5; complete absence of functional coupling to the cAMP pathway; reduced cell surface expression as a consequence of retention in the endoplasmic reticulum.|||In CMM5; complete absence of functional coupling to the cAMP pathway; trafficked to the cell surface but unable to bind agonist efficiently.|||In CMM5; moderate decrease in coupling to the cAMP pathway; reduced cell surface expression as a consequence of retention in the endoplasmic reticulum.|||Loss-of-function mutation abolishing agonist binding.|||May be associated with a risk for developing melanoma; reduced expression at the cell surface.|||Melanocyte-stimulating hormone receptor|||N-linked (GlcNAc...) asparagine|||Only minor effect on internalization rate and protein half-life; when associated with R-226; R-238 and R-310.|||Only minor effect on internalization rate and protein half-life; when associated with R-65; R-226 and R-238.|||Only minor effect on internalization rate and protein half-life; when associated with R-65; R-226 and R-310.|||Only minor effect on internalization rate and protein half-life; when associated with R-65; R-238 and R-310.|||S-palmitoyl cysteine|||Shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a decreased responses to low concentrations of NDP-MSH stimulation.|||Shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows a not significant decrease in cAMP production at any concentrations of NDP-MSH stimulation.|||Shows a moderate and not significant decrease of cAMP production to NDP-MSH stimulation; shows decreased responses to low concentrations of NDP-MSH stimulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069818|||http://purl.uniprot.org/annotation/VAR_003507|||http://purl.uniprot.org/annotation/VAR_003508|||http://purl.uniprot.org/annotation/VAR_008522|||http://purl.uniprot.org/annotation/VAR_008523|||http://purl.uniprot.org/annotation/VAR_008524|||http://purl.uniprot.org/annotation/VAR_009522|||http://purl.uniprot.org/annotation/VAR_009523|||http://purl.uniprot.org/annotation/VAR_013611|||http://purl.uniprot.org/annotation/VAR_013612|||http://purl.uniprot.org/annotation/VAR_013613|||http://purl.uniprot.org/annotation/VAR_013614|||http://purl.uniprot.org/annotation/VAR_013615|||http://purl.uniprot.org/annotation/VAR_013616|||http://purl.uniprot.org/annotation/VAR_013632|||http://purl.uniprot.org/annotation/VAR_042654|||http://purl.uniprot.org/annotation/VAR_042655|||http://purl.uniprot.org/annotation/VAR_042656|||http://purl.uniprot.org/annotation/VAR_042657|||http://purl.uniprot.org/annotation/VAR_042658|||http://purl.uniprot.org/annotation/VAR_042659|||http://purl.uniprot.org/annotation/VAR_042660|||http://purl.uniprot.org/annotation/VAR_042661|||http://purl.uniprot.org/annotation/VAR_042662|||http://purl.uniprot.org/annotation/VAR_059018|||http://purl.uniprot.org/annotation/VAR_059019|||http://purl.uniprot.org/annotation/VAR_059020|||http://purl.uniprot.org/annotation/VAR_059021|||http://purl.uniprot.org/annotation/VAR_059022|||http://purl.uniprot.org/annotation/VAR_059023|||http://purl.uniprot.org/annotation/VAR_059024|||http://purl.uniprot.org/annotation/VAR_059025
http://togogenome.org/gene/9606:COLEC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6Z7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||C-type lectin|||Collagen-like|||Collectin-10|||Disordered|||In 3MC3; results in lack of protein.|||In 3MC3; severely decreased secretion.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314233|||http://purl.uniprot.org/annotation/VAR_078811|||http://purl.uniprot.org/annotation/VAR_078812
http://togogenome.org/gene/9606:TRPC5OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMA1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Putative uncharacterized protein TRPC5OS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349178
http://togogenome.org/gene/9606:SFPQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N5Z8|||http://purl.uniprot.org/uniprot/P23246|||http://purl.uniprot.org/uniprot/Q86VG2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 3 AA repeats of R-G-G|||Abolishes phosphorylation by GSK3B. Impairs interaction with THRAP3.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Breakpoint for translocation to form SFPQ-TFE3|||Dimethylated arginine|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-546.|||Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-539 and A-549.|||Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-535; A-546 and A-549.|||Impairs DNA binding and ability to mediate transcriptional activation; when associated with A-539; A-546 and A-549.|||In isoform Short.|||N6,N6-dimethyllysine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on interaction with THRAP3 (phosphomimetic).|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MKNK2|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ALK|||Pro residues|||RRM|||RRM 1|||RRM 2|||Splicing factor, proline- and glutamine-rich                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081909|||http://purl.uniprot.org/annotation/VSP_005855
http://togogenome.org/gene/9606:LIPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXJ0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Lipase member K|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286699|||http://purl.uniprot.org/annotation/VAR_032160|||http://purl.uniprot.org/annotation/VAR_032161
http://togogenome.org/gene/9606:NAV3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YFX5|||http://purl.uniprot.org/uniprot/Q8IVL0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA+ ATPase|||Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||In a patient with Sezary syndrome.|||In isoform 2 and isoform 3.|||In isoform 3.|||Neuron navigator 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286976|||http://purl.uniprot.org/annotation/VAR_032249|||http://purl.uniprot.org/annotation/VAR_032250|||http://purl.uniprot.org/annotation/VAR_032251|||http://purl.uniprot.org/annotation/VSP_025268|||http://purl.uniprot.org/annotation/VSP_025269
http://togogenome.org/gene/9606:SHBG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0FWH2|||http://purl.uniprot.org/uniprot/I3L145|||http://purl.uniprot.org/uniprot/P04278                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Generates a N-glycosylation site.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Sex hormone-binding globulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000174|||http://purl.uniprot.org/annotation/PRO_0000032557|||http://purl.uniprot.org/annotation/PRO_5010104610|||http://purl.uniprot.org/annotation/VAR_013129|||http://purl.uniprot.org/annotation/VAR_013946|||http://purl.uniprot.org/annotation/VAR_016182|||http://purl.uniprot.org/annotation/VAR_022002|||http://purl.uniprot.org/annotation/VSP_006091|||http://purl.uniprot.org/annotation/VSP_006092|||http://purl.uniprot.org/annotation/VSP_045358|||http://purl.uniprot.org/annotation/VSP_045376|||http://purl.uniprot.org/annotation/VSP_061578
http://togogenome.org/gene/9606:KIAA1210                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acrosomal protein KIAA1210|||Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050790|||http://purl.uniprot.org/annotation/VAR_061243|||http://purl.uniprot.org/annotation/VAR_061244|||http://purl.uniprot.org/annotation/VAR_061245|||http://purl.uniprot.org/annotation/VAR_061246|||http://purl.uniprot.org/annotation/VAR_061247|||http://purl.uniprot.org/annotation/VAR_061248|||http://purl.uniprot.org/annotation/VAR_061249|||http://purl.uniprot.org/annotation/VAR_076260|||http://purl.uniprot.org/annotation/VAR_077001
http://togogenome.org/gene/9606:B4GALNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHY0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,4 N-acetylgalactosaminyltransferase 2|||Cytoplasmic|||Found in individuals with Sd(a-) phenotype.|||Helical; Signal-anchor for type II membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059103|||http://purl.uniprot.org/annotation/VAR_035990|||http://purl.uniprot.org/annotation/VAR_049238|||http://purl.uniprot.org/annotation/VAR_049239|||http://purl.uniprot.org/annotation/VAR_086499|||http://purl.uniprot.org/annotation/VAR_086500|||http://purl.uniprot.org/annotation/VSP_017131|||http://purl.uniprot.org/annotation/VSP_045195
http://togogenome.org/gene/9606:SNAI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95863                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes CK2 phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in cell survival. Abolishes phosphorylation in the serine-rich region; when associated with A-104 and A-107.|||Abolishes LATS2 phosphorylation. Does not affect binding to LATS2. Reduces protein stability. Equally distributed between nucleus and cytoplasm. Increases capacity to associate with nuclear pore importins. Unable to accumulate in the nucleus. Does not abrogate function.|||Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT.|||Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization.|||Abolishes recognition and ubiquitination by BTRC which increases steady state level and half-life. Preferentially localizes to the nucleus. Induces a more aggressive tissue invasion program. Lower sensitivity to BTRC-triggered degradation, impairs phosphorylation by GSK3B and does not affect NOTCH1-induced degradation; when associated with A-100. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-100; A-107; A-111; A-115 and A-119.|||Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A.|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||Decreases repression activity on E-cadherin/CDH1, occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1.|||Destruction motif|||Disordered|||Does not affect E-cadherin repression; when associated with R-9.|||Does not affect E-cadherin/CDH1 repression; when associated with R-16.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-191. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-220.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-161.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-170. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-187 and/or E-220.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-222. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-220.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-220 and E-224.|||Does not affect binding to KPNB1, KPNA2, IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1; when associated with E-222 and E-224. Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1 and abolishes nuclear localization, DNA binding and repressor activity on E-cadherin/CDH1 promoter; when associated with E-224. Abolishes binding to KPNB1, KPNA2, IPO7 and TNPO1 and nuclear localization; when associated with E-161 and/or E-187.|||Does not affect binding to KPNB1, KPNA2, IPO7, TNPO1 or DNA.|||Does not affect repressor activity on E-cadherin/CDH1 promoter.|||Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization.|||Impairs binding to KPNB1, IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus.|||Impairs binding to KPNB1, KPNA2, IPO7 and TNPO1. No change in subcellular localization.|||Increases protein stability, does not affect repressor activity on E-cadherin/CDH1 promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-107. Impairs phosphorylation in the serine-rich domain/region; when associated with A-92 and A-107. Abolishes phosphorylation at S-96.|||LATS2 binding|||Loss of binding to KPNB1 and nuclear import; when associated with E-191 and A-193.|||Loss of interaction with KDM1A.|||Lower sensitivity to BTRC-triggered degradation and impaired phosphorylation by GSK3B; when associated with A-96. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-107; A-111; A-115 and A-119. Does not affect NOTCH1-induced degradation; when associated with A-96. Abolishes phosphorylation at S-96.|||Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-115.|||Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-119.|||Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-115 and A-119.|||Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-111; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-111; A-115 and A-119. Increases protein stability, does not affect repressor activity on E-cadherin promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-104. Impairs phosphorylation in the serine-rich region; when associated with A-92 and A-104. Abolishes phosphorylation at S-96.|||Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-137. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation; when associated with R-98 and R-137.|||Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-146. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin; when associated with R-98 and R-146.|||Mildly reduces binding to KPNB1 and nuclear import.|||Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-193. Loss of binding to KPNB1 and nuclear import; when associated with A-193 and A-196.|||Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with A-228.|||Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with E-191. Loss of binding to KPNB1 and nuclear import; when associated with E-191 and A-196.|||Mildly reduces binding to KPNB1. Does not affect binding to KPNA2, IPO7 or TNPO1.|||No change. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin/CDH1; when associated with R-137 and R-146.|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by PAK1|||Phosphoserine; by PKA|||Phosphothreonine; by LATS2|||Polar residues|||Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115.|||Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119.|||Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119.|||Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119.|||Required and sufficient for interaction with KDM1A|||Required for FBXL14-triggered degradation|||Required for nuclear localization and interaction with KPNB1, NOTCH1 and PARP1|||SNAG domain|||Very minor effect on binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import; when associated with E-224.|||Zinc finger protein SNAI1 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047029|||http://purl.uniprot.org/annotation/VAR_019969|||http://purl.uniprot.org/annotation/VAR_069162
http://togogenome.org/gene/9606:PPP1R3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XI6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CBM21|||PP1-binding motif|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324543|||http://purl.uniprot.org/annotation/VAR_039814
http://togogenome.org/gene/9606:AGR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95994|||http://purl.uniprot.org/uniprot/Q4JM46                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Anterior gradient protein 2 homolog|||Disrupted dimerization.|||Homodimer stabilization; interchain|||In RIFTD; decreased interaction with MUC2.|||In RIFTD; unknown pathological significance.|||Loss of interaction with MUC2.|||Monomer only, and reduced cell adhesion efficiency.|||Required to promote cell adhesion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001037|||http://purl.uniprot.org/annotation/PRO_5014309370|||http://purl.uniprot.org/annotation/VAR_088087|||http://purl.uniprot.org/annotation/VAR_088088|||http://purl.uniprot.org/annotation/VAR_088089
http://togogenome.org/gene/9606:IFITM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01629                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Interferon-induced transmembrane protein 2|||Loss of anti-HCV activity. Partial loss of endosomal location.|||Loss of phosphorylation. Accumulates at the plasma membrane. Increases infection with influenza A virus and SARS-CoV-2. Increases anti-HCV properties.|||N-acetylmethionine|||No effect on anti-HCV activity. Partial loss of endosomal location.|||Phosphotyrosine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153728|||http://purl.uniprot.org/annotation/VAR_014848|||http://purl.uniprot.org/annotation/VAR_060470|||http://purl.uniprot.org/annotation/VAR_062677
http://togogenome.org/gene/9606:EMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50402                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.|||Emerin|||Helical|||In EDMD1.|||In EDMD1; loss of binding to F-actin.|||In EDMD1; no loss of binding to F-actin and enhanced rate of actin polymerization.|||In EDMD1; no loss of binding to F-actin, enhanced rate of actin polymerization and loss of binding to BCLAF1.|||Interaction with CTNNB1|||Interaction with F-actin|||LEM|||Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA.|||N-acetylmethionine|||No loss of binding to F-actin; when associated with A-196.|||No loss of binding to F-actin; when associated with A-197.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206140|||http://purl.uniprot.org/annotation/VAR_005198|||http://purl.uniprot.org/annotation/VAR_005199|||http://purl.uniprot.org/annotation/VAR_005200|||http://purl.uniprot.org/annotation/VAR_016016|||http://purl.uniprot.org/annotation/VAR_038433
http://togogenome.org/gene/9606:DUXA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Disordered|||Double homeobox protein A|||Homeobox 1|||Homeobox 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311327
http://togogenome.org/gene/9606:ZNF208                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QYK4|||http://purl.uniprot.org/uniprot/O43345                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 30|||C2H2-type 31|||C2H2-type 32|||C2H2-type 33|||C2H2-type 34|||C2H2-type 35|||C2H2-type 36|||C2H2-type 37|||C2H2-type 38|||C2H2-type 39|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 208                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047454|||http://purl.uniprot.org/annotation/VAR_052791|||http://purl.uniprot.org/annotation/VAR_052792|||http://purl.uniprot.org/annotation/VAR_052793|||http://purl.uniprot.org/annotation/VAR_059903|||http://purl.uniprot.org/annotation/VAR_059904|||http://purl.uniprot.org/annotation/VSP_053780|||http://purl.uniprot.org/annotation/VSP_053781|||http://purl.uniprot.org/annotation/VSP_053782
http://togogenome.org/gene/9606:GORAB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ87|||http://purl.uniprot.org/uniprot/Q5T7V8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Necessary for interaction with RCHY1|||Polar residues|||RAB6-interacting golgin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252444|||http://purl.uniprot.org/annotation/VAR_027867|||http://purl.uniprot.org/annotation/VSP_020978
http://togogenome.org/gene/9606:SPATA31C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYI2|||http://purl.uniprot.org/uniprot/Q9Y4N5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Putative spermatogenesis-associated protein 31C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420571
http://togogenome.org/gene/9606:TBC1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYX2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with CADH1|||Interaction with RAC1|||N-acetylmethionine|||PH|||Phosphoserine|||Rab-GAP TBC|||TBC1 domain family member 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208024|||http://purl.uniprot.org/annotation/VAR_046707|||http://purl.uniprot.org/annotation/VAR_046708|||http://purl.uniprot.org/annotation/VAR_046709|||http://purl.uniprot.org/annotation/VSP_039379|||http://purl.uniprot.org/annotation/VSP_039380|||http://purl.uniprot.org/annotation/VSP_039381|||http://purl.uniprot.org/annotation/VSP_039382|||http://purl.uniprot.org/annotation/VSP_039383
http://togogenome.org/gene/9606:KRT37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76014                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||Keratin, type I cuticular Ha7|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063694|||http://purl.uniprot.org/annotation/VAR_049795|||http://purl.uniprot.org/annotation/VAR_049796|||http://purl.uniprot.org/annotation/VAR_049797|||http://purl.uniprot.org/annotation/VAR_049798|||http://purl.uniprot.org/annotation/VAR_049799|||http://purl.uniprot.org/annotation/VAR_049800|||http://purl.uniprot.org/annotation/VAR_049801|||http://purl.uniprot.org/annotation/VAR_049802|||http://purl.uniprot.org/annotation/VAR_049803
http://togogenome.org/gene/9606:FBXO15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCQ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 15|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119893|||http://purl.uniprot.org/annotation/VAR_049040|||http://purl.uniprot.org/annotation/VSP_043033
http://togogenome.org/gene/9606:CFAP100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q494V2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 100|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234487|||http://purl.uniprot.org/annotation/VSP_018328
http://togogenome.org/gene/9606:NEUROD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z493|||http://purl.uniprot.org/uniprot/Q13562                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||BHLH|||Basic and acidic residues|||Disordered|||Found in one consanguineous family with non-syndromic autosomal recessive retinitis pigmentosa; unknown pathological significance.|||In MODY6.|||In MODY6; unknown pathological significance.|||In T2D.|||Neurogenic differentiation factor 1|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CaMK2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127381|||http://purl.uniprot.org/annotation/VAR_012487|||http://purl.uniprot.org/annotation/VAR_014820|||http://purl.uniprot.org/annotation/VAR_031260|||http://purl.uniprot.org/annotation/VAR_076552|||http://purl.uniprot.org/annotation/VAR_076553|||http://purl.uniprot.org/annotation/VAR_076554
http://togogenome.org/gene/9606:ZNF512B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6; atypical|||C2H2-type 7|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger protein 512B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047779|||http://purl.uniprot.org/annotation/VAR_024226|||http://purl.uniprot.org/annotation/VAR_024227|||http://purl.uniprot.org/annotation/VAR_061954
http://togogenome.org/gene/9606:RDH11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z583|||http://purl.uniprot.org/uniprot/Q8TC12                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Proton acceptor|||Retinol dehydrogenase 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054763|||http://purl.uniprot.org/annotation/PRO_5006608269|||http://purl.uniprot.org/annotation/VSP_008159|||http://purl.uniprot.org/annotation/VSP_046403
http://togogenome.org/gene/9606:NTMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV86                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity with CENPA.|||Decreased methyltransferase activity with CENPA.|||Decreased methyltransferase activity.|||Does not affect methyltransferase activity.|||In isoform 2.|||Induces a decrease in methyltransferase activity.|||Induces a slight decrease in methyltransferase activity.|||Induces a strong decrease in methyltransferase activity.|||Loss of methyltransferase activity.|||N-acetylmethionine|||N-acetylthreonine; in N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed|||N-terminal Xaa-Pro-Lys N-methyltransferase 1|||N-terminal Xaa-Pro-Lys N-methyltransferase 1, N-terminally processed|||Nearly abolishes methyltransferase activity with CENPA.|||Reduced methyltransferase activity with CENPA.|||Removed; alternate|||Strongly reduces methyltransferase activity with CENPA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119288|||http://purl.uniprot.org/annotation/PRO_0000423228|||http://purl.uniprot.org/annotation/VSP_039886
http://togogenome.org/gene/9606:UGT2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140T9Z0|||http://purl.uniprot.org/uniprot/D6RFW5|||http://purl.uniprot.org/uniprot/P0DTE4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 1.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036023|||http://purl.uniprot.org/annotation/PRO_5005126716|||http://purl.uniprot.org/annotation/PRO_5007305497|||http://purl.uniprot.org/annotation/VAR_024686|||http://purl.uniprot.org/annotation/VAR_057326|||http://purl.uniprot.org/annotation/VSP_061418|||http://purl.uniprot.org/annotation/VSP_061419|||http://purl.uniprot.org/annotation/VSP_061420
http://togogenome.org/gene/9606:METTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U44                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes localization to the nucleus.|||Abolishes methyltransferase activity.|||Basic and acidic residues|||Decreased methyltransferase activity.|||Disordered|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-219 and 348-A--A-350.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-219 and A-243.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-243 and 348-A--A-350.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-2; A-43 and A-48.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-2; A-43 and A-50.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-2; A-48 and A-50.|||Does not affect nuclear localization, interaction with METTL14 or WTAP or catalytic activity; when associated with A-43; A-48 and A-50.|||Found in patients with large intestine cancer; unknown pathological significance; does not affect interaction with METTL14; abolished RNA methyltransferase activity in vitro.|||Gate loop 1|||Gate loop 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Impaired RNA-binding and methyltransferase activities.|||In 3KR; decreased sumoylation. In 4KR; strongly decreased sumoylation; when associated with R-177.|||In 4KR; strongly decreased sumoylation; when associated with 211-R--R-215.|||In isoform 2.|||Interaction with METTL14|||Interphase loop|||Loss of function. Abolishes ability to regulate primary miRNA processing. Does not affect ability to promote mRNA translation. Abolishes formation of m6A at DNA damage sites.|||N-acetylserine; alternate|||N6-adenosine-methyltransferase catalytic subunit|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; alternate|||Phosphothreonine|||Polar residues|||Positively charged region required for RNA-binding|||Removed|||Slight reduction in methyltransferase activity.|||Slight reduction in methyltransferase activity. Strong reduction in methyltransferase activity; when associated with A-549.|||Slight reduction in methyltransferase activity. Strong reduction in methyltransferase activity; when associated with A-550.|||Strong reduction in methyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207630|||http://purl.uniprot.org/annotation/VAR_076859|||http://purl.uniprot.org/annotation/VSP_007864|||http://purl.uniprot.org/annotation/VSP_007865|||http://purl.uniprot.org/annotation/VSP_007866
http://togogenome.org/gene/9606:FDX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10109                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||Adrenodoxin, mitochondrial|||Disordered|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000988
http://togogenome.org/gene/9606:CENPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MT69                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Centromere protein X|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337180|||http://purl.uniprot.org/annotation/VSP_033948|||http://purl.uniprot.org/annotation/VSP_033949
http://togogenome.org/gene/9606:CPEB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLQ8|||http://purl.uniprot.org/uniprot/E5RFP2|||http://purl.uniprot.org/uniprot/Q17RY0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic polyadenylation element-binding protein 4|||Disordered|||Important for the positionning of RRM1 relative to RRM2|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||RNA-binding|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269264|||http://purl.uniprot.org/annotation/VSP_022040|||http://purl.uniprot.org/annotation/VSP_022041|||http://purl.uniprot.org/annotation/VSP_022042
http://togogenome.org/gene/9606:ANTXR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FUA5|||http://purl.uniprot.org/uniprot/J3KPY9|||http://purl.uniprot.org/uniprot/P58335|||http://purl.uniprot.org/uniprot/Q32Q26                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anthrax toxin receptor 2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HFS.|||In HFS; infantile form.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002694|||http://purl.uniprot.org/annotation/VAR_022687|||http://purl.uniprot.org/annotation/VAR_022688|||http://purl.uniprot.org/annotation/VAR_022689|||http://purl.uniprot.org/annotation/VAR_022690|||http://purl.uniprot.org/annotation/VAR_022691|||http://purl.uniprot.org/annotation/VAR_022692|||http://purl.uniprot.org/annotation/VAR_022693|||http://purl.uniprot.org/annotation/VAR_022694|||http://purl.uniprot.org/annotation/VSP_008343|||http://purl.uniprot.org/annotation/VSP_008344|||http://purl.uniprot.org/annotation/VSP_008345|||http://purl.uniprot.org/annotation/VSP_008346
http://togogenome.org/gene/9606:SELENOV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59797                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Non standard residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec); redox-active|||Disordered|||Pro residues|||Selenocysteine|||Selenoprotein V                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097675|||http://purl.uniprot.org/annotation/VAR_061790
http://togogenome.org/gene/9606:ZNF222                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK12                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 222                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047463|||http://purl.uniprot.org/annotation/VAR_052796|||http://purl.uniprot.org/annotation/VAR_052797|||http://purl.uniprot.org/annotation/VAR_052798|||http://purl.uniprot.org/annotation/VAR_061940|||http://purl.uniprot.org/annotation/VSP_046951|||http://purl.uniprot.org/annotation/VSP_046952
http://togogenome.org/gene/9606:CREB3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RA75|||http://purl.uniprot.org/uniprot/Q96BA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes proteolytic cleavage by MBTPS1.|||Abolishes proteolytic cleavage by MBTPS2.|||Abolishes proteolytic cleavage by MBTPS2; when associated with A-392.|||Abolishes proteolytic cleavage by MBTPS2; when associated with A-395.|||BZIP|||Basic motif|||Cleavage; by MBTPS1|||Cyclic AMP-responsive element-binding protein 3-like protein 1|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Leucine-zipper|||Lumenal|||MBTPS1 recognition|||MBTPS2 recognition|||N-linked (GlcNAc...) asparagine|||Polar residues|||Processed cyclic AMP-responsive element-binding protein 3-like protein 1|||Required for transcriptional activation|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288064|||http://purl.uniprot.org/annotation/PRO_0000296206|||http://purl.uniprot.org/annotation/VAR_032392|||http://purl.uniprot.org/annotation/VSP_025632
http://togogenome.org/gene/9606:MLKL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NB16                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATP-binding.|||Abolishes binding to necrosulfonamide inhibitor.|||Binds ATP with an enhanced affinity.|||Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-58.|||Does not affect formation of homotrimers, while translocation to the plasma membrane on necroptosis induction is impaired; when associated with G-76.|||Impairs ATP-binding.|||Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-162.|||Impairs formation of homotrimers and translocation to the plasma membrane on necroptosis induction; when associated with G-165.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Mimics phosphorylation state; acts as a dominant-negative mutant that impairs necroptosis.|||Mixed lineage kinase domain-like protein|||N-terminal bundle and brace (NBB); mediates INSP6 binding|||No effect. Abolishes ability to mediate necroptosis; when associated with A-357.|||No effect. Abolishes ability to mediate necroptosis; when associated with A-358.|||Phosphoserine|||Phosphoserine; by RIPK3|||Phosphothreonine; by RIPK3|||Protein kinase|||Target of necrosulfonamide inhibitor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248239|||http://purl.uniprot.org/annotation/VAR_041350|||http://purl.uniprot.org/annotation/VAR_041351|||http://purl.uniprot.org/annotation/VAR_041352|||http://purl.uniprot.org/annotation/VAR_041353|||http://purl.uniprot.org/annotation/VAR_041354|||http://purl.uniprot.org/annotation/VAR_041355|||http://purl.uniprot.org/annotation/VAR_041356|||http://purl.uniprot.org/annotation/VAR_041357|||http://purl.uniprot.org/annotation/VAR_041358|||http://purl.uniprot.org/annotation/VSP_052133|||http://purl.uniprot.org/annotation/VSP_052134
http://togogenome.org/gene/9606:SPMIP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW9|||http://purl.uniprot.org/uniprot/Q6URK8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Sperm microtubule inner protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325777|||http://purl.uniprot.org/annotation/PRO_5014247030|||http://purl.uniprot.org/annotation/VAR_060223|||http://purl.uniprot.org/annotation/VSP_032403
http://togogenome.org/gene/9606:GPM6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13491|||http://purl.uniprot.org/uniprot/Q59FD5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neuronal membrane glycoprotein M6-b|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159021|||http://purl.uniprot.org/annotation/VSP_003326|||http://purl.uniprot.org/annotation/VSP_041121|||http://purl.uniprot.org/annotation/VSP_043247
http://togogenome.org/gene/9606:STYXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZP5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine/tyrosine-interacting-like protein 2|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302838|||http://purl.uniprot.org/annotation/VAR_034964|||http://purl.uniprot.org/annotation/VAR_034965|||http://purl.uniprot.org/annotation/VAR_034966|||http://purl.uniprot.org/annotation/VAR_034967|||http://purl.uniprot.org/annotation/VAR_034968
http://togogenome.org/gene/9606:CSPG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUT8|||http://purl.uniprot.org/uniprot/B7Z2E0|||http://purl.uniprot.org/uniprot/O95196                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||CSPG5 sulphate attachment|||Chondroitin sulfate proteoglycan 5|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with GOPC|||Interaction with TNC and TNR|||N-linked (GlcNAc...) asparagine|||Neural chondroitin sulphate proteoglycan cytoplasmic|||O-linked (GalNAc...) serine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042151|||http://purl.uniprot.org/annotation/PRO_5001831922|||http://purl.uniprot.org/annotation/VAR_055089|||http://purl.uniprot.org/annotation/VAR_055090|||http://purl.uniprot.org/annotation/VSP_015760|||http://purl.uniprot.org/annotation/VSP_015761
http://togogenome.org/gene/9606:CCNYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7R7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-Y-like protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309321|||http://purl.uniprot.org/annotation/VSP_029133|||http://purl.uniprot.org/annotation/VSP_029134
http://togogenome.org/gene/9606:DNAH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6F3|||http://purl.uniprot.org/uniprot/Q8IU65|||http://purl.uniprot.org/uniprot/Q96JB1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||AAA+ ATPase|||Basic and acidic residues|||Disordered|||Dynein axonemal heavy chain 8|||Found in a patient with primary ciliary dyskinesia; unknown pathological significance.|||In SPGF46; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Stalk                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274044|||http://purl.uniprot.org/annotation/VAR_030171|||http://purl.uniprot.org/annotation/VAR_030172|||http://purl.uniprot.org/annotation/VAR_030173|||http://purl.uniprot.org/annotation/VAR_030174|||http://purl.uniprot.org/annotation/VAR_030175|||http://purl.uniprot.org/annotation/VAR_030176|||http://purl.uniprot.org/annotation/VAR_030177|||http://purl.uniprot.org/annotation/VAR_030178|||http://purl.uniprot.org/annotation/VAR_030179|||http://purl.uniprot.org/annotation/VAR_036213|||http://purl.uniprot.org/annotation/VAR_085187|||http://purl.uniprot.org/annotation/VAR_085188|||http://purl.uniprot.org/annotation/VAR_085189|||http://purl.uniprot.org/annotation/VAR_085190|||http://purl.uniprot.org/annotation/VAR_085191|||http://purl.uniprot.org/annotation/VSP_022614
http://togogenome.org/gene/9606:OR8K1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVZ6|||http://purl.uniprot.org/uniprot/Q8NGG5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8K1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150671|||http://purl.uniprot.org/annotation/VAR_034270|||http://purl.uniprot.org/annotation/VAR_034271|||http://purl.uniprot.org/annotation/VAR_034272
http://togogenome.org/gene/9606:LSS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R694|||http://purl.uniprot.org/uniprot/P48449                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In APMR4; changed localization; the protein is present in the ER but is also mislocalized to the cytoplasm.|||In APMR4; loss of protein expression.|||In APMR4; unknown pathological significance.|||In CTRCT44; associated with hypotrichosis; unknown pathological significance.|||In CTRCT44; loss of lanosterol synthase activity.|||In HYPT14; changed localization; the protein is present in the ER but is also mislocalized to the cytoplasm.|||In HYPT14; the protein is present in the ER but also mislocalized to the cytoplasm.|||In isoform 2.|||In isoform 3.|||Lanosterol synthase|||N-acetylthreonine|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||PFTB 6|||PFTB 7|||Proton donor|||Removed|||Squalene cyclase C-terminal|||Squalene cyclase N-terminal|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072659|||http://purl.uniprot.org/annotation/VAR_021522|||http://purl.uniprot.org/annotation/VAR_024648|||http://purl.uniprot.org/annotation/VAR_052057|||http://purl.uniprot.org/annotation/VAR_052058|||http://purl.uniprot.org/annotation/VAR_052059|||http://purl.uniprot.org/annotation/VAR_075664|||http://purl.uniprot.org/annotation/VAR_075665|||http://purl.uniprot.org/annotation/VAR_081921|||http://purl.uniprot.org/annotation/VAR_081922|||http://purl.uniprot.org/annotation/VAR_081923|||http://purl.uniprot.org/annotation/VAR_081924|||http://purl.uniprot.org/annotation/VAR_081925|||http://purl.uniprot.org/annotation/VAR_084019|||http://purl.uniprot.org/annotation/VAR_084020|||http://purl.uniprot.org/annotation/VAR_084021|||http://purl.uniprot.org/annotation/VAR_084022|||http://purl.uniprot.org/annotation/VAR_084023|||http://purl.uniprot.org/annotation/VAR_084024|||http://purl.uniprot.org/annotation/VAR_084025|||http://purl.uniprot.org/annotation/VAR_084026|||http://purl.uniprot.org/annotation/VAR_084027|||http://purl.uniprot.org/annotation/VAR_084028|||http://purl.uniprot.org/annotation/VSP_045407|||http://purl.uniprot.org/annotation/VSP_046188
http://togogenome.org/gene/9606:STMN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93045                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Membrane attachment|||Phosphoserine|||Regulatory/phosphorylation domain|||S-palmitoyl cysteine|||SLD|||Stathmin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182396|||http://purl.uniprot.org/annotation/VSP_045047
http://togogenome.org/gene/9606:RFK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDZ2|||http://purl.uniprot.org/uniprot/Q969G6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Loss of riboflavin kinase activity. No effect on TNFRSF1A- and CYBA-binding.|||Nucleophile|||Riboflavin kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194148
http://togogenome.org/gene/9606:AGO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCK5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||PAZ|||Piwi|||Protein argonaute-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194063
http://togogenome.org/gene/9606:TSKU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRF9|||http://purl.uniprot.org/uniprot/Q8WUA8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||Tsukushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240407|||http://purl.uniprot.org/annotation/PRO_5002790073|||http://purl.uniprot.org/annotation/VAR_026726|||http://purl.uniprot.org/annotation/VAR_028725|||http://purl.uniprot.org/annotation/VAR_028726|||http://purl.uniprot.org/annotation/VAR_028727
http://togogenome.org/gene/9606:NKX1-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15270                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Homeobox|||NK1 transcription factor-related protein 1|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333009
http://togogenome.org/gene/9606:BRD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEG9|||http://purl.uniprot.org/uniprot/B4DMS9|||http://purl.uniprot.org/uniprot/B4DN43|||http://purl.uniprot.org/uniprot/Q9H0E9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Bromo|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helical|||In isoform 2 and isoform 3.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211185|||http://purl.uniprot.org/annotation/VAR_030695|||http://purl.uniprot.org/annotation/VAR_048428|||http://purl.uniprot.org/annotation/VAR_048429|||http://purl.uniprot.org/annotation/VSP_012879|||http://purl.uniprot.org/annotation/VSP_012880|||http://purl.uniprot.org/annotation/VSP_012881|||http://purl.uniprot.org/annotation/VSP_012882|||http://purl.uniprot.org/annotation/VSP_012883|||http://purl.uniprot.org/annotation/VSP_012884|||http://purl.uniprot.org/annotation/VSP_023187|||http://purl.uniprot.org/annotation/VSP_023188|||http://purl.uniprot.org/annotation/VSP_023189|||http://purl.uniprot.org/annotation/VSP_023190|||http://purl.uniprot.org/annotation/VSP_023191
http://togogenome.org/gene/9606:FUT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51993|||http://purl.uniprot.org/uniprot/Q6P7E6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6|||Cytoplasmic|||Found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation when associated with S-124 and G-303.|||Found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation when associated with S-124 and V-244.|||Found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; complete enzyme inactivation.|||Found in individuals with plasma alpha(1,3)-fucosyltransferase deficiency and no clinically relevant phenotype; results in partial enzyme inactivation; complete enzyme inactivation when associated with V-244 and G-303.|||Fucosyltransferase N-terminal|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with W-110; D-111 and I-112. Increases VIM2 glycolipid product; when associated with W-110; D-111 and I-112.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Reduces dramatically alpha(1,3)fucosyltransferase activity towards type 2 chain acceptors. Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; D-111 and I-112. Increases VIM2 glycolipid product; when associated with T-73; D-111 and I-112.|||Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and D-111. Increases VIM2 glycolipid product; when associated with T-73; W-110 and D-111.|||Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and I-112. Increases VIM2 glycolipid product; when associated with T-73; W-110 and I-112.|||determines site-specific fucosylation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221110|||http://purl.uniprot.org/annotation/VAR_024463|||http://purl.uniprot.org/annotation/VAR_024464|||http://purl.uniprot.org/annotation/VAR_065915|||http://purl.uniprot.org/annotation/VAR_065916|||http://purl.uniprot.org/annotation/VAR_065917|||http://purl.uniprot.org/annotation/VSP_001780
http://togogenome.org/gene/9606:PLA2G2F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZM2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Group IIF secretory phospholipase A2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Required for localization on the plasma membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022759|||http://purl.uniprot.org/annotation/VSP_037524
http://togogenome.org/gene/9606:TMEM14C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0S9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 14C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221173|||http://purl.uniprot.org/annotation/VAR_046947|||http://purl.uniprot.org/annotation/VAR_046948|||http://purl.uniprot.org/annotation/VAR_046949|||http://purl.uniprot.org/annotation/VAR_046950
http://togogenome.org/gene/9606:UFL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94874                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with UFC1, impairing E3 protein ligase activity and ability to regulate ATM activation.|||Basic and acidic residues|||Disordered|||E3 UFM1-protein ligase 1|||Impaired recruitment to double-strand break sites.|||In isoform 2.|||In isoform 3.|||Involved in CDK5RAP3-binding|||Mediates interaction with CDK5RAP3|||Mediates interaction with DDRGK1|||Mediates interaction with TRIP4|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by ATM|||Removed|||Required for E3 UFM1-protein ligase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050771|||http://purl.uniprot.org/annotation/VAR_034037|||http://purl.uniprot.org/annotation/VSP_038759|||http://purl.uniprot.org/annotation/VSP_038760|||http://purl.uniprot.org/annotation/VSP_038761
http://togogenome.org/gene/9606:SCML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||Phosphoserine|||Polar residues|||SAM|||Sex comb on midleg-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097627|||http://purl.uniprot.org/annotation/VSP_037800|||http://purl.uniprot.org/annotation/VSP_037801
http://togogenome.org/gene/9606:ITGA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13612                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes almost completely cleavage.|||Abolishes completely cleavage.|||Abolishes phosphorylation.|||Blocks binding to PLA2G2A.|||Cleavage|||Cytoplasmic|||Disrupts PXN binding.|||Extracellular|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||In isoform 2.|||Integrin alpha-4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduces PXN binding.|||SG1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016244|||http://purl.uniprot.org/annotation/VAR_003978|||http://purl.uniprot.org/annotation/VAR_047423|||http://purl.uniprot.org/annotation/VAR_047424|||http://purl.uniprot.org/annotation/VSP_056612|||http://purl.uniprot.org/annotation/VSP_056613
http://togogenome.org/gene/9606:PSMA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A109NGN6|||http://purl.uniprot.org/uniprot/P28066                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||O-linked (GlcNAc) serine|||Phosphoserine|||Phosphothreonine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124117|||http://purl.uniprot.org/annotation/VSP_046241
http://togogenome.org/gene/9606:MMD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY49                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Lumenal|||Monocyte to macrophage differentiation factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218857|||http://purl.uniprot.org/annotation/VSP_011486|||http://purl.uniprot.org/annotation/VSP_045589
http://togogenome.org/gene/9606:CD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30203|||http://purl.uniprot.org/uniprot/Q6AZ88|||http://purl.uniprot.org/uniprot/Q8N4Q7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ALCAM.|||Adds an additional glycosylation site and impairs interaction with ALCAM.|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 6.|||In isoform 7.|||In isoform CD6B, isoform CD6C and isoform CD6D.|||In isoform CD6B.|||In isoform CD6C and isoform CD6E.|||In isoform CD6D and isoform CD6E.|||N-linked (GlcNAc...) asparagine|||Nearly abolishes interaction with ALCAM.|||Phosphotyrosine|||Polar residues|||Reduces interaction with ALCAM.|||Reduces tyrosine phosphorylation. Reduces affinity for LCP2. Impairs activation of T-cells.|||SRCR|||SRCR 1|||SRCR 2|||SRCR 3|||Soluble CD6|||Strongly reduces interaction with ALCAM.|||T-cell differentiation antigen CD6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033227|||http://purl.uniprot.org/annotation/PRO_0000435133|||http://purl.uniprot.org/annotation/PRO_5004271765|||http://purl.uniprot.org/annotation/PRO_5004311175|||http://purl.uniprot.org/annotation/VAR_057202|||http://purl.uniprot.org/annotation/VAR_057203|||http://purl.uniprot.org/annotation/VAR_057204|||http://purl.uniprot.org/annotation/VAR_057205|||http://purl.uniprot.org/annotation/VAR_059809|||http://purl.uniprot.org/annotation/VAR_060790|||http://purl.uniprot.org/annotation/VSP_006221|||http://purl.uniprot.org/annotation/VSP_006222|||http://purl.uniprot.org/annotation/VSP_006223|||http://purl.uniprot.org/annotation/VSP_054245|||http://purl.uniprot.org/annotation/VSP_054246|||http://purl.uniprot.org/annotation/VSP_061447
http://togogenome.org/gene/9606:H2AC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4FTV9|||http://purl.uniprot.org/uniprot/P0C0S8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Blocks the inhibition of transcription by RPS6KA5/MSK1.|||Citrulline; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A C-terminal|||Histone H2A type 1|||Histone H2A/H2B/H3|||Monoisotopic with N-acetylserine.|||N-acetylserine|||N5-methylglutamine|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by RPS6KA5|||Phosphothreonine; by DCAF1|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055235
http://togogenome.org/gene/9606:SUPT7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94864                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||STAGA complex 65 subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072233|||http://purl.uniprot.org/annotation/VSP_003974|||http://purl.uniprot.org/annotation/VSP_054839
http://togogenome.org/gene/9606:DDIT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes inhibition of mTORC1.|||DNA damage-inducible transcript 4 protein|||Disordered|||Mildly reduces inhibition of mTORC1.|||No effect on inhibition of mTORC1.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces inhibition of mTORC1.|||Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-219.|||Reduces inhibition of mTORC1. Abolishes inhibition of mTORC1; when associated with A-222.|||Strongly inhibits proteasomal degradation.|||Strongly inhibits proteasomal degradation. Strongly inhibits proteasomal degradation; when associated with A-25.|||Strongly inhibits proteasomal degradation; when associated with A-23.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307197
http://togogenome.org/gene/9606:CTBS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01459|||http://purl.uniprot.org/uniprot/Q8TC97                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Di-N-acetylchitobiase|||GH18|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011961|||http://purl.uniprot.org/annotation/PRO_5014312349|||http://purl.uniprot.org/annotation/VAR_020160|||http://purl.uniprot.org/annotation/VAR_049197
http://togogenome.org/gene/9606:SPDYE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Speedy protein E3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342336|||http://purl.uniprot.org/annotation/VSP_040737
http://togogenome.org/gene/9606:LINGO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C6S8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326529|||http://purl.uniprot.org/annotation/VAR_059395
http://togogenome.org/gene/9606:PRR29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG13|||http://purl.uniprot.org/uniprot/P0C7W0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DUF4587|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Pro residues|||Proline-rich protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344468|||http://purl.uniprot.org/annotation/VAR_069055|||http://purl.uniprot.org/annotation/VSP_045344|||http://purl.uniprot.org/annotation/VSP_045345|||http://purl.uniprot.org/annotation/VSP_045346|||http://purl.uniprot.org/annotation/VSP_046997
http://togogenome.org/gene/9606:ASB16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NS5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and SOCS box protein 16|||Found in a clear cell renal carcinoma case; somatic mutation.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066956|||http://purl.uniprot.org/annotation/VAR_059127|||http://purl.uniprot.org/annotation/VAR_064697
http://togogenome.org/gene/9606:DCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40126                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In OCA8.|||In isoform 2.|||L-dopachrome tautomerase|||Lumenal, melanosome|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035892|||http://purl.uniprot.org/annotation/VAR_085343|||http://purl.uniprot.org/annotation/VAR_085344|||http://purl.uniprot.org/annotation/VSP_043581
http://togogenome.org/gene/9606:CYP8B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNU6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase|||Helical|||Phosphoserine|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051913|||http://purl.uniprot.org/annotation/VAR_010381|||http://purl.uniprot.org/annotation/VAR_055102|||http://purl.uniprot.org/annotation/VAR_055103|||http://purl.uniprot.org/annotation/VAR_055104
http://togogenome.org/gene/9606:NUDT8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV74                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrial coenzyme A diphosphatase NUDT8|||N6-succinyllysine|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019948|||http://purl.uniprot.org/annotation/VSP_014282|||http://purl.uniprot.org/annotation/VSP_014283
http://togogenome.org/gene/9606:IRAK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAP9|||http://purl.uniprot.org/uniprot/B4E359|||http://purl.uniprot.org/uniprot/Q69FE3|||http://purl.uniprot.org/uniprot/Q9NWZ3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Death|||Disordered|||In IMD67; decreases inhibition of NF-kappa-B complex activation; impairs neutrophil migration and phagocytosis.|||In IMD67; no effect on inhibition of NF-kappa-B complex activation; loss of interaction with MYD88; decreases protein stability.|||In isoform 2.|||Increases inhibition of NF-kappa-B complex activation; decreases interaction with MYD88; decreases protein stability.|||Interleukin-1 receptor-associated kinase 4|||Loss of kinase activity.|||N-acetylmethionine|||N6-acetyllysine|||No effect on inhibition of NF-kappa-B activation; no effect on interaction with MYD88.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086035|||http://purl.uniprot.org/annotation/VAR_019354|||http://purl.uniprot.org/annotation/VAR_019355|||http://purl.uniprot.org/annotation/VAR_019356|||http://purl.uniprot.org/annotation/VAR_040588|||http://purl.uniprot.org/annotation/VAR_040589|||http://purl.uniprot.org/annotation/VAR_040590|||http://purl.uniprot.org/annotation/VAR_072888|||http://purl.uniprot.org/annotation/VAR_072889|||http://purl.uniprot.org/annotation/VAR_072890|||http://purl.uniprot.org/annotation/VAR_072891|||http://purl.uniprot.org/annotation/VAR_072892|||http://purl.uniprot.org/annotation/VSP_041556
http://togogenome.org/gene/9606:EN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19622                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein engrailed-2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000196067|||http://purl.uniprot.org/annotation/VAR_021985
http://togogenome.org/gene/9606:ZNF607                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SK3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 20|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; degenerate|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 607                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047689|||http://purl.uniprot.org/annotation/VAR_057974|||http://purl.uniprot.org/annotation/VAR_057975|||http://purl.uniprot.org/annotation/VAR_057976|||http://purl.uniprot.org/annotation/VAR_057977|||http://purl.uniprot.org/annotation/VAR_057978|||http://purl.uniprot.org/annotation/VAR_058306|||http://purl.uniprot.org/annotation/VAR_058307|||http://purl.uniprot.org/annotation/VSP_037503|||http://purl.uniprot.org/annotation/VSP_046843
http://togogenome.org/gene/9606:ITPRIPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6GPH6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Inositol 1,4,5-trisphosphate receptor-interacting protein-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320566|||http://purl.uniprot.org/annotation/VAR_039209|||http://purl.uniprot.org/annotation/VAR_039210|||http://purl.uniprot.org/annotation/VAR_039211|||http://purl.uniprot.org/annotation/VSP_031666|||http://purl.uniprot.org/annotation/VSP_054316
http://togogenome.org/gene/9606:H1-10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92522                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Citrulline|||Disordered|||H15|||Histone H1.10|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195912
http://togogenome.org/gene/9606:NENF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Cytochrome b5 heme-binding|||Disordered|||N6-acetyllysine|||Neudesin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018598
http://togogenome.org/gene/9606:ZIK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS08|||http://purl.uniprot.org/uniprot/B3KY01|||http://purl.uniprot.org/uniprot/F5H435|||http://purl.uniprot.org/uniprot/Q3SY52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||In isoform 3.|||KRAB|||Polar residues|||Zinc finger protein interacting with ribonucleoprotein K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286793|||http://purl.uniprot.org/annotation/VSP_025147|||http://purl.uniprot.org/annotation/VSP_025148
http://togogenome.org/gene/9606:PCID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JVF3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||PCI|||PCI domain-containing protein 2|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121029|||http://purl.uniprot.org/annotation/VSP_016843|||http://purl.uniprot.org/annotation/VSP_016844|||http://purl.uniprot.org/annotation/VSP_016845
http://togogenome.org/gene/9606:IFNL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZJ0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Interferon lambda-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015509|||http://purl.uniprot.org/annotation/VAR_053384|||http://purl.uniprot.org/annotation/VAR_053385
http://togogenome.org/gene/9606:CYGB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1K0FUB6|||http://purl.uniprot.org/uniprot/Q8WWM9                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Cytoglobin|||Globin|||Globin family profile|||Interchain (with C-38)|||Interchain (with C-83)|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053384
http://togogenome.org/gene/9606:RBM8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A023T787|||http://purl.uniprot.org/uniprot/Q9Y5S9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Complete loss of nonsense-mediated decay activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired nonsense-mediated decay activity.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||RNA-binding protein 8A|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081763|||http://purl.uniprot.org/annotation/VSP_005810
http://togogenome.org/gene/9606:TOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11387|||http://purl.uniprot.org/uniprot/Q9BVT2                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  5-fold decrease in sumoylation. Localizes in both nucleoplasm and nucleoli; when associated with or without R-103 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-153.|||Almost abolishes enzyme activity.|||Basic and acidic residues|||DNA topoisomerase 1|||DNA topoisomerase I eukaryotic-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In CPT-resistant leukemia.|||In CPT-resistant lung cancer.|||In breast cancer; somatic mutation.|||Interaction with DNA|||Localizes in both nucleoplasm and nucleoli; when associated with R-103 or R-117. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-117.|||Localizes in both nucleoplasm and nucleoli; when associated with R-117 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-117 and R-153.|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No change in CPT-induced clearing from nuclei.|||O-(3'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphoserine; by CK2|||Removed|||Strongly reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145201|||http://purl.uniprot.org/annotation/VAR_007530|||http://purl.uniprot.org/annotation/VAR_007531|||http://purl.uniprot.org/annotation/VAR_010666|||http://purl.uniprot.org/annotation/VAR_010667|||http://purl.uniprot.org/annotation/VAR_036555|||http://purl.uniprot.org/annotation/VAR_052592
http://togogenome.org/gene/9606:ANKIB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2G1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat and IBR domain-containing protein 1|||Disordered|||IBR-type|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||RING-type 1|||RING-type 2; atypical|||Removed|||TRIAD supradomain|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066892|||http://purl.uniprot.org/annotation/VAR_030862
http://togogenome.org/gene/9606:ATL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCN0|||http://purl.uniprot.org/uniprot/B7Z2H0|||http://purl.uniprot.org/uniprot/Q8NHH9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alters endoplasmic reticulum morphogenesis.|||Alters endoplasmic reticulum morphology.|||Atlastin-2|||Cytoplasmic|||Disordered|||GB1/RHD3-type G|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Lumenal|||N6-methyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287105|||http://purl.uniprot.org/annotation/VAR_032265|||http://purl.uniprot.org/annotation/VAR_032266|||http://purl.uniprot.org/annotation/VAR_032267|||http://purl.uniprot.org/annotation/VSP_025309|||http://purl.uniprot.org/annotation/VSP_025310|||http://purl.uniprot.org/annotation/VSP_041604|||http://purl.uniprot.org/annotation/VSP_041605
http://togogenome.org/gene/9606:SHPK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2A0|||http://purl.uniprot.org/uniprot/Q9UHJ6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Carbohydrate kinase FGGY N-terminal|||Sedoheptulokinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059564|||http://purl.uniprot.org/annotation/VAR_042580|||http://purl.uniprot.org/annotation/VAR_048591|||http://purl.uniprot.org/annotation/VAR_048592
http://togogenome.org/gene/9606:SAP130                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YDB8|||http://purl.uniprot.org/uniprot/H7BXF5|||http://purl.uniprot.org/uniprot/Q96DP1|||http://purl.uniprot.org/uniprot/Q9H0E3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP130|||Histone deacetylase complex subunit SAP130 C-terminal|||In isoform 2 and isoform 3.|||In isoform 2.|||Interactions with SIN3A and HDAC1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283736|||http://purl.uniprot.org/annotation/VSP_024355|||http://purl.uniprot.org/annotation/VSP_024356
http://togogenome.org/gene/9606:MTHFS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49914                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-formyltetrahydrofolate cyclo-ligase|||In NEDMEHM.|||In isoform 2.|||N-acetylalanine|||Reduces activity by 87%.|||Reduces activity by 93%.|||Reduces activity by 94%.|||Reduces activity by 97%.|||Reduces activity by 98%.|||Reduces activity by 99%.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200275|||http://purl.uniprot.org/annotation/VAR_034115|||http://purl.uniprot.org/annotation/VAR_082088|||http://purl.uniprot.org/annotation/VAR_082089|||http://purl.uniprot.org/annotation/VAR_082090|||http://purl.uniprot.org/annotation/VSP_046863
http://togogenome.org/gene/9606:BRINP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60477                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BMP/retinoic acid-inducible neural-specific protein 1|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||MACPF|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045766|||http://purl.uniprot.org/annotation/VAR_024930|||http://purl.uniprot.org/annotation/VAR_029989|||http://purl.uniprot.org/annotation/VAR_029990|||http://purl.uniprot.org/annotation/VAR_036336|||http://purl.uniprot.org/annotation/VSP_017021|||http://purl.uniprot.org/annotation/VSP_017022|||http://purl.uniprot.org/annotation/VSP_017023
http://togogenome.org/gene/9606:HMCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HLC3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||EGF-like|||Ig-like|||Nidogen G2 beta-barrel                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5035170362
http://togogenome.org/gene/9606:RSPO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2I0M5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FU|||In NDNC4.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||R-spondin-4|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234446|||http://purl.uniprot.org/annotation/VAR_030399|||http://purl.uniprot.org/annotation/VAR_030400|||http://purl.uniprot.org/annotation/VAR_030401|||http://purl.uniprot.org/annotation/VAR_030402|||http://purl.uniprot.org/annotation/VAR_052665|||http://purl.uniprot.org/annotation/VSP_018325
http://togogenome.org/gene/9606:FBXW9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XUX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box/WD repeat-containing protein 9|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050999|||http://purl.uniprot.org/annotation/VAR_057599|||http://purl.uniprot.org/annotation/VAR_062097|||http://purl.uniprot.org/annotation/VSP_060706|||http://purl.uniprot.org/annotation/VSP_060707
http://togogenome.org/gene/9606:TTC34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYJ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||Tetratricopeptide repeat protein 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341278
http://togogenome.org/gene/9606:GSTA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16772|||http://purl.uniprot.org/uniprot/Q5JW85                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase A3|||N-acetylalanine|||N6-succinyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185785|||http://purl.uniprot.org/annotation/VAR_049484|||http://purl.uniprot.org/annotation/VAR_049485|||http://purl.uniprot.org/annotation/VAR_062276|||http://purl.uniprot.org/annotation/VAR_062277|||http://purl.uniprot.org/annotation/VAR_062278
http://togogenome.org/gene/9606:EXOSC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01780                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Exosome complex component 10|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||HRDC|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087133|||http://purl.uniprot.org/annotation/VSP_004362
http://togogenome.org/gene/9606:RASSF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02833                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Pro residues|||Ras association domain-containing protein 7|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097173|||http://purl.uniprot.org/annotation/VAR_021859|||http://purl.uniprot.org/annotation/VAR_021860|||http://purl.uniprot.org/annotation/VSP_004136|||http://purl.uniprot.org/annotation/VSP_004137|||http://purl.uniprot.org/annotation/VSP_045623
http://togogenome.org/gene/9606:KCTD21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0X4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes interaction with CUL3.|||BTB|||BTB/POZ domain-containing protein KCTD21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281151
http://togogenome.org/gene/9606:FAAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2C6G4|||http://purl.uniprot.org/uniprot/Q6GMR7                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Acyl-ester intermediate|||Amidase|||Charge relay system|||Fatty-acid amide hydrolase 2|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291993
http://togogenome.org/gene/9606:MAPKAPK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49137                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory helix|||Bipartite nuclear localization signal 1|||Bipartite nuclear localization signal 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2.|||Induces decreased sumoylation and increase in protein kinase activity.|||Kinase defective mutant, abolishes activity.|||MAP kinase-activated protein kinase 2|||Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-222.|||Mimicks phosphorylation state and constitutive protein kinase activity; when associated with E-334.|||Mimicks phosphorylation state, leading to elevated basal kinase activity.|||Mimicks phosphorylation state, leading to slight increase of basal kinase activity.|||Nuclear export signal (NES)|||Phosphoserine|||Phosphoserine; by MAPK14|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by MAPK14|||Pro residues|||Protein kinase|||Proton acceptor|||Slight decrease in kinase activity.|||Strong decrease in kinase activity.|||p38 MAPK-binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086288|||http://purl.uniprot.org/annotation/VAR_040753|||http://purl.uniprot.org/annotation/VAR_040754|||http://purl.uniprot.org/annotation/VSP_004910
http://togogenome.org/gene/9606:TBL1Y                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ87                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  F-box-like|||F-box-like/WD repeat-containing protein TBL1Y|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DFNY2; unknown pathological significance; increased protein degradation.|||LisH|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051264|||http://purl.uniprot.org/annotation/VAR_082113
http://togogenome.org/gene/9606:ZNF483                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P088|||http://purl.uniprot.org/uniprot/Q8TF39                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||SCAN box|||Zinc finger protein 483                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047610|||http://purl.uniprot.org/annotation/VSP_043023|||http://purl.uniprot.org/annotation/VSP_043024
http://togogenome.org/gene/9606:CBLIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27352                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cobalamin binding intrinsic factor|||In IFD.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005558|||http://purl.uniprot.org/annotation/VAR_022742|||http://purl.uniprot.org/annotation/VAR_022743|||http://purl.uniprot.org/annotation/VAR_022744|||http://purl.uniprot.org/annotation/VAR_048753|||http://purl.uniprot.org/annotation/VSP_041585
http://togogenome.org/gene/9606:PAPOLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGK1|||http://purl.uniprot.org/uniprot/P51003                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||In isoform 2.|||Interaction with RNA|||N6-acetyllysine|||N6-acetyllysine; alternate|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Polar residues|||Poly(A) polymerase alpha|||Poly(A) polymerase central|||Polymerase nucleotidyl transferase|||Removed|||Required for interaction with NUDT21|||Ser/Thr-rich                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051612|||http://purl.uniprot.org/annotation/VSP_012895|||http://purl.uniprot.org/annotation/VSP_012896
http://togogenome.org/gene/9606:LRP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4F1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||Low-density lipoprotein receptor-related protein 10|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017335|||http://purl.uniprot.org/annotation/VAR_018172|||http://purl.uniprot.org/annotation/VAR_034097|||http://purl.uniprot.org/annotation/VSP_009820
http://togogenome.org/gene/9606:PSG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11465                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014909|||http://purl.uniprot.org/annotation/VAR_016039|||http://purl.uniprot.org/annotation/VAR_049918|||http://purl.uniprot.org/annotation/VAR_049919|||http://purl.uniprot.org/annotation/VAR_049920
http://togogenome.org/gene/9606:KLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYH5|||http://purl.uniprot.org/uniprot/Q86Z14                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-klotho|||Cytoplasmic|||Extracellular|||Glycosyl hydrolase-1 1|||Glycosyl hydrolase-1 2|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063905|||http://purl.uniprot.org/annotation/VAR_034053|||http://purl.uniprot.org/annotation/VAR_034054|||http://purl.uniprot.org/annotation/VAR_034055|||http://purl.uniprot.org/annotation/VAR_049296|||http://purl.uniprot.org/annotation/VAR_061207
http://togogenome.org/gene/9606:KCNV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIU1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Potassium voltage-gated channel subfamily V member 1|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308350|||http://purl.uniprot.org/annotation/VAR_036804
http://togogenome.org/gene/9606:BIVM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic immunoglobulin-like variable motif-containing protein|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328955|||http://purl.uniprot.org/annotation/VSP_032855|||http://purl.uniprot.org/annotation/VSP_032856
http://togogenome.org/gene/9606:POTEG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S5H5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||In isoform 1.|||In isoform 2.|||POTE ankyrin domain family member G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066916|||http://purl.uniprot.org/annotation/VSP_040056|||http://purl.uniprot.org/annotation/VSP_040057
http://togogenome.org/gene/9606:MRI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV20                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||In isoform 2.|||Methylthioribose-1-phosphate isomerase|||N-acetylmethionine|||Proton donor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317325|||http://purl.uniprot.org/annotation/VAR_059253|||http://purl.uniprot.org/annotation/VAR_059254|||http://purl.uniprot.org/annotation/VSP_030935
http://togogenome.org/gene/9606:TM2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX73                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TM2 domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298982|||http://purl.uniprot.org/annotation/VSP_027495
http://togogenome.org/gene/9606:UBE3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05086|||http://purl.uniprot.org/uniprot/Q9H2G0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C4-type; atypical|||Disordered|||Disrupt trimer formation, 50-fold reduction in E3 ligase activity.|||E6-binding|||Glycyl thioester intermediate|||HECT|||In AS.|||In AS; unknown pathological significance.|||In isoform I.|||In isoform III.|||Interaction with HCV core protein|||May be associated with AS.|||Phosphoserine|||Phosphotyrosine; by ABL1|||Polar residues|||Ubiquitin-protein ligase E3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194980|||http://purl.uniprot.org/annotation/VAR_007852|||http://purl.uniprot.org/annotation/VAR_007853|||http://purl.uniprot.org/annotation/VAR_008142|||http://purl.uniprot.org/annotation/VAR_008143|||http://purl.uniprot.org/annotation/VAR_008144|||http://purl.uniprot.org/annotation/VAR_047516|||http://purl.uniprot.org/annotation/VAR_073196|||http://purl.uniprot.org/annotation/VAR_073197|||http://purl.uniprot.org/annotation/VAR_073198|||http://purl.uniprot.org/annotation/VAR_073199|||http://purl.uniprot.org/annotation/VAR_073200|||http://purl.uniprot.org/annotation/VAR_073201|||http://purl.uniprot.org/annotation/VAR_073202|||http://purl.uniprot.org/annotation/VAR_073203|||http://purl.uniprot.org/annotation/VAR_073204|||http://purl.uniprot.org/annotation/VAR_073205|||http://purl.uniprot.org/annotation/VAR_073206|||http://purl.uniprot.org/annotation/VAR_073207|||http://purl.uniprot.org/annotation/VAR_073208|||http://purl.uniprot.org/annotation/VAR_073209|||http://purl.uniprot.org/annotation/VAR_073210|||http://purl.uniprot.org/annotation/VAR_073211|||http://purl.uniprot.org/annotation/VAR_073212|||http://purl.uniprot.org/annotation/VAR_073213|||http://purl.uniprot.org/annotation/VAR_073214|||http://purl.uniprot.org/annotation/VAR_073215|||http://purl.uniprot.org/annotation/VAR_073216|||http://purl.uniprot.org/annotation/VAR_073217|||http://purl.uniprot.org/annotation/VAR_073218|||http://purl.uniprot.org/annotation/VSP_006705|||http://purl.uniprot.org/annotation/VSP_006706
http://togogenome.org/gene/9606:CCNF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41002|||http://purl.uniprot.org/uniprot/Q59HD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes the interaction with CP110 and RRM2; when associated with A-309.|||Cyclin N-terminal|||Cyclin-F|||D box 1|||D box 2|||D box 3|||D box 4|||D box 5|||Disordered|||F-box|||Impairs interaction with SKP1 and CUL1 and prevents degradation of CP110, leading to promote the formation of micronuclei. Increased interaction with RRM2 and lack of RRM2 ubiquitination.|||In FTDALS5; impaired degradation by the ubiquitin proteasome system (UPS).|||In FTDALS5; increased 'Lys-48'-linked polyubiquitination of proteins targeted for proteasomal degradation, but no increase in 'Lys-63'-linked polyubiquitinated proteins; accumulation of ubiquitinated proteins including RRM2 and TARDBP/TDP43; impaired autophagosome-lysosome fusion; impaired degradation by the ubiquitin proteasome system (UPS); increased levels of ubiquitinated autophagy receptor SQSTM1/p62.|||In FTDALS5; unknown pathological significance.|||In FTDALS5; unknown pathological significance; impaired degradation by the ubiquitin proteasome system (UPS).|||Nuclear localization signal 1|||Nuclear localization signal 2|||PEST|||Polar residues|||Reduced degradation of RRM2 after UV-induced DNA-damage. Abolishes the interaction with CP110 and RRM2; when associated with A-352.|||Reduces the interaction with FZR1/CDH1.|||Reduces the interaction with FZR1/CDH1. Abolishes the interaction with FZR1/CDH1; when associated with 310-R--L-313. Loss of ubiquitination and impaired degradation; when associated with 310-R--L-313.|||Reduces the interaction with FZR1/CDH1. Reduced ubiquitination. Abolishes the interaction with FZR1/CDH1; when associated with 351-R--L-354. Loss of ubiquitination and impaired degradation; when associated with 351-R--L-354.|||Reduces the interaction with MYBL2/BMYB. Disrupts the interaction with CDC6. Does not disrupt interaction with CUL1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080463|||http://purl.uniprot.org/annotation/VAR_085177|||http://purl.uniprot.org/annotation/VAR_085178|||http://purl.uniprot.org/annotation/VAR_085179|||http://purl.uniprot.org/annotation/VAR_085180|||http://purl.uniprot.org/annotation/VAR_085181|||http://purl.uniprot.org/annotation/VAR_085182|||http://purl.uniprot.org/annotation/VAR_085183|||http://purl.uniprot.org/annotation/VAR_085184|||http://purl.uniprot.org/annotation/VAR_085185|||http://purl.uniprot.org/annotation/VAR_085186
http://togogenome.org/gene/9606:MRPS34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JJ19|||http://purl.uniprot.org/uniprot/P82930                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In COXPD32.|||In COXPD32; significant decrease in protein levels; destabilizes the small ribosomal subunit resulting in impaired mitochondrial translation.|||Small ribosomal subunit protein mS34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087730|||http://purl.uniprot.org/annotation/VAR_052050|||http://purl.uniprot.org/annotation/VAR_080218|||http://purl.uniprot.org/annotation/VAR_080219|||http://purl.uniprot.org/annotation/VAR_080220
http://togogenome.org/gene/9606:HEMK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK98|||http://purl.uniprot.org/uniprot/B2RA37|||http://purl.uniprot.org/uniprot/Q9Y5R4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  MTRF1L release factor glutamine methyltransferase|||Methyltransferase small|||Release factor glutamine methyltransferase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157178|||http://purl.uniprot.org/annotation/VAR_049503|||http://purl.uniprot.org/annotation/VAR_049504
http://togogenome.org/gene/9606:TMEM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALM5|||http://purl.uniprot.org/uniprot/B4E1H4|||http://purl.uniprot.org/uniprot/Q9P0T7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton-transporting V-type ATPase complex assembly regulator TMEM9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034374|||http://purl.uniprot.org/annotation/PRO_5002759923|||http://purl.uniprot.org/annotation/PRO_5002801107
http://togogenome.org/gene/9606:ENKD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0I2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Enkurin|||Enkurin domain-containing protein 1|||In isoform 2.|||Phosphoserine|||Pro residues|||Required for binding to microtubules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265931|||http://purl.uniprot.org/annotation/VSP_021904|||http://purl.uniprot.org/annotation/VSP_021905
http://togogenome.org/gene/9606:DUSP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75319                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Loss of activity. No effect in RNA-binding.|||No effect on phosphatase activity with ATP and ADP.|||Phosphocysteine intermediate|||Proton donor/acceptor|||RNA/RNP complex-1-interacting phosphatase|||Slightly decreases phosphatase activity with ATP. Strongly decreases phosphatase activity with ADP.|||Strongly decreases phosphatase activity with ATP and ADP.|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094816|||http://purl.uniprot.org/annotation/VSP_014136|||http://purl.uniprot.org/annotation/VSP_014137
http://togogenome.org/gene/9606:SHISA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N114                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||Protein shisa-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312878|||http://purl.uniprot.org/annotation/VAR_054031|||http://purl.uniprot.org/annotation/VSP_029953|||http://purl.uniprot.org/annotation/VSP_029954|||http://purl.uniprot.org/annotation/VSP_029955|||http://purl.uniprot.org/annotation/VSP_029956|||http://purl.uniprot.org/annotation/VSP_055712
http://togogenome.org/gene/9606:IP6K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHH9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Inositol hexakisphosphate kinase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066877|||http://purl.uniprot.org/annotation/VSP_010925|||http://purl.uniprot.org/annotation/VSP_010926|||http://purl.uniprot.org/annotation/VSP_010927|||http://purl.uniprot.org/annotation/VSP_010928|||http://purl.uniprot.org/annotation/VSP_042698|||http://purl.uniprot.org/annotation/VSP_042699|||http://purl.uniprot.org/annotation/VSP_042700|||http://purl.uniprot.org/annotation/VSP_042845|||http://purl.uniprot.org/annotation/VSP_045416|||http://purl.uniprot.org/annotation/VSP_045417
http://togogenome.org/gene/9606:RIOK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVS4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autophosphorylation; impairs release of pre-40S trans-acting factors and rRNA processing; when associated with A-123.|||Abolishes autophosphorylation; impairs release of pre-40S trans-acting factors and rRNA processing; when associated with A-246.|||Does not affect autophosphorylation activity; when associated with A-335 and A-380. Does not affect the timing of metaphase-anaphase transition; when associated with A-335 and A-380.|||Does not affect autophosphorylation activity; when associated with A-335 and A-548. Does not affect the timing of metaphase-anaphase transition; when associated with A-335 and A-548.|||Does not affect autophosphorylation activity; when associated with A-380 and A-548. Does not affect the timing of metaphase-anaphase transition; when associated with A-380 and A-548.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||Increases time spent in metaphase; when associated with D-335 and D-380.|||Increases time spent in metaphase; when associated with D-335 and D-548.|||Increases time spent in metaphase; when associated with D-380 and D-548.|||Nuclear export signal|||Nuclear relocalization; when associated with A-400.|||Nuclear relocalization; when associated with A-403.|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase RIO2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213527|||http://purl.uniprot.org/annotation/VAR_031597|||http://purl.uniprot.org/annotation/VAR_031598|||http://purl.uniprot.org/annotation/VAR_031599|||http://purl.uniprot.org/annotation/VAR_042347|||http://purl.uniprot.org/annotation/VAR_042348|||http://purl.uniprot.org/annotation/VAR_042349|||http://purl.uniprot.org/annotation/VAR_042350|||http://purl.uniprot.org/annotation/VAR_042351|||http://purl.uniprot.org/annotation/VAR_042352|||http://purl.uniprot.org/annotation/VAR_042353|||http://purl.uniprot.org/annotation/VAR_042354|||http://purl.uniprot.org/annotation/VSP_046388
http://togogenome.org/gene/9606:NPY4R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DQD5|||http://purl.uniprot.org/uniprot/P50391                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide Y receptor type 4|||Neuropeptide Y receptor type 4-2|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069935|||http://purl.uniprot.org/annotation/PRO_0000446660|||http://purl.uniprot.org/annotation/VAR_030337|||http://purl.uniprot.org/annotation/VAR_030338
http://togogenome.org/gene/9606:JCAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P266                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Junctional cadherin 5-associated protein|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314185|||http://purl.uniprot.org/annotation/VAR_037867|||http://purl.uniprot.org/annotation/VAR_037868|||http://purl.uniprot.org/annotation/VAR_037869|||http://purl.uniprot.org/annotation/VAR_037870|||http://purl.uniprot.org/annotation/VAR_037871|||http://purl.uniprot.org/annotation/VAR_037872
http://togogenome.org/gene/9606:SLC1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT87|||http://purl.uniprot.org/uniprot/A0A087X0U3|||http://purl.uniprot.org/uniprot/B4DF14|||http://purl.uniprot.org/uniprot/P43003|||http://purl.uniprot.org/uniprot/Q7Z5T0|||http://purl.uniprot.org/uniprot/Q8N169                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Discontinuously helical|||Excitatory amino acid transporter 1|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In EA6.|||In isoform 2.|||Loss of electrogenic glutamate transport. Strongly decreased L-aspartate and L-glutamate uptake combined with strongly increased permeability ot other ions; when associated with M-477.|||No effect on activity.|||Phosphoserine|||Strongly decreased L-aspartate and L-glutamate uptake combined with strongly increased permeability ot other ions; when associated with R-363.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202057|||http://purl.uniprot.org/annotation/VAR_011877|||http://purl.uniprot.org/annotation/VAR_031733|||http://purl.uniprot.org/annotation/VSP_043913
http://togogenome.org/gene/9606:ANAPC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM13                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 10|||DOC|||N-acetylthreonine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174011|||http://purl.uniprot.org/annotation/VAR_025200
http://togogenome.org/gene/9606:EIF3G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75821                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 3 subunit G|||Phosphoserine|||Phosphothreonine|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123510
http://togogenome.org/gene/9606:FRMPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJA6|||http://purl.uniprot.org/uniprot/Q5JV73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FERM|||FERM and PDZ domain-containing protein 3|||PDZ|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254650
http://togogenome.org/gene/9606:PRRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Pro residues|||Protein PRRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307338|||http://purl.uniprot.org/annotation/VSP_028720|||http://purl.uniprot.org/annotation/VSP_028721|||http://purl.uniprot.org/annotation/VSP_028722|||http://purl.uniprot.org/annotation/VSP_028723|||http://purl.uniprot.org/annotation/VSP_028724|||http://purl.uniprot.org/annotation/VSP_028725
http://togogenome.org/gene/9606:NAA30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS28|||http://purl.uniprot.org/uniprot/Q147X3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetyltransferase|||N-alpha-acetyltransferase 30|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320032|||http://purl.uniprot.org/annotation/VSP_031581
http://togogenome.org/gene/9606:ZNF594                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNC6|||http://purl.uniprot.org/uniprot/Q96JF6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16; degenerate|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23; degenerate|||C2H2-type 24|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||Zinc finger protein 594                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306878|||http://purl.uniprot.org/annotation/VAR_035333|||http://purl.uniprot.org/annotation/VAR_035334|||http://purl.uniprot.org/annotation/VAR_061957
http://togogenome.org/gene/9606:PFDN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQP4                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Prefoldin subunit 4|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124842
http://togogenome.org/gene/9606:ZNF554                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNM4|||http://purl.uniprot.org/uniprot/Q86TJ5                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 554                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274875|||http://purl.uniprot.org/annotation/VAR_052861|||http://purl.uniprot.org/annotation/VAR_052862
http://togogenome.org/gene/9606:SYS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2H4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Protein SYS1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213940|||http://purl.uniprot.org/annotation/VSP_044540
http://togogenome.org/gene/9606:SENP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC62                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Does not desumoylate CEBPB.|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Protease|||Sentrin-specific protease 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101718|||http://purl.uniprot.org/annotation/VAR_029650|||http://purl.uniprot.org/annotation/VSP_056697
http://togogenome.org/gene/9606:PTGIS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16647                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes prostaglandin-I synthase activity.|||Helical|||In allele CYP8A1*2.|||In allele CYP8A1*3.|||In allele CYP8A1*4.|||In allele CYP8A1*5; results in a significantly decreased enzyme activity.|||Prostacyclin synthase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051910|||http://purl.uniprot.org/annotation/VAR_010915|||http://purl.uniprot.org/annotation/VAR_010916|||http://purl.uniprot.org/annotation/VAR_010917|||http://purl.uniprot.org/annotation/VAR_014634|||http://purl.uniprot.org/annotation/VAR_014635|||http://purl.uniprot.org/annotation/VAR_014636|||http://purl.uniprot.org/annotation/VAR_014637|||http://purl.uniprot.org/annotation/VAR_073186
http://togogenome.org/gene/9606:OR6B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGW1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6B3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150622|||http://purl.uniprot.org/annotation/VAR_062049
http://togogenome.org/gene/9606:CEP19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LK0                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Centrosomal protein of 19 kDa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251960
http://togogenome.org/gene/9606:CT45A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHU0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A3|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308948|||http://purl.uniprot.org/annotation/VAR_075898
http://togogenome.org/gene/9606:IGFL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXB1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Insulin growth factor-like family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000044634|||http://purl.uniprot.org/annotation/VAR_034012
http://togogenome.org/gene/9606:RIPPLY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0D2K3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Protein ripply1|||Ripply homology domain|||WRPW motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307756|||http://purl.uniprot.org/annotation/VSP_052555
http://togogenome.org/gene/9606:C19orf81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J6K1                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative uncharacterized protein C19orf81                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000413696
http://togogenome.org/gene/9606:CDC42EP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NZY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  CRIB|||Cdc42 effector protein 5|||Disordered|||Omega-N-methylarginine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212653
http://togogenome.org/gene/9606:GJD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction delta-4 protein|||Helical|||In a colorectal cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312991|||http://purl.uniprot.org/annotation/VAR_037640|||http://purl.uniprot.org/annotation/VAR_037641|||http://purl.uniprot.org/annotation/VAR_047626
http://togogenome.org/gene/9606:CHRD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ESX1|||http://purl.uniprot.org/uniprot/Q8N2W7|||http://purl.uniprot.org/uniprot/Q9H2X0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CHRD|||CHRD 1|||CHRD 2|||CHRD 3|||CHRD 4|||Chordin|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||VWFC|||VWFC 1|||VWFC 2|||VWFC 3|||VWFC 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005364|||http://purl.uniprot.org/annotation/PRO_5003217525|||http://purl.uniprot.org/annotation/VAR_021517|||http://purl.uniprot.org/annotation/VAR_048727|||http://purl.uniprot.org/annotation/VSP_001069|||http://purl.uniprot.org/annotation/VSP_001070|||http://purl.uniprot.org/annotation/VSP_001071|||http://purl.uniprot.org/annotation/VSP_001072|||http://purl.uniprot.org/annotation/VSP_001073|||http://purl.uniprot.org/annotation/VSP_001074|||http://purl.uniprot.org/annotation/VSP_001075
http://togogenome.org/gene/9606:TMSB15B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG34|||http://purl.uniprot.org/uniprot/P0CG35|||http://purl.uniprot.org/uniprot/P0DX04                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Removed|||Thymosin beta-15A|||Thymosin beta-15B|||Thymosin beta-15C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185159|||http://purl.uniprot.org/annotation/PRO_0000395401|||http://purl.uniprot.org/annotation/PRO_0000457394
http://togogenome.org/gene/9606:OR11H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW19|||http://purl.uniprot.org/uniprot/Q8NGC9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 11H4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150725|||http://purl.uniprot.org/annotation/VAR_034298
http://togogenome.org/gene/9606:KLRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E93                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITIM motif|||In isoform 2.|||Killer cell lectin-like receptor subfamily G member 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331256|||http://purl.uniprot.org/annotation/VAR_042750|||http://purl.uniprot.org/annotation/VSP_033151
http://togogenome.org/gene/9606:NIFK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Interaction with MKI67|||Loss of phosphorylation site.|||Loss of phosphorylation site. Abrogates interaction with MKI67.|||MKI67 FHA domain-interacting nucleolar phosphoprotein|||N-acetylalanine|||Omega-N-methylarginine; by PRMT1 and PRMT8|||Omega-N-methylated arginine; by PRMT1 and PRMT8|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Reduces phosphorylation at T-234 and T-238.|||Reduces phosphorylation at T-234.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081629|||http://purl.uniprot.org/annotation/VAR_027182
http://togogenome.org/gene/9606:NABP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AH0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||OB|||Polar residues|||SOSS complex subunit B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333954|||http://purl.uniprot.org/annotation/VAR_043340|||http://purl.uniprot.org/annotation/VSP_033600|||http://purl.uniprot.org/annotation/VSP_033601|||http://purl.uniprot.org/annotation/VSP_033602
http://togogenome.org/gene/9606:MYT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01538                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CCHHC-type 1|||CCHHC-type 2|||CCHHC-type 3|||CCHHC-type 4|||CCHHC-type 5|||CCHHC-type 6|||CCHHC-type 7|||Disordered|||In isoform 2.|||Myelin transcription factor 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096676|||http://purl.uniprot.org/annotation/VSP_054313
http://togogenome.org/gene/9606:GPKOW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92917                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G-patch|||G-patch domain and KOW motifs-containing protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KOW 1|||KOW 2|||N-acetylalanine|||No loss of interaction with DHX16. Reduced pre-mRNA splicing activity. Decreased ability to suppress the splicing defect observed in dominant-negative DHX16 mutant expressing cells.|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Phosphothreonine; by PKA|||Reduced phosphorylation. Significant loss of phosphorylation and increased RNA-binding; when associated with A-27.|||Reduced phosphorylation. Significant loss of phosphorylation and increased RNA-binding; when associated with A-316.|||Removed|||Significant loss of interaction with DHX16. No loss of pre-mRNA splicing activity. Able to suppress the splicing defect observed in dominant-negative DHX16 mutant expressing cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087559
http://togogenome.org/gene/9606:ARHGEF40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TER5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho guanine nucleotide exchange factor 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314822|||http://purl.uniprot.org/annotation/VAR_038061|||http://purl.uniprot.org/annotation/VAR_038062|||http://purl.uniprot.org/annotation/VAR_038063|||http://purl.uniprot.org/annotation/VAR_060541|||http://purl.uniprot.org/annotation/VSP_030381|||http://purl.uniprot.org/annotation/VSP_030382|||http://purl.uniprot.org/annotation/VSP_030383
http://togogenome.org/gene/9606:SLC27A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8P6|||http://purl.uniprot.org/uniprot/Q9Y2P4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Helical|||Long-chain fatty acid transport protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193216|||http://purl.uniprot.org/annotation/VAR_048245
http://togogenome.org/gene/9606:OTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XKR4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein orthopedia|||OAR|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292432
http://togogenome.org/gene/9606:PFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07737                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In ALS18; the mutant protein is detected in the insoluble fraction of cells.|||In ALS18; unknown pathological significance; like the wild-type the mutant protein is detected in the soluble fraction of cells.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ROCK1|||Phosphotyrosine|||Profilin-1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199571|||http://purl.uniprot.org/annotation/VAR_068925|||http://purl.uniprot.org/annotation/VAR_068926|||http://purl.uniprot.org/annotation/VAR_068927|||http://purl.uniprot.org/annotation/VAR_068928
http://togogenome.org/gene/9606:MAP3K9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZC4|||http://purl.uniprot.org/uniprot/G3V347|||http://purl.uniprot.org/uniprot/J3KPI6|||http://purl.uniprot.org/uniprot/P80192|||http://purl.uniprot.org/uniprot/Q8NEB1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Impairs JNK activation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Leucine-zipper 1|||Leucine-zipper 2|||Little effect on threonine phosphorylation. Mildly impairs JNK activation.|||Loss of kinase activity and threonine phosphorylation.|||Loss of threonine phosphorylation. Strongly impairs JNK activation.|||Mitogen-activated protein kinase kinase kinase 9|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Reduces threonine phosphorylation. Impairs JNK activation.|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086258|||http://purl.uniprot.org/annotation/VAR_040698|||http://purl.uniprot.org/annotation/VAR_040699|||http://purl.uniprot.org/annotation/VAR_040700|||http://purl.uniprot.org/annotation/VAR_040701|||http://purl.uniprot.org/annotation/VSP_013765
http://togogenome.org/gene/9606:CLCN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4H5|||http://purl.uniprot.org/uniprot/B3KRR2|||http://purl.uniprot.org/uniprot/P51795|||http://purl.uniprot.org/uniprot/V9GYG7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NEDD4 and NEDD4L.|||Abolishes proton transport, but not chloride transport.|||CBS|||CBS 1|||CBS 2|||Cytoplasmic|||Disordered|||H(+)/Cl(-) exchange transporter 5|||Helical|||In DENT1.|||In DENT1; abolishes the chloride currents.|||In DENT1; abolishes the chloride currents; total loss of function.|||In DENT1; alters targeting to endosomes.|||In DENT1; associated with a marked reduction to about 30% of wild-type chloride currents; no significant differences between the expression of the mutated and wild-type protein.|||In DENT1; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.|||In DENT1; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane.|||In DENT1; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows reduced current at the plasma membrane.|||In DENT1; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current.|||In DENT1; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional.|||In DENT1; trafficks normally to the cell surface and to early endosomes and displays complex glycosylation at the cell surface like wild-type protein; exhibits no current.|||In DENT1; trafficks normally to the cell surface and to early endosomes; endergoes complex glycosylation at the cell surface like wild-type protein but exhibits significant reductions in outwardly rectifying ion currents.|||In DENT1; unknown pathological significance.|||In LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes.|||In LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.|||In XLRHR; trafficks normally to the cell surface and to early endosomes; displays complex glycosylation at the cell surface like wild-type protein; exhibits reduced current.|||In XRN.|||In isoform 2.|||Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport|||Mediates proton transfer from the protein to the inner aqueous phase|||No effect ATP binding or chloride transport.|||Note=Loop between two helices|||Polar residues|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3|||Strongly decreased affinity for ATP, but no effect on chloride transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094446|||http://purl.uniprot.org/annotation/VAR_001615|||http://purl.uniprot.org/annotation/VAR_001616|||http://purl.uniprot.org/annotation/VAR_001617|||http://purl.uniprot.org/annotation/VAR_001618|||http://purl.uniprot.org/annotation/VAR_001619|||http://purl.uniprot.org/annotation/VAR_001620|||http://purl.uniprot.org/annotation/VAR_001621|||http://purl.uniprot.org/annotation/VAR_001622|||http://purl.uniprot.org/annotation/VAR_001623|||http://purl.uniprot.org/annotation/VAR_048694|||http://purl.uniprot.org/annotation/VAR_065591|||http://purl.uniprot.org/annotation/VAR_065592|||http://purl.uniprot.org/annotation/VAR_065593|||http://purl.uniprot.org/annotation/VAR_065594|||http://purl.uniprot.org/annotation/VAR_065595|||http://purl.uniprot.org/annotation/VAR_065596|||http://purl.uniprot.org/annotation/VAR_065597|||http://purl.uniprot.org/annotation/VAR_065598|||http://purl.uniprot.org/annotation/VAR_065599|||http://purl.uniprot.org/annotation/VAR_065600|||http://purl.uniprot.org/annotation/VAR_065601|||http://purl.uniprot.org/annotation/VAR_065602|||http://purl.uniprot.org/annotation/VAR_065603|||http://purl.uniprot.org/annotation/VAR_065604|||http://purl.uniprot.org/annotation/VAR_065605|||http://purl.uniprot.org/annotation/VAR_065606|||http://purl.uniprot.org/annotation/VAR_065607|||http://purl.uniprot.org/annotation/VAR_065608|||http://purl.uniprot.org/annotation/VAR_065609|||http://purl.uniprot.org/annotation/VAR_065610|||http://purl.uniprot.org/annotation/VAR_065611|||http://purl.uniprot.org/annotation/VAR_065612|||http://purl.uniprot.org/annotation/VAR_065613|||http://purl.uniprot.org/annotation/VAR_065614|||http://purl.uniprot.org/annotation/VAR_065615|||http://purl.uniprot.org/annotation/VAR_075519|||http://purl.uniprot.org/annotation/VSP_060654
http://togogenome.org/gene/9606:HIGD1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P298                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||HIG1|||HIG1 domain family member 1B|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215774|||http://purl.uniprot.org/annotation/VAR_049354|||http://purl.uniprot.org/annotation/VAR_049355
http://togogenome.org/gene/9606:ABCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBJ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||ATP-binding cassette sub-family D member 2|||Helical|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||Interaction with PEX19|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093306|||http://purl.uniprot.org/annotation/VAR_062664
http://togogenome.org/gene/9606:USP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJZ1|||http://purl.uniprot.org/uniprot/P45974                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased rate of activity and decreased zinc binding.|||Decreased rate of activity.|||Disordered|||In isoform Short.|||Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734.|||Loss of polyubiquitin binding and hydrolysis.|||Loss of polyubiquitin binding and subsequent activation.|||Loss of polyubiquitin binding.|||Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335.|||Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666.|||Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734.|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed|||UBA|||UBA 1|||UBA 2|||UBP-type|||UBP-type; degenerate|||USP|||Ubiquitin carboxyl-terminal hydrolase 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080623|||http://purl.uniprot.org/annotation/VSP_005259
http://togogenome.org/gene/9606:ATF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18846                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic motif|||Breakpoint for translocation to form chimeric EWSR1/ATF1 protein|||Breakpoint for translocation to form chimeric FUS/ATF1 protein|||Cyclic AMP-dependent transcription factor ATF-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired CDK3-mediated phosphorylation and altered transactivation and transcriptional activities.|||In isoform 2.|||KID|||Leucine-zipper|||Phosphoserine; by CaMK1, CDK3, RPS6KA4 and RPS6KA5|||Phosphoserine; by HIPK2|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076575|||http://purl.uniprot.org/annotation/VAR_024382|||http://purl.uniprot.org/annotation/VSP_055559
http://togogenome.org/gene/9606:SLC8A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU59|||http://purl.uniprot.org/uniprot/P57103                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Calx-beta 1|||Calx-beta 2|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 3|||Sodium/calcium exchanger membrane region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019384|||http://purl.uniprot.org/annotation/VAR_036463|||http://purl.uniprot.org/annotation/VSP_008116|||http://purl.uniprot.org/annotation/VSP_008117|||http://purl.uniprot.org/annotation/VSP_008118|||http://purl.uniprot.org/annotation/VSP_043125|||http://purl.uniprot.org/annotation/VSP_043126|||http://purl.uniprot.org/annotation/VSP_043850|||http://purl.uniprot.org/annotation/VSP_044502
http://togogenome.org/gene/9606:EFNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52797                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ephrin RBD|||Ephrin-A3|||GPI-anchor amidated glycine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008369|||http://purl.uniprot.org/annotation/PRO_0000008370|||http://purl.uniprot.org/annotation/VAR_048937|||http://purl.uniprot.org/annotation/VSP_055483
http://togogenome.org/gene/9606:C1QTNF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXI9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 6|||Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003538|||http://purl.uniprot.org/annotation/VAR_046624|||http://purl.uniprot.org/annotation/VAR_046625|||http://purl.uniprot.org/annotation/VAR_046626|||http://purl.uniprot.org/annotation/VAR_046627|||http://purl.uniprot.org/annotation/VAR_046628|||http://purl.uniprot.org/annotation/VSP_059765|||http://purl.uniprot.org/annotation/VSP_059766
http://togogenome.org/gene/9606:SGF29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ES7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes H3K4me3 binding.|||Almost abolished H3K4me3 binding.|||Does not affect binding to H3K4me3.|||Does not strongly affect binding to H3K4me.|||Histone H3K4me3 N-terminus binding|||Histone H3K4me3 binding|||N6-acetyllysine|||Reduced H3K4me3 binding.|||SAGA-associated factor 29|||SGF29 C-terminal|||Slightly reduced H3K4me3 binding.|||Slightly reduced binding to H3K4me3.|||Strongly reduced H3K4me3 binding.|||Strongly reduced binding to H3K4me3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274268
http://togogenome.org/gene/9606:STAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V395|||http://purl.uniprot.org/uniprot/P40763                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Allysine; alternate|||Essential for nuclear import|||In ADMIO1.|||In ADMIO1; increases transcriptional activity; increases binding to ISL1 promoter region; decreases glucose stimulated insulin secretion.|||In HIES1.|||In HIES1; loss of function.|||In HIES1; loss of function; reduced DNA-binding ability.|||In HIES1; reduced DNA-binding ability.|||In HIES1; unknown pathological significance; reduced DNA-binding ability.|||In isoform 3.|||In isoform Del-701.|||Inhibits leptin-mediated transactivation of CCND1 promoter. Abolished phosphorylation by isoform M2 of PKM (PKM2).|||Inhibits leptin-mediated transactivation of CCND1 promoter. No effect on interaction with INPP5F.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FER and PTK6|||Removed|||SH2|||Signal transducer and activator of transcription 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182417|||http://purl.uniprot.org/annotation/VAR_018679|||http://purl.uniprot.org/annotation/VAR_018683|||http://purl.uniprot.org/annotation/VAR_037365|||http://purl.uniprot.org/annotation/VAR_037366|||http://purl.uniprot.org/annotation/VAR_037367|||http://purl.uniprot.org/annotation/VAR_037368|||http://purl.uniprot.org/annotation/VAR_037369|||http://purl.uniprot.org/annotation/VAR_037370|||http://purl.uniprot.org/annotation/VAR_037371|||http://purl.uniprot.org/annotation/VAR_037372|||http://purl.uniprot.org/annotation/VAR_037373|||http://purl.uniprot.org/annotation/VAR_037374|||http://purl.uniprot.org/annotation/VAR_037375|||http://purl.uniprot.org/annotation/VAR_037376|||http://purl.uniprot.org/annotation/VAR_037377|||http://purl.uniprot.org/annotation/VAR_037378|||http://purl.uniprot.org/annotation/VAR_037379|||http://purl.uniprot.org/annotation/VAR_037380|||http://purl.uniprot.org/annotation/VAR_037381|||http://purl.uniprot.org/annotation/VAR_071885|||http://purl.uniprot.org/annotation/VAR_071886|||http://purl.uniprot.org/annotation/VAR_071887|||http://purl.uniprot.org/annotation/VAR_071888|||http://purl.uniprot.org/annotation/VAR_075414|||http://purl.uniprot.org/annotation/VAR_075415|||http://purl.uniprot.org/annotation/VAR_078445|||http://purl.uniprot.org/annotation/VSP_010474|||http://purl.uniprot.org/annotation/VSP_055918|||http://purl.uniprot.org/annotation/VSP_055919
http://togogenome.org/gene/9606:MROH2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0Z6|||http://purl.uniprot.org/uniprot/Q7Z745                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In isoform 2.|||Maestro heat-like repeat-containing protein family member 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332243|||http://purl.uniprot.org/annotation/VAR_042983|||http://purl.uniprot.org/annotation/VAR_042984|||http://purl.uniprot.org/annotation/VAR_042985|||http://purl.uniprot.org/annotation/VAR_042986|||http://purl.uniprot.org/annotation/VAR_042987|||http://purl.uniprot.org/annotation/VAR_042988|||http://purl.uniprot.org/annotation/VAR_042989|||http://purl.uniprot.org/annotation/VAR_042990|||http://purl.uniprot.org/annotation/VAR_042991|||http://purl.uniprot.org/annotation/VAR_042992|||http://purl.uniprot.org/annotation/VAR_042993|||http://purl.uniprot.org/annotation/VSP_033361
http://togogenome.org/gene/9606:C10orf88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8K7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  ATPase PAAT|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260085
http://togogenome.org/gene/9606:CAPN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MX76|||http://purl.uniprot.org/uniprot/B7Z467                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-14|||Domain III|||Domain IV|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform 2.|||Linker                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341373|||http://purl.uniprot.org/annotation/VSP_034268|||http://purl.uniprot.org/annotation/VSP_034269
http://togogenome.org/gene/9606:KAT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXR9|||http://purl.uniprot.org/uniprot/O95251                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished histone acetyltransferase activity.|||Abolishes histone acetyltransferase activity.|||Basic and acidic residues|||C2HC MYST-type|||CCHHC-type|||Decreases ubiquitination.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone acetyltransferase KAT7|||Impaired phosphorylation by ATR, leading to decreased ubiquitination and increased stability in response to DNA damage.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 5.|||Leads to cell cycle arrest in the G1/S phase.|||MYST-type HAT|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||No interaction with MCM2 and ORC1.|||Phosphoserine|||Phosphoserine; by ATR|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Polar residues|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051569|||http://purl.uniprot.org/annotation/VSP_042552|||http://purl.uniprot.org/annotation/VSP_042553|||http://purl.uniprot.org/annotation/VSP_042554
http://togogenome.org/gene/9606:ESYT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSJ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes location at the cell membrane; when associated with A-663 and A-675.|||Abolishes location at the cell membrane; when associated with A-675 and 722-A--A-729.|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||Cytoplasmic|||Disordered|||Extended synaptotagmin-1|||Helical|||In isoform 2.|||Loss of translocation to sites of contact between the endoplasmic reticulum and the cell membrane.|||Lumenal|||N-acetylmethionine|||N6-acetyllysine|||No effect on translocation to sites of contact between the endoplasmic reticulum and the cell membrane.|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane|||SMP-LTD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234344|||http://purl.uniprot.org/annotation/VAR_038190|||http://purl.uniprot.org/annotation/VSP_018277
http://togogenome.org/gene/9606:TOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94900                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||HMG box|||Nuclear localization signal|||Polar residues|||Thymocyte selection-associated high mobility group box protein TOX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244569|||http://purl.uniprot.org/annotation/VAR_064759
http://togogenome.org/gene/9606:PWP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15269                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Periodic tryptophan protein 2 homolog|||Phosphoserine|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 14|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051175|||http://purl.uniprot.org/annotation/VAR_028104|||http://purl.uniprot.org/annotation/VAR_028105|||http://purl.uniprot.org/annotation/VAR_053412
http://togogenome.org/gene/9606:NFKBID                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NI38                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||In isoform 2.|||In isoform 3.|||NF-kappa-B inhibitor delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331114|||http://purl.uniprot.org/annotation/VAR_042737|||http://purl.uniprot.org/annotation/VSP_033143|||http://purl.uniprot.org/annotation/VSP_033144|||http://purl.uniprot.org/annotation/VSP_033145
http://togogenome.org/gene/9606:TRMT112                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI30                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with BUD23, THUMPD2 and THUMPD3. Reduces interaction with TRMT11, N6AMT1, METTL5 and ALKBH8. Reduces expression of exogenous TRMT112.|||Abolishes interaction with METTL5 and THUMPD3. Reduces interaction with ALKBH8 and THUMPD2. No effect on interaction with N6AMT1, BUD23 and TRMT11. Reduces expression of exogenous TRMT112.|||Abolishes interaction with METTL5 and THUMPD3. Reduces interaction with ALKBH8, THUMPD2 and TRMT11. No effect on interaction with N6AMT1 and BUD23. No effect on expression of exogenous TRMT112.|||Abolishes interaction with N6AMT1, METTL5, TRMT11, THUMPD3 and THUMPD2. Reduces interaction with BUD23 and ALKBH8. Reduces expression of exogenous TRMT112.|||Abolishes interaction with THUMPD2 and THUMPD3. Reduces interaction with N6AMT1, BUD23, TRMT11 and ALKBH8. Reduces expression of exogenous TRMT112. Increases interaction with METTL5.|||Abolishes interaction with THUMPD2 and THUMPD3. Reduces interaction with TRMT11, ALKBH8 and N6AMT1. No effect on interaction with BUD23 and METTL5. No effect on expression of exogenous TRMT112.|||Abolishes interaction with THUMPD2. Increases expression of exogenous TRMT112. No effect on interaction with N6AMT1, BUD23, METTL5, TRMT11, ALKBH8 and THUMPD3.|||In isoform 2.|||Increases interaction with METTL5. No effect on interaction with TRMT11, THUMPD2, THUMPD3, N6AMT1, BUD23 and ALKBH8. No effect on expression of exogenous TRMT112.|||Multifunctional methyltransferase subunit TRM112-like protein|||Phosphoserine|||Reduces interaction with THUMPD2, THUMPD3, ALKBH8, TRMT11, N6AMT1 and BUD23. Increases interaction with METTL5. Reduces expression of exogenous TRMT112.|||Strongly reduced ability to promote N5-methylation of ETF1 together with HEMK2/N6AMT1.|||TRM112                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215797|||http://purl.uniprot.org/annotation/VSP_054748
http://togogenome.org/gene/9606:GPR174                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXC1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 174                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069654|||http://purl.uniprot.org/annotation/VAR_049409
http://togogenome.org/gene/9606:FOXD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60548                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein D2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091815|||http://purl.uniprot.org/annotation/VAR_061185
http://togogenome.org/gene/9606:RALGPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JS13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of activity.|||PH|||PXXP|||Polar residues|||Ras-GEF|||Ras-specific guanine nucleotide-releasing factor RalGPS1|||Required for stimulation of nucleotide exchange by RALA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333192|||http://purl.uniprot.org/annotation/VAR_061785|||http://purl.uniprot.org/annotation/VSP_033471|||http://purl.uniprot.org/annotation/VSP_033472|||http://purl.uniprot.org/annotation/VSP_033473|||http://purl.uniprot.org/annotation/VSP_033474|||http://purl.uniprot.org/annotation/VSP_033475|||http://purl.uniprot.org/annotation/VSP_033476|||http://purl.uniprot.org/annotation/VSP_033477|||http://purl.uniprot.org/annotation/VSP_033478|||http://purl.uniprot.org/annotation/VSP_033479|||http://purl.uniprot.org/annotation/VSP_033480|||http://purl.uniprot.org/annotation/VSP_033481
http://togogenome.org/gene/9606:CKS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33552                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Cyclin-dependent kinases regulatory subunit 2|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206237
http://togogenome.org/gene/9606:PHKA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46020                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||In GSD9D.|||In isoform 2.|||In isoform 3.|||Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Polar residues|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057726|||http://purl.uniprot.org/annotation/VAR_020856|||http://purl.uniprot.org/annotation/VSP_004697|||http://purl.uniprot.org/annotation/VSP_042517|||http://purl.uniprot.org/annotation/VSP_042518
http://togogenome.org/gene/9606:RPS6KL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSP6|||http://purl.uniprot.org/uniprot/Q9Y6S9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 4.|||MIT|||Protein kinase|||Proton acceptor|||Ribosomal protein S6 kinase-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232641|||http://purl.uniprot.org/annotation/VAR_041065|||http://purl.uniprot.org/annotation/VAR_041066|||http://purl.uniprot.org/annotation/VAR_041067|||http://purl.uniprot.org/annotation/VSP_017931|||http://purl.uniprot.org/annotation/VSP_017932|||http://purl.uniprot.org/annotation/VSP_036440|||http://purl.uniprot.org/annotation/VSP_036441
http://togogenome.org/gene/9606:ABCG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H172                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-2|||ABC transporter|||ATP-binding cassette sub-family G member 4|||Abrogates ATPase activity. Induces a dominant-negative effect on ABCG1 ATP-activity. Does not affect subcellular localization.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093392|||http://purl.uniprot.org/annotation/VAR_048141|||http://purl.uniprot.org/annotation/VSP_054266|||http://purl.uniprot.org/annotation/VSP_054267|||http://purl.uniprot.org/annotation/VSP_054268
http://togogenome.org/gene/9606:XIAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9R2|||http://purl.uniprot.org/uniprot/P98170                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity and ability to ubiquitinate RIPK2.|||Abolishes dimerization. Interferes with ubiquitination.|||Abolishes inhibition of caspase-3. Reduced interaction with HTRA2; when associated with S-214.|||BIR 1|||BIR 2|||BIR 3|||Decreased interaction with DIABLO/SMAC and with HTRA2. Decreases interaction with HTRA2; when associated with D-259 or A-310. No effect on interaction with SEPTIN4 isoform ARTS.|||E3 ubiquitin-protein ligase XIAP|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In XLP2; unknown pathological significance.|||Inhibits degradation of active caspase-3.|||Interaction with caspase-7|||Loss of E3 ubiquitin-protein ligase activity.|||Loss of dimerization. Reduces activation of NF-kappa-B.|||Loss of interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B.|||Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75.|||No effect on dimerization.|||No effect on interaction with SEPTIN4 isoform ARTS.|||RING-type|||Reduced inhibition of caspase-3.|||Reduced inhibition of caspase-3. May affect protein folding and stability.|||Reduced interaction with HTRA2. Reduced interaction with HTRA2; when associated with A-148.|||Reduced interaction with HTRA2; when associated with S-314.|||Required for interaction with DIABLO|||Required for interaction with SEPTIN4 isoform ARTS|||Required for ubiquitination and subsequent degradation of BCL2 during apoptosis|||S-nitrosocysteine|||Strongly reduced interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122352|||http://purl.uniprot.org/annotation/VAR_022282|||http://purl.uniprot.org/annotation/VAR_022283|||http://purl.uniprot.org/annotation/VAR_022284|||http://purl.uniprot.org/annotation/VAR_022285|||http://purl.uniprot.org/annotation/VAR_088127|||http://purl.uniprot.org/annotation/VAR_088128|||http://purl.uniprot.org/annotation/VAR_088129|||http://purl.uniprot.org/annotation/VAR_088130|||http://purl.uniprot.org/annotation/VAR_088131|||http://purl.uniprot.org/annotation/VAR_088132|||http://purl.uniprot.org/annotation/VAR_088133|||http://purl.uniprot.org/annotation/VAR_088134|||http://purl.uniprot.org/annotation/VAR_088135
http://togogenome.org/gene/9606:MFSD4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSA1|||http://purl.uniprot.org/uniprot/Q5TF39                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Sodium-dependent glucose transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294510|||http://purl.uniprot.org/annotation/VAR_033192
http://togogenome.org/gene/9606:GCDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92947                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Glutaryl-CoA dehydrogenase, mitochondrial|||In GA1.|||In GA1; impaired association of subunits.|||In GA1; impaired protein stability; loss of activity.|||In GA1; loss of enzyme activity.|||In GA1; most common mutation identified; loss of tetramerization; loss enzyme activity.|||In GA1; severe phenotype; residual activity of 30% as measured in patient fibroblasts.|||In isoform Short.|||Mitochondrion|||N6-acetyllysine|||Proton acceptor|||Reduced catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000526|||http://purl.uniprot.org/annotation/VAR_000366|||http://purl.uniprot.org/annotation/VAR_000367|||http://purl.uniprot.org/annotation/VAR_000368|||http://purl.uniprot.org/annotation/VAR_000369|||http://purl.uniprot.org/annotation/VAR_000370|||http://purl.uniprot.org/annotation/VAR_000371|||http://purl.uniprot.org/annotation/VAR_000372|||http://purl.uniprot.org/annotation/VAR_000373|||http://purl.uniprot.org/annotation/VAR_000374|||http://purl.uniprot.org/annotation/VAR_000375|||http://purl.uniprot.org/annotation/VAR_000376|||http://purl.uniprot.org/annotation/VAR_000377|||http://purl.uniprot.org/annotation/VAR_000378|||http://purl.uniprot.org/annotation/VAR_000379|||http://purl.uniprot.org/annotation/VAR_000380|||http://purl.uniprot.org/annotation/VAR_000381|||http://purl.uniprot.org/annotation/VAR_000382|||http://purl.uniprot.org/annotation/VAR_000383|||http://purl.uniprot.org/annotation/VAR_000384|||http://purl.uniprot.org/annotation/VAR_000385|||http://purl.uniprot.org/annotation/VAR_000386|||http://purl.uniprot.org/annotation/VAR_000387|||http://purl.uniprot.org/annotation/VAR_000388|||http://purl.uniprot.org/annotation/VAR_000389|||http://purl.uniprot.org/annotation/VAR_000390|||http://purl.uniprot.org/annotation/VAR_000391|||http://purl.uniprot.org/annotation/VAR_000392|||http://purl.uniprot.org/annotation/VAR_000393|||http://purl.uniprot.org/annotation/VAR_000394|||http://purl.uniprot.org/annotation/VAR_000395|||http://purl.uniprot.org/annotation/VAR_000396|||http://purl.uniprot.org/annotation/VAR_000397|||http://purl.uniprot.org/annotation/VAR_000398|||http://purl.uniprot.org/annotation/VAR_000399|||http://purl.uniprot.org/annotation/VAR_000400|||http://purl.uniprot.org/annotation/VAR_000401|||http://purl.uniprot.org/annotation/VAR_000402|||http://purl.uniprot.org/annotation/VAR_000403|||http://purl.uniprot.org/annotation/VAR_000404|||http://purl.uniprot.org/annotation/VAR_000405|||http://purl.uniprot.org/annotation/VAR_000406|||http://purl.uniprot.org/annotation/VAR_000407|||http://purl.uniprot.org/annotation/VAR_000408|||http://purl.uniprot.org/annotation/VAR_000409|||http://purl.uniprot.org/annotation/VAR_000410|||http://purl.uniprot.org/annotation/VAR_000411|||http://purl.uniprot.org/annotation/VAR_000412|||http://purl.uniprot.org/annotation/VAR_000413|||http://purl.uniprot.org/annotation/VAR_000414|||http://purl.uniprot.org/annotation/VAR_000415|||http://purl.uniprot.org/annotation/VAR_000416|||http://purl.uniprot.org/annotation/VAR_000417|||http://purl.uniprot.org/annotation/VAR_000418|||http://purl.uniprot.org/annotation/VAR_000419|||http://purl.uniprot.org/annotation/VAR_000420|||http://purl.uniprot.org/annotation/VAR_000421|||http://purl.uniprot.org/annotation/VAR_000422|||http://purl.uniprot.org/annotation/VAR_060588|||http://purl.uniprot.org/annotation/VAR_071510|||http://purl.uniprot.org/annotation/VAR_071511|||http://purl.uniprot.org/annotation/VSP_000145
http://togogenome.org/gene/9606:CNR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21554|||http://purl.uniprot.org/uniprot/S5TLS4|||http://purl.uniprot.org/uniprot/V5KA96                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  7-fold lower affinity for a synthetic agonist, CP55940, possibly due the stabilization of an inactive conformation.|||Cannabinoid receptor 1|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||Loss of activity, when assayed for GNAI1 GTPase stimulatory activity.|||Loss of palmitoylation, marked loss of association with lipid rafts on the plasma membrane and loss of activity, when assayed for downstream GTP-binding and reduction in cAMP levels.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Required for mitochondrial localization|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069314|||http://purl.uniprot.org/annotation/VSP_001868|||http://purl.uniprot.org/annotation/VSP_016529
http://togogenome.org/gene/9606:ANKRD36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6QL64                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat domain-containing protein 36A|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334544|||http://purl.uniprot.org/annotation/VSP_039656|||http://purl.uniprot.org/annotation/VSP_039657|||http://purl.uniprot.org/annotation/VSP_039658|||http://purl.uniprot.org/annotation/VSP_039659|||http://purl.uniprot.org/annotation/VSP_039660|||http://purl.uniprot.org/annotation/VSP_039661|||http://purl.uniprot.org/annotation/VSP_039663|||http://purl.uniprot.org/annotation/VSP_039664|||http://purl.uniprot.org/annotation/VSP_039665
http://togogenome.org/gene/9606:DCAF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59GN6|||http://purl.uniprot.org/uniprot/Q8TEB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DDB1- and CUL4-associated factor 11|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051371|||http://purl.uniprot.org/annotation/VAR_020121|||http://purl.uniprot.org/annotation/VSP_008423|||http://purl.uniprot.org/annotation/VSP_008424
http://togogenome.org/gene/9606:OR5M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGP8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150604|||http://purl.uniprot.org/annotation/VAR_060010
http://togogenome.org/gene/9606:LGALS9C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSY2|||http://purl.uniprot.org/uniprot/Q6DKI2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Galectin|||Galectin 1|||Galectin 2|||Galectin-9C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332131|||http://purl.uniprot.org/annotation/VAR_056004
http://togogenome.org/gene/9606:PCDHB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FR6|||http://purl.uniprot.org/uniprot/Q9Y5E4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Protocadherin beta-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003922|||http://purl.uniprot.org/annotation/PRO_5004252733|||http://purl.uniprot.org/annotation/VAR_033704|||http://purl.uniprot.org/annotation/VAR_048552
http://togogenome.org/gene/9606:ATP6V1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21283                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylthreonine|||Removed|||V-type proton ATPase subunit C 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209348
http://togogenome.org/gene/9606:FBRS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTZ7|||http://purl.uniprot.org/uniprot/J3KNZ9|||http://purl.uniprot.org/uniprot/Q9HAH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 1.|||Phosphoserine|||Polar residues|||Pro residues|||Probable fibrosin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087206|||http://purl.uniprot.org/annotation/VSP_010991
http://togogenome.org/gene/9606:ZSCAN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15535                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||SCAN box|||Zinc finger and SCAN domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047446|||http://purl.uniprot.org/annotation/VAR_076868|||http://purl.uniprot.org/annotation/VSP_044798
http://togogenome.org/gene/9606:PLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13393|||http://purl.uniprot.org/uniprot/Q59EA4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Catalytic|||In CVDP1.|||In isoform PLD1B.|||In isoform PLD1C.|||In isoform PLD1D.|||PH|||PLD phosphodiesterase|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2|||PX|||Phospholipase D1|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218802|||http://purl.uniprot.org/annotation/VAR_022056|||http://purl.uniprot.org/annotation/VAR_022057|||http://purl.uniprot.org/annotation/VAR_034387|||http://purl.uniprot.org/annotation/VAR_051703|||http://purl.uniprot.org/annotation/VAR_078985|||http://purl.uniprot.org/annotation/VSP_005018|||http://purl.uniprot.org/annotation/VSP_005019|||http://purl.uniprot.org/annotation/VSP_005020|||http://purl.uniprot.org/annotation/VSP_005021|||http://purl.uniprot.org/annotation/VSP_005022
http://togogenome.org/gene/9606:POP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969H6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Ribonuclease P/MRP protein subunit POP5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239007|||http://purl.uniprot.org/annotation/VSP_042733
http://togogenome.org/gene/9606:STK11IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1F8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Phosphoserine|||Polar residues|||Pro residues|||Serine/threonine-protein kinase 11-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317462|||http://purl.uniprot.org/annotation/VAR_038529|||http://purl.uniprot.org/annotation/VAR_038530|||http://purl.uniprot.org/annotation/VAR_038531|||http://purl.uniprot.org/annotation/VAR_038532|||http://purl.uniprot.org/annotation/VAR_038533
http://togogenome.org/gene/9606:TEAD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99594                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphoserine|||Removed|||TEA|||Transcriptional activation|||Transcriptional enhancer factor TEF-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205934|||http://purl.uniprot.org/annotation/VAR_052278
http://togogenome.org/gene/9606:NDUFA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V438|||http://purl.uniprot.org/uniprot/H7C2X4|||http://purl.uniprot.org/uniprot/O95299                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Deoxynucleoside kinase|||In MC1DN22.|||In MC1DN22; unknown pathological significance.|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial|||Phosphoserine; by PINK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019988|||http://purl.uniprot.org/annotation/PRO_5029848207|||http://purl.uniprot.org/annotation/PRO_5029860560|||http://purl.uniprot.org/annotation/VAR_034149|||http://purl.uniprot.org/annotation/VAR_078937|||http://purl.uniprot.org/annotation/VAR_081458|||http://purl.uniprot.org/annotation/VSP_056417|||http://purl.uniprot.org/annotation/VSP_056418|||http://purl.uniprot.org/annotation/VSP_056419
http://togogenome.org/gene/9606:SYNM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B7B1|||http://purl.uniprot.org/uniprot/O15061                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||In isoform 3.|||Interaction with DMD and UTRN|||Interaction with TLN1 and VCL|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synemin|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063778|||http://purl.uniprot.org/annotation/VAR_012295|||http://purl.uniprot.org/annotation/VAR_012296|||http://purl.uniprot.org/annotation/VAR_012297|||http://purl.uniprot.org/annotation/VAR_012298|||http://purl.uniprot.org/annotation/VAR_012299|||http://purl.uniprot.org/annotation/VAR_012300|||http://purl.uniprot.org/annotation/VAR_012301|||http://purl.uniprot.org/annotation/VAR_012302|||http://purl.uniprot.org/annotation/VAR_012303|||http://purl.uniprot.org/annotation/VAR_012304|||http://purl.uniprot.org/annotation/VAR_012305|||http://purl.uniprot.org/annotation/VAR_012306|||http://purl.uniprot.org/annotation/VAR_012307|||http://purl.uniprot.org/annotation/VAR_059378|||http://purl.uniprot.org/annotation/VAR_059379|||http://purl.uniprot.org/annotation/VAR_059380|||http://purl.uniprot.org/annotation/VAR_059381|||http://purl.uniprot.org/annotation/VSP_002465|||http://purl.uniprot.org/annotation/VSP_036478|||http://purl.uniprot.org/annotation/VSP_036479
http://togogenome.org/gene/9606:CARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7E6|||http://purl.uniprot.org/uniprot/Q9HA77                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||In COXPD27.|||Mitochondrion|||Probable cysteine--tRNA ligase, mitochondrial|||tRNA synthetases class I catalytic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250741|||http://purl.uniprot.org/annotation/VAR_034523|||http://purl.uniprot.org/annotation/VAR_034524|||http://purl.uniprot.org/annotation/VAR_075667|||http://purl.uniprot.org/annotation/VAR_075668|||http://purl.uniprot.org/annotation/VAR_075669
http://togogenome.org/gene/9606:MARCHF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60337                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes auto-ubiquitination. Loss of ubiquitin ligase activity.|||Acidic residues|||Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase MARCHF6|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||RING-CH-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274298|||http://purl.uniprot.org/annotation/VAR_030251|||http://purl.uniprot.org/annotation/VSP_047035|||http://purl.uniprot.org/annotation/VSP_047036
http://togogenome.org/gene/9606:OR2L8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGY9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2L8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150489|||http://purl.uniprot.org/annotation/VAR_053147|||http://purl.uniprot.org/annotation/VAR_059987|||http://purl.uniprot.org/annotation/VAR_059988|||http://purl.uniprot.org/annotation/VAR_059989|||http://purl.uniprot.org/annotation/VAR_062024|||http://purl.uniprot.org/annotation/VAR_080452
http://togogenome.org/gene/9606:SH3RF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08AM8|||http://purl.uniprot.org/uniprot/Q8TEC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase SH3RF2|||In isoform 2.|||In isoform 3.|||Interaction with PAK4|||Interaction with PPP1CA|||Phosphoserine|||Polar residues|||RING-type|||SH3|||SH3 1|||SH3 2|||SH3 3|||Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-643.|||Significant loss of interaction with PPP1CA. Significant loss of interaction with PPP1CA; when associated with G-645.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269512|||http://purl.uniprot.org/annotation/VAR_029788|||http://purl.uniprot.org/annotation/VAR_029789|||http://purl.uniprot.org/annotation/VAR_029790|||http://purl.uniprot.org/annotation/VAR_029791|||http://purl.uniprot.org/annotation/VAR_052118|||http://purl.uniprot.org/annotation/VAR_052119|||http://purl.uniprot.org/annotation/VAR_052120|||http://purl.uniprot.org/annotation/VSP_022058|||http://purl.uniprot.org/annotation/VSP_022059|||http://purl.uniprot.org/annotation/VSP_040662
http://togogenome.org/gene/9606:GOLGA8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MQT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Golgi-targeting domain|||Golgin subfamily A member 8B|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316091|||http://purl.uniprot.org/annotation/VSP_030496
http://togogenome.org/gene/9606:COQ5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYK3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228628|||http://purl.uniprot.org/annotation/VAR_025702
http://togogenome.org/gene/9606:SCN3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A590UJH3|||http://purl.uniprot.org/uniprot/Q9C007|||http://purl.uniprot.org/uniprot/Q9NY46                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with NEDD4L.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IQ|||IV|||In DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component and a leftward shift in the voltage dependence of activation to more hyperpolarized potentials.|||In DEE62; prominent gain of channel function, with markedly increased amplitude of the slowly inactivating current component.|||In DEE62; unknown pathological significance; no gain of function in channel activity.|||In DEE62; unknown pathological significance; no gain of function in channel activity; channel recovery from inactivation is more rapid than that of wild-type channel.|||In FFEVF4; affects voltage-dependent sodium channel activity; increased level of persistent sodium current compared to wild-type channels and increased current activation in response to depolarizing voltage ramps.|||In FFEVF4; affects voltage-dependent sodium channel activity; smaller current density and slower activation compared to wild-type channels and increased current activation in response to depolarizing voltage ramps.|||In FFEVF4; loss of localization at the cell surface.|||In FFEVF4; unknown pathological significance; increased current activation in response to depolarizing voltage ramps.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||Ion transport|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Pore-forming|||Sodium channel protein type 3 subunit alpha|||Sodium ion transport-associated|||Voltage-gated Na+ ion channel cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048493|||http://purl.uniprot.org/annotation/VAR_014275|||http://purl.uniprot.org/annotation/VAR_029743|||http://purl.uniprot.org/annotation/VAR_029744|||http://purl.uniprot.org/annotation/VAR_029745|||http://purl.uniprot.org/annotation/VAR_055640|||http://purl.uniprot.org/annotation/VAR_076435|||http://purl.uniprot.org/annotation/VAR_080503|||http://purl.uniprot.org/annotation/VAR_080504|||http://purl.uniprot.org/annotation/VAR_080505|||http://purl.uniprot.org/annotation/VAR_080506|||http://purl.uniprot.org/annotation/VAR_080507|||http://purl.uniprot.org/annotation/VAR_080508|||http://purl.uniprot.org/annotation/VAR_080509|||http://purl.uniprot.org/annotation/VAR_080510|||http://purl.uniprot.org/annotation/VAR_080511|||http://purl.uniprot.org/annotation/VAR_080512|||http://purl.uniprot.org/annotation/VSP_001033|||http://purl.uniprot.org/annotation/VSP_001034
http://togogenome.org/gene/9606:SRRD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 7 AA tandem repeats of R-E-A-A-P-R-G|||Basic and acidic residues|||Disordered|||SRR1-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186123|||http://purl.uniprot.org/annotation/VAR_031211|||http://purl.uniprot.org/annotation/VAR_052064
http://togogenome.org/gene/9606:PSMG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT73                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand                                                                                  ^@                                                                                  N-acetylmethionine|||Proteasome assembly chaperone 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271358
http://togogenome.org/gene/9606:SFXN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9B4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylserine|||Removed|||Sideroflexin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000177032|||http://purl.uniprot.org/annotation/VAR_051966|||http://purl.uniprot.org/annotation/VAR_051967
http://togogenome.org/gene/9606:ISCA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUE6                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In MMDS5; unknown pathological significance.|||In isoform 2.|||Iron-sulfur cluster assembly 1 homolog, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042734|||http://purl.uniprot.org/annotation/VAR_079296|||http://purl.uniprot.org/annotation/VSP_057035
http://togogenome.org/gene/9606:ACOT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYK0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acetyl-coenzyme A thioesterase|||Found in a clear cell renal carcinoma case; somatic mutation.|||HotDog ACOT-type 1|||HotDog ACOT-type 2|||In isoform 2.|||N6-succinyllysine|||START                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053809|||http://purl.uniprot.org/annotation/VAR_048192|||http://purl.uniprot.org/annotation/VAR_048193|||http://purl.uniprot.org/annotation/VAR_064691|||http://purl.uniprot.org/annotation/VSP_055785|||http://purl.uniprot.org/annotation/VSP_055786
http://togogenome.org/gene/9606:FNBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQ35|||http://purl.uniprot.org/uniprot/A0A994J3V8|||http://purl.uniprot.org/uniprot/B7ZL13|||http://purl.uniprot.org/uniprot/H0Y7W6|||http://purl.uniprot.org/uniprot/Q96RU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes membrane invagination.|||Abrogates interaction with DNM1, DNM2 and DNM3.|||Abrogates interaction with TNKS.|||Disordered|||Disrupts helix kink and moderately increases diameter of the induced tubular membrane.|||F-BAR|||Formin-binding protein 1|||Impairs interaction with TNKS.|||Impairs interaction with TNKS; when associated with A-515.|||Impairs lipid-binding and induction of membrane tubulation.|||Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33.|||Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35.|||Impairs membrane tubulation but does not affect lipid-binding.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2|||Interaction with DNM1 and DNM3|||Interaction with DNM2 and WASL|||Interaction with FASLG|||Interaction with PDE6G|||Interaction with RND2|||Interaction with microtubules|||Mediates end-to-end attachment of dimers|||N6-acetyllysine|||No significant effect.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||REM-1|||Required for interaction with TNKS|||Required for self-association and induction of membrane tubulation|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261430|||http://purl.uniprot.org/annotation/VAR_029388|||http://purl.uniprot.org/annotation/VSP_021693|||http://purl.uniprot.org/annotation/VSP_021694|||http://purl.uniprot.org/annotation/VSP_021695|||http://purl.uniprot.org/annotation/VSP_021696
http://togogenome.org/gene/9606:CIMAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCV2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule-associated protein 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297585|||http://purl.uniprot.org/annotation/VAR_034645|||http://purl.uniprot.org/annotation/VAR_054410|||http://purl.uniprot.org/annotation/VSP_027294
http://togogenome.org/gene/9606:HVCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D96                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes channel activity.|||Alters channel selectivity. Converts the proton channel to an anion channel.|||Cytoplasmic|||Disordered|||Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-140.|||Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-193.|||Extracellular|||Faster channel activation and deactivation kinetics.|||Faster channel deactivation kinetics.|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of a phosphorylation site. Reduces phosphorylation.|||Loss of a phosphorylation site. Strongly reduces phosphorylation.|||No effect on channel activity and proton selectivity.|||Phosphoserine|||Phosphothreonine|||Voltage-gated hydrogen channel 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342187|||http://purl.uniprot.org/annotation/VSP_034395|||http://purl.uniprot.org/annotation/VSP_034396|||http://purl.uniprot.org/annotation/VSP_045052
http://togogenome.org/gene/9606:ADPRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E341|||http://purl.uniprot.org/uniprot/P54922                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylhydrolase ARH1|||Complete loss of activity.|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157283
http://togogenome.org/gene/9606:DSCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60469                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule DSCAM|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 10|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||Ig-like C2-type 9|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for netrin-mediated axon repulsion of neuronal growth cones                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014747|||http://purl.uniprot.org/annotation/VAR_020080|||http://purl.uniprot.org/annotation/VSP_002502|||http://purl.uniprot.org/annotation/VSP_002503
http://togogenome.org/gene/9606:GBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32456|||http://purl.uniprot.org/uniprot/Q8TCE5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||GB1/RHD3-type G|||GTPase domain (Globular)|||Guanylate-binding protein 2|||Loss of isoprenylation and of localization at the Golgi apparatus.|||No effect on subcellular location by confocal microscopy, but loss of membrane-association by subcellular fractionation.|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190964|||http://purl.uniprot.org/annotation/PRO_0000370782|||http://purl.uniprot.org/annotation/VAR_054815|||http://purl.uniprot.org/annotation/VAR_054816|||http://purl.uniprot.org/annotation/VAR_054817
http://togogenome.org/gene/9606:RPL18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02543                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein eL20|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213925
http://togogenome.org/gene/9606:OR4K15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH41                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4K15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150558|||http://purl.uniprot.org/annotation/VAR_055060|||http://purl.uniprot.org/annotation/VAR_055061|||http://purl.uniprot.org/annotation/VAR_055062|||http://purl.uniprot.org/annotation/VAR_055063|||http://purl.uniprot.org/annotation/VAR_055064|||http://purl.uniprot.org/annotation/VAR_055065
http://togogenome.org/gene/9606:WDR25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPW5|||http://purl.uniprot.org/uniprot/Q64LD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256227|||http://purl.uniprot.org/annotation/VAR_028888|||http://purl.uniprot.org/annotation/VAR_028889|||http://purl.uniprot.org/annotation/VAR_060042|||http://purl.uniprot.org/annotation/VAR_060043|||http://purl.uniprot.org/annotation/VSP_021331|||http://purl.uniprot.org/annotation/VSP_021332
http://togogenome.org/gene/9606:C1orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0U7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||Uncharacterized protein C1orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284489|||http://purl.uniprot.org/annotation/VAR_031745|||http://purl.uniprot.org/annotation/VAR_031746|||http://purl.uniprot.org/annotation/VAR_031747|||http://purl.uniprot.org/annotation/VAR_031748|||http://purl.uniprot.org/annotation/VAR_035493|||http://purl.uniprot.org/annotation/VSP_024540|||http://purl.uniprot.org/annotation/VSP_024541|||http://purl.uniprot.org/annotation/VSP_024542
http://togogenome.org/gene/9606:ZBED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTP6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  BED-type|||Basic and acidic residues|||Disordered|||Zinc finger BED domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066561|||http://purl.uniprot.org/annotation/VAR_083712
http://togogenome.org/gene/9606:CYP2A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16696                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2A13|||Decreases phenacetin O-deethylation activity 10 fold.|||Decreases phenacetin O-deethylation activity 2 fold.|||Decreases phenacetin O-deethylation activity 20 fold.|||Decreases phenacetin O-deethylation activity 3 fold.|||Decreases phenacetin O-deethylation activity 40 fold.|||Decreases phenacetin O-deethylation activity 7 fold.|||Decreases phenacetin O-deethylation activity 8 fold.|||Decreases phenacetin O-deethylation activity 9 fold.|||In allele CYP2A13*2.|||In allele CYP2A13*3 and allele CYP2A13*8.|||In allele CYP2A13*3.|||In allele CYP2A13*4.|||In allele CYP2A13*5.|||In allele CYP2A13*6.|||In allele CYP2A13*9.|||Increases phenacetin O-deethylation activity 3 fold.|||Increases phenacetin O-deethylation activity 5 fold.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051676|||http://purl.uniprot.org/annotation/VAR_013835|||http://purl.uniprot.org/annotation/VAR_018334|||http://purl.uniprot.org/annotation/VAR_018335|||http://purl.uniprot.org/annotation/VAR_018336|||http://purl.uniprot.org/annotation/VAR_018337|||http://purl.uniprot.org/annotation/VAR_018338|||http://purl.uniprot.org/annotation/VAR_018339|||http://purl.uniprot.org/annotation/VAR_018356
http://togogenome.org/gene/9606:ASCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9N2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Activating signal cointegrator 1 complex subunit 1|||Found in patients with Barrett esophagus.|||In isoform 2.|||KH|||Required for interaction with ASCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050100|||http://purl.uniprot.org/annotation/VAR_061278|||http://purl.uniprot.org/annotation/VAR_066588|||http://purl.uniprot.org/annotation/VSP_011007|||http://purl.uniprot.org/annotation/VSP_011008
http://togogenome.org/gene/9606:KIF3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15066                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Does not affect protein stability nor cilia length.|||Globular|||In RP89; increase in primary cilia length; does not affect protein stability; significant increase of rhodopsin in the rod inner segment when expressed in zebrafish; coinjection with wild-type rescued the rhodopsin mislocalization defects.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF3B|||Kinesin-like protein KIF3B, N-terminally processed|||N-acetylmethionine|||N-acetylserine; in Kinesin-like protein KIF3B, N-terminally processed|||Polar residues|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125395|||http://purl.uniprot.org/annotation/PRO_0000424495|||http://purl.uniprot.org/annotation/VAR_084674|||http://purl.uniprot.org/annotation/VAR_084675|||http://purl.uniprot.org/annotation/VSP_056489|||http://purl.uniprot.org/annotation/VSP_056490
http://togogenome.org/gene/9606:ZNF737                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75373                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 737                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340686|||http://purl.uniprot.org/annotation/VAR_067460|||http://purl.uniprot.org/annotation/VAR_067461|||http://purl.uniprot.org/annotation/VAR_067462|||http://purl.uniprot.org/annotation/VAR_067463
http://togogenome.org/gene/9606:CDS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95674                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphatidate cytidylyltransferase 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090716|||http://purl.uniprot.org/annotation/VSP_015477|||http://purl.uniprot.org/annotation/VSP_015480|||http://purl.uniprot.org/annotation/VSP_015482
http://togogenome.org/gene/9606:MACROD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1Z1Q3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribose glycohydrolase MACROD2|||Abolished hydrolase activity and ability to bind ADP-D-ribose.|||Abolishes interaction with ADP-ribosylated proteins. Strongly reduced ADP-ribosyl hydrolase activity.|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 1 and isoform 4.|||In isoform 4 and isoform 5.|||In isoform 6.|||Macro|||Polar residues|||Reduced ADP-ribosyl hydrolase activity. Reduced ADP-ribosyl hydrolase activity; when associated with A-92.|||Reduced ADP-ribosyl hydrolase activity; when associated with A-102.|||Reduced hydrolase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300461|||http://purl.uniprot.org/annotation/VAR_056935|||http://purl.uniprot.org/annotation/VAR_061681|||http://purl.uniprot.org/annotation/VSP_059641|||http://purl.uniprot.org/annotation/VSP_059642|||http://purl.uniprot.org/annotation/VSP_059643|||http://purl.uniprot.org/annotation/VSP_059644
http://togogenome.org/gene/9606:TBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDS4|||http://purl.uniprot.org/uniprot/Q9Y4P3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphothreonine; by ATM or ATR|||Transducin beta-like protein 2|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051270|||http://purl.uniprot.org/annotation/PRO_5036334047|||http://purl.uniprot.org/annotation/VAR_053420
http://togogenome.org/gene/9606:SOX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35713                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Basic residues|||Disordered|||Greatly reduced transactivating activity.|||HMG box|||Important for transcriptional activation|||In HLTS.|||Interaction with DNA|||Phosphoserine|||Pro residues|||Sox C-terminal|||Transcription factor SOX-18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048767|||http://purl.uniprot.org/annotation/VAR_016210|||http://purl.uniprot.org/annotation/VAR_016211
http://togogenome.org/gene/9606:SRGAP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A286YEY3                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:TMX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Di-lysine motif|||Disordered|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Protein disulfide-isomerase TMX3|||Redox-active|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034185|||http://purl.uniprot.org/annotation/VAR_022451|||http://purl.uniprot.org/annotation/VSP_013748|||http://purl.uniprot.org/annotation/VSP_013749
http://togogenome.org/gene/9606:CDC42EP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R6D8|||http://purl.uniprot.org/uniprot/Q9H3Q1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CRIB|||Cdc42 effector protein 4|||Disordered|||In isoform 2.|||N6-methyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212655|||http://purl.uniprot.org/annotation/VSP_055544
http://togogenome.org/gene/9606:SBK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52WX2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In an ovarian mucinous carcinoma sample; somatic mutation.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase SBK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238451|||http://purl.uniprot.org/annotation/VAR_041068|||http://purl.uniprot.org/annotation/VAR_041069|||http://purl.uniprot.org/annotation/VAR_041070|||http://purl.uniprot.org/annotation/VAR_051665
http://togogenome.org/gene/9606:CACNG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60359                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Voltage-dependent calcium channel gamma-3 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164675
http://togogenome.org/gene/9606:GLYATL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KVG3|||http://purl.uniprot.org/uniprot/A9ZM15|||http://purl.uniprot.org/uniprot/Q969I3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  Glycine N-acyltransferase C-terminal|||Glycine N-acyltransferase N-terminal|||Glycine N-acyltransferase-like protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281874|||http://purl.uniprot.org/annotation/VSP_024076
http://togogenome.org/gene/9606:RNF144A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50876                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Region|||Sequence Variant|||Strand|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  E3 ubiquitin-protein ligase RNF144A|||Helical|||IBR-type|||RING-type 1|||RING-type 2; atypical|||TRIAD supradomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056298|||http://purl.uniprot.org/annotation/VAR_035375
http://togogenome.org/gene/9606:TRABD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KPT4|||http://purl.uniprot.org/uniprot/Q9H4I3                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||Phosphothreonine|||TraB domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050825|||http://purl.uniprot.org/annotation/VSP_002441
http://togogenome.org/gene/9606:BTF3L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K17                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N6-methyllysine|||NAC-A/B|||Phosphothreonine|||Transcription factor BTF3 homolog 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213557|||http://purl.uniprot.org/annotation/VSP_044248|||http://purl.uniprot.org/annotation/VSP_045972|||http://purl.uniprot.org/annotation/VSP_045973
http://togogenome.org/gene/9606:CHCHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1N4|||http://purl.uniprot.org/uniprot/B7Z1X9|||http://purl.uniprot.org/uniprot/C9JRZ6|||http://purl.uniprot.org/uniprot/Q9NX63                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||MICOS complex subunit MIC19|||N-myristoyl glycine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129163
http://togogenome.org/gene/9606:MYC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01106                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Abolished ubiquitination and degradation by the DCX(TRPC4AP) complex.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Impaired inhibition of Ras-induced senescence. Abolishes phosphorylation by DYRK2, and subsequent phosphorylation by GSK3B at Thr-73.|||Impairs interaction with FBXW7 and subsequent degradation by the proteasome. Normal inhibition of Ras-induced senescence.|||In a Burkitt lymphoma sample.|||In isoform 1.|||In isoform 3.|||Leucine-zipper|||Myc proto-oncogene protein|||N6-acetyllysine; alternate|||N6-acetyllysine; by PCAF|||N6-acetyllysine; by PCAF; alternate|||O-linked (GlcNAc) threonine; alternate|||Phospho-mimetic mutant; abolished regulation by AMBRA1.|||Phosphoserine|||Phosphoserine; by DYRK2, GSK3 and CDK2|||Phosphoserine; by PIM2; in vitro|||Phosphothreonine; by GSK3; alternate|||Phosphothreonine; by RAF; in vitro|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000033|||http://purl.uniprot.org/annotation/PRO_0000127293|||http://purl.uniprot.org/annotation/VAR_016327|||http://purl.uniprot.org/annotation/VAR_016328|||http://purl.uniprot.org/annotation/VAR_016329|||http://purl.uniprot.org/annotation/VAR_016330|||http://purl.uniprot.org/annotation/VAR_063384|||http://purl.uniprot.org/annotation/VAR_063385|||http://purl.uniprot.org/annotation/VAR_063386|||http://purl.uniprot.org/annotation/VAR_063387|||http://purl.uniprot.org/annotation/VSP_061778|||http://purl.uniprot.org/annotation/VSP_061779
http://togogenome.org/gene/9606:HOXA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31268                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200071|||http://purl.uniprot.org/annotation/VAR_028001
http://togogenome.org/gene/9606:IKZF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 4 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein Helios                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047092|||http://purl.uniprot.org/annotation/VAR_028227|||http://purl.uniprot.org/annotation/VSP_006845|||http://purl.uniprot.org/annotation/VSP_055344|||http://purl.uniprot.org/annotation/VSP_055345|||http://purl.uniprot.org/annotation/VSP_055346|||http://purl.uniprot.org/annotation/VSP_055347|||http://purl.uniprot.org/annotation/VSP_055348|||http://purl.uniprot.org/annotation/VSP_055349|||http://purl.uniprot.org/annotation/VSP_055350|||http://purl.uniprot.org/annotation/VSP_055351|||http://purl.uniprot.org/annotation/VSP_055352
http://togogenome.org/gene/9606:SLCO1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05CV5|||http://purl.uniprot.org/uniprot/Q9Y6L6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased estradiol-17beta-d-glucuronide uptake.|||Decreased transport activity.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Kazal-like|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier organic anion transporter family member 1B1|||Strongly decreases expression at the plasma membrane; abolishes transport activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191050|||http://purl.uniprot.org/annotation/VAR_015070|||http://purl.uniprot.org/annotation/VAR_015071|||http://purl.uniprot.org/annotation/VAR_015072|||http://purl.uniprot.org/annotation/VAR_015073|||http://purl.uniprot.org/annotation/VAR_015074|||http://purl.uniprot.org/annotation/VAR_015075|||http://purl.uniprot.org/annotation/VAR_015076|||http://purl.uniprot.org/annotation/VAR_015077|||http://purl.uniprot.org/annotation/VAR_015078|||http://purl.uniprot.org/annotation/VAR_015079|||http://purl.uniprot.org/annotation/VAR_015080|||http://purl.uniprot.org/annotation/VAR_015081|||http://purl.uniprot.org/annotation/VAR_015082|||http://purl.uniprot.org/annotation/VAR_015083|||http://purl.uniprot.org/annotation/VAR_015084|||http://purl.uniprot.org/annotation/VAR_057724|||http://purl.uniprot.org/annotation/VAR_057725|||http://purl.uniprot.org/annotation/VAR_060108
http://togogenome.org/gene/9606:POLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K860|||http://purl.uniprot.org/uniprot/Q9UGP5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT|||Changed DNA polymerase activity characterized by decreased fidelity and unchanged polymerization capacity; changed function in DNA double-strand break repair by non-homologous end joining and homologous recombination; no effect on 5'-deoxyribose-5-phosphate lyase activity.|||DNA polymerase lambda|||DNA-binding|||Disordered|||In isoform 2.|||Involved in primer binding|||Loss of polymerase activity; when associated with A-427.|||Loss of polymerase activity; when associated with A-429.|||No effect on polymerase activity. Reduces terminal transferase activities.|||Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity|||Pro residues|||Reduces dRP lyase activity by over 90%.|||Schiff-base intermediate with DNA|||Strongly reduces polymerase and terminal transferase activities.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218783|||http://purl.uniprot.org/annotation/VAR_020268|||http://purl.uniprot.org/annotation/VAR_020269|||http://purl.uniprot.org/annotation/VSP_056540|||http://purl.uniprot.org/annotation/VSP_056541
http://togogenome.org/gene/9606:DNM1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYR6|||http://purl.uniprot.org/uniprot/O00429                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes GTP hydrolysis.|||Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance.|||Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity.|||Abolishes homodimerization and formation of higher order oligomers.|||Abolishes phosphorylation. Reduces interaction with MIEF1 and MIEF2. Promotes mitochondrial fission and cell vulnerability to apoptotic insults. Mostly mitochondrial. Disrupts, in vitro, binding to FIS1.|||B domain|||Basic residues|||Decreased localization to the perinuclear region.|||Diminishes intramolecular interaction between GTP-middle domain and GED domain but no effect on homooligomerization. Marked reduction in GTPase activity, in vitro. Decreased mitochondrial division.|||Disordered|||Does not impair homodimerization and formation of higher order oligomers.|||Dynamin-1-like protein|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||GED|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Impairs formation of higher order oligomers, but not homodimerization.|||Impairs homodimerization and formation of higher order oligomers.|||Impairs intramolecular interactions but not homooligomerization. Does not reduce interaction with MIEF1 and MIEF2. Impairs formation of higher order oligomers but not homodimerization. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. Slight reduction in GTPase activity. Inhibits mitochondrial fission. Retained in the cytoplasm.|||Important for homodimerization|||In EMPF1; autosomal recessive; impaired mitochondrial membrane fission; hypomorphic mutation retaining partial activity in mitochondrial membrane fission.|||In EMPF1; impaired mitochondrial and peroxisomal membrane fission.|||In EMPF1; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission; reduced oligomerization, decreased mitochondrial recruitment.|||In EMPF1; the mutation acts in a dominant-negative manner; defects observed in mitochondrial fission; significant decrease in mitochondrial respiratory chain complex IV activity.|||In EMPF1; the mutation acts in a dominant-negative manner; reduced oligomerization; decreased mitochondrial recruitment; defects observed in mitochondrial fission.|||In EMPF1; unknown pathological significance; unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site; presence of concentric cristae and/or increased dense granules in some mitochondria.|||In OPA5; changed localization to mitochondrion; impaired mitochondrial membrane fission.|||In isoform 2.|||In isoform 3 and isoform 9.|||In isoform 4 and isoform 8.|||In isoform 5.|||In isoform 6, isoform 8 and isoform 9.|||In isoform 7.|||Interaction with GSK3B|||Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3.|||Loss of activity. Little effect on mitochondrial morphology. Translocated to mitochondria.|||Middle domain|||N-acetylmethionine|||N6-acetyllysine; alternate|||No effect on S-nitrosylation.|||O-linked (GlcNAc) threonine|||Overexpression delays protein secretion. Rescues fragmented or truncated mitochondria in PRKN- or PINK1-depleted cells.|||Phosphoserine|||Phosphoserine; by CAMK1 and PKA|||Phosphoserine; by CDK1 and PINK1|||Reduces peroxisomal abundance.|||S-nitrosocysteine|||Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-558.|||Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-568.|||Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-558 and R-568.|||Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-535; R-558 and R-568.|||Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-606.|||Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-608.|||Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-606 and R-608.|||Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-597; R-606 and R-608.|||Temperature-sensitive. Impairs mitochondrial division.|||Unable to homooligomerize. Unable to associate with MIEF2 into filaments forming the tubular structures that wrap around the scission site. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206566|||http://purl.uniprot.org/annotation/VAR_022446|||http://purl.uniprot.org/annotation/VAR_030489|||http://purl.uniprot.org/annotation/VAR_063704|||http://purl.uniprot.org/annotation/VAR_076316|||http://purl.uniprot.org/annotation/VAR_076317|||http://purl.uniprot.org/annotation/VAR_076318|||http://purl.uniprot.org/annotation/VAR_080869|||http://purl.uniprot.org/annotation/VAR_080870|||http://purl.uniprot.org/annotation/VAR_080871|||http://purl.uniprot.org/annotation/VAR_080872|||http://purl.uniprot.org/annotation/VSP_013685|||http://purl.uniprot.org/annotation/VSP_013686|||http://purl.uniprot.org/annotation/VSP_013687|||http://purl.uniprot.org/annotation/VSP_013688|||http://purl.uniprot.org/annotation/VSP_039097|||http://purl.uniprot.org/annotation/VSP_054544|||http://purl.uniprot.org/annotation/VSP_054545
http://togogenome.org/gene/9606:ZDHHC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPG8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Di-lysine motif|||Does not affect localization to the endoplasmic reticulum.|||Helical|||Impaired localization to the endoplasmic reticulum.|||In a breast cancer sample; somatic mutation.|||Lumenal|||Palmitoyltransferase ZDHHC4|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212865|||http://purl.uniprot.org/annotation/VAR_023832|||http://purl.uniprot.org/annotation/VAR_036260
http://togogenome.org/gene/9606:FCMR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60667                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fas apoptotic inhibitory molecule 3|||Helical|||Ig-like|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284421|||http://purl.uniprot.org/annotation/VSP_042947|||http://purl.uniprot.org/annotation/VSP_045188|||http://purl.uniprot.org/annotation/VSP_045189
http://togogenome.org/gene/9606:ETHE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z580|||http://purl.uniprot.org/uniprot/A0A0S2Z5B3|||http://purl.uniprot.org/uniprot/A0A0S2Z5N8|||http://purl.uniprot.org/uniprot/B2RCZ7|||http://purl.uniprot.org/uniprot/O95571                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In EE.|||In EE; reduces protein stability and affinity for substrate.|||In EE; reduces protein stability, iron content and enzyme activity.|||In EE; reduces protein stability.|||Metallo-beta-lactamase|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Persulfide dioxygenase ETHE1, mitochondrial|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012289|||http://purl.uniprot.org/annotation/VAR_023395|||http://purl.uniprot.org/annotation/VAR_023396|||http://purl.uniprot.org/annotation/VAR_023397|||http://purl.uniprot.org/annotation/VAR_023398|||http://purl.uniprot.org/annotation/VAR_069507|||http://purl.uniprot.org/annotation/VAR_069508|||http://purl.uniprot.org/annotation/VAR_069509|||http://purl.uniprot.org/annotation/VAR_069510|||http://purl.uniprot.org/annotation/VAR_069511
http://togogenome.org/gene/9606:ZNG1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYH9|||http://purl.uniprot.org/uniprot/Q5JTY5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  CXCC motif|||CobW C-terminal|||Disordered|||In isoform 2.|||Zinc-regulated GTPase metalloprotein activator 1C|||psi-PxLVp motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317238|||http://purl.uniprot.org/annotation/VSP_055975
http://togogenome.org/gene/9606:OR51L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVJ8|||http://purl.uniprot.org/uniprot/Q8NGJ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150759|||http://purl.uniprot.org/annotation/VAR_034324|||http://purl.uniprot.org/annotation/VAR_034325
http://togogenome.org/gene/9606:LAMTOR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VGL1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Does not affect Ragulator complex assembly.|||Mimics phosphorylation; inhibiting Ragulator complex assembly.|||N-acetylmethionine|||N-acetylthreonine; in Ragulator complex protein LAMTOR4, N-terminally processed|||Phosphoserine; by PKA|||Ragulator complex protein LAMTOR4|||Ragulator complex protein LAMTOR4, N-terminally processed|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325841|||http://purl.uniprot.org/annotation/PRO_0000424498
http://togogenome.org/gene/9606:ABHD15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXT9                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Disordered|||Phosphoserine|||Protein ABHD15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345395|||http://purl.uniprot.org/annotation/VAR_045821
http://togogenome.org/gene/9606:CCDC80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76M96                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 80|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282418|||http://purl.uniprot.org/annotation/VSP_024135|||http://purl.uniprot.org/annotation/VSP_024136
http://togogenome.org/gene/9606:FAM200C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ13                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein FAM200C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348452|||http://purl.uniprot.org/annotation/VAR_046179
http://togogenome.org/gene/9606:LDLRAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KR97|||http://purl.uniprot.org/uniprot/Q5SW96                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  AP-2 complex binding|||Abolishes AP-2 complex binding.|||Abolishes LDLR cytoplasmic tail binding.|||Abolishes clathrin binding.|||Abolishes interaction with AP2B1.|||Clathrin box|||In FHCL4; Lebanon; requires 2 nucleotide substitutions.|||Low density lipoprotein receptor adapter protein 1|||N-acetylmethionine|||PID|||Phosphoserine|||Probable disease-associated variant found in patients with hypercholesterolemia.|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064675|||http://purl.uniprot.org/annotation/VAR_023320|||http://purl.uniprot.org/annotation/VAR_028403|||http://purl.uniprot.org/annotation/VAR_076925
http://togogenome.org/gene/9606:PIP5K1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60331                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to TLN2. Affects localization to focal adhesions.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Does not affect binding to TLN2 and localization to focal adhesions.|||In LCCS3; loss of activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates interaction with TLN2|||N6-acetyllysine|||Omega-N-methylarginine; alternate|||PIPK|||Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma|||Phosphoserine|||Phosphoserine; by CDK5, MAPK1 and CDK1|||Phosphothreonine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by EGFR|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185462|||http://purl.uniprot.org/annotation/VAR_036996|||http://purl.uniprot.org/annotation/VSP_042078|||http://purl.uniprot.org/annotation/VSP_042079|||http://purl.uniprot.org/annotation/VSP_042080
http://togogenome.org/gene/9606:MECOM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C3SFZ7|||http://purl.uniprot.org/uniprot/C7FEN9|||http://purl.uniprot.org/uniprot/Q03112                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; atypical|||C2H2-type 8|||C2H2-type 9|||CTBP-binding motif 1|||CTBP-binding motif 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase MECOM|||In RUSAT2; alters transcriptional regulation.|||In isoform 1, isoform 4, isoform 8 and isoform 2.|||In isoform 1, isoform 5 and isoform 6.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 8.|||In isoform 9.|||Interaction with MAPK9, SMAD3 and probably SUV39H1|||Nuclear localization signal|||Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 555-A-S-744.|||Partial loss of interaction with CTBP1. Loss of interaction with CTBP1; when associated with 586-A-S-775.|||Phosphoserine|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047273|||http://purl.uniprot.org/annotation/VAR_051183|||http://purl.uniprot.org/annotation/VAR_061928|||http://purl.uniprot.org/annotation/VAR_076308|||http://purl.uniprot.org/annotation/VAR_076309|||http://purl.uniprot.org/annotation/VAR_076310|||http://purl.uniprot.org/annotation/VSP_059479|||http://purl.uniprot.org/annotation/VSP_059480|||http://purl.uniprot.org/annotation/VSP_059481|||http://purl.uniprot.org/annotation/VSP_059482|||http://purl.uniprot.org/annotation/VSP_059483|||http://purl.uniprot.org/annotation/VSP_059484|||http://purl.uniprot.org/annotation/VSP_059485|||http://purl.uniprot.org/annotation/VSP_059486
http://togogenome.org/gene/9606:TIAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0TW27|||http://purl.uniprot.org/uniprot/A0A8V8TN84|||http://purl.uniprot.org/uniprot/Q13009                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DH|||Decreased ubiquitination and increased abundance.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In NEDLDS; unknown pathological significance.|||In a colorectal cancer sample and NEDLDS; somatic mutation; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-myristoyl glycine|||PDZ|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by NTRK2|||Polar residues|||RBD|||Removed|||Rho guanine nucleotide exchange factor TIAM1|||Strongly reduces affinity for SDC1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080976|||http://purl.uniprot.org/annotation/VAR_035977|||http://purl.uniprot.org/annotation/VAR_035978|||http://purl.uniprot.org/annotation/VAR_051991|||http://purl.uniprot.org/annotation/VAR_051992|||http://purl.uniprot.org/annotation/VAR_051993|||http://purl.uniprot.org/annotation/VAR_067424|||http://purl.uniprot.org/annotation/VAR_071102|||http://purl.uniprot.org/annotation/VAR_087427|||http://purl.uniprot.org/annotation/VAR_087428|||http://purl.uniprot.org/annotation/VAR_087429|||http://purl.uniprot.org/annotation/VAR_087430|||http://purl.uniprot.org/annotation/VAR_087431|||http://purl.uniprot.org/annotation/VSP_055865|||http://purl.uniprot.org/annotation/VSP_055866
http://togogenome.org/gene/9606:CNTN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGV0|||http://purl.uniprot.org/uniprot/Q9UQ52                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Contactin-6|||Disordered|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated serine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In a breast cancer sample; somatic mutation.|||In a patient with amyotrophic lateral sclerosis.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014727|||http://purl.uniprot.org/annotation/PRO_0000014728|||http://purl.uniprot.org/annotation/VAR_019913|||http://purl.uniprot.org/annotation/VAR_033611|||http://purl.uniprot.org/annotation/VAR_035509|||http://purl.uniprot.org/annotation/VAR_035510|||http://purl.uniprot.org/annotation/VAR_065744|||http://purl.uniprot.org/annotation/VAR_065745|||http://purl.uniprot.org/annotation/VAR_065746
http://togogenome.org/gene/9606:TRIM6-TRIM34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNG4                                                                                  ^@                                                                                  Coiled-Coil|||Domain Extent|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Domain Extent                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ZIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60481                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C2H2-type 1; atypical|||C2H2-type 2; atypical|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Does not increase its cytoplasmic localization.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CHTD1; Increase in transcriptional activator activity; decrease in nuclear localization.|||In CHTD1; does not affect its transcriptional activator activity; decrease in nuclear localization.|||In HTX1 and CHTD1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3; decrease in nuclear localization.|||In HTX1; decreases protein expression and transcriptional activity and increases its cytoplasmic localization.|||In HTX1; increases strongly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3.|||In HTX1; inreases weakly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3.|||In HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3.|||In VACTERLX.|||In VACTERLX; decrease in transcriptional activator activity; significant decrease in nuclear localization.|||In isoform 2.|||Increases its cytoplasmic localization.|||Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-337; A-341; A-346 and A-349.|||Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-337; A-341; A-349 and A-350.|||Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-337; A-346; A-349 and A-350.|||Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-341; A-346; A-349 and A-350.|||Increases its cytoplasmic localization. Does not interact with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-337; A-341; A-346; A-349 and A-350.|||Increases its cytoplasmic localization. Does not interacts with KPNA1 and KPNA6 and increases strongly its cytoplasmic localization; when associated with A-320; A-337; A-341; A-346 and A-350.|||Increases weakly its cytoplasmic localization.|||Nuclear localization signal|||Polar residues|||Unknown pathological significance; no effect on its transcriptional activator activity or subcellular localization.|||Zinc finger protein ZIC 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047250|||http://purl.uniprot.org/annotation/VAR_007753|||http://purl.uniprot.org/annotation/VAR_025632|||http://purl.uniprot.org/annotation/VAR_025633|||http://purl.uniprot.org/annotation/VAR_025634|||http://purl.uniprot.org/annotation/VAR_025635|||http://purl.uniprot.org/annotation/VAR_042416|||http://purl.uniprot.org/annotation/VAR_066626|||http://purl.uniprot.org/annotation/VAR_071330|||http://purl.uniprot.org/annotation/VAR_071331|||http://purl.uniprot.org/annotation/VAR_071332|||http://purl.uniprot.org/annotation/VAR_071333|||http://purl.uniprot.org/annotation/VAR_071334|||http://purl.uniprot.org/annotation/VSP_044010
http://togogenome.org/gene/9606:ALDOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05062                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Decreases enzymatic activity. Impairs the interaction with G6PD.|||Decreases enzymatic activity. Retains the ability to interact with G6PD.|||Fructose-bisphosphate aldolase B|||In HFI.|||In HFI; 100-fold decrease in catalytic efficiency for substrates F1,6BP and F1P.|||In HFI; America; partial activity.|||In HFI; Italy.|||In HFI; Turkey and South Europe.|||In HFI; Turkey; 4800-fold decrease in catalytic efficiency for F1,6BP and inactive with F1P.|||In HFI; affects proper folding.|||In HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures.|||In HFI; frequent mutation.|||In HFI; reduced enzymatic activity.|||In one subject with fructose intolerance; rare variant; America.|||Loss of enzymatic activity. Impairs the interaction with G6PD.|||Loss of enzymatic activity. Retains the ability to interact with G6PD.|||N-acetylalanine|||N6-succinyllysine|||Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed|||Schiff-base intermediate with dihydroxyacetone-P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216940|||http://purl.uniprot.org/annotation/VAR_000551|||http://purl.uniprot.org/annotation/VAR_000552|||http://purl.uniprot.org/annotation/VAR_000553|||http://purl.uniprot.org/annotation/VAR_000554|||http://purl.uniprot.org/annotation/VAR_000555|||http://purl.uniprot.org/annotation/VAR_000556|||http://purl.uniprot.org/annotation/VAR_000557|||http://purl.uniprot.org/annotation/VAR_000558|||http://purl.uniprot.org/annotation/VAR_020822|||http://purl.uniprot.org/annotation/VAR_020823|||http://purl.uniprot.org/annotation/VAR_020824|||http://purl.uniprot.org/annotation/VAR_020825|||http://purl.uniprot.org/annotation/VAR_020826|||http://purl.uniprot.org/annotation/VAR_020827|||http://purl.uniprot.org/annotation/VAR_020828|||http://purl.uniprot.org/annotation/VAR_038429|||http://purl.uniprot.org/annotation/VAR_038430|||http://purl.uniprot.org/annotation/VAR_058211|||http://purl.uniprot.org/annotation/VAR_058212|||http://purl.uniprot.org/annotation/VAR_075348|||http://purl.uniprot.org/annotation/VAR_075349
http://togogenome.org/gene/9606:ZFAND3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8U3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Region|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A20-type|||AN1-type|||AN1-type zinc finger protein 3|||Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076370
http://togogenome.org/gene/9606:HMGB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW32                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HMG box 1|||HMG box 2|||High mobility group protein B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269180|||http://purl.uniprot.org/annotation/VAR_055951|||http://purl.uniprot.org/annotation/VAR_067467|||http://purl.uniprot.org/annotation/VAR_067468
http://togogenome.org/gene/9606:MEIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSS6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Meiosis expressed gene 1 protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313025|||http://purl.uniprot.org/annotation/VAR_053979
http://togogenome.org/gene/9606:GRIA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42262                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutamate receptor 2|||Helical|||Helical; Name=M4|||Helical; Pore-forming|||In NEDLIB.|||In NEDLIB; homomeric channels show increased ionotropic glutamate receptor activity; decreased localization to cell membrane.|||In NEDLIB; loss of ionotropic glutamate receptor activity; no effect on localization to cell membrane.|||In NEDLIB; reduced ionotropic glutamate receptor activity.|||In NEDLIB; reduced ionotropic glutamate receptor activity; decreased localization to cell membrane.|||In NEDLIB; severe decrease of ionotropic glutamate receptor activity.|||In NEDLIB; unknown pathological significance.|||In NEDLIB; unknown pathological significance; decreased localization to cell membrane.|||In RNA edited version.|||In isoform 3.|||In isoform 4.|||In isoform Flip and isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by PKG|||Phosphotyrosine|||Required for interaction with IQSEC1|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011532|||http://purl.uniprot.org/annotation/VAR_000303|||http://purl.uniprot.org/annotation/VAR_037055|||http://purl.uniprot.org/annotation/VAR_084679|||http://purl.uniprot.org/annotation/VAR_084680|||http://purl.uniprot.org/annotation/VAR_084681|||http://purl.uniprot.org/annotation/VAR_084682|||http://purl.uniprot.org/annotation/VAR_084683|||http://purl.uniprot.org/annotation/VAR_084684|||http://purl.uniprot.org/annotation/VAR_084685|||http://purl.uniprot.org/annotation/VAR_084686|||http://purl.uniprot.org/annotation/VAR_084687|||http://purl.uniprot.org/annotation/VAR_084688|||http://purl.uniprot.org/annotation/VAR_084689|||http://purl.uniprot.org/annotation/VAR_084690|||http://purl.uniprot.org/annotation/VAR_084691|||http://purl.uniprot.org/annotation/VAR_084692|||http://purl.uniprot.org/annotation/VAR_084693|||http://purl.uniprot.org/annotation/VAR_084694|||http://purl.uniprot.org/annotation/VAR_084695|||http://purl.uniprot.org/annotation/VSP_029309|||http://purl.uniprot.org/annotation/VSP_053350|||http://purl.uniprot.org/annotation/VSP_055920
http://togogenome.org/gene/9606:CERS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53HF9|||http://purl.uniprot.org/uniprot/Q9HA82                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Altered specificity toward acyl donor; generates C24 ceramides instead of C18-C22-ceramides.|||Ceramide synthase 4|||Cytoplasmic|||Decreased phosphorylation.|||Disordered|||Helical|||Homeobox|||Homeobox-like|||Last loop motif|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185512|||http://purl.uniprot.org/annotation/VAR_019556|||http://purl.uniprot.org/annotation/VAR_019557|||http://purl.uniprot.org/annotation/VAR_034065|||http://purl.uniprot.org/annotation/VAR_060263|||http://purl.uniprot.org/annotation/VAR_060264
http://togogenome.org/gene/9606:TTC7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIF1|||http://purl.uniprot.org/uniprot/Q86TV6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Repeat|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||TPR|||TPR 1|||TPR 10|||TPR 11|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||Tetratricopeptide repeat protein 7 N-terminal|||Tetratricopeptide repeat protein 7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106387|||http://purl.uniprot.org/annotation/VSP_008061
http://togogenome.org/gene/9606:SMAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV97|||http://purl.uniprot.org/uniprot/Q8WU79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Arf-GAP|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PICALM|||Interaction with clathrin heavy chains|||Phosphoserine|||Stromal membrane-associated protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235841|||http://purl.uniprot.org/annotation/VAR_048327|||http://purl.uniprot.org/annotation/VSP_018504|||http://purl.uniprot.org/annotation/VSP_043789
http://togogenome.org/gene/9606:CFC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWV2|||http://purl.uniprot.org/uniprot/A0A087WX98|||http://purl.uniprot.org/uniprot/P0CG37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cryptic protein|||Disordered|||Does not affect the cellular localization and the biological activity.|||EGF-like|||GPI-anchor amidated aspartate|||In HTX2; complete loss of activity; abnormal cell surface localization.|||Increased NODAL dependent signaling.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000044630|||http://purl.uniprot.org/annotation/PRO_0000395407|||http://purl.uniprot.org/annotation/PRO_5001831989|||http://purl.uniprot.org/annotation/PRO_5001832024|||http://purl.uniprot.org/annotation/VAR_024322|||http://purl.uniprot.org/annotation/VAR_024323|||http://purl.uniprot.org/annotation/VAR_024324
http://togogenome.org/gene/9606:HSPA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34932                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heat shock 70 kDa protein 4|||In isoform 2.|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078262|||http://purl.uniprot.org/annotation/VSP_056885
http://togogenome.org/gene/9606:BBX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6U2|||http://purl.uniprot.org/uniprot/Q8WY36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box|||HMG box transcription factor BBX|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232885|||http://purl.uniprot.org/annotation/VAR_061264|||http://purl.uniprot.org/annotation/VSP_018006|||http://purl.uniprot.org/annotation/VSP_054880|||http://purl.uniprot.org/annotation/VSP_054881
http://togogenome.org/gene/9606:LARP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased RNA-binding.|||Disordered|||Does not affect RNA-binding.|||Does not affect binding to the 7SKRNA.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH La-type RNA-binding|||In ALAZS; reduced 2'-O-methylation of U6 snRNAs and defects in mRNA splicing.|||In isoform 2.|||In isoform 3.|||La-related protein 7|||Loss of 7SKRNA-binding and marked decrease in 7SKRNP complex formation.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RRM|||Reduced binding to U6 snRNA without affecting binding to 7SKRNA. Reduced 2'-O-methylation of U6 snRNAs.|||Reduced binding to the 7SKRNA. Does not affect binding to U6 snRNA.|||Strongly reduced binding to the stem loop 4 of 7SKRNA.|||xRRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281143|||http://purl.uniprot.org/annotation/VAR_083351|||http://purl.uniprot.org/annotation/VSP_024021|||http://purl.uniprot.org/annotation/VSP_047390
http://togogenome.org/gene/9606:NDUFC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95298                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MC1DN36; highly decreased mitochondrial membrane respiratory chain NADH dehydrogenase complex I activity; decreased complex I assembly and protein levels.|||In isoform 4.|||In isoform 5.|||NADH dehydrogenase [ubiquinone] 1 subunit C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118837|||http://purl.uniprot.org/annotation/VAR_014486|||http://purl.uniprot.org/annotation/VAR_085236|||http://purl.uniprot.org/annotation/VSP_047317|||http://purl.uniprot.org/annotation/VSP_047318
http://togogenome.org/gene/9606:IGFBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPF0|||http://purl.uniprot.org/uniprot/P17936                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||IGF-binding|||IGFBP N-terminal|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Insulin-like growth factor-binding protein 3|||N-linked (GlcNAc...) (complex) asparagine|||Phosphoserine; by FAM20C|||Polar residues|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014378|||http://purl.uniprot.org/annotation/VAR_021974|||http://purl.uniprot.org/annotation/VAR_025262|||http://purl.uniprot.org/annotation/VAR_025263|||http://purl.uniprot.org/annotation/VAR_025264|||http://purl.uniprot.org/annotation/VAR_036279|||http://purl.uniprot.org/annotation/VAR_036280|||http://purl.uniprot.org/annotation/VSP_047293
http://togogenome.org/gene/9606:ACSM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P461                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-coenzyme A synthetase ACSM6, mitochondrial|||In isoform 2.|||In isoform 3.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337112|||http://purl.uniprot.org/annotation/VAR_043606|||http://purl.uniprot.org/annotation/VAR_063090|||http://purl.uniprot.org/annotation/VAR_063091|||http://purl.uniprot.org/annotation/VSP_033908|||http://purl.uniprot.org/annotation/VSP_033909|||http://purl.uniprot.org/annotation/VSP_033910|||http://purl.uniprot.org/annotation/VSP_033911
http://togogenome.org/gene/9606:SERF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84101                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Small EDRK-rich factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050712|||http://purl.uniprot.org/annotation/VAR_051937|||http://purl.uniprot.org/annotation/VSP_046730|||http://purl.uniprot.org/annotation/VSP_046731|||http://purl.uniprot.org/annotation/VSP_046732
http://togogenome.org/gene/9606:HSPB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQS6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Heat shock protein beta-9|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125950|||http://purl.uniprot.org/annotation/VAR_022054
http://togogenome.org/gene/9606:SOX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56693                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Dimerization (DIM)|||Disordered|||Found in a patient with Kallmann syndrome.|||HMG box|||In PCWH.|||In PCWH; loss of DNA binding and transactivation capacity.|||In PCWH; reduced DNA binding capacity.|||In PCWH; without Hirschsprung disease; reduced DNA binding capacity.|||In WS2E and PCWH; increased DNA binding capacity.|||In WS2E; reduced DNA binding capacity.|||In WS2E; without neurologic involvement.|||In WS4C.|||In WS4C; loss of DNA binding and transactivation capacity.|||In isoform 2.|||Nuclear export signal|||Phosphoserine|||Polar residues|||Transactivation domain (TAC)|||Transactivation domain (TAM)|||Transcription factor SOX-10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048746|||http://purl.uniprot.org/annotation/VAR_003743|||http://purl.uniprot.org/annotation/VAR_021386|||http://purl.uniprot.org/annotation/VAR_066747|||http://purl.uniprot.org/annotation/VAR_066748|||http://purl.uniprot.org/annotation/VAR_066749|||http://purl.uniprot.org/annotation/VAR_066750|||http://purl.uniprot.org/annotation/VAR_066751|||http://purl.uniprot.org/annotation/VAR_066752|||http://purl.uniprot.org/annotation/VAR_066753|||http://purl.uniprot.org/annotation/VAR_066754|||http://purl.uniprot.org/annotation/VAR_066755|||http://purl.uniprot.org/annotation/VAR_066756|||http://purl.uniprot.org/annotation/VAR_066757|||http://purl.uniprot.org/annotation/VAR_066758|||http://purl.uniprot.org/annotation/VAR_072981|||http://purl.uniprot.org/annotation/VAR_072982|||http://purl.uniprot.org/annotation/VAR_072983|||http://purl.uniprot.org/annotation/VAR_072984|||http://purl.uniprot.org/annotation/VAR_072985|||http://purl.uniprot.org/annotation/VSP_053874
http://togogenome.org/gene/9606:ADAM33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A2L3|||http://purl.uniprot.org/uniprot/Q9BZ11                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine switch|||Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 33|||Disordered|||EGF-like|||Extracellular|||Helical|||In a cutaneous metastatic melanoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029142|||http://purl.uniprot.org/annotation/PRO_0000029143|||http://purl.uniprot.org/annotation/PRO_5014083392|||http://purl.uniprot.org/annotation/VAR_021847|||http://purl.uniprot.org/annotation/VAR_029143|||http://purl.uniprot.org/annotation/VAR_029144|||http://purl.uniprot.org/annotation/VAR_030512|||http://purl.uniprot.org/annotation/VAR_030513|||http://purl.uniprot.org/annotation/VAR_030514|||http://purl.uniprot.org/annotation/VAR_030515|||http://purl.uniprot.org/annotation/VAR_030516|||http://purl.uniprot.org/annotation/VAR_030517|||http://purl.uniprot.org/annotation/VAR_030518|||http://purl.uniprot.org/annotation/VAR_030519|||http://purl.uniprot.org/annotation/VAR_030520|||http://purl.uniprot.org/annotation/VAR_030521|||http://purl.uniprot.org/annotation/VAR_030522|||http://purl.uniprot.org/annotation/VAR_066337|||http://purl.uniprot.org/annotation/VSP_005495|||http://purl.uniprot.org/annotation/VSP_015421
http://togogenome.org/gene/9606:KDM5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6M4C8G8|||http://purl.uniprot.org/uniprot/P41229                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ARID|||Abolishes lysine-specific histone demethylase activity.|||Basic and acidic residues|||C5HC2|||De novo mutation found in a patient with intellectual disability.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRXSCJ.|||In MRXSCJ; decreases enzymatic activity.|||In MRXSCJ; impairs enzymatic activity and binding to H3-K9Me3.|||In MRXSCJ; impairs enzymatic activity.|||In MRXSCJ; no effect on subcellular location and enzymatic activity.|||In MRXSCJ; patient fibroblasts show decreased enzymatic activity.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||JmjC|||JmjN|||Lysine-specific demethylase 5C|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200586|||http://purl.uniprot.org/annotation/VAR_022730|||http://purl.uniprot.org/annotation/VAR_022731|||http://purl.uniprot.org/annotation/VAR_022732|||http://purl.uniprot.org/annotation/VAR_022733|||http://purl.uniprot.org/annotation/VAR_032986|||http://purl.uniprot.org/annotation/VAR_032987|||http://purl.uniprot.org/annotation/VAR_032988|||http://purl.uniprot.org/annotation/VAR_032989|||http://purl.uniprot.org/annotation/VAR_032990|||http://purl.uniprot.org/annotation/VAR_065091|||http://purl.uniprot.org/annotation/VAR_074308|||http://purl.uniprot.org/annotation/VSP_000315|||http://purl.uniprot.org/annotation/VSP_026410|||http://purl.uniprot.org/annotation/VSP_043752|||http://purl.uniprot.org/annotation/VSP_043753|||http://purl.uniprot.org/annotation/VSP_053420
http://togogenome.org/gene/9606:HESX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBX0                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Sequence Variant                                                                                  ^@                                                                                  Homeobox|||Homeobox expressed in ES cells 1|||In CPHD5.|||In CPHD5; the mutated protein is associated with impaired transcriptional repression but not DNA binding.|||In CPHD5; unknown pathological significance; loss of DNA binding ability; unable to repress PROP1-mediated activation; no effect on nuclear location; no effect on protein abundance.|||In GHDPA.|||In GHDPA; unable to repress PROP1-mediated activation.|||In SOD; loss of DNA-binding.|||In SOD; mild.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048922|||http://purl.uniprot.org/annotation/VAR_010225|||http://purl.uniprot.org/annotation/VAR_010400|||http://purl.uniprot.org/annotation/VAR_063230|||http://purl.uniprot.org/annotation/VAR_063231|||http://purl.uniprot.org/annotation/VAR_063232|||http://purl.uniprot.org/annotation/VAR_063233|||http://purl.uniprot.org/annotation/VAR_063234|||http://purl.uniprot.org/annotation/VAR_078488
http://togogenome.org/gene/9606:FANCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXW9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination; impairs chromatin binding, foci formation and DNA repair. Abolishes interaction with MTMR15/FAN1. No effect on S-222 phosphorylation by ATM.|||Acidic residues|||Basic and acidic residues|||Disordered|||Fanconi anemia group D2 protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In FANCD2.|||In FANCD2; no effect on ubiquitination.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Interaction with BRCA2|||Interaction with FANCE|||No effect on phosphorylation by ATM.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Reduces phosphorylation by ATM. No effect on ubiquitination, foci formation or DNA repair ability, but impairs S-phase checkpoint activation.|||Reduces phosphorylation by ATM; when associated with A-1401 and A-1404.|||Reduces phosphorylation by ATM; when associated with A-1401 and A-1418.|||Reduces phosphorylation by ATM; when associated with A-1404 and A-1418.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087168|||http://purl.uniprot.org/annotation/VAR_022559|||http://purl.uniprot.org/annotation/VAR_022560|||http://purl.uniprot.org/annotation/VAR_022561|||http://purl.uniprot.org/annotation/VAR_022562|||http://purl.uniprot.org/annotation/VAR_025827|||http://purl.uniprot.org/annotation/VAR_025828|||http://purl.uniprot.org/annotation/VAR_025829|||http://purl.uniprot.org/annotation/VAR_025830|||http://purl.uniprot.org/annotation/VAR_025831|||http://purl.uniprot.org/annotation/VAR_025832|||http://purl.uniprot.org/annotation/VAR_025833|||http://purl.uniprot.org/annotation/VAR_025834|||http://purl.uniprot.org/annotation/VAR_025835|||http://purl.uniprot.org/annotation/VAR_025836|||http://purl.uniprot.org/annotation/VAR_025837|||http://purl.uniprot.org/annotation/VSP_013883|||http://purl.uniprot.org/annotation/VSP_013884|||http://purl.uniprot.org/annotation/VSP_013885|||http://purl.uniprot.org/annotation/VSP_013886|||http://purl.uniprot.org/annotation/VSP_057198
http://togogenome.org/gene/9606:PON1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27169                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In allozyme B; increased arylesterase activity.|||In form B|||May be associated with an increased risk for prostate cancer; associated with decreased activity.|||N-linked (GlcNAc...) asparagine|||No loss of activity.|||Not cleaved|||Proton acceptor|||Reduces activity 10000-fold.|||Removed|||Serum paraoxonase/arylesterase 1|||Substantially reduced activity.|||The signal peptide is cleaved; not associated with HDL.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223281|||http://purl.uniprot.org/annotation/VAR_006043|||http://purl.uniprot.org/annotation/VAR_006044|||http://purl.uniprot.org/annotation/VAR_015882|||http://purl.uniprot.org/annotation/VAR_055342
http://togogenome.org/gene/9606:MPZL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWV2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||Myelin protein zero-like protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280282|||http://purl.uniprot.org/annotation/VAR_031108|||http://purl.uniprot.org/annotation/VAR_031109|||http://purl.uniprot.org/annotation/VAR_050455|||http://purl.uniprot.org/annotation/VAR_050456|||http://purl.uniprot.org/annotation/VSP_053988|||http://purl.uniprot.org/annotation/VSP_055324|||http://purl.uniprot.org/annotation/VSP_055325
http://togogenome.org/gene/9606:TMEM61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0U2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 61                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254130|||http://purl.uniprot.org/annotation/VAR_028820
http://togogenome.org/gene/9606:GRIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05586|||http://purl.uniprot.org/uniprot/Q59GW0|||http://purl.uniprot.org/uniprot/Q5VSF9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Found in a patient with schizophrenia; unknown pathological significance.|||Glutamate receptor|||Glutamate receptor ionotropic, NMDA 1|||Helical|||In DEE101; loss of function in calcium ion transmembrane import into cytosol.|||In NDHMSD.|||In NDHMSD; changed localization to the cell membrane; decreased glutamate-gated calcium ion channel activity.|||In NDHMSD; changed localization to the cell membrane; loss of glutamate-gated calcium ion channel activity.|||In NDHMSD; decreased glutamate-gated calcium ion channel activity.|||In NDHMSD; decreased localization to the plasma membrane of GRIN1/GRIN2BNMDA receptor complexes; changed glutamate-gated calcium ion channel activity; decreased activation by glutamate and glycine; decreased sensitivity to magnesium block; loss of function in calcium ion transmembrane import into cytosol.|||In NDHMSD; loss of function in calcium ion transmembrane import into cytosol.|||In NDHMSD; loss of glutamate-gated calcium ion channel activity.|||In NDHMSD; no effect on glutamate-gated calcium ion channel activity.|||In NDHMSD; there is near abolition of the activity of the NMDA receptor in Xenopus oocytes; alters the 3-dimensional structure at the receptor's channel pore entrance.|||In NDHMSD; this mutation produces a significant increase in NMDA receptor-induced calcium currents; excessive calcium influx through NMDA receptor could lead to excitotoxic neuronal cell damage.|||In NDHMSD; unknown pathological significance.|||In NDHMSD; unknown pathological significance; no effect on glutamate-gated calcium ion channel activity.|||In NDHMSR; changed glutamate-gated calcium ion channel activity; increased inhibition by zinc.|||In NDHMSR; unknown pathological significance.|||In isoform 1.|||In isoform 2.|||In isoform 4 and isoform 6.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 7.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC|||Pore-forming|||Slight decrease in glycine agonist potency; no effect on glutamate agonist potency.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011587|||http://purl.uniprot.org/annotation/PRO_5027165308|||http://purl.uniprot.org/annotation/VAR_049187|||http://purl.uniprot.org/annotation/VAR_066597|||http://purl.uniprot.org/annotation/VAR_066598|||http://purl.uniprot.org/annotation/VAR_069057|||http://purl.uniprot.org/annotation/VAR_079984|||http://purl.uniprot.org/annotation/VAR_079985|||http://purl.uniprot.org/annotation/VAR_079986|||http://purl.uniprot.org/annotation/VAR_079987|||http://purl.uniprot.org/annotation/VAR_079988|||http://purl.uniprot.org/annotation/VAR_079989|||http://purl.uniprot.org/annotation/VAR_079990|||http://purl.uniprot.org/annotation/VAR_079991|||http://purl.uniprot.org/annotation/VAR_079992|||http://purl.uniprot.org/annotation/VAR_079993|||http://purl.uniprot.org/annotation/VAR_079994|||http://purl.uniprot.org/annotation/VAR_079995|||http://purl.uniprot.org/annotation/VAR_079996|||http://purl.uniprot.org/annotation/VAR_079997|||http://purl.uniprot.org/annotation/VAR_079998|||http://purl.uniprot.org/annotation/VAR_079999|||http://purl.uniprot.org/annotation/VAR_080000|||http://purl.uniprot.org/annotation/VAR_080001|||http://purl.uniprot.org/annotation/VAR_080002|||http://purl.uniprot.org/annotation/VAR_080003|||http://purl.uniprot.org/annotation/VSP_000137|||http://purl.uniprot.org/annotation/VSP_000138|||http://purl.uniprot.org/annotation/VSP_000139|||http://purl.uniprot.org/annotation/VSP_011777|||http://purl.uniprot.org/annotation/VSP_011778|||http://purl.uniprot.org/annotation/VSP_011779|||http://purl.uniprot.org/annotation/VSP_045464
http://togogenome.org/gene/9606:FGFRL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJ49|||http://purl.uniprot.org/uniprot/Q8N441                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibroblast growth factor receptor-like 1|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021250|||http://purl.uniprot.org/annotation/VAR_022642|||http://purl.uniprot.org/annotation/VAR_024316
http://togogenome.org/gene/9606:PPY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01298                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Pancreatic icosapeptide|||Pancreatic polypeptide|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025365|||http://purl.uniprot.org/annotation/PRO_0000025366|||http://purl.uniprot.org/annotation/PRO_0000025367|||http://purl.uniprot.org/annotation/VAR_050615|||http://purl.uniprot.org/annotation/VSP_057852
http://togogenome.org/gene/9606:OLFM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTG9|||http://purl.uniprot.org/uniprot/Q6IMJ0|||http://purl.uniprot.org/uniprot/Q96PB7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||N-linked (GlcNAc...) asparagine|||Noelin-3|||Olfactomedin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020080|||http://purl.uniprot.org/annotation/VSP_003769|||http://purl.uniprot.org/annotation/VSP_003770|||http://purl.uniprot.org/annotation/VSP_003771|||http://purl.uniprot.org/annotation/VSP_003772
http://togogenome.org/gene/9606:TREX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ50                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost abolishes enzyme activity.|||In isoform 1.|||Loss of enzyme activity; when associated with A-14. Almost abolishes enzyme activity.|||Loss of enzyme activity; when associated with A-16. Almost abolishes enzyme activity.|||Loss of enzyme activity; when associated with A-188. Almost abolishes enzyme activity.|||Loss of enzyme activity; when associated with A-193. Almost abolishes enzyme activity.|||Proton donor/acceptor|||Strongly reduces DNA-binding; when associated with A-163 and A-167.|||Strongly reduces DNA-binding; when associated with A-165 and A-165.|||Strongly reduces DNA-binding; when associated with A-165 and A-167.|||Three prime repair exonuclease 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109870|||http://purl.uniprot.org/annotation/VAR_025211|||http://purl.uniprot.org/annotation/VSP_060357
http://togogenome.org/gene/9606:RANBP3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VV4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Ran-binding protein 3-like|||RanBD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312749|||http://purl.uniprot.org/annotation/VAR_037557|||http://purl.uniprot.org/annotation/VAR_037558|||http://purl.uniprot.org/annotation/VAR_037559|||http://purl.uniprot.org/annotation/VSP_029893|||http://purl.uniprot.org/annotation/VSP_029894|||http://purl.uniprot.org/annotation/VSP_044463
http://togogenome.org/gene/9606:UTP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYH9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||U3 small nucleolar RNA-associated protein 6 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205754|||http://purl.uniprot.org/annotation/VAR_026668|||http://purl.uniprot.org/annotation/VAR_031222|||http://purl.uniprot.org/annotation/VAR_049322
http://togogenome.org/gene/9606:NPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15118                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cholesterol and 25-hydroxycholesterol binding. Abolishes cholesterol transfer from NPC2 to NPC1.|||Abolishes cholesterol transport. No effect on subcellular location.|||Cytoplasmic|||Decreased affinity for NPC2 and decreased cholesterol transfer from NPC2 to NPC1; when associated with A-88 and A-92.|||Decreased affinity for NPC2 and decreased cholesterol transfer from NPC2 to NPC1; when associated with A-88 and A-96.|||Decreased affinity for NPC2 and decreased cholesterol transfer from NPC2 to NPC1; when associated with A-92 and A-96.|||Decreased cholesterol transport.|||Decreases affinity for NPC2. Abolishes cholesterol transfer from NPC2 to NPC1.|||Di-leucine motif|||Helical|||Important for cholesterol binding|||Important for cholesterol binding and cholesterol transfer from NPC1 to liposomes|||In NPC1.|||In NPC1; adult form.|||In NPC1; decreased affinity for NPC2; decreased cholesterol transfer from NPC2 to NPC1.|||In NPC1; found in the Nova Scotian clinical variant.|||In NPC1; juvenile form.|||In NPC1; late infantile form.|||In NPC1; late infantile form; Common in Japanese.|||In NPC1; partially mislocalized from late endocytic organelles diffusely to the cell periphery; localizes to the endoplasmic reticulum Rab7-negative endosomes and the cell surface; does not clear the lysosomal cholesterol accumulation in NPC1-deficient cells.|||In isoform 2.|||Loss of function.|||Loss of interaction with ebolavirus glycoprotein.|||Loss of location in lysosomes.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||NPC intracellular cholesterol transporter 1|||Nearly abolishes 25-hydroxycholesterol binding. Reduces cholesterol binding.|||Nearly abolishes cholesterol and 25-hydroxycholesterol binding.|||No effect on cholesterol and 25-hydroxycholesterol binding and transfer.|||No effect on cholesterol or 25-hydroxycholesterol binding. Decreases affinity for NPC2. Strongly reduces cholesterol transfer to liposomes in a NPC2-dependent manner.|||No effect on cholesterol or 25-hydroxycholesterol binding. Nearly abolishes cholesterol transfer to liposomes in a NPC2-dependent manner.|||No effect on function; colocalizes with the wild-type protein with Rab7-positive late endosomes; clears the lysosomal cholesterol accumulation in NPC1-deficient cells.|||Reduces glycosylation; when associated with Q-122 and Q-185. No effect on cholesterol and 25-hydroxycholesterol binding.|||Reduces glycosylation; when associated with Q-70 and Q-122. No effect on cholesterol and 25-hydroxycholesterol binding. Strongly reduces cholesterol transfer to liposomes in a NPC2-dependent manner.|||Reduces glycosylation; when associated with Q-70 and Q-185. No effect on cholesterol and 25-hydroxycholesterol binding.|||Required for location in lysosomes|||SSD|||Strongly reduces 25-hydroxycholesterol binding and cholesterol transfer to liposomes in a NPC2-dependent manner.|||Strongly reduces 25-hydroxycholesterol binding. No effect on cholesterol binding.|||Strongly reduces cholesterol and 25-hydroxycholesterol binding.|||Strongly reduces cholesterol transfer to liposomes in a NPC2-dependent manner.|||Strongly reduces interaction with ebolavirus glycoprotein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023261|||http://purl.uniprot.org/annotation/VAR_008815|||http://purl.uniprot.org/annotation/VAR_008816|||http://purl.uniprot.org/annotation/VAR_008817|||http://purl.uniprot.org/annotation/VAR_008818|||http://purl.uniprot.org/annotation/VAR_008819|||http://purl.uniprot.org/annotation/VAR_008820|||http://purl.uniprot.org/annotation/VAR_008821|||http://purl.uniprot.org/annotation/VAR_008822|||http://purl.uniprot.org/annotation/VAR_008823|||http://purl.uniprot.org/annotation/VAR_008824|||http://purl.uniprot.org/annotation/VAR_008825|||http://purl.uniprot.org/annotation/VAR_008826|||http://purl.uniprot.org/annotation/VAR_008827|||http://purl.uniprot.org/annotation/VAR_008828|||http://purl.uniprot.org/annotation/VAR_008829|||http://purl.uniprot.org/annotation/VAR_008830|||http://purl.uniprot.org/annotation/VAR_008831|||http://purl.uniprot.org/annotation/VAR_008832|||http://purl.uniprot.org/annotation/VAR_008833|||http://purl.uniprot.org/annotation/VAR_008834|||http://purl.uniprot.org/annotation/VAR_008835|||http://purl.uniprot.org/annotation/VAR_008836|||http://purl.uniprot.org/annotation/VAR_008837|||http://purl.uniprot.org/annotation/VAR_008838|||http://purl.uniprot.org/annotation/VAR_008839|||http://purl.uniprot.org/annotation/VAR_008840|||http://purl.uniprot.org/annotation/VAR_008841|||http://purl.uniprot.org/annotation/VAR_008842|||http://purl.uniprot.org/annotation/VAR_008843|||http://purl.uniprot.org/annotation/VAR_008844|||http://purl.uniprot.org/annotation/VAR_015561|||http://purl.uniprot.org/annotation/VAR_015562|||http://purl.uniprot.org/annotation/VAR_015563|||http://purl.uniprot.org/annotation/VAR_015564|||http://purl.uniprot.org/annotation/VAR_015565|||http://purl.uniprot.org/annotation/VAR_015566|||http://purl.uniprot.org/annotation/VAR_015567|||http://purl.uniprot.org/annotation/VAR_043172|||http://purl.uniprot.org/annotation/VAR_043173|||http://purl.uniprot.org/annotation/VAR_043174|||http://purl.uniprot.org/annotation/VAR_043175|||http://purl.uniprot.org/annotation/VAR_043176|||http://purl.uniprot.org/annotation/VAR_043177|||http://purl.uniprot.org/annotation/VAR_043178|||http://purl.uniprot.org/annotation/VAR_043179|||http://purl.uniprot.org/annotation/VAR_043180|||http://purl.uniprot.org/annotation/VAR_043181|||http://purl.uniprot.org/annotation/VAR_043182|||http://purl.uniprot.org/annotation/VAR_043183|||http://purl.uniprot.org/annotation/VAR_043184|||http://purl.uniprot.org/annotation/VAR_043185|||http://purl.uniprot.org/annotation/VAR_043187|||http://purl.uniprot.org/annotation/VAR_043188|||http://purl.uniprot.org/annotation/VAR_043189|||http://purl.uniprot.org/annotation/VAR_043190|||http://purl.uniprot.org/annotation/VAR_043191|||http://purl.uniprot.org/annotation/VAR_043192|||http://purl.uniprot.org/annotation/VAR_043193|||http://purl.uniprot.org/annotation/VAR_043194|||http://purl.uniprot.org/annotation/VAR_043195|||http://purl.uniprot.org/annotation/VAR_043196|||http://purl.uniprot.org/annotation/VAR_043197|||http://purl.uniprot.org/annotation/VAR_043198|||http://purl.uniprot.org/annotation/VAR_043199|||http://purl.uniprot.org/annotation/VAR_043200|||http://purl.uniprot.org/annotation/VAR_043201|||http://purl.uniprot.org/annotation/VAR_043202|||http://purl.uniprot.org/annotation/VAR_043203|||http://purl.uniprot.org/annotation/VAR_043204|||http://purl.uniprot.org/annotation/VAR_043205|||http://purl.uniprot.org/annotation/VAR_043206|||http://purl.uniprot.org/annotation/VAR_043207|||http://purl.uniprot.org/annotation/VAR_043208|||http://purl.uniprot.org/annotation/VAR_043209|||http://purl.uniprot.org/annotation/VAR_043210|||http://purl.uniprot.org/annotation/VAR_043211|||http://purl.uniprot.org/annotation/VAR_043212|||http://purl.uniprot.org/annotation/VAR_043213|||http://purl.uniprot.org/annotation/VAR_043214|||http://purl.uniprot.org/annotation/VAR_043215|||http://purl.uniprot.org/annotation/VAR_043216|||http://purl.uniprot.org/annotation/VAR_043217|||http://purl.uniprot.org/annotation/VAR_043218|||http://purl.uniprot.org/annotation/VAR_043219|||http://purl.uniprot.org/annotation/VAR_043220|||http://purl.uniprot.org/annotation/VAR_043221|||http://purl.uniprot.org/annotation/VAR_043222|||http://purl.uniprot.org/annotation/VAR_043223|||http://purl.uniprot.org/annotation/VAR_043224|||http://purl.uniprot.org/annotation/VAR_043225|||http://purl.uniprot.org/annotation/VAR_043226|||http://purl.uniprot.org/annotation/VAR_043227|||http://purl.uniprot.org/annotation/VAR_043228|||http://purl.uniprot.org/annotation/VAR_043229|||http://purl.uniprot.org/annotation/VAR_043230|||http://purl.uniprot.org/annotation/VAR_043231|||http://purl.uniprot.org/annotation/VAR_043232|||http://purl.uniprot.org/annotation/VAR_043233|||http://purl.uniprot.org/annotation/VAR_043234|||http://purl.uniprot.org/annotation/VAR_043235|||http://purl.uniprot.org/annotation/VAR_043236|||http://purl.uniprot.org/annotation/VAR_043237|||http://purl.uniprot.org/annotation/VAR_043238|||http://purl.uniprot.org/annotation/VAR_043239|||http://purl.uniprot.org/annotation/VAR_043240|||http://purl.uniprot.org/annotation/VAR_043241|||http://purl.uniprot.org/annotation/VAR_043242|||http://purl.uniprot.org/annotation/VAR_043243|||http://purl.uniprot.org/annotation/VAR_043244|||http://purl.uniprot.org/annotation/VAR_043245|||http://purl.uniprot.org/annotation/VAR_043246|||http://purl.uniprot.org/annotation/VAR_043247|||http://purl.uniprot.org/annotation/VAR_043248|||http://purl.uniprot.org/annotation/VAR_043249|||http://purl.uniprot.org/annotation/VAR_043250|||http://purl.uniprot.org/annotation/VAR_043251|||http://purl.uniprot.org/annotation/VAR_043252|||http://purl.uniprot.org/annotation/VAR_043253|||http://purl.uniprot.org/annotation/VAR_043254|||http://purl.uniprot.org/annotation/VAR_043255|||http://purl.uniprot.org/annotation/VAR_043256|||http://purl.uniprot.org/annotation/VAR_043257|||http://purl.uniprot.org/annotation/VAR_043258|||http://purl.uniprot.org/annotation/VAR_043259|||http://purl.uniprot.org/annotation/VAR_043260|||http://purl.uniprot.org/annotation/VAR_043261|||http://purl.uniprot.org/annotation/VAR_043262|||http://purl.uniprot.org/annotation/VAR_043263|||http://purl.uniprot.org/annotation/VAR_043264|||http://purl.uniprot.org/annotation/VAR_043265|||http://purl.uniprot.org/annotation/VAR_043266|||http://purl.uniprot.org/annotation/VAR_043267|||http://purl.uniprot.org/annotation/VAR_043268|||http://purl.uniprot.org/annotation/VAR_043269|||http://purl.uniprot.org/annotation/VAR_043270|||http://purl.uniprot.org/annotation/VAR_043271|||http://purl.uniprot.org/annotation/VAR_043272|||http://purl.uniprot.org/annotation/VAR_043273|||http://purl.uniprot.org/annotation/VAR_043274|||http://purl.uniprot.org/annotation/VAR_043275|||http://purl.uniprot.org/annotation/VAR_043276|||http://purl.uniprot.org/annotation/VAR_043277|||http://purl.uniprot.org/annotation/VAR_043278|||http://purl.uniprot.org/annotation/VAR_043279|||http://purl.uniprot.org/annotation/VAR_043280|||http://purl.uniprot.org/annotation/VAR_043281|||http://purl.uniprot.org/annotation/VAR_043282|||http://purl.uniprot.org/annotation/VAR_043283|||http://purl.uniprot.org/annotation/VAR_043284|||http://purl.uniprot.org/annotation/VAR_043285|||http://purl.uniprot.org/annotation/VAR_043286|||http://purl.uniprot.org/annotation/VAR_043287|||http://purl.uniprot.org/annotation/VAR_043288|||http://purl.uniprot.org/annotation/VAR_043289|||http://purl.uniprot.org/annotation/VAR_043290|||http://purl.uniprot.org/annotation/VAR_043291|||http://purl.uniprot.org/annotation/VAR_043292|||http://purl.uniprot.org/annotation/VAR_043293|||http://purl.uniprot.org/annotation/VAR_043294|||http://purl.uniprot.org/annotation/VAR_043295|||http://purl.uniprot.org/annotation/VAR_043296|||http://purl.uniprot.org/annotation/VAR_043297|||http://purl.uniprot.org/annotation/VAR_043298|||http://purl.uniprot.org/annotation/VAR_043299|||http://purl.uniprot.org/annotation/VAR_043300|||http://purl.uniprot.org/annotation/VAR_043301|||http://purl.uniprot.org/annotation/VAR_043302|||http://purl.uniprot.org/annotation/VSP_056431|||http://purl.uniprot.org/annotation/VSP_056432|||http://purl.uniprot.org/annotation/VSP_056433
http://togogenome.org/gene/9606:USP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4E8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||DUSP|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of activity towards polyubiquitin.|||Loss of enzyme activity.|||Mediates interaction with SART3|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||Removed|||USP|||Ubiquitin carboxyl-terminal hydrolase 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080641|||http://purl.uniprot.org/annotation/VSP_005260|||http://purl.uniprot.org/annotation/VSP_005261|||http://purl.uniprot.org/annotation/VSP_045165|||http://purl.uniprot.org/annotation/VSP_045166
http://togogenome.org/gene/9606:ARRDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2F6|||http://purl.uniprot.org/uniprot/Q8NCT1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Variant                                                                                  ^@                                                                                  Arrestin C-terminal-like|||Arrestin domain-containing protein 4|||PPxY motif 1|||PPxY motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244353|||http://purl.uniprot.org/annotation/VAR_026899|||http://purl.uniprot.org/annotation/VAR_026900|||http://purl.uniprot.org/annotation/VAR_026901
http://togogenome.org/gene/9606:CDC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99741                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cell division control protein 6 homolog|||Cy|||Disordered|||Disrupts the interaction with CCNF. Does not disrupt the interaction with CDH1. Increases protein stability.|||Does not change protein stability after CHX addition during mitosis; when associated with A-54 and A-106.|||Does not change protein stability after CHX addition during mitosis; when associated with A-54 and A-74.|||Does not change protein stability after CHX addition during mitosis; when associated with A-74 and A-106.|||Does not change protein stability after CHX addition during mitosis; when associated with D-54 and D-106.|||Does not change protein stability after CHX addition during mitosis; when associated with D-54 and D-74.|||Does not change protein stability after CHX addition during mitosis; when associated with D-74 and D-106.|||In MGORS5.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150979|||http://purl.uniprot.org/annotation/VAR_019349|||http://purl.uniprot.org/annotation/VAR_019350|||http://purl.uniprot.org/annotation/VAR_019351|||http://purl.uniprot.org/annotation/VAR_019352|||http://purl.uniprot.org/annotation/VAR_019353|||http://purl.uniprot.org/annotation/VAR_065493
http://togogenome.org/gene/9606:UGT1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22310                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Increased glucuronosyltransferase activity towards calcidiol.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 1A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036003|||http://purl.uniprot.org/annotation/VAR_024684|||http://purl.uniprot.org/annotation/VAR_052454|||http://purl.uniprot.org/annotation/VAR_058584|||http://purl.uniprot.org/annotation/VAR_059844|||http://purl.uniprot.org/annotation/VAR_061870|||http://purl.uniprot.org/annotation/VSP_053960
http://togogenome.org/gene/9606:NPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20594                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Atrial natriuretic peptide receptor 2|||Cytoplasmic|||Decreased glycosylation. Decreased guanylate cyclase activity.|||Does not affect C-type natriuretic peptide-induced signaling.|||Extracellular|||Guanylate cyclase|||Helical|||In AMD1.|||In AMD1; markedly deficient activity.|||In AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity.|||In AMD1; no effect on subcellular location; changed glycosylation; no effect on C-type natriuretic peptide binding; decreased guanylate cyclase activity; loss of natriuretic peptide receptor activity; dominant negative effect.|||In ECDM; mutant and wild-type alleles have similar expression levels; the mutation results in increased guanylate cyclase activity.|||In ECDM; the mutation results in higher guanylate cyclase activity; causes a 15-fold increase in basal Vmax; has higher affinity for GTP than wild-type in the presence of NPPC; might lead to a structural change that locks the enzyme in a conformation mimicking the ATP-bound state.|||In ECDM; the mutation results in increased guanylate cyclase activity.|||In SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; loss of localization to the plasma membrane.|||In SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; no effect on cell surface expression.|||In SNSK; loss of C-type natriuretic peptide-induced signaling; dominant negative effect; retained in the endoplasmic reticulum.|||In isoform Short.|||Interchain|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012364|||http://purl.uniprot.org/annotation/VAR_011968|||http://purl.uniprot.org/annotation/VAR_022583|||http://purl.uniprot.org/annotation/VAR_022584|||http://purl.uniprot.org/annotation/VAR_022585|||http://purl.uniprot.org/annotation/VAR_022586|||http://purl.uniprot.org/annotation/VAR_022587|||http://purl.uniprot.org/annotation/VAR_022588|||http://purl.uniprot.org/annotation/VAR_022589|||http://purl.uniprot.org/annotation/VAR_022590|||http://purl.uniprot.org/annotation/VAR_022591|||http://purl.uniprot.org/annotation/VAR_022592|||http://purl.uniprot.org/annotation/VAR_022593|||http://purl.uniprot.org/annotation/VAR_042219|||http://purl.uniprot.org/annotation/VAR_042220|||http://purl.uniprot.org/annotation/VAR_071875|||http://purl.uniprot.org/annotation/VAR_071876|||http://purl.uniprot.org/annotation/VAR_071877|||http://purl.uniprot.org/annotation/VAR_074678|||http://purl.uniprot.org/annotation/VAR_074679|||http://purl.uniprot.org/annotation/VAR_074680|||http://purl.uniprot.org/annotation/VAR_074681|||http://purl.uniprot.org/annotation/VAR_074682|||http://purl.uniprot.org/annotation/VAR_074683|||http://purl.uniprot.org/annotation/VAR_076481|||http://purl.uniprot.org/annotation/VSP_001810
http://togogenome.org/gene/9606:CRY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D2X7Z3|||http://purl.uniprot.org/uniprot/A2I2P1|||http://purl.uniprot.org/uniprot/Q49AN0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cryptochrome-2|||Disordered|||Electron transfer via tryptophanyl radical|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Phosphoserine|||Phosphoserine; by DYRK1A and MAPK|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK|||Photolyase/cryptochrome alpha/beta|||Polar residues|||Required for inhibition of CLOCK-BMAL1-mediated transcription                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261148|||http://purl.uniprot.org/annotation/VSP_038970
http://togogenome.org/gene/9606:JADE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2E2|||http://purl.uniprot.org/uniprot/Q6IE81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with KAT7/HBO1 and histones|||Interaction with histones|||N6-acetyllysine|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Jade-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253529|||http://purl.uniprot.org/annotation/VAR_053777|||http://purl.uniprot.org/annotation/VSP_021045|||http://purl.uniprot.org/annotation/VSP_021046|||http://purl.uniprot.org/annotation/VSP_021047
http://togogenome.org/gene/9606:LRRC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 1|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084489|||http://purl.uniprot.org/annotation/VAR_019431|||http://purl.uniprot.org/annotation/VSP_010912|||http://purl.uniprot.org/annotation/VSP_010913
http://togogenome.org/gene/9606:ZNF396                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N95                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||In isoform 2.|||In isoform 3.|||SCAN box|||Zinc finger protein 396                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047563|||http://purl.uniprot.org/annotation/VAR_057418|||http://purl.uniprot.org/annotation/VSP_006923|||http://purl.uniprot.org/annotation/VSP_008768|||http://purl.uniprot.org/annotation/VSP_020993
http://togogenome.org/gene/9606:LAMC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11047|||http://purl.uniprot.org/uniprot/Q6NVY8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Domain II and I|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||Interchain|||Laminin EGF-like 1|||Laminin EGF-like 10|||Laminin EGF-like 11|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5; first part|||Laminin EGF-like 5; second part|||Laminin EGF-like 6|||Laminin EGF-like 7|||Laminin EGF-like 8|||Laminin EGF-like 9|||Laminin IV type A|||Laminin N-terminal|||Laminin subunit gamma-1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017074|||http://purl.uniprot.org/annotation/PRO_5004278115|||http://purl.uniprot.org/annotation/VAR_014700|||http://purl.uniprot.org/annotation/VAR_014701|||http://purl.uniprot.org/annotation/VAR_014702|||http://purl.uniprot.org/annotation/VAR_035821|||http://purl.uniprot.org/annotation/VAR_054488|||http://purl.uniprot.org/annotation/VAR_080757
http://togogenome.org/gene/9606:PRR30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53SZ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Proline-rich protein 30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312276|||http://purl.uniprot.org/annotation/VAR_037469|||http://purl.uniprot.org/annotation/VAR_037470
http://togogenome.org/gene/9606:DRAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N682                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  DNA damage-regulated autophagy modulator protein 1|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287436|||http://purl.uniprot.org/annotation/VSP_056980
http://togogenome.org/gene/9606:AMFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKV5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolished binding to TAB3.|||Basic and acidic residues|||CUE|||Decreased palmitoylation.|||Decreased palmitoylation. No degradation of HMGCR.|||Disordered|||E3 ubiquitin-protein ligase AMFR|||Helical|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||Polar residues|||RING-type|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064579|||http://purl.uniprot.org/annotation/VAR_035790
http://togogenome.org/gene/9606:MOXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UVY6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  DBH-like monooxygenase protein 1|||DOMON|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305217|||http://purl.uniprot.org/annotation/VAR_035185|||http://purl.uniprot.org/annotation/VAR_035186|||http://purl.uniprot.org/annotation/VSP_028288|||http://purl.uniprot.org/annotation/VSP_028289
http://togogenome.org/gene/9606:P4HA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15460|||http://purl.uniprot.org/uniprot/Q05DA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Fe2OG dioxygenase|||In MYP25.|||In MYP25; decreases protein abundance.|||In MYP25; unknown pathological significance.|||In isoform IIa.|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Prolyl 4-hydroxylase subunit alpha-2|||TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022726|||http://purl.uniprot.org/annotation/VAR_074026|||http://purl.uniprot.org/annotation/VAR_074027|||http://purl.uniprot.org/annotation/VAR_074028|||http://purl.uniprot.org/annotation/VSP_004506
http://togogenome.org/gene/9606:PPP1R13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KQ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Apoptosis-stimulating of p53 protein 1|||Asymmetric dimethylarginine|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066962
http://togogenome.org/gene/9606:PPCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAB8                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In CMD2C; decreased phosphopantothenate--cysteine ligase activity; decreased protein abundance in patient fibroblasts.|||In CMD2C; loss of phosphopantothenate--cysteine ligase activity; decreased protein abundance in patient fibroblasts.|||In isoform 2.|||N-acetylalanine|||Phosphopantothenate--cysteine ligase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182040|||http://purl.uniprot.org/annotation/VAR_081990|||http://purl.uniprot.org/annotation/VAR_081991|||http://purl.uniprot.org/annotation/VAR_081992|||http://purl.uniprot.org/annotation/VSP_045796
http://togogenome.org/gene/9606:AP3S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H459|||http://purl.uniprot.org/uniprot/Q92572                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  AP complex mu/sigma subunit|||AP-3 complex subunit sigma-1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193815|||http://purl.uniprot.org/annotation/VAR_059111
http://togogenome.org/gene/9606:BCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCV8|||http://purl.uniprot.org/uniprot/Q9BYV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Carotenoid-cleaving dioxygenase, mitochondrial|||In isoform 2 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143937|||http://purl.uniprot.org/annotation/VAR_047047|||http://purl.uniprot.org/annotation/VAR_047048|||http://purl.uniprot.org/annotation/VAR_047049|||http://purl.uniprot.org/annotation/VSP_008599|||http://purl.uniprot.org/annotation/VSP_008600|||http://purl.uniprot.org/annotation/VSP_046915|||http://purl.uniprot.org/annotation/VSP_046916
http://togogenome.org/gene/9606:GALR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43603                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Galanin receptor type 2|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069466
http://togogenome.org/gene/9606:PRAMEF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DUQ1|||http://purl.uniprot.org/uniprot/P0DUQ2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 15|||PRAME family member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156983|||http://purl.uniprot.org/annotation/PRO_0000453159
http://togogenome.org/gene/9606:AGRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00468                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Agrin|||Agrin C-terminal 110 kDa subunit|||Agrin C-terminal 22 kDa fragment|||Agrin C-terminal 90 kDa fragment|||Agrin N-terminal 110 kDa subunit|||Alternative splice site to produce 'x' isoforms|||Alternative splice site to produce 'y' isoforms|||Alternative splice site to produce 'z' isoforms|||Cleavage, alpha site; by neurotrypsin|||Cleavage, beta site; by neurotrypsin|||Critical for cleavage by neurotrypsin|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Highly important for the agrin receptor complex activity of the 'z(8)' insert|||In CMS8.|||In CMS8; decreased AGRN-induced clustering of AChR by >100-fold and decreased phosphorylation of the MUSK receptor and AChR beta subunit by about 10-fold. Increased binding to alpha-dystroglycan.|||In CMS8; results in decreased AChR clustering.|||In CMS8; results in disruption of the neuromuscular junction architecture; does not affect phosphorylation of MUSK; does not affect AChR clustering.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||Kazal-like 1|||Kazal-like 2|||Kazal-like 3|||Kazal-like 4|||Kazal-like 5|||Kazal-like 6|||Kazal-like 7|||Kazal-like 8|||Kazal-like 9|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||N-linked (GlcNAc...) asparagine|||NtA|||O-linked (Fuc...) serine|||Or C-152 with C-183|||Phosphoserine|||Polar residues|||Pro residues|||SEA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007471|||http://purl.uniprot.org/annotation/PRO_0000421613|||http://purl.uniprot.org/annotation/PRO_0000421614|||http://purl.uniprot.org/annotation/PRO_0000421615|||http://purl.uniprot.org/annotation/PRO_0000421616|||http://purl.uniprot.org/annotation/VAR_048966|||http://purl.uniprot.org/annotation/VAR_068724|||http://purl.uniprot.org/annotation/VAR_068725|||http://purl.uniprot.org/annotation/VAR_068726|||http://purl.uniprot.org/annotation/VAR_068727|||http://purl.uniprot.org/annotation/VAR_068728|||http://purl.uniprot.org/annotation/VAR_068729|||http://purl.uniprot.org/annotation/VAR_068730|||http://purl.uniprot.org/annotation/VAR_068731|||http://purl.uniprot.org/annotation/VAR_068732|||http://purl.uniprot.org/annotation/VAR_068733|||http://purl.uniprot.org/annotation/VAR_068734|||http://purl.uniprot.org/annotation/VAR_068735|||http://purl.uniprot.org/annotation/VAR_068736|||http://purl.uniprot.org/annotation/VAR_068737|||http://purl.uniprot.org/annotation/VAR_068738|||http://purl.uniprot.org/annotation/VAR_068739|||http://purl.uniprot.org/annotation/VAR_068740|||http://purl.uniprot.org/annotation/VAR_068741|||http://purl.uniprot.org/annotation/VAR_068742|||http://purl.uniprot.org/annotation/VAR_068743|||http://purl.uniprot.org/annotation/VAR_068744|||http://purl.uniprot.org/annotation/VAR_068745|||http://purl.uniprot.org/annotation/VAR_069066|||http://purl.uniprot.org/annotation/VAR_071367|||http://purl.uniprot.org/annotation/VAR_071368|||http://purl.uniprot.org/annotation/VAR_071369|||http://purl.uniprot.org/annotation/VSP_045753|||http://purl.uniprot.org/annotation/VSP_045754|||http://purl.uniprot.org/annotation/VSP_045755|||http://purl.uniprot.org/annotation/VSP_045756|||http://purl.uniprot.org/annotation/VSP_045757|||http://purl.uniprot.org/annotation/VSP_045758
http://togogenome.org/gene/9606:FITM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5D6W6                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Fat storage-inducing transmembrane protein 1|||Helical|||Important for catalytic activity|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319575|||http://purl.uniprot.org/annotation/VSP_031493
http://togogenome.org/gene/9606:PLXNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15031                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage by proprotein convertases.|||Cleavage; by proprotein convertases|||Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Plexin-B2|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024673|||http://purl.uniprot.org/annotation/VAR_050600|||http://purl.uniprot.org/annotation/VAR_061537
http://togogenome.org/gene/9606:ANKRD13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZTS7|||http://purl.uniprot.org/uniprot/Q8IZ07|||http://purl.uniprot.org/uniprot/Q9Y5A3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Abolishes 'Lys-63'-linked ubiquitin binding and strongly inhibits interaction with EGFR. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 557-G--A-561. Strongly inhibits 'Lys-63'-linked ubiquitin binding; when associated with 527-G--A-531 and 557-G--A-561. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 491-G--A-495, 527-G--A-531 and 557-G--A-561.|||Ankyrin repeat domain-containing protein 13A|||No effect on 'Lys-63'-linked ubiquitin binding and interaction with EGFR. No effect on 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 491-G--A-495. Inhibits 'Lys-63'-linked ubiquitin binding; when associated with 557-G--A-561. Inhibits 'Lys-63'-linked ubiquitin binding; when associated with 491-G--A-495 and 557-G--A-561. Strongly inhibits 'Lys-63'-linked ubiquitin binding; when associated with 557-G--A-561 and 582-G--A-586. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 491-G--A-495, 557-G--A-561 and 582-G--A-586.|||No effect on 'Lys-63'-linked ubiquitin binding and interaction with EGFR. No effect on 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 527-G--A-531. Inhibits 'Lys-63'-linked ubiquitin binding; when associated with 527-G--A-531 and 557-G--A-561. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 527-G--A-531, 557-G--A-561 and 582-G--A-586.|||Phosphoserine|||Slightly inhibits 'Lys-63'-linked ubiquitin binding and strongly inhibits interaction with EGFR. No effect on 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 527-G--A-531. Inhibits 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 491-G--A-495 and 527-G--A-531. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 582-V--S-586. Abolishes 'Lys-63'-linked ubiquitin binding and interaction with EGFR; when associated with 491-G--A-495, 527-G--A-531 and 582-G--A-586.|||UIM 1|||UIM 2|||UIM 3|||UIM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066909|||http://purl.uniprot.org/annotation/VAR_048276
http://togogenome.org/gene/9606:HBE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZU7|||http://purl.uniprot.org/uniprot/P02100                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Globin family profile|||Hemoglobin subunit epsilon|||Phosphoserine|||Removed|||distal binding residue|||proximal binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053212
http://togogenome.org/gene/9606:TIMP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99727                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Involved in metalloproteinase-binding|||Metalloproteinase inhibitor 4|||NTR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034349
http://togogenome.org/gene/9606:DUSP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H596                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Dual specificity protein phosphatase 21|||In a colorectal cancer sample; somatic mutation.|||Phosphocysteine intermediate|||Sufficient for mitochondrial localization|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094834|||http://purl.uniprot.org/annotation/VAR_019423|||http://purl.uniprot.org/annotation/VAR_035644
http://togogenome.org/gene/9606:DIO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K415|||http://purl.uniprot.org/uniprot/P49895                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Non standard residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In THMA2; reduced catalytic activity, due to a 2-fold reduction in T4 substrate affinity.|||In THMA2; reduced catalytic activity, due to a 3-fold reduction in T4 substrate affinity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Selenocysteine|||Type I iodothyronine deiodinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154311|||http://purl.uniprot.org/annotation/VAR_087106|||http://purl.uniprot.org/annotation/VAR_087107|||http://purl.uniprot.org/annotation/VSP_012772|||http://purl.uniprot.org/annotation/VSP_012773|||http://purl.uniprot.org/annotation/VSP_012774|||http://purl.uniprot.org/annotation/VSP_012775|||http://purl.uniprot.org/annotation/VSP_012776|||http://purl.uniprot.org/annotation/VSP_012777|||http://purl.uniprot.org/annotation/VSP_012778|||http://purl.uniprot.org/annotation/VSP_012779|||http://purl.uniprot.org/annotation/VSP_012780|||http://purl.uniprot.org/annotation/VSP_012781|||http://purl.uniprot.org/annotation/VSP_012782|||http://purl.uniprot.org/annotation/VSP_012783|||http://purl.uniprot.org/annotation/VSP_012784
http://togogenome.org/gene/9606:RGS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVT7|||http://purl.uniprot.org/uniprot/B3KWG8|||http://purl.uniprot.org/uniprot/H7BXY1|||http://purl.uniprot.org/uniprot/P49796|||http://purl.uniprot.org/uniprot/Q53GP3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In isoform 1.|||In isoform 2.|||In isoform 4 and isoform 9.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9.|||Omega-N-methylarginine|||PDZ|||Phosphoserine|||Polar residues|||Pro residues|||RGS|||Regulator of G-protein signaling 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204182|||http://purl.uniprot.org/annotation/PRO_5002788687|||http://purl.uniprot.org/annotation/VAR_051794|||http://purl.uniprot.org/annotation/VAR_061769|||http://purl.uniprot.org/annotation/VSP_005662|||http://purl.uniprot.org/annotation/VSP_013958|||http://purl.uniprot.org/annotation/VSP_013959|||http://purl.uniprot.org/annotation/VSP_013960|||http://purl.uniprot.org/annotation/VSP_013961|||http://purl.uniprot.org/annotation/VSP_013962|||http://purl.uniprot.org/annotation/VSP_013963|||http://purl.uniprot.org/annotation/VSP_013964|||http://purl.uniprot.org/annotation/VSP_013965|||http://purl.uniprot.org/annotation/VSP_047029|||http://purl.uniprot.org/annotation/VSP_053533|||http://purl.uniprot.org/annotation/VSP_054690
http://togogenome.org/gene/9606:FAM161B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MY7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Protein FAM161B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089890|||http://purl.uniprot.org/annotation/VAR_027963|||http://purl.uniprot.org/annotation/VAR_027964|||http://purl.uniprot.org/annotation/VAR_069168|||http://purl.uniprot.org/annotation/VSP_046328
http://togogenome.org/gene/9606:MTG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT17                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  CP-type G|||In isoform 2.|||Mitochondrial ribosome-associated GTPase 1|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280262|||http://purl.uniprot.org/annotation/VAR_062181|||http://purl.uniprot.org/annotation/VSP_023581|||http://purl.uniprot.org/annotation/VSP_023582
http://togogenome.org/gene/9606:GLB1L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCI6                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Beta-galactosidase-1-like protein 3|||In isoform 2.|||In isoform 4.|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283028|||http://purl.uniprot.org/annotation/VAR_031477|||http://purl.uniprot.org/annotation/VAR_031478|||http://purl.uniprot.org/annotation/VSP_024280|||http://purl.uniprot.org/annotation/VSP_024283|||http://purl.uniprot.org/annotation/VSP_024284
http://togogenome.org/gene/9606:RAB37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylthreonine|||Ras-related protein Rab-37|||Removed|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121249|||http://purl.uniprot.org/annotation/PRO_0000370828|||http://purl.uniprot.org/annotation/VAR_034434|||http://purl.uniprot.org/annotation/VSP_041268|||http://purl.uniprot.org/annotation/VSP_043155|||http://purl.uniprot.org/annotation/VSP_043156
http://togogenome.org/gene/9606:NLRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C000                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by coronavirus SARS-CoV-2 proteinase nsp5|||(Microbial infection) Cleavage; by human rhinovirus 14 (HRV-14) Protease 3C|||Abolished ability to form the NLRP1 inflammasome.|||Abolished cleavage by the 3C-like proteinase nsp5 from human coronavirus SARS-CoV-2.|||Abolished formation of an inflammasome filament together with PYCARD/ASC.|||Abolished inflammasome filament formation. Impaired ability to induce programmed cell death, but retains CAPS1 processing.|||Basic and acidic residues|||CARD|||Cleavage; by autolysis|||Complete loss of autocatalytic processing and IL1B release. Autocatalytic processing cannot be restored by treatment with hydroxylamine.|||Complete loss of autocatalytic processing and of IL1B release.|||Complete loss of autocatalytic processing and of IL1B release. Autocatalytic processing can be restored by treatment with hydroxylamine.|||Complete loss of autocatalytic processing and of IL1B release. Autocatalytic processing cannot be restored by treatment with hydroxylamine.|||Complete loss of autocatalytic processing and of IL1B release. Autocatalytic processing cannot be restored by treatment with hydroxylamine. Abolished interaction with DPP9. Loss of activation by dsRNA or positive-strand RNA virus.|||Complete loss of autocatalytic processing, which can be restored by treatment with hydroxylamine.|||Disordered|||Does not affect ability to induce programmed cell death.|||Does not affect formation of an inflammasome filament together with PYCARD/ASC.|||FIIND|||Impaired ability to form the NLRP1 inflammasome.|||Impaired ability to induce programmed cell death.|||Impaired ability to induce programmed cell death. Abolished formation of an inflammasome filament together with PYCARD/ASC.|||In 3A mutant; abolished activation of the NLRP1 inflammasome in response to UV-B irradiation and ribosome collisions.|||In AIADK; decreased interaction with DPP9, leading to increased inflammasome activity.|||In AIADK; unknown pathological significance.|||In JRRP; gain-of-function variant resulting in spontaneous inflammasome activation; increased NLRP1-inflammasome complex assembly.|||In MSPC; destabilization of the N-terminal fragment.|||In MSPC; increased NLRP1-inflammasome complex assembly.|||In MSPC; increased NLRP1-inflammasome complex assembly; altered protein folding.|||In VAMAS1; risk factor.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 5.|||Increased autocatalytic processing and IL1B release.|||Inhibits cleavage by HRV-14 Protease 3C.|||Inhibits cleavage by Protease 3C from Coxsackievirus B3 and HRV-14.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||Loss of ATP binding.|||NACHT|||NACHT, LRR and PYD domains-containing protein 1|||NACHT, LRR and PYD domains-containing protein 1, C-terminus|||NACHT, LRR and PYD domains-containing protein 1, N-terminus|||No effect on autocatalytic processing, nor on IL1B release.|||No effect on cleavage by HRV-14 Protease 3C.|||No effect.|||Partial loss of autocatalytic processing (50%) and of IL1B release (50%).|||Partial loss of autocatalytic processing and of IL1B release.|||Phosphoserine; by MAP3K20|||Phosphoserine; by MAPK11|||Phosphoserine; by MAPK11 and MAP3K20|||Phosphoserine; by MAPK11 and MAPK14|||Phosphoserine; by MAPK11 and MAPk14|||Phosphoserine; by MAPK14|||Phosphothreonine; by MAP3K20|||Phosphothreonine; by MAPK11|||Phosphothreonine; by MAPK11 and MAP3K20|||Phosphothreonine; by MAPK11, MAPK14 and MAP3K20|||Polar residues|||Pyrin|||Reduced autocatalytic processing and reduced interaction with DPP9.|||Slightly reduced formation of an inflammasome filament together with PYCARD/ASC.|||UPA|||ZAKalpha motif 1|||ZAKalpha motif 2|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096710|||http://purl.uniprot.org/annotation/PRO_0000452851|||http://purl.uniprot.org/annotation/PRO_0000452852|||http://purl.uniprot.org/annotation/VAR_020437|||http://purl.uniprot.org/annotation/VAR_021886|||http://purl.uniprot.org/annotation/VAR_024238|||http://purl.uniprot.org/annotation/VAR_024239|||http://purl.uniprot.org/annotation/VAR_033239|||http://purl.uniprot.org/annotation/VAR_033240|||http://purl.uniprot.org/annotation/VAR_033241|||http://purl.uniprot.org/annotation/VAR_033242|||http://purl.uniprot.org/annotation/VAR_033243|||http://purl.uniprot.org/annotation/VAR_033244|||http://purl.uniprot.org/annotation/VAR_069901|||http://purl.uniprot.org/annotation/VAR_078798|||http://purl.uniprot.org/annotation/VAR_078799|||http://purl.uniprot.org/annotation/VAR_078800|||http://purl.uniprot.org/annotation/VAR_078801|||http://purl.uniprot.org/annotation/VAR_078802|||http://purl.uniprot.org/annotation/VAR_083844|||http://purl.uniprot.org/annotation/VSP_004326|||http://purl.uniprot.org/annotation/VSP_004327|||http://purl.uniprot.org/annotation/VSP_053803|||http://purl.uniprot.org/annotation/VSP_053804|||http://purl.uniprot.org/annotation/VSP_053805
http://togogenome.org/gene/9606:MYL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60660                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand 3|||In isoform Smooth muscle.|||Myosin light polypeptide 6|||N-acetylcysteine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198690|||http://purl.uniprot.org/annotation/VAR_034118|||http://purl.uniprot.org/annotation/VAR_050457|||http://purl.uniprot.org/annotation/VSP_009735
http://togogenome.org/gene/9606:PYGO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T170|||http://purl.uniprot.org/uniprot/Q9BRQ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Nuclear localization signal|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Pygopus homolog 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097123
http://togogenome.org/gene/9606:TMEM199                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N511                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In CDG2P.|||N-acetylalanine|||Removed|||Transmembrane protein 199                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079298|||http://purl.uniprot.org/annotation/VAR_033749|||http://purl.uniprot.org/annotation/VAR_033750|||http://purl.uniprot.org/annotation/VAR_075770|||http://purl.uniprot.org/annotation/VAR_075771|||http://purl.uniprot.org/annotation/VAR_075772
http://togogenome.org/gene/9606:CLIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DZ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||Acidic residues|||CAP-Gly 1|||CAP-Gly 2|||CAP-Gly domain-containing linker protein 3|||Disordered|||GoLD|||Inhibits interaction with ZDHHC13 and ZDHHC17.|||Phosphoserine|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine|||Strongly reduced plasma membrane association and decrease in the levels of Akt at the plasma membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076212|||http://purl.uniprot.org/annotation/VAR_027962
http://togogenome.org/gene/9606:PDP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2J9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Transit Peptide                                                                                  ^@                                                                                  Mitochondrion|||PPM-type phosphatase|||[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025421
http://togogenome.org/gene/9606:RTL6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICC9|||http://purl.uniprot.org/uniprot/Q9BQJ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Retrotransposon Gag-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289097
http://togogenome.org/gene/9606:C12orf43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRA4|||http://purl.uniprot.org/uniprot/B4DWJ9|||http://purl.uniprot.org/uniprot/E7ENF1|||http://purl.uniprot.org/uniprot/F5H7W8|||http://purl.uniprot.org/uniprot/G5EA44|||http://purl.uniprot.org/uniprot/Q96C57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nucleolar localization signal (NLS)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein CUSTOS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000276850|||http://purl.uniprot.org/annotation/VAR_030491
http://togogenome.org/gene/9606:LRAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95237                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Cytoplasmic|||Does not affect activity.|||Helical|||In LCA14; loss of function.|||LRAT|||Lecithin retinol acyltransferase|||Loss of activity.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152478|||http://purl.uniprot.org/annotation/VAR_018386|||http://purl.uniprot.org/annotation/VAR_063559
http://togogenome.org/gene/9606:FAM43A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2R8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM43A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187024
http://togogenome.org/gene/9606:B4GALT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KMT1|||http://purl.uniprot.org/uniprot/Q9UBV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 7|||Cytoplasmic|||Disordered|||Galactosyltransferase C-terminal|||Helical; Signal-anchor for type II membrane protein|||In EDSSPD1.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080550|||http://purl.uniprot.org/annotation/VAR_010293|||http://purl.uniprot.org/annotation/VAR_010294
http://togogenome.org/gene/9606:SNAP91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2N2|||http://purl.uniprot.org/uniprot/O60641                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Clathrin coat assembly protein AP180|||Disordered|||ENTH|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193864|||http://purl.uniprot.org/annotation/VSP_020997|||http://purl.uniprot.org/annotation/VSP_020998|||http://purl.uniprot.org/annotation/VSP_020999|||http://purl.uniprot.org/annotation/VSP_021000|||http://purl.uniprot.org/annotation/VSP_047049
http://togogenome.org/gene/9606:PPP1R42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4L9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRRCT|||Protein phosphatase 1 regulatory subunit 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326175|||http://purl.uniprot.org/annotation/VSP_032587|||http://purl.uniprot.org/annotation/VSP_032588
http://togogenome.org/gene/9606:MITF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXU1|||http://purl.uniprot.org/uniprot/B4DNC7|||http://purl.uniprot.org/uniprot/O75030|||http://purl.uniprot.org/uniprot/Q8WYR3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-180.|||Abolishes both transcription factor activity and ubiquitination, leading to an inert and stable protein; when associated with A-516.|||Accumulates in the nucleus due to impaired phosphorylation.|||BHLH|||Basic and acidic residues|||DNA-binding regulation|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Impaired phosphorylation by MTOR, leading to abolished ubiquitination and degradation by the SCF(BTRC) complex.|||In CMM8; associated with disease susceptibility; also associated with pheochromocytomas and paragangliomas susceptibility; results in impaired sumoylation.|||In COMMAD.|||In COMMAD; has both cytoplasmic and nuclear localization; decreased binding to M-box or E-box DNA sequences.|||In TADS.|||In WS2A and COMMAD; does not localize to the nucleus; does not bind M-box or E-box DNA sequences; loss of function in transcriptional regulation; dominant negative effect.|||In WS2A.|||In WS2A; unknown pathological significance.|||In isoform 12.|||In isoform A2, isoform B2, isoform C2, isoform H2 and isoform M2.|||In isoform B1 and isoform B2.|||In isoform C1 and isoform C2.|||In isoform H1 and isoform H2.|||In isoform M1, isoform M2 and isoform Mdel.|||In isoform Mdel and isoform 12.|||In isoform Mdel.|||Leucine-zipper|||Loss of phosphorylation and function.|||Loss of sumoylation; when associated with R-289.|||Loss of sumoylation; when associated with R-423.|||MiT/TFE transcription factors N-terminal|||Microphthalmia-associated transcription factor|||Phosphoserine|||Phosphoserine; by GSK3|||Phosphoserine; by MAPK|||Phosphoserine; by MARK3|||Phosphoserine; by MTOR|||Phosphoserine; by RPS6KA1|||Polar residues|||Transactivation|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127276|||http://purl.uniprot.org/annotation/VAR_010297|||http://purl.uniprot.org/annotation/VAR_010298|||http://purl.uniprot.org/annotation/VAR_010299|||http://purl.uniprot.org/annotation/VAR_010300|||http://purl.uniprot.org/annotation/VAR_010301|||http://purl.uniprot.org/annotation/VAR_010302|||http://purl.uniprot.org/annotation/VAR_067367|||http://purl.uniprot.org/annotation/VAR_077922|||http://purl.uniprot.org/annotation/VAR_077923|||http://purl.uniprot.org/annotation/VAR_078311|||http://purl.uniprot.org/annotation/VSP_002124|||http://purl.uniprot.org/annotation/VSP_002125|||http://purl.uniprot.org/annotation/VSP_002126|||http://purl.uniprot.org/annotation/VSP_002127|||http://purl.uniprot.org/annotation/VSP_002128|||http://purl.uniprot.org/annotation/VSP_045178|||http://purl.uniprot.org/annotation/VSP_045179|||http://purl.uniprot.org/annotation/VSP_046438
http://togogenome.org/gene/9606:GEMIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57678                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Gem-associated protein 4|||In NEDMCR; unknown pathological significance.|||Leucine-zipper|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087459|||http://purl.uniprot.org/annotation/VAR_020390|||http://purl.uniprot.org/annotation/VAR_021971|||http://purl.uniprot.org/annotation/VAR_024317|||http://purl.uniprot.org/annotation/VAR_056891|||http://purl.uniprot.org/annotation/VAR_056892|||http://purl.uniprot.org/annotation/VAR_056893|||http://purl.uniprot.org/annotation/VAR_056894|||http://purl.uniprot.org/annotation/VAR_056895|||http://purl.uniprot.org/annotation/VAR_056896|||http://purl.uniprot.org/annotation/VAR_056897|||http://purl.uniprot.org/annotation/VAR_080610|||http://purl.uniprot.org/annotation/VAR_082144
http://togogenome.org/gene/9606:TBC1D26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UD7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Rab-GAP TBC|||TBC1 domain family member 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337019|||http://purl.uniprot.org/annotation/VAR_043563|||http://purl.uniprot.org/annotation/VAR_047676|||http://purl.uniprot.org/annotation/VSP_033825|||http://purl.uniprot.org/annotation/VSP_033826|||http://purl.uniprot.org/annotation/VSP_033827|||http://purl.uniprot.org/annotation/VSP_033828
http://togogenome.org/gene/9606:ALG13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX43|||http://purl.uniprot.org/uniprot/Q9NP73                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Deubiquitinase activity|||Disordered|||For deubiquitinase activity|||Glycosyl transferase family 28 C-terminal|||Glycosyltransferase activity|||In DEE36; de novo mutation detected in unrelated patients.|||In DEE36; disease features include abnormal isoelectric focusing of serum transferrin consistent with a glycosylation defect; enzyme activity at about 17% of wild-type.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nucleophile; for deubiquitinase activity|||OTU|||Pro residues|||Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254573|||http://purl.uniprot.org/annotation/VAR_069218|||http://purl.uniprot.org/annotation/VAR_069412|||http://purl.uniprot.org/annotation/VSP_039298|||http://purl.uniprot.org/annotation/VSP_039299|||http://purl.uniprot.org/annotation/VSP_039300|||http://purl.uniprot.org/annotation/VSP_039301|||http://purl.uniprot.org/annotation/VSP_039302|||http://purl.uniprot.org/annotation/VSP_039303
http://togogenome.org/gene/9606:DDX42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XP3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX42|||Basic and acidic residues|||DEAD box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||N6-acetyllysine|||Necessary for interaction with TP53BP2|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280058|||http://purl.uniprot.org/annotation/VSP_023518
http://togogenome.org/gene/9606:DPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQC3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  2-(3-amino-3-carboxypropyl)histidine synthase subunit 2|||In DEDSSH2; severely impairs diphthamide modification of elongation factor 2.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307889|||http://purl.uniprot.org/annotation/VAR_086299|||http://purl.uniprot.org/annotation/VAR_086300|||http://purl.uniprot.org/annotation/VSP_047151|||http://purl.uniprot.org/annotation/VSP_056052|||http://purl.uniprot.org/annotation/VSP_056053
http://togogenome.org/gene/9606:PCP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48539                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Acidic; binds calcium and is required for modulating the calcium-binding kinetics of calmodulin|||Basic and acidic residues|||Calmodulin regulator protein PCP4|||Decreased calmodulin modulator function.|||Disordered|||IQ|||Loss of the calmodulin modulator function.|||No effect on the calmodulin modulator function.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058306
http://togogenome.org/gene/9606:RDX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YJ88|||http://purl.uniprot.org/uniprot/P35241|||http://purl.uniprot.org/uniprot/Q6PKD3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||FERM|||In DFNB24.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-succinyllysine|||Phosphothreonine; by ROCK2|||Pro residues|||Radixin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219421|||http://purl.uniprot.org/annotation/VAR_036857|||http://purl.uniprot.org/annotation/VAR_036858|||http://purl.uniprot.org/annotation/VAR_036859|||http://purl.uniprot.org/annotation/VSP_045315|||http://purl.uniprot.org/annotation/VSP_045316|||http://purl.uniprot.org/annotation/VSP_045317|||http://purl.uniprot.org/annotation/VSP_045318|||http://purl.uniprot.org/annotation/VSP_047276
http://togogenome.org/gene/9606:NTRK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7U4|||http://purl.uniprot.org/uniprot/O95193|||http://purl.uniprot.org/uniprot/Q16288|||http://purl.uniprot.org/uniprot/Q96CY4|||http://purl.uniprot.org/uniprot/X5D2R1|||http://purl.uniprot.org/uniprot/X5D7M5|||http://purl.uniprot.org/uniprot/X5DNW6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in patients with CHD; unknown pathological significance.|||Found in patients with CHD; unknown pathological significance; no change in autophosphorylation; no effect on NTRK3 signaling.|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||In a gastric adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung carcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||Interaction with PLC-gamma-1|||Interaction with PLCG1|||Interaction with SHC1|||LRR 1|||LRR 2|||LRRCT|||Loss of autophosphorylation and loss of NTRK3 signaling.|||N-linked (GlcNAc...) asparagine|||NT-3 growth factor receptor|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Probable disease-associated variant found in patients with CHD; associated with CHD susceptibility; no change in autophosphorylation; changed NTRK3 signaling with decreased apoptosis in absence of NTF3.|||Probable disease-associated variant found in patients with CHD; associated with CHD susceptibility; significantly reduced autophosphorylation; decreased NTRK3 signaling associated with decreased apoptosis in absence of NTF3.|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016731|||http://purl.uniprot.org/annotation/PRO_5004955312|||http://purl.uniprot.org/annotation/PRO_5010157049|||http://purl.uniprot.org/annotation/PRO_5010157057|||http://purl.uniprot.org/annotation/PRO_5014312573|||http://purl.uniprot.org/annotation/VAR_041471|||http://purl.uniprot.org/annotation/VAR_041472|||http://purl.uniprot.org/annotation/VAR_041473|||http://purl.uniprot.org/annotation/VAR_041474|||http://purl.uniprot.org/annotation/VAR_041475|||http://purl.uniprot.org/annotation/VAR_041476|||http://purl.uniprot.org/annotation/VAR_046521|||http://purl.uniprot.org/annotation/VAR_046522|||http://purl.uniprot.org/annotation/VAR_046523|||http://purl.uniprot.org/annotation/VAR_046524|||http://purl.uniprot.org/annotation/VAR_046770|||http://purl.uniprot.org/annotation/VAR_046771|||http://purl.uniprot.org/annotation/VAR_046772|||http://purl.uniprot.org/annotation/VAR_074601|||http://purl.uniprot.org/annotation/VAR_074602|||http://purl.uniprot.org/annotation/VAR_074603|||http://purl.uniprot.org/annotation/VAR_074604|||http://purl.uniprot.org/annotation/VAR_074605|||http://purl.uniprot.org/annotation/VAR_074606|||http://purl.uniprot.org/annotation/VSP_002924|||http://purl.uniprot.org/annotation/VSP_002925|||http://purl.uniprot.org/annotation/VSP_002926|||http://purl.uniprot.org/annotation/VSP_002927
http://togogenome.org/gene/9606:UGT2B17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75795                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||UDP-glucuronosyltransferase 2B17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036041
http://togogenome.org/gene/9606:CPLX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14810                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Complexin-1|||Disordered|||In DEE63.|||In DEE63; unknown pathological significance.|||Interaction with the SNARE complex                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144870|||http://purl.uniprot.org/annotation/VAR_080795|||http://purl.uniprot.org/annotation/VAR_080796|||http://purl.uniprot.org/annotation/VAR_080797
http://togogenome.org/gene/9606:AHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZD4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-hemoglobin-stabilizing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064509|||http://purl.uniprot.org/annotation/VAR_050650
http://togogenome.org/gene/9606:SEMA3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGV8|||http://purl.uniprot.org/uniprot/B4DEK9|||http://purl.uniprot.org/uniprot/Q13214|||http://purl.uniprot.org/uniprot/Q6PI51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like|||Ig-like C2-type|||In a non-small cell lung cancer cell line.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sema|||Semaphorin-3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032309|||http://purl.uniprot.org/annotation/PRO_5002178529|||http://purl.uniprot.org/annotation/VAR_014221|||http://purl.uniprot.org/annotation/VAR_014222|||http://purl.uniprot.org/annotation/VAR_014223|||http://purl.uniprot.org/annotation/VSP_023032
http://togogenome.org/gene/9606:ZNF229                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVZ7|||http://purl.uniprot.org/uniprot/Q9UJW7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 229                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047470|||http://purl.uniprot.org/annotation/VAR_057408|||http://purl.uniprot.org/annotation/VAR_057409|||http://purl.uniprot.org/annotation/VAR_060426|||http://purl.uniprot.org/annotation/VAR_060427|||http://purl.uniprot.org/annotation/VAR_061942|||http://purl.uniprot.org/annotation/VSP_054778
http://togogenome.org/gene/9606:ELFN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5R3F8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein phosphatase 1 regulatory subunit 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256138
http://togogenome.org/gene/9606:CFAP46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYW2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cilia- and flagella-associated protein 46|||Disordered|||In isoform 2.|||In isoform 3.|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089812|||http://purl.uniprot.org/annotation/VAR_023208|||http://purl.uniprot.org/annotation/VAR_023209|||http://purl.uniprot.org/annotation/VAR_046201|||http://purl.uniprot.org/annotation/VAR_056823|||http://purl.uniprot.org/annotation/VAR_056824|||http://purl.uniprot.org/annotation/VAR_056825|||http://purl.uniprot.org/annotation/VAR_056826|||http://purl.uniprot.org/annotation/VSP_042255|||http://purl.uniprot.org/annotation/VSP_042256|||http://purl.uniprot.org/annotation/VSP_042257|||http://purl.uniprot.org/annotation/VSP_042258
http://togogenome.org/gene/9606:MTRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75570                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  GGQ|||GGQ domain|||Impaired mitochondrial peptide chain release factor activity.|||In isoform 2.|||Mitochondrion|||N5-methylglutamine|||Peptide chain release factor 1, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030333|||http://purl.uniprot.org/annotation/VAR_024603|||http://purl.uniprot.org/annotation/VAR_034447|||http://purl.uniprot.org/annotation/VAR_051789|||http://purl.uniprot.org/annotation/VSP_055858|||http://purl.uniprot.org/annotation/VSP_055859
http://togogenome.org/gene/9606:DNAJA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5C0|||http://purl.uniprot.org/uniprot/P31689                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CR-type|||CXXCXGXG motif|||Cysteine methyl ester|||Disordered|||DnaJ homolog subfamily A member 1|||In isoform 2.|||J|||Loss of farnesylation.|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071008|||http://purl.uniprot.org/annotation/PRO_0000393941|||http://purl.uniprot.org/annotation/VSP_046566
http://togogenome.org/gene/9606:OR8U3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH85                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8U3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150612|||http://purl.uniprot.org/annotation/VAR_024102|||http://purl.uniprot.org/annotation/VAR_024103|||http://purl.uniprot.org/annotation/VAR_024104|||http://purl.uniprot.org/annotation/VAR_024105|||http://purl.uniprot.org/annotation/VAR_053205|||http://purl.uniprot.org/annotation/VAR_053206|||http://purl.uniprot.org/annotation/VAR_053207|||http://purl.uniprot.org/annotation/VAR_053208|||http://purl.uniprot.org/annotation/VAR_053209
http://togogenome.org/gene/9606:LTB4R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15722                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Leukotriene B4 receptor 1|||N-linked (GlcNAc...) asparagine|||No effect on affinity for leukotriene B4 or on desensitization by GRK6.|||No effect on affinity for leukotriene B4, induces resistance to desensitization by GRK6, but minor effect on phosphorylation by GRK6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069708|||http://purl.uniprot.org/annotation/VAR_060679
http://togogenome.org/gene/9606:STOM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VSL7|||http://purl.uniprot.org/uniprot/P27105                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Band 7|||Basic and acidic residues|||Complete loss of oligomerization and lipid raft association.|||Complete loss of oligomerization.|||Complete loss of oligomerization. No effect on lipid raft association.|||Complete loss of oligomerization. Reduced lipid raft association.|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Interaction with LANCL1|||No effect on oligomerization.|||Oligomerization reduced to 18%. Reduced lipid raft association.|||Phosphoserine|||Phosphoserine; by PKA|||Reduced oligomerization and lipid raft association.|||Required for homooligomerization|||Required for lipid raft association|||S-palmitoyl cysteine|||S-palmitoyl cysteine; partial|||Stomatin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094027|||http://purl.uniprot.org/annotation/VSP_044669
http://togogenome.org/gene/9606:RHOBTB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94955                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes ATP-binding.|||Abolishes interaction with RAB9A.|||BTB 1|||BTB 2|||Does not affect subcellular location, suggesting this protein is not prenylated.|||Interaction with Rab9|||Rho-like|||Rho-related BTB domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198964|||http://purl.uniprot.org/annotation/VAR_018481|||http://purl.uniprot.org/annotation/VAR_018482|||http://purl.uniprot.org/annotation/VAR_030490
http://togogenome.org/gene/9606:LCE5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCM9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 5A|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235339|||http://purl.uniprot.org/annotation/VAR_053487
http://togogenome.org/gene/9606:AKAP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  A-kinase anchor protein 11|||Disordered|||PKA-RII subunit binding domain|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064517|||http://purl.uniprot.org/annotation/VAR_020131|||http://purl.uniprot.org/annotation/VAR_048207|||http://purl.uniprot.org/annotation/VAR_048208
http://togogenome.org/gene/9606:TIMM23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14925                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial import inner membrane translocase subunit Tim23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210302
http://togogenome.org/gene/9606:RNF43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KSE3|||http://purl.uniprot.org/uniprot/Q68DV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Dominant-negative mutant, loss of E3 ligase activity and activation of the Wnt signaling pathway; when associated with S-290.|||Dominant-negative mutant, loss of E3 ligase activity and activation of the Wnt signaling pathway; when associated with S-292.|||Dominant-negative mutant, loss of E3 ligase activity and activation of the Wnt signaling pathway; when associated with S-295.|||Dominant-negative mutant, loss of E3 ligase activity and activation of the Wnt signaling pathway; when associated with S-298.|||E3 ubiquitin-protein ligase RNF43|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||RING-type|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278239|||http://purl.uniprot.org/annotation/VAR_030713|||http://purl.uniprot.org/annotation/VAR_030714|||http://purl.uniprot.org/annotation/VAR_030715|||http://purl.uniprot.org/annotation/VAR_030716|||http://purl.uniprot.org/annotation/VAR_030717|||http://purl.uniprot.org/annotation/VAR_030718|||http://purl.uniprot.org/annotation/VAR_052103|||http://purl.uniprot.org/annotation/VSP_037338|||http://purl.uniprot.org/annotation/VSP_037339|||http://purl.uniprot.org/annotation/VSP_037340
http://togogenome.org/gene/9606:BRMS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9I4|||http://purl.uniprot.org/uniprot/Q9HCU9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Region                                                                                  ^@                                                                                  Acidic residues|||Breast cancer metastasis-suppressor 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064988
http://togogenome.org/gene/9606:FXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3G4|||http://purl.uniprot.org/uniprot/Q16595                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes cleavage to yield frataxin intermediate form and allows accumulation of frataxin(56-210) and frataxin(78-210).|||Abolishes cleavage to yield frataxin mature form and allows accumulation of frataxin(56-210) and frataxin(78-210).|||Abolishes cleavage to yield frataxin mature form and allows the accumulation of frataxin(56-210).|||Does not affect interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.|||Drasticly reduces interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.|||Extramitochondrial frataxin|||Frataxin intermediate form|||Frataxin mature form|||Frataxin(56-210)|||Frataxin(78-210)|||In FRDA.|||In FRDA; mild form; decreases affinity for the SDAU complex by 40-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU.|||In FRDA; reduces interaction with LYRM4; the interaction is rescued by nickel; a murine cellular FRDA model, deleted for endogenous frataxin and expressing human mutant frataxin cDNA shows defects in mitochondrial structure, mitochondrial iron deposits, decreased enzymatic activity of some mitochondrial and cytoplasmic iron-sulfur cluster-containing enzymes, increased RNA-binding activity of ACO1 and increased sensitivity to oxidative stress; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU.|||In FRDA; reduces interaction with LYRM4; the interaction is rescued by nickel; drastically decreases affinity for the SDAU complex by > 75-fold; decreases the level of covalent incorporation of sulfur into both NFS1 and ISCU.|||In isoform 2.|||In isoform 3.|||Loss of interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.|||Mitochondrion|||No effect on processing of wild-type FXN.|||Reduces interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.|||Significantly reduces interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010129|||http://purl.uniprot.org/annotation/PRO_0000010130|||http://purl.uniprot.org/annotation/PRO_0000289331|||http://purl.uniprot.org/annotation/PRO_0000399388|||http://purl.uniprot.org/annotation/PRO_0000456947|||http://purl.uniprot.org/annotation/VAR_002428|||http://purl.uniprot.org/annotation/VAR_002429|||http://purl.uniprot.org/annotation/VAR_008140|||http://purl.uniprot.org/annotation/VAR_016065|||http://purl.uniprot.org/annotation/VAR_016066|||http://purl.uniprot.org/annotation/VAR_049100|||http://purl.uniprot.org/annotation/VAR_087120|||http://purl.uniprot.org/annotation/VAR_087121|||http://purl.uniprot.org/annotation/VAR_087122|||http://purl.uniprot.org/annotation/VSP_001576|||http://purl.uniprot.org/annotation/VSP_047282
http://togogenome.org/gene/9606:PLCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75038                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2|||Basic and acidic residues|||C2|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Necessary for plasma membrane localization|||PH|||PI-PLC X-box|||PI-PLC Y-box|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088507|||http://purl.uniprot.org/annotation/VSP_029067|||http://purl.uniprot.org/annotation/VSP_029068|||http://purl.uniprot.org/annotation/VSP_029069|||http://purl.uniprot.org/annotation/VSP_029070|||http://purl.uniprot.org/annotation/VSP_029071|||http://purl.uniprot.org/annotation/VSP_029072|||http://purl.uniprot.org/annotation/VSP_029073|||http://purl.uniprot.org/annotation/VSP_029074
http://togogenome.org/gene/9606:TMEM161A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX61                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Transmembrane protein 161A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288084|||http://purl.uniprot.org/annotation/VAR_036537|||http://purl.uniprot.org/annotation/VSP_046042
http://togogenome.org/gene/9606:UGT1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35503|||http://purl.uniprot.org/uniprot/Q5DT01                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036002|||http://purl.uniprot.org/annotation/PRO_5009998740|||http://purl.uniprot.org/annotation/VAR_052445|||http://purl.uniprot.org/annotation/VAR_052446|||http://purl.uniprot.org/annotation/VAR_052447|||http://purl.uniprot.org/annotation/VAR_052448|||http://purl.uniprot.org/annotation/VAR_052449|||http://purl.uniprot.org/annotation/VAR_052450|||http://purl.uniprot.org/annotation/VAR_052451|||http://purl.uniprot.org/annotation/VAR_052452|||http://purl.uniprot.org/annotation/VAR_052453|||http://purl.uniprot.org/annotation/VAR_058583|||http://purl.uniprot.org/annotation/VSP_053959
http://togogenome.org/gene/9606:TTLL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Disordered|||Essential for specifying initiation versus elongation step of the polyglutamylase activity|||Probable tubulin polyglutamylase TTLL2|||TTL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212440|||http://purl.uniprot.org/annotation/VAR_028119|||http://purl.uniprot.org/annotation/VAR_028120|||http://purl.uniprot.org/annotation/VAR_028121|||http://purl.uniprot.org/annotation/VAR_028122|||http://purl.uniprot.org/annotation/VAR_028123|||http://purl.uniprot.org/annotation/VAR_028124|||http://purl.uniprot.org/annotation/VAR_057312|||http://purl.uniprot.org/annotation/VAR_057313|||http://purl.uniprot.org/annotation/VAR_057314|||http://purl.uniprot.org/annotation/VAR_061866
http://togogenome.org/gene/9606:SIN3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z392|||http://purl.uniprot.org/uniprot/M0QYC5|||http://purl.uniprot.org/uniprot/O75182                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Histone deacetylase interacting|||In isoform 2.|||In isoform 3.|||Interaction with CRY1|||Interaction with NCOR1|||Interaction with REST|||Interaction with SUDS3 and HDAC1|||PAH 1|||PAH 2|||PAH 3|||Paired amphipathic helix protein Sin3b|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121539|||http://purl.uniprot.org/annotation/VSP_014185|||http://purl.uniprot.org/annotation/VSP_014186
http://togogenome.org/gene/9606:CD70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U5JA32|||http://purl.uniprot.org/uniprot/P32970                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD70 antigen|||Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In LPFS3; loss of interaction with CD27.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TNF family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185497|||http://purl.uniprot.org/annotation/VAR_081988|||http://purl.uniprot.org/annotation/VAR_081989|||http://purl.uniprot.org/annotation/VSP_056416
http://togogenome.org/gene/9606:MMP12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39900                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||Macrophage metalloelastase|||N-linked (GlcNAc...) asparagine|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028776|||http://purl.uniprot.org/annotation/PRO_0000028777|||http://purl.uniprot.org/annotation/VAR_021343|||http://purl.uniprot.org/annotation/VAR_021344
http://togogenome.org/gene/9606:GNB1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYB4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Guanine nucleotide-binding protein subunit beta-like protein 1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051008|||http://purl.uniprot.org/annotation/VAR_024698|||http://purl.uniprot.org/annotation/VAR_035882|||http://purl.uniprot.org/annotation/VAR_053394|||http://purl.uniprot.org/annotation/VAR_053395|||http://purl.uniprot.org/annotation/VSP_006767|||http://purl.uniprot.org/annotation/VSP_006768
http://togogenome.org/gene/9606:H2AX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16104                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Decreased acetylation and reduced H2AXK119ub ubiquitination.|||Disordered|||Displays a reduced apoptotic response. S-140 phosphorylation is reduced.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Histone H2AX|||Impaired phosphorylation without affecting H2AXK5ac acetylation.|||N-acetylserine|||N6-acetyllysine|||N6-lactoyllysine; alternate|||Phosphoserine|||Phosphoserine; by ATM, ATR and PRKDC|||Phosphotyrosine; by WSTF|||Reduced phosphorylation of S-140 in response to DNA damage.|||Removed|||[ST]-Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055242
http://togogenome.org/gene/9606:SYN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRB3|||http://purl.uniprot.org/uniprot/Q59GM1|||http://purl.uniprot.org/uniprot/Q86VA8|||http://purl.uniprot.org/uniprot/Q92777                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  A|||B; linker|||C; actin-binding and synaptic-vesicle binding|||Disordered|||E|||G; Pro-rich linker|||H; Pro/Ser-rich linker|||In isoform IIb.|||Phosphoserine|||Phosphoserine; by PKA and CaMK1|||Phosphothreonine|||Polar residues|||Pro residues|||Synapsin ATP-binding|||Synapsin pre-ATP-grasp|||Synapsin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183021|||http://purl.uniprot.org/annotation/VAR_059825|||http://purl.uniprot.org/annotation/VSP_006320|||http://purl.uniprot.org/annotation/VSP_006321
http://togogenome.org/gene/9606:FEM1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Abolished binding to C-degron with an arginine at the C-terminus.|||Found in a patient with neurodevelopmental disorder with absent speech, pyramidal signs and limb ataxia; probable disease-associated variant.|||In a breast cancer sample; somatic mutation.|||Modifies specificity for C-degron at the C-terminus and promotes increased affinity for C-degrons usually recognized by FEM1B; when associated with A-183--F-188.|||Modifies specificity for C-degron at the C-terminus and promotes increased affinity for C-degrons usually recognized by FEM1B; when associated with N-150.|||N-acetylmethionine|||Nearly abolished binding to C-degron with an arginine at the C-terminus.|||Protein fem-1 homolog C|||Reduced binding to C-degron with an arginine at the C-terminus.|||Reduced binding to C-degron with an arginine at the C-terminus. Abolished binding to C-degron with an arginine at the C-terminus; when associated with A-126.|||Reduced binding to C-degron with an arginine at the C-terminus. Abolished binding to C-degron with an arginine at the C-terminus; when associated with A-77.|||Strongly reduced binding to C-degron with an arginine at the C-terminus.|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324536|||http://purl.uniprot.org/annotation/VAR_039810|||http://purl.uniprot.org/annotation/VAR_039811|||http://purl.uniprot.org/annotation/VAR_087634
http://togogenome.org/gene/9606:CTNNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGU4|||http://purl.uniprot.org/uniprot/P35222                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Phosphothreonine|||ARM|||ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Abolished phosphorylation by SRC and interaction with isoform M2 of PKM (PKM2).|||Abolishes APC binding.|||Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386.|||Abolishes CTNNBIP1 binding; when associated with A-660.|||Abolishes CTNNBIP1 binding; when associated with A-661.|||Abolishes TCF7L2 and LEF1 binding.|||Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding.|||Abolishes TCF7L2 binding.|||Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-159.|||Abolishes or strongly reduces AXIN1 and AXIN2 binding.|||Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383.|||Abolishes or strongly reduces AXIN2 binding.|||Abolishes phosphorylation by PTK6.|||Catenin beta-1|||Disordered|||In EVR7; unknown pathological significance.|||In MDB and hepatocellular carcinoma; enhances transactivation of target genes.|||In NEDSDV.|||In NEDSDV; the patient also manifest features of exudative vitreoretinopathy.|||In PTR and hepatocellular carcinoma.|||In PTR, MDB and hepatocellular carcinoma.|||In PTR, hepatoblastoma and hepatocellular carcinoma.|||In PTR, hepatoblastoma and ovarian cancer.|||In PTR, hepatocellular carcinoma and ovarian cancer.|||In PTR.|||In colorectal cancer and PTR; constitutively active Wnt signaling pathway; enhances transactivation of target genes.|||In colorectal cancer.|||In hepatoblastoma and hepatocellular carcinoma; also in a desmoid tumor; strongly reduces phosphorylation and degradation; abolishes phosphorylation on Ser-33 and Ser-37 and enhances transactivation of target genes.|||In hepatoblastoma.|||In hepatocellular carcinoma.|||In hepatocellular carcinoma; no effect.|||Interaction with BCL9|||Interaction with SCRIB|||Interaction with VCL|||N-acetylalanine|||N6-acetyllysine|||No effect on interaction with BCL9 and BCL9L.|||No effect on interaction with BCL9 and CDH3.|||No effect on interaction with BCL9 and CDH3. Abolishes interaction with BCL9 but no effect on interaction with CDH3; when associated with A-156.|||No effect.|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by GSK3-beta|||Phosphoserine; by GSK3-beta and HIPK2|||Phosphoserine; by GSK3-beta; alternate|||Phosphothreonine|||Phosphothreonine; by GSK3-beta|||Phosphotyrosine; by FYN and PTK6|||Phosphotyrosine; by PTK6|||Phosphotyrosine; by SRC and PTK6|||Polar residues|||Removed|||S-nitrosocysteine|||Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383.|||Strongly reduces or abolishes LEF1 binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064271|||http://purl.uniprot.org/annotation/VAR_017612|||http://purl.uniprot.org/annotation/VAR_017613|||http://purl.uniprot.org/annotation/VAR_017614|||http://purl.uniprot.org/annotation/VAR_017615|||http://purl.uniprot.org/annotation/VAR_017616|||http://purl.uniprot.org/annotation/VAR_017617|||http://purl.uniprot.org/annotation/VAR_017618|||http://purl.uniprot.org/annotation/VAR_017619|||http://purl.uniprot.org/annotation/VAR_017620|||http://purl.uniprot.org/annotation/VAR_017621|||http://purl.uniprot.org/annotation/VAR_017622|||http://purl.uniprot.org/annotation/VAR_017623|||http://purl.uniprot.org/annotation/VAR_017624|||http://purl.uniprot.org/annotation/VAR_017625|||http://purl.uniprot.org/annotation/VAR_017626|||http://purl.uniprot.org/annotation/VAR_017627|||http://purl.uniprot.org/annotation/VAR_017628|||http://purl.uniprot.org/annotation/VAR_017629|||http://purl.uniprot.org/annotation/VAR_017630|||http://purl.uniprot.org/annotation/VAR_017631|||http://purl.uniprot.org/annotation/VAR_017632|||http://purl.uniprot.org/annotation/VAR_018954|||http://purl.uniprot.org/annotation/VAR_055430|||http://purl.uniprot.org/annotation/VAR_072282|||http://purl.uniprot.org/annotation/VAR_079199|||http://purl.uniprot.org/annotation/VAR_079200
http://togogenome.org/gene/9606:SLBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSC5|||http://purl.uniprot.org/uniprot/B3KST9|||http://purl.uniprot.org/uniprot/B4DUW7|||http://purl.uniprot.org/uniprot/E7EUV9|||http://purl.uniprot.org/uniprot/Q14493|||http://purl.uniprot.org/uniprot/Q53XR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decrease in 3'-end processing efficiency.|||Disordered|||Does not increase its stability at the end of the S phase and through G2 and mitosis.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone RNA hairpin-binding protein|||Histone RNA hairpin-binding protein RNA-binding|||In isoform 2.|||Increases its stability at the end of the S phase and through G2 and mitosis.|||Increases its stability at the end of the S phase and through G2 and mitosis. Active in histone pre-mRNA processing during the G2 phase.|||Increases its stability at the end of the S phase and through G2 and mitosis. Inhibits phosphorylation of T-62. Localizes in the nucleus. Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-241; A-242; A-243 and A-244.|||Inhibits histone RNA-binding and localization to the cytoplasm.|||Nuclear localization signal NLS1|||Nuclear localization signal NLS2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by CK2|||Polar residues|||RNA-binding|||Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-31; A-32; A-33 and A-34 or with A-96; A-97; A-98 and A-99.|||Reduces interaction with the importin alpha/importin beta receptor. Abolishes interaction with the importin alpha/importin beta receptor; when associated with A-96; A-97; A-98 and A-99 or with A-241; A-242; A-243 and A-244.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100356|||http://purl.uniprot.org/annotation/VSP_042164
http://togogenome.org/gene/9606:PICALM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13492                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form CALM/MLLT10 fusion protein|||Disordered|||ENTH|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PIMREG|||N-acetylserine|||Phosphatidylinositol-binding clathrin assembly protein|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187062|||http://purl.uniprot.org/annotation/VAR_028191|||http://purl.uniprot.org/annotation/VAR_028192|||http://purl.uniprot.org/annotation/VAR_028193|||http://purl.uniprot.org/annotation/VAR_028194|||http://purl.uniprot.org/annotation/VAR_028195|||http://purl.uniprot.org/annotation/VSP_004067|||http://purl.uniprot.org/annotation/VSP_009607|||http://purl.uniprot.org/annotation/VSP_009608|||http://purl.uniprot.org/annotation/VSP_044567|||http://purl.uniprot.org/annotation/VSP_044568
http://togogenome.org/gene/9606:DCTN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTE1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Dynactin subunit 5|||In isoform 2.|||In isoform 3.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079827|||http://purl.uniprot.org/annotation/VSP_046023|||http://purl.uniprot.org/annotation/VSP_046697
http://togogenome.org/gene/9606:DAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75553                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disabled homolog 1|||Disordered|||In isoform DAB213.|||In isoform DAB469.|||In isoform DAB537.|||In isoform DAB553 and isoform DAB537.|||In isoform DAB555.|||PID|||Phosphoserine; by CDK5|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079767|||http://purl.uniprot.org/annotation/VAR_056857|||http://purl.uniprot.org/annotation/VSP_026166|||http://purl.uniprot.org/annotation/VSP_026167|||http://purl.uniprot.org/annotation/VSP_026168|||http://purl.uniprot.org/annotation/VSP_026169|||http://purl.uniprot.org/annotation/VSP_026170|||http://purl.uniprot.org/annotation/VSP_026171
http://togogenome.org/gene/9606:EFHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7U6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||EF-hand domain-containing family member B|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252094|||http://purl.uniprot.org/annotation/VAR_027750|||http://purl.uniprot.org/annotation/VAR_027751|||http://purl.uniprot.org/annotation/VAR_027752|||http://purl.uniprot.org/annotation/VAR_055296|||http://purl.uniprot.org/annotation/VAR_055297|||http://purl.uniprot.org/annotation/VAR_055298|||http://purl.uniprot.org/annotation/VSP_020862|||http://purl.uniprot.org/annotation/VSP_020863|||http://purl.uniprot.org/annotation/VSP_020864|||http://purl.uniprot.org/annotation/VSP_020865
http://togogenome.org/gene/9606:MFSD14A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MC6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Hippocampus abundant transcript 1 protein|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084856
http://togogenome.org/gene/9606:BST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10588                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2|||GPI-anchor amidated alanine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004032|||http://purl.uniprot.org/annotation/PRO_0000004033|||http://purl.uniprot.org/annotation/VAR_021964|||http://purl.uniprot.org/annotation/VAR_021965|||http://purl.uniprot.org/annotation/VAR_028438|||http://purl.uniprot.org/annotation/VAR_028439|||http://purl.uniprot.org/annotation/VSP_055507
http://togogenome.org/gene/9606:SPRING1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H741                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Loss of glycosylation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||SREBP regulating gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294329|||http://purl.uniprot.org/annotation/VAR_033154
http://togogenome.org/gene/9606:PSG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15238                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014912|||http://purl.uniprot.org/annotation/VAR_016041|||http://purl.uniprot.org/annotation/VAR_060260|||http://purl.uniprot.org/annotation/VAR_060261|||http://purl.uniprot.org/annotation/VAR_060262
http://togogenome.org/gene/9606:NUMBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGH3|||http://purl.uniprot.org/uniprot/A8K033|||http://purl.uniprot.org/uniprot/B7Z5W0|||http://purl.uniprot.org/uniprot/Q9Y6R0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Numb-like protein|||PID|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057999
http://togogenome.org/gene/9606:ANXA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27216|||http://purl.uniprot.org/uniprot/Q53FB5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin A13|||In isoform B.|||Loss of dimerization. No effect on calcium-dependent membrane binding and location at the cell membrane.|||Loss of myristoylation. Loss of location at the cell membrane.|||N-myristoyl glycine|||Removed|||Slightly increased dimerization. Decreases calcium-dependent membrane binding and location at the cell membrane.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067514|||http://purl.uniprot.org/annotation/VAR_055501|||http://purl.uniprot.org/annotation/VAR_055502|||http://purl.uniprot.org/annotation/VAR_055503|||http://purl.uniprot.org/annotation/VSP_000291
http://togogenome.org/gene/9606:IRF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15306                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  IRF tryptophan pentad repeat|||In isoform 2.|||Interferon regulatory factor 4|||Phosphoserine; by ROCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154556|||http://purl.uniprot.org/annotation/VSP_002755
http://togogenome.org/gene/9606:ENDOV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8Q3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  46% decrease in activity.|||68% decrease in activity.|||Abolishes ability to bind branched DNA and RNA.|||Abolishes ribonuclease activity without affecting ability to bind branched DNA.|||Abolishes ribonuclease activity.|||Disordered|||Does not gain activity against single- or double-stranded DNA.|||Endonuclease V|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 6.|||Interaction with target RNA|||No effect on subcellular location or activity; when associated with A-171.|||No effect on subcellular location or activity; when associated with A-174.|||No significant effect on activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349223|||http://purl.uniprot.org/annotation/VAR_046285|||http://purl.uniprot.org/annotation/VAR_046286|||http://purl.uniprot.org/annotation/VAR_046287|||http://purl.uniprot.org/annotation/VAR_046288|||http://purl.uniprot.org/annotation/VAR_046289|||http://purl.uniprot.org/annotation/VSP_035228|||http://purl.uniprot.org/annotation/VSP_035229|||http://purl.uniprot.org/annotation/VSP_035230|||http://purl.uniprot.org/annotation/VSP_035231|||http://purl.uniprot.org/annotation/VSP_060583
http://togogenome.org/gene/9606:ZNF615                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH87|||http://purl.uniprot.org/uniprot/H9KV89|||http://purl.uniprot.org/uniprot/Q8N8J6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2 and isoform 3.|||In isoform 3.|||KRAB|||Zinc finger protein 615                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047690|||http://purl.uniprot.org/annotation/VAR_037285|||http://purl.uniprot.org/annotation/VAR_037286|||http://purl.uniprot.org/annotation/VAR_037287|||http://purl.uniprot.org/annotation/VSP_029582|||http://purl.uniprot.org/annotation/VSP_039717
http://togogenome.org/gene/9606:JAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TPQ9|||http://purl.uniprot.org/uniprot/P23458|||http://purl.uniprot.org/uniprot/Q6P669                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutively active. Increased receptor signaling pathway via JAK-STAT.|||FERM|||In AIIDE; constitutive gain of function resulting in increased receptor signaling pathway via JAK-STAT; no effect on protein abundance.|||In AIIDE; increased activation of protein kinase activity; constitutive gain of function through the transactivation of associated JAK kinases; increased receptor signaling pathway via JAK-STAT.|||Loss of protein tyrosine kinase activity.|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||SH2|||Tyrosine-protein kinase JAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088108|||http://purl.uniprot.org/annotation/VAR_041715|||http://purl.uniprot.org/annotation/VAR_084991|||http://purl.uniprot.org/annotation/VAR_084992
http://togogenome.org/gene/9606:FHIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49789                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  50% decrease in catalytic activity. No loss in substrate binding.|||75% decrease in catalytic activity. No loss in substrate binding.|||98% decrease in catalytic activity.|||Bis(5'-adenosyl)-triphosphatase|||HIT|||Histidine triad motif|||Impairs induction of apoptosis. Reduces affinity for substrates.|||Impairs induction of apoptosis. Strongly reduced affinity for substrates.|||Important for induction of apoptosis|||Loss of catalytic activity.|||Loss of phosphorylation by SRC. Impairs induction of apoptosis.|||No effect on phosphorylation by SRC.|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Reduces affinity for substrates and impairs apoptosis. Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-10.|||Strongly reduces affinity for substrates and impairs apoptosis; when associated with W-25.|||Tele-AMP-histidine intermediate|||Total loss of catalytic activity. No loss in substrate binding.|||Total loss of catalytic activity. Rescuable with free imidazole.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109789
http://togogenome.org/gene/9606:TCIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR00                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with CBY1.|||Abolishes interaction with CBY1. Forms irregular perinuclear cytoplasmic aggregates.|||No effect on interaction with CBY1.|||No effect on interaction with CBY1. Accumulates at nucleoli periphery.|||Transcriptional and immune response regulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089605|||http://purl.uniprot.org/annotation/VAR_050819
http://togogenome.org/gene/9606:NCOA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXK4|||http://purl.uniprot.org/uniprot/H0Y5F6|||http://purl.uniprot.org/uniprot/Q8N3C8|||http://purl.uniprot.org/uniprot/Q8NI08                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes completely the E2-induced ESR1 binding.|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||LysM|||N-acetylmethionine|||No action on the E2-induced ESR1 binding.|||Nuclear receptor coactivator 7|||Phosphoserine|||Phosphothreonine|||Polar residues|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245229|||http://purl.uniprot.org/annotation/VAR_026965|||http://purl.uniprot.org/annotation/VAR_026966|||http://purl.uniprot.org/annotation/VAR_050438|||http://purl.uniprot.org/annotation/VSP_019632|||http://purl.uniprot.org/annotation/VSP_019633|||http://purl.uniprot.org/annotation/VSP_019634|||http://purl.uniprot.org/annotation/VSP_019635|||http://purl.uniprot.org/annotation/VSP_019636|||http://purl.uniprot.org/annotation/VSP_019637|||http://purl.uniprot.org/annotation/VSP_019638|||http://purl.uniprot.org/annotation/VSP_019639|||http://purl.uniprot.org/annotation/VSP_044859
http://togogenome.org/gene/9606:HID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In DEE105.|||In DEE105; unknown pathological significance.|||In DEE105; unknown pathological significance; patient fibroblasts show normal expression and localization.|||In isoform 2.|||In isoform 3.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||Protein HID1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079296|||http://purl.uniprot.org/annotation/VAR_087635|||http://purl.uniprot.org/annotation/VAR_087636|||http://purl.uniprot.org/annotation/VAR_087637|||http://purl.uniprot.org/annotation/VAR_087638|||http://purl.uniprot.org/annotation/VSP_014472|||http://purl.uniprot.org/annotation/VSP_014473
http://togogenome.org/gene/9606:PCMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22061                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Protein-L-isoaspartate(D-aspartate) O-methyltransferase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000111875|||http://purl.uniprot.org/annotation/VAR_006173|||http://purl.uniprot.org/annotation/VSP_004716
http://togogenome.org/gene/9606:IGSF22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9C0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Fibronectin type-III 1|||Fibronectin type-III 2|||Found in a renal cell carcinoma sample; somatic mutation.|||Ig-like 1|||Ig-like 2|||Ig-like 3|||Ig-like 4|||Immunoglobulin superfamily member 22|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285255|||http://purl.uniprot.org/annotation/VAR_032000|||http://purl.uniprot.org/annotation/VAR_032001|||http://purl.uniprot.org/annotation/VAR_032002|||http://purl.uniprot.org/annotation/VAR_032003|||http://purl.uniprot.org/annotation/VAR_032004|||http://purl.uniprot.org/annotation/VAR_032005|||http://purl.uniprot.org/annotation/VAR_032006|||http://purl.uniprot.org/annotation/VAR_064722|||http://purl.uniprot.org/annotation/VSP_047394|||http://purl.uniprot.org/annotation/VSP_047395
http://togogenome.org/gene/9606:CGB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQP8|||http://purl.uniprot.org/uniprot/P0DN86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Choriogonadotropin subunit beta 3|||Disordered|||Glycoprotein hormone subunit beta|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Pro residues|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000042|||http://purl.uniprot.org/annotation/CAR_000043|||http://purl.uniprot.org/annotation/PRO_0000011676|||http://purl.uniprot.org/annotation/PRO_5014227020|||http://purl.uniprot.org/annotation/VAR_003188|||http://purl.uniprot.org/annotation/VAR_014585|||http://purl.uniprot.org/annotation/VAR_014586|||http://purl.uniprot.org/annotation/VAR_014587|||http://purl.uniprot.org/annotation/VAR_015231|||http://purl.uniprot.org/annotation/VAR_015232|||http://purl.uniprot.org/annotation/VAR_015233|||http://purl.uniprot.org/annotation/VAR_015234|||http://purl.uniprot.org/annotation/VAR_015235|||http://purl.uniprot.org/annotation/VSP_038396
http://togogenome.org/gene/9606:TMEM41B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BJD5                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Reduced infection with Yellow fever virus, Zika virus and Dengue virus; no effect on mobilization of neutral lipids from lipid droplets.|||Reduced infection with flaviviruses such as Yellow fever virus, Zika virus and Dengue virus; no effect on mobilization of neutral lipids from lipid droplets.|||Transmembrane protein 41B|||VTT domain; required for its function in autophagy                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291937|||http://purl.uniprot.org/annotation/VAR_084309|||http://purl.uniprot.org/annotation/VAR_084310|||http://purl.uniprot.org/annotation/VSP_026316|||http://purl.uniprot.org/annotation/VSP_026317|||http://purl.uniprot.org/annotation/VSP_045268|||http://purl.uniprot.org/annotation/VSP_045269
http://togogenome.org/gene/9606:ACSM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z530|||http://purl.uniprot.org/uniprot/F5GWL3|||http://purl.uniprot.org/uniprot/Q08AH3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  AMP-binding enzyme C-terminal|||AMP-dependent synthetase/ligase|||Acyl-coenzyme A synthetase ACSM2A, mitochondrial|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306093|||http://purl.uniprot.org/annotation/VAR_035247|||http://purl.uniprot.org/annotation/VAR_035248|||http://purl.uniprot.org/annotation/VAR_058692|||http://purl.uniprot.org/annotation/VAR_058694
http://togogenome.org/gene/9606:GAGE12E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L429                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 12B/C/D/E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311977
http://togogenome.org/gene/9606:OR2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVN9|||http://purl.uniprot.org/uniprot/Q9H210                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150467|||http://purl.uniprot.org/annotation/VAR_046723|||http://purl.uniprot.org/annotation/VAR_046724|||http://purl.uniprot.org/annotation/VAR_046725|||http://purl.uniprot.org/annotation/VAR_046726|||http://purl.uniprot.org/annotation/VAR_062017|||http://purl.uniprot.org/annotation/VAR_062018
http://togogenome.org/gene/9606:VPS53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS06|||http://purl.uniprot.org/uniprot/Q5VIR6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In PCH2E.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Vacuolar protein sorting-associated protein 53 homolog|||Vps53 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215189|||http://purl.uniprot.org/annotation/VAR_059959|||http://purl.uniprot.org/annotation/VAR_066561|||http://purl.uniprot.org/annotation/VAR_071803|||http://purl.uniprot.org/annotation/VSP_060662|||http://purl.uniprot.org/annotation/VSP_060663|||http://purl.uniprot.org/annotation/VSP_060664|||http://purl.uniprot.org/annotation/VSP_060665|||http://purl.uniprot.org/annotation/VSP_060787
http://togogenome.org/gene/9606:FAM110C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1W6H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Protein FAM110C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293461
http://togogenome.org/gene/9606:NRIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ35                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Nuclear receptor-interacting protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057953
http://togogenome.org/gene/9606:RCAN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKA8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calcineurin-binding|||Calcipressin-3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211420|||http://purl.uniprot.org/annotation/VAR_033727|||http://purl.uniprot.org/annotation/VSP_001319|||http://purl.uniprot.org/annotation/VSP_045968|||http://purl.uniprot.org/annotation/VSP_045969|||http://purl.uniprot.org/annotation/VSP_045970|||http://purl.uniprot.org/annotation/VSP_045971|||http://purl.uniprot.org/annotation/VSP_047510|||http://purl.uniprot.org/annotation/VSP_054855
http://togogenome.org/gene/9606:TOP3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K4N2|||http://purl.uniprot.org/uniprot/O95985                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||DNA topoisomerase 3-beta-1|||Disordered|||In isoform 2.|||In isoform 3.|||O-(5'-phospho-DNA)-tyrosine intermediate|||Toprim                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145192|||http://purl.uniprot.org/annotation/VAR_052591|||http://purl.uniprot.org/annotation/VSP_006525|||http://purl.uniprot.org/annotation/VSP_006526|||http://purl.uniprot.org/annotation/VSP_006527|||http://purl.uniprot.org/annotation/VSP_006528
http://togogenome.org/gene/9606:CLCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35523                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CBS 1|||CBS 2|||Changed chloride channel activity; changed gating of the channel.|||Changed gating of the channel.|||Chloride channel protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In MCAD and MCAR.|||In MCAD and MCAR; also found in myotonia levior; reduced chloride transport; changed calcium channel activity; changed channel gating; weak dominant negative effect.|||In MCAD and MCAR; changed ion selectivity; loss of chloride transport; mild dominant effect.|||In MCAD and MCAR; mild form; reduced chloride transport; changed chloride channel activity; changed gating of the channel; partial dominant negative effect.|||In MCAD.|||In MCAD; decreased protein abundance.|||In MCAD; loss of chloride transport; changed chloride channel activity; changed gating of the channel; dominant effect.|||In MCAD; reduced chloride transport; changed calcium channel activity; changed channel gating; no dominant negative effect.|||In MCAD; reduced chloride transport; changed calcium channel activity; changed gating of the channel.|||In MCAD; reduced chloride transport; changed calcium channel activity; changed gating of the channel; dominant negative effect.|||In MCAD; reduced chloride transport; changed chloride channel activity; changed gating of the channel.|||In MCAD; reduced chloride transport; changed chloride channel activity; changed gating of the channel; dominant negative effect.|||In MCAD; unknown pathological significance.|||In MCAR.|||In MCAR; altered chloride channel activity.|||In MCAR; changed chloride channel activity.|||In MCAR; decreased chloride channel activity.|||In MCAR; decreased chloride transport; decreased localization to the plasma membrane; dominant negative effect on chloride transport and localization to the plasma membrane; no significant effect on chloride channel activity; no effect on homodimerization.|||In MCAR; loss of calcium channel activity; no dominant negative effect.|||In MCAR; loss of chloride channel activity.|||In MCAR; loss of chloride channel activity; recessive.|||In MCAR; loss of chloride transport; changed calcium channel activity; changed gating of the channel.|||In MCAR; loss of chloride transport; decreased localization to the plasma membrane; loss of homodimerization; might be degraded.|||In MCAR; no effect on chloride transport.|||In MCAR; reduced calcium channel activity.|||In MCAR; reduced chloride transport; changed calcium channel activity; changed channel gating.|||In MCAR; reduced chloride transport; changed calcium channel activity; changed gating of the channel; no effect on protein abundance.|||In MCAR; reduced chloride transport; decreased localization to the plasma membrane; no significant effect on chloride channel activity.|||In MCAR; reduced chloride transport; no effect on protein abundance.|||In MCAR; unknown pathological significance.|||In MCAR; unknown pathological significance; no effect on calcium channel activity.|||In MCAR; unknown pathological significance; no effect on chloride channel activity.|||In MCAR; unknown pathological significance; no effect on chloride transport.|||In a breast cancer sample; somatic mutation.|||Loss of calcium channel activity.|||No effect on calcium channel activity.|||No effect on channel function.|||No effect on chloride transport.|||No effect on gating of the channel.|||Phosphoserine|||Polar residues|||Selectivity filter part_1|||Selectivity filter part_2|||Selectivity filter part_3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094429|||http://purl.uniprot.org/annotation/VAR_001582|||http://purl.uniprot.org/annotation/VAR_001583|||http://purl.uniprot.org/annotation/VAR_001584|||http://purl.uniprot.org/annotation/VAR_001585|||http://purl.uniprot.org/annotation/VAR_001586|||http://purl.uniprot.org/annotation/VAR_001587|||http://purl.uniprot.org/annotation/VAR_001588|||http://purl.uniprot.org/annotation/VAR_001589|||http://purl.uniprot.org/annotation/VAR_001590|||http://purl.uniprot.org/annotation/VAR_001591|||http://purl.uniprot.org/annotation/VAR_001592|||http://purl.uniprot.org/annotation/VAR_001593|||http://purl.uniprot.org/annotation/VAR_001594|||http://purl.uniprot.org/annotation/VAR_001595|||http://purl.uniprot.org/annotation/VAR_001596|||http://purl.uniprot.org/annotation/VAR_001597|||http://purl.uniprot.org/annotation/VAR_001598|||http://purl.uniprot.org/annotation/VAR_001599|||http://purl.uniprot.org/annotation/VAR_001600|||http://purl.uniprot.org/annotation/VAR_001601|||http://purl.uniprot.org/annotation/VAR_001602|||http://purl.uniprot.org/annotation/VAR_001603|||http://purl.uniprot.org/annotation/VAR_001604|||http://purl.uniprot.org/annotation/VAR_001605|||http://purl.uniprot.org/annotation/VAR_001606|||http://purl.uniprot.org/annotation/VAR_001607|||http://purl.uniprot.org/annotation/VAR_001608|||http://purl.uniprot.org/annotation/VAR_001609|||http://purl.uniprot.org/annotation/VAR_001610|||http://purl.uniprot.org/annotation/VAR_001611|||http://purl.uniprot.org/annotation/VAR_001612|||http://purl.uniprot.org/annotation/VAR_001613|||http://purl.uniprot.org/annotation/VAR_001614|||http://purl.uniprot.org/annotation/VAR_036300|||http://purl.uniprot.org/annotation/VAR_047779|||http://purl.uniprot.org/annotation/VAR_075588|||http://purl.uniprot.org/annotation/VAR_075589|||http://purl.uniprot.org/annotation/VAR_075590|||http://purl.uniprot.org/annotation/VAR_075591|||http://purl.uniprot.org/annotation/VAR_075592|||http://purl.uniprot.org/annotation/VAR_075593|||http://purl.uniprot.org/annotation/VAR_075594|||http://purl.uniprot.org/annotation/VAR_075595|||http://purl.uniprot.org/annotation/VAR_075596|||http://purl.uniprot.org/annotation/VAR_075597|||http://purl.uniprot.org/annotation/VAR_075598|||http://purl.uniprot.org/annotation/VAR_075599|||http://purl.uniprot.org/annotation/VAR_075600|||http://purl.uniprot.org/annotation/VAR_075601|||http://purl.uniprot.org/annotation/VAR_075602|||http://purl.uniprot.org/annotation/VAR_075603|||http://purl.uniprot.org/annotation/VAR_075604|||http://purl.uniprot.org/annotation/VAR_075605|||http://purl.uniprot.org/annotation/VAR_075606|||http://purl.uniprot.org/annotation/VAR_075607|||http://purl.uniprot.org/annotation/VAR_075608|||http://purl.uniprot.org/annotation/VAR_075609|||http://purl.uniprot.org/annotation/VAR_075610|||http://purl.uniprot.org/annotation/VAR_075611|||http://purl.uniprot.org/annotation/VAR_075612|||http://purl.uniprot.org/annotation/VAR_075613|||http://purl.uniprot.org/annotation/VAR_075614|||http://purl.uniprot.org/annotation/VAR_075615|||http://purl.uniprot.org/annotation/VAR_075616|||http://purl.uniprot.org/annotation/VAR_077244|||http://purl.uniprot.org/annotation/VAR_079520
http://togogenome.org/gene/9606:ATP1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3KLL5|||http://purl.uniprot.org/uniprot/P05026                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Sodium/potassium-transporting ATPase subunit beta-1|||immunoglobulin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219097|||http://purl.uniprot.org/annotation/VSP_000349
http://togogenome.org/gene/9606:CXCL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14625                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-X-C motif chemokine 11|||Citrulline; by PAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005106|||http://purl.uniprot.org/annotation/VAR_048700
http://togogenome.org/gene/9606:ARMH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BNL8                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Armadillo-like helical domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425554
http://togogenome.org/gene/9606:KDM6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15054                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes lysine-specific histone demethylase activity.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In NEDCFSA.|||In isoform 1.|||JmjC|||Lysine-specific demethylase 6B|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292007|||http://purl.uniprot.org/annotation/VAR_032927|||http://purl.uniprot.org/annotation/VAR_061670|||http://purl.uniprot.org/annotation/VAR_083120|||http://purl.uniprot.org/annotation/VAR_083121|||http://purl.uniprot.org/annotation/VAR_083122|||http://purl.uniprot.org/annotation/VAR_083123|||http://purl.uniprot.org/annotation/VAR_083124|||http://purl.uniprot.org/annotation/VSP_040102
http://togogenome.org/gene/9606:OGFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZT2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 20 AA approximate tandem repeats of [ST]-P-S-E-T-P-G-P-[SR]-P-A-G-P-[AT]-[GR]-D-E-P-A-[EK]|||Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||In isoform 2.|||N-acetylmethionine|||Opioid growth factor receptor|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058030|||http://purl.uniprot.org/annotation/VAR_030011|||http://purl.uniprot.org/annotation/VAR_059706|||http://purl.uniprot.org/annotation/VSP_004060
http://togogenome.org/gene/9606:MCM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14566                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Arginine finger|||DNA replication licensing factor MCM6|||Found in a patient with endocrine disorders, developmental regression, autism spectrum disorder and epilepsy; probable disease-associated variant.|||Found in a patient with intra-uterine growth restriction, developmental delay and autism spectrum disorder; probable disease-associated variant.|||Found in a patient with mild developmental delay and autism spectrum disorder; probable disease-associated variant.|||Found in two patients with microcephaly, developmental delay, typical facial characteristics, endocrine disorders, feeding difficulties and urogenital anomalies; probable disease-associated variant; impairs cell proliferation and ciliogenesis.|||Impairs interaction with CTD1.|||MCM|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194113|||http://purl.uniprot.org/annotation/VAR_014816|||http://purl.uniprot.org/annotation/VAR_016340|||http://purl.uniprot.org/annotation/VAR_088369|||http://purl.uniprot.org/annotation/VAR_088370|||http://purl.uniprot.org/annotation/VAR_088371|||http://purl.uniprot.org/annotation/VAR_088372
http://togogenome.org/gene/9606:MTMR14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCE2|||http://purl.uniprot.org/uniprot/Q8WYY9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Drastically reduced enzymatic activity.|||In CNM1; may act as a disease modifier; mutation found in a patient also carrying mutation Lys-368 in DNM2; reduced enzymatic activity.|||In CNM1; may act as a phenotype modifier; drastically reduced enzymatic activity.|||In isoform 2 and isoform 3.|||In isoform 3.|||Myotubularin-related protein 14|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260214|||http://purl.uniprot.org/annotation/VAR_033370|||http://purl.uniprot.org/annotation/VAR_033371|||http://purl.uniprot.org/annotation/VSP_021585|||http://purl.uniprot.org/annotation/VSP_021586
http://togogenome.org/gene/9606:HMGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09429                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Disulfide Bond|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  ADP-ribosylserine|||Abolishes cleavage by CASP1 and impairs ability to antagonize apoptosis-induced immune tolerance.|||Acidic residues|||Basic and acidic residues|||Binding to AGER/RAGE|||Cleavage; by CASP1|||Cleavage; by thrombin:thrombomodulin|||Cysteine sulfonic acid (-SO3H)|||Cysteine sulfonic acid (-SO3H); alternate|||Cytokine-stimulating activity|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-35; E-39; E-42; E-46 and E-181.|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-35; E-39; E-42; E-46 and E-53.|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-35; E-39; E-42; E-53 and E-181.|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-35; E-39; E-46; E-53 and E-181.|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-35; E-42; E-46; E-53 and E-181.|||Cytoplasmic localization (phosphorylation mimicking); when associated with E-39; E-42; E-46; E-53 and E-181.|||Disordered|||Greatly reduces phosphorylation, nuclear localization; when associated with A-35; A-39; A-42; A-46 and A-181.|||Greatly reduces phosphorylation, nuclear localization; when associated with A-35; A-39; A-42; A-46 and A-53.|||Greatly reduces phosphorylation, nuclear localization; when associated with A-35; A-39; A-42; A-53 and A-181.|||Greatly reduces phosphorylation, nuclear localization; when associated with A-35; A-39; A-46; A-53 and A-181.|||Greatly reduces phosphorylation, nuclear localization; when associated with A-35; A-42; A-46; A-53 and A-181.|||Greatly reduces phosphorylation, nuclear localization; when associated with A-39; A-42; A-46; A-53 and A-181.|||HMG box 1|||HMG box 2|||High mobility group protein B1|||In disulfide HMGB1; alternate|||In gastric-carcinoma cell line.|||Inhibits oxidation-dependent inactivation of immunostimmulatory activity in apoptotic cells.|||Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?)|||LPS binding (Lipid A)|||LPS binding (delipidated)|||N6-acetyllysine|||Nuclear localization signal (NLS) 1|||Nuclear localization signal (NLS) 2|||Phosphoserine|||Sufficient for interaction with HAVCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048526|||http://purl.uniprot.org/annotation/VAR_046451|||http://purl.uniprot.org/annotation/VAR_046452|||http://purl.uniprot.org/annotation/VAR_046453|||http://purl.uniprot.org/annotation/VAR_046454
http://togogenome.org/gene/9606:RTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQR2|||http://purl.uniprot.org/uniprot/B4DXL5|||http://purl.uniprot.org/uniprot/Q9BY42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Replication termination factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079427|||http://purl.uniprot.org/annotation/VAR_028134|||http://purl.uniprot.org/annotation/VAR_028135
http://togogenome.org/gene/9606:TTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG68                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  TTL|||Tubulin--tyrosine ligase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212434
http://togogenome.org/gene/9606:ART5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L15                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Ecto-ADP-ribosyltransferase 5|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TR mART core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019333|||http://purl.uniprot.org/annotation/VAR_063143|||http://purl.uniprot.org/annotation/VSP_013145|||http://purl.uniprot.org/annotation/VSP_013146
http://togogenome.org/gene/9606:SLC44A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWI5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Choline transporter-like protein 1|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191712|||http://purl.uniprot.org/annotation/VAR_048837|||http://purl.uniprot.org/annotation/VSP_015424|||http://purl.uniprot.org/annotation/VSP_015425|||http://purl.uniprot.org/annotation/VSP_015426|||http://purl.uniprot.org/annotation/VSP_015427
http://togogenome.org/gene/9606:SLC8A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPR5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Calx-beta 1|||Calx-beta 2|||Cytoplasmic|||Disordered|||Extracellular|||Found in a family with atypical autism and severe epilepsy; unknown pathological significance.|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Putative calmodulin-binding region|||Sodium/calcium exchanger 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019382|||http://purl.uniprot.org/annotation/VAR_050226|||http://purl.uniprot.org/annotation/VAR_072078
http://togogenome.org/gene/9606:CAPNS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L46                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Calpain small subunit 2|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073718
http://togogenome.org/gene/9606:F13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05160                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Coagulation factor XIII B chain|||In FA13BD.|||In FA13BD; impaired interaction with F13A1.|||In FA13BD; impaired interaction with F13A1; impaired structure.|||In FA13BD; may disrupt a disulfide bond; impaired interaction with F13A1; impaired structure.|||In FA13BD; may disrupt a disulfide bond; impaired subcellular location leading to accumulation in the endoplasmic reticulum; impaired interaction with F13A1; impaired structure.|||In FA13BD; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 10|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021222|||http://purl.uniprot.org/annotation/VAR_007475|||http://purl.uniprot.org/annotation/VAR_013930|||http://purl.uniprot.org/annotation/VAR_013931|||http://purl.uniprot.org/annotation/VAR_013932|||http://purl.uniprot.org/annotation/VAR_013933|||http://purl.uniprot.org/annotation/VAR_013934|||http://purl.uniprot.org/annotation/VAR_013935|||http://purl.uniprot.org/annotation/VAR_020612|||http://purl.uniprot.org/annotation/VAR_020613|||http://purl.uniprot.org/annotation/VAR_074563|||http://purl.uniprot.org/annotation/VAR_074564|||http://purl.uniprot.org/annotation/VAR_074565|||http://purl.uniprot.org/annotation/VAR_074566|||http://purl.uniprot.org/annotation/VAR_074567|||http://purl.uniprot.org/annotation/VAR_074568|||http://purl.uniprot.org/annotation/VAR_074569
http://togogenome.org/gene/9606:ERCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18074                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEAH box|||Decreased transcriptional activity of the reconstituted TFIIH complex.|||General transcription and DNA repair factor IIH helicase subunit XPD|||Helicase ATP-binding|||In TTD1 and XP-D.|||In TTD1.|||In TTD1; mild.|||In XP-D and COFS2.|||In XP-D and TTD1.|||In XP-D.|||In XP-D/CS; severe form.|||In XP-D; combined with features of Cockayne syndrome.|||In XP-D; mild.|||In XP-D; the corresponding mutation in fission yeast causes complete loss of activity.|||In XP-D; vitamin D-mediated activation of CYP24A1 is impaired in patient fibroblasts due to altered TFIIH-dependent phosphorylation of ETS1, subsequent impaired cooperation of ETS1 with VDR and altered VDR recruitment to CYP24A1 promoter.|||In isoform 2.|||May be associated with increased susceptibility to DNA damage.|||Mediates interaction with MMS19|||Nuclear localization signal|||Reduced iron-sulfur-binding. Iron-sulfur-binding is further decreased in absence of MMS19.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101980|||http://purl.uniprot.org/annotation/VAR_003622|||http://purl.uniprot.org/annotation/VAR_003623|||http://purl.uniprot.org/annotation/VAR_003624|||http://purl.uniprot.org/annotation/VAR_003625|||http://purl.uniprot.org/annotation/VAR_003626|||http://purl.uniprot.org/annotation/VAR_003627|||http://purl.uniprot.org/annotation/VAR_003628|||http://purl.uniprot.org/annotation/VAR_003629|||http://purl.uniprot.org/annotation/VAR_003630|||http://purl.uniprot.org/annotation/VAR_003631|||http://purl.uniprot.org/annotation/VAR_008187|||http://purl.uniprot.org/annotation/VAR_008188|||http://purl.uniprot.org/annotation/VAR_008189|||http://purl.uniprot.org/annotation/VAR_008190|||http://purl.uniprot.org/annotation/VAR_008191|||http://purl.uniprot.org/annotation/VAR_008192|||http://purl.uniprot.org/annotation/VAR_008193|||http://purl.uniprot.org/annotation/VAR_008194|||http://purl.uniprot.org/annotation/VAR_008195|||http://purl.uniprot.org/annotation/VAR_008196|||http://purl.uniprot.org/annotation/VAR_008197|||http://purl.uniprot.org/annotation/VAR_008198|||http://purl.uniprot.org/annotation/VAR_008199|||http://purl.uniprot.org/annotation/VAR_011412|||http://purl.uniprot.org/annotation/VAR_011413|||http://purl.uniprot.org/annotation/VAR_011414|||http://purl.uniprot.org/annotation/VAR_011415|||http://purl.uniprot.org/annotation/VAR_011416|||http://purl.uniprot.org/annotation/VAR_017282|||http://purl.uniprot.org/annotation/VAR_017283|||http://purl.uniprot.org/annotation/VAR_017284|||http://purl.uniprot.org/annotation/VAR_017285|||http://purl.uniprot.org/annotation/VAR_017286|||http://purl.uniprot.org/annotation/VAR_017287|||http://purl.uniprot.org/annotation/VAR_017288|||http://purl.uniprot.org/annotation/VAR_017289|||http://purl.uniprot.org/annotation/VAR_017290|||http://purl.uniprot.org/annotation/VAR_017291|||http://purl.uniprot.org/annotation/VAR_017292|||http://purl.uniprot.org/annotation/VAR_017293|||http://purl.uniprot.org/annotation/VSP_043132|||http://purl.uniprot.org/annotation/VSP_043133|||http://purl.uniprot.org/annotation/VSP_043134
http://togogenome.org/gene/9606:PIK3R6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRK9|||http://purl.uniprot.org/uniprot/Q5UE93                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Phosphoinositide 3-kinase regulatory subunit 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234338
http://togogenome.org/gene/9606:C8orf89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMQ9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative uncharacterized protein C8orf89                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431377
http://togogenome.org/gene/9606:GIPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48546                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gastric inhibitory polypeptide receptor|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012825|||http://purl.uniprot.org/annotation/VAR_011808|||http://purl.uniprot.org/annotation/VAR_011809|||http://purl.uniprot.org/annotation/VAR_011810|||http://purl.uniprot.org/annotation/VAR_029333|||http://purl.uniprot.org/annotation/VSP_053866|||http://purl.uniprot.org/annotation/VSP_053867|||http://purl.uniprot.org/annotation/VSP_053868
http://togogenome.org/gene/9606:PAQR7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WK9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Membrane progestin receptor alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218835|||http://purl.uniprot.org/annotation/VAR_048204|||http://purl.uniprot.org/annotation/VAR_060999
http://togogenome.org/gene/9606:REG3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06141|||http://purl.uniprot.org/uniprot/Q53S56                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-type lectin|||EPN|||No effect on binding to phospholipids and membrane toxicity.|||Reduces antibacterial activity but no effect on peptidoglycan binding.|||Reduces binding to phospholipids and membrane toxicity. Loss of filament formation.|||Reduces membrane toxicity.|||Reduces peptidoglycan binding and antibacterial activity. No effect on binding to phospholipids and membrane toxicity. No effect on filament formation.|||Regenerating islet-derived protein 3-alpha 15 kDa form|||Regenerating islet-derived protein 3-alpha 16.5 kDa form|||Sufficient to activate EXTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017429|||http://purl.uniprot.org/annotation/PRO_0000422741|||http://purl.uniprot.org/annotation/PRO_0000422742|||http://purl.uniprot.org/annotation/PRO_5014309513
http://togogenome.org/gene/9606:ATP8B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98198                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cytoplasmic|||Disordered|||Exoplasmic loop|||Helical|||Impairs ATPase activity.|||Impairs ATPase flippase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phospholipid-transporting ATPase ID|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046365|||http://purl.uniprot.org/annotation/VSP_007302|||http://purl.uniprot.org/annotation/VSP_007303|||http://purl.uniprot.org/annotation/VSP_037147|||http://purl.uniprot.org/annotation/VSP_037148|||http://purl.uniprot.org/annotation/VSP_037149|||http://purl.uniprot.org/annotation/VSP_037150
http://togogenome.org/gene/9606:MASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQY3|||http://purl.uniprot.org/uniprot/O00187                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||Abolishes autocatalytic cleavage.|||Associated with reduced MASP2 levels in plasma; no effect on catalytic activity.|||CUB|||CUB 1|||CUB 2|||Charge relay system|||Cleavage; by autolysis|||Decreases affinity for MBL2. Slight decrease in affinity for FCN2.|||EGF-like; calcium-binding|||In MASPD.|||In MASPD; found in a patient suffering from frequent infections and chronic inflammatory disease; strongly decreases affinity for MBL2 and FCN2.|||In isoform 2.|||Interchain (between A and B chains)|||Mannan-binding lectin serine protease 2|||Mannan-binding lectin serine protease 2 A chain|||Mannan-binding lectin serine protease 2 B chain|||Peptidase S1|||Strongly decreases affinity for MBL2, but not for FCN2.|||Strongly decreases affinity for MBL2. Decreases affinity for FCN2.|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027598|||http://purl.uniprot.org/annotation/PRO_0000027599|||http://purl.uniprot.org/annotation/PRO_0000027600|||http://purl.uniprot.org/annotation/PRO_5036474354|||http://purl.uniprot.org/annotation/VAR_025344|||http://purl.uniprot.org/annotation/VAR_025345|||http://purl.uniprot.org/annotation/VAR_025346|||http://purl.uniprot.org/annotation/VAR_025347|||http://purl.uniprot.org/annotation/VAR_028784|||http://purl.uniprot.org/annotation/VAR_028785|||http://purl.uniprot.org/annotation/VAR_028786|||http://purl.uniprot.org/annotation/VAR_028787|||http://purl.uniprot.org/annotation/VAR_065814|||http://purl.uniprot.org/annotation/VAR_075087|||http://purl.uniprot.org/annotation/VAR_075088|||http://purl.uniprot.org/annotation/VSP_005383|||http://purl.uniprot.org/annotation/VSP_005384
http://togogenome.org/gene/9606:PRPSAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60256                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoribosyl pyrophosphate synthase-associated protein 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141082|||http://purl.uniprot.org/annotation/VSP_044731|||http://purl.uniprot.org/annotation/VSP_046462|||http://purl.uniprot.org/annotation/VSP_054765
http://togogenome.org/gene/9606:PSMD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z489|||http://purl.uniprot.org/uniprot/O00232                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 12|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||PCI|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173861|||http://purl.uniprot.org/annotation/VAR_051558|||http://purl.uniprot.org/annotation/VSP_042718
http://togogenome.org/gene/9606:CLTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J8P9|||http://purl.uniprot.org/uniprot/P09496                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Clathrin light chain A|||Disordered|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform Non-brain and isoform 5.|||Involved in binding clathrin heavy chain|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205767|||http://purl.uniprot.org/annotation/VSP_001095|||http://purl.uniprot.org/annotation/VSP_024238|||http://purl.uniprot.org/annotation/VSP_043239|||http://purl.uniprot.org/annotation/VSP_047168
http://togogenome.org/gene/9606:DNAAF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9W5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein axonemal assembly factor 3|||In CILD2.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297580|||http://purl.uniprot.org/annotation/VAR_055306|||http://purl.uniprot.org/annotation/VAR_055307|||http://purl.uniprot.org/annotation/VAR_055308|||http://purl.uniprot.org/annotation/VAR_067300|||http://purl.uniprot.org/annotation/VAR_067301|||http://purl.uniprot.org/annotation/VSP_039966|||http://purl.uniprot.org/annotation/VSP_039967|||http://purl.uniprot.org/annotation/VSP_039968|||http://purl.uniprot.org/annotation/VSP_039969|||http://purl.uniprot.org/annotation/VSP_042976|||http://purl.uniprot.org/annotation/VSP_055742
http://togogenome.org/gene/9606:ZBTB34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFQ2|||http://purl.uniprot.org/uniprot/Q8NCN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047740
http://togogenome.org/gene/9606:GRIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0E4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glutamate receptor-interacting protein 2|||In isoform 2.|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||PDZ 7|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083852|||http://purl.uniprot.org/annotation/VSP_009757|||http://purl.uniprot.org/annotation/VSP_009758
http://togogenome.org/gene/9606:KLHDC8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXV7|||http://purl.uniprot.org/uniprot/Q96DZ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Repeat                                                                                  ^@                                                                                  Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch 7|||Kelch 8|||Kelch domain-containing protein 8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119131
http://togogenome.org/gene/9606:HTATSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43719                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HIV Tat-specific factor 1|||Loss of interaction with U snRNPs.|||Mediates interaction with the P-TEFb complex|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||RRM 1|||RRM 2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248604|||http://purl.uniprot.org/annotation/VAR_027362|||http://purl.uniprot.org/annotation/VAR_052206|||http://purl.uniprot.org/annotation/VAR_052207
http://togogenome.org/gene/9606:KDM4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75164                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to H3K4me3.|||Abolishes histone demethylase activity without affecting ability to bind H4K20me2.|||Abolishes histone demethylase activity.|||Abolishes histone demethylase activity; when associated with A-138.|||Abolishes histone demethylase activity; when associated with A-165.|||C2HC pre-PHD-type|||Disordered|||Displays histone demethylase activity for both dimethylated and H3-K9Me3.|||Histone H3K4me3 binding|||Impairs binding to H3K4me3.|||Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1.|||In isoform 2.|||Interaction with NCOR1|||JmjC|||JmjN|||Lysine-specific demethylase 4A|||N-acetylalanine|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Polar residues|||Removed|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183172|||http://purl.uniprot.org/annotation/VAR_023775|||http://purl.uniprot.org/annotation/VAR_031217|||http://purl.uniprot.org/annotation/VSP_044239
http://togogenome.org/gene/9606:OR4D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWK0|||http://purl.uniprot.org/uniprot/P58180                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150538|||http://purl.uniprot.org/annotation/VAR_062035
http://togogenome.org/gene/9606:KRTAP4-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYQ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||18 X 5 AA repeats of C-C-[GRQC]-[SPT]-[VSTL]|||2|||3|||4|||5|||6|||7|||8|||9|||In allele KAP4.10.|||Keratin-associated protein 4-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185177|||http://purl.uniprot.org/annotation/VAR_047044|||http://purl.uniprot.org/annotation/VAR_047045|||http://purl.uniprot.org/annotation/VAR_047046|||http://purl.uniprot.org/annotation/VAR_064550
http://togogenome.org/gene/9606:PITHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKP7|||http://purl.uniprot.org/uniprot/Q9GZP4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PITH|||PITH domain-containing protein 1|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285032|||http://purl.uniprot.org/annotation/VSP_024807
http://togogenome.org/gene/9606:CSTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01040                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Cystatin-A|||Cystatin-A, N-terminally processed|||N-acetylmethionine|||Reactive site|||Removed; alternate|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207128|||http://purl.uniprot.org/annotation/PRO_0000423202|||http://purl.uniprot.org/annotation/VAR_048851
http://togogenome.org/gene/9606:UBL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7B0|||http://purl.uniprot.org/uniprot/Q9BZL1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Does not impair binding to SART1 nor its pre-mRNA splicing function.|||Ubiquitin-like|||Ubiquitin-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114866
http://togogenome.org/gene/9606:ARHGAP28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXL2                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  Helical|||Rho-GAP                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:IPO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNG9|||http://purl.uniprot.org/uniprot/O95373                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Importin N-terminal|||Importin-7|||Lowered affinity for RanGTP-binding.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120750|||http://purl.uniprot.org/annotation/VAR_050003
http://togogenome.org/gene/9606:SHISAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SXP7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Pro residues|||Protein shisa-like-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318951
http://togogenome.org/gene/9606:MCUR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPW7|||http://purl.uniprot.org/uniprot/Q96AQ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial calcium uniporter regulator 1|||Mitochondrial intermembrane|||Mitochondrial matrix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295692|||http://purl.uniprot.org/annotation/VAR_033320|||http://purl.uniprot.org/annotation/VAR_033321|||http://purl.uniprot.org/annotation/VSP_026998|||http://purl.uniprot.org/annotation/VSP_026999
http://togogenome.org/gene/9606:TAF1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Bromo 1|||Bromo 2|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung small cell carcinoma sample; somatic mutation.|||Nuclear localization signal|||Polar residues|||Transcription initiation factor TFIID subunit 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211217|||http://purl.uniprot.org/annotation/VAR_041934|||http://purl.uniprot.org/annotation/VAR_041935|||http://purl.uniprot.org/annotation/VAR_041936|||http://purl.uniprot.org/annotation/VAR_041937|||http://purl.uniprot.org/annotation/VAR_041938|||http://purl.uniprot.org/annotation/VAR_041939|||http://purl.uniprot.org/annotation/VAR_041940|||http://purl.uniprot.org/annotation/VAR_041941|||http://purl.uniprot.org/annotation/VAR_041942|||http://purl.uniprot.org/annotation/VAR_041943|||http://purl.uniprot.org/annotation/VAR_041944|||http://purl.uniprot.org/annotation/VAR_041945|||http://purl.uniprot.org/annotation/VAR_041946|||http://purl.uniprot.org/annotation/VAR_041947|||http://purl.uniprot.org/annotation/VAR_041948|||http://purl.uniprot.org/annotation/VAR_041949|||http://purl.uniprot.org/annotation/VAR_041950|||http://purl.uniprot.org/annotation/VAR_041951|||http://purl.uniprot.org/annotation/VAR_041952|||http://purl.uniprot.org/annotation/VAR_041953|||http://purl.uniprot.org/annotation/VAR_041954|||http://purl.uniprot.org/annotation/VAR_041955|||http://purl.uniprot.org/annotation/VAR_048435
http://togogenome.org/gene/9606:GPR42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0PUY3|||http://purl.uniprot.org/uniprot/O15529                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor 42|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of response to propionate.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069570|||http://purl.uniprot.org/annotation/VAR_033468|||http://purl.uniprot.org/annotation/VAR_033469|||http://purl.uniprot.org/annotation/VAR_033470|||http://purl.uniprot.org/annotation/VAR_062860|||http://purl.uniprot.org/annotation/VAR_062862|||http://purl.uniprot.org/annotation/VAR_088067
http://togogenome.org/gene/9606:CCNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWL7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  D-box|||Disordered|||G2/mitotic-specific cyclin-B3|||In a colorectal cancer sample; somatic mutation.|||In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-63.|||In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-68.|||In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-63 and A-68.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080373|||http://purl.uniprot.org/annotation/VAR_036580|||http://purl.uniprot.org/annotation/VAR_047027|||http://purl.uniprot.org/annotation/VSP_010514|||http://purl.uniprot.org/annotation/VSP_010515
http://togogenome.org/gene/9606:SLC19A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8Y5|||http://purl.uniprot.org/uniprot/A0A024R928|||http://purl.uniprot.org/uniprot/O60779                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Essential for pyridoxine transport|||Extracellular|||Helical|||In TRMA.|||In isoform 2.|||Loss of pyridoxine transport; when associated with H-104; A-109; S-111; Y-112; P-186 and F-191.|||Loss of pyridoxine transport; when associated with H-104; V-105; A-109; S-111; P-186 and F-191.|||Loss of pyridoxine transport; when associated with H-104; V-105; A-109; S-111; Y-112 and F-191.|||Loss of pyridoxine transport; when associated with H-104; V-105; A-109; S-111; Y-112 and P-186.|||Loss of pyridoxine transport; when associated with H-104; V-105; A-109; Y-112; P-186 and F-191.|||Loss of pyridoxine transport; when associated with H-104; V-105; S-111; Y-112; P-186 and F-191.|||Loss of pyridoxine transport; when associated with V-105; A-109; S-111; Y-112; P-186 and F-191.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Thiamine transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178663|||http://purl.uniprot.org/annotation/VAR_010248|||http://purl.uniprot.org/annotation/VAR_010249|||http://purl.uniprot.org/annotation/VAR_010250|||http://purl.uniprot.org/annotation/VSP_036467
http://togogenome.org/gene/9606:CDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32320                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||Cytidine deaminase|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171682|||http://purl.uniprot.org/annotation/VAR_021559
http://togogenome.org/gene/9606:AP1S3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PC3                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP-1 complex subunit sigma-3|||In PSORS15; results in decreased TLR3 targeting to the endosomes indicating impaired function.|||In PSORS15; results in decreased protein levels.|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193801|||http://purl.uniprot.org/annotation/VAR_072545|||http://purl.uniprot.org/annotation/VAR_072546|||http://purl.uniprot.org/annotation/VAR_072547|||http://purl.uniprot.org/annotation/VAR_072548|||http://purl.uniprot.org/annotation/VAR_072549|||http://purl.uniprot.org/annotation/VAR_072550|||http://purl.uniprot.org/annotation/VAR_072551|||http://purl.uniprot.org/annotation/VAR_072552|||http://purl.uniprot.org/annotation/VSP_015942|||http://purl.uniprot.org/annotation/VSP_015943|||http://purl.uniprot.org/annotation/VSP_015944|||http://purl.uniprot.org/annotation/VSP_040384
http://togogenome.org/gene/9606:VIM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08670|||http://purl.uniprot.org/uniprot/V9HWE1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In CTRCT30; the mutation increases the proteasome activity in transfected cells; causes also a severe kinetic defect in vimentin assembly both in vitro and in vivo.|||In CTRCT30; unknown pathological significance.|||Linker 1|||Linker 12|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphoserine; by AURKB and ROCK2|||Phosphoserine; by CDK5 and CDK1|||Phosphoserine; by CaMK2, PKA, PKC and ROCK2|||Phosphoserine; by PKA and PKC; alternate|||Phosphoserine; by PKC|||Phosphoserine; by PKC; alternate|||Phosphothreonine|||Phosphotyrosine|||Removed|||Stutter|||Tail|||Vimentin|||[IL]-x-C-x-x-[DE] motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063754|||http://purl.uniprot.org/annotation/VAR_070100|||http://purl.uniprot.org/annotation/VAR_078860
http://togogenome.org/gene/9606:FSBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95073                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Fibrinogen silencer-binding protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087352|||http://purl.uniprot.org/annotation/VAR_019301|||http://purl.uniprot.org/annotation/VSP_010774
http://togogenome.org/gene/9606:PRRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-carboxyglutamate|||Cytoplasmic|||Disordered|||Extracellular|||Gla|||Helical|||Polar residues|||Transmembrane gamma-carboxyglutamic acid protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022547|||http://purl.uniprot.org/annotation/PRO_0000022548|||http://purl.uniprot.org/annotation/VAR_046712
http://togogenome.org/gene/9606:NAA60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYU5|||http://purl.uniprot.org/uniprot/Q9H7X0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Turn                                                                                  ^@                                                                                  Abolished acetyltransferase activity.|||Abolishes acetyltransferase activity.|||Cytoplasmic|||Decreased acetyltransferase activity.|||Decreased acetyltransferase activity; when associated with R-105, R-109, R-121 and R-156.|||Decreased acetyltransferase activity; when associated with R-79, R-105, R-109 and R-156.|||Decreased acetyltransferase activity; when associated with R-79, R-105, R-121 and R-156.|||Decreased acetyltransferase activity; when associated with R-79, R-109, R-121 and R-156.|||Decreased histone acetyltransferase activity; when associated with R-79, R-105, R-109 and R-121.|||Does not affect localization to the Golgi apparatus.|||Does not affect localization to the Golgi apparatus; when associated with S-19; S-132; S-207 and S-222.|||Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-207.|||Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-132 and S-222.|||Does not affect localization to the Golgi apparatus; when associated with S-19; S-30; S-207 and S-222.|||Does not affect localization to the Golgi apparatus; when associated with S-30; S-132; S-207 and S-222.|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increased acetyltransferase activity.|||N-acetyltransferase|||N-alpha-acetyltransferase 60|||N6-acetyllysine; by autocatalysis|||Only slightly affects acetyltransferase activity.|||Reduced acetyltransferase activity.|||Required for homodimerization|||Required to position thioacetyl group|||Slightly altered acetyltransferase activity.|||Slightly increased acetyltransferase activity.|||Slightly reduced acetyltransferase activity.|||Strongly reduced acetyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321566|||http://purl.uniprot.org/annotation/VAR_060995|||http://purl.uniprot.org/annotation/VSP_044122|||http://purl.uniprot.org/annotation/VSP_044123|||http://purl.uniprot.org/annotation/VSP_044124|||http://purl.uniprot.org/annotation/VSP_044125
http://togogenome.org/gene/9606:HEXB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RAJ6|||http://purl.uniprot.org/uniprot/P07686|||http://purl.uniprot.org/uniprot/Q5URX0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  1.5-fold increase in substrate affinity. 2300-fold reduction in catalytic efficiency. Reduces optimal pH to 3-3.5.|||2.7-fold reduction in substrate affinity. 39-fold reduction in catalytic efficiency.|||Beta-hexosaminidase eukaryotic type N-terminal|||Beta-hexosaminidase subunit beta|||Beta-hexosaminidase subunit beta chain A|||Beta-hexosaminidase subunit beta chain B|||Does not affect the native conformation of the isozyme A. Does not affect hydrolysis of GM2 ganglioside by the isozyme A.|||Glycoside hydrolase family 20 catalytic|||In GM2G2.|||In GM2G2; adult type; severe.|||In GM2G2; decreases the isozyme A transport out of the endoplasmic reticulum. Lowers its heat stability. Affects the ability of isozyme A to hydrolyze GM2 ganglioside.|||In GM2G2; infantile type.|||N-linked (GlcNAc...) asparagine|||No effect on substrate affinity and on catalytic efficiency.|||No effect on substrate affinity. 1750-fold reduction in catalytic efficiency.|||Not glycosylated|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012002|||http://purl.uniprot.org/annotation/PRO_0000012003|||http://purl.uniprot.org/annotation/PRO_0000012004|||http://purl.uniprot.org/annotation/PRO_0000012005|||http://purl.uniprot.org/annotation/VAR_003247|||http://purl.uniprot.org/annotation/VAR_003248|||http://purl.uniprot.org/annotation/VAR_003249|||http://purl.uniprot.org/annotation/VAR_003250|||http://purl.uniprot.org/annotation/VAR_003251|||http://purl.uniprot.org/annotation/VAR_003252|||http://purl.uniprot.org/annotation/VAR_003253|||http://purl.uniprot.org/annotation/VAR_003254|||http://purl.uniprot.org/annotation/VAR_011704|||http://purl.uniprot.org/annotation/VAR_011705|||http://purl.uniprot.org/annotation/VAR_011706
http://togogenome.org/gene/9606:ZEB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60315                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5; atypical|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox; atypical|||In MOWS.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SMAD-MH2 binding domain|||Zinc finger E-box-binding homeobox 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047236|||http://purl.uniprot.org/annotation/VAR_027016|||http://purl.uniprot.org/annotation/VAR_027017|||http://purl.uniprot.org/annotation/VAR_027018|||http://purl.uniprot.org/annotation/VAR_035563|||http://purl.uniprot.org/annotation/VSP_044797
http://togogenome.org/gene/9606:OSTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61366                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Peptide|||Signal Peptide                                                                                  ^@                                                                                  Arginine amide|||Osteocrin|||Processed Osteocrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021966|||http://purl.uniprot.org/annotation/PRO_0000439029
http://togogenome.org/gene/9606:CT45A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMV1|||http://purl.uniprot.org/uniprot/P0DMV2|||http://purl.uniprot.org/uniprot/Q5DJT8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  Cancer/testis antigen family 45 member A2|||Cancer/testis antigen family 45 member A8|||Cancer/testis antigen family 45 member A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308947|||http://purl.uniprot.org/annotation/PRO_0000433030|||http://purl.uniprot.org/annotation/PRO_0000433031
http://togogenome.org/gene/9606:RITA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes nuclear localization.|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with RBPJ/RBPSUH|||Interaction with tubulin|||Nuclear export signal|||Nuclear localization signal|||Polar residues|||RBPJ-interacting and tubulin-associated protein 1|||Results in nuclear accumulation; when associated with A-12 and A-15.|||Results in nuclear accumulation; when associated with A-7 and A-12.|||Results in nuclear accumulation; when associated with A-7 and A-15.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294429|||http://purl.uniprot.org/annotation/VAR_033175|||http://purl.uniprot.org/annotation/VAR_050865|||http://purl.uniprot.org/annotation/VSP_026636|||http://purl.uniprot.org/annotation/VSP_026637|||http://purl.uniprot.org/annotation/VSP_055649
http://togogenome.org/gene/9606:OPRPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99935                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mass|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) asparagine|||Opiorphin|||Opiorphin prepropeptide|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022111|||http://purl.uniprot.org/annotation/PRO_0000271169
http://togogenome.org/gene/9606:ENOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RDT8|||http://purl.uniprot.org/uniprot/Q8TC92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ecto-NOX disulfide-thiol exchanger 1|||In isoform 2.|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295900|||http://purl.uniprot.org/annotation/VAR_052205|||http://purl.uniprot.org/annotation/VSP_056985|||http://purl.uniprot.org/annotation/VSP_056986|||http://purl.uniprot.org/annotation/VSP_056987
http://togogenome.org/gene/9606:ZNF652                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9F2|||http://purl.uniprot.org/uniprot/Q9Y2D9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||Mediates interaction with CBFA2T3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 652                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280428
http://togogenome.org/gene/9606:CAST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6N0|||http://purl.uniprot.org/uniprot/E9PCH5|||http://purl.uniprot.org/uniprot/E9PDE4|||http://purl.uniprot.org/uniprot/P20810|||http://purl.uniprot.org/uniprot/Q59HE3|||http://purl.uniprot.org/uniprot/Q86YM9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calpastatin|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 4 and isoform 8.|||In isoform 5 and isoform 10.|||In isoform 6 and isoform 7.|||In isoform 9.|||Inhibitory domain 1|||Inhibitory domain 2|||Inhibitory domain 3|||Inhibitory domain 4|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147632|||http://purl.uniprot.org/annotation/VAR_005298|||http://purl.uniprot.org/annotation/VAR_022686|||http://purl.uniprot.org/annotation/VAR_030741|||http://purl.uniprot.org/annotation/VAR_030742|||http://purl.uniprot.org/annotation/VSP_000741|||http://purl.uniprot.org/annotation/VSP_000742|||http://purl.uniprot.org/annotation/VSP_000743|||http://purl.uniprot.org/annotation/VSP_000744|||http://purl.uniprot.org/annotation/VSP_038037|||http://purl.uniprot.org/annotation/VSP_038038|||http://purl.uniprot.org/annotation/VSP_047393
http://togogenome.org/gene/9606:TAF7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H9L4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Found in an oligozoospermic man; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||Polar residues|||Transcription initiation factor TFIID subunit 7-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307861|||http://purl.uniprot.org/annotation/VAR_036695|||http://purl.uniprot.org/annotation/VAR_036696|||http://purl.uniprot.org/annotation/VAR_036697|||http://purl.uniprot.org/annotation/VAR_036698|||http://purl.uniprot.org/annotation/VAR_036699|||http://purl.uniprot.org/annotation/VAR_086590|||http://purl.uniprot.org/annotation/VSP_028847|||http://purl.uniprot.org/annotation/VSP_028848
http://togogenome.org/gene/9606:H2AB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C5Z0                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Docking domain|||Histone H2A-Bbd type 2/3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055321
http://togogenome.org/gene/9606:DCAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDD6|||http://purl.uniprot.org/uniprot/B4DN30|||http://purl.uniprot.org/uniprot/Q8WV16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DDB1- and CUL4-associated factor 4|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||WD|||WD 1|||WD 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051368|||http://purl.uniprot.org/annotation/VAR_027908|||http://purl.uniprot.org/annotation/VAR_027909|||http://purl.uniprot.org/annotation/VAR_027910|||http://purl.uniprot.org/annotation/VAR_027911|||http://purl.uniprot.org/annotation/VAR_027912|||http://purl.uniprot.org/annotation/VAR_027913|||http://purl.uniprot.org/annotation/VSP_020986|||http://purl.uniprot.org/annotation/VSP_020987|||http://purl.uniprot.org/annotation/VSP_045427|||http://purl.uniprot.org/annotation/VSP_047171|||http://purl.uniprot.org/annotation/VSP_047172|||http://purl.uniprot.org/annotation/VSP_047173
http://togogenome.org/gene/9606:OR13C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVC9|||http://purl.uniprot.org/uniprot/Q8NGS5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13C4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150733
http://togogenome.org/gene/9606:KMT5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQB9|||http://purl.uniprot.org/uniprot/B7WNX0|||http://purl.uniprot.org/uniprot/B7Z5N2|||http://purl.uniprot.org/uniprot/C9J6S5|||http://purl.uniprot.org/uniprot/Q4FZB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes histone methyltransferase activity (H4-K20 specific).|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase KMT5B|||In MRD51.|||In MRD51; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Km for H4K20me1rise to 17 uM. 8-fold decrease in catalytic efficiency.|||Km for H4K20me1rise to 8.5 uM. 3-fold decrease in catalytic efficiency.|||Polar residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281787|||http://purl.uniprot.org/annotation/VAR_047765|||http://purl.uniprot.org/annotation/VAR_080549|||http://purl.uniprot.org/annotation/VAR_080550|||http://purl.uniprot.org/annotation/VAR_080551|||http://purl.uniprot.org/annotation/VAR_081278|||http://purl.uniprot.org/annotation/VSP_024051|||http://purl.uniprot.org/annotation/VSP_024052|||http://purl.uniprot.org/annotation/VSP_040034|||http://purl.uniprot.org/annotation/VSP_040035
http://togogenome.org/gene/9606:NKAIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMZ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000412169|||http://purl.uniprot.org/annotation/VSP_056113|||http://purl.uniprot.org/annotation/VSP_056114
http://togogenome.org/gene/9606:NAV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEY1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 6 and isoform 7.|||In isoform 3, isoform 4, isoform 5 and isoform 7.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||Neuron navigator 1|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286974|||http://purl.uniprot.org/annotation/VAR_032245|||http://purl.uniprot.org/annotation/VAR_032246|||http://purl.uniprot.org/annotation/VAR_032247|||http://purl.uniprot.org/annotation/VAR_032248|||http://purl.uniprot.org/annotation/VSP_025253|||http://purl.uniprot.org/annotation/VSP_025254|||http://purl.uniprot.org/annotation/VSP_025255|||http://purl.uniprot.org/annotation/VSP_025256|||http://purl.uniprot.org/annotation/VSP_025257|||http://purl.uniprot.org/annotation/VSP_025258|||http://purl.uniprot.org/annotation/VSP_025259
http://togogenome.org/gene/9606:LTV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GA3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In IPHAK; unknown pathological significance; due to a nucleotide substitution that creates a novel donor splice site resulting in aberrant splicing; small amounts of canonically spliced transcripts with the missense variant are also produced; decreased protein abundance in patient cells.|||Phosphoserine|||Protein LTV1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302813|||http://purl.uniprot.org/annotation/VAR_088086
http://togogenome.org/gene/9606:ARID3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99856                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ARID|||AT-rich interactive domain-containing protein 3A|||Abolishes DNA-binding.|||Abolishes nuclear targeting.|||Acidic|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homodimerization|||Impairs DNA-binding but not self-association.|||Impairs DNA-binding.|||Important for cytoplasmic localization|||Important for nuclear localization|||No effect on DNA-binding.|||Phosphoserine|||Phosphothreonine|||Polar residues|||REKLES                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200578|||http://purl.uniprot.org/annotation/VAR_033203|||http://purl.uniprot.org/annotation/VAR_033204|||http://purl.uniprot.org/annotation/VAR_033205
http://togogenome.org/gene/9606:SLC29A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14542|||http://purl.uniprot.org/uniprot/Q96FB2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Decreased inosine and guanosine transport; no change in uridine and hypoxanthine transport.|||Decreased nucleoside and nucleobase transport.|||Equilibrative nucleoside transporter 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||No change in nucleoside and nucleobase transport.|||No difference in uridine or cytidine uptake. No differences in Km values and lower Vmax values for either uridine or cytidine uptake; when associated with D-48.|||No difference in uridine or cytidine uptake. No differences in Km values and lower Vmax values for either uridine or cytidine uptake; when associated with D-57.|||Phosphoserine|||Reduces drastically localization at the cell surface and induces an significant reduction of adenosine or thymidine uptake; when associated with R-455.|||Reduces drastically localization at the cell surface. No effect on uptake of adenosine and thymidine. Reduces drastically localization at the cell surface and induces an significant reduction of adenosine or thymidine uptake; when associated with R-456.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209340|||http://purl.uniprot.org/annotation/VAR_029289|||http://purl.uniprot.org/annotation/VAR_029290|||http://purl.uniprot.org/annotation/VAR_029291|||http://purl.uniprot.org/annotation/VAR_036822|||http://purl.uniprot.org/annotation/VSP_040728|||http://purl.uniprot.org/annotation/VSP_040729|||http://purl.uniprot.org/annotation/VSP_040730|||http://purl.uniprot.org/annotation/VSP_040731|||http://purl.uniprot.org/annotation/VSP_061920
http://togogenome.org/gene/9606:PGAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9E5|||http://purl.uniprot.org/uniprot/P18669|||http://purl.uniprot.org/uniprot/Q6FHU2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Site|||Strand|||Turn                                                                                  ^@                                                                                  N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoglycerate mutase 1|||Phosphoserine|||Phosphotyrosine|||Proton donor/acceptor|||Removed|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179825
http://togogenome.org/gene/9606:MAP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ40|||http://purl.uniprot.org/uniprot/B7Z3E1|||http://purl.uniprot.org/uniprot/B7Z3Y3|||http://purl.uniprot.org/uniprot/B7ZB64|||http://purl.uniprot.org/uniprot/Q14244                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ensconsin|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255949|||http://purl.uniprot.org/annotation/VAR_028880|||http://purl.uniprot.org/annotation/VAR_034091|||http://purl.uniprot.org/annotation/VAR_034092|||http://purl.uniprot.org/annotation/VSP_021316|||http://purl.uniprot.org/annotation/VSP_021317|||http://purl.uniprot.org/annotation/VSP_043335|||http://purl.uniprot.org/annotation/VSP_043336|||http://purl.uniprot.org/annotation/VSP_046758
http://togogenome.org/gene/9606:BDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8Y1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1; approximate|||2|||3|||4|||5|||6|||7|||8; approximate|||9 X 55 AA repeats of G-R-R-X-I-S-P-X-E-N-G-X-E-E-V-K-P-X-X-E-M-E-T-D-L-K-X-T-G-R-E-X-X-X-R-E-K-T-X-E-X-X-D-A-X-E-E-I-D-X-D-L-E-E-T|||9; approximate|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Interaction with ZBTB43|||Myb-like|||Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-431 and A-437. CK2 treatment constitutively activates for U6 transcription; when associated with A-390; A-426; A-431 and A-437.|||Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-431 and A-446. CK2 treatment constitutively activates for U6 transcription; when associated with A-390; A-426; A-431 and A-446.|||Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-437 and A-446. CK2 treatment constitutively activates for U6 transcription; when associated with A-390; A-426; A-437 and A-446.|||Not phosphorylated by CSNK2A1; when associated with A-390; A-431; A-437 and A-446. CK2 treatment constitutively activates for U6 transcription; when associated with A-390; A-431; A-437 and A-446.|||Not phosphorylated by CSNK2A1; when associated with A-426; A-431; A-437 and A-446. CK2 treatment constitutively activates for U6 transcription; when associated with A-426; A-431; A-437 and A-446.|||Phosphothreonine|||Polar residues|||Required for phosphorylation by CSNK2A1|||Transcription factor TFIIIB component B"" homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333863|||http://purl.uniprot.org/annotation/VAR_043312|||http://purl.uniprot.org/annotation/VAR_043313|||http://purl.uniprot.org/annotation/VAR_043314|||http://purl.uniprot.org/annotation/VAR_043315|||http://purl.uniprot.org/annotation/VAR_043316|||http://purl.uniprot.org/annotation/VAR_043317|||http://purl.uniprot.org/annotation/VAR_043318|||http://purl.uniprot.org/annotation/VAR_056743|||http://purl.uniprot.org/annotation/VAR_056744|||http://purl.uniprot.org/annotation/VAR_056745|||http://purl.uniprot.org/annotation/VAR_056746|||http://purl.uniprot.org/annotation/VAR_056747|||http://purl.uniprot.org/annotation/VAR_056748|||http://purl.uniprot.org/annotation/VAR_056749|||http://purl.uniprot.org/annotation/VSP_033567|||http://purl.uniprot.org/annotation/VSP_033568|||http://purl.uniprot.org/annotation/VSP_033569|||http://purl.uniprot.org/annotation/VSP_033570|||http://purl.uniprot.org/annotation/VSP_033571|||http://purl.uniprot.org/annotation/VSP_033572|||http://purl.uniprot.org/annotation/VSP_033573|||http://purl.uniprot.org/annotation/VSP_033574|||http://purl.uniprot.org/annotation/VSP_033575|||http://purl.uniprot.org/annotation/VSP_033576|||http://purl.uniprot.org/annotation/VSP_033577|||http://purl.uniprot.org/annotation/VSP_033578|||http://purl.uniprot.org/annotation/VSP_033579|||http://purl.uniprot.org/annotation/VSP_033580|||http://purl.uniprot.org/annotation/VSP_033581|||http://purl.uniprot.org/annotation/VSP_033582
http://togogenome.org/gene/9606:SDK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5N4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Pro residues|||Protein sidekick-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226975|||http://purl.uniprot.org/annotation/VAR_025529|||http://purl.uniprot.org/annotation/VAR_025530|||http://purl.uniprot.org/annotation/VSP_017517|||http://purl.uniprot.org/annotation/VSP_017518|||http://purl.uniprot.org/annotation/VSP_017519
http://togogenome.org/gene/9606:C1RL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GWF3|||http://purl.uniprot.org/uniprot/F5H7C8|||http://purl.uniprot.org/uniprot/Q6P672|||http://purl.uniprot.org/uniprot/Q9NZP8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  CUB|||Charge relay system|||Complement C1r subcomponent-like protein|||Disordered|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Unable to cleave HP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318678|||http://purl.uniprot.org/annotation/PRO_5003322963|||http://purl.uniprot.org/annotation/PRO_5003323081|||http://purl.uniprot.org/annotation/VAR_038852
http://togogenome.org/gene/9606:STAU2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K276|||http://purl.uniprot.org/uniprot/Q4LE57|||http://purl.uniprot.org/uniprot/Q9NUL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DRBM|||DRBM 1|||DRBM 2|||DRBM 3|||DRBM 4|||Disordered|||Double-stranded RNA-binding protein Staufen homolog 2|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for dendritic transport                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072246|||http://purl.uniprot.org/annotation/VAR_023394|||http://purl.uniprot.org/annotation/VSP_015373|||http://purl.uniprot.org/annotation/VSP_015374|||http://purl.uniprot.org/annotation/VSP_015375|||http://purl.uniprot.org/annotation/VSP_015376|||http://purl.uniprot.org/annotation/VSP_015377|||http://purl.uniprot.org/annotation/VSP_046138|||http://purl.uniprot.org/annotation/VSP_046139|||http://purl.uniprot.org/annotation/VSP_046140|||http://purl.uniprot.org/annotation/VSP_046141|||http://purl.uniprot.org/annotation/VSP_046142
http://togogenome.org/gene/9606:GOLGA8K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RF30                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8K|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420859
http://togogenome.org/gene/9606:C15orf48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C002                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Normal mucosa of esophagus-specific gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118823
http://togogenome.org/gene/9606:CAPZB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AK85|||http://purl.uniprot.org/uniprot/P47756|||http://purl.uniprot.org/uniprot/Q7L4N0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||F-actin-capping protein subunit beta|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204634|||http://purl.uniprot.org/annotation/VSP_061615
http://togogenome.org/gene/9606:HMGXB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12766|||http://purl.uniprot.org/uniprot/Q562E5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||HMG box|||HMG domain-containing protein 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048806
http://togogenome.org/gene/9606:DLGAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2C2|||http://purl.uniprot.org/uniprot/Q9Y2H0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disks large-associated protein 4|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174297|||http://purl.uniprot.org/annotation/VAR_057716|||http://purl.uniprot.org/annotation/VAR_057717|||http://purl.uniprot.org/annotation/VSP_006013|||http://purl.uniprot.org/annotation/VSP_034910|||http://purl.uniprot.org/annotation/VSP_034911
http://togogenome.org/gene/9606:OR6C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGE1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150626|||http://purl.uniprot.org/annotation/VAR_034246|||http://purl.uniprot.org/annotation/VAR_053220
http://togogenome.org/gene/9606:NFX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12986                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with PABPC1 and PABC4|||NF-X1-type 1|||NF-X1-type 2|||NF-X1-type 3|||NF-X1-type 4|||NF-X1-type 5|||NF-X1-type 6|||NF-X1-type 7|||NF-X1-type 8|||Phosphoserine|||Polar residues|||R3H|||RING-type; atypical|||Reduces PABPC1 and PABC4 binding.|||Transcriptional repressor NF-X1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055979|||http://purl.uniprot.org/annotation/VAR_043380|||http://purl.uniprot.org/annotation/VAR_043381|||http://purl.uniprot.org/annotation/VAR_043382|||http://purl.uniprot.org/annotation/VSP_033682|||http://purl.uniprot.org/annotation/VSP_033683|||http://purl.uniprot.org/annotation/VSP_033684|||http://purl.uniprot.org/annotation/VSP_033685
http://togogenome.org/gene/9606:TRMT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233098|||http://purl.uniprot.org/annotation/VAR_053789|||http://purl.uniprot.org/annotation/VAR_053790|||http://purl.uniprot.org/annotation/VAR_053791|||http://purl.uniprot.org/annotation/VSP_018025|||http://purl.uniprot.org/annotation/VSP_031100|||http://purl.uniprot.org/annotation/VSP_031101|||http://purl.uniprot.org/annotation/VSP_054740
http://togogenome.org/gene/9606:HSPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04792|||http://purl.uniprot.org/uniprot/V9HW43                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Found in a patient with sporadic amyotrophic lateral sclerosis; unknown pathological significance.|||Heat shock protein beta-1|||In CMT2F and HMN2B.|||In CMT2F and HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport.|||In CMT2F.|||In CMT2F; decreased homodimerization only with the wild-type protein; increased client proteins binding; increased function in chaperone-mediated protein folding.|||In CMT2F; unknown pathological significance.|||In HMN2B and CMT2F; increased aggregation; increased homooligomerization; decreased phosphorylation by MAPKAPK2; changed function in chaperone-mediated protein folding.|||In HMN2B.|||In HMN2B; decreased homodimerization; increased client proteins binding; increased function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins and indirectly impairs their anterograde axonal transport.|||In HMN2B; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding.|||In HMN2B; decreased protein abundance; no effect on oligomerization; increased client proteins binding; no effect on function in chaperone-mediated protein folding; alters CDK5-mediated phosphorylation of neurofilament proteins; indirectly impairs their anterograde axonal transport.|||In HMN2B; decreased thermal stability; changed protein structure; changed homooligomerization; loss of heterooligomerization with HSPB6; decreased function in chaperone-mediated protein folding.|||In HMN2B; decreased thermal stability; changed protein structure; no effect on homooligomerization; changed heterooligomerization with HSPB6; slightly decreased function in chaperone-mediated protein folding.|||In HMN2B; formation of large cytoplasmic aggregates; no effect on dimerization.|||In HMN2B; increased aggregation; increased homooligomerization; changed function in chaperone-mediated protein folding.|||In HMN2B; induces hyperphosphorylation of neurofilaments; no effect on cytoplasmic location; no effect on dimerization.|||In HMN2B; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization.|||In HMN2B; no effect on homodimerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding.|||In HMN2B; unknown pathological significance.|||In HMN2B; unknown pathological significance; no effect on dimerization; no effect on cytoplasmic location; no effect on dimerization.|||Interaction with TGFB1I1|||Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78.|||Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82.|||Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82.|||N6-acetyllysine|||No effect on oligomerization; no effect on client proteins binding; no effect on function in chaperone-mediated protein folding.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MAPKAPK2 and MAPKAPK3|||Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5|||Phosphothreonine|||SHSP|||sHSP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125927|||http://purl.uniprot.org/annotation/VAR_018506|||http://purl.uniprot.org/annotation/VAR_018507|||http://purl.uniprot.org/annotation/VAR_018508|||http://purl.uniprot.org/annotation/VAR_018509|||http://purl.uniprot.org/annotation/VAR_018510|||http://purl.uniprot.org/annotation/VAR_067085|||http://purl.uniprot.org/annotation/VAR_077483|||http://purl.uniprot.org/annotation/VAR_077484|||http://purl.uniprot.org/annotation/VAR_077485|||http://purl.uniprot.org/annotation/VAR_077486|||http://purl.uniprot.org/annotation/VAR_077487|||http://purl.uniprot.org/annotation/VAR_077488|||http://purl.uniprot.org/annotation/VAR_077489|||http://purl.uniprot.org/annotation/VAR_077490|||http://purl.uniprot.org/annotation/VAR_077491|||http://purl.uniprot.org/annotation/VAR_077492|||http://purl.uniprot.org/annotation/VAR_077493|||http://purl.uniprot.org/annotation/VAR_077494|||http://purl.uniprot.org/annotation/VAR_078128|||http://purl.uniprot.org/annotation/VAR_078129|||http://purl.uniprot.org/annotation/VAR_078130|||http://purl.uniprot.org/annotation/VAR_078131|||http://purl.uniprot.org/annotation/VAR_078132
http://togogenome.org/gene/9606:GPRC5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZD1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor family C group 5 member D|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206897|||http://purl.uniprot.org/annotation/VAR_018297|||http://purl.uniprot.org/annotation/VSP_010006|||http://purl.uniprot.org/annotation/VSP_010007|||http://purl.uniprot.org/annotation/VSP_010008
http://togogenome.org/gene/9606:FPGT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5C6|||http://purl.uniprot.org/uniprot/O14772                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fucose-1-phosphate guanylyltransferase|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||L-fucokinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087327|||http://purl.uniprot.org/annotation/VAR_061650|||http://purl.uniprot.org/annotation/VSP_059541|||http://purl.uniprot.org/annotation/VSP_059542|||http://purl.uniprot.org/annotation/VSP_059543
http://togogenome.org/gene/9606:SLC2A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT42|||http://purl.uniprot.org/uniprot/Q5VVV9|||http://purl.uniprot.org/uniprot/Q8WZ05|||http://purl.uniprot.org/uniprot/Q9NY64                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Dileucine internalization motif|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Solute carrier family 2, facilitated glucose transporter member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050375|||http://purl.uniprot.org/annotation/VAR_061880
http://togogenome.org/gene/9606:PLEKHG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7P9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||In LDAMD; results in impaired regulation of actin polymerization.|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family G member 2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306861|||http://purl.uniprot.org/annotation/VAR_035324|||http://purl.uniprot.org/annotation/VAR_035325|||http://purl.uniprot.org/annotation/VAR_035326|||http://purl.uniprot.org/annotation/VAR_035327|||http://purl.uniprot.org/annotation/VAR_035328|||http://purl.uniprot.org/annotation/VAR_035329|||http://purl.uniprot.org/annotation/VAR_078577|||http://purl.uniprot.org/annotation/VSP_028529|||http://purl.uniprot.org/annotation/VSP_028530
http://togogenome.org/gene/9606:TTBK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCY1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In a lung large cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Tau-tubulin kinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234341|||http://purl.uniprot.org/annotation/VAR_041252|||http://purl.uniprot.org/annotation/VAR_041253|||http://purl.uniprot.org/annotation/VAR_041254|||http://purl.uniprot.org/annotation/VAR_041255|||http://purl.uniprot.org/annotation/VAR_041256|||http://purl.uniprot.org/annotation/VAR_041257|||http://purl.uniprot.org/annotation/VAR_041258|||http://purl.uniprot.org/annotation/VAR_041259|||http://purl.uniprot.org/annotation/VAR_041260|||http://purl.uniprot.org/annotation/VSP_026497|||http://purl.uniprot.org/annotation/VSP_026498|||http://purl.uniprot.org/annotation/VSP_026499
http://togogenome.org/gene/9606:RPUSD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BQN8|||http://purl.uniprot.org/uniprot/H3BUN6|||http://purl.uniprot.org/uniprot/Q9UJJ7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Pro residues|||Pseudouridine synthase RsuA/RluA-like|||RNA pseudouridylate synthase domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300816|||http://purl.uniprot.org/annotation/VAR_034883|||http://purl.uniprot.org/annotation/VAR_034884
http://togogenome.org/gene/9606:ABHD14A-ACY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNW0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Domain Extent|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Domain Extent                                                                                  ^@                                                                                  Peptidase M20 dimerisation|||Proton acceptor                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:PLAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBJ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Placenta-specific protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251144
http://togogenome.org/gene/9606:XKR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GH70                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Site|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase-3, caspase-6 and caspase-7|||Helical|||XK-related protein 9|||XK-related protein 9, processed form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190796|||http://purl.uniprot.org/annotation/PRO_0000453293
http://togogenome.org/gene/9606:FAM107A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95990|||http://purl.uniprot.org/uniprot/Q6IAM1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-associated protein FAM107A|||Decreases nuclear localization and ubiquitination of NF-kappa-B subunit RELA.|||Decreases nuclear localization.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In ovarian cancer and renal cell carcinoma cell lines.|||In renal cell carcinoma cell line.|||Increases diffused cytoplasm localization, loss of interaction with ACTB and colocalization with nuclear F-actin, decreases COMMD1 protein stability and ubiquitination of NF-kappa-B subunit RELA and decreases focal adhesion (FA) disassembly and cell migration; when associated with 122-A-A-123.|||Increases diffused cytoplasm localization, loss of interaction with ACTB and colocalization with nuclear F-actin, decreases COMMD1 protein stability and ubiquitination of NF-kappa-B subunit RELA and decreases focal adhesion (FA) disassembly and cell migration; when associated with 65-A-A-66.|||Increases nuclear and diffused cytoplasm localization, decreases interaction with MAP1A, alters actin cytoskeleton organization and decreases focal adhesion (FA) disassembly and cell migration.|||Nuclear localization signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080014|||http://purl.uniprot.org/annotation/VAR_017238|||http://purl.uniprot.org/annotation/VAR_017239|||http://purl.uniprot.org/annotation/VAR_049016|||http://purl.uniprot.org/annotation/VAR_049017|||http://purl.uniprot.org/annotation/VSP_009232|||http://purl.uniprot.org/annotation/VSP_054803|||http://purl.uniprot.org/annotation/VSP_054804
http://togogenome.org/gene/9606:CCT6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92526                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||T-complex protein 1 subunit zeta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128363|||http://purl.uniprot.org/annotation/VAR_057269|||http://purl.uniprot.org/annotation/VAR_060297|||http://purl.uniprot.org/annotation/VAR_060298|||http://purl.uniprot.org/annotation/VSP_043040|||http://purl.uniprot.org/annotation/VSP_047129
http://togogenome.org/gene/9606:MIGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZP8|||http://purl.uniprot.org/uniprot/Q7L4E1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||FFAT|||Helical|||In isoform 2.|||In isoform 3.|||Mitoguardin 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313657|||http://purl.uniprot.org/annotation/VAR_037690|||http://purl.uniprot.org/annotation/VAR_037691|||http://purl.uniprot.org/annotation/VAR_037692|||http://purl.uniprot.org/annotation/VSP_030087|||http://purl.uniprot.org/annotation/VSP_030088|||http://purl.uniprot.org/annotation/VSP_030089|||http://purl.uniprot.org/annotation/VSP_030090
http://togogenome.org/gene/9606:ST3GAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q11203                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In DEE15.|||In MRT12; most of the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function.|||In MRT12; the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function; shows a complete lack of enzyme activity; secretion of the mutant protein is dramatically reduced compared to wild-type.|||In isoform A1, isoform A7 and isoform A8.|||In isoform A7, isoform B7 and isoform C7.|||In isoform A8, isoform B8 and isoform C8.|||In isoform B1+32.|||In isoform B1-90.|||In isoform B10.|||In isoform B3 and isoform C11.|||In isoform B4+173.|||In isoform B4, isoform C4 and isoform C11.|||In isoform B5+173.|||In isoform B5+26 and isoform D2+26.|||In isoform C1, isoform C4, isoform C5, isoform C7, isoform C8, isoform C9, isoform C11 and isoform C12.|||In isoform C12.|||In isoform C5 and isoform D5.|||In isoform C9.|||In isoform D5 and isoform D2+26.|||In isoform E1.|||In isoform E3+32.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149266|||http://purl.uniprot.org/annotation/VAR_066594|||http://purl.uniprot.org/annotation/VAR_066595|||http://purl.uniprot.org/annotation/VAR_069319|||http://purl.uniprot.org/annotation/VSP_010591|||http://purl.uniprot.org/annotation/VSP_010592|||http://purl.uniprot.org/annotation/VSP_010593|||http://purl.uniprot.org/annotation/VSP_010594|||http://purl.uniprot.org/annotation/VSP_010595|||http://purl.uniprot.org/annotation/VSP_010596|||http://purl.uniprot.org/annotation/VSP_010597|||http://purl.uniprot.org/annotation/VSP_010598|||http://purl.uniprot.org/annotation/VSP_010599|||http://purl.uniprot.org/annotation/VSP_010600|||http://purl.uniprot.org/annotation/VSP_010601|||http://purl.uniprot.org/annotation/VSP_010602|||http://purl.uniprot.org/annotation/VSP_010603|||http://purl.uniprot.org/annotation/VSP_010604|||http://purl.uniprot.org/annotation/VSP_010605|||http://purl.uniprot.org/annotation/VSP_010606|||http://purl.uniprot.org/annotation/VSP_010607|||http://purl.uniprot.org/annotation/VSP_010608|||http://purl.uniprot.org/annotation/VSP_010609|||http://purl.uniprot.org/annotation/VSP_010610|||http://purl.uniprot.org/annotation/VSP_010611|||http://purl.uniprot.org/annotation/VSP_010612|||http://purl.uniprot.org/annotation/VSP_010613|||http://purl.uniprot.org/annotation/VSP_010614|||http://purl.uniprot.org/annotation/VSP_010615|||http://purl.uniprot.org/annotation/VSP_010616|||http://purl.uniprot.org/annotation/VSP_010617|||http://purl.uniprot.org/annotation/VSP_010618
http://togogenome.org/gene/9606:CRIPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P021                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine-rich PDZ-binding protein|||In SSMCF.|||PDZ3-binding|||Sufficient for interaction with DLG4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314563|||http://purl.uniprot.org/annotation/VAR_078425
http://togogenome.org/gene/9606:PCDHGA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with intellectual disability; unknown pathological significance.|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003966|||http://purl.uniprot.org/annotation/VAR_048566|||http://purl.uniprot.org/annotation/VAR_048567|||http://purl.uniprot.org/annotation/VAR_084654|||http://purl.uniprot.org/annotation/VSP_008677|||http://purl.uniprot.org/annotation/VSP_008678
http://togogenome.org/gene/9606:TBC1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A6J6|||http://purl.uniprot.org/uniprot/Q6PJJ8|||http://purl.uniprot.org/uniprot/Q86TI0|||http://purl.uniprot.org/uniprot/Q8NC59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||May be associated with risk of familial obesity.|||PID|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphothreonine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Rab-GAP TBC|||Substantially reduced RabGAPGTPase hydrolysis activity.|||TBC1 domain family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208022|||http://purl.uniprot.org/annotation/VAR_028089|||http://purl.uniprot.org/annotation/VAR_028090|||http://purl.uniprot.org/annotation/VAR_028091|||http://purl.uniprot.org/annotation/VAR_028092|||http://purl.uniprot.org/annotation/VAR_028093|||http://purl.uniprot.org/annotation/VAR_054392|||http://purl.uniprot.org/annotation/VSP_044749|||http://purl.uniprot.org/annotation/VSP_044750
http://togogenome.org/gene/9606:GGA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6M0|||http://purl.uniprot.org/uniprot/B7Z456|||http://purl.uniprot.org/uniprot/Q9NZ52                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-binding protein GGA3|||Acts as dominant negative. Prevents proteolytic cleavage by CASP3; when associated with A-328, A-333 and A-428.|||Binds to ARF1 (in long isoform)|||Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258.|||DXXLL|||Disordered|||GAE|||GAT|||In a breast cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform Short.|||Increased binding to IGF2R.|||Loss of UBC-binding and ubiquitination.|||Loss of UBC-binding and ubiquitination. Abolishes binding to ubiquitin. Abolishes regulation of BACE1 degradation. No effect on interaction with NTRK1.|||Loss of interaction with ARF1 and Golgi localization.|||No effect on regulation of BACE1 degradation.|||No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283.|||Phosphoserine|||Polar residues|||Prevents proteolytic cleavage by CASP3; when associated with A-313, A-328 and A-333.|||Prevents proteolytic cleavage by CASP3; when associated with A-313, A-328 and A-428.|||Prevents proteolytic cleavage by CASP3; when associated with A-313, A-333 and A-428.|||Pro residues|||Unstructured hinge|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212684|||http://purl.uniprot.org/annotation/VAR_036524|||http://purl.uniprot.org/annotation/VAR_075715|||http://purl.uniprot.org/annotation/VAR_075716|||http://purl.uniprot.org/annotation/VSP_001745|||http://purl.uniprot.org/annotation/VSP_045133|||http://purl.uniprot.org/annotation/VSP_045134|||http://purl.uniprot.org/annotation/VSP_046868
http://togogenome.org/gene/9606:PYGL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06737                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased acetylation; when associated with R-470.|||Decreased acetylation; when associated with R-796.|||Decreased glycogen phosphorylase activity.|||Glycogen phosphorylase, liver form|||In GSD6.|||In isoform 2.|||Involved in the association of subunits|||May be involved in allosteric control|||N-acetylalanine|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphoserine; by PHK; in form phosphorylase a|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188524|||http://purl.uniprot.org/annotation/VAR_007907|||http://purl.uniprot.org/annotation/VAR_007908|||http://purl.uniprot.org/annotation/VAR_007909|||http://purl.uniprot.org/annotation/VAR_013095|||http://purl.uniprot.org/annotation/VAR_013096|||http://purl.uniprot.org/annotation/VAR_034425|||http://purl.uniprot.org/annotation/VAR_034426|||http://purl.uniprot.org/annotation/VAR_034427|||http://purl.uniprot.org/annotation/VAR_069054|||http://purl.uniprot.org/annotation/VSP_045339
http://togogenome.org/gene/9606:SLC35A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96G79                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Probable UDP-sugar transporter protein SLC35A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337748
http://togogenome.org/gene/9606:NHERF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15599                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Na(+)/H(+) exchange regulatory cofactor NHE-RF2|||PDZ 1|||PDZ 2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096805|||http://purl.uniprot.org/annotation/VSP_009378|||http://purl.uniprot.org/annotation/VSP_046849|||http://purl.uniprot.org/annotation/VSP_046850
http://togogenome.org/gene/9606:ATP7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRW0|||http://purl.uniprot.org/uniprot/Q04656|||http://purl.uniprot.org/uniprot/Q762B6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Copper-transporting ATPase 1|||Cytoplasmic|||Endocytosis signal|||Extracellular|||HMA|||HMA 1|||HMA 2|||HMA 3|||HMA 4|||HMA 5|||HMA 6|||HMA 7|||Helical|||Impairs Cu(+)-bridged heterodimer formation with ATOX1 while increasing the reactivity toward cisplatin.|||Impairs tyrosinase activity involved in melanin synthesis.|||In DSMAX3; demonstrates impaired intracellular trafficking compared to control with some mutant protein remaining in the Golgi apparatus after exposure to copper.|||In DSMAX3; demonstrates impaired intracellular trafficking compared to control with some of the mutant protein remaining in the Golgi apparatus after exposure to copper.|||In MNK.|||In MNK; decreased protein abundance; impaired copper transport activity.|||In MNK; decreased protein abundance; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity.|||In MNK; decreased protein abundance; increased protein degradation; does not affect interaction with ATOX1; does not affect interaction with COMMD1; subcellular location restricted to TGN; does not localizes to the plasma membrane in response to elevated copper levels; impaired copper transport activity.|||In MNK; has no effect on copper-dependent trafficking from TGN to post-TGN compartments; impaired copper transport activity.|||In MNK; impaired copper-dependent trafficking from TGN to post-TGN compartments; subcellular location restricted to TGN; impaired copper transport activity.|||In MNK; increased protein abundance; does not affect interaction with ATOX1; does not affect interaction with COMMD1; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion.|||In MNK; loss of protein expression.|||In MNK; subcellular location restricted to post-TGN compartments; impaired copper transport activity.|||In OHS.|||In OHS; has approximately 33% residual copper transport; increased protein abundance; increased localization at the plasma membrane; does not cycle back to TGN under conditions of copper depletion; does not affect interaction with ATOX1; does not affect interaction with COMMD1.|||In OHS; has no effect on copper-dependent trafficking; impaired copper transport activity.|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Loss of relocalization to the trans-Golgi.|||N-linked (GlcNAc...) asparagine|||PDZD11-binding|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046311|||http://purl.uniprot.org/annotation/VAR_000699|||http://purl.uniprot.org/annotation/VAR_000700|||http://purl.uniprot.org/annotation/VAR_000701|||http://purl.uniprot.org/annotation/VAR_000702|||http://purl.uniprot.org/annotation/VAR_009999|||http://purl.uniprot.org/annotation/VAR_010000|||http://purl.uniprot.org/annotation/VAR_010001|||http://purl.uniprot.org/annotation/VAR_010002|||http://purl.uniprot.org/annotation/VAR_010003|||http://purl.uniprot.org/annotation/VAR_010004|||http://purl.uniprot.org/annotation/VAR_010005|||http://purl.uniprot.org/annotation/VAR_010006|||http://purl.uniprot.org/annotation/VAR_010007|||http://purl.uniprot.org/annotation/VAR_010008|||http://purl.uniprot.org/annotation/VAR_016119|||http://purl.uniprot.org/annotation/VAR_016120|||http://purl.uniprot.org/annotation/VAR_016121|||http://purl.uniprot.org/annotation/VAR_023261|||http://purl.uniprot.org/annotation/VAR_023262|||http://purl.uniprot.org/annotation/VAR_023263|||http://purl.uniprot.org/annotation/VAR_023264|||http://purl.uniprot.org/annotation/VAR_023265|||http://purl.uniprot.org/annotation/VAR_023266|||http://purl.uniprot.org/annotation/VAR_023267|||http://purl.uniprot.org/annotation/VAR_023268|||http://purl.uniprot.org/annotation/VAR_023269|||http://purl.uniprot.org/annotation/VAR_023270|||http://purl.uniprot.org/annotation/VAR_023271|||http://purl.uniprot.org/annotation/VAR_023272|||http://purl.uniprot.org/annotation/VAR_023273|||http://purl.uniprot.org/annotation/VAR_023274|||http://purl.uniprot.org/annotation/VAR_023275|||http://purl.uniprot.org/annotation/VAR_023276|||http://purl.uniprot.org/annotation/VAR_023277|||http://purl.uniprot.org/annotation/VAR_023278|||http://purl.uniprot.org/annotation/VAR_023279|||http://purl.uniprot.org/annotation/VAR_023280|||http://purl.uniprot.org/annotation/VAR_063882|||http://purl.uniprot.org/annotation/VAR_063883|||http://purl.uniprot.org/annotation/VAR_063884|||http://purl.uniprot.org/annotation/VAR_068831|||http://purl.uniprot.org/annotation/VAR_080663|||http://purl.uniprot.org/annotation/VAR_084344|||http://purl.uniprot.org/annotation/VAR_084345|||http://purl.uniprot.org/annotation/VAR_084346|||http://purl.uniprot.org/annotation/VAR_084347|||http://purl.uniprot.org/annotation/VAR_084348|||http://purl.uniprot.org/annotation/VAR_084349|||http://purl.uniprot.org/annotation/VAR_084350|||http://purl.uniprot.org/annotation/VAR_084351|||http://purl.uniprot.org/annotation/VAR_084352|||http://purl.uniprot.org/annotation/VAR_084353|||http://purl.uniprot.org/annotation/VAR_084354|||http://purl.uniprot.org/annotation/VAR_084355|||http://purl.uniprot.org/annotation/VAR_084356|||http://purl.uniprot.org/annotation/VAR_084357|||http://purl.uniprot.org/annotation/VAR_084358|||http://purl.uniprot.org/annotation/VSP_000419|||http://purl.uniprot.org/annotation/VSP_000420|||http://purl.uniprot.org/annotation/VSP_000421|||http://purl.uniprot.org/annotation/VSP_000422|||http://purl.uniprot.org/annotation/VSP_000423|||http://purl.uniprot.org/annotation/VSP_000424|||http://purl.uniprot.org/annotation/VSP_000425
http://togogenome.org/gene/9606:PLEKHA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQL5|||http://purl.uniprot.org/uniprot/Q5RGS4|||http://purl.uniprot.org/uniprot/Q9HB21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphatidylinositide binding.|||Binds both PtdIns3,4P2 and PtdIns3,4,5P3.|||Disordered|||In isoform 2.|||No effect on phosphatidylinositide binding.|||No effect.|||PH|||PH 1|||PH 2|||Phosphoserine|||Pleckstrin homology domain-containing family A member 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053873|||http://purl.uniprot.org/annotation/VAR_024562|||http://purl.uniprot.org/annotation/VSP_043091
http://togogenome.org/gene/9606:ZW10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43264                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centromere/kinetochore protein zw10 homolog|||In isoform 2.|||Interaction with RINT1|||Interaction with ZWINT|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184957|||http://purl.uniprot.org/annotation/VAR_053537|||http://purl.uniprot.org/annotation/VSP_056006
http://togogenome.org/gene/9606:NDUFS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43920|||http://purl.uniprot.org/uniprot/Q6IBA0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance.|||Disordered|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118786|||http://purl.uniprot.org/annotation/VAR_064569
http://togogenome.org/gene/9606:TECRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYJ1                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In CPVT3; unknown pathological significance.|||Phosphoserine|||Trans-2,3-enoyl-CoA reductase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317713|||http://purl.uniprot.org/annotation/VAR_074183|||http://purl.uniprot.org/annotation/VAR_078556
http://togogenome.org/gene/9606:TAF1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5J8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||Disordered|||Phosphoserine|||Polar residues|||TATA box-binding protein-associated factor RNA polymerase I subunit D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250717
http://togogenome.org/gene/9606:CLDN15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56746                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-15|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Impairs the charge selectivity for paracellular ion transport, favoring Cl(-) transport.|||Important for Na(+)-selective paracellular ion transport|||Important for the formation of tight-junction strand-like structures|||No effect on charge selectivity for paracellular ion transport.|||Phosphoserine|||Reverses the charge selectivity for paracellular ion transport, favoring Cl(-) transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144771
http://togogenome.org/gene/9606:TP53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WT22|||http://purl.uniprot.org/uniprot/A0A087WXZ1|||http://purl.uniprot.org/uniprot/A0A087X1Q1|||http://purl.uniprot.org/uniprot/H2EHT1|||http://purl.uniprot.org/uniprot/K7PPA8|||http://purl.uniprot.org/uniprot/P04637|||http://purl.uniprot.org/uniprot/Q53GA5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes S-315 phosphorylation by CDK2/cyclin A.|||Abolishes SUMO1 conjugation, in vitro and in vivo.|||Abolishes SUMO1 conjugation.|||Abolishes acetylation by CREBBP.|||Abolishes binding to USP7.|||Abolishes dimethylation by EHMT1 and EHMT2.|||Abolishes monomethylation by KMT5A.|||Abolishes phosphorylation by DYRK2 and HIPK2 and acetylation of K-382 by CREBBP.|||Abolishes phosphorylation by MAPKAPK5.|||Abolishes phosphorylation site. Abolishes increase in protein levels after DNA damage.|||Abolishes phosphorylation.|||Abolishes polyubiquitination by MKRN1.|||Abolishes strongly phosphorylation.|||Abolishes ubiquitination by MUL1.|||Alters interaction with WWOX.|||Basic (repression of DNA-binding)|||Basic and acidic residues|||Basic residues|||Bipartite nuclear localization signal|||Blocks phosphorylation by TAF1.|||Cellular tumor antigen p53|||Cellular tumor antigen p53 transactivation|||Constitutively increased TP53 protein levels.|||Decreased acetylation.|||Disordered|||Does not induce SNAI1 degradation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In LFS; germline mutation and in a sporadic cancer; somatic mutation.|||In LFS; germline mutation and in sporadic cancers; somatic mutation.|||In LFS; germline mutation and in sporadic cancers; somatic mutation; abolishes sequence-specific DNA binding; does not induce SNAI1 degradation.|||In LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation.|||In LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation; reduces interaction with ZNF385A; loss of susceptibility to calpain.|||In LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on susceptibility to calpain.|||In LFS; germline mutation.|||In a Burkitt lymphoma.|||In a brain tumor with no family history; germline mutation and in sporadic cancers; somatic mutation.|||In a breast cancer with no family history; germline mutation and in sporadic cancers; somatic mutation.|||In a familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation.|||In a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation.|||In a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation.|||In a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on interaction with CCAR2.|||In a familial cancer not matching LFS; germline mutation.|||In a kidney cancer with no family history; germline mutation and in a sporadic cancer; somatic mutation.|||In a sporadic cancer; somatic mutation.|||In a sporadic cancer; somatic mutation; abolishes strongly phosphorylation.|||In a sporadic cancer; somatic mutation; reduces interaction with ZNF385A.|||In a sporadic cancer; somatic mutation; requires 2 nucleotide substitutions.|||In an adrenocortical carcinoma with no family history; germline mutation and in sporadic cancers; somatic mutation.|||In an osteosarcoma with no family history; germline mutation and in sporadic cancers; somatic mutation.|||In familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation.|||In isoform 2, isoform 5 and isoform 8.|||In isoform 3, isoform 6 and isoform 9.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 7, isoform 8 and isoform 9.|||In kidney cancer; germline mutation.|||In sporadic cancers; somatic mutation.|||In sporadic cancers; somatic mutation; decreased E6-mediated binding to E6-AP.|||In sporadic cancers; somatic mutation; does not induce SNAI1 degradation.|||In sporadic cancers; somatic mutation; loss of nuclear localization.|||In sporadic cancers; somatic mutation; no effect on susceptibility to calpain.|||In sporadic cancers; somatic mutation; requires 2 nucleotide substitutions.|||In sporadic cancers; somatic mutation; strong DNA binding ability at 32.5 degrees Celsius; strong reduction of transcriptional activity at 37.5 degrees Celsius; severely represses interaction with ZNF385A.|||Induces a decrease in methylation by SMYD2.|||Induces a decrease in protein stabilization.|||Inhibits slightly its transcriptional activity.|||Inhibits strongly its transcriptional activity.|||Interaction with AXIN1|||Interaction with CARM1|||Interaction with CCAR2|||Interaction with DNA|||Interaction with E4F1|||Interaction with HIPK1|||Interaction with HIPK2|||Interaction with HRMT1L2|||Interaction with MORN3|||Interaction with USP7|||Interaction with WWOX|||Interaction with the 53BP2 SH3 domain|||Loss of interaction with MDM2, leading to constitutively increased TP53 protein levels.|||Loss of interaction with PPP2R5C, PPP2CAANDPPP2R1A.|||Loss of nuclear localization; when associated with A-319 and A-320.|||Loss of nuclear localization; when associated with A-319 and A-321.|||Loss of nuclear localization; when associated with A-320 and A-321.|||Mimics acetylation, leading to increased stability.|||N6,N6-dimethyllysine; alternate|||N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-acetyllysine; by KAT6A|||N6-acetyllysine; by KAT6A; alternate|||N6-methyllysine; by KMT5A; alternate|||N6-methyllysine; by SETD7|||N6-methyllysine; by SMYD2; alternate|||No effect SUMO1 conjugation.|||No effect on interaction with MDM2 and increase in protein levels after DNA damage.|||Nuclear export signal|||Oligomerization|||Omega-N-methylarginine; by PRMT5|||Phosphoserine; by AURKA, CDK1 and CDK2|||Phosphoserine; by AURKB|||Phosphoserine; by CDK5 and CDK7|||Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG|||Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM|||Phosphoserine; by CHEK2, CK1 and PLK3|||Phosphoserine; by CK2, CDK2 and NUAK1|||Phosphoserine; by HIPK4|||Phosphoserine; by MAPKAPK5|||Phosphothreonine; by AURKB|||Phosphothreonine; by CK1, VRK1 and VRK2|||Phosphothreonine; by TAF1 and GRK5|||Polar residues|||Pro residues|||Reduced SUMO1 conjugation.|||Reduced methylation by PRMT5. Reduced nuclear localization. Decreased binding to promoters of target genes. Reduced transcriptional activity. Decrease in cell cycle arrest.|||Required for interaction with FBXO42|||Required for interaction with ZNF385A|||Symmetric dimethylarginine; by PRMT5|||TADI|||TADII|||Transcription activation (acidic)|||[KR]-[STA]-K motif|||p53 DNA-binding|||p53 tetramerisation|||p53 transactivation ^@                                                                                  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http://togogenome.org/gene/9606:AEBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Adipocyte enhancer-binding protein 1|||Basic and acidic residues|||Disordered|||F5/8 type C|||In EDSCLL2.|||In isoform 2.|||Interaction with MAPK1 and MAPK3|||Interaction with PTEN|||N-linked (GlcNAc...) asparagine|||Pro residues|||Required for DNA-binding and interaction with NFKBIA|||Required for transcriptional repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333189|||http://purl.uniprot.org/annotation/VAR_043118|||http://purl.uniprot.org/annotation/VAR_043119|||http://purl.uniprot.org/annotation/VAR_043120|||http://purl.uniprot.org/annotation/VAR_043121|||http://purl.uniprot.org/annotation/VAR_043122|||http://purl.uniprot.org/annotation/VAR_080664|||http://purl.uniprot.org/annotation/VSP_033467|||http://purl.uniprot.org/annotation/VSP_033468|||http://purl.uniprot.org/annotation/VSP_033469
http://togogenome.org/gene/9606:INTS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVR2                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Integrator complex subunit 10|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235687
http://togogenome.org/gene/9606:PRY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14603                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||PTPN13-like protein, Y-linked                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097056|||http://purl.uniprot.org/annotation/VSP_004068|||http://purl.uniprot.org/annotation/VSP_004069
http://togogenome.org/gene/9606:CASP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYM1|||http://purl.uniprot.org/uniprot/A0A0S2Z3H1|||http://purl.uniprot.org/uniprot/P42575                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CARD|||Caspase family p10|||Caspase family p20|||Caspase-2 subunit p12|||Caspase-2 subunit p13|||Caspase-2 subunit p18|||Disordered|||In isoform 2.|||In isoform 3.|||Loss of function.|||Loss of interaction with CRADD.|||N-acetylalanine|||No effect on interaction with CRADD. Loss of interaction with CRADD; when associated A-100.|||No effect on interaction with CRADD. Loss of interaction with CRADD; when associated A-104.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004541|||http://purl.uniprot.org/annotation/PRO_0000004542|||http://purl.uniprot.org/annotation/PRO_0000004543|||http://purl.uniprot.org/annotation/PRO_0000004544|||http://purl.uniprot.org/annotation/PRO_0000004545|||http://purl.uniprot.org/annotation/VAR_016334|||http://purl.uniprot.org/annotation/VAR_016335|||http://purl.uniprot.org/annotation/VAR_016336|||http://purl.uniprot.org/annotation/VAR_055621|||http://purl.uniprot.org/annotation/VSP_000801|||http://purl.uniprot.org/annotation/VSP_000802|||http://purl.uniprot.org/annotation/VSP_046280|||http://purl.uniprot.org/annotation/VSP_046281|||http://purl.uniprot.org/annotation/VSP_046282
http://togogenome.org/gene/9606:MARK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP1|||http://purl.uniprot.org/uniprot/A8K2S4|||http://purl.uniprot.org/uniprot/Q7KZI7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 13, isoform 14, isoform 15 and isoform 16.|||In isoform 15.|||In isoform 2, isoform 3, isoform 6, isoform 7, isoform 10, isoform 12, isoform 13 and isoform 14.|||In isoform 2, isoform 4, isoform 5, isoform 7, isoform 9, isoform 10, isoform 13, isoform 15 and isoform 16.|||In isoform 3, isoform 4, isoform 7, isoform 8, isoform 13, isoform 14 and isoform 16.|||In isoform 5, isoform 11, isoform 10 and isoform 12.|||KA1|||Loss of membrane dissociation and binding to YWHAZ.|||Phosphoserine|||Phosphoserine; by CaMK1|||Phosphoserine; by GSK3-beta|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by CaMK1|||Phosphothreonine; by LKB1 and TAOK1|||Phosphothreonine; by PKC/PRKCZ|||Phosphothreonine; by autocatalysis|||Polar residues|||Prevents phosphorylation and activation by STK11/LKB1 complex.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase MARK2|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086301|||http://purl.uniprot.org/annotation/VSP_039872|||http://purl.uniprot.org/annotation/VSP_041853|||http://purl.uniprot.org/annotation/VSP_051705|||http://purl.uniprot.org/annotation/VSP_051706|||http://purl.uniprot.org/annotation/VSP_051707|||http://purl.uniprot.org/annotation/VSP_051708
http://togogenome.org/gene/9606:IL20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C4W0|||http://purl.uniprot.org/uniprot/Q9NYY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Interleukin family protein|||Interleukin-20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015381|||http://purl.uniprot.org/annotation/PRO_5035485050|||http://purl.uniprot.org/annotation/VAR_049577|||http://purl.uniprot.org/annotation/VSP_054904
http://togogenome.org/gene/9606:MRPL54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P161                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL54|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278280
http://togogenome.org/gene/9606:CPA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4T0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase A6|||In ETL5; affects protein secretion presumably by altering protein folding or stability.|||In FEB11; affects protein secretion presumably by altering protein folding or stability.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004365|||http://purl.uniprot.org/annotation/PRO_0000004366|||http://purl.uniprot.org/annotation/VAR_024241|||http://purl.uniprot.org/annotation/VAR_025003|||http://purl.uniprot.org/annotation/VAR_048597|||http://purl.uniprot.org/annotation/VAR_066946|||http://purl.uniprot.org/annotation/VAR_066947|||http://purl.uniprot.org/annotation/VSP_008808|||http://purl.uniprot.org/annotation/VSP_058375|||http://purl.uniprot.org/annotation/VSP_058376
http://togogenome.org/gene/9606:SCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NY87|||http://purl.uniprot.org/uniprot/B2R761|||http://purl.uniprot.org/uniprot/E9PLD1|||http://purl.uniprot.org/uniprot/P22307|||http://purl.uniprot.org/uniprot/Q59HG9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 3 and isoform 7.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform SCP2, isoform 5 and isoform 6.|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||SCP2|||Sterol carrier protein 2|||Strongly reduces sterol carrier and phosphatidylcholine transfer activity.|||Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528.|||Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530.|||Thiolase C-terminal|||Thiolase N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034091|||http://purl.uniprot.org/annotation/VAR_035706|||http://purl.uniprot.org/annotation/VSP_018977|||http://purl.uniprot.org/annotation/VSP_042686|||http://purl.uniprot.org/annotation/VSP_042687|||http://purl.uniprot.org/annotation/VSP_045187|||http://purl.uniprot.org/annotation/VSP_047267|||http://purl.uniprot.org/annotation/VSP_047268|||http://purl.uniprot.org/annotation/VSP_047269|||http://purl.uniprot.org/annotation/VSP_047270
http://togogenome.org/gene/9606:SECISBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR97|||http://purl.uniprot.org/uniprot/B4DZC7|||http://purl.uniprot.org/uniprot/Q96T21                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In THMA1.|||In isoform 2.|||In isoform 3.|||Nuclear localization signal|||Polar residues|||Pro residues|||RNA-binding|||Ribosomal protein eL8/eL30/eS12/Gadd45|||Selenocysteine insertion sequence-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097655|||http://purl.uniprot.org/annotation/VAR_025282|||http://purl.uniprot.org/annotation/VAR_061704|||http://purl.uniprot.org/annotation/VSP_039070|||http://purl.uniprot.org/annotation/VSP_039071|||http://purl.uniprot.org/annotation/VSP_055755
http://togogenome.org/gene/9606:PAX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXU6|||http://purl.uniprot.org/uniprot/A0A9L9PYK3|||http://purl.uniprot.org/uniprot/Q02962|||http://purl.uniprot.org/uniprot/Q5SZP1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with bilateral optic nerve colobomas; uncertain pathological significance.|||In FSGS7.|||In FSGS7; decreased DNA-binding capability and transactivation ability.|||In FSGS7; transactivation activity is dramatically decreased in presence of TLE4; dramatically enhances interaction with TLE4.|||In PAPRS.|||In PAPRS; the patient manifests oligomeganephronia and bilateral optic nerve coloboma.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||PAI subdomain|||Paired|||Paired box protein Pax-2|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with non-syndromic renal hypodysplasia.|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050175|||http://purl.uniprot.org/annotation/VAR_003788|||http://purl.uniprot.org/annotation/VAR_003789|||http://purl.uniprot.org/annotation/VAR_012442|||http://purl.uniprot.org/annotation/VAR_012443|||http://purl.uniprot.org/annotation/VAR_068079|||http://purl.uniprot.org/annotation/VAR_068080|||http://purl.uniprot.org/annotation/VAR_068081|||http://purl.uniprot.org/annotation/VAR_068082|||http://purl.uniprot.org/annotation/VAR_068083|||http://purl.uniprot.org/annotation/VAR_068084|||http://purl.uniprot.org/annotation/VAR_068085|||http://purl.uniprot.org/annotation/VAR_068086|||http://purl.uniprot.org/annotation/VAR_068087|||http://purl.uniprot.org/annotation/VAR_068088|||http://purl.uniprot.org/annotation/VAR_068089|||http://purl.uniprot.org/annotation/VAR_068090|||http://purl.uniprot.org/annotation/VAR_068091|||http://purl.uniprot.org/annotation/VAR_068092|||http://purl.uniprot.org/annotation/VAR_068093|||http://purl.uniprot.org/annotation/VAR_068094|||http://purl.uniprot.org/annotation/VAR_068095|||http://purl.uniprot.org/annotation/VAR_068096|||http://purl.uniprot.org/annotation/VAR_071937|||http://purl.uniprot.org/annotation/VAR_071938|||http://purl.uniprot.org/annotation/VAR_071939|||http://purl.uniprot.org/annotation/VAR_071940|||http://purl.uniprot.org/annotation/VAR_071941|||http://purl.uniprot.org/annotation/VAR_071942|||http://purl.uniprot.org/annotation/VAR_071943|||http://purl.uniprot.org/annotation/VAR_071944|||http://purl.uniprot.org/annotation/VAR_071945|||http://purl.uniprot.org/annotation/VAR_071946|||http://purl.uniprot.org/annotation/VAR_071947|||http://purl.uniprot.org/annotation/VSP_002345|||http://purl.uniprot.org/annotation/VSP_002346
http://togogenome.org/gene/9606:LHX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0D5|||http://purl.uniprot.org/uniprot/F1T0D9|||http://purl.uniprot.org/uniprot/Q9UBR4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In CPHD3.|||In CPHD3; associated with diminished DNA binding and pituitary gene activation.|||In CPHD3; unknown pathological significance.|||In isoform B.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075781|||http://purl.uniprot.org/annotation/VAR_010713|||http://purl.uniprot.org/annotation/VAR_063240|||http://purl.uniprot.org/annotation/VAR_079378|||http://purl.uniprot.org/annotation/VAR_079379|||http://purl.uniprot.org/annotation/VSP_003107
http://togogenome.org/gene/9606:PCDHGA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003964|||http://purl.uniprot.org/annotation/VAR_048565|||http://purl.uniprot.org/annotation/VSP_008675|||http://purl.uniprot.org/annotation/VSP_008676
http://togogenome.org/gene/9606:PARP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09874                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  0.6% of wild-type activity.|||1.5% of wild-type activity.|||10% of wild-type activity.|||14% of wild-type activity and increased branching 15-fold.|||4% of wild-type activity.|||<0.5% of wild-type activity.|||ADP-ribosylserine|||Able to bind BAD inhibitor in absence of DNA.|||Able to bind EB-47 or BAD inhibitors in absence of DNA. Released from DNA strand break independently of EB-47 or BAD inhibitors.|||Abolished DNA-binding.|||Abolished binding to DNA strand breaks.|||Abolished cleavage by caspase-7 (CASP7).|||Abolished interaction with TIMELESS.|||Abolished phosphorylation by PRKDC, inhibiting translocation into the cytosol.|||Abolished prolonged residence (trapping) to chromatin.|||Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-499 and A-507.|||Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-499 and A-519.|||Abolishes automodification on serine following interaction with HPF1, leading to delay dissociation from chromatin; when associated with A-507 and A-519.|||Abolishes enzymatic activity.|||Automodification domain|||BRCT|||Cleavage; by caspase-3 and caspase-7|||Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA.|||Decreased poly-ADP-ribosyltransferase activity upon binding to damaged DNA. Abolished ability to mediate DNA intrastrand transfer (named 'monkey-bar mechanism').|||Decreased polymerase activity, leading to the production of short poly-ADP-ribose chains.|||Decreased stability leading to impaired oly-ADP-ribosyltransferase activity.|||Disordered|||Does not affect ADP-ribosyltransferase activity.|||Does not affect DNA-binding.|||Does not affect DNA-binding. Decreased poly-ADP-ribosyltransferase activity.|||Does not affect DNA-independent poly-ADP-ribosyltransferase activity.|||Does not affect auto-poly-ADP-ribosylation.|||Does not affect translocation into the cytosol.|||For poly [ADP-ribose] polymerase activity|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a breast cancer sample; somatic mutation.|||Increased DNA-independent poly-ADP-ribosyltransferase activity.|||Increased affinity for DNA damage sites.|||Increased auto-poly-ADP-ribosylation.|||Leads to constitutive activity in absence of DNA damage due to unfolding of the PARP alpha-helical domain, relieving autoinhibition.|||N-acetylalanine|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||No effect.|||Nuclear localization signal|||PADR1 zinc-binding|||PARP alpha-helical|||PARP catalytic|||PARP-type 1|||PARP-type 2|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PRKDC|||Polar residues|||Poly [ADP-ribose] polymerase 1|||Poly [ADP-ribose] polymerase 1, processed C-terminus|||Poly [ADP-ribose] polymerase 1, processed N-terminus|||Poly-ADP-ribosyltransferase activity is impaired while mono-ADP-ribosyltransferase activity is not affected; produces a mixture of short and mono ADP-ribose chains.|||Poly-ADP-ribosyltransferase activity is inhibited while mono-ADP-ribosyltransferase activity is not affected; only monomers are added. Disrupts interaction with CHD1L and ability to recruit PARP2 to DNA damage sites.|||PolyADP-ribosyl aspartic acid|||PolyADP-ribosyl glutamic acid|||Removed|||Strongly decreased DNA-binding.|||Strongly decreased ability of the BRCT domain to bind intact DNA.|||Strongly decreased ability of the BRCT domain to bind intact DNA; when associated with Q-394.|||Strongly decreased ability of the BRCT domain to bind intact DNA; when associated with Q-418.|||Strongly decreased homodimerization.|||Strongly reduced interaction with TIMELESS.|||Strongly reduced poly-ADP-ribosyltransferase activity. Able to bind damaged DNA, however, defects in the interdomain communication prevent unfolding of the PARP alpha-helical domain, blocking catalytic activation.|||Strongly reduced poly-ADP-ribosyltransferase and ability to regulate chromatin compaction.|||Strongly reduced serine ADP-ribosylation, caused by abolished interaction with HPF1.|||WGR|||Zinc ribbon ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211320|||http://purl.uniprot.org/annotation/PRO_0000456361|||http://purl.uniprot.org/annotation/PRO_0000456362|||http://purl.uniprot.org/annotation/VAR_014714|||http://purl.uniprot.org/annotation/VAR_014715|||http://purl.uniprot.org/annotation/VAR_019171|||http://purl.uniprot.org/annotation/VAR_019172|||http://purl.uniprot.org/annotation/VAR_019173|||http://purl.uniprot.org/annotation/VAR_035852|||http://purl.uniprot.org/annotation/VAR_050460|||http://purl.uniprot.org/annotation/VAR_050461
http://togogenome.org/gene/9606:CCDC74A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR57|||http://purl.uniprot.org/uniprot/F5GZA4|||http://purl.uniprot.org/uniprot/Q96AQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CCDC92/74 N-terminal|||Coiled coil protein 74 C-terminal|||Coiled-coil domain-containing protein 74A|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274374|||http://purl.uniprot.org/annotation/VAR_030268|||http://purl.uniprot.org/annotation/VSP_022729
http://togogenome.org/gene/9606:ITM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDP7|||http://purl.uniprot.org/uniprot/Q9Y287                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Peptide|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Accumulates in intracellular compartments. Does not inhibit furin, ADAM10 and SPPL2A extracellular proteolytic processing activity.|||BRI2 intracellular domain|||BRI2, membrane form|||BRI2C, soluble form|||BRICHOS|||Bri23 peptide|||Cleavage; by furin|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In CAA-ITM2B1; amyloid ABri.|||In CAA-ITM2B2; amyloid ADan; colocalizes with APP amyloid-beta protein 42 in parenchymal and vascular lesions; interacts with APP amyloid-beta protein 42; oligomerizes and is subjected to disulfide bond formation; undergoes cyclic pyroglutamate formation on the N-terminus Gln residues and is further proteolytically cleaved in the cerebral cortex.|||In RDGCA.|||In isoform 2.|||Inhibits cleavage by furin. Does not prevent ADAM10 shedding.|||Integral membrane protein 2B|||Interchain|||Interchain (between ADan peptide variants)|||Lumenal|||N-linked (GlcNAc...) asparagine|||Necessary for interaction with APP and inhibitor effects on APP processing|||Strongly reduces intramembrane cleavage by SPPL2B.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016545|||http://purl.uniprot.org/annotation/PRO_0000045840|||http://purl.uniprot.org/annotation/PRO_0000417464|||http://purl.uniprot.org/annotation/PRO_0000417465|||http://purl.uniprot.org/annotation/PRO_0000417466|||http://purl.uniprot.org/annotation/VAR_010239|||http://purl.uniprot.org/annotation/VAR_010240|||http://purl.uniprot.org/annotation/VAR_071047|||http://purl.uniprot.org/annotation/VAR_072434|||http://purl.uniprot.org/annotation/VSP_055326
http://togogenome.org/gene/9606:ATR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13535                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes kinase activity.|||Abolishes kinase activity; increases sensitivity to IR and impairs translocation to nuclear foci upon DNA damage.|||Abolishes kinase activity; reduces cell viability, augments sensitivity to IR and UV.|||Activation loop|||Catalytic loop|||Disordered|||FAT|||FATC|||G-loop|||HEAT 1|||HEAT 2|||In FCTCS.|||In a breast infiltrating ductal carcinoma sample; somatic mutation.|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||PI3K/PI4K catalytic|||Phosphoserine|||Phosphothreonine|||Polar residues|||Serine/threonine-protein kinase ATR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088844|||http://purl.uniprot.org/annotation/VAR_041584|||http://purl.uniprot.org/annotation/VAR_041585|||http://purl.uniprot.org/annotation/VAR_041586|||http://purl.uniprot.org/annotation/VAR_041587|||http://purl.uniprot.org/annotation/VAR_041588|||http://purl.uniprot.org/annotation/VAR_041589|||http://purl.uniprot.org/annotation/VAR_041590|||http://purl.uniprot.org/annotation/VAR_041591|||http://purl.uniprot.org/annotation/VAR_041592|||http://purl.uniprot.org/annotation/VAR_041593|||http://purl.uniprot.org/annotation/VAR_041594|||http://purl.uniprot.org/annotation/VAR_041595|||http://purl.uniprot.org/annotation/VAR_041596|||http://purl.uniprot.org/annotation/VAR_041597|||http://purl.uniprot.org/annotation/VAR_041598|||http://purl.uniprot.org/annotation/VAR_041599|||http://purl.uniprot.org/annotation/VAR_041600|||http://purl.uniprot.org/annotation/VAR_041601|||http://purl.uniprot.org/annotation/VAR_050532|||http://purl.uniprot.org/annotation/VAR_050533|||http://purl.uniprot.org/annotation/VAR_067919|||http://purl.uniprot.org/annotation/VSP_013304|||http://purl.uniprot.org/annotation/VSP_013305|||http://purl.uniprot.org/annotation/VSP_036907|||http://purl.uniprot.org/annotation/VSP_036908
http://togogenome.org/gene/9606:ADAMTS17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BRA9|||http://purl.uniprot.org/uniprot/Q8TE56                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 17|||Cysteine switch|||Disintegrin|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029198|||http://purl.uniprot.org/annotation/PRO_0000029199|||http://purl.uniprot.org/annotation/PRO_5029478513|||http://purl.uniprot.org/annotation/VAR_057081|||http://purl.uniprot.org/annotation/VAR_057082|||http://purl.uniprot.org/annotation/VAR_060317|||http://purl.uniprot.org/annotation/VAR_064041|||http://purl.uniprot.org/annotation/VSP_040331|||http://purl.uniprot.org/annotation/VSP_040332|||http://purl.uniprot.org/annotation/VSP_040333
http://togogenome.org/gene/9606:PPFIA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVS8|||http://purl.uniprot.org/uniprot/Q13136                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Liprin-alpha-1|||Phosphoserine|||Phosphothreonine|||Polar residues|||SAM|||SAM 1|||SAM 2|||SAM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191026|||http://purl.uniprot.org/annotation/VAR_017756|||http://purl.uniprot.org/annotation/VAR_049998|||http://purl.uniprot.org/annotation/VSP_009391
http://togogenome.org/gene/9606:ADRA2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08913                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol.|||Alpha-2A adrenergic receptor|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Frequency in Caucasians 0.004 and in African-Americans 0.05; 40% increase in agonist-promoted Gi coupling.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Implicated in catechol agonist binding and receptor activation|||Implicated in ligand binding|||Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding.|||Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding.|||Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding.|||N-linked (GlcNAc...) asparagine|||No binding to yohimbine. Increase in adenylate cyclase activity.|||No change in binding affinity. eliminates guanine nucleotide-sensitive agonist binding.|||Omega-N-methylarginine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069080|||http://purl.uniprot.org/annotation/VAR_014957|||http://purl.uniprot.org/annotation/VAR_055908
http://togogenome.org/gene/9606:HYKK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU49                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Hydroxylysine kinase|||In dbSNP:4380026.|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326044|||http://purl.uniprot.org/annotation/VAR_082892|||http://purl.uniprot.org/annotation/VSP_032517|||http://purl.uniprot.org/annotation/VSP_032518|||http://purl.uniprot.org/annotation/VSP_032520
http://togogenome.org/gene/9606:DSG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32926                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cytoplasmic|||Desmoglein repeat 1|||Desmoglein repeat 2|||Desmoglein-3|||Extracellular|||Helical|||In ABOLM; unknown pathological significance; loss of expression in skin and mucosa.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003851|||http://purl.uniprot.org/annotation/PRO_0000003852|||http://purl.uniprot.org/annotation/VAR_055578|||http://purl.uniprot.org/annotation/VAR_059178|||http://purl.uniprot.org/annotation/VAR_085271
http://togogenome.org/gene/9606:GCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z322|||http://purl.uniprot.org/uniprot/H7BXD5|||http://purl.uniprot.org/uniprot/P28676                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Grancalcin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073721|||http://purl.uniprot.org/annotation/VAR_048657
http://togogenome.org/gene/9606:PPP1R16B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T49                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2.|||Phosphoserine|||Protein phosphatase 1 regulatory inhibitor subunit 16B|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine|||Strongly decreased interaction with EEF1A1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067043|||http://purl.uniprot.org/annotation/PRO_0000396710|||http://purl.uniprot.org/annotation/VSP_047508
http://togogenome.org/gene/9606:MSLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13421                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated serine|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Megakaryocyte-potentiating factor|||Mesothelin|||Mesothelin, cleaved form|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Removed in mature form|||Required for megakaryocyte-potentiating factor activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021769|||http://purl.uniprot.org/annotation/PRO_0000253559|||http://purl.uniprot.org/annotation/PRO_0000253560|||http://purl.uniprot.org/annotation/PRO_0000253561|||http://purl.uniprot.org/annotation/VAR_028381|||http://purl.uniprot.org/annotation/VAR_028382|||http://purl.uniprot.org/annotation/VAR_028383|||http://purl.uniprot.org/annotation/VAR_054012|||http://purl.uniprot.org/annotation/VSP_021058|||http://purl.uniprot.org/annotation/VSP_021059|||http://purl.uniprot.org/annotation/VSP_021060
http://togogenome.org/gene/9606:UBQLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMX0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with UBXN4|||N-acetylalanine|||Polar residues|||Removed|||STI1 1|||STI1 2|||STI1 3|||STI1 4|||UBA|||Ubiquilin-1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211008|||http://purl.uniprot.org/annotation/VSP_009787|||http://purl.uniprot.org/annotation/VSP_057689|||http://purl.uniprot.org/annotation/VSP_057690|||http://purl.uniprot.org/annotation/VSP_057691
http://togogenome.org/gene/9606:TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12270                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Basic and acidic residues|||Breakpoint for translocation to form TRK-T1|||Diminishes association to NPC but not homodimerization. Inhibits association to NPC, interaction with NUP153 and nuclear membrane localization but not homodimerization; when associated with P-458.|||Diminishes association to NPC but not homodimerization. Inhibits association to NPC, interaction with NUP153 and nuclear membrane localization but not homodimerization; when associated with P-489.|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Necessary for association to the NPC|||Necessary for interaction with HSF1|||Nucleoprotein TPR|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Sufficient and essential for mediating its nuclear import|||Sufficient for interaction with TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204920|||http://purl.uniprot.org/annotation/VAR_020429|||http://purl.uniprot.org/annotation/VAR_047289|||http://purl.uniprot.org/annotation/VAR_047290|||http://purl.uniprot.org/annotation/VSP_057406|||http://purl.uniprot.org/annotation/VSP_057407
http://togogenome.org/gene/9606:FAM110D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Protein FAM110D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318716|||http://purl.uniprot.org/annotation/VAR_038860
http://togogenome.org/gene/9606:C3orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUJ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Phosphoserine|||Uncharacterized protein C3orf62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239305|||http://purl.uniprot.org/annotation/VAR_050724
http://togogenome.org/gene/9606:CD3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0YIY4|||http://purl.uniprot.org/uniprot/P04234                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD3 gamma/delta subunit Ig-like|||Cytoplasmic|||Extracellular|||Helical|||ITAM|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||T-cell surface glycoprotein CD3 delta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016487|||http://purl.uniprot.org/annotation/PRO_5014298169|||http://purl.uniprot.org/annotation/VAR_049646|||http://purl.uniprot.org/annotation/VSP_045800
http://togogenome.org/gene/9606:ZBTB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15062|||http://purl.uniprot.org/uniprot/Q5T942                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047713|||http://purl.uniprot.org/annotation/VAR_052915
http://togogenome.org/gene/9606:RBM26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0H9|||http://purl.uniprot.org/uniprot/Q5T8P6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||C3H1-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||N6-acetyllysine|||Phosphoserine|||Pro residues|||RNA-binding protein 26|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273376|||http://purl.uniprot.org/annotation/VAR_030137|||http://purl.uniprot.org/annotation/VSP_022528|||http://purl.uniprot.org/annotation/VSP_022529|||http://purl.uniprot.org/annotation/VSP_022530|||http://purl.uniprot.org/annotation/VSP_022531|||http://purl.uniprot.org/annotation/VSP_022532
http://togogenome.org/gene/9606:NRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVG8|||http://purl.uniprot.org/uniprot/B9EGV5|||http://purl.uniprot.org/uniprot/P56975                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||Helical; Note=Internal signal sequence|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Neuregulin-3|||Polar residues|||Pro-neuregulin-3, membrane-bound isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019481|||http://purl.uniprot.org/annotation/PRO_0000019482|||http://purl.uniprot.org/annotation/VAR_047386|||http://purl.uniprot.org/annotation/VAR_047387|||http://purl.uniprot.org/annotation/VSP_021828|||http://purl.uniprot.org/annotation/VSP_021829|||http://purl.uniprot.org/annotation/VSP_021830|||http://purl.uniprot.org/annotation/VSP_035752
http://togogenome.org/gene/9606:CD300E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0V9|||http://purl.uniprot.org/uniprot/Q496F6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMRF35-like molecule 2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320123|||http://purl.uniprot.org/annotation/VAR_039129|||http://purl.uniprot.org/annotation/VAR_039130|||http://purl.uniprot.org/annotation/VAR_039131
http://togogenome.org/gene/9606:MAP2K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36507                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-acetylserine; by Yersinia YopJ; alternate|||Cleavage; by anthrax lethal factor|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 2|||In CFC4.|||In CFC4; results in increased kinase activity.|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by RAF; alternate|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086372|||http://purl.uniprot.org/annotation/VAR_035095|||http://purl.uniprot.org/annotation/VAR_069781|||http://purl.uniprot.org/annotation/VAR_069782|||http://purl.uniprot.org/annotation/VAR_069783
http://togogenome.org/gene/9606:ASB12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXK4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Ankyrin repeat and SOCS box protein 12|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066947|||http://purl.uniprot.org/annotation/VSP_044865
http://togogenome.org/gene/9606:CORO1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR76                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Coronin-1B|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine; by PKC|||Polar residues|||Stronger interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Enhanced ruffling in response to phorbol 12-myristate 13-acetate (PMA) and increased speed in fibroblasts.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||Weaker interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Attenuated PMA-induced ruffling and slower speed in fibroblasts.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050922|||http://purl.uniprot.org/annotation/VAR_035877|||http://purl.uniprot.org/annotation/VAR_053389
http://togogenome.org/gene/9606:NEDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1Z3|||http://purl.uniprot.org/uniprot/Q8NHV4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine; by CDK1|||Phosphothreonine; by PLK1|||Polar residues|||Protein NEDD1|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051095|||http://purl.uniprot.org/annotation/VSP_043411|||http://purl.uniprot.org/annotation/VSP_053794
http://togogenome.org/gene/9606:MEDAG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYS4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Mesenteric estrogen-dependent adipogenesis protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274333|||http://purl.uniprot.org/annotation/VAR_030261|||http://purl.uniprot.org/annotation/VSP_022714|||http://purl.uniprot.org/annotation/VSP_022715
http://togogenome.org/gene/9606:LTBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLY3|||http://purl.uniprot.org/uniprot/Q14766                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyasparagine|||8-Cys3 region|||Abolishes N-glycosylation at this site without affecting ability to interact with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1.|||Abolishes interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1; when associated with 1382-A--A-1385.|||Abolishes interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1; when associated with A-1348.|||C-terminal domain|||Cell attachment site|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17|||EGF-like 18; calcium-binding|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In ARCL2E; loss of interaction with FBN1 and FBN2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform Short, isoform 3 and isoform 5.|||Interchain (with C-33 in TGFB1); in linked form|||Latent-transforming growth factor beta-binding protein 1|||Loss of binding to TGFB1.|||N-linked (GlcNAc...) asparagine|||O-linked (Glc) serine|||Phosphoserine|||Phosphoserine; by FAM20C|||Polar residues|||Pro residues|||TB|||TB 1|||TB 2|||TB 3|||TB 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000184|||http://purl.uniprot.org/annotation/PRO_0000007635|||http://purl.uniprot.org/annotation/PRO_5002866951|||http://purl.uniprot.org/annotation/VAR_086071|||http://purl.uniprot.org/annotation/VAR_086072|||http://purl.uniprot.org/annotation/VSP_036963|||http://purl.uniprot.org/annotation/VSP_036964|||http://purl.uniprot.org/annotation/VSP_036965|||http://purl.uniprot.org/annotation/VSP_040125
http://togogenome.org/gene/9606:SIX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N196                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein SIX5|||In BOR2.|||In BOR2; affects Eya1 binding and the ability to activate gene transcription.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049305|||http://purl.uniprot.org/annotation/VAR_032941|||http://purl.uniprot.org/annotation/VAR_032942|||http://purl.uniprot.org/annotation/VAR_032943|||http://purl.uniprot.org/annotation/VAR_032944|||http://purl.uniprot.org/annotation/VAR_032945|||http://purl.uniprot.org/annotation/VAR_032946|||http://purl.uniprot.org/annotation/VAR_032947
http://togogenome.org/gene/9606:SRSF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z504|||http://purl.uniprot.org/uniprot/B3KNY6|||http://purl.uniprot.org/uniprot/O75494|||http://purl.uniprot.org/uniprot/Q5JRI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||RRM|||Serine/arginine-rich splicing factor 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081593|||http://purl.uniprot.org/annotation/VSP_010421|||http://purl.uniprot.org/annotation/VSP_010422|||http://purl.uniprot.org/annotation/VSP_010423|||http://purl.uniprot.org/annotation/VSP_010424|||http://purl.uniprot.org/annotation/VSP_010425|||http://purl.uniprot.org/annotation/VSP_043697|||http://purl.uniprot.org/annotation/VSP_043698
http://togogenome.org/gene/9606:TNFAIP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95379                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Tumor necrosis factor alpha-induced protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285718|||http://purl.uniprot.org/annotation/VAR_032047|||http://purl.uniprot.org/annotation/VSP_024898|||http://purl.uniprot.org/annotation/VSP_024899|||http://purl.uniprot.org/annotation/VSP_054827
http://togogenome.org/gene/9606:SBSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWP8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Suprabasin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317120|||http://purl.uniprot.org/annotation/VAR_069027|||http://purl.uniprot.org/annotation/VSP_044973
http://togogenome.org/gene/9606:LRRC43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N309                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Leucine-rich repeat-containing protein 43|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311908|||http://purl.uniprot.org/annotation/VAR_037338|||http://purl.uniprot.org/annotation/VAR_082884|||http://purl.uniprot.org/annotation/VSP_029636|||http://purl.uniprot.org/annotation/VSP_029637
http://togogenome.org/gene/9606:STAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGK3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Decrease in tyrosine phosphorylation.|||Disordered|||In isoform 2.|||Loss of tyrosine phosphorylation.|||PH|||Phosphotyrosine|||Phosphotyrosine; by PTK6|||Phosphotyrosine; by SRC|||Pro residues|||SH2|||Signal-transducing adaptor protein 2|||Small decrease in tyrosine phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072239|||http://purl.uniprot.org/annotation/VAR_055239|||http://purl.uniprot.org/annotation/VSP_041403
http://togogenome.org/gene/9606:RAB39A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14964                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine methyl ester|||Disrupts interaction with BECN1.|||Effector region|||Ras-related protein Rab-39A|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121253
http://togogenome.org/gene/9606:ACAD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKU7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In IBDD.|||In IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type.|||In IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity.|||In IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells.|||In isoform 2.|||In isoform 3.|||Isobutyryl-CoA dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000522|||http://purl.uniprot.org/annotation/VAR_035071|||http://purl.uniprot.org/annotation/VAR_035072|||http://purl.uniprot.org/annotation/VAR_035073|||http://purl.uniprot.org/annotation/VAR_035074|||http://purl.uniprot.org/annotation/VAR_035075|||http://purl.uniprot.org/annotation/VAR_035076|||http://purl.uniprot.org/annotation/VAR_035077|||http://purl.uniprot.org/annotation/VAR_035078|||http://purl.uniprot.org/annotation/VAR_035079|||http://purl.uniprot.org/annotation/VSP_055779|||http://purl.uniprot.org/annotation/VSP_055780|||http://purl.uniprot.org/annotation/VSP_055781|||http://purl.uniprot.org/annotation/VSP_055782
http://togogenome.org/gene/9606:BMPR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36894                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Affinity for BMP2 decreased by over 200-fold.|||Bone morphogenetic protein receptor type-1A|||Cytoplasmic|||Extracellular|||Found in a patient with tubular adenoma and rectal neuroendocrine tumor; unknown pathological significance.|||GS|||Helical|||In JPS.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||Mediates specificity for BMP ligand|||N-linked (GlcNAc...) asparagine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024410|||http://purl.uniprot.org/annotation/VAR_015533|||http://purl.uniprot.org/annotation/VAR_015534|||http://purl.uniprot.org/annotation/VAR_015535|||http://purl.uniprot.org/annotation/VAR_022828|||http://purl.uniprot.org/annotation/VAR_022829|||http://purl.uniprot.org/annotation/VAR_022830|||http://purl.uniprot.org/annotation/VAR_022831|||http://purl.uniprot.org/annotation/VAR_022832|||http://purl.uniprot.org/annotation/VAR_041397|||http://purl.uniprot.org/annotation/VAR_041398|||http://purl.uniprot.org/annotation/VAR_041399|||http://purl.uniprot.org/annotation/VAR_041400|||http://purl.uniprot.org/annotation/VAR_077353
http://togogenome.org/gene/9606:HIBADH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31937                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-hydroxyisobutyrate dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007158
http://togogenome.org/gene/9606:FRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42685                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Loss of ability to phosphorylate PTEN.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||SH3|||Tyrosine-protein kinase FRK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088097|||http://purl.uniprot.org/annotation/VAR_006283|||http://purl.uniprot.org/annotation/VAR_041702|||http://purl.uniprot.org/annotation/VAR_041703|||http://purl.uniprot.org/annotation/VSP_056496|||http://purl.uniprot.org/annotation/VSP_056497
http://togogenome.org/gene/9606:PER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV69|||http://purl.uniprot.org/uniprot/A2I2N5|||http://purl.uniprot.org/uniprot/P56645                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 18 AA tandem repeats of S-[HP]-[AP]-T-[AT]-[GST]-[ATV]-L-S-[MT]-G-[LS]-P-P-[MRS]-[EKR]-[NST]-P|||Associated with delayed sleep phase syndrome (DSPS).|||Associated with eveningness and better cognitive performance during sleep deprivation experiments.|||Basic and acidic residues|||CRY binding domain|||CSNK1E binding domain|||Disordered|||In FASPS3; decreased stability; decreased protein abundance.|||In isoform 2.|||Nuclear export signal 1|||Nuclear export signal 2|||Nuclear export signal 3|||Nuclear localization signal|||Only found in PER3.4 allele.|||PAC|||PAS|||PAS 1|||PAS 2|||Period circadian protein homolog 3|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000162633|||http://purl.uniprot.org/annotation/VAR_015514|||http://purl.uniprot.org/annotation/VAR_022428|||http://purl.uniprot.org/annotation/VAR_025532|||http://purl.uniprot.org/annotation/VAR_025533|||http://purl.uniprot.org/annotation/VAR_025534|||http://purl.uniprot.org/annotation/VAR_028728|||http://purl.uniprot.org/annotation/VAR_028729|||http://purl.uniprot.org/annotation/VAR_028730|||http://purl.uniprot.org/annotation/VAR_071049|||http://purl.uniprot.org/annotation/VAR_076416|||http://purl.uniprot.org/annotation/VAR_076417|||http://purl.uniprot.org/annotation/VAR_076418|||http://purl.uniprot.org/annotation/VSP_040326|||http://purl.uniprot.org/annotation/VSP_040327|||http://purl.uniprot.org/annotation/VSP_040328
http://togogenome.org/gene/9606:IL18RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95256                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to the preformed binary complex of IL18 and IL18R1. Impairs IL18 receptor signaling via NF-kappa-B; when associated with A-210 and A-214.|||Cytoplasmic|||Decreases binding to the preformed binary complex of IL18 and IL18R1.|||Decreases binding to the preformed binary complex of IL18 and IL18R1. Decreases IL18 receptor signaling via NF-kappa-B.|||Decreases binding to the preformed binary complex of IL18 and IL18R1. Impairs IL18 receptor signaling via NF-kappa-B; when associated with A-210 and A-212.|||Decreases binding to the preformed binary complex of IL18 and IL18R1. Impairs IL18 receptor signaling via NF-kappa-B; when associated with A-212 and A-214.|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Impairs IL18 receptor signaling via NF-kappa-B.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-18 receptor accessory protein|||N-linked (GlcNAc...) asparagine|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042185|||http://purl.uniprot.org/annotation/VAR_034005|||http://purl.uniprot.org/annotation/VSP_056295|||http://purl.uniprot.org/annotation/VSP_059114|||http://purl.uniprot.org/annotation/VSP_059115|||http://purl.uniprot.org/annotation/VSP_059116|||http://purl.uniprot.org/annotation/VSP_059117
http://togogenome.org/gene/9606:SLCO2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R5I4|||http://purl.uniprot.org/uniprot/A0A0A0MTF1|||http://purl.uniprot.org/uniprot/O94956                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased E1S transport, decreased cell surface expression; no change in Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.|||Decreased E1S transport, decreased cell surface expression; no change in Km value and decreased Vmax value. Decreased taurocholate transport.|||Decreased E1S transport, no change in cell surface expression, increased Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.|||Decreased E1S transport, no change in cell surface expression.|||Decreased E1S transport, no change in cell surface expression; increased Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.|||Decreased E1S transport, no change in cell surface expression; no change in Km value and decreased Vmax value for E1S transport activity. Decreased taurocholate transport.|||Decreased E1S transport.|||Decreased E1S transport; decreased cell surface expression.|||Decreased E1S transport; decreased cell surface expression. Strong decrease in cell surface expression; when associated with A-272 and A-276.|||Decreased E1S transport; decreased cell surface expression. Strong decrease in cell surface expression; when associated with A-272 and A-277.|||Decreased E1S transport; decreased cell surface expression. Strong decrease in cell surface expression; when associated with A-276 and A-277.|||Decreased E1S transport; decreased cell surface expression; no change in Km and Vmax values. Decreased taurocholate transport.|||Decreased E1S transport; no change in cell surface expression.|||Decreased high-affinity transport of E1S; no change in low-affinity transport of E1S.|||Decreased low- and high-affinity transport of E1S.|||Decreased low-affinity transport of E1S; no change in high affinity transport of E1S.|||Decreased low-affinity transport of E1S; no change in high-affinity transport of E1S.|||Disordered|||Essential for E1S and PGE2 transport activity and may interact with these substrates|||Essential for E1S transport activity and may interact with this substrate|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Implicated in high-affinity site for E1S transport|||Implicated in low-affinity site for E1S transport|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased high-affinity transport of E1S; decreased low-affinity transport of E1S.|||Increased low- and high-affinity transport of E1S.|||Kazal-like|||Loss of E1S transport; small decrease in cell surface expression. Strong decrease in low-affinity transport of E1S and loss of high-affinity transport of E1S. Decreased PGE2 transport.|||N-linked (GlcNAc...) asparagine|||No change in E1S transport.|||No change in E1S transport; decreased cell surface expression.|||No change in E1S transport; no change in cell surface expression.|||No change in low- and high-affinity transport of E1S.|||Phosphoserine|||Phosphothreonine|||Required for E1S and taurocholate transport; required for transporter stability|||Solute carrier organic anion transporter family member 2B1|||Strong decrease in high-affinity transport of E1S and lower Vmax/Km value; no change in low-affinity transport of E1S and higher Vmax/Km value. No change in PGE2 transport. Decreased in low- and high-affinity transport of E1S and lower Vmax/Km values; when associated with Q-579.|||Strong decrease in low-affinity and decreased in high-affinity transport of E1S; undetectable kinetic parameter for low-affinity and no change in Vmax/Km value for high-affinity transort. Increased PGE2 transport. Decreased in low- and high-affinity transport of E1S and lower Vmax/Km values; when associated with Q-618.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191061|||http://purl.uniprot.org/annotation/VAR_020294|||http://purl.uniprot.org/annotation/VAR_036412|||http://purl.uniprot.org/annotation/VAR_053675|||http://purl.uniprot.org/annotation/VAR_053676|||http://purl.uniprot.org/annotation/VAR_053677|||http://purl.uniprot.org/annotation/VSP_006147|||http://purl.uniprot.org/annotation/VSP_006148|||http://purl.uniprot.org/annotation/VSP_054109|||http://purl.uniprot.org/annotation/VSP_054110
http://togogenome.org/gene/9606:POLR1F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B726                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-directed RNA polymerase I subunit RPA43|||Disordered|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288632
http://togogenome.org/gene/9606:ZNF441                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8Z8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2; degenerate|||C2H2-type 3; degenerate|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 441                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047590|||http://purl.uniprot.org/annotation/VSP_039877
http://togogenome.org/gene/9606:TNFRSF12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP84                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Repeat|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||TNFR-Cys; atypical|||Tumor necrosis factor receptor superfamily member 12A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034611|||http://purl.uniprot.org/annotation/VSP_006519
http://togogenome.org/gene/9606:ETV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCT2|||http://purl.uniprot.org/uniprot/B7Z2C9|||http://purl.uniprot.org/uniprot/P50549                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ETS|||ETS translocation variant 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 4.|||Loss of phosphorylation by RPS6KA5.|||Phosphoserine|||Phosphoserine; by RPS6KA1 and RPS6KA5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204110|||http://purl.uniprot.org/annotation/VAR_048948|||http://purl.uniprot.org/annotation/VSP_001472|||http://purl.uniprot.org/annotation/VSP_043750|||http://purl.uniprot.org/annotation/VSP_043808|||http://purl.uniprot.org/annotation/VSP_043809
http://togogenome.org/gene/9606:ZNRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1B8|||http://purl.uniprot.org/uniprot/O60232                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphoserine|||Protein ZNRD2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072201|||http://purl.uniprot.org/annotation/VAR_051383
http://togogenome.org/gene/9606:CCKAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32238                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cholecystokinin receptor type A|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069223
http://togogenome.org/gene/9606:SYNDIG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7V2                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Phosphoserine|||Synapse differentiation-inducing gene protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135696|||http://purl.uniprot.org/annotation/VAR_053733
http://togogenome.org/gene/9606:ZPBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6X784                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Zona pellucida-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041601|||http://purl.uniprot.org/annotation/VAR_053747|||http://purl.uniprot.org/annotation/VAR_053748|||http://purl.uniprot.org/annotation/VAR_053749|||http://purl.uniprot.org/annotation/VAR_053750|||http://purl.uniprot.org/annotation/VAR_067003|||http://purl.uniprot.org/annotation/VSP_011683
http://togogenome.org/gene/9606:RAD52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2G8|||http://purl.uniprot.org/uniprot/B7Z5Q6|||http://purl.uniprot.org/uniprot/F5GX32|||http://purl.uniprot.org/uniprot/P43351|||http://purl.uniprot.org/uniprot/Q5DR82                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ssDNA-binding.|||Basic and acidic residues|||DNA repair protein RAD52 homolog|||Disordered|||In isoform beta.|||In isoform delta.|||In isoform gamma.|||Mediates interaction with RPA2|||Moderately defective in both ss and dsDNA-binding.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173881|||http://purl.uniprot.org/annotation/VAR_019218|||http://purl.uniprot.org/annotation/VAR_019219|||http://purl.uniprot.org/annotation/VAR_019220|||http://purl.uniprot.org/annotation/VSP_047749|||http://purl.uniprot.org/annotation/VSP_047750|||http://purl.uniprot.org/annotation/VSP_047751|||http://purl.uniprot.org/annotation/VSP_047752|||http://purl.uniprot.org/annotation/VSP_047753|||http://purl.uniprot.org/annotation/VSP_047754
http://togogenome.org/gene/9606:CRYGD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140CTX7|||http://purl.uniprot.org/uniprot/P07320                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Gamma-crystallin D|||In CTRCT4.|||In CTRCT4; lowered solubility; crystallizes easily.|||In CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation.|||In CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation.|||In CTRCT4; reduces solubility.|||In CTRCT4; unknown pathological significance.|||In CTRCT4; unknown pathological significance; reduces solubility.|||In CTRCT4; very low solubility; crystallizes spontaneously.|||No effect on solubility.|||Removed|||Slightly reduces solubility.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057588|||http://purl.uniprot.org/annotation/VAR_010733|||http://purl.uniprot.org/annotation/VAR_010734|||http://purl.uniprot.org/annotation/VAR_010735|||http://purl.uniprot.org/annotation/VAR_021145|||http://purl.uniprot.org/annotation/VAR_021146|||http://purl.uniprot.org/annotation/VAR_034955|||http://purl.uniprot.org/annotation/VAR_034956|||http://purl.uniprot.org/annotation/VAR_064829|||http://purl.uniprot.org/annotation/VAR_084800|||http://purl.uniprot.org/annotation/VAR_084801|||http://purl.uniprot.org/annotation/VAR_084802|||http://purl.uniprot.org/annotation/VAR_084803|||http://purl.uniprot.org/annotation/VAR_084804|||http://purl.uniprot.org/annotation/VAR_084805
http://togogenome.org/gene/9606:TSTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7W7                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cysteine persulfide intermediate|||Disordered|||In isoform 2.|||Phosphoserine|||Rhodanese|||Thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230673|||http://purl.uniprot.org/annotation/VAR_050842|||http://purl.uniprot.org/annotation/VAR_050843|||http://purl.uniprot.org/annotation/VSP_017825|||http://purl.uniprot.org/annotation/VSP_017826|||http://purl.uniprot.org/annotation/VSP_017827|||http://purl.uniprot.org/annotation/VSP_017828
http://togogenome.org/gene/9606:NPFF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15130                                                                                  ^@                                                                                  Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Neuropeptide AF|||Neuropeptide FF|||Neuropeptide SF|||Phenylalanine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009898|||http://purl.uniprot.org/annotation/PRO_0000009899|||http://purl.uniprot.org/annotation/PRO_0000009900|||http://purl.uniprot.org/annotation/PRO_0000009901|||http://purl.uniprot.org/annotation/PRO_0000009902|||http://purl.uniprot.org/annotation/VAR_049183|||http://purl.uniprot.org/annotation/VSP_056475
http://togogenome.org/gene/9606:LGALS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHV8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Strand|||Turn                                                                                  ^@                                                                                  Galactoside-binding soluble lectin 13|||Galectin|||Interchain (with C-136)|||Interchain (with C-138)|||Loss of homodimerization; when associated with S-136.|||Loss of homodimerization; when associated with S-138.|||No effect on its haemagglutinating activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076963
http://togogenome.org/gene/9606:XPOT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43592                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes binding to tRNA. Does not abolish shuttling behavior.|||Does not abolish binding to tRNA. Does not abolish shuttling behavior.|||Exportin-T|||N-acetylmethionine|||N6-acetyllysine|||Necessary for interaction with Ran, nuclear localization and nuclear import|||Necessary for tRNA-binding, cytoplasmic localization and nuclear export                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204716|||http://purl.uniprot.org/annotation/VAR_026528|||http://purl.uniprot.org/annotation/VAR_048962
http://togogenome.org/gene/9606:SP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXP2|||http://purl.uniprot.org/uniprot/Q3SY56                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In AI1K; decreased binding to the AMBN promoter; requires 2 nucleotide substitutions.|||In AI1K; requires 2 nucleotide substitutions.|||Polar residues|||Transcription factor Sp6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047148|||http://purl.uniprot.org/annotation/VAR_052714|||http://purl.uniprot.org/annotation/VAR_087744|||http://purl.uniprot.org/annotation/VAR_087745
http://togogenome.org/gene/9606:CNTRL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RP65|||http://purl.uniprot.org/uniprot/Q5JVD1|||http://purl.uniprot.org/uniprot/Q7Z7A1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form CEP110-FGFR1|||Centriolin|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||Phosphoserine|||Polar residues|||Required for centrosome localization|||Sufficient for interaction with HOOK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323675|||http://purl.uniprot.org/annotation/VAR_039559|||http://purl.uniprot.org/annotation/VAR_039560|||http://purl.uniprot.org/annotation/VAR_039561|||http://purl.uniprot.org/annotation/VAR_061622|||http://purl.uniprot.org/annotation/VSP_032046|||http://purl.uniprot.org/annotation/VSP_032047|||http://purl.uniprot.org/annotation/VSP_032048|||http://purl.uniprot.org/annotation/VSP_032049|||http://purl.uniprot.org/annotation/VSP_032050
http://togogenome.org/gene/9606:TRIM64C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLI5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||RING-type|||Tripartite motif-containing protein 64C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340248
http://togogenome.org/gene/9606:ALG1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J202                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Putative glycosyltransferase ALG1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393966
http://togogenome.org/gene/9606:ZNF630                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M218                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14; degenerate|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 630                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234603|||http://purl.uniprot.org/annotation/VSP_046855
http://togogenome.org/gene/9606:OXCT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R040|||http://purl.uniprot.org/uniprot/P55809                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  5-glutamyl coenzyme A thioester intermediate|||In SCOTD.|||In SCOTD; loss of activity.|||In SCOTD; partial loss of activity.|||In SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees.|||In SCOTD; unknown pathological significance.|||In isoform 2.|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial|||Succinyl-CoA:3-ketoacid-coenzyme A transferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002413|||http://purl.uniprot.org/annotation/PRO_5014214182|||http://purl.uniprot.org/annotation/VAR_000695|||http://purl.uniprot.org/annotation/VAR_000696|||http://purl.uniprot.org/annotation/VAR_000697|||http://purl.uniprot.org/annotation/VAR_010337|||http://purl.uniprot.org/annotation/VAR_010338|||http://purl.uniprot.org/annotation/VAR_010339|||http://purl.uniprot.org/annotation/VAR_065564|||http://purl.uniprot.org/annotation/VAR_065565|||http://purl.uniprot.org/annotation/VAR_065566|||http://purl.uniprot.org/annotation/VAR_065567|||http://purl.uniprot.org/annotation/VAR_065568|||http://purl.uniprot.org/annotation/VAR_065569|||http://purl.uniprot.org/annotation/VAR_085802|||http://purl.uniprot.org/annotation/VAR_085803|||http://purl.uniprot.org/annotation/VAR_085804|||http://purl.uniprot.org/annotation/VAR_085805|||http://purl.uniprot.org/annotation/VAR_085806|||http://purl.uniprot.org/annotation/VSP_056310
http://togogenome.org/gene/9606:ZFHX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15911|||http://purl.uniprot.org/uniprot/Q8N2Y6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 10; atypical|||C2H2-type 11; atypical|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19; atypical|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6; atypical|||C2H2-type 7; degenerate|||C2H2-type 8; atypical|||C2H2-type 9; atypical|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||In isoform B.|||Loss of nuclear localization.|||Loss of sumoylation.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Zinc finger homeobox protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046930|||http://purl.uniprot.org/annotation/VAR_011694|||http://purl.uniprot.org/annotation/VAR_011695|||http://purl.uniprot.org/annotation/VAR_011696|||http://purl.uniprot.org/annotation/VAR_019968|||http://purl.uniprot.org/annotation/VAR_026663|||http://purl.uniprot.org/annotation/VAR_026664|||http://purl.uniprot.org/annotation/VAR_026665|||http://purl.uniprot.org/annotation/VAR_026666|||http://purl.uniprot.org/annotation/VAR_052733|||http://purl.uniprot.org/annotation/VAR_061927|||http://purl.uniprot.org/annotation/VSP_006825
http://togogenome.org/gene/9606:HNRNPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL63|||http://purl.uniprot.org/uniprot/A0A7I2V2R3|||http://purl.uniprot.org/uniprot/B4DDB6|||http://purl.uniprot.org/uniprot/P51991                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Dimethylated arginine; alternate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein A3|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081838|||http://purl.uniprot.org/annotation/VSP_011418
http://togogenome.org/gene/9606:DEPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTK1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein DEPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079867|||http://purl.uniprot.org/annotation/VAR_050951
http://togogenome.org/gene/9606:BCAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KSK1|||http://purl.uniprot.org/uniprot/A0A8I5KUN3|||http://purl.uniprot.org/uniprot/B2RCQ5|||http://purl.uniprot.org/uniprot/G3XAF7|||http://purl.uniprot.org/uniprot/O75363|||http://purl.uniprot.org/uniprot/Q05CL3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Breast carcinoma-amplified sequence 1|||Disordered|||In isoform 2.|||Interacts with DYNLL1 and DYNLL2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064859|||http://purl.uniprot.org/annotation/VAR_024251|||http://purl.uniprot.org/annotation/VAR_026674|||http://purl.uniprot.org/annotation/VAR_026675|||http://purl.uniprot.org/annotation/VAR_026676|||http://purl.uniprot.org/annotation/VAR_050691|||http://purl.uniprot.org/annotation/VSP_018520|||http://purl.uniprot.org/annotation/VSP_018521|||http://purl.uniprot.org/annotation/VSP_018522|||http://purl.uniprot.org/annotation/VSP_018523
http://togogenome.org/gene/9606:LAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43561                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with GRB2 and PIK3R1; when associated with F-200.|||Abolishes interaction with GRB2 and PIK3R1; when associated with F-220.|||Abolishes interaction with PLCG1.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4 and isoform 5.|||Interaction with GRB2, GRAP2 and PIK3R1|||Interaction with PLCG1|||Linker for activation of T-cells family member 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Reduces palmitoylation; abolishes localization to lipid rafts.|||Reduces palmitoylation; impairs localization to lipid rafts.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083325|||http://purl.uniprot.org/annotation/VSP_004303|||http://purl.uniprot.org/annotation/VSP_054758|||http://purl.uniprot.org/annotation/VSP_054759
http://togogenome.org/gene/9606:PYCR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTV6|||http://purl.uniprot.org/uniprot/A0A0S2Z5U6|||http://purl.uniprot.org/uniprot/Q96C36                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In HLD10; mild decrease of homodimerization; does not affect mitochondrial localization.|||In HLD10; severe decrease of protein amount; does not affect mitochondrial localization.|||N-acetylserine|||Phosphoserine|||Pyrroline-5-carboxylate reductase 2|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Pyrroline-5-carboxylate reductase dimerisation|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187317|||http://purl.uniprot.org/annotation/VAR_074608|||http://purl.uniprot.org/annotation/VAR_074609
http://togogenome.org/gene/9606:TENM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIA3|||http://purl.uniprot.org/uniprot/F8VNQ3|||http://purl.uniprot.org/uniprot/G3V106|||http://purl.uniprot.org/uniprot/Q9NT68                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ten-2 intracellular domain|||Ten-2, soluble form|||Teneurin N-terminal|||Teneurin-2|||YD 1|||YD 10|||YD 11|||YD 12|||YD 13|||YD 14|||YD 15|||YD 16|||YD 17|||YD 18|||YD 19|||YD 2|||YD 20|||YD 21|||YD 22|||YD 23|||YD 3|||YD 4|||YD 5|||YD 6|||YD 7|||YD 8|||YD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259501|||http://purl.uniprot.org/annotation/PRO_0000421011|||http://purl.uniprot.org/annotation/PRO_0000421012|||http://purl.uniprot.org/annotation/VAR_028946|||http://purl.uniprot.org/annotation/VAR_060129|||http://purl.uniprot.org/annotation/VSP_045019|||http://purl.uniprot.org/annotation/VSP_045020|||http://purl.uniprot.org/annotation/VSP_045021|||http://purl.uniprot.org/annotation/VSP_045022
http://togogenome.org/gene/9606:MGAT4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NG13                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase-like protein MGAT4D|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311676
http://togogenome.org/gene/9606:ADO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXN9|||http://purl.uniprot.org/uniprot/Q96SZ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  2-aminoethanethiol dioxygenase|||3'-(S-cysteinyl)-tyrosine (Cys-Tyr)|||Disordered|||Moderate reduction in enzyme activity.|||No significant reduction in enzyme activity.|||Significant reduction in enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089784|||http://purl.uniprot.org/annotation/VAR_025333|||http://purl.uniprot.org/annotation/VAR_025334|||http://purl.uniprot.org/annotation/VAR_033691
http://togogenome.org/gene/9606:ARHGEF33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVX0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||Omega-N-methylarginine|||Polar residues|||Rho guanine nucleotide exchange factor 33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342343|||http://purl.uniprot.org/annotation/VSP_044905
http://togogenome.org/gene/9606:BLOC1S3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6QNY0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Biogenesis of lysosome-related organelles complex 1 subunit 3|||Disordered|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234548
http://togogenome.org/gene/9606:RHO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08100                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  'Ionic lock' involved in activated form stabilization|||Cytoplasmic|||Extracellular|||Found in a patient with retinitis pigmentosa; unknown pathological significance.|||Found in patients with pathologic myopia; unknown pathological significance.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CSNBAD1.|||In CSNBAD1; constitutive activity in the absence of bound retinal.|||In RP4.|||In RP4; autosomal recessive.|||In RP4; common variant.|||In RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system.|||Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Q-113.|||Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Y-257.|||Interaction with SAG|||Loss of phosphorylation sites and decreased interaction with SAG.|||Loss of phosphorylation sites and decreased interaction with SAG; when associated with 336-A--A-338.|||Loss of phosphorylation sites and decreased interaction with SAG; when associated with A-343.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||N6-(retinylidene)lysine|||Phosphoserine|||Phosphothreonine|||Plays an important role in the conformation switch to the active conformation|||Rhodopsin|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197677|||http://purl.uniprot.org/annotation/VAR_004765|||http://purl.uniprot.org/annotation/VAR_004766|||http://purl.uniprot.org/annotation/VAR_004767|||http://purl.uniprot.org/annotation/VAR_004768|||http://purl.uniprot.org/annotation/VAR_004769|||http://purl.uniprot.org/annotation/VAR_004770|||http://purl.uniprot.org/annotation/VAR_004771|||http://purl.uniprot.org/annotation/VAR_004772|||http://purl.uniprot.org/annotation/VAR_004773|||http://purl.uniprot.org/annotation/VAR_004774|||http://purl.uniprot.org/annotation/VAR_004775|||http://purl.uniprot.org/annotation/VAR_004776|||http://purl.uniprot.org/annotation/VAR_004777|||http://purl.uniprot.org/annotation/VAR_004778|||http://purl.uniprot.org/annotation/VAR_004779|||http://purl.uniprot.org/annotation/VAR_004780|||http://purl.uniprot.org/annotation/VAR_004781|||http://purl.uniprot.org/annotation/VAR_004782|||http://purl.uniprot.org/annotation/VAR_004783|||http://purl.uniprot.org/annotation/VAR_004784|||http://purl.uniprot.org/annotation/VAR_004785|||http://purl.uniprot.org/annotation/VAR_004786|||http://purl.uniprot.org/annotation/VAR_004787|||http://purl.uniprot.org/annotation/VAR_004788|||http://purl.uniprot.org/annotation/VAR_004789|||http://purl.uniprot.org/annotation/VAR_004790|||http://purl.uniprot.org/annotation/VAR_004791|||http://purl.uniprot.org/annotation/VAR_004792|||http://purl.uniprot.org/annotation/VAR_004793|||http://purl.uniprot.org/annotation/VAR_004794|||http://purl.uniprot.org/annotation/VAR_004795|||http://purl.uniprot.org/annotation/VAR_004796|||http://purl.uniprot.org/annotation/VAR_004797|||http://purl.uniprot.org/annotation/VAR_004798|||http://purl.uniprot.org/annotation/VAR_004799|||http://purl.uniprot.org/annotation/VAR_004800|||http://purl.uniprot.org/annotation/VAR_004801|||http://purl.uniprot.org/annotation/VAR_004802|||http://purl.uniprot.org/annotation/VAR_004803|||http://purl.uniprot.org/annotation/VAR_004804|||http://purl.uniprot.org/annotation/VAR_004805|||http://purl.uniprot.org/annotation/VAR_004806|||http://purl.uniprot.org/annotation/VAR_004807|||http://purl.uniprot.org/annotation/VAR_004808|||http://purl.uniprot.org/annotation/VAR_004809|||http://purl.uniprot.org/annotation/VAR_004810|||http://purl.uniprot.org/annotation/VAR_004811|||http://purl.uniprot.org/annotation/VAR_004812|||http://purl.uniprot.org/annotation/VAR_004813|||http://purl.uniprot.org/annotation/VAR_004814|||http://purl.uniprot.org/annotation/VAR_004815|||http://purl.uniprot.org/annotation/VAR_004816|||http://purl.uniprot.org/annotation/VAR_004817|||http://purl.uniprot.org/annotation/VAR_004818|||http://purl.uniprot.org/annotation/VAR_004819|||http://purl.uniprot.org/annotation/VAR_004820|||http://purl.uniprot.org/annotation/VAR_004821|||http://purl.uniprot.org/annotation/VAR_004822|||http://purl.uniprot.org/annotation/VAR_004823|||http://purl.uniprot.org/annotation/VAR_004824|||http://purl.uniprot.org/annotation/VAR_004825|||http://purl.uniprot.org/annotation/VAR_004826|||http://purl.uniprot.org/annotation/VAR_004827|||http://purl.uniprot.org/annotation/VAR_004828|||http://purl.uniprot.org/annotation/VAR_004829|||http://purl.uniprot.org/annotation/VAR_004830|||http://purl.uniprot.org/annotation/VAR_004831|||http://purl.uniprot.org/annotation/VAR_004832|||http://purl.uniprot.org/annotation/VAR_004833|||http://purl.uniprot.org/annotation/VAR_004834|||http://purl.uniprot.org/annotation/VAR_004835|||http://purl.uniprot.org/annotation/VAR_004836|||http://purl.uniprot.org/annotation/VAR_004837|||http://purl.uniprot.org/annotation/VAR_068359|||http://purl.uniprot.org/annotation/VAR_068360
http://togogenome.org/gene/9606:SOX21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y651                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  HMG box|||Transcription factor SOX-21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048770|||http://purl.uniprot.org/annotation/VAR_049562
http://togogenome.org/gene/9606:GOLIM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W785|||http://purl.uniprot.org/uniprot/O00461                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Endosome targeting|||Golgi integral membrane protein 4|||Golgi targeting|||Helical|||Helical; Signal-anchor for type II membrane protein|||In a breast cancer sample; somatic mutation.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285097|||http://purl.uniprot.org/annotation/VAR_036611
http://togogenome.org/gene/9606:DNAJB9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FIF1|||http://purl.uniprot.org/uniprot/Q9UBS3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Divergent targeting domain|||DnaJ homolog subfamily B member 9|||J|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071031|||http://purl.uniprot.org/annotation/PRO_5014310433|||http://purl.uniprot.org/annotation/VAR_048911
http://togogenome.org/gene/9606:CSAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PB30                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chondrosarcoma-associated gene 1 protein|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291848|||http://purl.uniprot.org/annotation/VAR_032868|||http://purl.uniprot.org/annotation/VAR_047336|||http://purl.uniprot.org/annotation/VSP_026267
http://togogenome.org/gene/9606:FANCM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATPase activity. Loss of DNA branch migration activity, even in the presence of CENPS/CENPX. Loss of cross-linker resistance. No effect on FAAP24-binding, nor on FANCD2 and FANCI monoubiquitination.|||Acidic residues|||Basic and acidic residues|||DEAH box|||Disordered|||Fanconi anemia group M protein|||Helicase ATP-binding|||Helicase C-terminal|||In POF15 and SPGF28; loss-of-function mutation resulting in impaired FANCD2 monoubiquitination in response to DNA damage.|||In SPGF28; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Interaction with CENPS/CENPSX|||Interaction with FAAP24|||Phosphoserine|||Polar residues|||Reduces ATPase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055176|||http://purl.uniprot.org/annotation/VAR_023697|||http://purl.uniprot.org/annotation/VAR_023698|||http://purl.uniprot.org/annotation/VAR_023699|||http://purl.uniprot.org/annotation/VAR_061827|||http://purl.uniprot.org/annotation/VAR_081138|||http://purl.uniprot.org/annotation/VAR_081139|||http://purl.uniprot.org/annotation/VSP_015989|||http://purl.uniprot.org/annotation/VSP_015990|||http://purl.uniprot.org/annotation/VSP_054504
http://togogenome.org/gene/9606:POP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75817                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Ribonuclease P protein subunit p20|||Strongly reduced interaction with RPP25.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058518
http://togogenome.org/gene/9606:GRINA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z429                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Pro residues|||Protein lifeguard 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314439|||http://purl.uniprot.org/annotation/VAR_037875
http://togogenome.org/gene/9606:TMPRSS11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T26                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 11B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299319|||http://purl.uniprot.org/annotation/VAR_034798|||http://purl.uniprot.org/annotation/VAR_034799|||http://purl.uniprot.org/annotation/VAR_047675
http://togogenome.org/gene/9606:SNAP47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0B7|||http://purl.uniprot.org/uniprot/Q5SQN1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Synaptosomal-associated protein 47|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology 1|||t-SNARE coiled-coil homology 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307151|||http://purl.uniprot.org/annotation/VAR_035367|||http://purl.uniprot.org/annotation/VAR_035368|||http://purl.uniprot.org/annotation/VAR_035369|||http://purl.uniprot.org/annotation/VAR_035370|||http://purl.uniprot.org/annotation/VSP_028613|||http://purl.uniprot.org/annotation/VSP_028614
http://togogenome.org/gene/9606:CHI3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15782                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chitinase-3-like protein 2|||Confers chitinase activity; when associated with D-143.|||Confers chitinase activity; when associated with E-145.|||GH18|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011969|||http://purl.uniprot.org/annotation/VAR_033731|||http://purl.uniprot.org/annotation/VAR_049198|||http://purl.uniprot.org/annotation/VAR_061189|||http://purl.uniprot.org/annotation/VSP_044262|||http://purl.uniprot.org/annotation/VSP_047245
http://togogenome.org/gene/9606:PEBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30086                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Hippocampal cholinergic neurostimulating peptide|||Interaction with RAF1|||Phosphatidylethanolamine-binding protein 1|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023271|||http://purl.uniprot.org/annotation/PRO_0000023272|||http://purl.uniprot.org/annotation/VAR_006048
http://togogenome.org/gene/9606:SARM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05B42|||http://purl.uniprot.org/uniprot/Q0D2N8|||http://purl.uniprot.org/uniprot/Q6SZW1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Abolished NAD(+) hydrolase activity.|||Abolished ability to promote axonal degeneration following injury.|||Constitutively active mutant; strong ability to trigger axonal degeneration caused by disrupted interaction between the TIR domain and ARM repeats.|||Decreased phosphorylation, leading to reduced NAD(+) hydrolase activity.|||Disordered|||Does not affect ability to promote axonal degeneration following injury.|||Does not affect phosphorylation level.|||Dominant negative mutant that blocks axon degeneration after axotomy.|||In RRK to A mutant: Slightly reduced NAD(+)-binding to ARM repeats; when associated with A-110 and A-157.|||In RRK to A mutant: Slightly reduced NAD(+)-binding to ARM repeats; when associated with A-110 and A-193.|||In RRK to A mutant: Slightly reduced NAD(+)-binding to ARM repeats; when associated with A-157 and A-193.|||In RRK to E mutant: Strongly reduced NAD(+)-binding to ARM repeats, leading to enhanced NAD(+) hydrolase activity and constitutive axonal degeneration in absence of injury; when associated with E-110 and A-193.|||In RRK to E mutant: Strongly reduced NAD(+)-binding to ARM repeats, leading to enhanced NAD(+) hydrolase activity and constitutive axonal degeneration in absence of injury; when associated with E-110 and E-157.|||In RRK to E mutant: Strongly reduced NAD(+)-binding to ARM repeats, leading to enhanced NAD(+) hydrolase activity and constitutive axonal degeneration in absence of injury; when associated with E-157 and A-193.|||In WQH to A mutant: Increased NAD(+)-binding to ARM repeats, leading to decreased NAD(+) hydrolase activity; when associated with A-103 and A-150.|||In WQH to A mutant: Increased NAD(+)-binding to ARM repeats, leading to decreased NAD(+) hydrolase activity; when associated with A-103 and A-190.|||In WQH to A mutant: Increased NAD(+)-binding to ARM repeats, leading to decreased NAD(+) hydrolase activity; when associated with A-150 and A-190.|||In isoform 2.|||Loss in ability to localize to mitochondria and reduction in apoptotic activity.|||Loss of NAD(+) hydrolase activity.|||Loss of NAD(+) hydrolase activity. Abolished ability to promote axonal degeneration following injury.|||Mitochondrion|||NAD(+) hydrolase SARM1|||No effect on mitochondrial localization.|||No effect on octamer formation. Shows increased NAD(+) hydrolase activity and ability to trigger axonal degeneration.|||No effect on octamer formation; does not affect NAD(+) hydrolase activity.|||Phosphoserine|||Reduced NAD(+) hydrolase activity.|||Reduced ability to form an octameric ring and promote axonal degeneration following injury.|||SAM|||SAM 1|||SAM 2|||Slightly reduced ability to form an octameric ring and promote axonal degeneration following injury.|||Strongly reduced ability to form an octameric ring and promote axonal degeneration following injury.|||TIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097589|||http://purl.uniprot.org/annotation/VAR_061702|||http://purl.uniprot.org/annotation/VSP_013603
http://togogenome.org/gene/9606:RAP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61224                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2-fold reduction in RAP1GAP-stimulated GTPase activity.|||25-fold reduction in RAP1GAP-stimulated GTPase activity.|||ADP-ribosylserine; by botulinum toxin|||Abolishes complex formation with RAP1GAP. Loss GTPase activity.|||Abolishes phosphorylation by PKA.|||Constitutively activated.|||Cysteine methyl ester|||Effector region|||Impairs interaction with KRIT1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with KRIT1|||Phosphoserine; by PKA|||Ras-related protein Rap-1b|||Removed in mature form|||S-geranylgeranyl cysteine|||Strong reduction in nucleotide exchange with EPAC2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030209|||http://purl.uniprot.org/annotation/PRO_0000030210|||http://purl.uniprot.org/annotation/VSP_045303|||http://purl.uniprot.org/annotation/VSP_045304|||http://purl.uniprot.org/annotation/VSP_045305
http://togogenome.org/gene/9606:USP17L12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JPN9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421088
http://togogenome.org/gene/9606:CDPF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NVV7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cysteine-rich DPF motif domain-containing protein 1|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341360|||http://purl.uniprot.org/annotation/VAR_044058|||http://purl.uniprot.org/annotation/VAR_062237
http://togogenome.org/gene/9606:DTNBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYP9|||http://purl.uniprot.org/uniprot/A0A0S2Z5U8|||http://purl.uniprot.org/uniprot/A6NFV8|||http://purl.uniprot.org/uniprot/D6RJC6|||http://purl.uniprot.org/uniprot/Q96EV8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes cytoplasmic location. Increased expression of SYN1.|||Disordered|||Dysbindin|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Phosphoserine|||Polar residues|||Reduced interaction with AP3M1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191001|||http://purl.uniprot.org/annotation/VAR_029644|||http://purl.uniprot.org/annotation/VAR_053069|||http://purl.uniprot.org/annotation/VSP_009023|||http://purl.uniprot.org/annotation/VSP_046062
http://togogenome.org/gene/9606:ZNF135                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLZ7|||http://purl.uniprot.org/uniprot/P52742|||http://purl.uniprot.org/uniprot/Q8N9M3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||KRAB|||Zinc finger protein 135                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047419|||http://purl.uniprot.org/annotation/VAR_052774|||http://purl.uniprot.org/annotation/VAR_052775|||http://purl.uniprot.org/annotation/VAR_052776|||http://purl.uniprot.org/annotation/VAR_052777|||http://purl.uniprot.org/annotation/VAR_052778|||http://purl.uniprot.org/annotation/VSP_046073|||http://purl.uniprot.org/annotation/VSP_046074|||http://purl.uniprot.org/annotation/VSP_046706
http://togogenome.org/gene/9606:C15orf61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNL5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Uncharacterized protein C15orf61                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332740
http://togogenome.org/gene/9606:NEK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8K8|||http://purl.uniprot.org/uniprot/Q8TDX7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-fold increase in catalytic activity.|||Abolished interaction with NEK9 and subsequent activation of NEK7 kinase activity.|||Abolished phosphorylation with NEK9 and protein kinase activity.|||Autoinhibitory|||Decreased interaction with NEK9 and subsequent activation of NEK7 kinase activity.|||Decreased interaction with NLRP3.|||Disordered|||Does not affect interaction with NEK9.|||Does not affect interaction with NLRP3.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Moderate increase in catalytic activity.|||N-acetylmethionine|||NTE motif|||Phosphoserine|||Phosphoserine; by NEK9|||Protein kinase|||Proton acceptor|||Reduced protein kinase activity.|||Serine/threonine-protein kinase Nek7|||Significant decrease in catalytic activity.|||Significant decrease in catalytic activity; when associated with A-28.|||Significant decrease in catalytic activity; when associated with A-31.|||Strongly increased protein kinase activity.|||Strongly reduced protein kinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086430|||http://purl.uniprot.org/annotation/VAR_040924|||http://purl.uniprot.org/annotation/VAR_040925|||http://purl.uniprot.org/annotation/VSP_041243|||http://purl.uniprot.org/annotation/VSP_041244
http://togogenome.org/gene/9606:PRKCQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q04759                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||C2|||Constitutively active form.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of function in T-cells proliferation. No effect on kinase activity.|||Loss of kinase activity.|||Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity.|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphothreonine; by PDPK1|||Phosphothreonine; by autocatalysis|||Phosphotyrosine; by LCK|||Protein kinase|||Protein kinase C theta type|||Proton acceptor|||Reduction in kinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055708|||http://purl.uniprot.org/annotation/VAR_020401|||http://purl.uniprot.org/annotation/VAR_042319|||http://purl.uniprot.org/annotation/VAR_042320|||http://purl.uniprot.org/annotation/VAR_042321|||http://purl.uniprot.org/annotation/VSP_017294|||http://purl.uniprot.org/annotation/VSP_054550
http://togogenome.org/gene/9606:CRYBB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53674                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-crystallin B1|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||C-terminal arm|||Connecting peptide|||Disordered|||In CTRCT17.|||In CTRCT17; unknown pathological significance.|||N-acetylserine|||N-terminal arm|||Probable disease-associated variant found in a family with autosomal dominant congenital cataract and microcornea; significantly decreased thermal stability of CRYBB1/CRYBA1-crystallin heteromer but not CRYBB1-crystallin homomer.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057550|||http://purl.uniprot.org/annotation/VAR_065296|||http://purl.uniprot.org/annotation/VAR_070030|||http://purl.uniprot.org/annotation/VAR_084783|||http://purl.uniprot.org/annotation/VAR_084784|||http://purl.uniprot.org/annotation/VAR_084785|||http://purl.uniprot.org/annotation/VAR_084786
http://togogenome.org/gene/9606:NPSR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Z1|||http://purl.uniprot.org/uniprot/Q6W5P4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Increases cell surface expression and NPS-dependent calcium mobilization; does not affect affinity for NPS..|||N-linked (GlcNAc...) asparagine|||Neuropeptide S receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069639|||http://purl.uniprot.org/annotation/VAR_023757|||http://purl.uniprot.org/annotation/VAR_023758|||http://purl.uniprot.org/annotation/VAR_023759|||http://purl.uniprot.org/annotation/VAR_025103|||http://purl.uniprot.org/annotation/VAR_025104|||http://purl.uniprot.org/annotation/VAR_025105|||http://purl.uniprot.org/annotation/VAR_025106|||http://purl.uniprot.org/annotation/VAR_025107|||http://purl.uniprot.org/annotation/VSP_016078|||http://purl.uniprot.org/annotation/VSP_016079|||http://purl.uniprot.org/annotation/VSP_016080|||http://purl.uniprot.org/annotation/VSP_016081|||http://purl.uniprot.org/annotation/VSP_016082|||http://purl.uniprot.org/annotation/VSP_016083|||http://purl.uniprot.org/annotation/VSP_016084|||http://purl.uniprot.org/annotation/VSP_016085|||http://purl.uniprot.org/annotation/VSP_016086|||http://purl.uniprot.org/annotation/VSP_016087|||http://purl.uniprot.org/annotation/VSP_016088|||http://purl.uniprot.org/annotation/VSP_016089
http://togogenome.org/gene/9606:JAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K910|||http://purl.uniprot.org/uniprot/B4DYV1|||http://purl.uniprot.org/uniprot/O60674                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form PCM1-JAK2 fusion protein|||FERM|||In AML.|||In PV, THCYT3 and AML; associated with susceptibility to Budd-Chiari syndrome; somatic mutation in a high percentage of patients with essential thrombocythemia or myelofibrosis; leads to constitutive tyrosine phosphorylation activity that promotes cytokine hypersensitivity.|||In THCYT3.|||In an ovarian serous carcinoma sample; somatic mutation.|||In myeloproliferative disorder with erythrocytosis.|||In myeloproliferative disorder with erythrocytosis; requires 2 nucleotide substitutions.|||Interaction with cytokine/interferon/growth hormone receptors|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||SH2|||SH2; atypical|||Tyrosine-protein kinase JAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088112|||http://purl.uniprot.org/annotation/VAR_032693|||http://purl.uniprot.org/annotation/VAR_032694|||http://purl.uniprot.org/annotation/VAR_032695|||http://purl.uniprot.org/annotation/VAR_032696|||http://purl.uniprot.org/annotation/VAR_032697|||http://purl.uniprot.org/annotation/VAR_041716|||http://purl.uniprot.org/annotation/VAR_041717|||http://purl.uniprot.org/annotation/VAR_041718|||http://purl.uniprot.org/annotation/VAR_041719|||http://purl.uniprot.org/annotation/VAR_041720|||http://purl.uniprot.org/annotation/VAR_041721|||http://purl.uniprot.org/annotation/VAR_043129|||http://purl.uniprot.org/annotation/VAR_067534
http://togogenome.org/gene/9606:LRRC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBW1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In a colorectal cancer sample; somatic mutation.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014833|||http://purl.uniprot.org/annotation/VAR_035519
http://togogenome.org/gene/9606:ZNF410                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FM1|||http://purl.uniprot.org/uniprot/Q86VK4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Polar residues|||Zinc finger protein 410                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047571|||http://purl.uniprot.org/annotation/VSP_008485|||http://purl.uniprot.org/annotation/VSP_008486|||http://purl.uniprot.org/annotation/VSP_008487|||http://purl.uniprot.org/annotation/VSP_042424|||http://purl.uniprot.org/annotation/VSP_043417|||http://purl.uniprot.org/annotation/VSP_043418
http://togogenome.org/gene/9606:LAPTM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13571|||http://purl.uniprot.org/uniprot/Q5TBB8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Lysosomal-associated transmembrane protein 5|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084357|||http://purl.uniprot.org/annotation/VAR_053653
http://togogenome.org/gene/9606:FAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14517                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 28|||Cadherin 29|||Cadherin 3|||Cadherin 30|||Cadherin 31|||Cadherin 32|||Cadherin 33|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5; calcium-binding|||Extracellular|||Found in a patient with spinocerebellar ataxia; unknown pathological significance.|||Helical|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||PTB-like motif|||Polar residues|||Pro residues|||Protocadherin Fat 1|||Protocadherin Fat 1, nuclear form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004017|||http://purl.uniprot.org/annotation/PRO_0000408559|||http://purl.uniprot.org/annotation/VAR_055590|||http://purl.uniprot.org/annotation/VAR_055591|||http://purl.uniprot.org/annotation/VAR_055592|||http://purl.uniprot.org/annotation/VAR_055593|||http://purl.uniprot.org/annotation/VAR_055594|||http://purl.uniprot.org/annotation/VAR_076441|||http://purl.uniprot.org/annotation/VAR_076442|||http://purl.uniprot.org/annotation/VAR_076443|||http://purl.uniprot.org/annotation/VAR_080732|||http://purl.uniprot.org/annotation/VAR_080733|||http://purl.uniprot.org/annotation/VAR_080734|||http://purl.uniprot.org/annotation/VAR_080735
http://togogenome.org/gene/9606:CDKL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX41|||http://purl.uniprot.org/uniprot/Q8IVW4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclin-dependent kinase-like 3|||Disordered|||In isoform 2.|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085820|||http://purl.uniprot.org/annotation/VAR_041991|||http://purl.uniprot.org/annotation/VSP_016148
http://togogenome.org/gene/9606:AMOT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VCS5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Angiomotin|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PDZ-binding|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190668|||http://purl.uniprot.org/annotation/VSP_015709
http://togogenome.org/gene/9606:GJA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IBV8|||http://purl.uniprot.org/uniprot/P57773                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Connexin N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-9 protein|||Gap junction protein cysteine-rich|||Helical|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057840|||http://purl.uniprot.org/annotation/VAR_019392|||http://purl.uniprot.org/annotation/VSP_035808
http://togogenome.org/gene/9606:PABPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11940                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Binding to HRSV M2-1 protein|||Asymmetric dimethylarginine; alternate|||CSDE1-binding|||Dimethylated arginine; alternate|||Greatly reduces methylation by CARM1 (in vitro); when associated with A-455.|||Greatly reduces methylation by CARM1 (in vitro); when associated with A-460.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||N6-methyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Omega-N-methylated arginine; by CARM1; partial|||PABC|||Phosphoserine|||Phosphothreonine|||Polyadenylate-binding protein 1|||RRM 1|||RRM 2|||RRM 3|||RRM 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081698|||http://purl.uniprot.org/annotation/VSP_009846
http://togogenome.org/gene/9606:PPIAL4E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B759|||http://purl.uniprot.org/uniprot/P0DN26                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase A-like 4E|||Peptidyl-prolyl cis-trans isomerase A-like 4F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433925|||http://purl.uniprot.org/annotation/PRO_0000433926
http://togogenome.org/gene/9606:TMED3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKD1|||http://purl.uniprot.org/uniprot/B4E277|||http://purl.uniprot.org/uniprot/F5H4M7|||http://purl.uniprot.org/uniprot/Q9Y3Q3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Disordered|||GOLD|||Helical|||In isoform 2.|||Lumenal|||Transmembrane emp24 domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010384|||http://purl.uniprot.org/annotation/PRO_5002803482|||http://purl.uniprot.org/annotation/PRO_5003323076|||http://purl.uniprot.org/annotation/PRO_5014247023|||http://purl.uniprot.org/annotation/VAR_049110|||http://purl.uniprot.org/annotation/VSP_044371
http://togogenome.org/gene/9606:AAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y312                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylalanine|||Protein AAR2 homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209706|||http://purl.uniprot.org/annotation/VAR_048127
http://togogenome.org/gene/9606:RPLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05386                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Large ribosomal subunit protein P1|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157686|||http://purl.uniprot.org/annotation/VSP_045244
http://togogenome.org/gene/9606:BDKRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46663                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  B1 bradykinin receptor|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069181|||http://purl.uniprot.org/annotation/VAR_014359|||http://purl.uniprot.org/annotation/VAR_049376
http://togogenome.org/gene/9606:PRAMEF25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGN4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348940
http://togogenome.org/gene/9606:AHCYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0A8|||http://purl.uniprot.org/uniprot/O43865                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ITPR1. Highly decreases phosphorylation. Abolishes interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3; when associated with A-68 and A-74.|||Abolishes interaction with ITPR1. Slightly decreases phosphorylation. Strongly decreases interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3; when associated with A-68 and A-71.|||Disordered|||Highly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1.|||Highly decreases interaction with ITPR1. Slightly decreases phosphorylation. Strongly decreases interaction with SLC4A4. Abolishes interaction with FIP1L1.|||Highly decreases interaction with ITPR1. Slightly increases phosphorylation. No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1.|||Highly decreases phosphorylation. Abolishes interaction with ITPR1. No effect on interaction with BCL2L10. Marked decrease in interaction of BCL2L10 with ITPR1. Decreased ability of BCL2L10 to reduce ITPR1-mediated calcium release and to prevent apoptosis. No effect on formation of multimers. Abolishes interaction with SLC4A4. Abolishes interaction with FIP1L1. Highly decreases interaction with SLC9A3. Highly decreases interaction with SLC9A3; when associated with A-71 and A-74.|||In isoform 2.|||Interaction with BCL2L10|||N-acetylmethionine|||N-acetylserine|||N6-acetyllysine|||NAD binding|||No effect on interaction with ITPR1. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1.|||No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1.|||No effect on interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. No effect on interaction with FIP1L1.|||No effect on interaction with SLC4A4.|||No effect on interaction with SLC4A4. Highly decreases interaction with FIP1L1.|||No effect on interaction with SLC4A4. No effect on interaction with FIP1L1.|||PDZ-binding|||PEST|||Phosphoserine|||Polar residues|||Removed|||S-adenosyl-L-homocysteine hydrolase NAD binding|||S-adenosylhomocysteine hydrolase-like protein 1|||Slightly decreases interaction with ITPR1. No effect on phosphorylation. No effect on interaction with SLC4A4. Decreases interaction with FIP1L1.|||Slightly decreases interaction with ITPR1. Slightly decreases phosphorylation. No effect on interaction with SLC4A4. Abolishes interaction with FIP1L1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116908|||http://purl.uniprot.org/annotation/VSP_021751
http://togogenome.org/gene/9606:GTPBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z563|||http://purl.uniprot.org/uniprot/Q969Y2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  GTP-binding protein TrmE N-terminal|||In COXPD23.|||In COXPD23; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||TrmE-type G|||tRNA modification GTPase GTPBP3, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280265|||http://purl.uniprot.org/annotation/VAR_031103|||http://purl.uniprot.org/annotation/VAR_031104|||http://purl.uniprot.org/annotation/VAR_073298|||http://purl.uniprot.org/annotation/VAR_073299|||http://purl.uniprot.org/annotation/VAR_073300|||http://purl.uniprot.org/annotation/VAR_073301|||http://purl.uniprot.org/annotation/VAR_073302|||http://purl.uniprot.org/annotation/VAR_073303|||http://purl.uniprot.org/annotation/VAR_073304|||http://purl.uniprot.org/annotation/VAR_073305|||http://purl.uniprot.org/annotation/VAR_073306|||http://purl.uniprot.org/annotation/VAR_073307|||http://purl.uniprot.org/annotation/VAR_073308|||http://purl.uniprot.org/annotation/VSP_023583|||http://purl.uniprot.org/annotation/VSP_023584|||http://purl.uniprot.org/annotation/VSP_045050
http://togogenome.org/gene/9606:CYTH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99418                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-terminal autoinhibitory region|||Cytohesin-2|||Does not reduce ARL4DGTP-dependent interaction but inhibits targeting to the plasma membrane mediated by ARL4C, ARL4C and ARL4D.|||In isoform 2.|||Inhibits GTPGDP exchange activity. Abolishes recruitment of ARF6 to the plasma membrane.|||PH|||Reduces ARL4DGTP-dependent interaction and targeting to the plasma membrane mediated by ARL4C, ARL4C and ARL4D.|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120197|||http://purl.uniprot.org/annotation/VSP_006036
http://togogenome.org/gene/9606:U2AF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01081|||http://purl.uniprot.org/uniprot/Q7Z780                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Decreases affinity for UAF2 by 3 orders of magnitude.|||Disordered|||In MDS; somatic mutation; affects alternative splicing of target sequences resulting in increased splicing efficiency, exon skipping and alternative splice site utilization; no effect on localization to nuclear speckles.|||In MDS; somatic mutation; affects alternative splicing of target sequences.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed|||Splicing factor U2AF 35 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081994|||http://purl.uniprot.org/annotation/VAR_079637|||http://purl.uniprot.org/annotation/VAR_079638|||http://purl.uniprot.org/annotation/VAR_079639|||http://purl.uniprot.org/annotation/VSP_042664|||http://purl.uniprot.org/annotation/VSP_042665|||http://purl.uniprot.org/annotation/VSP_042666|||http://purl.uniprot.org/annotation/VSP_042667
http://togogenome.org/gene/9606:COL9A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14055                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine|||Collagen alpha-2(IX) chain|||Disordered|||In IDD; requires 2 nucleotide substitutions.|||Interchain|||Nonhelical region 1 (NC1)|||Nonhelical region 2 (NC2)|||Nonhelical region 3 (NC3)|||Nonhelical region 4 (NC4)|||O-linked (Gal...) hydroxylysine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Pro residues|||Triple-helical region 1 (COL1)|||Triple-helical region 2 (COL2)|||Triple-helical region 3 (COL3)|||Triple-helical region 4 (COL4)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005837|||http://purl.uniprot.org/annotation/VAR_012658|||http://purl.uniprot.org/annotation/VAR_012659|||http://purl.uniprot.org/annotation/VAR_020014|||http://purl.uniprot.org/annotation/VAR_026465|||http://purl.uniprot.org/annotation/VAR_026466|||http://purl.uniprot.org/annotation/VAR_079749
http://togogenome.org/gene/9606:APTX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2E3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes DNA-binding and enzyme activity; when associated with A-333.|||Abolishes DNA-binding and enzyme activity; when associated with A-336.|||Abolishes enzyme activity.|||Aprataxin|||Basic and acidic residues|||C2H2-type|||Disordered|||FHA-like|||HIT|||Histidine triad motif|||Impairs interaction with MDC1 and localization at sites of DNA double-strand breaks.|||Impairs interaction with XRCC1 and XRCC4. Abolishes localization at sites of DNA double-strand breaks. Loss of interaction with MDC1.|||In AOA.|||In AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A.|||In AOA; heterozygous.|||In AOA; impairs binding to adenosine-5'-diphospho-5'-(DNA) and deadenylation activity.|||In isoform 12.|||In isoform 13.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 10.|||In isoform 5, isoform 7, isoform 9, isoform 12 and isoform 13.|||In isoform 6, isoform 9 and isoform 11.|||In isoform 6.|||In isoform 8.|||Interaction with DNA substrate|||Interactions with ADPRT/PARP1 and NCL|||Nuclear localization signal|||Phosphoserine|||Tele-AMP-histidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109838|||http://purl.uniprot.org/annotation/VAR_018794|||http://purl.uniprot.org/annotation/VAR_018795|||http://purl.uniprot.org/annotation/VAR_018796|||http://purl.uniprot.org/annotation/VAR_018797|||http://purl.uniprot.org/annotation/VAR_018798|||http://purl.uniprot.org/annotation/VAR_018799|||http://purl.uniprot.org/annotation/VAR_018800|||http://purl.uniprot.org/annotation/VAR_018801|||http://purl.uniprot.org/annotation/VAR_025365|||http://purl.uniprot.org/annotation/VSP_010534|||http://purl.uniprot.org/annotation/VSP_010535|||http://purl.uniprot.org/annotation/VSP_010536|||http://purl.uniprot.org/annotation/VSP_010537|||http://purl.uniprot.org/annotation/VSP_010538|||http://purl.uniprot.org/annotation/VSP_010539|||http://purl.uniprot.org/annotation/VSP_010540|||http://purl.uniprot.org/annotation/VSP_010541|||http://purl.uniprot.org/annotation/VSP_044091|||http://purl.uniprot.org/annotation/VSP_044092|||http://purl.uniprot.org/annotation/VSP_044093
http://togogenome.org/gene/9606:MRC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin 1|||C-type lectin 2|||C-type lectin 3|||C-type lectin 4|||C-type lectin 5|||C-type lectin 6|||C-type lectin 7|||C-type lectin 8|||C-type mannose receptor 2|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-II|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical|||Increased cell surface distribution.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||No alteration of distribution and trafficking.|||Polar residues|||Reduced sugar-binding activity.|||Reduction of endocytotic activity; distribution almost restricted to the cell surface.|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046078|||http://purl.uniprot.org/annotation/VAR_025304|||http://purl.uniprot.org/annotation/VAR_025305
http://togogenome.org/gene/9606:HBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ36|||http://purl.uniprot.org/uniprot/O60381                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AXH|||Basic and acidic residues|||Disordered|||HMG box|||HMG box-containing protein 1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048546|||http://purl.uniprot.org/annotation/VSP_014655|||http://purl.uniprot.org/annotation/VSP_014656
http://togogenome.org/gene/9606:TLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKI8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Loss of kinase activity.|||Loss of kinase inhibition in response to DNA damage.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase tousled-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086752|||http://purl.uniprot.org/annotation/VAR_041215|||http://purl.uniprot.org/annotation/VSP_043504|||http://purl.uniprot.org/annotation/VSP_043505|||http://purl.uniprot.org/annotation/VSP_043506|||http://purl.uniprot.org/annotation/VSP_050570|||http://purl.uniprot.org/annotation/VSP_050571
http://togogenome.org/gene/9606:EBLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2I7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Endogenous Bornavirus-like nucleoprotein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000358716
http://togogenome.org/gene/9606:DISP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Protein dispatched homolog 1|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310693|||http://purl.uniprot.org/annotation/VAR_037077
http://togogenome.org/gene/9606:SGPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TN35|||http://purl.uniprot.org/uniprot/O95470                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Almost no sphinganine-1-phosphate aldolase activity.|||Cytoplasmic|||Helical; Signal-anchor for type III membrane protein|||In NPHS14.|||In NPHS14; also found in a patient with isolated primary adrenal insufficiency; decreased protein abundance; increased aggregation; decreased sphinganine-1-phosphate aldolase activity.|||In NPHS14; decreased protein abundance.|||In NPHS14; unknown pathological significance.|||In NPHS1; decreased protein abundance in cells of patients homozygous for the mutation; increased aggregation; decreased sphinganine-1-phosphate aldolase activity.|||Loss of sphinganine-1-phosphate aldolase activity.|||Lumenal|||N6-(pyridoxal phosphate)lysine|||N6-(pyridoxal phosphate)lysine; alternate|||N6-acetyllysine; alternate|||No effect on the sphinganine-1-phosphate aldolase activity; no effect on protein abundance.|||Phosphoserine|||Probable disease-associated variant found in patients with atypical form of axonal peripheral neuropathy, characterized by acute or subacute onset and episodes of recurrent mononeuropathy.|||Sphingosine-1-phosphate lyase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147012|||http://purl.uniprot.org/annotation/VAR_048875|||http://purl.uniprot.org/annotation/VAR_079213|||http://purl.uniprot.org/annotation/VAR_079214|||http://purl.uniprot.org/annotation/VAR_079215|||http://purl.uniprot.org/annotation/VAR_079216|||http://purl.uniprot.org/annotation/VAR_079217|||http://purl.uniprot.org/annotation/VAR_079218|||http://purl.uniprot.org/annotation/VAR_081454|||http://purl.uniprot.org/annotation/VAR_081455|||http://purl.uniprot.org/annotation/VAR_081456
http://togogenome.org/gene/9606:INF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q27J81                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FH2|||GBD/FH3|||In CMTDIE and FSGS5.|||In CMTDIE.|||In CMTDIE; de novo mutation; unknown pathological significance.|||In CMTDIE; unknown pathological significance.|||In FSGS5.|||In FSGS5; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Inverted formin-2|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310963|||http://purl.uniprot.org/annotation/VAR_037117|||http://purl.uniprot.org/annotation/VAR_037118|||http://purl.uniprot.org/annotation/VAR_063075|||http://purl.uniprot.org/annotation/VAR_063076|||http://purl.uniprot.org/annotation/VAR_063077|||http://purl.uniprot.org/annotation/VAR_063078|||http://purl.uniprot.org/annotation/VAR_063079|||http://purl.uniprot.org/annotation/VAR_063080|||http://purl.uniprot.org/annotation/VAR_063081|||http://purl.uniprot.org/annotation/VAR_063082|||http://purl.uniprot.org/annotation/VAR_063083|||http://purl.uniprot.org/annotation/VAR_067589|||http://purl.uniprot.org/annotation/VAR_067590|||http://purl.uniprot.org/annotation/VAR_067591|||http://purl.uniprot.org/annotation/VAR_067592|||http://purl.uniprot.org/annotation/VAR_067593|||http://purl.uniprot.org/annotation/VAR_067594|||http://purl.uniprot.org/annotation/VAR_068845|||http://purl.uniprot.org/annotation/VAR_072229|||http://purl.uniprot.org/annotation/VAR_072230|||http://purl.uniprot.org/annotation/VAR_072231|||http://purl.uniprot.org/annotation/VAR_072232|||http://purl.uniprot.org/annotation/VAR_072233|||http://purl.uniprot.org/annotation/VAR_072234|||http://purl.uniprot.org/annotation/VAR_072235|||http://purl.uniprot.org/annotation/VAR_072236|||http://purl.uniprot.org/annotation/VAR_072237|||http://purl.uniprot.org/annotation/VAR_072238|||http://purl.uniprot.org/annotation/VAR_073984|||http://purl.uniprot.org/annotation/VAR_073985|||http://purl.uniprot.org/annotation/VAR_073986|||http://purl.uniprot.org/annotation/VAR_073987|||http://purl.uniprot.org/annotation/VAR_073988|||http://purl.uniprot.org/annotation/VAR_073989|||http://purl.uniprot.org/annotation/VAR_073990|||http://purl.uniprot.org/annotation/VAR_073991|||http://purl.uniprot.org/annotation/VAR_073992|||http://purl.uniprot.org/annotation/VAR_079801|||http://purl.uniprot.org/annotation/VAR_079802|||http://purl.uniprot.org/annotation/VAR_079803|||http://purl.uniprot.org/annotation/VAR_079804|||http://purl.uniprot.org/annotation/VAR_079805|||http://purl.uniprot.org/annotation/VAR_079806|||http://purl.uniprot.org/annotation/VAR_079807|||http://purl.uniprot.org/annotation/VSP_029360|||http://purl.uniprot.org/annotation/VSP_029361
http://togogenome.org/gene/9606:PKP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99959                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||Abolishes phosphorylation by MARK3.|||Disordered|||In ARVD9.|||In ARVD9; impairs protein stability.|||In ARVD9; unknown pathological significance.|||In ARVD9; unknown pathological significance; decreased interaction with DSP.|||In ARVD9; unknown pathological significance; decreased protein stability; decreased interaction with DSP; does not affect subcellular location to the desmosomes.|||In isoform 1.|||May be associated with increased susceptibility to arrhythmogenic right ventricular cardiomyopathy.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MARK3|||Phosphothreonine|||Plakophilin-2|||Polar residues|||Reduces phosphorylation of S-82 by MARK3. Reduces interaction with MARK3.|||Required for interaction with influenza A virus RNA polymerase subunit PB1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064286|||http://purl.uniprot.org/annotation/VAR_021148|||http://purl.uniprot.org/annotation/VAR_021149|||http://purl.uniprot.org/annotation/VAR_021150|||http://purl.uniprot.org/annotation/VAR_021151|||http://purl.uniprot.org/annotation/VAR_063108|||http://purl.uniprot.org/annotation/VAR_065701|||http://purl.uniprot.org/annotation/VAR_065702|||http://purl.uniprot.org/annotation/VAR_065703|||http://purl.uniprot.org/annotation/VAR_065704|||http://purl.uniprot.org/annotation/VAR_065705|||http://purl.uniprot.org/annotation/VAR_065706|||http://purl.uniprot.org/annotation/VAR_065707|||http://purl.uniprot.org/annotation/VAR_065708|||http://purl.uniprot.org/annotation/VAR_065709|||http://purl.uniprot.org/annotation/VAR_065710|||http://purl.uniprot.org/annotation/VAR_065711|||http://purl.uniprot.org/annotation/VAR_065712|||http://purl.uniprot.org/annotation/VAR_065713|||http://purl.uniprot.org/annotation/VAR_065714|||http://purl.uniprot.org/annotation/VAR_065715|||http://purl.uniprot.org/annotation/VAR_065716|||http://purl.uniprot.org/annotation/VAR_065717|||http://purl.uniprot.org/annotation/VAR_065718|||http://purl.uniprot.org/annotation/VAR_070037|||http://purl.uniprot.org/annotation/VAR_070276|||http://purl.uniprot.org/annotation/VAR_070277|||http://purl.uniprot.org/annotation/VAR_080397|||http://purl.uniprot.org/annotation/VAR_080398|||http://purl.uniprot.org/annotation/VSP_006736
http://togogenome.org/gene/9606:ZNF883                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG24                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 883                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395113
http://togogenome.org/gene/9606:SPTBN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRC6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||PH|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 23|||Spectrin 24|||Spectrin 25|||Spectrin 26|||Spectrin 27|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin beta chain, non-erythrocytic 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073466|||http://purl.uniprot.org/annotation/VAR_022050|||http://purl.uniprot.org/annotation/VAR_024395|||http://purl.uniprot.org/annotation/VAR_024396|||http://purl.uniprot.org/annotation/VAR_024397
http://togogenome.org/gene/9606:RHBDD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NTF9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||Rhomboid domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254596|||http://purl.uniprot.org/annotation/VAR_051581|||http://purl.uniprot.org/annotation/VSP_055407|||http://purl.uniprot.org/annotation/VSP_055608
http://togogenome.org/gene/9606:ELF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99607                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form ELF4-ERG oncogene|||Disordered|||ETS|||ETS-related transcription factor Elf-4|||In AIFBL2; elevated IL17A expression in patient colon biopsies; patient CD8+ T cells have reduced PRF1 expression when activated with IL-2 compared to CD8+ T cells from a healthy donor; severely decreased transcriptional activity shown in IFNB1 promoter-driven luciferase assay.|||In AIFBL2; loss of transcriptional activity shown in IFNB1 promoter-driven luciferase assay; decreased IFNB1 promoter binding; impaired binding to GPR35, GPR162 and PLCB2 promoters.|||Loss of transcriptional activity shown in IFNB1 promoter-driven luciferase assay.|||Loss of transcriptional activity shown in IFNB1 promoter-driven luciferase assay. Loss of INFB1 promoter binding. Does not bind GPR35, GPR162 and PLCB2 promoters.|||No effect on transcriptional activity shown in IFNB1 promoter-driven luciferase assay.|||Phosphoserine|||Polar residues|||RUNX1-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204089|||http://purl.uniprot.org/annotation/VAR_087047|||http://purl.uniprot.org/annotation/VAR_087048|||http://purl.uniprot.org/annotation/VAR_087049|||http://purl.uniprot.org/annotation/VAR_087050|||http://purl.uniprot.org/annotation/VAR_087051|||http://purl.uniprot.org/annotation/VAR_087052|||http://purl.uniprot.org/annotation/VAR_087053|||http://purl.uniprot.org/annotation/VAR_087054|||http://purl.uniprot.org/annotation/VAR_087055|||http://purl.uniprot.org/annotation/VAR_087056|||http://purl.uniprot.org/annotation/VAR_087057|||http://purl.uniprot.org/annotation/VAR_087058|||http://purl.uniprot.org/annotation/VAR_087059|||http://purl.uniprot.org/annotation/VAR_087060
http://togogenome.org/gene/9606:CAMK2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D2J9|||http://purl.uniprot.org/uniprot/B7Z1Z6|||http://purl.uniprot.org/uniprot/Q13554                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type II subunit beta|||Calmodulin-binding|||Disordered|||In MRD54.|||In MRD54; decreased protein abundance; increased autophosphorylation; decreased neuronal migration.|||In MRD54; no effect on protein abundance; increased autophosphorylation; decreased neuronal migration.|||In MRD54; no effect on protein abundance; loss of autophosphorylation; changed function in neuronal migration.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 1, isoform 2, isoform 3, isoform 5, isoform 6 and isoform 8.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 2, isoform 3, isoform 5 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086096|||http://purl.uniprot.org/annotation/VAR_045581|||http://purl.uniprot.org/annotation/VAR_045582|||http://purl.uniprot.org/annotation/VAR_080588|||http://purl.uniprot.org/annotation/VAR_080589|||http://purl.uniprot.org/annotation/VAR_080590|||http://purl.uniprot.org/annotation/VAR_080591|||http://purl.uniprot.org/annotation/VAR_080592|||http://purl.uniprot.org/annotation/VAR_081162|||http://purl.uniprot.org/annotation/VAR_081163|||http://purl.uniprot.org/annotation/VSP_004770|||http://purl.uniprot.org/annotation/VSP_004771|||http://purl.uniprot.org/annotation/VSP_004772|||http://purl.uniprot.org/annotation/VSP_004773|||http://purl.uniprot.org/annotation/VSP_004774|||http://purl.uniprot.org/annotation/VSP_004775|||http://purl.uniprot.org/annotation/VSP_004776|||http://purl.uniprot.org/annotation/VSP_004777|||http://purl.uniprot.org/annotation/VSP_041219
http://togogenome.org/gene/9606:MAP3K12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12852                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||In isoform 2.|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 12|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086261|||http://purl.uniprot.org/annotation/VAR_040705|||http://purl.uniprot.org/annotation/VAR_040706|||http://purl.uniprot.org/annotation/VAR_040707|||http://purl.uniprot.org/annotation/VSP_044646
http://togogenome.org/gene/9606:RSAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXG1                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Complete loss of antiviral activity against Zika virus.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Loss of Lys-6-linked ubiquitination.|||Loss of ability to assemble an Fe-S cluster and significant decrease in protein stability.|||Loss of acetylation.|||N6-acetyllysine|||Radical SAM core|||S-adenosylmethionine-dependent nucleotide dehydratase RSAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309583|||http://purl.uniprot.org/annotation/VAR_036980|||http://purl.uniprot.org/annotation/VAR_053974
http://togogenome.org/gene/9606:AKR7A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZX4|||http://purl.uniprot.org/uniprot/O43488|||http://purl.uniprot.org/uniprot/V9HWA2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aflatoxin B1 aldehyde reductase member 2|||Lowers pKa of active site Tyr|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||NADP-dependent oxidoreductase|||Phosphoserine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070375|||http://purl.uniprot.org/annotation/VAR_017413|||http://purl.uniprot.org/annotation/VAR_017414|||http://purl.uniprot.org/annotation/VAR_017415|||http://purl.uniprot.org/annotation/VAR_048209|||http://purl.uniprot.org/annotation/VAR_048210|||http://purl.uniprot.org/annotation/VAR_048211|||http://purl.uniprot.org/annotation/VAR_060222
http://togogenome.org/gene/9606:RHOV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96L33                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Pro residues|||Rho-related GTP-binding protein RhoV|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326438
http://togogenome.org/gene/9606:FOXJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92949                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein J1|||In CILD43; reduced number of cilia and mislocalized basal bodies; defects of axonemal microtubular organization; loss of ability to propel mucous along the surface of the epithelium; abnormal localization of PTK2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091850|||http://purl.uniprot.org/annotation/VAR_083456|||http://purl.uniprot.org/annotation/VAR_083457
http://togogenome.org/gene/9606:PROS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4K3|||http://purl.uniprot.org/uniprot/A0A0S2Z4L3|||http://purl.uniprot.org/uniprot/P07225                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Does not affect protein levels; the mutant is normally secreted.|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||Gla|||In THPH5.|||In THPH5; Tokushima; the specific activity decreases to 58% of that of the wild-type PROS1; the activated protein cofactor activity is inhibited by C4BPB with a dose dependency similar to that of wild-type PROS1.|||In THPH5; does not affect PROS1 production but results in 15.2-fold reduced PROS1 activity; has 5.4 fold reduced affinity for anionic phospholipid vesicles (P < 0.0001) and decreased affinity for an antibody specific for the Ca(2+)-dependent conformation of the PROS1 Gla domain.|||In THPH5; does not affect protein levels; the mutant is secreted at lower levels compared to wild-type.|||In THPH5; expresses very low/undetectable PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found.|||In THPH5; produces around 30% of PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found.|||In THPH5; produces around 50% of PROS1 levels compared to wild-type; has impaired secretion; intracellular degradation of unsecreted material is found.|||In THPH5; reduced mutant protein levels and secretion.|||In THPH5; reduces expression of PROS1 by 33.2% (P < 0.001) and activity by 3.6-fold; has only a modest 1.5-fold (P < 0.001) reduced affinity for phospholipid and an antibody specific for the Ca(2+)-dependent conformation of the PROS1 Gla domain.|||In THPH5; secretion of the mutant markedly decreased compared with that of the wild-type; intracellular degradation and impaired secretion of the mutant.|||In THPH5; shows intracellular degradation and decreased secretion.|||In THPH5; the activated protein cofactor activity is inhibited by C4BPB with a dose dependency similar to that of wild-type PROS1.|||In THPH5; unknown pathological significance.|||In THPH6.|||In a colorectal cancer sample; somatic mutation.|||Laminin G|||Laminin G-like 1|||Laminin G-like 2|||Markedly reduced secretion of the mutant.|||N-linked (GlcNAc...) asparagine|||No change in secretion of the mutant.|||Not glycosylated; in variant Heerlen|||Thrombin-sensitive|||Variant Heerlen; could be associated with THPH5.|||Vitamin K-dependent protein S                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022119|||http://purl.uniprot.org/annotation/PRO_0000022120|||http://purl.uniprot.org/annotation/PRO_5006608240|||http://purl.uniprot.org/annotation/PRO_5040060395|||http://purl.uniprot.org/annotation/VAR_005566|||http://purl.uniprot.org/annotation/VAR_005567|||http://purl.uniprot.org/annotation/VAR_005568|||http://purl.uniprot.org/annotation/VAR_014116|||http://purl.uniprot.org/annotation/VAR_014117|||http://purl.uniprot.org/annotation/VAR_014118|||http://purl.uniprot.org/annotation/VAR_014119|||http://purl.uniprot.org/annotation/VAR_014666|||http://purl.uniprot.org/annotation/VAR_035981|||http://purl.uniprot.org/annotation/VAR_046802|||http://purl.uniprot.org/annotation/VAR_046803|||http://purl.uniprot.org/annotation/VAR_046804|||http://purl.uniprot.org/annotation/VAR_046805|||http://purl.uniprot.org/annotation/VAR_046806|||http://purl.uniprot.org/annotation/VAR_046807|||http://purl.uniprot.org/annotation/VAR_046808|||http://purl.uniprot.org/annotation/VAR_046809|||http://purl.uniprot.org/annotation/VAR_046810|||http://purl.uniprot.org/annotation/VAR_046811|||http://purl.uniprot.org/annotation/VAR_046812|||http://purl.uniprot.org/annotation/VAR_046813|||http://purl.uniprot.org/annotation/VAR_046814|||http://purl.uniprot.org/annotation/VAR_046815|||http://purl.uniprot.org/annotation/VAR_046816|||http://purl.uniprot.org/annotation/VAR_046817|||http://purl.uniprot.org/annotation/VAR_046818|||http://purl.uniprot.org/annotation/VAR_046819|||http://purl.uniprot.org/annotation/VAR_046820|||http://purl.uniprot.org/annotation/VAR_046821|||http://purl.uniprot.org/annotation/VAR_046822|||http://purl.uniprot.org/annotation/VAR_046823|||http://purl.uniprot.org/annotation/VAR_046824|||http://purl.uniprot.org/annotation/VAR_046825|||http://purl.uniprot.org/annotation/VAR_046826|||http://purl.uniprot.org/annotation/VAR_046827|||http://purl.uniprot.org/annotation/VAR_046828|||http://purl.uniprot.org/annotation/VAR_046829|||http://purl.uniprot.org/annotation/VAR_046830|||http://purl.uniprot.org/annotation/VAR_046831|||http://purl.uniprot.org/annotation/VAR_046832|||http://purl.uniprot.org/annotation/VAR_046833|||http://purl.uniprot.org/annotation/VAR_046834|||http://purl.uniprot.org/annotation/VAR_046835|||http://purl.uniprot.org/annotation/VAR_046836|||http://purl.uniprot.org/annotation/VAR_046837|||http://purl.uniprot.org/annotation/VAR_046838|||http://purl.uniprot.org/annotation/VAR_046839|||http://purl.uniprot.org/annotation/VAR_046840|||http://purl.uniprot.org/annotation/VAR_046841|||http://purl.uniprot.org/annotation/VAR_046842|||http://purl.uniprot.org/annotation/VAR_046843|||http://purl.uniprot.org/annotation/VAR_046844|||http://purl.uniprot.org/annotation/VAR_046845|||http://purl.uniprot.org/annotation/VAR_046846|||http://purl.uniprot.org/annotation/VAR_046847|||http://purl.uniprot.org/annotation/VAR_046848|||http://purl.uniprot.org/annotation/VAR_046849|||http://purl.uniprot.org/annotation/VAR_046850|||http://purl.uniprot.org/annotation/VAR_046851|||http://purl.uniprot.org/annotation/VAR_046852|||http://purl.uniprot.org/annotation/VAR_046853|||http://purl.uniprot.org/annotation/VAR_046854|||http://purl.uniprot.org/annotation/VAR_046855|||http://purl.uniprot.org/annotation/VAR_046856|||http://purl.uniprot.org/annotation/VAR_046857|||http://purl.uniprot.org/annotation/VAR_046858|||http://purl.uniprot.org/annotation/VAR_046859|||http://purl.uniprot.org/annotation/VAR_046860|||http://purl.uniprot.org/annotation/VAR_046862|||http://purl.uniprot.org/annotation/VAR_046863|||http://purl.uniprot.org/annotation/VAR_046864|||http://purl.uniprot.org/annotation/VAR_046865|||http://purl.uniprot.org/annotation/VAR_046866|||http://purl.uniprot.org/annotation/VAR_046867|||http://purl.uniprot.org/annotation/VAR_046868|||http://purl.uniprot.org/annotation/VAR_046869|||http://purl.uniprot.org/annotation/VAR_046870|||http://purl.uniprot.org/annotation/VAR_046871|||http://purl.uniprot.org/annotation/VAR_046872|||http://purl.uniprot.org/annotation/VAR_046873|||http://purl.uniprot.org/annotation/VAR_046874|||http://purl.uniprot.org/annotation/VAR_046875|||http://purl.uniprot.org/annotation/VAR_046876|||http://purl.uniprot.org/annotation/VAR_046877|||http://purl.uniprot.org/annotation/VAR_046878|||http://purl.uniprot.org/annotation/VAR_046879|||http://purl.uniprot.org/annotation/VAR_046880|||http://purl.uniprot.org/annotation/VAR_046881|||http://purl.uniprot.org/annotation/VAR_046882|||http://purl.uniprot.org/annotation/VAR_046883|||http://purl.uniprot.org/annotation/VAR_046884|||http://purl.uniprot.org/annotation/VAR_046885|||http://purl.uniprot.org/annotation/VAR_046886|||http://purl.uniprot.org/annotation/VAR_046887|||http://purl.uniprot.org/annotation/VAR_046888|||http://purl.uniprot.org/annotation/VAR_046889|||http://purl.uniprot.org/annotation/VAR_046890|||http://purl.uniprot.org/annotation/VAR_046891|||http://purl.uniprot.org/annotation/VAR_067302
http://togogenome.org/gene/9606:MYMK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NI61                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In CFZS1; decreased localization at the plasma membrane; reduced cell fusion in a heterologous cell fusion assay in vitro compared to wild-type; partially rescues of mymk knockout fish.|||In CFZS1; loss of localization at the plasma membrane; loss of cell fusion in a heterologous cell fusion assay in vitro; no rescue of mymk knockout fish.|||In CFZS1; loss of localization at the plasma membrane; loss of cell fusion in a heterologous cell fusion assay in vitro; no rescue of mymk knockout fish; primary myoblasts from a compound heterozygote associating T-91 and R-185 exhibit no difference in their capability to differentiate compared to control myoblasts, but show a significant difference in the fusion index, with a higher percentage of singly-nucleated relative to multinucleated cells in compound heterozygous compared to control myoblasts.|||In CFZS1; unknown pathological significance.|||In CFZS1; unknown pathological significance; supports cell fusion in a heterologous cell fusion assay in vitro; decreased localization at the plasma membrane; partially rescues of mymk knockout fish; primary myoblasts from a compound heterozygote associating T-91 and R-185 exhibit no difference in their capability to differentiate compared to control myoblasts, but show a significant difference in the fusion index, with a higher percentage of singly-nucleated relative to multinucleated cells in compound heterozygous compared to control myoblasts.|||Protein myomaker|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319062|||http://purl.uniprot.org/annotation/VAR_079262|||http://purl.uniprot.org/annotation/VAR_079263|||http://purl.uniprot.org/annotation/VAR_079264|||http://purl.uniprot.org/annotation/VAR_079265|||http://purl.uniprot.org/annotation/VAR_081291
http://togogenome.org/gene/9606:ZCCHC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type 1|||CCHC-type 2|||CCHC-type 3|||Disordered|||In isoform 2.|||Phosphotyrosine|||Zinc finger CCHC domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150951|||http://purl.uniprot.org/annotation/VSP_055996
http://togogenome.org/gene/9606:IL1RAPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP60                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||TIR|||X-linked interleukin-1 receptor accessory protein-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015459|||http://purl.uniprot.org/annotation/VAR_036592
http://togogenome.org/gene/9606:WDR54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H977                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes cross-linking. Decreases ERK signaling pathway activation. Abolishes inhibition of EGF receptor degradation after EGF stimulation.|||Decreases cross-linking.|||Decreases cross-linking. Abolishes ubiquitination.|||In isoform 2.|||In isoform 3.|||No effect on cross-linking.|||Slightly decreases cross-linking.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 54                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051415|||http://purl.uniprot.org/annotation/VSP_060292|||http://purl.uniprot.org/annotation/VSP_060293|||http://purl.uniprot.org/annotation/VSP_060294|||http://purl.uniprot.org/annotation/VSP_060295
http://togogenome.org/gene/9606:RTRAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y224                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue                                                                                  ^@                                                                                  N6-acetyllysine|||RNA transcription, translation and transport factor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089956
http://togogenome.org/gene/9606:CEACAM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0K5|||http://purl.uniprot.org/uniprot/P06731|||http://purl.uniprot.org/uniprot/Q53G30                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Abolishes dimerization. Reduced affinity for E.coli Dr adhesins.|||Carcinoembryonic antigen-related cell adhesion molecule 5|||GPI-anchor amidated alanine|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No effect on dimerization.|||No effect on dimerization. Reduced affinity for E.coli Dr adhesins.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014566|||http://purl.uniprot.org/annotation/PRO_0000014567|||http://purl.uniprot.org/annotation/PRO_5004248789|||http://purl.uniprot.org/annotation/PRO_5014008696|||http://purl.uniprot.org/annotation/VAR_024493|||http://purl.uniprot.org/annotation/VAR_031091|||http://purl.uniprot.org/annotation/VAR_031092|||http://purl.uniprot.org/annotation/VAR_056028|||http://purl.uniprot.org/annotation/VAR_056029|||http://purl.uniprot.org/annotation/VAR_061310|||http://purl.uniprot.org/annotation/VAR_061311|||http://purl.uniprot.org/annotation/VSP_053414
http://togogenome.org/gene/9606:THOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Death|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In DFNA86; impaired function in hair cell formation, when tested in a heterologous system.|||In isoform 2.|||Loss of ability to induce apoptosis. Interferes with normal response of SaOS-2 cells to radiation.|||N-acetylmethionine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||THO complex subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072520|||http://purl.uniprot.org/annotation/VAR_088179|||http://purl.uniprot.org/annotation/VSP_038073|||http://purl.uniprot.org/annotation/VSP_038074
http://togogenome.org/gene/9606:ADD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HL01|||http://purl.uniprot.org/uniprot/P35611                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by ROCK2; when associated with D-445.|||Abolishes phosphorylation by ROCK2; when associated with D-480.|||Alpha-adducin|||Basic and acidic residues|||Class II aldolase/adducin N-terminal|||Disordered|||In isoform 2, isoform 4 and isoform 6.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5.|||Interaction with calmodulin|||N-acetylmethionine|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKA and PKC|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by ROCK2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218530|||http://purl.uniprot.org/annotation/VAR_014184|||http://purl.uniprot.org/annotation/VAR_014185|||http://purl.uniprot.org/annotation/VAR_014863|||http://purl.uniprot.org/annotation/VAR_014864|||http://purl.uniprot.org/annotation/VAR_014865|||http://purl.uniprot.org/annotation/VAR_022108|||http://purl.uniprot.org/annotation/VSP_000174|||http://purl.uniprot.org/annotation/VSP_000175|||http://purl.uniprot.org/annotation/VSP_000176|||http://purl.uniprot.org/annotation/VSP_054420|||http://purl.uniprot.org/annotation/VSP_055402|||http://purl.uniprot.org/annotation/VSP_055403
http://togogenome.org/gene/9606:AVPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30518                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In NDI1.|||In NDI1; binding capacity is 10% of wild-type, but binding affinity is stronger than wild-type.|||In NDI1; fails to activate the adenylyl cyclase system.|||In NSIAD; constitutively active.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reduced palmitoylation, reduced cell surface localization but coupling to G protein unaffected.|||S-palmitoyl cysteine|||Vasopressin V2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070208|||http://purl.uniprot.org/annotation/VAR_003516|||http://purl.uniprot.org/annotation/VAR_003517|||http://purl.uniprot.org/annotation/VAR_003518|||http://purl.uniprot.org/annotation/VAR_003519|||http://purl.uniprot.org/annotation/VAR_003520|||http://purl.uniprot.org/annotation/VAR_003521|||http://purl.uniprot.org/annotation/VAR_003522|||http://purl.uniprot.org/annotation/VAR_003523|||http://purl.uniprot.org/annotation/VAR_003524|||http://purl.uniprot.org/annotation/VAR_003525|||http://purl.uniprot.org/annotation/VAR_003526|||http://purl.uniprot.org/annotation/VAR_003527|||http://purl.uniprot.org/annotation/VAR_003528|||http://purl.uniprot.org/annotation/VAR_003529|||http://purl.uniprot.org/annotation/VAR_003530|||http://purl.uniprot.org/annotation/VAR_003531|||http://purl.uniprot.org/annotation/VAR_003532|||http://purl.uniprot.org/annotation/VAR_003533|||http://purl.uniprot.org/annotation/VAR_003534|||http://purl.uniprot.org/annotation/VAR_003535|||http://purl.uniprot.org/annotation/VAR_003536|||http://purl.uniprot.org/annotation/VAR_003537|||http://purl.uniprot.org/annotation/VAR_003538|||http://purl.uniprot.org/annotation/VAR_003539|||http://purl.uniprot.org/annotation/VAR_003540|||http://purl.uniprot.org/annotation/VAR_003541|||http://purl.uniprot.org/annotation/VAR_003542|||http://purl.uniprot.org/annotation/VAR_003543|||http://purl.uniprot.org/annotation/VAR_003544|||http://purl.uniprot.org/annotation/VAR_003545|||http://purl.uniprot.org/annotation/VAR_003546|||http://purl.uniprot.org/annotation/VAR_003547|||http://purl.uniprot.org/annotation/VAR_003548|||http://purl.uniprot.org/annotation/VAR_011858|||http://purl.uniprot.org/annotation/VAR_015296|||http://purl.uniprot.org/annotation/VAR_015297|||http://purl.uniprot.org/annotation/VAR_015298|||http://purl.uniprot.org/annotation/VAR_015299|||http://purl.uniprot.org/annotation/VAR_015300|||http://purl.uniprot.org/annotation/VAR_015301|||http://purl.uniprot.org/annotation/VAR_015302|||http://purl.uniprot.org/annotation/VAR_015303|||http://purl.uniprot.org/annotation/VAR_015304|||http://purl.uniprot.org/annotation/VAR_015305|||http://purl.uniprot.org/annotation/VAR_015306|||http://purl.uniprot.org/annotation/VAR_015307|||http://purl.uniprot.org/annotation/VAR_015308|||http://purl.uniprot.org/annotation/VAR_015309|||http://purl.uniprot.org/annotation/VAR_015310|||http://purl.uniprot.org/annotation/VAR_015311|||http://purl.uniprot.org/annotation/VAR_015312|||http://purl.uniprot.org/annotation/VAR_015313|||http://purl.uniprot.org/annotation/VAR_015314|||http://purl.uniprot.org/annotation/VAR_015315|||http://purl.uniprot.org/annotation/VAR_015316|||http://purl.uniprot.org/annotation/VAR_015317|||http://purl.uniprot.org/annotation/VAR_015318|||http://purl.uniprot.org/annotation/VAR_015319|||http://purl.uniprot.org/annotation/VAR_015320|||http://purl.uniprot.org/annotation/VAR_015321|||http://purl.uniprot.org/annotation/VAR_015322|||http://purl.uniprot.org/annotation/VAR_015323|||http://purl.uniprot.org/annotation/VAR_015324|||http://purl.uniprot.org/annotation/VAR_015325|||http://purl.uniprot.org/annotation/VAR_015326|||http://purl.uniprot.org/annotation/VAR_015327|||http://purl.uniprot.org/annotation/VAR_015328|||http://purl.uniprot.org/annotation/VAR_015329|||http://purl.uniprot.org/annotation/VAR_015330|||http://purl.uniprot.org/annotation/VAR_015331|||http://purl.uniprot.org/annotation/VAR_015332|||http://purl.uniprot.org/annotation/VAR_015333|||http://purl.uniprot.org/annotation/VAR_015334|||http://purl.uniprot.org/annotation/VAR_015335|||http://purl.uniprot.org/annotation/VAR_015336|||http://purl.uniprot.org/annotation/VAR_015337|||http://purl.uniprot.org/annotation/VAR_015338|||http://purl.uniprot.org/annotation/VAR_015339|||http://purl.uniprot.org/annotation/VAR_015340|||http://purl.uniprot.org/annotation/VAR_015341|||http://purl.uniprot.org/annotation/VAR_015342|||http://purl.uniprot.org/annotation/VAR_015343|||http://purl.uniprot.org/annotation/VAR_015344|||http://purl.uniprot.org/annotation/VAR_015345|||http://purl.uniprot.org/annotation/VAR_015346|||http://purl.uniprot.org/annotation/VAR_015347|||http://purl.uniprot.org/annotation/VAR_015348|||http://purl.uniprot.org/annotation/VAR_015349|||http://purl.uniprot.org/annotation/VAR_015350|||http://purl.uniprot.org/annotation/VAR_015351|||http://purl.uniprot.org/annotation/VAR_015352|||http://purl.uniprot.org/annotation/VAR_015353|||http://purl.uniprot.org/annotation/VAR_015354|||http://purl.uniprot.org/annotation/VAR_015355|||http://purl.uniprot.org/annotation/VAR_015356|||http://purl.uniprot.org/annotation/VAR_025901|||http://purl.uniprot.org/annotation/VAR_025902|||http://purl.uniprot.org/annotation/VAR_035769|||http://purl.uniprot.org/annotation/VAR_062591|||http://purl.uniprot.org/annotation/VSP_036990|||http://purl.uniprot.org/annotation/VSP_036991
http://togogenome.org/gene/9606:ZBTB37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7Z4|||http://purl.uniprot.org/uniprot/Q5TC79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger and BTB domain-containing protein 37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047741|||http://purl.uniprot.org/annotation/VSP_014440|||http://purl.uniprot.org/annotation/VSP_014441|||http://purl.uniprot.org/annotation/VSP_014442
http://togogenome.org/gene/9606:C12orf75                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAD7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Overexpressed in colon carcinoma 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000368221
http://togogenome.org/gene/9606:FMO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31512                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Dimethylaniline monooxygenase [N-oxide-forming] 4|||Found in a patient with intellectual disability; unknown pathological significance.|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147660|||http://purl.uniprot.org/annotation/VAR_015367|||http://purl.uniprot.org/annotation/VAR_015368|||http://purl.uniprot.org/annotation/VAR_015369|||http://purl.uniprot.org/annotation/VAR_022305|||http://purl.uniprot.org/annotation/VAR_022306|||http://purl.uniprot.org/annotation/VAR_022307|||http://purl.uniprot.org/annotation/VAR_049090|||http://purl.uniprot.org/annotation/VAR_084652
http://togogenome.org/gene/9606:FAM83H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZRV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased interaction with CSNK1A1 and loss of function in keratin cytoskeleton organization.|||Disordered|||In AI3A; mild form.|||Mediates interaction with CSNK1A1 and is required for FAM83H activity in keratin cytoskeleton organization|||No effect on interaction with CSNK1A1 and function in keratin cytoskeleton organization.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein FAM83H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324488|||http://purl.uniprot.org/annotation/VAR_062189|||http://purl.uniprot.org/annotation/VAR_073954
http://togogenome.org/gene/9606:OOEP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGQ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||KH; atypical|||Oocyte-expressed protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328802|||http://purl.uniprot.org/annotation/VAR_042523|||http://purl.uniprot.org/annotation/VAR_042524
http://togogenome.org/gene/9606:KLHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3I8|||http://purl.uniprot.org/uniprot/F5H1J3|||http://purl.uniprot.org/uniprot/Q8TBJ7|||http://purl.uniprot.org/uniprot/Q9NR64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  BTB|||Disordered|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119099
http://togogenome.org/gene/9606:N6AMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5N5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished DNA methyltransferase activity.|||Abolished protein N(5)-glutamine methyltransferase activity without affecting histone-lysine methyltransferase activity.|||Abolished protein N(5)-glutamine methyltransferase activity.|||Abolished protein N(5)-glutamine methyltransferase activity. Abolished histone-lysine methyltransferase activity.|||In isoform 2.|||Methyltransferase N6AMT1|||Reduced protein N(5)-glutamine methyltransferase activity.|||Slightly reduced protein N(5)-glutamine methyltransferase activity.|||Strongly reduced protein N(5)-glutamine methyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088049|||http://purl.uniprot.org/annotation/VAR_060445|||http://purl.uniprot.org/annotation/VAR_060446|||http://purl.uniprot.org/annotation/VAR_060447|||http://purl.uniprot.org/annotation/VSP_040294
http://togogenome.org/gene/9606:MSH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43246                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA mismatch repair protein Msh2|||Decreased mismatch repair activity; shows significantly decreased repair efficiency when associated with variant D-322.|||Decreases protein levels.|||Found in a colorectal cancer sample; normal mismatch repair activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CRC; unknown pathological significance.|||In CRC; unknown pathological significance; decreased mismatch repair activity.|||In CRC; unknown pathological significance; somatic mutation.|||In LYNCH1 and CRC; sporadic early-onset CRC; decreased mismatch repair activity.|||In LYNCH1 and CRC; unknown pathological significance.|||In LYNCH1 and CRC; unknown pathological significance; may decrease mismatch repair activity.|||In LYNCH1.|||In LYNCH1; decreased mismatch binding activity.|||In LYNCH1; decreased mismatch repair activity.|||In LYNCH1; decreased mismatch repair activity; affects protein stability; loss of protein expression.|||In LYNCH1; decreased mismatch repair activity; associated with an abnormal subcellular localization pattern; affects protein stability; loss of protein expression.|||In LYNCH1; decreased mismatch repair activity; confers multiple biochemical defects.|||In LYNCH1; decreased mismatch repair activity; has no effect on MSH2 splicing.|||In LYNCH1; decreased mismatch repair activity; loss of protein expression.|||In LYNCH1; decreased mismatch repair activity; loss of protein expression; confers multiple biochemical defects.|||In LYNCH1; decreased mismatch repair activity; no loss of protein expression.|||In LYNCH1; decreased mismatch repair activity; shows no functional defects in gel shift assay.|||In LYNCH1; decreases protein levels.|||In LYNCH1; has no effect on MSH2 splicing.|||In LYNCH1; has no effect on ex vivo splicing assay.|||In LYNCH1; loss of protein expression.|||In LYNCH1; no effect on MSH2 splicing.|||In LYNCH1; normal mismatch repair activity.|||In LYNCH1; presumed to enhance cancer risk considerably when associated with P-328; shows significantly decreased repair efficiency when associated with variant P-328.|||In LYNCH1; requires 2 nucleotide substitutions; unknown pathological significance; decreased mismatch repair activity.|||In LYNCH1; requires 2 nucleotide substitutions; unknown pathological significance; normal mismatch repair activity.|||In LYNCH1; shows a decreased expression level of the MutS alpha complex; associated with an abnormal subcellular localization pattern.|||In LYNCH1; shows reduced mismatch binding; does not show a decreased expression level of the MutS alpha complex; not associated with an abnormal subcellular localization pattern; normal mismatch repair activity.|||In LYNCH1; somatic mutation.|||In LYNCH1; the equivalent substitution in yeast does not affect mismatch repair efficiency in vitro.|||In LYNCH1; unknown pathological significance.|||In LYNCH1; unknown pathological significance; decreased mismatch repair activity.|||In LYNCH1; unknown pathological significance; no decrease in mismatch repair activity.|||In LYNCH1; unknown pathological significance; normal mismatch repair activity.|||In LYNCH1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency.|||In LYNCH1; unknown pathological significance; shows slightly reduced mismatch binding or release efficiency; results in partial MSH2 exon 5 skipping; normal mismatch repair activity.|||In gastric cancer; unknown pathological significance.|||In gastric cancer; unknown pathological significance; cryptic acceptor splice site suppressed on ex vivo splicing assay.|||In glioma; also associated with LYNCH1; no effect on MSH2 splicing.|||In isoform 2.|||Interaction with EXO1|||May be associated with increased colorectal cancer susceptibility; shows significantly decreased repair efficiency when associated with variant E-487.|||N-acetylalanine|||N6-acetyllysine|||No effect on mismatch binding, complete loss of DNA repair function when associated with MSH6 mutant R-1140.|||No effect on protein levels.|||Phosphoserine|||Removed|||Shows no defects; normal mismatch repair activity.|||Shows significantly decreased repair efficiency when associated with variant S-127; presumed to enhance cancer risk considerably when associated with variant S-127. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115183|||http://purl.uniprot.org/annotation/VAR_004470|||http://purl.uniprot.org/annotation/VAR_004471|||http://purl.uniprot.org/annotation/VAR_004472|||http://purl.uniprot.org/annotation/VAR_004473|||http://purl.uniprot.org/annotation/VAR_004474|||http://purl.uniprot.org/annotation/VAR_004475|||http://purl.uniprot.org/annotation/VAR_004476|||http://purl.uniprot.org/annotation/VAR_004477|||http://purl.uniprot.org/annotation/VAR_004478|||http://purl.uniprot.org/annotation/VAR_004479|||http://purl.uniprot.org/annotation/VAR_004480|||http://purl.uniprot.org/annotation/VAR_004481|||http://purl.uniprot.org/annotation/VAR_004482|||http://purl.uniprot.org/annotation/VAR_004483|||http://purl.uniprot.org/annotation/VAR_004484|||http://purl.uniprot.org/annotation/VAR_004485|||http://purl.uniprot.org/annotation/VAR_004486|||http://purl.uniprot.org/annotation/VAR_004487|||http://purl.uniprot.org/annotation/VAR_004488|||http://purl.uniprot.org/annotation/VAR_004489|||http://purl.uniprot.org/annotation/VAR_009250|||http://purl.uniprot.org/annotation/VAR_009251|||http://purl.uniprot.org/annotation/VAR_012936|||http://purl.uniprot.org/annotation/VAR_012937|||http://purl.uniprot.org/annotation/VAR_012938|||http://purl.uniprot.org/annotation/VAR_012939|||http://purl.uniprot.org/annotation/VAR_012940|||http://purl.uniprot.org/annotation/VAR_012941|||http://purl.uniprot.org/annotation/VAR_012942|||http://purl.uniprot.org/annotation/VAR_012943|||http://purl.uniprot.org/annotation/VAR_012944|||http://purl.uniprot.org/annotation/VAR_012945|||http://purl.uniprot.org/annotation/VAR_013171|||http://purl.uniprot.org/annotation/VAR_013172|||http://purl.uniprot.org/annotation/VAR_019233|||http://purl.uniprot.org/annotation/VAR_019234|||http://purl.uniprot.org/annotation/VAR_022670|||http://purl.uniprot.org/annotation/VAR_022671|||http://purl.uniprot.org/annotation/VAR_038026|||http://purl.uniprot.org/annotation/VAR_038027|||http://purl.uniprot.org/annotation/VAR_038028|||http://purl.uniprot.org/annotation/VAR_038029|||http://purl.uniprot.org/annotation/VAR_038030|||http://purl.uniprot.org/annotation/VAR_038031|||http://purl.uniprot.org/annotation/VAR_043736|||http://purl.uniprot.org/annotation/VAR_043737|||http://purl.uniprot.org/annotation/VAR_043738|||http://purl.uniprot.org/annotation/VAR_043739|||http://purl.uniprot.org/annotation/VAR_043740|||http://purl.uniprot.org/annotation/VAR_043741|||http://purl.uniprot.org/annotation/VAR_043742|||http://purl.uniprot.org/annotation/VAR_043743|||http://purl.uniprot.org/annotation/VAR_043744|||http://purl.uniprot.org/annotation/VAR_043745|||http://purl.uniprot.org/annotation/VAR_043746|||http://purl.uniprot.org/annotation/VAR_043747|||http://purl.uniprot.org/annotation/VAR_043748|||http://purl.uniprot.org/annotation/VAR_043749|||http://purl.uniprot.org/annotation/VAR_043750|||http://purl.uniprot.org/annotation/VAR_043751|||http://purl.uniprot.org/annotation/VAR_043752|||http://purl.uniprot.org/annotation/VAR_043753|||http://purl.uniprot.org/annotation/VAR_043754|||http://purl.uniprot.org/annotation/VAR_043755|||http://purl.uniprot.org/annotation/VAR_043756|||http://purl.uniprot.org/annotation/VAR_043757|||http://purl.uniprot.org/annotation/VAR_043758|||http://purl.uniprot.org/annotation/VAR_043759|||http://purl.uniprot.org/annotation/VAR_043760|||http://purl.uniprot.org/annotation/VAR_043761|||http://purl.uniprot.org/annotation/VAR_043762|||http://purl.uniprot.org/annotation/VAR_043763|||http://purl.uniprot.org/annotation/VAR_043764|||http://purl.uniprot.org/annotation/VAR_043765|||http://purl.uniprot.org/annotation/VAR_043766|||http://purl.uniprot.org/annotation/VAR_043767|||http://purl.uniprot.org/annotation/VAR_043768|||http://purl.uniprot.org/annotation/VAR_043769|||http://purl.uniprot.org/annotation/VAR_043770|||http://purl.uniprot.org/annotation/VAR_043771|||http://purl.uniprot.org/annotation/VAR_043772|||http://purl.uniprot.org/annotation/VAR_043773|||http://purl.uniprot.org/annotation/VAR_043774|||http://purl.uniprot.org/annotation/VAR_043775|||http://purl.uniprot.org/annotation/VAR_043776|||http://purl.uniprot.org/annotation/VAR_043777|||http://purl.uniprot.org/annotation/VAR_043778|||http://purl.uniprot.org/annotation/VAR_043779|||http://purl.uniprot.org/annotation/VAR_043780|||http://purl.uniprot.org/annotation/VAR_043781|||http://purl.uniprot.org/annotation/VAR_043782|||http://purl.uniprot.org/annotation/VAR_043783|||http://purl.uniprot.org/annotation/VAR_043784|||http://purl.uniprot.org/annotation/VAR_043785|||http://purl.uniprot.org/annotation/VAR_043786|||http://purl.uniprot.org/annotation/VAR_043787|||http://purl.uniprot.org/annotation/VAR_043788|||http://purl.uniprot.org/annotation/VAR_043789|||http://purl.uniprot.org/annotation/VAR_043790|||http://purl.uniprot.org/annotation/VAR_043791|||http://purl.uniprot.org/annotation/VAR_043792|||http://purl.uniprot.org/annotation/VAR_043793|||http://purl.uniprot.org/annotation/VAR_043794|||http://purl.uniprot.org/annotation/VAR_043795|||http://purl.uniprot.org/annotation/VAR_054511|||http://purl.uniprot.org/annotation/VAR_054512|||http://purl.uniprot.org/annotation/VAR_054513|||http://purl.uniprot.org/annotation/VAR_054514|||http://purl.uniprot.org/annotation/VAR_054515|||http://purl.uniprot.org/annotation/VAR_054516|||http://purl.uniprot.org/annotation/VAR_054517|||http://purl.uniprot.org/annotation/VAR_054518|||http://purl.uniprot.org/annotation/VAR_054519|||http://purl.uniprot.org/annotation/VAR_054520|||http://purl.uniprot.org/annotation/VAR_054521|||http://purl.uniprot.org/annotation/VAR_067284|||http://purl.uniprot.org/annotation/VAR_067285|||http://purl.uniprot.org/annotation/VAR_067286|||http://purl.uniprot.org/annotation/VAR_067287|||http://purl.uniprot.org/annotation/VAR_067288|||http://purl.uniprot.org/annotation/VAR_067289|||http://purl.uniprot.org/annotation/VAR_067290|||http://purl.uniprot.org/annotation/VAR_067291|||http://purl.uniprot.org/annotation/VAR_067292|||http://purl.uniprot.org/annotation/VAR_067293|||http://purl.uniprot.org/annotation/VAR_067761|||http://purl.uniprot.org/annotation/VAR_068705|||http://purl.uniprot.org/annotation/VAR_068706|||http://purl.uniprot.org/annotation/VAR_068707|||http://purl.uniprot.org/annotation/VAR_068708|||http://purl.uniprot.org/annotation/VAR_068709|||http://purl.uniprot.org/annotation/VAR_076352|||http://purl.uniprot.org/annotation/VAR_076353|||http://purl.uniprot.org/annotation/VAR_076354|||http://purl.uniprot.org/annotation/VAR_076355|||http://purl.uniprot.org/annotation/VAR_079822|||http://purl.uniprot.org/annotation/VAR_079823|||http://purl.uniprot.org/annotation/VAR_079824|||http://purl.uniprot.org/annotation/VAR_079825|||http://purl.uniprot.org/annotation/VSP_045536
http://togogenome.org/gene/9606:GGNBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3C7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Gametogenetin-binding protein 2|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239348|||http://purl.uniprot.org/annotation/VSP_019175|||http://purl.uniprot.org/annotation/VSP_019176|||http://purl.uniprot.org/annotation/VSP_019177|||http://purl.uniprot.org/annotation/VSP_019178
http://togogenome.org/gene/9606:ARHGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07960                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CRAL-TRIO|||Disordered|||Involved in G-protein binding to GAPs|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Rho GTPase-activating protein 1|||Rho-GAP|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056700|||http://purl.uniprot.org/annotation/VAR_049137
http://togogenome.org/gene/9606:SIRPB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9KV29|||http://purl.uniprot.org/uniprot/O00241|||http://purl.uniprot.org/uniprot/Q5TFQ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like C1-type 1|||Ig-like C1-type 2|||Ig-like V-type|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Signal-regulatory protein beta-1|||Signal-regulatory protein beta-1 isoform 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014956|||http://purl.uniprot.org/annotation/PRO_0000349108|||http://purl.uniprot.org/annotation/PRO_5003622143|||http://purl.uniprot.org/annotation/VAR_028789|||http://purl.uniprot.org/annotation/VAR_028790|||http://purl.uniprot.org/annotation/VAR_028791|||http://purl.uniprot.org/annotation/VAR_028792|||http://purl.uniprot.org/annotation/VAR_056077|||http://purl.uniprot.org/annotation/VAR_059411|||http://purl.uniprot.org/annotation/VSP_007026
http://togogenome.org/gene/9606:SLC25A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMK1|||http://purl.uniprot.org/uniprot/F6SL11|||http://purl.uniprot.org/uniprot/O95258                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Brain mitochondrial carrier protein 1|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 3.|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090677|||http://purl.uniprot.org/annotation/PRO_5002800917|||http://purl.uniprot.org/annotation/VAR_050138|||http://purl.uniprot.org/annotation/VSP_003272|||http://purl.uniprot.org/annotation/VSP_003273
http://togogenome.org/gene/9606:DPY30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIS3|||http://purl.uniprot.org/uniprot/Q9C005                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Region|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Protein dpy-30 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114683
http://togogenome.org/gene/9606:IGSF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5DX21                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||Immunoglobulin superfamily member 11|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317370|||http://purl.uniprot.org/annotation/VAR_038516|||http://purl.uniprot.org/annotation/VAR_038517|||http://purl.uniprot.org/annotation/VAR_056048|||http://purl.uniprot.org/annotation/VSP_030936|||http://purl.uniprot.org/annotation/VSP_030937
http://togogenome.org/gene/9606:EDIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43854                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like repeat and discoidin I-like domain-containing protein 3|||F5/8 type C 1|||F5/8 type C 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc...) threonine|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007522|||http://purl.uniprot.org/annotation/VSP_050006|||http://purl.uniprot.org/annotation/VSP_050007
http://togogenome.org/gene/9606:PCSK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RQD9|||http://purl.uniprot.org/uniprot/H7BXT3|||http://purl.uniprot.org/uniprot/P29122|||http://purl.uniprot.org/uniprot/Q59H04                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  CRM (Cys-rich motif)|||Cell attachment site|||Charge relay system|||Cleavage; by autolysis|||Disordered|||FU 1|||FU 2|||FU 3|||FU 4|||FU 5|||In isoform PACE4A-II and isoform PACE4E-II.|||In isoform PACE4B.|||In isoform PACE4C.|||In isoform PACE4CS.|||In isoform PACE4D.|||In isoform PACE4E-I and isoform PACE4E-II.|||N-linked (GlcNAc...) asparagine|||P/Homo B|||PLAC|||Peptidase S8|||Peptidase S8 pro-domain|||Peptidase S8/S53|||Pro residues|||Proprotein convertase subtilisin/kexin type 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027110|||http://purl.uniprot.org/annotation/PRO_0000027111|||http://purl.uniprot.org/annotation/VAR_051824|||http://purl.uniprot.org/annotation/VSP_005427|||http://purl.uniprot.org/annotation/VSP_005428|||http://purl.uniprot.org/annotation/VSP_005429|||http://purl.uniprot.org/annotation/VSP_005430|||http://purl.uniprot.org/annotation/VSP_005431|||http://purl.uniprot.org/annotation/VSP_005432|||http://purl.uniprot.org/annotation/VSP_005433|||http://purl.uniprot.org/annotation/VSP_005434|||http://purl.uniprot.org/annotation/VSP_005435|||http://purl.uniprot.org/annotation/VSP_005436|||http://purl.uniprot.org/annotation/VSP_005437
http://togogenome.org/gene/9606:LRIT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MR64|||http://purl.uniprot.org/uniprot/Q3SXY7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Fibronectin type-III|||Found in a patient with non-syndromic craniosynostosis; unknown pathological significance.|||Helical|||Ig-like|||In CSNB1F.|||In isoform 2.|||In one non-syndromic craniosynostosis patient; unknown pathological significance.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on LRIT3 function.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309284|||http://purl.uniprot.org/annotation/VAR_036927|||http://purl.uniprot.org/annotation/VAR_036928|||http://purl.uniprot.org/annotation/VAR_036929|||http://purl.uniprot.org/annotation/VAR_061317|||http://purl.uniprot.org/annotation/VAR_069133|||http://purl.uniprot.org/annotation/VAR_069134|||http://purl.uniprot.org/annotation/VAR_069746|||http://purl.uniprot.org/annotation/VAR_081904|||http://purl.uniprot.org/annotation/VSP_029126|||http://purl.uniprot.org/annotation/VSP_029127
http://togogenome.org/gene/9606:SUSD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92537                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Polar residues|||Sushi|||Sushi domain-containing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013985
http://togogenome.org/gene/9606:SP100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23497|||http://purl.uniprot.org/uniprot/Q6ZMK3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||D-box; recognition signal for CDC20-mediated degradation|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HMG box 1|||HMG box 2|||HSR|||In isoform 6.|||In isoform 7.|||In isoform Sp100-A, isoform 6 and isoform 7.|||In isoform Sp100-B.|||In isoform Sp100-C.|||In isoform SpAlt-C.|||N-acetylalanine|||Nuclear autoantigen Sp-100|||Nuclear localization signal|||PHD-type|||Phosphoserine|||Polar residues|||Prevents CDC20-mediated degradation; when associated with Ala-165.|||Prevents CDC20-mediated degradation; when associated with Ala-168.|||PxVxL motif|||Removed|||SAND|||Sufficient to mediate interaction with ETS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074096|||http://purl.uniprot.org/annotation/VAR_005621|||http://purl.uniprot.org/annotation/VAR_005622|||http://purl.uniprot.org/annotation/VAR_034510|||http://purl.uniprot.org/annotation/VSP_005978|||http://purl.uniprot.org/annotation/VSP_005979|||http://purl.uniprot.org/annotation/VSP_005980|||http://purl.uniprot.org/annotation/VSP_005981|||http://purl.uniprot.org/annotation/VSP_005982|||http://purl.uniprot.org/annotation/VSP_005983|||http://purl.uniprot.org/annotation/VSP_005984|||http://purl.uniprot.org/annotation/VSP_045868|||http://purl.uniprot.org/annotation/VSP_045869|||http://purl.uniprot.org/annotation/VSP_045870
http://togogenome.org/gene/9606:BARHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  BarH-like 1 homeobox protein|||Basic and acidic residues|||Disordered|||Homeobox|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048826
http://togogenome.org/gene/9606:C2CD4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1M9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  C2|||C2 calcium-dependent domain-containing protein 4D|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394960
http://togogenome.org/gene/9606:PTPN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43378|||http://purl.uniprot.org/uniprot/Q6IQ43                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||Disordered|||N-acetylmethionine|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094764
http://togogenome.org/gene/9606:NEK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V454|||http://purl.uniprot.org/uniprot/A0A7I2V5R1|||http://purl.uniprot.org/uniprot/Q6PKF2|||http://purl.uniprot.org/uniprot/Q8TD19                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In APUG.|||In NC; increased autophosphorylation at T-210.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||Interaction with NEK6|||Loss of activity and autophosphorylation.|||N-acetylserine|||No effect on autophosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||Removed|||Serine/threonine-protein kinase Nek9|||Significant reduction of autophosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086435|||http://purl.uniprot.org/annotation/VAR_027900|||http://purl.uniprot.org/annotation/VAR_040926|||http://purl.uniprot.org/annotation/VAR_040927|||http://purl.uniprot.org/annotation/VAR_077801|||http://purl.uniprot.org/annotation/VAR_077802|||http://purl.uniprot.org/annotation/VAR_077803
http://togogenome.org/gene/9606:CIAO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6Q4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytosolic iron-sulfur assembly component 3|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288485|||http://purl.uniprot.org/annotation/VAR_053911|||http://purl.uniprot.org/annotation/VAR_053912|||http://purl.uniprot.org/annotation/VSP_025694|||http://purl.uniprot.org/annotation/VSP_025695
http://togogenome.org/gene/9606:MTTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7X3|||http://purl.uniprot.org/uniprot/P55157                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Does not inhibit apolipoprotein B secretion.|||Does not inhibit triglyceride transfer activity and apolipoprotein B secretion.|||Does not inhibit triglyceride transfer activity.|||In ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity.|||In ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion.|||In ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion.|||In ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity.|||In ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion.|||In ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity.|||In ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity.|||In isoform 2.|||Inhibits triglyceride transfer activity.|||Microsomal triglyceride transfer protein large subunit|||No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB or P4HB/PDI, does partially reduce phospholipid or triglyceride transfer activity and apolipoprotein B secretion.|||No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion.|||No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion.|||No loss on localization to the endoplasmic reticulum. Does not inhibit triglyceride transfer activity.|||No loss on localization to the endoplasmic reticulum. Inhibits triglyceride transfer activity.|||No loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; reduces phospholipid or triglyceride transfer activity; does not inhibit apolipoprotein B secretion.|||Strongly reduces triglyceride transfer activity.|||Vitellogenin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041593|||http://purl.uniprot.org/annotation/VAR_010640|||http://purl.uniprot.org/annotation/VAR_010641|||http://purl.uniprot.org/annotation/VAR_010642|||http://purl.uniprot.org/annotation/VAR_010643|||http://purl.uniprot.org/annotation/VAR_010644|||http://purl.uniprot.org/annotation/VAR_014016|||http://purl.uniprot.org/annotation/VAR_014017|||http://purl.uniprot.org/annotation/VAR_014018|||http://purl.uniprot.org/annotation/VAR_014019|||http://purl.uniprot.org/annotation/VAR_022658|||http://purl.uniprot.org/annotation/VAR_052961|||http://purl.uniprot.org/annotation/VAR_052962|||http://purl.uniprot.org/annotation/VAR_074553|||http://purl.uniprot.org/annotation/VAR_074554|||http://purl.uniprot.org/annotation/VAR_074555|||http://purl.uniprot.org/annotation/VAR_074556|||http://purl.uniprot.org/annotation/VAR_074557|||http://purl.uniprot.org/annotation/VAR_074558|||http://purl.uniprot.org/annotation/VSP_056325|||http://purl.uniprot.org/annotation/VSP_056326
http://togogenome.org/gene/9606:CFAP61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHU2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 61|||Disordered|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079417|||http://purl.uniprot.org/annotation/VAR_027981|||http://purl.uniprot.org/annotation/VAR_027982|||http://purl.uniprot.org/annotation/VAR_027983|||http://purl.uniprot.org/annotation/VAR_027984|||http://purl.uniprot.org/annotation/VAR_027985|||http://purl.uniprot.org/annotation/VAR_027986|||http://purl.uniprot.org/annotation/VAR_027987|||http://purl.uniprot.org/annotation/VAR_069396|||http://purl.uniprot.org/annotation/VSP_003798|||http://purl.uniprot.org/annotation/VSP_003799|||http://purl.uniprot.org/annotation/VSP_003800|||http://purl.uniprot.org/annotation/VSP_003802|||http://purl.uniprot.org/annotation/VSP_003803|||http://purl.uniprot.org/annotation/VSP_003804|||http://purl.uniprot.org/annotation/VSP_013682|||http://purl.uniprot.org/annotation/VSP_013683
http://togogenome.org/gene/9606:MED12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93074                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Found in a family with X-linked intellectual disability; unknown pathological significance.|||In HDKR.|||In MRXSLF.|||In OHDOX.|||In OKS.|||In isoform 2.|||In isoform 3.|||Interaction with CTNNB1 and GLI3|||Mediator of RNA polymerase II transcription subunit 12|||N6-acetyllysine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096359|||http://purl.uniprot.org/annotation/VAR_033112|||http://purl.uniprot.org/annotation/VAR_037534|||http://purl.uniprot.org/annotation/VAR_046672|||http://purl.uniprot.org/annotation/VAR_069770|||http://purl.uniprot.org/annotation/VAR_069771|||http://purl.uniprot.org/annotation/VAR_069772|||http://purl.uniprot.org/annotation/VAR_074018|||http://purl.uniprot.org/annotation/VAR_086496|||http://purl.uniprot.org/annotation/VAR_086497|||http://purl.uniprot.org/annotation/VAR_086498|||http://purl.uniprot.org/annotation/VSP_035520|||http://purl.uniprot.org/annotation/VSP_035521
http://togogenome.org/gene/9606:UAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16222                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 3.|||In isoform AGX1.|||Substrate binding|||UDP-N-acetylhexosamine pyrophosphorylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185767|||http://purl.uniprot.org/annotation/VAR_014935|||http://purl.uniprot.org/annotation/VSP_004483|||http://purl.uniprot.org/annotation/VSP_014523
http://togogenome.org/gene/9606:FKBP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q658U4|||http://purl.uniprot.org/uniprot/Q8NAG5|||http://purl.uniprot.org/uniprot/Q96AY3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||In BRKS1.|||In OI11.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PPIase FKBP-type|||PPIase FKBP-type 1|||PPIase FKBP-type 2|||PPIase FKBP-type 3|||PPIase FKBP-type 4|||Peptidyl-prolyl cis-trans isomerase FKBP10|||Prevents secretion from ER|||peptidylprolyl isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025517|||http://purl.uniprot.org/annotation/PRO_5004267956|||http://purl.uniprot.org/annotation/PRO_5004314246|||http://purl.uniprot.org/annotation/VAR_050625|||http://purl.uniprot.org/annotation/VAR_063601|||http://purl.uniprot.org/annotation/VAR_069902|||http://purl.uniprot.org/annotation/VAR_069903|||http://purl.uniprot.org/annotation/VAR_069904|||http://purl.uniprot.org/annotation/VSP_056425|||http://purl.uniprot.org/annotation/VSP_056426|||http://purl.uniprot.org/annotation/VSP_056427|||http://purl.uniprot.org/annotation/VSP_056428
http://togogenome.org/gene/9606:LHFPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WI0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||LHFPL tetraspan subfamily member 1 protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244760|||http://purl.uniprot.org/annotation/VSP_019616|||http://purl.uniprot.org/annotation/VSP_019617
http://togogenome.org/gene/9606:TIMM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQS5|||http://purl.uniprot.org/uniprot/A0A1W2PRH9|||http://purl.uniprot.org/uniprot/G3V502|||http://purl.uniprot.org/uniprot/Q9Y5J7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Strand                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit Tim9|||N-acetylalanine|||Removed|||Tim10-like|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193595
http://togogenome.org/gene/9606:RELA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0W8|||http://purl.uniprot.org/uniprot/Q04206                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Phosphoserine|||9aaTAD|||Abolishes interaction with PIN1.|||Cysteine persulfide; alternate|||Disordered|||Found in a patient diagnosed with autoimmune lymphoproliferative syndrome; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of phosphorylation.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-acetyllysine; by PCAF and EP300; alternate|||N6-methyllysine; by SETD6; alternate|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by IKKB|||Phosphoserine; by IKKB and IKKE|||Phosphoserine; by PKC/PRKCZ|||Phosphoserine; by RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by CHEK1|||RHD|||S-nitrosocysteine; alternate|||Transcription factor p65|||Transcriptional activation domain 1|||Transcriptional activation domain 2|||Transcriptional activation domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205169|||http://purl.uniprot.org/annotation/VAR_081858|||http://purl.uniprot.org/annotation/VSP_005587|||http://purl.uniprot.org/annotation/VSP_005588|||http://purl.uniprot.org/annotation/VSP_012031|||http://purl.uniprot.org/annotation/VSP_031245
http://togogenome.org/gene/9606:NUDT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXY7|||http://purl.uniprot.org/uniprot/O95848                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Strand                                                                                  ^@                                                                                  Nudix box|||Nudix hydrolase|||Uridine diphosphate glucose pyrophosphatase NUDT14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057113
http://togogenome.org/gene/9606:PARM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWI2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Prostate androgen-regulated mucin-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045498|||http://purl.uniprot.org/annotation/VAR_062257
http://togogenome.org/gene/9606:SUMF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBJ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes endoplasmic reticulum retention.|||Abolishes interaction with and inhibition of SUMF1. Can still form homodimers.|||Disordered|||Does not affect endoplasmic reticulum retention.|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inactive C-alpha-formylglycine-generating enzyme 2|||N-linked (GlcNAc...) asparagine|||Non-canonical ER retention motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033459|||http://purl.uniprot.org/annotation/VAR_046951|||http://purl.uniprot.org/annotation/VAR_080774|||http://purl.uniprot.org/annotation/VSP_007878|||http://purl.uniprot.org/annotation/VSP_007879|||http://purl.uniprot.org/annotation/VSP_007880|||http://purl.uniprot.org/annotation/VSP_040878
http://togogenome.org/gene/9606:TTPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49638                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-tocopherol transfer protein|||CRAL-TRIO|||Disordered|||In AVED.|||In AVED; mild and slowly progressive form of the disease.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210764|||http://purl.uniprot.org/annotation/VAR_005668|||http://purl.uniprot.org/annotation/VAR_007858|||http://purl.uniprot.org/annotation/VAR_022388|||http://purl.uniprot.org/annotation/VAR_022389|||http://purl.uniprot.org/annotation/VAR_022390|||http://purl.uniprot.org/annotation/VAR_022391|||http://purl.uniprot.org/annotation/VAR_022392|||http://purl.uniprot.org/annotation/VAR_037973
http://togogenome.org/gene/9606:C12orf60                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5U649                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C12orf60                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274271|||http://purl.uniprot.org/annotation/VAR_030226|||http://purl.uniprot.org/annotation/VAR_030227|||http://purl.uniprot.org/annotation/VAR_030228
http://togogenome.org/gene/9606:MYO7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIF6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||FERM 1|||FERM 2|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||In isoform 2.|||Mediates interaction with ANKS4B|||Mediates interaction with CDHR2, CDHR5 and USH1C|||MyTH4 1|||MyTH4 2|||MyTH4 3|||Myosin motor|||Phosphoserine|||SH3|||Unconventional myosin-VIIb                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329046|||http://purl.uniprot.org/annotation/VAR_042626|||http://purl.uniprot.org/annotation/VAR_042627|||http://purl.uniprot.org/annotation/VAR_042628|||http://purl.uniprot.org/annotation/VAR_042629|||http://purl.uniprot.org/annotation/VSP_032930|||http://purl.uniprot.org/annotation/VSP_032931
http://togogenome.org/gene/9606:LOX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D0PNI2|||http://purl.uniprot.org/uniprot/P28300                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Abolishes sulfation and reduces binding to collagen; when associated with 183-F-F-184 and 186-F-F-187.|||Abolishes sulfation and reduces binding to collagen; when associated with 183-F-F-184 and F-190.|||Abolishes sulfation and reduces binding to collagen; when associated with 186-F-F-187 and F-190.|||Cleavage; by ADAMTS2 and ADAMTS14|||Disordered|||In AAT10.|||In AAT10; 21% decrease of lysyl oxidase activity.|||In AAT10; 50% decrease of lysyl oxidase activity.|||In AAT10; unknown pathological significance.|||In AAT10; unknown pathological significance; 8% decrease of lysyl oxidase activity.|||Lysine tyrosylquinone (Lys-Tyr)|||Lysyl oxidase homolog|||Lysyl-oxidase like|||N-linked (GlcNAc...) asparagine|||Protein-lysine 6-oxidase, long form|||Protein-lysine 6-oxidase, short form|||Removed by BMP1|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018520|||http://purl.uniprot.org/annotation/PRO_0000018521|||http://purl.uniprot.org/annotation/PRO_0000447885|||http://purl.uniprot.org/annotation/PRO_5014302415|||http://purl.uniprot.org/annotation/VAR_004282|||http://purl.uniprot.org/annotation/VAR_077534|||http://purl.uniprot.org/annotation/VAR_077535|||http://purl.uniprot.org/annotation/VAR_077536|||http://purl.uniprot.org/annotation/VAR_077537|||http://purl.uniprot.org/annotation/VAR_077538|||http://purl.uniprot.org/annotation/VAR_077539|||http://purl.uniprot.org/annotation/VAR_077540
http://togogenome.org/gene/9606:MDM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTR9|||http://purl.uniprot.org/uniprot/A0A087WUE3|||http://purl.uniprot.org/uniprot/A0A087WZ58|||http://purl.uniprot.org/uniprot/O15151|||http://purl.uniprot.org/uniprot/Q59FS6|||http://purl.uniprot.org/uniprot/Q68DC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DM2|||Disordered|||Fails to interact with MDM2.|||In BMFS6; altered capacity to interact with MDM2 RING domain in a yeast two-hybrid assay; no effect on ATP binding; expressed at lower levels than wild-type; when expressed in a mouse model, leads to increased TP53 activity, decreased telomerase length and ultimately to bone marrow failure.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform HDMX211.|||Necessary for interaction with USP2|||Nuclear localization signal|||Phosphoserine; by CHEK1 and CHEK2|||Phosphoserine; by CHEK2|||Polar residues|||Protein Mdm4|||RING-type|||RanBP2-type|||Region II|||SWIB/MDM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000157336|||http://purl.uniprot.org/annotation/VAR_017106|||http://purl.uniprot.org/annotation/VAR_017107|||http://purl.uniprot.org/annotation/VAR_084553|||http://purl.uniprot.org/annotation/VSP_035669|||http://purl.uniprot.org/annotation/VSP_035670|||http://purl.uniprot.org/annotation/VSP_042563|||http://purl.uniprot.org/annotation/VSP_043145
http://togogenome.org/gene/9606:IL17F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PD4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In CANDF6.|||Interchain (with C-137)|||Interchain (with C-47)|||Interleukin-17F|||N-linked (GlcNAc...) asparagine|||Significantly decreases the affinity for IL17RA and IL17RC by nearly 5-fold and 200-fold, respectively.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015432|||http://purl.uniprot.org/annotation/VAR_058287|||http://purl.uniprot.org/annotation/VAR_058288|||http://purl.uniprot.org/annotation/VAR_058289|||http://purl.uniprot.org/annotation/VAR_065813
http://togogenome.org/gene/9606:GAL3ST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99999                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Galactosylceramide sulfotransferase|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085201|||http://purl.uniprot.org/annotation/VAR_013684
http://togogenome.org/gene/9606:SLC11A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0X8GKR4|||http://purl.uniprot.org/uniprot/P49281                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes N-glycosylation; when associated with A-338. Does not affect endosome targeting; when associated with A-338. Impairs sorting to the apical membrane; when associated with A-338.|||Abolishes N-glycosylation; when associated with A-351. Does not affect endosome targeting; when associated with A-351. Impairs sorting to the apical membrane; when associated with A-351.|||Abolishes localization at early endosomes and leads to localization at late endosomes and lysosomes.|||Abolishes metal ion transport.|||Cytoplasmic|||Decreases affinity for divalent metal cations. Impairs metal ion transport.|||Disordered|||Extracellular|||Helical|||In AHMIO1.|||In AHMIO1; increased skipping of exon 12.|||In a colorectal cancer sample; somatic mutation.|||In isoform 1, isoform 3 and isoform 5.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Natural resistance-associated macrophage protein 2|||Phosphoserine|||Polar residues|||Required for early endosome targeting                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212594|||http://purl.uniprot.org/annotation/VAR_008882|||http://purl.uniprot.org/annotation/VAR_033011|||http://purl.uniprot.org/annotation/VAR_033012|||http://purl.uniprot.org/annotation/VAR_033013|||http://purl.uniprot.org/annotation/VAR_033014|||http://purl.uniprot.org/annotation/VAR_036434|||http://purl.uniprot.org/annotation/VSP_003595|||http://purl.uniprot.org/annotation/VSP_038144|||http://purl.uniprot.org/annotation/VSP_046058
http://togogenome.org/gene/9606:PIEZO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H5I5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Helical|||In DA3.|||In DA5.|||In DA5; causes slowing of inactivation of PIEZO2-dependent mechanically activated currents as well as significantly faster recovery from inactivation compared to wild-type.|||In DA5; recovers faster from inactivation.|||In DAIPT.|||In MWKS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Piezo-type mechanosensitive ion channel component 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186818|||http://purl.uniprot.org/annotation/VAR_033925|||http://purl.uniprot.org/annotation/VAR_070938|||http://purl.uniprot.org/annotation/VAR_071039|||http://purl.uniprot.org/annotation/VAR_071302|||http://purl.uniprot.org/annotation/VAR_071303|||http://purl.uniprot.org/annotation/VAR_071304|||http://purl.uniprot.org/annotation/VAR_071305|||http://purl.uniprot.org/annotation/VAR_071306|||http://purl.uniprot.org/annotation/VAR_071817|||http://purl.uniprot.org/annotation/VAR_071818|||http://purl.uniprot.org/annotation/VAR_077843|||http://purl.uniprot.org/annotation/VSP_040471|||http://purl.uniprot.org/annotation/VSP_040472|||http://purl.uniprot.org/annotation/VSP_040630
http://togogenome.org/gene/9606:RIMOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDU8                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  N-acetylalanine|||RAB7A-interacting MON1-CCZ1 complex subunit 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341214|||http://purl.uniprot.org/annotation/VAR_044032
http://togogenome.org/gene/9606:CLDN17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56750                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-17|||Cytoplasmic|||Decreased anion selectivity. Increased permeabilities not only for chloride, but also for sodium and thiocyanate. No effect on transepithelial resistance.|||Decreased anion selectivity. No effect on transepithelial resistance.|||Decreased transepithelial resistance and anion selectivity.|||Decreased transepithelial resistance and anion selectivity. Higher permeability to chloride, sodium and also to larger anions, including pyruvate, nitrate, and thiocyanate.|||Decreased transepithelial resistance, no effect on anion selectivity.|||Extracellular|||Helical|||Increased transepithelial resistance. Loss of anion selectivity in favor of cation (sodium) selectivity.|||Increased transepithelial resistance. No effect on localization to cell-cell junctions.|||Loss of anion selectivity. Strongly increased permeabilities not only for chloride, but also for sodium and the larger anions, including pyruvate, nitrate and thiocyanate. No effect on localization to cell-cell junctions.|||No effect on channel formation ability. Loss of anion selectivity in favor of cation selectivity. No effect on transepithelial resistance.|||No effect on transepithelial resistance, nor on anion selectivity. Elevated permeabilities not only for chloride, but also for sodium and the larger anions, including pyruvate, nitrate and thiocyanate.|||No effect on transepithelial resistance, nor on anion selectivity. Increased permeability for thiocyanate.|||Reduced channel formation ability. Increased transepithelial resistance. Loss of anion selectivity in favor of cation selectivity.|||Strongly reduced channel formation ability. Increased transepithelial resistance. Loss of anion selectivity in favor of cation selectivity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144777|||http://purl.uniprot.org/annotation/VAR_033774
http://togogenome.org/gene/9606:EFNB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52799                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Complete loss of Nipah protein G binding.|||Cytoplasmic|||Disordered|||Ephrin RBD|||Ephrin-B2|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008392
http://togogenome.org/gene/9606:BTBD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z503|||http://purl.uniprot.org/uniprot/D3DQW7|||http://purl.uniprot.org/uniprot/Q9BSF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein 10|||Basic and acidic residues|||Disordered|||In isoform 2.|||Interaction with AKT family members|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228985|||http://purl.uniprot.org/annotation/VAR_033638|||http://purl.uniprot.org/annotation/VSP_055552
http://togogenome.org/gene/9606:SPRY4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFS6|||http://purl.uniprot.org/uniprot/Q9C004                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In HH17; phenotype consistent with Kallmann syndrome.|||In HH17; rare variant associated with susceptibility to disease; some patients have a second mutation in another HH-associated gene including DUSP6 and FGFR1.|||In HH17; without anosmia.|||In isoform C.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein sprouty homolog 4|||Required for interaction with TESK1. Required for colocalization with TESK1 at vesicular spots in the cytoplasm and inhibition of TESK1 kinase activity, resulting in inhibition of cell spreading|||SPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076905|||http://purl.uniprot.org/annotation/VAR_069929|||http://purl.uniprot.org/annotation/VAR_069930|||http://purl.uniprot.org/annotation/VAR_069931|||http://purl.uniprot.org/annotation/VAR_069932|||http://purl.uniprot.org/annotation/VAR_069933|||http://purl.uniprot.org/annotation/VAR_069934|||http://purl.uniprot.org/annotation/VAR_069935|||http://purl.uniprot.org/annotation/VSP_006219|||http://purl.uniprot.org/annotation/VSP_006220
http://togogenome.org/gene/9606:PSIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75475                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Integrase-binding domain (IBD)|||Loss of interaction with human HIV-1 integrase and POGZ; reduced interaction with CDCA7L.|||Loss of interaction with human HIV-1 integrase; no effect on interaction with CDCA7L and POGZ.|||Loss of interaction with human HIV-1 integrase; no effect on interaction with KMT2A.|||Loss of interaction with human HIV-1 integrase; reduced interaction with POGZ and CDCA7L.|||Nuclear localization signal|||PC4 and SFRS1-interacting protein|||PWWP|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced interaction with KMT2A. Significant loss of interaction with KMT2A; when associated with A-368.|||Reduced interaction with KMT2A. Significant loss of interaction with KMT2A; when associated with D-407.|||Reduced interaction with POGZ, CDCA7L and human HIV-1 integrase.|||Reduced interaction with human HIV-1 integrase; no effect on interaction with POGZ and CDCA7L.|||Significant loss of interaction with KMT2A; when associated with D-404.|||Significant loss of interaction with KMT2A; when associated with D-405.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191708|||http://purl.uniprot.org/annotation/VSP_014297|||http://purl.uniprot.org/annotation/VSP_014298|||http://purl.uniprot.org/annotation/VSP_044435
http://togogenome.org/gene/9606:CADPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0E5|||http://purl.uniprot.org/uniprot/Q9ULU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2|||Calcium-dependent secretion activator 1|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with DRD2|||MHD1|||Mediates targeting and association with DCVs|||PH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053864|||http://purl.uniprot.org/annotation/VSP_016801|||http://purl.uniprot.org/annotation/VSP_016802|||http://purl.uniprot.org/annotation/VSP_016803|||http://purl.uniprot.org/annotation/VSP_016804|||http://purl.uniprot.org/annotation/VSP_016805|||http://purl.uniprot.org/annotation/VSP_016806|||http://purl.uniprot.org/annotation/VSP_016807|||http://purl.uniprot.org/annotation/VSP_016808
http://togogenome.org/gene/9606:DEFB104B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTQ1                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-defensin 104                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006973|||http://purl.uniprot.org/annotation/VAR_024767
http://togogenome.org/gene/9606:FIBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43427                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic fibroblast growth factor intracellular-binding protein|||In TROFAS.|||In isoform Short.|||N-acetylthreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087237|||http://purl.uniprot.org/annotation/VAR_050991|||http://purl.uniprot.org/annotation/VAR_050992|||http://purl.uniprot.org/annotation/VAR_060711|||http://purl.uniprot.org/annotation/VAR_077160|||http://purl.uniprot.org/annotation/VSP_004250
http://togogenome.org/gene/9606:PSMD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51665                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||MPN|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213943
http://togogenome.org/gene/9606:ENHO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWT2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Adropin|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292879|||http://purl.uniprot.org/annotation/VSP_026454
http://togogenome.org/gene/9606:NCR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14931|||http://purl.uniprot.org/uniprot/Q05D23                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In isoform 2 and isoform 5.|||In isoform 3 and isoform 6.|||In isoform 4, isoform 5 and isoform 6.|||N-linked (GlcNAc...) asparagine|||Natural cytotoxicity triggering receptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015032|||http://purl.uniprot.org/annotation/PRO_5014306692|||http://purl.uniprot.org/annotation/VAR_044114|||http://purl.uniprot.org/annotation/VAR_044115|||http://purl.uniprot.org/annotation/VSP_010411|||http://purl.uniprot.org/annotation/VSP_010412|||http://purl.uniprot.org/annotation/VSP_010413
http://togogenome.org/gene/9606:HLA-DQA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01906|||http://purl.uniprot.org/uniprot/Q76NI6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DQ alpha 2 chain|||Helical|||Ig-like|||Ig-like C1-type|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018973|||http://purl.uniprot.org/annotation/PRO_5007710552|||http://purl.uniprot.org/annotation/VAR_033431|||http://purl.uniprot.org/annotation/VAR_050392
http://togogenome.org/gene/9606:USP17L24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:ODAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M63                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In CILD20; expressed at very low levels in patients' nasal epithelial cells; the genetic variation producing this missense variant predominantly affects splicing.|||In isoform 2.|||In isoform 3.|||Outer dynein arm-docking complex subunit 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288807|||http://purl.uniprot.org/annotation/VAR_032501|||http://purl.uniprot.org/annotation/VAR_032502|||http://purl.uniprot.org/annotation/VAR_086948|||http://purl.uniprot.org/annotation/VSP_036212|||http://purl.uniprot.org/annotation/VSP_036213|||http://purl.uniprot.org/annotation/VSP_036214
http://togogenome.org/gene/9606:CH25H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95992                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cholesterol 25-hydroxylase|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||Loss of cholesterol 25-hydroxylase activity. Loss of inhibition of infection by SARS-COV-2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226801|||http://purl.uniprot.org/annotation/VAR_048899
http://togogenome.org/gene/9606:TMEM52B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4KMG9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Transmembrane protein 52B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294448|||http://purl.uniprot.org/annotation/VSP_026640
http://togogenome.org/gene/9606:GAGE13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4V321                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G antigen 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252476
http://togogenome.org/gene/9606:RNFT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||E3 ubiquitin-protein ligase RNFT2|||Extracellular|||Helical|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Loss of E3 ubiquitin-protein ligase activity.|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279508|||http://purl.uniprot.org/annotation/VSP_023465|||http://purl.uniprot.org/annotation/VSP_023466|||http://purl.uniprot.org/annotation/VSP_035513|||http://purl.uniprot.org/annotation/VSP_035514|||http://purl.uniprot.org/annotation/VSP_035515|||http://purl.uniprot.org/annotation/VSP_035516
http://togogenome.org/gene/9606:ACSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1RMZ4|||http://purl.uniprot.org/uniprot/Q9NUB1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  AMP-dependent synthetase/ligase|||Acetyl-coenzyme A synthetase 2-like, mitochondrial|||Acetyl-coenzyme A synthetase N-terminal|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of activity.|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000596|||http://purl.uniprot.org/annotation/VAR_048184|||http://purl.uniprot.org/annotation/VSP_007249|||http://purl.uniprot.org/annotation/VSP_044693|||http://purl.uniprot.org/annotation/VSP_044694|||http://purl.uniprot.org/annotation/VSP_045546|||http://purl.uniprot.org/annotation/VSP_045547
http://togogenome.org/gene/9606:VSIG10L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a family with Barrett esophagus and esophageal adenocarcinoma; unknown pathological significance.|||Found in esophageal adenocarcinoma; somatic mutation; unknown pathological significance.|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||V-set and immunoglobulin domain-containing protein 10-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395117|||http://purl.uniprot.org/annotation/VAR_063282|||http://purl.uniprot.org/annotation/VAR_063283|||http://purl.uniprot.org/annotation/VAR_063284|||http://purl.uniprot.org/annotation/VAR_063285|||http://purl.uniprot.org/annotation/VAR_080077|||http://purl.uniprot.org/annotation/VAR_080078|||http://purl.uniprot.org/annotation/VSP_039374
http://togogenome.org/gene/9606:NT5M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPB1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Secondary Structure|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  5'(3')-deoxyribonucleotidase, mitochondrial|||Mitochondrion|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000011
http://togogenome.org/gene/9606:ZNF425                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7U3|||http://purl.uniprot.org/uniprot/Q6IV72                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||KRAB-related|||Zinc finger protein 425                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234577|||http://purl.uniprot.org/annotation/VAR_033565
http://togogenome.org/gene/9606:CXCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19875                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-X-C motif chemokine 2|||GRO-beta(5-73)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005063|||http://purl.uniprot.org/annotation/PRO_0000005064
http://togogenome.org/gene/9606:SLC30A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXX8|||http://purl.uniprot.org/uniprot/Q99726                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased homodimerization. Decreased localization to intracellular vesicles. Loss of zinc transporter activity.|||Disordered|||Dityrosine (Tyr-Tyr) (interchain with Y-357)|||Dityrosine (Tyr-Tyr) (interchain with Y-372)|||Helical|||Increased homodimerization. Increased localization to intracellular vesicles.|||Lumenal|||May be associated with increased risk for febrile seizures; decreased zinc transport; decreased localization to synaptic vesicles.|||No effect on homodimerization.|||Probable proton-coupled zinc antiporter SLC30A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206096|||http://purl.uniprot.org/annotation/VAR_077209
http://togogenome.org/gene/9606:ARPC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D275|||http://purl.uniprot.org/uniprot/O15143                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Actin-related protein 2/3 complex subunit 1B|||In IMD71; unknown pathological significance.|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050855|||http://purl.uniprot.org/annotation/VAR_014477|||http://purl.uniprot.org/annotation/VAR_080353|||http://purl.uniprot.org/annotation/VAR_080354
http://togogenome.org/gene/9606:KERA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60938                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In CNA2.|||Keratocan|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) (keratan sulfate) asparagine|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032748|||http://purl.uniprot.org/annotation/VAR_012753|||http://purl.uniprot.org/annotation/VAR_012754|||http://purl.uniprot.org/annotation/VAR_013564
http://togogenome.org/gene/9606:OR10C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV80|||http://purl.uniprot.org/uniprot/Q96KK4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150693|||http://purl.uniprot.org/annotation/VAR_037822|||http://purl.uniprot.org/annotation/VAR_037823|||http://purl.uniprot.org/annotation/VAR_037824|||http://purl.uniprot.org/annotation/VAR_037825|||http://purl.uniprot.org/annotation/VAR_037826|||http://purl.uniprot.org/annotation/VAR_037827|||http://purl.uniprot.org/annotation/VAR_037828|||http://purl.uniprot.org/annotation/VAR_037829|||http://purl.uniprot.org/annotation/VAR_037830|||http://purl.uniprot.org/annotation/VAR_037831|||http://purl.uniprot.org/annotation/VAR_037832|||http://purl.uniprot.org/annotation/VAR_037833
http://togogenome.org/gene/9606:NPHP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW36|||http://purl.uniprot.org/uniprot/O75161                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Does not affect interaction with RPGRIP1L; does not affect interaction with RPGRIP1.|||Found in a patient with cardiac laterality defects; fails to rescue heart looping defects in zebrafish knockout.|||Found in a patient with cardiac laterality defects; unknown pathological significance.|||In NPHP4.|||In NPHP4; affects interaction with RPGRIP1L; disrupts interaction with RPGRIP1.|||In NPHP4; also found in a patient with cardiac laterality defects.|||In NPHP4; benign variant.|||In NPHP4; with color blindness.|||In NPHP4; with hearing loss.|||In SLSN4.|||In SLSN4; also found in a patient with cardiac laterality defects; impairs localization to the ciliary transition zone.|||In SLSN4; benign variant.|||In a patient with nephronophthisis with extra-renal features; the patient also carries W-735 in the same gene and L-209 in TTC21B.|||In isoform 2.|||Nephrocystin-4|||Phosphoserine|||Polar residues|||Pro residues|||Sufficient for basal bodies localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159769|||http://purl.uniprot.org/annotation/VAR_015186|||http://purl.uniprot.org/annotation/VAR_015214|||http://purl.uniprot.org/annotation/VAR_015215|||http://purl.uniprot.org/annotation/VAR_022526|||http://purl.uniprot.org/annotation/VAR_022527|||http://purl.uniprot.org/annotation/VAR_022528|||http://purl.uniprot.org/annotation/VAR_022529|||http://purl.uniprot.org/annotation/VAR_022530|||http://purl.uniprot.org/annotation/VAR_022531|||http://purl.uniprot.org/annotation/VAR_022532|||http://purl.uniprot.org/annotation/VAR_022533|||http://purl.uniprot.org/annotation/VAR_022534|||http://purl.uniprot.org/annotation/VAR_022535|||http://purl.uniprot.org/annotation/VAR_022536|||http://purl.uniprot.org/annotation/VAR_022537|||http://purl.uniprot.org/annotation/VAR_022538|||http://purl.uniprot.org/annotation/VAR_022539|||http://purl.uniprot.org/annotation/VAR_022540|||http://purl.uniprot.org/annotation/VAR_022541|||http://purl.uniprot.org/annotation/VAR_022542|||http://purl.uniprot.org/annotation/VAR_022543|||http://purl.uniprot.org/annotation/VAR_022544|||http://purl.uniprot.org/annotation/VAR_022545|||http://purl.uniprot.org/annotation/VAR_022546|||http://purl.uniprot.org/annotation/VAR_022547|||http://purl.uniprot.org/annotation/VAR_022548|||http://purl.uniprot.org/annotation/VAR_037622|||http://purl.uniprot.org/annotation/VAR_037623|||http://purl.uniprot.org/annotation/VAR_065557|||http://purl.uniprot.org/annotation/VAR_076785|||http://purl.uniprot.org/annotation/VAR_076786|||http://purl.uniprot.org/annotation/VAR_076787|||http://purl.uniprot.org/annotation/VAR_076788|||http://purl.uniprot.org/annotation/VAR_076789|||http://purl.uniprot.org/annotation/VAR_076790|||http://purl.uniprot.org/annotation/VAR_076791|||http://purl.uniprot.org/annotation/VAR_079179|||http://purl.uniprot.org/annotation/VSP_054514|||http://purl.uniprot.org/annotation/VSP_054515|||http://purl.uniprot.org/annotation/VSP_054516
http://togogenome.org/gene/9606:SWI5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7C5E9|||http://purl.uniprot.org/uniprot/Q1ZZU3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  DNA repair protein SWI5 homolog|||Disordered|||Does not affect interaction with SFR1/MEI5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324584
http://togogenome.org/gene/9606:MAGT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WU53|||http://purl.uniprot.org/uniprot/Q9H0U3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In CDG1CC; no effect on protein expression; decreased protein N-linked glycosylation of STT3B-specific substrates.|||In CDG1CC; no protein expression; decreased protein N-linked glycosylation of STT3B-specific substrates.|||In XMEN; decreased protein expression.|||In XMEN; no protein expression.|||In XMEN; no protein expression; decreased protein N-linked glycosylation of STT3B-specific substrates.|||In isoform 2.|||Magnesium transporter protein 1|||N-linked (GlcNAc...) asparagine|||Rare variant found in patients with X-linked intellectual disability; unknown pathological significance.|||Redox-active|||Reduces N-glycosylation of cysteine-proximal acceptor sites; when associated with S-87.|||Reduces N-glycosylation of cysteine-proximal acceptor sites; when associated with S-90.|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246057|||http://purl.uniprot.org/annotation/VAR_045837|||http://purl.uniprot.org/annotation/VAR_083418|||http://purl.uniprot.org/annotation/VAR_083419|||http://purl.uniprot.org/annotation/VAR_083420|||http://purl.uniprot.org/annotation/VAR_083421|||http://purl.uniprot.org/annotation/VAR_083422|||http://purl.uniprot.org/annotation/VSP_056556|||http://purl.uniprot.org/annotation/VSP_056557
http://togogenome.org/gene/9606:RACGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RE34|||http://purl.uniprot.org/uniprot/Q9H0H5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Abolishes GAP activity towards RHOA. Induces multiple blebs during cytokinesis.|||Cytokinesis failure.|||Cytokinesis failure. Abolishes localization at the cell membrane.|||Disordered|||Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-164. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-214.|||Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-170. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-170 and A-214.|||Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-164 and A-170. Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-164; A-170 and A-214.|||Does not inhibit interaction with ECT2. Strongly reduces phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CDAN3B; decreased function in erythropoiesis as shown by partial rescue of multinucleation defects in RACGAP1-deficient erythroid cells; decreased GAP activity towards RHOA, RAC1 and CDC42.|||In CDAN3B; loss of function in erythropoiesis as it does not rescue multinucleation and cytokinesis defects in RACGAP1-deficient erythroid and Hela cells; increased GAP activity towards RHOA; no effect on GAP activity towards RAC1 and CDC42.|||Interaction with SLC26A8|||More than 20-fold reduction in binding to ECT2.|||N-acetylmethionine|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphoserine; by PLK1|||Phosphothreonine|||Polar residues|||Rac GTPase-activating protein 1|||Rho-GAP|||Strongly reduces phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228808|||http://purl.uniprot.org/annotation/VAR_087032|||http://purl.uniprot.org/annotation/VAR_087033
http://togogenome.org/gene/9606:ASPHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICH7                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aspartate beta-hydroxylase domain-containing protein 2|||Cytoplasmic|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254162|||http://purl.uniprot.org/annotation/VAR_060123
http://togogenome.org/gene/9606:ASAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRE5|||http://purl.uniprot.org/uniprot/Q9ULH1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1|||Basic and acidic residues|||C4-type|||Disordered|||In isoform 1.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074196|||http://purl.uniprot.org/annotation/VAR_055528|||http://purl.uniprot.org/annotation/VSP_008365
http://togogenome.org/gene/9606:TBC1D15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Rab-GAP TBC|||Removed|||TBC1 domain family member 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208042|||http://purl.uniprot.org/annotation/VSP_023094|||http://purl.uniprot.org/annotation/VSP_046402
http://togogenome.org/gene/9606:SLURP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55000                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  In MDM.|||In MDM; decreased secretion.|||In MDM; no expression of the protein.|||In MDM; reduced expression of the protein.|||In MDM; reduced expression of the protein; decreased secretion.|||In MDM; unknown pathological significance; no effect on secretion.|||Secreted Ly-6/uPAR-related protein 1|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036167|||http://purl.uniprot.org/annotation/VAR_032871|||http://purl.uniprot.org/annotation/VAR_032872|||http://purl.uniprot.org/annotation/VAR_032873|||http://purl.uniprot.org/annotation/VAR_032874|||http://purl.uniprot.org/annotation/VAR_032875|||http://purl.uniprot.org/annotation/VAR_077307|||http://purl.uniprot.org/annotation/VAR_077308|||http://purl.uniprot.org/annotation/VAR_077309|||http://purl.uniprot.org/annotation/VAR_077310
http://togogenome.org/gene/9606:GARIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9W8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgi-associated RAB2 interactor protein 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089895|||http://purl.uniprot.org/annotation/VSP_009298
http://togogenome.org/gene/9606:CASKIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXD9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||CASK-binding|||Caskin-1|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM 1|||SAM 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066980
http://togogenome.org/gene/9606:TMEM74B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Transmembrane protein 74B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079431|||http://purl.uniprot.org/annotation/VAR_033757
http://togogenome.org/gene/9606:ACTL6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96019                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Actin-like protein 6A|||Found in a patient with developmental delay, speech difficulties, attention deficit hyperactivity disorder, behavioral problems and dysmorphic features; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Probable disease-associated variant found in a patient with developmental delay, speech and learning difficulties, dysmorphic features and abnormal digits.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089133|||http://purl.uniprot.org/annotation/VAR_079728|||http://purl.uniprot.org/annotation/VAR_079729|||http://purl.uniprot.org/annotation/VSP_000150
http://togogenome.org/gene/9606:SALL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DK65|||http://purl.uniprot.org/uniprot/E7EW59|||http://purl.uniprot.org/uniprot/Q9Y467                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||Sal-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047022|||http://purl.uniprot.org/annotation/VAR_014129|||http://purl.uniprot.org/annotation/VAR_014130|||http://purl.uniprot.org/annotation/VAR_014131|||http://purl.uniprot.org/annotation/VSP_056251|||http://purl.uniprot.org/annotation/VSP_056252|||http://purl.uniprot.org/annotation/VSP_056253
http://togogenome.org/gene/9606:ERCC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3L1|||http://purl.uniprot.org/uniprot/B3KPW7|||http://purl.uniprot.org/uniprot/B4DGZ9|||http://purl.uniprot.org/uniprot/Q13216                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA excision repair protein ERCC-8|||Disordered|||In CSA.|||In UVSS2.|||In isoform 2.|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050970|||http://purl.uniprot.org/annotation/VAR_016319|||http://purl.uniprot.org/annotation/VAR_025380|||http://purl.uniprot.org/annotation/VAR_025381|||http://purl.uniprot.org/annotation/VAR_053392|||http://purl.uniprot.org/annotation/VAR_063507|||http://purl.uniprot.org/annotation/VAR_063508|||http://purl.uniprot.org/annotation/VAR_063509|||http://purl.uniprot.org/annotation/VAR_063510|||http://purl.uniprot.org/annotation/VAR_068177|||http://purl.uniprot.org/annotation/VSP_013914|||http://purl.uniprot.org/annotation/VSP_013915
http://togogenome.org/gene/9606:C9orf43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9P8|||http://purl.uniprot.org/uniprot/B4DX97|||http://purl.uniprot.org/uniprot/Q8TAL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C9orf43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089692|||http://purl.uniprot.org/annotation/VAR_061597
http://togogenome.org/gene/9606:PDILT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N807                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Does not affect homodimerization; when associated with A-135.|||Does not affect homodimerization; when associated with A-420.|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Protein disulfide-isomerase-like protein of the testis|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325849|||http://purl.uniprot.org/annotation/VAR_039937|||http://purl.uniprot.org/annotation/VAR_039938|||http://purl.uniprot.org/annotation/VAR_039939|||http://purl.uniprot.org/annotation/VAR_039940|||http://purl.uniprot.org/annotation/VAR_039941|||http://purl.uniprot.org/annotation/VAR_039942|||http://purl.uniprot.org/annotation/VAR_039943
http://togogenome.org/gene/9606:GJB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95452                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in one patient with a syndrome resembling Vohwinkel and Bart-Pumphrey syndromes.|||Gap junction beta-6 protein|||Helical|||In DFNA3B; unknown pathological significance.|||In ECTD2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057871|||http://purl.uniprot.org/annotation/VAR_008711|||http://purl.uniprot.org/annotation/VAR_015696|||http://purl.uniprot.org/annotation/VAR_015697|||http://purl.uniprot.org/annotation/VAR_016838|||http://purl.uniprot.org/annotation/VAR_022424|||http://purl.uniprot.org/annotation/VAR_022425|||http://purl.uniprot.org/annotation/VAR_048825|||http://purl.uniprot.org/annotation/VAR_057960
http://togogenome.org/gene/9606:RER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15258|||http://purl.uniprot.org/uniprot/Q5T094                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylserine|||Phosphoserine|||Protein RER1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207589
http://togogenome.org/gene/9606:AUNIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7T9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aurora kinase A- and ninein-interacting protein|||Disordered|||In isoform 2.|||Interaction with AURKA|||Interaction with RBBP8/CtIP|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284572|||http://purl.uniprot.org/annotation/VAR_031776|||http://purl.uniprot.org/annotation/VSP_044288
http://togogenome.org/gene/9606:SATB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01826                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CASP6-resistant.|||CUT 1|||CUT 2|||CUTL|||Cleavage; by caspases|||DNA-binding protein SATB1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Impaired MAR-DNA-binding.|||In DEFDA; altered subcellular localization forming nuclear puncta; reduced transcriptional repression of some target genes.|||In DEFDA; reduced transcriptional repression.|||In KTZSL.|||In KTZSL; stabilized DNA-binding and increased transcriptional repression.|||In KTZSL; unknown pathological significance.|||In KTZSL; unknown pathological significance; no effect on DNA-binding or transcriptional repression.|||In isoform 2.|||Loss of nuclear localization, cytoplasmic.|||Loss of sumoylation.|||N6-acetyllysine|||No acetylation.|||No effect on DNA-binding or transcriptional repression.|||No phosphorylation.|||Normal nuclear localization.|||Normal sumoylation.|||Nuclear localization signal|||Nuclear matrix targeting sequence (NMTS)|||Phosphoserine|||Polar residues|||Pro residues|||Protein interaction|||Reduced MAR-DNA-binding.|||Reduced interaction with matrix attachment region (MAR) DNA.|||Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646.|||Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648.|||Slightly reduced MAR-DNA-binding.|||ULD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202398|||http://purl.uniprot.org/annotation/VAR_085437|||http://purl.uniprot.org/annotation/VAR_085438|||http://purl.uniprot.org/annotation/VAR_085439|||http://purl.uniprot.org/annotation/VAR_085440|||http://purl.uniprot.org/annotation/VAR_085441|||http://purl.uniprot.org/annotation/VAR_085442|||http://purl.uniprot.org/annotation/VAR_085443|||http://purl.uniprot.org/annotation/VAR_085444|||http://purl.uniprot.org/annotation/VAR_085445|||http://purl.uniprot.org/annotation/VAR_085446|||http://purl.uniprot.org/annotation/VAR_085447|||http://purl.uniprot.org/annotation/VAR_085448|||http://purl.uniprot.org/annotation/VAR_085449|||http://purl.uniprot.org/annotation/VAR_085450|||http://purl.uniprot.org/annotation/VAR_085451|||http://purl.uniprot.org/annotation/VAR_085452|||http://purl.uniprot.org/annotation/VAR_085453|||http://purl.uniprot.org/annotation/VAR_085454|||http://purl.uniprot.org/annotation/VAR_085455|||http://purl.uniprot.org/annotation/VAR_085456|||http://purl.uniprot.org/annotation/VSP_038296
http://togogenome.org/gene/9606:HCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL51                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||Does not affect channel activity.|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In EIG17; associated with disease susceptibility; causes a large negative shift of the activation curve; homomeric mutant channels transfected into rat cortical neurons lower the threshold of action potential firing and strongly increase cell excitability when compared with wild-type channels.|||In EIG17; associated with disease susceptibility; gain-of-function variant; affects channel activity resulting in a depolarizing shift in activation and faster activation kinetics compared to controls.|||In EIG17; unknown pathological significance; does not affect channel activity.|||In FEB2; affects channel activity resulting in faster kinetics and increased current density at higher temperature compared to wild type.|||Involved in subunit assembly|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKG/PRKG2|||Pore-forming; Name=Segment H5|||Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054111|||http://purl.uniprot.org/annotation/VAR_061106|||http://purl.uniprot.org/annotation/VAR_081530|||http://purl.uniprot.org/annotation/VAR_086190|||http://purl.uniprot.org/annotation/VAR_086191|||http://purl.uniprot.org/annotation/VAR_086192|||http://purl.uniprot.org/annotation/VAR_086193|||http://purl.uniprot.org/annotation/VAR_086194|||http://purl.uniprot.org/annotation/VAR_086195|||http://purl.uniprot.org/annotation/VAR_086196
http://togogenome.org/gene/9606:PLEKHF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8W4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE-type|||N6-acetyllysine|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family F member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251600
http://togogenome.org/gene/9606:DENND1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV53                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Clathrin box|||DENN domain-containing protein 1C|||Disordered|||FXDXF motif|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304676|||http://purl.uniprot.org/annotation/VAR_035056|||http://purl.uniprot.org/annotation/VAR_035057|||http://purl.uniprot.org/annotation/VAR_035058|||http://purl.uniprot.org/annotation/VSP_040669
http://togogenome.org/gene/9606:WFIKKN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J6G4|||http://purl.uniprot.org/uniprot/Q8TEU8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||Ig-like|||Ig-like C2-type|||Kazal-like|||N-linked (GlcNAc...) asparagine|||NTR|||Reactive bond|||WAP|||WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307820|||http://purl.uniprot.org/annotation/VAR_036692|||http://purl.uniprot.org/annotation/VAR_061984
http://togogenome.org/gene/9606:BAZ1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIG0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bromo|||C motif|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||Loss of tyrosine-protein kinase activity.|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tyrosine-protein kinase BAZ1B|||WAC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211170|||http://purl.uniprot.org/annotation/VSP_000552
http://togogenome.org/gene/9606:SLC4A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q91                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Anion exchange protein 4|||Basic and acidic residues|||Disordered|||Helical|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 4.|||Membrane (anion exchange)|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079223|||http://purl.uniprot.org/annotation/VSP_007085|||http://purl.uniprot.org/annotation/VSP_007086|||http://purl.uniprot.org/annotation/VSP_007087|||http://purl.uniprot.org/annotation/VSP_044785
http://togogenome.org/gene/9606:PNMA8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Paraneoplastic antigen-like protein 8A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325836|||http://purl.uniprot.org/annotation/VAR_039935|||http://purl.uniprot.org/annotation/VAR_039936|||http://purl.uniprot.org/annotation/VSP_032441|||http://purl.uniprot.org/annotation/VSP_032442
http://togogenome.org/gene/9606:TMEM140                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV12                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 140                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274357|||http://purl.uniprot.org/annotation/VAR_030262|||http://purl.uniprot.org/annotation/VAR_030263|||http://purl.uniprot.org/annotation/VAR_030264|||http://purl.uniprot.org/annotation/VAR_030265|||http://purl.uniprot.org/annotation/VAR_035670
http://togogenome.org/gene/9606:DNAH11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NAJ7|||http://purl.uniprot.org/uniprot/H9NAJ8|||http://purl.uniprot.org/uniprot/Q96DT5|||http://purl.uniprot.org/uniprot/Q96NT7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Dynein axonemal heavy chain 11|||Dynein heavy chain AAA lid|||Dynein heavy chain hydrolytic ATP-binding dynein motor region|||Dynein heavy chain linker|||Dynein heavy chain region D6 P-loop|||In CILD7.|||In CILD7; unknown pathological significance.|||Requires 2 nucleotide substitutions.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114633|||http://purl.uniprot.org/annotation/VAR_013851|||http://purl.uniprot.org/annotation/VAR_013852|||http://purl.uniprot.org/annotation/VAR_013853|||http://purl.uniprot.org/annotation/VAR_013854|||http://purl.uniprot.org/annotation/VAR_013855|||http://purl.uniprot.org/annotation/VAR_013856|||http://purl.uniprot.org/annotation/VAR_013857|||http://purl.uniprot.org/annotation/VAR_013858|||http://purl.uniprot.org/annotation/VAR_013859|||http://purl.uniprot.org/annotation/VAR_013860|||http://purl.uniprot.org/annotation/VAR_013861|||http://purl.uniprot.org/annotation/VAR_013862|||http://purl.uniprot.org/annotation/VAR_013863|||http://purl.uniprot.org/annotation/VAR_042944|||http://purl.uniprot.org/annotation/VAR_042945|||http://purl.uniprot.org/annotation/VAR_042946|||http://purl.uniprot.org/annotation/VAR_060141|||http://purl.uniprot.org/annotation/VAR_072472|||http://purl.uniprot.org/annotation/VAR_072473|||http://purl.uniprot.org/annotation/VAR_072474
http://togogenome.org/gene/9606:FAM168B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1KXE4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Myelin-associated neurite-outgrowth inhibitor|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325978|||http://purl.uniprot.org/annotation/VSP_032508
http://togogenome.org/gene/9606:ERI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K979                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ERI1 exoribonuclease 2|||Exonuclease|||GRF-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338973|||http://purl.uniprot.org/annotation/VAR_043848|||http://purl.uniprot.org/annotation/VAR_082819|||http://purl.uniprot.org/annotation/VAR_082820|||http://purl.uniprot.org/annotation/VSP_034077|||http://purl.uniprot.org/annotation/VSP_034078|||http://purl.uniprot.org/annotation/VSP_034079|||http://purl.uniprot.org/annotation/VSP_034080|||http://purl.uniprot.org/annotation/VSP_034081
http://togogenome.org/gene/9606:ZNF80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51504                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Zinc finger protein 80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047391|||http://purl.uniprot.org/annotation/VAR_019972|||http://purl.uniprot.org/annotation/VAR_046561
http://togogenome.org/gene/9606:CCDC186                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFU7|||http://purl.uniprot.org/uniprot/Q496Y1|||http://purl.uniprot.org/uniprot/Q7Z3E2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 186|||Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089823|||http://purl.uniprot.org/annotation/PRO_5004235087|||http://purl.uniprot.org/annotation/VAR_023047|||http://purl.uniprot.org/annotation/VAR_023048|||http://purl.uniprot.org/annotation/VAR_023049
http://togogenome.org/gene/9606:TMEM69                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SWH9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 69                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282850
http://togogenome.org/gene/9606:TBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16650                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased interaction with BCL11A.|||Disordered|||In IDDAS; de novo variant; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2; does not affect interaction with BCL11A.|||In IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; abolishes interaction with FOXP2; does not affect interaction with BCL11A.|||In IDDAS; de novo variant; localizes to the nucleus but forms abnormal aggregates; no effect on transcriptional repression of FEZF2; does not affect homodimerization; severely decreased interaction with FOXP2; loss of interaction with FOXP1; does not affect interaction with BCL11A.|||In IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; decreased interaction with FOXP2; loss of interaction with BCL11A.|||In IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2.|||In IDDAS; unknown pathological significance; does not affect nuclear localization; no effect on transcriptional repression of FEZF2; does not affect homodimerization; does not affect interaction with FOXP2; does not affect interaction with BCL11A.|||In isoform 2.|||No effect on interaction with BCL11A.|||Phosphoserine|||Phosphothreonine|||Polar residues|||T-box|||T-box brain protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184457|||http://purl.uniprot.org/annotation/VAR_052264|||http://purl.uniprot.org/annotation/VAR_078646|||http://purl.uniprot.org/annotation/VAR_081757|||http://purl.uniprot.org/annotation/VAR_081758|||http://purl.uniprot.org/annotation/VAR_081759|||http://purl.uniprot.org/annotation/VAR_081760|||http://purl.uniprot.org/annotation/VAR_081761|||http://purl.uniprot.org/annotation/VAR_081762|||http://purl.uniprot.org/annotation/VAR_081763|||http://purl.uniprot.org/annotation/VAR_081764|||http://purl.uniprot.org/annotation/VSP_056591
http://togogenome.org/gene/9606:OR4E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR8                                                                                  ^@                                                                                  Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Domain Extent|||Transmembrane                                                                                  ^@                                                                                  G-protein coupled receptors family 1 profile|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:DKK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DKK-type Cys-1|||DKK-type Cys-2|||Dickkopf-related protein 4|||Dickkopf-related protein 4 short form|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007225|||http://purl.uniprot.org/annotation/PRO_0000007226
http://togogenome.org/gene/9606:KRTAP5-11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6L8G4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 4 AA repeats of C-C-X-P|||Keratin-associated protein 5-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184109
http://togogenome.org/gene/9606:CCDC81                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN84                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 81|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288877|||http://purl.uniprot.org/annotation/VAR_032524|||http://purl.uniprot.org/annotation/VSP_025805|||http://purl.uniprot.org/annotation/VSP_025806|||http://purl.uniprot.org/annotation/VSP_025807
http://togogenome.org/gene/9606:TCEAL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHQ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Transcription elongation factor A protein-like 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274046
http://togogenome.org/gene/9606:REX1BD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EN9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Required for excision 1-B domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305285|||http://purl.uniprot.org/annotation/VSP_028325|||http://purl.uniprot.org/annotation/VSP_028326|||http://purl.uniprot.org/annotation/VSP_047493
http://togogenome.org/gene/9606:KRTAP1-3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUG1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  In allele KAP1.8A.|||In allele KAP1.8B.|||In allele KAP1.9.|||Keratin-associated protein 1-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223902|||http://purl.uniprot.org/annotation/VAR_025349|||http://purl.uniprot.org/annotation/VAR_025351|||http://purl.uniprot.org/annotation/VAR_025352|||http://purl.uniprot.org/annotation/VAR_085002
http://togogenome.org/gene/9606:GNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PCP0|||http://purl.uniprot.org/uniprot/F1T0G5|||http://purl.uniprot.org/uniprot/P16520                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3|||In CSNB1H.|||In CSNB1H; sporadic case; unknown pathological significance.|||In isoform 2.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127699|||http://purl.uniprot.org/annotation/VAR_014756|||http://purl.uniprot.org/annotation/VAR_014757|||http://purl.uniprot.org/annotation/VAR_014758|||http://purl.uniprot.org/annotation/VAR_029304|||http://purl.uniprot.org/annotation/VAR_029305|||http://purl.uniprot.org/annotation/VAR_049268|||http://purl.uniprot.org/annotation/VAR_049269|||http://purl.uniprot.org/annotation/VAR_077012|||http://purl.uniprot.org/annotation/VAR_077013|||http://purl.uniprot.org/annotation/VSP_055233
http://togogenome.org/gene/9606:CMSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ75                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Protein CMSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239014|||http://purl.uniprot.org/annotation/VAR_033658|||http://purl.uniprot.org/annotation/VAR_047645|||http://purl.uniprot.org/annotation/VSP_046688
http://togogenome.org/gene/9606:TREML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM|||Ig-like V-type|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Polar residues|||S-palmitoyl cysteine|||Trem-like transcript 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253855|||http://purl.uniprot.org/annotation/VAR_035526|||http://purl.uniprot.org/annotation/VAR_049950|||http://purl.uniprot.org/annotation/VSP_021124|||http://purl.uniprot.org/annotation/VSP_021125|||http://purl.uniprot.org/annotation/VSP_021126
http://togogenome.org/gene/9606:AKAP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43823                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  A-kinase anchor protein 8|||Abolishes chromosome-condensation activity and recruitment of condensin complex; when associated with S-481.|||Abolishes chromosome-condensation activity and recruitment of condensin complex; when associated with S-484.|||Abolishes chromosome-condensation activity; when associated with S-392.|||Abolishes chromosome-condensation activity; when associated with S-395.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Bipartite nuclear localization signal|||C2H2 AKAP95-type 1|||C2H2 AKAP95-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||Interaction with DDX5|||Interaction with DPY30|||Interaction with MCM2|||Involved in chromatin-binding|||Involved in condensin complex recruitment|||No effect on activity to regulate DNA replication and on condensin complex recruitment.|||No nuclear localization; when associated with 304-N-S-305.|||No nuclear localization; when associated with S-290.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||RII-binding|||Required for interaction with MYCBP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075381|||http://purl.uniprot.org/annotation/VAR_036534
http://togogenome.org/gene/9606:TFE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DIA5|||http://purl.uniprot.org/uniprot/P19532                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with Interacts with small GTPases Rag and recruitment to the lysosomal membrane.|||Abolished localization to the nucleus.|||Accumulates in the nucleus due to impaired phosphorylation. Does not affect ubiquitination by the SCF(BTRC) complex.|||Asymmetric dimethylarginine|||BHLH|||Breakpoint for translocation to form ASPSCR1-TFE3 oncogene|||Breakpoint for translocation to form NONO-TFE3, PSF-TFE3 and ASPSCR1-TFE3 oncogenes|||Breakpoint for translocation to form PRCC-TFE3 oncogene|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired phosphorylation by MTOR, leading to abolished ubiquitination and degradation by the SCF(BTRC) complex.|||In MRXSPF.|||In MRXSPF; abolished bolished interaction with small GTPases Rag (RagA/RRAGA and RagC/RRAGC).|||In isoform 2.|||Leucine-zipper|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MTOR|||Polar residues|||Strong transcription activation domain|||Transcription factor E3|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127471|||http://purl.uniprot.org/annotation/VAR_027501|||http://purl.uniprot.org/annotation/VAR_027502|||http://purl.uniprot.org/annotation/VAR_086338|||http://purl.uniprot.org/annotation/VAR_086339|||http://purl.uniprot.org/annotation/VAR_086340|||http://purl.uniprot.org/annotation/VAR_086341|||http://purl.uniprot.org/annotation/VAR_086342|||http://purl.uniprot.org/annotation/VAR_086343|||http://purl.uniprot.org/annotation/VAR_086344|||http://purl.uniprot.org/annotation/VAR_086345|||http://purl.uniprot.org/annotation/VAR_086346|||http://purl.uniprot.org/annotation/VAR_086347|||http://purl.uniprot.org/annotation/VAR_086348|||http://purl.uniprot.org/annotation/VAR_086349|||http://purl.uniprot.org/annotation/VSP_056882|||http://purl.uniprot.org/annotation/VSP_056883
http://togogenome.org/gene/9606:GYPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04921                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Ahonen (AN(a)) antigen.|||Cytoplasmic|||Disordered|||Duch (DH(a)) antigen.|||Extracellular|||Glycophorin-C|||Helical; Signal-anchor for type III membrane protein|||In isoform 3.|||In isoform Glycophorin-D.|||N-linked (GlcNAc...) asparagine|||Not glycosylated; in variant Webb antigen|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||Webb (WB) antigen.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149050|||http://purl.uniprot.org/annotation/VAR_003193|||http://purl.uniprot.org/annotation/VAR_003194|||http://purl.uniprot.org/annotation/VAR_003195|||http://purl.uniprot.org/annotation/VAR_021342|||http://purl.uniprot.org/annotation/VSP_001777|||http://purl.uniprot.org/annotation/VSP_054790
http://togogenome.org/gene/9606:TAS1R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTX0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished the response to brazzein.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Receptor unresponsive to all sweeteners tested.|||Reduces the response to brazzein and monellin.|||Reduces the response to brazzein; P-540 also enhances responses to the small molecule sweeteners.|||Reduces the response to monellin.|||Required for brazzein responsiveness|||Retains partial activity toward brazzein; however response to other sweeteners tested is suppressed.|||Taste receptor type 1 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012961|||http://purl.uniprot.org/annotation/VAR_020788
http://togogenome.org/gene/9606:SLC23A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z508|||http://purl.uniprot.org/uniprot/Q6PIS1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues|||Solute carrier family 23 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337203|||http://purl.uniprot.org/annotation/VSP_033970|||http://purl.uniprot.org/annotation/VSP_043670
http://togogenome.org/gene/9606:TMEM191B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7N4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 191B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340716
http://togogenome.org/gene/9606:CCZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86790|||http://purl.uniprot.org/uniprot/P86791                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar fusion protein CCZ1 homolog|||Vacuolar fusion protein CCZ1 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089584|||http://purl.uniprot.org/annotation/PRO_0000401065
http://togogenome.org/gene/9606:CDC42EP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKI2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||CRIB|||Cdc42 effector protein 3|||Disordered|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212651
http://togogenome.org/gene/9606:RRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZB55|||http://purl.uniprot.org/uniprot/F5H148|||http://purl.uniprot.org/uniprot/Q9NYV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with TAF1B and TAF1C.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with EIF3L|||Interaction with POLR1F|||Phosphoserine|||Phosphothreonine; by MAPK9|||Polar residues|||RNA polymerase I-specific transcription initiation factor RRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211426|||http://purl.uniprot.org/annotation/VAR_051886|||http://purl.uniprot.org/annotation/VSP_056338|||http://purl.uniprot.org/annotation/VSP_056339|||http://purl.uniprot.org/annotation/VSP_056519|||http://purl.uniprot.org/annotation/VSP_056520|||http://purl.uniprot.org/annotation/VSP_056521
http://togogenome.org/gene/9606:HRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00198                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Transmembrane                                                                                  ^@                                                                                  Activator of apoptosis harakiri|||BH3|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143106
http://togogenome.org/gene/9606:RNF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VTR2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase BRE1A|||N6-acetyllysine|||Phosphoserine|||Polar residues|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055836
http://togogenome.org/gene/9606:SNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13596                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes membrane remodeling capacity; no effect on dimerization.|||Abolishes phosphatidylinositol phosphate binding. Abolishes endosomal location.|||BAR|||Disordered|||In isoform 1A.|||In isoform 3.|||Loss of endosomal location.|||Membrane-binding amphipathic helix|||N6-acetyllysine|||No effect on membrane remodeling and membrane binding; when associated with A-442.|||No effect on membrane remodeling and membrane binding; when associated with A-445.|||PX|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sorting nexin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213835|||http://purl.uniprot.org/annotation/VAR_034507|||http://purl.uniprot.org/annotation/VAR_052477|||http://purl.uniprot.org/annotation/VSP_006189|||http://purl.uniprot.org/annotation/VSP_044823
http://togogenome.org/gene/9606:DOK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PKX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  DKFBH motif|||Disordered|||Docking protein 6|||IRS-type PTB|||PH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187279
http://togogenome.org/gene/9606:GSTM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46439|||http://purl.uniprot.org/uniprot/Q5T8R2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase Mu 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185825|||http://purl.uniprot.org/annotation/VAR_049491|||http://purl.uniprot.org/annotation/VAR_065098
http://togogenome.org/gene/9606:FAM47E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Protein FAM47E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326074|||http://purl.uniprot.org/annotation/VSP_040931|||http://purl.uniprot.org/annotation/VSP_040932|||http://purl.uniprot.org/annotation/VSP_040933|||http://purl.uniprot.org/annotation/VSP_040934
http://togogenome.org/gene/9606:POLE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07864                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||CysA-type|||CysB motif|||DNA polymerase epsilon catalytic subunit A|||Disordered|||Found in a colorectal sample; somatic mutation.|||In CRCS12.|||In CRCS12; associated with disease susceptibility.|||In IMAGEI.|||In IMAGEI; unknown pathological significance.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046455|||http://purl.uniprot.org/annotation/VAR_020276|||http://purl.uniprot.org/annotation/VAR_020277|||http://purl.uniprot.org/annotation/VAR_020278|||http://purl.uniprot.org/annotation/VAR_020279|||http://purl.uniprot.org/annotation/VAR_020280|||http://purl.uniprot.org/annotation/VAR_020281|||http://purl.uniprot.org/annotation/VAR_020282|||http://purl.uniprot.org/annotation/VAR_020283|||http://purl.uniprot.org/annotation/VAR_028429|||http://purl.uniprot.org/annotation/VAR_028430|||http://purl.uniprot.org/annotation/VAR_028431|||http://purl.uniprot.org/annotation/VAR_028432|||http://purl.uniprot.org/annotation/VAR_028433|||http://purl.uniprot.org/annotation/VAR_028434|||http://purl.uniprot.org/annotation/VAR_028435|||http://purl.uniprot.org/annotation/VAR_048881|||http://purl.uniprot.org/annotation/VAR_048882|||http://purl.uniprot.org/annotation/VAR_061138|||http://purl.uniprot.org/annotation/VAR_069339|||http://purl.uniprot.org/annotation/VAR_069340|||http://purl.uniprot.org/annotation/VAR_069341|||http://purl.uniprot.org/annotation/VAR_069342|||http://purl.uniprot.org/annotation/VAR_069343|||http://purl.uniprot.org/annotation/VAR_069344|||http://purl.uniprot.org/annotation/VAR_069345|||http://purl.uniprot.org/annotation/VAR_069346|||http://purl.uniprot.org/annotation/VAR_069347|||http://purl.uniprot.org/annotation/VAR_069348|||http://purl.uniprot.org/annotation/VAR_069349|||http://purl.uniprot.org/annotation/VAR_069350|||http://purl.uniprot.org/annotation/VAR_069351|||http://purl.uniprot.org/annotation/VAR_069352|||http://purl.uniprot.org/annotation/VAR_069353|||http://purl.uniprot.org/annotation/VAR_069354|||http://purl.uniprot.org/annotation/VAR_069355|||http://purl.uniprot.org/annotation/VAR_069356|||http://purl.uniprot.org/annotation/VAR_077349|||http://purl.uniprot.org/annotation/VAR_077350|||http://purl.uniprot.org/annotation/VAR_077351|||http://purl.uniprot.org/annotation/VAR_081996|||http://purl.uniprot.org/annotation/VAR_081997|||http://purl.uniprot.org/annotation/VAR_081998
http://togogenome.org/gene/9606:MOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16653|||http://purl.uniprot.org/uniprot/Q5SSB8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In NRCLP7.|||In isoform 10.|||In isoform 11.|||In isoform 13.|||In isoform 2 and isoform 6.|||In isoform 3, isoform 7 and isoform 12.|||In isoform 4 and isoform 12.|||In isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 8.|||In isoform 9.|||Myelin-oligodendrocyte glycoprotein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014888|||http://purl.uniprot.org/annotation/PRO_5014586883|||http://purl.uniprot.org/annotation/VAR_056056|||http://purl.uniprot.org/annotation/VAR_060215|||http://purl.uniprot.org/annotation/VAR_066415|||http://purl.uniprot.org/annotation/VSP_002539|||http://purl.uniprot.org/annotation/VSP_002540|||http://purl.uniprot.org/annotation/VSP_002541|||http://purl.uniprot.org/annotation/VSP_002542|||http://purl.uniprot.org/annotation/VSP_002543|||http://purl.uniprot.org/annotation/VSP_002544|||http://purl.uniprot.org/annotation/VSP_002545|||http://purl.uniprot.org/annotation/VSP_040344|||http://purl.uniprot.org/annotation/VSP_040345|||http://purl.uniprot.org/annotation/VSP_046856|||http://purl.uniprot.org/annotation/VSP_055600
http://togogenome.org/gene/9606:TAS2R43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59537                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082302
http://togogenome.org/gene/9606:WBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P602|||http://purl.uniprot.org/uniprot/Q96G27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Abolishes interaction with WWOX.|||Disordered|||Helical|||PPxY motif 1|||PPxY motif 2|||Polar residues|||WW domain-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065948
http://togogenome.org/gene/9606:FOXJ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0K8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fork-head|||Forkhead box protein J2|||In isoform FOXJ2.S.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091853|||http://purl.uniprot.org/annotation/VAR_021842|||http://purl.uniprot.org/annotation/VAR_049162|||http://purl.uniprot.org/annotation/VSP_001544
http://togogenome.org/gene/9606:ENPP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14638                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Causes the formation of covalently linked homodimers in solution; when associated with C-179.|||Causes the formation of covalently linked homodimers in solution; when associated with C-336.|||Cell attachment site|||Cytoplasmic|||Ectonucleotide pyrophosphatase/phosphodiesterase family member 3|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||No effect on affinity for nucleotides and enzyme activity.|||No effect on substrate specificity. Increases affinity for nucleotides and slows their hydrolysis.|||Nuclease|||Nucleophile|||Phosphodiesterase|||SMB 1|||SMB 2|||Strongly decreases affinity for nucleotides and slows their hydrolysis.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188570|||http://purl.uniprot.org/annotation/VAR_018516|||http://purl.uniprot.org/annotation/VAR_031253|||http://purl.uniprot.org/annotation/VAR_046538
http://togogenome.org/gene/9606:ZNF664                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3J9                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 664                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296273
http://togogenome.org/gene/9606:CATSPERG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZI7|||http://purl.uniprot.org/uniprot/Q32MQ2|||http://purl.uniprot.org/uniprot/Q6ZRH7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated auxiliary subunit gamma|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019565|||http://purl.uniprot.org/annotation/VAR_059631|||http://purl.uniprot.org/annotation/VAR_059632|||http://purl.uniprot.org/annotation/VAR_059633
http://togogenome.org/gene/9606:TAGLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01995|||http://purl.uniprot.org/uniprot/Q5U0D2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Calponin-like|||N-acetylalanine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||Transgelin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204781|||http://purl.uniprot.org/annotation/VAR_048670
http://togogenome.org/gene/9606:KLHDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ90                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228995
http://togogenome.org/gene/9606:THEMIS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TEJ8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CABIT 1|||CABIT 2|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphothreonine|||Phosphotyrosine|||Protein THEMIS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084143|||http://purl.uniprot.org/annotation/VAR_051060|||http://purl.uniprot.org/annotation/VAR_051061|||http://purl.uniprot.org/annotation/VSP_015326|||http://purl.uniprot.org/annotation/VSP_015327|||http://purl.uniprot.org/annotation/VSP_015328|||http://purl.uniprot.org/annotation/VSP_015329|||http://purl.uniprot.org/annotation/VSP_015330|||http://purl.uniprot.org/annotation/VSP_037966|||http://purl.uniprot.org/annotation/VSP_037967
http://togogenome.org/gene/9606:DFFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00273                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CIDE-N|||Cleavage; by caspase-3|||DNA fragmentation factor subunit alpha|||Disordered|||In isoform DFF35.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144716|||http://purl.uniprot.org/annotation/VSP_001085|||http://purl.uniprot.org/annotation/VSP_001086
http://togogenome.org/gene/9606:LUZP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TE4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leucine zipper protein 2|||Leucine-zipper|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315274|||http://purl.uniprot.org/annotation/VAR_038165|||http://purl.uniprot.org/annotation/VSP_030520|||http://purl.uniprot.org/annotation/VSP_030521|||http://purl.uniprot.org/annotation/VSP_030522|||http://purl.uniprot.org/annotation/VSP_030523|||http://purl.uniprot.org/annotation/VSP_044970
http://togogenome.org/gene/9606:CRBN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SW2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes thalidomide-binding without affecting DCX protein ligase complex activity; when associated with A-384. Abolishes pomalidomide-induced change in substrate specificity and abolishes pomalidomide-induced decrease in cell viability that is brought about by increased degradation of MYC, IRF4 and IKZF3.|||Abolishes thalidomide-binding without affecting DCX protein ligase complex activity; when associated with A-386.|||CULT|||Disordered|||Fails to rescue increased BK channel activity and decreased probability of neurotransmission in a mouse hippocampal neuron model.|||In MRT2.|||In isoform 2.|||Lon N-terminal|||Phosphoserine|||Protein cereblon                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076160|||http://purl.uniprot.org/annotation/VAR_079409|||http://purl.uniprot.org/annotation/VSP_015209
http://togogenome.org/gene/9606:NOXA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Constitutively interacts with YWHAZ; when associated with E-172.|||Constitutively interacts with YWHAZ; when associated with E-461.|||Disordered|||Found in a truncated form isolated from Caco-2 cells treated with butyrate.|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of function and loss of interaction with RAC1.|||Loss of function and loss of interaction with RAC1. Loss of localization to membranes.|||Loss of interaction with NOXO1 and NCF1. Loss of localization to membranes. Partial loss of function.|||Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-172.|||Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-461.|||Mediates interaction with RAC1|||NADPH oxidase activator 1|||PB1|||Partial loss of function.|||Phosphoserine; by PKA|||Polar residues|||SH3|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||Unable to activate NOX2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314609|||http://purl.uniprot.org/annotation/VAR_037985|||http://purl.uniprot.org/annotation/VAR_037986|||http://purl.uniprot.org/annotation/VSP_030335|||http://purl.uniprot.org/annotation/VSP_030336
http://togogenome.org/gene/9606:KCNG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ96                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Molecule Processing|||Motif|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Motif|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily G member 2|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054074
http://togogenome.org/gene/9606:LAPTM4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15012|||http://purl.uniprot.org/uniprot/Q6IBP4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||Lysosomal-associated transmembrane protein 4A|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096637
http://togogenome.org/gene/9606:KDM3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4C1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes histone demethylase activity.|||Abolishes lysine-specific histone demethylase activity.|||C6-type|||Disordered|||In a breast cancer sample; somatic mutation.|||JmjC|||LXXLL motif|||Lysine-specific demethylase 3A|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084285|||http://purl.uniprot.org/annotation/VAR_026220|||http://purl.uniprot.org/annotation/VAR_030623|||http://purl.uniprot.org/annotation/VAR_030624|||http://purl.uniprot.org/annotation/VAR_035940|||http://purl.uniprot.org/annotation/VAR_055977
http://togogenome.org/gene/9606:TP53INP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A56                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||LIR|||Tumor protein p53-inducible nuclear protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072406|||http://purl.uniprot.org/annotation/VAR_051404|||http://purl.uniprot.org/annotation/VSP_013176
http://togogenome.org/gene/9606:XAGE1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD64                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform D.|||Phosphoserine|||X antigen family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148349|||http://purl.uniprot.org/annotation/VSP_001596
http://togogenome.org/gene/9606:SDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20132|||http://purl.uniprot.org/uniprot/Q8WW81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  L-serine dehydratase/L-threonine deaminase|||Loss of enzyme activity.|||N6-(pyridoxal phosphate)lysine|||Tryptophan synthase beta chain-like PALP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185594
http://togogenome.org/gene/9606:AFDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MQ02|||http://purl.uniprot.org/uniprot/G1UI22|||http://purl.uniprot.org/uniprot/P55196                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Afadin|||Basic and acidic residues|||Breakpoint for translocation to form KMT2A/MLL1-AFDN|||Dilute|||Disordered|||FHA|||In isoform 1, isoform 2 and isoform 3.|||In isoform 1, isoform 2, isoform 3 and isoform 5.|||In isoform 1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||N6-acetyllysine|||PDZ|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Ras-associating|||Ras-associating 1|||Ras-associating 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215918|||http://purl.uniprot.org/annotation/VSP_000217|||http://purl.uniprot.org/annotation/VSP_000218|||http://purl.uniprot.org/annotation/VSP_019257|||http://purl.uniprot.org/annotation/VSP_038707|||http://purl.uniprot.org/annotation/VSP_038708|||http://purl.uniprot.org/annotation/VSP_038709|||http://purl.uniprot.org/annotation/VSP_038710|||http://purl.uniprot.org/annotation/VSP_038711|||http://purl.uniprot.org/annotation/VSP_041197|||http://purl.uniprot.org/annotation/VSP_041198|||http://purl.uniprot.org/annotation/VSP_041199
http://togogenome.org/gene/9606:ALDH3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L3I9|||http://purl.uniprot.org/uniprot/P30838|||http://purl.uniprot.org/uniprot/Q6PKA6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes activity.|||Aldehyde dehydrogenase|||Aldehyde dehydrogenase, dimeric NADP-preferring|||Basic and acidic residues|||Disordered|||In allele ALDH3A1*2.|||N-acetylserine|||N6-acetyllysine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056470|||http://purl.uniprot.org/annotation/VAR_011303|||http://purl.uniprot.org/annotation/VAR_018981|||http://purl.uniprot.org/annotation/VAR_018982
http://togogenome.org/gene/9606:HMSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTL9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Serpin-like protein HMSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343868
http://togogenome.org/gene/9606:DLST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z6J1|||http://purl.uniprot.org/uniprot/P36957                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial|||Disordered|||In PGL7; decreased dihydrolipoyllysine-residue succinyltransferase activity.|||In PGL7; unknown pathological significance; not changed dihydrolipoyllysine-residue succinyltransferase activity.|||In isoform 2.|||Lipoyl-binding|||Loss of dihydrolipoyllysine-residue succinyltransferase activity.|||Mitochondrion|||N6-acetyllysine|||N6-lipoyllysine|||Not changed dihydrolipoyllysine-residue succinyltransferase activity.|||Phosphoserine|||Pro residues|||Reduced nuclear localization of the 2-oxoglutarate dehydrogenase complex. Reduced histone succinylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020472|||http://purl.uniprot.org/annotation/VAR_004976|||http://purl.uniprot.org/annotation/VAR_004977|||http://purl.uniprot.org/annotation/VAR_083034|||http://purl.uniprot.org/annotation/VAR_083035|||http://purl.uniprot.org/annotation/VAR_083036|||http://purl.uniprot.org/annotation/VAR_083037|||http://purl.uniprot.org/annotation/VSP_056439|||http://purl.uniprot.org/annotation/VSP_056440
http://togogenome.org/gene/9606:VKORC1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0F7|||http://purl.uniprot.org/uniprot/Q8N0U8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes enzyme activity in cell-based assays. Reduces enzyme activity moderately in assays that regenerate the redox-active cysteines with dithiothreitol (in vitro).|||Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Redox-active|||Vitamin K epoxide reductase|||Vitamin K epoxide reductase complex subunit 1-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191671|||http://purl.uniprot.org/annotation/VSP_055709
http://togogenome.org/gene/9606:OR6C74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW13|||http://purl.uniprot.org/uniprot/A6NCV1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6C74                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309619|||http://purl.uniprot.org/annotation/VAR_036981|||http://purl.uniprot.org/annotation/VAR_036982|||http://purl.uniprot.org/annotation/VAR_036983|||http://purl.uniprot.org/annotation/VAR_036984|||http://purl.uniprot.org/annotation/VAR_036985
http://togogenome.org/gene/9606:ESPNL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXY4|||http://purl.uniprot.org/uniprot/Q6ZVH7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||Espin-like protein|||In isoform 2.|||In isoform 3.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312511|||http://purl.uniprot.org/annotation/VAR_037535|||http://purl.uniprot.org/annotation/VAR_037536|||http://purl.uniprot.org/annotation/VAR_037537|||http://purl.uniprot.org/annotation/VAR_037538|||http://purl.uniprot.org/annotation/VAR_037539|||http://purl.uniprot.org/annotation/VSP_029858|||http://purl.uniprot.org/annotation/VSP_029859
http://togogenome.org/gene/9606:KRTAP12-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59991                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||23 X 5 AA approximate repeats|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 12-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185197|||http://purl.uniprot.org/annotation/VAR_053468|||http://purl.uniprot.org/annotation/VAR_053469|||http://purl.uniprot.org/annotation/VAR_060057|||http://purl.uniprot.org/annotation/VAR_060058|||http://purl.uniprot.org/annotation/VAR_060059|||http://purl.uniprot.org/annotation/VAR_062115
http://togogenome.org/gene/9606:POMGNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KNB7|||http://purl.uniprot.org/uniprot/B7Z7F2|||http://purl.uniprot.org/uniprot/B7Z7Q4|||http://purl.uniprot.org/uniprot/Q8WZA1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Abolishes in vitro enzyme activity; when associated with A-473.|||Abolishes in vitro enzyme activity; when associated with A-477.|||Basic and acidic residues|||Catalytic|||Cytoplasmic|||Decreased enzyme activity.|||Decreased enzyme activity. Impairs protein stability.|||Decreased protein stability. Decreased enzyme activity.|||Disordered|||GG-type lectin|||Gives rise to a soluble form.|||Helical|||Helical; Signal-anchor for type II membrane protein|||ILEI/PANDER|||In MDDGA3 and MDDGB3.|||In MDDGA3.|||In MDDGA3; found on the same allele as Q-311; unknown pathological significance.|||In MDDGA3; specific activity abolished in the membrane bound form but not the soluble form.|||In MDDGA3; specific activity abolished of the membrane bound form but not the soluble form.|||In MDDGA3; specific activity abolished.|||In MDDGB3.|||In MDDGC3; normal enzyme activity but altered kinetic properties.|||In RP76.|||In RP76; no effect on protein abundance; reduced acetylglucosaminyltransferase activity.|||In RP76; reduced acetylglucosaminyltransferase activity.|||In isoform 2.|||Interaction with O-glycosylated substrate glycoprotein|||Lumenal|||Moderately increased enzyme activity. Decreased affinity for N-acetylglucosamine.|||Nearly abolishes enzyme activity.|||Phosphoserine|||Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191390|||http://purl.uniprot.org/annotation/VAR_023101|||http://purl.uniprot.org/annotation/VAR_023102|||http://purl.uniprot.org/annotation/VAR_023103|||http://purl.uniprot.org/annotation/VAR_023104|||http://purl.uniprot.org/annotation/VAR_023105|||http://purl.uniprot.org/annotation/VAR_023106|||http://purl.uniprot.org/annotation/VAR_023107|||http://purl.uniprot.org/annotation/VAR_023108|||http://purl.uniprot.org/annotation/VAR_023109|||http://purl.uniprot.org/annotation/VAR_023110|||http://purl.uniprot.org/annotation/VAR_030645|||http://purl.uniprot.org/annotation/VAR_030646|||http://purl.uniprot.org/annotation/VAR_065021|||http://purl.uniprot.org/annotation/VAR_065022|||http://purl.uniprot.org/annotation/VAR_065023|||http://purl.uniprot.org/annotation/VAR_065024|||http://purl.uniprot.org/annotation/VAR_065025|||http://purl.uniprot.org/annotation/VAR_065026|||http://purl.uniprot.org/annotation/VAR_076524|||http://purl.uniprot.org/annotation/VAR_076525|||http://purl.uniprot.org/annotation/VAR_076526|||http://purl.uniprot.org/annotation/VAR_077054|||http://purl.uniprot.org/annotation/VSP_054029
http://togogenome.org/gene/9606:ACSL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95573                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Fatty acid CoA ligase Acsl3|||Helical; Signal-anchor for type III membrane protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193107|||http://purl.uniprot.org/annotation/VAR_026716
http://togogenome.org/gene/9606:KCNU1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYU2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S0|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In SPGF79; no protein detected in patient sperm; a knockin mouse model recapitulates the phenotype of male infertility.|||In SPGF79; severely decreased protein abundance in patient sperm.|||Pore-forming; Name=P region|||Potassium channel subfamily U member 1|||RCK N-terminal|||Segment S10|||Segment S7|||Segment S8|||Segment S9|||Selectivity for potassium                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349186|||http://purl.uniprot.org/annotation/VAR_053868|||http://purl.uniprot.org/annotation/VAR_053869|||http://purl.uniprot.org/annotation/VAR_060148|||http://purl.uniprot.org/annotation/VAR_088020|||http://purl.uniprot.org/annotation/VAR_088021
http://togogenome.org/gene/9606:SLC30A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z514|||http://purl.uniprot.org/uniprot/Q6PML9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||In BILAPES; no effect on Wnt-signaling; no change in mitochondrial subcellular location; decrease in cytosolic free zinc levels.|||LXXLL motif|||Mitochondrion|||Proton-coupled zinc antiporter SLC30A9, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295805|||http://purl.uniprot.org/annotation/VAR_052003|||http://purl.uniprot.org/annotation/VAR_052004|||http://purl.uniprot.org/annotation/VAR_052005|||http://purl.uniprot.org/annotation/VAR_079365
http://togogenome.org/gene/9606:PLEKHH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z736                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FERM|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MyTH4|||Omega-N-methylarginine|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family H member 3|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311108|||http://purl.uniprot.org/annotation/VAR_061520|||http://purl.uniprot.org/annotation/VSP_029392|||http://purl.uniprot.org/annotation/VSP_029393|||http://purl.uniprot.org/annotation/VSP_029394|||http://purl.uniprot.org/annotation/VSP_029395|||http://purl.uniprot.org/annotation/VSP_029396|||http://purl.uniprot.org/annotation/VSP_029397|||http://purl.uniprot.org/annotation/VSP_029398
http://togogenome.org/gene/9606:TTLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95922                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes microtubule polyglutamylation. Decreases MAP4 recruitment to microtubules.|||Disordered|||Essential for specifying alpha-elongation versus initiation step of the polyglutamylase activity|||In isoform 4.|||In isoform B.|||Polyglutamylase complex subunit TTLL1|||TTL                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212438|||http://purl.uniprot.org/annotation/VAR_052409|||http://purl.uniprot.org/annotation/VSP_006671|||http://purl.uniprot.org/annotation/VSP_006672|||http://purl.uniprot.org/annotation/VSP_011825
http://togogenome.org/gene/9606:COX19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q49B96                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Cytochrome c oxidase assembly protein COX19|||Disordered|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273151
http://togogenome.org/gene/9606:TSPAN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYV6|||http://purl.uniprot.org/uniprot/A0A087WZU5|||http://purl.uniprot.org/uniprot/O43657                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Tetraspanin-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219246|||http://purl.uniprot.org/annotation/VAR_014494
http://togogenome.org/gene/9606:FAM111B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6SJ93                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Charge relay system|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In POIKTMP.|||In isoform 2.|||N-acetylmethionine|||Serine protease FAM111B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274409|||http://purl.uniprot.org/annotation/VAR_030282|||http://purl.uniprot.org/annotation/VAR_053821|||http://purl.uniprot.org/annotation/VAR_070953|||http://purl.uniprot.org/annotation/VAR_070954|||http://purl.uniprot.org/annotation/VAR_070955|||http://purl.uniprot.org/annotation/VSP_022739
http://togogenome.org/gene/9606:CD163                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VB7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; in calcium-free condition|||Cytoplasmic|||Extracellular|||Helical|||Impaired phosphorylation by PRKCA.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Internalization signal|||Massive decrease of endocytotic activity.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||SRCR 1|||SRCR 2|||SRCR 3|||SRCR 4|||SRCR 5|||SRCR 6|||SRCR 7|||SRCR 8|||SRCR 9|||Scavenger receptor cysteine-rich type 1 protein M130|||Soluble CD163                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238938|||http://purl.uniprot.org/annotation/PRO_0000238939|||http://purl.uniprot.org/annotation/VAR_026574|||http://purl.uniprot.org/annotation/VSP_019013|||http://purl.uniprot.org/annotation/VSP_019014|||http://purl.uniprot.org/annotation/VSP_019015
http://togogenome.org/gene/9606:ST7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDW4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8.|||Suppressor of tumorigenicity 7 protein-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339227|||http://purl.uniprot.org/annotation/VAR_043934|||http://purl.uniprot.org/annotation/VAR_043935|||http://purl.uniprot.org/annotation/VAR_043936|||http://purl.uniprot.org/annotation/VSP_034127|||http://purl.uniprot.org/annotation/VSP_034128|||http://purl.uniprot.org/annotation/VSP_034129|||http://purl.uniprot.org/annotation/VSP_034130|||http://purl.uniprot.org/annotation/VSP_034131|||http://purl.uniprot.org/annotation/VSP_034132|||http://purl.uniprot.org/annotation/VSP_034133|||http://purl.uniprot.org/annotation/VSP_034134|||http://purl.uniprot.org/annotation/VSP_034135|||http://purl.uniprot.org/annotation/VSP_034136
http://togogenome.org/gene/9606:NDRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N959|||http://purl.uniprot.org/uniprot/Q92597                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X 10 AA tandem repeats of G-T-R-S-R-S-H-T-S-E|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine|||Phosphothreonine; by SGK1|||Polar residues|||Protein NDRG1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159573|||http://purl.uniprot.org/annotation/VAR_050234|||http://purl.uniprot.org/annotation/VAR_050235|||http://purl.uniprot.org/annotation/VSP_045037|||http://purl.uniprot.org/annotation/VSP_045038
http://togogenome.org/gene/9606:GGT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEL3|||http://purl.uniprot.org/uniprot/P36269                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutathione hydrolase 5 heavy chain|||Glutathione hydrolase 5 light chain|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011072|||http://purl.uniprot.org/annotation/PRO_0000011073|||http://purl.uniprot.org/annotation/VAR_024455|||http://purl.uniprot.org/annotation/VAR_028006|||http://purl.uniprot.org/annotation/VAR_028007|||http://purl.uniprot.org/annotation/VAR_028008|||http://purl.uniprot.org/annotation/VSP_008146|||http://purl.uniprot.org/annotation/VSP_043470
http://togogenome.org/gene/9606:PYY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10082                                                                                  ^@                                                                                  Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by FAP|||Disordered|||In isoform 2.|||Peptide YY|||Peptide YY(3-36)|||Phosphoserine|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025384|||http://purl.uniprot.org/annotation/PRO_0000025385|||http://purl.uniprot.org/annotation/PRO_0000025386|||http://purl.uniprot.org/annotation/VAR_006382|||http://purl.uniprot.org/annotation/VAR_047407|||http://purl.uniprot.org/annotation/VAR_047408|||http://purl.uniprot.org/annotation/VSP_005081
http://togogenome.org/gene/9606:NHS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6T4R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin remodeling regulator NHS|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||WAVE homology domain (WHD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096810|||http://purl.uniprot.org/annotation/VAR_021527|||http://purl.uniprot.org/annotation/VAR_021528|||http://purl.uniprot.org/annotation/VAR_036225|||http://purl.uniprot.org/annotation/VAR_051234|||http://purl.uniprot.org/annotation/VAR_076261|||http://purl.uniprot.org/annotation/VAR_076438|||http://purl.uniprot.org/annotation/VSP_046537|||http://purl.uniprot.org/annotation/VSP_046538|||http://purl.uniprot.org/annotation/VSP_046539|||http://purl.uniprot.org/annotation/VSP_046540|||http://purl.uniprot.org/annotation/VSP_046541
http://togogenome.org/gene/9606:MAPK8IP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13387                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 2|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||JNK-binding domain (JBD)|||Necessary for interaction with FGF13|||PID|||Phosphoserine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220631|||http://purl.uniprot.org/annotation/VAR_049666|||http://purl.uniprot.org/annotation/VSP_002770|||http://purl.uniprot.org/annotation/VSP_002771|||http://purl.uniprot.org/annotation/VSP_002772|||http://purl.uniprot.org/annotation/VSP_002773|||http://purl.uniprot.org/annotation/VSP_002774
http://togogenome.org/gene/9606:ZC2HC1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KMY6|||http://purl.uniprot.org/uniprot/Q53FD0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC/C3H-type|||Disordered|||In isoform 2.|||Polar residues|||Zinc finger C2HC domain-containing protein 1C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089940|||http://purl.uniprot.org/annotation/VSP_043105
http://togogenome.org/gene/9606:SPI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17947                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ETS|||In AGM10; undetectable protein expression in peripheral blood mononuclear cells.|||In AGM10; very low protein expression, if any, in peripheral blood mononuclear cells; when tested in transfected cells, decreased transcription activation; in vitro, fails to bind PU motif-containing DNA probes; does not affect interaction with IRF4 and IRF8, nor nuclear localization.|||In isoform 2.|||Phosphoserine|||Transcription factor PU.1|||contacts bases in the GGAA sequence in the major groove|||contacts the phosphate backbone of the GGAA sequence in the minor groove upstream|||forms a salt bridge with the phosphate backbone of the opposite strand downstream of the GGAA core sequence                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204132|||http://purl.uniprot.org/annotation/VAR_086811|||http://purl.uniprot.org/annotation/VAR_086812|||http://purl.uniprot.org/annotation/VAR_086813|||http://purl.uniprot.org/annotation/VAR_086814|||http://purl.uniprot.org/annotation/VSP_038690
http://togogenome.org/gene/9606:MARS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GW9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||In COXPD25.|||Methionine--tRNA ligase, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045493|||http://purl.uniprot.org/annotation/VAR_073858
http://togogenome.org/gene/9606:CLDN22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7P3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-22|||Cytoplasmic|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144785
http://togogenome.org/gene/9606:ANKRD29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6D5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat domain-containing protein 29|||In a breast cancer sample; somatic mutation.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243903|||http://purl.uniprot.org/annotation/VAR_026869|||http://purl.uniprot.org/annotation/VAR_035610|||http://purl.uniprot.org/annotation/VSP_019488
http://togogenome.org/gene/9606:INTS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU90|||http://purl.uniprot.org/uniprot/Q9UL03                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  INTS6/SAGE1/DDX26B/CT45 C-terminal|||In isoform 2.|||In isoform 3.|||Integrator complex subunit 6|||Phosphoserine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259543|||http://purl.uniprot.org/annotation/VSP_021457|||http://purl.uniprot.org/annotation/VSP_021458|||http://purl.uniprot.org/annotation/VSP_041356
http://togogenome.org/gene/9606:RBM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4W4|||http://purl.uniprot.org/uniprot/A0A0S2Z4X1|||http://purl.uniprot.org/uniprot/P98175|||http://purl.uniprot.org/uniprot/Q7Z3D7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type; atypical|||Disordered|||G-patch|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||N-acetylserine|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||RNA-binding protein 10|||RRM|||RRM 1|||RRM 2|||RanBP2-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081767|||http://purl.uniprot.org/annotation/VAR_035486|||http://purl.uniprot.org/annotation/VSP_036035|||http://purl.uniprot.org/annotation/VSP_036173|||http://purl.uniprot.org/annotation/VSP_059341
http://togogenome.org/gene/9606:ILF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DY09|||http://purl.uniprot.org/uniprot/F4ZW62|||http://purl.uniprot.org/uniprot/Q12905|||http://purl.uniprot.org/uniprot/Q53FG3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine; alternate|||Completely abolishes the effect of CRBN on ILF2.|||DZF|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interleukin enhancer-binding factor 2|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126063
http://togogenome.org/gene/9606:KRTAP9-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MVA2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||16 X 5 AA repeats of C-C-[GSVRQ]-[QTSPHN]-[TPSGYC]|||2|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 9-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332260|||http://purl.uniprot.org/annotation/VAR_042997
http://togogenome.org/gene/9606:FFAR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C6KYL4|||http://purl.uniprot.org/uniprot/O15552                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of SCFA-induced G protein-coupled receptor activity.|||Complete loss of acetate-induced G protein-coupled receptor activity.|||Cytoplasmic|||Disordered|||Extracellular|||Free fatty acid receptor 2|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||No effect on SCFA-induced G protein-coupled receptor activity.|||Partial loss of SCFA-independent constitutive G protein-coupled receptor activity.|||Partial loss of SCFA-induced G protein-coupled receptor activity.|||Partial loss of propionate-induced G protein-coupled receptor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069571|||http://purl.uniprot.org/annotation/VAR_011861
http://togogenome.org/gene/9606:TFCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12800                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Alpha-globin transcription factor CP2|||Basic and acidic residues|||DNA-binding|||Disordered|||Does not affect DNA-binding activity.|||Grh/CP2 DB|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||Phosphoserine|||Polar residues|||Significant reduction of DNA-binding activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228001|||http://purl.uniprot.org/annotation/VSP_017647|||http://purl.uniprot.org/annotation/VSP_017648
http://togogenome.org/gene/9606:SEL1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TEA6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein sel-1 homolog 2|||Sel1-like 1|||Sel1-like 10|||Sel1-like 11|||Sel1-like 2|||Sel1-like 3|||Sel1-like 4|||Sel1-like 5|||Sel1-like 6|||Sel1-like 7|||Sel1-like 8|||Sel1-like 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305159|||http://purl.uniprot.org/annotation/VAR_035172|||http://purl.uniprot.org/annotation/VAR_053964|||http://purl.uniprot.org/annotation/VSP_046937
http://togogenome.org/gene/9606:PAXX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUH6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished interaction with XRCC5/Ku80 and XRCC6/Ku70.|||Abolishes the association with the non-homologous end joining complex and localization to double-strand break sites. Abolished interaction with XRCC6/Ku70.|||Abolishes the association with the non-homologous end joining complex.|||Abolishes the association with the non-homologous end joining complex. Abolished interaction with XRCC6/Ku70.|||Disordered|||Does not affect interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with 145-D--152.|||Does not affect interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with A-134.|||In isoform 2.|||Loss of function in DNA non-homologous end joining (NHEJ).|||Mediates interaction with XRCC5/Ku80 and XRCC6/Ku70 and association with the non-homologous end joining core complex|||PISA|||Phospho-mimetic mutant; abolished interaction with DNA-bound the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with 145-D--152.|||Phospho-mimetic mutant; abolished interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer; when associated with D-134.|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein PAXX|||XLM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286104|||http://purl.uniprot.org/annotation/VSP_024996|||http://purl.uniprot.org/annotation/VSP_024997
http://togogenome.org/gene/9606:LIFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1Z4|||http://purl.uniprot.org/uniprot/P42702                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Helical|||In STWS1.|||In a colorectal cancer sample; somatic mutation.|||Leukemia inhibitory factor receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010902|||http://purl.uniprot.org/annotation/VAR_021996|||http://purl.uniprot.org/annotation/VAR_025666|||http://purl.uniprot.org/annotation/VAR_029109|||http://purl.uniprot.org/annotation/VAR_029110|||http://purl.uniprot.org/annotation/VAR_029111|||http://purl.uniprot.org/annotation/VAR_036166|||http://purl.uniprot.org/annotation/VAR_038626
http://togogenome.org/gene/9606:PCDHGB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-B7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003983|||http://purl.uniprot.org/annotation/VAR_048573|||http://purl.uniprot.org/annotation/VSP_008696|||http://purl.uniprot.org/annotation/VSP_008697
http://togogenome.org/gene/9606:PAX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06710|||http://purl.uniprot.org/uniprot/R9W7C9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In CHNG2; loss of activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PAI subdomain|||Paired|||Paired box protein Pax-8|||Phosphoserine|||Polar residues|||RED subdomain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050197|||http://purl.uniprot.org/annotation/VAR_012769|||http://purl.uniprot.org/annotation/VAR_012770|||http://purl.uniprot.org/annotation/VAR_012771|||http://purl.uniprot.org/annotation/VAR_012772|||http://purl.uniprot.org/annotation/VAR_012773|||http://purl.uniprot.org/annotation/VSP_002372|||http://purl.uniprot.org/annotation/VSP_002373|||http://purl.uniprot.org/annotation/VSP_002374|||http://purl.uniprot.org/annotation/VSP_002375
http://togogenome.org/gene/9606:MCM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4T1|||http://purl.uniprot.org/uniprot/A0A499FHX9|||http://purl.uniprot.org/uniprot/B4DUQ9|||http://purl.uniprot.org/uniprot/P25205                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  50% reduction in phosphorylation by ATM or ATR.|||Arginine finger|||Basic and acidic residues|||DNA replication licensing factor MCM3|||Disordered|||In isoform 2.|||MCM|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194093|||http://purl.uniprot.org/annotation/VAR_014810|||http://purl.uniprot.org/annotation/VAR_014811|||http://purl.uniprot.org/annotation/VAR_014812|||http://purl.uniprot.org/annotation/VAR_020427|||http://purl.uniprot.org/annotation/VAR_020516|||http://purl.uniprot.org/annotation/VAR_020517|||http://purl.uniprot.org/annotation/VSP_057050
http://togogenome.org/gene/9606:GPR149                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2MKA6|||http://purl.uniprot.org/uniprot/Q86SP6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 149                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069626
http://togogenome.org/gene/9606:RBMS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15434                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||RNA-binding motif, single-stranded-interacting protein 2|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081800
http://togogenome.org/gene/9606:ATXN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBB4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  Ataxin-10|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064748|||http://purl.uniprot.org/annotation/VSP_042526
http://togogenome.org/gene/9606:PPHLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEY8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 2, isoform 6, isoform 8 and isoform 9.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 5 and isoform 7.|||In isoform 7.|||In isoform 9.|||N6-acetyllysine; alternate|||Nuclear localization signal|||Periphilin-1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058537|||http://purl.uniprot.org/annotation/VAR_036233|||http://purl.uniprot.org/annotation/VSP_009898|||http://purl.uniprot.org/annotation/VSP_009899|||http://purl.uniprot.org/annotation/VSP_009900|||http://purl.uniprot.org/annotation/VSP_009902|||http://purl.uniprot.org/annotation/VSP_009903|||http://purl.uniprot.org/annotation/VSP_009904|||http://purl.uniprot.org/annotation/VSP_009905|||http://purl.uniprot.org/annotation/VSP_009906|||http://purl.uniprot.org/annotation/VSP_009907|||http://purl.uniprot.org/annotation/VSP_054078
http://togogenome.org/gene/9606:GPRC6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6X5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor family C group 6 member A|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||In isoform 3.|||Interchain|||Loss of function.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000043196|||http://purl.uniprot.org/annotation/VAR_023966|||http://purl.uniprot.org/annotation/VAR_049283|||http://purl.uniprot.org/annotation/VAR_061203|||http://purl.uniprot.org/annotation/VSP_016454|||http://purl.uniprot.org/annotation/VSP_016455
http://togogenome.org/gene/9606:CTRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17538                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Chymotrypsin B chain A|||Chymotrypsin B chain B|||Chymotrypsin B chain C|||Chymotrypsinogen B|||Peptidase S1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027638|||http://purl.uniprot.org/annotation/PRO_0000027639|||http://purl.uniprot.org/annotation/PRO_0000027640|||http://purl.uniprot.org/annotation/PRO_0000027641|||http://purl.uniprot.org/annotation/VAR_014566|||http://purl.uniprot.org/annotation/VAR_057158
http://togogenome.org/gene/9606:CDK5R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13319                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region                                                                                  ^@                                                                                  Absent from the cell periphery.|||Cyclin-dependent kinase 5 activator 2|||Disordered|||N-myristoyl glycine|||Phosphothreonine|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004800|||http://purl.uniprot.org/annotation/PRO_0000004801
http://togogenome.org/gene/9606:UBXN7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94888                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with VCP/p97.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N-acetylalanine|||No effect on interactions with CUL2 and HIF1A.|||Phosphoserine|||Phosphothreonine|||Removed|||Severely reduces interaction with neddylated CUL2.|||UBA|||UBX|||UBX domain-containing protein 7|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211035
http://togogenome.org/gene/9606:SLC5A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q1EHB4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sodium-coupled monocarboxylate transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337680|||http://purl.uniprot.org/annotation/VAR_043703|||http://purl.uniprot.org/annotation/VSP_033994|||http://purl.uniprot.org/annotation/VSP_033995
http://togogenome.org/gene/9606:TRAF3IP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AJU2|||http://purl.uniprot.org/uniprot/B3KWQ9|||http://purl.uniprot.org/uniprot/Q9Y228                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Anchor for type IV membrane protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||TRAF3-interacting JNK-activating modulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072403|||http://purl.uniprot.org/annotation/VAR_024283|||http://purl.uniprot.org/annotation/VAR_035664|||http://purl.uniprot.org/annotation/VSP_017271|||http://purl.uniprot.org/annotation/VSP_017272|||http://purl.uniprot.org/annotation/VSP_017273
http://togogenome.org/gene/9606:NOC4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVI4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Nucleolar complex protein 4 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173484
http://togogenome.org/gene/9606:CRYGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2A4T3|||http://purl.uniprot.org/uniprot/P11844                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Beta/gamma crystallin 'Greek key'|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||Found in a patient with congenital bilateral cataract; unknown pathological significance.|||Found in a patient with congenital pediatric onset cataracts; unknown pathological significance.|||Gamma-crystallin A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057585|||http://purl.uniprot.org/annotation/VAR_021139|||http://purl.uniprot.org/annotation/VAR_084796|||http://purl.uniprot.org/annotation/VAR_084797
http://togogenome.org/gene/9606:IFNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8GUN6|||http://purl.uniprot.org/uniprot/P01579                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Interferon gamma|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; in dimeric form|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016444|||http://purl.uniprot.org/annotation/PRO_0000259481|||http://purl.uniprot.org/annotation/PRO_5030767341|||http://purl.uniprot.org/annotation/VAR_004017|||http://purl.uniprot.org/annotation/VAR_004018
http://togogenome.org/gene/9606:DYNLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63167                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand                                                                                  ^@                                                                                  Abolishes growth factor-mediated phosphorylation. Increases BCL2L11 protein level and promotes apoptosis.|||Abolishes homodimerization. Abolishes interaction with BCL2L11 isoform 1 and isoform 2.|||Abolishes interaction with PAK1.|||Dynein light chain 1, cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with ESR1|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195125
http://togogenome.org/gene/9606:PCBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57721                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 5.|||KH 1|||KH 2|||KH 3|||Poly(rC)-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050092|||http://purl.uniprot.org/annotation/VSP_009947|||http://purl.uniprot.org/annotation/VSP_009948|||http://purl.uniprot.org/annotation/VSP_010014
http://togogenome.org/gene/9606:CD44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16070                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD44 antigen|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In In(A) antigen.|||In isoform 10, isoform 13 and isoform 14.|||In isoform 11.|||In isoform 12, isoform 15 and isoform 18.|||In isoform 18.|||In isoform 19.|||In isoform 2.|||In isoform 3 and isoform 16.|||In isoform 4.|||In isoform 5 and isoform 17.|||In isoform 6, isoform 16 and isoform 17.|||In isoform 7 and isoform 14.|||In isoform 8, isoform 13 and isoform 14.|||In isoform 9 and isoform 15.|||Link|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues|||Required for interaction with EZR, MSN and RDX and for co-localization to microvilli|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026687|||http://purl.uniprot.org/annotation/VAR_006490|||http://purl.uniprot.org/annotation/VAR_021147|||http://purl.uniprot.org/annotation/VAR_030325|||http://purl.uniprot.org/annotation/VAR_030326|||http://purl.uniprot.org/annotation/VAR_030327|||http://purl.uniprot.org/annotation/VSP_005303|||http://purl.uniprot.org/annotation/VSP_005304|||http://purl.uniprot.org/annotation/VSP_005305|||http://purl.uniprot.org/annotation/VSP_005306|||http://purl.uniprot.org/annotation/VSP_005307|||http://purl.uniprot.org/annotation/VSP_005308|||http://purl.uniprot.org/annotation/VSP_005309|||http://purl.uniprot.org/annotation/VSP_005310|||http://purl.uniprot.org/annotation/VSP_005311|||http://purl.uniprot.org/annotation/VSP_005312|||http://purl.uniprot.org/annotation/VSP_005313|||http://purl.uniprot.org/annotation/VSP_005314|||http://purl.uniprot.org/annotation/VSP_005315|||http://purl.uniprot.org/annotation/VSP_005316|||http://purl.uniprot.org/annotation/VSP_005317|||http://purl.uniprot.org/annotation/VSP_005318|||http://purl.uniprot.org/annotation/VSP_005319|||http://purl.uniprot.org/annotation/VSP_005320|||http://purl.uniprot.org/annotation/VSP_005321|||http://purl.uniprot.org/annotation/VSP_022797|||http://purl.uniprot.org/annotation/VSP_043575|||http://purl.uniprot.org/annotation/VSP_043870|||http://purl.uniprot.org/annotation/VSP_043871
http://togogenome.org/gene/9606:SLC15A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T8H0|||http://purl.uniprot.org/uniprot/Q8IY34                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 15 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295912|||http://purl.uniprot.org/annotation/VAR_034592
http://togogenome.org/gene/9606:RBM41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KYC8|||http://purl.uniprot.org/uniprot/Q96IZ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||RNA-binding protein 41|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256267|||http://purl.uniprot.org/annotation/VAR_028897|||http://purl.uniprot.org/annotation/VSP_021346|||http://purl.uniprot.org/annotation/VSP_021347|||http://purl.uniprot.org/annotation/VSP_021348|||http://purl.uniprot.org/annotation/VSP_021349
http://togogenome.org/gene/9606:NRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWT2|||http://purl.uniprot.org/uniprot/Q9NPD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated glycine|||Neuritin|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262512|||http://purl.uniprot.org/annotation/PRO_0000262513
http://togogenome.org/gene/9606:UBE2QL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L167                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site                                                                                  ^@                                                                                  Enhanced ubiquitin binding.|||Glycyl thioester intermediate|||UBC core|||Ubiquitin-conjugating enzyme E2Q-like protein 1|||Unable to bind ubiquitin.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335811
http://togogenome.org/gene/9606:ZNF283                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7M2                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 283                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047507|||http://purl.uniprot.org/annotation/VAR_057416|||http://purl.uniprot.org/annotation/VAR_057417|||http://purl.uniprot.org/annotation/VAR_060605|||http://purl.uniprot.org/annotation/VAR_060606|||http://purl.uniprot.org/annotation/VAR_060607
http://togogenome.org/gene/9606:C4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C0L4|||http://purl.uniprot.org/uniprot/P0C0L5                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2.5-3 fold-decrease in hemolytic activity, 3-fold increase in C1-dependent binding to IgG.|||20% decrease in hemolytic activity, 2-fold increase in C1-dependent binding to IgG.|||30-40% decrease in hemolytic activity and C1-dependent binding to IgG.|||50-60% decrease in hemolytic activity and C1-dependent binding to IgG.|||Anaphylatoxin-like|||C4a anaphylatoxin|||C4b-A|||C4b-B|||C4d-A|||C4d-B|||Complement C4 beta chain|||Complement C4 gamma chain|||Complement C4-A alpha chain|||Complement C4-B alpha chain|||In allotype C4A1, allotype C4A13.|||In allotype C4A1, allotype C4A2.|||In allotype C4A1, allotype C4A3a, allotype C4A6.|||In allotype C4A1.|||In allotype C4A3a, allotype C4A6.|||In allotype C4A3a.|||In allotype C4A4.|||In allotype C4A6.|||In allotype C4B-long and allotype C4B2.|||In allotype C4B-long.|||In allotype C4B1-SC01.|||In allotype C4B1-hi.|||In allotype C4B1a.|||In allotype C4B2 and allotype C4B5-Rg1.|||In allotype C4B5-Rg1.|||In isoform 2.|||Isoglutamyl cysteine thioester (Cys-Gln)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||NTR|||No effect on hemolytic activity, nor on C1-dependent binding to IgG.|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphoserine; by FAM20C|||Responsible for effective binding to form amide bonds with immune aggregates or protein antigens|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005966|||http://purl.uniprot.org/annotation/PRO_0000005967|||http://purl.uniprot.org/annotation/PRO_0000005968|||http://purl.uniprot.org/annotation/PRO_0000005969|||http://purl.uniprot.org/annotation/PRO_0000005970|||http://purl.uniprot.org/annotation/PRO_0000005971|||http://purl.uniprot.org/annotation/PRO_0000005972|||http://purl.uniprot.org/annotation/PRO_0000042698|||http://purl.uniprot.org/annotation/PRO_0000042699|||http://purl.uniprot.org/annotation/PRO_0000042700|||http://purl.uniprot.org/annotation/PRO_0000042701|||http://purl.uniprot.org/annotation/PRO_0000042702|||http://purl.uniprot.org/annotation/PRO_0000042703|||http://purl.uniprot.org/annotation/PRO_0000042704|||http://purl.uniprot.org/annotation/PRO_0000042705|||http://purl.uniprot.org/annotation/PRO_0000042706|||http://purl.uniprot.org/annotation/VAR_001987|||http://purl.uniprot.org/annotation/VAR_001988|||http://purl.uniprot.org/annotation/VAR_001992|||http://purl.uniprot.org/annotation/VAR_001993|||http://purl.uniprot.org/annotation/VAR_001994|||http://purl.uniprot.org/annotation/VAR_001995|||http://purl.uniprot.org/annotation/VAR_019778|||http://purl.uniprot.org/annotation/VAR_019779|||http://purl.uniprot.org/annotation/VAR_019780|||http://purl.uniprot.org/annotation/VAR_023729|||http://purl.uniprot.org/annotation/VAR_023730|||http://purl.uniprot.org/annotation/VAR_023731|||http://purl.uniprot.org/annotation/VAR_023732|||http://purl.uniprot.org/annotation/VAR_023734|||http://purl.uniprot.org/annotation/VAR_023735|||http://purl.uniprot.org/annotation/VAR_069154|||http://purl.uniprot.org/annotation/VAR_069155|||http://purl.uniprot.org/annotation/VAR_069156|||http://purl.uniprot.org/annotation/VAR_069158|||http://purl.uniprot.org/annotation/VAR_069159|||http://purl.uniprot.org/annotation/VAR_069160|||http://purl.uniprot.org/annotation/VAR_069161|||http://purl.uniprot.org/annotation/VSP_046252
http://togogenome.org/gene/9606:CALR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJF7|||http://purl.uniprot.org/uniprot/Q96L12                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||3 X approximate repeats|||4 X approximate repeats|||C-domain|||Calreticulin|||Calreticulin-3|||Found in a patient with hypertrophic cardiomyopathy; unknown pathological significance.|||N-domain|||N-linked (GlcNAc...) asparagine|||P-domain|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004178|||http://purl.uniprot.org/annotation/PRO_5007356948|||http://purl.uniprot.org/annotation/VAR_027944|||http://purl.uniprot.org/annotation/VAR_027945|||http://purl.uniprot.org/annotation/VAR_027946|||http://purl.uniprot.org/annotation/VAR_048589|||http://purl.uniprot.org/annotation/VAR_065476
http://togogenome.org/gene/9606:CORO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57737                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coronin-7|||Disordered|||Does not affect ability to regulate the anterograde Golgi to endosome transport.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ability to regulate the anterograde Golgi to endosome transport.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050934|||http://purl.uniprot.org/annotation/VAR_057585|||http://purl.uniprot.org/annotation/VAR_057586|||http://purl.uniprot.org/annotation/VAR_057587|||http://purl.uniprot.org/annotation/VAR_057588|||http://purl.uniprot.org/annotation/VSP_038152|||http://purl.uniprot.org/annotation/VSP_046022|||http://purl.uniprot.org/annotation/VSP_046752
http://togogenome.org/gene/9606:RAB7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AH8                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif                                                                                  ^@                                                                                  Effector region|||Phosphoserine|||Ras-related protein Rab-7b|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121125
http://togogenome.org/gene/9606:ZNF644                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E234|||http://purl.uniprot.org/uniprot/Q9H582                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In MYP21.|||In MYP21; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Variant of uncertain significance.|||Zinc finger protein 644                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047698|||http://purl.uniprot.org/annotation/VAR_035593|||http://purl.uniprot.org/annotation/VAR_052885|||http://purl.uniprot.org/annotation/VAR_052886|||http://purl.uniprot.org/annotation/VAR_066389|||http://purl.uniprot.org/annotation/VAR_066390|||http://purl.uniprot.org/annotation/VAR_066391|||http://purl.uniprot.org/annotation/VAR_066392|||http://purl.uniprot.org/annotation/VAR_073995|||http://purl.uniprot.org/annotation/VAR_073996|||http://purl.uniprot.org/annotation/VAR_073997|||http://purl.uniprot.org/annotation/VAR_073998|||http://purl.uniprot.org/annotation/VAR_073999|||http://purl.uniprot.org/annotation/VAR_074000|||http://purl.uniprot.org/annotation/VAR_074001|||http://purl.uniprot.org/annotation/VAR_074002|||http://purl.uniprot.org/annotation/VAR_074003|||http://purl.uniprot.org/annotation/VAR_074004|||http://purl.uniprot.org/annotation/VAR_074005|||http://purl.uniprot.org/annotation/VAR_074006|||http://purl.uniprot.org/annotation/VAR_074007|||http://purl.uniprot.org/annotation/VAR_074008|||http://purl.uniprot.org/annotation/VSP_012158|||http://purl.uniprot.org/annotation/VSP_012159|||http://purl.uniprot.org/annotation/VSP_015855|||http://purl.uniprot.org/annotation/VSP_015856
http://togogenome.org/gene/9606:METTL14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCE5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased methyltransferase activity of the heterodimer complex formed with METTL3.|||Disordered|||Does not affect interaction with METTL3.|||Does not affect methyltransferase activity of the heterodimer complex formed with METTL3.|||Does not affect nuclear localization.|||Interaction with METTL3|||Little or no effect on S-adenosyl-L-methionine-binding or methyltransferase activity; when associated with A-192.|||Little or no effect on methyltransferase activity of the heterodimer complex formed with METTL3.|||Little or no effect on methyltransferase activity. Little or no effect on S-adenosyl-L-methionine-binding or methyltransferase activity; when associated with A-173.|||N6-adenosine-methyltransferase non-catalytic subunit|||Phosphoserine|||Positively charged region required for RNA-binding|||Reduced RNA-binding.|||Reduced RNA-binding. Reduced RNA-binding; when associated with E-255.|||Reduced RNA-binding; when associated with E-245.|||Strongly decreased methyltransferase activity of the heterodimer complex formed with METTL3, probably due to reduced RNA-binding.|||Strongly reduced methyltransferase activity of the heterodimer complex formed with METTL3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325790
http://togogenome.org/gene/9606:LY9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFU4|||http://purl.uniprot.org/uniprot/Q05CA2|||http://purl.uniprot.org/uniprot/Q0VAI0|||http://purl.uniprot.org/uniprot/Q5VYH9|||http://purl.uniprot.org/uniprot/Q9HBG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreases interaction with SH2D1A and INPP5D 2-fold, reduced T-cell response.|||Disordered|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type 1|||Ig-like V-type 2|||Immunoglobulin subtype|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||T-lymphocyte surface antigen Ly-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014851|||http://purl.uniprot.org/annotation/VAR_033612|||http://purl.uniprot.org/annotation/VSP_002524|||http://purl.uniprot.org/annotation/VSP_002525|||http://purl.uniprot.org/annotation/VSP_002526|||http://purl.uniprot.org/annotation/VSP_043328
http://togogenome.org/gene/9606:SPOCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08629                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Kazal-like|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (glycosaminoglycan) serine|||Testican-1|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026699
http://togogenome.org/gene/9606:LOC102723996                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y5W7|||http://purl.uniprot.org/uniprot/A0A8V8TQV9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Ig-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5036456740|||http://purl.uniprot.org/annotation/PRO_5036470495
http://togogenome.org/gene/9606:PSAPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUJ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Saposin A-like|||Saposin A-type 1|||Saposin A-type 2|||Saposin B-Val-like|||Saposin B-like|||Saposin B-type 1|||Saposin B-type 2|||Saposin B-type 3|||Saposin B-type 4|||Saposin C-like|||Saposin D-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280305|||http://purl.uniprot.org/annotation/PRO_0000280306|||http://purl.uniprot.org/annotation/PRO_0000280307|||http://purl.uniprot.org/annotation/PRO_0000280308|||http://purl.uniprot.org/annotation/PRO_0000280309|||http://purl.uniprot.org/annotation/PRO_0000280310|||http://purl.uniprot.org/annotation/PRO_0000280311|||http://purl.uniprot.org/annotation/PRO_0000280312|||http://purl.uniprot.org/annotation/PRO_0000280313|||http://purl.uniprot.org/annotation/PRO_0000280314|||http://purl.uniprot.org/annotation/VAR_051895|||http://purl.uniprot.org/annotation/VAR_051896|||http://purl.uniprot.org/annotation/VAR_061780|||http://purl.uniprot.org/annotation/VAR_061781|||http://purl.uniprot.org/annotation/VAR_061782
http://togogenome.org/gene/9606:CEP43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV25|||http://purl.uniprot.org/uniprot/B4DH64|||http://purl.uniprot.org/uniprot/O95684                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization and leads to aggregation.|||Basic and acidic residues|||Breakpoint for translocation to form CEP43-FGFR1 or FGFR1-CEP43 fusion proteins|||Centrosomal protein 43|||Disordered|||In isoform 2.|||In isoform 3.|||LisH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233293|||http://purl.uniprot.org/annotation/VAR_051000|||http://purl.uniprot.org/annotation/VAR_061651|||http://purl.uniprot.org/annotation/VSP_018119|||http://purl.uniprot.org/annotation/VSP_018120|||http://purl.uniprot.org/annotation/VSP_018121
http://togogenome.org/gene/9606:MT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07438                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197235
http://togogenome.org/gene/9606:TRIM62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVG3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin ligase activity.|||B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM62|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249574|||http://purl.uniprot.org/annotation/VSP_055441|||http://purl.uniprot.org/annotation/VSP_055442
http://togogenome.org/gene/9606:FAM83E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2I3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Polar residues|||Protein FAM83E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314929|||http://purl.uniprot.org/annotation/VAR_038130|||http://purl.uniprot.org/annotation/VAR_038131|||http://purl.uniprot.org/annotation/VAR_038132
http://togogenome.org/gene/9606:LRRC55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0H1|||http://purl.uniprot.org/uniprot/Q6ZSA7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232913
http://togogenome.org/gene/9606:RAB9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP90                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||Phosphoserine|||Ras-related protein Rab-9B|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121142
http://togogenome.org/gene/9606:ACBD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAA8|||http://purl.uniprot.org/uniprot/Q9BR61                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Turn                                                                                  ^@                                                                                  ACB|||ANK|||ANK 1|||ANK 2|||Acyl-CoA-binding domain-containing protein 6|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232879
http://togogenome.org/gene/9606:TH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07101|||http://purl.uniprot.org/uniprot/P78428                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects subcellular localization. Accumulates mainly in the soma of the neuroblastoma cells.|||Disordered|||Does not affect subcellular localization. Distributed throughout the soma and neurites.|||Found in a patient with ARSEGS; unknown pathological significance.|||Important for substrate specificity|||In ARSEGS.|||In ARSEGS; complete loss of tyrosine 3-monooxygenase activity.|||In ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity.|||In ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa.|||In ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity.|||In ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine.|||In ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa.|||In ARSEGS; no effect on tyrosine 3-monooxygenase activity.|||In ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity.|||In ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity.|||In ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D).|||In ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and tyrosine 3-monooxygenase activity; rare mutation.|||In isoform 1.|||In isoform 2 and isoform 6.|||In isoform 4 and isoform 5.|||In isoform 5 and isoform 6.|||Phosphoserine|||Phosphoserine; by CaMK2|||Phosphoserine; by CaMK2 and PKA|||Suppresses feedback inhibition induced by dopamine. Suppresses feedback inhibition induced by dopamine; when associated with A-207.|||Suppresses the decrease in tyrosine 3-monooxygenase activity induced by NEM modification. Suppresses feedback inhibition induced by dopamine; when associated with E-71.|||Tyrosine 3-monooxygenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205561|||http://purl.uniprot.org/annotation/VAR_014025|||http://purl.uniprot.org/annotation/VAR_014026|||http://purl.uniprot.org/annotation/VAR_014027|||http://purl.uniprot.org/annotation/VAR_014028|||http://purl.uniprot.org/annotation/VAR_014029|||http://purl.uniprot.org/annotation/VAR_014030|||http://purl.uniprot.org/annotation/VAR_014031|||http://purl.uniprot.org/annotation/VAR_014032|||http://purl.uniprot.org/annotation/VAR_014033|||http://purl.uniprot.org/annotation/VAR_071715|||http://purl.uniprot.org/annotation/VAR_071716|||http://purl.uniprot.org/annotation/VAR_071717|||http://purl.uniprot.org/annotation/VAR_071718|||http://purl.uniprot.org/annotation/VAR_071719|||http://purl.uniprot.org/annotation/VAR_071720|||http://purl.uniprot.org/annotation/VAR_072862|||http://purl.uniprot.org/annotation/VAR_072863|||http://purl.uniprot.org/annotation/VAR_072864|||http://purl.uniprot.org/annotation/VAR_072865|||http://purl.uniprot.org/annotation/VAR_072866|||http://purl.uniprot.org/annotation/VAR_072867|||http://purl.uniprot.org/annotation/VAR_072868|||http://purl.uniprot.org/annotation/VAR_072869|||http://purl.uniprot.org/annotation/VAR_072870|||http://purl.uniprot.org/annotation/VAR_072871|||http://purl.uniprot.org/annotation/VAR_072872|||http://purl.uniprot.org/annotation/VAR_072873|||http://purl.uniprot.org/annotation/VAR_072874|||http://purl.uniprot.org/annotation/VAR_072875|||http://purl.uniprot.org/annotation/VAR_072876|||http://purl.uniprot.org/annotation/VAR_072877|||http://purl.uniprot.org/annotation/VAR_072878|||http://purl.uniprot.org/annotation/VAR_072879|||http://purl.uniprot.org/annotation/VAR_072880|||http://purl.uniprot.org/annotation/VAR_072881|||http://purl.uniprot.org/annotation/VAR_072882|||http://purl.uniprot.org/annotation/VAR_072883|||http://purl.uniprot.org/annotation/VAR_072884|||http://purl.uniprot.org/annotation/VAR_072885|||http://purl.uniprot.org/annotation/VAR_072886|||http://purl.uniprot.org/annotation/VAR_072887|||http://purl.uniprot.org/annotation/VSP_000541|||http://purl.uniprot.org/annotation/VSP_000543|||http://purl.uniprot.org/annotation/VSP_000544|||http://purl.uniprot.org/annotation/VSP_054338
http://togogenome.org/gene/9606:RNF126                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0Q1|||http://purl.uniprot.org/uniprot/Q9BV68                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C4-type|||Disordered|||E3 ubiquitin-protein ligase RNF126|||Impaired interaction with BAG6.|||Loss of E3 ligase activity; when associated with A-229.|||Loss of E3 ligase activity; when associated with A-232.|||N-acetylalanine|||Phosphoserine|||Polar residues|||RING-type|||Removed|||Required for interaction with BAG6|||Sufficient for interaction with AICDA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056093|||http://purl.uniprot.org/annotation/VAR_057217
http://togogenome.org/gene/9606:BNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12981                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Loss of proapoptotic effect. No effect on interaction with RINT1.|||Lumenal|||Vesicle transport protein SEC20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064960|||http://purl.uniprot.org/annotation/VAR_019169|||http://purl.uniprot.org/annotation/VSP_004330|||http://purl.uniprot.org/annotation/VSP_017901
http://togogenome.org/gene/9606:FRMD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FERM|||FERM domain-containing protein 6|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219448|||http://purl.uniprot.org/annotation/VSP_008022|||http://purl.uniprot.org/annotation/VSP_008023
http://togogenome.org/gene/9606:HUS1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHY5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Checkpoint protein HUS1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226245|||http://purl.uniprot.org/annotation/VAR_025497|||http://purl.uniprot.org/annotation/VAR_031206|||http://purl.uniprot.org/annotation/VAR_031207
http://togogenome.org/gene/9606:PEX14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75381                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Peroxisomal matrix|||Peroxisomal membrane protein PEX14|||Phosphoserine|||Polar residues|||Reduced interaction with PEX19, minor effect on interaction with PEX5.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058325|||http://purl.uniprot.org/annotation/VAR_051269|||http://purl.uniprot.org/annotation/VAR_051270|||http://purl.uniprot.org/annotation/VAR_051271|||http://purl.uniprot.org/annotation/VSP_037021
http://togogenome.org/gene/9606:H4C12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:RNF225                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0QZC1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||RING finger protein 225|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431309
http://togogenome.org/gene/9606:ZNF524                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  A.T hook|||Acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Pro residues|||Zinc finger protein 524                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234579
http://togogenome.org/gene/9606:FAM186B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYM0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Protein FAM186B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252147|||http://purl.uniprot.org/annotation/VAR_027777|||http://purl.uniprot.org/annotation/VAR_027778|||http://purl.uniprot.org/annotation/VSP_056992|||http://purl.uniprot.org/annotation/VSP_056993
http://togogenome.org/gene/9606:CWC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P013                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylthreonine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Spliceosome-associated protein CWC15 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291543
http://togogenome.org/gene/9606:SIGLEC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y336                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||Loss of sialic acid binding.|||N-linked (GlcNAc...) asparagine|||SLAM-like motif|||Sialic acid-binding Ig-like lectin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014949|||http://purl.uniprot.org/annotation/VAR_014254|||http://purl.uniprot.org/annotation/VAR_014255|||http://purl.uniprot.org/annotation/VAR_014256|||http://purl.uniprot.org/annotation/VAR_014257|||http://purl.uniprot.org/annotation/VAR_014258|||http://purl.uniprot.org/annotation/VAR_033621|||http://purl.uniprot.org/annotation/VAR_033622|||http://purl.uniprot.org/annotation/VSP_054106
http://togogenome.org/gene/9606:PHF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDL5|||http://purl.uniprot.org/uniprot/Q9UIL8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2HC pre-PHD-type|||In isoform 2.|||PHD finger protein 11|||PHD-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059301|||http://purl.uniprot.org/annotation/VSP_038088
http://togogenome.org/gene/9606:IL23R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWK5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with reduced disease susceptibility; has a protective effect against Crohn disease and psoriasis.|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interleukin-23 receptor|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000268662|||http://purl.uniprot.org/annotation/VAR_029752|||http://purl.uniprot.org/annotation/VAR_029753|||http://purl.uniprot.org/annotation/VAR_029754|||http://purl.uniprot.org/annotation/VAR_047955|||http://purl.uniprot.org/annotation/VSP_021990|||http://purl.uniprot.org/annotation/VSP_021991|||http://purl.uniprot.org/annotation/VSP_021992|||http://purl.uniprot.org/annotation/VSP_021993|||http://purl.uniprot.org/annotation/VSP_021994|||http://purl.uniprot.org/annotation/VSP_021995|||http://purl.uniprot.org/annotation/VSP_021996|||http://purl.uniprot.org/annotation/VSP_021997|||http://purl.uniprot.org/annotation/VSP_021998|||http://purl.uniprot.org/annotation/VSP_021999
http://togogenome.org/gene/9606:CSF3R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99062                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Granulocyte colony-stimulating factor receptor|||Helical|||Ig-like C2-type|||In SCN7; decreases localization to plasma membrane; decreases receptor signaling.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In neutrophilia.|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with apparently autosomal dominant severe congenital neutropenia; affects CSF3 mediated proliferation and survival of myeloid cells; abrogates receptor signaling by altering ligand binding; dominant negative effect.|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010874|||http://purl.uniprot.org/annotation/VAR_014325|||http://purl.uniprot.org/annotation/VAR_014326|||http://purl.uniprot.org/annotation/VAR_014327|||http://purl.uniprot.org/annotation/VAR_014328|||http://purl.uniprot.org/annotation/VAR_014329|||http://purl.uniprot.org/annotation/VAR_014330|||http://purl.uniprot.org/annotation/VAR_014331|||http://purl.uniprot.org/annotation/VAR_014332|||http://purl.uniprot.org/annotation/VAR_062517|||http://purl.uniprot.org/annotation/VAR_063065|||http://purl.uniprot.org/annotation/VAR_077011|||http://purl.uniprot.org/annotation/VSP_001671|||http://purl.uniprot.org/annotation/VSP_001672|||http://purl.uniprot.org/annotation/VSP_001673|||http://purl.uniprot.org/annotation/VSP_001674
http://togogenome.org/gene/9606:ECHS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30084                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Enoyl-CoA hydratase, mitochondrial|||Important for catalytic activity|||In ECHS1D.|||In ECHS1D; decreases enoyl-CoA hydratase activity of 70%; decreases significantly protein expression.|||In ECHS1D; decreases significantly enoyl-CoA hydratase activity; decreases significantly protein expression.|||In ECHS1D; unknown pathological significance.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007411|||http://purl.uniprot.org/annotation/VAR_022273|||http://purl.uniprot.org/annotation/VAR_022274|||http://purl.uniprot.org/annotation/VAR_073373|||http://purl.uniprot.org/annotation/VAR_073374|||http://purl.uniprot.org/annotation/VAR_076185|||http://purl.uniprot.org/annotation/VAR_076186|||http://purl.uniprot.org/annotation/VAR_076187|||http://purl.uniprot.org/annotation/VAR_076188|||http://purl.uniprot.org/annotation/VAR_076189|||http://purl.uniprot.org/annotation/VAR_076190|||http://purl.uniprot.org/annotation/VAR_076191|||http://purl.uniprot.org/annotation/VAR_076192|||http://purl.uniprot.org/annotation/VAR_076193|||http://purl.uniprot.org/annotation/VAR_076194|||http://purl.uniprot.org/annotation/VAR_076195|||http://purl.uniprot.org/annotation/VAR_076196|||http://purl.uniprot.org/annotation/VAR_076479|||http://purl.uniprot.org/annotation/VAR_076480
http://togogenome.org/gene/9606:VASN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EMK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Fibronectin type-III|||Helical|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Vasorin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232630|||http://purl.uniprot.org/annotation/VAR_025991
http://togogenome.org/gene/9606:SLC4A1AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWU0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||FHA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Kanadaptin|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076268|||http://purl.uniprot.org/annotation/VAR_024748|||http://purl.uniprot.org/annotation/VAR_051219
http://togogenome.org/gene/9606:SERPINC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01008                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Antithrombin-III|||In AT3D.|||In AT3D; Dreux; complete loss af heparin binding.|||In AT3D; Tours/Alger/Amiens/Toyama/Paris-1/Paris-2/Padua-2/Barcelona-2/Kumamoto/Omura/Sasebo; lacks heparin-binding ability.|||In AT3D; severely decreased antithrombin activity.|||In AT3D; severely decreased antithrombin activity; low affinity for heparin.|||In AT3D; type I and type-II.|||In AT3D; type I.|||In AT3D; type-I and -II; Whitechapel.|||In AT3D; type-I.|||In AT3D; type-I; Budapest-6.|||In AT3D; type-I; does not undergo post-translational glycosylation.|||In AT3D; type-I; severely decreased antithrombin activity.|||In AT3D; type-II.|||In AT3D; type-II; Budapest-3/Budapest-7.|||In AT3D; type-II; Budapest-5.|||In AT3D; type-II; Budapest.|||In AT3D; type-II; Cambridge-2.|||In AT3D; type-II; Charleville/Sudbury/Vicenza/Cambridge-1.|||In AT3D; type-II; Denver/Milano-2; deprived of inhibitory activity.|||In AT3D; type-II; Geneva.|||In AT3D; type-II; Glasgow-3.|||In AT3D; type-II; Glasgow/Sheffield/Chicago/Avranches/Kumamoto-2; increases affinity for heparin; deprived of inhibitory activity.|||In AT3D; type-II; Hamilton/Glasgow-2; reduces interaction with thrombin by 90%.|||In AT3D; type-II; Haslar/Whitechapel.|||In AT3D; type-II; Kyoto.|||In AT3D; type-II; La Rochelle.|||In AT3D; type-II; Maisons-Laffite.|||In AT3D; type-II; Nagasaki; defective heparin binding associated with thrombosis.|||In AT3D; type-II; Oslo/Paris-3.|||In AT3D; type-II; Pescara; deprived of inhibitory of activity.|||In AT3D; type-II; Rosny.|||In AT3D; type-II; Rouen-1/Padua-1/Bligny/Budapest-2; lack of heparin-binding properties.|||In AT3D; type-II; Rouen-2; lack of heparin-binding properties.|||In AT3D; type-II; Rouen-3; lack of heparin-binding properties.|||In AT3D; type-II; Rouen-4; lack of heparin-binding properties.|||In AT3D; type-II; Rouen-6; increases affinity for heparin.|||In AT3D; type-II; Southport.|||In AT3D; type-II; Stockholm.|||In AT3D; type-II; Torino.|||In AT3D; type-II; Truro; increases affinity for heparin.|||In AT3D; type-II; Utah; deprived of inhibitory activity.|||In AT3D; type-II; Vienna.|||In AT3D; type-II; lacks heparin-binding ability.|||In Dublin.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Previously Whitechapel.|||Reactive bond|||Reduces interaction with thrombin by 80%.|||Reduces interaction with thrombin by 99%.|||Variant Thr-414.|||Variant of uncertain significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032489|||http://purl.uniprot.org/annotation/VAR_007032|||http://purl.uniprot.org/annotation/VAR_007033|||http://purl.uniprot.org/annotation/VAR_007034|||http://purl.uniprot.org/annotation/VAR_007035|||http://purl.uniprot.org/annotation/VAR_007036|||http://purl.uniprot.org/annotation/VAR_007037|||http://purl.uniprot.org/annotation/VAR_007038|||http://purl.uniprot.org/annotation/VAR_007039|||http://purl.uniprot.org/annotation/VAR_007040|||http://purl.uniprot.org/annotation/VAR_007041|||http://purl.uniprot.org/annotation/VAR_007042|||http://purl.uniprot.org/annotation/VAR_007043|||http://purl.uniprot.org/annotation/VAR_007044|||http://purl.uniprot.org/annotation/VAR_007045|||http://purl.uniprot.org/annotation/VAR_007046|||http://purl.uniprot.org/annotation/VAR_007047|||http://purl.uniprot.org/annotation/VAR_007048|||http://purl.uniprot.org/annotation/VAR_007049|||http://purl.uniprot.org/annotation/VAR_007050|||http://purl.uniprot.org/annotation/VAR_007051|||http://purl.uniprot.org/annotation/VAR_007052|||http://purl.uniprot.org/annotation/VAR_007053|||http://purl.uniprot.org/annotation/VAR_007054|||http://purl.uniprot.org/annotation/VAR_007055|||http://purl.uniprot.org/annotation/VAR_007056|||http://purl.uniprot.org/annotation/VAR_007057|||http://purl.uniprot.org/annotation/VAR_007058|||http://purl.uniprot.org/annotation/VAR_007059|||http://purl.uniprot.org/annotation/VAR_007060|||http://purl.uniprot.org/annotation/VAR_007061|||http://purl.uniprot.org/annotation/VAR_007062|||http://purl.uniprot.org/annotation/VAR_007063|||http://purl.uniprot.org/annotation/VAR_007064|||http://purl.uniprot.org/annotation/VAR_007065|||http://purl.uniprot.org/annotation/VAR_007066|||http://purl.uniprot.org/annotation/VAR_007067|||http://purl.uniprot.org/annotation/VAR_007068|||http://purl.uniprot.org/annotation/VAR_007069|||http://purl.uniprot.org/annotation/VAR_007070|||http://purl.uniprot.org/annotation/VAR_007071|||http://purl.uniprot.org/annotation/VAR_007072|||http://purl.uniprot.org/annotation/VAR_007073|||http://purl.uniprot.org/annotation/VAR_007074|||http://purl.uniprot.org/annotation/VAR_007075|||http://purl.uniprot.org/annotation/VAR_007076|||http://purl.uniprot.org/annotation/VAR_007077|||http://purl.uniprot.org/annotation/VAR_007078|||http://purl.uniprot.org/annotation/VAR_007079|||http://purl.uniprot.org/annotation/VAR_007080|||http://purl.uniprot.org/annotation/VAR_007081|||http://purl.uniprot.org/annotation/VAR_007082|||http://purl.uniprot.org/annotation/VAR_007083|||http://purl.uniprot.org/annotation/VAR_007084|||http://purl.uniprot.org/annotation/VAR_007085|||http://purl.uniprot.org/annotation/VAR_007086|||http://purl.uniprot.org/annotation/VAR_007087|||http://purl.uniprot.org/annotation/VAR_007088|||http://purl.uniprot.org/annotation/VAR_007089|||http://purl.uniprot.org/annotation/VAR_007090|||http://purl.uniprot.org/annotation/VAR_007091|||http://purl.uniprot.org/annotation/VAR_007092|||http://purl.uniprot.org/annotation/VAR_009258|||http://purl.uniprot.org/annotation/VAR_012316|||http://purl.uniprot.org/annotation/VAR_012748|||http://purl.uniprot.org/annotation/VAR_012749|||http://purl.uniprot.org/annotation/VAR_012750|||http://purl.uniprot.org/annotation/VAR_013085|||http://purl.uniprot.org/annotation/VAR_027450|||http://purl.uniprot.org/annotation/VAR_027451|||http://purl.uniprot.org/annotation/VAR_027452|||http://purl.uniprot.org/annotation/VAR_027453|||http://purl.uniprot.org/annotation/VAR_027454|||http://purl.uniprot.org/annotation/VAR_027455|||http://purl.uniprot.org/annotation/VAR_027456|||http://purl.uniprot.org/annotation/VAR_027457|||http://purl.uniprot.org/annotation/VAR_027458|||http://purl.uniprot.org/annotation/VAR_027459|||http://purl.uniprot.org/annotation/VAR_027460|||http://purl.uniprot.org/annotation/VAR_027461|||http://purl.uniprot.org/annotation/VAR_027462|||http://purl.uniprot.org/annotation/VAR_027463|||http://purl.uniprot.org/annotation/VAR_027464|||http://purl.uniprot.org/annotation/VAR_027465|||http://purl.uniprot.org/annotation/VAR_027466|||http://purl.uniprot.org/annotation/VAR_027467|||http://purl.uniprot.org/annotation/VAR_027468|||http://purl.uniprot.org/annotation/VAR_027469|||http://purl.uniprot.org/annotation/VAR_027470|||http://purl.uniprot.org/annotation/VAR_027471|||http://purl.uniprot.org/annotation/VAR_027472|||http://purl.uniprot.org/annotation/VAR_027473|||http://purl.uniprot.org/annotation/VAR_071199|||http://purl.uniprot.org/annotation/VAR_071200|||http://purl.uniprot.org/annotation/VAR_071201|||http://purl.uniprot.org/annotation/VAR_071202|||http://purl.uniprot.org/annotation/VAR_071203|||http://purl.uniprot.org/annotation/VAR_071204|||http://purl.uniprot.org/annotation/VAR_071205|||http://purl.uniprot.org/annotation/VAR_071206|||http://purl.uniprot.org/annotation/VAR_086197|||http://purl.uniprot.org/annotation/VAR_086198|||http://purl.uniprot.org/annotation/VAR_086227
http://togogenome.org/gene/9606:CALHM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HA72                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcium homeostasis modulator protein 2|||Helical|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186720|||http://purl.uniprot.org/annotation/VAR_033924|||http://purl.uniprot.org/annotation/VAR_053084|||http://purl.uniprot.org/annotation/VSP_013853|||http://purl.uniprot.org/annotation/VSP_013854|||http://purl.uniprot.org/annotation/VSP_013855|||http://purl.uniprot.org/annotation/VSP_013856
http://togogenome.org/gene/9606:OR5H14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHG9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5H14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311997|||http://purl.uniprot.org/annotation/VAR_037393|||http://purl.uniprot.org/annotation/VAR_037394
http://togogenome.org/gene/9606:XRCC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AHC9|||http://purl.uniprot.org/uniprot/B4DE32|||http://purl.uniprot.org/uniprot/B4E356|||http://purl.uniprot.org/uniprot/P12956                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes adduct formation; when associated with A-31 and A-160.|||Abolishes adduct formation; when associated with A-31 and A-164.|||Basic and acidic residues|||Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with DEAF1|||Ku|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine|||Removed|||SAP|||Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activity|||X-ray repair cross-complementing protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210179|||http://purl.uniprot.org/annotation/VSP_056030
http://togogenome.org/gene/9606:SPACA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96E40                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Essential for interaction with INCA1|||In isoform 2.|||Sperm acrosome-associated protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089673|||http://purl.uniprot.org/annotation/VAR_056817|||http://purl.uniprot.org/annotation/VSP_014456|||http://purl.uniprot.org/annotation/VSP_014457
http://togogenome.org/gene/9606:CWF19L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TBE0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CWF19-like protein 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315648|||http://purl.uniprot.org/annotation/VAR_038268|||http://purl.uniprot.org/annotation/VAR_038269|||http://purl.uniprot.org/annotation/VAR_038270|||http://purl.uniprot.org/annotation/VAR_038271|||http://purl.uniprot.org/annotation/VAR_038272|||http://purl.uniprot.org/annotation/VSP_030590|||http://purl.uniprot.org/annotation/VSP_030591|||http://purl.uniprot.org/annotation/VSP_030592|||http://purl.uniprot.org/annotation/VSP_030593
http://togogenome.org/gene/9606:NARF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHQ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear prelamin A recognition factor|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288479|||http://purl.uniprot.org/annotation/VSP_025690|||http://purl.uniprot.org/annotation/VSP_025691|||http://purl.uniprot.org/annotation/VSP_046371
http://togogenome.org/gene/9606:HAAO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46952                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyanthranilate 3,4-dioxygenase|||Domain A (catalytic)|||Domain B|||In VCRL1; strongly reduced 3-hydroxyanthranilate 3,4-dioxygenase activity in vitro.|||In isoform 2.|||Linker                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064372|||http://purl.uniprot.org/annotation/VAR_021507|||http://purl.uniprot.org/annotation/VAR_030470|||http://purl.uniprot.org/annotation/VAR_080252|||http://purl.uniprot.org/annotation/VAR_080253|||http://purl.uniprot.org/annotation/VSP_036239
http://togogenome.org/gene/9606:ZNF621                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSS3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||In isoform 2.|||KRAB|||Zinc finger protein 621                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047693|||http://purl.uniprot.org/annotation/VSP_016041|||http://purl.uniprot.org/annotation/VSP_016042
http://togogenome.org/gene/9606:CFAP20DC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVT6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||Protein CFAP20DC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317180|||http://purl.uniprot.org/annotation/VAR_056772|||http://purl.uniprot.org/annotation/VAR_056773|||http://purl.uniprot.org/annotation/VAR_061575|||http://purl.uniprot.org/annotation/VAR_061576|||http://purl.uniprot.org/annotation/VSP_030913
http://togogenome.org/gene/9606:TMEM218                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU14                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In JBTS39.|||In JBTS39; fails to rescue the ciliopathy phenotype in a zebrafish disease model.|||In JBTS39; unknown pathological significance.|||Probable disease-associated variant found in patients with Meckel syndrome.|||Transmembrane protein 218                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321836|||http://purl.uniprot.org/annotation/VAR_086385|||http://purl.uniprot.org/annotation/VAR_086386|||http://purl.uniprot.org/annotation/VAR_086387|||http://purl.uniprot.org/annotation/VAR_086388|||http://purl.uniprot.org/annotation/VAR_086402
http://togogenome.org/gene/9606:DMRTC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Doublesex- and mab-3-related transcription factor C1|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244102|||http://purl.uniprot.org/annotation/VSP_019519
http://togogenome.org/gene/9606:ACAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWD1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acetyl-CoA acetyltransferase, cytosolic|||Acyl-thioester intermediate|||In isoform 2.|||Increases nucleophilicity of active site Cys|||N-acetylmethionine|||N6-acetyllysine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206409|||http://purl.uniprot.org/annotation/VAR_019686|||http://purl.uniprot.org/annotation/VSP_056217
http://togogenome.org/gene/9606:HES2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y543                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Orange|||Pro residues|||Transcription factor HES-2|||WRPW motif|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127206|||http://purl.uniprot.org/annotation/VAR_061256|||http://purl.uniprot.org/annotation/VSP_002104
http://togogenome.org/gene/9606:EPHX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07099|||http://purl.uniprot.org/uniprot/R4SBI6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Cytoplasmic|||Dimethylated arginine|||Either a rare variant or a sequencing error.|||Epoxide hydrolase 1|||Helical; Signal-anchor for type III membrane protein|||In allele EPHX1*1G.|||In allele EPHX1*2.|||In allele EPHX1*3; benign variant; frequent in the human population; 55% of wild type enzyme activity.|||In allele EPHX1*4; benign variant; frequent in the human population; 62% of wild type enzyme activity.|||In allele EPHX1*5.|||Nucleophile|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080855|||http://purl.uniprot.org/annotation/VAR_005295|||http://purl.uniprot.org/annotation/VAR_005296|||http://purl.uniprot.org/annotation/VAR_005297|||http://purl.uniprot.org/annotation/VAR_013298|||http://purl.uniprot.org/annotation/VAR_013299|||http://purl.uniprot.org/annotation/VAR_013300|||http://purl.uniprot.org/annotation/VAR_018347|||http://purl.uniprot.org/annotation/VAR_023303|||http://purl.uniprot.org/annotation/VAR_023304|||http://purl.uniprot.org/annotation/VAR_023305|||http://purl.uniprot.org/annotation/VAR_023306|||http://purl.uniprot.org/annotation/VAR_051828
http://togogenome.org/gene/9606:MGP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08493                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  4-carboxyglutamate|||Gla|||In isoform 2.|||Matrix Gla protein|||Phosphoserine|||Removed in mature form; probably by carboxypeptidase N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011109|||http://purl.uniprot.org/annotation/PRO_0000011110|||http://purl.uniprot.org/annotation/VAR_016177|||http://purl.uniprot.org/annotation/VAR_016178|||http://purl.uniprot.org/annotation/VSP_046999
http://togogenome.org/gene/9606:TENT4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDF8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic, involved in binding of the RNA primer|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||PAP-associated|||Phosphoserine|||Polar residues|||Terminal nucleotidyltransferase 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120310|||http://purl.uniprot.org/annotation/VSP_012732|||http://purl.uniprot.org/annotation/VSP_012733|||http://purl.uniprot.org/annotation/VSP_012734|||http://purl.uniprot.org/annotation/VSP_012735|||http://purl.uniprot.org/annotation/VSP_012736|||http://purl.uniprot.org/annotation/VSP_012737|||http://purl.uniprot.org/annotation/VSP_046989|||http://purl.uniprot.org/annotation/VSP_046990
http://togogenome.org/gene/9606:RHOG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P84095|||http://purl.uniprot.org/uniprot/Q6ICQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate|||(Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdB; alternate|||ADP-ribosylasparagine; by botulinum toxin|||Cysteine methyl ester|||Effector region|||Found in a patient with hemophagocytic lymphohistiocytosis; probable disease-associated variant; reduced protein stability.|||Phosphothreonine|||Removed in mature form|||Rho-related GTP-binding protein RhoG|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042028|||http://purl.uniprot.org/annotation/PRO_0000042029|||http://purl.uniprot.org/annotation/VAR_088337
http://togogenome.org/gene/9606:NPFFR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZQ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Neuropeptide FF receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069913|||http://purl.uniprot.org/annotation/VAR_059327
http://togogenome.org/gene/9606:GOT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK69|||http://purl.uniprot.org/uniprot/P17174                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminotransferase class I/classII|||Aspartate aminotransferase, cytoplasmic|||In isoform 2.|||N6-(pyridoxal phosphate)lysine|||Phosphoserine|||Removed|||Results in markedly diminished enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123879|||http://purl.uniprot.org/annotation/VAR_067256|||http://purl.uniprot.org/annotation/VSP_055799
http://togogenome.org/gene/9606:TRIP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15642|||http://purl.uniprot.org/uniprot/W4VSQ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abrogates interaction with CDC42.|||Basic and acidic residues|||Cdc42-interacting protein 4|||Disordered|||F-BAR|||Impairs interaction with CDC42.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2|||Interaction with CDC42|||Interaction with DNM1 and WASL|||Interaction with DNM2 and WASL|||Interaction with PDE6G|||Interaction with WAS|||Mediates end-to-end attachment of dimers|||Phosphoserine|||Pro residues|||REM-1|||Required for interaction with FASLG and localization to lysosomes|||Required for podosome formation|||Required for podosome formation and interaction with AKAP9 and microtubules|||Required for translocation to the plasma membrane in response to insulin|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089766|||http://purl.uniprot.org/annotation/VSP_021716|||http://purl.uniprot.org/annotation/VSP_021717|||http://purl.uniprot.org/annotation/VSP_021718|||http://purl.uniprot.org/annotation/VSP_021719|||http://purl.uniprot.org/annotation/VSP_021720|||http://purl.uniprot.org/annotation/VSP_021721
http://togogenome.org/gene/9606:ARMC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH27|||http://purl.uniprot.org/uniprot/B4DIU9|||http://purl.uniprot.org/uniprot/J3KQ26|||http://purl.uniprot.org/uniprot/Q96C12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||Armadillo repeat-containing protein 5|||BTB|||Disordered|||In AIMAH2.|||In AIMAH2; loss of function in promoting apoptosis.|||In AIMAH2; loss of function in promoting apoptosis; unknown pathological significance.|||In AIMAH2; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284405|||http://purl.uniprot.org/annotation/VAR_050674|||http://purl.uniprot.org/annotation/VAR_072352|||http://purl.uniprot.org/annotation/VAR_072353|||http://purl.uniprot.org/annotation/VAR_072354|||http://purl.uniprot.org/annotation/VAR_072355|||http://purl.uniprot.org/annotation/VAR_072356|||http://purl.uniprot.org/annotation/VAR_072357|||http://purl.uniprot.org/annotation/VAR_072358|||http://purl.uniprot.org/annotation/VAR_072359|||http://purl.uniprot.org/annotation/VAR_072360|||http://purl.uniprot.org/annotation/VAR_079096|||http://purl.uniprot.org/annotation/VAR_079097|||http://purl.uniprot.org/annotation/VAR_079098|||http://purl.uniprot.org/annotation/VAR_079099|||http://purl.uniprot.org/annotation/VAR_079100|||http://purl.uniprot.org/annotation/VAR_079101|||http://purl.uniprot.org/annotation/VAR_079102|||http://purl.uniprot.org/annotation/VAR_079103|||http://purl.uniprot.org/annotation/VAR_079104|||http://purl.uniprot.org/annotation/VAR_079105|||http://purl.uniprot.org/annotation/VAR_079106|||http://purl.uniprot.org/annotation/VAR_079107|||http://purl.uniprot.org/annotation/VAR_079108|||http://purl.uniprot.org/annotation/VAR_079109|||http://purl.uniprot.org/annotation/VAR_079110|||http://purl.uniprot.org/annotation/VAR_079111|||http://purl.uniprot.org/annotation/VAR_079112|||http://purl.uniprot.org/annotation/VAR_079113|||http://purl.uniprot.org/annotation/VAR_079114|||http://purl.uniprot.org/annotation/VAR_079115|||http://purl.uniprot.org/annotation/VAR_079116|||http://purl.uniprot.org/annotation/VAR_079117|||http://purl.uniprot.org/annotation/VAR_079118|||http://purl.uniprot.org/annotation/VAR_079119|||http://purl.uniprot.org/annotation/VAR_079120|||http://purl.uniprot.org/annotation/VAR_079121|||http://purl.uniprot.org/annotation/VAR_079122|||http://purl.uniprot.org/annotation/VAR_079123|||http://purl.uniprot.org/annotation/VAR_079124|||http://purl.uniprot.org/annotation/VAR_079125|||http://purl.uniprot.org/annotation/VAR_079126|||http://purl.uniprot.org/annotation/VAR_079127|||http://purl.uniprot.org/annotation/VAR_079128|||http://purl.uniprot.org/annotation/VAR_079129|||http://purl.uniprot.org/annotation/VSP_024505|||http://purl.uniprot.org/annotation/VSP_024506|||http://purl.uniprot.org/annotation/VSP_024507|||http://purl.uniprot.org/annotation/VSP_024508
http://togogenome.org/gene/9606:SFI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K8P3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||In isoform 10.|||In isoform 2 and isoform 9.|||In isoform 3, isoform 4 and isoform 10.|||In isoform 4.|||In isoform 5 and isoform 9.|||In isoform 5.|||Interaction with CETN2|||Protein SFI1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334621|||http://purl.uniprot.org/annotation/VAR_043439|||http://purl.uniprot.org/annotation/VAR_043440|||http://purl.uniprot.org/annotation/VAR_043441|||http://purl.uniprot.org/annotation/VAR_043442|||http://purl.uniprot.org/annotation/VAR_043443|||http://purl.uniprot.org/annotation/VAR_043444|||http://purl.uniprot.org/annotation/VAR_043445|||http://purl.uniprot.org/annotation/VAR_062234|||http://purl.uniprot.org/annotation/VSP_033699|||http://purl.uniprot.org/annotation/VSP_033700|||http://purl.uniprot.org/annotation/VSP_033701|||http://purl.uniprot.org/annotation/VSP_033702|||http://purl.uniprot.org/annotation/VSP_033703|||http://purl.uniprot.org/annotation/VSP_033708|||http://purl.uniprot.org/annotation/VSP_038325
http://togogenome.org/gene/9606:PEG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q96|||http://purl.uniprot.org/uniprot/Q9GZU2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||2-1|||2-2|||2-3|||3 X 7 AA repeat of P-E-V-E-A-A-E|||4 X 5 AA repeat of P-X-G-E-A|||Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Paternally-expressed gene 3 protein|||SCAN box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249228|||http://purl.uniprot.org/annotation/VAR_027397|||http://purl.uniprot.org/annotation/VAR_027398|||http://purl.uniprot.org/annotation/VAR_027399|||http://purl.uniprot.org/annotation/VAR_027400|||http://purl.uniprot.org/annotation/VAR_035562|||http://purl.uniprot.org/annotation/VAR_052725|||http://purl.uniprot.org/annotation/VAR_052726|||http://purl.uniprot.org/annotation/VAR_052727|||http://purl.uniprot.org/annotation/VAR_052728|||http://purl.uniprot.org/annotation/VSP_020371|||http://purl.uniprot.org/annotation/VSP_020372|||http://purl.uniprot.org/annotation/VSP_020373|||http://purl.uniprot.org/annotation/VSP_020374|||http://purl.uniprot.org/annotation/VSP_045527|||http://purl.uniprot.org/annotation/VSP_045528
http://togogenome.org/gene/9606:NLRP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTR0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||NACHT|||NACHT, LRR and PYD domains-containing protein 9|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286334|||http://purl.uniprot.org/annotation/VAR_036386|||http://purl.uniprot.org/annotation/VSP_025021
http://togogenome.org/gene/9606:PPIP5K2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZV0|||http://purl.uniprot.org/uniprot/A0A8V8TMN4|||http://purl.uniprot.org/uniprot/B4DGV1|||http://purl.uniprot.org/uniprot/O43314                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In DFNB100; Impaired diphosphoinositol-pentakisphosphate kinase activity.|||In isoform 2.|||Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2|||Loss of enzyme activity.|||Phosphoserine|||Polar residues|||Polyphosphoinositide-binding domain|||Reduces enzyme activity by about 99%.|||VIP1 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315692|||http://purl.uniprot.org/annotation/VAR_038276|||http://purl.uniprot.org/annotation/VAR_038277|||http://purl.uniprot.org/annotation/VAR_038278|||http://purl.uniprot.org/annotation/VAR_038279|||http://purl.uniprot.org/annotation/VAR_038280|||http://purl.uniprot.org/annotation/VAR_082201|||http://purl.uniprot.org/annotation/VSP_030636
http://togogenome.org/gene/9606:SCAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7N4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Necessary for interaction with the CTD domain of POLR2A|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Splicing factor, arginine/serine-rich 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299406|||http://purl.uniprot.org/annotation/VAR_052235|||http://purl.uniprot.org/annotation/VAR_052236
http://togogenome.org/gene/9606:TMEM11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17152                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 11, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072562
http://togogenome.org/gene/9606:DEFB132                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7B7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 132|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007007
http://togogenome.org/gene/9606:DTX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9I9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Pro residues|||Probable E3 ubiquitin-protein ligase DTX3|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219085|||http://purl.uniprot.org/annotation/VSP_008354
http://togogenome.org/gene/9606:ZNF143                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52747                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphothreonine|||Zinc finger protein 143                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047426|||http://purl.uniprot.org/annotation/VAR_027254|||http://purl.uniprot.org/annotation/VAR_061937|||http://purl.uniprot.org/annotation/VSP_036978|||http://purl.uniprot.org/annotation/VSP_055109
http://togogenome.org/gene/9606:C16orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PH81                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||UPF0547 protein C16orf87                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326521|||http://purl.uniprot.org/annotation/VSP_032670
http://togogenome.org/gene/9606:PRKG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13976                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Acidic residues|||Autoinhibitory domain|||Disordered|||In AAT8; impairs cGMP binding; the mutant protein is constitutively active.|||In isoform 3.|||In isoform Beta.|||Interchain|||Leucine-zipper|||Loss of binding to PPP1R12A.|||N-acetylserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor|||Reduces cGMP binding affinity.|||Removed|||Required for dimerization|||cGMP-binding, high affinity|||cGMP-binding, low affinity|||cGMP-dependent protein kinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086115|||http://purl.uniprot.org/annotation/VAR_046773|||http://purl.uniprot.org/annotation/VAR_051632|||http://purl.uniprot.org/annotation/VAR_070434|||http://purl.uniprot.org/annotation/VAR_070435|||http://purl.uniprot.org/annotation/VAR_070436|||http://purl.uniprot.org/annotation/VSP_038714|||http://purl.uniprot.org/annotation/VSP_055541|||http://purl.uniprot.org/annotation/VSP_055542
http://togogenome.org/gene/9606:FAXC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TGI0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Failed axon connections homolog|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089556|||http://purl.uniprot.org/annotation/VSP_056994
http://togogenome.org/gene/9606:CDKN2AIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTW3|||http://purl.uniprot.org/uniprot/J3KNE1|||http://purl.uniprot.org/uniprot/Q9NXV6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||CDKN2A-interacting protein|||DRBM|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||XRN2-binding (XTBD)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324339
http://togogenome.org/gene/9606:ZFP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN57                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein ZFP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291967|||http://purl.uniprot.org/annotation/VAR_032904|||http://purl.uniprot.org/annotation/VAR_032905
http://togogenome.org/gene/9606:GLRX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDT9|||http://purl.uniprot.org/uniprot/Q86SX6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Glutaredoxin|||Glutaredoxin-related protein 5, mitochondrial|||In SIDBA3; deficiency in Fe-S cluster synthesis; does not impair ISCU binding.|||In SPAHGC; no effect on protein abundance in patient cells; probably reduced activity in iron-sulfur cluster assembly that results in reduced production of the lipoate cofactor and protein lipoylation.|||Mitochondrion|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141650|||http://purl.uniprot.org/annotation/VAR_026125|||http://purl.uniprot.org/annotation/VAR_074550|||http://purl.uniprot.org/annotation/VAR_074551|||http://purl.uniprot.org/annotation/VAR_076672
http://togogenome.org/gene/9606:NSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O96028                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AWS|||Basic and acidic residues|||Disordered|||HMG box|||Histone-lysine N-methyltransferase NSD2|||In RAUST.|||In RAUST; decreased histone methyltransferase activity H3-K36 specific.|||In RAUST; not changed histone methyltransferase activity H3-K36 specific.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1092 or G-1142.|||Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179.|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4; atypical|||PWWP 1|||PWWP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Post-SET|||Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179.|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259519|||http://purl.uniprot.org/annotation/VAR_086787|||http://purl.uniprot.org/annotation/VAR_086788|||http://purl.uniprot.org/annotation/VAR_086789|||http://purl.uniprot.org/annotation/VAR_086790|||http://purl.uniprot.org/annotation/VAR_086791|||http://purl.uniprot.org/annotation/VAR_086792|||http://purl.uniprot.org/annotation/VAR_086793|||http://purl.uniprot.org/annotation/VAR_086794|||http://purl.uniprot.org/annotation/VAR_086795|||http://purl.uniprot.org/annotation/VAR_086796|||http://purl.uniprot.org/annotation/VSP_021413|||http://purl.uniprot.org/annotation/VSP_021414|||http://purl.uniprot.org/annotation/VSP_021415|||http://purl.uniprot.org/annotation/VSP_021416|||http://purl.uniprot.org/annotation/VSP_021417|||http://purl.uniprot.org/annotation/VSP_021418|||http://purl.uniprot.org/annotation/VSP_021419|||http://purl.uniprot.org/annotation/VSP_021420|||http://purl.uniprot.org/annotation/VSP_021421|||http://purl.uniprot.org/annotation/VSP_021422|||http://purl.uniprot.org/annotation/VSP_021423
http://togogenome.org/gene/9606:GNAI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08754                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||Deamidated glutamine; by Photorhabdus PAU_02230|||Decreased affinity for CCDC88C and PLCD4.|||Decreased affinity for PLCD4.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(i) subunit alpha-3|||In ARCND1.|||Increased affinity for PLCD4.|||Increased affinity for PLCD4. No effect on binding to CCDC88C.|||N-myristoyl glycine|||No effect on binding to CCDC88C.|||No effect on binding to PLCD4.|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203692|||http://purl.uniprot.org/annotation/VAR_068558
http://togogenome.org/gene/9606:SLC25A35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KQZ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291794|||http://purl.uniprot.org/annotation/VSP_026237|||http://purl.uniprot.org/annotation/VSP_026238|||http://purl.uniprot.org/annotation/VSP_026239
http://togogenome.org/gene/9606:KCNAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z435|||http://purl.uniprot.org/uniprot/B7Z8E5|||http://purl.uniprot.org/uniprot/F8W6W4|||http://purl.uniprot.org/uniprot/Q14722|||http://purl.uniprot.org/uniprot/Q5MJQ3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform KvB1.1.|||In isoform KvB1.2.|||NADP-dependent oxidoreductase|||Nearly abolishes NADPH binding.|||Polar residues|||Proton donor/acceptor|||Reduces affinity for NADPH.|||Voltage-gated potassium channel subunit beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148739|||http://purl.uniprot.org/annotation/VSP_001050|||http://purl.uniprot.org/annotation/VSP_001051
http://togogenome.org/gene/9606:CEBPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17676                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  9aaTAD|||Asymmetric dimethylarginine; by CARM1|||Basic motif|||CCAAT/enhancer-binding protein beta|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||Leucine-zipper|||Loss of nuclear translocation.|||Loss of transactivation activity in response to IFNG.|||N6-acetyllysine; alternate|||N6-acetyllysine; by KAT2A and KAT2B|||N6-acetyllysine; by KAT2A and KAT2B; alternate|||N6-methylated lysine; alternate|||O-linked (GlcNAc) serine|||Phosphoserine; by CaMK2|||Phosphoserine; by GSK3-beta|||Phosphoserine; by PKC/PRKCA|||Phosphothreonine; by GSK3-beta|||Phosphothreonine; by RPS6KA1 and PKC/PRKCA|||Phosphothreonine; by RPS6KA1, CDK2 and MAPK|||Polar residues|||Pro residues|||Required for Lys-174 sumoylation|||Required for MYC transcriptional repression|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076617|||http://purl.uniprot.org/annotation/VAR_016300|||http://purl.uniprot.org/annotation/VSP_053313|||http://purl.uniprot.org/annotation/VSP_053314
http://togogenome.org/gene/9606:TMEM100                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV29                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Transmembrane protein 100                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240846
http://togogenome.org/gene/9606:AASS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0W4|||http://purl.uniprot.org/uniprot/Q9UDR5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Alanine dehydrogenase/pyridine nucleotide transhydrogenase N-terminal|||Alanine dehydrogenase/pyridine nucleotide transhydrogenase NAD(H)-binding|||Alpha-aminoadipic semialdehyde synthase, mitochondrial|||Lysine-ketoglutarate reductase|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Saccharopine dehydrogenase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001052
http://togogenome.org/gene/9606:RPP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8H3|||http://purl.uniprot.org/uniprot/Q9H633                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Polar residues|||Removed|||Ribonuclease P protein subunit p21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153845|||http://purl.uniprot.org/annotation/VAR_019116|||http://purl.uniprot.org/annotation/VAR_045986|||http://purl.uniprot.org/annotation/VSP_010695|||http://purl.uniprot.org/annotation/VSP_010696|||http://purl.uniprot.org/annotation/VSP_044901
http://togogenome.org/gene/9606:ANKRD46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KT99|||http://purl.uniprot.org/uniprot/Q86W74                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 46|||Helical|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244577|||http://purl.uniprot.org/annotation/VSP_060673
http://togogenome.org/gene/9606:MTPAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVV4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In SPAX4.|||In isoform 2.|||Loss of enzyme activity.|||Mitochondrion|||N6-acetyllysine|||No effect on dimerization. Loss of dimerization and of enzyme activity; when associated with 294-AAAA-297.|||PAP-associated|||Poly(A) RNA polymerase, mitochondrial|||Reduced dimerization. Loss of dimerization and of enzyme activity; when associated with 259-AAA-261.|||Reduced enzyme activity.|||Reduces dimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250689|||http://purl.uniprot.org/annotation/VAR_027601|||http://purl.uniprot.org/annotation/VAR_027602|||http://purl.uniprot.org/annotation/VAR_027603|||http://purl.uniprot.org/annotation/VAR_027604|||http://purl.uniprot.org/annotation/VAR_064907|||http://purl.uniprot.org/annotation/VSP_020724
http://togogenome.org/gene/9606:GUCA1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95843                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Deamidated asparagine|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Guanylyl cyclase-activating protein 3|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073812|||http://purl.uniprot.org/annotation/VAR_055632|||http://purl.uniprot.org/annotation/VAR_055633|||http://purl.uniprot.org/annotation/VAR_055634|||http://purl.uniprot.org/annotation/VAR_055635|||http://purl.uniprot.org/annotation/VSP_000736
http://togogenome.org/gene/9606:CSF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04141                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Granulocyte-macrophage colony-stimulating factor|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005865|||http://purl.uniprot.org/annotation/VAR_001975|||http://purl.uniprot.org/annotation/VAR_013089
http://togogenome.org/gene/9606:UBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBT2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATP-dependent activation of SUMO proteins.|||Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl thioester intermediate|||In ACCES.|||In ACCES; loss of function; does not rescue the abnormal phenotype in a zebrafish disease model.|||In isoform 2.|||Loss of enzyme activity.|||N6-acetyllysine; alternate|||No effect on enzyme activity.|||Phosphoserine|||Polar residues|||SUMO-activating enzyme subunit 2|||Slightly reduced enzyme activity.|||Strongly reduced interaction with UBE2I.|||Strongly reduced interaction with UBE2I; when associated with A-235.|||Strongly reduced interaction with UBE2I; when associated with A-238.|||Strongly reduces ATP-dependent activation of SUMO proteins.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194968|||http://purl.uniprot.org/annotation/VAR_017689|||http://purl.uniprot.org/annotation/VAR_087611|||http://purl.uniprot.org/annotation/VAR_087612|||http://purl.uniprot.org/annotation/VAR_087613|||http://purl.uniprot.org/annotation/VAR_087614|||http://purl.uniprot.org/annotation/VAR_087615|||http://purl.uniprot.org/annotation/VAR_087616|||http://purl.uniprot.org/annotation/VSP_056164
http://togogenome.org/gene/9606:COPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53621                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Peptide|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coatomer subunit alpha|||In AILJK.|||In AILJK; causes a defect in retrograde transport from the Golgi to the endoplasmic reticulum.|||In RNA edited version.|||In isoform 2.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Proxenin|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||Xenin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041400|||http://purl.uniprot.org/annotation/PRO_0000041401|||http://purl.uniprot.org/annotation/PRO_0000223307|||http://purl.uniprot.org/annotation/VAR_033803|||http://purl.uniprot.org/annotation/VAR_066525|||http://purl.uniprot.org/annotation/VAR_073844|||http://purl.uniprot.org/annotation/VAR_073845|||http://purl.uniprot.org/annotation/VAR_073846|||http://purl.uniprot.org/annotation/VAR_073847|||http://purl.uniprot.org/annotation/VSP_035043
http://togogenome.org/gene/9606:AQP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZHR4|||http://purl.uniprot.org/uniprot/F1DSG4|||http://purl.uniprot.org/uniprot/P55087|||http://purl.uniprot.org/uniprot/V9PBN7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Aquaporin-4|||Cytoplasmic|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||In isoform 1.|||N-linked (GlcNAc...) asparagine|||NPA 1|||NPA 2|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by PKG|||Phosphothreonine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063948|||http://purl.uniprot.org/annotation/VSP_003232
http://togogenome.org/gene/9606:LEFTY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00292                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In LRAM.|||In isoform 2.|||Left-right determination factor 2|||N-linked (GlcNAc...) asparagine|||Or 135                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033806|||http://purl.uniprot.org/annotation/PRO_0000033807|||http://purl.uniprot.org/annotation/VAR_010385|||http://purl.uniprot.org/annotation/VAR_021980|||http://purl.uniprot.org/annotation/VAR_021981|||http://purl.uniprot.org/annotation/VSP_045264
http://togogenome.org/gene/9606:GCSAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6F7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Does not affect IL6 induced phosphorylation. Does not affect the interaction with SYK.|||Does not affect the interaction with SYK.|||Germinal center-associated signaling and motility protein|||In isoform 2.|||In isoform 3.|||Loss of FBXO10-mediated ubiquitination and degradation.|||Phosphoserine|||Phosphotyrosine|||Prevents IL6 induced phosphorylation. Does not affect the interaction with SYK.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256228|||http://purl.uniprot.org/annotation/VSP_046085|||http://purl.uniprot.org/annotation/VSP_046984
http://togogenome.org/gene/9606:PTPRR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15256|||http://purl.uniprot.org/uniprot/Q7Z2V8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 4.|||In isoform Delta.|||In isoform Gamma.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by PKA|||Receptor-type tyrosine-protein phosphatase R|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025459|||http://purl.uniprot.org/annotation/VAR_014283|||http://purl.uniprot.org/annotation/VAR_057140|||http://purl.uniprot.org/annotation/VAR_057141|||http://purl.uniprot.org/annotation/VAR_057142|||http://purl.uniprot.org/annotation/VSP_005155|||http://purl.uniprot.org/annotation/VSP_005156|||http://purl.uniprot.org/annotation/VSP_005158|||http://purl.uniprot.org/annotation/VSP_046352|||http://purl.uniprot.org/annotation/VSP_046353
http://togogenome.org/gene/9606:ACTR5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9F9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-related protein 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247842|||http://purl.uniprot.org/annotation/VAR_027158|||http://purl.uniprot.org/annotation/VAR_027159|||http://purl.uniprot.org/annotation/VAR_027160|||http://purl.uniprot.org/annotation/VAR_048189
http://togogenome.org/gene/9606:INHBC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55103                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Inhibin beta C chain|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033730|||http://purl.uniprot.org/annotation/PRO_0000033731|||http://purl.uniprot.org/annotation/VAR_024230
http://togogenome.org/gene/9606:SLC24A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71RS6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with SHEP4; greatly reduced exchange activity.|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||Sodium/potassium/calcium exchanger 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045753|||http://purl.uniprot.org/annotation/VAR_024922|||http://purl.uniprot.org/annotation/VSP_047596
http://togogenome.org/gene/9606:SGTA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43765                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Reduces tail-anchored proteins transfer.|||Small glutamine-rich tetratricopeptide repeat-containing protein alpha|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106365
http://togogenome.org/gene/9606:PLA2G15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCC3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phospholipase and transacylase activity. Abolishes association with membranes.|||Acyl-ester intermediate|||Charge relay system|||Decreases membrane binding, phospholipase and transacylase activity at acidic pH.|||Has no effect on membrane binding or transacylase activity at acidic pH. Increases membrane binding and transacylase activity at neutral pH by 2-fold and 8-fold, respectively.|||In isoform 2.|||Loss of glycosylation site. Leads to retention in the endoplasmic reticulum and nearly abolishes the production of the mature, active enzyme.|||Loss of glycosylation site. Mildly reduces production of the mature, active enzyme.|||Loss of glycosylation site. Slightly reduces production of the mature, active enzyme.|||N-linked (GlcNAc...) asparagine|||No effect on phospholipase activity. Abolishes transacylase activity. Has no effect on association with membranes.|||No effect on phospholipase activity. Strongly decreases transacylase activity and abolishes association with membranes.|||No effect on phospholipase activity. Strongly decreases transacylase activity and association with membranes.|||Phospholipase A2 group XV                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017808|||http://purl.uniprot.org/annotation/VSP_056689|||http://purl.uniprot.org/annotation/VSP_056690
http://togogenome.org/gene/9606:SRPX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60687                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  HYR|||In RESDX; unknown pathological significance; affects intracellular processing; increases the interaction with PLAUR.|||In RESDX; unknown pathological significance; results in a gain of glycosylation; affects intracellular processing; does not affect interaction with PLAUR.|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi repeat-containing protein SRPX2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274525|||http://purl.uniprot.org/annotation/VAR_030312|||http://purl.uniprot.org/annotation/VAR_030313|||http://purl.uniprot.org/annotation/VAR_030314
http://togogenome.org/gene/9606:SPATA31E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZUB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||Spermatogenesis-associated protein 31E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089716|||http://purl.uniprot.org/annotation/VAR_022858|||http://purl.uniprot.org/annotation/VAR_022859|||http://purl.uniprot.org/annotation/VAR_022860|||http://purl.uniprot.org/annotation/VAR_022861|||http://purl.uniprot.org/annotation/VAR_022862|||http://purl.uniprot.org/annotation/VAR_053943|||http://purl.uniprot.org/annotation/VAR_053944|||http://purl.uniprot.org/annotation/VAR_053945|||http://purl.uniprot.org/annotation/VAR_053946|||http://purl.uniprot.org/annotation/VAR_053947|||http://purl.uniprot.org/annotation/VAR_053948|||http://purl.uniprot.org/annotation/VAR_053949|||http://purl.uniprot.org/annotation/VAR_062203
http://togogenome.org/gene/9606:CIMAP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PU9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Ciliary microtubule associated protein 1A|||Disordered|||In isoform 2.|||In isoform 3.|||STPGR 1|||STPGR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299464|||http://purl.uniprot.org/annotation/VSP_027686|||http://purl.uniprot.org/annotation/VSP_027687|||http://purl.uniprot.org/annotation/VSP_054893
http://togogenome.org/gene/9606:TNNI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48788                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DA2B1.|||In isoform 2.|||Involved in binding TNC|||Involved in binding TNC and actin|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Removed|||Troponin I, fast skeletal muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186143|||http://purl.uniprot.org/annotation/VAR_016087|||http://purl.uniprot.org/annotation/VSP_046052
http://togogenome.org/gene/9606:RPS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62277                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphotyrosine|||Removed|||Small ribosomal subunit protein uS15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115661
http://togogenome.org/gene/9606:ELMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1X5|||http://purl.uniprot.org/uniprot/Q92556                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ELMO|||Engulfment and cell motility protein 1|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||PH|||Phosphoserine|||Phosphotyrosine; by HCK|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153712|||http://purl.uniprot.org/annotation/VAR_065824|||http://purl.uniprot.org/annotation/VSP_007480|||http://purl.uniprot.org/annotation/VSP_038550|||http://purl.uniprot.org/annotation/VSP_038551
http://togogenome.org/gene/9606:CAMKV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKD5|||http://purl.uniprot.org/uniprot/Q8NCB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CaM kinase-like vesicle-associated protein|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphothreonine|||Polar residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250094|||http://purl.uniprot.org/annotation/VAR_027539|||http://purl.uniprot.org/annotation/VAR_041337|||http://purl.uniprot.org/annotation/VAR_041338|||http://purl.uniprot.org/annotation/VAR_041339|||http://purl.uniprot.org/annotation/VAR_041340|||http://purl.uniprot.org/annotation/VAR_041341|||http://purl.uniprot.org/annotation/VSP_020600|||http://purl.uniprot.org/annotation/VSP_020601
http://togogenome.org/gene/9606:MAP3K5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TMH5|||http://purl.uniprot.org/uniprot/Q99683                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; by PRMT1|||Basic and acidic residues|||Disordered|||Does not affect interaction with TRIM48.|||Enhanced induction of apoptosis and increased kinase activity.|||Enhanced induction of apoptosis, increased kinase activity, and loss of YWHAG binding.|||In isoform 2.|||Interaction with PPIA/CYPA|||Loss of kinase activity. Abolishes DAXX-mediated apoptosis. Loss of RC3H2-mediated ubiquitination.|||Loss of kinase activity. Inhibits activation of JNK and apoptosis mediated by TNFRSF6 and DAXX. Does not affect interaction with TRIM48.|||Mitogen-activated protein kinase kinase kinase 5|||No effect on methylation by PRMT1.|||Phosphoserine|||Phosphoserine; by PIM1 and PKB/AKT1|||Phosphoserine; by autocatalysis|||Phosphothreonine; by autocatalysis|||Phosphothreonine; by autocatalysis, MELK and MAP3K6|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Reduced methylation by PRMT1. Abolishes methylation by PRMT1 and PRMT1-mediated inhibition of MAPK35 activation; when associated with K-78.|||Reduced methylation by PRMT1. Abolishes methylation by PRMT1 and PRMT1-mediated inhibition of MAPK35 activation; when associated with K-80.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086249|||http://purl.uniprot.org/annotation/VAR_040693|||http://purl.uniprot.org/annotation/VAR_040694|||http://purl.uniprot.org/annotation/VAR_040695|||http://purl.uniprot.org/annotation/VAR_040696|||http://purl.uniprot.org/annotation/VAR_040697|||http://purl.uniprot.org/annotation/VSP_056182
http://togogenome.org/gene/9606:LRRC57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9N7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||Leucine-rich repeat-containing protein 57|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227778
http://togogenome.org/gene/9606:RTKN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BST9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Impairs interaction with TAX1BP3.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Polar residues|||REM-1|||Rhotekin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233940|||http://purl.uniprot.org/annotation/VSP_052004|||http://purl.uniprot.org/annotation/VSP_052005
http://togogenome.org/gene/9606:ALG14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F25                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In CMS15.|||In CMS15; results in a severe reduction in protein expression; loss of function mutation.|||In MEPCA.|||In MEPCA; unknown pathological significance.|||Lumenal|||UDP-N-acetylglucosamine transferase subunit ALG14 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265116|||http://purl.uniprot.org/annotation/VAR_029635|||http://purl.uniprot.org/annotation/VAR_073331|||http://purl.uniprot.org/annotation/VAR_084707|||http://purl.uniprot.org/annotation/VAR_084708|||http://purl.uniprot.org/annotation/VAR_084709|||http://purl.uniprot.org/annotation/VAR_084710
http://togogenome.org/gene/9606:GVQW3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U1RQW1|||http://purl.uniprot.org/uniprot/A0A590UK82|||http://purl.uniprot.org/uniprot/Q3ZCU0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Mos1 transposase HTH|||Protein GVQW3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320634|||http://purl.uniprot.org/annotation/VSP_031695|||http://purl.uniprot.org/annotation/VSP_031696
http://togogenome.org/gene/9606:DAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14118                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes LARGE1-dependent glycosylation, CHST10-dependent sulfation and consequent binding to laminin; when associated with 311-R--I-370 del.|||Abolishes LARGE1-dependent glycosylation, CHST10-dependent sulfation and consequent binding to laminin; when associated with A-379.|||Abolishes autoproteolysis and enhances laminin-binding.|||Abolishes nuclear translocation.|||Abolishes phosphorylation. Increase in nuclear location.|||Abolishes phosphorylation. No change in plasma membrane location.|||About 50% reduction in nuclear accumulation.|||Alpha-dystroglycan|||Basic and acidic residues|||Beta-dystroglycan|||Cleavage; by MMP9|||Cleavage; by autolysis|||Cytoplasmic|||Disordered|||Does not affect laminin-binding.|||Drastic reduction in nuclear accumulation.|||Extracellular|||Helical|||Impaired laminin-binding.|||In MDDGA9.|||In MDDGC9; does not affect dystroglycan expression; impairs alpha-dystroglycan glycosylation.|||In MDDGC9; no effect on dystroglycan expression; impairs alpha-dystroglycan glycosylation.|||In MDDGC9; results in impaired interaction with LARGE1 and incomplete DAG1 glycosylation.|||Moderate reduction in nuclear accumulation.|||Mucin-like domain|||N-linked (GlcNAc...) asparagine|||No change in nuclear location.|||Nuclear localization signal|||O-glycosylated at one site|||O-glycosylated at seven sites with GalNAc|||O-linked (GalNAc...) threonine|||O-linked (Hex...) threonine|||O-linked (Man6P...) threonine|||PPXY motif|||Peptidase S72|||Phosphothreonine|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||Redistributes to a vesicular internal membrane compartment.|||Reduced N-linked glycosylation. No change in nuclear translocation.|||Required for binding DMD and UTRN|||Required for interaction with CAV3|||Required for laminin recognition|||Retains the capacity to bind laminin.|||Significant reduction in nuclear accumulation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021065|||http://purl.uniprot.org/annotation/PRO_0000021066|||http://purl.uniprot.org/annotation/VAR_024335|||http://purl.uniprot.org/annotation/VAR_065266|||http://purl.uniprot.org/annotation/VAR_075809|||http://purl.uniprot.org/annotation/VAR_075810|||http://purl.uniprot.org/annotation/VAR_075811
http://togogenome.org/gene/9606:UTRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46939|||http://purl.uniprot.org/uniprot/Q6LBS5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In isoform 2.|||In isoform Up140.|||In isoform Up71.|||Interaction with SYNM|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Utrophin|||WW|||ZZ-type|||ZZ-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076082|||http://purl.uniprot.org/annotation/VAR_047794|||http://purl.uniprot.org/annotation/VAR_047795|||http://purl.uniprot.org/annotation/VAR_047796|||http://purl.uniprot.org/annotation/VAR_047797|||http://purl.uniprot.org/annotation/VSP_047925|||http://purl.uniprot.org/annotation/VSP_054942|||http://purl.uniprot.org/annotation/VSP_054943|||http://purl.uniprot.org/annotation/VSP_054944
http://togogenome.org/gene/9606:PCDHA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003884|||http://purl.uniprot.org/annotation/VAR_021872|||http://purl.uniprot.org/annotation/VAR_021873|||http://purl.uniprot.org/annotation/VAR_048521|||http://purl.uniprot.org/annotation/VAR_048522|||http://purl.uniprot.org/annotation/VSP_000670|||http://purl.uniprot.org/annotation/VSP_000671|||http://purl.uniprot.org/annotation/VSP_000672
http://togogenome.org/gene/9606:PRPF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43172|||http://purl.uniprot.org/uniprot/Q5T1M7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Decreases PRPF3 binding.|||Disordered|||In RP70.|||In RP70; does not affect nuclear speck localization; disrupts interaction with PRPF3; does not affect interaction with PPIH; does not integrated in spliceosomal snRNP complex.|||In isoform 2.|||N6-acetyllysine|||Polar residues|||Pre-mRNA processing factor 4 (PRP4)-like|||U4/U6 small nuclear ribonucleoprotein Prp4|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051149|||http://purl.uniprot.org/annotation/VAR_071872|||http://purl.uniprot.org/annotation/VAR_074029|||http://purl.uniprot.org/annotation/VSP_006785
http://togogenome.org/gene/9606:MYO18A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J771|||http://purl.uniprot.org/uniprot/Q92614|||http://purl.uniprot.org/uniprot/Q9NYE8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with actin.|||Acidic residues|||Basic and acidic residues|||Disordered|||IQ|||In isoform 2.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 5.|||Interaction with actin|||Mediates nucleotide-independent binding to F-actin and interaction with GOLPH3|||Myosin N-terminal SH3-like|||Myosin motor|||No effect on interaction with actin.|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RecA family profile 2|||Unconventional myosin-XVIIIa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123476|||http://purl.uniprot.org/annotation/VAR_030585|||http://purl.uniprot.org/annotation/VSP_007869|||http://purl.uniprot.org/annotation/VSP_007870|||http://purl.uniprot.org/annotation/VSP_007871|||http://purl.uniprot.org/annotation/VSP_007872|||http://purl.uniprot.org/annotation/VSP_023058
http://togogenome.org/gene/9606:IL25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H293                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interleukin-25|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015431|||http://purl.uniprot.org/annotation/VSP_010159
http://togogenome.org/gene/9606:VEGFC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49767                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Repeat|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-C|||Interchain|||N-linked (GlcNAc...) asparagine|||No proteolytic processing and lower effect on VEGFR-2 and VEGFR-3.|||Or 102|||Vascular endothelial growth factor C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023400|||http://purl.uniprot.org/annotation/PRO_0000023401|||http://purl.uniprot.org/annotation/PRO_0000023402
http://togogenome.org/gene/9606:WDTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5D0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5 and isoform 6.|||Phosphoserine|||TPR 1|||TPR 2|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD and tetratricopeptide repeats protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051434|||http://purl.uniprot.org/annotation/VSP_009290|||http://purl.uniprot.org/annotation/VSP_009291|||http://purl.uniprot.org/annotation/VSP_009292
http://togogenome.org/gene/9606:ATP4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51164                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Potassium-transporting ATPase subunit beta|||immunoglobulin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219091
http://togogenome.org/gene/9606:SMAD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R274|||http://purl.uniprot.org/uniprot/Q13485                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitination.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In JP/HHT and JPS.|||In JP/HHT.|||In JPS.|||In MYHRS.|||In MYHRS; there is an enhanced levels of SMAD4 protein with lower levels of ubiquitinated SMAD4 fibroblasts compared to controls suggesting stabilization of the mutant protein; 8-fold increase in phosphorylated SMAD2 and SMAD3; 11-fold increase in phosphorylated SMAD1, SMAD5 and SMAD8 in cell nuclei compared to controls.|||In a colorectal cancer sample; somatic mutation.|||In pancreatic carcinoma.|||MH1|||MH2|||Mediates interaction with ZBTB7A|||Mothers against decapentaplegic homolog 4|||N6-acetyllysine|||Necessary for heterotrimerization|||No effect on heterotrimerization. Greatly reduced transcriptional activation.|||No effect on heterotrimerization. Partially diminished transcriptional activation.|||Polar residues|||Rare variant; found in a patient with pulmonary hypertension; unknown pathological significance.|||Reduced heterotrimerization.|||Required for interaction with TSC22D1|||SAD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090861|||http://purl.uniprot.org/annotation/VAR_011380|||http://purl.uniprot.org/annotation/VAR_019571|||http://purl.uniprot.org/annotation/VAR_019572|||http://purl.uniprot.org/annotation/VAR_019573|||http://purl.uniprot.org/annotation/VAR_022833|||http://purl.uniprot.org/annotation/VAR_036475|||http://purl.uniprot.org/annotation/VAR_036476|||http://purl.uniprot.org/annotation/VAR_036477|||http://purl.uniprot.org/annotation/VAR_066870|||http://purl.uniprot.org/annotation/VAR_067602|||http://purl.uniprot.org/annotation/VAR_067603|||http://purl.uniprot.org/annotation/VAR_067604
http://togogenome.org/gene/9606:CIBAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1XBS5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-132 and E-134.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-132 and E-136.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-114; E-134 and E-136.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107; E-110; E-132; E-134 and E-136.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-107;E-114; E-132; E-134 and E-136.|||Abolishes ability to induce membrane remodeling in the presence of CBY1; when associated with E-110; E-114; E-132; E-134 and E-136.|||BAR-like|||CBY1-interacting BAR domain-containing protein 1|||Disordered|||In PAPA9; does not form homodimers; does not interact with CBY1; does not localize to cilium basal body.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mitochondrion|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-107 and A-109.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-107 and A-110.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-109 and A-110.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-132 and A-134.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-132 and A-136.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-134 and A-136.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-264 and A-266.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-264 and A-267.|||Reduced membrane-binding and significant reduction in membrane remodeling activity; when associated with A-266 and A-267.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287080|||http://purl.uniprot.org/annotation/VAR_062190|||http://purl.uniprot.org/annotation/VAR_081578|||http://purl.uniprot.org/annotation/VSP_025292|||http://purl.uniprot.org/annotation/VSP_025293|||http://purl.uniprot.org/annotation/VSP_025294|||http://purl.uniprot.org/annotation/VSP_025295|||http://purl.uniprot.org/annotation/VSP_025296
http://togogenome.org/gene/9606:STAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY15                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Extracellular|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||FAS1 5|||FAS1 6|||FAS1 7|||Helical|||In isoform 2.|||Laminin EGF-like 1|||Laminin EGF-like 2|||Link|||N-linked (GlcNAc...) asparagine|||Stabilin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007710|||http://purl.uniprot.org/annotation/VAR_019078|||http://purl.uniprot.org/annotation/VAR_055774|||http://purl.uniprot.org/annotation/VAR_055775|||http://purl.uniprot.org/annotation/VAR_060338|||http://purl.uniprot.org/annotation/VAR_060339|||http://purl.uniprot.org/annotation/VAR_060340|||http://purl.uniprot.org/annotation/VSP_050764|||http://purl.uniprot.org/annotation/VSP_050765
http://togogenome.org/gene/9606:BMP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95972                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Bone morphogenetic protein 15|||In ODG2; dominant-negative effect; may cause relevant modifications in the conformation of the precursor protein possibly leading to altered processing and impaired activation of latent forms or to abnormal dimerization.|||In POF4.|||In POF4; leads to marked reduction of mature protein production; does not generate a complete recovery of wild-type activity in granulosa cell line transfected with defective mutant and with equal amount of wild-type protein.|||In POF4; unknown pathological significance; no or minor deleterious effect detected.|||N-linked (GlcNAc...) asparagine|||No or minor deleterious effect detected.|||No or minor deleterious effect observed.|||O-linked (HexNAc...) threonine; in P17|||Phosphoserine; in P16|||Pyrrolidone carboxylic acid; in P16 and P17|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033892|||http://purl.uniprot.org/annotation/PRO_0000033893|||http://purl.uniprot.org/annotation/VAR_021195|||http://purl.uniprot.org/annotation/VAR_058974|||http://purl.uniprot.org/annotation/VAR_058975|||http://purl.uniprot.org/annotation/VAR_058976|||http://purl.uniprot.org/annotation/VAR_058977|||http://purl.uniprot.org/annotation/VAR_058978|||http://purl.uniprot.org/annotation/VAR_058979|||http://purl.uniprot.org/annotation/VAR_058980|||http://purl.uniprot.org/annotation/VAR_058981|||http://purl.uniprot.org/annotation/VAR_058982|||http://purl.uniprot.org/annotation/VAR_058983|||http://purl.uniprot.org/annotation/VAR_058984|||http://purl.uniprot.org/annotation/VAR_058985|||http://purl.uniprot.org/annotation/VAR_058986|||http://purl.uniprot.org/annotation/VAR_058987|||http://purl.uniprot.org/annotation/VAR_058988|||http://purl.uniprot.org/annotation/VAR_058989|||http://purl.uniprot.org/annotation/VAR_066932|||http://purl.uniprot.org/annotation/VAR_066933
http://togogenome.org/gene/9606:ZBTB8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BR9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 8A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000378508|||http://purl.uniprot.org/annotation/VAR_058085|||http://purl.uniprot.org/annotation/VSP_037597
http://togogenome.org/gene/9606:FNDC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z333                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Fibronectin type III domain-containing protein 10|||Fibronectin type-III|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416238
http://togogenome.org/gene/9606:KCNK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPC2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In BIBARS.|||In BIBARS; inactive.|||N-linked (GlcNAc...) asparagine|||Pore-forming; Name=Pore-forming 1|||Pore-forming; Name=Pore-forming 2|||Potassium channel subfamily K member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101754|||http://purl.uniprot.org/annotation/VAR_054373|||http://purl.uniprot.org/annotation/VAR_084510
http://togogenome.org/gene/9606:ELOVL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L3X0|||http://purl.uniprot.org/uniprot/D6RHD0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Di-lysine motif|||Elongation of very long chain fatty acids protein 7|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||HxxHH motif|||Loss of activity alone or when associated with A-151.|||Loss of activity; when associated with A-150.|||Lumenal|||N-acetylalanine|||Nucleophile|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311988
http://togogenome.org/gene/9606:ZNF568                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VDJ6|||http://purl.uniprot.org/uniprot/C9JLX5|||http://purl.uniprot.org/uniprot/Q3ZCX4|||http://purl.uniprot.org/uniprot/Q96AZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||KRAB|||Polar residues|||Zinc finger protein 568                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306877|||http://purl.uniprot.org/annotation/VAR_052867|||http://purl.uniprot.org/annotation/VAR_052868|||http://purl.uniprot.org/annotation/VSP_028556|||http://purl.uniprot.org/annotation/VSP_046815
http://togogenome.org/gene/9606:CAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40123|||http://purl.uniprot.org/uniprot/Q5JPJ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Adenylyl cyclase-associated protein 2|||C-CAP/cofactor C-like|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205700|||http://purl.uniprot.org/annotation/VAR_033717|||http://purl.uniprot.org/annotation/VAR_033718|||http://purl.uniprot.org/annotation/VSP_055519|||http://purl.uniprot.org/annotation/VSP_055520
http://togogenome.org/gene/9606:SYTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2 1|||C2 2|||Disordered|||FYVE-type|||In isoform 2.|||Phosphoserine|||Polar residues|||RabBD|||Synaptotagmin-like protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190219|||http://purl.uniprot.org/annotation/VAR_024601|||http://purl.uniprot.org/annotation/VAR_061753|||http://purl.uniprot.org/annotation/VSP_042659
http://togogenome.org/gene/9606:LYST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99698                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||Disordered|||In CHS.|||In CHS; loss of protein expression.|||In isoform 2.|||In isoform 3.|||Lysosomal-trafficking regulator|||Phosphoserine|||Phosphothreonine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051071|||http://purl.uniprot.org/annotation/VAR_013556|||http://purl.uniprot.org/annotation/VAR_013557|||http://purl.uniprot.org/annotation/VAR_022029|||http://purl.uniprot.org/annotation/VAR_024699|||http://purl.uniprot.org/annotation/VAR_053404|||http://purl.uniprot.org/annotation/VAR_053405|||http://purl.uniprot.org/annotation/VAR_053406|||http://purl.uniprot.org/annotation/VAR_053407|||http://purl.uniprot.org/annotation/VAR_053408|||http://purl.uniprot.org/annotation/VAR_053409|||http://purl.uniprot.org/annotation/VAR_060040|||http://purl.uniprot.org/annotation/VAR_071512|||http://purl.uniprot.org/annotation/VAR_083515|||http://purl.uniprot.org/annotation/VAR_083516|||http://purl.uniprot.org/annotation/VAR_083517|||http://purl.uniprot.org/annotation/VSP_006779|||http://purl.uniprot.org/annotation/VSP_006780|||http://purl.uniprot.org/annotation/VSP_006781|||http://purl.uniprot.org/annotation/VSP_006782
http://togogenome.org/gene/9606:DAAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YYF7|||http://purl.uniprot.org/uniprot/Q86T65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DAD|||Disheveled-associated activator of morphogenesis 2|||Disordered|||FH1|||FH2|||GBD/FH3|||In NPHS24; affects the regulation of filopodia formation.|||In NPHS24; unknown pathological significance; affects the regulation of filopodia formation.|||In isoform 2.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194909|||http://purl.uniprot.org/annotation/VAR_055805|||http://purl.uniprot.org/annotation/VAR_055806|||http://purl.uniprot.org/annotation/VAR_085585|||http://purl.uniprot.org/annotation/VAR_085586|||http://purl.uniprot.org/annotation/VAR_085587|||http://purl.uniprot.org/annotation/VAR_085588|||http://purl.uniprot.org/annotation/VAR_085589|||http://purl.uniprot.org/annotation/VSP_047360
http://togogenome.org/gene/9606:OPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KLJ9|||http://purl.uniprot.org/uniprot/E5KLK0|||http://purl.uniprot.org/uniprot/O60313                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cleavage at site S1|||Dynamin-like 120 kDa protein, form S1|||Dynamin-like 120 kDa protein, mitochondrial|||Dynamin-type G|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Helical|||In BEHRS.|||In DOA+ and OPA1.|||In DOA+ and OPA1; decreased GTPase activity; loss of function in promoting mitochondrial fusion.|||In DOA+.|||In DOA+; impairs protein folding; loss of function in promoting mitochondrial fusion.|||In MTDPS14.|||In OPA1 and BEHRS.|||In OPA1 and DOA+.|||In OPA1) (Ref.28.|||In OPA1.|||In OPA1; impairs protein folding; loss of function in promoting mitochondrial fusion.|||In OPA1; loss of GTPase activity; loss of function in promoting mitochondrial fusion.|||In OPA1; loss of function in promoting mitochondrial fusion.|||In OPA1; loss of lipid binding and partial loss of function in promoting mitochondrial fusion.|||In OPA1; unknown pathological significance.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 7.|||In isoform 4 and isoform 5.|||LQQQIQ motif|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007397|||http://purl.uniprot.org/annotation/PRO_0000253479|||http://purl.uniprot.org/annotation/VAR_011483|||http://purl.uniprot.org/annotation/VAR_011484|||http://purl.uniprot.org/annotation/VAR_011485|||http://purl.uniprot.org/annotation/VAR_015741|||http://purl.uniprot.org/annotation/VAR_022923|||http://purl.uniprot.org/annotation/VAR_022924|||http://purl.uniprot.org/annotation/VAR_022925|||http://purl.uniprot.org/annotation/VAR_022926|||http://purl.uniprot.org/annotation/VAR_022927|||http://purl.uniprot.org/annotation/VAR_022928|||http://purl.uniprot.org/annotation/VAR_022929|||http://purl.uniprot.org/annotation/VAR_022930|||http://purl.uniprot.org/annotation/VAR_026533|||http://purl.uniprot.org/annotation/VAR_028370|||http://purl.uniprot.org/annotation/VAR_060825|||http://purl.uniprot.org/annotation/VAR_060826|||http://purl.uniprot.org/annotation/VAR_060827|||http://purl.uniprot.org/annotation/VAR_060828|||http://purl.uniprot.org/annotation/VAR_060829|||http://purl.uniprot.org/annotation/VAR_060830|||http://purl.uniprot.org/annotation/VAR_060831|||http://purl.uniprot.org/annotation/VAR_060832|||http://purl.uniprot.org/annotation/VAR_060833|||http://purl.uniprot.org/annotation/VAR_060834|||http://purl.uniprot.org/annotation/VAR_060835|||http://purl.uniprot.org/annotation/VAR_060836|||http://purl.uniprot.org/annotation/VAR_060837|||http://purl.uniprot.org/annotation/VAR_060838|||http://purl.uniprot.org/annotation/VAR_060839|||http://purl.uniprot.org/annotation/VAR_060840|||http://purl.uniprot.org/annotation/VAR_060841|||http://purl.uniprot.org/annotation/VAR_060842|||http://purl.uniprot.org/annotation/VAR_060843|||http://purl.uniprot.org/annotation/VAR_060844|||http://purl.uniprot.org/annotation/VAR_060845|||http://purl.uniprot.org/annotation/VAR_060846|||http://purl.uniprot.org/annotation/VAR_060847|||http://purl.uniprot.org/annotation/VAR_060848|||http://purl.uniprot.org/annotation/VAR_060849|||http://purl.uniprot.org/annotation/VAR_060850|||http://purl.uniprot.org/annotation/VAR_060851|||http://purl.uniprot.org/annotation/VAR_060852|||http://purl.uniprot.org/annotation/VAR_060853|||http://purl.uniprot.org/annotation/VAR_060854|||http://purl.uniprot.org/annotation/VAR_060855|||http://purl.uniprot.org/annotation/VAR_060856|||http://purl.uniprot.org/annotation/VAR_060857|||http://purl.uniprot.org/annotation/VAR_060858|||http://purl.uniprot.org/annotation/VAR_060859|||http://purl.uniprot.org/annotation/VAR_060860|||http://purl.uniprot.org/annotation/VAR_060861|||http://purl.uniprot.org/annotation/VAR_060862|||http://purl.uniprot.org/annotation/VAR_060863|||http://purl.uniprot.org/annotation/VAR_060864|||http://purl.uniprot.org/annotation/VAR_060865|||http://purl.uniprot.org/annotation/VAR_060866|||http://purl.uniprot.org/annotation/VAR_060867|||http://purl.uniprot.org/annotation/VAR_060868|||http://purl.uniprot.org/annotation/VAR_060869|||http://purl.uniprot.org/annotation/VAR_067355|||http://purl.uniprot.org/annotation/VAR_072125|||http://purl.uniprot.org/annotation/VAR_072126|||http://purl.uniprot.org/annotation/VAR_072127|||http://purl.uniprot.org/annotation/VAR_072128|||http://purl.uniprot.org/annotation/VAR_072129|||http://purl.uniprot.org/annotation/VAR_072130|||http://purl.uniprot.org/annotation/VAR_072131|||http://purl.uniprot.org/annotation/VAR_072132|||http://purl.uniprot.org/annotation/VAR_072133|||http://purl.uniprot.org/annotation/VAR_075903|||http://purl.uniprot.org/annotation/VAR_075904|||http://purl.uniprot.org/annotation/VAR_082805|||http://purl.uniprot.org/annotation/VSP_021035|||http://purl.uniprot.org/annotation/VSP_059072|||http://purl.uniprot.org/annotation/VSP_059073|||http://purl.uniprot.org/annotation/VSP_059074
http://togogenome.org/gene/9606:KLHL28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1E0|||http://purl.uniprot.org/uniprot/J3KNY7|||http://purl.uniprot.org/uniprot/Q9NXS3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119064|||http://purl.uniprot.org/annotation/VAR_061339|||http://purl.uniprot.org/annotation/VSP_009800
http://togogenome.org/gene/9606:NADSYN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IA69                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CN hydrolase|||Eliminates glutamine-dependent NAD synthetase activity with the ammonia-dependent activity intact.|||For glutaminase activity|||Glutamine-dependent NAD(+) synthetase|||In VCRL3.|||In VCRL3; decreased protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity.|||In VCRL3; loss of protein expression.|||In VCRL3; no effect on protein expression; decreased NAD(+) synthase (glutamine-hydrolyzing) activity.|||In isoform 2.|||Ligase|||Nucleophile; for glutaminase activity|||Proton acceptor; for glutaminase activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237577|||http://purl.uniprot.org/annotation/VAR_026497|||http://purl.uniprot.org/annotation/VAR_056204|||http://purl.uniprot.org/annotation/VAR_056205|||http://purl.uniprot.org/annotation/VAR_056206|||http://purl.uniprot.org/annotation/VAR_058703|||http://purl.uniprot.org/annotation/VAR_084040|||http://purl.uniprot.org/annotation/VAR_084041|||http://purl.uniprot.org/annotation/VAR_084042|||http://purl.uniprot.org/annotation/VAR_084043|||http://purl.uniprot.org/annotation/VAR_084044|||http://purl.uniprot.org/annotation/VSP_056585|||http://purl.uniprot.org/annotation/VSP_056586
http://togogenome.org/gene/9606:MT1HL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DM35                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein 1H-like protein 1|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000422542
http://togogenome.org/gene/9606:LRRC74B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQY2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 74B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318964|||http://purl.uniprot.org/annotation/VAR_038923|||http://purl.uniprot.org/annotation/VAR_038924|||http://purl.uniprot.org/annotation/VSP_031321
http://togogenome.org/gene/9606:RASGRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RA89|||http://purl.uniprot.org/uniprot/O95267                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Decrease of Ras activation indicated by decrease of ERK phosphorylation.|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||In IMD64.|||In IMD64; loss of protein expression.|||In IMD64; no effect on protein expression; decreased T cell activation.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increase of Ras activation indicated by increase of ERK phosphorylation.|||Loss of function; prevents Ras activation.|||Loss of localization to the endoplasmic reticulum and the Golgi apparatus.|||N-terminal Ras-GEF|||PT region; mediates the BCR-dependent translocation to plasma membrane|||Phorbol-ester/DAG-type|||Phosphothreonine; by PKC|||RAS guanyl-releasing protein 1|||Ras exchanger motif region; required for transforming activity|||Ras-GEF|||Suppress the PT region-mediated translocation to plasma membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316978|||http://purl.uniprot.org/annotation/VAR_083338|||http://purl.uniprot.org/annotation/VAR_083339|||http://purl.uniprot.org/annotation/VAR_083340|||http://purl.uniprot.org/annotation/VAR_083341|||http://purl.uniprot.org/annotation/VSP_030836|||http://purl.uniprot.org/annotation/VSP_030837|||http://purl.uniprot.org/annotation/VSP_030838|||http://purl.uniprot.org/annotation/VSP_030839|||http://purl.uniprot.org/annotation/VSP_030840|||http://purl.uniprot.org/annotation/VSP_030841|||http://purl.uniprot.org/annotation/VSP_030842
http://togogenome.org/gene/9606:ARHGAP17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68EM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BAR|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of function; leading to defects in tight junction maintenance.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 17|||Rho-GAP|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280462|||http://purl.uniprot.org/annotation/VSP_023682|||http://purl.uniprot.org/annotation/VSP_023683|||http://purl.uniprot.org/annotation/VSP_023684|||http://purl.uniprot.org/annotation/VSP_023685|||http://purl.uniprot.org/annotation/VSP_023686|||http://purl.uniprot.org/annotation/VSP_023687|||http://purl.uniprot.org/annotation/VSP_023688|||http://purl.uniprot.org/annotation/VSP_023689
http://togogenome.org/gene/9606:SLC25A20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43772                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In CACTD.|||Mitochondrial carnitine/acylcarnitine carrier protein|||Mitochondrial matrix|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090628|||http://purl.uniprot.org/annotation/VAR_021818|||http://purl.uniprot.org/annotation/VAR_021819|||http://purl.uniprot.org/annotation/VAR_021820
http://togogenome.org/gene/9606:ATP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03928|||http://purl.uniprot.org/uniprot/U5YV54                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  ATP synthase protein 8|||Helical|||In MC5DM2 and CMHI.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195536|||http://purl.uniprot.org/annotation/VAR_008563|||http://purl.uniprot.org/annotation/VAR_008564|||http://purl.uniprot.org/annotation/VAR_008565|||http://purl.uniprot.org/annotation/VAR_069527
http://togogenome.org/gene/9606:GFOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXC2|||http://purl.uniprot.org/uniprot/S4R302                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gfo/Idh/MocA-like oxidoreductase N-terminal|||Glucose-fructose oxidoreductase domain-containing protein 1|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282968|||http://purl.uniprot.org/annotation/VAR_082824|||http://purl.uniprot.org/annotation/VSP_024261|||http://purl.uniprot.org/annotation/VSP_041468
http://togogenome.org/gene/9606:COL5A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2ZZ86|||http://purl.uniprot.org/uniprot/P20908|||http://purl.uniprot.org/uniprot/Q59EE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  5-hydroxylysine|||Associated with increased risk of cervical artery dissection.|||Basic and acidic residues|||C-terminal propeptide|||Collagen alpha-1(V) chain|||Disordered|||Fibrillar collagen NC1|||Found in a renal cell carcinoma case; somatic mutation.|||Hydroxyproline|||In EDSCL1.|||In EDSCL1; not or less efficiently secreted into the extracellular matrix.|||In FMDMF.|||In FMDMF; unknown pathological significance.|||In isoform 2.|||Interchain (with C-1645)|||Interchain (with C-1662)|||Interrupted collagenous region|||Laminin G-like|||Nonhelical region|||Polar residues|||Pro residues|||Sulfotyrosine|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005756|||http://purl.uniprot.org/annotation/PRO_0000005757|||http://purl.uniprot.org/annotation/PRO_5002785244|||http://purl.uniprot.org/annotation/VAR_001808|||http://purl.uniprot.org/annotation/VAR_015412|||http://purl.uniprot.org/annotation/VAR_015413|||http://purl.uniprot.org/annotation/VAR_057902|||http://purl.uniprot.org/annotation/VAR_057903|||http://purl.uniprot.org/annotation/VAR_057904|||http://purl.uniprot.org/annotation/VAR_057905|||http://purl.uniprot.org/annotation/VAR_057906|||http://purl.uniprot.org/annotation/VAR_057908|||http://purl.uniprot.org/annotation/VAR_057909|||http://purl.uniprot.org/annotation/VAR_064702|||http://purl.uniprot.org/annotation/VAR_075702|||http://purl.uniprot.org/annotation/VAR_075703|||http://purl.uniprot.org/annotation/VAR_085830|||http://purl.uniprot.org/annotation/VAR_085831|||http://purl.uniprot.org/annotation/VAR_085832|||http://purl.uniprot.org/annotation/VAR_085833|||http://purl.uniprot.org/annotation/VAR_085834|||http://purl.uniprot.org/annotation/VSP_059655
http://togogenome.org/gene/9606:ARPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15511                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Actin-related protein 2/3 complex subunit 5|||Disordered|||In isoform 2.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124054|||http://purl.uniprot.org/annotation/VSP_024028
http://togogenome.org/gene/9606:SCGB2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0G5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 2B member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342373
http://togogenome.org/gene/9606:RNF149                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC42                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase RNF149|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||PA|||Phosphoserine|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261611|||http://purl.uniprot.org/annotation/VAR_029455|||http://purl.uniprot.org/annotation/VAR_029456|||http://purl.uniprot.org/annotation/VAR_029457|||http://purl.uniprot.org/annotation/VAR_035958
http://togogenome.org/gene/9606:GNG14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PRI1                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent                                                                                  ^@                                                                                  G protein gamma                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:BBLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUW7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Bublin coiled-coil protein|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195161
http://togogenome.org/gene/9606:C2orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LR7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C2orf50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307802
http://togogenome.org/gene/9606:HIVEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31629                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||10 X 4 AA tandem repeats of S-P-[RGMKC]-[RK]|||2|||3|||4|||5|||6|||7|||8|||9|||Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Transcription factor HIVEP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047371|||http://purl.uniprot.org/annotation/VAR_052754|||http://purl.uniprot.org/annotation/VAR_052755|||http://purl.uniprot.org/annotation/VAR_052756|||http://purl.uniprot.org/annotation/VAR_052757
http://togogenome.org/gene/9606:DHRS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y394                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 7|||In isoform 2.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031968|||http://purl.uniprot.org/annotation/VAR_052319|||http://purl.uniprot.org/annotation/VSP_008103
http://togogenome.org/gene/9606:OR5B12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96R08                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5B12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150587|||http://purl.uniprot.org/annotation/VAR_053191|||http://purl.uniprot.org/annotation/VAR_053192
http://togogenome.org/gene/9606:EIF4G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSA7|||http://purl.uniprot.org/uniprot/O43432|||http://purl.uniprot.org/uniprot/Q59GJ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by enterovirus/rhinovirus protease 2A|||Cleavage; by foot-and-mouth disease virus leader protease|||Disordered|||EIF4A-binding|||EIF4E-binding|||Eukaryotic translation initiation factor 4 gamma 3|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MI|||MIF4G|||Necessary but not sufficient for MKNK1-binding|||PABPC1-binding|||Phosphoserine|||Phosphoserine; by CaMK1|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces binding to EIF4A; when associated with D-756 and D-759.|||Reduces binding to EIF4A; when associated with D-756 and D-764.|||Reduces binding to EIF4A; when associated with D-759 and D-764.|||Reduces binding to EIF4A; when associated with D-814.|||Reduces binding to EIF4A; when associated with D-820.|||Reduces binding to IRES.|||W2|||eIF3/EIF4A-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213329|||http://purl.uniprot.org/annotation/VAR_034009|||http://purl.uniprot.org/annotation/VAR_048924|||http://purl.uniprot.org/annotation/VAR_048925|||http://purl.uniprot.org/annotation/VSP_010487|||http://purl.uniprot.org/annotation/VSP_010488|||http://purl.uniprot.org/annotation/VSP_010489|||http://purl.uniprot.org/annotation/VSP_043447|||http://purl.uniprot.org/annotation/VSP_043448|||http://purl.uniprot.org/annotation/VSP_054502
http://togogenome.org/gene/9606:PRR12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In NOC.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243945|||http://purl.uniprot.org/annotation/VAR_086258|||http://purl.uniprot.org/annotation/VAR_086259|||http://purl.uniprot.org/annotation/VAR_086260|||http://purl.uniprot.org/annotation/VAR_086261|||http://purl.uniprot.org/annotation/VAR_086262|||http://purl.uniprot.org/annotation/VAR_086263|||http://purl.uniprot.org/annotation/VAR_086264|||http://purl.uniprot.org/annotation/VAR_086265|||http://purl.uniprot.org/annotation/VSP_019503
http://togogenome.org/gene/9606:DLD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R713|||http://purl.uniprot.org/uniprot/E9PEX6|||http://purl.uniprot.org/uniprot/P09622                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.|||Decreases dehydrogenase activity. Loss of proteolytic activity.|||Dihydrolipoyl dehydrogenase, mitochondrial|||Does not affect dihydrolipoyl dehydrogenase activity.|||Does not affect interaction with PDHX.|||FAD/NAD(P)-binding|||Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex|||In DLDD.|||In DLDD; loss of enzyme activity; abolished interaction with PDHX.|||In DLDD; loss of enzyme activity; reduced interaction with PDHX.|||In DLDD; no effect on interaction with PDHX.|||In DLDD; reduced dehydrogenase activity; increased proteolytic activity.|||In DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX.|||In DLDD; reduced enzyme activity.|||In isoform 2.|||In isoform 3.|||Loss of dehydrogenase activity. Increases proteolytic activity.|||Loss of proteolytic activity. Does not affect dehydrogenase activity.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Proton acceptor|||Pyridine nucleotide-disulphide oxidoreductase dimerisation|||Redox-active|||Reduces dihydrolipoyl dehydrogenase activity.|||Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.|||Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030295|||http://purl.uniprot.org/annotation/VAR_006907|||http://purl.uniprot.org/annotation/VAR_006908|||http://purl.uniprot.org/annotation/VAR_014555|||http://purl.uniprot.org/annotation/VAR_015820|||http://purl.uniprot.org/annotation/VAR_015821|||http://purl.uniprot.org/annotation/VAR_031922|||http://purl.uniprot.org/annotation/VAR_076985|||http://purl.uniprot.org/annotation/VAR_076986|||http://purl.uniprot.org/annotation/VAR_076987|||http://purl.uniprot.org/annotation/VAR_076988|||http://purl.uniprot.org/annotation/VAR_076989|||http://purl.uniprot.org/annotation/VAR_076990|||http://purl.uniprot.org/annotation/VAR_076991|||http://purl.uniprot.org/annotation/VSP_055855|||http://purl.uniprot.org/annotation/VSP_055856
http://togogenome.org/gene/9606:UROC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N76                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In UROCD.|||In UROCD; loss of activity.|||In isoform 2.|||Urocanate hydratase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207374|||http://purl.uniprot.org/annotation/VAR_034000|||http://purl.uniprot.org/annotation/VAR_034001|||http://purl.uniprot.org/annotation/VAR_042732|||http://purl.uniprot.org/annotation/VAR_060221|||http://purl.uniprot.org/annotation/VAR_062649|||http://purl.uniprot.org/annotation/VSP_045422
http://togogenome.org/gene/9606:BICRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZM4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BRD4-interacting chromatin-remodeling complex-associated protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CSS12.|||In CSS12; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083864|||http://purl.uniprot.org/annotation/VAR_059665|||http://purl.uniprot.org/annotation/VAR_061663|||http://purl.uniprot.org/annotation/VAR_085989|||http://purl.uniprot.org/annotation/VAR_085990|||http://purl.uniprot.org/annotation/VAR_085991|||http://purl.uniprot.org/annotation/VAR_085992|||http://purl.uniprot.org/annotation/VSP_035776
http://togogenome.org/gene/9606:P3H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32P28                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Fe2OG dioxygenase|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Prevents secretion from ER|||Prolyl 3-hydroxylase 1|||TPR 1|||TPR 2|||TPR 3|||TPR 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240352|||http://purl.uniprot.org/annotation/VAR_033252|||http://purl.uniprot.org/annotation/VAR_033253|||http://purl.uniprot.org/annotation/VAR_033254|||http://purl.uniprot.org/annotation/VAR_050442|||http://purl.uniprot.org/annotation/VSP_019346|||http://purl.uniprot.org/annotation/VSP_019347|||http://purl.uniprot.org/annotation/VSP_019348|||http://purl.uniprot.org/annotation/VSP_054864
http://togogenome.org/gene/9606:TREML2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2D2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Trem-like transcript 2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253857|||http://purl.uniprot.org/annotation/VAR_055418|||http://purl.uniprot.org/annotation/VAR_055419|||http://purl.uniprot.org/annotation/VAR_055420|||http://purl.uniprot.org/annotation/VAR_059412
http://togogenome.org/gene/9606:MTCP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56278                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Protein p13 MTCP-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184486
http://togogenome.org/gene/9606:EXOSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQW2|||http://purl.uniprot.org/uniprot/Q13868                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Exosome complex component RRP4|||In SHRF.|||In isoform 2.|||In isoform 3.|||K Homology|||Phosphoserine|||S1 motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087129|||http://purl.uniprot.org/annotation/VAR_080552|||http://purl.uniprot.org/annotation/VAR_080553|||http://purl.uniprot.org/annotation/VSP_054921|||http://purl.uniprot.org/annotation/VSP_057568
http://togogenome.org/gene/9606:CCN6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYW3|||http://purl.uniprot.org/uniprot/I6L968|||http://purl.uniprot.org/uniprot/O95389                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  CTCK|||Cellular communication network factor 6|||IGFBP N-terminal|||In PPRD.|||In PPRD; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||TSP type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014412|||http://purl.uniprot.org/annotation/PRO_5003704964|||http://purl.uniprot.org/annotation/PRO_5017483571|||http://purl.uniprot.org/annotation/VAR_016224|||http://purl.uniprot.org/annotation/VAR_016225|||http://purl.uniprot.org/annotation/VAR_049567|||http://purl.uniprot.org/annotation/VAR_081483|||http://purl.uniprot.org/annotation/VAR_081484|||http://purl.uniprot.org/annotation/VAR_081485|||http://purl.uniprot.org/annotation/VAR_081486|||http://purl.uniprot.org/annotation/VAR_081487|||http://purl.uniprot.org/annotation/VAR_081488|||http://purl.uniprot.org/annotation/VAR_081489|||http://purl.uniprot.org/annotation/VAR_081490|||http://purl.uniprot.org/annotation/VAR_081491|||http://purl.uniprot.org/annotation/VAR_081492|||http://purl.uniprot.org/annotation/VAR_081493|||http://purl.uniprot.org/annotation/VAR_081494|||http://purl.uniprot.org/annotation/VAR_081495|||http://purl.uniprot.org/annotation/VAR_081652|||http://purl.uniprot.org/annotation/VAR_081653|||http://purl.uniprot.org/annotation/VAR_081654|||http://purl.uniprot.org/annotation/VAR_081655|||http://purl.uniprot.org/annotation/VAR_081656|||http://purl.uniprot.org/annotation/VAR_081657|||http://purl.uniprot.org/annotation/VAR_081658|||http://purl.uniprot.org/annotation/VAR_081659|||http://purl.uniprot.org/annotation/VSP_037803
http://togogenome.org/gene/9606:MFSD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6N075                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Molybdate-anion transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273401|||http://purl.uniprot.org/annotation/VSP_046647
http://togogenome.org/gene/9606:CMAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFW8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BC1 motif|||BC2 motif|||BC3 motif|||Disordered|||In isoform 2.|||N-acetylmethionine|||N-acylneuraminate cytidylyltransferase|||Omega-N-methylarginine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213199|||http://purl.uniprot.org/annotation/VSP_012764
http://togogenome.org/gene/9606:SPATS2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZZ7|||http://purl.uniprot.org/uniprot/Q9NUQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||SPATS2-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307699|||http://purl.uniprot.org/annotation/VSP_028792|||http://purl.uniprot.org/annotation/VSP_054241|||http://purl.uniprot.org/annotation/VSP_054242
http://togogenome.org/gene/9606:PAXBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6E6|||http://purl.uniprot.org/uniprot/Q9Y5B6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a family with global developmental delay and myopathic hypotonia; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Necessary and sufficient for interaction with PAX7|||PAX3- and PAX7-binding protein 1|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087439|||http://purl.uniprot.org/annotation/VAR_079417|||http://purl.uniprot.org/annotation/VSP_004263|||http://purl.uniprot.org/annotation/VSP_004264|||http://purl.uniprot.org/annotation/VSP_004265|||http://purl.uniprot.org/annotation/VSP_004266|||http://purl.uniprot.org/annotation/VSP_004267
http://togogenome.org/gene/9606:SUN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E2A6|||http://purl.uniprot.org/uniprot/Q9UH99                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Decreases interaction with SYNE2.|||Decreases interaction with SYNE2. Disrupts interaction with SYNE2; when associated with E-603 and E-641.|||Decreases interaction with SYNE2. Disrupts interaction with SYNE2; when associated with E-603 and E-703.|||Decreases interaction with SYNE2. Disrupts interaction with SYNE2; when associated with E-641 and E-703.|||Decreases stability of the SUN2:SYNE2/KASH2 complex under tensile forces and inhibits force transmission through the complex.|||Disordered|||Disrupts interaction with SYNE2, impairs localization to the nuclear envelope.|||Disrupts interaction with SYNE2.|||Helical|||In isoform 2.|||In isoform 3.|||Interchain (with C-6862 in SYNE2)|||LMNA-binding|||N-linked (GlcNAc...) asparagine|||Nuclear|||Perinuclear space|||Phosphoserine|||Phosphothreonine|||Polar residues|||SUN|||SUN domain-containing protein 2|||Sufficient for interaction with SYNE1 and SYNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218913|||http://purl.uniprot.org/annotation/VAR_024624|||http://purl.uniprot.org/annotation/VAR_052282|||http://purl.uniprot.org/annotation/VAR_052283|||http://purl.uniprot.org/annotation/VAR_052284|||http://purl.uniprot.org/annotation/VSP_045882|||http://purl.uniprot.org/annotation/VSP_053702
http://togogenome.org/gene/9606:TAF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92804                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||21 X approximate tandem repeats of D-R-[S,G](0,3)-G-G-Y-G-G|||3|||4|||5|||6|||7|||8|||9|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; by PRMT1|||Asymmetric dimethylarginine; by PRMT1; alternate|||Basic and acidic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform Short.|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||RRM|||RanBP2-type|||TATA-binding protein-associated factor 2N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081749|||http://purl.uniprot.org/annotation/VSP_005806
http://togogenome.org/gene/9606:COL11A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12107|||http://purl.uniprot.org/uniprot/Q59HB5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Allysine|||Basic and acidic residues|||C-terminal propeptide|||Collagen alpha-1(XI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Collagen-like 8|||Disordered|||Fibrillar collagen NC1|||In FBCG1.|||In STL2.|||In STL2; overlapping phenotype with Marshall syndrome.|||In a breast cancer sample; somatic mutation.|||In isoform 4.|||In isoform B.|||In isoform C.|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide|||Nonhelical region|||Nonhelical region (C-terminal)|||Pro residues|||Short nonhelical segment|||Telopeptide|||Triple-helical region|||Triple-helical region (interrupted)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005774|||http://purl.uniprot.org/annotation/PRO_0000005775|||http://purl.uniprot.org/annotation/PRO_0000005776|||http://purl.uniprot.org/annotation/VAR_013583|||http://purl.uniprot.org/annotation/VAR_013584|||http://purl.uniprot.org/annotation/VAR_013585|||http://purl.uniprot.org/annotation/VAR_013586|||http://purl.uniprot.org/annotation/VAR_013587|||http://purl.uniprot.org/annotation/VAR_035743|||http://purl.uniprot.org/annotation/VAR_035744|||http://purl.uniprot.org/annotation/VAR_035745|||http://purl.uniprot.org/annotation/VAR_047723|||http://purl.uniprot.org/annotation/VAR_047724|||http://purl.uniprot.org/annotation/VAR_047725|||http://purl.uniprot.org/annotation/VAR_047726|||http://purl.uniprot.org/annotation/VAR_047727|||http://purl.uniprot.org/annotation/VAR_047728|||http://purl.uniprot.org/annotation/VAR_063675|||http://purl.uniprot.org/annotation/VAR_063676|||http://purl.uniprot.org/annotation/VAR_063677|||http://purl.uniprot.org/annotation/VAR_063678|||http://purl.uniprot.org/annotation/VAR_065904|||http://purl.uniprot.org/annotation/VAR_065905|||http://purl.uniprot.org/annotation/VSP_001145|||http://purl.uniprot.org/annotation/VSP_001146|||http://purl.uniprot.org/annotation/VSP_046318
http://togogenome.org/gene/9606:MYT1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YF72|||http://purl.uniprot.org/uniprot/A0A3B3IRM3|||http://purl.uniprot.org/uniprot/A0A3B3IRX5|||http://purl.uniprot.org/uniprot/A0A3B3IS14|||http://purl.uniprot.org/uniprot/A0A3B3IS61|||http://purl.uniprot.org/uniprot/A0A3B3ISW5|||http://purl.uniprot.org/uniprot/Q9UL68                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||CCHHC-type 1|||CCHHC-type 2|||CCHHC-type 3|||CCHHC-type 4|||CCHHC-type 5|||CCHHC-type 6|||Disordered|||In isoform 3.|||In isoform 4.|||Myelin transcription factor 1|||Myelin transcription factor 1-like protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096673|||http://purl.uniprot.org/annotation/VSP_015722|||http://purl.uniprot.org/annotation/VSP_015724|||http://purl.uniprot.org/annotation/VSP_015725
http://togogenome.org/gene/9606:LPAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZX0|||http://purl.uniprot.org/uniprot/Q92633                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs localization at the cell membrane.|||In isoform 2.|||Lysophosphatidic acid receptor 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069417|||http://purl.uniprot.org/annotation/VAR_049414|||http://purl.uniprot.org/annotation/VSP_057046
http://togogenome.org/gene/9606:GALNT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BM8|||http://purl.uniprot.org/uniprot/Q10472                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 1|||Polypeptide N-acetylgalactosaminyltransferase 1 soluble form|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012257|||http://purl.uniprot.org/annotation/PRO_0000223387|||http://purl.uniprot.org/annotation/VAR_033946|||http://purl.uniprot.org/annotation/VSP_011200
http://togogenome.org/gene/9606:IMMP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LU5                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Chain                                                                                  ^@                                                                                  Mitochondrial inner membrane protease subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259573
http://togogenome.org/gene/9606:HTR2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41595                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 2B|||Abolishes agonist binding.|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Hydrophobic barrier that decreases the speed of ligand binding and dissociation|||Impairs protein folding and stability. Strongly reduced cell surface expression.|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||No effect on agonist binding.|||No effect on agonist binding. Strongly increases dissociation of bound lysergic acid diethylamine, without affecting binding affinity. Reduces signaling via arrestins, but has no effect on signaling via the phosphatidylinositol-calcium second messenger system.|||PDZ-binding|||S-palmitoyl cysteine|||Slightly decreases agonist binding.|||[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068953|||http://purl.uniprot.org/annotation/VAR_055907|||http://purl.uniprot.org/annotation/VAR_064574|||http://purl.uniprot.org/annotation/VAR_064575|||http://purl.uniprot.org/annotation/VAR_064576
http://togogenome.org/gene/9606:SDAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DT66|||http://purl.uniprot.org/uniprot/E7EW05|||http://purl.uniprot.org/uniprot/Q9NVU7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein SDA1 homolog|||SDA1 C-terminal|||SDA1 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287482|||http://purl.uniprot.org/annotation/VAR_032312|||http://purl.uniprot.org/annotation/VAR_032313|||http://purl.uniprot.org/annotation/VAR_032314|||http://purl.uniprot.org/annotation/VAR_032315|||http://purl.uniprot.org/annotation/VSP_025505
http://togogenome.org/gene/9606:HDAC10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes deacetylase activity. Does not affect interaction with HDAC3. Loss of autophagy regulation.|||Disordered|||Histone deacetylase|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polyamine deacetylase HDAC10|||Proton donor/acceptor|||Substrate specificity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114712|||http://purl.uniprot.org/annotation/VAR_049356|||http://purl.uniprot.org/annotation/VSP_002089|||http://purl.uniprot.org/annotation/VSP_002090|||http://purl.uniprot.org/annotation/VSP_014698|||http://purl.uniprot.org/annotation/VSP_014699
http://togogenome.org/gene/9606:DEFB108B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NET1                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 108B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006981|||http://purl.uniprot.org/annotation/VAR_048862|||http://purl.uniprot.org/annotation/VAR_059246|||http://purl.uniprot.org/annotation/VAR_059247|||http://purl.uniprot.org/annotation/VAR_059248
http://togogenome.org/gene/9606:ODAPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WV33|||http://purl.uniprot.org/uniprot/Q17RF5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Odontogenesis associated phosphoprotein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301959|||http://purl.uniprot.org/annotation/PRO_5014013275|||http://purl.uniprot.org/annotation/VAR_034915|||http://purl.uniprot.org/annotation/VAR_034916|||http://purl.uniprot.org/annotation/VSP_046356
http://togogenome.org/gene/9606:USP17L29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0WX57                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes enzymatic activity. Loss of the pro-apoptotic function.|||Disordered|||Nucleophile|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 17-like protein 24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331643
http://togogenome.org/gene/9606:PIGY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MUY2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In HPMRS6; may diminish protein expression and/or stability; decreases cell surface expression of GPI-anchored proteins, including CD55 and CD59, in skin fibroblasts from affected individual.|||Lumenal|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246311|||http://purl.uniprot.org/annotation/VAR_076351
http://togogenome.org/gene/9606:TSLP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969D9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||Thymic stromal lymphopoietin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300873|||http://purl.uniprot.org/annotation/VSP_057462
http://togogenome.org/gene/9606:TMEM40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXI0|||http://purl.uniprot.org/uniprot/Q8WWA1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Transmembrane protein 40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280358|||http://purl.uniprot.org/annotation/VSP_023643|||http://purl.uniprot.org/annotation/VSP_055682
http://togogenome.org/gene/9606:TRIM24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15164                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with histone H3.|||B box-type 1|||B box-type 2|||Breakpoint for translocation to form TRIM24-RET oncogene|||Bromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In a lung squamous cell carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform Short.|||Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)|||Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)|||Nuclear localization signal|||Nuclear receptor binding site (NRBS)|||Omega-N-methylarginine|||PHD-type|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Pro residues|||RING-type|||Strongly reduced affinity for histone H3 that is acetylated at 'Lys-23' (H3K23ac).|||Strongly reduced affinity for histone H3 that is not methylated at 'Lys-4' (H3K4me0).|||Transcription intermediary factor 1-alpha|||Ubiquitination is significantly lower than wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056390|||http://purl.uniprot.org/annotation/VAR_042382|||http://purl.uniprot.org/annotation/VAR_042383|||http://purl.uniprot.org/annotation/VAR_042384|||http://purl.uniprot.org/annotation/VAR_042385|||http://purl.uniprot.org/annotation/VAR_052148|||http://purl.uniprot.org/annotation/VSP_005772
http://togogenome.org/gene/9606:ELMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BJ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ELMO|||Engulfment and cell motility protein 3|||In isoform 1.|||In isoform 3.|||PH|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153716|||http://purl.uniprot.org/annotation/VAR_055402|||http://purl.uniprot.org/annotation/VAR_055403|||http://purl.uniprot.org/annotation/VAR_055404|||http://purl.uniprot.org/annotation/VSP_037341|||http://purl.uniprot.org/annotation/VSP_037342
http://togogenome.org/gene/9606:ZNF431                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF32                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 431                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047579|||http://purl.uniprot.org/annotation/VAR_052825
http://togogenome.org/gene/9606:CA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35219                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Ancestral zinc ligand|||Carbonic anhydrase-related protein|||Disordered|||In CAMRQ3; affects protein stability owing to accelerated proteasomal degradation.|||Phosphoserine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077433|||http://purl.uniprot.org/annotation/VAR_063634
http://togogenome.org/gene/9606:SLC35F3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY50                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Solute carrier family 35 member F3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307879|||http://purl.uniprot.org/annotation/VAR_036700|||http://purl.uniprot.org/annotation/VSP_028850
http://togogenome.org/gene/9606:MYO3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEV4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||IQ 3|||In a renal clear cell carcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with MORN4|||Myosin motor|||Myosin-IIIa|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086413|||http://purl.uniprot.org/annotation/VAR_021866|||http://purl.uniprot.org/annotation/VAR_021867|||http://purl.uniprot.org/annotation/VAR_022779|||http://purl.uniprot.org/annotation/VAR_033905|||http://purl.uniprot.org/annotation/VAR_040871|||http://purl.uniprot.org/annotation/VAR_040872|||http://purl.uniprot.org/annotation/VAR_040873|||http://purl.uniprot.org/annotation/VAR_040874|||http://purl.uniprot.org/annotation/VAR_040875|||http://purl.uniprot.org/annotation/VAR_040876|||http://purl.uniprot.org/annotation/VAR_040877|||http://purl.uniprot.org/annotation/VAR_040878|||http://purl.uniprot.org/annotation/VAR_040879|||http://purl.uniprot.org/annotation/VAR_040880|||http://purl.uniprot.org/annotation/VAR_040881|||http://purl.uniprot.org/annotation/VAR_040882|||http://purl.uniprot.org/annotation/VAR_040883|||http://purl.uniprot.org/annotation/VAR_040884|||http://purl.uniprot.org/annotation/VAR_040885|||http://purl.uniprot.org/annotation/VSP_056231|||http://purl.uniprot.org/annotation/VSP_056232
http://togogenome.org/gene/9606:HSD11B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80365                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  11-beta-hydroxysteroid dehydrogenase type 2|||Abolishes cofactor specificity.|||Almost complete loss of enzyme activity.|||Complete loss of enzyme activity.|||Disordered|||Essential for protein stability|||In AME.|||In AME; abolishes enzyme activity.|||In AME; abolishes enzyme activity; decreased half-life from 21 to 3 hours compared to wild-type, probably due to degradation via the proteasomal pathway.|||In AME; associated with N-244.|||In AME; associated with R-250.|||In AME; decreased half-life from 21 to 4 hours compared to wild-type, probably due to degradation via the proteasomal pathway.|||In AME; decreases enzyme activity by 33%.|||In AME; decreases enzyme activity.|||In AME; reduces enzyme activity by 90%.|||In AME; reduces enzyme activity by at least 95%.|||In AME; reduces enzyme activity to about 6% of wild type.|||In AME; reduces enzyme activity.|||In hypertension; decreases affinity for cortisol.|||No effect on enzyme activity.|||Proton acceptor|||Reduced enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054627|||http://purl.uniprot.org/annotation/VAR_006958|||http://purl.uniprot.org/annotation/VAR_006959|||http://purl.uniprot.org/annotation/VAR_015634|||http://purl.uniprot.org/annotation/VAR_015635|||http://purl.uniprot.org/annotation/VAR_015636|||http://purl.uniprot.org/annotation/VAR_015637|||http://purl.uniprot.org/annotation/VAR_015638|||http://purl.uniprot.org/annotation/VAR_015639|||http://purl.uniprot.org/annotation/VAR_015640|||http://purl.uniprot.org/annotation/VAR_015641|||http://purl.uniprot.org/annotation/VAR_015642|||http://purl.uniprot.org/annotation/VAR_015643|||http://purl.uniprot.org/annotation/VAR_015644|||http://purl.uniprot.org/annotation/VAR_015645|||http://purl.uniprot.org/annotation/VAR_015646|||http://purl.uniprot.org/annotation/VAR_015647|||http://purl.uniprot.org/annotation/VAR_052317|||http://purl.uniprot.org/annotation/VAR_066514|||http://purl.uniprot.org/annotation/VAR_066515|||http://purl.uniprot.org/annotation/VAR_085553
http://togogenome.org/gene/9606:MAMDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z304                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||MAM 1|||MAM 2|||MAM 3|||MAM 4|||MAM domain-containing protein 2|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014862|||http://purl.uniprot.org/annotation/VAR_028080|||http://purl.uniprot.org/annotation/VAR_061318|||http://purl.uniprot.org/annotation/VSP_009834
http://togogenome.org/gene/9606:SYCE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L190                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Synaptonemal complex central element protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000367274|||http://purl.uniprot.org/annotation/VAR_060126
http://togogenome.org/gene/9606:RAD21L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4I0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Double-strand-break repair protein rad21-like protein 1|||Found in a patient with non-obstructive azoospermia; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321921|||http://purl.uniprot.org/annotation/VAR_064917|||http://purl.uniprot.org/annotation/VAR_064918|||http://purl.uniprot.org/annotation/VAR_064919|||http://purl.uniprot.org/annotation/VAR_087424|||http://purl.uniprot.org/annotation/VSP_038157|||http://purl.uniprot.org/annotation/VSP_038158
http://togogenome.org/gene/9606:ATG14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNE5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BATS|||Beclin 1-associated autophagy-related key regulator|||Cysteine repeats|||Disordered|||In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-46 and A-55.|||In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-46 and A-58.|||In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-43; A-55 and A-58.|||In Atg14L4C4A; fails to localize to the endoplasmic reticulum; when associated with A-46; A-55 and A-58.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050774|||http://purl.uniprot.org/annotation/VAR_049514|||http://purl.uniprot.org/annotation/VAR_061240|||http://purl.uniprot.org/annotation/VSP_013931
http://togogenome.org/gene/9606:NDST3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95803                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3|||Cytoplasmic|||For sulfotransferase activity|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate N-deacetylase 3|||Heparan sulfate N-sulfotransferase 3|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225659|||http://purl.uniprot.org/annotation/VAR_036131|||http://purl.uniprot.org/annotation/VSP_017405|||http://purl.uniprot.org/annotation/VSP_017406|||http://purl.uniprot.org/annotation/VSP_054350|||http://purl.uniprot.org/annotation/VSP_054351|||http://purl.uniprot.org/annotation/VSP_054352
http://togogenome.org/gene/9606:TMEM89                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUT3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Transmembrane protein 89                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290067|||http://purl.uniprot.org/annotation/VAR_051450
http://togogenome.org/gene/9606:H2AB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C5Z0                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||Docking domain|||Histone H2A-Bbd type 2/3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055321
http://togogenome.org/gene/9606:SAMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6K7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||SAM|||Sterile alpha motif domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279496|||http://purl.uniprot.org/annotation/VAR_030910|||http://purl.uniprot.org/annotation/VAR_069418|||http://purl.uniprot.org/annotation/VSP_023459|||http://purl.uniprot.org/annotation/VSP_023460|||http://purl.uniprot.org/annotation/VSP_055738
http://togogenome.org/gene/9606:ACTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSZ2|||http://purl.uniprot.org/uniprot/B4DZQ2|||http://purl.uniprot.org/uniprot/Q08043                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Alpha-actinin-3|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||N-acetylmethionine|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073438|||http://purl.uniprot.org/annotation/VAR_012705|||http://purl.uniprot.org/annotation/VAR_033488|||http://purl.uniprot.org/annotation/VAR_047528|||http://purl.uniprot.org/annotation/VAR_047529|||http://purl.uniprot.org/annotation/VAR_080044
http://togogenome.org/gene/9606:KLHL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K364|||http://purl.uniprot.org/uniprot/Q8IXQ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BACK|||BTB|||In PERCHING; subcellular localization in punctate structures at the perinuclear region of cytoplasm is similar to wild-type and colocalized with CUL3.|||In RP42.|||In RP42; impairs interaction with CUL3 and ubiquitin ligase activity of the BCR(KLHL7) complex.|||In a patient with retinitis pigmentosa; uncertain pathological significance.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228988|||http://purl.uniprot.org/annotation/VAR_060672|||http://purl.uniprot.org/annotation/VAR_060673|||http://purl.uniprot.org/annotation/VAR_060674|||http://purl.uniprot.org/annotation/VAR_060675|||http://purl.uniprot.org/annotation/VAR_060676|||http://purl.uniprot.org/annotation/VAR_060677|||http://purl.uniprot.org/annotation/VAR_077161|||http://purl.uniprot.org/annotation/VAR_077162|||http://purl.uniprot.org/annotation/VAR_077163|||http://purl.uniprot.org/annotation/VAR_082842|||http://purl.uniprot.org/annotation/VSP_038416|||http://purl.uniprot.org/annotation/VSP_038417|||http://purl.uniprot.org/annotation/VSP_038418|||http://purl.uniprot.org/annotation/VSP_046974
http://togogenome.org/gene/9606:HS3ST3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y663                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  17% loss of enzymatic activity.|||23.3% loss of enzymatic activity.|||32% loss of enzymatic activity.|||33.6% loss of enzymatic activity.|||43% loss of enzymatic activity.|||44.1% loss of enzymatic activity.|||47.6% loss of enzymatic activity.|||48.3% loss of enzymatic activity.|||65% loss of enzymatic activity.|||99.1% loss of enzymatic activity.|||99.2% loss of enzymatic activity.|||99.5% loss of enzymatic activity.|||99.6% loss of enzymatic activity.|||99.6% loss of enzymatic activity; no HSV1 entry activity.|||99.8% loss of enzymatic activity.|||99.9% loss of enzymatic activity.|||Abolishes enzymatic activity.|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Heparan sulfate glucosamine 3-O-sulfotransferase 3A1|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on enzymatic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085217
http://togogenome.org/gene/9606:SAXO4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3F4G3|||http://purl.uniprot.org/uniprot/Q7Z5V6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Stabilizer of axonemal microtubules 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274377|||http://purl.uniprot.org/annotation/VAR_030271|||http://purl.uniprot.org/annotation/VAR_030272|||http://purl.uniprot.org/annotation/VSP_022731
http://togogenome.org/gene/9606:OTUD6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0W9|||http://purl.uniprot.org/uniprot/Q8N6M0                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes the deubiquitinating enzyme activity.|||Cys-loop|||Deubiquitinase OTUD6B|||His-loop|||In IDDFSDA.|||In IDDFSDA; unknown pathological significance.|||In isoform 2.|||N-acetylmethionine|||Nucleophile|||OTU|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076279|||http://purl.uniprot.org/annotation/VAR_034144|||http://purl.uniprot.org/annotation/VAR_080403|||http://purl.uniprot.org/annotation/VAR_080404|||http://purl.uniprot.org/annotation/VSP_055378
http://togogenome.org/gene/9606:PLVAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX97                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In DIAR10.|||In DIAR10; the protein is not expressed in the patient biopsy tissues.|||N-linked (GlcNAc...) asparagine|||Plasmalemma vesicle-associated protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058462|||http://purl.uniprot.org/annotation/VAR_081738|||http://purl.uniprot.org/annotation/VAR_081739|||http://purl.uniprot.org/annotation/VAR_081740
http://togogenome.org/gene/9606:PLAAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53816                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Cytoplasmic|||Helical|||Induces a major structural rearrangement accompanied by domain-swapping dimerization and changes in substrate-specificity.|||LRAT|||Lumenal|||No effect on PPP2R1A-binding.|||No effect on PPP2R1A-binding. Impaired ability to act as a host factor for picornaviruses.|||Phospholipase A and acyltransferase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152484
http://togogenome.org/gene/9606:GDPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6W3E5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GP-PDE|||Glycerophosphodiester phosphodiesterase domain-containing protein 4|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251938|||http://purl.uniprot.org/annotation/VAR_055872|||http://purl.uniprot.org/annotation/VAR_055873|||http://purl.uniprot.org/annotation/VAR_055874|||http://purl.uniprot.org/annotation/VAR_064764|||http://purl.uniprot.org/annotation/VSP_020811|||http://purl.uniprot.org/annotation/VSP_020812
http://togogenome.org/gene/9606:DENND4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZ89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DENN domain-containing protein 4C|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 5.|||MABP|||PPR|||Phosphoserine|||Phosphothreonine|||Polar residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089697|||http://purl.uniprot.org/annotation/VAR_022891|||http://purl.uniprot.org/annotation/VAR_022892|||http://purl.uniprot.org/annotation/VAR_061640|||http://purl.uniprot.org/annotation/VSP_027379|||http://purl.uniprot.org/annotation/VSP_027382|||http://purl.uniprot.org/annotation/VSP_027383|||http://purl.uniprot.org/annotation/VSP_027384|||http://purl.uniprot.org/annotation/VSP_027386
http://togogenome.org/gene/9606:WIPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Phosphoserine|||Polar residues|||Pro residues|||Profilin-binding motif|||RLRK|||WAS/WASL-interacting protein family member 3|||WASP-binding motif|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337997|||http://purl.uniprot.org/annotation/VAR_043729
http://togogenome.org/gene/9606:BBS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZW61                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Associated with H-263 in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10.|||Associated with S-119 in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10.|||Bardet-Biedl syndrome 12 protein|||In BBS12.|||In BBS12; significantly reduces the interaction with MKKS; shows significantly decreased interaction with BBS7; the interaction with BBS10 is not affected by this mutation.|||In BBS12; unknown pathological significance.|||In BBS12; unknown pathological significance; significantly reduces the interaction with MKKS; the interaction with BBS10 is not affected by this mutation.|||In a patient with Bardet-Biedl syndrome compound heterozygote for BBS2 mutations; unknown pathological significance.|||In a patient with Bardet-Biedl syndrome homozygous for a mutation in BBS2; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301981|||http://purl.uniprot.org/annotation/VAR_034919|||http://purl.uniprot.org/annotation/VAR_034920|||http://purl.uniprot.org/annotation/VAR_034921|||http://purl.uniprot.org/annotation/VAR_034922|||http://purl.uniprot.org/annotation/VAR_034923|||http://purl.uniprot.org/annotation/VAR_034924|||http://purl.uniprot.org/annotation/VAR_034925|||http://purl.uniprot.org/annotation/VAR_034926|||http://purl.uniprot.org/annotation/VAR_034927|||http://purl.uniprot.org/annotation/VAR_034928|||http://purl.uniprot.org/annotation/VAR_034929|||http://purl.uniprot.org/annotation/VAR_034930|||http://purl.uniprot.org/annotation/VAR_034931|||http://purl.uniprot.org/annotation/VAR_034932|||http://purl.uniprot.org/annotation/VAR_034933|||http://purl.uniprot.org/annotation/VAR_062964|||http://purl.uniprot.org/annotation/VAR_062965|||http://purl.uniprot.org/annotation/VAR_066266|||http://purl.uniprot.org/annotation/VAR_066267|||http://purl.uniprot.org/annotation/VAR_066268|||http://purl.uniprot.org/annotation/VAR_066269|||http://purl.uniprot.org/annotation/VAR_066270|||http://purl.uniprot.org/annotation/VAR_066271|||http://purl.uniprot.org/annotation/VAR_066272|||http://purl.uniprot.org/annotation/VAR_066273|||http://purl.uniprot.org/annotation/VAR_066274|||http://purl.uniprot.org/annotation/VAR_066275|||http://purl.uniprot.org/annotation/VAR_066276|||http://purl.uniprot.org/annotation/VAR_066277
http://togogenome.org/gene/9606:SLC5A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJK1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium/mannose cotransporter SLC5A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311211|||http://purl.uniprot.org/annotation/VAR_052493|||http://purl.uniprot.org/annotation/VSP_029416|||http://purl.uniprot.org/annotation/VSP_029417|||http://purl.uniprot.org/annotation/VSP_029418|||http://purl.uniprot.org/annotation/VSP_029419|||http://purl.uniprot.org/annotation/VSP_045061
http://togogenome.org/gene/9606:PNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00491|||http://purl.uniprot.org/uniprot/V9HWH6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Important for substrate specificity|||In PNPD.|||N-acetylmethionine|||Nucleoside phosphorylase|||Phosphoserine|||Purine nucleoside phosphorylase|||Reduces catalytic activity towards inosine, hypoxanthine, guanosine and guanine. Increases catalytic activity towards adenosine and adenine.|||Reduces catalytic activity towards inosine.|||Reduces catalytic activity.|||Severe loss of catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184536|||http://purl.uniprot.org/annotation/VAR_002243|||http://purl.uniprot.org/annotation/VAR_002244|||http://purl.uniprot.org/annotation/VAR_002245|||http://purl.uniprot.org/annotation/VAR_002246|||http://purl.uniprot.org/annotation/VAR_002247|||http://purl.uniprot.org/annotation/VAR_010653
http://togogenome.org/gene/9606:TMEM160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX00                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Mitochondrion|||Phosphoserine|||Transmembrane protein 160                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277810|||http://purl.uniprot.org/annotation/VAR_030600
http://togogenome.org/gene/9606:PTOV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGR2|||http://purl.uniprot.org/uniprot/Q86YD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Interaction with FLOT1|||Mediator complex subunit Med25 PTOV|||Phosphoserine|||Polar residues|||Prostate tumor-overexpressed gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304965|||http://purl.uniprot.org/annotation/VSP_028153|||http://purl.uniprot.org/annotation/VSP_028154|||http://purl.uniprot.org/annotation/VSP_028155|||http://purl.uniprot.org/annotation/VSP_028156
http://togogenome.org/gene/9606:TULP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1E7|||http://purl.uniprot.org/uniprot/O75386                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In HRCDF.|||In HRCDF; almost complete loss of ciliary localization.|||In HRCDF; unknown pathological significance.|||In TULP3KR; abolishes phosphoinositide binding and impairs localization to cilia. Still associates with the IFT complex A (IFT-A).|||In isoform 2.|||In isoform 3.|||In mut12; abolishes association with the IFT complex A (IFT-A) without affecting phosphoinositide binding. Impaired localization to cilia.|||Polar residues|||Required for association with the IFT complex A (IFT-A)|||Tubby C-terminal|||Tubby-related protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186470|||http://purl.uniprot.org/annotation/VAR_087378|||http://purl.uniprot.org/annotation/VAR_087379|||http://purl.uniprot.org/annotation/VAR_087380|||http://purl.uniprot.org/annotation/VSP_054752|||http://purl.uniprot.org/annotation/VSP_055761|||http://purl.uniprot.org/annotation/VSP_055762|||http://purl.uniprot.org/annotation/VSP_055763
http://togogenome.org/gene/9606:ERLIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75477                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Erlin-1|||Helical|||In SPG62.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002784|||http://purl.uniprot.org/annotation/VAR_077847
http://togogenome.org/gene/9606:ZNF816                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VGE8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 816                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294362|||http://purl.uniprot.org/annotation/VAR_033165|||http://purl.uniprot.org/annotation/VAR_033166
http://togogenome.org/gene/9606:MON2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A286YFF8|||http://purl.uniprot.org/uniprot/B7ZM73|||http://purl.uniprot.org/uniprot/Q7Z3U7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 6.|||Mon2 C-terminal|||Mon2/Sec7/BIG1-like HDS|||Mon2/Sec7/BIG1-like HUS|||Mon2/Sec7/BIG1-like dimerisation and cyclophilin-binding|||N-acetylserine|||Phosphoserine|||Protein MON2 homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297902|||http://purl.uniprot.org/annotation/VAR_034689|||http://purl.uniprot.org/annotation/VSP_027389|||http://purl.uniprot.org/annotation/VSP_027390|||http://purl.uniprot.org/annotation/VSP_027391|||http://purl.uniprot.org/annotation/VSP_027392|||http://purl.uniprot.org/annotation/VSP_027393|||http://purl.uniprot.org/annotation/VSP_055628
http://togogenome.org/gene/9606:ZFP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 3 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233713
http://togogenome.org/gene/9606:TMPRSS11E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UL52                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Interchain (between non-catalytic and catalytic chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||SEA|||Transmembrane protease serine 11E catalytic chain|||Transmembrane protease serine 11E non-catalytic chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027891|||http://purl.uniprot.org/annotation/PRO_0000027892|||http://purl.uniprot.org/annotation/VAR_051847
http://togogenome.org/gene/9606:DMRT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQL9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DM|||DMA|||Disordered|||Doublesex- and mab-3-related transcription factor 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277794|||http://purl.uniprot.org/annotation/VAR_030591|||http://purl.uniprot.org/annotation/VAR_030592|||http://purl.uniprot.org/annotation/VAR_030593
http://togogenome.org/gene/9606:NEURL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DS86|||http://purl.uniprot.org/uniprot/O76050                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase NEURL1|||In isoform 2.|||N-myristoyl glycine|||NHR 1|||NHR 2|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181255|||http://purl.uniprot.org/annotation/VSP_013151
http://togogenome.org/gene/9606:TCHH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07283                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1-1; approximate|||1-2; approximate|||1-3; approximate|||1-4|||1-5|||10 X 30 AA tandem repeats|||2-1|||2-2|||2-3|||2-4|||2-5|||2-6|||2-7|||2-8|||23 X 26 AA approximate tandem repeats|||4-1|||4-10|||4-2|||4-3|||4-4|||4-5|||4-6|||4-7|||4-8|||4-9|||5 X 13 AA tandem repeats of R-R-E-Q-E-E-E-R-R-E-Q-Q-L|||8 X 6 AA tandem repeats of R-R-E-Q-Q-L|||9 X 28 AA approximate tandem repeats|||Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||Found in a renal cell carcinoma sample; somatic mutation.|||S-100-like|||Trichohyalin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144042|||http://purl.uniprot.org/annotation/VAR_047519|||http://purl.uniprot.org/annotation/VAR_047520|||http://purl.uniprot.org/annotation/VAR_047521|||http://purl.uniprot.org/annotation/VAR_047522|||http://purl.uniprot.org/annotation/VAR_047523|||http://purl.uniprot.org/annotation/VAR_047524|||http://purl.uniprot.org/annotation/VAR_064757
http://togogenome.org/gene/9606:IL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14116                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding of the preformed binary complex of IL18 and IL18R1 to IL18RAP.|||Impairs binding to IL18R1 and the ability to induce IFNG production.|||In isoform 2.|||Interleukin-18|||Reduces binding of the preformed binary complex of IL18 and IL18R1 to IL18RAP resulting in impaired IFNG production.|||Reduces binding of the preformed binary complex of IL18 and IL18R1 to IL18RAP.|||Reduces binding to IL18R1 and the ability to induce IFNG production.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015343|||http://purl.uniprot.org/annotation/PRO_0000015344|||http://purl.uniprot.org/annotation/VSP_044934
http://togogenome.org/gene/9606:SETD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBK2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes automethylation. Impairs the methyltransferase activity toward RELA and PAK4; when associated with Arg-39.|||Abolishes methyltransferase activity. Greatly decreases the stability of monomeric, homodimeric and homotrimeric structures.|||Decreases the methyltransferase activity toward RELA.|||Greatly decreases automethylation. Impairs the methyltransferase activity toward RELA and PAK4; when associated with Arg-179.|||Has little effect on automethylation level.|||Impairs the methyltransferase activity toward RELA.|||In isoform 2.|||N-lysine methyltransferase SETD6|||N6-methylated lysine; by autocatalysis|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281889|||http://purl.uniprot.org/annotation/VAR_064590|||http://purl.uniprot.org/annotation/VAR_064591|||http://purl.uniprot.org/annotation/VAR_064592|||http://purl.uniprot.org/annotation/VAR_064593|||http://purl.uniprot.org/annotation/VAR_064594|||http://purl.uniprot.org/annotation/VSP_024093
http://togogenome.org/gene/9606:IMPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14732                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Inositol monophosphatase 2|||Loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142520|||http://purl.uniprot.org/annotation/VAR_049601|||http://purl.uniprot.org/annotation/VSP_013674
http://togogenome.org/gene/9606:CCDC88C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZB8|||http://purl.uniprot.org/uniprot/Q9P219                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with and activation of GNAI3 and abolishes release of the beta and gamma subunits from the heterotrimeric G-protein complex. Abolishes WNT5A-mediated activation of RAC1. Failure to induce apical cell constriction but does not affect localization to apical cell junctions.|||Basic and acidic residues|||Calponin-homology (CH)|||DVL1-binding|||Disordered|||Failure to localize to apical cell junctions and to induce apical cell constriction.|||GBA|||In SCA40; no effect on subcellular location; increases activation of the JNK signaling pathway; induces apoptosis.|||In isoform 2.|||In isoform 3.|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein Daple                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286864|||http://purl.uniprot.org/annotation/VAR_046613|||http://purl.uniprot.org/annotation/VAR_046614|||http://purl.uniprot.org/annotation/VAR_046615|||http://purl.uniprot.org/annotation/VAR_057777|||http://purl.uniprot.org/annotation/VAR_071981|||http://purl.uniprot.org/annotation/VSP_052389|||http://purl.uniprot.org/annotation/VSP_052390|||http://purl.uniprot.org/annotation/VSP_052391|||http://purl.uniprot.org/annotation/VSP_052392
http://togogenome.org/gene/9606:NOL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8H0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N6-methyllysine|||Nucleolar protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096931|||http://purl.uniprot.org/annotation/VAR_051237|||http://purl.uniprot.org/annotation/VSP_053283|||http://purl.uniprot.org/annotation/VSP_053284
http://togogenome.org/gene/9606:ADGRG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVW2|||http://purl.uniprot.org/uniprot/F8W8F7|||http://purl.uniprot.org/uniprot/Q86Y34                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor G3|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012889|||http://purl.uniprot.org/annotation/VAR_055927
http://togogenome.org/gene/9606:NKRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A3F769|||http://purl.uniprot.org/uniprot/O15226                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with DHX15.|||Active repression domain|||Basic and acidic residues|||Decreased, but not abolished interaction, with DHX15.|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||NF-kappa-B-repressing factor|||Nuclear localization signal|||Phosphoserine|||Polar residues|||R3H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096869|||http://purl.uniprot.org/annotation/VSP_047377
http://togogenome.org/gene/9606:KRTAP3-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Region|||Repeat                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 5 AA repeats of C-C-X(3)|||Keratin-associated protein 3-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185163
http://togogenome.org/gene/9606:WNT10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00744                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Associated with obesity; abrogates the ability of WNT10B to activate canonical Wnt signaling and blocks adipogenesis.|||Disordered|||In SHFM6.|||In STHAG8; reduced activation of Wnt signaling; reduced endothelial differentiation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Phosphothreonine|||Protein Wnt-10b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041463|||http://purl.uniprot.org/annotation/VAR_062512|||http://purl.uniprot.org/annotation/VAR_062513|||http://purl.uniprot.org/annotation/VAR_062514|||http://purl.uniprot.org/annotation/VAR_062515|||http://purl.uniprot.org/annotation/VAR_062516|||http://purl.uniprot.org/annotation/VAR_076926|||http://purl.uniprot.org/annotation/VSP_056289|||http://purl.uniprot.org/annotation/VSP_056290
http://togogenome.org/gene/9606:OR52E6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVK5|||http://purl.uniprot.org/uniprot/Q96RD3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52E6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150775|||http://purl.uniprot.org/annotation/VAR_048066|||http://purl.uniprot.org/annotation/VAR_048067|||http://purl.uniprot.org/annotation/VAR_048068|||http://purl.uniprot.org/annotation/VAR_048069|||http://purl.uniprot.org/annotation/VAR_048070|||http://purl.uniprot.org/annotation/VAR_048071|||http://purl.uniprot.org/annotation/VAR_048072|||http://purl.uniprot.org/annotation/VAR_048073
http://togogenome.org/gene/9606:SNX30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VWJ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  BAR|||Disordered|||PX|||Phosphoserine|||Phosphothreonine|||Sorting nexin-30                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284533|||http://purl.uniprot.org/annotation/VAR_031771|||http://purl.uniprot.org/annotation/VAR_052483
http://togogenome.org/gene/9606:CNBD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G141|||http://purl.uniprot.org/uniprot/Q96M20                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclic nucleotide-binding domain-containing protein 2|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079471|||http://purl.uniprot.org/annotation/VAR_056853|||http://purl.uniprot.org/annotation/VAR_056854|||http://purl.uniprot.org/annotation/VAR_056855|||http://purl.uniprot.org/annotation/VSP_039149|||http://purl.uniprot.org/annotation/VSP_043858
http://togogenome.org/gene/9606:TRIB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RU8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  COP1-binding|||Decreased interaction with COP1.|||Disordered|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2.|||Loss of interaction with COP1.|||No effect on interaction with COP1.|||Pro residues|||Protein kinase|||Strongly decreased interaction with COP1.|||Tribbles homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131859|||http://purl.uniprot.org/annotation/VAR_042364|||http://purl.uniprot.org/annotation/VAR_042365|||http://purl.uniprot.org/annotation/VAR_042366|||http://purl.uniprot.org/annotation/VAR_042367|||http://purl.uniprot.org/annotation/VAR_042368|||http://purl.uniprot.org/annotation/VAR_042369|||http://purl.uniprot.org/annotation/VAR_042370|||http://purl.uniprot.org/annotation/VSP_054894
http://togogenome.org/gene/9606:AKR1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15121                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member B1|||Complete loss of glyceraldehyde oxidoreductase activity.|||Lowers pKa of active site Tyr|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Proton donor|||Reduced glyceraldehyde oxidoreductase activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124623|||http://purl.uniprot.org/annotation/VAR_014743|||http://purl.uniprot.org/annotation/VAR_014744|||http://purl.uniprot.org/annotation/VAR_014745|||http://purl.uniprot.org/annotation/VAR_014746|||http://purl.uniprot.org/annotation/VAR_014747|||http://purl.uniprot.org/annotation/VAR_048213
http://togogenome.org/gene/9606:TMEM185A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4G6|||http://purl.uniprot.org/uniprot/E7EMM1|||http://purl.uniprot.org/uniprot/Q8NFB2|||http://purl.uniprot.org/uniprot/Q8TCB3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mediates interaction with MAP1B|||Transmembrane protein 185A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188007|||http://purl.uniprot.org/annotation/PRO_5004313947|||http://purl.uniprot.org/annotation/VAR_033922|||http://purl.uniprot.org/annotation/VAR_033923
http://togogenome.org/gene/9606:ATG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NT62                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Caspase cleavage motif LETD|||Cleavage; by CASP8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)|||Glycyl thioester intermediate|||In isoform 2.|||Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate), a stable complex with an O-ester bond is formed.|||N-acetylmethionine|||Ubiquitin-like-conjugating enzyme ATG3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213569|||http://purl.uniprot.org/annotation/VSP_013037
http://togogenome.org/gene/9606:LDLRAD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V575|||http://purl.uniprot.org/uniprot/A8K6A9|||http://purl.uniprot.org/uniprot/O15165                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 8.|||In isoform Alpha-2, isoform Beta-2 and isoform 7.|||In isoform Beta-1 and isoform Beta-2.|||LDL-receptor class A|||Low-density lipoprotein receptor class A domain-containing protein 4|||Lumenal|||PPxY motif 1|||PPxY motif 2|||SMAD interaction motif (SIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185444|||http://purl.uniprot.org/annotation/VSP_006439|||http://purl.uniprot.org/annotation/VSP_006440|||http://purl.uniprot.org/annotation/VSP_013901|||http://purl.uniprot.org/annotation/VSP_043253|||http://purl.uniprot.org/annotation/VSP_054772
http://togogenome.org/gene/9606:H2BC21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16778                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 2-E|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071835
http://togogenome.org/gene/9606:FLT3LG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLY4|||http://purl.uniprot.org/uniprot/P49771                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fms-related tyrosine kinase 3 ligand|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021281|||http://purl.uniprot.org/annotation/PRO_5002864110|||http://purl.uniprot.org/annotation/VSP_004251|||http://purl.uniprot.org/annotation/VSP_004252|||http://purl.uniprot.org/annotation/VSP_054599
http://togogenome.org/gene/9606:PRKAR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31321                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Dimerization and phosphorylation|||Disordered|||In MASNS; decreased basal PKA enzymatic activity in lysates from transfected cells.|||In MASNS; unknown pathological significance; requires 2 nucleotide substitutions; decreased basal PKA enzymatic activity in lysates from transfected cells.|||Interchain (with C-18)|||Interchain (with C-39)|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pseudophosphorylation motif|||Removed|||cAMP-dependent protein kinase type I-beta regulatory subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205381|||http://purl.uniprot.org/annotation/VAR_086687|||http://purl.uniprot.org/annotation/VAR_086688|||http://purl.uniprot.org/annotation/VAR_086689
http://togogenome.org/gene/9606:OR2T35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGX2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150509
http://togogenome.org/gene/9606:WDR83OS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y284                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylserine|||PAT complex subunit Asterix|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071605|||http://purl.uniprot.org/annotation/VAR_052498
http://togogenome.org/gene/9606:RNF44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L0R7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||RING finger protein 44|||RING-type; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273413|||http://purl.uniprot.org/annotation/VSP_055432
http://togogenome.org/gene/9606:CDK5RAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z592|||http://purl.uniprot.org/uniprot/A0A0S2Z5J9|||http://purl.uniprot.org/uniprot/Q53H36|||http://purl.uniprot.org/uniprot/Q96SZ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Loss of mitochondrial tRNAs methylthiotransferase activity; when associated with A-258 and A-262.|||Loss of mitochondrial tRNAs methylthiotransferase activity; when associated with A-258 and A-265.|||Loss of mitochondrial tRNAs methylthiotransferase activity; when associated with A-262 and A-265.|||MTTase N-terminal|||Mitochondrial tRNA methylthiotransferase CDK5RAP1|||Mitochondrion|||Radical SAM core|||TRAM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141764|||http://purl.uniprot.org/annotation/VSP_007560|||http://purl.uniprot.org/annotation/VSP_007561|||http://purl.uniprot.org/annotation/VSP_007562|||http://purl.uniprot.org/annotation/VSP_047799|||http://purl.uniprot.org/annotation/VSP_047800|||http://purl.uniprot.org/annotation/VSP_047801|||http://purl.uniprot.org/annotation/VSP_047802
http://togogenome.org/gene/9606:ND4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03901|||http://purl.uniprot.org/uniprot/Q7GXZ4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In LHON; possible rare primary mutation.|||In colorectal cancer.|||NADH-ubiquinone oxidoreductase chain 4L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118431|||http://purl.uniprot.org/annotation/VAR_008397|||http://purl.uniprot.org/annotation/VAR_008496|||http://purl.uniprot.org/annotation/VAR_008605|||http://purl.uniprot.org/annotation/VAR_008606|||http://purl.uniprot.org/annotation/VAR_008607
http://togogenome.org/gene/9606:TCHP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Decreased ubiquitination. Negative effect on ubiquitination is higher when associated with R-50.|||Decreased ubiquitination. Negative effect on ubiquitination is higher when associated with R-57.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In a gastric carcinoma sample.|||In a pancreatic carcinoma sample.|||Interaction with keratin proteins|||Trichohyalin/plectin homology domain|||Trichoplein keratin filament-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292609|||http://purl.uniprot.org/annotation/VAR_053924|||http://purl.uniprot.org/annotation/VAR_053925|||http://purl.uniprot.org/annotation/VAR_064056|||http://purl.uniprot.org/annotation/VAR_064057
http://togogenome.org/gene/9606:MEPCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L2J0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  7SK snRNA methylphosphate capping enzyme|||Abolished methyltransferase activity and reduced interaction with LARP7, without affecting interaction with P-TEFb.|||Basic residues|||Bin3-type SAM|||Decreased methyltransferase activity.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Nearly abolished methyltransferase activity.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Strongly reduced methyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289262|||http://purl.uniprot.org/annotation/VSP_044512
http://togogenome.org/gene/9606:RFPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75679                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||In isoform 2.|||RING-type|||Ret finger protein-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056032|||http://purl.uniprot.org/annotation/VAR_052091|||http://purl.uniprot.org/annotation/VAR_052092|||http://purl.uniprot.org/annotation/VAR_052093|||http://purl.uniprot.org/annotation/VAR_059814|||http://purl.uniprot.org/annotation/VSP_045651
http://togogenome.org/gene/9606:CHMP4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY43                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with PDCD6IP.|||Charged multivesicular body protein 4a|||Disordered|||In isoform 2.|||Interaction with phosphoinosides|||Intramolecular interaction with C-terminus|||Intramolecular interaction with N-terminus|||Membrane association; releases autoinhibition.|||Phosphoserine|||Reduces interaction with PDCD6IP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211488|||http://purl.uniprot.org/annotation/VAR_023384|||http://purl.uniprot.org/annotation/VSP_056264
http://togogenome.org/gene/9606:SNX16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57768                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes binding to membranes enriched in phosphatidylinositol 3-phosphate.|||Abolishes binding to phosphatidylinositol 3-phosphate.|||Disordered|||In isoform 2.|||PX|||Phosphoserine|||Polar residues|||Sorting nexin-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213863|||http://purl.uniprot.org/annotation/VAR_052479|||http://purl.uniprot.org/annotation/VSP_042944
http://togogenome.org/gene/9606:DYNLT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZS6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Dynein light chain Tctex-type protein 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328728|||http://purl.uniprot.org/annotation/VAR_042499|||http://purl.uniprot.org/annotation/VAR_042500|||http://purl.uniprot.org/annotation/VAR_042501
http://togogenome.org/gene/9606:GNRH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01148                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Peptide|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Appears to be essential for biological activity|||Cleavage; by ACE|||Glycine amide|||GnRH-associated peptide 1|||Gonadoliberin-1|||In HH12; uncertain pathological significance; the patient also carries mutations in PROKR2 and FGFR1.|||Progonadoliberin-1|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012395|||http://purl.uniprot.org/annotation/PRO_0000012396|||http://purl.uniprot.org/annotation/PRO_0000012397|||http://purl.uniprot.org/annotation/VAR_013943|||http://purl.uniprot.org/annotation/VAR_069966
http://togogenome.org/gene/9606:RSPH10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RC85|||http://purl.uniprot.org/uniprot/P0C881                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||MORN 1|||MORN 10|||MORN 2|||MORN 3|||MORN 4|||MORN 5|||MORN 6|||MORN 7|||MORN 8|||MORN 9|||Polar residues|||Radial spoke head 10 homolog B|||Radial spoke head 10 homolog B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311943|||http://purl.uniprot.org/annotation/PRO_0000349254|||http://purl.uniprot.org/annotation/VAR_037357|||http://purl.uniprot.org/annotation/VSP_035277|||http://purl.uniprot.org/annotation/VSP_035278|||http://purl.uniprot.org/annotation/VSP_035279
http://togogenome.org/gene/9606:CRHBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24387                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Corticotropin-releasing factor-binding protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020994
http://togogenome.org/gene/9606:OBP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPH6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform Bb.|||In isoform Bg.|||Odorant-binding protein 2b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017938|||http://purl.uniprot.org/annotation/VAR_050177|||http://purl.uniprot.org/annotation/VSP_003138|||http://purl.uniprot.org/annotation/VSP_003139
http://togogenome.org/gene/9606:C2orf88                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSF0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Loss of plasma membrane localization.|||N-myristoyl glycine|||PKA-RI-binding|||Phosphoserine|||Removed|||S-palmitoyl cysteine|||Small membrane A-kinase anchor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348430|||http://purl.uniprot.org/annotation/VAR_046151
http://togogenome.org/gene/9606:FAM78A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JUQ0|||http://purl.uniprot.org/uniprot/Q8N2W3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Non-terminal Residue                                                                                  ^@                                                                                  Chain|||Non-terminal Residue                                                                                  ^@                                                                                  Protein FAM78A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265112
http://togogenome.org/gene/9606:MRPS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2R9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In COXPD34; results in decreased mitochondrial protein synthesis and reduced levels of respiratory complexes; MRPS7 mRNA and protein levels are reduced.|||Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein uS7m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273056|||http://purl.uniprot.org/annotation/VAR_030076|||http://purl.uniprot.org/annotation/VAR_080411
http://togogenome.org/gene/9606:SH2D1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14796                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||No stimulation of granule polarization during NK-mediated cytotoxicity, abolishes activation of CD244/2B4-mediated cytotoxicity, abolishes augmentation of CD244/2B4-triggered PLCG1 phosphorylation and ERK activation.|||Phosphotyrosine|||SH2|||SH2 domain-containing protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097724|||http://purl.uniprot.org/annotation/VAR_051347|||http://purl.uniprot.org/annotation/VAR_051348|||http://purl.uniprot.org/annotation/VSP_010341
http://togogenome.org/gene/9606:TCEANC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MN5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylmethionine|||TFIIS N-terminal|||TFIIS central|||Transcription elongation factor A N-terminal and central domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286574|||http://purl.uniprot.org/annotation/VSP_025096
http://togogenome.org/gene/9606:TYK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29597                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of catalytic activity.|||Disordered|||Does not affect phosphorylation state and enzymatic activity.|||FERM|||In a colorectal adenocarcinoma sample; somatic mutation.|||Non-receptor tyrosine-protein kinase TYK2|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase 1|||Protein kinase 2|||Proton acceptor|||Reduces basal catalytic activity and abolishes IFN-dependent activation.|||SH2; atypical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088177|||http://purl.uniprot.org/annotation/VAR_020286|||http://purl.uniprot.org/annotation/VAR_020597|||http://purl.uniprot.org/annotation/VAR_020598|||http://purl.uniprot.org/annotation/VAR_020599|||http://purl.uniprot.org/annotation/VAR_020600|||http://purl.uniprot.org/annotation/VAR_037797|||http://purl.uniprot.org/annotation/VAR_037798|||http://purl.uniprot.org/annotation/VAR_037799|||http://purl.uniprot.org/annotation/VAR_041870|||http://purl.uniprot.org/annotation/VAR_041871|||http://purl.uniprot.org/annotation/VAR_041872|||http://purl.uniprot.org/annotation/VAR_041873|||http://purl.uniprot.org/annotation/VAR_041874|||http://purl.uniprot.org/annotation/VAR_041875
http://togogenome.org/gene/9606:APOL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AH95|||http://purl.uniprot.org/uniprot/O14791|||http://purl.uniprot.org/uniprot/Q2KHQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Apolipoprotein L1|||Disordered|||In FSGS4.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002040|||http://purl.uniprot.org/annotation/PRO_5014084694|||http://purl.uniprot.org/annotation/PRO_5014308663|||http://purl.uniprot.org/annotation/VAR_011383|||http://purl.uniprot.org/annotation/VAR_011384|||http://purl.uniprot.org/annotation/VAR_011385|||http://purl.uniprot.org/annotation/VAR_036568|||http://purl.uniprot.org/annotation/VAR_046641|||http://purl.uniprot.org/annotation/VAR_061995|||http://purl.uniprot.org/annotation/VAR_063598|||http://purl.uniprot.org/annotation/VSP_000292|||http://purl.uniprot.org/annotation/VSP_045077
http://togogenome.org/gene/9606:PDE6H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13956                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Polar residues|||Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166120
http://togogenome.org/gene/9606:RPL36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3U8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Large ribosomal subunit protein eL36|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195007|||http://purl.uniprot.org/annotation/VAR_051804
http://togogenome.org/gene/9606:DPP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TI2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished dipeptidyl peptidase activity and ability to sequester NLRP1 and inhibit pyroptosis.|||Charge relay system|||Dipeptidyl peptidase 9|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Reduced interaction with CARD8 without affecting the peptidase activity.|||Reduced interaction with NLRP1 and CARD8 without affecting the peptidase activity.|||Reduced interaction with NLRP1 without affecting the peptidase activity.|||Removed|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122415|||http://purl.uniprot.org/annotation/VSP_013865|||http://purl.uniprot.org/annotation/VSP_013869
http://togogenome.org/gene/9606:ZGPAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5X3|||http://purl.uniprot.org/uniprot/Q8N5A5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||G-patch|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||Zinc finger CCCH-type with G patch domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213894|||http://purl.uniprot.org/annotation/VAR_025539|||http://purl.uniprot.org/annotation/VSP_007754|||http://purl.uniprot.org/annotation/VSP_038121|||http://purl.uniprot.org/annotation/VSP_053599
http://togogenome.org/gene/9606:BUD31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41223                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interaction with AR|||N6-acetyllysine|||Nuclear localization signal|||Protein BUD31 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193897|||http://purl.uniprot.org/annotation/VSP_055558
http://togogenome.org/gene/9606:KCNG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAE7                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In isoform 2.|||Potassium voltage-gated channel subfamily G member 3|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054077|||http://purl.uniprot.org/annotation/VSP_001026
http://togogenome.org/gene/9606:SRP68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHB9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with SRP72.|||Loss of interaction with SRP72. Diminished localization to endoplasmic reticulum.|||Loss of interaction with SRP72; when associated with A-56 in SRP72.|||N6-acetyllysine|||Phosphoserine|||RNA-binding|||Reduced interaction with SRP72.|||Required for interaction with SRP72|||Signal recognition particle subunit SRP68                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135227|||http://purl.uniprot.org/annotation/VSP_008347|||http://purl.uniprot.org/annotation/VSP_045132|||http://purl.uniprot.org/annotation/VSP_046944
http://togogenome.org/gene/9606:CREB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02930                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic motif|||Basic residues|||C2H2-type|||Cyclic AMP-responsive element-binding protein 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Leucine-zipper|||Phosphoserine|||Phosphothreonine|||Polar residues|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076604|||http://purl.uniprot.org/annotation/VSP_050010|||http://purl.uniprot.org/annotation/VSP_050011|||http://purl.uniprot.org/annotation/VSP_050012|||http://purl.uniprot.org/annotation/VSP_050013
http://togogenome.org/gene/9606:AS3MT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBK9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Arsenite methyltransferase|||Frequency in African-Americans 0.008; not detected in Caucasian-Americans; enzyme activity is 31% of wild-type.|||Frequency in African-Americans 0.108 and Caucasian-Americans 0.100; enzyme activity is 350% of wild-type.|||Frequency in Caucasian-Americans 0.008; not detected in African-Americans.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204447|||http://purl.uniprot.org/annotation/VAR_027392|||http://purl.uniprot.org/annotation/VAR_027393|||http://purl.uniprot.org/annotation/VAR_027394|||http://purl.uniprot.org/annotation/VSP_053494
http://togogenome.org/gene/9606:LCE2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14633                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084366|||http://purl.uniprot.org/annotation/VAR_053482|||http://purl.uniprot.org/annotation/VAR_062119
http://togogenome.org/gene/9606:KIAA1143                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AT1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA1143                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248338|||http://purl.uniprot.org/annotation/VAR_027272
http://togogenome.org/gene/9606:SMIM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71RC9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410867
http://togogenome.org/gene/9606:BCDIN3D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5W3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished O-methyltransferase activity.|||Bin3-type SAM|||Decreased O-methyltransferase activity.|||Disordered|||RNA 5'-monophosphate methyltransferase|||Slightly decreased O-methyltransferase activity.|||Strongly decreased O-methyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289265|||http://purl.uniprot.org/annotation/VAR_032614
http://togogenome.org/gene/9606:ZC4H2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQZ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C4H2-type|||In WRWF.|||In WRWF; causes a decrease in synapse number and density.|||In WRWF; increased cytoplasmic subcellular localization; partial loss of function; rescues partially interneurons differentiation when expressed in a zebrafish heterologous system.|||In WRWF; no effect on subcellular localization; no loss of function; rescues interneurons differentiation when expressed in a zebrafish heterologous system.|||In WRWF; no effect on subcellular localization; partial loss of function; rescues partially interneurons differentiation when expressed in a zebrafish heterologous system.|||In WRWFFR.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Zinc finger C4H2 domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083911|||http://purl.uniprot.org/annotation/VAR_069621|||http://purl.uniprot.org/annotation/VAR_069622|||http://purl.uniprot.org/annotation/VAR_069623|||http://purl.uniprot.org/annotation/VAR_069624|||http://purl.uniprot.org/annotation/VAR_079397|||http://purl.uniprot.org/annotation/VAR_079398|||http://purl.uniprot.org/annotation/VAR_083952|||http://purl.uniprot.org/annotation/VAR_083953|||http://purl.uniprot.org/annotation/VAR_083954|||http://purl.uniprot.org/annotation/VAR_083955|||http://purl.uniprot.org/annotation/VAR_083956|||http://purl.uniprot.org/annotation/VAR_083957|||http://purl.uniprot.org/annotation/VAR_083958|||http://purl.uniprot.org/annotation/VAR_083959|||http://purl.uniprot.org/annotation/VAR_083960|||http://purl.uniprot.org/annotation/VAR_083961|||http://purl.uniprot.org/annotation/VSP_008517|||http://purl.uniprot.org/annotation/VSP_008518|||http://purl.uniprot.org/annotation/VSP_013469|||http://purl.uniprot.org/annotation/VSP_042513|||http://purl.uniprot.org/annotation/VSP_047588
http://togogenome.org/gene/9606:FUCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTY2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||May be important for catalysis|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Plasma alpha-L-fucosidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010312|||http://purl.uniprot.org/annotation/VAR_022444|||http://purl.uniprot.org/annotation/VAR_022445|||http://purl.uniprot.org/annotation/VAR_055822|||http://purl.uniprot.org/annotation/VSP_057004|||http://purl.uniprot.org/annotation/VSP_057005
http://togogenome.org/gene/9606:FAM133B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BKY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Protein FAM133B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287616|||http://purl.uniprot.org/annotation/VSP_025571
http://togogenome.org/gene/9606:TLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y490                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  FERM|||Helical bundle R1|||Helical bundle R10|||Helical bundle R11|||Helical bundle R12|||Helical bundle R13|||Helical bundle R2|||Helical bundle R3|||Helical bundle R4|||Helical bundle R5|||Helical bundle R6|||Helical bundle R7A|||Helical bundle R7B|||Helical bundle R8|||Helical bundle R9|||I/LWEQ|||In isoform 2.|||Interaction with LAYN|||Interaction with SYNM|||Interaction with VCL and F-actin|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Talin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219428|||http://purl.uniprot.org/annotation/VAR_023751|||http://purl.uniprot.org/annotation/VAR_023752|||http://purl.uniprot.org/annotation/VAR_055538|||http://purl.uniprot.org/annotation/VSP_061952
http://togogenome.org/gene/9606:RPL10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62906                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein uL1|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125818|||http://purl.uniprot.org/annotation/VAR_034458
http://togogenome.org/gene/9606:POU2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14859                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||Loss of inhibition of DNA binding.|||POU domain, class 2, transcription factor 1|||POU-specific|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100707|||http://purl.uniprot.org/annotation/VAR_035816|||http://purl.uniprot.org/annotation/VSP_002320|||http://purl.uniprot.org/annotation/VSP_013421|||http://purl.uniprot.org/annotation/VSP_013422|||http://purl.uniprot.org/annotation/VSP_013423|||http://purl.uniprot.org/annotation/VSP_043195|||http://purl.uniprot.org/annotation/VSP_043196
http://togogenome.org/gene/9606:UNC13D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70J99                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes localization to lysosomes and interaction with RAB27A.|||C2 1|||C2 2|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with RAB27A|||MHD1|||MHD2|||Phosphoserine|||Protein unc-13 homolog D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188581|||http://purl.uniprot.org/annotation/VAR_029771|||http://purl.uniprot.org/annotation/VAR_029772|||http://purl.uniprot.org/annotation/VAR_052469|||http://purl.uniprot.org/annotation/VSP_011385|||http://purl.uniprot.org/annotation/VSP_011386|||http://purl.uniprot.org/annotation/VSP_011387|||http://purl.uniprot.org/annotation/VSP_037949
http://togogenome.org/gene/9606:RBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02753|||http://purl.uniprot.org/uniprot/Q5VY30                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  In MCOPCB10; dramatic reduction in retinol binding; has greater affinity for the STRA6 receptor.|||In RDCCAS.|||Lipocalin/cytosolic fatty-acid binding|||Omega-N-methylarginine|||Plasma retinol-binding protein(1-176)|||Plasma retinol-binding protein(1-179)|||Plasma retinol-binding protein(1-181)|||Plasma retinol-binding protein(1-182)|||Retinol-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017961|||http://purl.uniprot.org/annotation/PRO_0000017962|||http://purl.uniprot.org/annotation/PRO_0000017963|||http://purl.uniprot.org/annotation/PRO_0000017964|||http://purl.uniprot.org/annotation/PRO_0000017965|||http://purl.uniprot.org/annotation/VAR_009276|||http://purl.uniprot.org/annotation/VAR_009277|||http://purl.uniprot.org/annotation/VAR_073856|||http://purl.uniprot.org/annotation/VAR_073857
http://togogenome.org/gene/9606:ACTR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61160                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 2|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089067|||http://purl.uniprot.org/annotation/VSP_046178
http://togogenome.org/gene/9606:GSG1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUP6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Germ cell-specific gene 1-like protein 2|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343701
http://togogenome.org/gene/9606:CYP11B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19099                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cytochrome P450 11B2, mitochondrial|||In CMO-1 deficiency; abolishes the 18-hydroxylase activity required for conversion of 11-deoxycorticosterone to aldosterone.|||In CMO-1 deficiency; the enzyme is inactive.|||In CMO-2 deficiency.|||In CMO-2 deficiency; reduces 18-hydroxylase and abolishes 18-oxidase activities; leaves 11 beta-hydroxylase activity intact.|||In CMO-2 deficiency; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with A-386..|||In CMO-2 deficiency; small but consistent reduction in the production of 18-hydroxycorticosterone; slightly reduced 11-beta-hydroxylase activity, greatly decreased 18-hydroxylase activity and absent 18-oxidase activity when associated with D-198..|||Increases 11-beta- and 18-hydroxylase activities toward 11-deoxycorticosterone; increases 11-beta-hydroxylase activity toward 11-deoxycortisol.|||Increases 11-beta-hydroxylase activity toward 11-deoxycorticosterone and 11-deoxycortisol.|||Mitochondrion|||No significant effect on hydroxylase activities toward 11-deoxycorticosterone and 11-deoxycortisol.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003597|||http://purl.uniprot.org/annotation/VAR_001266|||http://purl.uniprot.org/annotation/VAR_001267|||http://purl.uniprot.org/annotation/VAR_001268|||http://purl.uniprot.org/annotation/VAR_001269|||http://purl.uniprot.org/annotation/VAR_014151|||http://purl.uniprot.org/annotation/VAR_014152|||http://purl.uniprot.org/annotation/VAR_014153|||http://purl.uniprot.org/annotation/VAR_014154|||http://purl.uniprot.org/annotation/VAR_014155|||http://purl.uniprot.org/annotation/VAR_014156|||http://purl.uniprot.org/annotation/VAR_014643|||http://purl.uniprot.org/annotation/VAR_014644|||http://purl.uniprot.org/annotation/VAR_014645|||http://purl.uniprot.org/annotation/VAR_014646|||http://purl.uniprot.org/annotation/VAR_018470|||http://purl.uniprot.org/annotation/VAR_018471|||http://purl.uniprot.org/annotation/VAR_018472|||http://purl.uniprot.org/annotation/VAR_018473
http://togogenome.org/gene/9606:CLDN19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6F1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-19|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HOMG5.|||In HOMG5; perinuclear retention of the mutant protein.|||In HOMG5; the mutant protein inserts correctly into the cell membrane although subsequent analyses suggested that dimer formation was disrupted.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144781|||http://purl.uniprot.org/annotation/VAR_031238|||http://purl.uniprot.org/annotation/VAR_031239|||http://purl.uniprot.org/annotation/VAR_031240|||http://purl.uniprot.org/annotation/VAR_031241|||http://purl.uniprot.org/annotation/VSP_010342|||http://purl.uniprot.org/annotation/VSP_044839
http://togogenome.org/gene/9606:COX6B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14854                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx10C motif|||Cx9C motif|||Cytochrome c oxidase subunit 6B1|||In MC4DN7.|||In MC4DN7; severely reduced COX6B1 protein levels in patient muscle.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194912|||http://purl.uniprot.org/annotation/VAR_046775|||http://purl.uniprot.org/annotation/VAR_084178
http://togogenome.org/gene/9606:TSPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O76068|||http://purl.uniprot.org/uniprot/P30536                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with higher levels of pregnenolone production by lymphomonocytes and with increased plasma levels of cholesterol-rich low density lipoprotein.|||Cytoplasmic|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Mitochondrial intermembrane|||Removed|||Translocator protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190997|||http://purl.uniprot.org/annotation/VAR_013617|||http://purl.uniprot.org/annotation/VAR_013618|||http://purl.uniprot.org/annotation/VAR_018868
http://togogenome.org/gene/9606:SOBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7XYQ1|||http://purl.uniprot.org/uniprot/Q24K27                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FCS-type 1|||FCS-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Pro residues|||SUMO interaction motif 1 (SIM); mediates the binding to polysumoylated substrates|||SUMO interaction motif 2 (SIM); mediates the binding to polysumoylated substrates|||Sine oculis-binding protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312232|||http://purl.uniprot.org/annotation/VAR_062215
http://togogenome.org/gene/9606:EIF2S3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41091                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 2 subunit 3|||G1|||G2|||G3|||G4|||G5|||In MEHMO; decreased interaction with the other eIF2 complex subunits EIF2S1 and EIF2S2.|||In MEHMO; unknown pathological significance.|||N-acetylalanine; partial|||Phosphoserine|||Removed|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137438|||http://purl.uniprot.org/annotation/VAR_002352|||http://purl.uniprot.org/annotation/VAR_077139|||http://purl.uniprot.org/annotation/VAR_077140|||http://purl.uniprot.org/annotation/VAR_078100
http://togogenome.org/gene/9606:ZBTB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DT7|||http://purl.uniprot.org/uniprot/Q9H9H3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger and BTB domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047725|||http://purl.uniprot.org/annotation/VAR_018384|||http://purl.uniprot.org/annotation/VAR_018385|||http://purl.uniprot.org/annotation/VSP_040316|||http://purl.uniprot.org/annotation/VSP_040317|||http://purl.uniprot.org/annotation/VSP_040318|||http://purl.uniprot.org/annotation/VSP_040319
http://togogenome.org/gene/9606:CACNA1H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQW2|||http://purl.uniprot.org/uniprot/B3KQH9|||http://purl.uniprot.org/uniprot/O95180                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Calcium ion selectivity and permeability|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with aldosterone-producing adenoma and aldosterism; unknown pathological significance; changed Ca(2+) channel activity.|||Found in a patient with autism; unknown pathological significance.|||Found in a patient with drug-resistant focal epilepsy; unknown pathological significance.|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IV|||In ECA6.|||In ECA6; creates a dileucine internalization motif that promotes recruitment of clathrin.|||In ECA6; results in increased T-current amplitude and lower threshold for spikes generation; results in increased neuronal excitability.|||In EIG6.|||In HALD4; changed calcium channel activity.|||In HALD4; changed calcium channel activity; increased aldosterone production in response to potassium ion stimulation; increased expression of genes involved in aldosterone biosynthesis, with the strongest effect observed on CYP11B2 expression in response to potassium ion stimulation.|||In isoform 2.|||Ion transport|||N-linked (GlcNAc...) asparagine|||Polar residues|||Voltage-dependent T-type calcium channel subunit alpha-1H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053954|||http://purl.uniprot.org/annotation/VAR_033698|||http://purl.uniprot.org/annotation/VAR_045935|||http://purl.uniprot.org/annotation/VAR_045936|||http://purl.uniprot.org/annotation/VAR_045937|||http://purl.uniprot.org/annotation/VAR_045938|||http://purl.uniprot.org/annotation/VAR_045939|||http://purl.uniprot.org/annotation/VAR_045940|||http://purl.uniprot.org/annotation/VAR_045941|||http://purl.uniprot.org/annotation/VAR_045942|||http://purl.uniprot.org/annotation/VAR_045943|||http://purl.uniprot.org/annotation/VAR_045944|||http://purl.uniprot.org/annotation/VAR_045945|||http://purl.uniprot.org/annotation/VAR_045946|||http://purl.uniprot.org/annotation/VAR_045947|||http://purl.uniprot.org/annotation/VAR_045948|||http://purl.uniprot.org/annotation/VAR_045949|||http://purl.uniprot.org/annotation/VAR_045950|||http://purl.uniprot.org/annotation/VAR_045951|||http://purl.uniprot.org/annotation/VAR_045952|||http://purl.uniprot.org/annotation/VAR_045953|||http://purl.uniprot.org/annotation/VAR_045954|||http://purl.uniprot.org/annotation/VAR_045955|||http://purl.uniprot.org/annotation/VAR_061104|||http://purl.uniprot.org/annotation/VAR_066986|||http://purl.uniprot.org/annotation/VAR_066987|||http://purl.uniprot.org/annotation/VAR_077064|||http://purl.uniprot.org/annotation/VAR_077065|||http://purl.uniprot.org/annotation/VAR_077066|||http://purl.uniprot.org/annotation/VAR_077067|||http://purl.uniprot.org/annotation/VAR_077068|||http://purl.uniprot.org/annotation/VAR_078237|||http://purl.uniprot.org/annotation/VAR_078702|||http://purl.uniprot.org/annotation/VSP_000949
http://togogenome.org/gene/9606:RASSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2L5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Ras association domain-containing protein 4|||Ras-associating|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240398|||http://purl.uniprot.org/annotation/VAR_034438|||http://purl.uniprot.org/annotation/VAR_034439|||http://purl.uniprot.org/annotation/VSP_019355|||http://purl.uniprot.org/annotation/VSP_019356|||http://purl.uniprot.org/annotation/VSP_019357|||http://purl.uniprot.org/annotation/VSP_019358|||http://purl.uniprot.org/annotation/VSP_019359
http://togogenome.org/gene/9606:RHOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08134                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB|||ADP-ribosylasparagine; by botulinum toxin|||Cysteine methyl ester|||Effector region|||O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230|||Removed in mature form|||Rho-related GTP-binding protein RhoC|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042022|||http://purl.uniprot.org/annotation/PRO_0000042023|||http://purl.uniprot.org/annotation/VAR_051974
http://togogenome.org/gene/9606:ZC3H14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V256|||http://purl.uniprot.org/uniprot/Q6PJT7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 10.|||In isoform 11.|||In isoform 2, isoform 3, isoform 6, isoform 9 and isoform 11.|||In isoform 3 and isoform 10.|||In isoform 4, isoform 6 and isoform 11.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||In isoform 9.|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Polar residues|||Zinc finger CCCH domain-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331311|||http://purl.uniprot.org/annotation/VSP_033162|||http://purl.uniprot.org/annotation/VSP_033163|||http://purl.uniprot.org/annotation/VSP_033164|||http://purl.uniprot.org/annotation/VSP_033165|||http://purl.uniprot.org/annotation/VSP_033166|||http://purl.uniprot.org/annotation/VSP_033167|||http://purl.uniprot.org/annotation/VSP_033168|||http://purl.uniprot.org/annotation/VSP_033169|||http://purl.uniprot.org/annotation/VSP_033171|||http://purl.uniprot.org/annotation/VSP_044645|||http://purl.uniprot.org/annotation/VSP_055096|||http://purl.uniprot.org/annotation/VSP_055097
http://togogenome.org/gene/9606:BORCS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FH0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  BLOC-1-related complex subunit 8|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000269843|||http://purl.uniprot.org/annotation/VSP_022103|||http://purl.uniprot.org/annotation/VSP_022104
http://togogenome.org/gene/9606:MPLKIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1W6|||http://purl.uniprot.org/uniprot/Q8TAP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with PLK1 in mitosis.|||Asymmetric dimethylarginine|||Disordered|||Has no effect on interaction with PLK1 in mitosis. Partially prevents phosphorylation.|||In TTD4.|||In a breast cancer sample; somatic mutation.|||M-phase-specific PLK1-interacting protein|||Omega-N-methylarginine|||Partially prevents phosphorylation.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065674|||http://purl.uniprot.org/annotation/VAR_022940|||http://purl.uniprot.org/annotation/VAR_036273
http://togogenome.org/gene/9606:SPIN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JZB7|||http://purl.uniprot.org/uniprot/Q9BPZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Histone H3K4me3 and H3R8me2a binding|||Polar residues|||Spindlin-2B|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181369
http://togogenome.org/gene/9606:TBX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95947                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In SCDO5; unknown pathological significance.|||In congenital scoliosis; unknown pathological significance; decreases transcriptional activity.|||In congenital scoliosis; unknown pathological significance; not change transcriptional activity.|||In isoform 2.|||T-box|||T-box transcription factor TBX6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184438|||http://purl.uniprot.org/annotation/VAR_027836|||http://purl.uniprot.org/annotation/VAR_027837|||http://purl.uniprot.org/annotation/VAR_061837|||http://purl.uniprot.org/annotation/VAR_078494|||http://purl.uniprot.org/annotation/VAR_078495|||http://purl.uniprot.org/annotation/VAR_078496|||http://purl.uniprot.org/annotation/VSP_054003|||http://purl.uniprot.org/annotation/VSP_054004
http://togogenome.org/gene/9606:HS1BP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53T59|||http://purl.uniprot.org/uniprot/Q9H7U7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HCLS1-binding protein 3|||N-acetylmethionine|||N6-acetyllysine|||PX|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313802|||http://purl.uniprot.org/annotation/VAR_037741|||http://purl.uniprot.org/annotation/VAR_037742|||http://purl.uniprot.org/annotation/VAR_037743|||http://purl.uniprot.org/annotation/VAR_037744
http://togogenome.org/gene/9606:KXD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQD3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||KxDL motif-containing protein 1|||N-acetylmethionine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295259|||http://purl.uniprot.org/annotation/VAR_033282
http://togogenome.org/gene/9606:FGD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98174                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||DH|||Disordered|||FYVE, RhoGEF and PH domain-containing protein 1|||FYVE-type|||In AAS.|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080940|||http://purl.uniprot.org/annotation/VAR_015236|||http://purl.uniprot.org/annotation/VAR_015237|||http://purl.uniprot.org/annotation/VAR_019268|||http://purl.uniprot.org/annotation/VAR_019269|||http://purl.uniprot.org/annotation/VAR_019270|||http://purl.uniprot.org/annotation/VAR_019271
http://togogenome.org/gene/9606:NSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FM2|||http://purl.uniprot.org/uniprot/Q96IY1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Kinetochore-associated protein NSL1 homolog|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089260|||http://purl.uniprot.org/annotation/VAR_016005|||http://purl.uniprot.org/annotation/VAR_051243|||http://purl.uniprot.org/annotation/VSP_045741
http://togogenome.org/gene/9606:TFF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04155                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Abolishes inhibition of gastric cancer cell growth.|||In a gastric adenoma sample; somatic mutation.|||In a gastric carcinoma sample; somatic mutation.|||In a gastric carcinoma sample; somatic mutation; abolishes inhibition of gastric cancer cell growth; abolishes inhibition of apoptosis in gasterointestinal epithelial cells; increases invasive activity in epithelial cells.|||P-type|||Trefoil factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023456|||http://purl.uniprot.org/annotation/VAR_015281|||http://purl.uniprot.org/annotation/VAR_015282|||http://purl.uniprot.org/annotation/VAR_015283|||http://purl.uniprot.org/annotation/VAR_015284|||http://purl.uniprot.org/annotation/VAR_015285|||http://purl.uniprot.org/annotation/VAR_015286|||http://purl.uniprot.org/annotation/VAR_053563
http://togogenome.org/gene/9606:CD2BP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZC1|||http://purl.uniprot.org/uniprot/O95400                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  CD2 antigen cytoplasmic tail-binding protein 2|||Disordered|||GYF|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089437|||http://purl.uniprot.org/annotation/VAR_050772|||http://purl.uniprot.org/annotation/VAR_050773
http://togogenome.org/gene/9606:WASF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6W5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Actin-binding protein WASF2|||Basic and acidic residues|||Constitutive induction of the formation of actin filaments. Strongly enhances formation of lamellipodia.|||Decreased interaction with WAVE complex; when associated with D-40.|||Decreased interaction with WAVE complex; when associated with D-50.|||Decreased interaction with WAVE complex; when associated with D-51.|||Decreased interaction with WAVE complex; when associated with D-54.|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188994|||http://purl.uniprot.org/annotation/VSP_042514|||http://purl.uniprot.org/annotation/VSP_042515
http://togogenome.org/gene/9606:FBXO48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FWF7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 48                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335677|||http://purl.uniprot.org/annotation/VAR_043466
http://togogenome.org/gene/9606:MCM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DN82|||http://purl.uniprot.org/uniprot/Q9UJA3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA helicase MCM8|||Decreases the formation of MRE11 and RPA1 foci in response to cisplatin-induced DNA damage.|||Disordered|||In POF10; inhibits protein recruitment to sites of DNA damage; shows significant reduction in DNA-binding affinity for single-strand DNA.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MCM|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194125|||http://purl.uniprot.org/annotation/VAR_015145|||http://purl.uniprot.org/annotation/VAR_050281|||http://purl.uniprot.org/annotation/VAR_050282|||http://purl.uniprot.org/annotation/VAR_050283|||http://purl.uniprot.org/annotation/VAR_050284|||http://purl.uniprot.org/annotation/VAR_050285|||http://purl.uniprot.org/annotation/VAR_073417|||http://purl.uniprot.org/annotation/VSP_015785|||http://purl.uniprot.org/annotation/VSP_041308|||http://purl.uniprot.org/annotation/VSP_044179
http://togogenome.org/gene/9606:GPR18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NIM1|||http://purl.uniprot.org/uniprot/Q14330                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Increased cell surface expression.|||N-arachidonyl glycine receptor|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069537
http://togogenome.org/gene/9606:RNF139                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WU17                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitination activity. Increases proliferation.|||Abolishes ubiquitination activity. Increases proliferation. Does not phosphorylate CHEK2 on T-68. Does not phosphorylate ATM on S-1981. Rescues MHC class I to the cell surface. Suppresses SREBF2 processing in the presence or absence of sterols. Fails to down-regulate SREBF1 and SREBF2. Decreases INSIG1 ubiquitination.|||Disordered|||E3 ubiquitin-protein ligase RNF139|||Helical|||Increases proliferation. Rescues MHC class I to the cell surface. Fails to down-regulate SREBF1 and SREBF2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||RING-type; atypical|||Removed|||Retaines about 30% of ubiquitination activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056098
http://togogenome.org/gene/9606:SERPINA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05543                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Associated with F-303 in San Diego; partial thyroxine-binding globulin deficiency.|||Associated with T-43 in San Diego.|||CD5; complete thyroxine-binding globulin deficiency.|||Gary; severe thyroxine-binding globulin deficiency.|||Kumamoto; partial thyroxine-binding globulin deficiency.|||Montreal/TBG-M; partial thyroxine-binding globulin deficiency.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; in variant Gary|||Quebec; partial thyroxine-binding globulin deficiency.|||TBG-A/Aborigine.|||TBG-S/Slow.|||Thyroxine-binding globulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032436|||http://purl.uniprot.org/annotation/VAR_007102|||http://purl.uniprot.org/annotation/VAR_007103|||http://purl.uniprot.org/annotation/VAR_007104|||http://purl.uniprot.org/annotation/VAR_007105|||http://purl.uniprot.org/annotation/VAR_007106|||http://purl.uniprot.org/annotation/VAR_007107|||http://purl.uniprot.org/annotation/VAR_007108|||http://purl.uniprot.org/annotation/VAR_007109|||http://purl.uniprot.org/annotation/VAR_007110
http://togogenome.org/gene/9606:ZNF319                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2F9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Pro residues|||Zinc finger protein 319                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047527
http://togogenome.org/gene/9606:GPSM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCP6|||http://purl.uniprot.org/uniprot/Q9Y4H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Disordered|||G-protein-signaling modulator 3|||GoLoco 1|||GoLoco 2|||GoLoco 3|||Phosphoserine|||Phosphothreonine|||Pro residues|||Restores G(i) alpha binding and GDI activity of the GoLoco 2 domain.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233717
http://togogenome.org/gene/9606:CTSC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53634                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dipeptidyl peptidase 1 exclusion domain chain|||Dipeptidyl peptidase 1 heavy chain|||Dipeptidyl peptidase 1 light chain|||In AP1.|||In HMS and PLS.|||In PLS and AP1.|||In PLS.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026338|||http://purl.uniprot.org/annotation/PRO_0000026339|||http://purl.uniprot.org/annotation/PRO_0000026340|||http://purl.uniprot.org/annotation/PRO_0000026341|||http://purl.uniprot.org/annotation/VAR_009541|||http://purl.uniprot.org/annotation/VAR_009542|||http://purl.uniprot.org/annotation/VAR_009543|||http://purl.uniprot.org/annotation/VAR_009544|||http://purl.uniprot.org/annotation/VAR_009545|||http://purl.uniprot.org/annotation/VAR_009546|||http://purl.uniprot.org/annotation/VAR_016933|||http://purl.uniprot.org/annotation/VAR_016934|||http://purl.uniprot.org/annotation/VAR_016935|||http://purl.uniprot.org/annotation/VAR_016936|||http://purl.uniprot.org/annotation/VAR_016943|||http://purl.uniprot.org/annotation/VAR_016944|||http://purl.uniprot.org/annotation/VAR_016945|||http://purl.uniprot.org/annotation/VAR_016946|||http://purl.uniprot.org/annotation/VAR_019035|||http://purl.uniprot.org/annotation/VAR_019036|||http://purl.uniprot.org/annotation/VAR_019037|||http://purl.uniprot.org/annotation/VAR_019038|||http://purl.uniprot.org/annotation/VAR_019039|||http://purl.uniprot.org/annotation/VAR_019040|||http://purl.uniprot.org/annotation/VAR_019041|||http://purl.uniprot.org/annotation/VAR_019042|||http://purl.uniprot.org/annotation/VAR_019043|||http://purl.uniprot.org/annotation/VAR_019044|||http://purl.uniprot.org/annotation/VAR_019045|||http://purl.uniprot.org/annotation/VAR_019046|||http://purl.uniprot.org/annotation/VAR_019047|||http://purl.uniprot.org/annotation/VAR_019048|||http://purl.uniprot.org/annotation/VAR_027249|||http://purl.uniprot.org/annotation/VAR_027250|||http://purl.uniprot.org/annotation/VAR_039686|||http://purl.uniprot.org/annotation/VSP_039123|||http://purl.uniprot.org/annotation/VSP_039124|||http://purl.uniprot.org/annotation/VSP_043232|||http://purl.uniprot.org/annotation/VSP_043233
http://togogenome.org/gene/9606:CELA3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09093                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Chymotrypsin-like elastase family member 3A|||N-linked (GlcNAc...) asparagine|||Or 16|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027697|||http://purl.uniprot.org/annotation/PRO_0000027698|||http://purl.uniprot.org/annotation/VAR_051838|||http://purl.uniprot.org/annotation/VAR_059783|||http://purl.uniprot.org/annotation/VAR_059784|||http://purl.uniprot.org/annotation/VAR_059785
http://togogenome.org/gene/9606:SHMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34896                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-(pyridoxal phosphate)lysine|||N6-acetyllysine|||Serine hydroxymethyltransferase, cytosolic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000113504|||http://purl.uniprot.org/annotation/VAR_022010|||http://purl.uniprot.org/annotation/VAR_059795|||http://purl.uniprot.org/annotation/VSP_006095|||http://purl.uniprot.org/annotation/VSP_006096|||http://purl.uniprot.org/annotation/VSP_054610
http://togogenome.org/gene/9606:DOCK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9U8|||http://purl.uniprot.org/uniprot/Q96HP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 6|||Disordered|||Omega-N-methylarginine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189993|||http://purl.uniprot.org/annotation/VAR_029830|||http://purl.uniprot.org/annotation/VAR_029831|||http://purl.uniprot.org/annotation/VAR_029832|||http://purl.uniprot.org/annotation/VAR_029833|||http://purl.uniprot.org/annotation/VAR_057522|||http://purl.uniprot.org/annotation/VAR_057523
http://togogenome.org/gene/9606:IFRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0U1|||http://purl.uniprot.org/uniprot/O00458                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||In isoform 2.|||Interferon-related developmental regulator 1|||Interferon-related developmental regulator C-terminal|||Interferon-related developmental regulator N-terminal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153285|||http://purl.uniprot.org/annotation/VAR_064723|||http://purl.uniprot.org/annotation/VSP_044304
http://togogenome.org/gene/9606:DYNLT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51808                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  3'-nitrotyrosine|||Dynein light chain Tctex-type 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195158
http://togogenome.org/gene/9606:PCDH11X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZA7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Protocadherin-11 X-linked                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232758|||http://purl.uniprot.org/annotation/VAR_036109|||http://purl.uniprot.org/annotation/VAR_048575|||http://purl.uniprot.org/annotation/VSP_017979|||http://purl.uniprot.org/annotation/VSP_017980|||http://purl.uniprot.org/annotation/VSP_017981|||http://purl.uniprot.org/annotation/VSP_017982|||http://purl.uniprot.org/annotation/VSP_017983|||http://purl.uniprot.org/annotation/VSP_017984|||http://purl.uniprot.org/annotation/VSP_017985|||http://purl.uniprot.org/annotation/VSP_017986|||http://purl.uniprot.org/annotation/VSP_017987
http://togogenome.org/gene/9606:SLC22A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1K9|||http://purl.uniprot.org/uniprot/Q86VW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Polar residues|||Solute carrier family 22 member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318991|||http://purl.uniprot.org/annotation/VAR_038930|||http://purl.uniprot.org/annotation/VAR_038931|||http://purl.uniprot.org/annotation/VAR_038932|||http://purl.uniprot.org/annotation/VAR_038933|||http://purl.uniprot.org/annotation/VSP_031336|||http://purl.uniprot.org/annotation/VSP_031337|||http://purl.uniprot.org/annotation/VSP_031338
http://togogenome.org/gene/9606:PRDM15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ER26|||http://purl.uniprot.org/uniprot/P57071                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||PR domain zinc finger protein 15|||Polar residues|||Pro residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047772|||http://purl.uniprot.org/annotation/VAR_014992|||http://purl.uniprot.org/annotation/VAR_014993|||http://purl.uniprot.org/annotation/VAR_014994|||http://purl.uniprot.org/annotation/VSP_055110|||http://purl.uniprot.org/annotation/VSP_055111|||http://purl.uniprot.org/annotation/VSP_055112|||http://purl.uniprot.org/annotation/VSP_055113|||http://purl.uniprot.org/annotation/VSP_055114|||http://purl.uniprot.org/annotation/VSP_055115|||http://purl.uniprot.org/annotation/VSP_055116|||http://purl.uniprot.org/annotation/VSP_055117
http://togogenome.org/gene/9606:TMEM236                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5W0B7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 236                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186716
http://togogenome.org/gene/9606:VPS13D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5THJ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Chorein N-terminal|||Disordered|||In SCAR4.|||In SCAR4; altered mitochondrial morphology in patient cells.|||In SCAR4; decreased protein abundance; altered mitochondrial morphology in patient cells.|||In SCAR4; unknown pathological significance.|||In isoform 2.|||Intermembrane lipid transfer protein VPS13D|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||SHR-BD|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262951|||http://purl.uniprot.org/annotation/VAR_029557|||http://purl.uniprot.org/annotation/VAR_029558|||http://purl.uniprot.org/annotation/VAR_029559|||http://purl.uniprot.org/annotation/VAR_029560|||http://purl.uniprot.org/annotation/VAR_062169|||http://purl.uniprot.org/annotation/VAR_080911|||http://purl.uniprot.org/annotation/VAR_080912|||http://purl.uniprot.org/annotation/VAR_080913|||http://purl.uniprot.org/annotation/VAR_080914|||http://purl.uniprot.org/annotation/VAR_080915|||http://purl.uniprot.org/annotation/VAR_080916|||http://purl.uniprot.org/annotation/VAR_081496|||http://purl.uniprot.org/annotation/VAR_081497|||http://purl.uniprot.org/annotation/VAR_081498|||http://purl.uniprot.org/annotation/VAR_081499|||http://purl.uniprot.org/annotation/VAR_081500|||http://purl.uniprot.org/annotation/VAR_081501|||http://purl.uniprot.org/annotation/VAR_081502|||http://purl.uniprot.org/annotation/VAR_081503|||http://purl.uniprot.org/annotation/VAR_081504|||http://purl.uniprot.org/annotation/VAR_081505|||http://purl.uniprot.org/annotation/VSP_052249
http://togogenome.org/gene/9606:ZNF292                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60281                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; degenerate|||C2H2-type 9|||Disordered|||In MRD64.|||In MRD64; unknown pathological significance.|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Zinc finger protein 292                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047514|||http://purl.uniprot.org/annotation/VAR_062972|||http://purl.uniprot.org/annotation/VAR_062973|||http://purl.uniprot.org/annotation/VAR_085258|||http://purl.uniprot.org/annotation/VAR_085259|||http://purl.uniprot.org/annotation/VAR_085260|||http://purl.uniprot.org/annotation/VAR_085261|||http://purl.uniprot.org/annotation/VAR_085262|||http://purl.uniprot.org/annotation/VAR_085263|||http://purl.uniprot.org/annotation/VAR_085264|||http://purl.uniprot.org/annotation/VAR_085265|||http://purl.uniprot.org/annotation/VAR_085266|||http://purl.uniprot.org/annotation/VAR_085267|||http://purl.uniprot.org/annotation/VAR_085268|||http://purl.uniprot.org/annotation/VAR_085269|||http://purl.uniprot.org/annotation/VAR_085270|||http://purl.uniprot.org/annotation/VSP_038857|||http://purl.uniprot.org/annotation/VSP_038858
http://togogenome.org/gene/9606:C4orf46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504U0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Renal cancer differentiation gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335689
http://togogenome.org/gene/9606:CDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J126|||http://purl.uniprot.org/uniprot/P19022                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In ACOGS.|||In ACOGS; decreased function in cell-cell adhesion.|||In ACOGS; unknown pathological significance.|||In ADHD8; decreased propeptide cleavage.|||In ARVD14; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PH|||Phosphoserine; by FAM20C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003731|||http://purl.uniprot.org/annotation/PRO_0000003732|||http://purl.uniprot.org/annotation/VAR_028254|||http://purl.uniprot.org/annotation/VAR_028255|||http://purl.uniprot.org/annotation/VAR_028256|||http://purl.uniprot.org/annotation/VAR_028257|||http://purl.uniprot.org/annotation/VAR_028258|||http://purl.uniprot.org/annotation/VAR_048503|||http://purl.uniprot.org/annotation/VAR_084438|||http://purl.uniprot.org/annotation/VAR_084439|||http://purl.uniprot.org/annotation/VAR_084440|||http://purl.uniprot.org/annotation/VAR_084441|||http://purl.uniprot.org/annotation/VAR_084442|||http://purl.uniprot.org/annotation/VAR_084443|||http://purl.uniprot.org/annotation/VAR_084444|||http://purl.uniprot.org/annotation/VAR_084445|||http://purl.uniprot.org/annotation/VAR_084446|||http://purl.uniprot.org/annotation/VAR_084447|||http://purl.uniprot.org/annotation/VAR_084448|||http://purl.uniprot.org/annotation/VAR_084449|||http://purl.uniprot.org/annotation/VAR_087507|||http://purl.uniprot.org/annotation/VSP_056448
http://togogenome.org/gene/9606:MOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00540                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  In a lung adenocarcinoma sample; somatic mutation.|||Protein kinase|||Proto-oncogene serine/threonine-protein kinase mos|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086344|||http://purl.uniprot.org/annotation/VAR_040813|||http://purl.uniprot.org/annotation/VAR_040814|||http://purl.uniprot.org/annotation/VAR_040815|||http://purl.uniprot.org/annotation/VAR_040816
http://togogenome.org/gene/9606:RAD51AP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09MP3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Interaction with RAD51|||RAD51-associated protein 2|||Strongly decreases interaction with RAD51; when associated with 1143-AA-1144.|||Strongly decreases interaction with RAD51; when associated with A-1134.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336071|||http://purl.uniprot.org/annotation/VAR_043478|||http://purl.uniprot.org/annotation/VAR_043479|||http://purl.uniprot.org/annotation/VAR_043480
http://togogenome.org/gene/9606:ZNF70                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV76|||http://purl.uniprot.org/uniprot/Q9UC06                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Zinc finger protein 70                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047380
http://togogenome.org/gene/9606:HACE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYU2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Disordered|||E3 ubiquitin-protein ligase HACE1|||Glycyl thioester intermediate|||HECT|||In SPPRS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of E3 ubiquitin ligase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280622|||http://purl.uniprot.org/annotation/VAR_031180|||http://purl.uniprot.org/annotation/VAR_031181|||http://purl.uniprot.org/annotation/VAR_076311|||http://purl.uniprot.org/annotation/VSP_023829|||http://purl.uniprot.org/annotation/VSP_023830|||http://purl.uniprot.org/annotation/VSP_023831|||http://purl.uniprot.org/annotation/VSP_042378
http://togogenome.org/gene/9606:TEX35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0J7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Testis-expressed protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251187|||http://purl.uniprot.org/annotation/VAR_027656|||http://purl.uniprot.org/annotation/VAR_027657|||http://purl.uniprot.org/annotation/VAR_027658|||http://purl.uniprot.org/annotation/VAR_059592|||http://purl.uniprot.org/annotation/VSP_020737|||http://purl.uniprot.org/annotation/VSP_020738|||http://purl.uniprot.org/annotation/VSP_020739|||http://purl.uniprot.org/annotation/VSP_020740|||http://purl.uniprot.org/annotation/VSP_020741|||http://purl.uniprot.org/annotation/VSP_045739
http://togogenome.org/gene/9606:UMOD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07911                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by HPN. Abolishes polymerization, in a dominant-negative manner. Suppresses the dominant-negative loss of polymerization; when associated with A-415.|||Abolishes polymerization and filament formation of the secreted form.|||Abolishes polymerization, in a dominant-negative manner. No effect on protein trafficking or secretion. Suppresses the dominant-negative loss of polymerization; when associated with A-415.|||Abolishes polymerization. No effect on protein trafficking or secretion. Suppresses the dominant-negative loss of polymerization in 555-F-A-556 DEL or 586-A--A-589; when associated with 555-F-A-556 DEL or 586-A--A-589.|||Beta hairpin|||Cleavage|||D10C|||Decreased export from the endoplasmic reticulum, leading to decreased secretion. Impairs polymerization.|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||Essential for cleavage by HPN|||External hydrophobic patch (EHP); regulates polymerization into filaments|||Flexible ZP-N/ZP-C linker; important for secretion and polymerization into filaments|||GPI-anchor amidated serine|||Impairs polymerization and filament formation of the secreted form.|||In ADTKD1.|||In ADTKD1; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER.|||In ADTKD1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER.|||In ADTKD1; phenotype overlapping with medullary cystic kidney disease; causes a delay in protein export to the plasma membrane due to a longer retention time in the ER; results is abnormal intracellular polymerization of the mutant protein.|||In ADTKD1; results in defective trafficking of mutant protein to the plasma membrane; the mutant is retained in the ER.|||In ADTKD1; serum levels severely reduced.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Internal hydrophobic patch (IHP)|||Leads to retention in the endoplasmic reticulum, probably due to misfolding.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (complex) asparagine; alternate|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) (high mannose) asparagine; alternate|||N-linked (GlcNAc...) asparagine|||No effect on secretion. Does not impair polymerization.|||Probable-disease association mutation found in a patient with cystic kidney disease; results in mutant retention in the ER; results is abnormal intracellular polymerization of the mutant protein.|||Removed in mature form|||Uromodulin|||Uromodulin, secreted form|||ZP|||ZP-C|||ZP-N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041671|||http://purl.uniprot.org/annotation/PRO_0000041672|||http://purl.uniprot.org/annotation/PRO_0000407909|||http://purl.uniprot.org/annotation/VAR_017666|||http://purl.uniprot.org/annotation/VAR_017667|||http://purl.uniprot.org/annotation/VAR_017668|||http://purl.uniprot.org/annotation/VAR_025950|||http://purl.uniprot.org/annotation/VAR_025951|||http://purl.uniprot.org/annotation/VAR_025952|||http://purl.uniprot.org/annotation/VAR_025953|||http://purl.uniprot.org/annotation/VAR_025954|||http://purl.uniprot.org/annotation/VAR_025955|||http://purl.uniprot.org/annotation/VAR_025956|||http://purl.uniprot.org/annotation/VAR_025957|||http://purl.uniprot.org/annotation/VAR_025958|||http://purl.uniprot.org/annotation/VAR_025959|||http://purl.uniprot.org/annotation/VAR_025960|||http://purl.uniprot.org/annotation/VAR_025961|||http://purl.uniprot.org/annotation/VAR_025962|||http://purl.uniprot.org/annotation/VAR_061993|||http://purl.uniprot.org/annotation/VAR_071398|||http://purl.uniprot.org/annotation/VAR_071399|||http://purl.uniprot.org/annotation/VAR_071400|||http://purl.uniprot.org/annotation/VAR_071401|||http://purl.uniprot.org/annotation/VAR_073052|||http://purl.uniprot.org/annotation/VAR_073053|||http://purl.uniprot.org/annotation/VAR_073054|||http://purl.uniprot.org/annotation/VAR_073055|||http://purl.uniprot.org/annotation/VAR_073056|||http://purl.uniprot.org/annotation/VAR_073057|||http://purl.uniprot.org/annotation/VAR_073058|||http://purl.uniprot.org/annotation/VAR_073059|||http://purl.uniprot.org/annotation/VAR_073060|||http://purl.uniprot.org/annotation/VAR_073061|||http://purl.uniprot.org/annotation/VAR_073062|||http://purl.uniprot.org/annotation/VAR_073063|||http://purl.uniprot.org/annotation/VAR_073064|||http://purl.uniprot.org/annotation/VAR_073065|||http://purl.uniprot.org/annotation/VAR_073066|||http://purl.uniprot.org/annotation/VAR_073067|||http://purl.uniprot.org/annotation/VAR_073068|||http://purl.uniprot.org/annotation/VAR_073069|||http://purl.uniprot.org/annotation/VAR_077514|||http://purl.uniprot.org/annotation/VSP_017565|||http://purl.uniprot.org/annotation/VSP_017566|||http://purl.uniprot.org/annotation/VSP_040973|||http://purl.uniprot.org/annotation/VSP_054828
http://togogenome.org/gene/9606:LOC102724594                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01081                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C3H1-type 1|||C3H1-type 2|||Decreases affinity for UAF2 by 3 orders of magnitude.|||Disordered|||In MDS; somatic mutation; affects alternative splicing of target sequences resulting in increased splicing efficiency, exon skipping and alternative splice site utilization; no effect on localization to nuclear speckles.|||In MDS; somatic mutation; affects alternative splicing of target sequences.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-methyllysine|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed|||Splicing factor U2AF 35 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081994|||http://purl.uniprot.org/annotation/VAR_079637|||http://purl.uniprot.org/annotation/VAR_079638|||http://purl.uniprot.org/annotation/VAR_079639|||http://purl.uniprot.org/annotation/VSP_042664|||http://purl.uniprot.org/annotation/VSP_042665|||http://purl.uniprot.org/annotation/VSP_042666|||http://purl.uniprot.org/annotation/VSP_042667
http://togogenome.org/gene/9606:SPOP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43791                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||Important for binding substrate proteins|||Important for homodimerization|||In NSDVS1; gain-of-function, reduced BET proteins stability.|||In NSDVS2; dominant-negative, increased BET proteins stability.|||MATH|||Required for nuclear localization|||Speckle-type POZ protein|||Strongly reduced affinity for substrate proteins.|||Strongly reduced homodimerization. Reduces the activity of the cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191621|||http://purl.uniprot.org/annotation/VAR_083851|||http://purl.uniprot.org/annotation/VAR_083852|||http://purl.uniprot.org/annotation/VAR_083853|||http://purl.uniprot.org/annotation/VAR_083854|||http://purl.uniprot.org/annotation/VAR_083855|||http://purl.uniprot.org/annotation/VAR_083856
http://togogenome.org/gene/9606:CEP63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HIX3|||http://purl.uniprot.org/uniprot/Q96MT8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein Cep63/Deup1 N-terminal|||Centrosomal protein of 63 kDa|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089493|||http://purl.uniprot.org/annotation/VAR_020604|||http://purl.uniprot.org/annotation/VSP_012251|||http://purl.uniprot.org/annotation/VSP_012252|||http://purl.uniprot.org/annotation/VSP_012253|||http://purl.uniprot.org/annotation/VSP_012254
http://togogenome.org/gene/9606:MT1X                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJP8|||http://purl.uniprot.org/uniprot/P80297                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  Alpha|||Beta|||Metallothionein-1X|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197243
http://togogenome.org/gene/9606:OVCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ82                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Charge relay system|||Disordered|||Esterase OVCA2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300876
http://togogenome.org/gene/9606:FASTKD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8L6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  FAST kinase domain-containing protein 5, mitochondrial|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||RAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284979|||http://purl.uniprot.org/annotation/VAR_053891|||http://purl.uniprot.org/annotation/VAR_053892|||http://purl.uniprot.org/annotation/VAR_053893
http://togogenome.org/gene/9606:NOMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KN36|||http://purl.uniprot.org/uniprot/P69849|||http://purl.uniprot.org/uniprot/Q1LZN2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BOS complex subunit NOMO3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Prealbumin-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021821|||http://purl.uniprot.org/annotation/PRO_5014098587
http://togogenome.org/gene/9606:TRMT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUP7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CHHC U11-48K-type|||Disordered|||In isoform 2.|||N-acetylalanine|||Removed|||tRNA:m(4)X modification enzyme TRM13 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236678|||http://purl.uniprot.org/annotation/VAR_057806|||http://purl.uniprot.org/annotation/VSP_018578|||http://purl.uniprot.org/annotation/VSP_018579
http://togogenome.org/gene/9606:ISL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61371                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Homeobox|||Insulin gene enhancer protein ISL-1|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM-binding domain (LID)|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075746
http://togogenome.org/gene/9606:SLC38A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VX04|||http://purl.uniprot.org/uniprot/Q9H2H9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Amino acid transporter transmembrane|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium-coupled neutral amino acid symporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310475
http://togogenome.org/gene/9606:MRPL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRX2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein bL17m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237331
http://togogenome.org/gene/9606:THAP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DKM9|||http://purl.uniprot.org/uniprot/H9CWI5|||http://purl.uniprot.org/uniprot/Q8NA92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Pro residues|||THAP domain-containing protein 8|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068650|||http://purl.uniprot.org/annotation/VAR_020264|||http://purl.uniprot.org/annotation/VAR_034552|||http://purl.uniprot.org/annotation/VAR_034553|||http://purl.uniprot.org/annotation/VAR_052288|||http://purl.uniprot.org/annotation/VAR_052289
http://togogenome.org/gene/9606:ERCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRG2|||http://purl.uniprot.org/uniprot/B3KTH1|||http://purl.uniprot.org/uniprot/P19447                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEVH box|||Disordered|||General transcription and DNA repair factor IIH helicase subunit XPB|||Helicase ATP-binding|||Helicase C-terminal|||Impairs protein folding.|||In TTD2; mild.|||In XP-B; combined with features of Cockayne syndrome; mild.|||In a breast cancer sample; somatic mutation.|||No transcriptional activity of the reconstituted TFIIH complex.|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101987|||http://purl.uniprot.org/annotation/VAR_003632|||http://purl.uniprot.org/annotation/VAR_008186|||http://purl.uniprot.org/annotation/VAR_014344|||http://purl.uniprot.org/annotation/VAR_014766|||http://purl.uniprot.org/annotation/VAR_014767|||http://purl.uniprot.org/annotation/VAR_017294|||http://purl.uniprot.org/annotation/VAR_035942
http://togogenome.org/gene/9606:ITGBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WY35|||http://purl.uniprot.org/uniprot/B4DN32|||http://purl.uniprot.org/uniprot/O95965                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine-rich tandem repeats|||EGF-like|||I|||II|||III|||IV|||IX|||In isoform 2.|||In isoform 3.|||Integrin beta-like protein 1|||N-linked (GlcNAc...) asparagine|||V|||VI|||VII|||VIII|||X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000054386|||http://purl.uniprot.org/annotation/PRO_5001832065|||http://purl.uniprot.org/annotation/VAR_039542|||http://purl.uniprot.org/annotation/VSP_054799|||http://purl.uniprot.org/annotation/VSP_054800
http://togogenome.org/gene/9606:APC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25054|||http://purl.uniprot.org/uniprot/Q4LE70                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM|||ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||Adenomatous polyposis coli N-terminal dimerisation|||Adenomatous polyposis coli protein|||Adenomatous polyposis coli protein basic|||Basic and acidic residues|||Basic region|||Disordered|||EB-1 binding|||Found in a family whose members exhibit gastrointestinal cancers and multiple pigmented cutaneous lesions; unknown pathological significance.|||Highly charged|||Impairs interaction with KHDRBS1.|||In FAP1 and colorectal tumor.|||In FAP1.|||In FAP1; unknown pathological significance.|||In MDB; sporadic.|||In a colorectal cancer sample; somatic mutation.|||In colorectal carcinoma and gastric cancer; from a patient with MMRCS.|||In colorectal carcinoma from a patient with MMRCS.|||In colorectal carcinoma; from a patient with MMRCS.|||In colorectal tumor.|||In gastric cancer.|||In hepatoblastoma.|||In isoform 1B.|||In isoform 2.|||Interaction with AXIN1|||Interaction with DLG1|||Interaction with MAPRE1|||Interaction with catenins|||Loss of interaction with SCRIB.|||May be associated with increased risk of colon and breast cancer.|||May contribute to colorectal tumor development.|||Microtubule tip localization signal|||N-acetylalanine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||Responsible for down-regulation through a process mediated by direct ubiquitination                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064627|||http://purl.uniprot.org/annotation/VAR_005032|||http://purl.uniprot.org/annotation/VAR_005033|||http://purl.uniprot.org/annotation/VAR_005034|||http://purl.uniprot.org/annotation/VAR_005035|||http://purl.uniprot.org/annotation/VAR_005036|||http://purl.uniprot.org/annotation/VAR_005037|||http://purl.uniprot.org/annotation/VAR_005038|||http://purl.uniprot.org/annotation/VAR_005039|||http://purl.uniprot.org/annotation/VAR_005040|||http://purl.uniprot.org/annotation/VAR_005041|||http://purl.uniprot.org/annotation/VAR_005042|||http://purl.uniprot.org/annotation/VAR_005043|||http://purl.uniprot.org/annotation/VAR_005044|||http://purl.uniprot.org/annotation/VAR_005045|||http://purl.uniprot.org/annotation/VAR_005046|||http://purl.uniprot.org/annotation/VAR_005047|||http://purl.uniprot.org/annotation/VAR_005048|||http://purl.uniprot.org/annotation/VAR_005049|||http://purl.uniprot.org/annotation/VAR_005050|||http://purl.uniprot.org/annotation/VAR_005051|||http://purl.uniprot.org/annotation/VAR_005052|||http://purl.uniprot.org/annotation/VAR_005053|||http://purl.uniprot.org/annotation/VAR_005054|||http://purl.uniprot.org/annotation/VAR_005055|||http://purl.uniprot.org/annotation/VAR_005056|||http://purl.uniprot.org/annotation/VAR_005057|||http://purl.uniprot.org/annotation/VAR_008992|||http://purl.uniprot.org/annotation/VAR_008993|||http://purl.uniprot.org/annotation/VAR_008994|||http://purl.uniprot.org/annotation/VAR_009613|||http://purl.uniprot.org/annotation/VAR_009614|||http://purl.uniprot.org/annotation/VAR_009615|||http://purl.uniprot.org/annotation/VAR_009616|||http://purl.uniprot.org/annotation/VAR_009617|||http://purl.uniprot.org/annotation/VAR_012975|||http://purl.uniprot.org/annotation/VAR_012976|||http://purl.uniprot.org/annotation/VAR_017653|||http://purl.uniprot.org/annotation/VAR_017654|||http://purl.uniprot.org/annotation/VAR_017655|||http://purl.uniprot.org/annotation/VAR_020141|||http://purl.uniprot.org/annotation/VAR_020142|||http://purl.uniprot.org/annotation/VAR_035794|||http://purl.uniprot.org/annotation/VAR_053976|||http://purl.uniprot.org/annotation/VAR_053977|||http://purl.uniprot.org/annotation/VAR_053978|||http://purl.uniprot.org/annotation/VAR_065133|||http://purl.uniprot.org/annotation/VSP_004115|||http://purl.uniprot.org/annotation/VSP_059027|||http://purl.uniprot.org/annotation/VSP_059028
http://togogenome.org/gene/9606:EPHB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54760|||http://purl.uniprot.org/uniprot/Q541P7|||http://purl.uniprot.org/uniprot/Q96L35                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect tyrosine phosphorylation; does not affect interaction with RASA1.|||Eph LBD|||Ephrin type-B receptor 4|||Extracellular|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In CMAVM2.|||In CMAVM2; highly decreased tyrosine phosphorylation; highly decreased interaction with RASA1.|||In CMAVM2; loss of tyrosine phosphorylation; loss of interaction with RASA1.|||In CMAVM2; the mutant protein is not detected by Western blot; loss of localization to cell membrane.|||In CMAVM2; unknown pathological significance.|||In LMPHM7; loss of kinase activity.|||In a gastric adenocarcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Reduces binding affinity for EFNB2.|||SAM|||receptor protein-tyrosine kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016834|||http://purl.uniprot.org/annotation/PRO_5014309534|||http://purl.uniprot.org/annotation/PRO_5014589237|||http://purl.uniprot.org/annotation/VAR_042181|||http://purl.uniprot.org/annotation/VAR_042182|||http://purl.uniprot.org/annotation/VAR_042183|||http://purl.uniprot.org/annotation/VAR_042184|||http://purl.uniprot.org/annotation/VAR_042185|||http://purl.uniprot.org/annotation/VAR_042186|||http://purl.uniprot.org/annotation/VAR_042187|||http://purl.uniprot.org/annotation/VAR_042188|||http://purl.uniprot.org/annotation/VAR_042189|||http://purl.uniprot.org/annotation/VAR_071163|||http://purl.uniprot.org/annotation/VAR_078063|||http://purl.uniprot.org/annotation/VAR_078064|||http://purl.uniprot.org/annotation/VAR_081689|||http://purl.uniprot.org/annotation/VAR_081690|||http://purl.uniprot.org/annotation/VAR_081691|||http://purl.uniprot.org/annotation/VAR_081692|||http://purl.uniprot.org/annotation/VAR_081693|||http://purl.uniprot.org/annotation/VAR_081694|||http://purl.uniprot.org/annotation/VAR_081695|||http://purl.uniprot.org/annotation/VAR_081696|||http://purl.uniprot.org/annotation/VAR_081697|||http://purl.uniprot.org/annotation/VAR_081698|||http://purl.uniprot.org/annotation/VAR_081699|||http://purl.uniprot.org/annotation/VAR_081700|||http://purl.uniprot.org/annotation/VAR_081701|||http://purl.uniprot.org/annotation/VAR_081702|||http://purl.uniprot.org/annotation/VAR_081703|||http://purl.uniprot.org/annotation/VAR_081704|||http://purl.uniprot.org/annotation/VAR_081705|||http://purl.uniprot.org/annotation/VAR_081706|||http://purl.uniprot.org/annotation/VAR_081707|||http://purl.uniprot.org/annotation/VAR_081708|||http://purl.uniprot.org/annotation/VAR_081709|||http://purl.uniprot.org/annotation/VAR_081710|||http://purl.uniprot.org/annotation/VAR_081711|||http://purl.uniprot.org/annotation/VAR_081712|||http://purl.uniprot.org/annotation/VAR_081713|||http://purl.uniprot.org/annotation/VAR_081714|||http://purl.uniprot.org/annotation/VAR_081715|||http://purl.uniprot.org/annotation/VAR_081716|||http://purl.uniprot.org/annotation/VAR_081717|||http://purl.uniprot.org/annotation/VAR_081718|||http://purl.uniprot.org/annotation/VAR_081719|||http://purl.uniprot.org/annotation/VAR_081720|||http://purl.uniprot.org/annotation/VAR_081721|||http://purl.uniprot.org/annotation/VAR_081722|||http://purl.uniprot.org/annotation/VAR_081723|||http://purl.uniprot.org/annotation/VAR_081724|||http://purl.uniprot.org/annotation/VAR_081725|||http://purl.uniprot.org/annotation/VSP_056020|||http://purl.uniprot.org/annotation/VSP_056021|||http://purl.uniprot.org/annotation/VSP_056022|||http://purl.uniprot.org/annotation/VSP_056023|||http://purl.uniprot.org/annotation/VSP_056024|||http://purl.uniprot.org/annotation/VSP_056025
http://togogenome.org/gene/9606:KIF3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RU78|||http://purl.uniprot.org/uniprot/O14782                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Globular|||Kinesin motor|||Kinesin-like protein KIF3C|||Polar residues|||Probable disease-associated variant found in a patient with early infantile epileptic encephalopathy.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125397|||http://purl.uniprot.org/annotation/VAR_055120|||http://purl.uniprot.org/annotation/VAR_078709
http://togogenome.org/gene/9606:STRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13033                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Calmodulin-binding|||Caveolin-binding|||Disordered|||In isoform Alpha.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Striatin-3|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051236|||http://purl.uniprot.org/annotation/VAR_054337|||http://purl.uniprot.org/annotation/VSP_006786
http://togogenome.org/gene/9606:H4C5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4R0|||http://purl.uniprot.org/uniprot/P62805                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ufmylation.|||Asymmetric dimethylarginine; by PRMT1; alternate|||Citrulline; alternate|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance; results in early developmental defects when expressed in zebrafish embryos.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H4|||Impaired methylation by N6AMT1.|||In TEBIVANED1.|||In TEBIVANED1; results in severe early developmental defects when expressed in zebrafish embryos; results in defective cell cycle progression when expressed in zebrafish embryos.|||In TEBIVANED2 and TEBIVANED3; unknown pathological significance; does not affect early development when expressed in zebrafish embryos.|||In TEBIVANED2; results in severe early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED3.|||In TEBIVANED3; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in early developmental defects when expressed in zebrafish embryos.|||In TEBIVANED4; results in severe early developmental defects when expressed in zebrafish embryos.|||In a breast cancer sample; somatic mutation.|||N-acetylserine|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine; alternate|||N6-propionyllysine; alternate|||N6-succinyllysine; alternate|||Omega-N-methylarginine; by PRMT1; alternate|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine|||Phosphotyrosine|||Removed|||Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate|||TATA box binding protein associated factor (TAF) histone-like fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158320|||http://purl.uniprot.org/annotation/VAR_036206|||http://purl.uniprot.org/annotation/VAR_086990|||http://purl.uniprot.org/annotation/VAR_086991|||http://purl.uniprot.org/annotation/VAR_086992|||http://purl.uniprot.org/annotation/VAR_086993|||http://purl.uniprot.org/annotation/VAR_086994|||http://purl.uniprot.org/annotation/VAR_086995|||http://purl.uniprot.org/annotation/VAR_086996|||http://purl.uniprot.org/annotation/VAR_086997|||http://purl.uniprot.org/annotation/VAR_086998|||http://purl.uniprot.org/annotation/VAR_086999|||http://purl.uniprot.org/annotation/VAR_087000|||http://purl.uniprot.org/annotation/VAR_087001|||http://purl.uniprot.org/annotation/VAR_087002|||http://purl.uniprot.org/annotation/VAR_087003|||http://purl.uniprot.org/annotation/VAR_087004|||http://purl.uniprot.org/annotation/VAR_087005
http://togogenome.org/gene/9606:MACF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSD7|||http://purl.uniprot.org/uniprot/Q9UPN3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4 X 4 AA tandem repeats of [GS]-S-R-[AR]|||Actin-binding|||Basic and acidic residues|||C-terminal tail|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||EF-hand 1|||EF-hand 2|||GAR|||In LIS9.|||In LIS9; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 23|||LRR 24|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Plectin 1|||Plectin 10|||Plectin 11|||Plectin 2|||Plectin 3|||Plectin 4|||Plectin 5|||Plectin 6|||Plectin 7|||Plectin 8|||Plectin 9|||Polar residues|||SH3|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073449|||http://purl.uniprot.org/annotation/VAR_035451|||http://purl.uniprot.org/annotation/VAR_035452|||http://purl.uniprot.org/annotation/VAR_048625|||http://purl.uniprot.org/annotation/VAR_048626|||http://purl.uniprot.org/annotation/VAR_048627|||http://purl.uniprot.org/annotation/VAR_048628|||http://purl.uniprot.org/annotation/VAR_048629|||http://purl.uniprot.org/annotation/VAR_048630|||http://purl.uniprot.org/annotation/VAR_065256|||http://purl.uniprot.org/annotation/VAR_081966|||http://purl.uniprot.org/annotation/VAR_081967|||http://purl.uniprot.org/annotation/VAR_081968|||http://purl.uniprot.org/annotation/VAR_081969|||http://purl.uniprot.org/annotation/VAR_081970|||http://purl.uniprot.org/annotation/VSP_041390|||http://purl.uniprot.org/annotation/VSP_041391|||http://purl.uniprot.org/annotation/VSP_041392|||http://purl.uniprot.org/annotation/VSP_041393|||http://purl.uniprot.org/annotation/VSP_043626|||http://purl.uniprot.org/annotation/VSP_043627
http://togogenome.org/gene/9606:FZD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSL8|||http://purl.uniprot.org/uniprot/Q9ULW2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-10|||G-protein coupled receptors family 2 profile 2|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013005|||http://purl.uniprot.org/annotation/PRO_5004277828
http://togogenome.org/gene/9606:KRT74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In ADWH; results in disruption of keratin intermediate filament formation in cultured cells.|||In ECTD7; autosomal recessive.|||In HYPT3.|||Keratin, type II cytoskeletal 74|||Linker 1|||Linker 12|||Phosphothreonine|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314885|||http://purl.uniprot.org/annotation/VAR_038096|||http://purl.uniprot.org/annotation/VAR_038097|||http://purl.uniprot.org/annotation/VAR_049806|||http://purl.uniprot.org/annotation/VAR_061299|||http://purl.uniprot.org/annotation/VAR_061300|||http://purl.uniprot.org/annotation/VAR_063587|||http://purl.uniprot.org/annotation/VAR_065951|||http://purl.uniprot.org/annotation/VAR_071383
http://togogenome.org/gene/9606:SIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P81133                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Nuclear localization signal|||PAC|||PAS 1|||PAS 2|||Polar residues|||Single-minded C-terminal|||Single-minded homolog 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127439|||http://purl.uniprot.org/annotation/VAR_034496|||http://purl.uniprot.org/annotation/VAR_034497|||http://purl.uniprot.org/annotation/VAR_049549
http://togogenome.org/gene/9606:PHF20L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQS0|||http://purl.uniprot.org/uniprot/A0A0A8K9A6|||http://purl.uniprot.org/uniprot/A8MW92|||http://purl.uniprot.org/uniprot/Q9H8G4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Agenet|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 4.|||N6-acetyllysine|||PHD finger protein 20 AT hook|||PHD finger protein 20-like protein 1|||PHD-type|||Phosphoserine|||Polar residues|||Tudor|||Tudor 1|||Tudor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336001|||http://purl.uniprot.org/annotation/VSP_033781|||http://purl.uniprot.org/annotation/VSP_033782|||http://purl.uniprot.org/annotation/VSP_033783|||http://purl.uniprot.org/annotation/VSP_040407|||http://purl.uniprot.org/annotation/VSP_040408
http://togogenome.org/gene/9606:CLEC6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EIG7                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||C-type lectin domain family 6 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046635|||http://purl.uniprot.org/annotation/VSP_041514
http://togogenome.org/gene/9606:TPSAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15661                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In allele alpha.|||In allele alpha; requires 2 nucleotide substitutions.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Tryptase alpha/beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027479|||http://purl.uniprot.org/annotation/PRO_0000027480|||http://purl.uniprot.org/annotation/VAR_014557|||http://purl.uniprot.org/annotation/VAR_014558|||http://purl.uniprot.org/annotation/VAR_014559|||http://purl.uniprot.org/annotation/VAR_014560|||http://purl.uniprot.org/annotation/VAR_014561|||http://purl.uniprot.org/annotation/VAR_014562|||http://purl.uniprot.org/annotation/VAR_014563|||http://purl.uniprot.org/annotation/VAR_014564|||http://purl.uniprot.org/annotation/VAR_016102|||http://purl.uniprot.org/annotation/VAR_051830|||http://purl.uniprot.org/annotation/VAR_064277|||http://purl.uniprot.org/annotation/VAR_064278|||http://purl.uniprot.org/annotation/VAR_064279|||http://purl.uniprot.org/annotation/VAR_064280|||http://purl.uniprot.org/annotation/VAR_064281|||http://purl.uniprot.org/annotation/VAR_064282|||http://purl.uniprot.org/annotation/VAR_064283|||http://purl.uniprot.org/annotation/VAR_064284|||http://purl.uniprot.org/annotation/VAR_064285|||http://purl.uniprot.org/annotation/VAR_064286|||http://purl.uniprot.org/annotation/VAR_064287|||http://purl.uniprot.org/annotation/VAR_064288|||http://purl.uniprot.org/annotation/VAR_064289|||http://purl.uniprot.org/annotation/VAR_064290|||http://purl.uniprot.org/annotation/VAR_064291|||http://purl.uniprot.org/annotation/VAR_064292|||http://purl.uniprot.org/annotation/VAR_064293|||http://purl.uniprot.org/annotation/VAR_064294|||http://purl.uniprot.org/annotation/VSP_005375
http://togogenome.org/gene/9606:ADAM23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75077                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disintegrin|||Disintegrin and metalloproteinase domain-containing protein 23|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform Beta.|||In isoform Gamma.|||May bind the integrin receptor|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Significantly lower of adhesion-promoting activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029118|||http://purl.uniprot.org/annotation/PRO_0000029119|||http://purl.uniprot.org/annotation/VSP_012045|||http://purl.uniprot.org/annotation/VSP_012046
http://togogenome.org/gene/9606:ECSCR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q19T08                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Endothelial cell-specific chemotaxis regulator|||Extracellular|||Helical|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000365017
http://togogenome.org/gene/9606:SLC7A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS82                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Asc-type amino acid transporter 1|||Disordered|||Helical|||In a family with cystinuria.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054276|||http://purl.uniprot.org/annotation/VAR_014282|||http://purl.uniprot.org/annotation/VAR_048158
http://togogenome.org/gene/9606:SF3A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DW90|||http://purl.uniprot.org/uniprot/Q12874                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Loss of nuclear location.|||Matrin-type|||N-acetylmethionine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Splicing factor 3A subunit 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000174318
http://togogenome.org/gene/9606:MYADM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96S97                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||MARVEL 1|||MARVEL 2|||Myeloid-associated differentiation marker|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156816
http://togogenome.org/gene/9606:CAMKK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KPJ3|||http://purl.uniprot.org/uniprot/Q8N5S9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase kinase 1|||Calmodulin-binding|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor|||RP domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086141|||http://purl.uniprot.org/annotation/VAR_020531|||http://purl.uniprot.org/annotation/VSP_012140|||http://purl.uniprot.org/annotation/VSP_012141
http://togogenome.org/gene/9606:HOOK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ED9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Protein Hook homolog 2|||Required for localization to the centrosome and induction of aggresome formation|||Sufficient for interaction with CNTRL|||Sufficient for interaction with microtubules                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219194|||http://purl.uniprot.org/annotation/VAR_017575|||http://purl.uniprot.org/annotation/VAR_017576|||http://purl.uniprot.org/annotation/VSP_009342
http://togogenome.org/gene/9606:DDIAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DMA1|||http://purl.uniprot.org/uniprot/Q8IXT1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA damage-induced apoptosis suppressor protein|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311838|||http://purl.uniprot.org/annotation/VAR_037326|||http://purl.uniprot.org/annotation/VAR_037327|||http://purl.uniprot.org/annotation/VAR_037328|||http://purl.uniprot.org/annotation/VAR_037329|||http://purl.uniprot.org/annotation/VAR_037330|||http://purl.uniprot.org/annotation/VSP_029606|||http://purl.uniprot.org/annotation/VSP_029607
http://togogenome.org/gene/9606:USP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK80                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ubiquitin thioesterase activity.|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Nuclear export signal|||Nucleophile|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080648|||http://purl.uniprot.org/annotation/VAR_051531|||http://purl.uniprot.org/annotation/VAR_051532|||http://purl.uniprot.org/annotation/VAR_051533|||http://purl.uniprot.org/annotation/VSP_036717|||http://purl.uniprot.org/annotation/VSP_036718|||http://purl.uniprot.org/annotation/VSP_036719
http://togogenome.org/gene/9606:DCTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14203|||http://purl.uniprot.org/uniprot/Q6MZZ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CLIP1.|||Affects centrosomal localization; when associated with A-145 and A-146.|||Affects centrosomal localization; when associated with A-145 and A-147.|||Affects centrosomal localization; when associated with A-146 and A-147.|||Basic residues|||CAP-Gly|||Disordered|||Dynactin subunit 1|||Found in a patient with hereditary motor and sensory neuropathy; unknown pathological significance.|||In ALS; associated with disease susceptibility.|||In ALS; unknown pathological significance.|||In HMN7B; reduced affinity for microtubules which has been suggested to impair axonal transport; the effect is identical to that of complete loss of the CAP-Gly domain; decreased interaction with MAPRE1; no effect on its interaction with TBCB.|||In PERRYS.|||In PERRYS; diminishes microtubule binding and lead to intracytoplasmic inclusions; significant decrease in motility of dynein-dynactin complex along microtubules; defective in inhibiting microtubule catastrophe in neurons.|||In PERRYS; mutation carriers either do not develop depression or they do develop it late in the disease course.|||In PERRYS; reduced microtubule binding; results in the accumulation of intracytoplasmic inclusions; loss of interaction with CLIP1; significant decrease in motility of dynein-dynactin complex along microtubules.|||In PERRYS; significantly reduced microtubule binding.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 6.|||In isoform p135 and isoform 5.|||Interaction with HPS6|||No effect of its interaction with TBCB; no loss of localization to microtubules.|||No effect on its interaction with CLIP1 and PLK1.|||No loss of localization to nuclear envelope. Decrease in microtubule-binding. No effect on its interaction with CLIP1.|||Non-phosphorylatable by PLK1. Decreased nuclear envelope localization. No loss of microtubule-binding. No effect on its interaction with CLIP1.|||Phosphoserine; by CDK1|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by SLK|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083518|||http://purl.uniprot.org/annotation/VAR_001373|||http://purl.uniprot.org/annotation/VAR_015850|||http://purl.uniprot.org/annotation/VAR_048677|||http://purl.uniprot.org/annotation/VAR_048678|||http://purl.uniprot.org/annotation/VAR_063867|||http://purl.uniprot.org/annotation/VAR_063868|||http://purl.uniprot.org/annotation/VAR_063869|||http://purl.uniprot.org/annotation/VAR_063870|||http://purl.uniprot.org/annotation/VAR_063871|||http://purl.uniprot.org/annotation/VAR_063872|||http://purl.uniprot.org/annotation/VAR_063873|||http://purl.uniprot.org/annotation/VAR_063874|||http://purl.uniprot.org/annotation/VAR_063875|||http://purl.uniprot.org/annotation/VAR_071452|||http://purl.uniprot.org/annotation/VAR_071453|||http://purl.uniprot.org/annotation/VAR_073287|||http://purl.uniprot.org/annotation/VAR_076920|||http://purl.uniprot.org/annotation/VSP_000760|||http://purl.uniprot.org/annotation/VSP_045392|||http://purl.uniprot.org/annotation/VSP_045393|||http://purl.uniprot.org/annotation/VSP_045394|||http://purl.uniprot.org/annotation/VSP_047174
http://togogenome.org/gene/9606:CYP4Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W10                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome P450 4Z1|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051864|||http://purl.uniprot.org/annotation/VAR_048461
http://togogenome.org/gene/9606:PSENEN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ42                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||INTRAMEM|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased APP processing by the gamma-secretase complex.|||Decreased expression levels, and decreased stimulation of presenilin endoproteolysis.|||Gamma-secretase subunit PEN-2|||Helical|||Increased expression at the cell membrane.|||Induces a N-linked glycosylation on N-8.|||Induces a N-linked glycosylation.|||Lumenal|||No effect on APP processing by the gamma-secretase complex.|||No effect.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190900
http://togogenome.org/gene/9606:NAT16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8M0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||N-acetyltransferase|||Probable N-acetyltransferase 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309189|||http://purl.uniprot.org/annotation/VAR_036903|||http://purl.uniprot.org/annotation/VSP_055771|||http://purl.uniprot.org/annotation/VSP_055772
http://togogenome.org/gene/9606:ZNF669                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BR6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 669                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233988|||http://purl.uniprot.org/annotation/VAR_057439|||http://purl.uniprot.org/annotation/VAR_059928|||http://purl.uniprot.org/annotation/VSP_047204
http://togogenome.org/gene/9606:UQCC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A8K8N9|||http://purl.uniprot.org/uniprot/Q4G0I0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Ubiquinol-cytochrome c reductase complex assembly factor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348602
http://togogenome.org/gene/9606:NUP93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1F7                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction.|||In NPHS12; doesnt affect nuclear envelope localization; doesn't affect nuclear pore complex assembly; doesn't abrogate interaction with NUP205; abrogates SMAD4 interaction; abrogates IPO7 interaction; impairs SMAD4 protein import; impairs SMAD4 protein signal transduction into nucleus;.|||In NPHS12; doesnt affect nuclear envelope localization; impairs nuclear pore complex assembly; doesn't abrogate interaction with NUP205; doesn't affect SMAD4 interaction; doesn't affect IPO7 interaction; impairs SMAD4 protein import into nucleus; impairs SMAD4 protein signal transduction.|||In isoform 2.|||Nuclear pore complex protein Nup93|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124782|||http://purl.uniprot.org/annotation/VAR_028160|||http://purl.uniprot.org/annotation/VAR_076473|||http://purl.uniprot.org/annotation/VAR_076474|||http://purl.uniprot.org/annotation/VAR_076475|||http://purl.uniprot.org/annotation/VSP_043117
http://togogenome.org/gene/9606:HAO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K058|||http://purl.uniprot.org/uniprot/Q9UJM8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  2-Hydroxyacid oxidase 1|||FMN hydroxy acid dehydrogenase|||Microbody targeting signal|||N6-succinyllysine|||Phosphoserine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206318
http://togogenome.org/gene/9606:CFAP300                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRQ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 300|||In CILD38; loss of ciliary axoneme inner dynein arm and outer dynein arm structures in patient respiratory epithelial cells.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274276|||http://purl.uniprot.org/annotation/VAR_080472|||http://purl.uniprot.org/annotation/VAR_080473|||http://purl.uniprot.org/annotation/VAR_080474|||http://purl.uniprot.org/annotation/VAR_080475|||http://purl.uniprot.org/annotation/VSP_022694|||http://purl.uniprot.org/annotation/VSP_046692|||http://purl.uniprot.org/annotation/VSP_046693
http://togogenome.org/gene/9606:ACCSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3C1W0|||http://purl.uniprot.org/uniprot/Q4AC99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Aminotransferase class I/classII|||Disordered|||N6-(pyridoxal phosphate)lysine|||Probable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337057|||http://purl.uniprot.org/annotation/VAR_060626
http://togogenome.org/gene/9606:EFNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98172                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Ephrin RBD|||Ephrin-B1|||Ephrin-B1 C-terminal fragment|||Ephrin-B1 intracellular domain|||Extracellular|||Helical|||In CFNS.|||Interaction with ZHX2|||N-linked (GlcNAc...) asparagine|||No effect on gamma-secretase mediated proteolysis of the C-terminal fragment.|||Nuclear localization signal|||PDZ-binding|||Phosphoserine|||Polar residues|||The intracellular domain peptide fails to localize to the nucleus.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008387|||http://purl.uniprot.org/annotation/PRO_0000445791|||http://purl.uniprot.org/annotation/PRO_0000445792|||http://purl.uniprot.org/annotation/VAR_023127|||http://purl.uniprot.org/annotation/VAR_023128|||http://purl.uniprot.org/annotation/VAR_023129|||http://purl.uniprot.org/annotation/VAR_023130|||http://purl.uniprot.org/annotation/VAR_023131|||http://purl.uniprot.org/annotation/VAR_023132|||http://purl.uniprot.org/annotation/VAR_023133|||http://purl.uniprot.org/annotation/VAR_023134|||http://purl.uniprot.org/annotation/VAR_023135|||http://purl.uniprot.org/annotation/VAR_023136|||http://purl.uniprot.org/annotation/VAR_023137|||http://purl.uniprot.org/annotation/VAR_023138|||http://purl.uniprot.org/annotation/VAR_023139|||http://purl.uniprot.org/annotation/VAR_023140|||http://purl.uniprot.org/annotation/VAR_023141|||http://purl.uniprot.org/annotation/VAR_023142|||http://purl.uniprot.org/annotation/VAR_023143|||http://purl.uniprot.org/annotation/VAR_023144|||http://purl.uniprot.org/annotation/VAR_023145|||http://purl.uniprot.org/annotation/VAR_023146|||http://purl.uniprot.org/annotation/VAR_023147|||http://purl.uniprot.org/annotation/VAR_059256
http://togogenome.org/gene/9606:KIF20A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95235                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Globular|||Impairs phosphorylation by PLK1 and recruitment of PLK1 to the spindle.|||In RCM6; loss-of-function variant unable to rescue cardiac defects in zebrafish morphants; results in greatly reduced microtubule activated motor activity; does not localize to the spindle midzone.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF20A|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PLK1|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125460|||http://purl.uniprot.org/annotation/VAR_049704|||http://purl.uniprot.org/annotation/VAR_049705|||http://purl.uniprot.org/annotation/VAR_086018|||http://purl.uniprot.org/annotation/VSP_056007
http://togogenome.org/gene/9606:FAM180B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P0A1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Protein FAM180B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349380|||http://purl.uniprot.org/annotation/VAR_046379
http://togogenome.org/gene/9606:MICOS10-NBL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41271                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  CTCK|||Disordered|||In isoform 2.|||Neuroblastoma suppressor of tumorigenicity 1|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006722|||http://purl.uniprot.org/annotation/VSP_036438
http://togogenome.org/gene/9606:SGPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWX5                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Region|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Proton donor|||Sphingosine-1-phosphate phosphatase 2|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114480|||http://purl.uniprot.org/annotation/VSP_039385
http://togogenome.org/gene/9606:NR1D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8S3|||http://purl.uniprot.org/uniprot/P20393                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Crucial for activation of GJA1|||Disordered|||Modulating|||N6-acetyllysine|||N6-acetyllysine; by KAT5|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 1 group D member 1|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by CDK1|||Polar residues|||Pro residues|||Required for phosphorylation by CSNK1E and cytoplasmic localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053499
http://togogenome.org/gene/9606:NES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48681|||http://purl.uniprot.org/uniprot/Q9H6U9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||Linker 1|||Linker 12|||Linker 2|||N-acetylmethionine|||Nestin|||Phosphoserine|||Phosphothreonine|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063853|||http://purl.uniprot.org/annotation/VAR_049814|||http://purl.uniprot.org/annotation/VAR_049815|||http://purl.uniprot.org/annotation/VAR_049816|||http://purl.uniprot.org/annotation/VAR_049817|||http://purl.uniprot.org/annotation/VAR_049818|||http://purl.uniprot.org/annotation/VAR_061301
http://togogenome.org/gene/9606:SULF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWU6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  3-oxoalanine (Cys)|||Catalytic domain; necessary for arylsulfatase activity|||Cleavage; by furin|||Disordered|||Extracellular sulfatase Sulf-1|||Extracellular sulfatase Sulf-2 secreted form|||Hydrophilic domain; necessary for endoglucosamine-6-sulfatase activity|||Loss of arylsulfatase activity and loss of ability to modulate apoptosis.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||via 3-oxoalanine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033434|||http://purl.uniprot.org/annotation/PRO_0000457756
http://togogenome.org/gene/9606:LZTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NL67|||http://purl.uniprot.org/uniprot/Q8N653                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BTB|||BTB 1|||BTB 2|||Has not effect on protein abundance; does not affect localization to Golgi apparatus; does not affect function in regulation of RAS-MAPK signaling.|||In GLM; increased Ras signaling.|||In GLM; increased Ras signaling; decreased ubiquitination of Ras.|||In NS10 and GLM; increased RAS-MAPK signaling; decreased ubiquitination of Ras; decreased stability; no effect on localization to Golgi apparatus.|||In NS10 and SWNTS2; increased RAS-MAPK signaling; decreased stability; no effect on localization to Golgi apparatus.|||In NS10.|||In NS10; increased RAS-MAPK signaling; decreased stability; no effect on localization to Golgi apparatus.|||In NS10; increased Ras signaling.|||In NS10; unknown pathological significance.|||In NS2 and SWNTS2.|||In NS2.|||In NS2; decreased ubiquitination of Ras.|||In NS2; unknown pathological significance.|||In NS2; unknown pathological significance; no effect on RAS-MAPK signaling; decreased localization to Golgi apparatus; no effect on stability.|||In NS2; unknown pathological significance; no effect on RAS-MAPK signaling; decreased stability.|||In NS2; unknown pathological significance; no effect on RAS-MAPK signaling; no effect on stability.|||In NS2; unknown pathological significance; no effect on RAS-MAPK signaling; strongly decreased stability.|||In NS2; unknown pathological significance; when associated with W-170.|||In NS2; when associated with T-205.|||In SWNTS2.|||In SWNTS2; decreased binding to Ras.|||In SWNTS2; decreased interaction with CUL3; impaired subcellular location; decreased ubiquitination of Ras.|||In SWNTS2; increased RAS-MAPK signaling.|||In SWNTS2; increased Ras signaling.|||In SWNTS2; increased Ras signaling; decreased binding to Ras.|||In SWNTS2; increased Ras signaling; decreased interaction with CUL3; impaired subcellular location.|||In SWNTS2; increased Ras signaling; decreased interaction with CUL3; impaired subcellular location; impaired subcellular location.|||In SWNTS2; increased Ras signaling; impaired subcellular location.|||In SWNTS2; unknown pathological significance.|||In SWNTS2; unknown pathological significance; no effect on stability.|||In SWNTS2; unknown pathological significance; no effect on stability; no effect on localization to Golgi apparatus.|||In SWNTS2; unknown pathological significance; somatic mutation.|||Increased RAS-MAPK signaling.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Leucine-zipper-like transcriptional regulator 1|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119135|||http://purl.uniprot.org/annotation/VAR_071145|||http://purl.uniprot.org/annotation/VAR_071146|||http://purl.uniprot.org/annotation/VAR_071147|||http://purl.uniprot.org/annotation/VAR_071148|||http://purl.uniprot.org/annotation/VAR_071149|||http://purl.uniprot.org/annotation/VAR_071150|||http://purl.uniprot.org/annotation/VAR_071151|||http://purl.uniprot.org/annotation/VAR_075657|||http://purl.uniprot.org/annotation/VAR_075658|||http://purl.uniprot.org/annotation/VAR_075659|||http://purl.uniprot.org/annotation/VAR_075660|||http://purl.uniprot.org/annotation/VAR_075661|||http://purl.uniprot.org/annotation/VAR_075662|||http://purl.uniprot.org/annotation/VAR_075663|||http://purl.uniprot.org/annotation/VAR_081292|||http://purl.uniprot.org/annotation/VAR_081293|||http://purl.uniprot.org/annotation/VAR_081294|||http://purl.uniprot.org/annotation/VAR_081295|||http://purl.uniprot.org/annotation/VAR_081296|||http://purl.uniprot.org/annotation/VAR_081297|||http://purl.uniprot.org/annotation/VAR_081298|||http://purl.uniprot.org/annotation/VAR_081299|||http://purl.uniprot.org/annotation/VAR_081300|||http://purl.uniprot.org/annotation/VAR_081301|||http://purl.uniprot.org/annotation/VAR_081302|||http://purl.uniprot.org/annotation/VAR_081303|||http://purl.uniprot.org/annotation/VAR_081304|||http://purl.uniprot.org/annotation/VAR_081305|||http://purl.uniprot.org/annotation/VAR_081306|||http://purl.uniprot.org/annotation/VAR_081307|||http://purl.uniprot.org/annotation/VAR_081308|||http://purl.uniprot.org/annotation/VAR_081309|||http://purl.uniprot.org/annotation/VAR_081310|||http://purl.uniprot.org/annotation/VAR_081311|||http://purl.uniprot.org/annotation/VAR_081312|||http://purl.uniprot.org/annotation/VAR_081313|||http://purl.uniprot.org/annotation/VAR_081314|||http://purl.uniprot.org/annotation/VAR_081315|||http://purl.uniprot.org/annotation/VAR_081316|||http://purl.uniprot.org/annotation/VAR_081317|||http://purl.uniprot.org/annotation/VAR_081318|||http://purl.uniprot.org/annotation/VAR_081319|||http://purl.uniprot.org/annotation/VAR_081320|||http://purl.uniprot.org/annotation/VAR_081321|||http://purl.uniprot.org/annotation/VAR_081322|||http://purl.uniprot.org/annotation/VAR_081323|||http://purl.uniprot.org/annotation/VAR_081324|||http://purl.uniprot.org/annotation/VAR_081325|||http://purl.uniprot.org/annotation/VAR_081326|||http://purl.uniprot.org/annotation/VAR_081327|||http://purl.uniprot.org/annotation/VAR_081328|||http://purl.uniprot.org/annotation/VAR_081329|||http://purl.uniprot.org/annotation/VAR_081330|||http://purl.uniprot.org/annotation/VAR_081331|||http://purl.uniprot.org/annotation/VAR_081332|||http://purl.uniprot.org/annotation/VAR_081333|||http://purl.uniprot.org/annotation/VAR_086931
http://togogenome.org/gene/9606:RAB2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61019                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Effector region|||In isoform 2.|||N-acetylalanine|||Ras-related protein Rab-2A|||Removed|||Required for interaction with PRKCI|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121066|||http://purl.uniprot.org/annotation/VSP_042917
http://togogenome.org/gene/9606:APIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GX9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.|||Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.|||Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.|||Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.|||Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.|||Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.|||Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.|||Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.|||In isoform 2.|||Methylthioribulose-1-phosphate dehydratase|||Mildly reduced enzyme activity.|||Phosphoserine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239022|||http://purl.uniprot.org/annotation/VAR_026575|||http://purl.uniprot.org/annotation/VAR_026576|||http://purl.uniprot.org/annotation/VAR_026577|||http://purl.uniprot.org/annotation/VAR_026578|||http://purl.uniprot.org/annotation/VSP_044403
http://togogenome.org/gene/9606:KRTAP19-7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SYF9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Keratin-associated protein 19-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223909
http://togogenome.org/gene/9606:FPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25090                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-formyl peptide receptor 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069451
http://togogenome.org/gene/9606:GABRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18507                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with generalized tonic-clonic seizures.|||Found in a patient with idiopathic generalized epilepsy; unknown pathological significance; the currents elicited by mutant receptors are indistinguishable from wild-type; no difference in sensitivity of the mutant receptors to the allosteric regulators zinc and benzodiazepine diazepam compared to wild-type.|||Gamma-aminobutyric acid receptor subunit gamma-2|||Helical|||In DEE74; does not affect protein abundance; decreases cell surface expression; decreases current amplitude in response to GABA; does not affect zinc sensitivity; accelerates activation and prolonges deactivation.|||In DEE74; does not affect protein abundance; decreases cell surface expression; decreases current amplitude in response to GABA; increases zinc sensitivity; accelerates deactivation.|||In DEE74; increases protein abundance; retained in the endoplasmic reticulum decreases; cell surface expression; decreases current amplitude in response to GABA; increases zinc sensitivity; accelerates activation and prolonges deactivation.|||In DEE74; increases protein abundance; retained in the endoplasmic reticulum; decreases cell surface expression; decreases current amplitude in response to GABA; increases zinc sensitivity; accelerates activation and prolonges deactivation.|||In ECA2 and FEB8; abolishes in vitro sensitivity to diazepam.|||In FEB8.|||In GEFSP3 and DEE74; does not affect protein abundance; decreases cell surface expression; decreases current amplitude in response to GABA; increases zinc sensitivity; accelerates deactivation.|||In GEFSP3.|||In isoform 2.|||In isoform 3.|||Interaction with GABARAP|||N-linked (GlcNAc...) asparagine|||Probable disease-associated variant found in a patient with generalized epilepsy with myoclonic atonic seizures, cognitive impairment and behavioral disorder.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000477|||http://purl.uniprot.org/annotation/VAR_014265|||http://purl.uniprot.org/annotation/VAR_014266|||http://purl.uniprot.org/annotation/VAR_038602|||http://purl.uniprot.org/annotation/VAR_065163|||http://purl.uniprot.org/annotation/VAR_065226|||http://purl.uniprot.org/annotation/VAR_071813|||http://purl.uniprot.org/annotation/VAR_078226|||http://purl.uniprot.org/annotation/VAR_078620|||http://purl.uniprot.org/annotation/VAR_082266|||http://purl.uniprot.org/annotation/VAR_082267|||http://purl.uniprot.org/annotation/VAR_082268|||http://purl.uniprot.org/annotation/VAR_082269|||http://purl.uniprot.org/annotation/VAR_082270|||http://purl.uniprot.org/annotation/VSP_061922|||http://purl.uniprot.org/annotation/VSP_061923
http://togogenome.org/gene/9606:BOLA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53S33|||http://purl.uniprot.org/uniprot/Q8N338                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BolA-like protein 3|||In MMDS2.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245501|||http://purl.uniprot.org/annotation/VAR_076180|||http://purl.uniprot.org/annotation/VAR_077910|||http://purl.uniprot.org/annotation/VAR_077911|||http://purl.uniprot.org/annotation/VSP_045787
http://togogenome.org/gene/9606:KNTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50748                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Kinetochore-associated protein 1|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084312|||http://purl.uniprot.org/annotation/VAR_051082|||http://purl.uniprot.org/annotation/VAR_051083|||http://purl.uniprot.org/annotation/VAR_051084|||http://purl.uniprot.org/annotation/VAR_051085|||http://purl.uniprot.org/annotation/VAR_051086|||http://purl.uniprot.org/annotation/VSP_057013|||http://purl.uniprot.org/annotation/VSP_057014|||http://purl.uniprot.org/annotation/VSP_057015
http://togogenome.org/gene/9606:NRBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Nuclear receptor-binding protein 2|||Phosphothreonine|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225608|||http://purl.uniprot.org/annotation/VSP_039308|||http://purl.uniprot.org/annotation/VSP_039309|||http://purl.uniprot.org/annotation/VSP_039310|||http://purl.uniprot.org/annotation/VSP_039311|||http://purl.uniprot.org/annotation/VSP_039312|||http://purl.uniprot.org/annotation/VSP_039313
http://togogenome.org/gene/9606:PPM1M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MI6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PPM-type phosphatase|||Pro residues|||Protein phosphatase 1M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057756|||http://purl.uniprot.org/annotation/VSP_050659|||http://purl.uniprot.org/annotation/VSP_050660|||http://purl.uniprot.org/annotation/VSP_050661|||http://purl.uniprot.org/annotation/VSP_050663|||http://purl.uniprot.org/annotation/VSP_050664|||http://purl.uniprot.org/annotation/VSP_061125|||http://purl.uniprot.org/annotation/VSP_061126|||http://purl.uniprot.org/annotation/VSP_061127
http://togogenome.org/gene/9606:MSANTD3-TMEFF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYR6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||In isoform 2.|||Kazal-like 1|||Kazal-like 2|||Polar residues|||Tomoregulin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286056|||http://purl.uniprot.org/annotation/VAR_032060|||http://purl.uniprot.org/annotation/VSP_024959
http://togogenome.org/gene/9606:SAA2-SAA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LPE2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5001919116
http://togogenome.org/gene/9606:OR8H3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N146                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8H3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150667|||http://purl.uniprot.org/annotation/VAR_024122|||http://purl.uniprot.org/annotation/VAR_034264|||http://purl.uniprot.org/annotation/VAR_034265|||http://purl.uniprot.org/annotation/VAR_060012
http://togogenome.org/gene/9606:PGAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCN3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes shedding of CRIPTO.|||Cytoplasmic|||Disordered|||EGF-like|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||No effect.|||Post-GPI attachment to proteins factor 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022539|||http://purl.uniprot.org/annotation/VAR_025307|||http://purl.uniprot.org/annotation/VAR_025308|||http://purl.uniprot.org/annotation/VAR_057810
http://togogenome.org/gene/9606:ANKRD30A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXX3|||http://purl.uniprot.org/uniprot/R4GNA2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat domain-containing protein 30A|||Basic and acidic residues|||CCDC144C-like coiled-coil|||Disordered|||In a breast cancer sample; somatic mutation.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243905|||http://purl.uniprot.org/annotation/VAR_033504|||http://purl.uniprot.org/annotation/VAR_033505|||http://purl.uniprot.org/annotation/VAR_035611|||http://purl.uniprot.org/annotation/VAR_055515
http://togogenome.org/gene/9606:DEDD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Bipartite nuclear localization signal|||DED|||DNA-binding death effector domain-containing protein 2|||Disordered|||In isoform 2.|||Nuclear localization signal|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191277|||http://purl.uniprot.org/annotation/VSP_010312
http://togogenome.org/gene/9606:WBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969T9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GRAM|||In DFNB107.|||In DFNB107; unknown pathological significance.|||In isoform 2.|||Loss of coactivator activity in presence of estrogen.|||No effect on phosphorylation induced by EGF.|||PPxY motif 1|||PPxY motif 2|||Phosphotyrosine; by YES and SRC|||Pro residues|||Strongly decreases phosphorylation induced by EGF. Abolishes phosphorylation in response to EGF, estrogen and progesterone; when associated with F-231.|||WW domain-binding protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065950|||http://purl.uniprot.org/annotation/VAR_079500|||http://purl.uniprot.org/annotation/VAR_079501|||http://purl.uniprot.org/annotation/VAR_079502|||http://purl.uniprot.org/annotation/VSP_059233
http://togogenome.org/gene/9606:VAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GZV7|||http://purl.uniprot.org/uniprot/P23763                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by C.botulinum neurotoxin type B (BoNT/B, botB)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)|||(Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)|||1000-fold increase in susceptibility to C.botulinum BoNT/D, no change in susceptibility to BoNT/B or BoNT/F.|||Cytoplasmic|||Disordered|||Helical|||Helical; Anchor for type IV membrane protein|||In CMS25; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||No change in susceptibility to C.botulinum BoNT/B, BoNT/D or BoNT/F.|||Phosphoserine|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 1|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206719|||http://purl.uniprot.org/annotation/VAR_082265|||http://purl.uniprot.org/annotation/VSP_006325|||http://purl.uniprot.org/annotation/VSP_029185
http://togogenome.org/gene/9606:B3GNT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C0J1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289207|||http://purl.uniprot.org/annotation/VAR_032600|||http://purl.uniprot.org/annotation/VAR_032601|||http://purl.uniprot.org/annotation/VAR_032602|||http://purl.uniprot.org/annotation/VSP_025962
http://togogenome.org/gene/9606:NSMAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92636                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BEACH|||BEACH-type PH|||GRAM|||In isoform 2.|||Protein FAN|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050975|||http://purl.uniprot.org/annotation/VAR_047023|||http://purl.uniprot.org/annotation/VSP_042036
http://togogenome.org/gene/9606:KCNC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISR9|||http://purl.uniprot.org/uniprot/Q96PR1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  BTB|||Cytoplasmic|||Disordered|||Found in a patient with myoclonic-atonic epilepsy; unknown pathological significance.|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In DEE103.|||In DEE103; affects voltage-gated potassium channel activity; results in a shift in voltage dependence of activation to more hyperpolarized potentials.|||In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it causes a shift in voltage dependence of steady-state activation to more hyperpolarized potentials and results in a significant reduction of potassium currents.|||In DEE103; affects voltage-gated potassium channel activity; when expressed in Xenopus laevis oocytes, it results in a shift in voltage dependence of activation to more hyperpolarized potentials and a slower deactivation time.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Potassium voltage-gated channel subfamily C member 2|||Pro residues|||Probable disease-associated variant found in a patient with generalized epilepsy; loss of voltage-gated potassium channel activity; no current is detected when mutant channels are expressed in Xenopus laevis oocytes.|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310416|||http://purl.uniprot.org/annotation/VAR_087366|||http://purl.uniprot.org/annotation/VAR_087367|||http://purl.uniprot.org/annotation/VAR_087368|||http://purl.uniprot.org/annotation/VAR_087369|||http://purl.uniprot.org/annotation/VAR_087370|||http://purl.uniprot.org/annotation/VAR_087371|||http://purl.uniprot.org/annotation/VAR_087372|||http://purl.uniprot.org/annotation/VAR_087373|||http://purl.uniprot.org/annotation/VAR_087374|||http://purl.uniprot.org/annotation/VSP_029269|||http://purl.uniprot.org/annotation/VSP_029270|||http://purl.uniprot.org/annotation/VSP_029271|||http://purl.uniprot.org/annotation/VSP_029272|||http://purl.uniprot.org/annotation/VSP_044742|||http://purl.uniprot.org/annotation/VSP_046002
http://togogenome.org/gene/9606:SLC25A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3H3|||http://purl.uniprot.org/uniprot/P12235                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP/ATP translocase 1|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important for transport activity|||In MTDPS12A; decreased function in ADP transport.|||In MTDPS12A; severely decreased function in ADP transport.|||In MTDPS12B; loss of function in ADP transport.|||In PEOA2; decreased function in ADP transport.|||In PEOA2; decreased function in ADP transport; inverted direction of ADP:ATP transport, with ATP entering the mitochondrial matrix.|||In PEOA2; inverted direction of ADP:ATP transport, with ATP entering the mitochondrial matrix.|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylglycine|||N6,N6,N6-trimethyllysine|||N6-succinyllysine|||Nucleotide carrier signature motif|||Phosphoserine|||Removed|||S-nitrosocysteine|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090574|||http://purl.uniprot.org/annotation/VAR_012111|||http://purl.uniprot.org/annotation/VAR_012112|||http://purl.uniprot.org/annotation/VAR_022459|||http://purl.uniprot.org/annotation/VAR_022460|||http://purl.uniprot.org/annotation/VAR_038814|||http://purl.uniprot.org/annotation/VAR_038815|||http://purl.uniprot.org/annotation/VAR_078071|||http://purl.uniprot.org/annotation/VAR_078072|||http://purl.uniprot.org/annotation/VAR_078073
http://togogenome.org/gene/9606:TM2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BX74                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||TM2 domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5000060231
http://togogenome.org/gene/9606:DCAF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8C9|||http://purl.uniprot.org/uniprot/Q5TAQ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abrogates cytoplasmic localization.|||Abrogates nuclear localization.|||Basic and acidic residues|||DDB1- and CUL4-associated factor 8|||Disordered|||In GAN2; interaction with DDB1 is decreased.|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||Omega-N-methylarginine; by PRMT1|||Phosphoserine|||Polar residues|||Reduces association with DDB1.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296957|||http://purl.uniprot.org/annotation/VAR_071265|||http://purl.uniprot.org/annotation/VSP_027264|||http://purl.uniprot.org/annotation/VSP_027265
http://togogenome.org/gene/9606:SULT1C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IMI6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Proton acceptor|||Sulfotransferase 1C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249887|||http://purl.uniprot.org/annotation/VAR_033732|||http://purl.uniprot.org/annotation/VAR_033733|||http://purl.uniprot.org/annotation/VAR_033734|||http://purl.uniprot.org/annotation/VAR_052519|||http://purl.uniprot.org/annotation/VSP_020583
http://togogenome.org/gene/9606:ANKRD61                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGH8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||Ankyrin repeat domain-containing protein 61                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328762
http://togogenome.org/gene/9606:ZNF180                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MP75|||http://purl.uniprot.org/uniprot/G5E9B8|||http://purl.uniprot.org/uniprot/Q9UJW8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||Zinc finger protein 180                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047442|||http://purl.uniprot.org/annotation/VAR_030864|||http://purl.uniprot.org/annotation/VAR_030865|||http://purl.uniprot.org/annotation/VAR_030866|||http://purl.uniprot.org/annotation/VSP_056705|||http://purl.uniprot.org/annotation/VSP_056706|||http://purl.uniprot.org/annotation/VSP_056707
http://togogenome.org/gene/9606:CCDC171                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6TFL3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 171|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089727|||http://purl.uniprot.org/annotation/VAR_022803|||http://purl.uniprot.org/annotation/VAR_022804|||http://purl.uniprot.org/annotation/VAR_022805|||http://purl.uniprot.org/annotation/VAR_033685|||http://purl.uniprot.org/annotation/VAR_050841|||http://purl.uniprot.org/annotation/VSP_014445|||http://purl.uniprot.org/annotation/VSP_014446|||http://purl.uniprot.org/annotation/VSP_043768
http://togogenome.org/gene/9606:ST8SIA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92185                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase|||Cytoplasmic|||Enzyme activity is 19% of the wild-type.|||Enzyme activity is 20% of the wild-type. A 10-fold increase in Km value for ganglioside GM3. A 5-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3.|||Enzyme activity is 33% of the wild-type. A 2-fold increase in Km value for ganglioside GM3 and 1.25 fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3.|||Enzyme activity is 42% of the wild-type. A 2.5-fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 2.3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3.|||Enzyme activity is 91% of the wild-type.|||Enzyme activity is 98% of the wild-type.|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149282|||http://purl.uniprot.org/annotation/VSP_047583|||http://purl.uniprot.org/annotation/VSP_047584
http://togogenome.org/gene/9606:GDE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZC3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||GP-PDE|||Glycerophosphodiester phosphodiesterase 1|||Helical|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251944|||http://purl.uniprot.org/annotation/VAR_044018|||http://purl.uniprot.org/annotation/VAR_044019
http://togogenome.org/gene/9606:PTRH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQ48|||http://purl.uniprot.org/uniprot/Q9Y3E5                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Sequence Variant|||Strand|||Transmembrane                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In IMNEPD1.|||Peptidyl-tRNA hydrolase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029862|||http://purl.uniprot.org/annotation/VAR_073386
http://togogenome.org/gene/9606:PPP1R36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LQ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Protein phosphatase 1 regulatory subunit 36                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089893|||http://purl.uniprot.org/annotation/VAR_022999|||http://purl.uniprot.org/annotation/VAR_061612
http://togogenome.org/gene/9606:PTPN22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZW8|||http://purl.uniprot.org/uniprot/G3K0T4|||http://purl.uniprot.org/uniprot/Q9Y2R2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases activity 2 fold.|||Decreases activity 7 fold.|||Disordered|||In T1D, RA, SLE and VTLG; also found in patients with Graves disease, Hashimoto thyroiditis and Addison disease; associated with reduced risk of Crohn disease but not of ulcerative colitis; affects CSK kinase binding; alters B cell receptor signaling and memory B cell proliferation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Loss of phosphorylation by PKC/PRKCD.|||Moderately reduces phosphatase activity.|||No effect on phosphorylation by PKC/PRKCD.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by PKC/PRKCD|||Reduces risk of SLE and RA but not T1D; associated with reduced risk of ulcerative colitis but not of Crohn disease; severely reduces phosphatase activity.|||Severely reduces phosphatase activity.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094775|||http://purl.uniprot.org/annotation/VAR_022605|||http://purl.uniprot.org/annotation/VAR_072629|||http://purl.uniprot.org/annotation/VAR_072630|||http://purl.uniprot.org/annotation/VAR_072631|||http://purl.uniprot.org/annotation/VSP_005134|||http://purl.uniprot.org/annotation/VSP_039725|||http://purl.uniprot.org/annotation/VSP_039726|||http://purl.uniprot.org/annotation/VSP_039727|||http://purl.uniprot.org/annotation/VSP_039728|||http://purl.uniprot.org/annotation/VSP_039729|||http://purl.uniprot.org/annotation/VSP_044428|||http://purl.uniprot.org/annotation/VSP_044429
http://togogenome.org/gene/9606:ADAMTS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95450                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 2|||Cell attachment site|||Disintegrin|||Disordered|||In isoform SpNPI.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029158|||http://purl.uniprot.org/annotation/PRO_0000029159|||http://purl.uniprot.org/annotation/VAR_020058|||http://purl.uniprot.org/annotation/VAR_020059|||http://purl.uniprot.org/annotation/VAR_047927|||http://purl.uniprot.org/annotation/VAR_047928|||http://purl.uniprot.org/annotation/VAR_047929|||http://purl.uniprot.org/annotation/VAR_047930|||http://purl.uniprot.org/annotation/VAR_047931|||http://purl.uniprot.org/annotation/VSP_005497|||http://purl.uniprot.org/annotation/VSP_005498
http://togogenome.org/gene/9606:RNF17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7S1|||http://purl.uniprot.org/uniprot/Q9BXT8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||RING finger protein 17|||RING-type|||Tudor|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183165|||http://purl.uniprot.org/annotation/VAR_024613|||http://purl.uniprot.org/annotation/VAR_028132|||http://purl.uniprot.org/annotation/VAR_028133|||http://purl.uniprot.org/annotation/VAR_052098|||http://purl.uniprot.org/annotation/VAR_052099|||http://purl.uniprot.org/annotation/VAR_052100|||http://purl.uniprot.org/annotation/VAR_052101|||http://purl.uniprot.org/annotation/VSP_005753|||http://purl.uniprot.org/annotation/VSP_005754|||http://purl.uniprot.org/annotation/VSP_033073|||http://purl.uniprot.org/annotation/VSP_033074|||http://purl.uniprot.org/annotation/VSP_033075|||http://purl.uniprot.org/annotation/VSP_033076
http://togogenome.org/gene/9606:SPMIP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNM6                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Sperm-associated microtubule inner protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321824
http://togogenome.org/gene/9606:OR1I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60431                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 1I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150437|||http://purl.uniprot.org/annotation/VAR_034164|||http://purl.uniprot.org/annotation/VAR_034165|||http://purl.uniprot.org/annotation/VAR_034166|||http://purl.uniprot.org/annotation/VAR_034167|||http://purl.uniprot.org/annotation/VAR_062009|||http://purl.uniprot.org/annotation/VAR_080450|||http://purl.uniprot.org/annotation/VAR_080451
http://togogenome.org/gene/9606:GTSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW33                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  CHHC U11-48K-type 1|||CHHC U11-48K-type 2|||Gametocyte-specific factor 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221621
http://togogenome.org/gene/9606:TMEM120A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X266|||http://purl.uniprot.org/uniprot/Q9BXJ8                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||Ion channel TACAN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309339|||http://purl.uniprot.org/annotation/VAR_036933|||http://purl.uniprot.org/annotation/VAR_036934|||http://purl.uniprot.org/annotation/VSP_029148
http://togogenome.org/gene/9606:RPS17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08708                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein eS17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000141525|||http://purl.uniprot.org/annotation/VAR_034478
http://togogenome.org/gene/9606:GYPA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFT7|||http://purl.uniprot.org/uniprot/A0A2R8Y7F9|||http://purl.uniprot.org/uniprot/E9PD10|||http://purl.uniprot.org/uniprot/P02724|||http://purl.uniprot.org/uniprot/Q14419                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes dimerization.|||Cytoplasmic|||Diminishes dimerization.|||Disordered|||Extracellular|||Glycophorin|||Glycophorin-A|||Helical|||In ENAV/MARS antigen.|||In ENEH/Hut antigen.|||In ENEH/Vw antigen.|||In ENEP/HAG antigen.|||In ERIK antigen.|||In M(g) antigen.|||In Mt(a) antigen.|||In N antigen and M(g) antigen.|||In N antigen, M(c) antigen and M(g) antigen.|||In Ny(a) antigen.|||In Or antigen.|||In Os(a) antigen.|||In Ri(a) antigen.|||In Vr antigen.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012134|||http://purl.uniprot.org/annotation/PRO_5003242780|||http://purl.uniprot.org/annotation/PRO_5004183039|||http://purl.uniprot.org/annotation/PRO_5015343120|||http://purl.uniprot.org/annotation/PRO_5039969580|||http://purl.uniprot.org/annotation/VAR_003190|||http://purl.uniprot.org/annotation/VAR_003191|||http://purl.uniprot.org/annotation/VAR_058911|||http://purl.uniprot.org/annotation/VAR_058912|||http://purl.uniprot.org/annotation/VAR_058913|||http://purl.uniprot.org/annotation/VAR_058914|||http://purl.uniprot.org/annotation/VAR_058915|||http://purl.uniprot.org/annotation/VAR_058916|||http://purl.uniprot.org/annotation/VAR_058917|||http://purl.uniprot.org/annotation/VAR_058918|||http://purl.uniprot.org/annotation/VAR_058919|||http://purl.uniprot.org/annotation/VAR_058920|||http://purl.uniprot.org/annotation/VAR_058921|||http://purl.uniprot.org/annotation/VAR_058922|||http://purl.uniprot.org/annotation/VAR_058923|||http://purl.uniprot.org/annotation/VAR_058924|||http://purl.uniprot.org/annotation/VAR_059977|||http://purl.uniprot.org/annotation/VSP_047822|||http://purl.uniprot.org/annotation/VSP_047823
http://togogenome.org/gene/9606:DAOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59103                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  D-amino acid oxidase activator|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079781|||http://purl.uniprot.org/annotation/VAR_014313|||http://purl.uniprot.org/annotation/VAR_050943|||http://purl.uniprot.org/annotation/VSP_004053|||http://purl.uniprot.org/annotation/VSP_004054|||http://purl.uniprot.org/annotation/VSP_044292|||http://purl.uniprot.org/annotation/VSP_044293
http://togogenome.org/gene/9606:PCDHA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003886|||http://purl.uniprot.org/annotation/VAR_024389|||http://purl.uniprot.org/annotation/VAR_048523|||http://purl.uniprot.org/annotation/VAR_059179|||http://purl.uniprot.org/annotation/VSP_000673|||http://purl.uniprot.org/annotation/VSP_000674|||http://purl.uniprot.org/annotation/VSP_008040|||http://purl.uniprot.org/annotation/VSP_008041
http://togogenome.org/gene/9606:PHKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93100                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||In GSD9B.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-acetylalanine|||Phosphorylase b kinase regulatory subunit beta|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Removed|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057736|||http://purl.uniprot.org/annotation/VAR_006187|||http://purl.uniprot.org/annotation/VAR_015536|||http://purl.uniprot.org/annotation/VAR_020857|||http://purl.uniprot.org/annotation/VAR_034056|||http://purl.uniprot.org/annotation/VAR_036486|||http://purl.uniprot.org/annotation/VAR_036487|||http://purl.uniprot.org/annotation/VSP_012445|||http://purl.uniprot.org/annotation/VSP_012446
http://togogenome.org/gene/9606:CRYBG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DQ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Beta/gamma crystallin 'Greek key' 5|||Beta/gamma crystallin 'Greek key' 6|||Beta/gamma crystallin 'Greek key' 7|||Beta/gamma crystallin 'Greek key' 8|||Beta/gamma crystallin 'Greek key' 9|||Disordered|||In isoform 1.|||In isoform 2.|||Phosphoserine|||Polar residues|||RII-binding helix|||Ricin B-type lectin|||Very large A-kinase anchor protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325758|||http://purl.uniprot.org/annotation/VAR_039906|||http://purl.uniprot.org/annotation/VAR_039907|||http://purl.uniprot.org/annotation/VAR_039908|||http://purl.uniprot.org/annotation/VSP_057114|||http://purl.uniprot.org/annotation/VSP_057115|||http://purl.uniprot.org/annotation/VSP_057116
http://togogenome.org/gene/9606:MATK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0G6|||http://purl.uniprot.org/uniprot/P42679                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Megakaryocyte-associated tyrosine-protein kinase|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||SH2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088073|||http://purl.uniprot.org/annotation/VAR_041679|||http://purl.uniprot.org/annotation/VAR_041680|||http://purl.uniprot.org/annotation/VAR_041681|||http://purl.uniprot.org/annotation/VSP_043123|||http://purl.uniprot.org/annotation/VSP_044277
http://togogenome.org/gene/9606:VGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15240                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Antimicrobial peptide VGF[554-577]|||Basic and acidic residues|||Basic residues|||Disordered|||Neuroendocrine regulatory peptide-1|||Neuroendocrine regulatory peptide-2|||Neurosecretory protein VGF|||Phosphoserine; by FAM20C|||Phosphothreonine; by FAM20C|||Polar residues|||Pro residues|||Proline amide|||Pyrrolidone carboxylic acid|||VGF-derived peptide TLQP-21|||VGF-derived peptide TLQP-62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022655|||http://purl.uniprot.org/annotation/PRO_0000403364|||http://purl.uniprot.org/annotation/PRO_0000403365|||http://purl.uniprot.org/annotation/PRO_0000422072|||http://purl.uniprot.org/annotation/PRO_0000446626|||http://purl.uniprot.org/annotation/PRO_0000446627
http://togogenome.org/gene/9606:ATP5F1E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56381                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  ATP synthase subunit epsilon, mitochondrial|||In MC5DN3.|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071662|||http://purl.uniprot.org/annotation/VAR_066211
http://togogenome.org/gene/9606:SMAGP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0VAQ4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Small cell adhesion glycoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328795
http://togogenome.org/gene/9606:C5orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Uncharacterized protein C5orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341210
http://togogenome.org/gene/9606:ZNF689                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CS4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 689                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234008
http://togogenome.org/gene/9606:STEAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHE8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ferric oxidoreductase|||Helical|||STEAP1 protein|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191694|||http://purl.uniprot.org/annotation/VAR_053696|||http://purl.uniprot.org/annotation/VAR_053697
http://togogenome.org/gene/9606:TNXB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95680|||http://purl.uniprot.org/uniprot/O95681|||http://purl.uniprot.org/uniprot/P22105|||http://purl.uniprot.org/uniprot/Q6IPK3|||http://purl.uniprot.org/uniprot/Q9Y464                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cell attachment site|||Disordered|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 1; incomplete|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Fibrinogen C-terminal|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 18|||Fibronectin type-III 19|||Fibronectin type-III 2|||Fibronectin type-III 20|||Fibronectin type-III 21|||Fibronectin type-III 22|||Fibronectin type-III 23|||Fibronectin type-III 24|||Fibronectin type-III 25|||Fibronectin type-III 26|||Fibronectin type-III 27|||Fibronectin type-III 28|||Fibronectin type-III 29|||Fibronectin type-III 3|||Fibronectin type-III 30|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||In EDSCLL.|||In VUR8.|||In VUR8; shows significantly impaired migration in a wound-healing assay; associated with decreased expression of phosphorylated PTK2 protein.|||In isoform 3 and isoform 5.|||In isoform 5.|||In isoform XB-short.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Tenascin-X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007751|||http://purl.uniprot.org/annotation/VAR_020170|||http://purl.uniprot.org/annotation/VAR_020171|||http://purl.uniprot.org/annotation/VAR_020172|||http://purl.uniprot.org/annotation/VAR_021908|||http://purl.uniprot.org/annotation/VAR_024270|||http://purl.uniprot.org/annotation/VAR_044347|||http://purl.uniprot.org/annotation/VAR_046499|||http://purl.uniprot.org/annotation/VAR_046500|||http://purl.uniprot.org/annotation/VAR_046501|||http://purl.uniprot.org/annotation/VAR_055781|||http://purl.uniprot.org/annotation/VAR_055782|||http://purl.uniprot.org/annotation/VAR_055783|||http://purl.uniprot.org/annotation/VAR_055784|||http://purl.uniprot.org/annotation/VAR_059276|||http://purl.uniprot.org/annotation/VAR_059277|||http://purl.uniprot.org/annotation/VAR_072580|||http://purl.uniprot.org/annotation/VAR_072581|||http://purl.uniprot.org/annotation/VAR_072582|||http://purl.uniprot.org/annotation/VSP_059792|||http://purl.uniprot.org/annotation/VSP_059793|||http://purl.uniprot.org/annotation/VSP_059794
http://togogenome.org/gene/9606:KCNN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92952                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Calmodulin-binding|||Disordered|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||In isoform 2.|||Increased inhibition by apamin or d-tubocurarine (IC(50)=11.1 uM). Additive increase in inhibition by apamin or d-tubocurarine (IC(50)=6.3 uM); when associated with D-312. Significant increase in inhibition by apamin (IC(50)=366 pM); when associated with Q-310 and D-312. Significant increase in inhibition by apamin (IC(50)=26 pM); when associated with S-216, Q-310 and D-312.|||Increased inhibition by apamin or d-tubocurarine (IC(50)=62.6 uM). Additive increase in inhibition by apamin or d-tubocurarine (IC(50)=6.3 uM); when associated with N-339. Additive increase in inhibition by apamin; when associated with Q-310. Significant increase in inhibition by apamin (IC(50)=366 pM); when associated with Q-310 and N-339. Significant increase in inhibition by apamin (IC(50)=26 pM); when associated with S-216, Q-310 and N-339.|||Increased inhibition by tetraethylammonium (TEA).|||Loss of inhibition by apamin. No effect on inhibition by d-tubocurarine. Increased inhibition by apamin; when associated with D-312. Significant increase in inhibition by apamin (IC(50)=366 pM); when associated with D-312 and N-339. Significant increase in inhibition by apamin (IC(50)=26 pM); when associated with S-216, D-312 and N-339.|||Pore-forming; Name=Segment H5|||Pro residues|||Significantly increased inhibition by apamin (IC(50)=167 pM). No effect on inhibition by d-tubocurarine and tetraethylammonium (TEA). Significant increase in inhibition by apamin (IC(50)=26 pM); when associated with Q-310, D-312 and N-339.|||Small conductance calcium-activated potassium channel protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000155007|||http://purl.uniprot.org/annotation/VSP_022501
http://togogenome.org/gene/9606:ELP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0PNE2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  Elongator complex protein 6|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274360|||http://purl.uniprot.org/annotation/VSP_022721|||http://purl.uniprot.org/annotation/VSP_022722
http://togogenome.org/gene/9606:ZNF573                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YE8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KRAB|||Zinc finger protein 573                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274877|||http://purl.uniprot.org/annotation/VAR_030356|||http://purl.uniprot.org/annotation/VAR_057426|||http://purl.uniprot.org/annotation/VSP_022894|||http://purl.uniprot.org/annotation/VSP_022895|||http://purl.uniprot.org/annotation/VSP_022896|||http://purl.uniprot.org/annotation/VSP_022897
http://togogenome.org/gene/9606:CAPN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH4|||http://purl.uniprot.org/uniprot/O15484                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2|||Calpain catalytic|||Calpain-5|||Domain III|||In VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207713|||http://purl.uniprot.org/annotation/VAR_069277|||http://purl.uniprot.org/annotation/VAR_069278
http://togogenome.org/gene/9606:TAB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5C8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) S-methylcysteine|||Abolished Cys methylation and ability to bind 'Lys-63'-linked ubiquitin.|||Almost complete loss of AMFR-induced 'Lys-27'-linked ubiquitination.|||CUE|||Disordered|||Disrupted zinc-finger; abolished methylation at C-692.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by MAPKAPK2 and MAPKAPK3|||Phosphothreonine|||Polar residues|||Pro residues|||RanBP2-type|||Removed|||TGF-beta-activated kinase 1 and MAP3K7-binding protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226972|||http://purl.uniprot.org/annotation/VAR_055294|||http://purl.uniprot.org/annotation/VSP_017516
http://togogenome.org/gene/9606:CNFN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYD5                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Cornifelin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261195
http://togogenome.org/gene/9606:ICE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q659A1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Little elongation complex subunit 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297964|||http://purl.uniprot.org/annotation/VSP_041612|||http://purl.uniprot.org/annotation/VSP_041613
http://togogenome.org/gene/9606:ZNF852                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMS4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Phosphoserine|||Zinc finger protein 852                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332125
http://togogenome.org/gene/9606:HCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60741|||http://purl.uniprot.org/uniprot/Q86WJ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cyclic nucleotide-binding|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with childhood focal epilepsy; unknown pathological significance.|||Found in a patient with infantile-onset epilepsy; unknown pathological significance.|||Found in a patient with intellectual disability and language delay; unknown pathological significance.|||Found in a patient with sinus bradychardia; unknown pathological significance; affects channel properties as it results in a negative shift in the threshold voltage of activation and slower activation kinetics compared to the wild-type.|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In DEE24; absence of hyperpolarization-activated currents; highly reduced amount of protein at the cell membrane.|||In DEE24; affects channel gating properties; the half-activation voltage is shifted to the depolarizing direction; significantly faster activation and slower deactivation kinetics than wild-type channel.|||In DEE24; dominant-negative mutation resulting in gain of channel function.|||In DEE24; dominant-negative mutation resulting in loss of channel currents.|||In DEE24; likely benign variant.|||In DEE24; results in a gain of channel function.|||In DEE24; results in absence of hyperpolarization-activated currents; reduced amount of protein at the cell membrane.|||In DEE24; the half-activation voltage is shifted to the depolarizing direction; reduced amount of protein at the cell membrane.|||In DEE24; unknown pathological significance.|||In GEFSP10; affects channel gating properties as the half-activation voltage is shifted to the depolarizing direction; reduced amount of protein at the cell membrane.|||In GEFSP10; affects channel gating properties as the half-activation voltage is shifted to the hyperpolarizing direction.|||In GEFSP10; decreased current densities; half-activation voltage is slightly shifted to the hyperpolarizing direction.|||In GEFSP10; decreased current density; voltage-dependence of activation as well as the activation and deactivation kinetics are not altered.|||In GEFSP10; results in a depolarizing shift of the half-activation voltage and faster activation kinetics.|||In GEFSP10; significantly decreased current densities.|||In GEFSP10; unknown pathological significance.|||In GEFSP10; unknown pathological significance; reduced current density; affects channel gating properties as the half-activation voltage is shifted to the depolarizing direction; neurons expressing mutant channels show increased excitability.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1|||Pro residues|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054107|||http://purl.uniprot.org/annotation/VAR_061105|||http://purl.uniprot.org/annotation/VAR_071825|||http://purl.uniprot.org/annotation/VAR_071826|||http://purl.uniprot.org/annotation/VAR_071827|||http://purl.uniprot.org/annotation/VAR_071828|||http://purl.uniprot.org/annotation/VAR_071829|||http://purl.uniprot.org/annotation/VAR_071830|||http://purl.uniprot.org/annotation/VAR_078216|||http://purl.uniprot.org/annotation/VAR_078217|||http://purl.uniprot.org/annotation/VAR_082653|||http://purl.uniprot.org/annotation/VAR_082654|||http://purl.uniprot.org/annotation/VAR_082655|||http://purl.uniprot.org/annotation/VAR_082656|||http://purl.uniprot.org/annotation/VAR_082657|||http://purl.uniprot.org/annotation/VAR_082658|||http://purl.uniprot.org/annotation/VAR_082659|||http://purl.uniprot.org/annotation/VAR_082660|||http://purl.uniprot.org/annotation/VAR_082661|||http://purl.uniprot.org/annotation/VAR_082662|||http://purl.uniprot.org/annotation/VAR_082663|||http://purl.uniprot.org/annotation/VAR_082664|||http://purl.uniprot.org/annotation/VAR_082665|||http://purl.uniprot.org/annotation/VAR_082666|||http://purl.uniprot.org/annotation/VAR_082667|||http://purl.uniprot.org/annotation/VAR_082668|||http://purl.uniprot.org/annotation/VAR_082669|||http://purl.uniprot.org/annotation/VAR_082670|||http://purl.uniprot.org/annotation/VAR_082671|||http://purl.uniprot.org/annotation/VAR_082672|||http://purl.uniprot.org/annotation/VAR_082673|||http://purl.uniprot.org/annotation/VAR_085692|||http://purl.uniprot.org/annotation/VAR_085693
http://togogenome.org/gene/9606:GIPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5H2|||http://purl.uniprot.org/uniprot/Q8TF65                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||PDZ|||PDZ domain-containing protein GIPC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247188|||http://purl.uniprot.org/annotation/VAR_027084|||http://purl.uniprot.org/annotation/VAR_027085
http://togogenome.org/gene/9606:TAF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15542                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform Short.|||LisH|||NTD2; involved in homo-dimerization; also involved in TFIID-TFIIF contacts in the RNA Pol II pre-initiation complex (PIC)|||Polar residues|||Transcription initiation factor TFIID subunit 5|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051257|||http://purl.uniprot.org/annotation/VAR_018462|||http://purl.uniprot.org/annotation/VSP_006787
http://togogenome.org/gene/9606:LRRCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTJ0|||http://purl.uniprot.org/uniprot/Q9C099                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||Leucine-rich repeat and coiled-coil domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337081|||http://purl.uniprot.org/annotation/VAR_043584|||http://purl.uniprot.org/annotation/VAR_043585|||http://purl.uniprot.org/annotation/VAR_043586|||http://purl.uniprot.org/annotation/VSP_033868
http://togogenome.org/gene/9606:RASL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYN1                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Ras-like protein family member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333868|||http://purl.uniprot.org/annotation/VSP_055845|||http://purl.uniprot.org/annotation/VSP_055846
http://togogenome.org/gene/9606:ACO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21399|||http://purl.uniprot.org/uniprot/Q9HBB2|||http://purl.uniprot.org/uniprot/V9HWB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aconitase A/isopropylmalate dehydratase small subunit swivel|||Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha|||Cytoplasmic aconitate hydratase|||Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.|||Nearly abolishes RNA binding.|||No effect on RNA binding.|||No effect on aconitase activity or on RNA binding.|||No effect on iron-regulated RNA binding. Loss of aconitase activity.|||Phosphothreonine|||Strongly reduced RNA binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076680|||http://purl.uniprot.org/annotation/VAR_048180|||http://purl.uniprot.org/annotation/VAR_048181|||http://purl.uniprot.org/annotation/VAR_069413
http://togogenome.org/gene/9606:RUFY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG59|||http://purl.uniprot.org/uniprot/B4DKC2|||http://purl.uniprot.org/uniprot/Q7L099                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Protein RUFY3|||RUN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245833|||http://purl.uniprot.org/annotation/VSP_041250|||http://purl.uniprot.org/annotation/VSP_041251|||http://purl.uniprot.org/annotation/VSP_041252|||http://purl.uniprot.org/annotation/VSP_041253|||http://purl.uniprot.org/annotation/VSP_041254|||http://purl.uniprot.org/annotation/VSP_041255
http://togogenome.org/gene/9606:INHBE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58166                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||Inhibin beta E chain|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033736|||http://purl.uniprot.org/annotation/PRO_0000033737|||http://purl.uniprot.org/annotation/VAR_036198|||http://purl.uniprot.org/annotation/VAR_036199
http://togogenome.org/gene/9606:KRBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DH65|||http://purl.uniprot.org/uniprot/A5PL33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||KRAB|||Phosphoserine|||Polar residues|||Pro residues|||Protein KRBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300111|||http://purl.uniprot.org/annotation/VAR_056922|||http://purl.uniprot.org/annotation/VAR_068701|||http://purl.uniprot.org/annotation/VSP_027779|||http://purl.uniprot.org/annotation/VSP_027780
http://togogenome.org/gene/9606:SMARCC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VXC8|||http://purl.uniprot.org/uniprot/Q8TAQ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRCT; C-terminus|||BRCT; N-terminus|||Basic and acidic residues|||Chromo|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In CSS8.|||In CSS8; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||MarR-like|||MarR-like, BRCT and chromo domains module|||Myb-like|||N6-(ADP-ribosyl)lysine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SANT|||SWI/SNF complex subunit SMARCC2|||SWIRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197117|||http://purl.uniprot.org/annotation/VAR_082077|||http://purl.uniprot.org/annotation/VAR_082078|||http://purl.uniprot.org/annotation/VAR_082079|||http://purl.uniprot.org/annotation/VAR_082080|||http://purl.uniprot.org/annotation/VAR_082081|||http://purl.uniprot.org/annotation/VAR_082082|||http://purl.uniprot.org/annotation/VAR_082083|||http://purl.uniprot.org/annotation/VAR_082084|||http://purl.uniprot.org/annotation/VSP_012490|||http://purl.uniprot.org/annotation/VSP_012491|||http://purl.uniprot.org/annotation/VSP_044647
http://togogenome.org/gene/9606:GFRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60609                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GDNF family receptor alpha-3|||GPI-anchor amidated asparagine|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010789|||http://purl.uniprot.org/annotation/PRO_0000010790|||http://purl.uniprot.org/annotation/VSP_010942
http://togogenome.org/gene/9606:COL7A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02388|||http://purl.uniprot.org/uniprot/Q59F16                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  4-hydroxyproline|||5-hydroxylysine; alternate|||Acidic residues|||BPTI/Kunitz inhibitor|||Basic and acidic residues|||Cell attachment site|||Collagen alpha-1(VII) chain|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||In DDEB and EBDSC; interferes with collagen VII folding and secretion.|||In DDEB and EBP.|||In DDEB.|||In DDEB/RDEB; mild form.|||In DDEB; also in recessive forms.|||In DDEB; associated with squamous cell carcinoma.|||In DDEB; interferes with collagen VII folding and secretion.|||In DDEB; localized type.|||In EBP.|||In NDNC8.|||In PR-DEB; dominant.|||In RDEB.|||In RDEB; also found in isolated toenail dystrophy.|||In RDEB; localized type; mild.|||In RDEB; mild form.|||In RDEB; mitis type.|||In RDEB; severe and mitis type.|||In RDEB; severe phenotype.|||In RDEB; unknown pathological significance; may affect exon 3 splicing.|||In TBDN.|||In TBDN; also found in isolated toenail dystrophy.|||In a breast cancer sample; somatic mutation.|||In a patient with dystrophic epidermolysis bullosa; mitis type.|||In isoform 2.|||Interchain|||Interrupted collagenous region|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||O-linked (Gal...) hydroxylysine; alternate|||Pro residues|||Reactive bond|||Triple-helical region|||VWFA 1|||VWFA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005761|||http://purl.uniprot.org/annotation/VAR_001809|||http://purl.uniprot.org/annotation/VAR_001810|||http://purl.uniprot.org/annotation/VAR_001811|||http://purl.uniprot.org/annotation/VAR_001812|||http://purl.uniprot.org/annotation/VAR_001813|||http://purl.uniprot.org/annotation/VAR_001814|||http://purl.uniprot.org/annotation/VAR_001815|||http://purl.uniprot.org/annotation/VAR_001816|||http://purl.uniprot.org/annotation/VAR_001817|||http://purl.uniprot.org/annotation/VAR_001818|||http://purl.uniprot.org/annotation/VAR_001819|||http://purl.uniprot.org/annotation/VAR_001820|||http://purl.uniprot.org/annotation/VAR_001821|||http://purl.uniprot.org/annotation/VAR_001822|||http://purl.uniprot.org/annotation/VAR_001823|||http://purl.uniprot.org/annotation/VAR_001825|||http://purl.uniprot.org/annotation/VAR_001826|||http://purl.uniprot.org/annotation/VAR_001827|||http://purl.uniprot.org/annotation/VAR_001828|||http://purl.uniprot.org/annotation/VAR_001829|||http://purl.uniprot.org/annotation/VAR_001830|||http://purl.uniprot.org/annotation/VAR_001831|||http://purl.uniprot.org/annotation/VAR_001832|||http://purl.uniprot.org/annotation/VAR_001833|||http://purl.uniprot.org/annotation/VAR_001834|||http://purl.uniprot.org/annotation/VAR_001835|||http://purl.uniprot.org/annotation/VAR_001836|||http://purl.uniprot.org/annotation/VAR_001837|||http://purl.uniprot.org/annotation/VAR_011160|||http://purl.uniprot.org/annotation/VAR_011161|||http://purl.uniprot.org/annotation/VAR_011162|||http://purl.uniprot.org/annotation/VAR_011163|||http://purl.uniprot.org/annotation/VAR_011164|||http://purl.uniprot.org/annotation/VAR_011165|||http://purl.uniprot.org/annotation/VAR_011166|||http://purl.uniprot.org/annotation/VAR_011167|||http://purl.uniprot.org/annotation/VAR_011168|||http://purl.uniprot.org/annotation/VAR_011169|||http://purl.uniprot.org/annotation/VAR_011170|||http://purl.uniprot.org/annotation/VAR_011171|||http://purl.uniprot.org/annotation/VAR_011172|||http://purl.uniprot.org/annotation/VAR_011173|||http://purl.uniprot.org/annotation/VAR_011174|||http://purl.uniprot.org/annotation/VAR_011175|||http://purl.uniprot.org/annotation/VAR_011176|||http://purl.uniprot.org/annotation/VAR_011177|||http://purl.uniprot.org/annotation/VAR_011178|||http://purl.uniprot.org/annotation/VAR_011179|||http://purl.uniprot.org/annotation/VAR_011180|||http://purl.uniprot.org/annotation/VAR_011181|||http://purl.uniprot.org/annotation/VAR_011182|||http://purl.uniprot.org/annotation/VAR_011183|||http://purl.uniprot.org/annotation/VAR_011184|||http://purl.uniprot.org/annotation/VAR_011185|||http://purl.uniprot.org/annotation/VAR_011186|||http://purl.uniprot.org/annotation/VAR_011187|||http://purl.uniprot.org/annotation/VAR_011188|||http://purl.uniprot.org/annotation/VAR_011189|||http://purl.uniprot.org/annotation/VAR_011190|||http://purl.uniprot.org/annotation/VAR_011191|||http://purl.uniprot.org/annotation/VAR_011192|||http://purl.uniprot.org/annotation/VAR_011193|||http://purl.uniprot.org/annotation/VAR_011194|||http://purl.uniprot.org/annotation/VAR_011195|||http://purl.uniprot.org/annotation/VAR_011196|||http://purl.uniprot.org/annotation/VAR_011197|||http://purl.uniprot.org/annotation/VAR_011198|||http://purl.uniprot.org/annotation/VAR_011199|||http://purl.uniprot.org/annotation/VAR_011200|||http://purl.uniprot.org/annotation/VAR_011201|||http://purl.uniprot.org/annotation/VAR_015519|||http://purl.uniprot.org/annotation/VAR_015520|||http://purl.uniprot.org/annotation/VAR_033786|||http://purl.uniprot.org/annotation/VAR_035740|||http://purl.uniprot.org/annotation/VAR_035741|||http://purl.uniprot.org/annotation/VAR_035742|||http://purl.uniprot.org/annotation/VAR_048766|||http://purl.uniprot.org/annotation/VAR_064994|||http://purl.uniprot.org/annotation/VAR_064995|||http://purl.uniprot.org/annotation/VAR_064996|||http://purl.uniprot.org/annotation/VAR_064997|||http://purl.uniprot.org/annotation/VAR_064998|||http://purl.uniprot.org/annotation/VAR_064999|||http://purl.uniprot.org/annotation/VAR_065000|||http://purl.uniprot.org/annotation/VAR_065001|||http://purl.uniprot.org/annotation/VSP_024026
http://togogenome.org/gene/9606:TNPO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92973                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with the ADAR nuclear localization signal. Abolishes ADAR nuclear import.|||Acidic residues|||Disordered|||HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 16|||HEAT 17|||HEAT 18|||HEAT 19|||HEAT 2|||HEAT 20|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||Important for interaction with cargo nuclear localization signals|||Importin N-terminal|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Transportin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120765|||http://purl.uniprot.org/annotation/VSP_038028|||http://purl.uniprot.org/annotation/VSP_038029
http://togogenome.org/gene/9606:ASB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A047|||http://purl.uniprot.org/uniprot/Q9Y576                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 1|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066923
http://togogenome.org/gene/9606:SCLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NL6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Removed|||Sodium channel and clathrin linker 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317127|||http://purl.uniprot.org/annotation/VAR_038481|||http://purl.uniprot.org/annotation/VSP_030904|||http://purl.uniprot.org/annotation/VSP_030905|||http://purl.uniprot.org/annotation/VSP_030906|||http://purl.uniprot.org/annotation/VSP_030907
http://togogenome.org/gene/9606:ADGRL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2G2|||http://purl.uniprot.org/uniprot/E7ESV6|||http://purl.uniprot.org/uniprot/E7EUP0|||http://purl.uniprot.org/uniprot/E7EUW2|||http://purl.uniprot.org/uniprot/Q9HAR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes FLRT3 binding; when associated with 249-A--A-252.|||Adhesion G protein-coupled receptor L3|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Interaction with FLRT3|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Phosphoserine|||Polar residues|||SUEL-type lectin|||Strongly reduces FLRT3 binding. Abolishes FLRT3 binding; when associated with A-308.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012913|||http://purl.uniprot.org/annotation/PRO_5003217340|||http://purl.uniprot.org/annotation/PRO_5003217521|||http://purl.uniprot.org/annotation/PRO_5003217552|||http://purl.uniprot.org/annotation/VAR_055934|||http://purl.uniprot.org/annotation/VAR_064477|||http://purl.uniprot.org/annotation/VAR_064478|||http://purl.uniprot.org/annotation/VAR_064479|||http://purl.uniprot.org/annotation/VSP_010235|||http://purl.uniprot.org/annotation/VSP_010236|||http://purl.uniprot.org/annotation/VSP_010237|||http://purl.uniprot.org/annotation/VSP_010238|||http://purl.uniprot.org/annotation/VSP_010239|||http://purl.uniprot.org/annotation/VSP_010240
http://togogenome.org/gene/9606:F10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00742|||http://purl.uniprot.org/uniprot/Q5JVE7|||http://purl.uniprot.org/uniprot/Q5JVE8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-3-hydroxyaspartate|||4-carboxyglutamate|||Activated factor Xa heavy chain|||Activation peptide|||Charge relay system|||Coagulation factor X|||Disordered|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2|||Factor X heavy chain|||Factor X light chain|||Gla|||In FA10D.|||In FA10D; Friuli.|||In FA10D; Ketchikan.|||In FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin.|||In FA10D; Padua 3.|||In FA10D; Padua 4.|||In FA10D; Riyadh.|||In FA10D; Roma.|||In FA10D; San Antonio.|||In FA10D; San Giovanni Rotondo.|||In FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor.|||In FA10D; Stockton; 50% decrease in specific activity.|||In FA10D; Tokyo.|||In FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium.|||In FA10D; almost complete loss of activity.|||In FA10D; may affect splicing.|||In FA10D; partial loss of activity.|||In FA10D; significant loss of activity.|||In FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity.|||In FA10D; unknown pathological significance.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-linked (GalNAc...) threonine|||Peptidase S1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000012|||http://purl.uniprot.org/annotation/CAR_000013|||http://purl.uniprot.org/annotation/PRO_0000027786|||http://purl.uniprot.org/annotation/PRO_0000027787|||http://purl.uniprot.org/annotation/PRO_0000027788|||http://purl.uniprot.org/annotation/PRO_0000027789|||http://purl.uniprot.org/annotation/PRO_0000027790|||http://purl.uniprot.org/annotation/PRO_0000027791|||http://purl.uniprot.org/annotation/PRO_5004257906|||http://purl.uniprot.org/annotation/PRO_5014309842|||http://purl.uniprot.org/annotation/VAR_014162|||http://purl.uniprot.org/annotation/VAR_014163|||http://purl.uniprot.org/annotation/VAR_020176|||http://purl.uniprot.org/annotation/VAR_020177|||http://purl.uniprot.org/annotation/VAR_065428|||http://purl.uniprot.org/annotation/VAR_065429|||http://purl.uniprot.org/annotation/VAR_065430|||http://purl.uniprot.org/annotation/VAR_065431|||http://purl.uniprot.org/annotation/VAR_065432|||http://purl.uniprot.org/annotation/VAR_065433|||http://purl.uniprot.org/annotation/VAR_065434|||http://purl.uniprot.org/annotation/VAR_065435|||http://purl.uniprot.org/annotation/VAR_065436|||http://purl.uniprot.org/annotation/VAR_065437|||http://purl.uniprot.org/annotation/VAR_065438|||http://purl.uniprot.org/annotation/VAR_065439|||http://purl.uniprot.org/annotation/VAR_065440|||http://purl.uniprot.org/annotation/VAR_065441|||http://purl.uniprot.org/annotation/VAR_065442|||http://purl.uniprot.org/annotation/VAR_065443|||http://purl.uniprot.org/annotation/VAR_065444|||http://purl.uniprot.org/annotation/VAR_065445|||http://purl.uniprot.org/annotation/VAR_065446|||http://purl.uniprot.org/annotation/VAR_065447|||http://purl.uniprot.org/annotation/VAR_065448|||http://purl.uniprot.org/annotation/VAR_065449|||http://purl.uniprot.org/annotation/VAR_065450|||http://purl.uniprot.org/annotation/VAR_065451|||http://purl.uniprot.org/annotation/VAR_065452|||http://purl.uniprot.org/annotation/VAR_072751|||http://purl.uniprot.org/annotation/VAR_072752|||http://purl.uniprot.org/annotation/VAR_075212|||http://purl.uniprot.org/annotation/VAR_075213
http://togogenome.org/gene/9606:HLA-C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10321|||http://purl.uniprot.org/uniprot/Q6R739|||http://purl.uniprot.org/uniprot/Q95HC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class I histocompatibility antigen, C alpha chain|||Helical|||Ig-like|||Ig-like C1-type|||Impairs N-linked glycosylation resulting in impaired interaction with CANX and CALR chaperones as well as TAPBPL.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02 and allele C*16:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and allele C*18:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*12:02, allele C*14:02, allele C*15:02, allele C*17:01 and allele C*18:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01.|||In allele C*01:02, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*14:02, allele C*15:02 and allele C*16:01.|||In allele C*01:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02 and allele C*16:01.|||In allele C*01:02, allele C*04:01 and allele C*14:02.|||In allele C*01:02, allele C*04:01, allele C*05:01, allele C*14:02 and allele C*18:01.|||In allele C*01:02, allele C*06:02, allele C*14:02 and allele C*16:01.|||In allele C*01:02.|||In allele C*01:02; requires 2 nucleotide substitutions.|||In allele C*02:02, allele C*03:02, allele C*03:04 and allele C*15:02.|||In allele C*02:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01.|||In allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, allele C*12:02, allele C*15:02, allele C*16:01 and allele C*17:01.|||In allele C*02:02, allele C*04:01, allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, allele C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01.|||In allele C*02:02, allele C*04:01, allele C*05:01, allele C*06:02, allele C*15:02, allele C*17:01 and allele C*18:01.|||In allele C*02:02, allele C*06:02 and allele C*12:02.|||In allele C*02:02.|||In allele C*03:02 and allele C*03:04.|||In allele C*03:02 and allele C*03:04; requires 2 nucleotide substitutions.|||In allele C*03:02, allele C*03:04 and allele C*15:02.|||In allele C*03:02, allele C*03:04, allele C*04:01 and allele C*17:01.|||In allele C*03:04, allele C*15:02 and allele C*17:01.|||In allele C*04:01 and allele C*14:02; requires 2 nucleotide substitutions.|||In allele C*04:01, allele C*05:01, allele C*07:04, allele C*08:01, allele C*17:01 and allele C*18:01.|||In allele C*04:01, allele C*05:01, allele C*08:01, allele C*17:01 and allele C*18:01.|||In allele C*04:01, allele C*14:02 and allele C*18:01.|||In allele C*04:01, allele C*17:01 and allele C*18:01.|||In allele C*04:01.|||In allele C*05:01 and C*08:01.|||In allele C*05:01, allele C*06:02, allele C*08:01, allele C*12:02 and allele C*15:02.|||In allele C*05:01, allele C*07:04 and allele C*08:01.|||In allele C*05:01.|||In allele C*07:01, C*15:02.|||In allele C*07:01, allele C*02:02, allele C*03:02, allele C*03:04, allele C*05:01, allele C*06:02, allele C*07:04, allele C*08:01, allele C*12:02, allele C*15:02, allele C*16:01 and allele C*17:01.|||In allele C*07:04.|||In allele C*07:04; requires 2 nucleotide substitutions.|||In allele C*08:01.|||In allele C*15:02.|||In allele C*16:01.|||In allele C*17:01.|||In allele C*17:01; requires 2 nucleotide substitutions.|||In alleles C*01:02, C*03:04.|||In alleles C*01:02, allele C*03:02, allele C*03:04, allele C*04:01, allele C*14:02 and allele C*18:01.|||In alleles C*02:02 and allele C*17:01; requires 2 nucleotide substitutions.|||In alleles C*05:01 and allele C*08:01.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||VL9 epitope ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018868|||http://purl.uniprot.org/annotation/PRO_5004321112|||http://purl.uniprot.org/annotation/PRO_5015098476|||http://purl.uniprot.org/annotation/VAR_082408|||http://purl.uniprot.org/annotation/VAR_082409|||http://purl.uniprot.org/annotation/VAR_082410|||http://purl.uniprot.org/annotation/VAR_082411|||http://purl.uniprot.org/annotation/VAR_082412|||http://purl.uniprot.org/annotation/VAR_082413|||http://purl.uniprot.org/annotation/VAR_082414|||http://purl.uniprot.org/annotation/VAR_082415|||http://purl.uniprot.org/annotation/VAR_082416|||http://purl.uniprot.org/annotation/VAR_082417|||http://purl.uniprot.org/annotation/VAR_082418|||http://purl.uniprot.org/annotation/VAR_082419|||http://purl.uniprot.org/annotation/VAR_082420|||http://purl.uniprot.org/annotation/VAR_082421|||http://purl.uniprot.org/annotation/VAR_082422|||http://purl.uniprot.org/annotation/VAR_082423|||http://purl.uniprot.org/annotation/VAR_082424|||http://purl.uniprot.org/annotation/VAR_082425|||http://purl.uniprot.org/annotation/VAR_082426|||http://purl.uniprot.org/annotation/VAR_082427|||http://purl.uniprot.org/annotation/VAR_082428|||http://purl.uniprot.org/annotation/VAR_082429|||http://purl.uniprot.org/annotation/VAR_082430|||http://purl.uniprot.org/annotation/VAR_082431|||http://purl.uniprot.org/annotation/VAR_082432|||http://purl.uniprot.org/annotation/VAR_082433|||http://purl.uniprot.org/annotation/VAR_082434|||http://purl.uniprot.org/annotation/VAR_082435|||http://purl.uniprot.org/annotation/VAR_082436|||http://purl.uniprot.org/annotation/VAR_082437|||http://purl.uniprot.org/annotation/VAR_082438|||http://purl.uniprot.org/annotation/VAR_082439|||http://purl.uniprot.org/annotation/VAR_082440|||http://purl.uniprot.org/annotation/VAR_082441|||http://purl.uniprot.org/annotation/VAR_082442|||http://purl.uniprot.org/annotation/VAR_082443|||http://purl.uniprot.org/annotation/VAR_082444|||http://purl.uniprot.org/annotation/VAR_082445|||http://purl.uniprot.org/annotation/VAR_082446|||http://purl.uniprot.org/annotation/VAR_082447|||http://purl.uniprot.org/annotation/VAR_082448|||http://purl.uniprot.org/annotation/VAR_082449|||http://purl.uniprot.org/annotation/VAR_082450|||http://purl.uniprot.org/annotation/VAR_082451|||http://purl.uniprot.org/annotation/VAR_082452|||http://purl.uniprot.org/annotation/VAR_082453|||http://purl.uniprot.org/annotation/VAR_082454|||http://purl.uniprot.org/annotation/VAR_082455|||http://purl.uniprot.org/annotation/VAR_082456|||http://purl.uniprot.org/annotation/VAR_082457|||http://purl.uniprot.org/annotation/VAR_082458|||http://purl.uniprot.org/annotation/VAR_082459|||http://purl.uniprot.org/annotation/VAR_082460|||http://purl.uniprot.org/annotation/VAR_082461|||http://purl.uniprot.org/annotation/VAR_082462|||http://purl.uniprot.org/annotation/VAR_082463|||http://purl.uniprot.org/annotation/VAR_082464|||http://purl.uniprot.org/annotation/VAR_082465|||http://purl.uniprot.org/annotation/VAR_082466|||http://purl.uniprot.org/annotation/VAR_082467|||http://purl.uniprot.org/annotation/VAR_082468|||http://purl.uniprot.org/annotation/VAR_082469|||http://purl.uniprot.org/annotation/VAR_082470|||http://purl.uniprot.org/annotation/VAR_082471|||http://purl.uniprot.org/annotation/VAR_082472|||http://purl.uniprot.org/annotation/VAR_082473|||http://purl.uniprot.org/annotation/VAR_082474|||http://purl.uniprot.org/annotation/VAR_082475|||http://purl.uniprot.org/annotation/VAR_082476|||http://purl.uniprot.org/annotation/VAR_082477|||http://purl.uniprot.org/annotation/VAR_082478|||http://purl.uniprot.org/annotation/VAR_082479|||http://purl.uniprot.org/annotation/VAR_082480|||http://purl.uniprot.org/annotation/VAR_082481|||http://purl.uniprot.org/annotation/VAR_082482|||http://purl.uniprot.org/annotation/VSP_060393|||http://purl.uniprot.org/annotation/VSP_060394
http://togogenome.org/gene/9606:DHX29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z478                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DHX29|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245535|||http://purl.uniprot.org/annotation/VAR_026985|||http://purl.uniprot.org/annotation/VAR_052180
http://togogenome.org/gene/9606:ELK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P28324|||http://purl.uniprot.org/uniprot/Q8IXL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ETS|||ETS domain-containing protein Elk-4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204099|||http://purl.uniprot.org/annotation/VSP_001468
http://togogenome.org/gene/9606:PRSS50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY3|||http://purl.uniprot.org/uniprot/Q9UI38                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Loss of catalytic activity.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Probable threonine protease PRSS50                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028492|||http://purl.uniprot.org/annotation/PRO_5014247025|||http://purl.uniprot.org/annotation/VAR_051859|||http://purl.uniprot.org/annotation/VAR_051860
http://togogenome.org/gene/9606:PLSCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15162                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  60% reduction in nuclease activity; when associated with A-12; A-111; A-211 and A-262.|||60% reduction in nuclease activity; when associated with A-12; A-53; A-111 and A-211.|||60% reduction in nuclease activity; when associated with A-12; A-53; A-111 and A-262.|||60% reduction in nuclease activity; when associated with A-12; A-53; A-211 and A-262.|||60% reduction in nuclease activity; when associated with A-53; A-111; A-211 and A-262.|||Complete inactivation of the Ca(2+)-dependent phospholipid scrambling.|||Complete inactivation of the Ca(2+)-dependent phospholipid scrambling. No effect on its nuclease activity.|||Cytoplasmic|||Decrease in phosphorylation.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Interaction with hepatitis C virus E2 glycoprotein|||No induction by PKC/PRKCD.|||No palmitoylation; constitutively localizes in the nucleus. Loss of protection against SARS-CoV-2-containing vesicles.|||Nuclear localization signal|||PPXY motif 1|||PPXY motif 2|||Phospholipid scramblase 1|||Phosphothreonine; by PKC/PRKCD|||Phosphotyrosine; by ABL|||Pro residues|||Proline-rich domain (PRD)|||Reduces the Ca(2+)-dependent phospholipid scrambling.|||S-palmitoyl cysteine|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3|||Significantly impaired anti-SARS-CoV-2 activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100784|||http://purl.uniprot.org/annotation/VAR_034388|||http://purl.uniprot.org/annotation/VSP_055237|||http://purl.uniprot.org/annotation/VSP_055238
http://togogenome.org/gene/9606:TEX13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXU2                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Testis-expressed protein 13B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065701
http://togogenome.org/gene/9606:PAFAH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99487                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Lipid Binding|||Sequence Conflict                                                                                  ^@                                                                                  Charge relay system|||N-myristoyl glycine|||Nucleophile|||Platelet-activating factor acetylhydrolase 2, cytoplasmic|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090383
http://togogenome.org/gene/9606:MCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23508                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Colorectal mutant cancer protein|||Disordered|||Higher membrane localization, reduced formation of lamellipodia, accumulation of MYH10 at the cell cortex.|||In a colorectal cancer sample.|||In colorectal cancer samples; somatic mutation.|||In colorectal cancer samples; somatic mutation; decreased binding to CCAR2; significant decrease in its ability to induce the relocalization of CCAR2 to the cytoplasm; loss of its ability to repress the beta-catenin pathway; loss of its ability to induce the SIRT1-mediated deacetylation of beta-catenin.|||In isoform 2.|||Nuclear localization signal|||PDZ-binding|||Phosphoserine|||Reduced binding to SCRIB.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079333|||http://purl.uniprot.org/annotation/VAR_005141|||http://purl.uniprot.org/annotation/VAR_005142|||http://purl.uniprot.org/annotation/VAR_005143|||http://purl.uniprot.org/annotation/VAR_005144|||http://purl.uniprot.org/annotation/VAR_005145|||http://purl.uniprot.org/annotation/VAR_033753|||http://purl.uniprot.org/annotation/VAR_050905|||http://purl.uniprot.org/annotation/VAR_079267|||http://purl.uniprot.org/annotation/VSP_037660
http://togogenome.org/gene/9606:CC2D2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DHV5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Protein CC2D2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244089|||http://purl.uniprot.org/annotation/VAR_050697|||http://purl.uniprot.org/annotation/VAR_050698|||http://purl.uniprot.org/annotation/VAR_050699|||http://purl.uniprot.org/annotation/VSP_058929|||http://purl.uniprot.org/annotation/VSP_058932|||http://purl.uniprot.org/annotation/VSP_058933|||http://purl.uniprot.org/annotation/VSP_060523|||http://purl.uniprot.org/annotation/VSP_060524|||http://purl.uniprot.org/annotation/VSP_060525
http://togogenome.org/gene/9606:OAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UD1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Out at first protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292427|||http://purl.uniprot.org/annotation/VAR_032993|||http://purl.uniprot.org/annotation/VAR_032994
http://togogenome.org/gene/9606:TRIM14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14142                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform Beta.|||More than 50% loss of interaction with MAVS.|||Tripartite motif-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220370|||http://purl.uniprot.org/annotation/VAR_048399|||http://purl.uniprot.org/annotation/VSP_000510|||http://purl.uniprot.org/annotation/VSP_000511|||http://purl.uniprot.org/annotation/VSP_044097|||http://purl.uniprot.org/annotation/VSP_044098|||http://purl.uniprot.org/annotation/VSP_044099
http://togogenome.org/gene/9606:COMMD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZQ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  COMM|||COMM domain-containing protein 5|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077395|||http://purl.uniprot.org/annotation/VAR_020130|||http://purl.uniprot.org/annotation/VAR_048812
http://togogenome.org/gene/9606:TRPM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A3F4|||http://purl.uniprot.org/uniprot/E9PBI7|||http://purl.uniprot.org/uniprot/G5E9G1|||http://purl.uniprot.org/uniprot/H7BYP1|||http://purl.uniprot.org/uniprot/Q6NW43|||http://purl.uniprot.org/uniprot/Q9H200|||http://purl.uniprot.org/uniprot/Q9HCF6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In CTRCT50.|||In NEDFSS; gain-of-function variant resulting in increased calcium ion transmembrane transport; basal channel activity is increased and the channel is more sensitive to stimulation by heat or the neurosteroid pregnenolone sulfate; the mutant channel can be down-regulated by the TRPM3 antagonist and anti-epileptic drug primidone.|||In NEDFSS; gain-of-function variant resulting in increased calcium ion transmembrane transport; basal channel activity is increased and the channel is more sensitive to stimulation by heat or the neurosteroid pregnenolone sulfate; the mutant channel can be inhibited by the TRPM3 antagonist and anti-epileptic drug primidone.|||In NEDFSS; unknown pathological significance.|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 8, isoform 10 and isoform 12.|||In isoform 3 and isoform 5.|||In isoform 4, isoform 5, isoform 7 and isoform 8.|||In isoform 6.|||In isoform 8.|||Ion transport|||Polar residues|||TRPM SLOG|||TRPM tetramerisation|||Transient receptor potential cation channel subfamily M member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215328|||http://purl.uniprot.org/annotation/VAR_021257|||http://purl.uniprot.org/annotation/VAR_057305|||http://purl.uniprot.org/annotation/VAR_057306|||http://purl.uniprot.org/annotation/VAR_061862|||http://purl.uniprot.org/annotation/VAR_088074|||http://purl.uniprot.org/annotation/VAR_088075|||http://purl.uniprot.org/annotation/VAR_088076|||http://purl.uniprot.org/annotation/VAR_088077|||http://purl.uniprot.org/annotation/VSP_012826|||http://purl.uniprot.org/annotation/VSP_012827|||http://purl.uniprot.org/annotation/VSP_012828|||http://purl.uniprot.org/annotation/VSP_012829|||http://purl.uniprot.org/annotation/VSP_012830|||http://purl.uniprot.org/annotation/VSP_012831|||http://purl.uniprot.org/annotation/VSP_012832|||http://purl.uniprot.org/annotation/VSP_039107|||http://purl.uniprot.org/annotation/VSP_043515|||http://purl.uniprot.org/annotation/VSP_043516
http://togogenome.org/gene/9606:EXT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93063                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Exostosin-2|||Helical; Signal-anchor for type II membrane protein|||In EXT2.|||In EXT2; no effect on oligomeric complex formation with EXT1.|||In SSMS; decreased protein abundance; levels of the EXT2-interacting protein NDST1 are abolished in patient cells.|||In isoform 2.|||In isoform 3.|||In osteochondroma.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149651|||http://purl.uniprot.org/annotation/VAR_002378|||http://purl.uniprot.org/annotation/VAR_012823|||http://purl.uniprot.org/annotation/VAR_012824|||http://purl.uniprot.org/annotation/VAR_012825|||http://purl.uniprot.org/annotation/VAR_012826|||http://purl.uniprot.org/annotation/VAR_012827|||http://purl.uniprot.org/annotation/VAR_012828|||http://purl.uniprot.org/annotation/VAR_012829|||http://purl.uniprot.org/annotation/VAR_033921|||http://purl.uniprot.org/annotation/VAR_076469|||http://purl.uniprot.org/annotation/VAR_076470|||http://purl.uniprot.org/annotation/VSP_001798|||http://purl.uniprot.org/annotation/VSP_046053
http://togogenome.org/gene/9606:CCNC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24863|||http://purl.uniprot.org/uniprot/Q7Z4L3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-C|||Cyclin-like|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080420|||http://purl.uniprot.org/annotation/VSP_043075
http://togogenome.org/gene/9606:MGAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26572                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191384|||http://purl.uniprot.org/annotation/VAR_028272|||http://purl.uniprot.org/annotation/VAR_028273
http://togogenome.org/gene/9606:ELSPBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKL6|||http://purl.uniprot.org/uniprot/Q96BH3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Epididymal sperm-binding protein 1|||Fibronectin type-II|||Fibronectin type-II 1|||Fibronectin type-II 2|||Fibronectin type-II 3|||Fibronectin type-II 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308249|||http://purl.uniprot.org/annotation/PRO_5017444428|||http://purl.uniprot.org/annotation/VAR_036760|||http://purl.uniprot.org/annotation/VAR_036761|||http://purl.uniprot.org/annotation/VAR_036762|||http://purl.uniprot.org/annotation/VAR_036763
http://togogenome.org/gene/9606:TSPAN14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG11                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Necessary and sufficient for interaction with ADAM10|||Tetraspanin-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219261|||http://purl.uniprot.org/annotation/VSP_011878|||http://purl.uniprot.org/annotation/VSP_043194
http://togogenome.org/gene/9606:NBN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DG07|||http://purl.uniprot.org/uniprot/O60934                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Abrogates ATM-dependent phosphorylation.|||Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2.|||BRCT|||Basic and acidic residues|||Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation.|||Decreases ATM binding.|||Disordered|||Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation.|||EEXXXDDL motif|||FHA|||Found in a renal cell carcinoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BC.|||In some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant.|||In some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity.|||Interaction with MTOR, MAPKAP1 and RICTOR|||Mediates interaction with SP100|||Nibrin|||Nibrin C-terminal|||No loss of interaction with KPNA2.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231043|||http://purl.uniprot.org/annotation/VAR_025792|||http://purl.uniprot.org/annotation/VAR_025793|||http://purl.uniprot.org/annotation/VAR_025794|||http://purl.uniprot.org/annotation/VAR_025795|||http://purl.uniprot.org/annotation/VAR_025796|||http://purl.uniprot.org/annotation/VAR_025797|||http://purl.uniprot.org/annotation/VAR_025798|||http://purl.uniprot.org/annotation/VAR_025799|||http://purl.uniprot.org/annotation/VAR_025800|||http://purl.uniprot.org/annotation/VAR_025801|||http://purl.uniprot.org/annotation/VAR_025802|||http://purl.uniprot.org/annotation/VAR_025803|||http://purl.uniprot.org/annotation/VAR_051226|||http://purl.uniprot.org/annotation/VAR_051227|||http://purl.uniprot.org/annotation/VAR_064738
http://togogenome.org/gene/9606:SPMIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SVJ3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein SPMIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274315|||http://purl.uniprot.org/annotation/VSP_022710
http://togogenome.org/gene/9606:SHFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUL5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased efficiency in the interaction with PABPC1 and reduced inhibitory activity against DENV replication.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with PABPC1|||N-acetylserine|||Nuclear export signal|||Nuclear localization signal|||Removed|||Shiftless antiviral inhibitor of ribosomal frameshifting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318701|||http://purl.uniprot.org/annotation/VSP_031272|||http://purl.uniprot.org/annotation/VSP_031273|||http://purl.uniprot.org/annotation/VSP_031274
http://togogenome.org/gene/9606:KIF26A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULI4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In CDCBM11; unknown pathological significance.|||In CDCBM11; unknown pathological significance; results in increased microtubule depolymerization.|||Kinesin motor|||Kinesin-like protein KIF26A|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307299|||http://purl.uniprot.org/annotation/VAR_087893|||http://purl.uniprot.org/annotation/VAR_087894|||http://purl.uniprot.org/annotation/VAR_087895|||http://purl.uniprot.org/annotation/VAR_087896|||http://purl.uniprot.org/annotation/VAR_087897
http://togogenome.org/gene/9606:PSORS1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2IYL0|||http://purl.uniprot.org/uniprot/Q9UIG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Psoriasis susceptibility 1 candidate gene 1 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097057|||http://purl.uniprot.org/annotation/VAR_017391|||http://purl.uniprot.org/annotation/VAR_017392|||http://purl.uniprot.org/annotation/VAR_017393|||http://purl.uniprot.org/annotation/VAR_017394|||http://purl.uniprot.org/annotation/VAR_047088|||http://purl.uniprot.org/annotation/VAR_047089|||http://purl.uniprot.org/annotation/VAR_047090|||http://purl.uniprot.org/annotation/VSP_009008
http://togogenome.org/gene/9606:AHCY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTQ3|||http://purl.uniprot.org/uniprot/P23526                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenosylhomocysteinase|||Affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus.|||Decreased adenosylhomocysteinase activity; when associated with S-84.|||Decreased adenosylhomocysteinase activity; when associated with V-89.|||Does not affect nuclear-cytoplasmic protein distribution resulting in subcellular localization similar to the wild-type protein.|||In HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; reduced thermal stability; decreased adenosylhomocysteinase activity.|||In HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; results in protein aggregation and formation of inclusion bodies.|||In HMAHCHD; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus; severely decreased adenosylhomocysteinase activity; reduced thermal stability.|||In HMAHCHD; loss of adenosylhomocysteinase activity.|||In HMAHCHD; reduced tetramerization; affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus.|||In HMAHCHD; results in high molecular weight protein aggregates; severely decreased function in homocysteine synthesis; affects nuclear-cytoplasmic protein distribution resulting in slightly decreased protein amount in the nucleus.|||In HMAHCHD; severely decreased adenosylhomocysteinase activity measured under reducing conditions; affects protein self-interaction and is able to form tetramers only under reducing conditions; does not affect nuclear-cytoplasmic protein distribution.|||In isoform 2.|||N-acetylserine|||N6-(2-hydroxyisobutyryl)lysine|||No effect on adenosylhomocysteinase activity.|||Phosphoserine|||Phosphotyrosine|||Removed|||S-adenosyl-L-homocysteine hydrolase NAD binding|||Severely decreased adenosylhomocysteinase activity.|||Slightly reduced adenosylhomocysteinase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116902|||http://purl.uniprot.org/annotation/VAR_006934|||http://purl.uniprot.org/annotation/VAR_052286|||http://purl.uniprot.org/annotation/VAR_058588|||http://purl.uniprot.org/annotation/VAR_058589|||http://purl.uniprot.org/annotation/VAR_058590|||http://purl.uniprot.org/annotation/VAR_058591|||http://purl.uniprot.org/annotation/VAR_087996|||http://purl.uniprot.org/annotation/VAR_087997|||http://purl.uniprot.org/annotation/VAR_087998|||http://purl.uniprot.org/annotation/VSP_045404
http://togogenome.org/gene/9606:IFNA16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C397|||http://purl.uniprot.org/uniprot/P05015                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016368|||http://purl.uniprot.org/annotation/PRO_5031033906
http://togogenome.org/gene/9606:COL4A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53420                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  7S domain|||Basic and acidic residues|||Cell attachment site|||Cleavage; by collagenase|||Collagen IV NC1|||Collagen alpha-4(IV) chain|||Disordered|||In APSAR.|||In ATS2.|||In BFH1.|||N-linked (GlcNAc...) asparagine|||Or C-1480 with C-1566|||Or C-1513 with C-1569|||Or C-1588 with C-1683|||Or C-1622 with C-1686|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005850|||http://purl.uniprot.org/annotation/VAR_001912|||http://purl.uniprot.org/annotation/VAR_001913|||http://purl.uniprot.org/annotation/VAR_008148|||http://purl.uniprot.org/annotation/VAR_008149|||http://purl.uniprot.org/annotation/VAR_008150|||http://purl.uniprot.org/annotation/VAR_008151|||http://purl.uniprot.org/annotation/VAR_008152|||http://purl.uniprot.org/annotation/VAR_008153|||http://purl.uniprot.org/annotation/VAR_008154|||http://purl.uniprot.org/annotation/VAR_008155|||http://purl.uniprot.org/annotation/VAR_022069|||http://purl.uniprot.org/annotation/VAR_031622|||http://purl.uniprot.org/annotation/VAR_031623|||http://purl.uniprot.org/annotation/VAR_031624|||http://purl.uniprot.org/annotation/VAR_031625|||http://purl.uniprot.org/annotation/VAR_031626|||http://purl.uniprot.org/annotation/VAR_031627|||http://purl.uniprot.org/annotation/VAR_031628|||http://purl.uniprot.org/annotation/VAR_055680|||http://purl.uniprot.org/annotation/VAR_055681|||http://purl.uniprot.org/annotation/VAR_055682
http://togogenome.org/gene/9606:SLC25A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05141|||http://purl.uniprot.org/uniprot/Q6NVC0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP/ATP translocase 2|||ADP/ATP translocase 2, N-terminally processed|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important for transport activity|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylmethionine|||N-acetylthreonine; in ADP/ATP translocase 2, N-terminally processed|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-malonyllysine|||N6-malonyllysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Nucleotide carrier signature motif|||Phosphoserine|||Removed; alternate|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090579|||http://purl.uniprot.org/annotation/PRO_0000423220|||http://purl.uniprot.org/annotation/VAR_030039
http://togogenome.org/gene/9606:LRRK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q38SD2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Disordered|||In OSMD.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat serine/threonine-protein kinase 1|||Loss of GTP/GDP-binding.|||Loss of autophosphorylation.|||No effect on GTP-binding but loss of subsequent stimulation of kinase activity.|||No effect on GTP-binding but reduction in subsequent stimulation of kinase activity.|||Polar residues|||Protein kinase|||Proton acceptor|||Roc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233377|||http://purl.uniprot.org/annotation/VAR_040674|||http://purl.uniprot.org/annotation/VAR_040675|||http://purl.uniprot.org/annotation/VAR_040676|||http://purl.uniprot.org/annotation/VAR_040677|||http://purl.uniprot.org/annotation/VAR_086690|||http://purl.uniprot.org/annotation/VSP_040119|||http://purl.uniprot.org/annotation/VSP_040120
http://togogenome.org/gene/9606:YTHDF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7W5|||http://purl.uniprot.org/uniprot/A0A087WY31|||http://purl.uniprot.org/uniprot/B4DPX9|||http://purl.uniprot.org/uniprot/Q658Z6|||http://purl.uniprot.org/uniprot/Q7Z739|||http://purl.uniprot.org/uniprot/Q8N3V9|||http://purl.uniprot.org/uniprot/Q8NA80                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by HIV-1 protease|||Disordered|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed|||YTH|||YTH domain-containing family protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230991
http://togogenome.org/gene/9606:DYDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWB3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Splice Variant                                                                                  ^@                                                                                  Chain|||Splice Variant                                                                                  ^@                                                                                  DPY30 domain-containing protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247556|||http://purl.uniprot.org/annotation/VSP_056983
http://togogenome.org/gene/9606:GPATCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NW75                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||G patch domain-containing protein 2|||G-patch|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087566|||http://purl.uniprot.org/annotation/VSP_010527|||http://purl.uniprot.org/annotation/VSP_010528
http://togogenome.org/gene/9606:SPATA31G1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with asthenozoospermia; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Polar residues|||Uncharacterized protein C9orf131                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294443|||http://purl.uniprot.org/annotation/VAR_047239|||http://purl.uniprot.org/annotation/VAR_047240|||http://purl.uniprot.org/annotation/VAR_047241|||http://purl.uniprot.org/annotation/VAR_047242|||http://purl.uniprot.org/annotation/VAR_047243|||http://purl.uniprot.org/annotation/VAR_088336|||http://purl.uniprot.org/annotation/VSP_046224|||http://purl.uniprot.org/annotation/VSP_046225
http://togogenome.org/gene/9606:BLM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKN7|||http://purl.uniprot.org/uniprot/H0YNU5|||http://purl.uniprot.org/uniprot/P54132                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  3' overhang DNA-binding|||3' overhang DNA-binding; via amide nitrogen|||Basic and acidic residues|||Basic residues|||DEAH box|||DNA Holliday junction binding|||Decreased DNAHolliday junction binding.|||Decreased slightly DNAHolliday junction binding.|||Decreased strongly DNAHolliday junction binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HRDC|||Helicase ATP-binding|||Helicase C-terminal|||In BLM.|||N6-acetyllysine|||Necessary for dimerization and homooligomerization|||Necessary for interaction with SPIDR|||Necessary for ssDNA and DNA Holliday junction binding|||No change in ssDNA binding. Decreased DNAHolliday junction binding.|||No change in ssDNA binding. Increased DNAHolliday junction binding.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||RecQ-like DNA helicase BLM|||Reduced intramolecular association between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain. No change in forked duplex DNA helicase activity. No change in DNA 4-way junction branch migration and Holliday junction dissolution activities. No change in suppression of enhanced sister chromatide exchange activity.|||Reduced intramolecular interaction between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain.|||Reduced intramolecular interaction between both the helicase ATP-binding domain and the helicase C-terminal domain with the HRDC domain. No change in forked duplex DNA helicase activity. No change in DNA 4-way junction branch migration and Holliday junction dissolution activities. No change in suppression of enhanced sister chromatide exchange activity.|||Reduced ssDNA binding. Increased DNAHolliday junction binding.|||Reduced ssDNA binding. No change in DNAHolliday junction binding.|||Reduced strongly DNA helicase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205039|||http://purl.uniprot.org/annotation/VAR_006901|||http://purl.uniprot.org/annotation/VAR_006902|||http://purl.uniprot.org/annotation/VAR_006903|||http://purl.uniprot.org/annotation/VAR_009138|||http://purl.uniprot.org/annotation/VAR_009139|||http://purl.uniprot.org/annotation/VAR_009140|||http://purl.uniprot.org/annotation/VAR_014912|||http://purl.uniprot.org/annotation/VAR_016032|||http://purl.uniprot.org/annotation/VAR_016033|||http://purl.uniprot.org/annotation/VAR_022295|||http://purl.uniprot.org/annotation/VAR_022296|||http://purl.uniprot.org/annotation/VAR_022297|||http://purl.uniprot.org/annotation/VAR_022298|||http://purl.uniprot.org/annotation/VAR_022299|||http://purl.uniprot.org/annotation/VAR_022300|||http://purl.uniprot.org/annotation/VAR_022301|||http://purl.uniprot.org/annotation/VAR_051731
http://togogenome.org/gene/9606:AMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48728                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Aminomethyltransferase, mitochondrial|||In NKH.|||In NKH; decreased aminomethyltransferase activity.|||In NKH; loss of aminomethyltransferase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of aminomethyltransferase activity.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010755|||http://purl.uniprot.org/annotation/VAR_007951|||http://purl.uniprot.org/annotation/VAR_007952|||http://purl.uniprot.org/annotation/VAR_007953|||http://purl.uniprot.org/annotation/VAR_007954|||http://purl.uniprot.org/annotation/VAR_007955|||http://purl.uniprot.org/annotation/VAR_016847|||http://purl.uniprot.org/annotation/VAR_016848|||http://purl.uniprot.org/annotation/VAR_074107|||http://purl.uniprot.org/annotation/VAR_078794|||http://purl.uniprot.org/annotation/VAR_078795|||http://purl.uniprot.org/annotation/VAR_078796|||http://purl.uniprot.org/annotation/VSP_042557|||http://purl.uniprot.org/annotation/VSP_043288|||http://purl.uniprot.org/annotation/VSP_045418
http://togogenome.org/gene/9606:RPRML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4K4                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||Phosphoserine|||Reprimo-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312756
http://togogenome.org/gene/9606:IAH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL6|||http://purl.uniprot.org/uniprot/Q05D21|||http://purl.uniprot.org/uniprot/Q2TAA2|||http://purl.uniprot.org/uniprot/Q6NVV8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Isoamyl acetate-hydrolyzing esterase 1 homolog|||N6-succinyllysine|||Nucleophile|||Proton acceptor|||Proton donor|||SGNH hydrolase-type esterase|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315723|||http://purl.uniprot.org/annotation/VSP_056571
http://togogenome.org/gene/9606:KRT6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z428|||http://purl.uniprot.org/uniprot/P02538                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In PC3.|||Keratin, type II cytoskeletal 6A|||Linker 1|||Linker 12|||N-acetylalanine|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063731|||http://purl.uniprot.org/annotation/VAR_003878|||http://purl.uniprot.org/annotation/VAR_017075|||http://purl.uniprot.org/annotation/VAR_017076|||http://purl.uniprot.org/annotation/VAR_017077|||http://purl.uniprot.org/annotation/VAR_021264|||http://purl.uniprot.org/annotation/VAR_035030|||http://purl.uniprot.org/annotation/VAR_072446|||http://purl.uniprot.org/annotation/VAR_072447|||http://purl.uniprot.org/annotation/VAR_072448|||http://purl.uniprot.org/annotation/VAR_072449|||http://purl.uniprot.org/annotation/VAR_072450|||http://purl.uniprot.org/annotation/VAR_072451|||http://purl.uniprot.org/annotation/VAR_072452|||http://purl.uniprot.org/annotation/VAR_072453|||http://purl.uniprot.org/annotation/VAR_072454|||http://purl.uniprot.org/annotation/VAR_072455|||http://purl.uniprot.org/annotation/VAR_072456|||http://purl.uniprot.org/annotation/VAR_072457|||http://purl.uniprot.org/annotation/VAR_072458|||http://purl.uniprot.org/annotation/VAR_072459|||http://purl.uniprot.org/annotation/VAR_072460|||http://purl.uniprot.org/annotation/VAR_072461|||http://purl.uniprot.org/annotation/VAR_072462|||http://purl.uniprot.org/annotation/VAR_072463|||http://purl.uniprot.org/annotation/VAR_072464|||http://purl.uniprot.org/annotation/VAR_072465|||http://purl.uniprot.org/annotation/VAR_072466|||http://purl.uniprot.org/annotation/VAR_072467
http://togogenome.org/gene/9606:CHST13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NET6                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 13|||Cell attachment site|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189671|||http://purl.uniprot.org/annotation/VAR_021477|||http://purl.uniprot.org/annotation/VAR_021478|||http://purl.uniprot.org/annotation/VAR_053698|||http://purl.uniprot.org/annotation/VSP_057175|||http://purl.uniprot.org/annotation/VSP_057176
http://togogenome.org/gene/9606:FBXO32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q498Y9|||http://purl.uniprot.org/uniprot/Q969P5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||F-box|||F-box only protein 32|||In isoform 2.|||Nuclear export signal|||Nuclear localization signal|||Probable disease-associated variant found in patients with familial dilated cardiomyopathy; impairs the formation of SCF complex; reduced ubiquitination of cellular proteins.|||Significantly increases nuclear localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119922|||http://purl.uniprot.org/annotation/VAR_049045|||http://purl.uniprot.org/annotation/VAR_049046|||http://purl.uniprot.org/annotation/VAR_076453|||http://purl.uniprot.org/annotation/VSP_042744
http://togogenome.org/gene/9606:NFKBIZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYH8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with NFKB1/p50|||NF-kappa-B inhibitor zeta|||Nuclear localization signal|||OCA|||Polar residues|||Required for transcriptional activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323577|||http://purl.uniprot.org/annotation/VAR_039547|||http://purl.uniprot.org/annotation/VSP_032022|||http://purl.uniprot.org/annotation/VSP_032023
http://togogenome.org/gene/9606:ZNF581                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0T4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Polar residues|||Zinc finger protein 581                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047673
http://togogenome.org/gene/9606:FER                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16591|||http://purl.uniprot.org/uniprot/Q6PEJ9|||http://purl.uniprot.org/uniprot/W0S0X4|||http://purl.uniprot.org/uniprot/W0S1B5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes kinase activity.|||Abolishes kinase activity. Abolishes location at microtubules.|||F-BAR|||Important for interaction with membranes containing phosphoinositides|||In a lung small cell carcinoma sample; somatic mutation.|||In an ovarian Endometrioid carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2|||Tyrosine-protein kinase Fer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088084|||http://purl.uniprot.org/annotation/VAR_006282|||http://purl.uniprot.org/annotation/VAR_041691|||http://purl.uniprot.org/annotation/VAR_041692|||http://purl.uniprot.org/annotation/VAR_041693|||http://purl.uniprot.org/annotation/VAR_041694|||http://purl.uniprot.org/annotation/VAR_041695|||http://purl.uniprot.org/annotation/VAR_041696|||http://purl.uniprot.org/annotation/VAR_051695|||http://purl.uniprot.org/annotation/VSP_041765|||http://purl.uniprot.org/annotation/VSP_043846|||http://purl.uniprot.org/annotation/VSP_043847
http://togogenome.org/gene/9606:ZNF844                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSG8|||http://purl.uniprot.org/uniprot/Q08AG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 844                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349877|||http://purl.uniprot.org/annotation/VAR_059941|||http://purl.uniprot.org/annotation/VAR_059942|||http://purl.uniprot.org/annotation/VAR_059943|||http://purl.uniprot.org/annotation/VAR_059944|||http://purl.uniprot.org/annotation/VAR_059945|||http://purl.uniprot.org/annotation/VAR_059946|||http://purl.uniprot.org/annotation/VAR_059947|||http://purl.uniprot.org/annotation/VAR_059948|||http://purl.uniprot.org/annotation/VAR_061980
http://togogenome.org/gene/9606:CEP152                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94986|||http://purl.uniprot.org/uniprot/Q3B7A2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Centrosomal protein of 152 kDa|||Disordered|||Impairs interaction with PLK4; impaired procentriole assembly and chromosome segregation.|||In MCPH9.|||In SCKL5.|||In isoform 1 and isoform 2.|||In isoform 1.|||In isoform 3.|||Interaction with PLK4|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089462|||http://purl.uniprot.org/annotation/VAR_047932|||http://purl.uniprot.org/annotation/VAR_050779|||http://purl.uniprot.org/annotation/VAR_050780|||http://purl.uniprot.org/annotation/VAR_050781|||http://purl.uniprot.org/annotation/VAR_063813|||http://purl.uniprot.org/annotation/VAR_065258|||http://purl.uniprot.org/annotation/VSP_035981|||http://purl.uniprot.org/annotation/VSP_035983|||http://purl.uniprot.org/annotation/VSP_035984|||http://purl.uniprot.org/annotation/VSP_047002
http://togogenome.org/gene/9606:GPR12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2F5|||http://purl.uniprot.org/uniprot/B4DG25|||http://purl.uniprot.org/uniprot/P47775                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 12|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069527|||http://purl.uniprot.org/annotation/PRO_5002803536
http://togogenome.org/gene/9606:SPTY2D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D10                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for interaction with DNA|||Important for interaction with histones|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Protein SPT2 homolog|||Strongly reduces affinity for histones.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315736|||http://purl.uniprot.org/annotation/VAR_038298|||http://purl.uniprot.org/annotation/VAR_038299|||http://purl.uniprot.org/annotation/VAR_038300|||http://purl.uniprot.org/annotation/VSP_030688|||http://purl.uniprot.org/annotation/VSP_030689|||http://purl.uniprot.org/annotation/VSP_030690
http://togogenome.org/gene/9606:CST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01037                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Mass|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Mass|||Motif|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cystatin-SN|||Reactive site|||Secondary area of contact|||Variant Leu-31.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006649|||http://purl.uniprot.org/annotation/VAR_028932|||http://purl.uniprot.org/annotation/VAR_028933|||http://purl.uniprot.org/annotation/VAR_028934|||http://purl.uniprot.org/annotation/VAR_028935|||http://purl.uniprot.org/annotation/VAR_028936
http://togogenome.org/gene/9606:CCT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99832                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Omega-N-methylarginine|||Removed; alternate|||T-complex protein 1 subunit eta|||T-complex protein 1 subunit eta, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000128365|||http://purl.uniprot.org/annotation/PRO_0000434391|||http://purl.uniprot.org/annotation/VAR_052269|||http://purl.uniprot.org/annotation/VSP_043572|||http://purl.uniprot.org/annotation/VSP_043573|||http://purl.uniprot.org/annotation/VSP_043574
http://togogenome.org/gene/9606:NFKBIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25963                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN; partial|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Almost abolished ability to inhibit NF-kappa-BDNA-binding activity; when associated with A-210.|||Almost abolished ability to inhibit NF-kappa-BDNA-binding activity; when associated with A-244.|||Basic and acidic residues|||Decrease in phosphorylation and degradation; when associated with T-32.|||Decrease in phosphorylation and degradation; when associated with T-36.|||Destruction motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Greatly reduced nuclear localization. Great reduction in its ability to inhibit DNA binding of RELA.|||In EDAID2.|||Little change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-38.|||Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-21. Does not affect activation by FK506.|||Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-22. Does not affect activation by FK506.|||Loss in phosphorylation; when associated with A-31.|||Loss of phosphorylation, ubiquitination and degradation; when associated with A-36. Abolished activation by FK506.|||Loss of phosphorylation, ubiquitination, and degradation; when associated with A-32. Does not affect activation by FK506.|||Loss of phosphorylation; when associated with A-35.|||Mimics phosphorylation; promoting ubiquitination and degradation; when associated with E-32.|||Mimics phosphorylation; promoting ubiquitination and degradation; when associated with E-36.|||NF-kappa-B inhibitor alpha|||No change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-47.|||No change neither in phosphorylation, nor on degradation.|||No inducible ubiquitination nor protein degradation.|||No nuclear export.|||No phosphorylation.|||Nuclear export signal|||Nuclear import signal|||Phosphoserine; by CK2|||Phosphoserine; by IKKA and IKKE|||Phosphoserine; by IKKA, IKKB, IKKE and TBK1|||Phosphothreonine; by CK2|||Phosphotyrosine; by Tyr-kinases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066999|||http://purl.uniprot.org/annotation/VAR_034871
http://togogenome.org/gene/9606:ACY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HD9                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Hydrolytic domain|||N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming)|||Shielding domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000216875|||http://purl.uniprot.org/annotation/VAR_048341|||http://purl.uniprot.org/annotation/VAR_048342
http://togogenome.org/gene/9606:TSPYL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ04                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Testis-specific Y-encoded-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185673|||http://purl.uniprot.org/annotation/VAR_050228
http://togogenome.org/gene/9606:TMEM59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6Z8|||http://purl.uniprot.org/uniprot/Q5T703|||http://purl.uniprot.org/uniprot/Q9BXS4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATG16L1-binding motif|||Cytoplasmic|||Does not affect ability to activate LC3.|||Does not affect ability to activate LC3. No effect on interaction with ATG16L1.|||Extracellular|||Helical|||Impaired ability to activate LC3. Impaired interaction with ATG16L1.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with ATG16L1.|||Phosphothreonine|||Transmembrane protein 59                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003003|||http://purl.uniprot.org/annotation/PRO_5004262290|||http://purl.uniprot.org/annotation/PRO_5014586921|||http://purl.uniprot.org/annotation/VAR_063397
http://togogenome.org/gene/9606:TRIM29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5V5|||http://purl.uniprot.org/uniprot/B7Z8U9|||http://purl.uniprot.org/uniprot/E9PRL4|||http://purl.uniprot.org/uniprot/Q14134                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform Beta.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Tripartite motif-containing protein 29                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056242|||http://purl.uniprot.org/annotation/VAR_035962|||http://purl.uniprot.org/annotation/VSP_011999
http://togogenome.org/gene/9606:NKX2-6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCS4                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Nkx-2.6|||In CTHM.|||In CTHM; impairs transcriptional activation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300262|||http://purl.uniprot.org/annotation/VAR_063278|||http://purl.uniprot.org/annotation/VAR_073164|||http://purl.uniprot.org/annotation/VAR_073165
http://togogenome.org/gene/9606:SERF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75920                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreases SNCA binding.|||Disordered|||Drastically decreases SNCA binding.|||In isoform Short.|||Inhibits SNCA binding.|||No effect on SNCA binding.|||Required for SNCA binding|||Slightly decreases SNCA binding.|||Small EDRK-rich factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050710|||http://purl.uniprot.org/annotation/VSP_006057
http://togogenome.org/gene/9606:CHST12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRB3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Carbohydrate sulfotransferase 12|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189668|||http://purl.uniprot.org/annotation/VAR_021471|||http://purl.uniprot.org/annotation/VAR_021472|||http://purl.uniprot.org/annotation/VAR_021473|||http://purl.uniprot.org/annotation/VAR_021474|||http://purl.uniprot.org/annotation/VAR_033738
http://togogenome.org/gene/9606:MYO9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RTY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||Disordered|||Helical|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||In CMS24; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Myosin motor|||Neck or regulatory domain|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Polar residues|||Ras-associating|||Rho-GAP|||Tail|||Unconventional myosin-IXa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348440|||http://purl.uniprot.org/annotation/VAR_046165|||http://purl.uniprot.org/annotation/VAR_046166|||http://purl.uniprot.org/annotation/VAR_046167|||http://purl.uniprot.org/annotation/VAR_046168|||http://purl.uniprot.org/annotation/VAR_046169|||http://purl.uniprot.org/annotation/VAR_046170|||http://purl.uniprot.org/annotation/VAR_046171|||http://purl.uniprot.org/annotation/VAR_046172|||http://purl.uniprot.org/annotation/VAR_046173|||http://purl.uniprot.org/annotation/VAR_046174|||http://purl.uniprot.org/annotation/VAR_046175|||http://purl.uniprot.org/annotation/VAR_046176|||http://purl.uniprot.org/annotation/VAR_046177|||http://purl.uniprot.org/annotation/VAR_056189|||http://purl.uniprot.org/annotation/VAR_081671|||http://purl.uniprot.org/annotation/VAR_081672|||http://purl.uniprot.org/annotation/VAR_081673|||http://purl.uniprot.org/annotation/VAR_081674|||http://purl.uniprot.org/annotation/VAR_081675|||http://purl.uniprot.org/annotation/VAR_082148|||http://purl.uniprot.org/annotation/VSP_035156|||http://purl.uniprot.org/annotation/VSP_035157|||http://purl.uniprot.org/annotation/VSP_035158|||http://purl.uniprot.org/annotation/VSP_035159|||http://purl.uniprot.org/annotation/VSP_035160
http://togogenome.org/gene/9606:HSD17B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4J1|||http://purl.uniprot.org/uniprot/B2R659|||http://purl.uniprot.org/uniprot/B3KSP2|||http://purl.uniprot.org/uniprot/P51659                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3R)-hydroxyacyl-CoA dehydrogenase|||Completely inactive.|||Enoyl-CoA hydratase 2|||In DBPD.|||In DBPD; no dehydrogenase activity.|||In DBPD; the mutation leads to an unstable protein.|||In PRLTS1.|||In isoform 2.|||In isoform 3.|||MaoC-like|||Microbody targeting signal|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect.|||No hydratase activity.|||Peroxisomal multifunctional enzyme type 2|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||SCP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054583|||http://purl.uniprot.org/annotation/PRO_0000400082|||http://purl.uniprot.org/annotation/PRO_0000400083|||http://purl.uniprot.org/annotation/VAR_014872|||http://purl.uniprot.org/annotation/VAR_014873|||http://purl.uniprot.org/annotation/VAR_014874|||http://purl.uniprot.org/annotation/VAR_024625|||http://purl.uniprot.org/annotation/VAR_037576|||http://purl.uniprot.org/annotation/VAR_052309|||http://purl.uniprot.org/annotation/VAR_052310|||http://purl.uniprot.org/annotation/VAR_052311|||http://purl.uniprot.org/annotation/VAR_052312|||http://purl.uniprot.org/annotation/VAR_052313|||http://purl.uniprot.org/annotation/VAR_052314|||http://purl.uniprot.org/annotation/VAR_052315|||http://purl.uniprot.org/annotation/VAR_065906|||http://purl.uniprot.org/annotation/VAR_065907|||http://purl.uniprot.org/annotation/VAR_065908|||http://purl.uniprot.org/annotation/VSP_046152|||http://purl.uniprot.org/annotation/VSP_046153
http://togogenome.org/gene/9606:C1QL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B0J0F3|||http://purl.uniprot.org/uniprot/Q5VWW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C1q|||Collagen-like|||Complement C1q-like protein 3|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274337|||http://purl.uniprot.org/annotation/PRO_5035366278|||http://purl.uniprot.org/annotation/VSP_027130|||http://purl.uniprot.org/annotation/VSP_027131
http://togogenome.org/gene/9606:ITGB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXP3|||http://purl.uniprot.org/uniprot/B4E2B8|||http://purl.uniprot.org/uniprot/E9PEE8|||http://purl.uniprot.org/uniprot/P18564                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||Extracellular|||Helical|||In AI1H.|||In isoform 2.|||Integrin beta|||Integrin beta subunit VWA|||Integrin beta subunit cytoplasmic|||Integrin beta subunit tail|||Integrin beta-6|||Interaction with HAX1|||N-linked (GlcNAc...) asparagine|||PSI|||VWFA|||in ADMIDAS binding site|||in ADMIDAS binding site and liganded-open conformation|||in ADMIDAS binding site and unliganded-closed conformation|||in LIMBS binding site|||in MIDAS binding site                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016350|||http://purl.uniprot.org/annotation/PRO_5001832044|||http://purl.uniprot.org/annotation/VAR_049636|||http://purl.uniprot.org/annotation/VAR_073328|||http://purl.uniprot.org/annotation/VAR_073329|||http://purl.uniprot.org/annotation/VAR_073330|||http://purl.uniprot.org/annotation/VSP_055189
http://togogenome.org/gene/9606:PSMD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55036|||http://purl.uniprot.org/uniprot/Q5VWC4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 4|||Basic and acidic residues|||Disordered|||Essential for ubiquitin-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform Rpn10E.|||Interaction with UBQLN1|||Phosphoserine|||Phosphothreonine|||UIM 1|||UIM 2|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173828|||http://purl.uniprot.org/annotation/VSP_005291|||http://purl.uniprot.org/annotation/VSP_005292
http://togogenome.org/gene/9606:LIPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07098                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Gastric triacylglycerol lipase|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017766|||http://purl.uniprot.org/annotation/VAR_011947|||http://purl.uniprot.org/annotation/VAR_020565|||http://purl.uniprot.org/annotation/VAR_020566|||http://purl.uniprot.org/annotation/VSP_047295|||http://purl.uniprot.org/annotation/VSP_047296
http://togogenome.org/gene/9606:BRI3BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY22                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  BRI3-binding protein|||Helical|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229747
http://togogenome.org/gene/9606:ATL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5A2|||http://purl.uniprot.org/uniprot/A0A0S2Z5B0|||http://purl.uniprot.org/uniprot/Q53F53|||http://purl.uniprot.org/uniprot/Q8WXF7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes GTPase activity and impairs homodimerization.|||Abolishes homodimerization.|||Affects endoplasmic reticulum and Golgi morphology.|||Alters endoplasmic reticulum morphogenesis.|||Atlastin-1|||Cytoplasmic|||Disordered|||GB1/RHD3-type G|||Helical|||Impairs homodimerization and GTPase activity.|||In HSN1D; shows no significant changes in GTPase activity and no changes in endoplasmic reticulum morphology.|||In HSN1D; the mutant protein has decreased GTPase activity compared to wild-type and causes disruption of endoplasmic reticulum network morphology.|||In SPG3.|||In SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology.|||In SPG3; affects endoplasmic reticulum and Golgi morphology.|||In SPG3; does not affect GTPase activity; does not affect interaction with SPAST; patients' lymphoblasts show decreased protein levels but normal levels of mRNA.|||In a patient with hereditary spastic paraplegia; unknown pathological significance; no effect on homodimerization and GTPase activity.|||In isoform 2.|||Lumenal|||N6-acetyllysine|||Phosphoserine|||Sufficient for membrane association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190971|||http://purl.uniprot.org/annotation/VAR_017146|||http://purl.uniprot.org/annotation/VAR_017147|||http://purl.uniprot.org/annotation/VAR_017148|||http://purl.uniprot.org/annotation/VAR_017149|||http://purl.uniprot.org/annotation/VAR_019446|||http://purl.uniprot.org/annotation/VAR_019447|||http://purl.uniprot.org/annotation/VAR_058963|||http://purl.uniprot.org/annotation/VAR_058964|||http://purl.uniprot.org/annotation/VAR_065508|||http://purl.uniprot.org/annotation/VAR_065509|||http://purl.uniprot.org/annotation/VAR_065510|||http://purl.uniprot.org/annotation/VAR_065511|||http://purl.uniprot.org/annotation/VAR_065512|||http://purl.uniprot.org/annotation/VAR_065513|||http://purl.uniprot.org/annotation/VAR_067655|||http://purl.uniprot.org/annotation/VAR_067656|||http://purl.uniprot.org/annotation/VAR_067657|||http://purl.uniprot.org/annotation/VAR_067658|||http://purl.uniprot.org/annotation/VAR_067659|||http://purl.uniprot.org/annotation/VAR_067660|||http://purl.uniprot.org/annotation/VAR_071708|||http://purl.uniprot.org/annotation/VAR_071709|||http://purl.uniprot.org/annotation/VAR_071874|||http://purl.uniprot.org/annotation/VSP_044864
http://togogenome.org/gene/9606:KLK12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R4M4|||http://purl.uniprot.org/uniprot/B9EGA9|||http://purl.uniprot.org/uniprot/Q9UKR0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||In isoform 3.|||Kallikrein-12|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027956|||http://purl.uniprot.org/annotation/PRO_5010010681|||http://purl.uniprot.org/annotation/VSP_005403|||http://purl.uniprot.org/annotation/VSP_045851|||http://purl.uniprot.org/annotation/VSP_045852
http://togogenome.org/gene/9606:GJB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IBS8|||http://purl.uniprot.org/uniprot/Q9NTQ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||INTRAMEM|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-4 protein|||Gap junction protein cysteine-rich|||Helical|||In EKVP2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057865|||http://purl.uniprot.org/annotation/VAR_010206|||http://purl.uniprot.org/annotation/VAR_015088|||http://purl.uniprot.org/annotation/VAR_015089|||http://purl.uniprot.org/annotation/VAR_015090|||http://purl.uniprot.org/annotation/VAR_015091|||http://purl.uniprot.org/annotation/VAR_015092|||http://purl.uniprot.org/annotation/VAR_079194|||http://purl.uniprot.org/annotation/VAR_079195|||http://purl.uniprot.org/annotation/VAR_079196|||http://purl.uniprot.org/annotation/VAR_079197
http://togogenome.org/gene/9606:PLAC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JTB5|||http://purl.uniprot.org/uniprot/Q5JTB6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Placenta-specific protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261405|||http://purl.uniprot.org/annotation/PRO_5004258035
http://togogenome.org/gene/9606:MAP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2BDK6|||http://purl.uniprot.org/uniprot/P46821|||http://purl.uniprot.org/uniprot/Q6PJD3|||http://purl.uniprot.org/uniprot/Q86X89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In DFNA83; unknown pathological significance; reduced neurite length in otic sensory neuron-like cells from patient-derived indifferentiated pluripotent stem cells.|||In PVNH9.|||In PVNH9; no effect on protein expression.|||In a colorectal cancer sample; somatic mutation.|||MAP1 light chain LC1|||MAP1B 1|||MAP1B 10|||MAP1B 2|||MAP1B 3|||MAP1B 4|||MAP1B 5|||MAP1B 6|||MAP1B 7|||MAP1B 8|||MAP1B 9|||MAP1B heavy chain|||Mediates interaction with TMEM185A|||Microtubule-associated protein 1B|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018604|||http://purl.uniprot.org/annotation/PRO_0000018605|||http://purl.uniprot.org/annotation/PRO_0000418379|||http://purl.uniprot.org/annotation/VAR_024530|||http://purl.uniprot.org/annotation/VAR_030347|||http://purl.uniprot.org/annotation/VAR_034105|||http://purl.uniprot.org/annotation/VAR_036016|||http://purl.uniprot.org/annotation/VAR_036017|||http://purl.uniprot.org/annotation/VAR_056123|||http://purl.uniprot.org/annotation/VAR_084525|||http://purl.uniprot.org/annotation/VAR_084526|||http://purl.uniprot.org/annotation/VAR_084527|||http://purl.uniprot.org/annotation/VAR_084528|||http://purl.uniprot.org/annotation/VAR_084529|||http://purl.uniprot.org/annotation/VAR_084530|||http://purl.uniprot.org/annotation/VAR_087096|||http://purl.uniprot.org/annotation/VAR_087097|||http://purl.uniprot.org/annotation/VAR_087098
http://togogenome.org/gene/9606:GNA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14344                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by PKA; disrupts heterotrimer stability.|||Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation.|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-13|||In isoform 2.|||Phosphothreonine; by PKA|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203773|||http://purl.uniprot.org/annotation/VAR_017160|||http://purl.uniprot.org/annotation/VSP_055140
http://togogenome.org/gene/9606:PAFAH1B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68402|||http://purl.uniprot.org/uniprot/V9HW44                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Platelet-activating factor acetylhydrolase IB subunit alpha2|||Removed|||SGNH hydrolase-type esterase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058151|||http://purl.uniprot.org/annotation/VSP_042896|||http://purl.uniprot.org/annotation/VSP_043217|||http://purl.uniprot.org/annotation/VSP_044680
http://togogenome.org/gene/9606:ZKSCAN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z658|||http://purl.uniprot.org/uniprot/B7Z7H3|||http://purl.uniprot.org/uniprot/Q969J2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Polar residues|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047525|||http://purl.uniprot.org/annotation/VAR_059951
http://togogenome.org/gene/9606:PTPMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUK0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mitochondrion|||Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1|||Phosphocysteine intermediate|||Probable loss of catalytic activity. Does not affect interaction with STYXL1.|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025423|||http://purl.uniprot.org/annotation/VSP_015009|||http://purl.uniprot.org/annotation/VSP_045030|||http://purl.uniprot.org/annotation/VSP_045031
http://togogenome.org/gene/9606:CRIP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Q6R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cysteine-rich protein 3|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LIM zinc-binding 1|||LIM zinc-binding 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225638|||http://purl.uniprot.org/annotation/VSP_017391|||http://purl.uniprot.org/annotation/VSP_017392|||http://purl.uniprot.org/annotation/VSP_017393
http://togogenome.org/gene/9606:TUSC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13454                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In isoform 2.|||Lumenal|||Redox-active|||Reduces N-glycosylation of cysteine-proximal acceptor sites; when associated with S-102.|||Reduces N-glycosylation of cysteine-proximal acceptor sites; when associated with S-99.|||Thioredoxin|||Tumor suppressor candidate 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215300|||http://purl.uniprot.org/annotation/VAR_045836|||http://purl.uniprot.org/annotation/VAR_069369|||http://purl.uniprot.org/annotation/VSP_003776
http://togogenome.org/gene/9606:LFNG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NES3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe|||Cleavage; by furin-like protease|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In SCDO3; not localized to the correct compartment of the cell; unable to modulate Notch signaling in a cell-based assay; enzymatically inactive.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219176|||http://purl.uniprot.org/annotation/VAR_025850|||http://purl.uniprot.org/annotation/VAR_046785|||http://purl.uniprot.org/annotation/VAR_046786|||http://purl.uniprot.org/annotation/VSP_001792|||http://purl.uniprot.org/annotation/VSP_001793|||http://purl.uniprot.org/annotation/VSP_001794|||http://purl.uniprot.org/annotation/VSP_001795|||http://purl.uniprot.org/annotation/VSP_044850|||http://purl.uniprot.org/annotation/VSP_044851
http://togogenome.org/gene/9606:DHRS13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX07                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Dehydrogenase/reductase SDR family member 13|||Disordered|||In isoform 2.|||In isoform 3.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311920|||http://purl.uniprot.org/annotation/VAR_037348|||http://purl.uniprot.org/annotation/VAR_037349|||http://purl.uniprot.org/annotation/VSP_029640|||http://purl.uniprot.org/annotation/VSP_057529
http://togogenome.org/gene/9606:NEUROG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0H3|||http://purl.uniprot.org/uniprot/Q92886                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  BHLH|||Disordered|||Neurogenin-1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127396
http://togogenome.org/gene/9606:IL21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A224B028|||http://purl.uniprot.org/uniprot/Q9HBE4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In CVID11; interferes with binding to IL21R.|||In isoform 2.|||Interleukin|||Interleukin-21|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015505|||http://purl.uniprot.org/annotation/PRO_5011188492|||http://purl.uniprot.org/annotation/VAR_071292|||http://purl.uniprot.org/annotation/VSP_030129
http://togogenome.org/gene/9606:SETMAR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DND2|||http://purl.uniprot.org/uniprot/Q53H47|||http://purl.uniprot.org/uniprot/Q96H41                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DNA cleavage.|||Abolishes TIR-specific DNA-binding.|||Abolishes homodimerization and DNA-binding and reduces cleavage of single-stranded DNA.|||H-T-H motif|||Histone-lysine N-methyltransferase|||Histone-lysine N-methyltransferase SETMAR|||In isoform 2.|||In isoform 3.|||Loss of function in DNA repair. Altered DNA-binding properties.|||Mariner transposase Hsmar1|||Mos1 transposase HTH|||N6-methyllysine|||Phosphoserine; by CHEK1|||Post-SET|||Pre-SET|||Prevents phosphorylation. Impairs recruitment to damaged DNA and double-strand break repair. Impairs interaction with histone H3 and its methylation. Allows replication fork restart.|||Reduces activity in double-strand break repair.|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259526|||http://purl.uniprot.org/annotation/VSP_021440|||http://purl.uniprot.org/annotation/VSP_021441|||http://purl.uniprot.org/annotation/VSP_054089
http://togogenome.org/gene/9606:DOK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6M4C8X9|||http://purl.uniprot.org/uniprot/D6RAM3|||http://purl.uniprot.org/uniprot/Q7L591                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Docking protein 3|||IRS-type PTB|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187272|||http://purl.uniprot.org/annotation/VAR_057525|||http://purl.uniprot.org/annotation/VAR_062002|||http://purl.uniprot.org/annotation/VSP_013712|||http://purl.uniprot.org/annotation/VSP_013713|||http://purl.uniprot.org/annotation/VSP_013714|||http://purl.uniprot.org/annotation/VSP_013715|||http://purl.uniprot.org/annotation/VSP_013716
http://togogenome.org/gene/9606:NYX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZU5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In CSNB1A.|||In CSNB1A; requires 2 nucleotide substitutions.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine|||Nyctalopin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032776|||http://purl.uniprot.org/annotation/VAR_013867|||http://purl.uniprot.org/annotation/VAR_013868|||http://purl.uniprot.org/annotation/VAR_013869|||http://purl.uniprot.org/annotation/VAR_013870|||http://purl.uniprot.org/annotation/VAR_013871|||http://purl.uniprot.org/annotation/VAR_013872|||http://purl.uniprot.org/annotation/VAR_013873|||http://purl.uniprot.org/annotation/VAR_013874|||http://purl.uniprot.org/annotation/VAR_013875|||http://purl.uniprot.org/annotation/VAR_013876|||http://purl.uniprot.org/annotation/VAR_013877|||http://purl.uniprot.org/annotation/VAR_013878|||http://purl.uniprot.org/annotation/VAR_013879|||http://purl.uniprot.org/annotation/VAR_013880|||http://purl.uniprot.org/annotation/VAR_013881|||http://purl.uniprot.org/annotation/VAR_013882|||http://purl.uniprot.org/annotation/VAR_014084|||http://purl.uniprot.org/annotation/VAR_014085|||http://purl.uniprot.org/annotation/VAR_014086|||http://purl.uniprot.org/annotation/VAR_014087|||http://purl.uniprot.org/annotation/VAR_014088|||http://purl.uniprot.org/annotation/VAR_014089|||http://purl.uniprot.org/annotation/VAR_014090|||http://purl.uniprot.org/annotation/VAR_052020
http://togogenome.org/gene/9606:OR52J3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH60                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52J3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150780|||http://purl.uniprot.org/annotation/VAR_034343|||http://purl.uniprot.org/annotation/VAR_034344|||http://purl.uniprot.org/annotation/VAR_034345|||http://purl.uniprot.org/annotation/VAR_034346
http://togogenome.org/gene/9606:WNT8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NKY7|||http://purl.uniprot.org/uniprot/Q93098                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine|||Protein Wnt|||Protein Wnt-8b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041450|||http://purl.uniprot.org/annotation/PRO_5033788021|||http://purl.uniprot.org/annotation/VAR_020310|||http://purl.uniprot.org/annotation/VAR_036288
http://togogenome.org/gene/9606:SNX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRI2|||http://purl.uniprot.org/uniprot/Q9UNH7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  BAR|||In isoform 2.|||Interaction with PIM1|||Membrane-binding amphipathic helix|||N-acetylmethionine|||N-acetylmethionine; in Sorting nexin-6, N-terminally processed|||No effect on subcellular location.|||PX|||Phosphoserine|||Reduces interaction with SNX1. Abolishes location at endosome membranes.|||Removed; alternate|||Sorting nexin-6|||Sorting nexin-6, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213846|||http://purl.uniprot.org/annotation/PRO_0000423277|||http://purl.uniprot.org/annotation/VSP_044824
http://togogenome.org/gene/9606:CCNI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMN8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-I2|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335821|||http://purl.uniprot.org/annotation/VAR_043471|||http://purl.uniprot.org/annotation/VSP_057179|||http://purl.uniprot.org/annotation/VSP_057180
http://togogenome.org/gene/9606:GSTO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4Y5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DHAR activity.|||GST C-terminal|||GST N-terminal|||Glutathione S-transferase omega-2|||In isoform 2.|||In isoform 3.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185888|||http://purl.uniprot.org/annotation/VAR_016812|||http://purl.uniprot.org/annotation/VAR_049492|||http://purl.uniprot.org/annotation/VSP_042567|||http://purl.uniprot.org/annotation/VSP_045267
http://togogenome.org/gene/9606:LEMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2U8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical|||Impairs binding to SMAD1.|||Impairs binding to SMAD1. Loss of ability to repress transcriptional activation in response to TGF-beta, BMP2 and activin signaling.|||In BOS.|||In BOS; patient does not show osteopoikilosis.|||Inner nuclear membrane protein Man1|||Interaction with SMAD1, SMAD2, SMAD3 and SMAD5|||LEM|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206149|||http://purl.uniprot.org/annotation/VAR_034605|||http://purl.uniprot.org/annotation/VAR_080412|||http://purl.uniprot.org/annotation/VAR_080413
http://togogenome.org/gene/9606:FMC1-LUC7L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYJ8|||http://purl.uniprot.org/uniprot/Q96HJ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Protein FMC1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328780|||http://purl.uniprot.org/annotation/VAR_042520|||http://purl.uniprot.org/annotation/VSP_047244
http://togogenome.org/gene/9606:PRKCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFV1|||http://purl.uniprot.org/uniprot/Q05655                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||C2|||Cleavage; by caspase-3|||In isoform 2.|||Interaction with phosphotyrosine-containing peptide|||Loss of phosphorylation.|||No effect on kinase activity.|||Phorbol-ester/DAG-type|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Phosphotyrosine; by SRC|||Protein kinase|||Protein kinase C delta type|||Protein kinase C delta type catalytic subunit|||Protein kinase C delta type regulatory subunit|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055694|||http://purl.uniprot.org/annotation/PRO_0000421667|||http://purl.uniprot.org/annotation/PRO_0000421668|||http://purl.uniprot.org/annotation/VAR_006175|||http://purl.uniprot.org/annotation/VAR_006176|||http://purl.uniprot.org/annotation/VAR_020610|||http://purl.uniprot.org/annotation/VAR_035347|||http://purl.uniprot.org/annotation/VAR_035348|||http://purl.uniprot.org/annotation/VAR_046009|||http://purl.uniprot.org/annotation/VSP_043899
http://togogenome.org/gene/9606:OR2W3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3T1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a family with retinitis pigmentosa.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2W3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150512|||http://purl.uniprot.org/annotation/VAR_034180|||http://purl.uniprot.org/annotation/VAR_034181|||http://purl.uniprot.org/annotation/VAR_034182|||http://purl.uniprot.org/annotation/VAR_034183|||http://purl.uniprot.org/annotation/VAR_034184|||http://purl.uniprot.org/annotation/VAR_034185|||http://purl.uniprot.org/annotation/VAR_074043
http://togogenome.org/gene/9606:RB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06400                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with Pocket domain; when associated with A-821.|||Abolishes interaction with Pocket domain; when associated with A-826.|||Abolishes monomethylation by SMYD2 and subsequent interaction with L3MBTL1.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Does not affect the ability to be methylated by SMYD2; when associated with 873-R-R-874.|||Does not alter Rb localization in cycling cells, but mislocalizes to the cytoplasm during keratinocyte differentiation. Does not affect the ability to arrest cell growth. Probable loss of acetylation by PCAF.|||Domain A|||Domain B|||Domain C; mediates interaction with E4F1|||In RB.|||In RB; mild form.|||In RB; unilateral form.|||In RB; unknown pathological significance.|||Interaction with LIMD1|||N,N-dimethylproline|||N6-acetyllysine; by PCAF|||N6-methyllysine; by SMYD2|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CDK1 and CDK3|||Phosphoserine; by CDK2|||Phosphoserine; by CHEK2 and CHEK1|||Phosphothreonine|||Phosphothreonine; by CDK1|||Phosphothreonine; by CDK4|||Phosphothreonine; by CDK6|||Pocket; binds T and E1A|||Polar residues|||Pro residues|||Removed|||Retinoblastoma-associated protein|||Spacer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167836|||http://purl.uniprot.org/annotation/VAR_005572|||http://purl.uniprot.org/annotation/VAR_005573|||http://purl.uniprot.org/annotation/VAR_005574|||http://purl.uniprot.org/annotation/VAR_005575|||http://purl.uniprot.org/annotation/VAR_005576|||http://purl.uniprot.org/annotation/VAR_005577|||http://purl.uniprot.org/annotation/VAR_005578|||http://purl.uniprot.org/annotation/VAR_005579|||http://purl.uniprot.org/annotation/VAR_005580|||http://purl.uniprot.org/annotation/VAR_005581|||http://purl.uniprot.org/annotation/VAR_005582|||http://purl.uniprot.org/annotation/VAR_005583|||http://purl.uniprot.org/annotation/VAR_005584|||http://purl.uniprot.org/annotation/VAR_005585|||http://purl.uniprot.org/annotation/VAR_005586|||http://purl.uniprot.org/annotation/VAR_005587|||http://purl.uniprot.org/annotation/VAR_005588|||http://purl.uniprot.org/annotation/VAR_010045|||http://purl.uniprot.org/annotation/VAR_010046|||http://purl.uniprot.org/annotation/VAR_010048|||http://purl.uniprot.org/annotation/VAR_010049|||http://purl.uniprot.org/annotation/VAR_010050|||http://purl.uniprot.org/annotation/VAR_011580|||http://purl.uniprot.org/annotation/VAR_011581|||http://purl.uniprot.org/annotation/VAR_019379|||http://purl.uniprot.org/annotation/VAR_019380|||http://purl.uniprot.org/annotation/VAR_034442|||http://purl.uniprot.org/annotation/VAR_051909|||http://purl.uniprot.org/annotation/VAR_051910|||http://purl.uniprot.org/annotation/VAR_051911|||http://purl.uniprot.org/annotation/VAR_069376
http://togogenome.org/gene/9606:METAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE3|||http://purl.uniprot.org/uniprot/F8VQZ7|||http://purl.uniprot.org/uniprot/P50579                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Methionine aminopeptidase 2|||N-acetylalanine|||O-linked (GlcNAc) serine; alternate|||Peptidase M24|||Phosphoserine|||Phosphoserine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148982|||http://purl.uniprot.org/annotation/VSP_055467|||http://purl.uniprot.org/annotation/VSP_055468|||http://purl.uniprot.org/annotation/VSP_057353
http://togogenome.org/gene/9606:TCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20062                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Transcobalamin-2|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005564|||http://purl.uniprot.org/annotation/VAR_001638|||http://purl.uniprot.org/annotation/VAR_001639|||http://purl.uniprot.org/annotation/VAR_001640|||http://purl.uniprot.org/annotation/VAR_001641|||http://purl.uniprot.org/annotation/VAR_054539|||http://purl.uniprot.org/annotation/VAR_054540|||http://purl.uniprot.org/annotation/VAR_054541|||http://purl.uniprot.org/annotation/VAR_054542|||http://purl.uniprot.org/annotation/VAR_054543|||http://purl.uniprot.org/annotation/VAR_054544|||http://purl.uniprot.org/annotation/VSP_043711
http://togogenome.org/gene/9606:RFX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22670                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||MHC class II regulatory factor RFX1|||Necessary for dimerization|||Phosphoserine|||Polar residues|||Pro residues|||RFX-type winged-helix                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215286|||http://purl.uniprot.org/annotation/VAR_059781
http://togogenome.org/gene/9606:CHRNA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGM1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Key residue important for potent inhibition of the CHRNA9-CHRNA10 receptor by the alpha-conotoxin RgIA (AC P0C1D0)|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-9|||The CHRNA9-CHRNA10 receptor is 250-fold more potently inhibited by the alpha-conotoxin RgIA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000371|||http://purl.uniprot.org/annotation/VAR_025425|||http://purl.uniprot.org/annotation/VAR_031151|||http://purl.uniprot.org/annotation/VAR_060996
http://togogenome.org/gene/9606:SCN5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PG18|||http://purl.uniprot.org/uniprot/E9PHB6|||http://purl.uniprot.org/uniprot/H9KVD2|||http://purl.uniprot.org/uniprot/K4DIA1|||http://purl.uniprot.org/uniprot/Q14524|||http://purl.uniprot.org/uniprot/Q86V90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4.2-fold decrease of channel inhibition potency by the spider Jingzhaotoxin-I.|||Abolishes calcium response on channel inactivation.|||Acidic residues|||Associated with I-232 in a case of lidocaine-induced Brugada syndrome.|||Basic and acidic residues|||Channels properties are similar to wild-type; the double mutant R-558/I-512 channel shows that R-558 eliminates the negative shift induced by Ile-512 but only partially restores the kinetic abnormalities; can modulate the gating defects caused by Ala-2006 and other mutations.|||Complete loss of channel inhibition by the spider Jingzhaotoxin-I.|||Cytoplasmic|||Dimethylated arginine; alternate|||Disordered|||Extracellular|||Found in a patient with long QT syndrome; unknown pathological significance.|||Found in a patient with long QT syndrome; unknown pathological significance; causes an increase of persistent sodium current and produces a depolarizing shift in voltage dependence of inactivation.|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||High decrease in affinity to the sea anemone toxin anthopleurin-B.|||I|||II|||III|||IQ|||IV|||In ATFB10.|||In BRGDA1 and LQT3.|||In BRGDA1 and LQT3; also found in patients with atrial fibrillation; accelerates the inactivation of the sodium channel current and exhibit reduced sodium channel current at the end of phase I of the action potential.|||In BRGDA1 and LQT3; also found in patients with atrial fibrillation; unknown pathological significance.|||In BRGDA1 and LQT3; complete loss of sodium currents due to defective channel trafficking to the plasma membrane.|||In BRGDA1 and LQT3; express no current.|||In BRGDA1 and LQT3; unknown pathological significance.|||In BRGDA1 and PFHB1A.|||In BRGDA1 and SSS1; expresses currents with steady state activation voltage shifted to more positive potentials and exhibit reduced sodium channel current at the end of phase I of the action potential.|||In BRGDA1, ATFB10 and LQT3; abolishes binding to ANK3 and also prevents accumulation of SCN5A at cell surface sites in ventricular cardiomyocytes.|||In BRGDA1.|||In BRGDA1; 7-fold current reduction.|||In BRGDA1; accelerates the onset of activation and causes a marked negative shift in the voltage dependence of inactivation; does not affect the kinetics of the recovery from inactivation; increases the expression of sustained Na(+) channel activity and promotes entrance into an intermediate or slowly developing inactivated state.|||In BRGDA1; affects channel activity; the mutant displays a hyperpolarizing shift in the voltage dependence of inactivation causing slower inactivation compared to the wild type, slower recovery and a reduced availability of channels at rest.|||In BRGDA1; arrhythmogenicity revealed only at temperatures approaching the physiologic range.|||In BRGDA1; asymptomatic patient; associated with P-1569.|||In BRGDA1; asymptomatic patient; associated with R-1527.|||In BRGDA1; changed voltage-gated sodium channel activity; no difference in current density but changed inactivation kinetics and prolonged recovery from inactivation.|||In BRGDA1; decreased I(Na) density; shift of the steady-state inactivation towards negative potentials.|||In BRGDA1; decreased localization to the plasma membrane; decreased voltage-gated sodium channel activity; dominant negative effect; changed voltage dependence for activation and inactivation.|||In BRGDA1; decreased localization to the plasma membrane; decreased voltage-gated sodium channel activity; dominant negative effect; no effect on voltage dependence for activation and inactivation.|||In BRGDA1; decreased protein abundance; retained intracellularly; decreased voltage-gated sodium channel activity; hyperpolarizing shift of the voltage dependence of inactivation leading to reduced sodium window current; no dominant negative effect.|||In BRGDA1; decreases expression at the cell membrane; yields nearly undetectable currents in transfected cells.|||In BRGDA1; express no current.|||In BRGDA1; loss of function.|||In BRGDA1; no effect on localization to the plasma membrane; decreased voltage-gated sodium channel activity; shift in the voltage dependence of activation and changed recovery from inactivation.|||In BRGDA1; severe reduction of sodium currents.|||In BRGDA1; significantly affect cardiac sodium channel characteristics; associated with an increase in inward sodium current during the action potential upstroke.|||In BRGDA1; significantly affects cardiac sodium channel characteristics; associated with an increase in inward sodium current during the action potential upstroke.|||In BRGDA1; steady state inactivation shifted to a more negative potential; slower recovery from inactivation.|||In BRGDA1; strong decrease of current density; does not affect ion selectivity properties.|||In BRGDA1; unknown pathological significance.|||In BRGDA1; unknown pathological significance; also found in patients with atrial fibrillation.|||In CMD1E, BRGDA1, PFHB1A and ATRST1; in familial atrial standstill is found in association with variants in the regulatory region of GJA5; decreases expression at the cell membrane; alters channel kinetics; shifts activation and inactivation to more positive membrane potentials.|||In LQT3 and ATFB10; likely benign variant.|||In LQT3 and BRGDA1.|||In LQT3 and BRGDA1; 7.3-mV negative shift of the steady-state inactivation curve and 8.1-mV positive shift of the steady-state activation curve; may reduce sodium current during the upstroke of the action potential.|||In LQT3 and BRGDA1; also found in patients with atrial fibrillation; results in channels with decreased peak and persistent current amplitudes; increased closed-state and slow inactivation; decelerated recovery from inactivation.|||In LQT3 and BRGDA1; drug-induced LQT syndrome.|||In LQT3 and PFHB1A.|||In LQT3 and SIDS.|||In LQT3.|||In LQT3; affects protein trafficking.|||In LQT3; also found in patients with atrial fibrillation; sodium current characterized by slower decay and a 2- to 3-fold increase in late sodium current.|||In LQT3; also in SIDS.|||In LQT3; also in a family associating LQT syndrome and atrial fibrillation; slows the onset of activation, but does not cause a marked negative shift in the voltage dependence of inactivation or affect the kinetics of the recovery from inactivation; increases the expression of sustained Na(+) channel activity and promotes entrance into an intermediate or slowly developing inactivated state.|||In LQT3; causes significant positive shifts in the half-maximal voltage of steady-state inactivation and activation.|||In LQT3; decreased interaction with FGF12, FGF13 and FGF14; increased voltage-gated sodium channel activity; altered inactivation.|||In LQT3; digenic; the patient also carries mutation G-100 on KCNH2.|||In LQT3; does not affect baseline kinetics of sodium currents; causes an unusual hyperpolarizing shift of the activation kinetics after lidocaine treatment.|||In LQT3; drug-induced LQT syndrome.|||In LQT3; increases the rate of recovery from inactivation and the channel availability, observed as a positive shift of the steady-state inactivation curve.|||In LQT3; promotes late sodium currents by increasing the propensity of the channel to reopen during prolonged depolarization.|||In LQT3; sodium current characterized by slower decay and a 2- to 3-fold increase in late sodium current.|||In LQT3; unknown pathological significance.|||In PFHB1A, BRGDA1 and LQT3.|||In PFHB1A; also in irritable bowel syndrome; results in reduction of whole cell current density and a delay in channel activation kinetics without a change in single-channel conductance.|||In PFHB1A; significant defect in the kinetics of fast-channel inactivation distinct from mutations reported in LQT3.|||In PFHB1A; voltage-dependent activation and inactivation of the I-512 channel is shifted negatively by 8 to 9 mV and had enhanced slow activation and slower recovery from inactivation commpared to the wild-type channel; the double mutant R-558/I-512 channel shows that R-558 eliminates the negative shift induced by I-512 but only partially restores the kinetic abnormalities.|||In SIDS and BRGDA1.|||In SIDS; causes a hyperpolarizing shift of steady-state inactivation and delayed recovery from inactivation.|||In SIDS; unknown pathological significance.|||In SSS1 and BRGDA1.|||In SSS1.|||In VF1.|||In atrial fibrillation; pronounced depolarized shift of the voltage dependence of steady-state inactivation; no persistent sodium current.|||In isoform 2 and isoform 3.|||In isoform 3, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||Induces accelerated recovery from channel fast inactivation.|||Interaction with FGF13|||Interaction with NEDD4, NEDD4L and WWP2|||Ion transport|||May confer susceptibility to acquired arrhythmia.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with NEDD4, NEDD4L or WWP2.|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Polar residues|||Pore-forming|||Rare variant found in patients with atrial fibrillation; unknown pathological significance.|||Rare variant; found in a patient with long QT syndrome; unknown pathological significance.|||Sodium channel protein type 5 subunit alpha|||Sodium ion transport-associated|||Strongly reduces interaction with NEDD4, NEDD4L or WWP2.|||Strongly reduces interaction with NEDD4L.|||Voltage-gated Na+ ion channel cytoplasmic ^@                                                                                  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org/annotation/VAR_074443|||http://purl.uniprot.org/annotation/VAR_074444|||http://purl.uniprot.org/annotation/VAR_074445|||http://purl.uniprot.org/annotation/VAR_074446|||http://purl.uniprot.org/annotation/VAR_074447|||http://purl.uniprot.org/annotation/VAR_074448|||http://purl.uniprot.org/annotation/VAR_074449|||http://purl.uniprot.org/annotation/VAR_074450|||http://purl.uniprot.org/annotation/VAR_074451|||http://purl.uniprot.org/annotation/VAR_074452|||http://purl.uniprot.org/annotation/VAR_074453|||http://purl.uniprot.org/annotation/VAR_074454|||http://purl.uniprot.org/annotation/VAR_074455|||http://purl.uniprot.org/annotation/VAR_074456|||http://purl.uniprot.org/annotation/VAR_074457|||http://purl.uniprot.org/annotation/VAR_074458|||http://purl.uniprot.org/annotation/VAR_074459|||http://purl.uniprot.org/annotation/VAR_074460|||http://purl.uniprot.org/annotation/VAR_074461|||http://purl.uniprot.org/annotation/VAR_074462|||http://purl.uniprot.org/annotation/VAR_074463|||http://purl.uniprot.org/annotation/VAR_074464|||http://purl.uniprot.org/annotation/VAR_074465|||http://purl.uniprot.org/annotation/VAR_074466|||http://purl.uniprot.org/annotation/VAR_074467|||http://purl.uniprot.org/annotation/VAR_074468|||http://purl.uniprot.org/annotation/VAR_074469|||http://purl.uniprot.org/annotation/VAR_074470|||http://purl.uniprot.org/annotation/VAR_074471|||http://purl.uniprot.org/annotation/VAR_074472|||http://purl.uniprot.org/annotation/VAR_074473|||http://purl.uniprot.org/annotation/VAR_074474|||http://purl.uniprot.org/annotation/VAR_074475|||http://purl.uniprot.org/annotation/VAR_074476|||http://purl.uniprot.org/annotation/VAR_074477|||http://purl.uniprot.org/annotation/VAR_074478|||http://purl.uniprot.org/annotation/VAR_074479|||http://purl.uniprot.org/annotation/VAR_074480|||http://purl.uniprot.org/annotation/VAR_074481|||http://purl.uniprot.org/annotation/VAR_074482|||http://purl.uniprot.org/annotation/VAR_074483|||http://purl.uniprot.org/annotation/VAR_074484|||http://purl.uniprot.org/annotation/VAR_074695|||http://purl.uniprot.org/annotation/VAR_074696|||http://purl.uniprot.org/annotation/VAR_074697|||http://purl.uniprot.org/annotation/VAR_074698|||http://purl.uniprot.org/annotation/VAR_074699|||http://purl.uniprot.org/annotation/VAR_074700|||http://purl.uniprot.org/annotation/VAR_074701|||http://purl.uniprot.org/annotation/VAR_074702|||http://purl.uniprot.org/annotation/VAR_074703|||http://purl.uniprot.org/annotation/VAR_074704|||http://purl.uniprot.org/annotation/VAR_074705|||http://purl.uniprot.org/annotation/VAR_074706|||http://purl.uniprot.org/annotation/VAR_074707|||http://purl.uniprot.org/annotation/VAR_074708|||http://purl.uniprot.org/annotation/VAR_074709|||http://purl.uniprot.org/annotation/VAR_074710|||http://purl.uniprot.org/annotation/VAR_074711|||http://purl.uniprot.org/annotation/VAR_074712|||http://purl.uniprot.org/annotation/VAR_074713|||http://purl.uniprot.org/annotation/VAR_074714|||http://purl.uniprot.org/annotation/VAR_074715|||http://purl.uniprot.org/annotation/VAR_074716|||http://purl.uniprot.org/annotation/VAR_074717|||http://purl.uniprot.org/annotation/VAR_074718|||http://purl.uniprot.org/annotation/VAR_074719|||http://purl.uniprot.org/annotation/VAR_074720|||http://purl.uniprot.org/annotation/VAR_074721|||http://purl.uniprot.org/annotation/VAR_074722|||http://purl.uniprot.org/annotation/VAR_074723|||http://purl.uniprot.org/annotation/VAR_074724|||http://purl.uniprot.org/annotation/VAR_074725|||http://purl.uniprot.org/annotation/VAR_074726|||http://purl.uniprot.org/annotation/VAR_074727|||http://purl.uniprot.org/annotation/VAR_074728|||http://purl.uniprot.org/annotation/VAR_074729|||http://purl.uniprot.org/annotation/VAR_074730|||http://purl.uniprot.org/annotation/VAR_074731|||http://purl.uniprot.org/annotation/VAR_074732|||http://purl.uniprot.org/annotation/VAR_074733|||http://purl.uniprot.org/annotation/VAR_074734|||http://purl.uniprot.org/annotation/VAR_074735|||http://purl.uniprot.org/annotation/VAR_074736|||http://purl.uniprot.org/annotation/VAR_074737|||http://purl.uniprot.org/annotation/VAR_074738|||http://purl.uniprot.org/annotation/VAR_074739|||http://purl.uniprot.org/annotation/VAR_074740|||http://purl.uniprot.org/annotation/VAR_074741|||http://purl.uniprot.org/annotation/VAR_074742|||http://purl.uniprot.org/annotation/VAR_074743|||http://purl.uniprot.org/annotation/VAR_074744|||http://purl.uniprot.org/annotation/VAR_074745|||http://purl.uniprot.org/annotation/VAR_074746|||http://purl.uniprot.org/annotation/VAR_074747|||http://purl.uniprot.org/annotation/VAR_074748|||http://purl.uniprot.org/annotation/VAR_074749|||http://purl.uniprot.org/annotation/VAR_074750|||http://purl.uniprot.org/annotation/VAR_074751|||http://purl.uniprot.org/annotation/VAR_074752|||http://purl.uniprot.org/annotation/VAR_074753|||http://purl.uniprot.org/annotation/VAR_074754|||http://purl.uniprot.org/annotation/VAR_074755|||http://purl.uniprot.org/annotation/VAR_074756|||http://purl.uniprot.org/annotation/VAR_074757|||http://purl.uniprot.org/annotation/VAR_074758|||http://purl.uniprot.org/annotation/VAR_074759|||http://purl.uniprot.org/annotation/VAR_074760|||http://purl.uniprot.org/annotation/VAR_074761|||http://purl.uniprot.org/annotation/VAR_074762|||http://purl.uniprot.org/annotation/VAR_074763|||http://purl.uniprot.org/annotation/VAR_074764|||http://purl.uniprot.org/annotation/VAR_076555|||http://purl.uniprot.org/annotation/VAR_076556|||http://purl.uniprot.org/annotation/VAR_076557|||http://purl.uniprot.org/annotation/VAR_076558|||http://purl.uniprot.org/annotation/VAR_076559|||http://purl.uniprot.org/annotation/VAR_085793|||http://purl.uniprot.org/annotation/VSP_037477|||http://purl.uniprot.org/annotation/VSP_037478|||http://purl.uniprot.org/annotation/VSP_037479|||http://purl.uniprot.org/annotation/VSP_037480|||http://purl.uniprot.org/annotation/VSP_037481
http://togogenome.org/gene/9606:EIF3M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L2H7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Eukaryotic translation initiation factor 3 subunit M|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Interaction with HSV-1 and HSV-2|||N-acetylserine|||N6-acetyllysine|||PCI|||Phosphoserine|||Reduces HSV binding and entry.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308195|||http://purl.uniprot.org/annotation/VAR_036752|||http://purl.uniprot.org/annotation/VAR_036753|||http://purl.uniprot.org/annotation/VAR_036754|||http://purl.uniprot.org/annotation/VSP_056911
http://togogenome.org/gene/9606:ZNF493                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZR52                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6; degenerate|||C2H2-type 7; degenerate|||C2H2-type 8; degenerate|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||Zinc finger protein 493                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047616|||http://purl.uniprot.org/annotation/VAR_052846|||http://purl.uniprot.org/annotation/VAR_052847|||http://purl.uniprot.org/annotation/VSP_038298|||http://purl.uniprot.org/annotation/VSP_046656|||http://purl.uniprot.org/annotation/VSP_046657
http://togogenome.org/gene/9606:RTP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14D33                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Helical|||Receptor-transporting protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348428|||http://purl.uniprot.org/annotation/VAR_060791|||http://purl.uniprot.org/annotation/VAR_069402
http://togogenome.org/gene/9606:GOLGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08379                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with GORASP1. Abolishes membrane clustering.|||Abolishes interaction with importin-alpha.|||Acidic residues|||Dimethylated arginine|||Disordered|||Golgin subfamily A member 2|||Impaired methylation; when associated with R-18 and R-35.|||Impaired methylation; when associated with R-30 and R-35.|||In DEDHMB.|||In isoform 2.|||Interaction with GORASP1/GRASP65|||Interaction with p115/USO1|||Nuclear localization signal|||Phosphomimetic mutant. Does not affect interaction with importin-alpha.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190054|||http://purl.uniprot.org/annotation/VAR_033974|||http://purl.uniprot.org/annotation/VAR_088096|||http://purl.uniprot.org/annotation/VSP_007727
http://togogenome.org/gene/9606:CYP21A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08686|||http://purl.uniprot.org/uniprot/Q08AG9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased steroid 21-monooxygenase activity.|||In AH3.|||In AH3; does not affect membrane binding; enzyme function abolished.|||In AH3; exhibits low enzymatic activity toward 17-hydroxyprogesterone and progesterone.|||In AH3; loss of activity.|||In AH3; loss of enzymatic activity toward 17-hydroxyprogesterone and progesterone.|||In AH3; loss of enzymatic activity toward 17-hydroxyprogesterone.|||In AH3; loss of hydroxylase activity toward 17-hydroxyprogesterone and progesterone.|||In AH3; moderate.|||In AH3; moderate; 1-2% of activity.|||In AH3; no activity.|||In AH3; non-classic form; 10% of non-classic AH3 Texan patients; 50% steroid 21-monooxygenase activity.|||In AH3; non-classic form; 50% activity.|||In AH3; non-classic form; 50% activity; most common variant; normal KM but 20% reduced Vmax.|||In AH3; non-classic form; loss of steroid 21-monooxygenase activity.|||In AH3; non-classic form; mild.|||In AH3; non-classic form; pathogenicity uncertain.|||In AH3; non-classic form; reduced activity; decreased affinity for 17-hydroxyprogesterone and progesterone.|||In AH3; non-classic form; simple virilizing form when associated with L-62; 50% of activity; almost completely abolished enzyme activity when associated with S-375.|||In AH3; non-classic form; simple virilizing form when associated with a second mild mutation such as S-453 or L-30; activity is significantly reduced in association with S-453.|||In AH3; non-classic form; unknown pathological significance; no effect on steroid 21-monooxygenase activity.|||In AH3; reduced enzyme activity to 70% of normal.|||In AH3; salt wasting form.|||In AH3; salt wasting form; 0.15% activity.|||In AH3; salt wasting form; less then 1% activity.|||In AH3; salt wasting form; loss of activity.|||In AH3; salt wasting form; loss of steroid 21-monooxygenase activity.|||In AH3; salt wasting form; unknown pathological significance; no significant difference in steroid 21-monooxygenase activity.|||In AH3; simple virilizing form.|||In AH3; simple virilizing form; 1-4% activity.|||In AH3; simple virilizing form; 4% activity.|||In AH3; simple virilizing form; mild; 0.65% activity.|||In AH3; very low activity.|||In AH3; very low residual activity.|||In allele CYP21A2*2.|||In allele CYP21A2*3.|||In allele CYP21A2*4.|||In allele CYP21A2*5.|||In allele CYP21A2*6.|||In hyperandrogenism; due to 21-hydroxylase deficiency; almost completely abolished enzyme activity.|||In hyperandrogenism; due to 21-hydroxylase deficiency; non-classic type; residual activity of 46% for conversion of 17-hydroxyprogesterone and 26% for conversion of progesterone compared with the normal enzyme.|||In isoform 2.|||Loss of activity and loss of P450 absorption.|||No loss of function.|||Normal KM but 10% reduced Vmax.|||Normal KM but 50% reduced Vmax.|||Steroid 21-hydroxylase|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051976|||http://purl.uniprot.org/annotation/PRO_5004166638|||http://purl.uniprot.org/annotation/VAR_001281|||http://purl.uniprot.org/annotation/VAR_001282|||http://purl.uniprot.org/annotation/VAR_001283|||http://purl.uniprot.org/annotation/VAR_001284|||http://purl.uniprot.org/annotation/VAR_001285|||http://purl.uniprot.org/annotation/VAR_001286|||http://purl.uniprot.org/annotation/VAR_001287|||http://purl.uniprot.org/annotation/VAR_001288|||http://purl.uniprot.org/annotation/VAR_001289|||http://purl.uniprot.org/annotation/VAR_001290|||http://purl.uniprot.org/annotation/VAR_001291|||http://purl.uniprot.org/annotation/VAR_001292|||http://purl.uniprot.org/annotation/VAR_001293|||http://purl.uniprot.org/annotation/VAR_001294|||http://purl.uniprot.org/annotation/VAR_001295|||http://purl.uniprot.org/annotation/VAR_001296|||http://purl.uniprot.org/annotation/VAR_001297|||http://purl.uniprot.org/annotation/VAR_001298|||http://purl.uniprot.org/annotation/VAR_001299|||http://purl.uniprot.org/annotation/VAR_001300|||http://purl.uniprot.org/annotation/VAR_001301|||http://purl.uniprot.org/annotation/VAR_001302|||http://purl.uniprot.org/annotation/VAR_007923|||http://purl.uniprot.org/annotation/VAR_007924|||http://purl.uniprot.org/annotation/VAR_008688|||http://purl.uniprot.org/annotation/VAR_018363|||http://purl.uniprot.org/annotation/VAR_018364|||http://purl.uniprot.org/annotation/VAR_018365|||http://purl.uniprot.org/annotation/VAR_018366|||http://purl.uniprot.org/annotation/VAR_018367|||http://purl.uniprot.org/annotation/VAR_018368|||http://purl.uniprot.org/annotation/VAR_026059|||http://purl.uniprot.org/annotation/VAR_026060|||http://purl.uniprot.org/annotation/VAR_026061|||http://purl.uniprot.org/annotation/VAR_026062|||http://purl.uniprot.org/annotation/VAR_026063|||http://purl.uniprot.org/annotation/VAR_026064|||http://purl.uniprot.org/annotation/VAR_026065|||http://purl.uniprot.org/annotation/VAR_026066|||http://purl.uniprot.org/annotation/VAR_026067|||http://purl.uniprot.org/annotation/VAR_026068|||http://purl.uniprot.org/annotation/VAR_026069|||http://purl.uniprot.org/annotation/VAR_026070|||http://purl.uniprot.org/annotation/VAR_026071|||http://purl.uniprot.org/annotation/VAR_026072|||http://purl.uniprot.org/annotation/VAR_026073|||http://purl.uniprot.org/annotation/VAR_026074|||http://purl.uniprot.org/annotation/VAR_026075|||http://purl.uniprot.org/annotation/VAR_026076|||http://purl.uniprot.org/annotation/VAR_026077|||http://purl.uniprot.org/annotation/VAR_026078|||http://purl.uniprot.org/annotation/VAR_026079|||http://purl.uniprot.org/annotation/VAR_026080|||http://purl.uniprot.org/annotation/VAR_026081|||http://purl.uniprot.org/annotation/VAR_026082|||http://purl.uniprot.org/annotation/VAR_026083|||http://purl.uniprot.org/annotation/VAR_065668|||http://purl.uniprot.org/annotation/VAR_065669|||http://purl.uniprot.org/annotation/VAR_065670|||http://purl.uniprot.org/annotation/VAR_065671|||http://purl.uniprot.org/annotation/VAR_065672|||http://purl.uniprot.org/annotation/VAR_065673|||http://purl.uniprot.org/annotation/VAR_065674|||http://purl.uniprot.org/annotation/VAR_065675|||http://purl.uniprot.org/annotation/VAR_065676|||http://purl.uniprot.org/annotation/VAR_065677|||http://purl.uniprot.org/annotation/VAR_065678|||http://purl.uniprot.org/annotation/VAR_075372|||http://purl.uniprot.org/annotation/VAR_075373|||http://purl.uniprot.org/annotation/VAR_075374|||http://purl.uniprot.org/annotation/VAR_075375|||http://purl.uniprot.org/annotation/VAR_075376|||http://purl.uniprot.org/annotation/VAR_075377|||http://purl.uniprot.org/annotation/VAR_075378|||http://purl.uniprot.org/annotation/VAR_077582|||http://purl.uniprot.org/annotation/VAR_077583|||http://purl.uniprot.org/annotation/VAR_077584|||http://purl.uniprot.org/annotation/VAR_077585|||http://purl.uniprot.org/annotation/VAR_077586|||http://purl.uniprot.org/annotation/VAR_077587|||http://purl.uniprot.org/annotation/VAR_077588|||http://purl.uniprot.org/annotation/VAR_077589|||http://purl.uniprot.org/annotation/VSP_046264|||http://purl.uniprot.org/annotation/VSP_046265
http://togogenome.org/gene/9606:OCLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3T2|||http://purl.uniprot.org/uniprot/Q16625                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In PTORCH1.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||Loss of localization to the tight junctions.|||Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-398.|||Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-402.|||Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-398.|||Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-402.|||Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-398.|||Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-402.|||MARVEL|||OCEL|||Occludin|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PKC/PRKCH|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146739|||http://purl.uniprot.org/annotation/VAR_064910|||http://purl.uniprot.org/annotation/VSP_043872|||http://purl.uniprot.org/annotation/VSP_043873|||http://purl.uniprot.org/annotation/VSP_043874|||http://purl.uniprot.org/annotation/VSP_043875|||http://purl.uniprot.org/annotation/VSP_043876|||http://purl.uniprot.org/annotation/VSP_043877|||http://purl.uniprot.org/annotation/VSP_043878|||http://purl.uniprot.org/annotation/VSP_043879
http://togogenome.org/gene/9606:C4BPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20851                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C4b-binding protein beta chain|||In isoform 2.|||Interchain (with alpha chain)|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005892|||http://purl.uniprot.org/annotation/VAR_012039|||http://purl.uniprot.org/annotation/VAR_038734|||http://purl.uniprot.org/annotation/VSP_022594
http://togogenome.org/gene/9606:MS4A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BY19                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Membrane-spanning 4-domains subfamily A member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158645|||http://purl.uniprot.org/annotation/VAR_053523
http://togogenome.org/gene/9606:PAQR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L1A2|||http://purl.uniprot.org/uniprot/I3L265|||http://purl.uniprot.org/uniprot/Q8N4S7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Progestin and adipoQ receptor family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218848|||http://purl.uniprot.org/annotation/VSP_011481|||http://purl.uniprot.org/annotation/VSP_011482
http://togogenome.org/gene/9606:SLC2A13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QE2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proton myo-inositol cotransporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050456
http://togogenome.org/gene/9606:LRP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75096                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Compromises AGRN-mediated up-regulation of MUSK signaling.|||Compromises Wnt-suppressive activity.|||Cytoplasmic|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3|||Endocytosis signal|||Extracellular|||Helical|||In CLSS.|||In CLSS; abolishes the antagonistic effect of LRP4 on LRP6-mediated activation of Wnt signaling.|||In CMS17; decreases binding affinity for AGRN and MUSK proteins; does not enhance downstream activation of the MUSK signaling pathway thus impairing clustering of AChRs.|||In SOST2; impairs the interaction with SOST; loss of function as facilitator of SOST-mediated inhibition of Wnt signaling; has no effect on AGRN-mediated MUSK signaling; retains the ability to bind AGRN and MUSK.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 18|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Low-density lipoprotein receptor-related protein 4|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017325|||http://purl.uniprot.org/annotation/VAR_057955|||http://purl.uniprot.org/annotation/VAR_057956|||http://purl.uniprot.org/annotation/VAR_057957|||http://purl.uniprot.org/annotation/VAR_058290|||http://purl.uniprot.org/annotation/VAR_058291|||http://purl.uniprot.org/annotation/VAR_058292|||http://purl.uniprot.org/annotation/VAR_063776|||http://purl.uniprot.org/annotation/VAR_063777|||http://purl.uniprot.org/annotation/VAR_063778|||http://purl.uniprot.org/annotation/VAR_063779|||http://purl.uniprot.org/annotation/VAR_063780|||http://purl.uniprot.org/annotation/VAR_063781|||http://purl.uniprot.org/annotation/VAR_063782|||http://purl.uniprot.org/annotation/VAR_066630|||http://purl.uniprot.org/annotation/VAR_066631|||http://purl.uniprot.org/annotation/VAR_073695|||http://purl.uniprot.org/annotation/VAR_073696
http://togogenome.org/gene/9606:FNDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBE3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Fibronectin type III domain-containing protein 9|||Fibronectin type-III|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299409|||http://purl.uniprot.org/annotation/VAR_047138|||http://purl.uniprot.org/annotation/VAR_047139|||http://purl.uniprot.org/annotation/VAR_047140
http://togogenome.org/gene/9606:PREB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MC98|||http://purl.uniprot.org/uniprot/Q05DB2|||http://purl.uniprot.org/uniprot/Q9HCU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Prolactin regulatory element-binding protein|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051154
http://togogenome.org/gene/9606:APP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRG2|||http://purl.uniprot.org/uniprot/A0A140VJC8|||http://purl.uniprot.org/uniprot/B4DGD0|||http://purl.uniprot.org/uniprot/B4DJT9|||http://purl.uniprot.org/uniprot/E9PG40|||http://purl.uniprot.org/uniprot/P05067                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  50% decrease in copper reducing activity.|||60-70% zinc-induced amyloid-beta protein 28 aggregation.|||APP internalization unchanged. No change in amyloid-beta protein 42 secretion.|||Abolishes chondroitin sulfate binding in L-APP733 isoform.|||Acidic residues|||Amyloid-beta A4 protein|||Amyloid-beta precursor protein|||Amyloid-beta protein 40|||Amyloid-beta protein 42|||BPTI/Kunitz inhibitor|||Basolateral sorting signal|||Binds copper. Forms dimer.|||Binds copper. No dimer formation. No copper reducing activity.|||C31|||C80|||C83|||C99|||Causes formation of an artifactual disulfide bond with PSEN1.|||Cleavage; by ACE|||Cleavage; by alpha-secretase|||Cleavage; by beta-secretase|||Cleavage; by caspase-6, caspase-8 or caspase-9|||Cleavage; by caspase-6; when associated with variant 670-N-L-671|||Cleavage; by caspases|||Cleavage; by gamma-secretase; site 1|||Cleavage; by gamma-secretase; site 2|||Cleavage; by gamma-secretase; site 3|||Cleavage; by theta-secretase|||Collagen-binding|||CuBD subdomain|||Cytoplasmic|||Decreased amyloid-beta protein 42/total amyloid-beta ratio.|||Disordered|||E1|||E2|||Extracellular|||GFLD subdomain|||Gamma-secretase C-terminal fragment 50|||Gamma-secretase C-terminal fragment 57|||Gamma-secretase C-terminal fragment 59|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Greatly reduced casein kinase phosphorylation.|||Greatly reduced copper-mediated low-density lipoprotein oxidation.|||Greatly reduces the binding to SHC1 and APBB family members; no effect on NGF-stimulated neurite extension. Loss of phosphorylation by LRRK2.|||Helical|||Heparin-binding|||Implicated in free radical propagation|||In AD1.|||In AD1; Flemish mutation; increases the solubility of processed amyloid-beta peptides and increases the stability of peptide oligomers.|||In AD1; Swedish mutation; highly increases hydrolysis by BACE1 and amyloid-beta proteins production.|||In AD1; decreased amyloid-beta protein 40/total amyloid-beta.|||In AD1; increased amyloid-beta protein 42/40 ratio.|||In CAA-APP; Dutch type.|||In CAA-APP; Iowa type.|||In CAA-APP; Italian type.|||In a patient with late onset Alzheimer disease.|||In isoform 11.|||In isoform APP305.|||In isoform APP639.|||In isoform APP695 and isoform L-APP677.|||In isoform APP695, isoform L-APP696, isoform L-APP677 and isoform APP714.|||In isoform L-APP677, isoform L-APP696, isoform L-APP733 and isoform L-APP752.|||In isoform L-APP696 and isoform APP714.|||In isoform L-APP733 and isoform APP751.|||In one chronic schizophrenia patient; unknown pathological significance.|||Increased amyloid-beta protein 42/40 ratio. No change in apoptosis after caspase cleavage.|||Interaction with G(o)-alpha|||Interaction with PSEN1|||Little APP internalization. Reduced amyloid-beta protein 42 secretion.|||Loss of a copper binding site; when associated with A-147.|||Loss of a copper binding site; when associated with A-151.|||Loss of binding to APBA1 and APBB1. APP internalization unchanged. No change in amyloid-beta protein 42 secretion.|||Loss of binding to MAPK8IP1, APBA1, APBB1, APPBP2 and SHC1.|||Loss of the copper binding site in the GFLD subdomain; when associated with A-108.|||Loss of the copper binding site in the GFLD subdomain; when associated with A-110.|||N-APP|||N-linked (GlcNAc...) asparagine|||No binding to APBA1, no effect on APBB1 binding. Little APP internalization. Reduced amyloid-beta protein 42 secretion.|||No cleavage by caspases during apoptosis.|||No effect on APBA1 nor APBB1 binding. Greatly reduces the binding to APPBP2. APP internalization unchanged. No change in amyloid-beta protein 42 secretion.|||No effect on C99 interaction with SORL1.|||No effect on FADD-induced apoptosis.|||No free radical production. No hippocampal neuron toxicity.|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine; partial|||O-linked (HexNAc...) threonine; partial|||O-linked (HexNAc...) tyrosine; partial|||O-linked (Xyl...) (chondroitin sulfate) serine; in L-APP isoforms|||OX-2|||Only 23% zinc-induced amyloid-beta protein 28 aggregation.|||P3(40)|||P3(42)|||Phosphoserine; by APP-kinase I|||Phosphoserine; by CK1|||Phosphoserine; by CK2|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphothreonine; by CDK5 and MAPK10|||Phosphotyrosine|||Polar residues|||Reactive bond|||Reduced NGF-stimulated neurite extension. No effect on APP maturation.|||Reduced affinity for heparin; when associated with A-499.|||Reduced affinity for heparin; when associated with A-503.|||Reduced casein kinase phosphorylation.|||Reduced heparin-binding.|||Reduced lipid peroxidation inhibition.|||Reduced protein oxidation. No hippocampal neuron toxicity.|||Required for Cu(2+) reduction|||Required for the interaction with KIF5B and for anterograde transport in axons|||Soluble APP-alpha|||Soluble APP-beta|||Some decrease in copper reducing activity.|||Sulfotyrosine|||Susceptible to oxidation|||Unchanged amyloid-beta protein 42/total amyloid-beta ratio.|||YENPXY motif; contains endocytosis signal ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000088|||http://purl.uniprot.org/annotation/PRO_0000000089|||http://purl.uniprot.org/annotation/PRO_0000000090|||http://purl.uniprot.org/annotation/PRO_0000000091|||http://purl.uniprot.org/annotation/PRO_0000000092|||http://purl.uniprot.org/annotation/PRO_0000000093|||http://purl.uniprot.org/annotation/PRO_0000000094|||http://purl.uniprot.org/annotation/PRO_0000000095|||http://purl.uniprot.org/annotation/PRO_0000000096|||http://purl.uniprot.org/annotation/PRO_0000000097|||http://purl.uniprot.org/annotation/PRO_0000000098|||http://purl.uniprot.org/annotation/PRO_0000000099|||http://purl.uniprot.org/annotation/PRO_0000000100|||http://purl.uniprot.org/annotation/PRO_0000381966|||http://purl.uniprot.org/annotation/PRO_0000384574|||http://purl.uniprot.org/annotation/PRO_5002803541|||http://purl.uniprot.org/annotation/PRO_5003242798|||http://purl.uniprot.org/annotation/PRO_5007491718|||http://purl.uniprot.org/annotation/VAR_000015|||http://purl.uniprot.org/annotation/VAR_000016|||http://purl.uniprot.org/annotation/VAR_000017|||http://purl.uniprot.org/annotation/VAR_000018|||http://purl.uniprot.org/annotation/VAR_000019|||http://purl.uniprot.org/annotation/VAR_000020|||http://purl.uniprot.org/annotation/VAR_000021|||http://purl.uniprot.org/annotation/VAR_000022|||http://purl.uniprot.org/annotation/VAR_000023|||http://purl.uniprot.org/annotation/VAR_010107|||http://purl.uniprot.org/annotation/VAR_010108|||http://purl.uniprot.org/annotation/VAR_010109|||http://purl.uniprot.org/annotation/VAR_014215|||http://purl.uniprot.org/annotation/VAR_014216|||http://purl.uniprot.org/annotation/VAR_014217|||http://purl.uniprot.org/annotation/VAR_014218|||http://purl.uniprot.org/annotation/VAR_014219|||http://purl.uniprot.org/annotation/VAR_022315|||http://purl.uniprot.org/annotation/VAR_032276|||http://purl.uniprot.org/annotation/VAR_032277|||http://purl.uniprot.org/annotation/VAR_044424|||http://purl.uniprot.org/annotation/VSP_000002|||http://purl.uniprot.org/annotation/VSP_000003|||http://purl.uniprot.org/annotation/VSP_000004|||http://purl.uniprot.org/annotation/VSP_000005|||http://purl.uniprot.org/annotation/VSP_000006|||http://purl.uniprot.org/annotation/VSP_000007|||http://purl.uniprot.org/annotation/VSP_000008|||http://purl.uniprot.org/annotation/VSP_000009|||http://purl.uniprot.org/annotation/VSP_009116|||http://purl.uniprot.org/annotation/VSP_009117|||http://purl.uniprot.org/annotation/VSP_009118|||http://purl.uniprot.org/annotation/VSP_045446|||http://purl.uniprot.org/annotation/VSP_045447
http://togogenome.org/gene/9606:PDGFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04085                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In isoform Short.|||Interchain|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor subunit A|||Receptor binding site|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023356|||http://purl.uniprot.org/annotation/PRO_0000023357|||http://purl.uniprot.org/annotation/VSP_004602|||http://purl.uniprot.org/annotation/VSP_004603
http://togogenome.org/gene/9606:RPS18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62269                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||N-acetylserine|||N6-acetyllysine; alternate|||Removed|||Small ribosomal subunit protein uS13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000132212
http://togogenome.org/gene/9606:POU2AF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K830                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with POU2F3.|||Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||OCA|||POU class 2 homeobox associating factor 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335687|||http://purl.uniprot.org/annotation/VSP_061665|||http://purl.uniprot.org/annotation/VSP_061666|||http://purl.uniprot.org/annotation/VSP_061667
http://togogenome.org/gene/9606:MROH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDA8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Maestro heat-like repeat-containing protein family member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329402|||http://purl.uniprot.org/annotation/VAR_062166|||http://purl.uniprot.org/annotation/VSP_032963|||http://purl.uniprot.org/annotation/VSP_032965|||http://purl.uniprot.org/annotation/VSP_032966|||http://purl.uniprot.org/annotation/VSP_032967|||http://purl.uniprot.org/annotation/VSP_032968|||http://purl.uniprot.org/annotation/VSP_032969|||http://purl.uniprot.org/annotation/VSP_032970|||http://purl.uniprot.org/annotation/VSP_032971|||http://purl.uniprot.org/annotation/VSP_032972|||http://purl.uniprot.org/annotation/VSP_032973|||http://purl.uniprot.org/annotation/VSP_032974|||http://purl.uniprot.org/annotation/VSP_032975|||http://purl.uniprot.org/annotation/VSP_032976|||http://purl.uniprot.org/annotation/VSP_032977|||http://purl.uniprot.org/annotation/VSP_032978
http://togogenome.org/gene/9606:TM4SF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48230                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane 4 L6 family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219299
http://togogenome.org/gene/9606:DPY19L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZPD9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Probable C-mannosyltransferase DPY19L3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311901|||http://purl.uniprot.org/annotation/VAR_037336|||http://purl.uniprot.org/annotation/VSP_029634|||http://purl.uniprot.org/annotation/VSP_029635
http://togogenome.org/gene/9606:ZHX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4I2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||Disordered|||Homeobox 1|||Homeobox 2|||Homeobox 3|||Homeobox 4|||Homeobox 5|||In isoform 2.|||Phosphoserine|||Polar residues|||Required for homodimerization and interaction with NFYA|||Required for nuclear localization|||Required for repressor activity|||Zinc fingers and homeoboxes protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049395|||http://purl.uniprot.org/annotation/VAR_049597|||http://purl.uniprot.org/annotation/VSP_054307
http://togogenome.org/gene/9606:C10orf120                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SQS8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C10orf120                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243940|||http://purl.uniprot.org/annotation/VAR_050859|||http://purl.uniprot.org/annotation/VAR_050860
http://togogenome.org/gene/9606:SRPRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08240                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||NG domain|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced SR compaction. Impaired interaction with SRP. Impaired detachement from ribosome. Does not impair GTP hydrolysis by the SRP-SR complex.|||Signal recognition particle receptor subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101213|||http://purl.uniprot.org/annotation/VSP_046055
http://togogenome.org/gene/9606:ASF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y294                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Abolished phosphorylation in response to DNA damage.|||Abrogates interaction with CHAF1B and HIRA.|||Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci.|||Abrogates interaction with histone H3 and histone H4. Loss of interaction with TLK2. Reduced phosphorylation.|||Does not affect phosphorylation in response to DNA damage.|||Histone chaperone ASF1A|||Interaction with histone H3, CHAF1B, and HIRA|||Loss of interaction with TLK2.|||Loss of interaction with TLK2. Reduced phosphorylation.|||Mimics phosphorylation; promoting recruitment to chromatin in response to DNA damage.|||Phosphoserine; by PRKDC and TLK2|||Reduces interaction with histone H3.|||Required for interaction with HIRA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284012
http://togogenome.org/gene/9606:MRTFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULH7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form ZFTA-MRTFB fusion protein|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Myocardin-related transcription factor B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RPEL 1|||RPEL 2|||RPEL 3|||Required for interaction with itself and with MRTFA|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126628|||http://purl.uniprot.org/annotation/VAR_064732|||http://purl.uniprot.org/annotation/VSP_007653|||http://purl.uniprot.org/annotation/VSP_007654|||http://purl.uniprot.org/annotation/VSP_007655|||http://purl.uniprot.org/annotation/VSP_007656|||http://purl.uniprot.org/annotation/VSP_007657|||http://purl.uniprot.org/annotation/VSP_013355|||http://purl.uniprot.org/annotation/VSP_013356
http://togogenome.org/gene/9606:HERC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15751                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  B30.2/SPRY|||Basic and acidic residues|||De novo variant found in a patient with childhood apraxia of speech; unknown pathological significance.|||Disordered|||Glycyl thioester intermediate|||HECT|||In MDFPMR.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable E3 ubiquitin-protein ligase HERC1|||RCC1 1|||RCC1 10|||RCC1 11|||RCC1 12|||RCC1 13|||RCC1 14|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 7|||RCC1 8|||RCC1 9|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328871|||http://purl.uniprot.org/annotation/VAR_042556|||http://purl.uniprot.org/annotation/VAR_042557|||http://purl.uniprot.org/annotation/VAR_042558|||http://purl.uniprot.org/annotation/VAR_042559|||http://purl.uniprot.org/annotation/VAR_042560|||http://purl.uniprot.org/annotation/VAR_042561|||http://purl.uniprot.org/annotation/VAR_042562|||http://purl.uniprot.org/annotation/VAR_042563|||http://purl.uniprot.org/annotation/VAR_042564|||http://purl.uniprot.org/annotation/VAR_042565|||http://purl.uniprot.org/annotation/VAR_042566|||http://purl.uniprot.org/annotation/VAR_042567|||http://purl.uniprot.org/annotation/VAR_057122|||http://purl.uniprot.org/annotation/VAR_076995|||http://purl.uniprot.org/annotation/VAR_081534
http://togogenome.org/gene/9606:TNFAIP8L2-SCNM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In OFD19; the genetic variation producing this missense variant predominantly affects splicing and the resulting mRNA is predicted to undergo nonsense-mediated mRNA decay.|||In isoform 2.|||In isoform 3.|||Matrin-type|||Phosphoserine|||Required for interaction with LUC7L2|||Sodium channel modifier 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259635|||http://purl.uniprot.org/annotation/VAR_087730|||http://purl.uniprot.org/annotation/VSP_021489|||http://purl.uniprot.org/annotation/VSP_053982|||http://purl.uniprot.org/annotation/VSP_053983
http://togogenome.org/gene/9606:EPN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H201                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 3 AA repeats of N-P-F|||4|||5|||5 X 3 AA repeats of [DE]-P-W|||Basic and acidic residues|||Disordered|||ENTH|||Epsin-3|||In isoform 2.|||Phosphoserine|||Polar residues|||Pro residues|||UIM 1|||UIM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074519|||http://purl.uniprot.org/annotation/VAR_059973|||http://purl.uniprot.org/annotation/VSP_009158|||http://purl.uniprot.org/annotation/VSP_009159
http://togogenome.org/gene/9606:DUSP28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G0W2                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  Decreases the already low catalytic activity.|||Dual specificity phosphatase 28|||Increases activity with phosphotyrosine; when associated with A-105.|||Increases activity with phosphotyrosine; when associated with V-107.|||Loss of catalytic activity.|||Phosphocysteine intermediate|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302840
http://togogenome.org/gene/9606:BHLHE22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF88|||http://purl.uniprot.org/uniprot/Q8NFJ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  BHLH|||Class E basic helix-loop-helix protein 22|||Disordered|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274285|||http://purl.uniprot.org/annotation/VAR_061255
http://togogenome.org/gene/9606:WNT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56705                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In MULLAPL; unable to suppress expression of steroidogenic enzymes in ovarian and adrenal cell lines.|||In MULLAPL; unable to suppress steroidogenesis in an ovarian adenocarcinoma cell line resulting in increased androgen production.|||In MULLAPL; with androgen excess, normal kidney size and location; unable to suppress expression of steroidogenic enzymes in ovarian; impairs protein secretion.|||In SERKAL; reduced transcript levels.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Protein Wnt-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041421|||http://purl.uniprot.org/annotation/VAR_034703|||http://purl.uniprot.org/annotation/VAR_043497|||http://purl.uniprot.org/annotation/VAR_043498|||http://purl.uniprot.org/annotation/VAR_043499|||http://purl.uniprot.org/annotation/VAR_052955|||http://purl.uniprot.org/annotation/VSP_054017
http://togogenome.org/gene/9606:RIPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y572                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished cleavage by S.flexneri OspD3.|||Abolishes ability to mediate necroptosis. Partial loss of kinase activity. No loss of PELI1-mediated degradation.|||Abolishes kinase activity and ability to mediate necroptosis.|||Abolishes kinase activity.|||Abolishes kinase activity. Loss of PGAM5- and MLKL-binding. No effect on RIPK1-binding. Loss of interaction with PELI1 and PELI1-mediated ubiquitination. No loss of STUB1-mediated ubiquitination.|||Abolishes kinase activity. Loss of interaction with PELI1 and PELI1-mediated ubiquitination. No loss of interaction with STUB1 and STUB1-mediated ubiquitination. No loss of interaction with RIPK1. Loss of ability to mediate TNF-induced necroptosis. Loss of autophosphorylation at Ser-227.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Loss of PELI1-mediated ubiquitination. No loss of interaction with PELI1.|||Loss of interaction with PELI1 and PELI1-mediated ubiquitination.|||No loss of PELI1-mediated degradation.|||No loss of interaction with PELI1 and PELI1-mediated ubiquitination. No loss of interaction with RIPK1 and MLKL.|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||RIP homotypic interaction motif (RHIM)|||Receptor-interacting serine/threonine-protein kinase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086610|||http://purl.uniprot.org/annotation/VAR_041048|||http://purl.uniprot.org/annotation/VAR_041049|||http://purl.uniprot.org/annotation/VAR_051664|||http://purl.uniprot.org/annotation/VSP_035106|||http://purl.uniprot.org/annotation/VSP_035107
http://togogenome.org/gene/9606:FZD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H461                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FZ|||Frizzled-8|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Pro residues|||Wnt-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013000
http://togogenome.org/gene/9606:NR1D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXD3|||http://purl.uniprot.org/uniprot/F1D8P2|||http://purl.uniprot.org/uniprot/Q14995                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||DNA Binding|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Interaction with ZNHIT1|||Modulating|||N6-acetyllysine; by KAT5|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 1 group D member 2|||Phosphoserine; by GSK3-beta|||Polar residues|||Required for phosphorylation by CSNK1E and cytoplasmic localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053501|||http://purl.uniprot.org/annotation/VAR_047377|||http://purl.uniprot.org/annotation/VAR_047378|||http://purl.uniprot.org/annotation/VAR_047379|||http://purl.uniprot.org/annotation/VAR_047380
http://togogenome.org/gene/9606:JMJD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NYC1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes 2-oxoglutarate-binding and enzyme activity.|||Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6|||Decreases interaction with the NET domain of BRD4.|||Disordered|||Impairs both hydroxylation activity and 2-oxoglutarate turnover assays.|||Impairs enzyme activity and 2-oxoglutarate-binding.|||Impairs enzyme activity without affecting 2-oxoglutarate-binding.|||Impairs enzyme activity.|||In isoform 2 and isoform 3.|||In isoform 2.|||JmjC|||Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-187 and A-189.|||Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-187 and A-273.|||Loss of histone arginine demethylase and lysyl-hydroxylase activities. Abolishes homooligomerisation. Loss of arginine demethylase and a lysyl-hydroxylase activities; when associated with A-189 and A-273.|||Nearly abolishes the interaction with the NET domain of BRD4.|||Nuclear localization signal 1|||Nuclear localization signal 2|||Nuclear localization signal 3|||Nuclear localization signal 4|||Nuclear localization signal 5|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129369|||http://purl.uniprot.org/annotation/VSP_014022|||http://purl.uniprot.org/annotation/VSP_014023
http://togogenome.org/gene/9606:SLC22A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63ZE4                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233716|||http://purl.uniprot.org/annotation/VSP_056645|||http://purl.uniprot.org/annotation/VSP_056646|||http://purl.uniprot.org/annotation/VSP_056647
http://togogenome.org/gene/9606:LXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BS40                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-helical linker|||Cystatin LXN-type 1|||Cystatin LXN-type 2|||Latexin|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191343|||http://purl.uniprot.org/annotation/VAR_019117|||http://purl.uniprot.org/annotation/VAR_062139
http://togogenome.org/gene/9606:CDK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49336                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates kinase activity and TFIIH-dependent transcriptional repression.|||Cyclin-dependent kinase 8|||Disordered|||In IDDHBA; decreased protein kinase activity.|||In IDDHBA; unknown pathological significance.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||In isoform 2.|||Interaction with CCNC|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085797|||http://purl.uniprot.org/annotation/VAR_041980|||http://purl.uniprot.org/annotation/VAR_041981|||http://purl.uniprot.org/annotation/VAR_083786|||http://purl.uniprot.org/annotation/VAR_083787|||http://purl.uniprot.org/annotation/VAR_083788|||http://purl.uniprot.org/annotation/VAR_083789|||http://purl.uniprot.org/annotation/VAR_083790|||http://purl.uniprot.org/annotation/VAR_083791|||http://purl.uniprot.org/annotation/VAR_083792|||http://purl.uniprot.org/annotation/VAR_083793|||http://purl.uniprot.org/annotation/VSP_029970
http://togogenome.org/gene/9606:TLR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15455                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In IMD83; causes TLR3 deficiency and predisposition to herpes simplex encephalitis; inhibition of IFNL1 induction.|||In isoform 2.|||Inhibition of IFNL1 induction.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 17|||LRR 18|||LRR 19|||LRR 2|||LRR 20|||LRR 21|||LRR 22|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Loss of RNA binding. Abolishes activation of NF-kappa-B.|||Loss of RNA binding. Constitutive activation of NF-kappa-B.|||Loss of interaction with WDFY1.|||Loss of ubiquitination by TRIM3.|||Loss of ubiquitination by ZNRF1.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on IFNL1 induction.|||No effect.|||Phosphotyrosine|||Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA. Loss of interaction with WDFY1.|||Reduced expression levels; when associated with R-247.|||Reduced response to ds-RNA.|||Reduced response to ds-RNA. Reduced expression levels; when associated with G-196.|||TIR|||Toll-like receptor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034715|||http://purl.uniprot.org/annotation/VAR_021976|||http://purl.uniprot.org/annotation/VAR_024664|||http://purl.uniprot.org/annotation/VAR_052361|||http://purl.uniprot.org/annotation/VAR_052362|||http://purl.uniprot.org/annotation/VAR_054887|||http://purl.uniprot.org/annotation/VAR_084046|||http://purl.uniprot.org/annotation/VAR_084047|||http://purl.uniprot.org/annotation/VAR_084048|||http://purl.uniprot.org/annotation/VAR_084049|||http://purl.uniprot.org/annotation/VAR_084050|||http://purl.uniprot.org/annotation/VAR_084051|||http://purl.uniprot.org/annotation/VAR_084052|||http://purl.uniprot.org/annotation/VSP_054188
http://togogenome.org/gene/9606:RPL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61313                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Large ribosomal subunit protein eL15|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127527|||http://purl.uniprot.org/annotation/VSP_045144
http://togogenome.org/gene/9606:ANAPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H0F9|||http://purl.uniprot.org/uniprot/Q9UJX4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 5|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064597|||http://purl.uniprot.org/annotation/VAR_035793|||http://purl.uniprot.org/annotation/VSP_008466|||http://purl.uniprot.org/annotation/VSP_008467|||http://purl.uniprot.org/annotation/VSP_008468|||http://purl.uniprot.org/annotation/VSP_008469|||http://purl.uniprot.org/annotation/VSP_044878|||http://purl.uniprot.org/annotation/VSP_044879
http://togogenome.org/gene/9606:ETFB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38117                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Does not abolish electron transfer activity. Abolishes sensitivity to inhibition by lysine methyltransferase ETFBKMT.|||Does not abolish electron transfer activity. Decreases sensitivity to inhibition by lysine methyltransferase ETFBKMT.|||Does not abolish methylation by ETFBKMT.|||Drastically increases interprotein electron transfer rates.|||Electron transfer flavoprotein subunit beta|||In GA2B; decreased protein stability.|||In GA2B; reduced electron transfer activity.|||In isoform 2.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; by ETFBKMT|||N6,N6,N6-trimethyllysine; by ETFBKMT; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Recognition loop|||Removed|||Severely impaired in complex formation with ACADM.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167870|||http://purl.uniprot.org/annotation/VAR_002369|||http://purl.uniprot.org/annotation/VAR_008548|||http://purl.uniprot.org/annotation/VAR_025804|||http://purl.uniprot.org/annotation/VSP_017850
http://togogenome.org/gene/9606:IFI44L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53G44                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Interferon-induced protein 44-like|||TLDc                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337845|||http://purl.uniprot.org/annotation/VAR_043726|||http://purl.uniprot.org/annotation/VAR_054648|||http://purl.uniprot.org/annotation/VAR_054649|||http://purl.uniprot.org/annotation/VAR_054650|||http://purl.uniprot.org/annotation/VAR_054651|||http://purl.uniprot.org/annotation/VAR_054652|||http://purl.uniprot.org/annotation/VAR_054653|||http://purl.uniprot.org/annotation/VSP_036554|||http://purl.uniprot.org/annotation/VSP_036555
http://togogenome.org/gene/9606:GSR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00390|||http://purl.uniprot.org/uniprot/V9HW90                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  FAD/NAD(P)-binding|||Glutathione reductase, mitochondrial|||In HAGRD.|||In HAGRD; decreased glutathione reductase activity; decreased enzyme stability.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform Cytoplasmic.|||Interchain|||Mitochondrion|||N6-acetyllysine|||Proton acceptor|||Pyridine nucleotide-disulphide oxidoreductase dimerisation|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030276|||http://purl.uniprot.org/annotation/VAR_014554|||http://purl.uniprot.org/annotation/VAR_019079|||http://purl.uniprot.org/annotation/VAR_019080|||http://purl.uniprot.org/annotation/VAR_019081|||http://purl.uniprot.org/annotation/VAR_019082|||http://purl.uniprot.org/annotation/VAR_051775|||http://purl.uniprot.org/annotation/VAR_083444|||http://purl.uniprot.org/annotation/VAR_083445|||http://purl.uniprot.org/annotation/VSP_018972|||http://purl.uniprot.org/annotation/VSP_042908|||http://purl.uniprot.org/annotation/VSP_042909
http://togogenome.org/gene/9606:UTS2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WCV4|||http://purl.uniprot.org/uniprot/Q765I0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Urotensin-2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036357|||http://purl.uniprot.org/annotation/PRO_0000036358|||http://purl.uniprot.org/annotation/PRO_5003385583|||http://purl.uniprot.org/annotation/VAR_044517
http://togogenome.org/gene/9606:CLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49759                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085866|||http://purl.uniprot.org/annotation/VAR_040409|||http://purl.uniprot.org/annotation/VAR_040410|||http://purl.uniprot.org/annotation/VAR_040411|||http://purl.uniprot.org/annotation/VAR_040412|||http://purl.uniprot.org/annotation/VAR_046551|||http://purl.uniprot.org/annotation/VAR_051620|||http://purl.uniprot.org/annotation/VSP_004852|||http://purl.uniprot.org/annotation/VSP_004853|||http://purl.uniprot.org/annotation/VSP_043578
http://togogenome.org/gene/9606:PFKFB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5C3|||http://purl.uniprot.org/uniprot/Q16877|||http://purl.uniprot.org/uniprot/Q5XLC3|||http://purl.uniprot.org/uniprot/Q66S35                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  6-phosphofructo-2-kinase|||6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4|||Fructose-2,6-bisphosphatase|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phosphothreonine; by PKC|||Proton donor/acceptor|||Tele-phosphohistidine intermediate|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179970|||http://purl.uniprot.org/annotation/VAR_036075|||http://purl.uniprot.org/annotation/VSP_056530|||http://purl.uniprot.org/annotation/VSP_056621
http://togogenome.org/gene/9606:GART                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22102|||http://purl.uniprot.org/uniprot/Q59HH3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  AIRS domain|||ATP-grasp|||GART domain|||Helical|||In isoform Short.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Proton donor|||Raises pKa of active site His|||Removed|||Trifunctional purine biosynthetic protein adenosine-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074937|||http://purl.uniprot.org/annotation/VAR_011817|||http://purl.uniprot.org/annotation/VAR_011818|||http://purl.uniprot.org/annotation/VAR_011819|||http://purl.uniprot.org/annotation/VAR_051882|||http://purl.uniprot.org/annotation/VAR_051883|||http://purl.uniprot.org/annotation/VSP_005517
http://togogenome.org/gene/9606:PTH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01270                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Abolishes processing of the precursor; when associated with variant R-18.|||Basic and acidic residues|||Disordered|||Important for receptor binding|||In FIH1; dominant form; leads to inefficient processing of the precursor; the expressed mutant hormone is trapped intracellularly in the endoplasmic reticulum resulting in apoptosis; mutant protein-expressing cells also show marked up-regulation of the endoplasmic reticulum stress-responsive hormones HSPA5 and EIF2AK3 and the proapoptotic transcription factor DDIT3.|||In FIH1; recessive form; might lead to inefficient processing of the precursor.|||Parathyroid hormone|||Reduced affinity for PTH1R.|||Strongly reduced affinity for PTH1R.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023249|||http://purl.uniprot.org/annotation/PRO_0000023250|||http://purl.uniprot.org/annotation/VAR_006047|||http://purl.uniprot.org/annotation/VAR_018464
http://togogenome.org/gene/9606:LMOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5Q4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In CMD2G.|||In CMD2G; no protein detected by Western blot in cardiac tissue from a homozygous patient.|||In isoform 2.|||In isoform 3.|||Interaction with actin 1|||Interaction with actin 2|||Interaction with actin 3|||Interaction with tropomyosin alpha|||Leiomodin-2|||Mildly impaired activity in promoting actin polymerization.|||Mildly impaired activity in promoting actin polymerization; when associated with D-64.|||Mildly impaired activity in promoting actin polymerization; when associated with D-69.|||Phosphoserine|||Polar residues|||Pro residues|||Strongly impaired activity in promoting actin polymerization.|||Strongly impaired activity in promoting actin polymerization; when associated with G-304 and A-356.|||Strongly impaired activity in promoting actin polymerization; when associated with G-304 and G-334.|||Strongly impaired activity in promoting actin polymerization; when associated with G-334 and A-356.|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311340|||http://purl.uniprot.org/annotation/VAR_087458|||http://purl.uniprot.org/annotation/VAR_087459|||http://purl.uniprot.org/annotation/VSP_029525|||http://purl.uniprot.org/annotation/VSP_029526|||http://purl.uniprot.org/annotation/VSP_029527|||http://purl.uniprot.org/annotation/VSP_029528
http://togogenome.org/gene/9606:SOST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQB4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||CTCK|||Disordered|||In CDD; affects protein secretion.|||In CDD; de novo mutation; affects protein secretion.|||In SOST1; leads to retention of the mutant protein in the endoplasmic reticulum; leads to a complete loss of function of the protein.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sclerostin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033177|||http://purl.uniprot.org/annotation/VAR_063982|||http://purl.uniprot.org/annotation/VAR_065766|||http://purl.uniprot.org/annotation/VAR_065767|||http://purl.uniprot.org/annotation/VSP_010189
http://togogenome.org/gene/9606:GOLT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVE7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||Vesicle transport protein GOT1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000237607
http://togogenome.org/gene/9606:CHRM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08912|||http://purl.uniprot.org/uniprot/Q8IVW0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Muscarinic acetylcholine receptor M5|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069042
http://togogenome.org/gene/9606:TMTC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4D3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Protein O-mannosyl-transferase TMTC4|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280295|||http://purl.uniprot.org/annotation/VAR_031117|||http://purl.uniprot.org/annotation/VAR_031118|||http://purl.uniprot.org/annotation/VAR_036455|||http://purl.uniprot.org/annotation/VSP_023622|||http://purl.uniprot.org/annotation/VSP_023623|||http://purl.uniprot.org/annotation/VSP_038261|||http://purl.uniprot.org/annotation/VSP_054873
http://togogenome.org/gene/9606:KRTAP22-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIV0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 22-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223914|||http://purl.uniprot.org/annotation/VAR_057650|||http://purl.uniprot.org/annotation/VAR_060443
http://togogenome.org/gene/9606:RNASEH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUD4|||http://purl.uniprot.org/uniprot/E5KN15|||http://purl.uniprot.org/uniprot/O60930                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In PEOB2; has partial residual endonuclease activity.|||RNase H type-1|||Ribonuclease H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195433|||http://purl.uniprot.org/annotation/VAR_023469|||http://purl.uniprot.org/annotation/VAR_074561|||http://purl.uniprot.org/annotation/VAR_074562
http://togogenome.org/gene/9606:MMS19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T76                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-1002, 1007-R-R-1008 and R-1013.|||Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, 1007-R-R-1008 and R-1013.|||Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, R-1002 and 1007-R-R-1008.|||Impairs MAGEF1-NSMCE1-mediated polyubiquitination when associated with R-993, R-1002 and R-1013.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MMS19 nucleotide excision repair protein homolog|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096514|||http://purl.uniprot.org/annotation/VAR_023448|||http://purl.uniprot.org/annotation/VAR_023449|||http://purl.uniprot.org/annotation/VAR_023450|||http://purl.uniprot.org/annotation/VAR_023451|||http://purl.uniprot.org/annotation/VAR_023452|||http://purl.uniprot.org/annotation/VAR_023453|||http://purl.uniprot.org/annotation/VAR_023454|||http://purl.uniprot.org/annotation/VAR_023455|||http://purl.uniprot.org/annotation/VAR_023456|||http://purl.uniprot.org/annotation/VAR_023457|||http://purl.uniprot.org/annotation/VAR_023458|||http://purl.uniprot.org/annotation/VSP_015565|||http://purl.uniprot.org/annotation/VSP_040310|||http://purl.uniprot.org/annotation/VSP_040311|||http://purl.uniprot.org/annotation/VSP_040312|||http://purl.uniprot.org/annotation/VSP_040313|||http://purl.uniprot.org/annotation/VSP_044182|||http://purl.uniprot.org/annotation/VSP_044183
http://togogenome.org/gene/9606:VXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Vexin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271014|||http://purl.uniprot.org/annotation/VSP_038986
http://togogenome.org/gene/9606:GPR160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJ42                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 160                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069643
http://togogenome.org/gene/9606:OTULINL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUU6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fails to confer catalytic activity; when associated with C-139.|||Fails to confer catalytic activity; when associated with N-352.|||Inactive ubiquitin thioesterase OTULINL|||Loss of membrane binding.|||OTU|||Required for membrane binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274404|||http://purl.uniprot.org/annotation/VAR_030281
http://togogenome.org/gene/9606:TCAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DST7|||http://purl.uniprot.org/uniprot/Q9Y4C2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Peptidase M60|||TRPM8 channel-associated factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320182|||http://purl.uniprot.org/annotation/VSP_031631
http://togogenome.org/gene/9606:COL4A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZY5|||http://purl.uniprot.org/uniprot/A8MXH5|||http://purl.uniprot.org/uniprot/A8VPY0|||http://purl.uniprot.org/uniprot/B2RTX6|||http://purl.uniprot.org/uniprot/B7ZMM7|||http://purl.uniprot.org/uniprot/F5H3Q5|||http://purl.uniprot.org/uniprot/Q14031                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  7S domain|||Cell attachment site|||Collagen IV NC1|||Collagen alpha-6(IV) chain|||Disordered|||In DFNX6.|||In a colorectal cancer sample; somatic mutation.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Or C-1482 with C-1568|||Or C-1515 with C-1571|||Or C-1590 with C-1684|||Or C-1624 with C-1687|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005853|||http://purl.uniprot.org/annotation/PRO_5001832103|||http://purl.uniprot.org/annotation/PRO_5002726085|||http://purl.uniprot.org/annotation/PRO_5002781865|||http://purl.uniprot.org/annotation/PRO_5002864141|||http://purl.uniprot.org/annotation/PRO_5003324755|||http://purl.uniprot.org/annotation/VAR_015216|||http://purl.uniprot.org/annotation/VAR_015217|||http://purl.uniprot.org/annotation/VAR_032972|||http://purl.uniprot.org/annotation/VAR_032973|||http://purl.uniprot.org/annotation/VAR_032974|||http://purl.uniprot.org/annotation/VAR_035748|||http://purl.uniprot.org/annotation/VAR_059242|||http://purl.uniprot.org/annotation/VAR_070936|||http://purl.uniprot.org/annotation/VSP_001174
http://togogenome.org/gene/9606:ABCF2-H2BK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7Y2|||http://purl.uniprot.org/uniprot/Q9UG63                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family F member 2|||Basic and acidic residues|||Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093323|||http://purl.uniprot.org/annotation/VSP_054715
http://togogenome.org/gene/9606:HSFX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK21|||http://purl.uniprot.org/uniprot/Q9UBD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||HSF-type DNA-binding|||Heat shock transcription factor, X-linked|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339188
http://togogenome.org/gene/9606:USP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z855|||http://purl.uniprot.org/uniprot/B7ZAX6|||http://purl.uniprot.org/uniprot/Q6U8A4|||http://purl.uniprot.org/uniprot/Q93009                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Catalytically inactive mutant. No effect on p53/TP53 and PTEN binding but is defective in deubiquitinating p53/TP53 and PTEN. Partial loss of KMT2E/mml5 deubiquitination. Decreases deubiquitinase activity toward 'Lys-48'-polyubiquitinated ALKBH3. Reduced deubiquitination of REST. Reduced deubiquitination of TRIM27 and WASHC1.|||Complete loss of activity.|||Complete loss of activity. Localized in the nucleus and does not inhibit FOXO4-dependent transcriptional activity. Loss of ability to deubiquitinate CRY2.|||Decreased binding to p53/TP53 and MDM2.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In HAFOUS.|||In HAFOUS; unknown pathological significance; the patient also carries a de novo clinically relevant variant in SLC2A1.|||In HAFOUS; when expressed in USP7-deficient cells does not rescue defective endosomal protein recycling and reduced F-actin levels.|||In isoform 3.|||Interaction with ICP0/VMW110|||Interaction with TSPYL5|||Interaction with p53/TP53, MDM2 and EBNA1|||Loss of binding to p53/TP53 and MDM2.|||MATH|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for nuclear localization|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080626|||http://purl.uniprot.org/annotation/VAR_086825|||http://purl.uniprot.org/annotation/VAR_086826|||http://purl.uniprot.org/annotation/VAR_086827|||http://purl.uniprot.org/annotation/VAR_086828|||http://purl.uniprot.org/annotation/VAR_086829|||http://purl.uniprot.org/annotation/VAR_086830|||http://purl.uniprot.org/annotation/VAR_086831|||http://purl.uniprot.org/annotation/VAR_086832|||http://purl.uniprot.org/annotation/VAR_086833|||http://purl.uniprot.org/annotation/VAR_086834|||http://purl.uniprot.org/annotation/VSP_054884
http://togogenome.org/gene/9606:EGR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZKU3|||http://purl.uniprot.org/uniprot/Q05215                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Early growth response protein 4|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047128
http://togogenome.org/gene/9606:SLC9B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ1|||http://purl.uniprot.org/uniprot/Q4ZJI4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cation/H+ exchanger|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Polar residues|||Sodium/hydrogen exchanger 9B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314007|||http://purl.uniprot.org/annotation/VAR_061370|||http://purl.uniprot.org/annotation/VSP_030175|||http://purl.uniprot.org/annotation/VSP_030176|||http://purl.uniprot.org/annotation/VSP_030177|||http://purl.uniprot.org/annotation/VSP_030180
http://togogenome.org/gene/9606:SMCR8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TEV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanine nucleotide exchange protein SMCR8|||Impaired autophagosome maturation; when associated with A-402.|||Impaired autophagosome maturation; when associated with A-796.|||In isoform 2.|||Interacts with WDR41 within the C9orf72-SMCR8 complex|||Loss of C9ORF72-SMCR8 complex-mediated stimulation of RAB8A and RAB11AGTPase activity.|||Phosphomimetic mutant; able to promote autophagosome maturation; when associated with D-402.|||Phosphomimetic mutant; able to promote autophagosome maturation; when associated with D-796.|||Phosphoserine|||Phosphoserine; by TBK1|||Phosphothreonine; by TBK1|||Polar residues|||Required for the homodimerization of the C9orf72-SMCR8 complex|||cDENN FLCN/SMCR8-type|||dDENN FLCN/SMCR8-type|||uDENN FLCN/SMCR8-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287469|||http://purl.uniprot.org/annotation/VAR_032309|||http://purl.uniprot.org/annotation/VAR_032310|||http://purl.uniprot.org/annotation/VAR_032311|||http://purl.uniprot.org/annotation/VSP_025487
http://togogenome.org/gene/9606:WDR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TDG3|||http://purl.uniprot.org/uniprot/Q9UNX4                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 4-like WD40|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Small-subunit processome Utp12|||WD|||WD 1|||WD 10|||WD 11|||WD 12|||WD 13|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD 9|||WD repeat-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051347|||http://purl.uniprot.org/annotation/VAR_033809
http://togogenome.org/gene/9606:FCGR2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12318                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||In isoform 2.|||Low affinity immunoglobulin gamma Fc region receptor II-a|||May be associated with susceptibility to lupus nephritis; does not efficiently recognize IgG2.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine; by SRC-type Tyr-kinases                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015145|||http://purl.uniprot.org/annotation/VAR_003955|||http://purl.uniprot.org/annotation/VAR_054857|||http://purl.uniprot.org/annotation/VAR_054858|||http://purl.uniprot.org/annotation/VAR_054859|||http://purl.uniprot.org/annotation/VSP_036865
http://togogenome.org/gene/9606:KAZALD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I82                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  IGFBP N-terminal|||Ig-like C2-type|||In isoform 2.|||Kazal-like|||Kazal-type serine protease inhibitor domain-containing protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015076|||http://purl.uniprot.org/annotation/VAR_022739|||http://purl.uniprot.org/annotation/VAR_033628|||http://purl.uniprot.org/annotation/VAR_033629|||http://purl.uniprot.org/annotation/VAR_049977|||http://purl.uniprot.org/annotation/VSP_014303|||http://purl.uniprot.org/annotation/VSP_014304
http://togogenome.org/gene/9606:ISX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M1V0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Intestine-specific homeobox                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288602|||http://purl.uniprot.org/annotation/VAR_032448|||http://purl.uniprot.org/annotation/VAR_032449|||http://purl.uniprot.org/annotation/VAR_032450|||http://purl.uniprot.org/annotation/VAR_032451
http://togogenome.org/gene/9606:ALAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DVA0|||http://purl.uniprot.org/uniprot/P13196|||http://purl.uniprot.org/uniprot/Q5JAM2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  5-aminolevulinate synthase presequence|||5-aminolevulinate synthase, non-specific, mitochondrial|||Aminotransferase class I/classII|||Disordered|||Hydroxyproline|||In isoform 2.|||Loss of interaction with VHL.|||Mitochondrion|||N6-(pyridoxal phosphate)lysine|||Polar residues|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001230|||http://purl.uniprot.org/annotation/VSP_025924|||http://purl.uniprot.org/annotation/VSP_025925
http://togogenome.org/gene/9606:SERPINB13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQW3|||http://purl.uniprot.org/uniprot/B7Z447|||http://purl.uniprot.org/uniprot/Q9UIV8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Reactive bond|||Serpin|||Serpin B13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094121|||http://purl.uniprot.org/annotation/VAR_024356|||http://purl.uniprot.org/annotation/VSP_006058
http://togogenome.org/gene/9606:ZNF331                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D63|||http://purl.uniprot.org/uniprot/Q71QC4|||http://purl.uniprot.org/uniprot/Q71QC5|||http://purl.uniprot.org/uniprot/Q71QC6|||http://purl.uniprot.org/uniprot/Q9NQX6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 331                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047535
http://togogenome.org/gene/9606:MLX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UH92                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform Alpha and isoform Beta.|||In isoform Alpha.|||Leucine-zipper|||Max-like protein X|||Phosphoserine|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127279|||http://purl.uniprot.org/annotation/VAR_049547|||http://purl.uniprot.org/annotation/VSP_002137|||http://purl.uniprot.org/annotation/VSP_002138
http://togogenome.org/gene/9606:GCLC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48506                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Glutamate--cysteine ligase catalytic subunit|||In HAGGSD.|||In HAGGSD; strongly decreased glutamate-cysteine ligase activity.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192563|||http://purl.uniprot.org/annotation/VAR_013514|||http://purl.uniprot.org/annotation/VAR_014884|||http://purl.uniprot.org/annotation/VAR_015403|||http://purl.uniprot.org/annotation/VAR_021100|||http://purl.uniprot.org/annotation/VAR_021110
http://togogenome.org/gene/9606:CNTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12860                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Contactin-1|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||GPI-anchor amidated serine|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014685|||http://purl.uniprot.org/annotation/PRO_0000014686|||http://purl.uniprot.org/annotation/VAR_011722|||http://purl.uniprot.org/annotation/VAR_035506|||http://purl.uniprot.org/annotation/VAR_049866|||http://purl.uniprot.org/annotation/VSP_002500|||http://purl.uniprot.org/annotation/VSP_011959|||http://purl.uniprot.org/annotation/VSP_011960
http://togogenome.org/gene/9606:ANKRD65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RJM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 65|||Disordered|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000414484|||http://purl.uniprot.org/annotation/VSP_042085|||http://purl.uniprot.org/annotation/VSP_042086|||http://purl.uniprot.org/annotation/VSP_045962|||http://purl.uniprot.org/annotation/VSP_045963
http://togogenome.org/gene/9606:PRR14L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5THK1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Protein PRR14L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295739|||http://purl.uniprot.org/annotation/VAR_059641|||http://purl.uniprot.org/annotation/VAR_059642|||http://purl.uniprot.org/annotation/VAR_059643|||http://purl.uniprot.org/annotation/VAR_059644|||http://purl.uniprot.org/annotation/VAR_059645|||http://purl.uniprot.org/annotation/VAR_059646|||http://purl.uniprot.org/annotation/VAR_059647|||http://purl.uniprot.org/annotation/VAR_059648|||http://purl.uniprot.org/annotation/VAR_059649|||http://purl.uniprot.org/annotation/VAR_061637|||http://purl.uniprot.org/annotation/VSP_027046|||http://purl.uniprot.org/annotation/VSP_027047|||http://purl.uniprot.org/annotation/VSP_027048|||http://purl.uniprot.org/annotation/VSP_027049
http://togogenome.org/gene/9606:PRDM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQV7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||DNA-binding|||Disordered|||Histone-lysine N-methyltransferase PRDM9|||In allele A.|||In allele L13; Increases affinity for the DNA-binding motif 5'-GCCTCCCTAGCCACG-3'.|||In allele L20; reduces affinity for the DNA-binding motif 5?-GCCTCCCTAGCCACG-3'.|||In allele L9/24; significantly reduces affinity for the DNA-binding motif 5'-GCCTCCCTAGCCACG-3'.|||Increases histone-lysine N-methyltransferase activity; when associated with D-374.|||Increases histone-lysine N-methyltransferase activity; when associated with Y-199.|||KRAB-related|||Loss of histone-lysine N-methyltransferase activity.|||N6,N6,N6-trimethyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||Polar residues|||SET|||Variant of uncertain significance; may be a genetic risk for patients with azoospermia caused by meiotic arrest.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047766|||http://purl.uniprot.org/annotation/VAR_054417|||http://purl.uniprot.org/annotation/VAR_082281|||http://purl.uniprot.org/annotation/VAR_082282|||http://purl.uniprot.org/annotation/VAR_082283|||http://purl.uniprot.org/annotation/VAR_082284
http://togogenome.org/gene/9606:TMEM243                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JY04|||http://purl.uniprot.org/uniprot/Q9BU79                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetylmethionine|||Transmembrane protein 243                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089579
http://togogenome.org/gene/9606:VPS35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QK1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disrupts interaction with VPS26; no effect on interaction with VPS29.|||Disrupts interaction with VPS29. Does not effect interaction with VPS26.|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||Found in a patient with Parkinson disease.|||In PARK17; decreases interaction with WASHC2C, FKBP15 and the WASH complex; impairs recruitment of the WASH complex to endosomes; shows reduced retrograde transport of selective cargo between lysosomes and the Golgi apparatus; shows a progressive reduction in neurite length and branching.|||Interaction with IGF2R cytoplasmic domain|||Interaction with SLC11A2|||Interaction with SNX3|||Phosphoserine|||Phosphotyrosine|||Vacuolar protein sorting-associated protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065896|||http://purl.uniprot.org/annotation/VAR_054046|||http://purl.uniprot.org/annotation/VAR_066653|||http://purl.uniprot.org/annotation/VAR_066654|||http://purl.uniprot.org/annotation/VAR_066655|||http://purl.uniprot.org/annotation/VAR_066656|||http://purl.uniprot.org/annotation/VAR_066657|||http://purl.uniprot.org/annotation/VAR_066658|||http://purl.uniprot.org/annotation/VAR_066659|||http://purl.uniprot.org/annotation/VAR_066660|||http://purl.uniprot.org/annotation/VAR_066661|||http://purl.uniprot.org/annotation/VAR_080769
http://togogenome.org/gene/9606:TWIST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15672                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Found in a patient with non-syndromic ventricular septal defect; unknown pathological significance; loss of function in negative regulation of transcription from E-cadherin promoter.|||In CRS1.|||In SCS.|||In SCS; variant form with features overlapping Baller-Gerold syndrome.|||In SWCOS.|||No effect on negative regulation of transcription from E-cadherin promoter.|||Polar residues|||Sufficient for transactivation activity|||Twist-related protein 1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127483|||http://purl.uniprot.org/annotation/VAR_004495|||http://purl.uniprot.org/annotation/VAR_004496|||http://purl.uniprot.org/annotation/VAR_004497|||http://purl.uniprot.org/annotation/VAR_004498|||http://purl.uniprot.org/annotation/VAR_015219|||http://purl.uniprot.org/annotation/VAR_034985|||http://purl.uniprot.org/annotation/VAR_034986|||http://purl.uniprot.org/annotation/VAR_077470|||http://purl.uniprot.org/annotation/VAR_077471|||http://purl.uniprot.org/annotation/VAR_080515|||http://purl.uniprot.org/annotation/VAR_080516
http://togogenome.org/gene/9606:PPM1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8E4|||http://purl.uniprot.org/uniprot/P35813                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 3.|||In isoform Alpha-2.|||N-myristoyl glycine|||No effect on binding SMAD2.|||PPM-type phosphatase|||Phosphoserine|||Protein phosphatase 1A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057741|||http://purl.uniprot.org/annotation/VSP_005085|||http://purl.uniprot.org/annotation/VSP_005086|||http://purl.uniprot.org/annotation/VSP_045687
http://togogenome.org/gene/9606:CDH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33151|||http://purl.uniprot.org/uniprot/Q59EA3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-5|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Required for interaction with PALS1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003755|||http://purl.uniprot.org/annotation/PRO_0000003756|||http://purl.uniprot.org/annotation/VAR_028003|||http://purl.uniprot.org/annotation/VAR_028004|||http://purl.uniprot.org/annotation/VSP_053861
http://togogenome.org/gene/9606:MPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5U8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||In MPYCD.|||In MPYCD; inactive.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrial pyruvate carrier 1|||N-acetylalanine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212797|||http://purl.uniprot.org/annotation/VAR_052486|||http://purl.uniprot.org/annotation/VAR_068099|||http://purl.uniprot.org/annotation/VAR_068100
http://togogenome.org/gene/9606:TENT5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A09                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Does not affect polyadenylation activity.|||Loss of polyadenylation activity.|||Reduces polyadenylation activity.|||Substantially reduces polyadenylation activity.|||Terminal nucleotidyltransferase 5B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259931
http://togogenome.org/gene/9606:CTXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4LDR2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Cortexin-3|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284513|||http://purl.uniprot.org/annotation/VAR_031763|||http://purl.uniprot.org/annotation/VAR_053885
http://togogenome.org/gene/9606:UNC13A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPW8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2 1|||C2 2|||C2 3|||Disordered|||MHD1|||MHD2|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein unc-13 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188573|||http://purl.uniprot.org/annotation/VAR_061872
http://togogenome.org/gene/9606:TFPI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10646                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes inhibition of VII(a)/TF.|||Abolishes inhibition of X(a).|||BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||BPTI/Kunitz inhibitor 3|||In isoform Beta.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (GalNAc...) serine; partial|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||Reactive bond|||Tissue factor pathway inhibitor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016871|||http://purl.uniprot.org/annotation/VAR_012004|||http://purl.uniprot.org/annotation/VSP_003030|||http://purl.uniprot.org/annotation/VSP_003031
http://togogenome.org/gene/9606:OR2T10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV79|||http://purl.uniprot.org/uniprot/Q8NGZ9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2T10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150502
http://togogenome.org/gene/9606:MADD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRB5|||http://purl.uniprot.org/uniprot/Q8WXG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Death|||Disordered|||In DEEAH and NEDDISH; unknown pathological significance.|||In DEEAH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization.|||In DEEAH; unknown pathological significance.|||In NEDDISH; impaired TNFA-induced activation of the MAP kinases ERK1/2; enhanced susceptibility to TNFA-induced apoptosis; decreased EGF internalization.|||In NEDDISH; unknown pathological significance.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8.|||In isoform 3, isoform 5, isoform 6 and isoform 8.|||In isoform 3.|||In isoform 4, isoform 5, isoform 6 and isoform 8.|||In isoform 6 and isoform 7.|||In isoform 8.|||MAP kinase-activating death domain protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||UDENN|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278138|||http://purl.uniprot.org/annotation/VAR_030666|||http://purl.uniprot.org/annotation/VAR_030667|||http://purl.uniprot.org/annotation/VAR_030668|||http://purl.uniprot.org/annotation/VAR_030669|||http://purl.uniprot.org/annotation/VAR_051148|||http://purl.uniprot.org/annotation/VAR_051149|||http://purl.uniprot.org/annotation/VAR_084659|||http://purl.uniprot.org/annotation/VAR_084660|||http://purl.uniprot.org/annotation/VAR_084661|||http://purl.uniprot.org/annotation/VAR_084662|||http://purl.uniprot.org/annotation/VAR_084663|||http://purl.uniprot.org/annotation/VAR_084664|||http://purl.uniprot.org/annotation/VAR_084665|||http://purl.uniprot.org/annotation/VAR_084666|||http://purl.uniprot.org/annotation/VAR_084667|||http://purl.uniprot.org/annotation/VAR_084668|||http://purl.uniprot.org/annotation/VAR_084669|||http://purl.uniprot.org/annotation/VAR_084670|||http://purl.uniprot.org/annotation/VAR_084671|||http://purl.uniprot.org/annotation/VAR_084672|||http://purl.uniprot.org/annotation/VAR_084673|||http://purl.uniprot.org/annotation/VSP_044848|||http://purl.uniprot.org/annotation/VSP_052293|||http://purl.uniprot.org/annotation/VSP_052294|||http://purl.uniprot.org/annotation/VSP_052295|||http://purl.uniprot.org/annotation/VSP_052296|||http://purl.uniprot.org/annotation/VSP_052297|||http://purl.uniprot.org/annotation/VSP_052298|||http://purl.uniprot.org/annotation/VSP_055676
http://togogenome.org/gene/9606:NOP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86U38                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Nucleolar protein 9|||Phosphoserine|||Polar residues|||Pumilio 1|||Pumilio 2|||Pumilio 3|||Pumilio 4|||Pumilio 5|||Pumilio 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075927|||http://purl.uniprot.org/annotation/VAR_024600|||http://purl.uniprot.org/annotation/VAR_036456|||http://purl.uniprot.org/annotation/VAR_036457|||http://purl.uniprot.org/annotation/VAR_051612|||http://purl.uniprot.org/annotation/VSP_055693|||http://purl.uniprot.org/annotation/VSP_055694
http://togogenome.org/gene/9606:SLC38A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZM9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Solute carrier family 38 member 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311421|||http://purl.uniprot.org/annotation/VAR_037247|||http://purl.uniprot.org/annotation/VAR_080631|||http://purl.uniprot.org/annotation/VSP_029563
http://togogenome.org/gene/9606:MRPL36                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0J6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Large ribosomal subunit protein bL36m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030529
http://togogenome.org/gene/9606:C11orf24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PRU5|||http://purl.uniprot.org/uniprot/Q96F05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||Uncharacterized protein C11orf24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251887|||http://purl.uniprot.org/annotation/PRO_5003244193|||http://purl.uniprot.org/annotation/VAR_027713|||http://purl.uniprot.org/annotation/VAR_027714
http://togogenome.org/gene/9606:SRSF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXF0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Polar residues|||RRM|||Serine/arginine-rich splicing factor 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081960
http://togogenome.org/gene/9606:PSTK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IV42                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||L-seryl-tRNA(Sec) kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097080|||http://purl.uniprot.org/annotation/VAR_028156|||http://purl.uniprot.org/annotation/VSP_014989
http://togogenome.org/gene/9606:APEX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P27695|||http://purl.uniprot.org/uniprot/Q5TZP7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes AP endodeoxyribonuclease activity.|||Abolishes AP endodeoxyribonuclease activity. Lacks MYCCRDRNA cleavage activity.|||Abolishes partially the redox activity.|||Abolishes the AP endodeoxyribonuclease activity.|||Abolishes the AP endodeoxyribonuclease activity. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-65.|||Abolishes the redox activity. Does not abolish the AP endodeoxyribonuclease and phosphodiesterase activities. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-210.|||Alternate|||Basic and acidic residues|||Cleavage; by granzyme A|||DNA-(apurinic or apyrimidinic site) endonuclease|||DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial|||Decreases AP endodeoxyribonuclease activity.|||Disordered|||Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-310.|||Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-93.|||Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export.|||Does not abolish the redox activity.|||Endonuclease/exonuclease/phosphatase|||Enhances the interaction with TOMM20. Does not inhibit redox and AP endodeoyribonuclease activities. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-32. Reduces protection from granzyme A-mediated cell death; when associated with A-65 and A-210.|||Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-27.|||Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-25; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-25 and K-27.|||Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoyribonuclease activity; when associated with A-24; A-25; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-25.|||Important for catalytic activity|||Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-31.|||Interaction with DNA substrate|||Lack of acetylation and does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-6.|||Lack of acetylation, does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-7. Does not inhibit interaction with HDAC1, HDAC2 and HDAC3. Absence of increase in nCaRE binding activity.|||Lacks MYCCRDRNA cleavage activity.|||Mitochondrial targeting sequence (MTS)|||N6-acetyllysine|||N6-acetyllysine; by EP300|||Nearly abolishes AP endodeoxyribonuclease activity.|||Necessary for interaction with NPM1 and for efficient rRNA binding|||Necessary for interaction with YBX1, binding to RNA, NPM1-dependent association with rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoli|||Nuclear export signal (NES)|||Nuclear localization signal (NLS)|||Phosphoserine|||Phosphothreonine; by CDK5|||Proton acceptor|||Proton donor/acceptor|||Reduces AP endodeoxyribonuclease activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-283.|||Reduces nuclear localization; when associated with A-12.|||Reduces nuclear localization; when associated with A-13.|||Reduces the interaction with TOMM20.|||Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-299.|||Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-301.|||Removed|||S-nitrosocysteine|||S-nitrosocysteine; alternate|||Strongly reduces AP endodeoxyribonuclease activity, but does not affect RNA cleavage activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-308.|||Strongly reduces AP endodeoxyribonuclease activity.|||Transition state stabilizer ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200010|||http://purl.uniprot.org/annotation/PRO_0000402572|||http://purl.uniprot.org/annotation/VAR_013455|||http://purl.uniprot.org/annotation/VAR_014823|||http://purl.uniprot.org/annotation/VAR_019790
http://togogenome.org/gene/9606:ITIH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP62|||http://purl.uniprot.org/uniprot/C9J2H1|||http://purl.uniprot.org/uniprot/G5E9D8|||http://purl.uniprot.org/uniprot/Q86UX2|||http://purl.uniprot.org/uniprot/Q96JW9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inter-alpha-trypsin inhibitor heavy chain H5|||N-linked (GlcNAc...) asparagine|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331408|||http://purl.uniprot.org/annotation/PRO_5002997584|||http://purl.uniprot.org/annotation/PRO_5014092030|||http://purl.uniprot.org/annotation/VAR_042847|||http://purl.uniprot.org/annotation/VAR_042848|||http://purl.uniprot.org/annotation/VAR_042849|||http://purl.uniprot.org/annotation/VAR_042850|||http://purl.uniprot.org/annotation/VAR_055973|||http://purl.uniprot.org/annotation/VAR_055974|||http://purl.uniprot.org/annotation/VAR_061276|||http://purl.uniprot.org/annotation/VSP_033188|||http://purl.uniprot.org/annotation/VSP_033189|||http://purl.uniprot.org/annotation/VSP_033190|||http://purl.uniprot.org/annotation/VSP_033191|||http://purl.uniprot.org/annotation/VSP_035727|||http://purl.uniprot.org/annotation/VSP_035728|||http://purl.uniprot.org/annotation/VSP_035729|||http://purl.uniprot.org/annotation/VSP_035730
http://togogenome.org/gene/9606:EPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6I3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 3 AA repeats of N-P-F|||4|||5|||6|||7|||8|||8 X 3 AA repeats of [ED]-P-W|||Abolishes phosphorylation by CDK1 and reduces REPS2 binding.|||Abolishes phosphorylation by CDK1.|||Disordered|||ENTH|||Epsin-1|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine|||Pro residues|||Reduces interaction with AP2B1.|||UIM 1|||UIM 2|||UIM 3|||[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074513|||http://purl.uniprot.org/annotation/VSP_041010|||http://purl.uniprot.org/annotation/VSP_041011|||http://purl.uniprot.org/annotation/VSP_041012
http://togogenome.org/gene/9606:ZNF730                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMV8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; degenerate|||C2H2-type 9|||KRAB|||Putative zinc finger protein 730                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328986|||http://purl.uniprot.org/annotation/VAR_057449
http://togogenome.org/gene/9606:KLF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZAX4|||http://purl.uniprot.org/uniprot/O14901|||http://purl.uniprot.org/uniprot/Q53QU8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||High frequency in individuals with diabetes mellitus type 2; increased repression activity; increased binding to SIN3A; impairs activation of insulin promoter.|||In MODY7; absent in one family member with diabetes; increased repression activity; no alteration in binding affinity to SIN3A.|||In MODY7; increased repression activity; no alteration in binding affinity to SIN3A.|||In isoform 2.|||Krueppel-like factor 11|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047180|||http://purl.uniprot.org/annotation/VAR_031522|||http://purl.uniprot.org/annotation/VAR_031523|||http://purl.uniprot.org/annotation/VAR_031524|||http://purl.uniprot.org/annotation/VAR_052717|||http://purl.uniprot.org/annotation/VSP_042695
http://togogenome.org/gene/9606:STX10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60499|||http://purl.uniprot.org/uniprot/Q5U8S2|||http://purl.uniprot.org/uniprot/X6R2W0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Syntaxin-10|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210220|||http://purl.uniprot.org/annotation/VSP_006347
http://togogenome.org/gene/9606:FZR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM11                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Constitutively active; when associated with A-121; A-151 and A-163. Does not affect APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-121; A-151 and A-163. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-121 and A-151. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-121 and A-163.|||Constitutively active; when associated with A-40; A-121 and A-151. Does not affect APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-40; A-121 and A-151. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-40 and A-121. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-121 and A-151. Decreases ubiquitination; when associated with A-40 and A-151.|||Constitutively active; when associated with A-40; A-121 and A-163. Does not affect ubiquitination; when associated with A-40; A-121 and A-163. Decreases ubiquitination; when associated with A-40 and A-163. Decreases ubiquitination; when associated with A-121 and A-163.|||Constitutively active; when associated with A-40; A-151 and A-163. Does not affect APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-40; A-151 and A-163. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-40 and A-151. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-40 and A-163. Decreases APC/FZR1 E3 ubiquitin-protein ligase complex activity; when associated with A-151 and A-163.|||Disordered|||Fizzy-related protein homolog|||In DEE109; fails to rescue neurodevelopmental defects in a Drosophila model system; does not affect nuclear localization.|||In DEE109; loss-of-function variant affecting cell cycle regulation; unable to rescue aberrant cell cycle in FZR1-deficient mouse cortical cells; decreased protein levels in patient cells.|||In isoform 2 and isoform 3.|||In isoform 3.|||Inhibits APC/FZR1 E3 ubiquitin-protein ligase complex activity.|||Involved in APC/FZR1 E3 ubiquitin-protein ligase complex activity|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced interaction with CCNF.|||Reduced interaction with CCNF. Impaired degradation.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051001|||http://purl.uniprot.org/annotation/VAR_087872|||http://purl.uniprot.org/annotation/VAR_087873|||http://purl.uniprot.org/annotation/VAR_087874|||http://purl.uniprot.org/annotation/VSP_008503|||http://purl.uniprot.org/annotation/VSP_008504
http://togogenome.org/gene/9606:KRTAP10-11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60411|||http://purl.uniprot.org/uniprot/P60412                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||25 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-11|||Keratin-associated protein 10-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185217|||http://purl.uniprot.org/annotation/PRO_0000185219|||http://purl.uniprot.org/annotation/VAR_017739|||http://purl.uniprot.org/annotation/VAR_060052|||http://purl.uniprot.org/annotation/VAR_060056
http://togogenome.org/gene/9606:ABHD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5D6|||http://purl.uniprot.org/uniprot/Q8WTS1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1-acylglycerol-3-phosphate O-acyltransferase ABHD5|||AB hydrolase-1|||Found in a patient with CDS but without evidence it may cause the disease.|||HXXXXD motif|||In CDS.|||In CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080866|||http://purl.uniprot.org/annotation/VAR_023387|||http://purl.uniprot.org/annotation/VAR_023388|||http://purl.uniprot.org/annotation/VAR_023389|||http://purl.uniprot.org/annotation/VAR_037574|||http://purl.uniprot.org/annotation/VAR_057953|||http://purl.uniprot.org/annotation/VAR_057954
http://togogenome.org/gene/9606:RPL23A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62750                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Beta-like import receptor binding (BIB) domain|||Citrulline|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Large ribosomal subunit protein uL23|||N,N,N-trimethylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Rare variant found in Diamond-Blackfan anemia patients; unknown pathological significance.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129467|||http://purl.uniprot.org/annotation/VAR_069221
http://togogenome.org/gene/9606:OR4M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWC3|||http://purl.uniprot.org/uniprot/Q8NGD0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4M1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150561|||http://purl.uniprot.org/annotation/VAR_034206|||http://purl.uniprot.org/annotation/VAR_048031
http://togogenome.org/gene/9606:WDR46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8W1|||http://purl.uniprot.org/uniprot/A8K806|||http://purl.uniprot.org/uniprot/B4DP15|||http://purl.uniprot.org/uniprot/O15213                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  BING4 C-terminal|||Basic and acidic residues|||Disordered|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD repeat-containing protein 46                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051395|||http://purl.uniprot.org/annotation/VAR_022025|||http://purl.uniprot.org/annotation/VAR_053433|||http://purl.uniprot.org/annotation/VAR_053434
http://togogenome.org/gene/9606:OR2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWD0|||http://purl.uniprot.org/uniprot/Q9GZK3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In allele 6M1-10*02.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150460|||http://purl.uniprot.org/annotation/VAR_010943|||http://purl.uniprot.org/annotation/VAR_057536|||http://purl.uniprot.org/annotation/VAR_062014
http://togogenome.org/gene/9606:GABRR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MPY1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit rho-3|||Helical|||Interaction with SQSTM1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332189|||http://purl.uniprot.org/annotation/VAR_088019
http://togogenome.org/gene/9606:CLIC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96NY7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||13 X 10 AA tandem repeat of G-D-[SNG]-[VIM]-[DEQ]-A-[EAG]-[GDVE]-[PRG]-[LAVP]|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Chloride intracellular channel protein 6|||Disordered|||GST C-terminal|||Helical; Note=After insertion into the membrane|||In isoform A.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144217|||http://purl.uniprot.org/annotation/VAR_014139|||http://purl.uniprot.org/annotation/VSP_008963
http://togogenome.org/gene/9606:TPTE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XPS3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C2 tensin-type|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Loss of activity.|||Phosphatase tensin-type|||Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase TPTE2|||Phosphocysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000224187|||http://purl.uniprot.org/annotation/VAR_047501|||http://purl.uniprot.org/annotation/VAR_057349|||http://purl.uniprot.org/annotation/VSP_017322|||http://purl.uniprot.org/annotation/VSP_017323|||http://purl.uniprot.org/annotation/VSP_017324|||http://purl.uniprot.org/annotation/VSP_017325|||http://purl.uniprot.org/annotation/VSP_044506|||http://purl.uniprot.org/annotation/VSP_047569|||http://purl.uniprot.org/annotation/VSP_053978
http://togogenome.org/gene/9606:ADCY10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0K0K1J8|||http://purl.uniprot.org/uniprot/Q96PN6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adenylate cyclase type 10|||Guanylate cyclase|||Guanylate cyclase 1|||Guanylate cyclase 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nearly abolishes bicarbonate-mediated increase of enzyme activity. Abolishes bicarbonate-mediated increase of enzyme activity; when associated with A-176.|||Reduces bicarbonate-mediated increase of enzyme activity. Abolishes bicarbonate-mediated increase of enzyme activity; when associated with A-95.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317101|||http://purl.uniprot.org/annotation/VAR_038476|||http://purl.uniprot.org/annotation/VAR_038477|||http://purl.uniprot.org/annotation/VSP_030866|||http://purl.uniprot.org/annotation/VSP_030867|||http://purl.uniprot.org/annotation/VSP_030868|||http://purl.uniprot.org/annotation/VSP_030869|||http://purl.uniprot.org/annotation/VSP_030870|||http://purl.uniprot.org/annotation/VSP_046329
http://togogenome.org/gene/9606:CYP2C19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33261                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2C19|||In allele CYP2C19*10.|||In allele CYP2C19*11.|||In allele CYP2C19*13.|||In allele CYP2C19*14.|||In allele CYP2C19*15.|||In allele CYP2C19*16; lowered catalytic activity.|||In allele CYP2C19*18.|||In allele CYP2C19*19.|||In allele CYP2C19*1B, allele CYP2C19*1C, allele CYP2C19*2A, allele CYP2C19*2B, allele CYP2C19*2C, allele CYP2C19*2E, allele CYP2C19*2F, allele CYP2C19*2G, allele CYP2C19*2H, allele CYP2C19*2J, allele CYP2C19*3A, allele CYP2C19*3B, allele CYP2C19*3C, allele CYP2C19*4A, allele CYP2C19*4B, allele CYP2C19*6, allele CYP2C19*9, allele CYP2C19*10, allele CYP2C19*11, allele CYP2C19*12, allele CYP2C19*13, allele CYP2C19*14, allele CYP2C19*15, allele CYP2C19*18, allele CYP2C19*19, allele CYP2C19*22, allele CYP2C19*23, allele CYP2C19*24, allele CYP2C19*25, allele CYP2C19*26, allele CYP2C19*27, allele CYP2C19*28, allele CYP2C19*29, allele CYP2C19*31, allele CYP2C19*32, allele CYP2C19*33 and allele CYP2C19*35.|||In allele CYP2C19*5A and allele CYP2C19*5B; loss of activity.|||In allele CYP2C19*6; loss of activity.|||In allele CYP2C19*8; loss of activity.|||In allele CYP2C19*9.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051708|||http://purl.uniprot.org/annotation/VAR_001255|||http://purl.uniprot.org/annotation/VAR_008357|||http://purl.uniprot.org/annotation/VAR_008358|||http://purl.uniprot.org/annotation/VAR_008359|||http://purl.uniprot.org/annotation/VAR_020123|||http://purl.uniprot.org/annotation/VAR_021268|||http://purl.uniprot.org/annotation/VAR_021269|||http://purl.uniprot.org/annotation/VAR_021270|||http://purl.uniprot.org/annotation/VAR_021271|||http://purl.uniprot.org/annotation/VAR_021272|||http://purl.uniprot.org/annotation/VAR_021273|||http://purl.uniprot.org/annotation/VAR_021274|||http://purl.uniprot.org/annotation/VAR_021275|||http://purl.uniprot.org/annotation/VAR_024083|||http://purl.uniprot.org/annotation/VAR_024084|||http://purl.uniprot.org/annotation/VAR_024085|||http://purl.uniprot.org/annotation/VAR_024718|||http://purl.uniprot.org/annotation/VAR_024719
http://togogenome.org/gene/9606:ASGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07306|||http://purl.uniprot.org/uniprot/Q6FGQ5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Asialoglycoprotein receptor 1|||Basic and acidic residues|||C-type lectin|||Cytoplasmic|||Disordered|||Endocytosis signal|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform H1b.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046650|||http://purl.uniprot.org/annotation/VSP_044480
http://togogenome.org/gene/9606:SLC13A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68D44|||http://purl.uniprot.org/uniprot/Q86YT5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In DEE25; loss of function in citrate transport; loss of localization to plasma membrane.|||In DEE25; loss of function in citrate transport; no effect on localization to plasma membrane.|||In DEE25; loss of localization to plasma membrane; loss of function in citrate transport.|||In DEE25; no loss of localization to plasma membrane; loss of function in citrate transport.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of localization to plasma membrane; loss of function in citrate transport.|||N-linked (GlcNAc...) asparagine|||Na(+)/citrate cotransporter|||No effect on its function in citrate transport.|||No effect on localization to plasma membrane; no effect on its function in citrate transport.|||No effect on localization to plasma membrane; reduced function in citrate transport; increased Km and Vmax values compared with that of wild type with citrate as substrate.|||Significant loss of function in citrate transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260101|||http://purl.uniprot.org/annotation/VAR_078912|||http://purl.uniprot.org/annotation/VAR_078913|||http://purl.uniprot.org/annotation/VAR_078914|||http://purl.uniprot.org/annotation/VAR_078915|||http://purl.uniprot.org/annotation/VAR_078916|||http://purl.uniprot.org/annotation/VAR_078917|||http://purl.uniprot.org/annotation/VAR_078918|||http://purl.uniprot.org/annotation/VAR_084747|||http://purl.uniprot.org/annotation/VAR_084748|||http://purl.uniprot.org/annotation/VAR_084749|||http://purl.uniprot.org/annotation/VAR_084750|||http://purl.uniprot.org/annotation/VSP_043098|||http://purl.uniprot.org/annotation/VSP_054910|||http://purl.uniprot.org/annotation/VSP_055652
http://togogenome.org/gene/9606:ZNF747                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KWK6|||http://purl.uniprot.org/uniprot/B7ZAD9|||http://purl.uniprot.org/uniprot/Q9BV97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In isoform 1.|||In isoform 2.|||KRAB|||Zinc finger protein 747                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293691|||http://purl.uniprot.org/annotation/VSP_061285|||http://purl.uniprot.org/annotation/VSP_061286
http://togogenome.org/gene/9606:MYBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10244                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type 1|||HTH myb-type 2|||HTH myb-type 3|||In isoform 2.|||Myb-related protein B|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK2|||Phosphothreonine|||Phosphothreonine; by CDK2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197058|||http://purl.uniprot.org/annotation/VAR_020422|||http://purl.uniprot.org/annotation/VAR_050190|||http://purl.uniprot.org/annotation/VAR_050191|||http://purl.uniprot.org/annotation/VAR_050192|||http://purl.uniprot.org/annotation/VSP_053987
http://togogenome.org/gene/9606:HAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42357                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  2,3-didehydroalanine (Ser)|||5-imidazolinone (Ala-Gly)|||Histidine ammonia-lyase|||In HISTID.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161058|||http://purl.uniprot.org/annotation/VAR_006042|||http://purl.uniprot.org/annotation/VAR_022915|||http://purl.uniprot.org/annotation/VAR_022916|||http://purl.uniprot.org/annotation/VAR_022917|||http://purl.uniprot.org/annotation/VAR_022918|||http://purl.uniprot.org/annotation/VSP_044704|||http://purl.uniprot.org/annotation/VSP_046003
http://togogenome.org/gene/9606:UTS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95399                                                                                  ^@                                                                                  Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disulfide Bond|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Urotensin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036346|||http://purl.uniprot.org/annotation/PRO_0000036347|||http://purl.uniprot.org/annotation/VAR_029313|||http://purl.uniprot.org/annotation/VAR_053734|||http://purl.uniprot.org/annotation/VSP_013638
http://togogenome.org/gene/9606:DDTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHG4|||http://purl.uniprot.org/uniprot/B5MC82                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  D-dopachrome decarboxylase-like protein|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337242
http://togogenome.org/gene/9606:DDX18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N254|||http://purl.uniprot.org/uniprot/Q9NVP1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX18|||Basic and acidic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In a breast cancer sample; somatic mutation.|||Polar residues|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055001|||http://purl.uniprot.org/annotation/VAR_013293|||http://purl.uniprot.org/annotation/VAR_033857|||http://purl.uniprot.org/annotation/VAR_035841
http://togogenome.org/gene/9606:PDIA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30101|||http://purl.uniprot.org/uniprot/V9HVY3                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activity changed to serine protease.|||Activity changed to serine protease; when associated with S-409.|||Activity changed to serine protease; when associated with S-60.|||Basic and acidic residues|||Contributes to redox potential value|||Disordered|||Interchain (with C-115 in TAPBP); in linked form; reversible|||Lowers pKa of C-terminal Cys of first active site|||Lowers pKa of C-terminal Cys of second active site|||N6-acetyllysine|||N6-methyllysine|||N6-succinyllysine|||No effect on disulfide bond with TAPBP.|||No loss of activity. No loss of activity; when associated with A-406.|||No loss of activity. No loss of activity; when associated with A-57.|||Nucleophile|||Phosphothreonine|||Prevents secretion from ER|||Protein disulfide-isomerase|||Protein disulfide-isomerase A3|||Redox-active|||Redox-active; reversible|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2|||Trapped via disulfide bond with TAPBP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034225|||http://purl.uniprot.org/annotation/PRO_5014206131|||http://purl.uniprot.org/annotation/VAR_020027
http://togogenome.org/gene/9606:MED14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60244                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||Interaction with SREBF1|||Interaction with STAT2|||LXXLL motif 1|||LXXLL motif 2|||Mediator of RNA polymerase II transcription subunit 14|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079357|||http://purl.uniprot.org/annotation/VAR_036608
http://togogenome.org/gene/9606:TBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9ZGG0|||http://purl.uniprot.org/uniprot/O43435|||http://purl.uniprot.org/uniprot/Q152R5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In CTHM and VCFS.|||In DGS.|||In VCFS.|||In a colorectal cancer sample; somatic mutation.|||In isoform B.|||In isoform C.|||Polar residues|||Pro residues|||T-box|||T-box transcription factor TBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184423|||http://purl.uniprot.org/annotation/VAR_024657|||http://purl.uniprot.org/annotation/VAR_034545|||http://purl.uniprot.org/annotation/VAR_035025|||http://purl.uniprot.org/annotation/VAR_035026|||http://purl.uniprot.org/annotation/VAR_036065|||http://purl.uniprot.org/annotation/VSP_006383|||http://purl.uniprot.org/annotation/VSP_007423
http://togogenome.org/gene/9606:SPAG11B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRG4|||http://purl.uniprot.org/uniprot/Q08648|||http://purl.uniprot.org/uniprot/Q6PDA7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform EP2B.|||In isoform EP2C.|||In isoform EP2D.|||In isoform EP2E.|||N-linked (GlcNAc...) asparagine|||Sperm-associated antigen 11A|||Sperm-associated antigen 11B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033185|||http://purl.uniprot.org/annotation/PRO_0000314165|||http://purl.uniprot.org/annotation/PRO_5001974179|||http://purl.uniprot.org/annotation/VAR_005269|||http://purl.uniprot.org/annotation/VAR_053683|||http://purl.uniprot.org/annotation/VAR_082918|||http://purl.uniprot.org/annotation/VSP_006208|||http://purl.uniprot.org/annotation/VSP_006209|||http://purl.uniprot.org/annotation/VSP_006210|||http://purl.uniprot.org/annotation/VSP_030220|||http://purl.uniprot.org/annotation/VSP_030221|||http://purl.uniprot.org/annotation/VSP_030222|||http://purl.uniprot.org/annotation/VSP_030223|||http://purl.uniprot.org/annotation/VSP_044926|||http://purl.uniprot.org/annotation/VSP_044927
http://togogenome.org/gene/9606:CDH20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2C5|||http://purl.uniprot.org/uniprot/Q8N9J3|||http://purl.uniprot.org/uniprot/Q9HBT6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-20|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003819|||http://purl.uniprot.org/annotation/PRO_0000003820|||http://purl.uniprot.org/annotation/PRO_5002722120|||http://purl.uniprot.org/annotation/VAR_036103|||http://purl.uniprot.org/annotation/VAR_036104|||http://purl.uniprot.org/annotation/VAR_036105|||http://purl.uniprot.org/annotation/VAR_039119|||http://purl.uniprot.org/annotation/VAR_039120|||http://purl.uniprot.org/annotation/VAR_039121
http://togogenome.org/gene/9606:UQCRB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14927                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cytochrome b-c1 complex subunit 7|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193524|||http://purl.uniprot.org/annotation/VAR_052443|||http://purl.uniprot.org/annotation/VSP_045601
http://togogenome.org/gene/9606:NUTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61970                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Strand                                                                                  ^@                                                                                  N6-acetyllysine|||NTF2|||No effect on localization to the nucleoplasm.|||Nuclear transport factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194775
http://togogenome.org/gene/9606:CADM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3XHN4|||http://purl.uniprot.org/uniprot/Q8N3J6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell adhesion molecule 2|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||In isoform 5 and isoform 6.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291970|||http://purl.uniprot.org/annotation/PRO_5003460192|||http://purl.uniprot.org/annotation/VSP_026333|||http://purl.uniprot.org/annotation/VSP_026334|||http://purl.uniprot.org/annotation/VSP_026335|||http://purl.uniprot.org/annotation/VSP_055355|||http://purl.uniprot.org/annotation/VSP_055356
http://togogenome.org/gene/9606:GM2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17900                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Ganglioside GM2 activator|||Ganglioside GM2 activator isoform short|||In GM2GAB.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031639|||http://purl.uniprot.org/annotation/PRO_0000031640|||http://purl.uniprot.org/annotation/PRO_0000031641|||http://purl.uniprot.org/annotation/VAR_006947|||http://purl.uniprot.org/annotation/VAR_011697|||http://purl.uniprot.org/annotation/VAR_011698|||http://purl.uniprot.org/annotation/VAR_013830|||http://purl.uniprot.org/annotation/VAR_036892|||http://purl.uniprot.org/annotation/VAR_036893
http://togogenome.org/gene/9606:RNF223                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ERA6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||RING finger protein 223|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410919
http://togogenome.org/gene/9606:TRAF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUZ4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Complete loss of E3 ligase activity.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||MATH|||Phosphoserine|||RING-type|||TNF receptor-associated factor 4|||TRAF-type 1|||TRAF-type 2|||TRAF-type 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056403|||http://purl.uniprot.org/annotation/VAR_025805|||http://purl.uniprot.org/annotation/VAR_052150|||http://purl.uniprot.org/annotation/VSP_007403
http://togogenome.org/gene/9606:C1GALT1C1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DN25                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C1GALT1-specific chaperone 1-like protein|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000433923
http://togogenome.org/gene/9606:MIXL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2W2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein MIXL1|||In isoform 2.|||Phosphotyrosine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311333|||http://purl.uniprot.org/annotation/VSP_054305
http://togogenome.org/gene/9606:SH3BP5L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8J4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||SH3 domain-binding protein 5-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317508|||http://purl.uniprot.org/annotation/VSP_056075
http://togogenome.org/gene/9606:MYEOV                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K256|||http://purl.uniprot.org/uniprot/F5H0B3|||http://purl.uniprot.org/uniprot/Q96EZ4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Myeloma-overexpressed gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096668|||http://purl.uniprot.org/annotation/VAR_016603|||http://purl.uniprot.org/annotation/VAR_056948|||http://purl.uniprot.org/annotation/VAR_056949|||http://purl.uniprot.org/annotation/VAR_056950
http://togogenome.org/gene/9606:CHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TR54|||http://purl.uniprot.org/uniprot/B3KWV4|||http://purl.uniprot.org/uniprot/Q12873|||http://purl.uniprot.org/uniprot/Q2TAZ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes sumoylation by ZBED1/hDREF and increases binding to chromatin.|||Acidic residues|||Basic and acidic residues|||Basic residues|||CHD subfamily II SANT-like|||Chromo|||Chromo 1|||Chromo 2|||Chromodomain-helicase-DNA-binding protein 3|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Helicase ATP-binding|||Helicase C-terminal|||In SNIBCPS.|||In SNIBCPS; decreased function in chromatin remodeling; decreased ATPase activity.|||In SNIBCPS; highly decreased function in chromatin remodeling.|||In SNIBCPS; increased function in chromatin remodeling.|||In SNIBCPS; the patient also carries a truncating variant in CIC; both variants may contribute to disease phenotype.|||In SNIBCPS; unknown pathological significance.|||In SNIBCPS; unknown pathological significance; does not affect function in chromatin remodeling; no effect on ATPase activity.|||In isoform 2.|||In isoform 3.|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with PCNT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080227|||http://purl.uniprot.org/annotation/VAR_048728|||http://purl.uniprot.org/annotation/VAR_081506|||http://purl.uniprot.org/annotation/VAR_081507|||http://purl.uniprot.org/annotation/VAR_081508|||http://purl.uniprot.org/annotation/VAR_081509|||http://purl.uniprot.org/annotation/VAR_081510|||http://purl.uniprot.org/annotation/VAR_081511|||http://purl.uniprot.org/annotation/VAR_081512|||http://purl.uniprot.org/annotation/VAR_081513|||http://purl.uniprot.org/annotation/VAR_081514|||http://purl.uniprot.org/annotation/VAR_081515|||http://purl.uniprot.org/annotation/VAR_081516|||http://purl.uniprot.org/annotation/VAR_081517|||http://purl.uniprot.org/annotation/VAR_081518|||http://purl.uniprot.org/annotation/VAR_081519|||http://purl.uniprot.org/annotation/VAR_081520|||http://purl.uniprot.org/annotation/VAR_081521|||http://purl.uniprot.org/annotation/VAR_081522|||http://purl.uniprot.org/annotation/VAR_081523|||http://purl.uniprot.org/annotation/VAR_081524|||http://purl.uniprot.org/annotation/VAR_081525|||http://purl.uniprot.org/annotation/VAR_081526|||http://purl.uniprot.org/annotation/VSP_017231|||http://purl.uniprot.org/annotation/VSP_047097
http://togogenome.org/gene/9606:HOXB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09067                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200128
http://togogenome.org/gene/9606:MAB21L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R805|||http://purl.uniprot.org/uniprot/F1T0A2|||http://purl.uniprot.org/uniprot/Q13394                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased protein stability.|||In COFG.|||In COFG; unknown pathological significance.|||Mab-21-like HhH/H2TH-like|||Mab-21-like nucleotidyltransferase|||Putative nucleotidyltransferase MAB21L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312781|||http://purl.uniprot.org/annotation/VAR_037568|||http://purl.uniprot.org/annotation/VAR_082959|||http://purl.uniprot.org/annotation/VAR_082960
http://togogenome.org/gene/9606:SULT1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49888|||http://purl.uniprot.org/uniprot/Q53X91                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of sulfonation activity towards all substrates tested.|||Decreased gradually the sulfotransferase activity.|||Does not have decreased sulfonation activity towards the estrogens and DHEA.|||Does not prevent the formation of homodimer.|||Proton acceptor|||Substrate specificity constants for estradiol and estrone are reduced. Dramatic 400-fold increase in the ability to sulfonate dopamine.|||Sulfotransferase|||Sulfotransferase 1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085153|||http://purl.uniprot.org/annotation/VAR_018907
http://togogenome.org/gene/9606:RAB33A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14088                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Ras-related protein Rab-33A|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121237|||http://purl.uniprot.org/annotation/VAR_006849
http://togogenome.org/gene/9606:APOL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQE5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Apolipoprotein L2|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137601|||http://purl.uniprot.org/annotation/VAR_012978|||http://purl.uniprot.org/annotation/VAR_024366
http://togogenome.org/gene/9606:DNPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43598                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2'-deoxynucleoside 5'-phosphate N-hydrolase 1|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097200|||http://purl.uniprot.org/annotation/VSP_040509|||http://purl.uniprot.org/annotation/VSP_040510
http://togogenome.org/gene/9606:ZEB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RBI8|||http://purl.uniprot.org/uniprot/B4DGU2|||http://purl.uniprot.org/uniprot/P37275                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; atypical|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; atypical|||Disordered|||Found in a patient with FECD6.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Homeobox; atypical|||In FECD6.|||In FECD6; down-regulation of several collagen genes expression.|||In FECD6; no effect on protein expression; no effect on nuclear localization.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger E-box-binding homeobox 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047231|||http://purl.uniprot.org/annotation/VAR_031824|||http://purl.uniprot.org/annotation/VAR_052731|||http://purl.uniprot.org/annotation/VAR_063759|||http://purl.uniprot.org/annotation/VAR_063760|||http://purl.uniprot.org/annotation/VAR_063761|||http://purl.uniprot.org/annotation/VAR_063762|||http://purl.uniprot.org/annotation/VAR_063763|||http://purl.uniprot.org/annotation/VAR_072897|||http://purl.uniprot.org/annotation/VAR_072898|||http://purl.uniprot.org/annotation/VAR_072899|||http://purl.uniprot.org/annotation/VAR_072900|||http://purl.uniprot.org/annotation/VSP_045184|||http://purl.uniprot.org/annotation/VSP_047279|||http://purl.uniprot.org/annotation/VSP_047280|||http://purl.uniprot.org/annotation/VSP_047281
http://togogenome.org/gene/9606:FCRL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RD9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fc receptor-like protein 5|||Helical|||ITIM motif 1|||ITIM motif 2|||ITIM motif 3|||ITIM motif 4|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||Ig-like C2-type 7|||Ig-like C2-type 8|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225622|||http://purl.uniprot.org/annotation/VAR_025447|||http://purl.uniprot.org/annotation/VAR_025448|||http://purl.uniprot.org/annotation/VAR_025449|||http://purl.uniprot.org/annotation/VAR_025450|||http://purl.uniprot.org/annotation/VAR_035514|||http://purl.uniprot.org/annotation/VAR_056044|||http://purl.uniprot.org/annotation/VAR_056045|||http://purl.uniprot.org/annotation/VSP_017379|||http://purl.uniprot.org/annotation/VSP_017380|||http://purl.uniprot.org/annotation/VSP_017381|||http://purl.uniprot.org/annotation/VSP_017382|||http://purl.uniprot.org/annotation/VSP_017383|||http://purl.uniprot.org/annotation/VSP_017384|||http://purl.uniprot.org/annotation/VSP_017385|||http://purl.uniprot.org/annotation/VSP_017386
http://togogenome.org/gene/9606:BROX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z953|||http://purl.uniprot.org/uniprot/F5GXQ0|||http://purl.uniprot.org/uniprot/Q5VW32                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BRO1|||BRO1 domain-containing protein BROX|||Basic and acidic residues|||Cysteine methyl ester|||Disordered|||Does not affect SYN2 interaction. Does not induce SYN2 ubiquitination. Does not affect recruitment to sites of rupture. Impairs NE repair.|||In isoform 2.|||Loss of SYN2 interaction. Abolishes BROX recruitment to sites of nuclear envelope (NE) rupture. Impairs NE resealing. Does not induce SYN2 ubiquitination.|||Loss of association with the nuclear envelop. Abolishes its recruitment to rupture sites. Abolishes its repair function.|||N6-acetyllysine|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304612|||http://purl.uniprot.org/annotation/PRO_0000396736|||http://purl.uniprot.org/annotation/VSP_055551
http://togogenome.org/gene/9606:KRT76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01546                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In a breast cancer sample; somatic mutation.|||Keratin, type II cytoskeletal 2 oral|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063714|||http://purl.uniprot.org/annotation/VAR_028425|||http://purl.uniprot.org/annotation/VAR_028426|||http://purl.uniprot.org/annotation/VAR_028427|||http://purl.uniprot.org/annotation/VAR_036368
http://togogenome.org/gene/9606:OR51V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2C8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51V1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150764|||http://purl.uniprot.org/annotation/VAR_057580|||http://purl.uniprot.org/annotation/VAR_079498
http://togogenome.org/gene/9606:KIF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K932|||http://purl.uniprot.org/uniprot/Q9HAQ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF9|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125442|||http://purl.uniprot.org/annotation/VAR_020443|||http://purl.uniprot.org/annotation/VAR_022139|||http://purl.uniprot.org/annotation/VAR_024513|||http://purl.uniprot.org/annotation/VSP_002868
http://togogenome.org/gene/9606:ADAMTS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5IR90|||http://purl.uniprot.org/uniprot/Q9UKP5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 6|||Disintegrin|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||PLAC|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029174|||http://purl.uniprot.org/annotation/PRO_0000029175|||http://purl.uniprot.org/annotation/VSP_037093|||http://purl.uniprot.org/annotation/VSP_037094|||http://purl.uniprot.org/annotation/VSP_037095|||http://purl.uniprot.org/annotation/VSP_037096|||http://purl.uniprot.org/annotation/VSP_037097|||http://purl.uniprot.org/annotation/VSP_037098|||http://purl.uniprot.org/annotation/VSP_037099
http://togogenome.org/gene/9606:FAM210A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ND0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  DUF1279|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||Protein FAM210A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274424|||http://purl.uniprot.org/annotation/VAR_035686|||http://purl.uniprot.org/annotation/VAR_035687|||http://purl.uniprot.org/annotation/VAR_056844|||http://purl.uniprot.org/annotation/VAR_060439
http://togogenome.org/gene/9606:MOB1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8S9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||MOB kinase activator 1A|||N-acetylserine|||Phosphothreonine|||Phosphothreonine; by STK3/MST2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193566|||http://purl.uniprot.org/annotation/VSP_012295|||http://purl.uniprot.org/annotation/VSP_012296
http://togogenome.org/gene/9606:HOXA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31271|||http://purl.uniprot.org/uniprot/Q6DI00                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Homeobox|||Homeobox protein Hox-A13|||In GUTTS.|||In HFG.|||In HFG; severe phenotype overlapping with Guttmacher syndrome.|||In HFG; severe.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200101|||http://purl.uniprot.org/annotation/VAR_017773|||http://purl.uniprot.org/annotation/VAR_017774|||http://purl.uniprot.org/annotation/VAR_017775|||http://purl.uniprot.org/annotation/VAR_017776|||http://purl.uniprot.org/annotation/VAR_075341|||http://purl.uniprot.org/annotation/VAR_075342
http://togogenome.org/gene/9606:SAE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBE0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ATP-dependent activation of SUMO proteins.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processed|||N6-acetyllysine|||Phosphoserine|||Removed; alternate|||SUMO-activating enzyme subunit 1|||SUMO-activating enzyme subunit 1, N-terminally processed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194966|||http://purl.uniprot.org/annotation/PRO_0000423290|||http://purl.uniprot.org/annotation/VSP_045372|||http://purl.uniprot.org/annotation/VSP_045373|||http://purl.uniprot.org/annotation/VSP_045374|||http://purl.uniprot.org/annotation/VSP_045375
http://togogenome.org/gene/9606:PGM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15124                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoglucomutase-like protein 5|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147787|||http://purl.uniprot.org/annotation/VSP_030014|||http://purl.uniprot.org/annotation/VSP_030015
http://togogenome.org/gene/9606:PITPNA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00169|||http://purl.uniprot.org/uniprot/V9HWC5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity.|||Disordered|||N6-acetyllysine|||No effect on phosphatidylinositol transfer activity.|||No effect on phosphatidylinositol transfer activity. Resistant to inhibition by N-ethylmaleimide.|||Phosphatidylinositol transfer protein alpha isoform|||Reduced phosphatidylinositol and phosphatidylcholine transfer activity.|||Reduced phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity.|||Removed|||Significant loss of phosphatidylinositol and phosphatidylcholine transfer activity.|||Significant loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191639
http://togogenome.org/gene/9606:DEFA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12838                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Mutagenesis Site|||Peptide|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Decreased antibacterial activity against E.coli and S.aureus. Weakens interaction with B.anthracis lef and with HIV-1 gp120.|||Decreased antibacterial activity against E.coli. Weakens interaction with B.anthracis lef and with HIV-1 gp120.|||Decreased antibacterial activity against S.aureus.|||Defensin alpha 4|||Impaired homodimerization. Decreased antibacterial activity against S.aureus. Disrupts interaction with B.anthracis lef and with HIV-1 gp120.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-82 and Ala-92.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-82 and Ala-93.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-92 and Ala-93.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-82, Ala-92 and Ala-93.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-72, Ala-82, Ala-92 and Ala-93.|||Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-67, Ala-72, Ala-82, Ala-92 and Ala-93.|||In a colorectal cancer sample; somatic mutation.|||Slight decrease in antibacterial activity against E.coli and S.aureus.|||Slight decrease in antibacterial activity against E.coli.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006781|||http://purl.uniprot.org/annotation/PRO_0000006782|||http://purl.uniprot.org/annotation/PRO_0000006783|||http://purl.uniprot.org/annotation/VAR_036315|||http://purl.uniprot.org/annotation/VAR_048861|||http://purl.uniprot.org/annotation/VAR_061132
http://togogenome.org/gene/9606:B4GALT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15291                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1,4-galactosyltransferase 1|||Cleavage; to produce soluble form|||Cytoplasmic|||Disordered|||Favors the closed conformation of the enzyme.|||Helical; Signal-anchor for type II membrane protein|||In isoform Short.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No change in enzymatic activity.|||Processed beta-1,4-galactosyltransferase 1|||Reduction in N-acetylglucosamine and UDP-galactose binding.|||Reduction in N-acetylglucosamine binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012278|||http://purl.uniprot.org/annotation/PRO_0000296229|||http://purl.uniprot.org/annotation/VAR_054019|||http://purl.uniprot.org/annotation/VAR_054020|||http://purl.uniprot.org/annotation/VSP_018802
http://togogenome.org/gene/9606:MEIS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPD8|||http://purl.uniprot.org/uniprot/B7Z6F6|||http://purl.uniprot.org/uniprot/O14770                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Meis2|||Homeobox; TALE-type|||Impairs DNA binding and PBX1-dependent transcriptional activation. No effect on interaction with PBX1.|||Impairs interaction with PBX1.|||Impairs interaction with PBX1; when associated with 158-A-A-159.|||Impairs interaction with PBX1; when associated with A-151.|||Impairs interaction with PBX1; when associated with A-154.|||Impairs interaction with PBX1; when associated with A-161.|||Impairs interaction with PBX1; when associated with A-85. HELIX 285 297.|||Impairs interaction with PBX1; when associated with A-88.|||In CPCMR.|||In isoform 2, isoform 3, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 4, isoform 6 and isoform 7.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 8.|||Interaction with DNA|||MEIS N-terminal|||Polar residues|||Required for interaction with PBX1|||Transcriptional activation domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049108|||http://purl.uniprot.org/annotation/VAR_078978|||http://purl.uniprot.org/annotation/VAR_078979|||http://purl.uniprot.org/annotation/VSP_002242|||http://purl.uniprot.org/annotation/VSP_002243|||http://purl.uniprot.org/annotation/VSP_002244|||http://purl.uniprot.org/annotation/VSP_002245|||http://purl.uniprot.org/annotation/VSP_002246|||http://purl.uniprot.org/annotation/VSP_043219|||http://purl.uniprot.org/annotation/VSP_043494
http://togogenome.org/gene/9606:GRIK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z256|||http://purl.uniprot.org/uniprot/B7Z3V7|||http://purl.uniprot.org/uniprot/E7ENK3|||http://purl.uniprot.org/uniprot/E7EPY9|||http://purl.uniprot.org/uniprot/E9PD61|||http://purl.uniprot.org/uniprot/P39086                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glutamate receptor ionotropic, kainate 1|||Helical|||In RNA edited version.|||In isoform 2.|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC|||Phosphothreonine; by PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011541|||http://purl.uniprot.org/annotation/VAR_000304|||http://purl.uniprot.org/annotation/VAR_012041|||http://purl.uniprot.org/annotation/VAR_012042|||http://purl.uniprot.org/annotation/VAR_012043|||http://purl.uniprot.org/annotation/VAR_012751|||http://purl.uniprot.org/annotation/VAR_012752|||http://purl.uniprot.org/annotation/VSP_000127|||http://purl.uniprot.org/annotation/VSP_000128
http://togogenome.org/gene/9606:SMIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RUZ4|||http://purl.uniprot.org/uniprot/M4WDD3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Displays the Vel antigen|||Extracellular|||Found in Vel-negative population; unknown pathological significance; heterozygous with the 17-nucleotide frameshift deletion.|||Helical|||Helical; Signal-anchor for type II membrane protein|||Loss of cell-surface expression of the Vel antigen.|||N-acetylmethionine|||No effect on cell membrane localization; when associated with A-17; A-22 and A-27. No effect on cell surface expression of the Vel antigen; when associated with A-17; A-22 and A-27.|||No effect on cell membrane localization; when associated with A-6; A-17 and A-22. No effect on cell surface expression of the Vel antigen; when associated with A-6; A-17 and A-22.|||No effect on cell membrane localization; when associated with A-6; A-17 and A-27. No effect on cell surface expression of the Vel antigen; when associated with A-6; A-17 and A-27.|||No effect on cell membrane localization; when associated with A-6; A-22 and A-27. No effect on cell surface expression of the Vel antigen; when associated with A-6; A-22 and A-27.|||No effect on cell surface expression of the Vel antigen; when associated with S-35.|||No effect on cell surface expression of the Vel antigen; when associated with S-43.|||Phosphoserine|||Small integral membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000356182|||http://purl.uniprot.org/annotation/VAR_069360|||http://purl.uniprot.org/annotation/VAR_069361
http://togogenome.org/gene/9606:TTI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RIH5|||http://purl.uniprot.org/uniprot/Q6NXR4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In MRT39; impaired TTT complex formation.|||TELO2-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279414|||http://purl.uniprot.org/annotation/VAR_030886|||http://purl.uniprot.org/annotation/VAR_030887|||http://purl.uniprot.org/annotation/VAR_070671
http://togogenome.org/gene/9606:CGB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0F7RQP8|||http://purl.uniprot.org/uniprot/P0DN86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Choriogonadotropin subunit beta 3|||Disordered|||Glycoprotein hormone subunit beta|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||Pro residues|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000042|||http://purl.uniprot.org/annotation/CAR_000043|||http://purl.uniprot.org/annotation/PRO_0000011676|||http://purl.uniprot.org/annotation/PRO_5014227020|||http://purl.uniprot.org/annotation/VAR_003188|||http://purl.uniprot.org/annotation/VAR_014585|||http://purl.uniprot.org/annotation/VAR_014586|||http://purl.uniprot.org/annotation/VAR_014587|||http://purl.uniprot.org/annotation/VAR_015231|||http://purl.uniprot.org/annotation/VAR_015232|||http://purl.uniprot.org/annotation/VAR_015233|||http://purl.uniprot.org/annotation/VAR_015234|||http://purl.uniprot.org/annotation/VAR_015235|||http://purl.uniprot.org/annotation/VSP_038396
http://togogenome.org/gene/9606:CFHR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02985                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Complement factor H-related protein 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005898|||http://purl.uniprot.org/annotation/VAR_048817|||http://purl.uniprot.org/annotation/VSP_043041
http://togogenome.org/gene/9606:TMED9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVK6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||GOLD|||Helical|||Localization to plasma membrane and endocytosis.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Required for interaction with STX17|||Transmembrane emp24 domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010396|||http://purl.uniprot.org/annotation/VAR_061178
http://togogenome.org/gene/9606:SUSD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK55|||http://purl.uniprot.org/uniprot/B3KTY0|||http://purl.uniprot.org/uniprot/Q5VX71                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4|||Sushi domain-containing protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251975|||http://purl.uniprot.org/annotation/VSP_020838|||http://purl.uniprot.org/annotation/VSP_020839|||http://purl.uniprot.org/annotation/VSP_020840|||http://purl.uniprot.org/annotation/VSP_020841|||http://purl.uniprot.org/annotation/VSP_020842|||http://purl.uniprot.org/annotation/VSP_020843
http://togogenome.org/gene/9606:NDUFS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75251|||http://purl.uniprot.org/uniprot/Q6ZS38|||http://purl.uniprot.org/uniprot/Q7LD69                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a patient with Leigh syndrome; unknown pathological significance; decrease in enzyme activity.|||Hydroxyarginine|||In MC1DN3.|||In isoform 2.|||Mitochondrion|||NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial|||NADH:ubiquinone oxidoreductase-like 20kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020027|||http://purl.uniprot.org/annotation/VAR_008848|||http://purl.uniprot.org/annotation/VAR_014482|||http://purl.uniprot.org/annotation/VAR_084360|||http://purl.uniprot.org/annotation/VSP_057067
http://togogenome.org/gene/9606:DDN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94850                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Dendrin|||Disordered|||Interaction with ACTN1|||Interaction with CD2AP and NPHS1|||Interaction with MAGI2|||Nuclear localization|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079861|||http://purl.uniprot.org/annotation/VAR_059651
http://togogenome.org/gene/9606:IGFL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWQ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Insulin growth factor-like family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045061|||http://purl.uniprot.org/annotation/VSP_016606
http://togogenome.org/gene/9606:SERP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6R1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||Lumenal|||Stress-associated endoplasmic reticulum protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274799
http://togogenome.org/gene/9606:HYAL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3T9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Hyaluronidase-4|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000301999|||http://purl.uniprot.org/annotation/VAR_034936
http://togogenome.org/gene/9606:LAGE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14657                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EKC/KEOPS complex subunit LAGE3|||In GAMOS2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218924|||http://purl.uniprot.org/annotation/VAR_080374|||http://purl.uniprot.org/annotation/VAR_080375
http://togogenome.org/gene/9606:HLA-G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17693|||http://purl.uniprot.org/uniprot/Q31611|||http://purl.uniprot.org/uniprot/Q6DU14                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to COPB1 and Golgi-to-ER retrograde transport.|||Abolishes homodimerization and homotrimerization. Decreases functional interaction with LILRB1. Does not affect homodimerization of isoform 2 and its binding to LILRB2.|||Abolishes homodimerization. Decreases functional interaction with LILRB1.|||Alpha-1|||Alpha-2|||Alpha-3|||Connecting peptide|||Cytoplasmic|||Decreases TAPBP-dependent transport to the cell surface.|||ER-retrieval signal|||Enables TAPBP-independent transport to the cell surface.|||Extracellular|||HLA class I histocompatibility antigen, alpha chain G|||Helical|||Ig-like|||Ig-like C1-type|||In isoform 2 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||In isoform 7.|||Interchain|||N-linked (GlcNAc...) asparagine|||Soluble HLA class I histocompatibility antigen, alpha chain G|||VL9 epitope                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018886|||http://purl.uniprot.org/annotation/PRO_0000445908|||http://purl.uniprot.org/annotation/PRO_5014586278|||http://purl.uniprot.org/annotation/PRO_5014587280|||http://purl.uniprot.org/annotation/VSP_059191|||http://purl.uniprot.org/annotation/VSP_059192|||http://purl.uniprot.org/annotation/VSP_059193|||http://purl.uniprot.org/annotation/VSP_059194|||http://purl.uniprot.org/annotation/VSP_059195|||http://purl.uniprot.org/annotation/VSP_059196|||http://purl.uniprot.org/annotation/VSP_059197|||http://purl.uniprot.org/annotation/VSP_061749
http://togogenome.org/gene/9606:ADAMTS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB33|||http://purl.uniprot.org/uniprot/Q9UHI8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 1|||Cysteine switch|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Polar residues|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029150|||http://purl.uniprot.org/annotation/PRO_0000029151|||http://purl.uniprot.org/annotation/PRO_5002781853|||http://purl.uniprot.org/annotation/VAR_030001
http://togogenome.org/gene/9606:HIVEP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1R4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||6 X 4 AA tandem repeats of S-P-X-[RK]|||Acidic 1|||Acidic 2|||Acidic 3|||Acidic residues|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||CCHC HIVEP-type|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUN|||Nuclear localization signal|||Polar residues|||Pro residues|||Transcription factor HIVEP3|||ZAS1|||ZAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331627|||http://purl.uniprot.org/annotation/VAR_042910|||http://purl.uniprot.org/annotation/VAR_042911|||http://purl.uniprot.org/annotation/VAR_042912|||http://purl.uniprot.org/annotation/VAR_042913|||http://purl.uniprot.org/annotation/VAR_042914|||http://purl.uniprot.org/annotation/VAR_042915|||http://purl.uniprot.org/annotation/VAR_042916|||http://purl.uniprot.org/annotation/VAR_042917|||http://purl.uniprot.org/annotation/VAR_087891|||http://purl.uniprot.org/annotation/VSP_033279
http://togogenome.org/gene/9606:RNF185                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GF1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity and ability to regulate the cGAS-STING pathway; when associated with A-39.|||Abolished E3 ubiquitin-protein ligase activity and ability to regulate the cGAS-STING pathway; when associated with A-79.|||Cytoplasmic|||Decreased ubiquitin ligase activity.|||Disordered|||E3 ubiquitin-protein ligase RNF185|||Helical|||In isoform 2.|||Mitochondrial intermembrane|||RING-type|||Required for ubiquitin ligase activity and protection against ER stress-induced cell death                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247520|||http://purl.uniprot.org/annotation/VSP_020004
http://togogenome.org/gene/9606:LARP1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISF0|||http://purl.uniprot.org/uniprot/A0A3B3IT29|||http://purl.uniprot.org/uniprot/A0A994J4X5|||http://purl.uniprot.org/uniprot/G3V0E9|||http://purl.uniprot.org/uniprot/Q659C4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6 and isoform 7.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||La-related protein 1B|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299411|||http://purl.uniprot.org/annotation/VAR_034813|||http://purl.uniprot.org/annotation/VAR_034814|||http://purl.uniprot.org/annotation/VSP_027638|||http://purl.uniprot.org/annotation/VSP_027639|||http://purl.uniprot.org/annotation/VSP_027640|||http://purl.uniprot.org/annotation/VSP_027641|||http://purl.uniprot.org/annotation/VSP_027642|||http://purl.uniprot.org/annotation/VSP_027643|||http://purl.uniprot.org/annotation/VSP_027644|||http://purl.uniprot.org/annotation/VSP_027645|||http://purl.uniprot.org/annotation/VSP_027646|||http://purl.uniprot.org/annotation/VSP_027647|||http://purl.uniprot.org/annotation/VSP_027648|||http://purl.uniprot.org/annotation/VSP_027649|||http://purl.uniprot.org/annotation/VSP_027650|||http://purl.uniprot.org/annotation/VSP_027651|||http://purl.uniprot.org/annotation/VSP_027652|||http://purl.uniprot.org/annotation/VSP_027653
http://togogenome.org/gene/9606:FHIP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DH4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHF complex subunit HOOK-interacting protein 1A|||Found in siblings with familial natural-killer/T-cell lymphoma; unknown pathological significance.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319578|||http://purl.uniprot.org/annotation/VAR_084431
http://togogenome.org/gene/9606:PRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02812                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||15 X 20 AA approximate tandem repeats of P-P-G-K-P-Q-G-P-P-P-Q-G-[GD]-[NKS]-[KSQ]-[PRS]-[QRS] [GPS]-[PSAR]-[PSR]|||2|||3|||4|||5|||6|||7|||8|||9|||Basic proline-rich peptide IB-1|||Basic proline-rich peptide IB-4|||Basic proline-rich peptide IB-7|||Basic proline-rich peptide IB-8c|||Basic proline-rich peptide P-E|||Basic salivary proline-rich protein 2|||Disordered|||N-linked (GlcNAc...) asparagine|||O-linked (Hex) serine|||Phosphoserine|||Pro residues|||Pyrrolidone carboxylic acid                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022095|||http://purl.uniprot.org/annotation/PRO_0000022096|||http://purl.uniprot.org/annotation/PRO_0000097038|||http://purl.uniprot.org/annotation/PRO_0000372439|||http://purl.uniprot.org/annotation/PRO_0000372440|||http://purl.uniprot.org/annotation/PRO_0000395485|||http://purl.uniprot.org/annotation/VAR_019695|||http://purl.uniprot.org/annotation/VAR_061693
http://togogenome.org/gene/9606:OR10J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWQ9|||http://purl.uniprot.org/uniprot/P30954                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150707|||http://purl.uniprot.org/annotation/VAR_034292|||http://purl.uniprot.org/annotation/VAR_034293|||http://purl.uniprot.org/annotation/VAR_053281
http://togogenome.org/gene/9606:VCPIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JH7                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Abolished phosphorylation in response to covalent DNA-protein cross-links (DPCs).|||Deubiquitinating protein VCPIP1|||Disordered|||Loss of deubiquitinating activity and ability to deubiquitinate SPRTN.|||N6-acetyllysine|||Nucleophile|||OTU|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065769
http://togogenome.org/gene/9606:WFDC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWY7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||WAP|||WAP four-disulfide core domain protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041390
http://togogenome.org/gene/9606:ATP13A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VNC0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Helical|||N-linked (GlcNAc...) asparagine|||Probable cation-transporting ATPase 13A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337122|||http://purl.uniprot.org/annotation/VAR_043614|||http://purl.uniprot.org/annotation/VAR_043615|||http://purl.uniprot.org/annotation/VAR_043616|||http://purl.uniprot.org/annotation/VAR_043617|||http://purl.uniprot.org/annotation/VAR_043618|||http://purl.uniprot.org/annotation/VAR_061039
http://togogenome.org/gene/9606:CDH10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6N8|||http://purl.uniprot.org/uniprot/X5D8X5|||http://purl.uniprot.org/uniprot/X5DNG6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin-10|||Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003781|||http://purl.uniprot.org/annotation/PRO_0000003782|||http://purl.uniprot.org/annotation/PRO_5004954902|||http://purl.uniprot.org/annotation/PRO_5011954870|||http://purl.uniprot.org/annotation/VAR_028751|||http://purl.uniprot.org/annotation/VAR_036102
http://togogenome.org/gene/9606:CTAGE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEG8|||http://purl.uniprot.org/uniprot/Q96RT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||cTAGE family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189538|||http://purl.uniprot.org/annotation/VAR_046956
http://togogenome.org/gene/9606:PHLDB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of binding to PtdIns(3,4,5)P3.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology-like domain family B member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053894|||http://purl.uniprot.org/annotation/VAR_024760|||http://purl.uniprot.org/annotation/VSP_016744|||http://purl.uniprot.org/annotation/VSP_016745
http://togogenome.org/gene/9606:MAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V302|||http://purl.uniprot.org/uniprot/P61244|||http://purl.uniprot.org/uniprot/Q8TAX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||Does not affect MYC transcriptional activity.|||In PCC; does not repress MYC transcriptional activity.|||In PCC; unknown pathological significance.|||In PCC; unknown pathological significance; does not affect MYC transcriptional activity.|||In PCC; unknown pathological significance; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154.|||Leucine-zipper|||Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154.|||Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153.|||Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154.|||Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153.|||Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154.|||N-acetylserine|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein max|||Removed|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127269|||http://purl.uniprot.org/annotation/VAR_079347|||http://purl.uniprot.org/annotation/VAR_079348|||http://purl.uniprot.org/annotation/VAR_079349|||http://purl.uniprot.org/annotation/VAR_079350|||http://purl.uniprot.org/annotation/VAR_079351|||http://purl.uniprot.org/annotation/VAR_079352|||http://purl.uniprot.org/annotation/VAR_079353|||http://purl.uniprot.org/annotation/VAR_079354|||http://purl.uniprot.org/annotation/VAR_079355|||http://purl.uniprot.org/annotation/VAR_079356|||http://purl.uniprot.org/annotation/VAR_079357|||http://purl.uniprot.org/annotation/VAR_079358|||http://purl.uniprot.org/annotation/VAR_079359|||http://purl.uniprot.org/annotation/VAR_079360|||http://purl.uniprot.org/annotation/VAR_079361|||http://purl.uniprot.org/annotation/VAR_079362|||http://purl.uniprot.org/annotation/VSP_002117|||http://purl.uniprot.org/annotation/VSP_002118|||http://purl.uniprot.org/annotation/VSP_043183|||http://purl.uniprot.org/annotation/VSP_043430|||http://purl.uniprot.org/annotation/VSP_047661
http://togogenome.org/gene/9606:PRXL2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTV5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Peroxiredoxin-like 2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221624|||http://purl.uniprot.org/annotation/VAR_052598
http://togogenome.org/gene/9606:MPV17L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q567V2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mpv17-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317621|||http://purl.uniprot.org/annotation/VAR_058299|||http://purl.uniprot.org/annotation/VSP_031102
http://togogenome.org/gene/9606:C6orf132                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T0Z8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Uncharacterized protein C6orf132                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320612|||http://purl.uniprot.org/annotation/VAR_056799|||http://purl.uniprot.org/annotation/VSP_034432|||http://purl.uniprot.org/annotation/VSP_034433|||http://purl.uniprot.org/annotation/VSP_040816|||http://purl.uniprot.org/annotation/VSP_040817
http://togogenome.org/gene/9606:PRSS53                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L4Q9                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide                                                                                  ^@                                                                                  Charge relay system|||Disordered|||Peptidase S1 1|||Peptidase S1 2|||Serine protease 53                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316763
http://togogenome.org/gene/9606:TOM1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75674                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||GAT|||In isoform 2.|||In isoform 3.|||Interaction with GRB2|||Interaction with PIK3R1|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH2-binding|||SH3-binding|||TOM1-like protein 1|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072566|||http://purl.uniprot.org/annotation/VAR_047469|||http://purl.uniprot.org/annotation/VSP_056852|||http://purl.uniprot.org/annotation/VSP_056853|||http://purl.uniprot.org/annotation/VSP_057424
http://togogenome.org/gene/9606:VWA5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00534                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||VIT|||VWFA|||von Willebrand factor A domain-containing protein 5A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084411|||http://purl.uniprot.org/annotation/VAR_014193|||http://purl.uniprot.org/annotation/VAR_014194|||http://purl.uniprot.org/annotation/VAR_014195|||http://purl.uniprot.org/annotation/VAR_014196|||http://purl.uniprot.org/annotation/VAR_059692|||http://purl.uniprot.org/annotation/VAR_059693|||http://purl.uniprot.org/annotation/VSP_013364|||http://purl.uniprot.org/annotation/VSP_013365|||http://purl.uniprot.org/annotation/VSP_013366|||http://purl.uniprot.org/annotation/VSP_013367|||http://purl.uniprot.org/annotation/VSP_013368
http://togogenome.org/gene/9606:NCAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14594|||http://purl.uniprot.org/uniprot/Q4LE67                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C-type lectin|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||Helical|||Ig-like|||Ig-like V-type|||Link|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine|||Neurocan core protein|||O-glycosylated at one site|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017516|||http://purl.uniprot.org/annotation/VAR_016176|||http://purl.uniprot.org/annotation/VAR_020213|||http://purl.uniprot.org/annotation/VAR_024521
http://togogenome.org/gene/9606:IDH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSZ6|||http://purl.uniprot.org/uniprot/P48735                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  20-fold decrease in Vmax.|||44-fold loss in activity.|||Critical for catalysis|||Found in patients with cartilagenous tumors.|||In D2HGA2.|||In GLM; somatic mutation.|||In GLM; somatic mutation; reduces enzymatic activity.|||In isoform 2.|||Isocitrate dehydrogenase [NADP], mitochondrial|||Isopropylmalate dehydrogenase-like|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||No appreciable difference in Km for isocitrate and NADP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014420|||http://purl.uniprot.org/annotation/VAR_065174|||http://purl.uniprot.org/annotation/VAR_065175|||http://purl.uniprot.org/annotation/VAR_073181|||http://purl.uniprot.org/annotation/VAR_073182|||http://purl.uniprot.org/annotation/VAR_073183|||http://purl.uniprot.org/annotation/VAR_073184|||http://purl.uniprot.org/annotation/VAR_073185|||http://purl.uniprot.org/annotation/VAR_076512|||http://purl.uniprot.org/annotation/VAR_076513|||http://purl.uniprot.org/annotation/VAR_076514|||http://purl.uniprot.org/annotation/VSP_056278
http://togogenome.org/gene/9606:ZPLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||ZP|||Zona pellucida-like domain-containing protein 1|||Zona pellucida-like domain-containing protein 1, secreted form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307284|||http://purl.uniprot.org/annotation/PRO_0000441814|||http://purl.uniprot.org/annotation/VAR_035400|||http://purl.uniprot.org/annotation/VAR_035401|||http://purl.uniprot.org/annotation/VAR_035402|||http://purl.uniprot.org/annotation/VSP_037072
http://togogenome.org/gene/9606:HEATR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VDI1|||http://purl.uniprot.org/uniprot/B2RWN5|||http://purl.uniprot.org/uniprot/Q9H583                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  BP28 C-terminal|||Confirmed at protein level.|||Disordered|||HEAT|||HEAT repeat-containing protein 1|||HEAT repeat-containing protein 1, N-terminally processed|||N-acetylmethionine|||N-acetylthreonine; in HEAT repeat-containing protein 1, N-terminally processed|||Phosphoserine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186201|||http://purl.uniprot.org/annotation/PRO_0000424485|||http://purl.uniprot.org/annotation/VAR_010939|||http://purl.uniprot.org/annotation/VAR_010940|||http://purl.uniprot.org/annotation/VAR_010941|||http://purl.uniprot.org/annotation/VAR_010942|||http://purl.uniprot.org/annotation/VAR_049329|||http://purl.uniprot.org/annotation/VAR_049330|||http://purl.uniprot.org/annotation/VAR_049331|||http://purl.uniprot.org/annotation/VAR_049332|||http://purl.uniprot.org/annotation/VAR_049333|||http://purl.uniprot.org/annotation/VAR_049334|||http://purl.uniprot.org/annotation/VAR_049335
http://togogenome.org/gene/9606:GJB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654IE64|||http://purl.uniprot.org/uniprot/O95377                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-5 protein|||Gap junction protein cysteine-rich|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057868
http://togogenome.org/gene/9606:SLC39A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P5W5|||http://purl.uniprot.org/uniprot/Q9NX22                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes zinc transport activity.|||Abrogates endocytosis of the A-511 mutant which undergoes zinc-independent endocytosis.|||Abrogates endocytosis.|||Basic and acidic residues|||Cytoplasmic|||Decreases location at cell membrane. Retained in the ER. Loss of zinc transport activity.|||Decreases location at cell membrane; retained in the ER.|||Decreases zinc transport activity; when associated with S-238; S-241 and S-243. Decreases Vmax for Zn(2+) by 20% but does not affect the KM; when associated with S-238; S-241 and S-243.|||Decreases zinc transport activity; when associated with S-238; S-241 and S-245. Decreases Vmax for Zn(2+) by 20% does not affect the KM; when associated with S-238; S-241 and S-245.|||Decreases zinc transport activity; when associated with S-238; S-243 and S-245. Decreases Vmax for Zn(2+) by 20% does not affect the KM; when associated with S-238; S-243 and S-245.|||Decreases zinc transport activity; when associated with S-241; S-243; S-245. Decreases Vmax for Zn(2+) by 20% but does not affect the KM; when associated with S-241; S-243; S-245.|||Decreases zinc uptake activity.|||Disordered|||Does not affect location at cell membrane. Does not affect zinc transport activity.|||Does not affect zinc sensing.|||Does not affect zinc transport activity.|||Essential for SLC39A4 endocytosis|||Essential role in Zn(2+) sensing|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||In AEZ.|||In AEZ; Decreases location at cell membrane. Retained in the ER.|||In AEZ; Loss of zinc transport activity. Decreases location at cell membrane. Retained in the ER.|||In AEZ; Loss of zinc transport activity. Decreases location at cell membrane; retained in the ER.|||In AEZ; Loss of zinc transport activity. Decreases location at cell membrane; retained in the ER..|||In AEZ; requires 2 nucleotide substitutions.|||In AEZ; unknown pathological significance.|||In AEZ; unknown pathological significance; Loss of zinc transport activity. Decreases location at cell membrane. Retained in the ER.|||In isoform 2.|||Increases zinc transport activity. Reduces affinity toward zinc. No defect in endocytosis or zinc sensing. Completely abrogated zinc transport activity; when associated with A-507 and A-536.|||Loss of zinc transport activity.|||M1 metal binding site|||M2 metal binding site|||Moderately Reduces zinc transport activity. Reduced zinc transmembrane transporter activity; when associated with A-537. Does not affect substrate specificity; when associated with A-537. Exhibits a zinc transport activity dependent on pH; when associated with A-537.|||Moderately reduces zinc transport activity. Completely abrogated zinc transport activity; when associated with A-536 and A-540.|||Moderately reduces zinc transport activity. Completely abrogates zinc transport activity; when associated with A-507 and A-540.|||Moderately reduces zinc transport activity. Reduces zinc transmembrane transporter activity; when associated with A-508. Does not affect substrate specificity; when associated with A-508. Exhibits a zinc transport activity dependent on pH; when associated with A-508.|||N-linked (GlcNAc...) asparagine|||No effect on SLC39A4 endocytosis. No effect on SLC39A4 endocytosis; when associated with A-481.|||No effect on SLC39A4 endocytosis. No effect on SLC39A4 endocytosis; when associated with A-482.|||No effect on SLC39A4 endocytosis. No effect on SLC39A4 endocytosis; when associated with R-463.|||No effect on SLC39A4 endocytosis. No effect on SLC39A4 endocytosis; when associated with R-611.|||No glycosylated. Very low cell surface expression. Decreases zinc uptake activity.|||Reduces endocytosis.|||Reduces glycosylation level. Reduces cell surface expression. Decreases zinc uptake activity.|||Reduces zinc transport activity by 60%.|||Reduces zinc transport activity; when associated with A-375.|||Reduces zinc transport activity; when associated with A-379.|||Strong reduction of zinc transport activity; when associated with K-537.|||Strong reduction of zinc transport activity; when associated with S-537.|||Strongly reduced zinc transport activity. Loss of zinc-sensing function; endocytosis of this mutant becomes a zinc-independent process.|||Zinc transporter ZIP4 ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042620|||http://purl.uniprot.org/annotation/VAR_023627|||http://purl.uniprot.org/annotation/VAR_023628|||http://purl.uniprot.org/annotation/VAR_023629|||http://purl.uniprot.org/annotation/VAR_023630|||http://purl.uniprot.org/annotation/VAR_023631|||http://purl.uniprot.org/annotation/VAR_023632|||http://purl.uniprot.org/annotation/VAR_023633|||http://purl.uniprot.org/annotation/VAR_023634|||http://purl.uniprot.org/annotation/VAR_023635|||http://purl.uniprot.org/annotation/VAR_023636|||http://purl.uniprot.org/annotation/VAR_023637|||http://purl.uniprot.org/annotation/VAR_023638|||http://purl.uniprot.org/annotation/VAR_023639|||http://purl.uniprot.org/annotation/VAR_023640|||http://purl.uniprot.org/annotation/VAR_023641|||http://purl.uniprot.org/annotation/VAR_023642|||http://purl.uniprot.org/annotation/VAR_057481|||http://purl.uniprot.org/annotation/VAR_057482|||http://purl.uniprot.org/annotation/VAR_057483|||http://purl.uniprot.org/annotation/VAR_060487|||http://purl.uniprot.org/annotation/VSP_015911|||http://purl.uniprot.org/annotation/VSP_015912
http://togogenome.org/gene/9606:ANKRD49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 49|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244585
http://togogenome.org/gene/9606:ACOT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49753                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-coenzyme A thioesterase 2, mitochondrial|||Charge relay system|||In isoform 2.|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202147|||http://purl.uniprot.org/annotation/VAR_016136|||http://purl.uniprot.org/annotation/VAR_057271|||http://purl.uniprot.org/annotation/VSP_012225|||http://purl.uniprot.org/annotation/VSP_012226
http://togogenome.org/gene/9606:RUNX1T1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSU1|||http://purl.uniprot.org/uniprot/B2R6I9|||http://purl.uniprot.org/uniprot/E5RH72|||http://purl.uniprot.org/uniprot/Q06455|||http://purl.uniprot.org/uniprot/W8FW32                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with corepressor.|||Basic and acidic residues|||Breakpoint for translocation to form AML1-MTG8 in AML-M2|||Causes unfolding of the MYND-type zinc finger domain.|||Decreases interaction with TCF12, no effect on oligomerization. Impairs AML1-MTG8/ETO activity in hematopoietic stem/progenitor cell self-renewal but no effect in inhibiting differentiation; when associated with 379-A--A-381.|||Disordered|||Disrupts interaction with TCF12, no effect on oligomerization. Impairs AML1-MTG8/ETO activity in hematopoietic stem/progenitor cell self-renewal but no effect in inhibiting differentiation; when associated with 352-E-E-353.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2 when associated with E-345; R-357; R-360; E-361; E-375 and R-389.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with E-345; R-357; E-361; E-375; R-378 and R-389.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with E-345; R-357; R-360; E-361; E-375 and R-378.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with E-345; R-357; R-360; E-361; R-378 and R-389.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with E-345; R-357; R-360; E-375; R-378 and R-389.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with E-345; R-360; E- 61; E-375; R-378 and R-389.|||Disrupts tetramerization, disrupts AML1-MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when associated with R-357; R-360; E-361; E-375; R-378 and R-389.|||Important for oligomerization|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||In isoform MTG8A and isoform MTG8A-2.|||In isoform MTG8B-2 and isoform MTG8A-2.|||Loss of interaction with TCF12.|||MYND-type|||Nervy homology region 2 (NHR2)|||Nervy homology region 3 (NHR3)|||Phosphoserine|||Polar residues|||Protein CBFA2T1|||TAFH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218299|||http://purl.uniprot.org/annotation/VAR_036321|||http://purl.uniprot.org/annotation/VAR_036322|||http://purl.uniprot.org/annotation/VAR_036323|||http://purl.uniprot.org/annotation/VSP_003327|||http://purl.uniprot.org/annotation/VSP_044558|||http://purl.uniprot.org/annotation/VSP_045442|||http://purl.uniprot.org/annotation/VSP_058512|||http://purl.uniprot.org/annotation/VSP_058513
http://togogenome.org/gene/9606:FAM236A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GUQ0|||http://purl.uniprot.org/uniprot/A0A1B0GV22                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM236A|||Protein FAM236B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000440023|||http://purl.uniprot.org/annotation/PRO_0000440024
http://togogenome.org/gene/9606:OR1L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGR5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1L4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150444|||http://purl.uniprot.org/annotation/VAR_053124|||http://purl.uniprot.org/annotation/VAR_053125
http://togogenome.org/gene/9606:KRIT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1F7|||http://purl.uniprot.org/uniprot/O00522                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  40-fold-reduced affinity for Rap1A.|||ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||FERM|||Impairs interaction with RAP1B.|||In CCM1.|||In isoform 2.|||In isoform 3.|||Interaction with ITGB1BP1|||Interaction with RAP1B|||Krev interaction trapped protein 1|||N-terminal domain similar to Nudix hydrolase domain|||Reduces ITGB1BP1 binding; when associated with A-192.|||Reduces ITGB1BP1 binding; when associated with A-195.|||Reduces interaction with ITGB1BP1.|||Reduces interaction with microtubules, but not with ITGB1BP1.|||Strongly reduced affinity for HEG1; when associated with A-717.|||Strongly reduced affinity for HEG1; when associated with A-721.|||Strongly reduces ITGB1BP1 binding; when associated with A-179.|||Strongly reduces ITGB1BP1 binding; when associated with D-176.|||Strongly reduces ITGB1BP1 binding; when associated with D-182.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067023|||http://purl.uniprot.org/annotation/VAR_023573|||http://purl.uniprot.org/annotation/VAR_023574|||http://purl.uniprot.org/annotation/VSP_015800|||http://purl.uniprot.org/annotation/VSP_043327
http://togogenome.org/gene/9606:SMC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDV3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N6-acetyllysine|||SMC hinge|||Structural maintenance of chromosomes protein 1B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118993|||http://purl.uniprot.org/annotation/VAR_045913|||http://purl.uniprot.org/annotation/VAR_045914|||http://purl.uniprot.org/annotation/VAR_057324|||http://purl.uniprot.org/annotation/VAR_057325|||http://purl.uniprot.org/annotation/VSP_035028
http://togogenome.org/gene/9606:ARL4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40617                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 4A|||Inhibits relocalization of CYTH2 to the plasma membrane. Strongly localized in the nucleolus.|||Localized in the nucleus and nucleolus.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207459
http://togogenome.org/gene/9606:F2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25116                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by CTSG but not by thrombin.|||Cleavage; by CTSG|||Cleavage; by thrombin and CTSG|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Proteinase-activated receptor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012740|||http://purl.uniprot.org/annotation/PRO_0000012741|||http://purl.uniprot.org/annotation/VAR_014167|||http://purl.uniprot.org/annotation/VAR_049432|||http://purl.uniprot.org/annotation/VAR_049433|||http://purl.uniprot.org/annotation/VAR_049434|||http://purl.uniprot.org/annotation/VAR_060680|||http://purl.uniprot.org/annotation/VAR_060681
http://togogenome.org/gene/9606:GLG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92896                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cys-rich GLG1 1|||Cys-rich GLG1 10|||Cys-rich GLG1 11|||Cys-rich GLG1 12|||Cys-rich GLG1 13|||Cys-rich GLG1 14|||Cys-rich GLG1 15|||Cys-rich GLG1 16|||Cys-rich GLG1 2|||Cys-rich GLG1 3|||Cys-rich GLG1 4|||Cys-rich GLG1 5|||Cys-rich GLG1 6|||Cys-rich GLG1 7|||Cys-rich GLG1 8|||Cys-rich GLG1 9|||Cytoplasmic|||Disordered|||Extracellular|||Golgi apparatus protein 1|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011120|||http://purl.uniprot.org/annotation/VSP_035998|||http://purl.uniprot.org/annotation/VSP_043472
http://togogenome.org/gene/9606:RAB3IP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QF0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Important for RAB11A binding|||In isoform 1, isoform 3, isoform 5 and isoform 7.|||In isoform 3 and isoform 4.|||In isoform 5 and isoform 6.|||In isoform 7.|||In isoform 8.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Rab-3A-interacting protein|||Reduced complex formation with RAB11A; when associated with A-435 and A-439.|||Reduced complex formation with RAB11A; when associated with A-435 and A-444.|||Reduced complex formation with RAB11A; when associated with A-439 and A-444.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097144|||http://purl.uniprot.org/annotation/VSP_051755|||http://purl.uniprot.org/annotation/VSP_051756|||http://purl.uniprot.org/annotation/VSP_051757|||http://purl.uniprot.org/annotation/VSP_051758|||http://purl.uniprot.org/annotation/VSP_051759|||http://purl.uniprot.org/annotation/VSP_051760|||http://purl.uniprot.org/annotation/VSP_051761|||http://purl.uniprot.org/annotation/VSP_051762
http://togogenome.org/gene/9606:NLRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9G6|||http://purl.uniprot.org/uniprot/J3KN39|||http://purl.uniprot.org/uniprot/Q9NX02                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Found in patients with female infertility; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||NACHT|||NACHT, LRR and PYD domains-containing protein 2|||Phosphoserine|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080888|||http://purl.uniprot.org/annotation/VAR_020006|||http://purl.uniprot.org/annotation/VAR_025011|||http://purl.uniprot.org/annotation/VAR_053616|||http://purl.uniprot.org/annotation/VAR_053617|||http://purl.uniprot.org/annotation/VAR_062140|||http://purl.uniprot.org/annotation/VAR_068977|||http://purl.uniprot.org/annotation/VAR_068978|||http://purl.uniprot.org/annotation/VAR_068979|||http://purl.uniprot.org/annotation/VAR_084172|||http://purl.uniprot.org/annotation/VAR_084586|||http://purl.uniprot.org/annotation/VAR_084587|||http://purl.uniprot.org/annotation/VAR_084588|||http://purl.uniprot.org/annotation/VAR_084589|||http://purl.uniprot.org/annotation/VAR_084590|||http://purl.uniprot.org/annotation/VAR_084591|||http://purl.uniprot.org/annotation/VSP_005522|||http://purl.uniprot.org/annotation/VSP_017085|||http://purl.uniprot.org/annotation/VSP_017086|||http://purl.uniprot.org/annotation/VSP_044898
http://togogenome.org/gene/9606:PLTP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55058                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased nuclear localization; when associated with A-64; A-117 and A-143.|||Increased nuclear localization; when associated with A-64; A-94 and A-117.|||Increased nuclear localization; when associated with A-64; A-94 and A-143.|||Increased nuclear localization; when associated with A-94; A-117 and A-143.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phospholipid transfer protein|||Significant reduction in HDL-binding and absence of lipid transfer activity.|||Significant reduction in phospholipid transfer activity. Increased secretion.|||Significant reduction in phospholipid transfer activity. No effect on secretion.|||Significant reduction in phospholipid transfer activity. Reduced secretion.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017162|||http://purl.uniprot.org/annotation/VAR_012073|||http://purl.uniprot.org/annotation/VAR_012074|||http://purl.uniprot.org/annotation/VAR_017020|||http://purl.uniprot.org/annotation/VAR_017021|||http://purl.uniprot.org/annotation/VAR_017022|||http://purl.uniprot.org/annotation/VAR_018879|||http://purl.uniprot.org/annotation/VAR_018880|||http://purl.uniprot.org/annotation/VSP_003050|||http://purl.uniprot.org/annotation/VSP_045877|||http://purl.uniprot.org/annotation/VSP_054028
http://togogenome.org/gene/9606:TFAP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92481                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In CHAR.|||In isoform 2.|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Transcription factor AP-2-beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184801|||http://purl.uniprot.org/annotation/VAR_011318|||http://purl.uniprot.org/annotation/VAR_011319|||http://purl.uniprot.org/annotation/VAR_016977|||http://purl.uniprot.org/annotation/VAR_016978|||http://purl.uniprot.org/annotation/VAR_016979|||http://purl.uniprot.org/annotation/VAR_016980|||http://purl.uniprot.org/annotation/VSP_006408
http://togogenome.org/gene/9606:THAP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2Z0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Polar residues|||THAP domain-containing protein 10|||THAP-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068651
http://togogenome.org/gene/9606:RBBP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16576|||http://purl.uniprot.org/uniprot/Q6FHQ0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Repeat|||Splice Variant|||Strand                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone-binding protein RBBP4 N-terminal|||Histone-binding protein RBBP7|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051195|||http://purl.uniprot.org/annotation/VSP_043016
http://togogenome.org/gene/9606:TMEM270                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UE05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane protein 270                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308415|||http://purl.uniprot.org/annotation/VAR_036813|||http://purl.uniprot.org/annotation/VAR_036814|||http://purl.uniprot.org/annotation/VAR_036815|||http://purl.uniprot.org/annotation/VAR_061720|||http://purl.uniprot.org/annotation/VSP_039997|||http://purl.uniprot.org/annotation/VSP_039998
http://togogenome.org/gene/9606:C8orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7E9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Removed|||UPF0488 protein C8orf33                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304982|||http://purl.uniprot.org/annotation/VSP_028169
http://togogenome.org/gene/9606:CLNS1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PJF4|||http://purl.uniprot.org/uniprot/P54105                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Methylosome subunit pICln|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185155|||http://purl.uniprot.org/annotation/VAR_015736|||http://purl.uniprot.org/annotation/VAR_015737
http://togogenome.org/gene/9606:SOX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41225                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Disordered|||HMG box|||In MRXGH.|||In PHPX; reduced transcriptional activity and impaired nuclear localization.|||Transcription factor SOX-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048720|||http://purl.uniprot.org/annotation/VAR_026451|||http://purl.uniprot.org/annotation/VAR_026452|||http://purl.uniprot.org/annotation/VAR_033258
http://togogenome.org/gene/9606:CCDC106                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWC9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Bipartite nuclear localization signal|||Coiled-coil domain-containing protein 106|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274343
http://togogenome.org/gene/9606:OOSP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR6|||http://purl.uniprot.org/uniprot/Q86WS3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Oocyte-secreted protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251150|||http://purl.uniprot.org/annotation/PRO_5014247033
http://togogenome.org/gene/9606:COMP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49747                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||COMP N-terminal|||Cartilage oligomeric matrix protein|||Cell attachment site|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||In CTS2; reduced secretion in tendon cells; no effect on secretion in chondrocytes; disrupted pentamerization; induced ER stress.|||In EDM1 and CTS2; reduced secretion in tendon cells and chondrocytes.|||In EDM1 and PSACH.|||In EDM1.|||In EDM1; Fairbank type.|||In EDM1; Ribbing type.|||In EDM1; atypical form.|||In EDM1; binds less calcium.|||In EDM1; phenotype overlapping with mild PSACH.|||In EDM1; phenotypic features overlapping with mild PSACH.|||In PSACH.|||In PSACH; mild form and EDM1.|||In PSACH; mild form.|||In PSACH; severe form.|||In PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen.|||In PSACH; severe.|||In a patient with multiple epiphyseal dysplasia.|||In isoform 2.|||Interchain|||Mediates cell survival and induction of the IAP family of survival proteins|||N-linked (GlcNAc...) asparagine|||TSP C-terminal|||TSP type-3 1|||TSP type-3 2|||TSP type-3 3|||TSP type-3 4|||TSP type-3 5|||TSP type-3 6|||TSP type-3 7|||TSP type-3 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035857|||http://purl.uniprot.org/annotation/VAR_007614|||http://purl.uniprot.org/annotation/VAR_007615|||http://purl.uniprot.org/annotation/VAR_007616|||http://purl.uniprot.org/annotation/VAR_007617|||http://purl.uniprot.org/annotation/VAR_007618|||http://purl.uniprot.org/annotation/VAR_007619|||http://purl.uniprot.org/annotation/VAR_007620|||http://purl.uniprot.org/annotation/VAR_007621|||http://purl.uniprot.org/annotation/VAR_007622|||http://purl.uniprot.org/annotation/VAR_007623|||http://purl.uniprot.org/annotation/VAR_007624|||http://purl.uniprot.org/annotation/VAR_007625|||http://purl.uniprot.org/annotation/VAR_007626|||http://purl.uniprot.org/annotation/VAR_007627|||http://purl.uniprot.org/annotation/VAR_007628|||http://purl.uniprot.org/annotation/VAR_007629|||http://purl.uniprot.org/annotation/VAR_007630|||http://purl.uniprot.org/annotation/VAR_007631|||http://purl.uniprot.org/annotation/VAR_007632|||http://purl.uniprot.org/annotation/VAR_007633|||http://purl.uniprot.org/annotation/VAR_007634|||http://purl.uniprot.org/annotation/VAR_007635|||http://purl.uniprot.org/annotation/VAR_007636|||http://purl.uniprot.org/annotation/VAR_007637|||http://purl.uniprot.org/annotation/VAR_007638|||http://purl.uniprot.org/annotation/VAR_007639|||http://purl.uniprot.org/annotation/VAR_007640|||http://purl.uniprot.org/annotation/VAR_007641|||http://purl.uniprot.org/annotation/VAR_007642|||http://purl.uniprot.org/annotation/VAR_016254|||http://purl.uniprot.org/annotation/VAR_016255|||http://purl.uniprot.org/annotation/VAR_016257|||http://purl.uniprot.org/annotation/VAR_016258|||http://purl.uniprot.org/annotation/VAR_016261|||http://purl.uniprot.org/annotation/VAR_017102|||http://purl.uniprot.org/annotation/VAR_017103|||http://purl.uniprot.org/annotation/VAR_026239|||http://purl.uniprot.org/annotation/VAR_026240|||http://purl.uniprot.org/annotation/VAR_046796|||http://purl.uniprot.org/annotation/VAR_066789|||http://purl.uniprot.org/annotation/VAR_066790|||http://purl.uniprot.org/annotation/VAR_066791|||http://purl.uniprot.org/annotation/VAR_066792|||http://purl.uniprot.org/annotation/VAR_066793|||http://purl.uniprot.org/annotation/VAR_066794|||http://purl.uniprot.org/annotation/VAR_066795|||http://purl.uniprot.org/annotation/VAR_066796|||http://purl.uniprot.org/annotation/VAR_066797|||http://purl.uniprot.org/annotation/VAR_066798|||http://purl.uniprot.org/annotation/VAR_066799|||http://purl.uniprot.org/annotation/VAR_066800|||http://purl.uniprot.org/annotation/VAR_066801|||http://purl.uniprot.org/annotation/VAR_066802|||http://purl.uniprot.org/annotation/VAR_066803|||http://purl.uniprot.org/annotation/VAR_066804|||http://purl.uniprot.org/annotation/VAR_066805|||http://purl.uniprot.org/annotation/VAR_066806|||http://purl.uniprot.org/annotation/VAR_066807|||http://purl.uniprot.org/annotation/VAR_066808|||http://purl.uniprot.org/annotation/VAR_066809|||http://purl.uniprot.org/annotation/VAR_066810|||http://purl.uniprot.org/annotation/VAR_066811|||http://purl.uniprot.org/annotation/VAR_066812|||http://purl.uniprot.org/annotation/VAR_066813|||http://purl.uniprot.org/annotation/VAR_066814|||http://purl.uniprot.org/annotation/VAR_066815|||http://purl.uniprot.org/annotation/VAR_066816|||http://purl.uniprot.org/annotation/VAR_066817|||http://purl.uniprot.org/annotation/VAR_066818|||http://purl.uniprot.org/annotation/VAR_066819|||http://purl.uniprot.org/annotation/VAR_066820|||http://purl.uniprot.org/annotation/VAR_066821|||http://purl.uniprot.org/annotation/VAR_066822|||http://purl.uniprot.org/annotation/VAR_066823|||http://purl.uniprot.org/annotation/VAR_066824|||http://purl.uniprot.org/annotation/VAR_066825|||http://purl.uniprot.org/annotation/VAR_066826|||http://purl.uniprot.org/annotation/VAR_066827|||http://purl.uniprot.org/annotation/VAR_066828|||http://purl.uniprot.org/annotation/VAR_066829|||http://purl.uniprot.org/annotation/VAR_085230|||http://purl.uniprot.org/annotation/VSP_055758
http://togogenome.org/gene/9606:TRPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5H6B6|||http://purl.uniprot.org/uniprot/Q86TN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||tRNA 2'-phosphotransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273363|||http://purl.uniprot.org/annotation/VAR_030134|||http://purl.uniprot.org/annotation/VAR_030135|||http://purl.uniprot.org/annotation/VAR_030136|||http://purl.uniprot.org/annotation/VSP_022524|||http://purl.uniprot.org/annotation/VSP_045273|||http://purl.uniprot.org/annotation/VSP_045827
http://togogenome.org/gene/9606:ATAD3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T2N8                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Binding Site|||Chain                                                                                  ^@                                                                                  ATPase family AAA domain-containing protein 3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311979
http://togogenome.org/gene/9606:OR9I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVJ4|||http://purl.uniprot.org/uniprot/Q8NGQ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 9I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150681
http://togogenome.org/gene/9606:LMAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49257                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mass|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||ER export motif|||Helical|||In F5F8D1; loss of interaction with MCFD2 and ability to bind D-mannose.|||Interchain|||L-type lectin-like|||Lumenal|||Mediates interaction with RAB3GAP1, RAB3GAP2 and UBXN6|||Phosphoserine|||Protein ERGIC-53|||Required for ER export                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017660|||http://purl.uniprot.org/annotation/VAR_013703|||http://purl.uniprot.org/annotation/VAR_013704|||http://purl.uniprot.org/annotation/VAR_013705|||http://purl.uniprot.org/annotation/VAR_049770|||http://purl.uniprot.org/annotation/VAR_071969
http://togogenome.org/gene/9606:PI4K2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTU6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity.|||Abolishes enzyme activity; when associated with A-165 and A-168.|||Abolishes enzyme activity; when associated with A-165 and A-172.|||Abolishes enzyme activity; when associated with A-168 and A-172.|||Abolishes enzyme activity; when associated with A-184.|||Abolishes enzyme activity; when associated with A-263.|||Abolishes enzyme activity; when associated with A-345.|||Abolishes enzyme activity; when associated with A-349.|||Abolishes palmitoylation and impairs membrane-association.|||Activation loop|||Catalytic loop|||Disordered|||G-loop|||Important for interaction with membranes|||Important for substrate binding|||N-acetylmethionine|||No effect on membrane-association.|||PI3K/PI4K catalytic|||Phosphatidylinositol 4-kinase type 2-alpha|||Phosphoserine|||Reduces enzyme activity by half.|||Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-359 and A-365.|||Reduces enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-368 and A-359.|||Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-275.|||Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-129 and E-276.|||Reduces enzyme activity, probably due to impaired membrane-association; when associated with E-275 and E-276.|||Reduces enzyme activity.|||S-palmitoyl cysteine|||Strongly reduced enzyme activity, probably due to impaired membrane-association. Abolishes enzyme activity; when associated with A-365 and A-368.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285158
http://togogenome.org/gene/9606:PI4KB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J1S8|||http://purl.uniprot.org/uniprot/Q9UBF8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Catalytic loop|||Disordered|||Drastically decreased ACBD3-binding. No effect on ARMH3-, nor RAB11B-binding.|||Drastically decreased ARMH3- and RAB11B-binding. 6-fold increase in ACBD3-binding.|||G-loop|||In DFNA87; unable to rescue defective inner ear phenotype and sound stimuli response in zebrafish morphants.|||In DFNA87; unknown pathological significance; unable to rescue defective inner ear phenotype and sound stimuli response in zebrafish morphants.|||In isoform 2.|||In isoform 3.|||Interaction with ACBD3|||Loss of interaction with ACBD3.|||N-acetylglycine|||No effect on ACBD3-, ARMH3-, nor RAB11B-binding.|||No loss of interaction with ACBD3.|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4-kinase beta|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Small decrease in ARMH3-binding. No effect on ACBD3-, nor RAB11B-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088829|||http://purl.uniprot.org/annotation/VAR_088345|||http://purl.uniprot.org/annotation/VAR_088346|||http://purl.uniprot.org/annotation/VAR_088347|||http://purl.uniprot.org/annotation/VAR_088348|||http://purl.uniprot.org/annotation/VSP_037133|||http://purl.uniprot.org/annotation/VSP_050627
http://togogenome.org/gene/9606:TSPAN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60637                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Tetraspanin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219239|||http://purl.uniprot.org/annotation/VSP_042679|||http://purl.uniprot.org/annotation/VSP_043519
http://togogenome.org/gene/9606:NLE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVX2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||Notchless protein homolog 1|||Phosphoserine|||Removed|||Ubiquitin-like (UBL) domain|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051098|||http://purl.uniprot.org/annotation/VAR_035886|||http://purl.uniprot.org/annotation/VAR_057616|||http://purl.uniprot.org/annotation/VAR_057617|||http://purl.uniprot.org/annotation/VAR_060327|||http://purl.uniprot.org/annotation/VAR_060328|||http://purl.uniprot.org/annotation/VSP_040555
http://togogenome.org/gene/9606:SHISA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSJ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein shisa-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326154|||http://purl.uniprot.org/annotation/VSP_032565|||http://purl.uniprot.org/annotation/VSP_040558
http://togogenome.org/gene/9606:KIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60870                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Almost complete loss of in vitro methylation by METTL22.|||Basic and acidic residues|||C-terminal subdomain A|||C-terminal subdomain B|||C2H2-type|||DNA/RNA-binding protein KIN17|||Disordered|||In isoform 2.|||N6,N6,N6-trimethyllysine; by METTL22; in vitro|||N6-methyllysine|||Polar residues|||Significant reduction of RNA-binding activity.|||Winged helix-turn-helix (wHTH)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289134|||http://purl.uniprot.org/annotation/VSP_056074
http://togogenome.org/gene/9606:BABAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQS6|||http://purl.uniprot.org/uniprot/Q9NWV8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||BRISC and BRCA1-A complex member 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||VWFA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288458|||http://purl.uniprot.org/annotation/VSP_037246|||http://purl.uniprot.org/annotation/VSP_037247|||http://purl.uniprot.org/annotation/VSP_037248|||http://purl.uniprot.org/annotation/VSP_037249
http://togogenome.org/gene/9606:SNAPC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75971                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Minimal effect on SNAPC4 binding in the absence of SNAPC1. Reduced SNAPC4 binding in the presence of SNAPC1.|||Phosphothreonine|||Reduced SNAPC4 binding in both the presence or absence of SNAPC1.|||snRNA-activating protein complex subunit 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072028|||http://purl.uniprot.org/annotation/VSP_012785
http://togogenome.org/gene/9606:PTGFRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2B2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell attachment site|||Cytoplasmic|||Endoplasmic reticulum retention signal|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Prostaglandin F2 receptor negative regulator                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014762|||http://purl.uniprot.org/annotation/VAR_024496|||http://purl.uniprot.org/annotation/VAR_059388
http://togogenome.org/gene/9606:PMCH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20382                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modified Residue|||Peptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Isoleucine amide|||Melanin-concentrating hormone|||Neuropeptide-glutamic acid-isoleucine|||Neuropeptide-glycine-glutamic acid|||Pro-MCH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019104|||http://purl.uniprot.org/annotation/PRO_0000019105|||http://purl.uniprot.org/annotation/PRO_0000019106|||http://purl.uniprot.org/annotation/PRO_0000019107
http://togogenome.org/gene/9606:MKRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHC7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Disordered|||E3 ubiquitin-protein ligase makorin-1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of E3 ligase activity, but no effect on transcription regulation.|||Makorin-type Cys-His|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055952|||http://purl.uniprot.org/annotation/VAR_012161|||http://purl.uniprot.org/annotation/VAR_057214|||http://purl.uniprot.org/annotation/VSP_040361|||http://purl.uniprot.org/annotation/VSP_040362|||http://purl.uniprot.org/annotation/VSP_040363|||http://purl.uniprot.org/annotation/VSP_040364
http://togogenome.org/gene/9606:SLITRK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTY4|||http://purl.uniprot.org/uniprot/Q9H156                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Does not affect synaptogenesis; no effect on localization to cell membrane.|||Extracellular|||Found in a patient with schizophrenia; unknown pathological significance; does not impair synaptogenesis; no effect on localization to cell membrane.|||Helical|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Polar residues|||Required for interaction with PTPRD|||SLIT and NTRK-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032675|||http://purl.uniprot.org/annotation/PRO_5014567666|||http://purl.uniprot.org/annotation/VAR_027756|||http://purl.uniprot.org/annotation/VAR_077630|||http://purl.uniprot.org/annotation/VAR_077631|||http://purl.uniprot.org/annotation/VSP_050706|||http://purl.uniprot.org/annotation/VSP_050707
http://togogenome.org/gene/9606:IFNAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17181                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished STAT1 activation upon IFNA2 binding but no effect upon IFNG binding.|||Abolishes interaction with FBXW11 and decreases ubiquitination.|||Abolishes phosphorylation at this site and interaction with SHMT2.|||Basic and acidic residues|||Cytoplasmic|||Decreased STAT1 activation upon IFNA2 binding but no effect upon IFNG binding.|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Impairs interaction with TYK2.|||Impairs internalization in response to interferon.|||Important for interaction with TYK2|||In IMD106; decreased protein abundance.|||In IMD106; loss of localization at the plasma membrane; loss of type I interferon receptor activity.|||In IMD106; no protein detected in homozygous patient cells; loss of type I interferon receptor activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interferon alpha/beta receptor 1|||Mildly reduces ubiquitination. Nearly abolishes ubiquitination and subsequent degradation; when associated with 525-R-R-526.|||N-linked (GlcNAc...) asparagine|||No effect on activation of STAT1 upon IFNA2 or IFNG binding IFNG binding.|||No effect on activation of STAT1 upon IFNA2 or IFNG binding.|||Phosphoserine|||Phosphotyrosine; by TYK2|||Reduces ubiquitination. Nearly abolishes ubiquitination and subsequent degradation; when associated with R-501.|||Requires 2 nucleotide substitutions; no effect on activation of STAT1 upon IFNA2 or IFNG binding.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011001|||http://purl.uniprot.org/annotation/VAR_002717|||http://purl.uniprot.org/annotation/VAR_020502|||http://purl.uniprot.org/annotation/VAR_020503|||http://purl.uniprot.org/annotation/VAR_084085|||http://purl.uniprot.org/annotation/VAR_084086|||http://purl.uniprot.org/annotation/VAR_084087|||http://purl.uniprot.org/annotation/VAR_084088|||http://purl.uniprot.org/annotation/VAR_084089|||http://purl.uniprot.org/annotation/VAR_084090|||http://purl.uniprot.org/annotation/VAR_084091|||http://purl.uniprot.org/annotation/VAR_084092|||http://purl.uniprot.org/annotation/VAR_084093|||http://purl.uniprot.org/annotation/VAR_084094|||http://purl.uniprot.org/annotation/VAR_084095|||http://purl.uniprot.org/annotation/VAR_084096|||http://purl.uniprot.org/annotation/VAR_084097|||http://purl.uniprot.org/annotation/VAR_084098|||http://purl.uniprot.org/annotation/VAR_087556|||http://purl.uniprot.org/annotation/VAR_087557|||http://purl.uniprot.org/annotation/VAR_087558|||http://purl.uniprot.org/annotation/VSP_029928|||http://purl.uniprot.org/annotation/VSP_029929|||http://purl.uniprot.org/annotation/VSP_029930|||http://purl.uniprot.org/annotation/VSP_029931|||http://purl.uniprot.org/annotation/VSP_055322
http://togogenome.org/gene/9606:AHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35869                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes specific ligand binding.|||Abolishes transcription factor activity. Alters on nuclear translocation upon ligand binding.|||Abolishes transcription factor activity; when associated with D-50 and D-79.|||Abolishes transcription factor activity; when associated with D-50 and D-82.|||Abolishes transcription factor activity; when associated with D-79 and D-82.|||Almost abolishes transcription factor activity. No effect on nuclear translocation upon ligand binding.|||Aryl hydrocarbon receptor|||DNA-binding|||Disordered|||Increases specific ligand binding.|||Interfers with transcription factor activity.|||N-acetylmethionine|||No effect on specific ligand binding.|||Nuclear export signal|||Nuclear localization signal 1|||Nuclear localization signal 2|||PAC|||PAS 1|||PAS 2|||Required for maintaining the overall integrity of the AHR:ARNT heterodimer and its transcriptional activity|||Strongly reduces transcription factor activity.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013450|||http://purl.uniprot.org/annotation/PRO_0000013451|||http://purl.uniprot.org/annotation/VAR_009281|||http://purl.uniprot.org/annotation/VAR_009282|||http://purl.uniprot.org/annotation/VAR_015516|||http://purl.uniprot.org/annotation/VAR_015517
http://togogenome.org/gene/9606:DYNC1I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1I7|||http://purl.uniprot.org/uniprot/O14576|||http://purl.uniprot.org/uniprot/Q8N542                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic dynein 1 intermediate chain 1|||Decreases interaction with DYNLT1.|||Disordered|||Disrupts interaction with DYNLT1.|||Found in a renal cell carcinoma case; somatic mutation.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||Interaction with DCTN1|||Interaction with DYNLT1|||N-acetylserine|||No effect on interaction with DYNLT1.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114652|||http://purl.uniprot.org/annotation/VAR_048905|||http://purl.uniprot.org/annotation/VAR_064709|||http://purl.uniprot.org/annotation/VSP_001332|||http://purl.uniprot.org/annotation/VSP_001333|||http://purl.uniprot.org/annotation/VSP_054766
http://togogenome.org/gene/9606:YY1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25490                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished phosphorylation by CK2, leading to increased cleavage by caspase-7 (CASP7).|||Acidic residues|||Basic residues|||Binding to DNA|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Cleavage; by caspase-7|||Disordered|||Found in patients with late onset insulinomas; alters DNA-binding motif; increases transactivation activity; produces a constitutive activation of cAMP and Ca2+ signaling pathways involved in insulin secretion.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In GADEVS.|||In GADEVS; reduced DNA-binding; reduced transcription regulator activity.|||In GADEVS; unknown pathological significance.|||Interaction with the SMAD1/SMAD4 complex|||Involved in masking transactivation domain|||Involved in nuclear matrix association|||Involved in repression of activated transcription|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Transcriptional repressor protein YY1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047190|||http://purl.uniprot.org/annotation/VAR_065086|||http://purl.uniprot.org/annotation/VAR_074172|||http://purl.uniprot.org/annotation/VAR_079202|||http://purl.uniprot.org/annotation/VAR_079203|||http://purl.uniprot.org/annotation/VAR_079204|||http://purl.uniprot.org/annotation/VAR_079205|||http://purl.uniprot.org/annotation/VAR_079206|||http://purl.uniprot.org/annotation/VAR_079207|||http://purl.uniprot.org/annotation/VAR_079208
http://togogenome.org/gene/9606:BLOC1S5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTN6|||http://purl.uniprot.org/uniprot/Q8TDH9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Biogenesis of lysosome-related organelles complex 1 subunit 5|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096651|||http://purl.uniprot.org/annotation/VSP_015088|||http://purl.uniprot.org/annotation/VSP_015089|||http://purl.uniprot.org/annotation/VSP_045013
http://togogenome.org/gene/9606:SPATC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV4|||http://purl.uniprot.org/uniprot/Q76KD6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Necessary for targeting centrosomes|||Polar residues|||Speriolin|||Speriolin N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312300|||http://purl.uniprot.org/annotation/VSP_042815|||http://purl.uniprot.org/annotation/VSP_042816
http://togogenome.org/gene/9606:GPR137B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60478                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Integral membrane protein GPR137B|||Lumenal|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072583
http://togogenome.org/gene/9606:CCDC124                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CT7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 124|||Disordered|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263735|||http://purl.uniprot.org/annotation/VAR_053809
http://togogenome.org/gene/9606:TBC1D31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7ERK7|||http://purl.uniprot.org/uniprot/Q96DN5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Loss of interaction with PJA2.|||Mediates direct interaction with PJA2|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 31|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051420|||http://purl.uniprot.org/annotation/VAR_027960|||http://purl.uniprot.org/annotation/VAR_027961|||http://purl.uniprot.org/annotation/VAR_057632|||http://purl.uniprot.org/annotation/VSP_016184|||http://purl.uniprot.org/annotation/VSP_043414
http://togogenome.org/gene/9606:DDX55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX55|||Basic and acidic residues|||Basic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Phosphoserine|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252210|||http://purl.uniprot.org/annotation/VAR_027789|||http://purl.uniprot.org/annotation/VAR_027790|||http://purl.uniprot.org/annotation/VAR_027791|||http://purl.uniprot.org/annotation/VAR_027792|||http://purl.uniprot.org/annotation/VSP_056155
http://togogenome.org/gene/9606:CTSK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43235                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cathepsin K|||In PKND.|||In PKND; does not affect protein level; does not detect cysteine-type endopeptidase activity.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026295|||http://purl.uniprot.org/annotation/PRO_0000026296|||http://purl.uniprot.org/annotation/VAR_006725|||http://purl.uniprot.org/annotation/VAR_006726|||http://purl.uniprot.org/annotation/VAR_015738|||http://purl.uniprot.org/annotation/VAR_015739|||http://purl.uniprot.org/annotation/VAR_074023|||http://purl.uniprot.org/annotation/VAR_074024
http://togogenome.org/gene/9606:KRT78                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1N4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Head|||IF rod|||In isoform 2.|||Keratin, type II cytoskeletal 78|||Linker 1|||Linker 12|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314891|||http://purl.uniprot.org/annotation/VAR_038109|||http://purl.uniprot.org/annotation/VAR_038110|||http://purl.uniprot.org/annotation/VAR_038111|||http://purl.uniprot.org/annotation/VAR_038112|||http://purl.uniprot.org/annotation/VSP_030419|||http://purl.uniprot.org/annotation/VSP_030420
http://togogenome.org/gene/9606:CLDN23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B33                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-23|||Cytoplasmic|||Disordered|||Extracellular|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144787|||http://purl.uniprot.org/annotation/VAR_059219
http://togogenome.org/gene/9606:FBXO46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJ61                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 46|||Phosphoserine|||Phosphothreonine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119950
http://togogenome.org/gene/9606:NHEJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9Q4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished DNA-binding.|||Abolished ability to participate in V(D)J recombination.|||Abolished ability to repair double-strand breaks (DSBs). Abolished ability to participate in V(D)J recombination.|||Abolished ability to repair double-strand breaks (DSBs). Abolished ability to participate in V(D)J recombination. Abolished interaction with XRCC4.|||Abolished ability to repair double-strand breaks (DSBs). Abolished ability to participate in V(D)J recombination. Decreased interaction with XRCC4.|||Abolished ability to repair double-strand breaks (DSBs). Abolished interaction with XRCC4. Abolished ability to participate in V(D)J recombination.|||Abolished interaction with XRCC4.|||Decreased ability to repair double-strand breaks (DSBs). Impaired ability to participate in V(D)J recombination.|||Disordered|||Does not affect ability to participate in V(D)J recombination.|||Does not affect ability to repair double-strand breaks (DSBs). Does not affect interaction with XRCC4.|||Does not affect interaction with XRCC4.|||Globular head|||Impaired ability to repair double-strand breaks (DSBs). Abolished interaction with XRCC4. Abolished ability to bridge DNA.|||Impaired ability to repair double-strand breaks (DSBs). Does not affect interaction with XRCC4.|||Impaired ability to repair double-strand breaks (DSBs). Does not affect interaction with XRCC4. Does not affect ability to participate in V(D)J recombination.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-251 and A-263.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-251 and A-266.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-132, A-203 and A-245.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-251, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-132, A-203 and A-251.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-245, A-251, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-132, A-245 and A-251.|||In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-203, A-245, A-251, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-203, A-245 and A-251.|||In NHEJ1-SCID.|||In NHEJ1-SCID; fails to translocate to the nucleus.|||In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-132, D-203 and D-245.|||In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-132, D-203 and D-251.|||In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-132, D-245 and D-251.|||In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-203, D-245 and D-251.|||In isoform 2.|||Leu-lock|||Non-homologous end-joining factor 1|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine|||Polar residues|||XLM ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228654|||http://purl.uniprot.org/annotation/VAR_025704|||http://purl.uniprot.org/annotation/VAR_025705|||http://purl.uniprot.org/annotation/VAR_038790|||http://purl.uniprot.org/annotation/VAR_038791|||http://purl.uniprot.org/annotation/VAR_038792|||http://purl.uniprot.org/annotation/VSP_017689
http://togogenome.org/gene/9606:ZNF609                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15014                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 609                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280422|||http://purl.uniprot.org/annotation/VSP_059082|||http://purl.uniprot.org/annotation/VSP_059083
http://togogenome.org/gene/9606:RECQL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94761                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent DNA helicase Q4|||Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In BGS.|||In RTS2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205053|||http://purl.uniprot.org/annotation/VAR_023295|||http://purl.uniprot.org/annotation/VAR_023296|||http://purl.uniprot.org/annotation/VAR_023297|||http://purl.uniprot.org/annotation/VAR_023298|||http://purl.uniprot.org/annotation/VAR_023299|||http://purl.uniprot.org/annotation/VAR_025117|||http://purl.uniprot.org/annotation/VAR_025118|||http://purl.uniprot.org/annotation/VAR_025119|||http://purl.uniprot.org/annotation/VAR_025120|||http://purl.uniprot.org/annotation/VAR_025121|||http://purl.uniprot.org/annotation/VAR_025122|||http://purl.uniprot.org/annotation/VAR_025123|||http://purl.uniprot.org/annotation/VAR_025124|||http://purl.uniprot.org/annotation/VAR_025125|||http://purl.uniprot.org/annotation/VAR_025126|||http://purl.uniprot.org/annotation/VAR_025127|||http://purl.uniprot.org/annotation/VAR_025128|||http://purl.uniprot.org/annotation/VAR_025129|||http://purl.uniprot.org/annotation/VAR_025130|||http://purl.uniprot.org/annotation/VAR_025131|||http://purl.uniprot.org/annotation/VAR_025132|||http://purl.uniprot.org/annotation/VAR_025133|||http://purl.uniprot.org/annotation/VAR_025134|||http://purl.uniprot.org/annotation/VAR_025135|||http://purl.uniprot.org/annotation/VAR_025136|||http://purl.uniprot.org/annotation/VAR_025137|||http://purl.uniprot.org/annotation/VAR_026590|||http://purl.uniprot.org/annotation/VAR_026591|||http://purl.uniprot.org/annotation/VAR_057125|||http://purl.uniprot.org/annotation/VAR_083742|||http://purl.uniprot.org/annotation/VAR_083743|||http://purl.uniprot.org/annotation/VAR_083744|||http://purl.uniprot.org/annotation/VAR_083745
http://togogenome.org/gene/9606:NUBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Y2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cytosolic Fe-S cluster assembly factor NUBP2|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184945|||http://purl.uniprot.org/annotation/VAR_050099|||http://purl.uniprot.org/annotation/VAR_050100|||http://purl.uniprot.org/annotation/VAR_061353
http://togogenome.org/gene/9606:UGT3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SY77                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 3A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299153|||http://purl.uniprot.org/annotation/VAR_036036|||http://purl.uniprot.org/annotation/VAR_057329|||http://purl.uniprot.org/annotation/VSP_046099
http://togogenome.org/gene/9606:FCSK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0W3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In CDGF2; unknown pathological significance.|||In isoform 2.|||L-fucose kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156672|||http://purl.uniprot.org/annotation/VAR_021327|||http://purl.uniprot.org/annotation/VAR_021328|||http://purl.uniprot.org/annotation/VAR_021329|||http://purl.uniprot.org/annotation/VAR_021330|||http://purl.uniprot.org/annotation/VAR_021331|||http://purl.uniprot.org/annotation/VAR_021332|||http://purl.uniprot.org/annotation/VAR_021333|||http://purl.uniprot.org/annotation/VAR_021334|||http://purl.uniprot.org/annotation/VAR_021335|||http://purl.uniprot.org/annotation/VAR_081646|||http://purl.uniprot.org/annotation/VAR_081647|||http://purl.uniprot.org/annotation/VAR_081648|||http://purl.uniprot.org/annotation/VSP_015422|||http://purl.uniprot.org/annotation/VSP_015423
http://togogenome.org/gene/9606:RIPPLY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TAB7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Protein ripply2|||Ripply homology domain|||WRPW motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307759|||http://purl.uniprot.org/annotation/VSP_052556
http://togogenome.org/gene/9606:CPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22792                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Carboxypeptidase N subunit 2|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020989|||http://purl.uniprot.org/annotation/VAR_019721|||http://purl.uniprot.org/annotation/VAR_019722|||http://purl.uniprot.org/annotation/VAR_065186
http://togogenome.org/gene/9606:AIFM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  4-hydroxy-2-nonenal adduction|||Ferroptosis suppressor protein 1|||Helical|||Impairs N-myristoylation and ferroptosis suppression.|||Impairs the reductase activity toward coenzyme Q1/ubiquinone-1. Impairs ferroptosis suppression.|||In isoform 2.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238922|||http://purl.uniprot.org/annotation/VAR_050651|||http://purl.uniprot.org/annotation/VAR_050652|||http://purl.uniprot.org/annotation/VSP_052047|||http://purl.uniprot.org/annotation/VSP_052048
http://togogenome.org/gene/9606:SEMA4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PSI|||Phosphoserine|||Polar residues|||Sema|||Semaphorin-4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032324|||http://purl.uniprot.org/annotation/VAR_010758|||http://purl.uniprot.org/annotation/VSP_012460
http://togogenome.org/gene/9606:ZNF234                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14588                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||KRNB|||Zinc finger protein 234                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047473|||http://purl.uniprot.org/annotation/VAR_019977|||http://purl.uniprot.org/annotation/VAR_052799
http://togogenome.org/gene/9606:SSMEM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ISA2|||http://purl.uniprot.org/uniprot/A4D1L0|||http://purl.uniprot.org/uniprot/Q8WWF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Serine-rich single-pass membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271354|||http://purl.uniprot.org/annotation/VAR_029873
http://togogenome.org/gene/9606:GPR141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z602                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069618|||http://purl.uniprot.org/annotation/VAR_074185
http://togogenome.org/gene/9606:CST6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15828                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cystatin-M|||In ECTD15; loss of cystein protease inhibitory activity toward cathepsin L, cathepsin V and legumain.|||N-linked (GlcNAc...) asparagine|||Reactive site|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006648|||http://purl.uniprot.org/annotation/VAR_083237
http://togogenome.org/gene/9606:CD1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29016                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||In isoform 2.|||Internalization signal|||N-linked (GlcNAc...) asparagine|||Strongly reduced internalization and trafficking to endosomes.|||T-cell surface glycoprotein CD1b                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014579|||http://purl.uniprot.org/annotation/VSP_016911
http://togogenome.org/gene/9606:DNAJB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBS4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  DnaJ homolog subfamily B member 11|||Drastic loss of interaction with denatured substrates.|||In PKD6.|||J|||Loss of HSPA5-binding, but no effect on interaction with denatured substrates.|||N-linked (GlcNAc...) asparagine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007260|||http://purl.uniprot.org/annotation/VAR_016092|||http://purl.uniprot.org/annotation/VAR_081002|||http://purl.uniprot.org/annotation/VAR_081003|||http://purl.uniprot.org/annotation/VAR_081004
http://togogenome.org/gene/9606:PCNX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RV3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Pecanex-like protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215793|||http://purl.uniprot.org/annotation/VAR_028305|||http://purl.uniprot.org/annotation/VAR_028306|||http://purl.uniprot.org/annotation/VAR_050478|||http://purl.uniprot.org/annotation/VSP_008401|||http://purl.uniprot.org/annotation/VSP_008402|||http://purl.uniprot.org/annotation/VSP_008403|||http://purl.uniprot.org/annotation/VSP_054500|||http://purl.uniprot.org/annotation/VSP_054501
http://togogenome.org/gene/9606:LTBR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36941                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034552|||http://purl.uniprot.org/annotation/VAR_052346|||http://purl.uniprot.org/annotation/VSP_047533
http://togogenome.org/gene/9606:STOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In PEE4.|||In isoform B.|||In isoform C.|||Polar residues|||Storkhead-box protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072281|||http://purl.uniprot.org/annotation/VAR_023784|||http://purl.uniprot.org/annotation/VAR_023785|||http://purl.uniprot.org/annotation/VAR_023786|||http://purl.uniprot.org/annotation/VAR_023787|||http://purl.uniprot.org/annotation/VAR_051388|||http://purl.uniprot.org/annotation/VSP_016226|||http://purl.uniprot.org/annotation/VSP_016227|||http://purl.uniprot.org/annotation/VSP_016228|||http://purl.uniprot.org/annotation/VSP_016229
http://togogenome.org/gene/9606:RHOXF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQY4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in infertile men; unknown pathological significance.|||Found in infertile men; unknown pathological significance; decreased induction of target genes expression.|||Homeobox|||Nuclear localization signal|||Rhox homeobox family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049246|||http://purl.uniprot.org/annotation/VAR_078297|||http://purl.uniprot.org/annotation/VAR_078298|||http://purl.uniprot.org/annotation/VAR_078299|||http://purl.uniprot.org/annotation/VAR_078300
http://togogenome.org/gene/9606:ALG12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV10                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase|||Helical|||In CDG1G.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215781|||http://purl.uniprot.org/annotation/VAR_017904|||http://purl.uniprot.org/annotation/VAR_017905|||http://purl.uniprot.org/annotation/VAR_017906|||http://purl.uniprot.org/annotation/VAR_017907|||http://purl.uniprot.org/annotation/VAR_024466|||http://purl.uniprot.org/annotation/VAR_038428
http://togogenome.org/gene/9606:BSG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35613|||http://purl.uniprot.org/uniprot/Q54A51                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basigin|||Cytoplasmic|||Disordered|||Essential for interaction with KDR/VEGFR2|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In Ok(A-); 2-fold reduction in the binding affinity for P.falciparum RH5 with reduced erythrocyte invasion by P.falciparum isolates 3D7 and Dd2.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of ability to stimulate interleukin-6 secretion.|||Loss of interaction with P.falciparum RH5.|||Loss of interaction with PPIL2.|||Loss of its ability to mediate chemotactic activity of PPIA/CYPA.|||N-linked (GlcNAc...) asparagine|||No effect on the interaction with P.falciparum RH5.|||No effect on the interaction with P.falciparum RH5; when associated with D-160 and D-268.|||No effect on the interaction with P.falciparum RH5; when associated with D-160 and D-302.|||No effect on the interaction with P.falciparum RH5; when associated with D-268 and D-302.|||Phosphoserine|||Reduced interaction with KDR/VEGFR2.|||Reduced interaction with KDR/VEGFR2. Complete loss of interaction with KDR/VEGFR2 when associated with A-199.|||Reduced interaction with KDR/VEGFR2. Complete loss of interaction with KDR/VEGFR2; when associated with A-195.|||Reduced interaction with KDR/VEGFR2. Significant loss of interaction with KDR/VEGFR2; when associated with A-182.|||Reduced interaction with KDR/VEGFR2. Significant loss of interaction with KDR/VEGFR2; when associated with A-184.|||Severe reduction in the interaction with P.falciparum RH5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014518|||http://purl.uniprot.org/annotation/PRO_5014309621|||http://purl.uniprot.org/annotation/VAR_011720|||http://purl.uniprot.org/annotation/VAR_013574|||http://purl.uniprot.org/annotation/VAR_082637|||http://purl.uniprot.org/annotation/VAR_082638|||http://purl.uniprot.org/annotation/VAR_082639|||http://purl.uniprot.org/annotation/VAR_084546|||http://purl.uniprot.org/annotation/VAR_084547|||http://purl.uniprot.org/annotation/VAR_084548|||http://purl.uniprot.org/annotation/VSP_011501|||http://purl.uniprot.org/annotation/VSP_043225|||http://purl.uniprot.org/annotation/VSP_043226|||http://purl.uniprot.org/annotation/VSP_043227
http://togogenome.org/gene/9606:DPPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7J5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Developmental pluripotency-associated protein 2|||Disordered|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239263|||http://purl.uniprot.org/annotation/VAR_028087
http://togogenome.org/gene/9606:FXYD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14802                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glutathionylation but does not affect interaction with ATP1B1; when associated with S-43; S-49 and S-61.|||Abolishes glutathionylation but does not affect interaction with ATP1B1; when associated with S-43; S-49 and S-63.|||Abolishes glutathionylation but does not affect interaction with ATP1B1; when associated with S-43; S-61 and S-63.|||Abolishes glutathionylation but does not affect interaction with ATP1B1; when associated with S-49; S-61 and S-63.|||Cytoplasmic|||Disordered|||Extracellular|||FXYD domain-containing ion transport regulator 3|||Helical|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010362|||http://purl.uniprot.org/annotation/VAR_049109|||http://purl.uniprot.org/annotation/VSP_034598|||http://purl.uniprot.org/annotation/VSP_045716|||http://purl.uniprot.org/annotation/VSP_047286|||http://purl.uniprot.org/annotation/VSP_047287
http://togogenome.org/gene/9606:PPP2R1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30154                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HEAT 1|||HEAT 10|||HEAT 11|||HEAT 12|||HEAT 13|||HEAT 14|||HEAT 15|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In a colon adenocarcinoma.|||In a colorectal cancer patient.|||In a lung cancer patient.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-acetylalanine|||Removed|||Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071403|||http://purl.uniprot.org/annotation/VAR_006384|||http://purl.uniprot.org/annotation/VAR_022895|||http://purl.uniprot.org/annotation/VAR_022896|||http://purl.uniprot.org/annotation/VAR_022897|||http://purl.uniprot.org/annotation/VAR_022898|||http://purl.uniprot.org/annotation/VAR_022899|||http://purl.uniprot.org/annotation/VAR_022900|||http://purl.uniprot.org/annotation/VAR_022901|||http://purl.uniprot.org/annotation/VAR_022902|||http://purl.uniprot.org/annotation/VAR_022903|||http://purl.uniprot.org/annotation/VAR_022904|||http://purl.uniprot.org/annotation/VAR_022905|||http://purl.uniprot.org/annotation/VAR_022906|||http://purl.uniprot.org/annotation/VSP_036460|||http://purl.uniprot.org/annotation/VSP_043379|||http://purl.uniprot.org/annotation/VSP_045275|||http://purl.uniprot.org/annotation/VSP_046684
http://togogenome.org/gene/9606:SERTAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GC0|||http://purl.uniprot.org/uniprot/Q9UHV2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||SERTA|||SERTA domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191611|||http://purl.uniprot.org/annotation/VAR_015881
http://togogenome.org/gene/9606:PLEKHG5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804EMX3|||http://purl.uniprot.org/uniprot/O94827                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||DH|||Disordered|||In CMTRIC; in vitro assay suggests a defect in activating the NF-kappa-B signaling pathway.|||In DSMA4; stability and intracellular location affected severely impairing the NF-kappa-B transduction pathway.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family G member 5|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307134|||http://purl.uniprot.org/annotation/VAR_035357|||http://purl.uniprot.org/annotation/VAR_070217|||http://purl.uniprot.org/annotation/VAR_070218|||http://purl.uniprot.org/annotation/VSP_060959|||http://purl.uniprot.org/annotation/VSP_060960|||http://purl.uniprot.org/annotation/VSP_060961|||http://purl.uniprot.org/annotation/VSP_060962
http://togogenome.org/gene/9606:TMEM171                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVE6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Polar residues|||Transmembrane protein 171                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249570|||http://purl.uniprot.org/annotation/VAR_057003|||http://purl.uniprot.org/annotation/VAR_057004|||http://purl.uniprot.org/annotation/VAR_057005|||http://purl.uniprot.org/annotation/VSP_020520
http://togogenome.org/gene/9606:UGT2A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWM9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase 2A3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299146
http://togogenome.org/gene/9606:ITSN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8W8|||http://purl.uniprot.org/uniprot/Q9NZM3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||DH|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EH|||EH 1|||EH 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Intersectin-2|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 3|||SH3 4|||SH3 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080961|||http://purl.uniprot.org/annotation/VAR_020193|||http://purl.uniprot.org/annotation/VAR_021937|||http://purl.uniprot.org/annotation/VAR_024287|||http://purl.uniprot.org/annotation/VAR_024288|||http://purl.uniprot.org/annotation/VSP_003892|||http://purl.uniprot.org/annotation/VSP_003893|||http://purl.uniprot.org/annotation/VSP_003894|||http://purl.uniprot.org/annotation/VSP_003895
http://togogenome.org/gene/9606:C1QTNF7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXJ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 7|||Disordered|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003539|||http://purl.uniprot.org/annotation/VSP_046778
http://togogenome.org/gene/9606:PTCH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6C5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In BCNS; unknown pathological significance; does not inhibit cell growth when overexpressed in vitro.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protein patched homolog 2|||SSD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205970|||http://purl.uniprot.org/annotation/VAR_018935|||http://purl.uniprot.org/annotation/VAR_018936|||http://purl.uniprot.org/annotation/VAR_018937|||http://purl.uniprot.org/annotation/VAR_018938|||http://purl.uniprot.org/annotation/VAR_018939|||http://purl.uniprot.org/annotation/VAR_018940|||http://purl.uniprot.org/annotation/VAR_050466|||http://purl.uniprot.org/annotation/VAR_081391|||http://purl.uniprot.org/annotation/VSP_004542
http://togogenome.org/gene/9606:MMP17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Motif|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cysteine switch|||Disordered|||GPI-anchor amidated serine|||Hemopexin 1|||Hemopexin 2|||Hemopexin 3|||Hemopexin 4|||In isoform Short.|||Matrix metalloproteinase-17|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028818|||http://purl.uniprot.org/annotation/PRO_0000028819|||http://purl.uniprot.org/annotation/PRO_0000028820|||http://purl.uniprot.org/annotation/VSP_005456
http://togogenome.org/gene/9606:CD80                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0N0P2|||http://purl.uniprot.org/uniprot/P33681                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||T-lymphocyte activation antigen CD80                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014547|||http://purl.uniprot.org/annotation/PRO_5014296554|||http://purl.uniprot.org/annotation/VSP_047698|||http://purl.uniprot.org/annotation/VSP_047699|||http://purl.uniprot.org/annotation/VSP_047700
http://togogenome.org/gene/9606:H2BC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99879                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2B type 1-M|||In a colorectal cancer sample; somatic mutation.|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071831|||http://purl.uniprot.org/annotation/VAR_036205
http://togogenome.org/gene/9606:FGF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3L649|||http://purl.uniprot.org/uniprot/Q9NP95                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Fibroblast growth factor 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147616|||http://purl.uniprot.org/annotation/VAR_020946|||http://purl.uniprot.org/annotation/VAR_020947|||http://purl.uniprot.org/annotation/VAR_020948
http://togogenome.org/gene/9606:SYT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9I0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2 1|||C2 2|||Cytoplasmic|||Disordered|||Helical|||In CMS7A.|||In CMS7B.|||N-linked (GlcNAc...) asparagine|||Phospholipid binding|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Synaptotagmin-2|||Vesicular                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183942|||http://purl.uniprot.org/annotation/VAR_072578|||http://purl.uniprot.org/annotation/VAR_072579|||http://purl.uniprot.org/annotation/VAR_086137|||http://purl.uniprot.org/annotation/VAR_086138|||http://purl.uniprot.org/annotation/VAR_086139|||http://purl.uniprot.org/annotation/VAR_086140
http://togogenome.org/gene/9606:CBLN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTU7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  C1q|||Cerebellin-4|||Interchain|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003556
http://togogenome.org/gene/9606:RASA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15283                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Btk-type|||C2 1|||C2 2|||Disordered|||In isoform 2.|||N-acetylalanine|||PH|||Phosphoserine|||Ras GTPase-activating protein 2|||Ras-GAP|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056638|||http://purl.uniprot.org/annotation/VSP_046545
http://togogenome.org/gene/9606:DAW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKH6|||http://purl.uniprot.org/uniprot/B4DX89|||http://purl.uniprot.org/uniprot/Q8N136                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dynein assembly factor with WD repeat domains 1|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Probable disease-associated variant found in a patient with congenital heart disease.|||Probable disease-associated variant found in a patient with congenital heart disease; decreased protein stability.|||Probable disease-associated variant found in a patient with congenital heart disease; partial loss of function.|||Probable disease-associated variant found in a patient with heterotaxy presented in infancy; decreased ODA assembly to ciliary axonemes in respiratory cells.|||Probable disease-associated variant found in patients with mild primary ciliary dyskinesia; loss of function; multiciliated respiratory cells show a subtle reduction of the beating amplitude; slightly decreased protein stability; normal ODA assembly to ciliary axonemes in respiratory cells.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242654|||http://purl.uniprot.org/annotation/VAR_026853|||http://purl.uniprot.org/annotation/VAR_026854|||http://purl.uniprot.org/annotation/VAR_033811|||http://purl.uniprot.org/annotation/VAR_033812|||http://purl.uniprot.org/annotation/VAR_035891|||http://purl.uniprot.org/annotation/VAR_088355|||http://purl.uniprot.org/annotation/VAR_088356|||http://purl.uniprot.org/annotation/VAR_088357|||http://purl.uniprot.org/annotation/VAR_088358|||http://purl.uniprot.org/annotation/VAR_088359|||http://purl.uniprot.org/annotation/VSP_019460|||http://purl.uniprot.org/annotation/VSP_019461
http://togogenome.org/gene/9606:SLC2A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11168|||http://purl.uniprot.org/uniprot/Q6PAU8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In FBS.|||In NIDDM; abolishes transport activity of the transporter expressed in Xenopus oocytes.|||In isoform 2.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Reduced fructose transport.|||Solute carrier family 2, facilitated glucose transporter member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050346|||http://purl.uniprot.org/annotation/VAR_007169|||http://purl.uniprot.org/annotation/VAR_014718|||http://purl.uniprot.org/annotation/VAR_014719|||http://purl.uniprot.org/annotation/VAR_014720|||http://purl.uniprot.org/annotation/VAR_018650|||http://purl.uniprot.org/annotation/VAR_018651|||http://purl.uniprot.org/annotation/VAR_018652|||http://purl.uniprot.org/annotation/VAR_018653|||http://purl.uniprot.org/annotation/VAR_052501|||http://purl.uniprot.org/annotation/VSP_054835
http://togogenome.org/gene/9606:MID2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJV3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1; degenerate|||B box-type 2|||B30.2/SPRY|||COS|||Fibronectin type-III|||In XLID101; the mutant is abnormally localized in aggregates or enclosed in cytoplasmic vesicles rather than being bound to microtubules.|||In isoform 2.|||Probable E3 ubiquitin-protein ligase MID2|||RING-type|||The protein is normally bound to microtubules.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056193|||http://purl.uniprot.org/annotation/VAR_052123|||http://purl.uniprot.org/annotation/VAR_071835|||http://purl.uniprot.org/annotation/VAR_071836|||http://purl.uniprot.org/annotation/VSP_009009
http://togogenome.org/gene/9606:EIF2B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUP5|||http://purl.uniprot.org/uniprot/E7ERK9|||http://purl.uniprot.org/uniprot/F8W8L6|||http://purl.uniprot.org/uniprot/Q71US4|||http://purl.uniprot.org/uniprot/Q9HBP7|||http://purl.uniprot.org/uniprot/Q9UI10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In VWM4.|||In VWM4; with ovarian failure.|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Translation initiation factor eIF-2B subunit delta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156067|||http://purl.uniprot.org/annotation/VAR_015405|||http://purl.uniprot.org/annotation/VAR_015406|||http://purl.uniprot.org/annotation/VAR_015407|||http://purl.uniprot.org/annotation/VAR_015408|||http://purl.uniprot.org/annotation/VAR_016843|||http://purl.uniprot.org/annotation/VAR_016844|||http://purl.uniprot.org/annotation/VAR_048918|||http://purl.uniprot.org/annotation/VAR_068455|||http://purl.uniprot.org/annotation/VAR_068456|||http://purl.uniprot.org/annotation/VSP_001433|||http://purl.uniprot.org/annotation/VSP_040130
http://togogenome.org/gene/9606:IRGM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4Y4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished GTPase activity, preventing interaction with STX17 and/or NLRP3.|||IRG-type G|||Immunity-related GTPase family M protein|||In isoform IRGMb.|||In isoform IRGMc.|||In isoform IRGMd.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325749|||http://purl.uniprot.org/annotation/VAR_039899|||http://purl.uniprot.org/annotation/VAR_039900|||http://purl.uniprot.org/annotation/VSP_061869|||http://purl.uniprot.org/annotation/VSP_061870|||http://purl.uniprot.org/annotation/VSP_061871
http://togogenome.org/gene/9606:ANXA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z2Z6|||http://purl.uniprot.org/uniprot/P08133                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Annexin 1|||Annexin 2|||Annexin 3|||Annexin 4|||Annexin 5|||Annexin 6|||Annexin 7|||Annexin 8|||Annexin A6|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067494|||http://purl.uniprot.org/annotation/VSP_045480
http://togogenome.org/gene/9606:ENO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13929                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Beta-enolase|||In GSD13; when associated with D-156.|||In GSD13; when associated with E-374.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton acceptor|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000134107|||http://purl.uniprot.org/annotation/VAR_020618|||http://purl.uniprot.org/annotation/VAR_020619|||http://purl.uniprot.org/annotation/VAR_020620|||http://purl.uniprot.org/annotation/VAR_020621|||http://purl.uniprot.org/annotation/VSP_037752|||http://purl.uniprot.org/annotation/VSP_037753
http://togogenome.org/gene/9606:ZNF627                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L945                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 627                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280425
http://togogenome.org/gene/9606:KANSL1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AUZ9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||KAT8 regulatory NSL complex subunit 1-like protein|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319582|||http://purl.uniprot.org/annotation/VSP_031497|||http://purl.uniprot.org/annotation/VSP_031498|||http://purl.uniprot.org/annotation/VSP_031499|||http://purl.uniprot.org/annotation/VSP_031500|||http://purl.uniprot.org/annotation/VSP_031501
http://togogenome.org/gene/9606:TEDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L2K0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphoserine|||Polar residues|||Tubulin epsilon and delta complex protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286557|||http://purl.uniprot.org/annotation/VAR_032115|||http://purl.uniprot.org/annotation/VSP_025086|||http://purl.uniprot.org/annotation/VSP_025087|||http://purl.uniprot.org/annotation/VSP_025088
http://togogenome.org/gene/9606:SCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75880                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||Important for dimerization|||In MC4DN4; no effect on synthesis of cytochrome c oxidase subunit II; reduced stability of newly synthesized cytochrome c oxidase subunit II; reduced copper-binding.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||Protein SCO1 homolog, mitochondrial|||Redox-active                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031921|||http://purl.uniprot.org/annotation/VAR_012109|||http://purl.uniprot.org/annotation/VAR_014537
http://togogenome.org/gene/9606:PAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00439                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ACT|||In HPA and PKU.|||In HPA and PKU; does not affect oligomerization; results in loss of substrate activation.|||In HPA and PKU; haplotype 1.|||In HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In HPA and PKU; haplotypes 1,2,4,5,13,34,41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In HPA and PKU; mild; haplotypes 1,2,4,22, 24,28.|||In HPA.|||In HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In PKU and non-PKUHPA; haplotype 4.|||In PKU, HPA and non-PKUHPA; haplotype 1.|||In PKU, HPA and non-PKUHPA; haplotypes 3,7.|||In PKU.|||In PKU; does not affect oligomerization.|||In PKU; haplotype 1.|||In PKU; haplotype 10.|||In PKU; haplotype 11.|||In PKU; haplotype 12.|||In PKU; haplotype 1; abolishes phenylalanine binding.|||In PKU; haplotype 2.|||In PKU; haplotype 21.|||In PKU; haplotype 28.|||In PKU; haplotype 3.|||In PKU; haplotype 36.|||In PKU; haplotype 4.|||In PKU; haplotype 5.|||In PKU; haplotype 5; significantly reduces phenylalanine binding.|||In PKU; haplotype 6.|||In PKU; haplotype 7.|||In PKU; haplotype 8.|||In PKU; haplotypes 1,2,4,16,38; partial residual activity.|||In PKU; haplotypes 1,2,4,7,16, 28.|||In PKU; haplotypes 1,2,7.|||In PKU; haplotypes 1,2.|||In PKU; haplotypes 1,4.|||In PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding.|||In PKU; haplotypes 1,5.|||In PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity.|||In PKU; haplotypes 1,7,10.|||In PKU; haplotypes 1,8.|||In PKU; haplotypes 18,21.|||In PKU; haplotypes 2,3.|||In PKU; haplotypes 3,4.|||In PKU; haplotypes 4,12.|||In PKU; haplotypes 7,42.|||In PKU; haplotypes 9,21.|||In PKU; mild haplotype 9.|||In PKU; mild.|||In PKU; mild; haplotype 1.|||In PKU; mild; haplotype 2.|||In PKU; mild; haplotypes 3,4.|||In PKU; partial loss of activity.|||In PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity.|||In PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery.|||In PKU; results in disturbed oligomerization; results in loss of substrate activation.|||In PKU; severe.|||In PKU; severe; 5% activity; requires 2 nucleotide substitutions.|||In PKU; severe; haplotype 4.|||In PKU; unknown pathological significance.|||In non-PKUHPA and PKU.|||In non-PKUHPA and PKU; haplotype 34.|||In non-PKUHPA and PKU; haplotype 4.|||In non-PKUHPA and PKU; haplotype 43.|||In non-PKUHPA and PKU; haplotypes 4,7,9.|||In non-PKUHPA.|||In non-PKUHPA; haplotype 1.|||In non-PKUHPA; haplotype 4; significantly reduces phenylalanine binding.|||Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.|||Phenylalanine-4-hydroxylase|||Phosphoserine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205548|||http://purl.uniprot.org/annotation/VAR_000869|||http://purl.uniprot.org/annotation/VAR_000870|||http://purl.uniprot.org/annotation/VAR_000871|||http://purl.uniprot.org/annotation/VAR_000872|||http://purl.uniprot.org/annotation/VAR_000873|||http://purl.uniprot.org/annotation/VAR_000874|||http://purl.uniprot.org/annotation/VAR_000875|||http://purl.uniprot.org/annotation/VAR_000876|||http://purl.uniprot.org/annotation/VAR_000877|||http://purl.uniprot.org/annotation/VAR_000878|||http://purl.uniprot.org/annotation/VAR_000879|||http://purl.uniprot.org/annotation/VAR_000880|||http://purl.uniprot.org/annotation/VAR_000881|||http://purl.uniprot.org/annotation/VAR_000882|||http://purl.uniprot.org/annotation/VAR_000883|||http://purl.uniprot.org/annotation/VAR_000884|||http://purl.uniprot.org/annotation/VAR_000885|||http://purl.uniprot.org/annotation/VAR_000886|||http://purl.uniprot.org/annotation/VAR_000887|||http://purl.uniprot.org/annotation/VAR_000888|||http://purl.uniprot.org/annotation/VAR_000889|||http://purl.uniprot.org/annotation/VAR_000890|||http://purl.uniprot.org/annotation/VAR_000891|||http://purl.uniprot.org/annotation/VAR_000892|||http://purl.uniprot.org/annotation/VAR_000893|||http://purl.uniprot.org/annotation/VAR_000894|||http://purl.uniprot.org/annotation/VAR_000895|||http://purl.uniprot.org/annotation/VAR_000896|||http://purl.uniprot.org/annotation/VAR_000897|||http://purl.uniprot.org/annotation/VAR_000898|||http://purl.uniprot.org/annotation/VAR_000899|||http://purl.uniprot.org/annotation/VAR_000900|||http://purl.uniprot.org/annotation/VAR_000901|||http://purl.uniprot.org/annotation/VAR_000902|||http://purl.uniprot.org/annotation/VAR_000903|||http://purl.uniprot.org/annotation/VAR_000904|||http://purl.uniprot.org/annotation/VAR_000905|||http://purl.uniprot.org/annotation/VAR_000906|||http://purl.uniprot.org/annotation/VAR_000907|||http://purl.uniprot.org/annotation/VAR_000908|||http://purl.uniprot.org/annotation/VAR_000909|||http://purl.uniprot.org/annotation/VAR_000910|||http://purl.uniprot.org/annotation/VAR_000911|||http://purl.uniprot.org/annotation/VAR_000912|||http://purl.uniprot.org/annotation/VAR_000913|||http://purl.uniprot.org/annotation/VAR_000914|||http://purl.uniprot.org/annotation/VAR_000915|||http://purl.uniprot.org/annotation/VAR_000916|||http://purl.uniprot.org/annotation/VAR_000917|||http://purl.uniprot.org/annotation/VAR_000918|||http://purl.uniprot.org/annotation/VAR_000922|||http://purl.uniprot.org/annotation/VAR_000923|||http://purl.uniprot.org/annotation/VAR_000924|||http://purl.uniprot.org/annotation/VAR_000925|||http://purl.uniprot.org/annotation/VAR_000926|||http://purl.uniprot.org/annotation/VAR_000927|||http://purl.uniprot.org/annotation/VAR_000928|||http://purl.uniprot.org/annotation/VAR_000929|||http://purl.uniprot.org/annotation/VAR_000930|||http://purl.uniprot.org/annotation/VAR_000931|||http://purl.uniprot.org/annotation/VAR_000932|||http://purl.uniprot.org/annotation/VAR_000933|||http://purl.uniprot.org/annotation/VAR_000934|||http://purl.uniprot.org/annotation/VAR_000935|||http://purl.uniprot.org/annotation/VAR_000936|||http://purl.uniprot.org/annotation/VAR_000937|||http://purl.uniprot.org/annotation/VAR_000938|||http://purl.uniprot.org/annotation/VAR_000939|||http://purl.uniprot.org/annotation/VAR_000940|||http://purl.uniprot.org/annotation/VAR_000941|||http://purl.uniprot.org/annotation/VAR_000942|||http://purl.uniprot.org/annotation/VAR_000943|||http://purl.uniprot.org/annotation/VAR_000944|||http://purl.uniprot.org/annotation/VAR_000945|||http://purl.uniprot.org/annotation/VAR_000946|||http://purl.uniprot.org/annotation/VAR_000947|||http://purl.uniprot.org/annotation/VAR_000948|||http://purl.uniprot.org/annotation/VAR_000949|||http://purl.uniprot.org/annotation/VAR_000950|||http://purl.uniprot.org/annotation/VAR_000951|||http://purl.uniprot.org/annotation/VAR_000952|||http://purl.uniprot.org/annotation/VAR_000953|||http://purl.uniprot.org/annotation/VAR_000954|||http://purl.uniprot.org/annotation/VAR_000955|||http://purl.uniprot.org/annotation/VAR_000956|||http://purl.uniprot.org/annotation/VAR_000957|||http://purl.uniprot.org/annotation/VAR_000958|||http://purl.uniprot.org/annotation/VAR_000959|||http://purl.uniprot.org/annotation/VAR_000960|||http://purl.uniprot.org/annotation/VAR_000961|||http://purl.uniprot.org/annotation/VAR_000962|||http://purl.uniprot.org/annotation/VAR_000963|||http://purl.uniprot.org/annotation/VAR_000964|||http://purl.uniprot.org/annotation/VAR_000965|||http://purl.uniprot.org/annotation/VAR_000966|||http://purl.uniprot.org/annotation/VAR_000967|||http://purl.uniprot.org/annotation/VAR_000968|||http://purl.uniprot.org/annotation/VAR_000969|||http://purl.uniprot.org/annotation/VAR_000970|||http://purl.uniprot.org/annotation/VAR_000971|||http://purl.uniprot.org/annotation/VAR_000972|||http://purl.uniprot.org/annotation/VAR_000973|||http://purl.uniprot.org/annotation/VAR_000974|||http://purl.uniprot.org/annotation/VAR_000975|||http://purl.uniprot.org/annotation/VAR_000976|||http://purl.uniprot.org/annotation/VAR_000977|||http://purl.uniprot.org/annotation/VAR_000978|||http://purl.uniprot.org/annotation/VAR_000979|||http://purl.uniprot.org/annotation/VAR_000980|||http://purl.uniprot.org/annotation/VAR_000981|||http://purl.uniprot.org/annotation/VAR_000982|||http://purl.uniprot.org/annotation/VAR_000983|||http://purl.uniprot.org/annotation/VAR_000984|||http://purl.uniprot.org/annotation/VAR_000985|||http://purl.uniprot.org/annotation/VAR_000986|||http://purl.uniprot.org/annotation/VAR_000987|||http://purl.uniprot.org/annotation/VAR_000988|||http://purl.uniprot.org/annotation/VAR_000989|||http://purl.uniprot.org/annotation/VAR_000990|||http://purl.uniprot.org/annotation/VAR_000991|||http://purl.uniprot.org/annotation/VAR_000992|||http://purl.uniprot.org/annotation/VAR_000993|||http://purl.uniprot.org/annotation/VAR_000994|||http://purl.uniprot.org/annotation/VAR_000995|||http://purl.uniprot.org/annotation/VAR_000996|||http://purl.uniprot.org/annotation/VAR_000997|||http://purl.uniprot.org/annotation/VAR_000998|||http://purl.uniprot.org/annotation/VAR_000999|||http://purl.uniprot.org/annotation/VAR_001000|||http://purl.uniprot.org/annotation/VAR_001001|||http://purl.uniprot.org/annotation/VAR_001002|||http://purl.uniprot.org/annotation/VAR_001003|||http://purl.uniprot.org/annotation/VAR_001004|||http://purl.uniprot.org/annotation/VAR_001005|||http://purl.uniprot.org/annotation/VAR_001006|||http://purl.uniprot.org/annotation/VAR_001007|||http://purl.uniprot.org/annotation/VAR_001008|||http://purl.uniprot.org/annotation/VAR_001009|||http://purl.uniprot.org/annotation/VAR_001010|||http://purl.uniprot.org/annotation/VAR_001011|||http://purl.uniprot.org/annotation/VAR_001012|||http://purl.uniprot.org/annotation/VAR_001013|||http://purl.uniprot.org/annotation/VAR_001014|||http://purl.uniprot.org/annotation/VAR_001015|||http://purl.uniprot.org/annotation/VAR_001016|||http://purl.uniprot.org/annotation/VAR_001017|||http://purl.uniprot.org/annotation/VAR_001018|||http://purl.uniprot.org/annotation/VAR_001019|||http://purl.uniprot.org/annotation/VAR_001020|||http://purl.uniprot.org/annotation/VAR_001021|||http://purl.uniprot.org/annotation/VAR_001022|||http://purl.uniprot.org/annotation/VAR_001023|||http://purl.uniprot.org/annotation/VAR_001024|||http://purl.uniprot.org/annotation/VAR_001025|||http://purl.uniprot.org/annotation/VAR_001026|||http://purl.uniprot.org/annotation/VAR_001027|||http://purl.uniprot.org/annotation/VAR_001028|||http://purl.uniprot.org/annotation/VAR_001029|||http://purl.uniprot.org/annotation/VAR_001030|||http://purl.uniprot.org/annotation/VAR_001031|||http://purl.uniprot.org/annotation/VAR_001033|||http://purl.uniprot.org/annotation/VAR_001034|||http://purl.uniprot.org/annotation/VAR_001035|||http://purl.uniprot.org/annotation/VAR_001036|||http://purl.uniprot.org/annotation/VAR_001037|||http://purl.uniprot.org/annotation/VAR_001038|||http://purl.uniprot.org/annotation/VAR_001039|||http://purl.uniprot.org/annotation/VAR_001040|||http://purl.uniprot.org/annotation/VAR_001041|||http://purl.uniprot.org/annotation/VAR_001042|||http://purl.uniprot.org/annotation/VAR_009239|||http://purl.uniprot.org/annotation/VAR_009240|||http://purl.uniprot.org/annotation/VAR_009241|||http://purl.uniprot.org/annotation/VAR_009242|||http://purl.uniprot.org/annotation/VAR_009243|||http://purl.uniprot.org/annotation/VAR_009244|||http://purl.uniprot.org/annotation/VAR_009245|||http://purl.uniprot.org/annotation/VAR_009246|||http://purl.uniprot.org/annotation/VAR_009247|||http://purl.uniprot.org/annotation/VAR_009248|||http://purl.uniprot.org/annotation/VAR_009249|||http://purl.uniprot.org/annotation/VAR_011566|||http://purl.uniprot.org/annotation/VAR_011567|||http://purl.uniprot.org/annotation/VAR_011568|||http://purl.uniprot.org/annotation/VAR_011569|||http://purl.uniprot.org/annotation/VAR_011570|||http://purl.uniprot.org/annotation/VAR_011571|||http://purl.uniprot.org/annotation/VAR_011572|||http://purl.uniprot.org/annotation/VAR_011573|||http://purl.uniprot.org/annotation/VAR_011574|||http://purl.uniprot.org/annotation/VAR_011575|||http://purl.uniprot.org/annotation/VAR_011576|||http://purl.uniprot.org/annotation/VAR_067758|||http://purl.uniprot.org/annotation/VAR_067759|||http://purl.uniprot.org/annotation/VAR_067760|||http://purl.uniprot.org/annotation/VAR_067994|||http://purl.uniprot.org/annotation/VAR_067995|||http://purl.uniprot.org/annotation/VAR_067996|||http://purl.uniprot.org/annotation/VAR_067997|||http://purl.uniprot.org/annotation/VAR_067998|||http://purl.uniprot.org/annotation/VAR_067999|||http://purl.uniprot.org/annotation/VAR_068000|||http://purl.uniprot.org/annotation/VAR_068001|||http://purl.uniprot.org/annotation/VAR_068002|||http://purl.uniprot.org/annotation/VAR_068003|||http://purl.uniprot.org/annotation/VAR_068004|||http://purl.uniprot.org/annotation/VAR_068005|||http://purl.uniprot.org/annotation/VAR_068006|||http://purl.uniprot.org/annotation/VAR_068007|||http://purl.uniprot.org/annotation/VAR_068008|||http://purl.uniprot.org/annotation/VAR_069776|||http://purl.uniprot.org/annotation/VAR_069777
http://togogenome.org/gene/9606:ZMAT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H898                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Matrin-type 4|||Zinc finger matrin-type protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298916|||http://purl.uniprot.org/annotation/VAR_034736|||http://purl.uniprot.org/annotation/VSP_027476
http://togogenome.org/gene/9606:IQCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6M8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IQ 1|||IQ 2|||IQ domain-containing protein F1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282556|||http://purl.uniprot.org/annotation/VAR_031414|||http://purl.uniprot.org/annotation/VAR_055096|||http://purl.uniprot.org/annotation/VSP_024184|||http://purl.uniprot.org/annotation/VSP_024185
http://togogenome.org/gene/9606:DIO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92813                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Non standard residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Selenocysteine|||Type II iodothyronine deiodinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154317|||http://purl.uniprot.org/annotation/VAR_047549|||http://purl.uniprot.org/annotation/VAR_049640|||http://purl.uniprot.org/annotation/VSP_026154|||http://purl.uniprot.org/annotation/VSP_060028|||http://purl.uniprot.org/annotation/VSP_060029|||http://purl.uniprot.org/annotation/VSP_060030
http://togogenome.org/gene/9606:BFSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z999|||http://purl.uniprot.org/uniprot/B7ZAD2|||http://purl.uniprot.org/uniprot/Q12934                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage by CASP2.|||Basic and acidic residues|||Cleavage|||Cleavage (by CASP2, CASP3, and CASP7)|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Filensin|||Filensin C-terminal fragment|||Filensin N-terminal fragment|||Head|||IF rod|||In CTRCT33.|||In isoform 2.|||In isoform 3.|||Interaction with MIP|||Linker 1|||Linker 12|||N-acetylalanine|||N-myristoyl glycine|||No effect on cleavage.|||Phosphoserine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063847|||http://purl.uniprot.org/annotation/PRO_0000448670|||http://purl.uniprot.org/annotation/PRO_0000448671|||http://purl.uniprot.org/annotation/VAR_024492|||http://purl.uniprot.org/annotation/VAR_036683|||http://purl.uniprot.org/annotation/VAR_078861|||http://purl.uniprot.org/annotation/VSP_024921|||http://purl.uniprot.org/annotation/VSP_024922|||http://purl.uniprot.org/annotation/VSP_055064
http://togogenome.org/gene/9606:LGALS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17931                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  1|||2|||3|||4; approximate|||5|||6; approximate|||7; approximate|||8 X 9 AA tandem repeats of Y-P-G-X(3)-P-G-A|||8; approximate|||Disordered|||Galectin|||Galectin-3|||Interchain|||N-acetylalanine|||Nuclear export signal|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076930|||http://purl.uniprot.org/annotation/VAR_012988|||http://purl.uniprot.org/annotation/VAR_012989|||http://purl.uniprot.org/annotation/VAR_049768
http://togogenome.org/gene/9606:RD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3Z2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Does not affect ability to suppress GUCY2D activity induced by GCAPA.|||Does not affect affinity of RD3 for GUCY2D.|||In an individual with an atypical late-onset form of retinitis pigmentosa.|||In an individual with an atypical late-onset form of retinitis pigmentosa; does not affect ability to suppress GUCY2D activity induced by GCAPA.|||In an individual with cone-rod degeneration; abolishes protein expression; less effective in suppressing GUCY2D activity by GCAPA.|||In an individual with cone-rod dystrophy features; less effective in suppressing GUCY2D activity by GCAPA.|||Increased the affinity of RD3 for GUCY2D.|||Less effective in suppressing GUCY2D activity induced by GCAPA.|||Protein RD3|||Reduced RD3 affinity for GUCY2D by 80-fold.|||Reduced the affinity of RD3 for GUCY2D.|||Strongly affects RD3 ability to suppress GUCY2D activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089248|||http://purl.uniprot.org/annotation/VAR_023050|||http://purl.uniprot.org/annotation/VAR_031510|||http://purl.uniprot.org/annotation/VAR_031511|||http://purl.uniprot.org/annotation/VAR_031512|||http://purl.uniprot.org/annotation/VAR_031513|||http://purl.uniprot.org/annotation/VAR_031514|||http://purl.uniprot.org/annotation/VAR_031515|||http://purl.uniprot.org/annotation/VAR_031516|||http://purl.uniprot.org/annotation/VAR_031517
http://togogenome.org/gene/9606:CLDN10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78369                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-10|||Cytoplasmic|||Extracellular|||Helical|||In HELIX; decreased function in regulation of paracellular ion transport as shown by reduced sodium permeability of cell layers expressing the mutant; affects self-interaction by inhibiting homodimerization in trans and promoting homodimerization in cis; no effect on localization to plasma membrane.|||In HELIX; strongly reduced localization at the plasma membrane.|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144757|||http://purl.uniprot.org/annotation/VAR_080053|||http://purl.uniprot.org/annotation/VAR_080054|||http://purl.uniprot.org/annotation/VSP_042898|||http://purl.uniprot.org/annotation/VSP_053550
http://togogenome.org/gene/9606:MTNR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48039                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Exhibits significantly reduced B(max) and slightly enhanced affinity.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melatonin receptor type 1A|||N-linked (GlcNAc...) asparagine|||Similar binding characteristics compared to wild-type.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069862|||http://purl.uniprot.org/annotation/VAR_009260|||http://purl.uniprot.org/annotation/VAR_009261|||http://purl.uniprot.org/annotation/VAR_049420
http://togogenome.org/gene/9606:TM9SF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3A9|||http://purl.uniprot.org/uniprot/G3V1B9|||http://purl.uniprot.org/uniprot/O15321                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane 9 superfamily member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034361|||http://purl.uniprot.org/annotation/VAR_024662|||http://purl.uniprot.org/annotation/VAR_053728|||http://purl.uniprot.org/annotation/VSP_042781
http://togogenome.org/gene/9606:TRMT12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53H54                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Does not affect activity.|||Lack of activity.|||tRNA wybutosine-synthesizing protein 2 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281836|||http://purl.uniprot.org/annotation/VAR_031291
http://togogenome.org/gene/9606:HMGCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01581                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-thioester intermediate|||Disordered|||Hydroxymethylglutaryl-CoA synthase, cytoplasmic|||Loss of activity.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213747
http://togogenome.org/gene/9606:EGFL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHF1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Disrupts RGD motif and results in a 79% loss of cell adhesion.|||EGF-like 1|||EGF-like 2; calcium-binding|||EMI|||Epidermal growth factor-like protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007528|||http://purl.uniprot.org/annotation/VAR_019791|||http://purl.uniprot.org/annotation/VAR_048981|||http://purl.uniprot.org/annotation/VAR_048982|||http://purl.uniprot.org/annotation/VAR_070951
http://togogenome.org/gene/9606:CCNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8S5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-P|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263704|||http://purl.uniprot.org/annotation/VSP_044165|||http://purl.uniprot.org/annotation/VSP_044166|||http://purl.uniprot.org/annotation/VSP_044167
http://togogenome.org/gene/9606:GTF2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52655                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes cleavage.|||Acidic residues|||Cleavage; by TASP1|||Disordered|||Does not affect cleavage.|||Eliminates phosphorylation; when associated with A-280; A-316 and A-321.|||In a breast cancer sample; somatic mutation.|||In isoform 37 kDa.|||N-acetylalanine|||Phosphoserine; by TAF1|||Polar residues|||Removed|||Significant reduction of cleavage.|||Slightly affects cleavage and yields elevated levels of the precursor.|||Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321.|||Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316.|||Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321.|||Transcription initiation factor IIA alpha chain|||Transcription initiation factor IIA beta chain|||Transcription initiation factor IIA subunit 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022481|||http://purl.uniprot.org/annotation/PRO_0000042593|||http://purl.uniprot.org/annotation/PRO_0000042594|||http://purl.uniprot.org/annotation/VAR_035667|||http://purl.uniprot.org/annotation/VAR_054043|||http://purl.uniprot.org/annotation/VSP_018798
http://togogenome.org/gene/9606:SPRR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Mass|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||14 X 8 AA approximate tandem repeats|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||N-acetylserine|||Polar residues|||Removed|||Small proline-rich protein 3|||Variants Del 98-Cys--Pro-105 and Val-149.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150003|||http://purl.uniprot.org/annotation/VAR_023377|||http://purl.uniprot.org/annotation/VAR_053048|||http://purl.uniprot.org/annotation/VAR_065255
http://togogenome.org/gene/9606:TXNDC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PKC3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Redox-active|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin domain-containing protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120173|||http://purl.uniprot.org/annotation/VAR_022767|||http://purl.uniprot.org/annotation/VSP_014335|||http://purl.uniprot.org/annotation/VSP_014336|||http://purl.uniprot.org/annotation/VSP_014337
http://togogenome.org/gene/9606:CNOT10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9A5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 10|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314579|||http://purl.uniprot.org/annotation/VAR_037957|||http://purl.uniprot.org/annotation/VAR_053982|||http://purl.uniprot.org/annotation/VSP_030311|||http://purl.uniprot.org/annotation/VSP_030312|||http://purl.uniprot.org/annotation/VSP_030313|||http://purl.uniprot.org/annotation/VSP_030314|||http://purl.uniprot.org/annotation/VSP_045557
http://togogenome.org/gene/9606:NFIC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4T6|||http://purl.uniprot.org/uniprot/P08651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  9aaTAD|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||CTF/NF-I|||Disordered|||In isoform 1, isoform 2 and isoform 3.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||Nuclear factor 1 C-type|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100199|||http://purl.uniprot.org/annotation/VAR_057656|||http://purl.uniprot.org/annotation/VSP_003552|||http://purl.uniprot.org/annotation/VSP_003553|||http://purl.uniprot.org/annotation/VSP_003554|||http://purl.uniprot.org/annotation/VSP_003555|||http://purl.uniprot.org/annotation/VSP_003556|||http://purl.uniprot.org/annotation/VSP_047539
http://togogenome.org/gene/9606:IL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05113                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Interchain (with C-105)|||Interchain (with C-63)|||Interleukin-5|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||O-linked (GalNAc...) threonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015560
http://togogenome.org/gene/9606:OR10A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H209                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10A4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150686|||http://purl.uniprot.org/annotation/VAR_024124|||http://purl.uniprot.org/annotation/VAR_034280|||http://purl.uniprot.org/annotation/VAR_034281|||http://purl.uniprot.org/annotation/VAR_060023
http://togogenome.org/gene/9606:MBD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P267                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MRD1; unknown pathological significance.|||In isoform 2.|||MBD|||Methyl-CpG-binding domain protein 5|||PWWP|||Polar residues|||Pro residues|||Shows diffuse nuclear pattern.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096266|||http://purl.uniprot.org/annotation/VAR_037561|||http://purl.uniprot.org/annotation/VAR_037562|||http://purl.uniprot.org/annotation/VAR_037563|||http://purl.uniprot.org/annotation/VAR_037564|||http://purl.uniprot.org/annotation/VAR_037565|||http://purl.uniprot.org/annotation/VAR_037566|||http://purl.uniprot.org/annotation/VAR_037567|||http://purl.uniprot.org/annotation/VSP_011083|||http://purl.uniprot.org/annotation/VSP_011084
http://togogenome.org/gene/9606:PRR20B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P86478|||http://purl.uniprot.org/uniprot/P86479|||http://purl.uniprot.org/uniprot/P86480|||http://purl.uniprot.org/uniprot/P86481|||http://purl.uniprot.org/uniprot/P86496                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 20A|||Proline-rich protein 20B|||Proline-rich protein 20C|||Proline-rich protein 20D|||Proline-rich protein 20E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000336092|||http://purl.uniprot.org/annotation/PRO_0000393890|||http://purl.uniprot.org/annotation/PRO_0000393891|||http://purl.uniprot.org/annotation/PRO_0000393892|||http://purl.uniprot.org/annotation/PRO_0000393893
http://togogenome.org/gene/9606:EIF4E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RBW1|||http://purl.uniprot.org/uniprot/P06730|||http://purl.uniprot.org/uniprot/Q32Q75|||http://purl.uniprot.org/uniprot/X5D7E3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Interaction with potato virus Y VPg|||Abolishes binding to EIF4EBP1. Impairs interaction with DDX3X. Does not impair mRNA nuclear export. Does not affect affinity for ribavirin.|||Abolishes resistance to cellular stress and DNA-damaging agents. Does not affect ability to rescue growth of yeast lacking a functional EIF4E/CDC33 gene.|||Basic and acidic residues|||Decrease in mRNA cap binding; when associated with A-105.|||Decrease in mRNA cap binding; when associated with L-102.|||Disordered|||Does not affect ability to rescue growth of yeast lacking a functional EIF4E/CDC33 gene.|||EIF4EBP1/2/3 binding|||Eukaryotic translation initiation factor 4E|||Higher affinity for EIF4G1.|||Impairs mRNA nuclear export. Reduces affinity for ribavirin.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||No effect on phosphorylation level nor incorporation into eIF4F complex.|||No effect.|||Phosphomimetic mutant; confers resistance to cellular stress and DNA-damaging agents. Does not affect ability to rescue growth of yeast lacking a functional EIF4E/CDC33 gene.|||Phosphoserine; by PKC and MKNK2|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193634|||http://purl.uniprot.org/annotation/VSP_042014|||http://purl.uniprot.org/annotation/VSP_043591
http://togogenome.org/gene/9606:ZNF510                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUI8|||http://purl.uniprot.org/uniprot/Q9Y2H8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 510                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047628|||http://purl.uniprot.org/annotation/VAR_019982|||http://purl.uniprot.org/annotation/VAR_021893|||http://purl.uniprot.org/annotation/VAR_052848|||http://purl.uniprot.org/annotation/VAR_052849|||http://purl.uniprot.org/annotation/VAR_052850|||http://purl.uniprot.org/annotation/VAR_052851
http://togogenome.org/gene/9606:IGFBP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24593                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IGFBP N-terminal|||Insulin-like growth factor-binding protein 5|||O-linked (HexNAc...) threonine|||Phosphoserine; by FAM20C|||Thyroglobulin type-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014385|||http://purl.uniprot.org/annotation/VAR_019284
http://togogenome.org/gene/9606:FBXW4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5X9|||http://purl.uniprot.org/uniprot/P57775                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  F-box|||F-box/WD repeat-containing protein 4|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050990
http://togogenome.org/gene/9606:CEMIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUJ3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell migration-inducing and hyaluronan-binding protein|||Does not inhibit hyaluronic acid degradation activity.|||G8|||GG-type lectin 1|||GG-type lectin 2|||In a family with non-syndromic hearing loss; reduces hyaluronic acid degradation activity.|||In a sporadic case of non-syndromic hearing loss.|||In isoform 2.|||In two unrelated families with non-syndromic hearing loss; reduces hyaluronic acid (HA) degradation activity.|||N-linked (GlcNAc...) asparagine|||Necessary for its endoplasmic reticulum (ER) retention and interaction with HSPA5|||PbH1 1|||PbH1 2|||PbH1 3|||PbH1 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021538|||http://purl.uniprot.org/annotation/VAR_018165|||http://purl.uniprot.org/annotation/VAR_018166|||http://purl.uniprot.org/annotation/VAR_018167|||http://purl.uniprot.org/annotation/VAR_018168|||http://purl.uniprot.org/annotation/VAR_018169|||http://purl.uniprot.org/annotation/VAR_018170|||http://purl.uniprot.org/annotation/VSP_009814|||http://purl.uniprot.org/annotation/VSP_009815
http://togogenome.org/gene/9606:PARG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W56                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  A-domain|||Abolished poly(ADP-ribose) glycohydrolase activity.|||Abolishes nuclear targeting; when associated with A-12.|||Abolishes nuclear targeting; when associated with G-13.|||Basic and acidic residues|||Catalytic|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||N-acetylmethionine|||N6-acetyllysine|||No effect.|||Nuclear localization signal|||PIP-box (PCNA interacting peptide)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Poly(ADP-ribose) glycohydrolase|||Reduced poly(ADP-ribose) glycohydrolase activity.|||Reduces hydrolase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066602|||http://purl.uniprot.org/annotation/VSP_011769|||http://purl.uniprot.org/annotation/VSP_011770|||http://purl.uniprot.org/annotation/VSP_044674|||http://purl.uniprot.org/annotation/VSP_044675|||http://purl.uniprot.org/annotation/VSP_044676|||http://purl.uniprot.org/annotation/VSP_044677
http://togogenome.org/gene/9606:LRRC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15048                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156974|||http://purl.uniprot.org/annotation/VAR_053603
http://togogenome.org/gene/9606:FOXR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJQ5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fork-head|||Forkhead box protein R2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253780|||http://purl.uniprot.org/annotation/VAR_028731
http://togogenome.org/gene/9606:KLRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1S0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C-type lectin|||Disordered|||Helical|||In isoform 2.|||Killer cell lectin-like receptor subfamily G member 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316792|||http://purl.uniprot.org/annotation/VAR_038396|||http://purl.uniprot.org/annotation/VAR_038397|||http://purl.uniprot.org/annotation/VSP_030779|||http://purl.uniprot.org/annotation/VSP_030780
http://togogenome.org/gene/9606:FOCAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VW36                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Focadhesin|||In SCOLIV.|||In SCOLIV; unknown pathological significance.|||In SCOLIV; unknown pathological significance; when associated with C-563.|||In SCOLIV; unknown pathological significance; when associated with P-1232.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314457|||http://purl.uniprot.org/annotation/VAR_037877|||http://purl.uniprot.org/annotation/VAR_037878|||http://purl.uniprot.org/annotation/VAR_037879|||http://purl.uniprot.org/annotation/VAR_037880|||http://purl.uniprot.org/annotation/VAR_037881|||http://purl.uniprot.org/annotation/VAR_037882|||http://purl.uniprot.org/annotation/VAR_049528|||http://purl.uniprot.org/annotation/VAR_061251|||http://purl.uniprot.org/annotation/VAR_061252|||http://purl.uniprot.org/annotation/VAR_087617|||http://purl.uniprot.org/annotation/VAR_087618|||http://purl.uniprot.org/annotation/VAR_087619|||http://purl.uniprot.org/annotation/VAR_087620|||http://purl.uniprot.org/annotation/VAR_087621|||http://purl.uniprot.org/annotation/VAR_087622|||http://purl.uniprot.org/annotation/VAR_087623|||http://purl.uniprot.org/annotation/VAR_087624
http://togogenome.org/gene/9606:ATP6V1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15313                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In DRTA2.|||In DRTA2; disruption of V-ATPase assembly resulting in loss of enzyme activity; impaired trafficking of V-ATPase to apical cell membrane; impaired renal proton secretion.|||Loss of interactions with NHERF1 and SCL4A7.|||PDZ-binding|||V-type proton ATPase subunit B, kidney isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144624|||http://purl.uniprot.org/annotation/VAR_007866|||http://purl.uniprot.org/annotation/VAR_007867|||http://purl.uniprot.org/annotation/VAR_007868|||http://purl.uniprot.org/annotation/VAR_007869|||http://purl.uniprot.org/annotation/VAR_007870|||http://purl.uniprot.org/annotation/VAR_007871|||http://purl.uniprot.org/annotation/VAR_007872|||http://purl.uniprot.org/annotation/VAR_021011|||http://purl.uniprot.org/annotation/VAR_021012|||http://purl.uniprot.org/annotation/VAR_021013|||http://purl.uniprot.org/annotation/VAR_021014|||http://purl.uniprot.org/annotation/VAR_021015|||http://purl.uniprot.org/annotation/VAR_085740
http://togogenome.org/gene/9606:POU4F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01851                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In ATITHS; decreased transcriptional activity shown in a luciferase assay.|||In isoform 2.|||POU domain, class 4, transcription factor 1|||POU-IV box|||POU-specific                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100736|||http://purl.uniprot.org/annotation/VAR_046449|||http://purl.uniprot.org/annotation/VAR_085801|||http://purl.uniprot.org/annotation/VSP_058636
http://togogenome.org/gene/9606:MRPL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IY40|||http://purl.uniprot.org/uniprot/Q5T653                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||Large ribosomal subunit protein uL2 RNA-binding|||Large ribosomal subunit protein uL2m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261640|||http://purl.uniprot.org/annotation/VAR_029470
http://togogenome.org/gene/9606:TNC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1W8|||http://purl.uniprot.org/uniprot/J3QSU6|||http://purl.uniprot.org/uniprot/P24821|||http://purl.uniprot.org/uniprot/Q4LE33                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EGF-like|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 1; incomplete|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Fibrinogen C-terminal|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||In DFNA56.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Tenascin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007741|||http://purl.uniprot.org/annotation/PRO_5002804054|||http://purl.uniprot.org/annotation/PRO_5003777214|||http://purl.uniprot.org/annotation/VAR_014665|||http://purl.uniprot.org/annotation/VAR_020169|||http://purl.uniprot.org/annotation/VAR_024266|||http://purl.uniprot.org/annotation/VAR_024267|||http://purl.uniprot.org/annotation/VAR_024268|||http://purl.uniprot.org/annotation/VAR_055778|||http://purl.uniprot.org/annotation/VAR_055779|||http://purl.uniprot.org/annotation/VAR_060738|||http://purl.uniprot.org/annotation/VAR_070984|||http://purl.uniprot.org/annotation/VAR_070985|||http://purl.uniprot.org/annotation/VSP_001412|||http://purl.uniprot.org/annotation/VSP_001413|||http://purl.uniprot.org/annotation/VSP_001414|||http://purl.uniprot.org/annotation/VSP_001415
http://togogenome.org/gene/9606:CSTPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUV7|||http://purl.uniprot.org/uniprot/Q9H6J7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Centriolar satellite-associated tubulin polyglutamylase complex regulator 1|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Required for interaction with PCM1|||Required for interaction with TPGS1, LRRC49, and TTLL1|||Required for interaction with TPGS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281425|||http://purl.uniprot.org/annotation/VSP_024000|||http://purl.uniprot.org/annotation/VSP_024001|||http://purl.uniprot.org/annotation/VSP_044902
http://togogenome.org/gene/9606:UBR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXG6|||http://purl.uniprot.org/uniprot/Q8IWV8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||E3 ubiquitin-protein ligase|||E3 ubiquitin-protein ligase UBR-like C-terminal|||E3 ubiquitin-protein ligase UBR2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Polar residues|||RING-type; atypical|||Removed|||UBR-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056140|||http://purl.uniprot.org/annotation/PRO_5002788473|||http://purl.uniprot.org/annotation/VAR_023283|||http://purl.uniprot.org/annotation/VAR_052117|||http://purl.uniprot.org/annotation/VAR_059816|||http://purl.uniprot.org/annotation/VAR_059817|||http://purl.uniprot.org/annotation/VSP_015166|||http://purl.uniprot.org/annotation/VSP_015167|||http://purl.uniprot.org/annotation/VSP_015168|||http://purl.uniprot.org/annotation/VSP_015169|||http://purl.uniprot.org/annotation/VSP_015170|||http://purl.uniprot.org/annotation/VSP_015171|||http://purl.uniprot.org/annotation/VSP_017130
http://togogenome.org/gene/9606:ZNF530                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/M0R1P0|||http://purl.uniprot.org/uniprot/Q6P9A1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||KRAB|||Polar residues|||Zinc finger protein 530                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304997|||http://purl.uniprot.org/annotation/VAR_035144|||http://purl.uniprot.org/annotation/VAR_035145|||http://purl.uniprot.org/annotation/VAR_035146|||http://purl.uniprot.org/annotation/VAR_035147|||http://purl.uniprot.org/annotation/VAR_035148
http://togogenome.org/gene/9606:HERPUD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4UAE9|||http://purl.uniprot.org/uniprot/Q15011|||http://purl.uniprot.org/uniprot/Q53FP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with SYVN1|||Interaction with UBQLN1|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114920|||http://purl.uniprot.org/annotation/VAR_024277|||http://purl.uniprot.org/annotation/VSP_006708|||http://purl.uniprot.org/annotation/VSP_006709|||http://purl.uniprot.org/annotation/VSP_047333
http://togogenome.org/gene/9606:TNFRSF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43489                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In IMD16.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3; truncated|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034554|||http://purl.uniprot.org/annotation/VAR_025164|||http://purl.uniprot.org/annotation/VAR_070942
http://togogenome.org/gene/9606:USP17L7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7H9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Inactive ubiquitin carboxyl-terminal hydrolase 17-like protein 7|||Polar residues|||USP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331649|||http://purl.uniprot.org/annotation/VAR_051526|||http://purl.uniprot.org/annotation/VAR_051527
http://togogenome.org/gene/9606:ERCC6L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NKX8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Abolishes ATPase activity.|||Abolishes chromatin association.|||Basic and acidic residues|||DEAH box|||DNA excision repair protein ERCC-6-like|||Decreased affinity for BEND3, and abolishes BEND3-mediated stimulation of ATPase activity; when associated with A-11 and A-13.|||Decreased affinity for BEND3, and abolishes BEND3-mediated stimulation of ATPase activity; when associated with A-11 and A-21.|||Decreased affinity for BEND3, and abolishes BEND3-mediated stimulation of ATPase activity; when associated with A-13 and A-21.|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Induces a decrease in phosphorylation.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PLK1|||Polar residues|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328831
http://togogenome.org/gene/9606:DYNLT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JR98                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased colocalization with PPP1CC by 27%.|||Disordered|||Dynein light chain Tctex-type 4|||Partially reduces the binding to PP1CC.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316872|||http://purl.uniprot.org/annotation/VAR_087892
http://togogenome.org/gene/9606:IQCD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DY2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Dynein regulatory complex protein 10|||IQ|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282548|||http://purl.uniprot.org/annotation/VAR_056921|||http://purl.uniprot.org/annotation/VSP_024178|||http://purl.uniprot.org/annotation/VSP_024179|||http://purl.uniprot.org/annotation/VSP_024180
http://togogenome.org/gene/9606:BLOC1S4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUP1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Biogenesis of lysosome-related organelles complex 1 subunit 4|||Disordered|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089975
http://togogenome.org/gene/9606:NR2C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H9NIM2|||http://purl.uniprot.org/uniprot/H9NIM3|||http://purl.uniprot.org/uniprot/P13056                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 2 group C member 1|||Phosphoserine|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Required for interaction with KAT2B|||Required for interaction with NRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053586|||http://purl.uniprot.org/annotation/VSP_036855|||http://purl.uniprot.org/annotation/VSP_036856|||http://purl.uniprot.org/annotation/VSP_036857|||http://purl.uniprot.org/annotation/VSP_036858
http://togogenome.org/gene/9606:JOSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7N5|||http://purl.uniprot.org/uniprot/Q8TAC2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Josephin|||Josephin-2|||Loss of deubiquitination activity, no change in subcellular location.|||Nucleophile|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053843|||http://purl.uniprot.org/annotation/VSP_047537
http://togogenome.org/gene/9606:SLC22A17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUG5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220507|||http://purl.uniprot.org/annotation/VSP_003774|||http://purl.uniprot.org/annotation/VSP_039782|||http://purl.uniprot.org/annotation/VSP_039783
http://togogenome.org/gene/9606:LYNX1-SLURP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DP58                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GPI-anchor amidated cysteine|||In isoform 2.|||Ly-6/neurotoxin-like protein 1|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036154|||http://purl.uniprot.org/annotation/PRO_0000440641|||http://purl.uniprot.org/annotation/VSP_058978
http://togogenome.org/gene/9606:STEAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KS24|||http://purl.uniprot.org/uniprot/Q6YPB2|||http://purl.uniprot.org/uniprot/Q8NFT2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Ferric oxidoreductase|||Helical|||In isoform 2.|||In isoform 3.|||Metalloreductase STEAP2|||Phosphoserine|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191697|||http://purl.uniprot.org/annotation/VAR_057727|||http://purl.uniprot.org/annotation/VAR_057728|||http://purl.uniprot.org/annotation/VAR_060387|||http://purl.uniprot.org/annotation/VAR_060388|||http://purl.uniprot.org/annotation/VAR_060389|||http://purl.uniprot.org/annotation/VSP_030999|||http://purl.uniprot.org/annotation/VSP_045590
http://togogenome.org/gene/9606:APOB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04114|||http://purl.uniprot.org/uniprot/Q59HB3|||http://purl.uniprot.org/uniprot/Q7Z7Q0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Apolipoprotein B-100|||Apolipoprotein B-48|||Apolipoprotein B100 C-terminal|||Basic (possible receptor binding region)|||Does not affect plasma lipid levels.|||Does not affect protein secretion.|||Heparin-binding|||Impairs protein secretion.|||In FHBL1; reduced protein secretion.|||In FHBL1; unknown pathological significance; does not affect interaction with MTTP.|||In FHCL2.|||In a colorectal cancer sample; somatic mutation; confirmed at protein level.|||Influences plasma concentrations of low density lipoprotein cholesterol.|||LDL receptor binding|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by FAM20C|||Phosphothreonine|||S-palmitoyl cysteine|||Vitellogenin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020750|||http://purl.uniprot.org/annotation/PRO_0000020751|||http://purl.uniprot.org/annotation/PRO_5004296945|||http://purl.uniprot.org/annotation/VAR_005016|||http://purl.uniprot.org/annotation/VAR_005017|||http://purl.uniprot.org/annotation/VAR_005018|||http://purl.uniprot.org/annotation/VAR_005019|||http://purl.uniprot.org/annotation/VAR_005020|||http://purl.uniprot.org/annotation/VAR_005021|||http://purl.uniprot.org/annotation/VAR_005022|||http://purl.uniprot.org/annotation/VAR_005023|||http://purl.uniprot.org/annotation/VAR_005024|||http://purl.uniprot.org/annotation/VAR_005025|||http://purl.uniprot.org/annotation/VAR_005026|||http://purl.uniprot.org/annotation/VAR_005027|||http://purl.uniprot.org/annotation/VAR_005028|||http://purl.uniprot.org/annotation/VAR_005029|||http://purl.uniprot.org/annotation/VAR_005030|||http://purl.uniprot.org/annotation/VAR_005031|||http://purl.uniprot.org/annotation/VAR_016184|||http://purl.uniprot.org/annotation/VAR_016185|||http://purl.uniprot.org/annotation/VAR_016186|||http://purl.uniprot.org/annotation/VAR_016187|||http://purl.uniprot.org/annotation/VAR_016188|||http://purl.uniprot.org/annotation/VAR_019827|||http://purl.uniprot.org/annotation/VAR_019828|||http://purl.uniprot.org/annotation/VAR_019829|||http://purl.uniprot.org/annotation/VAR_019830|||http://purl.uniprot.org/annotation/VAR_019831|||http://purl.uniprot.org/annotation/VAR_019832|||http://purl.uniprot.org/annotation/VAR_019833|||http://purl.uniprot.org/annotation/VAR_019834|||http://purl.uniprot.org/annotation/VAR_019835|||http://purl.uniprot.org/annotation/VAR_020135|||http://purl.uniprot.org/annotation/VAR_020136|||http://purl.uniprot.org/annotation/VAR_020137|||http://purl.uniprot.org/annotation/VAR_020138|||http://purl.uniprot.org/annotation/VAR_020139|||http://purl.uniprot.org/annotation/VAR_020140|||http://purl.uniprot.org/annotation/VAR_022036|||http://purl.uniprot.org/annotation/VAR_022037|||http://purl.uniprot.org/annotation/VAR_022038|||http://purl.uniprot.org/annotation/VAR_022610|||http://purl.uniprot.org/annotation/VAR_022611|||http://purl.uniprot.org/annotation/VAR_029341|||http://purl.uniprot.org/annotation/VAR_029342|||http://purl.uniprot.org/annotation/VAR_029343|||http://purl.uniprot.org/annotation/VAR_029344|||http://purl.uniprot.org/annotation/VAR_029345|||http://purl.uniprot.org/annotation/VAR_029346|||http://purl.uniprot.org/annotation/VAR_029347|||http://purl.uniprot.org/annotation/VAR_029348|||http://purl.uniprot.org/annotation/VAR_029349|||http://purl.uniprot.org/annotation/VAR_029350|||http://purl.uniprot.org/annotation/VAR_035795|||http://purl.uniprot.org/annotation/VAR_056737|||http://purl.uniprot.org/annotation/VAR_056738|||http://purl.uniprot.org/annotation/VAR_059582|||http://purl.uniprot.org/annotation/VAR_061558|||http://purl.uniprot.org/annotation/VAR_067277|||http://purl.uniprot.org/annotation/VAR_067278|||http://purl.uniprot.org/annotation/VAR_067279|||http://purl.uniprot.org/annotation/VAR_067280|||http://purl.uniprot.org/annotation/VAR_067281|||http://purl.uniprot.org/annotation/VAR_068911|||http://purl.uniprot.org/annotation/VAR_068912|||http://purl.uniprot.org/annotation/VAR_076538|||http://purl.uniprot.org/annotation/VAR_076539
http://togogenome.org/gene/9606:ANGPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15123                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Angiopoietin-2|||Fibrinogen C-terminal|||In LMPHM10; no effect on protein abundance; mutant protein is not secreted; loss of interaction with TEK.|||In LMPHM10; unknown pathological significance; no effect on protein abundance; reduced secretion; reduced glycosylation; no effect on interaction with TEK.|||In LMPHM10; unknown pathological significance; no effect on protein abundance; severely decreased secretion.|||In LMPHM10; unknown pathological significance; results in increased lymphangiogenesis; decreased interaction with ITGA5; no effect on protein abundance; no effect on secretion; no effect on interaction with TEK.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009113|||http://purl.uniprot.org/annotation/VAR_049069|||http://purl.uniprot.org/annotation/VAR_085861|||http://purl.uniprot.org/annotation/VAR_085862|||http://purl.uniprot.org/annotation/VAR_085863|||http://purl.uniprot.org/annotation/VAR_085864|||http://purl.uniprot.org/annotation/VSP_001540|||http://purl.uniprot.org/annotation/VSP_040096
http://togogenome.org/gene/9606:ETNK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HBU6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Ethanolamine kinase 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206227|||http://purl.uniprot.org/annotation/VSP_047191
http://togogenome.org/gene/9606:LPIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14693                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C-LIP|||DXDXT motif|||Decreased acetylation by KAT5.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2, isoform 5 and isoform 6.|||In isoform 3, isoform 5, isoform 6 and isoform 7.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||LXXIL motif|||N-LIP|||N6-acetyllysine|||Nuclear localization signal|||Phosphatidate phosphatase LPIN1|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209879|||http://purl.uniprot.org/annotation/VAR_013885|||http://purl.uniprot.org/annotation/VAR_035874|||http://purl.uniprot.org/annotation/VAR_054878|||http://purl.uniprot.org/annotation/VSP_045533|||http://purl.uniprot.org/annotation/VSP_053970|||http://purl.uniprot.org/annotation/VSP_053971|||http://purl.uniprot.org/annotation/VSP_055361|||http://purl.uniprot.org/annotation/VSP_055362|||http://purl.uniprot.org/annotation/VSP_055384
http://togogenome.org/gene/9606:FSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L4K1|||http://purl.uniprot.org/uniprot/B7ZM05                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  B30.2/SPRY|||Fibronectin type III and SPRY domain-containing protein 2|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317362|||http://purl.uniprot.org/annotation/VAR_051001|||http://purl.uniprot.org/annotation/VAR_051002|||http://purl.uniprot.org/annotation/VSP_054600
http://togogenome.org/gene/9606:PRRT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JH25                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Proline-rich transmembrane protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000394498|||http://purl.uniprot.org/annotation/VSP_039273|||http://purl.uniprot.org/annotation/VSP_039274|||http://purl.uniprot.org/annotation/VSP_039275
http://togogenome.org/gene/9606:NAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15742                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||NCD1|||NCD2|||NGFI-A-binding protein 2|||Necessary for nuclear localization|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077042|||http://purl.uniprot.org/annotation/VSP_003385|||http://purl.uniprot.org/annotation/VSP_003386|||http://purl.uniprot.org/annotation/VSP_003387
http://togogenome.org/gene/9606:ABCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33527                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Abolishes resistance to anthracyclines.|||Cytoplasmic|||Decreases resistance to anthracyclines.|||Decreases resistance to vincristine, VP-16 and doxorubicin.|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=16|||Helical; Name=17|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Impairs estradiol glucuronide transport.|||Impairs estradiol glucuronide transport; loss of resistance to alkaloid vincristine, cationic anthracyclines, epipodophyllotoxin VP-16, but not potassium antimony tartrate; partial loss of resistance to sodium arsenite.|||Impairs leukotriene C4 and estradiol glucuronide transport.|||Impairs leukotriene C4 transport.|||Impairs protein maturation and leukotriene C4 transport.|||In DFNA77; changes protein subcellular localization expressed in both membrane and cytoplasm; produces unstable mRNA.|||In DFNA77; unknown pathological significance.|||In isoform 2, isoform 5, isoform 6 and isoform 8.|||In isoform 3, isoform 5, isoform 7 and isoform 8.|||In isoform 4, isoform 6, isoform 7 and isoform 8.|||In isoform 9.|||Increases estradiol glucuronide transport.|||Increases resistance to vincristine and decreases resistance to VP-16.|||Multidrug resistance-associated protein 1|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||No effect on leukotriene C4 and estradiol glucuronide transport.|||No effect on protein maturation and leukotriene C4 transport.|||No effect.|||Only partially affects protein maturation; impairs leukotriene C4 transport.|||Phosphoserine|||Phosphotyrosine|||Reduced cGAMP export.|||Reduced transport of glutathione.|||Reduced transport of leukotriene C4 and of glutathione.|||Reduced transport of leukotriene C4, estradiol glucuronide and of glutathione.|||Slightly impairs leukotriene C4 and estradiol glucuronide transport.|||Strongly reduced transport of leukotriene C4, estradiol glucuronide and of glutathione.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093351|||http://purl.uniprot.org/annotation/VAR_011488|||http://purl.uniprot.org/annotation/VAR_011489|||http://purl.uniprot.org/annotation/VAR_013317|||http://purl.uniprot.org/annotation/VAR_013318|||http://purl.uniprot.org/annotation/VAR_013319|||http://purl.uniprot.org/annotation/VAR_013320|||http://purl.uniprot.org/annotation/VAR_013321|||http://purl.uniprot.org/annotation/VAR_013322|||http://purl.uniprot.org/annotation/VAR_013323|||http://purl.uniprot.org/annotation/VAR_055384|||http://purl.uniprot.org/annotation/VAR_055385|||http://purl.uniprot.org/annotation/VAR_055386|||http://purl.uniprot.org/annotation/VAR_083988|||http://purl.uniprot.org/annotation/VAR_083989|||http://purl.uniprot.org/annotation/VAR_083990|||http://purl.uniprot.org/annotation/VAR_083991|||http://purl.uniprot.org/annotation/VAR_083992|||http://purl.uniprot.org/annotation/VAR_083993|||http://purl.uniprot.org/annotation/VAR_083994|||http://purl.uniprot.org/annotation/VSP_000037|||http://purl.uniprot.org/annotation/VSP_000038|||http://purl.uniprot.org/annotation/VSP_000039|||http://purl.uniprot.org/annotation/VSP_017014
http://togogenome.org/gene/9606:HFE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DV50|||http://purl.uniprot.org/uniprot/F8W7W8|||http://purl.uniprot.org/uniprot/Q30201                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Alpha-3|||Associated with hemochromatosis and variegate porphyria; increased frequency among patients with diabetic nephropathy.|||Connecting peptide|||Cytoplasmic|||Extracellular|||Helical|||Hereditary hemochromatosis protein|||Ig-like|||Ig-like C1-type|||In HFE1.|||In HFE1; associated with D-63 in one patient.|||In HFE1; associated with susceptibility to porphyria cutanea tarda; associated with increased serum transferrin levels; higher frequency in patients with type 2 diabetes than in controls.|||In HFE1; destabilizing effect on the tertiary structure of the protein; prevents the normal interaction between HFE and B2M and between HFE and TFRC; decreases the capacity of HFE to reduce transferrin-mediated iron uptake.|||In HFE1; mild form.|||In HFE1; uncertain pathological significance.|||In HFE1; unknown pathological significance.|||In isoform 10.|||In isoform 11.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018892|||http://purl.uniprot.org/annotation/PRO_5002801010|||http://purl.uniprot.org/annotation/PRO_5003379636|||http://purl.uniprot.org/annotation/VAR_004396|||http://purl.uniprot.org/annotation/VAR_004397|||http://purl.uniprot.org/annotation/VAR_004398|||http://purl.uniprot.org/annotation/VAR_008111|||http://purl.uniprot.org/annotation/VAR_008112|||http://purl.uniprot.org/annotation/VAR_008113|||http://purl.uniprot.org/annotation/VAR_008114|||http://purl.uniprot.org/annotation/VAR_008729|||http://purl.uniprot.org/annotation/VAR_008730|||http://purl.uniprot.org/annotation/VAR_008731|||http://purl.uniprot.org/annotation/VAR_020270|||http://purl.uniprot.org/annotation/VAR_037304|||http://purl.uniprot.org/annotation/VAR_042506|||http://purl.uniprot.org/annotation/VAR_042507|||http://purl.uniprot.org/annotation/VAR_042508|||http://purl.uniprot.org/annotation/VAR_042509|||http://purl.uniprot.org/annotation/VAR_042510|||http://purl.uniprot.org/annotation/VAR_042511|||http://purl.uniprot.org/annotation/VAR_062279|||http://purl.uniprot.org/annotation/VSP_003218|||http://purl.uniprot.org/annotation/VSP_003219|||http://purl.uniprot.org/annotation/VSP_003220|||http://purl.uniprot.org/annotation/VSP_003221|||http://purl.uniprot.org/annotation/VSP_003222|||http://purl.uniprot.org/annotation/VSP_003223|||http://purl.uniprot.org/annotation/VSP_003224|||http://purl.uniprot.org/annotation/VSP_003225|||http://purl.uniprot.org/annotation/VSP_003226|||http://purl.uniprot.org/annotation/VSP_003227|||http://purl.uniprot.org/annotation/VSP_043477|||http://purl.uniprot.org/annotation/VSP_043478|||http://purl.uniprot.org/annotation/VSP_047336
http://togogenome.org/gene/9606:GAS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14393                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreases activation of AXL.|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||Gla|||Growth arrest-specific protein 6|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Laminin G-like 1|||Laminin G-like 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||Phosphothreonine|||Phosphotyrosine|||Reduces affinity for AXL 15-fold and decreases activation of AXL.|||Reduces affinity for AXL 3-fold.|||Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007589|||http://purl.uniprot.org/annotation/VAR_038823|||http://purl.uniprot.org/annotation/VAR_038824|||http://purl.uniprot.org/annotation/VAR_038825|||http://purl.uniprot.org/annotation/VAR_038826|||http://purl.uniprot.org/annotation/VAR_038827|||http://purl.uniprot.org/annotation/VAR_038828|||http://purl.uniprot.org/annotation/VAR_038829|||http://purl.uniprot.org/annotation/VSP_059767|||http://purl.uniprot.org/annotation/VSP_059768|||http://purl.uniprot.org/annotation/VSP_059769|||http://purl.uniprot.org/annotation/VSP_059770
http://togogenome.org/gene/9606:PTK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13882                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-fold lower specific kinase activity. Decreased, but still significant, autophosphorylation. Decreased, but still significant, autophosphorylation; when associated with A-447.|||Abolishes kinase activity and cell transformation, and phosphorylation of STAP2.|||Abolishes kinase activity.|||Abrogates interaction between PTK6-domain kinase and PTK6-linker. Abrogates autophosphorylation and phosphorylation of KHDRBS1.|||Decrease in STAP2 phosphorylation.|||Decrease in transforming potential and increase in the kinase activity level. Decreased, but still significant, autophosphorylation; when associated with A-342.|||In a renal papillary sample; somatic mutation.|||In isoform 2.|||Linker|||Phosphotyrosine|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Protein-tyrosine kinase 6|||Proton acceptor|||SH2|||SH3|||Strong decrease in STAP2 phosphorylation. Markedly decreased interaction between SH3 domain the linker region.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088133|||http://purl.uniprot.org/annotation/VAR_041760|||http://purl.uniprot.org/annotation/VAR_041761|||http://purl.uniprot.org/annotation/VSP_042066|||http://purl.uniprot.org/annotation/VSP_042067
http://togogenome.org/gene/9606:PRKAA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54646                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  5'-AMP-activated protein kinase catalytic subunit alpha-2|||AIS|||Disordered|||In a breast cancer sample; somatic mutation.|||In a gastric adenocarcinoma sample; somatic mutation.|||In breast cancer samples; infiltrating ductal carcinoma; somatic mutation.|||Phosphomimetic mutant.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by LKB1 and CaMKK2|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085594|||http://purl.uniprot.org/annotation/VAR_035623|||http://purl.uniprot.org/annotation/VAR_035624|||http://purl.uniprot.org/annotation/VAR_040355
http://togogenome.org/gene/9606:RLN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RU28|||http://purl.uniprot.org/uniprot/K7ENX1|||http://purl.uniprot.org/uniprot/Q8WXF3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Peptide|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Peptide|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Connecting peptide|||Insulin-like|||Interchain (between B and A chains)|||Relaxin-3 A chain|||Relaxin-3 B chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016082|||http://purl.uniprot.org/annotation/PRO_0000016083|||http://purl.uniprot.org/annotation/PRO_0000016084|||http://purl.uniprot.org/annotation/PRO_5002781869|||http://purl.uniprot.org/annotation/PRO_5003900785
http://togogenome.org/gene/9606:MAMDC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXC1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Apical endosomal glycoprotein|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||LDL-receptor class A 1; truncated|||LDL-receptor class A 2|||LDL-receptor class A 3|||MAM 1|||MAM 2|||MAM 3|||MAM 4|||MAM 5|||MAM 6|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286578|||http://purl.uniprot.org/annotation/VAR_032128|||http://purl.uniprot.org/annotation/VAR_035778|||http://purl.uniprot.org/annotation/VAR_035779|||http://purl.uniprot.org/annotation/VSP_026431|||http://purl.uniprot.org/annotation/VSP_026432|||http://purl.uniprot.org/annotation/VSP_052395
http://togogenome.org/gene/9606:OR10A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR3|||http://purl.uniprot.org/uniprot/Q8NGE5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150690|||http://purl.uniprot.org/annotation/VAR_053266
http://togogenome.org/gene/9606:XPNPEP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQH7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Impairs catalytic activity.|||In NPHPL1.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with TNFRSF1B|||Mitochondrion|||Prevents cleavage of N-terminal transit peptide; when associated with A-18; A-29-30-A and A-39-40-A.|||Prevents cleavage of N-terminal transit peptide; when associated with A-18; A-29-30-A and A-44.|||Prevents cleavage of N-terminal transit peptide; when associated with A-18; A-39-40-A and A-44.|||Prevents cleavage of N-terminal transit peptide; when associated with A-29-30-A; A-39-40-A and A-44.|||Xaa-Pro aminopeptidase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255654|||http://purl.uniprot.org/annotation/VAR_051573|||http://purl.uniprot.org/annotation/VAR_063820|||http://purl.uniprot.org/annotation/VSP_021296|||http://purl.uniprot.org/annotation/VSP_021297|||http://purl.uniprot.org/annotation/VSP_021298|||http://purl.uniprot.org/annotation/VSP_040142|||http://purl.uniprot.org/annotation/VSP_040143|||http://purl.uniprot.org/annotation/VSP_040144
http://togogenome.org/gene/9606:GPR150                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGU9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Pro residues|||Probable G-protein coupled receptor 150                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069630
http://togogenome.org/gene/9606:CHRNA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YM98|||http://purl.uniprot.org/uniprot/P30532|||http://purl.uniprot.org/uniprot/Q6EWN4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with receptor activation|||Associated with susceptibility to lung cancer.|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit alpha-5|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000356|||http://purl.uniprot.org/annotation/PRO_5014092436|||http://purl.uniprot.org/annotation/VAR_046211|||http://purl.uniprot.org/annotation/VAR_046212
http://togogenome.org/gene/9606:OR13F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGS4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150738|||http://purl.uniprot.org/annotation/VAR_024137|||http://purl.uniprot.org/annotation/VAR_034309|||http://purl.uniprot.org/annotation/VAR_034310|||http://purl.uniprot.org/annotation/VAR_034311|||http://purl.uniprot.org/annotation/VAR_053302|||http://purl.uniprot.org/annotation/VAR_053303
http://togogenome.org/gene/9606:KPNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52294                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  ARM 10; atypical|||ARM 1; truncated|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Basic and acidic residues|||Binding to RAG1|||Disordered|||IBB|||Importin subunit alpha-5|||Importin subunit alpha-5, N-terminally processed|||N-acetylmethionine|||N-acetylthreonine; in Importin subunit alpha-5, N-terminally processed|||NLS binding site (major)|||NLS binding site (minor)|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120719|||http://purl.uniprot.org/annotation/PRO_0000424491|||http://purl.uniprot.org/annotation/VAR_050002
http://togogenome.org/gene/9606:NLGN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Neuroligin-2|||Phosphoserine|||Pro residues|||Required for interaction with LHFPL4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008643
http://togogenome.org/gene/9606:ZPBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BS86                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In SPGF66; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Zona pellucida-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041598|||http://purl.uniprot.org/annotation/VAR_076826|||http://purl.uniprot.org/annotation/VAR_076827|||http://purl.uniprot.org/annotation/VAR_076828|||http://purl.uniprot.org/annotation/VAR_076829|||http://purl.uniprot.org/annotation/VAR_076830|||http://purl.uniprot.org/annotation/VAR_076831|||http://purl.uniprot.org/annotation/VAR_076832|||http://purl.uniprot.org/annotation/VAR_086974|||http://purl.uniprot.org/annotation/VSP_045491
http://togogenome.org/gene/9606:PANX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QZ0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Pannexin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208491|||http://purl.uniprot.org/annotation/VAR_034367|||http://purl.uniprot.org/annotation/VAR_034368
http://togogenome.org/gene/9606:NBPF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T75                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Neuroblastoma breakpoint family member 11|||Olduvai 1|||Olduvai 2|||Olduvai 3|||Olduvai 4|||Olduvai 5|||Olduvai 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288046|||http://purl.uniprot.org/annotation/VSP_040663|||http://purl.uniprot.org/annotation/VSP_040664
http://togogenome.org/gene/9606:WFDC11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEX6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Signal Peptide                                                                                  ^@                                                                                  Protein WFDC11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041389
http://togogenome.org/gene/9606:GPR27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1DAM3|||http://purl.uniprot.org/uniprot/Q9NS67                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069548
http://togogenome.org/gene/9606:ARIH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4X5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ubiquitin-protein ligase activity.|||Acidic residues|||Ariadne domain|||Defects in ligation.|||Defects in ligation. Does not affect zinc binding, folding. Does not impair E3 ubiquitin-protein ligase activity.|||Disordered|||Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity.|||Does not affect E3 ubiquitin-protein ligase activity.|||Does not affect E3 ubiquitin-protein ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes.|||Does not affect zinc binding and folding. Abolishes ability to transfer ubiquitin and E3 ubiquitin-protein ligase activity.|||E3 ubiquitin-protein ligase ARIH1|||Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity.|||IBR-type|||Impaired interaction with UBE2L3 without affecting interaction with neddylated cullin-RING complexes.|||Impairs E3 ubiquitin-protein ligase activity.|||Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity.|||Loss of interaction with UBE2L3.|||Loss of interaction with UBE2L3. Decreased E3 ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes.|||N6-acetyllysine|||No loss of interaction with UBE2L3.|||Probable disease-associated variant found in patient with an acute aortic dissection and ascending aortic aneurysm.|||Probable disease-associated variant found in patient with basilar tip artery aneurysm and distal left internal carotid artery aneurysm.|||Probable disease-associated variant found in patient with fusiform aneurysm of the aortic root and ascending aorta.|||RING-type 1|||RING-type 2; atypical|||Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 420-A--A-423.|||Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with A-503. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503.|||Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain.|||Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503.|||Strongly decreased ability to initiate ubiquitination of cullin-RING complexes.|||TRIAD supradomain|||UBA-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055752|||http://purl.uniprot.org/annotation/VAR_082646|||http://purl.uniprot.org/annotation/VAR_082647|||http://purl.uniprot.org/annotation/VAR_082648
http://togogenome.org/gene/9606:PACS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6VY07                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In SHMS.|||In isoform 2.|||Involved in binding to AP-1|||N-acetylalanine|||Phosphofurin acidic cluster sorting protein 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058171|||http://purl.uniprot.org/annotation/VAR_053797|||http://purl.uniprot.org/annotation/VAR_069534|||http://purl.uniprot.org/annotation/VSP_011557
http://togogenome.org/gene/9606:PGAP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0P7|||http://purl.uniprot.org/uniprot/J3QKU0|||http://purl.uniprot.org/uniprot/Q96FM1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Found in a patient with Toriello-Carey syndrome; unknown pathological significance.|||Helical|||In HPMRS4; results in loss of function; the mutant localizes to the Golgi apparatus as the wild-type.|||In HPMRS4; results in partial functional impairment; the mutant does not localize to the Golgi apparatus but is retained in the endoplasmic reticulum.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Post-GPI attachment to proteins factor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339356|||http://purl.uniprot.org/annotation/PRO_5016481432|||http://purl.uniprot.org/annotation/VAR_071155|||http://purl.uniprot.org/annotation/VAR_071156|||http://purl.uniprot.org/annotation/VAR_071157|||http://purl.uniprot.org/annotation/VAR_084138|||http://purl.uniprot.org/annotation/VSP_034158|||http://purl.uniprot.org/annotation/VSP_057229
http://togogenome.org/gene/9606:MAPK12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53778|||http://purl.uniprot.org/uniprot/Q6N076                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Emulation of the active state.|||In isoform 2.|||Loss of activity.|||Mitogen-activated protein kinase 12|||No effect.|||Phosphothreonine; by MAP2K3 and MAP2K6|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186282|||http://purl.uniprot.org/annotation/VAR_012002|||http://purl.uniprot.org/annotation/VAR_042265|||http://purl.uniprot.org/annotation/VAR_042266|||http://purl.uniprot.org/annotation/VSP_055224
http://togogenome.org/gene/9606:SFMBT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes histone-binding.|||Acidic residues|||Antigenic epitope|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||Phosphoserine|||Polar residues|||Reduced histone-binding.|||SAM|||Scm-like with four MBT domains protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071966|||http://purl.uniprot.org/annotation/VSP_013857
http://togogenome.org/gene/9606:S100A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P33764                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes calcium binding; when associated with Ala-30.|||Abolishes calcium binding; when associated with Ala-68.|||Citrulline; by PAD3|||EF-hand 1|||EF-hand 2|||Increases affinity for calcium; when associated with Ala-81.|||Increases affinity for calcium; when associated with Ala-99.|||N-acetylalanine|||Protein S100-A3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143972|||http://purl.uniprot.org/annotation/VAR_061047
http://togogenome.org/gene/9606:UTF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T230                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes coactivation activity; when associated with P-296.|||Abolishes coactivation activity; when associated with P-303.|||Disordered|||Leucine-zipper|||Phosphoserine|||Pro residues|||Undifferentiated embryonic cell transcription factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274551|||http://purl.uniprot.org/annotation/VAR_051485
http://togogenome.org/gene/9606:ATG12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94817                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-130 in ATG5)|||Impairs ATG12 stability.|||Impairs E3 activity of the ATG12-ATG5 conjugate.|||In isoform 2.|||Polar residues|||Ubiquitin-like protein ATG12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212471|||http://purl.uniprot.org/annotation/VSP_018104|||http://purl.uniprot.org/annotation/VSP_018105
http://togogenome.org/gene/9606:SPPL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCT6|||http://purl.uniprot.org/uniprot/Q9UG23                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Does not affect complex glycosylation pattern of cellular glycoproteins; when associated with A-271.|||Helical|||In isoform 3.|||Loss of intramembrane-cleaving activity toward the simian foamy virus envelope glycoprotein gp130. Does not affect complex glycosylation pattern of cellular glycoproteins; when associated with A-200.|||Lumenal|||PAL|||Signal peptide peptidase-like 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073912|||http://purl.uniprot.org/annotation/VSP_005205
http://togogenome.org/gene/9606:GOLGA8R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I6L899                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 8R|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000420862|||http://purl.uniprot.org/annotation/VSP_044756|||http://purl.uniprot.org/annotation/VSP_044757|||http://purl.uniprot.org/annotation/VSP_044758
http://togogenome.org/gene/9606:C1QTNF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFP7|||http://purl.uniprot.org/uniprot/A0A3B0J271|||http://purl.uniprot.org/uniprot/Q9BXJ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C1q|||Collagen-like|||Complement C1q tumor necrosis factor-related protein 1|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003529|||http://purl.uniprot.org/annotation/PRO_5033791832|||http://purl.uniprot.org/annotation/VAR_068885|||http://purl.uniprot.org/annotation/VSP_055570
http://togogenome.org/gene/9606:CASQ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31415                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Calsequestrin-1|||In TAM1; increased calcium-dependent susceptibility to proteolytic degradation; decreased calcium-dependent aggregation; decreased calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; loss of the ability to inhibit store-operated calcium entry (SOCE) activity.|||In TAM1; increased calcium-dependent susceptibility to proteolytic degradation; decreased calcium-dependent aggregation; decreased calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; no effect of the ability to inhibit store-operated calcium entry (SOCE) activity; muscle fibers with the mutation have significantly decreased calcium-dependent sensitivity to caffeine.|||In TAM1; no effect on calcium-dependent susceptibility to proteolytic degradation; increased moderately calcium-dependent aggregation; increased moderately calcium-dependent polymerization; no effect on subcellular localization; no effect on the subcellular localization of STIM1; decreased calcium content of intracellular stores; loss of the ability to inhibit store-operated calcium entry (SOCE) activity.|||In VMCQA; no effect on calcium-dependent susceptibility to proteolytic degradation; increased calcium-dependent aggregation; causes impaired polymerization of the protein; no effect on subcellular localization; decreased calcium content of sarcoplasmic reticulum stores; reduced sarcoplasmic reticulum calcium release during excitation-contraction coupling.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004212|||http://purl.uniprot.org/annotation/VAR_053021|||http://purl.uniprot.org/annotation/VAR_073337|||http://purl.uniprot.org/annotation/VAR_079704|||http://purl.uniprot.org/annotation/VAR_079705|||http://purl.uniprot.org/annotation/VAR_079706
http://togogenome.org/gene/9606:KCNA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q09470                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||INTRAMEM|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes channel activity, but does not affect expression at the cell membrane.|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Pore helix|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Impairs expression at the cell membrane.|||Impairs phosphorylation by PKA.|||In EA1.|||In EA1; alters voltage dependence and kinetics of activation though not of C-type inactivation.|||In EA1; channels have voltage dependence similar to that of wild-type channels but with faster kinetics and increased C-type inactivation; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4.|||In EA1; phenotype without myokymia.|||In EA1; results in non-functional homomeric channels; accelerates recovery from N-type inactivation due to interaction with KCNAB1; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4.|||In EA1; results in slower channel activation compared to wild-type; slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4.|||In EA1; yields currents with a largely reduced amplitude.|||In MK1; 10% reduction of mean peak current amplitudes compared to wil-dtype; mutant and wild-type expression together is consistent with a loss-of-function effect of the mutation.|||In MK1; does not affect channel activity.|||In MK1; induces a reduced efflux of potassium ions during depolarization which results in increased muscle cell activity; coexpression studies of the mutant protein with the wild-type protein produces significantly reduced currents suggesting a severe effect of the mutation.|||In MK1; strongly reduces the activity of homomeric channels with dominant negative effects on wild-type channels.|||In RNA edited version.|||N-linked (GlcNAc...) asparagine|||No effect on channel activity.|||No effect on palmitoylation, no effect on current kinetics.|||PDZ-binding|||Phosphoserine|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 1|||Probable disease-associated variant found in a patient with neonatal onset epileptic encephalopathy.|||S-palmitoyl cysteine|||S4-S5 linker|||Selectivity filter|||Slightly increases channel activity, but does not affect expression at the cell membrane.|||Slows down N-type inactivation of heteromeric channels formed by KCNA1 and KCNA4.|||Strongly decreases palmitoylation and alters current kinetics.|||Strongly reduces channel activity, but does not affect expression at the cell membrane.|||Tetramerization domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053968|||http://purl.uniprot.org/annotation/VAR_001508|||http://purl.uniprot.org/annotation/VAR_001509|||http://purl.uniprot.org/annotation/VAR_001510|||http://purl.uniprot.org/annotation/VAR_001511|||http://purl.uniprot.org/annotation/VAR_001512|||http://purl.uniprot.org/annotation/VAR_001513|||http://purl.uniprot.org/annotation/VAR_001514|||http://purl.uniprot.org/annotation/VAR_016805|||http://purl.uniprot.org/annotation/VAR_020051|||http://purl.uniprot.org/annotation/VAR_020830|||http://purl.uniprot.org/annotation/VAR_020831|||http://purl.uniprot.org/annotation/VAR_020832|||http://purl.uniprot.org/annotation/VAR_020833|||http://purl.uniprot.org/annotation/VAR_020834|||http://purl.uniprot.org/annotation/VAR_037100|||http://purl.uniprot.org/annotation/VAR_037101|||http://purl.uniprot.org/annotation/VAR_037102|||http://purl.uniprot.org/annotation/VAR_037103|||http://purl.uniprot.org/annotation/VAR_072397|||http://purl.uniprot.org/annotation/VAR_078205
http://togogenome.org/gene/9606:PYCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E2QRB3|||http://purl.uniprot.org/uniprot/J3QL32|||http://purl.uniprot.org/uniprot/P32322|||http://purl.uniprot.org/uniprot/Q8TBX0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In ARCL2B.|||In ARCL2B; may cause skipping of exon 6.|||In ARCL3B.|||In ARCL3B; results in a reduction of protein expression in skin fibroblasts from the patient.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Pyrroline-5-carboxylate reductase 1, mitochondrial|||Pyrroline-5-carboxylate reductase catalytic N-terminal|||Pyrroline-5-carboxylate reductase dimerisation|||Reduced enzyme activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187314|||http://purl.uniprot.org/annotation/VAR_059068|||http://purl.uniprot.org/annotation/VAR_059069|||http://purl.uniprot.org/annotation/VAR_059070|||http://purl.uniprot.org/annotation/VAR_059071|||http://purl.uniprot.org/annotation/VAR_059072|||http://purl.uniprot.org/annotation/VAR_059073|||http://purl.uniprot.org/annotation/VAR_059074|||http://purl.uniprot.org/annotation/VAR_059075|||http://purl.uniprot.org/annotation/VAR_059076|||http://purl.uniprot.org/annotation/VAR_067600|||http://purl.uniprot.org/annotation/VAR_067601|||http://purl.uniprot.org/annotation/VSP_044507|||http://purl.uniprot.org/annotation/VSP_054616
http://togogenome.org/gene/9606:CHDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE62                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Choline dehydrogenase, mitochondrial|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012329|||http://purl.uniprot.org/annotation/VAR_020421|||http://purl.uniprot.org/annotation/VAR_049357|||http://purl.uniprot.org/annotation/VAR_055097
http://togogenome.org/gene/9606:NGFR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08138                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Death|||Decreased interaction with ARHGDIA.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Mediates interaction with KIDINS220|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||TNFR-Cys 4|||Tumor necrosis factor receptor superfamily member 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000231|||http://purl.uniprot.org/annotation/PRO_0000034591|||http://purl.uniprot.org/annotation/VAR_020010|||http://purl.uniprot.org/annotation/VSP_056850
http://togogenome.org/gene/9606:HSPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSM0|||http://purl.uniprot.org/uniprot/B4DY72|||http://purl.uniprot.org/uniprot/Q92598                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Heat shock protein 105 kDa|||In isoform 3.|||In isoform 4.|||In isoform Beta.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078284|||http://purl.uniprot.org/annotation/VSP_002428|||http://purl.uniprot.org/annotation/VSP_035428|||http://purl.uniprot.org/annotation/VSP_054883
http://togogenome.org/gene/9606:ZFYVE9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95405                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Diminishes complex formation with SMAD2.|||Disordered|||FYVE-type|||In isoform 2.|||In isoform 3.|||No effect on complex formation with SMAD2.|||Phosphoserine|||Polar residues|||SBD|||Zinc finger FYVE domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098715|||http://purl.uniprot.org/annotation/VAR_052985|||http://purl.uniprot.org/annotation/VAR_052986|||http://purl.uniprot.org/annotation/VAR_052987|||http://purl.uniprot.org/annotation/VSP_004315|||http://purl.uniprot.org/annotation/VSP_004316|||http://purl.uniprot.org/annotation/VSP_004317
http://togogenome.org/gene/9606:GRID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAN9|||http://purl.uniprot.org/uniprot/Q9ULK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for dimerization|||Extracellular|||Glutamate receptor|||Glutamate receptor ionotropic, delta-1|||Helical|||In isoform 2.|||Interaction with CBLN1|||Ionotropic glutamate receptor C-terminal|||Ionotropic glutamate receptor L-glutamate and glycine-binding|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011561|||http://purl.uniprot.org/annotation/PRO_5027164531|||http://purl.uniprot.org/annotation/VAR_022011|||http://purl.uniprot.org/annotation/VSP_057019
http://togogenome.org/gene/9606:CT47A4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:RRAGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L523                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with TFE3 and TFEB without affecting interaction with RPTOR.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In RA1 mutant; abolished interaction with RPTOR without affecting GTP-binding. Does not affect interaction with TFE3 and TFEB.|||In RA2 mutant; abolished interaction with RPTOR without affecting GTP-binding; when associated with A-35. In RA3 mutant; abolished interaction with RPTOR without affecting GTP-binding; when associated with F-29 and Y-35. Abolished interaction with RPTOR without affecting interaction with TFE3 and TFEB. Does not affect interaction with TFE3 and TFEB; when associated with A-35.|||In RA2 mutant; abolished interaction with RPTOR without affecting GTP-binding; when associated with A-46. Does not affect interaction with TFE3 and TFEB; when associated with A-46.|||In RA3 mutant; abolished interaction with RPTOR without affecting GTP-binding; when associated with F-29 and A-46.|||In RA3 mutant; abolished interaction with RPTOR without affecting GTP-binding; when associated with Y-35 and A-46.|||Maintains GTP-bound state, leading to activate mTORC1.|||Phosphoserine|||Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with R-142, R-230 and R-244.|||Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with R-220, R-230 and R-244.|||Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with RR-142, R-220 and R-230.|||Prevents RRAGA ubiquitination and alters interaction and regulation by GATOR1; when associated with RR-142, R-220 and R-244.|||Ras-related GTP-binding protein A|||Reduced affinity for all nucleotides, but with preferential binding of GDP over GTP.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239945
http://togogenome.org/gene/9606:MROH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0P682|||http://purl.uniprot.org/uniprot/Q6PF12|||http://purl.uniprot.org/uniprot/Q9H579                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Protein MROH8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079462|||http://purl.uniprot.org/annotation/VSP_003821|||http://purl.uniprot.org/annotation/VSP_003822
http://togogenome.org/gene/9606:ANTXR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53FL1|||http://purl.uniprot.org/uniprot/Q96EC6|||http://purl.uniprot.org/uniprot/Q9H6X2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Anthrax toxin receptor 1|||Anthrax toxin receptor extracellular|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation disrupts interaction of these molecules in a dominant-negative manner.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with PA|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002692|||http://purl.uniprot.org/annotation/PRO_5004249171|||http://purl.uniprot.org/annotation/VAR_053015|||http://purl.uniprot.org/annotation/VAR_063146|||http://purl.uniprot.org/annotation/VSP_000444|||http://purl.uniprot.org/annotation/VSP_000445|||http://purl.uniprot.org/annotation/VSP_000446|||http://purl.uniprot.org/annotation/VSP_000447|||http://purl.uniprot.org/annotation/VSP_000448|||http://purl.uniprot.org/annotation/VSP_000449|||http://purl.uniprot.org/annotation/VSP_047863|||http://purl.uniprot.org/annotation/VSP_047864|||http://purl.uniprot.org/annotation/VSP_047865
http://togogenome.org/gene/9606:RGS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43665                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation site and leads to strongly reduced overall phosphorylation.|||Disordered|||In isoform 1.|||In isoform 2.|||Phosphoserine|||RGS|||Regulator of G-protein signaling 10|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204207|||http://purl.uniprot.org/annotation/VAR_011896|||http://purl.uniprot.org/annotation/VSP_060087|||http://purl.uniprot.org/annotation/VSP_060088
http://togogenome.org/gene/9606:NXPE4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWF7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-linked (GlcNAc...) asparagine|||NXPE family member 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019553|||http://purl.uniprot.org/annotation/VAR_049025|||http://purl.uniprot.org/annotation/VAR_049026|||http://purl.uniprot.org/annotation/VSP_014701
http://togogenome.org/gene/9606:PCDHGA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003956|||http://purl.uniprot.org/annotation/VSP_008667|||http://purl.uniprot.org/annotation/VSP_008668
http://togogenome.org/gene/9606:PLEKHA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X1S6|||http://purl.uniprot.org/uniprot/A0A2P1JJM6|||http://purl.uniprot.org/uniprot/Q96JA3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes binding to phosphatylinositol 4-phosphate, less association with Golgi and no preference for TGN location.|||Glycolipid transfer protein homology domain|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Loss of glucosylceramide transfer activity from the TGN to the plasma membrane.|||PH|||Phosphoserine|||Phosphothreonine|||Pleckstrin homology domain-containing family A member 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306865|||http://purl.uniprot.org/annotation/VAR_035444|||http://purl.uniprot.org/annotation/VSP_028543|||http://purl.uniprot.org/annotation/VSP_028544|||http://purl.uniprot.org/annotation/VSP_028545|||http://purl.uniprot.org/annotation/VSP_028546
http://togogenome.org/gene/9606:ZXDC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2QGD7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with CIITA|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for transcriptional activation|||Zinc finger protein ZXDC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292803|||http://purl.uniprot.org/annotation/VAR_057464|||http://purl.uniprot.org/annotation/VSP_026437|||http://purl.uniprot.org/annotation/VSP_026438|||http://purl.uniprot.org/annotation/VSP_047464
http://togogenome.org/gene/9606:TMEM203                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 203                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317203
http://togogenome.org/gene/9606:TEKTIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCJ1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Tektin bundle-interacting protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332195|||http://purl.uniprot.org/annotation/VAR_061253|||http://purl.uniprot.org/annotation/VAR_061254
http://togogenome.org/gene/9606:TARDBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13148                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters but does not abolish RNA binding.|||Complete loss of self-oligomerization.|||Completely abolishes RNA binding.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Highly reduces binding to RNA and DNA.|||In ALS10.|||In ALS10; a patient with bulbar signs and dementia.|||In ALS10; also in a patient with frontotemporal dementia.|||In ALS10; also in patients with frontotemporal lobar degeneration with motor neuron disease.|||In ALS10; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos; loss of ability to negatively regulate the expression of CDK6.|||In ALS10; loss of ability to negatively regulate the expression of CDK6.|||In ALS10; loss of interaction with PPIA/CYPA.|||In ALS10; significant reduction in interaction with PPIA/CYPA.|||In ALS10; triggers mitochondrial DNA release into the cytosol, which is then detected by CGAS, leading to activation of the cGAS-STING pathway and autoinflammation; impedes the development of normal limb and tail buds and increases the number of apoptotic nuclei when expressed in chick embryos; does not affect the interaction with ATXN2.|||In ALS10; triggers mitochondrial DNA release into the cytosol, which is then detected by CGAS, leading to activation of the cGAS-STING pathway and autoinflammation; slight reduction in interaction with PPIA/CYPA.|||In isoform 2.|||Interaction with UBQLN2|||Loss of RNA-binding and reduced interaction with PPIA/CYPA.|||Nuclear export signal|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||RRM 1|||RRM 2|||TAR DNA-binding protein 43                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081972|||http://purl.uniprot.org/annotation/VAR_045656|||http://purl.uniprot.org/annotation/VAR_045657|||http://purl.uniprot.org/annotation/VAR_045658|||http://purl.uniprot.org/annotation/VAR_045659|||http://purl.uniprot.org/annotation/VAR_045660|||http://purl.uniprot.org/annotation/VAR_045661|||http://purl.uniprot.org/annotation/VAR_045662|||http://purl.uniprot.org/annotation/VAR_045663|||http://purl.uniprot.org/annotation/VAR_045664|||http://purl.uniprot.org/annotation/VAR_045665|||http://purl.uniprot.org/annotation/VAR_045666|||http://purl.uniprot.org/annotation/VAR_045667|||http://purl.uniprot.org/annotation/VAR_045668|||http://purl.uniprot.org/annotation/VAR_045669|||http://purl.uniprot.org/annotation/VAR_058611|||http://purl.uniprot.org/annotation/VAR_058612|||http://purl.uniprot.org/annotation/VAR_058613|||http://purl.uniprot.org/annotation/VAR_058614|||http://purl.uniprot.org/annotation/VAR_058615|||http://purl.uniprot.org/annotation/VAR_058616|||http://purl.uniprot.org/annotation/VAR_058617|||http://purl.uniprot.org/annotation/VAR_058618|||http://purl.uniprot.org/annotation/VAR_058619|||http://purl.uniprot.org/annotation/VAR_062767|||http://purl.uniprot.org/annotation/VAR_067499|||http://purl.uniprot.org/annotation/VAR_067500|||http://purl.uniprot.org/annotation/VAR_083737|||http://purl.uniprot.org/annotation/VAR_083738|||http://purl.uniprot.org/annotation/VSP_056406|||http://purl.uniprot.org/annotation/VSP_056407
http://togogenome.org/gene/9606:CASP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRL7|||http://purl.uniprot.org/uniprot/B4DWA2|||http://purl.uniprot.org/uniprot/P55210                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) ADP-riboxanated arginine|||Abolished ADP-riboxanation by C.violaceum CopC.|||Abolished cleavage at the N-terminus, leading to impaired activation and thiol protease activity. In P7-D2A mutant; abolished cleavage and activation, leading to decreased but mesureable activity; when associated with A-198.|||Abolished phosphorylation by PAK2; when associated with A-173 and A-239.|||Abolished phosphorylation by PAK2; when associated with A-30 and A-173.|||Abolished phosphorylation by PAK2; when associated with A-30 and A-239.|||Abolished thiol protease activity.|||Acidic residues|||Caspase family p10|||Caspase family p20|||Caspase-7 subunit p11|||Caspase-7 subunit p20|||Cleavage; by CAPN1|||Decreased ability to cleave PARP1 and PTGES3.|||Decreased ability to cleave PARP1.|||Decreased ability to cleave PARP1. Decreased RNA-binding.|||Decreased phosphorylation by PAK2.|||Disordered|||Does not affect ability to cleave PARP1.|||Does not significantly affect thiol protease catalytic activity.|||Does not significantly affect thiol protease catalytic efficiency.|||Exosite|||In dsCasp-7 mutant; unable to cleave DEVD and VEID peptides; when associated with F-276.|||In dsCasp-7 mutant; unable to cleave DEVD sand VEID peptides; when associated with 232-H--E-234.|||In esCasp-7 V3 mutant; promotes specificity toward alternate peptides with VEID, YVAD, WEHD, LETD or LEHD sequence; when associated with 230-V--V-234.|||In esCasp-7 V3 mutant; promotes specificity toward alternate peptides with VEID, YVAD, WEHD, LETD or LEHD sequence; when associated with C-276. In esCasp-7 V4 mutant; promotes specificity toward alternate peptides with VEID, YVAD, WEHD, LETD or LEHD sequence; when associated with D-276.|||In esCasp-7 V4 mutant; promotes specificity toward alternate peptides with VEID, YVAD, WEHD, LETD or LEHD sequence; when associated with 230-V--V-234.|||In isoform 4.|||In isoform Alpha'.|||In isoform Beta.|||In mutant II; prevents cleavage of loop L2 region; retains significant thiol protease activity.|||In mutant III; prevents cleavage of loop L2 region; abolished thiol protease activity.|||In mutant IV; prevents cleavage of loop L2 region; retains significant thiol protease activity.|||Involved in allosteric regulation|||Loop L1|||Loop L2|||Loop L3|||Loop L4|||Mimics phosphorylation; does not affect thiol protease activity.|||Mimics phosphorylation; leading to inactivate thiol protease activity.|||N-acetylalanine|||N-terminally processed|||Phosphoserine|||Phosphoserine; by PAK2|||Phosphothreonine; by PAK2|||Reduced cleavage and activation by initiator caspases. Abolished cleavage and activation by initiator caspases; when associated with A-198.|||Reduced thiol protease catalytic efficiency.|||Removed|||Strongly reduced cleavage and activation by initiator caspases. Abolished cleavage and activation by initiator caspases; when associated with A-206. In P7-D2A mutant; abolished cleavage and activation, leading to decreased but mesureable activity; when associated with A-23.|||Strongly reduced thiol protease activity.|||Strongly reduced thiol protease catalytic efficiency.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004616|||http://purl.uniprot.org/annotation/PRO_0000004617|||http://purl.uniprot.org/annotation/PRO_0000004618|||http://purl.uniprot.org/annotation/PRO_0000004619|||http://purl.uniprot.org/annotation/VAR_048617|||http://purl.uniprot.org/annotation/VAR_048618|||http://purl.uniprot.org/annotation/VSP_000806|||http://purl.uniprot.org/annotation/VSP_000807|||http://purl.uniprot.org/annotation/VSP_045325
http://togogenome.org/gene/9606:MARVELD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A59                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||MARVEL|||MARVEL domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271529|||http://purl.uniprot.org/annotation/VAR_029893|||http://purl.uniprot.org/annotation/VSP_022322|||http://purl.uniprot.org/annotation/VSP_047541|||http://purl.uniprot.org/annotation/VSP_047542
http://togogenome.org/gene/9606:MAFG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15525                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes acetylation. Has no effect on binding to NFE2 but impairs the DNA binding and transcriptional activities of NFE2; when associated with A-53; A-60 and A-71.|||Abolishes acetylation. Has no effect on binding to NFE2 but impairs the DNA binding and transcriptional activities of NFE2; when associated with A-53; A-60; and A-76.|||Abolishes acetylation. Has no effect on binding to NFE2 but impairs the DNA binding and transcriptional activities of NFE2; when associated with A-53; A-71 and A-76.|||Abolishes acetylation. Has no effect on binding to NFE2 but impairs the DNA binding and transcriptional activities of NFE2; when associated with A-60; A-71 and A-76.|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Leucine-zipper|||N6-acetyllysine|||Phosphoserine|||Transcription factor MafG|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076500
http://togogenome.org/gene/9606:MUC19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5P9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Approximate repeats of G-V-T-G-T-T-G-P-S-A|||Basic and acidic residues|||CTCK|||Disordered|||In isoform 2.|||Mucin-19|||Polar residues|||VWFC|||VWFD 1|||VWFD 2|||VWFD 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342664|||http://purl.uniprot.org/annotation/VAR_056617|||http://purl.uniprot.org/annotation/VAR_056618|||http://purl.uniprot.org/annotation/VAR_056619|||http://purl.uniprot.org/annotation/VAR_056620|||http://purl.uniprot.org/annotation/VAR_056621|||http://purl.uniprot.org/annotation/VAR_056622|||http://purl.uniprot.org/annotation/VAR_056623|||http://purl.uniprot.org/annotation/VAR_056624|||http://purl.uniprot.org/annotation/VAR_056625|||http://purl.uniprot.org/annotation/VAR_056626|||http://purl.uniprot.org/annotation/VAR_056627|||http://purl.uniprot.org/annotation/VAR_056628|||http://purl.uniprot.org/annotation/VAR_056629|||http://purl.uniprot.org/annotation/VAR_056630|||http://purl.uniprot.org/annotation/VAR_056631|||http://purl.uniprot.org/annotation/VAR_056632|||http://purl.uniprot.org/annotation/VAR_056633|||http://purl.uniprot.org/annotation/VAR_056634|||http://purl.uniprot.org/annotation/VAR_056635|||http://purl.uniprot.org/annotation/VAR_056636|||http://purl.uniprot.org/annotation/VAR_056637|||http://purl.uniprot.org/annotation/VAR_056638|||http://purl.uniprot.org/annotation/VAR_056639|||http://purl.uniprot.org/annotation/VAR_056640|||http://purl.uniprot.org/annotation/VSP_034521|||http://purl.uniprot.org/annotation/VSP_034522
http://togogenome.org/gene/9606:SSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05455                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HTH La-type RNA-binding|||Lupus La protein|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||RRM|||xRRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207599
http://togogenome.org/gene/9606:CPSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10570                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage and polyadenylation specificity factor subunit 1|||Disordered|||In MYP27.|||In MYP27; unknown pathological significance.|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074387|||http://purl.uniprot.org/annotation/VAR_083935|||http://purl.uniprot.org/annotation/VAR_083936|||http://purl.uniprot.org/annotation/VAR_083937
http://togogenome.org/gene/9606:C11orf86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJI1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Uncharacterized protein C11orf86                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328809
http://togogenome.org/gene/9606:SRSF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with SAFB1|||Phosphoserine|||Phosphotyrosine|||Polar residues|||RRM 1|||RRM 2|||Serine/arginine-rich splicing factor 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081935
http://togogenome.org/gene/9606:PTCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPU6|||http://purl.uniprot.org/uniprot/Q8WV60                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||PPR|||Pentatricopeptide repeat-containing protein 2, mitochondrial|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344050|||http://purl.uniprot.org/annotation/VSP_055257|||http://purl.uniprot.org/annotation/VSP_055258|||http://purl.uniprot.org/annotation/VSP_055680
http://togogenome.org/gene/9606:CCL20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78556                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C-C motif chemokine 20|||CCL20(1-64)|||CCL20(1-67)|||CCL20(2-70)|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005217|||http://purl.uniprot.org/annotation/PRO_0000041854|||http://purl.uniprot.org/annotation/PRO_0000041855|||http://purl.uniprot.org/annotation/PRO_0000041856|||http://purl.uniprot.org/annotation/VAR_011915|||http://purl.uniprot.org/annotation/VSP_001061
http://togogenome.org/gene/9606:KATNIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60303                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS26; unknown pathological significance.|||Katanin-interacting protein|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313090|||http://purl.uniprot.org/annotation/VAR_037654|||http://purl.uniprot.org/annotation/VAR_037655|||http://purl.uniprot.org/annotation/VAR_037656|||http://purl.uniprot.org/annotation/VAR_037657|||http://purl.uniprot.org/annotation/VAR_037658|||http://purl.uniprot.org/annotation/VAR_037659|||http://purl.uniprot.org/annotation/VAR_061238|||http://purl.uniprot.org/annotation/VAR_082145
http://togogenome.org/gene/9606:ANKRD23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SG2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 23|||Disordered|||In isoform 2.|||Interaction with TTN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240666|||http://purl.uniprot.org/annotation/VSP_019424
http://togogenome.org/gene/9606:TLCD3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0F5|||http://purl.uniprot.org/uniprot/Q71RH2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Ceramide synthase|||Helical|||In CORD22; unknown pathological significance.|||In isoform 2.|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185542|||http://purl.uniprot.org/annotation/VAR_086272|||http://purl.uniprot.org/annotation/VSP_013343
http://togogenome.org/gene/9606:PQBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4V5|||http://purl.uniprot.org/uniprot/O60828                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||1-5|||2-1|||2-2|||2-3|||3 X 2 AA tandem repeats of [DE]-R|||3-1|||3-2|||3-3|||3-4|||3-5|||3-6|||3-7|||5 X 7 AA approximate tandem repeats of D-R-[SG]-H-D-K-S|||7 X 2 AA tandem repeats of [DE]-R|||Abolishes interaction with TXNL4A.|||Basic and acidic residues|||Disordered|||Enhances transcriptional activation. Reduces transcriptional activation; when associated with A-75. Markedly reduced transcriptional activation; when associated with A-64; A-65 and A-66. Abolishes transcriptional activation; when associated with A-64; A-65; A-66 and A-75.|||Important for interaction with TXNL4A|||In RENS1; impairs interaction with WBP11, CGAS, SF3B1 and ATN1.|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||No effect on transcriptional activation.|||No effect on transcriptional activation. Reduces transcriptional activation; when associated with A-52. Abolishes transcriptional activation; when associated with A-52; A-64; A-65 and A-66.|||No effect on transcriptional activation; when associated with A-64 and A-65. Markedly reduced transcriptional activation; when associated with A-52; A-64 and A-65. Abolishes transcriptional activation; when associated with A-52; A-64; A-65 and A-75.|||No effect on transcriptional activation; when associated with A-64 and A-66. Markedly reduced transcriptional activation; when associated with A-52; A-64 and A-66. Abolishes transcriptional activation; when associated with A-52; A-64; A-66 and A-75.|||No effect on transcriptional activation; when associated with A-65 and A-66. Markedly reduced transcriptional activation; when associated with A-52; A-65 and A-66. Abolishes transcriptional activation; when associated with A-52; A-65; A-66 and A-75.|||Phosphoserine|||Polar residues|||Polyglutamine-binding protein 1|||Probable disease-associated variant found in a patient with autism.|||Removed|||Strongly reduces affinity for TXNL4A.|||WW                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076089|||http://purl.uniprot.org/annotation/VAR_036357|||http://purl.uniprot.org/annotation/VAR_071063|||http://purl.uniprot.org/annotation/VAR_078695|||http://purl.uniprot.org/annotation/VSP_015896|||http://purl.uniprot.org/annotation/VSP_015897|||http://purl.uniprot.org/annotation/VSP_015898|||http://purl.uniprot.org/annotation/VSP_015899|||http://purl.uniprot.org/annotation/VSP_015900|||http://purl.uniprot.org/annotation/VSP_015901|||http://purl.uniprot.org/annotation/VSP_015902|||http://purl.uniprot.org/annotation/VSP_015903|||http://purl.uniprot.org/annotation/VSP_015904|||http://purl.uniprot.org/annotation/VSP_015905|||http://purl.uniprot.org/annotation/VSP_015906|||http://purl.uniprot.org/annotation/VSP_015907|||http://purl.uniprot.org/annotation/VSP_015908|||http://purl.uniprot.org/annotation/VSP_015909|||http://purl.uniprot.org/annotation/VSP_015910
http://togogenome.org/gene/9606:IARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41252|||http://purl.uniprot.org/uniprot/Q6P0M4|||http://purl.uniprot.org/uniprot/Q7L4K8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Aminoacyl-tRNA synthetase class Ia|||In GRIDHH.|||Isoleucine--tRNA ligase, cytoplasmic|||Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098597|||http://purl.uniprot.org/annotation/VAR_057951|||http://purl.uniprot.org/annotation/VAR_057952|||http://purl.uniprot.org/annotation/VAR_058300|||http://purl.uniprot.org/annotation/VAR_071387|||http://purl.uniprot.org/annotation/VAR_071388|||http://purl.uniprot.org/annotation/VAR_077055|||http://purl.uniprot.org/annotation/VAR_077056|||http://purl.uniprot.org/annotation/VAR_077057|||http://purl.uniprot.org/annotation/VAR_077058
http://togogenome.org/gene/9606:ADRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WX59|||http://purl.uniprot.org/uniprot/Q16186                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DEUBAD|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with UCHL5|||N-acetylthreonine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Proteasomal ubiquitin receptor ADRM1|||Pru|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020631
http://togogenome.org/gene/9606:GARRE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15063                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Granule associated Rac and RHOG effector protein 1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050748
http://togogenome.org/gene/9606:GCLM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48507                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glutamate--cysteine ligase regulatory subunit|||In isoform 2.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192573|||http://purl.uniprot.org/annotation/VAR_021063|||http://purl.uniprot.org/annotation/VSP_057008
http://togogenome.org/gene/9606:RPL28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46779                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Large ribosomal subunit protein eL28|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122389|||http://purl.uniprot.org/annotation/VAR_034460|||http://purl.uniprot.org/annotation/VSP_043026|||http://purl.uniprot.org/annotation/VSP_046173|||http://purl.uniprot.org/annotation/VSP_047026|||http://purl.uniprot.org/annotation/VSP_047027
http://togogenome.org/gene/9606:WDR59                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJI9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished interaction with WDR24 and assembly of the GATOR2 complex; when associated with 728-E--E-732.|||Abolished interaction with WDR24 and assembly of the GATOR2 complex; when associated with E-698.|||Basic and acidic residues|||C4-type|||Disordered|||GATOR2 complex protein WDR59|||Impaired amino-acid-mediated mTORC1 activation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||RING-type; atypical|||RWD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280721|||http://purl.uniprot.org/annotation/VAR_053436|||http://purl.uniprot.org/annotation/VSP_023881|||http://purl.uniprot.org/annotation/VSP_023882|||http://purl.uniprot.org/annotation/VSP_023883|||http://purl.uniprot.org/annotation/VSP_023884
http://togogenome.org/gene/9606:CABP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V35                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcium-binding protein 7|||Cytoplasmic|||EF-hand 1|||EF-hand 2|||Extracellular|||Helical; Anchor for type IV membrane protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073526
http://togogenome.org/gene/9606:ZC3H7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UGR2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Almost no effect on NSP3 binding.|||C2H2-type|||C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||Complete loss of NSP3 binding.|||Disordered|||LD motif; interaction with NSP3|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Zinc finger CCCH domain-containing protein 7B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106322|||http://purl.uniprot.org/annotation/VAR_054313
http://togogenome.org/gene/9606:CYP2F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24903                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cytochrome P450 2F1|||In allele CYP2F1*3 and in allele CYP2F1*4.|||In allele CYP2F1*3.|||In allele CYP2F1*4.|||In allele CYP2F1*5A and in allele CYP2F1*5B.|||In allele CYP2F1*6.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051759|||http://purl.uniprot.org/annotation/VAR_058863|||http://purl.uniprot.org/annotation/VAR_058864|||http://purl.uniprot.org/annotation/VAR_058865|||http://purl.uniprot.org/annotation/VAR_058866|||http://purl.uniprot.org/annotation/VAR_058867|||http://purl.uniprot.org/annotation/VAR_058868|||http://purl.uniprot.org/annotation/VSP_055575|||http://purl.uniprot.org/annotation/VSP_055576
http://togogenome.org/gene/9606:SLC15A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIM6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Solute carrier family 15 member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332233|||http://purl.uniprot.org/annotation/VAR_042979|||http://purl.uniprot.org/annotation/VAR_042980|||http://purl.uniprot.org/annotation/VAR_042981|||http://purl.uniprot.org/annotation/VAR_042982
http://togogenome.org/gene/9606:CENATAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UT8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Centrosomal AT-AC splicing factor|||Disordered|||Increases interaction with SASS6.|||N6-acetyllysine; by NAT10|||Polar residues|||Required for centrosome location|||Strongly reduces acetylation. No effect on interaction with SASS6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271022|||http://purl.uniprot.org/annotation/VAR_029848
http://togogenome.org/gene/9606:ZNF763                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0D2J5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 763                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330294|||http://purl.uniprot.org/annotation/VAR_042692|||http://purl.uniprot.org/annotation/VAR_057450|||http://purl.uniprot.org/annotation/VSP_039173|||http://purl.uniprot.org/annotation/VSP_055970
http://togogenome.org/gene/9606:CNOT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YKK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CNOT7.|||Abolishes interaction with CNOT7; when associated with Y-1209.|||Abolishes interaction with CNOT7; when associated with Y-1257.|||CCR4-NOT transcription complex subunit 1|||Disordered|||Impairs interaction with CNOT7; when associated with E-1208 and E-1218.|||Impairs interaction with CNOT7; when associated with E-1208 and Y-1212.|||Impairs interaction with CNOT7; when associated with Y-1212 and E-1218.|||In HPE12.|||In VIBOS.|||In VIBOS; uncertain pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with CNOT6, CNOT6L, CNOT7 and CNOT8|||Interaction with ZFP36|||LXXLL|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315541|||http://purl.uniprot.org/annotation/VAR_038254|||http://purl.uniprot.org/annotation/VAR_083066|||http://purl.uniprot.org/annotation/VAR_084311|||http://purl.uniprot.org/annotation/VAR_084312|||http://purl.uniprot.org/annotation/VAR_084313|||http://purl.uniprot.org/annotation/VAR_084314|||http://purl.uniprot.org/annotation/VAR_084315|||http://purl.uniprot.org/annotation/VAR_084316|||http://purl.uniprot.org/annotation/VAR_084317|||http://purl.uniprot.org/annotation/VAR_084318|||http://purl.uniprot.org/annotation/VAR_084319|||http://purl.uniprot.org/annotation/VAR_084320|||http://purl.uniprot.org/annotation/VAR_084321|||http://purl.uniprot.org/annotation/VAR_084322|||http://purl.uniprot.org/annotation/VAR_084323|||http://purl.uniprot.org/annotation/VAR_084324|||http://purl.uniprot.org/annotation/VAR_084325|||http://purl.uniprot.org/annotation/VAR_084326|||http://purl.uniprot.org/annotation/VAR_084327|||http://purl.uniprot.org/annotation/VSP_030559|||http://purl.uniprot.org/annotation/VSP_030560|||http://purl.uniprot.org/annotation/VSP_030561|||http://purl.uniprot.org/annotation/VSP_030562|||http://purl.uniprot.org/annotation/VSP_030563
http://togogenome.org/gene/9606:NEDD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUD2|||http://purl.uniprot.org/uniprot/Q14511                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with BCAR3.|||Abolishes interaction with PLK1.|||Abolishes the oxidation-mediated reduction in interaction with SMAD3.|||CAS family C-terminal|||Caspase cleavage related site|||Disordered|||Divergent helix-loop-helix motif|||Enhancer of filamentation 1|||Enhancer of filamentation 1 p55|||In isoform 2.|||In isoform 3.|||Interacts strongly with spindle-regulatory protein D1M1|||Interacts with CTTN|||No effect on interaction with BCAR3.|||No effect on interaction with PLK1.|||Phosphoserine|||Phosphoserine; by CSNK1D and CSNK1E|||Phosphothreonine; by CSNK1E|||Phosphotyrosine; by ABL1|||Polar residues|||Reduces interaction with PLK1. Abolishes interaction with PLK1; when associated with D-780.|||Reduces interaction with PLK1. Abolishes interaction with PLK1; when associated with D-804.|||Reduces interaction with PLK1. Reduces protein phosphorylation by CSNK1D; when associated with A-780.|||Reduces interaction with PLK1. Reduces protein phosphorylation by CSNK1D; when associated with A-804.|||Required for interaction with ITCH|||Required for interaction with PLK1|||SH3|||Serine rich protein interaction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089328|||http://purl.uniprot.org/annotation/PRO_0000296242|||http://purl.uniprot.org/annotation/VAR_021857|||http://purl.uniprot.org/annotation/VAR_054082|||http://purl.uniprot.org/annotation/VAR_054083|||http://purl.uniprot.org/annotation/VSP_042835|||http://purl.uniprot.org/annotation/VSP_042836|||http://purl.uniprot.org/annotation/VSP_044579
http://togogenome.org/gene/9606:EI24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PK61|||http://purl.uniprot.org/uniprot/O14681                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Etoposide-induced protein 2.4 homolog|||Helical|||In isoform 2.|||In some patients with early onset breast cancer.|||In some patients with early onset breast cancer; requires 2 nucleotide substitutions.|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086945|||http://purl.uniprot.org/annotation/VAR_065459|||http://purl.uniprot.org/annotation/VAR_065460|||http://purl.uniprot.org/annotation/VAR_065461|||http://purl.uniprot.org/annotation/VAR_065462|||http://purl.uniprot.org/annotation/VAR_065463|||http://purl.uniprot.org/annotation/VAR_065464|||http://purl.uniprot.org/annotation/VSP_055466
http://togogenome.org/gene/9606:PDK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1H4|||http://purl.uniprot.org/uniprot/Q16654                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Histidine kinase|||Interaction with the other subunit in the homodimer|||Loss of activity.|||Loss of activity; when associated with A-394.|||Loss of activity; when associated with A-395.|||Mitochondrion|||[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023445|||http://purl.uniprot.org/annotation/VAR_042298|||http://purl.uniprot.org/annotation/VAR_042299|||http://purl.uniprot.org/annotation/VAR_042300
http://togogenome.org/gene/9606:MED20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H944                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Mediator of RNA polymerase II transcription subunit 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065731|||http://purl.uniprot.org/annotation/VSP_057052
http://togogenome.org/gene/9606:TBX22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUL8|||http://purl.uniprot.org/uniprot/Q9Y458                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In CPX.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||T-box|||T-box transcription factor TBX22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184455|||http://purl.uniprot.org/annotation/VAR_015383|||http://purl.uniprot.org/annotation/VAR_015384|||http://purl.uniprot.org/annotation/VAR_021829|||http://purl.uniprot.org/annotation/VAR_021830|||http://purl.uniprot.org/annotation/VAR_021831|||http://purl.uniprot.org/annotation/VAR_021832|||http://purl.uniprot.org/annotation/VAR_021833|||http://purl.uniprot.org/annotation/VAR_036066|||http://purl.uniprot.org/annotation/VAR_036067|||http://purl.uniprot.org/annotation/VAR_036068|||http://purl.uniprot.org/annotation/VAR_069416|||http://purl.uniprot.org/annotation/VAR_069900|||http://purl.uniprot.org/annotation/VSP_040987
http://togogenome.org/gene/9606:SLC16A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTX9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||Monocarboxylate transporter 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288923|||http://purl.uniprot.org/annotation/VSP_025826
http://togogenome.org/gene/9606:SPATA16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJV8|||http://purl.uniprot.org/uniprot/Q9BXB7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In SPGF6.|||Spermatogenesis-associated protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315830|||http://purl.uniprot.org/annotation/VAR_038329|||http://purl.uniprot.org/annotation/VAR_038330|||http://purl.uniprot.org/annotation/VAR_038331|||http://purl.uniprot.org/annotation/VAR_038332|||http://purl.uniprot.org/annotation/VAR_038333|||http://purl.uniprot.org/annotation/VAR_038334|||http://purl.uniprot.org/annotation/VAR_038335|||http://purl.uniprot.org/annotation/VAR_038336|||http://purl.uniprot.org/annotation/VAR_038337|||http://purl.uniprot.org/annotation/VAR_038338|||http://purl.uniprot.org/annotation/VAR_038339
http://togogenome.org/gene/9606:CDKAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VV42                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||MTTase N-terminal|||Phosphoserine|||Phosphothreonine|||Radical SAM core|||TRAM|||Threonylcarbamoyladenosine tRNA methylthiotransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298670|||http://purl.uniprot.org/annotation/VAR_052705|||http://purl.uniprot.org/annotation/VSP_027450|||http://purl.uniprot.org/annotation/VSP_027451|||http://purl.uniprot.org/annotation/VSP_027452|||http://purl.uniprot.org/annotation/VSP_027453
http://togogenome.org/gene/9606:TNFRSF10C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14798                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated alanine|||N-linked (GlcNAc...) (high mannose) asparagine|||Polar residues|||Removed in mature form|||TAPE 1|||TAPE 2|||TAPE 3|||TAPE 4|||TAPE 5|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 10C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034582|||http://purl.uniprot.org/annotation/PRO_0000034583|||http://purl.uniprot.org/annotation/VAR_046534|||http://purl.uniprot.org/annotation/VAR_046535
http://togogenome.org/gene/9606:ADAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6V5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||In isoform 2.|||Proton donor|||tRNA-specific adenosine deaminase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287653|||http://purl.uniprot.org/annotation/VSP_025582
http://togogenome.org/gene/9606:SCAI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9R8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Necessary to inhibit MRTFA-induced SRF transcriptional activity|||Phosphotyrosine|||Protein SCAI|||Required for interaction with MRTFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089735|||http://purl.uniprot.org/annotation/VAR_023236|||http://purl.uniprot.org/annotation/VSP_015120
http://togogenome.org/gene/9606:CALCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01258|||http://purl.uniprot.org/uniprot/P06881                                                                                  ^@                                                                                  Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Calcitonin|||Calcitonin gene-related peptide 1|||Disordered|||In isoform 2.|||Katacalcin|||Phenylalanine amide|||Phosphoserine|||Proline amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004050|||http://purl.uniprot.org/annotation/PRO_0000004051|||http://purl.uniprot.org/annotation/PRO_0000004052|||http://purl.uniprot.org/annotation/PRO_0000004053|||http://purl.uniprot.org/annotation/PRO_0000004054|||http://purl.uniprot.org/annotation/PRO_0000004055|||http://purl.uniprot.org/annotation/VAR_014592|||http://purl.uniprot.org/annotation/VAR_014593|||http://purl.uniprot.org/annotation/VAR_025271|||http://purl.uniprot.org/annotation/VAR_025272|||http://purl.uniprot.org/annotation/VAR_025273|||http://purl.uniprot.org/annotation/VAR_025274|||http://purl.uniprot.org/annotation/VAR_048584|||http://purl.uniprot.org/annotation/VSP_000709
http://togogenome.org/gene/9606:GMIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7N1|||http://purl.uniprot.org/uniprot/B4DLZ1|||http://purl.uniprot.org/uniprot/Q9P107                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||GEM-interacting protein|||In isoform 2.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056725|||http://purl.uniprot.org/annotation/VAR_044518|||http://purl.uniprot.org/annotation/VSP_056142
http://togogenome.org/gene/9606:RORC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1D8P6|||http://purl.uniprot.org/uniprot/P51449|||http://purl.uniprot.org/uniprot/Q6I9R9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AF-2|||Completely abolishes transcriptional activity.|||Disordered|||In IMD42; does not affect nuclear localization; loss of transcription regulatory region sequence-specific DNA binding; loss of transcriptional activity.|||In isoform 2.|||Modulating|||NR C4-type|||NR LBD|||Nearly abolishes transcriptional activity.|||Nuclear receptor|||Nuclear receptor ROR-gamma|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053517|||http://purl.uniprot.org/annotation/VAR_073725|||http://purl.uniprot.org/annotation/VSP_010632|||http://purl.uniprot.org/annotation/VSP_010633
http://togogenome.org/gene/9606:TRANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8YEM9|||http://purl.uniprot.org/uniprot/O15050                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Acidic residues|||Disordered|||Polar residues|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR and ankyrin repeat-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348238|||http://purl.uniprot.org/annotation/VAR_046117|||http://purl.uniprot.org/annotation/VAR_046118|||http://purl.uniprot.org/annotation/VAR_061021
http://togogenome.org/gene/9606:C1orf105                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95561                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C1orf105                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251727|||http://purl.uniprot.org/annotation/VAR_027710|||http://purl.uniprot.org/annotation/VAR_027711
http://togogenome.org/gene/9606:MYH11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZJ4|||http://purl.uniprot.org/uniprot/P35749                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Basic and acidic residues|||C-terminal|||Disordered|||IQ|||In AAT4.|||In MMIHS2.|||In VSCM2; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-11|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123424|||http://purl.uniprot.org/annotation/VAR_030239|||http://purl.uniprot.org/annotation/VAR_030240|||http://purl.uniprot.org/annotation/VAR_030241|||http://purl.uniprot.org/annotation/VAR_031734|||http://purl.uniprot.org/annotation/VAR_031735|||http://purl.uniprot.org/annotation/VAR_050205|||http://purl.uniprot.org/annotation/VAR_050206|||http://purl.uniprot.org/annotation/VAR_085645|||http://purl.uniprot.org/annotation/VAR_085646|||http://purl.uniprot.org/annotation/VAR_085647|||http://purl.uniprot.org/annotation/VAR_085875|||http://purl.uniprot.org/annotation/VSP_043017|||http://purl.uniprot.org/annotation/VSP_043018
http://togogenome.org/gene/9606:HP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGL8|||http://purl.uniprot.org/uniprot/P00738|||http://purl.uniprot.org/uniprot/Q6PEJ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Haptoglobin|||Haptoglobin alpha chain|||Haptoglobin beta chain|||In AHP; causes reduced expression of the protein.|||In allele HP*1F and allele HP*1S.|||In allele HP*1F.|||In isoform 2.|||Interaction with CD163|||Interchain|||Interchain (between alpha and beta chains)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Sushi|||Sushi 1|||Sushi 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028456|||http://purl.uniprot.org/annotation/PRO_0000028457|||http://purl.uniprot.org/annotation/PRO_0000028458|||http://purl.uniprot.org/annotation/PRO_5002170051|||http://purl.uniprot.org/annotation/VAR_005294|||http://purl.uniprot.org/annotation/VAR_017112|||http://purl.uniprot.org/annotation/VAR_017113|||http://purl.uniprot.org/annotation/VAR_017114|||http://purl.uniprot.org/annotation/VAR_066214|||http://purl.uniprot.org/annotation/VSP_055024
http://togogenome.org/gene/9606:IDI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXS1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  Isopentenyl-diphosphate delta-isomerase 2|||Microbody targeting signal|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205228
http://togogenome.org/gene/9606:VIT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LCCL|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA 1|||VWFA 2|||Vitrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248210|||http://purl.uniprot.org/annotation/VAR_068964|||http://purl.uniprot.org/annotation/VAR_068965|||http://purl.uniprot.org/annotation/VAR_068966|||http://purl.uniprot.org/annotation/VSP_020209|||http://purl.uniprot.org/annotation/VSP_020210|||http://purl.uniprot.org/annotation/VSP_020211|||http://purl.uniprot.org/annotation/VSP_040124|||http://purl.uniprot.org/annotation/VSP_044597
http://togogenome.org/gene/9606:FARSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSD9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  B5|||In RILDBC1.|||In RILDBC1; has no defect in protein synthesis.|||In isoform 2.|||Phenylalanine--tRNA ligase beta subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127016|||http://purl.uniprot.org/annotation/VAR_071245|||http://purl.uniprot.org/annotation/VAR_081054|||http://purl.uniprot.org/annotation/VAR_081055|||http://purl.uniprot.org/annotation/VAR_081056|||http://purl.uniprot.org/annotation/VAR_081057|||http://purl.uniprot.org/annotation/VAR_081058|||http://purl.uniprot.org/annotation/VAR_081059|||http://purl.uniprot.org/annotation/VAR_081060|||http://purl.uniprot.org/annotation/VAR_081061|||http://purl.uniprot.org/annotation/VSP_056866
http://togogenome.org/gene/9606:SLFN11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7L1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes ATPase activity without affecting its role in DNA damage response; when associated with A-668.|||Abolishes ATPase activity without affecting its role in DNA damage response; when associated with M-605.|||Abolishes ATPase activity, leading to abolish ability to inhibit DNA replication without affecting subcellular location.|||Schlafen family member 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283091|||http://purl.uniprot.org/annotation/VAR_031492|||http://purl.uniprot.org/annotation/VAR_031493|||http://purl.uniprot.org/annotation/VAR_031494|||http://purl.uniprot.org/annotation/VAR_062186
http://togogenome.org/gene/9606:POLR2E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ89|||http://purl.uniprot.org/uniprot/E5KT65|||http://purl.uniprot.org/uniprot/P19388                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  DNA-directed RNA polymerases I, II, and III subunit RPABC1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||RNA polymerase Rpb5 N-terminal|||RNA polymerase subunit H/Rpb5 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146075|||http://purl.uniprot.org/annotation/VAR_028259
http://togogenome.org/gene/9606:ADAMTS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5FWF1|||http://purl.uniprot.org/uniprot/Q9UP79                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 8|||Basic and acidic residues|||Disintegrin|||Disordered|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029178|||http://purl.uniprot.org/annotation/PRO_0000029179
http://togogenome.org/gene/9606:ABCB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WW65|||http://purl.uniprot.org/uniprot/A0A0S2Z2Z3|||http://purl.uniprot.org/uniprot/O75027                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||Helical|||In ASAT.|||In ASAT; impaired maturation of cytosolic Fe/S proteins, loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain;; loss of [2Fe-2S]-(GS)4 cluster transport.|||In isoform 2.|||In isoform 3.|||Iron-sulfur clusters transporter ABCB7, mitochondrial|||Loss of ATPase activity stimulation by [2Fe-2S]-(GS)4 cluster stimulation. Loss of the ability to couple MgATP binding with stimulation of ATPase activity at the nucleotide binding domain. Loss of [2Fe-2S]-(GS)4 cluster transport.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Significantly increases ATPase activity by [2Fe-2S]-(GS)4 cluster stimulation. Increases affinity for Mg-ATP. Does not affect affinity for Mg-ATP in the presence of the in the presence of [2Fe-2S]-(GS)4 cluster. Does not affect [2Fe-2S]-(GS)4 cluster transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000249|||http://purl.uniprot.org/annotation/VAR_009156|||http://purl.uniprot.org/annotation/VAR_012640|||http://purl.uniprot.org/annotation/VAR_022872|||http://purl.uniprot.org/annotation/VAR_022873|||http://purl.uniprot.org/annotation/VAR_022874|||http://purl.uniprot.org/annotation/VAR_037972|||http://purl.uniprot.org/annotation/VAR_055471|||http://purl.uniprot.org/annotation/VAR_067354|||http://purl.uniprot.org/annotation/VSP_014635|||http://purl.uniprot.org/annotation/VSP_054700
http://togogenome.org/gene/9606:DOCK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YB76|||http://purl.uniprot.org/uniprot/Q5XG91|||http://purl.uniprot.org/uniprot/Q92608                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 2|||Disordered|||In IMD40.|||In isoform 2.|||Interaction with CRKL|||N6-acetyllysine|||Phosphoserine|||Polar residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189986|||http://purl.uniprot.org/annotation/VAR_015822|||http://purl.uniprot.org/annotation/VAR_022137|||http://purl.uniprot.org/annotation/VAR_053064|||http://purl.uniprot.org/annotation/VAR_073859|||http://purl.uniprot.org/annotation/VAR_073860|||http://purl.uniprot.org/annotation/VSP_007696|||http://purl.uniprot.org/annotation/VSP_007697|||http://purl.uniprot.org/annotation/VSP_007698|||http://purl.uniprot.org/annotation/VSP_007699|||http://purl.uniprot.org/annotation/VSP_007700
http://togogenome.org/gene/9606:FER1L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVI2|||http://purl.uniprot.org/uniprot/Q2NNQ7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  C2|||C2 1|||C2 2|||C2 3|||C2 4|||C2 5|||C2 6|||C2 7|||Fer-1-like protein 5|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300498|||http://purl.uniprot.org/annotation/VAR_059285|||http://purl.uniprot.org/annotation/VAR_059286|||http://purl.uniprot.org/annotation/VSP_031852|||http://purl.uniprot.org/annotation/VSP_059071
http://togogenome.org/gene/9606:ETV7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y603                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ETS|||In isoform A.|||In isoform C.|||In isoform D and isoform F.|||In isoform E and isoform F.|||In isoform G.|||In isoform H.|||PNT|||Transcription factor ETV7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204123|||http://purl.uniprot.org/annotation/VAR_020314|||http://purl.uniprot.org/annotation/VAR_048952|||http://purl.uniprot.org/annotation/VAR_048953|||http://purl.uniprot.org/annotation/VAR_048954|||http://purl.uniprot.org/annotation/VAR_059257|||http://purl.uniprot.org/annotation/VSP_001473|||http://purl.uniprot.org/annotation/VSP_001474|||http://purl.uniprot.org/annotation/VSP_001475|||http://purl.uniprot.org/annotation/VSP_001476|||http://purl.uniprot.org/annotation/VSP_001477|||http://purl.uniprot.org/annotation/VSP_044285
http://togogenome.org/gene/9606:OR2M4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV73|||http://purl.uniprot.org/uniprot/Q96R27                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2M4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150493
http://togogenome.org/gene/9606:SYNGAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8L0|||http://purl.uniprot.org/uniprot/B7ZCA0|||http://purl.uniprot.org/uniprot/Q96PV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||In MRD5; associated with autistic spectrum disorder and epileptic encephalopathy.|||In MRD5; associated with autistic spectrum disorder and epileptic encephalopathy; unknown pathological significance.|||In MRD5; moderate; associated with autistic spectrum disorder and epileptic encephalopathy.|||In MRD5; the disease phenotype consists of intellectual disability and autism; the mutant protein is less efficient in inhibiting ERK phosphorylation induced by neuronal activity.|||In MRD5; the disease phenotype consists of intellectual disability, autism and epilepsy; the mutant protein is less efficient in inhibiting ERK phosphorylation induced by neuronal activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PH|||Phosphoserine|||Phosphoserine; by PLK2|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Probable disease-associated variant found in a patient with West syndrome.|||Probable disease-associated variant found in a patient with drug-resistant generalized epilepsy, cognitive impairment and autism spectrum disorder.|||Ras-GAP|||Ras/Rap GTPase-activating protein SynGAP|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056654|||http://purl.uniprot.org/annotation/VAR_065078|||http://purl.uniprot.org/annotation/VAR_065079|||http://purl.uniprot.org/annotation/VAR_065080|||http://purl.uniprot.org/annotation/VAR_065081|||http://purl.uniprot.org/annotation/VAR_065082|||http://purl.uniprot.org/annotation/VAR_065083|||http://purl.uniprot.org/annotation/VAR_065084|||http://purl.uniprot.org/annotation/VAR_069232|||http://purl.uniprot.org/annotation/VAR_069233|||http://purl.uniprot.org/annotation/VAR_078233|||http://purl.uniprot.org/annotation/VAR_078234|||http://purl.uniprot.org/annotation/VAR_078616|||http://purl.uniprot.org/annotation/VAR_078617|||http://purl.uniprot.org/annotation/VAR_078618|||http://purl.uniprot.org/annotation/VSP_007973|||http://purl.uniprot.org/annotation/VSP_026376|||http://purl.uniprot.org/annotation/VSP_026377
http://togogenome.org/gene/9606:RADX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSI4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased binding to single-stranded DNA; when associated with E-240; 252-E--E-256; A-279; E-304; E-310 and A-327.|||Decreased binding to single-stranded DNA; when associated with E-240; E-248; 252-E--E-256; A-279; E-304 and A-327.|||Decreased binding to single-stranded DNA; when associated with E-240; E-248; 252-E--E-256; A-279; E-304 and E-310.|||Decreased binding to single-stranded DNA; when associated with E-240; E-248; 252-E--E-256; A-279; E-310 and A-327.|||Decreased binding to single-stranded DNA; when associated with E-240; E-248; 252-E--E-256; E-304; E-310 and A-327.|||Decreased binding to single-stranded DNA; when associated with E-240; E-248; A-279; E-304; E-310 and A-327.|||Decreased binding to single-stranded DNA; when associated with E-248; 252-E--E-256; A-279; E-304; E-310 and A-327.|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||OB|||Polar residues|||RPA-related protein RADX                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254127|||http://purl.uniprot.org/annotation/VAR_028816|||http://purl.uniprot.org/annotation/VSP_021182|||http://purl.uniprot.org/annotation/VSP_021183|||http://purl.uniprot.org/annotation/VSP_044983|||http://purl.uniprot.org/annotation/VSP_044984
http://togogenome.org/gene/9606:OR52D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVG9|||http://purl.uniprot.org/uniprot/Q9H346                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150770|||http://purl.uniprot.org/annotation/VAR_024146|||http://purl.uniprot.org/annotation/VAR_034331|||http://purl.uniprot.org/annotation/VAR_034332|||http://purl.uniprot.org/annotation/VAR_034333|||http://purl.uniprot.org/annotation/VAR_034334
http://togogenome.org/gene/9606:ASIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7X8|||http://purl.uniprot.org/uniprot/A0A090N8Q1|||http://purl.uniprot.org/uniprot/A0A090N8Z6|||http://purl.uniprot.org/uniprot/Q9UHC3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acid-sensing ion channel 3|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of interaction with GOPC. No effect on interaction LIN7B and MAGI1.|||Loss of interaction with LIN7B, MAGI1 and GOPC.|||Loss of interaction with LIN7B, MAGI1.|||N-linked (GlcNAc...) asparagine|||No effect on interaction with LIN7B, MAGI1 and GOPC.|||PDZ-binding|||Potassium ion selectivity and permeability                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181301|||http://purl.uniprot.org/annotation/VAR_052037|||http://purl.uniprot.org/annotation/VSP_015600|||http://purl.uniprot.org/annotation/VSP_015601|||http://purl.uniprot.org/annotation/VSP_015602|||http://purl.uniprot.org/annotation/VSP_015603
http://togogenome.org/gene/9606:KIR2DS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4ZN30|||http://purl.uniprot.org/uniprot/A0A1W2PR63|||http://purl.uniprot.org/uniprot/P43632|||http://purl.uniprot.org/uniprot/Q86VI6|||http://purl.uniprot.org/uniprot/Q8NHJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Immunoglobulin|||Immunoglobulin domain-containing protein|||Killer cell immunoglobulin-like receptor 2DS4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015085|||http://purl.uniprot.org/annotation/PRO_5004300508|||http://purl.uniprot.org/annotation/PRO_5010697950|||http://purl.uniprot.org/annotation/PRO_5014019457|||http://purl.uniprot.org/annotation/VAR_049980|||http://purl.uniprot.org/annotation/VAR_049981|||http://purl.uniprot.org/annotation/VAR_049982|||http://purl.uniprot.org/annotation/VAR_049983|||http://purl.uniprot.org/annotation/VAR_049984|||http://purl.uniprot.org/annotation/VAR_049985|||http://purl.uniprot.org/annotation/VAR_049986|||http://purl.uniprot.org/annotation/VAR_059423|||http://purl.uniprot.org/annotation/VAR_059424|||http://purl.uniprot.org/annotation/VAR_059425
http://togogenome.org/gene/9606:FAM220A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z4H9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein FAM220A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321923|||http://purl.uniprot.org/annotation/VAR_039375|||http://purl.uniprot.org/annotation/VAR_039376|||http://purl.uniprot.org/annotation/VAR_039377|||http://purl.uniprot.org/annotation/VAR_039378|||http://purl.uniprot.org/annotation/VAR_039379
http://togogenome.org/gene/9606:AKNAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1N1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein AKNAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342470|||http://purl.uniprot.org/annotation/VAR_044198|||http://purl.uniprot.org/annotation/VAR_044199|||http://purl.uniprot.org/annotation/VAR_044200|||http://purl.uniprot.org/annotation/VAR_044201|||http://purl.uniprot.org/annotation/VAR_044202|||http://purl.uniprot.org/annotation/VAR_044203|||http://purl.uniprot.org/annotation/VAR_044204|||http://purl.uniprot.org/annotation/VAR_061565|||http://purl.uniprot.org/annotation/VSP_034460|||http://purl.uniprot.org/annotation/VSP_034461|||http://purl.uniprot.org/annotation/VSP_034462|||http://purl.uniprot.org/annotation/VSP_034463|||http://purl.uniprot.org/annotation/VSP_034464
http://togogenome.org/gene/9606:MOV10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JR04|||http://purl.uniprot.org/uniprot/Q9HCE1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes 5' to 3' directional unwinding activity.|||Abolishes 5' to 3' directional unwinding activity. Abolishes inhibition of RNA chaperonne activity of LIRE1. No effect on interaction with UPF1.|||About 70% more antiviral activity against encephalomyocarditis virus replication; when associated with A-129.|||About 70% more antiviral activity against encephalomyocarditis virus replication; when associated with A-869.|||Almost complete lost of the ability to prevent the degradation of APOBEC3G mediated by HIV-1 Vif. Attenuated anti-HBV activity.|||Attenuated anti-HBV activity.|||DEAG box|||DNA2/NAM7 helicase-like C-terminal|||Disordered|||Helicase MOV-10|||In isoform 2.|||In isoform 3.|||Interaction with AGO2 and APOBEC3G|||Loss of interaction with DCAF12 and proteasomal degradation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080704|||http://purl.uniprot.org/annotation/VSP_010943|||http://purl.uniprot.org/annotation/VSP_010944|||http://purl.uniprot.org/annotation/VSP_037305|||http://purl.uniprot.org/annotation/VSP_037306
http://togogenome.org/gene/9606:GATAD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YP4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||CR1; interaction with HDAC1, HDAC2, MBD2 and MTA2|||CR2; histone tail-binding and interaction with CHD4 and CDK2AP1|||Disordered|||Disruption of MBD2-binding, loss of enhancement of MBD2-mediated repression and loss of speckled nuclear localization.|||GATA-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Interaction with ZMYND8|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcriptional repressor p66-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083500|||http://purl.uniprot.org/annotation/VAR_059308|||http://purl.uniprot.org/annotation/VAR_059309|||http://purl.uniprot.org/annotation/VSP_010929|||http://purl.uniprot.org/annotation/VSP_053410
http://togogenome.org/gene/9606:VIRMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q69YN4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Protein virilizer homolog|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308605|||http://purl.uniprot.org/annotation/VAR_036845|||http://purl.uniprot.org/annotation/VSP_029017|||http://purl.uniprot.org/annotation/VSP_029018|||http://purl.uniprot.org/annotation/VSP_029019|||http://purl.uniprot.org/annotation/VSP_029020|||http://purl.uniprot.org/annotation/VSP_029021
http://togogenome.org/gene/9606:NPIPA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WFD2|||http://purl.uniprot.org/uniprot/O15103                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Nuclear pore complex-interacting protein family member A3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423917
http://togogenome.org/gene/9606:LILRA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59901                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3'-nitrotyrosine|||Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||Leukocyte immunoglobulin-like receptor subfamily A member 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014819|||http://purl.uniprot.org/annotation/VAR_056054|||http://purl.uniprot.org/annotation/VAR_056055|||http://purl.uniprot.org/annotation/VSP_038694
http://togogenome.org/gene/9606:PITRM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRX9|||http://purl.uniprot.org/uniprot/A0A7I2V397|||http://purl.uniprot.org/uniprot/Q5JRX3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Decreased metalloendopeptidase activity towards an amyloid-beta peptide derivative.|||Decreased metalloendopeptidase activity without effect on protein stability.|||Disordered|||In SCAR30; decreased function in degradation of amyloid-beta protein 40; decreased metalloendopeptidase activity towards different substrates including an amyloid-beta peptide derivative; decreased protein levels in patient tissues; no effect on mitochondrial localization.|||In SCAR30; strongly decreased metalloendopeptidase activity towards amyloid-beta protein 40 and amyloid-beta protein 42.|||In isoform 2.|||In isoform 3.|||Loss of localization to the mitochondrion.|||Loss of metalloendopeptidase activity towards an amyloid-beta peptide derivative.|||Loss of metalloendopeptidase activity. Loss of activity towards an amyloid-beta peptide derivative.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No effect on metalloendopeptidase activity towards an amyloid-beta peptide derivative.|||No loss of metalloendopeptidase activity under oxidizing conditions.|||Peptidase M16C associated|||Presequence protease, mitochondrial|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249931|||http://purl.uniprot.org/annotation/VAR_027517|||http://purl.uniprot.org/annotation/VAR_027518|||http://purl.uniprot.org/annotation/VAR_027519|||http://purl.uniprot.org/annotation/VAR_027520|||http://purl.uniprot.org/annotation/VAR_027521|||http://purl.uniprot.org/annotation/VAR_027522|||http://purl.uniprot.org/annotation/VAR_027523|||http://purl.uniprot.org/annotation/VAR_027524|||http://purl.uniprot.org/annotation/VAR_027525|||http://purl.uniprot.org/annotation/VAR_027526|||http://purl.uniprot.org/annotation/VAR_027527|||http://purl.uniprot.org/annotation/VAR_057059|||http://purl.uniprot.org/annotation/VAR_057060|||http://purl.uniprot.org/annotation/VAR_085987|||http://purl.uniprot.org/annotation/VAR_085988|||http://purl.uniprot.org/annotation/VSP_020597|||http://purl.uniprot.org/annotation/VSP_046494|||http://purl.uniprot.org/annotation/VSP_046495
http://togogenome.org/gene/9606:CDH16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75309                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin-16|||Cytoplasmic|||Ectodomain G|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003809|||http://purl.uniprot.org/annotation/VAR_021870|||http://purl.uniprot.org/annotation/VAR_021871|||http://purl.uniprot.org/annotation/VAR_061058|||http://purl.uniprot.org/annotation/VSP_013354|||http://purl.uniprot.org/annotation/VSP_046027|||http://purl.uniprot.org/annotation/VSP_046467
http://togogenome.org/gene/9606:PLD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2A8                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type; atypical|||Cytoplasmic|||Helical|||Mitochondrial cardiolipin hydrolase|||Mitochondrial fragmentation. No apoptosis, no alterations of cell homeostasis.|||Mitochondrial intermembrane|||PLD phosphodiesterase|||Required for mitochondrial localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325910|||http://purl.uniprot.org/annotation/VAR_039951|||http://purl.uniprot.org/annotation/VAR_039952
http://togogenome.org/gene/9606:COASY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13057                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Bifunctional coenzyme A synthase|||DPCK|||In NBIA6; reduced protein abundance.|||In NBIA6; reduced protein abundance; loss of dephospho-CoA kinase activity.|||In NBIA6; unknown pathological significance.|||In isoform 2.|||Phosphopantetheine adenylyltransferase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173039|||http://purl.uniprot.org/annotation/VAR_030299|||http://purl.uniprot.org/annotation/VAR_070975|||http://purl.uniprot.org/annotation/VAR_082222|||http://purl.uniprot.org/annotation/VAR_082223|||http://purl.uniprot.org/annotation/VSP_036404
http://togogenome.org/gene/9606:TRIM72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||In isoform 2.|||Interchain|||No decrease in level upon treatment with hydrogen peroxide.|||Phosphoserine|||RING-type|||S-nitrosocysteine|||Tripartite motif-containing protein 72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278130|||http://purl.uniprot.org/annotation/VSP_052318
http://togogenome.org/gene/9606:ALKBH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13686|||http://purl.uniprot.org/uniprot/Q5XKL0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Does not affect DNA lyase activity.|||Does not affect DNA lyase activity. Strongly reduced activity; when associated with A-133.|||Fe2OG dioxygenase|||Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity.|||Loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c). Abolished DNAN6-methyl adenine demethylase activity.|||Loss of catalytic activity. Abolishes ability to regulate translation in respose to glucose deprivation.|||Moderate decrease in DNA lyase activity. Reduced DNA lyase activity; when associated with A-133.|||Near loss of Fe2OG dioxygenase activity. No effect on DNA lyase activity.|||Nucleic acid dioxygenase ALKBH1|||Primary catalytic residue forming the imine linkage with DNA|||Reduced DNA lyase activity. Slightly more reduced DNA lyase activity; when associated with A-25. Strongly reduced activity; when associated with A-154.|||Reduced Fe2OG dioxygenase activity.|||Reduced Fe2OG dioxygenase activity. Abolishes ability to mediate oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c).|||Reduces Fe2OG dioxygenase activity by 50%.|||Secondary catalytic residue forming the imine linkage with DNA|||tRNA-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066668|||http://purl.uniprot.org/annotation/VAR_048221|||http://purl.uniprot.org/annotation/VAR_048222
http://togogenome.org/gene/9606:OXSM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3Q7|||http://purl.uniprot.org/uniprot/Q9NWU1                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial|||For beta-ketoacyl synthase activity|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Ketosynthase family 3 (KS3)|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232660|||http://purl.uniprot.org/annotation/VAR_036064|||http://purl.uniprot.org/annotation/VSP_041671
http://togogenome.org/gene/9606:ZFP30                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D3Y2A0|||http://purl.uniprot.org/uniprot/Q9Y2G7                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5; degenerate|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 30 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047291
http://togogenome.org/gene/9606:HNRNPLL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z6K1|||http://purl.uniprot.org/uniprot/A8K894|||http://purl.uniprot.org/uniprot/Q8WVV9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Heterogeneous nuclear ribonucleoprotein L-like|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081609|||http://purl.uniprot.org/annotation/VSP_013285|||http://purl.uniprot.org/annotation/VSP_013286|||http://purl.uniprot.org/annotation/VSP_013287|||http://purl.uniprot.org/annotation/VSP_013288|||http://purl.uniprot.org/annotation/VSP_013289|||http://purl.uniprot.org/annotation/VSP_054470
http://togogenome.org/gene/9606:SMPDL3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEC6|||http://purl.uniprot.org/uniprot/B4DW34|||http://purl.uniprot.org/uniprot/Q92485                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acid sphingomyelinase-like phosphodiesterase|||Acid sphingomyelinase-like phosphodiesterase 3b|||Calcineurin-like phosphoesterase|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reduced phosphodiesterase activity.|||Sphingomyelin phosphodiesterase C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002331|||http://purl.uniprot.org/annotation/PRO_5014212952|||http://purl.uniprot.org/annotation/VAR_048340|||http://purl.uniprot.org/annotation/VSP_013478|||http://purl.uniprot.org/annotation/VSP_013479
http://togogenome.org/gene/9606:TTLL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KQB2|||http://purl.uniprot.org/uniprot/Q9Y4R7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Essential for specifying initiation versus elongation step of the glycylase activity|||In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||TTL|||Tubulin monoglycylase TTLL3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212441|||http://purl.uniprot.org/annotation/VAR_020207|||http://purl.uniprot.org/annotation/VAR_036054|||http://purl.uniprot.org/annotation/VAR_036055|||http://purl.uniprot.org/annotation/VAR_052410|||http://purl.uniprot.org/annotation/VAR_052411|||http://purl.uniprot.org/annotation/VAR_052412|||http://purl.uniprot.org/annotation/VSP_032567|||http://purl.uniprot.org/annotation/VSP_032568|||http://purl.uniprot.org/annotation/VSP_032572|||http://purl.uniprot.org/annotation/VSP_032573|||http://purl.uniprot.org/annotation/VSP_032576|||http://purl.uniprot.org/annotation/VSP_032577
http://togogenome.org/gene/9606:CPNE9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-9|||Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277583|||http://purl.uniprot.org/annotation/VSP_039523
http://togogenome.org/gene/9606:CHCHD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4Q1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Affects import and stability of CHCHD4 in mitochondria; when associated with S-64. No effect on interaction with AIFM1.|||Affects import and stability of CHCHD4 in mitochondria; when associated with S-74.|||CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||Does not strongly affect import and stability of CHCHD4 in mitochondria; when associated with S-53. Nearly abolishes disulfide exchange with substrate proteins. Abolishes interaction with COA7.|||Does not strongly affect import and stability of CHCHD4 in mitochondria; when associated with S-55. No effect on disulfide exchange with substrate proteins. Does not affect interaction with COA7. No effect on interaction with AIFM1.|||In isoform 2.|||Mitochondrial intermembrane space import and assembly protein 40|||No effect on interaction with AIFM1.|||Redox-active|||Strongly affects import and stability of CHCHD4 in mitochondria; when associated with S-87. No effect on interaction with AIFM1.|||Strongly affects import and stability of CHCHD4 in mitochondria; when associated with S-97. No effect on interaction with AIFM1.|||Sufficient for interaction with AIFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129165|||http://purl.uniprot.org/annotation/VSP_018433
http://togogenome.org/gene/9606:DERL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q80                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Derlin-3|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lumenal|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219048|||http://purl.uniprot.org/annotation/VAR_019517|||http://purl.uniprot.org/annotation/VAR_048897|||http://purl.uniprot.org/annotation/VSP_011086|||http://purl.uniprot.org/annotation/VSP_011087|||http://purl.uniprot.org/annotation/VSP_011088|||http://purl.uniprot.org/annotation/VSP_011089|||http://purl.uniprot.org/annotation/VSP_046330
http://togogenome.org/gene/9606:BCHE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06276                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Acyl-ester intermediate|||Charge relay system|||Cholinesterase|||Does not affect enzymatic activity.|||Does not affect enzyme activity.|||In BCHED.|||In BCHED; BChE variant form; fluoride-resistant.|||In BCHED; allele H variant.|||In BCHED; allele J variant.|||In BCHED; allele K variant; with reduced enzyme activity.|||In BCHED; allele fluoride-1.|||In BCHED; allele fluoride-2.|||In BCHED; atypical form; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of V-62 or at homozygosity.|||In BCHED; enzymatically inactive in the plasma.|||In BCHED; expressed at very low level.|||In BCHED; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of G-98; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of G-98.|||In BCHED; reduced enzyme activity.|||In BCHED; results in 20% of activity compared to wild-type.|||In BCHED; seems to cause reduced expression of the protein.|||In BCHED; the mutant undergoes rapid degradation.|||Interchain|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008613|||http://purl.uniprot.org/annotation/VAR_002360|||http://purl.uniprot.org/annotation/VAR_002362|||http://purl.uniprot.org/annotation/VAR_002364|||http://purl.uniprot.org/annotation/VAR_040011|||http://purl.uniprot.org/annotation/VAR_040012|||http://purl.uniprot.org/annotation/VAR_040013|||http://purl.uniprot.org/annotation/VAR_040014|||http://purl.uniprot.org/annotation/VAR_040015|||http://purl.uniprot.org/annotation/VAR_040016|||http://purl.uniprot.org/annotation/VAR_040017|||http://purl.uniprot.org/annotation/VAR_040018|||http://purl.uniprot.org/annotation/VAR_040019|||http://purl.uniprot.org/annotation/VAR_040020|||http://purl.uniprot.org/annotation/VAR_040021|||http://purl.uniprot.org/annotation/VAR_040022|||http://purl.uniprot.org/annotation/VAR_040023|||http://purl.uniprot.org/annotation/VAR_040024|||http://purl.uniprot.org/annotation/VAR_040025|||http://purl.uniprot.org/annotation/VAR_040026|||http://purl.uniprot.org/annotation/VAR_040027|||http://purl.uniprot.org/annotation/VAR_040028|||http://purl.uniprot.org/annotation/VAR_040029|||http://purl.uniprot.org/annotation/VAR_040030|||http://purl.uniprot.org/annotation/VAR_040031|||http://purl.uniprot.org/annotation/VAR_040032|||http://purl.uniprot.org/annotation/VAR_040033|||http://purl.uniprot.org/annotation/VAR_040034|||http://purl.uniprot.org/annotation/VAR_040035|||http://purl.uniprot.org/annotation/VAR_040036|||http://purl.uniprot.org/annotation/VAR_040037|||http://purl.uniprot.org/annotation/VAR_040038|||http://purl.uniprot.org/annotation/VAR_040039|||http://purl.uniprot.org/annotation/VAR_040040|||http://purl.uniprot.org/annotation/VAR_040041|||http://purl.uniprot.org/annotation/VAR_040042|||http://purl.uniprot.org/annotation/VAR_072094|||http://purl.uniprot.org/annotation/VAR_072095|||http://purl.uniprot.org/annotation/VAR_072096|||http://purl.uniprot.org/annotation/VAR_072097|||http://purl.uniprot.org/annotation/VAR_072098|||http://purl.uniprot.org/annotation/VAR_072099|||http://purl.uniprot.org/annotation/VAR_072100|||http://purl.uniprot.org/annotation/VAR_072101|||http://purl.uniprot.org/annotation/VAR_072730
http://togogenome.org/gene/9606:LBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18428|||http://purl.uniprot.org/uniprot/Q8TCF0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Abolishes lipopolysaccharide binding and causes increased proteolytic degradation of the protein.|||Lipid-binding serum glycoprotein C-terminal|||Lipid-binding serum glycoprotein N-terminal|||Lipopolysaccharide-binding protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017158|||http://purl.uniprot.org/annotation/PRO_5004315150|||http://purl.uniprot.org/annotation/VAR_028243|||http://purl.uniprot.org/annotation/VAR_028244|||http://purl.uniprot.org/annotation/VAR_028245|||http://purl.uniprot.org/annotation/VAR_028246|||http://purl.uniprot.org/annotation/VAR_028247|||http://purl.uniprot.org/annotation/VAR_028248|||http://purl.uniprot.org/annotation/VAR_028249|||http://purl.uniprot.org/annotation/VAR_028250|||http://purl.uniprot.org/annotation/VAR_028251|||http://purl.uniprot.org/annotation/VAR_028252|||http://purl.uniprot.org/annotation/VAR_049737|||http://purl.uniprot.org/annotation/VAR_049738|||http://purl.uniprot.org/annotation/VAR_049739|||http://purl.uniprot.org/annotation/VAR_061293
http://togogenome.org/gene/9606:PRAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KF2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Small nuclear protein PRAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312417|||http://purl.uniprot.org/annotation/VAR_051285
http://togogenome.org/gene/9606:NECAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6G3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ABM|||Asymmetric dimethylarginine|||EF-hand 1|||EF-hand 2|||In isoform 2.|||N-terminal EF-hand calcium-binding protein 2|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282613|||http://purl.uniprot.org/annotation/VAR_048639|||http://purl.uniprot.org/annotation/VAR_048640|||http://purl.uniprot.org/annotation/VAR_048641|||http://purl.uniprot.org/annotation/VAR_048642|||http://purl.uniprot.org/annotation/VSP_058936
http://togogenome.org/gene/9606:IGLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15814                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C region|||Ig-like C1-type|||Immunoglobulin lambda-like polypeptide 1|||In AGM2.|||In isoform 2.|||Interchain (with a heavy chain)|||J region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014777|||http://purl.uniprot.org/annotation/VAR_034869|||http://purl.uniprot.org/annotation/VAR_059392|||http://purl.uniprot.org/annotation/VSP_042748
http://togogenome.org/gene/9606:C2CD4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCU7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||C2 calcium-dependent domain-containing protein 4A|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324305
http://togogenome.org/gene/9606:SERPINA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01011                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-1-antichymotrypsin|||Alpha-1-antichymotrypsin His-Pro-less|||Associated with occlusive-cerebrovascular disease; Isehara-1.|||In Bochum-1.|||In Bonn-1.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||RCL|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032411|||http://purl.uniprot.org/annotation/PRO_0000032412|||http://purl.uniprot.org/annotation/VAR_006973|||http://purl.uniprot.org/annotation/VAR_006974|||http://purl.uniprot.org/annotation/VAR_006975|||http://purl.uniprot.org/annotation/VAR_006976|||http://purl.uniprot.org/annotation/VAR_006977|||http://purl.uniprot.org/annotation/VAR_011742|||http://purl.uniprot.org/annotation/VAR_037902|||http://purl.uniprot.org/annotation/VSP_014225|||http://purl.uniprot.org/annotation/VSP_014226|||http://purl.uniprot.org/annotation/VSP_014227|||http://purl.uniprot.org/annotation/VSP_014228
http://togogenome.org/gene/9606:BEGAIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BUH8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Brain-enriched guanylate kinase-associated protein|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064904
http://togogenome.org/gene/9606:SOX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48436                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD 1|||9aaTAD 2|||9aaTAD 3|||Basic and acidic residues|||Dimerization (DIM)|||Disordered|||Does not affect ability to activate transcription in vitro.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HMG box|||Impaired ability to activate transcription in vitro.|||Impaired, but not abolished, ability to activate transcription in vitro.|||In CMD1.|||In CMD1; 17% of wild-type DNA binding activity; shows a 2-fold reduction in nuclear import efficiency; transcriptional activation is only reduced to 62% of wild-type activity.|||In CMD1; 5% of wild-type DNA binding activity; transcriptional activation is only reduced to 26% of wild-type activity.|||In CMD1; almost no loss of DNA binding.|||In CMD1; decreased 75% transactivational activity.|||In CMD1; dimerization and the resulting capacity to activate promoters via dimeric binding sites is lost; other features of the protein function remain unaltered.|||In CMD1; loss of DNA binding.|||In CMD1; mild form overlapping with small patella syndrome; decreased 50% transactivational activity.|||In CMD1; residual DNA binding and transactivation of regulated genes.|||PQA|||Phosphoserine|||Polar residues|||Pro residues|||Transactivation domain (TAC)|||Transactivation domain (TAM)|||Transcription factor SOX-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048739|||http://purl.uniprot.org/annotation/VAR_003735|||http://purl.uniprot.org/annotation/VAR_003736|||http://purl.uniprot.org/annotation/VAR_003737|||http://purl.uniprot.org/annotation/VAR_003738|||http://purl.uniprot.org/annotation/VAR_003739|||http://purl.uniprot.org/annotation/VAR_003740|||http://purl.uniprot.org/annotation/VAR_003741|||http://purl.uniprot.org/annotation/VAR_003742|||http://purl.uniprot.org/annotation/VAR_008529|||http://purl.uniprot.org/annotation/VAR_008530|||http://purl.uniprot.org/annotation/VAR_008531|||http://purl.uniprot.org/annotation/VAR_063642|||http://purl.uniprot.org/annotation/VAR_063643|||http://purl.uniprot.org/annotation/VAR_063644|||http://purl.uniprot.org/annotation/VAR_063645|||http://purl.uniprot.org/annotation/VAR_063646|||http://purl.uniprot.org/annotation/VAR_063647|||http://purl.uniprot.org/annotation/VAR_078490|||http://purl.uniprot.org/annotation/VAR_078491|||http://purl.uniprot.org/annotation/VAR_078492|||http://purl.uniprot.org/annotation/VAR_083521
http://togogenome.org/gene/9606:TNN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXB6|||http://purl.uniprot.org/uniprot/Q9UQP3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Fibrinogen C-terminal|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||N-linked (GlcNAc...) asparagine|||Tenascin-N                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007745|||http://purl.uniprot.org/annotation/PRO_5002788471|||http://purl.uniprot.org/annotation/VAR_024269|||http://purl.uniprot.org/annotation/VAR_033832|||http://purl.uniprot.org/annotation/VAR_033833|||http://purl.uniprot.org/annotation/VAR_033834|||http://purl.uniprot.org/annotation/VAR_033835|||http://purl.uniprot.org/annotation/VAR_049007|||http://purl.uniprot.org/annotation/VAR_049008|||http://purl.uniprot.org/annotation/VAR_049009|||http://purl.uniprot.org/annotation/VAR_049010|||http://purl.uniprot.org/annotation/VAR_059275
http://togogenome.org/gene/9606:DNAJC17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVM6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 17|||J|||N6-methyllysine|||Phosphoserine|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247118
http://togogenome.org/gene/9606:HMGCL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35914                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.|||Hydroxymethylglutaryl-CoA lyase, mitochondrial|||In HMGCLD.|||In HMGCLD; abolishes almost all enzymatic activity.|||In HMGCLD; activity lower than 5% respect to the wild-type.|||In HMGCLD; complete loss of activity.|||In HMGCLD; loss of activity and of proton exchange.|||In HMGCLD; loss of activity.|||In HMGCLD; reduced activity.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interchain|||Loss of activity, and reduced affinity for metal cofactor and substrate.|||Loss of activity, and reduced proton exchange rate.|||Loss of activity.|||Microbody targeting signal|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Normal activity.|||Pyruvate carboxyltransferase|||Reduced activity, and loss of proton exchange.|||Reduced activity, and reduced affinity for metal cofactor and substrate.|||Reduced thermal stability, but normal activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013478|||http://purl.uniprot.org/annotation/VAR_003744|||http://purl.uniprot.org/annotation/VAR_003745|||http://purl.uniprot.org/annotation/VAR_003746|||http://purl.uniprot.org/annotation/VAR_003747|||http://purl.uniprot.org/annotation/VAR_003748|||http://purl.uniprot.org/annotation/VAR_003749|||http://purl.uniprot.org/annotation/VAR_014202|||http://purl.uniprot.org/annotation/VAR_058440|||http://purl.uniprot.org/annotation/VAR_058441|||http://purl.uniprot.org/annotation/VAR_058442|||http://purl.uniprot.org/annotation/VAR_058443|||http://purl.uniprot.org/annotation/VAR_058444|||http://purl.uniprot.org/annotation/VAR_058445|||http://purl.uniprot.org/annotation/VAR_058446|||http://purl.uniprot.org/annotation/VAR_058447|||http://purl.uniprot.org/annotation/VAR_058448|||http://purl.uniprot.org/annotation/VAR_058449|||http://purl.uniprot.org/annotation/VAR_058450|||http://purl.uniprot.org/annotation/VAR_065453|||http://purl.uniprot.org/annotation/VSP_043788|||http://purl.uniprot.org/annotation/VSP_047444
http://togogenome.org/gene/9606:FARSA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IBR2|||http://purl.uniprot.org/uniprot/Q9Y285                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminoacyl-transfer RNA synthetases class-II family profile|||In RILDBC2; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Phenylalanine--tRNA ligase alpha subunit|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126824|||http://purl.uniprot.org/annotation/VAR_052641|||http://purl.uniprot.org/annotation/VAR_084994|||http://purl.uniprot.org/annotation/VAR_084995|||http://purl.uniprot.org/annotation/VSP_056196
http://togogenome.org/gene/9606:POTEA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S8J7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic and acidic residues|||Disordered|||In isoform 2.|||POTE ankyrin domain family member A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066915|||http://purl.uniprot.org/annotation/VSP_011974
http://togogenome.org/gene/9606:CCL16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15467                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005209
http://togogenome.org/gene/9606:GRK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32298                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||G protein-coupled receptor kinase 4|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||N-acetylmethionine|||N-terminal|||Phosphoserine|||Protein kinase|||Proton acceptor|||RGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085967|||http://purl.uniprot.org/annotation/VAR_007806|||http://purl.uniprot.org/annotation/VAR_024573|||http://purl.uniprot.org/annotation/VAR_024574|||http://purl.uniprot.org/annotation/VAR_024575|||http://purl.uniprot.org/annotation/VAR_040516|||http://purl.uniprot.org/annotation/VAR_046043|||http://purl.uniprot.org/annotation/VAR_046044|||http://purl.uniprot.org/annotation/VAR_046045|||http://purl.uniprot.org/annotation/VAR_046046|||http://purl.uniprot.org/annotation/VAR_051621|||http://purl.uniprot.org/annotation/VAR_051622|||http://purl.uniprot.org/annotation/VAR_051623|||http://purl.uniprot.org/annotation/VSP_004936|||http://purl.uniprot.org/annotation/VSP_004937
http://togogenome.org/gene/9606:TPPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59282                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Tubulin polymerization-promoting protein family member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221137|||http://purl.uniprot.org/annotation/VAR_059147
http://togogenome.org/gene/9606:SNRNP40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0MNP2|||http://purl.uniprot.org/uniprot/Q96DI7                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||U5 small nuclear ribonucleoprotein 40 kDa protein|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051417|||http://purl.uniprot.org/annotation/VSP_056395
http://togogenome.org/gene/9606:CHN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15882                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  In DURS2; behaves as a dominant gain-of -function allele that increases CHN1 activity in vitro.|||In DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro.|||In DURS2; behaves as a dominant gain-of-function allele that increases CHN1 activity in vitro; appears to enhance membrane translocation and CHN1 activity by destabilizing the closed conformation of CHN1 protein in response to phorbol 12-myristate 13-acetate (PMA).|||In isoform 3.|||In isoform Alpha-1.|||N-acetylalanine|||N-chimaerin|||Phorbol-ester/DAG-type|||Phosphothreonine|||Removed|||Rho-GAP|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056694|||http://purl.uniprot.org/annotation/VAR_047940|||http://purl.uniprot.org/annotation/VAR_047941|||http://purl.uniprot.org/annotation/VAR_047942|||http://purl.uniprot.org/annotation/VAR_047943|||http://purl.uniprot.org/annotation/VAR_047944|||http://purl.uniprot.org/annotation/VAR_047945|||http://purl.uniprot.org/annotation/VAR_047946|||http://purl.uniprot.org/annotation/VSP_001636|||http://purl.uniprot.org/annotation/VSP_043297
http://togogenome.org/gene/9606:LARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6I8PL42|||http://purl.uniprot.org/uniprot/B4DER1|||http://purl.uniprot.org/uniprot/B4E266|||http://purl.uniprot.org/uniprot/Q9P2J5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Aminoacyl-tRNA synthetase class Ia|||Editing domain|||In ILFS1.|||In isoform 2.|||In isoform 3.|||Leucine--tRNA ligase, cytoplasmic|||Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152150|||http://purl.uniprot.org/annotation/VAR_052637|||http://purl.uniprot.org/annotation/VAR_070437|||http://purl.uniprot.org/annotation/VAR_070438|||http://purl.uniprot.org/annotation/VSP_057204|||http://purl.uniprot.org/annotation/VSP_057205
http://togogenome.org/gene/9606:FHL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TD97                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||Four and a half LIM domains protein 5|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075742|||http://purl.uniprot.org/annotation/VAR_022824|||http://purl.uniprot.org/annotation/VAR_056160|||http://purl.uniprot.org/annotation/VAR_056161|||http://purl.uniprot.org/annotation/VAR_056162
http://togogenome.org/gene/9606:OR10T2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV74|||http://purl.uniprot.org/uniprot/Q8NGX3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10T2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150717|||http://purl.uniprot.org/annotation/VAR_053284|||http://purl.uniprot.org/annotation/VAR_053285|||http://purl.uniprot.org/annotation/VAR_053286|||http://purl.uniprot.org/annotation/VAR_053287|||http://purl.uniprot.org/annotation/VAR_053288|||http://purl.uniprot.org/annotation/VAR_053289
http://togogenome.org/gene/9606:ZNF280B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SEJ8|||http://purl.uniprot.org/uniprot/B3KUN2|||http://purl.uniprot.org/uniprot/Q86YH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Zinc finger protein 280B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047056|||http://purl.uniprot.org/annotation/VAR_028013|||http://purl.uniprot.org/annotation/VAR_028014
http://togogenome.org/gene/9606:RAPGEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4G8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes cAMP-binding.|||Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1406.|||Abolishes interaction with NEDD4 and NEDD4-induced ubiquitination and degradation; when associated with A-1428.|||Abolishes interaction with RAP1AGTP-bound form and translocation from the cytoplasm to the perinuclear region. Does not abolish GEF activity on RAP1A.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not abolish cAMP-binding.|||Does not inhibit interaction with NEDD4. Does not interact with HRAS. Reduces ubiquitination.|||Loss of cell membrane targeting.|||N-terminal Ras-GEF|||No loss of cell membrane targeting.|||PDZ|||Phosphoserine|||Phosphoserine; by PLK2|||Phosphothreonine; by PLK2|||Polar residues|||Rap guanine nucleotide exchange factor 2|||Ras-GEF|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068865
http://togogenome.org/gene/9606:B3GNT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFL0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264618|||http://purl.uniprot.org/annotation/VAR_029633
http://togogenome.org/gene/9606:NSMCE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with EID3.|||Basic and acidic residues|||Decreases interaction with NSMCE1, no effect on interaction with NSMCE4A, abolishes in vitro promotion of NSMCE1 ubiquitin ligase activity.|||Disordered|||In LICS; creates novel endoproteolytic cleavage sites compared to wild-type; loss of interaction with NSMCE4; loss of interaction with NSMCE1.|||In LICS; no loss of protein stability; loss of interaction with NSMCE4; decreased interaction with NSMCE1; decreased association with the SMC5-SMC6 complex; decreased DNA repair.|||Interaction with NSMCE1|||MAGE|||Non-structural maintenance of chromosomes element 3 homolog|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156733|||http://purl.uniprot.org/annotation/VAR_078021|||http://purl.uniprot.org/annotation/VAR_078022
http://togogenome.org/gene/9606:CRYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2S2|||http://purl.uniprot.org/uniprot/V9HWG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyacyl-CoA dehydrogenase C-terminal|||3-hydroxyacyl-CoA dehydrogenase NAD binding|||Important for catalytic activity|||In isoform 2.|||Lambda-crystallin homolog|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109320|||http://purl.uniprot.org/annotation/VSP_034641
http://togogenome.org/gene/9606:NPY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D158|||http://purl.uniprot.org/uniprot/P01303                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  C-flanking peptide of NPY|||Cleavage; by FAP|||Neuropeptide Y|||Phosphothreonine|||Tyrosine amide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025321|||http://purl.uniprot.org/annotation/PRO_0000025322|||http://purl.uniprot.org/annotation/PRO_5014296874|||http://purl.uniprot.org/annotation/VAR_014598|||http://purl.uniprot.org/annotation/VAR_014599
http://togogenome.org/gene/9606:EGF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01133                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9|||Epidermal growth factor|||Extracellular|||Helical|||In HOMG4; affects basolateral sorting of pro-EGF preventing the hormone to stimulate EGFR; lack of TRPM6 activation.|||In isoform 2.|||In isoform 3.|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||Pro-epidermal growth factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007540|||http://purl.uniprot.org/annotation/PRO_0000007541|||http://purl.uniprot.org/annotation/VAR_002275|||http://purl.uniprot.org/annotation/VAR_020161|||http://purl.uniprot.org/annotation/VAR_020162|||http://purl.uniprot.org/annotation/VAR_020163|||http://purl.uniprot.org/annotation/VAR_020164|||http://purl.uniprot.org/annotation/VAR_020165|||http://purl.uniprot.org/annotation/VAR_020166|||http://purl.uniprot.org/annotation/VAR_020968|||http://purl.uniprot.org/annotation/VAR_020969|||http://purl.uniprot.org/annotation/VAR_020970|||http://purl.uniprot.org/annotation/VAR_020971|||http://purl.uniprot.org/annotation/VAR_020972|||http://purl.uniprot.org/annotation/VAR_033825|||http://purl.uniprot.org/annotation/VAR_033826|||http://purl.uniprot.org/annotation/VAR_039474|||http://purl.uniprot.org/annotation/VSP_041586|||http://purl.uniprot.org/annotation/VSP_047190
http://togogenome.org/gene/9606:ZNF418                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1P3|||http://purl.uniprot.org/uniprot/B7Z993|||http://purl.uniprot.org/uniprot/J3KQR4|||http://purl.uniprot.org/uniprot/M0QX82|||http://purl.uniprot.org/uniprot/Q8TF45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 418                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047573
http://togogenome.org/gene/9606:LCE4A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA78                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 4A|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235338|||http://purl.uniprot.org/annotation/VAR_053486
http://togogenome.org/gene/9606:PXT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFP0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Sequence Conflict                                                                                  ^@                                                                                  Microbody targeting signal|||Peroxisomal testis-specific protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324593
http://togogenome.org/gene/9606:MRPL11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3B7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Large ribosomal subunit protein uL11m|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030443|||http://purl.uniprot.org/annotation/VSP_041077|||http://purl.uniprot.org/annotation/VSP_045237
http://togogenome.org/gene/9606:PACRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M98                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||Parkin coregulated gene protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058169|||http://purl.uniprot.org/annotation/VSP_010033
http://togogenome.org/gene/9606:LOC730098                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V523                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ERAS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z444                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Propeptide|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||GTPase ERas|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247538|||http://purl.uniprot.org/annotation/PRO_0000247539
http://togogenome.org/gene/9606:S100A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06703                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Protein S100-A6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143984|||http://purl.uniprot.org/annotation/VAR_011982|||http://purl.uniprot.org/annotation/VAR_011983|||http://purl.uniprot.org/annotation/VAR_011984|||http://purl.uniprot.org/annotation/VAR_029281
http://togogenome.org/gene/9606:PPIG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13427                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase G|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064150|||http://purl.uniprot.org/annotation/VAR_055084|||http://purl.uniprot.org/annotation/VAR_055085|||http://purl.uniprot.org/annotation/VSP_009662|||http://purl.uniprot.org/annotation/VSP_009663
http://togogenome.org/gene/9606:WAPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K273|||http://purl.uniprot.org/uniprot/B2RTX8|||http://purl.uniprot.org/uniprot/Q7Z5K2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FGF motif 1|||FGF motif 2|||FGF motif 3|||Found in a patient with cohesinopathy; unknown pathological significance.|||Impaired sister chromatid cohesion and resolution.|||Impaired sister chromatid cohesion and resolution; when associated with A-1116.|||Impaired sister chromatid cohesion and resolution; when associated with A-1120.|||In isoform 2.|||In isoform 3.|||Loss of interaction with PDS5B; when associated with 429-E--E-431 and 453-E--E-455.|||Loss of interaction with PDS5B; when associated with 73-E--E-75 and 429-E--E-431.|||Loss of interaction with PDS5B; when associated with 73-E--E-75 and 453-E--E-455.|||Mediates interaction with the cohesin complex|||N6-acetyllysine|||No effect.|||Phosphoserine|||Polar residues|||WAPL|||Wings apart-like protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245232|||http://purl.uniprot.org/annotation/VAR_026967|||http://purl.uniprot.org/annotation/VAR_082314|||http://purl.uniprot.org/annotation/VSP_019649|||http://purl.uniprot.org/annotation/VSP_019650|||http://purl.uniprot.org/annotation/VSP_019651
http://togogenome.org/gene/9606:PRAMEF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TYX0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  LRR 1; degenerate|||LRR 2; degenerate|||LRR 3; degenerate|||LRR 4; degenerate|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||PRAME family member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156979
http://togogenome.org/gene/9606:AK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK93|||http://purl.uniprot.org/uniprot/F8VY04|||http://purl.uniprot.org/uniprot/F8W1A4|||http://purl.uniprot.org/uniprot/G3V213|||http://purl.uniprot.org/uniprot/P54819                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylate kinase 2, mitochondrial|||Adenylate kinase 2, mitochondrial, N-terminally processed|||Adenylate kinase active site lid|||Disordered|||In RDYS.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||LID|||N-acetylmethionine|||N6-acetyllysine|||N6-succinyllysine|||NMP|||NMPbind|||Phosphoserine|||Phosphothreonine|||Removed|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158917|||http://purl.uniprot.org/annotation/PRO_0000423212|||http://purl.uniprot.org/annotation/VAR_050032|||http://purl.uniprot.org/annotation/VAR_054630|||http://purl.uniprot.org/annotation/VAR_054631|||http://purl.uniprot.org/annotation/VSP_002790|||http://purl.uniprot.org/annotation/VSP_002791|||http://purl.uniprot.org/annotation/VSP_002792|||http://purl.uniprot.org/annotation/VSP_002793|||http://purl.uniprot.org/annotation/VSP_002794|||http://purl.uniprot.org/annotation/VSP_036503
http://togogenome.org/gene/9606:KIAA1549L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12914|||http://purl.uniprot.org/uniprot/Q6ZVL6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Polar residues|||UPF0606 protein KIAA1549L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274780|||http://purl.uniprot.org/annotation/VSP_034445|||http://purl.uniprot.org/annotation/VSP_034446|||http://purl.uniprot.org/annotation/VSP_034447
http://togogenome.org/gene/9606:SLC39A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDK0|||http://purl.uniprot.org/uniprot/C4N9M8|||http://purl.uniprot.org/uniprot/M0QX28|||http://purl.uniprot.org/uniprot/Q9NUM3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Zinc transporter ZIP9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297597|||http://purl.uniprot.org/annotation/VAR_034648|||http://purl.uniprot.org/annotation/VAR_034649|||http://purl.uniprot.org/annotation/VAR_034650|||http://purl.uniprot.org/annotation/VSP_027302|||http://purl.uniprot.org/annotation/VSP_054057|||http://purl.uniprot.org/annotation/VSP_054058
http://togogenome.org/gene/9606:MRGPRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SM5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor member G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069767
http://togogenome.org/gene/9606:HCCS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53701                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HRM 1|||HRM 2|||Holocytochrome c-type synthase|||In LSDMCA1; loss of function; loss of localization to mitochondrion.|||In LSDMCA1; loss of function; no effect on localization to mitochondrion.|||Loss of holocytochrome C synthase activity. Loss of heme-binding. Loss of interaction with cytochrome C.|||N-myristoyl glycine|||No effect on holocytochrome C synthase activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121712|||http://purl.uniprot.org/annotation/VAR_030823|||http://purl.uniprot.org/annotation/VAR_083982
http://togogenome.org/gene/9606:EDDM3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56851|||http://purl.uniprot.org/uniprot/W0UV31                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Epididymal secretory protein E3-beta|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021189|||http://purl.uniprot.org/annotation/PRO_5014314782|||http://purl.uniprot.org/annotation/VAR_038946
http://togogenome.org/gene/9606:TMCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKB8|||http://purl.uniprot.org/uniprot/Q7Z6W1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane and coiled-coil domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249435
http://togogenome.org/gene/9606:DMBX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Diencephalon/mesencephalon homeobox protein 1|||Disordered|||Found in a patient with global delayed development; unknown pathological significance.|||Homeobox|||In isoform 2.|||Interaction with OTX2 and is required for repressor activity|||OAR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262954|||http://purl.uniprot.org/annotation/VAR_049578|||http://purl.uniprot.org/annotation/VAR_082142|||http://purl.uniprot.org/annotation/VSP_052251
http://togogenome.org/gene/9606:RHCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBD6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ammonium transporter Rh type C|||Cytoplasmic|||Extracellular|||Helical|||Loss of function.|||N-linked (GlcNAc...) asparagine|||Reduction of ammonia transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283577|||http://purl.uniprot.org/annotation/VAR_031496
http://togogenome.org/gene/9606:GLIPR1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G1C9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Disordered|||GLIPR1-like protein 2|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324387|||http://purl.uniprot.org/annotation/VSP_032239|||http://purl.uniprot.org/annotation/VSP_032240|||http://purl.uniprot.org/annotation/VSP_032241|||http://purl.uniprot.org/annotation/VSP_032242|||http://purl.uniprot.org/annotation/VSP_032243|||http://purl.uniprot.org/annotation/VSP_032244|||http://purl.uniprot.org/annotation/VSP_032245|||http://purl.uniprot.org/annotation/VSP_032246
http://togogenome.org/gene/9606:RAB44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z6P3                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||Polar residues|||Pro residues|||Ras-related protein Rab-44|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333077
http://togogenome.org/gene/9606:NLRX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UT6                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRRCT|||LRRNT|||Mitochondrion|||NACHT|||NLR family member X1|||Required for interaction with MAVS|||Required for the repression of MAVS-induced interferon signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296190|||http://purl.uniprot.org/annotation/VAR_034614|||http://purl.uniprot.org/annotation/VAR_034615|||http://purl.uniprot.org/annotation/VAR_034616|||http://purl.uniprot.org/annotation/VAR_034617|||http://purl.uniprot.org/annotation/VSP_027158|||http://purl.uniprot.org/annotation/VSP_027159
http://togogenome.org/gene/9606:RPIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49247                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In RPIAD.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Ribose-5-phosphate isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158521|||http://purl.uniprot.org/annotation/VAR_019122
http://togogenome.org/gene/9606:TMEM65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI78                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Mitochondrion|||Transmembrane protein 65                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251404|||http://purl.uniprot.org/annotation/VAR_060384
http://togogenome.org/gene/9606:SPANXN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5MJ09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Sperm protein associated with the nucleus on the X chromosome N3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285540|||http://purl.uniprot.org/annotation/VAR_032026|||http://purl.uniprot.org/annotation/VAR_053684
http://togogenome.org/gene/9606:RYK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34925|||http://purl.uniprot.org/uniprot/Q59FQ5|||http://purl.uniprot.org/uniprot/Q8WTZ8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gain of an autophosphorylation activity. Gain of an autophosphorylation activity; when associated with A-359. Gain of an autophosphorylation activity; when associated with G-334 and G-482.|||Gain of an autophosphorylation activity. Gain of an autophosphorylation activity; when associated with G-334 and F-481.|||Helical|||In an ovarian mucinous carcinoma sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||No induction of the MAPK pathway.|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase RYK|||WIF                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024464|||http://purl.uniprot.org/annotation/VAR_041800|||http://purl.uniprot.org/annotation/VAR_041801|||http://purl.uniprot.org/annotation/VAR_041802|||http://purl.uniprot.org/annotation/VSP_005009
http://togogenome.org/gene/9606:OR8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGG7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150653|||http://purl.uniprot.org/annotation/VAR_053238|||http://purl.uniprot.org/annotation/VAR_062057
http://togogenome.org/gene/9606:THPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITS0|||http://purl.uniprot.org/uniprot/F8W6L1|||http://purl.uniprot.org/uniprot/P40225|||http://purl.uniprot.org/uniprot/Q5FBX8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues|||Pro residues|||Thrombopoietin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008411|||http://purl.uniprot.org/annotation/PRO_5003385432|||http://purl.uniprot.org/annotation/PRO_5040057993|||http://purl.uniprot.org/annotation/VAR_011795|||http://purl.uniprot.org/annotation/VAR_011796|||http://purl.uniprot.org/annotation/VSP_001450|||http://purl.uniprot.org/annotation/VSP_001451
http://togogenome.org/gene/9606:DNAJB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YX62|||http://purl.uniprot.org/uniprot/O75190                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||DnaJ homolog subfamily B member 6|||Found in a family with autosomal-dominantly inherited distal-onset myopathy; significant loss of its ability to suppress aggregation of polyglutamine-containing proteins.|||In LGMDD1.|||In LGMDD1; the mutation results in inefficient inhibition of protein aggregation by isoform B.|||In isoform B.|||In isoform C.|||In isoform D.|||Interaction with HSP70|||Interaction with KRT18|||J|||Omega-N-methylarginine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071025|||http://purl.uniprot.org/annotation/VAR_067833|||http://purl.uniprot.org/annotation/VAR_067834|||http://purl.uniprot.org/annotation/VAR_067835|||http://purl.uniprot.org/annotation/VAR_079428|||http://purl.uniprot.org/annotation/VSP_001289|||http://purl.uniprot.org/annotation/VSP_001290|||http://purl.uniprot.org/annotation/VSP_026180|||http://purl.uniprot.org/annotation/VSP_053894
http://togogenome.org/gene/9606:ORC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBD5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Origin recognition complex subunit 3|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127083|||http://purl.uniprot.org/annotation/VAR_014516|||http://purl.uniprot.org/annotation/VAR_014517|||http://purl.uniprot.org/annotation/VAR_014518|||http://purl.uniprot.org/annotation/VAR_014519|||http://purl.uniprot.org/annotation/VAR_014520|||http://purl.uniprot.org/annotation/VAR_014521|||http://purl.uniprot.org/annotation/VAR_014522|||http://purl.uniprot.org/annotation/VAR_020656|||http://purl.uniprot.org/annotation/VSP_017129|||http://purl.uniprot.org/annotation/VSP_044893
http://togogenome.org/gene/9606:LMBRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DH5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptor-associated protein LMBRD2|||Helical|||In DENBA.|||In DENBA; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299161|||http://purl.uniprot.org/annotation/VAR_086730|||http://purl.uniprot.org/annotation/VAR_086731|||http://purl.uniprot.org/annotation/VAR_086732|||http://purl.uniprot.org/annotation/VAR_086733|||http://purl.uniprot.org/annotation/VAR_086734|||http://purl.uniprot.org/annotation/VAR_086735|||http://purl.uniprot.org/annotation/VAR_086736
http://togogenome.org/gene/9606:PIGZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DL68|||http://purl.uniprot.org/uniprot/Q86VD9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  GPI mannosyltransferase 4|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246268|||http://purl.uniprot.org/annotation/VAR_027032|||http://purl.uniprot.org/annotation/VAR_027033|||http://purl.uniprot.org/annotation/VAR_027034|||http://purl.uniprot.org/annotation/VAR_054965
http://togogenome.org/gene/9606:FBXO27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR61|||http://purl.uniprot.org/uniprot/Q8NI29                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||F-box|||F-box only protein 27|||FBA|||Reduces interaction with glycosylated concanavalin-A in vitro.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119914
http://togogenome.org/gene/9606:PIGK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92643                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Decreased function in GPI-anchor attachment to protein.|||Essential for GPI attachment|||GPI-anchor transamidase|||Helical|||In NEDHCAS.|||In NEDHCAS; unknown pathological significance.|||In isoform 2.|||Interchain (with C-182 in PIGT)|||Loss of activity.|||Loss of function in GPI-anchor attachment to protein.|||Lumenal|||No effect on function in GPI-anchor attachment to protein.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026529|||http://purl.uniprot.org/annotation/VAR_051518|||http://purl.uniprot.org/annotation/VAR_084273|||http://purl.uniprot.org/annotation/VAR_084274|||http://purl.uniprot.org/annotation/VAR_084275|||http://purl.uniprot.org/annotation/VAR_084276|||http://purl.uniprot.org/annotation/VAR_084277|||http://purl.uniprot.org/annotation/VAR_084278|||http://purl.uniprot.org/annotation/VAR_084279|||http://purl.uniprot.org/annotation/VAR_084280|||http://purl.uniprot.org/annotation/VAR_084281|||http://purl.uniprot.org/annotation/VSP_056457
http://togogenome.org/gene/9606:MED4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPJ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 4|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096383|||http://purl.uniprot.org/annotation/VSP_047072
http://togogenome.org/gene/9606:BAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99933                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 6 AA tandem repeat of E-E-X(4)|||BAG|||BAG family molecular chaperone regulator 1|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with HSPA8|||Interaction with PPP1R15A|||Phosphoserine|||Polar residues|||Significant loss of interaction with HSPA8.|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088865|||http://purl.uniprot.org/annotation/VSP_000453|||http://purl.uniprot.org/annotation/VSP_038394|||http://purl.uniprot.org/annotation/VSP_038395
http://togogenome.org/gene/9606:SNF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96H20                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Omega-N-methylarginine|||Vacuolar-sorting protein SNF8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215209|||http://purl.uniprot.org/annotation/VSP_015340
http://togogenome.org/gene/9606:PML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29590                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  (Microbial infection) Cleavage by protease 3C of enterovirus 71|||Abolished conjugation of one SUMO1P1/SUMO5. Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-160.|||Abolishes SUMO1 binding.|||Abolishes ubiquitination by the BCR(KLHL20) E3 ubiquitin ligase complex.|||B box-type 1; atypical|||B box-type 2|||Basic and acidic residues|||Breakpoint for translocation to form PML-RARA oncogene in type A APL|||Breakpoint for translocation to form PML-RARA oncogene in type B APL|||Compromised the formation of high molecular weight species of SUMO1P1/SUMO5 conjugation on PML. Loss of 2 sumoylations; when associated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-65 and R-490.|||Disordered|||Does not affect SUMO1P1/SUMO5 conjugation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in /SUMO5); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1P1/SUMO5); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform PML-11, isoform PML-12 and isoform PML-13.|||In isoform PML-14.|||In isoform PML-2 and isoform PML-13.|||In isoform PML-3.|||In isoform PML-4 and isoform PML-12.|||In isoform PML-5.|||In isoform PML-6.|||In isoform PML-7.|||In isoform PML-8.|||Interaction with PER2|||Loss of 2 sumoylations; when associated with R-65 and R-490.|||Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160.|||Loss of 2 sumoylations; when associated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490.|||Loss of cleavage by enterovirus 71 protease 3C.|||Loss of nuclear localization. Reduced acetylation. Further decrease in acetylation; when associated with R-515.|||Loss of nuclear localization; when associated with A-487.|||Loss of nuclear localization; when associated with A-490.|||Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. Loss the ability to be conjugated by SUMO1P1/SUMO5 but could be conjugated by SUMO1; when associated with R-160 and R-490.|||Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. No sumoylation nor nuclear body formation; when associated with R-160 and R-490.|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on sumoylation levels.|||No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with R-89.|||No nuclear microspeckle location, no sumoylation and loss of intrinsic transcriptional repressor activity of PML-RARA oncoprotein; when associated with S-88.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by CDK1 and CDK2|||Phosphoserine; by CHEK2|||Phosphoserine; by CK2|||Phosphoserine; by HIPK2|||Phosphoserine; by HIPK2 and MAPK1|||Phosphoserine; by MAPK1|||Phosphoserine; by MAPK1 and MAPK7|||Phosphothreonine|||Polar residues|||Pro residues|||Protein PML|||RING-type|||Slightly reduced acetylation. Further decrease in acetylation; when associated with R-487.|||Strongly reduced sumoylation; when associated with S-57.|||Strongly reduced sumoylation; when associated with S-60.|||Sumo interaction motif (SIM) ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056001|||http://purl.uniprot.org/annotation/VAR_052090|||http://purl.uniprot.org/annotation/VSP_005739|||http://purl.uniprot.org/annotation/VSP_005740|||http://purl.uniprot.org/annotation/VSP_005741|||http://purl.uniprot.org/annotation/VSP_005742|||http://purl.uniprot.org/annotation/VSP_005743|||http://purl.uniprot.org/annotation/VSP_005744|||http://purl.uniprot.org/annotation/VSP_005745|||http://purl.uniprot.org/annotation/VSP_040590|||http://purl.uniprot.org/annotation/VSP_040591|||http://purl.uniprot.org/annotation/VSP_040592|||http://purl.uniprot.org/annotation/VSP_040593|||http://purl.uniprot.org/annotation/VSP_040594|||http://purl.uniprot.org/annotation/VSP_040595|||http://purl.uniprot.org/annotation/VSP_040596|||http://purl.uniprot.org/annotation/VSP_040597
http://togogenome.org/gene/9606:CATSPER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEC5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cation channel sperm-associated protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Pore-forming|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295674|||http://purl.uniprot.org/annotation/VAR_033304|||http://purl.uniprot.org/annotation/VAR_033305|||http://purl.uniprot.org/annotation/VAR_033306
http://togogenome.org/gene/9606:MLC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15049                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In MLC1.|||In MLC1; accumulates in the cytoplasmic perinuclear region and endoplasmic reticulum; affects interaction with ATP1B1.|||In MLC1; accumulates in the cytoplasmic perinuclear region and endoplasmic reticulum; affects the interaction with ATP1B1, TRPV4, AQP4 and HEPACAM.|||In MLC1; does not affect subcellular location.|||In a pedigree affected by schizophrenia.|||In isoform 2.|||Membrane protein MLC1|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096496|||http://purl.uniprot.org/annotation/VAR_011699|||http://purl.uniprot.org/annotation/VAR_011700|||http://purl.uniprot.org/annotation/VAR_011701|||http://purl.uniprot.org/annotation/VAR_011702|||http://purl.uniprot.org/annotation/VAR_012731|||http://purl.uniprot.org/annotation/VAR_017438|||http://purl.uniprot.org/annotation/VAR_017439|||http://purl.uniprot.org/annotation/VAR_017440|||http://purl.uniprot.org/annotation/VAR_017441|||http://purl.uniprot.org/annotation/VAR_051186|||http://purl.uniprot.org/annotation/VAR_051187|||http://purl.uniprot.org/annotation/VAR_067762|||http://purl.uniprot.org/annotation/VAR_067763|||http://purl.uniprot.org/annotation/VAR_067764|||http://purl.uniprot.org/annotation/VAR_067765|||http://purl.uniprot.org/annotation/VAR_067766|||http://purl.uniprot.org/annotation/VAR_067767|||http://purl.uniprot.org/annotation/VAR_067768|||http://purl.uniprot.org/annotation/VSP_055494
http://togogenome.org/gene/9606:GINS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y248                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Mass|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  DNA replication complex GINS protein PSF2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||This is the measured mass for the GINS complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194813
http://togogenome.org/gene/9606:SIRT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRF5|||http://purl.uniprot.org/uniprot/Q8IXJ6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes CDK2-dependent phosphorylation.|||Abolishes CDK2-dependent phosphorylation. Inhibits interaction with a cyclin E-CDK2 complex. Reduces strongly histone deacetylation activity.|||Abolishes deacetylation of alpha-tubulin. Inhibits deacetylation of histone H3 at 'Lys-18'. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-187.|||Basic and acidic residues|||Deacetylase sirtuin-type|||Disordered|||Does not affect deacetylase activity. Abolishes CDK2-dependent phosphorylation. Inhibits cellular proliferation delay in the early metaphase to prevent chromosomal instability. Does not inhibit interaction with a cyclin E-CDK2 complex. Does not inhibit interaction with HDAC6 and ubiquitination. Inhibits cell adhesion and migration and neurite outgrowth. Inhibits deacetylase activity; when associated with A-372.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibits deacetylase activity toward histone, alpha-tubulin, FZR1 and CDC20. No effect on CDK2-dependent phosphorylation. Does not inhibit interaction with alpha-tubulin, HDAC6, HIF1A and the cyclin E-CDK2 complex. Inhibits interaction with BEX4 and KMT5A. Abolishes deacetylation, dimeric formation and enzymatic activity increase of G6PD. Prevents histone H4 methylation at 'Lys-20'(H4K20me1) in metaphase chromosomes. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-167 and A-168. Strongly reduced activity toward long-chain fatty acyl groups.|||Inhibits deacetylase activity.|||N-acetylalanine|||NAD-dependent protein deacetylase sirtuin-2|||No effect on deacetylase activity.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by CDK2 and CDK5|||Proton acceptor|||Reduces binding for the peptide inhibitor S2iL5.|||Reduces deacetylase activity.|||Reduces deacetylase activity. Inhibits the block of entry to chromosome condensation and subsequent hyperploidy cell formation in response to mitotic stress; when associated with A-168 and A-187.|||Reduces phosphorylation. Does not inhibit interaction with HDAC6, ubiquitination and deacetylase activity. Inhibits deacetylase activity; when associated with A-368.|||Removed|||Strongly reduces binding for the peptide inhibitor S2iL5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000110258|||http://purl.uniprot.org/annotation/VSP_008724|||http://purl.uniprot.org/annotation/VSP_008726|||http://purl.uniprot.org/annotation/VSP_008727|||http://purl.uniprot.org/annotation/VSP_008728|||http://purl.uniprot.org/annotation/VSP_055328
http://togogenome.org/gene/9606:CCDC144A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUR9|||http://purl.uniprot.org/uniprot/B7ZM27                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CCDC144C-like coiled-coil|||Coiled-coil domain-containing protein 144A|||DUF3496|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312279|||http://purl.uniprot.org/annotation/VSP_029787|||http://purl.uniprot.org/annotation/VSP_029788|||http://purl.uniprot.org/annotation/VSP_029789|||http://purl.uniprot.org/annotation/VSP_029790|||http://purl.uniprot.org/annotation/VSP_029791
http://togogenome.org/gene/9606:TBC1D3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X179                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431605
http://togogenome.org/gene/9606:H2BC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R4S9|||http://purl.uniprot.org/uniprot/P62807                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid|||ADP-ribosylserine|||Basic residues|||Dimethylated arginine|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A/H2B/H3|||Histone H2B type 1-C/E/F/G/I|||N-acetylproline|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-malonyllysine; alternate|||N6-methylated lysine; alternate|||N6-methyllysine; alternate|||N6-succinyllysine; alternate|||O-linked (GlcNAc) serine|||Omega-N-methylarginine|||Phosphoserine; by AMPK|||Phosphoserine; by STK4/MST1|||Phosphothreonine|||PolyADP-ribosyl glutamic acid|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071826|||http://purl.uniprot.org/annotation/VAR_055887
http://togogenome.org/gene/9606:DEFB126                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDP8|||http://purl.uniprot.org/uniprot/Q9BYW3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin|||Beta-defensin 126|||In vitro binds to LPS, mediates antimicrobial activity and inhibits LPS-mediated inflammation|||Interchain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000436299|||http://purl.uniprot.org/annotation/PRO_5017102872
http://togogenome.org/gene/9606:DTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0E6|||http://purl.uniprot.org/uniprot/Q9NZJ0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Blocks association with DDB1 and ubiquitination by DCX(DTL). No effect on ubiquitination by SCF(FBXO11).|||Blocks interaction with FBXO11 and increases protein stability. Not phosphorylated by CDK1 or CDK2.|||Blocks interaction with FBXO11 and ubiquitination, increasing protein stability. Delays cell migration.|||Blocks interaction with FBXO11.|||DDB1-binding motif|||Denticleless protein homolog|||Disordered|||In isoform 2.|||Increases protein stability, but no effect on interaction with FBXO11 and polyubiquitination. Delays cell migration.|||Inhibits phosphorylation on T-464. No effect on interaction with FBXO11.|||N-acetylmethionine|||No effect on interaction with FBXO11.|||No effect on interaction with FBXO11. Increases protein stability.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CDK1 and CDK2|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274867|||http://purl.uniprot.org/annotation/VAR_030353|||http://purl.uniprot.org/annotation/VAR_030354|||http://purl.uniprot.org/annotation/VAR_062095|||http://purl.uniprot.org/annotation/VSP_022879|||http://purl.uniprot.org/annotation/VSP_022880|||http://purl.uniprot.org/annotation/VSP_022881
http://togogenome.org/gene/9606:IHO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZP6|||http://purl.uniprot.org/uniprot/Q8IYA8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Interactor of HORMAD1 protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302875|||http://purl.uniprot.org/annotation/VAR_035002|||http://purl.uniprot.org/annotation/VSP_027987|||http://purl.uniprot.org/annotation/VSP_027988|||http://purl.uniprot.org/annotation/VSP_027989|||http://purl.uniprot.org/annotation/VSP_027990
http://togogenome.org/gene/9606:CXCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25024                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-X-C chemokine receptor type 1|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069330|||http://purl.uniprot.org/annotation/VAR_003479|||http://purl.uniprot.org/annotation/VAR_016236|||http://purl.uniprot.org/annotation/VAR_016237|||http://purl.uniprot.org/annotation/VAR_016238|||http://purl.uniprot.org/annotation/VAR_021061|||http://purl.uniprot.org/annotation/VAR_021062|||http://purl.uniprot.org/annotation/VAR_026525
http://togogenome.org/gene/9606:EDRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3B7T1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Erythroid differentiation-related factor 1|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244260|||http://purl.uniprot.org/annotation/VAR_035862|||http://purl.uniprot.org/annotation/VAR_035863|||http://purl.uniprot.org/annotation/VSP_019531|||http://purl.uniprot.org/annotation/VSP_019532|||http://purl.uniprot.org/annotation/VSP_035712|||http://purl.uniprot.org/annotation/VSP_035713|||http://purl.uniprot.org/annotation/VSP_035714
http://togogenome.org/gene/9606:PCYT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5K3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Choline-phosphate cytidylyltransferase B|||Disordered|||In isoform 1.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208456|||http://purl.uniprot.org/annotation/VSP_001226|||http://purl.uniprot.org/annotation/VSP_020045|||http://purl.uniprot.org/annotation/VSP_020046|||http://purl.uniprot.org/annotation/VSP_044659
http://togogenome.org/gene/9606:REEP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUK4|||http://purl.uniprot.org/uniprot/X5DP57|||http://purl.uniprot.org/uniprot/X5DR89                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Receptor expression-enhancing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101826|||http://purl.uniprot.org/annotation/VAR_048926|||http://purl.uniprot.org/annotation/VSP_016634|||http://purl.uniprot.org/annotation/VSP_016635
http://togogenome.org/gene/9606:NUDCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVJ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  CS|||Disordered|||N-acetylserine|||NudC domain-containing protein 2|||Phosphoserine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057982
http://togogenome.org/gene/9606:ULK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75385                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished serine/threonine-protein kinase activity.|||C-terminal domain; mediates interaction with SESN2|||Disordered|||In a lung adenocarcinoma sample; somatic mutation.|||In an ovarian mucinous carcinoma sample; somatic mutation.|||Interaction with GABARAP and GABARAPL2|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase ULK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086780|||http://purl.uniprot.org/annotation/VAR_041274|||http://purl.uniprot.org/annotation/VAR_041275|||http://purl.uniprot.org/annotation/VAR_041276|||http://purl.uniprot.org/annotation/VAR_041277|||http://purl.uniprot.org/annotation/VAR_041278|||http://purl.uniprot.org/annotation/VAR_041279|||http://purl.uniprot.org/annotation/VAR_041280|||http://purl.uniprot.org/annotation/VAR_054892
http://togogenome.org/gene/9606:IQCG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JKX8|||http://purl.uniprot.org/uniprot/Q9H095|||http://purl.uniprot.org/uniprot/Q9H5C8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dynein regulatory complex protein 9|||IQ|||In isoform 2.|||Loss of calmodulin binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282561|||http://purl.uniprot.org/annotation/VAR_031415|||http://purl.uniprot.org/annotation/VSP_024187
http://togogenome.org/gene/9606:KLHL18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94889                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119122|||http://purl.uniprot.org/annotation/VSP_035974
http://togogenome.org/gene/9606:IQSEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGT3|||http://purl.uniprot.org/uniprot/B4DGC5|||http://purl.uniprot.org/uniprot/Q6DN90                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes guanosine nucleotide exchange factor activity.|||Basic and acidic residues|||Basic residues|||Disordered|||IQ|||IQ motif and SEC7 domain-containing protein 1|||In IDDSSBA; loss of function.|||In isoform 2.|||In isoform 3.|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245606|||http://purl.uniprot.org/annotation/VAR_027004|||http://purl.uniprot.org/annotation/VAR_051927|||http://purl.uniprot.org/annotation/VAR_083480|||http://purl.uniprot.org/annotation/VAR_083481|||http://purl.uniprot.org/annotation/VSP_019758|||http://purl.uniprot.org/annotation/VSP_060581|||http://purl.uniprot.org/annotation/VSP_060582
http://togogenome.org/gene/9606:GIMAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Z4|||http://purl.uniprot.org/uniprot/Q8WWP7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  AIG1-type G|||Cytoplasmic|||Disordered|||G1|||G2|||G3|||G4|||G5|||GTPase IMAP family member 1|||Helical|||Helical; Anchor for type IV membrane protein|||In a breast cancer sample; somatic mutation.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190984|||http://purl.uniprot.org/annotation/VAR_036301|||http://purl.uniprot.org/annotation/VAR_049530
http://togogenome.org/gene/9606:PPP4C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R625|||http://purl.uniprot.org/uniprot/P60510                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site                                                                                  ^@                                                                                  Abolishes interaction with PPP4R4.|||Abolishes interaction with PPP4R4; no effect on interaction with PPP4R1 and PPP4R2.|||Diminishes interaction with PPP4R4.|||Leucine methyl ester|||Loss of activity.|||N-acetylalanine|||Proton donor|||Removed|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase 4 catalytic subunit|||Unable to dephosphorylate 53BP1 and KAR1, loss of DSB repair activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058883
http://togogenome.org/gene/9606:AIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJ38|||http://purl.uniprot.org/uniprot/A0A804HKL7|||http://purl.uniprot.org/uniprot/O00170                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AH receptor-interacting protein|||In PITA1; ACTH-secreting pituitary adenoma.|||In PITA1; ACTH-secreting pituitary adenoma; unknown pathological significance.|||In PITA1; unknown pathological significance.|||PPIase FKBP-type|||Phosphoserine|||TPR|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075339|||http://purl.uniprot.org/annotation/VAR_043908|||http://purl.uniprot.org/annotation/VAR_043909|||http://purl.uniprot.org/annotation/VAR_043910|||http://purl.uniprot.org/annotation/VAR_043911|||http://purl.uniprot.org/annotation/VAR_043912|||http://purl.uniprot.org/annotation/VAR_043913|||http://purl.uniprot.org/annotation/VAR_058407|||http://purl.uniprot.org/annotation/VAR_061545
http://togogenome.org/gene/9606:SEMA6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQU6|||http://purl.uniprot.org/uniprot/Q9H2E6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Sema|||Semaphorin-6A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032339|||http://purl.uniprot.org/annotation/PRO_5014506430|||http://purl.uniprot.org/annotation/VAR_030296|||http://purl.uniprot.org/annotation/VAR_030297|||http://purl.uniprot.org/annotation/VAR_030298|||http://purl.uniprot.org/annotation/VSP_007113
http://togogenome.org/gene/9606:ZNF248                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTK3|||http://purl.uniprot.org/uniprot/A2RUI7|||http://purl.uniprot.org/uniprot/Q8NDW4                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 248                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047482|||http://purl.uniprot.org/annotation/VAR_052800|||http://purl.uniprot.org/annotation/VSP_045321
http://togogenome.org/gene/9606:FILIP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4L180                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Filamin A-interacting protein 1-like|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309470|||http://purl.uniprot.org/annotation/VAR_050993|||http://purl.uniprot.org/annotation/VAR_050994|||http://purl.uniprot.org/annotation/VSP_029201|||http://purl.uniprot.org/annotation/VSP_029202|||http://purl.uniprot.org/annotation/VSP_029203|||http://purl.uniprot.org/annotation/VSP_029204|||http://purl.uniprot.org/annotation/VSP_029205|||http://purl.uniprot.org/annotation/VSP_029206|||http://purl.uniprot.org/annotation/VSP_036502
http://togogenome.org/gene/9606:CFAP77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2A393|||http://purl.uniprot.org/uniprot/Q6ZQR2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 77|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325973|||http://purl.uniprot.org/annotation/VAR_039959|||http://purl.uniprot.org/annotation/VAR_039960|||http://purl.uniprot.org/annotation/VAR_039961|||http://purl.uniprot.org/annotation/VAR_062164|||http://purl.uniprot.org/annotation/VSP_032507
http://togogenome.org/gene/9606:MUC15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT67|||http://purl.uniprot.org/uniprot/A0A0A0MTD6|||http://purl.uniprot.org/uniprot/Q8N387                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Mucin-15|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019288|||http://purl.uniprot.org/annotation/VAR_019376|||http://purl.uniprot.org/annotation/VAR_019377|||http://purl.uniprot.org/annotation/VAR_050452|||http://purl.uniprot.org/annotation/VSP_010825
http://togogenome.org/gene/9606:FLVCR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RB38|||http://purl.uniprot.org/uniprot/Q9Y5Y0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Heme transporter FLVCR1|||In PCARP.|||In PCARP; also found in a patient with sensory neuropathy and pain insensitivity.|||In isoform 2.|||Major facilitator superfamily (MFS) profile|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Probable disease-associated variant found in a patient with sensory neuropathy and pain insensitivity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084844|||http://purl.uniprot.org/annotation/VAR_050297|||http://purl.uniprot.org/annotation/VAR_050298|||http://purl.uniprot.org/annotation/VAR_065158|||http://purl.uniprot.org/annotation/VAR_065159|||http://purl.uniprot.org/annotation/VAR_065160|||http://purl.uniprot.org/annotation/VAR_065161|||http://purl.uniprot.org/annotation/VAR_077884|||http://purl.uniprot.org/annotation/VSP_047866
http://togogenome.org/gene/9606:PCSK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29120                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Associated with susceptibility to obesity; induces a 10.4% reduction of activity (P = 0.03) when compared to the wild-type enzyme.|||Basic and acidic residues|||Charge relay system|||Disordered|||In PC1 deficiency.|||In PC1 deficiency; in vitro the mutation markedly impairs the catalytic activity of the enzyme; however intracellular trafficking of this mutant enzyme appears normal; retains some autocatalytic activity even though it is completely inactive on other substrates.|||In PC1 deficiency; prevents processing of pro-PCSK1 and leads to its retention in the endoplasmic reticulum.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neuroendocrine convertase 1|||O-linked (GalNAc...) threonine|||P/Homo B|||Peptidase S8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027057|||http://purl.uniprot.org/annotation/PRO_0000027058|||http://purl.uniprot.org/annotation/VAR_013906|||http://purl.uniprot.org/annotation/VAR_013907|||http://purl.uniprot.org/annotation/VAR_013908|||http://purl.uniprot.org/annotation/VAR_013909|||http://purl.uniprot.org/annotation/VAR_022777|||http://purl.uniprot.org/annotation/VAR_022778|||http://purl.uniprot.org/annotation/VAR_055002|||http://purl.uniprot.org/annotation/VSP_046100
http://togogenome.org/gene/9606:UBE2T                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPD8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased FANCD2 ubiquitination.|||Decreased binding to FANCL.|||Decreased monoubiquitination.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||In FANCT; abolishes FANCD2 monoubiquitination; abolishes interaction with FANCL.|||Loss of E2 enzyme activity.|||Loss of FANCL-binding and of FANCL-dependent monoubiquitination of FANCD2.|||No effect on FANCL-binding, nor on FANCL-dependent monoubiquitination of FANCD2.|||Phosphoserine|||UBC core|||Ubiquitin-conjugating enzyme E2 T                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082509|||http://purl.uniprot.org/annotation/VAR_073861
http://togogenome.org/gene/9606:LUC7L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MYV2|||http://purl.uniprot.org/uniprot/Q1W6G4|||http://purl.uniprot.org/uniprot/Q9NQ29                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Putative RNA-binding protein Luc7-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187280|||http://purl.uniprot.org/annotation/VSP_010214|||http://purl.uniprot.org/annotation/VSP_010215
http://togogenome.org/gene/9606:RIMS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJD0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  C2|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||Regulating synaptic membrane exocytosis protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190204|||http://purl.uniprot.org/annotation/VSP_055836|||http://purl.uniprot.org/annotation/VSP_055837
http://togogenome.org/gene/9606:LMNTD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXW0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||LTD|||Lamin tail domain-containing protein 2|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251929|||http://purl.uniprot.org/annotation/VAR_027732
http://togogenome.org/gene/9606:ALKBH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT30                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial|||Does not affect ability to trigger programmed necrosis.|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239288|||http://purl.uniprot.org/annotation/VAR_048224
http://togogenome.org/gene/9606:TIPARP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BQ2|||http://purl.uniprot.org/uniprot/Q7Z3E1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  ADP-ribosylcysteine|||Abolishes ADP-ribosyltransferase activity.|||C3H1-type|||Disordered|||Does not affect ADP-ribosyltransferase activity.|||Nuclear localization signal|||PARP catalytic|||Partial relocalization to the cytoplasm.|||Protein mono-ADP-ribosyltransferase TIPARP|||Relocalization to the cytosol.|||Slight reduction of auto-mono-ADP-ribosylation.|||WWE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247835|||http://purl.uniprot.org/annotation/VAR_027155
http://togogenome.org/gene/9606:GRAMD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IC98                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||GRAM|||GRAM domain-containing protein 4|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328742|||http://purl.uniprot.org/annotation/VAR_042505|||http://purl.uniprot.org/annotation/VSP_032771
http://togogenome.org/gene/9606:RELN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78509                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BNR 1|||BNR 10|||BNR 11|||BNR 12|||BNR 13|||BNR 14|||BNR 15|||BNR 16|||BNR 2|||BNR 3|||BNR 4|||BNR 5|||BNR 6|||BNR 7|||BNR 8|||BNR 9|||EGF-like 1|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||In ETL7.|||In isoform 2.|||In isoform 3.|||Interchain|||N-linked (GlcNAc...) asparagine|||Reelin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030304|||http://purl.uniprot.org/annotation/VAR_047977|||http://purl.uniprot.org/annotation/VAR_047978|||http://purl.uniprot.org/annotation/VAR_057712|||http://purl.uniprot.org/annotation/VAR_073862|||http://purl.uniprot.org/annotation/VAR_073863|||http://purl.uniprot.org/annotation/VAR_073864|||http://purl.uniprot.org/annotation/VAR_073865|||http://purl.uniprot.org/annotation/VAR_073866|||http://purl.uniprot.org/annotation/VAR_073867|||http://purl.uniprot.org/annotation/VAR_073868|||http://purl.uniprot.org/annotation/VSP_005575|||http://purl.uniprot.org/annotation/VSP_005576
http://togogenome.org/gene/9606:NUDT21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43809                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes acetylation.|||Abolishes interaction with CPSF6; when associated with A-158.|||Abolishes interaction with CPSF6; when associated with A-160.|||Cleavage and polyadenylation specificity factor subunit 5|||Interaction with RNA|||N-acetylserine|||N6-acetyllysine|||Necessary for RNA-binding|||Necessary for interactions with PAPOLA and PABPN1|||No effect on acetylation.|||Nudix box|||Nudix hydrolase|||Omega-N-methylarginine|||Phosphotyrosine|||Reduces affinity for UGUARNA by 12%.|||Reduces affinity for UGUARNA by 50%.|||Reduces affinity for UGUARNA by 88%.|||Reduces affinity for UGUARNA by 99%.|||Reduces affinity for UGUARNA by over 90%.|||Reduces interactions with CPSF6 and CPSF7 and decreases mRNA 3'-processing activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057150
http://togogenome.org/gene/9606:BST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10589                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5.|||Bone marrow stromal antigen 2|||Cytoplasmic|||Extracellular|||GPI-anchor amidated serine|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interchain|||Loss of glycosylation site.|||Loss of glycosylation site. Impairs anti-viral activity.|||N-linked (GlcNAc...) asparagine|||No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5.|||Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-6.|||Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-8.|||Partial resistance to Vpu.|||Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-53 and A-63.|||Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-53 and A-91.|||Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-63 and A-91.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065005|||http://purl.uniprot.org/annotation/PRO_0000253552|||http://purl.uniprot.org/annotation/VAR_012067|||http://purl.uniprot.org/annotation/VSP_053250
http://togogenome.org/gene/9606:PPP2R3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06190                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||In isoform 3.|||In isoform PR72.|||Pro residues|||Serine/threonine-protein phosphatase 2A regulatory subunit B" subunit alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071443|||http://purl.uniprot.org/annotation/VAR_022095|||http://purl.uniprot.org/annotation/VAR_051739|||http://purl.uniprot.org/annotation/VAR_051740|||http://purl.uniprot.org/annotation/VAR_051741|||http://purl.uniprot.org/annotation/VAR_051742|||http://purl.uniprot.org/annotation/VAR_051743|||http://purl.uniprot.org/annotation/VAR_051744|||http://purl.uniprot.org/annotation/VAR_061760|||http://purl.uniprot.org/annotation/VSP_005107|||http://purl.uniprot.org/annotation/VSP_005108|||http://purl.uniprot.org/annotation/VSP_045203
http://togogenome.org/gene/9606:PLGLB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02325                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  PAN|||Plasminogen-like protein B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022105
http://togogenome.org/gene/9606:TMEM179B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7N9                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Phosphoserine|||Transmembrane protein 179B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328987
http://togogenome.org/gene/9606:UPF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAU5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with UPF1.|||Abolishes interaction with UPF1; reduces NMD efficiency.|||Abolishes interaction with UPF3B and association with SMG1 and RBM8A; reduces phosphorylation of UPF1.|||Acidic residues|||Basic and acidic residues|||Binds to UPF3B|||Decreases interaction with UPF1.|||Decreases interaction with UPF1; does not reduce NMD efficiency.|||Disordered|||Does not abolish interaction with UPF3B.|||Does not abolish interaction with UPF3B. Does not abolish interaction with UPF3B; when associated with D-854.|||Does not abolish interaction with UPF3B; when associated with K-851 and R-852.|||Does not impair RNA-binding; when associated with A-894.|||Does not impair RNA-binding; when associated with A-932.|||Greatly reduces NMD efficiency; when associated with E-1171 and E-1173.|||Greatly reduces NMD efficiency; when associated with E-1171 and E-1174.|||Greatly reduces NMD efficiency; when associated with E-1173 and E-1174.|||Interaction with UPF1|||MIF4G 1|||MIF4G 2|||MIF4G 3|||Necessary for interaction with UPF1|||Phosphothreonine|||Regulator of nonsense transcripts 2|||Strongly impairs RNA-binding.|||Sufficient for interaction with EIF4A1 and EIF1|||Sufficient for interaction with UPF1|||Sufficient for interaction with UPF1 C-terminus|||Sufficient for interaction with UPF3A and UPF3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097248|||http://purl.uniprot.org/annotation/VAR_024345
http://togogenome.org/gene/9606:CPT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLL0|||http://purl.uniprot.org/uniprot/Q53FV7|||http://purl.uniprot.org/uniprot/Q92523                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carnitine O-palmitoyltransferase 1, muscle isoform|||Carnitine O-palmitoyltransferase N-terminal|||Choline/carnitine acyltransferase|||Cytoplasmic|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrial intermembrane|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210162|||http://purl.uniprot.org/annotation/VAR_011739|||http://purl.uniprot.org/annotation/VAR_011740|||http://purl.uniprot.org/annotation/VAR_020029|||http://purl.uniprot.org/annotation/VAR_021854|||http://purl.uniprot.org/annotation/VAR_024188|||http://purl.uniprot.org/annotation/VSP_034246|||http://purl.uniprot.org/annotation/VSP_034247|||http://purl.uniprot.org/annotation/VSP_043184|||http://purl.uniprot.org/annotation/VSP_044451
http://togogenome.org/gene/9606:TUB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50607                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Tubby protein homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186463|||http://purl.uniprot.org/annotation/VSP_023030
http://togogenome.org/gene/9606:AP1M2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53GI5|||http://purl.uniprot.org/uniprot/Q9Y6Q5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP-1 complex subunit mu-2|||In isoform 2.|||MHD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193772|||http://purl.uniprot.org/annotation/VSP_000169
http://togogenome.org/gene/9606:KHDRBS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75525                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of SIAH1-mediated degradation.|||Complete loss of nuclear sublocalization.|||Disordered|||Fails to influence alternative splicing of CD44, NRXN2 and NRXN3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with SIAH1|||Involved in homodimerization|||KH|||KH domain-containing, RNA-binding, signal transduction-associated protein 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232522|||http://purl.uniprot.org/annotation/VSP_017905|||http://purl.uniprot.org/annotation/VSP_017906
http://togogenome.org/gene/9606:CD9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNI4|||http://purl.uniprot.org/uniprot/B4DK09|||http://purl.uniprot.org/uniprot/P21926                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CD9 antigen|||Cytoplasmic|||Extracellular|||Helical|||Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219.|||Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219.|||Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218.|||Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219.|||Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219.|||Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219.|||N-linked (GlcNAc...) asparagine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219205
http://togogenome.org/gene/9606:MEF2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14814                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes K-439 sumoylation.|||Abolishes K-439 sumoylation. Reduced neurotoxin-induced apoptosis of neuronal cells. More resistant to degradation.|||Abolishes MAPK7- and EGF-mediated transcriptional activation.|||Abolishes cleavage by caspase 7.|||Abolishes sumoylation and acetylation.|||Abolishes transcriptional activity; when associated with N-288 and N-291.|||Abolishes transcriptional activity; when associated with Q-287 and N-288.|||Abolishes transcriptional activity; when associated with Q-287 and N-291.|||Beta domain|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||In isoform MEF2D0B and isoform MEF2D00.|||In isoform MEF2DA'B and isoform MEF2DA'0.|||In isoform MEF2DA0, isoform MEF2DA'0 and isoform MEF2D00.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2D|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on K-439 sumoylation.|||No effect on MAPK7- or EGF-mediated transcriptional activity.|||Phosphoserine|||Phosphoserine; by MAPK7|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||Same transcriptional activity as for isoforms with beta domain.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199435|||http://purl.uniprot.org/annotation/VAR_022155|||http://purl.uniprot.org/annotation/VSP_006250|||http://purl.uniprot.org/annotation/VSP_006251|||http://purl.uniprot.org/annotation/VSP_006252
http://togogenome.org/gene/9606:LEAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969E1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Propeptide|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Liver-expressed antimicrobial peptide 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017355|||http://purl.uniprot.org/annotation/PRO_0000017356
http://togogenome.org/gene/9606:SWSAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NVH7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ATPase SWSAP1|||Disordered|||Loss of function in HRR associated with altered ssDNA-stimulated ATPase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294240|||http://purl.uniprot.org/annotation/VAR_033151
http://togogenome.org/gene/9606:FIG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92562                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In ALS11.|||In BTOP; partial loss of function.|||In CMT4J.|||In CMT4J; loss of function.|||In CMT4J; the mutant protein is unstable; low levels of the protein results from impaired interaction with VAC14.|||In YVS; complete loss of function mutation.|||Loss of activity.|||Loss of phosphatase activity on PIKFYVE.|||Polyphosphoinositide phosphatase|||SAC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209743|||http://purl.uniprot.org/annotation/VAR_020378|||http://purl.uniprot.org/annotation/VAR_022826|||http://purl.uniprot.org/annotation/VAR_036974|||http://purl.uniprot.org/annotation/VAR_054831|||http://purl.uniprot.org/annotation/VAR_054832|||http://purl.uniprot.org/annotation/VAR_054833|||http://purl.uniprot.org/annotation/VAR_054834|||http://purl.uniprot.org/annotation/VAR_054835|||http://purl.uniprot.org/annotation/VAR_054836|||http://purl.uniprot.org/annotation/VAR_070051|||http://purl.uniprot.org/annotation/VAR_070052|||http://purl.uniprot.org/annotation/VAR_071957|||http://purl.uniprot.org/annotation/VAR_071958|||http://purl.uniprot.org/annotation/VAR_071959
http://togogenome.org/gene/9606:TACR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25103                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Display properties similar to those of the wild-type receptor.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||S-palmitoyl cysteine|||Substance-P receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069885|||http://purl.uniprot.org/annotation/VAR_026826|||http://purl.uniprot.org/annotation/VSP_053824
http://togogenome.org/gene/9606:SLC12A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2X9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased phosphorylation by WNK kinases, leading to increased potassium-chloride cotransport activity; when associated with A-1030.|||Decreased phosphorylation by WNK kinases, leading to increased potassium-chloride cotransport activity; when associated with A-929.|||Discontinuously helical|||Disordered|||Extracellular|||Helical|||In DEE34; results in loss of chloride transport; decreased localization at the cell surface.|||In DEE34; results in reduced chloride transport; decreased localization at the cell surface.|||In EIG14; rare variant associated with disease susceptibility; results in reduced chloride transport.|||In EIG14; rare variant associated with disease susceptibility; results in reduced chloride transport; decreased localization at the cell surface; unable to induce cortical dendritic spines formation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by OXSR1 and STK39|||Solute carrier family 12 member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178034|||http://purl.uniprot.org/annotation/VAR_024994|||http://purl.uniprot.org/annotation/VAR_027414|||http://purl.uniprot.org/annotation/VAR_036557|||http://purl.uniprot.org/annotation/VAR_075078|||http://purl.uniprot.org/annotation/VAR_075079|||http://purl.uniprot.org/annotation/VAR_075080|||http://purl.uniprot.org/annotation/VAR_075081|||http://purl.uniprot.org/annotation/VAR_075082|||http://purl.uniprot.org/annotation/VAR_075083|||http://purl.uniprot.org/annotation/VSP_029909
http://togogenome.org/gene/9606:PIGG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6RFE8|||http://purl.uniprot.org/uniprot/E7EWV1|||http://purl.uniprot.org/uniprot/Q5H8A4|||http://purl.uniprot.org/uniprot/Q8NCI4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Found in SNIBFIS; unknown pathological significance.|||GPI ethanolamine phosphate transferase 2|||GPI ethanolamine phosphate transferase 2 C-terminal|||Helical|||In NEDHSCA.|||In NEDHSCA; almost complete loss of ethanolamine phosphate transferase activity as evidenced by abnormal accumulation of the GPI precursors H7 and H7' and absence of mature GPI precursor H8 in patient lymphoblasts; does not affect protein expression levels in transfected HEK293 cells.|||In NEDHSCA; decreased protein abundance.|||In NEDHSCA; loss of ethanolamine phosphate transferase activity as evidenced by abnormal accumulation of the GPI precursors H7 and H7' and absence of mature GPI precursor H8 in patient lymphoblasts.|||In NEDHSCA; unable to rescue surface expression of Emm in PIGG-null cells.|||In NEDHSCA; unknown pathological significance.|||In NEDHSCA; unknown pathological significance; shows a mild decrease in phosphotransferase activity.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246185|||http://purl.uniprot.org/annotation/VAR_027022|||http://purl.uniprot.org/annotation/VAR_027023|||http://purl.uniprot.org/annotation/VAR_027024|||http://purl.uniprot.org/annotation/VAR_027025|||http://purl.uniprot.org/annotation/VAR_057680|||http://purl.uniprot.org/annotation/VAR_060086|||http://purl.uniprot.org/annotation/VAR_060087|||http://purl.uniprot.org/annotation/VAR_076775|||http://purl.uniprot.org/annotation/VAR_083080|||http://purl.uniprot.org/annotation/VAR_083081|||http://purl.uniprot.org/annotation/VAR_087224|||http://purl.uniprot.org/annotation/VAR_087225|||http://purl.uniprot.org/annotation/VAR_087226|||http://purl.uniprot.org/annotation/VAR_087227|||http://purl.uniprot.org/annotation/VAR_087228|||http://purl.uniprot.org/annotation/VAR_087229|||http://purl.uniprot.org/annotation/VAR_087230|||http://purl.uniprot.org/annotation/VAR_087231|||http://purl.uniprot.org/annotation/VAR_087232|||http://purl.uniprot.org/annotation/VAR_087233|||http://purl.uniprot.org/annotation/VAR_087234|||http://purl.uniprot.org/annotation/VAR_087235|||http://purl.uniprot.org/annotation/VAR_087236|||http://purl.uniprot.org/annotation/VAR_087237|||http://purl.uniprot.org/annotation/VAR_087238|||http://purl.uniprot.org/annotation/VAR_087239|||http://purl.uniprot.org/annotation/VAR_087240|||http://purl.uniprot.org/annotation/VAR_087241|||http://purl.uniprot.org/annotation/VSP_019827|||http://purl.uniprot.org/annotation/VSP_019828|||http://purl.uniprot.org/annotation/VSP_019829|||http://purl.uniprot.org/annotation/VSP_019830|||http://purl.uniprot.org/annotation/VSP_019831|||http://purl.uniprot.org/annotation/VSP_019832|||http://purl.uniprot.org/annotation/VSP_019833|||http://purl.uniprot.org/annotation/VSP_054387|||http://purl.uniprot.org/annotation/VSP_054388
http://togogenome.org/gene/9606:ANAPC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1A4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Anaphase-promoting complex subunit 1|||Disordered|||PC 1|||PC 2|||PC 3|||PC 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215871
http://togogenome.org/gene/9606:DCDC2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2VCK2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305008
http://togogenome.org/gene/9606:SLC2A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRM0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased fructose transport. Higher affinity and lower transport capacity for urate.|||Decreased urate uptake. Decreased Vmax for urate transport. Has no effect on glucose transport.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In RHUC2; decreased protein expression; decreased urate uptake; no effect on glucose transport.|||In RHUC2; decreased urate uptake; increased Km for urate; no effect on protein expression; no effect on glucose transport.|||In RHUC2; markedly reduced urate transport activity; decreased Vmax; decreased urate uptake; no effect on protein expression; no effect on glucose transport.|||In RHUC2; markedly reduced urate transport activity; decreased Vmax; no effect on protein expression; no effect on glucose transport.|||In RHUC2; markedly reduced urate transport activity; decreased protein expression; decreased urate uptake; no effect on glucose transport.|||In RHUC2; reduced urate transport activity; decreased protein expression; decreased urate uptake; no effect on glucose transport.|||In RHUC2; unknown pathological significance; according to PubMed:18701466 the variant results in decreased urate uptake, however according to PubMed:22132964 and PubMed:29967582 urate transport activity is not affected; no effect on Vmax for urate uptake; no effect on affinity for urate; no effect on protein expression; no effect on localization to plasma membrane; no effect on glucose transport.|||In RHUC2; unknown pathological significance; according to PubMed:21810765 the variant results in markedly reduced urate uptake, however according to PubMed:29967582 urate transport activity is not affected; no effect on Vmax; no effect on Km for urate; decreased protein expression; no effect on glucose transport.|||In isoform 2.|||Increased fructose binding affinity and decreased fructose transport capacity.|||Increased fructose transport. Highly reduced urate transport.|||N-linked (GlcNAc...) asparagine|||No effect on fructose transport. Higher affinity and lower transport capacity for urate.|||No effect on fructose transport. Highly reduced urate transport.|||No effect on fructose transport. Increased urate binding affinity and decreased urate transport capacity.|||No effect on urate and fructose transport.|||No effect on urate transport activity.|||No effect on urate transport activity; no effect on protein expression; no effect on glucose transport.|||No effect on urate transport activity; no effect on urate transport; no effect on protein expression; no effect on glucose transport.|||Phosphoserine|||Solute carrier family 2, facilitated glucose transporter member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050378|||http://purl.uniprot.org/annotation/VAR_012157|||http://purl.uniprot.org/annotation/VAR_012158|||http://purl.uniprot.org/annotation/VAR_012159|||http://purl.uniprot.org/annotation/VAR_020337|||http://purl.uniprot.org/annotation/VAR_045648|||http://purl.uniprot.org/annotation/VAR_045649|||http://purl.uniprot.org/annotation/VAR_045650|||http://purl.uniprot.org/annotation/VAR_045651|||http://purl.uniprot.org/annotation/VAR_045652|||http://purl.uniprot.org/annotation/VAR_045653|||http://purl.uniprot.org/annotation/VAR_065772|||http://purl.uniprot.org/annotation/VAR_065773|||http://purl.uniprot.org/annotation/VAR_065774|||http://purl.uniprot.org/annotation/VAR_065775|||http://purl.uniprot.org/annotation/VAR_065776|||http://purl.uniprot.org/annotation/VAR_075343|||http://purl.uniprot.org/annotation/VAR_082920|||http://purl.uniprot.org/annotation/VAR_086380|||http://purl.uniprot.org/annotation/VAR_086381|||http://purl.uniprot.org/annotation/VSP_034860
http://togogenome.org/gene/9606:MIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30301                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Deamidated asparagine; by deterioration|||Extracellular|||Helical|||Important for water channel gating|||In CTRCT15.|||In CTRCT15; likely benign variant.|||In CTRCT15; loss of plasma membrane expression.|||In CTRCT15; non-progressive lamellar cataract; loss of activity.|||In CTRCT15; progressive polymorphic and lamellar cataract; loss of activity.|||In CTRCT15; reduces cell-to-cell adhesion, reduces cell-to-cell gap junction coupling, no loss of cell membrane localization, no loss of water channel activity.|||In CTRCT15; unknown pathological significance.|||In CTRCT15; unknown pathological significance; loss of plasma membrane expression.|||Interaction with BFSP1|||Interaction with CALM|||Lens fiber major intrinsic protein|||NPA 1|||NPA 2|||Phosphoserine|||interaction with BFSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063912|||http://purl.uniprot.org/annotation/VAR_011497|||http://purl.uniprot.org/annotation/VAR_011498|||http://purl.uniprot.org/annotation/VAR_071601|||http://purl.uniprot.org/annotation/VAR_071602|||http://purl.uniprot.org/annotation/VAR_071603|||http://purl.uniprot.org/annotation/VAR_071604|||http://purl.uniprot.org/annotation/VAR_075528|||http://purl.uniprot.org/annotation/VAR_075529|||http://purl.uniprot.org/annotation/VAR_084819|||http://purl.uniprot.org/annotation/VAR_084820|||http://purl.uniprot.org/annotation/VAR_084821
http://togogenome.org/gene/9606:BTBD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYR4|||http://purl.uniprot.org/uniprot/Q96KE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein 6|||Disordered|||In isoform 2.|||In isoform 3.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186213|||http://purl.uniprot.org/annotation/VSP_061435|||http://purl.uniprot.org/annotation/VSP_061436
http://togogenome.org/gene/9606:SPTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11277                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by P.falciparum SERA6|||Actin-binding|||Basic and acidic residues|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In EL3; Buffalo.|||In EL3; Cagliary.|||In EL3; Kayes.|||In EL3; Linguere.|||In EL3; Paris.|||In EL3; Providence.|||In SPH2; spectrin Kissimmee.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||Spectrin beta chain, erythrocytic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073459|||http://purl.uniprot.org/annotation/VAR_001352|||http://purl.uniprot.org/annotation/VAR_001353|||http://purl.uniprot.org/annotation/VAR_001354|||http://purl.uniprot.org/annotation/VAR_001355|||http://purl.uniprot.org/annotation/VAR_001356|||http://purl.uniprot.org/annotation/VAR_001357|||http://purl.uniprot.org/annotation/VAR_001358|||http://purl.uniprot.org/annotation/VAR_001359|||http://purl.uniprot.org/annotation/VAR_001360|||http://purl.uniprot.org/annotation/VAR_001361|||http://purl.uniprot.org/annotation/VAR_001362|||http://purl.uniprot.org/annotation/VAR_038514|||http://purl.uniprot.org/annotation/VAR_038515|||http://purl.uniprot.org/annotation/VAR_061084|||http://purl.uniprot.org/annotation/VSP_000719|||http://purl.uniprot.org/annotation/VSP_007242
http://togogenome.org/gene/9606:PSMA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YLC2|||http://purl.uniprot.org/uniprot/H0YN18|||http://purl.uniprot.org/uniprot/P25789                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Proteasome alpha-type subunits|||Proteasome subunit alpha type-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124103|||http://purl.uniprot.org/annotation/VSP_043102
http://togogenome.org/gene/9606:AOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19801                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  2',4',5'-topaquinone|||Amiloride-sensitive amine oxidase [copper-containing]|||In isoform 2.|||Interchain|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Schiff-base intermediate with substrate; via topaquinone                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035666|||http://purl.uniprot.org/annotation/VAR_007542|||http://purl.uniprot.org/annotation/VAR_025078|||http://purl.uniprot.org/annotation/VAR_025079|||http://purl.uniprot.org/annotation/VAR_025080|||http://purl.uniprot.org/annotation/VAR_025081|||http://purl.uniprot.org/annotation/VSP_055190
http://togogenome.org/gene/9606:IRX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78411                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox; TALE-type|||In HMMS; hypomorphic mutation.|||In isoform 2.|||In isoform 3.|||Iroquois-class homeodomain protein IRX-5|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049160|||http://purl.uniprot.org/annotation/VAR_068483|||http://purl.uniprot.org/annotation/VAR_068484|||http://purl.uniprot.org/annotation/VSP_047363|||http://purl.uniprot.org/annotation/VSP_047364
http://togogenome.org/gene/9606:ENOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16206|||http://purl.uniprot.org/uniprot/Q32ND0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Ecto-NOX disulfide-thiol exchanger 2|||In isoform 2.|||Loss of activity.|||No effect on activity but response to capsaicin is lost.|||No effect on activity.|||Period length of activity extended to 36 minutes.|||Period length of activity extended to 42 minutes.|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079275|||http://purl.uniprot.org/annotation/VAR_069427|||http://purl.uniprot.org/annotation/VSP_015719
http://togogenome.org/gene/9606:KCNA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22001                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Phosphoserine; by PKA|||Potassium voltage-gated channel subfamily A member 3|||S-palmitoyl cysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053977
http://togogenome.org/gene/9606:PSME3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ25|||http://purl.uniprot.org/uniprot/P61289|||http://purl.uniprot.org/uniprot/V9HWJ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Assembles into less stable hexamers/heptamers and therefore impairs specificity of activation of trypsin-like subunits of the proteasome.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine; by P300/CBP|||Phosphoserine|||Phosphoserine; by CHEK2|||Proteasome activator PA28 C-terminal|||Proteasome activator PA28 N-terminal|||Proteasome activator complex subunit 3|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161789|||http://purl.uniprot.org/annotation/VSP_004516|||http://purl.uniprot.org/annotation/VSP_055047
http://togogenome.org/gene/9606:NDEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIZ0|||http://purl.uniprot.org/uniprot/Q9GZM8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with DISC1; when associated with A-266.|||Abolishes interaction with DISC1; when associated with A-267.|||Abolishes oligopeptidase activity.|||Abrogates mitotic phosphorylation; when associated with A-198; A-231; A-242 and V-245.|||Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and A-242.|||Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and V-245.|||Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-198 and A-219.|||Abrogates mitotic phosphorylation; when associated with V-219; A-231; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-219 and A-231.|||Abrogates phosphorylation by CDK5; when associated with A-198 and A-231.|||Disordered|||Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-242.|||Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-245.|||Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-242 and E-245.|||Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-231; E-242 and E-245.|||Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-219; E-231; E-242 and E-245.|||In isoform 2.|||In isoform 3.|||Interaction with CENPF|||Interaction with DISC1|||Interaction with KATNA1|||Interaction with KATNB1|||Interaction with NEFL|||Interaction with YWHAE|||NUDE|||Nuclear distribution protein nudE-like 1|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphothreonine; by CDK1 and MAPK1|||Required for interaction with PAFAH1B1|||Required for localization to the centrosome and interaction with dynein, dynactin, tubulin gamma, PCM1 and PCNT|||S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7|||Self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240210|||http://purl.uniprot.org/annotation/VSP_019310|||http://purl.uniprot.org/annotation/VSP_047509
http://togogenome.org/gene/9606:HMGN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82970                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||High mobility group nucleosome-binding domain-containing protein 5|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206717
http://togogenome.org/gene/9606:ITIH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXX5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Inter-alpha-trypsin inhibitor heavy chain H6|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues|||VIT|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285680|||http://purl.uniprot.org/annotation/VAR_032042|||http://purl.uniprot.org/annotation/VAR_032043|||http://purl.uniprot.org/annotation/VAR_032044|||http://purl.uniprot.org/annotation/VAR_032045
http://togogenome.org/gene/9606:CHAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Chromosome alignment-maintaining phosphoprotein 1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Mediates interaction with MAD2L2|||Mediates localization to the chromosome and the spindle and negatively regulates chromosome alignment|||Mediates localization to the spindle and the kinetochore and is required for the attachment of spindle microtubules to the kinetochore|||N-acetylmethionine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248319|||http://purl.uniprot.org/annotation/VAR_027270|||http://purl.uniprot.org/annotation/VAR_027271|||http://purl.uniprot.org/annotation/VAR_052910
http://togogenome.org/gene/9606:TMEM68                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RJN2|||http://purl.uniprot.org/uniprot/Q96MH6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||In isoform 3.|||Monoacylglycerol/Diacylglycerol O-acyltransferase|||Phospholipid/glycerol acyltransferase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254592|||http://purl.uniprot.org/annotation/VSP_021244|||http://purl.uniprot.org/annotation/VSP_021245|||http://purl.uniprot.org/annotation/VSP_021246
http://togogenome.org/gene/9606:GJB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A654ICJ7|||http://purl.uniprot.org/uniprot/P08034                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Connexin N-terminal|||Cytoplasmic|||Extracellular|||Gap junction beta-1 protein|||Gap junction protein cysteine-rich|||Helical|||In CMTX1 and DSS; found in a DSS patient with severe symptoms also carrying W-359 in the EGR2 gene; may act as a modifier of disease severity.|||In CMTX1.|||In CMTX1; demyelinating form.|||In CMTX1; forms channels normally.|||In CMTX1; functional channel.|||In CMTX1; functional channel; localized in the Golgi apparatus without reaching the cell membrane.|||In CMTX1; localized in the Golgi apparatus but also forming rare small gap junction-like plaques.|||In CMTX1; localized in the Golgi apparatus but also forming rare small junction-like plaques.|||In CMTX1; localized in the Golgi apparatus without reaching the cell membrane.|||In CMTX1; localized mainly on the cell membrane forming gap junction-like plaques.|||In CMTX1; localized to the endoplasmic reticulum.|||In CMTX1; mild phenotype; increased sensitivity to acidification-induced closure.|||In CMTX1; mild.|||In CMTX1; mild/moderate.|||In CMTX1; mild/moderate; non-functional channel.|||In CMTX1; moderate.|||In CMTX1; mutant have a higher open probability than hemichannels formed of GJB1 wild-type.|||In CMTX1; non-detectable levels of hemichannel activation and non-detectable levels of electrical coupling.|||In CMTX1; non-functional channel.|||In CMTX1; profoundly impaired in their ability to support the earliest stages of regeneration of myelinated fibers.|||In CMTX1; requires 2 nucleotide substitutions.|||In CMTX1; severe.|||In CMTX1; suggests a failure to incorporate the mutant protein in the cell membrane.|||In CMTX1; the mutation causes abnormal hemichannel opening with excessive permeability of the plasma membrane and decreased cell survival.|||In CMTX1; unknown pathological significance.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057849|||http://purl.uniprot.org/annotation/VAR_002006|||http://purl.uniprot.org/annotation/VAR_002007|||http://purl.uniprot.org/annotation/VAR_002008|||http://purl.uniprot.org/annotation/VAR_002009|||http://purl.uniprot.org/annotation/VAR_002010|||http://purl.uniprot.org/annotation/VAR_002011|||http://purl.uniprot.org/annotation/VAR_002012|||http://purl.uniprot.org/annotation/VAR_002013|||http://purl.uniprot.org/annotation/VAR_002014|||http://purl.uniprot.org/annotation/VAR_002015|||http://purl.uniprot.org/annotation/VAR_002016|||http://purl.uniprot.org/annotation/VAR_002017|||http://purl.uniprot.org/annotation/VAR_002018|||http://purl.uniprot.org/annotation/VAR_002019|||http://purl.uniprot.org/annotation/VAR_002020|||http://purl.uniprot.org/annotation/VAR_002021|||http://purl.uniprot.org/annotation/VAR_002022|||http://purl.uniprot.org/annotation/VAR_002023|||http://purl.uniprot.org/annotation/VAR_002024|||http://purl.uniprot.org/annotation/VAR_002025|||http://purl.uniprot.org/annotation/VAR_002026|||http://purl.uniprot.org/annotation/VAR_002027|||http://purl.uniprot.org/annotation/VAR_002028|||http://purl.uniprot.org/annotation/VAR_002029|||http://purl.uniprot.org/annotation/VAR_002030|||http://purl.uniprot.org/annotation/VAR_002031|||http://purl.uniprot.org/annotation/VAR_002032|||http://purl.uniprot.org/annotation/VAR_002033|||http://purl.uniprot.org/annotation/VAR_002034|||http://purl.uniprot.org/annotation/VAR_002035|||http://purl.uniprot.org/annotation/VAR_002036|||http://purl.uniprot.org/annotation/VAR_002037|||http://purl.uniprot.org/annotation/VAR_002038|||http://purl.uniprot.org/annotation/VAR_002039|||http://purl.uniprot.org/annotation/VAR_002040|||http://purl.uniprot.org/annotation/VAR_002041|||http://purl.uniprot.org/annotation/VAR_002042|||http://purl.uniprot.org/annotation/VAR_002043|||http://purl.uniprot.org/annotation/VAR_002044|||http://purl.uniprot.org/annotation/VAR_002045|||http://purl.uniprot.org/annotation/VAR_002046|||http://purl.uniprot.org/annotation/VAR_002047|||http://purl.uniprot.org/annotation/VAR_002048|||http://purl.uniprot.org/annotation/VAR_002049|||http://purl.uniprot.org/annotation/VAR_002050|||http://purl.uniprot.org/annotation/VAR_002051|||http://purl.uniprot.org/annotation/VAR_002052|||http://purl.uniprot.org/annotation/VAR_002053|||http://purl.uniprot.org/annotation/VAR_002054|||http://purl.uniprot.org/annotation/VAR_002055|||http://purl.uniprot.org/annotation/VAR_002056|||http://purl.uniprot.org/annotation/VAR_002057|||http://purl.uniprot.org/annotation/VAR_002058|||http://purl.uniprot.org/annotation/VAR_002059|||http://purl.uniprot.org/annotation/VAR_002060|||http://purl.uniprot.org/annotation/VAR_002061|||http://purl.uniprot.org/annotation/VAR_002062|||http://purl.uniprot.org/annotation/VAR_002063|||http://purl.uniprot.org/annotation/VAR_002064|||http://purl.uniprot.org/annotation/VAR_002065|||http://purl.uniprot.org/annotation/VAR_002066|||http://purl.uniprot.org/annotation/VAR_002067|||http://purl.uniprot.org/annotation/VAR_002068|||http://purl.uniprot.org/annotation/VAR_002069|||http://purl.uniprot.org/annotation/VAR_002070|||http://purl.uniprot.org/annotation/VAR_002071|||http://purl.uniprot.org/annotation/VAR_002072|||http://purl.uniprot.org/annotation/VAR_002073|||http://purl.uniprot.org/annotation/VAR_002074|||http://purl.uniprot.org/annotation/VAR_002075|||http://purl.uniprot.org/annotation/VAR_002076|||http://purl.uniprot.org/annotation/VAR_002077|||http://purl.uniprot.org/annotation/VAR_002078|||http://purl.uniprot.org/annotation/VAR_002079|||http://purl.uniprot.org/annotation/VAR_002080|||http://purl.uniprot.org/annotation/VAR_002081|||http://purl.uniprot.org/annotation/VAR_002082|||http://purl.uniprot.org/annotation/VAR_002083|||http://purl.uniprot.org/annotation/VAR_002084|||http://purl.uniprot.org/annotation/VAR_002085|||http://purl.uniprot.org/annotation/VAR_002086|||http://purl.uniprot.org/annotation/VAR_002087|||http://purl.uniprot.org/annotation/VAR_002088|||http://purl.uniprot.org/annotation/VAR_002089|||http://purl.uniprot.org/annotation/VAR_002090|||http://purl.uniprot.org/annotation/VAR_002091|||http://purl.uniprot.org/annotation/VAR_002092|||http://purl.uniprot.org/annotation/VAR_002093|||http://purl.uniprot.org/annotation/VAR_002094|||http://purl.uniprot.org/annotation/VAR_002095|||http://purl.uniprot.org/annotation/VAR_002096|||http://purl.uniprot.org/annotation/VAR_002097|||http://purl.uniprot.org/annotation/VAR_002098|||http://purl.uniprot.org/annotation/VAR_002099|||http://purl.uniprot.org/annotation/VAR_002100|||http://purl.uniprot.org/annotation/VAR_002101|||http://purl.uniprot.org/annotation/VAR_002102|||http://purl.uniprot.org/annotation/VAR_002103|||http://purl.uniprot.org/annotation/VAR_002104|||http://purl.uniprot.org/annotation/VAR_002105|||http://purl.uniprot.org/annotation/VAR_002106|||http://purl.uniprot.org/annotation/VAR_002107|||http://purl.uniprot.org/annotation/VAR_002108|||http://purl.uniprot.org/annotation/VAR_002109|||http://purl.uniprot.org/annotation/VAR_002110|||http://purl.uniprot.org/annotation/VAR_002111|||http://purl.uniprot.org/annotation/VAR_002112|||http://purl.uniprot.org/annotation/VAR_002113|||http://purl.uniprot.org/annotation/VAR_002114|||http://purl.uniprot.org/annotation/VAR_002115|||http://purl.uniprot.org/annotation/VAR_002116|||http://purl.uniprot.org/annotation/VAR_002117|||http://purl.uniprot.org/annotation/VAR_002118|||http://purl.uniprot.org/annotation/VAR_002119|||http://purl.uniprot.org/annotation/VAR_002120|||http://purl.uniprot.org/annotation/VAR_002121|||http://purl.uniprot.org/annotation/VAR_002122|||http://purl.uniprot.org/annotation/VAR_002123|||http://purl.uniprot.org/annotation/VAR_002124|||http://purl.uniprot.org/annotation/VAR_002125|||http://purl.uniprot.org/annotation/VAR_002126|||http://purl.uniprot.org/annotation/VAR_002127|||http://purl.uniprot.org/annotation/VAR_002128|||http://purl.uniprot.org/annotation/VAR_002129|||http://purl.uniprot.org/annotation/VAR_002130|||http://purl.uniprot.org/annotation/VAR_002131|||http://purl.uniprot.org/annotation/VAR_002132|||http://purl.uniprot.org/annotation/VAR_002133|||http://purl.uniprot.org/annotation/VAR_002134|||http://purl.uniprot.org/annotation/VAR_002135|||http://purl.uniprot.org/annotation/VAR_002136|||http://purl.uniprot.org/annotation/VAR_008137|||http://purl.uniprot.org/annotation/VAR_008138|||http://purl.uniprot.org/annotation/VAR_012313|||http://purl.uniprot.org/annotation/VAR_021611|||http://purl.uniprot.org/annotation/VAR_021612|||http://purl.uniprot.org/annotation/VAR_029894|||http://purl.uniprot.org/annotation/VAR_029895|||http://purl.uniprot.org/annotation/VAR_029896|||http://purl.uniprot.org/annotation/VAR_029897|||http://purl.uniprot.org/annotation/VAR_029898|||http://purl.uniprot.org/annotation/VAR_029899|||http://purl.uniprot.org/annotation/VAR_029900|||http://purl.uniprot.org/annotation/VAR_029901|||http://purl.uniprot.org/annotation/VAR_029902|||http://purl.uniprot.org/annotation/VAR_029903|||http://purl.uniprot.org/annotation/VAR_029904|||http://purl.uniprot.org/annotation/VAR_029905|||http://purl.uniprot.org/annotation/VAR_029906|||http://purl.uniprot.org/annotation/VAR_029907|||http://purl.uniprot.org/annotation/VAR_029908|||http://purl.uniprot.org/annotation/VAR_029909|||http://purl.uniprot.org/annotation/VAR_029910|||http://purl.uniprot.org/annotation/VAR_029911|||http://purl.uniprot.org/annotation/VAR_029912|||http://purl.uniprot.org/annotation/VAR_029913|||http://purl.uniprot.org/annotation/VAR_029914|||http://purl.uniprot.org/annotation/VAR_029915|||http://purl.uniprot.org/annotation/VAR_029916|||http://purl.uniprot.org/annotation/VAR_029917|||http://purl.uniprot.org/annotation/VAR_029918|||http://purl.uniprot.org/annotation/VAR_029919|||http://purl.uniprot.org/annotation/VAR_029920|||http://purl.uniprot.org/annotation/VAR_029921|||http://purl.uniprot.org/annotation/VAR_029922|||http://purl.uniprot.org/annotation/VAR_029923|||http://purl.uniprot.org/annotation/VAR_029924|||http://purl.uniprot.org/annotation/VAR_029925|||http://purl.uniprot.org/annotation/VAR_029926|||http://purl.uniprot.org/annotation/VAR_029927|||http://purl.uniprot.org/annotation/VAR_029928|||http://purl.uniprot.org/annotation/VAR_029929|||http://purl.uniprot.org/annotation/VAR_029930|||http://purl.uniprot.org/annotation/VAR_029931|||http://purl.uniprot.org/annotation/VAR_029932|||http://purl.uniprot.org/annotation/VAR_029933|||http://purl.uniprot.org/annotation/VAR_029934|||http://purl.uniprot.org/annotation/VAR_029935|||http://purl.uniprot.org/annotation/VAR_029936|||http://purl.uniprot.org/annotation/VAR_029937|||http://purl.uniprot.org/annotation/VAR_029938|||http://purl.uniprot.org/annotation/VAR_029939|||http://purl.uniprot.org/annotation/VAR_029940|||http://purl.uniprot.org/annotation/VAR_029941|||http://purl.uniprot.org/annotation/VAR_029942|||http://purl.uniprot.org/annotation/VAR_029943|||http://purl.uniprot.org/annotation/VAR_029944|||http://purl.uniprot.org/annotation/VAR_029945|||http://purl.uniprot.org/annotation/VAR_029946|||http://purl.uniprot.org/annotation/VAR_029947|||http://purl.uniprot.org/annotation/VAR_029948|||http://purl.uniprot.org/annotation/VAR_029949|||http://purl.uniprot.org/annotation/VAR_029950|||http://purl.uniprot.org/annotation/VAR_029951|||http://purl.uniprot.org/annotation/VAR_029952|||http://purl.uniprot.org/annotation/VAR_029953|||http://purl.uniprot.org/annotation/VAR_029954|||http://purl.uniprot.org/annotation/VAR_029955|||http://purl.uniprot.org/annotation/VAR_029956|||http://purl.uniprot.org/annotation/VAR_029957|||http://purl.uniprot.org/annotation/VAR_076567
http://togogenome.org/gene/9606:RNPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BMS0|||http://purl.uniprot.org/uniprot/Q15287                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes exon-skipping.|||Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization.|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs interaction with SAP18.|||In isoform 2 and isoform 3.|||In isoform 3.|||Interaction with SAP18 and ACIN1|||N6-acetyllysine|||Necessary for interaction with PNN and exon-skipping|||Necessary for interaction with SRP54, nuclear localization and exon-skipping|||Necessary for interaction with TRA2B, nuclear localization and exon-skipping|||Necessary for interaction with the cleaved p110 isoform of CDC2L1|||Necessary for interactions with UPF2 and UPF3B and UPF2-dependent NMD|||Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization.|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||Pro residues|||RNA-binding protein with serine-rich domain 1|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081816|||http://purl.uniprot.org/annotation/VSP_016243|||http://purl.uniprot.org/annotation/VSP_037601
http://togogenome.org/gene/9606:ACTBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q562R1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Beta-actin-like protein 2|||Methionine (R)-sulfoxide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318849
http://togogenome.org/gene/9606:OR2Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVT8|||http://purl.uniprot.org/uniprot/Q8NG97                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2Z1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150514|||http://purl.uniprot.org/annotation/VAR_062031
http://togogenome.org/gene/9606:VSTM2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLU5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type|||Polar residues|||V-set and transmembrane domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319943
http://togogenome.org/gene/9606:KRT27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3Y8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type I cytoskeletal 27|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312701|||http://purl.uniprot.org/annotation/VAR_056007|||http://purl.uniprot.org/annotation/VAR_056008|||http://purl.uniprot.org/annotation/VAR_063138|||http://purl.uniprot.org/annotation/VAR_063139|||http://purl.uniprot.org/annotation/VAR_063140
http://togogenome.org/gene/9606:FYCO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQS8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||FYVE and coiled-coil domain-containing protein 1|||FYVE-type|||GOLD|||In CTRCT18.|||In CTRCT18; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RUN|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245837|||http://purl.uniprot.org/annotation/VAR_027006|||http://purl.uniprot.org/annotation/VAR_027007|||http://purl.uniprot.org/annotation/VAR_027008|||http://purl.uniprot.org/annotation/VAR_027009|||http://purl.uniprot.org/annotation/VAR_027010|||http://purl.uniprot.org/annotation/VAR_027011|||http://purl.uniprot.org/annotation/VAR_056882|||http://purl.uniprot.org/annotation/VAR_056883|||http://purl.uniprot.org/annotation/VAR_065974|||http://purl.uniprot.org/annotation/VAR_084824|||http://purl.uniprot.org/annotation/VSP_019795|||http://purl.uniprot.org/annotation/VSP_019796|||http://purl.uniprot.org/annotation/VSP_019797|||http://purl.uniprot.org/annotation/VSP_054477
http://togogenome.org/gene/9606:NUCKS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1E3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057978|||http://purl.uniprot.org/annotation/VAR_051246|||http://purl.uniprot.org/annotation/VAR_051247|||http://purl.uniprot.org/annotation/VSP_021770
http://togogenome.org/gene/9606:CLDN16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5I7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Claudin-16|||Cytoplasmic|||Extracellular|||Helical|||In HOMG3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144774|||http://purl.uniprot.org/annotation/VAR_008172|||http://purl.uniprot.org/annotation/VAR_008174|||http://purl.uniprot.org/annotation/VAR_008175|||http://purl.uniprot.org/annotation/VAR_008176|||http://purl.uniprot.org/annotation/VAR_008177|||http://purl.uniprot.org/annotation/VAR_008178|||http://purl.uniprot.org/annotation/VAR_008179|||http://purl.uniprot.org/annotation/VAR_017228|||http://purl.uniprot.org/annotation/VAR_017229|||http://purl.uniprot.org/annotation/VAR_017230|||http://purl.uniprot.org/annotation/VAR_017231|||http://purl.uniprot.org/annotation/VAR_017232|||http://purl.uniprot.org/annotation/VAR_017233|||http://purl.uniprot.org/annotation/VAR_017234|||http://purl.uniprot.org/annotation/VAR_017235|||http://purl.uniprot.org/annotation/VAR_017236|||http://purl.uniprot.org/annotation/VAR_017237
http://togogenome.org/gene/9606:AADACL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUY0                                                                                  ^@                                                                                  Active Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Motif|||Sequence Variant                                                                                  ^@                                                                                  Arylacetamide deacetylase-like 3|||Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000265936|||http://purl.uniprot.org/annotation/VAR_060665|||http://purl.uniprot.org/annotation/VAR_060666|||http://purl.uniprot.org/annotation/VAR_060667|||http://purl.uniprot.org/annotation/VAR_060668|||http://purl.uniprot.org/annotation/VAR_060670|||http://purl.uniprot.org/annotation/VAR_060671
http://togogenome.org/gene/9606:CXCL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q07325                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Signal Peptide                                                                                  ^@                                                                                  Basic residues|||C-X-C motif chemokine 9|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005099
http://togogenome.org/gene/9606:ARPIN-AP3S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYH1                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent                                                                                  ^@                                                                                  AP complex mu/sigma subunit                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:OR12D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D2XT27|||http://purl.uniprot.org/uniprot/Q9UGF7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 12D3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150729|||http://purl.uniprot.org/annotation/VAR_020383|||http://purl.uniprot.org/annotation/VAR_036209|||http://purl.uniprot.org/annotation/VAR_053298
http://togogenome.org/gene/9606:NPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJE6|||http://purl.uniprot.org/uniprot/P16066                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Atrial natriuretic peptide receptor 1|||Cytoplasmic|||Extracellular|||Guanylate cyclase|||Helical|||In a breast pleomorphic lobular carcinoma sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012360|||http://purl.uniprot.org/annotation/PRO_5007491729|||http://purl.uniprot.org/annotation/VAR_042214|||http://purl.uniprot.org/annotation/VAR_042215|||http://purl.uniprot.org/annotation/VAR_042216|||http://purl.uniprot.org/annotation/VAR_042217|||http://purl.uniprot.org/annotation/VAR_042218
http://togogenome.org/gene/9606:TXNDC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14530                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Phosphoserine|||Thioredoxin|||Thioredoxin domain-containing protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120166|||http://purl.uniprot.org/annotation/VAR_058328|||http://purl.uniprot.org/annotation/VAR_058329|||http://purl.uniprot.org/annotation/VSP_056553
http://togogenome.org/gene/9606:TSFM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KS95|||http://purl.uniprot.org/uniprot/P43897                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Elongation factor Ts, mitochondrial|||In COXPD3.|||In COXPD3; decreased protein abundance; decreased mitochondrial translation products; patient fibroblast phenotype can be rescued by coexpression with wild-type TSFM.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Translation elongation factor EFTs/EF1B dimerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007468|||http://purl.uniprot.org/annotation/VAR_068973|||http://purl.uniprot.org/annotation/VAR_077697|||http://purl.uniprot.org/annotation/VSP_001364|||http://purl.uniprot.org/annotation/VSP_043517|||http://purl.uniprot.org/annotation/VSP_043518|||http://purl.uniprot.org/annotation/VSP_045283|||http://purl.uniprot.org/annotation/VSP_045284
http://togogenome.org/gene/9606:ASB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5HYF3|||http://purl.uniprot.org/uniprot/Q8WWX0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 5|||Helical|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066930|||http://purl.uniprot.org/annotation/VSP_054425
http://togogenome.org/gene/9606:SH3GLB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZC38|||http://purl.uniprot.org/uniprot/Q9NR46                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BAR|||Endophilin-B2|||In isoform 2.|||Membrane-binding amphipathic helix|||N-acetylmethionine|||Phosphoserine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146755|||http://purl.uniprot.org/annotation/VAR_053078|||http://purl.uniprot.org/annotation/VAR_053079|||http://purl.uniprot.org/annotation/VSP_009278|||http://purl.uniprot.org/annotation/VSP_009279
http://togogenome.org/gene/9606:MCHR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99705                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Melanin-concentrating hormone receptor 1|||N-linked (GlcNAc...) asparagine|||No changes in receptor binding or functional signaling.|||No significant functional differences.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069734|||http://purl.uniprot.org/annotation/VAR_016221|||http://purl.uniprot.org/annotation/VAR_026652|||http://purl.uniprot.org/annotation/VAR_026653|||http://purl.uniprot.org/annotation/VAR_026654|||http://purl.uniprot.org/annotation/VAR_026655|||http://purl.uniprot.org/annotation/VAR_026656|||http://purl.uniprot.org/annotation/VAR_026657|||http://purl.uniprot.org/annotation/VAR_026658|||http://purl.uniprot.org/annotation/VAR_026659|||http://purl.uniprot.org/annotation/VAR_026660|||http://purl.uniprot.org/annotation/VAR_049417
http://togogenome.org/gene/9606:TBC1D21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYX1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Arginine finger|||Glutamine finger|||In isoform 2.|||Rab-GAP TBC|||TBC1 domain family member 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208050|||http://purl.uniprot.org/annotation/VAR_034544|||http://purl.uniprot.org/annotation/VSP_053999
http://togogenome.org/gene/9606:SMCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49901|||http://purl.uniprot.org/uniprot/Q5T7P5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X 7 (OR 8) AA approximate repeats|||Disordered|||Polar residues|||Sperm mitochondrial-associated cysteine-rich protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096307
http://togogenome.org/gene/9606:CBX8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Chromo|||Chromobox protein homolog 8|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080215|||http://purl.uniprot.org/annotation/VAR_014954
http://togogenome.org/gene/9606:CA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTY8|||http://purl.uniprot.org/uniprot/Q9NS85                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase-related protein 10|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000077436|||http://purl.uniprot.org/annotation/PRO_5017202253|||http://purl.uniprot.org/annotation/VSP_056940
http://togogenome.org/gene/9606:PFN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHR9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Profilin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199581
http://togogenome.org/gene/9606:GK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZS86                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Putative glycerol kinase 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000323754|||http://purl.uniprot.org/annotation/VSP_032121|||http://purl.uniprot.org/annotation/VSP_032122|||http://purl.uniprot.org/annotation/VSP_032123
http://togogenome.org/gene/9606:RFX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48382                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||DNA-binding protein RFX5|||Disordered|||In BLS2.|||In isoform 2.|||Leucine-rich region; critical for dimer formation and for interaction with RFXAP|||N-acetylalanine|||N-terminal domain|||Phosphoserine|||Polar residues|||PxLPxI/L motif; mediates interaction with RFXANK|||RFX-type winged-helix|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215292|||http://purl.uniprot.org/annotation/VAR_015550|||http://purl.uniprot.org/annotation/VAR_034448|||http://purl.uniprot.org/annotation/VAR_034449|||http://purl.uniprot.org/annotation/VAR_034450|||http://purl.uniprot.org/annotation/VSP_055864
http://togogenome.org/gene/9606:B3GALNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCR0                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In MDDGA11.|||In MDDGA11; affects subcellular localization.|||In MDDGA11; does not affect subcellular localization.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248362|||http://purl.uniprot.org/annotation/VAR_035860|||http://purl.uniprot.org/annotation/VAR_069638|||http://purl.uniprot.org/annotation/VAR_069639|||http://purl.uniprot.org/annotation/VAR_069640|||http://purl.uniprot.org/annotation/VAR_069641|||http://purl.uniprot.org/annotation/VSP_020250|||http://purl.uniprot.org/annotation/VSP_020251|||http://purl.uniprot.org/annotation/VSP_020252
http://togogenome.org/gene/9606:OTUD6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L8S5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Cys-loop|||Disordered|||His-loop|||Nucleophile|||OTU|||OTU domain-containing protein 6A|||Variable-loop                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076277
http://togogenome.org/gene/9606:MCOLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZK6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||INTRAMEM|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Blocks channel activity. Decreases recycling of internalized CD59 to the cell surface.|||Constitutive active Ca(2+) permeable and inward rectifying channel.|||Cytoplasmic|||Does not effect current amplitude; possible effect on regulation.|||Extracellular|||Extracellular/lumenal pore loop|||Helical|||In isoform 2.|||Mucolipin-2|||Pore-forming|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215365|||http://purl.uniprot.org/annotation/VAR_052394|||http://purl.uniprot.org/annotation/VAR_052395|||http://purl.uniprot.org/annotation/VSP_034642
http://togogenome.org/gene/9606:PRR22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ63                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Proline-rich protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332165|||http://purl.uniprot.org/annotation/VAR_042962
http://togogenome.org/gene/9606:FCGBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6R7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  IgGFc-binding|||IgGFc-binding protein|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||TIL 1|||TIL 10|||TIL 11|||TIL 12|||TIL 2|||TIL 3|||TIL 4|||TIL 5|||TIL 6|||TIL 7|||TIL 8|||TIL 9|||VWFD 1|||VWFD 10|||VWFD 11|||VWFD 12|||VWFD 13|||VWFD 2|||VWFD 3|||VWFD 4|||VWFD 5|||VWFD 6|||VWFD 7|||VWFD 8|||VWFD 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256698|||http://purl.uniprot.org/annotation/VAR_028903|||http://purl.uniprot.org/annotation/VAR_028904|||http://purl.uniprot.org/annotation/VAR_028905|||http://purl.uniprot.org/annotation/VAR_028906|||http://purl.uniprot.org/annotation/VAR_028907|||http://purl.uniprot.org/annotation/VAR_028908|||http://purl.uniprot.org/annotation/VAR_028909|||http://purl.uniprot.org/annotation/VAR_028910|||http://purl.uniprot.org/annotation/VAR_028911|||http://purl.uniprot.org/annotation/VAR_028912|||http://purl.uniprot.org/annotation/VAR_028913|||http://purl.uniprot.org/annotation/VAR_028914|||http://purl.uniprot.org/annotation/VAR_028915|||http://purl.uniprot.org/annotation/VAR_028916|||http://purl.uniprot.org/annotation/VAR_054490|||http://purl.uniprot.org/annotation/VAR_054491|||http://purl.uniprot.org/annotation/VAR_054492|||http://purl.uniprot.org/annotation/VAR_054493|||http://purl.uniprot.org/annotation/VAR_054494|||http://purl.uniprot.org/annotation/VAR_054495|||http://purl.uniprot.org/annotation/VAR_054496|||http://purl.uniprot.org/annotation/VAR_054497|||http://purl.uniprot.org/annotation/VAR_054498
http://togogenome.org/gene/9606:CENPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02224                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere-associated protein E|||Cysteine methyl ester|||Disordered|||Globular autoinhibitory domain|||In MCPH13; results in defective mitotic spindle formation and chromosome segregation; results in delayed mitotic progression.|||In isoform 3.|||Kinesin motor|||Kinetochore-binding domain|||Phosphoserine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125436|||http://purl.uniprot.org/annotation/PRO_0000396742|||http://purl.uniprot.org/annotation/VAR_049689|||http://purl.uniprot.org/annotation/VAR_049690|||http://purl.uniprot.org/annotation/VAR_049691|||http://purl.uniprot.org/annotation/VAR_049692|||http://purl.uniprot.org/annotation/VAR_059370|||http://purl.uniprot.org/annotation/VAR_072429|||http://purl.uniprot.org/annotation/VAR_072430|||http://purl.uniprot.org/annotation/VSP_028820|||http://purl.uniprot.org/annotation/VSP_028821
http://togogenome.org/gene/9606:DNAH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99499|||http://purl.uniprot.org/uniprot/Q9NYC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  AAA 1|||AAA 2|||AAA 3|||AAA 4|||AAA 5|||AAA 6|||Dynein axonemal heavy chain 9|||Dynein heavy chain AAA lid|||Dynein heavy chain C-terminal|||Dynein heavy chain region D6 P-loop|||In CILD40.|||In CILD40; associated in cis with E-1881; no protein detected by Western blot when associated with E-1881; loss of localization to cilium axonema when associated with E-1881.|||In CILD40; associated in cis with H-2965; no protein detected by Western blot when associated with H-2965; loss of localization to cilium axonema associated with H-2965.|||In CILD40; loss of localization to cilium axonema.|||In CILD40; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Stalk|||Stem                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114632|||http://purl.uniprot.org/annotation/VAR_036214|||http://purl.uniprot.org/annotation/VAR_036215|||http://purl.uniprot.org/annotation/VAR_036216|||http://purl.uniprot.org/annotation/VAR_046312|||http://purl.uniprot.org/annotation/VAR_046313|||http://purl.uniprot.org/annotation/VAR_046314|||http://purl.uniprot.org/annotation/VAR_046315|||http://purl.uniprot.org/annotation/VAR_046316|||http://purl.uniprot.org/annotation/VAR_046317|||http://purl.uniprot.org/annotation/VAR_046318|||http://purl.uniprot.org/annotation/VAR_046319|||http://purl.uniprot.org/annotation/VAR_046320|||http://purl.uniprot.org/annotation/VAR_046321|||http://purl.uniprot.org/annotation/VAR_046322|||http://purl.uniprot.org/annotation/VAR_046323|||http://purl.uniprot.org/annotation/VAR_046324|||http://purl.uniprot.org/annotation/VAR_046325|||http://purl.uniprot.org/annotation/VAR_046326|||http://purl.uniprot.org/annotation/VAR_046327|||http://purl.uniprot.org/annotation/VAR_081802|||http://purl.uniprot.org/annotation/VAR_081803|||http://purl.uniprot.org/annotation/VAR_081804|||http://purl.uniprot.org/annotation/VAR_081805|||http://purl.uniprot.org/annotation/VAR_081806|||http://purl.uniprot.org/annotation/VAR_081807|||http://purl.uniprot.org/annotation/VAR_081808|||http://purl.uniprot.org/annotation/VAR_081809|||http://purl.uniprot.org/annotation/VSP_035285|||http://purl.uniprot.org/annotation/VSP_043443
http://togogenome.org/gene/9606:FAM228B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C875                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein FAM228B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348449
http://togogenome.org/gene/9606:OR10G3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWE3|||http://purl.uniprot.org/uniprot/Q8NGC4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10G3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150696|||http://purl.uniprot.org/annotation/VAR_053274
http://togogenome.org/gene/9606:NECAB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N987                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ABM|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||N-terminal EF-hand calcium-binding protein 1|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282609|||http://purl.uniprot.org/annotation/VSP_024214
http://togogenome.org/gene/9606:CTBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13363|||http://purl.uniprot.org/uniprot/X5D8Y5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance.|||C-terminal-binding protein 1|||Cleavage; by CAPN1|||Cleavage; by CAPN1 and CAPN3|||D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding|||D-isomer specific 2-hydroxyacid dehydrogenase catalytic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In HADDTS.|||In isoform 2.|||Interaction with GLIS2 1|||Interaction with GLIS2 2|||Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.|||Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.|||Phosphoserine|||Phosphoserine; by HIPK2|||Proton donor|||Reduced proteolytic processing mediated by CAPN3.|||Reduced proteolytic processing mediated by CAPN3; when associated with A-183.|||Reduced proteolytic processing mediated by CAPN3; when associated with A-186.|||Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.|||Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.|||Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.|||Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.|||Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.|||Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.|||Strongly reduces E1A binding; when associated with A-163 and A-171.|||Strongly reduces E1A binding; when associated with A-266; A-290 and A-295.|||Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.|||Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.|||Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.|||Strongly reduces E1A binding; when associated with V-181 and A-204.|||Strongly reduces E1A binding; when associated with V-181 and V-183.|||Strongly reduces E1A binding; when associated with V-183 and A-204.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076041|||http://purl.uniprot.org/annotation/VAR_080622|||http://purl.uniprot.org/annotation/VSP_043305
http://togogenome.org/gene/9606:UBXN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RJ36|||http://purl.uniprot.org/uniprot/Q14CS0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||SEP|||UBX|||UBX domain-containing protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315228
http://togogenome.org/gene/9606:ARHGAP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43182|||http://purl.uniprot.org/uniprot/Q59HG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1 and isoform 5.|||In isoform 2.|||In isoform 4 and isoform 5.|||Phosphoserine|||Polar residues|||Pro residues|||Rho GTPase-activating protein 6|||Rho-GAP|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056704|||http://purl.uniprot.org/annotation/VAR_024453|||http://purl.uniprot.org/annotation/VSP_001637|||http://purl.uniprot.org/annotation/VSP_001638|||http://purl.uniprot.org/annotation/VSP_001639|||http://purl.uniprot.org/annotation/VSP_001640|||http://purl.uniprot.org/annotation/VSP_001641|||http://purl.uniprot.org/annotation/VSP_001642
http://togogenome.org/gene/9606:PEX5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z480|||http://purl.uniprot.org/uniprot/A0A0S2Z4F3|||http://purl.uniprot.org/uniprot/A0A0S2Z4H1|||http://purl.uniprot.org/uniprot/B4DR50|||http://purl.uniprot.org/uniprot/B4E0T2|||http://purl.uniprot.org/uniprot/P50542                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished interaction with PEX14.|||Abolished interaction with SQSTM1, leading to decreased pexophagy in response to reactive oxygen species (ROS).|||Abolished monoubiquitination by TRIM37, leading to decreased stability.|||Abolished phosphorylation by ATM, leading to impaired monoubiquitination at K-209.|||Amphipathic helix 1 (AH1)|||Amphipathic helix 2 (AH2)|||Amphipathic helix 3 (AH3)|||Amphipathic helix 4 (AH4)|||Decreased interaction with PEX14.|||Disordered|||Does not affect PEX5 recycling.|||Does not affect ability to mediate peroxisomal import of proteins.|||Does not affect monoubiquitination by TRIM37.|||Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In PBD2B; impaired ability to mediate peroxisomal import of proteins containing both a C-terminal PTS1- and PTS2-type targeting signals.|||In PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import.|||In PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import containing a C-terminal PTS1-type targeting signal without affecting import of proteins with a PTS2 targeting signal.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||LVxEF motif|||Mimics phosphorylation, leading to increased pexophagy in response to reactive oxygen species (ROS).|||Peroxisomal targeting signal 1 receptor|||Phosphoserine|||Phosphoserine; by ATM|||Probable disease-associated variant found in a family with congenital cataract; impaired interaction with PEX7; impaired ability to mediate peroxisomal import of proteins containing a C-terminal PTS2-type targeting signal without affecting import of proteins with a PTS1 targeting signal.|||Promotes accumulation at the peroxisomal membrane because of impaired export into the cytosol.|||Promotes accumulation at the peroxisomal membrane because of impaired export into the cytosol. Does not affect monoubiquitination by TRIM37.|||Sensor of redox state|||Strongly reduced interaction with PEX14.|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||WxxxF/Y motif 1|||WxxxF/Y motif 2|||WxxxF/Y motif 3|||WxxxF/Y motif 4|||WxxxF/Y motif 5|||WxxxF/Y motif 6|||WxxxF/Y motif 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106305|||http://purl.uniprot.org/annotation/VAR_007543|||http://purl.uniprot.org/annotation/VAR_031328|||http://purl.uniprot.org/annotation/VAR_087152|||http://purl.uniprot.org/annotation/VAR_087153|||http://purl.uniprot.org/annotation/VSP_021880|||http://purl.uniprot.org/annotation/VSP_024106|||http://purl.uniprot.org/annotation/VSP_043639
http://togogenome.org/gene/9606:ZNF541                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0D2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||ELM2|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Polar residues|||SANT|||Zinc finger protein 541                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197136|||http://purl.uniprot.org/annotation/VAR_035717|||http://purl.uniprot.org/annotation/VAR_054220|||http://purl.uniprot.org/annotation/VAR_054221|||http://purl.uniprot.org/annotation/VAR_054222|||http://purl.uniprot.org/annotation/VSP_016024
http://togogenome.org/gene/9606:LRRC8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384N5V6|||http://purl.uniprot.org/uniprot/Q6P9F7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRC8 pannexin-like TM region|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Volume-regulated anion channel subunit LRRC8B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076245|||http://purl.uniprot.org/annotation/VAR_025275|||http://purl.uniprot.org/annotation/VAR_051126|||http://purl.uniprot.org/annotation/VAR_051127|||http://purl.uniprot.org/annotation/VAR_051128
http://togogenome.org/gene/9606:C18orf63                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68DL7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C18orf63                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348945
http://togogenome.org/gene/9606:LRRC34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHF2|||http://purl.uniprot.org/uniprot/Q8IZ02                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LRR 1|||LRR 2|||Leucine-rich repeat-containing protein 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228669|||http://purl.uniprot.org/annotation/VAR_034086|||http://purl.uniprot.org/annotation/VAR_051115|||http://purl.uniprot.org/annotation/VAR_051116|||http://purl.uniprot.org/annotation/VSP_059511
http://togogenome.org/gene/9606:TAS2R39                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59534                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 39                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082281|||http://purl.uniprot.org/annotation/VAR_053348|||http://purl.uniprot.org/annotation/VAR_053349
http://togogenome.org/gene/9606:SLC2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11166|||http://purl.uniprot.org/uniprot/Q59GX2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes glucose transport.|||Abolishes phosphorylation by PKA, leading to impaired response to TPA.|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with GLUT1 deficiency syndrome.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In EIG12; decreased glucose transport.|||In EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC.|||In EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type.|||In EIG12; unknown pathological significance.|||In EIG12; unknown pathological significance; decreased glucose transport.|||In EIG12; unknown pathological significance; no effect on glucose transport; impaired phosphorylation by PKC.|||In GLUT1DS1 and DYT9.|||In GLUT1DS1 and GLUT1DS2.|||In GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity.|||In GLUT1DS1.|||In GLUT1DS1; 43% of wild-type glucose uptake activity.|||In GLUT1DS1; 44% of wild-type glucose uptake activity.|||In GLUT1DS1; 48% of wild-type glucose uptake activity.|||In GLUT1DS1; 55% of wild-type glucose uptake activity.|||In GLUT1DS1; 75% of wild-type glucose uptake activity.|||In GLUT1DS1; creates a dileucine internalization motif that promotes recruitment of clathrin and mislocalization of the protein to endocytic compartments.|||In GLUT1DS1; impaired phosphorylation by PKC.|||In GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity.|||In GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose.|||In GLUT1DS1; stabilizes the inward-open conformation.|||In GLUT1DS2.|||In GLUT1DS2; accompanied by hemolytic anemia and altered erythrocyte ion concentrations; the mutation decreases glucose transport and causes a cation leak that alteres intracellular concentrations of sodium potassium and calcium.|||In GLUT1DS2; mild phenotype; reduced transporter activity.|||In GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability.|||In SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage.|||Loss of glycosylation site.|||Major facilitator superfamily (MFS) profile|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Phosphoserine|||Phosphoserine; by PKC/PRKCB|||Phosphothreonine|||Solute carrier family 2, facilitated glucose transporter member 1|||Strongly decreases glucose transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050338|||http://purl.uniprot.org/annotation/VAR_013182|||http://purl.uniprot.org/annotation/VAR_013183|||http://purl.uniprot.org/annotation/VAR_013184|||http://purl.uniprot.org/annotation/VAR_013185|||http://purl.uniprot.org/annotation/VAR_013283|||http://purl.uniprot.org/annotation/VAR_013284|||http://purl.uniprot.org/annotation/VAR_013285|||http://purl.uniprot.org/annotation/VAR_013286|||http://purl.uniprot.org/annotation/VAR_054755|||http://purl.uniprot.org/annotation/VAR_054756|||http://purl.uniprot.org/annotation/VAR_054757|||http://purl.uniprot.org/annotation/VAR_054758|||http://purl.uniprot.org/annotation/VAR_054759|||http://purl.uniprot.org/annotation/VAR_054760|||http://purl.uniprot.org/annotation/VAR_054761|||http://purl.uniprot.org/annotation/VAR_054762|||http://purl.uniprot.org/annotation/VAR_054763|||http://purl.uniprot.org/annotation/VAR_054764|||http://purl.uniprot.org/annotation/VAR_065206|||http://purl.uniprot.org/annotation/VAR_065207|||http://purl.uniprot.org/annotation/VAR_065208|||http://purl.uniprot.org/annotation/VAR_065209|||http://purl.uniprot.org/annotation/VAR_065210|||http://purl.uniprot.org/annotation/VAR_065211|||http://purl.uniprot.org/annotation/VAR_065212|||http://purl.uniprot.org/annotation/VAR_065213|||http://purl.uniprot.org/annotation/VAR_065214|||http://purl.uniprot.org/annotation/VAR_065215|||http://purl.uniprot.org/annotation/VAR_065216|||http://purl.uniprot.org/annotation/VAR_065217|||http://purl.uniprot.org/annotation/VAR_065218|||http://purl.uniprot.org/annotation/VAR_065219|||http://purl.uniprot.org/annotation/VAR_065220|||http://purl.uniprot.org/annotation/VAR_065221|||http://purl.uniprot.org/annotation/VAR_065222|||http://purl.uniprot.org/annotation/VAR_065223|||http://purl.uniprot.org/annotation/VAR_065224|||http://purl.uniprot.org/annotation/VAR_065784|||http://purl.uniprot.org/annotation/VAR_069077|||http://purl.uniprot.org/annotation/VAR_069078|||http://purl.uniprot.org/annotation/VAR_069079|||http://purl.uniprot.org/annotation/VAR_069080|||http://purl.uniprot.org/annotation/VAR_076226|||http://purl.uniprot.org/annotation/VAR_076227|||http://purl.uniprot.org/annotation/VAR_076228|||http://purl.uniprot.org/annotation/VAR_076229|||http://purl.uniprot.org/annotation/VAR_076230|||http://purl.uniprot.org/annotation/VAR_076231|||http://purl.uniprot.org/annotation/VAR_076232|||http://purl.uniprot.org/annotation/VAR_076233|||http://purl.uniprot.org/annotation/VAR_076234|||http://purl.uniprot.org/annotation/VAR_076235|||http://purl.uniprot.org/annotation/VAR_076236
http://togogenome.org/gene/9606:TMEM200C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Polar residues|||Pro residues|||Transmembrane protein 200C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348944
http://togogenome.org/gene/9606:MTFP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UDX5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Mitochondrial fission process protein 1|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212411|||http://purl.uniprot.org/annotation/VSP_041425
http://togogenome.org/gene/9606:BOP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14137                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Ribosome biogenesis protein BOP1|||Sufficient for nucleolar localization|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050885|||http://purl.uniprot.org/annotation/VSP_056391
http://togogenome.org/gene/9606:CD93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPY3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C-type lectin|||Complement component C1q receptor|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||Extracellular|||Helical|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017367|||http://purl.uniprot.org/annotation/VAR_013573|||http://purl.uniprot.org/annotation/VAR_036400|||http://purl.uniprot.org/annotation/VAR_050102
http://togogenome.org/gene/9606:CDK11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4VBY6|||http://purl.uniprot.org/uniprot/Q5QPR3|||http://purl.uniprot.org/uniprot/Q9UQ88                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Cyclin-dependent kinase 11A|||Disordered|||In isoform 4.|||In isoform SV1, isoform SV2, isoform SV3 and isoform SV13.|||In isoform SV1.|||In isoform SV12.|||In isoform SV13.|||In isoform SV2 and isoform SV13.|||In isoform SV7.|||Phosphoserine|||Phosphoserine; by CDK7|||Phosphothreonine|||Phosphothreonine; by CDK7|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024315|||http://purl.uniprot.org/annotation/VAR_031716|||http://purl.uniprot.org/annotation/VAR_031717|||http://purl.uniprot.org/annotation/VAR_060152|||http://purl.uniprot.org/annotation/VAR_060153|||http://purl.uniprot.org/annotation/VAR_062200|||http://purl.uniprot.org/annotation/VSP_008281|||http://purl.uniprot.org/annotation/VSP_008283|||http://purl.uniprot.org/annotation/VSP_008284|||http://purl.uniprot.org/annotation/VSP_008286|||http://purl.uniprot.org/annotation/VSP_008287|||http://purl.uniprot.org/annotation/VSP_008288|||http://purl.uniprot.org/annotation/VSP_008289|||http://purl.uniprot.org/annotation/VSP_008290|||http://purl.uniprot.org/annotation/VSP_008291|||http://purl.uniprot.org/annotation/VSP_008292|||http://purl.uniprot.org/annotation/VSP_018836
http://togogenome.org/gene/9606:RSKR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5H1ZRP1                                                                                  ^@                                                                                  Domain Extent|||Region                                                                                  ^@                                                                                  Domain Extent                                                                                  ^@                                                                                  Protein kinase                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:STIMATE-MUSTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MSY1                                                                                  ^@                                                                                  Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ARHGAP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42331|||http://purl.uniprot.org/uniprot/V9HWC8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2, isoform 3 and isoform 6.|||In isoform 2, isoform 4 and isoform 6.|||In isoform 2.|||In isoform 5.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 25|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056716|||http://purl.uniprot.org/annotation/VAR_049142|||http://purl.uniprot.org/annotation/VAR_049143|||http://purl.uniprot.org/annotation/VAR_049144|||http://purl.uniprot.org/annotation/VSP_010275|||http://purl.uniprot.org/annotation/VSP_010276|||http://purl.uniprot.org/annotation/VSP_037345|||http://purl.uniprot.org/annotation/VSP_045391
http://togogenome.org/gene/9606:H3C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:DCLRE1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TLX1|||http://purl.uniprot.org/uniprot/B3KMX5|||http://purl.uniprot.org/uniprot/Q96SD1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination.|||DNA repair metallo-beta-lactamase|||Disordered|||In Omenn syndrome.|||In RSSCID.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Metallo-beta-lactamase|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Protein artemis|||Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-561.|||Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-562.|||Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-561 and A-562.|||Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-553; A-561 and A-562.|||Reduced IR induced phosphorylation; when associated with A-516; A-534; A-548; A-553; A-561 and A-562.|||Reduced IR induced phosphorylation; when associated with A-516; A-538; A-548; A-553; A-561 and A-562.|||Reduced IR induced phosphorylation; when associated with A-534; A-538; A-548; A-553; A-561 and A-562.|||Reduces PRKDC-dependent endonuclease activity, although V(D)J recombination is largely normal.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209122|||http://purl.uniprot.org/annotation/VAR_023077|||http://purl.uniprot.org/annotation/VAR_023078|||http://purl.uniprot.org/annotation/VAR_023079|||http://purl.uniprot.org/annotation/VAR_048892|||http://purl.uniprot.org/annotation/VAR_048893|||http://purl.uniprot.org/annotation/VAR_048894|||http://purl.uniprot.org/annotation/VAR_060689|||http://purl.uniprot.org/annotation/VAR_060690|||http://purl.uniprot.org/annotation/VAR_060691|||http://purl.uniprot.org/annotation/VSP_014888|||http://purl.uniprot.org/annotation/VSP_014889|||http://purl.uniprot.org/annotation/VSP_014890|||http://purl.uniprot.org/annotation/VSP_014891|||http://purl.uniprot.org/annotation/VSP_014892
http://togogenome.org/gene/9606:FSTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95633                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Follistatin-like 1|||Follistatin-like 2|||Follistatin-related protein 3|||In isoform 2.|||Kazal-like 1|||Kazal-like 2|||N-linked (GlcNAc...) asparagine|||Nuclear localization.|||Phosphoserine; by FAM20C|||TB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010115|||http://purl.uniprot.org/annotation/VSP_038553
http://togogenome.org/gene/9606:PRSS21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6M0                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Charge relay system|||GPI-anchor amidated serine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Removed in mature form|||Testisin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027849|||http://purl.uniprot.org/annotation/PRO_0000027850|||http://purl.uniprot.org/annotation/PRO_0000027851|||http://purl.uniprot.org/annotation/VAR_051840|||http://purl.uniprot.org/annotation/VSP_005389|||http://purl.uniprot.org/annotation/VSP_005390
http://togogenome.org/gene/9606:ABCC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15438|||http://purl.uniprot.org/uniprot/Q86VN9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 3|||Cytoplasmic|||Disordered|||Does not affect subcellular localizattion; does not affect the transport of monoglucuronosyl bilirubin, bisglucuronosyl bilirubin, leukotriene C4, dehydroepiandrosterone-3-sulfate and 17-beta-glucuronosyl oestradiol.|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=16|||Helical; Name=17|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093360|||http://purl.uniprot.org/annotation/VAR_020235|||http://purl.uniprot.org/annotation/VAR_020237|||http://purl.uniprot.org/annotation/VAR_020239|||http://purl.uniprot.org/annotation/VAR_020240|||http://purl.uniprot.org/annotation/VAR_029119|||http://purl.uniprot.org/annotation/VAR_029120|||http://purl.uniprot.org/annotation/VAR_084161|||http://purl.uniprot.org/annotation/VSP_000040|||http://purl.uniprot.org/annotation/VSP_000041|||http://purl.uniprot.org/annotation/VSP_000042|||http://purl.uniprot.org/annotation/VSP_039041|||http://purl.uniprot.org/annotation/VSP_039042|||http://purl.uniprot.org/annotation/VSP_043864
http://togogenome.org/gene/9606:HGSNAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q68CP4|||http://purl.uniprot.org/uniprot/Q8IVU6                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.|||Cytoplasmic|||Disordered|||Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208.|||Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209.|||Helical|||Heparan-alpha-glucosaminide N-acetyltransferase|||In MPS3C.|||In MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity.|||In MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum.|||In MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage.|||In MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity.|||In MPS3C; shows practically no enzyme activity.|||In RP73 and MPS3C; unknown pathological significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity.|||In RP73.|||In isoform 2.|||Likely benign variant; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme.|||Likely benign variant; no loss of enzymatic activity.|||Loss of enzymatic activity, but correctly targeted and processed.|||Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum.|||Loss of intralysosomal proteolytic cleavage and enzymatic activity.|||Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane.|||Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation.|||Lumenal, vesicle|||Lysosomal targeting region|||N-linked (GlcNAc...) asparagine|||No loss of enzymatic activity.|||No loss of intralysosomal proteolytic cleavage and enzymatic activity.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273153|||http://purl.uniprot.org/annotation/PRO_5004308663|||http://purl.uniprot.org/annotation/VAR_030083|||http://purl.uniprot.org/annotation/VAR_030084|||http://purl.uniprot.org/annotation/VAR_030085|||http://purl.uniprot.org/annotation/VAR_030086|||http://purl.uniprot.org/annotation/VAR_030087|||http://purl.uniprot.org/annotation/VAR_030088|||http://purl.uniprot.org/annotation/VAR_030089|||http://purl.uniprot.org/annotation/VAR_030090|||http://purl.uniprot.org/annotation/VAR_063983|||http://purl.uniprot.org/annotation/VAR_063984|||http://purl.uniprot.org/annotation/VAR_063985|||http://purl.uniprot.org/annotation/VAR_063986|||http://purl.uniprot.org/annotation/VAR_063987|||http://purl.uniprot.org/annotation/VAR_063988|||http://purl.uniprot.org/annotation/VAR_063989|||http://purl.uniprot.org/annotation/VAR_063990|||http://purl.uniprot.org/annotation/VAR_063991|||http://purl.uniprot.org/annotation/VAR_063992|||http://purl.uniprot.org/annotation/VAR_063993|||http://purl.uniprot.org/annotation/VAR_063994|||http://purl.uniprot.org/annotation/VAR_063995|||http://purl.uniprot.org/annotation/VAR_063996|||http://purl.uniprot.org/annotation/VAR_063997|||http://purl.uniprot.org/annotation/VAR_075812|||http://purl.uniprot.org/annotation/VAR_075813|||http://purl.uniprot.org/annotation/VAR_075814|||http://purl.uniprot.org/annotation/VAR_075815|||http://purl.uniprot.org/annotation/VAR_075816|||http://purl.uniprot.org/annotation/VAR_075817|||http://purl.uniprot.org/annotation/VSP_040504
http://togogenome.org/gene/9606:GTF3C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Q9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||General transcription factor 3C polypeptide 3|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||TPR 1|||TPR 10|||TPR 11|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106363|||http://purl.uniprot.org/annotation/VAR_061902|||http://purl.uniprot.org/annotation/VSP_010353|||http://purl.uniprot.org/annotation/VSP_010354
http://togogenome.org/gene/9606:PLET1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UQ28                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||N-linked (GlcNAc...) asparagine|||Placenta-expressed transcript 1 protein|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320952|||http://purl.uniprot.org/annotation/PRO_0000424667|||http://purl.uniprot.org/annotation/VAR_039321
http://togogenome.org/gene/9606:TBC1D12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60347                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000208037
http://togogenome.org/gene/9606:RMND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXU0|||http://purl.uniprot.org/uniprot/Q9NWS8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  DUF155|||In COXPD11; alters homooligomeric formation of the protein; decreases the levels of mitochondrial protein synthesis.|||In isoform 2.|||In isoform 3.|||Mitochondrion|||Required for meiotic nuclear division protein 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229732|||http://purl.uniprot.org/annotation/VAR_025754|||http://purl.uniprot.org/annotation/VAR_051864|||http://purl.uniprot.org/annotation/VAR_051865|||http://purl.uniprot.org/annotation/VAR_069036|||http://purl.uniprot.org/annotation/VSP_017735|||http://purl.uniprot.org/annotation/VSP_017738|||http://purl.uniprot.org/annotation/VSP_017739
http://togogenome.org/gene/9606:XRCC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCY5|||http://purl.uniprot.org/uniprot/P18887|||http://purl.uniprot.org/uniprot/Q59HH7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to poly-ADP-ribose and ability to inhibit PARP1 activity; when associated with A-335.|||Abolished binding to poly-ADP-ribose and ability to inhibit PARP1 activity; when associated with A-369.|||BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||DNA repair protein XRCC1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In SCAR26.|||In SCAR26; may result in aberrant splicing.|||In a colorectal cancer sample; somatic mutation.|||Phosphoserine|||Phosphoserine; by PRKDC|||Phosphothreonine|||Polar residues|||Pro residues|||Reduced binding to poly-ADP-ribose nuclear foci.|||Strongly reduced binding to poly-ADP-ribose nuclear foci.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066044|||http://purl.uniprot.org/annotation/VAR_011487|||http://purl.uniprot.org/annotation/VAR_013400|||http://purl.uniprot.org/annotation/VAR_013401|||http://purl.uniprot.org/annotation/VAR_014773|||http://purl.uniprot.org/annotation/VAR_014774|||http://purl.uniprot.org/annotation/VAR_014775|||http://purl.uniprot.org/annotation/VAR_014776|||http://purl.uniprot.org/annotation/VAR_014777|||http://purl.uniprot.org/annotation/VAR_014778|||http://purl.uniprot.org/annotation/VAR_014779|||http://purl.uniprot.org/annotation/VAR_014780|||http://purl.uniprot.org/annotation/VAR_014781|||http://purl.uniprot.org/annotation/VAR_014782|||http://purl.uniprot.org/annotation/VAR_016168|||http://purl.uniprot.org/annotation/VAR_016169|||http://purl.uniprot.org/annotation/VAR_018775|||http://purl.uniprot.org/annotation/VAR_029228|||http://purl.uniprot.org/annotation/VAR_036277|||http://purl.uniprot.org/annotation/VAR_061727|||http://purl.uniprot.org/annotation/VAR_079140|||http://purl.uniprot.org/annotation/VAR_079141
http://togogenome.org/gene/9606:ENTPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y227                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Ectonucleoside triphosphate diphosphohydrolase 4|||Found in a renal cell carcinoma case; somatic mutation.|||Helical|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209911|||http://purl.uniprot.org/annotation/VAR_020444|||http://purl.uniprot.org/annotation/VAR_064711|||http://purl.uniprot.org/annotation/VSP_003614
http://togogenome.org/gene/9606:ZNF671                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1N1|||http://purl.uniprot.org/uniprot/Q8TAW3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 671                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233990|||http://purl.uniprot.org/annotation/VAR_026151|||http://purl.uniprot.org/annotation/VAR_055240
http://togogenome.org/gene/9606:CAVIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5BKX8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Caveolae-associated protein 4|||Disordered|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325763
http://togogenome.org/gene/9606:TANC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCD6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Found in a patient with isolated coloboma; unknown pathological significance.|||In IDDALDS.|||In IDDALDS; reduced interaction with KIF1A; impaired neuronal dense core vesicles transport; no effect on dendritic spine location.|||In IDDALDS; strongly reduced interaction with KIF1A; strongly reduced localization at the dendritic spine.|||In IDDALDS; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pro residues|||Protein TANC2|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000333811|||http://purl.uniprot.org/annotation/VAR_069374|||http://purl.uniprot.org/annotation/VAR_079853|||http://purl.uniprot.org/annotation/VAR_084328|||http://purl.uniprot.org/annotation/VAR_084329|||http://purl.uniprot.org/annotation/VAR_084330|||http://purl.uniprot.org/annotation/VAR_084331|||http://purl.uniprot.org/annotation/VAR_084332|||http://purl.uniprot.org/annotation/VAR_084333|||http://purl.uniprot.org/annotation/VAR_084334|||http://purl.uniprot.org/annotation/VSP_033546|||http://purl.uniprot.org/annotation/VSP_033547|||http://purl.uniprot.org/annotation/VSP_033548|||http://purl.uniprot.org/annotation/VSP_033549|||http://purl.uniprot.org/annotation/VSP_033550
http://togogenome.org/gene/9606:MUCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DR8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  1|||2|||3|||3 X 8 AA tandem repeat of T-T-A-A-[APS]-T-T-A|||Disordered|||Mucin-like protein 1|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228159|||http://purl.uniprot.org/annotation/VAR_025700
http://togogenome.org/gene/9606:PUS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRB2|||http://purl.uniprot.org/uniprot/B3KY42|||http://purl.uniprot.org/uniprot/Q96PZ0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In IDDABS.|||In IDDABS; decreased pseudouridylate synthase activity.|||In IDDABS; unknown pathological significance.|||In IDDABS; unknown pathological significance; mild phenotype; decreased pseudouridylate synthase activity.|||In isoform 2.|||Loss of pseudouridylate synthase activity.|||N-acetylmethionine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Pseudouridylate synthase 7 homolog|||TRUD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152558|||http://purl.uniprot.org/annotation/VAR_082041|||http://purl.uniprot.org/annotation/VAR_082042|||http://purl.uniprot.org/annotation/VAR_086160|||http://purl.uniprot.org/annotation/VAR_086161|||http://purl.uniprot.org/annotation/VSP_059620
http://togogenome.org/gene/9606:DCDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6ZDN3|||http://purl.uniprot.org/uniprot/M0R2J8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||Doublecortin domain-containing protein 1|||In isoform 2.|||In isoform 3.|||Polar residues|||Ricin B-type lectin 1|||Ricin B-type lectin 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000446088|||http://purl.uniprot.org/annotation/VAR_033767|||http://purl.uniprot.org/annotation/VAR_037284|||http://purl.uniprot.org/annotation/VSP_060022|||http://purl.uniprot.org/annotation/VSP_060023|||http://purl.uniprot.org/annotation/VSP_060024|||http://purl.uniprot.org/annotation/VSP_060025
http://togogenome.org/gene/9606:OR1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30953                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1E1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150425|||http://purl.uniprot.org/annotation/VAR_010226|||http://purl.uniprot.org/annotation/VAR_053119|||http://purl.uniprot.org/annotation/VAR_053120
http://togogenome.org/gene/9606:KPNA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A9QM74                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ARM 1|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||IBB|||Importin subunit alpha-8|||In OZEMA17; unknown pathological significance; decreased function in protein import into nucleus; decreased interaction with RSL1D1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326082|||http://purl.uniprot.org/annotation/VAR_088429|||http://purl.uniprot.org/annotation/VAR_088430|||http://purl.uniprot.org/annotation/VAR_088431|||http://purl.uniprot.org/annotation/VAR_088432
http://togogenome.org/gene/9606:NME7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5B8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  DM10|||In isoform 2.|||Nucleoside diphosphate kinase 7|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137130|||http://purl.uniprot.org/annotation/VSP_040996
http://togogenome.org/gene/9606:ZSCAN16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DFB7|||http://purl.uniprot.org/uniprot/Q9H4T2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In a colorectal cancer sample; somatic mutation.|||SCAN box|||Zinc finger and SCAN domain-containing protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047583|||http://purl.uniprot.org/annotation/VAR_035604
http://togogenome.org/gene/9606:NBPF20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPF2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Neuroblastoma breakpoint family member 20|||Olduvai 1|||Olduvai 10|||Olduvai 11|||Olduvai 12|||Olduvai 13|||Olduvai 14|||Olduvai 15|||Olduvai 16|||Olduvai 17|||Olduvai 18|||Olduvai 19|||Olduvai 2|||Olduvai 20|||Olduvai 21|||Olduvai 22|||Olduvai 23|||Olduvai 24|||Olduvai 25|||Olduvai 26|||Olduvai 27|||Olduvai 28|||Olduvai 29|||Olduvai 3|||Olduvai 30|||Olduvai 31|||Olduvai 32|||Olduvai 33|||Olduvai 34|||Olduvai 35|||Olduvai 36|||Olduvai 37|||Olduvai 38|||Olduvai 39|||Olduvai 4|||Olduvai 40|||Olduvai 41|||Olduvai 42|||Olduvai 43|||Olduvai 44|||Olduvai 45|||Olduvai 46|||Olduvai 47|||Olduvai 48|||Olduvai 49|||Olduvai 5|||Olduvai 50|||Olduvai 51|||Olduvai 52|||Olduvai 53|||Olduvai 54|||Olduvai 55|||Olduvai 56|||Olduvai 57|||Olduvai 58|||Olduvai 59|||Olduvai 6|||Olduvai 60|||Olduvai 61|||Olduvai 62|||Olduvai 63|||Olduvai 64|||Olduvai 7|||Olduvai 8|||Olduvai 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288051
http://togogenome.org/gene/9606:ARL10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PCE2|||http://purl.uniprot.org/uniprot/Q8N8L6                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Transmembrane                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 10|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207476
http://togogenome.org/gene/9606:KCNJ14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UNX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||INTRAMEM|||Modified Residue|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 14|||Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||Pore-forming|||S-nitrosocysteine|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154968|||http://purl.uniprot.org/annotation/VAR_034019
http://togogenome.org/gene/9606:PGGT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53609                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Geranylgeranyl transferase type-1 subunit beta|||In isoform 2.|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119769|||http://purl.uniprot.org/annotation/VAR_034381|||http://purl.uniprot.org/annotation/VSP_021827
http://togogenome.org/gene/9606:MAPK6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16659                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FRIEDE motif|||Mitogen-activated protein kinase 6|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||Phosphoserine|||Phosphoserine; by PAK1, PAK2 and PAK3|||Protein kinase|||Proton acceptor|||SEG motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186257|||http://purl.uniprot.org/annotation/VAR_042256
http://togogenome.org/gene/9606:SH3BGRL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H299                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Glutaredoxin|||N-acetylserine|||O-linked (GalNAc...) threonine|||Removed|||SH3 domain-binding glutamic acid-rich-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220749
http://togogenome.org/gene/9606:S100A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06702                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Blocked amino end (Thr)|||Disordered|||Disrupts interaction with NOS2 and inhibits LDL(ox)-induced GAPDHS-nitrosylation; no effect on interaction with S100A8.|||EF-hand 1|||EF-hand 2|||Loss of antifungal activity.|||Loss of resistance to bacterial invasion; when associated with Q-36.|||Loss of resistance to bacterial invasion; when associated with Q-78.|||No effect on antifungal activity.|||Phosphothreonine; by MAPK14|||Pros-methylhistidine|||Protein S100-A9|||S-nitrosocysteine; transient                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143997|||http://purl.uniprot.org/annotation/VAR_013008
http://togogenome.org/gene/9606:TP53TG3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 3.|||TP53-target gene 3 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328983|||http://purl.uniprot.org/annotation/VSP_060197|||http://purl.uniprot.org/annotation/VSP_060198|||http://purl.uniprot.org/annotation/VSP_060199
http://togogenome.org/gene/9606:AFG3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TA92|||http://purl.uniprot.org/uniprot/Q9Y4W6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  AAA+ ATPase|||AFG3-like protein 2|||Basic and acidic residues|||Disordered|||Helical|||In OPA12 and SPAX5; decreased proteolytic function.|||In OPA12.|||In OPA12; decreased proteolytic function resulting in impaired autocatalytic processing and impaired proteolytic maturation of SPG7; does not affect the interaction with SPG7.|||In OPA12; decreased proteolytic function.|||In OPA12; loss-of-function variant resulting in aberrant OPA1 processing and mitochondrial fragmentation.|||In OPA12; unknown pathological significance.|||In OPA12; unknown pathological significance; decreased proteolytic function.|||In SCA28.|||In SCA28; impaired function shown in a yeast complementation assay.|||In SCA28; unknown pathological significance.|||In SPAX5; hypomorphic mutation; results in impaired oligomerization with itself and SPG7; retains ATPase and proteolytic activities.|||In SPAX5; impaired function shown in a yeast complementation assay.|||In SPAX5; unknown pathological significance.|||Loss of autocatalytic processing. Impaired proteolytic maturation of SPG7.|||Mitochondrion|||N6-succinyllysine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000442311|||http://purl.uniprot.org/annotation/PRO_0000442312|||http://purl.uniprot.org/annotation/VAR_063544|||http://purl.uniprot.org/annotation/VAR_063545|||http://purl.uniprot.org/annotation/VAR_063546|||http://purl.uniprot.org/annotation/VAR_063547|||http://purl.uniprot.org/annotation/VAR_064402|||http://purl.uniprot.org/annotation/VAR_064403|||http://purl.uniprot.org/annotation/VAR_064404|||http://purl.uniprot.org/annotation/VAR_064405|||http://purl.uniprot.org/annotation/VAR_064406|||http://purl.uniprot.org/annotation/VAR_064407|||http://purl.uniprot.org/annotation/VAR_064408|||http://purl.uniprot.org/annotation/VAR_067330|||http://purl.uniprot.org/annotation/VAR_075198|||http://purl.uniprot.org/annotation/VAR_075199|||http://purl.uniprot.org/annotation/VAR_080736|||http://purl.uniprot.org/annotation/VAR_084603|||http://purl.uniprot.org/annotation/VAR_084604|||http://purl.uniprot.org/annotation/VAR_084605|||http://purl.uniprot.org/annotation/VAR_084606|||http://purl.uniprot.org/annotation/VAR_084607|||http://purl.uniprot.org/annotation/VAR_084608|||http://purl.uniprot.org/annotation/VAR_084609|||http://purl.uniprot.org/annotation/VAR_084610|||http://purl.uniprot.org/annotation/VAR_084611|||http://purl.uniprot.org/annotation/VAR_084612|||http://purl.uniprot.org/annotation/VAR_084613|||http://purl.uniprot.org/annotation/VAR_084614|||http://purl.uniprot.org/annotation/VAR_084615|||http://purl.uniprot.org/annotation/VAR_084616|||http://purl.uniprot.org/annotation/VAR_084617|||http://purl.uniprot.org/annotation/VAR_084618|||http://purl.uniprot.org/annotation/VAR_084619
http://togogenome.org/gene/9606:SEC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MWR8|||http://purl.uniprot.org/uniprot/P55735                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylvaline|||Phosphoserine|||Protein SEC13 homolog|||Removed|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051203|||http://purl.uniprot.org/annotation/VAR_053413|||http://purl.uniprot.org/annotation/VSP_046191|||http://purl.uniprot.org/annotation/VSP_054695|||http://purl.uniprot.org/annotation/VSP_058966
http://togogenome.org/gene/9606:C21orf91                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYK6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Protein EURL homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087077|||http://purl.uniprot.org/annotation/VAR_011631|||http://purl.uniprot.org/annotation/VAR_011632|||http://purl.uniprot.org/annotation/VAR_054506|||http://purl.uniprot.org/annotation/VAR_054507|||http://purl.uniprot.org/annotation/VAR_054508|||http://purl.uniprot.org/annotation/VSP_036451|||http://purl.uniprot.org/annotation/VSP_036452
http://togogenome.org/gene/9606:MASTL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GX5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Disordered|||Found in a large family with autosomal dominant thrombocytopenia; unknown pathological significance; no effect on nuclear localization.|||Hyperactive form.|||In isoform 2 and isoform 3.|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase greatwall                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086315|||http://purl.uniprot.org/annotation/VAR_022838|||http://purl.uniprot.org/annotation/VAR_022839|||http://purl.uniprot.org/annotation/VAR_040792|||http://purl.uniprot.org/annotation/VAR_040793|||http://purl.uniprot.org/annotation/VAR_057103|||http://purl.uniprot.org/annotation/VSP_014574|||http://purl.uniprot.org/annotation/VSP_014575
http://togogenome.org/gene/9606:GOPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HD26                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with MARCHF2.|||Breakpoint for translocation to form GOPC-ROS1 fusion protein|||Disordered|||Golgi-associated PDZ and coiled-coil motif-containing protein|||In isoform 2.|||In isoform 3.|||N-acetylserine|||No effect on subcellular location; when associated with V-175; V-182 and V-189.|||No effect on subcellular location; when associated with V-175; V-182 and V-196.|||No effect on subcellular location; when associated with V-175; V-189 and V-196.|||No effect on subcellular location; when associated with V-182; V-189 and V-196.|||PDZ|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087542|||http://purl.uniprot.org/annotation/VSP_016062|||http://purl.uniprot.org/annotation/VSP_016063|||http://purl.uniprot.org/annotation/VSP_016064
http://togogenome.org/gene/9606:C1orf35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU76                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Multiple myeloma tumor-associated protein 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096518|||http://purl.uniprot.org/annotation/VSP_015129|||http://purl.uniprot.org/annotation/VSP_015130|||http://purl.uniprot.org/annotation/VSP_015131|||http://purl.uniprot.org/annotation/VSP_015132|||http://purl.uniprot.org/annotation/VSP_015133|||http://purl.uniprot.org/annotation/VSP_015134
http://togogenome.org/gene/9606:CAVIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95810                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Caveolae-associated protein 2|||Disordered|||Interaction with CAVIN1|||Leucine-zipper|||Loss of localization in caveolae; when associated with E-86 or E-100.|||Loss of localization in caveolae; when associated with E-86 or E-93.|||Loss of localization in caveolae; when associated with E-93 or E-100.|||N-acetylglycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238918|||http://purl.uniprot.org/annotation/VAR_034422
http://togogenome.org/gene/9606:HNF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGS8|||http://purl.uniprot.org/uniprot/E0YMJ6|||http://purl.uniprot.org/uniprot/P35680|||http://purl.uniprot.org/uniprot/Q6FHW6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dimerization|||Disordered|||HNF-p1|||Hepatocyte nuclear factor 1-beta|||Homeobox|||Homeobox; HNF1-type|||In RCAD.|||In RCAD; gain-of-function mutation.|||In RCAD; has diminished transcriptional activity by loss of DNA binding activity.|||In RCAD; insignificant differences in transactivation ability between wild-type and mutated HNF1B.|||In RCAD; no impact on interaction with PCBD1; reduced coactivation by PCBD1.|||In RCAD; unknown pathological significance.|||In T2D; 22% reduction in activity.|||In diabetes; early onset association; unknown pathological significance.|||In isoform 4.|||In isoform B and isoform 4.|||In isoform C.|||Loss of interaction with PCBD1. Loss of PCBD1 recruitment to the nucleus.|||No impact on interaction with PCBD1. Reduced PCBD1 recruitment to the nucleus. Reduced coactivation by PCBD1.|||POU-specific atypical|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049121|||http://purl.uniprot.org/annotation/VAR_012058|||http://purl.uniprot.org/annotation/VAR_017665|||http://purl.uniprot.org/annotation/VAR_046012|||http://purl.uniprot.org/annotation/VAR_046013|||http://purl.uniprot.org/annotation/VAR_046014|||http://purl.uniprot.org/annotation/VAR_046015|||http://purl.uniprot.org/annotation/VAR_046016|||http://purl.uniprot.org/annotation/VAR_046017|||http://purl.uniprot.org/annotation/VAR_046018|||http://purl.uniprot.org/annotation/VAR_046019|||http://purl.uniprot.org/annotation/VAR_046020|||http://purl.uniprot.org/annotation/VAR_046021|||http://purl.uniprot.org/annotation/VAR_046022|||http://purl.uniprot.org/annotation/VAR_046023|||http://purl.uniprot.org/annotation/VAR_046024|||http://purl.uniprot.org/annotation/VAR_046025|||http://purl.uniprot.org/annotation/VAR_046026|||http://purl.uniprot.org/annotation/VAR_046027|||http://purl.uniprot.org/annotation/VAR_046028|||http://purl.uniprot.org/annotation/VAR_046029|||http://purl.uniprot.org/annotation/VAR_046030|||http://purl.uniprot.org/annotation/VAR_046031|||http://purl.uniprot.org/annotation/VAR_046032|||http://purl.uniprot.org/annotation/VAR_046033|||http://purl.uniprot.org/annotation/VAR_046034|||http://purl.uniprot.org/annotation/VSP_002254|||http://purl.uniprot.org/annotation/VSP_002255|||http://purl.uniprot.org/annotation/VSP_002256|||http://purl.uniprot.org/annotation/VSP_053327|||http://purl.uniprot.org/annotation/VSP_053328|||http://purl.uniprot.org/annotation/VSP_053329
http://togogenome.org/gene/9606:DMAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Distal membrane-arm assembly complex protein 1|||Helical|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089729|||http://purl.uniprot.org/annotation/VAR_056819|||http://purl.uniprot.org/annotation/VSP_014455
http://togogenome.org/gene/9606:VMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DED7|||http://purl.uniprot.org/uniprot/B4DEJ9|||http://purl.uniprot.org/uniprot/B4DGZ7|||http://purl.uniprot.org/uniprot/Q96GC9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreases interaction with ATP2A2.|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-acetylalanine|||Removed|||VTT domain|||Vacuole membrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284546|||http://purl.uniprot.org/annotation/VSP_056106
http://togogenome.org/gene/9606:EVA1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8M9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Necessary for the localization and biological activity|||Phosphoserine; by FAM20C|||Phosphothreonine|||Protein eva-1 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278671|||http://purl.uniprot.org/annotation/VAR_054077
http://togogenome.org/gene/9606:ATP6V0A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53ET5|||http://purl.uniprot.org/uniprot/Q53X12|||http://purl.uniprot.org/uniprot/Q5CZH6|||http://purl.uniprot.org/uniprot/Q93050                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In DEE104.|||In DEE104; impaired acidification of endolysosomal compartments; when tested in transgenic mice, homozygosity leads to embryonic death at 5 to 6 dpc.|||In DEE104; unknown pathological significance.|||In NEDEBA; impaired acidification of endolysosomal compartments; when tested in transgenic mice, homozygosity leads to body weights lower than in wild-type animals, impaired motor function, defects in the neuronal development and synapse formation and eventually death at about 2 weeks of age.|||In NEDEBA; unknown pathological significance.|||In NEDEBA; unknown pathological significance; impaired acidification of endolysosomal compartments.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GalNAc...) asparagine|||Phosphothreonine|||Phosphotyrosine|||V-type proton ATPase 116 kDa subunit a 1|||Vacuolar                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119211|||http://purl.uniprot.org/annotation/VAR_087489|||http://purl.uniprot.org/annotation/VAR_087490|||http://purl.uniprot.org/annotation/VAR_087491|||http://purl.uniprot.org/annotation/VAR_087492|||http://purl.uniprot.org/annotation/VAR_087493|||http://purl.uniprot.org/annotation/VAR_087494|||http://purl.uniprot.org/annotation/VAR_087495|||http://purl.uniprot.org/annotation/VSP_012814|||http://purl.uniprot.org/annotation/VSP_043532
http://togogenome.org/gene/9606:NAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96HR8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H/ACA ribonucleoprotein complex non-core subunit NAF1|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315637|||http://purl.uniprot.org/annotation/VAR_057795|||http://purl.uniprot.org/annotation/VAR_063101|||http://purl.uniprot.org/annotation/VSP_046217|||http://purl.uniprot.org/annotation/VSP_046218
http://togogenome.org/gene/9606:HTR1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5W4|||http://purl.uniprot.org/uniprot/P08908|||http://purl.uniprot.org/uniprot/Q5ZGX3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 1A|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068903|||http://purl.uniprot.org/annotation/VAR_003446|||http://purl.uniprot.org/annotation/VAR_011826|||http://purl.uniprot.org/annotation/VAR_011827|||http://purl.uniprot.org/annotation/VAR_011828|||http://purl.uniprot.org/annotation/VAR_011829|||http://purl.uniprot.org/annotation/VAR_011830
http://togogenome.org/gene/9606:GSK3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49840                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Glycogen synthase kinase-3 alpha|||N-acetylserine|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085978|||http://purl.uniprot.org/annotation/VAR_040539|||http://purl.uniprot.org/annotation/VAR_051625
http://togogenome.org/gene/9606:ZMYM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95789                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||MYM-type 1|||MYM-type 2|||MYM-type 3|||MYM-type 4|||MYM-type 5|||MYM-type 6|||MYM-type 7|||MYM-type 8|||Phosphoserine|||Polar residues|||Zinc finger MYM-type protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191381|||http://purl.uniprot.org/annotation/VAR_044432|||http://purl.uniprot.org/annotation/VAR_044433|||http://purl.uniprot.org/annotation/VSP_011446|||http://purl.uniprot.org/annotation/VSP_011447|||http://purl.uniprot.org/annotation/VSP_034680|||http://purl.uniprot.org/annotation/VSP_034681|||http://purl.uniprot.org/annotation/VSP_034682|||http://purl.uniprot.org/annotation/VSP_034683|||http://purl.uniprot.org/annotation/VSP_035287|||http://purl.uniprot.org/annotation/VSP_035288
http://togogenome.org/gene/9606:FZD7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75084                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Essential for SDCBP-mediated plasma membrane phosphatidylinositol-4,5-bisphosphate recognition|||Extracellular|||FZ|||Frizzled-7|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impaired SDCBP-mediated interaction with phosphatidylinositol-4,5-bisphosphate.|||Lys-Thr-X-X-X-Trp motif, mediates interaction with the PDZ domain of Dvl family members|||N-linked (GlcNAc...) asparagine|||PDZ-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012996|||http://purl.uniprot.org/annotation/VAR_033024|||http://purl.uniprot.org/annotation/VAR_033941|||http://purl.uniprot.org/annotation/VAR_033942|||http://purl.uniprot.org/annotation/VAR_049292
http://togogenome.org/gene/9606:SLC34A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95436                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Breakpoint for translocation to form a SLC34A2-ROS1 fusion protein|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=M1|||Helical; Name=M2|||Helical; Name=M3|||Helical; Name=M4|||Helical; Name=M5|||Helical; Name=M6|||Helical; Name=M7|||Helical; Name=M8|||In PULAM.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Sodium-dependent phosphate transport protein 2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068613|||http://purl.uniprot.org/annotation/VAR_030677|||http://purl.uniprot.org/annotation/VAR_030678|||http://purl.uniprot.org/annotation/VAR_034156|||http://purl.uniprot.org/annotation/VSP_016755
http://togogenome.org/gene/9606:KCTD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WZ19                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CUL3 and induces abnormal actin stress fibers.|||BTB|||BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1|||Disordered|||Found in a patient with schizophrenia; unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191297|||http://purl.uniprot.org/annotation/VAR_080045
http://togogenome.org/gene/9606:PPIF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30405                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Blocks Ca(2+)-induced mPTP opening and reduces hydrogen peroxide-induced cell death.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||PPIase cyclophilin-type|||Peptidyl-prolyl cis-trans isomerase F, mitochondrial|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025489|||http://purl.uniprot.org/annotation/VSP_056286
http://togogenome.org/gene/9606:ABI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B6VEX3|||http://purl.uniprot.org/uniprot/B6VEX4|||http://purl.uniprot.org/uniprot/B6VEX5|||http://purl.uniprot.org/uniprot/Q8IZP0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abl interactor 1|||Breakpoint for translocation to form KMT2A/MLL1-ABI1|||Disordered|||In isoform 10 and isoform 11.|||In isoform 11.|||In isoform 12.|||In isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 2, isoform 3, isoform 4, isoform 8, isoform 10, isoform 11 and isoform 12.|||In isoform 2, isoform 4, isoform 6, isoform 7, isoform 8, isoform 10 and isoform 11.|||In isoform 2, isoform 5 and isoform 10.|||In isoform 7, isoform 8, isoform 10 and isoform 11.|||In isoform 7.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||Removed|||Required for binding to WASF1|||SH3|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191787|||http://purl.uniprot.org/annotation/VAR_048159|||http://purl.uniprot.org/annotation/VSP_010749|||http://purl.uniprot.org/annotation/VSP_010750|||http://purl.uniprot.org/annotation/VSP_010751|||http://purl.uniprot.org/annotation/VSP_010752|||http://purl.uniprot.org/annotation/VSP_010753|||http://purl.uniprot.org/annotation/VSP_010754|||http://purl.uniprot.org/annotation/VSP_010755|||http://purl.uniprot.org/annotation/VSP_043403|||http://purl.uniprot.org/annotation/VSP_044604
http://togogenome.org/gene/9606:RREB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92766                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ras-responsive element-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047326|||http://purl.uniprot.org/annotation/VAR_033197|||http://purl.uniprot.org/annotation/VAR_033198|||http://purl.uniprot.org/annotation/VAR_033199|||http://purl.uniprot.org/annotation/VAR_033200|||http://purl.uniprot.org/annotation/VAR_033201|||http://purl.uniprot.org/annotation/VAR_033202|||http://purl.uniprot.org/annotation/VSP_026704|||http://purl.uniprot.org/annotation/VSP_026705|||http://purl.uniprot.org/annotation/VSP_026706|||http://purl.uniprot.org/annotation/VSP_026707|||http://purl.uniprot.org/annotation/VSP_053538|||http://purl.uniprot.org/annotation/VSP_053539|||http://purl.uniprot.org/annotation/VSP_053540
http://togogenome.org/gene/9606:TUBB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4B7                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  5-glutamyl polyglutamate|||Disordered|||In MACTHC1.|||MREI motif|||Phosphoserine; by CDK1|||Tubulin beta-1 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048242|||http://purl.uniprot.org/annotation/VAR_034542|||http://purl.uniprot.org/annotation/VAR_034543|||http://purl.uniprot.org/annotation/VAR_052671|||http://purl.uniprot.org/annotation/VAR_052672|||http://purl.uniprot.org/annotation/VAR_063411
http://togogenome.org/gene/9606:CT47A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:FAM118B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KP39|||http://purl.uniprot.org/uniprot/Q9BPY3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Protein FAM118B|||Removed|||SIR2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295103
http://togogenome.org/gene/9606:CD200                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDZ6|||http://purl.uniprot.org/uniprot/F8W7G1|||http://purl.uniprot.org/uniprot/P41217                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||Immunoglobulin|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||OX-2 membrane glycoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015124|||http://purl.uniprot.org/annotation/VAR_027605|||http://purl.uniprot.org/annotation/VAR_027606|||http://purl.uniprot.org/annotation/VAR_056110|||http://purl.uniprot.org/annotation/VSP_002613|||http://purl.uniprot.org/annotation/VSP_040027
http://togogenome.org/gene/9606:MIPOL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K735|||http://purl.uniprot.org/uniprot/Q4G0U7|||http://purl.uniprot.org/uniprot/Q8TD10                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Mirror-image polydactyly gene 1 protein|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096490|||http://purl.uniprot.org/annotation/VAR_034095|||http://purl.uniprot.org/annotation/VSP_009460|||http://purl.uniprot.org/annotation/VSP_009461|||http://purl.uniprot.org/annotation/VSP_009462
http://togogenome.org/gene/9606:STAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42224                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosyl glutamic acid; by PARP14|||Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation.|||Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PRKCD-induced apoptosis. Upon IFNB induction, phosphorylated at Y-701 but not at S-708.|||Enhances STAT1 nuclear translocation and interferon (IFN)-stimulated gene (ISG) expression in response to IFN-beta stimulation. Reduces viral load in infected cultured cells.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Impaired phosphorylation at S-727.|||In IMD31A; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27.|||In IMD31A; affects the DNA-binding activity of the protein.|||In IMD31A; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27.|||In IMD31A; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein.|||In IMD31B; disrupts transactivation activity in response to IFNG.|||In IMD31B; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency.|||In IMD31B; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%.|||In IMD31C.|||In IMD31C; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation.|||In IMD31C; gain of function; increases STAT1 phosphorylation due to impaired nuclear dephosphorylation; increases transactivation activity in response to IFNG.|||In IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation.|||In IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation.|||In IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation.|||In IMD31C; gain of function; increases transactivation activity in response to IFNG.|||In a breast cancer sample; somatic mutation.|||In isoform Beta.|||Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-657.|||Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-705.|||N-acetylserine|||N6-methyllysine|||No change in enhancement of MAPK-induced sumoylation.|||No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation.|||No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation.|||No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction.|||Not phosphorylated at S-708 upon IFNB induction.|||Not phosphorylated at Y-701 upon IFNB induction.|||Phosphorylated at Y-701 upon IFNB induction.|||Phosphoserine; by CAMK2 and MAPK14|||Phosphoserine; by IKKE|||Phosphotyrosine; by JAK1, JAK2 or TYK2|||Removed|||Required for recruitment of EP300/p300|||SH2|||Signal transducer and activator of transcription 1-alpha/beta|||Strongly reduced IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. Does not affect ability to homodimerize.|||Sumoylated.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000182410|||http://purl.uniprot.org/annotation/VAR_018265|||http://purl.uniprot.org/annotation/VAR_018266|||http://purl.uniprot.org/annotation/VAR_034521|||http://purl.uniprot.org/annotation/VAR_036001|||http://purl.uniprot.org/annotation/VAR_065815|||http://purl.uniprot.org/annotation/VAR_065816|||http://purl.uniprot.org/annotation/VAR_065817|||http://purl.uniprot.org/annotation/VAR_065934|||http://purl.uniprot.org/annotation/VAR_065935|||http://purl.uniprot.org/annotation/VAR_065936|||http://purl.uniprot.org/annotation/VAR_065937|||http://purl.uniprot.org/annotation/VAR_065938|||http://purl.uniprot.org/annotation/VAR_065939|||http://purl.uniprot.org/annotation/VAR_065940|||http://purl.uniprot.org/annotation/VAR_065941|||http://purl.uniprot.org/annotation/VAR_065942|||http://purl.uniprot.org/annotation/VAR_065943|||http://purl.uniprot.org/annotation/VAR_065944|||http://purl.uniprot.org/annotation/VAR_065945|||http://purl.uniprot.org/annotation/VAR_068713|||http://purl.uniprot.org/annotation/VAR_068714|||http://purl.uniprot.org/annotation/VAR_075494|||http://purl.uniprot.org/annotation/VAR_075495|||http://purl.uniprot.org/annotation/VAR_075496|||http://purl.uniprot.org/annotation/VAR_075497|||http://purl.uniprot.org/annotation/VAR_075498|||http://purl.uniprot.org/annotation/VAR_075499|||http://purl.uniprot.org/annotation/VAR_075500|||http://purl.uniprot.org/annotation/VSP_006282
http://togogenome.org/gene/9606:CCDC150                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ03|||http://purl.uniprot.org/uniprot/Q8NCX0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 150|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328984|||http://purl.uniprot.org/annotation/VAR_042600|||http://purl.uniprot.org/annotation/VSP_032872|||http://purl.uniprot.org/annotation/VSP_032873|||http://purl.uniprot.org/annotation/VSP_032874|||http://purl.uniprot.org/annotation/VSP_032875|||http://purl.uniprot.org/annotation/VSP_032876|||http://purl.uniprot.org/annotation/VSP_032877|||http://purl.uniprot.org/annotation/VSP_032878
http://togogenome.org/gene/9606:PCDHGB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5G3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Protocadherin gamma-B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003972|||http://purl.uniprot.org/annotation/VSP_008684|||http://purl.uniprot.org/annotation/VSP_008685
http://togogenome.org/gene/9606:QNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6V5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  N-acetylmethionine|||Nucleophile or transition state stabilizer|||Queuosine 5'-phosphate N-glycosylase/hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089700
http://togogenome.org/gene/9606:NINJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92982                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by MMP9|||Cytoplasmic|||Disordered|||Does not affect ability to homooligomerize and mediate plasma membrane rupture (cytolysis).|||Does not affect ability to homooligomerize in vitro.|||Does not affect ability to homooligomerize, but shows reduced ability to mediate plasma membrane rupture (cytolysis).|||Extracellular|||Helical; Name=Helix alpha3|||Helical;Name=Helix alpha4|||Helix alpha1|||Helix alpha2|||N-acetylmethionine|||N-linked (GlcNAc...) asparagine|||N-terminal adhesion motif|||Ninjurin-1|||Phosphoserine|||Required to induce plasma membrane rupture|||Secreted ninjurin-1|||Strongly reduced ability to homooligomerize and mediate plasma membrane rupture (cytolysis).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000159643|||http://purl.uniprot.org/annotation/PRO_0000452824|||http://purl.uniprot.org/annotation/VAR_025549
http://togogenome.org/gene/9606:MARVELD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSK0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||MARVEL|||MARVEL domain-containing protein 1|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271522
http://togogenome.org/gene/9606:PLEKHG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFH4|||http://purl.uniprot.org/uniprot/A1L390                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DH|||Disordered|||In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||PH|||Phosphoserine|||Pleckstrin homology domain-containing family G member 3|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306863|||http://purl.uniprot.org/annotation/VAR_035330|||http://purl.uniprot.org/annotation/VAR_061518|||http://purl.uniprot.org/annotation/VSP_028533|||http://purl.uniprot.org/annotation/VSP_028534|||http://purl.uniprot.org/annotation/VSP_041513
http://togogenome.org/gene/9606:TAS2R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082197
http://togogenome.org/gene/9606:CLDN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14493|||http://purl.uniprot.org/uniprot/Q75L80                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes interaction with Clostridium perfringens CPE.|||Claudin-4|||Cytoplasmic|||Decreases interaction with Clostridium perfringens CPE.|||Extracellular|||Helical|||Interaction with EPHA2|||Interactions with TJP1, TJP2 and TJP3|||Loss of phosphorylation by EPHA2.|||No effect on interaction with Clostridium perfringens CPE.|||Phosphotyrosine; by EPHA2|||Strongly decreases interaction with Clostridium perfringens CPE.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144743
http://togogenome.org/gene/9606:ANKRD34B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PLL1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat domain-containing protein 34B|||Disordered|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319102|||http://purl.uniprot.org/annotation/VAR_038952
http://togogenome.org/gene/9606:IP6K3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1M0|||http://purl.uniprot.org/uniprot/Q5TAQ4|||http://purl.uniprot.org/uniprot/Q96PC2                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Inositol hexakisphosphate kinase 3|||Loss of activity.|||Strongly reduces activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066881|||http://purl.uniprot.org/annotation/VAR_031590|||http://purl.uniprot.org/annotation/VAR_031591|||http://purl.uniprot.org/annotation/VAR_031592|||http://purl.uniprot.org/annotation/VAR_031593
http://togogenome.org/gene/9606:RBMY1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7P1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Polar residues|||RNA-binding motif protein, Y chromosome, family 1 member D|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341538|||http://purl.uniprot.org/annotation/VSP_056242
http://togogenome.org/gene/9606:INHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05111                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Cleavage|||Found in a patient with early-onset epithelial ovarian tumor; unknown pathological significance; alters the ratio of secreted activins and ihibins.|||Inhibin alpha N-terminal region|||Inhibin alpha chain|||Interchain|||Loss of cleavage.|||Loss of cleavage; when associated with 55-AA-56.|||Loss of cleavage; when associated with 60-AA-61.|||Loss of glycosylation.|||May play a role in premature ovarian failure.|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033685|||http://purl.uniprot.org/annotation/PRO_0000033686|||http://purl.uniprot.org/annotation/PRO_0000033687|||http://purl.uniprot.org/annotation/VAR_015110|||http://purl.uniprot.org/annotation/VAR_034016|||http://purl.uniprot.org/annotation/VAR_072639
http://togogenome.org/gene/9606:CASTOR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTX7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ACT 1|||ACT 2|||Abolished phosphorylation by AKT1, leading to decreased interaction with RNF167 and subsequent ubiquitination.|||Cytosolic arginine sensor for mTORC1 subunit 1|||Decreased arginine-binding. Constitutively interacts with the GATOR2 complex.|||In 3KR mutant; abolished ubiquitination by RNF167; when associated with R-61 and R-213.|||In 3KR mutant; abolished ubiquitination by RNF167; when associated with R-61 and R-96.|||In 3KR mutant; abolished ubiquitination by RNF167; when associated with R-96 and R-213.|||Loss of arginine-binding. Constitutively inhibits the TORC1 signaling pathway.|||Loss of arginine-binding. Constitutively interacts with the GATOR2 complex.|||Loss of arginine-binding. Constitutively interacts with the GATOR2 complex. Constitutively inhibits the TORC1 signaling pathway.|||Mimics phosphorylation, leading to promote interaction with RNF167 and subsequent ubiquitination.|||No effect on arginine-binding. Loss of homodimerization. Decreased interaction with the GATOR2 complex which constitutively activates the TORC1 signaling pathway.|||No effect on arginine-binding. No effect on homodimerization. Loss of interaction with the GATOR2 complex which constitutively activates the TORC1 signaling pathway.|||No effect on arginine-binding. No effect on homodimerization. Loss of interaction with the GATOR2 complex.|||No effect on interaction with the GATOR2 complex.|||Phosphoserine; by PKB/AKT1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348590
http://togogenome.org/gene/9606:NAGS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NKP2|||http://purl.uniprot.org/uniprot/Q8N159                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  10-fold reduction in catalytic activity.|||15% reduction in catalytic activity.|||7-fold reduction in catalytic activity.|||Amino-acid kinase domain (AAK)|||Disordered|||In NAGSD.|||In NAGSD; markedly decreases activity.|||In NAGSD; unknown pathological significance.|||Mitochondrion|||N-acetylglutamate synthase conserved domain form|||N-acetylglutamate synthase long form|||N-acetylglutamate synthase short form|||N-acetyltransferase|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041930|||http://purl.uniprot.org/annotation/PRO_0000041931|||http://purl.uniprot.org/annotation/PRO_0000041932|||http://purl.uniprot.org/annotation/VAR_023505|||http://purl.uniprot.org/annotation/VAR_023506|||http://purl.uniprot.org/annotation/VAR_023507|||http://purl.uniprot.org/annotation/VAR_023508|||http://purl.uniprot.org/annotation/VAR_023509|||http://purl.uniprot.org/annotation/VAR_023510|||http://purl.uniprot.org/annotation/VAR_077329|||http://purl.uniprot.org/annotation/VAR_077330|||http://purl.uniprot.org/annotation/VAR_077331|||http://purl.uniprot.org/annotation/VAR_077332|||http://purl.uniprot.org/annotation/VAR_077333|||http://purl.uniprot.org/annotation/VAR_077334|||http://purl.uniprot.org/annotation/VAR_077335|||http://purl.uniprot.org/annotation/VAR_077336
http://togogenome.org/gene/9606:SELENOW                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63302                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Non standard residue                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Non standard residue                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec); redox-active|||S-glutathionyl cysteine|||Selenocysteine|||Selenoprotein W                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097678
http://togogenome.org/gene/9606:OR6Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP6|||http://purl.uniprot.org/uniprot/Q8NGQ2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6Q1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150636|||http://purl.uniprot.org/annotation/VAR_057561|||http://purl.uniprot.org/annotation/VAR_064742
http://togogenome.org/gene/9606:LILRA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZH0|||http://purl.uniprot.org/uniprot/Q8N149                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  3'-nitrotyrosine|||Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Leukocyte immunoglobulin-like receptor subfamily A member 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014817|||http://purl.uniprot.org/annotation/PRO_5002726090|||http://purl.uniprot.org/annotation/VAR_016988|||http://purl.uniprot.org/annotation/VAR_016989|||http://purl.uniprot.org/annotation/VAR_056051|||http://purl.uniprot.org/annotation/VAR_056052|||http://purl.uniprot.org/annotation/VAR_056053|||http://purl.uniprot.org/annotation/VSP_008455|||http://purl.uniprot.org/annotation/VSP_057085|||http://purl.uniprot.org/annotation/VSP_057086
http://togogenome.org/gene/9606:PCNX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H6A9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Pecanex-like protein 3|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331529|||http://purl.uniprot.org/annotation/VAR_042889|||http://purl.uniprot.org/annotation/VAR_042890|||http://purl.uniprot.org/annotation/VAR_042891|||http://purl.uniprot.org/annotation/VAR_061500|||http://purl.uniprot.org/annotation/VAR_061501|||http://purl.uniprot.org/annotation/VSP_033242|||http://purl.uniprot.org/annotation/VSP_033243|||http://purl.uniprot.org/annotation/VSP_033244|||http://purl.uniprot.org/annotation/VSP_033245
http://togogenome.org/gene/9606:PCNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine|||PEST proteolytic signal-containing nuclear protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058253|||http://purl.uniprot.org/annotation/VSP_013879|||http://purl.uniprot.org/annotation/VSP_013880|||http://purl.uniprot.org/annotation/VSP_013881
http://togogenome.org/gene/9606:KCMF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0J7                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||E3 ubiquitin-protein ligase KCMF1|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||ZZ-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349219
http://togogenome.org/gene/9606:ATXN3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DYC7|||http://purl.uniprot.org/uniprot/Q9H3M9                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Ataxin-3-like protein|||Basic and acidic residues|||Disordered|||Josephin|||Nucleophile|||Polar residues|||Proton acceptor|||UIM 1|||UIM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271099|||http://purl.uniprot.org/annotation/VAR_029861|||http://purl.uniprot.org/annotation/VAR_029862
http://togogenome.org/gene/9606:SLC7A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52569                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cationic amino acid transporter 2|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054264|||http://purl.uniprot.org/annotation/VAR_030799|||http://purl.uniprot.org/annotation/VAR_030800|||http://purl.uniprot.org/annotation/VAR_030801|||http://purl.uniprot.org/annotation/VAR_058414|||http://purl.uniprot.org/annotation/VSP_023354|||http://purl.uniprot.org/annotation/VSP_037354
http://togogenome.org/gene/9606:AEBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN18                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||C2H2-type 1|||C2H2-type 2; degenerate|||C2H2-type 3|||Disordered|||Important for nucleosome binding activity of the PRC2 complex|||In isoform 2.|||In isoform 3.|||Interaction with RBBP4|||Interaction with SUZ12|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Zinc finger protein AEBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341590|||http://purl.uniprot.org/annotation/VSP_034357|||http://purl.uniprot.org/annotation/VSP_034358|||http://purl.uniprot.org/annotation/VSP_034359
http://togogenome.org/gene/9606:PSMD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75832                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  26S proteasome non-ATPase regulatory subunit 10|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Abolishes interaction with RB1.|||In isoform 2.|||Interaction with RB1|||Interaction with RELA|||Required for nuclear localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067045|||http://purl.uniprot.org/annotation/VSP_043043
http://togogenome.org/gene/9606:GFPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06210                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  For GATase activity|||Glutamine amidotransferase type-2|||Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1|||In CMS12.|||In isoform 2.|||Isomerase|||Phosphoserine|||Removed|||SIS 1|||SIS 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135280|||http://purl.uniprot.org/annotation/VAR_065339|||http://purl.uniprot.org/annotation/VAR_065340|||http://purl.uniprot.org/annotation/VAR_065341|||http://purl.uniprot.org/annotation/VAR_065342|||http://purl.uniprot.org/annotation/VAR_065343|||http://purl.uniprot.org/annotation/VAR_065344|||http://purl.uniprot.org/annotation/VAR_065345|||http://purl.uniprot.org/annotation/VAR_065346|||http://purl.uniprot.org/annotation/VAR_065347|||http://purl.uniprot.org/annotation/VAR_065348|||http://purl.uniprot.org/annotation/VAR_065349|||http://purl.uniprot.org/annotation/VAR_065350|||http://purl.uniprot.org/annotation/VAR_065351|||http://purl.uniprot.org/annotation/VSP_007497
http://togogenome.org/gene/9606:PKIG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q549H9|||http://purl.uniprot.org/uniprot/Q9Y2B9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Site                                                                                  ^@                                                                                  Disordered|||Important for inhibition|||Polar residues|||cAMP-dependent protein kinase inhibitor gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154542
http://togogenome.org/gene/9606:SLCO4C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZQN7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Kazal-like|||Phosphoserine|||Polar residues|||Solute carrier organic anion transporter family member 4C1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337151
http://togogenome.org/gene/9606:UFSP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUQ7                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Catalytically inactive.|||In BFHD; loss of protease activity toward the C-terminal of UFM1.|||In DEE106; decreased function in deUFMylation; reduced UFSP2 abundance and increased abundance of UFMylated targets in homozygous patient-derived fibroblasts.|||In SEMDDR.|||N-acetylmethionine|||Ufm1-specific protease 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280362|||http://purl.uniprot.org/annotation/VAR_031126|||http://purl.uniprot.org/annotation/VAR_074673|||http://purl.uniprot.org/annotation/VAR_079708|||http://purl.uniprot.org/annotation/VAR_087725|||http://purl.uniprot.org/annotation/VAR_087726
http://togogenome.org/gene/9606:CSMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59FF8|||http://purl.uniprot.org/uniprot/Q96PZ7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB|||CUB 1|||CUB 10|||CUB 11|||CUB 12|||CUB 13|||CUB 14|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||CUB 6|||CUB 7|||CUB 8|||CUB 9|||CUB and sushi domain-containing protein 1|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Sushi|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 21|||Sushi 22|||Sushi 23|||Sushi 24|||Sushi 25|||Sushi 26|||Sushi 27|||Sushi 28|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021025|||http://purl.uniprot.org/annotation/VAR_056846|||http://purl.uniprot.org/annotation/VAR_059634|||http://purl.uniprot.org/annotation/VAR_059635|||http://purl.uniprot.org/annotation/VAR_059636|||http://purl.uniprot.org/annotation/VAR_076444|||http://purl.uniprot.org/annotation/VAR_076445|||http://purl.uniprot.org/annotation/VSP_009030|||http://purl.uniprot.org/annotation/VSP_009031|||http://purl.uniprot.org/annotation/VSP_009032|||http://purl.uniprot.org/annotation/VSP_009033|||http://purl.uniprot.org/annotation/VSP_009034|||http://purl.uniprot.org/annotation/VSP_009035
http://togogenome.org/gene/9606:TRIM17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP04|||http://purl.uniprot.org/uniprot/Q9Y577                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM17|||In isoform 2.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056224|||http://purl.uniprot.org/annotation/VSP_040994|||http://purl.uniprot.org/annotation/VSP_040995
http://togogenome.org/gene/9606:CORT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00230|||http://purl.uniprot.org/uniprot/Q8IUV6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Non-terminal Residue|||Peptide|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Non-terminal Residue|||Peptide|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  Cortistatin-17|||Cortistatin-29|||Somatostatin/Cortistatin C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033154|||http://purl.uniprot.org/annotation/PRO_0000033155|||http://purl.uniprot.org/annotation/PRO_0000033156|||http://purl.uniprot.org/annotation/PRO_5004308990
http://togogenome.org/gene/9606:CATSPER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XQ3                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cation channel sperm-associated protein 3|||Cytoplasmic|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S4|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Pore-forming                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295679|||http://purl.uniprot.org/annotation/VAR_033309
http://togogenome.org/gene/9606:RBM4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PLB0|||http://purl.uniprot.org/uniprot/Q9BQ04                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Interaction with TNPO3|||RNA-binding protein 4B|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081787|||http://purl.uniprot.org/annotation/VAR_064766
http://togogenome.org/gene/9606:NRXN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58401|||http://purl.uniprot.org/uniprot/Q9P2S2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 2|||EGF-like 3|||Extracellular|||Helical|||In isoform 2a.|||Laminin G-like|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||Laminin G-like 6|||N-linked (GlcNAc...) asparagine|||Neurexin-2|||Neurexin-2-beta|||O-linked (Xyl...) (heparan sulfate) serine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019495|||http://purl.uniprot.org/annotation/PRO_0000019497|||http://purl.uniprot.org/annotation/VAR_050266|||http://purl.uniprot.org/annotation/VSP_003505|||http://purl.uniprot.org/annotation/VSP_003506|||http://purl.uniprot.org/annotation/VSP_003507|||http://purl.uniprot.org/annotation/VSP_003508
http://togogenome.org/gene/9606:UBE3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3V4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Glycyl thioester intermediate|||HECT|||IQ|||In KOS.|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||Phosphoserine|||Ubiquitin-protein ligase E3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281882|||http://purl.uniprot.org/annotation/VAR_031302|||http://purl.uniprot.org/annotation/VAR_069712|||http://purl.uniprot.org/annotation/VSP_024085|||http://purl.uniprot.org/annotation/VSP_024086|||http://purl.uniprot.org/annotation/VSP_024087|||http://purl.uniprot.org/annotation/VSP_024088
http://togogenome.org/gene/9606:CCBE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3WKU1|||http://purl.uniprot.org/uniprot/Q6UXH8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Collagen and calcium-binding EGF domain-containing protein 1|||Collagen-like 1|||Collagen-like 2|||Disordered|||EGF-like|||EGF-like; calcium-binding|||In HKLLS1.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279516|||http://purl.uniprot.org/annotation/PRO_5035842139|||http://purl.uniprot.org/annotation/VAR_048971|||http://purl.uniprot.org/annotation/VAR_063746|||http://purl.uniprot.org/annotation/VAR_063747|||http://purl.uniprot.org/annotation/VAR_063748|||http://purl.uniprot.org/annotation/VAR_063749|||http://purl.uniprot.org/annotation/VAR_063750|||http://purl.uniprot.org/annotation/VSP_023469|||http://purl.uniprot.org/annotation/VSP_023470|||http://purl.uniprot.org/annotation/VSP_023471
http://togogenome.org/gene/9606:CNOT7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIV1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNA deadenylase activity.|||Abolishes RNA deadenylase activity. Drastically reduces the rate of deadenylation and decay of CBEP3-tethered mRNA.|||Abolishes interaction with CNOT1.|||Abolishes interaction with CNOT1; when associated with K-138 and K-149.|||Abolishes interaction with CNOT1; when associated with K-138 and Y-142.|||Abolishes interaction with CNOT1; when associated with Y-142 and K-149.|||Abolishes interaction with TOB1.|||CCR4-NOT transcription complex subunit 7|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212844|||http://purl.uniprot.org/annotation/VSP_045497
http://togogenome.org/gene/9606:NEK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JXL9|||http://purl.uniprot.org/uniprot/Q96PY6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In ALS24; associated with disease susceptibility.|||In SRTD6.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung large cell carcinoma sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 6.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086418|||http://purl.uniprot.org/annotation/VAR_040900|||http://purl.uniprot.org/annotation/VAR_040901|||http://purl.uniprot.org/annotation/VAR_040902|||http://purl.uniprot.org/annotation/VAR_040903|||http://purl.uniprot.org/annotation/VAR_040904|||http://purl.uniprot.org/annotation/VAR_040905|||http://purl.uniprot.org/annotation/VAR_040906|||http://purl.uniprot.org/annotation/VAR_046486|||http://purl.uniprot.org/annotation/VAR_046488|||http://purl.uniprot.org/annotation/VAR_046489|||http://purl.uniprot.org/annotation/VAR_051651|||http://purl.uniprot.org/annotation/VAR_061743|||http://purl.uniprot.org/annotation/VAR_069617|||http://purl.uniprot.org/annotation/VAR_069618|||http://purl.uniprot.org/annotation/VAR_080694|||http://purl.uniprot.org/annotation/VAR_080695|||http://purl.uniprot.org/annotation/VAR_080696|||http://purl.uniprot.org/annotation/VAR_080697|||http://purl.uniprot.org/annotation/VSP_004870|||http://purl.uniprot.org/annotation/VSP_035435|||http://purl.uniprot.org/annotation/VSP_035436|||http://purl.uniprot.org/annotation/VSP_035437|||http://purl.uniprot.org/annotation/VSP_035438|||http://purl.uniprot.org/annotation/VSP_035439
http://togogenome.org/gene/9606:COX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQM2|||http://purl.uniprot.org/uniprot/Q7KZN9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase assembly protein COX15 homolog|||Helical|||In MC4DN6.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183931|||http://purl.uniprot.org/annotation/VAR_019596|||http://purl.uniprot.org/annotation/VAR_033117|||http://purl.uniprot.org/annotation/VSP_011281
http://togogenome.org/gene/9606:MEX3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN04                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||KH 1|||KH 2|||Phosphoserine|||Polar residues|||Prevents RNA binding.|||RING-type|||RNA-binding protein MEX3B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278784|||http://purl.uniprot.org/annotation/VSP_041891|||http://purl.uniprot.org/annotation/VSP_041892
http://togogenome.org/gene/9606:LYPD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UX82                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||Ly6/PLAUR domain-containing protein 8|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317739|||http://purl.uniprot.org/annotation/PRO_0000317740
http://togogenome.org/gene/9606:SLC36A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q495M3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HG and IG; no effect on localization to the plasma membrane; decreased amino acid:proton symporter activity; no effect on protein reaction kinetics; decreased affinity for proline; 3-fold increase of Km value for proline; decreased affinity for glycine; 5-fold increase of Km for glycine.|||In isoform 2.|||In isoform 3.|||Proton-coupled amino acid transporter 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324819|||http://purl.uniprot.org/annotation/VAR_039887|||http://purl.uniprot.org/annotation/VAR_064795|||http://purl.uniprot.org/annotation/VSP_032371|||http://purl.uniprot.org/annotation/VSP_032372|||http://purl.uniprot.org/annotation/VSP_032373
http://togogenome.org/gene/9606:TNFRSF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS68                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||TNFR-Cys 1|||TNFR-Cys 2|||TNFR-Cys 3|||Tumor necrosis factor receptor superfamily member 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034597|||http://purl.uniprot.org/annotation/VAR_024278|||http://purl.uniprot.org/annotation/VAR_024279|||http://purl.uniprot.org/annotation/VAR_070812|||http://purl.uniprot.org/annotation/VSP_006512|||http://purl.uniprot.org/annotation/VSP_044886
http://togogenome.org/gene/9606:ADCY5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384P5Q5|||http://purl.uniprot.org/uniprot/B3KWA8|||http://purl.uniprot.org/uniprot/B7Z2C7|||http://purl.uniprot.org/uniprot/O95622                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 5|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Guanylate cyclase|||Guanylate cyclase 1|||Guanylate cyclase 2|||Helical|||In DSKOD; increases cAMP production upon activation of ADRB1.|||In DSKOR.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195694|||http://purl.uniprot.org/annotation/VAR_068821|||http://purl.uniprot.org/annotation/VAR_073778|||http://purl.uniprot.org/annotation/VAR_086538|||http://purl.uniprot.org/annotation/VAR_086539|||http://purl.uniprot.org/annotation/VAR_086540|||http://purl.uniprot.org/annotation/VAR_086541|||http://purl.uniprot.org/annotation/VAR_086542|||http://purl.uniprot.org/annotation/VSP_042914|||http://purl.uniprot.org/annotation/VSP_042915
http://togogenome.org/gene/9606:MAP3K15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZN16                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished protein kinase activity.|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Mitogen-activated protein kinase kinase kinase 15|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253481|||http://purl.uniprot.org/annotation/VAR_040716|||http://purl.uniprot.org/annotation/VAR_040717|||http://purl.uniprot.org/annotation/VAR_040718|||http://purl.uniprot.org/annotation/VAR_040719|||http://purl.uniprot.org/annotation/VAR_040720|||http://purl.uniprot.org/annotation/VAR_040721|||http://purl.uniprot.org/annotation/VAR_040722|||http://purl.uniprot.org/annotation/VAR_040723|||http://purl.uniprot.org/annotation/VAR_040724|||http://purl.uniprot.org/annotation/VAR_040725|||http://purl.uniprot.org/annotation/VAR_040726|||http://purl.uniprot.org/annotation/VAR_040727|||http://purl.uniprot.org/annotation/VAR_040728|||http://purl.uniprot.org/annotation/VSP_021038|||http://purl.uniprot.org/annotation/VSP_021039|||http://purl.uniprot.org/annotation/VSP_021040
http://togogenome.org/gene/9606:RAI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z5J4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2HC pre-PHD-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In SMS.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nuclear localization signal|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Retinoic acid-induced protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097159|||http://purl.uniprot.org/annotation/VAR_024344|||http://purl.uniprot.org/annotation/VAR_051300|||http://purl.uniprot.org/annotation/VAR_051301|||http://purl.uniprot.org/annotation/VAR_079636|||http://purl.uniprot.org/annotation/VSP_010995|||http://purl.uniprot.org/annotation/VSP_010996|||http://purl.uniprot.org/annotation/VSP_010997|||http://purl.uniprot.org/annotation/VSP_010998|||http://purl.uniprot.org/annotation/VSP_010999|||http://purl.uniprot.org/annotation/VSP_011000|||http://purl.uniprot.org/annotation/VSP_011001|||http://purl.uniprot.org/annotation/VSP_011002|||http://purl.uniprot.org/annotation/VSP_011003
http://togogenome.org/gene/9606:ACRBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD6|||http://purl.uniprot.org/uniprot/Q8NEB7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acrosin-binding protein|||Acrosin-binding protein, mature form|||Basic and acidic residues|||Disordered|||Polar residues|||Pro-ACR binding|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227516|||http://purl.uniprot.org/annotation/PRO_0000449367|||http://purl.uniprot.org/annotation/PRO_0000449368|||http://purl.uniprot.org/annotation/PRO_5014247024|||http://purl.uniprot.org/annotation/VAR_050633
http://togogenome.org/gene/9606:TDRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW6|||http://purl.uniprot.org/uniprot/Q9BXT4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||MYND-type|||Polar residues|||Tudor|||Tudor 1|||Tudor 2|||Tudor 3|||Tudor 4|||Tudor domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183161|||http://purl.uniprot.org/annotation/VAR_057321|||http://purl.uniprot.org/annotation/VAR_057322|||http://purl.uniprot.org/annotation/VSP_035481|||http://purl.uniprot.org/annotation/VSP_035482|||http://purl.uniprot.org/annotation/VSP_036667|||http://purl.uniprot.org/annotation/VSP_036668|||http://purl.uniprot.org/annotation/VSP_036669|||http://purl.uniprot.org/annotation/VSP_036670
http://togogenome.org/gene/9606:USP42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9J4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||Nucleophile|||Phosphoserine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080672|||http://purl.uniprot.org/annotation/VAR_059754|||http://purl.uniprot.org/annotation/VSP_040529
http://togogenome.org/gene/9606:BOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DN7|||http://purl.uniprot.org/uniprot/Q9BWV1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Brother of CDO|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234052|||http://purl.uniprot.org/annotation/PRO_5014589242|||http://purl.uniprot.org/annotation/VAR_033600|||http://purl.uniprot.org/annotation/VAR_033601|||http://purl.uniprot.org/annotation/VAR_035503|||http://purl.uniprot.org/annotation/VSP_034684
http://togogenome.org/gene/9606:AXDND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1B0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Axonemal dynein light chain domain-containing protein 1|||Basic and acidic residues|||Disordered|||Found in non-obstructive azoospermia in one patient; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284868|||http://purl.uniprot.org/annotation/VAR_031841|||http://purl.uniprot.org/annotation/VAR_031842|||http://purl.uniprot.org/annotation/VAR_050705|||http://purl.uniprot.org/annotation/VAR_050706|||http://purl.uniprot.org/annotation/VAR_088327|||http://purl.uniprot.org/annotation/VAR_088328|||http://purl.uniprot.org/annotation/VAR_088329|||http://purl.uniprot.org/annotation/VAR_088330|||http://purl.uniprot.org/annotation/VAR_088331|||http://purl.uniprot.org/annotation/VAR_088332|||http://purl.uniprot.org/annotation/VAR_088333|||http://purl.uniprot.org/annotation/VAR_088334|||http://purl.uniprot.org/annotation/VAR_088335|||http://purl.uniprot.org/annotation/VSP_024703|||http://purl.uniprot.org/annotation/VSP_024704|||http://purl.uniprot.org/annotation/VSP_024705|||http://purl.uniprot.org/annotation/VSP_024706|||http://purl.uniprot.org/annotation/VSP_024707|||http://purl.uniprot.org/annotation/VSP_024708
http://togogenome.org/gene/9606:IFNLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU57                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interferon lambda receptor 1|||More resistant to viral-induced degradation; when associated with R-319.|||More resistant to viral-induced degradation; when associated with R-320.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011019|||http://purl.uniprot.org/annotation/VSP_011888|||http://purl.uniprot.org/annotation/VSP_011889|||http://purl.uniprot.org/annotation/VSP_011890|||http://purl.uniprot.org/annotation/VSP_011891|||http://purl.uniprot.org/annotation/VSP_011892
http://togogenome.org/gene/9606:PGBD5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N414                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decreased DNA transposase activity.|||Disordered|||In isoform 2.|||Loss of DNA transposase activity and of cell transforming activity.|||Loss of DNA transposase activity. No effect on cell transforming activity.|||No effect on DNA transposase activity, nor on cell transforming activity.|||No effect on DNA transposase activity.|||Phosphoserine|||PiggyBac transposable element-derived protein 5|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288056|||http://purl.uniprot.org/annotation/VSP_059131
http://togogenome.org/gene/9606:OR2G2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGZ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2G2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150476|||http://purl.uniprot.org/annotation/VAR_034174|||http://purl.uniprot.org/annotation/VAR_034175|||http://purl.uniprot.org/annotation/VAR_034176|||http://purl.uniprot.org/annotation/VAR_034177
http://togogenome.org/gene/9606:SLIRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUN7|||http://purl.uniprot.org/uniprot/Q9GZT3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Impairs SRA-mediated repression; when associated with 24-A-A-25.|||Impairs SRA-mediated repression; when associated with A-62.|||Impairs corepressor activity; when associated with 13-A-A-14.|||Impairs corepressor activity; when associated with A-7.|||In isoform 2.|||Mitochondrion|||Phosphoserine|||Phosphothreonine|||RRM|||SRA stem-loop-interacting RNA-binding protein, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247051|||http://purl.uniprot.org/annotation/VSP_047350
http://togogenome.org/gene/9606:POLR2J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52435                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Modified Residue                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB11-a|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149309
http://togogenome.org/gene/9606:ZNF597                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LX8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 597                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047687|||http://purl.uniprot.org/annotation/VAR_033581
http://togogenome.org/gene/9606:FAM32A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y421                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Protein FAM32A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223250|||http://purl.uniprot.org/annotation/VSP_043860|||http://purl.uniprot.org/annotation/VSP_043861
http://togogenome.org/gene/9606:EVI2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P34910|||http://purl.uniprot.org/uniprot/Q9BRW1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein EVI2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021213|||http://purl.uniprot.org/annotation/VAR_056871|||http://purl.uniprot.org/annotation/VSP_056461
http://togogenome.org/gene/9606:CALN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1Z1|||http://purl.uniprot.org/uniprot/Q9BXU9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium-binding protein 8|||Cytoplasmic|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Extracellular|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073529|||http://purl.uniprot.org/annotation/VSP_060873
http://togogenome.org/gene/9606:SYNJ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PR85|||http://purl.uniprot.org/uniprot/B4DG94|||http://purl.uniprot.org/uniprot/O15056                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Catalytic|||Disordered|||In isoform 2A.|||In isoform 2B1.|||Phosphoserine|||Polar residues|||Pro residues|||RRM|||SAC|||Synaptojanin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209733|||http://purl.uniprot.org/annotation/VAR_024507|||http://purl.uniprot.org/annotation/VSP_012911|||http://purl.uniprot.org/annotation/VSP_012912|||http://purl.uniprot.org/annotation/VSP_012913
http://togogenome.org/gene/9606:RAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P55895                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||In CHIDG; reduced recombination activity.|||In OS.|||In T(-)B(-)NK(+) SCID.|||PHD-type; atypical|||Polar residues|||V(D)J recombination-activating protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167137|||http://purl.uniprot.org/annotation/VAR_005570|||http://purl.uniprot.org/annotation/VAR_005571|||http://purl.uniprot.org/annotation/VAR_008895|||http://purl.uniprot.org/annotation/VAR_008896|||http://purl.uniprot.org/annotation/VAR_045960|||http://purl.uniprot.org/annotation/VAR_045961|||http://purl.uniprot.org/annotation/VAR_045962
http://togogenome.org/gene/9606:CTDSP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZU7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1|||Completely abolishes phosphatase activity; when associated with E-96.|||Disordered|||FCP1 homology|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||No effect. Completely abolishes phosphatase activity; when associated with N-98.|||Proton donor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212572|||http://purl.uniprot.org/annotation/VAR_049054|||http://purl.uniprot.org/annotation/VSP_045865|||http://purl.uniprot.org/annotation/VSP_045866
http://togogenome.org/gene/9606:DRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MZF9|||http://purl.uniprot.org/uniprot/P55039                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  (3S)-3-hydroxylysine|||Developmentally-regulated GTP-binding protein 2|||Impairs JMJD7-mediated hydroxylation and ribonucleic acid binding.|||OBG-type G|||TGS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205427|||http://purl.uniprot.org/annotation/VAR_067452|||http://purl.uniprot.org/annotation/VAR_067453
http://togogenome.org/gene/9606:XAGE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTP9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||X antigen family member 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148351
http://togogenome.org/gene/9606:GBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In SPG46; loss of glucosylceramide catabolic process.|||In isoform 2.|||In isoform 3.|||Loss of glucosylceramide catabolic process.|||Non-lysosomal glucosylceramidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283758|||http://purl.uniprot.org/annotation/VAR_069634|||http://purl.uniprot.org/annotation/VAR_069635|||http://purl.uniprot.org/annotation/VAR_081406|||http://purl.uniprot.org/annotation/VAR_081407|||http://purl.uniprot.org/annotation/VAR_081408|||http://purl.uniprot.org/annotation/VAR_081409|||http://purl.uniprot.org/annotation/VAR_081410|||http://purl.uniprot.org/annotation/VSP_024383|||http://purl.uniprot.org/annotation/VSP_024384
http://togogenome.org/gene/9606:RAPSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4A2|||http://purl.uniprot.org/uniprot/A0A0S2Z4A6|||http://purl.uniprot.org/uniprot/A0A0S2Z4F8|||http://purl.uniprot.org/uniprot/A0A0S2Z4M9|||http://purl.uniprot.org/uniprot/Q13702                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  43 kDa receptor-associated protein of the synapse|||In CMS11.|||In CMS11; reduced coclustering with acetylcholine receptor.|||In FADS2.|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Phosphotyrosine|||RING-type|||Removed|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167591|||http://purl.uniprot.org/annotation/VAR_021216|||http://purl.uniprot.org/annotation/VAR_021217|||http://purl.uniprot.org/annotation/VAR_043897|||http://purl.uniprot.org/annotation/VAR_043898|||http://purl.uniprot.org/annotation/VAR_043899|||http://purl.uniprot.org/annotation/VAR_043900|||http://purl.uniprot.org/annotation/VAR_043901|||http://purl.uniprot.org/annotation/VAR_043902|||http://purl.uniprot.org/annotation/VAR_043903|||http://purl.uniprot.org/annotation/VAR_062142|||http://purl.uniprot.org/annotation/VSP_005533
http://togogenome.org/gene/9606:LIN28A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9Z2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ability to suppress pre-let-7 biogenesis and localization to P-bodies without affecting pre-let-7 binding; when associated with A-147.|||Abolishes ability to suppress pre-let-7 biogenesis and localization to P-bodies without affecting pre-let-7 binding; when associated with A-169.|||CCHC-type 1|||CCHC-type 2|||CSD|||Disordered|||Does not affect localization to P-bodies; when associated with A-46 and A-55.|||Does not affect localization to P-bodies; when associated with A-46 and A-73.|||Does not affect localization to P-bodies; when associated with A-55 and A-73.|||Flexible linker|||N-acetylglycine|||Phosphoserine|||Protein lin-28 homolog A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253787
http://togogenome.org/gene/9606:XYLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75191                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Xylulose kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000230985|||http://purl.uniprot.org/annotation/VAR_055151|||http://purl.uniprot.org/annotation/VAR_055152|||http://purl.uniprot.org/annotation/VAR_055153|||http://purl.uniprot.org/annotation/VAR_055154|||http://purl.uniprot.org/annotation/VAR_055155|||http://purl.uniprot.org/annotation/VSP_055522
http://togogenome.org/gene/9606:OR5J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVP0|||http://purl.uniprot.org/uniprot/Q8NH18                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5J2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150599|||http://purl.uniprot.org/annotation/VAR_034226
http://togogenome.org/gene/9606:COG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2V7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 6|||In CDG2L.|||In isoform 2.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213513|||http://purl.uniprot.org/annotation/VAR_048759|||http://purl.uniprot.org/annotation/VAR_048760|||http://purl.uniprot.org/annotation/VAR_048761|||http://purl.uniprot.org/annotation/VAR_061110|||http://purl.uniprot.org/annotation/VAR_068240|||http://purl.uniprot.org/annotation/VSP_001131|||http://purl.uniprot.org/annotation/VSP_001132|||http://purl.uniprot.org/annotation/VSP_040375|||http://purl.uniprot.org/annotation/VSP_040376
http://togogenome.org/gene/9606:TRIM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9C026                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||B30.2/SPRY|||COS|||E3 ubiquitin-protein ligase TRIM9|||Fibronectin type-III|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Phosphothreonine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056208|||http://purl.uniprot.org/annotation/VAR_016202|||http://purl.uniprot.org/annotation/VSP_007922|||http://purl.uniprot.org/annotation/VSP_007923|||http://purl.uniprot.org/annotation/VSP_007924|||http://purl.uniprot.org/annotation/VSP_007925|||http://purl.uniprot.org/annotation/VSP_007926
http://togogenome.org/gene/9606:ALOX12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75342                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Arachidonate 12-lipoxygenase, 12R-type|||In ARCI2.|||In ARCI2; complete loss of the enzyme activity.|||Lipoxygenase|||PLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220689|||http://purl.uniprot.org/annotation/VAR_015173|||http://purl.uniprot.org/annotation/VAR_015174|||http://purl.uniprot.org/annotation/VAR_050000|||http://purl.uniprot.org/annotation/VAR_069545|||http://purl.uniprot.org/annotation/VAR_069546|||http://purl.uniprot.org/annotation/VAR_069547|||http://purl.uniprot.org/annotation/VAR_069548|||http://purl.uniprot.org/annotation/VAR_069549|||http://purl.uniprot.org/annotation/VAR_069550|||http://purl.uniprot.org/annotation/VAR_069551|||http://purl.uniprot.org/annotation/VAR_069552|||http://purl.uniprot.org/annotation/VAR_069553|||http://purl.uniprot.org/annotation/VAR_069554|||http://purl.uniprot.org/annotation/VAR_069555|||http://purl.uniprot.org/annotation/VAR_069556|||http://purl.uniprot.org/annotation/VAR_069557|||http://purl.uniprot.org/annotation/VAR_069558|||http://purl.uniprot.org/annotation/VAR_069559|||http://purl.uniprot.org/annotation/VAR_069560
http://togogenome.org/gene/9606:SCAND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P57086|||http://purl.uniprot.org/uniprot/Q9NZG6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||SCAN box|||SCAN domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097632
http://togogenome.org/gene/9606:P2RX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32MC3|||http://purl.uniprot.org/uniprot/Q9UBL9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||In DFNA41.|||In DFNA41; found in heterozygous status in patients; abolished ATP-stimulated permeability.|||In isoform B and isoform K.|||In isoform C and isoform K.|||In isoform D.|||In isoform H.|||In isoform I.|||In isoform K.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 2|||Polar residues|||Pore-forming motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161549|||http://purl.uniprot.org/annotation/VAR_070687|||http://purl.uniprot.org/annotation/VAR_070688|||http://purl.uniprot.org/annotation/VSP_004495|||http://purl.uniprot.org/annotation/VSP_004496|||http://purl.uniprot.org/annotation/VSP_004497|||http://purl.uniprot.org/annotation/VSP_004498|||http://purl.uniprot.org/annotation/VSP_004499|||http://purl.uniprot.org/annotation/VSP_014135
http://togogenome.org/gene/9606:ZFP42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Zinc finger protein 42 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287289
http://togogenome.org/gene/9606:POLR2J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZM3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA-directed RNA polymerase II subunit RPB11-b1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316946|||http://purl.uniprot.org/annotation/VAR_070807|||http://purl.uniprot.org/annotation/VSP_030820
http://togogenome.org/gene/9606:DGCR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14129|||http://purl.uniprot.org/uniprot/X5D7D2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein DGCR6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070259|||http://purl.uniprot.org/annotation/VAR_033866|||http://purl.uniprot.org/annotation/VSP_055898|||http://purl.uniprot.org/annotation/VSP_055899
http://togogenome.org/gene/9606:TMEM198                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66K66                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Pro residues|||Transmembrane protein 198                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000326030
http://togogenome.org/gene/9606:BCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V3S7|||http://purl.uniprot.org/uniprot/P10415                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cleavage by caspase-3.|||Apoptosis regulator Bcl-2|||Apoptosis regulator Bcl-2 family BH4|||BH1|||BH2|||BH3|||BH4|||Cleavage; by caspase-3|||Disordered|||Helical|||In isoform Beta.|||In non-Hodgkin lymphoma; somatic mutation.|||Loss of BAX-binding and of anti-apoptotic activity.|||Loss of BAX-binding and of anti-apoptotic activity. May also affect protein stability.|||Loss of BAX-binding and of anti-apoptotic activity. No effect on NLRP1-induced IL1B release, nor on homodimerization. Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146.|||Loss of BAX-binding and of anti-apoptotic activity. No effect on homodimerization.|||Loss of BAX-binding and of anti-apoptotic activity; when associated with A-144 and A145.|||Loss of BAX-binding and of anti-apoptotic activity; when associated with A-145 and A146.|||No effect on BAX-binding, nor on anti-apoptotic activity. Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-192. No effect on homodimerization; when associated with L-190 and A-191.|||No effect on cleavage by caspase-3.|||Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity.|||Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with A-191 and A-192. No effect on homodimerization; when associated with L-190 and A-191.|||Partial loss of BAX-binding and 50% decrease in anti-apoptotic activity; when associated with L-190 and A-191. No effect on homodimerization; when associated with L-190 and A-191.|||Phosphoserine; by MAPK8|||Phosphoserine; by MAPK8 and PKC|||Phosphothreonine; by MAPK8|||Required for interaction with SEPTIN4 isoform ARTS. Required XIAP-mediated ubiquitination and apoptosis                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143048|||http://purl.uniprot.org/annotation/VAR_000827|||http://purl.uniprot.org/annotation/VAR_000828|||http://purl.uniprot.org/annotation/VAR_000829|||http://purl.uniprot.org/annotation/VAR_014716|||http://purl.uniprot.org/annotation/VSP_000512
http://togogenome.org/gene/9606:LCMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIC8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Leucine carboxyl methyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204422|||http://purl.uniprot.org/annotation/VSP_017428|||http://purl.uniprot.org/annotation/VSP_041416
http://togogenome.org/gene/9606:PRDM13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H4Q3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Disordered|||In PCH17; unknown pathological significance.|||PR domain zinc finger protein 13|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047770|||http://purl.uniprot.org/annotation/VAR_087006
http://togogenome.org/gene/9606:PPP1CB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62140|||http://purl.uniprot.org/uniprot/V9HW04                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In NSLH2.|||In NSLH2; unknown pathological significance.|||N-acetylalanine|||Phosphothreonine|||Proton donor|||Removed|||Serine/threonine specific protein phosphatases|||Serine/threonine-protein phosphatase PP1-beta catalytic subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058779|||http://purl.uniprot.org/annotation/VAR_076839|||http://purl.uniprot.org/annotation/VAR_076840|||http://purl.uniprot.org/annotation/VAR_079189|||http://purl.uniprot.org/annotation/VAR_079190|||http://purl.uniprot.org/annotation/VAR_079191|||http://purl.uniprot.org/annotation/VAR_079192
http://togogenome.org/gene/9606:TERF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54274                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization and telomere binding; when associated with D-74.|||Abolishes dimerization and telomere binding; when associated with P-75.|||Abolishes telomere binding.|||Basic and acidic residues|||Diminishes telomere binding.|||Disordered|||Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants).|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type|||In isoform 2.|||Interaction with RLIM|||Loss of interaction with FBXO4.|||Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells.|||N-acetylalanine|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by ATM|||Polar residues|||Removed|||TRFH mediates dimerization|||Telomeric repeat-binding factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197129|||http://purl.uniprot.org/annotation/VSP_003303
http://togogenome.org/gene/9606:MIA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G155|||http://purl.uniprot.org/uniprot/Q59FD2|||http://purl.uniprot.org/uniprot/Q96PC5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Decreased interaction with PERB. No effect on interaction with MIA3.|||Disordered|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 10 and isoform 12.|||In isoform 11 and isoform 12.|||In isoform 2.|||In isoform 4 and isoform 7.|||In isoform 4 and isoform 8.|||In isoform 5 and isoform 13.|||In isoform 5.|||In isoform 6, isoform 7, isoform 9 and isoform 11.|||In isoform 9.|||Loss of interaction with PERB. Unable to recruit PERB to the endoplasmic reticulum exit sites. Loss of function in collagen VII transport. No effect on interaction with MIA3.|||Lumenal|||Mediates interaction with MIA3|||Melanoma inhibitory activity protein 2|||N-linked (GlcNAc...) asparagine|||No effect on interaction with PERB.|||Polar residues|||Pro residues|||Proline-rich domain (PRD); mediates interaction with the COPII coat subunits SEC23A and SEC23B|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019031|||http://purl.uniprot.org/annotation/VAR_036460|||http://purl.uniprot.org/annotation/VAR_047891|||http://purl.uniprot.org/annotation/VAR_047892|||http://purl.uniprot.org/annotation/VAR_047893|||http://purl.uniprot.org/annotation/VAR_047894|||http://purl.uniprot.org/annotation/VAR_047895|||http://purl.uniprot.org/annotation/VAR_047896|||http://purl.uniprot.org/annotation/VAR_082860|||http://purl.uniprot.org/annotation/VAR_082861|||http://purl.uniprot.org/annotation/VAR_082862|||http://purl.uniprot.org/annotation/VAR_082863|||http://purl.uniprot.org/annotation/VAR_082864|||http://purl.uniprot.org/annotation/VSP_058472|||http://purl.uniprot.org/annotation/VSP_058473|||http://purl.uniprot.org/annotation/VSP_060003|||http://purl.uniprot.org/annotation/VSP_060004|||http://purl.uniprot.org/annotation/VSP_060005|||http://purl.uniprot.org/annotation/VSP_060006|||http://purl.uniprot.org/annotation/VSP_060007|||http://purl.uniprot.org/annotation/VSP_060008|||http://purl.uniprot.org/annotation/VSP_060009|||http://purl.uniprot.org/annotation/VSP_060010|||http://purl.uniprot.org/annotation/VSP_060011|||http://purl.uniprot.org/annotation/VSP_060012|||http://purl.uniprot.org/annotation/VSP_060013|||http://purl.uniprot.org/annotation/VSP_060014|||http://purl.uniprot.org/annotation/VSP_060015
http://togogenome.org/gene/9606:RIC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z607|||http://purl.uniprot.org/uniprot/A0A0S2Z6D3|||http://purl.uniprot.org/uniprot/B7Z3Z0|||http://purl.uniprot.org/uniprot/Q7Z5B4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Lumenal|||N6-acetyllysine; alternate|||Protein RIC-3|||Resistance to inhibitors of cholinesterase protein 3 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302731|||http://purl.uniprot.org/annotation/VAR_034943|||http://purl.uniprot.org/annotation/VAR_036391|||http://purl.uniprot.org/annotation/VAR_062208|||http://purl.uniprot.org/annotation/VSP_027939|||http://purl.uniprot.org/annotation/VSP_027940|||http://purl.uniprot.org/annotation/VSP_027941|||http://purl.uniprot.org/annotation/VSP_027943|||http://purl.uniprot.org/annotation/VSP_043786
http://togogenome.org/gene/9606:CLEC9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXN8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes binding to damaged cells; when associated with A-131.|||Abolishes binding to damaged cells; when associated with A-227.|||C-type lectin|||C-type lectin domain family 9 member A|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||ITAM-like|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046637|||http://purl.uniprot.org/annotation/VAR_050112
http://togogenome.org/gene/9606:COL5A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25940                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Collagen alpha-3(V) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Disordered|||Fibrillar collagen NC1|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Pro residues|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005845|||http://purl.uniprot.org/annotation/VAR_020015|||http://purl.uniprot.org/annotation/VAR_020016|||http://purl.uniprot.org/annotation/VAR_020017|||http://purl.uniprot.org/annotation/VAR_020018|||http://purl.uniprot.org/annotation/VAR_020019|||http://purl.uniprot.org/annotation/VAR_055678|||http://purl.uniprot.org/annotation/VAR_055679|||http://purl.uniprot.org/annotation/VAR_060789
http://togogenome.org/gene/9606:BEST1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4M4|||http://purl.uniprot.org/uniprot/A0A0S2Z579|||http://purl.uniprot.org/uniprot/B7Z375|||http://purl.uniprot.org/uniprot/O76090                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||INTRAMEM|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Bestrophin-1|||Cytoplasmic|||Extracellular|||Helical|||In ARB and VMD2; no effect on subcellular location in transfected MDCK.2 and HEK293T cells; possible decrease in protein stability; reduced chloride conductance.|||In ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance.|||In ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced whole-cell conductance.|||In ARB; possible decrease in protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance.|||In ARB; unknown pathological significance; no effect on subcellular location in transfected HEK293T cells; loss of chloride conductance.|||In RP50 and ARB; possible decrease in protein stability; causes protein mislocalization to the cytoplasm and reduction of channel activity.|||In RP50 and VMD2.|||In RP50; causes protein mislocalization to the cytoplasm.|||In RP50; reduced channel activity.|||In VMD2 and ARB; no effect on protein stability; loss of cell membrane localization in transfected MDCK.2 cells; reduced chloride conductance.|||In VMD2 and ARB; no effect on subcellular location in induced pluripotent stem cell-derived retinal pigment epithelial cells; loss of cell membrane localization in transfected MDCK.2 cells; possible decrease in protein stability; reduced chloride conductance.|||In VMD2 and ARB; no effect on subcellular location in transfected MDCK.2 cells; possible decrease in protein stability; reduced chloride conductance.|||In VMD2.|||In VMD2; benign variant.|||In VMD2; decreased chloride and bicarbonate conductance.|||In VMD2; late-onset of visual disturbance.|||In VMD2; loss of cloride and bicarbonate conductance.|||In VMD2; no effect on subcellular location in transfected HEK293T cells; loss of cloride and bicarbonate conductance.|||In VMD2; sporadic; requires 2 nucleotide substitutions.|||In VMD2; unknown pathological significance.|||In VRCP.|||In a family affected by Leber congenital amaurosis/VMD2 and VMD2.|||In a sporadic case of age-related macular degeneration.|||In a sporadic case of age-related macular degeneration; unknown pathological significance.|||In a sporadic case of concentric annular macular dystrophy and VMD2.|||In age-related macular degeneration.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143114|||http://purl.uniprot.org/annotation/VAR_000830|||http://purl.uniprot.org/annotation/VAR_000831|||http://purl.uniprot.org/annotation/VAR_000832|||http://purl.uniprot.org/annotation/VAR_000833|||http://purl.uniprot.org/annotation/VAR_000834|||http://purl.uniprot.org/annotation/VAR_000835|||http://purl.uniprot.org/annotation/VAR_000836|||http://purl.uniprot.org/annotation/VAR_000837|||http://purl.uniprot.org/annotation/VAR_000838|||http://purl.uniprot.org/annotation/VAR_000839|||http://purl.uniprot.org/annotation/VAR_000840|||http://purl.uniprot.org/annotation/VAR_000841|||http://purl.uniprot.org/annotation/VAR_000842|||http://purl.uniprot.org/annotation/VAR_000843|||http://purl.uniprot.org/annotation/VAR_000844|||http://purl.uniprot.org/annotation/VAR_000845|||http://purl.uniprot.org/annotation/VAR_000846|||http://purl.uniprot.org/annotation/VAR_000847|||http://purl.uniprot.org/annotation/VAR_000848|||http://purl.uniprot.org/annotation/VAR_000849|||http://purl.uniprot.org/annotation/VAR_000850|||http://purl.uniprot.org/annotation/VAR_000851|||http://purl.uniprot.org/annotation/VAR_000852|||http://purl.uniprot.org/annotation/VAR_000853|||http://purl.uniprot.org/annotation/VAR_000854|||http://purl.uniprot.org/annotation/VAR_000855|||http://purl.uniprot.org/annotation/VAR_000856|||http://purl.uniprot.org/annotation/VAR_000857|||http://purl.uniprot.org/annotation/VAR_000858|||http://purl.uniprot.org/annotation/VAR_000859|||http://purl.uniprot.org/annotation/VAR_000860|||http://purl.uniprot.org/annotation/VAR_000861|||http://purl.uniprot.org/annotation/VAR_000862|||http://purl.uniprot.org/annotation/VAR_000863|||http://purl.uniprot.org/annotation/VAR_000864|||http://purl.uniprot.org/annotation/VAR_000865|||http://purl.uniprot.org/annotation/VAR_000866|||http://purl.uniprot.org/annotation/VAR_000867|||http://purl.uniprot.org/annotation/VAR_000868|||http://purl.uniprot.org/annotation/VAR_009278|||http://purl.uniprot.org/annotation/VAR_010468|||http://purl.uniprot.org/annotation/VAR_010469|||http://purl.uniprot.org/annotation/VAR_010470|||http://purl.uniprot.org/annotation/VAR_010471|||http://purl.uniprot.org/annotation/VAR_010472|||http://purl.uniprot.org/annotation/VAR_010473|||http://purl.uniprot.org/annotation/VAR_010474|||http://purl.uniprot.org/annotation/VAR_010475|||http://purl.uniprot.org/annotation/VAR_010476|||http://purl.uniprot.org/annotation/VAR_010477|||http://purl.uniprot.org/annotation/VAR_010478|||http://purl.uniprot.org/annotation/VAR_010479|||http://purl.uniprot.org/annotation/VAR_010480|||http://purl.uniprot.org/annotation/VAR_010481|||http://purl.uniprot.org/annotation/VAR_010482|||http://purl.uniprot.org/annotation/VAR_010483|||http://purl.uniprot.org/annotation/VAR_010484|||http://purl.uniprot.org/annotation/VAR_010485|||http://purl.uniprot.org/annotation/VAR_010486|||http://purl.uniprot.org/annotation/VAR_010487|||http://purl.uniprot.org/annotation/VAR_010488|||http://purl.uniprot.org/annotation/VAR_010489|||http://purl.uniprot.org/annotation/VAR_010490|||http://purl.uniprot.org/annotation/VAR_010491|||http://purl.uniprot.org/annotation/VAR_017366|||http://purl.uniprot.org/annotation/VAR_017367|||http://purl.uniprot.org/annotation/VAR_017368|||http://purl.uniprot.org/annotation/VAR_017369|||http://purl.uniprot.org/annotation/VAR_017370|||http://purl.uniprot.org/annotation/VAR_017371|||http://purl.uniprot.org/annotation/VAR_017372|||http://purl.uniprot.org/annotation/VAR_017373|||http://purl.uniprot.org/annotation/VAR_017374|||http://purl.uniprot.org/annotation/VAR_017375|||http://purl.uniprot.org/annotation/VAR_017376|||http://purl.uniprot.org/annotation/VAR_017377|||http://purl.uniprot.org/annotation/VAR_017378|||http://purl.uniprot.org/annotation/VAR_017379|||http://purl.uniprot.org/annotation/VAR_017380|||http://purl.uniprot.org/annotation/VAR_017381|||http://purl.uniprot.org/annotation/VAR_025731|||http://purl.uniprot.org/annotation/VAR_025732|||http://purl.uniprot.org/annotation/VAR_025733|||http://purl.uniprot.org/annotation/VAR_025734|||http://purl.uniprot.org/annotation/VAR_025735|||http://purl.uniprot.org/annotation/VAR_025736|||http://purl.uniprot.org/annotation/VAR_025737|||http://purl.uniprot.org/annotation/VAR_025738|||http://purl.uniprot.org/annotation/VAR_025739|||http://purl.uniprot.org/annotation/VAR_025740|||http://purl.uniprot.org/annotation/VAR_025741|||http://purl.uniprot.org/annotation/VAR_025742|||http://purl.uniprot.org/annotation/VAR_025743|||http://purl.uniprot.org/annotation/VAR_025744|||http://purl.uniprot.org/annotation/VAR_025745|||http://purl.uniprot.org/annotation/VAR_025746|||http://purl.uniprot.org/annotation/VAR_025747|||http://purl.uniprot.org/annotation/VAR_025748|||http://purl.uniprot.org/annotation/VAR_025749|||http://purl.uniprot.org/annotation/VAR_025750|||http://purl.uniprot.org/annotation/VAR_025751|||http://purl.uniprot.org/annotation/VAR_025752|||http://purl.uniprot.org/annotation/VAR_025753|||http://purl.uniprot.org/annotation/VAR_043493|||http://purl.uniprot.org/annotation/VAR_043494|||http://purl.uniprot.org/annotation/VAR_043495|||http://purl.uniprot.org/annotation/VAR_043496|||http://purl.uniprot.org/annotation/VAR_058273|||http://purl.uniprot.org/annotation/VAR_058274|||http://purl.uniprot.org/annotation/VAR_058275|||http://purl.uniprot.org/annotation/VAR_058276|||http://purl.uniprot.org/annotation/VAR_058277|||http://purl.uniprot.org/annotation/VAR_058278|||http://purl.uniprot.org/annotation/VAR_058313|||http://purl.uniprot.org/annotation/VAR_063169|||http://purl.uniprot.org/annotation/VAR_063170|||http://purl.uniprot.org/annotation/VAR_063171|||http://purl.uniprot.org/annotation/VAR_075346|||http://purl.uniprot.org/annotation/VAR_075347|||http://purl.uniprot.org/annotation/VSP_008973|||http://purl.uniprot.org/annotation/VSP_008974|||http://purl.uniprot.org/annotation/VSP_008975
http://togogenome.org/gene/9606:SP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDD2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Enhances osteogenic differentiation in C2C12 cells.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||N6-propionyllysine|||Pro residues|||Transcription factor Sp7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047150|||http://purl.uniprot.org/annotation/VSP_047639
http://togogenome.org/gene/9606:TJP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2R3|||http://purl.uniprot.org/uniprot/B7Z954|||http://purl.uniprot.org/uniprot/Q9UDY2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In FHCA1; affects the interaction with claudins.|||In isoform 6.|||In isoform 7.|||In isoform A2 and isoform C2.|||In isoform A3.|||In isoform C1 and isoform C2.|||Interaction with SCRIB|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SH3|||Tight junction protein ZO-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094543|||http://purl.uniprot.org/annotation/VAR_016004|||http://purl.uniprot.org/annotation/VAR_030798|||http://purl.uniprot.org/annotation/VAR_046675|||http://purl.uniprot.org/annotation/VAR_046676|||http://purl.uniprot.org/annotation/VAR_046677|||http://purl.uniprot.org/annotation/VAR_046678|||http://purl.uniprot.org/annotation/VSP_003149|||http://purl.uniprot.org/annotation/VSP_006953|||http://purl.uniprot.org/annotation/VSP_007835|||http://purl.uniprot.org/annotation/VSP_007836|||http://purl.uniprot.org/annotation/VSP_046114|||http://purl.uniprot.org/annotation/VSP_046115|||http://purl.uniprot.org/annotation/VSP_046116
http://togogenome.org/gene/9606:TOMM20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15388                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Defects in mitophagy; when associated with R-56 and R-61.|||Defects in mitophagy; when associated with R-56 and R-68.|||Defects in mitophagy; when associated with R-61 and R-68.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||Mitochondrial import receptor subunit TOM20 homolog|||Mitochondrial intermembrane|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051538|||http://purl.uniprot.org/annotation/VAR_052366|||http://purl.uniprot.org/annotation/VAR_052367
http://togogenome.org/gene/9606:GP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40197                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Platelet glycoprotein V                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021361
http://togogenome.org/gene/9606:DNASE2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66K39|||http://purl.uniprot.org/uniprot/Q8WZ79                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Deoxyribonuclease-2-beta|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007295|||http://purl.uniprot.org/annotation/VAR_048872|||http://purl.uniprot.org/annotation/VAR_059250|||http://purl.uniprot.org/annotation/VAR_059251|||http://purl.uniprot.org/annotation/VSP_009812
http://togogenome.org/gene/9606:TRIQK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q629K1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Triple QxxK/R motif-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340674
http://togogenome.org/gene/9606:SFRP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6FHJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FZ|||N-linked (GlcNAc...) asparagine|||NTR|||Secreted frizzled-related protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032550|||http://purl.uniprot.org/annotation/VAR_051964|||http://purl.uniprot.org/annotation/VAR_051965
http://togogenome.org/gene/9606:FAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PIA2|||http://purl.uniprot.org/uniprot/Q9NYQ8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 10|||Cadherin 11|||Cadherin 12|||Cadherin 13|||Cadherin 14|||Cadherin 15|||Cadherin 16|||Cadherin 17|||Cadherin 18|||Cadherin 19|||Cadherin 2|||Cadherin 20|||Cadherin 21|||Cadherin 22|||Cadherin 23|||Cadherin 24|||Cadherin 25|||Cadherin 26|||Cadherin 27|||Cadherin 28|||Cadherin 29|||Cadherin 3|||Cadherin 30|||Cadherin 31|||Cadherin 32|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2|||Extracellular|||Helical|||In SCA45; unknown pathological significance.|||Laminin G|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Protocadherin Fat 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004018|||http://purl.uniprot.org/annotation/VAR_055595|||http://purl.uniprot.org/annotation/VAR_055596|||http://purl.uniprot.org/annotation/VAR_055597|||http://purl.uniprot.org/annotation/VAR_055598|||http://purl.uniprot.org/annotation/VAR_055599|||http://purl.uniprot.org/annotation/VAR_055600|||http://purl.uniprot.org/annotation/VAR_055601|||http://purl.uniprot.org/annotation/VAR_055602|||http://purl.uniprot.org/annotation/VAR_055603|||http://purl.uniprot.org/annotation/VAR_055604|||http://purl.uniprot.org/annotation/VAR_055605|||http://purl.uniprot.org/annotation/VAR_055606|||http://purl.uniprot.org/annotation/VAR_055607|||http://purl.uniprot.org/annotation/VAR_055608|||http://purl.uniprot.org/annotation/VAR_055609|||http://purl.uniprot.org/annotation/VAR_055610|||http://purl.uniprot.org/annotation/VAR_055611|||http://purl.uniprot.org/annotation/VAR_055612|||http://purl.uniprot.org/annotation/VAR_055613|||http://purl.uniprot.org/annotation/VAR_055614|||http://purl.uniprot.org/annotation/VAR_058286|||http://purl.uniprot.org/annotation/VAR_061076|||http://purl.uniprot.org/annotation/VAR_061077|||http://purl.uniprot.org/annotation/VAR_080665|||http://purl.uniprot.org/annotation/VAR_080666
http://togogenome.org/gene/9606:CCL21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00585                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  C-C motif chemokine 21|||C-terminal basic extension|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005220
http://togogenome.org/gene/9606:TREML4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXN2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Trem-like transcript 4 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307276|||http://purl.uniprot.org/annotation/VAR_035390|||http://purl.uniprot.org/annotation/VAR_035391|||http://purl.uniprot.org/annotation/VAR_035392
http://togogenome.org/gene/9606:GRM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1D0|||http://purl.uniprot.org/uniprot/Q14832                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 3 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Metabotropic glutamate receptor 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012927|||http://purl.uniprot.org/annotation/PRO_5014296875|||http://purl.uniprot.org/annotation/VAR_049274|||http://purl.uniprot.org/annotation/VSP_047679|||http://purl.uniprot.org/annotation/VSP_047680
http://togogenome.org/gene/9606:SNX27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y8A7|||http://purl.uniprot.org/uniprot/Q96L92                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ADRB2, sorting and recycling of ADRB2.|||Disordered|||FERM-like region F1|||FERM-like region F2|||FERM-like region F3|||In isoform 2 and isoform 3.|||In isoform 3.|||PDZ|||PX|||Phosphoserine|||Ras-associating|||Sorting nexin-27                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315356|||http://purl.uniprot.org/annotation/VAR_059851|||http://purl.uniprot.org/annotation/VSP_030537|||http://purl.uniprot.org/annotation/VSP_030538|||http://purl.uniprot.org/annotation/VSP_030539
http://togogenome.org/gene/9606:CHRND                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3W4|||http://purl.uniprot.org/uniprot/Q07001                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acetylcholine receptor subunit delta|||Cytoplasmic|||Disordered|||Extracellular|||Has no appreciable kinetic effects; allows for robust AChR expression.|||Helical|||In CMS3A; delayed closure of AchR ion channels, increasing the propensity for open-channel block, as well as a reduced rate of channel opening.|||In CMS3B; burst duration was decreased and disassociation of ACh was increased resulting in brief channel opening episodes; shows abnormal association with alpha CHRNA1 subunit resulting in a decreased number of fully assembled AChRs.|||In CMS3B; prevents expression of the AChR on the cell surface; is a null mutation.|||In CMS3B; reduced adult and fetal AChR expression and a reduced probability of both adult and fetal AChR being in the open state.|||In CMS3B; results in reduced gating efficiency; slows opening of the channel; decreases probability that the channel will open in response to ACh.|||In CMS3C; results in reduced expression of the AChR at the cell surface; impairs normal clustering of the AChR channel with RAPSN.|||In LMPS.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increased length of channel opening.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel transmembrane|||Phosphotyrosine; by Tyr-kinases|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000322|||http://purl.uniprot.org/annotation/VAR_019566|||http://purl.uniprot.org/annotation/VAR_021210|||http://purl.uniprot.org/annotation/VAR_021211|||http://purl.uniprot.org/annotation/VAR_021212|||http://purl.uniprot.org/annotation/VAR_036031|||http://purl.uniprot.org/annotation/VAR_043905|||http://purl.uniprot.org/annotation/VAR_073691|||http://purl.uniprot.org/annotation/VAR_073692|||http://purl.uniprot.org/annotation/VAR_073693|||http://purl.uniprot.org/annotation/VAR_073694|||http://purl.uniprot.org/annotation/VSP_046423
http://togogenome.org/gene/9606:SH2D3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K2M8|||http://purl.uniprot.org/uniprot/Q9BRG2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Loss of phosphorylation.|||Phosphoserine|||SH2|||SH2 domain-containing protein 3A|||Weak phosphorylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233132|||http://purl.uniprot.org/annotation/VAR_026054|||http://purl.uniprot.org/annotation/VAR_035989|||http://purl.uniprot.org/annotation/VAR_051349|||http://purl.uniprot.org/annotation/VSP_056268|||http://purl.uniprot.org/annotation/VSP_056269|||http://purl.uniprot.org/annotation/VSP_056270
http://togogenome.org/gene/9606:HTR3E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5X5Y0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 3E|||Cytoplasmic|||Extracellular|||HA-stretch; determines single-channel conductance in 5-HT3 receptors|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 5.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312294|||http://purl.uniprot.org/annotation/VAR_037481|||http://purl.uniprot.org/annotation/VAR_037482|||http://purl.uniprot.org/annotation/VSP_029803|||http://purl.uniprot.org/annotation/VSP_029804|||http://purl.uniprot.org/annotation/VSP_045573
http://togogenome.org/gene/9606:PEPD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJR2|||http://purl.uniprot.org/uniprot/P12955                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Aminopeptidase P N-terminal|||In PD.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Removed|||Xaa-Pro dipeptidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185087|||http://purl.uniprot.org/annotation/VAR_004404|||http://purl.uniprot.org/annotation/VAR_004405|||http://purl.uniprot.org/annotation/VAR_004406|||http://purl.uniprot.org/annotation/VAR_011614|||http://purl.uniprot.org/annotation/VAR_011615|||http://purl.uniprot.org/annotation/VAR_014723|||http://purl.uniprot.org/annotation/VAR_051574|||http://purl.uniprot.org/annotation/VSP_042629|||http://purl.uniprot.org/annotation/VSP_045370
http://togogenome.org/gene/9606:SCRIB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0G2JNZ2|||http://purl.uniprot.org/uniprot/A0A0G2JPP5|||http://purl.uniprot.org/uniprot/A0PJK8|||http://purl.uniprot.org/uniprot/Q14160                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Alters interaction with LPP.|||Basic and acidic residues|||Decreased palmitoylation. Loss of localization at the plasma membrane. Loss of targeting to cell-cell junctions. Alters interaction with TJP2. Loss of pro-apoptotic function. Loss of function in epithelial cell polarization and signaling pathways regulation.|||Disordered|||In NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane.|||In isoform 2.|||In isoform 3.|||Interaction with ARHGEF7|||Interaction with tick-borne encephalitis virus RNA-directed RNA polymerase NS5|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 16|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of anti-proliferative activity.|||Loss of interaction with LPP and TRIP6.|||Loss of palmitoylation. Loss of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-10.|||Loss of palmitoylation. Loss of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-4.|||No effect on palmitoylation.|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein scribble homolog|||Sufficient for targeting to adherens junction and to inhibit cell proliferation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000188303|||http://purl.uniprot.org/annotation/VAR_019429|||http://purl.uniprot.org/annotation/VAR_067219|||http://purl.uniprot.org/annotation/VAR_067220|||http://purl.uniprot.org/annotation/VSP_010906|||http://purl.uniprot.org/annotation/VSP_010908
http://togogenome.org/gene/9606:EZHIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A515VFR0|||http://purl.uniprot.org/uniprot/Q86X51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with the PRC2 complex and causes increased H3K27me3 levels.|||Acts as a substrate of the PRC2/EED-EZH2 complex and does not reduce H3K27me3 levels.|||Basic and acidic residues|||Decreases inhibition of H3K27me3.|||Disordered|||Does not act as a substrate of the PRC2/EED-EZH2 complex.|||Does not affect inhibition of H3K27me3 levels.|||Does not inhibit PRC2/EED-EZH2 complex activity and abolishes ability to decrease H3K27me3 levels.|||Does not reduce H3K27me3 levels.|||EZH inhibitory protein|||Necessary and sufficient for inhibition of PRC2/EED-EZH1 and PRC2/EED-EZH2 complex activity|||No effect on H3K27me3 levels.|||Phosphoserine|||Polar residues|||Pro residues|||Slightly decreases inhibition of H3K27me3.|||Sufficient for interaction with EZH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319058|||http://purl.uniprot.org/annotation/VAR_038938
http://togogenome.org/gene/9606:DUS3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RDV7|||http://purl.uniprot.org/uniprot/Q96G46                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished synthesis of dihydrouridine.|||Basic and acidic residues|||C3H1-type|||C3H1-type 1|||C3H1-type 2|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton donor|||Removed|||tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247342|||http://purl.uniprot.org/annotation/VAR_027092|||http://purl.uniprot.org/annotation/VAR_027093|||http://purl.uniprot.org/annotation/VSP_019970|||http://purl.uniprot.org/annotation/VSP_019971|||http://purl.uniprot.org/annotation/VSP_019972
http://togogenome.org/gene/9606:ZNF16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17020                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Necessary for transcription activation|||Required for nuclear localization|||Zinc finger protein 16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047338|||http://purl.uniprot.org/annotation/VAR_024193|||http://purl.uniprot.org/annotation/VAR_024194
http://togogenome.org/gene/9606:C16orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Uncharacterized protein C16orf96                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345628
http://togogenome.org/gene/9606:PABIR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX07|||http://purl.uniprot.org/uniprot/Q96E09                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Loss of phosphorylation and interaction with 14-3-3 proteins. Enhanced interaction with PPP2R2A.|||PPP2R1A-PPP2R2A-interacting phosphatase regulator 1|||Phosphoserine|||Phosphoserine; by CHEK1|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089689
http://togogenome.org/gene/9606:SPAG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0Z4G5|||http://purl.uniprot.org/uniprot/Q9NPE6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||SUN|||Sperm-associated antigen 4 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218916
http://togogenome.org/gene/9606:PRLHR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5JUU5|||http://purl.uniprot.org/uniprot/P49683                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes binding to GRIP1 and PICK1.|||Abolishes binding to GRIP1.|||Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||No effect on binding to GRIP1.|||Prolactin-releasing peptide receptor|||Required for interaction with GRIP1, GRIP2 and PICK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069524|||http://purl.uniprot.org/annotation/VAR_023948|||http://purl.uniprot.org/annotation/VAR_029746
http://togogenome.org/gene/9606:CSAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1W2PQG5                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Region                                                                                  ^@                                                                                  Disordered                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:YIPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZM5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Protein YIPF3|||Protein YIPF3, 36 kDa form III|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244446|||http://purl.uniprot.org/annotation/PRO_0000418216|||http://purl.uniprot.org/annotation/VAR_026906
http://togogenome.org/gene/9606:EGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18146|||http://purl.uniprot.org/uniprot/Q546S1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Early growth response protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with DNA|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047109|||http://purl.uniprot.org/annotation/VAR_029330|||http://purl.uniprot.org/annotation/VAR_029331|||http://purl.uniprot.org/annotation/VAR_029332|||http://purl.uniprot.org/annotation/VAR_052712
http://togogenome.org/gene/9606:ZNF426                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EME3|||http://purl.uniprot.org/uniprot/K7ER43|||http://purl.uniprot.org/uniprot/Q59EH4|||http://purl.uniprot.org/uniprot/Q9BUY5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 426                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047576|||http://purl.uniprot.org/annotation/VAR_024214|||http://purl.uniprot.org/annotation/VAR_052824
http://togogenome.org/gene/9606:HOXD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35453                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D13|||In BDE1 and BDD.|||In BDE1; decreases the transcriptional activator activity.|||In BDSD; does not affect capacity to transactivate EPHA7 promoter.|||In BDSDO.|||In SDTY5; impairs capacity to transactivate EPHA7 promoter.|||In SPD1.|||In SPD1; decreases the transcriptional activator activity.|||In SPD1; disrupts interaction with DNA.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200244|||http://purl.uniprot.org/annotation/VAR_003818|||http://purl.uniprot.org/annotation/VAR_015952|||http://purl.uniprot.org/annotation/VAR_015953|||http://purl.uniprot.org/annotation/VAR_031648|||http://purl.uniprot.org/annotation/VAR_031649|||http://purl.uniprot.org/annotation/VAR_031650|||http://purl.uniprot.org/annotation/VAR_031651|||http://purl.uniprot.org/annotation/VAR_031652|||http://purl.uniprot.org/annotation/VAR_075400|||http://purl.uniprot.org/annotation/VAR_076833|||http://purl.uniprot.org/annotation/VAR_076834|||http://purl.uniprot.org/annotation/VAR_076835
http://togogenome.org/gene/9606:FBLN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8S0LWY1|||http://purl.uniprot.org/uniprot/P23142|||http://purl.uniprot.org/uniprot/Q8NBH6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Anaphylatoxin-like|||Anaphylatoxin-like 1|||Anaphylatoxin-like 2|||Anaphylatoxin-like 3|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibulin-1|||Found in a family with syndactyly, undescended testes, delayed motor milestones, intellectual disability and signs of brain atrophy; unknown pathological significance.|||In isoform A.|||In isoform B.|||In isoform C.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Self-association and FN1-binding; calcium is necessary for homotypic binding, but not for heterotypic binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007563|||http://purl.uniprot.org/annotation/PRO_5035908824|||http://purl.uniprot.org/annotation/VAR_015650|||http://purl.uniprot.org/annotation/VAR_055720|||http://purl.uniprot.org/annotation/VAR_055721|||http://purl.uniprot.org/annotation/VAR_072739|||http://purl.uniprot.org/annotation/VSP_001383|||http://purl.uniprot.org/annotation/VSP_001384|||http://purl.uniprot.org/annotation/VSP_001385
http://togogenome.org/gene/9606:CCDC27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M243                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Coiled-coil domain-containing protein 27|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234020|||http://purl.uniprot.org/annotation/VAR_026159|||http://purl.uniprot.org/annotation/VAR_026160|||http://purl.uniprot.org/annotation/VAR_026161|||http://purl.uniprot.org/annotation/VAR_056777
http://togogenome.org/gene/9606:CDO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16878                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-(S-cysteinyl)-tyrosine (Cys-Tyr)|||Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%.|||Cysteine dioxygenase type 1|||In a colorectal cancer sample; somatic mutation.|||Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%.|||Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation.|||Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206606|||http://purl.uniprot.org/annotation/VAR_023536|||http://purl.uniprot.org/annotation/VAR_036170
http://togogenome.org/gene/9606:ZNF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21506|||http://purl.uniprot.org/uniprot/Q9UG14                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047332|||http://purl.uniprot.org/annotation/VAR_052746
http://togogenome.org/gene/9606:WNT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2E5|||http://purl.uniprot.org/uniprot/Q9Y6F9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Region|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||N-linked (GlcNAc...) asparagine|||O-palmitoleoyl serine; by PORCN|||Pro residues|||Protein Wnt|||Protein Wnt-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041440|||http://purl.uniprot.org/annotation/PRO_5004311166
http://togogenome.org/gene/9606:PACSIN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKS6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-BAR|||Phosphoserine|||Phosphothreonine|||Protein kinase C and casein kinase substrate in neurons protein 3|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161800|||http://purl.uniprot.org/annotation/VAR_053556
http://togogenome.org/gene/9606:GNAO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09471|||http://purl.uniprot.org/uniprot/Q6AWC5                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-glutamyl histamine|||ADP-ribosylarginine; by cholera toxin|||ADP-ribosylcysteine; by pertussis toxin|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(o) subunit alpha|||In DEE17 and NEDIM.|||In DEE17; loss of GTP binding; decreased interaction with RGS19; decreased interaction with heterodimers formed by GNB1 and GNG3; strongly decreased localization to cell membrane.|||In DEE17; somatic mosaic mutation; the mutant protein has some abnormal cytoplasmic localization.|||In DEE17; the mutant protein accumulates in the cytoplasmic compartment; increased basal calcium-current density compared to wild-type.|||In DEE17; the mutant protein has some abnormal cytoplasmic localization.|||In DEE17; the mutant protein localizes normally to the cell periphery.|||In NEDIM.|||In isoform Alpha-2.|||N-myristoyl glycine|||Probable disease-associated variant found in a patient with intractable early-onset epilepsy.|||Probable disease-associated variant found in a patient with intractable early-onset epilepsy; loss of GTP binding; decreased interaction with RGS19; decreased interaction with heterodimers formed by GNB1 and GNG3; strongly decreased localization to cell membrane.|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203702|||http://purl.uniprot.org/annotation/VAR_070864|||http://purl.uniprot.org/annotation/VAR_070865|||http://purl.uniprot.org/annotation/VAR_070866|||http://purl.uniprot.org/annotation/VAR_070867|||http://purl.uniprot.org/annotation/VAR_075416|||http://purl.uniprot.org/annotation/VAR_077337|||http://purl.uniprot.org/annotation/VAR_077338|||http://purl.uniprot.org/annotation/VAR_077339|||http://purl.uniprot.org/annotation/VAR_079278|||http://purl.uniprot.org/annotation/VAR_079279|||http://purl.uniprot.org/annotation/VAR_079280|||http://purl.uniprot.org/annotation/VAR_079281|||http://purl.uniprot.org/annotation/VAR_079282|||http://purl.uniprot.org/annotation/VAR_079283|||http://purl.uniprot.org/annotation/VAR_087220|||http://purl.uniprot.org/annotation/VAR_087221|||http://purl.uniprot.org/annotation/VAR_087222|||http://purl.uniprot.org/annotation/VSP_031250
http://togogenome.org/gene/9606:LOXHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7T7|||http://purl.uniprot.org/uniprot/F5GZB4|||http://purl.uniprot.org/uniprot/J3QKX9|||http://purl.uniprot.org/uniprot/Q8IVV2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 4.|||Lipoxygenase homology domain-containing protein 1|||PLAT|||PLAT 1|||PLAT 10|||PLAT 11|||PLAT 12|||PLAT 13|||PLAT 14|||PLAT 15|||PLAT 2|||PLAT 3|||PLAT 4|||PLAT 5|||PLAT 6|||PLAT 7|||PLAT 8|||PLAT 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308256|||http://purl.uniprot.org/annotation/VAR_056923|||http://purl.uniprot.org/annotation/VAR_056924|||http://purl.uniprot.org/annotation/VAR_056925|||http://purl.uniprot.org/annotation/VAR_056926|||http://purl.uniprot.org/annotation/VAR_056927|||http://purl.uniprot.org/annotation/VAR_056928|||http://purl.uniprot.org/annotation/VAR_056929|||http://purl.uniprot.org/annotation/VSP_028947|||http://purl.uniprot.org/annotation/VSP_059671|||http://purl.uniprot.org/annotation/VSP_059672|||http://purl.uniprot.org/annotation/VSP_059673|||http://purl.uniprot.org/annotation/VSP_059674
http://togogenome.org/gene/9606:SARNP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82979                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed|||SAP|||SAP domain-containing ribonucleoprotein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083916
http://togogenome.org/gene/9606:EXOC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYI6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Exocyst complex component 8|||Found in a patient with Joubert syndrome; unknown pathological significance.|||PH|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227550|||http://purl.uniprot.org/annotation/VAR_082196
http://togogenome.org/gene/9606:CEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSX9|||http://purl.uniprot.org/uniprot/O75612|||http://purl.uniprot.org/uniprot/Q86SR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Signal Peptide                                                                                  ^@                                                                                  Carboxylesterase type B|||Disordered|||Mucin-like|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5007323512
http://togogenome.org/gene/9606:TMEM106B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NUM4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Decreased number of infected cells by SARS-CoV-2. No effect on infection with HCoV-229E.|||Disordered|||Helical|||Highly decreased number of infected cells by SARS-CoV-2. No effect on infection with HCoV-229E.|||In HLD16.|||Lumenal|||N-linked (GlcNAc...) asparagine|||N-myristoyl glycine|||Phosphoserine|||Removed|||Transmembrane protein 106B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000242650|||http://purl.uniprot.org/annotation/VAR_026849|||http://purl.uniprot.org/annotation/VAR_081068
http://togogenome.org/gene/9606:ABCA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWZ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family A member 10|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253572|||http://purl.uniprot.org/annotation/VAR_028384|||http://purl.uniprot.org/annotation/VAR_028385|||http://purl.uniprot.org/annotation/VAR_028386|||http://purl.uniprot.org/annotation/VAR_055469|||http://purl.uniprot.org/annotation/VSP_021061|||http://purl.uniprot.org/annotation/VSP_021062|||http://purl.uniprot.org/annotation/VSP_021063|||http://purl.uniprot.org/annotation/VSP_021064|||http://purl.uniprot.org/annotation/VSP_021065|||http://purl.uniprot.org/annotation/VSP_021066|||http://purl.uniprot.org/annotation/VSP_021067
http://togogenome.org/gene/9606:RPS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46783                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes monoubiquitination by ZNF598, leading to enhanced readthrough on the poly(A)-stall sequences.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Omega-N-methylarginine|||Phosphoserine|||Phosphotyrosine|||Small ribosomal subunit protein eS10|||Symmetric dimethylarginine|||Weakly methylated. Complete loss of methylation; inefficient assembly into ribosomes; instability; increased degradation by the proteasomal pathway; decreased interaction with NPM1; absence of localization in the granular component (GC) region of the nucleolus; when associated with K-158.|||Weakly methylated. Complete loss of methylation; inefficient assembly into ribosomes; instability; increased degradation by the proteasomal pathway; decreased interaction with NPM1; absence of localization in the granular component (GC) region of the nucleolus; when associated with K-160.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000116360
http://togogenome.org/gene/9606:BRS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32247                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Bombesin receptor subtype-3|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069196|||http://purl.uniprot.org/annotation/VAR_011844|||http://purl.uniprot.org/annotation/VAR_011845
http://togogenome.org/gene/9606:MYCBP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99417                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Removed|||c-Myc-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220980
http://togogenome.org/gene/9606:PRCC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z456|||http://purl.uniprot.org/uniprot/Q92733|||http://purl.uniprot.org/uniprot/Q96FT4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Mediates interaction with MAD2L2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Proline-rich protein PRCC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058568|||http://purl.uniprot.org/annotation/VAR_024341
http://togogenome.org/gene/9606:AKT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y243                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment.|||2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment.|||67% decrease of activity after pervanadate treatment.|||AGC-kinase C-terminal|||Disordered|||In MPPH2 and melanoma; results in activation of AKT.|||In MPPH2.|||In MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome.|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||N-acetylserine|||No activation after pervanadate treatment.|||No effect.|||O-linked (GlcNAc) threonine|||PH|||Phosphoserine; by PKC/PRKCZ|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Protein kinase|||Proton acceptor|||RAC-gamma serine/threonine-protein kinase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085611|||http://purl.uniprot.org/annotation/VAR_040358|||http://purl.uniprot.org/annotation/VAR_065830|||http://purl.uniprot.org/annotation/VAR_069260|||http://purl.uniprot.org/annotation/VAR_069261|||http://purl.uniprot.org/annotation/VSP_004947
http://togogenome.org/gene/9606:GUCY2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25092                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Guanylate cyclase|||Guanylyl cyclase C|||Helical|||In DIAR6; activating mutation; exposure of the mutant receptor to its ligands results in markedly increased production of cyclic guanosine monophosphate.|||In MECIL; activation of guanylate cyclase activity is 60% lower than in wild-type.|||In a metastatic melanoma sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Not glycosylated|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012376|||http://purl.uniprot.org/annotation/VAR_042221|||http://purl.uniprot.org/annotation/VAR_042222|||http://purl.uniprot.org/annotation/VAR_042223|||http://purl.uniprot.org/annotation/VAR_042224|||http://purl.uniprot.org/annotation/VAR_042225|||http://purl.uniprot.org/annotation/VAR_042226|||http://purl.uniprot.org/annotation/VAR_042227|||http://purl.uniprot.org/annotation/VAR_042228|||http://purl.uniprot.org/annotation/VAR_049253|||http://purl.uniprot.org/annotation/VAR_067724|||http://purl.uniprot.org/annotation/VAR_068174
http://togogenome.org/gene/9606:CSGALNACT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5F5|||http://purl.uniprot.org/uniprot/A0A0S2Z5F9|||http://purl.uniprot.org/uniprot/A0A0S2Z5K4|||http://purl.uniprot.org/uniprot/Q8N6G5                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Glycosylation Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate N-acetylgalactosaminyltransferase 2|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189566|||http://purl.uniprot.org/annotation/VAR_048715|||http://purl.uniprot.org/annotation/VAR_048716|||http://purl.uniprot.org/annotation/VSP_012729|||http://purl.uniprot.org/annotation/VSP_012730
http://togogenome.org/gene/9606:UBALD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EM88|||http://purl.uniprot.org/uniprot/Q8TB05                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Pro residues|||UBA-like domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236079|||http://purl.uniprot.org/annotation/VSP_018573
http://togogenome.org/gene/9606:AQP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YK62|||http://purl.uniprot.org/uniprot/O43315                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Motif|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-9|||Cytoplasmic|||Discontinuously helical|||Extracellular|||Helical|||NPA 1|||NPA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063964|||http://purl.uniprot.org/annotation/VAR_024538
http://togogenome.org/gene/9606:LEPROT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0N2|||http://purl.uniprot.org/uniprot/O15243                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Leptin receptor gene-related protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215194
http://togogenome.org/gene/9606:MRLN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DMT0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Myoregulin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000432708
http://togogenome.org/gene/9606:HCN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3Q4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In EIG18; associated with disease susceptibility; alters the channel kinetics by causing a leftward shift in the voltage dependence of the channel activation curve; neurons expressing mutant channels present lower current thresholds to firing and higher firing rates.|||In SSS2.|||In SSS2; results in a significant reduction of current density compared to wild-type.|||In SSS2; results in decreased affinity for cAMP but does not abolish channel activation; shifts the current activation range to hyperpolarized voltages; slows channel opening and speeds up channel closure.|||Involved in subunit assembly|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054117|||http://purl.uniprot.org/annotation/VAR_026534|||http://purl.uniprot.org/annotation/VAR_026535|||http://purl.uniprot.org/annotation/VAR_066614|||http://purl.uniprot.org/annotation/VAR_086273
http://togogenome.org/gene/9606:TMEM127                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75204                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In PCC.|||In PCC; localized diffusely within the cytoplasm.|||N-acetylmethionine|||Phosphoserine|||Transmembrane protein 127                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251718|||http://purl.uniprot.org/annotation/VAR_063595|||http://purl.uniprot.org/annotation/VAR_072273|||http://purl.uniprot.org/annotation/VAR_072274|||http://purl.uniprot.org/annotation/VAR_072275|||http://purl.uniprot.org/annotation/VAR_072276|||http://purl.uniprot.org/annotation/VAR_072277|||http://purl.uniprot.org/annotation/VAR_072278
http://togogenome.org/gene/9606:EEF2K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00418                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abrogates phosphorylation by RPS6KB1.|||Alpha-type protein kinase|||Basic and acidic residues|||Calmodulin-binding|||Decreased kinase activity.|||Disordered|||Eukaryotic elongation factor 2 kinase|||In a colorectal adenocarcinoma sample; somatic mutation.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by MAPK13 and CDK1|||Phosphoserine; by PKA|||Phosphoserine; by autocatalysis|||Phosphoserine; by autocatalysis and TRPM7|||Phosphoserine; by autocatalysis, RPS6KA1 and RPS6KB1|||Phosphothreonine; by autocatalysis|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086936|||http://purl.uniprot.org/annotation/VAR_033915|||http://purl.uniprot.org/annotation/VAR_033916|||http://purl.uniprot.org/annotation/VAR_041534|||http://purl.uniprot.org/annotation/VAR_041535|||http://purl.uniprot.org/annotation/VAR_041536|||http://purl.uniprot.org/annotation/VAR_058405
http://togogenome.org/gene/9606:DNAI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJZ8|||http://purl.uniprot.org/uniprot/Q8IWG1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||Dynein axonemal intermediate chain 3|||In isoform 2.|||WD 1|||WD 2|||WD 3|||WD 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233162|||http://purl.uniprot.org/annotation/VAR_057630|||http://purl.uniprot.org/annotation/VAR_057631|||http://purl.uniprot.org/annotation/VSP_018080
http://togogenome.org/gene/9606:INO80E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNE2|||http://purl.uniprot.org/uniprot/Q8NBZ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||INO80 complex subunit E|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234292|||http://purl.uniprot.org/annotation/VSP_055984
http://togogenome.org/gene/9606:SSX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99909                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||KRAB-related|||Phosphoserine|||Protein SSX3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181830|||http://purl.uniprot.org/annotation/VSP_042777
http://togogenome.org/gene/9606:ATP10A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60312                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Basic and acidic residues|||Cytoplasmic|||Decreases PC-flipping activity.|||Disordered|||Exoplasmic loop|||Found in a patient with autism and Parkinson's disease; unknown pathological significance.|||Helical|||Impairs PC-flipping activity.|||In isoform 2.|||Phospholipid-transporting ATPase VA|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046379|||http://purl.uniprot.org/annotation/VAR_022004|||http://purl.uniprot.org/annotation/VAR_022005|||http://purl.uniprot.org/annotation/VAR_022006|||http://purl.uniprot.org/annotation/VAR_022007|||http://purl.uniprot.org/annotation/VAR_022008|||http://purl.uniprot.org/annotation/VAR_022009|||http://purl.uniprot.org/annotation/VAR_048380|||http://purl.uniprot.org/annotation/VAR_048381|||http://purl.uniprot.org/annotation/VAR_048382|||http://purl.uniprot.org/annotation/VAR_048383|||http://purl.uniprot.org/annotation/VAR_061038|||http://purl.uniprot.org/annotation/VAR_078700|||http://purl.uniprot.org/annotation/VSP_056604|||http://purl.uniprot.org/annotation/VSP_056605
http://togogenome.org/gene/9606:ELOC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15369                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Elongin-C|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187258|||http://purl.uniprot.org/annotation/VSP_045955
http://togogenome.org/gene/9606:CAMTA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L3W6|||http://purl.uniprot.org/uniprot/O94983                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||CG-1|||Calmodulin-binding transcription activator 2|||Disordered|||IPT/TIG|||IQ 1|||IQ 2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4 and isoform 6.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Nuclear localization signal|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235821|||http://purl.uniprot.org/annotation/VAR_026417|||http://purl.uniprot.org/annotation/VAR_026418|||http://purl.uniprot.org/annotation/VSP_018489|||http://purl.uniprot.org/annotation/VSP_018490|||http://purl.uniprot.org/annotation/VSP_018491|||http://purl.uniprot.org/annotation/VSP_018492|||http://purl.uniprot.org/annotation/VSP_018493|||http://purl.uniprot.org/annotation/VSP_046059
http://togogenome.org/gene/9606:ST3GAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q11201                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1|||Cytoplasmic|||Decreases the affinity and the catalytic efficiency for both donor and acceptor substrates.|||Decreases the affinity and the specific activity for both donor and acceptor substrates. Decreases the catalytic efficiency for the donor and acceptor substrates by 17- and 32-fold, respectively.|||Decreases the affinity for the donor and acceptor substrates by 4.5- and 4-fold, respectively. Almost no change in specific activity.|||Decreases the catalytic efficiency for the donor and acceptor substrates by 2- and 12-fold, respectively.|||Decreases the catalytic efficiency for the donor and acceptor substrates by 2.5- and 35-fold, respectively.|||Decreases the catalytic efficiency for the donor and acceptor substrates by 5- and 70-fold, respectively.|||Drastic decrease of the catalytic efficiency for both donor and acceptor substrates by 44- and 115-fold, respectively.|||Drastic decrease of the catalytic efficiency for both donor and acceptor substrates by 67- and 344-fold, respectively. Does not change the enzyme regioselectivity.|||Has no effect on the catalytic efficiency; when associated with S-59.|||Has no effect on the catalytic efficiency; when associated with S-64.|||Helical; Signal-anchor for type II membrane protein|||Loss of the catalytic activity; when associated with S-139.|||Loss of the catalytic activity; when associated with S-142.|||Loss of the catalytic activity; when associated with S-281.|||Loss of the catalytic activity; when associated with S-61.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149253|||http://purl.uniprot.org/annotation/VAR_049225
http://togogenome.org/gene/9606:LRRTM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86VH5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane neuronal protein 3|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018355|||http://purl.uniprot.org/annotation/VSP_014189|||http://purl.uniprot.org/annotation/VSP_014190
http://togogenome.org/gene/9606:ALPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05186                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolished alkaline phosphatase activity.|||Alkaline phosphatase, tissue-nonspecific isozyme|||GPI-anchor amidated serine|||In HOPS and HPPC; moderate allele; normal alkaline phosphatase activity toward diphosphate and increased activity toward pyridoxal 5'-phosphate.|||In HOPS and HPPC; severe allele; abolished alkaline phosphatase activity.|||In HOPS and HPPI.|||In HOPS.|||In HOPS; 0.4% of alkaline phosphatase activity; severe allele; no effect on subcellular location; fails to assemble into dimeric structure; dominant negative effect.|||In HOPS; 1% of activity.|||In HOPS; 1.3% of wild-type activity.|||In HOPS; 15% of activity.|||In HOPS; 16% alkaline of phosphatase activity.|||In HOPS; 2% of activity.|||In HOPS; 30% of alkaline phosphatase activity.|||In HOPS; 4% of activity.|||In HOPS; 4% of wild-type activity.|||In HOPS; 6.8% of wild-type activity.|||In HOPS; 8.5% of wild-type activity.|||In HOPS; 9% of activity.|||In HOPS; abolished alkaline phosphatase activity.|||In HOPS; absence of residual enzymatic activity.|||In HOPS; dominant-negative mutant; abolished alkaline phosphatase activity.|||In HOPS; in a patient carrying also K-291.|||In HOPS; lethal form; benign variant.|||In HOPS; loss of activity.|||In HOPS; loss of alkaline phosphatase activity.|||In HOPS; moderate; 27% of activity.|||In HOPS; moderate; 33% of activity.|||In HOPS; moderate; 4-10% of alkaline phosphatase activity.|||In HOPS; moderate; 8% of activity.|||In HOPS; moderate; frequent mutation in European countries; slightly reduced alkaline phosphatase activity.|||In HOPS; odonto.|||In HOPS; odonto; abolished alkaline phosphatase activity.|||In HOPS; odonto; partial loss of activity.|||In HOPS; odonto; slightly reduced alkaline phosphatase activity.|||In HOPS; partial loss of activity.|||In HOPS; reduced alkaline phosphatase activity toward diphosphate and pyridoxal 5'-phosphate.|||In HOPS; reduced alkaline phosphatase toward diphosphate and pyridoxal 5'-phosphate.|||In HOPS; reduces alkaline phosphatase activity.|||In HOPS; requires 2 nucleotide substitutions.|||In HOPS; severe; 1% of activity.|||In HOPS; severe; 2% of activity.|||In HOPS; severe; 3.5% of activity.|||In HOPS; severe; 4% of activity.|||In HOPS; strongly reduced alkaline phosphatase activity.|||In HOPS; unknown pathological significance.|||In HOPS; very low alkaline phosphatase activity; does not affect subcellular location.|||In HOPS; very low alkaline phosphatase activity; does not affect subcellular location; fails to assemble into dimeric structure.|||In HOPS; weak alkaline phosphatase activity.|||In HOPS; weak alkaline phosphatase activity; severely affects homodimerization; reduced cell surface expression.|||In HPPC and HOPS; severe allele; loss of alkaline phosphatase activity.|||In HPPC; severe allele.|||In HPPI and HOPS; strongly reduced alkaline phosphatase activity.|||In HPPI.|||In HPPI; 7% of activity.|||In HPPI; does not affect alkaline phosphatase activity.|||In HPPI; partial loss of activity.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine intermediate|||Reduced alkaline phosphatase activity.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024023|||http://purl.uniprot.org/annotation/PRO_0000024024|||http://purl.uniprot.org/annotation/VAR_006147|||http://purl.uniprot.org/annotation/VAR_006148|||http://purl.uniprot.org/annotation/VAR_006149|||http://purl.uniprot.org/annotation/VAR_006150|||http://purl.uniprot.org/annotation/VAR_006151|||http://purl.uniprot.org/annotation/VAR_006152|||http://purl.uniprot.org/annotation/VAR_006153|||http://purl.uniprot.org/annotation/VAR_006154|||http://purl.uniprot.org/annotation/VAR_006155|||http://purl.uniprot.org/annotation/VAR_006156|||http://purl.uniprot.org/annotation/VAR_006157|||http://purl.uniprot.org/annotation/VAR_006158|||http://purl.uniprot.org/annotation/VAR_006159|||http://purl.uniprot.org/annotation/VAR_006160|||http://purl.uniprot.org/annotation/VAR_006161|||http://purl.uniprot.org/annotation/VAR_006162|||http://purl.uniprot.org/annotation/VAR_006163|||http://purl.uniprot.org/annotation/VAR_006164|||http://purl.uniprot.org/annotation/VAR_006165|||http://purl.uniprot.org/annotation/VAR_006166|||http://purl.uniprot.org/annotation/VAR_006167|||http://purl.uniprot.org/annotation/VAR_006168|||http://purl.uniprot.org/annotation/VAR_006169|||http://purl.uniprot.org/annotation/VAR_006170|||http://purl.uniprot.org/annotation/VAR_011081|||http://purl.uniprot.org/annotation/VAR_011082|||http://purl.uniprot.org/annotation/VAR_011083|||http://purl.uniprot.org/annotation/VAR_011084|||http://purl.uniprot.org/annotation/VAR_011085|||http://purl.uniprot.org/annotation/VAR_011086|||http://purl.uniprot.org/annotation/VAR_011087|||http://purl.uniprot.org/annotation/VAR_011088|||http://purl.uniprot.org/annotation/VAR_011089|||http://purl.uniprot.org/annotation/VAR_011090|||http://purl.uniprot.org/annotation/VAR_011091|||http://purl.uniprot.org/annotation/VAR_011092|||http://purl.uniprot.org/annotation/VAR_011093|||http://purl.uniprot.org/annotation/VAR_011094|||http://purl.uniprot.org/annotation/VAR_013146|||http://purl.uniprot.org/annotation/VAR_013972|||http://purl.uniprot.org/annotation/VAR_013973|||http://purl.uniprot.org/annotation/VAR_013974|||http://purl.uniprot.org/annotation/VAR_013975|||http://purl.uniprot.org/annotation/VAR_013976|||http://purl.uniprot.org/annotation/VAR_013977|||http://purl.uniprot.org/annotation/VAR_013978|||http://purl.uniprot.org/annotation/VAR_013979|||http://purl.uniprot.org/annotation/VAR_013980|||http://purl.uniprot.org/annotation/VAR_013981|||http://purl.uniprot.org/annotation/VAR_013982|||http://purl.uniprot.org/annotation/VAR_013983|||http://purl.uniprot.org/annotation/VAR_013984|||http://purl.uniprot.org/annotation/VAR_013985|||http://purl.uniprot.org/annotation/VAR_013986|||http://purl.uniprot.org/annotation/VAR_013987|||http://purl.uniprot.org/annotation/VAR_013988|||http://purl.uniprot.org/annotation/VAR_013989|||http://purl.uniprot.org/annotation/VAR_013990|||http://purl.uniprot.org/annotation/VAR_013991|||http://purl.uniprot.org/annotation/VAR_013992|||http://purl.uniprot.org/annotation/VAR_013993|||http://purl.uniprot.org/annotation/VAR_013994|||http://purl.uniprot.org/annotation/VAR_013995|||http://purl.uniprot.org/annotation/VAR_013996|||http://purl.uniprot.org/annotation/VAR_013997|||http://purl.uniprot.org/annotation/VAR_013998|||http://purl.uniprot.org/annotation/VAR_013999|||http://purl.uniprot.org/annotation/VAR_014000|||http://purl.uniprot.org/annotation/VAR_014001|||http://purl.uniprot.org/annotation/VAR_025903|||http://purl.uniprot.org/annotation/VAR_025904|||http://purl.uniprot.org/annotation/VAR_025905|||http://purl.uniprot.org/annotation/VAR_025906|||http://purl.uniprot.org/annotation/VAR_025907|||http://purl.uniprot.org/annotation/VAR_025908|||http://purl.uniprot.org/annotation/VAR_025909|||http://purl.uniprot.org/annotation/VAR_025910|||http://purl.uniprot.org/annotation/VAR_025911|||http://purl.uniprot.org/annotation/VAR_025912|||http://purl.uniprot.org/annotation/VAR_025913|||http://purl.uniprot.org/annotation/VAR_025914|||http://purl.uniprot.org/annotation/VAR_025915|||http://purl.uniprot.org/annotation/VAR_025916|||http://purl.uniprot.org/annotation/VAR_025917|||http://purl.uniprot.org/annotation/VAR_025918|||http://purl.uniprot.org/annotation/VAR_025919|||http://purl.uniprot.org/annotation/VAR_025920|||http://purl.uniprot.org/annotation/VAR_025921|||http://purl.uniprot.org/annotation/VAR_025922|||http://purl.uniprot.org/annotation/VAR_025923|||http://purl.uniprot.org/annotation/VAR_025924|||http://purl.uniprot.org/annotation/VAR_025925|||http://purl.uniprot.org/annotation/VAR_025926|||http://purl.uniprot.org/annotation/VAR_025927|||http://purl.uniprot.org/annotation/VAR_025928|||http://purl.uniprot.org/annotation/VAR_025929|||http://purl.uniprot.org/annotation/VAR_025930|||http://purl.uniprot.org/annotation/VAR_025931|||http://purl.uniprot.org/annotation/VAR_025932|||http://purl.uniprot.org/annotation/VAR_025933|||http://purl.uniprot.org/annotation/VAR_025934|||http://purl.uniprot.org/annotation/VAR_025935|||http://purl.uniprot.org/annotation/VAR_025936|||http://purl.uniprot.org/annotation/VAR_025937|||http://purl.uniprot.org/annotation/VAR_025938|||http://purl.uniprot.org/annotation/VAR_025939|||http://purl.uniprot.org/annotation/VAR_025940|||http://purl.uniprot.org/annotation/VAR_075557|||http://purl.uniprot.org/annotation/VAR_075558|||http://purl.uniprot.org/annotation/VAR_075559|||http://purl.uniprot.org/annotation/VAR_075560|||http://purl.uniprot.org/annotation/VAR_075561|||http://purl.uniprot.org/annotation/VAR_085155|||http://purl.uniprot.org/annotation/VAR_085156|||http://purl.uniprot.org/annotation/VAR_085157|||http://purl.uniprot.org/annotation/VAR_085158|||http://purl.uniprot.org/annotation/VAR_085159|||http://purl.uniprot.org/annotation/VSP_042711|||http://purl.uniprot.org/annotation/VSP_044228
http://togogenome.org/gene/9606:LCT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09848                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Glycosyl hydrolase-1 1; Region I|||Glycosyl hydrolase-1 2; Region II|||Glycosyl hydrolase-1 3; Region III. Phlorizin hydrolase/glycosylceramidase activity|||Glycosyl hydrolase-1 4; Region IV. Lactase activity|||Helical|||In COLACD.|||Lactase/phlorizin hydrolase|||Loss of lactase activity. No effect on phlorizin hydrolase activity. No effect on localization to the plasma membrane.|||N-linked (GlcNAc...) asparagine|||No effect on lactase activity. Decreased phlorizin hydrolase activity. No effect on localization to the plasma membrane.|||Nucleophile; for lactase activity|||Nucleophile; for phlorizin hydrolase/Glycosylceramidase activity|||Proton donor; for lactase activity|||Proton donor; for phlorizin hydrolase/Glycosylceramidase activity|||Required for homodimerization and transport to the plasma membrane|||XBetaGly                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011767|||http://purl.uniprot.org/annotation/PRO_0000011768|||http://purl.uniprot.org/annotation/VAR_026705|||http://purl.uniprot.org/annotation/VAR_026706|||http://purl.uniprot.org/annotation/VAR_026707|||http://purl.uniprot.org/annotation/VAR_026708|||http://purl.uniprot.org/annotation/VAR_026709|||http://purl.uniprot.org/annotation/VAR_055882|||http://purl.uniprot.org/annotation/VAR_055883
http://togogenome.org/gene/9606:SHKBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBC3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BTB|||Disordered|||In isoform 2.|||N-acetylalanine|||PXXXPR|||PXXXPW|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||SH3KBP1-binding protein 1|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307932|||http://purl.uniprot.org/annotation/VAR_036714|||http://purl.uniprot.org/annotation/VSP_028873|||http://purl.uniprot.org/annotation/VSP_028874
http://togogenome.org/gene/9606:FOXO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A856PRE8|||http://purl.uniprot.org/uniprot/O43524                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes YWHAZ-binding; when associated with A-253. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-253 and A-315.|||Abolishes YWHAZ-binding; when associated with A-32. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-315.|||Abolishes phosphorylation. Loss of localization to the mitochondrion outer membrane and loss of translocation into the mitochondrion following metabolic stress.|||Acidic residues|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-179; A-399; A-413; A-555 and A-588.|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-179; A-399; A-413; A-555 and A-626.|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-179; A-399; A-413; A-588 and A-626.|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-179; A-399; A-555; A-588 and A-626.|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-179; A-413; A-555; A-588 and A-626.|||Decreased phosphorylation by AMPK and impaired ability to transactivate a reporter gene; when associated with A-399; A-413; A-555; A-588 and A-626.|||Decreases DNA affinity.|||Disordered|||FOXO protein KIX-binding|||FOXO protein transactivation|||Fork-head|||Forkhead box protein O3|||Impairs nuclear translocation upon oxidative stress.|||In isoform 2.|||In normal cells, no defect in mitochondrion import following metabolic stress. In cancer cells, defective mitochondrion import following metabolic stress and abolition of ERK-mediated phosphorylation.|||Loss of localization to the mitochondrion outer membrane and loss of translocation into the mitochondrion following metabolic stress.|||Loss of nuclear import.|||Loss of phosphorylation by IKKB.|||Loss of translocation into the mitochondrion following metabolic stress.|||Mediates interaction with CHUK/IKKA and IKBKB/IKKB|||Methylation levels similar to wild-type; when associated with Arg-269.|||Methylation levels similar to wild-type; when associated with Arg-270.|||Methylation levels strongly reduced.|||N6-acetyllysine|||N6-methyllysine|||No effect on YWHAZ-binding. Promotes nuclear translocation. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-253.|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by AMPK|||Phosphoserine; by AMPK and MAPKAPK5|||Phosphoserine; by CaMK2A|||Phosphoserine; by IKKB|||Phosphoserine; by MAPKAPK5|||Phosphoserine; by PKB/AKT1 and MAPKAPK5|||Phosphoserine; by SGK1|||Phosphoserine; by STK4/MST1|||Phosphothreonine; by AMPK|||Phosphothreonine; by PKB/AKT1|||Polar residues|||Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-290.|||Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-569.|||Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-290 and R-569.|||Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-259; R-290 and R-569.|||Required for mitochondrial import|||Slightly decreases DNA affinity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000091874|||http://purl.uniprot.org/annotation/VSP_056225
http://togogenome.org/gene/9606:PRPH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23942                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In CACD2.|||In CACD2; increased protein expression.|||In MDPT1 and RP7; also in adult-onset foveomacular dystrophy with choroidal neovascularization.|||In MDPT1.|||In MDPT1; also in cone-rod dystrophy.|||In MDPT1; butterfly-shaped.|||In MDPT1; increased protein expression.|||In RP7 and VMD3.|||In RP7 and VMD3; results in retinitis pigmentosa in combination with a null mutation of ROM1.|||In RP7.|||In RP7; also found in a patient with central areolar choroidal dystrophy.|||In RP7; decreased protein expression.|||In RP7; digenic inheritance; results in disease in combination with a null mutation of ROM1.|||In RP7; in combination with a null mutation of ROM1.|||In RP7; with bulls-eye maculopathy.|||In VMD3.|||In VMD3; increased protein expression.|||In cone-rod dystrophy.|||In some patients with macular dystrophy.|||In some patients with macular dystrophy; also in a family affected by central areolar choroidal dystrophy.|||Interaction with MREG|||Interchain (with ROM1)|||Lumenal|||N-linked (GlcNAc...) asparagine|||Peripherin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000168105|||http://purl.uniprot.org/annotation/VAR_006853|||http://purl.uniprot.org/annotation/VAR_006854|||http://purl.uniprot.org/annotation/VAR_006855|||http://purl.uniprot.org/annotation/VAR_006856|||http://purl.uniprot.org/annotation/VAR_006857|||http://purl.uniprot.org/annotation/VAR_006858|||http://purl.uniprot.org/annotation/VAR_006859|||http://purl.uniprot.org/annotation/VAR_006860|||http://purl.uniprot.org/annotation/VAR_006861|||http://purl.uniprot.org/annotation/VAR_006862|||http://purl.uniprot.org/annotation/VAR_006863|||http://purl.uniprot.org/annotation/VAR_006864|||http://purl.uniprot.org/annotation/VAR_006865|||http://purl.uniprot.org/annotation/VAR_006866|||http://purl.uniprot.org/annotation/VAR_006867|||http://purl.uniprot.org/annotation/VAR_006868|||http://purl.uniprot.org/annotation/VAR_006869|||http://purl.uniprot.org/annotation/VAR_006870|||http://purl.uniprot.org/annotation/VAR_006871|||http://purl.uniprot.org/annotation/VAR_006872|||http://purl.uniprot.org/annotation/VAR_006873|||http://purl.uniprot.org/annotation/VAR_006874|||http://purl.uniprot.org/annotation/VAR_006875|||http://purl.uniprot.org/annotation/VAR_006876|||http://purl.uniprot.org/annotation/VAR_006877|||http://purl.uniprot.org/annotation/VAR_006878|||http://purl.uniprot.org/annotation/VAR_006879|||http://purl.uniprot.org/annotation/VAR_006880|||http://purl.uniprot.org/annotation/VAR_006881|||http://purl.uniprot.org/annotation/VAR_006882|||http://purl.uniprot.org/annotation/VAR_006883|||http://purl.uniprot.org/annotation/VAR_006884|||http://purl.uniprot.org/annotation/VAR_006885|||http://purl.uniprot.org/annotation/VAR_006886|||http://purl.uniprot.org/annotation/VAR_006887|||http://purl.uniprot.org/annotation/VAR_006888|||http://purl.uniprot.org/annotation/VAR_006889|||http://purl.uniprot.org/annotation/VAR_006890|||http://purl.uniprot.org/annotation/VAR_006891|||http://purl.uniprot.org/annotation/VAR_006892|||http://purl.uniprot.org/annotation/VAR_006893|||http://purl.uniprot.org/annotation/VAR_006894|||http://purl.uniprot.org/annotation/VAR_006895|||http://purl.uniprot.org/annotation/VAR_032052|||http://purl.uniprot.org/annotation/VAR_032053|||http://purl.uniprot.org/annotation/VAR_032054|||http://purl.uniprot.org/annotation/VAR_071974|||http://purl.uniprot.org/annotation/VAR_071975|||http://purl.uniprot.org/annotation/VAR_075758|||http://purl.uniprot.org/annotation/VAR_075759|||http://purl.uniprot.org/annotation/VAR_075760|||http://purl.uniprot.org/annotation/VAR_075761|||http://purl.uniprot.org/annotation/VAR_075762|||http://purl.uniprot.org/annotation/VAR_075763|||http://purl.uniprot.org/annotation/VAR_075764|||http://purl.uniprot.org/annotation/VAR_075765|||http://purl.uniprot.org/annotation/VAR_075766|||http://purl.uniprot.org/annotation/VAR_075767|||http://purl.uniprot.org/annotation/VAR_075768
http://togogenome.org/gene/9606:MYO1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KRL0|||http://purl.uniprot.org/uniprot/J3QRN6|||http://purl.uniprot.org/uniprot/O94832|||http://purl.uniprot.org/uniprot/Q8N618                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||IQ 1|||IQ 2|||Myosin motor|||N-acetylalanine|||Phosphoserine|||Phosphotyrosine|||Removed|||TH1|||Unconventional myosin-Id                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123447|||http://purl.uniprot.org/annotation/VAR_050210|||http://purl.uniprot.org/annotation/VAR_050211
http://togogenome.org/gene/9606:IL37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZH6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In IBD31; decreased stability; increased degradation; decreased localization to the nucleus; decreased localization to the extracellular space; decreased function in regulation of inflammatory response.|||In isoform A.|||In isoform C.|||In isoform D.|||In isoform E.|||Interleukin-37|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000015335|||http://purl.uniprot.org/annotation/PRO_0000015336|||http://purl.uniprot.org/annotation/VAR_014260|||http://purl.uniprot.org/annotation/VAR_014261|||http://purl.uniprot.org/annotation/VAR_023334|||http://purl.uniprot.org/annotation/VAR_023335|||http://purl.uniprot.org/annotation/VAR_023336|||http://purl.uniprot.org/annotation/VAR_023337|||http://purl.uniprot.org/annotation/VAR_049574|||http://purl.uniprot.org/annotation/VAR_049575|||http://purl.uniprot.org/annotation/VAR_086000|||http://purl.uniprot.org/annotation/VSP_002653|||http://purl.uniprot.org/annotation/VSP_002654|||http://purl.uniprot.org/annotation/VSP_002655|||http://purl.uniprot.org/annotation/VSP_002656
http://togogenome.org/gene/9606:CDC34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49427                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-233.|||Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-231 and A-236.|||Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-222; A-233 and A-236.|||Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-203; A-231; A-233 and A-236.|||Abolishes phosphorylation by CK2. Impairs nuclear localization; when associated with A-222; A-231; A-233 and A-236.|||Complete loss of activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay.|||Decreases monoubiquitination of NFKBIA and inhibits polyubiquitination of NFKBIA.|||Decreases polyubiquitination of NFKBIA.|||Disordered|||Glycyl thioester intermediate|||Inhibits both mono and polyubiquitination of NFKBIA.|||Inhibits both mono and polyubiquitination of NFKBIA; when associated with A-112.|||Inhibits both mono andpolyubiquitination of NFKBIA; when associated with A-108.|||Inhibits polyubiquitination of NFKBIA; when associated with A-102.|||Inhibits polyubiquitination of NFKBIA; when associated with A-103.|||Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-150.|||Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-147; A-149 and A-153.|||Inhibits polyubiquitination of NFKBIA; when associated with A-143; A-149; A-150 and A-153.|||Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-147; A-150 and A-153.|||Inhibits polyubiquitination of NFKBIA; when associated with A-147; A-149; A-150 and A-153.|||Loss of RBX1-binding.|||Loss of function.|||No effect on activity, when assayed in a Sic1-SCF-cdc4 ubiquitination assay.|||Phosphoserine; by CK2|||Phosphothreonine; by CK2|||SCF-binding|||UBC core|||Ubiquitin-conjugating enzyme E2 R1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082451|||http://purl.uniprot.org/annotation/VAR_021277
http://togogenome.org/gene/9606:ZC3H12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5D1E8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes RNase activity.|||C3H1-type|||Disordered|||Does not inhibit antiviral effects.|||Endoribonuclease ZC3H12A|||Inhibits transcriptional activity; when associated with G-311.|||Inhibits transcriptional activity; when associated with G-312.|||Inhibits transcriptional activity; when associated with G-317.|||Inhibits transcriptional activity; when associated with G-318.|||Loss of interleukin IL17A mRNA instability. Reduces weakly pre-miRNARNase activity. Attenuates miRNA silencing activity. Does not inhibit binding to Japanese encephalitis virus (JEV) and dengue virus (DEN) RNAs and weakly attenuates antiviral effects. Loss of HIV-1 antiviral activity.|||Loss of pre-miRNARNase activity, IL17A mRNA instability and antiviral effects; when associated with A-225. Loss of IL1B mRNA instability; when associated with N-141.|||Loss of pre-miRNARNase activity, IL17A mRNA instability and antiviral effects; when associated with A-226.|||Loss of pre-miRNARNase activity. Attenuates strongly miRNA silencing activity. Loss of interleukin IL17A and IL6 mRNA instabilities. Reduces angiogenic differentiation. Loss of RNase activity on JEV and DEN viral RNAs and antiviral effects. Loss of HIV-1 antiviral activity. Loss of IL1B mRNA instability; when associated with A-226.|||Necessary for interaction with TANK|||Necessary for interaction with ZC3H12D|||No change in RNase activity.|||Phosphoserine|||Polar residues|||RNA binding|||RNase|||RNase NYN|||Ubiquitin association domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341512|||http://purl.uniprot.org/annotation/VAR_044082|||http://purl.uniprot.org/annotation/VAR_052968
http://togogenome.org/gene/9606:WNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PCD1|||http://purl.uniprot.org/uniprot/Q9Y3S1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase WNK2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086822|||http://purl.uniprot.org/annotation/VAR_057114|||http://purl.uniprot.org/annotation/VAR_059773|||http://purl.uniprot.org/annotation/VSP_050639|||http://purl.uniprot.org/annotation/VSP_050640|||http://purl.uniprot.org/annotation/VSP_050641|||http://purl.uniprot.org/annotation/VSP_050642|||http://purl.uniprot.org/annotation/VSP_050643|||http://purl.uniprot.org/annotation/VSP_050644|||http://purl.uniprot.org/annotation/VSP_050645|||http://purl.uniprot.org/annotation/VSP_050646|||http://purl.uniprot.org/annotation/VSP_050647
http://togogenome.org/gene/9606:FOXI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MTJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  9aaTAD|||Disordered|||Fork-head|||Forkhead box protein I3|||In CFM; decreased transcription factor activity; decreased localization to the nucleus.|||In CFM; decreased transcription factor activity; does not affect localization to the nucleus.|||In CFM; decreased transcription factor activity; localization to the nucleus but aggregating into granular foci.|||In CFM; unknown pathological significance; decreased transcription factor activity; does not affect localization to the nucleus.|||Nuclear localization signal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341225|||http://purl.uniprot.org/annotation/VAR_088275|||http://purl.uniprot.org/annotation/VAR_088276|||http://purl.uniprot.org/annotation/VAR_088277|||http://purl.uniprot.org/annotation/VAR_088278|||http://purl.uniprot.org/annotation/VAR_088279|||http://purl.uniprot.org/annotation/VAR_088280|||http://purl.uniprot.org/annotation/VAR_088281|||http://purl.uniprot.org/annotation/VAR_088282|||http://purl.uniprot.org/annotation/VAR_088283|||http://purl.uniprot.org/annotation/VAR_088284|||http://purl.uniprot.org/annotation/VAR_088285|||http://purl.uniprot.org/annotation/VAR_088286|||http://purl.uniprot.org/annotation/VAR_088287|||http://purl.uniprot.org/annotation/VAR_088288|||http://purl.uniprot.org/annotation/VAR_088289|||http://purl.uniprot.org/annotation/VAR_088290|||http://purl.uniprot.org/annotation/VAR_088291
http://togogenome.org/gene/9606:FERD3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RJ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Fer3-like protein|||In a colorectal cancer sample; somatic mutation.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328682|||http://purl.uniprot.org/annotation/VAR_042439
http://togogenome.org/gene/9606:MEF2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D8L7E9|||http://purl.uniprot.org/uniprot/Q06413                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation; when associated with A-293.|||Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation; when associated with A-300.|||Abolishes cleavage by caspase 7.|||Abolishes sumoylation.|||Abolishes sumoylation. Enhanced transcriptional activity.|||Basic and acidic residues|||Beta domain|||Cleavage|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||MADS-box|||Mef2-type|||Myocyte-specific enhancer factor 2C|||N6-acetyllysine|||No change in transactivational activation for isoforms with or without the beta domain.|||No effect on MAPK14-mediated phosphorylation. Abolishes MAPK7-mediated phosphorylation and reduces transactivation activity.|||No effect on sumoylation. No effect on transcriptional activity.|||No effect on transcriptional activation.|||Phosphoserine|||Phosphoserine; by CDK5|||Phosphoserine; by CK2|||Phosphoserine; by MAPK7|||Phosphothreonine; by MAPK14|||Polar residues|||Probable disease-associated variant found in a patient with infantile onset epileptic encephalopathy and autism spectrum disorder.|||Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239 and R-252.|||Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239 and R-264.|||Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-252 and R-264.|||Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-239; R-252 and R-264.|||Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-234; R-239; R-252 and R-262.|||Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-119; R-234; R-239; R-252 and R-262.|||Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with N-273 and N-275.|||Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Q-272 and N-273.|||Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Q-272 and N-275.|||Transcription repressor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199433|||http://purl.uniprot.org/annotation/VAR_078228|||http://purl.uniprot.org/annotation/VAR_078621|||http://purl.uniprot.org/annotation/VSP_006248|||http://purl.uniprot.org/annotation/VSP_006249|||http://purl.uniprot.org/annotation/VSP_043339|||http://purl.uniprot.org/annotation/VSP_045478|||http://purl.uniprot.org/annotation/VSP_046251
http://togogenome.org/gene/9606:DACT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYF0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with YWHAB; when associated with A-237.|||Abolishes nuclear export; when associated with A-132.|||Abolishes nuclear export; when associated with A-136.|||Basic and acidic residues|||Bipartite nuclear localization signal|||Dapper homolog 1|||Disordered|||Found in a patient with closed spina bifida; sporadic case; unknown pathological significance.|||Found in a patient with craniorachischisis; sporadic case; unknown pathological significance.|||Found in a patient with encephalocele; sporadic case; unknown pathological significance.|||Impairs interaction with YWHAB. Abolishes interaction with YWHAB; when associated with A-827.|||In NTD; does not affect interaction with DVL2; does not affect subcellular location; results in reduced RHOA and JNK activation.|||In NTD; uncertain pathological significance; does not affect interaction with DVL2; does not affect subcellular location; increases RHOA activation but decreases the ability to activate JNK.|||In TBS2; the mutant protein is stable and expressed.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Nuclear export signal|||PDZ-binding|||Partial nuclear accumulation upon LMB treatment.|||Phosphoserine; by PKA|||Polar residues|||Required for self-association                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191353|||http://purl.uniprot.org/annotation/VAR_036461|||http://purl.uniprot.org/annotation/VAR_036462|||http://purl.uniprot.org/annotation/VAR_053057|||http://purl.uniprot.org/annotation/VAR_053058|||http://purl.uniprot.org/annotation/VAR_053059|||http://purl.uniprot.org/annotation/VAR_053060|||http://purl.uniprot.org/annotation/VAR_068427|||http://purl.uniprot.org/annotation/VAR_068428|||http://purl.uniprot.org/annotation/VAR_068429|||http://purl.uniprot.org/annotation/VAR_068430|||http://purl.uniprot.org/annotation/VAR_068431|||http://purl.uniprot.org/annotation/VAR_068432|||http://purl.uniprot.org/annotation/VAR_080125|||http://purl.uniprot.org/annotation/VSP_044198
http://togogenome.org/gene/9606:OPN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHM6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2.|||Melanopsin|||N6-(retinylidene)lysine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197815|||http://purl.uniprot.org/annotation/VAR_020430|||http://purl.uniprot.org/annotation/VAR_029774|||http://purl.uniprot.org/annotation/VAR_029775|||http://purl.uniprot.org/annotation/VSP_041123
http://togogenome.org/gene/9606:KLHL35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PF15                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Splice Variant                                                                                  ^@                                                                                  BACK|||BTB|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 35                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344466|||http://purl.uniprot.org/annotation/VSP_034783|||http://purl.uniprot.org/annotation/VSP_034784|||http://purl.uniprot.org/annotation/VSP_034785
http://togogenome.org/gene/9606:NAT14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUY8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-acetyltransferase|||Probable N-acetyltransferase 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307786
http://togogenome.org/gene/9606:CLNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z7G1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cytokine-dependent hematopoietic cell linker|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with FYB1|||Mediates interaction with LAT, GRB2, and FGR; involved in translocation to the glycolipid-enriched microdomain and restoration of BCR-induced calcium response in BLNK-deficient DT40 cells expressing LAT|||Mediates interaction with PLCG1; essential for BCR signaling; involved in restoration of BCR-induced calcium response and ERK2 and JNK2 activation in BLNK-deficient cells expressing LAT|||Phosphotyrosine; by LYN|||Polar residues|||Pro residues|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314597|||http://purl.uniprot.org/annotation/VAR_037984|||http://purl.uniprot.org/annotation/VSP_030330|||http://purl.uniprot.org/annotation/VSP_030331|||http://purl.uniprot.org/annotation/VSP_030332|||http://purl.uniprot.org/annotation/VSP_030333
http://togogenome.org/gene/9606:MTF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZ69|||http://purl.uniprot.org/uniprot/B4DZG1|||http://purl.uniprot.org/uniprot/Q7Z534|||http://purl.uniprot.org/uniprot/Q9Y483                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes chromatin binding activity of the PRC2.1 complex.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Metal-response element-binding transcription factor 2|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduced chromatin binding activity of the PRC2.1 complex, probably due to loss of dimer stability.|||Tudor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059317|||http://purl.uniprot.org/annotation/VAR_054765|||http://purl.uniprot.org/annotation/VSP_004696|||http://purl.uniprot.org/annotation/VSP_040329|||http://purl.uniprot.org/annotation/VSP_053348
http://togogenome.org/gene/9606:TUBA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NY65                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Motif|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dephenylalaninated tubulin alpha-8 chain|||In MACTHC2; unknown pathological significance.|||In MACTHC2; unknown pathological significance; results in impaired TUBA8 incorporation into the microtubule network.|||In isoform 2.|||MREC motif|||Tubulin alpha-8 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048113|||http://purl.uniprot.org/annotation/PRO_0000456434|||http://purl.uniprot.org/annotation/VAR_024680|||http://purl.uniprot.org/annotation/VAR_052670|||http://purl.uniprot.org/annotation/VAR_087194|||http://purl.uniprot.org/annotation/VAR_087195|||http://purl.uniprot.org/annotation/VAR_087196|||http://purl.uniprot.org/annotation/VAR_087197|||http://purl.uniprot.org/annotation/VAR_087198|||http://purl.uniprot.org/annotation/VAR_087199|||http://purl.uniprot.org/annotation/VSP_042810
http://togogenome.org/gene/9606:ARHGAP23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXQ2|||http://purl.uniprot.org/uniprot/Q9P227                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PDZ|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rho GTPase-activating protein 23|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280471|||http://purl.uniprot.org/annotation/VSP_023708|||http://purl.uniprot.org/annotation/VSP_023709
http://togogenome.org/gene/9606:SIVA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15304                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation and apoptotic activity.|||Apoptosis regulatory protein Siva|||In isoform 2.|||Interaction with BCL2L1 isoform Bcl-x(L) and inhibition of BCL2L1 anti-apoptotic activity|||Interaction with coxsackievirus B3 VP2|||No effect on phosphorylation or apoptotic activity.|||Phosphoserine|||Phosphotyrosine; by ABL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097774|||http://purl.uniprot.org/annotation/VSP_007525
http://togogenome.org/gene/9606:AP2M1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNB9|||http://purl.uniprot.org/uniprot/E9PFW3|||http://purl.uniprot.org/uniprot/Q96CW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AP-2 complex subunit mu|||In MRD60; reduced clathrin-mediated endocytosis; no effect on clathrin-coated pit location; no effect on protein stability and membrane recruitment.|||In isoform 2.|||MHD|||Phosphoserine|||Phosphothreonine; by AAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193774|||http://purl.uniprot.org/annotation/VAR_082954|||http://purl.uniprot.org/annotation/VSP_034599
http://togogenome.org/gene/9606:ND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03886|||http://purl.uniprot.org/uniprot/U5Z754                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a patient with epileptic encephalopathy evolving to Lennox-Gastaut syndrome; unknown pathological significance.|||Helical|||In AD-MT; may be associated with disease susceptibility.|||In LHON; primary mutation; medium severity; some vision recovery; 80% reduction in rotenone-sensitive and ubiquinone-dependent electron transfer activity, whereas the proximal NADH dehydrogenase activity of the complex is unaffected.|||In LHON; secondary mutation; unknown pathological significance.|||In MELAS.|||In a patient with hypertrophic cardiomyopathy and profound hearing loss.|||Might contribute to non-insulin dependent diabetes mellitus susceptibility in some populations.|||NADH-ubiquinone oxidoreductase chain 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117414|||http://purl.uniprot.org/annotation/VAR_004747|||http://purl.uniprot.org/annotation/VAR_004748|||http://purl.uniprot.org/annotation/VAR_004749|||http://purl.uniprot.org/annotation/VAR_004750|||http://purl.uniprot.org/annotation/VAR_004751|||http://purl.uniprot.org/annotation/VAR_004752|||http://purl.uniprot.org/annotation/VAR_004753|||http://purl.uniprot.org/annotation/VAR_004754|||http://purl.uniprot.org/annotation/VAR_008587|||http://purl.uniprot.org/annotation/VAR_008588|||http://purl.uniprot.org/annotation/VAR_008589|||http://purl.uniprot.org/annotation/VAR_011346|||http://purl.uniprot.org/annotation/VAR_011347|||http://purl.uniprot.org/annotation/VAR_065195|||http://purl.uniprot.org/annotation/VAR_073352
http://togogenome.org/gene/9606:IKZF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2S9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||CTBP-binding motif PEDLA|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Interaction with FOXP3|||N6-acetyllysine|||No effect on CTBP2 interaction.|||Phosphoserine|||Polar residues|||Zinc finger protein Eos                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299468|||http://purl.uniprot.org/annotation/VSP_027688
http://togogenome.org/gene/9606:EEF1AKMT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVE0                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  EEF1A lysine methyltransferase 1|||N-acetylserine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311294|||http://purl.uniprot.org/annotation/VAR_037216
http://togogenome.org/gene/9606:ZDHHC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKD9|||http://purl.uniprot.org/uniprot/Q9UIJ5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||DHHC|||Disordered|||Helical|||In a colorectal cancer sample; somatic mutation.|||In a hepatocellular carcinoma sample; somatic mutation.|||Loss of protein-cysteine S-palmitoyltransferase activity.|||Lumenal|||Mediates localization to plasma membrane and recycling endosomes|||NPxY-like endocytic signal|||Non-canonical dileucine endocytic signal|||Palmitoyltransferase DHHC|||Palmitoyltransferase ZDHHC2|||Phosphoserine|||Polar residues|||S-palmitoyl cysteine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212859|||http://purl.uniprot.org/annotation/VAR_015229|||http://purl.uniprot.org/annotation/VAR_015230
http://togogenome.org/gene/9606:PDCD2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRP1                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Programmed cell death protein 2-like|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272645
http://togogenome.org/gene/9606:RP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Z0|||http://purl.uniprot.org/uniprot/Q8TA86                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CCHC-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In RP9.|||PIM1-binding|||Phosphoserine; by PIM1|||Retinitis pigmentosa 9 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097428|||http://purl.uniprot.org/annotation/VAR_017252|||http://purl.uniprot.org/annotation/VAR_017253|||http://purl.uniprot.org/annotation/VAR_017254
http://togogenome.org/gene/9606:BCAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GW7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Brevican core protein|||C-type lectin|||Disordered|||EGF-like|||GPI-anchor amidated alanine|||Ig-like V-type|||In isoform 2.|||Link 1|||Link 2|||N-linked (GlcNAc...) asparagine|||O-glycosylated at one site|||O-glycosylated at two sites|||O-linked (GalNAc...) serine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Phosphoserine|||Polar residues|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017511|||http://purl.uniprot.org/annotation/VAR_019551|||http://purl.uniprot.org/annotation/VAR_050123|||http://purl.uniprot.org/annotation/VSP_011184|||http://purl.uniprot.org/annotation/VSP_011185
http://togogenome.org/gene/9606:RXRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZ88|||http://purl.uniprot.org/uniprot/F1D8Q7|||http://purl.uniprot.org/uniprot/F1T097|||http://purl.uniprot.org/uniprot/P48443                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Hinge|||Modulating|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear/hormone receptor activator site AF-1|||Polar residues|||Retinoic acid receptor RXR-gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053576
http://togogenome.org/gene/9606:C2orf76                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KRA6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  UPF0538 protein C2orf76                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325824|||http://purl.uniprot.org/annotation/VAR_039931|||http://purl.uniprot.org/annotation/VAR_039932
http://togogenome.org/gene/9606:SNTA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13424                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Alpha-1-syntrophin|||Calmodulin-binding|||Disordered|||In LQT12; leads to a gain of function of the voltage dependent sodium channel.|||In LQT12; results in released inhibition of nNOS, S-nitrosylation of SCN5A and increased late sodium current.|||In isoform 2.|||PDZ|||PH 1|||PH 2|||Phosphoserine|||Polar residues|||SU                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184006|||http://purl.uniprot.org/annotation/VAR_014075|||http://purl.uniprot.org/annotation/VAR_062399|||http://purl.uniprot.org/annotation/VAR_062400|||http://purl.uniprot.org/annotation/VSP_056827
http://togogenome.org/gene/9606:PPP5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53041                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Catalytic|||Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation.|||Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1.|||Disordered|||Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6.|||Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1.|||N-acetylalanine|||No effect on interaction with HSP90AA1.|||Proton donor/acceptor|||Removed|||Required for autoinhibition|||Serine/threonine-protein phosphatase 5|||TPR 1|||TPR 2|||TPR 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058894
http://togogenome.org/gene/9606:USH1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4U9|||http://purl.uniprot.org/uniprot/A0A0S2Z4V1|||http://purl.uniprot.org/uniprot/Q9Y6N9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Harmonin|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Mediates interaction with MYO7B|||N-terminal domain|||PDZ|||PDZ 1|||PDZ 2|||PDZ 3|||Phosphoserine|||Strongly reduced affinity for USH1G.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065727|||http://purl.uniprot.org/annotation/VAR_012320|||http://purl.uniprot.org/annotation/VSP_003789|||http://purl.uniprot.org/annotation/VSP_003790|||http://purl.uniprot.org/annotation/VSP_007422|||http://purl.uniprot.org/annotation/VSP_043520|||http://purl.uniprot.org/annotation/VSP_043521
http://togogenome.org/gene/9606:CFAP96                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7E2U8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Cilia-and flagella-associated protein 96|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341950
http://togogenome.org/gene/9606:MUC21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SSG8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||28 X 15 AA approximate tandem repeats|||3|||4|||5|||6|||7|||8|||9|||Cleavage|||Cytoplasmic|||Cytoplasmic tail|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Mucin-21|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340102|||http://purl.uniprot.org/annotation/VAR_043995|||http://purl.uniprot.org/annotation/VAR_043996|||http://purl.uniprot.org/annotation/VAR_043997|||http://purl.uniprot.org/annotation/VAR_043998|||http://purl.uniprot.org/annotation/VAR_043999|||http://purl.uniprot.org/annotation/VAR_044000|||http://purl.uniprot.org/annotation/VAR_044001|||http://purl.uniprot.org/annotation/VAR_044002|||http://purl.uniprot.org/annotation/VAR_044003|||http://purl.uniprot.org/annotation/VAR_044004|||http://purl.uniprot.org/annotation/VAR_044005|||http://purl.uniprot.org/annotation/VAR_060457|||http://purl.uniprot.org/annotation/VAR_060458|||http://purl.uniprot.org/annotation/VAR_060459|||http://purl.uniprot.org/annotation/VSP_034188|||http://purl.uniprot.org/annotation/VSP_034189
http://togogenome.org/gene/9606:UBQLN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZF6|||http://purl.uniprot.org/uniprot/Q59F94|||http://purl.uniprot.org/uniprot/Q9NRR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation by ATM in response to DNA damage and impaired ability to regulate DNA repair.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In ALS; impaired proteasome efficiency leading to accumulation of CTNNB1.|||In isoform 2.|||Loss of interaction with UBQLN1.|||Phosphoserine|||Phosphoserine; by ATM|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in patients with UBQLN4 deficiency syndrome (UBDS).|||STI1 1|||STI1 2|||STI1 3|||STI1 4|||UBA|||Ubiquilin-4|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211015|||http://purl.uniprot.org/annotation/VAR_052685|||http://purl.uniprot.org/annotation/VAR_081427|||http://purl.uniprot.org/annotation/VAR_081428|||http://purl.uniprot.org/annotation/VSP_041187|||http://purl.uniprot.org/annotation/VSP_041188
http://togogenome.org/gene/9606:NPIPB8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PQR5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Nuclear pore complex-interacting protein family member B8|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000423922
http://togogenome.org/gene/9606:GRB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0LPF3|||http://purl.uniprot.org/uniprot/P62993                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with SHB; when associated with L-49.|||Growth factor receptor-bound protein 2|||In isoform 2.|||Ineffective in DNA synthesis. Abolishes interaction with SHB; when associated with L-206. Abolishes interaction with SOS1.|||Ineffective in DNA synthesis. Abolishes interaction with SOS1.|||N-acetylmethionine|||N6-acetyllysine|||No effect on the interaction with SOS1.|||Phosphothreonine|||SH2|||SH3|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088198|||http://purl.uniprot.org/annotation/VSP_001839
http://togogenome.org/gene/9606:RERG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96A58                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Ras-related and estrogen-regulated growth inhibitor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082723|||http://purl.uniprot.org/annotation/VSP_043393
http://togogenome.org/gene/9606:NUDT6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DG76|||http://purl.uniprot.org/uniprot/P53370                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Nucleoside diphosphate-linked moiety X motif 6|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057107|||http://purl.uniprot.org/annotation/VAR_021909|||http://purl.uniprot.org/annotation/VAR_050412|||http://purl.uniprot.org/annotation/VSP_003729
http://togogenome.org/gene/9606:NUFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHK0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Bipartite nuclear localization signal|||C2H2-type|||Disordered|||FMR1-interacting protein NUFIP1|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245518|||http://purl.uniprot.org/annotation/VAR_026978
http://togogenome.org/gene/9606:ZNF44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W7T7|||http://purl.uniprot.org/uniprot/P15621                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; atypical|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2 and isoform 3.|||In isoform 2.|||KRAB|||Zinc finger protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047377|||http://purl.uniprot.org/annotation/VAR_047425|||http://purl.uniprot.org/annotation/VAR_047426|||http://purl.uniprot.org/annotation/VSP_035757|||http://purl.uniprot.org/annotation/VSP_035758|||http://purl.uniprot.org/annotation/VSP_035759
http://togogenome.org/gene/9606:CABIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWW8|||http://purl.uniprot.org/uniprot/Q9Y6J0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates binding to MEF2B.|||Acidic residues|||Basic and acidic residues|||Calcineurin-binding protein cabin-1|||Calcineurin-binding protein cabin-1 MEF2-binding|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Required for interaction with calcineurin|||TPR|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106275|||http://purl.uniprot.org/annotation/VAR_052607|||http://purl.uniprot.org/annotation/VAR_052608|||http://purl.uniprot.org/annotation/VAR_052609|||http://purl.uniprot.org/annotation/VAR_052610|||http://purl.uniprot.org/annotation/VAR_052611|||http://purl.uniprot.org/annotation/VAR_052612|||http://purl.uniprot.org/annotation/VSP_054161|||http://purl.uniprot.org/annotation/VSP_054162
http://togogenome.org/gene/9606:SUPT20HL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2YQ69                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Spt20-like SEP                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:CPZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MDV6|||http://purl.uniprot.org/uniprot/Q66K79                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Carboxypeptidase Z|||Disordered|||FZ|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252456|||http://purl.uniprot.org/annotation/PRO_5033788017|||http://purl.uniprot.org/annotation/VAR_027883|||http://purl.uniprot.org/annotation/VAR_027884|||http://purl.uniprot.org/annotation/VAR_047244|||http://purl.uniprot.org/annotation/VAR_047245|||http://purl.uniprot.org/annotation/VAR_047246|||http://purl.uniprot.org/annotation/VSP_020983|||http://purl.uniprot.org/annotation/VSP_040356
http://togogenome.org/gene/9606:ARRDC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5I2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Arrestin domain-containing protein 1|||Decreased interaction with TSG101. No effect on localization to the cell membrane. Loss of localization to extracellular vesicles.|||Decreased localization to the cell membrane and extracellular vesicles.|||Disordered|||Loss of interaction with ITCH; when associated with A-403.|||Loss of interaction with ITCH; when associated with A-416.|||Loss of localization to the cell membrane and extracellular vesicles. Localizes to the cytoplasm.|||PPxY motif 1|||PPxY motif 2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244345|||http://purl.uniprot.org/annotation/VAR_048335
http://togogenome.org/gene/9606:KIAA0513                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60268                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||Uncharacterized protein KIAA0513                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050757|||http://purl.uniprot.org/annotation/VAR_034035|||http://purl.uniprot.org/annotation/VSP_011551|||http://purl.uniprot.org/annotation/VSP_054680
http://togogenome.org/gene/9606:MAS1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35410|||http://purl.uniprot.org/uniprot/Q502V9|||http://purl.uniprot.org/uniprot/W8W3J1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Mas-related G-protein coupled receptor MRG|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069717|||http://purl.uniprot.org/annotation/PRO_5004248176|||http://purl.uniprot.org/annotation/VAR_049416
http://togogenome.org/gene/9606:LPCAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1A2                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Di-lysine motif|||Helical|||In isoform 2.|||Lysophospholipid acyltransferase 5|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233382|||http://purl.uniprot.org/annotation/VAR_050027|||http://purl.uniprot.org/annotation/VAR_050028|||http://purl.uniprot.org/annotation/VSP_053680
http://togogenome.org/gene/9606:METAP1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UB28                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Methionine aminopeptidase 1D, mitochondrial|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314126|||http://purl.uniprot.org/annotation/VAR_050273
http://togogenome.org/gene/9606:GALNT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4A0                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC.|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interaction with glycopeptide substrate|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 4|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059108|||http://purl.uniprot.org/annotation/VAR_019576|||http://purl.uniprot.org/annotation/VAR_019577|||http://purl.uniprot.org/annotation/VAR_065257|||http://purl.uniprot.org/annotation/VSP_045009|||http://purl.uniprot.org/annotation/VSP_045010
http://togogenome.org/gene/9606:SLC13A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D0X1|||http://purl.uniprot.org/uniprot/Q2NKK0|||http://purl.uniprot.org/uniprot/Q9BZW2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Solute carrier family 13 member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000172485|||http://purl.uniprot.org/annotation/VAR_022018|||http://purl.uniprot.org/annotation/VAR_029247|||http://purl.uniprot.org/annotation/VAR_029248|||http://purl.uniprot.org/annotation/VAR_029249|||http://purl.uniprot.org/annotation/VAR_029250|||http://purl.uniprot.org/annotation/VAR_029251|||http://purl.uniprot.org/annotation/VAR_029252|||http://purl.uniprot.org/annotation/VAR_029253|||http://purl.uniprot.org/annotation/VAR_059804
http://togogenome.org/gene/9606:PIGQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAU6|||http://purl.uniprot.org/uniprot/Q9BRB3                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In MCAHS4.|||In isoform 2.|||In isoform 3.|||Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215664|||http://purl.uniprot.org/annotation/VAR_015596|||http://purl.uniprot.org/annotation/VAR_053579|||http://purl.uniprot.org/annotation/VAR_053580|||http://purl.uniprot.org/annotation/VAR_053581|||http://purl.uniprot.org/annotation/VAR_083110|||http://purl.uniprot.org/annotation/VAR_083111|||http://purl.uniprot.org/annotation/VSP_007279|||http://purl.uniprot.org/annotation/VSP_007280|||http://purl.uniprot.org/annotation/VSP_007281|||http://purl.uniprot.org/annotation/VSP_007282
http://togogenome.org/gene/9606:LY86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95711                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Lymphocyte antigen 86|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018614|||http://purl.uniprot.org/annotation/VAR_014539|||http://purl.uniprot.org/annotation/VAR_024531|||http://purl.uniprot.org/annotation/VAR_050029
http://togogenome.org/gene/9606:RNF123                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5XPI4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity and ability to promote maturation of the NFKB1 component of NF-kappa-B.|||Abolished ability to bind and ubiquitinate NFKB1.|||Asymmetric dimethylarginine|||B30.2/SPRY|||E3 ubiquitin-protein ligase RNF123|||In isoform 2.|||Interaction with NFKB1|||N-acetylalanine|||Phosphoserine|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250447|||http://purl.uniprot.org/annotation/VAR_027561|||http://purl.uniprot.org/annotation/VAR_052106|||http://purl.uniprot.org/annotation/VAR_052107|||http://purl.uniprot.org/annotation/VAR_052108|||http://purl.uniprot.org/annotation/VSP_020650
http://togogenome.org/gene/9606:RBM44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZP01|||http://purl.uniprot.org/uniprot/Q8N7S3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||RNA-binding protein 44|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294174|||http://purl.uniprot.org/annotation/VAR_033147|||http://purl.uniprot.org/annotation/VAR_033148|||http://purl.uniprot.org/annotation/VAR_057247
http://togogenome.org/gene/9606:ANGPTL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXH0                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Angiopoietin-like protein 8|||Lover plasma LDL-cholesterol and HDL-cholesterol levels.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319617|||http://purl.uniprot.org/annotation/VAR_039046|||http://purl.uniprot.org/annotation/VAR_039047
http://togogenome.org/gene/9606:RP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56715                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Doublecortin 1|||Doublecortin 2|||In RP1.|||In RP1; unknown pathological significance.|||Oxygen-regulated protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097410|||http://purl.uniprot.org/annotation/VAR_007810|||http://purl.uniprot.org/annotation/VAR_007811|||http://purl.uniprot.org/annotation/VAR_007812|||http://purl.uniprot.org/annotation/VAR_007813|||http://purl.uniprot.org/annotation/VAR_007814|||http://purl.uniprot.org/annotation/VAR_051323|||http://purl.uniprot.org/annotation/VAR_051324|||http://purl.uniprot.org/annotation/VAR_051325|||http://purl.uniprot.org/annotation/VAR_051326|||http://purl.uniprot.org/annotation/VAR_064182|||http://purl.uniprot.org/annotation/VAR_064183|||http://purl.uniprot.org/annotation/VAR_064466|||http://purl.uniprot.org/annotation/VAR_064467|||http://purl.uniprot.org/annotation/VAR_064468|||http://purl.uniprot.org/annotation/VAR_064469|||http://purl.uniprot.org/annotation/VAR_064470|||http://purl.uniprot.org/annotation/VAR_064471|||http://purl.uniprot.org/annotation/VAR_064472|||http://purl.uniprot.org/annotation/VAR_064473|||http://purl.uniprot.org/annotation/VAR_064474|||http://purl.uniprot.org/annotation/VAR_066948|||http://purl.uniprot.org/annotation/VAR_066949|||http://purl.uniprot.org/annotation/VAR_066950|||http://purl.uniprot.org/annotation/VAR_066951|||http://purl.uniprot.org/annotation/VAR_066952|||http://purl.uniprot.org/annotation/VAR_066953|||http://purl.uniprot.org/annotation/VAR_066954|||http://purl.uniprot.org/annotation/VAR_066955|||http://purl.uniprot.org/annotation/VAR_066956|||http://purl.uniprot.org/annotation/VAR_066957|||http://purl.uniprot.org/annotation/VAR_066958|||http://purl.uniprot.org/annotation/VAR_066959|||http://purl.uniprot.org/annotation/VAR_068351
http://togogenome.org/gene/9606:BTF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20290                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N6-methyllysine|||NAC-A/B|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Transcription factor BTF3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213548|||http://purl.uniprot.org/annotation/VSP_013587
http://togogenome.org/gene/9606:SPTSSB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWB5|||http://purl.uniprot.org/uniprot/Q8NFR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Serine palmitoyltransferase small subunit B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239719
http://togogenome.org/gene/9606:PSMB10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40306                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||In PRAAS5; unknown pathological significance; impaired autocleavage and maturation.|||N-acetylmethionine|||Nucleophile|||Phosphoserine|||Proteasome subunit beta type-10|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026651|||http://purl.uniprot.org/annotation/PRO_0000026652|||http://purl.uniprot.org/annotation/VAR_085404
http://togogenome.org/gene/9606:HDAC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T8F4|||http://purl.uniprot.org/uniprot/A0A7P0TAB5|||http://purl.uniprot.org/uniprot/A0A9L9PXL9|||http://purl.uniprot.org/uniprot/B7Z3P7|||http://purl.uniprot.org/uniprot/Q9UKV0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a renal cell carcinoma sample; somatic mutation.|||Histone deacetylase|||Histone deacetylase 9|||Histone deacetylase glutamine rich N-terminal|||In isoform 10 and isoform 11.|||In isoform 11.|||In isoform 2.|||In isoform 3, isoform 8, isoform 9, isoform 10 and isoform 11.|||In isoform 4.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 6, isoform 7 and isoform 10.|||In isoform 6, isoform 8, isoform 9 and isoform 11.|||In isoform 8.|||Interaction with CTBP1|||Interaction with ETV6|||Interaction with MAPK10|||Interaction with MEF2|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114710|||http://purl.uniprot.org/annotation/VAR_064719|||http://purl.uniprot.org/annotation/VSP_002082|||http://purl.uniprot.org/annotation/VSP_002083|||http://purl.uniprot.org/annotation/VSP_002084|||http://purl.uniprot.org/annotation/VSP_002085|||http://purl.uniprot.org/annotation/VSP_002086|||http://purl.uniprot.org/annotation/VSP_023766|||http://purl.uniprot.org/annotation/VSP_023767|||http://purl.uniprot.org/annotation/VSP_023768|||http://purl.uniprot.org/annotation/VSP_043428|||http://purl.uniprot.org/annotation/VSP_046827|||http://purl.uniprot.org/annotation/VSP_046828
http://togogenome.org/gene/9606:DEFB114                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q30KQ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 114                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045342
http://togogenome.org/gene/9606:DNALI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A499FIY3|||http://purl.uniprot.org/uniprot/O14645                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Axonemal dynein light intermediate polypeptide 1|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114675|||http://purl.uniprot.org/annotation/VAR_014473|||http://purl.uniprot.org/annotation/VAR_035701|||http://purl.uniprot.org/annotation/VSP_056965|||http://purl.uniprot.org/annotation/VSP_056966
http://togogenome.org/gene/9606:PSMG4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JS54                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Proteasome assembly chaperone 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341397|||http://purl.uniprot.org/annotation/VAR_084585|||http://purl.uniprot.org/annotation/VSP_046635|||http://purl.uniprot.org/annotation/VSP_046636
http://togogenome.org/gene/9606:NDRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN36                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased interaction with CTNNB1. Abolishes down-regulation of Wnt signaling.|||Disordered|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Protein NDRG2|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000441166|||http://purl.uniprot.org/annotation/VAR_026572|||http://purl.uniprot.org/annotation/VAR_050236|||http://purl.uniprot.org/annotation/VSP_003417|||http://purl.uniprot.org/annotation/VSP_003418|||http://purl.uniprot.org/annotation/VSP_019007|||http://purl.uniprot.org/annotation/VSP_019008|||http://purl.uniprot.org/annotation/VSP_054583
http://togogenome.org/gene/9606:FNDC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC99                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Fibronectin type III domain-containing protein 8|||Fibronectin type-III                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284530|||http://purl.uniprot.org/annotation/VAR_031770|||http://purl.uniprot.org/annotation/VAR_050999
http://togogenome.org/gene/9606:OGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJQ5|||http://purl.uniprot.org/uniprot/B4E3E9|||http://purl.uniprot.org/uniprot/E9PCR7|||http://purl.uniprot.org/uniprot/Q02218                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  2-oxoglutarate dehydrogenase E1 component N-terminal|||2-oxoglutarate dehydrogenase complex component E1|||Abolished enzyme activity and ability to promote histone succinylation.|||Dehydrogenase E1 component|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Six-fold decrease in sensitivity for calcium.|||Transketolase-like pyrimidine-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020432|||http://purl.uniprot.org/annotation/VAR_050435|||http://purl.uniprot.org/annotation/VSP_042313|||http://purl.uniprot.org/annotation/VSP_043628|||http://purl.uniprot.org/annotation/VSP_043629
http://togogenome.org/gene/9606:IVD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MT83|||http://purl.uniprot.org/uniprot/A0A0S2Z4K7|||http://purl.uniprot.org/uniprot/P26440                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase/oxidase C-terminal|||Acyl-CoA dehydrogenase/oxidase N-terminal|||Acyl-CoA oxidase/dehydrogenase middle|||Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.|||In IVA.|||In IVA; unknown pathological significance.|||In isoform 2.|||Isovaleryl-CoA dehydrogenase, mitochondrial|||Loss of isovaleryl-CoA dehydrogenase activity.|||Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton acceptor|||Residual isovaleryl-CoA dehydrogenase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000531|||http://purl.uniprot.org/annotation/VAR_000423|||http://purl.uniprot.org/annotation/VAR_000424|||http://purl.uniprot.org/annotation/VAR_015960|||http://purl.uniprot.org/annotation/VAR_015961|||http://purl.uniprot.org/annotation/VAR_015962|||http://purl.uniprot.org/annotation/VAR_015963|||http://purl.uniprot.org/annotation/VAR_015964|||http://purl.uniprot.org/annotation/VAR_015965|||http://purl.uniprot.org/annotation/VAR_015966|||http://purl.uniprot.org/annotation/VAR_070061|||http://purl.uniprot.org/annotation/VAR_070062|||http://purl.uniprot.org/annotation/VAR_070063|||http://purl.uniprot.org/annotation/VAR_070064|||http://purl.uniprot.org/annotation/VAR_070065|||http://purl.uniprot.org/annotation/VAR_079552|||http://purl.uniprot.org/annotation/VAR_079553|||http://purl.uniprot.org/annotation/VAR_079554|||http://purl.uniprot.org/annotation/VAR_079555|||http://purl.uniprot.org/annotation/VAR_079556|||http://purl.uniprot.org/annotation/VSP_045193
http://togogenome.org/gene/9606:ERAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ08                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Endoplasmic reticulum aminopeptidase 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Loss of enzyme activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026751|||http://purl.uniprot.org/annotation/VAR_012779|||http://purl.uniprot.org/annotation/VAR_012780|||http://purl.uniprot.org/annotation/VAR_012781|||http://purl.uniprot.org/annotation/VAR_012782|||http://purl.uniprot.org/annotation/VAR_012783|||http://purl.uniprot.org/annotation/VAR_012784|||http://purl.uniprot.org/annotation/VAR_021555|||http://purl.uniprot.org/annotation/VAR_021556|||http://purl.uniprot.org/annotation/VAR_046681|||http://purl.uniprot.org/annotation/VAR_046682|||http://purl.uniprot.org/annotation/VSP_005450
http://togogenome.org/gene/9606:PIK3CA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42336|||http://purl.uniprot.org/uniprot/Q4LE51                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||C2 PI3K-type|||Catalytic loop|||Found in a cancer sample; unknown pathological significance.|||Found in a glioblastoma multiforme sample; unknown pathological significance.|||Found in an anaplastic astrocytoma sample; unknown pathological significance.|||Found in an endometrial carcinoma sample; unknown pathological significance.|||Found in brain tumors; unknown pathological significance.|||G-loop|||Implicated in the recognition of ATP as well as PIP2. Also crucial for autophosphorylation of the p85alpha subunit|||In BC, CLAPO, MADAC and CCM4; somatic mutation.|||In BC; unknown pathological significance.|||In CLAPO and MADAC; unknown pathological significance; somatic mutation in CLAPO and MADAC patients.|||In CLAPO; unknown pathological significance; somatic mutation.|||In CLOVE, CRC and CLAPO; unknown pathological significance; somatic mutation in CLAPO patients; shows an increase in lipid kinase activity; may increase the affinity for lipid membranes.|||In CLOVE, KERSEB, CRC, BC, CLAPO, MADAC and CCM4; also found in glioblastoma multiforme and endometrial carcinoma; somatic mutation; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation.|||In CLOVE, KERSEB, CRC, BC, OC, MADAC and CCM4; also found in an endometrial carcinoma sample; somatic mutation; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane.|||In CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity.|||In CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain.|||In CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction of the C2 PI3K-type domain with the iSH2 region of the p85 regulatory subunit.|||In CRC; unknown pathological significance.|||In CWS5 and HCC; also found in a glioblastoma multiforme sample.|||In CWS5.|||In KERSEB; also found in an endometrial carcinoma sample.|||In MCAP and CRC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity.|||In MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells.|||In MCAP.|||In MCAP; also found in a glioblastoma multiforme sample.|||In MCAP; also found in an endometrial carcinoma sample.|||In MCAP; increased phosphatidylinositol 3-kinase signaling; decreased interaction with p85 regulatory subunit; no effect on protein abundance.|||In OC; unknown pathological significance.|||PI3K-ABD|||PI3K-RBD|||PI3K/PI4K catalytic|||PIK helical|||Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088785|||http://purl.uniprot.org/annotation/VAR_026166|||http://purl.uniprot.org/annotation/VAR_026167|||http://purl.uniprot.org/annotation/VAR_026168|||http://purl.uniprot.org/annotation/VAR_026169|||http://purl.uniprot.org/annotation/VAR_026170|||http://purl.uniprot.org/annotation/VAR_026171|||http://purl.uniprot.org/annotation/VAR_026172|||http://purl.uniprot.org/annotation/VAR_026173|||http://purl.uniprot.org/annotation/VAR_026174|||http://purl.uniprot.org/annotation/VAR_026175|||http://purl.uniprot.org/annotation/VAR_026176|||http://purl.uniprot.org/annotation/VAR_026177|||http://purl.uniprot.org/annotation/VAR_026178|||http://purl.uniprot.org/annotation/VAR_026179|||http://purl.uniprot.org/annotation/VAR_026180|||http://purl.uniprot.org/annotation/VAR_026181|||http://purl.uniprot.org/annotation/VAR_026182|||http://purl.uniprot.org/annotation/VAR_026183|||http://purl.uniprot.org/annotation/VAR_026184|||http://purl.uniprot.org/annotation/VAR_026185|||http://purl.uniprot.org/annotation/VAR_026186|||http://purl.uniprot.org/annotation/VAR_026187|||http://purl.uniprot.org/annotation/VAR_026188|||http://purl.uniprot.org/annotation/VAR_026189|||http://purl.uniprot.org/annotation/VAR_026190|||http://purl.uniprot.org/annotation/VAR_026191|||http://purl.uniprot.org/annotation/VAR_026192|||http://purl.uniprot.org/annotation/VAR_026193|||http://purl.uniprot.org/annotation/VAR_026194|||http://purl.uniprot.org/annotation/VAR_026195|||http://purl.uniprot.org/annotation/VAR_026196|||http://purl.uniprot.org/annotation/VAR_026197|||http://purl.uniprot.org/annotation/VAR_042942|||http://purl.uniprot.org/annotation/VAR_042943|||http://purl.uniprot.org/annotation/VAR_069251|||http://purl.uniprot.org/annotation/VAR_069252|||http://purl.uniprot.org/annotation/VAR_069253|||http://purl.uniprot.org/annotation/VAR_069254|||http://purl.uniprot.org/annotation/VAR_069255|||http://purl.uniprot.org/annotation/VAR_069256|||http://purl.uniprot.org/annotation/VAR_069257|||http://purl.uniprot.org/annotation/VAR_069258|||http://purl.uniprot.org/annotation/VAR_069259|||http://purl.uniprot.org/annotation/VAR_069786|||http://purl.uniprot.org/annotation/VAR_069787|||http://purl.uniprot.org/annotation/VAR_069788|||http://purl.uniprot.org/annotation/VAR_069789|||http://purl.uniprot.org/annotation/VAR_069790|||http://purl.uniprot.org/annotation/VAR_075634|||http://purl.uniprot.org/annotation/VAR_081475|||http://purl.uniprot.org/annotation/VAR_081476
http://togogenome.org/gene/9606:CHCHD6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRQ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  CHCH|||Cx9C motif 1|||Cx9C motif 2|||Disordered|||MICOS complex subunit MIC25|||N-myristoyl glycine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000129169|||http://purl.uniprot.org/annotation/VAR_024412
http://togogenome.org/gene/9606:TMEM184C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVA4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||Phosphoserine|||Polar residues|||Transmembrane protein 184C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287567|||http://purl.uniprot.org/annotation/VSP_025566
http://togogenome.org/gene/9606:ROCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13464                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes cleavage by caspase-3.|||Auto-inhibitory|||Cleavage; by caspase-3|||Disordered|||In a lung neuroendocrine carcinoma sample; somatic mutation.|||Interaction with FHOD1|||N-acetylserine|||N6-acetyllysine|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Polar residues|||Protein kinase|||Proton acceptor|||REM-1|||RHOA binding|||Removed|||Rho-associated protein kinase 1|||RhoBD|||SHROOM3 binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086619|||http://purl.uniprot.org/annotation/VAR_041055|||http://purl.uniprot.org/annotation/VAR_041056|||http://purl.uniprot.org/annotation/VAR_041057|||http://purl.uniprot.org/annotation/VAR_041058|||http://purl.uniprot.org/annotation/VAR_041059|||http://purl.uniprot.org/annotation/VAR_041060|||http://purl.uniprot.org/annotation/VAR_041061
http://togogenome.org/gene/9606:GPR34                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VT14|||http://purl.uniprot.org/uniprot/Q9UPC5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 34                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069559
http://togogenome.org/gene/9606:OR4A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW87|||http://purl.uniprot.org/uniprot/Q8NH70                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4A16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150526|||http://purl.uniprot.org/annotation/VAR_034187|||http://purl.uniprot.org/annotation/VAR_034188|||http://purl.uniprot.org/annotation/VAR_053164
http://togogenome.org/gene/9606:VTI1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J5N6|||http://purl.uniprot.org/uniprot/Q96AJ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 1.|||T-SNARE coiled-coil homology|||Vesicle transport through interaction with t-SNAREs homolog 1A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218225|||http://purl.uniprot.org/annotation/VSP_039848
http://togogenome.org/gene/9606:ZNF829                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KNS6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||In isoform 3.|||KRAB|||Zinc finger protein 829                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000335808|||http://purl.uniprot.org/annotation/VSP_033769|||http://purl.uniprot.org/annotation/VSP_033770|||http://purl.uniprot.org/annotation/VSP_057606
http://togogenome.org/gene/9606:CXorf38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB03                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Omega-N-methylarginine|||Phosphothreonine|||Uncharacterized protein CXorf38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079732|||http://purl.uniprot.org/annotation/VAR_050936|||http://purl.uniprot.org/annotation/VSP_014620|||http://purl.uniprot.org/annotation/VSP_014621|||http://purl.uniprot.org/annotation/VSP_014622
http://togogenome.org/gene/9606:SLC3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4E1|||http://purl.uniprot.org/uniprot/B8ZZK1|||http://purl.uniprot.org/uniprot/Q07837                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amino acid transporter heavy chain SLC3A1|||Cytoplasmic|||Disordered|||Extracellular|||Glycosyl hydrolase family 13 catalytic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In CSNU.|||In CSNU; impairs protein stability and dimer formation.|||In CSNU; impairs protein stability and dimer formation; loss of 80% of amino acid transport activity.|||In CSNU; reduction in amino acid transport activity.|||In CSNU; unknown pathological significance.|||In CSNU; unknown pathological significance; impairs protein stability and dimer formation.|||In isoform B.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||In isoform G.|||Interchain (with C-144 in SLC7A5)|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071950|||http://purl.uniprot.org/annotation/VAR_011420|||http://purl.uniprot.org/annotation/VAR_011421|||http://purl.uniprot.org/annotation/VAR_011422|||http://purl.uniprot.org/annotation/VAR_011423|||http://purl.uniprot.org/annotation/VAR_011424|||http://purl.uniprot.org/annotation/VAR_011425|||http://purl.uniprot.org/annotation/VAR_011426|||http://purl.uniprot.org/annotation/VAR_011427|||http://purl.uniprot.org/annotation/VAR_011428|||http://purl.uniprot.org/annotation/VAR_011429|||http://purl.uniprot.org/annotation/VAR_011430|||http://purl.uniprot.org/annotation/VAR_011431|||http://purl.uniprot.org/annotation/VAR_011432|||http://purl.uniprot.org/annotation/VAR_011433|||http://purl.uniprot.org/annotation/VAR_011434|||http://purl.uniprot.org/annotation/VAR_022600|||http://purl.uniprot.org/annotation/VAR_022601|||http://purl.uniprot.org/annotation/VAR_022602|||http://purl.uniprot.org/annotation/VAR_038200|||http://purl.uniprot.org/annotation/VAR_038201|||http://purl.uniprot.org/annotation/VAR_038202|||http://purl.uniprot.org/annotation/VAR_038203|||http://purl.uniprot.org/annotation/VAR_038204|||http://purl.uniprot.org/annotation/VAR_038205|||http://purl.uniprot.org/annotation/VAR_038206|||http://purl.uniprot.org/annotation/VAR_038207|||http://purl.uniprot.org/annotation/VAR_038208|||http://purl.uniprot.org/annotation/VAR_038209|||http://purl.uniprot.org/annotation/VAR_064040|||http://purl.uniprot.org/annotation/VAR_072283|||http://purl.uniprot.org/annotation/VAR_072284|||http://purl.uniprot.org/annotation/VAR_072285|||http://purl.uniprot.org/annotation/VAR_072286|||http://purl.uniprot.org/annotation/VAR_072287|||http://purl.uniprot.org/annotation/VAR_072288|||http://purl.uniprot.org/annotation/VAR_072289|||http://purl.uniprot.org/annotation/VAR_072290|||http://purl.uniprot.org/annotation/VAR_072291|||http://purl.uniprot.org/annotation/VAR_072292|||http://purl.uniprot.org/annotation/VAR_072293|||http://purl.uniprot.org/annotation/VAR_072294|||http://purl.uniprot.org/annotation/VAR_072295|||http://purl.uniprot.org/annotation/VAR_072296|||http://purl.uniprot.org/annotation/VAR_072297|||http://purl.uniprot.org/annotation/VAR_072298|||http://purl.uniprot.org/annotation/VAR_072299|||http://purl.uniprot.org/annotation/VAR_072300|||http://purl.uniprot.org/annotation/VAR_072301|||http://purl.uniprot.org/annotation/VAR_072302|||http://purl.uniprot.org/annotation/VAR_072303|||http://purl.uniprot.org/annotation/VAR_072304|||http://purl.uniprot.org/annotation/VAR_072305|||http://purl.uniprot.org/annotation/VAR_072306|||http://purl.uniprot.org/annotation/VAR_072307|||http://purl.uniprot.org/annotation/VSP_054339|||http://purl.uniprot.org/annotation/VSP_054340|||http://purl.uniprot.org/annotation/VSP_054341|||http://purl.uniprot.org/annotation/VSP_054342|||http://purl.uniprot.org/annotation/VSP_054343|||http://purl.uniprot.org/annotation/VSP_054344|||http://purl.uniprot.org/annotation/VSP_054345|||http://purl.uniprot.org/annotation/VSP_054346|||http://purl.uniprot.org/annotation/VSP_054347|||http://purl.uniprot.org/annotation/VSP_054348|||http://purl.uniprot.org/annotation/VSP_054349
http://togogenome.org/gene/9606:OR1N1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW31|||http://purl.uniprot.org/uniprot/Q8NGS0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1N1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150448|||http://purl.uniprot.org/annotation/VAR_024089|||http://purl.uniprot.org/annotation/VAR_036208|||http://purl.uniprot.org/annotation/VAR_062011
http://togogenome.org/gene/9606:NRBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8W6G1|||http://purl.uniprot.org/uniprot/Q9UHY1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In an ovarian mucinous carcinoma sample; somatic mutation.|||N-acetylserine|||Nuclear receptor-binding protein|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086449|||http://purl.uniprot.org/annotation/VAR_041359|||http://purl.uniprot.org/annotation/VAR_041360|||http://purl.uniprot.org/annotation/VAR_041361
http://togogenome.org/gene/9606:SYK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43405                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes YWHAG binding.|||In IMD82; constitutively active protein tyrosine kinase activity.|||In isoform Short.|||Interdomain A|||Interdomain B|||Loss of interaction with BLNK.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by LYN|||Phosphotyrosine; by autocatalysis|||Protein kinase|||Proton acceptor|||SH2 1|||SH2 2|||Tyrosine-protein kinase SYK                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088165|||http://purl.uniprot.org/annotation/VAR_033838|||http://purl.uniprot.org/annotation/VAR_085995|||http://purl.uniprot.org/annotation/VAR_085996|||http://purl.uniprot.org/annotation/VAR_085997|||http://purl.uniprot.org/annotation/VAR_085998|||http://purl.uniprot.org/annotation/VAR_085999|||http://purl.uniprot.org/annotation/VSP_005010
http://togogenome.org/gene/9606:MAN2B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6A7|||http://purl.uniprot.org/uniprot/O00754                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Alpha-mannosidase|||Glycoside hydrolase family 38 central|||In MANSA.|||In MANSA; no residual enzyme activity.|||In MANSA; reduced enzyme activity.|||In MANSA; results in less than 20% of wild-type enzyme activity.|||In MANSA; type I.|||In MANSA; type II.|||In MANSA; unknown pathological significance.|||In isoform 2.|||Lysosomal alpha-mannosidase|||Lysosomal alpha-mannosidase A peptide|||Lysosomal alpha-mannosidase B peptide|||Lysosomal alpha-mannosidase C peptide|||Lysosomal alpha-mannosidase D peptide|||Lysosomal alpha-mannosidase E peptide|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012069|||http://purl.uniprot.org/annotation/PRO_0000012070|||http://purl.uniprot.org/annotation/PRO_0000012071|||http://purl.uniprot.org/annotation/PRO_0000012072|||http://purl.uniprot.org/annotation/PRO_0000012073|||http://purl.uniprot.org/annotation/PRO_0000012074|||http://purl.uniprot.org/annotation/PRO_5002724659|||http://purl.uniprot.org/annotation/VAR_003338|||http://purl.uniprot.org/annotation/VAR_003339|||http://purl.uniprot.org/annotation/VAR_003340|||http://purl.uniprot.org/annotation/VAR_003341|||http://purl.uniprot.org/annotation/VAR_003342|||http://purl.uniprot.org/annotation/VAR_003343|||http://purl.uniprot.org/annotation/VAR_003344|||http://purl.uniprot.org/annotation/VAR_003345|||http://purl.uniprot.org/annotation/VAR_003346|||http://purl.uniprot.org/annotation/VAR_003347|||http://purl.uniprot.org/annotation/VAR_003348|||http://purl.uniprot.org/annotation/VAR_026412|||http://purl.uniprot.org/annotation/VAR_026413|||http://purl.uniprot.org/annotation/VAR_026414|||http://purl.uniprot.org/annotation/VAR_049209|||http://purl.uniprot.org/annotation/VAR_049210|||http://purl.uniprot.org/annotation/VAR_068034|||http://purl.uniprot.org/annotation/VAR_068035|||http://purl.uniprot.org/annotation/VAR_068036|||http://purl.uniprot.org/annotation/VAR_068037|||http://purl.uniprot.org/annotation/VAR_068038|||http://purl.uniprot.org/annotation/VAR_068039|||http://purl.uniprot.org/annotation/VAR_068040|||http://purl.uniprot.org/annotation/VAR_068041|||http://purl.uniprot.org/annotation/VAR_068042|||http://purl.uniprot.org/annotation/VAR_068043|||http://purl.uniprot.org/annotation/VAR_068044|||http://purl.uniprot.org/annotation/VAR_068045|||http://purl.uniprot.org/annotation/VAR_068046|||http://purl.uniprot.org/annotation/VAR_068047|||http://purl.uniprot.org/annotation/VAR_068048|||http://purl.uniprot.org/annotation/VAR_068049|||http://purl.uniprot.org/annotation/VAR_068050|||http://purl.uniprot.org/annotation/VAR_068051|||http://purl.uniprot.org/annotation/VAR_068052|||http://purl.uniprot.org/annotation/VAR_068053|||http://purl.uniprot.org/annotation/VAR_068054|||http://purl.uniprot.org/annotation/VAR_068055|||http://purl.uniprot.org/annotation/VAR_068056|||http://purl.uniprot.org/annotation/VAR_068057|||http://purl.uniprot.org/annotation/VAR_068058|||http://purl.uniprot.org/annotation/VAR_068059|||http://purl.uniprot.org/annotation/VAR_068060|||http://purl.uniprot.org/annotation/VAR_068061|||http://purl.uniprot.org/annotation/VAR_068062|||http://purl.uniprot.org/annotation/VAR_068063|||http://purl.uniprot.org/annotation/VAR_068064|||http://purl.uniprot.org/annotation/VAR_068065|||http://purl.uniprot.org/annotation/VAR_068066|||http://purl.uniprot.org/annotation/VAR_068067|||http://purl.uniprot.org/annotation/VAR_068068|||http://purl.uniprot.org/annotation/VAR_068069|||http://purl.uniprot.org/annotation/VSP_047391
http://togogenome.org/gene/9606:RAD51AP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished interaction with DMC1 without affecting interaction with RAD51.|||Abolished interaction with RAD51.|||Abolished interaction with WDR48/UAF1.|||Acidic residues|||Basic and acidic residues|||Decreased interacting with RAD51 and ability to stimulate RAD51-mediated homologous recombination. Does not affect interaction with DMC1.|||Decreased interaction with WDR48/UAF1.|||Disordered|||Does not affect interaction with WDR48/UAF1.|||Does not affect sumoylation.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin; alternate)|||In K2RA; impaired DNA-binding.|||In K3WA; reduced DNA-binding. In K7WA; strongly decreased DNA-binding; when associated with 248-A--A-253.|||In K4A; reduced DNA-binding. In K7WA; strongly decreased DNA-binding; when associated with 300-A--A-304.|||In K6RA; impaired DNA-binding.|||In isoform 2.|||In isoform 3.|||In mutant delta25; abolished interaction with RAD51.|||Interaction with DNA|||Interaction with RAD51|||Phosphoserine|||Phosphothreonine|||Polar residues|||RAD51-associated protein 1|||Reduced sumoylation. Reduced ubiquitination.|||SIM motif|||Strongly decreases interaction with RAD51; when associated with A-333, A-345 and A-346. Decreased interacting with RAD51 and ability to stimulate RAD51-mediated homologous recombination. Does not affect interaction with DMC1.|||Strongly decreases interaction with RAD51; when associated with A-333; and Q-336.|||Strongly decreases interaction with RAD51; when associated with Q-336, A-345 and A-346.|||Strongly reduced sumoylation. Strongly reduced ubiquitination.|||WVPP motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097140|||http://purl.uniprot.org/annotation/VAR_056976|||http://purl.uniprot.org/annotation/VSP_051739|||http://purl.uniprot.org/annotation/VSP_051740
http://togogenome.org/gene/9606:CLPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZW1|||http://purl.uniprot.org/uniprot/A0A087X0Q7|||http://purl.uniprot.org/uniprot/P04118                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Colipase|||Colipase C-terminal|||Colipase N-terminal|||Enterostatin, activation peptide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005696|||http://purl.uniprot.org/annotation/PRO_0000005697|||http://purl.uniprot.org/annotation/PRO_5014503712|||http://purl.uniprot.org/annotation/VAR_047105|||http://purl.uniprot.org/annotation/VAR_053040
http://togogenome.org/gene/9606:NDUFA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00483                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit NDUFA4|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118821
http://togogenome.org/gene/9606:HOXC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09017|||http://purl.uniprot.org/uniprot/Q86TF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-C4|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200164|||http://purl.uniprot.org/annotation/VAR_055961|||http://purl.uniprot.org/annotation/VAR_055962
http://togogenome.org/gene/9606:MCM3AP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60318                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acetyltransferase|||Asymmetric dimethylarginine|||Basic and acidic residues|||CID|||Disordered|||FG-repeats|||Germinal-center associated nuclear protein|||In PNRIID.|||In PNRIID; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform MCM3AP.|||Interaction with Centrin|||Interaction with ENY2|||Interaction with PCID2 and SEM1|||Loss of i nteraction with MCM3, loss of nuclear localization, loss of chromatin-binding.|||N6-acetyllysine|||PCI|||Phosphoserine|||Polar residues|||Severely decreased acetylase activity, loss of DNA replication inhibition. Does not affect chromatin-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096284|||http://purl.uniprot.org/annotation/VAR_019240|||http://purl.uniprot.org/annotation/VAR_019241|||http://purl.uniprot.org/annotation/VAR_019242|||http://purl.uniprot.org/annotation/VAR_019243|||http://purl.uniprot.org/annotation/VAR_019244|||http://purl.uniprot.org/annotation/VAR_019245|||http://purl.uniprot.org/annotation/VAR_019246|||http://purl.uniprot.org/annotation/VAR_019247|||http://purl.uniprot.org/annotation/VAR_019248|||http://purl.uniprot.org/annotation/VAR_019249|||http://purl.uniprot.org/annotation/VAR_019250|||http://purl.uniprot.org/annotation/VAR_019251|||http://purl.uniprot.org/annotation/VAR_035472|||http://purl.uniprot.org/annotation/VAR_053973|||http://purl.uniprot.org/annotation/VAR_070560|||http://purl.uniprot.org/annotation/VAR_081543|||http://purl.uniprot.org/annotation/VAR_081544|||http://purl.uniprot.org/annotation/VAR_081545|||http://purl.uniprot.org/annotation/VAR_081546|||http://purl.uniprot.org/annotation/VAR_081547|||http://purl.uniprot.org/annotation/VAR_081548|||http://purl.uniprot.org/annotation/VAR_081549|||http://purl.uniprot.org/annotation/VAR_081550|||http://purl.uniprot.org/annotation/VAR_081551|||http://purl.uniprot.org/annotation/VAR_081552|||http://purl.uniprot.org/annotation/VSP_053438
http://togogenome.org/gene/9606:TBC1D28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M2D7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  Rab-GAP TBC|||TBC1 domain family member 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337020
http://togogenome.org/gene/9606:SMIM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZL3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Chain|||Site|||Transmembrane                                                                                  ^@                                                                                  Cleavage|||Helical|||Small integral membrane protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096816
http://togogenome.org/gene/9606:CCDC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60826                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 22|||Disordered|||In RTSC2.|||In RTSC2; may affect splicing and/or have a negative impact on transcription efficiency; results in decreased interaction with COMMD1.|||Phosphoserine|||Sufficicient and required for interaction with CCDC93|||Sufficient for interaction with COMMD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076199|||http://purl.uniprot.org/annotation/VAR_065912|||http://purl.uniprot.org/annotation/VAR_075063|||http://purl.uniprot.org/annotation/VAR_076265
http://togogenome.org/gene/9606:TMEM95                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KNT9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Sperm-egg fusion protein TMEM95                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286970|||http://purl.uniprot.org/annotation/VSP_025245|||http://purl.uniprot.org/annotation/VSP_025246
http://togogenome.org/gene/9606:ACVR1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P36896                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activin receptor type-1B|||Cytoplasmic|||Decreases binding to activin.|||Extracellular|||GS|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Increases binding to activin.|||Leads to constitutive activation.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024417|||http://purl.uniprot.org/annotation/VAR_011716|||http://purl.uniprot.org/annotation/VAR_041406|||http://purl.uniprot.org/annotation/VAR_082894|||http://purl.uniprot.org/annotation/VSP_004953|||http://purl.uniprot.org/annotation/VSP_004954|||http://purl.uniprot.org/annotation/VSP_041841|||http://purl.uniprot.org/annotation/VSP_041842
http://togogenome.org/gene/9606:SAMD8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LT4|||http://purl.uniprot.org/uniprot/V9HVY4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes CPE synthase activity.|||Cytoplasmic|||Helical|||In isoform 2.|||SAM|||Sphingomyelin synthase-related protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221080|||http://purl.uniprot.org/annotation/VSP_038403|||http://purl.uniprot.org/annotation/VSP_038404
http://togogenome.org/gene/9606:HPRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJL3|||http://purl.uniprot.org/uniprot/P00492                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Enzyme activity 37% of normal; asymptomatic.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hypoxanthine-guanine phosphoribosyltransferase|||In Edinburgh.|||In HRH and LNS; Asia.|||In HRH; AD and DD.|||In HRH; Ann-Arbor.|||In HRH; Arlington.|||In HRH; Ashville.|||In HRH; Asia.|||In HRH; Brisbane.|||In HRH; Dirranbandi, Asia.|||In HRH; Gravesend.|||In HRH; JF.|||In HRH; JS.|||In HRH; Japan-2.|||In HRH; London.|||In HRH; MG.|||In HRH; Mashad; strongly reduces enzymatic activity.|||In HRH; Milwaukee/RJK 949.|||In HRH; Moose-Jaw; results in cooperativity and decreased substrate affinities.|||In HRH; Munich.|||In HRH; RB.|||In HRH; Reduces enzymatic activity.|||In HRH; Swan.|||In HRH; TE.|||In HRH; Toowong.|||In HRH; Toronto.|||In HRH; Urangan.|||In HRH; Yeronga.|||In LNS; 1265.|||In LNS; 779.|||In LNS; Asia.|||In LNS; Banbury.|||In LNS; Detroit.|||In LNS; FG.|||In LNS; Farnham.|||In LNS; Flint/RJK 892/DW/Perth/1522, Japan.|||In LNS; GM.|||In LNS; HB.|||In LNS; Heapey.|||In LNS; Isar.|||In LNS; Japan-1.|||In LNS; Japan.|||In LNS; Kinston/RJK 2188.|||In LNS; LW.|||In LNS; Marlow.|||In LNS; Michigan.|||In LNS; Midland/RJK 896.|||In LNS; Montreal.|||In LNS; New Briton/RJK 950.|||In LNS; New Haven/1510, Asia.|||In LNS; RJK 1210.|||In LNS; RJK 1784.|||In LNS; RJK 1874.|||In LNS; RJK 2163.|||In LNS; RJK 2185.|||In LNS; RW.|||In LNS; Reading/RJK 1727.|||In LNS; Roanne.|||In LNS; Runcorn.|||In LNS; Salamanca.|||In LNS; Yale.|||N-acetylalanine|||N6-acetyllysine|||Phosphoribosyltransferase|||Phosphothreonine|||Proton acceptor|||Reduced affinity for hypoxanthine, phosphoribosylpyrophosphate and IMP. Reduced catalytic activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139585|||http://purl.uniprot.org/annotation/VAR_006750|||http://purl.uniprot.org/annotation/VAR_006751|||http://purl.uniprot.org/annotation/VAR_006752|||http://purl.uniprot.org/annotation/VAR_006753|||http://purl.uniprot.org/annotation/VAR_006754|||http://purl.uniprot.org/annotation/VAR_006755|||http://purl.uniprot.org/annotation/VAR_006756|||http://purl.uniprot.org/annotation/VAR_006757|||http://purl.uniprot.org/annotation/VAR_006758|||http://purl.uniprot.org/annotation/VAR_006759|||http://purl.uniprot.org/annotation/VAR_006760|||http://purl.uniprot.org/annotation/VAR_006761|||http://purl.uniprot.org/annotation/VAR_006762|||http://purl.uniprot.org/annotation/VAR_006763|||http://purl.uniprot.org/annotation/VAR_006764|||http://purl.uniprot.org/annotation/VAR_006765|||http://purl.uniprot.org/annotation/VAR_006766|||http://purl.uniprot.org/annotation/VAR_006767|||http://purl.uniprot.org/annotation/VAR_006768|||http://purl.uniprot.org/annotation/VAR_006769|||http://purl.uniprot.org/annotation/VAR_006770|||http://purl.uniprot.org/annotation/VAR_006771|||http://purl.uniprot.org/annotation/VAR_006772|||http://purl.uniprot.org/annotation/VAR_006773|||http://purl.uniprot.org/annotation/VAR_006774|||http://purl.uniprot.org/annotation/VAR_006775|||http://purl.uniprot.org/annotation/VAR_006776|||http://purl.uniprot.org/annotation/VAR_006777|||http://purl.uniprot.org/annotation/VAR_006778|||http://purl.uniprot.org/annotation/VAR_006779|||http://purl.uniprot.org/annotation/VAR_006780|||http://purl.uniprot.org/annotation/VAR_006781|||http://purl.uniprot.org/annotation/VAR_006782|||http://purl.uniprot.org/annotation/VAR_006783|||http://purl.uniprot.org/annotation/VAR_006784|||http://purl.uniprot.org/annotation/VAR_006785|||http://purl.uniprot.org/annotation/VAR_006786|||http://purl.uniprot.org/annotation/VAR_006787|||http://purl.uniprot.org/annotation/VAR_006788|||http://purl.uniprot.org/annotation/VAR_006789|||http://purl.uniprot.org/annotation/VAR_006790|||http://purl.uniprot.org/annotation/VAR_006791|||http://purl.uniprot.org/annotation/VAR_006792|||http://purl.uniprot.org/annotation/VAR_006793|||http://purl.uniprot.org/annotation/VAR_006794|||http://purl.uniprot.org/annotation/VAR_006795|||http://purl.uniprot.org/annotation/VAR_006796|||http://purl.uniprot.org/annotation/VAR_006797|||http://purl.uniprot.org/annotation/VAR_006798|||http://purl.uniprot.org/annotation/VAR_006799|||http://purl.uniprot.org/annotation/VAR_006800|||http://purl.uniprot.org/annotation/VAR_006801|||http://purl.uniprot.org/annotation/VAR_006802|||http://purl.uniprot.org/annotation/VAR_006803|||http://purl.uniprot.org/annotation/VAR_006804|||http://purl.uniprot.org/annotation/VAR_006805|||http://purl.uniprot.org/annotation/VAR_006806|||http://purl.uniprot.org/annotation/VAR_012312|||http://purl.uniprot.org/annotation/VAR_071609|||http://purl.uniprot.org/annotation/VAR_071610|||http://purl.uniprot.org/annotation/VAR_071611|||http://purl.uniprot.org/annotation/VAR_071612|||http://purl.uniprot.org/annotation/VAR_071613|||http://purl.uniprot.org/annotation/VAR_071614|||http://purl.uniprot.org/annotation/VAR_071615|||http://purl.uniprot.org/annotation/VAR_071616|||http://purl.uniprot.org/annotation/VAR_071617|||http://purl.uniprot.org/annotation/VAR_071618|||http://purl.uniprot.org/annotation/VAR_071619|||http://purl.uniprot.org/annotation/VAR_071620|||http://purl.uniprot.org/annotation/VAR_071621|||http://purl.uniprot.org/annotation/VAR_071622|||http://purl.uniprot.org/annotation/VAR_071623
http://togogenome.org/gene/9606:CA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22748                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-carbonic anhydrase|||Carbonic anhydrase 4|||GPI-anchor amidated serine|||In RP17.|||In RP17; abolishes carbonate dehydratase activity; impaired SLC4A4 cotransporter activity stimulation.|||In RP17; abolishes interaction with SLC4A4; impaired SLC4A4 cotransporter activity stimulation.|||In RP17; has no effect on carbonate dehydratase activity; loss of interaction with SLC4A4.|||In isoform 2.|||Loss of C-terminal domain removal and abolishes carbonate dehydratase activity.|||Proton donor/acceptor|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004226|||http://purl.uniprot.org/annotation/PRO_0000004227|||http://purl.uniprot.org/annotation/VAR_024749|||http://purl.uniprot.org/annotation/VAR_024750|||http://purl.uniprot.org/annotation/VAR_048680|||http://purl.uniprot.org/annotation/VAR_071430|||http://purl.uniprot.org/annotation/VAR_071431|||http://purl.uniprot.org/annotation/VAR_071432|||http://purl.uniprot.org/annotation/VSP_055973|||http://purl.uniprot.org/annotation/VSP_055974
http://togogenome.org/gene/9606:GLCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94923                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Almost abolishes enzyme activity.|||Critical for catalysis|||Cytoplasmic|||D-glucuronyl C5-epimerase|||Helical; Signal-anchor for type II membrane protein|||Loss of enzyme activity.|||Lumenal|||Mildly decreased enzyme activity.|||N-linked (GlcNAc...) asparagine|||Reduces enzyme activity by about 30%.|||Reduces enzyme activity by about 60%.|||Reduces enzyme activity by about 75%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192645|||http://purl.uniprot.org/annotation/VAR_055837|||http://purl.uniprot.org/annotation/VAR_057958
http://togogenome.org/gene/9606:PHLDB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NSJ2|||http://purl.uniprot.org/uniprot/Q96HZ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PH|||Pleckstrin homology-like domain family B member 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053896|||http://purl.uniprot.org/annotation/VAR_056671|||http://purl.uniprot.org/annotation/VSP_039923|||http://purl.uniprot.org/annotation/VSP_039924
http://togogenome.org/gene/9606:CDC73                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Found in a Wilms tumor sample; somatic mutation.|||Found in a clear cell renal carcinoma sample; somatic mutation; unlike wild-type protein the mutant is defective in suppressing CCND1 expression in vivo.|||Found in a parathyroid adenoma sample.|||Found in a parathyroid carcinoma sample; somatic mutation.|||Found in a patient with isolated hyperparathyroidism and parathyroid adenomas.|||Found in parathyroid adenoma samples; somatic mutation; parathyroid adenoma samples are from a patient with isolated hyperparathyroidism who also carries germline mutation P-91.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In HRPT1; does not affect interaction with the Pfa1 complex.|||In HRPT1; unknown pathological significance.|||In HRPT1; unknown pathological significance; found as somatic mutation in a parathyroid adenoma sample from a patient who also carries a germline frameshift mutation.|||In HRPT2.|||In HRPT2; unknown pathological significance; found as somatic mutation in a parathyroid carcinoma sample from a patient who also carries a germline mutation causing a splicing defect.|||Interaction with CTNNB1|||Interaction with POLR2A and PAF1|||N-acetylalanine|||Nuclear localization signal|||Parafibromin|||Phosphoserine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191803|||http://purl.uniprot.org/annotation/VAR_024082|||http://purl.uniprot.org/annotation/VAR_031825|||http://purl.uniprot.org/annotation/VAR_064927|||http://purl.uniprot.org/annotation/VAR_064928|||http://purl.uniprot.org/annotation/VAR_064929|||http://purl.uniprot.org/annotation/VAR_064930|||http://purl.uniprot.org/annotation/VAR_064931|||http://purl.uniprot.org/annotation/VAR_064932|||http://purl.uniprot.org/annotation/VAR_064933|||http://purl.uniprot.org/annotation/VAR_064934|||http://purl.uniprot.org/annotation/VAR_064935|||http://purl.uniprot.org/annotation/VAR_064936
http://togogenome.org/gene/9606:RGPD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NKT7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||Phosphoserine|||Polar residues|||RanBD1 1|||RanBD1 2|||RanBP2-like and GRIP domain-containing protein 3|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340666
http://togogenome.org/gene/9606:BABAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXR7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BRISC and BRCA1-A complex member 2|||In isoform 1.|||In isoform 3.|||In isoform 4.|||N-acetylmethionine|||Phosphoserine|||UEV-like 1|||UEV-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000224189|||http://purl.uniprot.org/annotation/VSP_037261|||http://purl.uniprot.org/annotation/VSP_051956|||http://purl.uniprot.org/annotation/VSP_051957
http://togogenome.org/gene/9606:HSBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75506                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict                                                                                  ^@                                                                                  Heat shock factor-binding protein 1|||Loss of interaction with HSF1; in association with K-16.|||Loss of interaction with HSF1; in association with K-19.|||Loss of interaction with HSF1; in association with K-45.|||Loss of interaction with HSF1; in association with K-48.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124805
http://togogenome.org/gene/9606:OVOL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14753                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||Putative transcription factor Ovo-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047011
http://togogenome.org/gene/9606:HOXA10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31260                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-A10|||In isoform 2.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200090|||http://purl.uniprot.org/annotation/VSP_002384|||http://purl.uniprot.org/annotation/VSP_002385
http://togogenome.org/gene/9606:DEPDC1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUY9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEP|||DEP domain-containing protein 1B|||In isoform 2.|||Phosphoserine|||Rho-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284790|||http://purl.uniprot.org/annotation/VAR_031819|||http://purl.uniprot.org/annotation/VAR_031820|||http://purl.uniprot.org/annotation/VSP_042922
http://togogenome.org/gene/9606:SLC66A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N2U9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||PQ-loop 1|||PQ-loop 2|||Phosphoserine|||Solute carrier family 66 member 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282430|||http://purl.uniprot.org/annotation/VAR_035979|||http://purl.uniprot.org/annotation/VSP_024145|||http://purl.uniprot.org/annotation/VSP_043275|||http://purl.uniprot.org/annotation/VSP_043276
http://togogenome.org/gene/9606:PNPLA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZV29                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||DGA/G|||Disordered|||GXGXXG|||GXSXG|||Helical|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Involved in the binding to lipid droplets|||Lumenal|||Nucleophile|||PNPLA|||Patatin-like phospholipase domain-containing protein 7|||Phosphoserine|||Phosphothreonine|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293489|||http://purl.uniprot.org/annotation/VAR_033060|||http://purl.uniprot.org/annotation/VAR_033061|||http://purl.uniprot.org/annotation/VAR_033062|||http://purl.uniprot.org/annotation/VAR_033063|||http://purl.uniprot.org/annotation/VAR_033064|||http://purl.uniprot.org/annotation/VAR_033065|||http://purl.uniprot.org/annotation/VAR_033066|||http://purl.uniprot.org/annotation/VAR_055696|||http://purl.uniprot.org/annotation/VAR_055697|||http://purl.uniprot.org/annotation/VAR_060409|||http://purl.uniprot.org/annotation/VAR_061139|||http://purl.uniprot.org/annotation/VSP_026500|||http://purl.uniprot.org/annotation/VSP_026501|||http://purl.uniprot.org/annotation/VSP_026502|||http://purl.uniprot.org/annotation/VSP_026503|||http://purl.uniprot.org/annotation/VSP_026504|||http://purl.uniprot.org/annotation/VSP_026505
http://togogenome.org/gene/9606:ACTL7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK03|||http://purl.uniprot.org/uniprot/Q9Y615                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Abolishes interaction with TES.|||Actin-like protein 7A|||Actin-like protein 7A N-terminal|||Disordered|||Found in two infertile brothers from a consanguineous family. The brothers present normal semen analysis, but both couples have no embryos for transfer after several IVF and intracytoplasmic sperm injection. The sperm of the affected brothers dysplay acrosomal ultrastructural defects.|||Polar residues|||Required for interaction with TES                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089137|||http://purl.uniprot.org/annotation/VAR_024362|||http://purl.uniprot.org/annotation/VAR_031425|||http://purl.uniprot.org/annotation/VAR_033460|||http://purl.uniprot.org/annotation/VAR_060998|||http://purl.uniprot.org/annotation/VAR_085430
http://togogenome.org/gene/9606:FAM72B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X60                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Protein FAM72B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340258|||http://purl.uniprot.org/annotation/VAR_044011|||http://purl.uniprot.org/annotation/VAR_044012|||http://purl.uniprot.org/annotation/VSP_034206
http://togogenome.org/gene/9606:ERN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5YM46|||http://purl.uniprot.org/uniprot/A5YM65|||http://purl.uniprot.org/uniprot/E7ETG2|||http://purl.uniprot.org/uniprot/Q76MJ5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||KEN|||Loss of autophosphorylation, of induction of apoptosis and of 28S rRNA cleavage, attenuation of repression of protein synthesis.|||Lumenal|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase/endoribonuclease IRE2|||non-specific serine/threonine protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024329|||http://purl.uniprot.org/annotation/PRO_5002687923|||http://purl.uniprot.org/annotation/PRO_5002688582|||http://purl.uniprot.org/annotation/PRO_5003217532|||http://purl.uniprot.org/annotation/VAR_040495|||http://purl.uniprot.org/annotation/VAR_040496|||http://purl.uniprot.org/annotation/VAR_040497|||http://purl.uniprot.org/annotation/VAR_040498|||http://purl.uniprot.org/annotation/VAR_040499|||http://purl.uniprot.org/annotation/VAR_040500|||http://purl.uniprot.org/annotation/VAR_040501|||http://purl.uniprot.org/annotation/VAR_040502|||http://purl.uniprot.org/annotation/VAR_040503|||http://purl.uniprot.org/annotation/VAR_040504
http://togogenome.org/gene/9606:TMX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3N1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Loss of reductase activity; when associated with S-56.|||Loss of reductase activity; when associated with S-59.|||Phosphoserine|||Polar residues|||Redox-active|||Thioredoxin|||Thioredoxin-related transmembrane protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034153
http://togogenome.org/gene/9606:TDRKH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ68|||http://purl.uniprot.org/uniprot/Q9Y2W6                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||KH 1|||KH 2|||Phosphoserine|||Tudor|||Tudor and KH domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050141|||http://purl.uniprot.org/annotation/VAR_055980|||http://purl.uniprot.org/annotation/VSP_040981
http://togogenome.org/gene/9606:DNAAF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPE2|||http://purl.uniprot.org/uniprot/Q86Y56                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dynein axonemal assembly factor 5|||HEAT|||HEAT 1|||HEAT 10|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||HEAT 7|||HEAT 8|||HEAT 9|||In CILD18; decreased protein abundance.|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050820|||http://purl.uniprot.org/annotation/VAR_056911|||http://purl.uniprot.org/annotation/VAR_060463|||http://purl.uniprot.org/annotation/VAR_060464|||http://purl.uniprot.org/annotation/VAR_068969|||http://purl.uniprot.org/annotation/VSP_016109|||http://purl.uniprot.org/annotation/VSP_016110
http://togogenome.org/gene/9606:ZNF273                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14593                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8; degenerate|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 273                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047500|||http://purl.uniprot.org/annotation/VAR_059077|||http://purl.uniprot.org/annotation/VAR_059078|||http://purl.uniprot.org/annotation/VSP_038180
http://togogenome.org/gene/9606:CCDC97                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96F63                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Coiled-coil domain-containing protein 97|||Disordered|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286096
http://togogenome.org/gene/9606:STK38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15208                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Decreases autophosphorylation and kinase activity.|||Decreases autophosphorylation and kinase activity. Reduced binding of S100B.|||In a metastatic melanoma sample; somatic mutation.|||Interaction with S100B|||Loss of autophosphorylation and kinase activity.|||N-acetylalanine|||Phosphoserine|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphothreonine; by STK24/MST3|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086718|||http://purl.uniprot.org/annotation/VAR_041196|||http://purl.uniprot.org/annotation/VAR_041197|||http://purl.uniprot.org/annotation/VAR_041198
http://togogenome.org/gene/9606:UGT1A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35504|||http://purl.uniprot.org/uniprot/Q5DSZ9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||UDP-glucuronosyltransferase|||UDP-glucuronosyltransferase 1A5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036004|||http://purl.uniprot.org/annotation/PRO_5009998734|||http://purl.uniprot.org/annotation/VAR_052455|||http://purl.uniprot.org/annotation/VAR_052456|||http://purl.uniprot.org/annotation/VAR_052457|||http://purl.uniprot.org/annotation/VAR_052458|||http://purl.uniprot.org/annotation/VAR_052459|||http://purl.uniprot.org/annotation/VAR_052460|||http://purl.uniprot.org/annotation/VAR_052461|||http://purl.uniprot.org/annotation/VAR_059845|||http://purl.uniprot.org/annotation/VAR_059846|||http://purl.uniprot.org/annotation/VSP_053961
http://togogenome.org/gene/9606:LCE2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA79                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 2A|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235330|||http://purl.uniprot.org/annotation/VAR_062118
http://togogenome.org/gene/9606:NOL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6H8Z4|||http://purl.uniprot.org/uniprot/Q76FK4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 4.|||Nucleolar protein 8|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239443|||http://purl.uniprot.org/annotation/VAR_052211|||http://purl.uniprot.org/annotation/VAR_052212|||http://purl.uniprot.org/annotation/VAR_052213|||http://purl.uniprot.org/annotation/VAR_052214|||http://purl.uniprot.org/annotation/VAR_061830|||http://purl.uniprot.org/annotation/VSP_052055|||http://purl.uniprot.org/annotation/VSP_052056
http://togogenome.org/gene/9606:KRTAP4-2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYR5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||20 X 5 AA repeats OF C-C-[GRQVS]-[SPT]-[VSTQ]|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 4-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185170|||http://purl.uniprot.org/annotation/VAR_060241
http://togogenome.org/gene/9606:CNGA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXY3|||http://purl.uniprot.org/uniprot/Q16280                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cyclic nucleotide-binding|||Cyclic nucleotide-gated olfactory channel|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=H1|||Helical; Name=H2|||Helical; Name=H3|||Helical; Name=H4|||Helical; Name=H5|||Helical; Name=H6|||In a breast cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219312|||http://purl.uniprot.org/annotation/VAR_036603|||http://purl.uniprot.org/annotation/VAR_036604|||http://purl.uniprot.org/annotation/VAR_048748|||http://purl.uniprot.org/annotation/VAR_048749|||http://purl.uniprot.org/annotation/VAR_061107
http://togogenome.org/gene/9606:TRIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0J9YW02|||http://purl.uniprot.org/uniprot/A0A6Q8PG16|||http://purl.uniprot.org/uniprot/Q9C040                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||Disordered|||Filamin|||In CMT2R; reduced stability of the mutant protein.|||In isoform 2.|||NHL|||NHL 1|||NHL 2|||NHL 3|||NHL 4|||NHL 5|||NHL 6|||Phosphoserine|||Phosphothreonine|||RING-type|||Tripartite motif-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056195|||http://purl.uniprot.org/annotation/VAR_070874|||http://purl.uniprot.org/annotation/VSP_046923
http://togogenome.org/gene/9606:TSPY10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CV98|||http://purl.uniprot.org/uniprot/P0CW01|||http://purl.uniprot.org/uniprot/Q01534                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Testis-specific Y-encoded protein 1|||Testis-specific Y-encoded protein 10|||Testis-specific Y-encoded protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185668|||http://purl.uniprot.org/annotation/PRO_0000408001|||http://purl.uniprot.org/annotation/PRO_0000408004|||http://purl.uniprot.org/annotation/VAR_016226|||http://purl.uniprot.org/annotation/VAR_016227|||http://purl.uniprot.org/annotation/VAR_016228|||http://purl.uniprot.org/annotation/VSP_008012
http://togogenome.org/gene/9606:AKR1C4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17516                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aldo-keto reductase family 1 member C4|||Important for substrate specificity|||Lowers pKa of active site Tyr|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124640|||http://purl.uniprot.org/annotation/VAR_013290|||http://purl.uniprot.org/annotation/VAR_013291|||http://purl.uniprot.org/annotation/VAR_028240|||http://purl.uniprot.org/annotation/VAR_028241|||http://purl.uniprot.org/annotation/VAR_028242
http://togogenome.org/gene/9606:LDOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95751                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Protein LDOC1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084391
http://togogenome.org/gene/9606:H3C15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71DI3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Abolishes S-palmitoylation.|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.2|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphotyrosine|||S-palmitoyl cysteine|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250357|||http://purl.uniprot.org/annotation/VAR_059313|||http://purl.uniprot.org/annotation/VAR_059314
http://togogenome.org/gene/9606:SLC30A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU87|||http://purl.uniprot.org/uniprot/B5MCR8|||http://purl.uniprot.org/uniprot/Q6NXT4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||No effect on heterodimer formation with SLC30A5 and no effect on zinc transport; when associated with A-205.|||No effect on heterodimer formation with SLC30A5 and no effect on zinc transport; when associated with A-70.|||No effect on heterodimer formation with SLC30A5 and no effect on zinc transport; when associated with H-201.|||No effect on heterodimer formation with SLC30A5 and no effect on zinc transport; when associated with H-66.|||Zinc transporter 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312573|||http://purl.uniprot.org/annotation/VSP_029861|||http://purl.uniprot.org/annotation/VSP_029862|||http://purl.uniprot.org/annotation/VSP_045198
http://togogenome.org/gene/9606:TMEM209                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJX5|||http://purl.uniprot.org/uniprot/Q96SK2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Transmembrane protein 209                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331632|||http://purl.uniprot.org/annotation/VAR_042918|||http://purl.uniprot.org/annotation/VAR_042919|||http://purl.uniprot.org/annotation/VSP_033280|||http://purl.uniprot.org/annotation/VSP_033281|||http://purl.uniprot.org/annotation/VSP_033282|||http://purl.uniprot.org/annotation/VSP_033283
http://togogenome.org/gene/9606:MTHFD1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVM4|||http://purl.uniprot.org/uniprot/B2RD24|||http://purl.uniprot.org/uniprot/B7ZM99|||http://purl.uniprot.org/uniprot/Q6UB35                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Formyltetrahydrofolate synthetase|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Methylenetetrahydrofolate dehydrogenase and cyclohydrolase|||Mitochondrion|||Monofunctional C1-tetrahydrofolate synthase, mitochondrial|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Phosphoserine|||Tetrahydrofolate dehydrogenase/cyclohydrolase NAD(P)-binding|||Tetrahydrofolate dehydrogenase/cyclohydrolase catalytic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343177|||http://purl.uniprot.org/annotation/VAR_044346|||http://purl.uniprot.org/annotation/VSP_034565|||http://purl.uniprot.org/annotation/VSP_034566
http://togogenome.org/gene/9606:CDKL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H7BZI6|||http://purl.uniprot.org/uniprot/Q5MAI5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-dependent kinase-like 4|||Disordered|||In isoform 2.|||Protein kinase|||Proton acceptor|||[NKR]KIAxRE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085824|||http://purl.uniprot.org/annotation/VAR_041992|||http://purl.uniprot.org/annotation/VAR_041993|||http://purl.uniprot.org/annotation/VAR_041994|||http://purl.uniprot.org/annotation/VAR_041995|||http://purl.uniprot.org/annotation/VAR_041996|||http://purl.uniprot.org/annotation/VAR_053930|||http://purl.uniprot.org/annotation/VSP_055220
http://togogenome.org/gene/9606:RSPH9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1X1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In CILD12.|||In isoform 2.|||Radial spoke head protein 9 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089561|||http://purl.uniprot.org/annotation/VAR_050815|||http://purl.uniprot.org/annotation/VAR_055236|||http://purl.uniprot.org/annotation/VSP_042934|||http://purl.uniprot.org/annotation/VSP_042935
http://togogenome.org/gene/9606:PLXND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4D7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||In CHTD9.|||In CHTD9; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Plexin-D1|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024676|||http://purl.uniprot.org/annotation/VAR_022144|||http://purl.uniprot.org/annotation/VAR_056723|||http://purl.uniprot.org/annotation/VAR_056724|||http://purl.uniprot.org/annotation/VAR_059558|||http://purl.uniprot.org/annotation/VAR_061539|||http://purl.uniprot.org/annotation/VAR_088299|||http://purl.uniprot.org/annotation/VAR_088300|||http://purl.uniprot.org/annotation/VAR_088301|||http://purl.uniprot.org/annotation/VAR_088302|||http://purl.uniprot.org/annotation/VSP_011516
http://togogenome.org/gene/9606:H3C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P68431                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  5-glutamyl dopamine; alternate|||5-glutamyl serotonin; alternate|||ADP-ribosylserine; alternate|||Allysine; alternate|||Asymmetric dimethylarginine; by CARM1; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Citrulline|||Citrulline; alternate|||Disordered|||Histone H3.1|||In GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels.|||N6,N6,N6-trimethyllysine; alternate|||N6,N6-dimethyllysine; alternate|||N6-(2-hydroxyisobutyryl)lysine; alternate|||N6-(beta-hydroxybutyryl)lysine; alternate|||N6-acetyllysine; alternate|||N6-butyryllysine; alternate|||N6-crotonyllysine; alternate|||N6-decanoyllysine|||N6-glutaryllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||N6-methyllysine; alternate|||N6-methyllysine; by EHMT2; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5|||Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5|||Phosphothreonine|||Phosphothreonine; by HASPIN|||Phosphothreonine; by PKC|||Phosphothreonine; by PKC and CHEK1|||Phosphotyrosine|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Probable disease-associated variant found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels.|||Removed|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221245|||http://purl.uniprot.org/annotation/VAR_079018|||http://purl.uniprot.org/annotation/VAR_079019|||http://purl.uniprot.org/annotation/VAR_079020
http://togogenome.org/gene/9606:BCAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXM8|||http://purl.uniprot.org/uniprot/P50895                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basal cell adhesion molecule|||Cytoplasmic|||Defines the Lu(a) antigen.|||Disordered|||Dramatically reduced cell adhesion.|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type 1|||Ig-like V-type 2|||Interaction with laminin alpha5|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by CK2|||Phosphoserine; by GSK3|||Phosphoserine; by PKA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014850|||http://purl.uniprot.org/annotation/PRO_5030002789|||http://purl.uniprot.org/annotation/VAR_021348|||http://purl.uniprot.org/annotation/VAR_021349|||http://purl.uniprot.org/annotation/VAR_021350|||http://purl.uniprot.org/annotation/VAR_021351|||http://purl.uniprot.org/annotation/VAR_021352|||http://purl.uniprot.org/annotation/VAR_021353|||http://purl.uniprot.org/annotation/VAR_021354|||http://purl.uniprot.org/annotation/VAR_021355
http://togogenome.org/gene/9606:ELMOD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ81                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  ELMO|||ELMO domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225017
http://togogenome.org/gene/9606:FAM86B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C5J1                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  N-acetylmethionine|||Putative protein N-methyltransferase FAM86B2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307639|||http://purl.uniprot.org/annotation/VAR_036617|||http://purl.uniprot.org/annotation/VAR_036618
http://togogenome.org/gene/9606:TEDDM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T9Z0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane epididymal protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307129|||http://purl.uniprot.org/annotation/VAR_035356
http://togogenome.org/gene/9606:TBC1D9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KM54|||http://purl.uniprot.org/uniprot/Q66K14|||http://purl.uniprot.org/uniprot/Q9BW24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Arginine finger|||Basic and acidic residues|||Disordered|||EF-hand|||GRAM 1|||GRAM 2|||Glutamine finger|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Rab-GAP TBC|||TBC1 domain family member 9B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288501|||http://purl.uniprot.org/annotation/VAR_032440|||http://purl.uniprot.org/annotation/VAR_032441|||http://purl.uniprot.org/annotation/VAR_032442|||http://purl.uniprot.org/annotation/VAR_036196|||http://purl.uniprot.org/annotation/VSP_025699
http://togogenome.org/gene/9606:TPK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y0|||http://purl.uniprot.org/uniprot/F5GZG6|||http://purl.uniprot.org/uniprot/Q9H3S4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In THMD5.|||In isoform 2.|||Thiamin pyrophosphokinase 1|||Thiamin pyrophosphokinase thiamin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072647|||http://purl.uniprot.org/annotation/VAR_067391|||http://purl.uniprot.org/annotation/VAR_067392|||http://purl.uniprot.org/annotation/VAR_067393|||http://purl.uniprot.org/annotation/VSP_056302|||http://purl.uniprot.org/annotation/VSP_056303
http://togogenome.org/gene/9606:ENTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96C92                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Disrupts interaction with PTPN13.|||Endosome-associated-trafficking regulator 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Polar residues|||Required for interaction with PTPN13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000324285|||http://purl.uniprot.org/annotation/VAR_039687|||http://purl.uniprot.org/annotation/VAR_039688|||http://purl.uniprot.org/annotation/VAR_039689|||http://purl.uniprot.org/annotation/VAR_039690|||http://purl.uniprot.org/annotation/VAR_039691|||http://purl.uniprot.org/annotation/VSP_032176|||http://purl.uniprot.org/annotation/VSP_032177|||http://purl.uniprot.org/annotation/VSP_040477
http://togogenome.org/gene/9606:ZNF688                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z633|||http://purl.uniprot.org/uniprot/P0C7X2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 688                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234007|||http://purl.uniprot.org/annotation/VAR_052896|||http://purl.uniprot.org/annotation/VSP_046955
http://togogenome.org/gene/9606:CBL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22681                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  4H|||Abolishes interaction with ZAP70 and EPHB1, but does not affect interaction with SLA. Reduces ubiquitination and therefore proteasomal degradation of SPRED2.|||Abolishes interaction with ZAP70.|||Cbl-PTB|||Disordered|||Does not affect interaction with TNS4 following EGF stimulation.|||Does not affect interaction with TNS4 following EGF stimulation. Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-774.|||E3 ubiquitin-protein ligase CBL|||EF-hand-like|||Found in patients with acute myeloid leukemia; unknown pathological significance.|||Found in patients with acute myeloid leukemia; unknown pathological significance; loss of the ability to negatively regulate signaling pathways; promotes cell cycle progression; decreases apoptosis.|||In NSLL.|||In NSLL; dominant-negative; impairs CBL-mediated ubiquitination, internalization and degradation of the EGF receptor/EGFR; decreases the ability to negatively regulate EGFR signaling.|||Interaction with CD2AP|||Linker|||Loss of interaction with TNS4 following EGF stimulation. Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-700.|||Loss of ubiquitin ligase activity.|||No effect on tyrosine phosphorylation by INSR. Loss of phosphorylation by SRC. Inhibition of bone resorption. Abolishes interaction with PIK3R1. Does not affect interaction with TNS4 following EGF stimulation.|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by ABL1|||Phosphotyrosine; by INSR|||Phosphotyrosine; by SRC|||Polar residues|||Pro residues|||RING-type|||Required for ubiquitination of SPRED2|||SH2-like|||Strongly reduces tyrosine phosphorylation by INSR; when associated with F-700 and F-774.|||Sufficient for interaction with EPHB1|||UBA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055858|||http://purl.uniprot.org/annotation/VAR_057211|||http://purl.uniprot.org/annotation/VAR_057212|||http://purl.uniprot.org/annotation/VAR_057213|||http://purl.uniprot.org/annotation/VAR_064332|||http://purl.uniprot.org/annotation/VAR_064333|||http://purl.uniprot.org/annotation/VAR_064334|||http://purl.uniprot.org/annotation/VAR_064335|||http://purl.uniprot.org/annotation/VAR_071040|||http://purl.uniprot.org/annotation/VAR_071041|||http://purl.uniprot.org/annotation/VAR_071042|||http://purl.uniprot.org/annotation/VAR_071043
http://togogenome.org/gene/9606:TAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03519|||http://purl.uniprot.org/uniprot/Q5JNW1|||http://purl.uniprot.org/uniprot/Q9UP03                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1|||ABC transporter|||Antigen peptide transporter 2|||Complete loss of interaction with TAPBP, resulting in impaired PLC assembly and antigen presentation.|||Cytoplasmic|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In allele TAP2*01:02, allele TAP2*01D, allele TAP2*02E and allele TAP2*02F.|||In allele TAP2*01:03 and allele TAP2*01G.|||In allele TAP2*01D, allele TAP2*01E, allele TAP2*01G, allele TAP2*02C and allele TAP2*02F.|||In allele TAP2*01F and allele TAP2*02D.|||In allele TAP2*01F, allele TAP2*01G, allele TAP2*01H, allele TAP2*02B and allele TAP2*02D.|||In allele TAP2*02:01, allele TAP2*02B, allele TAP2*02C, allele TAP2*02D, allele TAP2*02E, allele TAP2*02F, allele TAP2*03A and allele TAP2*BKY2.|||In allele TAP2*02:01, allele TAP2*02B, allele TAP2*02C, allele TAP2*02D, allele TAP2*02E, allele TAP2*02F, allele TAP2*04A and allele TAP2*Bky2.|||In allele TAP2*BKY2.|||In isoform 2.|||Inactive in peptide transport when associated with 'A-734' of TAP1.|||Inter-subunit salt bridge with TAPBP|||Lumenal|||Part of the peptide-binding site|||Variant of uncertain significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093329|||http://purl.uniprot.org/annotation/VAR_000094|||http://purl.uniprot.org/annotation/VAR_000095|||http://purl.uniprot.org/annotation/VAR_000096|||http://purl.uniprot.org/annotation/VAR_000097|||http://purl.uniprot.org/annotation/VAR_000098|||http://purl.uniprot.org/annotation/VAR_014997|||http://purl.uniprot.org/annotation/VAR_014998|||http://purl.uniprot.org/annotation/VAR_014999|||http://purl.uniprot.org/annotation/VAR_015000|||http://purl.uniprot.org/annotation/VAR_036873|||http://purl.uniprot.org/annotation/VSP_038904
http://togogenome.org/gene/9606:OR1J2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW18|||http://purl.uniprot.org/uniprot/Q8NGS2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1J2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150439|||http://purl.uniprot.org/annotation/VAR_053123|||http://purl.uniprot.org/annotation/VAR_062010
http://togogenome.org/gene/9606:PVRIG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DKI7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||No effect on global phosphorylation.|||Phosphotyrosine|||Reduced phosphorylation.|||Transmembrane protein PVRIG                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337142|||http://purl.uniprot.org/annotation/VAR_043624
http://togogenome.org/gene/9606:ABTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N961                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||Ankyrin repeat and BTB/POZ domain-containing protein 2|||BTB|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066887|||http://purl.uniprot.org/annotation/VAR_022087|||http://purl.uniprot.org/annotation/VAR_024171|||http://purl.uniprot.org/annotation/VSP_046439
http://togogenome.org/gene/9606:KIAA2013                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYS2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Uncharacterized protein KIAA2013                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000293468|||http://purl.uniprot.org/annotation/VSP_026487
http://togogenome.org/gene/9606:FUT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22083                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-(1,3)-fucosyltransferase 4|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform Short.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221100|||http://purl.uniprot.org/annotation/VAR_055844|||http://purl.uniprot.org/annotation/VSP_061247
http://togogenome.org/gene/9606:CKMT1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12532                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Cardiolipin-binding|||Creatine kinase U-type, mitochondrial|||In isoform 2.|||Mitochondrion|||Phosphagen kinase C-terminal|||Phosphagen kinase N-terminal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016590|||http://purl.uniprot.org/annotation/VSP_038045
http://togogenome.org/gene/9606:KCNMB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W47                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Calcium-activated potassium channel subunit beta-4|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Loss of N-glycosylation and reduced protection against charybdotoxin; when associated with A-53.|||Loss of N-glycosylation and reduced protection against charybdotoxin; when associated with A-90.|||N-linked (GlcNAc...) asparagine|||Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with D-11 and E-17.|||Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with D-11 and E-210.|||Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with E-17 and E-210.|||Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-11 and A-17.|||Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-11 and A-210.|||Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-17 and A-210.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187055|||http://purl.uniprot.org/annotation/VAR_018178
http://togogenome.org/gene/9606:OR4C3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVR6|||http://purl.uniprot.org/uniprot/A0A126GW65|||http://purl.uniprot.org/uniprot/Q8NH37                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor|||Olfactory receptor 4C3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150529|||http://purl.uniprot.org/annotation/PRO_5014041219
http://togogenome.org/gene/9606:KIF1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3IT28|||http://purl.uniprot.org/uniprot/A0A3B3ITE5|||http://purl.uniprot.org/uniprot/A0A3B3IU40|||http://purl.uniprot.org/uniprot/Q12756                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FHA|||In KAND.|||In KAND; affects subcellular location and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows a strongly reduced velocity.|||In KAND; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; may decrease interaction with microtubules.|||In KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells.|||In KAND; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; complete loss of motility, when tested in vitro.|||In KAND; affects subcellular location; strong decrease in localization at the distal tip of neurites and accumulation in the neuronal cell body, when assayed in differentiated SH-SY5Y cells.|||In KAND; complete loss of motility, when tested in vitro.|||In KAND; retains its ability to move processively along microtubules, but shows reduced velocity and processivity; decreased interaction with microtubules.|||In KAND; strong decrease in localization at the distal tip of neurites and accumulation in the neuronal cell body, when assayed in differentiated SH-SY5Y cells.|||In KAND; unknown pathological significance.|||In NESCAVS and SPG30.|||In NESCAVS.|||In NESCAVS; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity and processivity; increased interaction with microtubules.|||In NESCAVS; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; small decrease of interaction with microtubules.|||In NESCAVS; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells.|||In NESCAVS; affects subcellular location; reduced distal localization and increased accumulation throughout the cell body and proximal neurites; disrupts microtubule motility.|||In NESCAVS; affects subcellular location; reduces accumulation in distal regions of the neurites.|||In NESCAVS; disrupts microtubule motility.|||In NESCAVS; reduces accumulation in distal regions of the neurites.|||In NESCAVS; reduces accumulation in distal regions of the neurites; disrupts microtubule motility.|||In NESCAVS; unknown pathological significance.|||In SPG30.|||In SPG30; affects subcellular location, binding to microtubules and motility; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells; retains its ability to move processively along microtubules, but shows reduced velocity; small decrease of interaction with microtubules.|||In SPG30; affects subcellular location; contrary to wild-type, does not accumulate in the distal tips of differentiated SH-SY5Y cells, but localizes closer to the cell body in transfected cells.|||In SPG30; reduces accumulation in distal regions of the neurites.|||In SPG30; reduces accumulation in distal regions of the neurites; no effect on microtubule motility.|||In SPG30; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||Kinesin motor|||Kinesin-like protein KIF1A|||No effect on microtubule motility.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125405|||http://purl.uniprot.org/annotation/VAR_066649|||http://purl.uniprot.org/annotation/VAR_066650|||http://purl.uniprot.org/annotation/VAR_075471|||http://purl.uniprot.org/annotation/VAR_075472|||http://purl.uniprot.org/annotation/VAR_075473|||http://purl.uniprot.org/annotation/VAR_075474|||http://purl.uniprot.org/annotation/VAR_075475|||http://purl.uniprot.org/annotation/VAR_075476|||http://purl.uniprot.org/annotation/VAR_075477|||http://purl.uniprot.org/annotation/VAR_075478|||http://purl.uniprot.org/annotation/VAR_075479|||http://purl.uniprot.org/annotation/VAR_075480|||http://purl.uniprot.org/annotation/VAR_075481|||http://purl.uniprot.org/annotation/VAR_075482|||http://purl.uniprot.org/annotation/VAR_075483|||http://purl.uniprot.org/annotation/VAR_075484|||http://purl.uniprot.org/annotation/VAR_075485|||http://purl.uniprot.org/annotation/VAR_075486|||http://purl.uniprot.org/annotation/VAR_075487|||http://purl.uniprot.org/annotation/VAR_075488|||http://purl.uniprot.org/annotation/VAR_075489|||http://purl.uniprot.org/annotation/VAR_075490|||http://purl.uniprot.org/annotation/VAR_075491|||http://purl.uniprot.org/annotation/VAR_077467|||http://purl.uniprot.org/annotation/VAR_077468|||http://purl.uniprot.org/annotation/VAR_077469|||http://purl.uniprot.org/annotation/VAR_083686|||http://purl.uniprot.org/annotation/VAR_083687|||http://purl.uniprot.org/annotation/VAR_083688|||http://purl.uniprot.org/annotation/VAR_083689|||http://purl.uniprot.org/annotation/VAR_083690|||http://purl.uniprot.org/annotation/VAR_083691|||http://purl.uniprot.org/annotation/VAR_083692|||http://purl.uniprot.org/annotation/VAR_083693|||http://purl.uniprot.org/annotation/VAR_083694|||http://purl.uniprot.org/annotation/VAR_083695|||http://purl.uniprot.org/annotation/VAR_083696|||http://purl.uniprot.org/annotation/VAR_083697|||http://purl.uniprot.org/annotation/VAR_083698|||http://purl.uniprot.org/annotation/VAR_083699|||http://purl.uniprot.org/annotation/VAR_083700|||http://purl.uniprot.org/annotation/VAR_083701|||http://purl.uniprot.org/annotation/VAR_083702|||http://purl.uniprot.org/annotation/VAR_083703|||http://purl.uniprot.org/annotation/VAR_083704|||http://purl.uniprot.org/annotation/VAR_083705|||http://purl.uniprot.org/annotation/VAR_083706|||http://purl.uniprot.org/annotation/VAR_083707|||http://purl.uniprot.org/annotation/VAR_083708|||http://purl.uniprot.org/annotation/VAR_083709|||http://purl.uniprot.org/annotation/VAR_083710|||http://purl.uniprot.org/annotation/VAR_083711|||http://purl.uniprot.org/annotation/VAR_086844|||http://purl.uniprot.org/annotation/VAR_086845|||http://purl.uniprot.org/annotation/VAR_086846|||http://purl.uniprot.org/annotation/VAR_086847|||http://purl.uniprot.org/annotation/VAR_086848|||http://purl.uniprot.org/annotation/VAR_086849|||http://purl.uniprot.org/annotation/VAR_086850|||http://purl.uniprot.org/annotation/VAR_086851|||http://purl.uniprot.org/annotation/VAR_086852|||http://purl.uniprot.org/annotation/VAR_086853|||http://purl.uniprot.org/annotation/VAR_086854|||http://purl.uniprot.org/annotation/VAR_086855|||http://purl.uniprot.org/annotation/VAR_086856|||http://purl.uniprot.org/annotation/VAR_086857|||http://purl.uniprot.org/annotation/VAR_086858|||http://purl.uniprot.org/annotation/VAR_086859|||http://purl.uniprot.org/annotation/VAR_086860|||http://purl.uniprot.org/annotation/VAR_086861|||http://purl.uniprot.org/annotation/VAR_086862|||http://purl.uniprot.org/annotation/VAR_086863|||http://purl.uniprot.org/annotation/VAR_086864|||http://purl.uniprot.org/annotation/VAR_086865|||http://purl.uniprot.org/annotation/VAR_086866|||http://purl.uniprot.org/annotation/VAR_086867|||http://purl.uniprot.org/annotation/VAR_086868|||http://purl.uniprot.org/annotation/VAR_086869|||http://purl.uniprot.org/annotation/VAR_086870|||http://purl.uniprot.org/annotation/VAR_086871|||http://purl.uniprot.org/annotation/VAR_086872|||http://purl.uniprot.org/annotation/VAR_086873|||http://purl.uniprot.org/annotation/VAR_086874|||http://purl.uniprot.org/annotation/VAR_086875|||http://purl.uniprot.org/annotation/VAR_086876|||http://purl.uniprot.org/annotation/VAR_086877|||http://purl.uniprot.org/annotation/VAR_086878|||http://purl.uniprot.org/annotation/VAR_086879|||http://purl.uniprot.org/annotation/VAR_086880|||http://purl.uniprot.org/annotation/VAR_086881|||http://purl.uniprot.org/annotation/VAR_086882|||http://purl.uniprot.org/annotation/VAR_086883|||http://purl.uniprot.org/annotation/VAR_086884|||http://purl.uniprot.org/annotation/VAR_086885|||http://purl.uniprot.org/annotation/VSP_021853|||http://purl.uniprot.org/annotation/VSP_021854|||http://purl.uniprot.org/annotation/VSP_021855
http://togogenome.org/gene/9606:SMLR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BR10                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Small leucine-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000421260
http://togogenome.org/gene/9606:CLEC11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y240                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Motif|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||C-type lectin|||C-type lectin domain family 11 member A|||Cell attachment site|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017468|||http://purl.uniprot.org/annotation/VAR_050116
http://togogenome.org/gene/9606:TPCN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSG7|||http://purl.uniprot.org/uniprot/B7Z3R2|||http://purl.uniprot.org/uniprot/Q9ULQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Pore-forming|||In isoform 2.|||In isoform 3.|||Ion transport|||Loss of NAADP-mediated cytoplasmic calcium release.|||Loss of voltage sensitivity.|||N-linked (GlcNAc...) asparagine|||No effect on subcellular location.|||Polar residues|||Two pore channel protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000276853|||http://purl.uniprot.org/annotation/VSP_023003|||http://purl.uniprot.org/annotation/VSP_023004|||http://purl.uniprot.org/annotation/VSP_023005|||http://purl.uniprot.org/annotation/VSP_041346
http://togogenome.org/gene/9606:AGAP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VVT9|||http://purl.uniprot.org/uniprot/Q99490                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Arf-GAP|||Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2|||Basic and acidic residues|||C4-type|||Disordered|||G domain|||In a breast cancer sample; somatic mutation.|||In a glioblastoma cell line.|||In a neuroblastoma cell line.|||In a sarcoma cell line.|||In isoform 2.|||Interaction with EPB41L1|||Interaction with PLCG1|||Interactions with HOMER1 and NF2|||PH|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074217|||http://purl.uniprot.org/annotation/VAR_022046|||http://purl.uniprot.org/annotation/VAR_026438|||http://purl.uniprot.org/annotation/VAR_026439|||http://purl.uniprot.org/annotation/VAR_026440|||http://purl.uniprot.org/annotation/VAR_026441|||http://purl.uniprot.org/annotation/VAR_026442|||http://purl.uniprot.org/annotation/VAR_026443|||http://purl.uniprot.org/annotation/VAR_026444|||http://purl.uniprot.org/annotation/VAR_026445|||http://purl.uniprot.org/annotation/VAR_036183|||http://purl.uniprot.org/annotation/VAR_036184|||http://purl.uniprot.org/annotation/VAR_055532|||http://purl.uniprot.org/annotation/VSP_018531|||http://purl.uniprot.org/annotation/VSP_018532|||http://purl.uniprot.org/annotation/VSP_018533
http://togogenome.org/gene/9606:SEC14L6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B5MCN3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent                                                                                  ^@                                                                                  CRAL-TRIO|||GOLD|||Putative SEC14-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410725
http://togogenome.org/gene/9606:HNRNPA1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32P51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Disordered|||Globular A domain|||Globular B domain|||Heterogeneous nuclear ribonucleoprotein A1-like 2|||N6-acetyllysine|||Nuclear targeting sequence|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||RNA-binding RGG-box|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318848|||http://purl.uniprot.org/annotation/VAR_038904
http://togogenome.org/gene/9606:DCPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTI8|||http://purl.uniprot.org/uniprot/Q96C86                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activates decapping activity to 120% of wild-type.|||Basic and acidic residues|||Disordered|||Histidine triad motif|||In ARS; results in a severe decrease of decapase activity.|||Increases cytoplasmic localization.|||Increases decapping activity to 125% of wild-type.|||Increases decapping activity to 140% of wild-type.|||Increases decapping activity to 180% of wild-type.|||Increases decapping activity to 250% of wild-type.|||Inhibits nuclear export to the cytoplasm.|||Loss of decapping activity.|||Loss of decapping activity. Does not inhibit cap structure and capped RNA binding. Preferentially hydrolyzes cap structure (m7GpppG) at least 2500-fold more efficiently than capped RNA (m7Gppp-RNA).|||N-acetylalanine|||N6-acetyllysine|||No effect.|||Nucleophile|||Phosphoserine|||Reduces decapping activity.|||Removed|||Strongly reduces decapping activity.|||m7GpppX diphosphatase|||nuclear export sequence (NES)|||nuclear localization signal (NLS)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000109794|||http://purl.uniprot.org/annotation/VAR_027958|||http://purl.uniprot.org/annotation/VAR_073956
http://togogenome.org/gene/9606:VPS11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXL6|||http://purl.uniprot.org/uniprot/B7Z879|||http://purl.uniprot.org/uniprot/Q9H270                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CHCR|||CHCR 1|||CHCR 2|||In DYT32; unknown pathological significance.|||In HLD12.|||N-acetylalanine|||Omega-N-methylarginine|||Phosphoserine|||RING-type|||Removed|||Vacuolar protein sorting-associated protein 11 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055902|||http://purl.uniprot.org/annotation/VAR_059813|||http://purl.uniprot.org/annotation/VAR_076393|||http://purl.uniprot.org/annotation/VAR_086501
http://togogenome.org/gene/9606:ATP6V1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38606                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of interaction with Rabies virus protein M; when associated with Q-256.|||Complete loss of interaction with Rabies virus protein M; when associated with Q-279.|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Found in a patient with severe developmental disorder; unknown pathological significance.|||In ARCL2D.|||In IECEE3; gain-of-function variant leading to decreased pH in intracellular organelles; affects neurite arborization and impairs the formation and maintenance of excitatory synapses, when tested in a heterologous system; not effect on subcellular location.|||In IECEE3; loss-of-function variant leading to increased pH in intracellular organelles; affects neurite arborization and impairs the formation and maintenance of excitatory synapses, when tested in a heterologous system; not effect on subcellular location.|||In IECEE3; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||Phosphoserine; by AMPK|||Phosphothreonine|||Removed|||V-type proton ATPase catalytic subunit A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144560|||http://purl.uniprot.org/annotation/VAR_078606|||http://purl.uniprot.org/annotation/VAR_078607|||http://purl.uniprot.org/annotation/VAR_080994|||http://purl.uniprot.org/annotation/VAR_080995|||http://purl.uniprot.org/annotation/VAR_080996|||http://purl.uniprot.org/annotation/VAR_080997|||http://purl.uniprot.org/annotation/VAR_080998|||http://purl.uniprot.org/annotation/VAR_080999|||http://purl.uniprot.org/annotation/VSP_056408
http://togogenome.org/gene/9606:EXO5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H790                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-343.|||Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-346.|||Does not affect exonuclease activity.|||Exonuclease V|||Nearly abolishes exonuclease activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307320|||http://purl.uniprot.org/annotation/VAR_035407|||http://purl.uniprot.org/annotation/VAR_035408
http://togogenome.org/gene/9606:GPR21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSD1|||http://purl.uniprot.org/uniprot/H9NIL4|||http://purl.uniprot.org/uniprot/Q99679                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Probable G-protein coupled receptor 21                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069542
http://togogenome.org/gene/9606:RBSN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5H3|||http://purl.uniprot.org/uniprot/Q9H1K0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||FYVE-type|||Found in a patient with intractable epileptic encephalopathy, developmental delay and additional multi-organ symptoms; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||Necessary for interaction with EHD1|||Necessary for interaction with RAB4A|||Necessary for interaction with RAB5A|||Necessary for the correct targeting to endosomes|||Phosphoserine|||Polar residues|||Rabenosyn-5|||Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628.|||Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664.|||Removed|||UIM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098711|||http://purl.uniprot.org/annotation/VAR_052982|||http://purl.uniprot.org/annotation/VAR_052983|||http://purl.uniprot.org/annotation/VAR_052984|||http://purl.uniprot.org/annotation/VAR_072416|||http://purl.uniprot.org/annotation/VSP_056003|||http://purl.uniprot.org/annotation/VSP_056004
http://togogenome.org/gene/9606:KCTD19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q17RG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  BTB 1|||BTB 2|||BTB/POZ domain-containing protein KCTD19|||Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313587|||http://purl.uniprot.org/annotation/VAR_049723
http://togogenome.org/gene/9606:SLC35B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB61                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Adenosine 3'-phospho 5'-phosphosulfate transporter 1|||Helical|||In HLD26; unknown pathological significance; decreased expression in homozygous patient's skin fibroblasts compared to control cells; partial mislocalization of the protein, with diffuse signal in the cell and only partial localization to the Golgi apparatus; decreased chondroitin sulfate disaccharide sulfation in homozygous patient's skin fibroblasts compared to control cells, suggesting impaired function.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213374|||http://purl.uniprot.org/annotation/VAR_022657|||http://purl.uniprot.org/annotation/VAR_088180|||http://purl.uniprot.org/annotation/VSP_014084|||http://purl.uniprot.org/annotation/VSP_026949|||http://purl.uniprot.org/annotation/VSP_054696|||http://purl.uniprot.org/annotation/VSP_054697|||http://purl.uniprot.org/annotation/VSP_057436
http://togogenome.org/gene/9606:PPL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60437                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Interacts with BFSP2 and VIM|||Periplakin|||Phosphoserine|||Plectin 1|||Plectin 2|||SH3|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000078149|||http://purl.uniprot.org/annotation/VAR_055125|||http://purl.uniprot.org/annotation/VAR_055126|||http://purl.uniprot.org/annotation/VAR_055127|||http://purl.uniprot.org/annotation/VAR_055128|||http://purl.uniprot.org/annotation/VAR_055129|||http://purl.uniprot.org/annotation/VAR_055130|||http://purl.uniprot.org/annotation/VAR_055131|||http://purl.uniprot.org/annotation/VAR_055132|||http://purl.uniprot.org/annotation/VAR_055133|||http://purl.uniprot.org/annotation/VAR_055134
http://togogenome.org/gene/9606:TXNDC12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95881                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Motif|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Loss of protein-disulfide reductase (glutathione) activity. Loss of the formation of disulfide bonds in substrate.|||Prevents secretion from ER|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034189
http://togogenome.org/gene/9606:COX7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24311                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 7B, mitochondrial|||Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006158
http://togogenome.org/gene/9606:TSR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJK0                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region                                                                                  ^@                                                                                  18S rRNA aminocarboxypropyltransferase|||Disordered|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278669
http://togogenome.org/gene/9606:SEC31A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94979                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ALG-2-binding site motif-2 (ABS-2),|||Disordered|||Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-1217.|||Does not abolish monoubiquitination by the BCR(KLHL12) E3 ubiquitin ligase complex, revealing flexibility of ubiquitination sites; when associated with R-647.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2, isoform 7, isoform 9 and isoform 10.|||In isoform 3 and isoform 6.|||In isoform 4, isoform 6, isoform 7 and isoform 10.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||Interaction with PDCD6|||Interaction with SEC13|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Protein transport protein Sec31A|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8; interaction with SEC13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295147|||http://purl.uniprot.org/annotation/VAR_033225|||http://purl.uniprot.org/annotation/VAR_033226|||http://purl.uniprot.org/annotation/VAR_033227|||http://purl.uniprot.org/annotation/VAR_053414|||http://purl.uniprot.org/annotation/VSP_026742|||http://purl.uniprot.org/annotation/VSP_026743|||http://purl.uniprot.org/annotation/VSP_026744|||http://purl.uniprot.org/annotation/VSP_026745|||http://purl.uniprot.org/annotation/VSP_026746|||http://purl.uniprot.org/annotation/VSP_026747|||http://purl.uniprot.org/annotation/VSP_026748|||http://purl.uniprot.org/annotation/VSP_026749|||http://purl.uniprot.org/annotation/VSP_026750|||http://purl.uniprot.org/annotation/VSP_026751|||http://purl.uniprot.org/annotation/VSP_044602
http://togogenome.org/gene/9606:FAM124A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V42                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Protein FAM124A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286380|||http://purl.uniprot.org/annotation/VAR_032098|||http://purl.uniprot.org/annotation/VSP_025039|||http://purl.uniprot.org/annotation/VSP_025040|||http://purl.uniprot.org/annotation/VSP_025041
http://togogenome.org/gene/9606:CD24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25063                                                                                  ^@                                                                                  Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Glycosylation Site|||Lipid Binding|||Peptide|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated glycine|||In isoform 2.|||May be associated with an increased risk for multiple sclerosis; homozygous patients express higher levels of CD24 on peripheral blood T-cells than homozygous controls.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Signal transducer CD24                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020893|||http://purl.uniprot.org/annotation/PRO_0000020894|||http://purl.uniprot.org/annotation/VAR_016156|||http://purl.uniprot.org/annotation/VAR_031576|||http://purl.uniprot.org/annotation/VSP_059359
http://togogenome.org/gene/9606:SOWAHA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M3V2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein SOWAHA|||Disordered|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244373|||http://purl.uniprot.org/annotation/VAR_059125|||http://purl.uniprot.org/annotation/VAR_060465
http://togogenome.org/gene/9606:STK17B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94768|||http://purl.uniprot.org/uniprot/Q53QE7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of activity and of apoptotic function.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 17B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086706|||http://purl.uniprot.org/annotation/VAR_041147
http://togogenome.org/gene/9606:CCDC181                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R917|||http://purl.uniprot.org/uniprot/Q5TID7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil|||Coiled-coil domain-containing protein 181|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279465|||http://purl.uniprot.org/annotation/VAR_030907|||http://purl.uniprot.org/annotation/VAR_056764|||http://purl.uniprot.org/annotation/VAR_056765|||http://purl.uniprot.org/annotation/VSP_023448|||http://purl.uniprot.org/annotation/VSP_023449
http://togogenome.org/gene/9606:ZBTB22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8V3|||http://purl.uniprot.org/uniprot/O15209                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||Disordered|||Phosphoserine|||Polar residues|||Zinc finger and BTB domain-containing protein 22                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047517|||http://purl.uniprot.org/annotation/VAR_022702|||http://purl.uniprot.org/annotation/VAR_057457
http://togogenome.org/gene/9606:GHRH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01286                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Leucine amide|||Somatoliberin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011438|||http://purl.uniprot.org/annotation/PRO_0000011439|||http://purl.uniprot.org/annotation/PRO_0000011440|||http://purl.uniprot.org/annotation/VAR_024328|||http://purl.uniprot.org/annotation/VAR_049185|||http://purl.uniprot.org/annotation/VSP_023146
http://togogenome.org/gene/9606:QSER1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KWV1|||http://purl.uniprot.org/uniprot/Q2KHR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DUF4211|||Disordered|||Glutamine and serine-rich protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288933|||http://purl.uniprot.org/annotation/VAR_032535|||http://purl.uniprot.org/annotation/VAR_032536|||http://purl.uniprot.org/annotation/VAR_032537|||http://purl.uniprot.org/annotation/VAR_056975|||http://purl.uniprot.org/annotation/VSP_039815|||http://purl.uniprot.org/annotation/VSP_039816
http://togogenome.org/gene/9606:RBM25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49756                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Necessary for nuclear speckle localization|||PWI|||Phosphoserine|||Polar residues|||RNA-binding protein 25|||RRM|||Reduced DNA/RNA binding.|||Reduced DNA/RNA binding; when associated with A-825.|||Reduced DNA/RNA binding; when associated with A-828.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081784|||http://purl.uniprot.org/annotation/VSP_036791|||http://purl.uniprot.org/annotation/VSP_036792|||http://purl.uniprot.org/annotation/VSP_036793|||http://purl.uniprot.org/annotation/VSP_036794|||http://purl.uniprot.org/annotation/VSP_039881|||http://purl.uniprot.org/annotation/VSP_039882
http://togogenome.org/gene/9606:NIPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8Q9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a patient with childhood absence epilepsy; loss of cell membrane localization; no significant effect on magnesium transport; unknown pathological significance.|||Found in a patient with childhood absence epilepsy; loss of cell membrane localization; significant decrease in magnesium transport; unknown pathological significance.|||Helical|||In isoform 2.|||Magnesium transporter NIPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191743|||http://purl.uniprot.org/annotation/VAR_088398|||http://purl.uniprot.org/annotation/VAR_088399|||http://purl.uniprot.org/annotation/VAR_088400|||http://purl.uniprot.org/annotation/VSP_044587
http://togogenome.org/gene/9606:MBTPS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43462                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In IFAP1; does not affect subcellular localization; impairs activity.|||In KFSDX; sterol responsiveness is reduced by half.|||In OI19; decreased regulated intramembrane proteolysis resulting in reduced transcriptional activation of genes relevant to osteoblast differentiation and bone formation.|||In OLMSX.|||Loss of activity.|||Lumenal|||Membrane-bound transcription factor site-2 protease|||N-linked (GlcNAc...) asparagine|||Partial loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088482|||http://purl.uniprot.org/annotation/VAR_063054|||http://purl.uniprot.org/annotation/VAR_063055|||http://purl.uniprot.org/annotation/VAR_063056|||http://purl.uniprot.org/annotation/VAR_063057|||http://purl.uniprot.org/annotation/VAR_063058|||http://purl.uniprot.org/annotation/VAR_064409|||http://purl.uniprot.org/annotation/VAR_071323|||http://purl.uniprot.org/annotation/VAR_081103|||http://purl.uniprot.org/annotation/VAR_081104
http://togogenome.org/gene/9606:ZCCHC18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG32                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CCHC-type|||Disordered|||Polar residues|||Zinc finger CCHC domain-containing protein 18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395361
http://togogenome.org/gene/9606:BPIFA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP55                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BPI fold-containing family A member 1|||Forms an artificial disulfide bond. Negligible effect on surfactant activity; when associated with C-253.|||Forms an artificial disulfide bond. Negligible effect on surfactant activity; when associated with C-48.|||Forms an artificial disulfide bond. Reduced surfactant activity; when associated with C-214.|||Forms an artificial disulfide bond. Reduced surfactant activity; when associated with C-76.|||Impaired surfactant activity and lipopolysaccharide (LPS) binding. Reduced bacteriostatic activity.|||Important for surfactant activity and antibacterial properties|||In isoform 2.|||No effect on surfactant activity; when associated with 191-A--A-195.|||No effect on surfactant activity; when associated with 203-A-A-204.|||No effect on surfactant activity; when associated with A-180.|||No effect on surfactant activity; when associated with A-224.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017175|||http://purl.uniprot.org/annotation/VSP_057345
http://togogenome.org/gene/9606:MTSS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q765P7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||IMD|||In IDDOF; decreased protein abundance in patient cells; decreased function suggested by rescue assays in mutant fly.|||In isoform 2.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149 and D-152.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-138, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-137, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-130, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-127, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-123, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-116, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-115, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Marked reduction in RAC1-binding, loss of increase in RAC1 activity and of dorsal ruffles formation in response to PDGF treatment; when associated with D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-149, D-152 and D-157.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein MTSS 2|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319610|||http://purl.uniprot.org/annotation/VAR_087784|||http://purl.uniprot.org/annotation/VSP_031513|||http://purl.uniprot.org/annotation/VSP_031514|||http://purl.uniprot.org/annotation/VSP_031515
http://togogenome.org/gene/9606:SPINK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTA9|||http://purl.uniprot.org/uniprot/D6RC51|||http://purl.uniprot.org/uniprot/D6RI10|||http://purl.uniprot.org/uniprot/P20155                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Disordered|||Kazal-like|||Loss of inhibitory activity towards trypsin.|||No effect on inhibitory activity towards trypsin.|||Pyrrolidone carboxylic acid|||Reactive bond|||Reduces inhibitory activity towards trypsin.|||Serine protease inhibitor Kazal-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016561|||http://purl.uniprot.org/annotation/PRO_5001831900|||http://purl.uniprot.org/annotation/PRO_5003087455|||http://purl.uniprot.org/annotation/PRO_5003087590
http://togogenome.org/gene/9606:COX4I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BNV9|||http://purl.uniprot.org/uniprot/P13073                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Cytochrome c oxidase subunit 4 isoform 1, mitochondrial|||Helical|||In MC4DN16.|||In MC4DN16; decreased COX4I1 protein levels.|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006084|||http://purl.uniprot.org/annotation/VAR_002170|||http://purl.uniprot.org/annotation/VAR_061127|||http://purl.uniprot.org/annotation/VAR_084181|||http://purl.uniprot.org/annotation/VAR_084182
http://togogenome.org/gene/9606:ANKRD50                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB46|||http://purl.uniprot.org/uniprot/Q9ULJ7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat domain-containing protein 50|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066920|||http://purl.uniprot.org/annotation/VSP_045459
http://togogenome.org/gene/9606:IPO8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15397                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Importin N-terminal|||Importin-8|||In VISS.|||In VISS; undetectable protein expression levels in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines.|||In VISS; undetectable protein levels in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines.|||In VISS; undetectable protein levels in patient's fibroblasts, although mRNA levels seem unaffected.|||In VISS; unknown pathological significance.|||In VISS; very low protein expression levels, if any, in either patient's fibroblasts or patient's Epstein-Barr virus-immortalized B cell lines.|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120752|||http://purl.uniprot.org/annotation/VAR_055118|||http://purl.uniprot.org/annotation/VAR_055119|||http://purl.uniprot.org/annotation/VAR_086233|||http://purl.uniprot.org/annotation/VAR_086234|||http://purl.uniprot.org/annotation/VAR_086235|||http://purl.uniprot.org/annotation/VAR_086236|||http://purl.uniprot.org/annotation/VAR_086237|||http://purl.uniprot.org/annotation/VAR_086238|||http://purl.uniprot.org/annotation/VAR_086239|||http://purl.uniprot.org/annotation/VAR_086240|||http://purl.uniprot.org/annotation/VAR_086241|||http://purl.uniprot.org/annotation/VAR_086242|||http://purl.uniprot.org/annotation/VAR_086243|||http://purl.uniprot.org/annotation/VSP_042574
http://togogenome.org/gene/9606:RGN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15493|||http://purl.uniprot.org/uniprot/V9HWF8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N6-succinyllysine|||Proton donor/acceptor|||Reduces enzyme activity by about 90%.|||Reduces enzyme activity by about 95%.|||Reduces enzyme activity by over 98%.|||Regucalcin|||SMP-30/Gluconolactonase/LRE-like region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173046|||http://purl.uniprot.org/annotation/VSP_025456|||http://purl.uniprot.org/annotation/VSP_025457
http://togogenome.org/gene/9606:INPP5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92835                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In one patient with acute myeloid leukemya; somatic mutation.|||Interaction with DAB2|||NPXY motif 1|||NPXY motif 2|||Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||SH2|||SH3-binding 1|||SH3-binding 2|||SH3-binding 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302866|||http://purl.uniprot.org/annotation/VAR_034979|||http://purl.uniprot.org/annotation/VAR_059358|||http://purl.uniprot.org/annotation/VSP_027977|||http://purl.uniprot.org/annotation/VSP_027978|||http://purl.uniprot.org/annotation/VSP_027979
http://togogenome.org/gene/9606:L3MBTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y468                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to monomethylated and dimethylated peptides.|||Abolishes binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'.|||Abolishes binding to p53/TP53 monomethylated at 'Lys-382'.|||Basic and acidic residues|||Basic residues|||CCHHC-type|||Disordered|||Does not affect binding to monomethylated and dimethylated peptides.|||In isoform 1, isoform 2 and isoform 4.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Interaction with monomethylated and dimethylated peptides|||Lethal(3)malignant brain tumor-like protein 1|||MBT 1|||MBT 2|||MBT 3|||Mediates recognition of monomethylated and dimethylated peptides|||Phosphoserine|||Polar residues|||Positioned at the entrance of MBT 2 and is required for recognition of monomethylated and dimethylated peptides|||Strongly impairs binding to monomethylated and dimethylated peptides.|||Strongly impairs binding to monomethylated and dimethylated peptides. Abolishes binding to p53/TP53 monomethylated at 'Lys-382'.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084452|||http://purl.uniprot.org/annotation/VAR_051097|||http://purl.uniprot.org/annotation/VAR_051098|||http://purl.uniprot.org/annotation/VAR_082883|||http://purl.uniprot.org/annotation/VSP_003901|||http://purl.uniprot.org/annotation/VSP_059458|||http://purl.uniprot.org/annotation/VSP_059459|||http://purl.uniprot.org/annotation/VSP_059460
http://togogenome.org/gene/9606:FAM13C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K181|||http://purl.uniprot.org/uniprot/B4DSU7|||http://purl.uniprot.org/uniprot/B7Z2K3|||http://purl.uniprot.org/uniprot/Q8NE31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||Phosphoserine|||Polar residues|||Protein FAM13C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058922|||http://purl.uniprot.org/annotation/VAR_047661|||http://purl.uniprot.org/annotation/VSP_035840|||http://purl.uniprot.org/annotation/VSP_035841|||http://purl.uniprot.org/annotation/VSP_035842|||http://purl.uniprot.org/annotation/VSP_044286|||http://purl.uniprot.org/annotation/VSP_045812
http://togogenome.org/gene/9606:CD300LF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DQD2|||http://purl.uniprot.org/uniprot/J3KS52|||http://purl.uniprot.org/uniprot/Q8TDQ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CMRF35-like molecule 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with PTPN6.|||N-linked (GlcNAc...) asparagine|||No interaction with PTPN6.|||Phosphatase-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247825|||http://purl.uniprot.org/annotation/PRO_5002803503|||http://purl.uniprot.org/annotation/PRO_5003771674|||http://purl.uniprot.org/annotation/VAR_027152|||http://purl.uniprot.org/annotation/VAR_039128|||http://purl.uniprot.org/annotation/VSP_020056|||http://purl.uniprot.org/annotation/VSP_020057|||http://purl.uniprot.org/annotation/VSP_020058|||http://purl.uniprot.org/annotation/VSP_020059|||http://purl.uniprot.org/annotation/VSP_020060|||http://purl.uniprot.org/annotation/VSP_020061|||http://purl.uniprot.org/annotation/VSP_020062|||http://purl.uniprot.org/annotation/VSP_020063|||http://purl.uniprot.org/annotation/VSP_020064|||http://purl.uniprot.org/annotation/VSP_020065
http://togogenome.org/gene/9606:TFPI2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48307                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||BPTI/Kunitz inhibitor 3|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Reactive bond|||Tissue factor pathway inhibitor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016876|||http://purl.uniprot.org/annotation/VAR_012005|||http://purl.uniprot.org/annotation/VAR_050064|||http://purl.uniprot.org/annotation/VSP_056031
http://togogenome.org/gene/9606:NTMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VVY1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Increases methylation activity. Higher affinity for mono-methylated peptide than wild-type.|||N-terminal Xaa-Pro-Lys N-methyltransferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271077|||http://purl.uniprot.org/annotation/VAR_029859|||http://purl.uniprot.org/annotation/VAR_060621|||http://purl.uniprot.org/annotation/VAR_060622
http://togogenome.org/gene/9606:DMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3B5|||http://purl.uniprot.org/uniprot/A0A0S2Z3J7|||http://purl.uniprot.org/uniprot/A7E212|||http://purl.uniprot.org/uniprot/P11532|||http://purl.uniprot.org/uniprot/Q16484|||http://purl.uniprot.org/uniprot/Q4G0X0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  ANK2- and ANK-3 binding|||Actin-binding|||Binds to SNTB1|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||Dystrophin|||In BMD.|||In CMD3B.|||In CMD3B; decreased thermodynamic stability; accelerated unfolding, perturbed protein structure; no effect on anchoring function.|||In DMD.|||In DMD; does not affect protein stability; does not affect protein expression at the sarcolemma; interaction with DAG1 is reduced.|||In DMD; results in highly reduced protein levels and expression at the sarcolemma.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a patient with Becker muscular dystrophy.|||In isoform 11.|||In isoform 12, isoform 13, isoform 14, isoform 15, isoform 16 and isoform 17.|||In isoform 17.|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6, isoform 7, isoform 8, isoform 9 and isoform 10.|||In isoform 7, isoform 10 and isoform 16.|||In isoform 8, isoform 9, isoform 10, isoform 14, isoform 15 and isoform 16.|||In isoform 9, isoform 13 and isoform 15.|||In one patient with Becker muscular dystrophy.|||Interaction with SYNM|||Phosphoserine|||Phosphothreonine|||Polar residues|||Spectrin 1|||Spectrin 10|||Spectrin 11|||Spectrin 12|||Spectrin 13|||Spectrin 14|||Spectrin 15|||Spectrin 16|||Spectrin 17|||Spectrin 18|||Spectrin 19|||Spectrin 2|||Spectrin 20|||Spectrin 21|||Spectrin 22|||Spectrin 23|||Spectrin 24|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9|||WW|||ZZ-type|||ZZ-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076075|||http://purl.uniprot.org/annotation/VAR_005146|||http://purl.uniprot.org/annotation/VAR_005147|||http://purl.uniprot.org/annotation/VAR_005148|||http://purl.uniprot.org/annotation/VAR_005149|||http://purl.uniprot.org/annotation/VAR_005150|||http://purl.uniprot.org/annotation/VAR_005151|||http://purl.uniprot.org/annotation/VAR_005152|||http://purl.uniprot.org/annotation/VAR_005153|||http://purl.uniprot.org/annotation/VAR_005154|||http://purl.uniprot.org/annotation/VAR_005155|||http://purl.uniprot.org/annotation/VAR_005156|||http://purl.uniprot.org/annotation/VAR_005157|||http://purl.uniprot.org/annotation/VAR_005158|||http://purl.uniprot.org/annotation/VAR_005159|||http://purl.uniprot.org/annotation/VAR_005160|||http://purl.uniprot.org/annotation/VAR_005161|||http://purl.uniprot.org/annotation/VAR_005162|||http://purl.uniprot.org/annotation/VAR_005163|||http://purl.uniprot.org/annotation/VAR_005164|||http://purl.uniprot.org/annotation/VAR_005165|||http://purl.uniprot.org/annotation/VAR_005166|||http://purl.uniprot.org/annotation/VAR_005167|||http://purl.uniprot.org/annotation/VAR_005168|||http://purl.uniprot.org/annotation/VAR_005169|||http://purl.uniprot.org/annotation/VAR_005170|||http://purl.uniprot.org/annotation/VAR_005171|||http://purl.uniprot.org/annotation/VAR_005172|||http://purl.uniprot.org/annotation/VAR_023537|||http://purl.uniprot.org/annotation/VAR_023538|||http://purl.uniprot.org/annotation/VAR_023539|||http://purl.uniprot.org/annotation/VAR_023540|||http://purl.uniprot.org/annotation/VAR_023541|||http://purl.uniprot.org/annotation/VAR_023542|||http://purl.uniprot.org/annotation/VAR_023543|||http://purl.uniprot.org/annotation/VAR_023544|||http://purl.uniprot.org/annotation/VAR_023545|||http://purl.uniprot.org/annotation/VAR_023546|||http://purl.uniprot.org/annotation/VAR_023547|||http://purl.uniprot.org/annotation/VAR_036353|||http://purl.uniprot.org/annotation/VAR_036354|||http://purl.uniprot.org/annotation/VAR_036355|||http://purl.uniprot.org/annotation/VAR_036356|||http://purl.uniprot.org/annotation/VAR_057642|||http://purl.uniprot.org/annotation/VAR_057643|||http://purl.uniprot.org/annotation/VAR_057644|||http://purl.uniprot.org/annotation/VAR_057645|||http://purl.uniprot.org/annotation/VAR_057646|||http://purl.uniprot.org/annotation/VAR_057647|||http://purl.uniprot.org/annotation/VAR_062110|||http://purl.uniprot.org/annotation/VAR_065764|||http://purl.uniprot.org/annotation/VSP_006806|||http://purl.uniprot.org/annotation/VSP_006807|||http://purl.uniprot.org/annotation/VSP_006808|||http://purl.uniprot.org/annotation/VSP_006809|||http://purl.uniprot.org/annotation/VSP_017490|||http://purl.uniprot.org/annotation/VSP_017491|||http://purl.uniprot.org/annotation/VSP_017492|||http://purl.uniprot.org/annotation/VSP_017493|||http://purl.uniprot.org/annotation/VSP_046319|||http://purl.uniprot.org/annotation/VSP_060274|||http://purl.uniprot.org/annotation/VSP_060275|||http://purl.uniprot.org/annotation/VSP_060276|||http://purl.uniprot.org/annotation/VSP_060277|||http://purl.uniprot.org/annotation/VSP_060278
http://togogenome.org/gene/9606:OR7A10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVC8|||http://purl.uniprot.org/uniprot/O76100                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7A10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150644|||http://purl.uniprot.org/annotation/VAR_034254|||http://purl.uniprot.org/annotation/VAR_053225|||http://purl.uniprot.org/annotation/VAR_053226|||http://purl.uniprot.org/annotation/VAR_053227
http://togogenome.org/gene/9606:LILRB5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75023                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif 1|||ITIM motif 2|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||In isoform 2 and isoform 3.|||In isoform 2.|||Leukocyte immunoglobulin-like receptor subfamily B member 5|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014825|||http://purl.uniprot.org/annotation/VAR_061316|||http://purl.uniprot.org/annotation/VAR_085724|||http://purl.uniprot.org/annotation/VSP_008461|||http://purl.uniprot.org/annotation/VSP_008462
http://togogenome.org/gene/9606:PDCD1LG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQ51                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Programmed cell death 1 ligand 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014555|||http://purl.uniprot.org/annotation/VAR_022449|||http://purl.uniprot.org/annotation/VAR_049842|||http://purl.uniprot.org/annotation/VAR_049843|||http://purl.uniprot.org/annotation/VSP_013738|||http://purl.uniprot.org/annotation/VSP_013739|||http://purl.uniprot.org/annotation/VSP_013740
http://togogenome.org/gene/9606:PDCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0M3M0G7|||http://purl.uniprot.org/uniprot/Q15116                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes ubiquitination by the SCF(FBXO38) complex.|||Cytoplasmic|||Decreased N-glycosylation without affecting binding to binding to nivolumab drug.|||Disordered|||Does not affect ubiquitination by the SCF(FBXO38) complex.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||ITIM motif|||ITSM motif|||Ig-like|||Ig-like V-type|||Interaction with CD274/PDCD1L1|||N-linked (GlcNAc...) asparagine|||Nivolumab binding|||Pembrolizumab binding|||Phosphotyrosine|||Programmed cell death protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014892|||http://purl.uniprot.org/annotation/VAR_031685
http://togogenome.org/gene/9606:MCRIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JLW8|||http://purl.uniprot.org/uniprot/I3L3A7|||http://purl.uniprot.org/uniprot/I3L4Q0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region                                                                                  ^@                                                                                  Disordered|||Mapk-regulated corepressor-interacting protein 1|||N6-acetyllysine|||PXDLS motif|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393954
http://togogenome.org/gene/9606:RNF157                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||D-box 1|||D-box 2|||Disordered|||E3 ubiquitin ligase RNF157|||In isoform 2.|||N-myristoyl glycine|||Phosphoserine|||Polar residues|||RING-type|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261614|||http://purl.uniprot.org/annotation/VAR_029458|||http://purl.uniprot.org/annotation/VAR_029459|||http://purl.uniprot.org/annotation/VAR_061817|||http://purl.uniprot.org/annotation/VSP_021735
http://togogenome.org/gene/9606:AURKA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14965                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes cilia disassembly and kinase activity.|||Activation segment|||Aurora kinase A|||Decreases the interaction with phosphatase type 1 isoforms.|||Disordered|||Enhances interaction with TPX2.|||Enhances stability; when associated with A-290.|||Enhances stability; when associated with A-393.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal adenocarcinoma sample; somatic mutation; reduces interaction with TPX2.|||In a metastatic melanoma sample; somatic mutation; constitutively enhanced kinase activity.|||Increased kinase activity.|||Loss of kinase activity.|||Mimics phosphorylation state and increases kinase activity.|||No direct effect on catalytic activity.|||Phosphoserine|||Phosphoserine; by PKA and PAK|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||Reduces binding to MYCN.|||Reduces cilia disassembly and kinase activity.|||Reduces interaction with TPX2. Reduces kinase activity tenfold. Promotes interaction with the AURKB binding partners INCENP and BIRC5 that are normally not bound by AURKA.|||Reduces ubiquitination and proteasomal degradation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086692|||http://purl.uniprot.org/annotation/VAR_030840|||http://purl.uniprot.org/annotation/VAR_030841|||http://purl.uniprot.org/annotation/VAR_030842|||http://purl.uniprot.org/annotation/VAR_041127|||http://purl.uniprot.org/annotation/VAR_041128|||http://purl.uniprot.org/annotation/VAR_041129|||http://purl.uniprot.org/annotation/VAR_041130|||http://purl.uniprot.org/annotation/VAR_061745
http://togogenome.org/gene/9606:GPX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22352                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Non standard residue|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Glutathione peroxidase 3|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013062|||http://purl.uniprot.org/annotation/VAR_020943
http://togogenome.org/gene/9606:CTSL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07711|||http://purl.uniprot.org/uniprot/Q9HBQ7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Catalytically inactive. Unable to autocleave procathepsin L.|||Cathepsin L|||Cathepsin L heavy chain|||Cathepsin L light chain|||Cleavage; by autolysis|||In isoform 2.|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Peptidase C1A papain C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026244|||http://purl.uniprot.org/annotation/PRO_0000026245|||http://purl.uniprot.org/annotation/PRO_0000026246|||http://purl.uniprot.org/annotation/PRO_0000026247|||http://purl.uniprot.org/annotation/PRO_0000450791|||http://purl.uniprot.org/annotation/VSP_060720
http://togogenome.org/gene/9606:CENPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU64                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Centromere protein O|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249502|||http://purl.uniprot.org/annotation/VAR_027420|||http://purl.uniprot.org/annotation/VSP_020446
http://togogenome.org/gene/9606:SHOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NLG4|||http://purl.uniprot.org/uniprot/O60902                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||In isoform 2.|||In isoform 3.|||OAR|||Short stature homeobox protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049292|||http://purl.uniprot.org/annotation/VSP_002288|||http://purl.uniprot.org/annotation/VSP_024427
http://togogenome.org/gene/9606:ZNF684                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSP5|||http://purl.uniprot.org/uniprot/Q5T5D7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||KRAB|||Zinc finger protein 684                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234003
http://togogenome.org/gene/9606:GXYLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4G148                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glucoside xylosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288534|||http://purl.uniprot.org/annotation/VSP_025709
http://togogenome.org/gene/9606:CTTNBP2NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2B4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CTTNBP2 N-terminal-like protein|||Disordered|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000226997|||http://purl.uniprot.org/annotation/VAR_050925|||http://purl.uniprot.org/annotation/VAR_050926
http://togogenome.org/gene/9606:TRIM67                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1; degenerate|||B box-type 2|||B30.2/SPRY|||COS|||Disordered|||Fibronectin type-III|||In isoform 2.|||Pro residues|||RING-type; degenerate|||Tripartite motif-containing protein 67                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256864|||http://purl.uniprot.org/annotation/VSP_021359|||http://purl.uniprot.org/annotation/VSP_021360
http://togogenome.org/gene/9606:CPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31327                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ATP-grasp 1|||ATP-grasp 2|||Anthranilate phosphoribosyltransferase homolog|||Associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability.|||Associated with susceptibility to neonatal pulmonary hypertension; also highly associated with hepatocellular carcinoma progression.|||Carbamoyl-phosphate synthase [ammonia], mitochondrial|||Found in a patient with VACTERL syndrome and postsurgical PHN; unknown pathological significance.|||Glutamine amidotransferase type-1|||In CPS1D.|||In CPS1D; almost complete loss of enzyme activity.|||In CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG.|||In CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia.|||In CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability.|||In CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia.|||In CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield.|||In CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity.|||In CPS1D; associated with T-986.|||In CPS1D; associated with V-304.|||In CPS1D; may affect splicing.|||In CPS1D; moderate decrease in protein yield and partial loss of enzyme activity.|||In CPS1D; modestly decreases enzyme activity.|||In CPS1D; partial loss of enzyme activity and significant decrease in thermal stability.|||In CPS1D; partial loss of enzyme activity.|||In CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding.|||In CPS1D; significant decrease in protein yield and enzyme activity.|||In CPS1D; significant decrease in protein yield and partial loss of enzyme activity.|||In CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity.|||In CPS1D; significant loss of protein stability.|||In CPS1D; significant reduction in thermal stability.|||In CPS1D; the enzyme is inactive.|||In CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG).|||In CPS1D; unknown pathological significance.|||In CPS1D; unknown pathological significance; associated with N-937 in a patient.|||In isoform 2.|||In isoform 3.|||MGS-like|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-glutaryllysine|||N6-glutaryllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||No functional consequences; no negative effect on protein stability, enzyme activity and thermal stability.|||No negative effect on protein stability, enzyme activity and thermal stability.|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) serine; alternate|||O-linked (GlcNAc) threonine|||Phosphoserine|||Phosphoserine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029897|||http://purl.uniprot.org/annotation/VAR_006834|||http://purl.uniprot.org/annotation/VAR_006835|||http://purl.uniprot.org/annotation/VAR_014077|||http://purl.uniprot.org/annotation/VAR_017562|||http://purl.uniprot.org/annotation/VAR_017563|||http://purl.uniprot.org/annotation/VAR_017564|||http://purl.uniprot.org/annotation/VAR_017565|||http://purl.uniprot.org/annotation/VAR_017566|||http://purl.uniprot.org/annotation/VAR_017567|||http://purl.uniprot.org/annotation/VAR_017568|||http://purl.uniprot.org/annotation/VAR_017569|||http://purl.uniprot.org/annotation/VAR_030675|||http://purl.uniprot.org/annotation/VAR_030676|||http://purl.uniprot.org/annotation/VAR_061752|||http://purl.uniprot.org/annotation/VAR_063560|||http://purl.uniprot.org/annotation/VAR_063561|||http://purl.uniprot.org/annotation/VAR_063562|||http://purl.uniprot.org/annotation/VAR_063563|||http://purl.uniprot.org/annotation/VAR_063564|||http://purl.uniprot.org/annotation/VAR_063565|||http://purl.uniprot.org/annotation/VAR_063566|||http://purl.uniprot.org/annotation/VAR_063567|||http://purl.uniprot.org/annotation/VAR_063568|||http://purl.uniprot.org/annotation/VAR_063569|||http://purl.uniprot.org/annotation/VAR_063570|||http://purl.uniprot.org/annotation/VAR_063571|||http://purl.uniprot.org/annotation/VAR_063572|||http://purl.uniprot.org/annotation/VAR_063573|||http://purl.uniprot.org/annotation/VAR_063574|||http://purl.uniprot.org/annotation/VAR_063575|||http://purl.uniprot.org/annotation/VAR_064062|||http://purl.uniprot.org/annotation/VAR_064063|||http://purl.uniprot.org/annotation/VAR_064064|||http://purl.uniprot.org/annotation/VAR_064065|||http://purl.uniprot.org/annotation/VAR_064066|||http://purl.uniprot.org/annotation/VAR_064067|||http://purl.uniprot.org/annotation/VAR_064068|||http://purl.uniprot.org/annotation/VAR_064069|||http://purl.uniprot.org/annotation/VAR_066104|||http://purl.uniprot.org/annotation/VAR_066105|||http://purl.uniprot.org/annotation/VAR_066106|||http://purl.uniprot.org/annotation/VAR_066107|||http://purl.uniprot.org/annotation/VAR_066108|||http://purl.uniprot.org/annotation/VAR_066109|||http://purl.uniprot.org/annotation/VAR_066110|||http://purl.uniprot.org/annotation/VAR_066111|||http://purl.uniprot.org/annotation/VAR_066112|||http://purl.uniprot.org/annotation/VAR_066113|||http://purl.uniprot.org/annotation/VAR_066114|||http://purl.uniprot.org/annotation/VAR_066115|||http://purl.uniprot.org/annotation/VAR_066116|||http://purl.uniprot.org/annotation/VAR_066117|||http://purl.uniprot.org/annotation/VAR_066118|||http://purl.uniprot.org/annotation/VAR_066119|||http://purl.uniprot.org/annotation/VAR_066120|||http://purl.uniprot.org/annotation/VAR_066121|||http://purl.uniprot.org/annotation/VAR_066122|||http://purl.uniprot.org/annotation/VAR_066123|||http://purl.uniprot.org/annotation/VAR_066124|||http://purl.uniprot.org/annotation/VAR_066125|||http://purl.uniprot.org/annotation/VAR_066126|||http://purl.uniprot.org/annotation/VAR_066127|||http://purl.uniprot.org/annotation/VAR_066128|||http://purl.uniprot.org/annotation/VAR_066129|||http://purl.uniprot.org/annotation/VAR_066130|||http://purl.uniprot.org/annotation/VAR_066131|||http://purl.uniprot.org/annotation/VAR_066132|||http://purl.uniprot.org/annotation/VAR_066133|||http://purl.uniprot.org/annotation/VAR_066134|||http://purl.uniprot.org/annotation/VAR_066135|||http://purl.uniprot.org/annotation/VAR_066136|||http://purl.uniprot.org/annotation/VAR_066137|||http://purl.uniprot.org/annotation/VAR_066138|||http://purl.uniprot.org/annotation/VAR_066139|||http://purl.uniprot.org/annotation/VAR_066140|||http://purl.uniprot.org/annotation/VAR_066141|||http://purl.uniprot.org/annotation/VAR_066142|||http://purl.uniprot.org/annotation/VAR_066143|||http://purl.uniprot.org/annotation/VAR_066144|||http://purl.uniprot.org/annotation/VAR_066145|||http://purl.uniprot.org/annotation/VAR_066146|||http://purl.uniprot.org/annotation/VAR_066147|||http://purl.uniprot.org/annotation/VAR_066148|||http://purl.uniprot.org/annotation/VAR_066149|||http://purl.uniprot.org/annotation/VAR_066150|||http://purl.uniprot.org/annotation/VAR_066151|||http://purl.uniprot.org/annotation/VAR_066152|||http://purl.uniprot.org/annotation/VAR_066153|||http://purl.uniprot.org/annotation/VAR_066154|||http://purl.uniprot.org/annotation/VAR_066155|||http://purl.uniprot.org/annotation/VAR_066156|||http://purl.uniprot.org/annotation/VAR_066157|||http://purl.uniprot.org/annotation/VAR_066158|||http://purl.uniprot.org/annotation/VAR_066159|||http://purl.uniprot.org/annotation/VAR_066160|||http://purl.uniprot.org/annotation/VAR_066161|||http://purl.uniprot.org/annotation/VAR_066162|||http://purl.uniprot.org/annotation/VAR_066163|||http://purl.uniprot.org/annotation/VAR_066164|||http://purl.uniprot.org/annotation/VAR_066165|||http://purl.uniprot.org/annotation/VAR_066166|||http://purl.uniprot.org/annotation/VAR_066167|||http://purl.uniprot.org/annotation/VAR_066168|||http://purl.uniprot.org/annotation/VAR_066169|||http://purl.uniprot.org/annotation/VAR_066170|||http://purl.uniprot.org/annotation/VAR_066171|||http://purl.uniprot.org/annotation/VAR_066172|||http://purl.uniprot.org/annotation/VAR_066173|||http://purl.uniprot.org/annotation/VAR_066174|||http://purl.uniprot.org/annotation/VAR_066175|||http://purl.uniprot.org/annotation/VAR_066176|||http://purl.uniprot.org/annotation/VAR_066177|||http://purl.uniprot.org/annotation/VAR_066178|||http://purl.uniprot.org/annotation/VAR_066179|||http://purl.uniprot.org/annotation/VAR_066180|||http://purl.uniprot.org/annotation/VAR_066181|||http://purl.uniprot.org/annotation/VAR_066182|||http://purl.uniprot.org/annotation/VAR_066183|||http://purl.uniprot.org/annotation/VAR_066184|||http://purl.uniprot.org/annotation/VAR_066185|||http://purl.uniprot.org/annotation/VAR_066186|||http://purl.uniprot.org/annotation/VAR_066187|||http://purl.uniprot.org/annotation/VAR_066188|||http://purl.uniprot.org/annotation/VAR_066189|||http://purl.uniprot.org/annotation/VAR_066190|||http://purl.uniprot.org/annotation/VAR_066191|||http://purl.uniprot.org/annotation/VAR_066192|||http://purl.uniprot.org/annotation/VAR_066193|||http://purl.uniprot.org/annotation/VAR_066194|||http://purl.uniprot.org/annotation/VAR_066195|||http://purl.uniprot.org/annotation/VAR_066196|||http://purl.uniprot.org/annotation/VAR_066197|||http://purl.uniprot.org/annotation/VAR_066198|||http://purl.uniprot.org/annotation/VAR_066199|||http://purl.uniprot.org/annotation/VAR_066200|||http://purl.uniprot.org/annotation/VAR_066201|||http://purl.uniprot.org/annotation/VAR_066202|||http://purl.uniprot.org/annotation/VAR_066203|||http://purl.uniprot.org/annotation/VAR_066204|||http://purl.uniprot.org/annotation/VAR_066205|||http://purl.uniprot.org/annotation/VAR_070211|||http://purl.uniprot.org/annotation/VAR_075404|||http://purl.uniprot.org/annotation/VAR_075405|||http://purl.uniprot.org/annotation/VAR_075406|||http://purl.uniprot.org/annotation/VAR_075407|||http://purl.uniprot.org/annotation/VAR_075408|||http://purl.uniprot.org/annotation/VAR_075409|||http://purl.uniprot.org/annotation/VAR_075410|||http://purl.uniprot.org/annotation/VAR_075411|||http://purl.uniprot.org/annotation/VAR_075412|||http://purl.uniprot.org/annotation/VAR_075413|||http://purl.uniprot.org/annotation/VAR_075806|||http://purl.uniprot.org/annotation/VAR_075807|||http://purl.uniprot.org/annotation/VAR_075808|||http://purl.uniprot.org/annotation/VSP_009332|||http://purl.uniprot.org/annotation/VSP_046685
http://togogenome.org/gene/9606:IFT27                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BW83                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  GDP-locked.|||GTP-locked.|||In BBS19; loss-of-function mutation; results in significantly reduced protein levels.|||In isoform 2.|||Intraflagellar transport protein 27 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082715|||http://purl.uniprot.org/annotation/VAR_071804|||http://purl.uniprot.org/annotation/VSP_021019
http://togogenome.org/gene/9606:DZANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TNE5|||http://purl.uniprot.org/uniprot/A0A8V8TNH6|||http://purl.uniprot.org/uniprot/Q9NVP4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  ANK 1|||ANK 2|||DZANK-type|||DZANK-type 1|||DZANK-type 2|||Disordered|||Double zinc ribbon and ankyrin repeat-containing protein 1|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066986|||http://purl.uniprot.org/annotation/VSP_042090|||http://purl.uniprot.org/annotation/VSP_042091|||http://purl.uniprot.org/annotation/VSP_042092|||http://purl.uniprot.org/annotation/VSP_042093|||http://purl.uniprot.org/annotation/VSP_042094|||http://purl.uniprot.org/annotation/VSP_042095|||http://purl.uniprot.org/annotation/VSP_042096|||http://purl.uniprot.org/annotation/VSP_042097
http://togogenome.org/gene/9606:PCDH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SI70|||http://purl.uniprot.org/uniprot/A0A8V8TM73|||http://purl.uniprot.org/uniprot/O60245                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform B.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Protocadherin-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003992|||http://purl.uniprot.org/annotation/PRO_5035858660|||http://purl.uniprot.org/annotation/PRO_5036482792|||http://purl.uniprot.org/annotation/VSP_000704
http://togogenome.org/gene/9606:GPR75-ASB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y575                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 10|||ANK 11|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Ankyrin repeat and SOCS box protein 3|||In isoform 2.|||In isoform 3.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066926|||http://purl.uniprot.org/annotation/VSP_036392|||http://purl.uniprot.org/annotation/VSP_044606
http://togogenome.org/gene/9606:SLC25A23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV35                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes the ability to regulate mitochondrial calcium uptake; when associated with A-22; A-90 and K-101.|||Abolishes the ability to regulate mitochondrial calcium uptake; when associated with A-22; K-33 and A-90.|||Abolishes the ability to regulate mitochondrial calcium uptake; when associated with A-22; K-33 and K-101.|||Abolishes the ability to regulate mitochondrial calcium uptake; when associated with K-33; A-90 and K-101.|||C-terminal transmembrane transporter domain|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||Linker region|||Mitochondrial adenyl nucleotide antiporter SLC25A23|||Mitochondrial intermembrane|||Mitochondrial matrix|||Regulatory N-terminal domain|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317609|||http://purl.uniprot.org/annotation/VSP_031074|||http://purl.uniprot.org/annotation/VSP_031075|||http://purl.uniprot.org/annotation/VSP_031076
http://togogenome.org/gene/9606:RBMXL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7X1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||RNA-binding motif protein, X-linked-like-3|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261176
http://togogenome.org/gene/9606:NSDHL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NPZ7|||http://purl.uniprot.org/uniprot/Q15738                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  3-beta hydroxysteroid dehydrogenase/isomerase|||Helical|||In CHILD.|||In CKS; temperature-sensitive hypomorphic mutation; able to correctly fold and complement Erg26 mutant yeast at 30 degrees Celsius; Abolishes ability to complement Erg26 mutant yeast at 37 degrees Celsius due to abnormal folding and protein degradation.|||N-acetylmethionine|||Phosphothreonine|||Prevents secretion from ER|||Proton acceptor|||Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087799|||http://purl.uniprot.org/annotation/VAR_010207|||http://purl.uniprot.org/annotation/VAR_010208|||http://purl.uniprot.org/annotation/VAR_065289|||http://purl.uniprot.org/annotation/VAR_065290
http://togogenome.org/gene/9606:C5AR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21730                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  C5a anaphylatoxin chemotactic receptor 1|||Cytoplasmic|||Extracellular|||Fails to homodimerize.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs C5a binding (10-fold reduction) and C5a-induced 5-HT secretion.|||Impairs C5a binding. Strongly impairs C5a binding; when associated with A-27.|||Involved in C5a binding|||Moderately impairs CHIPS binding.|||N-linked (GlcNAc...) asparagine|||No effect on homodimer formation.|||Phosphoserine|||Required for CHIPS binding|||Strongly impairs C5a binding (45,000-fold).|||Strongly impairs C5a binding; when associated with 2-D--L-22 Del.|||Strongly impairs C5a binding; when associated with A-10; A-15; A-16 and A-18.|||Strongly impairs C5a binding; when associated with A-10; A-15; A-16 and A-21 (PubMed:8182049). Impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-10 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-15 (PubMed:15542591).|||Strongly impairs C5a binding; when associated with A-10; A-15; A-18 and A-21.|||Strongly impairs C5a binding; when associated with A-10; A-16; A-18 and A-21 (PubMed:8182049). Moderately impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-10 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-18 (PubMed:15542591).|||Strongly impairs C5a binding; when associated with A-15; A-16; A-18 and A-21 (PubMed:8182049). Moderately impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-15 (PubMed:15542591). Strongly impairs CHIPS binding; when associated with A-18 (PubMed:15542591).|||Sulfotyrosine|||Weakly impairs CHIPS binding (PubMed:15542591). Strongly impairs CHIPS binding (PubMed:21706042). Loss of CHIPS binding; when associated with F-11 (PubMed:21706042).|||Weakly impairs CHIPS binding. Loss of CHIPS binding; when associated with F-14.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069209|||http://purl.uniprot.org/annotation/VAR_049377|||http://purl.uniprot.org/annotation/VAR_049378
http://togogenome.org/gene/9606:CDAN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWY9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Codanin-1|||Disordered|||Helical|||In CDAN1A.|||In CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis.|||In CDAN1A; partially disrupts ASF1 binding.|||In isoform 1.|||Interaction with ASF1A/B|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089439|||http://purl.uniprot.org/annotation/VAR_017218|||http://purl.uniprot.org/annotation/VAR_017219|||http://purl.uniprot.org/annotation/VAR_017220|||http://purl.uniprot.org/annotation/VAR_017221|||http://purl.uniprot.org/annotation/VAR_017222|||http://purl.uniprot.org/annotation/VAR_017223|||http://purl.uniprot.org/annotation/VAR_017224|||http://purl.uniprot.org/annotation/VAR_017225|||http://purl.uniprot.org/annotation/VAR_017226|||http://purl.uniprot.org/annotation/VAR_056785|||http://purl.uniprot.org/annotation/VAR_056786|||http://purl.uniprot.org/annotation/VAR_059602|||http://purl.uniprot.org/annotation/VSP_027097|||http://purl.uniprot.org/annotation/VSP_027098
http://togogenome.org/gene/9606:RAMP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PC20|||http://purl.uniprot.org/uniprot/O60894                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Receptor activity-modifying protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030168
http://togogenome.org/gene/9606:ZNF770                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IQ21                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 770                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280436
http://togogenome.org/gene/9606:DCUN1D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DCN1-like protein 3|||DCUN1|||Disordered|||Does not affect myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-4. Reduces cell membrane localization.|||Does not affect myristoylation; when associated with A-8. Loss of myristoylation; when associated with A-2. Loss of palmitoylation; when associated with A-8. Reduces cell membrane localization.|||In a cancer; unknown pathological significance.|||Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with N-241 and N-271. Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and RBX1; when associated with A-241 and A-271. Does not affect both nucleus and cytoplasm localization; when associated with A-241 and A-271. Loss of interaction with CUL3; when associated with A-241 and A-271.|||Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with N-241 and R-265.|||Loss of CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation, but no effect on localization at the cell membrane; when associated with R-265 and N-271.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5 CALD1 and RBX1; when associated with A-241 and R-265. Does not affect both nucleus and cytoplasm localization; when associated with A-241 and R-265. Loss of interaction with CUL3; when associated with A-241 and A-271.|||Loss of interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and RBX1; when associated with R-265 and A-271. Does not affect both nucleus and cytoplasm localization; when associated with R-265 and A-271. Loss of interaction with CUL3; when associated with R-265 and A-271.|||N-myristoyl glycine|||No effect on CAND1-, CUL1-, CUL3- and RBX1-binding.|||No effect on CAND1-, CUL1-, CUL3- and RBX1-binding. Loss of localization at the cell membrane. Loss of function of inhibition of DCUN1D1-mediated CUL1 neddylation. Loss of myristoylation. Loss of myristoylation; when associated with A-4. Loss of myristoylation; when associated with A-8. Loss of palmitoylation. Affects cell membrane localization, and localizes throughout the cytoplasm. Does not relocalizes CUL3 to the cell membrane.|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320048|||http://purl.uniprot.org/annotation/VAR_072689|||http://purl.uniprot.org/annotation/VAR_072690
http://togogenome.org/gene/9606:FGF10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JW18|||http://purl.uniprot.org/uniprot/O15520                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Fibroblast growth factor|||Fibroblast growth factor 10|||In LADD3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008981|||http://purl.uniprot.org/annotation/PRO_5031608867|||http://purl.uniprot.org/annotation/VAR_029888|||http://purl.uniprot.org/annotation/VAR_029889
http://togogenome.org/gene/9606:CEP85L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3ZCQ5|||http://purl.uniprot.org/uniprot/Q5SZL2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form the CEP85L-PDGFRB fusion protein|||Centrosomal protein of 85 kDa-like|||Disordered|||In LIS10.|||In LIS10; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3 and isoform 5.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297676|||http://purl.uniprot.org/annotation/VAR_034670|||http://purl.uniprot.org/annotation/VAR_034671|||http://purl.uniprot.org/annotation/VAR_034672|||http://purl.uniprot.org/annotation/VAR_036247|||http://purl.uniprot.org/annotation/VAR_053941|||http://purl.uniprot.org/annotation/VAR_053942|||http://purl.uniprot.org/annotation/VAR_084269|||http://purl.uniprot.org/annotation/VAR_084270|||http://purl.uniprot.org/annotation/VAR_084271|||http://purl.uniprot.org/annotation/VAR_084272|||http://purl.uniprot.org/annotation/VSP_027337|||http://purl.uniprot.org/annotation/VSP_027338|||http://purl.uniprot.org/annotation/VSP_027339|||http://purl.uniprot.org/annotation/VSP_027340
http://togogenome.org/gene/9606:MTAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384ME80|||http://purl.uniprot.org/uniprot/Q13126                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for substrate specificity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N6-acetyllysine|||Nucleoside phosphorylase|||S-methyl-5'-thioadenosine phosphorylase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184545|||http://purl.uniprot.org/annotation/VAR_031470|||http://purl.uniprot.org/annotation/VSP_044071|||http://purl.uniprot.org/annotation/VSP_044072|||http://purl.uniprot.org/annotation/VSP_044073|||http://purl.uniprot.org/annotation/VSP_044074|||http://purl.uniprot.org/annotation/VSP_044075|||http://purl.uniprot.org/annotation/VSP_044076
http://togogenome.org/gene/9606:ROMO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60602                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Reactive oxygen species modulator 1|||Removed|||Sufficient for antibacterial activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079433|||http://purl.uniprot.org/annotation/VAR_014127|||http://purl.uniprot.org/annotation/VSP_036486
http://togogenome.org/gene/9606:TSEN15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2U3TZM3|||http://purl.uniprot.org/uniprot/B1ALV0|||http://purl.uniprot.org/uniprot/E9PPN1|||http://purl.uniprot.org/uniprot/Q8WW01                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In PCH2F; Almost complete loss of tRNA-intron endonuclease activity in vitro.|||In PCH2F; Almost complete loss of tRNA-intron endonuclease activity in vitro; may affect protein levels.|||In isoform 2.|||Phosphoserine|||tRNA-splicing endonuclease subunit Sen15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194023|||http://purl.uniprot.org/annotation/VAR_019457|||http://purl.uniprot.org/annotation/VAR_019458|||http://purl.uniprot.org/annotation/VAR_077061|||http://purl.uniprot.org/annotation/VAR_077062|||http://purl.uniprot.org/annotation/VAR_077063|||http://purl.uniprot.org/annotation/VSP_042723
http://togogenome.org/gene/9606:FBXL8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CD0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict                                                                                  ^@                                                                                  F-box|||F-box/LRR-repeat protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119850
http://togogenome.org/gene/9606:RAP2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10114                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-linked (Glc) threonine; by C.difficile toxin TcdA, and by P.sordellii toxin TcsL|||Cysteine methyl ester|||Decreases affinity for GTP and 3-fold reduction of GTPase activity.|||Dominant active. 2-fold decrease in GDP dissociation rate constant and GTPase activity. No change in interaction with TNIK.|||Dominant negative. Severely impairs GTP-binding and partial loss of interaction with MAP4K4, MINK1 and TNIK.|||Effector region|||Imperfect binding of guanyl nucleotides.|||Loss of RASGEF1A- and RASGEF1B-mediated GDP to GTP exchange. Complete loss of interaction with MAP4K4, MINK1 and TNIK, and loss of ubiquitination by NEDD4.|||Ras-related protein Rap-2a|||Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-148 and R-150.|||Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-148.|||Reduced NEDD4-dependent ubiquitination; when associated with R-5; R-94 and R-150.|||Reduced NEDD4-dependent ubiquitination; when associated with R-94; R-148 and R-150.|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082687|||http://purl.uniprot.org/annotation/PRO_0000281336
http://togogenome.org/gene/9606:ACTR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZN1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Actin-related protein 6|||In isoform 2.|||N-acetylthreonine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089105|||http://purl.uniprot.org/annotation/VSP_054637|||http://purl.uniprot.org/annotation/VSP_054638
http://togogenome.org/gene/9606:TDRP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YL5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Testis development-related protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308219|||http://purl.uniprot.org/annotation/VSP_045212
http://togogenome.org/gene/9606:THBS4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z832|||http://purl.uniprot.org/uniprot/E7ES19|||http://purl.uniprot.org/uniprot/P35443                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Associated with a pro-atherogenic phenotype.|||Basic and acidic residues|||Cell attachment site|||Disordered|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EGF-like 4|||Interchain|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP C-terminal|||TSP type-3|||TSP type-3 1|||TSP type-3 2|||TSP type-3 3|||TSP type-3 4|||TSP type-3 5|||TSP type-3 6|||TSP type-3 7|||TSP type-3 8|||Thrombospondin-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035852|||http://purl.uniprot.org/annotation/VAR_019951|||http://purl.uniprot.org/annotation/VAR_019952|||http://purl.uniprot.org/annotation/VAR_019953|||http://purl.uniprot.org/annotation/VAR_019954|||http://purl.uniprot.org/annotation/VAR_052659
http://togogenome.org/gene/9606:ERLEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DZ1|||http://purl.uniprot.org/uniprot/V9HWD3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Abolishes binding to KREMEN2.|||Abolishes interaction with SEL1L.|||Endoplasmic reticulum lectin|||Endoplasmic reticulum lectin 1|||In isoform 2.|||In isoform 3.|||MRH|||MRH 1|||MRH 2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042182|||http://purl.uniprot.org/annotation/PRO_5004777097|||http://purl.uniprot.org/annotation/VAR_051493|||http://purl.uniprot.org/annotation/VSP_015790|||http://purl.uniprot.org/annotation/VSP_047155
http://togogenome.org/gene/9606:PHGDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43175                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  D-3-phosphoglycerate dehydrogenase|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In NLS1.|||In PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity.|||In PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate.|||In PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076012|||http://purl.uniprot.org/annotation/VAR_013461|||http://purl.uniprot.org/annotation/VAR_059026|||http://purl.uniprot.org/annotation/VAR_059027|||http://purl.uniprot.org/annotation/VAR_059028|||http://purl.uniprot.org/annotation/VAR_059029|||http://purl.uniprot.org/annotation/VAR_059030|||http://purl.uniprot.org/annotation/VAR_071819|||http://purl.uniprot.org/annotation/VAR_071820
http://togogenome.org/gene/9606:MARCHF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NNE9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Motif|||Region|||Splice Variant|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||E3 ubiquitin-protein ligase MARCHF11|||Helical|||In isoform 2.|||PDZ-binding|||Polar residues|||Pro residues|||RING-CH-type|||YXXL motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339344|||http://purl.uniprot.org/annotation/VSP_034147
http://togogenome.org/gene/9606:GOLGA7B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2TAP0|||http://purl.uniprot.org/uniprot/Q6ZUQ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Golgin subfamily A member 7B|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244090
http://togogenome.org/gene/9606:KCNQ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43525                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  >50% Reduction of wt heteromeric current; ratio of 1:1 and 1:1:2.|||Abolishes currents without reducing channel protein expression.|||Cytoplasmic|||Disordered|||Extracellular|||Found in patients with benign familial infantile seizures; unknown pathological significance.|||Has no statistically significant effect on the current or biophysical properties of the heteromeric channel.|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In BFNS2.|||In BFNS2; about 50% reduction of wild-type heteromeric current; ratio of 1:1; or 20%; ratio of 1:1:2.|||In BFNS2; reduces the maximal heteromeric current by 40% with no alteration in voltage dependence of activation or deactivation kinetics.|||In BFNS2; unknown pathological significance.|||In isoform 2.|||Mediates interaction with calmodulin|||No effect on current or expression.|||Phosphothreonine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily KQT member 3|||Rare variant; found in a patient with rolandic epilepsy and additional features such as mild developmental delay and abnormal behavior; unknown pathological significance.|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054034|||http://purl.uniprot.org/annotation/VAR_001546|||http://purl.uniprot.org/annotation/VAR_010935|||http://purl.uniprot.org/annotation/VAR_026994|||http://purl.uniprot.org/annotation/VAR_026995|||http://purl.uniprot.org/annotation/VAR_053859|||http://purl.uniprot.org/annotation/VAR_072741|||http://purl.uniprot.org/annotation/VAR_078681|||http://purl.uniprot.org/annotation/VAR_078682|||http://purl.uniprot.org/annotation/VSP_044906|||http://purl.uniprot.org/annotation/VSP_044907
http://togogenome.org/gene/9606:MAGI3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TCQ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Guanylate kinase-like|||In isoform 3 and isoform 2.|||In isoform 4 and isoform 2.|||Interaction with ADGRB1|||Interaction with ADRB1 and TGFA|||Interaction with LPAR2 and GRIN2B|||Interaction with PTEN|||Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3|||PDZ 1|||PDZ 2|||PDZ 3|||PDZ 4|||PDZ 5|||PDZ 6|||Phosphoserine|||Polar residues|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341407|||http://purl.uniprot.org/annotation/VSP_059502|||http://purl.uniprot.org/annotation/VSP_059503|||http://purl.uniprot.org/annotation/VSP_059504
http://togogenome.org/gene/9606:FAM8A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBU6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Decreased interaction with HERPUD1; no effect on interaction with SYVN1.|||Decreased interaction with SYVN1 and HERPUD1.|||Disordered|||Helical|||Necessary and sufficient to interact with SYVN1|||Phosphoserine|||Pro residues|||Protein FAM8A1|||RDD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087167
http://togogenome.org/gene/9606:SINHCAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NP50                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||SIN3-HDAC complex-associated factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187086|||http://purl.uniprot.org/annotation/VAR_049027|||http://purl.uniprot.org/annotation/VSP_014705
http://togogenome.org/gene/9606:PHF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KP41|||http://purl.uniprot.org/uniprot/D6R9X2|||http://purl.uniprot.org/uniprot/Q92576                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||PHD finger protein 3|||PHD-type|||Phosphoserine|||Polar residues|||TFIIS central                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059292|||http://purl.uniprot.org/annotation/VAR_022040|||http://purl.uniprot.org/annotation/VAR_051599|||http://purl.uniprot.org/annotation/VSP_026434
http://togogenome.org/gene/9606:CTNNBIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSA3                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue                                                                                  ^@                                                                                  Beta-catenin-interacting protein 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152882
http://togogenome.org/gene/9606:HTT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42858                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ZDHHC17.|||Basic and acidic residues|||Cleavage; by caspase-3|||Cleavage; by caspase-6|||Disordered|||Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||Huntingtin|||Huntingtin, myristoylated N-terminal fragment|||In LOMARS.|||Inhibits interaction with ZDHHC13 and ZDHHC17.|||Inhibits proteolytic cleavage at D-550; abolishes post-translational myristoylation; results in increased cleavage at D-511.|||Interaction with ZDHHC17|||Loss of myristoylation.|||Loss of proteolytic cleavage.|||Loss of proteolytic cleavage. Loss of myristoylation.|||N-myristoyl glycine|||N6-acetyllysine|||No effect on proteolytic cleavage.|||Nuclear export signal|||Phosphoserine|||Phosphoserine; by CDK5|||Polar residues|||Pro residues|||Sufficient for interaction with TPR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083942|||http://purl.uniprot.org/annotation/PRO_0000447477|||http://purl.uniprot.org/annotation/VAR_005268|||http://purl.uniprot.org/annotation/VAR_054017|||http://purl.uniprot.org/annotation/VAR_060170|||http://purl.uniprot.org/annotation/VAR_060171|||http://purl.uniprot.org/annotation/VAR_060172|||http://purl.uniprot.org/annotation/VAR_060173|||http://purl.uniprot.org/annotation/VAR_060174|||http://purl.uniprot.org/annotation/VAR_060175|||http://purl.uniprot.org/annotation/VAR_060176|||http://purl.uniprot.org/annotation/VAR_060177|||http://purl.uniprot.org/annotation/VAR_060178|||http://purl.uniprot.org/annotation/VAR_060179|||http://purl.uniprot.org/annotation/VAR_079026|||http://purl.uniprot.org/annotation/VAR_079027|||http://purl.uniprot.org/annotation/VAR_081737
http://togogenome.org/gene/9606:DSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02487                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cytoplasmic|||Desmocollin-2|||Extracellular|||Helical|||In ARVD11.|||In ARVD11; can be processed into a mature form but shows a higher pro-protein to mature protein ratio; only a proportion of the partly functional mutant is incorporated into the desmosomes.|||In ARVD11; fails to undergo complete processing into a mature form; fails to localize at the desmosomes.|||In ARVD11; unknown pathological significance.|||In isoform 2B.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003869|||http://purl.uniprot.org/annotation/PRO_0000003870|||http://purl.uniprot.org/annotation/VAR_024388|||http://purl.uniprot.org/annotation/VAR_029480|||http://purl.uniprot.org/annotation/VAR_062391|||http://purl.uniprot.org/annotation/VAR_062392|||http://purl.uniprot.org/annotation/VAR_065687|||http://purl.uniprot.org/annotation/VAR_065688|||http://purl.uniprot.org/annotation/VAR_065689|||http://purl.uniprot.org/annotation/VAR_065690|||http://purl.uniprot.org/annotation/VAR_065691|||http://purl.uniprot.org/annotation/VAR_065692|||http://purl.uniprot.org/annotation/VAR_078340|||http://purl.uniprot.org/annotation/VAR_087290|||http://purl.uniprot.org/annotation/VSP_000657|||http://purl.uniprot.org/annotation/VSP_000658
http://togogenome.org/gene/9606:ZNF564                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBZ8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 564                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047654
http://togogenome.org/gene/9606:OR5L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVL0|||http://purl.uniprot.org/uniprot/Q8NGL2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5L1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150602|||http://purl.uniprot.org/annotation/VAR_034227|||http://purl.uniprot.org/annotation/VAR_034228|||http://purl.uniprot.org/annotation/VAR_062044
http://togogenome.org/gene/9606:YBEY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58557                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Splice Variant                                                                                  ^@                                                                                  Endoribonuclease YbeY|||In isoform B.|||In isoform C.|||In isoform D.|||No endonuclease activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102578|||http://purl.uniprot.org/annotation/VSP_006721|||http://purl.uniprot.org/annotation/VSP_006722|||http://purl.uniprot.org/annotation/VSP_006723
http://togogenome.org/gene/9606:ZNF691                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VV50|||http://purl.uniprot.org/uniprot/Q5VV52                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine|||Zinc finger protein 691                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234012|||http://purl.uniprot.org/annotation/VSP_018183
http://togogenome.org/gene/9606:UBE2E2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LR5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||N-acetylserine|||Phosphoserine|||Polar residues|||Removed|||UBC core|||Ubiquitin-conjugating enzyme E2 E2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082472
http://togogenome.org/gene/9606:HAUS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94927                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HAUS augmin-like complex subunit 5|||In isoform 2.|||N-acetylmethionine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050776|||http://purl.uniprot.org/annotation/VAR_034038|||http://purl.uniprot.org/annotation/VAR_034039|||http://purl.uniprot.org/annotation/VSP_013927|||http://purl.uniprot.org/annotation/VSP_013928
http://togogenome.org/gene/9606:ZSCAN5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJL1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Polar residues|||SCAN box|||Zinc finger and SCAN domain-containing protein 5B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332169|||http://purl.uniprot.org/annotation/VAR_042965|||http://purl.uniprot.org/annotation/VAR_042966|||http://purl.uniprot.org/annotation/VAR_042967|||http://purl.uniprot.org/annotation/VAR_042968|||http://purl.uniprot.org/annotation/VAR_042969
http://togogenome.org/gene/9606:CFAP47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZTR5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Calponin-homology (CH)|||Cilia- and flagella-associated protein 47|||Disordered|||In SPGFX3; unknown pathological significance; loss of protein expression; loss of CFAP65 flagellar location.|||In SPGFX3; unknown pathological significance; loss of protein expression; loss of CFAP65 flagellar location; unknown pathological significance.|||In SPGFX3; unknown pathological significance; strongly decreased protein expression.|||In isoform 1.|||In isoform 2.|||In isoform 6.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079731|||http://purl.uniprot.org/annotation/VAR_056856|||http://purl.uniprot.org/annotation/VAR_060280|||http://purl.uniprot.org/annotation/VAR_060281|||http://purl.uniprot.org/annotation/VAR_060282|||http://purl.uniprot.org/annotation/VAR_082879|||http://purl.uniprot.org/annotation/VAR_085272|||http://purl.uniprot.org/annotation/VAR_085273|||http://purl.uniprot.org/annotation/VAR_085274|||http://purl.uniprot.org/annotation/VSP_014372|||http://purl.uniprot.org/annotation/VSP_014373|||http://purl.uniprot.org/annotation/VSP_057885|||http://purl.uniprot.org/annotation/VSP_057886|||http://purl.uniprot.org/annotation/VSP_059490|||http://purl.uniprot.org/annotation/VSP_059491
http://togogenome.org/gene/9606:ACER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2Q2|||http://purl.uniprot.org/uniprot/B7Z2V2|||http://purl.uniprot.org/uniprot/Q9NUN7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alkaline ceramidase 3|||Cytoplasmic|||Decreased enzyme activity.|||Helical|||In PLDECO; impaired protein stability; strongly decreased enzyme activity; decreased ceramide catabolic process; in fibroblasts of patients homozygous for the mutation.|||In isoform 2.|||Lumenal|||Mildly decreased enzyme activity.|||No effect on enzyme activity.|||Strongly decreased enzyme activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212463|||http://purl.uniprot.org/annotation/VAR_081205|||http://purl.uniprot.org/annotation/VSP_039162|||http://purl.uniprot.org/annotation/VSP_039163
http://togogenome.org/gene/9606:EOLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE69                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ASCH|||In isoform 2.|||Protein EOLA1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079740|||http://purl.uniprot.org/annotation/VSP_047240
http://togogenome.org/gene/9606:TMEM237                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96Q45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found at heterozygosity in a patient with Bardet-Biedl syndrome also carrying BBS6 mutation A-57 in MKKS; hypomorphic variant.|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Transmembrane protein 237                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076169|||http://purl.uniprot.org/annotation/VAR_067019|||http://purl.uniprot.org/annotation/VSP_016628|||http://purl.uniprot.org/annotation/VSP_042381|||http://purl.uniprot.org/annotation/VSP_042382|||http://purl.uniprot.org/annotation/VSP_042383
http://togogenome.org/gene/9606:IKBIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70UQ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inhibitor of nuclear factor kappa-B kinase-interacting protein|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000342261|||http://purl.uniprot.org/annotation/VAR_051067|||http://purl.uniprot.org/annotation/VAR_082882|||http://purl.uniprot.org/annotation/VSP_034407|||http://purl.uniprot.org/annotation/VSP_034408|||http://purl.uniprot.org/annotation/VSP_034409|||http://purl.uniprot.org/annotation/VSP_034410
http://togogenome.org/gene/9606:MICALL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3F8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Altered association with membranes.|||Calponin-homology (CH)|||Disordered|||In a breast cancer sample; somatic mutation.|||LIM zinc-binding|||MICAL-like protein 1|||Mediates the interaction with RAB13 and RAB35 and intramolecular interaction with the CH domain|||NPF1|||NPF2|||Necessary and sufficient to associate with tubular recycling endosome membranes, mediate phosphatidic acid-binding and membrane tubulation|||No effect on interaction with EHD1. Complete loss of interaction with EHD1; when associated with 425-A--A-427.|||No effect on interaction with PACSIN2. Loss of interaction with PACSIN2; when associated with 385-A--A-387.|||No effect on interaction with PACSIN2. Loss of interaction with PACSIN2; when associated with 480-A--A-483.|||Partial loss of interaction with EHD1. Complete loss of interaction with EHD1; when associated with 633-A--A-635.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Strongly reduces interaction with EHD1.|||bMERB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075848|||http://purl.uniprot.org/annotation/VAR_018262|||http://purl.uniprot.org/annotation/VAR_020258|||http://purl.uniprot.org/annotation/VAR_036192|||http://purl.uniprot.org/annotation/VAR_050158
http://togogenome.org/gene/9606:TESMIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4I5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CRC|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Tesmin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096626|||http://purl.uniprot.org/annotation/VAR_054067|||http://purl.uniprot.org/annotation/VAR_062236|||http://purl.uniprot.org/annotation/VSP_035297|||http://purl.uniprot.org/annotation/VSP_035298|||http://purl.uniprot.org/annotation/VSP_035299
http://togogenome.org/gene/9606:RIGI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95786                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37|||(Microbial infection) Phosphoserine|||Antiviral innate immune response receptor RIG-I|||CARD 1|||CARD 2|||Complete loss of herpes simplex virus 1 UL37-mediated deamidation; when associated with Q-495.|||Complete loss of herpes simplex virus 1 UL37-mediated deamidation; when associated with Q-549.|||Complete loss of ubiquitination. No interaction with MAVS/IPS1. No induction of IFN-beta.|||DECH box|||Decreased polyubiquitination. Loss of function in RIG-I signaling pathway. Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-849, R-851, R-888, R-907 and R-909.|||Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-788, R-849, R-851, R-888 and R-907.|||Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-788, R-849, R-851, R-888 and R-909.|||Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-788, R-849, R-851, R-907 and R-909.|||Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-788, R-849, R-888, R-907 and R-909.|||Decreased ubiquitination and function in RIG-I signaling pathway without effect on RNA-binding; when associated with R-788, R-851, R-888, R-907 and R-909.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helicase ATP-binding|||Helicase C-terminal|||In SGMRT2; results in constitutive activation and enhanced interferon-mediated signaling.|||In isoform 2.|||Interaction with ZC3HAV1|||Little or no effect on ubiquitination of the 2 CARD domain. Abolishes ubiquitination by RNF125.|||Little or no effect on ubiquitination of the 2 CARD domains.|||Loss of dsRNA-induced ATPase activity. Changed RIG-I signaling pathway.|||Loss of dsRNA-induced ATPase activity. No effect on ds-RNA binding. Changed RIG-I signaling pathway.|||Mediates interaction with RNF135|||N6-acetyllysine|||No IRF3 signaling activity. Loss of dsRNA-induced ATPase activity. No effect on ds-RNA binding. Changed RIG-I signaling pathway.|||No IRF3 signaling activity. No effect on dsRNA binding.|||No effect on dsRNA-induced ATPase activity. Changed RIG-I signaling pathway.|||Phosphoserine; by CK2|||Phosphothreonine; by CK2|||RLR CTR|||Reduction of ubiquitination. Reduction of INFB induction.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144093|||http://purl.uniprot.org/annotation/VAR_023747|||http://purl.uniprot.org/annotation/VAR_023748|||http://purl.uniprot.org/annotation/VAR_073667|||http://purl.uniprot.org/annotation/VAR_073668|||http://purl.uniprot.org/annotation/VSP_016054
http://togogenome.org/gene/9606:COPZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P299                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Coatomer subunit zeta-2|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193831
http://togogenome.org/gene/9606:NPM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75607                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||N-acetylalanine|||Nucleoplasmin-3|||Omega-N-methylarginine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219489|||http://purl.uniprot.org/annotation/VAR_050410|||http://purl.uniprot.org/annotation/VAR_050411
http://togogenome.org/gene/9606:NSD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZ95                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  AWS|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase NSD3|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||PHD-type 1|||PHD-type 2|||PHD-type 3|||PHD-type 4; atypical|||PWWP 1|||PWWP 2|||Phosphoserine|||Polar residues|||Post-SET|||Pro residues|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259521|||http://purl.uniprot.org/annotation/VAR_028950|||http://purl.uniprot.org/annotation/VAR_061215|||http://purl.uniprot.org/annotation/VSP_021427|||http://purl.uniprot.org/annotation/VSP_021428|||http://purl.uniprot.org/annotation/VSP_021429|||http://purl.uniprot.org/annotation/VSP_021430|||http://purl.uniprot.org/annotation/VSP_054489
http://togogenome.org/gene/9606:NEXN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDI0|||http://purl.uniprot.org/uniprot/Q0ZGT2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ig-like|||In CMD1CC; affects cardiac Z line integrity; no effect on protein expression and stability.|||In CMD1CC; affects cardiac Z-disk integrity; no effect on protein expression and stability.|||In CMH20; affects interaction with ACTA1 and F-actin.|||In CMH20; the mutant protein accumulates in the cytoplasm but binding to ACTA1 is not altered.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Nexilin|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302085|||http://purl.uniprot.org/annotation/VAR_049963|||http://purl.uniprot.org/annotation/VAR_059414|||http://purl.uniprot.org/annotation/VAR_063009|||http://purl.uniprot.org/annotation/VAR_063010|||http://purl.uniprot.org/annotation/VAR_063011|||http://purl.uniprot.org/annotation/VAR_065477|||http://purl.uniprot.org/annotation/VAR_065478|||http://purl.uniprot.org/annotation/VSP_043439|||http://purl.uniprot.org/annotation/VSP_052541|||http://purl.uniprot.org/annotation/VSP_052542|||http://purl.uniprot.org/annotation/VSP_052543
http://togogenome.org/gene/9606:TRMT10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z9F7|||http://purl.uniprot.org/uniprot/Q6PF06                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||SAM-dependent MTase TRM10-type|||tRNA methyltransferase 10 homolog B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311321|||http://purl.uniprot.org/annotation/VAR_037224|||http://purl.uniprot.org/annotation/VAR_037225|||http://purl.uniprot.org/annotation/VSP_029519|||http://purl.uniprot.org/annotation/VSP_029520|||http://purl.uniprot.org/annotation/VSP_029521|||http://purl.uniprot.org/annotation/VSP_054652|||http://purl.uniprot.org/annotation/VSP_054653|||http://purl.uniprot.org/annotation/VSP_055735
http://togogenome.org/gene/9606:AMDHD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y303                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In a colorectal cancer sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylglucosamine-6-phosphate deacetylase|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315776|||http://purl.uniprot.org/annotation/VAR_038301|||http://purl.uniprot.org/annotation/VSP_030698|||http://purl.uniprot.org/annotation/VSP_038782
http://togogenome.org/gene/9606:SFTPC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTC9|||http://purl.uniprot.org/uniprot/A0A0S2Z4Q0|||http://purl.uniprot.org/uniprot/E5RI64|||http://purl.uniprot.org/uniprot/P11686                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  BRICHOS|||Helical|||In SMDP2.|||In SMDP2; abnormal trafficking and accumulation of aberrantly processed proSPC within alveoli.|||In SMDP2; targeted abnormally to early endosomes and likely to result in a toxic gain of function.|||In isoform 2.|||Influences susceptibility to RDS in premature infants.|||Pulmonary surfactant-associated protein C|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033477|||http://purl.uniprot.org/annotation/PRO_0000033478|||http://purl.uniprot.org/annotation/PRO_0000033479|||http://purl.uniprot.org/annotation/VAR_007453|||http://purl.uniprot.org/annotation/VAR_016175|||http://purl.uniprot.org/annotation/VAR_026753|||http://purl.uniprot.org/annotation/VAR_026754|||http://purl.uniprot.org/annotation/VAR_026755|||http://purl.uniprot.org/annotation/VAR_026756|||http://purl.uniprot.org/annotation/VAR_036855|||http://purl.uniprot.org/annotation/VSP_006311
http://togogenome.org/gene/9606:LIN52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q52LA3                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Turn                                                                                  ^@                                                                                  Phosphoserine|||Protein lin-52 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252154
http://togogenome.org/gene/9606:FREM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5H8C1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  C-type lectin|||CSPG 1|||CSPG 10|||CSPG 11|||CSPG 12|||CSPG 2|||CSPG 3|||CSPG 4|||CSPG 5|||CSPG 6|||CSPG 7|||CSPG 8|||CSPG 9|||Calx-beta|||Cell attachment site|||FRAS1-related extracellular matrix protein 1|||In BNAR.|||In MOTA.|||In MOTA; unknown pathological significance.|||In TRIGNO2.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010122|||http://purl.uniprot.org/annotation/VAR_047317|||http://purl.uniprot.org/annotation/VAR_047318|||http://purl.uniprot.org/annotation/VAR_047319|||http://purl.uniprot.org/annotation/VAR_047320|||http://purl.uniprot.org/annotation/VAR_047321|||http://purl.uniprot.org/annotation/VAR_047322|||http://purl.uniprot.org/annotation/VAR_047323|||http://purl.uniprot.org/annotation/VAR_047324|||http://purl.uniprot.org/annotation/VAR_047325|||http://purl.uniprot.org/annotation/VAR_047326|||http://purl.uniprot.org/annotation/VAR_063422|||http://purl.uniprot.org/annotation/VAR_063423|||http://purl.uniprot.org/annotation/VAR_066412|||http://purl.uniprot.org/annotation/VAR_066413|||http://purl.uniprot.org/annotation/VAR_067916|||http://purl.uniprot.org/annotation/VAR_067917|||http://purl.uniprot.org/annotation/VAR_078339|||http://purl.uniprot.org/annotation/VSP_015025|||http://purl.uniprot.org/annotation/VSP_015026|||http://purl.uniprot.org/annotation/VSP_015029|||http://purl.uniprot.org/annotation/VSP_015030|||http://purl.uniprot.org/annotation/VSP_015031|||http://purl.uniprot.org/annotation/VSP_047283|||http://purl.uniprot.org/annotation/VSP_047284
http://togogenome.org/gene/9606:INPP5J                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WVS7|||http://purl.uniprot.org/uniprot/B4DF95|||http://purl.uniprot.org/uniprot/Q15735                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Catalytic|||Disordered|||In isoform 2.|||In isoform 3.|||Inositol polyphosphate-related phosphatase|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A|||Phosphoserine|||Polar residues|||Pro residues|||RSXSXX motif 1|||RSXSXX motif 2|||RSXSXX motif 3|||RSXSXX motif 4|||RSXSXX motif 5|||Required for ruffle localization|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209738|||http://purl.uniprot.org/annotation/VAR_028107|||http://purl.uniprot.org/annotation/VSP_007296|||http://purl.uniprot.org/annotation/VSP_021017
http://togogenome.org/gene/9606:SH3BGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9JJT2|||http://purl.uniprot.org/uniprot/P55822                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||SH3 domain-binding glutamic acid-rich protein|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220743|||http://purl.uniprot.org/annotation/VAR_028233|||http://purl.uniprot.org/annotation/VAR_057182|||http://purl.uniprot.org/annotation/VAR_057183|||http://purl.uniprot.org/annotation/VSP_045788
http://togogenome.org/gene/9606:PET117                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/L0R6F6|||http://purl.uniprot.org/uniprot/Q6UWS5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide|||Transit Peptide                                                                                  ^@                                                                                  In MC4DN19.|||Mitochondrion|||Protein PET117 homolog, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000416096|||http://purl.uniprot.org/annotation/PRO_5003947635|||http://purl.uniprot.org/annotation/VAR_084185
http://togogenome.org/gene/9606:SDC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75056                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage of ectodomain|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||O-linked (GalNAc) serine; by GALNT13|||O-linked (GalNAc) threonine; by GALNT13|||O-linked (Xyl...) (glycosaminoglycan) serine|||Phosphotyrosine|||Polar residues|||Syndecan-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183989|||http://purl.uniprot.org/annotation/VAR_027251|||http://purl.uniprot.org/annotation/VAR_027252|||http://purl.uniprot.org/annotation/VAR_027253
http://togogenome.org/gene/9606:PPP1R10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L6I0|||http://purl.uniprot.org/uniprot/Q96QC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C3H1-type|||Disordered|||Essential for PPP1CA inhibition|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with TOX4|||Interaction with WDR82|||Necessary for interaction with PPP1CA|||Necessary for interaction with PPP1CC|||Omega-N-methylarginine|||PP1-binding motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Serine/threonine-protein phosphatase 1 regulatory subunit 10|||TFIIS N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071510|||http://purl.uniprot.org/annotation/VAR_051747
http://togogenome.org/gene/9606:NUP43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFH3|||http://purl.uniprot.org/uniprot/Q8TEA6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N-acetylmethionine|||Nucleoporin Nup43|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051111|||http://purl.uniprot.org/annotation/VSP_056167
http://togogenome.org/gene/9606:FAM47A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JRC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FAM47A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187037|||http://purl.uniprot.org/annotation/VAR_054412|||http://purl.uniprot.org/annotation/VAR_054413|||http://purl.uniprot.org/annotation/VAR_054414|||http://purl.uniprot.org/annotation/VAR_054415|||http://purl.uniprot.org/annotation/VAR_054416
http://togogenome.org/gene/9606:DUSP13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXN7|||http://purl.uniprot.org/uniprot/Q6B8I1|||http://purl.uniprot.org/uniprot/Q9UII6                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Dual specificity protein phosphatase 13A|||Dual specificity protein phosphatase 13B|||In isoform 2.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Loss of enzyme activity. No effect on interaction with MAP3K5.|||No effect on interaction with MAP3K5.|||Phosphocysteine intermediate|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||protein-serine/threonine phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094820|||http://purl.uniprot.org/annotation/PRO_0000381973|||http://purl.uniprot.org/annotation/PRO_5040046720|||http://purl.uniprot.org/annotation/VAR_025431|||http://purl.uniprot.org/annotation/VAR_057130|||http://purl.uniprot.org/annotation/VAR_057131|||http://purl.uniprot.org/annotation/VAR_058495|||http://purl.uniprot.org/annotation/VSP_037858|||http://purl.uniprot.org/annotation/VSP_046445|||http://purl.uniprot.org/annotation/VSP_046446|||http://purl.uniprot.org/annotation/VSP_046447|||http://purl.uniprot.org/annotation/VSP_046448|||http://purl.uniprot.org/annotation/VSP_046449|||http://purl.uniprot.org/annotation/VSP_047819|||http://purl.uniprot.org/annotation/VSP_061945
http://togogenome.org/gene/9606:ZNF174                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/I3L2H2|||http://purl.uniprot.org/uniprot/Q15697                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Region|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Polar residues|||SCAN box|||Zinc finger protein 174                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047439|||http://purl.uniprot.org/annotation/VSP_006897|||http://purl.uniprot.org/annotation/VSP_006898
http://togogenome.org/gene/9606:C17orf49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXM2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Chromatin complexes subunit BAP18|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Pro residues|||SANT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000264251|||http://purl.uniprot.org/annotation/VSP_043754|||http://purl.uniprot.org/annotation/VSP_047095
http://togogenome.org/gene/9606:SPAG9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60271|||http://purl.uniprot.org/uniprot/Q5JB53                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C-Jun-amino-terminal kinase-interacting protein 4|||Disordered|||In isoform 2, isoform 4, isoform 5 and isoform 6.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||RH1|||RH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234076|||http://purl.uniprot.org/annotation/VAR_059364|||http://purl.uniprot.org/annotation/VSP_018214|||http://purl.uniprot.org/annotation/VSP_018220|||http://purl.uniprot.org/annotation/VSP_018221|||http://purl.uniprot.org/annotation/VSP_018222|||http://purl.uniprot.org/annotation/VSP_042253|||http://purl.uniprot.org/annotation/VSP_042254
http://togogenome.org/gene/9606:PRMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3N3|||http://purl.uniprot.org/uniprot/P55345                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform PRMT2Alpha.|||In isoform PRMT2Beta.|||In isoform PRMT2Gamma.|||In isoform PRMT2L2.|||Interaction with ESR1|||Interaction with RB1|||Protein arginine N-methyltransferase 2|||SAM-dependent MTase PRMT-type|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212324|||http://purl.uniprot.org/annotation/VSP_042680|||http://purl.uniprot.org/annotation/VSP_043381|||http://purl.uniprot.org/annotation/VSP_054927|||http://purl.uniprot.org/annotation/VSP_054928|||http://purl.uniprot.org/annotation/VSP_054929|||http://purl.uniprot.org/annotation/VSP_054930|||http://purl.uniprot.org/annotation/VSP_054931|||http://purl.uniprot.org/annotation/VSP_054932
http://togogenome.org/gene/9606:YTHDF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYJ9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished binding to N6-methyladenosine (m6A)-containing RNAs.|||Disordered|||In isoform 2.|||Increased binding to N6-methyladenosine (m6A)-containing RNAs.|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Reduced binding to N6-methyladenosine (m6A)-containing RNAs.|||Removed|||Strongly reduced binding to N6-methyladenosine (m6A)-containing RNAs.|||YTH|||YTH domain-containing family protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223073|||http://purl.uniprot.org/annotation/VSP_006815|||http://purl.uniprot.org/annotation/VSP_006816|||http://purl.uniprot.org/annotation/VSP_006817
http://togogenome.org/gene/9606:VARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RCN6|||http://purl.uniprot.org/uniprot/P26640                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  'HIGH' region|||'KMSKS' region|||Basic and acidic residues|||Disordered|||GST C-terminal|||In NDMSCA; unknown pathological significance.|||In isoform 2.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Removed|||Valine--tRNA ligase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106253|||http://purl.uniprot.org/annotation/VAR_052647|||http://purl.uniprot.org/annotation/VAR_052648|||http://purl.uniprot.org/annotation/VAR_052649|||http://purl.uniprot.org/annotation/VAR_052650|||http://purl.uniprot.org/annotation/VAR_061909|||http://purl.uniprot.org/annotation/VAR_080602|||http://purl.uniprot.org/annotation/VAR_080603|||http://purl.uniprot.org/annotation/VSP_056480|||http://purl.uniprot.org/annotation/VSP_056481|||http://purl.uniprot.org/annotation/VSP_056482
http://togogenome.org/gene/9606:FBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09467|||http://purl.uniprot.org/uniprot/Q2TU34                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fructose-1,6-bisphosphatase 1|||Fructose-1-6-bisphosphatase class 1 C-terminal|||Fructose-1-6-bisphosphatase class I N-terminal|||In FBP1D.|||In FBP1D; unknown pathological significance.|||Increased affinity towards Ca(2+) and Mg(2+).|||N-acetylalanine|||N6-succinyllysine|||Phosphotyrosine|||Reduced activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200498|||http://purl.uniprot.org/annotation/VAR_002380|||http://purl.uniprot.org/annotation/VAR_002381|||http://purl.uniprot.org/annotation/VAR_002382|||http://purl.uniprot.org/annotation/VAR_022212|||http://purl.uniprot.org/annotation/VAR_022213|||http://purl.uniprot.org/annotation/VAR_022214|||http://purl.uniprot.org/annotation/VAR_038812|||http://purl.uniprot.org/annotation/VAR_038813|||http://purl.uniprot.org/annotation/VAR_075492
http://togogenome.org/gene/9606:CCDC62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P9F0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abrogates interaction with ESR1 and ESR2.|||Coiled-coil domain-containing protein 62|||Disordered|||In SPGF67.|||In SPGF67; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||LXXLL motif 1|||LXXLL motif 2|||No effect on interaction with ESR1 or ESR2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240247|||http://purl.uniprot.org/annotation/VAR_026715|||http://purl.uniprot.org/annotation/VAR_035498|||http://purl.uniprot.org/annotation/VAR_061585|||http://purl.uniprot.org/annotation/VAR_086975|||http://purl.uniprot.org/annotation/VAR_086976|||http://purl.uniprot.org/annotation/VSP_019327|||http://purl.uniprot.org/annotation/VSP_019328|||http://purl.uniprot.org/annotation/VSP_019329
http://togogenome.org/gene/9606:CDRT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9R6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  CMT1A duplicated region transcript 4 protein|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314903|||http://purl.uniprot.org/annotation/VAR_038119|||http://purl.uniprot.org/annotation/VAR_038120
http://togogenome.org/gene/9606:MYO5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8CDT9|||http://purl.uniprot.org/uniprot/Q9UES4|||http://purl.uniprot.org/uniprot/Q9Y4I1                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Actin-binding|||Dilute|||Disordered|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||In isoform 2.|||In isoform 3.|||Myosin N-terminal SH3-like|||Myosin motor|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Unconventional myosin-Va                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123456|||http://purl.uniprot.org/annotation/VAR_010645|||http://purl.uniprot.org/annotation/VAR_056180|||http://purl.uniprot.org/annotation/VAR_056181|||http://purl.uniprot.org/annotation/VSP_003351|||http://purl.uniprot.org/annotation/VSP_003352
http://togogenome.org/gene/9606:ZNF277                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRM2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||Drastic reduction in binding to RPS2.|||In a breast cancer sample; somatic mutation.|||Modest reduction in binding to RPS2.|||N-acetylalanine|||Removed|||Zinc finger protein 277                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047503|||http://purl.uniprot.org/annotation/VAR_035574|||http://purl.uniprot.org/annotation/VAR_035575|||http://purl.uniprot.org/annotation/VAR_057415|||http://purl.uniprot.org/annotation/VAR_059908
http://togogenome.org/gene/9606:XDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P47989                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  2Fe-2S ferredoxin-type|||Abolishes xanthine oxidase activity.|||FAD-binding PCMH-type|||In XAN1.|||In a breast cancer sample; somatic mutation.|||In oxidase form|||Proton acceptor|||Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes.|||Xanthine dehydrogenase/oxidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166084|||http://purl.uniprot.org/annotation/VAR_023976|||http://purl.uniprot.org/annotation/VAR_023977|||http://purl.uniprot.org/annotation/VAR_023978|||http://purl.uniprot.org/annotation/VAR_023979|||http://purl.uniprot.org/annotation/VAR_023980|||http://purl.uniprot.org/annotation/VAR_023981|||http://purl.uniprot.org/annotation/VAR_023982|||http://purl.uniprot.org/annotation/VAR_023983|||http://purl.uniprot.org/annotation/VAR_023984|||http://purl.uniprot.org/annotation/VAR_023985|||http://purl.uniprot.org/annotation/VAR_023986|||http://purl.uniprot.org/annotation/VAR_023987|||http://purl.uniprot.org/annotation/VAR_023988|||http://purl.uniprot.org/annotation/VAR_023989|||http://purl.uniprot.org/annotation/VAR_023990|||http://purl.uniprot.org/annotation/VAR_023991|||http://purl.uniprot.org/annotation/VAR_035899|||http://purl.uniprot.org/annotation/VAR_035900|||http://purl.uniprot.org/annotation/VAR_045900|||http://purl.uniprot.org/annotation/VAR_045901
http://togogenome.org/gene/9606:NSUN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08J23                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolished mRNA methyltransferase activity; when associated with A-271.|||Abolished mRNA methyltransferase activity; when associated with A-321.|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In MRT5; impairs proper intracellular localization.|||In isoform 2.|||In isoform 3.|||Induces a constitutive association with NPM1.|||Loss of RNA methyltransferase activity.|||Mimicks constitutive phosphorylation and abolishes methyltransferase activity.|||N6-acetyllysine; alternate|||N6-malonyllysine; alternate|||Nucleophile|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphothreonine|||Polar residues|||RNA cytosine C(5)-methyltransferase NSUN2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289223|||http://purl.uniprot.org/annotation/VAR_032604|||http://purl.uniprot.org/annotation/VAR_068530|||http://purl.uniprot.org/annotation/VSP_042621|||http://purl.uniprot.org/annotation/VSP_053598
http://togogenome.org/gene/9606:GNG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK08                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Propeptide                                                                                  ^@                                                                                  Chain|||Lipid Binding|||Modified Residue|||Propeptide                                                                                  ^@                                                                                  Cysteine methyl ester|||Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012649|||http://purl.uniprot.org/annotation/PRO_0000012650
http://togogenome.org/gene/9606:KCNH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7W1|||http://purl.uniprot.org/uniprot/A0A090N7X5|||http://purl.uniprot.org/uniprot/A0A090N8Q0|||http://purl.uniprot.org/uniprot/Q12809|||http://purl.uniprot.org/uniprot/Q15BH2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes cell surface expression; has no effect on N-glycosylation.|||Abolishes phosphorylation; when associated with A-283; A-890 and A-1137.|||Abolishes phosphorylation; when associated with A-283; A-890 and A-895.|||Abolishes phosphorylation; when associated with A-283; A-895 and A-1137.|||Abolishes phosphorylation; when associated with A-890; A-895 and A-1137.|||Basic and acidic residues|||Cyclic nucleotide-binding|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In LQT2.|||In LQT2; aberrant protein folding increases the association of mutant KCNH2 with CANX and results in defective protein trafficking.|||In LQT2; bradycardia-induced.|||In LQT2; decreased protein stability.|||In LQT2; digenic; the patient also carries mutation N-1819 on SCN5A.|||In LQT2; impairs channel function; exhibits reduced activating currents compared to wild-type; cell surface trafficking is not impaired; does not exert dominant-negative effects on wild-type channel; the half-maximal activation voltage is not significantly affected by the mutation.|||In LQT2; located on the same allele as Asn-525.|||In LQT2; located on the same allele as Pro-528.|||In LQT2; severe form.|||In LQT2; the mutation reduces wild-type channel expression.|||In LQT2; unknown pathological significance.|||In SQT1.|||In isoform 3.1.|||In isoform 4.|||In isoform A-USO and isoform B-USO.|||In isoform B-USO.|||In isoform B.|||N-linked (GlcNAc...) asparagine|||No effect on cell surface expression, but changes inactivation kinetics; when associated with A-631.|||No effect on cell surface expression, but changes inactivation kinetics; when associated with Q-598.|||Omega-N-methylarginine|||PAC|||PAS|||Phosphoserine|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 2|||Predisposes to LQT2 and torsades de pointes while taking the drug amiodarone; in vitro studies confirmed a significant reduction in potassium currents; the ECG abnormalities reversed on drug withdrawal.|||Selectivity filter|||Slows down deactivation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053999|||http://purl.uniprot.org/annotation/VAR_008578|||http://purl.uniprot.org/annotation/VAR_008579|||http://purl.uniprot.org/annotation/VAR_008580|||http://purl.uniprot.org/annotation/VAR_008581|||http://purl.uniprot.org/annotation/VAR_008582|||http://purl.uniprot.org/annotation/VAR_008583|||http://purl.uniprot.org/annotation/VAR_008584|||http://purl.uniprot.org/annotation/VAR_008907|||http://purl.uniprot.org/annotation/VAR_008908|||http://purl.uniprot.org/annotation/VAR_008909|||http://purl.uniprot.org/annotation/VAR_008910|||http://purl.uniprot.org/annotation/VAR_008911|||http://purl.uniprot.org/annotation/VAR_008912|||http://purl.uniprot.org/annotation/VAR_008913|||http://purl.uniprot.org/annotation/VAR_008914|||http://purl.uniprot.org/annotation/VAR_008915|||http://purl.uniprot.org/annotation/VAR_008916|||http://purl.uniprot.org/annotation/VAR_008917|||http://purl.uniprot.org/annotation/VAR_008918|||http://purl.uniprot.org/annotation/VAR_008919|||http://purl.uniprot.org/annotation/VAR_008920|||http://purl.uniprot.org/annotation/VAR_008921|||http://purl.uniprot.org/annotation/VAR_008922|||http://purl.uniprot.org/annotation/VAR_008923|||http://purl.uniprot.org/annotation/VAR_008924|||http://purl.uniprot.org/annotation/VAR_008925|||http://purl.uniprot.org/annotation/VAR_008926|||http://purl.uniprot.org/annotation/VAR_008927|||http://purl.uniprot.org/annotation/VAR_008928|||http://purl.uniprot.org/annotation/VAR_008929|||http://purl.uniprot.org/annotation/VAR_008930|||http://purl.uniprot.org/annotation/VAR_008931|||http://purl.uniprot.org/annotation/VAR_008932|||http://purl.uniprot.org/annotation/VAR_008933|||http://purl.uniprot.org/annotation/VAR_008934|||http://purl.uniprot.org/annotation/VAR_008935|||http://purl.uniprot.org/annotation/VAR_008936|||http://purl.uniprot.org/annotation/VAR_008937|||http://purl.uniprot.org/annotation/VAR_008938|||http://purl.uniprot.org/annotation/VAR_009178|||http://purl.uniprot.org/annotation/VAR_009179|||http://purl.uniprot.org/annotation/VAR_009909|||http://purl.uniprot.org/annotation/VAR_009910|||http://purl.uniprot.org/annotation/VAR_009911|||http://purl.uniprot.org/annotation/VAR_009912|||http://purl.uniprot.org/annotation/VAR_009913|||http://purl.uniprot.org/annotation/VAR_009914|||http://purl.uniprot.org/annotation/VAR_009915|||http://purl.uniprot.org/annotation/VAR_009916|||http://purl.uniprot.org/annotation/VAR_014371|||http://purl.uniprot.org/annotation/VAR_014372|||http://purl.uniprot.org/annotation/VAR_014373|||http://purl.uniprot.org/annotation/VAR_014374|||http://purl.uniprot.org/annotation/VAR_014375|||http://purl.uniprot.org/annotation/VAR_014376|||http://purl.uniprot.org/annotation/VAR_014377|||http://purl.uniprot.org/annotation/VAR_014378|||http://purl.uniprot.org/annotation/VAR_014379|||http://purl.uniprot.org/annotation/VAR_014380|||http://purl.uniprot.org/annotation/VAR_014381|||http://purl.uniprot.org/annotation/VAR_014382|||http://purl.uniprot.org/annotation/VAR_014383|||http://purl.uniprot.org/annotation/VAR_014384|||http://purl.uniprot.org/annotation/VAR_014385|||http://purl.uniprot.org/annotation/VAR_014386|||http://purl.uniprot.org/annotation/VAR_014387|||http://purl.uniprot.org/annotation/VAR_014388|||http://purl.uniprot.org/annotation/VAR_014389|||http://purl.uniprot.org/annotation/VAR_014390|||http://purl.uniprot.org/annotation/VAR_023840|||http://purl.uniprot.org/annotation/VAR_036669|||http://purl.uniprot.org/annotation/VAR_036670|||http://purl.uniprot.org/annotation/VAR_036671|||http://purl.uniprot.org/annotation/VAR_036672|||http://purl.uniprot.org/annotation/VAR_036673|||http://purl.uniprot.org/annotation/VAR_036674|||http://purl.uniprot.org/annotation/VAR_036675|||http://purl.uniprot.org/annotation/VAR_036676|||http://purl.uniprot.org/annotation/VAR_036677|||http://purl.uniprot.org/annotation/VAR_036678|||http://purl.uniprot.org/annotation/VAR_036679|||http://purl.uniprot.org/annotation/VAR_036680|||http://purl.uniprot.org/annotation/VAR_036681|||http://purl.uniprot.org/annotation/VAR_036682|||http://purl.uniprot.org/annotation/VAR_068249|||http://purl.uniprot.org/annotation/VAR_068250|||http://purl.uniprot.org/annotation/VAR_068251|||http://purl.uniprot.org/annotation/VAR_068252|||http://purl.uniprot.org/annotation/VAR_068253|||http://purl.uniprot.org/annotation/VAR_068254|||http://purl.uniprot.org/annotation/VAR_068255|||http://purl.uniprot.org/annotation/VAR_068256|||http://purl.uniprot.org/annotation/VAR_068257|||http://purl.uniprot.org/annotation/VAR_068258|||http://purl.uniprot.org/annotation/VAR_068259|||http://purl.uniprot.org/annotation/VAR_068260|||http://purl.uniprot.org/annotation/VAR_068261|||http://purl.uniprot.org/annotation/VAR_068262|||http://purl.uniprot.org/annotation/VAR_068263|||http://purl.uniprot.org/annotation/VAR_068264|||http://purl.uniprot.org/annotation/VAR_068265|||http://purl.uniprot.org/annotation/VAR_068266|||http://purl.uniprot.org/annotation/VAR_068267|||http://purl.uniprot.org/annotation/VAR_068268|||http://purl.uniprot.org/annotation/VAR_068269|||http://purl.uniprot.org/annotation/VAR_068270|||http://purl.uniprot.org/annotation/VAR_068271|||http://purl.uniprot.org/annotation/VAR_068272|||http://purl.uniprot.org/annotation/VAR_068273|||http://purl.uniprot.org/annotation/VAR_068274|||http://purl.uniprot.org/annotation/VAR_068275|||http://purl.uniprot.org/annotation/VAR_068276|||http://purl.uniprot.org/annotation/VAR_068277|||http://purl.uniprot.org/annotation/VAR_068278|||http://purl.uniprot.org/annotation/VAR_068279|||http://purl.uniprot.org/annotation/VAR_068280|||http://purl.uniprot.org/annotation/VAR_068281|||http://purl.uniprot.org/annotation/VAR_068282|||http://purl.uniprot.org/annotation/VAR_068283|||http://purl.uniprot.org/annotation/VAR_068284|||http://purl.uniprot.org/annotation/VAR_068285|||http://purl.uniprot.org/annotation/VAR_068286|||http://purl.uniprot.org/annotation/VAR_074684|||http://purl.uniprot.org/annotation/VAR_074685|||http://purl.uniprot.org/annotation/VAR_074686|||http://purl.uniprot.org/annotation/VAR_074765|||http://purl.uniprot.org/annotation/VAR_074766|||http://purl.uniprot.org/annotation/VAR_074767|||http://purl.uniprot.org/annotation/VAR_074768|||http://purl.uniprot.org/annotation/VAR_074769|||http://purl.uniprot.org/annotation/VAR_074770|||http://purl.uniprot.org/annotation/VAR_074771|||http://purl.uniprot.org/annotation/VAR_074772|||http://purl.uniprot.org/annotation/VAR_074773|||http://purl.uniprot.org/annotation/VAR_074774|||http://purl.uniprot.org/annotation/VAR_074775|||http://purl.uniprot.org/annotation/VAR_074776|||http://purl.uniprot.org/annotation/VAR_074777|||http://purl.uniprot.org/annotation/VAR_074778|||http://purl.uniprot.org/annotation/VAR_074779|||http://purl.uniprot.org/annotation/VAR_074780|||http://purl.uniprot.org/annotation/VAR_074781|||http://purl.uniprot.org/annotation/VAR_074782|||http://purl.uniprot.org/annotation/VAR_074783|||http://purl.uniprot.org/annotation/VAR_074784|||http://purl.uniprot.org/annotation/VAR_074785|||http://purl.uniprot.org/annotation/VAR_074786|||http://purl.uniprot.org/annotation/VAR_074787|||http://purl.uniprot.org/annotation/VAR_074788|||http://purl.uniprot.org/annotation/VAR_074789|||http://purl.uniprot.org/annotation/VAR_074790|||http://purl.uniprot.org/annotation/VAR_074791|||http://purl.uniprot.org/annotation/VAR_074792|||http://purl.uniprot.org/annotation/VAR_074793|||http://purl.uniprot.org/annotation/VAR_074794|||http://purl.uniprot.org/annotation/VAR_074795|||http://purl.uniprot.org/annotation/VAR_074796|||http://purl.uniprot.org/annotation/VAR_074797|||http://purl.uniprot.org/annotation/VAR_074798|||http://purl.uniprot.org/annotation/VAR_074799|||http://purl.uniprot.org/annotation/VAR_074800|||http://purl.uniprot.org/annotation/VAR_074801|||http://purl.uniprot.org/annotation/VAR_074802|||http://purl.uniprot.org/annotation/VAR_074803|||http://purl.uniprot.org/annotation/VAR_074804|||http://purl.uniprot.org/annotation/VAR_074805|||http://purl.uniprot.org/annotation/VAR_074806|||http://purl.uniprot.org/annotation/VAR_074807|||http://purl.uniprot.org/annotation/VAR_074808|||http://purl.uniprot.org/annotation/VAR_074809|||http://purl.uniprot.org/annotation/VAR_074810|||http://purl.uniprot.org/annotation/VAR_074811|||http://purl.uniprot.org/annotation/VAR_074812|||http://purl.uniprot.org/annotation/VAR_074813|||http://purl.uniprot.org/annotation/VAR_074814|||http://purl.uniprot.org/annotation/VAR_074815|||http://purl.uniprot.org/annotation/VAR_074816|||http://purl.uniprot.org/annotation/VAR_074817|||http://purl.uniprot.org/annotation/VAR_074818|||http://purl.uniprot.org/annotation/VAR_074819|||http://purl.uniprot.org/annotation/VAR_074820|||http://purl.uniprot.org/annotation/VAR_074821|||http://purl.uniprot.org/annotation/VAR_074822|||http://purl.uniprot.org/annotation/VAR_074823|||http://purl.uniprot.org/annotation/VAR_074824|||http://purl.uniprot.org/annotation/VAR_074825|||http://purl.uniprot.org/annotation/VAR_074826|||http://purl.uniprot.org/annotation/VAR_074827|||http://purl.uniprot.org/annotation/VAR_074828|||http://purl.uniprot.org/annotation/VAR_074829|||http://purl.uniprot.org/annotation/VAR_074830|||http://purl.uniprot.org/annotation/VAR_074831|||http://purl.uniprot.org/annotation/VAR_074832|||http://purl.uniprot.org/annotation/VAR_074833|||http://purl.uniprot.org/annotation/VAR_074834|||http://purl.uniprot.org/annotation/VAR_074835|||http://purl.uniprot.org/annotation/VAR_074836|||http://purl.uniprot.org/annotation/VAR_074837|||http://purl.uniprot.org/annotation/VAR_074838|||http://purl.uniprot.org/annotation/VAR_074839|||http://purl.uniprot.org/annotation/VAR_074840|||http://purl.uniprot.org/annotation/VAR_074841|||http://purl.uniprot.org/annotation/VAR_074842|||http://purl.uniprot.org/annotation/VAR_074843|||http://purl.uniprot.org/annotation/VAR_074844|||http://purl.uniprot.org/annotation/VAR_074845|||http://purl.uniprot.org/annotation/VAR_074846|||http://purl.uniprot.org/annotation/VAR_074847|||http://purl.uniprot.org/annotation/VAR_074848|||http://purl.uniprot.org/annotation/VAR_074849|||http://purl.uniprot.org/annotation/VAR_074850|||http://purl.uniprot.org/annotation/VAR_074851|||http://purl.uniprot.org/annotation/VAR_074852|||http://purl.uniprot.org/annotation/VAR_074853|||http://purl.uniprot.org/annotation/VAR_074854|||http://purl.uniprot.org/annotation/VAR_074855|||http://purl.uniprot.org/annotation/VAR_074856|||http://purl.uniprot.org/annotation/VAR_074857|||http://purl.uniprot.org/annotation/VAR_074858|||http://purl.uniprot.org/annotation/VAR_074859|||http://purl.uniprot.org/annotation/VAR_074860|||http://purl.uniprot.org/annotation/VAR_074861|||http://purl.uniprot.org/annotation/VAR_074862|||http://purl.uniprot.org/annotation/VAR_074863|||http://purl.uniprot.org/annotation/VAR_074864|||http://purl.uniprot.org/annotation/VAR_074865|||http://purl.uniprot.org/annotation/VAR_074866|||http://purl.uniprot.org/annotation/VAR_074867|||http://purl.uniprot.org/annotation/VAR_074868|||http://purl.uniprot.org/annotation/VAR_074869|||http://purl.uniprot.org/annotation/VAR_074870|||http://purl.uniprot.org/annotation/VAR_074871|||http://purl.uniprot.org/annotation/VAR_074872|||http://purl.uniprot.org/annotation/VAR_074873|||http://purl.uniprot.org/annotation/VAR_074874|||http://purl.uniprot.org/annotation/VAR_074875|||http://purl.uniprot.org/annotation/VAR_074876|||http://purl.uniprot.org/annotation/VAR_074877|||http://purl.uniprot.org/annotation/VAR_074878|||http://purl.uniprot.org/annotation/VAR_074879|||http://purl.uniprot.org/annotation/VAR_074880|||http://purl.uniprot.org/annotation/VAR_074881|||http://purl.uniprot.org/annotation/VAR_074882|||http://purl.uniprot.org/annotation/VAR_074883|||http://purl.uniprot.org/annotation/VAR_074884|||http://purl.uniprot.org/annotation/VAR_074885|||http://purl.uniprot.org/annotation/VAR_074886|||http://purl.uniprot.org/annotation/VAR_074887|||http://purl.uniprot.org/annotation/VAR_074888|||http://purl.uniprot.org/annotation/VAR_074889|||http://purl.uniprot.org/annotation/VAR_074890|||http://purl.uniprot.org/annotation/VAR_074891|||http://purl.uniprot.org/annotation/VAR_074892|||http://purl.uniprot.org/annotation/VAR_074893|||http://purl.uniprot.org/annotation/VAR_074894|||http://purl.uniprot.org/annotation/VAR_074895|||http://purl.uniprot.org/annotation/VAR_074896|||http://purl.uniprot.org/annotation/VAR_074897|||http://purl.uniprot.org/annotation/VAR_074898|||http://purl.uniprot.org/annotation/VAR_074899|||http://purl.uniprot.org/annotation/VAR_074900|||http://purl.uniprot.org/annotation/VAR_074901|||http://purl.uniprot.org/annotation/VAR_074902|||http://purl.uniprot.org/annotation/VAR_074903|||http://purl.uniprot.org/annotation/VAR_074904|||http://purl.uniprot.org/annotation/VAR_074905|||http://purl.uniprot.org/annotation/VAR_074906|||http://purl.uniprot.org/annotation/VAR_074907|||http://purl.uniprot.org/annotation/VAR_077953|||http://purl.uniprot.org/annotation/VSP_000965|||http://purl.uniprot.org/annotation/VSP_000966|||http://purl.uniprot.org/annotation/VSP_047877|||http://purl.uniprot.org/annotation/VSP_047878|||http://purl.uniprot.org/annotation/VSP_047879|||http://purl.uniprot.org/annotation/VSP_047880|||http://purl.uniprot.org/annotation/VSP_047881
http://togogenome.org/gene/9606:SLC25A47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6Q0C1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Repeat|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Impaired NAD(+) uptake.|||In isoform 2.|||Solcar 1|||Solcar 2|||Solcar 3|||Solute carrier family 25 member 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291779|||http://purl.uniprot.org/annotation/VSP_026233|||http://purl.uniprot.org/annotation/VSP_026234
http://togogenome.org/gene/9606:MDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NU22                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  AAA-ATPase protomer 1|||AAA-ATPase protomer 2|||AAA-ATPase protomer 3|||AAA-ATPase protomer 4|||AAA-ATPase protomer 5|||AAA-ATPase protomer 6|||Acidic residues|||Basic and acidic residues|||Disordered|||Linker|||Midasin|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096336|||http://purl.uniprot.org/annotation/VAR_024234|||http://purl.uniprot.org/annotation/VAR_024235|||http://purl.uniprot.org/annotation/VAR_024236|||http://purl.uniprot.org/annotation/VAR_051171|||http://purl.uniprot.org/annotation/VAR_051172|||http://purl.uniprot.org/annotation/VAR_051173|||http://purl.uniprot.org/annotation/VAR_051174|||http://purl.uniprot.org/annotation/VAR_051175|||http://purl.uniprot.org/annotation/VAR_051176|||http://purl.uniprot.org/annotation/VAR_051177|||http://purl.uniprot.org/annotation/VAR_051178|||http://purl.uniprot.org/annotation/VAR_051179|||http://purl.uniprot.org/annotation/VAR_051180|||http://purl.uniprot.org/annotation/VAR_051181|||http://purl.uniprot.org/annotation/VAR_051182
http://togogenome.org/gene/9606:CELF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N6W0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CUGBP Elav-like family member 5|||Disordered|||In isoform 2.|||Polar residues|||RRM 1|||RRM 2|||RRM 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295227|||http://purl.uniprot.org/annotation/VAR_033264|||http://purl.uniprot.org/annotation/VSP_026844|||http://purl.uniprot.org/annotation/VSP_026845|||http://purl.uniprot.org/annotation/VSP_026846
http://togogenome.org/gene/9606:TMEM114                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LNY9|||http://purl.uniprot.org/uniprot/B3SHH9|||http://purl.uniprot.org/uniprot/H3BM71                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 114                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000352759|||http://purl.uniprot.org/annotation/VAR_058707|||http://purl.uniprot.org/annotation/VAR_058708|||http://purl.uniprot.org/annotation/VAR_058709
http://togogenome.org/gene/9606:CCDC160                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGH7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 160|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345951
http://togogenome.org/gene/9606:RPS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62263                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Phosphothreonine|||Removed|||Small ribosomal subunit protein uS11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123337
http://togogenome.org/gene/9606:ABCB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21439                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Accumulates predominantly in intracellular compartments with only a small fraction at the plasma membrane and inhibits partially the efflux activity for PC.|||Cytoplasmic|||Does not inhibit efflux activity for PC.|||Extracellular|||Found in patients with cholangitis; unknown pathological significance.|||Found in patients with gallbladder and cholestasis; unknown pathological significance.|||Helical|||In GBD1.|||In GBD1; benign variant.|||In GBD1; loss of phosphatidylcholine transporter activity; does not alter plasma membrane location.|||In GBD1; partly retained intracellularly; reduces efflux activity for PC in a phosphorylation-dependent manner.|||In GBD1; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location.|||In GBD1; reduces efflux activity for PC in a phosphorylation-dependent manner.|||In GBD1; requires 2 nucleotide substitutions.|||In GBD1; severely reduced phosphatidylcholine transporter activity; does not alter plasma membrane location.|||In GBD1; unknown pathological significance; moderate decrease of phosphatidylcholine transporter activity; does not alter plasma membrane location.|||In ICP3, GBD1 and PFIC3; unknown pathological significance; does not alter plasma membrane location; does not inhibit efflux activity for PC.|||In ICP3.|||In ICP3; disruption of protein trafficking with subsequent lack of functional protein at the cell surface.|||In PFIC3 and GBD1.|||In PFIC3 and GBD1; does not alter plasma membrane location; inhibits efflux activity for PC.|||In PFIC3.|||In PFIC3; alters efflux activity for PC.|||In PFIC3; does not alter cytoplasmic and cell membrane location; inhibits efflux activity for PC and cholesterol.|||In PFIC3; greatly reduced expression; alters efflux activity for PC.|||In PFIC3; reduced phosphatidylcholine transporter activity; does not alter plasma membrane location.|||In PFIC3; retained in the reticulum endoplasmic; greatly reduced expression.|||In a heterozygous patient with amoxicillin/clavulanic acid-induced cholestasis.|||In a heterozygous patient with risperidone-induced cholestasis.|||In isoform 2 and isoform 3.|||In isoform 3.|||Inhibits efflux activity for PC and cholesterol, but does not alter glycosylation and surface expression in the presence of taurocholate.|||Interaction with HAX1|||Loss of floppase activity. Strongly reduce the ATPase activity.|||N-linked (GlcNAc...) asparagine|||Phosphatidylcholine translocator ABCB4|||Phosphoserine|||Phosphothreonine|||Reduces efflux activity for PC. Does not alter apical membrane location.|||Requires 2 nucleotide substitutions; found in patients with cholangitis; unknown pathological significance.|||Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and Q-989.|||Significantly reduces phosphatidylcholine floppase activity; when associated with M-985 and V-990.|||Significantly reduces phosphatidylcholine floppase activity; when associated with Q-989 and V-990.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093333|||http://purl.uniprot.org/annotation/VAR_020223|||http://purl.uniprot.org/annotation/VAR_020225|||http://purl.uniprot.org/annotation/VAR_023501|||http://purl.uniprot.org/annotation/VAR_023502|||http://purl.uniprot.org/annotation/VAR_023503|||http://purl.uniprot.org/annotation/VAR_023504|||http://purl.uniprot.org/annotation/VAR_024359|||http://purl.uniprot.org/annotation/VAR_030763|||http://purl.uniprot.org/annotation/VAR_030765|||http://purl.uniprot.org/annotation/VAR_043078|||http://purl.uniprot.org/annotation/VAR_043079|||http://purl.uniprot.org/annotation/VAR_043080|||http://purl.uniprot.org/annotation/VAR_043081|||http://purl.uniprot.org/annotation/VAR_043082|||http://purl.uniprot.org/annotation/VAR_043083|||http://purl.uniprot.org/annotation/VAR_043084|||http://purl.uniprot.org/annotation/VAR_043085|||http://purl.uniprot.org/annotation/VAR_043086|||http://purl.uniprot.org/annotation/VAR_043087|||http://purl.uniprot.org/annotation/VAR_043088|||http://purl.uniprot.org/annotation/VAR_043089|||http://purl.uniprot.org/annotation/VAR_043090|||http://purl.uniprot.org/annotation/VAR_043091|||http://purl.uniprot.org/annotation/VAR_043092|||http://purl.uniprot.org/annotation/VAR_043093|||http://purl.uniprot.org/annotation/VAR_043094|||http://purl.uniprot.org/annotation/VAR_043095|||http://purl.uniprot.org/annotation/VAR_043096|||http://purl.uniprot.org/annotation/VAR_043097|||http://purl.uniprot.org/annotation/VAR_043098|||http://purl.uniprot.org/annotation/VAR_043099|||http://purl.uniprot.org/annotation/VAR_043100|||http://purl.uniprot.org/annotation/VAR_043101|||http://purl.uniprot.org/annotation/VAR_043102|||http://purl.uniprot.org/annotation/VAR_043103|||http://purl.uniprot.org/annotation/VAR_043104|||http://purl.uniprot.org/annotation/VAR_043105|||http://purl.uniprot.org/annotation/VAR_073728|||http://purl.uniprot.org/annotation/VAR_073729|||http://purl.uniprot.org/annotation/VAR_073730|||http://purl.uniprot.org/annotation/VAR_073731|||http://purl.uniprot.org/annotation/VAR_073732|||http://purl.uniprot.org/annotation/VAR_073733|||http://purl.uniprot.org/annotation/VAR_073734|||http://purl.uniprot.org/annotation/VAR_073735|||http://purl.uniprot.org/annotation/VAR_073736|||http://purl.uniprot.org/annotation/VAR_073737|||http://purl.uniprot.org/annotation/VAR_073738|||http://purl.uniprot.org/annotation/VAR_073739|||http://purl.uniprot.org/annotation/VAR_073740|||http://purl.uniprot.org/annotation/VAR_073741|||http://purl.uniprot.org/annotation/VAR_073742|||http://purl.uniprot.org/annotation/VAR_073743|||http://purl.uniprot.org/annotation/VAR_073744|||http://purl.uniprot.org/annotation/VAR_073745|||http://purl.uniprot.org/annotation/VAR_073746|||http://purl.uniprot.org/annotation/VAR_073747|||http://purl.uniprot.org/annotation/VAR_073748|||http://purl.uniprot.org/annotation/VAR_073749|||http://purl.uniprot.org/annotation/VAR_073750|||http://purl.uniprot.org/annotation/VAR_073751|||http://purl.uniprot.org/annotation/VAR_073752|||http://purl.uniprot.org/annotation/VAR_073753|||http://purl.uniprot.org/annotation/VAR_073754|||http://purl.uniprot.org/annotation/VAR_073755|||http://purl.uniprot.org/annotation/VAR_073756|||http://purl.uniprot.org/annotation/VAR_073757|||http://purl.uniprot.org/annotation/VAR_073758|||http://purl.uniprot.org/annotation/VAR_073759|||http://purl.uniprot.org/annotation/VAR_073760|||http://purl.uniprot.org/annotation/VAR_073761|||http://purl.uniprot.org/annotation/VAR_073762|||http://purl.uniprot.org/annotation/VAR_073763|||http://purl.uniprot.org/annotation/VAR_073764|||http://purl.uniprot.org/annotation/VAR_073765|||http://purl.uniprot.org/annotation/VAR_073766|||http://purl.uniprot.org/annotation/VAR_073767|||http://purl.uniprot.org/annotation/VAR_073768|||http://purl.uniprot.org/annotation/VAR_073769|||http://purl.uniprot.org/annotation/VAR_073770|||http://purl.uniprot.org/annotation/VAR_073771|||http://purl.uniprot.org/annotation/VAR_073772|||http://purl.uniprot.org/annotation/VAR_073773|||http://purl.uniprot.org/annotation/VAR_073774|||http://purl.uniprot.org/annotation/VAR_073775|||http://purl.uniprot.org/annotation/VAR_073776|||http://purl.uniprot.org/annotation/VAR_073777|||http://purl.uniprot.org/annotation/VAR_079611|||http://purl.uniprot.org/annotation/VAR_079612|||http://purl.uniprot.org/annotation/VAR_079613|||http://purl.uniprot.org/annotation/VSP_023263|||http://purl.uniprot.org/annotation/VSP_046258
http://togogenome.org/gene/9606:OGG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5KPM5|||http://purl.uniprot.org/uniprot/E5KPM6|||http://purl.uniprot.org/uniprot/E5KPM7|||http://purl.uniprot.org/uniprot/E5KPM8|||http://purl.uniprot.org/uniprot/E5KPM9|||http://purl.uniprot.org/uniprot/E5KPN0|||http://purl.uniprot.org/uniprot/E5KPN1|||http://purl.uniprot.org/uniprot/O15527                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  8-oxoguanine DNA glycosylase N-terminal|||Basic and acidic residues|||Decreases activity about 65-fold.|||Disordered|||Found in a clear cell renal cell carcinoma sample; somatic mutation; diminished activity.|||Found in a gastric cancer sample; no effect on base-excision activity; alters substrate specificity and strongly increases mutagenic mis-repair.|||Found in a kidney cancer sample.|||Found in a kidney cancer sample; no effect on activity; abolishes mitochondrial localization.|||Found in a lung cancer sample.|||Found in a lung cancer sample; loss of activity.|||HhH-GPD|||In isoform 1B.|||In isoform 1C.|||In isoform 2A.|||In isoform 2B.|||In isoform 2C.|||In isoform 2D.|||In isoform 2E.|||Loss of activity.|||N-glycosylase/DNA lyase|||No effect on activity.|||Polar residues|||Schiff-base intermediate with DNA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058591|||http://purl.uniprot.org/annotation/VAR_009519|||http://purl.uniprot.org/annotation/VAR_009520|||http://purl.uniprot.org/annotation/VAR_009521|||http://purl.uniprot.org/annotation/VAR_014487|||http://purl.uniprot.org/annotation/VAR_014488|||http://purl.uniprot.org/annotation/VAR_018890|||http://purl.uniprot.org/annotation/VAR_018891|||http://purl.uniprot.org/annotation/VAR_024831|||http://purl.uniprot.org/annotation/VAR_024832|||http://purl.uniprot.org/annotation/VAR_024833|||http://purl.uniprot.org/annotation/VAR_024834|||http://purl.uniprot.org/annotation/VSP_003746|||http://purl.uniprot.org/annotation/VSP_003747|||http://purl.uniprot.org/annotation/VSP_003748|||http://purl.uniprot.org/annotation/VSP_003749|||http://purl.uniprot.org/annotation/VSP_003750|||http://purl.uniprot.org/annotation/VSP_003751|||http://purl.uniprot.org/annotation/VSP_003752|||http://purl.uniprot.org/annotation/VSP_003753
http://togogenome.org/gene/9606:ANKS1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1VKB5|||http://purl.uniprot.org/uniprot/B7Z9I9|||http://purl.uniprot.org/uniprot/Q6V0K8|||http://purl.uniprot.org/uniprot/Q7Z6G8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Ankyrin repeat and sterile alpha motif domain-containing protein 1B|||Basic and acidic residues|||Disordered|||In isoform 10.|||In isoform 2, isoform 6, isoform 7 and isoform 10.|||In isoform 3, isoform 4, isoform 5, isoform 2 and isoform 7.|||In isoform 3, isoform 5 and isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 8 and isoform 10.|||In isoform 8.|||In isoform 9.|||Nuclear localization signal|||PID|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||SAM 1|||SAM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327259|||http://purl.uniprot.org/annotation/VSP_032701|||http://purl.uniprot.org/annotation/VSP_032702|||http://purl.uniprot.org/annotation/VSP_032703|||http://purl.uniprot.org/annotation/VSP_032704|||http://purl.uniprot.org/annotation/VSP_032705|||http://purl.uniprot.org/annotation/VSP_032706|||http://purl.uniprot.org/annotation/VSP_032707|||http://purl.uniprot.org/annotation/VSP_032708|||http://purl.uniprot.org/annotation/VSP_032709|||http://purl.uniprot.org/annotation/VSP_032710|||http://purl.uniprot.org/annotation/VSP_032711|||http://purl.uniprot.org/annotation/VSP_032712|||http://purl.uniprot.org/annotation/VSP_046414|||http://purl.uniprot.org/annotation/VSP_046415
http://togogenome.org/gene/9606:MYH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y623                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||IQ|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-4|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Pros-methylhistidine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123398|||http://purl.uniprot.org/annotation/VAR_022110|||http://purl.uniprot.org/annotation/VAR_024542|||http://purl.uniprot.org/annotation/VAR_030198|||http://purl.uniprot.org/annotation/VAR_030199|||http://purl.uniprot.org/annotation/VAR_030200|||http://purl.uniprot.org/annotation/VAR_030201|||http://purl.uniprot.org/annotation/VAR_030202|||http://purl.uniprot.org/annotation/VAR_056175
http://togogenome.org/gene/9606:ZNF19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17023                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 19                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047343|||http://purl.uniprot.org/annotation/VAR_054792|||http://purl.uniprot.org/annotation/VAR_054793|||http://purl.uniprot.org/annotation/VSP_036733
http://togogenome.org/gene/9606:PARVB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WZB5|||http://purl.uniprot.org/uniprot/Q9HBI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ILK. Abolishes location at focal adhesion sites.|||Abolishes interaction with PXN.|||Basic and acidic residues|||Beta-parvin|||Calponin-homology (CH)|||Calponin-homology (CH) 1|||Calponin-homology (CH) 2|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121583|||http://purl.uniprot.org/annotation/VAR_017242|||http://purl.uniprot.org/annotation/VAR_034369|||http://purl.uniprot.org/annotation/VSP_041336|||http://purl.uniprot.org/annotation/VSP_045555
http://togogenome.org/gene/9606:STAC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR96|||http://purl.uniprot.org/uniprot/B4DZ13|||http://purl.uniprot.org/uniprot/E9PEA7|||http://purl.uniprot.org/uniprot/Q8WUK8|||http://purl.uniprot.org/uniprot/Q99469                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Phorbol-ester/DAG-type|||Polar residues|||SH3|||SH3 1|||SH3 2|||SH3 and cysteine-rich domain-containing protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072235|||http://purl.uniprot.org/annotation/VAR_034505
http://togogenome.org/gene/9606:CSMD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z407                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 10|||CUB 11|||CUB 12|||CUB 13|||CUB 14|||CUB 2|||CUB 3|||CUB 4|||CUB 5|||CUB 6|||CUB 7|||CUB 8|||CUB 9|||CUB and sushi domain-containing protein 3|||Cytoplasmic|||Disordered|||Extracellular|||Found in a renal cell carcinoma case; somatic mutation.|||Helical|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sushi 1|||Sushi 10|||Sushi 11|||Sushi 12|||Sushi 13|||Sushi 14|||Sushi 15|||Sushi 16|||Sushi 17|||Sushi 18|||Sushi 19|||Sushi 2|||Sushi 20|||Sushi 21|||Sushi 22|||Sushi 23|||Sushi 24|||Sushi 25|||Sushi 26|||Sushi 27|||Sushi 28|||Sushi 3|||Sushi 4|||Sushi 5|||Sushi 6|||Sushi 7|||Sushi 8|||Sushi 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021027|||http://purl.uniprot.org/annotation/VAR_017404|||http://purl.uniprot.org/annotation/VAR_017405|||http://purl.uniprot.org/annotation/VAR_017406|||http://purl.uniprot.org/annotation/VAR_035688|||http://purl.uniprot.org/annotation/VAR_035689|||http://purl.uniprot.org/annotation/VAR_035690|||http://purl.uniprot.org/annotation/VAR_064703|||http://purl.uniprot.org/annotation/VSP_009047|||http://purl.uniprot.org/annotation/VSP_009048|||http://purl.uniprot.org/annotation/VSP_009049|||http://purl.uniprot.org/annotation/VSP_009050|||http://purl.uniprot.org/annotation/VSP_009051|||http://purl.uniprot.org/annotation/VSP_009052
http://togogenome.org/gene/9606:UBASH3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF42                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Phosphoserine|||Phosphothreonine|||Protein tyrosine phosphatase|||SH3|||Tele-phosphohistidine intermediate|||UBA|||Ubiquitin-associated and SH3 domain-containing protein B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000245508|||http://purl.uniprot.org/annotation/VAR_052676|||http://purl.uniprot.org/annotation/VAR_061923
http://togogenome.org/gene/9606:AREG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15514                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amphiregulin|||Basic residues|||Disordered|||EGF-like|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007473|||http://purl.uniprot.org/annotation/PRO_0000007474|||http://purl.uniprot.org/annotation/PRO_0000007475|||http://purl.uniprot.org/annotation/VAR_018918|||http://purl.uniprot.org/annotation/VAR_018919
http://togogenome.org/gene/9606:LHX9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ69                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM/homeobox protein Lhx9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075798|||http://purl.uniprot.org/annotation/VSP_036428|||http://purl.uniprot.org/annotation/VSP_036429
http://togogenome.org/gene/9606:LRRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K6Q2|||http://purl.uniprot.org/uniprot/Q6UXK5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||Ig-like|||Ig-like C2-type|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat neuronal protein 1|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014847|||http://purl.uniprot.org/annotation/PRO_5002724668|||http://purl.uniprot.org/annotation/VAR_049896|||http://purl.uniprot.org/annotation/VAR_049897
http://togogenome.org/gene/9606:GDF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0J1|||http://purl.uniprot.org/uniprot/P43026                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Growth/differentiation factor 5|||In AMD2A.|||In AMD2B, SYNS2 and BDA2; the mutant is almost inactive; loss of binding to BMPR1A and BMPR1B ectodomains; no induction of SMAD1-SMAD5-SMAD8 protein complex phosphorylation; impairs nuclear translocation of phosphotylated SMAD1-SMAD5-SMAD8 protein complex; no ability to induce SMAD protein signal transduction; binds to NOG.|||In AMD2B.|||In AMD2B; located on the same allele as L-437 del and L-440.|||In AMD2B; located on the same allele as L-437 del and T-439.|||In AMD2B; located on the same allele as T-439 and L-440.|||In BDA1C; less effective than wild-type in stimulating chondrogenesis; impairs BMP signaling through BMPR1A.|||In BDA2; reduces activity; impairs processing.|||In BDC.|||In BDC; decrease of induction of SMAD protein signal transduction with either BMPR1A or BMPR1B; less induction of chondrgenesis; no phosphorylation of SMAD1-SMAD5-SMAD8 protein complex; reduction of protein level; abnormal proteolysis product.|||In BDC; no induction of SMAD protein signal transduction via BMPR1A; less induction of chondrgenesis; no phosphorylation of SMAD1-SMAD5-SMAD8 protein complex; reduction of protein level; abnormal proteolysis product.|||In SYM1B.|||In SYM1B; the mature GDF5 protein is detected as the wild-type in the supernatant derived from the mutant transfected cells.|||In SYNS2 and BDA1C; reduced interaction with NOG; reduces affinity to BMPR1A; impairs BMP signaling through BMPR1A; impairs chondrogenesis.|||In SYNS2 and SYM1B; increased biological activity when compared to wild-type; normal binding to BMPR1B ectodomain but increased binding to that of BMPR1A.|||In SYNS2.|||In SYNS2; reduction in binding affinity with BMPR2; no change in binding affinity with BMPR1A; no change in binding affinity with BMPR1B; decreases induction of SMAD1-SMAD5-SMAD8 protein complex phosphorylation; delay of phosphotylated SMAD1-SMAD5-SMAD8 protein complex nuclear translocation; strong reduction of SMAD protein signal transduction; reduction of chondrocyte differentiation; strong improvement of chondrogenesis; decrease of NOG binding; resistant to NOG inhibition; no chondrogenesis inhibition.|||In SYNS2; resistant to NOG inhibition; no change in binding with MPR1A and BMPR1B; strong induction of chondrogenesis.|||Interchain|||N-linked (GlcNAc...) asparagine|||Resitant to NOG inhibition.|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033912|||http://purl.uniprot.org/annotation/PRO_0000033913|||http://purl.uniprot.org/annotation/PRO_5003275837|||http://purl.uniprot.org/annotation/VAR_017407|||http://purl.uniprot.org/annotation/VAR_017408|||http://purl.uniprot.org/annotation/VAR_026120|||http://purl.uniprot.org/annotation/VAR_026545|||http://purl.uniprot.org/annotation/VAR_037977|||http://purl.uniprot.org/annotation/VAR_037978|||http://purl.uniprot.org/annotation/VAR_037979|||http://purl.uniprot.org/annotation/VAR_037980|||http://purl.uniprot.org/annotation/VAR_037981|||http://purl.uniprot.org/annotation/VAR_037982|||http://purl.uniprot.org/annotation/VAR_037983|||http://purl.uniprot.org/annotation/VAR_046743|||http://purl.uniprot.org/annotation/VAR_054909|||http://purl.uniprot.org/annotation/VAR_054910|||http://purl.uniprot.org/annotation/VAR_054911|||http://purl.uniprot.org/annotation/VAR_064416|||http://purl.uniprot.org/annotation/VAR_073139|||http://purl.uniprot.org/annotation/VAR_073140|||http://purl.uniprot.org/annotation/VAR_073141|||http://purl.uniprot.org/annotation/VAR_073142|||http://purl.uniprot.org/annotation/VAR_073143|||http://purl.uniprot.org/annotation/VAR_074161|||http://purl.uniprot.org/annotation/VAR_074162
http://togogenome.org/gene/9606:PTTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZH5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  D-box|||Disordered|||In isoform 2.|||Polar residues|||SH3-binding|||Securin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319106|||http://purl.uniprot.org/annotation/VAR_038956|||http://purl.uniprot.org/annotation/VSP_031444
http://togogenome.org/gene/9606:PTPRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16849|||http://purl.uniprot.org/uniprot/Q96IA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||ICA512-N-terminal fragment|||ICA512-cleaved cytosolic fragment|||ICA512-transmembrane fragment|||Impairs normal processing and leads to retention in the endoplasmic reticulum and degradation.|||In isoform 2.|||In isoform 3.|||Interchain (with C-40 or C-47); in multimeric form|||Lumenal|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine|||Polar residues|||RESP18 homology domain|||Receptor-type tyrosine-protein phosphatase-like N|||Reduces N-glycosylation.|||Sufficient for dimerization of proICA512|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025451|||http://purl.uniprot.org/annotation/PRO_0000438079|||http://purl.uniprot.org/annotation/PRO_0000438080|||http://purl.uniprot.org/annotation/PRO_0000438081|||http://purl.uniprot.org/annotation/VAR_051762|||http://purl.uniprot.org/annotation/VSP_043654|||http://purl.uniprot.org/annotation/VSP_045867
http://togogenome.org/gene/9606:ADCY2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08462|||http://purl.uniprot.org/uniprot/Q71UM8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adenylate cyclase type 2|||Cytoplasmic|||Guanylate cyclase|||Helical|||In isoform 2.|||Interaction with GNAS|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195684|||http://purl.uniprot.org/annotation/VAR_029012|||http://purl.uniprot.org/annotation/VAR_048247|||http://purl.uniprot.org/annotation/VSP_055811|||http://purl.uniprot.org/annotation/VSP_055812
http://togogenome.org/gene/9606:TMPRSS11F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWK6                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||Peptidase S1|||SEA|||Transmembrane protease serine 11F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299322|||http://purl.uniprot.org/annotation/VAR_034800|||http://purl.uniprot.org/annotation/VAR_046636
http://togogenome.org/gene/9606:STAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  190 kDa form stabilin-2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 10|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 16|||EGF-like 17|||EGF-like 2|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Extracellular|||FAS1 1|||FAS1 2|||FAS1 3|||FAS1 4|||FAS1 5|||FAS1 6|||FAS1 7|||Helical|||Interaction with TMSB4X|||Laminin EGF-like 1|||Laminin EGF-like 2|||Link|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Stabilin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007712|||http://purl.uniprot.org/annotation/PRO_0000007713|||http://purl.uniprot.org/annotation/VAR_019541|||http://purl.uniprot.org/annotation/VAR_048995|||http://purl.uniprot.org/annotation/VAR_048996|||http://purl.uniprot.org/annotation/VAR_048997|||http://purl.uniprot.org/annotation/VAR_048998|||http://purl.uniprot.org/annotation/VAR_048999|||http://purl.uniprot.org/annotation/VAR_049000|||http://purl.uniprot.org/annotation/VAR_049001|||http://purl.uniprot.org/annotation/VAR_049002
http://togogenome.org/gene/9606:CISD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5K1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Mutagenesis Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  CDGSH iron-sulfur domain-containing protein 2|||Cytoplasmic|||Has the same optical signature of the native protein and improves yields of purified protein and a decreased tendency to aggregate.|||Helical|||Impairs interaction with BCL2; when associated with S-101; S-110 and Q-114.|||Impairs interaction with BCL2; when associated with S-99; S-101 and Q-114.|||Impairs interaction with BCL2; when associated with S-99; S-101 and S-110.|||Impairs interaction with BCL2; when associated with S-99; S-110 and Q-114.|||Lumenal|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316005
http://togogenome.org/gene/9606:TMEM126B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUX1                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Complex I assembly factor TMEM126B, mitochondrial|||Helical|||In MC1DN29; decreased function in complex I assembly.|||In MC1DN29; loss of function in complex I assembly.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280716|||http://purl.uniprot.org/annotation/VAR_031188|||http://purl.uniprot.org/annotation/VAR_081464|||http://purl.uniprot.org/annotation/VAR_081465|||http://purl.uniprot.org/annotation/VSP_023870|||http://purl.uniprot.org/annotation/VSP_023871|||http://purl.uniprot.org/annotation/VSP_023872|||http://purl.uniprot.org/annotation/VSP_023873|||http://purl.uniprot.org/annotation/VSP_023874|||http://purl.uniprot.org/annotation/VSP_023875
http://togogenome.org/gene/9606:MSH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20585                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||DNA mismatch repair protein Msh3|||Disordered|||Interaction with EXO1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000115192|||http://purl.uniprot.org/annotation/VAR_016160|||http://purl.uniprot.org/annotation/VAR_016161|||http://purl.uniprot.org/annotation/VAR_016162|||http://purl.uniprot.org/annotation/VAR_016163|||http://purl.uniprot.org/annotation/VAR_020934|||http://purl.uniprot.org/annotation/VAR_020935|||http://purl.uniprot.org/annotation/VAR_020936|||http://purl.uniprot.org/annotation/VAR_055251
http://togogenome.org/gene/9606:ATP5IF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UII2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  ATPase inhibitor, mitochondrial|||Antiparallel alpha-helical coiled coil region|||Disordered|||In isoform 2.|||In isoform 3.|||Mitochondrion|||N-terminal inhibitory region|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002547|||http://purl.uniprot.org/annotation/VSP_041417|||http://purl.uniprot.org/annotation/VSP_041418
http://togogenome.org/gene/9606:RPS23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K517|||http://purl.uniprot.org/uniprot/P62266                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  3-hydroxyproline|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into polysomes; patient cells become highly sensitive to oxidative stress.|||In BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into ribosomes and polysomes; patient cells become highly sensitive to oxidative stress.|||N6-acetyllysine|||N6-succinyllysine|||Removed|||Small ribosomal subunit protein uS12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146457|||http://purl.uniprot.org/annotation/VAR_079133|||http://purl.uniprot.org/annotation/VAR_079134
http://togogenome.org/gene/9606:ST6GALNAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSC7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Found in patients with Inflammatory bowel disease; unknown pathological significance; does dot affect protein sialyltransferase activity.|||Found in patients with Inflammatory bowel disease; unknown pathological significance; reduced protein sialyltransferase activity.|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polar residues|||Probable disease-associated variant found in patients with Inflammatory bowel disease; impaired localization to the Golgi apparatus; abolished protein sialyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000149269|||http://purl.uniprot.org/annotation/VAR_021514|||http://purl.uniprot.org/annotation/VAR_049226|||http://purl.uniprot.org/annotation/VAR_086492|||http://purl.uniprot.org/annotation/VAR_086493|||http://purl.uniprot.org/annotation/VAR_086494|||http://purl.uniprot.org/annotation/VAR_086495
http://togogenome.org/gene/9606:LYG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86SG7                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Lysozyme g-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012025|||http://purl.uniprot.org/annotation/VSP_056329
http://togogenome.org/gene/9606:AMMECR1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6DCA0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  AMMECR1|||AMMECR1-like protein|||Disordered|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278479
http://togogenome.org/gene/9606:GZMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12544                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protease activity.|||Activation peptide|||Charge relay system|||Granzyme A|||In isoform beta.|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027393|||http://purl.uniprot.org/annotation/PRO_0000027394|||http://purl.uniprot.org/annotation/VAR_024291|||http://purl.uniprot.org/annotation/VSP_038571|||http://purl.uniprot.org/annotation/VSP_038572
http://togogenome.org/gene/9606:ZNF791                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3KP31                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 791                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311799|||http://purl.uniprot.org/annotation/VSP_056674
http://togogenome.org/gene/9606:DAPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNB3|||http://purl.uniprot.org/uniprot/Q9UN19                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Dual adapter for phosphotyrosine and 3-phosphotyrosine and 3-phosphoinositide|||In isoform 2.|||No change in BCR-induced NFAT activation.|||No interaction with 3-phosphoinositides.|||No membrane association.|||PH|||Phosphoserine|||Phosphotyrosine|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079785|||http://purl.uniprot.org/annotation/VSP_010699
http://togogenome.org/gene/9606:OR5D18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGL1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5D18                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150594|||http://purl.uniprot.org/annotation/VAR_034224|||http://purl.uniprot.org/annotation/VAR_048046|||http://purl.uniprot.org/annotation/VAR_048047|||http://purl.uniprot.org/annotation/VAR_062042
http://togogenome.org/gene/9606:FOXRED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWF2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||FAD-dependent oxidoreductase domain-containing protein 2|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337692|||http://purl.uniprot.org/annotation/VAR_043704|||http://purl.uniprot.org/annotation/VAR_043705|||http://purl.uniprot.org/annotation/VAR_043706|||http://purl.uniprot.org/annotation/VAR_043707|||http://purl.uniprot.org/annotation/VAR_062247|||http://purl.uniprot.org/annotation/VSP_033997
http://togogenome.org/gene/9606:PRR13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ81                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform 2.|||Pro residues|||Proline-rich protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243946|||http://purl.uniprot.org/annotation/VSP_024394
http://togogenome.org/gene/9606:PCDHA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN72                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  5 X 4 AA repeats of P-X-X-P|||Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PXXP 1|||PXXP 2|||PXXP 3|||PXXP 4|||PXXP 5|||Polar residues|||Protocadherin alpha-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003896|||http://purl.uniprot.org/annotation/VAR_048527|||http://purl.uniprot.org/annotation/VAR_048528|||http://purl.uniprot.org/annotation/VSP_000684|||http://purl.uniprot.org/annotation/VSP_000685
http://togogenome.org/gene/9606:IMPACT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2X3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Protein IMPACT|||RWD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000330850|||http://purl.uniprot.org/annotation/VAR_042723|||http://purl.uniprot.org/annotation/VAR_042724|||http://purl.uniprot.org/annotation/VAR_077844|||http://purl.uniprot.org/annotation/VSP_033136
http://togogenome.org/gene/9606:VIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01282                                                                                  ^@                                                                                  Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Helix|||Modified Residue|||Peptide|||Propeptide|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Asparagine amide|||In isoform 2.|||Intestinal peptide PHM-27|||Intestinal peptide PHV-42|||Methionine amide|||Phosphoserine|||Vasoactive intestinal peptide                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011457|||http://purl.uniprot.org/annotation/PRO_0000011458|||http://purl.uniprot.org/annotation/PRO_0000011459|||http://purl.uniprot.org/annotation/PRO_0000011460|||http://purl.uniprot.org/annotation/PRO_0000011461|||http://purl.uniprot.org/annotation/VSP_023256
http://togogenome.org/gene/9606:ATP5MF-PTCD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ38|||http://purl.uniprot.org/uniprot/G3V325                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region|||Repeat                                                                                  ^@                                                                                  Disordered|||PPR|||Pentacotripeptide-repeat region of PRORP|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:SMARCA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60264                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Abolishes ATP hydrolysis. Binds to chromatin itself, but abolishes the chromatin binding of the cohesin complex component RAD21.|||Basic and acidic residues|||DEAH box|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Removed|||SANT 1|||SANT 2|||SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074354
http://togogenome.org/gene/9606:PLAU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DNJ4|||http://purl.uniprot.org/uniprot/P00749|||http://purl.uniprot.org/uniprot/Q59GZ8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158.|||Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323.|||Binds urokinase plasminogen activator surface receptor|||Charge relay system|||Cleavage; during zymogen activation|||Connecting peptide|||EGF-like|||In isoform 2.|||Interchain (between A and B chains)|||Kringle|||N-linked (GlcNAc...) asparagine|||O-linked (Fuc) threonine|||Peptidase S1|||Phosphoserine|||Urokinase-type plasminogen activator|||Urokinase-type plasminogen activator chain B|||Urokinase-type plasminogen activator long chain A|||Urokinase-type plasminogen activator short chain A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000026|||http://purl.uniprot.org/annotation/PRO_0000028318|||http://purl.uniprot.org/annotation/PRO_0000028319|||http://purl.uniprot.org/annotation/PRO_0000028320|||http://purl.uniprot.org/annotation/PRO_0000028321|||http://purl.uniprot.org/annotation/VAR_006722|||http://purl.uniprot.org/annotation/VAR_013102|||http://purl.uniprot.org/annotation/VAR_038730|||http://purl.uniprot.org/annotation/VAR_038731|||http://purl.uniprot.org/annotation/VSP_038368
http://togogenome.org/gene/9606:STYK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6J9G0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In a glioblastoma multiforme sample; somatic mutation.|||Protein kinase|||Proton acceptor|||Tyrosine-protein kinase STYK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088163|||http://purl.uniprot.org/annotation/VAR_022245|||http://purl.uniprot.org/annotation/VAR_030766|||http://purl.uniprot.org/annotation/VAR_041841|||http://purl.uniprot.org/annotation/VAR_041842|||http://purl.uniprot.org/annotation/VAR_041843|||http://purl.uniprot.org/annotation/VAR_041844|||http://purl.uniprot.org/annotation/VAR_041845
http://togogenome.org/gene/9606:ZFAND2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0D9|||http://purl.uniprot.org/uniprot/Q8WV99                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  AN1-type|||AN1-type 1|||AN1-type 2|||AN1-type zinc finger protein 2B|||CAAX motif|||Cysteine methyl ester|||Disordered|||In isoform 2.|||Phosphoserine|||Removed in mature form|||S-geranylgeranyl cysteine|||UIM 1|||UIM 2|||VCP/p97-interacting motif (VIM)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232876|||http://purl.uniprot.org/annotation/PRO_0000444335|||http://purl.uniprot.org/annotation/VSP_018001
http://togogenome.org/gene/9606:FPGT-TNNI3K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59H18|||http://purl.uniprot.org/uniprot/V9GXZ4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 10|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Disordered|||In CCDD; the mutation results in decreased protein solubility; causes abnormal aggregation; markedly reduced protein expression is observed in the sarcoplasm and nuclei of patient cardiomyocytes.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In a head & Neck squamous cell carcinoma sample; somatic mutation.|||In isoform 1, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of autophosphorylation activity.|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase TNNI3K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086757|||http://purl.uniprot.org/annotation/VAR_035639|||http://purl.uniprot.org/annotation/VAR_038821|||http://purl.uniprot.org/annotation/VAR_038822|||http://purl.uniprot.org/annotation/VAR_041223|||http://purl.uniprot.org/annotation/VAR_041224|||http://purl.uniprot.org/annotation/VAR_041225|||http://purl.uniprot.org/annotation/VAR_041226|||http://purl.uniprot.org/annotation/VAR_041227|||http://purl.uniprot.org/annotation/VAR_041228|||http://purl.uniprot.org/annotation/VAR_041229|||http://purl.uniprot.org/annotation/VAR_041230|||http://purl.uniprot.org/annotation/VAR_072650|||http://purl.uniprot.org/annotation/VSP_039403|||http://purl.uniprot.org/annotation/VSP_051882|||http://purl.uniprot.org/annotation/VSP_051883|||http://purl.uniprot.org/annotation/VSP_051884|||http://purl.uniprot.org/annotation/VSP_051885
http://togogenome.org/gene/9606:EMC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43402|||http://purl.uniprot.org/uniprot/Q53Y03                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ER membrane protein complex subunit 8|||In isoform 2.|||MPN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221187|||http://purl.uniprot.org/annotation/VSP_045089
http://togogenome.org/gene/9606:ZNF578                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MI94|||http://purl.uniprot.org/uniprot/Q96N58                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 578                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047668|||http://purl.uniprot.org/annotation/VAR_069167
http://togogenome.org/gene/9606:CAPS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYV7|||http://purl.uniprot.org/uniprot/Q13938|||http://purl.uniprot.org/uniprot/Q96ET4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calcyphosin|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Phosphoserine; by PKA|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073538|||http://purl.uniprot.org/annotation/VAR_048638|||http://purl.uniprot.org/annotation/VAR_080772|||http://purl.uniprot.org/annotation/VSP_055154|||http://purl.uniprot.org/annotation/VSP_059695
http://togogenome.org/gene/9606:TACC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWP4|||http://purl.uniprot.org/uniprot/B7ZMJ9|||http://purl.uniprot.org/uniprot/D6RAA5|||http://purl.uniprot.org/uniprot/O95359|||http://purl.uniprot.org/uniprot/Q4VXL4|||http://purl.uniprot.org/uniprot/Q4VXL8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 1 and isoform 6.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SPAZ|||Transforming acidic coiled-coil-containing protein 2|||Transforming acidic coiled-coil-containing protein C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179988|||http://purl.uniprot.org/annotation/VAR_020478|||http://purl.uniprot.org/annotation/VAR_020479|||http://purl.uniprot.org/annotation/VAR_020480|||http://purl.uniprot.org/annotation/VAR_020481|||http://purl.uniprot.org/annotation/VAR_020482|||http://purl.uniprot.org/annotation/VAR_029803|||http://purl.uniprot.org/annotation/VAR_029804|||http://purl.uniprot.org/annotation/VAR_029805|||http://purl.uniprot.org/annotation/VAR_036381|||http://purl.uniprot.org/annotation/VAR_036382|||http://purl.uniprot.org/annotation/VAR_053706|||http://purl.uniprot.org/annotation/VAR_053707|||http://purl.uniprot.org/annotation/VAR_053708|||http://purl.uniprot.org/annotation/VAR_053709|||http://purl.uniprot.org/annotation/VAR_053710|||http://purl.uniprot.org/annotation/VAR_053711|||http://purl.uniprot.org/annotation/VAR_053712|||http://purl.uniprot.org/annotation/VAR_053713|||http://purl.uniprot.org/annotation/VSP_006368|||http://purl.uniprot.org/annotation/VSP_006369|||http://purl.uniprot.org/annotation/VSP_022151|||http://purl.uniprot.org/annotation/VSP_022153|||http://purl.uniprot.org/annotation/VSP_022154|||http://purl.uniprot.org/annotation/VSP_022155|||http://purl.uniprot.org/annotation/VSP_022156|||http://purl.uniprot.org/annotation/VSP_022158
http://togogenome.org/gene/9606:DAGLA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y4D2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Charge relay system|||Cytoplasmic|||Diacylglycerol lipase-alpha|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphomimetic mutation; decreased the Vmax of 2-AG production without affecting the KM; when associated with E-782.|||Phosphomimetic mutation; decreased the Vmax of 2-AG production without affecting the KM; when associated with E-808.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Reduces phosphorylation by CAMK2A. Abolishes phosphorylation by CAMK2A; when associated with A-782.|||Slightly reduces phosphorylation by CAMK2A. Abolishes phosphorylation by CAMK2A; when associated with A-808.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248347|||http://purl.uniprot.org/annotation/VAR_027274|||http://purl.uniprot.org/annotation/VAR_049822|||http://purl.uniprot.org/annotation/VAR_049823
http://togogenome.org/gene/9606:OPTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96CV9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes colocalization with cytosolic Salmonella.|||Abolishes interaction with MAP1LC3A and GABARAPL1, no effect on binding to linear ubiquitin.|||Basic and acidic residues|||CCHC NOA-type|||Disordered|||In ALS12.|||In ALS12; no effect on Golgi subcellular location; no effect on protein expression level; increased Golgi fragmentation; decreased Golgi ribbon formation; increased susceptibility to endoplasmic reticulum (ER) stress.|||In GLC1E.|||In GLC1E; juvenile onset.|||In GLC1E; selectively promotes cell death of retinal ganglion cells probably by inducing TBC1D17-mediated inhibition of autophagy; affects Rab8-mediated endocytic trafficking; no effect on interaction with TBC1D17; increases colocalization with TBC1D17 and Rab8; increases interaction with TFRC and impairs its endocytic recycling; increases interactions with TBK1; decreases self-association; disturbs transition from the ER to Golgi; no effect on ubiquitin-binding; increases interaction with RAB8A as shown by immunoprecipitation in transfected HeLa cells, although other assays in yeast and mice show loss of direct interaction, it has been proposed that the variant might abolish direct interaction with Rab8 and enhance indirect interaction, hence altering the functional positioning of the molecules in the complex in such a way that it leads to constitutive or increased inactivation of Rab8 by TBC1D17.|||In GLC1E; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Increases interaction with MAP1LC3B.|||Interaction with HD|||Interaction with MYO6|||Interaction with Rab8|||LIR|||May modify intraocular pressure and increase risk of GLC1E and NPG; induces TFRC degradation leading to autophagic death in retinal ganglion cells.|||No effect on retinal ganglion cell death, decreased interaction with TFRC, loss of localization to recycling endosomes, loss of ubiquitin-binding; when associated with N-474.|||No effect on retinal ganglion cell death, drastically decreased interaction with TFRC, loss of localization to recycling endosomes, loss of ubiquitin-binding; when associated with K-50.|||Optineurin|||Phosphoserine|||Phosphoserine; by TBK1|||Polar residues|||Requires 2 nucleotide substitutions.|||Significant reduction in ubiquitin binding, decreased interaction with TBK1, loss of localization to recycling endosomes, disruption of interaction with TFRC, loss of inhibition of IFNB activation in response to TLR3 or RIG-I signaling, no effect on retinal ganglion cell death.|||UBAN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058066|||http://purl.uniprot.org/annotation/VAR_021537|||http://purl.uniprot.org/annotation/VAR_021538|||http://purl.uniprot.org/annotation/VAR_021539|||http://purl.uniprot.org/annotation/VAR_021540|||http://purl.uniprot.org/annotation/VAR_021541|||http://purl.uniprot.org/annotation/VAR_021542|||http://purl.uniprot.org/annotation/VAR_021543|||http://purl.uniprot.org/annotation/VAR_021544|||http://purl.uniprot.org/annotation/VAR_021545|||http://purl.uniprot.org/annotation/VAR_021546|||http://purl.uniprot.org/annotation/VAR_021547|||http://purl.uniprot.org/annotation/VAR_030769|||http://purl.uniprot.org/annotation/VAR_063597|||http://purl.uniprot.org/annotation/VAR_078108|||http://purl.uniprot.org/annotation/VSP_013261|||http://purl.uniprot.org/annotation/VSP_013262
http://togogenome.org/gene/9606:CNOT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKZ1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  CCR4-NOT transcription complex subunit 11|||Disordered|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089357
http://togogenome.org/gene/9606:NCKIPSD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZQ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Breakpoint for translocation to form KMT2A/MLL1-AF3P21 oncogene|||Disordered|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||In isoform 5.|||NCK-interacting protein with SH3 domain|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072130|||http://purl.uniprot.org/annotation/VAR_051378|||http://purl.uniprot.org/annotation/VAR_063400|||http://purl.uniprot.org/annotation/VSP_003971|||http://purl.uniprot.org/annotation/VSP_039422|||http://purl.uniprot.org/annotation/VSP_039423|||http://purl.uniprot.org/annotation/VSP_039424|||http://purl.uniprot.org/annotation/VSP_039425|||http://purl.uniprot.org/annotation/VSP_039426
http://togogenome.org/gene/9606:ARHGAP32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7KAX9|||http://purl.uniprot.org/uniprot/Q86T64                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with FYN|||Interaction with GAB2|||Loss of GAP activity.|||Loss of GAP activity. In isoform 1, no inhibitory effect on neurite extension.|||Loss of binding to phospholipids. Cytoplasmic localization.|||Mild effect on GAP activity and neurite-promotion upon nerve growth factor stimulation.|||Omega-N-methylarginine|||PX; atypical|||Phosphoserine|||Polar residues|||Rho GTPase-activating protein 32|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345203|||http://purl.uniprot.org/annotation/VSP_034933|||http://purl.uniprot.org/annotation/VSP_034934|||http://purl.uniprot.org/annotation/VSP_034935|||http://purl.uniprot.org/annotation/VSP_034936
http://togogenome.org/gene/9606:INSM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T92                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1; atypical|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Insulinoma-associated protein 2|||Polar residues|||SNAG domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000331576|||http://purl.uniprot.org/annotation/VAR_070885
http://togogenome.org/gene/9606:ND5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03915|||http://purl.uniprot.org/uniprot/U5ZC31                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Found in a patient with mitochondrial complex I deficiency; unknown pathological significance.|||Helical|||In LHON.|||In LHON; primary rare mutation.|||In LHON; secondary mutation; does not seem to directly cause the disease.|||In LS.|||In MELAS.|||In MELAS; disease features overlapping with Leber optic atrophy and Leigh syndrome.|||NADH dehydrogenase subunit 5 C-terminal|||NADH-Ubiquinone oxidoreductase (complex I) chain 5 N-terminal|||NADH-ubiquinone oxidoreductase chain 5|||NADH:quinone oxidoreductase/Mrp antiporter membrane subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118101|||http://purl.uniprot.org/annotation/PRO_5015101636|||http://purl.uniprot.org/annotation/VAR_004761|||http://purl.uniprot.org/annotation/VAR_004762|||http://purl.uniprot.org/annotation/VAR_008603|||http://purl.uniprot.org/annotation/VAR_008864|||http://purl.uniprot.org/annotation/VAR_008865|||http://purl.uniprot.org/annotation/VAR_008866|||http://purl.uniprot.org/annotation/VAR_008867|||http://purl.uniprot.org/annotation/VAR_008868|||http://purl.uniprot.org/annotation/VAR_008869|||http://purl.uniprot.org/annotation/VAR_008870|||http://purl.uniprot.org/annotation/VAR_008871|||http://purl.uniprot.org/annotation/VAR_008872|||http://purl.uniprot.org/annotation/VAR_011357|||http://purl.uniprot.org/annotation/VAR_011358|||http://purl.uniprot.org/annotation/VAR_011359|||http://purl.uniprot.org/annotation/VAR_035424|||http://purl.uniprot.org/annotation/VAR_035425|||http://purl.uniprot.org/annotation/VAR_035426|||http://purl.uniprot.org/annotation/VAR_035427|||http://purl.uniprot.org/annotation/VAR_035428|||http://purl.uniprot.org/annotation/VAR_035429|||http://purl.uniprot.org/annotation/VAR_035430|||http://purl.uniprot.org/annotation/VAR_064566|||http://purl.uniprot.org/annotation/VAR_064567
http://togogenome.org/gene/9606:GGACT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BVM4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Gamma-glutamylaminecyclotransferase|||Loss of activity.|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320203
http://togogenome.org/gene/9606:COLQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y215                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acetylcholinesterase collagenic tail peptide|||Basic and acidic residues|||Collagen-like 1|||Collagen-like 2|||Disordered|||Heparan sulfate proteoglycan binding|||In CMS5.|||In CMS5; abrogates binding to T subunit.|||In CMS5; impairs anchoring to the basal lamina.|||In isoform II.|||In isoform III.|||In isoform IV.|||In isoform V.|||In isoform VI.|||In isoform VII.|||In isoform VIII.|||Interchain|||Interchain (with T subunit)|||PRAD|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005854|||http://purl.uniprot.org/annotation/VAR_010133|||http://purl.uniprot.org/annotation/VAR_010134|||http://purl.uniprot.org/annotation/VAR_010135|||http://purl.uniprot.org/annotation/VAR_010136|||http://purl.uniprot.org/annotation/VAR_010137|||http://purl.uniprot.org/annotation/VAR_048809|||http://purl.uniprot.org/annotation/VAR_071710|||http://purl.uniprot.org/annotation/VSP_001175|||http://purl.uniprot.org/annotation/VSP_001176|||http://purl.uniprot.org/annotation/VSP_001177|||http://purl.uniprot.org/annotation/VSP_001178|||http://purl.uniprot.org/annotation/VSP_001179|||http://purl.uniprot.org/annotation/VSP_001180|||http://purl.uniprot.org/annotation/VSP_001181|||http://purl.uniprot.org/annotation/VSP_001182|||http://purl.uniprot.org/annotation/VSP_001183|||http://purl.uniprot.org/annotation/VSP_001184
http://togogenome.org/gene/9606:TNRC6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPQ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In GDSBA.|||In GDSBA; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Interaction with argonaute proteins|||PABPC1-interacting motif-2 (PAM2)|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RRM|||Silencing domain; interaction with CNOT1 and PAN3|||Trinucleotide repeat-containing gene 6B protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072605|||http://purl.uniprot.org/annotation/VAR_051452|||http://purl.uniprot.org/annotation/VAR_081535|||http://purl.uniprot.org/annotation/VAR_085412|||http://purl.uniprot.org/annotation/VAR_085413|||http://purl.uniprot.org/annotation/VAR_085414|||http://purl.uniprot.org/annotation/VAR_085415|||http://purl.uniprot.org/annotation/VAR_085416|||http://purl.uniprot.org/annotation/VSP_037290|||http://purl.uniprot.org/annotation/VSP_037291|||http://purl.uniprot.org/annotation/VSP_037292|||http://purl.uniprot.org/annotation/VSP_037293
http://togogenome.org/gene/9606:ADH5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11766|||http://purl.uniprot.org/uniprot/Q6IRT1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alcohol dehydrogenase class-3|||Alcohol dehydrogenase-like C-terminal|||Alcohol dehydrogenase-like N-terminal|||Important for FDH activity and activation by fatty acids|||In AMEDS.|||Loss of FDH activity and loss of activation by fatty acids.|||N-acetylalanine|||N6-succinyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160759|||http://purl.uniprot.org/annotation/VAR_025823|||http://purl.uniprot.org/annotation/VAR_025824|||http://purl.uniprot.org/annotation/VAR_048199|||http://purl.uniprot.org/annotation/VAR_086835
http://togogenome.org/gene/9606:SCN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60939|||http://purl.uniprot.org/uniprot/Q5U0K8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binds SCN2A|||Cytoplasmic|||Disordered|||Does not bind alpha subunit. Loss of ability to protect alpha subunit from inhibition by the spider protoxin-II.|||Extracellular|||Found in a patient with Brugada syndrome; unknown pathological significance; induces a reduction in sodium current density most likely by decreasing SCN5A protein cell surface expression.|||Helical|||Ig-like|||Ig-like C2-type|||In ATFB14; the mutant results in reduced sodium currents and altered channel gating when coexpressed with SCN5A in a heterologous expression system.|||Interchain; with alpha subunit|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine|||Sodium channel subunit beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014931|||http://purl.uniprot.org/annotation/PRO_5014310135|||http://purl.uniprot.org/annotation/VAR_029131|||http://purl.uniprot.org/annotation/VAR_029132|||http://purl.uniprot.org/annotation/VAR_070229|||http://purl.uniprot.org/annotation/VAR_070230
http://togogenome.org/gene/9606:ASH1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2V316|||http://purl.uniprot.org/uniprot/A0A7I2V3D6|||http://purl.uniprot.org/uniprot/Q9NR48                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||AWS|||Abolishes methylation by N6AMT1.|||BAH|||Basic and acidic residues|||Basic residues|||Bromo|||Catalytic domain|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone-lysine N-methyltransferase ASH1L|||In MRD52.|||In MRD52; unknown pathological significance.|||In isoform 2.|||N5-methylglutamine|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Polar residues|||Post-SET|||SET                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259516|||http://purl.uniprot.org/annotation/VAR_028949|||http://purl.uniprot.org/annotation/VAR_055905|||http://purl.uniprot.org/annotation/VAR_069405|||http://purl.uniprot.org/annotation/VAR_069406|||http://purl.uniprot.org/annotation/VAR_069407|||http://purl.uniprot.org/annotation/VAR_069408|||http://purl.uniprot.org/annotation/VAR_069409|||http://purl.uniprot.org/annotation/VAR_069410|||http://purl.uniprot.org/annotation/VAR_080559|||http://purl.uniprot.org/annotation/VAR_080560|||http://purl.uniprot.org/annotation/VAR_080561|||http://purl.uniprot.org/annotation/VAR_080562|||http://purl.uniprot.org/annotation/VSP_039421
http://togogenome.org/gene/9606:RTL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N8U3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type|||Disordered|||Retrotransposon Gag-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150956|||http://purl.uniprot.org/annotation/VAR_053752
http://togogenome.org/gene/9606:S100A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P80511                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Mass|||Molecule Processing|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Mass|||Peptide|||Region|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Calcitermin|||EF-hand 1|||EF-hand 2|||Hinge domain|||Protein S100-A12|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004774|||http://purl.uniprot.org/annotation/PRO_0000045383
http://togogenome.org/gene/9606:BEST2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFU1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||INTRAMEM|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||INTRAMEM|||Region|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Bestrophin-2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143118
http://togogenome.org/gene/9606:HLA-DPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20036|||http://purl.uniprot.org/uniprot/X5CKE2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alpha-1|||Alpha-2|||Connecting peptide|||Cytoplasmic|||Extracellular|||HLA class II histocompatibility antigen, DP alpha 1 chain|||Helical|||Ig-like|||Ig-like C1-type|||In allele DPA1*01:04, allele DPA1*01:08, allele DPA1*03:03 and allele DPA1*04:01.|||In allele DPA1*01:05, allele DPA1*02:01, allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and allele DPA1*04:01.|||In allele DPA1*01:06, allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*02:04; requires 2 nucleotide substitutions.|||In allele DPA1*01:07.|||In allele DPA1*01:08, allele DPA1*02:01, allele DPA1*02:02, allele DPA1*02:03, allele DPA1*02:04 and allele DPA1*04:01.|||In allele DPA1*01:09.|||In allele DPA1*01:10.|||In allele DPA1*02:01 and allele DPA1*02:02.|||In allele DPA1*02:01, allele DPA1*02:02 and allele DPA1*04:01.|||In allele DPA1*02:02, allele DPA1*02:04, allele DPA1*03:01, allele DPA1*03:02 and allele DPA1*03:03; requires 2 nucleotide substitutions.|||In allele DPA1*02:04.|||In allele DPA1*03:01 and allele DPA1*03:03.|||In allele DPA1*04:01.|||In allele DPA1*04:01; requires 2 nucleotide substitutions.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018967|||http://purl.uniprot.org/annotation/PRO_5014316166|||http://purl.uniprot.org/annotation/VAR_047683|||http://purl.uniprot.org/annotation/VAR_047684|||http://purl.uniprot.org/annotation/VAR_047685|||http://purl.uniprot.org/annotation/VAR_047686|||http://purl.uniprot.org/annotation/VAR_047687|||http://purl.uniprot.org/annotation/VAR_047688|||http://purl.uniprot.org/annotation/VAR_047689|||http://purl.uniprot.org/annotation/VAR_047690|||http://purl.uniprot.org/annotation/VAR_058832|||http://purl.uniprot.org/annotation/VAR_058833|||http://purl.uniprot.org/annotation/VAR_058834|||http://purl.uniprot.org/annotation/VAR_058835|||http://purl.uniprot.org/annotation/VAR_058836|||http://purl.uniprot.org/annotation/VAR_058837|||http://purl.uniprot.org/annotation/VAR_058838|||http://purl.uniprot.org/annotation/VAR_058839|||http://purl.uniprot.org/annotation/VAR_058840|||http://purl.uniprot.org/annotation/VAR_058841|||http://purl.uniprot.org/annotation/VAR_058842|||http://purl.uniprot.org/annotation/VAR_058843|||http://purl.uniprot.org/annotation/VAR_058844|||http://purl.uniprot.org/annotation/VAR_058845|||http://purl.uniprot.org/annotation/VAR_058850
http://togogenome.org/gene/9606:RPEL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2QD12                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain                                                                                  ^@                                                                                  Proton acceptor|||Proton donor|||Ribulose-phosphate 3-epimerase-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425564
http://togogenome.org/gene/9606:DHX40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DR88|||http://purl.uniprot.org/uniprot/Q8IX18                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DEAH box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Probable ATP-dependent RNA helicase DHX40                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252395|||http://purl.uniprot.org/annotation/VSP_020932|||http://purl.uniprot.org/annotation/VSP_020933|||http://purl.uniprot.org/annotation/VSP_020934|||http://purl.uniprot.org/annotation/VSP_020935|||http://purl.uniprot.org/annotation/VSP_046973
http://togogenome.org/gene/9606:EMILIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6C2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  C1q|||Collagen-like|||Disordered|||EMI|||EMILIN-1|||Found in a patient with connective tissue disorder and peripheral neuropathy; unknown pathological significance; decreased secretion; accumulates in the endoplasmic reticulum.|||In HMN10; unable to rescue locomotor defects in Emilin1a zebrafish morphants; reduced extracellular deposition of EMILIN-1 from patient cells.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007815|||http://purl.uniprot.org/annotation/VAR_046095|||http://purl.uniprot.org/annotation/VAR_046096|||http://purl.uniprot.org/annotation/VAR_046097|||http://purl.uniprot.org/annotation/VAR_077591|||http://purl.uniprot.org/annotation/VAR_087801|||http://purl.uniprot.org/annotation/VSP_055478|||http://purl.uniprot.org/annotation/VSP_055479|||http://purl.uniprot.org/annotation/VSP_055480
http://togogenome.org/gene/9606:PSG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16557                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Cell attachment site|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||N-linked (GlcNAc...) asparagine|||Pregnancy-specific beta-1-glycoprotein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014910|||http://purl.uniprot.org/annotation/VAR_015679|||http://purl.uniprot.org/annotation/VAR_026722|||http://purl.uniprot.org/annotation/VAR_026723|||http://purl.uniprot.org/annotation/VAR_049921|||http://purl.uniprot.org/annotation/VAR_059409|||http://purl.uniprot.org/annotation/VAR_061323
http://togogenome.org/gene/9606:CYFIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7L576                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845.|||Constitutive induction of the formation of actin filaments; when associated with A-841.|||Constitutive induction of the formation of actin filaments; when associated with D-697.|||Constitutive induction of the formation of actin filaments; when associated with D-704.|||Cytoplasmic FMR1-interacting protein 1|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Reduced interaction with RAC1.|||Reduced interaction with RAC1; when associated with A-626.|||Reduced interaction with RAC1; when associated with K-434.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279706|||http://purl.uniprot.org/annotation/VAR_053849|||http://purl.uniprot.org/annotation/VAR_053850|||http://purl.uniprot.org/annotation/VAR_053851|||http://purl.uniprot.org/annotation/VSP_052345|||http://purl.uniprot.org/annotation/VSP_052346|||http://purl.uniprot.org/annotation/VSP_052347
http://togogenome.org/gene/9606:USP13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YZ17|||http://purl.uniprot.org/uniprot/Q92995                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes deubiquitinating activity. Does not abolish ability to stabilize SIAH2. Does not abolish ability to stabilize SIAH2; when associated with A-814 and A-823.|||Does not abolish ability to stabilize SIAH2.|||Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-814.|||Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-823.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impairs ability to stabilize SIAH2 and STAT1. Abolishes ability to stabilize SIAH2 and STAT1; when associated with E-664.|||Impairs ability to stabilize SIAH2 and STAT1. Abolishes ability to stabilize SIAH2 and STAT1; when associated with E-739.|||Impairs ability to stabilize SIAH2.|||In isoform 2.|||Nucleophile|||Phosphoserine; by AURKB|||Phosphothreonine|||Proton acceptor|||UBA|||UBA 1|||UBA 2|||UBP-type|||UBP-type; degenerate|||USP|||Ubiquitin carboxyl-terminal hydrolase 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080635|||http://purl.uniprot.org/annotation/VSP_043954
http://togogenome.org/gene/9606:POTEH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6S545                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Basic and acidic residues|||Disordered|||In isoform 2.|||POTE ankyrin domain family member H                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066918|||http://purl.uniprot.org/annotation/VSP_039738
http://togogenome.org/gene/9606:PASK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7R6|||http://purl.uniprot.org/uniprot/Q96RG2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Does not affect protein kinase activity.|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Induces lower protein kinase activity and ability to autophosphorylate.|||Induces lower protein kinase activity.|||Loss of autophosphorylating activity.|||Loss of catalytic activity (PubMed:11459942). According to another report, does not affect the protein kinase activity (PubMed:20943661). Does not affect protein translation.|||Loss of catalytic activity. Does not affect protein translation.|||N-acetylmethionine|||PAS|||PAS 1|||PAS 2|||PAS domain-containing serine/threonine-protein kinase|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086480|||http://purl.uniprot.org/annotation/VAR_028293|||http://purl.uniprot.org/annotation/VAR_028294|||http://purl.uniprot.org/annotation/VAR_028295|||http://purl.uniprot.org/annotation/VAR_028296|||http://purl.uniprot.org/annotation/VAR_028297|||http://purl.uniprot.org/annotation/VAR_028298|||http://purl.uniprot.org/annotation/VAR_040986|||http://purl.uniprot.org/annotation/VAR_040987|||http://purl.uniprot.org/annotation/VAR_040988|||http://purl.uniprot.org/annotation/VAR_040989|||http://purl.uniprot.org/annotation/VAR_040990|||http://purl.uniprot.org/annotation/VAR_040991|||http://purl.uniprot.org/annotation/VAR_040992|||http://purl.uniprot.org/annotation/VAR_040993|||http://purl.uniprot.org/annotation/VSP_009302|||http://purl.uniprot.org/annotation/VSP_045543|||http://purl.uniprot.org/annotation/VSP_045544
http://togogenome.org/gene/9606:TRIM48                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Mutagenesis Site|||Zinc Finger                                                                                  ^@                                                                                  Abolishes PRMT1 ubiquitination and MAP3K5 activation.|||B box-type|||E3 ubiquitin-protein ligase TRIM48|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056272
http://togogenome.org/gene/9606:EYS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T1H1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11|||EGF-like 12|||EGF-like 13|||EGF-like 14; calcium-binding|||EGF-like 15|||EGF-like 16; calcium-binding|||EGF-like 17|||EGF-like 18|||EGF-like 19|||EGF-like 2|||EGF-like 20; calcium-binding|||EGF-like 21|||EGF-like 22|||EGF-like 23|||EGF-like 24|||EGF-like 25|||EGF-like 26|||EGF-like 27|||EGF-like 3|||EGF-like 4|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||In RP25.|||In RP25; unknown pathological significance.|||In isoform 1.|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Laminin G-like 1|||Laminin G-like 2|||Laminin G-like 3|||Laminin G-like 4|||Laminin G-like 5|||N-linked (GlcNAc...) asparagine|||Protein eyes shut homolog|||Requires 2 nucleotide substitutions.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337014|||http://purl.uniprot.org/annotation/VAR_035301|||http://purl.uniprot.org/annotation/VAR_043561|||http://purl.uniprot.org/annotation/VAR_063437|||http://purl.uniprot.org/annotation/VAR_063438|||http://purl.uniprot.org/annotation/VAR_063439|||http://purl.uniprot.org/annotation/VAR_063440|||http://purl.uniprot.org/annotation/VAR_063441|||http://purl.uniprot.org/annotation/VAR_063442|||http://purl.uniprot.org/annotation/VAR_063443|||http://purl.uniprot.org/annotation/VAR_063444|||http://purl.uniprot.org/annotation/VAR_063445|||http://purl.uniprot.org/annotation/VAR_063446|||http://purl.uniprot.org/annotation/VAR_063447|||http://purl.uniprot.org/annotation/VAR_063448|||http://purl.uniprot.org/annotation/VAR_063449|||http://purl.uniprot.org/annotation/VAR_063450|||http://purl.uniprot.org/annotation/VAR_063451|||http://purl.uniprot.org/annotation/VAR_063452|||http://purl.uniprot.org/annotation/VAR_063453|||http://purl.uniprot.org/annotation/VAR_063454|||http://purl.uniprot.org/annotation/VAR_063455|||http://purl.uniprot.org/annotation/VAR_063456|||http://purl.uniprot.org/annotation/VAR_063457|||http://purl.uniprot.org/annotation/VAR_063458|||http://purl.uniprot.org/annotation/VAR_063459|||http://purl.uniprot.org/annotation/VAR_063460|||http://purl.uniprot.org/annotation/VAR_063461|||http://purl.uniprot.org/annotation/VAR_063462|||http://purl.uniprot.org/annotation/VAR_063463|||http://purl.uniprot.org/annotation/VAR_063464|||http://purl.uniprot.org/annotation/VAR_063465|||http://purl.uniprot.org/annotation/VAR_063466|||http://purl.uniprot.org/annotation/VAR_063467|||http://purl.uniprot.org/annotation/VAR_063468|||http://purl.uniprot.org/annotation/VAR_063469|||http://purl.uniprot.org/annotation/VAR_063470|||http://purl.uniprot.org/annotation/VAR_063471|||http://purl.uniprot.org/annotation/VAR_063472|||http://purl.uniprot.org/annotation/VAR_063473|||http://purl.uniprot.org/annotation/VAR_063474|||http://purl.uniprot.org/annotation/VAR_063475|||http://purl.uniprot.org/annotation/VAR_063476|||http://purl.uniprot.org/annotation/VAR_063477|||http://purl.uniprot.org/annotation/VAR_063478|||http://purl.uniprot.org/annotation/VAR_063479|||http://purl.uniprot.org/annotation/VAR_063480|||http://purl.uniprot.org/annotation/VAR_063481|||http://purl.uniprot.org/annotation/VAR_063482|||http://purl.uniprot.org/annotation/VAR_063483|||http://purl.uniprot.org/annotation/VAR_063484|||http://purl.uniprot.org/annotation/VAR_063485|||http://purl.uniprot.org/annotation/VAR_063486|||http://purl.uniprot.org/annotation/VAR_063487|||http://purl.uniprot.org/annotation/VAR_063488|||http://purl.uniprot.org/annotation/VAR_063489|||http://purl.uniprot.org/annotation/VAR_064417|||http://purl.uniprot.org/annotation/VAR_064418|||http://purl.uniprot.org/annotation/VAR_064419|||http://purl.uniprot.org/annotation/VAR_064420|||http://purl.uniprot.org/annotation/VSP_035821|||http://purl.uniprot.org/annotation/VSP_035822|||http://purl.uniprot.org/annotation/VSP_036709|||http://purl.uniprot.org/annotation/VSP_047161
http://togogenome.org/gene/9606:CCNG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51959                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cyclin-G1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080465|||http://purl.uniprot.org/annotation/VAR_021079|||http://purl.uniprot.org/annotation/VAR_021080|||http://purl.uniprot.org/annotation/VSP_056943
http://togogenome.org/gene/9606:MGAT5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3V5L5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2 and isoform 3.|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288611|||http://purl.uniprot.org/annotation/VAR_032452|||http://purl.uniprot.org/annotation/VSP_025731|||http://purl.uniprot.org/annotation/VSP_025734
http://togogenome.org/gene/9606:SPRED2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPL5|||http://purl.uniprot.org/uniprot/Q7Z698                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In NS14; results in loss of MAPK down-regulation; increased protein degradation.|||In NS14; results in loss of MAPK down-regulation; increased protein degradation; properly targeted to the cell membrane; loss of interaction with NF1.|||In isoform 2.|||KBD|||No effect on phosphorylation or ubiquitination.|||No effect on phosphorylation or ubiquitination; when associated with F-264.|||No effect on phosphorylation or ubiquitination; when associated with F-266.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Reduces ubiquitination and CBL-induced phosphorylation; when associated with F-228.|||Reduces ubiquitination and CBL-induced phosphorylation; when associated with F-231.|||SPR|||Sprouty-related, EVH1 domain-containing protein 2|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076910|||http://purl.uniprot.org/annotation/VAR_086929|||http://purl.uniprot.org/annotation/VAR_086930|||http://purl.uniprot.org/annotation/VSP_043755
http://togogenome.org/gene/9606:ZNF45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02386                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 45                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047378|||http://purl.uniprot.org/annotation/VAR_012019|||http://purl.uniprot.org/annotation/VAR_012020|||http://purl.uniprot.org/annotation/VAR_012021|||http://purl.uniprot.org/annotation/VAR_012022|||http://purl.uniprot.org/annotation/VAR_012023
http://togogenome.org/gene/9606:CABYR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024RC21|||http://purl.uniprot.org/uniprot/A0A0D9SFQ2|||http://purl.uniprot.org/uniprot/B4DXA8|||http://purl.uniprot.org/uniprot/O75952                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Calcium-binding tyrosine phosphorylation-regulated protein|||Decreases phosphorylation and interaction with GSK3B. Abolishes phosphorylation and decreases interaction with GSK3B; when associated with A-151.|||Decreases phosphorylation. Abolishes phosphorylation; when associated with A-155.|||Disordered|||Does not affect phosphorylation.|||Does not affect phosphorylation. Does not affect phosphorylation; when associated with A-154.|||Does not affect phosphorylation. Does not affect phosphorylation; when associated with A-159.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RIIa                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089268|||http://purl.uniprot.org/annotation/VAR_023818|||http://purl.uniprot.org/annotation/VAR_030040|||http://purl.uniprot.org/annotation/VAR_030041|||http://purl.uniprot.org/annotation/VAR_050709|||http://purl.uniprot.org/annotation/VSP_016245|||http://purl.uniprot.org/annotation/VSP_016246|||http://purl.uniprot.org/annotation/VSP_016247|||http://purl.uniprot.org/annotation/VSP_016248|||http://purl.uniprot.org/annotation/VSP_016249|||http://purl.uniprot.org/annotation/VSP_016250|||http://purl.uniprot.org/annotation/VSP_016251
http://togogenome.org/gene/9606:SUPT6H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7KZ85                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with IWS1|||Interaction with KDM6A|||Interaction with PAAF1|||Interaction with histone H2B and H3|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Removed|||S1 motif|||SH2|||Transcription elongation factor SPT6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072171|||http://purl.uniprot.org/annotation/VSP_011505|||http://purl.uniprot.org/annotation/VSP_011506|||http://purl.uniprot.org/annotation/VSP_011507
http://togogenome.org/gene/9606:LSM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y333                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue                                                                                  ^@                                                                                  Phosphothreonine|||Sm|||U6 snRNA-associated Sm-like protein LSm2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125556
http://togogenome.org/gene/9606:LPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8W0|||http://purl.uniprot.org/uniprot/B7ZLW0|||http://purl.uniprot.org/uniprot/Q93052                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes binding to SCRIB.|||Breakpoint for translocation to form HMGA2-LPP|||Breakpoint for translocation to form HMGA2-LPP and KMT2A/MLL1-LPP|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Lipoma-preferred partner|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075832|||http://purl.uniprot.org/annotation/VAR_034070|||http://purl.uniprot.org/annotation/VAR_050150|||http://purl.uniprot.org/annotation/VAR_050151
http://togogenome.org/gene/9606:GALP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBC7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Propeptide|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Galanin-like peptide|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010463|||http://purl.uniprot.org/annotation/PRO_0000010464|||http://purl.uniprot.org/annotation/VAR_020426|||http://purl.uniprot.org/annotation/VSP_030460
http://togogenome.org/gene/9606:TMEM30A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV96                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cell cycle control protein 50A|||Cytoplasmic|||Decreases PS- and PE-dependent ATPase activity of ATP11C:TMEM30A; when associated with A-132 and A-133.|||Decreases PS- and PE-dependent ATPase activity of ATP11C:TMEM30A; when associated with A-132 and A-136.|||Decreases PS- and PE-dependent ATPase activity of ATP11C:TMEM30A; when associated with A-133 and A-136.|||Disordered|||Exoplasmic loop|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244469|||http://purl.uniprot.org/annotation/VSP_019567|||http://purl.uniprot.org/annotation/VSP_019568
http://togogenome.org/gene/9606:IDH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3Y6|||http://purl.uniprot.org/uniprot/O75874                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Critical for catalysis|||In a glioma sample; glioblastoma multiforme; somatic mutation; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate.|||In a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors.|||In a glioma sample; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate.|||In colorectal cancer and glioma samples; glioblastoma multiforme; somatic mutation; found in patients with cartilaginous tumors; abolishes magnesium binding and alters enzyme activity so that isocitrate is no longer converted to alpha-ketoglutarate but instead alpha-ketoglutarate is converted to R(-)-2-hydroxyglutarate; induces histone methylation; enhances expression of chondrocyte-related genes; disturbs the formation of cartilaginous matrix; inhibits osteogenic differentiation.|||Isocitrate dehydrogenase [NADP] cytoplasmic|||N-acetylserine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083575|||http://purl.uniprot.org/annotation/VAR_036013|||http://purl.uniprot.org/annotation/VAR_049780|||http://purl.uniprot.org/annotation/VAR_055454|||http://purl.uniprot.org/annotation/VAR_055455|||http://purl.uniprot.org/annotation/VAR_055456|||http://purl.uniprot.org/annotation/VAR_055457
http://togogenome.org/gene/9606:HBB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D9YZU5|||http://purl.uniprot.org/uniprot/P68871                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Mass|||Modified Residue|||Peptide|||Sequence Conflict|||Sequence Variant|||Site|||Turn                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by N.americanus apr-2|||Globin family profile|||Hemoglobin subunit beta|||In Aalborg; unstable.|||In Abruzzo; O(2) affinity up.|||In Agenogi; O(2) affinity down.|||In Alabama.|||In Alamo.|||In Alberta; O(2) affinity up.|||In Alesha; unstable.|||In Altdorf; O(2) affinity up; unstable.|||In Ankara.|||In Atlanta; unstable.|||In Aurora; O(2) affinity up.|||In Avicenna.|||In B-THAL; Dhonburi/Neapolis; unstable.|||In B-THAL; Durham-N.C./Brescia.|||In B-THAL; Hb E; confers resistance to severe malaria.|||In B-THAL; Hradec Kralove; unstable.|||In Bab-Saadoum; slightly unstable.|||In Baden; slightly unstable.|||In Barcelona; O(2) affinity up.|||In Baylor; unstable.|||In Beckman; originally reported as E-136; O(2) affinity down; unstable.|||In Beirut.|||In Belfast; O(2) affinity up; unstable.|||In Beth Israel; O(2) affinity down; unstable.|||In Bethesda; O(2) affinity up.|||In Bologna; O(2) affinity down.|||In Boras; unstable.|||In Brest; unstable.|||In Brigham; O(2) affinity up.|||In Brisbane; O(2) affinity up.|||In Bristol.|||In British Columbia; O(2) affinity up.|||In Brockton; unstable.|||In Bruxelles.|||In Bunbury; O(2) affinity up.|||In Burke; O(2) affinity down; unstable.|||In Bushwick; unstable.|||In Camden/Tokuchi/Motown.|||In Camperdown and Duino; associated with P-92 in Duino; unstable.|||In Canterbury.|||In Caribbean; O(2) affinity down; unstable.|||In Castilla; unstable.|||In Chandigarh.|||In Cheverly; unstable.|||In Chico; O(2) affinity down.|||In Christchurch; unstable.|||In City of Hope.|||In Cocody.|||In Coimbra; O(2) affinity up.|||In Collingwood; unstable.|||In Complutense.|||In Connecticut; O(2) affinity down.|||In Costa Rica.|||In Cowtown; O(2) affinity up.|||In Crete; O(2) affinity up; unstable.|||In Creteil; O(2) affinity up.|||In D-Bushman.|||In D-Camperdown/Beograd.|||In D-Granada.|||In D-Ibadan.|||In D-Iran.|||In D-Los Angeles/D-Punjab/D-Portugal/D-Chicago/D-Oak Ridge.|||In D-Neath.|||In D-Ouleh RABAH.|||In Debrousse; unstable; O(2) affinity up.|||In Deer Lodge; O(2) affinity up.|||In Detroit.|||In Dhofar/Yukuhashi.|||In Duarte; unstable.|||In E-Saskatoon.|||In Edmonton.|||In Extredemura.|||In Freiburg.|||In Fukuoka.|||In Fukuyama.|||In G-Coushatta/G-Saskatoon/G-Taegu/Hsin Chu.|||In G-Makassar.|||In G-San Jose; mildly unstable.|||In G-Siriraj.|||In G-Szuhu/Gifu.|||In G-Taipei.|||In G-Taiwan Ami.|||In G-ferrara; unstable.|||In Gavello.|||In Geelong; unstable.|||In Genova/Hyogo; unstable.|||In Grange-blanche; O(2) affinity up.|||In Graz.|||In Hafnia.|||In Hamadan.|||In Hamilton.|||In Hammersmith.|||In Hb C; confers resistance to severe malaria.|||In Heathrow; O(2) affinity up.|||In Helsinki; O(2) affinity up.|||In Henri Mondor; slightly unstable.|||In Hijiyama.|||In Hikari.|||In Himeji; unstable; O(2) affinity down.|||In Hinsdale; O(2) affinity down.|||In Hinwil; O(2) affinity up.|||In Hirose; O(2) affinity up.|||In Hiroshima; O(2) affinity up.|||In Hofu; unstable.|||In Hope; O(2) affinity down; unstable.|||In Hoshida/Chaya.|||In Howick.|||In I-High Wycombe.|||In Indianapolis.|||In Iowa.|||In Iraq-Halabja.|||In Isehara; unstable.|||In Istambul; unstable.|||In J-Altgelds Gardens; unstable.|||In J-Amiens.|||In J-Antakya.|||In J-Auckland; unstable; O(2) affinity down.|||In J-Baltimore/J-Trinidad/J-Ireland/J-Georgia/N-New Haven.|||In J-Cairo.|||In J-Chicago.|||In J-Cordoba.|||In J-Europa.|||In J-Guantanamo; unstable.|||In J-Iran.|||In J-Lens.|||In J-Luhe.|||In J-Sicilia.|||In Jacksonville; O(2) affinity up; unstable.|||In Jianghua.|||In K-Ibadan.|||In K-Woolwich.|||In Karlskoga.|||In Kenitra.|||In Khartoum; unstable.|||In Knossos.|||In Kodaira; O(2) affinity up.|||In Kofu.|||In La Desirade; O(2) affinity down; unstable.|||In La Roche-sur-Yon; unstable and O(2) affinity up.|||In Las Palmas; slightly unstable.|||In Linkoping/Finlandia; O(2) affinity up.|||In Little Rock; O(2) affinity up.|||In Louisville; unstable.|||In Lufkin; unstable.|||In M-Saskatoon; O(2) affinity up.|||In Machida.|||In Madrid; unstable.|||In Malay.|||In Malmoe; O(2) affinity up.|||In Maputo.|||In Matera; unstable.|||In Mequon.|||In Mississippi.|||In Mito; O(2) affinity up.|||In Miyashiro; O(2) affinity up; unstable.|||In Mizuho; unstable.|||In Mobile; O(2) affinity down.|||In Moriguchi.|||In Moscva; O(2) affinity down; unstable.|||In Muscat; slightly unstable.|||In Muskegon.|||In N-Seatlle.|||In N-Timone.|||In Nagasaki.|||In Nagoya; O(2) affinity up; unstable.|||In Nantes; increased oxygen affinity.|||In Nevers.|||In New Mexico.|||In Newcastle and Duino; associated with S-104 in Duino; unstable.|||In Nikosia.|||In North Chicago; O(2) affinity up.|||In North Shore-Caracas; unstable.|||In Nottingham; unstable.|||In O-Arab.|||In Ocho Rios.|||In Ohio; O(2) affinity up.|||In Okayama; O(2) affinity up.|||In Okazaki; O(2) affinity up; unstable.|||In Olmsted; unstable.|||In Olomouc; O(2) affinity up.|||In Olympia; O(2) affinity up.|||In P-Galveston.|||In Palmerston North; O(2) affinity up; unstable.|||In Pasadena; O(2) affinity up; unstable.|||In Philly; O(2) affinity up; unstable.|||In Pierre-Benite; O(2) affinity up.|||In Pitie-Salpetriere; O(2) affinity up.|||In Porto Alegre; O(2) affinity up.|||In Potomac; O(2) affinity up.|||In Presbyterian; O(2) affinity down; unstable.|||In Providence.|||In Puttelange; polycythemia; O(2) affinity up.|||In Pyrgos.|||In Quebec-Chori.|||In Quin-hai.|||In Rainier; O(2) affinity up.|||In Raleigh; O(2) affinity down.|||In Rambam.|||In Rancho Mirage.|||In Randwick; unstable.|||In Regina; O(2) affinity up.|||In Rio Grande.|||In Riverdale-Bronx; O(2) affinity up; unstable.|||In Rothschild; O(2) affinity down.|||In Rush; unstable.|||In S-Wake; associated with V-6.|||In SKCA; Hb S; at heterozygosity confers resistance to malaria.|||In Sabine; unstable.|||In Saitama; unstable.|||In Saki; unstable.|||In San Diego; O(2) affinity up.|||In Santa Ana; unstable.|||In Santander; unstable.|||In Sarrebourg; unstable.|||In Savannah; unstable.|||In Seattle; O(2) affinity down; unstable.|||In Shangai; unstable.|||In Shelby/Leslie/Deaconess; unstable.|||In Sherwood Forest.|||In Showa-Yakushiji.|||In Soegn; unstable.|||In St Francis.|||In St Jacques; O(2) affinity up.|||In St Louis.|||In St Mande; O(2) affinity down.|||In Stanmore; O(2) affinity down; unstable.|||In Strasbourg; O(2) affinity up.|||In Summer Hill.|||In Sunnybrook.|||In Sydney; unstable.|||In Syracuse; O(2) affinity up.|||In Tacoma; unstable.|||In Takamatsu.|||In Tampa.|||In Tianshui.|||In Tilburg; O(2) affinity down.|||In Tsukumi.|||In Tunis.|||In Ty Gard; O(2) affinity up.|||In Vaasa; unstable.|||In Valletta.|||In Vancouver; O(2) affinity down.|||In Vanderbilt; O(2) affinity up.|||In Vexin; increased oxygen affinity.|||In Vigo; O(2) affinity down.|||In Villejuif; asymptomatic variant.|||In Volga/Drenthe; unstable.|||In Warwickshire.|||In Wien; unstable.|||In Willamette; O(2) affinity up; unstable.|||In Windsor; O(2) affinity up; unstable.|||In Wood; O(2) affinity up.|||In Yahata.|||In Yamagata; O(2) affinity down.|||In Yokohama; unstable.|||In York; O(2) affinity up.|||In Yusa.|||In Zengcheng.|||In non-spherocytic haemolytic anemia; Manukau.|||LVV-hemorphin-7|||N-acetylvaline|||N-linked (Glc) (glycation) lysine|||N-linked (Glc) (glycation) lysine; alternate|||N-linked (Glc) (glycation) valine; in Hb A1c|||N-pyruvate 2-iminyl-valine; in Hb A1b|||N6-acetyllysine|||N6-acetyllysine; alternate|||Not glycated|||Phosphoserine|||Phosphothreonine|||Removed|||S-nitrosocysteine|||Spinorphin|||distal binding residue|||proximal binding residue ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000052976|||http://purl.uniprot.org/annotation/PRO_0000296641|||http://purl.uniprot.org/annotation/PRO_0000424226|||http://purl.uniprot.org/annotation/VAR_002856|||http://purl.uniprot.org/annotation/VAR_002857|||http://purl.uniprot.org/annotation/VAR_002858|||http://purl.uniprot.org/annotation/VAR_002859|||http://purl.uniprot.org/annotation/VAR_002860|||http://purl.uniprot.org/annotation/VAR_002861|||http://purl.uniprot.org/annotation/VAR_002862|||http://purl.uniprot.org/annotation/VAR_002863|||http://purl.uniprot.org/annotation/VAR_002864|||http://purl.uniprot.org/annotation/VAR_002865|||http://purl.uniprot.org/annotation/VAR_002866|||http://purl.uniprot.org/annotation/VAR_002867|||http://purl.uniprot.org/annotation/VAR_002868|||http://purl.uniprot.org/annotation/VAR_002869|||http://purl.uniprot.org/annotation/VAR_002870|||http://purl.uniprot.org/annotation/VAR_002871|||http://purl.uniprot.org/annotation/VAR_002872|||http://purl.uniprot.org/annotation/VAR_002873|||http://purl.uniprot.org/annotation/VAR_002874|||http://purl.uniprot.org/annotation/VAR_002875|||http://purl.uniprot.org/annotation/VAR_002876|||http://purl.uniprot.org/annotation/VAR_002877|||http://purl.uniprot.org/annotation/VAR_002878|||http://purl.uniprot.org/annotation/VAR_002879|||http://purl.uniprot.org/annotation/VAR_002880|||http://purl.uniprot.org/annotation/VAR_002881|||http://purl.uniprot.org/annotation/VAR_002882|||http://purl.uniprot.org/annotation/VAR_002883|||http://purl.uniprot.org/annotation/VAR_002884|||http://purl.uniprot.org/annotation/VAR_002885|||http://purl.uniprot.org/annotation/VAR_002886|||http://purl.uniprot.org/annotation/VAR_002887|||http://purl.uniprot.org/annotation/VAR_002888|||http://purl.uniprot.org/annotation/VAR_002889|||http://purl.uniprot.org/annotation/VAR_002890|||http://purl.uniprot.org/annotation/VAR_002891|||http://purl.uniprot.org/annotation/VAR_002892|||http://purl.uniprot.org/annotation/VAR_002893|||http://purl.uniprot.org/annotation/VAR_002894|||http://purl.uniprot.org/annotation/VAR_002895|||http://purl.uniprot.org/annotation/VAR_002896|||http://purl.uniprot.org/annotation/VAR_002897|||http://purl.uniprot.org/annotation/VAR_002898|||http://purl.uniprot.org/annotation/VAR_002899|||http://purl.uniprot.org/annotation/VAR_002900|||http://purl.uniprot.org/annotation/VAR_002901|||http://purl.uniprot.org/annotation/VAR_002902|||http://purl.uniprot.org/annotation/VAR_002903|||http://purl.uniprot.org/annotation/VAR_002904|||http://purl.uniprot.org/annotation/VAR_002905|||http://purl.uniprot.org/annotation/VAR_002906|||http://purl.uniprot.org/annotation/VAR_002907|||http://purl.uniprot.org/annotation/VAR_002908|||http://purl.uniprot.org/annotation/VAR_002909|||http://purl.uniprot.org/annotation/VAR_002910|||http://purl.uniprot.org/annotation/VAR_002911|||http://purl.uniprot.org/annotation/VAR_002912|||http://purl.uniprot.org/annotation/VAR_002913|||http://purl.uniprot.org/annotation/VAR_002914|||http://purl.uniprot.org/annotation/VAR_002915|||http://purl.uniprot.org/annotation/VAR_002916|||http://purl.uniprot.org/annotation/VAR_002917|||http://purl.uniprot.org/annotation/VAR_002918|||http://purl.uniprot.org/annotation/VAR_002919|||http://purl.uniprot.org/annotation/VAR_002920|||http://purl.uniprot.org/annotation/VAR_002921|||http://purl.uniprot.org/annotation/VAR_002922|||http://purl.uniprot.org/annotation/VAR_002923|||http://purl.uniprot.org/annotation/VAR_002924|||http://purl.uniprot.org/annotation/VAR_002925|||http://purl.uniprot.org/annotation/VAR_002926|||http://purl.uniprot.org/annotation/VAR_002927|||http://purl.uniprot.org/annotation/VAR_002928|||http://purl.uniprot.org/annotation/VAR_002929|||http://purl.uniprot.org/annotation/VAR_002930|||http://purl.uniprot.org/annotation/VAR_002931|||http://purl.uniprot.org/annotation/VAR_002932|||http://purl.uniprot.org/annotation/VAR_002933|||http://purl.uniprot.org/annotation/VAR_002934|||http://purl.uniprot.org/annotation/VAR_002935|||http://purl.uniprot.org/annotation/VAR_002936|||http://purl.uniprot.org/annotation/VAR_002937|||http://purl.uniprot.org/annotation/VAR_002938|||http://purl.uniprot.org/annotation/VAR_002939|||http://purl.uniprot.org/annotation/VAR_002940|||http://purl.uniprot.org/annotation/VAR_002941|||http://purl.uniprot.org/annotation/VAR_002942|||http://purl.uniprot.org/annotation/VAR_002943|||http://purl.uniprot.org/annotation/VAR_002944|||http://purl.uniprot.org/annotation/VAR_002945|||http://purl.uniprot.org/annotation/VAR_002946|||http://purl.uniprot.org/annotation/VAR_002947|||http://purl.uniprot.org/annotation/VAR_002948|||http://purl.uniprot.org/annotation/VAR_002949|||http://purl.uniprot.org/annotation/VAR_002950|||http://purl.uniprot.org/annotation/VAR_002951|||http://purl.uniprot.org/annotation/VAR_002952|||http://purl.uniprot.org/annotation/VAR_002953|||http://purl.uniprot.org/annotation/VAR_002954|||http://purl.uniprot.org/annotation/VAR_002955|||http://purl.uniprot.org/annotation/VAR_002956|||http://purl.uniprot.org/annotation/VAR_002957|||http://purl.uniprot.org/annotation/VAR_002958|||http://purl.uniprot.org/annotation/VAR_002959|||http://purl.uniprot.org/annotation/VAR_002960|||http://purl.uniprot.org/annotation/VAR_002961|||http://purl.uniprot.org/annotation/VAR_002962|||http://purl.uniprot.org/annotation/VAR_002963|||http://purl.uniprot.org/annotation/VAR_002964|||http://purl.uniprot.org/annotation/VAR_002965|||http://purl.uniprot.org/annotation/VAR_002966|||http://purl.uniprot.org/annotation/VAR_002967|||http://purl.uniprot.org/annotation/VAR_002968|||http://purl.uniprot.org/annotation/VAR_002969|||http://purl.uniprot.org/annotation/VAR_002970|||http://purl.uniprot.org/annotation/VAR_002971|||http://purl.uniprot.org/annotation/VAR_002972|||http://purl.uniprot.org/annotation/VAR_002973|||http://purl.uniprot.org/annotation/VAR_002974|||http://purl.uniprot.org/annotation/VAR_002975|||http://purl.uniprot.org/annotation/VAR_002976|||http://purl.uniprot.org/annotation/VAR_002977|||http://purl.uniprot.org/annotation/VAR_002978|||http://purl.uniprot.org/annotation/VAR_002979|||http://purl.uniprot.org/annotation/VAR_002980|||http://purl.uniprot.org/annotation/VAR_002981|||http://purl.uniprot.org/annotation/VAR_002982|||http://purl.uniprot.org/annotation/VAR_002983|||http://purl.uniprot.org/annotation/VAR_002984|||http://purl.uniprot.org/annotation/VAR_002985|||http://purl.uniprot.org/annotation/VAR_002986|||http://purl.uniprot.org/annotation/VAR_002987|||http://purl.uniprot.org/annotation/VAR_002988|||http://purl.uniprot.org/annotation/VAR_002989|||http://purl.uniprot.org/annotation/VAR_002990|||http://purl.uniprot.org/annotation/VAR_002991|||http://purl.uniprot.org/annotation/VAR_002992|||http://purl.uniprot.org/annotation/VAR_002993|||http://purl.uniprot.org/annotation/VAR_002994|||http://purl.uniprot.org/annotation/VAR_002995|||http://purl.uniprot.org/annotation/VAR_002996|||http://purl.uniprot.org/annotation/VAR_002997|||http://purl.uniprot.org/annotation/VAR_002998|||http://purl.uniprot.org/annotation/VAR_002999|||http://purl.uniprot.org/annotation/VAR_003000|||http://purl.uniprot.org/annotation/VAR_003001|||http://purl.uniprot.org/annotation/VAR_003002|||http://purl.uniprot.org/annotation/VAR_003003|||http://purl.uniprot.org/annotation/VAR_003004|||http://purl.uniprot.org/annotation/VAR_003005|||http://purl.uniprot.org/annotation/VAR_003006|||http://purl.uniprot.org/annotation/VAR_003007|||http://purl.uniprot.org/annotation/VAR_003008|||http://purl.uniprot.org/annotation/VAR_003009|||http://purl.uniprot.org/annotation/VAR_003010|||http://purl.uniprot.org/annotation/VAR_003011|||http://purl.uniprot.org/annotation/VAR_003012|||http://purl.uniprot.org/annotation/VAR_003013|||http://purl.uniprot.org/annotation/VAR_003014|||http://purl.uniprot.org/annotation/VAR_003015|||http://purl.uniprot.org/annotation/VAR_003016|||http://purl.uniprot.org/annotation/VAR_003017|||http://purl.uniprot.org/annotation/VAR_003018|||http://purl.uniprot.org/annotation/VAR_003019|||http://purl.uniprot.org/annotation/VAR_003020|||http://purl.uniprot.org/annotation/VAR_003021|||http://purl.uniprot.org/annotation/VAR_003022|||http://purl.uniprot.org/annotation/VAR_003023|||http://purl.uniprot.org/annotation/VAR_003024|||http://purl.uniprot.org/annotation/VAR_003025|||http://purl.uniprot.org/annotation/VAR_003026|||http://purl.uniprot.org/annotation/VAR_003027|||http://purl.uniprot.org/annotation/VAR_003028|||http://purl.uniprot.org/annotation/VAR_003029|||http://purl.uniprot.org/annotation/VAR_003030|||http://purl.uniprot.org/annotation/VAR_003031|||http://purl.uniprot.org/annotation/VAR_003032|||http://purl.uniprot.org/annotation/VAR_003033|||http://purl.uniprot.org/annotation/VAR_003034|||http://purl.uniprot.org/annotation/VAR_003035|||http://purl.uniprot.org/annotation/VAR_003036|||http://purl.uniprot.org/annotation/VAR_003037|||http://purl.uniprot.org/annotation/VAR_003038|||http://purl.uniprot.org/annotation/VAR_003039|||http://purl.uniprot.org/annotation/VAR_003040|||http://purl.uniprot.org/annotation/VAR_003041|||http://purl.uniprot.org/annotation/VAR_003042|||http://purl.uniprot.org/annotation/VAR_003043|||http://purl.uniprot.org/annotation/VAR_003044|||http://purl.uniprot.org/annotation/VAR_003045|||http://purl.uniprot.org/annotation/VAR_003046|||http://purl.uniprot.org/annotation/VAR_003047|||http://purl.uniprot.org/annotation/VAR_003048|||http://purl.uniprot.org/annotation/VAR_003049|||http://purl.uniprot.org/annotation/VAR_003050|||http://purl.uniprot.org/annotation/VAR_003051|||http://purl.uniprot.org/annotation/VAR_003052|||http://purl.uniprot.org/annotation/VAR_003053|||http://purl.uniprot.org/annotation/VAR_003054|||http://purl.uniprot.org/annotation/VAR_003055|||http://purl.uniprot.org/annotation/VAR_003056|||http://purl.uniprot.org/annotation/VAR_003057|||http://purl.uniprot.org/annotation/VAR_003058|||http://purl.uniprot.org/annotation/VAR_003059|||http://purl.uniprot.org/annotation/VAR_003060|||http://purl.uniprot.org/annotation/VAR_003061|||http://purl.uniprot.org/annotation/VAR_003062|||http://purl.uniprot.org/annotation/VAR_003063|||http://purl.uniprot.org/annotation/VAR_003064|||http://purl.uniprot.org/annotation/VAR_003065|||http://purl.uniprot.org/annotation/VAR_003066|||http://purl.uniprot.org/annotation/VAR_003067|||http://purl.uniprot.org/annotation/VAR_003068|||http://purl.uniprot.org/annotation/VAR_003069|||http://purl.uniprot.org/annotation/VAR_003070|||http://purl.uniprot.org/annotation/VAR_003071|||http://purl.uniprot.org/annotation/VAR_003072|||http://purl.uniprot.org/annotation/VAR_003073|||http://purl.uniprot.org/annotation/VAR_003074|||http://purl.uniprot.org/annotation/VAR_003075|||http://purl.uniprot.org/annotation/VAR_003076|||http://purl.uniprot.org/annotation/VAR_003077|||http://purl.uniprot.org/annotation/VAR_003078|||http://purl.uniprot.org/annotation/VAR_003079|||http://purl.uniprot.org/annotation/VAR_003080|||http://purl.uniprot.org/annotation/VAR_003081|||http://purl.uniprot.org/annotation/VAR_003082|||http://purl.uniprot.org/annotation/VAR_003083|||http://purl.uniprot.org/annotation/VAR_003084|||http://purl.uniprot.org/annotation/VAR_003085|||http://purl.uniprot.org/annotation/VAR_003086|||http://purl.uniprot.org/annotation/VAR_003087|||http://purl.uniprot.org/annotation/VAR_003088|||http://purl.uniprot.org/annotation/VAR_003089|||http://purl.uniprot.org/annotation/VAR_003090|||http://purl.uniprot.org/annotation/VAR_003091|||http://purl.uniprot.org/annotation/VAR_003092|||http://purl.uniprot.org/annotation/VAR_003093|||http://purl.uniprot.org/annotation/VAR_003094|||http://purl.uniprot.org/annotation/VAR_003095|||http://purl.uniprot.org/annotation/VAR_010144|||http://purl.uniprot.org/annotation/VAR_010145|||http://purl.uniprot.org/annotation/VAR_012663|||http://purl.uniprot.org/annotation/VAR_012664|||http://purl.uniprot.org/annotation/VAR_025335|||http://purl.uniprot.org/annotation/VAR_025393|||http://purl.uniprot.org/annotation/VAR_025394|||http://purl.uniprot.org/annotation/VAR_025395|||http://purl.uniprot.org/annotation/VAR_025396|||http://purl.uniprot.org/annotation/VAR_025397|||http://purl.uniprot.org/annotation/VAR_025398|||http://purl.uniprot.org/annotation/VAR_025399|||http://purl.uniprot.org/annotation/VAR_035236|||http://purl.uniprot.org/annotation/VAR_035237|||http://purl.uniprot.org/annotation/VAR_035238|||http://purl.uniprot.org/annotation/VAR_035239|||http://purl.uniprot.org/annotation/VAR_035240|||http://purl.uniprot.org/annotation/VAR_040060|||http://purl.uniprot.org/annotation/VAR_049273|||http://purl.uniprot.org/annotation/VAR_069169|||http://purl.uniprot.org/annotation/VAR_079528
http://togogenome.org/gene/9606:SAP18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00422                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-118.|||Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-121.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone deacetylase complex subunit SAP18|||In isoform 2.|||Involved in splicing regulation activity|||N-acetylalanine|||No effect on splicing regulation activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220975|||http://purl.uniprot.org/annotation/VSP_060066
http://togogenome.org/gene/9606:SLC24A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUG1|||http://purl.uniprot.org/uniprot/B4E1W0|||http://purl.uniprot.org/uniprot/F5H127|||http://purl.uniprot.org/uniprot/O60721                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Alpha-1|||Alpha-2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Not cleaved|||Phosphoserine|||Phosphothreonine|||Sodium/calcium exchanger membrane region|||Sodium/potassium/calcium exchanger 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223303|||http://purl.uniprot.org/annotation/VAR_050221|||http://purl.uniprot.org/annotation/VAR_050222|||http://purl.uniprot.org/annotation/VAR_050223|||http://purl.uniprot.org/annotation/VSP_006160|||http://purl.uniprot.org/annotation/VSP_054491
http://togogenome.org/gene/9606:ZNF853                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0CG23                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Polar residues|||Zinc finger protein 853                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000395112|||http://purl.uniprot.org/annotation/VAR_063279|||http://purl.uniprot.org/annotation/VAR_063280|||http://purl.uniprot.org/annotation/VAR_063281
http://togogenome.org/gene/9606:HDHD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSH5                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Haloacid dehalogenase-like hydrolase domain-containing protein 3|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287313|||http://purl.uniprot.org/annotation/VAR_032298
http://togogenome.org/gene/9606:DEFB124                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NES8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 124                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045352
http://togogenome.org/gene/9606:DOCK7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96N67                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis protein 7|||Disordered|||In isoform 2 and isoform 4.|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 7.|||N6-acetyllysine|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189995|||http://purl.uniprot.org/annotation/VAR_057524|||http://purl.uniprot.org/annotation/VSP_007707|||http://purl.uniprot.org/annotation/VSP_012440|||http://purl.uniprot.org/annotation/VSP_022240|||http://purl.uniprot.org/annotation/VSP_054534|||http://purl.uniprot.org/annotation/VSP_054535
http://togogenome.org/gene/9606:SLC43A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N370                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes sensitivity to N-ethymaleimide. Severely decreases phenylalanine transport activity. Decreases affinity for phenylalanine. Strongly decreases glycosylation. Strongly decreases expression. Reduces membrane localization.|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increases affinity for phenylalanine.|||Increases affinity for phenylalanine. Increases phenylalanine transport activity. Strongly decreases glycosylation. Strongly decreases expression. Increases membrane localization.|||Large neutral amino acids transporter small subunit 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Slightly decreases phenylalanine transport.|||Slightly decreases phenylalanine transport. Does not affect membrane localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307272|||http://purl.uniprot.org/annotation/VSP_028664|||http://purl.uniprot.org/annotation/VSP_028665|||http://purl.uniprot.org/annotation/VSP_028666|||http://purl.uniprot.org/annotation/VSP_055373|||http://purl.uniprot.org/annotation/VSP_055374
http://togogenome.org/gene/9606:IZUMO3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/S4R3E6                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_5004522673
http://togogenome.org/gene/9606:ERC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G8JLD3|||http://purl.uniprot.org/uniprot/Q8IUD2|||http://purl.uniprot.org/uniprot/X6RLX0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Breakpoint for translocation to form ERC1-RET oncogene|||Disordered|||ELKS/Rab6-interacting/CAST family member 1|||FIP-RBD|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097176|||http://purl.uniprot.org/annotation/VAR_051304|||http://purl.uniprot.org/annotation/VAR_051305|||http://purl.uniprot.org/annotation/VSP_011450|||http://purl.uniprot.org/annotation/VSP_011451|||http://purl.uniprot.org/annotation/VSP_011452|||http://purl.uniprot.org/annotation/VSP_011453|||http://purl.uniprot.org/annotation/VSP_011454|||http://purl.uniprot.org/annotation/VSP_011455
http://togogenome.org/gene/9606:PIK3R2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00459                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In MPPH1.|||In MPPH1; unknown pathological significance.|||Loss of interaction with FBXL2 and increased half-life; when associated with A-651.|||Loss of interaction with FBXL2 and increased half-life; when associated with A-652.|||Phosphatidylinositol 3-kinase regulatory subunit beta|||Phosphotyrosine|||Pro residues|||Rho-GAP|||SH2 1|||SH2 2|||SH3|||Stabilized interaction with FBXL2 and decreased half-life.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080763|||http://purl.uniprot.org/annotation/VAR_030679|||http://purl.uniprot.org/annotation/VAR_030680|||http://purl.uniprot.org/annotation/VAR_069262|||http://purl.uniprot.org/annotation/VAR_075556|||http://purl.uniprot.org/annotation/VAR_075683|||http://purl.uniprot.org/annotation/VAR_075684
http://togogenome.org/gene/9606:ASB17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXJ9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  ANK|||Ankyrin repeat and SOCS box protein 17|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066959|||http://purl.uniprot.org/annotation/VAR_024174|||http://purl.uniprot.org/annotation/VAR_048288
http://togogenome.org/gene/9606:PTPN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3N4|||http://purl.uniprot.org/uniprot/K7EQG9|||http://purl.uniprot.org/uniprot/P17706|||http://purl.uniprot.org/uniprot/Q59F91                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Alters location to the endoplasmic reticulum; isoform 1.|||Alters phosphorylation by cyclin-dependent kinases of isoform 2 but has no effect on its phosphatase activity.|||Basic and acidic residues|||Disordered|||Endoplasmic reticulum location|||Helical|||Impairs phosphatase activity.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Mediates interaction with STX17|||Phosphocysteine intermediate|||Phosphoserine|||Phosphotyrosine|||Prevents location to the nucleus; isoform 2.|||S-nitrosocysteine|||Substrate-trapping mutant; catalytically inactive it forms a stable complex with physiological substrates including INSR and EGFR. Accumulates in the cytoplasm upon stimulation by insulin or EGF; isoform 2.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094752|||http://purl.uniprot.org/annotation/VSP_005125|||http://purl.uniprot.org/annotation/VSP_043383|||http://purl.uniprot.org/annotation/VSP_054821
http://togogenome.org/gene/9606:TMEM242                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWH2                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial intermembrane|||Mitochondrial matrix|||N-acetylmethionine|||Transmembrane protein 242                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295848
http://togogenome.org/gene/9606:TRIM35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RGB3|||http://purl.uniprot.org/uniprot/Q9UPQ4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||E3 ubiquitin-protein ligase TRIM35|||In isoform 2.|||N-acetylmethionine|||Phosphoserine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056250|||http://purl.uniprot.org/annotation/VSP_012061
http://togogenome.org/gene/9606:ZNF839                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K0R7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||Zinc finger protein 839                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328721|||http://purl.uniprot.org/annotation/VAR_042468|||http://purl.uniprot.org/annotation/VAR_042469|||http://purl.uniprot.org/annotation/VAR_042470|||http://purl.uniprot.org/annotation/VAR_057456|||http://purl.uniprot.org/annotation/VSP_032760|||http://purl.uniprot.org/annotation/VSP_040648
http://togogenome.org/gene/9606:CCDC33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GV97|||http://purl.uniprot.org/uniprot/Q8N5R6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  C2|||Coiled-coil domain-containing protein 33|||Disordered|||In isoform 2 and isoform 5.|||In isoform 2.|||In isoform 4 and isoform 5.|||In isoform 6.|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307643|||http://purl.uniprot.org/annotation/VAR_036625|||http://purl.uniprot.org/annotation/VAR_045602|||http://purl.uniprot.org/annotation/VAR_045603|||http://purl.uniprot.org/annotation/VSP_028755|||http://purl.uniprot.org/annotation/VSP_028756|||http://purl.uniprot.org/annotation/VSP_028757|||http://purl.uniprot.org/annotation/VSP_028758|||http://purl.uniprot.org/annotation/VSP_028759|||http://purl.uniprot.org/annotation/VSP_040258|||http://purl.uniprot.org/annotation/VSP_040259
http://togogenome.org/gene/9606:CHST8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2A9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 8|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In PSS3; results in decreased enzyme activity; the mutant protein shows reduced glycosylation.|||In a colorectal cancer sample; somatic mutation.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189653|||http://purl.uniprot.org/annotation/VAR_036538|||http://purl.uniprot.org/annotation/VAR_067723
http://togogenome.org/gene/9606:MYOM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P54296                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Myomesin-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072686|||http://purl.uniprot.org/annotation/VAR_020083|||http://purl.uniprot.org/annotation/VAR_020084|||http://purl.uniprot.org/annotation/VAR_033613|||http://purl.uniprot.org/annotation/VAR_033614|||http://purl.uniprot.org/annotation/VAR_033615|||http://purl.uniprot.org/annotation/VAR_033616|||http://purl.uniprot.org/annotation/VAR_033617|||http://purl.uniprot.org/annotation/VAR_033618|||http://purl.uniprot.org/annotation/VAR_033619|||http://purl.uniprot.org/annotation/VAR_054501|||http://purl.uniprot.org/annotation/VAR_061320
http://togogenome.org/gene/9606:SLC4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48751                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Anion exchange protein 3|||Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Helical|||In SQT7; loss-of-function variant unable to rescue systolic contraction abnormalities in zebrafish morphants; decreased chloride-bicarbonate exchange in transfected cells; decreased localization to cell membrane.|||In SQT7; unknown pathological significance; unable to rescue heart rate abnormalities in zebrafish morphants.|||In isoform 3.|||In isoform CAE3.|||Membrane (anion exchange)|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Pro residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079219|||http://purl.uniprot.org/annotation/VAR_055536|||http://purl.uniprot.org/annotation/VAR_059081|||http://purl.uniprot.org/annotation/VAR_059082|||http://purl.uniprot.org/annotation/VAR_088079|||http://purl.uniprot.org/annotation/VAR_088080|||http://purl.uniprot.org/annotation/VAR_088081|||http://purl.uniprot.org/annotation/VAR_088082|||http://purl.uniprot.org/annotation/VAR_088083|||http://purl.uniprot.org/annotation/VSP_000462|||http://purl.uniprot.org/annotation/VSP_000463|||http://purl.uniprot.org/annotation/VSP_038184
http://togogenome.org/gene/9606:HSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00613                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  5-fold derepression of transcriptional activity at control temperature; when associated with D-303. Decreased HSF1-induced expression of HSPA1A mRNA in a IER5-dependent manner; when associated with D-121; D-314; D-323 and D-367.|||9aaTAD|||Abolishes sumoylation. No effect on phosphorylation of S-303 nor of S-307. No change in subcellular location to nuclear stress granules upon heat shock. Loss of colocalization with SUMO1 to nuclear stress granules upon heat shock. Does not change interaction with XRCC5 and XRCC6. No effect on binding to HSE nor on transactivation of HSP70. Increases transcriptional activity in a DAXX-dependent manner. No change in protein abundance.|||D domain|||DNA-binding domain|||Decreased HSF1-induced expression of HSPA1A mRNA in a IER5-dependent manner; when associated with D-121; D-307; D-314 and D-323.|||Decreased HSF1-induced expression of HSPA1A mRNA in a IER5-dependent manner; when associated with D-121; D-307; D-314 and D-367.|||Decreased HSF1-induced expression of HSPA1A mRNA in a IER5-dependent manner; when associated with D-121; D-307; D-323 and D-367.|||Decreased nuclear localization and transcriptional activity upon heat shock.|||Decreased spindle pole localization. Decreased interaction with BTRC. Increased protein stability.|||Decreases MAPK8-induced phosphorylation and does not negatively regulates transactivating activity upon heat shock. No effect on sumoylation.|||Disordered|||Does not change interaction with XRCC5 and XRCC6.|||Does not change interaction with XRCC5 and XRCC6. Decreased nuclear localization upon heat shock. Strongly decreases PLK1-induced phosphorylation. No change in PLK1-induced phosphorylation in mitosis.|||Does not change interaction with XRCC5 and XRCC6. Loss of nuclear stress bodies localization. Decreased nuclear stress bodies localization. Loss of DNA-binding and transcriptional activities upon heat shock.|||Does not change interaction with XRCC5 and XRCC6. No PLK1-induced phosphorylation in mitosis. Inhibits PLK1-stimulated ubiquitinylation. Increased protein stability.|||Does not change interaction with XRCC5 and XRCC6. No change in spindle pole localization. Increases weakly PLK1-stimulated ubiquitinylation. No change in protein stability. Increased interaction with BTRC.|||Does not lead to constitutive DNA-binding activity at 20 degrees Celsius. Leads to weak constitutive DNA-binding and homotrimerization activities at 30 degrees Celsius. Decreased DNA-binding activity at 37 degrees Celsius.|||Does not lead to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Leads to constitutive homotrimerization and DNA-binding activities at 30 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.|||Does not lead to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Loss of DNA-binding activity at 37 degrees Celsius.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heat shock factor protein 1|||Hydrophobic repeat HR-A/B|||Hydrophobic repeat HR-C|||In isoform Short.|||Increased binding HSE and transcriptional activity. Greatly reduced binding to HSP90AA1. No effect on MAPKAPK2 binding.|||Increased nuclear localization and transcriptional activity upon heat shock.|||Induces derepression of transcriptional activity at control temperature.|||Inhibits HSEDNA-binding activity and transcriptional activation.|||Leads to constitutive DNA-binding and homotrimerization activities at 20 degrees Celsius. Does not lead to constitutive transactivation activity at 20 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive DNA-binding and homotrimerization activities at 20 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Decreased DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Does not lead to constitutive transactivation activity at 20 degrees Celsius. Decreased DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Does not lead to constitutive transactivation activity at 20 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. Loss of DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization and DNA-binding activities at 20 degrees Celsius. No effect on DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive homotrimerization, DNA-binding and transactivation activities at 20 degrees Celsius. Decreased DNA-binding activity at 37 degrees Celsius.|||Leads to constitutive transactivation activity at room temperature. Inhibits interaction with YWHAE and increases cytoplasmic localization; when associated with G-303.|||Leads to constitutive transactivation activity at room temperature. Inhibits interaction with YWHAE and increases cytoplasmic localization; when associated with G-307.|||Leads to weak constitutive transactivation activity at room temperature.|||Loss of nuclear stress bodies localization. Loss of DNA-binding and transcriptional activities upon heat shock. No change in homotrimerization upon heat shock.|||Loss of nuclear stress bodies localization. No change in protein abundance.|||Mimics phosphorylation. No effect on in vitro sumoylation. Greatly increased transcriptional activity on heat induction. 5-fold derepression of transcriptional activity at control temperature; when associated with D-307.|||Mimics phosphorylation. No effect on transcriptional activity upon heat shock.|||N-acetylmethionine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-527.|||No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-529.|||No change in nuclear stress bodies localization.|||No change in nuclear stress bodies localization. Increased protein abundance.|||No change in nuclear stress bodies localization. No change in protein abundance.|||No effect neither on repression of transcriptional activity at control temperature nor on transcriptional activation upon heat shock.|||No effect on binding HSE nor on transcriptional activity.|||No effect on repression of transcriptional activity at control temperature.|||No effect on sumoylation.|||No phosphorylation nor sumoylation. No change in nuclear stress granules subcellular location upon heat shock. Loss of colocalization with SUMO1 to nuclear stress granules upon heat shock. Slight decrease in transcriptional activity on heat treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-307.|||No phosphorylation. Does not reduce Ser-303 phosphorylation. 1.5% increase in transcriptional activity on heat-treatment. No change in PLK1-induced phosphorylation in mitosis, induces derepression of transcription activation at control temperature, abolishes sumoylation and induces 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303.|||No phosphorylation. Increased nuclear localization upon heat shock. No effect on oligomerization, DNA-binding activities and nuclear localization. Significant decrease in transcriptional activity by heat shock. Decreases transcriptional activity in a DAXX-dependent manner. Does not change interaction with XRCC5 and XRCC6. Weak decreased PLK1-induced phosphorylation.|||No phosphorylation. No change in PLK1-induced phosphorylation in mitosis. No change in DNA-binding activity upon heat shock. Decreased transcriptional activity upon heat shock.|||Phosphoserine|||Phosphoserine; by CAMK2A|||Phosphoserine; by GSK3-beta|||Phosphoserine; by MAPK12|||Phosphoserine; by MAPK3|||Phosphoserine; by MAPK8|||Phosphoserine; by MAPKAPK2|||Phosphoserine; by PKA|||Phosphoserine; by PLK1|||Phosphothreonine|||Phosphothreonine; by CK2|||Reduced increase in heat-induced transcriptional activity.|||Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2.|||Regulatory domain|||Slight effect on derepression of transcriptional activity at control temperature and on transcriptional activation upon heat shock.|||Some inhibition of binding HSE and transcriptional activity. No change in binding HSP90AA1. Inhibits MAPKAPK2 binding. Decreased HSF1-induced expression of HSPA1A mRNA in a IER5-dependent manner; when associated with D-307; D-314; D-323 and D-367.|||Transactivation domain|||Weak decreased PLK1-induced phosphorylation.|||Weak decreased PLK1-induced phosphorylation. Increased nuclear localization upon heat shock. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000124567|||http://purl.uniprot.org/annotation/VSP_002414|||http://purl.uniprot.org/annotation/VSP_002415
http://togogenome.org/gene/9606:WDR93                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E3E2|||http://purl.uniprot.org/uniprot/Q6P2C0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||WD|||WD repeat-containing protein 93                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319603|||http://purl.uniprot.org/annotation/VAR_039017|||http://purl.uniprot.org/annotation/VAR_039018|||http://purl.uniprot.org/annotation/VAR_039019|||http://purl.uniprot.org/annotation/VSP_031512
http://togogenome.org/gene/9606:MANF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K878|||http://purl.uniprot.org/uniprot/P55145                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  14-fold decrease in secretion.|||ARMET C-terminal|||ARMET N-terminal|||Mesencephalic astrocyte-derived neurotrophic factor|||Phosphotyrosine|||Reduced sulfatide binding and uptake by target cells. Reduces cytoprotective effect of the wild-type protein. Attenuates stress granule formation in response to endoplasmic reticulum stress.|||Two-fold increase in secretion.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002305|||http://purl.uniprot.org/annotation/PRO_5014566187
http://togogenome.org/gene/9606:SYNDIG1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Synapse differentiation-inducing gene protein 1-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332725
http://togogenome.org/gene/9606:CLRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58418                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Clarin-1|||Helical|||In RP61; the mutant protein is retained in the endoplasmic reticulum.|||In USH3A.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065729|||http://purl.uniprot.org/annotation/VAR_012241|||http://purl.uniprot.org/annotation/VAR_012242|||http://purl.uniprot.org/annotation/VAR_030345|||http://purl.uniprot.org/annotation/VAR_030346|||http://purl.uniprot.org/annotation/VAR_053825|||http://purl.uniprot.org/annotation/VAR_054555|||http://purl.uniprot.org/annotation/VAR_054556|||http://purl.uniprot.org/annotation/VAR_066673|||http://purl.uniprot.org/annotation/VAR_066674|||http://purl.uniprot.org/annotation/VAR_071434|||http://purl.uniprot.org/annotation/VSP_022868|||http://purl.uniprot.org/annotation/VSP_022869|||http://purl.uniprot.org/annotation/VSP_043303
http://togogenome.org/gene/9606:NDUFA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z768|||http://purl.uniprot.org/uniprot/P51970                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Initiator Methionine|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CHCH|||CHCH 1|||CHCH 2|||Cx9C motif 1|||Cx9C motif 2|||Cx9C motif 3|||Cx9C motif 4|||Disordered|||In MC1DN37; defect in the assembly of respiratory chain complex I; reduced enzymatic activity of the respiratory chain complex I; altered fibroblast mitochondria morphology and reduced mitochondrial network branching; no significant differences in mitochondrial respiratory capacity.|||In MC1DN37; reduced enzymatic activity of the respiratory chain complex I; reduced NDUFA8 protein levels; decrease in respiratory supercomplexes comprising complex I (CI/CIII 2/CIV and CI/CIII 2) as well as an increase in unintegrated complex III dimers.|||In a breast cancer sample; somatic mutation.|||NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000118734|||http://purl.uniprot.org/annotation/VAR_036176|||http://purl.uniprot.org/annotation/VAR_085554|||http://purl.uniprot.org/annotation/VAR_085555
http://togogenome.org/gene/9606:HOXD12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35452                                                                                  ^@                                                                                  Chain|||DNA Binding|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein Hox-D12|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200238|||http://purl.uniprot.org/annotation/VAR_071211|||http://purl.uniprot.org/annotation/VSP_056816
http://togogenome.org/gene/9606:SOCS6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14544                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Polar residues|||SH2|||SOCS box|||Suppressor of cytokine signaling 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181251
http://togogenome.org/gene/9606:PANK4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVE7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||4'-phosphopantetheine phosphatase|||Does not induce acetyl-CoA production. Restores a moderate increase in acetyl-CoA production; when associated with E-147.|||Does not induce acetyl-CoA production. Restores a moderate increase in acetyl-CoA production; when associated with R-211.|||In a colorectal cancer sample; somatic mutation.|||N-acetylalanine|||Pantothenate kinase|||Phosphoserine|||Phosphothreonine|||Removed|||Subfamily II EGMGR motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161806|||http://purl.uniprot.org/annotation/VAR_015170|||http://purl.uniprot.org/annotation/VAR_027409|||http://purl.uniprot.org/annotation/VAR_035470
http://togogenome.org/gene/9606:TMIGD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2A9|||http://purl.uniprot.org/uniprot/Q96BF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Partial loss of phosphorylation; when associated with F-192 or with F-222.|||Partial loss of phosphorylation; when associated with F-197. Complete loss of phosphorylation; when associated with F-222.|||Partial loss of phosphorylation; when tested individually or when associated with F-197. Complete loss of phosphorylation; when associated with F-192.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||Transmembrane and immunoglobulin domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000275870|||http://purl.uniprot.org/annotation/VAR_030469|||http://purl.uniprot.org/annotation/VAR_061328|||http://purl.uniprot.org/annotation/VSP_022967
http://togogenome.org/gene/9606:ADA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z381|||http://purl.uniprot.org/uniprot/F5GWI4|||http://purl.uniprot.org/uniprot/P00813                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Adenosine deaminase|||Allele ADA*2; found in about 10% of the population; affects duration and intensity of deep sleep; enhances negative effects of sleep loss during sleep deprivation; may have a protective role against male infertility; 20% to 30% decrease in activity.|||Decreases enzyme activity by reducing maximum velocity; reduces ADORA1 modulation.|||Decreases enzyme activity by reducing maximum velocity; reduces ADORA2A modulation.|||Decreases enzyme activity by reducing substrate affinity and maximum velocity.|||Decreases enzyme activity by reducing substrate affinity and maximum velocity; abolishes ADORA1 and ADORA2A modulator function.|||Decreases enzyme activity by reducing substrate affinity and maximum velocity; reduces ADORA1 and ADORA2A modulation.|||Important for catalytic activity|||Important for interaction with adenosine receptors and increasing their affinity for agonists|||In ADASCID.|||In ADASCID; 8% of activity.|||In ADASCID; delayed-onset.|||In ADASCID; late onset; 4% of activity.|||In ADASCID; loss of activity.|||In ADASCID; severe.|||In ADASCID; unknown pathological significance; 30% of activity; total loss of activity; when associated with C-97.|||In ADASCID; unknown pathological significance; loss of activity on its own; total loss of activity; when associated with V-106.|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In an individual with partial ADA deficiency but no immunodeficiency; 1,5% of activity.|||In an individual with partial ADA deficiency but no immunodeficiency; 20% of activity.|||Moderately reduces enzyme activity.|||Moderately reduces enzyme activity; no change in ADORA1 and ADORA2A modulation.|||Moderately reduces enzyme activity; reduces ADORA1 and ADORA2A modulation.|||N-acetylalanine|||N6-acetyllysine|||No change in enzyme activity.|||No change in enzyme activity; no change in ADORA1 and ADORA2A modulation.|||Proton donor|||Removed|||Required for binding to DDP4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194352|||http://purl.uniprot.org/annotation/VAR_002209|||http://purl.uniprot.org/annotation/VAR_002210|||http://purl.uniprot.org/annotation/VAR_002211|||http://purl.uniprot.org/annotation/VAR_002212|||http://purl.uniprot.org/annotation/VAR_002213|||http://purl.uniprot.org/annotation/VAR_002214|||http://purl.uniprot.org/annotation/VAR_002215|||http://purl.uniprot.org/annotation/VAR_002216|||http://purl.uniprot.org/annotation/VAR_002217|||http://purl.uniprot.org/annotation/VAR_002218|||http://purl.uniprot.org/annotation/VAR_002219|||http://purl.uniprot.org/annotation/VAR_002220|||http://purl.uniprot.org/annotation/VAR_002221|||http://purl.uniprot.org/annotation/VAR_002222|||http://purl.uniprot.org/annotation/VAR_002223|||http://purl.uniprot.org/annotation/VAR_002224|||http://purl.uniprot.org/annotation/VAR_002225|||http://purl.uniprot.org/annotation/VAR_002226|||http://purl.uniprot.org/annotation/VAR_002227|||http://purl.uniprot.org/annotation/VAR_002228|||http://purl.uniprot.org/annotation/VAR_002229|||http://purl.uniprot.org/annotation/VAR_002230|||http://purl.uniprot.org/annotation/VAR_002231|||http://purl.uniprot.org/annotation/VAR_002232|||http://purl.uniprot.org/annotation/VAR_002233|||http://purl.uniprot.org/annotation/VAR_002234|||http://purl.uniprot.org/annotation/VAR_002235|||http://purl.uniprot.org/annotation/VAR_002236|||http://purl.uniprot.org/annotation/VAR_002237|||http://purl.uniprot.org/annotation/VAR_002238|||http://purl.uniprot.org/annotation/VAR_002239|||http://purl.uniprot.org/annotation/VAR_002240|||http://purl.uniprot.org/annotation/VAR_002241|||http://purl.uniprot.org/annotation/VAR_076954|||http://purl.uniprot.org/annotation/VAR_076955
http://togogenome.org/gene/9606:HADHB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F5GZQ3|||http://purl.uniprot.org/uniprot/P55084                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||INTRAMEM|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Acyl-thioester intermediate|||In MTPD2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||Increases nucleophilicity of active site Cys|||Mitochondrion|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate|||Proton donor/acceptor|||Thiolase C-terminal|||Thiolase N-terminal|||Trifunctional enzyme subunit beta, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034080|||http://purl.uniprot.org/annotation/VAR_007493|||http://purl.uniprot.org/annotation/VAR_007494|||http://purl.uniprot.org/annotation/VAR_007495|||http://purl.uniprot.org/annotation/VAR_017409|||http://purl.uniprot.org/annotation/VAR_021128|||http://purl.uniprot.org/annotation/VAR_021129|||http://purl.uniprot.org/annotation/VAR_021130|||http://purl.uniprot.org/annotation/VAR_021131|||http://purl.uniprot.org/annotation/VAR_021132|||http://purl.uniprot.org/annotation/VAR_021133|||http://purl.uniprot.org/annotation/VAR_021134|||http://purl.uniprot.org/annotation/VAR_021135|||http://purl.uniprot.org/annotation/VAR_021136|||http://purl.uniprot.org/annotation/VAR_021137|||http://purl.uniprot.org/annotation/VAR_021138|||http://purl.uniprot.org/annotation/VAR_028231|||http://purl.uniprot.org/annotation/VAR_035705|||http://purl.uniprot.org/annotation/VAR_061897|||http://purl.uniprot.org/annotation/VSP_054426
http://togogenome.org/gene/9606:KLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07288|||http://purl.uniprot.org/uniprot/Q546G3                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Prostate-specific antigen                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027931|||http://purl.uniprot.org/annotation/PRO_0000027932|||http://purl.uniprot.org/annotation/PRO_5014309586|||http://purl.uniprot.org/annotation/VAR_021941|||http://purl.uniprot.org/annotation/VAR_021942|||http://purl.uniprot.org/annotation/VAR_051852|||http://purl.uniprot.org/annotation/VSP_045786|||http://purl.uniprot.org/annotation/VSP_046169|||http://purl.uniprot.org/annotation/VSP_046170|||http://purl.uniprot.org/annotation/VSP_046171|||http://purl.uniprot.org/annotation/VSP_047643
http://togogenome.org/gene/9606:ATOH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92858                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Pro residues|||Transcription factor ATOH1|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127139|||http://purl.uniprot.org/annotation/VAR_049539
http://togogenome.org/gene/9606:MXRA8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRK3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Matrix remodeling-associated protein 8|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by FAM20C|||RGD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298665|||http://purl.uniprot.org/annotation/VAR_070893|||http://purl.uniprot.org/annotation/VSP_027448|||http://purl.uniprot.org/annotation/VSP_027449|||http://purl.uniprot.org/annotation/VSP_054528|||http://purl.uniprot.org/annotation/VSP_054529
http://togogenome.org/gene/9606:TCEAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15170                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In NEDGFAX.|||In NEDGFAX; unknown pathological significance.|||Loss of transcriptional repression.|||No effect on transcriptional repression.|||Phosphoserine|||Transcription elongation factor A protein-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239203|||http://purl.uniprot.org/annotation/VAR_057270|||http://purl.uniprot.org/annotation/VAR_087930|||http://purl.uniprot.org/annotation/VAR_087931|||http://purl.uniprot.org/annotation/VAR_087932|||http://purl.uniprot.org/annotation/VAR_087933
http://togogenome.org/gene/9606:HSD17B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQS7|||http://purl.uniprot.org/uniprot/P14061                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  17-beta-hydroxysteroid dehydrogenase type 1|||Abolishes phosphorylation. No effect on 17-beta-hydroxysteroid dehydrogenase activity.|||Alters substrate specificity.|||Disordered|||Loss of 17-beta-hydroxysteroid dehydrogenase activity.|||No effect on conversion of estrone to 17beta-estradiol.|||Phosphoserine; by PKA|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054567|||http://purl.uniprot.org/annotation/VAR_006951|||http://purl.uniprot.org/annotation/VAR_006952
http://togogenome.org/gene/9606:SC5D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75845                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Fatty acid hydroxylase|||Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||In LATHOS.|||Lathosterol oxidase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000117028|||http://purl.uniprot.org/annotation/VAR_014423|||http://purl.uniprot.org/annotation/VAR_014424|||http://purl.uniprot.org/annotation/VAR_020829
http://togogenome.org/gene/9606:NUDT16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96DE0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2 and isoform 4.|||In isoform 2.|||In isoform 3.|||Nudix box|||Nudix hydrolase|||U8 snoRNA-decapping enzyme                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057117|||http://purl.uniprot.org/annotation/VSP_045449|||http://purl.uniprot.org/annotation/VSP_045450|||http://purl.uniprot.org/annotation/VSP_045451|||http://purl.uniprot.org/annotation/VSP_045452
http://togogenome.org/gene/9606:MAP2K4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P45985                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine; alternate|||Cleavage; by anthrax lethal factor|||D domain|||DVD domain|||Disordered|||Dual specificity mitogen-activated protein kinase kinase 4|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung squamous cell carcinoma sample; somatic mutation.|||In a metastatic melanoma sample; somatic mutation.|||In an ovarian serous carcinoma sample; somatic mutation.|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by MAP3K|||Phosphothreonine; by MAP3K|||Protein kinase|||Proton acceptor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086381|||http://purl.uniprot.org/annotation/VAR_040818|||http://purl.uniprot.org/annotation/VAR_040819|||http://purl.uniprot.org/annotation/VAR_040820|||http://purl.uniprot.org/annotation/VAR_040821|||http://purl.uniprot.org/annotation/VAR_040822|||http://purl.uniprot.org/annotation/VAR_062963|||http://purl.uniprot.org/annotation/VSP_038838
http://togogenome.org/gene/9606:GNAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1Y9|||http://purl.uniprot.org/uniprot/P38405                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(olf) subunit alpha|||In DYT25.|||In DYT25; loss of function mutation.|||In isoform 2.|||In isoform 3.|||N-palmitoyl glycine|||Phosphothreonine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203732|||http://purl.uniprot.org/annotation/VAR_069329|||http://purl.uniprot.org/annotation/VAR_069330|||http://purl.uniprot.org/annotation/VAR_069331|||http://purl.uniprot.org/annotation/VAR_069332|||http://purl.uniprot.org/annotation/VSP_043050|||http://purl.uniprot.org/annotation/VSP_045130
http://togogenome.org/gene/9606:DEPTOR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB45                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  BetaTrCP degron motif|||DDEX motif|||DEP 1|||DEP 2|||DEP domain-containing mTOR-interacting protein|||Decreased phosphatidic acid-binding.|||Decreased phosphorylation, leading to impaired deubiquitination by USP7.|||Decreased phosphorylation, leading to increased interaction with MTOR.|||Disordered|||Does not affect phosphorylation.|||In isoform 2.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-297 and A-298.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-297 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-297, A-298 and A-299. Reduced ubiquitination by the SCF(BTRC) complex.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-293, A-297, A-298 and A-299. Reduced ubiquitination by the SCF(BTRC) complex.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-282, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-265, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-263, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-259, A-265, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-258, A-263, A-265, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-244, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-241, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||In mutant 13A; abolished phosphorylation, leading to promote interaction with MTOR without affecting ability to bind phosphatidic acid; when associated with A-244, A-258, A-259, A-263, A-265, A-282, A-283, A-287, A-293, A-297, A-298 and A-299.|||Mimics phosphorylation, leading to slightly decreased interaction with MTOR.|||Mimics phosphorylation, leading to slightly increased stability.|||Mimics phosphorylation; promoting association with the SCF(BTRC) complex.|||N-acetylmethionine|||PDZ|||Phosphoserine|||Phosphoserine; by CK1|||Phosphoserine; by MAPK3|||Phosphoserine; by MTOR|||Phosphothreonine|||Phosphothreonine; by MTOR|||Phosphotyrosine; by SYK|||Polar residues|||Reduced ubiquitination by the SCF(BTRC) complex. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284784|||http://purl.uniprot.org/annotation/VAR_031816|||http://purl.uniprot.org/annotation/VAR_031817|||http://purl.uniprot.org/annotation/VAR_031818|||http://purl.uniprot.org/annotation/VSP_054681
http://togogenome.org/gene/9606:SLC6A15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T8I1|||http://purl.uniprot.org/uniprot/Q8IXG2|||http://purl.uniprot.org/uniprot/Q9H2J7|||http://purl.uniprot.org/uniprot/Q9NW50                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sodium-dependent neutral amino acid transporter B(0)AT2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000214798|||http://purl.uniprot.org/annotation/VAR_052065|||http://purl.uniprot.org/annotation/VAR_052066|||http://purl.uniprot.org/annotation/VSP_043030|||http://purl.uniprot.org/annotation/VSP_043031|||http://purl.uniprot.org/annotation/VSP_045192
http://togogenome.org/gene/9606:POC1B-GALNT4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VUJ3|||http://purl.uniprot.org/uniprot/Q8N4A0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC.|||Basic and acidic residues|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interaction with glycopeptide substrate|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 4|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059108|||http://purl.uniprot.org/annotation/VAR_019576|||http://purl.uniprot.org/annotation/VAR_019577|||http://purl.uniprot.org/annotation/VAR_065257|||http://purl.uniprot.org/annotation/VSP_045009|||http://purl.uniprot.org/annotation/VSP_045010
http://togogenome.org/gene/9606:CRISPLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z8V9|||http://purl.uniprot.org/uniprot/Q9H336                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine-rich secretory protein LCCL domain-containing 1|||Disordered|||In isoform 2.|||LCCL|||LCCL 1|||LCCL 2|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000248146|||http://purl.uniprot.org/annotation/VAR_027255|||http://purl.uniprot.org/annotation/VSP_055281|||http://purl.uniprot.org/annotation/VSP_055282
http://togogenome.org/gene/9606:TVP23C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96ET8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Golgi apparatus membrane protein TVP23 homolog C|||Helical|||In isoform 2.|||In isoform 3.|||N-acetylmethionine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212831|||http://purl.uniprot.org/annotation/VAR_024929|||http://purl.uniprot.org/annotation/VAR_055797|||http://purl.uniprot.org/annotation/VSP_017019|||http://purl.uniprot.org/annotation/VSP_017020|||http://purl.uniprot.org/annotation/VSP_040556|||http://purl.uniprot.org/annotation/VSP_040557
http://togogenome.org/gene/9606:CACHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQY7|||http://purl.uniprot.org/uniprot/Q5VU97                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cache 1|||Cache 2|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA|||VWFA and cache domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304661|||http://purl.uniprot.org/annotation/VAR_035052|||http://purl.uniprot.org/annotation/VSP_028072
http://togogenome.org/gene/9606:ERV3-1-ZNF117                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q03924                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11; degenerate|||C2H2-type 12|||C2H2-type 13|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Zinc finger protein 117                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047407|||http://purl.uniprot.org/annotation/VAR_057396|||http://purl.uniprot.org/annotation/VAR_057397
http://togogenome.org/gene/9606:TNFRSF13B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14836|||http://purl.uniprot.org/uniprot/Q4ACX1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Helical|||Helical; Signal-anchor for type III membrane protein|||In CVID2 and IGAD2.|||In CVID2.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||TACI cysteine-rich|||TNFR-Cys 1|||TNFR-Cys 2|||Tumor necrosis factor receptor superfamily member 13B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058931|||http://purl.uniprot.org/annotation/VAR_024027|||http://purl.uniprot.org/annotation/VAR_024028|||http://purl.uniprot.org/annotation/VAR_024029|||http://purl.uniprot.org/annotation/VAR_052353|||http://purl.uniprot.org/annotation/VAR_064758|||http://purl.uniprot.org/annotation/VSP_013798|||http://purl.uniprot.org/annotation/VSP_054184|||http://purl.uniprot.org/annotation/VSP_054185
http://togogenome.org/gene/9606:TEX38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZLT1|||http://purl.uniprot.org/uniprot/B7ZLT2|||http://purl.uniprot.org/uniprot/C9W8M6|||http://purl.uniprot.org/uniprot/Q6PEX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Polar residues|||Testis-expressed protein 38                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322538|||http://purl.uniprot.org/annotation/VAR_039405|||http://purl.uniprot.org/annotation/VAR_039406
http://togogenome.org/gene/9606:NFATC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K9C6|||http://purl.uniprot.org/uniprot/B4DER8|||http://purl.uniprot.org/uniprot/F5H4S8|||http://purl.uniprot.org/uniprot/O95644                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||3 X SP repeats|||Calcineurin-binding|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform A-alpha'.|||In isoform A-alpha, isoform A-alpha' and isoform A-beta.|||In isoform A-beta, isoform B-beta, isoform C-beta and isoform IB-deltaIX.|||In isoform B-alpha, isoform B-beta and isoform 10.|||In isoform IA-deltaIX and isoform IB-deltaIX.|||No effect on subcellular localization.|||Nuclear export signal|||Nuclear factor of activated T-cells, cytoplasmic 1|||Nuclear localization signal|||Partial nuclear translocation.|||Phosphoserine|||Phosphoserine; by PKA|||Polar residues|||Pro residues|||RHD|||Transactivation domain A (TAD-A)|||Transactivation domain B (TAD-B)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030329|||http://purl.uniprot.org/annotation/VAR_036529|||http://purl.uniprot.org/annotation/VAR_057145|||http://purl.uniprot.org/annotation/VAR_057146|||http://purl.uniprot.org/annotation/VSP_005590|||http://purl.uniprot.org/annotation/VSP_005591|||http://purl.uniprot.org/annotation/VSP_005592|||http://purl.uniprot.org/annotation/VSP_005593|||http://purl.uniprot.org/annotation/VSP_018978|||http://purl.uniprot.org/annotation/VSP_047820|||http://purl.uniprot.org/annotation/VSP_053806
http://togogenome.org/gene/9606:DNAJC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KC8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||DnaJ homolog subfamily C member 1|||Helical|||J|||Lumenal|||Phosphoserine|||Polar residues|||SANT 1|||SANT 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071042
http://togogenome.org/gene/9606:IL31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6EBC2                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Signal Peptide                                                                                  ^@                                                                                  Interleukin-31|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274570
http://togogenome.org/gene/9606:DOP1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RWN9|||http://purl.uniprot.org/uniprot/Q5JWR5|||http://purl.uniprot.org/uniprot/Q5TA12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Dopey N-terminal|||In a breast cancer sample; somatic mutation.|||Phosphoserine|||Polar residues|||Protein dopey-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297947|||http://purl.uniprot.org/annotation/VAR_034690|||http://purl.uniprot.org/annotation/VAR_034691|||http://purl.uniprot.org/annotation/VAR_036607
http://togogenome.org/gene/9606:LCE3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5A8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 3C|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235335
http://togogenome.org/gene/9606:RAD54B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95073|||http://purl.uniprot.org/uniprot/Q9Y620                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEGH box|||DNA repair and recombination protein RAD54B|||Disordered|||Fibrinogen silencer-binding protein|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||In a colon cancer sample.|||In a non-Hodgkin lymphoma sample.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074340|||http://purl.uniprot.org/annotation/PRO_0000087352|||http://purl.uniprot.org/annotation/VAR_019301|||http://purl.uniprot.org/annotation/VAR_019563|||http://purl.uniprot.org/annotation/VAR_019564|||http://purl.uniprot.org/annotation/VAR_034430|||http://purl.uniprot.org/annotation/VAR_037885|||http://purl.uniprot.org/annotation/VAR_075089|||http://purl.uniprot.org/annotation/VAR_075090|||http://purl.uniprot.org/annotation/VSP_010774|||http://purl.uniprot.org/annotation/VSP_045956|||http://purl.uniprot.org/annotation/VSP_045957
http://togogenome.org/gene/9606:NOP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KA74|||http://purl.uniprot.org/uniprot/P78316                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleolar protein 14|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137155|||http://purl.uniprot.org/annotation/VAR_053540|||http://purl.uniprot.org/annotation/VAR_060075|||http://purl.uniprot.org/annotation/VSP_018021|||http://purl.uniprot.org/annotation/VSP_018022
http://togogenome.org/gene/9606:OR13H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GW70|||http://purl.uniprot.org/uniprot/Q8NG92                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 13H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150740|||http://purl.uniprot.org/annotation/VAR_034312
http://togogenome.org/gene/9606:OR52N1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH53                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52N1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150786|||http://purl.uniprot.org/annotation/VAR_024149|||http://purl.uniprot.org/annotation/VAR_034351|||http://purl.uniprot.org/annotation/VAR_053335|||http://purl.uniprot.org/annotation/VAR_053336|||http://purl.uniprot.org/annotation/VAR_053337
http://togogenome.org/gene/9606:WSB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||SOCS box|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat and SOCS box-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051460|||http://purl.uniprot.org/annotation/VSP_054016|||http://purl.uniprot.org/annotation/VSP_054576
http://togogenome.org/gene/9606:SRRM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WXA3                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||CWF21|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:CNMD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75829                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  BRICHOS|||Chondromodulin-1|||Chondrosurfactant protein|||Disordered|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005346|||http://purl.uniprot.org/annotation/PRO_0000005347|||http://purl.uniprot.org/annotation/PRO_0000005348|||http://purl.uniprot.org/annotation/VAR_024413|||http://purl.uniprot.org/annotation/VAR_048719|||http://purl.uniprot.org/annotation/VSP_038380
http://togogenome.org/gene/9606:TRIM25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14258                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Almost complete loss of ZAP/ZC3HAV1 ubiquitination; when associated with S-50.|||Almost complete loss of ZAP/ZC3HAV1 ubiquitination; when associated with S-53.|||Almost complete loss of ubiquitination activity.|||B30.2/SPRY|||Basic and acidic residues|||Complete loss of viral inhibition independently of the host interferon response.|||Disordered|||E3 ubiquitin/ISG15 ligase TRIM25|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)|||Interaction with influenza A virus NS1|||N6-acetyllysine|||No ISGylation.|||No effect on ISGylation.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056233|||http://purl.uniprot.org/annotation/VAR_024614|||http://purl.uniprot.org/annotation/VAR_024615
http://togogenome.org/gene/9606:AKT1S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B36                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolished ability to inhibit the kinase activity of MTOR.|||Abolished association with the MTORC1 complex. Does not affect phosphorylatiuon by MTOR.|||Decreased interaction with 14-3-3; increased inhibitory activity toward mTORC1.|||Disordered|||Does not affect phosphorylation by MTOR.|||In isoform 2.|||In isoform 3.|||Mimics phosphorylation; reduced interaction with RPTOR.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine; by PKB/AKT1 and DYRK3|||Pro residues|||Proline-rich AKT1 substrate 1|||Reduced phosphorylation by MTOR.|||Suppresses RPS6KB1 phosphorylation by mTORC1.|||TOS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253446|||http://purl.uniprot.org/annotation/VAR_028239|||http://purl.uniprot.org/annotation/VSP_047536|||http://purl.uniprot.org/annotation/VSP_052182
http://togogenome.org/gene/9606:UBA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22314                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1-1|||1-2|||2 approximate repeats|||Disordered|||Glycyl thioester intermediate|||In SMAX2.|||In VEXAS; somatic mutation; does not affect ubiquitin activating enzyme activity; does not affect subcellular localization; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity.|||In VEXAS; somatic mutation; the underlying nucleotide substitution affects normal alternative translation initiation and leads to aberrant initiation from M-67 to produce a shorter protein with strongly reduced enzymatic activity.|||In isoform 2.|||Localizes to the cytoplasm.|||Localizes to the cytoplasm; when associated with A-67.|||Localizes to the nucleus; when associated with A-41. Localizes to the cytoplasm; when associated with 1-M--G-40 del.|||Localizes to the nucleus; when associated with A-67.|||Loss of nuclear localization and a 90-95% decrease in the phosphorylation.|||N-acetylalanine|||N-acetylserine|||N6-acetyllysine|||N6-succinyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Reduces phosphorylation.|||Removed|||Ubiquitin-like modifier-activating enzyme 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194934|||http://purl.uniprot.org/annotation/VAR_043500|||http://purl.uniprot.org/annotation/VAR_043501|||http://purl.uniprot.org/annotation/VAR_043502|||http://purl.uniprot.org/annotation/VAR_071121|||http://purl.uniprot.org/annotation/VAR_085160|||http://purl.uniprot.org/annotation/VAR_085161|||http://purl.uniprot.org/annotation/VAR_085162|||http://purl.uniprot.org/annotation/VSP_055913
http://togogenome.org/gene/9606:LGALS14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCE9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Galectin|||In isoform 2.|||Placental protein 13-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076964|||http://purl.uniprot.org/annotation/VAR_055245|||http://purl.uniprot.org/annotation/VAR_055246|||http://purl.uniprot.org/annotation/VSP_047067
http://togogenome.org/gene/9606:KIF5C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60282|||http://purl.uniprot.org/uniprot/Q59GB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Globular|||In CDCBM2; the mutant protein has a complete loss of ATP hydrolysis activity; colocalizes with microtubules throughout the cell but does not appear as puncta or accumulates in cortical clusters as does the wild-type protein.|||In CDCBM2; the mutation results in a significant decrease of excitatory post-synaptic currents when expressed in cultured primary hippocampal neurons; decreased localization to distal regions of dendrites; accumulates in dendrite cell body.|||In isoform 2.|||Kinesin heavy chain isoform 5C|||Kinesin motor|||Microtubule-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125355|||http://purl.uniprot.org/annotation/VAR_069389|||http://purl.uniprot.org/annotation/VAR_070574|||http://purl.uniprot.org/annotation/VSP_035715|||http://purl.uniprot.org/annotation/VSP_035716
http://togogenome.org/gene/9606:LEPROTL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95214|||http://purl.uniprot.org/uniprot/Q6FHL7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform 2.|||Leptin receptor overlapping transcript-like 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215197|||http://purl.uniprot.org/annotation/VSP_046307
http://togogenome.org/gene/9606:FNBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3X1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Formin-binding protein 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Rare variant found in a patient with microphthalmia with limb anomalies; unknown pathological significance.|||WW 1|||WW 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289863|||http://purl.uniprot.org/annotation/VAR_032623|||http://purl.uniprot.org/annotation/VAR_032624|||http://purl.uniprot.org/annotation/VAR_075345|||http://purl.uniprot.org/annotation/VSP_040292
http://togogenome.org/gene/9606:PRKCSH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJQ5|||http://purl.uniprot.org/uniprot/K7ELL7|||http://purl.uniprot.org/uniprot/P14314                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||Glucosidase 2 subunit beta|||In PCLD1.|||In isoform 2.|||LDL-receptor class A 1|||LDL-receptor class A 2|||MRH|||N-linked (GlcNAc...) asparagine|||N6-succinyllysine|||Phosphoserine; by FAM20C|||Phosphoserine; by PKC|||Prevents secretion from ER|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004143|||http://purl.uniprot.org/annotation/VAR_028761|||http://purl.uniprot.org/annotation/VAR_028762|||http://purl.uniprot.org/annotation/VAR_048658|||http://purl.uniprot.org/annotation/VAR_080939|||http://purl.uniprot.org/annotation/VAR_080940|||http://purl.uniprot.org/annotation/VAR_080941|||http://purl.uniprot.org/annotation/VAR_080942|||http://purl.uniprot.org/annotation/VAR_080943|||http://purl.uniprot.org/annotation/VSP_043749
http://togogenome.org/gene/9606:OR6F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV68|||http://purl.uniprot.org/uniprot/Q8NGZ6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6F1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150627|||http://purl.uniprot.org/annotation/VAR_034247|||http://purl.uniprot.org/annotation/VAR_053221|||http://purl.uniprot.org/annotation/VAR_062051
http://togogenome.org/gene/9606:TGFBRAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUH2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CHCR|||CNH|||Transforming growth factor-beta receptor-associated protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345405|||http://purl.uniprot.org/annotation/VAR_045822
http://togogenome.org/gene/9606:PNPO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVS9|||http://purl.uniprot.org/uniprot/V9HW45                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Has no effect on the catalytic activity.|||In PNPOD.|||In PNPOD; strong activity decrease.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of catalytic activity.|||Phosphoserine|||Phosphothreonine|||Pyridoxamine 5'-phosphate oxidase putative|||Pyridoxine 5'-phosphate oxidase dimerisation C-terminal|||Pyridoxine-5'-phosphate oxidase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167783|||http://purl.uniprot.org/annotation/VAR_029358|||http://purl.uniprot.org/annotation/VAR_029359|||http://purl.uniprot.org/annotation/VAR_029360|||http://purl.uniprot.org/annotation/VAR_078229|||http://purl.uniprot.org/annotation/VAR_078643|||http://purl.uniprot.org/annotation/VSP_056410|||http://purl.uniprot.org/annotation/VSP_056411|||http://purl.uniprot.org/annotation/VSP_058769|||http://purl.uniprot.org/annotation/VSP_058770
http://togogenome.org/gene/9606:PLPPR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2D5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Found in a patient with infantile epileptic spasms also carrying a SCN1A variant; unknown pathological significance.|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Phospholipid phosphatase-related protein type 4|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317436|||http://purl.uniprot.org/annotation/VAR_050618|||http://purl.uniprot.org/annotation/VAR_050619|||http://purl.uniprot.org/annotation/VAR_085196|||http://purl.uniprot.org/annotation/VAR_088174|||http://purl.uniprot.org/annotation/VSP_030950|||http://purl.uniprot.org/annotation/VSP_030951|||http://purl.uniprot.org/annotation/VSP_046784
http://togogenome.org/gene/9606:TCP11L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4U5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Phosphoserine|||Polar residues|||T-complex protein 11-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313750|||http://purl.uniprot.org/annotation/VAR_037728|||http://purl.uniprot.org/annotation/VAR_037729|||http://purl.uniprot.org/annotation/VAR_037730|||http://purl.uniprot.org/annotation/VSP_055736|||http://purl.uniprot.org/annotation/VSP_055737
http://togogenome.org/gene/9606:METTL21C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VZV1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes methyltransferase activity.|||Disordered|||Protein-lysine methyltransferase METTL21C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319590|||http://purl.uniprot.org/annotation/VAR_039013|||http://purl.uniprot.org/annotation/VAR_062229
http://togogenome.org/gene/9606:RFXANK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7P0|||http://purl.uniprot.org/uniprot/O14593                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||DNA-binding protein RFXANK|||Disordered|||In BLS2; loss of expression.|||In isoform 2 and isoform 3.|||In isoform 2.|||Loss of expression.|||Loss of interaction with RFX5.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067049|||http://purl.uniprot.org/annotation/VAR_009941|||http://purl.uniprot.org/annotation/VAR_014472|||http://purl.uniprot.org/annotation/VAR_048311|||http://purl.uniprot.org/annotation/VSP_000283|||http://purl.uniprot.org/annotation/VSP_000284|||http://purl.uniprot.org/annotation/VSP_054618
http://togogenome.org/gene/9606:CHTF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVB6                                                                                  ^@                                                                                  Binding Site|||Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chromosome transmission fidelity protein 18 homolog|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340081|||http://purl.uniprot.org/annotation/VAR_043990|||http://purl.uniprot.org/annotation/VAR_043991|||http://purl.uniprot.org/annotation/VAR_043992|||http://purl.uniprot.org/annotation/VAR_043993|||http://purl.uniprot.org/annotation/VAR_043994|||http://purl.uniprot.org/annotation/VSP_034179|||http://purl.uniprot.org/annotation/VSP_034180
http://togogenome.org/gene/9606:BCAS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05D99|||http://purl.uniprot.org/uniprot/Q9H6U6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Almost abolishes recruitment to preautophagosomal structure in response to mitophagy. No effect on interaction with PHAF1.|||BCAS3 microtubule associated cell migration factor|||Breakpoint for translocation to form BCAS4-BCAS3|||Decreases recruitment to preautophagosomal structure in response to mitophagy. No effect on interaction with PHAF1.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In HEMARS.|||In HEMARS; no protein detected in patient cells that also carry L-567, suggesting the mutant is unstable.|||In HEMARS; no protein detected in patient cells that also carry R-577, suggesting the mutant is unstable.|||In isoform 1, isoform 3, isoform 5 and isoform 6.|||In isoform 3 and isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||No effect on recruitment to preautophagosomal structure in response to mitophagy. No effect on interaction with PHAF1.|||Phosphoserine|||Polar residues|||Required for recruitment to preautophagosomal structure in response to mitophagy|||WD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050883|||http://purl.uniprot.org/annotation/VAR_057583|||http://purl.uniprot.org/annotation/VAR_065093|||http://purl.uniprot.org/annotation/VAR_086504|||http://purl.uniprot.org/annotation/VAR_086505|||http://purl.uniprot.org/annotation/VAR_086506|||http://purl.uniprot.org/annotation/VAR_086507|||http://purl.uniprot.org/annotation/VAR_086508|||http://purl.uniprot.org/annotation/VAR_086509|||http://purl.uniprot.org/annotation/VAR_086510|||http://purl.uniprot.org/annotation/VAR_086511|||http://purl.uniprot.org/annotation/VSP_007858|||http://purl.uniprot.org/annotation/VSP_007860|||http://purl.uniprot.org/annotation/VSP_040112|||http://purl.uniprot.org/annotation/VSP_040113
http://togogenome.org/gene/9606:ENPP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UWR7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated serine|||Glycerophosphocholine cholinephosphodiesterase ENPP6|||Interchain|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Phosphoserine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239361|||http://purl.uniprot.org/annotation/PRO_0000420890|||http://purl.uniprot.org/annotation/VAR_026644|||http://purl.uniprot.org/annotation/VAR_052942
http://togogenome.org/gene/9606:GOLGA6C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDK9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Golgin subfamily A member 6C|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000332249
http://togogenome.org/gene/9606:SAPCD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UD0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Phosphoserine|||Phosphothreonine|||Pro residues|||Suppressor APC domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286596
http://togogenome.org/gene/9606:CYP2A6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11509                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 2A6|||In allele CYP2A6*13.|||In allele CYP2A6*14.|||In allele CYP2A6*15.|||In allele CYP2A6*16.|||In allele CYP2A6*17; increases phenacetin O-deethylation activity 2 fold.|||In allele CYP2A6*23; greatly reduced activity toward nicotine C-oxidation as well as reduced coumarin 7-hydroxylation.|||In allele CYP2A6*24.|||In allele CYP2A6*24; increases phenacetin O-deethylation activity 4 fold.|||In allele CYP2A6*25 and allele CYP2A6*26.|||In allele CYP2A6*26.|||In allele CYP2A6*28.|||In allele CYP2A6*2; unable to catalyze 7-hydroxylation of coumarin; causes switching from coumarin 7-hydroxylation to 3-hydroxylation.|||In allele CYP2A6*5; loss of activity.|||In allele CYP2A6*6; loss of activity.|||In allele CYP2A6*7.|||In allele CYP2A6*8.|||Increases phenacetin O-deethylation activity 10 fold; when associated with F-300 and A-301. Increases phenacetin O-deethylation activity 38 fold; when associated with F-300; A-301 and G-369.|||Increases phenacetin O-deethylation activity 2 fold.|||Increases phenacetin O-deethylation activity 3 fold. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; F-300 and A-301.|||Increases phenacetin O-deethylation activity 3 fold. Increases phenacetin O-deethylation activity 8 fold; when associated with A-301. Increases phenacetin O-deethylation activity 10 fold; when associated with S-208 and A-301. Increases phenacetin O-deethylation activity 12 fold; when associated with A-301 and G-369. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; A-301 and G-369.|||No effect on phenacetin O-deethylation activity.|||Slightly decreases phenacetin O-deethylation activity. Increases phenacetin O-deethylation activity 8 fold; when associated with F-300. Increases phenacetin O-deethylation activity 10 fold; when associated with S-208 and F-300. Increases phenacetin O-deethylation activity 12 fold; when associated with F-300 and G-369. Increases phenacetin O-deethylation activity 38 fold; when associated with S-208; F-300 and G-369.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051668|||http://purl.uniprot.org/annotation/VAR_001249|||http://purl.uniprot.org/annotation/VAR_008356|||http://purl.uniprot.org/annotation/VAR_011577|||http://purl.uniprot.org/annotation/VAR_011578|||http://purl.uniprot.org/annotation/VAR_011579|||http://purl.uniprot.org/annotation/VAR_018330|||http://purl.uniprot.org/annotation/VAR_018331|||http://purl.uniprot.org/annotation/VAR_018332|||http://purl.uniprot.org/annotation/VAR_018333|||http://purl.uniprot.org/annotation/VAR_018375|||http://purl.uniprot.org/annotation/VAR_024711|||http://purl.uniprot.org/annotation/VAR_024712|||http://purl.uniprot.org/annotation/VAR_024713|||http://purl.uniprot.org/annotation/VAR_024714|||http://purl.uniprot.org/annotation/VAR_024715|||http://purl.uniprot.org/annotation/VAR_048448|||http://purl.uniprot.org/annotation/VAR_055033|||http://purl.uniprot.org/annotation/VAR_055034|||http://purl.uniprot.org/annotation/VAR_055035|||http://purl.uniprot.org/annotation/VAR_055036|||http://purl.uniprot.org/annotation/VAR_055037|||http://purl.uniprot.org/annotation/VAR_055038|||http://purl.uniprot.org/annotation/VAR_059149
http://togogenome.org/gene/9606:CMKLR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46091                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chemerin-like receptor 2|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069505|||http://purl.uniprot.org/annotation/VAR_023839
http://togogenome.org/gene/9606:MTMR10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXD2|||http://purl.uniprot.org/uniprot/X5D963                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Myotubularin phosphatase|||Myotubularin-related protein 10|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284360|||http://purl.uniprot.org/annotation/VAR_047539|||http://purl.uniprot.org/annotation/VSP_024465|||http://purl.uniprot.org/annotation/VSP_024466|||http://purl.uniprot.org/annotation/VSP_024467|||http://purl.uniprot.org/annotation/VSP_024468|||http://purl.uniprot.org/annotation/VSP_035774
http://togogenome.org/gene/9606:TEX55                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M34                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Testis-specific expressed protein 55                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254576|||http://purl.uniprot.org/annotation/VAR_028841|||http://purl.uniprot.org/annotation/VAR_028842|||http://purl.uniprot.org/annotation/VAR_028843|||http://purl.uniprot.org/annotation/VAR_028844|||http://purl.uniprot.org/annotation/VAR_028845|||http://purl.uniprot.org/annotation/VAR_061574
http://togogenome.org/gene/9606:PSMC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X2I1|||http://purl.uniprot.org/uniprot/P62333                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  26S proteasome regulatory subunit 10B|||AAA+ ATPase|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084732
http://togogenome.org/gene/9606:NCOA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCD5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes E2-inducible strong interaction with ESR1, but not basal interaction.|||Abolishes interaction with ESR1.|||Basic and acidic residues|||Disordered|||LXXLL motif|||N-acetylmethionine|||Nuclear receptor coactivator 5|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription activation|||Transcription repression                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094411|||http://purl.uniprot.org/annotation/VAR_053530
http://togogenome.org/gene/9606:SF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DX42|||http://purl.uniprot.org/uniprot/H7C561|||http://purl.uniprot.org/uniprot/Q15637                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes RNA-binding.|||Abolishes interaction with U2AF2.|||CCHC-type|||Decreases RNA-binding.|||Decreases interaction with U2AF2 and spliceosome assembly.|||Decreases interaction with U2AF2.|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||KH|||N-acetylalanine|||No effect.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by PKG|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||Slightly decreases RNA-binding.|||Splicing factor 1|||Strongly decreases interaction with U2AF2 and spliceosome assembly.|||Strongly reduces RNA-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050129|||http://purl.uniprot.org/annotation/VAR_017196|||http://purl.uniprot.org/annotation/VSP_008833|||http://purl.uniprot.org/annotation/VSP_008834|||http://purl.uniprot.org/annotation/VSP_008835|||http://purl.uniprot.org/annotation/VSP_008836|||http://purl.uniprot.org/annotation/VSP_008837|||http://purl.uniprot.org/annotation/VSP_008838|||http://purl.uniprot.org/annotation/VSP_008839|||http://purl.uniprot.org/annotation/VSP_045274
http://togogenome.org/gene/9606:PDHA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29803                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Abolishes enzyme activity. Increases neuronal cell death in response to glutamate excitotoxicity.|||In SPGF70; unknown pathological significance.|||Increases enzyme activity in stem cells.|||Mitochondrion|||Phosphoserine|||Phosphoserine; by PDK1, PDK2, PDK3 and PDK4|||Phosphoserine; by PDK3|||Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial|||Slightly reduces enzyme activity.|||Strongly reduces enzyme activity. Increases enzyme activity in stem cells.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020447|||http://purl.uniprot.org/annotation/VAR_034359|||http://purl.uniprot.org/annotation/VAR_087365
http://togogenome.org/gene/9606:RRP7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3A4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  In MCPH28; increased proteolytic degradation; decreased recruitment to the nucleolus; decreased interaction with NOL6; decreased function in localization of NOL6 to the nucleolus; loss of function in rRNA processing; changed function in cilia resorption.|||Phosphoserine|||RRM|||Ribosomal RNA-processing protein 7 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082008|||http://purl.uniprot.org/annotation/VAR_052227|||http://purl.uniprot.org/annotation/VAR_052228|||http://purl.uniprot.org/annotation/VAR_052229|||http://purl.uniprot.org/annotation/VAR_086134
http://togogenome.org/gene/9606:DRAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14919                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Dr1-associated corepressor|||Histone-fold|||In isoform 2.|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080001|||http://purl.uniprot.org/annotation/VSP_012215
http://togogenome.org/gene/9606:ZBTB32                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Polar residues|||Zinc finger and BTB domain-containing protein 32                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000273417|||http://purl.uniprot.org/annotation/VAR_030145
http://togogenome.org/gene/9606:ZIM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||KRAB|||Polar residues|||Zinc finger imprinted 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047774|||http://purl.uniprot.org/annotation/VAR_021896|||http://purl.uniprot.org/annotation/VAR_052931|||http://purl.uniprot.org/annotation/VAR_052932
http://togogenome.org/gene/9606:C10orf71                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q711Q0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cardiac-enriched FHL2-interacting protein|||Disordered|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000282979|||http://purl.uniprot.org/annotation/VAR_031441|||http://purl.uniprot.org/annotation/VAR_031442|||http://purl.uniprot.org/annotation/VAR_059608|||http://purl.uniprot.org/annotation/VAR_059609|||http://purl.uniprot.org/annotation/VAR_059610|||http://purl.uniprot.org/annotation/VAR_059611|||http://purl.uniprot.org/annotation/VAR_059612|||http://purl.uniprot.org/annotation/VAR_059613|||http://purl.uniprot.org/annotation/VAR_059614|||http://purl.uniprot.org/annotation/VAR_061604|||http://purl.uniprot.org/annotation/VAR_061605|||http://purl.uniprot.org/annotation/VAR_061606|||http://purl.uniprot.org/annotation/VSP_024267|||http://purl.uniprot.org/annotation/VSP_024268
http://togogenome.org/gene/9606:KNL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG31                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||2 X 104 AA approximate repeats|||Basic and acidic residues|||Breakpoint for translocation to form KMT2A-KNL1|||Disordered|||In MCPH4; may inactivate an exonic splicing enhancer and result in abnormal splicing.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||Interaction with BUB1 and BUB1B|||Kinetochore scaffold 1|||Necessary for kinetochore localization and for interaction with NSL1 and DSN1|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089327|||http://purl.uniprot.org/annotation/VAR_026428|||http://purl.uniprot.org/annotation/VAR_026429|||http://purl.uniprot.org/annotation/VAR_026430|||http://purl.uniprot.org/annotation/VAR_026431|||http://purl.uniprot.org/annotation/VAR_026432|||http://purl.uniprot.org/annotation/VAR_026433|||http://purl.uniprot.org/annotation/VAR_026434|||http://purl.uniprot.org/annotation/VAR_054342|||http://purl.uniprot.org/annotation/VAR_061568|||http://purl.uniprot.org/annotation/VAR_061569|||http://purl.uniprot.org/annotation/VAR_061570|||http://purl.uniprot.org/annotation/VAR_069085|||http://purl.uniprot.org/annotation/VSP_013795|||http://purl.uniprot.org/annotation/VSP_013796|||http://purl.uniprot.org/annotation/VSP_013797|||http://purl.uniprot.org/annotation/VSP_018524|||http://purl.uniprot.org/annotation/VSP_018525
http://togogenome.org/gene/9606:RNF187                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TA31                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Zinc Finger                                                                                  ^@                                                                                  Abolishes ubiquitination by TRIM7; when associated with K-109.|||Abolishes ubiquitination by TRIM7; when associated with K-98.|||Asymmetric dimethylarginine; by PRMT1|||E3 ubiquitin-protein ligase RNF187|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Increased RNF187 stability and reduced polyubiquitination; when associated with A-12.|||Increased RNF187 stability and reduced polyubiquitination; when associated with A-15.|||Loss of protein expression.|||No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-223.|||No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-195 and R-224.|||No detectable effect on ubiquitination. Marked decrease in ubiquitination, but no effect on subcellular location; when associated with R-223 and R-224.|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000278241
http://togogenome.org/gene/9606:ASXL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TKV8|||http://purl.uniprot.org/uniprot/Q9C0F0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||DEUBAD|||Disordered|||Found in a patient with cohesinopathy; unknown pathological significance.|||HTH HARE-type|||In isoform 2.|||PHD-type; atypical|||Polar residues|||Pro residues|||Putative Polycomb group protein ASXL3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320670|||http://purl.uniprot.org/annotation/VAR_039267|||http://purl.uniprot.org/annotation/VAR_039268|||http://purl.uniprot.org/annotation/VAR_039269|||http://purl.uniprot.org/annotation/VAR_039270|||http://purl.uniprot.org/annotation/VAR_082310|||http://purl.uniprot.org/annotation/VSP_042433|||http://purl.uniprot.org/annotation/VSP_042434
http://togogenome.org/gene/9606:OR4D10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVJ1|||http://purl.uniprot.org/uniprot/Q8NGI6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4D10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150542
http://togogenome.org/gene/9606:KRTAP27-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI81                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Keratin-associated protein 27-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307916|||http://purl.uniprot.org/annotation/VAR_053479
http://togogenome.org/gene/9606:SMOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3U7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand 1|||EF-hand 2|||In isoform 2.|||Kazal-like|||N-linked (GlcNAc...) asparagine|||Polar residues|||SPARC-related modular calcium-binding protein 2|||Thyroglobulin type-1 1|||Thyroglobulin type-1 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020318|||http://purl.uniprot.org/annotation/VSP_008722
http://togogenome.org/gene/9606:BPIFB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NFQ5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  BPI fold-containing family B member 6|||De novo variant found in a patient with intellectual disability.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017168|||http://purl.uniprot.org/annotation/VAR_024518|||http://purl.uniprot.org/annotation/VAR_033632|||http://purl.uniprot.org/annotation/VAR_033633|||http://purl.uniprot.org/annotation/VAR_033634|||http://purl.uniprot.org/annotation/VAR_065088
http://togogenome.org/gene/9606:XAB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCS7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||HAT 1|||HAT 10|||HAT 11|||HAT 12|||HAT 13|||HAT 14|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||HAT 9|||N6-acetyllysine|||Phosphoserine|||Pre-mRNA-splicing factor SYF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106414|||http://purl.uniprot.org/annotation/VAR_016248|||http://purl.uniprot.org/annotation/VAR_016249|||http://purl.uniprot.org/annotation/VAR_016250
http://togogenome.org/gene/9606:GAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22466                                                                                  ^@                                                                                  Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Compositionally Biased Region|||Helix|||Modified Residue|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Galanin|||Galanin message-associated peptide|||In ETL8; decreased affinity for GALR2; but no effect on affinity for GALR1 and GALR3; decreased activity in GALR2-mediated signaling; dominant-negative that inhibits GALR1-mediated signaling.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010448|||http://purl.uniprot.org/annotation/PRO_0000010449|||http://purl.uniprot.org/annotation/PRO_0000010450|||http://purl.uniprot.org/annotation/VAR_049121|||http://purl.uniprot.org/annotation/VAR_074671
http://togogenome.org/gene/9606:VAMP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B8ZZT4|||http://purl.uniprot.org/uniprot/Q9BV40                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  (Microbial infection) N6-stearoyl lysine|||Abolished stearoylation in response to S.flexneri infection.|||Cytoplasmic|||Does not affect stearoylation in response to S.flexneri infection.|||Helical; Anchor for type IV membrane protein|||Interaction with STX8|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||V-SNARE coiled-coil homology|||Vesicle-associated membrane protein 8|||Vesicular|||v-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206736
http://togogenome.org/gene/9606:ART3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13508                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 10 AA tandem repeats of [GS]-E-K-N-[QW]-K-L-E-D-H|||Disordered|||Ecto-ADP-ribosyltransferase 3|||Found in patients with non-obstructive azoospermia; unknown pathological significance.|||GPI-anchor amidated serine|||In isoform 1.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Removed in mature form|||TR mART core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019325|||http://purl.uniprot.org/annotation/PRO_0000019326|||http://purl.uniprot.org/annotation/VAR_060072|||http://purl.uniprot.org/annotation/VAR_081146|||http://purl.uniprot.org/annotation/VSP_003374|||http://purl.uniprot.org/annotation/VSP_003375
http://togogenome.org/gene/9606:CDKN1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P38936                                                                                  ^@                                                                                  Chain|||Crosslink|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes UV radiation-induced phosphorylation and subsequent degradation.|||Abolishes degradation by the proteasome without affecting the interaction with PCNA.|||Abolishes interaction with PCNA and subsequent degradation by the proteasome.|||C4-type|||Cyclin-dependent kinase inhibitor 1|||Disordered|||Glycyl serine ester (Ser-Gly) (interchain with G-Cter in ubiquitin)|||Interaction with TRIM39|||Loss of interaction with TRIM39.|||N-acetylserine|||No change in interaction with PCNA. Abolishes UV radiation-induced phosphorylation and subsequent degradation.|||No interaction with PCNA; 59% inhibition of CDK2 binding; modest inhibition of CDK4 binding; no change in subcellular location.|||Nuclear localization signal|||PIP-box K+4 motif|||Phosphomimetic mutant, increases ubiquitination by the DCX(DTL) complex.|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphoserine; by PKC and NUAK1|||Phosphoserine; by PKC; in vitro|||Phosphothreonine; by LKB1|||Phosphothreonine; by PKA, PKB/AKT1, PIM1 and PIM2|||Reduces interaction with PCNA.|||Reduces phosphorylation by Akt; no change in interaction with PCNA, CDK2 or CDK4; no change in subcellular location.|||Removed|||Required for binding CDKs|||Required for binding cyclins                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190079|||http://purl.uniprot.org/annotation/VAR_011870|||http://purl.uniprot.org/annotation/VAR_048686|||http://purl.uniprot.org/annotation/VAR_048687
http://togogenome.org/gene/9606:GPR37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15354                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Prosaposin receptor GPR37                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012799
http://togogenome.org/gene/9606:RCBTB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DWG0|||http://purl.uniprot.org/uniprot/B4E372|||http://purl.uniprot.org/uniprot/O95199|||http://purl.uniprot.org/uniprot/Q59FB7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Non-terminal Residue|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||In isoform 2.|||RCC1|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5|||RCC1 6|||RCC1 and BTB domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206644|||http://purl.uniprot.org/annotation/VAR_024758|||http://purl.uniprot.org/annotation/VAR_024759|||http://purl.uniprot.org/annotation/VSP_016723
http://togogenome.org/gene/9606:GSTA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15217                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase A4|||In isoform 2.|||N-acetylmethionine|||Reduces catalytic activity 70-fold.|||Strongly reduced activity towards 4-hydroxynon-2-enal and 1-chloro-2,4-dinitrobenzene.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185786|||http://purl.uniprot.org/annotation/VAR_022210|||http://purl.uniprot.org/annotation/VAR_022211|||http://purl.uniprot.org/annotation/VSP_056473
http://togogenome.org/gene/9606:VSX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58304                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Motif|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CVC|||Disordered|||Homeobox|||In MCOP2.|||In MCOPCB3; the patient also has cataracts.|||In MCOPCTI; loss of DNA binding capacity at consensus sequences; abnormal and prolonged expression of MITF and WLS; mislocalization of CTNNB1.|||In MCOPCTI; loss of DNA binding capacity.|||Loss of SAG repressor activity. Loss of competitive inhibition of ISL1-LHX3 binding to common response elements.|||OAR|||Polar residues|||Visual system homeobox 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049362|||http://purl.uniprot.org/annotation/VAR_011618|||http://purl.uniprot.org/annotation/VAR_011619|||http://purl.uniprot.org/annotation/VAR_029357|||http://purl.uniprot.org/annotation/VAR_049593|||http://purl.uniprot.org/annotation/VAR_067269|||http://purl.uniprot.org/annotation/VAR_075633
http://togogenome.org/gene/9606:CCL15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0B4J2E2|||http://purl.uniprot.org/uniprot/Q16663                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine|||C-C motif chemokine 15|||CCL15(22-92)|||CCL15(25-92)|||CCL15(29-92)|||Chemokine interleukin-8-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005208|||http://purl.uniprot.org/annotation/PRO_0000041868|||http://purl.uniprot.org/annotation/PRO_0000041869|||http://purl.uniprot.org/annotation/PRO_0000041870|||http://purl.uniprot.org/annotation/PRO_5013980090|||http://purl.uniprot.org/annotation/VAR_011640
http://togogenome.org/gene/9606:CPA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48052                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Carboxypeptidase A2|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004353|||http://purl.uniprot.org/annotation/PRO_0000004354|||http://purl.uniprot.org/annotation/VAR_031204
http://togogenome.org/gene/9606:TPP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14773                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In CLN2.|||In CLN2; displays no residual enzyme activity; altered intracellular trafficking.|||In CLN2; displays no residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment.|||In CLN2; displays no residual enzyme activity; altered intracellular trafficking;.|||In CLN2; displays no residual enzyme activity; effectively transported to the lysosome.|||In CLN2; displays residual enzyme activity; effectively transported to the lysosome.|||In CLN2; displays very low residual enzyme activity; altered intracellular trafficking.|||In CLN2; displays very low residual enzyme activity; altered intracellular trafficking; demonstrates enhanced processing in response to folding improvement treatment; shows a five fold increase under permissive temperature conditions.|||In CLN2; enzymatically inactive; lacks one oligosaccharide chain resulting in enzymatic inactivation and possibly prelysosomal protein degradation; altered intracellular trafficking.|||In SCAR7.|||In isoform 2.|||Inactive. Impaired processing.|||N-linked (GlcNAc...) asparagine|||No effect.|||Peptidase S53|||Removed in mature form|||Tripeptidyl-peptidase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027374|||http://purl.uniprot.org/annotation/PRO_0000027375|||http://purl.uniprot.org/annotation/VAR_005642|||http://purl.uniprot.org/annotation/VAR_005643|||http://purl.uniprot.org/annotation/VAR_005644|||http://purl.uniprot.org/annotation/VAR_005645|||http://purl.uniprot.org/annotation/VAR_009603|||http://purl.uniprot.org/annotation/VAR_009604|||http://purl.uniprot.org/annotation/VAR_009605|||http://purl.uniprot.org/annotation/VAR_009606|||http://purl.uniprot.org/annotation/VAR_009607|||http://purl.uniprot.org/annotation/VAR_009608|||http://purl.uniprot.org/annotation/VAR_009609|||http://purl.uniprot.org/annotation/VAR_009610|||http://purl.uniprot.org/annotation/VAR_009611|||http://purl.uniprot.org/annotation/VAR_009612|||http://purl.uniprot.org/annotation/VAR_016790|||http://purl.uniprot.org/annotation/VAR_016791|||http://purl.uniprot.org/annotation/VAR_016792|||http://purl.uniprot.org/annotation/VAR_016793|||http://purl.uniprot.org/annotation/VAR_016794|||http://purl.uniprot.org/annotation/VAR_016795|||http://purl.uniprot.org/annotation/VAR_016796|||http://purl.uniprot.org/annotation/VAR_016797|||http://purl.uniprot.org/annotation/VAR_016798|||http://purl.uniprot.org/annotation/VAR_016799|||http://purl.uniprot.org/annotation/VAR_016800|||http://purl.uniprot.org/annotation/VAR_037572|||http://purl.uniprot.org/annotation/VAR_037573|||http://purl.uniprot.org/annotation/VAR_058435|||http://purl.uniprot.org/annotation/VAR_063640|||http://purl.uniprot.org/annotation/VAR_063641|||http://purl.uniprot.org/annotation/VAR_066883|||http://purl.uniprot.org/annotation/VAR_066884|||http://purl.uniprot.org/annotation/VAR_066885|||http://purl.uniprot.org/annotation/VAR_066886|||http://purl.uniprot.org/annotation/VAR_066887|||http://purl.uniprot.org/annotation/VAR_066888|||http://purl.uniprot.org/annotation/VAR_066889|||http://purl.uniprot.org/annotation/VAR_066890|||http://purl.uniprot.org/annotation/VAR_066891|||http://purl.uniprot.org/annotation/VAR_070917|||http://purl.uniprot.org/annotation/VAR_072749|||http://purl.uniprot.org/annotation/VSP_013118
http://togogenome.org/gene/9606:BIRC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TQB4|||http://purl.uniprot.org/uniprot/A0A8V8TR92|||http://purl.uniprot.org/uniprot/Q9NR09                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  BIR|||Baculoviral IAP repeat-containing protein 6|||Basic and acidic residues|||Disordered|||Glycyl thioester intermediate|||Phosphoserine|||Phosphothreonine|||Polar residues|||UBC core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122361
http://togogenome.org/gene/9606:SEC62                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99442                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Lumenal|||Phosphoserine|||Phosphothreonine|||Translocation protein SEC62                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206616
http://togogenome.org/gene/9606:ANKRD40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8IK34|||http://purl.uniprot.org/uniprot/Q6AI12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Ankyrin repeat domain-containing protein 40|||Disordered|||N-acetylmethionine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244368
http://togogenome.org/gene/9606:SOX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT81                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HMG box|||In isoform 2.|||Sox C-terminal|||Transcription factor SOX-7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048731|||http://purl.uniprot.org/annotation/VSP_056667
http://togogenome.org/gene/9606:HNRNPUL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRA5|||http://purl.uniprot.org/uniprot/A8K3W4|||http://purl.uniprot.org/uniprot/B7Z4B8|||http://purl.uniprot.org/uniprot/Q9BUJ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-2|||1-3|||1-4|||1-5|||5 X 3 AA repeats of R-G-G|||Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||B30.2/SPRY|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Heterogeneous nuclear ribonucleoprotein U-like protein 1|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Necessary for interaction with BRD7 and transcriptional activation|||Necessary for interaction with HRMT1L1|||Necessary for interaction with TP53|||Necessary for transcription repression|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||SAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227555|||http://purl.uniprot.org/annotation/VAR_025606|||http://purl.uniprot.org/annotation/VSP_017546|||http://purl.uniprot.org/annotation/VSP_017547|||http://purl.uniprot.org/annotation/VSP_017548|||http://purl.uniprot.org/annotation/VSP_017549|||http://purl.uniprot.org/annotation/VSP_017550|||http://purl.uniprot.org/annotation/VSP_017551|||http://purl.uniprot.org/annotation/VSP_017552
http://togogenome.org/gene/9606:DNAAF11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X45                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CS|||Disordered|||Dynein axonemal assembly factor 11|||In CILD19.|||In CILD19; loss of interaction with ZMYND10.|||In CILD19; loss of protein expression.|||In CILD19; no effect on interaction with ZMYND10.|||In CILD19; no effect on interaction with ZMYND10; reduced expression in cytoplasm; decreased expression of inner and outer dynein proteins; mislocation of inner and outer dynein proteins.|||In CILD19; unknown pathological significance.|||In isoform 2.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084496|||http://purl.uniprot.org/annotation/VAR_023603|||http://purl.uniprot.org/annotation/VAR_031223|||http://purl.uniprot.org/annotation/VAR_069038|||http://purl.uniprot.org/annotation/VAR_069039|||http://purl.uniprot.org/annotation/VAR_084433|||http://purl.uniprot.org/annotation/VAR_084434|||http://purl.uniprot.org/annotation/VAR_084435|||http://purl.uniprot.org/annotation/VAR_084436|||http://purl.uniprot.org/annotation/VAR_084437|||http://purl.uniprot.org/annotation/VSP_015862|||http://purl.uniprot.org/annotation/VSP_015863
http://togogenome.org/gene/9606:KRTAP7-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC3                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  11 X 2 AA repeats of G-[YCGS]|||Keratin-associated protein 7-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185182
http://togogenome.org/gene/9606:POLB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1W5|||http://purl.uniprot.org/uniprot/P06746                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes 5'-dRP lyase activity. No effect on DNA polymerase activity.|||Abolishes DNA polymerase and 5'-dRP lyase activity.|||Abolishes ubiquitination; when associated with R-41 and R-61.|||Abolishes ubiquitination; when associated with R-41 and R-81.|||Abolishes ubiquitination; when associated with R-61 and R-81.|||Affects DNA-directed DNA polymerase activity; contrary to wild-type enzyme, the mutant efficiently extends mispaired termini in gapped DNA. No effect on secondary structure shown by circular dichroism.|||Changed DNA-directed DNA polymerase activity; in complex with the DNA template and the incoming dNTP, it assumes a close conformation faster than wild-type POLB and exhibits a slower rate of nucleotide release. Results in decreased fidelity on one-base-gapped DNA and increased mutation frequency at A-T base pairs. No effect on secondary structure shown by circular dichroism. No effect on thermal stability.|||DNA polymerase beta|||DNA-binding|||DNA-directed DNA polymerase X|||Decreased 5'-dRP lyase activity. Decreased ssDNA binding.|||Decreased 5'-dRP lyase activity. Decreased ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-68 and A-72. Decreased ssDNA binding; when associated with A-68 and A-72. No effect on structure shown by circular dichroism.|||Decreased DNA-directed DNA polymerase activity; does not affect secondary structure as shown by circular dichroism.|||Decreased function in base-excision repair; decreased DNA-directed DNA polymerase activity; no effect on 5'-dRP lyase activity; no effect on DNA binding; decreased interaction with PCNA.|||Found in a colon cancer sample; unknown pathological significance; affects DNA-directed DNA polymerase activity resulting in nucleotide misincorporation in gapped DNA and decreased fidelity during DNA synthesis in base-excision repair; decreased affinity for gapped DNA; due to altered structure of the C-terminal region, the mutant enzyme in complex with DNA and dGTP does not undergo the open to closed conformational change that is necessary to assembly a catalytically competent active site.|||Found in a gastric cancer sample; unknown pathological significance.|||Found in a gastric cancer sample; unknown pathological significance; dominant negative variant; induces cellular transformation when expressed in mouse cells; results in loss of function in base-excision repair; loss of DNA-directed DNA polymerase activity; retains 5'-dRP lyase activity; does not affect DNA binding.|||Found in a gastric cancer sample; unknown pathological significance; loss of function in base-excision repair; decreased DNA-directed DNA polymerase activity; loss of 5'-dRP lyase activity; lower affinity for gapped DNA.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||N6-acetyllysine|||No effect on 5'-dRP lyase activity.|||No effect on 5'-dRP lyase activity. Decreased ssDNA binding.|||No effect on 5'-dRP lyase activity. Decreased ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-35 and A-72. Decreased ssDNA binding; when associated with A-35 and A-72. No effect on structure shown by circular dichroism.|||No effect on 5'-dRP lyase activity. No effect on structure shown by circular dichroism. No effect on ssDNA binding.|||No effect on structure shown by circular dichroism. No effect on ssDNA binding.|||Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity|||Omega-N-methylarginine; by PRMT6|||Reduces 5'-dRP lyase activity slightly.|||Severely decreased function in base-excision repair. Severely decreased DNA-directed DNA polymerase activity. No effect on 5'-dRP lyase activity. No effect on DNA binding. No effect on structure shown by circular dichroism. No effect on interaction with APEX1, FEN1 and PCNA.|||Severely reduced 5'-dRP lyase activity. Does not affect ssDNA binding. Loss of 5'-dRP lyase activity; when associated with A-35 and A-68. Decreased ssDNA binding; when associated with A-35 and A-68. No effect on structure shown by circular dichroism.|||Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-152.|||Slight effect. Abolishes methylation by PRMT6 and impairs the polymerase activity; when associated with K-83.|||Slightly decreased 5'-dRP lyase activity. Decreased ssDNA binding. No effect on structure shown by circular dichroism.|||Slightly reduces 5'-dRP lyase activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218778|||http://purl.uniprot.org/annotation/VAR_018881|||http://purl.uniprot.org/annotation/VAR_088253|||http://purl.uniprot.org/annotation/VAR_088254|||http://purl.uniprot.org/annotation/VAR_088255|||http://purl.uniprot.org/annotation/VAR_088256|||http://purl.uniprot.org/annotation/VAR_088257|||http://purl.uniprot.org/annotation/VAR_088258|||http://purl.uniprot.org/annotation/VAR_088259|||http://purl.uniprot.org/annotation/VAR_088260|||http://purl.uniprot.org/annotation/VAR_088261|||http://purl.uniprot.org/annotation/VAR_088262
http://togogenome.org/gene/9606:RCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96D15                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Decreased function in PCSK6 maturation and/or secretion.|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||EF-hand 5|||EF-hand 6|||N-linked (GlcNAc...) asparagine|||Prevents secretion from ER|||Reticulocalbin-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004151|||http://purl.uniprot.org/annotation/VAR_033696
http://togogenome.org/gene/9606:MND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTC6|||http://purl.uniprot.org/uniprot/Q9BWT6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Meiotic nuclear division protein 1 homolog|||Mnd1 HTH|||N-acetylserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318081
http://togogenome.org/gene/9606:ZCWPW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0M4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||CW-type|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4.|||Loss of histone H3K4me3 binding; when associated with I-256; L-302 and P-303.|||Loss of histone H3K4me3 binding; when associated with I-256; R-301 and L-302.|||Loss of histone H3K4me3 binding; when associated with I-256; R-301 and P-303.|||Loss of histone H3K4me3 binding; when associated with R-301; L-302 and P-303.|||PWWP|||Phosphoserine|||Polar residues|||Reduced histone H3K4me3 binding but complete loss of non-methylated histone H3K4 binding.|||Reduced histone H3K4me3 binding but no effect on non-methylated histone H3K4 binding.|||Silghtly reduced histone H3K4me3 and non-methylated histone H3K4 binding.|||Zinc finger CW-type PWWP domain protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066567|||http://purl.uniprot.org/annotation/VAR_019659|||http://purl.uniprot.org/annotation/VAR_047050|||http://purl.uniprot.org/annotation/VSP_011431|||http://purl.uniprot.org/annotation/VSP_011432|||http://purl.uniprot.org/annotation/VSP_011433|||http://purl.uniprot.org/annotation/VSP_011434|||http://purl.uniprot.org/annotation/VSP_011436|||http://purl.uniprot.org/annotation/VSP_035590|||http://purl.uniprot.org/annotation/VSP_035591|||http://purl.uniprot.org/annotation/VSP_035592
http://togogenome.org/gene/9606:BRAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15056                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Blocks EGF-induced ubiquitination and ERK activation.|||Breakpoint for translocation to form KIAA1549-BRAF fusion protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CFC1 and LPRD3.|||In CFC1 and colon cancer.|||In CFC1.|||In CFC1; also found in colon cancer.|||In CRC.|||In CRC; also found in sarcoma, metastatic melanoma, ovarian serous carcinoma, pilocytic astrocytoma; somatic mutation; most common mutation; constitutive and elevated kinase activity; efficiently induces cell transformation; suppression of mutation in melanoma causes growth arrest and promotes apoptosis; loss of regulation by PMRT5.|||In LNCR.|||In LNCR; also found in an ovarian serous carcinoma sample; somatic mutation.|||In NHL.|||In NHL; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation.|||In NS7.|||In NS7; also in a lung adenocarcinoma sample; somatic mutation; elevated kinase activity; efficiently induces cell transformation.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a colorectal cancer cell line; elevated kinase activity; efficiently induces cell transformation.|||In a melanoma cell line; requires 2 nucleotide substitutions.|||In melanoma.|||In ovarian cancer.|||Increased kinase activity and stability in response to EGF treatment.|||Loss of MAP2K1-mediated-BRAF-KSR1 dimerization.|||N-acetylalanine|||No effect on MAP2K1-mediated-BRAF-KSR1 dimerization, however loss of BRAF-mediated phosphorylation of MAP2K1.|||Omega-N-methylarginine; by PRMT5|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by SGK1|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Phosphothreonine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||RBD|||Reduces interaction with KSR1 and MAP2K1 and thus phosphorylation of MAP2K1.|||Reduces kinase activity with MAP2K1.|||Removed|||Serine/threonine-protein kinase B-raf                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085665|||http://purl.uniprot.org/annotation/VAR_018512|||http://purl.uniprot.org/annotation/VAR_018513|||http://purl.uniprot.org/annotation/VAR_018613|||http://purl.uniprot.org/annotation/VAR_018614|||http://purl.uniprot.org/annotation/VAR_018615|||http://purl.uniprot.org/annotation/VAR_018616|||http://purl.uniprot.org/annotation/VAR_018617|||http://purl.uniprot.org/annotation/VAR_018618|||http://purl.uniprot.org/annotation/VAR_018620|||http://purl.uniprot.org/annotation/VAR_018621|||http://purl.uniprot.org/annotation/VAR_018622|||http://purl.uniprot.org/annotation/VAR_018623|||http://purl.uniprot.org/annotation/VAR_018624|||http://purl.uniprot.org/annotation/VAR_018625|||http://purl.uniprot.org/annotation/VAR_018626|||http://purl.uniprot.org/annotation/VAR_018627|||http://purl.uniprot.org/annotation/VAR_018628|||http://purl.uniprot.org/annotation/VAR_018629|||http://purl.uniprot.org/annotation/VAR_018630|||http://purl.uniprot.org/annotation/VAR_026113|||http://purl.uniprot.org/annotation/VAR_026114|||http://purl.uniprot.org/annotation/VAR_026115|||http://purl.uniprot.org/annotation/VAR_026116|||http://purl.uniprot.org/annotation/VAR_026117|||http://purl.uniprot.org/annotation/VAR_026118|||http://purl.uniprot.org/annotation/VAR_026119|||http://purl.uniprot.org/annotation/VAR_035096|||http://purl.uniprot.org/annotation/VAR_035097|||http://purl.uniprot.org/annotation/VAR_035098|||http://purl.uniprot.org/annotation/VAR_040391|||http://purl.uniprot.org/annotation/VAR_040392|||http://purl.uniprot.org/annotation/VAR_040393|||http://purl.uniprot.org/annotation/VAR_058620|||http://purl.uniprot.org/annotation/VAR_058621|||http://purl.uniprot.org/annotation/VAR_058622|||http://purl.uniprot.org/annotation/VAR_058623|||http://purl.uniprot.org/annotation/VAR_058624|||http://purl.uniprot.org/annotation/VAR_058625|||http://purl.uniprot.org/annotation/VAR_058626|||http://purl.uniprot.org/annotation/VAR_058627|||http://purl.uniprot.org/annotation/VAR_058628|||http://purl.uniprot.org/annotation/VAR_058629|||http://purl.uniprot.org/annotation/VAR_058630|||http://purl.uniprot.org/annotation/VAR_058631|||http://purl.uniprot.org/annotation/VAR_065171|||http://purl.uniprot.org/annotation/VAR_065172|||http://purl.uniprot.org/annotation/VAR_065173
http://togogenome.org/gene/9606:SPINT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43278                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor 1|||BPTI/Kunitz inhibitor 2|||In isoform 2.|||Kunitz-type protease inhibitor 1|||LDL-receptor class A|||MANSC|||N-linked (GlcNAc...) asparagine|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016883|||http://purl.uniprot.org/annotation/VAR_050065|||http://purl.uniprot.org/annotation/VAR_050066|||http://purl.uniprot.org/annotation/VAR_050067|||http://purl.uniprot.org/annotation/VSP_013019
http://togogenome.org/gene/9606:CCDC65                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IXS2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Dynein regulatory complex subunit 2|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284778|||http://purl.uniprot.org/annotation/VAR_056780|||http://purl.uniprot.org/annotation/VAR_056781|||http://purl.uniprot.org/annotation/VSP_024644
http://togogenome.org/gene/9606:UBFD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14562                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ubiquitin domain-containing protein UBFD1|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000283075
http://togogenome.org/gene/9606:LAG3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18627                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  12 X 2 AA tandem repeats of E-X|||Abolishes binding to MHC class II (MHC-II) without affecting interaction with FGL1.|||Acidic residues|||Connecting peptide|||Cytoplasmic|||Disordered|||Does not affect binding to MHC class II (MHC-II).|||Does not significantly affect binding to MHC class II (MHC-II).|||Extracellular|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like V-type|||In isoform 2.|||Increased binding to MHC class II (MHC-II).|||Interaction with FGL1|||KIEELE motif|||Lymphocyte activation gene 3 protein|||N-linked (GlcNAc...) asparagine|||Pro residues|||Reduced binding to MHC class II (MHC-II).|||Secreted lymphocyte activation gene 3 protein|||Slightly affects binding to MHC class II (MHC-II).                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014631|||http://purl.uniprot.org/annotation/PRO_0000446642|||http://purl.uniprot.org/annotation/VAR_058295|||http://purl.uniprot.org/annotation/VSP_056311|||http://purl.uniprot.org/annotation/VSP_056312
http://togogenome.org/gene/9606:FAM168A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92567                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||N-acetylmethionine|||Protein FAM168A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050742|||http://purl.uniprot.org/annotation/VSP_010095|||http://purl.uniprot.org/annotation/VSP_034630
http://togogenome.org/gene/9606:CD37                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11049                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 3.|||In isoform 3.|||Leukocyte antigen CD37|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219209|||http://purl.uniprot.org/annotation/VSP_047228|||http://purl.uniprot.org/annotation/VSP_047229
http://togogenome.org/gene/9606:TGDS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95455                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Sequence Variant                                                                                  ^@                                                                                  In CATMANS.|||Proton acceptor|||Proton donor|||dTDP-D-glucose 4,6-dehydratase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000183250|||http://purl.uniprot.org/annotation/VAR_049122|||http://purl.uniprot.org/annotation/VAR_072682|||http://purl.uniprot.org/annotation/VAR_072683|||http://purl.uniprot.org/annotation/VAR_072684|||http://purl.uniprot.org/annotation/VAR_072685|||http://purl.uniprot.org/annotation/VAR_072686
http://togogenome.org/gene/9606:FBXO22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEZ5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  F-box|||F-box only protein 22|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119906|||http://purl.uniprot.org/annotation/VSP_013058|||http://purl.uniprot.org/annotation/VSP_013059|||http://purl.uniprot.org/annotation/VSP_041821
http://togogenome.org/gene/9606:ITFG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TB96                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Repeat|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  FG-GAP; atypical|||Helical|||N-linked (GlcNAc...) asparagine|||T-cell immunomodulatory protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034354
http://togogenome.org/gene/9606:THOC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96J01                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-acetylalanine|||Removed|||THO complex subunit 3|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051273|||http://purl.uniprot.org/annotation/VAR_081223|||http://purl.uniprot.org/annotation/VSP_056173
http://togogenome.org/gene/9606:RNF170                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K19                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Cytoplasmic|||E3 ubiquitin-protein ligase RNF170|||Helical|||In SNAX1.|||In SPG85.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Lumenal|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280700|||http://purl.uniprot.org/annotation/VAR_068219|||http://purl.uniprot.org/annotation/VAR_086712|||http://purl.uniprot.org/annotation/VAR_086713|||http://purl.uniprot.org/annotation/VAR_086714|||http://purl.uniprot.org/annotation/VSP_023851|||http://purl.uniprot.org/annotation/VSP_023852|||http://purl.uniprot.org/annotation/VSP_023853|||http://purl.uniprot.org/annotation/VSP_023854|||http://purl.uniprot.org/annotation/VSP_023855|||http://purl.uniprot.org/annotation/VSP_023856|||http://purl.uniprot.org/annotation/VSP_023857|||http://purl.uniprot.org/annotation/VSP_044556
http://togogenome.org/gene/9606:VCY                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O14598                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Testis-specific basic protein Y 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000184663
http://togogenome.org/gene/9606:SERPINB6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QZX5|||http://purl.uniprot.org/uniprot/A0A087X1N8|||http://purl.uniprot.org/uniprot/A0A2R8YD12|||http://purl.uniprot.org/uniprot/P35237                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Reactive bond|||Serpin|||Serpin B6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094106|||http://purl.uniprot.org/annotation/VAR_037295|||http://purl.uniprot.org/annotation/VAR_037296
http://togogenome.org/gene/9606:ALDH1A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00352|||http://purl.uniprot.org/uniprot/V9HW83                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Aldehyde dehydrogenase|||Aldehyde dehydrogenase 1A1|||Does not prevent inhibition by duocarmycin analogs.|||Mediates interaction with PRMT3|||N-acetylserine|||N6-acetyllysine|||No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Proton acceptor|||Removed|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056415|||http://purl.uniprot.org/annotation/VAR_017778|||http://purl.uniprot.org/annotation/VAR_048901|||http://purl.uniprot.org/annotation/VAR_048902
http://togogenome.org/gene/9606:MED31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3C7                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  Mediator of RNA polymerase II transcription subunit 31|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212527
http://togogenome.org/gene/9606:SPMIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW14                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Sperm-associated microtubule inner protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089807|||http://purl.uniprot.org/annotation/VAR_050854|||http://purl.uniprot.org/annotation/VSP_036117|||http://purl.uniprot.org/annotation/VSP_036118|||http://purl.uniprot.org/annotation/VSP_036119
http://togogenome.org/gene/9606:GRAMD1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3M2|||http://purl.uniprot.org/uniprot/A0A2R8Y5X2|||http://purl.uniprot.org/uniprot/B7Z4N9|||http://purl.uniprot.org/uniprot/Q3KR37                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||GRAM|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein Aster-B|||VASt                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287449|||http://purl.uniprot.org/annotation/VSP_025469|||http://purl.uniprot.org/annotation/VSP_025470|||http://purl.uniprot.org/annotation/VSP_025471|||http://purl.uniprot.org/annotation/VSP_025472|||http://purl.uniprot.org/annotation/VSP_057573
http://togogenome.org/gene/9606:CTTN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14247|||http://purl.uniprot.org/uniprot/Q53HG7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Cortactin 1|||Cortactin 2|||Cortactin 3|||Cortactin 4|||Cortactin 5|||Cortactin 6|||Cortactin 7; truncated|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2 and isoform 3.|||In isoform 2.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by FAK1|||Phosphotyrosine; by SRC|||SH3|||Src substrate cortactin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072189|||http://purl.uniprot.org/annotation/VSP_043120|||http://purl.uniprot.org/annotation/VSP_043121
http://togogenome.org/gene/9606:TTC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99614                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106376|||http://purl.uniprot.org/annotation/VAR_081225
http://togogenome.org/gene/9606:CEP85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P2H3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Centrosomal protein of 85 kDa|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mediates interaction with NEK2 and is required for its function in the suppression of centrosome disjunction|||Phosphoserine|||Polar residues|||Required for centrosome localization and for its function in the suppression of centrosome disjunction                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233660|||http://purl.uniprot.org/annotation/VAR_033665|||http://purl.uniprot.org/annotation/VAR_053938|||http://purl.uniprot.org/annotation/VAR_053939|||http://purl.uniprot.org/annotation/VAR_053940|||http://purl.uniprot.org/annotation/VSP_018147|||http://purl.uniprot.org/annotation/VSP_026435|||http://purl.uniprot.org/annotation/VSP_055609
http://togogenome.org/gene/9606:SI                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14410                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||For isomaltase activity|||For sucrase activity|||Helical; Signal-anchor for type II membrane protein|||In CSID.|||In CSID; SI accumulates predominantly in the ER.|||In CSID; causes loss of anchored SI from the membrane.|||In CSID; exhibits intracellular accumulation of mannose-rich SI in the Golgi.|||In CSID; missorting of the enzyme to the basolateral membrane.|||Isomaltase|||Lumenal|||N-linked (GlcNAc...) asparagine|||Nucleophile; for isomaltase activity|||Nucleophile; for sucrase activity|||P-type 1|||P-type 2|||Phosphoserine; by PKA|||Proton donor; for isomaltase activity|||Removed|||Sucrase|||Sucrase-isomaltase, intestinal|||Sulfotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018551|||http://purl.uniprot.org/annotation/PRO_0000018552|||http://purl.uniprot.org/annotation/PRO_0000018553|||http://purl.uniprot.org/annotation/VAR_007854|||http://purl.uniprot.org/annotation/VAR_025367|||http://purl.uniprot.org/annotation/VAR_025368|||http://purl.uniprot.org/annotation/VAR_025369|||http://purl.uniprot.org/annotation/VAR_025370|||http://purl.uniprot.org/annotation/VAR_025371|||http://purl.uniprot.org/annotation/VAR_025372|||http://purl.uniprot.org/annotation/VAR_025373|||http://purl.uniprot.org/annotation/VAR_025374|||http://purl.uniprot.org/annotation/VAR_025375|||http://purl.uniprot.org/annotation/VAR_025376|||http://purl.uniprot.org/annotation/VAR_025377|||http://purl.uniprot.org/annotation/VAR_025378|||http://purl.uniprot.org/annotation/VAR_025379|||http://purl.uniprot.org/annotation/VAR_034522
http://togogenome.org/gene/9606:ANO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0L7|||http://purl.uniprot.org/uniprot/Q9NQ90                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Anoctamin dimerisation|||Anoctamin-2|||Cytoplasmic|||DLG4 binding (PDZ)|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072564|||http://purl.uniprot.org/annotation/VAR_020331|||http://purl.uniprot.org/annotation/VAR_021932|||http://purl.uniprot.org/annotation/VAR_057286|||http://purl.uniprot.org/annotation/VAR_061853|||http://purl.uniprot.org/annotation/VSP_040493|||http://purl.uniprot.org/annotation/VSP_040494
http://togogenome.org/gene/9606:FGF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31371                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fibroblast growth factor 9|||In SYNS3; expressed and secreted as efficiently as wild-type; however it induces compromised chondrocyte proliferation and differentiation accompanied by enhanced osteogenic differentiation and matrix mineralization of bone marrow-derived mesenchymal stem cells.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008973|||http://purl.uniprot.org/annotation/PRO_0000008974|||http://purl.uniprot.org/annotation/VAR_020944|||http://purl.uniprot.org/annotation/VAR_063254
http://togogenome.org/gene/9606:IFT74                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LB3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic region|||Disordered|||Important for interaction with IFT27|||In JBTS40.|||In JBTS40; partial loss of function; contrary to wild-type, only partially rescues the phenotype of IFT74 knockdown zebrafish; does not affect interaction with IFT81 and IFT27; does not affect protein level.|||In SPGF58; affects subcellular location, instead of being homogenously distributed along the sperm flagellum, concentrates in the proximal part of the flagellum; also affects splicing.|||In isoform 2.|||Intraflagellar transport protein 74 homolog|||Omega-N-methylarginine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084169|||http://purl.uniprot.org/annotation/VAR_051062|||http://purl.uniprot.org/annotation/VAR_051063|||http://purl.uniprot.org/annotation/VAR_051064|||http://purl.uniprot.org/annotation/VAR_051065|||http://purl.uniprot.org/annotation/VAR_051066|||http://purl.uniprot.org/annotation/VAR_061667|||http://purl.uniprot.org/annotation/VAR_076977|||http://purl.uniprot.org/annotation/VAR_086331|||http://purl.uniprot.org/annotation/VAR_086332|||http://purl.uniprot.org/annotation/VAR_086333|||http://purl.uniprot.org/annotation/VAR_086334|||http://purl.uniprot.org/annotation/VSP_041328
http://togogenome.org/gene/9606:E2F8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0AVK6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-156.|||Loss of DNA-binding and inhibition of E2F1-dependent activation. Impairs DNA-binding and dimerization; when associated with A-314.|||Phosphoserine|||Polar residues|||Transcription factor E2F8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298909|||http://purl.uniprot.org/annotation/VAR_034735
http://togogenome.org/gene/9606:PCDHGB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UN71                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protocadherin gamma-B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003977|||http://purl.uniprot.org/annotation/VSP_008690|||http://purl.uniprot.org/annotation/VSP_008691
http://togogenome.org/gene/9606:GRHL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE85                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Grainyhead-like protein 3 homolog|||Grh/CP2 DB|||In VWS2.|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Transcription activation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227997|||http://purl.uniprot.org/annotation/VAR_027907|||http://purl.uniprot.org/annotation/VAR_055881|||http://purl.uniprot.org/annotation/VAR_072616|||http://purl.uniprot.org/annotation/VAR_072617|||http://purl.uniprot.org/annotation/VAR_072618|||http://purl.uniprot.org/annotation/VSP_017643|||http://purl.uniprot.org/annotation/VSP_017644|||http://purl.uniprot.org/annotation/VSP_017645|||http://purl.uniprot.org/annotation/VSP_017646
http://togogenome.org/gene/9606:SLC25A40                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBP6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Probable mitochondrial glutathione transporter SLC25A40|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291809|||http://purl.uniprot.org/annotation/VAR_032863|||http://purl.uniprot.org/annotation/VAR_032864|||http://purl.uniprot.org/annotation/VAR_079372
http://togogenome.org/gene/9606:PRELID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y255                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Mitochondrion|||PRELI domain-containing protein 1, mitochondrial|||PRELI/MSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097119|||http://purl.uniprot.org/annotation/VSP_054731
http://togogenome.org/gene/9606:TMEM253                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0C7T8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 253                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000343722
http://togogenome.org/gene/9606:VPS51                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UID3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In PCH13; impaired association with VPS50 and VPS53 subunits; reduced levels of assembled GARP and EARP complexes.|||In PCH13; unknown pathological significance.|||In isoform 2.|||N-acetylalanine|||Phosphoserine|||Removed|||Vacuolar protein sorting-associated protein 51 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089831|||http://purl.uniprot.org/annotation/VAR_083138|||http://purl.uniprot.org/annotation/VAR_083139|||http://purl.uniprot.org/annotation/VSP_014700
http://togogenome.org/gene/9606:UBL4B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N7F7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Ubiquitin-like|||Ubiquitin-like protein 4B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263701
http://togogenome.org/gene/9606:EDN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05305|||http://purl.uniprot.org/uniprot/Q6FH53                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Associated with HDL cholesterol levels is some populations and in a sex-specific manner.|||Big endothelin-1|||Cleavage; by KEL|||Disordered|||Endothelin-1|||Endothelin-like|||Endothelin-like toxin|||In ARCND3.|||In QME.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008058|||http://purl.uniprot.org/annotation/PRO_0000008059|||http://purl.uniprot.org/annotation/PRO_0000008060|||http://purl.uniprot.org/annotation/PRO_0000008061|||http://purl.uniprot.org/annotation/PRO_5014310453|||http://purl.uniprot.org/annotation/VAR_014188|||http://purl.uniprot.org/annotation/VAR_048933|||http://purl.uniprot.org/annotation/VAR_071152|||http://purl.uniprot.org/annotation/VAR_071153|||http://purl.uniprot.org/annotation/VAR_071154
http://togogenome.org/gene/9606:C5orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9J3I9                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative uncharacterized protein C5orf58                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000392541
http://togogenome.org/gene/9606:RAPH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9K0J5|||http://purl.uniprot.org/uniprot/Q70E73                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform RMO1, isoform RMO1a, isoform RMO1b and isoform RMO1ab.|||In isoform RMO1a and isoform RMO1ac.|||In isoform RMO1ab and isoform RMO1abc.|||In isoform RMO1b and isoform RMO1bc.|||In isoform RMO1c, isoform RMO1ac, isoform RMO1bc and isoform RMO1abc.|||N-acetylmethionine|||PH|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1|||Polar residues|||Pro residues|||Ras-associated and pleckstrin homology domains-containing protein 1|||Ras-associating                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181352|||http://purl.uniprot.org/annotation/VAR_036009|||http://purl.uniprot.org/annotation/VAR_036010|||http://purl.uniprot.org/annotation/VSP_035784|||http://purl.uniprot.org/annotation/VSP_035785|||http://purl.uniprot.org/annotation/VSP_035786|||http://purl.uniprot.org/annotation/VSP_035787|||http://purl.uniprot.org/annotation/VSP_035788|||http://purl.uniprot.org/annotation/VSP_035789
http://togogenome.org/gene/9606:MPG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29372|||http://purl.uniprot.org/uniprot/Q1W6H1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  DNA-3-methyladenine glycosylase|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||Mitochondrion|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100065|||http://purl.uniprot.org/annotation/VAR_014831|||http://purl.uniprot.org/annotation/VAR_014832|||http://purl.uniprot.org/annotation/VAR_014833|||http://purl.uniprot.org/annotation/VAR_014834|||http://purl.uniprot.org/annotation/VAR_014835|||http://purl.uniprot.org/annotation/VAR_014836|||http://purl.uniprot.org/annotation/VAR_019138|||http://purl.uniprot.org/annotation/VAR_050096|||http://purl.uniprot.org/annotation/VSP_003249|||http://purl.uniprot.org/annotation/VSP_035485|||http://purl.uniprot.org/annotation/VSP_046678
http://togogenome.org/gene/9606:CDHR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYE9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cadherin 7|||Cadherin 8|||Cadherin 9|||Cadherin-related family member 2|||Cytoplasmic|||Disordered|||Extracellular|||Found in an acute myeloid leukemia sample; somatic mutation.|||Helical|||Loss of interaction with USH1C.|||Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organization|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000004011|||http://purl.uniprot.org/annotation/VAR_021548|||http://purl.uniprot.org/annotation/VAR_046695|||http://purl.uniprot.org/annotation/VAR_046696|||http://purl.uniprot.org/annotation/VAR_046697|||http://purl.uniprot.org/annotation/VAR_046698|||http://purl.uniprot.org/annotation/VAR_046699|||http://purl.uniprot.org/annotation/VAR_046700|||http://purl.uniprot.org/annotation/VAR_046701|||http://purl.uniprot.org/annotation/VAR_054148
http://togogenome.org/gene/9606:ZNHIT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHR6                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||HIT-type|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Phosphothreonine|||Zinc finger HIT domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173548|||http://purl.uniprot.org/annotation/VAR_035720|||http://purl.uniprot.org/annotation/VAR_053757|||http://purl.uniprot.org/annotation/VAR_053758
http://togogenome.org/gene/9606:CUL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTN0|||http://purl.uniprot.org/uniprot/A0A140VKB1|||http://purl.uniprot.org/uniprot/A0A8I5KVR3|||http://purl.uniprot.org/uniprot/B7Z1Y1|||http://purl.uniprot.org/uniprot/Q13617                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Cullin family profile|||Cullin-2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)|||In isoform 2.|||Loss of conjugation with NEDD8.|||N6-acetyllysine|||No effect on conjugation with NEDD8.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119790|||http://purl.uniprot.org/annotation/VAR_011374|||http://purl.uniprot.org/annotation/VSP_044498
http://togogenome.org/gene/9606:UNC5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZJ1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes cleavage by caspase-3 and subsequent induction of apoptosis.|||Cleavage; by caspase-3|||Cytoplasmic|||Death|||Extracellular|||Helical|||Ig-like|||Ig-like C2-type|||In isoform 2.|||Interaction with DCC|||N-linked (GlcNAc...) asparagine|||Netrin receptor UNC5B|||Phosphotyrosine|||S-palmitoyl cysteine|||TSP type-1 1|||TSP type-1 2|||UPA domain|||ZU5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036071|||http://purl.uniprot.org/annotation/VAR_019730|||http://purl.uniprot.org/annotation/VAR_052472|||http://purl.uniprot.org/annotation/VSP_011698
http://togogenome.org/gene/9606:FGF18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7U3JVY7|||http://purl.uniprot.org/uniprot/O76093                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fibroblast growth factor|||Fibroblast growth factor 18|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008990|||http://purl.uniprot.org/annotation/PRO_5031601580
http://togogenome.org/gene/9606:DEFB106A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N104                                                                                  ^@                                                                                  Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Peptide|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Disulfide Bond|||Helix|||Peptide|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Beta-defensin 106                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006977
http://togogenome.org/gene/9606:CERS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IU89                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Ceramide synthase 3|||Cytoplasmic|||Decreased phosphorylation.|||Disordered|||Helical|||Homeobox-like|||Phosphoserine|||TLC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185511|||http://purl.uniprot.org/annotation/VAR_019328|||http://purl.uniprot.org/annotation/VAR_057276|||http://purl.uniprot.org/annotation/VAR_061847
http://togogenome.org/gene/9606:MTDH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UE4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Activation of NF-kappa-B|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical|||Interaction with BCCIP|||Interaction with RELA|||Lumenal|||Lung-homing for mammary tumors|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein LYRIC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084533|||http://purl.uniprot.org/annotation/VAR_054661
http://togogenome.org/gene/9606:SLC22A9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVM8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Organic anion transporter 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233715|||http://purl.uniprot.org/annotation/VAR_036403|||http://purl.uniprot.org/annotation/VAR_036404|||http://purl.uniprot.org/annotation/VAR_036405|||http://purl.uniprot.org/annotation/VSP_036710|||http://purl.uniprot.org/annotation/VSP_036711
http://togogenome.org/gene/9606:TSNAX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99598                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Interaction with C1D|||Translin-associated protein X                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191686
http://togogenome.org/gene/9606:URGCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RAT5|||http://purl.uniprot.org/uniprot/B7Z7T1|||http://purl.uniprot.org/uniprot/Q8TCY9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Up-regulator of cell proliferation|||VLIG-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000337148|||http://purl.uniprot.org/annotation/VAR_043668|||http://purl.uniprot.org/annotation/VAR_051479|||http://purl.uniprot.org/annotation/VAR_051480|||http://purl.uniprot.org/annotation/VSP_033942|||http://purl.uniprot.org/annotation/VSP_047068|||http://purl.uniprot.org/annotation/VSP_052799
http://togogenome.org/gene/9606:NOTCH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UM47                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Basic residues|||Cleavage; by furin-like protease|||Cytoplasmic|||Disordered|||EGF-like 1|||EGF-like 10; calcium-binding|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13; calcium-binding|||EGF-like 14; calcium-binding|||EGF-like 15; calcium-binding|||EGF-like 16; calcium-binding|||EGF-like 17; calcium-binding|||EGF-like 18|||EGF-like 19|||EGF-like 2|||EGF-like 20|||EGF-like 21; calcium-binding|||EGF-like 22; calcium-binding|||EGF-like 23; calcium-binding|||EGF-like 24|||EGF-like 25|||EGF-like 26|||EGF-like 27|||EGF-like 28|||EGF-like 29; calcium-binding|||EGF-like 3|||EGF-like 30; calcium-binding|||EGF-like 31|||EGF-like 32|||EGF-like 33|||EGF-like 34|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like 6; calcium-binding|||EGF-like 7|||EGF-like 8; calcium-binding|||EGF-like 9|||Extracellular|||Helical|||In CADASIL1.|||In CADASIL1; impaired ligand-binding; strongly reduced signaling activity; no effect on cell membrane localization; reduced proteolytic processing.|||In CADASIL1; no effect on ligand-binding; no effect on cell membrane localization; reduced proteolytic processing.|||In CADASIL1; requires 2 nucleotide substitutions.|||In IMF2.|||In brain small-vessel-disease; exhibits increased NOTCH3 signaling in a ligand-independent fashion.|||LNR 1|||LNR 2|||LNR 3|||N-linked (GlcNAc...) asparagine|||Neurogenic locus notch homolog protein 3|||Notch 3 extracellular truncation|||Notch 3 intracellular domain|||Omega-N-methylarginine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007692|||http://purl.uniprot.org/annotation/PRO_0000007693|||http://purl.uniprot.org/annotation/PRO_0000007694|||http://purl.uniprot.org/annotation/VAR_012871|||http://purl.uniprot.org/annotation/VAR_012872|||http://purl.uniprot.org/annotation/VAR_012873|||http://purl.uniprot.org/annotation/VAR_012874|||http://purl.uniprot.org/annotation/VAR_012875|||http://purl.uniprot.org/annotation/VAR_012876|||http://purl.uniprot.org/annotation/VAR_012877|||http://purl.uniprot.org/annotation/VAR_012878|||http://purl.uniprot.org/annotation/VAR_012879|||http://purl.uniprot.org/annotation/VAR_012880|||http://purl.uniprot.org/annotation/VAR_012881|||http://purl.uniprot.org/annotation/VAR_012882|||http://purl.uniprot.org/annotation/VAR_012883|||http://purl.uniprot.org/annotation/VAR_012884|||http://purl.uniprot.org/annotation/VAR_012885|||http://purl.uniprot.org/annotation/VAR_012886|||http://purl.uniprot.org/annotation/VAR_012887|||http://purl.uniprot.org/annotation/VAR_012888|||http://purl.uniprot.org/annotation/VAR_012889|||http://purl.uniprot.org/annotation/VAR_012890|||http://purl.uniprot.org/annotation/VAR_012891|||http://purl.uniprot.org/annotation/VAR_012892|||http://purl.uniprot.org/annotation/VAR_012893|||http://purl.uniprot.org/annotation/VAR_012894|||http://purl.uniprot.org/annotation/VAR_012895|||http://purl.uniprot.org/annotation/VAR_012896|||http://purl.uniprot.org/annotation/VAR_012897|||http://purl.uniprot.org/annotation/VAR_012898|||http://purl.uniprot.org/annotation/VAR_012899|||http://purl.uniprot.org/annotation/VAR_012900|||http://purl.uniprot.org/annotation/VAR_012901|||http://purl.uniprot.org/annotation/VAR_044230|||http://purl.uniprot.org/annotation/VAR_044231|||http://purl.uniprot.org/annotation/VAR_044232|||http://purl.uniprot.org/annotation/VAR_044233|||http://purl.uniprot.org/annotation/VAR_044234|||http://purl.uniprot.org/annotation/VAR_044235|||http://purl.uniprot.org/annotation/VAR_044236|||http://purl.uniprot.org/annotation/VAR_044237|||http://purl.uniprot.org/annotation/VAR_044238|||http://purl.uniprot.org/annotation/VAR_044239|||http://purl.uniprot.org/annotation/VAR_044240|||http://purl.uniprot.org/annotation/VAR_044241|||http://purl.uniprot.org/annotation/VAR_044242|||http://purl.uniprot.org/annotation/VAR_044243|||http://purl.uniprot.org/annotation/VAR_044244|||http://purl.uniprot.org/annotation/VAR_044245|||http://purl.uniprot.org/annotation/VAR_044246|||http://purl.uniprot.org/annotation/VAR_044247|||http://purl.uniprot.org/annotation/VAR_044248|||http://purl.uniprot.org/annotation/VAR_044249|||http://purl.uniprot.org/annotation/VAR_044250|||http://purl.uniprot.org/annotation/VAR_044251|||http://purl.uniprot.org/annotation/VAR_044252|||http://purl.uniprot.org/annotation/VAR_044253|||http://purl.uniprot.org/annotation/VAR_044254|||http://purl.uniprot.org/annotation/VAR_044255|||http://purl.uniprot.org/annotation/VAR_044256|||http://purl.uniprot.org/annotation/VAR_044257|||http://purl.uniprot.org/annotation/VAR_044258|||http://purl.uniprot.org/annotation/VAR_044259|||http://purl.uniprot.org/annotation/VAR_044260|||http://purl.uniprot.org/annotation/VAR_044261|||http://purl.uniprot.org/annotation/VAR_044262|||http://purl.uniprot.org/annotation/VAR_044263|||http://purl.uniprot.org/annotation/VAR_044264|||http://purl.uniprot.org/annotation/VAR_044265|||http://purl.uniprot.org/annotation/VAR_044266|||http://purl.uniprot.org/annotation/VAR_044267|||http://purl.uniprot.org/annotation/VAR_044268|||http://purl.uniprot.org/annotation/VAR_044269|||http://purl.uniprot.org/annotation/VAR_044270|||http://purl.uniprot.org/annotation/VAR_044271|||http://purl.uniprot.org/annotation/VAR_044272|||http://purl.uniprot.org/annotation/VAR_044273|||http://purl.uniprot.org/annotation/VAR_044274|||http://purl.uniprot.org/annotation/VAR_044275|||http://purl.uniprot.org/annotation/VAR_044276|||http://purl.uniprot.org/annotation/VAR_044277|||http://purl.uniprot.org/annotation/VAR_044278|||http://purl.uniprot.org/annotation/VAR_044279|||http://purl.uniprot.org/annotation/VAR_044280|||http://purl.uniprot.org/annotation/VAR_044281|||http://purl.uniprot.org/annotation/VAR_044282|||http://purl.uniprot.org/annotation/VAR_044283|||http://purl.uniprot.org/annotation/VAR_044284|||http://purl.uniprot.org/annotation/VAR_044285|||http://purl.uniprot.org/annotation/VAR_044286|||http://purl.uniprot.org/annotation/VAR_044287|||http://purl.uniprot.org/annotation/VAR_044288|||http://purl.uniprot.org/annotation/VAR_044289|||http://purl.uniprot.org/annotation/VAR_044290|||http://purl.uniprot.org/annotation/VAR_044291|||http://purl.uniprot.org/annotation/VAR_044292|||http://purl.uniprot.org/annotation/VAR_044293|||http://purl.uniprot.org/annotation/VAR_044294|||http://purl.uniprot.org/annotation/VAR_044295|||http://purl.uniprot.org/annotation/VAR_044296|||http://purl.uniprot.org/annotation/VAR_044297|||http://purl.uniprot.org/annotation/VAR_044298|||http://purl.uniprot.org/annotation/VAR_044299|||http://purl.uniprot.org/annotation/VAR_044300|||http://purl.uniprot.org/annotation/VAR_044301|||http://purl.uniprot.org/annotation/VAR_044302|||http://purl.uniprot.org/annotation/VAR_044303|||http://purl.uniprot.org/annotation/VAR_044304|||http://purl.uniprot.org/annotation/VAR_044305|||http://purl.uniprot.org/annotation/VAR_044306|||http://purl.uniprot.org/annotation/VAR_044307|||http://purl.uniprot.org/annotation/VAR_044308|||http://purl.uniprot.org/annotation/VAR_044309|||http://purl.uniprot.org/annotation/VAR_044310|||http://purl.uniprot.org/annotation/VAR_044311|||http://purl.uniprot.org/annotation/VAR_044312|||http://purl.uniprot.org/annotation/VAR_044313|||http://purl.uniprot.org/annotation/VAR_044314|||http://purl.uniprot.org/annotation/VAR_044315|||http://purl.uniprot.org/annotation/VAR_044316|||http://purl.uniprot.org/annotation/VAR_044317|||http://purl.uniprot.org/annotation/VAR_044318|||http://purl.uniprot.org/annotation/VAR_069927|||http://purl.uniprot.org/annotation/VAR_072080
http://togogenome.org/gene/9606:HCN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P1Z3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||Interaction with KCTD3|||Involved in subunit assembly|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pore-forming; Name=Segment H5|||Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054114|||http://purl.uniprot.org/annotation/VAR_048746
http://togogenome.org/gene/9606:SLC39A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q504Y0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||XEXPHE-motif|||Zinc transporter ZIP12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312497|||http://purl.uniprot.org/annotation/VAR_037516|||http://purl.uniprot.org/annotation/VAR_037517|||http://purl.uniprot.org/annotation/VAR_037518|||http://purl.uniprot.org/annotation/VAR_037519|||http://purl.uniprot.org/annotation/VAR_037520|||http://purl.uniprot.org/annotation/VSP_029847|||http://purl.uniprot.org/annotation/VSP_029848|||http://purl.uniprot.org/annotation/VSP_029849|||http://purl.uniprot.org/annotation/VSP_029850|||http://purl.uniprot.org/annotation/VSP_057594
http://togogenome.org/gene/9606:MRPL44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9J2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  DRBM|||In COXPD16.|||Large ribosomal subunit protein mL44|||Mitochondrion|||RNase III                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030821|||http://purl.uniprot.org/annotation/VAR_034464|||http://purl.uniprot.org/annotation/VAR_070568
http://togogenome.org/gene/9606:SLC35F6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N357                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Transmembrane                                                                                  ^@                                                                                  Disordered|||EamA|||Helical|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Solute carrier family 35 member F6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232514
http://togogenome.org/gene/9606:APLP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51693                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Peptide|||Region|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Amyloid beta precursor like protein 1|||Basic and acidic residues|||Basolateral sorting signal|||C30|||Clathrin-binding|||Cleavage; by caspase-3|||Collagen-binding|||CuBD subdomain|||Cytoplasmic|||Disordered|||E1|||E2|||Extracellular|||GFLD subdomain|||Helical|||Heparin-binding|||In isoform 2.|||Interaction with DAB1|||Interaction with DAB2|||N-linked (GlcNAc...) asparagine|||NPXY motif; contains endocytosis signal|||O-glycosylated at three sites|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Reduced affinity for heparin. Reduces homodimerization.|||Strongly reduced affinity for heparin. Strongly reduced homodimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000203|||http://purl.uniprot.org/annotation/PRO_0000000204|||http://purl.uniprot.org/annotation/VSP_039100
http://togogenome.org/gene/9606:ITPKA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23677                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-binding|||Decreases to 12% of kinase activity.|||Decreases to 44% of kinase activity.|||Decreases to 80% of kinase activity.|||Disordered|||Inositol-trisphosphate 3-kinase A|||Loss of kinase activity.|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Required for cytoskeleton location                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066865
http://togogenome.org/gene/9606:ESRRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5E9|||http://purl.uniprot.org/uniprot/C0SQ93|||http://purl.uniprot.org/uniprot/F1D8R5|||http://purl.uniprot.org/uniprot/F1D8R6|||http://purl.uniprot.org/uniprot/P62508                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  4-fold increase in transcriptional activity.|||Abolishes sumoylation. 7-fold increase in transcriptional activity.|||Abolishes sumoylation. Increased transcriptional activity.|||Disordered|||Estrogen-related receptor gamma|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||NR C4-type|||NR LBD|||No change in sumoylation nor transcriptional activity.|||No effect on transcriptional activity.|||Nuclear receptor|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053665|||http://purl.uniprot.org/annotation/VAR_019229|||http://purl.uniprot.org/annotation/VSP_003702|||http://purl.uniprot.org/annotation/VSP_013301|||http://purl.uniprot.org/annotation/VSP_045980|||http://purl.uniprot.org/annotation/VSP_047156
http://togogenome.org/gene/9606:NOA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC60                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CP-type G|||Disordered|||In a breast cancer sample; somatic mutation.|||Nitric oxide-associated protein 1|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232510|||http://purl.uniprot.org/annotation/VAR_025941|||http://purl.uniprot.org/annotation/VAR_025942|||http://purl.uniprot.org/annotation/VAR_035500
http://togogenome.org/gene/9606:ZNF33B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06732                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 33B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047334|||http://purl.uniprot.org/annotation/VAR_024192|||http://purl.uniprot.org/annotation/VAR_052752
http://togogenome.org/gene/9606:EPPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NYB9|||http://purl.uniprot.org/uniprot/B2R4Q0|||http://purl.uniprot.org/uniprot/O95925                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  BPTI/Kunitz inhibitor|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-123.|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-110 and A-127.|||Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1; when associated with A-123 and A-127.|||Eppin|||In isoform 2.|||In isoform 3.|||Interaction with LTF|||Interaction with SEMG1|||Loss of effect on KLK3 activity.|||Reduces the binding to SEMG1 by 45%.|||Reduces the binding to SEMG1 by 68% and to LTF by 73%.|||Reduces the binding to SEMG1 by 68%.|||WAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041378|||http://purl.uniprot.org/annotation/PRO_5002780091|||http://purl.uniprot.org/annotation/PRO_5036073199|||http://purl.uniprot.org/annotation/VAR_024696|||http://purl.uniprot.org/annotation/VAR_052950|||http://purl.uniprot.org/annotation/VSP_006755|||http://purl.uniprot.org/annotation/VSP_043679
http://togogenome.org/gene/9606:C6orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T4I8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Putative uncharacterized protein C6orf52                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000295687|||http://purl.uniprot.org/annotation/VAR_033318|||http://purl.uniprot.org/annotation/VSP_026991
http://togogenome.org/gene/9606:STX1A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16623|||http://purl.uniprot.org/uniprot/Q75ME0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Complete loss of sumoylation; when associated with R-252 and R-253.|||Complete loss of sumoylation; when associated with R-252 and R-256.|||Complete loss of sumoylation; when associated with R-253 and R-256.|||Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphoserine; by DAPK1|||Syntaxin-1A|||T-SNARE coiled-coil homology|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210186|||http://purl.uniprot.org/annotation/VSP_006338|||http://purl.uniprot.org/annotation/VSP_006339
http://togogenome.org/gene/9606:KLHL12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53G59                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ubiquitination by the SCF(FBXL17) complex.|||Abolishes interaction with SEC31A and subsequent monoubiquitination of SEC31A. Abolishes ubiquitination of PEF1.|||BACK|||BTB|||In isoform 2.|||Increased recognition and ubiquitination by the SCF(FBXL17) complex.|||Interaction with DVL3|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234349|||http://purl.uniprot.org/annotation/VAR_050049|||http://purl.uniprot.org/annotation/VSP_042975
http://togogenome.org/gene/9606:ARL17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J5U5|||http://purl.uniprot.org/uniprot/A8K0M5|||http://purl.uniprot.org/uniprot/Q8IVW1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 17|||ADP-ribosylation factor-like protein 17 C-terminal|||In isoform 2.|||In isoform 4.|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207482|||http://purl.uniprot.org/annotation/VAR_017170|||http://purl.uniprot.org/annotation/VSP_008753|||http://purl.uniprot.org/annotation/VSP_008756
http://togogenome.org/gene/9606:KCP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWJ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 4.|||Kielin/chordin-like protein|||N-linked (GlcNAc...) asparagine|||Polar residues|||TIL|||VWFC 1|||VWFC 10|||VWFC 11|||VWFC 12|||VWFC 13|||VWFC 14|||VWFC 15|||VWFC 16|||VWFC 2|||VWFC 3|||VWFC 4|||VWFC 5|||VWFC 6|||VWFC 7|||VWFC 8|||VWFC 9|||VWFD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318586|||http://purl.uniprot.org/annotation/VAR_038783|||http://purl.uniprot.org/annotation/VAR_059625|||http://purl.uniprot.org/annotation/VAR_059626|||http://purl.uniprot.org/annotation/VAR_059627|||http://purl.uniprot.org/annotation/VSP_059352|||http://purl.uniprot.org/annotation/VSP_059353|||http://purl.uniprot.org/annotation/VSP_059354|||http://purl.uniprot.org/annotation/VSP_059355|||http://purl.uniprot.org/annotation/VSP_059356|||http://purl.uniprot.org/annotation/VSP_059357
http://togogenome.org/gene/9606:MAN1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60476                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB|||N-acetylthreonine|||N-linked (GlcNAc...) asparagine|||Proton donor|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210312
http://togogenome.org/gene/9606:KRTAP10-5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60370                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||22 X 5 AA repeats of C-C-X(3)|||3|||4|||5|||6|||7|||8|||9|||Keratin-associated protein 10-5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185213|||http://purl.uniprot.org/annotation/VAR_017696|||http://purl.uniprot.org/annotation/VAR_017697|||http://purl.uniprot.org/annotation/VAR_047505|||http://purl.uniprot.org/annotation/VAR_047506|||http://purl.uniprot.org/annotation/VAR_047507|||http://purl.uniprot.org/annotation/VAR_062113
http://togogenome.org/gene/9606:G6PC3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIG5|||http://purl.uniprot.org/uniprot/K7EJC5|||http://purl.uniprot.org/uniprot/Q9BUM1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Glucose-6-phosphatase 3|||Helical|||In DURSS and SCN4; complete loss of activity.|||In SCN4.|||In SCN4; complete loss of activity.|||In SCN4; complete loss of activity; peripheral-blood patient neutrophils have an increased rate of spontaneous apoptosis; transmission electron microscopy of patient bone marrow cells shows an enlarged rough endoplasmic reticulum in myeloid progenitor cells consistent with increased ER stress.|||In SCN4; complete loss of activity; purified neutrophils from patients have higher levels of spontaneous and staurosporine-induced apoptosis than controls.|||In SCN4; partial loss of activity.|||In SCN4; purified neutrophils from patients have higher levels of spontaneous and staurosporine-induced apoptosis than controls.|||In SCN4; the patient also carries mutation Thr-166 in ELANE; complete loss of activity.|||Loss of catalytic activity.|||Lumenal|||Nucleophile|||Phosphatidic acid phosphatase type 2/haloperoxidase|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334512|||http://purl.uniprot.org/annotation/VAR_043378|||http://purl.uniprot.org/annotation/VAR_055156|||http://purl.uniprot.org/annotation/VAR_055157|||http://purl.uniprot.org/annotation/VAR_055158|||http://purl.uniprot.org/annotation/VAR_064508|||http://purl.uniprot.org/annotation/VAR_064509|||http://purl.uniprot.org/annotation/VAR_064510|||http://purl.uniprot.org/annotation/VAR_064511|||http://purl.uniprot.org/annotation/VAR_072753|||http://purl.uniprot.org/annotation/VAR_072754|||http://purl.uniprot.org/annotation/VAR_072755|||http://purl.uniprot.org/annotation/VAR_072756|||http://purl.uniprot.org/annotation/VAR_072757|||http://purl.uniprot.org/annotation/VAR_072758|||http://purl.uniprot.org/annotation/VAR_072759|||http://purl.uniprot.org/annotation/VAR_072760|||http://purl.uniprot.org/annotation/VAR_072761|||http://purl.uniprot.org/annotation/VAR_073174|||http://purl.uniprot.org/annotation/VAR_073175|||http://purl.uniprot.org/annotation/VAR_073176|||http://purl.uniprot.org/annotation/VAR_073177|||http://purl.uniprot.org/annotation/VAR_073178
http://togogenome.org/gene/9606:POGK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DF62|||http://purl.uniprot.org/uniprot/Q9P215                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||DDE-1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HTH CENPB-type|||KRAB|||Pogo transposable element with KRAB domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126131
http://togogenome.org/gene/9606:AQR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60306                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Decreased affinity for ATP and ADP. Loss of RNA helicase activity. Disrupts spliceosomal pre-mRNA splicing and leads to the accumulation of spliceosomal B complexes.|||Disordered|||Helical region with structural similarity to ARM repeat domains|||N6-acetyllysine|||Polar residues|||RNA helicase aquarius|||Required for assembly of the IB complex|||Strongly reduced RNA helicase activity. No effect on ATPase activity. No effect on spliceosomal pre-mRNA splicing.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252389
http://togogenome.org/gene/9606:ACKR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16570|||http://purl.uniprot.org/uniprot/Q5Y7A1|||http://purl.uniprot.org/uniprot/Q5Y7A2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Antigen Fy(b).|||Antigen Fy(x).|||Atypical chemokine receptor 1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 1.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000152585|||http://purl.uniprot.org/annotation/VAR_003480|||http://purl.uniprot.org/annotation/VAR_015068|||http://purl.uniprot.org/annotation/VAR_015069|||http://purl.uniprot.org/annotation/VAR_044116|||http://purl.uniprot.org/annotation/VAR_044117|||http://purl.uniprot.org/annotation/VSP_001323
http://togogenome.org/gene/9606:SIRPB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTG0|||http://purl.uniprot.org/uniprot/Q5JXA9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type 1|||Ig-like V-type 2|||In isoform 2 and isoform 3.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Signal-regulatory protein beta-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338629|||http://purl.uniprot.org/annotation/PRO_5002790080|||http://purl.uniprot.org/annotation/VAR_043814|||http://purl.uniprot.org/annotation/VAR_043815|||http://purl.uniprot.org/annotation/VAR_043816|||http://purl.uniprot.org/annotation/VSP_034065|||http://purl.uniprot.org/annotation/VSP_034066
http://togogenome.org/gene/9606:GALC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQV0|||http://purl.uniprot.org/uniprot/P54803                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Galactocerebrosidase|||Glycosyl hydrolase family 59 central|||In KRB.|||In KRB; Arab patients.|||In KRB; adult.|||In KRB; adult; reduction of activity; when associated with V-2105.|||In KRB; bilateral cherry red spots.|||In KRB; infantile.|||In KRB; infantile; Druze patients.|||In KRB; infantile; significant reduction of activity.|||In KRB; late infantile.|||In KRB; loss of activity.|||In KRB; significant reduction of activity.|||In KRB; unknown pathological significance.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Nucleophile|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012230|||http://purl.uniprot.org/annotation/PRO_5014220091|||http://purl.uniprot.org/annotation/VAR_003380|||http://purl.uniprot.org/annotation/VAR_003381|||http://purl.uniprot.org/annotation/VAR_003382|||http://purl.uniprot.org/annotation/VAR_003383|||http://purl.uniprot.org/annotation/VAR_003384|||http://purl.uniprot.org/annotation/VAR_003385|||http://purl.uniprot.org/annotation/VAR_003386|||http://purl.uniprot.org/annotation/VAR_003387|||http://purl.uniprot.org/annotation/VAR_003388|||http://purl.uniprot.org/annotation/VAR_003389|||http://purl.uniprot.org/annotation/VAR_003390|||http://purl.uniprot.org/annotation/VAR_003391|||http://purl.uniprot.org/annotation/VAR_003392|||http://purl.uniprot.org/annotation/VAR_003393|||http://purl.uniprot.org/annotation/VAR_003394|||http://purl.uniprot.org/annotation/VAR_003395|||http://purl.uniprot.org/annotation/VAR_003396|||http://purl.uniprot.org/annotation/VAR_003397|||http://purl.uniprot.org/annotation/VAR_003398|||http://purl.uniprot.org/annotation/VAR_003399|||http://purl.uniprot.org/annotation/VAR_003400|||http://purl.uniprot.org/annotation/VAR_003401|||http://purl.uniprot.org/annotation/VAR_003402|||http://purl.uniprot.org/annotation/VAR_003403|||http://purl.uniprot.org/annotation/VAR_003404|||http://purl.uniprot.org/annotation/VAR_003405|||http://purl.uniprot.org/annotation/VAR_003406|||http://purl.uniprot.org/annotation/VAR_003407|||http://purl.uniprot.org/annotation/VAR_013956|||http://purl.uniprot.org/annotation/VAR_013957|||http://purl.uniprot.org/annotation/VAR_013958|||http://purl.uniprot.org/annotation/VAR_013959|||http://purl.uniprot.org/annotation/VAR_013960|||http://purl.uniprot.org/annotation/VAR_013961|||http://purl.uniprot.org/annotation/VAR_013962|||http://purl.uniprot.org/annotation/VAR_013963|||http://purl.uniprot.org/annotation/VAR_013964|||http://purl.uniprot.org/annotation/VAR_013965|||http://purl.uniprot.org/annotation/VAR_013966|||http://purl.uniprot.org/annotation/VAR_013967|||http://purl.uniprot.org/annotation/VAR_013968|||http://purl.uniprot.org/annotation/VAR_013969|||http://purl.uniprot.org/annotation/VAR_064430|||http://purl.uniprot.org/annotation/VAR_064431|||http://purl.uniprot.org/annotation/VAR_064432|||http://purl.uniprot.org/annotation/VAR_064433|||http://purl.uniprot.org/annotation/VAR_064434|||http://purl.uniprot.org/annotation/VAR_064435|||http://purl.uniprot.org/annotation/VAR_064436|||http://purl.uniprot.org/annotation/VAR_064437|||http://purl.uniprot.org/annotation/VAR_069512|||http://purl.uniprot.org/annotation/VSP_036974|||http://purl.uniprot.org/annotation/VSP_036975|||http://purl.uniprot.org/annotation/VSP_036976|||http://purl.uniprot.org/annotation/VSP_036977
http://togogenome.org/gene/9606:CLK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRI8|||http://purl.uniprot.org/uniprot/P49761                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Dual specificity protein kinase CLK3|||In isoform 1, isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085870|||http://purl.uniprot.org/annotation/VAR_040413|||http://purl.uniprot.org/annotation/VAR_045579|||http://purl.uniprot.org/annotation/VAR_045580|||http://purl.uniprot.org/annotation/VSP_004858|||http://purl.uniprot.org/annotation/VSP_004859|||http://purl.uniprot.org/annotation/VSP_004860|||http://purl.uniprot.org/annotation/VSP_026138
http://togogenome.org/gene/9606:ADGRL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A6I8PTT2|||http://purl.uniprot.org/uniprot/O95490                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Adhesion G protein-coupled receptor L2|||Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Found in a child with sporadic epilepsy; unknown pathological significance.|||G-protein coupled receptors family 2 profile 1|||G-protein coupled receptors family 2 profile 2|||GPS|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 2, isoform 3, isoform 4 and isoform 7.|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 6 and isoform 7.|||N-linked (GlcNAc...) asparagine|||Olfactomedin-like|||Phosphoserine|||Polar residues|||SUEL-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012910|||http://purl.uniprot.org/annotation/PRO_5040080844|||http://purl.uniprot.org/annotation/VAR_077836|||http://purl.uniprot.org/annotation/VSP_010104|||http://purl.uniprot.org/annotation/VSP_010105|||http://purl.uniprot.org/annotation/VSP_010106|||http://purl.uniprot.org/annotation/VSP_010107|||http://purl.uniprot.org/annotation/VSP_010108|||http://purl.uniprot.org/annotation/VSP_010109|||http://purl.uniprot.org/annotation/VSP_042267
http://togogenome.org/gene/9606:MYCBPAP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZQ1|||http://purl.uniprot.org/uniprot/Q8TBZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||MYCBP-associated protein|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302877|||http://purl.uniprot.org/annotation/VAR_035003|||http://purl.uniprot.org/annotation/VAR_035004|||http://purl.uniprot.org/annotation/VAR_035005
http://togogenome.org/gene/9606:HARS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DDD8|||http://purl.uniprot.org/uniprot/B4E1C5|||http://purl.uniprot.org/uniprot/P12081                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Histidine--tRNA ligase, cytoplasmic|||In CMT2W; fails to complement deletion of the yeast ortholog; decreases histidine-tRNA ligase activity; increases in the KM for ATP binding; does not disrupt dimerization.|||In CMT2W; has a neurotoxic effect in an animal model; results in loss of function.|||In CMT2W; hypomorphic variant.|||In CMT2W; loss-of-function variant.|||In CMT2W; unknown pathological significance.|||In CMT2W; unknown pathological significance; fails to complement deletion of the yeast ortholog; decreases histidine-tRNA ligase activity; increases in the KM for ATP binding; does not disrupt dimerization.|||In USH3B; unknown pathological significance.|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||N-acetylalanine|||Phosphoserine|||Removed|||WHEP-TRS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000136332|||http://purl.uniprot.org/annotation/VAR_061908|||http://purl.uniprot.org/annotation/VAR_067918|||http://purl.uniprot.org/annotation/VAR_069021|||http://purl.uniprot.org/annotation/VAR_069022|||http://purl.uniprot.org/annotation/VAR_069023|||http://purl.uniprot.org/annotation/VAR_069024|||http://purl.uniprot.org/annotation/VAR_069025|||http://purl.uniprot.org/annotation/VAR_069026|||http://purl.uniprot.org/annotation/VAR_075064|||http://purl.uniprot.org/annotation/VAR_075065|||http://purl.uniprot.org/annotation/VAR_075066|||http://purl.uniprot.org/annotation/VAR_075067|||http://purl.uniprot.org/annotation/VAR_083003|||http://purl.uniprot.org/annotation/VAR_083004|||http://purl.uniprot.org/annotation/VAR_083005|||http://purl.uniprot.org/annotation/VSP_045118|||http://purl.uniprot.org/annotation/VSP_046662
http://togogenome.org/gene/9606:DDX19B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0U4B4U6|||http://purl.uniprot.org/uniprot/B4DL69|||http://purl.uniprot.org/uniprot/Q9UMR2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX19B|||C-terminal lobe|||DEAD box|||DEAD-box RNA helicase Q|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||Impairs interaction with NUP214 and RNA.|||Impairs interaction with NUP214.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of activity.|||N-acetylalanine|||N-terminal helix|||N-terminal lobe|||Q motif|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055022|||http://purl.uniprot.org/annotation/VAR_052160|||http://purl.uniprot.org/annotation/VSP_015239|||http://purl.uniprot.org/annotation/VSP_041347|||http://purl.uniprot.org/annotation/VSP_044727
http://togogenome.org/gene/9606:DENND1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3S1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Almost completely abolishes AP2B1-binding.|||Causes only a slight reduction in AP2B1-binding.|||Clathrin box|||DENN domain-containing protein 1B|||Disordered|||FXDXF motif|||Greatly reduce AP2B1-binding.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4, isoform 2 and isoform 1.|||In isoform 4.|||No effect.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||cDENN|||dDENN|||uDENN                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304674|||http://purl.uniprot.org/annotation/VAR_035055|||http://purl.uniprot.org/annotation/VSP_028082|||http://purl.uniprot.org/annotation/VSP_028083|||http://purl.uniprot.org/annotation/VSP_028084|||http://purl.uniprot.org/annotation/VSP_028085|||http://purl.uniprot.org/annotation/VSP_034515
http://togogenome.org/gene/9606:PHF5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTV0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Alters the structure of the presumed branchpoint (BP) adenosine binding pocket within the splicing factor SF3B complex which may lead to decreased binding affinity and thus affect pre-mRNA splicing.|||Interaction with RNA|||Interaction with SF3B1 and SF3B3|||Interaction with SF3B3|||N-acetylalanine|||N6-acetyllysine|||No apparent effect on cell growth, localization of SF3B1 protein or formation of nuclear speckles. Alters the structure of the presumed branchpoint (BP) adenosine binding pocket within the splicing factor SF3B complex which may lead to decreased binding affinity and thus affect pre-mRNA splicing.|||PHD finger-like domain-containing protein 5A|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218716
http://togogenome.org/gene/9606:ZNF860                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NHJ4                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; degenerate|||C2H2-type 14|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Zinc finger protein 860                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000350815
http://togogenome.org/gene/9606:UBE2K                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSH4|||http://purl.uniprot.org/uniprot/B4DIZ2|||http://purl.uniprot.org/uniprot/P61086                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased lysine reactivity and impaired formation of free polyubiquitin chains.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl thioester intermediate|||In isoform 2.|||In isoform 3.|||N-acetylalanine|||N6-acetyllysine; alternate|||Phosphoserine|||Removed|||UBA|||UBC core|||Ubiquitin-conjugating enzyme E2 K                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082443|||http://purl.uniprot.org/annotation/PRO_5010105241|||http://purl.uniprot.org/annotation/VSP_011798|||http://purl.uniprot.org/annotation/VSP_046211
http://togogenome.org/gene/9606:MADCAM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13477                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  1; truncated|||2|||3|||4|||5|||5.5 X 8 AA tandem repeats of [PS]-P-D-T-T-S-[QP]-E|||6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like 1|||Ig-like 2|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 4.|||Mucin-like|||Mucosal addressin cell adhesion molecule 1|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014853|||http://purl.uniprot.org/annotation/VAR_017580|||http://purl.uniprot.org/annotation/VAR_047901|||http://purl.uniprot.org/annotation/VSP_043202|||http://purl.uniprot.org/annotation/VSP_047694|||http://purl.uniprot.org/annotation/VSP_050014
http://togogenome.org/gene/9606:THSD7A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UPZ6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Polar residues|||TSP type-1 1|||TSP type-1 10|||TSP type-1 11|||TSP type-1 12|||TSP type-1 13|||TSP type-1 14|||TSP type-1 15|||TSP type-1 16|||TSP type-1 17|||TSP type-1 18|||TSP type-1 19|||TSP type-1 2|||TSP type-1 3|||TSP type-1 4|||TSP type-1 5|||TSP type-1 6|||TSP type-1 7|||TSP type-1 8|||TSP type-1 9|||Thrombospondin type-1 domain-containing protein 7A|||Thrombospondin type-1 domain-containing protein 7A, soluble form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000256126|||http://purl.uniprot.org/annotation/PRO_0000444430|||http://purl.uniprot.org/annotation/VAR_057366|||http://purl.uniprot.org/annotation/VAR_057367|||http://purl.uniprot.org/annotation/VAR_068676|||http://purl.uniprot.org/annotation/VAR_068677|||http://purl.uniprot.org/annotation/VAR_068678
http://togogenome.org/gene/9606:F8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00451                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  B|||Cleavage (activation)|||Cleavage; by thrombin|||Coagulation factor VIII|||Disordered|||F5/8 type A 1|||F5/8 type A 2|||F5/8 type A 3|||F5/8 type C 1|||F5/8 type C 2|||Factor VIII B chain|||Factor VIIIa heavy chain, 200 kDa isoform|||Factor VIIIa heavy chain, 92 kDa isoform|||Factor VIIIa light chain|||In HEMA.|||In HEMA; East Hartford; severe/moderate/mild; abolishes thrombin cleavage at the light chain.|||In HEMA; Kumamoto; mild/moderate; abolishes the normal cleavage by thrombin.|||In HEMA; Okayama; moderate/severe; abolishes the normal cleavage by thrombin.|||In HEMA; mild familial.|||In HEMA; mild sporadic.|||In HEMA; mild-moderate/severe.|||In HEMA; mild-moderate; affinity for VWF reduced 8-fold.|||In HEMA; mild.|||In HEMA; mild/moderate.|||In HEMA; mild/moderate; secretion impaired.|||In HEMA; mild/severe.|||In HEMA; mild; abolishes normal cleavage by thrombin.|||In HEMA; mild; abolishes thrombin cleavage at the light chain.|||In HEMA; mild; may cause reduced phospholipid binding.|||In HEMA; mild; secretion impaired.|||In HEMA; mild; unknown pathological significance; decreases binding with VWF and phospholipid; no effect on reaction with F9, F2 and F10; decreases specific activity by 30%; patient develops inhibitor alloantibodies.|||In HEMA; moderate-severe.|||In HEMA; moderate.|||In HEMA; moderate/mild.|||In HEMA; moderate/mild; may cause reduced phospholipid binding.|||In HEMA; moderate/severe.|||In HEMA; moderate; affinity for VWF reduced 80-fold.|||In HEMA; not severe.|||In HEMA; requires 2 nucleotide substitutions.|||In HEMA; severe familial.|||In HEMA; severe sporadic.|||In HEMA; severe sporadic/moderate.|||In HEMA; severe.|||In HEMA; severe/mild.|||In HEMA; severe/mild; affinity for VWF reduced 3-fold.|||In HEMA; severe/moderate.|||In HEMA; severe/moderate/mild.|||In HEMA; severe/moderate; may cause reduced phospholipid binding.|||In HEMA; severe; abolishes the normal cleavage by thrombin.|||In HEMA; sporadic.|||In HEMA; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Plastocyanin-like 1|||Plastocyanin-like 2|||Plastocyanin-like 3|||Plastocyanin-like 4|||Plastocyanin-like 5|||Plastocyanin-like 6|||Sulfotyrosine                                                                                  ^@                                                                                  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uniprot.org/annotation/VAR_028667|||http://purl.uniprot.org/annotation/VAR_028668|||http://purl.uniprot.org/annotation/VAR_028669|||http://purl.uniprot.org/annotation/VAR_028670|||http://purl.uniprot.org/annotation/VAR_028671|||http://purl.uniprot.org/annotation/VAR_028672|||http://purl.uniprot.org/annotation/VAR_028673|||http://purl.uniprot.org/annotation/VAR_028674|||http://purl.uniprot.org/annotation/VAR_028675|||http://purl.uniprot.org/annotation/VAR_028676|||http://purl.uniprot.org/annotation/VAR_028677|||http://purl.uniprot.org/annotation/VAR_028678|||http://purl.uniprot.org/annotation/VAR_028679|||http://purl.uniprot.org/annotation/VAR_028680|||http://purl.uniprot.org/annotation/VAR_028681|||http://purl.uniprot.org/annotation/VAR_028682|||http://purl.uniprot.org/annotation/VAR_028683|||http://purl.uniprot.org/annotation/VAR_028684|||http://purl.uniprot.org/annotation/VAR_028685|||http://purl.uniprot.org/annotation/VAR_028686|||http://purl.uniprot.org/annotation/VAR_028687|||http://purl.uniprot.org/annotation/VAR_028688|||http://purl.uniprot.org/annotation/VAR_028689|||http://purl.uniprot.org/annotation/VAR_028691|||http://purl.uniprot.org/annotation/VAR_028692|||http://purl.uniprot.org/annotation/VAR_028693|||http://purl.uniprot.org/annotation/VAR_028694|||http://purl.uniprot.org/annotation/VAR_028695|||http://purl.uniprot.org/annotation/VAR_028696|||http://purl.uniprot.org/annotation/VAR_028697|||http://purl.uniprot.org/annotation/VAR_028698|||http://purl.uniprot.org/annotation/VAR_028699|||http://purl.uniprot.org/annotation/VAR_028700|||http://purl.uniprot.org/annotation/VAR_028701|||http://purl.uniprot.org/annotation/VAR_028702|||http://purl.uniprot.org/annotation/VAR_028703|||http://purl.uniprot.org/annotation/VAR_028704|||http://purl.uniprot.org/annotation/VAR_028705|||http://purl.uniprot.org/annotation/VAR_028706|||http://purl.uniprot.org/annotation/VAR_028707|||http://purl.uniprot.org/annotation/VAR_028708|||http://purl.uniprot.org/annotation/VAR_028709|||http://purl.uniprot.org/annotation/VAR_028710|||http://purl.uniprot.org/annotation/VAR_028711|||http://purl.uniprot.org/annotation/VAR_028712|||http://purl.uniprot.org/annotation/VAR_028713|||http://purl.uniprot.org/annotation/VAR_028714|||http://purl.uniprot.org/annotation/VAR_028715|||http://purl.uniprot.org/annotation/VAR_028716|||http://purl.uniprot.org/annotation/VAR_048438|||http://purl.uniprot.org/annotation/VAR_065303|||http://purl.uniprot.org/annotation/VAR_065304|||http://purl.uniprot.org/annotation/VAR_065305|||http://purl.uniprot.org/annotation/VAR_065306|||http://purl.uniprot.org/annotation/VAR_065307|||http://purl.uniprot.org/annotation/VAR_065308|||http://purl.uniprot.org/annotation/VAR_065309|||http://purl.uniprot.org/annotation/VAR_065310|||http://purl.uniprot.org/annotation/VAR_065311|||http://purl.uniprot.org/annotation/VAR_065312|||http://purl.uniprot.org/annotation/VAR_065313|||http://purl.uniprot.org/annotation/VAR_065314|||http://purl.uniprot.org/annotation/VAR_065315|||http://purl.uniprot.org/annotation/VAR_065316|||http://purl.uniprot.org/annotation/VAR_065317|||http://purl.uniprot.org/annotation/VAR_065318|||http://purl.uniprot.org/annotation/VAR_065319|||http://purl.uniprot.org/annotation/VAR_065320|||http://purl.uniprot.org/annotation/VAR_065321|||http://purl.uniprot.org/annotation/VAR_065322|||http://purl.uniprot.org/annotation/VAR_065323|||http://purl.uniprot.org/annotation/VAR_065324|||http://purl.uniprot.org/annotation/VAR_065325|||http://purl.uniprot.org/annotation/VAR_075624|||http://purl.uniprot.org/annotation/VSP_042656|||http://purl.uniprot.org/annotation/VSP_042657
http://togogenome.org/gene/9606:NKIRAS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYS0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Effector region|||Interactions with NFKBIA and NFKBIB|||Loss of function.|||NF-kappa-B inhibitor-interacting Ras-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225675
http://togogenome.org/gene/9606:INSYN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMK8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein INSYN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349183
http://togogenome.org/gene/9606:MLPH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BV36                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes RAB27A binding.|||Basic and acidic residues|||Decreases RAB27A binding.|||Disordered|||FYVE-type|||In GS3; abolishes RAB27A binding.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Melanophilin|||Polar residues|||RabBD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190222|||http://purl.uniprot.org/annotation/VAR_015690|||http://purl.uniprot.org/annotation/VAR_015691|||http://purl.uniprot.org/annotation/VAR_015692|||http://purl.uniprot.org/annotation/VAR_015693|||http://purl.uniprot.org/annotation/VAR_015694|||http://purl.uniprot.org/annotation/VAR_015695|||http://purl.uniprot.org/annotation/VAR_018724|||http://purl.uniprot.org/annotation/VAR_038410|||http://purl.uniprot.org/annotation/VAR_061754|||http://purl.uniprot.org/annotation/VSP_007554|||http://purl.uniprot.org/annotation/VSP_042158|||http://purl.uniprot.org/annotation/VSP_042159|||http://purl.uniprot.org/annotation/VSP_054367|||http://purl.uniprot.org/annotation/VSP_054368|||http://purl.uniprot.org/annotation/VSP_055730
http://togogenome.org/gene/9606:CCDC116                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYX3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Coiled-coil domain-containing protein 116|||Disordered|||In isoform 1.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254052|||http://purl.uniprot.org/annotation/VAR_028803|||http://purl.uniprot.org/annotation/VAR_028804|||http://purl.uniprot.org/annotation/VAR_028805|||http://purl.uniprot.org/annotation/VAR_028806|||http://purl.uniprot.org/annotation/VAR_028807|||http://purl.uniprot.org/annotation/VAR_061578|||http://purl.uniprot.org/annotation/VSP_059645|||http://purl.uniprot.org/annotation/VSP_059646
http://togogenome.org/gene/9606:SHC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29353                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alters interaction with GRB2; isoform p52Shc (in vitro).|||CH1|||Disordered|||In isoform 5.|||In isoform 7 and isoform 6.|||In isoform p46Shc.|||In isoform p52Shc and isoform 7.|||N-acetylmethionine|||N6-acetyllysine|||No effect on interaction with GRB2; isoform p52Shc (in vitro).|||PID|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SH2|||SHC-transforming protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097731|||http://purl.uniprot.org/annotation/VAR_042428|||http://purl.uniprot.org/annotation/VAR_051353|||http://purl.uniprot.org/annotation/VSP_016107|||http://purl.uniprot.org/annotation/VSP_016108|||http://purl.uniprot.org/annotation/VSP_040090|||http://purl.uniprot.org/annotation/VSP_040091|||http://purl.uniprot.org/annotation/VSP_040092
http://togogenome.org/gene/9606:MACROH2A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J4J7|||http://purl.uniprot.org/uniprot/O75367                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Core histone macro-H2A.1|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||Histone H2A|||Histone H2A C-terminal|||Histone H2A/H2B/H3|||In isoform 2 and isoform 3.|||In isoform 3.|||Macro|||N6,N6-dimethyllysine; alternate|||N6-acetyllysine; alternate|||N6-lactoyllysine; alternate|||N6-methyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055318|||http://purl.uniprot.org/annotation/VSP_061609|||http://purl.uniprot.org/annotation/VSP_061610
http://togogenome.org/gene/9606:SUMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61956                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes the formation of poly(SUMO) chains.|||Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform 2.|||N6-acetyllysine; alternate|||Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)|||Significantly impairs sumoylation of MTA1.|||Small ubiquitin-related modifier 2|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000035949|||http://purl.uniprot.org/annotation/PRO_0000035950|||http://purl.uniprot.org/annotation/VAR_047508|||http://purl.uniprot.org/annotation/VSP_042351
http://togogenome.org/gene/9606:RAB3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20336                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||Loss of phosphorylation.|||Phosphomimetic mutant. Loss of GDI1, GDI2, CHM and CHML binding.|||Phosphoserine|||Phosphothreonine; by LRRK2|||Ras-related protein Rab-3A|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121076
http://togogenome.org/gene/9606:BMP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K571|||http://purl.uniprot.org/uniprot/P18075                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Bone morphogenetic protein 7|||Disordered|||Found in a patient with unilateral microphthalmia, optic disk and chorioretinal coloboma, mild learning difficulties.|||Interchain|||N-linked (GlcNAc...) asparagine|||TGF-beta family profile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033876|||http://purl.uniprot.org/annotation/PRO_0000033877|||http://purl.uniprot.org/annotation/PRO_5014297538|||http://purl.uniprot.org/annotation/VAR_064058|||http://purl.uniprot.org/annotation/VAR_064059
http://togogenome.org/gene/9606:LINGO1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FE5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like C2-type|||In MRT64.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328642|||http://purl.uniprot.org/annotation/VAR_042436|||http://purl.uniprot.org/annotation/VAR_081164|||http://purl.uniprot.org/annotation/VAR_081165|||http://purl.uniprot.org/annotation/VSP_032749
http://togogenome.org/gene/9606:FRG2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues|||Protein FRG2-like-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300691
http://togogenome.org/gene/9606:BTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78543                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with CNOT7 and CNOT8.|||Abolishes interaction with CNOT7 and CNOT8; impairs anti-proliferative activity.|||Impairs PIN1-binding.|||Impairs interaction with CNOT7 and CNOT8.|||Impairs interaction with CNOT7. Inhibits CNOT7 mRNA deadenylase activity.|||Impairs phosphorylation by MAPK1 and MAPK3, and decreases PIN1-binding.|||Impairs phosphorylation by MAPK14, and decreases PIN1-binding.|||Phosphoserine; by MAPK1 and MAPK3|||Phosphoserine; by MAPK14|||Protein BTG2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143804|||http://purl.uniprot.org/annotation/VAR_048437
http://togogenome.org/gene/9606:OGT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15294                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211.|||Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208.|||Found in a renal cell carcinoma sample; somatic mutation.|||In XLID106; decreased protein abundance; decreased enzyme activity; reduced protein stability.|||In XLID106; decreased protein abundance; reduced protein stability.|||In XLID106; unknown pathological significance.|||In isoform 1.|||In isoform 2.|||In isoform 4.|||Loss of enzyme activity. Moderate increase in KMT2E ubiquitination. Moderate increase in KMT2E ubiquitination; when associated with A-508.|||N-acetylalanine|||Nuclear localization signal|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; by GSK3-beta; alternate|||Phosphotyrosine|||Proton acceptor|||Reduces enzyme activity by about 95%. Moderate increase in KMT2E ubiquitination; when associated with A-508.|||Reduces enzyme activity by over 90%.|||Removed|||Required for phosphatidylinositol 3,4,5-triphosphate binding|||TPR 1|||TPR 10|||TPR 11|||TPR 12|||TPR 13; truncated|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8|||TPR 9|||UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191772|||http://purl.uniprot.org/annotation/VAR_064736|||http://purl.uniprot.org/annotation/VAR_074019|||http://purl.uniprot.org/annotation/VAR_079183|||http://purl.uniprot.org/annotation/VAR_079254|||http://purl.uniprot.org/annotation/VSP_006553|||http://purl.uniprot.org/annotation/VSP_014164|||http://purl.uniprot.org/annotation/VSP_040764
http://togogenome.org/gene/9606:PPP1R14D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PAT1|||http://purl.uniprot.org/uniprot/Q9NXH3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Interaction with protein phosphatase 1|||Phosphothreonine|||Polar residues|||Protein phosphatase 1 regulatory subunit 14D|||Reduces inhibitory activity by 13%.|||Reduces inhibitory activity by 16%. Reduces phosphorylation.|||Reduces inhibitory activity by 57%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071497
http://togogenome.org/gene/9606:HOXB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14653                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Antp-type hexapeptide|||Disordered|||Homeobox|||Homeobox protein Hox-B1|||In HCFP3; decreased transactivation activity at low DNA concentrations; increased transactivation activity at high DNA concentrations compared to wild-type.|||In allele HOXB1*B.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000200107|||http://purl.uniprot.org/annotation/VAR_003817|||http://purl.uniprot.org/annotation/VAR_055959|||http://purl.uniprot.org/annotation/VAR_055960|||http://purl.uniprot.org/annotation/VAR_058129|||http://purl.uniprot.org/annotation/VAR_068723|||http://purl.uniprot.org/annotation/VSP_056813|||http://purl.uniprot.org/annotation/VSP_056814
http://togogenome.org/gene/9606:ZNF605                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T29                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 605                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234594|||http://purl.uniprot.org/annotation/VSP_043213
http://togogenome.org/gene/9606:RBM23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5D9|||http://purl.uniprot.org/uniprot/A0A0S2Z5I1|||http://purl.uniprot.org/uniprot/A0A0S2Z5J3|||http://purl.uniprot.org/uniprot/B7Z8M4|||http://purl.uniprot.org/uniprot/G3XAP0|||http://purl.uniprot.org/uniprot/Q86U06                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||In M1; abolished ability to regulate steroid hormone receptor-mediated transcription, without affecting the pre-mRNA splicing factor activity.|||In M2; reduced pre-mRNA splicing factor activity without affecting steroid hormone receptor-mediated transcription.|||In M3; reduced pre-mRNA splicing factor activity without affecting steroid hormone receptor-mediated transcription.|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Phosphoserine|||Polar residues|||Probable RNA-binding protein 23|||RRM|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081783|||http://purl.uniprot.org/annotation/VAR_016841|||http://purl.uniprot.org/annotation/VAR_052221|||http://purl.uniprot.org/annotation/VAR_052222|||http://purl.uniprot.org/annotation/VSP_008311|||http://purl.uniprot.org/annotation/VSP_008312|||http://purl.uniprot.org/annotation/VSP_008313|||http://purl.uniprot.org/annotation/VSP_008314|||http://purl.uniprot.org/annotation/VSP_008315
http://togogenome.org/gene/9606:DBF4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXK0|||http://purl.uniprot.org/uniprot/B7Z8C6|||http://purl.uniprot.org/uniprot/Q9UBU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BRCT|||BRCT 1|||BRCT 2|||Basic and acidic residues|||DBF4-type|||Disordered|||In isoform 2.|||Integrase domain-binding motif 1 (IBM1)|||Integrase domain-binding motif 2 (IBM2)|||Loss of interaction with PSIP1; when associated with A-631.|||Loss of interaction with PSIP1; when associated with A-634.|||Phosphomimetic mutant. Increased interaction with PSIP1.|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-667.|||Phosphomimetic mutant. Increased interaction with PSIP1; when associated with D-669.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein DBF4 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234061|||http://purl.uniprot.org/annotation/VAR_052970|||http://purl.uniprot.org/annotation/VAR_052971|||http://purl.uniprot.org/annotation/VSP_018203|||http://purl.uniprot.org/annotation/VSP_018204
http://togogenome.org/gene/9606:VAV2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52735                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Calponin-homology (CH)|||DH|||Guanine nucleotide exchange factor VAV2|||In isoform 2 and isoform 3.|||In isoform 3.|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphotyrosine; by EGFR|||SH2|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080984|||http://purl.uniprot.org/annotation/VAR_045690|||http://purl.uniprot.org/annotation/VSP_034900|||http://purl.uniprot.org/annotation/VSP_034901|||http://purl.uniprot.org/annotation/VSP_034902
http://togogenome.org/gene/9606:NT5C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MED8|||http://purl.uniprot.org/uniprot/A8K6K2|||http://purl.uniprot.org/uniprot/P49902                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytosolic purine 5'-nucleotidase|||Disordered|||In SPG45; unknown pathological significance.|||In isoform 2.|||Loss of 5' nucleotidase activity.|||Nucleophile|||Phosphoserine|||Proton donor|||Required for tetramer assembly                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064389|||http://purl.uniprot.org/annotation/VAR_024244|||http://purl.uniprot.org/annotation/VAR_030242|||http://purl.uniprot.org/annotation/VAR_079707|||http://purl.uniprot.org/annotation/VSP_054235
http://togogenome.org/gene/9606:KCNJ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K432|||http://purl.uniprot.org/uniprot/P48048                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Motif|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ATP-sensitive inward rectifier potassium channel 1|||Cytoplasmic|||Extracellular|||Helical|||Helical; Name=M1|||Helical; Name=M2|||Helical; Pore-forming; Name=H5|||In BARTS2.|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Inward rectifier potassium channel C-terminal|||N-linked (GlcNAc...) asparagine|||Phosphoserine; by SGK1|||Pore-forming|||Potassium channel inwardly rectifying transmembrane|||Role in the control of polyamine-mediated channel gating and in the blocking by intracellular magnesium|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000154917|||http://purl.uniprot.org/annotation/VAR_001548|||http://purl.uniprot.org/annotation/VAR_001549|||http://purl.uniprot.org/annotation/VAR_001550|||http://purl.uniprot.org/annotation/VAR_001551|||http://purl.uniprot.org/annotation/VAR_001552|||http://purl.uniprot.org/annotation/VAR_001553|||http://purl.uniprot.org/annotation/VAR_001554|||http://purl.uniprot.org/annotation/VAR_001555|||http://purl.uniprot.org/annotation/VAR_001556|||http://purl.uniprot.org/annotation/VAR_019724|||http://purl.uniprot.org/annotation/VAR_019725|||http://purl.uniprot.org/annotation/VAR_019726|||http://purl.uniprot.org/annotation/VAR_019727|||http://purl.uniprot.org/annotation/VAR_036426|||http://purl.uniprot.org/annotation/VAR_049668|||http://purl.uniprot.org/annotation/VSP_002797|||http://purl.uniprot.org/annotation/VSP_002798
http://togogenome.org/gene/9606:SLC26A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WA9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||STAS|||Sodium-independent sulfate anion transporter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320686|||http://purl.uniprot.org/annotation/VAR_068239
http://togogenome.org/gene/9606:ELF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32519|||http://purl.uniprot.org/uniprot/Q6MZZ4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||ETS|||ETS-related transcription factor Elf-1|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204085|||http://purl.uniprot.org/annotation/VAR_048942|||http://purl.uniprot.org/annotation/VAR_048943|||http://purl.uniprot.org/annotation/VAR_048944|||http://purl.uniprot.org/annotation/VSP_045682
http://togogenome.org/gene/9606:TMEM141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96I45                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||Transmembrane protein 141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279507
http://togogenome.org/gene/9606:SYNC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H7C4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1b|||Coil 2|||Disordered|||Head|||IF rod|||In isoform 2.|||Linker 1|||Linker 2|||Phosphoserine|||Polar residues|||Syncoilin|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306180|||http://purl.uniprot.org/annotation/VSP_039404
http://togogenome.org/gene/9606:DDX43                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NXZ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||KH|||Probable ATP-dependent RNA helicase DDX43|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054972|||http://purl.uniprot.org/annotation/VAR_057234|||http://purl.uniprot.org/annotation/VAR_057235|||http://purl.uniprot.org/annotation/VSP_056955|||http://purl.uniprot.org/annotation/VSP_056956
http://togogenome.org/gene/9606:PAWR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IZ0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  B30.2/SPRY domain-binding motif|||Basic and acidic residues|||Disordered|||Increased interaction with SPSB2. Only slightly increased interaction with SPSB4. Increased interaction with SPSB1, SPSB2 and SPSB4; when associated with A-69.|||Leucine-zipper|||Loss of interaction with SPSB1, SPSB2 and SPSB4.|||Loss of interaction with SPSB1-Elongin BC complex and SPSB2 and SPSB4.|||No loss of interaction with SPSB1, SPSB2 and SPSB4.|||Nuclear localization signal|||Only slighlty increased interaction with SPSB2. Only slightly increased interaction with SPSB4. Increased interaction with SPSB1, SPSB2 and SPSB4; when associated with A-68.|||PRKC apoptosis WT1 regulator protein|||Phosphoserine|||Phosphothreonine; by PKA|||Polar residues|||Selective for apoptosis induction in cancer cells (SAC)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058236|||http://purl.uniprot.org/annotation/VAR_022465|||http://purl.uniprot.org/annotation/VAR_022466|||http://purl.uniprot.org/annotation/VAR_022467|||http://purl.uniprot.org/annotation/VAR_022468
http://togogenome.org/gene/9606:ZNF205                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95201                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Pro residues|||Transcriptional repressor RHIT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047451|||http://purl.uniprot.org/annotation/VAR_028798|||http://purl.uniprot.org/annotation/VAR_028799
http://togogenome.org/gene/9606:STAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZT2|||http://purl.uniprot.org/uniprot/Q92783                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||ITAM|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Removed|||SH3|||Signal transducing adapter molecule 1|||UIM|||VHS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190145|||http://purl.uniprot.org/annotation/VAR_036348|||http://purl.uniprot.org/annotation/VSP_014846|||http://purl.uniprot.org/annotation/VSP_014847
http://togogenome.org/gene/9606:CETN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41208                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Centrin-2|||Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Required for self-assembly                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073561
http://togogenome.org/gene/9606:ACAD10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6JQN1                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acyl-CoA dehydrogenase family member 10|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N6-acetyllysine; alternate|||N6-succinyllysine|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284770|||http://purl.uniprot.org/annotation/VAR_031811|||http://purl.uniprot.org/annotation/VAR_031812|||http://purl.uniprot.org/annotation/VAR_031813|||http://purl.uniprot.org/annotation/VAR_031814|||http://purl.uniprot.org/annotation/VSP_024630|||http://purl.uniprot.org/annotation/VSP_024631|||http://purl.uniprot.org/annotation/VSP_024632|||http://purl.uniprot.org/annotation/VSP_024633|||http://purl.uniprot.org/annotation/VSP_024634|||http://purl.uniprot.org/annotation/VSP_024635|||http://purl.uniprot.org/annotation/VSP_044980
http://togogenome.org/gene/9606:HMBS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8I5KXV4|||http://purl.uniprot.org/uniprot/P08397                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Decreased hydroxymethylbilane synthase activity.|||Found in a patient with unclear porphyria-related biochemical findings and abdominal pain; unknown pathological significance; does not affect hydroxymethylbilane synthase activity; does not affect Vmax; does not affect KM; does not affect thermal stability.|||In AIP.|||In AIP; 19% of wild-type deaminase activity.|||In AIP; 46% wild-type deaminase activity; decreased enzyme stability.|||In AIP; <2% residual activity.|||In AIP; complete loss of hydroxymethylbilane synthase activity.|||In AIP; decreased hydroxymethylbilane synthase activity due to defective enzyme-intermediate complexes turnover and regeneration of free enzyme molecules.|||In AIP; less than 1% of wild-type activity.|||In AIP; less than 1% of wild-type deaminase activity.|||In AIP; less than 3% of activity.|||In AIP; loss of activity.|||In AIP; loss of hydroxymethylbilane synthase activity; 1% of wild-type activity; lower thermal stability than wild-type enzyme.|||In AIP; residual activity.|||In AIP; severely decreased hydroxymethylbilane synthase activity corresponding to less than 1% of wild-type activity.|||In AIP; severely decreased hydroxymethylbilane synthase activity.|||In AIP; severely decreased hydroxymethylbilane synthase activity; results in less than 5% of wild-type activity; 2-fold decrease of Vmax; 33-fold increase of KM.|||In AIP; severely decreased in hydroxymethylbilane synthase activity.|||In AIP; severely decreased, if any, hydroxymethylbilane synthase activity.|||In AIP; severely decreased, if any, hydroxymethylbilane synthase activity; affects protein conformation; lower thermal stability than wild-type enzyme.|||In AIP; unknown pathological significance.|||In AIP; unknown pathological significance; decreased hydroxymethylbilane synthase activity; results in 30% of wild-type activity; 3-fold decrease of Vmax; normal KM; affects protein conformation.|||In AIP; unknown pathological significance; has 80% of wild-type activity.|||In AIP; unknown pathological significance; slightly decreased hydroxymethylbilane synthase activity corresponding to 80% of wild-type activity.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Loss of hydroxymethylbilane synthase activity.|||N-acetylserine|||N6-acetyllysine|||Phosphoserine|||Porphobilinogen deaminase|||Porphobilinogen deaminase C-terminal|||Porphobilinogen deaminase N-terminal|||Removed|||S-(dipyrrolylmethanemethyl)cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143034|||http://purl.uniprot.org/annotation/VAR_003638|||http://purl.uniprot.org/annotation/VAR_003639|||http://purl.uniprot.org/annotation/VAR_003640|||http://purl.uniprot.org/annotation/VAR_003641|||http://purl.uniprot.org/annotation/VAR_003642|||http://purl.uniprot.org/annotation/VAR_003643|||http://purl.uniprot.org/annotation/VAR_003644|||http://purl.uniprot.org/annotation/VAR_003645|||http://purl.uniprot.org/annotation/VAR_003646|||http://purl.uniprot.org/annotation/VAR_003647|||http://purl.uniprot.org/annotation/VAR_003648|||http://purl.uniprot.org/annotation/VAR_003649|||http://purl.uniprot.org/annotation/VAR_003650|||http://purl.uniprot.org/annotation/VAR_003651|||http://purl.uniprot.org/annotation/VAR_003652|||http://purl.uniprot.org/annotation/VAR_003653|||http://purl.uniprot.org/annotation/VAR_003654|||http://purl.uniprot.org/annotation/VAR_003655|||http://purl.uniprot.org/annotation/VAR_003656|||http://purl.uniprot.org/annotation/VAR_003657|||http://purl.uniprot.org/annotation/VAR_003658|||http://purl.uniprot.org/annotation/VAR_003659|||http://purl.uniprot.org/annotation/VAR_003660|||http://purl.uniprot.org/annotation/VAR_003661|||http://purl.uniprot.org/annotation/VAR_003662|||http://purl.uniprot.org/annotation/VAR_003663|||http://purl.uniprot.org/annotation/VAR_003664|||http://purl.uniprot.org/annotation/VAR_003665|||http://purl.uniprot.org/annotation/VAR_003666|||http://purl.uniprot.org/annotation/VAR_003667|||http://purl.uniprot.org/annotation/VAR_003668|||http://purl.uniprot.org/annotation/VAR_003669|||http://purl.uniprot.org/annotation/VAR_003670|||http://purl.uniprot.org/annotation/VAR_003671|||http://purl.uniprot.org/annotation/VAR_003672|||http://purl.uniprot.org/annotation/VAR_003673|||http://purl.uniprot.org/annotation/VAR_009223|||http://purl.uniprot.org/annotation/VAR_011001|||http://purl.uniprot.org/annotation/VAR_011002|||http://purl.uniprot.org/annotation/VAR_011003|||http://purl.uniprot.org/annotation/VAR_011004|||http://purl.uniprot.org/annotation/VAR_011005|||http://purl.uniprot.org/annotation/VAR_011006|||http://purl.uniprot.org/annotation/VAR_011007|||http://purl.uniprot.org/annotation/VAR_011008|||http://purl.uniprot.org/annotation/VAR_011009|||http://purl.uniprot.org/annotation/VAR_011010|||http://purl.uniprot.org/annotation/VAR_011011|||http://purl.uniprot.org/annotation/VAR_011012|||http://purl.uniprot.org/annotation/VAR_011013|||http://purl.uniprot.org/annotation/VAR_011014|||http://purl.uniprot.org/annotation/VAR_011015|||http://purl.uniprot.org/annotation/VAR_011016|||http://purl.uniprot.org/annotation/VAR_011017|||http://purl.uniprot.org/annotation/VAR_011018|||http://purl.uniprot.org/annotation/VAR_011019|||http://purl.uniprot.org/annotation/VAR_011020|||http://purl.uniprot.org/annotation/VAR_011021|||http://purl.uniprot.org/annotation/VAR_011022|||http://purl.uniprot.org/annotation/VAR_011023|||http://purl.uniprot.org/annotation/VAR_011024|||http://purl.uniprot.org/annotation/VAR_011025|||http://purl.uniprot.org/annotation/VAR_011026|||http://purl.uniprot.org/annotation/VAR_011027|||http://purl.uniprot.org/annotation/VAR_011028|||http://purl.uniprot.org/annotation/VAR_011029|||http://purl.uniprot.org/annotation/VAR_025558|||http://purl.uniprot.org/annotation/VAR_025559|||http://purl.uniprot.org/annotation/VAR_025560|||http://purl.uniprot.org/annotation/VAR_025561|||http://purl.uniprot.org/annotation/VAR_025562|||http://purl.uniprot.org/annotation/VAR_025563|||http://purl.uniprot.org/annotation/VAR_025564|||http://purl.uniprot.org/annotation/VAR_025565|||http://purl.uniprot.org/annotation/VAR_025566|||http://purl.uniprot.org/annotation/VAR_025567|||http://purl.uniprot.org/annotation/VAR_025568|||http://purl.uniprot.org/annotation/VAR_025569|||http://purl.uniprot.org/annotation/VAR_025570|||http://purl.uniprot.org/annotation/VAR_025571|||http://purl.uniprot.org/annotation/VAR_025572|||http://purl.uniprot.org/annotation/VAR_025573|||http://purl.uniprot.org/annotation/VAR_025574|||http://purl.uniprot.org/annotation/VAR_025575|||http://purl.uniprot.org/annotation/VAR_025576|||http://purl.uniprot.org/annotation/VAR_025577|||http://purl.uniprot.org/annotation/VAR_025578|||http://purl.uniprot.org/annotation/VAR_025579|||http://purl.uniprot.org/annotation/VAR_025580|||http://purl.uniprot.org/annotation/VAR_073714|||http://purl.uniprot.org/annotation/VAR_073715|||http://purl.uniprot.org/annotation/VAR_073716|||http://purl.uniprot.org/annotation/VAR_074151|||http://purl.uniprot.org/annotation/VAR_074152|||http://purl.uniprot.org/annotation/VAR_074153|||http://purl.uniprot.org/annotation/VAR_074154|||http://purl.uniprot.org/annotation/VAR_074155|||http://purl.uniprot.org/annotation/VAR_074156|||http://purl.uniprot.org/annotation/VAR_074157|||http://purl.uniprot.org/annotation/VAR_087876|||http://purl.uniprot.org/annotation/VAR_087877|||http://purl.uniprot.org/annotation/VSP_002067|||http://purl.uniprot.org/annotation/VSP_047294
http://togogenome.org/gene/9606:LRWD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD0|||http://purl.uniprot.org/uniprot/Q9UFC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||Leucine-rich repeat and WD repeat-containing protein 1|||Phosphoserine|||Polar residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310994
http://togogenome.org/gene/9606:GDPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9F7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||GP-PDE|||Helical|||In isoform 2.|||In isoform 3.|||Lysophospholipase D GDPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251931|||http://purl.uniprot.org/annotation/VSP_020806|||http://purl.uniprot.org/annotation/VSP_020807|||http://purl.uniprot.org/annotation/VSP_020808
http://togogenome.org/gene/9606:PURA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00577                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In NEDRIHF.|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Transcriptional activator protein Pur-alpha                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097107|||http://purl.uniprot.org/annotation/VAR_072698|||http://purl.uniprot.org/annotation/VAR_072699|||http://purl.uniprot.org/annotation/VAR_072700|||http://purl.uniprot.org/annotation/VAR_072701|||http://purl.uniprot.org/annotation/VAR_072702|||http://purl.uniprot.org/annotation/VAR_072703|||http://purl.uniprot.org/annotation/VAR_072704|||http://purl.uniprot.org/annotation/VAR_073993|||http://purl.uniprot.org/annotation/VAR_073994
http://togogenome.org/gene/9606:PUS10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MIT2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished tRNA pseudouridine synthase without affecting ability to promote miRNA processing.|||In a colorectal cancer sample; somatic mutation.|||Nucleophile|||Phosphoserine|||RNA binding forefinger loop|||RNA binding thumb loop|||tRNA pseudouridine synthase Pus10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299022|||http://purl.uniprot.org/annotation/VAR_035617
http://togogenome.org/gene/9606:ADGRV1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXG9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADGRV1 subunit alpha|||ADGRV1 subunit beta|||Adhesion G-protein coupled receptor V1|||Calx-beta 1|||Calx-beta 10|||Calx-beta 11|||Calx-beta 12|||Calx-beta 13|||Calx-beta 14|||Calx-beta 15|||Calx-beta 16|||Calx-beta 17|||Calx-beta 18|||Calx-beta 19|||Calx-beta 2|||Calx-beta 20|||Calx-beta 21|||Calx-beta 22|||Calx-beta 23|||Calx-beta 24|||Calx-beta 25|||Calx-beta 26|||Calx-beta 27|||Calx-beta 28|||Calx-beta 29|||Calx-beta 3|||Calx-beta 30|||Calx-beta 31|||Calx-beta 32|||Calx-beta 33|||Calx-beta 34|||Calx-beta 35|||Calx-beta 4|||Calx-beta 5|||Calx-beta 6|||Calx-beta 7|||Calx-beta 8|||Calx-beta 9|||Cleavage|||Cytoplasmic|||Disordered|||EAR 1|||EAR 2|||EAR 3|||EAR 4|||EAR 5|||EAR 6|||Extracellular|||GPS|||Helical|||In USH2C.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000232735|||http://purl.uniprot.org/annotation/PRO_0000445731|||http://purl.uniprot.org/annotation/PRO_0000445732|||http://purl.uniprot.org/annotation/VAR_025995|||http://purl.uniprot.org/annotation/VAR_025996|||http://purl.uniprot.org/annotation/VAR_025997|||http://purl.uniprot.org/annotation/VAR_025998|||http://purl.uniprot.org/annotation/VAR_025999|||http://purl.uniprot.org/annotation/VAR_026000|||http://purl.uniprot.org/annotation/VAR_026001|||http://purl.uniprot.org/annotation/VAR_026002|||http://purl.uniprot.org/annotation/VAR_026003|||http://purl.uniprot.org/annotation/VAR_026004|||http://purl.uniprot.org/annotation/VAR_026005|||http://purl.uniprot.org/annotation/VAR_026006|||http://purl.uniprot.org/annotation/VAR_026007|||http://purl.uniprot.org/annotation/VAR_026008|||http://purl.uniprot.org/annotation/VAR_026009|||http://purl.uniprot.org/annotation/VAR_026010|||http://purl.uniprot.org/annotation/VAR_026011|||http://purl.uniprot.org/annotation/VAR_026012|||http://purl.uniprot.org/annotation/VAR_026013|||http://purl.uniprot.org/annotation/VAR_046346|||http://purl.uniprot.org/annotation/VAR_046347|||http://purl.uniprot.org/annotation/VAR_046348|||http://purl.uniprot.org/annotation/VAR_046349|||http://purl.uniprot.org/annotation/VAR_046350|||http://purl.uniprot.org/annotation/VAR_046351|||http://purl.uniprot.org/annotation/VAR_046352|||http://purl.uniprot.org/annotation/VAR_055933|||http://purl.uniprot.org/annotation/VAR_068032|||http://purl.uniprot.org/annotation/VAR_068033|||http://purl.uniprot.org/annotation/VSP_017947|||http://purl.uniprot.org/annotation/VSP_017948|||http://purl.uniprot.org/annotation/VSP_017949|||http://purl.uniprot.org/annotation/VSP_017950|||http://purl.uniprot.org/annotation/VSP_035313|||http://purl.uniprot.org/annotation/VSP_035314
http://togogenome.org/gene/9606:RNF213                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTR7|||http://purl.uniprot.org/uniprot/Q63HN8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolished E3 ubiquitin-protein ligase activity; does not affect ubiquitination of lipopolysaccharide.|||Abolished ability to ubiquitinate lipopolysaccharide.|||Basic and acidic residues|||Decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant B1B2; abolished ATPase activity and localization to lipid droplets; when associated with A-2488.|||Decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant B1B2; abolished ATPase activity and localization to lipid droplets; when associated with A-2845.|||Disordered|||E3 ubiquitin-protein ligase RNF213|||Found in a heterozygous family with heterogeneous intracerebral vasculopathy.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Impaired ATP-binding leading to decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant A1A2; abolished ATP-binding and localization to lipid droplets; when associated with A-2426.|||Impaired ATP-binding leading to decreased ATPase activity; abolished ubiquitination of lipopolysaccharide. In mutant A1A2; abolished ATP-binding and localization to lipid droplets; when associated with A-2775.|||In MYMY2.|||In MYMY2; variant detected in cases of Moyamoya disease in Caucasian and Asian populations; inhibitory effect on angiogenic activity of vascular endothelial cells; does not affect E3 ubiquitin-protein ligase activity.|||In MYMY2; very frequent in individuals affected by Moyamoya disease; strongly increases the risk of Moyamoya disease; induces genomic instability; shows decreased ATPase activity; does not affect ubiquitination of lipopolysaccharide.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of ATPase hydrolysis.|||Nucleophile; for E3 ubiquitin-lipopolysaccharide ligase activity|||Phosphoserine|||Polar residues|||RING-type|||RZ-type|||Rare variant detected in a case of Moyamoya disease; does not affect ubiquitination of lipopolysaccharide.|||Rare variant detected in a patient with Moyamoya disease in Caucasian population.|||Rare variant detected in a patient with Moyamoya disease in Caucasian population; abolished E3 ubiquitin-protein ligase activity.|||Rare variant detected in a sporadic case of Moyamoya disease in Asian population.|||Rare variant detected in a sporadic case of Moyamoya disease in Caucasian population.|||Rare variant detected in a sporadic case of Moyamoya disease in Caucasian population; abolished E3 ubiquitin-protein ligase activity.|||Rare variant detected in a sporadic case of Moyamoya disease in East Asian population.|||Rare variant detected in a sporadic case of Moyamoya disease in East Asian population; abolished E3 ubiquitin-protein ligase activity.|||Rare variant detected in a sporadic case of Moyamoya disease.|||Rare variant detected in cases of Moyamoya disease in East Asian populations.|||Rare variant detected in cases of Moyamoya disease in Slovakian and Czech populations; inhibitory effect on angiogenic activity of vascular endothelial cells.|||Rare variant detected in cases of Moyamoya disease.|||Rare variant detected in patients with Moyamoya disease in Caucasian population.|||Rare variant detected in patients with Moyamoya disease in Caucasian population; strongly decreased E3 ubiquitin-protein ligase activity.|||Rare variant detected in patients with Moyamoya disease in East Asian and Caucasian populations.|||Rare variant detected in patients with Moyamoya disease.|||Rare variant detected in patients with Moyamoya disease; abolished E3 ubiquitin-protein ligase activity.|||Variant detected in cases of Moyamoya disease in Caucasian and East Asian populations.|||Variant detected in cases of Moyamoya disease in Caucasian populations.|||Variant detected in cases of Moyamoya disease in East Asian populations and rare variant detected in a sporadic case of Moyamoya disease; does not affect ubiquitination of lipopolysaccharide.|||Variant detected in cases of Moyamoya disease in East Asian populations.|||Variant detected in cases of Moyamoya disease in a Caucasian family.|||Variant detected in patients with Moyamoya disease; strongly decreased E3 ubiquitin-protein ligase activity. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000415917|||http://purl.uniprot.org/annotation/VAR_067020|||http://purl.uniprot.org/annotation/VAR_067021|||http://purl.uniprot.org/annotation/VAR_067022|||http://purl.uniprot.org/annotation/VAR_067023|||http://purl.uniprot.org/annotation/VAR_067024|||http://purl.uniprot.org/annotation/VAR_067025|||http://purl.uniprot.org/annotation/VAR_067026|||http://purl.uniprot.org/annotation/VAR_067027|||http://purl.uniprot.org/annotation/VAR_067028|||http://purl.uniprot.org/annotation/VAR_067029|||http://purl.uniprot.org/annotation/VAR_067030|||http://purl.uniprot.org/annotation/VAR_067031|||http://purl.uniprot.org/annotation/VAR_067032|||http://purl.uniprot.org/annotation/VAR_067033|||http://purl.uniprot.org/annotation/VAR_067034|||http://purl.uniprot.org/annotation/VAR_067035|||http://purl.uniprot.org/annotation/VAR_075635|||http://purl.uniprot.org/annotation/VAR_075636|||http://purl.uniprot.org/annotation/VAR_075637|||http://purl.uniprot.org/annotation/VAR_075638|||http://purl.uniprot.org/annotation/VAR_075639|||http://purl.uniprot.org/annotation/VAR_075640|||http://purl.uniprot.org/annotation/VAR_075641|||http://purl.uniprot.org/annotation/VAR_075642|||http://purl.uniprot.org/annotation/VAR_075643|||http://purl.uniprot.org/annotation/VAR_075644|||http://purl.uniprot.org/annotation/VAR_075645|||http://purl.uniprot.org/annotation/VAR_075646|||http://purl.uniprot.org/annotation/VAR_075647|||http://purl.uniprot.org/annotation/VAR_075648|||http://purl.uniprot.org/annotation/VAR_075649|||http://purl.uniprot.org/annotation/VAR_075650|||http://purl.uniprot.org/annotation/VAR_075651|||http://purl.uniprot.org/annotation/VAR_075652|||http://purl.uniprot.org/annotation/VAR_075653|||http://purl.uniprot.org/annotation/VAR_079573|||http://purl.uniprot.org/annotation/VAR_079574|||http://purl.uniprot.org/annotation/VAR_079575|||http://purl.uniprot.org/annotation/VAR_085287|||http://purl.uniprot.org/annotation/VAR_085288|||http://purl.uniprot.org/annotation/VAR_085289|||http://purl.uniprot.org/annotation/VAR_085290|||http://purl.uniprot.org/annotation/VAR_085291|||http://purl.uniprot.org/annotation/VAR_085292|||http://purl.uniprot.org/annotation/VAR_085293|||http://purl.uniprot.org/annotation/VAR_085294|||http://purl.uniprot.org/annotation/VAR_085295|||http://purl.uniprot.org/annotation/VAR_085296|||http://purl.uniprot.org/annotation/VAR_085297|||http://purl.uniprot.org/annotation/VAR_085298|||http://purl.uniprot.org/annotation/VAR_085299|||http://purl.uniprot.org/annotation/VAR_085300|||http://purl.uniprot.org/annotation/VAR_085301|||http://purl.uniprot.org/annotation/VAR_085302|||http://purl.uniprot.org/annotation/VAR_085303|||http://purl.uniprot.org/annotation/VAR_085304|||http://purl.uniprot.org/annotation/VAR_085305|||http://purl.uniprot.org/annotation/VAR_085306|||http://purl.uniprot.org/annotation/VAR_085307|||http://purl.uniprot.org/annotation/VAR_085308|||http://purl.uniprot.org/annotation/VAR_085309|||http://purl.uniprot.org/annotation/VAR_085310|||http://purl.uniprot.org/annotation/VAR_085311|||http://purl.uniprot.org/annotation/VAR_085312|||http://purl.uniprot.org/annotation/VSP_042416|||http://purl.uniprot.org/annotation/VSP_042417|||http://purl.uniprot.org/annotation/VSP_042418|||http://purl.uniprot.org/annotation/VSP_042419|||http://purl.uniprot.org/annotation/VSP_042420
http://togogenome.org/gene/9606:MSL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCI7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic residues|||Disordered|||E3 ubiquitin-protein ligase MSL2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Great reduction in H2B ubiquitination. No effect on MSL1-binding.|||In isoform 2.|||Phosphoserine|||RING-type|||Sufficient for interaction with MSL1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299536|||http://purl.uniprot.org/annotation/VSP_046200
http://togogenome.org/gene/9606:TMEM132B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14DG7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Transmembrane protein 132B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284620|||http://purl.uniprot.org/annotation/VAR_031786|||http://purl.uniprot.org/annotation/VSP_024576|||http://purl.uniprot.org/annotation/VSP_024577|||http://purl.uniprot.org/annotation/VSP_024578
http://togogenome.org/gene/9606:RPS29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62273                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In DBA13; results in reduced protein expression; results in pre-rRNA processing defect.|||In isoform 2.|||N6-acetyllysine|||Omega-N-methylarginine|||Phosphoserine|||Removed|||Small ribosomal subunit protein uS14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131019|||http://purl.uniprot.org/annotation/VAR_071328|||http://purl.uniprot.org/annotation/VAR_071329|||http://purl.uniprot.org/annotation/VSP_042844
http://togogenome.org/gene/9606:FAHD2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96GK7                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Fumarylacetoacetate hydrolase domain-containing protein 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289795|||http://purl.uniprot.org/annotation/VAR_049015
http://togogenome.org/gene/9606:F8A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23610                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  40-kDa huntingtin-associated protein|||Disordered|||N-acetylalanine|||Nuclear localization signal|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087159
http://togogenome.org/gene/9606:ZNRF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y8|||http://purl.uniprot.org/uniprot/Q8NHG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Zinc Finger                                                                                  ^@                                                                                  Complete loss of binding to ATP1A1.|||Counteracts the N-myristoyl-mediated targeting of ZNRF2 to membranes.|||Disordered|||E3 ubiquitin-protein ligase ZNRF2|||N-myristoyl glycine|||Partial decrease of YWHAE binding upon IGF1 stimulation.|||Partial decrease of YWHAE binding upon IGF1 stimulation. More distinct membranal localization.|||Phosphoserine|||Phosphoserine; by MTOR|||Polar residues|||RING-type|||RING-type; atypical|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000277803
http://togogenome.org/gene/9606:H1-0                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07305                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  ADP-ribosylserine|||Basic and acidic residues|||Basic residues|||Citrulline|||Deamidated asparagine; partial|||Disordered|||H15|||Histone H1.0|||Histone H1.0, N-terminally processed|||In RNA edited version.|||In isoform 2.|||N-acetylmethionine|||N-acetylthreonine; partial; in Histone H1.0, N-terminally processed|||Removed; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195904|||http://purl.uniprot.org/annotation/PRO_0000423207|||http://purl.uniprot.org/annotation/VAR_054789|||http://purl.uniprot.org/annotation/VSP_042163
http://togogenome.org/gene/9606:DIAPH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DPV3|||http://purl.uniprot.org/uniprot/Q9NSV4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DAD|||Disordered|||FH1|||FH2|||GBD/FH3|||In isoform 1 and isoform 2.|||In isoform 2.|||In isoform 4, isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||In isoform 7 and isoform 1.|||Nuclear export signal|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Pro residues|||Protein diaphanous homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194897|||http://purl.uniprot.org/annotation/VAR_049097|||http://purl.uniprot.org/annotation/VAR_049098|||http://purl.uniprot.org/annotation/VAR_049099|||http://purl.uniprot.org/annotation/VSP_001574|||http://purl.uniprot.org/annotation/VSP_001575|||http://purl.uniprot.org/annotation/VSP_015958|||http://purl.uniprot.org/annotation/VSP_027774|||http://purl.uniprot.org/annotation/VSP_027775|||http://purl.uniprot.org/annotation/VSP_027776|||http://purl.uniprot.org/annotation/VSP_027777|||http://purl.uniprot.org/annotation/VSP_027778
http://togogenome.org/gene/9606:OR5H15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDH6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5H15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310413|||http://purl.uniprot.org/annotation/VAR_037027|||http://purl.uniprot.org/annotation/VAR_037028|||http://purl.uniprot.org/annotation/VAR_037029
http://togogenome.org/gene/9606:CRYBG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1P7|||http://purl.uniprot.org/uniprot/Q9NWG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 10|||Beta/gamma crystallin 'Greek key' 11|||Beta/gamma crystallin 'Greek key' 12|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Beta/gamma crystallin 'Greek key' 5|||Beta/gamma crystallin 'Greek key' 6|||Beta/gamma crystallin 'Greek key' 7|||Beta/gamma crystallin 'Greek key' 8|||Beta/gamma crystallin 'Greek key' 9|||Beta/gamma crystallin domain-containing protein 2|||Disordered|||Polar residues|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285105|||http://purl.uniprot.org/annotation/VAR_048835
http://togogenome.org/gene/9606:PCDHB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5F3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cadherin 1|||Cadherin 2|||Cadherin 3|||Cadherin 4|||Cadherin 5|||Cadherin 6|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||Protocadherin beta-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000003914|||http://purl.uniprot.org/annotation/VAR_048541|||http://purl.uniprot.org/annotation/VAR_048542|||http://purl.uniprot.org/annotation/VAR_048543|||http://purl.uniprot.org/annotation/VAR_048544|||http://purl.uniprot.org/annotation/VAR_048545|||http://purl.uniprot.org/annotation/VAR_048546|||http://purl.uniprot.org/annotation/VAR_048547
http://togogenome.org/gene/9606:PHPT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NRX4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  14 kDa phosphohistidine phosphatase|||Decreased affinity for substrate and reduced catalytic activity.|||Decreased affinity for substrate and slightly reduced catalytic activity.|||Decreased affinity for substrate and strongly reduced catalytic activity.|||In isoform 2.|||Loss of activity.|||N-acetylalanine|||Proton acceptor|||Removed|||Slightly decreased affinity for substrate, but no effect on catalytic activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206152|||http://purl.uniprot.org/annotation/VSP_041159
http://togogenome.org/gene/9606:CXCL17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6UXB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Mutagenesis Site|||Region|||Signal Peptide|||Site                                                                                  ^@                                                                                  4-Cys CXCL17|||Basic residues|||C-X-C motif chemokine 17|||Cleavage|||Disordered|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-103 and S-110.|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-77 and S-103.|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-77 and S-110.|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-77; S-103 and S-110.|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-75; S-77; S-103 and S-110.|||Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-52; S-75; S-77; S-103 and S-110.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311097|||http://purl.uniprot.org/annotation/PRO_0000438487
http://togogenome.org/gene/9606:MBD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95983                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Augments DNA binding activity, irrespective of DNA methylation.|||Confers weak binding to methylated CpG (in vitro). Confers strong binding to methylated CpG (in vitro); when associated with K-30.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||MBD|||Methyl-CpG-binding domain protein 3|||No effect. Confers strong binding to methylated CpG (in vitro); when associated with Y-34.|||Phosphoserine|||Required for interaction with MBD2|||Required for interaction with MBD3L2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096262|||http://purl.uniprot.org/annotation/VSP_011081
http://togogenome.org/gene/9606:GET1-SH3BGR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A3B3ITX9                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Region|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Helical                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:SEMA4F                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYZ7|||http://purl.uniprot.org/uniprot/O95754                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like C2-type|||In isoform Short.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||PSI|||Phosphoserine|||Sema|||Semaphorin-4F                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032330|||http://purl.uniprot.org/annotation/PRO_5001832090|||http://purl.uniprot.org/annotation/VSP_006043
http://togogenome.org/gene/9606:VLDLR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0T897|||http://purl.uniprot.org/uniprot/A0A7P0T9P7|||http://purl.uniprot.org/uniprot/P98155|||http://purl.uniprot.org/uniprot/Q5VVF5                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Clustered O-linked oligosaccharides|||Cytoplasmic|||EGF-like|||EGF-like 1|||EGF-like 2; calcium-binding|||EGF-like 3|||Endocytosis signal|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Helical|||In isoform Short.|||Insensitive to MYLIP-triggered degradation. Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-828.|||Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-839.|||Insensitive to MYLIP-triggered degradation; when associated with R-828 and R-839.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class B|||LDL-receptor class B 1|||LDL-receptor class B 2|||LDL-receptor class B 3|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||N-linked (GlcNAc...) asparagine|||Very low-density lipoprotein receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017343|||http://purl.uniprot.org/annotation/PRO_5014310172|||http://purl.uniprot.org/annotation/PRO_5030783030|||http://purl.uniprot.org/annotation/PRO_5031152599|||http://purl.uniprot.org/annotation/VAR_011865|||http://purl.uniprot.org/annotation/VAR_011866|||http://purl.uniprot.org/annotation/VAR_025063|||http://purl.uniprot.org/annotation/VAR_025064|||http://purl.uniprot.org/annotation/VAR_025065|||http://purl.uniprot.org/annotation/VAR_025066|||http://purl.uniprot.org/annotation/VAR_025067|||http://purl.uniprot.org/annotation/VSP_004304
http://togogenome.org/gene/9606:ATP5PD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJH2|||http://purl.uniprot.org/uniprot/O75947                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Splice Variant                                                                                  ^@                                                                                  ATP synthase subunit d, mitochondrial|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071673|||http://purl.uniprot.org/annotation/VSP_000436
http://togogenome.org/gene/9606:PLCB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7P0MRI8|||http://purl.uniprot.org/uniprot/Q15147                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4|||Acidic residues|||Basic and acidic residues|||C2|||Disordered|||In ARCND2.|||In isoform 1.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||PI-PLC X-box|||PI-PLC Y-box|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088495|||http://purl.uniprot.org/annotation/VAR_056694|||http://purl.uniprot.org/annotation/VAR_056695|||http://purl.uniprot.org/annotation/VAR_068559|||http://purl.uniprot.org/annotation/VAR_068560|||http://purl.uniprot.org/annotation/VAR_068561|||http://purl.uniprot.org/annotation/VAR_068562|||http://purl.uniprot.org/annotation/VAR_068563|||http://purl.uniprot.org/annotation/VSP_004721|||http://purl.uniprot.org/annotation/VSP_004722|||http://purl.uniprot.org/annotation/VSP_037818|||http://purl.uniprot.org/annotation/VSP_055182
http://togogenome.org/gene/9606:SUSD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJW3|||http://purl.uniprot.org/uniprot/Q9UGT4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  AMOP|||Alternate|||Cytoplasmic|||Extracellular|||Helical|||N-linked (GlcNAc...) asparagine|||SMB|||Sushi|||Sushi domain-containing protein 2|||VWFD                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249439|||http://purl.uniprot.org/annotation/PRO_5014247034|||http://purl.uniprot.org/annotation/VAR_027416|||http://purl.uniprot.org/annotation/VAR_027417|||http://purl.uniprot.org/annotation/VAR_027418
http://togogenome.org/gene/9606:PRSS8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16651                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Signal Peptide|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Signal Peptide|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Activation peptide|||Charge relay system|||Helical|||In isoform 2.|||Interchain (between light and heavy chains)|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Prostasin|||Prostasin heavy chain|||Prostasin light chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028027|||http://purl.uniprot.org/annotation/PRO_0000028028|||http://purl.uniprot.org/annotation/PRO_0000028029|||http://purl.uniprot.org/annotation/PRO_0000028030|||http://purl.uniprot.org/annotation/PRO_0000240511|||http://purl.uniprot.org/annotation/VSP_056632
http://togogenome.org/gene/9606:NAP1L4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99733                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||N-acetylalanine|||N6-acetyllysine|||Nuclear localization signal|||Nucleosome assembly protein 1-like 4|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185658|||http://purl.uniprot.org/annotation/VSP_053910
http://togogenome.org/gene/9606:TOMM6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96B49                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Disordered|||Mitochondrial import receptor subunit TOM6 homolog|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302856
http://togogenome.org/gene/9606:EMG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92979                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In BWCNS; studies in fibroblasts show a dramatically reduced level of EMG1 protein in a BWCNS-affected patient compared to normal fibroblasts although patient fibroblasts do not have complete EMG1 deficiency; the mutation increases dimerization of EMG1 subunits suggesting that aggregation of EMG1 leads to reduced levels of the protein.|||Interaction with substrate rRNA|||N-acetylalanine|||Phosphoserine|||Removed|||Ribosomal RNA small subunit methyltransferase NEP1|||Stabilizes Arg-84                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158606|||http://purl.uniprot.org/annotation/VAR_050237|||http://purl.uniprot.org/annotation/VAR_062480
http://togogenome.org/gene/9606:ZNF585A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DFY4|||http://purl.uniprot.org/uniprot/Q6P3V2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7; degenerate|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 585A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047677|||http://purl.uniprot.org/annotation/VSP_016017|||http://purl.uniprot.org/annotation/VSP_016018
http://togogenome.org/gene/9606:CARD14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BXL6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  CARD|||Caspase recruitment domain-containing protein 14|||Guanylate kinase-like|||In PRP.|||In PSORS2 and PRP; may result in altered splicing of exon 3; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity.|||In PSORS2; increases NF-kappaB transcription factor activity.|||In PSORS2; increases NF-kappaB transcription factor activity; enhances CBCL10-MALT1-CARD14 complex formation; enhances MALT1 protease activity.|||In PSORS2; increases NF-kappaB transcription factor activity; enhances MALT1 protease activity.|||In PSORS2; reduces NF-kappa-B activation.|||In PSORS2; unknown pathological significance; decreases NF-kappaB transcription factor activity.|||In PSORS2; unknown pathological significance; does not change NF-kappaB transcription factor activity.|||In PSORS2; unknown pathological significance; no effect on NF-kappaB transcription factor activity.|||In isoform 2.|||In isoform 3.|||Maintains the protein in an inactive state|||May be associated with susceptibility to psoriasis.|||May be associated with susceptibility to psoriasis; does not change MALT1 protease activity.|||PDZ|||Phosphoserine|||Unknown pathological significance; decreases NF-kappaB transcription factor activity.|||Unknown pathological significance; does not change NF-kappaB transcription factor activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144088|||http://purl.uniprot.org/annotation/VAR_022043|||http://purl.uniprot.org/annotation/VAR_024401|||http://purl.uniprot.org/annotation/VAR_048608|||http://purl.uniprot.org/annotation/VAR_059196|||http://purl.uniprot.org/annotation/VAR_061080|||http://purl.uniprot.org/annotation/VAR_068222|||http://purl.uniprot.org/annotation/VAR_068223|||http://purl.uniprot.org/annotation/VAR_068224|||http://purl.uniprot.org/annotation/VAR_068225|||http://purl.uniprot.org/annotation/VAR_068226|||http://purl.uniprot.org/annotation/VAR_068227|||http://purl.uniprot.org/annotation/VAR_068228|||http://purl.uniprot.org/annotation/VAR_068229|||http://purl.uniprot.org/annotation/VAR_068230|||http://purl.uniprot.org/annotation/VAR_068231|||http://purl.uniprot.org/annotation/VAR_068232|||http://purl.uniprot.org/annotation/VAR_068233|||http://purl.uniprot.org/annotation/VAR_068234|||http://purl.uniprot.org/annotation/VAR_068235|||http://purl.uniprot.org/annotation/VAR_068236|||http://purl.uniprot.org/annotation/VAR_068237|||http://purl.uniprot.org/annotation/VAR_068238|||http://purl.uniprot.org/annotation/VAR_068819|||http://purl.uniprot.org/annotation/VAR_068820|||http://purl.uniprot.org/annotation/VAR_078583|||http://purl.uniprot.org/annotation/VAR_078584|||http://purl.uniprot.org/annotation/VAR_078585|||http://purl.uniprot.org/annotation/VAR_078586|||http://purl.uniprot.org/annotation/VAR_078587|||http://purl.uniprot.org/annotation/VAR_078588|||http://purl.uniprot.org/annotation/VAR_078589|||http://purl.uniprot.org/annotation/VAR_078590|||http://purl.uniprot.org/annotation/VAR_078591|||http://purl.uniprot.org/annotation/VAR_078592|||http://purl.uniprot.org/annotation/VAR_078593|||http://purl.uniprot.org/annotation/VAR_078594|||http://purl.uniprot.org/annotation/VAR_078595|||http://purl.uniprot.org/annotation/VAR_078596|||http://purl.uniprot.org/annotation/VAR_078597|||http://purl.uniprot.org/annotation/VSP_047400|||http://purl.uniprot.org/annotation/VSP_047401|||http://purl.uniprot.org/annotation/VSP_047402|||http://purl.uniprot.org/annotation/VSP_047403
http://togogenome.org/gene/9606:TADA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K899|||http://purl.uniprot.org/uniprot/O75528                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Transcriptional adapter 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072416|||http://purl.uniprot.org/annotation/VSP_009739
http://togogenome.org/gene/9606:COG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTW3                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Conserved oligomeric Golgi complex subunit 1|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213491|||http://purl.uniprot.org/annotation/VAR_020415|||http://purl.uniprot.org/annotation/VAR_048756|||http://purl.uniprot.org/annotation/VAR_059231
http://togogenome.org/gene/9606:NCBP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P52298                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes mRNA cap-binding.|||Basic and acidic residues|||Disordered|||Does not affect mRNA cap-binding.|||Impairs mRNA cap-binding.|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Nuclear cap-binding protein subunit 2|||Omega-N-methylarginine|||Phosphoserine|||RRM|||Removed|||Strongly impairs mRNA cap-binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081499|||http://purl.uniprot.org/annotation/VSP_038125|||http://purl.uniprot.org/annotation/VSP_053823
http://togogenome.org/gene/9606:IDNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T6J7                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Probable gluconokinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000327370|||http://purl.uniprot.org/annotation/VAR_042433|||http://purl.uniprot.org/annotation/VSP_032735|||http://purl.uniprot.org/annotation/VSP_032736
http://togogenome.org/gene/9606:HECA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UBI9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Headcase protein homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083934
http://togogenome.org/gene/9606:ZZZ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IYH5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H-T-H motif|||HTH myb-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loss of histone H3 binding.|||Loss of histone H3 binding. Significant reduction in the acetyltransferase activity of the ATAC complex on histone H3 but no effect on the complex integrity.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Reduced histone H3 binding. Significant reduction in the acetyltransferase activity of the ATAC complex on histone H3 but no effect on the complex integrity.|||ZZ-type|||ZZ-type zinc finger-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287495|||http://purl.uniprot.org/annotation/VAR_035718|||http://purl.uniprot.org/annotation/VSP_025509|||http://purl.uniprot.org/annotation/VSP_025510|||http://purl.uniprot.org/annotation/VSP_025511|||http://purl.uniprot.org/annotation/VSP_025512|||http://purl.uniprot.org/annotation/VSP_025513
http://togogenome.org/gene/9606:GLMN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92990                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Alpha-helical region with structural similarity to HEAT repeats|||Disrupts interaction with RBX1. Loss of inhibition of SCF (SKP1-Cullin-F-box protein) E3 ubiquitin-protein ligase activity.|||Glomulin|||Important for interaction with RBX1|||In GVMs; loss of interaction with CUL1 and RBX1.|||In isoform 2.|||Loss of interaction with FKBP4 and FKBP1A.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000087513|||http://purl.uniprot.org/annotation/VAR_017241|||http://purl.uniprot.org/annotation/VAR_061653|||http://purl.uniprot.org/annotation/VSP_008882|||http://purl.uniprot.org/annotation/VSP_008883
http://togogenome.org/gene/9606:HARBI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MB7                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent                                                                                  ^@                                                                                  DDE Tnp4|||Putative nuclease HARBI1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263614
http://togogenome.org/gene/9606:ACOX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99424                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Motif|||Sequence Variant                                                                                  ^@                                                                                  In CBAS6; patient liver samples show absence of the protein; complete loss of fatty acid beta-oxidation activity.|||In CBAS6; reduces fatty acid beta-oxidation activity; does not alter subcellular location.|||Microbody targeting signal|||N6-succinyllysine|||Peroxisomal acyl-coenzyme A oxidase 2|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204681|||http://purl.uniprot.org/annotation/VAR_078764|||http://purl.uniprot.org/annotation/VAR_078765
http://togogenome.org/gene/9606:RWDD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H446                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||Interaction with DRG2|||N-acetylthreonine|||Phosphothreonine|||RWD|||RWD domain-containing protein 1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097540|||http://purl.uniprot.org/annotation/VSP_044500
http://togogenome.org/gene/9606:FAM50A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14320                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos.|||In MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect FAM50A protein levels in patient cells; does not affect localization to the nucleus.|||In MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect localization to the nucleus.|||In MRXSA; unknown pathological significance; does not affect FAM50A protein levels in patient cells; does not affect localization to the nucleus.|||Likely benign variant; it rescues craniofacial patterning defects in zebrafish morphant embryos.|||N-acetylalanine|||Nuclear localization signal|||Protein FAM50A|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068284|||http://purl.uniprot.org/annotation/VAR_084563|||http://purl.uniprot.org/annotation/VAR_084564|||http://purl.uniprot.org/annotation/VAR_084565|||http://purl.uniprot.org/annotation/VAR_084566|||http://purl.uniprot.org/annotation/VAR_084567|||http://purl.uniprot.org/annotation/VAR_084568|||http://purl.uniprot.org/annotation/VAR_084569
http://togogenome.org/gene/9606:INTU                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULD6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In SRTD20; loss of subcellular location to cilium basal body, when tested in a heterologous system.|||In SRTD20; unknown pathological significance; impairs recruitment of IFT43 to the basal body, but no effect on subcellular location, when tested in a heterologous system.|||In SRTD7/20; in an SRTD7/20 patient who also carries variant WDR35 L-311.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||PDZ|||Phosphoserine|||Polar residues|||Protein inturned                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058296|||http://purl.uniprot.org/annotation/VAR_076782|||http://purl.uniprot.org/annotation/VAR_076783|||http://purl.uniprot.org/annotation/VAR_080710|||http://purl.uniprot.org/annotation/VAR_080711|||http://purl.uniprot.org/annotation/VSP_015073|||http://purl.uniprot.org/annotation/VSP_015074|||http://purl.uniprot.org/annotation/VSP_042585|||http://purl.uniprot.org/annotation/VSP_042586|||http://purl.uniprot.org/annotation/VSP_042587
http://togogenome.org/gene/9606:KRT13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4E9|||http://purl.uniprot.org/uniprot/P13646                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||In WSN2.|||In WSN2; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Keratin, type I cytoskeletal 13|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Phosphoserine|||Polar residues|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063647|||http://purl.uniprot.org/annotation/VAR_003836|||http://purl.uniprot.org/annotation/VAR_016035|||http://purl.uniprot.org/annotation/VAR_016036|||http://purl.uniprot.org/annotation/VAR_016037|||http://purl.uniprot.org/annotation/VAR_023924|||http://purl.uniprot.org/annotation/VAR_024488|||http://purl.uniprot.org/annotation/VAR_059376|||http://purl.uniprot.org/annotation/VAR_059377|||http://purl.uniprot.org/annotation/VAR_060724|||http://purl.uniprot.org/annotation/VAR_086269|||http://purl.uniprot.org/annotation/VAR_086270|||http://purl.uniprot.org/annotation/VAR_086271|||http://purl.uniprot.org/annotation/VSP_016376|||http://purl.uniprot.org/annotation/VSP_016377|||http://purl.uniprot.org/annotation/VSP_038433
http://togogenome.org/gene/9606:SMCO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFE2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Single-pass membrane and coiled-coil domain-containing protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340699
http://togogenome.org/gene/9606:CIZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E0A3|||http://purl.uniprot.org/uniprot/B7Z3U7|||http://purl.uniprot.org/uniprot/F5H2X7|||http://purl.uniprot.org/uniprot/Q9BTG3|||http://purl.uniprot.org/uniprot/Q9ULV3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Cip1-interacting zinc finger protein|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 5.|||Matrin-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a family with adult onset primary cervical dystonia; exonic splicing enhancer mutation resulting in altered CIZ1 splicing pattern.|||Probable disease-associated variant found in patients with adult onset primary cervical dystonia.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089776|||http://purl.uniprot.org/annotation/VAR_056820|||http://purl.uniprot.org/annotation/VAR_056821|||http://purl.uniprot.org/annotation/VAR_056822|||http://purl.uniprot.org/annotation/VAR_063105|||http://purl.uniprot.org/annotation/VAR_063106|||http://purl.uniprot.org/annotation/VAR_067971|||http://purl.uniprot.org/annotation/VAR_067972|||http://purl.uniprot.org/annotation/VAR_067973|||http://purl.uniprot.org/annotation/VAR_067974|||http://purl.uniprot.org/annotation/VAR_067975|||http://purl.uniprot.org/annotation/VAR_067976|||http://purl.uniprot.org/annotation/VSP_004164|||http://purl.uniprot.org/annotation/VSP_004165|||http://purl.uniprot.org/annotation/VSP_039894|||http://purl.uniprot.org/annotation/VSP_044729
http://togogenome.org/gene/9606:TOB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P50616                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||Disordered|||Impairs interaction with CNOT7 and CNOT8.|||Important for nuclear localization|||Nuclear export signal|||Phosphothreonine|||Pro residues|||Protein Tob1|||Required for interaction with CPEB3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143812|||http://purl.uniprot.org/annotation/VAR_037840
http://togogenome.org/gene/9606:ADIPOR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86V24                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes response to ADIPOQ binding; when associated with A-202; A-219 and A-348.|||Abolishes response to ADIPOQ binding; when associated with A-219; A-348 and A-352.|||Adiponectin receptor protein 2|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with autism spectrum disorder; unknown pathological significance.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Impairs response to ADIPOQ binding. Abolishes response to ADIPOQ binding; when associated with A-202; A-219 and A-352.|||Impairs response to ADIPOQ binding. Abolishes response to ADIPOQ binding; when associated with A-202; A-348 and A-352.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218829|||http://purl.uniprot.org/annotation/VAR_048203|||http://purl.uniprot.org/annotation/VAR_078687
http://togogenome.org/gene/9606:SCN8A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6B4S4|||http://purl.uniprot.org/uniprot/Q9UQD0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Name=S1 of repeat I|||Helical; Name=S1 of repeat II|||Helical; Name=S1 of repeat III|||Helical; Name=S1 of repeat IV|||Helical; Name=S2 of repeat I|||Helical; Name=S2 of repeat II|||Helical; Name=S2 of repeat III|||Helical; Name=S2 of repeat IV|||Helical; Name=S3 of repeat I|||Helical; Name=S3 of repeat II|||Helical; Name=S3 of repeat III|||Helical; Name=S3 of repeat IV|||Helical; Name=S4 of repeat I|||Helical; Name=S4 of repeat II|||Helical; Name=S4 of repeat III|||Helical; Name=S4 of repeat IV|||Helical; Name=S5 of repeat I|||Helical; Name=S5 of repeat II|||Helical; Name=S5 of repeat III|||Helical; Name=S5 of repeat IV|||Helical; Name=S6 of repeat I|||Helical; Name=S6 of repeat II|||Helical; Name=S6 of repeat III|||Helical; Name=S6 of repeat IV|||I|||II|||III|||IQ|||IV|||In BFIS5.|||In DEE13 and BFIS5; also found in a patient with drug-resistant focal epilepsy and mild intellectual disability.|||In DEE13.|||In DEE13; gain-of-function mutation; increased channel activity.|||In DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation.|||In DEE13; gain-of-function mutation; increased channel activity; impaired channel inactivation; no effect on interactions with FGF14, SCN1B, GNB2 and GNG3.|||In DEE13; gain-of-function mutation; increases channel activity.|||In DEE13; gain-of-function mutation; results in increased persistent sodium currents and incomplete channel inactivation.|||In DEE13; loss of channel activity.|||In DEE13; loss of function mutation; reduces channel activity.|||In DEE13; requires 2 nucleotide substitutions.|||In DEE13; unknown pathological significance.|||In DEE13; unknown pathological significance; no effect on channel activity.|||In DEE13; unknown pathological significance; requires 2 nucleotide substitutions.|||In MYOCL2; decreased channel activity; results in significantly reduced inward sodium current without changes of voltage-dependent channel activation and inactivation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interchain; with SCN2B or SCN4B|||Interchain; with the conotoxin GVIIJ (when the channel is not linked to SCN2B or SCN4B; the bond to SCN2B or SCN4B protects the channel from the inhibition by toxin)|||Ion transport|||N-linked (GlcNAc...) (high mannose) asparagine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Pore-forming|||Reduced inhibition by 4,9-anhydro-tetrodotoxin.|||Sodium channel protein type 8 subunit alpha|||Voltage-gated Na+ ion channel cytoplasmic                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048500|||http://purl.uniprot.org/annotation/VAR_067539|||http://purl.uniprot.org/annotation/VAR_071674|||http://purl.uniprot.org/annotation/VAR_071675|||http://purl.uniprot.org/annotation/VAR_071676|||http://purl.uniprot.org/annotation/VAR_071677|||http://purl.uniprot.org/annotation/VAR_071678|||http://purl.uniprot.org/annotation/VAR_071679|||http://purl.uniprot.org/annotation/VAR_071680|||http://purl.uniprot.org/annotation/VAR_071681|||http://purl.uniprot.org/annotation/VAR_072182|||http://purl.uniprot.org/annotation/VAR_072183|||http://purl.uniprot.org/annotation/VAR_076598|||http://purl.uniprot.org/annotation/VAR_076599|||http://purl.uniprot.org/annotation/VAR_076600|||http://purl.uniprot.org/annotation/VAR_076601|||http://purl.uniprot.org/annotation/VAR_076602|||http://purl.uniprot.org/annotation/VAR_076603|||http://purl.uniprot.org/annotation/VAR_076604|||http://purl.uniprot.org/annotation/VAR_076605|||http://purl.uniprot.org/annotation/VAR_076606|||http://purl.uniprot.org/annotation/VAR_076607|||http://purl.uniprot.org/annotation/VAR_076608|||http://purl.uniprot.org/annotation/VAR_076609|||http://purl.uniprot.org/annotation/VAR_076610|||http://purl.uniprot.org/annotation/VAR_076611|||http://purl.uniprot.org/annotation/VAR_076612|||http://purl.uniprot.org/annotation/VAR_076613|||http://purl.uniprot.org/annotation/VAR_076614|||http://purl.uniprot.org/annotation/VAR_076615|||http://purl.uniprot.org/annotation/VAR_076616|||http://purl.uniprot.org/annotation/VAR_076617|||http://purl.uniprot.org/annotation/VAR_076927|||http://purl.uniprot.org/annotation/VAR_078202|||http://purl.uniprot.org/annotation/VAR_078203|||http://purl.uniprot.org/annotation/VAR_078204|||http://purl.uniprot.org/annotation/VAR_078612|||http://purl.uniprot.org/annotation/VAR_078613|||http://purl.uniprot.org/annotation/VAR_078752|||http://purl.uniprot.org/annotation/VAR_078753|||http://purl.uniprot.org/annotation/VAR_078754|||http://purl.uniprot.org/annotation/VAR_078755|||http://purl.uniprot.org/annotation/VAR_078756|||http://purl.uniprot.org/annotation/VAR_079722|||http://purl.uniprot.org/annotation/VAR_079723|||http://purl.uniprot.org/annotation/VAR_079724|||http://purl.uniprot.org/annotation/VAR_079725|||http://purl.uniprot.org/annotation/VAR_082076|||http://purl.uniprot.org/annotation/VSP_038651|||http://purl.uniprot.org/annotation/VSP_050589|||http://purl.uniprot.org/annotation/VSP_050590|||http://purl.uniprot.org/annotation/VSP_050591|||http://purl.uniprot.org/annotation/VSP_050592|||http://purl.uniprot.org/annotation/VSP_050593
http://togogenome.org/gene/9606:ASXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q76L83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Breakpoint for translocation to form KAT6A-ASXL2 protein|||DEUBAD|||Disordered|||HTH HARE-type|||In isoform 2.|||LXXLL motif 1|||LXXLL motif 2|||Nuclear localization signal|||PHD-type; atypical|||Phosphoserine|||Polar residues|||Putative Polycomb group protein ASXL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313826|||http://purl.uniprot.org/annotation/VAR_037773|||http://purl.uniprot.org/annotation/VAR_037774|||http://purl.uniprot.org/annotation/VAR_037775|||http://purl.uniprot.org/annotation/VAR_037776|||http://purl.uniprot.org/annotation/VSP_030163|||http://purl.uniprot.org/annotation/VSP_030164
http://togogenome.org/gene/9606:ARL6IP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q66PJ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 6-interacting protein 4|||Basic and acidic residues|||Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In RNA edited version.|||In isoform 1, isoform 2, isoform 3, isoform 6 and isoform 4.|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4, isoform 9 and isoform 10.|||In isoform 4 and isoform 10.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312270|||http://purl.uniprot.org/annotation/VAR_058333|||http://purl.uniprot.org/annotation/VSP_061424|||http://purl.uniprot.org/annotation/VSP_061425|||http://purl.uniprot.org/annotation/VSP_061426|||http://purl.uniprot.org/annotation/VSP_061427|||http://purl.uniprot.org/annotation/VSP_061428|||http://purl.uniprot.org/annotation/VSP_061429|||http://purl.uniprot.org/annotation/VSP_061430|||http://purl.uniprot.org/annotation/VSP_061431
http://togogenome.org/gene/9606:FBXW10B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WSX6|||http://purl.uniprot.org/uniprot/O95170|||http://purl.uniprot.org/uniprot/Q59EB2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  B box-type|||Basic and acidic residues|||Disordered|||F-box and WD repeat domain containing protein 10B|||In isoform 2.|||Pro residues|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315833|||http://purl.uniprot.org/annotation/VAR_038340|||http://purl.uniprot.org/annotation/VSP_040554
http://togogenome.org/gene/9606:HLA-DRB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A224MM52|||http://purl.uniprot.org/uniprot/D7RIH8|||http://purl.uniprot.org/uniprot/P01911|||http://purl.uniprot.org/uniprot/X5DNQ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Beta-1|||Beta-2|||Cytoplasmic|||Decreases the interaction with CD4.|||Decreases the interaction with CD4; when assocated with A-166.|||Decreases the interaction with CD4; when assocated with A-172.|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||HLA class II histocompatibility antigen, DRB1 beta chain|||Helical|||Ig-like|||Ig-like C1-type|||Impairs MARCHF1-dependent down-regulation through ubiquitination.|||In allele DRB1*01:01 and allele DRB1*01:02.|||In allele DRB1*01:01 and allele DRB1*01:02; associated with increased risk for rheumatoid arthritis.|||In allele DRB1*01:01, allele DRB1*01:02 and allele DRB1*09:01.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*10:01, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07 and allele DRB1*16:02.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:01, allele DRB1*03:02,allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*13:03, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*03:02, allele DRB1*07:01, allele DRB1*10:01, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*14:03 and allele DRB1*14:06.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06, allele DRB1*14:07, allele DRB1*16:01 and allele DRB1*16:02; requires 2 nucleotide substitutions.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*09:01 and allele DRB1*10:01; associated with increased risk for rheumatoid arthritis; requires 2 nucleotide substitutions.|||In allele DRB1*01:01, allele DRB1*01:02, allele DRB1*10:01, allele DRB1*12:01 and allele DRB1*12:02.|||In allele DRB1*01:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:05, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:03, allele DRB1*14:07, allele DRB1*15:02, allele DRB1*16:01 and allele DRB1*16:02.|||In allele DRB1*01:02, allele DRB1*11:06, allele DRB1*12:01, allele DRB1*12:02.|||In allele DRB1*03:01 and allele DRB1*03:02; requires 2 nucleotide substitutions.|||In allele DRB1*03:01, allele DRB1*03:02 and allele DRB1*07:01.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01 and allele DRB1*13:03; requires 2 nucleotide substitutions.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07; requires 2 nucleotide substitutions.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07; requires 2 nucleotide substitutions.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*09:01, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:05, allele DRB1*14:03 and allele DRB1*14:06.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*10:01, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:05, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:01, allele DRB1*14:03, allele DRB1*14:05, allele DRB1*14:06 and allele DRB1*14:07.|||In allele DRB1*03:01, allele DRB1*03:02.|||In allele DRB1*03:01, allele DRB1*09:01.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11; associated with increased risk for rheumatoid arthritis.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10 and allele DRB1*04:11; requires 2 nucleotide substitutions.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11 and allele DRB1*10:01.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11 and allele DRB1*10:01; associated with increased risk for rheumatoid arthritis; requires 2 nucleotide substitutions.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*07:01 and allele DRB1*09:01.|||In allele DRB1*04:01, allele DRB1*04:02, allele DRB1*04:04, allele DRB1*04:05, allele DRB1*04:07, allele DRB1*04:08, allele DRB1*04:10, allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*10:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*13:03, allele DRB1*13:07 and allele DRB1*13:12.|||In allele DRB1*04:02, allele DRB1*07:01, allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*11:19, allele DRB1*12:01, allele DRB1*12:02, allele DRB1*13:01, allele DRB1*13:02, allele DRB1*13:03, allele DRB1*13:05, allele DRB1*13:07, allele DRB1*13:12, allele DRB1*14:03, allele DRB1*16:01 and allele DRB1*16:02; requires 2 nucleotide substitutions.|||In allele DRB1*04:02, allele DRB1*11:11, allele DRB1*13:01 and allele DRB1*13:02.|||In allele DRB1*04:05, allele DRB1*04:10; allele DRB1*04:11, allele DRB1*08:01, allele DRB1*08:03, allele DRB1*13:03 and allele DRB1*13:12; requires 2 nucleotide substitutions.|||In allele DRB1*04:06, allele DRB1*04:07, allele DRB1*04:11, allele DRB1*09:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07.|||In allele DRB1*07:01 and allele DRB1*09:01.|||In allele DRB1*07:01 and allele DRB1*09:01; requires 2 nucleotide substitutions.|||In allele DRB1*07:01, allele DRB1*09:01 and allele DRB1*10:01.|||In allele DRB1*07:01, allele DRB1*09:01, allele DRB1*12:01 and allele DRB1*12:02.|||In allele DRB1*07:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07.|||In allele DRB1*07:01.|||In allele DRB1*07:01; requires 2 nucleotide substitutions.|||In allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03 and allele DRB1*08:04.|||In allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04 and allele DRB1*14:03; requires 2 nucleotide substitutions.|||In allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:03, allele DRB1*08:04, allele DRB1*12:01 and allele DRB1*12:02.|||In allele DRB1*08:01, allele DRB1*08:02, allele DRB1*08:04, allele DRB1*09:01, allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11, allele DRB1*12:02, allele DRB1*13:05, allele DRB1*13:07 and allele DRB1*16:01.|||In allele DRB1*09:01, allele DRB1*10:01, allele DRB1*14:01, allele DRB1*14:05 and allele DRB1*14:07.|||In allele DRB1*09:01.|||In allele DRB1*09:01; requires 2 nucleotide substitutions.|||In allele DRB1*10:01.|||In allele DRB1*10:01; requires 2 nucleotide substitutions.|||In allele DRB1*11:01, allele DRB1*11:04, allele DRB1*11:06, allele DRB1*11:11 and allele DRB1*11:19.|||In allele DRB1*12:01 and allele DRB1*12:02.|||In allele DRB1*12:01, allele DRB1*12:02 and allele DRB1*15:03.|||In allele DRB1*14:01, allele DRB1*14:07.|||In allele DRB1*14:01.|||In allele DRB1*14:05.|||N-linked (GlcNAc...) asparagine|||Reduces the interaction with HLA-DM complex that results in impaired dissociation of CLIP from MHCII. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080744|||http://purl.uniprot.org/annotation/PRO_5004954496|||http://purl.uniprot.org/annotation/PRO_5014302684|||http://purl.uniprot.org/annotation/PRO_5033294908|||http://purl.uniprot.org/annotation/VAR_082703|||http://purl.uniprot.org/annotation/VAR_082704|||http://purl.uniprot.org/annotation/VAR_082705|||http://purl.uniprot.org/annotation/VAR_082706|||http://purl.uniprot.org/annotation/VAR_082707|||http://purl.uniprot.org/annotation/VAR_082708|||http://purl.uniprot.org/annotation/VAR_082709|||http://purl.uniprot.org/annotation/VAR_082710|||http://purl.uniprot.org/annotation/VAR_082711|||http://purl.uniprot.org/annotation/VAR_082712|||http://purl.uniprot.org/annotation/VAR_082713|||http://purl.uniprot.org/annotation/VAR_082714|||http://purl.uniprot.org/annotation/VAR_082715|||http://purl.uniprot.org/annotation/VAR_082716|||http://purl.uniprot.org/annotation/VAR_082717|||http://purl.uniprot.org/annotation/VAR_082718|||http://purl.uniprot.org/annotation/VAR_082719|||http://purl.uniprot.org/annotation/VAR_082720|||http://purl.uniprot.org/annotation/VAR_082721|||http://purl.uniprot.org/annotation/VAR_082722|||http://purl.uniprot.org/annotation/VAR_082723|||http://purl.uniprot.org/annotation/VAR_082724|||http://purl.uniprot.org/annotation/VAR_082725|||http://purl.uniprot.org/annotation/VAR_082726|||http://purl.uniprot.org/annotation/VAR_082727|||http://purl.uniprot.org/annotation/VAR_082728|||http://purl.uniprot.org/annotation/VAR_082729|||http://purl.uniprot.org/annotation/VAR_082730|||http://purl.uniprot.org/annotation/VAR_082731|||http://purl.uniprot.org/annotation/VAR_082732|||http://purl.uniprot.org/annotation/VAR_082733|||http://purl.uniprot.org/annotation/VAR_082734|||http://purl.uniprot.org/annotation/VAR_082735|||http://purl.uniprot.org/annotation/VAR_082736|||http://purl.uniprot.org/annotation/VAR_082737|||http://purl.uniprot.org/annotation/VAR_082738|||http://purl.uniprot.org/annotation/VAR_082739|||http://purl.uniprot.org/annotation/VAR_082740|||http://purl.uniprot.org/annotation/VAR_082741|||http://purl.uniprot.org/annotation/VAR_082742|||http://purl.uniprot.org/annotation/VAR_082743|||http://purl.uniprot.org/annotation/VAR_082744|||http://purl.uniprot.org/annotation/VAR_082745|||http://purl.uniprot.org/annotation/VAR_082746|||http://purl.uniprot.org/annotation/VAR_082747|||http://purl.uniprot.org/annotation/VAR_082748|||http://purl.uniprot.org/annotation/VAR_082749|||http://purl.uniprot.org/annotation/VAR_082750|||http://purl.uniprot.org/annotation/VAR_082751|||http://purl.uniprot.org/annotation/VAR_082752|||http://purl.uniprot.org/annotation/VAR_082753|||http://purl.uniprot.org/annotation/VAR_082754|||http://purl.uniprot.org/annotation/VAR_082755|||http://purl.uniprot.org/annotation/VAR_082756|||http://purl.uniprot.org/annotation/VAR_082757|||http://purl.uniprot.org/annotation/VAR_082758|||http://purl.uniprot.org/annotation/VAR_082759|||http://purl.uniprot.org/annotation/VAR_082760|||http://purl.uniprot.org/annotation/VAR_082761|||http://purl.uniprot.org/annotation/VAR_082762|||http://purl.uniprot.org/annotation/VAR_082763|||http://purl.uniprot.org/annotation/VAR_082764|||http://purl.uniprot.org/annotation/VAR_082765|||http://purl.uniprot.org/annotation/VAR_082766|||http://purl.uniprot.org/annotation/VAR_082767|||http://purl.uniprot.org/annotation/VAR_082768|||http://purl.uniprot.org/annotation/VAR_082769|||http://purl.uniprot.org/annotation/VAR_082770|||http://purl.uniprot.org/annotation/VAR_082771|||http://purl.uniprot.org/annotation/VAR_082772|||http://purl.uniprot.org/annotation/VAR_082773|||http://purl.uniprot.org/annotation/VAR_082774|||http://purl.uniprot.org/annotation/VAR_082775|||http://purl.uniprot.org/annotation/VAR_082776|||http://purl.uniprot.org/annotation/VAR_082777|||http://purl.uniprot.org/annotation/VAR_082778|||http://purl.uniprot.org/annotation/VAR_082779|||http://purl.uniprot.org/annotation/VAR_082780|||http://purl.uniprot.org/annotation/VAR_082781|||http://purl.uniprot.org/annotation/VAR_082782|||http://purl.uniprot.org/annotation/VAR_082783|||http://purl.uniprot.org/annotation/VAR_082784|||http://purl.uniprot.org/annotation/VAR_082785|||http://purl.uniprot.org/annotation/VAR_082786|||http://purl.uniprot.org/annotation/VAR_082787
http://togogenome.org/gene/9606:ENAH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A4D6J698|||http://purl.uniprot.org/uniprot/Q8N8S7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||8|||9|||9 X 5 AA tandem repeats of [LMQ]-E-[QR]-E-[QR]|||Basic and acidic residues|||Disordered|||EVH2|||EVH2 block A|||EVH2 block B|||EVH2 block C|||In isoform 2.|||In isoform 3.|||KLKR|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Pro residues|||Protein enabled homolog|||WH1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086971|||http://purl.uniprot.org/annotation/VSP_010564|||http://purl.uniprot.org/annotation/VSP_053772|||http://purl.uniprot.org/annotation/VSP_053773
http://togogenome.org/gene/9606:PLXNB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K920|||http://purl.uniprot.org/uniprot/Q9ULL4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||IPT/TIG 1|||IPT/TIG 2|||IPT/TIG 3|||IPT/TIG 4|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PSI 1|||PSI 2|||PSI 3|||Plexin-B3|||Sema                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024674|||http://purl.uniprot.org/annotation/PRO_5002722814|||http://purl.uniprot.org/annotation/VAR_019681|||http://purl.uniprot.org/annotation/VAR_019682|||http://purl.uniprot.org/annotation/VAR_050601|||http://purl.uniprot.org/annotation/VAR_061538|||http://purl.uniprot.org/annotation/VAR_068807|||http://purl.uniprot.org/annotation/VAR_079495|||http://purl.uniprot.org/annotation/VSP_044467
http://togogenome.org/gene/9606:TFDP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14186                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||DCB1|||DCB2|||DEF box|||Dimerization|||Disordered|||Enhances binding of RB protein to E2F|||In isoform 2.|||Interaction with CEBPA|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Transcription factor Dp-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219475|||http://purl.uniprot.org/annotation/VAR_029293|||http://purl.uniprot.org/annotation/VSP_056499|||http://purl.uniprot.org/annotation/VSP_056500
http://togogenome.org/gene/9606:GPAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86T70|||http://purl.uniprot.org/uniprot/Q8N1G6|||http://purl.uniprot.org/uniprot/Q9HCL2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transit Peptide|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Glycerol-3-phosphate acyltransferase 1, mitochondrial|||HXXXXD motif|||Helical|||Mitochondrial intermembrane|||Mitochondrion|||N6-acetyllysine|||Phospholipid/glycerol acyltransferase|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024690|||http://purl.uniprot.org/annotation/VAR_050585|||http://purl.uniprot.org/annotation/VAR_050586|||http://purl.uniprot.org/annotation/VAR_050587|||http://purl.uniprot.org/annotation/VAR_050588
http://togogenome.org/gene/9606:RBFOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z1U7|||http://purl.uniprot.org/uniprot/Q59HD3|||http://purl.uniprot.org/uniprot/Q9NWB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Interaction with RNA|||No effect on RNA-binding.|||Omega-N-methylarginine|||Polar residues|||RNA binding protein fox-1 homolog 1|||RRM|||Reduces RNA-binding affinity 15-fold.|||Reduces RNA-binding affinity 1500-fold.|||Reduces RNA-binding affinity 160-fold.|||Reduces RNA-binding affinity 30'000-fold.|||Reduces RNA-binding affinity 700-fold.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081480|||http://purl.uniprot.org/annotation/VSP_030874|||http://purl.uniprot.org/annotation/VSP_030875|||http://purl.uniprot.org/annotation/VSP_030876|||http://purl.uniprot.org/annotation/VSP_030877|||http://purl.uniprot.org/annotation/VSP_030878
http://togogenome.org/gene/9606:CABLES2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BTV7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  CDK5 and ABL1 enzyme substrate 2|||Disordered|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080512|||http://purl.uniprot.org/annotation/VAR_026532
http://togogenome.org/gene/9606:TRIM56                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRZ2                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  B box-type 1|||B box-type 2|||Basic and acidic residues|||Complete loss of autoubiquitination, loss of antiviral activity against yellow fever virus and human coronavirus virus OC43, but normal induction of interferon-beta following Sendia virus infection; when associated with A-24.|||Complete loss of autoubiquitination. Complete loss of autoubiquitination, loss of antiviral activity against yellow fever virus and human coronavirus virus OC43, but normal induction of interferon-beta following Sendai virus infection; when associated with A-24.|||Disordered|||E3 ubiquitin-protein ligase TRIM56|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056288|||http://purl.uniprot.org/annotation/VSP_029109|||http://purl.uniprot.org/annotation/VSP_029110|||http://purl.uniprot.org/annotation/VSP_029111|||http://purl.uniprot.org/annotation/VSP_029112
http://togogenome.org/gene/9606:OR5P2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVJ7|||http://purl.uniprot.org/uniprot/Q8WZ92                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 5P2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150610|||http://purl.uniprot.org/annotation/VAR_053203|||http://purl.uniprot.org/annotation/VAR_053204
http://togogenome.org/gene/9606:COPG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK12|||http://purl.uniprot.org/uniprot/Q9NSM7|||http://purl.uniprot.org/uniprot/Q9UBF2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Clathrin/coatomer adaptor adaptin-like N-terminal|||Coatomer gamma subunit appendage Ig-like subdomain|||Coatomer subunit gamma C-terminal|||Coatomer subunit gamma-2|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||HEAT 5|||HEAT 6|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193862|||http://purl.uniprot.org/annotation/VAR_060181|||http://purl.uniprot.org/annotation/VAR_060182|||http://purl.uniprot.org/annotation/VSP_055534|||http://purl.uniprot.org/annotation/VSP_055535
http://togogenome.org/gene/9606:TSBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7D1|||http://purl.uniprot.org/uniprot/B4DXY0|||http://purl.uniprot.org/uniprot/E9PLW3|||http://purl.uniprot.org/uniprot/Q13647|||http://purl.uniprot.org/uniprot/Q5SRN2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||Polar residues|||Testis-expressed basic protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089503|||http://purl.uniprot.org/annotation/VAR_022875|||http://purl.uniprot.org/annotation/VAR_022876|||http://purl.uniprot.org/annotation/VAR_022877|||http://purl.uniprot.org/annotation/VAR_022878|||http://purl.uniprot.org/annotation/VAR_022879|||http://purl.uniprot.org/annotation/VAR_022880|||http://purl.uniprot.org/annotation/VAR_022881|||http://purl.uniprot.org/annotation/VAR_022882|||http://purl.uniprot.org/annotation/VAR_022883|||http://purl.uniprot.org/annotation/VAR_033068|||http://purl.uniprot.org/annotation/VAR_056793|||http://purl.uniprot.org/annotation/VAR_056794|||http://purl.uniprot.org/annotation/VAR_056795|||http://purl.uniprot.org/annotation/VAR_056796|||http://purl.uniprot.org/annotation/VSP_014645|||http://purl.uniprot.org/annotation/VSP_014646|||http://purl.uniprot.org/annotation/VSP_014647|||http://purl.uniprot.org/annotation/VSP_055702
http://togogenome.org/gene/9606:ATG9A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3C6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||INTRAMEM|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished N-glycosylation.|||Abolished interaction with the AP-4 complex.|||Autophagy-related protein 9A|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect interaction with the AP-4 complex.|||Does not affect lipid scramblase activity. Strongly reduced autophagy; when associated with L-321--L-323.|||Helical|||Impaired autophagy.|||Impaired transport from the endoplasmic reticulum to the Golgi apparatus without affecting homooligomerization.|||Impaired transport through the Golgi apparatus.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylalanine|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Reduced lipid scramblase activity and autophagy. Strongly reduced autophagy; when associated with W-412. Strongly reduced lipid scramblase activity and autophagy; when associated with W-419.|||Removed|||Strongly reduced lipid scramblase activity and autophagy; when associated with L-321--L-323.|||Tyrosine-based sorting signal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119820|||http://purl.uniprot.org/annotation/VAR_021835|||http://purl.uniprot.org/annotation/VAR_055534|||http://purl.uniprot.org/annotation/VSP_013396|||http://purl.uniprot.org/annotation/VSP_013397|||http://purl.uniprot.org/annotation/VSP_013398
http://togogenome.org/gene/9606:F11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P03951                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Apple 1|||Apple 2|||Apple 3|||Apple 4|||Charge relay system|||Coagulation factor XIa heavy chain|||Coagulation factor XIa light chain|||Found in a patient with factor XI deficiency that also carries mutation N-266.|||In FA11D.|||In FA11D; although the mutant protein is synthesized the secretion is reduced.|||In FA11D; dominant-negative mutation that results in severely decreased protein secretion.|||In FA11D; mild phenotype.|||In FA11D; mutant is not secreted by transfected fibroblasts; dominant-negative effect.|||In FA11D; secretion of the mutant protein is impaired.|||In FA11D; transfected cells contain reduced amount of mutant protein and display decreased secretion.|||In isoform 2.|||Interchain|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) (complex) asparagine; atypical|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027825|||http://purl.uniprot.org/annotation/PRO_0000027826|||http://purl.uniprot.org/annotation/VAR_006622|||http://purl.uniprot.org/annotation/VAR_011774|||http://purl.uniprot.org/annotation/VAR_011775|||http://purl.uniprot.org/annotation/VAR_011776|||http://purl.uniprot.org/annotation/VAR_011777|||http://purl.uniprot.org/annotation/VAR_011778|||http://purl.uniprot.org/annotation/VAR_012085|||http://purl.uniprot.org/annotation/VAR_012086|||http://purl.uniprot.org/annotation/VAR_012087|||http://purl.uniprot.org/annotation/VAR_012088|||http://purl.uniprot.org/annotation/VAR_012089|||http://purl.uniprot.org/annotation/VAR_012090|||http://purl.uniprot.org/annotation/VAR_012091|||http://purl.uniprot.org/annotation/VAR_012092|||http://purl.uniprot.org/annotation/VAR_012093|||http://purl.uniprot.org/annotation/VAR_012094|||http://purl.uniprot.org/annotation/VAR_012095|||http://purl.uniprot.org/annotation/VAR_012096|||http://purl.uniprot.org/annotation/VAR_054894|||http://purl.uniprot.org/annotation/VAR_054895|||http://purl.uniprot.org/annotation/VAR_054896|||http://purl.uniprot.org/annotation/VAR_054897|||http://purl.uniprot.org/annotation/VAR_054898|||http://purl.uniprot.org/annotation/VAR_054899|||http://purl.uniprot.org/annotation/VAR_054900|||http://purl.uniprot.org/annotation/VAR_054901|||http://purl.uniprot.org/annotation/VAR_054902|||http://purl.uniprot.org/annotation/VAR_054903|||http://purl.uniprot.org/annotation/VAR_054904|||http://purl.uniprot.org/annotation/VAR_054905|||http://purl.uniprot.org/annotation/VAR_054906|||http://purl.uniprot.org/annotation/VAR_067929|||http://purl.uniprot.org/annotation/VAR_067930|||http://purl.uniprot.org/annotation/VAR_067931|||http://purl.uniprot.org/annotation/VAR_067932|||http://purl.uniprot.org/annotation/VAR_067933|||http://purl.uniprot.org/annotation/VAR_067934|||http://purl.uniprot.org/annotation/VAR_067935|||http://purl.uniprot.org/annotation/VAR_067936|||http://purl.uniprot.org/annotation/VAR_067937|||http://purl.uniprot.org/annotation/VAR_067938|||http://purl.uniprot.org/annotation/VAR_067939|||http://purl.uniprot.org/annotation/VAR_067940|||http://purl.uniprot.org/annotation/VAR_067941|||http://purl.uniprot.org/annotation/VAR_067942|||http://purl.uniprot.org/annotation/VAR_067943|||http://purl.uniprot.org/annotation/VAR_067944|||http://purl.uniprot.org/annotation/VAR_067945|||http://purl.uniprot.org/annotation/VAR_067946|||http://purl.uniprot.org/annotation/VAR_067947|||http://purl.uniprot.org/annotation/VAR_067948|||http://purl.uniprot.org/annotation/VAR_067949|||http://purl.uniprot.org/annotation/VAR_067950|||http://purl.uniprot.org/annotation/VAR_067951|||http://purl.uniprot.org/annotation/VAR_067952|||http://purl.uniprot.org/annotation/VAR_067953|||http://purl.uniprot.org/annotation/VAR_067954|||http://purl.uniprot.org/annotation/VAR_067955|||http://purl.uniprot.org/annotation/VAR_076515|||http://purl.uniprot.org/annotation/VAR_076516|||http://purl.uniprot.org/annotation/VAR_076517|||http://purl.uniprot.org/annotation/VAR_076518|||http://purl.uniprot.org/annotation/VAR_076519|||http://purl.uniprot.org/annotation/VSP_005388
http://togogenome.org/gene/9606:CCNJ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T5M9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  Cyclin N-terminal|||Cyclin-J|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309316|||http://purl.uniprot.org/annotation/VSP_029128|||http://purl.uniprot.org/annotation/VSP_041163
http://togogenome.org/gene/9606:SCGB1C1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TD33                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Secretoglobin family 1C member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223332|||http://purl.uniprot.org/annotation/VAR_063102
http://togogenome.org/gene/9606:SPRR2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22532                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 9 AA tandem repeats of P-K-C-P-[EQ]-P-C-P-[PS]|||Disordered|||Small proline-rich protein 2D                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150010|||http://purl.uniprot.org/annotation/VAR_053049
http://togogenome.org/gene/9606:NLRP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86W26                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Site|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||NACHT|||NACHT, LRR and PYD domains-containing protein 10|||Polar residues|||Pyrin|||Reduced release of IL8 following invasive bacterial infection.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080896
http://togogenome.org/gene/9606:KLF15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UIH9                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Helix|||Motif|||Region|||Strand|||Zinc Finger                                                                                  ^@                                                                                  9aaTAD|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 15                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047187
http://togogenome.org/gene/9606:PYCARD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULZ3                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes homooligomerization.|||Abolishes interaction with NLRP2.|||Abolishes interaction with PYDC1.|||Abolishes promotion of apoptosis and NF-kappa-B activation.|||Apoptosis-associated speck-like protein containing a CARD|||CARD|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Loss of inflammasome activation activity.|||Phosphoserine|||Pyrin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064692|||http://purl.uniprot.org/annotation/VSP_004118|||http://purl.uniprot.org/annotation/VSP_004119
http://togogenome.org/gene/9606:TMED10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49755                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  COPI vesicle coat-binding|||COPII vesicle coat-binding|||Cytoplasmic|||Dimethylated arginine|||Disrupts interaction with COPG1 and association with coatomer; when associated with 211-A-A-212.|||Disrupts interaction with COPG1 and association with coatomer; when associated with 215-A-A-216.|||GOLD|||Helical|||Interaction with ARF1 and IL1B|||Interaction with COPG1|||Lumenal|||N-linked (GlcNAc...) asparagine|||No decrease in binding to COPG1. Disrupts interaction with SEC23A.|||Required for TMED10 and TMED2 cis-Golgi network localization|||Required for interaction with STX17|||Significant reduction in binding to COPG1.|||Transmembrane emp24 domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010399|||http://purl.uniprot.org/annotation/VAR_012051|||http://purl.uniprot.org/annotation/VAR_049111
http://togogenome.org/gene/9606:AICDA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q546Y9|||http://purl.uniprot.org/uniprot/Q7Z599|||http://purl.uniprot.org/uniprot/Q9GZX7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Bipartite nuclear localization signal|||CMP/dCMP-type deaminase|||Completely abolishes nuclear import; when associated with W-24 or D-112. Little affect on nuclear import; when associated with A-10. Greatly impaired nuclear import; when associated with K-20 or G-50. Almost completely abolishes nuclear import; when associated with S-18 and V-19.|||Greatly impaired nuclear import; when associated with S-18 and A-193. Reduced interaction with both CTNNBL1 and KPNA1, and abolishes immunoglobulin class switching; when associated with S-18.|||Greatly impaired nuclear import; when associated with V-19 and A-193. Reduced interaction with both CTNNBL1 and KPNA1, and abolishes immunoglobulin class switching; when associated with V-19.|||Greatly reduced interaction with CTNNBL1 but no effect on subcellular location, enzyme activity, ability to oligomerize nor on phosphorylation at Ser-38. Diminished antibody diversification.|||Greatly reduced nuclear import; when associated with A-193.|||Impaired nuclear import; when associated with A-193. No effect on CTNNBL1 binding.|||Important for interaction with CTNNBL1|||In HIGM2.|||In HIGM2; completely abolishes nuclear import and interaction with CTNNBL1, diminishes interaction with KPNA1 and abolishes immunoglobulin class switching.|||In HIGM2; slightly decreased mutagenic activity.|||In HIGM2; unknown pathological significance.|||In HIGM2; unknown pathological significance; loss of mutagenic activity.|||In isoform 2.|||Interaction with SUPT6H|||Little effect on nuclear import; when associated with A-193. No effect on CTNNBL1 binding.|||Loss of phosphorylation. Impaired class-switch recombination activity. No effect on interaction with CTNNBL1.|||Loss of phosphorylation. No effect on cytidine deaminase activity. Impaired class-switch recombination activity.|||No effect on interaction with CTNNBL1.|||Nuclear export signal|||Phosphomimetic mutant which shows loss of cytidine deaminase activity and impaired class-switch recombination activity.|||Phosphoserine; by PKA|||Phosphothreonine; by PKA|||Proton donor|||Required for interaction with RNF126|||Single-stranded DNA cytosine deaminase|||Some reduced nuclear import; when associated with A-193.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171687|||http://purl.uniprot.org/annotation/VAR_013774|||http://purl.uniprot.org/annotation/VAR_013775|||http://purl.uniprot.org/annotation/VAR_013776|||http://purl.uniprot.org/annotation/VAR_013777|||http://purl.uniprot.org/annotation/VAR_013778|||http://purl.uniprot.org/annotation/VAR_014091|||http://purl.uniprot.org/annotation/VAR_077563|||http://purl.uniprot.org/annotation/VAR_077564|||http://purl.uniprot.org/annotation/VAR_077565|||http://purl.uniprot.org/annotation/VAR_077566|||http://purl.uniprot.org/annotation/VAR_077567|||http://purl.uniprot.org/annotation/VAR_077568|||http://purl.uniprot.org/annotation/VSP_047803
http://togogenome.org/gene/9606:IFNGR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3Y2|||http://purl.uniprot.org/uniprot/A0A2R8Y4U4|||http://purl.uniprot.org/uniprot/P15260                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with susceptibility to Helicobacter pylori infection; may influence susceptibility to allergic diseases such as bronchial asthma and allergic rhinitis; could be detected on the cell surface; no significant effect on interferon-gamma-mediated signaling pathway.|||Associated with susceptibility to Helicobacter pylori infection; no significant effect on interferon-gamma-mediated signaling pathway.|||Associated with susceptibility to atopic dermatitis complicated by eczema herpeticum; does not affect completely interferon-gamma-mediated signaling pathway.|||Could be detected on the cell surface; does not affect interferon-gamma-mediated signaling pathway.|||Cytoplasmic|||Disordered|||Extracellular|||Fibronectin type-III|||Helical|||In IMD27A.|||In IMD27A; could be detected on the cell surface; interferon-gamma-mediated signaling pathway completely abrogated.|||In IMD27A; fails to bind IFN-gamma.|||In IMD27A; fails to bind IFN-gamma; could be detected on the cell surface; interferon-gamma-mediated signaling pathway completely abrogated.|||In IMD27A; interferon-gamma-mediated signaling pathway completely abrogated.|||In IMD27A; interferon-gamma-mediated signaling pathway severely reduced although not completely abrogated.|||In IMD27A; interferon-gamma-mediated signaling pathway severely reduced.|||In IMD27B.|||In isoform 2.|||Interferon gamma receptor 1|||Interferon gamma receptor D2|||Loss of function in the interferon-gamma-mediated signaling pathway.|||May influence susceptibility to atopic dermatitis complicated by eczema herpeticum; could be detected on the cell surface; no significant effect on interferon-gamma-mediated signaling pathway.|||May influence susceptibility to autoimmune and inflammatory diseases such as systemic lupus erythematosus, atopic asthma and atopic dermatitis complicated by eczema herpeticum; no significant effect on interferon-gamma-mediated signaling pathway.|||N-linked (GlcNAc...) asparagine|||No significant effect on interferon-gamma-mediated signaling pathway.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Strong decreased level of ubiquitination; when associated with R-277 and R-279.|||Strong decreased level of ubiquitination; when associated with R-277 and R-285.|||Strong decreased level of ubiquitination; when associated with R-279 and R-285.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011009|||http://purl.uniprot.org/annotation/PRO_5006608279|||http://purl.uniprot.org/annotation/VAR_017577|||http://purl.uniprot.org/annotation/VAR_017578|||http://purl.uniprot.org/annotation/VAR_017579|||http://purl.uniprot.org/annotation/VAR_019281|||http://purl.uniprot.org/annotation/VAR_019282|||http://purl.uniprot.org/annotation/VAR_019283|||http://purl.uniprot.org/annotation/VAR_080058|||http://purl.uniprot.org/annotation/VAR_080059|||http://purl.uniprot.org/annotation/VAR_080060|||http://purl.uniprot.org/annotation/VAR_080062|||http://purl.uniprot.org/annotation/VAR_080063|||http://purl.uniprot.org/annotation/VAR_080064|||http://purl.uniprot.org/annotation/VAR_080065|||http://purl.uniprot.org/annotation/VAR_080066|||http://purl.uniprot.org/annotation/VAR_080067|||http://purl.uniprot.org/annotation/VAR_080068|||http://purl.uniprot.org/annotation/VAR_080069|||http://purl.uniprot.org/annotation/VAR_080070|||http://purl.uniprot.org/annotation/VAR_080071|||http://purl.uniprot.org/annotation/VAR_080072|||http://purl.uniprot.org/annotation/VAR_080073|||http://purl.uniprot.org/annotation/VAR_080074|||http://purl.uniprot.org/annotation/VAR_080075|||http://purl.uniprot.org/annotation/VAR_080076|||http://purl.uniprot.org/annotation/VSP_055589|||http://purl.uniprot.org/annotation/VSP_055590|||http://purl.uniprot.org/annotation/VSP_055591
http://togogenome.org/gene/9606:SMIM9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGZ8                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Small integral membrane protein 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348247
http://togogenome.org/gene/9606:LY6G5B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7Y3|||http://purl.uniprot.org/uniprot/N0E641|||http://purl.uniprot.org/uniprot/Q8NDX9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Non-terminal Residue|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||Lymphocyte antigen 6 complex locus protein G5b|||N-linked (GlcNAc...) asparagine|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318602|||http://purl.uniprot.org/annotation/PRO_5004106786|||http://purl.uniprot.org/annotation/PRO_5010747595|||http://purl.uniprot.org/annotation/VAR_038842|||http://purl.uniprot.org/annotation/VAR_038843|||http://purl.uniprot.org/annotation/VAR_038844|||http://purl.uniprot.org/annotation/VSP_031255
http://togogenome.org/gene/9606:ZBED3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IU2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Molecule Processing|||Region|||Site|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Region|||Zinc Finger                                                                                  ^@                                                                                  BED-type|||Disordered|||Pro residues|||Zinc finger BED domain-containing protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066562
http://togogenome.org/gene/9606:GPR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1DAM5|||http://purl.uniprot.org/uniprot/P46089                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 3|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069510|||http://purl.uniprot.org/annotation/VAR_011859
http://togogenome.org/gene/9606:SPDEF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95238                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||ETS|||In isoform 2.|||PNT|||Polar residues|||SAM pointed domain-containing Ets transcription factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223958|||http://purl.uniprot.org/annotation/VAR_048955|||http://purl.uniprot.org/annotation/VSP_044722
http://togogenome.org/gene/9606:BLVRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJF4|||http://purl.uniprot.org/uniprot/P53004                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Biliverdin reductase A|||Biliverdin reductase catalytic|||Gfo/Idh/MocA-like oxidoreductase N-terminal|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010852|||http://purl.uniprot.org/annotation/PRO_0000010853|||http://purl.uniprot.org/annotation/VAR_014851|||http://purl.uniprot.org/annotation/VAR_019230|||http://purl.uniprot.org/annotation/VAR_019231
http://togogenome.org/gene/9606:IFI6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A348GSI1|||http://purl.uniprot.org/uniprot/P09912                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||In isoform B.|||In isoform C.|||Interferon alpha-inducible protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008741|||http://purl.uniprot.org/annotation/PRO_5017079522|||http://purl.uniprot.org/annotation/VSP_001502|||http://purl.uniprot.org/annotation/VSP_001503
http://togogenome.org/gene/9606:KRT85                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z7N3|||http://purl.uniprot.org/uniprot/F5GYI5|||http://purl.uniprot.org/uniprot/P78386                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Head|||IF rod|||In ECTD4.|||Keratin, type II cuticular Hb5|||Linker 1|||Linker 12|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063702|||http://purl.uniprot.org/annotation/VAR_029657|||http://purl.uniprot.org/annotation/VAR_049804
http://togogenome.org/gene/9606:KLF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13886                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||Disordered|||Krueppel-like factor 9|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047154
http://togogenome.org/gene/9606:NIF3L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZT8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Mediates interaction with COPS2|||N6-acetyllysine|||NIF3-like protein 1|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147353|||http://purl.uniprot.org/annotation/VAR_037084|||http://purl.uniprot.org/annotation/VSP_029328|||http://purl.uniprot.org/annotation/VSP_043248
http://togogenome.org/gene/9606:ZNF622                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q969S3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Cytoplasmic 60S subunit biogenesis factor ZNF622|||Disordered|||N-acetylalanine|||Phosphoserine|||Removed|||U1-type 1|||U1-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191815
http://togogenome.org/gene/9606:ZNF646                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15015                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17; degenerate|||C2H2-type 18|||C2H2-type 19|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 31|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||In isoform 1.|||Phosphoserine|||Polar residues|||Pro residues|||Zinc finger protein 646                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047699|||http://purl.uniprot.org/annotation/VAR_035594|||http://purl.uniprot.org/annotation/VAR_057430|||http://purl.uniprot.org/annotation/VAR_057431|||http://purl.uniprot.org/annotation/VAR_057432|||http://purl.uniprot.org/annotation/VAR_057433|||http://purl.uniprot.org/annotation/VAR_057434|||http://purl.uniprot.org/annotation/VAR_057435|||http://purl.uniprot.org/annotation/VAR_057436|||http://purl.uniprot.org/annotation/VAR_057437|||http://purl.uniprot.org/annotation/VSP_060189
http://togogenome.org/gene/9606:SLC25A11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02978|||http://purl.uniprot.org/uniprot/Q6IBH0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In PGL6; loss of protein expression.|||In isoform 2.|||Mitochondrial 2-oxoglutarate/malate carrier protein|||N-acetylalanine|||N6-acetyllysine|||N6-succinyllysine|||Phosphoserine|||Phosphotyrosine|||Removed|||Solcar|||Solcar 1|||Solcar 2|||Solcar 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090625|||http://purl.uniprot.org/annotation/VAR_082966|||http://purl.uniprot.org/annotation/VAR_082967|||http://purl.uniprot.org/annotation/VAR_082968|||http://purl.uniprot.org/annotation/VSP_046745
http://togogenome.org/gene/9606:ZNF879                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DU55                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 879                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000393967
http://togogenome.org/gene/9606:RLBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12271                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CRAL-TRIO|||In BRD.|||In RPA.|||In RPA; loss of ability to bind 11-cis-retinaldehyde.|||N-acetylserine|||Removed|||Retinaldehyde-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079330|||http://purl.uniprot.org/annotation/VAR_005140|||http://purl.uniprot.org/annotation/VAR_015172|||http://purl.uniprot.org/annotation/VAR_037317
http://togogenome.org/gene/9606:STKLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NE28                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Protein kinase|||Serine/threonine kinase-like domain-containing protein STKLD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227568|||http://purl.uniprot.org/annotation/VAR_025611|||http://purl.uniprot.org/annotation/VAR_025612|||http://purl.uniprot.org/annotation/VAR_041371|||http://purl.uniprot.org/annotation/VSP_021657|||http://purl.uniprot.org/annotation/VSP_021658|||http://purl.uniprot.org/annotation/VSP_021659|||http://purl.uniprot.org/annotation/VSP_021660
http://togogenome.org/gene/9606:GPR15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R8H6|||http://purl.uniprot.org/uniprot/B6V9G9|||http://purl.uniprot.org/uniprot/P49685                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 15|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069531|||http://purl.uniprot.org/annotation/VAR_020075|||http://purl.uniprot.org/annotation/VAR_049391
http://togogenome.org/gene/9606:CSTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P04080|||http://purl.uniprot.org/uniprot/Q76LA1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Cystatin|||Cystatin-B|||In EPM1.|||N-acetylmethionine|||Reactive site|||Secondary area of contact                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207136|||http://purl.uniprot.org/annotation/VAR_002206
http://togogenome.org/gene/9606:CD244                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BZW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Disrupts interaction with CD48; when associated with A-68.|||Disrupts interaction with CD48; when associated with A-70.|||Extracellular|||Helical|||ITSM 1|||ITSM 2|||ITSM 3|||ITSM 4|||Ig-like 1|||Ig-like 2|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Natural killer cell receptor 2B4|||Phosphotyrosine|||Phosphotyrosine; by FYN|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014668|||http://purl.uniprot.org/annotation/VAR_056036|||http://purl.uniprot.org/annotation/VAR_056037|||http://purl.uniprot.org/annotation/VSP_010397|||http://purl.uniprot.org/annotation/VSP_010398|||http://purl.uniprot.org/annotation/VSP_010399|||http://purl.uniprot.org/annotation/VSP_010400
http://togogenome.org/gene/9606:WBP2NL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICG8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  1|||10|||10 X 7 AA tandem repeat of Y-G-X-P-P-X-G|||2|||3|||4|||5|||6|||7|||8|||9|||Disordered|||GRAM|||PPxY motif|||Polar residues|||Postacrosomal sheath WW domain-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000289127|||http://purl.uniprot.org/annotation/VAR_032578|||http://purl.uniprot.org/annotation/VAR_032579|||http://purl.uniprot.org/annotation/VAR_032580|||http://purl.uniprot.org/annotation/VAR_032581
http://togogenome.org/gene/9606:PTPN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z2F8|||http://purl.uniprot.org/uniprot/P54829|||http://purl.uniprot.org/uniprot/Q86TL3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||Phosphocysteine intermediate|||Phosphoserine; by MAPK|||Phosphoserine; by PKA|||Phosphothreonine; by MAPK|||Pro residues|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000363657|||http://purl.uniprot.org/annotation/VAR_054369|||http://purl.uniprot.org/annotation/VAR_054370|||http://purl.uniprot.org/annotation/VSP_042654|||http://purl.uniprot.org/annotation/VSP_054561
http://togogenome.org/gene/9606:TRIM39-RPP21                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A096LP39|||http://purl.uniprot.org/uniprot/A6ZJ12                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region                                                                                  ^@                                                                                  B box-type|||B30.2/SPRY|||Disordered|||Polar residues|||RING-type                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:ESAM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96AP7                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Endothelial cell-selective adhesion molecule|||Extracellular|||Helical|||Ig-like C2-type|||Ig-like V-type|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014752|||http://purl.uniprot.org/annotation/VAR_049872|||http://purl.uniprot.org/annotation/VSP_055594|||http://purl.uniprot.org/annotation/VSP_055595|||http://purl.uniprot.org/annotation/VSP_055596
http://togogenome.org/gene/9606:SETD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86TU7                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished protein-histidine N-methyltransferase activity.|||Actin-histidine N-methyltransferase|||Decreased binding to actin and decreased protein-histidine N-methyltransferase activity.|||Decreased binding to actin and decreased protein-histidine N-methyltransferase activity. Increased protein-lysine methyltransferase activity toward an actin mutant with a Lys instead of a His target residue. Increased protein-methionine methyltransferase activity toward an actin mutant with a Met instead of a His target residue.|||Decreased ubiquitination and degradation by the SCF(FBXW7) complex.|||Disordered|||Does not affect ubiquitination and degradation by the SCF(FBXW7) complex.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues|||SET|||Shows protein-lysine methyltransferase activity toward an actin mutant with a Lys instead of a His target residue; when associated with A-274.|||Shows protein-lysine methyltransferase activity toward an actin mutant with a Lys instead of a His target residue; when associated with F-256.|||Strongly decreased binding to actin and decreased protein-histidine N-methyltransferase activity.|||Strongly decreased ubiquitination and degradation by the SCF(FBXW7) complex.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254175|||http://purl.uniprot.org/annotation/VAR_028830|||http://purl.uniprot.org/annotation/VSP_021190|||http://purl.uniprot.org/annotation/VSP_021191|||http://purl.uniprot.org/annotation/VSP_021192|||http://purl.uniprot.org/annotation/VSP_021193
http://togogenome.org/gene/9606:CHURC1-FNTB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49356                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Important for selectivity against geranylgeranyl diphosphate|||In isoform 2.|||PFTB 1|||PFTB 2|||PFTB 3|||PFTB 4|||PFTB 5|||Phosphothreonine|||Protein farnesyltransferase subunit beta|||Reduced catalytic efficiency.|||Removes the steric hindrance that normally precludes geranylgeranyl diphosphate binding. Reduces farnesyltransferase activity and confers geranylgeranyltransferase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119761|||http://purl.uniprot.org/annotation/VSP_054657
http://togogenome.org/gene/9606:MYRF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Cytoplasmic|||Decreased affinity for DNA.|||Disordered|||Does not affect autocatalytic cleavage.|||Helical|||In CUGS.|||In CUGS; unknown pathological significance.|||In MMERV.|||In isoform 2.|||Lumenal|||Myelin regulatory factor|||Myelin regulatory factor, C-terminal|||Myelin regulatory factor, N-terminal|||N-linked (GlcNAc...) asparagine|||N6-acetyllysine|||NDT80|||Nuclear localization signal|||Peptidase S74|||Prevents autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part.|||Pro residues|||Reduces autocatalytic cleavage and generation of Myelin regulatory factor, N-terminal part.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318919|||http://purl.uniprot.org/annotation/PRO_0000424310|||http://purl.uniprot.org/annotation/PRO_0000424311|||http://purl.uniprot.org/annotation/VAR_038907|||http://purl.uniprot.org/annotation/VAR_081183|||http://purl.uniprot.org/annotation/VAR_081884|||http://purl.uniprot.org/annotation/VAR_081885|||http://purl.uniprot.org/annotation/VAR_081886|||http://purl.uniprot.org/annotation/VAR_081887|||http://purl.uniprot.org/annotation/VAR_081888|||http://purl.uniprot.org/annotation/VSP_031300|||http://purl.uniprot.org/annotation/VSP_031301|||http://purl.uniprot.org/annotation/VSP_031302
http://togogenome.org/gene/9606:ZBTB17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13105|||http://purl.uniprot.org/uniprot/Q53EM1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  BTB|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2.|||In isoform 3.|||Interaction with HCFC1|||Interaction with MYC|||Phosphoserine|||Zinc finger and BTB domain-containing protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047730|||http://purl.uniprot.org/annotation/VSP_013424|||http://purl.uniprot.org/annotation/VSP_044564
http://togogenome.org/gene/9606:WFDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MTN6|||http://purl.uniprot.org/uniprot/Q14508                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||WAP|||WAP 1|||WAP 2|||WAP four-disulfide core domain protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041370|||http://purl.uniprot.org/annotation/PRO_5035365865|||http://purl.uniprot.org/annotation/VSP_007666|||http://purl.uniprot.org/annotation/VSP_007667|||http://purl.uniprot.org/annotation/VSP_007668|||http://purl.uniprot.org/annotation/VSP_007669|||http://purl.uniprot.org/annotation/VSP_007670|||http://purl.uniprot.org/annotation/VSP_007671|||http://purl.uniprot.org/annotation/VSP_007672
http://togogenome.org/gene/9606:PTMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P06454|||http://purl.uniprot.org/uniprot/Q53S24                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Peptide|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Initiator Methionine|||Modified Residue|||Peptide|||Region|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||N-acetylmethionine|||N-acetylserine; in Prothymosin alpha, N-terminally processed|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Prothymosin alpha|||Prothymosin alpha, N-terminally processed|||Removed; alternate|||Thymosin alpha-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029865|||http://purl.uniprot.org/annotation/PRO_0000299250|||http://purl.uniprot.org/annotation/PRO_0000423255|||http://purl.uniprot.org/annotation/VSP_011508
http://togogenome.org/gene/9606:MFGE8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8Q3SIZ9|||http://purl.uniprot.org/uniprot/B3KTQ2|||http://purl.uniprot.org/uniprot/B4E396|||http://purl.uniprot.org/uniprot/H0YKB5|||http://purl.uniprot.org/uniprot/Q08431                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||EGF-like|||F5/8 type C|||F5/8 type C 1|||F5/8 type C 2|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lactadherin|||Lactadherin short form|||Medin|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; atypical|||Phosphoserine; by FAM20C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007650|||http://purl.uniprot.org/annotation/PRO_0000007651|||http://purl.uniprot.org/annotation/PRO_0000007652|||http://purl.uniprot.org/annotation/PRO_5002801157|||http://purl.uniprot.org/annotation/PRO_5035733413|||http://purl.uniprot.org/annotation/VAR_024263|||http://purl.uniprot.org/annotation/VAR_029794|||http://purl.uniprot.org/annotation/VSP_039108|||http://purl.uniprot.org/annotation/VSP_039953|||http://purl.uniprot.org/annotation/VSP_059818
http://togogenome.org/gene/9606:CHRDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BU40                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Cell attachment site|||Chordin-like protein 1|||Disordered|||In MGC1.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||VWFC 1|||VWFC 2|||VWFC 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005368|||http://purl.uniprot.org/annotation/VAR_068175|||http://purl.uniprot.org/annotation/VSP_060078|||http://purl.uniprot.org/annotation/VSP_060079|||http://purl.uniprot.org/annotation/VSP_060080
http://togogenome.org/gene/9606:ONECUT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95948                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic residues|||CUT|||Disordered|||Homeobox|||One cut domain family member 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000202405
http://togogenome.org/gene/9606:SOHLH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NX45                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315700|||http://purl.uniprot.org/annotation/VAR_038283|||http://purl.uniprot.org/annotation/VAR_038284|||http://purl.uniprot.org/annotation/VSP_030652|||http://purl.uniprot.org/annotation/VSP_030653|||http://purl.uniprot.org/annotation/VSP_042423
http://togogenome.org/gene/9606:PARD6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYG5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Interaction with PARD3 and CDC42|||PB1|||PDZ|||Partitioning defective 6 homolog beta|||Phosphoserine|||Polar residues|||Pseudo-CRIB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000112516|||http://purl.uniprot.org/annotation/VSP_053311|||http://purl.uniprot.org/annotation/VSP_053312
http://togogenome.org/gene/9606:CLRN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCR9                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Clarin-3|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274698|||http://purl.uniprot.org/annotation/VAR_053828|||http://purl.uniprot.org/annotation/VAR_069399|||http://purl.uniprot.org/annotation/VSP_022871|||http://purl.uniprot.org/annotation/VSP_022872
http://togogenome.org/gene/9606:CRYBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P53672                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Beta-crystallin A2|||Beta/gamma crystallin 'Greek key' 1|||Beta/gamma crystallin 'Greek key' 2|||Beta/gamma crystallin 'Greek key' 3|||Beta/gamma crystallin 'Greek key' 4|||Connecting peptide|||In CTRCT42.|||N-terminal arm                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057539|||http://purl.uniprot.org/annotation/VAR_070029|||http://purl.uniprot.org/annotation/VAR_070208
http://togogenome.org/gene/9606:RASAL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YV0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||C2|||Disordered|||In isoform 2.|||PH|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||RAS protein activator like-3|||Ras-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000322566|||http://purl.uniprot.org/annotation/VAR_061179|||http://purl.uniprot.org/annotation/VAR_061180|||http://purl.uniprot.org/annotation/VAR_061181|||http://purl.uniprot.org/annotation/VSP_033824
http://togogenome.org/gene/9606:ATP11A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PEJ6|||http://purl.uniprot.org/uniprot/P98196|||http://purl.uniprot.org/uniprot/Q659C3|||http://purl.uniprot.org/uniprot/Q6PJ25                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cleavage; by CASP3|||Cytoplasmic|||Does not affect flippase activity toward phosphatidylserine. Like the wild type, it is unable to translocate phosphatidylcholine.|||Extracellular|||Has no effect on endoplasmic reticulum to plasma membrane trafficking. Impairs ATPase flippase activity.|||Helical|||Impairs caspase-mediated cleavage; when associated with A-454, A-457 and A-487.|||Impairs caspase-mediated cleavage; when associated with A-454, A-457 and A-490.|||Impairs caspase-mediated cleavage; when associated with A-454, A-487 and A-490.|||Impairs caspase-mediated cleavage; when associated with A-457, A-487 and A-490.|||Impairs endoplasmic reticulum to plasma membrane trafficking.|||In HLD24; results in altered lipid distribution at the cell membrane characterized by decreased phosphatidylcholine and increased sphingomyelin concentrations in the outer leaflet; affects substrate specificity resulting in novel flippase activity toward phosphatidylcholine; does not affect flippase activity toward phosphatidylserine and phosphatidylethanolamine; does not affect location to the cell membrane.|||P-type ATPase C-terminal|||P-type ATPase N-terminal|||Phospholipid-transporting ATPase IH|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046369|||http://purl.uniprot.org/annotation/VAR_048379|||http://purl.uniprot.org/annotation/VAR_059139|||http://purl.uniprot.org/annotation/VAR_087099
http://togogenome.org/gene/9606:KLK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MQY9|||http://purl.uniprot.org/uniprot/O60259                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Charge relay system|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Kallikrein-8|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027946|||http://purl.uniprot.org/annotation/PRO_0000027947|||http://purl.uniprot.org/annotation/VAR_051855|||http://purl.uniprot.org/annotation/VSP_005401|||http://purl.uniprot.org/annotation/VSP_030350|||http://purl.uniprot.org/annotation/VSP_030351|||http://purl.uniprot.org/annotation/VSP_030352
http://togogenome.org/gene/9606:MYO1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B0I1S9|||http://purl.uniprot.org/uniprot/E9PDF6|||http://purl.uniprot.org/uniprot/O43795                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||IQ 1|||IQ 2|||IQ 3|||IQ 4|||IQ 5|||IQ 6|||In a colorectal cancer sample; somatic mutation.|||In a melanoma patient.|||In isoform 2.|||Myosin motor|||Phosphoserine|||TH1|||Unconventional myosin-Ib                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123442|||http://purl.uniprot.org/annotation/VAR_014113|||http://purl.uniprot.org/annotation/VAR_036007|||http://purl.uniprot.org/annotation/VAR_036008|||http://purl.uniprot.org/annotation/VSP_012759
http://togogenome.org/gene/9606:TCEAL7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRU2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Transcription elongation factor A protein-like 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239214
http://togogenome.org/gene/9606:EIPR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MUM1|||http://purl.uniprot.org/uniprot/Q53HC9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EARP and GARP complex-interacting protein 1|||N-acetylmethionine|||Phosphoserine|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051298
http://togogenome.org/gene/9606:MAP3K10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02779                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||In a metastatic melanoma sample; somatic mutation.|||Leucine-zipper 1|||Leucine-zipper 2|||Mitogen-activated protein kinase kinase kinase 10|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by autocatalysis and MAP4K1|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Polar residues|||Pro residues|||Protein kinase|||Proton acceptor|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086259|||http://purl.uniprot.org/annotation/VAR_040702|||http://purl.uniprot.org/annotation/VAR_051639
http://togogenome.org/gene/9606:RGPD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3J3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||GRIP|||In isoform 2.|||Phosphoserine|||Polar residues|||RanBD1 1|||RanBD1 2|||RanBP2-like and GRIP domain-containing protein 4|||TPR 1|||TPR 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314141|||http://purl.uniprot.org/annotation/VSP_030214|||http://purl.uniprot.org/annotation/VSP_030215
http://togogenome.org/gene/9606:GNAZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19086|||http://purl.uniprot.org/uniprot/Q8IY73                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||Disordered|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein G(z) subunit alpha|||N-myristoyl glycine|||Removed|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203696
http://togogenome.org/gene/9606:SCRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12765                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-acetylalanine|||Removed|||Secernin-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221436|||http://purl.uniprot.org/annotation/VAR_029512|||http://purl.uniprot.org/annotation/VAR_057709|||http://purl.uniprot.org/annotation/VSP_044453|||http://purl.uniprot.org/annotation/VSP_044454
http://togogenome.org/gene/9606:PAK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5M4|||http://purl.uniprot.org/uniprot/Q13177                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes kinase activity and autophosphorylation.|||Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34.|||Abolishes myristoylation of PAK-2p34 and membrane location.|||Abolishes nuclear export.|||Autoregulatory region|||Basic and acidic residues|||CRIB|||Cleavage; by caspase-3 or caspase-3-like proteases|||Disordered|||GTPase-binding|||Greatly inhibits nuclear localization.|||In KNO2; loss of protein serine/threonine kinase activity.|||Inhibits caspase-mediated cleavage.|||N-acetylserine|||N-myristoyl glycine; in form PAK-2p34|||N6-acetyllysine|||Nuclear localization signal|||PAK-2p27|||PAK-2p34|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by autocatalysis|||Phosphotyrosine|||Protein kinase|||Proton acceptor|||Removed|||Serine/threonine-protein kinase PAK 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086465|||http://purl.uniprot.org/annotation/PRO_0000304922|||http://purl.uniprot.org/annotation/PRO_0000304923|||http://purl.uniprot.org/annotation/VAR_087512
http://togogenome.org/gene/9606:ZMYND10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75800                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  In CILD22.|||In CILD22; loss of interaction with DNAAF11.|||In CILD22; loss of interaction with DNAL1.|||In CILD22; no loss of interaction with DNAAF11.|||In isoform 2.|||In non-small cell lung cancer cell lines.|||Interaction with DNAAF11|||MYND-type|||Zinc finger MYND domain-containing protein 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218314|||http://purl.uniprot.org/annotation/VAR_014227|||http://purl.uniprot.org/annotation/VAR_070184|||http://purl.uniprot.org/annotation/VAR_070185|||http://purl.uniprot.org/annotation/VAR_070186|||http://purl.uniprot.org/annotation/VAR_070187|||http://purl.uniprot.org/annotation/VAR_070188|||http://purl.uniprot.org/annotation/VAR_070189|||http://purl.uniprot.org/annotation/VAR_080482|||http://purl.uniprot.org/annotation/VAR_080483|||http://purl.uniprot.org/annotation/VSP_003328
http://togogenome.org/gene/9606:CRLS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJA2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Cardiolipin synthase (CMP-forming)|||Disordered|||Helical|||In COXPD57; decreased function in cardiolipin synthesis; reduced cardiolipin and increased phosphatidylglycerol levels in fibroblasts from a homozygous patient.|||In COXPD57; unknown pathological significance.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056816|||http://purl.uniprot.org/annotation/VAR_087984|||http://purl.uniprot.org/annotation/VAR_087985|||http://purl.uniprot.org/annotation/VAR_087986|||http://purl.uniprot.org/annotation/VSP_041398|||http://purl.uniprot.org/annotation/VSP_041399
http://togogenome.org/gene/9606:TWNK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2R8Y4V4|||http://purl.uniprot.org/uniprot/A0A2R8Y746|||http://purl.uniprot.org/uniprot/E5KSY5|||http://purl.uniprot.org/uniprot/Q96RR1|||http://purl.uniprot.org/uniprot/Q9H6V3                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Contributes to single strand DNA binding activity|||Disordered|||In MTDPS7.|||In MTDPS7; affects helicase activity.|||In MTDPS7; infantile spinocerebellar ataxia phenotype.|||In MTDPS7; patients manifest multi-organ failure; requires 2 nucleotide substitutions.|||In PEO; sporadic case; the patient also carries the S-848 mutation in the POLG gene suggesting digenic inheritance; retains hexamer and heptamer formation.|||In PEOA3.|||In PEOA3; also detected in a case showing digenic inheritance.|||In PEOA3; displays unusual oligomeric forms.|||In PEOA3; reduced single-strand DNA binding; increased heptamer oligomerization.|||In PEOA3; reduces closed-ring quaternary structure formation.|||In PEOA3; reduces helicase activity and alters nucleoid structure.|||In PEOA3; reduces helicase activity.|||In PEOA3; reduces helicase activity; increases single strand DNA affinity; reduces closed-ring quaternary structure formation.|||In PEOA3; reduces helicase activity; reduced single-strand DNA binding.|||In PEOA3; the phenotype highly overlaps with sensory ataxic neuropathy dysarthria and ophthalmoparesis; reduces helicase activity and single-strand DNA binding.|||In PRLTS5.|||In isoform 2.|||In isoform 3.|||Loss of helicase activity on 5'-tailed substrate.|||Maybe required for stable oligomeric structure|||Might negatively regulate ATPase activity|||Mitochondrion|||Polar residues|||Required for hexamers formation and DNA helicase activity|||SF4 helicase|||Twinkle mtDNA helicase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000042640|||http://purl.uniprot.org/annotation/VAR_023647|||http://purl.uniprot.org/annotation/VAR_023648|||http://purl.uniprot.org/annotation/VAR_023649|||http://purl.uniprot.org/annotation/VAR_023650|||http://purl.uniprot.org/annotation/VAR_023651|||http://purl.uniprot.org/annotation/VAR_023652|||http://purl.uniprot.org/annotation/VAR_023653|||http://purl.uniprot.org/annotation/VAR_023654|||http://purl.uniprot.org/annotation/VAR_023655|||http://purl.uniprot.org/annotation/VAR_023656|||http://purl.uniprot.org/annotation/VAR_023657|||http://purl.uniprot.org/annotation/VAR_023658|||http://purl.uniprot.org/annotation/VAR_023659|||http://purl.uniprot.org/annotation/VAR_023660|||http://purl.uniprot.org/annotation/VAR_023661|||http://purl.uniprot.org/annotation/VAR_023662|||http://purl.uniprot.org/annotation/VAR_039045|||http://purl.uniprot.org/annotation/VAR_043797|||http://purl.uniprot.org/annotation/VAR_051267|||http://purl.uniprot.org/annotation/VAR_062268|||http://purl.uniprot.org/annotation/VAR_062269|||http://purl.uniprot.org/annotation/VAR_065102|||http://purl.uniprot.org/annotation/VAR_065103|||http://purl.uniprot.org/annotation/VAR_065104|||http://purl.uniprot.org/annotation/VAR_065105|||http://purl.uniprot.org/annotation/VAR_065106|||http://purl.uniprot.org/annotation/VAR_065107|||http://purl.uniprot.org/annotation/VAR_065108|||http://purl.uniprot.org/annotation/VAR_065109|||http://purl.uniprot.org/annotation/VAR_065110|||http://purl.uniprot.org/annotation/VAR_065111|||http://purl.uniprot.org/annotation/VAR_065112|||http://purl.uniprot.org/annotation/VAR_065113|||http://purl.uniprot.org/annotation/VAR_065114|||http://purl.uniprot.org/annotation/VAR_065115|||http://purl.uniprot.org/annotation/VAR_065116|||http://purl.uniprot.org/annotation/VAR_065117|||http://purl.uniprot.org/annotation/VAR_065118|||http://purl.uniprot.org/annotation/VAR_067722|||http://purl.uniprot.org/annotation/VAR_072657|||http://purl.uniprot.org/annotation/VAR_072658|||http://purl.uniprot.org/annotation/VAR_072659|||http://purl.uniprot.org/annotation/VAR_072660|||http://purl.uniprot.org/annotation/VSP_015959|||http://purl.uniprot.org/annotation/VSP_015960|||http://purl.uniprot.org/annotation/VSP_015961
http://togogenome.org/gene/9606:CAD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8VPD4|||http://purl.uniprot.org/uniprot/P27708                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  11.5% of wild-type catalytic activity.|||3% of wild-type catalytic activity.|||ATCase (Aspartate transcarbamylase)|||ATP-grasp|||ATP-grasp 1|||ATP-grasp 2|||Abolishes PMA-induced Thr-456 phosphorylation.|||Abolishes dihydroorotase activity.|||Basic and acidic residues|||CAD protein|||CPSase (Carbamoyl-phosphate synthase)|||CPSase A|||CPSase B|||DHOase (dihydroorotase)|||Disordered|||For GATase activity|||GATase (Glutamine amidotransferase)|||Glutamine amidotransferase type-1|||In DEE50.|||In DEE50; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||Linker|||MGS-like|||N-acetylalanine|||N6-acetyllysine|||N6-carboxylysine|||No catalytic activity.|||No change in catalytic activity.|||No zinc-binding and no catalytic activity.|||Nucleophile|||Nucleophile; for GATase activity|||Phosphoserine|||Phosphoserine; by PKA|||Phosphoserine; by PKC; in vitro|||Phosphoserine; by RPS6KB1 and PKA|||Phosphothreonine|||Phosphothreonine; by MAPK1|||Reduces dihydroorotase activity.|||Removed|||via carbamate group                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000199506|||http://purl.uniprot.org/annotation/VAR_035897|||http://purl.uniprot.org/annotation/VAR_035898|||http://purl.uniprot.org/annotation/VAR_073955|||http://purl.uniprot.org/annotation/VAR_078289|||http://purl.uniprot.org/annotation/VAR_078290
http://togogenome.org/gene/9606:DIS3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1J5|||http://purl.uniprot.org/uniprot/Q9Y2L1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Exosome complex exonuclease RRP44|||In isoform 2.|||Loss of endonuclease activity; when associated with N-487.|||Loss of exonuclease activity. Loss of endonuclease activity; when associated with N-146.|||N-acetylmethionine|||N6-acetyllysine|||PINc|||Phosphoserine|||Ribonuclease II/R                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000166419|||http://purl.uniprot.org/annotation/VAR_023099|||http://purl.uniprot.org/annotation/VAR_023100|||http://purl.uniprot.org/annotation/VSP_014971
http://togogenome.org/gene/9606:BHMT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93088|||http://purl.uniprot.org/uniprot/V9HWA4                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Betaine--homocysteine S-methyltransferase 1|||Decreases the catalytic efficiency.|||Has no significant effect on catalytic activity.|||Hcy-binding|||Impairs zinc ion binding. Loss of catalytic activity.|||May decrease risk for coronary artery disease.|||N6-succinyllysine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114621|||http://purl.uniprot.org/annotation/VAR_015886|||http://purl.uniprot.org/annotation/VAR_061345
http://togogenome.org/gene/9606:NFE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3E0|||http://purl.uniprot.org/uniprot/Q16621                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict                                                                                  ^@                                                                                  60% loss of DNA-binding and 5-fold loss of transactivation activity. Almost no colocalization with nuclear bodies.|||BZIP|||Basic motif|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Leucine-zipper|||PXY motif 1|||PXY motif 2|||Phosphoserine; by MAPK8|||Phosphoserine; by PKA|||Required for interaction with MAPK8|||Transactivation domain|||Transcription factor NF-E2 45 kDa subunit|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076446
http://togogenome.org/gene/9606:HSH2D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JZ2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Hematopoietic SH2 domain-containing protein|||In isoform 2.|||Loss of the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation.|||No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation.|||Polar residues|||SH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000233129|||http://purl.uniprot.org/annotation/VSP_018052
http://togogenome.org/gene/9606:DPEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI3|||http://purl.uniprot.org/uniprot/P16444                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Abolished dipeptidase activity. Does not affect ability to bind neutrophils.|||Complete loss of activity.|||Dipeptidase|||Dipeptidase 1|||GPI-anchor amidated serine|||In a colorectal cancer sample; somatic mutation.|||Interchain|||Loss of ability to hydrolyze cystinyl-bis-glycine.|||Loss of zinc binding.|||N-linked (GlcNAc...) asparagine|||Partial loss of activity.|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018652|||http://purl.uniprot.org/annotation/PRO_0000018653|||http://purl.uniprot.org/annotation/PRO_5007356949|||http://purl.uniprot.org/annotation/VAR_036496|||http://purl.uniprot.org/annotation/VAR_061375|||http://purl.uniprot.org/annotation/VAR_061376
http://togogenome.org/gene/9606:FMO2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99518                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Flavin-containing monooxygenase 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Helical|||In allele FMO2*2A; loss of monooxygenase activity.|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000147646|||http://purl.uniprot.org/annotation/VAR_014840|||http://purl.uniprot.org/annotation/VAR_014841|||http://purl.uniprot.org/annotation/VAR_014842|||http://purl.uniprot.org/annotation/VAR_014843|||http://purl.uniprot.org/annotation/VAR_014844|||http://purl.uniprot.org/annotation/VAR_015361|||http://purl.uniprot.org/annotation/VAR_015362|||http://purl.uniprot.org/annotation/VAR_015363|||http://purl.uniprot.org/annotation/VAR_022185|||http://purl.uniprot.org/annotation/VAR_022186|||http://purl.uniprot.org/annotation/VAR_081836
http://togogenome.org/gene/9606:MRPL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYD3                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Large ribosomal subunit protein uL4m|||Omega-N-methylarginine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238949|||http://purl.uniprot.org/annotation/VSP_019027|||http://purl.uniprot.org/annotation/VSP_019028
http://togogenome.org/gene/9606:TMBIM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G3V1M2|||http://purl.uniprot.org/uniprot/G3XAA5|||http://purl.uniprot.org/uniprot/Q9HC19|||http://purl.uniprot.org/uniprot/Q9HC24                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Protein lifeguard 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000179092|||http://purl.uniprot.org/annotation/VAR_014946|||http://purl.uniprot.org/annotation/VAR_055547
http://togogenome.org/gene/9606:TRPM5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZQ8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Transient receptor potential cation channel subfamily M member 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328933|||http://purl.uniprot.org/annotation/VAR_042578|||http://purl.uniprot.org/annotation/VAR_052377|||http://purl.uniprot.org/annotation/VAR_052378|||http://purl.uniprot.org/annotation/VAR_052379|||http://purl.uniprot.org/annotation/VAR_059836|||http://purl.uniprot.org/annotation/VSP_052741|||http://purl.uniprot.org/annotation/VSP_052742|||http://purl.uniprot.org/annotation/VSP_052743
http://togogenome.org/gene/9606:PABPC1L2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQF8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Disordered|||Polyadenylate-binding protein 1-like 2|||RRM 1|||RRM 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304509
http://togogenome.org/gene/9606:EIF2B2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49770                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Found in a patient with Rett syndrome-like phenotype; unknown pathological significance.|||In VWM2.|||In VWM2; with and without ovarian failure.|||In VWM2; with ovarian failure.|||Translation initiation factor eIF-2B subunit beta                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156061|||http://purl.uniprot.org/annotation/VAR_012289|||http://purl.uniprot.org/annotation/VAR_012290|||http://purl.uniprot.org/annotation/VAR_012321|||http://purl.uniprot.org/annotation/VAR_012322|||http://purl.uniprot.org/annotation/VAR_016842|||http://purl.uniprot.org/annotation/VAR_068451|||http://purl.uniprot.org/annotation/VAR_068452|||http://purl.uniprot.org/annotation/VAR_068453|||http://purl.uniprot.org/annotation/VAR_068454|||http://purl.uniprot.org/annotation/VAR_079034
http://togogenome.org/gene/9606:WTIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NIX2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Pro residues|||Wilms tumor protein 1-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328860
http://togogenome.org/gene/9606:OR52W1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IF63                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52W1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150792|||http://purl.uniprot.org/annotation/VAR_044514|||http://purl.uniprot.org/annotation/VAR_044515|||http://purl.uniprot.org/annotation/VAR_044516
http://togogenome.org/gene/9606:CCPG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULG6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cell cycle progression protein 1|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Interaction with MCF2L and SRC|||Lumenal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310538|||http://purl.uniprot.org/annotation/VAR_037063|||http://purl.uniprot.org/annotation/VAR_037064|||http://purl.uniprot.org/annotation/VAR_037065|||http://purl.uniprot.org/annotation/VAR_037066|||http://purl.uniprot.org/annotation/VAR_037067|||http://purl.uniprot.org/annotation/VAR_037068|||http://purl.uniprot.org/annotation/VAR_037069|||http://purl.uniprot.org/annotation/VAR_037070|||http://purl.uniprot.org/annotation/VAR_037071|||http://purl.uniprot.org/annotation/VAR_037072|||http://purl.uniprot.org/annotation/VAR_037073|||http://purl.uniprot.org/annotation/VAR_037074|||http://purl.uniprot.org/annotation/VSP_029311|||http://purl.uniprot.org/annotation/VSP_029312|||http://purl.uniprot.org/annotation/VSP_029313|||http://purl.uniprot.org/annotation/VSP_029314|||http://purl.uniprot.org/annotation/VSP_029315|||http://purl.uniprot.org/annotation/VSP_029316
http://togogenome.org/gene/9606:GTF2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13984                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  General transcription factor IIF subunit 2|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211235
http://togogenome.org/gene/9606:SRD5A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P31213                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  3-oxo-5-alpha-steroid 4-dehydrogenase 2|||Found in individual with micropenis.|||Found in individual with micropenis; unknown pathological significance.|||Helical|||In PPSH.|||In PPSH; also found in individuals with micropenis; increased affinity for testosterone; increased affinity for NADPH; decreased Vmax.|||Increased affinity for testosterone; increased affinity for NADPH; decreased Vmax.|||Increased affinity for testosterone; no effect on affinity for NADPH; increased Vmax.|||No effect on affinity for testosterone; increased affinity for NADPH; decreased Vmax.|||No effect on affinity for testosterone; increased affinity for NADPH; increased Vmax.|||No effect on affinity for testosterone; no effect on affinity for NADPH; increased Vmax.|||No effect on affinity for testosterone; no effect on affinity for NADPH; no effect on Vmax.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213676|||http://purl.uniprot.org/annotation/VAR_005609|||http://purl.uniprot.org/annotation/VAR_013104|||http://purl.uniprot.org/annotation/VAR_013105|||http://purl.uniprot.org/annotation/VAR_013106|||http://purl.uniprot.org/annotation/VAR_013107|||http://purl.uniprot.org/annotation/VAR_013108|||http://purl.uniprot.org/annotation/VAR_013109|||http://purl.uniprot.org/annotation/VAR_013110|||http://purl.uniprot.org/annotation/VAR_013111|||http://purl.uniprot.org/annotation/VAR_013112|||http://purl.uniprot.org/annotation/VAR_013113|||http://purl.uniprot.org/annotation/VAR_013130|||http://purl.uniprot.org/annotation/VAR_013131|||http://purl.uniprot.org/annotation/VAR_013132|||http://purl.uniprot.org/annotation/VAR_013133|||http://purl.uniprot.org/annotation/VAR_013134|||http://purl.uniprot.org/annotation/VAR_022302|||http://purl.uniprot.org/annotation/VAR_025851|||http://purl.uniprot.org/annotation/VAR_025852|||http://purl.uniprot.org/annotation/VAR_025853|||http://purl.uniprot.org/annotation/VAR_025854|||http://purl.uniprot.org/annotation/VAR_025855|||http://purl.uniprot.org/annotation/VAR_025856|||http://purl.uniprot.org/annotation/VAR_025857|||http://purl.uniprot.org/annotation/VAR_037585|||http://purl.uniprot.org/annotation/VAR_037586|||http://purl.uniprot.org/annotation/VAR_059791|||http://purl.uniprot.org/annotation/VAR_059792|||http://purl.uniprot.org/annotation/VAR_077546|||http://purl.uniprot.org/annotation/VAR_077547|||http://purl.uniprot.org/annotation/VAR_077548|||http://purl.uniprot.org/annotation/VAR_077549|||http://purl.uniprot.org/annotation/VAR_077550|||http://purl.uniprot.org/annotation/VAR_077551|||http://purl.uniprot.org/annotation/VAR_077552|||http://purl.uniprot.org/annotation/VAR_087980|||http://purl.uniprot.org/annotation/VAR_087981
http://togogenome.org/gene/9606:TXNDC8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A9Z1W9|||http://purl.uniprot.org/uniprot/B7ZME0|||http://purl.uniprot.org/uniprot/Q6A555                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Redox-active|||Thioredoxin|||Thioredoxin domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120162|||http://purl.uniprot.org/annotation/VAR_057353|||http://purl.uniprot.org/annotation/VSP_014333
http://togogenome.org/gene/9606:CNST                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Consortin|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288906|||http://purl.uniprot.org/annotation/VAR_032530|||http://purl.uniprot.org/annotation/VAR_032531|||http://purl.uniprot.org/annotation/VAR_032532|||http://purl.uniprot.org/annotation/VAR_056762|||http://purl.uniprot.org/annotation/VSP_025817|||http://purl.uniprot.org/annotation/VSP_025818|||http://purl.uniprot.org/annotation/VSP_025819|||http://purl.uniprot.org/annotation/VSP_025820
http://togogenome.org/gene/9606:LGALS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MR27|||http://purl.uniprot.org/uniprot/P09382                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Strand                                                                                  ^@                                                                                  Galectin|||Galectin-1|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate|||Phosphoserine; by FAM20C|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076917
http://togogenome.org/gene/9606:FNIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNG8|||http://purl.uniprot.org/uniprot/Q8TF40                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cys degron|||Disordered|||Folliculin-interacting protein 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired phosphorylation by CK2 and interaction with HSP90AA1/Hsp90.|||Impaired ubiquitination, leading to increased stability.|||In IMD93; undetectable protein in homozygous patient cells.|||In IMD93; unknown pathological significance.|||In SA5 mutant; Abolishes phosphorylation by AMPK, leading to activation of the non-canonical mTORC1 signaling; when associated with 230-A--A-232, A-261 and A-593.|||In SA5 mutant; Abolishes phosphorylation by AMPK, leading to activation of the non-canonical mTORC1 signaling; when associated with A-220, 230-A--A-232 and A-261.|||In SA5 mutant; Abolishes phosphorylation by AMPK, leading to activation of the non-canonical mTORC1 signaling; when associated with A-220, 230-A--A-232 and A-593.|||In SA5 mutant; Abolishes phosphorylation by AMPK, leading to activation of the non-canonical mTORC1 signaling; when associated with A-220, A-261 and A-593.|||In isoform 2.|||In isoform 3.|||Interaction with HSP90AA1|||KY-finger|||Mimics phosphorylation status; leading to inhibit ATPase activity of HSP90AA1/Hsp90.|||No effect on ubiquitination and protein stability.|||O-linked (GlcNAc) serine; alternate|||Phosphoserine|||Phosphoserine; alternate; by CK2|||Phosphoserine; by AMPK|||Phosphoserine; by CK2|||Phosphothreonine|||UDENN FNIP1/2-type|||cDENN FNIP1/2-type|||dDENN FNIP1/2-type|||uDENN FNIP1/2-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308484|||http://purl.uniprot.org/annotation/VAR_036824|||http://purl.uniprot.org/annotation/VAR_036825|||http://purl.uniprot.org/annotation/VAR_036826|||http://purl.uniprot.org/annotation/VAR_036827|||http://purl.uniprot.org/annotation/VAR_036828|||http://purl.uniprot.org/annotation/VAR_086807|||http://purl.uniprot.org/annotation/VAR_086808|||http://purl.uniprot.org/annotation/VSP_028982|||http://purl.uniprot.org/annotation/VSP_028983|||http://purl.uniprot.org/annotation/VSP_028984
http://togogenome.org/gene/9606:OR6N2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GV57|||http://purl.uniprot.org/uniprot/Q8NGY6                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 6N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150634|||http://purl.uniprot.org/annotation/VAR_053224|||http://purl.uniprot.org/annotation/VAR_062054
http://togogenome.org/gene/9606:COL21A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A158RFW1|||http://purl.uniprot.org/uniprot/B3KU30|||http://purl.uniprot.org/uniprot/B7ZLK3|||http://purl.uniprot.org/uniprot/Q96P44                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Collagen alpha-1(XXI) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Collagen-like 5|||Collagen-like 6|||Collagen-like 7|||Disordered|||In isoform 2.|||In isoform 3.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Pro residues|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317613|||http://purl.uniprot.org/annotation/PRO_5002867175|||http://purl.uniprot.org/annotation/PRO_5007631735|||http://purl.uniprot.org/annotation/VAR_038555|||http://purl.uniprot.org/annotation/VAR_038556|||http://purl.uniprot.org/annotation/VAR_038557|||http://purl.uniprot.org/annotation/VAR_038558|||http://purl.uniprot.org/annotation/VAR_038559|||http://purl.uniprot.org/annotation/VAR_038560|||http://purl.uniprot.org/annotation/VAR_038561|||http://purl.uniprot.org/annotation/VSP_031083|||http://purl.uniprot.org/annotation/VSP_031084|||http://purl.uniprot.org/annotation/VSP_031085|||http://purl.uniprot.org/annotation/VSP_031086
http://togogenome.org/gene/9606:NFKB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00653                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||Basic and acidic residues|||Breakpoint for translocation to form NFKB2-IGHA1 oncogene|||Cleavage (when cotranslationally processed)|||Death|||Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865.|||Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869.|||Disordered|||GRR|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In CVID10; unknown pathological significance; de novo mutation.|||In isoform 3.|||In isoform 4.|||In truncated form EB308.|||In truncated form LB40.|||In truncated form p80HT.|||Loss of phosphorylation; when associated with A-715 and A-717.|||Loss of phosphorylation; when associated with G-713 and A-715.|||Loss of phosphorylation; when associated with G-713 and A-717.|||No change in cleavage rate or products.|||Nuclear factor NF-kappa-B p100 subunit|||Nuclear factor NF-kappa-B p52 subunit|||Nuclear localization signal|||Phosphoserine|||Phosphoserine; by MAP3K14|||Phosphothreonine|||RHD|||Two-fold reduction in heterodimerization with RelA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030321|||http://purl.uniprot.org/annotation/PRO_0000030322|||http://purl.uniprot.org/annotation/VAR_006909|||http://purl.uniprot.org/annotation/VAR_006910|||http://purl.uniprot.org/annotation/VAR_018452|||http://purl.uniprot.org/annotation/VAR_018453|||http://purl.uniprot.org/annotation/VAR_022223|||http://purl.uniprot.org/annotation/VAR_022224|||http://purl.uniprot.org/annotation/VAR_022225|||http://purl.uniprot.org/annotation/VAR_051781|||http://purl.uniprot.org/annotation/VAR_074035|||http://purl.uniprot.org/annotation/VAR_074036|||http://purl.uniprot.org/annotation/VSP_040082|||http://purl.uniprot.org/annotation/VSP_040083|||http://purl.uniprot.org/annotation/VSP_040084
http://togogenome.org/gene/9606:THAP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WY91                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HCFC1-binding motif (HBM)|||In isoform 2.|||Nitrobindin|||Peroxynitrite isomerase THAP4|||Phosphoserine|||Polar residues|||THAP-type|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068646|||http://purl.uniprot.org/annotation/VAR_027161|||http://purl.uniprot.org/annotation/VSP_020078|||http://purl.uniprot.org/annotation/VSP_020079
http://togogenome.org/gene/9606:IL7R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16871                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Fibronectin type-III|||Helical|||In IMD104.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-7 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||Phosphothreonine; by PKC|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010909|||http://purl.uniprot.org/annotation/VAR_021286|||http://purl.uniprot.org/annotation/VAR_021287|||http://purl.uniprot.org/annotation/VAR_021288|||http://purl.uniprot.org/annotation/VAR_021289|||http://purl.uniprot.org/annotation/VAR_021290|||http://purl.uniprot.org/annotation/VAR_034870|||http://purl.uniprot.org/annotation/VAR_047742|||http://purl.uniprot.org/annotation/VSP_001713|||http://purl.uniprot.org/annotation/VSP_001714|||http://purl.uniprot.org/annotation/VSP_012618|||http://purl.uniprot.org/annotation/VSP_012619
http://togogenome.org/gene/9606:METTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3J2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolished methyltransferase activity.|||Found in a renal cell carcinoma sample; somatic mutation.|||N(6)-adenine-specific methyltransferase METTL4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251225|||http://purl.uniprot.org/annotation/VAR_027670|||http://purl.uniprot.org/annotation/VAR_027671|||http://purl.uniprot.org/annotation/VAR_027672|||http://purl.uniprot.org/annotation/VAR_056159|||http://purl.uniprot.org/annotation/VAR_064731
http://togogenome.org/gene/9606:TCTN3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804G9W2|||http://purl.uniprot.org/uniprot/Q6NUS6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with Joubert syndrome also carrying 2 mutations in MKS1 gene, a deletion in intron 15 and a missense mutation 'C-80'; unknown pathological significance.|||Helical|||In JBTS18.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Tectonic|||Tectonic-3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000229921|||http://purl.uniprot.org/annotation/VAR_068823|||http://purl.uniprot.org/annotation/VAR_077521|||http://purl.uniprot.org/annotation/VSP_017791|||http://purl.uniprot.org/annotation/VSP_017792|||http://purl.uniprot.org/annotation/VSP_017793|||http://purl.uniprot.org/annotation/VSP_017794|||http://purl.uniprot.org/annotation/VSP_017795|||http://purl.uniprot.org/annotation/VSP_017796|||http://purl.uniprot.org/annotation/VSP_043266|||http://purl.uniprot.org/annotation/VSP_043267
http://togogenome.org/gene/9606:RGMA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTQ4|||http://purl.uniprot.org/uniprot/Q96B86                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cleavage; by autolysis|||Disordered|||GPI-anchor amidated alanine|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Removed in mature form|||Repulsive guidance molecule A|||Repulsive guidance molecule C-terminal|||Repulsive guidance molecule N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030385|||http://purl.uniprot.org/annotation/PRO_0000030386|||http://purl.uniprot.org/annotation/PRO_0000030387|||http://purl.uniprot.org/annotation/VAR_060105|||http://purl.uniprot.org/annotation/VAR_062144|||http://purl.uniprot.org/annotation/VSP_054070|||http://purl.uniprot.org/annotation/VSP_054071
http://togogenome.org/gene/9606:CLCA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14CN2                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Calcium-activated chloride channel regulator 4|||Calcium-activated chloride channel regulator 4, 110 kDa form|||Calcium-activated chloride channel regulator 4, 30 kDa form|||Cleavage; by autolysis|||Disordered|||Helical|||In isoform 2.|||Metalloprotease domain|||N-linked (GlcNAc...) asparagine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000345389|||http://purl.uniprot.org/annotation/PRO_0000345390|||http://purl.uniprot.org/annotation/PRO_0000345391|||http://purl.uniprot.org/annotation/VAR_045816|||http://purl.uniprot.org/annotation/VAR_045817|||http://purl.uniprot.org/annotation/VAR_045818|||http://purl.uniprot.org/annotation/VAR_045819|||http://purl.uniprot.org/annotation/VAR_045820|||http://purl.uniprot.org/annotation/VSP_056117|||http://purl.uniprot.org/annotation/VSP_056118|||http://purl.uniprot.org/annotation/VSP_056119
http://togogenome.org/gene/9606:ADORA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29275                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Lipid Binding|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Adenosine receptor A2b|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069003
http://togogenome.org/gene/9606:EIF4EBP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60516                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Motif|||Mutagenesis Site|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Eukaryotic translation initiation factor 4E-binding protein 3|||Loss of interaction with EIF4E.|||TOS motif|||YXXXXLphi motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190518
http://togogenome.org/gene/9606:ZNF521                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KTI4|||http://purl.uniprot.org/uniprot/Q8IYZ2|||http://purl.uniprot.org/uniprot/Q96K83                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form PAX5-ZNF521|||C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13; atypical|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 18|||C2H2-type 19|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 20|||C2H2-type 21; degenerate|||C2H2-type 22|||C2H2-type 23|||C2H2-type 24|||C2H2-type 25; degenerate|||C2H2-type 26|||C2H2-type 27|||C2H2-type 28|||C2H2-type 29|||C2H2-type 3|||C2H2-type 30|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Phosphoserine|||Polar residues|||Zinc finger protein 521                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000306871
http://togogenome.org/gene/9606:IHH                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14623                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Cholesterol glycine ester|||Cleavage; by autolysis|||Essential for auto-cleavage|||In ACFD.|||In BDA1; decreases the stability of the indian hedgehog protein N-product.|||In BDA1; no effect on the stability of the indian hedgehog protein N-product.|||Increases the lysosomal degradation of the indian hedgehog protein N-product.|||Indian hedgehog protein|||Indian hedgehog protein N-product|||Involved in auto-cleavage|||Involved in cholesterol transfer|||N-linked (GlcNAc...) asparagine|||N-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013229|||http://purl.uniprot.org/annotation/PRO_0000013230|||http://purl.uniprot.org/annotation/VAR_015981|||http://purl.uniprot.org/annotation/VAR_015982|||http://purl.uniprot.org/annotation/VAR_015983|||http://purl.uniprot.org/annotation/VAR_015984|||http://purl.uniprot.org/annotation/VAR_015985|||http://purl.uniprot.org/annotation/VAR_015986
http://togogenome.org/gene/9606:CNIH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBE1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122228
http://togogenome.org/gene/9606:MTREX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42285|||http://purl.uniprot.org/uniprot/Q3MHC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes RNA helicase activity.|||Basic and acidic residues|||DEIH box|||Decreased interaction with NRDE2.|||Decreased interaction with NRDE2. Impairs the binding of both NVL and NOP53.|||Disordered|||Exosome RNA helicase MTR4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helicase ATP-binding|||Helicase C-terminal|||Loss of interaction with NRDE2.|||N-acetylalanine|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000102094|||http://purl.uniprot.org/annotation/VAR_049343
http://togogenome.org/gene/9606:PARP15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7ZL48|||http://purl.uniprot.org/uniprot/C9J7L3|||http://purl.uniprot.org/uniprot/Q460N3                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes catalytic activity.|||Disordered|||In isoform 2.|||Macro|||Macro 1|||Macro 2|||PARP catalytic|||Poly [ADP-ribose] polymerase|||Protein mono-ADP-ribosyltransferase PARP15|||Reduces catalytic activity 20-fold. Abolishes activity; when associated with Y-559 and A-560.|||Slightly reduces catalytic activity. Abolishes activity; when associated with Y-559 and C-604.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252436|||http://purl.uniprot.org/annotation/PRO_5014568445|||http://purl.uniprot.org/annotation/VAR_027862|||http://purl.uniprot.org/annotation/VAR_027863|||http://purl.uniprot.org/annotation/VAR_056658|||http://purl.uniprot.org/annotation/VSP_020971|||http://purl.uniprot.org/annotation/VSP_020972
http://togogenome.org/gene/9606:LGALS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00182                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Galectin 1|||Galectin 2|||Galectin-9|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3, isoform 5 and isoform 6.|||In isoform 4 and isoform 5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076946|||http://purl.uniprot.org/annotation/VAR_020453|||http://purl.uniprot.org/annotation/VSP_003096|||http://purl.uniprot.org/annotation/VSP_057842|||http://purl.uniprot.org/annotation/VSP_057843
http://togogenome.org/gene/9606:FOS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P01100|||http://purl.uniprot.org/uniprot/Q6FG41                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN.|||BZIP|||Basic motif; required for the activation of phospholipid synthesis, but not for CDS1-binding|||Decreased sumoylation levels.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362.|||Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374.|||Leucine-zipper|||Loss of activation of phospholipid synthesis; when associated with E-10.|||Loss of activation of phospholipid synthesis; when associated with E-30.|||Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374.|||No change in sumoylation levels.|||No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362.|||No change in sumoylation.|||No effect on Tyr-phosphorylation. Loss of endoplasmic reticulum localization in quiescent cells.|||Overall loss of Tyr-phosphorylation, including that of Y-10 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells.|||Overall loss of Tyr-phosphorylation, including that of Y-30 phosphorylation. Localizes to the endoplasmic reticulum in quiescent cells. Activates phospholipid synthesis in growing cells.|||Phosphoserine; by MAPK1 and MAPK3|||Phosphoserine; by MAPK1, MAPK3 and RPS6KA3|||Phosphothreonine|||Phosphothreonine; by MAPK1 and MAPK3|||Phosphotyrosine; by SRC|||Polar residues|||Protein c-Fos|||bZIP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000076465|||http://purl.uniprot.org/annotation/VSP_055560|||http://purl.uniprot.org/annotation/VSP_055561
http://togogenome.org/gene/9606:GABRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N1C3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Gamma-aminobutyric acid receptor subunit gamma-1|||Helical|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000473|||http://purl.uniprot.org/annotation/VAR_047056
http://togogenome.org/gene/9606:IL3RA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P26951                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Motif|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Box 1 motif|||Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||Interleukin-3 receptor subunit alpha|||N-linked (GlcNAc...) asparagine|||WSXWS motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010883|||http://purl.uniprot.org/annotation/VAR_021113|||http://purl.uniprot.org/annotation/VAR_021114|||http://purl.uniprot.org/annotation/VAR_021115|||http://purl.uniprot.org/annotation/VAR_021116|||http://purl.uniprot.org/annotation/VSP_040622
http://togogenome.org/gene/9606:SFMBT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VUG0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Repeat|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||MBT 1|||MBT 2|||MBT 3|||MBT 4|||Polar residues|||SAM|||Scm-like with four MBT domains protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071969|||http://purl.uniprot.org/annotation/VAR_051362
http://togogenome.org/gene/9606:PDIA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Y2|||http://purl.uniprot.org/uniprot/P13667                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||CXXC|||Disordered|||N6-acetyllysine|||Prevents secretion from ER|||Protein disulfide-isomerase A4|||Redox-active|||Thioredoxin|||Thioredoxin 1|||Thioredoxin 2|||Thioredoxin 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034229|||http://purl.uniprot.org/annotation/PRO_5014203101|||http://purl.uniprot.org/annotation/VAR_052580
http://togogenome.org/gene/9606:RSF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05DG0|||http://purl.uniprot.org/uniprot/Q96T23                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||DDT|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||PHD-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Remodeling and spacing factor 1|||WHIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059326|||http://purl.uniprot.org/annotation/VAR_020885|||http://purl.uniprot.org/annotation/VAR_061741|||http://purl.uniprot.org/annotation/VSP_012499|||http://purl.uniprot.org/annotation/VSP_012500
http://togogenome.org/gene/9606:POU6F1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1C7CYV8|||http://purl.uniprot.org/uniprot/B3KT91|||http://purl.uniprot.org/uniprot/Q14863                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Homeobox|||POU domain, class 6, transcription factor 1|||POU-specific                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100759
http://togogenome.org/gene/9606:TNFAIP8L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVP5                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Tumor necrosis factor alpha-induced protein 8-like protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285724|||http://purl.uniprot.org/annotation/VAR_032048
http://togogenome.org/gene/9606:DRD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1A4V4|||http://purl.uniprot.org/uniprot/A8K8E4|||http://purl.uniprot.org/uniprot/E9PCM4|||http://purl.uniprot.org/uniprot/P35462|||http://purl.uniprot.org/uniprot/X5D2G4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||D(3) dopamine receptor|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform 3.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069397|||http://purl.uniprot.org/annotation/VAR_003463|||http://purl.uniprot.org/annotation/VSP_040570
http://togogenome.org/gene/9606:ZKSCAN5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNK8|||http://purl.uniprot.org/uniprot/Q8N718|||http://purl.uniprot.org/uniprot/Q9Y2L8                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11; atypical|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||SCAN box|||Zinc finger protein with KRAB and SCAN domains 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047315
http://togogenome.org/gene/9606:C11orf54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R3B0|||http://purl.uniprot.org/uniprot/A0A087WT99|||http://purl.uniprot.org/uniprot/A8K718|||http://purl.uniprot.org/uniprot/Q9H0W9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DUF1907|||Ester hydrolase C11orf54|||In isoform 2.|||In isoform 3.|||In isoform 4.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000246029|||http://purl.uniprot.org/annotation/VSP_019817|||http://purl.uniprot.org/annotation/VSP_019818|||http://purl.uniprot.org/annotation/VSP_019821
http://togogenome.org/gene/9606:MS4A6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DUN6|||http://purl.uniprot.org/uniprot/E9PSA9|||http://purl.uniprot.org/uniprot/Q9H2W1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Membrane-spanning 4-domains subfamily A member 6A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158638|||http://purl.uniprot.org/annotation/VAR_015652|||http://purl.uniprot.org/annotation/VAR_015653|||http://purl.uniprot.org/annotation/VSP_007381|||http://purl.uniprot.org/annotation/VSP_007382|||http://purl.uniprot.org/annotation/VSP_007383|||http://purl.uniprot.org/annotation/VSP_007384|||http://purl.uniprot.org/annotation/VSP_041191|||http://purl.uniprot.org/annotation/VSP_041192|||http://purl.uniprot.org/annotation/VSP_056732
http://togogenome.org/gene/9606:HEXD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WVB3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreases hexosaminidase activity.|||Decreases hexosaminidase activity. Optimum pH shifts to 7.5.|||Hexosaminidase D|||In isoform 2.|||Loss of hexosaminidase activity.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316790|||http://purl.uniprot.org/annotation/VAR_038395|||http://purl.uniprot.org/annotation/VAR_060726|||http://purl.uniprot.org/annotation/VSP_030777
http://togogenome.org/gene/9606:TNNI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P19237                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Involved in binding TNC|||Involved in binding TNC and actin|||N-acetylproline|||Phosphoserine|||Removed|||Troponin I, slow skeletal muscle                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186139|||http://purl.uniprot.org/annotation/VAR_052403
http://togogenome.org/gene/9606:USP25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UHP3                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes sumoylation. Decreased enzymatic activity.|||Abrogates deubiquitinating activity. No effect on homo- or oligomerization.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In isoform USP25b.|||In isoform USP25m.|||No effect on interaction with SYK.|||No interaction with SUMO3; when associated with A-91.|||No interaction with SUMO3; when associated with A-92.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Required for SUMO paralog-specific binding|||SUMO interaction domain (SIM)|||UBA-like|||UIM 1|||UIM 2|||USP|||Ubiquitin carboxyl-terminal hydrolase 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080653|||http://purl.uniprot.org/annotation/VSP_039631|||http://purl.uniprot.org/annotation/VSP_039632
http://togogenome.org/gene/9606:ERRFI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KTV8|||http://purl.uniprot.org/uniprot/Q9UJM3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes inhibition of EGFR activity.|||Cdc42 binding|||Disordered|||ERBB receptor feedback inhibitor 1|||Interaction with EGFR and ERBB2 and regulation of EGFR activation|||Mig-6|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096487|||http://purl.uniprot.org/annotation/VAR_050975|||http://purl.uniprot.org/annotation/VAR_063039
http://togogenome.org/gene/9606:E2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14209                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Motif|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cyclin A/CDK2 binding|||DEF box|||Dimerization|||Disordered|||Leucine-zipper|||Polar residues|||Pro residues|||Retinoblastoma protein binding|||Transactivation|||Transcription factor E2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219464|||http://purl.uniprot.org/annotation/VAR_018990|||http://purl.uniprot.org/annotation/VAR_018991
http://togogenome.org/gene/9606:C11orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N5U0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Pro residues|||Uncharacterized protein C11orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240702|||http://purl.uniprot.org/annotation/VAR_026831
http://togogenome.org/gene/9606:XYLT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86Y38                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes enzyme activity but does not affect UDP-binding.|||Basic and acidic residues|||Cytoplasmic|||Decreased enzyme activity.|||Decreased enzyme activity. Strongly decreased enzyme activity; when associated with A-598.|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In DBQD2; causes retention in the endoplasmic reticulum.|||In DBQD2; causes retention in the endoplasmic reticulum; impairs dermatan sulfate proteoglycan synthesis.|||In PXE; acts as a modifier of disease severity; results in higher serum xylosyltransferase activity.|||Loss of enzyme activity.|||Lumenal|||N-linked (GlcNAc...) asparagine|||No effect on enzyme activity.|||No effect.|||Polar residues|||Reduced enzyme activity but does not affect UDP-binding.|||Strongly decreased enzyme activity; when associated with A-599.|||Strongly reduced enzyme activity but does not affect UDP-binding.|||Strongly reduced enzyme activity.|||Xylosyltransferase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191400|||http://purl.uniprot.org/annotation/VAR_049324|||http://purl.uniprot.org/annotation/VAR_049325|||http://purl.uniprot.org/annotation/VAR_049326|||http://purl.uniprot.org/annotation/VAR_049327|||http://purl.uniprot.org/annotation/VAR_071271|||http://purl.uniprot.org/annotation/VAR_071272|||http://purl.uniprot.org/annotation/VAR_071273|||http://purl.uniprot.org/annotation/VAR_071274|||http://purl.uniprot.org/annotation/VAR_071275
http://togogenome.org/gene/9606:VGLL4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A075B6E4|||http://purl.uniprot.org/uniprot/A0A0A6YYI5|||http://purl.uniprot.org/uniprot/G5E9M7|||http://purl.uniprot.org/uniprot/G5E9M9|||http://purl.uniprot.org/uniprot/Q14135                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Transcription cofactor vestigial-like protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191351|||http://purl.uniprot.org/annotation/VAR_024689|||http://purl.uniprot.org/annotation/VSP_010776|||http://purl.uniprot.org/annotation/VSP_040210|||http://purl.uniprot.org/annotation/VSP_040211|||http://purl.uniprot.org/annotation/VSP_040212|||http://purl.uniprot.org/annotation/VSP_040213|||http://purl.uniprot.org/annotation/VSP_040214|||http://purl.uniprot.org/annotation/VSP_040215|||http://purl.uniprot.org/annotation/VSP_040216
http://togogenome.org/gene/9606:NR2F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24468                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Zinc Finger                                                                                  ^@                                                                                  COUP transcription factor 2|||Disordered|||Important for dimerization|||In CHTD4.|||In CHTD4; the mutation results in increased transcription activation of the EGR1 promoter; transcription activation of the APOB promoter is decreased.|||In CHTD4; the mutation results in reduced transcription activation of the EGR1 promoter; does not affect transcription activation of the APOBFT promoter.|||In CHTD4; the mutation results in reduced transcriptional activity.|||In isoform 2.|||In isoform 3.|||Interaction with ZFPM2|||NR C4-type|||NR LBD|||Nuclear receptor|||Phosphothreonine|||Polar residues|||Pro residues|||Reduces transcription activation by 40%; when associated with E-228.|||Reduces transcription activation by 40%; when associated with R-398.|||Reduces transcription activation by 50%.|||Reduces transcription activation by 50%; when associated with A-249.|||Reduces transcription activation by 50%; when associated with A-250.|||Reduces transcription activation by 80%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053606|||http://purl.uniprot.org/annotation/VAR_071766|||http://purl.uniprot.org/annotation/VAR_071767|||http://purl.uniprot.org/annotation/VAR_071768|||http://purl.uniprot.org/annotation/VAR_071769|||http://purl.uniprot.org/annotation/VAR_071770|||http://purl.uniprot.org/annotation/VAR_071771|||http://purl.uniprot.org/annotation/VSP_042630|||http://purl.uniprot.org/annotation/VSP_043897
http://togogenome.org/gene/9606:GALNT17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2L4S5|||http://purl.uniprot.org/uniprot/Q6IS24                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Polypeptide N-acetylgalactosaminyltransferase 17|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059139
http://togogenome.org/gene/9606:JRK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75564                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||DDE-1|||Disordered|||H-T-H motif|||HTH CENPB-type|||HTH psq-type|||In isoform 2.|||Jerky protein homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000126128|||http://purl.uniprot.org/annotation/VSP_059375
http://togogenome.org/gene/9606:SLC22A25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6T423                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328926|||http://purl.uniprot.org/annotation/VAR_042576|||http://purl.uniprot.org/annotation/VAR_042577|||http://purl.uniprot.org/annotation/VAR_057783|||http://purl.uniprot.org/annotation/VAR_057784|||http://purl.uniprot.org/annotation/VAR_060287
http://togogenome.org/gene/9606:MAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H063                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1 and SUMO2)|||Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-68 and A-75.|||No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-68.|||No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-75.|||No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-68 and D-75.|||No interaction with RNA pol III and impaired recruitment to tRNA gene promoters.|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Polar residues|||Repressor of RNA polymerase III transcription MAF1 homolog|||Stronger repressive effect on RNA polymerase III transcription. Stronger repressive effect on RNA polymerase III transcription; when associated with A-60 and A-68. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-64 and A-68.|||Stronger repressive effect on RNA polymerase III transcription; when associated with A-60 and A-75. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-64 and A-75.|||Stronger repressive effect on RNA polymerase III transcription; when associated with A-68 and A-75. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-64, A-68 and A-75.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000213973|||http://purl.uniprot.org/annotation/VAR_060408
http://togogenome.org/gene/9606:CDKN2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42772                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1; truncated|||ANK 2|||ANK 3|||ANK 4|||Cyclin-dependent kinase 4 inhibitor B|||In isoform 2.|||In lung adenocarcinoma.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144184|||http://purl.uniprot.org/annotation/VAR_001488|||http://purl.uniprot.org/annotation/VAR_001489|||http://purl.uniprot.org/annotation/VSP_043898
http://togogenome.org/gene/9606:ANK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KX39|||http://purl.uniprot.org/uniprot/P16157                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (3S)-3-hydroxyasparagine; by HIF1AN; partial|||(3S)-3-hydroxyaspartate; by HIF1AN; partial|||55 kDa regulatory domain|||89 kDa domain|||ANK|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 17|||ANK 18|||ANK 19|||ANK 2|||ANK 20|||ANK 21|||ANK 22|||ANK 23|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Abolishes interaction with OBSCN (in isoform Mu17).|||Ankyrin-1|||Basic and acidic residues|||Death|||Disordered|||In Brueggen.|||In Duesseldorf.|||In SPH1.|||In a breast cancer sample; somatic mutation.|||In isoform 22.|||In isoform Br21.|||In isoform Er11 and isoform Er12.|||In isoform Er13 and isoform Er14.|||In isoform Er15 and isoform Mu18.|||In isoform Er16.|||In isoform Er2, isoform Er4, isoform Er6, isoform Er8, isoform Er10, isoform Er12 and isoform Er14.|||In isoform Er3, isoform Er4 and isoform Br21.|||In isoform Er5, isoform Er6 and isoform Mu17.|||In isoform Er7 and isoform Er8.|||In isoform Er9, isoform Er10 and isoform Mu19.|||In isoform Mu17, isoform Mu18, isoform Mu19, isoform 22 and isoform 23.|||In isoform Mu17, isoform Mu18, isoform Mu19, isoform Mu20, isoform 22 and isoform 23.|||In isoform Mu20.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||UPA domain|||ZU5|||ZU5 1|||ZU5 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066883|||http://purl.uniprot.org/annotation/VAR_000595|||http://purl.uniprot.org/annotation/VAR_000596|||http://purl.uniprot.org/annotation/VAR_000597|||http://purl.uniprot.org/annotation/VAR_000598|||http://purl.uniprot.org/annotation/VAR_000599|||http://purl.uniprot.org/annotation/VAR_000600|||http://purl.uniprot.org/annotation/VAR_000601|||http://purl.uniprot.org/annotation/VAR_000602|||http://purl.uniprot.org/annotation/VAR_026411|||http://purl.uniprot.org/annotation/VAR_028769|||http://purl.uniprot.org/annotation/VAR_028770|||http://purl.uniprot.org/annotation/VAR_028771|||http://purl.uniprot.org/annotation/VAR_028772|||http://purl.uniprot.org/annotation/VAR_028773|||http://purl.uniprot.org/annotation/VAR_035605|||http://purl.uniprot.org/annotation/VAR_048263|||http://purl.uniprot.org/annotation/VAR_054991|||http://purl.uniprot.org/annotation/VAR_054992|||http://purl.uniprot.org/annotation/VAR_061012|||http://purl.uniprot.org/annotation/VSP_000264|||http://purl.uniprot.org/annotation/VSP_000265|||http://purl.uniprot.org/annotation/VSP_000266|||http://purl.uniprot.org/annotation/VSP_018439|||http://purl.uniprot.org/annotation/VSP_018440|||http://purl.uniprot.org/annotation/VSP_018441|||http://purl.uniprot.org/annotation/VSP_018442|||http://purl.uniprot.org/annotation/VSP_018443|||http://purl.uniprot.org/annotation/VSP_018444|||http://purl.uniprot.org/annotation/VSP_018445|||http://purl.uniprot.org/annotation/VSP_018446|||http://purl.uniprot.org/annotation/VSP_018447|||http://purl.uniprot.org/annotation/VSP_018448|||http://purl.uniprot.org/annotation/VSP_018449|||http://purl.uniprot.org/annotation/VSP_018450|||http://purl.uniprot.org/annotation/VSP_018451|||http://purl.uniprot.org/annotation/VSP_045439
http://togogenome.org/gene/9606:LRP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98164|||http://purl.uniprot.org/uniprot/Q7Z5C0|||http://purl.uniprot.org/uniprot/Q7Z5C1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like|||EGF-like 1; calcium-binding|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6|||Endocytosis signal|||Extracellular|||Found in a renal cell carcinoma sample; somatic mutation.|||Found in patients with a phenotype suggestive of Stickler syndrome; unknown pathological significance.|||Found in patients with mild intellectual disability; unknown pathological significance.|||Helical|||In DBS.|||In a colorectal cancer sample; somatic mutation.|||Interaction with DAB2|||LDL-receptor class A 1|||LDL-receptor class A 10|||LDL-receptor class A 11|||LDL-receptor class A 12|||LDL-receptor class A 13|||LDL-receptor class A 14|||LDL-receptor class A 15|||LDL-receptor class A 16|||LDL-receptor class A 17|||LDL-receptor class A 18|||LDL-receptor class A 19|||LDL-receptor class A 2|||LDL-receptor class A 20|||LDL-receptor class A 21|||LDL-receptor class A 22|||LDL-receptor class A 23|||LDL-receptor class A 24|||LDL-receptor class A 25|||LDL-receptor class A 26|||LDL-receptor class A 27|||LDL-receptor class A 28|||LDL-receptor class A 29|||LDL-receptor class A 3|||LDL-receptor class A 30|||LDL-receptor class A 31|||LDL-receptor class A 32|||LDL-receptor class A 33|||LDL-receptor class A 34|||LDL-receptor class A 35|||LDL-receptor class A 36|||LDL-receptor class A 4|||LDL-receptor class A 5|||LDL-receptor class A 6|||LDL-receptor class A 7|||LDL-receptor class A 8|||LDL-receptor class A 9|||LDL-receptor class B|||LDL-receptor class B 1|||LDL-receptor class B 10|||LDL-receptor class B 11|||LDL-receptor class B 12|||LDL-receptor class B 13|||LDL-receptor class B 14|||LDL-receptor class B 15|||LDL-receptor class B 16|||LDL-receptor class B 17|||LDL-receptor class B 18|||LDL-receptor class B 19|||LDL-receptor class B 2|||LDL-receptor class B 20|||LDL-receptor class B 21|||LDL-receptor class B 22|||LDL-receptor class B 23|||LDL-receptor class B 24|||LDL-receptor class B 25|||LDL-receptor class B 26|||LDL-receptor class B 27|||LDL-receptor class B 28|||LDL-receptor class B 29|||LDL-receptor class B 3|||LDL-receptor class B 30|||LDL-receptor class B 31|||LDL-receptor class B 32|||LDL-receptor class B 33|||LDL-receptor class B 34|||LDL-receptor class B 35|||LDL-receptor class B 4|||LDL-receptor class B 5|||LDL-receptor class B 6|||LDL-receptor class B 7|||LDL-receptor class B 8|||LDL-receptor class B 9|||Low-density lipoprotein receptor-related protein 2|||N-linked (GlcNAc...) asparagine|||NPXY motif|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||PxLPxI/L motif 1; mediates interaction with ANKRA2|||PxLPxI/L motif 2; mediates interaction with ANKRA2|||SH2-binding|||SH3-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017321|||http://purl.uniprot.org/annotation/PRO_5004296933|||http://purl.uniprot.org/annotation/PRO_5004298552|||http://purl.uniprot.org/annotation/VAR_005421|||http://purl.uniprot.org/annotation/VAR_005422|||http://purl.uniprot.org/annotation/VAR_005423|||http://purl.uniprot.org/annotation/VAR_005424|||http://purl.uniprot.org/annotation/VAR_020218|||http://purl.uniprot.org/annotation/VAR_020219|||http://purl.uniprot.org/annotation/VAR_029182|||http://purl.uniprot.org/annotation/VAR_029183|||http://purl.uniprot.org/annotation/VAR_029184|||http://purl.uniprot.org/annotation/VAR_035996|||http://purl.uniprot.org/annotation/VAR_037009|||http://purl.uniprot.org/annotation/VAR_037010|||http://purl.uniprot.org/annotation/VAR_037011|||http://purl.uniprot.org/annotation/VAR_037012|||http://purl.uniprot.org/annotation/VAR_037013|||http://purl.uniprot.org/annotation/VAR_037014|||http://purl.uniprot.org/annotation/VAR_061294|||http://purl.uniprot.org/annotation/VAR_064727|||http://purl.uniprot.org/annotation/VAR_075534|||http://purl.uniprot.org/annotation/VAR_075535
http://togogenome.org/gene/9606:SAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384NQ10|||http://purl.uniprot.org/uniprot/P21673                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Diamine acetyltransferase 1|||N-acetyltransferase|||Proton donor|||Reduces activity by 95%.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074591
http://togogenome.org/gene/9606:LRRC20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TCA0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Repeat|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 20|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084475|||http://purl.uniprot.org/annotation/VSP_015933|||http://purl.uniprot.org/annotation/VSP_015934
http://togogenome.org/gene/9606:GATA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P23769                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Disordered|||Endothelial transcription factor GATA-2|||GATA-type 1|||GATA-type 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In IMD21 and MDS.|||In IMD21.|||In LMPM.|||In MDS.|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083403|||http://purl.uniprot.org/annotation/VAR_055004|||http://purl.uniprot.org/annotation/VAR_055005|||http://purl.uniprot.org/annotation/VAR_066405|||http://purl.uniprot.org/annotation/VAR_066406|||http://purl.uniprot.org/annotation/VAR_066407|||http://purl.uniprot.org/annotation/VAR_066643|||http://purl.uniprot.org/annotation/VAR_066644|||http://purl.uniprot.org/annotation/VAR_066645|||http://purl.uniprot.org/annotation/VSP_041126
http://togogenome.org/gene/9606:PTP4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q93096                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Propeptide|||Region|||Secondary Structure|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Strand|||Turn                                                                                  ^@                                                                                  80% loss of catalytic activity; delay in progression through G2/M.|||Abolishes enzymatic activity.|||Cysteine methyl ester|||Interaction with ATF5|||No effect on catalytic activity.|||No effect on subcellular location.|||Phosphocysteine intermediate|||Protein tyrosine phosphatase type IVA 1|||Proton donor|||Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis.|||Reduces trimerization.|||Removed in mature form|||S-farnesyl cysteine|||Tyrosine-protein phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094780|||http://purl.uniprot.org/annotation/PRO_0000396726
http://togogenome.org/gene/9606:PRKD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94806                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a glioblastoma multiforme sample; somatic mutation.|||In isoform 2.|||Increased ability to bind DAG, no effect on phorbol-ester binding.|||No effect on ability to bind phorbol ester, increase in ability to bind DAG.|||No effect on ability to bind phorbol ester, loss of ability to bind DAG, reduced DAG-induced membrane translocation.|||PH|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphoserine|||Phosphoserine; by PKC|||Phosphoserine; by autocatalysis|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase D3|||Slight increase in ability to bind DAG, no effect on phorbol-ester binding.|||Slight loss in ability to bind DAG and phorbol-ester.|||Slight loss in ability to bind DAG and phorbol-ester; when associated with A-156.|||Slight loss in ability to bind DAG and phorbol-ester; when associated with F-158.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055717|||http://purl.uniprot.org/annotation/VAR_037147|||http://purl.uniprot.org/annotation/VAR_037148|||http://purl.uniprot.org/annotation/VAR_037149|||http://purl.uniprot.org/annotation/VAR_042336|||http://purl.uniprot.org/annotation/VAR_050561|||http://purl.uniprot.org/annotation/VAR_061532|||http://purl.uniprot.org/annotation/VSP_029405|||http://purl.uniprot.org/annotation/VSP_029406
http://togogenome.org/gene/9606:ABCA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KVV3|||http://purl.uniprot.org/uniprot/Q86UK0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  ABC transporter|||ABC transporter 1|||ABC transporter 2|||Disordered|||Glucosylceramide transporter ABCA12|||Helical|||In ARCI4A.|||In ARCI4A; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma.|||In ARCI4B.|||In ARCI4B; unknown pathological significance.|||In a pancreatic ductal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093300|||http://purl.uniprot.org/annotation/VAR_019597|||http://purl.uniprot.org/annotation/VAR_019598|||http://purl.uniprot.org/annotation/VAR_019599|||http://purl.uniprot.org/annotation/VAR_019600|||http://purl.uniprot.org/annotation/VAR_019601|||http://purl.uniprot.org/annotation/VAR_019602|||http://purl.uniprot.org/annotation/VAR_027444|||http://purl.uniprot.org/annotation/VAR_027445|||http://purl.uniprot.org/annotation/VAR_027446|||http://purl.uniprot.org/annotation/VAR_027447|||http://purl.uniprot.org/annotation/VAR_027448|||http://purl.uniprot.org/annotation/VAR_027449|||http://purl.uniprot.org/annotation/VAR_055473|||http://purl.uniprot.org/annotation/VAR_055474|||http://purl.uniprot.org/annotation/VAR_055475|||http://purl.uniprot.org/annotation/VAR_055476|||http://purl.uniprot.org/annotation/VAR_062663|||http://purl.uniprot.org/annotation/VAR_067075|||http://purl.uniprot.org/annotation/VAR_067076|||http://purl.uniprot.org/annotation/VAR_067077|||http://purl.uniprot.org/annotation/VAR_067078|||http://purl.uniprot.org/annotation/VAR_067079|||http://purl.uniprot.org/annotation/VAR_067080|||http://purl.uniprot.org/annotation/VAR_067081|||http://purl.uniprot.org/annotation/VAR_067082|||http://purl.uniprot.org/annotation/VAR_067083|||http://purl.uniprot.org/annotation/VAR_084428|||http://purl.uniprot.org/annotation/VAR_084429|||http://purl.uniprot.org/annotation/VAR_084430|||http://purl.uniprot.org/annotation/VSP_011283|||http://purl.uniprot.org/annotation/VSP_011284
http://togogenome.org/gene/9606:MUSTN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVN3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Musculoskeletal embryonic nuclear protein 1|||Nuclear localization signal|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299447
http://togogenome.org/gene/9606:GPX6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P59796                                                                                  ^@                                                                                  Active Site|||Chain|||Modification|||Molecule Processing|||Natural Variation|||Non standard residue|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Non standard residue|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Glutathione peroxidase 6|||Selenocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013081|||http://purl.uniprot.org/annotation/VAR_025249|||http://purl.uniprot.org/annotation/VAR_025250|||http://purl.uniprot.org/annotation/VAR_025251|||http://purl.uniprot.org/annotation/VAR_025252|||http://purl.uniprot.org/annotation/VAR_025253|||http://purl.uniprot.org/annotation/VAR_025254|||http://purl.uniprot.org/annotation/VAR_025255|||http://purl.uniprot.org/annotation/VAR_025256|||http://purl.uniprot.org/annotation/VAR_025257|||http://purl.uniprot.org/annotation/VAR_025258
http://togogenome.org/gene/9606:CHRNB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P30926                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||Key residue for a low dissociation (K(off)) from the conotoxin BuIA|||Key residue that facilitates effective access of the conotoxin BuIA to the channel binding site|||N-linked (GlcNAc...) asparagine|||Neuronal acetylcholine receptor subunit beta-4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000389|||http://purl.uniprot.org/annotation/VAR_013241|||http://purl.uniprot.org/annotation/VAR_013242|||http://purl.uniprot.org/annotation/VAR_013243|||http://purl.uniprot.org/annotation/VAR_048174|||http://purl.uniprot.org/annotation/VSP_046674|||http://purl.uniprot.org/annotation/VSP_046675
http://togogenome.org/gene/9606:LCE1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7P3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope protein 1B|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235325
http://togogenome.org/gene/9606:POLDIP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DEM9|||http://purl.uniprot.org/uniprot/Q9Y2S7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  ApaG|||Mitochondrion|||Phosphothreonine|||Polymerase delta-interacting protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000197975
http://togogenome.org/gene/9606:RBM33                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EV2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylalanine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Polar residues|||Pro residues|||RNA-binding protein 33|||RRM|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000292982|||http://purl.uniprot.org/annotation/VAR_052223|||http://purl.uniprot.org/annotation/VSP_030143|||http://purl.uniprot.org/annotation/VSP_030144
http://togogenome.org/gene/9606:MOCS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZB8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||For molybdenum cofactor biosynthesis protein C activity|||Impairs precursor Z synthesis.|||In MOCODA.|||In isoform 2 and isoform 8.|||In isoform 3.|||In isoform 4 and isoform 7.|||In isoform 4.|||In isoform 6 and isoform 7.|||In isoform MOCS1A, isoform 2 and isoform 3.|||Molybdenum cofactor biosynthesis protein 1|||Molybdenum cofactor biosynthesis protein A|||Molybdenum cofactor biosynthesis protein C|||N6-acetyllysine|||Phosphoserine|||Radical SAM core                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097870|||http://purl.uniprot.org/annotation/VAR_015658|||http://purl.uniprot.org/annotation/VAR_015659|||http://purl.uniprot.org/annotation/VAR_015660|||http://purl.uniprot.org/annotation/VAR_015661|||http://purl.uniprot.org/annotation/VAR_015662|||http://purl.uniprot.org/annotation/VAR_054823|||http://purl.uniprot.org/annotation/VAR_054824|||http://purl.uniprot.org/annotation/VAR_054825|||http://purl.uniprot.org/annotation/VAR_054826|||http://purl.uniprot.org/annotation/VAR_054827|||http://purl.uniprot.org/annotation/VAR_056131|||http://purl.uniprot.org/annotation/VAR_061346|||http://purl.uniprot.org/annotation/VSP_007439|||http://purl.uniprot.org/annotation/VSP_036821|||http://purl.uniprot.org/annotation/VSP_036822|||http://purl.uniprot.org/annotation/VSP_036823|||http://purl.uniprot.org/annotation/VSP_036824|||http://purl.uniprot.org/annotation/VSP_036825|||http://purl.uniprot.org/annotation/VSP_036826|||http://purl.uniprot.org/annotation/VSP_036827
http://togogenome.org/gene/9606:ZAR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9EG67|||http://purl.uniprot.org/uniprot/Q86SH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Basic and acidic residues|||Disordered|||Polar residues|||Zygote arrest protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187011
http://togogenome.org/gene/9606:GPX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96SL4                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Sequence Conflict|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Glutathione peroxidase 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000013084
http://togogenome.org/gene/9606:OR52E8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVH0|||http://purl.uniprot.org/uniprot/Q6IFG1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 52E8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150776
http://togogenome.org/gene/9606:PAG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NWQ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type III membrane protein|||Interaction with CSK|||Interaction with NHERF1|||No effect on interaction with FYN or CSK.|||No effect on interaction with FYN. Abolishes interaction with CSK.|||Phosphoprotein associated with glycosphingolipid-enriched microdomains 1|||Phosphoserine|||Phosphotyrosine|||Phosphotyrosine; by FYN and LYN|||Phosphotyrosine; by LYN|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000083338
http://togogenome.org/gene/9606:CCDC77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BR77                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 77|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271003|||http://purl.uniprot.org/annotation/VAR_029838|||http://purl.uniprot.org/annotation/VAR_029839|||http://purl.uniprot.org/annotation/VSP_043135
http://togogenome.org/gene/9606:TTC39C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3X0|||http://purl.uniprot.org/uniprot/G3V1P2|||http://purl.uniprot.org/uniprot/Q8N584                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||TPR 1|||TPR 2|||TPR 3|||Tetratricopeptide repeat protein 39C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274352|||http://purl.uniprot.org/annotation/PRO_5002863952|||http://purl.uniprot.org/annotation/PRO_5015091609|||http://purl.uniprot.org/annotation/VSP_022720|||http://purl.uniprot.org/annotation/VSP_046039|||http://purl.uniprot.org/annotation/VSP_046040
http://togogenome.org/gene/9606:ATG4D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGM8|||http://purl.uniprot.org/uniprot/Q86TL0                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes cleavage by CASP3.|||Basic and acidic residues|||Cleavage; by CASP3|||Cryptic mitochondrial signal peptide|||Cysteine protease ATG4D|||Cysteine protease ATG4D, mitochondrial|||Disordered|||Found in patients with non-obstructive azoospermia; unknown pathological significance.|||Found in patients with non-obstructive azoospermia; unknown pathological significance; decreased expression of MAP1LC3B; increased programmed cell death in spermatogenic cells.|||In isoform 2.|||Nucleophile|||Peptidase C54 catalytic|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215853|||http://purl.uniprot.org/annotation/PRO_0000423408|||http://purl.uniprot.org/annotation/VAR_085353|||http://purl.uniprot.org/annotation/VAR_085354|||http://purl.uniprot.org/annotation/VAR_085355|||http://purl.uniprot.org/annotation/VAR_085356|||http://purl.uniprot.org/annotation/VSP_056671
http://togogenome.org/gene/9606:TCP10L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDR4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Disrupts self-association.|||Greatly decreases in vitro transcription inhibition activity.|||Leucine-zipper|||Polar residues|||T-complex protein 10A homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072462|||http://purl.uniprot.org/annotation/VAR_016099|||http://purl.uniprot.org/annotation/VAR_049089
http://togogenome.org/gene/9606:NOX4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KQ17|||http://purl.uniprot.org/uniprot/B7Z523|||http://purl.uniprot.org/uniprot/B7Z529|||http://purl.uniprot.org/uniprot/Q9NPH5                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||FAD-binding FR-type|||Ferric oxidoreductase|||Helical|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 6 and isoform 9.|||In isoform 5.|||In isoform 7.|||In isoform 8 and isoform 9.|||Mediates interaction with TLR4|||N-linked (GlcNAc...) asparagine|||NADPH oxidase 4|||Partial loss of catalytic activity. No effect on CYBA localization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238980|||http://purl.uniprot.org/annotation/VAR_047114|||http://purl.uniprot.org/annotation/VSP_019052|||http://purl.uniprot.org/annotation/VSP_019053|||http://purl.uniprot.org/annotation/VSP_019054|||http://purl.uniprot.org/annotation/VSP_019055|||http://purl.uniprot.org/annotation/VSP_019056|||http://purl.uniprot.org/annotation/VSP_019057|||http://purl.uniprot.org/annotation/VSP_019058|||http://purl.uniprot.org/annotation/VSP_053826
http://togogenome.org/gene/9606:ITGA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R627|||http://purl.uniprot.org/uniprot/P08648                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||FG-GAP|||FG-GAP 1|||FG-GAP 2|||FG-GAP 3|||FG-GAP 4|||FG-GAP 5|||FG-GAP 6|||FG-GAP 7|||GFFKR motif|||Helical|||Integrin alpha-2|||Integrin alpha-5|||Integrin alpha-5 heavy chain|||Integrin alpha-5 light chain|||Interaction with HPS5|||Interchain (between heavy and light chains)|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016249|||http://purl.uniprot.org/annotation/PRO_0000016250|||http://purl.uniprot.org/annotation/PRO_0000016251|||http://purl.uniprot.org/annotation/VAR_049631
http://togogenome.org/gene/9606:LANCL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NS86                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Interaction with inositol phospholipids|||LanC-like protein 2|||Loss of membrane localization and results in localization to the nucleus, particularly to the nucleoli.|||N-myristoyl glycine|||Phosphotyrosine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191272|||http://purl.uniprot.org/annotation/VAR_053480|||http://purl.uniprot.org/annotation/VAR_060064
http://togogenome.org/gene/9606:KCTD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y597                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein KCTD3|||Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||Interaction with HCN3|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247839|||http://purl.uniprot.org/annotation/VAR_027156|||http://purl.uniprot.org/annotation/VSP_020068|||http://purl.uniprot.org/annotation/VSP_020069
http://togogenome.org/gene/9606:CHMP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96FZ7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Abolishes interaction with VPS4A.|||Abolishes myristoylation.|||Charged multivesicular body protein 6|||Does not affect the subcellular location.|||Interaction with VPS4A|||Membrane association; releases autoinhibition.|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Reduces interaction with VPS4A.|||Removed|||Type-2 MIT-interacting motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211508|||http://purl.uniprot.org/annotation/VAR_061807
http://togogenome.org/gene/9606:ALDH1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DTU7|||http://purl.uniprot.org/uniprot/Q3SY69                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Aldehyde dehydrogenase domain|||Carrier|||Essential for catalytic activity|||Hydrolase domain|||In isoform 2.|||In isoform 3.|||Loss of phosphopantetheinylation.|||Mitochondrial 10-formyltetrahydrofolate dehydrogenase|||Mitochondrion; not cleaved|||N6-acetyllysine|||N6-succinyllysine|||No effect on phosphopantetheinylation.|||O-(pantetheine 4'-phosphoryl)serine|||Phosphoserine|||Proton acceptor|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316001|||http://purl.uniprot.org/annotation/VSP_030752|||http://purl.uniprot.org/annotation/VSP_030753|||http://purl.uniprot.org/annotation/VSP_030754|||http://purl.uniprot.org/annotation/VSP_030755
http://togogenome.org/gene/9606:SERPINE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05121                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Increased half-life of the active form when associated with C-197.|||Increased half-life of the active form when associated with C-355.|||N-linked (GlcNAc...) asparagine|||Plasminogen activator inhibitor 1|||Reactive bond                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032499|||http://purl.uniprot.org/annotation/VAR_007099|||http://purl.uniprot.org/annotation/VAR_011750|||http://purl.uniprot.org/annotation/VAR_013086|||http://purl.uniprot.org/annotation/VAR_013087|||http://purl.uniprot.org/annotation/VAR_013088|||http://purl.uniprot.org/annotation/VSP_045493
http://togogenome.org/gene/9606:WDR44                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JSH3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Binding activity|||Disordered|||Important for interaction with RAB11A|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||Phosphoinactive mutant. Impaired interaction with RAB11A; when associated with Ala-342. Increased ciliogenesis in serum-starved conditions; when associated with Ala-342.|||Phosphoinactive mutant. Impaired interaction with RAB11A; when associated with Ala-344. Induced ciliogenesis in serum-starved conditions; when associated with Ala-344.|||Phosphomimetic mutant. No ciliogenesis induction in serum-starved conditions; when associated with Asp-342.|||Phosphomimetic mutant. No ciliogenesis induction in serum-starved conditions; when associated with Asp-344.|||Phosphoserine|||Phosphoserine; by PKB/AKT1|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Pro residues|||Removed|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD repeat-containing protein 44                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262769|||http://purl.uniprot.org/annotation/VAR_029538|||http://purl.uniprot.org/annotation/VAR_029539|||http://purl.uniprot.org/annotation/VSP_021807|||http://purl.uniprot.org/annotation/VSP_021808|||http://purl.uniprot.org/annotation/VSP_021809|||http://purl.uniprot.org/annotation/VSP_021810|||http://purl.uniprot.org/annotation/VSP_046637|||http://purl.uniprot.org/annotation/VSP_046638
http://togogenome.org/gene/9606:OTOA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q05BM7|||http://purl.uniprot.org/uniprot/Q7RTW8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Lipid Binding|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GPI-anchor amidated alanine|||In isoform 2.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Otoancorin|||Polar residues|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021971|||http://purl.uniprot.org/annotation/PRO_0000021972|||http://purl.uniprot.org/annotation/VSP_012211|||http://purl.uniprot.org/annotation/VSP_012212|||http://purl.uniprot.org/annotation/VSP_012213|||http://purl.uniprot.org/annotation/VSP_012214|||http://purl.uniprot.org/annotation/VSP_043345|||http://purl.uniprot.org/annotation/VSP_043346|||http://purl.uniprot.org/annotation/VSP_043347
http://togogenome.org/gene/9606:LOC102723553                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P58511                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Small integral membrane protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079517|||http://purl.uniprot.org/annotation/VAR_054066
http://togogenome.org/gene/9606:SPNS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IVW8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In DFNB115; unknown pathological significance.|||Loss of function; does not rescue the cardia bifida phenotype in the morpholino knockdown in zebrafish.|||Sphingosine-1-phosphate transporter SPNS2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305043|||http://purl.uniprot.org/annotation/VAR_082112
http://togogenome.org/gene/9606:MRPS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P82933                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Variant|||Strand|||Transit Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Mitochondrion|||N6-acetyllysine|||Small ribosomal subunit protein uS9m                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030655|||http://purl.uniprot.org/annotation/VAR_047902
http://togogenome.org/gene/9606:FGFR3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P22607|||http://purl.uniprot.org/uniprot/Q0IJ44                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Constitutively activated kinase.|||Cytoplasmic|||Disordered|||Extracellular|||Fibroblast growth factor receptor 3|||Helical|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||In ACH.|||In CAN.|||In CATSHLS.|||In KERSEB and TD1.|||In KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation.|||In KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling.|||In KERSEB, BLC, cervical cancer and TD1.|||In KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1.|||In KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation.|||In KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling.|||In LADD2; unknown pathological significance.|||In MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis.|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a lung adenocarcinoma sample; somatic mutation.|||In colorectal cancer.|||In hypochondroplasia and BLC; in hypochondroplasia the form is milder than that seen in individuals with the K-540 or M-650 mutations; constitutively activated kinase.|||In hypochondroplasia.|||In hypochondroplasia; mild.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In keratinocytic non-epidermolytic nevus and ACH; very common mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling.|||Loss of kinase activity. Abolishes ubiquitination.|||Minor effect on kinase activity.|||Minor effect on kinase activity. Increased mitogen activity.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Strongly reduced kinase activity. Strongly reduced mitogen activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016785|||http://purl.uniprot.org/annotation/VAR_004148|||http://purl.uniprot.org/annotation/VAR_004149|||http://purl.uniprot.org/annotation/VAR_004150|||http://purl.uniprot.org/annotation/VAR_004151|||http://purl.uniprot.org/annotation/VAR_004152|||http://purl.uniprot.org/annotation/VAR_004153|||http://purl.uniprot.org/annotation/VAR_004154|||http://purl.uniprot.org/annotation/VAR_004155|||http://purl.uniprot.org/annotation/VAR_004156|||http://purl.uniprot.org/annotation/VAR_004157|||http://purl.uniprot.org/annotation/VAR_004158|||http://purl.uniprot.org/annotation/VAR_004159|||http://purl.uniprot.org/annotation/VAR_004160|||http://purl.uniprot.org/annotation/VAR_004161|||http://purl.uniprot.org/annotation/VAR_018388|||http://purl.uniprot.org/annotation/VAR_018389|||http://purl.uniprot.org/annotation/VAR_018390|||http://purl.uniprot.org/annotation/VAR_022167|||http://purl.uniprot.org/annotation/VAR_022168|||http://purl.uniprot.org/annotation/VAR_022169|||http://purl.uniprot.org/annotation/VAR_022170|||http://purl.uniprot.org/annotation/VAR_022171|||http://purl.uniprot.org/annotation/VAR_029108|||http://purl.uniprot.org/annotation/VAR_029887|||http://purl.uniprot.org/annotation/VAR_042207|||http://purl.uniprot.org/annotation/VAR_042208|||http://purl.uniprot.org/annotation/VAR_042209|||http://purl.uniprot.org/annotation/VAR_042210|||http://purl.uniprot.org/annotation/VSP_002988|||http://purl.uniprot.org/annotation/VSP_002989|||http://purl.uniprot.org/annotation/VSP_040945
http://togogenome.org/gene/9606:AP4B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1ALD0|||http://purl.uniprot.org/uniprot/B3KSJ4|||http://purl.uniprot.org/uniprot/B4DTG3|||http://purl.uniprot.org/uniprot/Q9Y6B7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  AP-4 complex subunit beta-1|||Beta-adaptin appendage C-terminal subdomain|||Decreased interaction with TEPSIN.|||Decreased interaction with TEPSIN; when associated with A-669.|||Decreased interaction with TEPSIN; when associated with S-670.|||Ear; mediates interaction with TEPSIN|||Hinge|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193750|||http://purl.uniprot.org/annotation/VAR_030804|||http://purl.uniprot.org/annotation/VSP_055787|||http://purl.uniprot.org/annotation/VSP_055788|||http://purl.uniprot.org/annotation/VSP_055789
http://togogenome.org/gene/9606:RGS20                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSW4|||http://purl.uniprot.org/uniprot/H9NIM5|||http://purl.uniprot.org/uniprot/O76081                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1, isoform 4 and isoform 5.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||RGS|||Regulator of G-protein signaling 20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204233|||http://purl.uniprot.org/annotation/VSP_005694|||http://purl.uniprot.org/annotation/VSP_005695|||http://purl.uniprot.org/annotation/VSP_005696|||http://purl.uniprot.org/annotation/VSP_005697|||http://purl.uniprot.org/annotation/VSP_005698|||http://purl.uniprot.org/annotation/VSP_005699|||http://purl.uniprot.org/annotation/VSP_005700
http://togogenome.org/gene/9606:ACP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK37|||http://purl.uniprot.org/uniprot/P24666|||http://purl.uniprot.org/uniprot/Q59EH3                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Helical|||In allele ACP1*A.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactive.|||Low molecular weight phosphotyrosine protein phosphatase|||N-acetylalanine|||Nucleophile|||Phosphotyrosine|||Phosphotyrosine protein phosphatase I|||Proton donor|||Reduced phosphorylation and activity.|||Reduced phosphorylation. No effect on activity.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046558|||http://purl.uniprot.org/annotation/VAR_006171|||http://purl.uniprot.org/annotation/VAR_050526|||http://purl.uniprot.org/annotation/VAR_050527|||http://purl.uniprot.org/annotation/VSP_010087|||http://purl.uniprot.org/annotation/VSP_010088|||http://purl.uniprot.org/annotation/VSP_054074|||http://purl.uniprot.org/annotation/VSP_054075
http://togogenome.org/gene/9606:GSC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15499                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein goosecoid-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048891|||http://purl.uniprot.org/annotation/VAR_008549
http://togogenome.org/gene/9606:OAS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29728                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  2'-5'-oligoadenylate synthase 2|||In isoform 3.|||In isoform p69.|||Loss of activity.|||Loss of activity; when associated with A-408.|||Loss of activity; when associated with A-410.|||Loss of activity; when associated with A-668 and A-669.|||Loss of activity; when associated with A-668 and A-670.|||Loss of activity; when associated with A-669 and A-670.|||N-myristoyl glycine|||N6-acetyllysine|||No loss of activity.|||OAS domain 1|||OAS domain 2|||Partial loss of activity.|||Removed|||Significant loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000160264|||http://purl.uniprot.org/annotation/VSP_003741|||http://purl.uniprot.org/annotation/VSP_003742|||http://purl.uniprot.org/annotation/VSP_043354|||http://purl.uniprot.org/annotation/VSP_043355
http://togogenome.org/gene/9606:PRG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13727                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic|||Acidic residues|||Bone marrow proteoglycan|||C-type lectin|||Disordered|||Eosinophil granule major basic protein|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||Interchain (with C-461 in PAPPA)|||Interchain (with C-732 in PAPPA)|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||O-linked (GalNAc...) threonine; partial|||O-linked (Xyl...) (chondroitin sulfate) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017385|||http://purl.uniprot.org/annotation/PRO_0000017386|||http://purl.uniprot.org/annotation/PRO_0000259923|||http://purl.uniprot.org/annotation/VAR_036401|||http://purl.uniprot.org/annotation/VAR_060729|||http://purl.uniprot.org/annotation/VSP_056735
http://togogenome.org/gene/9606:TMEM263                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WUH6                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 263                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263629
http://togogenome.org/gene/9606:VWA7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8T7|||http://purl.uniprot.org/uniprot/Q9Y334                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||VWFA|||von Willebrand factor A domain-containing protein 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000231631|||http://purl.uniprot.org/annotation/PRO_5010666571|||http://purl.uniprot.org/annotation/VAR_056884|||http://purl.uniprot.org/annotation/VAR_056885|||http://purl.uniprot.org/annotation/VAR_056886|||http://purl.uniprot.org/annotation/VAR_056887|||http://purl.uniprot.org/annotation/VAR_056888|||http://purl.uniprot.org/annotation/VAR_060378|||http://purl.uniprot.org/annotation/VSP_026494|||http://purl.uniprot.org/annotation/VSP_026495
http://togogenome.org/gene/9606:RNF222                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NCQ9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Region|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Disordered|||Helical|||RING finger protein 222|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329085
http://togogenome.org/gene/9606:CRX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43186                                                                                  ^@                                                                                  Chain|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Region|||Sequence Variant                                                                                  ^@                                                                                  Cone-rod homeobox protein|||Disordered|||Homeobox|||In CORD2.|||In CORD2; exhibits reduced DNA binding, transcriptional synergy and interaction with NRL.|||In LCA7.|||In LCA7; reduced DNA-binding ability, transcriptional synergy and interaction with NRL.|||In LCA7; reduces NRL transactivation and reduces steady state levels of CRX and NRL; altered localization to the cytoplasm.|||In LCA7; unknown pathological significance.|||In RP.|||In RP; unknown pathological significance.|||In a breast cancer sample; somatic mutation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048862|||http://purl.uniprot.org/annotation/VAR_003750|||http://purl.uniprot.org/annotation/VAR_003751|||http://purl.uniprot.org/annotation/VAR_007946|||http://purl.uniprot.org/annotation/VAR_007947|||http://purl.uniprot.org/annotation/VAR_007948|||http://purl.uniprot.org/annotation/VAR_007949|||http://purl.uniprot.org/annotation/VAR_008282|||http://purl.uniprot.org/annotation/VAR_008714|||http://purl.uniprot.org/annotation/VAR_036438|||http://purl.uniprot.org/annotation/VAR_063919|||http://purl.uniprot.org/annotation/VAR_067189|||http://purl.uniprot.org/annotation/VAR_067190|||http://purl.uniprot.org/annotation/VAR_076956|||http://purl.uniprot.org/annotation/VAR_076957|||http://purl.uniprot.org/annotation/VAR_076958
http://togogenome.org/gene/9606:CDIP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H305                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cell death-inducing p53-target protein 1|||Disordered|||In isoform 2.|||In isoform 3.|||LITAF|||Membrane-binding amphipathic helix|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280336|||http://purl.uniprot.org/annotation/VSP_046928|||http://purl.uniprot.org/annotation/VSP_046929
http://togogenome.org/gene/9606:TRIM41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WV44                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes E3 ligase activity.|||Acidic residues|||B box-type|||B30.2/SPRY|||Disordered|||E3 ubiquitin-protein ligase TRIM41|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||RING-type; degenerate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056262|||http://purl.uniprot.org/annotation/VAR_027914|||http://purl.uniprot.org/annotation/VAR_027915|||http://purl.uniprot.org/annotation/VSP_010395|||http://purl.uniprot.org/annotation/VSP_010396|||http://purl.uniprot.org/annotation/VSP_012515|||http://purl.uniprot.org/annotation/VSP_012516|||http://purl.uniprot.org/annotation/VSP_012517
http://togogenome.org/gene/9606:TMEM17                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X19                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a family diagnosed with orofaciodigital syndrome; unknown pathological significance; reduced cilia formation in patient fibroblasts compared to control.|||Helical|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 17                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255260|||http://purl.uniprot.org/annotation/VAR_028864|||http://purl.uniprot.org/annotation/VAR_075897
http://togogenome.org/gene/9606:CUX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P39880|||http://purl.uniprot.org/uniprot/Q13948|||http://purl.uniprot.org/uniprot/Q3LIA3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||CASP C-terminal|||CDP/Cux p110|||CUT 1|||CUT 2|||CUT 3|||Cleavage; by CTSL|||Cytoplasmic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Helical|||Helical; Anchor for type IV membrane protein|||Homeobox|||Homeobox protein cut-like 1|||In GDDI.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 10.|||In isoform 11.|||In isoform 2.|||In isoform 3 and isoform 11.|||In isoform 5 and isoform 7.|||In isoform 6 and isoform 7.|||In isoform 8 and isoform 9.|||In isoform 9.|||Lumenal|||No effect on subcellular location.|||Phosphoserine|||Polar residues|||Pro residues|||Protein CASP|||Retained in the endoplasmic reticulum.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071790|||http://purl.uniprot.org/annotation/PRO_0000202393|||http://purl.uniprot.org/annotation/PRO_0000450797|||http://purl.uniprot.org/annotation/VAR_024923|||http://purl.uniprot.org/annotation/VAR_024924|||http://purl.uniprot.org/annotation/VAR_036285|||http://purl.uniprot.org/annotation/VAR_036286|||http://purl.uniprot.org/annotation/VAR_081977|||http://purl.uniprot.org/annotation/VSP_002310|||http://purl.uniprot.org/annotation/VSP_015747|||http://purl.uniprot.org/annotation/VSP_017358|||http://purl.uniprot.org/annotation/VSP_017359|||http://purl.uniprot.org/annotation/VSP_040094|||http://purl.uniprot.org/annotation/VSP_045593|||http://purl.uniprot.org/annotation/VSP_045924|||http://purl.uniprot.org/annotation/VSP_045925|||http://purl.uniprot.org/annotation/VSP_045926|||http://purl.uniprot.org/annotation/VSP_045927
http://togogenome.org/gene/9606:UNCX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJT0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Homeobox|||Homeobox protein unc-4 homolog|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334624
http://togogenome.org/gene/9606:PDLIM7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR12                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Asymmetric dimethylarginine|||Basic and acidic residues|||Disordered|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||Loss of binding to TPM2.|||PDZ|||PDZ and LIM domain protein 7|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075881|||http://purl.uniprot.org/annotation/VAR_036193|||http://purl.uniprot.org/annotation/VAR_050168|||http://purl.uniprot.org/annotation/VSP_016509|||http://purl.uniprot.org/annotation/VSP_016510|||http://purl.uniprot.org/annotation/VSP_016511|||http://purl.uniprot.org/annotation/VSP_016512|||http://purl.uniprot.org/annotation/VSP_016513|||http://purl.uniprot.org/annotation/VSP_016514|||http://purl.uniprot.org/annotation/VSP_016515|||http://purl.uniprot.org/annotation/VSP_016516
http://togogenome.org/gene/9606:MAGEA12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43365                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 12|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156711|||http://purl.uniprot.org/annotation/VAR_053498
http://togogenome.org/gene/9606:ARL2BP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2Y0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ADP-ribosylation factor-like protein 2-binding protein|||Decreases interaction with ARL2.|||Does not decrease interaction with ARL2.|||In RP82; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287113|||http://purl.uniprot.org/annotation/VAR_053904|||http://purl.uniprot.org/annotation/VAR_070227|||http://purl.uniprot.org/annotation/VSP_025317|||http://purl.uniprot.org/annotation/VSP_025318
http://togogenome.org/gene/9606:UROS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z4T8|||http://purl.uniprot.org/uniprot/A0A0S2Z5C5|||http://purl.uniprot.org/uniprot/A0A3B3ISM6|||http://purl.uniprot.org/uniprot/A0A3B3ITJ2|||http://purl.uniprot.org/uniprot/P10746|||http://purl.uniprot.org/uniprot/Q5T3L8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Does not affect enzymatic activity.|||Impairs enzymatic activity.|||In CEP.|||In CEP; frequent mutation in Western countries; severe phenotype; loss of enzymatic activity, when tested in vitro.|||In CEP; less than 2% wild-type activity.|||In CEP; less than 5% wild-type activity.|||In CEP; loss of enzymatic activity, when tested in vitro.|||In CEP; mild phenotype; high residual activity.|||In CEP; mild phenotype; less than 2% wild-type activity.|||In CEP; mild phenotype; strong decrease in enzymatic activity, when tested in vitro; may affect thermal stability.|||In CEP; moderately-severe phenotype; less than 2% wild-type activity.|||In CEP; no residual activity.|||In CEP; residual activity.|||In CEP; severe cutaneous lesions; less than 3% wild-type activity.|||In CEP; severe phenotype; no detectable activity.|||In CEP; the effect on catalytic activity is controversial.|||Slightly affects enzymatic activity.|||Tetrapyrrole biosynthesis uroporphyrinogen III synthase|||Uroporphyrinogen-III synthase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135251|||http://purl.uniprot.org/annotation/VAR_003674|||http://purl.uniprot.org/annotation/VAR_003675|||http://purl.uniprot.org/annotation/VAR_003676|||http://purl.uniprot.org/annotation/VAR_003677|||http://purl.uniprot.org/annotation/VAR_003678|||http://purl.uniprot.org/annotation/VAR_003679|||http://purl.uniprot.org/annotation/VAR_003680|||http://purl.uniprot.org/annotation/VAR_003681|||http://purl.uniprot.org/annotation/VAR_003682|||http://purl.uniprot.org/annotation/VAR_003683|||http://purl.uniprot.org/annotation/VAR_003684|||http://purl.uniprot.org/annotation/VAR_003685|||http://purl.uniprot.org/annotation/VAR_013558|||http://purl.uniprot.org/annotation/VAR_021615|||http://purl.uniprot.org/annotation/VAR_021616|||http://purl.uniprot.org/annotation/VAR_021617|||http://purl.uniprot.org/annotation/VAR_021618|||http://purl.uniprot.org/annotation/VAR_021619|||http://purl.uniprot.org/annotation/VAR_021620|||http://purl.uniprot.org/annotation/VAR_021621|||http://purl.uniprot.org/annotation/VAR_049345|||http://purl.uniprot.org/annotation/VAR_049346|||http://purl.uniprot.org/annotation/VAR_066247|||http://purl.uniprot.org/annotation/VAR_067318
http://togogenome.org/gene/9606:NXF2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZY0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Repeat                                                                                  ^@                                                                                  Has no effect on FG-nucleoporin binding.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||NTF2|||Nuclear RNA export factor 2|||Phosphoserine|||RRM|||Suppresses FG-nucleoporin binding.|||TAP-C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220533
http://togogenome.org/gene/9606:SLC39A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZMH5                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolished histidine methylation by METTL9.|||Cytoplasmic|||Disordered|||Does not affect histidine methylation by METTL9.|||Extracellular|||Helical|||In MYP24; affects the BMP/TGF-beta pathway by suppressing expression of SMAD1; loss of function mutation.|||In MYP24; unknown pathological significance.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pros-methylhistidine|||Reduced histidine methylation by METTL9.|||Zinc transporter ZIP5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000045795|||http://purl.uniprot.org/annotation/VAR_071911|||http://purl.uniprot.org/annotation/VAR_074009
http://togogenome.org/gene/9606:MRPL57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQC6                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Strand|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein mL63                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000253541
http://togogenome.org/gene/9606:C12orf4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NQ89                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In MRT66.|||Protein C12orf4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089842|||http://purl.uniprot.org/annotation/VAR_081778|||http://purl.uniprot.org/annotation/VAR_081779
http://togogenome.org/gene/9606:MAPK1IP1L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NDC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||MAPK-interacting and spindle-stabilizing protein-like|||N-acetylserine|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000209890
http://togogenome.org/gene/9606:SSBP4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BWG4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||LisH|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Single-stranded DNA-binding protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123832|||http://purl.uniprot.org/annotation/VSP_054113
http://togogenome.org/gene/9606:SLC48A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P1K1                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Mutagenesis Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Di-leucine motif|||Helical|||Heme transporter HRG1|||In isoform 2.|||No effect on heme transport.|||Slightly decreases heme transport.|||Strongly decreases heme transport.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348575|||http://purl.uniprot.org/annotation/VSP_035184
http://togogenome.org/gene/9606:MVP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14764|||http://purl.uniprot.org/uniprot/X5D2M8|||http://purl.uniprot.org/uniprot/X5D7K9|||http://purl.uniprot.org/uniprot/X5DNU0                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||MVP|||MVP 1|||MVP 2|||MVP 3|||MVP 4|||MVP 5|||MVP 6|||MVP 7|||MVP 8|||MVP 9|||Major vault protein|||Major vault protein repeat|||Major vault protein shoulder|||N-acetylalanine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158980|||http://purl.uniprot.org/annotation/VAR_050179|||http://purl.uniprot.org/annotation/VAR_050180|||http://purl.uniprot.org/annotation/VAR_079710
http://togogenome.org/gene/9606:APOBEC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P41238                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  C->U-editing enzyme APOBEC-1|||CMP/dCMP-type deaminase|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171742|||http://purl.uniprot.org/annotation/VAR_013779|||http://purl.uniprot.org/annotation/VAR_048720
http://togogenome.org/gene/9606:ITPRID1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUB1|||http://purl.uniprot.org/uniprot/Q6ZRS4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ITPR-interacting|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Polar residues|||Protein ITPRID1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000270963|||http://purl.uniprot.org/annotation/VAR_033660|||http://purl.uniprot.org/annotation/VAR_033661|||http://purl.uniprot.org/annotation/VAR_033662|||http://purl.uniprot.org/annotation/VAR_033663|||http://purl.uniprot.org/annotation/VAR_035496|||http://purl.uniprot.org/annotation/VAR_063505|||http://purl.uniprot.org/annotation/VSP_039586|||http://purl.uniprot.org/annotation/VSP_039587|||http://purl.uniprot.org/annotation/VSP_045000|||http://purl.uniprot.org/annotation/VSP_045001
http://togogenome.org/gene/9606:EPX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11678                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  3'-nitrotyrosine|||Associated with Japanese cedar pollinosis.|||Eosinophil peroxidase heavy chain|||Eosinophil peroxidase light chain|||In EPXD.|||N-linked (GlcNAc...) asparagine|||Proton acceptor|||Transition state stabilizer|||axial binding residue|||covalent|||covalent; partial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000023639|||http://purl.uniprot.org/annotation/PRO_0000023640|||http://purl.uniprot.org/annotation/PRO_0000023641|||http://purl.uniprot.org/annotation/VAR_015376|||http://purl.uniprot.org/annotation/VAR_020031|||http://purl.uniprot.org/annotation/VAR_025138|||http://purl.uniprot.org/annotation/VAR_025139|||http://purl.uniprot.org/annotation/VAR_025140|||http://purl.uniprot.org/annotation/VAR_025141|||http://purl.uniprot.org/annotation/VAR_025142|||http://purl.uniprot.org/annotation/VAR_025143|||http://purl.uniprot.org/annotation/VAR_025144|||http://purl.uniprot.org/annotation/VAR_025145|||http://purl.uniprot.org/annotation/VAR_025146|||http://purl.uniprot.org/annotation/VAR_025147|||http://purl.uniprot.org/annotation/VAR_050485|||http://purl.uniprot.org/annotation/VAR_050486|||http://purl.uniprot.org/annotation/VAR_060197|||http://purl.uniprot.org/annotation/VAR_060198
http://togogenome.org/gene/9606:ZNF346                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z4J8|||http://purl.uniprot.org/uniprot/B7Z4N4|||http://purl.uniprot.org/uniprot/Q9UL40                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Matrin-type 1|||Matrin-type 2|||Matrin-type 3|||Matrin-type 4|||N-acetylmethionine|||Zinc finger protein 346                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191809|||http://purl.uniprot.org/annotation/VSP_015971|||http://purl.uniprot.org/annotation/VSP_055098
http://togogenome.org/gene/9606:C7orf25                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BPX7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||UPF0415 protein C7orf25                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279529|||http://purl.uniprot.org/annotation/VAR_053848|||http://purl.uniprot.org/annotation/VSP_047243
http://togogenome.org/gene/9606:STX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15400                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Syntaxin-7|||Vesicular|||t-SNARE coiled-coil homology                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210213|||http://purl.uniprot.org/annotation/VSP_012938
http://togogenome.org/gene/9606:KPLCE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T750                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Protein KPLCE                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307808|||http://purl.uniprot.org/annotation/VAR_059739|||http://purl.uniprot.org/annotation/VAR_059740|||http://purl.uniprot.org/annotation/VAR_061726
http://togogenome.org/gene/9606:TLE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KUA2|||http://purl.uniprot.org/uniprot/H0YL70|||http://purl.uniprot.org/uniprot/Q04726|||http://purl.uniprot.org/uniprot/Q6PRX3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||CcN domain|||Disordered|||GP domain|||Groucho/TLE N-terminal Q-rich|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3, isoform 5 and isoform 7.|||In isoform 4.|||In isoform 6.|||In isoform 7.|||N6-acetyllysine|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Q domain|||SP domain|||Transducin-like enhancer protein 3|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051280|||http://purl.uniprot.org/annotation/VAR_053421|||http://purl.uniprot.org/annotation/VSP_006788|||http://purl.uniprot.org/annotation/VSP_006789|||http://purl.uniprot.org/annotation/VSP_006790|||http://purl.uniprot.org/annotation/VSP_007023|||http://purl.uniprot.org/annotation/VSP_007024|||http://purl.uniprot.org/annotation/VSP_054598|||http://purl.uniprot.org/annotation/VSP_055168
http://togogenome.org/gene/9606:GDF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NR23                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Growth/differentiation factor 3|||In KFS3 and MCOPCB6; reduces the amount of active ligand secreted; reduced amout of mature protein in the cytosol.|||In MCOP7; also detected in a patient with bilateral iris coloboma; reduces the amount of active ligand secreted.|||In MCOP7; reduces the amount of active ligand secreted.|||In MCOPCB6.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000033908|||http://purl.uniprot.org/annotation/PRO_0000033909|||http://purl.uniprot.org/annotation/VAR_020064|||http://purl.uniprot.org/annotation/VAR_052574|||http://purl.uniprot.org/annotation/VAR_065147|||http://purl.uniprot.org/annotation/VAR_065148|||http://purl.uniprot.org/annotation/VAR_065149|||http://purl.uniprot.org/annotation/VAR_065150
http://togogenome.org/gene/9606:FBLN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P98095|||http://purl.uniprot.org/uniprot/Q86V58|||http://purl.uniprot.org/uniprot/Q9Y3V7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Anaphylatoxin-like|||Anaphylatoxin-like 1|||Anaphylatoxin-like 2|||Anaphylatoxin-like 3|||Basic and acidic residues|||Disordered|||Domain III|||EGF-like|||EGF-like 10; calcium-binding|||EGF-like 1; calcium-binding|||EGF-like 2|||EGF-like 3; calcium-binding|||EGF-like 4; calcium-binding|||EGF-like 5; calcium-binding|||EGF-like 6; calcium-binding|||EGF-like 7; calcium-binding|||EGF-like 8; calcium-binding|||EGF-like 9; calcium-binding|||Fibulin-2|||In isoform 2.|||N|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Subdomain NA (Cys-rich)|||Subdomain NB (Cys-free)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007568|||http://purl.uniprot.org/annotation/PRO_5004300515|||http://purl.uniprot.org/annotation/VAR_055722|||http://purl.uniprot.org/annotation/VAR_059266|||http://purl.uniprot.org/annotation/VAR_059267|||http://purl.uniprot.org/annotation/VAR_059268|||http://purl.uniprot.org/annotation/VAR_061159|||http://purl.uniprot.org/annotation/VAR_061160|||http://purl.uniprot.org/annotation/VSP_041404
http://togogenome.org/gene/9606:GABARAPL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0R8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Lipid Binding|||Mutagenesis Site|||Propeptide|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  (Microbial infection) Cleavage; by RavZ|||Abolished interaction with ATG4B.|||Cleavage; by ATG4B|||Does not affect interaction with ATG4B.|||Gamma-aminobutyric acid receptor-associated protein-like 1|||In isoform 2.|||No processing of precursor.|||Phosphatidylethanolamine amidated glycine; alternate|||Phosphatidylserine amidated glycine; alternate|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000212369|||http://purl.uniprot.org/annotation/PRO_0000420208|||http://purl.uniprot.org/annotation/VSP_044422
http://togogenome.org/gene/9606:KRTAP11-1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IUC1                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Variant                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 10 AA approximate repeats|||Keratin-associated protein 11-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185194|||http://purl.uniprot.org/annotation/VAR_053467
http://togogenome.org/gene/9606:ARHGAP10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A2X0SFB3|||http://purl.uniprot.org/uniprot/A1A4S6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Strand                                                                                  ^@                                                                                  BAR|||Disordered|||PH|||Polar residues|||Rho GTPase-activating protein 10|||Rho-GAP|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000304914|||http://purl.uniprot.org/annotation/VAR_035114|||http://purl.uniprot.org/annotation/VAR_049141
http://togogenome.org/gene/9606:POLR3GL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGX6|||http://purl.uniprot.org/uniprot/Q9BT43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA-directed RNA polymerase III subunit RPC7-like|||Disordered|||In SOFM; unknown pathological significance; decrease in transcript levels, possibly due to nonsense-mediated mRNA decay.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311590|||http://purl.uniprot.org/annotation/VAR_085496
http://togogenome.org/gene/9606:RPL35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P42766                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In DBA19; unknown pathological significance.|||Large ribosomal subunit protein uL29|||N6-acetyllysine|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000130533|||http://purl.uniprot.org/annotation/VAR_081936
http://togogenome.org/gene/9606:OR4S2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVG1|||http://purl.uniprot.org/uniprot/Q8NH73                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 4S2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150569|||http://purl.uniprot.org/annotation/VAR_057547|||http://purl.uniprot.org/annotation/VAR_057548
http://togogenome.org/gene/9606:WDR72                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTC3|||http://purl.uniprot.org/uniprot/Q3MJ13                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Phosphoserine|||Polar residues|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD repeat-containing protein 72                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000241447|||http://purl.uniprot.org/annotation/VAR_026837|||http://purl.uniprot.org/annotation/VAR_026838|||http://purl.uniprot.org/annotation/VAR_057633|||http://purl.uniprot.org/annotation/VAR_057634|||http://purl.uniprot.org/annotation/VAR_060045|||http://purl.uniprot.org/annotation/VAR_062106
http://togogenome.org/gene/9606:GALNT11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7X6|||http://purl.uniprot.org/uniprot/B7Z5G5|||http://purl.uniprot.org/uniprot/Q8NCW6                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes glycosyltransferase activity and ability to rescue left-right patterning defects induced by galnt11 knockdown in X.tropicalis.|||Catalytic subdomain A|||Catalytic subdomain B|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polypeptide N-acetylgalactosaminyltransferase 11|||Ricin B lectin|||Ricin B-type lectin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000059125|||http://purl.uniprot.org/annotation/VAR_019589|||http://purl.uniprot.org/annotation/VAR_019590|||http://purl.uniprot.org/annotation/VSP_011215|||http://purl.uniprot.org/annotation/VSP_011216
http://togogenome.org/gene/9606:CLOCK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15516|||http://purl.uniprot.org/uniprot/Q3ZCT4|||http://purl.uniprot.org/uniprot/Q53EU0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand                                                                                  ^@                                                                                  3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity.|||3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity; when associated with E-116 and L-601.|||3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity; when associated with E-332.|||3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity; when associated with K-116 and K-367.|||3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity; when associated with K-367 and L-601.|||3-fold increase in PER1 reporter activity by CLOCK-BMAL1. Some reduction of CRY1 inhibition of CLOCK-BMAL1 transcriptional activity; when associated with L-840.|||BHLH|||Circadian locomoter output cycles protein kaput|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Impaired BMAL1 binding.|||Implicated in the circadian rhythmicity|||Important for interaction with BMAL1|||Interaction with E-box DNA|||Interaction with NR3C1|||Interaction with SIRT1|||No effect on BMAL1 binding.|||Nuclear localization signal|||PAC|||PAS|||PAS 1|||PAS 2|||Phosphomimetic mutant with no effect on DNA binding or CLOCK-BMAL1 transcriptional activity.|||Phosphoserine|||Phosphoserine; by GSK3-beta|||Phosphothreonine; by CDK5|||Polar residues|||Significant loss in phosphorylation.|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127163|||http://purl.uniprot.org/annotation/VAR_029076|||http://purl.uniprot.org/annotation/VAR_029077|||http://purl.uniprot.org/annotation/VAR_040061|||http://purl.uniprot.org/annotation/VAR_040062
http://togogenome.org/gene/9606:ADRA2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P18089                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Lipid Binding|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Acidic residues|||Alpha-2B adrenergic receptor|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Found with a frequency of 0.31 in Caucasians and 0.12 in African-Americans; exhibits impaired phosphorylation and desensitization by G protein-coupled receptor kinases; does not affect ligand-binding.|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Implicated in catechol agonist binding|||Implicated in ligand binding|||In FAME2; gain of function; decreases interaction with PPP1R9B upon activation by neurotransmitter.|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069094|||http://purl.uniprot.org/annotation/VAR_025099|||http://purl.uniprot.org/annotation/VAR_025100|||http://purl.uniprot.org/annotation/VAR_033462|||http://purl.uniprot.org/annotation/VAR_033463|||http://purl.uniprot.org/annotation/VAR_070775|||http://purl.uniprot.org/annotation/VAR_073953
http://togogenome.org/gene/9606:RXFP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXD0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In CRYPTO; functionally inactive.|||In isoform 2.|||LDL-receptor class A|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leads to constitutive increase of basal cAMP.|||N-linked (GlcNAc...) asparagine|||Relaxin receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069702|||http://purl.uniprot.org/annotation/VAR_015386|||http://purl.uniprot.org/annotation/VAR_015387|||http://purl.uniprot.org/annotation/VSP_042831
http://togogenome.org/gene/9606:CYP3A5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z3P6|||http://purl.uniprot.org/uniprot/P20815                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cytochrome P450 3A|||Cytochrome P450 3A5|||In allele CYP3A5*2.|||In allele CYP3A5*4.|||In allele CYP3A5*8.|||In allele CYP3A5*9.|||In isoform 2.|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051787|||http://purl.uniprot.org/annotation/PRO_5002863874|||http://purl.uniprot.org/annotation/VAR_008365|||http://purl.uniprot.org/annotation/VAR_024728|||http://purl.uniprot.org/annotation/VAR_024729|||http://purl.uniprot.org/annotation/VAR_024730|||http://purl.uniprot.org/annotation/VAR_024731|||http://purl.uniprot.org/annotation/VAR_024732|||http://purl.uniprot.org/annotation/VAR_024733|||http://purl.uniprot.org/annotation/VAR_029161|||http://purl.uniprot.org/annotation/VAR_029162|||http://purl.uniprot.org/annotation/VSP_042734|||http://purl.uniprot.org/annotation/VSP_042735
http://togogenome.org/gene/9606:APOC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R0T9|||http://purl.uniprot.org/uniprot/P02655                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Apolipoprotein C-II|||In Africa.|||In HLPP1B; variant Wakayama.|||In San Francisco; found in hyperlipidemic patients.|||Lipid binding|||Lipoprotein lipase cofactor|||O-glycosylated at one site|||Proapolipoprotein C-II                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002024|||http://purl.uniprot.org/annotation/PRO_0000430839|||http://purl.uniprot.org/annotation/PRO_5014214194|||http://purl.uniprot.org/annotation/VAR_000639|||http://purl.uniprot.org/annotation/VAR_000640|||http://purl.uniprot.org/annotation/VAR_000641|||http://purl.uniprot.org/annotation/VAR_000642
http://togogenome.org/gene/9606:SLC16A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60669                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||May be protonated during monocarboxylate transport|||Monocarboxylate transporter 2|||No effect on protein abundance. Does not affect cell surface localization.|||Polar residues|||Reduced proton-dependent active symport, but not pyruvate transport.|||Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.|||Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization. Dominant negative mutant.|||Reduces pyruvate transmembrane transporter activity. Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization.|||Reduces pyruvate transmembrane transporter activity. Reduces pyruvate transmembrane transporter activity. No effect on protein abundance. Does not affect cell surface localization. Dominant negative mutant.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211385|||http://purl.uniprot.org/annotation/VAR_031660
http://togogenome.org/gene/9606:ZNF771                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R9V3|||http://purl.uniprot.org/uniprot/Q7L3S4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Zinc finger protein 771                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280439|||http://purl.uniprot.org/annotation/VAR_031150
http://togogenome.org/gene/9606:HAUS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NVX0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  HAUS augmin-like complex subunit 2|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089484|||http://purl.uniprot.org/annotation/VAR_050793|||http://purl.uniprot.org/annotation/VSP_012223|||http://purl.uniprot.org/annotation/VSP_040918
http://togogenome.org/gene/9606:DDX31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H8H2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||DEAD box|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Omega-N-methylarginine|||Polar residues|||Probable ATP-dependent RNA helicase DDX31|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055049|||http://purl.uniprot.org/annotation/VAR_023065|||http://purl.uniprot.org/annotation/VAR_023066|||http://purl.uniprot.org/annotation/VAR_052164|||http://purl.uniprot.org/annotation/VAR_052165|||http://purl.uniprot.org/annotation/VSP_014787|||http://purl.uniprot.org/annotation/VSP_014788|||http://purl.uniprot.org/annotation/VSP_014789|||http://purl.uniprot.org/annotation/VSP_014790
http://togogenome.org/gene/9606:DES                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P17661|||http://purl.uniprot.org/uniprot/Q53SB5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  ADP-ribosylarginine|||Asymmetric dimethylarginine; alternate|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Desmin|||Does not result in impaired filaments formation.|||Found in a patient with severe arrhythmogenic right ventricular cardiomyopathy; unknown pathological significance; the patient also carries a frameshift mutation in PKP2.|||Head|||IF rod|||In CMD1I and MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; reduced interaction with CRYAB.|||In CMD1I; results in impaired filaments formation, does not localize at intercalated disks.|||In CMD1I; unknown pathological significance; does not affect filaments formation.|||In CMD1I; unknown pathological significance; impaired subcellular localization.|||In Kaeser syndrome and MFM1; incapable of de novo formation of a desmin intermediate filaments network; exerts a dominant negative effect on the ordered lateral arrangement of desmin subunits; may produce structural changes; forms subsarcolemmal aggregates.|||In MFM1.|||In MFM1; distal onset; incapable of forming filamentous networks.|||In MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB and NEBL; enhanced binding affinity towards NEB and NEBL.|||In MFM1; exhibits significantly delayed filament assembly kinetics when bound to NEB; enhanced binding affinity towards NEB.|||In MFM1; found in a family with myofibrillar myopathy and arrhythmogenic right ventricular cardiomyopathy.|||In MFM1; heterozygous with I-393 gives a severe childhood-onset; unable to form a functional filamentous network in the presence of I-393; abolishes binding to MTM1.|||In MFM1; heterozygous with P-360 gives a severe childhood-onset; filamentous network is not affected however several spots indicate focal disorganization.|||In MFM1; mild adult-onset; unable to form a functional filamentous network.|||In MFM1; results in the formation of a filamentous network disrupted by multiple breaks and clumps or large aggregates.|||In MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions.|||In MFM1; reveals a severe disturbance of filament-formation competence and filament-filament interactions; increased interaction with CRYAB.|||In MFM1; severe form.|||In MFM1; some patients manifest a severe cardiac phenotype with right ventricular predominance.|||In MFM1; the clinical picture is dominated by arrhythmogenic right ventricular cardiomyopathy and terminal heart failure; results in impaired filaments formation.|||In MFM1; the mutant cannot form de novo desmin intermediate filaments causing disruption of the endogenous intermediate filament network and formation of pathologic aggregates.|||In MFM1; unable to form a filamentous network.|||In MFM1; unable to form a filamentous network; abolishes binding to MTM1.|||In MFM1; unable to polymerize and form an intracellular filamentous network; abolishes binding to MTM1.|||In MFM1; unable to polymerize and form an intracellular filamentous network; does not affect binding to MTM1.|||Interaction with CRYAB|||Interaction with NEB|||Linker 1|||Linker 12|||Linker 2|||May play a role in cardiomyopathies and distal myopathies if combined with other DES mutations or mutations in other genes; does not affect the formation of a normal complete filamentous network.|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by AURKB|||Phosphoserine; by CDK1|||Phosphothreonine; by AURKB and ROCK1|||Phosphothreonine; by ROCK1|||Removed|||Results in impaired filaments formation.|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063771|||http://purl.uniprot.org/annotation/VAR_007900|||http://purl.uniprot.org/annotation/VAR_007901|||http://purl.uniprot.org/annotation/VAR_007902|||http://purl.uniprot.org/annotation/VAR_009188|||http://purl.uniprot.org/annotation/VAR_009189|||http://purl.uniprot.org/annotation/VAR_018769|||http://purl.uniprot.org/annotation/VAR_018770|||http://purl.uniprot.org/annotation/VAR_018771|||http://purl.uniprot.org/annotation/VAR_018772|||http://purl.uniprot.org/annotation/VAR_018773|||http://purl.uniprot.org/annotation/VAR_042448|||http://purl.uniprot.org/annotation/VAR_042449|||http://purl.uniprot.org/annotation/VAR_042450|||http://purl.uniprot.org/annotation/VAR_042451|||http://purl.uniprot.org/annotation/VAR_042452|||http://purl.uniprot.org/annotation/VAR_042453|||http://purl.uniprot.org/annotation/VAR_042454|||http://purl.uniprot.org/annotation/VAR_042455|||http://purl.uniprot.org/annotation/VAR_042456|||http://purl.uniprot.org/annotation/VAR_042457|||http://purl.uniprot.org/annotation/VAR_042458|||http://purl.uniprot.org/annotation/VAR_042459|||http://purl.uniprot.org/annotation/VAR_042460|||http://purl.uniprot.org/annotation/VAR_042461|||http://purl.uniprot.org/annotation/VAR_042462|||http://purl.uniprot.org/annotation/VAR_042463|||http://purl.uniprot.org/annotation/VAR_067207|||http://purl.uniprot.org/annotation/VAR_067208|||http://purl.uniprot.org/annotation/VAR_067209|||http://purl.uniprot.org/annotation/VAR_067210|||http://purl.uniprot.org/annotation/VAR_067211|||http://purl.uniprot.org/annotation/VAR_069074|||http://purl.uniprot.org/annotation/VAR_069191|||http://purl.uniprot.org/annotation/VAR_069192|||http://purl.uniprot.org/annotation/VAR_070101|||http://purl.uniprot.org/annotation/VAR_075228|||http://purl.uniprot.org/annotation/VAR_075229|||http://purl.uniprot.org/annotation/VAR_075230|||http://purl.uniprot.org/annotation/VAR_079048|||http://purl.uniprot.org/annotation/VAR_079049|||http://purl.uniprot.org/annotation/VAR_086534
http://togogenome.org/gene/9606:EIF2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F8WAE5|||http://purl.uniprot.org/uniprot/Q9BY44                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Eukaryotic translation initiation factor 2A|||Eukaryotic translation initiation factor 2A, N-terminally processed|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine; in Eukaryotic translation initiation factor 2A, N-terminally processed|||N-acetylmethionine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed; alternate|||Translation initiation factor beta propellor-like|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286076|||http://purl.uniprot.org/annotation/PRO_0000424466|||http://purl.uniprot.org/annotation/VAR_032066|||http://purl.uniprot.org/annotation/VAR_032067|||http://purl.uniprot.org/annotation/VSP_024975|||http://purl.uniprot.org/annotation/VSP_024976|||http://purl.uniprot.org/annotation/VSP_056047|||http://purl.uniprot.org/annotation/VSP_056048
http://togogenome.org/gene/9606:PIWIL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TC59|||http://purl.uniprot.org/uniprot/W0HK13                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; by PRMT5; alternate|||PAZ|||Piwi|||Piwi-like protein 2|||Pro residues|||Symmetric dimethylarginine|||Symmetric dimethylarginine; alternate|||Symmetric dimethylarginine; by PRMT5|||Symmetric dimethylarginine; by PRMT5; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234569|||http://purl.uniprot.org/annotation/VSP_036664
http://togogenome.org/gene/9606:PI4K2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E9Z4|||http://purl.uniprot.org/uniprot/Q8TCG2                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Activation loop|||Basic and acidic residues|||Catalytic loop|||Disordered|||G-loop|||Important for interaction with membranes|||Important for substrate binding|||Increased localization to plasma membrane.|||PI3K/PI4K catalytic|||Phosphatidylinositol 4-kinase type 2-beta|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000285164|||http://purl.uniprot.org/annotation/VAR_031974
http://togogenome.org/gene/9606:MED26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95402                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Mediator of RNA polymerase II transcription subunit 26|||Phosphoserine|||Polar residues|||TFIIS N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000079360|||http://purl.uniprot.org/annotation/VSP_028151|||http://purl.uniprot.org/annotation/VSP_028152
http://togogenome.org/gene/9606:TBXA2R                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21731|||http://purl.uniprot.org/uniprot/Q05C92|||http://purl.uniprot.org/uniprot/Q0VAB0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In BDPLT13; does not affect TXA2 binding; defective interaction with G proteins; impairs phospholipase C and adenylyl cyclase activation; isoform 1; has no effect on adenylyl cyclase inhibition; isoform 2.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Pro residues|||Reduces antagonist binding.|||Suppresses antagonist binding.|||Thromboxane A2 receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070138|||http://purl.uniprot.org/annotation/VAR_003515|||http://purl.uniprot.org/annotation/VAR_014688|||http://purl.uniprot.org/annotation/VAR_014689|||http://purl.uniprot.org/annotation/VAR_014690|||http://purl.uniprot.org/annotation/VAR_014691|||http://purl.uniprot.org/annotation/VAR_014692|||http://purl.uniprot.org/annotation/VAR_014693|||http://purl.uniprot.org/annotation/VSP_001925
http://togogenome.org/gene/9606:SPCS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15005                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Lumenal|||N-acetylalanine|||N6-acetyllysine|||Removed|||Signal peptidase complex subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000221158
http://togogenome.org/gene/9606:CEND1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N111                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cell cycle exit and neuronal differentiation protein 1|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Anchor for type IV membrane protein|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064951
http://togogenome.org/gene/9606:CALD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VKA0|||http://purl.uniprot.org/uniprot/Q05682                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  1|||2|||3|||3 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-I-K|||Basic and acidic residues|||Caldesmon|||Calmodulin-binding|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2, isoform 3 and isoform 6.|||In isoform 3 and isoform 5.|||In isoform 4 and isoform 5.|||In isoform 6.|||Myosin and calmodulin-binding|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Strong actin-binding|||Tropomyosin-binding|||Weak actin-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000089288|||http://purl.uniprot.org/annotation/VAR_065254|||http://purl.uniprot.org/annotation/VSP_004154|||http://purl.uniprot.org/annotation/VSP_004155|||http://purl.uniprot.org/annotation/VSP_004156|||http://purl.uniprot.org/annotation/VSP_043292
http://togogenome.org/gene/9606:GMPR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H0YNJ6|||http://purl.uniprot.org/uniprot/Q6PKC0|||http://purl.uniprot.org/uniprot/Q9P2T1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  GMP reductase 2|||IMP dehydrogenase/GMP reductase|||In isoform 2.|||In isoform 3.|||Loss of enzyme activity.|||N6-acetyllysine|||Proton acceptor|||Proton donor/acceptor|||Thioimidate intermediate|||in other chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093726|||http://purl.uniprot.org/annotation/VAR_049602|||http://purl.uniprot.org/annotation/VSP_041459|||http://purl.uniprot.org/annotation/VSP_054585
http://togogenome.org/gene/9606:PTDSS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P48651                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Cytoplasmic|||Disordered|||Helical|||In LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine.|||In isoform 2.|||In isoform 3.|||Lumenal|||N-acetylalanine|||Phosphatidylserine synthase 1|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056829|||http://purl.uniprot.org/annotation/VAR_048735|||http://purl.uniprot.org/annotation/VAR_070987|||http://purl.uniprot.org/annotation/VAR_070988|||http://purl.uniprot.org/annotation/VAR_070989|||http://purl.uniprot.org/annotation/VSP_055980|||http://purl.uniprot.org/annotation/VSP_057421|||http://purl.uniprot.org/annotation/VSP_057422
http://togogenome.org/gene/9606:TIMM10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62072                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Motif|||Strand|||Turn                                                                                  ^@                                                                                  Mitochondrial import inner membrane translocase subunit Tim10|||Twin CX3C motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193612
http://togogenome.org/gene/9606:RPL22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35268                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue                                                                                  ^@                                                                                  Large ribosomal subunit protein eL22|||N6-succinyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215501
http://togogenome.org/gene/9606:TRAPPC14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KNS5|||http://purl.uniprot.org/uniprot/Q8WVR3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In MCPH25.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Trafficking protein particle complex subunit 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280344|||http://purl.uniprot.org/annotation/VAR_050817|||http://purl.uniprot.org/annotation/VAR_081463|||http://purl.uniprot.org/annotation/VSP_023633|||http://purl.uniprot.org/annotation/VSP_023634|||http://purl.uniprot.org/annotation/VSP_023635|||http://purl.uniprot.org/annotation/VSP_023636|||http://purl.uniprot.org/annotation/VSP_023637
http://togogenome.org/gene/9606:CCDC125                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DSR1|||http://purl.uniprot.org/uniprot/Q86Z20                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Coiled-coil domain-containing protein 125|||Disordered|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288812|||http://purl.uniprot.org/annotation/VAR_032505|||http://purl.uniprot.org/annotation/VSP_025781
http://togogenome.org/gene/9606:MOB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y3A3                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||MOB-like protein phocein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193576|||http://purl.uniprot.org/annotation/VSP_012303|||http://purl.uniprot.org/annotation/VSP_041091
http://togogenome.org/gene/9606:SIPA1L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2F8                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||PDZ|||Phosphoserine|||Polar residues|||Rap-GAP|||Signal-induced proliferation-associated 1-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056749|||http://purl.uniprot.org/annotation/VAR_049153|||http://purl.uniprot.org/annotation/VAR_049154|||http://purl.uniprot.org/annotation/VAR_049155|||http://purl.uniprot.org/annotation/VAR_049156|||http://purl.uniprot.org/annotation/VAR_061183|||http://purl.uniprot.org/annotation/VSP_010920|||http://purl.uniprot.org/annotation/VSP_010921|||http://purl.uniprot.org/annotation/VSP_010922
http://togogenome.org/gene/9606:MYH6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13533                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Actin-binding|||Disordered|||IQ|||In ASD3.|||In CMD1EE.|||In CMD1EE; unknown pathological significance.|||In CMH14.|||In CMH14; late onset.|||In SSS3; rare variant predisposing to sick sinus syndrome.|||Myosin N-terminal SH3-like|||Myosin motor|||Myosin-6|||N6,N6,N6-trimethyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000123401|||http://purl.uniprot.org/annotation/VAR_030203|||http://purl.uniprot.org/annotation/VAR_030204|||http://purl.uniprot.org/annotation/VAR_030205|||http://purl.uniprot.org/annotation/VAR_030206|||http://purl.uniprot.org/annotation/VAR_031882|||http://purl.uniprot.org/annotation/VAR_031883|||http://purl.uniprot.org/annotation/VAR_061364|||http://purl.uniprot.org/annotation/VAR_063550|||http://purl.uniprot.org/annotation/VAR_063551|||http://purl.uniprot.org/annotation/VAR_063552|||http://purl.uniprot.org/annotation/VAR_063553|||http://purl.uniprot.org/annotation/VAR_063554|||http://purl.uniprot.org/annotation/VAR_063555|||http://purl.uniprot.org/annotation/VAR_063556|||http://purl.uniprot.org/annotation/VAR_063557|||http://purl.uniprot.org/annotation/VAR_063558|||http://purl.uniprot.org/annotation/VAR_065561
http://togogenome.org/gene/9606:CHGA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G5E968|||http://purl.uniprot.org/uniprot/P10645|||http://purl.uniprot.org/uniprot/Q86T07                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Peptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Peptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  AL-11|||Acidic residues|||Arginine amide|||Basic and acidic residues|||Catestatin|||Chromogranin-A|||Disordered|||EA-92|||ER-37|||ES-43|||GE-25|||GR-44|||GV-19|||Glycine amide|||Increases activity 2.3 fold; decrease in plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro.|||LF-19|||May be associated with a reduced risk for hypertension especially in men; reduces activity 4.7 fold; no effect on plasmin-mediated proteolytic processing; increase in ability to inhibit nicotine-evoked catecholamine secretion in vitro; displays alterations in baroreceptor function.|||Methionine sulfoxide|||No effect on plasmin-mediated proteolytic processing; decrease in ability to inhibit nicotine-evoked catecholamine secretion in vitro.|||O-glycosylated at one site only in cerebrospinal fluid|||O-linked (GalNAc...) threonine|||O-linked (Xyl...) (chondroitin sulfate) serine|||Pancreastatin|||Phosphoserine|||Phosphotyrosine|||Polar residues|||SS-18|||Serpinin|||Serpinin-RRG|||Vasostatin-1|||Vasostatin-2|||WA-8|||WE-14|||p-Glu serpinin precursor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000116|||http://purl.uniprot.org/annotation/CAR_000117|||http://purl.uniprot.org/annotation/CAR_000118|||http://purl.uniprot.org/annotation/PRO_0000005408|||http://purl.uniprot.org/annotation/PRO_0000005409|||http://purl.uniprot.org/annotation/PRO_0000005410|||http://purl.uniprot.org/annotation/PRO_0000005411|||http://purl.uniprot.org/annotation/PRO_0000005412|||http://purl.uniprot.org/annotation/PRO_0000005413|||http://purl.uniprot.org/annotation/PRO_0000005414|||http://purl.uniprot.org/annotation/PRO_0000005415|||http://purl.uniprot.org/annotation/PRO_0000005416|||http://purl.uniprot.org/annotation/PRO_0000005417|||http://purl.uniprot.org/annotation/PRO_0000005418|||http://purl.uniprot.org/annotation/PRO_0000005419|||http://purl.uniprot.org/annotation/PRO_0000005420|||http://purl.uniprot.org/annotation/PRO_0000005421|||http://purl.uniprot.org/annotation/PRO_0000432682|||http://purl.uniprot.org/annotation/PRO_0000432683|||http://purl.uniprot.org/annotation/PRO_0000432684|||http://purl.uniprot.org/annotation/PRO_0000432685|||http://purl.uniprot.org/annotation/PRO_0000432686|||http://purl.uniprot.org/annotation/PRO_5014092027|||http://purl.uniprot.org/annotation/VAR_025636|||http://purl.uniprot.org/annotation/VAR_025637|||http://purl.uniprot.org/annotation/VAR_025638|||http://purl.uniprot.org/annotation/VAR_025639|||http://purl.uniprot.org/annotation/VAR_025640|||http://purl.uniprot.org/annotation/VAR_025641|||http://purl.uniprot.org/annotation/VAR_025642|||http://purl.uniprot.org/annotation/VAR_025643|||http://purl.uniprot.org/annotation/VAR_025644|||http://purl.uniprot.org/annotation/VAR_025645|||http://purl.uniprot.org/annotation/VAR_047417|||http://purl.uniprot.org/annotation/VAR_072687
http://togogenome.org/gene/9606:HPS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3U9|||http://purl.uniprot.org/uniprot/A0A8V8TMQ9|||http://purl.uniprot.org/uniprot/A0A8V8TN94|||http://purl.uniprot.org/uniprot/H0Y4K4|||http://purl.uniprot.org/uniprot/Q658M9|||http://purl.uniprot.org/uniprot/Q92902                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Motif|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BLOC-3 complex member HPS1|||Disordered|||FUZ/MON1/HPS1 first Longin|||FUZ/MON1/HPS1 second Longin|||FUZ/MON1/HPS1 third Longin|||In HPS1; mild.|||In isoform II.|||In isoform III.|||In isoform IV.|||Melanosome targeting signal|||Polar residues|||[DE]-X(4)-L-L 1|||[DE]-X(4)-L-L 2|||[DE]-X(4)-L-L 3|||[DE]-X(4)-L-L 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084047|||http://purl.uniprot.org/annotation/VAR_005290|||http://purl.uniprot.org/annotation/VAR_005291|||http://purl.uniprot.org/annotation/VAR_005292|||http://purl.uniprot.org/annotation/VAR_005293|||http://purl.uniprot.org/annotation/VAR_007950|||http://purl.uniprot.org/annotation/VAR_014887|||http://purl.uniprot.org/annotation/VAR_014888|||http://purl.uniprot.org/annotation/VAR_038378|||http://purl.uniprot.org/annotation/VSP_004288|||http://purl.uniprot.org/annotation/VSP_004289|||http://purl.uniprot.org/annotation/VSP_004290|||http://purl.uniprot.org/annotation/VSP_004291
http://togogenome.org/gene/9606:SERPINA9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86WD7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2 and isoform 7.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||N-linked (GlcNAc...) asparagine|||Serpin A9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041971|||http://purl.uniprot.org/annotation/VAR_047344|||http://purl.uniprot.org/annotation/VAR_047345|||http://purl.uniprot.org/annotation/VAR_047346|||http://purl.uniprot.org/annotation/VAR_047347|||http://purl.uniprot.org/annotation/VAR_047348|||http://purl.uniprot.org/annotation/VSP_041488|||http://purl.uniprot.org/annotation/VSP_041489|||http://purl.uniprot.org/annotation/VSP_041490|||http://purl.uniprot.org/annotation/VSP_041491|||http://purl.uniprot.org/annotation/VSP_041492|||http://purl.uniprot.org/annotation/VSP_041493|||http://purl.uniprot.org/annotation/VSP_041494|||http://purl.uniprot.org/annotation/VSP_041495
http://togogenome.org/gene/9606:IFIT5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13325                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes PPP-RNA-binding.|||Abolishes RNA-binding.|||In isoform 2.|||Inhibits RNA-binding.|||Interaction with PPP-RNA|||Interaction with the 5'-triphosphate group of PPP-RNA|||Interferon-induced protein with tetratricopeptide repeats 5|||No effect RNA-binding.|||No effect on RNA-binding but changes size profile of RNA bound.|||No effect on RNA-binding but changes size profile of RNA bound. Abolishes PPP-RNA-binding.|||No effect on RNA-binding but changes size profile of RNA bound. Reduces PPP-RNA-binding.|||No effect on RNA-binding. Reduces PPP-RNA-binding.|||Reduced RNA-binding.|||Reduces PPP-RNA-binding.|||Reduces RNA-binding.|||Reduces RNA-binding. 25 fold reduction in tRNA-binding.|||Reduces RNA-binding. 5 fold reduction in tRNA-binding.|||Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-384.|||Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-415.|||Reduces binding to RNA and DNA.|||Strongly reduces binding to dsDNA. No effect on ssRNA binding.|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7|||TPR 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000106351|||http://purl.uniprot.org/annotation/VSP_056412
http://togogenome.org/gene/9606:VSIG8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DPA2                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type 1|||Ig-like V-type 2|||V-set and immunoglobulin domain-containing protein 8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313627
http://togogenome.org/gene/9606:MAEA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KRN7|||http://purl.uniprot.org/uniprot/B4DJP8|||http://purl.uniprot.org/uniprot/B4DQT1|||http://purl.uniprot.org/uniprot/B4DVN3|||http://purl.uniprot.org/uniprot/D6RIB6|||http://purl.uniprot.org/uniprot/Q7L5Y9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CTLH|||Disordered|||E3 ubiquitin-protein transferase MAEA|||Essential for ubiquitin ligase activity|||Extracellular and involved in cell to cell contact|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||LisH|||Phosphothreonine|||RING-Gid-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284936|||http://purl.uniprot.org/annotation/VAR_051150|||http://purl.uniprot.org/annotation/VSP_024784|||http://purl.uniprot.org/annotation/VSP_024785|||http://purl.uniprot.org/annotation/VSP_024786|||http://purl.uniprot.org/annotation/VSP_024788|||http://purl.uniprot.org/annotation/VSP_024789|||http://purl.uniprot.org/annotation/VSP_024790
http://togogenome.org/gene/9606:ADAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3A2|||http://purl.uniprot.org/uniprot/B4DUZ7|||http://purl.uniprot.org/uniprot/O75689                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  40-45% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-273.|||70% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-149.|||Arf-GAP|||Arf-GAP with dual PH domain-containing protein 1|||C4-type|||In isoform 2.|||In isoform 3.|||Loss of GTPase-activating activity.|||N6-acetyllysine|||PH|||PH 1|||PH 2|||Phosphoserine; by PKC|||Phosphothreonine; by PKC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074205|||http://purl.uniprot.org/annotation/VAR_047470|||http://purl.uniprot.org/annotation/VSP_054793|||http://purl.uniprot.org/annotation/VSP_054794
http://togogenome.org/gene/9606:AKAP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86UN6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  A-kinase anchor protein 14|||Abolishes RII-binding; when associated with P-43.|||Abolishes RII-binding; when associated with P-47.|||Disordered|||In isoform 2.|||In isoform 3.|||RII-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000064521|||http://purl.uniprot.org/annotation/VSP_009909|||http://purl.uniprot.org/annotation/VSP_009910|||http://purl.uniprot.org/annotation/VSP_009911
http://togogenome.org/gene/9606:DOCK8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E2J6M5|||http://purl.uniprot.org/uniprot/E2J6M6|||http://purl.uniprot.org/uniprot/Q8NF50                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Abolishes phosphorylation. No migration in response to chemokine CXCL12/SDF-1-alpha stimulation; when associated with A-2077 and A-2082.|||Abolishes phosphorylation. No migration in response to chemokine CXCL12/SDF-1-alpha stimulation; when associated with A-2077 and A-2087.|||Abolishes phosphorylation. No migration in response to chemokine CXCL12/SDF-1-alpha stimulation; when associated with A-2082 and A-2087.|||C2 DOCK-type|||DOCKER|||Dedicator of cytokinesis C/D N-terminal|||Dedicator of cytokinesis protein 8|||In HIES2.|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||Phosphomimetic mutant. Enhances migration in response to chemokine CXCL12/SDF-1-alpha stimulation and reduces interaction with LRCH1; when associated with E-2077 and E-2082.|||Phosphomimetic mutant. Enhances migration in response to chemokine CXCL12/SDF-1-alpha stimulation and reduces interaction with LRCH1; when associated with E-2077 and E-2087.|||Phosphomimetic mutant. Enhances migration in response to chemokine CXCL12/SDF-1-alpha stimulation and reduces interaction with LRCH1; when associated with E-2082 and E-2087.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189997|||http://purl.uniprot.org/annotation/VAR_033888|||http://purl.uniprot.org/annotation/VAR_033889|||http://purl.uniprot.org/annotation/VAR_033890|||http://purl.uniprot.org/annotation/VAR_033891|||http://purl.uniprot.org/annotation/VAR_033892|||http://purl.uniprot.org/annotation/VAR_033893|||http://purl.uniprot.org/annotation/VAR_059972|||http://purl.uniprot.org/annotation/VAR_063753|||http://purl.uniprot.org/annotation/VAR_071964|||http://purl.uniprot.org/annotation/VSP_027373|||http://purl.uniprot.org/annotation/VSP_039838
http://togogenome.org/gene/9606:FHAD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AJZ9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||FHA|||Forkhead-associated domain-containing protein 1|||In isoform 3.|||In isoform 4.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349365|||http://purl.uniprot.org/annotation/VAR_046372|||http://purl.uniprot.org/annotation/VSP_035366|||http://purl.uniprot.org/annotation/VSP_035369
http://togogenome.org/gene/9606:SNRPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09661                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRRCT|||N6-acetyllysine; alternate|||No change in spliceosome assembly.|||Phosphoserine|||Removed|||Results in defective spliceosome assembly.|||U2 small nuclear ribonucleoprotein A'                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074173
http://togogenome.org/gene/9606:OR51B4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5P0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51B4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150746|||http://purl.uniprot.org/annotation/VAR_024141|||http://purl.uniprot.org/annotation/VAR_030348
http://togogenome.org/gene/9606:GPR52                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2YGU0|||http://purl.uniprot.org/uniprot/Q9Y2T5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 52|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069576
http://togogenome.org/gene/9606:KITLG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P21583                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In DCUA; loss of cell membrane association.|||In FPHH; gain-of-function mutation; sKITLG reveales that the mutant Ser-36 sKITLG increases the content of the melanin by 109% compared with the wild-type sKITLG; tyrosinase activity is significantly increased by the mutant sKITLG compared to wild-type control.|||In WS2F; unknown pathological significance.|||In WS2F; unknown pathological significance; reduces secretion.|||In isoform 2.|||In isoform 3.|||Kit ligand|||N-linked (GlcNAc...) asparagine|||N-linked (GlcNAc...) asparagine; partial|||Not glycosylated|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Soluble KIT ligand                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031913|||http://purl.uniprot.org/annotation/PRO_0000403391|||http://purl.uniprot.org/annotation/VAR_042652|||http://purl.uniprot.org/annotation/VAR_042653|||http://purl.uniprot.org/annotation/VAR_063237|||http://purl.uniprot.org/annotation/VAR_063238|||http://purl.uniprot.org/annotation/VAR_076222|||http://purl.uniprot.org/annotation/VAR_076223|||http://purl.uniprot.org/annotation/VAR_087496|||http://purl.uniprot.org/annotation/VAR_087497|||http://purl.uniprot.org/annotation/VAR_087498|||http://purl.uniprot.org/annotation/VSP_006022|||http://purl.uniprot.org/annotation/VSP_032762|||http://purl.uniprot.org/annotation/VSP_032763
http://togogenome.org/gene/9606:ASNS                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P08243                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Asparagine synthetase|||Asparagine synthetase [glutamine-hydrolyzing]|||For GATase activity|||Glutamine amidotransferase type-2|||Important for beta-aspartyl-AMP intermediate formation|||In ASNSD; dramatic reduction in protein abundance.|||In ASNSD; increases level of protein abundance.|||In isoform 2.|||In isoform 3.|||Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056910|||http://purl.uniprot.org/annotation/VAR_023443|||http://purl.uniprot.org/annotation/VAR_070896|||http://purl.uniprot.org/annotation/VAR_070897|||http://purl.uniprot.org/annotation/VAR_070898|||http://purl.uniprot.org/annotation/VSP_045817|||http://purl.uniprot.org/annotation/VSP_045818
http://togogenome.org/gene/9606:ANGPTL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86XS5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Angiopoietin-related protein 5|||Fibrinogen C-terminal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009127|||http://purl.uniprot.org/annotation/VAR_055803
http://togogenome.org/gene/9606:FAM227B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M60                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Polar residues|||Protein FAM227B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244098|||http://purl.uniprot.org/annotation/VSP_019517|||http://purl.uniprot.org/annotation/VSP_019518
http://togogenome.org/gene/9606:MPZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A5F9ZI26|||http://purl.uniprot.org/uniprot/P25189                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In CHN2.|||In CMT1B and CMT2I; severe; reduces intercellular adhesion; does not affect targeting to the cell membrane.|||In CMT1B and CMTDID.|||In CMT1B and DSS.|||In CMT1B and DSS; severe.|||In CMT1B, CMT2I and CMT2J; CMTJ2 patients present Adie pupil; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane; affects glycosylation.|||In CMT1B, CMT2I and DSS.|||In CMT1B.|||In CMT1B; affects targeting to the cell membrane; reduces intercellular adhesion.|||In CMT1B; also in two asymptomatic individuals from the same family.|||In CMT1B; loss of glycosylation site.|||In CMT1B; moderate.|||In CMT1B; severe.|||In CMT1B; severe/mild.|||In CMT1B; slightly reduces intercellular adhesion; does not affect targeting to the cell membrane.|||In CMT2.|||In CMT2I and CMT1B.|||In CMT2I and DSS.|||In CMT2I.|||In CMT2I; patient carrying also Asn-89 and Met-162.|||In CMT2I; patient carrying also Asn-89 and Met-92.|||In CMT2I; patient carrying also Met-92 and Met-162.|||In CMT2J and CMT2I.|||In CMT2J.|||In CMT; associated with F-113.|||In CMT; unclassified; associated with Y-81.|||In DSS and CMT1B.|||In DSS.|||In DSS; associated on the same allele as His-116 and Asn-128 in one patient.|||In DSS; associated on the same allele as Thr-114 and Asn-128 in one patient.|||In DSS; associated on the same allele as Thr-114 and His-116 in one patient.|||In ROULS.|||In isoform L-MPZ.|||Myelin protein P0|||N-linked (GlcNAc...) (complex) asparagine|||Phosphoserine|||Phosphoserine; by PKC|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019300|||http://purl.uniprot.org/annotation/PRO_5023910374|||http://purl.uniprot.org/annotation/VAR_004500|||http://purl.uniprot.org/annotation/VAR_004501|||http://purl.uniprot.org/annotation/VAR_004502|||http://purl.uniprot.org/annotation/VAR_004503|||http://purl.uniprot.org/annotation/VAR_004504|||http://purl.uniprot.org/annotation/VAR_004505|||http://purl.uniprot.org/annotation/VAR_004506|||http://purl.uniprot.org/annotation/VAR_004507|||http://purl.uniprot.org/annotation/VAR_004508|||http://purl.uniprot.org/annotation/VAR_004509|||http://purl.uniprot.org/annotation/VAR_004510|||http://purl.uniprot.org/annotation/VAR_004511|||http://purl.uniprot.org/annotation/VAR_004512|||http://purl.uniprot.org/annotation/VAR_004513|||http://purl.uniprot.org/annotation/VAR_004514|||http://purl.uniprot.org/annotation/VAR_004515|||http://purl.uniprot.org/annotation/VAR_004516|||http://purl.uniprot.org/annotation/VAR_004517|||http://purl.uniprot.org/annotation/VAR_004518|||http://purl.uniprot.org/annotation/VAR_004519|||http://purl.uniprot.org/annotation/VAR_004520|||http://purl.uniprot.org/annotation/VAR_004521|||http://purl.uniprot.org/annotation/VAR_004522|||http://purl.uniprot.org/annotation/VAR_004523|||http://purl.uniprot.org/annotation/VAR_004524|||http://purl.uniprot.org/annotation/VAR_004525|||http://purl.uniprot.org/annotation/VAR_004526|||http://purl.uniprot.org/annotation/VAR_004527|||http://purl.uniprot.org/annotation/VAR_004528|||http://purl.uniprot.org/annotation/VAR_004529|||http://purl.uniprot.org/annotation/VAR_004530|||http://purl.uniprot.org/annotation/VAR_004531|||http://purl.uniprot.org/annotation/VAR_004532|||http://purl.uniprot.org/annotation/VAR_004533|||http://purl.uniprot.org/annotation/VAR_004534|||http://purl.uniprot.org/annotation/VAR_004535|||http://purl.uniprot.org/annotation/VAR_004536|||http://purl.uniprot.org/annotation/VAR_004537|||http://purl.uniprot.org/annotation/VAR_004538|||http://purl.uniprot.org/annotation/VAR_004539|||http://purl.uniprot.org/annotation/VAR_004540|||http://purl.uniprot.org/annotation/VAR_004541|||http://purl.uniprot.org/annotation/VAR_004542|||http://purl.uniprot.org/annotation/VAR_004543|||http://purl.uniprot.org/annotation/VAR_004544|||http://purl.uniprot.org/annotation/VAR_004545|||http://purl.uniprot.org/annotation/VAR_015971|||http://purl.uniprot.org/annotation/VAR_015972|||http://purl.uniprot.org/annotation/VAR_015973|||http://purl.uniprot.org/annotation/VAR_015974|||http://purl.uniprot.org/annotation/VAR_015975|||http://purl.uniprot.org/annotation/VAR_015976|||http://purl.uniprot.org/annotation/VAR_015977|||http://purl.uniprot.org/annotation/VAR_015978|||http://purl.uniprot.org/annotation/VAR_015979|||http://purl.uniprot.org/annotation/VAR_015980|||http://purl.uniprot.org/annotation/VAR_021609|||http://purl.uniprot.org/annotation/VAR_021610|||http://purl.uniprot.org/annotation/VAR_029971|||http://purl.uniprot.org/annotation/VAR_029972|||http://purl.uniprot.org/annotation/VAR_029973|||http://purl.uniprot.org/annotation/VAR_029974|||http://purl.uniprot.org/annotation/VAR_029975|||http://purl.uniprot.org/annotation/VAR_029976|||http://purl.uniprot.org/annotation/VAR_029977|||http://purl.uniprot.org/annotation/VAR_029978|||http://purl.uniprot.org/annotation/VAR_029979|||http://purl.uniprot.org/annotation/VAR_029980|||http://purl.uniprot.org/annotation/VAR_029981|||http://purl.uniprot.org/annotation/VAR_029982|||http://purl.uniprot.org/annotation/VAR_029983|||http://purl.uniprot.org/annotation/VAR_029984|||http://purl.uniprot.org/annotation/VAR_029985|||http://purl.uniprot.org/annotation/VAR_029986|||http://purl.uniprot.org/annotation/VAR_029987|||http://purl.uniprot.org/annotation/VAR_031884|||http://purl.uniprot.org/annotation/VAR_031885|||http://purl.uniprot.org/annotation/VAR_031886|||http://purl.uniprot.org/annotation/VAR_031887|||http://purl.uniprot.org/annotation/VAR_031888|||http://purl.uniprot.org/annotation/VAR_031889|||http://purl.uniprot.org/annotation/VAR_031890|||http://purl.uniprot.org/annotation/VAR_031891|||http://purl.uniprot.org/annotation/VAR_031892|||http://purl.uniprot.org/annotation/VAR_054393|||http://purl.uniprot.org/annotation/VAR_054394|||http://purl.uniprot.org/annotation/VAR_054395|||http://purl.uniprot.org/annotation/VAR_054396|||http://purl.uniprot.org/annotation/VAR_054397|||http://purl.uniprot.org/annotation/VAR_054398|||http://purl.uniprot.org/annotation/VAR_081765|||http://purl.uniprot.org/annotation/VSP_045844
http://togogenome.org/gene/9606:VPS16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H269                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  3'-nitrotyrosine|||Disrupts interaction with VPS33A, no effect on interaction with VPS18 and impairs endosome-lysosome fusion; when associated with D-669.|||Disrupts interaction with VPS33A, no effect on interaction with VPS18 and impairs endosome-lysosome fusion; when associated with E-725.|||In DYT30.|||In isoform 2.|||Interaction with VPS33A|||Vacuolar protein sorting-associated protein 16 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065888|||http://purl.uniprot.org/annotation/VAR_053776|||http://purl.uniprot.org/annotation/VAR_076520|||http://purl.uniprot.org/annotation/VAR_085701|||http://purl.uniprot.org/annotation/VAR_085702|||http://purl.uniprot.org/annotation/VAR_085703|||http://purl.uniprot.org/annotation/VSP_004018
http://togogenome.org/gene/9606:SIGLEC7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y286                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||ITIM motif|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like V-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Sialic acid-binding Ig-like lectin 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014947|||http://purl.uniprot.org/annotation/VAR_035523|||http://purl.uniprot.org/annotation/VSP_002555|||http://purl.uniprot.org/annotation/VSP_002556|||http://purl.uniprot.org/annotation/VSP_002557|||http://purl.uniprot.org/annotation/VSP_002558
http://togogenome.org/gene/9606:PHETA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ICB4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Motif|||Mutagenesis Site|||Sequence Variant                                                                                  ^@                                                                                  F&H|||Loss of OCRL-binding.|||PH|||Sesquipedalian-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000254133|||http://purl.uniprot.org/annotation/VAR_028822
http://togogenome.org/gene/9606:ZNF611                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N823                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17|||C2H2-type 1; degenerate|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Requires 2 nucleotide substitutions.|||Zinc finger protein 611                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234596|||http://purl.uniprot.org/annotation/VAR_052876|||http://purl.uniprot.org/annotation/VAR_052877|||http://purl.uniprot.org/annotation/VAR_059927|||http://purl.uniprot.org/annotation/VAR_060429|||http://purl.uniprot.org/annotation/VAR_060722|||http://purl.uniprot.org/annotation/VSP_038425
http://togogenome.org/gene/9606:POLQ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75417|||http://purl.uniprot.org/uniprot/Q59EE4                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes DNA polymerase activity.|||Basic and acidic residues|||DEAH box|||DNA polymerase theta|||Disordered|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Interaction with RAD51|||Loop 1|||Loop 2|||Loop 3|||N6-acetyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101279|||http://purl.uniprot.org/annotation/VAR_055707|||http://purl.uniprot.org/annotation/VSP_040747|||http://purl.uniprot.org/annotation/VSP_040748
http://togogenome.org/gene/9606:LTA4H                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VK27|||http://purl.uniprot.org/uniprot/P09960                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes aminopeptidase activity. Decreased epoxide hydrolase activity.|||Abolishes epoxide hydrolase activity. Reduced aminopeptidase activity.|||Aminopeptidase activity almost absent, but keeps LTA4 activity.|||Aminopeptidase activity strongly impaired, but keeps LTA4 activity.|||Complete loss of LTA4 hydrolase and peptidase enzyme activities.|||Complete loss of epoxide hydrolase activity and aminopeptidase activity.|||Covalently modified during suicide inhibition by leukotrienes|||Essential for epoxide hydrolase activity, but not for aminopeptidase activity|||In isoform 2 and isoform 3.|||In isoform 3 and isoform 4.|||Leukotriene A-4 hydrolase|||Loss of LTA4 hydrolase activity, and aminopeptidase activity strongly impaired.|||Loss of aminopeptidase activity, but keeps LTA4 hydrolase activity.|||Loss of epoxide hydrolase and aminopeptidase activities.|||N6-acetyllysine|||No effect on epoxide hydrolase and aminopeptidase activity.|||No loss of activity.|||No loss of epoxide hydrolase activity and aminopeptidase activity.|||Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal|||Phosphoserine|||Pro-Gly-Pro binding|||Proton acceptor|||Proton donor|||Reduced aminopeptidase activity. Minor effect on epoxide hydrolase activity.|||Removed|||Srongly increased epoxide hydrolase activity.|||Strongly reduced affinity for peptide substrates. Reduced epoxide hydrolase and aminopeptidase activity.|||Strongly reduced aminopeptidase activity. Abolishes epoxide hydrolase activity.|||Strongly reduced aminopeptidase activity. Strongly decreased affinity for leukotriene. Abolishes epoxide hydrolase activity.|||Strongly reduced hydrolysis of peptides starting with Arg. Small effect on hydrolysis of peptides starting with Ala. Abolishes epoxide hydrolase activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000095124|||http://purl.uniprot.org/annotation/VAR_051570|||http://purl.uniprot.org/annotation/VSP_041107|||http://purl.uniprot.org/annotation/VSP_041108|||http://purl.uniprot.org/annotation/VSP_041109
http://togogenome.org/gene/9606:CPSF4L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NMK7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  C3H1-type 1|||C3H1-type 2|||C3H1-type 3|||C3H1-type 4|||C3H1-type 5|||Putative cleavage and polyadenylation specificity factor subunit 4-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317366
http://togogenome.org/gene/9606:TTPAL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RA57|||http://purl.uniprot.org/uniprot/Q9BTX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Alpha-tocopherol transfer protein-like|||CRAL-TRIO|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210772|||http://purl.uniprot.org/annotation/VAR_061788
http://togogenome.org/gene/9606:SNED1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TER0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EGF-like 1|||EGF-like 10|||EGF-like 11; calcium-binding|||EGF-like 12; calcium-binding|||EGF-like 13|||EGF-like 14|||EGF-like 15|||EGF-like 2|||EGF-like 3|||EGF-like 4; calcium-binding|||EGF-like 5|||EGF-like 6|||EGF-like 7|||EGF-like 8|||EGF-like 9|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Follistatin-like 1|||Follistatin-like 2|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||NIDO|||Sushi|||Sushi, nidogen and EGF-like domain-containing protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299554|||http://purl.uniprot.org/annotation/VAR_034847|||http://purl.uniprot.org/annotation/VAR_034848|||http://purl.uniprot.org/annotation/VAR_034849|||http://purl.uniprot.org/annotation/VAR_034850|||http://purl.uniprot.org/annotation/VSP_027749|||http://purl.uniprot.org/annotation/VSP_027750|||http://purl.uniprot.org/annotation/VSP_027751|||http://purl.uniprot.org/annotation/VSP_027752|||http://purl.uniprot.org/annotation/VSP_027753|||http://purl.uniprot.org/annotation/VSP_027754
http://togogenome.org/gene/9606:C1orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F2Z2X7|||http://purl.uniprot.org/uniprot/Q5JVX7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Uncharacterized protein C1orf141                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000294456|||http://purl.uniprot.org/annotation/VAR_033186|||http://purl.uniprot.org/annotation/VAR_033187|||http://purl.uniprot.org/annotation/VSP_026643|||http://purl.uniprot.org/annotation/VSP_026644
http://togogenome.org/gene/9606:NEDD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P46934                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes interaction with ARRDC3; when associated with A-795 and A-868.|||Abolishes interaction with ARRDC3; when associated with A-795 and A-920.|||Abolishes interaction with ARRDC3; when associated with A-868 and A-920.|||Abolishes ubiquitination of DAZAP2.|||Disordered|||E3 ubiquitin-protein ligase NEDD4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Glycyl thioester intermediate|||HECT|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Increased nuclear localization.|||Mediates interaction with TNIK|||N-acetylalanine|||Nuclear export signal|||Phosphoserine|||Phosphothreonine|||Removed|||WW 1|||WW 2|||WW 3|||WW 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120319|||http://purl.uniprot.org/annotation/VAR_036472|||http://purl.uniprot.org/annotation/VAR_047909|||http://purl.uniprot.org/annotation/VAR_047910|||http://purl.uniprot.org/annotation/VAR_061985|||http://purl.uniprot.org/annotation/VSP_038256|||http://purl.uniprot.org/annotation/VSP_038257|||http://purl.uniprot.org/annotation/VSP_038258|||http://purl.uniprot.org/annotation/VSP_038259
http://togogenome.org/gene/9606:TOP2B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q02880|||http://purl.uniprot.org/uniprot/Q59H80                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||DNA topoisomerase 2-beta|||DNA topoisomerase type IIA|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for DNA bending; intercalates between base pairs of target DNA|||In BILU; decreased protein abundance; severely decreased DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity.|||In BILU; loss-of-function variant in a yeast complementation assay.|||In isoform Beta-1.|||Interaction with DNA|||Interaction with PLSCR1|||N-acetylalanine|||N6-acetyllysine|||Nuclear export signal|||O-(5'-phospho-DNA)-tyrosine intermediate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Probable disease-associated variant found in patients with global developmental delay and autism spectrum disorder.|||Removed|||Slightly reduced enzyme activity.|||Strongly reduced enzyme activity.|||Toprim|||Transition state stabilizer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000145369|||http://purl.uniprot.org/annotation/VAR_079273|||http://purl.uniprot.org/annotation/VAR_086569|||http://purl.uniprot.org/annotation/VAR_086570|||http://purl.uniprot.org/annotation/VAR_086571|||http://purl.uniprot.org/annotation/VAR_086572|||http://purl.uniprot.org/annotation/VSP_006532
http://togogenome.org/gene/9606:IGSF23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A1L1A6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Found in a patient with osteopetrosis; unknown pathological significance.|||Helical|||Ig-like|||Immunoglobulin superfamily member 23|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000410772|||http://purl.uniprot.org/annotation/VAR_087628
http://togogenome.org/gene/9606:CFAP161                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P656                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Cilia- and flagella-associated protein 161|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244092|||http://purl.uniprot.org/annotation/VAR_050883|||http://purl.uniprot.org/annotation/VSP_019511|||http://purl.uniprot.org/annotation/VSP_019512|||http://purl.uniprot.org/annotation/VSP_019513
http://togogenome.org/gene/9606:DGKK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5KSL6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||18|||19|||2|||20|||21|||22|||23|||24|||25|||26|||27|||28|||29|||3|||30|||31|||32|||33|||33 X 4 AA approximate tandem repeats of E-P-A-P|||4|||5|||6|||7|||8|||9|||DAGKc|||Diacylglycerol kinase kappa|||Disordered|||Does not affect phosphorylation.|||Induces a strong reduction in phosphorylation but is still sensitive to H(2)O(2).|||PH|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2|||Phosphotyrosine|||Pro residues|||Required for localization to the plasma membrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239368|||http://purl.uniprot.org/annotation/VAR_048859
http://togogenome.org/gene/9606:HMGA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A994J434|||http://purl.uniprot.org/uniprot/P17096|||http://purl.uniprot.org/uniprot/Q5T6U8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Experimental Information|||Initiator Methionine|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Initiator Methionine|||Mass|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  A.T hook 1|||A.T hook 2|||A.T hook 3|||ADP-ribosylserine|||ADP-ribosylserine; alternate|||Asymmetric dimethylarginine; alternate|||Asymmetric dimethylarginine; by PRMT6; alternate|||Basic and acidic residues|||Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58.|||Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60.|||Disordered|||Does not affect methylation by PRMT6.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||High mobility group protein HMG-I/HMG-Y|||In isoform HMG-R.|||In isoform HMG-Y.|||Interaction with HIPK2|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Omega-N-methylarginine; alternate|||Omega-N-methylarginine; by PRMT6; alternate|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CK|||Phosphoserine; by HIPK2 and CDC2|||Phosphothreonine|||Phosphothreonine; by HIPK2 and CDC2|||Polar residues|||Removed|||Symmetric dimethylarginine; alternate|||With 1 acetyl and 2 phosphate groups. The measured range is 2-107.|||With 1 acetyl and 3 phosphate groups. The measured range is 2-107.|||With 1 acetyl, 1 methyl and 2 phosphate groups. The measured range is 2-107.|||With 1 acetyl, 1 methyl and 3 phosphate groups. The measured range is 2-107.|||With 1 acetyl, 2 methyl and 2 phosphate groups. The measured range is 2-107.|||With 1 acetyl, 2 methyl and 3 phosphate groups. The measured range is 2-107.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206708|||http://purl.uniprot.org/annotation/VSP_002182|||http://purl.uniprot.org/annotation/VSP_018084
http://togogenome.org/gene/9606:MAGEA9B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43362                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 9|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156708|||http://purl.uniprot.org/annotation/VAR_064160
http://togogenome.org/gene/9606:ACAN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P16112                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  1-1|||1-10; approximate|||1-11|||1-12|||1-2|||1-3|||1-4|||1-5|||1-6|||1-7; approximate|||1-8; approximate|||1-9|||12 X 6 AA approximate tandem repeats of E-[GVE]-P-[SFY]-[APT]-[TSP]|||2-1|||2-10|||2-11|||2-12|||2-13|||2-14|||2-15|||2-16|||2-17|||2-18|||2-19|||2-2|||2-20|||2-21|||2-22|||2-23|||2-24|||2-25|||2-26|||2-27|||2-28|||2-29|||2-3|||2-30|||2-31|||2-32|||2-33; approximate|||2-34|||2-35|||2-4|||2-5|||2-6|||2-7|||2-8|||2-9|||35 X 19 AA approximate tandem repeats of E-[IVDG]-[LV]-[EV]-[GTI]-[STA]-[ATV]-[SP]-[GA]-[VIFAD]-[GEDL]-[DE]-[LVI]-[SG]-[GERK]-[LV]-P-S-G|||Aggrecan core protein|||Aggrecan core protein 2|||Basic residues|||C-type lectin|||CS-1|||CS-2|||Cleavage; by aggrecanase|||Disordered|||EGF-like|||G1-A|||G1-B|||G1-B'|||G2-B|||G2-B'|||G3|||Ig-like V-type|||In SEMDAG; creates a functional N-glycosylation site; does not adversely affect protein trafficking and secretion.|||In SSOAOD.|||In isoform 2 and isoform 3.|||In isoform 3.|||KS|||Link 1|||Link 2|||Link 3|||Link 4|||N-linked (GlcNAc...) asparagine|||O-linked (Xyl...) (chondroitin sulfate) serine|||O-linked (Xyl...) (keratan sulfate) threonine|||Polar residues|||Pro residues|||Sushi                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000017505|||http://purl.uniprot.org/annotation/PRO_0000017506|||http://purl.uniprot.org/annotation/VAR_056152|||http://purl.uniprot.org/annotation/VAR_056153|||http://purl.uniprot.org/annotation/VAR_056154|||http://purl.uniprot.org/annotation/VAR_056155|||http://purl.uniprot.org/annotation/VAR_063053|||http://purl.uniprot.org/annotation/VAR_063765|||http://purl.uniprot.org/annotation/VAR_080159|||http://purl.uniprot.org/annotation/VAR_080160|||http://purl.uniprot.org/annotation/VAR_080161|||http://purl.uniprot.org/annotation/VAR_080162|||http://purl.uniprot.org/annotation/VAR_080163|||http://purl.uniprot.org/annotation/VAR_080164|||http://purl.uniprot.org/annotation/VAR_080165|||http://purl.uniprot.org/annotation/VAR_080166|||http://purl.uniprot.org/annotation/VAR_080167|||http://purl.uniprot.org/annotation/VAR_080168|||http://purl.uniprot.org/annotation/VAR_080169|||http://purl.uniprot.org/annotation/VSP_003074|||http://purl.uniprot.org/annotation/VSP_003075
http://togogenome.org/gene/9606:VEGFA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0Y0IMM4|||http://purl.uniprot.org/uniprot/A2A2V4|||http://purl.uniprot.org/uniprot/P15692                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic residues|||Disordered|||In isoform VEGF111 and isoform 18.|||In isoform VEGF121 and isoform L-VEGF121.|||In isoform VEGF145.|||In isoform VEGF148 and isoform 17.|||In isoform VEGF165, isoform VEGF148, isoform VEGF165B, isoform L-VEGF165, isoform 15 and isoform 17.|||In isoform VEGF165B and isoform 15.|||In isoform VEGF183 and isoform 16.|||In isoform VEGF206 and isoform L-VEGF206.|||In isoform VEGF206, isoform VEGF189, isoform VEGF183, isoform VEGF165, isoform VEGF148, isoform VEGF145, isoform VEGF165B, isoform VEGF121 and isoform VEGF111.|||Interchain|||N-VEGF|||N-linked (GlcNAc...) asparagine|||Platelet-derived growth factor (PDGF) family profile|||VEGFA|||Vascular endothelial growth factor A, long form|||Vascular permeability factor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000458064|||http://purl.uniprot.org/annotation/PRO_0000458065|||http://purl.uniprot.org/annotation/PRO_0000458066|||http://purl.uniprot.org/annotation/PRO_5007072960|||http://purl.uniprot.org/annotation/VSP_061891|||http://purl.uniprot.org/annotation/VSP_061892|||http://purl.uniprot.org/annotation/VSP_061893|||http://purl.uniprot.org/annotation/VSP_061894|||http://purl.uniprot.org/annotation/VSP_061895|||http://purl.uniprot.org/annotation/VSP_061896|||http://purl.uniprot.org/annotation/VSP_061897|||http://purl.uniprot.org/annotation/VSP_061898|||http://purl.uniprot.org/annotation/VSP_061899|||http://purl.uniprot.org/annotation/VSP_061900|||http://purl.uniprot.org/annotation/VSP_061901|||http://purl.uniprot.org/annotation/VSP_061902|||http://purl.uniprot.org/annotation/VSP_061903
http://togogenome.org/gene/9606:HNRNPCL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60812                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||Heterogeneous nuclear ribonucleoprotein C-like 1|||Polar residues|||RRM                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081848|||http://purl.uniprot.org/annotation/VAR_033723|||http://purl.uniprot.org/annotation/VAR_052225|||http://purl.uniprot.org/annotation/VAR_059824
http://togogenome.org/gene/9606:OR14A16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NHC5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 14A16                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150581|||http://purl.uniprot.org/annotation/VAR_043796
http://togogenome.org/gene/9606:RAB19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A4D1S5                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Lipid Binding|||Modified Residue|||Motif|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2.|||Ras-related protein Rab-19|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300459|||http://purl.uniprot.org/annotation/VSP_036588
http://togogenome.org/gene/9606:FABP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P12104                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Fatty acid-binding protein, intestinal|||Found in 29% of the population; associated with increased plasma insulin concentration, increased fat oxidation and insulin resistance; 2-fold greater affinity for long-chain fatty acids.|||Localized reduction in stability.|||N-acetylalanine|||Reduced stability.|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000067328|||http://purl.uniprot.org/annotation/VAR_002379
http://togogenome.org/gene/9606:BCL6B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KA13|||http://purl.uniprot.org/uniprot/Q8N143                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Zinc Finger                                                                                  ^@                                                                                  B-cell CLL/lymphoma 6 member B protein|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047100
http://togogenome.org/gene/9606:MARCO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q4ZG40|||http://purl.uniprot.org/uniprot/Q9UEW3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Collagen-like|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Macrophage receptor MARCO|||N-linked (GlcNAc...) asparagine|||SRCR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181630|||http://purl.uniprot.org/annotation/VAR_024650|||http://purl.uniprot.org/annotation/VSP_056698
http://togogenome.org/gene/9606:PHYHIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92561                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Fibronectin type-III|||N-linked (GlcNAc...) asparagine|||Phytanoyl-CoA hydroxylase-interacting protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058416|||http://purl.uniprot.org/annotation/VAR_018475
http://togogenome.org/gene/9606:MBD3L5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NJ08                                                                                  ^@                                                                                  Chain|||Molecule Processing                                                                                  ^@                                                                                  Chain                                                                                  ^@                                                                                  Putative methyl-CpG-binding domain protein 3-like 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349235
http://togogenome.org/gene/9606:GFM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/C9IZ01|||http://purl.uniprot.org/uniprot/E5KND5|||http://purl.uniprot.org/uniprot/Q96RP9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Elongation factor G, mitochondrial|||In COXPD1.|||In isoform 2.|||Mitochondrion|||N6-acetyllysine|||Phosphoserine|||Tr-type G|||tr-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007440|||http://purl.uniprot.org/annotation/VAR_021512|||http://purl.uniprot.org/annotation/VAR_028303|||http://purl.uniprot.org/annotation/VAR_031901|||http://purl.uniprot.org/annotation/VAR_076197|||http://purl.uniprot.org/annotation/VAR_076198|||http://purl.uniprot.org/annotation/VSP_038189
http://togogenome.org/gene/9606:R3HDML                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H3Y0                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  N-linked (GlcNAc...) asparagine|||Peptidase inhibitor R3HDML|||SCP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287635|||http://purl.uniprot.org/annotation/PRO_0000287636|||http://purl.uniprot.org/annotation/VAR_032339|||http://purl.uniprot.org/annotation/VAR_048834
http://togogenome.org/gene/9606:CHIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3T7|||http://purl.uniprot.org/uniprot/Q1M0P3|||http://purl.uniprot.org/uniprot/Q1M0P4|||http://purl.uniprot.org/uniprot/Q2VT96|||http://purl.uniprot.org/uniprot/Q9BZP6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic mammalian chitinase|||Chitin-binding type-2|||GH18|||In isoform 2.|||In isoform 3.|||Increased chitinase activity; when associated with D-45 and M-61.|||Increased chitinase activity; when associated with D-45 and N-47.|||Increased chitinase activity; when associated with N-47 and M-61.|||Loss of chitinase activity. No effect on protection against apoptosis or on AKT1 activation.|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011944|||http://purl.uniprot.org/annotation/VAR_033730|||http://purl.uniprot.org/annotation/VAR_049192|||http://purl.uniprot.org/annotation/VAR_049193|||http://purl.uniprot.org/annotation/VAR_049194|||http://purl.uniprot.org/annotation/VAR_049195|||http://purl.uniprot.org/annotation/VAR_049196|||http://purl.uniprot.org/annotation/VAR_063030|||http://purl.uniprot.org/annotation/VAR_063031|||http://purl.uniprot.org/annotation/VAR_063032|||http://purl.uniprot.org/annotation/VAR_063033|||http://purl.uniprot.org/annotation/VSP_008634|||http://purl.uniprot.org/annotation/VSP_008635
http://togogenome.org/gene/9606:MRPL19                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49406                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Large ribosomal subunit protein bL19m|||Mitochondrion|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030473
http://togogenome.org/gene/9606:PRXL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRX8                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Decrease of about 125% in antioxidant activity in TNFSF11-stimulated osteoclasts and reduced inhibition of TNFSF11-induced osteoclast formation.|||Decrease of about 38% in antioxidant activity in TNFSF11-stimulated osteoclasts and reduced inhibition of TNFSF11-induced osteoclast formation. Does not change anti-inflammatory properties.|||In isoform 2.|||Peroxiredoxin-like 2A|||Redox-active|||Thioredoxin fold                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019550|||http://purl.uniprot.org/annotation/VSP_042229
http://togogenome.org/gene/9606:NAPRT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6XQN6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Complete loss of activity.|||In isoform 2.|||In isoform 3.|||Nicotinate phosphoribosyltransferase|||Partial loss of activity in the presence of ATP, almost complete loss in the absence of ATP.|||Partial loss of activity in the presence of ATP, complete loss in the absence of ATP.|||Partial loss of activity.|||Phosphohistidine|||Phosphoserine|||Small loss of activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000315681|||http://purl.uniprot.org/annotation/VAR_038275|||http://purl.uniprot.org/annotation/VSP_030610|||http://purl.uniprot.org/annotation/VSP_030612
http://togogenome.org/gene/9606:TSC22D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99576                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  AP1-binding|||Disordered|||In isoform 2.|||In isoform 4.|||Leucine-zipper|||Phosphoserine|||TSC22 domain family protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219370|||http://purl.uniprot.org/annotation/VSP_012689|||http://purl.uniprot.org/annotation/VSP_061579
http://togogenome.org/gene/9606:DDX54                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDD1                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ATP-dependent RNA helicase DDX54|||Basic and acidic residues|||Basic residues|||DEAD box|||Disordered|||Found in a patient with a neurodevelopmental disorder; unknown pathological significance.|||Helicase ATP-binding|||Helicase C-terminal|||In isoform 2.|||Interaction with nuclear receptors|||Phosphoserine|||Q motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055056|||http://purl.uniprot.org/annotation/VAR_033860|||http://purl.uniprot.org/annotation/VAR_052171|||http://purl.uniprot.org/annotation/VAR_052172|||http://purl.uniprot.org/annotation/VAR_052173|||http://purl.uniprot.org/annotation/VAR_083615|||http://purl.uniprot.org/annotation/VAR_083616|||http://purl.uniprot.org/annotation/VAR_083617|||http://purl.uniprot.org/annotation/VAR_083618|||http://purl.uniprot.org/annotation/VAR_083619|||http://purl.uniprot.org/annotation/VSP_040135
http://togogenome.org/gene/9606:WASHC2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYF6|||http://purl.uniprot.org/uniprot/E7ESD2|||http://purl.uniprot.org/uniprot/Q641Q2|||http://purl.uniprot.org/uniprot/Q6P0Q7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Basic residues|||Disordered|||FAM21/CAPZIP|||In isoform 2.|||Interaction with VPS35|||Interaction with phospholipids|||LFa 1|||LFa 10|||LFa 11|||LFa 12|||LFa 13|||LFa 14|||LFa 15|||LFa 16|||LFa 17|||LFa 18|||LFa 19|||LFa 2|||LFa 20|||LFa 21|||LFa 3|||LFa 4|||LFa 5|||LFa 6|||LFa 7|||LFa 8|||LFa 9|||Phosphoserine|||Polar residues|||Required for interaction with CCDC22 and VPS35L|||Required for interaction with F-actin-capping protein subunit alpha (CAPZA1 or CAPZA2 or CAPZA3)|||Sufficient for interaction with CCDC93|||Sufficient for interaction with WASHC3, WASHC4 and WASHC5; required for interaction with WASHC1|||WASH complex subunit 2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317299|||http://purl.uniprot.org/annotation/VSP_030948
http://togogenome.org/gene/9606:B2M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P61769                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Beta-2-microglobulin|||Beta-2-microglobulin form pI 5.3|||Decreases tendency towards amyloid formation.|||Ig-like C1-type|||In AMYL8; reduced stability; in contrast to the wild-type, the mutant aggregates into fibrils with classic amyloid-like properties under physiologic solvent conditions.|||In IMD43; lower levels of B2M, MHC class I and FCGRT proteins.|||Increases tendency towards amyloid formation.|||N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis|||N-linked (Glc) (glycation) lysine; in vitro|||Pyrrolidone carboxylic acid; in form pI 5.3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018779|||http://purl.uniprot.org/annotation/PRO_0000018780|||http://purl.uniprot.org/annotation/VAR_030660|||http://purl.uniprot.org/annotation/VAR_076691
http://togogenome.org/gene/9606:NCF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P14598                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes autoinhibition and promotes phospholipid binding.|||Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-359.|||Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-328 and E-370.|||Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-304; E-359 and E-370.|||Abolishes autoinhibition and promotes phospholipid binding; when associated with E-303; E-328; E-359 and E-370.|||Abolishes autoinhibition and promotes phospholipid binding; when associated with E-304; E-328; E-359 and E-370.|||Disordered|||In CGD1.|||In isoform 2.|||May influence susceptibility to systemic lupus erythematosus.|||Neutrophil cytosol factor 1|||PX|||Phosphoserine|||Polar residues|||Reduces affinity for membranes enriched in phosphatidylinositol 3,4-bisphosphate.|||SH3 1|||SH3 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096762|||http://purl.uniprot.org/annotation/VAR_012476|||http://purl.uniprot.org/annotation/VAR_012477|||http://purl.uniprot.org/annotation/VAR_012478|||http://purl.uniprot.org/annotation/VAR_012479|||http://purl.uniprot.org/annotation/VAR_012480|||http://purl.uniprot.org/annotation/VAR_014735|||http://purl.uniprot.org/annotation/VAR_018476|||http://purl.uniprot.org/annotation/VAR_018479|||http://purl.uniprot.org/annotation/VSP_035032|||http://purl.uniprot.org/annotation/VSP_035033
http://togogenome.org/gene/9606:IER3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7X2|||http://purl.uniprot.org/uniprot/P46695                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphoserine; by MAPK1|||Phosphothreonine; by MAPK1|||Polar residues|||Radiation-inducible immediate-early gene IEX-1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084159|||http://purl.uniprot.org/annotation/VAR_058496
http://togogenome.org/gene/9606:HERC5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXV3|||http://purl.uniprot.org/uniprot/Q9UII4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||E3 ISG15--protein ligase HERC5|||Glycyl thioester intermediate|||HECT|||Loss of activity; no effect on IRF3 interaction.|||RCC1 1|||RCC1 2|||RCC1 3|||RCC1 4|||RCC1 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000206641|||http://purl.uniprot.org/annotation/VAR_057123
http://togogenome.org/gene/9606:YES1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07947                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  About 50% loss of CSK-mediated inhibition.|||Disordered|||N-myristoyl glycine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by CSK|||Phosphotyrosine; by autocatalysis|||Polar residues|||Protein kinase|||Proton acceptor|||Removed|||S-palmitoyl cysteine; in membrane form|||SH2|||SH3|||Tyrosine-protein kinase Yes                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000088181|||http://purl.uniprot.org/annotation/VAR_041879|||http://purl.uniprot.org/annotation/VAR_041880
http://togogenome.org/gene/9606:GMEB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AT47|||http://purl.uniprot.org/uniprot/B2RCN8|||http://purl.uniprot.org/uniprot/Q9Y692                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Glucocorticoid modulatory element-binding protein 1|||In isoform 2.|||N-acetylalanine|||Removed|||SAND                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074089|||http://purl.uniprot.org/annotation/VAR_051894|||http://purl.uniprot.org/annotation/VSP_005970
http://togogenome.org/gene/9606:KICS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96MD2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  KICSTOR subunit 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000321902|||http://purl.uniprot.org/annotation/VAR_039371|||http://purl.uniprot.org/annotation/VAR_039372
http://togogenome.org/gene/9606:FMR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q06787                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Agenet-like 1|||Agenet-like 2|||Alters the structural integrity of the N-terminus and leads to aggregation.|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Disordered|||Does not affect RNA-binding to G-quadruplex structure.|||Fragile X messenger ribonucleoprotein 1|||In FXS; alters protein folding and stability; increases nucleocytoplasmic shuttling; reduces localization in Cajal bodies; reduces the association with cytoplasmic granules; reduces association with polyribosome; reduces RNA-binding; attenuates mRNA translation repression; impairs homooligomerization; reduces interaction with TDRD3; reduces interaction with viral influenza A nucleoprotein (NP); does not inhibit interaction with SMN1, FXR1 and FXR2.|||In FXS; rare variant found in a developmentally delayed male; inhibits nucleosome binding; reduces interaction with KCNMB4; inhibits presynaptic action potential (AP) broadening; does not alter postsynaptic RNA-binding and polyribosome association.|||In FXS; reduces association with polyribosome; reduces RNA-binding.|||In isoform 1, isoform 3, isoform 5 and isoform 7.|||In isoform 1, isoform 8, isoform 9 and isoform 11.|||In isoform 10 and isoform 11.|||In isoform 2 and isoform 3.|||In isoform 4, isoform 5 and isoform 8.|||Interaction with RANBP9|||KH 1|||KH 2|||Loss of phosphorylation. Does not affect interaction with MCRS1. Does not affect localization to cytoplasmic granules. Does not affect association with polyribosome.|||N-acetylmethionine|||Necessary for interaction with CYFIP1, CYFIP2, FXR1 and FXR2|||Nuclear export signal|||Nucleolar localization signal 1|||Nucleolar localization signal 2|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphoserine; by CK2|||Phosphothreonine|||Polar residues|||RNA-binding RGG-box|||Reduces arginine methylation by 80%.|||Reduces binding to nucleosome.|||Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 527-E--E-534.|||Reduces nucleolar localization. Strongly reduces nucleolar localization; when associated with 613-E--E-617.|||Required for nuclear export|||Required for nuclear localization|||Slightly reduced methylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050102|||http://purl.uniprot.org/annotation/VAR_005234|||http://purl.uniprot.org/annotation/VAR_005235|||http://purl.uniprot.org/annotation/VAR_029278|||http://purl.uniprot.org/annotation/VAR_064507|||http://purl.uniprot.org/annotation/VAR_075977|||http://purl.uniprot.org/annotation/VSP_002823|||http://purl.uniprot.org/annotation/VSP_002824|||http://purl.uniprot.org/annotation/VSP_002825|||http://purl.uniprot.org/annotation/VSP_002826|||http://purl.uniprot.org/annotation/VSP_058423
http://togogenome.org/gene/9606:ACP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZNF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Acid phosphatase type 7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316824
http://togogenome.org/gene/9606:CYRIA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H0Q0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Sequence Conflict                                                                                  ^@                                                                                  CYFIP-related Rac1 interactor A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000187058
http://togogenome.org/gene/9606:OR2A14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVB0|||http://purl.uniprot.org/uniprot/Q96R47                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2A14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150458|||http://purl.uniprot.org/annotation/VAR_060477|||http://purl.uniprot.org/annotation/VAR_060478
http://togogenome.org/gene/9606:KRT18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05783                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Abolishes binding to YWHAE and YWHAZ.|||Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis.|||Cleavage; by caspase-3, caspase-6 or caspase-7|||Coil 1A|||Coil 1B|||Coil 2|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In CIRRH.|||In CIRRH; interfers with the ability to form normal filaments.|||In transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation.|||Interaction with DNAJB6|||Interaction with TRADD|||Keratin, type I cytoskeletal 18|||Linker 1|||Linker 12|||N-acetylserine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Necessary for interaction with PNN|||No effect on phosphorylation; when associated with A-15 and A-18.|||No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53.|||No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53.|||No effect on phosphorylation; when associated with A-2 and A-10.|||No effect on phosphorylation; when associated with A-2 and A-7.|||No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53.|||No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49.|||No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53.|||No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49.|||No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51.|||No effect on phosphorylation; when associated with A-44.|||No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31.|||No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53.|||No effect on phosphorylation; when associated with A-7 and A-10.|||O-linked (GlcNAc) serine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; alternate|||Phosphoserine; by CAMK, PKC/PRKCE and AURKA|||Phosphoserine; by CDK1|||Phosphoserine; by MAPKAPK2 and MAPKAPK3|||Phosphothreonine|||Phosphotyrosine|||Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization.|||Removed|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/CAR_000175|||http://purl.uniprot.org/annotation/CAR_000193|||http://purl.uniprot.org/annotation/CAR_000194|||http://purl.uniprot.org/annotation/PRO_0000063666|||http://purl.uniprot.org/annotation/VAR_003852|||http://purl.uniprot.org/annotation/VAR_023054|||http://purl.uniprot.org/annotation/VAR_023055|||http://purl.uniprot.org/annotation/VAR_023056|||http://purl.uniprot.org/annotation/VAR_023057
http://togogenome.org/gene/9606:SMIM13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJ93                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Small integral membrane protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000414060
http://togogenome.org/gene/9606:NPAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZP6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal cancer sample; somatic mutation.|||Nuclear pore-associated protein 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000243929|||http://purl.uniprot.org/annotation/VAR_026872|||http://purl.uniprot.org/annotation/VAR_026873|||http://purl.uniprot.org/annotation/VAR_026874|||http://purl.uniprot.org/annotation/VAR_026875|||http://purl.uniprot.org/annotation/VAR_035682|||http://purl.uniprot.org/annotation/VAR_035683|||http://purl.uniprot.org/annotation/VAR_050878|||http://purl.uniprot.org/annotation/VAR_050879|||http://purl.uniprot.org/annotation/VAR_050880|||http://purl.uniprot.org/annotation/VAR_050881|||http://purl.uniprot.org/annotation/VAR_050882
http://togogenome.org/gene/9606:TBC1D3L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B9A6J9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Lipid Binding|||Region                                                                                  ^@                                                                                  Disordered|||Pro residues|||Rab-GAP TBC|||S-palmitoyl cysteine|||TBC1 domain family member 3L                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000431608
http://togogenome.org/gene/9606:ARMC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NEN0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ARM 1|||ARM 10|||ARM 11|||ARM 12|||ARM 2|||ARM 3|||ARM 4|||ARM 5|||ARM 6|||ARM 7|||ARM 8|||ARM 9|||Armadillo repeat-containing protein 2|||Disordered|||In SPGF38; unknown pathological significance.|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284401|||http://purl.uniprot.org/annotation/VAR_031948|||http://purl.uniprot.org/annotation/VAR_031949|||http://purl.uniprot.org/annotation/VAR_082205|||http://purl.uniprot.org/annotation/VAR_082206|||http://purl.uniprot.org/annotation/VSP_055622
http://togogenome.org/gene/9606:CD8B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10966|||http://purl.uniprot.org/uniprot/Q53QL8                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Sequence Conflict|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like|||Ig-like V-type|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3 and isoform 6.|||In isoform 4.|||In isoform 7.|||In isoform 8.|||N-linked (GlcNAc...) asparagine|||Phosphotyrosine|||T-cell surface glycoprotein CD8 beta chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014643|||http://purl.uniprot.org/annotation/PRO_5004249461|||http://purl.uniprot.org/annotation/VSP_002490|||http://purl.uniprot.org/annotation/VSP_002491|||http://purl.uniprot.org/annotation/VSP_002492|||http://purl.uniprot.org/annotation/VSP_002493|||http://purl.uniprot.org/annotation/VSP_039654|||http://purl.uniprot.org/annotation/VSP_039655
http://togogenome.org/gene/9606:FBXW7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G0Z2K0|||http://purl.uniprot.org/uniprot/Q969H0|||http://purl.uniprot.org/uniprot/S4R3U4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished phosphorylation by ATM.|||Acidic residues|||Basic and acidic residues|||Disordered|||Does not affect interaction with PIN1.|||Does not affect phosphorylation by ATM.|||F-box|||F-box/WD repeat-containing protein 7|||Impaired interaction with PIN1.|||In DEDHIL.|||In DEDHIL; also found in a colorectal cancer sample.|||In DEDHIL; decreased protein abundance; no effect on proteasome-mediated ubiquitin-dependent protein catabolic process.|||In DEDHIL; no effect on protein abundance; changed on proteasome-mediated ubiquitin-dependent protein catabolic process.|||In DEDHIL; no effect on protein abundance; changed proteasome-mediated ubiquitin-dependent protein catabolic process.|||In DEDHIL; unknown pathological significance.|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In an acute lymphoblastic leukemia cell line; loss of interaction with substrate; does not affect interaction with SKP1 or STYX.|||In an ovarian cancer cell line.|||In isoform 2.|||In isoform 3.|||Phosphoserine; by ATM|||Phosphoserine; by SGK1|||Phosphothreonine|||Polar residues|||Prevents homodimerization.|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050994|||http://purl.uniprot.org/annotation/VAR_017812|||http://purl.uniprot.org/annotation/VAR_017813|||http://purl.uniprot.org/annotation/VAR_017814|||http://purl.uniprot.org/annotation/VAR_017815|||http://purl.uniprot.org/annotation/VAR_017816|||http://purl.uniprot.org/annotation/VAR_017817|||http://purl.uniprot.org/annotation/VAR_033030|||http://purl.uniprot.org/annotation/VAR_035880|||http://purl.uniprot.org/annotation/VAR_035881|||http://purl.uniprot.org/annotation/VAR_087662|||http://purl.uniprot.org/annotation/VAR_087663|||http://purl.uniprot.org/annotation/VAR_087664|||http://purl.uniprot.org/annotation/VAR_087665|||http://purl.uniprot.org/annotation/VAR_087666|||http://purl.uniprot.org/annotation/VAR_087667|||http://purl.uniprot.org/annotation/VAR_087668|||http://purl.uniprot.org/annotation/VAR_087669|||http://purl.uniprot.org/annotation/VAR_087670|||http://purl.uniprot.org/annotation/VAR_087671|||http://purl.uniprot.org/annotation/VAR_087672|||http://purl.uniprot.org/annotation/VAR_087673|||http://purl.uniprot.org/annotation/VAR_087674|||http://purl.uniprot.org/annotation/VAR_087675|||http://purl.uniprot.org/annotation/VAR_087676|||http://purl.uniprot.org/annotation/VAR_087677|||http://purl.uniprot.org/annotation/VAR_087678|||http://purl.uniprot.org/annotation/VAR_087679|||http://purl.uniprot.org/annotation/VAR_087680|||http://purl.uniprot.org/annotation/VAR_087681|||http://purl.uniprot.org/annotation/VAR_087682|||http://purl.uniprot.org/annotation/VSP_009482|||http://purl.uniprot.org/annotation/VSP_009483|||http://purl.uniprot.org/annotation/VSP_009484|||http://purl.uniprot.org/annotation/VSP_009485
http://togogenome.org/gene/9606:NLRP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7I2R3P8|||http://purl.uniprot.org/uniprot/Q96P20                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to activate the NLRP3 inflammasome.|||Abolished binding to small-inhibitor MCC950 and ability to activate the NLRP3 inflammasome following stimulation with nigericin.|||Abolished formation of the NLRP3 inflammasome.|||Abolished palmitoylation by ZDHHC12, preventing degradation by the chaperone-mediated autophagy pathway.|||Abolished phosphorylation by CSNK1A1; increased activation of the NLRP3 inflammasome.|||Abolished phosphorylation by MAPK8/JNK1; decreased activation of the NLRP3 inflammasome.|||Abolished phosphorylation.|||Abolished ubiquitination by the SCF(FBXL2) complex.|||Complete loss of PYCARD/ASC filament nucleation.|||Complete loss of PYCARD/ASC filament nucleation. Decreased PYCARD/ASC filament nucleation.|||Complete loss of PYCARD/ASC filament nucleation; when associated with E-23.|||Complete loss of PYCARD/ASC filament nucleation; when associated with E-24.|||Decreased ability to activate the NLRP3 inflammasome.|||Decreased interaction with HSPA8/HSC70 and NLRP3 degradation by the chaperone-mediated autophagy pathway.|||Decreased interaction with MAPK4.|||Decreased phosphorylation by BTK; when associated with 136-F--F-143.|||Decreased phosphorylation by BTK; when associated with F-168.|||Decreased phosphorylation; increased activation of the NLRP3 inflammasome.|||Decreased ubiquitination by the SCF(FBXL2) complex.|||Does not affect ability to activate the NLRP3 inflammasome.|||Does not affect ability to homooligomerize into ordered polymers.|||Does not affect activation of the NLRP3 inflammasome.|||Does not affect autoinhibition of the protein.|||Does not affect ubiquitination by the SCF(FBXL2) complex.|||FISNA|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||Impaired ability to activate the NLRP3 inflammasome.|||Impaired ability to homooligomerize into ordered polymers.|||Impaired ability to homooligomerize into ordered polymers. Complete loss of PYCARD/ASC filament nucleation.|||Impaired ability to homooligomerize into ordered polymers. Decreased PYCARD/ASC filament nucleation.|||In CINCA and MWS; spontaneous polymerization into inflammasome speck.|||In CINCA.|||In DFNA34; unknown pathological significance; increases inflammatory response.|||In FCAS1 and MWS.|||In FCAS1 and MWS; spontaneous polymerization into inflammasome speck.|||In FCAS1.|||In KEFH; does not affect ability to homooligomerize into ordered polymers.|||In MWS and CINCA; spontaneous polymerization into inflammasome speck.|||In MWS.|||In Walker A mutant; abolished ATPase activity. Reduced ATP-binding leading to decreased activation of the NLRP3 inflammasome.|||In Walker B mutant; abolished ATPase activity. Abolished binding to small-inhibitor MCC950.|||In isoform 1 and isoform 4.|||In isoform 1 and isoform 5.|||In isoform 3.|||In isoform 6.|||Induces the formation of short but ordered homopolymers.|||KFERQ-like motif 1|||KFERQ-like motif 2|||KFERQ-like motif 3|||KFERQ-like motif 4|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Loss of PYCARD/ASC-binding. No effect on GBP5-binding.|||Loss of autoinhibition of the protein.|||Mimicks phosphorylation state; increased activation of the NLRP3 inflammasome.|||Mimics phosphorylation state; decreased activation of the NLRP3 inflammasome.|||NACHT|||NACHT, LRR and PYD domains-containing protein 3|||Phosphoserine|||Phosphoserine; by CSNK1A1|||Phosphoserine; by MAPK8|||Phosphotyrosine|||Phosphotyrosine; by BTK|||Pyrin|||Redox-active|||Required for binding to phosphatidylinositol 4-phosphate (PtdIns4P)|||S-palmitoyl cysteine|||Slightly decreased ability to activate the NLRP3 inflammasome; when associated with D-816.|||Slightly decreased ability to activate the NLRP3 inflammasome; when associated with E-788.|||Slightly decreased ability to activate the NLRP3 inflammasome; when associated with E-813.|||Slightly decreased ability to activate the NLRP3 inflammasome; when associated with R-789.|||Slightly impaired autoinhibition of the protein; when associated with 788-A-R-789.|||Slightly impaired autoinhibition of the protein; when associated with A-831.|||Strongly decreased ability to activate the NLRP3 inflammasome.|||Strongly decreased interaction with MAVS and localization to mitochondria. ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080886|||http://purl.uniprot.org/annotation/VAR_013227|||http://purl.uniprot.org/annotation/VAR_013228|||http://purl.uniprot.org/annotation/VAR_013229|||http://purl.uniprot.org/annotation/VAR_013230|||http://purl.uniprot.org/annotation/VAR_014104|||http://purl.uniprot.org/annotation/VAR_014105|||http://purl.uniprot.org/annotation/VAR_014106|||http://purl.uniprot.org/annotation/VAR_014107|||http://purl.uniprot.org/annotation/VAR_014108|||http://purl.uniprot.org/annotation/VAR_014124|||http://purl.uniprot.org/annotation/VAR_014366|||http://purl.uniprot.org/annotation/VAR_014367|||http://purl.uniprot.org/annotation/VAR_014368|||http://purl.uniprot.org/annotation/VAR_014369|||http://purl.uniprot.org/annotation/VAR_014370|||http://purl.uniprot.org/annotation/VAR_023551|||http://purl.uniprot.org/annotation/VAR_031853|||http://purl.uniprot.org/annotation/VAR_043679|||http://purl.uniprot.org/annotation/VAR_043680|||http://purl.uniprot.org/annotation/VAR_043681|||http://purl.uniprot.org/annotation/VAR_043682|||http://purl.uniprot.org/annotation/VAR_043683|||http://purl.uniprot.org/annotation/VAR_043684|||http://purl.uniprot.org/annotation/VAR_043685|||http://purl.uniprot.org/annotation/VAR_043686|||http://purl.uniprot.org/annotation/VAR_043687|||http://purl.uniprot.org/annotation/VAR_043688|||http://purl.uniprot.org/annotation/VAR_043689|||http://purl.uniprot.org/annotation/VAR_043690|||http://purl.uniprot.org/annotation/VAR_043691|||http://purl.uniprot.org/annotation/VAR_043692|||http://purl.uniprot.org/annotation/VAR_043693|||http://purl.uniprot.org/annotation/VAR_080490|||http://purl.uniprot.org/annotation/VAR_081008|||http://purl.uniprot.org/annotation/VSP_005519|||http://purl.uniprot.org/annotation/VSP_005520|||http://purl.uniprot.org/annotation/VSP_005521|||http://purl.uniprot.org/annotation/VSP_053714
http://togogenome.org/gene/9606:GLOD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HC38                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glyoxalase domain-containing protein 4|||In isoform 2 and isoform 3.|||In isoform 3.|||N6-succinyllysine|||Phosphoserine|||VOC 1|||VOC 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280391|||http://purl.uniprot.org/annotation/VAR_031128|||http://purl.uniprot.org/annotation/VSP_023646|||http://purl.uniprot.org/annotation/VSP_023647|||http://purl.uniprot.org/annotation/VSP_023648
http://togogenome.org/gene/9606:RAB6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P20340|||http://purl.uniprot.org/uniprot/Q53ET8                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Effector region|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||Loss of APBA1-binding. No loss of RIC1- and RGP1-binding.|||Loss of GTPase activity. Interacts with APBA1.|||Loss of RAB6IP1-binding.|||N-acetylserine|||O-AMP-tyrosine; by Legionella DrrA|||Phosphoserine|||Ras-related protein Rab-6A|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121112|||http://purl.uniprot.org/annotation/VSP_005527|||http://purl.uniprot.org/annotation/VSP_045302|||http://purl.uniprot.org/annotation/VSP_046967
http://togogenome.org/gene/9606:NME2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F6XY72|||http://purl.uniprot.org/uniprot/P22392|||http://purl.uniprot.org/uniprot/Q6FHN3                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Decreased single-stranded DNA-binding and nucleotide-binding activity. No effect on 3D-structure.|||In isoform 3.|||Interaction with AKAP13|||Nucleoside diphosphate kinase B|||Nucleoside diphosphate kinase-like|||Pros-phosphohistidine intermediate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137117|||http://purl.uniprot.org/annotation/VSP_036708
http://togogenome.org/gene/9606:IFITM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P13164                                                                                  ^@                                                                                  Chain|||Experimental Information|||INTRAMEM|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||INTRAMEM|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Interaction with CAV1|||Interferon-induced transmembrane protein 1|||Loss of anti-HCV activity. Only localizes at the lysosome.|||No effect on anti-HCV activity. Only localizes at the lysosome.|||Phosphoserine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153727|||http://purl.uniprot.org/annotation/VAR_047422
http://togogenome.org/gene/9606:PMEL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P40967                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||10|||11|||12|||12 X 13 AA approximate tandem repeats, RPT domain|||2|||3|||4|||5|||6|||7|||8|||9|||Abolishes disulfide linkage rearrangement that converts dimer to monomer.|||Abolishes interchain and intrachain disulfide linkage formation.|||Amyloidogenic unit|||Antigenic peptide; presented by A*02:01|||Cleavage; by ADAM metalloproteinases|||Cleavage; by furin-like proprotein convertase|||Cytoplasmic|||Disordered|||Does not affect dimer formation.|||ER exit signal|||Endocytosis signal|||Essential for fibril formation|||Forms fibrils at normal levels.|||Has normal fibril formation.|||Has normal fibril formation. Reduces fibril formation; when associated with L-207.|||Has normal fibril formation. Reduces fibril formation; when associated with L-215.|||Helical|||Impairs the cleavage of the C-terminal fragment.|||In isoform 2 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||Interchain (in monomeric form)|||Intrachain (in dimeric form)|||Kringle-like fold|||Leads to inefficient ER exit, endocytic trafficking and protein maturation.|||Leads to inefficient ER exit.|||Leads to inefficient endocytic trafficking.|||Loss of proteolytic cleavage.|||Loss-of-function. Abolishes fibril formation. Does not exert dominant negative effect; when associated with A-211.|||Loss-of-function. Abolishes fibrillar amyloid formation. Does not exert dominant negative effect and retains the amyloidogenic potential; when associated with A-211.|||Loss-of-function. Likely misfolded and rapidly degraded.|||Loss-of-function. Retained in the endoplasmic reticulum likely due to misfolding.|||Lumenal|||M-alpha|||M-beta|||Markedly reduces fibril formation.|||Markedly reduces fibril formation. Does not exert dominant negative effect; when associated with A-211.|||Melanocyte protein PMEL|||N-linked (GlcNAc...) asparagine|||PKD|||Reduces fibril formation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000024712|||http://purl.uniprot.org/annotation/PRO_0000292263|||http://purl.uniprot.org/annotation/PRO_0000386648|||http://purl.uniprot.org/annotation/VAR_050606|||http://purl.uniprot.org/annotation/VAR_050607|||http://purl.uniprot.org/annotation/VSP_038266|||http://purl.uniprot.org/annotation/VSP_038267|||http://purl.uniprot.org/annotation/VSP_038268
http://togogenome.org/gene/9606:GPATCH8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKJ3                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||C2H2-type|||Disordered|||G patch domain-containing protein 8|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050761|||http://purl.uniprot.org/annotation/VAR_059658|||http://purl.uniprot.org/annotation/VAR_059659|||http://purl.uniprot.org/annotation/VAR_067000|||http://purl.uniprot.org/annotation/VAR_067001|||http://purl.uniprot.org/annotation/VAR_067002|||http://purl.uniprot.org/annotation/VSP_037683|||http://purl.uniprot.org/annotation/VSP_037684|||http://purl.uniprot.org/annotation/VSP_037685
http://togogenome.org/gene/9606:RBL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q08999                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Domain A|||Domain B|||In BRUWAG.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pocket; binds E1A|||Polar residues|||Pro residues|||Retinoblastoma-like protein 2|||Spacer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000167841|||http://purl.uniprot.org/annotation/VAR_028437|||http://purl.uniprot.org/annotation/VAR_069377|||http://purl.uniprot.org/annotation/VAR_086722|||http://purl.uniprot.org/annotation/VSP_054328|||http://purl.uniprot.org/annotation/VSP_054329
http://togogenome.org/gene/9606:TMPRSS12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJY1|||http://purl.uniprot.org/uniprot/Q86WS5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Found in a patient with azoospermia; unknown pathological significance.|||Found in patients with azoospermia; unknown pathological significance.|||Helical|||N-linked (GlcNAc...) asparagine|||Peptidase S1|||Transmembrane protease serine 12                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000290438|||http://purl.uniprot.org/annotation/PRO_5007491789|||http://purl.uniprot.org/annotation/VAR_051848|||http://purl.uniprot.org/annotation/VAR_051849|||http://purl.uniprot.org/annotation/VAR_051850|||http://purl.uniprot.org/annotation/VAR_088098|||http://purl.uniprot.org/annotation/VAR_088099|||http://purl.uniprot.org/annotation/VAR_088100|||http://purl.uniprot.org/annotation/VAR_088101|||http://purl.uniprot.org/annotation/VAR_088102|||http://purl.uniprot.org/annotation/VAR_088103
http://togogenome.org/gene/9606:SERBP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VU21|||http://purl.uniprot.org/uniprot/Q63HR1|||http://purl.uniprot.org/uniprot/Q8NC51                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Hyaluronan/mRNA-binding protein|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N6-acetyllysine|||N6-acetyllysine; alternate|||Not sumoylated; when associated with R-102 and R-228.|||Not sumoylated; when associated with R-102 and R-281.|||Not sumoylated; when associated with R-228 and R-281.|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by MTOR|||Phosphothreonine|||Phosphothreonine; by MTOR|||Polar residues|||Removed|||SERPINE1 mRNA-binding protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058182|||http://purl.uniprot.org/annotation/VSP_011630|||http://purl.uniprot.org/annotation/VSP_011631
http://togogenome.org/gene/9606:CACNG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFR2|||http://purl.uniprot.org/uniprot/A6NP74|||http://purl.uniprot.org/uniprot/Q9BXT2                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Voltage-dependent calcium channel gamma-6 subunit                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164684|||http://purl.uniprot.org/annotation/VAR_061540
http://togogenome.org/gene/9606:S100P                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P25815                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  EF-hand 1|||EF-hand 2|||In S100Ppa; permanently active, interacts with EZR and PPP5C in absence of calcium; when associated with 21-S--G-23, C-64 and K-68.|||In S100Ppa; permanently active, interacts with EZR and PPP5C in absence of calcium; when associated with 21-S--G-23, C-64 and S-73.|||In S100Ppa; permanently active, interacts with EZR and PPP5C in absence of calcium; when associated with 21-S--G-23, K-68 and S-73.|||In S100Ppa; permanently active, interacts with EZR and PPP5C in absence of calcium; when associated with C-64, K-68 and S-73.|||Protein S100-P                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144032
http://togogenome.org/gene/9606:OR8D1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVG6|||http://purl.uniprot.org/uniprot/Q8WZ84                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8D1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150659|||http://purl.uniprot.org/annotation/VAR_024116|||http://purl.uniprot.org/annotation/VAR_053242|||http://purl.uniprot.org/annotation/VAR_053243
http://togogenome.org/gene/9606:ZNF256                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2P7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 256                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047489|||http://purl.uniprot.org/annotation/VAR_058326|||http://purl.uniprot.org/annotation/VSP_037721
http://togogenome.org/gene/9606:OSGIN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UJX0                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Oxidative stress-induced growth inhibitor 1|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000165371|||http://purl.uniprot.org/annotation/VAR_056575
http://togogenome.org/gene/9606:COPS5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R7W9|||http://purl.uniprot.org/uniprot/Q92905                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Sequence Conflict|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to deneddylate cullins, without affecting the 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex.|||COP9 signalosome complex subunit 5|||JAMM motif|||MPN|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194835
http://togogenome.org/gene/9606:ATP1A2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3W6|||http://purl.uniprot.org/uniprot/P50993                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Propeptide|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  4-aspartylphosphate intermediate|||Cation-transporting P-type ATPase N-terminal|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AHC1.|||In DEE98.|||In DEE98; decreased affinity for sodium ions; decreased affinity for potassium ions.|||In DEE98; decreased sodium/potassium-exchanging ATPase activity.|||In DEE98; decreased sodium/potassium-exchanging ATPase activity; decreased affinity for sodium ions.|||In FARIMPD; unknown pathological significance.|||In FHM2.|||In FHM2; de novo mutation in a sporadic case.|||In FHM2; loss of function.|||In FHM2; some patients exhibit a clinical overlap between migraine and epilepsy.|||Interaction with phosphoinositide-3 kinase|||Phosphoserine|||Phosphoserine; by PKA|||Phosphothreonine|||Polar residues|||Probable disease-associated variant found in a patient with generalized tonic-clonic seizures; decreased sodium/potassium-exchanging ATPase activity.|||Sodium/potassium-transporting ATPase subunit alpha-2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002503|||http://purl.uniprot.org/annotation/PRO_0000002504|||http://purl.uniprot.org/annotation/VAR_019934|||http://purl.uniprot.org/annotation/VAR_019935|||http://purl.uniprot.org/annotation/VAR_019936|||http://purl.uniprot.org/annotation/VAR_019937|||http://purl.uniprot.org/annotation/VAR_019938|||http://purl.uniprot.org/annotation/VAR_065685|||http://purl.uniprot.org/annotation/VAR_069991|||http://purl.uniprot.org/annotation/VAR_069992|||http://purl.uniprot.org/annotation/VAR_078231|||http://purl.uniprot.org/annotation/VAR_078232|||http://purl.uniprot.org/annotation/VAR_086441|||http://purl.uniprot.org/annotation/VAR_086442|||http://purl.uniprot.org/annotation/VAR_086443|||http://purl.uniprot.org/annotation/VAR_086444|||http://purl.uniprot.org/annotation/VAR_086445
http://togogenome.org/gene/9606:DNAJC22                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4W6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Transmembrane                                                                                  ^@                                                                                  DnaJ homolog subfamily C member 22|||Helical|||J                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325862
http://togogenome.org/gene/9606:OS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13438                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||In isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 4 and isoform 8.|||In isoform 5 and isoform 7.|||In isoform 5.|||In isoform 6.|||In isoform 8.|||Loss of glycan-binding activity and partial inhibition of ERAD of the misfolded glycoprotein NHK (PubMed:19346256). Reduced interaction with SEL1L (PubMed:18264092) not confirmed in (PubMed:19346256).|||MRH|||N-linked (GlcNAc...) asparagine|||Protein OS-9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021951|||http://purl.uniprot.org/annotation/VAR_011897|||http://purl.uniprot.org/annotation/VAR_034364|||http://purl.uniprot.org/annotation/VAR_069062|||http://purl.uniprot.org/annotation/VSP_004352|||http://purl.uniprot.org/annotation/VSP_004353|||http://purl.uniprot.org/annotation/VSP_044701|||http://purl.uniprot.org/annotation/VSP_044702|||http://purl.uniprot.org/annotation/VSP_046001|||http://purl.uniprot.org/annotation/VSP_046770
http://togogenome.org/gene/9606:LMNB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DZT3|||http://purl.uniprot.org/uniprot/P20700                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Cysteine methyl ester|||Disordered|||Found in a family with amyotrophic lateral sclerosis carrying a probable causative mutation in MATR3; unknown pathological significance.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Head|||IF rod|||In ADLD; unknown pathological significance; no effect on localization to nuclear lamina.|||In MCPH26; decreased localization to nuclear lamina; changed nuclear envelope organization; increased aggregation.|||In MCPH26; decreased localization to nuclear lamina; increased aggregation; changed nuclear envelope organization.|||In MCPH26; decreased protein abundance; changed localization to nuclear lamina; changed nuclear envelope organization.|||In MCPH26; increased aggregation; changed nuclear envelope organization.|||Interchain|||LTD|||Lamin-B1|||Linker 1|||Linker 2|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||No effect on localization to nuclear lamina.|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed|||Removed in mature form|||S-farnesyl cysteine|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063816|||http://purl.uniprot.org/annotation/PRO_0000393945|||http://purl.uniprot.org/annotation/VAR_031646|||http://purl.uniprot.org/annotation/VAR_071077|||http://purl.uniprot.org/annotation/VAR_085497|||http://purl.uniprot.org/annotation/VAR_085498|||http://purl.uniprot.org/annotation/VAR_085499|||http://purl.uniprot.org/annotation/VAR_085500|||http://purl.uniprot.org/annotation/VAR_085501|||http://purl.uniprot.org/annotation/VAR_085502|||http://purl.uniprot.org/annotation/VAR_085503
http://togogenome.org/gene/9606:PIP4P2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N4L2                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Region|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Region|||Transmembrane                                                                                  ^@                                                                                  CX5R motif|||Disordered|||Helical|||Phosphoserine|||Phosphothreonine|||Polar residues|||Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000235228
http://togogenome.org/gene/9606:PIK3R3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXM8|||http://purl.uniprot.org/uniprot/Q68CY7|||http://purl.uniprot.org/uniprot/Q7Z3W2|||http://purl.uniprot.org/uniprot/Q8N381|||http://purl.uniprot.org/uniprot/Q92569                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Phosphatidylinositol 3-kinase regulatory subunit gamma|||Phosphotyrosine|||SH2|||SH2 1|||SH2 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080767|||http://purl.uniprot.org/annotation/VAR_047153|||http://purl.uniprot.org/annotation/VSP_004713|||http://purl.uniprot.org/annotation/VSP_004714
http://togogenome.org/gene/9606:KLHDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2U9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Mutagenesis Site|||Repeat|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolished ability to recognize truncated SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the C-terminus.|||Abolished ability to recognize truncated SELENOK with a diglycine (Gly-Gly) at the C-terminus.|||Does not affect ability to recognize truncated SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the C-terminus.|||Does not affect ability to recognize truncated SELENOK with a diglycine (Gly-Gly) at the C-terminus.|||Does not affect ability to recognize truncated SELENOK with a diglycine (Gly-Gly) at the C-terminus. Abolished ability to recognize cleaved USP1 with a diglycine (Gly-Gly) at the C-terminus.|||In isoform 2.|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch domain-containing protein 2|||Strongly impaired ability to recognize truncated SELENOK or cleaved USP1 with a diglycine (Gly-Gly) at the C-terminus.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119127|||http://purl.uniprot.org/annotation/VSP_030165|||http://purl.uniprot.org/annotation/VSP_030166
http://togogenome.org/gene/9606:BAG6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7A6|||http://purl.uniprot.org/uniprot/P46379                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  1|||2|||3|||4|||4 X 29 AA approximate repeats|||Abolishes cleavage by the caspase CASP3.|||BAG-similar domain, required and sufficient for interaction with UBL4A|||Basic and acidic residues|||Cleavage; by CASP3|||Decreases interaction with GET4. Localizes in the nucleus and cytoplasm. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042.|||Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1010 or A-1018.|||Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042.|||Disordered|||In isoform 2, isoform 3, isoform 4 and isoform 5.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||Large proline-rich protein BAG6|||N-acetylmethionine|||No effect on interaction with GET4 and KPNA2.|||No effect on interaction with GET4. Inhibits interaction with KPNA2.|||No effect on interaction with UBL4A.|||No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with A-1078. Abolishes on interaction with UBL4A; when associated with R-1085.|||No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with R-1067 or R-1085.|||No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with R-1078. Abolishes on interaction with UBL4A; when associated with R-1067.|||Nuclear localization site|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues|||Required for interaction with GET4|||Sufficient for the delivery of client proteins to the endoplasmic reticulum|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000114897|||http://purl.uniprot.org/annotation/VAR_023531|||http://purl.uniprot.org/annotation/VAR_037150|||http://purl.uniprot.org/annotation/VSP_015695|||http://purl.uniprot.org/annotation/VSP_030519|||http://purl.uniprot.org/annotation/VSP_045910|||http://purl.uniprot.org/annotation/VSP_045911|||http://purl.uniprot.org/annotation/VSP_045912|||http://purl.uniprot.org/annotation/VSP_045913
http://togogenome.org/gene/9606:QTRT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q71RF8|||http://purl.uniprot.org/uniprot/Q9BXR0                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Loss of transglycosylase activity.|||N-acetylalanine|||Nucleophile|||Phosphoserine|||Proton acceptor|||Queuine tRNA-ribosyltransferase catalytic subunit 1|||RNA binding|||RNA binding; important for wobble base 34 recognition|||Removed|||tRNA-guanine(15) transglycosylase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135565|||http://purl.uniprot.org/annotation/VSP_056470|||http://purl.uniprot.org/annotation/VSP_056471
http://togogenome.org/gene/9606:PMPCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10713|||http://purl.uniprot.org/uniprot/Q5SXN9                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mass|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  In SCAR2.|||In SCAR2; impairs cleavage of FXN; does not impair cleavage of DLD, NFS1 and PRDX3.|||In isoform 2.|||Mitochondrial-processing peptidase subunit alpha|||Mitochondrion|||N6-acetyllysine|||N6-succinyllysine|||Peptidase M16 C-terminal|||Peptidase M16 N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000026767|||http://purl.uniprot.org/annotation/VAR_076237|||http://purl.uniprot.org/annotation/VAR_076238|||http://purl.uniprot.org/annotation/VAR_076239|||http://purl.uniprot.org/annotation/VAR_076240|||http://purl.uniprot.org/annotation/VSP_054916|||http://purl.uniprot.org/annotation/VSP_054917
http://togogenome.org/gene/9606:MLH3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M1Z1|||http://purl.uniprot.org/uniprot/Q9UHC1                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DNA mismatch repair protein Mlh3|||DNA mismatch repair protein S5|||Disordered|||In HNPCC7.|||In isoform 2.|||MutL C-terminal dimerisation                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000178003|||http://purl.uniprot.org/annotation/VAR_010790|||http://purl.uniprot.org/annotation/VAR_012946|||http://purl.uniprot.org/annotation/VAR_012947|||http://purl.uniprot.org/annotation/VAR_012948|||http://purl.uniprot.org/annotation/VAR_012949|||http://purl.uniprot.org/annotation/VAR_012950|||http://purl.uniprot.org/annotation/VAR_012951|||http://purl.uniprot.org/annotation/VAR_012952|||http://purl.uniprot.org/annotation/VAR_012953|||http://purl.uniprot.org/annotation/VAR_012954|||http://purl.uniprot.org/annotation/VAR_023338|||http://purl.uniprot.org/annotation/VAR_023339|||http://purl.uniprot.org/annotation/VAR_023340|||http://purl.uniprot.org/annotation/VAR_023341|||http://purl.uniprot.org/annotation/VAR_023342|||http://purl.uniprot.org/annotation/VAR_023343|||http://purl.uniprot.org/annotation/VAR_023344|||http://purl.uniprot.org/annotation/VAR_023345|||http://purl.uniprot.org/annotation/VAR_023346|||http://purl.uniprot.org/annotation/VAR_023347|||http://purl.uniprot.org/annotation/VAR_023348|||http://purl.uniprot.org/annotation/VAR_023349|||http://purl.uniprot.org/annotation/VAR_023350|||http://purl.uniprot.org/annotation/VAR_023351|||http://purl.uniprot.org/annotation/VAR_023352|||http://purl.uniprot.org/annotation/VAR_023353|||http://purl.uniprot.org/annotation/VAR_023354|||http://purl.uniprot.org/annotation/VAR_023355|||http://purl.uniprot.org/annotation/VAR_023356|||http://purl.uniprot.org/annotation/VAR_036781|||http://purl.uniprot.org/annotation/VSP_003290
http://togogenome.org/gene/9606:AIFM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z376|||http://purl.uniprot.org/uniprot/Q96NN9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Apoptosis-inducing factor 3|||Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||Rieske                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000255660|||http://purl.uniprot.org/annotation/VAR_061553|||http://purl.uniprot.org/annotation/VSP_021300|||http://purl.uniprot.org/annotation/VSP_021303
http://togogenome.org/gene/9606:SPACA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJN7|||http://purl.uniprot.org/uniprot/Q96QH8                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Domain Extent|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  C-type lysozyme|||Sperm acrosome-associated protein 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284470|||http://purl.uniprot.org/annotation/PRO_5010061088
http://togogenome.org/gene/9606:ZBTB14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R850|||http://purl.uniprot.org/uniprot/O43829                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||BTB|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Nuclear localization signal|||Polar residues|||Zinc finger and BTB domain-containing protein 14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047317|||http://purl.uniprot.org/annotation/VAR_027810|||http://purl.uniprot.org/annotation/VAR_027811
http://togogenome.org/gene/9606:BMF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96LC9                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  BH3|||Bcl-2-modifying factor|||In isoform 2.|||In isoform 3.|||Interaction with DLC2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143111|||http://purl.uniprot.org/annotation/VSP_012292|||http://purl.uniprot.org/annotation/VSP_012293|||http://purl.uniprot.org/annotation/VSP_012294
http://togogenome.org/gene/9606:CCDC157                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q569K6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 157|||Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319420|||http://purl.uniprot.org/annotation/VAR_038999|||http://purl.uniprot.org/annotation/VAR_039000|||http://purl.uniprot.org/annotation/VAR_060124
http://togogenome.org/gene/9606:H2BW1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z2G1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Histone H2B type W-T|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244828|||http://purl.uniprot.org/annotation/VAR_049315|||http://purl.uniprot.org/annotation/VAR_054318
http://togogenome.org/gene/9606:TAF1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53T94                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes Pol I transcription but not recruitment of SL1/TIF-IB complex to rDNA promoters.|||B-linker|||B-reader|||C-terminal cyclin fold|||In isoform 2.|||In isoform 3.|||N-acetylmethionine|||N-terminal cyclin fold|||N6-acetyllysine|||RRN7-type|||TATA box-binding protein-associated factor RNA polymerase I subunit B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000261392|||http://purl.uniprot.org/annotation/VAR_029378|||http://purl.uniprot.org/annotation/VAR_029379|||http://purl.uniprot.org/annotation/VAR_029380|||http://purl.uniprot.org/annotation/VAR_029381|||http://purl.uniprot.org/annotation/VAR_029382|||http://purl.uniprot.org/annotation/VAR_057260|||http://purl.uniprot.org/annotation/VSP_021677|||http://purl.uniprot.org/annotation/VSP_042954
http://togogenome.org/gene/9606:DHCR24                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15392                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cleavage; by caspase|||Cytoplasmic|||Delta(24)-sterol reductase|||FAD-binding PCMH-type|||Helical|||In DESMOS; complete loss of ability to convert desmosterol to cholesterol.|||In DESMOS; decreases production of cholesterol from desmosterol.|||In isoform 2.|||Lumenal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007230|||http://purl.uniprot.org/annotation/VAR_012732|||http://purl.uniprot.org/annotation/VAR_012733|||http://purl.uniprot.org/annotation/VAR_012734|||http://purl.uniprot.org/annotation/VAR_012735|||http://purl.uniprot.org/annotation/VAR_081889|||http://purl.uniprot.org/annotation/VAR_081890|||http://purl.uniprot.org/annotation/VSP_056479
http://togogenome.org/gene/9606:CYBRD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53TN4                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytochrome b561|||Cytoplasmic|||Decreased heme b reduction by ascorbate.|||Decreased transmembrane ascorbate ferrireductase activity.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||In isoform 3.|||In some patients with hereditary hemochromatosis.|||Loss of iron binding. Loss of transmembrane ascorbate ferrireductase activity.|||Loss of transmembrane ascorbate ferrireductase activity.|||Phosphoserine|||Phosphothreonine|||Plasma membrane ascorbate-dependent reductase CYBRD1|||Polar residues|||axial binding residue                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000314830|||http://purl.uniprot.org/annotation/VAR_038065|||http://purl.uniprot.org/annotation/VAR_038066|||http://purl.uniprot.org/annotation/VAR_038067|||http://purl.uniprot.org/annotation/VSP_042039|||http://purl.uniprot.org/annotation/VSP_044945
http://togogenome.org/gene/9606:KRTAP19-8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3LI54                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Keratin-associated protein 19-8                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000307914|||http://purl.uniprot.org/annotation/VAR_053476
http://togogenome.org/gene/9606:RELB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q01201                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In IMD53.|||Leucine-zipper|||Nuclear localization signal|||Omega-N-methylarginine|||Phosphoserine|||RHD|||Transcription factor RelB                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205173|||http://purl.uniprot.org/annotation/VAR_051782|||http://purl.uniprot.org/annotation/VAR_079201
http://togogenome.org/gene/9606:EXOSC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPD3                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Strand|||Turn                                                                                  ^@                                                                                  Exosome complex component RRP41|||N-acetylalanine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000139958
http://togogenome.org/gene/9606:NUDT15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NV35                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Motif|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Associated with increased risk for thiopurines toxicity; decreased thermostability; decreased diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP.|||Associated with increased risk for thiopurines toxicity; decreased thermostability; loss of diphosphatase activity towards 6-thio-dGTP and 6-thio-GTP.|||Interaction with PCNA|||Nucleotide triphosphate diphosphatase NUDT15|||Nudix box|||Nudix hydrolase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057115|||http://purl.uniprot.org/annotation/VAR_076806|||http://purl.uniprot.org/annotation/VAR_076807|||http://purl.uniprot.org/annotation/VAR_076808|||http://purl.uniprot.org/annotation/VAR_076809
http://togogenome.org/gene/9606:IQCM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GVH7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Domain Extent|||Region                                                                                  ^@                                                                                  Disordered|||IQ|||IQ domain-containing protein M                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000441625
http://togogenome.org/gene/9606:KLHL42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RNT7|||http://purl.uniprot.org/uniprot/F5H523|||http://purl.uniprot.org/uniprot/Q9P2K6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Repeat                                                                                  ^@                                                                                  BTB|||Kelch 1|||Kelch 2|||Kelch 3|||Kelch 4|||Kelch 5|||Kelch 6|||Kelch-like protein 42|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119128
http://togogenome.org/gene/9606:ISG20L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9L3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Exonuclease|||Interferon-stimulated 20 kDa exonuclease-like 2|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084121|||http://purl.uniprot.org/annotation/VAR_038171
http://togogenome.org/gene/9606:GOLM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4E1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||In isoform 5.|||Lumenal|||N-acetylmethionine|||Phosphoserine|||Polar residues|||Protein GOLM2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291843|||http://purl.uniprot.org/annotation/VSP_060178|||http://purl.uniprot.org/annotation/VSP_060179|||http://purl.uniprot.org/annotation/VSP_060180|||http://purl.uniprot.org/annotation/VSP_060181
http://togogenome.org/gene/9606:AK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P00568|||http://purl.uniprot.org/uniprot/Q5T9B7|||http://purl.uniprot.org/uniprot/Q6FGX9                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Adenylate kinase isoenzyme 1|||In HAAKD.|||In HAAKD; the same mutation in the chicken sequence shows reduced adenylate kinase activity.|||LID|||N-acetylmethionine|||NMP|||NMPbind|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000158910|||http://purl.uniprot.org/annotation/VAR_004021|||http://purl.uniprot.org/annotation/VAR_034046|||http://purl.uniprot.org/annotation/VAR_055337|||http://purl.uniprot.org/annotation/VAR_055338|||http://purl.uniprot.org/annotation/VAR_055339|||http://purl.uniprot.org/annotation/VAR_055340
http://togogenome.org/gene/9606:SENP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P0U3                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes SUMO2 processing and SUMO2 deconjugating activities.|||Disordered|||Exclusively nuclear. Loss of CCAR2 desumoylation.|||Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity.|||Impairs SUMO2 processing and SUMO2 deconjugating activities.|||In isoform 2.|||Interaction with CCAR2|||No effect on SUMO2 processing and SUMO2 deconjugating activities.|||Nuclear export signal|||Nuclear localization signal|||Nucleophile|||Phosphoserine|||Protease|||Sentrin-specific protease 1|||Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000101716|||http://purl.uniprot.org/annotation/VAR_029648|||http://purl.uniprot.org/annotation/VAR_029649|||http://purl.uniprot.org/annotation/VAR_047547|||http://purl.uniprot.org/annotation/VSP_035777
http://togogenome.org/gene/9606:SSX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16384                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form the SSXT-SSX1 fusion protein|||Breakpoint for translocation to form the SSXT-SSX1 fusion protein (rare)|||Disordered|||In SPGFX5; unknown pathological significance.|||KRAB-related|||Phosphoserine|||Protein SSX1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181828|||http://purl.uniprot.org/annotation/VAR_088251
http://togogenome.org/gene/9606:GPR182                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15218                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptor 182|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069112|||http://purl.uniprot.org/annotation/VAR_033464
http://togogenome.org/gene/9606:SUGP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IWZ8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||G-patch|||In isoform 2.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SURP and G-patch domain-containing protein 1|||SURP motif 1|||SURP motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097701|||http://purl.uniprot.org/annotation/VAR_051339|||http://purl.uniprot.org/annotation/VAR_051340|||http://purl.uniprot.org/annotation/VSP_013109|||http://purl.uniprot.org/annotation/VSP_013110
http://togogenome.org/gene/9606:CT47A12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5JQC4                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Cancer/testis antigen 47A|||Disordered|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000284450
http://togogenome.org/gene/9606:CD46                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P15529                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In AHUS2.|||In AHUS2; no cell surface expression.|||In AHUS2; no change in cell surface expression but reduced activity.|||In AHUS2; reduced cell surface expression.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform B, isoform D, isoform F, isoform H, isoform J, isoform L and isoform 3.|||In isoform C, isoform D, isoform I, isoform J and isoform M.|||In isoform E, isoform F and isoform N.|||In isoform G, isoform H, isoform I and isoform J.|||In isoform K and isoform L.|||In isoform M.|||In isoform N.|||Membrane cofactor protein|||N-linked (GlcNAc...) asparagine|||No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding.|||O-linked (GalNAc...) serine|||O-linked (GalNAc...) threonine|||Phosphotyrosine|||Polar residues|||Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding.|||Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding.|||Sushi 1|||Sushi 2|||Sushi 3|||Sushi 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000006008|||http://purl.uniprot.org/annotation/VAR_022262|||http://purl.uniprot.org/annotation/VAR_022263|||http://purl.uniprot.org/annotation/VAR_022264|||http://purl.uniprot.org/annotation/VAR_022265|||http://purl.uniprot.org/annotation/VAR_026567|||http://purl.uniprot.org/annotation/VAR_026568|||http://purl.uniprot.org/annotation/VAR_026569|||http://purl.uniprot.org/annotation/VAR_026570|||http://purl.uniprot.org/annotation/VAR_026571|||http://purl.uniprot.org/annotation/VAR_035828|||http://purl.uniprot.org/annotation/VAR_063656|||http://purl.uniprot.org/annotation/VAR_063657|||http://purl.uniprot.org/annotation/VAR_063658|||http://purl.uniprot.org/annotation/VSP_001201|||http://purl.uniprot.org/annotation/VSP_001202|||http://purl.uniprot.org/annotation/VSP_001203|||http://purl.uniprot.org/annotation/VSP_001204|||http://purl.uniprot.org/annotation/VSP_009174|||http://purl.uniprot.org/annotation/VSP_009175|||http://purl.uniprot.org/annotation/VSP_009176|||http://purl.uniprot.org/annotation/VSP_009177|||http://purl.uniprot.org/annotation/VSP_009178|||http://purl.uniprot.org/annotation/VSP_019005|||http://purl.uniprot.org/annotation/VSP_019006
http://togogenome.org/gene/9606:RMND5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H871                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  CTLH|||E3 ubiquitin-protein transferase RMND5A|||In isoform 2.|||LisH|||N-acetylmethionine|||RING-Gid-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272648|||http://purl.uniprot.org/annotation/VSP_022454|||http://purl.uniprot.org/annotation/VSP_022455
http://togogenome.org/gene/9606:CPNE8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YQ8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  C2 1|||C2 2|||Copine-8|||In isoform 2.|||Phosphoserine|||VWFA                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144849|||http://purl.uniprot.org/annotation/VSP_056287
http://togogenome.org/gene/9606:BTBD16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q32M84                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BTB|||BTB/POZ domain-containing protein 16|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247121|||http://purl.uniprot.org/annotation/VAR_027070|||http://purl.uniprot.org/annotation/VAR_027071|||http://purl.uniprot.org/annotation/VAR_027072|||http://purl.uniprot.org/annotation/VAR_027073|||http://purl.uniprot.org/annotation/VSP_019929
http://togogenome.org/gene/9606:FDXACB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BRP7                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  FDX-ACB|||Ferredoxin-fold anticodon-binding domain-containing protein 1|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325956|||http://purl.uniprot.org/annotation/VAR_060321|||http://purl.uniprot.org/annotation/VAR_060322|||http://purl.uniprot.org/annotation/VAR_062165|||http://purl.uniprot.org/annotation/VSP_056997
http://togogenome.org/gene/9606:SFT2D3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q587I9                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Lumenal|||Vesicle transport protein SFT2C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000238613|||http://purl.uniprot.org/annotation/VAR_026558
http://togogenome.org/gene/9606:PPP2R5E                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16537                                                                                  ^@                                                                                  Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071454|||http://purl.uniprot.org/annotation/VSP_054588|||http://purl.uniprot.org/annotation/VSP_055163
http://togogenome.org/gene/9606:TMEM191C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NGB0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Transmembrane protein 191C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000340717
http://togogenome.org/gene/9606:USE1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZ43                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||Vesicle transport protein USE1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215579|||http://purl.uniprot.org/annotation/VAR_021052|||http://purl.uniprot.org/annotation/VSP_012662|||http://purl.uniprot.org/annotation/VSP_012663|||http://purl.uniprot.org/annotation/VSP_012664|||http://purl.uniprot.org/annotation/VSP_012665
http://togogenome.org/gene/9606:CDC123                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75794                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict                                                                                  ^@                                                                                  Cell division cycle protein 123 homolog|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228662
http://togogenome.org/gene/9606:MMP7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P09237                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Motif|||Propeptide|||Sequence Variant|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Activation peptide|||Cysteine switch|||Matrilysin|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000028738|||http://purl.uniprot.org/annotation/PRO_0000028739|||http://purl.uniprot.org/annotation/VAR_006729|||http://purl.uniprot.org/annotation/VAR_021027|||http://purl.uniprot.org/annotation/VAR_021028
http://togogenome.org/gene/9606:MFSD11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43934                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Found in a patient with intellectual disability; unknown pathological significance.|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||UNC93-like protein MFSD11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305019|||http://purl.uniprot.org/annotation/VAR_035151|||http://purl.uniprot.org/annotation/VAR_084653|||http://purl.uniprot.org/annotation/VSP_028187
http://togogenome.org/gene/9606:PTPN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29074                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||FERM|||PDZ|||Phosphocysteine intermediate|||Phosphoserine|||Polar residues|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219434|||http://purl.uniprot.org/annotation/VAR_061033
http://togogenome.org/gene/9606:TAAR9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96RI9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Trace amine-associated receptor 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000070181|||http://purl.uniprot.org/annotation/VAR_049449
http://togogenome.org/gene/9606:UBA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TBC4                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes NEDD8 adenylation.|||Abolishes specificity for NEDD8.|||Abolishes thioester intermediate formation.|||Determines specificity for NEDD8|||Glycyl thioester intermediate|||Impairs NEDD8 transfer to UBE2M.|||In isoform 2.|||Interaction with NAE1|||Interaction with NEDD8|||Interaction with UBE2M N-terminus|||Interaction with UBE2M core domain|||N-acetylalanine|||NEDD8-activating enzyme E1 catalytic subunit|||No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M.|||No effect on NEDD8 adenylation.|||No effect on NEDD8 adenylation; impairs thioester intermediate formation.|||No effect on NEDD8 transfer to UBE2M.|||Reduces affinity for UBE2M.|||Reduces affinity for UBE2M; when associated with A-192 and A-195.|||Reduces affinity for UBE2M; when associated with A-192 and A-197.|||Reduces affinity for UBE2M; when associated with A-195 and A-197.|||Reduces affinity for UBE2M; when associated with A-214.|||Reduces affinity for UBE2M; when associated with A-217.|||Removed|||Strongly reduces NEDD8 adenylation.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000194941|||http://purl.uniprot.org/annotation/VAR_023945|||http://purl.uniprot.org/annotation/VSP_041127
http://togogenome.org/gene/9606:FKBP14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7V8|||http://purl.uniprot.org/uniprot/Q9NWM8                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Region|||Secondary Structure|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||N-linked (GlcNAc...) asparagine|||PPIase FKBP-type|||Peptidyl-prolyl cis-trans isomerase FKBP14|||Prevents secretion from ER|||peptidylprolyl isomerase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025521|||http://purl.uniprot.org/annotation/PRO_5014219318
http://togogenome.org/gene/9606:CNIH2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PI25                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Lumenal|||Protein cornichon homolog 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122225
http://togogenome.org/gene/9606:CASKIN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WXE0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Basic and acidic residues|||Caskin-2|||Disordered|||In isoform 2.|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Pro residues|||SAM 1|||SAM 2|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000066983|||http://purl.uniprot.org/annotation/VAR_060244|||http://purl.uniprot.org/annotation/VSP_040568
http://togogenome.org/gene/9606:DEFB129                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A384MEC8|||http://purl.uniprot.org/uniprot/Q9H1M3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Beta-defensin 129|||Disordered|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007005|||http://purl.uniprot.org/annotation/PRO_5036073203|||http://purl.uniprot.org/annotation/VAR_024327
http://togogenome.org/gene/9606:RASGRF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K270|||http://purl.uniprot.org/uniprot/Q13972|||http://purl.uniprot.org/uniprot/Q8IUU5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  DH|||Disordered|||IQ|||In isoform 2.|||In isoform 3.|||N-terminal Ras-GEF|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphoserine; by PLK2|||Polar residues|||Ras-GEF|||Ras-specific guanine nucleotide-releasing factor 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068880|||http://purl.uniprot.org/annotation/VSP_012032|||http://purl.uniprot.org/annotation/VSP_054072|||http://purl.uniprot.org/annotation/VSP_054073
http://togogenome.org/gene/9606:UMODL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5DID0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||EGF-like 1; calcium-binding|||EGF-like 2; calcium-binding|||EGF-like 3; calcium-binding|||EMI|||Extracellular|||Fibronectin type-III 1|||Fibronectin type-III 2|||Helical|||In isoform 2 and isoform 4.|||In isoform 3 and isoform 4.|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEA 1|||SEA 2|||Uromodulin-like 1|||WAP|||ZP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228127|||http://purl.uniprot.org/annotation/VAR_025668|||http://purl.uniprot.org/annotation/VAR_025669|||http://purl.uniprot.org/annotation/VAR_025670|||http://purl.uniprot.org/annotation/VAR_025671|||http://purl.uniprot.org/annotation/VAR_025672|||http://purl.uniprot.org/annotation/VAR_025673|||http://purl.uniprot.org/annotation/VAR_025674|||http://purl.uniprot.org/annotation/VAR_025675|||http://purl.uniprot.org/annotation/VAR_025676|||http://purl.uniprot.org/annotation/VAR_025677|||http://purl.uniprot.org/annotation/VAR_025678|||http://purl.uniprot.org/annotation/VAR_025679|||http://purl.uniprot.org/annotation/VAR_025680|||http://purl.uniprot.org/annotation/VAR_082944|||http://purl.uniprot.org/annotation/VAR_082945|||http://purl.uniprot.org/annotation/VAR_082946|||http://purl.uniprot.org/annotation/VSP_017658|||http://purl.uniprot.org/annotation/VSP_017659
http://togogenome.org/gene/9606:DDAH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2R644|||http://purl.uniprot.org/uniprot/B4DGT0|||http://purl.uniprot.org/uniprot/B4DYP1|||http://purl.uniprot.org/uniprot/B4E3V1|||http://purl.uniprot.org/uniprot/O94760                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N(G),N(G)-dimethylarginine dimethylaminohydrolase 1|||N-acetylalanine|||Nucleophile|||Proton donor|||Reduces enzyme activity about 10-fold, and affinity for asymmetric dimethylarginine about 7-fold.|||Reduces enzyme activity about 1000-fold, and affinity for asymmetric dimethylarginine about 100-fold.|||Reduces enzyme activity and affinity for asymmetric dimethylarginine about 12-fold.|||Removed|||S-nitrosocysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000171118|||http://purl.uniprot.org/annotation/VSP_043813
http://togogenome.org/gene/9606:SLC31A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15431                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Affects copper(2+) binding. Increases the efficiency of the reduction.|||Affects homotrimer formation; when associated with 40-A--A-45. Does not affect localization at the plasma membrane; when associated with 40-A--A-45.|||Affects homotrimer formation; when associated with 7-A--A-12. Does not affect localization at the plasma membrane; when associated with 7-A--A-12.|||Bis-His motif|||Cleavage|||Cysteine sulfenic acid (-SOH)|||Cytoplasmic|||Decreases affinity towards copper(1+).|||Decreases of 45-fold copper(1+) affinity.|||Decreases of about 40% the copper(1+) transport activity.|||Disordered|||Does not affect copper(1+)-induced MAPK activation. Does not affect copper(1+)-induced endothelial cells migration and capillary formation. Almost completely loss of VEGFA-induced internalization of KDR and SLC31A1. Almost completely loss of VEGFA-induced interaction between KDR and SLC31A1. Decreases of 200-fold affinity for copper(1+) ion. Loss of ATOX1 interaction in the absence of copper(1+).|||Does not affect expression. Does not affect cell membrane localization. Moderately affects copper(1+) transport activity.|||Does not affect expression. Does not affect cell membrane localization. Significantly reduces copper(1+) transport activity.|||Dramatically affects copper(1+) transport activity.|||Dramatically decreases copper(1+) affinity. Reduces copper(1+) uptake; when associated with L-150 and L-154. Does not affect cell membrane expression.|||Extracellular|||Helical|||High affinity copper uptake protein 1|||In NSCT; unknown pathological significance.|||In NSCT; unknown pathological significance; does not affect localization at the plasma membrane.|||Increases copper(1+) uptake.|||Increases copper(1+) uptake. Reduces affinity for copper(1+).|||Increases copper(1+) uptake. Reduces affinity for copper(1+). Reduces copper(1+) uptake; when associated with L-150 and L-154. Impairs endocytosis in response to higher extracellular copper(1+) concentration.|||Increases the efficiency of the reduction.|||Inhibits copper(1+)-induced MAPK activation. Loss of copper(1+)-induced endothelil cell (EC) migration and capillary formation.|||Interchain (with C-1208 in KDR)|||Markedly decreases the copper(1+) transport activity; when associated with S-161.|||Markedly decreases the copper(1+) transport activity; when associated with S-189.|||Methionine segments (Mets) motif|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphothreonine|||Polar residues|||Reduces copper(1+) uptake; when associated with L-150. Reduces copper(1+) uptake; when associated with L-150 and R-139. Reduces copper(1+) uptake; when associated with L-150 and 188-A--A-190.|||Reduces copper(1+) uptake; when associated with L-154. Reduces copper(1+) uptake; when associated with L-154 and R-139. Reduces copper(1+) uptake; when associated with L-154 and 188-A--A-190.|||Reduces of about 30% the copper(1+) transport activity; when associated with I-150. Does not affect copper(1+) affinity; when associated with I-150. Abolishes silver(1+) transport activity when associated with I-150.|||Reduces of about 30% the copper(1+) transport activity; when associated with I-154. Does not affect copper(1+) affinity; when associated with I-154. Abolishes silver(1+) transport activity; when associated with I-154.|||Truncated CTR1 form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195040|||http://purl.uniprot.org/annotation/PRO_0000458008|||http://purl.uniprot.org/annotation/VAR_029338|||http://purl.uniprot.org/annotation/VAR_088353|||http://purl.uniprot.org/annotation/VAR_088354
http://togogenome.org/gene/9606:MLXIP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAP2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2, isoform 4 and isoform 5.|||In isoform 3 and isoform 5.|||In isoform 4.|||In isoform 5.|||Leucine-zipper|||MLX-interacting protein|||Mediates heterotypic interactions between MLXIP and MLX and is required for cytoplasmic localization|||N-acetylalanine|||Phosphoserine|||Polar residues|||Removed|||Required for cytoplasmic localization|||Transactivation domain|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000298763|||http://purl.uniprot.org/annotation/VAR_059344|||http://purl.uniprot.org/annotation/VAR_059345|||http://purl.uniprot.org/annotation/VSP_052499|||http://purl.uniprot.org/annotation/VSP_052500|||http://purl.uniprot.org/annotation/VSP_052501|||http://purl.uniprot.org/annotation/VSP_052502|||http://purl.uniprot.org/annotation/VSP_052503|||http://purl.uniprot.org/annotation/VSP_052504
http://togogenome.org/gene/9606:AP1B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q10567                                                                                  ^@                                                                                  Chain|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  3'-nitrotyrosine|||AP-1 complex subunit beta-1|||Disordered|||In KIDAR.|||In KIDAR; no protein detected by Western blot in patient cells.|||In isoform 4.|||In isoform B, isoform C and isoform 4.|||In isoform C and isoform 4.|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193738|||http://purl.uniprot.org/annotation/VAR_062816|||http://purl.uniprot.org/annotation/VAR_083524|||http://purl.uniprot.org/annotation/VAR_083525|||http://purl.uniprot.org/annotation/VSP_000163|||http://purl.uniprot.org/annotation/VSP_038753|||http://purl.uniprot.org/annotation/VSP_044928
http://togogenome.org/gene/9606:ISLR                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A146E5L3|||http://purl.uniprot.org/uniprot/O14498                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Repeat|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Ig-like|||Immunoglobulin superfamily containing leucine-rich repeat protein|||In a colorectal cancer sample; somatic mutation.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRRCT|||LRRNT|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312208|||http://purl.uniprot.org/annotation/PRO_5007523465|||http://purl.uniprot.org/annotation/VAR_037454
http://togogenome.org/gene/9606:ENPP5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DHN2|||http://purl.uniprot.org/uniprot/Q9UJA9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Ectonucleotide pyrophosphatase/phosphodiesterase family member 5|||Helical|||N-linked (GlcNAc...) asparagine|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036401|||http://purl.uniprot.org/annotation/VAR_020248|||http://purl.uniprot.org/annotation/VAR_024693|||http://purl.uniprot.org/annotation/VAR_033918|||http://purl.uniprot.org/annotation/VAR_052940|||http://purl.uniprot.org/annotation/VAR_052941
http://togogenome.org/gene/9606:KCNH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95259                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes inhibition of channel activity by elevated cytoplasmic Ca(2+).|||Basic and acidic residues|||CAD (involved in subunit assembly)|||Calmodulin-binding|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In TMBTS and ZLS1; gain-of-function effect; resulting in a decreased threshold of channel activation and slower deactivation.|||In TMBTS; gain-of-function mutation resulting in a decreased threshold of channel activation and slower deactivation compared to wild-type.|||In ZLS1.|||In ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation.|||In ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with L-383.|||In ZLS1; gain-of-function effect; accelerated channel activation and slower deactivation; associated in cis with Y-352.|||In ZLS1; gain-of-function effect; increased conductance at negative potentials.|||In isoform 1.|||Interaction with cyclic nucleotide-binding pocket|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Phosphoserine|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 1|||Required for phosphatidylinositol bisphosphate binding|||Selectivity filter|||Shifts the voltage-dependence of channel gating and decreases the rate of channel opening.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053994|||http://purl.uniprot.org/annotation/VAR_072612|||http://purl.uniprot.org/annotation/VAR_072613|||http://purl.uniprot.org/annotation/VAR_072614|||http://purl.uniprot.org/annotation/VAR_072615|||http://purl.uniprot.org/annotation/VAR_073957|||http://purl.uniprot.org/annotation/VAR_073958|||http://purl.uniprot.org/annotation/VAR_073959|||http://purl.uniprot.org/annotation/VAR_073960|||http://purl.uniprot.org/annotation/VAR_073961|||http://purl.uniprot.org/annotation/VSP_000964
http://togogenome.org/gene/9606:ADRA1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35368                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Abolishes targeting to the nuclear membrane of cardiac myocytes.|||Alpha-1B adrenergic receptor|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Nuclear localization signal|||Phosphothreonine|||Polar residues|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069069|||http://purl.uniprot.org/annotation/VAR_019510
http://togogenome.org/gene/9606:SCYL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96KG9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||In a metastatic melanoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Interaction with COPB1|||N-terminal kinase-like protein|||Phosphoserine|||Polar residues|||Pro residues|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249541|||http://purl.uniprot.org/annotation/VAR_041364|||http://purl.uniprot.org/annotation/VAR_041365|||http://purl.uniprot.org/annotation/VAR_041366|||http://purl.uniprot.org/annotation/VAR_041367|||http://purl.uniprot.org/annotation/VSP_020503|||http://purl.uniprot.org/annotation/VSP_020504|||http://purl.uniprot.org/annotation/VSP_020505|||http://purl.uniprot.org/annotation/VSP_020506|||http://purl.uniprot.org/annotation/VSP_020507|||http://purl.uniprot.org/annotation/VSP_020508
http://togogenome.org/gene/9606:PALM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75781                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Lipid Binding|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cysteine methyl ester|||Disordered|||In isoform 2.|||Inhibits axonal and dendritic filopodia formation and reduces axonal and dendritic branching.|||N-acetylmethionine|||Paralemmin-1|||Phosphoserine|||Phosphothreonine|||Polar residues|||Removed in mature form|||S-farnesyl cysteine|||S-palmitoyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058218|||http://purl.uniprot.org/annotation/PRO_0000396689|||http://purl.uniprot.org/annotation/VAR_053803|||http://purl.uniprot.org/annotation/VSP_003918
http://togogenome.org/gene/9606:ZNF101                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZC7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 2|||C2H2-type 3; degenerate|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||In isoform 2.|||KRAB|||Polar residues|||Zinc finger protein 101                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047406|||http://purl.uniprot.org/annotation/VAR_024197|||http://purl.uniprot.org/annotation/VSP_055937
http://togogenome.org/gene/9606:KCNE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y6J6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||In ATFB4; gain-of-function mutation associated with the initiation and/or maintenance of AF.|||In LQT6.|||In LQT6; forms I(KR) channels that deactivate twice as fast as wild type.|||In LQT6; may affect KCNQ1/KCNE2 channel.|||In LQT6; unknown pathological significance.|||Increases tail current in KCNH2/KCNE2 channel.|||N-linked (GlcNAc...) asparagine|||Potassium voltage-gated channel subfamily E member 2|||Risk factor for drug-induced arrhythmia; impedes activation and increases sensitivity to macrolide antibiotics; may lower current in KCNQ1/KCNE2 channel.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144285|||http://purl.uniprot.org/annotation/VAR_008375|||http://purl.uniprot.org/annotation/VAR_008376|||http://purl.uniprot.org/annotation/VAR_008377|||http://purl.uniprot.org/annotation/VAR_008378|||http://purl.uniprot.org/annotation/VAR_015063|||http://purl.uniprot.org/annotation/VAR_022052|||http://purl.uniprot.org/annotation/VAR_029334|||http://purl.uniprot.org/annotation/VAR_035386|||http://purl.uniprot.org/annotation/VAR_037794|||http://purl.uniprot.org/annotation/VAR_037795|||http://purl.uniprot.org/annotation/VAR_074921|||http://purl.uniprot.org/annotation/VAR_074922|||http://purl.uniprot.org/annotation/VAR_074923|||http://purl.uniprot.org/annotation/VAR_074924|||http://purl.uniprot.org/annotation/VAR_074925|||http://purl.uniprot.org/annotation/VAR_074926
http://togogenome.org/gene/9606:AMBN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q546D7|||http://purl.uniprot.org/uniprot/Q9NP70                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  1|||2|||Ameloblastin|||Disordered|||Hydroxyproline|||In ameloblastoma.|||In an ameloblastoma sample.|||In isoform 2.|||O-linked (GalNAc...) serine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001192|||http://purl.uniprot.org/annotation/PRO_5014309647|||http://purl.uniprot.org/annotation/VAR_014066|||http://purl.uniprot.org/annotation/VAR_014067|||http://purl.uniprot.org/annotation/VAR_014068|||http://purl.uniprot.org/annotation/VAR_014069|||http://purl.uniprot.org/annotation/VAR_048225|||http://purl.uniprot.org/annotation/VSP_000224
http://togogenome.org/gene/9606:DLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10515|||http://purl.uniprot.org/uniprot/Q86YI5                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Catalytic|||Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial|||Disordered|||Lipoyl-binding|||Lipoyl-binding 1|||Lipoyl-binding 2|||Mitochondrion|||N6-acetyllysine|||N6-lipoyllysine|||N6-succinyllysine|||Peripheral subunit-binding (PSBD)|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000020479|||http://purl.uniprot.org/annotation/VAR_047410|||http://purl.uniprot.org/annotation/VAR_047411|||http://purl.uniprot.org/annotation/VAR_047412|||http://purl.uniprot.org/annotation/VAR_047413|||http://purl.uniprot.org/annotation/VAR_047414|||http://purl.uniprot.org/annotation/VAR_047415|||http://purl.uniprot.org/annotation/VAR_047416
http://togogenome.org/gene/9606:SMAD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z5N5|||http://purl.uniprot.org/uniprot/Q15796|||http://purl.uniprot.org/uniprot/Q53XR6                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binds RANBP3.|||Disordered|||Found in a patient suspected to suffer from Marfan syndrome; unknown pathological significance.|||Found in a patient with Marfan syndrome-like phenotype; unknown pathological significance.|||Greatly reduced RANBP2 binding.|||Helical|||In CHTD8.|||In LDS6.|||In LDS6; unknown pathological significance.|||In a colorectal cancer sample; somatic mutation.|||In a colorectal carcinoma sample.|||In isoform Short.|||Increased binding to PPM1A.|||Loss of acetylation.|||Loss of binding to SARA.|||Loss of binding to SMURF2.|||Loss of interaction with PMEPA1.|||Loss of phosphorylation by TGFBR1; when associated with A-465 and A-467.|||MH1|||MH2|||Mothers against decapentaplegic homolog 2|||N-acetylserine|||N6-acetyllysine|||No change in binding to PPM1A.|||No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-465.|||No change in binding to PPM1A. Loss of phosphorylation by TGFBR1; when associated with A-464 and A-467.|||No effect on acetylation.|||PY-motif|||Phosphoserine|||Phosphoserine; by CAMK2|||Phosphoserine; by TGFBR1|||Phosphothreonine|||Phosphothreonine; by MAPK3|||Polar residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000090852|||http://purl.uniprot.org/annotation/VAR_011375|||http://purl.uniprot.org/annotation/VAR_011376|||http://purl.uniprot.org/annotation/VAR_011377|||http://purl.uniprot.org/annotation/VAR_011378|||http://purl.uniprot.org/annotation/VAR_011379|||http://purl.uniprot.org/annotation/VAR_036473|||http://purl.uniprot.org/annotation/VAR_086573|||http://purl.uniprot.org/annotation/VAR_086574|||http://purl.uniprot.org/annotation/VAR_086575|||http://purl.uniprot.org/annotation/VAR_086576|||http://purl.uniprot.org/annotation/VAR_086577|||http://purl.uniprot.org/annotation/VAR_086578|||http://purl.uniprot.org/annotation/VAR_086579|||http://purl.uniprot.org/annotation/VAR_086580|||http://purl.uniprot.org/annotation/VAR_086581|||http://purl.uniprot.org/annotation/VAR_086582|||http://purl.uniprot.org/annotation/VAR_086583|||http://purl.uniprot.org/annotation/VSP_006178
http://togogenome.org/gene/9606:KRT77                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q0IIN1|||http://purl.uniprot.org/uniprot/Q7Z794                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Coil 1A|||Coil 1B|||Coil 2|||Disordered|||Head|||IF rod|||Keratin, type II cytoskeletal 1b|||Linker 1|||Linker 12|||Omega-N-methylarginine|||Polar residues|||Stutter|||Tail                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063711|||http://purl.uniprot.org/annotation/VAR_056022
http://togogenome.org/gene/9606:ABCB11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95342                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||Bile salt export pump|||Cytoplasmic|||Disordered|||Does not affect ATPase-coupled bile acid transport activity. Decreases protein stability.|||Does not affect taurocholate transport activity; does not affect cell surface protein expression.|||Does not affect taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression.|||Extracellular|||Helical|||Impairs taurocholate transport activity; does not affect protein expression; decreases cell surface protein expression; reduces plasma membrane localization.|||Impairs taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression; does not affect cell membrane localization.|||In BRIC2.|||In BRIC2; reduced transport capacity for taurocholate; reduces transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment.|||In PFIC2 and BRIC2; reduces transport capacity for taurocholate; decreases protein expression; affects maturation of protein in the reticulum endoplasmic; does not affect apical membrane localization; does not affect cell surface expression of the mature form; does not affect transport of taurocholate and glycocholate; enhances ubiquitination susceptibility; reduces transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment; does not affect protein expression; does not affect cell membrane localization.|||In PFIC2.|||In PFIC2; decreases protein expression; affects maturation of protein in the reticulum endoplasmic; decreases apical membrane localization; affects cell surface expression; does not affect transport of taurocholate and glycocholate; enhances ubiquitination susceptibility.|||In PFIC2; impairs taurocholate transport activity; significantly reduces protein expression; decreases cell surface protein expression; loss of ell membrane localization.|||In PFIC2; loss of cell membrane localization; significantly reduces taurocholate transport activity.|||In PFIC2; unknown pathological significance.|||In a patient with intrahepatic cholestasis of pregnancy; impairs taurocholate transport activity; does not affect protein expression; does not affect cell surface protein expression; does not affect cell membrane localization.|||In ethinylestradiol/gestodene-induced cholestasis; loss of transport capacity for taurocholate.|||In fluvastatin-induced cholestasis; does not affect transport capacity for taurocholate.|||Interaction with HAX1|||Loss of interaction with AP2A1 and AP2A2. Promotes ABCB11 plasma membrane trafficking. Does not affect plasma membrane localization. Inhibits ABCB11 internalization.|||Mediates internalization from the plasma membrane|||Might be associated with increased risk of intrahepatic stones; decreases protein expression; deacreases localization to the cell membrane; decreases the trafficking to the plasma membrane.|||More frequent in patients with drug-induced cholestasis than healthy controls; associated with lower hepatic expression; does not affect transport capacity for taurocholate; increases transport activity of taurocholate in a low cholesterol environment; increases transport activity of taurocholate in a high cholesterol environment; does not affect cell surface protein expression; does not affect protein expression.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093296|||http://purl.uniprot.org/annotation/VAR_010271|||http://purl.uniprot.org/annotation/VAR_013332|||http://purl.uniprot.org/annotation/VAR_013333|||http://purl.uniprot.org/annotation/VAR_013334|||http://purl.uniprot.org/annotation/VAR_013335|||http://purl.uniprot.org/annotation/VAR_013336|||http://purl.uniprot.org/annotation/VAR_013337|||http://purl.uniprot.org/annotation/VAR_013338|||http://purl.uniprot.org/annotation/VAR_013339|||http://purl.uniprot.org/annotation/VAR_030386|||http://purl.uniprot.org/annotation/VAR_030387|||http://purl.uniprot.org/annotation/VAR_030388|||http://purl.uniprot.org/annotation/VAR_030389|||http://purl.uniprot.org/annotation/VAR_030390|||http://purl.uniprot.org/annotation/VAR_030391|||http://purl.uniprot.org/annotation/VAR_030392|||http://purl.uniprot.org/annotation/VAR_030393|||http://purl.uniprot.org/annotation/VAR_030394|||http://purl.uniprot.org/annotation/VAR_030395|||http://purl.uniprot.org/annotation/VAR_030396|||http://purl.uniprot.org/annotation/VAR_030397|||http://purl.uniprot.org/annotation/VAR_030398|||http://purl.uniprot.org/annotation/VAR_035349|||http://purl.uniprot.org/annotation/VAR_035350|||http://purl.uniprot.org/annotation/VAR_035351|||http://purl.uniprot.org/annotation/VAR_035352|||http://purl.uniprot.org/annotation/VAR_035353|||http://purl.uniprot.org/annotation/VAR_035354|||http://purl.uniprot.org/annotation/VAR_043074|||http://purl.uniprot.org/annotation/VAR_043075|||http://purl.uniprot.org/annotation/VAR_043076|||http://purl.uniprot.org/annotation/VAR_043077|||http://purl.uniprot.org/annotation/VAR_055472|||http://purl.uniprot.org/annotation/VAR_059106|||http://purl.uniprot.org/annotation/VAR_059107|||http://purl.uniprot.org/annotation/VAR_073967|||http://purl.uniprot.org/annotation/VAR_073968|||http://purl.uniprot.org/annotation/VAR_073969|||http://purl.uniprot.org/annotation/VAR_073970|||http://purl.uniprot.org/annotation/VAR_073971|||http://purl.uniprot.org/annotation/VAR_073972|||http://purl.uniprot.org/annotation/VAR_083783|||http://purl.uniprot.org/annotation/VAR_083784|||http://purl.uniprot.org/annotation/VAR_083785
http://togogenome.org/gene/9606:NRG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024QY88|||http://purl.uniprot.org/uniprot/A0A494C0K4|||http://purl.uniprot.org/uniprot/A0A494C0L9|||http://purl.uniprot.org/uniprot/A0A494C0Q4|||http://purl.uniprot.org/uniprot/A0A494C114|||http://purl.uniprot.org/uniprot/A0A494C1B5|||http://purl.uniprot.org/uniprot/A0A494C1F5|||http://purl.uniprot.org/uniprot/A0A494C1F8|||http://purl.uniprot.org/uniprot/A5YAK6|||http://purl.uniprot.org/uniprot/A5YAK8|||http://purl.uniprot.org/uniprot/A6MW54|||http://purl.uniprot.org/uniprot/A6MW55|||http://purl.uniprot.org/uniprot/A6MW56|||http://purl.uniprot.org/uniprot/B0FWZ3|||http://purl.uniprot.org/uniprot/B0FYA7|||http://purl.uniprot.org/uniprot/B0FYA8|||http://purl.uniprot.org/uniprot/B0FYA9|||http://purl.uniprot.org/uniprot/B7Z1D7|||http://purl.uniprot.org/uniprot/B7Z1E3|||http://purl.uniprot.org/uniprot/E3SFM9|||http://purl.uniprot.org/uniprot/E5RHP6|||http://purl.uniprot.org/uniprot/Q02297|||http://purl.uniprot.org/uniprot/Q6PK61|||http://purl.uniprot.org/uniprot/Q7RTW3|||http://purl.uniprot.org/uniprot/Q7RTW5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Mutagenesis Site|||Non-terminal Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Breakpoint for translocation to form gamma-heregulin|||Cytoplasmic|||Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-181 or E-185. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-181 and E-185.|||Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-181 or E-187. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-181 and E-187.|||Defective in integrin-binding and in inducing ERBB3 phosphorylation; when associated with or without E-185 or E-187. No effect on ERBB3-binding, defective in integrin-binding and in ternary complex formation with ERBB3 and integrins, and defective in inducing NRG1-ERBB signaling; when associated with E-185 and E-187.|||Disordered|||EGF-like|||Extracellular|||Helical|||Helical; Note=Internal signal sequence|||Ig-like|||Ig-like C2-type|||In isoform 10.|||In isoform 11.|||In isoform 12.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 6 and isoform 11.|||In isoform 7 and isoform 12.|||In isoform 8, isoform 9 and isoform 10.|||In isoform 9 and isoform 11.|||In isoform 9.|||N-linked (GlcNAc...) asparagine|||Neuregulin-1|||Polar residues|||Pro-neuregulin-1, membrane-bound isoform                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019462|||http://purl.uniprot.org/annotation/PRO_0000019463|||http://purl.uniprot.org/annotation/PRO_0000019464|||http://purl.uniprot.org/annotation/VAR_009307|||http://purl.uniprot.org/annotation/VAR_009308|||http://purl.uniprot.org/annotation/VAR_053531|||http://purl.uniprot.org/annotation/VAR_082866|||http://purl.uniprot.org/annotation/VAR_082867|||http://purl.uniprot.org/annotation/VSP_003425|||http://purl.uniprot.org/annotation/VSP_003426|||http://purl.uniprot.org/annotation/VSP_003427|||http://purl.uniprot.org/annotation/VSP_003428|||http://purl.uniprot.org/annotation/VSP_003429|||http://purl.uniprot.org/annotation/VSP_003430|||http://purl.uniprot.org/annotation/VSP_003431|||http://purl.uniprot.org/annotation/VSP_003432|||http://purl.uniprot.org/annotation/VSP_003433|||http://purl.uniprot.org/annotation/VSP_003434|||http://purl.uniprot.org/annotation/VSP_003435|||http://purl.uniprot.org/annotation/VSP_037562|||http://purl.uniprot.org/annotation/VSP_037563|||http://purl.uniprot.org/annotation/VSP_037564|||http://purl.uniprot.org/annotation/VSP_037565|||http://purl.uniprot.org/annotation/VSP_046417
http://togogenome.org/gene/9606:PLD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DI07|||http://purl.uniprot.org/uniprot/B4DJQ6|||http://purl.uniprot.org/uniprot/F5H2B5|||http://purl.uniprot.org/uniprot/Q96BZ4                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  5'-3' exonuclease PLD4|||Helical|||N-linked (GlcNAc...) asparagine|||PLD phosphodiesterase|||PLD phosphodiesterase 1|||PLD phosphodiesterase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280333|||http://purl.uniprot.org/annotation/VAR_031119|||http://purl.uniprot.org/annotation/VAR_031120|||http://purl.uniprot.org/annotation/VAR_061751
http://togogenome.org/gene/9606:MRPL49                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13405                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Large ribosomal subunit protein mL49|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207664|||http://purl.uniprot.org/annotation/VAR_021991
http://togogenome.org/gene/9606:TMC6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z403                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Lumenal|||N-linked (GlcNAc...) asparagine|||Omega-N-methylarginine|||Phosphothreonine|||Transmembrane channel-like protein 6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185384|||http://purl.uniprot.org/annotation/VAR_023963|||http://purl.uniprot.org/annotation/VAR_052336|||http://purl.uniprot.org/annotation/VAR_061851|||http://purl.uniprot.org/annotation/VSP_016437|||http://purl.uniprot.org/annotation/VSP_016438|||http://purl.uniprot.org/annotation/VSP_016439|||http://purl.uniprot.org/annotation/VSP_016440|||http://purl.uniprot.org/annotation/VSP_016441|||http://purl.uniprot.org/annotation/VSP_016442
http://togogenome.org/gene/9606:TSHZ3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q63HK5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||Disordered|||Does not inhibit interaction with APBB1.|||Homeobox; atypical|||Phosphoserine|||Polar residues|||Teashirt homolog 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047066|||http://purl.uniprot.org/annotation/VAR_052708|||http://purl.uniprot.org/annotation/VAR_063635
http://togogenome.org/gene/9606:ELL2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00472|||http://purl.uniprot.org/uniprot/Q59FW6|||http://purl.uniprot.org/uniprot/Q7Z656                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||OCEL|||Phosphoserine|||Polar residues|||Pro residues|||RNA polymerase II elongation factor ELL2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000146735|||http://purl.uniprot.org/annotation/VAR_058406|||http://purl.uniprot.org/annotation/VSP_055476
http://togogenome.org/gene/9606:TSHZ1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A7YF73|||http://purl.uniprot.org/uniprot/Q6ZSZ6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3; atypical|||C2H2-type 4|||C2H2-type 5|||Disordered|||Homeobox; atypical|||In isoform 2.|||Phosphoserine|||Polar residues|||Teashirt homolog 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047062|||http://purl.uniprot.org/annotation/VAR_061926|||http://purl.uniprot.org/annotation/VSP_040877
http://togogenome.org/gene/9606:CCR6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P51684                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Region|||Secondary Structure|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  C-C chemokine receptor type 6|||Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Loss of calcium flux and chemotaxis in response to CCL20 stimulation, impaired CCL20-binding and significant reduction in cell surface expression; when associated with or without S-118. Loss of calcium flux in response to CCL20 stimulation and significant reduction in cell surface expression; when associated with S-36; S-118 and S-288.|||Loss of calcium flux and chemotaxis in response to CCL20 stimulation, impaired CCL20-binding and significant reduction in cell surface expression; when associated with or without S-197. Loss of calcium flux in response to CCL20 stimulation and significant reduction in cell surface expression; when associated with S-36; S-197 and S-288.|||Loss of calcium flux and chemotaxis in response to CCL20 stimulation. No effect on cell surface expression.|||N-linked (GlcNAc...) asparagine|||No effect on calcium flux and chemotaxis in response to CCL20 stimulation. No effect on CCL20-binding and cell surface expression.|||No effect on calcium flux and chemotaxis in response to CCL20 stimulation. No effect on cell surface expression.|||No loss of calcium flux but loss of chemotaxis in response to CCL20 stimulation, impaired CCL20-binding and no effect on cell surface expression; when associated with or without S-288. Loss of calcium flux in response to CCL20 stimulation and significant reduction in cell surface expression; when associated with S-118; S-197 and S-288.|||No loss of calcium flux but loss of chemotaxis in response to CCL20 stimulation, impaired CCL20-binding and no effect on cell surface expression; when associated with or without S-36. Loss of calcium flux in response to CCL20 stimulation and significant reduction in cell surface expression; when associated with S-36; S-118 and S-197.|||No loss of calcium flux but loss of chemotaxis in response to CCL20 stimulation. No effect on cell surface expression.|||Reduced calcium flux and chemotaxis in response to CCL20 stimulation, and reduced CCL20-binding. No effect on cell surface expression.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069286
http://togogenome.org/gene/9606:GTF2H4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X7S4|||http://purl.uniprot.org/uniprot/Q92759                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  General transcription factor IIH subunit 4|||In isoform 2.|||Transcription factor Tfb2 C-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119253|||http://purl.uniprot.org/annotation/VAR_019056|||http://purl.uniprot.org/annotation/VSP_056835|||http://purl.uniprot.org/annotation/VSP_056836|||http://purl.uniprot.org/annotation/VSP_056837
http://togogenome.org/gene/9606:SRP9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49458                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||N6-acetyllysine|||Removed|||Signal recognition particle 9 kDa protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000135182|||http://purl.uniprot.org/annotation/VSP_041270
http://togogenome.org/gene/9606:TXNRD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E7EWK1|||http://purl.uniprot.org/uniprot/Q9NNW7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non standard residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Domain Extent|||Modified Residue|||Non standard residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Cysteinyl-selenocysteine (Cys-Sec)|||FAD/NAD(P)-binding|||In GCCD5; the mutant protein is undetectable in patient cells.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Mitochondrion|||N6-succinyllysine|||Proton acceptor|||Redox-active|||Selenocysteine|||Thioredoxin reductase 2, mitochondrial                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030288|||http://purl.uniprot.org/annotation/VAR_051777|||http://purl.uniprot.org/annotation/VAR_051778|||http://purl.uniprot.org/annotation/VAR_051779|||http://purl.uniprot.org/annotation/VAR_051780|||http://purl.uniprot.org/annotation/VAR_080529|||http://purl.uniprot.org/annotation/VSP_008304|||http://purl.uniprot.org/annotation/VSP_008305|||http://purl.uniprot.org/annotation/VSP_008306
http://togogenome.org/gene/9606:COBLL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0D9SG04|||http://purl.uniprot.org/uniprot/A0A0X1KG75|||http://purl.uniprot.org/uniprot/B7Z2P5|||http://purl.uniprot.org/uniprot/Q53SF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cordon-bleu protein-like 1|||Disordered|||In isoform 2.|||In isoform 3.|||KKRRAP 1|||KKRRAP 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000260493|||http://purl.uniprot.org/annotation/VSP_060296|||http://purl.uniprot.org/annotation/VSP_060297|||http://purl.uniprot.org/annotation/VSP_060298
http://togogenome.org/gene/9606:COL4A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PKV2|||http://purl.uniprot.org/uniprot/P02462                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand                                                                                  ^@                                                                                  3-hydroxyproline|||4-hydroxyproline|||Arresten|||Basic and acidic residues|||Collagen IV NC1|||Collagen alpha-1(IV) chain|||Disordered|||In BSVD1.|||In BSVD1; associated with ocular anomalies of variable severity in some patients.|||In BSVD1; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy.|||In HANAC and RATOR.|||In HANAC.|||In HANAC; requires 2 nucleotide substitutions.|||In ICH; the mutant protein is retained intracellularly and is not secreted normally.|||In SCHZC.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||N-terminal propeptide (7S domain)|||Pro residues|||S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)|||S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)|||Triple-helical region                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005748|||http://purl.uniprot.org/annotation/PRO_0000005749|||http://purl.uniprot.org/annotation/PRO_0000390482|||http://purl.uniprot.org/annotation/PRO_5002687408|||http://purl.uniprot.org/annotation/VAR_020013|||http://purl.uniprot.org/annotation/VAR_030027|||http://purl.uniprot.org/annotation/VAR_030028|||http://purl.uniprot.org/annotation/VAR_030029|||http://purl.uniprot.org/annotation/VAR_030030|||http://purl.uniprot.org/annotation/VAR_030031|||http://purl.uniprot.org/annotation/VAR_030032|||http://purl.uniprot.org/annotation/VAR_030511|||http://purl.uniprot.org/annotation/VAR_044158|||http://purl.uniprot.org/annotation/VAR_044159|||http://purl.uniprot.org/annotation/VAR_044160|||http://purl.uniprot.org/annotation/VAR_044161|||http://purl.uniprot.org/annotation/VAR_064493|||http://purl.uniprot.org/annotation/VAR_064494|||http://purl.uniprot.org/annotation/VAR_064495|||http://purl.uniprot.org/annotation/VAR_064496|||http://purl.uniprot.org/annotation/VAR_064497|||http://purl.uniprot.org/annotation/VAR_064498|||http://purl.uniprot.org/annotation/VAR_064499|||http://purl.uniprot.org/annotation/VAR_073809|||http://purl.uniprot.org/annotation/VAR_073810|||http://purl.uniprot.org/annotation/VAR_073811|||http://purl.uniprot.org/annotation/VAR_073812|||http://purl.uniprot.org/annotation/VAR_073813|||http://purl.uniprot.org/annotation/VAR_073814|||http://purl.uniprot.org/annotation/VAR_073815|||http://purl.uniprot.org/annotation/VAR_073816|||http://purl.uniprot.org/annotation/VAR_073817|||http://purl.uniprot.org/annotation/VAR_073818|||http://purl.uniprot.org/annotation/VAR_073819|||http://purl.uniprot.org/annotation/VAR_073820|||http://purl.uniprot.org/annotation/VAR_073821|||http://purl.uniprot.org/annotation/VAR_073822|||http://purl.uniprot.org/annotation/VAR_073823|||http://purl.uniprot.org/annotation/VAR_073824|||http://purl.uniprot.org/annotation/VAR_073825|||http://purl.uniprot.org/annotation/VAR_073826|||http://purl.uniprot.org/annotation/VSP_059564|||http://purl.uniprot.org/annotation/VSP_059565
http://togogenome.org/gene/9606:NFRKB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P4R8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEUBAD|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Nuclear factor related to kappa-B-binding protein|||Phosphoserine|||Polar residues|||Pro residues|||Winged-helix like domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000227807|||http://purl.uniprot.org/annotation/VSP_017592|||http://purl.uniprot.org/annotation/VSP_017593|||http://purl.uniprot.org/annotation/VSP_017594
http://togogenome.org/gene/9606:ILK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13418|||http://purl.uniprot.org/uniprot/V9HWF0                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||Alters interaction with LIMS1.|||Found in a patient with severe dilated cardiomyopathy; unknown pathological significance.|||In isoform 2.|||In isoform 3.|||Inactivation of ILK.|||Integrin-linked protein kinase|||Interaction with LIMS1|||N-acetylmethionine|||N6-acetyllysine|||PH-like; mediates interaction with TGFB1I1|||Phosphoserine|||Protein kinase                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086020|||http://purl.uniprot.org/annotation/VAR_069753|||http://purl.uniprot.org/annotation/VSP_054920|||http://purl.uniprot.org/annotation/VSP_055925
http://togogenome.org/gene/9606:PLPP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IY26                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Helical|||Loss of polyisoprenoid diphosphate phosphatase activity.|||Lumenal|||Nucleophile|||Phosphatase sequence motif I|||Phosphatase sequence motif II|||Phosphatase sequence motif III|||Phosphoserine|||Polar residues|||Polyisoprenoid diphosphate/phosphate phosphohydrolase PLPP6|||Proton donors|||Stabilizes the active site histidine for nucleophilic attack                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000239396|||http://purl.uniprot.org/annotation/VAR_026645|||http://purl.uniprot.org/annotation/VAR_050616|||http://purl.uniprot.org/annotation/VAR_050617
http://togogenome.org/gene/9606:MAGEH1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H213                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||MAGE|||Melanoma-associated antigen H1|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156735
http://togogenome.org/gene/9606:MEAF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HAF1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic residues|||Chromatin modification-related protein MEAF6|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-acetylalanine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272609|||http://purl.uniprot.org/annotation/VSP_022450|||http://purl.uniprot.org/annotation/VSP_022451|||http://purl.uniprot.org/annotation/VSP_047018
http://togogenome.org/gene/9606:PRR23D2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E9PI22|||http://purl.uniprot.org/uniprot/P0DMB1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Disordered|||Polar residues|||Proline-rich protein 23D1|||Proline-rich protein 23D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000425121|||http://purl.uniprot.org/annotation/PRO_0000425122
http://togogenome.org/gene/9606:ANKFN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/H3BM45|||http://purl.uniprot.org/uniprot/Q8N957                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK|||ANK 1|||ANK 2|||Ankyrin repeat and fibronectin type-III domain-containing protein 1|||Disordered|||Fibronectin type-III|||Highly conserved peptide sequence|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247138|||http://purl.uniprot.org/annotation/VAR_060725|||http://purl.uniprot.org/annotation/VSP_061839|||http://purl.uniprot.org/annotation/VSP_061840|||http://purl.uniprot.org/annotation/VSP_061841
http://togogenome.org/gene/9606:PIN4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y237                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes phosphorylation and strongly reduces nuclear localization.|||Disordered|||Does not abolish nuclear localization and reduces DNA-binding ability.|||In isoform 2 and isoform 3.|||In isoform 3.|||Necessary for association with the pre-rRNP complexes|||Necessary for nuclear localization and DNA-binding|||Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4|||Phosphoserine; by CK2|||PpiC                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000193438|||http://purl.uniprot.org/annotation/VAR_082896|||http://purl.uniprot.org/annotation/VAR_082897|||http://purl.uniprot.org/annotation/VSP_037754|||http://purl.uniprot.org/annotation/VSP_046122
http://togogenome.org/gene/9606:EIF5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63241                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes acetylation.|||Causes total inactivation of eIF5A in supporting yeast growth.|||Decreases significantly the acetylation at position K-47 and causes total inactivation of eIF5A in supporting yeast growth.|||Eukaryotic translation initiation factor 5A-1|||Hypusine|||In FABAS.|||In FABAS; in yeast, exhibits reduced ribosome binding and cells show impaired synthesis of proteins containing poly-proline tracts.|||In FABAS; in yeast, exhibits reduced ribosome binding, reduced levels of hypusination and transfected cells show impaired synthesis of proteins containing poly-proline tracts.|||In isoform 2.|||Interaction with DOHH|||Leads to temperature sensitivity when expressed in yeast cells.|||N-acetylalanine|||N6-acetyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000142451|||http://purl.uniprot.org/annotation/VAR_085973|||http://purl.uniprot.org/annotation/VAR_085974|||http://purl.uniprot.org/annotation/VAR_085975|||http://purl.uniprot.org/annotation/VAR_085976|||http://purl.uniprot.org/annotation/VAR_085977|||http://purl.uniprot.org/annotation/VAR_085978|||http://purl.uniprot.org/annotation/VSP_022020
http://togogenome.org/gene/9606:ZNF532                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KXW2|||http://purl.uniprot.org/uniprot/Q9HCE3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 10; degenerate|||C2H2-type 11|||C2H2-type 12|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a breast cancer sample; somatic mutation.|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Zinc finger protein 532                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299552|||http://purl.uniprot.org/annotation/VAR_034846|||http://purl.uniprot.org/annotation/VAR_035585
http://togogenome.org/gene/9606:IL17RD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXM5|||http://purl.uniprot.org/uniprot/Q8NFM7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In HH18; rare variant associated with susceptibility to disease; some patients have a second mutation in the HH-associated gene FGFR1; reduced activity.|||In HH18; rare variant associated with susceptibility to disease; the patient carries a second mutation in the HH-associated gene KISS1R; results in decreased expression at the cell surface.|||In HH18; reduced activity.|||In HH18; results in decreased expression at the cell surface and reduced activity.|||In HH18; results in decreased expression at the cell surface.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interleukin-17 receptor D|||N-linked (GlcNAc...) asparagine|||Polar residues|||SEFIR                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000041871|||http://purl.uniprot.org/annotation/VAR_023478|||http://purl.uniprot.org/annotation/VAR_023479|||http://purl.uniprot.org/annotation/VAR_069936|||http://purl.uniprot.org/annotation/VAR_069937|||http://purl.uniprot.org/annotation/VAR_069938|||http://purl.uniprot.org/annotation/VAR_069939|||http://purl.uniprot.org/annotation/VAR_069940|||http://purl.uniprot.org/annotation/VAR_069941|||http://purl.uniprot.org/annotation/VAR_069942|||http://purl.uniprot.org/annotation/VSP_015582|||http://purl.uniprot.org/annotation/VSP_015583|||http://purl.uniprot.org/annotation/VSP_015584
http://togogenome.org/gene/9606:FCN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15485                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Collagen-like|||Disordered|||Fibrinogen C-terminal|||Ficolin-2|||Hydroxyproline|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000009139|||http://purl.uniprot.org/annotation/VAR_036342|||http://purl.uniprot.org/annotation/VAR_049072|||http://purl.uniprot.org/annotation/VAR_049073|||http://purl.uniprot.org/annotation/VAR_049074|||http://purl.uniprot.org/annotation/VAR_049075|||http://purl.uniprot.org/annotation/VSP_030027
http://togogenome.org/gene/9606:PRPF6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94906                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||HAT 1|||HAT 2|||HAT 3|||HAT 4|||HAT 5|||HAT 6|||HAT 7|||HAT 8|||HAT 9|||In RP60; impaired function in pre-mRNA splicing; mislocalized in Cajal bodies; partial loss of localization in splicing speckles.|||In isoform 2.|||Phosphoserine|||Phosphothreonine|||Pre-mRNA-processing factor 6|||Very rare variant found in a family with neuronal ceroid lipofuscinosis carrying a causative mutation in DNAJC5; uncertain role as a disease phenotype modifier.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205759|||http://purl.uniprot.org/annotation/VAR_065768|||http://purl.uniprot.org/annotation/VAR_069766|||http://purl.uniprot.org/annotation/VSP_041857
http://togogenome.org/gene/9606:TEX264                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTU3|||http://purl.uniprot.org/uniprot/Q9Y6I9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Completely abolishes the interaction with LC3B.|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type III membrane protein|||LIR motif|||Lumenal|||Phosphoserine|||Polar residues|||Testis-expressed protein 264                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022601|||http://purl.uniprot.org/annotation/VAR_061718
http://togogenome.org/gene/9606:RINT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NUQ1                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||In ILFS3.|||RAD50-interacting protein 1|||RINT1/TIP20                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097349|||http://purl.uniprot.org/annotation/VAR_034418|||http://purl.uniprot.org/annotation/VAR_034419|||http://purl.uniprot.org/annotation/VAR_051322|||http://purl.uniprot.org/annotation/VAR_083238|||http://purl.uniprot.org/annotation/VAR_083239|||http://purl.uniprot.org/annotation/VAR_083240
http://togogenome.org/gene/9606:PARP6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2NL67                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  ADP-ribosyl aspartic acid|||ADP-ribosylcysteine|||In isoform 2.|||In isoform 3.|||PARP catalytic|||Protein mono-ADP-ribosyltransferase PARP6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252430|||http://purl.uniprot.org/annotation/VSP_020963|||http://purl.uniprot.org/annotation/VSP_020964|||http://purl.uniprot.org/annotation/VSP_020965|||http://purl.uniprot.org/annotation/VSP_020966
http://togogenome.org/gene/9606:BICDL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZP65                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Motif|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  BICD family-like cargo adapter 1|||CC1 box|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000302858|||http://purl.uniprot.org/annotation/VSP_056941|||http://purl.uniprot.org/annotation/VSP_056942
http://togogenome.org/gene/9606:LGR4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q59ER8|||http://purl.uniprot.org/uniprot/Q9BXB1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In DPSL; unknown pathological significance; when transfected in HEK293T cells has no effect on WNT signaling; decreased protein expression in transfected cells.|||In DPSL; unknown pathological significance; when transfected in HEK293T cells it results in slightly reduced WNT signaling; decreased protein expression in transfected cells.|||In isoform 2.|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 13|||LRR 14|||LRR 15|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||Leucine-rich repeat-containing G-protein coupled receptor 4|||N-linked (GlcNAc...) asparagine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012792|||http://purl.uniprot.org/annotation/VAR_044528|||http://purl.uniprot.org/annotation/VAR_044529|||http://purl.uniprot.org/annotation/VAR_044530|||http://purl.uniprot.org/annotation/VAR_044531|||http://purl.uniprot.org/annotation/VAR_044532|||http://purl.uniprot.org/annotation/VAR_044533|||http://purl.uniprot.org/annotation/VAR_086463|||http://purl.uniprot.org/annotation/VAR_086464|||http://purl.uniprot.org/annotation/VSP_047136
http://togogenome.org/gene/9606:FOXB2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VYV0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Fork-head|||Forkhead box protein B2|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263091
http://togogenome.org/gene/9606:GATC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43716                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial|||In COXPD42; decreased protein abundance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000105365|||http://purl.uniprot.org/annotation/VAR_049129|||http://purl.uniprot.org/annotation/VAR_083987
http://togogenome.org/gene/9606:OTX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32242                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Modification|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||DNA Binding|||Region                                                                                  ^@                                                                                  Basic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Homeobox|||Homeobox protein OTX1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049207
http://togogenome.org/gene/9606:OR10P1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGE3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 10P1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150713|||http://purl.uniprot.org/annotation/VAR_034294|||http://purl.uniprot.org/annotation/VAR_034295
http://togogenome.org/gene/9606:OR10G9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NGN4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 10G9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150701|||http://purl.uniprot.org/annotation/VAR_034286|||http://purl.uniprot.org/annotation/VAR_034287|||http://purl.uniprot.org/annotation/VAR_053280|||http://purl.uniprot.org/annotation/VAR_060029
http://togogenome.org/gene/9606:NEIL3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TAT5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes AP lyase activity.|||Disordered|||Endonuclease 8-like 3|||FPG-type|||GRF-type 1|||GRF-type 2|||Important for monofunctional glycosylase activity|||Loss of glycosylase and lyase activities.|||No effect on AP lyase activity.|||No effect on AP lyase activity. Impairs monofunctional glycosylase activity.|||Phosphoserine|||RanBP2-type|||Removed|||Required for glycosylase and lyase activities|||Schiff-base intermediate with DNA; via amino nitrogen                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000170910|||http://purl.uniprot.org/annotation/VAR_020590|||http://purl.uniprot.org/annotation/VAR_020591|||http://purl.uniprot.org/annotation/VAR_020592|||http://purl.uniprot.org/annotation/VAR_025806|||http://purl.uniprot.org/annotation/VAR_025807|||http://purl.uniprot.org/annotation/VAR_025808|||http://purl.uniprot.org/annotation/VAR_025809|||http://purl.uniprot.org/annotation/VAR_025810|||http://purl.uniprot.org/annotation/VAR_025811|||http://purl.uniprot.org/annotation/VAR_025812|||http://purl.uniprot.org/annotation/VAR_025813|||http://purl.uniprot.org/annotation/VAR_025814
http://togogenome.org/gene/9606:PPAN-P2RY11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A6YYI3|||http://purl.uniprot.org/uniprot/A0A0B4J1V8|||http://purl.uniprot.org/uniprot/Q9NQ55                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Brix|||Disordered|||G-protein coupled receptors family 1 profile|||Helical|||In isoform 2.|||In isoform 3.|||N6-acetyllysine|||Phosphoserine|||Polar residues|||Suppressor of SWI4 1 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000120257|||http://purl.uniprot.org/annotation/VAR_022157|||http://purl.uniprot.org/annotation/VAR_048422|||http://purl.uniprot.org/annotation/VSP_003973|||http://purl.uniprot.org/annotation/VSP_046377
http://togogenome.org/gene/9606:CHST15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DH74|||http://purl.uniprot.org/uniprot/Q7LFX5                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 15|||Cytoplasmic|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000225623|||http://purl.uniprot.org/annotation/VSP_017387
http://togogenome.org/gene/9606:CTDNEP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95476                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Mutagenesis Site|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Abolishes phosphatase activity.|||CTD nuclear envelope phosphatase 1|||FCP1 homology|||Helical                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297967|||http://purl.uniprot.org/annotation/VAR_034699
http://togogenome.org/gene/9606:UCK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R8E7|||http://purl.uniprot.org/uniprot/A0A0S2Z5Y6|||http://purl.uniprot.org/uniprot/Q9HA47                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoribulokinase/uridine kinase|||Phosphoserine|||Phosphothreonine|||Uridine-cytidine kinase 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164453|||http://purl.uniprot.org/annotation/VSP_041269|||http://purl.uniprot.org/annotation/VSP_045174|||http://purl.uniprot.org/annotation/VSP_056748
http://togogenome.org/gene/9606:ARHGDIG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/F1T0H7|||http://purl.uniprot.org/uniprot/Q99819                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Rho GDP-dissociation inhibitor 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000219018|||http://purl.uniprot.org/annotation/PRO_5014303373
http://togogenome.org/gene/9606:PF4V1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P10720                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Mass|||Modification|||Molecule Processing|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Mass|||Sequence Conflict|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Platelet factor 4 variant|||Platelet factor 4 variant(4-74)|||Platelet factor 4 variant(4-74).|||Platelet factor 4 variant(5-74)|||Platelet factor 4 variant(5-74).|||Platelet factor 4 variant(6-74)|||Platelet factor 4 variant(6-74).|||Platelet factor 4 variant.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005071|||http://purl.uniprot.org/annotation/PRO_0000005072|||http://purl.uniprot.org/annotation/PRO_0000005073|||http://purl.uniprot.org/annotation/PRO_0000005074
http://togogenome.org/gene/9606:ZNF550                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z398                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||Disordered|||In isoform 2.|||KRAB|||Zinc finger protein 550                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000234585|||http://purl.uniprot.org/annotation/VAR_026294|||http://purl.uniprot.org/annotation/VSP_018380
http://togogenome.org/gene/9606:LRRTM4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KV11|||http://purl.uniprot.org/uniprot/B8ZZ84|||http://purl.uniprot.org/uniprot/Q4KMX1|||http://purl.uniprot.org/uniprot/Q6ZT31|||http://purl.uniprot.org/uniprot/Q86VH4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||LRR 1|||LRR 10|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT|||LRRNT|||Leucine-rich repeat transmembrane neuronal protein 4|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000018358|||http://purl.uniprot.org/annotation/PRO_5002788677|||http://purl.uniprot.org/annotation/PRO_5002880902|||http://purl.uniprot.org/annotation/PRO_5004283911|||http://purl.uniprot.org/annotation/PRO_5014309398|||http://purl.uniprot.org/annotation/VSP_030989|||http://purl.uniprot.org/annotation/VSP_030990
http://togogenome.org/gene/9606:MSANTD4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NCY6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Myb-like|||Myb/SANT-like DNA-binding domain-containing protein 4|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311830
http://togogenome.org/gene/9606:HGD                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KW64|||http://purl.uniprot.org/uniprot/Q93099                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Homogentisate 1,2-dioxygenase|||Homogentisate 1,2-dioxygenase C-terminal|||Homogentisate 1,2-dioxygenase N-terminal|||In AKU.|||In AKU; complete loss of activity.|||In AKU; loss of activity.|||In AKU; loss of activity; most prevalent mutation in Slovak and Czech patients.|||N6-acetyllysine|||N6-succinyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220240|||http://purl.uniprot.org/annotation/VAR_005272|||http://purl.uniprot.org/annotation/VAR_005273|||http://purl.uniprot.org/annotation/VAR_005274|||http://purl.uniprot.org/annotation/VAR_005275|||http://purl.uniprot.org/annotation/VAR_005276|||http://purl.uniprot.org/annotation/VAR_005277|||http://purl.uniprot.org/annotation/VAR_005278|||http://purl.uniprot.org/annotation/VAR_005279|||http://purl.uniprot.org/annotation/VAR_005280|||http://purl.uniprot.org/annotation/VAR_005281|||http://purl.uniprot.org/annotation/VAR_005282|||http://purl.uniprot.org/annotation/VAR_005283|||http://purl.uniprot.org/annotation/VAR_005284|||http://purl.uniprot.org/annotation/VAR_005285|||http://purl.uniprot.org/annotation/VAR_005286|||http://purl.uniprot.org/annotation/VAR_005287|||http://purl.uniprot.org/annotation/VAR_008744|||http://purl.uniprot.org/annotation/VAR_008745|||http://purl.uniprot.org/annotation/VAR_009618|||http://purl.uniprot.org/annotation/VAR_009619|||http://purl.uniprot.org/annotation/VAR_009620|||http://purl.uniprot.org/annotation/VAR_049353|||http://purl.uniprot.org/annotation/VAR_073076|||http://purl.uniprot.org/annotation/VAR_073077|||http://purl.uniprot.org/annotation/VAR_073078|||http://purl.uniprot.org/annotation/VAR_073079|||http://purl.uniprot.org/annotation/VAR_073080|||http://purl.uniprot.org/annotation/VAR_073081|||http://purl.uniprot.org/annotation/VAR_073082|||http://purl.uniprot.org/annotation/VAR_073083|||http://purl.uniprot.org/annotation/VAR_073084|||http://purl.uniprot.org/annotation/VAR_073085|||http://purl.uniprot.org/annotation/VAR_073086|||http://purl.uniprot.org/annotation/VAR_073087|||http://purl.uniprot.org/annotation/VAR_073088|||http://purl.uniprot.org/annotation/VAR_073089|||http://purl.uniprot.org/annotation/VAR_073090|||http://purl.uniprot.org/annotation/VAR_073091|||http://purl.uniprot.org/annotation/VAR_073092|||http://purl.uniprot.org/annotation/VAR_073093|||http://purl.uniprot.org/annotation/VAR_073094|||http://purl.uniprot.org/annotation/VAR_073095|||http://purl.uniprot.org/annotation/VAR_073096|||http://purl.uniprot.org/annotation/VAR_073097|||http://purl.uniprot.org/annotation/VAR_073098|||http://purl.uniprot.org/annotation/VAR_073099|||http://purl.uniprot.org/annotation/VAR_073100|||http://purl.uniprot.org/annotation/VAR_073101|||http://purl.uniprot.org/annotation/VAR_073102|||http://purl.uniprot.org/annotation/VAR_073103|||http://purl.uniprot.org/annotation/VAR_073104|||http://purl.uniprot.org/annotation/VAR_073105|||http://purl.uniprot.org/annotation/VAR_073106|||http://purl.uniprot.org/annotation/VAR_073107|||http://purl.uniprot.org/annotation/VAR_073108|||http://purl.uniprot.org/annotation/VAR_073109|||http://purl.uniprot.org/annotation/VAR_073110|||http://purl.uniprot.org/annotation/VAR_073111|||http://purl.uniprot.org/annotation/VAR_073112|||http://purl.uniprot.org/annotation/VAR_073113|||http://purl.uniprot.org/annotation/VAR_073114|||http://purl.uniprot.org/annotation/VAR_073115|||http://purl.uniprot.org/annotation/VAR_073116|||http://purl.uniprot.org/annotation/VAR_073117|||http://purl.uniprot.org/annotation/VAR_073118|||http://purl.uniprot.org/annotation/VAR_073119|||http://purl.uniprot.org/annotation/VAR_073120|||http://purl.uniprot.org/annotation/VAR_073121|||http://purl.uniprot.org/annotation/VAR_073122|||http://purl.uniprot.org/annotation/VAR_073123
http://togogenome.org/gene/9606:TOGARAM2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DLF7|||http://purl.uniprot.org/uniprot/Q6ZUX3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||In isoform 3.|||Polar residues|||TOG|||TOG array regulator of axonemal microtubules protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000325938|||http://purl.uniprot.org/annotation/VAR_054091|||http://purl.uniprot.org/annotation/VAR_054092|||http://purl.uniprot.org/annotation/VAR_054093|||http://purl.uniprot.org/annotation/VAR_054094|||http://purl.uniprot.org/annotation/VAR_054095|||http://purl.uniprot.org/annotation/VAR_054096|||http://purl.uniprot.org/annotation/VAR_054097|||http://purl.uniprot.org/annotation/VAR_062242|||http://purl.uniprot.org/annotation/VSP_032491|||http://purl.uniprot.org/annotation/VSP_032492|||http://purl.uniprot.org/annotation/VSP_032493|||http://purl.uniprot.org/annotation/VSP_032494|||http://purl.uniprot.org/annotation/VSP_032495
http://togogenome.org/gene/9606:USP31                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70CQ4                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||Nucleophile|||Polar residues|||Pro residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 31                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249518|||http://purl.uniprot.org/annotation/VAR_027422|||http://purl.uniprot.org/annotation/VAR_027423|||http://purl.uniprot.org/annotation/VAR_027424|||http://purl.uniprot.org/annotation/VAR_027425|||http://purl.uniprot.org/annotation/VAR_027426|||http://purl.uniprot.org/annotation/VAR_051534|||http://purl.uniprot.org/annotation/VAR_051535|||http://purl.uniprot.org/annotation/VSP_020459|||http://purl.uniprot.org/annotation/VSP_020460|||http://purl.uniprot.org/annotation/VSP_020461|||http://purl.uniprot.org/annotation/VSP_020462
http://togogenome.org/gene/9606:CYP4F2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78329                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Propeptide|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Associated with coumarin resistance; increased warfarin maintenance dose in patients on warfarin anti-coagulant therapy due to decreased vitamin K catabolism; decreased phylloquinone omega-hydroxylase activity; decreased production of 20-hydroxyeicosatetraenoic acid (20-HETE).|||Cytochrome P450 4F2|||In isoform 2.|||axial binding residue|||covalent                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051850|||http://purl.uniprot.org/annotation/PRO_0000430581|||http://purl.uniprot.org/annotation/VAR_013116|||http://purl.uniprot.org/annotation/VAR_013117|||http://purl.uniprot.org/annotation/VAR_013118|||http://purl.uniprot.org/annotation/VAR_013119|||http://purl.uniprot.org/annotation/VAR_013120|||http://purl.uniprot.org/annotation/VAR_020125|||http://purl.uniprot.org/annotation/VSP_055578|||http://purl.uniprot.org/annotation/VSP_055579|||http://purl.uniprot.org/annotation/VSP_055580
http://togogenome.org/gene/9606:ECHDC2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86YB7                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transit Peptide                                                                                  ^@                                                                                  Enoyl-CoA hydratase domain-containing protein 2, mitochondrial|||Important for catalytic activity|||In isoform 2.|||Mitochondrion|||N6-acetyllysine; alternate|||N6-succinyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000309459|||http://purl.uniprot.org/annotation/VAR_036951|||http://purl.uniprot.org/annotation/VSP_029177
http://togogenome.org/gene/9606:DUT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0C4DGL3|||http://purl.uniprot.org/uniprot/H0YNW5|||http://purl.uniprot.org/uniprot/P33316                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Transit Peptide|||Turn                                                                                  ^@                                                                                  Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial|||Disordered|||In BMFDMS.|||In BMFDMS; unknown pathological significance.|||In isoform 2.|||Loss of phosphorylation.|||Mitochondrion|||Phosphoserine|||Removed|||dUTPase-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007392|||http://purl.uniprot.org/annotation/VAR_022314|||http://purl.uniprot.org/annotation/VAR_087697|||http://purl.uniprot.org/annotation/VAR_087698|||http://purl.uniprot.org/annotation/VAR_087699|||http://purl.uniprot.org/annotation/VSP_001324
http://togogenome.org/gene/9606:C19orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HLH2|||http://purl.uniprot.org/uniprot/Q8N9M1                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Splice Variant                                                                                  ^@                                                                                  DUF5577|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Uncharacterized protein C19orf47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000291860|||http://purl.uniprot.org/annotation/VSP_026275|||http://purl.uniprot.org/annotation/VSP_026276
http://togogenome.org/gene/9606:LRRC3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PB8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Signal Peptide|||Strand|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Repeat|||Signal Peptide|||Strand|||Transmembrane                                                                                  ^@                                                                                  Helical|||LRR 1|||LRR 2|||LRR 3|||LRRCT|||LRRNT|||Leucine-rich repeat-containing protein 3B|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000021616
http://togogenome.org/gene/9606:SHARPIN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6PJD5|||http://purl.uniprot.org/uniprot/Q9H0F6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to ubiquitin and ability to mediate linear polyubiquitination.|||Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-354.|||Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-357.|||Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-368.|||Abolishes binding to ubiquitin without affecting interaction with RNF31; when associated with S-371.|||Abolishes homodimerization.|||Abolishes interaction with RNF31 and ability to mediate linear polyubiquitination.|||Disordered|||In isoform 2.|||Interaction with SHANK1|||Phosphoserine|||Pro residues|||RanBP2-type|||Self-association|||Sharpin|||Ubiquitin-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280634|||http://purl.uniprot.org/annotation/VAR_047799|||http://purl.uniprot.org/annotation/VAR_047800|||http://purl.uniprot.org/annotation/VAR_047801|||http://purl.uniprot.org/annotation/VSP_023837|||http://purl.uniprot.org/annotation/VSP_023838
http://togogenome.org/gene/9606:BRD3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15059                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acetylated histone H3 binding|||Basic and acidic residues|||Breakpoint for translocation to form BDR3-NUTM1 fusion protein|||Bromo 1|||Bromo 2|||Bromodomain-containing protein 3|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a gastric adenocarcinoma sample; somatic mutation.|||In a renal clear cell carcinoma sample; somatic mutation.|||In isoform 2.|||N-acetylserine|||NET|||Phosphoserine|||Polar residues|||Pro residues|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211181|||http://purl.uniprot.org/annotation/VAR_041913|||http://purl.uniprot.org/annotation/VAR_041914|||http://purl.uniprot.org/annotation/VAR_041915|||http://purl.uniprot.org/annotation/VAR_041916|||http://purl.uniprot.org/annotation/VAR_041917|||http://purl.uniprot.org/annotation/VAR_041918|||http://purl.uniprot.org/annotation/VSP_010247|||http://purl.uniprot.org/annotation/VSP_010248
http://togogenome.org/gene/9606:NR4A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92570                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Activation function (AF)-1 domain|||Basic residues|||Disordered|||In isoform 3.|||In isoform Beta.|||Interaction with KAT2B|||Interaction with NCOA1, NCOA2, NCOA3 and KAT2B|||NR C4-type|||NR LBD|||Nuclear receptor|||Nuclear receptor subfamily 4 group A member 3|||Polar residues|||Required for DNA-PK heterotrimer                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053722|||http://purl.uniprot.org/annotation/VSP_003712|||http://purl.uniprot.org/annotation/VSP_003713|||http://purl.uniprot.org/annotation/VSP_037877
http://togogenome.org/gene/9606:KALRN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HKJ7|||http://purl.uniprot.org/uniprot/A0A804HKT9|||http://purl.uniprot.org/uniprot/C9IZQ6|||http://purl.uniprot.org/uniprot/O60229                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||CRAL-TRIO|||DH|||DH 1|||DH 2|||Disordered|||Fibronectin type-III|||Ig-like C2-type|||In a breast cancer sample; somatic mutation.|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 4 and isoform 6.|||In isoform 5 and isoform 6.|||In isoform 5.|||Kalirin|||Loss of autophosphorylation.|||PH|||PH 1|||PH 2|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||SH3|||SH3 1|||SH3 2|||Spectrin 1|||Spectrin 2|||Spectrin 3|||Spectrin 4|||Spectrin 5|||Spectrin 6|||Spectrin 7|||Spectrin 8|||Spectrin 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080955|||http://purl.uniprot.org/annotation/VAR_020192|||http://purl.uniprot.org/annotation/VAR_035625|||http://purl.uniprot.org/annotation/VAR_035976|||http://purl.uniprot.org/annotation/VAR_041898|||http://purl.uniprot.org/annotation/VAR_057190|||http://purl.uniprot.org/annotation/VSP_028903|||http://purl.uniprot.org/annotation/VSP_028904|||http://purl.uniprot.org/annotation/VSP_028909|||http://purl.uniprot.org/annotation/VSP_028910|||http://purl.uniprot.org/annotation/VSP_028911|||http://purl.uniprot.org/annotation/VSP_028912|||http://purl.uniprot.org/annotation/VSP_028913|||http://purl.uniprot.org/annotation/VSP_028914|||http://purl.uniprot.org/annotation/VSP_028915
http://togogenome.org/gene/9606:SLC22A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y694                                                                                  ^@                                                                                  Active Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||Important for glutamate counteranion efflux|||In isoform 2 and isoform 3.|||In isoform 3.|||In isoform 4.|||Loss of glutamate transport activity; strong decrease in orotate transport activity.|||N-linked (GlcNAc...) asparagine|||Solute carrier family 22 member 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317481|||http://purl.uniprot.org/annotation/VAR_047875|||http://purl.uniprot.org/annotation/VAR_047876|||http://purl.uniprot.org/annotation/VAR_047877|||http://purl.uniprot.org/annotation/VSP_030991|||http://purl.uniprot.org/annotation/VSP_030992|||http://purl.uniprot.org/annotation/VSP_030993|||http://purl.uniprot.org/annotation/VSP_030994
http://togogenome.org/gene/9606:C22orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IC83                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Sequence Variant                                                                                  ^@                                                                                  Uncharacterized protein C22orf42                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344364|||http://purl.uniprot.org/annotation/VAR_045606
http://togogenome.org/gene/9606:ADAMTS15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TE58                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Propeptide|||Region|||Sequence Variant|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Motif|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  A disintegrin and metalloproteinase with thrombospondin motifs 15|||Basic and acidic residues|||Cysteine switch|||Disintegrin|||Disordered|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||Peptidase M12B|||Spacer|||TSP type-1 1|||TSP type-1 2|||TSP type-1 3|||in inhibited form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000029192|||http://purl.uniprot.org/annotation/PRO_0000029193|||http://purl.uniprot.org/annotation/VAR_036150|||http://purl.uniprot.org/annotation/VAR_036151|||http://purl.uniprot.org/annotation/VAR_051594
http://togogenome.org/gene/9606:STK17A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UEE5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Loss of activity and of apoptotic function.|||Phosphoserine|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase 17A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086704|||http://purl.uniprot.org/annotation/VAR_019991|||http://purl.uniprot.org/annotation/VAR_032823|||http://purl.uniprot.org/annotation/VAR_041145|||http://purl.uniprot.org/annotation/VAR_041146
http://togogenome.org/gene/9606:ARHGEF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92974                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes microtubule binding, increased activity in vitro.|||Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-143.|||Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-896.|||Basic and acidic residues|||DH|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||Increases activity. Abolishes nucleotide exchange activity; when associated with D-886.|||Increases activity. Abolishes nucleotide exchange activity; when associated with D-960.|||Interaction with DYNLT1|||N6-acetyllysine|||Normal activity.|||PH|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphoserine; by PAK1 and AURKA|||Phosphoserine; by PAK4|||Phosphothreonine|||Phosphothreonine; by MAPK1 or MAPK3|||Phosphotyrosine|||Reduces phosphorylation level, normal microtubule localization and activity.|||Reduces phosphorylation level.|||Rho guanine nucleotide exchange factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080909|||http://purl.uniprot.org/annotation/VSP_039457|||http://purl.uniprot.org/annotation/VSP_039458
http://togogenome.org/gene/9606:ZNF492                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P255                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12; degenerate|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||KRAB|||Zinc finger protein 492                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047615|||http://purl.uniprot.org/annotation/VAR_052845
http://togogenome.org/gene/9606:GPCPD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NPB8                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  CBM20|||GP-PDE|||Glycerophosphocholine phosphodiesterase GPCPD1|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000050797|||http://purl.uniprot.org/annotation/VAR_022060
http://togogenome.org/gene/9606:LRRC42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y546                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||Leucine-rich repeat-containing protein 42|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000223622
http://togogenome.org/gene/9606:FTO                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1B0GTC5|||http://purl.uniprot.org/uniprot/B3KU60|||http://purl.uniprot.org/uniprot/Q9C0B1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs.|||Abolishes enzyme activity.|||Abolishes enzyme activity. Abolishes ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs; when associated with Q-322.|||Almost abolishes enzyme activity.|||Alpha-ketoglutarate-dependent dioxygenase FTO|||Alpha-ketoglutarate-dependent dioxygenase FTO catalytic|||Fe2OG dioxygenase domain|||Found in a patient with microcephaly, developmental delay, behavioral abnormalities, dysmorphic facial features, hypotonia and other various phenotypic abnormalities; unknown pathological significance.|||In GDFD.|||In GDFD; has no residual normal activity, impaired ability to demethylate N(6)-methyladenosine RNAs (m6A) RNAs.|||In GDFD; reduced enzyme activity.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Loop L1; predicted to block binding of double-stranded DNA or RNA|||N6-acetyllysine|||Perturbs interaction between N-terminal and C-terminal domains and strongly reduces enzyme activity.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286163|||http://purl.uniprot.org/annotation/VAR_032078|||http://purl.uniprot.org/annotation/VAR_063252|||http://purl.uniprot.org/annotation/VAR_075468|||http://purl.uniprot.org/annotation/VAR_075469|||http://purl.uniprot.org/annotation/VAR_076423|||http://purl.uniprot.org/annotation/VSP_025002|||http://purl.uniprot.org/annotation/VSP_025003|||http://purl.uniprot.org/annotation/VSP_025004|||http://purl.uniprot.org/annotation/VSP_025005|||http://purl.uniprot.org/annotation/VSP_025006
http://togogenome.org/gene/9606:PRSS35                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3Z0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Inactive serine protease 35|||N-linked (GlcNAc...) asparagine|||Peptidase S1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000299358|||http://purl.uniprot.org/annotation/VAR_034810
http://togogenome.org/gene/9606:CENPP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6IPU0|||http://purl.uniprot.org/uniprot/Q7Z672                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Modified Residue|||Non-terminal Residue|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Centromere protein P|||In isoform 2.|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249506|||http://purl.uniprot.org/annotation/VSP_055368|||http://purl.uniprot.org/annotation/VSP_055369
http://togogenome.org/gene/9606:ABCC9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60706                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ABC transmembrane type-1 1|||ABC transmembrane type-1 2|||ABC transporter 1|||ABC transporter 2|||ATP-binding cassette sub-family C member 9|||Acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=13|||Helical; Name=14|||Helical; Name=15|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||In ATFB12; compromises adenine nucleotide-dependent induction of KATP current; mutant ABCC9 that is coexpressed with KCNJ11 pore generates an aberrant channel that retains ATP-induced inhibition of potassium current, but shows a blunted response to ADP.|||In CMD1O.|||In HTOCD.|||In HTOCD; mutant channels show reduced ATP sensitivity.|||In HTOCD; mutant channels show reduced ATP sensitivity; rat ABCC9 construct containing this mutation shows gain of function.|||In HTOCD; rat ABCC9 construct containing this mutation shows gain of function.|||In isoform SUR2B.|||N-linked (GlcNAc...) asparagine|||Unknown pathological significance.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000093402|||http://purl.uniprot.org/annotation/VAR_018483|||http://purl.uniprot.org/annotation/VAR_048143|||http://purl.uniprot.org/annotation/VAR_066210|||http://purl.uniprot.org/annotation/VAR_068485|||http://purl.uniprot.org/annotation/VAR_068486|||http://purl.uniprot.org/annotation/VAR_068487|||http://purl.uniprot.org/annotation/VAR_068488|||http://purl.uniprot.org/annotation/VAR_068489|||http://purl.uniprot.org/annotation/VAR_068490|||http://purl.uniprot.org/annotation/VAR_068491|||http://purl.uniprot.org/annotation/VAR_068492|||http://purl.uniprot.org/annotation/VAR_068493|||http://purl.uniprot.org/annotation/VAR_068494|||http://purl.uniprot.org/annotation/VAR_068495|||http://purl.uniprot.org/annotation/VAR_068496|||http://purl.uniprot.org/annotation/VAR_068497|||http://purl.uniprot.org/annotation/VAR_083082|||http://purl.uniprot.org/annotation/VSP_000058
http://togogenome.org/gene/9606:HIC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0PJI1|||http://purl.uniprot.org/uniprot/Q14526                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes interaction with CTBP1 and CTBP2. Impairs transcriptional repression.|||Abolishes repression activity.|||Abolishes sumoylation; impairs transcriptional repression activity.|||BTB|||Basic and acidic residues|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Hypermethylated in cancer 1 protein|||Impairs K-333 acetylation; no effect on sumoylation. Decreases interaction with MTA1.|||Impairs transcriptional repression activity. Decreases interaction with MTA1.|||In isoform 2.|||Interaction with CTBP1|||Mediates HDAC-dependent transcriptional repression|||Mimicks acetylation. Impairs interaction with RBBP4 and MTA1 and no effect on interaction with CTBP2. Reduces transcriptional repression.|||N6-acetyllysine; alternate|||Omega-N-methylarginine|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046942|||http://purl.uniprot.org/annotation/VAR_063109|||http://purl.uniprot.org/annotation/VSP_006826
http://togogenome.org/gene/9606:TPM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWU8|||http://purl.uniprot.org/uniprot/A0A0S2Z4G4|||http://purl.uniprot.org/uniprot/A0A0S2Z4I4|||http://purl.uniprot.org/uniprot/B4DQ80|||http://purl.uniprot.org/uniprot/P06753                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Helix|||Initiator Methionine|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In CMYP4A.|||In CMYP4A; also found in patients with undefined congenital myopathy.|||In CMYP4A; decrease in the sensitivity of contraction to activating calcium.|||In isoform 2, isoform 3 and isoform 6.|||In isoform 2, isoform 5 and isoform 7.|||In isoform 3.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 7.|||N-acetylalanine|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Probable disease-associated variant found in patients with undefined congenital myopathy.|||Removed|||Tropomyosin alpha-3 chain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000205632|||http://purl.uniprot.org/annotation/VAR_013460|||http://purl.uniprot.org/annotation/VAR_070066|||http://purl.uniprot.org/annotation/VAR_070067|||http://purl.uniprot.org/annotation/VAR_070068|||http://purl.uniprot.org/annotation/VAR_070069|||http://purl.uniprot.org/annotation/VAR_070070|||http://purl.uniprot.org/annotation/VAR_070071|||http://purl.uniprot.org/annotation/VAR_071499|||http://purl.uniprot.org/annotation/VAR_071500|||http://purl.uniprot.org/annotation/VAR_071501|||http://purl.uniprot.org/annotation/VAR_071502|||http://purl.uniprot.org/annotation/VAR_071503|||http://purl.uniprot.org/annotation/VAR_071504|||http://purl.uniprot.org/annotation/VAR_071505|||http://purl.uniprot.org/annotation/VAR_071506|||http://purl.uniprot.org/annotation/VAR_071507|||http://purl.uniprot.org/annotation/VAR_071508|||http://purl.uniprot.org/annotation/VAR_071509|||http://purl.uniprot.org/annotation/VSP_006604|||http://purl.uniprot.org/annotation/VSP_006605|||http://purl.uniprot.org/annotation/VSP_006606|||http://purl.uniprot.org/annotation/VSP_006607|||http://purl.uniprot.org/annotation/VSP_047302|||http://purl.uniprot.org/annotation/VSP_047303|||http://purl.uniprot.org/annotation/VSP_047304|||http://purl.uniprot.org/annotation/VSP_047305|||http://purl.uniprot.org/annotation/VSP_047306|||http://purl.uniprot.org/annotation/VSP_054792
http://togogenome.org/gene/9606:EFHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WYH2|||http://purl.uniprot.org/uniprot/Q9BUP0                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand domain-containing protein D1|||In isoform 2.|||In mtEFHD1; abolished ability to enhance mitoflash activity; when associated with A-103; A-139 and K-150.|||In mtEFHD1; abolished ability to enhance mitoflash activity; when associated with A-103; K-114 and A-139.|||In mtEFHD1; abolished ability to enhance mitoflash activity; when associated with A-103; K-114 and K-150.|||In mtEFHD1; abolished ability to enhance mitoflash activity; when associated with K-114; A-139 and K-150.|||Phosphoserine|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073643|||http://purl.uniprot.org/annotation/VAR_047966|||http://purl.uniprot.org/annotation/VSP_045541
http://togogenome.org/gene/9606:LRRC28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X40                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||LRR 1|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||Leucine-rich repeat-containing protein 28                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000272298|||http://purl.uniprot.org/annotation/VAR_034084|||http://purl.uniprot.org/annotation/VSP_022393|||http://purl.uniprot.org/annotation/VSP_022394|||http://purl.uniprot.org/annotation/VSP_022395
http://togogenome.org/gene/9606:GATB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75879                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Transit Peptide                                                                                  ^@                                                                                  Disordered|||Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial|||In COXPD41; unknown pathological significance.|||Mitochondrion|||N6-succinyllysine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010710|||http://purl.uniprot.org/annotation/VAR_049128|||http://purl.uniprot.org/annotation/VAR_083986
http://togogenome.org/gene/9606:PTPN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K3M3|||http://purl.uniprot.org/uniprot/B4DSN5|||http://purl.uniprot.org/uniprot/P18031                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Associated with low glucose tolerance.|||Catalytically inactive mutant; abolishes sulfhydration.|||Cysteine persulfide; alternate|||Cysteine sulfenic acid (-SOH); alternate|||Cysteine sulfinic acid (-SO2H); alternate|||Disordered|||Helical|||N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form|||N-acetylmethionine|||No phosphorylation.|||Phosphocysteine intermediate|||Phosphoserine|||Phosphoserine; by CDK1|||Phosphoserine; by CLK1 and CLK2|||Phosphoserine; by PKB/AKT1, CLK1 and CLK2|||Phosphoserine; by PKC|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by EGFR|||S-nitrosocysteine; in reversibly inhibited form|||Substrate-trapping mutant.|||Tyrosine specific protein phosphatases|||Tyrosine-protein phosphatase|||Tyrosine-protein phosphatase non-receptor type 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094748|||http://purl.uniprot.org/annotation/VAR_022013|||http://purl.uniprot.org/annotation/VAR_022014
http://togogenome.org/gene/9606:ABHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJD1|||http://purl.uniprot.org/uniprot/Q96SE0                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  AB hydrolase-1|||Charge relay system|||Helical|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein ABHD1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280204|||http://purl.uniprot.org/annotation/VAR_031087|||http://purl.uniprot.org/annotation/VAR_031088|||http://purl.uniprot.org/annotation/VAR_052484|||http://purl.uniprot.org/annotation/VSP_054269|||http://purl.uniprot.org/annotation/VSP_054270
http://togogenome.org/gene/9606:PRPF3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43395                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In RP18.|||In RP18; reduces phosphorylation; impairs binding to PRPF4; impairs self-association; affects interaction with the U4/U5/U6 tri-snRNP complex; does not affect global pre-mRNA splicing.|||In isoform 2.|||Mediates interaction with SART3|||PWI|||Phosphoserine|||Phosphothreonine|||U4/U6 small nuclear ribonucleoprotein Prp3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097044|||http://purl.uniprot.org/annotation/VAR_016877|||http://purl.uniprot.org/annotation/VAR_046735|||http://purl.uniprot.org/annotation/VAR_051286|||http://purl.uniprot.org/annotation/VSP_056265|||http://purl.uniprot.org/annotation/VSP_056266|||http://purl.uniprot.org/annotation/VSP_056267
http://togogenome.org/gene/9606:RNASE12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5GAN4|||http://purl.uniprot.org/uniprot/W0UV30                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide                                                                                  ^@                                                                                  Probable inactive ribonuclease-like protein 12|||Ribonuclease A-domain                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000308702|||http://purl.uniprot.org/annotation/PRO_5014314783
http://togogenome.org/gene/9606:XRN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZH2                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5'-3' exoribonuclease 1|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071392|||http://purl.uniprot.org/annotation/VAR_053000|||http://purl.uniprot.org/annotation/VAR_053001|||http://purl.uniprot.org/annotation/VSP_016692|||http://purl.uniprot.org/annotation/VSP_016693|||http://purl.uniprot.org/annotation/VSP_016694|||http://purl.uniprot.org/annotation/VSP_016695
http://togogenome.org/gene/9606:GSTA5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTV2                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  GST C-terminal|||GST N-terminal|||Glutathione S-transferase A5|||N-acetylalanine|||N6-succinyllysine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000185787|||http://purl.uniprot.org/annotation/VAR_024483
http://togogenome.org/gene/9606:DCLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A9L9PXT2|||http://purl.uniprot.org/uniprot/B7Z5K4|||http://purl.uniprot.org/uniprot/O15075|||http://purl.uniprot.org/uniprot/Q5VZY9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||Doublecortin|||Doublecortin 1|||Doublecortin 2|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 1 and isoform 3.|||In isoform 3 and isoform 4.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase DCLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085919|||http://purl.uniprot.org/annotation/VAR_045673|||http://purl.uniprot.org/annotation/VAR_045674|||http://purl.uniprot.org/annotation/VAR_045675|||http://purl.uniprot.org/annotation/VAR_045676|||http://purl.uniprot.org/annotation/VAR_045677|||http://purl.uniprot.org/annotation/VSP_004905|||http://purl.uniprot.org/annotation/VSP_004906|||http://purl.uniprot.org/annotation/VSP_004907
http://togogenome.org/gene/9606:OR1J1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWP9|||http://purl.uniprot.org/uniprot/Q8NGS3                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 1J1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150438|||http://purl.uniprot.org/annotation/VAR_059978
http://togogenome.org/gene/9606:KRBA2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8MX02|||http://purl.uniprot.org/uniprot/Q6ZNG9                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Integrase catalytic|||KRAB|||KRAB-A domain-containing protein 2|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000300113|||http://purl.uniprot.org/annotation/VAR_051087
http://togogenome.org/gene/9606:EVX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DRC0|||http://purl.uniprot.org/uniprot/P49640                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox even-skipped homolog protein 1|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048870|||http://purl.uniprot.org/annotation/VSP_056502
http://togogenome.org/gene/9606:ZSCAN23                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3MJ62                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||SCAN box|||Zinc finger and SCAN domain-containing protein 23                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000280411
http://togogenome.org/gene/9606:NBPF8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A8V8TN03                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Basic residues|||Disordered|||Olduvai                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:SCGB3A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96QR1                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Modification|||Molecule Processing|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Interchain|||Secretoglobin family 3A member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000036383
http://togogenome.org/gene/9606:ZCCHC13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WW36                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Zinc Finger                                                                                  ^@                                                                                  CCHC-type 1; degenerate|||CCHC-type 2; degenerate|||CCHC-type 3|||CCHC-type 4|||CCHC-type 5|||CCHC-type 6|||Zinc finger CCHC domain-containing protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150974
http://togogenome.org/gene/9606:PALD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULE6                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||N-myristoyl glycine|||Paladin|||Phosphoserine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286130|||http://purl.uniprot.org/annotation/VAR_032076|||http://purl.uniprot.org/annotation/VAR_032077|||http://purl.uniprot.org/annotation/VAR_062188
http://togogenome.org/gene/9606:PGP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NDG6                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Molecule Processing|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Site                                                                                  ^@                                                                                  Glycerol-3-phosphate phosphatase|||Important for substrate specificity|||Nucleophile|||Proton donor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000316888
http://togogenome.org/gene/9606:MAPK9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D7R525|||http://purl.uniprot.org/uniprot/P45984                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In a head & Neck squamous cell carcinoma sample; somatic mutation.|||In isoform 5.|||In isoform Alpha-1 and isoform Beta-1.|||In isoform Beta-1 and isoform Beta-2.|||Mitogen-activated protein kinase 9|||Phosphothreonine; by MAP2K7|||Phosphotyrosine; by MAP2K4|||Polar residues|||Protein kinase|||Proton acceptor|||TXY                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000186273|||http://purl.uniprot.org/annotation/VAR_025175|||http://purl.uniprot.org/annotation/VAR_042260|||http://purl.uniprot.org/annotation/VAR_042261|||http://purl.uniprot.org/annotation/VAR_042262|||http://purl.uniprot.org/annotation/VAR_042263|||http://purl.uniprot.org/annotation/VSP_004834|||http://purl.uniprot.org/annotation/VSP_004835|||http://purl.uniprot.org/annotation/VSP_041908|||http://purl.uniprot.org/annotation/VSP_041909
http://togogenome.org/gene/9606:METTL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96IZ6                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Phosphoserine|||Phosphothreonine|||Removed|||tRNA N(3)-methylcytidine methyltransferase METTL2A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204452|||http://purl.uniprot.org/annotation/VSP_008477
http://togogenome.org/gene/9606:TAS2R9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NYW1                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Taste receptor type 2 member 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000082232|||http://purl.uniprot.org/annotation/VAR_020204|||http://purl.uniprot.org/annotation/VAR_053345|||http://purl.uniprot.org/annotation/VAR_053346
http://togogenome.org/gene/9606:SAMD13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5VXD3                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||SAM|||Sterile alpha motif domain-containing protein 13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279505|||http://purl.uniprot.org/annotation/VSP_023463|||http://purl.uniprot.org/annotation/VSP_023464|||http://purl.uniprot.org/annotation/VSP_044972
http://togogenome.org/gene/9606:ZFYVE28                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9HCC9                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Abolishes binding to phosphatidylinositol 3-phosphate (PI3P).|||Abolishes monoubiquitination and promotes localization to early endosomes.|||Disordered|||FYVE-type|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)|||In isoform 2 and isoform 4.|||In isoform 3, isoform 4 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||In isoform 8.|||Lateral signaling target protein 2 homolog|||Phosphoserine|||Phosphoserine; by MAP2K|||Phosphothreonine|||Phosphothreonine; by MAP2K|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000098722|||http://purl.uniprot.org/annotation/VAR_052988|||http://purl.uniprot.org/annotation/VAR_052989|||http://purl.uniprot.org/annotation/VSP_037614|||http://purl.uniprot.org/annotation/VSP_037615|||http://purl.uniprot.org/annotation/VSP_037616|||http://purl.uniprot.org/annotation/VSP_045805|||http://purl.uniprot.org/annotation/VSP_045806|||http://purl.uniprot.org/annotation/VSP_046092|||http://purl.uniprot.org/annotation/VSP_046093|||http://purl.uniprot.org/annotation/VSP_046094|||http://purl.uniprot.org/annotation/VSP_046379
http://togogenome.org/gene/9606:CATSPERZ                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NTU4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Cation channel sperm-associated auxiliary subunit zeta|||Disordered                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000349322|||http://purl.uniprot.org/annotation/VAR_046370
http://togogenome.org/gene/9606:TIMM29                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BSF4                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transit Peptide|||Transmembrane                                                                                  ^@                                                                                  Helical|||Mitochondrial import inner membrane translocase subunit Tim29|||Mitochondrial intermembrane|||Mitochondrial matrix|||Mitochondrion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271006
http://togogenome.org/gene/9606:SEC16B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96JE7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Central conserved domain (CCD); required for localization to endoplasmic reticulum exit sites|||Disordered|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein transport protein Sec16B|||Required for endoplasmic reticulum localization                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000341974|||http://purl.uniprot.org/annotation/VAR_044130|||http://purl.uniprot.org/annotation/VAR_044131|||http://purl.uniprot.org/annotation/VAR_044132|||http://purl.uniprot.org/annotation/VAR_044133|||http://purl.uniprot.org/annotation/VAR_044134|||http://purl.uniprot.org/annotation/VSP_034371|||http://purl.uniprot.org/annotation/VSP_034372|||http://purl.uniprot.org/annotation/VSP_034373|||http://purl.uniprot.org/annotation/VSP_034374|||http://purl.uniprot.org/annotation/VSP_034375|||http://purl.uniprot.org/annotation/VSP_034376
http://togogenome.org/gene/9606:C5orf15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NC54                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Keratinocyte-associated transmembrane protein 2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000019579
http://togogenome.org/gene/9606:CCDC138                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96M89                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Modified Residue|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 138|||In isoform 2.|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000288454|||http://purl.uniprot.org/annotation/VAR_032420|||http://purl.uniprot.org/annotation/VAR_032421|||http://purl.uniprot.org/annotation/VSP_025683|||http://purl.uniprot.org/annotation/VSP_025684
http://togogenome.org/gene/9606:SOX15                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60248                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||HMG box|||In isoform 2.|||Interaction with FHL3|||Phosphoserine|||Polar residues|||Pro residues|||Protein SOX-15|||Required to promote HAND1 transcriptional activator activity                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048762|||http://purl.uniprot.org/annotation/VSP_056668
http://togogenome.org/gene/9606:CHST5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZS9                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Carbohydrate sulfotransferase 5|||Cytoplasmic|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085195|||http://purl.uniprot.org/annotation/VAR_021416|||http://purl.uniprot.org/annotation/VAR_057993|||http://purl.uniprot.org/annotation/VSP_037526
http://togogenome.org/gene/9606:NALF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B1AL88                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Region|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Disordered|||Helical|||N-linked (GlcNAc...) asparagine|||NALCN channel auxiliary factor 1|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000339373
http://togogenome.org/gene/9606:HTR2C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K9J958|||http://purl.uniprot.org/uniprot/P28335                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  5-hydroxytryptamine receptor 2C|||Cytoplasmic|||DRY motif; important for ligand-induced conformation changes|||Decreases interaction with ARRB2.|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In RNA edited version.|||In isoform 2.|||Loss of interaction with MPDZ.|||N-linked (GlcNAc...) asparagine|||NPxxY motif; important for ligand-induced conformation changes and signaling|||No effect on interaction with MPDZ.|||PDZ-binding                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068958|||http://purl.uniprot.org/annotation/VAR_003450|||http://purl.uniprot.org/annotation/VAR_010166|||http://purl.uniprot.org/annotation/VAR_010167|||http://purl.uniprot.org/annotation/VAR_010168|||http://purl.uniprot.org/annotation/VSP_045171
http://togogenome.org/gene/9606:ZNF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYR5|||http://purl.uniprot.org/uniprot/B4DR15|||http://purl.uniprot.org/uniprot/Q68CY6|||http://purl.uniprot.org/uniprot/Q9BSG1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type|||C2H2-type 1|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9; degenerate|||Disordered|||In isoform 3.|||In isoform 4.|||KRAB|||Zinc finger protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274049|||http://purl.uniprot.org/annotation/VSP_060237|||http://purl.uniprot.org/annotation/VSP_060238
http://togogenome.org/gene/9606:GTPBP8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N3Z3|||http://purl.uniprot.org/uniprot/Q9P025                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  EngB-type G|||GTP-binding protein 8|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000338612|||http://purl.uniprot.org/annotation/VAR_048934|||http://purl.uniprot.org/annotation/VSP_034055|||http://purl.uniprot.org/annotation/VSP_034056|||http://purl.uniprot.org/annotation/VSP_034057
http://togogenome.org/gene/9606:GADD45A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P24522                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Modified Residue|||Mutagenesis Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes dimerization.|||Growth arrest and DNA damage-inducible protein GADD45 alpha|||In isoform 2.|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000148331|||http://purl.uniprot.org/annotation/VSP_042523
http://togogenome.org/gene/9606:CTAG1B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P78358                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Region|||Splice Variant|||Turn                                                                                  ^@                                                                                  Cancer/testis antigen 1|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218922|||http://purl.uniprot.org/annotation/VSP_028548
http://togogenome.org/gene/9606:RRP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P56182                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant                                                                                  ^@                                                                                  Abolishes methylation by N6AMT1.|||Basic and acidic residues|||Disordered|||N5-methylglutamine|||Phosphoserine|||Phosphothreonine|||Ribosomal RNA processing protein 1 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096887|||http://purl.uniprot.org/annotation/VAR_053894|||http://purl.uniprot.org/annotation/VAR_053895
http://togogenome.org/gene/9606:ABLIM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KSG3|||http://purl.uniprot.org/uniprot/B4DQA3|||http://purl.uniprot.org/uniprot/O14639                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Actin-binding LIM protein 1|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||HP|||In isoform 2 and isoform 6.|||In isoform 3, isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 6.|||LIM zinc-binding|||LIM zinc-binding 1|||LIM zinc-binding 2|||LIM zinc-binding 3|||LIM zinc-binding 4|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075697|||http://purl.uniprot.org/annotation/VAR_050141|||http://purl.uniprot.org/annotation/VAR_050142|||http://purl.uniprot.org/annotation/VSP_012099|||http://purl.uniprot.org/annotation/VSP_012100|||http://purl.uniprot.org/annotation/VSP_012101|||http://purl.uniprot.org/annotation/VSP_012102|||http://purl.uniprot.org/annotation/VSP_041185|||http://purl.uniprot.org/annotation/VSP_057209
http://togogenome.org/gene/9606:AQP12B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NM10|||http://purl.uniprot.org/uniprot/Q8IUS6                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Motif|||Non-terminal Residue|||Region|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Aquaporin-12B|||Disordered|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||In isoform 2.|||NPA 1|||NPA 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000328826|||http://purl.uniprot.org/annotation/VSP_032800
http://togogenome.org/gene/9606:RGS9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K1G1|||http://purl.uniprot.org/uniprot/O75916                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  DEP|||Disordered|||G protein gamma|||In PERRS1.|||In isoform 2.|||In isoform 3 and isoform 5.|||In isoform 3.|||In isoform 4.|||Polar residues|||RGS|||Regulator of G-protein signaling 9                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204203|||http://purl.uniprot.org/annotation/VAR_017912|||http://purl.uniprot.org/annotation/VAR_051796|||http://purl.uniprot.org/annotation/VSP_005674|||http://purl.uniprot.org/annotation/VSP_005675|||http://purl.uniprot.org/annotation/VSP_038381|||http://purl.uniprot.org/annotation/VSP_038382|||http://purl.uniprot.org/annotation/VSP_038383
http://togogenome.org/gene/9606:GSG1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A494C0G6|||http://purl.uniprot.org/uniprot/F1T0A1|||http://purl.uniprot.org/uniprot/Q2KHT4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Germ cell-specific gene 1 protein|||Helical|||In isoform 2 and isoform 5.|||In isoform 3, isoform 4, isoform 5, isoform 6 and isoform 8.|||In isoform 4.|||In isoform 6 and isoform 7.|||In isoform 7.|||In isoform 8.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000329461|||http://purl.uniprot.org/annotation/VAR_042684|||http://purl.uniprot.org/annotation/VAR_042685|||http://purl.uniprot.org/annotation/VSP_032992|||http://purl.uniprot.org/annotation/VSP_032993|||http://purl.uniprot.org/annotation/VSP_032994|||http://purl.uniprot.org/annotation/VSP_032995|||http://purl.uniprot.org/annotation/VSP_032996|||http://purl.uniprot.org/annotation/VSP_032997
http://togogenome.org/gene/9606:OAZ2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95190                                                                                  ^@                                                                                  Chain|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  Ornithine decarboxylase antizyme 2|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220857|||http://purl.uniprot.org/annotation/VAR_050420
http://togogenome.org/gene/9606:CCDC127                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BQ5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Sequence Variant                                                                                  ^@                                                                                  Coiled-coil domain-containing protein 127                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263750|||http://purl.uniprot.org/annotation/VAR_050737
http://togogenome.org/gene/9606:FBF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TES7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Crosslink|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Fas-binding factor 1|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5 and isoform 6.|||In isoform 5.|||In isoform 6.|||Phosphoserine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000297646|||http://purl.uniprot.org/annotation/VAR_034659|||http://purl.uniprot.org/annotation/VAR_034660|||http://purl.uniprot.org/annotation/VAR_034661|||http://purl.uniprot.org/annotation/VAR_034662|||http://purl.uniprot.org/annotation/VSP_027318|||http://purl.uniprot.org/annotation/VSP_027319|||http://purl.uniprot.org/annotation/VSP_027320|||http://purl.uniprot.org/annotation/VSP_027321|||http://purl.uniprot.org/annotation/VSP_027322|||http://purl.uniprot.org/annotation/VSP_027323|||http://purl.uniprot.org/annotation/VSP_040769|||http://purl.uniprot.org/annotation/VSP_040770|||http://purl.uniprot.org/annotation/VSP_041555
http://togogenome.org/gene/9606:TSSK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96PN8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Sequence Variant                                                                                  ^@                                                                                  Protein kinase|||Proton acceptor|||Testis-specific serine/threonine-protein kinase 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086770|||http://purl.uniprot.org/annotation/VAR_041245|||http://purl.uniprot.org/annotation/VAR_041246|||http://purl.uniprot.org/annotation/VAR_051678
http://togogenome.org/gene/9606:TMPRSS7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7RTY8                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Region|||Sequence Conflict|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  CUB 1|||CUB 2|||Charge relay system|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||LDL-receptor class A 1|||LDL-receptor class A 2|||LDL-receptor class A 3|||Peptidase S1|||Pro residues|||SEA|||Transmembrane protease serine 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000027859|||http://purl.uniprot.org/annotation/VSP_040771|||http://purl.uniprot.org/annotation/VSP_040772|||http://purl.uniprot.org/annotation/VSP_040773|||http://purl.uniprot.org/annotation/VSP_040774
http://togogenome.org/gene/9606:EIF2S1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P05198|||http://purl.uniprot.org/uniprot/Q53XC0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||Eukaryotic translation initiation factor 2 subunit 1|||N6-acetyllysine|||Phosphoserine|||Phosphoserine; by HRI|||Phosphothreonine|||S1 motif                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000137382
http://togogenome.org/gene/9606:PDS5A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/G1UI16|||http://purl.uniprot.org/uniprot/Q29RF7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Found in a patient with cohesinopathy; unknown pathological significance.|||HEAT|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Sister chromatid cohesion protein PDS5 homolog A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000296341|||http://purl.uniprot.org/annotation/VAR_082313|||http://purl.uniprot.org/annotation/VSP_052491|||http://purl.uniprot.org/annotation/VSP_052492
http://togogenome.org/gene/9606:MAGEA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P43360                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||MAGE|||Melanoma-associated antigen 6|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000156706|||http://purl.uniprot.org/annotation/VAR_053493
http://togogenome.org/gene/9606:NAT8L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9F0                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||N-acetylaspartate synthetase|||N-acetyltransferase|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000305229
http://togogenome.org/gene/9606:RTP3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BQQ7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Topological Domain|||Transmembrane|||Zinc Finger                                                                                  ^@                                                                                  3CxxC-type|||Cytoplasmic|||Helical|||Receptor-transporting protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181993
http://togogenome.org/gene/9606:ARNT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3A3|||http://purl.uniprot.org/uniprot/Q86TN1|||http://purl.uniprot.org/uniprot/Q9HBZ2|||http://purl.uniprot.org/uniprot/X5DQN9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Aryl hydrocarbon receptor nuclear translocator 2|||BHLH|||Basic and acidic residues|||Decreased transcription factor activity due to impaired localization to the nucleus.|||Decreased transcription factor activity.|||Disordered|||Does not affect the transcription factor activity.|||In isoform 2.|||Omega-N-methylarginine|||PAC|||PAS|||PAS 1|||PAS 2|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127122|||http://purl.uniprot.org/annotation/VAR_049538|||http://purl.uniprot.org/annotation/VAR_076841|||http://purl.uniprot.org/annotation/VAR_076842|||http://purl.uniprot.org/annotation/VAR_076843|||http://purl.uniprot.org/annotation/VAR_076844|||http://purl.uniprot.org/annotation/VSP_022687
http://togogenome.org/gene/9606:RHEX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZWK4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modification|||Modified Residue|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Modified Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Phosphotyrosine|||Regulator of hemoglobinization and erythroid cell expansion protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271103
http://togogenome.org/gene/9606:ASB18                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZVZ8                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Repeat|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||Ankyrin repeat and SOCS box protein 18|||In isoform 2.|||SOCS box                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000311875|||http://purl.uniprot.org/annotation/VAR_037331|||http://purl.uniprot.org/annotation/VAR_048289|||http://purl.uniprot.org/annotation/VAR_048290|||http://purl.uniprot.org/annotation/VAR_059128|||http://purl.uniprot.org/annotation/VSP_029621
http://togogenome.org/gene/9606:C12orf57                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99622                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  In TEMTYS.|||N-acetylalanine|||Protein C10|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000065034|||http://purl.uniprot.org/annotation/VAR_069774
http://togogenome.org/gene/9606:SSPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q14714                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||Sarcospan                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072226|||http://purl.uniprot.org/annotation/VAR_051384|||http://purl.uniprot.org/annotation/VAR_051385|||http://purl.uniprot.org/annotation/VSP_004431|||http://purl.uniprot.org/annotation/VSP_046351
http://togogenome.org/gene/9606:PRKAG2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N8Q6|||http://purl.uniprot.org/uniprot/A0A384MDZ2|||http://purl.uniprot.org/uniprot/B7Z6X8|||http://purl.uniprot.org/uniprot/E9PGP6|||http://purl.uniprot.org/uniprot/Q9UGJ0                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  5'-AMP-activated protein kinase subunit gamma-2|||AMPK pseudosubstrate|||Basic and acidic residues|||CBS|||CBS 1|||CBS 2|||CBS 3|||CBS 4|||Disordered|||In CMH6; severe.|||In CMH6; severe; impaired AMP- and ATP-binding.|||In GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit.|||In WPW and CMH6; impaired AMP- and ATP-binding.|||In WPW; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding.|||In isoform B.|||In isoform C.|||Induces phosphorylation by AMPK.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000204381|||http://purl.uniprot.org/annotation/VAR_013264|||http://purl.uniprot.org/annotation/VAR_013265|||http://purl.uniprot.org/annotation/VAR_013266|||http://purl.uniprot.org/annotation/VAR_013267|||http://purl.uniprot.org/annotation/VAR_013268|||http://purl.uniprot.org/annotation/VAR_013269|||http://purl.uniprot.org/annotation/VAR_032909|||http://purl.uniprot.org/annotation/VAR_048250|||http://purl.uniprot.org/annotation/VSP_000261|||http://purl.uniprot.org/annotation/VSP_015589
http://togogenome.org/gene/9606:MXI1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z3X5|||http://purl.uniprot.org/uniprot/P50539                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  BHLH|||Basic and acidic residues|||Disordered|||In isoform 2 and isoform 4.|||In isoform 3.|||In isoform 4.|||In prostate cancer.|||Max-interacting protein 1|||Polar residues|||bHLH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000127285|||http://purl.uniprot.org/annotation/VAR_004499|||http://purl.uniprot.org/annotation/VSP_012825|||http://purl.uniprot.org/annotation/VSP_037943|||http://purl.uniprot.org/annotation/VSP_043170
http://togogenome.org/gene/9606:KCNH4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UQ05                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Site|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||INTRAMEM|||Motif|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical; Name=Segment S1|||Helical; Name=Segment S2|||Helical; Name=Segment S3|||Helical; Name=Segment S5|||Helical; Name=Segment S6|||Helical; Voltage-sensor; Name=Segment S4|||In a colorectal cancer sample; somatic mutation.|||N-linked (GlcNAc...) asparagine|||PAC|||PAS|||Polar residues|||Pore-forming; Name=Segment H5|||Potassium voltage-gated channel subfamily H member 4|||Pro residues|||Selectivity filter                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054008|||http://purl.uniprot.org/annotation/VAR_035771
http://togogenome.org/gene/9606:SLC7A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q53EM9|||http://purl.uniprot.org/uniprot/Q9UHI5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolishes leucine and tryptophan transport activities.|||Basic and acidic residues|||Cytoplasmic|||Disordered|||Does not affect protein expression, plasma membrane localization, or L-alanine uptake.|||Extracellular|||Found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity.|||Found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity.|||Found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity.|||Found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization.|||Helical|||Helical; Name=1|||Helical; Name=10|||Helical; Name=11|||Helical; Name=12|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Helical; Name=8|||Helical; Name=9|||Important for substrate specificity|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interchain (with C-210 in SLC3A2)|||Large neutral amino acids transporter small subunit 2|||Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.|||Phosphoserine|||Polar residues|||Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.|||Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.|||Strongly reduces L-leucine uptake activity.|||Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.|||The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000054273|||http://purl.uniprot.org/annotation/VAR_088247|||http://purl.uniprot.org/annotation/VAR_088248|||http://purl.uniprot.org/annotation/VAR_088249|||http://purl.uniprot.org/annotation/VAR_088250|||http://purl.uniprot.org/annotation/VSP_046945|||http://purl.uniprot.org/annotation/VSP_046946|||http://purl.uniprot.org/annotation/VSP_046947
http://togogenome.org/gene/9606:CDK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7W4|||http://purl.uniprot.org/uniprot/A0A0S2Z355|||http://purl.uniprot.org/uniprot/Q00535                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cyclin-dependent kinase 5|||Impaired p35/p25 (CDK5R1) binding.|||In isoform 2.|||N6-acetyllysine|||No phenotype.|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine; by ABL1, EPHA4 and FYN|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085784|||http://purl.uniprot.org/annotation/VAR_041977|||http://purl.uniprot.org/annotation/VSP_041948
http://togogenome.org/gene/9606:TLK2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HJZ9|||http://purl.uniprot.org/uniprot/A0A804HK10|||http://purl.uniprot.org/uniprot/B4DUC2|||http://purl.uniprot.org/uniprot/J3QLK5|||http://purl.uniprot.org/uniprot/Q86UE8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In MRD57.|||In MRD57; exhibits abnormal perinuclear localization instead of diffuse nuclear localization; impairs kinase activity; reduced phosphorylation of ASF1A.|||In MRD57; reduced kinase activity.|||In MRD57; reduced phosphorylation of ASF1A.|||In MRD57; severely reduced kinase activity.|||In MRD57; unknown pathological significance.|||In MRD57; unknown pathological significance; exhibits abnormal perinuclear localization instead of diffuse nuclear localization; mildly impairs kinase activity; reduced phosphorylation of ASF1A.|||In a gastric adenocarcinoma sample; somatic mutation.|||In isoform 2 and isoform 3.|||In isoform 3.|||Increase in autophosphorylation.|||Loss of kinase activity.|||Loss of kinase activity. No impact on interaction with ASF1A.|||Phosphoserine|||Phosphoserine; by CHEK1|||Polar residues|||Protein kinase|||Proton acceptor|||Reduced kinase activity.|||Reduced phosphorylation of ASF1A.|||Required for interaction with TLK1 and DYNLL1/LC8|||Serine/threonine-protein kinase tousled-like 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086754|||http://purl.uniprot.org/annotation/VAR_041216|||http://purl.uniprot.org/annotation/VAR_041217|||http://purl.uniprot.org/annotation/VAR_041218|||http://purl.uniprot.org/annotation/VAR_041219|||http://purl.uniprot.org/annotation/VAR_041220|||http://purl.uniprot.org/annotation/VAR_041221|||http://purl.uniprot.org/annotation/VAR_041222|||http://purl.uniprot.org/annotation/VAR_081017|||http://purl.uniprot.org/annotation/VAR_081018|||http://purl.uniprot.org/annotation/VAR_081019|||http://purl.uniprot.org/annotation/VAR_081020|||http://purl.uniprot.org/annotation/VAR_081021|||http://purl.uniprot.org/annotation/VAR_081022|||http://purl.uniprot.org/annotation/VAR_081023|||http://purl.uniprot.org/annotation/VAR_081024|||http://purl.uniprot.org/annotation/VAR_081025|||http://purl.uniprot.org/annotation/VAR_081026|||http://purl.uniprot.org/annotation/VAR_081027|||http://purl.uniprot.org/annotation/VAR_081028|||http://purl.uniprot.org/annotation/VAR_081029|||http://purl.uniprot.org/annotation/VAR_081030|||http://purl.uniprot.org/annotation/VAR_081031|||http://purl.uniprot.org/annotation/VAR_081032|||http://purl.uniprot.org/annotation/VAR_081033|||http://purl.uniprot.org/annotation/VAR_081034|||http://purl.uniprot.org/annotation/VAR_081035|||http://purl.uniprot.org/annotation/VAR_087040|||http://purl.uniprot.org/annotation/VAR_087041|||http://purl.uniprot.org/annotation/VAR_087042|||http://purl.uniprot.org/annotation/VSP_050572|||http://purl.uniprot.org/annotation/VSP_050573
http://togogenome.org/gene/9606:HPSE2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q2M1H9|||http://purl.uniprot.org/uniprot/Q8WWQ2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||In isoform 4.|||Inactive heparanase-2|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000068140|||http://purl.uniprot.org/annotation/PRO_5004212376|||http://purl.uniprot.org/annotation/VAR_023601|||http://purl.uniprot.org/annotation/VAR_030472|||http://purl.uniprot.org/annotation/VSP_015850|||http://purl.uniprot.org/annotation/VSP_015851|||http://purl.uniprot.org/annotation/VSP_015852|||http://purl.uniprot.org/annotation/VSP_015853
http://togogenome.org/gene/9606:GFRA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9GZZ7                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Modification|||Molecule Processing|||Natural Variation|||Propeptide|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Lipid Binding|||Propeptide|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Disordered|||GDNF family receptor alpha-4|||GPI-anchor amidated glycine|||In isoform GFRalpha4a.|||In isoform GFRalpha4c.|||N-linked (GlcNAc...) asparagine|||Removed in mature form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000010793|||http://purl.uniprot.org/annotation/PRO_0000010794|||http://purl.uniprot.org/annotation/VSP_007223|||http://purl.uniprot.org/annotation/VSP_007224|||http://purl.uniprot.org/annotation/VSP_007225
http://togogenome.org/gene/9606:GJA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35212                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Gap junction alpha-4 protein|||Helical|||In allele CX37*2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057814|||http://purl.uniprot.org/annotation/VAR_009159|||http://purl.uniprot.org/annotation/VAR_009160|||http://purl.uniprot.org/annotation/VAR_009161|||http://purl.uniprot.org/annotation/VAR_009162
http://togogenome.org/gene/9606:KAT6A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A5PKX7|||http://purl.uniprot.org/uniprot/A5PLL3|||http://purl.uniprot.org/uniprot/Q92794                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abrogates HAT activity.|||Acidic residues|||Basic and acidic residues|||Basic residues|||Breakpoint for translocation to form KAT6A-ASXL2|||Breakpoint for translocation to form KAT6A-CREBBP|||Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA2|||C2HC MYST-type|||Catalytic|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||H15|||Histone acetyltransferase KAT6A|||Interaction with PML|||Interaction with RUNX1-1|||Interaction with RUNX1-2|||MYST-type HAT|||Mediates interaction with BRPF1, required for histone H3 acetyltransferase activity|||N6-acetyllysine|||N6-acetyllysine; by autocatalysis|||PHD-type|||PHD-type 1|||PHD-type 2|||Phosphoserine|||Phosphothreonine; by PKB/AKT1|||Phosphotyrosine|||Polar residues|||Pro residues|||Proton donor/acceptor|||Reduced affinity for DNA.|||Required for activation of RUNX1-1|||Required for activation of RUNX1-2|||Required for nuclear localization|||SAMD1-like winged helix (WH)|||Slightly reduced affinity for DNA.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051572|||http://purl.uniprot.org/annotation/VAR_047548
http://togogenome.org/gene/9606:FBXO41                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TF61                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||F-box|||F-box only protein 41|||Omega-N-methylarginine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000119940
http://togogenome.org/gene/9606:ESRRA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P11474|||http://purl.uniprot.org/uniprot/Q569H8                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  15% loss of phosphorylation but little transactivating activity. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in the presence of coactivator; when associated with A-19.|||50% loss of phosphorylation but represses transactivation activity in the absence of coactivator. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in response to coactivator; when associated with A-22.|||AF-2 domain|||Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-160.|||Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-162.|||Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-160 and R-162.|||Abolishes acetylation by PCAF/KAT2B; when associated with R-138, R-160 and R-162.|||Almost complete loss of interaction to L2 or to L3 of PPARGC1A.|||Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A.|||Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A.|||Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A.|||In isoform 2.|||Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A.|||Little effect on binding L3 of PPARGC1A.|||Loss of coactivation activity; when associated with A-413. Loss of increased response to coactivator activity; when associated with A-19 and A-413.|||Loss of coactivation activity; when associated with A-418. Loss of increased response to coactivator; when associated with A-19 and A-418.|||N6-acetyllysine; by PCAF/KAT2B|||NR C4-type|||NR LBD|||No effect on binding L3 of PPARGC1A.|||Nuclear receptor|||Phosphoserine|||Represses transactivation activity in response to coactivator as for wild type; when associated with D-19.|||Represses transactivation activity in response to coactivator as for wild type; when associated with D-22.|||Repressor domain|||Required for DNA-dependent dimerization|||Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403.|||Steroid hormone receptor ERR1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000053660|||http://purl.uniprot.org/annotation/VSP_035756
http://togogenome.org/gene/9606:PKNOX1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DGV5|||http://purl.uniprot.org/uniprot/E7EPN6|||http://purl.uniprot.org/uniprot/P55347|||http://purl.uniprot.org/uniprot/Q6PKH2|||http://purl.uniprot.org/uniprot/Q96I87                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Turn                                                                                  ^@                                                                                  Disordered|||Homeobox|||Homeobox protein PKNOX1|||Homeobox; TALE-type|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||MEIS N-terminal|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000049248|||http://purl.uniprot.org/annotation/VAR_036440|||http://purl.uniprot.org/annotation/VAR_049588|||http://purl.uniprot.org/annotation/VAR_049589|||http://purl.uniprot.org/annotation/VSP_017260
http://togogenome.org/gene/9606:A1CF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4E1E3|||http://purl.uniprot.org/uniprot/F8W9F8|||http://purl.uniprot.org/uniprot/Q9NQ94                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  APOBEC1 complementation factor|||Greatly reduced RNA binding.|||In isoform 2, isoform 3 and isoform 4.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Phosphothreonine|||RRM|||RRM 1|||RRM 2|||RRM 3|||Required for nuclear localization|||Slightly reduced RNA binding.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000081482|||http://purl.uniprot.org/annotation/VAR_052201|||http://purl.uniprot.org/annotation/VAR_059821|||http://purl.uniprot.org/annotation/VSP_051925|||http://purl.uniprot.org/annotation/VSP_051926|||http://purl.uniprot.org/annotation/VSP_051927|||http://purl.uniprot.org/annotation/VSP_051928|||http://purl.uniprot.org/annotation/VSP_051929
http://togogenome.org/gene/9606:RPL38                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P63173                                                                                  ^@                                                                                  Chain|||Crosslink|||Modification|||Modified Residue|||Molecule Processing                                                                                  ^@                                                                                  Chain|||Crosslink|||Modified Residue                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Large ribosomal subunit protein eL38|||N6-acetyllysine|||N6-acetyllysine; alternate                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215434
http://togogenome.org/gene/9606:OR51A7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NH64                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 51A7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150744|||http://purl.uniprot.org/annotation/VAR_024140|||http://purl.uniprot.org/annotation/VAR_034315|||http://purl.uniprot.org/annotation/VAR_034316
http://togogenome.org/gene/9606:WDR86                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7X3|||http://purl.uniprot.org/uniprot/A0A0C4DGX6|||http://purl.uniprot.org/uniprot/Q86TI4                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 1.|||In isoform 2.|||In isoform 4.|||WD|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5|||WD 6|||WD 7|||WD 8|||WD repeat-containing protein 86                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320674|||http://purl.uniprot.org/annotation/VAR_063633|||http://purl.uniprot.org/annotation/VSP_031725|||http://purl.uniprot.org/annotation/VSP_031726|||http://purl.uniprot.org/annotation/VSP_039818|||http://purl.uniprot.org/annotation/VSP_054908
http://togogenome.org/gene/9606:KIF18B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6NWY8|||http://purl.uniprot.org/uniprot/Q86Y91                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Acidic residues|||Disordered|||In isoform 2.|||KIF2C-binding|||Kinesin motor|||Kinesin-like protein KIF18B|||MAPRE1-binding|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000318969|||http://purl.uniprot.org/annotation/VAR_038925|||http://purl.uniprot.org/annotation/VSP_060111|||http://purl.uniprot.org/annotation/VSP_060112|||http://purl.uniprot.org/annotation/VSP_060113
http://togogenome.org/gene/9606:APOF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13790                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modified Residue|||Propeptide|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Apolipoprotein F|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) threonine|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000002051|||http://purl.uniprot.org/annotation/PRO_0000002052|||http://purl.uniprot.org/annotation/VAR_055520
http://togogenome.org/gene/9606:SLC17A3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00476                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Found in a patient with gout; does not affect isoform 2 localization at the cell membrane; results in reduced urate efflux.|||Found in a patient with hyperuricemia; decreased expression of isoform 2 at the cell membrane; results in highly reduced urate efflux.|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Polar residues|||Sodium-dependent phosphate transport protein 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000351138|||http://purl.uniprot.org/annotation/VAR_024533|||http://purl.uniprot.org/annotation/VAR_034700|||http://purl.uniprot.org/annotation/VAR_046633|||http://purl.uniprot.org/annotation/VAR_068680|||http://purl.uniprot.org/annotation/VAR_068681|||http://purl.uniprot.org/annotation/VSP_042888
http://togogenome.org/gene/9606:ZNF778                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSW5|||http://purl.uniprot.org/uniprot/Q96MU6                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 14|||C2H2-type 15|||C2H2-type 16|||C2H2-type 17; degenerate|||C2H2-type 18|||C2H2-type 1; degenerate|||C2H2-type 2; degenerate|||C2H2-type 3|||C2H2-type 4; degenerate|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||In isoform 2.|||KRAB|||Zinc finger protein 778                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000263109|||http://purl.uniprot.org/annotation/VAR_061966|||http://purl.uniprot.org/annotation/VSP_040338|||http://purl.uniprot.org/annotation/VSP_040339
http://togogenome.org/gene/9606:GC                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P02774                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Albumin 1|||Albumin 2|||Albumin 3|||In allele GC*1F, allele GC*2 and allele GC*1S.|||In allele GC*1S.|||In allele GC*2, allele GC*2A9.|||In allele GC*2A9; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3.|||Vitamin D-binding protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000001102|||http://purl.uniprot.org/annotation/VAR_000548|||http://purl.uniprot.org/annotation/VAR_000549|||http://purl.uniprot.org/annotation/VAR_014120|||http://purl.uniprot.org/annotation/VAR_014121|||http://purl.uniprot.org/annotation/VSP_038427|||http://purl.uniprot.org/annotation/VSP_044523
http://togogenome.org/gene/9606:CNPY3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BT09                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In DEE60; unknown pathological significance.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Protein canopy homolog 3|||Saposin B-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000313780|||http://purl.uniprot.org/annotation/VAR_037731|||http://purl.uniprot.org/annotation/VAR_037732|||http://purl.uniprot.org/annotation/VAR_080491|||http://purl.uniprot.org/annotation/VSP_030132|||http://purl.uniprot.org/annotation/VSP_030133
http://togogenome.org/gene/9606:NEK5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P3R8                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||Protein kinase|||Proton acceptor|||Serine/threonine-protein kinase Nek5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000259765|||http://purl.uniprot.org/annotation/VAR_040922|||http://purl.uniprot.org/annotation/VAR_040923|||http://purl.uniprot.org/annotation/VAR_051652
http://togogenome.org/gene/9606:IL1F10                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WWZ1                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Interleukin-1 family member 10                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000153650|||http://purl.uniprot.org/annotation/VAR_014262|||http://purl.uniprot.org/annotation/VAR_014263|||http://purl.uniprot.org/annotation/VSP_002658
http://togogenome.org/gene/9606:PKD2L2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZM6                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||N-linked (GlcNAc...) asparagine|||Polycystin-2-like protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164361|||http://purl.uniprot.org/annotation/VAR_047542|||http://purl.uniprot.org/annotation/VAR_047543|||http://purl.uniprot.org/annotation/VSP_004732|||http://purl.uniprot.org/annotation/VSP_004733|||http://purl.uniprot.org/annotation/VSP_004734|||http://purl.uniprot.org/annotation/VSP_004735|||http://purl.uniprot.org/annotation/VSP_004736|||http://purl.uniprot.org/annotation/VSP_004737|||http://purl.uniprot.org/annotation/VSP_035775|||http://purl.uniprot.org/annotation/VSP_045581|||http://purl.uniprot.org/annotation/VSP_045582
http://togogenome.org/gene/9606:MED6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WYL7|||http://purl.uniprot.org/uniprot/O75586                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||In isoform 3.|||Mediator of RNA polymerase II transcription subunit 6|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096388|||http://purl.uniprot.org/annotation/VSP_054589|||http://purl.uniprot.org/annotation/VSP_054590
http://togogenome.org/gene/9606:TCAF2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A6NFQ2                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Peptidase M60|||TRPM8 channel-associated factor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000320187|||http://purl.uniprot.org/annotation/VSP_031635|||http://purl.uniprot.org/annotation/VSP_042050|||http://purl.uniprot.org/annotation/VSP_042051
http://togogenome.org/gene/9606:SPIN2A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99865                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Conflict|||Site                                                                                  ^@                                                                                  Disordered|||Histone H3K4me3 and H3R8me2a binding|||Polar residues|||Spindlin-2A|||Tudor-like domain 1|||Tudor-like domain 2|||Tudor-like domain 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000181371
http://togogenome.org/gene/9606:SLC5A8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N695                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Helix|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Loss of interaction with PDZK1.|||N-linked (GlcNAc...) asparagine|||PDZ-binding|||Polar residues|||Sodium-coupled monocarboxylate transporter 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000334499|||http://purl.uniprot.org/annotation/VAR_057336|||http://purl.uniprot.org/annotation/VAR_057337
http://togogenome.org/gene/9606:CENPT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KPB2|||http://purl.uniprot.org/uniprot/Q96BT3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  CENP-T/Histone H4 histone fold|||Centromere kinetochore component CENP-T N-terminal|||Centromere protein T|||Disordered|||Flexible stalk domain|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphothreonine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249514|||http://purl.uniprot.org/annotation/VAR_027421|||http://purl.uniprot.org/annotation/VSP_020455|||http://purl.uniprot.org/annotation/VSP_020456|||http://purl.uniprot.org/annotation/VSP_020457|||http://purl.uniprot.org/annotation/VSP_020458
http://togogenome.org/gene/9606:TNFSF12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43508|||http://purl.uniprot.org/uniprot/Q4ACW9                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cleavage|||Cytoplasmic|||Disordered|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform TWE-PRIL.|||N-linked (GlcNAc...) asparagine|||TNF family profile|||Tumor necrosis factor ligand superfamily member 12, membrane form|||Tumor necrosis factor ligand superfamily member 12, secreted form                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000034520|||http://purl.uniprot.org/annotation/PRO_0000034521|||http://purl.uniprot.org/annotation/VSP_045245
http://togogenome.org/gene/9606:MCTS1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9ULC4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||Malignant T-cell-amplified sequence 1|||No phosphorylation by CDK1; No cell growth alteration.|||No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction.|||PUA|||Phosphoserine; by CDK1|||Phosphothreonine; by MAPK1 and MAPK3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000344786|||http://purl.uniprot.org/annotation/VAR_045632|||http://purl.uniprot.org/annotation/VSP_034856|||http://purl.uniprot.org/annotation/VSP_041352
http://togogenome.org/gene/9606:RPL9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P32969|||http://purl.uniprot.org/uniprot/Q53Z07                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Large ribosomal subunit protein uL6|||Large ribosomal subunit protein uL6 alpha-beta|||N6-acetyllysine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131097
http://togogenome.org/gene/9606:ADCYAP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B7Z222|||http://purl.uniprot.org/uniprot/P18509                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Peptide|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Peptide|||Propeptide|||Region|||Sequence Variant|||Signal Peptide                                                                                  ^@                                                                                  Disordered|||Glucagon / GIP / secretin / VIP family|||Important for receptor binding|||Leucine amide|||Lysine amide|||PACAP-related peptide|||Pituitary adenylate cyclase-activating polypeptide 27|||Pituitary adenylate cyclase-activating polypeptide 38|||Polar residues|||Strongly reduced affinity for ADCYAP1R1.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000011486|||http://purl.uniprot.org/annotation/PRO_0000011487|||http://purl.uniprot.org/annotation/PRO_0000011488|||http://purl.uniprot.org/annotation/PRO_0000011489|||http://purl.uniprot.org/annotation/PRO_0000011490|||http://purl.uniprot.org/annotation/VAR_014597
http://togogenome.org/gene/9606:OR51I1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GWE7|||http://purl.uniprot.org/uniprot/Q9H343                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Olfactory receptor 51I1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150757|||http://purl.uniprot.org/annotation/VAR_024142|||http://purl.uniprot.org/annotation/VAR_034320|||http://purl.uniprot.org/annotation/VAR_053328
http://togogenome.org/gene/9606:CALM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DJ51|||http://purl.uniprot.org/uniprot/P0DP23|||http://purl.uniprot.org/uniprot/P0DP24|||http://purl.uniprot.org/uniprot/P0DP25                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Calmodulin-1|||Calmodulin-2|||Calmodulin-3|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate|||In CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In CPVT6; decreased calcium-binding affinity; not changed binding to RYR2; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed action potential duration.|||In LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release.|||In LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential.|||In LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2.|||In LQT15.|||In LQT15; reduction in calcium affinity.|||In LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.|||In LQT16.|||In LQT16; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding.|||N-acetylalanine|||N6,N6,N6-trimethyllysine; alternate|||N6-acetyllysine|||N6-acetyllysine; alternate|||N6-methyllysine; alternate|||Necessary and sufficient for interaction with PCP4|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by CaMK4|||Phosphotyrosine|||Removed ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000439932|||http://purl.uniprot.org/annotation/PRO_0000439933|||http://purl.uniprot.org/annotation/PRO_0000439934|||http://purl.uniprot.org/annotation/VAR_069222|||http://purl.uniprot.org/annotation/VAR_073275|||http://purl.uniprot.org/annotation/VAR_073276|||http://purl.uniprot.org/annotation/VAR_073277|||http://purl.uniprot.org/annotation/VAR_073279|||http://purl.uniprot.org/annotation/VAR_073280|||http://purl.uniprot.org/annotation/VAR_073281|||http://purl.uniprot.org/annotation/VAR_073282|||http://purl.uniprot.org/annotation/VAR_078261|||http://purl.uniprot.org/annotation/VAR_078262|||http://purl.uniprot.org/annotation/VAR_078263|||http://purl.uniprot.org/annotation/VAR_078541|||http://purl.uniprot.org/annotation/VAR_078542|||http://purl.uniprot.org/annotation/VAR_078543|||http://purl.uniprot.org/annotation/VAR_078544|||http://purl.uniprot.org/annotation/VAR_083814|||http://purl.uniprot.org/annotation/VAR_083815|||http://purl.uniprot.org/annotation/VAR_083816
http://togogenome.org/gene/9606:PTGDR2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y5Y4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Glycosylation Site|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  45% increase in internalization of PTGDR2.|||45% increases internalization of PTGDR2.|||Cytoplasmic|||Decreases in PKC-induced internalization of PTGDR2.|||Disordered|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||Involved in the recycling of CRTH2|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Polar residues|||Prostaglandin D2 receptor 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069572|||http://purl.uniprot.org/annotation/VAR_063131
http://togogenome.org/gene/9606:RPL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A2RUM7|||http://purl.uniprot.org/uniprot/P46777                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate|||In DBA6.|||Large ribosomal subunit protein uL18|||Large ribosomal subunit protein uL18 C-terminal eukaryotes|||N-acetylglycine|||N6-acetyllysine|||N6-acetyllysine; alternate|||Phosphoserine|||Phosphothreonine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000131431|||http://purl.uniprot.org/annotation/VAR_052009|||http://purl.uniprot.org/annotation/VAR_055450|||http://purl.uniprot.org/annotation/VAR_055451
http://togogenome.org/gene/9606:TRAPPC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y296                                                                                  ^@                                                                                  Chain|||Helix|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Helix|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  In isoform 2.|||Trafficking protein particle complex subunit 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000211569|||http://purl.uniprot.org/annotation/VAR_052397|||http://purl.uniprot.org/annotation/VSP_056348
http://togogenome.org/gene/9606:USP47                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96K76                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Active Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N6-acetyllysine|||Nucleophile|||Phosphoserine|||Phosphothreonine|||Polar residues|||Proton acceptor|||USP|||Ubiquitin carboxyl-terminal hydrolase 47                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080676|||http://purl.uniprot.org/annotation/VAR_022787|||http://purl.uniprot.org/annotation/VSP_014414|||http://purl.uniprot.org/annotation/VSP_014415|||http://purl.uniprot.org/annotation/VSP_055650
http://togogenome.org/gene/9606:CAPN12                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6ZSI9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Domain Extent|||Region|||Sequence Variant                                                                                  ^@                                                                                  Calpain catalytic|||Calpain-12|||Disordered|||Domain III|||Domain IV|||EF-hand                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000207730|||http://purl.uniprot.org/annotation/VAR_051516
http://togogenome.org/gene/9606:CHL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087X0M8|||http://purl.uniprot.org/uniprot/O00533                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cleavage; by ADAM8|||Cytoplasmic|||DGEA|||Disordered|||Extracellular|||FIG[AQ]Y|||Fibronectin type-III|||Fibronectin type-III 1|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Helical|||Ig-like|||Ig-like C2-type 1|||Ig-like C2-type 2|||Ig-like C2-type 3|||Ig-like C2-type 4|||Ig-like C2-type 5|||Ig-like C2-type 6|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Neural cell adhesion molecule L1-like protein|||Phosphoserine|||Polar residues|||Processed neural cell adhesion molecule L1-like protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000247896|||http://purl.uniprot.org/annotation/PRO_0000314777|||http://purl.uniprot.org/annotation/PRO_5001832147|||http://purl.uniprot.org/annotation/VAR_027167|||http://purl.uniprot.org/annotation/VAR_027168|||http://purl.uniprot.org/annotation/VAR_027169|||http://purl.uniprot.org/annotation/VAR_035505|||http://purl.uniprot.org/annotation/VSP_020082
http://togogenome.org/gene/9606:MYL12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QRS3|||http://purl.uniprot.org/uniprot/O14950|||http://purl.uniprot.org/uniprot/P19105                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||Myosin regulatory light chain 12A|||Myosin regulatory light chain 12B|||Phosphoserine; by MLCK|||Phosphoserine; by MLCK and ZIPK/DAPK3|||Phosphothreonine; by MLCK|||Phosphothreonine; by MLCK and ZIPK/DAPK3|||Shows a decrease in the number of actin filament bundles.|||Shows a larger number of actin filament bundles.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000198733|||http://purl.uniprot.org/annotation/PRO_0000349364|||http://purl.uniprot.org/annotation/VAR_046371
http://togogenome.org/gene/9606:OR2L3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NG85                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 2L3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150487|||http://purl.uniprot.org/annotation/VAR_053146|||http://purl.uniprot.org/annotation/VAR_062021|||http://purl.uniprot.org/annotation/VAR_062022|||http://purl.uniprot.org/annotation/VAR_062023
http://togogenome.org/gene/9606:IK                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q13123|||http://purl.uniprot.org/uniprot/Q95HA6|||http://purl.uniprot.org/uniprot/Q9UK43                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  1|||10|||11|||12|||13|||14|||15|||16|||17|||17 X 2 AA tandem repeats of R-[ED]|||2|||3|||4|||5|||6|||7|||8|||9|||Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Protein RED C-terminal|||Protein Red|||RED-like N-terminal                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097235
http://togogenome.org/gene/9606:VWC2L                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RUY7|||http://purl.uniprot.org/uniprot/B7ZW27                                                                                  ^@                                                                                  Chain|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Domain Extent|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||VWFC 1|||VWFC 2|||von Willebrand factor C domain-containing protein 2-like                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000348060|||http://purl.uniprot.org/annotation/PRO_5014300232|||http://purl.uniprot.org/annotation/VSP_035088|||http://purl.uniprot.org/annotation/VSP_035089
http://togogenome.org/gene/9606:IFNA6                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A7R8C308|||http://purl.uniprot.org/uniprot/P05013                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Signal Peptide                                                                                  ^@                                                                                  Interferon alpha-6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016363|||http://purl.uniprot.org/annotation/PRO_5031034512
http://togogenome.org/gene/9606:SLITRK3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O94933                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||LRR 1|||LRR 10|||LRR 11|||LRR 12|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRCT 1|||LRRCT 2|||LRRNT|||N-linked (GlcNAc...) asparagine|||Pro residues|||SLIT and NTRK-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032677|||http://purl.uniprot.org/annotation/VAR_027757
http://togogenome.org/gene/9606:POLR3B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q7Z3R8|||http://purl.uniprot.org/uniprot/Q9NW08                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  C4-type|||DNA-directed RNA polymerase III subunit RPC2|||DNA-directed RNA polymerase subunit 2 hybrid-binding|||In CMT1I; affects RNA polymerase III assembly; no effect on nuclear localization.|||In HLD8.|||In isoform 2.|||RNA polymerase Rpb2|||RNA polymerase beta subunit protrusion                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048092|||http://purl.uniprot.org/annotation/VAR_057255|||http://purl.uniprot.org/annotation/VAR_067005|||http://purl.uniprot.org/annotation/VAR_067006|||http://purl.uniprot.org/annotation/VAR_067007|||http://purl.uniprot.org/annotation/VAR_067008|||http://purl.uniprot.org/annotation/VAR_067009|||http://purl.uniprot.org/annotation/VAR_072344|||http://purl.uniprot.org/annotation/VAR_072345|||http://purl.uniprot.org/annotation/VAR_072346|||http://purl.uniprot.org/annotation/VAR_072347|||http://purl.uniprot.org/annotation/VAR_086912|||http://purl.uniprot.org/annotation/VAR_086913|||http://purl.uniprot.org/annotation/VAR_086914|||http://purl.uniprot.org/annotation/VAR_086915|||http://purl.uniprot.org/annotation/VAR_086916|||http://purl.uniprot.org/annotation/VAR_086917|||http://purl.uniprot.org/annotation/VSP_045286
http://togogenome.org/gene/9606:MEGF9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H1U4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Region|||Signal Peptide|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||Laminin EGF-like 1|||Laminin EGF-like 2|||Laminin EGF-like 3|||Laminin EGF-like 4|||Laminin EGF-like 5|||Multiple epidermal growth factor-like domains protein 9|||N-linked (GlcNAc...) asparagine|||Polar residues|||Pro residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000007526
http://togogenome.org/gene/9606:ADAT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/D6W601|||http://purl.uniprot.org/uniprot/Q96EY9                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  CMP/dCMP-type deaminase|||Disordered|||In NEDBGF.|||In a breast cancer sample; somatic mutation.|||N-acetylmethionine|||Probable inactive tRNA-specific adenosine deaminase-like protein 3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287658|||http://purl.uniprot.org/annotation/VAR_035804|||http://purl.uniprot.org/annotation/VAR_069778
http://togogenome.org/gene/9606:ARAF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A024R178|||http://purl.uniprot.org/uniprot/P10398|||http://purl.uniprot.org/uniprot/Q96II5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In a colorectal adenocarcinoma sample; somatic mutation.|||In isoform 2.|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein kinase|||Proton acceptor|||RBD|||Serine/threonine-protein kinase A-Raf                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000085622|||http://purl.uniprot.org/annotation/VAR_040375|||http://purl.uniprot.org/annotation/VAR_040376|||http://purl.uniprot.org/annotation/VAR_040377|||http://purl.uniprot.org/annotation/VSP_045609|||http://purl.uniprot.org/annotation/VSP_045610
http://togogenome.org/gene/9606:FIRRM                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSG2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Decreased binding to PLK1.|||Decreased binding to PPP1CC. Does not rescue the mitotic defects seen in FIRRM-depleted cells.|||Does not affect binding to PPP1CC. Rescues the mitotic defects seen in FIRRM-depleted cells.|||FIGNL1-interacting regulator of recombination and mitosis|||In isoform 2.|||In isoform 3.|||Increased binding to PLK1.|||N6-acetyllysine|||Phosphoserine; by PLK1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000279461|||http://purl.uniprot.org/annotation/VAR_030906|||http://purl.uniprot.org/annotation/VSP_023444|||http://purl.uniprot.org/annotation/VSP_023445
http://togogenome.org/gene/9606:SNRPD2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62316                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Sm|||Small nuclear ribonucleoprotein Sm D2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000122207|||http://purl.uniprot.org/annotation/VSP_045371
http://togogenome.org/gene/9606:OR7C2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O60412                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Sequence Conflict|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 7C2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150647|||http://purl.uniprot.org/annotation/VAR_027808|||http://purl.uniprot.org/annotation/VAR_053234
http://togogenome.org/gene/9606:CAMK1D                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5SQQ7|||http://purl.uniprot.org/uniprot/Q8IU85                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Autoinhibitory domain|||Calcium/calmodulin-dependent protein kinase type 1D|||Calmodulin-binding|||Catalytically inactive form.|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||Loss of ionomycin-induced activation.|||Nuclear export signal|||Phosphoserine|||Phosphothreonine; by CaMKK1 and CaMKK2|||Protein kinase|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000086082|||http://purl.uniprot.org/annotation/VAR_040599|||http://purl.uniprot.org/annotation/VSP_012135
http://togogenome.org/gene/9606:SYNRG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UMZ2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||DFXDF motif 1|||DFXDF motif 2|||DFXDF motif 3|||Disordered|||EH|||Found in a consanguineous family with intellectual disability; unknown pathological significance.|||In isoform 2, isoform 3, isoform 5, isoform 6, isoform 7 and isoform 8.|||In isoform 3, isoform 4 and isoform 8.|||In isoform 5 and isoform 8.|||In isoform 5.|||In isoform 6.|||In isoform 7.|||Interaction with AP1G1|||Interaction with AP1G1, AP1G2 and GGA1|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Polar residues|||Synergin gamma                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000072387|||http://purl.uniprot.org/annotation/VAR_051395|||http://purl.uniprot.org/annotation/VAR_051396|||http://purl.uniprot.org/annotation/VAR_080768|||http://purl.uniprot.org/annotation/VSP_023015|||http://purl.uniprot.org/annotation/VSP_023016|||http://purl.uniprot.org/annotation/VSP_043281|||http://purl.uniprot.org/annotation/VSP_043282|||http://purl.uniprot.org/annotation/VSP_054732|||http://purl.uniprot.org/annotation/VSP_054733
http://togogenome.org/gene/9606:RALGAPB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q86X10                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Disordered|||In isoform 2 and isoform 3.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Phosphoserine|||Phosphothreonine|||Polar residues|||Ral GTPase-activating protein subunit beta|||Rap-GAP                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000056756|||http://purl.uniprot.org/annotation/VSP_009693|||http://purl.uniprot.org/annotation/VSP_009694|||http://purl.uniprot.org/annotation/VSP_009695|||http://purl.uniprot.org/annotation/VSP_009696
http://togogenome.org/gene/9606:ASPN                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6P528|||http://purl.uniprot.org/uniprot/Q9BXN1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Propeptide|||Region|||Repeat|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Acidic residues|||Asporin|||Disordered|||Interaction with TGFB1|||LRR 1|||LRR 10|||LRR 11|||LRR 2|||LRR 3|||LRR 4|||LRR 5|||LRR 6|||LRR 7|||LRR 8|||LRR 9|||LRRNT|||N-linked (GlcNAc...) asparagine|||O-linked (GalNAc...) serine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000032727|||http://purl.uniprot.org/annotation/PRO_0000032728|||http://purl.uniprot.org/annotation/PRO_5012339073
http://togogenome.org/gene/9606:KLC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NSK0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Initiator Methionine|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Kinesin light chain 4|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||TPR 1|||TPR 2|||TPR 3|||TPR 4|||TPR 5|||TPR 6|||TPR 7                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215097|||http://purl.uniprot.org/annotation/VAR_049708|||http://purl.uniprot.org/annotation/VSP_037875|||http://purl.uniprot.org/annotation/VSP_037876|||http://purl.uniprot.org/annotation/VSP_038083|||http://purl.uniprot.org/annotation/VSP_043324|||http://purl.uniprot.org/annotation/VSP_043325|||http://purl.uniprot.org/annotation/VSP_057231
http://togogenome.org/gene/9606:ANKRD45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TZF3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Repeat|||Splice Variant                                                                                  ^@                                                                                  ANK 1|||ANK 2|||Acidic residues|||Ankyrin repeat domain-containing protein 45|||Disordered|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000244574|||http://purl.uniprot.org/annotation/VSP_059723
http://togogenome.org/gene/9606:MROH7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B4DXB3|||http://purl.uniprot.org/uniprot/B7Z7S6|||http://purl.uniprot.org/uniprot/Q68CQ1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Glycosylation Site|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||HEAT 1|||HEAT 2|||HEAT 3|||HEAT 4|||Helical|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||Maestro heat-like repeat-containing protein family member 7|||N-linked (GlcNAc...) asparagine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286866|||http://purl.uniprot.org/annotation/VAR_032218|||http://purl.uniprot.org/annotation/VAR_032219|||http://purl.uniprot.org/annotation/VAR_032220|||http://purl.uniprot.org/annotation/VAR_032221|||http://purl.uniprot.org/annotation/VAR_032222|||http://purl.uniprot.org/annotation/VAR_032223|||http://purl.uniprot.org/annotation/VAR_035495|||http://purl.uniprot.org/annotation/VAR_055042|||http://purl.uniprot.org/annotation/VAR_055043|||http://purl.uniprot.org/annotation/VAR_055044|||http://purl.uniprot.org/annotation/VSP_037024|||http://purl.uniprot.org/annotation/VSP_037025|||http://purl.uniprot.org/annotation/VSP_037026|||http://purl.uniprot.org/annotation/VSP_037027|||http://purl.uniprot.org/annotation/VSP_037028|||http://purl.uniprot.org/annotation/VSP_037029|||http://purl.uniprot.org/annotation/VSP_037030|||http://purl.uniprot.org/annotation/VSP_037031|||http://purl.uniprot.org/annotation/VSP_037032|||http://purl.uniprot.org/annotation/VSP_037033
http://togogenome.org/gene/9606:VPS37B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H9H4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region                                                                                  ^@                                                                                  Disordered|||Interaction with IST1|||Omega-N-methylarginine|||Pro residues|||VPS37 C-terminal|||Vacuolar protein sorting-associated protein 37B                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287200
http://togogenome.org/gene/9606:RARRES2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A090N7U9|||http://purl.uniprot.org/uniprot/Q99969                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Modification|||Molecule Processing|||Propeptide|||Secondary Structure|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Propeptide|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Retinoic acid receptor responder protein 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022529|||http://purl.uniprot.org/annotation/PRO_0000424870|||http://purl.uniprot.org/annotation/PRO_5001860373
http://togogenome.org/gene/9606:NPIPB4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A804HK81                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Compositionally Biased Region|||Region                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Polar residues                                                                                  ^@                                                                                  
http://togogenome.org/gene/9606:LMOD1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29536                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||5 X 4 AA approximate tandem repeats|||6|||7|||8|||8 X approximate tandem repeats|||Basic and acidic residues|||Disordered|||In MMIHS3; markedly reduced LMOD1 protein levels in homozygous patient cells.|||In isoform 2.|||Leiomodin-1|||Phosphoserine|||Pro residues|||WH2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000084453|||http://purl.uniprot.org/annotation/VAR_021839|||http://purl.uniprot.org/annotation/VAR_085835|||http://purl.uniprot.org/annotation/VSP_035745
http://togogenome.org/gene/9606:PPM1G                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O15355|||http://purl.uniprot.org/uniprot/Q6IAU5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Region                                                                                  ^@                                                                                  Acidic residues|||Basic and acidic residues|||Disordered|||N-myristoyl glycine|||N6-acetyllysine|||Omega-N-methylarginine|||PPM-type phosphatase|||Phosphoserine|||Phosphothreonine|||Polar residues|||Protein phosphatase 1G|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000057750
http://togogenome.org/gene/9606:COL12A1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99715                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modified Residue|||Motif|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  4-hydroxyproline|||Cell attachment site|||Collagen alpha-1(XII) chain|||Collagen-like 1|||Collagen-like 2|||Collagen-like 3|||Collagen-like 4|||Disordered|||Fibronectin type-III 1|||Fibronectin type-III 10|||Fibronectin type-III 11|||Fibronectin type-III 12|||Fibronectin type-III 13|||Fibronectin type-III 14|||Fibronectin type-III 15|||Fibronectin type-III 16|||Fibronectin type-III 17|||Fibronectin type-III 18|||Fibronectin type-III 2|||Fibronectin type-III 3|||Fibronectin type-III 4|||Fibronectin type-III 5|||Fibronectin type-III 6|||Fibronectin type-III 7|||Fibronectin type-III 8|||Fibronectin type-III 9|||In BTHLM2.|||In BTHLM2; unknown pathological significance.|||In isoform 2.|||In isoform 4.|||Laminin G-like|||N-linked (GlcNAc...) asparagine|||Nonhelical region (NC1)|||Nonhelical region (NC2)|||Nonhelical region (NC3)|||O-linked (Xyl...) (chondroitin sulfate) serine|||Polar residues|||Pro residues|||Triple-helical region (COL1) with 2 imperfections|||Triple-helical region (COL2) with 1 imperfection|||VWFA 1|||VWFA 2|||VWFA 3|||VWFA 4                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005783|||http://purl.uniprot.org/annotation/VAR_048768|||http://purl.uniprot.org/annotation/VAR_048769|||http://purl.uniprot.org/annotation/VAR_048770|||http://purl.uniprot.org/annotation/VAR_048771|||http://purl.uniprot.org/annotation/VAR_061111|||http://purl.uniprot.org/annotation/VAR_061112|||http://purl.uniprot.org/annotation/VAR_074546|||http://purl.uniprot.org/annotation/VAR_074547|||http://purl.uniprot.org/annotation/VAR_074548|||http://purl.uniprot.org/annotation/VAR_074549|||http://purl.uniprot.org/annotation/VSP_001149|||http://purl.uniprot.org/annotation/VSP_024942
http://togogenome.org/gene/9606:TRIP11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15643                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Initiator Methionine|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Abolishes interaction with RAB2A.|||Abolishes tethering of intra-Golgi vesicles.|||Amphipathic lipid-packing sensor required for tethering of intra-Golgi vesicles|||Basic and acidic residues|||Breakpoint for translocation to form TRIP11-PDGFRB|||Disordered|||GRIP|||In ACG1A and ODCD1.|||In ACG1A.|||In ACG1A; does not localize to cis-Golgi; results in disruption of Golgi cisternal stack architecture.|||In ODCD1.|||In ODCD1; due to a nucleotide substitution that causes in-frame exon 9 skipping or results in missense variant Y-410; patient cells contain both type of transcripts; the transcript lacking exon 9 is the most abundant.|||In ODCD1; due to a nucleotide substitution that causes missplicing of exon 18 or results in missense variant V-1806; patient cells contain both type of transcripts; the transcript with the missense variant is the most abundant.|||In ODCD1; due to a nucleotide substitution that causes protein truncation or in-frame exon 4 skipping.|||In ODCD1; in-frame exon 4 skipping; due to a nucleotide substitution that may also cause protein truncation.|||In isoform 2.|||Involved in RAB2A binding|||N-acetylserine|||Phosphoserine|||Phosphothreonine|||Removed|||Thyroid receptor-interacting protein 11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000190076|||http://purl.uniprot.org/annotation/VAR_054151|||http://purl.uniprot.org/annotation/VAR_055861|||http://purl.uniprot.org/annotation/VAR_055862|||http://purl.uniprot.org/annotation/VAR_055863|||http://purl.uniprot.org/annotation/VAR_055864|||http://purl.uniprot.org/annotation/VAR_055865|||http://purl.uniprot.org/annotation/VAR_055866|||http://purl.uniprot.org/annotation/VAR_055867|||http://purl.uniprot.org/annotation/VAR_055868|||http://purl.uniprot.org/annotation/VAR_055869|||http://purl.uniprot.org/annotation/VAR_060344|||http://purl.uniprot.org/annotation/VAR_060345|||http://purl.uniprot.org/annotation/VAR_060346|||http://purl.uniprot.org/annotation/VAR_079175|||http://purl.uniprot.org/annotation/VAR_082008|||http://purl.uniprot.org/annotation/VAR_082009|||http://purl.uniprot.org/annotation/VAR_082010|||http://purl.uniprot.org/annotation/VAR_082011|||http://purl.uniprot.org/annotation/VAR_082012|||http://purl.uniprot.org/annotation/VAR_082013|||http://purl.uniprot.org/annotation/VAR_082014|||http://purl.uniprot.org/annotation/VAR_082015|||http://purl.uniprot.org/annotation/VAR_082016|||http://purl.uniprot.org/annotation/VAR_082017|||http://purl.uniprot.org/annotation/VAR_082285|||http://purl.uniprot.org/annotation/VSP_060242
http://togogenome.org/gene/9606:ALOXE3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9BYJ1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Hydroperoxide isomerase ALOXE3|||In ARCI3.|||In ARCI3; complete loss of the enzyme activity.|||In ARCI3; no effect on enzyme activity.|||In isoform 2.|||Increases the O2-dependent dioxygenase activity.|||Lipoxygenase|||PLAT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220691|||http://purl.uniprot.org/annotation/VAR_015175|||http://purl.uniprot.org/annotation/VAR_015176|||http://purl.uniprot.org/annotation/VAR_069561|||http://purl.uniprot.org/annotation/VAR_069562|||http://purl.uniprot.org/annotation/VAR_069563|||http://purl.uniprot.org/annotation/VAR_069564|||http://purl.uniprot.org/annotation/VAR_069565|||http://purl.uniprot.org/annotation/VSP_043287
http://togogenome.org/gene/9606:SCARB1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8WTV0                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Lipid Binding|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Associated with higher plasma triglyceride concentration in subjects with hypercholesterolemia.|||Cytoplasmic|||Extracellular|||Helical|||In isoform 1, isoform 2 and isoform 4.|||In isoform 2.|||In isoform 4.|||In isoform 5.|||Mutation carriers have increased HDL cholesterol levels and a reduction in cholesterol efflux from macrophages.|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Rare variant; associated with high HDL-cholesterol levels and increased risk for coronary heart disease; results in highly reduced cholesterol uptake from HDL; markedly reduced localization at the cell surface.|||S-palmitoyl cysteine|||Scavenger receptor class B member 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000144160|||http://purl.uniprot.org/annotation/VAR_017098|||http://purl.uniprot.org/annotation/VAR_017099|||http://purl.uniprot.org/annotation/VAR_017100|||http://purl.uniprot.org/annotation/VAR_017101|||http://purl.uniprot.org/annotation/VAR_019507|||http://purl.uniprot.org/annotation/VAR_064909|||http://purl.uniprot.org/annotation/VAR_076314|||http://purl.uniprot.org/annotation/VSP_008553|||http://purl.uniprot.org/annotation/VSP_008554|||http://purl.uniprot.org/annotation/VSP_011037|||http://purl.uniprot.org/annotation/VSP_054083
http://togogenome.org/gene/9606:P2RX7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q99572                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Glycosylation Site|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  ADP-ribosylarginine|||Alters cell surface expression.|||Cytoplasmic|||Decreases cell surface expression; decreases phagocytosis activity.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||In a colorectal cancer sample; somatic mutation.|||In isoform B, isoform E and isoform G.|||In isoform C.|||In isoform D.|||In isoform E.|||In isoform F.|||In isoform G and isoform H.|||May influence susceptibility to multiple sclerosis in the presence of variant S-135 in P2RX4; decreases cell surface expression; decreases pore complex assembly; decreases phagocytosis activity.|||May influence susceptibility to multiple sclerosis in the presence of variant S-135 in P2RX4; no effect on cell surface expression; no effect on pore complex assembly.|||N-linked (GlcNAc...) asparagine|||P2X purinoceptor 7|||Phosphoserine|||Phosphotyrosine|||Results in a loss of function.|||Results in trafficking defect and around 50% loss of function.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000161560|||http://purl.uniprot.org/annotation/VAR_019648|||http://purl.uniprot.org/annotation/VAR_019649|||http://purl.uniprot.org/annotation/VAR_019650|||http://purl.uniprot.org/annotation/VAR_019651|||http://purl.uniprot.org/annotation/VAR_019652|||http://purl.uniprot.org/annotation/VAR_036444|||http://purl.uniprot.org/annotation/VAR_036445|||http://purl.uniprot.org/annotation/VAR_057665|||http://purl.uniprot.org/annotation/VAR_057666|||http://purl.uniprot.org/annotation/VAR_057667|||http://purl.uniprot.org/annotation/VAR_057668|||http://purl.uniprot.org/annotation/VAR_057669|||http://purl.uniprot.org/annotation/VAR_057670|||http://purl.uniprot.org/annotation/VAR_057671|||http://purl.uniprot.org/annotation/VAR_057672|||http://purl.uniprot.org/annotation/VAR_057673|||http://purl.uniprot.org/annotation/VAR_057674|||http://purl.uniprot.org/annotation/VAR_057675|||http://purl.uniprot.org/annotation/VAR_068011|||http://purl.uniprot.org/annotation/VAR_079880|||http://purl.uniprot.org/annotation/VAR_079881|||http://purl.uniprot.org/annotation/VAR_079882|||http://purl.uniprot.org/annotation/VAR_079883|||http://purl.uniprot.org/annotation/VAR_079884|||http://purl.uniprot.org/annotation/VAR_079885|||http://purl.uniprot.org/annotation/VAR_079886|||http://purl.uniprot.org/annotation/VAR_079887|||http://purl.uniprot.org/annotation/VAR_079888|||http://purl.uniprot.org/annotation/VSP_047776|||http://purl.uniprot.org/annotation/VSP_047777|||http://purl.uniprot.org/annotation/VSP_047778|||http://purl.uniprot.org/annotation/VSP_047779|||http://purl.uniprot.org/annotation/VSP_047780|||http://purl.uniprot.org/annotation/VSP_047781|||http://purl.uniprot.org/annotation/VSP_047782|||http://purl.uniprot.org/annotation/VSP_047783|||http://purl.uniprot.org/annotation/VSP_047784|||http://purl.uniprot.org/annotation/VSP_047785
http://togogenome.org/gene/9606:ZFP90                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3QKQ8|||http://purl.uniprot.org/uniprot/Q8TF47                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Experimental Information|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Crosslink|||Domain Extent|||Sequence Conflict|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 2.|||KRAB|||Zinc finger protein 90 homolog                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047310|||http://purl.uniprot.org/annotation/VSP_057516|||http://purl.uniprot.org/annotation/VSP_057517
http://togogenome.org/gene/9606:RASSF5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5F3|||http://purl.uniprot.org/uniprot/Q8WWW0                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2.|||In isoform 3.|||N-acetylthreonine|||Phorbol-ester/DAG-type|||Phosphoserine|||Phosphothreonine|||Pro residues|||Ras association domain-containing protein 5|||Ras-associating|||Removed|||SARAH                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000240401|||http://purl.uniprot.org/annotation/VSP_019363|||http://purl.uniprot.org/annotation/VSP_019364|||http://purl.uniprot.org/annotation/VSP_019365|||http://purl.uniprot.org/annotation/VSP_019366
http://togogenome.org/gene/9606:GNA14                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O95837                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Region|||Site                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Modified Residue|||Region                                                                                  ^@                                                                                  ADP-ribosylarginine; by cholera toxin|||G-alpha|||G1 motif|||G2 motif|||G3 motif|||G4 motif|||G5 motif|||Guanine nucleotide-binding protein subunit alpha-14                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000203752
http://togogenome.org/gene/9606:POMT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UKY4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Domain Extent|||Glycosylation Site|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Disordered|||Helical|||In MDDGA2 and MDDGB2.|||In MDDGA2.|||In MDDGB2 and MDDGA2.|||In MDDGB2.|||In MDDGC2.|||In isoform 2.|||MIR 1|||MIR 2|||MIR 3|||N-linked (GlcNAc...) asparagine|||Phosphoserine|||Protein O-mannosyl-transferase 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121488|||http://purl.uniprot.org/annotation/VAR_022083|||http://purl.uniprot.org/annotation/VAR_065037|||http://purl.uniprot.org/annotation/VAR_065038|||http://purl.uniprot.org/annotation/VAR_065039|||http://purl.uniprot.org/annotation/VAR_065040|||http://purl.uniprot.org/annotation/VAR_065041|||http://purl.uniprot.org/annotation/VAR_065042|||http://purl.uniprot.org/annotation/VAR_065043|||http://purl.uniprot.org/annotation/VAR_065044|||http://purl.uniprot.org/annotation/VAR_065045|||http://purl.uniprot.org/annotation/VAR_065046|||http://purl.uniprot.org/annotation/VAR_065047|||http://purl.uniprot.org/annotation/VAR_065048|||http://purl.uniprot.org/annotation/VAR_065049|||http://purl.uniprot.org/annotation/VAR_068968|||http://purl.uniprot.org/annotation/VSP_041457
http://togogenome.org/gene/9606:CPT1C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B3KU49|||http://purl.uniprot.org/uniprot/Q8TCG5                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Carnitine O-palmitoyltransferase 1, brain isoform|||Choline/carnitine acyltransferase|||Cytoplasmic|||Disordered|||Helical|||In SPG73; alters protein conformation; dominant negative mutation.|||In isoform 2.|||In isoform 3.|||Mitochondrial intermembrane|||Polar residues|||Proton acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000210166|||http://purl.uniprot.org/annotation/VAR_073433|||http://purl.uniprot.org/annotation/VSP_010677|||http://purl.uniprot.org/annotation/VSP_012457
http://togogenome.org/gene/9606:SNRPE                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P62304                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Sequence Variant|||Strand                                                                                  ^@                                                                                  In HYPT11; does not affect subcellular localization.|||Sm|||Small nuclear ribonucleoprotein E                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000125529|||http://purl.uniprot.org/annotation/VAR_069619
http://togogenome.org/gene/9606:C1orf185                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T7R7                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Transmembrane                                                                                  ^@                                                                                  Helical|||Uncharacterized protein C1orf185                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271101
http://togogenome.org/gene/9606:DGKG                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P49619                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Zinc Finger                                                                                  ^@                                                                                  DAGKc|||Diacylglycerol kinase gamma|||Disordered|||EF-hand 1|||EF-hand 2|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||Phorbol-ester/DAG-type 1|||Phorbol-ester/DAG-type 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000218459|||http://purl.uniprot.org/annotation/VAR_020259|||http://purl.uniprot.org/annotation/VAR_020260|||http://purl.uniprot.org/annotation/VAR_024430|||http://purl.uniprot.org/annotation/VAR_036119|||http://purl.uniprot.org/annotation/VSP_001267|||http://purl.uniprot.org/annotation/VSP_039922
http://togogenome.org/gene/9606:BCL2L13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WTL4|||http://purl.uniprot.org/uniprot/A0A087WX97|||http://purl.uniprot.org/uniprot/A8K5Y4|||http://purl.uniprot.org/uniprot/B7Z238|||http://purl.uniprot.org/uniprot/B7Z737|||http://purl.uniprot.org/uniprot/E9PDD6|||http://purl.uniprot.org/uniprot/Q86T62|||http://purl.uniprot.org/uniprot/Q9BXK5                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  A|||A; approximate|||B|||B; approximate|||BH1|||BH2|||BH3|||BH4|||Basic and acidic residues|||Bcl-2 Bcl-2 homology region 1-3|||Bcl-2-like protein 13|||Disordered|||Helical|||In isoform 1.|||In isoform 3.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143073|||http://purl.uniprot.org/annotation/VAR_024377|||http://purl.uniprot.org/annotation/VAR_024378|||http://purl.uniprot.org/annotation/VAR_059141|||http://purl.uniprot.org/annotation/VAR_059142|||http://purl.uniprot.org/annotation/VSP_000526|||http://purl.uniprot.org/annotation/VSP_000527|||http://purl.uniprot.org/annotation/VSP_046931
http://togogenome.org/gene/9606:PREX2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q70Z35                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  DEP 1|||DEP 2|||DH|||Disordered|||In a colorectal cancer sample; somatic mutation.|||In isoform 3.|||In isoform 4.|||PDZ 1|||PDZ 2|||PH|||Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000286795|||http://purl.uniprot.org/annotation/VAR_032163|||http://purl.uniprot.org/annotation/VAR_035973|||http://purl.uniprot.org/annotation/VAR_035974|||http://purl.uniprot.org/annotation/VSP_025150|||http://purl.uniprot.org/annotation/VSP_025152|||http://purl.uniprot.org/annotation/VSP_055612|||http://purl.uniprot.org/annotation/VSP_055613|||http://purl.uniprot.org/annotation/VSP_055614
http://togogenome.org/gene/9606:PPP1R8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q12972|||http://purl.uniprot.org/uniprot/Q6ICT4                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Splice Variant|||Strand                                                                                  ^@                                                                                  Abolishes in vitro phosphorylation of isoform gamma by Lyn.|||Abolishes interaction with CDC5L, SF3B1 and MELK, and localization in nuclear speckles. No effect on repressor activity.|||Abolishes nuclear import; when associated with A-195-197-A.|||Abolishes nuclear import; when associated with A-234--237-A.|||Decreases the ability of isoform Gamma to bind and inhibit PP-1.|||Disordered|||FHA|||In isoform Beta.|||In isoform Gamma.|||Interaction with CDC5L, SF3B1 and MELK|||Interaction with EED|||Involved in PP-1 binding|||Involved in PP-1 inhibition|||No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-199 or D-199.|||No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-204 or D-204.|||No effect on interaction with EED.|||No effect on the ability of isoform Gamma to inhibit PP-1.|||Nuclear inhibitor of protein phosphatase 1|||Nuclear localization signal 1|||Nuclear localization signal 2|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Phosphotyrosine; by LYN; in vitro|||RNA-binding|||Reduces PP-1 binding, no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles; when associated with A-201.|||Reduces PP-1 binding, no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles; when associated with A-203.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071505|||http://purl.uniprot.org/annotation/VSP_005119|||http://purl.uniprot.org/annotation/VSP_005120
http://togogenome.org/gene/9606:NEFL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P07196                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Acidic residues|||Asymmetric dimethylarginine; alternate|||Basic and acidic residues|||Coil 1A|||Coil 1B|||Coil 2A|||Coil 2B|||Disordered|||Epitope; recognized by IF-specific monoclonal antibody|||Head|||IF rod|||In CMT1F and CMTDIG.|||In CMT1F.|||In CMT2E and CMT1F.|||In CMT2E.|||In CMT2E; unknown pathological significance.|||In CMTDIG and CMT2E.|||In a Charcot-Marie-Tooth disease patient.|||Linker 1|||Linker 12|||Linker 2|||N-acetylserine|||Neurofilament light polypeptide|||O-linked (GlcNAc) serine|||O-linked (GlcNAc) threonine|||Omega-N-methylarginine|||Omega-N-methylarginine; alternate|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Removed|||Tail|||Tail, subdomain A|||Tail, subdomain B (acidic)                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000063787|||http://purl.uniprot.org/annotation/VAR_009703|||http://purl.uniprot.org/annotation/VAR_016017|||http://purl.uniprot.org/annotation/VAR_016018|||http://purl.uniprot.org/annotation/VAR_016019|||http://purl.uniprot.org/annotation/VAR_016020|||http://purl.uniprot.org/annotation/VAR_016021|||http://purl.uniprot.org/annotation/VAR_016022|||http://purl.uniprot.org/annotation/VAR_016023|||http://purl.uniprot.org/annotation/VAR_016024|||http://purl.uniprot.org/annotation/VAR_016025|||http://purl.uniprot.org/annotation/VAR_021613|||http://purl.uniprot.org/annotation/VAR_021614|||http://purl.uniprot.org/annotation/VAR_081565|||http://purl.uniprot.org/annotation/VAR_081566|||http://purl.uniprot.org/annotation/VAR_081567|||http://purl.uniprot.org/annotation/VAR_081568|||http://purl.uniprot.org/annotation/VAR_081569
http://togogenome.org/gene/9606:DEGS2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q6QHC5                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Initiator Methionine|||Lipid Binding|||Motif|||Region|||Sequence Variant|||Transmembrane                                                                                  ^@                                                                                  Helical|||Histidine box-1|||Histidine box-2|||Histidine box-3|||N-myristoyl glycine|||Removed|||Required for C4-hydroxylase activity|||Sphingolipid delta(4)-desaturase/C4-monooxygenase DES2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000312816|||http://purl.uniprot.org/annotation/VAR_055698|||http://purl.uniprot.org/annotation/VAR_060347
http://togogenome.org/gene/9606:BEX3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q00994                                                                                  ^@                                                                                  Binding Site|||Chain|||Molecule Processing|||Motif|||Natural Variation|||Region|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Motif|||Region|||Splice Variant                                                                                  ^@                                                                                  Disordered|||His cluster|||In isoform 2.|||Interaction with 14-3-3 epsilon|||Interaction with p75NTR/NGFR|||Nuclear export signal|||Protein BEX3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000096688|||http://purl.uniprot.org/annotation/VSP_046343
http://togogenome.org/gene/9606:MPP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MRU0|||http://purl.uniprot.org/uniprot/A0A0C4DH75|||http://purl.uniprot.org/uniprot/B4DRL7|||http://purl.uniprot.org/uniprot/B4DZ84|||http://purl.uniprot.org/uniprot/D3DX48|||http://purl.uniprot.org/uniprot/D3DX49|||http://purl.uniprot.org/uniprot/Q14168                                                                                  ^@                                                                                  Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Sequence Conflict|||Splice Variant|||Strand                                                                                  ^@                                                                                  Enhances association with the cytoskeleton.|||Enhances association with the cytoskeleton. Diminishes the inhibitory effect on SRC.|||Guanylate kinase-like|||In isoform 2, isoform 3, isoform 4 and isoform 6.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 6.|||L27|||L27 1|||L27 2|||MAGUK p55 subfamily member 2|||PDZ|||Phosphoserine|||Phosphothreonine|||SH3                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000094573|||http://purl.uniprot.org/annotation/VSP_003156|||http://purl.uniprot.org/annotation/VSP_022951|||http://purl.uniprot.org/annotation/VSP_055136|||http://purl.uniprot.org/annotation/VSP_055137|||http://purl.uniprot.org/annotation/VSP_055138
http://togogenome.org/gene/9606:TKT                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P29401|||http://purl.uniprot.org/uniprot/V9HWD9                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Important for catalytic activity|||In SDDHD; decreased of transketolase activity.|||In isoform 2.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Proton donor|||Transketolase|||Transketolase signature 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000191894|||http://purl.uniprot.org/annotation/VAR_052634|||http://purl.uniprot.org/annotation/VAR_077030|||http://purl.uniprot.org/annotation/VSP_045566
http://togogenome.org/gene/9606:MAGIX                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WUY6|||http://purl.uniprot.org/uniprot/A0A087X263|||http://purl.uniprot.org/uniprot/Q9H6Y5                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In isoform 2 and isoform 3.|||In isoform 3.|||PDZ|||PDZ domain-containing protein MAGIX|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000310542|||http://purl.uniprot.org/annotation/VAR_037075|||http://purl.uniprot.org/annotation/VAR_047035|||http://purl.uniprot.org/annotation/VAR_047036|||http://purl.uniprot.org/annotation/VAR_047037|||http://purl.uniprot.org/annotation/VSP_029319|||http://purl.uniprot.org/annotation/VSP_029320
http://togogenome.org/gene/9606:TOR3A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H497                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||No effect on subcellular location.|||Torsin-3A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000228147|||http://purl.uniprot.org/annotation/VAR_025697|||http://purl.uniprot.org/annotation/VSP_017665|||http://purl.uniprot.org/annotation/VSP_017666|||http://purl.uniprot.org/annotation/VSP_017667
http://togogenome.org/gene/9606:DPM3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJI4|||http://purl.uniprot.org/uniprot/Q86TM7|||http://purl.uniprot.org/uniprot/Q9P2X0                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Dolichol-phosphate mannosyltransferase subunit 3|||Helical|||In MDDGB15; unknown pathological significance.|||In MDDGC15; unknown pathological significance.|||In MDDGC15; when transfected into DPM3-deficient cells, only slightly restores dolichol-phosphate mannose synthase activity contrary to wild-type DPM3; reduced interaction with DPM1.|||In isoform 2.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195000|||http://purl.uniprot.org/annotation/VAR_062518|||http://purl.uniprot.org/annotation/VAR_085122|||http://purl.uniprot.org/annotation/VAR_085123|||http://purl.uniprot.org/annotation/VAR_085124|||http://purl.uniprot.org/annotation/VSP_001308
http://togogenome.org/gene/9606:CCL26                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y258                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  C-C motif chemokine 26                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000005238|||http://purl.uniprot.org/annotation/VAR_029192
http://togogenome.org/gene/9606:GRM8                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00222                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Crosslink|||Disulfide Bond|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In isoform B.|||In isoform C.|||Metabotropic glutamate receptor 8|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000012941|||http://purl.uniprot.org/annotation/VAR_014446|||http://purl.uniprot.org/annotation/VAR_014447|||http://purl.uniprot.org/annotation/VAR_014448|||http://purl.uniprot.org/annotation/VAR_014449|||http://purl.uniprot.org/annotation/VAR_049278|||http://purl.uniprot.org/annotation/VAR_054477|||http://purl.uniprot.org/annotation/VAR_054478|||http://purl.uniprot.org/annotation/VAR_054479|||http://purl.uniprot.org/annotation/VAR_054752|||http://purl.uniprot.org/annotation/VAR_054753|||http://purl.uniprot.org/annotation/VAR_054754|||http://purl.uniprot.org/annotation/VSP_002032|||http://purl.uniprot.org/annotation/VSP_002033|||http://purl.uniprot.org/annotation/VSP_002034
http://togogenome.org/gene/9606:TRIML1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N9V2                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Domain Extent|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  B30.2/SPRY|||In a breast cancer sample; somatic mutation.|||Probable E3 ubiquitin-protein ligase TRIML1|||RING-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000274598|||http://purl.uniprot.org/annotation/VAR_035963|||http://purl.uniprot.org/annotation/VAR_052145
http://togogenome.org/gene/9606:SOX11                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P35716                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||DNA Binding|||Helix|||Modified Residue|||Region|||Sequence Variant                                                                                  ^@                                                                                  Disordered|||HMG box|||In IDDMOH.|||In IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces a reduced GDF5 promoter activation using an in vitro reporter system.|||In IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces a severely reduced GDF5 promoter activation using an in vitro reporter system.|||In IDDMOH; decreased function in positive regulation of DNA-templated transcription; compared to the wild-type, the mutant induces reduced GDF5 promoter activation using an in vitro reporter system; no effect on nuclear localization.|||In IDDMOH; decreases transcriptional activity.|||In IDDMOH; unknown pathological significance.|||In IDDMOH; unknown pathological significance; no effect on nuclear localization.|||Phosphoserine|||Polar residues|||Required for transcriptional activation activity and synergistic coactivation of transcriptional activity with POU3F2|||Transcription factor SOX-11                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000048750|||http://purl.uniprot.org/annotation/VAR_071461|||http://purl.uniprot.org/annotation/VAR_071462|||http://purl.uniprot.org/annotation/VAR_088026|||http://purl.uniprot.org/annotation/VAR_088027|||http://purl.uniprot.org/annotation/VAR_088028|||http://purl.uniprot.org/annotation/VAR_088029|||http://purl.uniprot.org/annotation/VAR_088030|||http://purl.uniprot.org/annotation/VAR_088031|||http://purl.uniprot.org/annotation/VAR_088032|||http://purl.uniprot.org/annotation/VAR_088033|||http://purl.uniprot.org/annotation/VAR_088034|||http://purl.uniprot.org/annotation/VAR_088035|||http://purl.uniprot.org/annotation/VAR_088036|||http://purl.uniprot.org/annotation/VAR_088037|||http://purl.uniprot.org/annotation/VAR_088038|||http://purl.uniprot.org/annotation/VAR_088039|||http://purl.uniprot.org/annotation/VAR_088040|||http://purl.uniprot.org/annotation/VAR_088041|||http://purl.uniprot.org/annotation/VAR_088042|||http://purl.uniprot.org/annotation/VAR_088043|||http://purl.uniprot.org/annotation/VAR_088044|||http://purl.uniprot.org/annotation/VAR_088045|||http://purl.uniprot.org/annotation/VAR_088046|||http://purl.uniprot.org/annotation/VAR_088047|||http://purl.uniprot.org/annotation/VAR_088048|||http://purl.uniprot.org/annotation/VAR_088049|||http://purl.uniprot.org/annotation/VAR_088050|||http://purl.uniprot.org/annotation/VAR_088051|||http://purl.uniprot.org/annotation/VAR_088052|||http://purl.uniprot.org/annotation/VAR_088053|||http://purl.uniprot.org/annotation/VAR_088054|||http://purl.uniprot.org/annotation/VAR_088055|||http://purl.uniprot.org/annotation/VAR_088056|||http://purl.uniprot.org/annotation/VAR_088057|||http://purl.uniprot.org/annotation/VAR_088058|||http://purl.uniprot.org/annotation/VAR_088059|||http://purl.uniprot.org/annotation/VAR_088060|||http://purl.uniprot.org/annotation/VAR_088061|||http://purl.uniprot.org/annotation/VAR_088062
http://togogenome.org/gene/9606:CIART                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5TB12|||http://purl.uniprot.org/uniprot/Q8N365|||http://purl.uniprot.org/uniprot/Q8WVX4                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Non-terminal Residue|||Region|||Sequence Conflict|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Circadian-associated transcriptional repressor|||Disordered|||In isoform 2.|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000251193|||http://purl.uniprot.org/annotation/VSP_020743|||http://purl.uniprot.org/annotation/VSP_020744
http://togogenome.org/gene/9606:SUGP2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K5G0|||http://purl.uniprot.org/uniprot/M0R2Z9|||http://purl.uniprot.org/uniprot/Q8IX01                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Region|||Repeat|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Acidic residues|||Disordered|||G-patch|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In isoform 3 and isoform 4.|||In isoform 3.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Polar residues|||SURP and G-patch domain-containing protein 2|||SURP motif|||SURP motif 1|||SURP motif 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000097708|||http://purl.uniprot.org/annotation/VAR_023711|||http://purl.uniprot.org/annotation/VAR_051341|||http://purl.uniprot.org/annotation/VAR_051342|||http://purl.uniprot.org/annotation/VAR_051343|||http://purl.uniprot.org/annotation/VAR_051344|||http://purl.uniprot.org/annotation/VSP_013112|||http://purl.uniprot.org/annotation/VSP_013113
http://togogenome.org/gene/9606:RAB27B                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00194                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Helix|||Initiator Methionine|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Variant|||Strand|||Turn                                                                                  ^@                                                                                  Cysteine methyl ester|||Disordered|||Effector region|||GDP-locked. Increases interaction with DENND10. Disrupts late endocytic pathway homeostasis.|||GTP-locked. decreases interaction with DENND10.|||N-acetylthreonine|||Ras-related protein Rab-27B|||Removed|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000121224|||http://purl.uniprot.org/annotation/VAR_051714
http://togogenome.org/gene/9606:PKD1L1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8TDX9                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Region|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||GPS|||Helical|||In HTX8.|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||PKD 1|||PKD 2|||PLAT|||Polar residues|||Polycystin-1-like protein 1|||REJ                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000164358|||http://purl.uniprot.org/annotation/VAR_021944|||http://purl.uniprot.org/annotation/VAR_024566|||http://purl.uniprot.org/annotation/VAR_024567|||http://purl.uniprot.org/annotation/VAR_024568|||http://purl.uniprot.org/annotation/VAR_050552|||http://purl.uniprot.org/annotation/VAR_050553|||http://purl.uniprot.org/annotation/VAR_050554|||http://purl.uniprot.org/annotation/VAR_061522|||http://purl.uniprot.org/annotation/VAR_061523|||http://purl.uniprot.org/annotation/VAR_061524|||http://purl.uniprot.org/annotation/VAR_065825|||http://purl.uniprot.org/annotation/VAR_077879|||http://purl.uniprot.org/annotation/VSP_013215|||http://purl.uniprot.org/annotation/VSP_013216
http://togogenome.org/gene/9606:GABRB3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/B2RCW8|||http://purl.uniprot.org/uniprot/P28472|||http://purl.uniprot.org/uniprot/X5DQY4                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Non-terminal Residue|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Found in a subject suffering from insomnia; functional analysis reveals a slower rate of the fast phase of desensitization compared with alpha1beta3gamma2SGABA(A) receptors; current deactivation is faster in the mutated receptors.|||Found in patients with Dravet syndrome; unknown pathological significance.|||Gamma-aminobutyric acid receptor subunit beta-3|||Helical|||In DEE43.|||In DEE43; no effect on localization to the plasma membrane; decreased GABA-gated chloride ion channel activity; decreased single channel open probability.|||In DEE43; unknown pathological significance.|||In ECA5, the mutant protein is hyperglycosylated and has reduced mean current densities compared to wild-type.|||In ECA5; the mutant protein is hyperglycosylated and has reduced mean current densities compared to wild-type.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel ligand-binding|||Neurotransmitter-gated ion-channel transmembrane                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000462|||http://purl.uniprot.org/annotation/PRO_5022267020|||http://purl.uniprot.org/annotation/PRO_5022270819|||http://purl.uniprot.org/annotation/VAR_047957|||http://purl.uniprot.org/annotation/VAR_047958|||http://purl.uniprot.org/annotation/VAR_047959|||http://purl.uniprot.org/annotation/VAR_077076|||http://purl.uniprot.org/annotation/VAR_077077|||http://purl.uniprot.org/annotation/VAR_077078|||http://purl.uniprot.org/annotation/VAR_077079|||http://purl.uniprot.org/annotation/VAR_077080|||http://purl.uniprot.org/annotation/VAR_077081|||http://purl.uniprot.org/annotation/VAR_077082|||http://purl.uniprot.org/annotation/VAR_078223|||http://purl.uniprot.org/annotation/VAR_078224|||http://purl.uniprot.org/annotation/VAR_078619|||http://purl.uniprot.org/annotation/VAR_078719|||http://purl.uniprot.org/annotation/VAR_079429|||http://purl.uniprot.org/annotation/VAR_082790|||http://purl.uniprot.org/annotation/VAR_082791|||http://purl.uniprot.org/annotation/VSP_000088|||http://purl.uniprot.org/annotation/VSP_046126|||http://purl.uniprot.org/annotation/VSP_046676
http://togogenome.org/gene/9606:CLEC4M                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9H2X3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Motif|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Motif|||Region|||Repeat|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  1|||2|||3|||4|||5|||6|||7|||7 X approximate tandem repeats|||C-type lectin|||C-type lectin domain family 4 member M|||Cytoplasmic|||Endocytosis signal|||Extracellular|||Helical; Signal-anchor for type II membrane protein|||In isoform 10.|||In isoform 2, isoform 6 and isoform 10.|||In isoform 3, isoform 4 and isoform 9.|||In isoform 4 and isoform 5.|||In isoform 4.|||In isoform 5 and isoform 8.|||In isoform 5, isoform 6 and isoform 7.|||In isoform 7.|||In isoform 9 and isoform 10.|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000046626|||http://purl.uniprot.org/annotation/VAR_021957|||http://purl.uniprot.org/annotation/VAR_050107|||http://purl.uniprot.org/annotation/VAR_050108|||http://purl.uniprot.org/annotation/VAR_050109|||http://purl.uniprot.org/annotation/VSP_010056|||http://purl.uniprot.org/annotation/VSP_010057|||http://purl.uniprot.org/annotation/VSP_010058|||http://purl.uniprot.org/annotation/VSP_010059|||http://purl.uniprot.org/annotation/VSP_010060|||http://purl.uniprot.org/annotation/VSP_010061|||http://purl.uniprot.org/annotation/VSP_010062|||http://purl.uniprot.org/annotation/VSP_010063|||http://purl.uniprot.org/annotation/VSP_010064|||http://purl.uniprot.org/annotation/VSP_010065|||http://purl.uniprot.org/annotation/VSP_010066
http://togogenome.org/gene/9606:EHF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9NZC4                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||DNA Binding|||Domain Extent|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||ETS|||ETS homologous factor|||In isoform 2.|||In isoform 3.|||PNT                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000257969|||http://purl.uniprot.org/annotation/VAR_048941|||http://purl.uniprot.org/annotation/VSP_046373|||http://purl.uniprot.org/annotation/VSP_052190
http://togogenome.org/gene/9606:HPCAL1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75544|||http://purl.uniprot.org/uniprot/P37235|||http://purl.uniprot.org/uniprot/Q6FGY1                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Lipid Binding|||Modification|||Molecule Processing|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Strand                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Lipid Binding|||Non-terminal Residue|||Sequence Conflict|||Strand                                                                                  ^@                                                                                  EF-hand|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand 4|||Hippocalcin-like protein 1|||N-myristoyl glycine|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000073771
http://togogenome.org/gene/9606:CHPF                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8IZ52                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chondroitin sulfate synthase 2|||Cytoplasmic|||Disordered|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||In isoform 3.|||Lumenal|||N-linked (GlcNAc...) asparagine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189560|||http://purl.uniprot.org/annotation/VAR_047394|||http://purl.uniprot.org/annotation/VSP_053433|||http://purl.uniprot.org/annotation/VSP_053434
http://togogenome.org/gene/9606:PAFAH1B3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q15102                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Sequence Variant|||Site                                                                                  ^@                                                                                  Active Site|||Chain|||Initiator Methionine|||Modified Residue|||Sequence Variant                                                                                  ^@                                                                                  N-acetylserine|||Phosphoserine|||Platelet-activating factor acetylhydrolase IB subunit alpha1|||Removed                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058155|||http://purl.uniprot.org/annotation/VAR_051261
http://togogenome.org/gene/9606:OR8H1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A126GVW6|||http://purl.uniprot.org/uniprot/Q8NGG4                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||N-linked (GlcNAc...) asparagine|||Olfactory receptor 8H1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000150665|||http://purl.uniprot.org/annotation/VAR_034261|||http://purl.uniprot.org/annotation/VAR_053246
http://togogenome.org/gene/9606:FAM149B1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96BN6                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In JBTS36; changed protein localization to cilium; changed cilium assembly; no difference in the number of ciliated cells but SHH signaling is altered.|||In isoform 2.|||Polar residues|||Primary cilium assembly protein FAM149B1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000319933|||http://purl.uniprot.org/annotation/VAR_060167|||http://purl.uniprot.org/annotation/VAR_083866|||http://purl.uniprot.org/annotation/VSP_031533|||http://purl.uniprot.org/annotation/VSP_031534
http://togogenome.org/gene/9606:DEAF1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75398                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn|||Zinc Finger                                                                                  ^@                                                                                  Abolishes DNA-binding.|||Abolishes DNA-binding. Loss of DEAF1-promoter repression; when associated with A-253. Loss of transcriptional activation of EIF4G3; when associated with A-253. Loss of interaction with XRCC6; when associated with A-253. Loss of DNA binding; when associated with A-253.|||Abolishes DNA-binding. oss of DEAF1-promoter repression; when associated with A-250. Loss of transcriptional activation of EIF4G3; when associated with A-250. Loss of interaction with XRCC6; when associated with A-250. Loss of DNA binding; when associated with A-250.|||Abolishes nuclear localization.|||Deformed epidermal autoregulatory factor 1 homolog|||Disordered|||In VSVS; loss of DEAF1-promoter repression; gain of transcriptional activation of EIF4G3; a 9-fold reduction in DNA binding.|||In VSVS; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; decreased interaction with XRCC6.|||In VSVS; loss of DEAF1-promoter repression; loss of transcriptional activation of EIF4G3; loss of DNA binding; loss of interaction with XRCC6.|||In a primary colorectal cancer.|||In a primary colorectal cancer; requires 2 nucleotide substitutions.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||Interaction with LMO4|||MYND-type|||No effect on folding of MYND-type zinc finger.|||Nuclear localization signal|||Phosphoserine|||Phosphothreonine|||Reduces transcription activation.|||SAND                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000074084|||http://purl.uniprot.org/annotation/VAR_013725|||http://purl.uniprot.org/annotation/VAR_013726|||http://purl.uniprot.org/annotation/VAR_013727|||http://purl.uniprot.org/annotation/VAR_013728|||http://purl.uniprot.org/annotation/VAR_013729|||http://purl.uniprot.org/annotation/VAR_013730|||http://purl.uniprot.org/annotation/VAR_013731|||http://purl.uniprot.org/annotation/VAR_013732|||http://purl.uniprot.org/annotation/VAR_013733|||http://purl.uniprot.org/annotation/VAR_013734|||http://purl.uniprot.org/annotation/VAR_013735|||http://purl.uniprot.org/annotation/VAR_013736|||http://purl.uniprot.org/annotation/VAR_013737|||http://purl.uniprot.org/annotation/VAR_013738|||http://purl.uniprot.org/annotation/VAR_013739|||http://purl.uniprot.org/annotation/VAR_013740|||http://purl.uniprot.org/annotation/VAR_013741|||http://purl.uniprot.org/annotation/VAR_013742|||http://purl.uniprot.org/annotation/VAR_013743|||http://purl.uniprot.org/annotation/VAR_013744|||http://purl.uniprot.org/annotation/VAR_013745|||http://purl.uniprot.org/annotation/VAR_013746|||http://purl.uniprot.org/annotation/VAR_013747|||http://purl.uniprot.org/annotation/VAR_013748|||http://purl.uniprot.org/annotation/VAR_065089|||http://purl.uniprot.org/annotation/VAR_071371|||http://purl.uniprot.org/annotation/VAR_071372|||http://purl.uniprot.org/annotation/VAR_071373|||http://purl.uniprot.org/annotation/VAR_071374|||http://purl.uniprot.org/annotation/VSP_005966|||http://purl.uniprot.org/annotation/VSP_005967|||http://purl.uniprot.org/annotation/VSP_038701|||http://purl.uniprot.org/annotation/VSP_038702
http://togogenome.org/gene/9606:WASL                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O00401                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Region|||Secondary Structure|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Region|||Sequence Conflict|||Turn                                                                                  ^@                                                                                  Acidic residues|||Actin nucleation-promoting factor WASL|||CRIB|||Disordered|||N-acetylserine|||Omega-N-methylarginine|||Phosphoserine|||Phosphoserine; by TNK2|||Phosphotyrosine; by FAK1 and TNK2|||Pro residues|||Removed|||WH1|||WH2 1|||WH2 2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000189000
http://togogenome.org/gene/9606:B3GAT1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P2W7                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Glycosylation Site|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Essential for transport from endoplasmic reticulum to Golgi apparatus and interaction with SAR1A|||Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1|||Helical; Signal-anchor for type II membrane protein|||In isoform 2.|||Interaction with galactose moiety of substrate glycoprotein|||Lumenal|||N-linked (GlcNAc...) asparagine|||Phosphothreonine|||Proton donor/acceptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000195167|||http://purl.uniprot.org/annotation/VAR_044538|||http://purl.uniprot.org/annotation/VSP_058538
http://togogenome.org/gene/9606:TRPA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75762                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||INTRAMEM|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Repeat|||Secondary Structure|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Disulfide Bond|||Glycosylation Site|||Helix|||INTRAMEM|||Modified Residue|||Mutagenesis Site|||Repeat|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  4-hydroxyproline; by EGLN1; transient; in normoxia and hyperoxia|||ANK 1|||ANK 10|||ANK 11|||ANK 12|||ANK 13|||ANK 14|||ANK 15|||ANK 16|||ANK 2|||ANK 3|||ANK 4|||ANK 5|||ANK 6|||ANK 7|||ANK 8|||ANK 9|||Alternate|||Alternate; transient; in hyperoxia; unknown whether inter- or intrachain|||Cysteine sulfenic acid (-SOH); transient; in hyperoxia|||Cytoplasmic|||Decrease in activation by hyperoxia and diallyl disulfide.|||Decrease in activation by hyperoxia and diallyl disulfide. Important decrease in activation by hyperoxia and diallyl disulfide; when associated with S-633.|||Decrease in activation by hyperoxia and diallyl disulfide. Important decrease in activation by hyperoxia and diallyl disulfide; when associated with S-856.|||Decrease in electrophile-evoked and hyperoxia response. In TRPA1-3C-K708R/Q; loss in irritant-evoked response.|||Decrease in electrophile-evoked response. No change in answer to hyperoxia and diallyl disulfide. In TRPA1-3C-K708R/Q; loss in irritant-evoked response.|||Extracellular|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Important decrease in electrophile-evoked response.|||Important residue for activation by the scorpion wasabi receptor toxin|||In FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation.|||Key residue for activation by the scorpion wasabi receptor toxin|||Loss of activation by the scorpion wasabi receptor toxin.|||Loss of answer to hypoxia and hydroxylase inhibitor DMOG, but not to AITC and hyperoxia.|||Loss of inhibition by A-967079, AP-18, and ASD. Increase in activation by cinnamaldehyde, AITC and acrolein.|||Loss of inhibition by A-967079, AP-18, and ASD. Weak or no change in activation by cinnamaldehyde, AITC and acrolein.|||N-linked (GlcNAc...) asparagine|||No change in electrophile sensitivity. In TRPA1-3C-K708R/Q; loss in irritant-evoked response.|||Pore-forming|||Required for C-621 reactivity|||Transient receptor potential cation channel subfamily A member 1|||covalent|||covalent; Cys highly reactive                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215369|||http://purl.uniprot.org/annotation/VAR_020660|||http://purl.uniprot.org/annotation/VAR_020661|||http://purl.uniprot.org/annotation/VAR_020662|||http://purl.uniprot.org/annotation/VAR_020663|||http://purl.uniprot.org/annotation/VAR_047471|||http://purl.uniprot.org/annotation/VAR_069737
http://togogenome.org/gene/9606:TMEM178A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8NBL3                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Modification|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Glycosylation Site|||Region|||Sequence Variant|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Disordered|||Extracellular|||Helical|||In isoform 2.|||N-linked (GlcNAc...) asparagine|||Transmembrane protein 178A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000287280|||http://purl.uniprot.org/annotation/VAR_032296|||http://purl.uniprot.org/annotation/VSP_025428|||http://purl.uniprot.org/annotation/VSP_025429
http://togogenome.org/gene/9606:TREM1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/K7EKM5|||http://purl.uniprot.org/uniprot/Q38L15|||http://purl.uniprot.org/uniprot/Q9NP99                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Helical|||Ig-like V-type|||Immunoglobulin subtype|||In a breast cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||N-linked (GlcNAc...) asparagine|||Triggering receptor expressed on myeloid cells 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000014986|||http://purl.uniprot.org/annotation/PRO_5014309051|||http://purl.uniprot.org/annotation/PRO_5014580460|||http://purl.uniprot.org/annotation/VAR_019333|||http://purl.uniprot.org/annotation/VAR_033624|||http://purl.uniprot.org/annotation/VAR_035525|||http://purl.uniprot.org/annotation/VAR_049949|||http://purl.uniprot.org/annotation/VSP_010790|||http://purl.uniprot.org/annotation/VSP_010791|||http://purl.uniprot.org/annotation/VSP_053939
http://togogenome.org/gene/9606:DBR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UK59                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||In IIAE11; decreased protein abundance; decreased RNA lariat debranching enzyme activity.|||In IIAE11; loss of protein expression.|||In IIAE11; requires 2 nucleotide substitutions; decreased protein abundance; decreased RNA lariat debranching enzyme activity.|||In isoform 2.|||Lariat debranching enzyme|||Lariat recognition loop|||N6-acetyllysine|||No effect on protein abundance. Loss of RNA lariat debranching enzyme activity.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000250358|||http://purl.uniprot.org/annotation/VAR_086073|||http://purl.uniprot.org/annotation/VAR_086074|||http://purl.uniprot.org/annotation/VAR_086075|||http://purl.uniprot.org/annotation/VAR_086076|||http://purl.uniprot.org/annotation/VSP_020631|||http://purl.uniprot.org/annotation/VSP_020632
http://togogenome.org/gene/9606:EFCAB7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8K855                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Splice Variant                                                                                  ^@                                                                                  Disordered|||EF-hand 1|||EF-hand 2|||EF-hand 3|||EF-hand calcium-binding domain-containing protein 7|||In isoform 2.|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000317266|||http://purl.uniprot.org/annotation/VAR_038493|||http://purl.uniprot.org/annotation/VAR_038494|||http://purl.uniprot.org/annotation/VAR_038495|||http://purl.uniprot.org/annotation/VAR_038496|||http://purl.uniprot.org/annotation/VAR_038497|||http://purl.uniprot.org/annotation/VSP_030930
http://togogenome.org/gene/9606:DNAJC16                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9Y2G8                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Glycosylation Site|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Glycosylation Site|||Mutagenesis Site|||Region|||Signal Peptide|||Splice Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Cytoplasmic|||Disordered|||DnaJ homolog subfamily C member 16|||Does not lead to enlargement of autophagosomes when overexpressed.|||Does not lead to enlargement of autophagosomes when overexpressed; when associated with A-171.|||Does not lead to enlargement of autophagosomes when overexpressed; when associated with A-174.|||Extracellular|||Helical; Anchor for type IV membrane protein|||In isoform 2.|||J|||N-linked (GlcNAc...) asparagine|||Thioredoxin                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000236683|||http://purl.uniprot.org/annotation/VSP_018583
http://togogenome.org/gene/9606:SEPTIN9                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z5A5|||http://purl.uniprot.org/uniprot/Q9UHD8                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Non-terminal Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||G1 motif|||G3 motif|||G4 motif|||In HNA.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||In isoform 7.|||In isoform 8.|||In isoform 9.|||N-acetylmethionine|||N6-acetyllysine|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues|||Septin-9|||Septin-type G                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000173535|||http://purl.uniprot.org/annotation/VAR_020667|||http://purl.uniprot.org/annotation/VAR_020668|||http://purl.uniprot.org/annotation/VAR_020669|||http://purl.uniprot.org/annotation/VAR_033101|||http://purl.uniprot.org/annotation/VAR_033102|||http://purl.uniprot.org/annotation/VSP_012335|||http://purl.uniprot.org/annotation/VSP_012336|||http://purl.uniprot.org/annotation/VSP_012337|||http://purl.uniprot.org/annotation/VSP_012338|||http://purl.uniprot.org/annotation/VSP_038315|||http://purl.uniprot.org/annotation/VSP_038316|||http://purl.uniprot.org/annotation/VSP_038317|||http://purl.uniprot.org/annotation/VSP_038318|||http://purl.uniprot.org/annotation/VSP_038319
http://togogenome.org/gene/9606:TBCA                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/E5RIX8|||http://purl.uniprot.org/uniprot/O75347|||http://purl.uniprot.org/uniprot/Q6FGD7                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Splice Variant                                                                                  ^@                                                                                  Chain|||Coiled-Coil|||Helix|||Initiator Methionine|||Modified Residue|||Splice Variant                                                                                  ^@                                                                                  In isoform 2.|||N-acetylalanine|||Removed|||Tubulin-specific chaperone A                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000080039|||http://purl.uniprot.org/annotation/VSP_056357
http://togogenome.org/gene/9606:CDC42                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P60953                                                                                  ^@                                                                                  Binding Site|||Chain|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Glycosylation Site|||Helix|||Lipid Binding|||Modified Residue|||Motif|||Mutagenesis Site|||Propeptide|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  (Microbial infection) O-AMP-threonine; by Vibrio VopS|||(Microbial infection) O-AMP-tyrosine; by Haemophilus IbpA; alternate|||(Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate|||(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate|||(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate|||Abolishes AMPylation by Haemophilus IbpA.|||Cell division control protein 42 homolog|||Constitutively active. Interacts with PARD6 proteins.|||Constitutively active. Interacts with PARD6 proteins. Does not inhibit filopodia formation. No effect on NR3C2 transcriptional activity.|||Constitutively inactive. Does not interact with PARD6 proteins. Inhibits filopodia formation. No effect on NR3C2 transcriptional activity.|||Cysteine methyl ester|||Effector region|||In TKS.|||In isoform 1.|||Phosphotyrosine; by SRC|||Removed in mature form|||S-geranylgeranyl cysteine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000030425|||http://purl.uniprot.org/annotation/PRO_0000030426|||http://purl.uniprot.org/annotation/VAR_076337|||http://purl.uniprot.org/annotation/VSP_040583|||http://purl.uniprot.org/annotation/VSP_040584
http://togogenome.org/gene/9606:GLRA3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75311|||http://purl.uniprot.org/uniprot/Q9UPF3                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Modified Residue|||Non-terminal Residue|||Sequence Conflict|||Signal Peptide|||Site|||Splice Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Cytoplasmic|||Extracellular|||Glycine receptor subunit alpha-3|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Important for obstruction of the ion pore in the closed conformation|||In isoform Alpha-3K.|||N-linked (GlcNAc...) asparagine|||Neurotransmitter-gated ion-channel transmembrane|||Phosphoserine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000000419|||http://purl.uniprot.org/annotation/VSP_000084
http://togogenome.org/gene/9606:RABAC1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9UI14                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Region|||Sequence Conflict|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Cytoplasmic|||Helical|||Homodimerization|||Prenylated Rab acceptor protein 1|||Required for interaction with GDI1|||Required for interaction with prenylated RAB3A and VAMP2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000220878
http://togogenome.org/gene/9606:AGTR1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MSE3|||http://purl.uniprot.org/uniprot/D3DNG8|||http://purl.uniprot.org/uniprot/P30556|||http://purl.uniprot.org/uniprot/Q53YY0|||http://purl.uniprot.org/uniprot/Q6NUP5                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Experimental Information|||Glycosylation Site|||Helix|||Lipid Binding|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Disulfide Bond|||Domain Extent|||Glycosylation Site|||Helix|||Lipid Binding|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Strand|||Topological Domain|||Transmembrane|||Turn                                                                                  ^@                                                                                  Abolished binding to angiotensin II.|||Abolished binding to angiotensin II; abolished binding to olmesartan inhibitor.|||Cytoplasmic|||Decreased binding to eprosartan inhibitor.|||Decreased binding to telmisartan inhibitor.|||Disordered|||Extracellular|||G-protein coupled receptors family 1 profile|||Helical|||Helical; Name=1|||Helical; Name=2|||Helical; Name=3|||Helical; Name=4|||Helical; Name=5|||Helical; Name=6|||Helical; Name=7|||In RTD.|||Increased affinity for angiotensin II.|||Induces a conformational change in the angiotensin II-binding pocket, leading to constitutive activation of the receptor.|||Mimics the disordered side chain induced by angiotensin II-binding; increased affinity for G-protein subunit alpha proteins. Decreased affinity for telmisartan.|||N-linked (GlcNAc...) (complex) asparagine|||N-linked (GlcNAc...) asparagine|||Polar residues|||Reduced affinity for angiotensin II.|||Reduced binding to angiotensin II without affecting binding to candesartan inhibitor.|||S-palmitoyl cysteine|||Slightly affects binding to eprosartan inhibitor.|||Type-1 angiotensin II receptor                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000069153|||http://purl.uniprot.org/annotation/VAR_011847|||http://purl.uniprot.org/annotation/VAR_011848|||http://purl.uniprot.org/annotation/VAR_029206|||http://purl.uniprot.org/annotation/VAR_029207|||http://purl.uniprot.org/annotation/VAR_035086|||http://purl.uniprot.org/annotation/VAR_070375|||http://purl.uniprot.org/annotation/VAR_070376
http://togogenome.org/gene/9606:IFNA13                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A087WWS6|||http://purl.uniprot.org/uniprot/P01562                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Experimental Information|||Helix|||Modification|||Molecule Processing|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Helix|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Turn                                                                                  ^@                                                                                  In alpha-1B.|||Interferon alpha-1/13                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000016359|||http://purl.uniprot.org/annotation/PRO_5001832002|||http://purl.uniprot.org/annotation/VAR_013000|||http://purl.uniprot.org/annotation/VAR_024508|||http://purl.uniprot.org/annotation/VAR_025173
http://togogenome.org/gene/9606:LELP1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q5T871                                                                                  ^@                                                                                  Chain|||Molecule Processing|||Region                                                                                  ^@                                                                                  Chain|||Region                                                                                  ^@                                                                                  Disordered|||Late cornified envelope-like proline-rich protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000271603
http://togogenome.org/gene/9606:SPACA4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A140VJU1|||http://purl.uniprot.org/uniprot/Q8TDM5                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Modification|||Molecule Processing|||Propeptide|||Region|||Signal Peptide                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Lipid Binding|||Propeptide|||Signal Peptide                                                                                  ^@                                                                                  GPI-anchor amidated asparagine|||Removed in mature form|||Sperm acrosome membrane-associated protein 4|||UPAR/Ly6                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000252450|||http://purl.uniprot.org/annotation/PRO_0000252451|||http://purl.uniprot.org/annotation/PRO_5014247029
http://togogenome.org/gene/9606:PPT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A1U9X8D2|||http://purl.uniprot.org/uniprot/Q9UMR5                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Experimental Information|||Glycosylation Site|||Helix|||Modification|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Chain|||Disulfide Bond|||Glycosylation Site|||Helix|||Mutagenesis Site|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Abolishes enzymatic activity.|||In isoform 2.|||In isoform 3.|||Lysosomal thioesterase PPT2|||N-linked (GlcNAc...) asparagine|||No effect on enzymatic activity.|||Nucleophile                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000025554|||http://purl.uniprot.org/annotation/PRO_5010700917|||http://purl.uniprot.org/annotation/VAR_027107|||http://purl.uniprot.org/annotation/VAR_027108|||http://purl.uniprot.org/annotation/VSP_005188|||http://purl.uniprot.org/annotation/VSP_054027
http://togogenome.org/gene/9606:SAA1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/P0DJI8                                                                                  ^@                                                                                  Chain|||Experimental Information|||Helix|||Mass|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Propeptide|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Chain|||Helix|||Mass|||Modified Residue|||Mutagenesis Site|||Propeptide|||Region|||Sequence Conflict|||Sequence Variant|||Signal Peptide|||Strand                                                                                  ^@                                                                                  Amyloid protein A|||Disordered|||Important for amyloid formation; forms amyloid fibrils in vitro|||In allele SAA1.2, SAA1.3, SAA1.4 and SAA1.5.|||In allele SAA1.2, SAA1.4 and SAA1.5.|||In allele SAA1.2.|||In allele SAA1.4.|||N4,N4-dimethylasparagine|||Often cleaved during amyloidogenesis|||Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-80.|||Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-89.|||Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-80 and A-89.|||Reduces affinity for heparin; when associated with A-33 and A-37.|||Reduces affinity for heparin; when associated with A-33 and A-65.|||Reduces affinity for heparin; when associated with A-37 and A-65.|||Serum amyloid A-1 protein|||Serum amyloid protein A(2-102)|||Serum amyloid protein A(2-103)|||Serum amyloid protein A(2-104)|||Serum amyloid protein A(3-104)|||Serum amyloid protein A(4-101)|||With variant Ala-70.|||With variants Ala-70, Val-75, Asn-78 and 86-Leu-Thr-87.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000031575|||http://purl.uniprot.org/annotation/PRO_0000031576|||http://purl.uniprot.org/annotation/PRO_0000031577|||http://purl.uniprot.org/annotation/PRO_0000031578|||http://purl.uniprot.org/annotation/PRO_0000031579|||http://purl.uniprot.org/annotation/PRO_0000031580|||http://purl.uniprot.org/annotation/PRO_0000031581|||http://purl.uniprot.org/annotation/PRO_0000031582|||http://purl.uniprot.org/annotation/VAR_006925|||http://purl.uniprot.org/annotation/VAR_006926|||http://purl.uniprot.org/annotation/VAR_006927|||http://purl.uniprot.org/annotation/VAR_006928|||http://purl.uniprot.org/annotation/VAR_006931|||http://purl.uniprot.org/annotation/VAR_057167
http://togogenome.org/gene/9606:ZNF264                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O43296                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Modified Residue|||Region|||Sequence Variant|||Zinc Finger                                                                                  ^@                                                                                  Basic and acidic residues|||C2H2-type 1|||C2H2-type 10|||C2H2-type 11|||C2H2-type 12|||C2H2-type 13|||C2H2-type 2|||C2H2-type 3|||C2H2-type 4|||C2H2-type 5|||C2H2-type 6|||C2H2-type 7|||C2H2-type 8|||C2H2-type 9|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||KRAB|||Phosphoserine|||Phosphotyrosine|||Polar residues|||Zinc finger protein 264                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000047492|||http://purl.uniprot.org/annotation/VAR_052803|||http://purl.uniprot.org/annotation/VAR_052804
http://togogenome.org/gene/9606:FAM3C                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q92520                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Modification|||Molecule Processing|||Region|||Secondary Structure|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Disulfide Bond|||Domain Extent|||Helix|||Signal Peptide|||Strand|||Turn                                                                                  ^@                                                                                  GG-type lectin|||Protein FAM3C                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000008752
http://togogenome.org/gene/9606:CDC45                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/O75419                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Cell division control protein 45 homolog|||Disordered|||In MGORS7; decreased protein level.|||In MGORS7; unknown pathological significance.|||In MGORS7; unknown pathological significance; associated in cis with G-155.|||In MGORS7; unknown pathological significance; associated in cis with T-321.|||In isoform 2.|||In isoform 3.|||Phosphoserine|||Phosphotyrosine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000192815|||http://purl.uniprot.org/annotation/VAR_019286|||http://purl.uniprot.org/annotation/VAR_019287|||http://purl.uniprot.org/annotation/VAR_053026|||http://purl.uniprot.org/annotation/VAR_080963|||http://purl.uniprot.org/annotation/VAR_080964|||http://purl.uniprot.org/annotation/VAR_080965|||http://purl.uniprot.org/annotation/VAR_080966|||http://purl.uniprot.org/annotation/VAR_080967|||http://purl.uniprot.org/annotation/VAR_080968|||http://purl.uniprot.org/annotation/VAR_080969|||http://purl.uniprot.org/annotation/VAR_080970|||http://purl.uniprot.org/annotation/VAR_080971|||http://purl.uniprot.org/annotation/VAR_080972|||http://purl.uniprot.org/annotation/VAR_080973|||http://purl.uniprot.org/annotation/VAR_080974|||http://purl.uniprot.org/annotation/VSP_043129|||http://purl.uniprot.org/annotation/VSP_045411
http://togogenome.org/gene/9606:THYN1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q9P016                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Experimental Information|||Helix|||Molecule Processing|||Motif|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Helix|||Motif|||Region|||Sequence Conflict|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Disordered|||In isoform 2.|||Nuclear localization signal|||Polar residues|||Thymocyte nuclear protein 1                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000262564|||http://purl.uniprot.org/annotation/VSP_021789
http://togogenome.org/gene/9606:DNAJC4                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/J3KNJ8|||http://purl.uniprot.org/uniprot/Q6PIN0|||http://purl.uniprot.org/uniprot/Q86VG4|||http://purl.uniprot.org/uniprot/Q9NNZ3                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Molecule Processing|||Non-terminal Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Non-terminal Residue|||Region|||Transmembrane                                                                                  ^@                                                                                  Disordered|||DnaJ homolog subfamily C member 4|||Helical|||J|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000071049
http://togogenome.org/gene/9606:OSBPL5                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A8KAD5|||http://purl.uniprot.org/uniprot/Q9H0X9                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Sequence Variant|||Site|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Binding Site|||Chain|||Coiled-Coil|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Basic and acidic residues|||Disordered|||Helical|||Impaired lipid countertransport between the endoplasmic reticulum and the plasma membrane.|||In isoform 2.|||In isoform 3.|||Oxysterol-binding protein-related protein 5|||PH|||Phosphoserine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000100373|||http://purl.uniprot.org/annotation/VAR_020414|||http://purl.uniprot.org/annotation/VAR_060079|||http://purl.uniprot.org/annotation/VSP_043071|||http://purl.uniprot.org/annotation/VSP_057408|||http://purl.uniprot.org/annotation/VSP_057409
http://togogenome.org/gene/9606:LMO7                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0A0MTE2|||http://purl.uniprot.org/uniprot/E9PMT2|||http://purl.uniprot.org/uniprot/F8J2B5|||http://purl.uniprot.org/uniprot/F8WD26|||http://purl.uniprot.org/uniprot/Q8WWI1                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand                                                                                  ^@                                                                                  Basic and acidic residues|||Calponin-homology (CH)|||Disordered|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||In a colorectal cancer sample; somatic mutation.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||LIM domain only protein 7|||LIM zinc-binding|||N-acetylmethionine|||PDZ|||Phosphoserine|||Phosphothreonine|||Phosphotyrosine|||Polar residues                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000075824|||http://purl.uniprot.org/annotation/VAR_036189|||http://purl.uniprot.org/annotation/VAR_036190|||http://purl.uniprot.org/annotation/VAR_056163|||http://purl.uniprot.org/annotation/VSP_009718|||http://purl.uniprot.org/annotation/VSP_009719|||http://purl.uniprot.org/annotation/VSP_009720|||http://purl.uniprot.org/annotation/VSP_055683|||http://purl.uniprot.org/annotation/VSP_055684|||http://purl.uniprot.org/annotation/VSP_055685
http://togogenome.org/gene/9606:PLA2G12A                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q542Y6|||http://purl.uniprot.org/uniprot/Q9BZM1                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Experimental Information|||Mass|||Molecule Processing|||Sequence Conflict|||Signal Peptide|||Site                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Mass|||Sequence Conflict|||Signal Peptide                                                                                  ^@                                                                                  Group XIIA secretory phospholipase A2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000022770|||http://purl.uniprot.org/annotation/PRO_5014309601
http://togogenome.org/gene/9606:FMR1NB                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q8N0W7                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Molecule Processing|||Natural Variation|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Domain Extent|||Region|||Sequence Variant|||Topological Domain|||Transmembrane                                                                                  ^@                                                                                  Basic residues|||Cytoplasmic|||Disordered|||Extracellular|||FMR1 neighbor protein|||Helical|||P-type                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000281735|||http://purl.uniprot.org/annotation/VAR_031254
http://togogenome.org/gene/9606:PKN2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q16513                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Mutagenesis Site|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Active Site|||Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Helix|||Modified Residue|||Mutagenesis Site|||Region|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AGC-kinase C-terminal|||Abolishes catalytic activity.|||Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'.|||Abolishes interaction with PDPK1 and prevents the phosphorylation of AKT1 at 'Ser-473'. Reduces catalytic activity by 90%.|||C2|||Cleavage; by caspase-3|||Disordered|||Does not inhibit catalytic activity.|||Does not inhibit interaction with PTPN13.|||Does not suppress ciliogenesis; when associated with A-121.|||Does not suppress ciliogenesis; when associated with A-124.|||In isoform 2.|||In isoform 3.|||In isoform 4.|||In isoform 5.|||Inhibits interaction with PTPN13.|||N6-acetyllysine|||Necessary for the catalytic activity|||Necessary to rescue apical junction formation|||Negatively regulates the responsiveness of the catalytic activity by cardiolipin and is required for optimal activation by the GTP-bound RhoA|||Phosphoserine|||Phosphothreonine|||Phosphothreonine; by PDPK1|||Polar residues|||Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with A-117.|||Prevents proteolytic processing by caspase-3 during apoptosis. Diminishes pro-apoptotic function; when associated with E-700.|||Protein kinase|||Proton acceptor|||REM-1 1|||REM-1 2|||REM-1 3|||Reduces catalytic activity by 25%.|||Reduces catalytic activity by 50%.|||Reduces catalytic activity.|||Serine/threonine-protein kinase N2                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000055722|||http://purl.uniprot.org/annotation/VAR_050562|||http://purl.uniprot.org/annotation/VAR_050563|||http://purl.uniprot.org/annotation/VAR_050564|||http://purl.uniprot.org/annotation/VSP_042180|||http://purl.uniprot.org/annotation/VSP_042181|||http://purl.uniprot.org/annotation/VSP_042182|||http://purl.uniprot.org/annotation/VSP_042183|||http://purl.uniprot.org/annotation/VSP_042184
http://togogenome.org/gene/9606:BAK1                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z391|||http://purl.uniprot.org/uniprot/Q16611                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Experimental Information|||Helix|||Initiator Methionine|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Variant|||Site|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Domain Extent|||Helix|||Initiator Methionine|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Variant|||Splice Variant|||Strand|||Transmembrane|||Turn                                                                                  ^@                                                                                  BH1|||BH2|||BH3|||Bcl-2 Bcl-2 homology region 1-3|||Bcl-2 homologous antagonist/killer|||Disordered|||Helical|||In isoform 2.|||N-acetylalanine|||Removed|||Strongly reduced zinc binding and homodimerization.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000143059|||http://purl.uniprot.org/annotation/VAR_018829|||http://purl.uniprot.org/annotation/VAR_018830|||http://purl.uniprot.org/annotation/VAR_048417|||http://purl.uniprot.org/annotation/VSP_056551|||http://purl.uniprot.org/annotation/VSP_056552
http://togogenome.org/gene/9606:MOGAT2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q3SYC2                                                                                  ^@                                                                                  Chain|||Experimental Information|||Molecule Processing|||Natural Variation|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  Chain|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Transmembrane                                                                                  ^@                                                                                  2-acylglycerol O-acyltransferase 2|||Helical|||In isoform 2.|||In isoform 3.                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000249062|||http://purl.uniprot.org/annotation/VAR_027390|||http://purl.uniprot.org/annotation/VAR_027391|||http://purl.uniprot.org/annotation/VAR_048857|||http://purl.uniprot.org/annotation/VSP_020358|||http://purl.uniprot.org/annotation/VSP_020359|||http://purl.uniprot.org/annotation/VSP_020360
http://togogenome.org/gene/9606:PNKP                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96T60                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Secondary Structure|||Sequence Conflict|||Sequence Variant|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Binding Site|||Chain|||Compositionally Biased Region|||Domain Extent|||Modified Residue|||Region|||Sequence Conflict|||Sequence Variant|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Basic and acidic residues|||Bifunctional polynucleotide phosphatase/kinase|||Disordered|||FHA|||In AOA4.|||In MCSZ.|||In MCSZ; atypical phenotype.|||In MCSZ; impaired recruitment to DNA damage sites.|||In isoform 2.|||Kinase|||N-acetylmethionine|||Phosphatase|||Phosphoserine|||Phosphothreonine                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000058478|||http://purl.uniprot.org/annotation/VAR_019260|||http://purl.uniprot.org/annotation/VAR_019261|||http://purl.uniprot.org/annotation/VAR_019262|||http://purl.uniprot.org/annotation/VAR_019263|||http://purl.uniprot.org/annotation/VAR_019264|||http://purl.uniprot.org/annotation/VAR_063835|||http://purl.uniprot.org/annotation/VAR_063836|||http://purl.uniprot.org/annotation/VAR_073369|||http://purl.uniprot.org/annotation/VAR_073370|||http://purl.uniprot.org/annotation/VAR_076537|||http://purl.uniprot.org/annotation/VSP_055500
http://togogenome.org/gene/9606:DYNC2I2                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/Q96EX3                                                                                  ^@                                                                                  Chain|||Experimental Information|||Modification|||Modified Residue|||Molecule Processing|||Natural Variation|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Chain|||Modified Residue|||Region|||Repeat|||Sequence Conflict|||Sequence Variant                                                                                  ^@                                                                                  Cytoplasmic dynein 2 intermediate chain 2|||DYNLL2 binding|||DYNLRB1 binding|||In SRTD11.|||Phosphoserine|||WD 1|||WD 2|||WD 3|||WD 4|||WD 5                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000051383|||http://purl.uniprot.org/annotation/VAR_070962|||http://purl.uniprot.org/annotation/VAR_070963|||http://purl.uniprot.org/annotation/VAR_070964|||http://purl.uniprot.org/annotation/VAR_070965|||http://purl.uniprot.org/annotation/VAR_070966|||http://purl.uniprot.org/annotation/VAR_070967|||http://purl.uniprot.org/annotation/VAR_070968|||http://purl.uniprot.org/annotation/VAR_070969|||http://purl.uniprot.org/annotation/VAR_070970|||http://purl.uniprot.org/annotation/VAR_070971|||http://purl.uniprot.org/annotation/VAR_070972|||http://purl.uniprot.org/annotation/VAR_083840
http://togogenome.org/gene/9606:MLLT3                                                                                  ^@                                                                                  http://purl.uniprot.org/uniprot/A0A0S2Z448|||http://purl.uniprot.org/uniprot/P42568                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Experimental Information|||Helix|||Modification|||Modified Residue|||Molecule Processing|||Motif|||Mutagenesis Site|||Natural Variation|||Non-terminal Residue|||Region|||Secondary Structure|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  Chain|||Compositionally Biased Region|||Crosslink|||Domain Extent|||Helix|||Modified Residue|||Motif|||Mutagenesis Site|||Non-terminal Residue|||Region|||Sequence Conflict|||Site|||Splice Variant|||Strand|||Turn                                                                                  ^@                                                                                  AF-9 ANC1 homology|||Acidic residues|||Basic and acidic residues|||Binds equally well acetylated and crotonylated histone H3.|||Decreased DNA-binding.|||Decreased binding to acetylated histone H3.|||Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3.|||Disordered|||Does not affect ability to discriminate between acetylated and crotonylated histone H3.|||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)|||Histone H3K9cr binding|||In isoform 2.|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient CO)|||KMT2A/MLL1 fusion point (in acute myeloid leukemia patient F1)|||Nuclear localization signal|||Phosphoserine|||Polar residues|||Protein AF-9|||Strongly decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3.|||YEATS                                                                                  ^@                                                                                  http://purl.uniprot.org/annotation/PRO_0000215921|||http://purl.uniprot.org/annotation/VSP_054924